diff --git a/content/3.defense-systems/thoeris.md b/content/3.defense-systems/thoeris.md
index 8267588579acddbb64dbaae5ec4498dadd4f1c42..f5060a0c394da92cce98d048d6e656928c3e7f11 100644
--- a/content/3.defense-systems/thoeris.md
+++ b/content/3.defense-systems/thoeris.md
@@ -7,15 +7,34 @@ tableColumns:
       abstract: |
         The arms race between bacteria and phages led to the development of sophisticated antiphage defense systems, including CRISPR-Cas and restriction-modification systems. Evidence suggests that known and unknown defense systems are located in "defense islands" in microbial genomes. Here, we comprehensively characterized the bacterial defensive arsenal by examining gene families that are clustered next to known defense genes in prokaryotic genomes. Candidate defense systems were systematically engineered and validated in model bacteria for their antiphage activities. We report nine previously unknown antiphage systems and one antiplasmid system that are widespread in microbes and strongly protect against foreign invaders. These include systems that adopted components of the bacterial flagella and condensin complexes. Our data also suggest a common, ancient ancestry of innate immunity components shared between animals, plants, and bacteria.
     Sensor: Unknown
-    Activator: Signaling
+    Activator: Signaling system
     Effector: Nucleotide modifying
     PFAM: PF08937, PF13289, PF18185
+contributors: 
+  - Marie Guillaume
+  - Helena Shomar
+  - Florian Tesson
 relevantAbstracts:
-    - doi: 10.1038/s41586-021-04098-7
-    - doi: 10.1126/science.aar4120
+  - doi: 10.1038/s41586-021-04098-7
+  - doi: 10.1126/science.aar4120
+  - doi: 10.1038/s41467-020-16703-w
 ---
 
 # Thoeris
+
+## Description
+Thoeris is a two-gene defense system identified in more than 2000 bacterial genomes. It consists of the genes ThsA and thsB. Its anti-phage function was experimentally validated in *Bacillus subtilis* :ref{doi=10.1126/science.aar4120}. In response to phage infection, it produces an isomer of cyclic ADP-ribose, which leads to  depletion of NAD+ and results in abortive infection.
+
+ThsA contains the sirtuin-like domain which binds to nicotinamide adenine dinucleotide (NAD) metabolites. The N112A point mutation neutralizes the Thoeris defense system and abolishes the NAD+ hydrolase activity of thsA :ref{doi=10.1126/science.aar4120}. It lacks a N-terminal transmembrane domain, and is predicted to be cytoplasmic. 
+
+ThsB contains a TIR domain :ref{doi=10.1126/science.aar4120} is proposed to participate in the recognition of phage infection, as various thsB proteins sense different phage components.ThsB is found in more than 50% of Thoeris systems in multiple diverse copies :ref{doi=10.1126/science.aar4120}.
+
+## Molecular mechanism
+
+The Thoeris system functions by degrading NAD+ (a cofactor of central metabolism) to stop the growth of phage-infected cells and prevent the transmission of the phage to neighboring bacteria :ref{doi=10.1038/s41467-020-16703-w}.
+
+The protein ThsB, featuring the TIR domain, plays a cruial role in identifying phage invasion. Upon detecting the infection, the TIR domain becomes enzymatically active, initiating the synthesis of a cADPR isomer molecule :ref{doi=10.1038/s41586-021-04098-7}. This molecule acts as a signal, binding to the ThsA effector, likely through its C-terminal SLOG domain, thereby activating its NADase activity :ref{doi=10.1038/s41586-021-04098-7}. Consequently, the NADase effector reduces NAD+ cellular levels, creating an environment unsuitable for phage replication :ref{doi=10.1038/s41586-021-04098-7,10.1038/s41467-020-16703-w}.
+
 ## Example of genomic structure
 
 The Thoeris is composed of 2 proteins: ThsA and ThsB.
@@ -39,6 +58,21 @@ Proportion of genome encoding the Thoeris system for the 14 phyla with more than
 
 
 ## Structure
+
+### Experimentaly determined structure
+
+From :ref{doi=10.1038/s41467-020-16703-w} in *Bacillus cereus* MSX-D12:
+
+::molstar-pdbe-plugin
+---
+height: 700
+dataUrls: 
+    - /thoeris/6lhx_BcThsA_4mer.pdb
+    - /thoeris/6lhy_BcThsB_1mer.pdb
+    - /thoeris/7uxs_BcThsA_2mer_cdpr.pdb
+---
+::
+
 ### Thoeris_I
 ##### Example 1
 
diff --git a/public/thoeris/6lhx_BcThsA_4mer.pdb b/public/thoeris/6lhx_BcThsA_4mer.pdb
new file mode 100644
index 0000000000000000000000000000000000000000..84fd7ae5b914fb6c40092edf190152319f0a70c7
--- /dev/null
+++ b/public/thoeris/6lhx_BcThsA_4mer.pdb
@@ -0,0 +1,28281 @@
+HEADER    HYDROLASE                               10-DEC-19   6LHX              
+TITLE     CRYSTAL STRUCTURE OF THSA                                             
+COMPND    MOL_ID: 1;                                                            
+COMPND   2 MOLECULE: THSA;                                                      
+COMPND   3 CHAIN: A, B, C, D;                                                   
+COMPND   4 ENGINEERED: YES;                                                     
+COMPND   5 OTHER_DETAILS: SF FILE CONTAINS FRIEDEL PAIRS.                       
+SOURCE    MOL_ID: 1;                                                            
+SOURCE   2 ORGANISM_SCIENTIFIC: BACILLUS CEREUS MSX-D12;                        
+SOURCE   3 ORGANISM_TAXID: 1053222;                                             
+SOURCE   4 GENE: II9_05448;                                                     
+SOURCE   5 EXPRESSION_SYSTEM: ESCHERICHIA COLI BL21(DE3);                       
+SOURCE   6 EXPRESSION_SYSTEM_TAXID: 469008                                      
+KEYWDS    NAD+ HYDROLYSIS, HYDROLASE                                            
+EXPDTA    X-RAY DIFFRACTION                                                     
+AUTHOR    E.BAE,D.KA,H.OH                                                       
+REVDAT   1   24-JUN-20 6LHX    0                                                
+JRNL        AUTH   D.KA,H.OH,E.PARK,J.H.KIM,E.BAE                               
+JRNL        TITL   STRUCTURAL AND FUNCTIONAL EVIDENCE OF BACTERIAL ANTIPHAGE    
+JRNL        TITL 2 PROTECTION BY THOERIS DEFENSE SYSTEM VIA NAD+DEGRADATION.    
+JRNL        REF    NAT COMMUN                    V.  11  2816 2020              
+JRNL        REFN                   ESSN 2041-1723                               
+JRNL        PMID   32499527                                                     
+JRNL        DOI    10.1038/S41467-020-16703-W                                   
+REMARK   2                                                                      
+REMARK   2 RESOLUTION.    2.50 ANGSTROMS.                                       
+REMARK   3                                                                      
+REMARK   3 REFINEMENT.                                                          
+REMARK   3   PROGRAM     : PHENIX 1.9_1692                                      
+REMARK   3   AUTHORS     : PAUL ADAMS,PAVEL AFONINE,VINCENT CHEN,IAN            
+REMARK   3               : DAVIS,KRESHNA GOPAL,RALF GROSSE-KUNSTLEVE,           
+REMARK   3               : LI-WEI HUNG,ROBERT IMMORMINO,TOM IOERGER,            
+REMARK   3               : AIRLIE MCCOY,ERIK MCKEE,NIGEL MORIARTY,              
+REMARK   3               : REETAL PAI,RANDY READ,JANE RICHARDSON,               
+REMARK   3               : DAVID RICHARDSON,TOD ROMO,JIM SACCHETTINI,           
+REMARK   3               : NICHOLAS SAUTER,JACOB SMITH,LAURENT                  
+REMARK   3               : STORONI,TOM TERWILLIGER,PETER ZWART                  
+REMARK   3                                                                      
+REMARK   3    REFINEMENT TARGET : ML                                            
+REMARK   3                                                                      
+REMARK   3  DATA USED IN REFINEMENT.                                            
+REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 2.50                           
+REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 31.64                          
+REMARK   3   MIN(FOBS/SIGMA_FOBS)              : 1.340                          
+REMARK   3   COMPLETENESS FOR RANGE        (%) : 99.2                           
+REMARK   3   NUMBER OF REFLECTIONS             : 181015                         
+REMARK   3                                                                      
+REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
+REMARK   3   R VALUE     (WORKING + TEST SET) : 0.242                           
+REMARK   3   R VALUE            (WORKING SET) : 0.242                           
+REMARK   3   FREE R VALUE                     : 0.273                           
+REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 2.190                           
+REMARK   3   FREE R VALUE TEST SET COUNT      : 3958                            
+REMARK   3                                                                      
+REMARK   3  FIT TO DATA USED IN REFINEMENT (IN BINS).                           
+REMARK   3   BIN  RESOLUTION RANGE  COMPL.    NWORK NFREE   RWORK  RFREE        
+REMARK   3     1 31.6410 -  7.5618    0.99     6354   143  0.2067 0.1923        
+REMARK   3     2  7.5618 -  6.0155    1.00     6359   143  0.2463 0.3128        
+REMARK   3     3  6.0155 -  5.2590    1.00     6398   143  0.2334 0.2754        
+REMARK   3     4  5.2590 -  4.7800    1.00     6358   144  0.2023 0.2336        
+REMARK   3     5  4.7800 -  4.4384    1.00     6359   142  0.1918 0.1911        
+REMARK   3     6  4.4384 -  4.1773    1.00     6402   143  0.2068 0.2489        
+REMARK   3     7  4.1773 -  3.9685    1.00     6344   141  0.2116 0.2738        
+REMARK   3     8  3.9685 -  3.7961    1.00     6426   144  0.2233 0.2136        
+REMARK   3     9  3.7961 -  3.6501    1.00     6337   140  0.2326 0.2416        
+REMARK   3    10  3.6501 -  3.5244    1.00     6346   145  0.2323 0.2935        
+REMARK   3    11  3.5244 -  3.4143    1.00     6385   143  0.2462 0.2802        
+REMARK   3    12  3.4143 -  3.3168    1.00     6322   140  0.2489 0.3033        
+REMARK   3    13  3.3168 -  3.2296    1.00     6343   140  0.2723 0.3286        
+REMARK   3    14  3.2296 -  3.1508    1.00     6352   140  0.2806 0.3041        
+REMARK   3    15  3.1508 -  3.0793    0.99     6382   146  0.2798 0.3202        
+REMARK   3    16  3.0793 -  3.0138    0.99     6261   138  0.2930 0.3665        
+REMARK   3    17  3.0138 -  2.9536    0.99     6369   142  0.2971 0.3417        
+REMARK   3    18  2.9536 -  2.8979    0.99     6378   146  0.2970 0.3247        
+REMARK   3    19  2.8979 -  2.8461    0.99     6285   140  0.2986 0.3179        
+REMARK   3    20  2.8461 -  2.7979    0.99     6283   139  0.3158 0.3643        
+REMARK   3    21  2.7979 -  2.7528    0.99     6263   138  0.3212 0.3719        
+REMARK   3    22  2.7528 -  2.7105    0.99     6384   143  0.3227 0.3804        
+REMARK   3    23  2.7105 -  2.6706    0.99     6305   139  0.3344 0.3559        
+REMARK   3    24  2.6706 -  2.6330    0.99     6262   140  0.3337 0.3955        
+REMARK   3    25  2.6330 -  2.5975    0.99     6270   140  0.3347 0.3740        
+REMARK   3    26  2.5975 -  2.5638    0.98     6270   142  0.3313 0.3835        
+REMARK   3    27  2.5638 -  2.5317    0.98     6211   137  0.3369 0.3954        
+REMARK   3    28  2.5317 -  2.5012    0.94     6049   137  0.3410 0.3490        
+REMARK   3                                                                      
+REMARK   3  BULK SOLVENT MODELLING.                                             
+REMARK   3   METHOD USED        : FLAT BULK SOLVENT MODEL                       
+REMARK   3   SOLVENT RADIUS     : 1.11                                          
+REMARK   3   SHRINKAGE RADIUS   : 0.90                                          
+REMARK   3   K_SOL              : NULL                                          
+REMARK   3   B_SOL              : NULL                                          
+REMARK   3                                                                      
+REMARK   3  ERROR ESTIMATES.                                                    
+REMARK   3   COORDINATE ERROR (MAXIMUM-LIKELIHOOD BASED)     : 0.440            
+REMARK   3   PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 31.450           
+REMARK   3                                                                      
+REMARK   3  B VALUES.                                                           
+REMARK   3   FROM WILSON PLOT           (A**2) : 63.54                          
+REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 82.17                          
+REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
+REMARK   3    B11 (A**2) : NULL                                                 
+REMARK   3    B22 (A**2) : NULL                                                 
+REMARK   3    B33 (A**2) : NULL                                                 
+REMARK   3    B12 (A**2) : NULL                                                 
+REMARK   3    B13 (A**2) : NULL                                                 
+REMARK   3    B23 (A**2) : NULL                                                 
+REMARK   3                                                                      
+REMARK   3  TWINNING INFORMATION.                                               
+REMARK   3   FRACTION: NULL                                                     
+REMARK   3   OPERATOR: NULL                                                     
+REMARK   3                                                                      
+REMARK   3  DEVIATIONS FROM IDEAL VALUES.                                       
+REMARK   3                 RMSD          COUNT                                  
+REMARK   3   BOND      :  0.003          13534                                  
+REMARK   3   ANGLE     :  0.810          18340                                  
+REMARK   3   CHIRALITY :  0.032           2093                                  
+REMARK   3   PLANARITY :  0.004           2364                                  
+REMARK   3   DIHEDRAL  : 13.163           4762                                  
+REMARK   3                                                                      
+REMARK   3  TLS DETAILS                                                         
+REMARK   3   NUMBER OF TLS GROUPS  : 13                                         
+REMARK   3   TLS GROUP : 1                                                      
+REMARK   3    SELECTION: CHAIN 'A' AND (RESID 2 THROUGH 164 )                   
+REMARK   3    ORIGIN FOR THE GROUP (A): -24.7185  23.4043  -9.7470              
+REMARK   3    T TENSOR                                                          
+REMARK   3      T11:   0.4651 T22:   0.5711                                     
+REMARK   3      T33:   0.3902 T12:   0.0138                                     
+REMARK   3      T13:   0.1308 T23:   0.0444                                     
+REMARK   3    L TENSOR                                                          
+REMARK   3      L11:   1.4312 L22:   3.9572                                     
+REMARK   3      L33:   1.9229 L12:   1.1242                                     
+REMARK   3      L13:   1.5481 L23:   1.2267                                     
+REMARK   3    S TENSOR                                                          
+REMARK   3      S11:  -0.1674 S12:   0.4112 S13:   0.1353                       
+REMARK   3      S21:  -0.3272 S22:   0.0251 S23:  -0.0068                       
+REMARK   3      S31:  -0.0533 S32:  -0.1082 S33:   0.1881                       
+REMARK   3   TLS GROUP : 2                                                      
+REMARK   3    SELECTION: CHAIN 'A' AND (RESID 165 THROUGH 340 )                 
+REMARK   3    ORIGIN FOR THE GROUP (A): -33.7342   9.1760  -6.5766              
+REMARK   3    T TENSOR                                                          
+REMARK   3      T11:   0.6453 T22:   0.4967                                     
+REMARK   3      T33:   0.4170 T12:  -0.1405                                     
+REMARK   3      T13:   0.1082 T23:  -0.0610                                     
+REMARK   3    L TENSOR                                                          
+REMARK   3      L11:   2.9506 L22:   1.4198                                     
+REMARK   3      L33:   3.2418 L12:   0.0357                                     
+REMARK   3      L13:  -1.1978 L23:   0.4102                                     
+REMARK   3    S TENSOR                                                          
+REMARK   3      S11:  -0.3469 S12:   0.5389 S13:  -0.2785                       
+REMARK   3      S21:  -0.0189 S22:   0.0154 S23:   0.1400                       
+REMARK   3      S31:   0.6905 S32:  -0.5114 S33:   0.2985                       
+REMARK   3   TLS GROUP : 3                                                      
+REMARK   3    SELECTION: CHAIN 'A' AND (RESID 341 THROUGH 476 )                 
+REMARK   3    ORIGIN FOR THE GROUP (A): -58.5357  12.0181   5.6255              
+REMARK   3    T TENSOR                                                          
+REMARK   3      T11:   0.6385 T22:   0.8792                                     
+REMARK   3      T33:   0.5212 T12:  -0.1563                                     
+REMARK   3      T13:   0.1797 T23:  -0.0781                                     
+REMARK   3    L TENSOR                                                          
+REMARK   3      L11:   3.9019 L22:   5.8191                                     
+REMARK   3      L33:   6.7264 L12:   0.2635                                     
+REMARK   3      L13:   1.5147 L23:   1.5842                                     
+REMARK   3    S TENSOR                                                          
+REMARK   3      S11:  -0.3119 S12:   0.9457 S13:  -0.1022                       
+REMARK   3      S21:  -0.7686 S22:  -0.1021 S23:   0.3521                       
+REMARK   3      S31:   0.3807 S32:  -0.5980 S33:   0.4148                       
+REMARK   3   TLS GROUP : 4                                                      
+REMARK   3    SELECTION: CHAIN 'B' AND (RESID 2 THROUGH 176 )                   
+REMARK   3    ORIGIN FOR THE GROUP (A): -17.3965   3.1948  17.6380              
+REMARK   3    T TENSOR                                                          
+REMARK   3      T11:   0.6041 T22:   0.5916                                     
+REMARK   3      T33:   0.5255 T12:  -0.0413                                     
+REMARK   3      T13:   0.2095 T23:   0.1494                                     
+REMARK   3    L TENSOR                                                          
+REMARK   3      L11:   4.2031 L22:   6.7374                                     
+REMARK   3      L33:   3.6115 L12:   1.9759                                     
+REMARK   3      L13:   2.0260 L23:   1.0067                                     
+REMARK   3    S TENSOR                                                          
+REMARK   3      S11:   0.0920 S12:  -0.5647 S13:  -0.7521                       
+REMARK   3      S21:   0.3516 S22:  -0.0894 S23:  -0.2408                       
+REMARK   3      S31:   0.8041 S32:  -0.1563 S33:  -0.0330                       
+REMARK   3   TLS GROUP : 5                                                      
+REMARK   3    SELECTION: CHAIN 'B' AND (RESID 177 THROUGH 288 )                 
+REMARK   3    ORIGIN FOR THE GROUP (A):  -6.5790  12.3040  20.4203              
+REMARK   3    T TENSOR                                                          
+REMARK   3      T11:   0.5531 T22:   0.6308                                     
+REMARK   3      T33:   0.4090 T12:   0.0107                                     
+REMARK   3      T13:   0.1511 T23:   0.0817                                     
+REMARK   3    L TENSOR                                                          
+REMARK   3      L11:   5.5509 L22:   0.7117                                     
+REMARK   3      L33:   0.0825 L12:   0.0081                                     
+REMARK   3      L13:   1.1832 L23:   0.0050                                     
+REMARK   3    S TENSOR                                                          
+REMARK   3      S11:  -0.0588 S12:  -0.4684 S13:  -0.0737                       
+REMARK   3      S21:   0.0485 S22:   0.0553 S23:  -0.0820                       
+REMARK   3      S31:  -0.0447 S32:   0.1068 S33:   0.0503                       
+REMARK   3   TLS GROUP : 6                                                      
+REMARK   3    SELECTION: CHAIN 'B' AND (RESID 289 THROUGH 315 )                 
+REMARK   3    ORIGIN FOR THE GROUP (A): -49.2497  31.2022  31.9122              
+REMARK   3    T TENSOR                                                          
+REMARK   3      T11:   0.7251 T22:   0.9481                                     
+REMARK   3      T33:   0.9093 T12:   0.0089                                     
+REMARK   3      T13:   0.1658 T23:  -0.3721                                     
+REMARK   3    L TENSOR                                                          
+REMARK   3      L11:   3.0281 L22:   1.9690                                     
+REMARK   3      L33:   0.0774 L12:  -2.4509                                     
+REMARK   3      L13:  -0.1295 L23:   0.1172                                     
+REMARK   3    S TENSOR                                                          
+REMARK   3      S11:   0.0327 S12:  -1.0755 S13:   1.4176                       
+REMARK   3      S21:   1.0313 S22:   0.1191 S23:   0.4662                       
+REMARK   3      S31:  -0.5616 S32:  -0.3836 S33:   0.0701                       
+REMARK   3   TLS GROUP : 7                                                      
+REMARK   3    SELECTION: CHAIN 'B' AND (RESID 316 THROUGH 476 )                 
+REMARK   3    ORIGIN FOR THE GROUP (A): -42.4409  20.2286  33.1403              
+REMARK   3    T TENSOR                                                          
+REMARK   3      T11:   0.6477 T22:   1.0690                                     
+REMARK   3      T33:   0.4953 T12:  -0.0400                                     
+REMARK   3      T13:   0.2250 T23:  -0.1422                                     
+REMARK   3    L TENSOR                                                          
+REMARK   3      L11:   4.2868 L22:   3.0764                                     
+REMARK   3      L33:   4.3382 L12:   0.3428                                     
+REMARK   3      L13:   0.4196 L23:   0.0653                                     
+REMARK   3    S TENSOR                                                          
+REMARK   3      S11:   0.0397 S12:  -1.1105 S13:   0.2837                       
+REMARK   3      S21:   0.3701 S22:  -0.1336 S23:  -0.0706                       
+REMARK   3      S31:   0.3886 S32:   0.2763 S33:   0.1425                       
+REMARK   3   TLS GROUP : 8                                                      
+REMARK   3    SELECTION: CHAIN 'C' AND (RESID 2 THROUGH 220 )                   
+REMARK   3    ORIGIN FOR THE GROUP (A): -22.3278  46.6075   9.1666              
+REMARK   3    T TENSOR                                                          
+REMARK   3      T11:   0.4667 T22:   0.4883                                     
+REMARK   3      T33:   0.4383 T12:   0.0362                                     
+REMARK   3      T13:   0.1622 T23:  -0.0232                                     
+REMARK   3    L TENSOR                                                          
+REMARK   3      L11:   2.1831 L22:   2.8813                                     
+REMARK   3      L33:   2.2099 L12:  -0.5155                                     
+REMARK   3      L13:   0.5599 L23:  -0.6454                                     
+REMARK   3    S TENSOR                                                          
+REMARK   3      S11:  -0.0954 S12:  -0.5049 S13:   0.1602                       
+REMARK   3      S21:   0.3473 S22:   0.1045 S23:   0.1564                       
+REMARK   3      S31:  -0.0832 S32:  -0.2135 S33:  -0.0403                       
+REMARK   3   TLS GROUP : 9                                                      
+REMARK   3    SELECTION: CHAIN 'C' AND (RESID 221 THROUGH 315 )                 
+REMARK   3    ORIGIN FOR THE GROUP (A): -40.3645  60.0218   9.1455              
+REMARK   3    T TENSOR                                                          
+REMARK   3      T11:   0.6931 T22:   0.7381                                     
+REMARK   3      T33:   0.7607 T12:   0.2295                                     
+REMARK   3      T13:   0.2067 T23:  -0.1514                                     
+REMARK   3    L TENSOR                                                          
+REMARK   3      L11:   2.4047 L22:   1.0295                                     
+REMARK   3      L33:   2.6881 L12:  -0.0584                                     
+REMARK   3      L13:   0.8186 L23:   0.5972                                     
+REMARK   3    S TENSOR                                                          
+REMARK   3      S11:  -0.3305 S12:  -1.0581 S13:   0.1802                       
+REMARK   3      S21:   0.1400 S22:   0.0896 S23:   0.2108                       
+REMARK   3      S31:  -0.5193 S32:  -0.9575 S33:   0.1450                       
+REMARK   3   TLS GROUP : 10                                                     
+REMARK   3    SELECTION: CHAIN 'C' AND (RESID 316 THROUGH 475 )                 
+REMARK   3    ORIGIN FOR THE GROUP (A): -57.5835  56.4872  -9.0575              
+REMARK   3    T TENSOR                                                          
+REMARK   3      T11:   0.6226 T22:   0.7452                                     
+REMARK   3      T33:   0.8401 T12:   0.1656                                     
+REMARK   3      T13:   0.1016 T23:  -0.1341                                     
+REMARK   3    L TENSOR                                                          
+REMARK   3      L11:   6.2341 L22:   3.4359                                     
+REMARK   3      L33:   6.5183 L12:   0.0978                                     
+REMARK   3      L13:  -0.5445 L23:   0.4128                                     
+REMARK   3    S TENSOR                                                          
+REMARK   3      S11:  -0.1012 S12:  -0.4951 S13:  -0.7396                       
+REMARK   3      S21:   0.3452 S22:  -0.2548 S23:   0.6221                       
+REMARK   3      S31:  -0.1856 S32:  -0.9847 S33:   0.3819                       
+REMARK   3   TLS GROUP : 11                                                     
+REMARK   3    SELECTION: CHAIN 'D' AND (RESID 2 THROUGH 202 )                   
+REMARK   3    ORIGIN FOR THE GROUP (A): -15.5215  63.2245 -17.0253              
+REMARK   3    T TENSOR                                                          
+REMARK   3      T11:   0.5619 T22:   0.4160                                     
+REMARK   3      T33:   0.6074 T12:   0.0131                                     
+REMARK   3      T13:   0.0153 T23:   0.2328                                     
+REMARK   3    L TENSOR                                                          
+REMARK   3      L11:   5.5722 L22:   2.2906                                     
+REMARK   3      L33:   3.5623 L12:  -0.8343                                     
+REMARK   3      L13:  -0.8688 L23:   0.3334                                     
+REMARK   3    S TENSOR                                                          
+REMARK   3      S11:   0.0245 S12:   0.8038 S13:   1.1049                       
+REMARK   3      S21:  -0.5087 S22:  -0.0579 S23:   0.0912                       
+REMARK   3      S31:  -0.8349 S32:   0.0687 S33:   0.0797                       
+REMARK   3   TLS GROUP : 12                                                     
+REMARK   3    SELECTION: CHAIN 'D' AND (RESID 203 THROUGH 290 )                 
+REMARK   3    ORIGIN FOR THE GROUP (A):  -5.8696  54.0664 -23.4411              
+REMARK   3    T TENSOR                                                          
+REMARK   3      T11:   0.6592 T22:   0.6600                                     
+REMARK   3      T33:   0.5238 T12:   0.0359                                     
+REMARK   3      T13:   0.0871 T23:   0.1535                                     
+REMARK   3    L TENSOR                                                          
+REMARK   3      L11:   6.1134 L22:   1.0888                                     
+REMARK   3      L33:   1.7341 L12:  -0.4429                                     
+REMARK   3      L13:  -0.5499 L23:   0.6614                                     
+REMARK   3    S TENSOR                                                          
+REMARK   3      S11:  -0.0474 S12:   1.0973 S13:   0.3007                       
+REMARK   3      S21:  -0.3669 S22:  -0.1278 S23:  -0.1235                       
+REMARK   3      S31:  -0.3470 S32:   0.4733 S33:   0.0575                       
+REMARK   3   TLS GROUP : 13                                                     
+REMARK   3    SELECTION: CHAIN 'D' AND (RESID 291 THROUGH 475 )                 
+REMARK   3    ORIGIN FOR THE GROUP (A): -42.4863  48.1688 -35.1842              
+REMARK   3    T TENSOR                                                          
+REMARK   3      T11:   0.6913 T22:   1.0305                                     
+REMARK   3      T33:   0.8231 T12:   0.1639                                     
+REMARK   3      T13:   0.0327 T23:  -0.3527                                     
+REMARK   3    L TENSOR                                                          
+REMARK   3      L11:   5.1750 L22:   4.1544                                     
+REMARK   3      L33:   5.9963 L12:  -0.1779                                     
+REMARK   3      L13:  -2.5782 L23:   1.0924                                     
+REMARK   3    S TENSOR                                                          
+REMARK   3      S11:  -0.0448 S12:   1.5558 S13:  -0.9971                       
+REMARK   3      S21:  -0.6067 S22:  -0.3709 S23:   0.1961                       
+REMARK   3      S31:  -0.0035 S32:  -0.7017 S33:   0.3771                       
+REMARK   3                                                                      
+REMARK   3  NCS DETAILS                                                         
+REMARK   3   NUMBER OF NCS GROUPS : 1                                           
+REMARK   3   NCS GROUP : 1                                                      
+REMARK   3    NCS OPERATOR : 1                                                  
+REMARK   3     REFERENCE SELECTION: CHAIN A                                     
+REMARK   3     SELECTION          : CHAIN B                                     
+REMARK   3     ATOM PAIRS NUMBER  : 7397                                        
+REMARK   3     RMSD               : NULL                                        
+REMARK   3    NCS OPERATOR : 2                                                  
+REMARK   3     REFERENCE SELECTION: CHAIN A                                     
+REMARK   3     SELECTION          : CHAIN C                                     
+REMARK   3     ATOM PAIRS NUMBER  : 7397                                        
+REMARK   3     RMSD               : NULL                                        
+REMARK   3    NCS OPERATOR : 3                                                  
+REMARK   3     REFERENCE SELECTION: CHAIN A                                     
+REMARK   3     SELECTION          : CHAIN D                                     
+REMARK   3     ATOM PAIRS NUMBER  : 7397                                        
+REMARK   3     RMSD               : NULL                                        
+REMARK   3                                                                      
+REMARK   3  OTHER REFINEMENT REMARKS: NULL                                      
+REMARK   4                                                                      
+REMARK   4 6LHX COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
+REMARK 100                                                                      
+REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 11-DEC-19.                  
+REMARK 100 THE DEPOSITION ID IS D_1300014781.                                   
+REMARK 200                                                                      
+REMARK 200 EXPERIMENTAL DETAILS                                                 
+REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
+REMARK 200  DATE OF DATA COLLECTION        : 12-MAR-19                          
+REMARK 200  TEMPERATURE           (KELVIN) : 100                                
+REMARK 200  PH                             : NULL                               
+REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
+REMARK 200                                                                      
+REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
+REMARK 200  RADIATION SOURCE               : PAL/PLS                            
+REMARK 200  BEAMLINE                       : 7A (6B, 6C1)                       
+REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
+REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
+REMARK 200  WAVELENGTH OR RANGE        (A) : 0.97910                            
+REMARK 200  MONOCHROMATOR                  : NULL                               
+REMARK 200  OPTICS                         : NULL                               
+REMARK 200                                                                      
+REMARK 200  DETECTOR TYPE                  : CCD                                
+REMARK 200  DETECTOR MANUFACTURER          : ADSC QUANTUM 270                   
+REMARK 200  INTENSITY-INTEGRATION SOFTWARE : HKL-2000                           
+REMARK 200  DATA SCALING SOFTWARE          : HKL-2000                           
+REMARK 200                                                                      
+REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 181015                             
+REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.500                              
+REMARK 200  RESOLUTION RANGE LOW       (A) : 50.000                             
+REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : NULL                               
+REMARK 200                                                                      
+REMARK 200 OVERALL.                                                             
+REMARK 200  COMPLETENESS FOR RANGE     (%) : 99.6                               
+REMARK 200  DATA REDUNDANCY                : 7.300                              
+REMARK 200  R MERGE                    (I) : 0.14000                            
+REMARK 200  R SYM                      (I) : NULL                               
+REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 10.5400                            
+REMARK 200                                                                      
+REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
+REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.50                     
+REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.59                     
+REMARK 200  COMPLETENESS FOR SHELL     (%) : 99.1                               
+REMARK 200  DATA REDUNDANCY IN SHELL       : NULL                               
+REMARK 200  R MERGE FOR SHELL          (I) : 1.66600                            
+REMARK 200  R SYM FOR SHELL            (I) : NULL                               
+REMARK 200  <I/SIGMA(I)> FOR SHELL         : 1.150                              
+REMARK 200                                                                      
+REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
+REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: SAD                          
+REMARK 200 SOFTWARE USED: AUTOSOL                                               
+REMARK 200 STARTING MODEL: NULL                                                 
+REMARK 200                                                                      
+REMARK 200 REMARK: NULL                                                         
+REMARK 280                                                                      
+REMARK 280 CRYSTAL                                                              
+REMARK 280 SOLVENT CONTENT, VS   (%): 63.51                                     
+REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.37                     
+REMARK 280                                                                      
+REMARK 280 CRYSTALLIZATION CONDITIONS: 22% PPG400, 0.1 M MES PH 6.5, 0.2 M      
+REMARK 280  MGCL2, VAPOR DIFFUSION, SITTING DROP, TEMPERATURE 293K              
+REMARK 290                                                                      
+REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
+REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: C 1 2 1                          
+REMARK 290                                                                      
+REMARK 290      SYMOP   SYMMETRY                                                
+REMARK 290     NNNMMM   OPERATOR                                                
+REMARK 290       1555   X,Y,Z                                                   
+REMARK 290       2555   -X,Y,-Z                                                 
+REMARK 290       3555   X+1/2,Y+1/2,Z                                           
+REMARK 290       4555   -X+1/2,Y+1/2,-Z                                         
+REMARK 290                                                                      
+REMARK 290     WHERE NNN -> OPERATOR NUMBER                                     
+REMARK 290           MMM -> TRANSLATION VECTOR                                  
+REMARK 290                                                                      
+REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS                            
+REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM             
+REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY                
+REMARK 290 RELATED MOLECULES.                                                   
+REMARK 290   SMTRY1   1  1.000000  0.000000  0.000000        0.00000            
+REMARK 290   SMTRY2   1  0.000000  1.000000  0.000000        0.00000            
+REMARK 290   SMTRY3   1  0.000000  0.000000  1.000000        0.00000            
+REMARK 290   SMTRY1   2 -1.000000  0.000000  0.000000        0.00000            
+REMARK 290   SMTRY2   2  0.000000  1.000000  0.000000        0.00000            
+REMARK 290   SMTRY3   2  0.000000  0.000000 -1.000000        0.00000            
+REMARK 290   SMTRY1   3  1.000000  0.000000  0.000000       90.21200            
+REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000       84.29200            
+REMARK 290   SMTRY3   3  0.000000  0.000000  1.000000        0.00000            
+REMARK 290   SMTRY1   4 -1.000000  0.000000  0.000000       90.21200            
+REMARK 290   SMTRY2   4  0.000000  1.000000  0.000000       84.29200            
+REMARK 290   SMTRY3   4  0.000000  0.000000 -1.000000        0.00000            
+REMARK 290                                                                      
+REMARK 290 REMARK: NULL                                                         
+REMARK 300                                                                      
+REMARK 300 BIOMOLECULE: 1                                                       
+REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM                
+REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN                  
+REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON               
+REMARK 300 BURIED SURFACE AREA.                                                 
+REMARK 350                                                                      
+REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN           
+REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE                
+REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS          
+REMARK 350 GIVEN BELOW.  BOTH NON-CRYSTALLOGRAPHIC AND                          
+REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.                               
+REMARK 350                                                                      
+REMARK 350 BIOMOLECULE: 1                                                       
+REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: TETRAMERIC                        
+REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B, C, D                            
+REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
+REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
+REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
+REMARK 465                                                                      
+REMARK 465 MISSING RESIDUES                                                     
+REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE                       
+REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
+REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)                
+REMARK 465                                                                      
+REMARK 465   M RES C SSSEQI                                                     
+REMARK 465     GLY A     1                                                      
+REMARK 465     GLU A    45                                                      
+REMARK 465     ASN A    56                                                      
+REMARK 465     LYS A    57                                                      
+REMARK 465     GLU A    58                                                      
+REMARK 465     ASN A   295                                                      
+REMARK 465     ASN A   343                                                      
+REMARK 465     GLN A   344                                                      
+REMARK 465     GLY A   345                                                      
+REMARK 465     GLY A   392                                                      
+REMARK 465     GLN A   393                                                      
+REMARK 465     TYR A   422                                                      
+REMARK 465     ALA A   444                                                      
+REMARK 465     ASN A   455                                                      
+REMARK 465     GLU A   456                                                      
+REMARK 465     GLY B     1                                                      
+REMARK 465     SER B    39                                                      
+REMARK 465     TRP B    40                                                      
+REMARK 465     ALA B    41                                                      
+REMARK 465     LYS B    42                                                      
+REMARK 465     LEU B    43                                                      
+REMARK 465     LEU B    44                                                      
+REMARK 465     GLU B    45                                                      
+REMARK 465     PRO B    46                                                      
+REMARK 465     ILE B    47                                                      
+REMARK 465     ALA B    48                                                      
+REMARK 465     GLN B    49                                                      
+REMARK 465     GLU B    50                                                      
+REMARK 465     ILE B    51                                                      
+REMARK 465     GLY B    52                                                      
+REMARK 465     LEU B    53                                                      
+REMARK 465     ASP B    54                                                      
+REMARK 465     VAL B    55                                                      
+REMARK 465     ASN B    56                                                      
+REMARK 465     LYS B    57                                                      
+REMARK 465     GLU B    58                                                      
+REMARK 465     ASN B    59                                                      
+REMARK 465     ASP B    60                                                      
+REMARK 465     LEU B    61                                                      
+REMARK 465     VAL B    62                                                      
+REMARK 465     SER B    63                                                      
+REMARK 465     LEU B    64                                                      
+REMARK 465     ALA B    65                                                      
+REMARK 465     GLN B    66                                                      
+REMARK 465     TYR B    67                                                      
+REMARK 465     TYR B    68                                                      
+REMARK 465     CYS B    69                                                      
+REMARK 465     ASN B    70                                                      
+REMARK 465     GLU B    71                                                      
+REMARK 465     ASN B    72                                                      
+REMARK 465     GLN B    73                                                      
+REMARK 465     GLY B    74                                                      
+REMARK 465     ASN B    75                                                      
+REMARK 465     ARG B    76                                                      
+REMARK 465     GLY B    77                                                      
+REMARK 465     ARG B    78                                                      
+REMARK 465     ILE B    79                                                      
+REMARK 465     ASN B    80                                                      
+REMARK 465     GLN B    81                                                      
+REMARK 465     ILE B    82                                                      
+REMARK 465     ILE B    83                                                      
+REMARK 465     ALA B   161                                                      
+REMARK 465     VAL B   162                                                      
+REMARK 465     LEU B   163                                                      
+REMARK 465     ILE B   164                                                      
+REMARK 465     LYS B   165                                                      
+REMARK 465     ASP B   166                                                      
+REMARK 465     ASP B   167                                                      
+REMARK 465     TYR B   168                                                      
+REMARK 465     GLU B   169                                                      
+REMARK 465     LYS B   170                                                      
+REMARK 465     TYR B   171                                                      
+REMARK 465     SER B   172                                                      
+REMARK 465     GLN B   344                                                      
+REMARK 465     GLY B   345                                                      
+REMARK 465     ALA B   419                                                      
+REMARK 465     THR B   420                                                      
+REMARK 465     GLY B   421                                                      
+REMARK 465     TYR B   422                                                      
+REMARK 465     ASP B   443                                                      
+REMARK 465     ALA B   444                                                      
+REMARK 465     ARG B   445                                                      
+REMARK 465     ASN B   455                                                      
+REMARK 465     GLU B   456                                                      
+REMARK 465     ALA B   457                                                      
+REMARK 465     GLY C     1                                                      
+REMARK 465     LEU C    53                                                      
+REMARK 465     ASP C    54                                                      
+REMARK 465     VAL C    55                                                      
+REMARK 465     ASN C    56                                                      
+REMARK 465     LYS C    57                                                      
+REMARK 465     GLU C    58                                                      
+REMARK 465     ASN C   343                                                      
+REMARK 465     GLN C   344                                                      
+REMARK 465     GLY C   345                                                      
+REMARK 465     ASP C   443                                                      
+REMARK 465     ALA C   444                                                      
+REMARK 465     ARG C   445                                                      
+REMARK 465     ASN C   455                                                      
+REMARK 465     GLU C   456                                                      
+REMARK 465     ALA C   457                                                      
+REMARK 465     LEU C   458                                                      
+REMARK 465     ASN C   476                                                      
+REMARK 465     GLY D     1                                                      
+REMARK 465     TRP D    40                                                      
+REMARK 465     ALA D    41                                                      
+REMARK 465     LYS D    42                                                      
+REMARK 465     LEU D    43                                                      
+REMARK 465     LEU D    44                                                      
+REMARK 465     GLU D    45                                                      
+REMARK 465     PRO D    46                                                      
+REMARK 465     ILE D    47                                                      
+REMARK 465     ALA D    48                                                      
+REMARK 465     GLN D    49                                                      
+REMARK 465     GLU D    50                                                      
+REMARK 465     ILE D    51                                                      
+REMARK 465     GLY D    52                                                      
+REMARK 465     LEU D    53                                                      
+REMARK 465     ASP D    54                                                      
+REMARK 465     VAL D    55                                                      
+REMARK 465     ASN D    56                                                      
+REMARK 465     LYS D    57                                                      
+REMARK 465     GLU D    58                                                      
+REMARK 465     ASN D    59                                                      
+REMARK 465     ASP D    60                                                      
+REMARK 465     LEU D    61                                                      
+REMARK 465     VAL D    62                                                      
+REMARK 465     SER D    63                                                      
+REMARK 465     LEU D    64                                                      
+REMARK 465     ALA D    65                                                      
+REMARK 465     GLN D    66                                                      
+REMARK 465     TYR D    67                                                      
+REMARK 465     TYR D    68                                                      
+REMARK 465     CYS D    69                                                      
+REMARK 465     ASN D    70                                                      
+REMARK 465     GLU D    71                                                      
+REMARK 465     ASN D    72                                                      
+REMARK 465     GLN D    73                                                      
+REMARK 465     GLY D    74                                                      
+REMARK 465     ASN D    75                                                      
+REMARK 465     ARG D    76                                                      
+REMARK 465     GLY D    77                                                      
+REMARK 465     ARG D    78                                                      
+REMARK 465     ILE D    79                                                      
+REMARK 465     ASN D    80                                                      
+REMARK 465     GLN D    81                                                      
+REMARK 465     SER D   159                                                      
+REMARK 465     GLU D   160                                                      
+REMARK 465     ALA D   161                                                      
+REMARK 465     VAL D   162                                                      
+REMARK 465     LEU D   163                                                      
+REMARK 465     ILE D   164                                                      
+REMARK 465     LYS D   165                                                      
+REMARK 465     ASP D   166                                                      
+REMARK 465     ASP D   167                                                      
+REMARK 465     TYR D   168                                                      
+REMARK 465     GLU D   169                                                      
+REMARK 465     LYS D   170                                                      
+REMARK 465     TYR D   171                                                      
+REMARK 465     SER D   172                                                      
+REMARK 465     VAL D   292                                                      
+REMARK 465     GLU D   293                                                      
+REMARK 465     TYR D   294                                                      
+REMARK 465     ASN D   295                                                      
+REMARK 465     TYR D   341                                                      
+REMARK 465     MSE D   342                                                      
+REMARK 465     ASN D   343                                                      
+REMARK 465     GLN D   344                                                      
+REMARK 465     GLY D   345                                                      
+REMARK 465     THR D   346                                                      
+REMARK 465     GLN D   393                                                      
+REMARK 465     ALA D   444                                                      
+REMARK 465     ARG D   445                                                      
+REMARK 465     ASN D   454                                                      
+REMARK 465     ASN D   455                                                      
+REMARK 465     GLU D   456                                                      
+REMARK 465     ALA D   457                                                      
+REMARK 465     ASN D   476                                                      
+REMARK 470                                                                      
+REMARK 470 MISSING ATOM                                                         
+REMARK 470 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER;           
+REMARK 470 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;          
+REMARK 470 I=INSERTION CODE):                                                   
+REMARK 470   M RES CSSEQI  ATOMS                                                
+REMARK 470     HIS A   2    CG   ND1  CD2  CE1  NE2                             
+REMARK 470     LYS A  42    CG   CD   CE   NZ                                   
+REMARK 470     LEU A  43    CG   CD1  CD2                                       
+REMARK 470     LEU A  44    CG   CD1  CD2                                       
+REMARK 470     GLN A  49    CG   CD   OE1  NE2                                  
+REMARK 470     GLU A  50    CG   CD   OE1  OE2                                  
+REMARK 470     LEU A  53    CG   CD1  CD2                                       
+REMARK 470     ASP A  54    CG   OD1  OD2                                       
+REMARK 470     VAL A  55    CG1  CG2                                            
+REMARK 470     ASN A  59    CG   OD1  ND2                                       
+REMARK 470     ASP A  60    CG   OD1  OD2                                       
+REMARK 470     GLU A  71    CG   CD   OE1  OE2                                  
+REMARK 470     GLN A  73    CG   CD   OE1  NE2                                  
+REMARK 470     ARG A  78    CG   CD   NE   CZ   NH1  NH2                        
+REMARK 470     GLU A  86    CG   CD   OE1  OE2                                  
+REMARK 470     ARG A  89    CG   CD   NE   CZ   NH1  NH2                        
+REMARK 470     LYS A  90    CG   CD   CE   NZ                                   
+REMARK 470     LYS A 165    CG   CD   CE   NZ                                   
+REMARK 470     TYR A 214    CG   CD1  CD2  CE1  CE2  CZ   OH                    
+REMARK 470     GLU A 215    CG   CD   OE1  OE2                                  
+REMARK 470     ARG A 216    CG   CD   NE   CZ   NH1  NH2                        
+REMARK 470     ASP A 233    CG   OD1  OD2                                       
+REMARK 470     ARG A 255    CG   CD   NE   CZ   NH1  NH2                        
+REMARK 470     GLU A 298    CG   CD   OE1  OE2                                  
+REMARK 470     HIS A 301    CG   ND1  CD2  CE1  NE2                             
+REMARK 470     ARG A 315    CG   CD   NE   CZ   NH1  NH2                        
+REMARK 470     LYS A 316    CG   CD   CE   NZ                                   
+REMARK 470     LEU A 326    CG   CD1  CD2                                       
+REMARK 470     GLU A 339    CG   CD   OE1  OE2                                  
+REMARK 470     MSE A 342    CG  SE    CE                                        
+REMARK 470     THR A 346    OG1  CG2                                            
+REMARK 470     LYS A 361    CG   CD   CE   NZ                                   
+REMARK 470     LYS A 362    CG   CD   CE   NZ                                   
+REMARK 470     LYS A 369    CG   CD   CE   NZ                                   
+REMARK 470     ILE A 389    CG1  CG2  CD1                                       
+REMARK 470     ASP A 390    CG   OD1  OD2                                       
+REMARK 470     LYS A 391    CG   CD   CE   NZ                                   
+REMARK 470     LYS A 396    CG   CD   CE   NZ                                   
+REMARK 470     LYS A 398    CG   CD   CE   NZ                                   
+REMARK 470     ASN A 411    CG   OD1  ND2                                       
+REMARK 470     VAL A 417    CG1  CG2                                            
+REMARK 470     ILE A 423    CG1  CG2  CD1                                       
+REMARK 470     LYS A 425    CG   CD   CE   NZ                                   
+REMARK 470     GLU A 433    CG   CD   OE1  OE2                                  
+REMARK 470     GLU A 436    CG   CD   OE1  OE2                                  
+REMARK 470     THR A 437    OG1  CG2                                            
+REMARK 470     ASP A 443    CG   OD1  OD2                                       
+REMARK 470     LYS A 447    CG   CD   CE   NZ                                   
+REMARK 470     LYS A 448    CG   CD   CE   NZ                                   
+REMARK 470     LEU A 449    CG   CD1  CD2                                       
+REMARK 470     PHE A 450    CG   CD1  CD2  CE1  CE2  CZ                         
+REMARK 470     GLU A 452    CG   CD   OE1  OE2                                  
+REMARK 470     LEU A 453    CG   CD1  CD2                                       
+REMARK 470     ASN A 454    CG   OD1  ND2                                       
+REMARK 470     LEU A 458    CG   CD1  CD2                                       
+REMARK 470     ILE A 460    CG1  CG2  CD1                                       
+REMARK 470     GLU A 462    CG   CD   OE1  OE2                                  
+REMARK 470     ILE A 473    CG1  CG2  CD1                                       
+REMARK 470     HIS B   2    CG   ND1  CD2  CE1  NE2                             
+REMARK 470     LEU B  84    CG   CD1  CD2                                       
+REMARK 470     ASP B  85    CG   OD1  OD2                                       
+REMARK 470     GLU B  86    CG   CD   OE1  OE2                                  
+REMARK 470     PHE B  87    CG   CD1  CD2  CE1  CE2  CZ                         
+REMARK 470     SER B  88    OG                                                  
+REMARK 470     ARG B  89    CG   CD   NE   CZ   NH1  NH2                        
+REMARK 470     LYS B 143    CG   CD   CE   NZ                                   
+REMARK 470     GLU B 160    CG   CD   OE1  OE2                                  
+REMARK 470     ILE B 173    CG1  CG2  CD1                                       
+REMARK 470     LYS B 174    CG   CD   CE   NZ                                   
+REMARK 470     PRO B 177    CG   CD                                             
+REMARK 470     ARG B 216    CG   CD   NE   CZ   NH1  NH2                        
+REMARK 470     ASP B 233    CG   OD1  OD2                                       
+REMARK 470     GLU B 293    CG   CD   OE1  OE2                                  
+REMARK 470     ASN B 295    CG   OD1  ND2                                       
+REMARK 470     HIS B 296    CG   ND1  CD2  CE1  NE2                             
+REMARK 470     ARG B 315    CG   CD   NE   CZ   NH1  NH2                        
+REMARK 470     GLU B 339    CG   CD   OE1  OE2                                  
+REMARK 470     ASN B 343    CG   OD1  ND2                                       
+REMARK 470     THR B 346    OG1  CG2                                            
+REMARK 470     ASP B 350    CG   OD1  OD2                                       
+REMARK 470     LYS B 361    CG   CD   CE   NZ                                   
+REMARK 470     LYS B 362    CG   CD   CE   NZ                                   
+REMARK 470     GLU B 365    CG   CD   OE1  OE2                                  
+REMARK 470     LYS B 369    CG   CD   CE   NZ                                   
+REMARK 470     ARG B 371    CG   CD   NE   CZ   NH1  NH2                        
+REMARK 470     LYS B 391    CG   CD   CE   NZ                                   
+REMARK 470     GLN B 393    CG   CD   OE1  NE2                                  
+REMARK 470     VAL B 414    CG1  CG2                                            
+REMARK 470     ILE B 423    CG1  CG2  CD1                                       
+REMARK 470     GLU B 434    CG   CD   OE1  OE2                                  
+REMARK 470     GLU B 436    CG   CD   OE1  OE2                                  
+REMARK 470     THR B 437    OG1  CG2                                            
+REMARK 470     LYS B 447    CG   CD   CE   NZ                                   
+REMARK 470     LYS B 448    CG   CD   CE   NZ                                   
+REMARK 470     LEU B 449    CG   CD1  CD2                                       
+REMARK 470     PHE B 450    CG   CD1  CD2  CE1  CE2  CZ                         
+REMARK 470     GLU B 452    CG   CD   OE1  OE2                                  
+REMARK 470     LEU B 453    CG   CD1  CD2                                       
+REMARK 470     ASN B 454    CG   OD1  ND2                                       
+REMARK 470     LEU B 458    CG   CD1  CD2                                       
+REMARK 470     GLU B 461    CG   CD   OE1  OE2                                  
+REMARK 470     GLU B 462    CG   CD   OE1  OE2                                  
+REMARK 470     ASN B 476    CG   OD1  ND2                                       
+REMARK 470     HIS C   2    CG   ND1  CD2  CE1  NE2                             
+REMARK 470     LYS C  16    CG   CD   CE   NZ                                   
+REMARK 470     LYS C  42    CG   CD   CE   NZ                                   
+REMARK 470     LEU C  43    CG   CD1  CD2                                       
+REMARK 470     ILE C  51    CG1  CG2  CD1                                       
+REMARK 470     ASN C  59    CG   OD1  ND2                                       
+REMARK 470     GLU C  71    CG   CD   OE1  OE2                                  
+REMARK 470     ARG C  78    CG   CD   NE   CZ   NH1  NH2                        
+REMARK 470     ARG C  89    CG   CD   NE   CZ   NH1  NH2                        
+REMARK 470     LYS C  90    CG   CD   CE   NZ                                   
+REMARK 470     GLU C 123    CG   CD   OE1  OE2                                  
+REMARK 470     LYS C 165    CG   CD   CE   NZ                                   
+REMARK 470     LYS C 174    CG   CD   CE   NZ                                   
+REMARK 470     VAL C 210    CG1  CG2                                            
+REMARK 470     TYR C 214    CG   CD1  CD2  CE1  CE2  CZ   OH                    
+REMARK 470     ARG C 216    CG   CD   NE   CZ   NH1  NH2                        
+REMARK 470     ARG C 231    CG   CD   NE   CZ   NH1  NH2                        
+REMARK 470     ASP C 233    CG   OD1  OD2                                       
+REMARK 470     GLU C 247    CG   CD   OE1  OE2                                  
+REMARK 470     LYS C 281    CG   CD   CE   NZ                                   
+REMARK 470     VAL C 292    CG1  CG2                                            
+REMARK 470     GLU C 293    CG   CD   OE1  OE2                                  
+REMARK 470     HIS C 296    CG   ND1  CD2  CE1  NE2                             
+REMARK 470     GLU C 300    CG   CD   OE1  OE2                                  
+REMARK 470     ARG C 315    CG   CD   NE   CZ   NH1  NH2                        
+REMARK 470     LYS C 316    CG   CD   CE   NZ                                   
+REMARK 470     MSE C 342    CG  SE    CE                                        
+REMARK 470     THR C 346    OG1  CG2                                            
+REMARK 470     ASP C 349    CG   OD1  OD2                                       
+REMARK 470     LYS C 361    CG   CD   CE   NZ                                   
+REMARK 470     LYS C 362    CG   CD   CE   NZ                                   
+REMARK 470     GLU C 365    CG   CD   OE1  OE2                                  
+REMARK 470     LYS C 369    CG   CD   CE   NZ                                   
+REMARK 470     LYS C 388    CG   CD   CE   NZ                                   
+REMARK 470     ILE C 389    CG1  CG2  CD1                                       
+REMARK 470     ASP C 390    CG   OD1  OD2                                       
+REMARK 470     LYS C 391    CG   CD   CE   NZ                                   
+REMARK 470     GLN C 393    CG   CD   OE1  NE2                                  
+REMARK 470     LYS C 396    CG   CD   CE   NZ                                   
+REMARK 470     LYS C 398    CG   CD   CE   NZ                                   
+REMARK 470     GLN C 410    CG   CD   OE1  NE2                                  
+REMARK 470     THR C 420    OG1  CG2                                            
+REMARK 470     LYS C 425    CG   CD   CE   NZ                                   
+REMARK 470     TRP C 428    CG   CD1  CD2  NE1  CE2  CE3  CZ2                   
+REMARK 470     TRP C 428    CZ3  CH2                                            
+REMARK 470     LYS C 430    CG   CD   CE   NZ                                   
+REMARK 470     VAL C 431    CG1  CG2                                            
+REMARK 470     GLU C 434    CG   CD   OE1  OE2                                  
+REMARK 470     GLU C 436    CG   CD   OE1  OE2                                  
+REMARK 470     LYS C 447    CG   CD   CE   NZ                                   
+REMARK 470     LYS C 448    CG   CD   CE   NZ                                   
+REMARK 470     LEU C 449    CG   CD1  CD2                                       
+REMARK 470     GLU C 452    CG   CD   OE1  OE2                                  
+REMARK 470     LEU C 453    CG   CD1  CD2                                       
+REMARK 470     ASN C 454    CG   OD1  ND2                                       
+REMARK 470     GLU C 461    CG   CD   OE1  OE2                                  
+REMARK 470     SER C 475    OG                                                  
+REMARK 470     VAL D  38    CG1  CG2                                            
+REMARK 470     SER D  39    OG                                                  
+REMARK 470     ILE D  82    CG1  CG2  CD1                                       
+REMARK 470     ILE D  83    CG1  CG2  CD1                                       
+REMARK 470     LEU D  84    CG   CD1  CD2                                       
+REMARK 470     ASP D  85    CG   OD1  OD2                                       
+REMARK 470     GLU D  86    CG   CD   OE1  OE2                                  
+REMARK 470     PHE D  87    CG   CD1  CD2  CE1  CE2  CZ                         
+REMARK 470     ARG D  89    CG   CD   NE   CZ   NH1  NH2                        
+REMARK 470     LYS D  90    CG   CD   CE   NZ                                   
+REMARK 470     ASP D  92    CG   OD1  OD2                                       
+REMARK 470     TYR D 113    CG   CD1  CD2  CE1  CE2  CZ   OH                    
+REMARK 470     LYS D 119    CG   CD   CE   NZ                                   
+REMARK 470     LYS D 143    CG   CD   CE   NZ                                   
+REMARK 470     HIS D 152    CG   ND1  CD2  CE1  NE2                             
+REMARK 470     ASP D 154    CG   OD1  OD2                                       
+REMARK 470     GLU D 156    CG   CD   OE1  OE2                                  
+REMARK 470     ILE D 173    CG1  CG2  CD1                                       
+REMARK 470     LYS D 174    CG   CD   CE   NZ                                   
+REMARK 470     ARG D 209    CG   CD   NE   CZ   NH1  NH2                        
+REMARK 470     GLU D 215    CG   CD   OE1  OE2                                  
+REMARK 470     ARG D 216    CG   CD   NE   CZ   NH1  NH2                        
+REMARK 470     LYS D 226    CG   CD   CE   NZ                                   
+REMARK 470     LYS D 283    CG   CD   CE   NZ                                   
+REMARK 470     GLU D 298    CG   CD   OE1  OE2                                  
+REMARK 470     THR D 299    OG1  CG2                                            
+REMARK 470     HIS D 301    CG   ND1  CD2  CE1  NE2                             
+REMARK 470     GLU D 303    CG   CD   OE1  OE2                                  
+REMARK 470     GLN D 308    CG   CD   OE1  NE2                                  
+REMARK 470     LYS D 311    CG   CD   CE   NZ                                   
+REMARK 470     ARG D 315    CG   CD   NE   CZ   NH1  NH2                        
+REMARK 470     LYS D 316    CG   CD   CE   NZ                                   
+REMARK 470     LEU D 326    CG   CD1  CD2                                       
+REMARK 470     GLU D 339    CG   CD   OE1  OE2                                  
+REMARK 470     LEU D 340    CG   CD1  CD2                                       
+REMARK 470     ILE D 347    CG1  CG2  CD1                                       
+REMARK 470     LYS D 361    CG   CD   CE   NZ                                   
+REMARK 470     LYS D 362    CG   CD   CE   NZ                                   
+REMARK 470     GLU D 365    CG   CD   OE1  OE2                                  
+REMARK 470     LYS D 369    CG   CD   CE   NZ                                   
+REMARK 470     ASN D 387    CG   OD1  ND2                                       
+REMARK 470     LYS D 396    CG   CD   CE   NZ                                   
+REMARK 470     LYS D 398    CG   CD   CE   NZ                                   
+REMARK 470     GLN D 401    CG   CD   OE1  NE2                                  
+REMARK 470     SER D 402    OG                                                  
+REMARK 470     GLU D 409    CG   CD   OE1  OE2                                  
+REMARK 470     THR D 420    OG1  CG2                                            
+REMARK 470     LYS D 425    CG   CD   CE   NZ                                   
+REMARK 470     LEU D 427    CG   CD1  CD2                                       
+REMARK 470     ASN D 432    CG   OD1  ND2                                       
+REMARK 470     GLU D 433    CG   CD   OE1  OE2                                  
+REMARK 470     GLU D 434    CG   CD   OE1  OE2                                  
+REMARK 470     ASP D 443    CG   OD1  OD2                                       
+REMARK 470     LYS D 447    CG   CD   CE   NZ                                   
+REMARK 470     LYS D 448    CG   CD   CE   NZ                                   
+REMARK 470     LEU D 449    CG   CD1  CD2                                       
+REMARK 470     PHE D 450    CG   CD1  CD2  CE1  CE2  CZ                         
+REMARK 470     GLU D 452    CG   CD   OE1  OE2                                  
+REMARK 470     LEU D 453    CG   CD1  CD2                                       
+REMARK 470     LEU D 458    CG   CD1  CD2                                       
+REMARK 470     SER D 459    OG                                                  
+REMARK 470     ILE D 460    CG1  CG2  CD1                                       
+REMARK 470     GLU D 461    CG   CD   OE1  OE2                                  
+REMARK 470     GLU D 462    CG   CD   OE1  OE2                                  
+REMARK 470     ILE D 468    CG1  CG2  CD1                                       
+REMARK 470     GLU D 469    CG   CD   OE1  OE2                                  
+REMARK 470     ILE D 473    CG1  CG2  CD1                                       
+REMARK 470     SER D 475    OG                                                  
+REMARK 500                                                                      
+REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
+REMARK 500 SUBTOPIC: TORSION ANGLES                                             
+REMARK 500                                                                      
+REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:            
+REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
+REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                             
+REMARK 500                                                                      
+REMARK 500 STANDARD TABLE:                                                      
+REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)                    
+REMARK 500                                                                      
+REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-           
+REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400            
+REMARK 500                                                                      
+REMARK 500  M RES CSSEQI        PSI       PHI                                   
+REMARK 500    PRO A 104       48.37    -74.27                                   
+REMARK 500    TYR A 214       -2.48     63.58                                   
+REMARK 500    LYS A 316       36.66    -98.11                                   
+REMARK 500    TYR A 385     -120.88     54.72                                   
+REMARK 500    PRO A 440       91.31    -65.60                                   
+REMARK 500    HIS B 157       62.95     76.84                                   
+REMARK 500    LYS B 174       36.95    -98.78                                   
+REMARK 500    ASP B 233       77.25     59.31                                   
+REMARK 500    ASN B 295     -106.97     49.78                                   
+REMARK 500    LYS B 316       38.03    -98.07                                   
+REMARK 500    TYR B 385     -120.54     55.23                                   
+REMARK 500    LYS B 388     -145.75   -138.61                                   
+REMARK 500    LYS B 391       27.42   -158.61                                   
+REMARK 500    GLU B 434       52.89   -100.09                                   
+REMARK 500    PRO B 440       89.97    -66.50                                   
+REMARK 500    GLU C  50      -74.51    -75.60                                   
+REMARK 500    PRO C 104       48.05    -74.73                                   
+REMARK 500    TYR C 214       -2.58     63.33                                   
+REMARK 500    ASP C 233       75.57     59.26                                   
+REMARK 500    ASN C 295     -113.44     49.26                                   
+REMARK 500    LYS C 316       36.43    -98.16                                   
+REMARK 500    TYR C 341       41.48    -87.65                                   
+REMARK 500    TYR C 385     -121.72     54.24                                   
+REMARK 500    LYS C 391       29.33   -143.63                                   
+REMARK 500    TYR C 422      -76.47   -112.90                                   
+REMARK 500    PRO C 440       91.74    -67.06                                   
+REMARK 500    LYS D 150       71.32   -105.81                                   
+REMARK 500    GLU D 156       47.58    -91.00                                   
+REMARK 500    HIS D 157       64.41   -174.86                                   
+REMARK 500    ASP D 233       80.21     60.17                                   
+REMARK 500    LYS D 316       37.62    -96.69                                   
+REMARK 500    ASP D 349     -140.12   -105.88                                   
+REMARK 500    TYR D 385     -121.77     56.17                                   
+REMARK 500    ALA D 419      -78.75    -62.81                                   
+REMARK 500    TYR D 422      -79.29   -114.41                                   
+REMARK 500    PRO D 440       89.64    -64.38                                   
+REMARK 500                                                                      
+REMARK 500 REMARK: NULL                                                         
+DBREF  6LHX A    3   476  UNP    J8G6Z1   J8G6Z1_BACCE     1    474             
+DBREF  6LHX B    3   476  UNP    J8G6Z1   J8G6Z1_BACCE     1    474             
+DBREF  6LHX C    3   476  UNP    J8G6Z1   J8G6Z1_BACCE     1    474             
+DBREF  6LHX D    3   476  UNP    J8G6Z1   J8G6Z1_BACCE     1    474             
+SEQADV 6LHX GLY A    1  UNP  J8G6Z1              EXPRESSION TAG                 
+SEQADV 6LHX HIS A    2  UNP  J8G6Z1              EXPRESSION TAG                 
+SEQADV 6LHX GLY B    1  UNP  J8G6Z1              EXPRESSION TAG                 
+SEQADV 6LHX HIS B    2  UNP  J8G6Z1              EXPRESSION TAG                 
+SEQADV 6LHX GLY C    1  UNP  J8G6Z1              EXPRESSION TAG                 
+SEQADV 6LHX HIS C    2  UNP  J8G6Z1              EXPRESSION TAG                 
+SEQADV 6LHX GLY D    1  UNP  J8G6Z1              EXPRESSION TAG                 
+SEQADV 6LHX HIS D    2  UNP  J8G6Z1              EXPRESSION TAG                 
+SEQRES   1 A  476  GLY HIS MSE ASN PRO ILE VAL GLU LEU PHE ILE LYS ASP          
+SEQRES   2 A  476  PHE THR LYS GLU VAL MSE GLU GLU ASN ALA ALA ILE PHE          
+SEQRES   3 A  476  ALA GLY ALA GLY LEU SER MSE SER VAL GLY TYR VAL SER          
+SEQRES   4 A  476  TRP ALA LYS LEU LEU GLU PRO ILE ALA GLN GLU ILE GLY          
+SEQRES   5 A  476  LEU ASP VAL ASN LYS GLU ASN ASP LEU VAL SER LEU ALA          
+SEQRES   6 A  476  GLN TYR TYR CYS ASN GLU ASN GLN GLY ASN ARG GLY ARG          
+SEQRES   7 A  476  ILE ASN GLN ILE ILE LEU ASP GLU PHE SER ARG LYS VAL          
+SEQRES   8 A  476  ASP LEU THR GLU ASN HIS LYS ILE LEU ALA ARG LEU PRO          
+SEQRES   9 A  476  ILE HIS THR TYR TRP THR THR ASN TYR ASP ARG LEU ILE          
+SEQRES  10 A  476  GLU LYS ALA LEU GLU GLU GLU ASN LYS ILE ALA ASP VAL          
+SEQRES  11 A  476  LYS TYR THR VAL LYS GLN LEU ALA THR THR LYS VAL LYS          
+SEQRES  12 A  476  ARG ASP ALA VAL VAL TYR LYS MSE HIS GLY ASP VAL GLU          
+SEQRES  13 A  476  HIS PRO SER GLU ALA VAL LEU ILE LYS ASP ASP TYR GLU          
+SEQRES  14 A  476  LYS TYR SER ILE LYS MSE ASP PRO TYR ILE LYS ALA LEU          
+SEQRES  15 A  476  SER GLY ASP LEU VAL SER LYS THR PHE LEU PHE VAL GLY          
+SEQRES  16 A  476  PHE SER PHE THR ASP PRO ASN LEU ASP TYR ILE LEU SER          
+SEQRES  17 A  476  ARG VAL ARG SER ALA TYR GLU ARG ASP GLN ARG ARG HIS          
+SEQRES  18 A  476  TYR CYS LEU ILE LYS LYS GLU GLU ARG ARG PRO ASP GLU          
+SEQRES  19 A  476  LEU GLU ALA ASP PHE GLU TYR ARG VAL ARG LYS GLN GLU          
+SEQRES  20 A  476  LEU PHE ILE SER ASP LEU SER ARG PHE ASN ILE LYS THR          
+SEQRES  21 A  476  ILE VAL LEU ASN ASN TYR ASN GLU ILE THR GLU ILE LEU          
+SEQRES  22 A  476  GLN ARG ILE GLU ASN ASN ILE LYS THR LYS THR VAL PHE          
+SEQRES  23 A  476  LEU SER GLY SER ALA VAL GLU TYR ASN HIS TRP GLU THR          
+SEQRES  24 A  476  GLU HIS ALA GLU GLN PHE ILE HIS GLN LEU SER LYS GLU          
+SEQRES  25 A  476  LEU ILE ARG LYS ASP PHE ASN ILE VAL SER GLY PHE GLY          
+SEQRES  26 A  476  LEU GLY VAL GLY SER PHE VAL ILE ASN GLY VAL LEU GLU          
+SEQRES  27 A  476  GLU LEU TYR MSE ASN GLN GLY THR ILE ASP ASP ASP ARG          
+SEQRES  28 A  476  LEU ILE LEU ARG PRO PHE PRO GLN GLY LYS LYS GLY GLU          
+SEQRES  29 A  476  GLU GLN TRP ASP LYS TYR ARG ARG ASP MSE ILE THR ARG          
+SEQRES  30 A  476  THR GLY VAL SER ILE PHE LEU TYR GLY ASN LYS ILE ASP          
+SEQRES  31 A  476  LYS GLY GLN VAL VAL LYS ALA LYS GLY VAL GLN SER GLU          
+SEQRES  32 A  476  PHE ASN ILE SER PHE GLU GLN ASN ASN TYR VAL VAL PRO          
+SEQRES  33 A  476  VAL GLY ALA THR GLY TYR ILE ALA LYS ASP LEU TRP ASN          
+SEQRES  34 A  476  LYS VAL ASN GLU GLU PHE GLU THR TYR TYR PRO GLY ALA          
+SEQRES  35 A  476  ASP ALA ARG MSE LYS LYS LEU PHE GLY GLU LEU ASN ASN          
+SEQRES  36 A  476  GLU ALA LEU SER ILE GLU GLU LEU ILE ASN THR ILE ILE          
+SEQRES  37 A  476  GLU PHE VAL GLU ILE LEU SER ASN                              
+SEQRES   1 B  476  GLY HIS MSE ASN PRO ILE VAL GLU LEU PHE ILE LYS ASP          
+SEQRES   2 B  476  PHE THR LYS GLU VAL MSE GLU GLU ASN ALA ALA ILE PHE          
+SEQRES   3 B  476  ALA GLY ALA GLY LEU SER MSE SER VAL GLY TYR VAL SER          
+SEQRES   4 B  476  TRP ALA LYS LEU LEU GLU PRO ILE ALA GLN GLU ILE GLY          
+SEQRES   5 B  476  LEU ASP VAL ASN LYS GLU ASN ASP LEU VAL SER LEU ALA          
+SEQRES   6 B  476  GLN TYR TYR CYS ASN GLU ASN GLN GLY ASN ARG GLY ARG          
+SEQRES   7 B  476  ILE ASN GLN ILE ILE LEU ASP GLU PHE SER ARG LYS VAL          
+SEQRES   8 B  476  ASP LEU THR GLU ASN HIS LYS ILE LEU ALA ARG LEU PRO          
+SEQRES   9 B  476  ILE HIS THR TYR TRP THR THR ASN TYR ASP ARG LEU ILE          
+SEQRES  10 B  476  GLU LYS ALA LEU GLU GLU GLU ASN LYS ILE ALA ASP VAL          
+SEQRES  11 B  476  LYS TYR THR VAL LYS GLN LEU ALA THR THR LYS VAL LYS          
+SEQRES  12 B  476  ARG ASP ALA VAL VAL TYR LYS MSE HIS GLY ASP VAL GLU          
+SEQRES  13 B  476  HIS PRO SER GLU ALA VAL LEU ILE LYS ASP ASP TYR GLU          
+SEQRES  14 B  476  LYS TYR SER ILE LYS MSE ASP PRO TYR ILE LYS ALA LEU          
+SEQRES  15 B  476  SER GLY ASP LEU VAL SER LYS THR PHE LEU PHE VAL GLY          
+SEQRES  16 B  476  PHE SER PHE THR ASP PRO ASN LEU ASP TYR ILE LEU SER          
+SEQRES  17 B  476  ARG VAL ARG SER ALA TYR GLU ARG ASP GLN ARG ARG HIS          
+SEQRES  18 B  476  TYR CYS LEU ILE LYS LYS GLU GLU ARG ARG PRO ASP GLU          
+SEQRES  19 B  476  LEU GLU ALA ASP PHE GLU TYR ARG VAL ARG LYS GLN GLU          
+SEQRES  20 B  476  LEU PHE ILE SER ASP LEU SER ARG PHE ASN ILE LYS THR          
+SEQRES  21 B  476  ILE VAL LEU ASN ASN TYR ASN GLU ILE THR GLU ILE LEU          
+SEQRES  22 B  476  GLN ARG ILE GLU ASN ASN ILE LYS THR LYS THR VAL PHE          
+SEQRES  23 B  476  LEU SER GLY SER ALA VAL GLU TYR ASN HIS TRP GLU THR          
+SEQRES  24 B  476  GLU HIS ALA GLU GLN PHE ILE HIS GLN LEU SER LYS GLU          
+SEQRES  25 B  476  LEU ILE ARG LYS ASP PHE ASN ILE VAL SER GLY PHE GLY          
+SEQRES  26 B  476  LEU GLY VAL GLY SER PHE VAL ILE ASN GLY VAL LEU GLU          
+SEQRES  27 B  476  GLU LEU TYR MSE ASN GLN GLY THR ILE ASP ASP ASP ARG          
+SEQRES  28 B  476  LEU ILE LEU ARG PRO PHE PRO GLN GLY LYS LYS GLY GLU          
+SEQRES  29 B  476  GLU GLN TRP ASP LYS TYR ARG ARG ASP MSE ILE THR ARG          
+SEQRES  30 B  476  THR GLY VAL SER ILE PHE LEU TYR GLY ASN LYS ILE ASP          
+SEQRES  31 B  476  LYS GLY GLN VAL VAL LYS ALA LYS GLY VAL GLN SER GLU          
+SEQRES  32 B  476  PHE ASN ILE SER PHE GLU GLN ASN ASN TYR VAL VAL PRO          
+SEQRES  33 B  476  VAL GLY ALA THR GLY TYR ILE ALA LYS ASP LEU TRP ASN          
+SEQRES  34 B  476  LYS VAL ASN GLU GLU PHE GLU THR TYR TYR PRO GLY ALA          
+SEQRES  35 B  476  ASP ALA ARG MSE LYS LYS LEU PHE GLY GLU LEU ASN ASN          
+SEQRES  36 B  476  GLU ALA LEU SER ILE GLU GLU LEU ILE ASN THR ILE ILE          
+SEQRES  37 B  476  GLU PHE VAL GLU ILE LEU SER ASN                              
+SEQRES   1 C  476  GLY HIS MSE ASN PRO ILE VAL GLU LEU PHE ILE LYS ASP          
+SEQRES   2 C  476  PHE THR LYS GLU VAL MSE GLU GLU ASN ALA ALA ILE PHE          
+SEQRES   3 C  476  ALA GLY ALA GLY LEU SER MSE SER VAL GLY TYR VAL SER          
+SEQRES   4 C  476  TRP ALA LYS LEU LEU GLU PRO ILE ALA GLN GLU ILE GLY          
+SEQRES   5 C  476  LEU ASP VAL ASN LYS GLU ASN ASP LEU VAL SER LEU ALA          
+SEQRES   6 C  476  GLN TYR TYR CYS ASN GLU ASN GLN GLY ASN ARG GLY ARG          
+SEQRES   7 C  476  ILE ASN GLN ILE ILE LEU ASP GLU PHE SER ARG LYS VAL          
+SEQRES   8 C  476  ASP LEU THR GLU ASN HIS LYS ILE LEU ALA ARG LEU PRO          
+SEQRES   9 C  476  ILE HIS THR TYR TRP THR THR ASN TYR ASP ARG LEU ILE          
+SEQRES  10 C  476  GLU LYS ALA LEU GLU GLU GLU ASN LYS ILE ALA ASP VAL          
+SEQRES  11 C  476  LYS TYR THR VAL LYS GLN LEU ALA THR THR LYS VAL LYS          
+SEQRES  12 C  476  ARG ASP ALA VAL VAL TYR LYS MSE HIS GLY ASP VAL GLU          
+SEQRES  13 C  476  HIS PRO SER GLU ALA VAL LEU ILE LYS ASP ASP TYR GLU          
+SEQRES  14 C  476  LYS TYR SER ILE LYS MSE ASP PRO TYR ILE LYS ALA LEU          
+SEQRES  15 C  476  SER GLY ASP LEU VAL SER LYS THR PHE LEU PHE VAL GLY          
+SEQRES  16 C  476  PHE SER PHE THR ASP PRO ASN LEU ASP TYR ILE LEU SER          
+SEQRES  17 C  476  ARG VAL ARG SER ALA TYR GLU ARG ASP GLN ARG ARG HIS          
+SEQRES  18 C  476  TYR CYS LEU ILE LYS LYS GLU GLU ARG ARG PRO ASP GLU          
+SEQRES  19 C  476  LEU GLU ALA ASP PHE GLU TYR ARG VAL ARG LYS GLN GLU          
+SEQRES  20 C  476  LEU PHE ILE SER ASP LEU SER ARG PHE ASN ILE LYS THR          
+SEQRES  21 C  476  ILE VAL LEU ASN ASN TYR ASN GLU ILE THR GLU ILE LEU          
+SEQRES  22 C  476  GLN ARG ILE GLU ASN ASN ILE LYS THR LYS THR VAL PHE          
+SEQRES  23 C  476  LEU SER GLY SER ALA VAL GLU TYR ASN HIS TRP GLU THR          
+SEQRES  24 C  476  GLU HIS ALA GLU GLN PHE ILE HIS GLN LEU SER LYS GLU          
+SEQRES  25 C  476  LEU ILE ARG LYS ASP PHE ASN ILE VAL SER GLY PHE GLY          
+SEQRES  26 C  476  LEU GLY VAL GLY SER PHE VAL ILE ASN GLY VAL LEU GLU          
+SEQRES  27 C  476  GLU LEU TYR MSE ASN GLN GLY THR ILE ASP ASP ASP ARG          
+SEQRES  28 C  476  LEU ILE LEU ARG PRO PHE PRO GLN GLY LYS LYS GLY GLU          
+SEQRES  29 C  476  GLU GLN TRP ASP LYS TYR ARG ARG ASP MSE ILE THR ARG          
+SEQRES  30 C  476  THR GLY VAL SER ILE PHE LEU TYR GLY ASN LYS ILE ASP          
+SEQRES  31 C  476  LYS GLY GLN VAL VAL LYS ALA LYS GLY VAL GLN SER GLU          
+SEQRES  32 C  476  PHE ASN ILE SER PHE GLU GLN ASN ASN TYR VAL VAL PRO          
+SEQRES  33 C  476  VAL GLY ALA THR GLY TYR ILE ALA LYS ASP LEU TRP ASN          
+SEQRES  34 C  476  LYS VAL ASN GLU GLU PHE GLU THR TYR TYR PRO GLY ALA          
+SEQRES  35 C  476  ASP ALA ARG MSE LYS LYS LEU PHE GLY GLU LEU ASN ASN          
+SEQRES  36 C  476  GLU ALA LEU SER ILE GLU GLU LEU ILE ASN THR ILE ILE          
+SEQRES  37 C  476  GLU PHE VAL GLU ILE LEU SER ASN                              
+SEQRES   1 D  476  GLY HIS MSE ASN PRO ILE VAL GLU LEU PHE ILE LYS ASP          
+SEQRES   2 D  476  PHE THR LYS GLU VAL MSE GLU GLU ASN ALA ALA ILE PHE          
+SEQRES   3 D  476  ALA GLY ALA GLY LEU SER MSE SER VAL GLY TYR VAL SER          
+SEQRES   4 D  476  TRP ALA LYS LEU LEU GLU PRO ILE ALA GLN GLU ILE GLY          
+SEQRES   5 D  476  LEU ASP VAL ASN LYS GLU ASN ASP LEU VAL SER LEU ALA          
+SEQRES   6 D  476  GLN TYR TYR CYS ASN GLU ASN GLN GLY ASN ARG GLY ARG          
+SEQRES   7 D  476  ILE ASN GLN ILE ILE LEU ASP GLU PHE SER ARG LYS VAL          
+SEQRES   8 D  476  ASP LEU THR GLU ASN HIS LYS ILE LEU ALA ARG LEU PRO          
+SEQRES   9 D  476  ILE HIS THR TYR TRP THR THR ASN TYR ASP ARG LEU ILE          
+SEQRES  10 D  476  GLU LYS ALA LEU GLU GLU GLU ASN LYS ILE ALA ASP VAL          
+SEQRES  11 D  476  LYS TYR THR VAL LYS GLN LEU ALA THR THR LYS VAL LYS          
+SEQRES  12 D  476  ARG ASP ALA VAL VAL TYR LYS MSE HIS GLY ASP VAL GLU          
+SEQRES  13 D  476  HIS PRO SER GLU ALA VAL LEU ILE LYS ASP ASP TYR GLU          
+SEQRES  14 D  476  LYS TYR SER ILE LYS MSE ASP PRO TYR ILE LYS ALA LEU          
+SEQRES  15 D  476  SER GLY ASP LEU VAL SER LYS THR PHE LEU PHE VAL GLY          
+SEQRES  16 D  476  PHE SER PHE THR ASP PRO ASN LEU ASP TYR ILE LEU SER          
+SEQRES  17 D  476  ARG VAL ARG SER ALA TYR GLU ARG ASP GLN ARG ARG HIS          
+SEQRES  18 D  476  TYR CYS LEU ILE LYS LYS GLU GLU ARG ARG PRO ASP GLU          
+SEQRES  19 D  476  LEU GLU ALA ASP PHE GLU TYR ARG VAL ARG LYS GLN GLU          
+SEQRES  20 D  476  LEU PHE ILE SER ASP LEU SER ARG PHE ASN ILE LYS THR          
+SEQRES  21 D  476  ILE VAL LEU ASN ASN TYR ASN GLU ILE THR GLU ILE LEU          
+SEQRES  22 D  476  GLN ARG ILE GLU ASN ASN ILE LYS THR LYS THR VAL PHE          
+SEQRES  23 D  476  LEU SER GLY SER ALA VAL GLU TYR ASN HIS TRP GLU THR          
+SEQRES  24 D  476  GLU HIS ALA GLU GLN PHE ILE HIS GLN LEU SER LYS GLU          
+SEQRES  25 D  476  LEU ILE ARG LYS ASP PHE ASN ILE VAL SER GLY PHE GLY          
+SEQRES  26 D  476  LEU GLY VAL GLY SER PHE VAL ILE ASN GLY VAL LEU GLU          
+SEQRES  27 D  476  GLU LEU TYR MSE ASN GLN GLY THR ILE ASP ASP ASP ARG          
+SEQRES  28 D  476  LEU ILE LEU ARG PRO PHE PRO GLN GLY LYS LYS GLY GLU          
+SEQRES  29 D  476  GLU GLN TRP ASP LYS TYR ARG ARG ASP MSE ILE THR ARG          
+SEQRES  30 D  476  THR GLY VAL SER ILE PHE LEU TYR GLY ASN LYS ILE ASP          
+SEQRES  31 D  476  LYS GLY GLN VAL VAL LYS ALA LYS GLY VAL GLN SER GLU          
+SEQRES  32 D  476  PHE ASN ILE SER PHE GLU GLN ASN ASN TYR VAL VAL PRO          
+SEQRES  33 D  476  VAL GLY ALA THR GLY TYR ILE ALA LYS ASP LEU TRP ASN          
+SEQRES  34 D  476  LYS VAL ASN GLU GLU PHE GLU THR TYR TYR PRO GLY ALA          
+SEQRES  35 D  476  ASP ALA ARG MSE LYS LYS LEU PHE GLY GLU LEU ASN ASN          
+SEQRES  36 D  476  GLU ALA LEU SER ILE GLU GLU LEU ILE ASN THR ILE ILE          
+SEQRES  37 D  476  GLU PHE VAL GLU ILE LEU SER ASN                              
+MODRES 6LHX MSE A    3  MET  MODIFIED RESIDUE                                   
+MODRES 6LHX MSE A   19  MET  MODIFIED RESIDUE                                   
+MODRES 6LHX MSE A   33  MET  MODIFIED RESIDUE                                   
+MODRES 6LHX MSE A  151  MET  MODIFIED RESIDUE                                   
+MODRES 6LHX MSE A  175  MET  MODIFIED RESIDUE                                   
+MODRES 6LHX MSE A  342  MET  MODIFIED RESIDUE                                   
+MODRES 6LHX MSE A  374  MET  MODIFIED RESIDUE                                   
+MODRES 6LHX MSE A  446  MET  MODIFIED RESIDUE                                   
+MODRES 6LHX MSE B    3  MET  MODIFIED RESIDUE                                   
+MODRES 6LHX MSE B   19  MET  MODIFIED RESIDUE                                   
+MODRES 6LHX MSE B   33  MET  MODIFIED RESIDUE                                   
+MODRES 6LHX MSE B  151  MET  MODIFIED RESIDUE                                   
+MODRES 6LHX MSE B  175  MET  MODIFIED RESIDUE                                   
+MODRES 6LHX MSE B  342  MET  MODIFIED RESIDUE                                   
+MODRES 6LHX MSE B  374  MET  MODIFIED RESIDUE                                   
+MODRES 6LHX MSE B  446  MET  MODIFIED RESIDUE                                   
+MODRES 6LHX MSE C    3  MET  MODIFIED RESIDUE                                   
+MODRES 6LHX MSE C   19  MET  MODIFIED RESIDUE                                   
+MODRES 6LHX MSE C   33  MET  MODIFIED RESIDUE                                   
+MODRES 6LHX MSE C  151  MET  MODIFIED RESIDUE                                   
+MODRES 6LHX MSE C  175  MET  MODIFIED RESIDUE                                   
+MODRES 6LHX MSE C  342  MET  MODIFIED RESIDUE                                   
+MODRES 6LHX MSE C  374  MET  MODIFIED RESIDUE                                   
+MODRES 6LHX MSE C  446  MET  MODIFIED RESIDUE                                   
+MODRES 6LHX MSE D    3  MET  MODIFIED RESIDUE                                   
+MODRES 6LHX MSE D   19  MET  MODIFIED RESIDUE                                   
+MODRES 6LHX MSE D   33  MET  MODIFIED RESIDUE                                   
+MODRES 6LHX MSE D  151  MET  MODIFIED RESIDUE                                   
+MODRES 6LHX MSE D  175  MET  MODIFIED RESIDUE                                   
+MODRES 6LHX MSE D  374  MET  MODIFIED RESIDUE                                   
+MODRES 6LHX MSE D  446  MET  MODIFIED RESIDUE                                   
+HET    MSE  A   3       8                                                       
+HET    MSE  A  19       8                                                       
+HET    MSE  A  33       8                                                       
+HET    MSE  A 151       8                                                       
+HET    MSE  A 175       8                                                       
+HET    MSE  A 342       5                                                       
+HET    MSE  A 374       8                                                       
+HET    MSE  A 446       8                                                       
+HET    MSE  B   3       8                                                       
+HET    MSE  B  19       8                                                       
+HET    MSE  B  33       8                                                       
+HET    MSE  B 151       8                                                       
+HET    MSE  B 175       8                                                       
+HET    MSE  B 342       8                                                       
+HET    MSE  B 374       8                                                       
+HET    MSE  B 446       8                                                       
+HET    MSE  C   3       8                                                       
+HET    MSE  C  19       8                                                       
+HET    MSE  C  33       8                                                       
+HET    MSE  C 151       8                                                       
+HET    MSE  C 175       8                                                       
+HET    MSE  C 342       5                                                       
+HET    MSE  C 374       8                                                       
+HET    MSE  C 446       8                                                       
+HET    MSE  D   3       8                                                       
+HET    MSE  D  19       8                                                       
+HET    MSE  D  33       8                                                       
+HET    MSE  D 151       8                                                       
+HET    MSE  D 175       8                                                       
+HET    MSE  D 374       8                                                       
+HET    MSE  D 446       8                                                       
+HETNAM     MSE SELENOMETHIONINE                                                 
+FORMUL   1  MSE    31(C5 H11 N O2 SE)                                           
+FORMUL   5  HOH   *36(H2 O)                                                     
+HELIX    1 AA1 ASN A    4  GLU A   20  1                                  17    
+HELIX    2 AA2 ALA A   29  MSE A   33  5                                   5    
+HELIX    3 AA3 SER A   39  LEU A   44  1                                   6    
+HELIX    4 AA4 ASP A   60  CYS A   69  1                                  10    
+HELIX    5 AA5 ASN A   72  VAL A   91  1                                  20    
+HELIX    6 AA6 THR A   94  LEU A  103  1                                  10    
+HELIX    7 AA7 ARG A  115  GLU A  124  1                                  10    
+HELIX    8 AA8 VAL A  134  THR A  139  5                                   6    
+HELIX    9 AA9 HIS A  157  ALA A  161  5                                   5    
+HELIX   10 AB1 LYS A  165  TYR A  171  1                                   7    
+HELIX   11 AB2 TYR A  171  LYS A  189  1                                  19    
+HELIX   12 AB3 ASN A  202  ARG A  211  1                                  10    
+HELIX   13 AB4 LEU A  235  PHE A  256  1                                  22    
+HELIX   14 AB5 TYR A  266  THR A  282  1                                  17    
+HELIX   15 AB6 GLU A  298  ARG A  315  1                                  18    
+HELIX   16 AB7 VAL A  328  TYR A  341  1                                  14    
+HELIX   17 AB8 GLY A  360  GLN A  366  1                                   7    
+HELIX   18 AB9 GLN A  366  ARG A  377  1                                  12    
+HELIX   19 AC1 ALA A  397  GLN A  410  1                                  14    
+HELIX   20 AC2 ALA A  424  GLU A  433  1                                  10    
+HELIX   21 AC3 GLU A  434  TYR A  438  5                                   5    
+HELIX   22 AC4 MSE A  446  GLU A  452  1                                   7    
+HELIX   23 AC5 SER A  459  SER A  475  1                                  17    
+HELIX   24 AC6 ASN B    4  GLU B   20  1                                  17    
+HELIX   25 AC7 ALA B   29  MSE B   33  5                                   5    
+HELIX   26 AC8 ASP B   85  VAL B   91  1                                   7    
+HELIX   27 AC9 THR B   94  LEU B  103  1                                  10    
+HELIX   28 AD1 ARG B  115  GLU B  124  1                                  10    
+HELIX   29 AD2 VAL B  134  THR B  139  5                                   6    
+HELIX   30 AD3 MSE B  175  LYS B  189  1                                  15    
+HELIX   31 AD4 ASN B  202  ARG B  211  1                                  10    
+HELIX   32 AD5 LEU B  235  PHE B  256  1                                  22    
+HELIX   33 AD6 TYR B  266  THR B  282  1                                  17    
+HELIX   34 AD7 GLU B  298  LYS B  316  1                                  19    
+HELIX   35 AD8 VAL B  328  TYR B  341  1                                  14    
+HELIX   36 AD9 GLY B  360  GLU B  365  1                                   6    
+HELIX   37 AE1 GLN B  366  ARG B  377  1                                  12    
+HELIX   38 AE2 ALA B  397  GLN B  410  1                                  14    
+HELIX   39 AE3 ALA B  424  GLU B  434  1                                  11    
+HELIX   40 AE4 PHE B  435  TYR B  438  5                                   4    
+HELIX   41 AE5 LYS B  447  LEU B  453  1                                   7    
+HELIX   42 AE6 SER B  459  SER B  475  1                                  17    
+HELIX   43 AE7 ASN C    4  GLU C   20  1                                  17    
+HELIX   44 AE8 ALA C   29  MSE C   33  5                                   5    
+HELIX   45 AE9 SER C   39  GLN C   49  1                                  11    
+HELIX   46 AF1 ASP C   60  CYS C   69  1                                  10    
+HELIX   47 AF2 ASN C   72  VAL C   91  1                                  20    
+HELIX   48 AF3 THR C   94  LEU C  103  1                                  10    
+HELIX   49 AF4 ARG C  115  GLU C  124  1                                  10    
+HELIX   50 AF5 VAL C  134  THR C  139  5                                   6    
+HELIX   51 AF6 HIS C  157  ALA C  161  5                                   5    
+HELIX   52 AF7 LYS C  165  TYR C  171  1                                   7    
+HELIX   53 AF8 TYR C  171  LYS C  189  1                                  19    
+HELIX   54 AF9 ASN C  202  ARG C  211  1                                  10    
+HELIX   55 AG1 LEU C  235  ARG C  255  1                                  21    
+HELIX   56 AG2 TYR C  266  THR C  282  1                                  17    
+HELIX   57 AG3 GLU C  298  ARG C  315  1                                  18    
+HELIX   58 AG4 VAL C  328  TYR C  341  1                                  14    
+HELIX   59 AG5 GLY C  360  GLU C  365  1                                   6    
+HELIX   60 AG6 GLN C  366  ARG C  377  1                                  12    
+HELIX   61 AG7 ALA C  397  GLN C  410  1                                  14    
+HELIX   62 AG8 TYR C  422  GLU C  433  1                                  12    
+HELIX   63 AG9 GLU C  434  TYR C  438  5                                   5    
+HELIX   64 AH1 LYS C  447  GLU C  452  1                                   6    
+HELIX   65 AH2 ILE C  460  SER C  475  1                                  16    
+HELIX   66 AH3 ASN D    4  GLU D   20  1                                  17    
+HELIX   67 AH4 ALA D   29  MSE D   33  5                                   5    
+HELIX   68 AH5 ILE D   83  ARG D   89  1                                   7    
+HELIX   69 AH6 THR D   94  LEU D  103  1                                  10    
+HELIX   70 AH7 ARG D  115  GLU D  124  1                                  10    
+HELIX   71 AH8 VAL D  134  THR D  139  5                                   6    
+HELIX   72 AH9 MSE D  175  LYS D  189  1                                  15    
+HELIX   73 AI1 ASN D  202  ARG D  211  1                                  10    
+HELIX   74 AI2 LEU D  235  PHE D  256  1                                  22    
+HELIX   75 AI3 TYR D  266  THR D  282  1                                  17    
+HELIX   76 AI4 GLU D  298  LYS D  316  1                                  19    
+HELIX   77 AI5 VAL D  328  LEU D  340  1                                  13    
+HELIX   78 AI6 GLY D  360  GLU D  365  1                                   6    
+HELIX   79 AI7 GLN D  366  ARG D  377  1                                  12    
+HELIX   80 AI8 ALA D  397  GLN D  410  1                                  14    
+HELIX   81 AI9 TYR D  422  GLU D  433  1                                  12    
+HELIX   82 AJ1 GLU D  434  TYR D  438  5                                   5    
+HELIX   83 AJ2 LYS D  447  GLU D  452  1                                   6    
+HELIX   84 AJ3 SER D  459  SER D  475  1                                  17    
+SHEET    1 AA1 7 ALA A 128  LYS A 131  0                                        
+SHEET    2 AA1 7 ALA A 146  LYS A 150  1  O  LYS A 150   N  LYS A 131           
+SHEET    3 AA1 7 THR A 107  THR A 110  1  N  TYR A 108   O  VAL A 147           
+SHEET    4 AA1 7 ALA A  23  ALA A  27  1  N  ILE A  25   O  TRP A 109           
+SHEET    5 AA1 7 THR A 190  VAL A 194  1  O  LEU A 192   N  PHE A  26           
+SHEET    6 AA1 7 HIS A 221  LYS A 226  1  O  TYR A 222   N  PHE A 193           
+SHEET    7 AA1 7 ILE A 258  LEU A 263  1  O  LEU A 263   N  ILE A 225           
+SHEET    1 AA2 5 LEU A 352  LEU A 354  0                                        
+SHEET    2 AA2 5 ASN A 319  SER A 322  1  N  SER A 322   O  ILE A 353           
+SHEET    3 AA2 5 THR A 284  SER A 288  1  N  VAL A 285   O  ASN A 319           
+SHEET    4 AA2 5 VAL A 380  PHE A 383  1  O  ILE A 382   N  SER A 288           
+SHEET    5 AA2 5 TYR A 413  PRO A 416  1  O  VAL A 415   N  SER A 381           
+SHEET    1 AA3 2 ASN A 387  LYS A 388  0                                        
+SHEET    2 AA3 2 VAL A 395  LYS A 396 -1  O  VAL A 395   N  LYS A 388           
+SHEET    1 AA4 7 ALA B 128  LYS B 131  0                                        
+SHEET    2 AA4 7 ALA B 146  LYS B 150  1  O  ALA B 146   N  ASP B 129           
+SHEET    3 AA4 7 THR B 107  THR B 110  1  N  TYR B 108   O  VAL B 147           
+SHEET    4 AA4 7 ALA B  23  ALA B  27  1  N  ILE B  25   O  TRP B 109           
+SHEET    5 AA4 7 THR B 190  VAL B 194  1  O  THR B 190   N  ALA B  24           
+SHEET    6 AA4 7 HIS B 221  LYS B 226  1  O  TYR B 222   N  PHE B 193           
+SHEET    7 AA4 7 ILE B 258  LEU B 263  1  O  LEU B 263   N  ILE B 225           
+SHEET    1 AA5 5 LEU B 352  LEU B 354  0                                        
+SHEET    2 AA5 5 ASN B 319  SER B 322  1  N  SER B 322   O  ILE B 353           
+SHEET    3 AA5 5 THR B 284  SER B 288  1  N  VAL B 285   O  ASN B 319           
+SHEET    4 AA5 5 VAL B 380  PHE B 383  1  O  ILE B 382   N  SER B 288           
+SHEET    5 AA5 5 TYR B 413  PRO B 416  1  O  VAL B 415   N  SER B 381           
+SHEET    1 AA6 7 ALA C 128  LYS C 131  0                                        
+SHEET    2 AA6 7 ALA C 146  LYS C 150  1  O  LYS C 150   N  LYS C 131           
+SHEET    3 AA6 7 THR C 107  THR C 110  1  N  TYR C 108   O  VAL C 147           
+SHEET    4 AA6 7 ALA C  23  ALA C  27  1  N  ILE C  25   O  TRP C 109           
+SHEET    5 AA6 7 THR C 190  VAL C 194  1  O  THR C 190   N  ALA C  24           
+SHEET    6 AA6 7 HIS C 221  LYS C 226  1  O  TYR C 222   N  PHE C 193           
+SHEET    7 AA6 7 ILE C 258  LEU C 263  1  O  LEU C 263   N  ILE C 225           
+SHEET    1 AA7 5 LEU C 352  LEU C 354  0                                        
+SHEET    2 AA7 5 ASN C 319  SER C 322  1  N  ILE C 320   O  ILE C 353           
+SHEET    3 AA7 5 THR C 284  SER C 288  1  N  VAL C 285   O  ASN C 319           
+SHEET    4 AA7 5 VAL C 380  LEU C 384  1  O  LEU C 384   N  SER C 288           
+SHEET    5 AA7 5 TYR C 413  VAL C 417  1  O  VAL C 415   N  SER C 381           
+SHEET    1 AA8 2 ASN C 387  ILE C 389  0                                        
+SHEET    2 AA8 2 VAL C 394  LYS C 396 -1  O  VAL C 395   N  LYS C 388           
+SHEET    1 AA9 7 ALA D 128  LYS D 131  0                                        
+SHEET    2 AA9 7 ALA D 146  LYS D 150  1  O  LYS D 150   N  LYS D 131           
+SHEET    3 AA9 7 THR D 107  THR D 110  1  N  TYR D 108   O  TYR D 149           
+SHEET    4 AA9 7 ALA D  23  ALA D  27  1  N  ILE D  25   O  TRP D 109           
+SHEET    5 AA9 7 THR D 190  VAL D 194  1  O  LEU D 192   N  PHE D  26           
+SHEET    6 AA9 7 HIS D 221  LYS D 226  1  O  TYR D 222   N  PHE D 193           
+SHEET    7 AA9 7 ILE D 258  LEU D 263  1  O  LEU D 263   N  ILE D 225           
+SHEET    1 AB1 5 LEU D 352  LEU D 354  0                                        
+SHEET    2 AB1 5 ASN D 319  SER D 322  1  N  ILE D 320   O  ILE D 353           
+SHEET    3 AB1 5 THR D 284  SER D 290  1  N  VAL D 285   O  ASN D 319           
+SHEET    4 AB1 5 VAL D 380  TYR D 385  1  O  VAL D 380   N  PHE D 286           
+SHEET    5 AB1 5 TYR D 413  GLY D 421  1  O  VAL D 415   N  SER D 381           
+SHEET    1 AB2 2 ASN D 387  LYS D 388  0                                        
+SHEET    2 AB2 2 VAL D 395  LYS D 396 -1  O  VAL D 395   N  LYS D 388           
+LINK         C   HIS A   2                 N   MSE A   3     1555   1555  1.33  
+LINK         C   MSE A   3                 N   ASN A   4     1555   1555  1.33  
+LINK         C   VAL A  18                 N   MSE A  19     1555   1555  1.33  
+LINK         C   MSE A  19                 N   GLU A  20     1555   1555  1.33  
+LINK         C   SER A  32                 N   MSE A  33     1555   1555  1.33  
+LINK         C   MSE A  33                 N   SER A  34     1555   1555  1.33  
+LINK         C   LYS A 150                 N   MSE A 151     1555   1555  1.33  
+LINK         C   MSE A 151                 N   HIS A 152     1555   1555  1.33  
+LINK         C   LYS A 174                 N   MSE A 175     1555   1555  1.33  
+LINK         C   MSE A 175                 N   ASP A 176     1555   1555  1.33  
+LINK         C   TYR A 341                 N   MSE A 342     1555   1555  1.33  
+LINK         C   ASP A 373                 N   MSE A 374     1555   1555  1.33  
+LINK         C   MSE A 374                 N   ILE A 375     1555   1555  1.33  
+LINK         C   ARG A 445                 N   MSE A 446     1555   1555  1.33  
+LINK         C   MSE A 446                 N   LYS A 447     1555   1555  1.33  
+LINK         C   HIS B   2                 N   MSE B   3     1555   1555  1.33  
+LINK         C   MSE B   3                 N   ASN B   4     1555   1555  1.33  
+LINK         C   VAL B  18                 N   MSE B  19     1555   1555  1.33  
+LINK         C   MSE B  19                 N   GLU B  20     1555   1555  1.33  
+LINK         C   SER B  32                 N   MSE B  33     1555   1555  1.33  
+LINK         C   MSE B  33                 N   SER B  34     1555   1555  1.33  
+LINK         C   LYS B 150                 N   MSE B 151     1555   1555  1.33  
+LINK         C   MSE B 151                 N   HIS B 152     1555   1555  1.33  
+LINK         C   LYS B 174                 N   MSE B 175     1555   1555  1.33  
+LINK         C   MSE B 175                 N   ASP B 176     1555   1555  1.33  
+LINK         C   TYR B 341                 N   MSE B 342     1555   1555  1.33  
+LINK         C   MSE B 342                 N   ASN B 343     1555   1555  1.33  
+LINK         C   ASP B 373                 N   MSE B 374     1555   1555  1.33  
+LINK         C   MSE B 374                 N   ILE B 375     1555   1555  1.33  
+LINK         C   MSE B 446                 N   LYS B 447     1555   1555  1.33  
+LINK         C   HIS C   2                 N   MSE C   3     1555   1555  1.33  
+LINK         C   MSE C   3                 N   ASN C   4     1555   1555  1.33  
+LINK         C   VAL C  18                 N   MSE C  19     1555   1555  1.33  
+LINK         C   MSE C  19                 N   GLU C  20     1555   1555  1.33  
+LINK         C   SER C  32                 N   MSE C  33     1555   1555  1.33  
+LINK         C   MSE C  33                 N   SER C  34     1555   1555  1.33  
+LINK         C   LYS C 150                 N   MSE C 151     1555   1555  1.33  
+LINK         C   MSE C 151                 N   HIS C 152     1555   1555  1.33  
+LINK         C   LYS C 174                 N   MSE C 175     1555   1555  1.33  
+LINK         C   MSE C 175                 N   ASP C 176     1555   1555  1.33  
+LINK         C   TYR C 341                 N   MSE C 342     1555   1555  1.33  
+LINK         C   ASP C 373                 N   MSE C 374     1555   1555  1.33  
+LINK         C   MSE C 374                 N   ILE C 375     1555   1555  1.33  
+LINK         C   MSE C 446                 N   LYS C 447     1555   1555  1.33  
+LINK         C   HIS D   2                 N   MSE D   3     1555   1555  1.33  
+LINK         C   MSE D   3                 N   ASN D   4     1555   1555  1.33  
+LINK         C   VAL D  18                 N   MSE D  19     1555   1555  1.33  
+LINK         C   MSE D  19                 N   GLU D  20     1555   1555  1.33  
+LINK         C   SER D  32                 N   MSE D  33     1555   1555  1.33  
+LINK         C   MSE D  33                 N   SER D  34     1555   1555  1.33  
+LINK         C   LYS D 150                 N   MSE D 151     1555   1555  1.33  
+LINK         C   MSE D 151                 N   HIS D 152     1555   1555  1.33  
+LINK         C   LYS D 174                 N   MSE D 175     1555   1555  1.33  
+LINK         C   MSE D 175                 N   ASP D 176     1555   1555  1.33  
+LINK         C   ASP D 373                 N   MSE D 374     1555   1555  1.33  
+LINK         C   MSE D 374                 N   ILE D 375     1555   1555  1.33  
+LINK         C   MSE D 446                 N   LYS D 447     1555   1555  1.33  
+CRYST1  180.424  168.584   93.614  90.00 106.71  90.00 C 1 2 1      16          
+ORIGX1      1.000000  0.000000  0.000000        0.00000                         
+ORIGX2      0.000000  1.000000  0.000000        0.00000                         
+ORIGX3      0.000000  0.000000  1.000000        0.00000                         
+SCALE1      0.005542  0.000000  0.001664        0.00000                         
+SCALE2      0.000000  0.005932  0.000000        0.00000                         
+SCALE3      0.000000  0.000000  0.011153        0.00000                         
+ATOM      1  N   HIS A   2     -46.489   2.202 -15.549  1.00 90.41           N  
+ANISOU    1  N   HIS A   2    10657  12716  10980  -2021   -279  -1084       N  
+ATOM      2  CA  HIS A   2     -46.781   3.049 -16.700  1.00 93.90           C  
+ANISOU    2  CA  HIS A   2    11024  13163  11492  -1830   -484  -1097       C  
+ATOM      3  C   HIS A   2     -45.576   3.152 -17.630  1.00101.46           C  
+ANISOU    3  C   HIS A   2    12294  14060  12197  -1635   -570  -1017       C  
+ATOM      4  O   HIS A   2     -45.678   2.877 -18.826  1.00111.99           O  
+ANISOU    4  O   HIS A   2    13763  15332  13457  -1572   -804  -1017       O  
+ATOM      5  CB  HIS A   2     -47.213   4.444 -16.243  1.00 87.06           C  
+ANISOU    5  CB  HIS A   2     9862  12391  10827  -1745   -385  -1140       C  
+HETATM    6  N   MSE A   3     -44.436   3.548 -17.073  1.00 86.40           N  
+ANISOU    6  N   MSE A   3    10502  12171  10156  -1551   -376   -958       N  
+HETATM    7  CA  MSE A   3     -43.214   3.707 -17.854  1.00 84.09           C  
+ANISOU    7  CA  MSE A   3    10473  11840   9639  -1379   -403   -900       C  
+HETATM    8  C   MSE A   3     -42.542   2.357 -18.100  1.00 82.44           C  
+ANISOU    8  C   MSE A   3    10532  11540   9253  -1425   -442   -909       C  
+HETATM    9  O   MSE A   3     -42.963   1.340 -17.550  1.00 82.62           O  
+ANISOU    9  O   MSE A   3    10556  11518   9320  -1593   -450   -937       O  
+HETATM   10  CB  MSE A   3     -42.255   4.668 -17.147  1.00 82.82           C  
+ANISOU   10  CB  MSE A   3    10303  11727   9439  -1274   -189   -845       C  
+HETATM   11  CG  MSE A   3     -42.884   6.014 -16.809  1.00 84.37           C  
+ANISOU   11  CG  MSE A   3    10237  11999   9819  -1221   -153   -849       C  
+HETATM   12 SE   MSE A   3     -41.642   7.289 -16.011  1.00 93.47          SE  
+ANISOU   12 SE   MSE A   3    11404  13196  10915  -1079     82   -772      SE  
+HETATM   13  CE  MSE A   3     -40.643   7.781 -17.612  1.00100.65           C  
+ANISOU   13  CE  MSE A   3    12572  14071  11600   -894    -58   -699       C  
+ATOM     14  N   ASN A   4     -41.505   2.352 -18.935  1.00 80.55           N  
+ANISOU   14  N   ASN A   4    10518  11269   8818  -1282   -468   -895       N  
+ATOM     15  CA  ASN A   4     -40.802   1.122 -19.296  1.00 78.65           C  
+ANISOU   15  CA  ASN A   4    10527  10936   8423  -1288   -520   -937       C  
+ATOM     16  C   ASN A   4     -40.124   0.475 -18.085  1.00 77.18           C  
+ANISOU   16  C   ASN A   4    10389  10695   8240  -1357   -376   -935       C  
+ATOM     17  O   ASN A   4     -39.715   1.175 -17.160  1.00 78.57           O  
+ANISOU   17  O   ASN A   4    10474  10915   8464  -1339   -199   -889       O  
+ATOM     18  CB  ASN A   4     -39.779   1.403 -20.405  1.00 77.33           C  
+ANISOU   18  CB  ASN A   4    10561  10769   8052  -1119   -527   -949       C  
+ATOM     19  CG  ASN A   4     -38.636   2.283 -19.944  1.00 87.85           C  
+ANISOU   19  CG  ASN A   4    11883  12154   9342  -1005   -312   -906       C  
+ATOM     20  OD1 ASN A   4     -37.737   1.835 -19.232  1.00 97.60           O  
+ANISOU   20  OD1 ASN A   4    13175  13346  10562   -993   -191   -925       O  
+ATOM     21  ND2 ASN A   4     -38.661   3.545 -20.356  1.00 97.96           N  
+ANISOU   21  ND2 ASN A   4    13100  13509  10612   -924   -289   -849       N  
+ATOM     22  N   PRO A   5     -40.014  -0.868 -18.088  1.00 79.18           N  
+ANISOU   22  N   PRO A   5    10807  10835   8444  -1439   -480   -983       N  
+ATOM     23  CA  PRO A   5     -39.515  -1.659 -16.953  1.00 80.44           C  
+ANISOU   23  CA  PRO A   5    11054  10898   8612  -1539   -417   -979       C  
+ATOM     24  C   PRO A   5     -38.200  -1.166 -16.343  1.00 79.80           C  
+ANISOU   24  C   PRO A   5    11022  10808   8490  -1414   -252   -959       C  
+ATOM     25  O   PRO A   5     -38.034  -1.246 -15.124  1.00 86.57           O  
+ANISOU   25  O   PRO A   5    11873  11625   9394  -1513   -162   -918       O  
+ATOM     26  CB  PRO A   5     -39.324  -3.048 -17.566  1.00 75.22           C  
+ANISOU   26  CB  PRO A   5    10615  10098   7868  -1558   -612  -1055       C  
+ATOM     27  CG  PRO A   5     -40.359  -3.119 -18.621  1.00 76.01           C  
+ANISOU   27  CG  PRO A   5    10671  10232   7976  -1586   -776  -1079       C  
+ATOM     28  CD  PRO A   5     -40.434  -1.736 -19.206  1.00 76.66           C  
+ANISOU   28  CD  PRO A   5    10620  10450   8057  -1452   -701  -1046       C  
+ATOM     29  N   ILE A   6     -37.290  -0.663 -17.171  1.00 75.77           N  
+ANISOU   29  N   ILE A   6    10569  10333   7889  -1218   -215   -988       N  
+ATOM     30  CA  ILE A   6     -36.010  -0.163 -16.680  1.00 78.49           C  
+ANISOU   30  CA  ILE A   6    10935  10670   8217  -1095    -64   -981       C  
+ATOM     31  C   ILE A   6     -36.212   1.061 -15.791  1.00 68.36           C  
+ANISOU   31  C   ILE A   6     9472   9482   7021  -1113     97   -886       C  
+ATOM     32  O   ILE A   6     -35.696   1.131 -14.666  1.00 66.96           O  
+ANISOU   32  O   ILE A   6     9299   9256   6887  -1142    189   -853       O  
+ATOM     33  CB  ILE A   6     -35.065   0.201 -17.844  1.00 72.10           C  
+ANISOU   33  CB  ILE A   6    10200   9902   7291   -907    -28  -1042       C  
+ATOM     34  CG1 ILE A   6     -34.785  -1.029 -18.710  1.00 70.03           C  
+ANISOU   34  CG1 ILE A   6    10124   9546   6939   -876   -170  -1169       C  
+ATOM     35  CG2 ILE A   6     -33.766   0.787 -17.315  1.00 78.05           C  
+ANISOU   35  CG2 ILE A   6    10936  10657   8062   -790    136  -1038       C  
+ATOM     36  CD1 ILE A   6     -33.860  -0.759 -19.879  1.00 64.98           C  
+ANISOU   36  CD1 ILE A   6     9570   8957   6163   -718   -102  -1259       C  
+ATOM     37  N   VAL A   7     -36.991   2.012 -16.298  1.00 69.88           N  
+ANISOU   37  N   VAL A   7     9518   9792   7242  -1095    105   -848       N  
+ATOM     38  CA  VAL A   7     -37.301   3.229 -15.561  1.00 72.97           C  
+ANISOU   38  CA  VAL A   7     9721  10272   7731  -1097    236   -780       C  
+ATOM     39  C   VAL A   7     -38.051   2.909 -14.272  1.00 74.87           C  
+ANISOU   39  C   VAL A   7     9873  10498   8078  -1284    290   -766       C  
+ATOM     40  O   VAL A   7     -37.769   3.495 -13.231  1.00 71.34           O  
+ANISOU   40  O   VAL A   7     9368  10065   7672  -1300    434   -728       O  
+ATOM     41  CB  VAL A   7     -38.133   4.207 -16.417  1.00 72.87           C  
+ANISOU   41  CB  VAL A   7     9573  10359   7755  -1046    172   -761       C  
+ATOM     42  CG1 VAL A   7     -38.623   5.373 -15.576  1.00 74.11           C  
+ANISOU   42  CG1 VAL A   7     9514  10593   8053  -1055    282   -718       C  
+ATOM     43  CG2 VAL A   7     -37.304   4.717 -17.583  1.00 80.58           C  
+ANISOU   43  CG2 VAL A   7    10669  11356   8590   -889    153   -753       C  
+ATOM     44  N   GLU A   8     -38.982   1.963 -14.337  1.00 78.98           N  
+ANISOU   44  N   GLU A   8    10397  10984   8627  -1443    180   -801       N  
+ATOM     45  CA  GLU A   8     -39.748   1.560 -13.159  1.00 76.52           C  
+ANISOU   45  CA  GLU A   8    10017  10664   8394  -1669    248   -796       C  
+ATOM     46  C   GLU A   8     -38.846   0.953 -12.089  1.00 74.19           C  
+ANISOU   46  C   GLU A   8     9914  10249   8027  -1738    307   -767       C  
+ATOM     47  O   GLU A   8     -38.958   1.279 -10.898  1.00 74.61           O  
+ANISOU   47  O   GLU A   8     9926  10315   8106  -1854    450   -735       O  
+ATOM     48  CB  GLU A   8     -40.834   0.554 -13.548  1.00 78.21           C  
+ANISOU   48  CB  GLU A   8    10220  10848   8646  -1839    100   -839       C  
+ATOM     49  CG  GLU A   8     -41.877   1.087 -14.516  1.00 80.20           C  
+ANISOU   49  CG  GLU A   8    10274  11194   9003  -1797      0   -874       C  
+ATOM     50  CD  GLU A   8     -42.814   2.090 -13.876  1.00 81.65           C  
+ANISOU   50  CD  GLU A   8    10160  11500   9364  -1858    131   -891       C  
+ATOM     51  OE1 GLU A   8     -42.864   2.154 -12.629  1.00 87.77           O  
+ANISOU   51  OE1 GLU A   8    10887  12296  10167  -1994    314   -884       O  
+ATOM     52  OE2 GLU A   8     -43.505   2.819 -14.619  1.00 82.89           O  
+ANISOU   52  OE2 GLU A   8    10138  11723   9634  -1771     40   -922       O  
+ATOM     53  N   LEU A   9     -37.938   0.085 -12.528  1.00 71.99           N  
+ANISOU   53  N   LEU A   9     9851   9843   7658  -1661    183   -791       N  
+ATOM     54  CA  LEU A   9     -36.983  -0.550 -11.630  1.00 69.81           C  
+ANISOU   54  CA  LEU A   9     9777   9413   7334  -1697    172   -776       C  
+ATOM     55  C   LEU A   9     -36.131   0.507 -10.938  1.00 67.55           C  
+ANISOU   55  C   LEU A   9     9447   9156   7062  -1584    329   -732       C  
+ATOM     56  O   LEU A   9     -35.937   0.464  -9.714  1.00 69.83           O  
+ANISOU   56  O   LEU A   9     9812   9375   7345  -1702    389   -688       O  
+ATOM     57  CB  LEU A   9     -36.099  -1.537 -12.394  1.00 67.92           C  
+ANISOU   57  CB  LEU A   9     9735   9037   7037  -1578     -1   -847       C  
+ATOM     58  CG  LEU A   9     -35.067  -2.308 -11.570  1.00 66.15           C  
+ANISOU   58  CG  LEU A   9     9726   8610   6797  -1591    -81   -855       C  
+ATOM     59  CD1 LEU A   9     -35.731  -2.985 -10.382  1.00 67.22           C  
+ANISOU   59  CD1 LEU A   9     9973   8647   6920  -1877   -119   -792       C  
+ATOM     60  CD2 LEU A   9     -34.343  -3.327 -12.436  1.00 64.79           C  
+ANISOU   60  CD2 LEU A   9     9711   8306   6602  -1463   -268   -966       C  
+ATOM     61  N   PHE A  10     -35.633   1.459 -11.723  1.00 66.02           N  
+ANISOU   61  N   PHE A  10     9152   9058   6875  -1372    386   -739       N  
+ATOM     62  CA  PHE A  10     -34.885   2.573 -11.151  1.00 66.16           C  
+ANISOU   62  CA  PHE A  10     9107   9113   6918  -1264    528   -692       C  
+ATOM     63  C   PHE A  10     -35.712   3.346 -10.133  1.00 63.78           C  
+ANISOU   63  C   PHE A  10     8666   8894   6673  -1391    667   -643       C  
+ATOM     64  O   PHE A  10     -35.210   3.719  -9.075  1.00 60.94           O  
+ANISOU   64  O   PHE A  10     8348   8490   6315  -1413    756   -603       O  
+ATOM     65  CB  PHE A  10     -34.414   3.541 -12.230  1.00 61.38           C  
+ANISOU   65  CB  PHE A  10     8408   8611   6302  -1057    569   -697       C  
+ATOM     66  CG  PHE A  10     -34.063   4.903 -11.695  1.00 60.66           C  
+ANISOU   66  CG  PHE A  10     8201   8590   6257   -977    712   -635       C  
+ATOM     67  CD1 PHE A  10     -32.917   5.086 -10.937  1.00 55.50           C  
+ANISOU   67  CD1 PHE A  10     7619   7853   5616   -917    767   -615       C  
+ATOM     68  CD2 PHE A  10     -34.883   5.994 -11.933  1.00 59.21           C  
+ANISOU   68  CD2 PHE A  10     7837   8537   6123   -960    766   -603       C  
+ATOM     69  CE1 PHE A  10     -32.591   6.330 -10.434  1.00 52.46           C  
+ANISOU   69  CE1 PHE A  10     7137   7521   5274   -847    885   -557       C  
+ATOM     70  CE2 PHE A  10     -34.562   7.243 -11.430  1.00 58.71           C  
+ANISOU   70  CE2 PHE A  10     7677   8522   6107   -883    878   -551       C  
+ATOM     71  CZ  PHE A  10     -33.414   7.410 -10.680  1.00 55.46           C  
+ANISOU   71  CZ  PHE A  10     7347   8034   5690   -831    944   -524       C  
+ATOM     72  N   ILE A  11     -36.974   3.596 -10.469  1.00 67.13           N  
+ANISOU   72  N   ILE A  11     8920   9433   7153  -1469    679   -660       N  
+ATOM     73  CA  ILE A  11     -37.862   4.350  -9.597  1.00 71.57           C  
+ANISOU   73  CA  ILE A  11     9303  10093   7797  -1582    825   -655       C  
+ATOM     74  C   ILE A  11     -38.009   3.669  -8.248  1.00 73.55           C  
+ANISOU   74  C   ILE A  11     9677  10265   8004  -1818    896   -642       C  
+ATOM     75  O   ILE A  11     -37.936   4.321  -7.209  1.00 81.48           O  
+ANISOU   75  O   ILE A  11    10655  11290   9012  -1867   1045   -623       O  
+ATOM     76  CB  ILE A  11     -39.260   4.528 -10.229  1.00 71.56           C  
+ANISOU   76  CB  ILE A  11     9081  10207   7903  -1639    790   -708       C  
+ATOM     77  CG1 ILE A  11     -39.198   5.521 -11.389  1.00 72.19           C  
+ANISOU   77  CG1 ILE A  11     9044  10361   8024  -1418    723   -706       C  
+ATOM     78  CG2 ILE A  11     -40.264   5.018  -9.197  1.00 69.60           C  
+ANISOU   78  CG2 ILE A  11     8638  10049   7759  -1801    956   -747       C  
+ATOM     79  CD1 ILE A  11     -40.500   5.650 -12.148  1.00 77.27           C  
+ANISOU   79  CD1 ILE A  11     9494  11081   8786  -1449    619   -762       C  
+ATOM     80  N   LYS A  12     -38.168   2.352  -8.261  1.00 69.28           N  
+ANISOU   80  N   LYS A  12     9301   9619   7405  -1972    778   -650       N  
+ATOM     81  CA  LYS A  12     -38.365   1.622  -7.014  1.00 73.94           C  
+ANISOU   81  CA  LYS A  12    10054  10116   7925  -2241    822   -626       C  
+ATOM     82  C   LYS A  12     -37.066   1.555  -6.199  1.00 65.60           C  
+ANISOU   82  C   LYS A  12     9238   8901   6784  -2193    799   -570       C  
+ATOM     83  O   LYS A  12     -37.072   1.798  -4.982  1.00 67.18           O  
+ANISOU   83  O   LYS A  12     9516   9075   6933  -2341    918   -536       O  
+ATOM     84  CB  LYS A  12     -38.941   0.232  -7.316  1.00 82.21           C  
+ANISOU   84  CB  LYS A  12    11221  11078   8938  -2431    669   -642       C  
+ATOM     85  CG  LYS A  12     -38.578  -0.894  -6.366  1.00 86.14           C  
+ANISOU   85  CG  LYS A  12    12035  11378   9317  -2652    584   -595       C  
+ATOM     86  CD  LYS A  12     -39.310  -2.164  -6.804  1.00 82.60           C  
+ANISOU   86  CD  LYS A  12    11668  10862   8854  -2840    424   -614       C  
+ATOM     87  CE  LYS A  12     -38.714  -3.428  -6.211  1.00 91.05           C  
+ANISOU   87  CE  LYS A  12    13105  11681   9810  -2994    234   -569       C  
+ATOM     88  NZ  LYS A  12     -37.256  -3.535  -6.481  1.00 98.29           N  
+ANISOU   88  NZ  LYS A  12    14186  12441  10718  -2727     76   -575       N  
+ATOM     89  N   ASP A  13     -35.952   1.268  -6.869  1.00 65.46           N  
+ANISOU   89  N   ASP A  13     9332   8778   6760  -1985    649   -575       N  
+ATOM     90  CA  ASP A  13     -34.666   1.169  -6.176  1.00 71.78           C  
+ANISOU   90  CA  ASP A  13    10337   9409   7526  -1915    589   -542       C  
+ATOM     91  C   ASP A  13     -34.254   2.508  -5.547  1.00 65.93           C  
+ANISOU   91  C   ASP A  13     9495   8742   6814  -1817    755   -505       C  
+ATOM     92  O   ASP A  13     -33.879   2.574  -4.368  1.00 70.61           O  
+ANISOU   92  O   ASP A  13    10241   9232   7357  -1918    781   -460       O  
+ATOM     93  CB  ASP A  13     -33.578   0.686  -7.137  1.00 77.50           C  
+ANISOU   93  CB  ASP A  13    11133  10033   8281  -1689    421   -594       C  
+ATOM     94  CG  ASP A  13     -33.823  -0.727  -7.636  1.00 88.36           C  
+ANISOU   94  CG  ASP A  13    12658  11290   9626  -1776    222   -642       C  
+ATOM     95  OD1 ASP A  13     -34.485  -1.507  -6.920  1.00100.88           O  
+ANISOU   95  OD1 ASP A  13    14385  12791  11154  -2034    168   -607       O  
+ATOM     96  OD2 ASP A  13     -33.354  -1.056  -8.746  1.00 96.54           O  
+ANISOU   96  OD2 ASP A  13    13680  12315  10686  -1598    124   -717       O  
+ATOM     97  N   PHE A  14     -34.340   3.574  -6.336  1.00 57.08           N  
+ANISOU   97  N   PHE A  14     8138   7785   5764  -1631    849   -521       N  
+ATOM     98  CA  PHE A  14     -33.940   4.899  -5.878  1.00 54.93           C  
+ANISOU   98  CA  PHE A  14     7761   7579   5530  -1517    985   -487       C  
+ATOM     99  C   PHE A  14     -34.932   5.447  -4.860  1.00 65.68           C  
+ANISOU   99  C   PHE A  14     9040   9030   6886  -1698   1155   -483       C  
+ATOM    100  O   PHE A  14     -34.556   6.225  -3.982  1.00 56.30           O  
+ANISOU  100  O   PHE A  14     7870   7830   5691  -1684   1252   -454       O  
+ATOM    101  CB  PHE A  14     -33.790   5.867  -7.053  1.00 52.21           C  
+ANISOU  101  CB  PHE A  14     7216   7369   5253  -1289   1012   -499       C  
+ATOM    102  CG  PHE A  14     -32.962   7.079  -6.730  1.00 48.52           C  
+ANISOU  102  CG  PHE A  14     6695   6915   4825  -1137   1093   -458       C  
+ATOM    103  CD1 PHE A  14     -31.614   6.955  -6.432  1.00 52.63           C  
+ANISOU  103  CD1 PHE A  14     7352   7299   5346  -1041   1036   -440       C  
+ATOM    104  CD2 PHE A  14     -33.531   8.341  -6.722  1.00 49.33           C  
+ANISOU  104  CD2 PHE A  14     6603   7155   4985  -1086   1207   -446       C  
+ATOM    105  CE1 PHE A  14     -30.851   8.068  -6.128  1.00 49.27           C  
+ANISOU  105  CE1 PHE A  14     6872   6880   4967   -913   1102   -399       C  
+ATOM    106  CE2 PHE A  14     -32.772   9.458  -6.424  1.00 55.86           C  
+ANISOU  106  CE2 PHE A  14     7393   7982   5848   -953   1264   -403       C  
+ATOM    107  CZ  PHE A  14     -31.432   9.321  -6.123  1.00 51.25           C  
+ANISOU  107  CZ  PHE A  14     6949   7268   5254   -874   1218   -373       C  
+ATOM    108  N   THR A  15     -36.198   5.054  -4.984  1.00 58.19           N  
+ANISOU  108  N   THR A  15     7990   8173   5948  -1869   1198   -526       N  
+ATOM    109  CA  THR A  15     -37.185   5.392  -3.965  1.00 58.70           C  
+ANISOU  109  CA  THR A  15     7973   8324   6008  -2082   1384   -555       C  
+ATOM    110  C   THR A  15     -36.735   4.788  -2.647  1.00 60.78           C  
+ANISOU  110  C   THR A  15     8534   8431   6129  -2288   1397   -506       C  
+ATOM    111  O   THR A  15     -36.772   5.448  -1.607  1.00 65.12           O  
+ANISOU  111  O   THR A  15     9104   9001   6638  -2366   1551   -505       O  
+ATOM    112  CB  THR A  15     -38.591   4.879  -4.305  1.00 58.04           C  
+ANISOU  112  CB  THR A  15     7730   8347   5975  -2264   1417   -624       C  
+ATOM    113  OG1 THR A  15     -39.112   5.615  -5.418  1.00 72.53           O  
+ANISOU  113  OG1 THR A  15     9284  10320   7955  -2078   1394   -674       O  
+ATOM    114  CG2 THR A  15     -39.516   5.055  -3.115  1.00 54.99           C  
+ANISOU  114  CG2 THR A  15     7284   8039   5569  -2529   1640   -676       C  
+ATOM    115  N   LYS A  16     -36.310   3.528  -2.699  1.00 54.73           N  
+ANISOU  115  N   LYS A  16     8018   7494   5282  -2378   1215   -471       N  
+ATOM    116  CA  LYS A  16     -35.782   2.874  -1.508  1.00 58.42           C  
+ANISOU  116  CA  LYS A  16     8824   7764   5609  -2571   1157   -412       C  
+ATOM    117  C   LYS A  16     -34.598   3.652  -0.939  1.00 55.97           C  
+ANISOU  117  C   LYS A  16     8608   7361   5297  -2401   1143   -368       C  
+ATOM    118  O   LYS A  16     -34.528   3.890   0.267  1.00 62.87           O  
+ANISOU  118  O   LYS A  16     9646   8174   6068  -2556   1225   -335       O  
+ATOM    119  CB  LYS A  16     -35.362   1.437  -1.815  1.00 69.53           C  
+ANISOU  119  CB  LYS A  16    10483   8968   6967  -2633    897   -388       C  
+ATOM    120  CG  LYS A  16     -34.737   0.721  -0.631  1.00 85.57           C  
+ANISOU  120  CG  LYS A  16    12904  10748   8859  -2823    767   -319       C  
+ATOM    121  CD  LYS A  16     -34.348  -0.703  -0.980  1.00 98.68           C  
+ANISOU  121  CD  LYS A  16    14808  12188  10499  -2868    471   -310       C  
+ATOM    122  CE  LYS A  16     -33.557  -1.345   0.148  1.00103.15           C  
+ANISOU  122  CE  LYS A  16    15783  12459  10951  -3013    274   -239       C  
+ATOM    123  NZ  LYS A  16     -32.278  -0.626   0.406  1.00103.19           N  
+ANISOU  123  NZ  LYS A  16    15811  12366  11030  -2758    208   -231       N  
+ATOM    124  N   GLU A  17     -33.669   4.049  -1.805  1.00 52.40           N  
+ANISOU  124  N   GLU A  17     8060   6897   4952  -2098   1045   -372       N  
+ATOM    125  CA  GLU A  17     -32.492   4.786  -1.344  1.00 52.39           C  
+ANISOU  125  CA  GLU A  17     8123   6804   4980  -1930   1018   -335       C  
+ATOM    126  C   GLU A  17     -32.808   6.193  -0.828  1.00 51.68           C  
+ANISOU  126  C   GLU A  17     7866   6860   4910  -1893   1233   -333       C  
+ATOM    127  O   GLU A  17     -32.194   6.657   0.133  1.00 62.97           O  
+ANISOU  127  O   GLU A  17     9434   8192   6299  -1900   1243   -294       O  
+ATOM    128  CB  GLU A  17     -31.445   4.865  -2.455  1.00 63.56           C  
+ANISOU  128  CB  GLU A  17     9449   8189   6512  -1638    891   -356       C  
+ATOM    129  CG  GLU A  17     -30.829   3.521  -2.793  1.00 67.36           C  
+ANISOU  129  CG  GLU A  17    10122   8477   6993  -1635    654   -382       C  
+ATOM    130  CD  GLU A  17     -30.093   2.911  -1.614  1.00 78.03           C  
+ANISOU  130  CD  GLU A  17    11790   9563   8293  -1746    486   -341       C  
+ATOM    131  OE1 GLU A  17     -29.473   3.669  -0.837  1.00 88.24           O  
+ANISOU  131  OE1 GLU A  17    13129  10801   9597  -1700    515   -301       O  
+ATOM    132  OE2 GLU A  17     -30.139   1.673  -1.460  1.00 87.22           O  
+ANISOU  132  OE2 GLU A  17    13177  10558   9406  -1885    301   -346       O  
+ATOM    133  N   VAL A  18     -33.761   6.870  -1.462  1.00 54.74           N  
+ANISOU  133  N   VAL A  18     7965   7464   5370  -1848   1379   -383       N  
+ATOM    134  CA  VAL A  18     -34.156   8.211  -1.034  1.00 48.02           C  
+ANISOU  134  CA  VAL A  18     6933   6749   4564  -1800   1565   -407       C  
+ATOM    135  C   VAL A  18     -34.867   8.180   0.316  1.00 56.00           C  
+ANISOU  135  C   VAL A  18     8050   7767   5462  -2073   1730   -432       C  
+ATOM    136  O   VAL A  18     -34.612   9.013   1.186  1.00 55.50           O  
+ANISOU  136  O   VAL A  18     8026   7692   5369  -2064   1828   -428       O  
+ATOM    137  CB  VAL A  18     -35.074   8.889  -2.078  1.00 56.06           C  
+ANISOU  137  CB  VAL A  18     7617   7973   5712  -1685   1636   -469       C  
+ATOM    138  CG1 VAL A  18     -35.819  10.072  -1.465  1.00 47.59           C  
+ANISOU  138  CG1 VAL A  18     6354   7033   4697  -1698   1830   -532       C  
+ATOM    139  CG2 VAL A  18     -34.266   9.331  -3.288  1.00 43.93           C  
+ANISOU  139  CG2 VAL A  18     5993   6442   4257  -1411   1516   -436       C  
+HETATM  140  N   MSE A  19     -35.753   7.205   0.484  1.00 73.98           N  
+ANISOU  140  N   MSE A  19    10385  10060   7665  -2330   1765   -462       N  
+HETATM  141  CA  MSE A  19     -36.560   7.094   1.691  1.00 66.58           C  
+ANISOU  141  CA  MSE A  19     9541   9156   6602  -2640   1961   -503       C  
+HETATM  142  C   MSE A  19     -35.709   6.808   2.923  1.00 74.15           C  
+ANISOU  142  C   MSE A  19    10892   9906   7377  -2777   1904   -423       C  
+HETATM  143  O   MSE A  19     -36.077   7.174   4.041  1.00 78.61           O  
+ANISOU  143  O   MSE A  19    11553  10495   7822  -2971   2089   -453       O  
+HETATM  144  CB  MSE A  19     -37.613   6.003   1.520  1.00 70.40           C  
+ANISOU  144  CB  MSE A  19    10017   9687   7046  -2908   1989   -541       C  
+HETATM  145  CG  MSE A  19     -38.749   6.068   2.518  1.00 72.98           C  
+ANISOU  145  CG  MSE A  19    10309  10131   7287  -3232   2267   -628       C  
+HETATM  146 SE   MSE A  19     -40.325   5.191   1.800  1.00141.44          SE  
+ANISOU  146 SE   MSE A  19    18727  18962  16052  -3459   2338   -725      SE  
+HETATM  147  CE  MSE A  19     -39.516   3.473   1.358  1.00 91.24           C  
+ANISOU  147  CE  MSE A  19    12768  12334   9566  -3535   1979   -577       C  
+ATOM    148  N   GLU A  20     -34.569   6.157   2.714  1.00 68.94           N  
+ANISOU  148  N   GLU A  20    10461   9032   6701  -2676   1639   -335       N  
+ATOM    149  CA  GLU A  20     -33.668   5.849   3.810  1.00 60.70           C  
+ANISOU  149  CA  GLU A  20     9803   7746   5513  -2780   1511   -256       C  
+ATOM    150  C   GLU A  20     -32.794   7.063   4.105  1.00 60.11           C  
+ANISOU  150  C   GLU A  20     9682   7650   5507  -2545   1521   -239       C  
+ATOM    151  O   GLU A  20     -31.895   7.015   4.947  1.00 67.91           O  
+ANISOU  151  O   GLU A  20    10960   8428   6414  -2569   1386   -175       O  
+ATOM    152  CB  GLU A  20     -32.808   4.624   3.481  1.00 58.29           C  
+ANISOU  152  CB  GLU A  20     9745   7197   5205  -2757   1189   -194       C  
+ATOM    153  CG  GLU A  20     -33.497   3.285   3.731  1.00 61.72           C  
+ANISOU  153  CG  GLU A  20    10405   7548   5496  -3085   1127   -176       C  
+ATOM    154  CD  GLU A  20     -33.851   3.070   5.192  1.00 78.21           C  
+ANISOU  154  CD  GLU A  20    12832   9543   7340  -3453   1216   -134       C  
+ATOM    155  OE1 GLU A  20     -34.863   2.392   5.467  1.00 89.04           O  
+ANISOU  155  OE1 GLU A  20    14279  10969   8582  -3779   1327   -145       O  
+ATOM    156  OE2 GLU A  20     -33.135   3.603   6.067  1.00 84.86           O  
+ANISOU  156  OE2 GLU A  20    13870  10262   8112  -3433   1185    -92       O  
+ATOM    157  N   GLU A  21     -33.073   8.145   3.385  1.00 53.41           N  
+ANISOU  157  N   GLU A  21     8475   7005   4813  -2323   1655   -294       N  
+ATOM    158  CA  GLU A  21     -32.477   9.459   3.612  1.00 57.66           C  
+ANISOU  158  CA  GLU A  21     8917   7564   5427  -2115   1702   -289       C  
+ATOM    159  C   GLU A  21     -30.954   9.494   3.510  1.00 69.16           C  
+ANISOU  159  C   GLU A  21    10509   8819   6950  -1909   1465   -211       C  
+ATOM    160  O   GLU A  21     -30.299  10.257   4.219  1.00 68.04           O  
+ANISOU  160  O   GLU A  21    10456   8594   6803  -1844   1453   -181       O  
+ATOM    161  CB  GLU A  21     -32.902   9.996   4.981  1.00 54.36           C  
+ANISOU  161  CB  GLU A  21     8637   7155   4863  -2311   1887   -318       C  
+ATOM    162  CG  GLU A  21     -34.407  10.054   5.189  1.00 68.60           C  
+ANISOU  162  CG  GLU A  21    10271   9171   6622  -2525   2163   -432       C  
+ATOM    163  CD  GLU A  21     -34.791  10.951   6.350  1.00 82.51           C  
+ANISOU  163  CD  GLU A  21    12068  10992   8288  -2636   2392   -505       C  
+ATOM    164  OE1 GLU A  21     -33.934  11.746   6.793  1.00 70.17           O  
+ANISOU  164  OE1 GLU A  21    10599   9333   6730  -2486   2330   -464       O  
+ATOM    165  OE2 GLU A  21     -35.941  10.855   6.827  1.00 84.88           O  
+ANISOU  165  OE2 GLU A  21    12302  11435   8513  -2879   2639   -615       O  
+ATOM    166  N   ASN A  22     -30.389   8.674   2.631  1.00 79.63           N  
+ANISOU  166  N   ASN A  22    11840  10064   8351  -1807   1276   -194       N  
+ATOM    167  CA  ASN A  22     -28.944   8.678   2.441  1.00 73.29           C  
+ANISOU  167  CA  ASN A  22    11110   9082   7654  -1603   1064   -155       C  
+ATOM    168  C   ASN A  22     -28.578   8.794   0.963  1.00 66.84           C  
+ANISOU  168  C   ASN A  22    10030   8368   6998  -1357   1031   -186       C  
+ATOM    169  O   ASN A  22     -27.465   8.462   0.560  1.00 79.66           O  
+ANISOU  169  O   ASN A  22    11684   9859   8723  -1208    861   -189       O  
+ATOM    170  CB  ASN A  22     -28.315   7.429   3.054  1.00 71.97           C  
+ANISOU  170  CB  ASN A  22    11293   8637   7417  -1734    817   -122       C  
+ATOM    171  CG  ASN A  22     -26.835   7.604   3.334  1.00 74.03           C  
+ANISOU  171  CG  ASN A  22    11661   8675   7793  -1561    599    -95       C  
+ATOM    172  OD1 ASN A  22     -26.418   8.603   3.921  1.00 56.21           O  
+ANISOU  172  OD1 ASN A  22     9400   6403   5555  -1494    643    -66       O  
+ATOM    173  ND2 ASN A  22     -26.033   6.633   2.915  1.00 79.40           N  
+ANISOU  173  ND2 ASN A  22    12425   9175   8568  -1483    354   -120       N  
+ATOM    174  N   ALA A  23     -29.524   9.268   0.160  1.00 51.46           N  
+ANISOU  174  N   ALA A  23     7825   6652   5076  -1324   1192   -222       N  
+ATOM    175  CA  ALA A  23     -29.298   9.432  -1.271  1.00 48.45           C  
+ANISOU  175  CA  ALA A  23     7226   6378   4805  -1123   1173   -246       C  
+ATOM    176  C   ALA A  23     -28.730  10.814  -1.565  1.00 51.83           C  
+ANISOU  176  C   ALA A  23     7482   6879   5332   -921   1234   -220       C  
+ATOM    177  O   ALA A  23     -28.965  11.765  -0.821  1.00 50.23           O  
+ANISOU  177  O   ALA A  23     7254   6710   5121   -936   1331   -201       O  
+ATOM    178  CB  ALA A  23     -30.588   9.209  -2.046  1.00 46.30           C  
+ANISOU  178  CB  ALA A  23     6792   6287   4514  -1192   1263   -291       C  
+ATOM    179  N   ALA A  24     -27.977  10.915  -2.655  1.00 46.76           N  
+ANISOU  179  N   ALA A  24     6732   6258   4776   -744   1180   -228       N  
+ATOM    180  CA  ALA A  24     -27.394  12.185  -3.064  1.00 46.79           C  
+ANISOU  180  CA  ALA A  24     6585   6329   4866   -573   1231   -194       C  
+ATOM    181  C   ALA A  24     -27.706  12.498  -4.520  1.00 49.40           C  
+ANISOU  181  C   ALA A  24     6734   6823   5214   -476   1275   -208       C  
+ATOM    182  O   ALA A  24     -27.960  11.597  -5.320  1.00 57.05           O  
+ANISOU  182  O   ALA A  24     7708   7820   6148   -497   1236   -255       O  
+ATOM    183  CB  ALA A  24     -25.889  12.172  -2.839  1.00 39.61           C  
+ANISOU  183  CB  ALA A  24     5747   5256   4045   -467   1126   -182       C  
+ATOM    184  N   ILE A  25     -27.690  13.783  -4.855  1.00 49.14           N  
+ANISOU  184  N   ILE A  25     6564   6883   5224   -377   1337   -166       N  
+ATOM    185  CA  ILE A  25     -27.908  14.210  -6.232  1.00 52.99           C  
+ANISOU  185  CA  ILE A  25     6921   7503   5708   -296   1354   -162       C  
+ATOM    186  C   ILE A  25     -26.634  14.851  -6.744  1.00 55.52           C  
+ANISOU  186  C   ILE A  25     7213   7803   6080   -174   1355   -124       C  
+ATOM    187  O   ILE A  25     -26.051  15.677  -6.060  1.00 55.52           O  
+ANISOU  187  O   ILE A  25     7208   7744   6141   -131   1364    -76       O  
+ATOM    188  CB  ILE A  25     -29.067  15.220  -6.352  1.00 47.37           C  
+ANISOU  188  CB  ILE A  25     6076   6914   5008   -296   1398   -145       C  
+ATOM    189  CG1 ILE A  25     -30.379  14.592  -5.886  1.00 42.34           C  
+ANISOU  189  CG1 ILE A  25     5423   6318   4344   -431   1424   -207       C  
+ATOM    190  CG2 ILE A  25     -29.187  15.736  -7.782  1.00 41.39           C  
+ANISOU  190  CG2 ILE A  25     5232   6259   4236   -217   1370   -122       C  
+ATOM    191  CD1 ILE A  25     -30.877  13.485  -6.783  1.00 42.96           C  
+ANISOU  191  CD1 ILE A  25     5515   6436   4372   -487   1373   -252       C  
+ATOM    192  N   PHE A  26     -26.197  14.485  -7.942  1.00 51.19           N  
+ANISOU  192  N   PHE A  26     6646   7302   5502   -130   1355   -154       N  
+ATOM    193  CA  PHE A  26     -25.093  15.208  -8.548  1.00 42.30           C  
+ANISOU  193  CA  PHE A  26     5471   6190   4413    -44   1395   -125       C  
+ATOM    194  C   PHE A  26     -25.648  15.873  -9.804  1.00 50.21           C  
+ANISOU  194  C   PHE A  26     6419   7332   5327    -36   1422    -86       C  
+ATOM    195  O   PHE A  26     -26.049  15.205 -10.755  1.00 53.45           O  
+ANISOU  195  O   PHE A  26     6855   7806   5649    -61   1412   -135       O  
+ATOM    196  CB  PHE A  26     -23.929  14.242  -8.820  1.00 37.85           C  
+ANISOU  196  CB  PHE A  26     4940   5549   3894     -9   1387   -217       C  
+ATOM    197  CG  PHE A  26     -22.593  14.910  -9.034  1.00 41.40           C  
+ANISOU  197  CG  PHE A  26     5320   5978   4434     63   1441   -210       C  
+ATOM    198  CD1 PHE A  26     -21.472  14.420  -8.378  1.00 60.09           C  
+ANISOU  198  CD1 PHE A  26     7693   8198   6942    107   1392   -275       C  
+ATOM    199  CD2 PHE A  26     -22.470  16.084  -9.757  1.00 46.28           C  
+ANISOU  199  CD2 PHE A  26     5871   6700   5011     75   1519   -132       C  
+ATOM    200  CE1 PHE A  26     -20.241  15.028  -8.520  1.00 59.39           C  
+ANISOU  200  CE1 PHE A  26     7509   8087   6970    166   1443   -283       C  
+ATOM    201  CE2 PHE A  26     -21.234  16.692  -9.915  1.00 41.80           C  
+ANISOU  201  CE2 PHE A  26     5235   6115   4531    114   1581   -125       C  
+ATOM    202  CZ  PHE A  26     -20.120  16.167  -9.287  1.00 41.90           C  
+ANISOU  202  CZ  PHE A  26     5219   5997   4703    161   1553   -207       C  
+ATOM    203  N   ALA A  27     -25.662  17.203  -9.786  1.00 52.43           N  
+ANISOU  203  N   ALA A  27     6648   7642   5631     -4   1430      4       N  
+ATOM    204  CA  ALA A  27     -26.370  17.989 -10.792  1.00 46.58           C  
+ANISOU  204  CA  ALA A  27     5884   7000   4814     -7   1402     59       C  
+ATOM    205  C   ALA A  27     -25.440  18.697 -11.764  1.00 53.30           C  
+ANISOU  205  C   ALA A  27     6754   7888   5611      5   1447    116       C  
+ATOM    206  O   ALA A  27     -24.547  19.439 -11.357  1.00 62.15           O  
+ANISOU  206  O   ALA A  27     7849   8963   6802     32   1483    169       O  
+ATOM    207  CB  ALA A  27     -27.276  19.005 -10.114  1.00 42.23           C  
+ANISOU  207  CB  ALA A  27     5270   6446   4330     11   1345    109       C  
+ATOM    208  N   GLY A  28     -25.668  18.472 -13.053  1.00 58.28           N  
+ANISOU  208  N   GLY A  28     7442   8598   6105    -33   1445    107       N  
+ATOM    209  CA  GLY A  28     -24.934  19.175 -14.085  1.00 40.67           C  
+ANISOU  209  CA  GLY A  28     5262   6415   3774    -65   1500    165       C  
+ATOM    210  C   GLY A  28     -25.676  20.412 -14.549  1.00 44.79           C  
+ANISOU  210  C   GLY A  28     5822   6954   4244    -81   1383    286       C  
+ATOM    211  O   GLY A  28     -26.748  20.738 -14.038  1.00 51.32           O  
+ANISOU  211  O   GLY A  28     6599   7756   5145    -46   1262    302       O  
+ATOM    212  N   ALA A  29     -25.093  21.107 -15.520  1.00 47.38           N  
+ANISOU  212  N   ALA A  29     6238   7317   4449   -144   1415    361       N  
+ATOM    213  CA  ALA A  29     -25.640  22.365 -16.013  1.00 45.51           C  
+ANISOU  213  CA  ALA A  29     6074   7063   4155   -171   1270    491       C  
+ATOM    214  C   ALA A  29     -26.993  22.169 -16.694  1.00 50.46           C  
+ANISOU  214  C   ALA A  29     6765   7703   4706   -179   1095    483       C  
+ATOM    215  O   ALA A  29     -27.797  23.099 -16.774  1.00 50.06           O  
+ANISOU  215  O   ALA A  29     6728   7603   4689   -159    907    558       O  
+ATOM    216  CB  ALA A  29     -24.657  23.024 -16.962  1.00 54.37           C  
+ANISOU  216  CB  ALA A  29     7316   8216   5126   -279   1355    574       C  
+ATOM    217  N   GLY A  30     -27.230  20.958 -17.192  1.00 58.97           N  
+ANISOU  217  N   GLY A  30     7877   8832   5695   -205   1138    383       N  
+ATOM    218  CA  GLY A  30     -28.469  20.629 -17.874  1.00 57.69           C  
+ANISOU  218  CA  GLY A  30     7774   8676   5468   -219    966    362       C  
+ATOM    219  C   GLY A  30     -29.689  20.806 -16.991  1.00 56.81           C  
+ANISOU  219  C   GLY A  30     7510   8521   5555   -140    820    336       C  
+ATOM    220  O   GLY A  30     -30.770  21.147 -17.470  1.00 55.61           O  
+ANISOU  220  O   GLY A  30     7372   8344   5414   -135    617    352       O  
+ATOM    221  N   LEU A  31     -29.514  20.567 -15.695  1.00 57.79           N  
+ANISOU  221  N   LEU A  31     7488   8629   5839    -85    922    285       N  
+ATOM    222  CA  LEU A  31     -30.607  20.685 -14.737  1.00 53.27           C  
+ANISOU  222  CA  LEU A  31     6760   8032   5448    -31    842    233       C  
+ATOM    223  C   LEU A  31     -31.026  22.141 -14.539  1.00 55.09           C  
+ANISOU  223  C   LEU A  31     6940   8209   5784     28    701    303       C  
+ATOM    224  O   LEU A  31     -32.152  22.421 -14.129  1.00 57.73           O  
+ANISOU  224  O   LEU A  31     7144   8527   6264     75    587    245       O  
+ATOM    225  CB  LEU A  31     -30.206  20.070 -13.394  1.00 56.97           C  
+ANISOU  225  CB  LEU A  31     7141   8488   6019    -17    996    168       C  
+ATOM    226  CG  LEU A  31     -31.338  19.828 -12.393  1.00 55.33           C  
+ANISOU  226  CG  LEU A  31     6790   8278   5955     -9    976     81       C  
+ATOM    227  CD1 LEU A  31     -32.258  18.723 -12.885  1.00 52.04           C  
+ANISOU  227  CD1 LEU A  31     6363   7903   5506    -68    928     -1       C  
+ATOM    228  CD2 LEU A  31     -30.787  19.496 -11.018  1.00 48.07           C  
+ANISOU  228  CD2 LEU A  31     5844   7322   5100    -14   1115     48       C  
+ATOM    229  N   SER A  32     -30.119  23.064 -14.843  1.00 61.83           N  
+ANISOU  229  N   SER A  32     7888   9031   6573     22    705    416       N  
+ATOM    230  CA  SER A  32     -30.398  24.489 -14.696  1.00 59.76           C  
+ANISOU  230  CA  SER A  32     7607   8695   6404     77    545    492       C  
+ATOM    231  C   SER A  32     -31.013  25.084 -15.958  1.00 61.77           C  
+ANISOU  231  C   SER A  32     7991   8911   6569     47    305    564       C  
+ATOM    232  O   SER A  32     -31.225  26.294 -16.044  1.00 64.78           O  
+ANISOU  232  O   SER A  32     8398   9206   7010     83    122    639       O  
+ATOM    233  CB  SER A  32     -29.118  25.247 -14.335  1.00 54.07           C  
+ANISOU  233  CB  SER A  32     6934   7939   5671     71    644    590       C  
+ATOM    234  OG  SER A  32     -28.466  24.650 -13.228  1.00 54.34           O  
+ANISOU  234  OG  SER A  32     6880   7985   5781     94    834    528       O  
+HETATM  235  N   MSE A  33     -31.295  24.230 -16.936  1.00 62.27           N  
+ANISOU  235  N   MSE A  33     8156   9021   6484    -23    283    539       N  
+HETATM  236  CA  MSE A  33     -31.903  24.676 -18.184  1.00 66.22           C  
+ANISOU  236  CA  MSE A  33     8820   9469   6872    -69     30    606       C  
+HETATM  237  C   MSE A  33     -33.290  24.071 -18.367  1.00 70.66           C  
+ANISOU  237  C   MSE A  33     9285  10026   7536    -31   -141    496       C  
+HETATM  238  O   MSE A  33     -33.508  22.893 -18.078  1.00 69.46           O  
+ANISOU  238  O   MSE A  33     9043   9947   7402    -40     -9    389       O  
+HETATM  239  CB  MSE A  33     -31.011  24.314 -19.372  1.00 63.37           C  
+ANISOU  239  CB  MSE A  33     8714   9155   6210   -208    126    678       C  
+HETATM  240  CG  MSE A  33     -29.576  24.785 -19.227  1.00 61.84           C  
+ANISOU  240  CG  MSE A  33     8585   8984   5928   -267    333    762       C  
+HETATM  241 SE   MSE A  33     -29.389  26.718 -19.368  1.00 91.47          SE  
+ANISOU  241 SE   MSE A  33    12457  12604   9692   -288    113    952      SE  
+HETATM  242  CE  MSE A  33     -27.489  26.883 -18.958  1.00103.57           C  
+ANISOU  242  CE  MSE A  33    13990  14201  11160   -370    462   1007       C  
+ATOM    243  N   SER A  34     -34.223  24.886 -18.847  1.00 74.92           N  
+ANISOU  243  N   SER A  34     9843  10464   8158      8   -456    522       N  
+ATOM    244  CA  SER A  34     -35.589  24.439 -19.096  1.00 78.23           C  
+ANISOU  244  CA  SER A  34    10152  10860   8713     46   -663    412       C  
+ATOM    245  C   SER A  34     -35.627  23.340 -20.152  1.00 77.42           C  
+ANISOU  245  C   SER A  34    10225  10802   8390    -59   -662    406       C  
+ATOM    246  O   SER A  34     -36.445  22.424 -20.079  1.00 79.02           O  
+ANISOU  246  O   SER A  34    10302  11037   8684    -51   -684    289       O  
+ATOM    247  CB  SER A  34     -36.468  25.614 -19.528  1.00 81.87           C  
+ANISOU  247  CB  SER A  34    10623  11171   9313    113  -1050    443       C  
+ATOM    248  OG  SER A  34     -36.619  26.553 -18.478  1.00 82.80           O  
+ANISOU  248  OG  SER A  34    10538  11245   9679    232  -1065    402       O  
+ATOM    249  N   VAL A  35     -34.732  23.437 -21.130  1.00 75.09           N  
+ANISOU  249  N   VAL A  35    10224  10508   7799   -168   -629    526       N  
+ATOM    250  CA  VAL A  35     -34.660  22.454 -22.204  1.00 74.21           C  
+ANISOU  250  CA  VAL A  35    10319  10438   7440   -274   -615    514       C  
+ATOM    251  C   VAL A  35     -33.961  21.175 -21.750  1.00 70.42           C  
+ANISOU  251  C   VAL A  35     9766  10085   6905   -294   -277    419       C  
+ATOM    252  O   VAL A  35     -33.988  20.162 -22.449  1.00 70.19           O  
+ANISOU  252  O   VAL A  35     9855  10095   6717   -358   -247    366       O  
+ATOM    253  CB  VAL A  35     -33.927  23.019 -23.435  1.00 74.63           C  
+ANISOU  253  CB  VAL A  35    10734  10455   7168   -410   -669    659       C  
+ATOM    254  CG1 VAL A  35     -34.728  24.156 -24.052  1.00 75.76           C  
+ANISOU  254  CG1 VAL A  35    11012  10434   7339   -407  -1081    758       C  
+ATOM    255  CG2 VAL A  35     -32.532  23.489 -23.051  1.00 84.00           C  
+ANISOU  255  CG2 VAL A  35    11950  11701   8264   -453   -386    734       C  
+ATOM    256  N   GLY A  36     -33.335  21.226 -20.580  1.00 67.54           N  
+ANISOU  256  N   GLY A  36     9222   9765   6674   -238    -50    395       N  
+ATOM    257  CA  GLY A  36     -32.768  20.037 -19.971  1.00 63.54           C  
+ANISOU  257  CA  GLY A  36     8628   9344   6172   -241    216    296       C  
+ATOM    258  C   GLY A  36     -31.323  19.750 -20.333  1.00 61.72           C  
+ANISOU  258  C   GLY A  36     8539   9172   5740   -306    458    318       C  
+ATOM    259  O   GLY A  36     -30.747  18.772 -19.856  1.00 58.17           O  
+ANISOU  259  O   GLY A  36     8024   8770   5306   -298    655    227       O  
+ATOM    260  N   TYR A  37     -30.729  20.597 -21.167  1.00 62.73           N  
+ANISOU  260  N   TYR A  37     8859   9287   5687   -380    438    429       N  
+ATOM    261  CA  TYR A  37     -29.347  20.384 -21.581  1.00 64.60           C  
+ANISOU  261  CA  TYR A  37     9211   9594   5741   -461    692    429       C  
+ATOM    262  C   TYR A  37     -28.641  21.699 -21.879  1.00 71.72           C  
+ANISOU  262  C   TYR A  37    10228  10470   6551   -533    699    574       C  
+ATOM    263  O   TYR A  37     -29.274  22.750 -21.983  1.00 76.19           O  
+ANISOU  263  O   TYR A  37    10846  10950   7154   -527    462    685       O  
+ATOM    264  CB  TYR A  37     -29.288  19.488 -22.821  1.00 56.01           C  
+ANISOU  264  CB  TYR A  37     8330   8556   4394   -558    724    366       C  
+ATOM    265  CG  TYR A  37     -29.889  20.119 -24.060  1.00 65.89           C  
+ANISOU  265  CG  TYR A  37     9849   9756   5431   -659    489    469       C  
+ATOM    266  CD1 TYR A  37     -31.260  20.095 -24.285  1.00 65.44           C  
+ANISOU  266  CD1 TYR A  37     9801   9619   5445   -620    178    474       C  
+ATOM    267  CD2 TYR A  37     -29.081  20.738 -25.007  1.00 70.65           C  
+ANISOU  267  CD2 TYR A  37    10703  10379   5760   -809    568    558       C  
+ATOM    268  CE1 TYR A  37     -31.809  20.673 -25.416  1.00 77.26           C  
+ANISOU  268  CE1 TYR A  37    11564  11036   6753   -711    -86    570       C  
+ATOM    269  CE2 TYR A  37     -29.621  21.317 -26.140  1.00 74.05           C  
+ANISOU  269  CE2 TYR A  37    11430  10739   5966   -925    326    665       C  
+ATOM    270  CZ  TYR A  37     -30.985  21.282 -26.340  1.00 83.75           C  
+ANISOU  270  CZ  TYR A  37    12676  11867   7277   -867    -20    674       C  
+ATOM    271  OH  TYR A  37     -31.525  21.857 -27.467  1.00 84.54           O  
+ANISOU  271  OH  TYR A  37    13093  11867   7162   -980   -308    782       O  
+ATOM    272  N   VAL A  38     -27.322  21.627 -22.017  1.00 70.53           N  
+ANISOU  272  N   VAL A  38    10112  10388   6298   -604    962    563       N  
+ATOM    273  CA  VAL A  38     -26.518  22.784 -22.382  1.00 73.06           C  
+ANISOU  273  CA  VAL A  38    10555  10698   6506   -712   1009    698       C  
+ATOM    274  C   VAL A  38     -25.680  22.489 -23.615  1.00 66.93           C  
+ANISOU  274  C   VAL A  38    10001  10011   5420   -890   1201    677       C  
+ATOM    275  O   VAL A  38     -24.930  21.513 -23.638  1.00 70.33           O  
+ANISOU  275  O   VAL A  38    10359  10532   5831   -890   1454    529       O  
+ATOM    276  CB  VAL A  38     -25.582  23.213 -21.238  1.00 70.25           C  
+ANISOU  276  CB  VAL A  38     9994  10338   6358   -649   1171    706       C  
+ATOM    277  CG1 VAL A  38     -24.727  24.399 -21.666  1.00 68.14           C  
+ANISOU  277  CG1 VAL A  38     9856  10060   5973   -785   1222    848       C  
+ATOM    278  CG2 VAL A  38     -26.384  23.556 -20.006  1.00 75.70           C  
+ANISOU  278  CG2 VAL A  38    10491  10946   7326   -490   1005    717       C  
+ATOM    279  N   SER A  39     -25.800  23.325 -24.639  1.00 76.79           N  
+ANISOU  279  N   SER A  39    11529  11225   6423  -1048   1079    814       N  
+ATOM    280  CA  SER A  39     -24.930  23.189 -25.795  1.00 82.31           C  
+ANISOU  280  CA  SER A  39    12462  12017   6796  -1256   1298    799       C  
+ATOM    281  C   SER A  39     -23.650  23.940 -25.464  1.00 85.93           C  
+ANISOU  281  C   SER A  39    12845  12516   7288  -1341   1533    853       C  
+ATOM    282  O   SER A  39     -23.552  25.148 -25.679  1.00 93.54           O  
+ANISOU  282  O   SER A  39    13956  13412   8171  -1456   1422   1031       O  
+ATOM    283  CB  SER A  39     -25.592  23.737 -27.060  1.00 91.48           C  
+ANISOU  283  CB  SER A  39    14006  13112   7642  -1424   1057    931       C  
+ATOM    284  OG  SER A  39     -26.086  25.047 -26.850  1.00109.00           O  
+ANISOU  284  OG  SER A  39    16293  15190   9933  -1426    762   1123       O  
+ATOM    285  N   TRP A  40     -22.679  23.209 -24.923  1.00 77.68           N  
+ANISOU  285  N   TRP A  40    11567  11565   6383  -1282   1835    693       N  
+ATOM    286  CA  TRP A  40     -21.473  23.804 -24.357  1.00 82.68           C  
+ANISOU  286  CA  TRP A  40    12044  12225   7147  -1318   2045    714       C  
+ATOM    287  C   TRP A  40     -20.677  24.627 -25.363  1.00 89.83           C  
+ANISOU  287  C   TRP A  40    13178  13184   7768  -1591   2198    812       C  
+ATOM    288  O   TRP A  40     -20.141  25.683 -25.027  1.00 91.86           O  
+ANISOU  288  O   TRP A  40    13411  13400   8092  -1661   2203    945       O  
+ATOM    289  CB  TRP A  40     -20.585  22.708 -23.767  1.00 84.69           C  
+ANISOU  289  CB  TRP A  40    12025  12558   7594  -1211   2318    491       C  
+ATOM    290  CG  TRP A  40     -21.170  22.060 -22.550  1.00 88.32           C  
+ANISOU  290  CG  TRP A  40    12260  12945   8353   -972   2179    422       C  
+ATOM    291  CD1 TRP A  40     -21.842  20.874 -22.496  1.00 83.32           C  
+ANISOU  291  CD1 TRP A  40    11595  12315   7747   -863   2119    290       C  
+ATOM    292  CD2 TRP A  40     -21.129  22.560 -21.209  1.00 83.39           C  
+ANISOU  292  CD2 TRP A  40    11432  12230   8023   -836   2087    482       C  
+ATOM    293  NE1 TRP A  40     -22.226  20.606 -21.204  1.00 84.26           N  
+ANISOU  293  NE1 TRP A  40    11512  12355   8148   -687   2006    271       N  
+ATOM    294  CE2 TRP A  40     -21.799  21.626 -20.394  1.00 84.05           C  
+ANISOU  294  CE2 TRP A  40    11382  12271   8281   -665   1989    382       C  
+ATOM    295  CE3 TRP A  40     -20.591  23.708 -20.618  1.00 65.09           C  
+ANISOU  295  CE3 TRP A  40     9050   9856   5826   -855   2074    610       C  
+ATOM    296  CZ2 TRP A  40     -21.945  21.804 -19.021  1.00 79.41           C  
+ANISOU  296  CZ2 TRP A  40    10615  11594   7961   -524   1896    402       C  
+ATOM    297  CZ3 TRP A  40     -20.738  23.882 -19.254  1.00 68.07           C  
+ANISOU  297  CZ3 TRP A  40     9241  10140   6484   -693   1968    624       C  
+ATOM    298  CH2 TRP A  40     -21.409  22.935 -18.471  1.00 79.15           C  
+ANISOU  298  CH2 TRP A  40    10530  11510   8035   -535   1888    519       C  
+ATOM    299  N   ALA A  41     -20.597  24.135 -26.595  1.00 82.18           N  
+ANISOU  299  N   ALA A  41    12446  12306   6473  -1759   2328    745       N  
+ATOM    300  CA  ALA A  41     -19.937  24.869 -27.667  1.00 88.23           C  
+ANISOU  300  CA  ALA A  41    13434  13094   6994  -2005   2432    829       C  
+ATOM    301  C   ALA A  41     -20.665  26.177 -27.958  1.00 93.57           C  
+ANISOU  301  C   ALA A  41    14412  13637   7502  -2137   2108   1104       C  
+ATOM    302  O   ALA A  41     -20.062  27.250 -27.968  1.00101.13           O  
+ANISOU  302  O   ALA A  41    15408  14550   8468  -2261   2119   1241       O  
+ATOM    303  CB  ALA A  41     -19.854  24.016 -28.923  1.00 92.12           C  
+ANISOU  303  CB  ALA A  41    14078  13654   7267  -2078   2546    681       C  
+ATOM    304  N   LYS A  42     -21.968  26.069 -28.197  1.00 97.45           N  
+ANISOU  304  N   LYS A  42    15099  14041   7885  -2087   1780   1174       N  
+ATOM    305  CA  LYS A  42     -22.805  27.222 -28.515  1.00103.99           C  
+ANISOU  305  CA  LYS A  42    16201  14697   8613  -2159   1380   1410       C  
+ATOM    306  C   LYS A  42     -22.885  28.252 -27.390  1.00102.45           C  
+ANISOU  306  C   LYS A  42    15808  14379   8740  -2022   1191   1537       C  
+ATOM    307  O   LYS A  42     -23.038  29.445 -27.648  1.00110.68           O  
+ANISOU  307  O   LYS A  42    17069  15291   9692  -2144    957   1740       O  
+ATOM    308  CB  LYS A  42     -24.216  26.757 -28.882  1.00105.27           C  
+ANISOU  308  CB  LYS A  42    16495  14765   8740  -2048   1028   1400       C  
+ATOM    309  N   LEU A  43     -22.793  27.794 -26.146  1.00100.66           N  
+ANISOU  309  N   LEU A  43    15191  14177   8877  -1776   1275   1417       N  
+ATOM    310  CA  LEU A  43     -22.833  28.705 -25.006  1.00 97.60           C  
+ANISOU  310  CA  LEU A  43    14609  13679   8795  -1637   1122   1511       C  
+ATOM    311  C   LEU A  43     -21.577  29.567 -24.909  1.00105.46           C  
+ANISOU  311  C   LEU A  43    15606  14694   9769  -1803   1320   1607       C  
+ATOM    312  O   LEU A  43     -21.657  30.768 -24.652  1.00118.37           O  
+ANISOU  312  O   LEU A  43    17315  16198  11462  -1833   1105   1780       O  
+ATOM    313  CB  LEU A  43     -23.025  27.922 -23.706  1.00 81.54           C  
+ANISOU  313  CB  LEU A  43    12197  11668   7119  -1359   1179   1351       C  
+ATOM    314  N   LEU A  44     -20.419  28.949 -25.123  1.00100.06           N  
+ANISOU  314  N   LEU A  44    14829  14170   9019  -1912   1721   1481       N  
+ATOM    315  CA  LEU A  44     -19.149  29.663 -25.065  1.00 86.05           C  
+ANISOU  315  CA  LEU A  44    13017  12435   7243  -2089   1952   1543       C  
+ATOM    316  C   LEU A  44     -18.944  30.537 -26.300  1.00 93.37           C  
+ANISOU  316  C   LEU A  44    14329  13340   7808  -2411   1924   1713       C  
+ATOM    317  O   LEU A  44     -17.838  31.008 -26.565  1.00 96.36           O  
+ANISOU  317  O   LEU A  44    14659  13751   8201  -2555   2129   1715       O  
+ATOM    318  CB  LEU A  44     -17.988  28.677 -24.914  1.00 76.78           C  
+ANISOU  318  CB  LEU A  44    11582  11432   6159  -2088   2384   1315       C  
+ATOM    319  N   PRO A  46     -20.083  32.047 -29.925  1.00108.74           N  
+ANISOU  319  N   PRO A  46    17373  15026   8915  -2965   1359   2035       N  
+ATOM    320  CA  PRO A  46     -20.941  33.233 -30.000  1.00107.63           C  
+ANISOU  320  CA  PRO A  46    17512  14654   8728  -3006    881   2272       C  
+ATOM    321  C   PRO A  46     -20.506  34.334 -29.038  1.00111.24           C  
+ANISOU  321  C   PRO A  46    17845  15022   9400  -2989    803   2418       C  
+ATOM    322  O   PRO A  46     -20.958  35.472 -29.162  1.00106.38           O  
+ANISOU  322  O   PRO A  46    17455  14202   8762  -3050    428   2609       O  
+ATOM    323  CB  PRO A  46     -22.317  32.683 -29.624  1.00 99.11           C  
+ANISOU  323  CB  PRO A  46    16444  13511   7704  -2787    568   2263       C  
+ATOM    324  CG  PRO A  46     -22.278  31.277 -30.113  1.00 98.12           C  
+ANISOU  324  CG  PRO A  46    16252  13557   7472  -2755    840   2046       C  
+ATOM    325  CD  PRO A  46     -20.872  30.805 -29.849  1.00104.18           C  
+ANISOU  325  CD  PRO A  46    16727  14519   8340  -2785   1347   1886       C  
+ATOM    326  N   ILE A  47     -19.639  33.994 -28.090  1.00106.99           N  
+ANISOU  326  N   ILE A  47    16950  14617   9082  -2899   1129   2320       N  
+ATOM    327  CA  ILE A  47     -19.047  34.995 -27.213  1.00 99.59           C  
+ANISOU  327  CA  ILE A  47    15886  13605   8346  -2905   1101   2445       C  
+ATOM    328  C   ILE A  47     -17.637  35.310 -27.695  1.00112.18           C  
+ANISOU  328  C   ILE A  47    17435  15292   9895  -3130   1443   2411       C  
+ATOM    329  O   ILE A  47     -17.149  36.428 -27.531  1.00122.95           O  
+ANISOU  329  O   ILE A  47    18853  16554  11307  -3251   1358   2560       O  
+ATOM    330  CB  ILE A  47     -19.015  34.526 -25.743  1.00 89.63           C  
+ANISOU  330  CB  ILE A  47    14266  12403   7387  -2667   1195   2375       C  
+ATOM    331  CG1 ILE A  47     -20.433  34.243 -25.249  1.00 94.50           C  
+ANISOU  331  CG1 ILE A  47    14812  12905   8188  -2353    831   2331       C  
+ATOM    332  CG2 ILE A  47     -18.377  35.579 -24.849  1.00 69.64           C  
+ANISOU  332  CG2 ILE A  47    11594   9772   5094  -2656   1145   2491       C  
+ATOM    333  CD1 ILE A  47     -21.337  35.458 -25.273  1.00102.51           C  
+ANISOU  333  CD1 ILE A  47    16054  13675   9221  -2330    327   2530       C  
+ATOM    334  N   ALA A  48     -16.996  34.334 -28.332  1.00106.43           N  
+ANISOU  334  N   ALA A  48    16614  14748   9076  -3190   1813   2209       N  
+ATOM    335  CA  ALA A  48     -15.676  34.571 -28.894  1.00 96.52           C  
+ANISOU  335  CA  ALA A  48    15314  13592   7770  -3412   2142   2154       C  
+ATOM    336  C   ALA A  48     -15.843  35.163 -30.285  1.00 99.19           C  
+ANISOU  336  C   ALA A  48    16068  13859   7761  -3689   2018   2256       C  
+ATOM    337  O   ALA A  48     -14.903  35.714 -30.859  1.00 96.99           O  
+ANISOU  337  O   ALA A  48    15855  13614   7383  -3934   2198   2277       O  
+ATOM    338  CB  ALA A  48     -14.870  33.286 -28.941  1.00 89.45           C  
+ANISOU  338  CB  ALA A  48    14116  12910   6961  -3342   2573   1875       C  
+ATOM    339  N   GLN A  49     -17.053  35.038 -30.822  1.00 96.07           N  
+ANISOU  339  N   GLN A  49    15958  13360   7186  -3656   1699   2316       N  
+ATOM    340  CA  GLN A  49     -17.391  35.651 -32.097  1.00 96.58           C  
+ANISOU  340  CA  GLN A  49    16459  13309   6928  -3909   1494   2430       C  
+ATOM    341  C   GLN A  49     -17.638  37.131 -31.840  1.00 96.01           C  
+ANISOU  341  C   GLN A  49    16577  13011   6892  -3992   1116   2677       C  
+ATOM    342  O   GLN A  49     -17.432  37.978 -32.709  1.00102.11           O  
+ANISOU  342  O   GLN A  49    17662  13684   7451  -4263   1009   2791       O  
+ATOM    343  CB  GLN A  49     -18.619  34.988 -32.724  1.00 99.19           C  
+ANISOU  343  CB  GLN A  49    17018  13583   7089  -3832   1249   2400       C  
+ATOM    344  N   GLU A  50     -18.089  37.418 -30.621  1.00104.62           N  
+ANISOU  344  N   GLU A  50    17480  14012   8258  -3755    907   2750       N  
+ATOM    345  CA  GLU A  50     -18.344  38.779 -30.163  1.00106.16           C  
+ANISOU  345  CA  GLU A  50    17795  13981   8559  -3770    527   2964       C  
+ATOM    346  C   GLU A  50     -17.060  39.510 -29.779  1.00111.53           C  
+ANISOU  346  C   GLU A  50    18331  14701   9345  -3916    760   3012       C  
+ATOM    347  O   GLU A  50     -17.098  40.665 -29.354  1.00118.87           O  
+ANISOU  347  O   GLU A  50    19337  15449  10378  -3939    479   3181       O  
+ATOM    348  CB  GLU A  50     -19.308  38.763 -28.974  1.00 93.51           C  
+ANISOU  348  CB  GLU A  50    16031  12273   7226  -3448    223   3005       C  
+ATOM    349  N   ILE A  51     -15.927  38.832 -29.928  1.00108.58           N  
+ANISOU  349  N   ILE A  51    17737  14553   8965  -4005   1257   2851       N  
+ATOM    350  CA  ILE A  51     -14.628  39.439 -29.663  1.00100.64           C  
+ANISOU  350  CA  ILE A  51    16576  13602   8062  -4164   1510   2873       C  
+ATOM    351  C   ILE A  51     -13.763  39.332 -30.920  1.00 94.74           C  
+ANISOU  351  C   ILE A  51    15969  12982   7044  -4479   1825   2794       C  
+ATOM    352  O   ILE A  51     -12.681  39.915 -31.005  1.00106.10           O  
+ANISOU  352  O   ILE A  51    17351  14464   8499  -4684   2029   2817       O  
+ATOM    353  CB  ILE A  51     -13.928  38.764 -28.456  1.00 89.60           C  
+ANISOU  353  CB  ILE A  51    14699  12346   6998  -3956   1819   2731       C  
+ATOM    354  CG1 ILE A  51     -14.903  38.625 -27.286  1.00 82.06           C  
+ANISOU  354  CG1 ILE A  51    13622  11290   6265  -3644   1538   2777       C  
+ATOM    355  CG2 ILE A  51     -12.720  39.565 -27.999  1.00103.93           C  
+ANISOU  355  CG2 ILE A  51    16351  14162   8976  -4093   1981   2789       C  
+ATOM    356  CD1 ILE A  51     -14.285  38.040 -26.037  1.00 99.21           C  
+ANISOU  356  CD1 ILE A  51    15363  13570   8765  -3453   1789   2654       C  
+ATOM    357  N   GLY A  52     -14.263  38.598 -31.908  1.00103.51           N  
+ANISOU  357  N   GLY A  52    17277  14149   7904  -4526   1853   2699       N  
+ATOM    358  CA  GLY A  52     -13.555  38.427 -33.163  1.00101.01           C  
+ANISOU  358  CA  GLY A  52    17129  13948   7300  -4826   2138   2612       C  
+ATOM    359  C   GLY A  52     -12.487  37.354 -33.095  1.00108.66           C  
+ANISOU  359  C   GLY A  52    17726  15178   8382  -4787   2668   2351       C  
+ATOM    360  O   GLY A  52     -11.657  37.234 -33.996  1.00121.77           O  
+ANISOU  360  O   GLY A  52    19446  16960   9860  -5035   2973   2252       O  
+ATOM    361  N   LEU A  53     -12.505  36.575 -32.019  1.00103.25           N  
+ANISOU  361  N   LEU A  53    16656  14569   8006  -4477   2765   2230       N  
+ATOM    362  CA  LEU A  53     -11.564  35.475 -31.855  1.00102.47           C  
+ANISOU  362  CA  LEU A  53    16176  14689   8069  -4389   3214   1960       C  
+ATOM    363  C   LEU A  53     -12.235  34.150 -32.200  1.00103.39           C  
+ANISOU  363  C   LEU A  53    16286  14889   8107  -4215   3256   1779       C  
+ATOM    364  O   LEU A  53     -12.758  33.463 -31.325  1.00106.56           O  
+ANISOU  364  O   LEU A  53    16474  15294   8720  -3924   3184   1712       O  
+ATOM    365  CB  LEU A  53     -11.018  35.439 -30.426  1.00 92.55           C  
+ANISOU  365  CB  LEU A  53    14488  13452   7225  -4174   3300   1923       C  
+ATOM    366  N   ASP A  54     -12.217  33.800 -33.482  1.00100.81           N  
+ANISOU  366  N   ASP A  54    16209  14626   7470  -4407   3371   1699       N  
+ATOM    367  CA  ASP A  54     -12.885  32.593 -33.956  1.00106.36           C  
+ANISOU  367  CA  ASP A  54    16961  15390   8059  -4275   3386   1540       C  
+ATOM    368  C   ASP A  54     -12.118  31.330 -33.579  1.00100.00           C  
+ANISOU  368  C   ASP A  54    15736  14775   7484  -4092   3760   1243       C  
+ATOM    369  O   ASP A  54     -10.895  31.271 -33.708  1.00108.18           O  
+ANISOU  369  O   ASP A  54    16564  15936   8604  -4201   4103   1106       O  
+ATOM    370  CB  ASP A  54     -13.078  32.654 -35.473  1.00115.05           C  
+ANISOU  370  CB  ASP A  54    18487  16483   8744  -4558   3383   1550       C  
+ATOM    371  N   VAL A  55     -12.848  30.321 -33.115  1.00 93.59           N  
+ANISOU  371  N   VAL A  55    14801  13975   6784  -3815   3676   1138       N  
+ATOM    372  CA  VAL A  55     -12.249  29.046 -32.740  1.00 96.09           C  
+ANISOU  372  CA  VAL A  55    14743  14439   7327  -3616   3966    850       C  
+ATOM    373  C   VAL A  55     -11.746  28.295 -33.968  1.00110.57           C  
+ANISOU  373  C   VAL A  55    16664  16404   8942  -3761   4246    641       C  
+ATOM    374  O   VAL A  55     -11.534  27.083 -33.923  1.00111.76           O  
+ANISOU  374  O   VAL A  55    16601  16656   9206  -3594   4422    393       O  
+ATOM    375  CB  VAL A  55     -13.248  28.155 -31.978  1.00 87.96           C  
+ANISOU  375  CB  VAL A  55    13605  13374   6443  -3303   3777    798       C  
+ATOM    376  N   ASN A  59      -5.592  28.364 -32.552  1.00105.88           N  
+ANISOU  376  N   ASN A  59    14493  16260   9478  -3927   5627    -59       N  
+ATOM    377  CA  ASN A  59      -4.867  29.542 -33.014  1.00120.32           C  
+ANISOU  377  CA  ASN A  59    16428  18105  11185  -4255   5749     71       C  
+ATOM    378  C   ASN A  59      -5.129  30.750 -32.123  1.00124.95           C  
+ANISOU  378  C   ASN A  59    17049  18545  11880  -4263   5486    371       C  
+ATOM    379  O   ASN A  59      -4.214  31.277 -31.493  1.00120.63           O  
+ANISOU  379  O   ASN A  59    16234  18003  11597  -4299   5588    375       O  
+ATOM    380  CB  ASN A  59      -5.243  29.865 -34.461  1.00120.56           C  
+ANISOU  380  CB  ASN A  59    16922  18157  10727  -4562   5778    149       C  
+ATOM    381  N   ASP A  60      -6.378  31.203 -32.088  1.00122.67           N  
+ANISOU  381  N   ASP A  60    17094  18120  11395  -4234   5139    616       N  
+ATOM    382  CA  ASP A  60      -6.755  32.287 -31.191  1.00109.78           C  
+ANISOU  382  CA  ASP A  60    15506  16333   9875  -4208   4854    891       C  
+ATOM    383  C   ASP A  60      -7.088  31.709 -29.821  1.00100.99           C  
+ANISOU  383  C   ASP A  60    14082  15169   9120  -3851   4722    841       C  
+ATOM    384  O   ASP A  60      -7.110  32.422 -28.813  1.00 91.93           O  
+ANISOU  384  O   ASP A  60    12834  13915   8180  -3784   4558    999       O  
+ATOM    385  CB  ASP A  60      -7.945  33.069 -31.750  1.00105.10           C  
+ANISOU  385  CB  ASP A  60    15406  15597   8930  -4335   4513   1164       C  
+ATOM    386  N   LEU A  61      -7.332  30.402 -29.795  1.00100.64           N  
+ANISOU  386  N   LEU A  61    13899  15197   9144  -3634   4794    616       N  
+ATOM    387  CA  LEU A  61      -7.719  29.723 -28.567  1.00101.18           C  
+ANISOU  387  CA  LEU A  61    13707  15217   9521  -3305   4667    549       C  
+ATOM    388  C   LEU A  61      -6.540  29.567 -27.614  1.00104.03           C  
+ANISOU  388  C   LEU A  61    13616  15609  10303  -3204   4839    397       C  
+ATOM    389  O   LEU A  61      -6.727  29.510 -26.401  1.00109.18           O  
+ANISOU  389  O   LEU A  61    14074  16177  11231  -2998   4693    425       O  
+ATOM    390  CB  LEU A  61      -8.324  28.354 -28.882  1.00100.85           C  
+ANISOU  390  CB  LEU A  61    13673  15231   9414  -3121   4679    350       C  
+ATOM    391  CG  LEU A  61      -9.558  28.349 -29.789  1.00103.42           C  
+ANISOU  391  CG  LEU A  61    14427  15519   9350  -3193   4486    474       C  
+ATOM    392  CD1 LEU A  61     -10.146  26.950 -29.889  1.00104.58           C  
+ANISOU  392  CD1 LEU A  61    14533  15709   9494  -2979   4481    275       C  
+ATOM    393  CD2 LEU A  61     -10.601  29.338 -29.287  1.00 96.07           C  
+ANISOU  393  CD2 LEU A  61    13724  14430   8347  -3186   4127    778       C  
+ATOM    394  N   VAL A  62      -5.329  29.483 -28.157  1.00108.98           N  
+ANISOU  394  N   VAL A  62    14073  16350  10984  -3354   5143    225       N  
+ATOM    395  CA  VAL A  62      -4.152  29.371 -27.304  1.00115.14           C  
+ANISOU  395  CA  VAL A  62    14416  17150  12184  -3272   5291     70       C  
+ATOM    396  C   VAL A  62      -3.848  30.735 -26.694  1.00117.59           C  
+ANISOU  396  C   VAL A  62    14721  17365  12594  -3407   5188    318       C  
+ATOM    397  O   VAL A  62      -3.379  30.833 -25.559  1.00129.64           O  
+ANISOU  397  O   VAL A  62    15946  18828  14482  -3274   5141    298       O  
+ATOM    398  CB  VAL A  62      -2.916  28.840 -28.070  1.00115.02           C  
+ANISOU  398  CB  VAL A  62    14193  17287  12224  -3390   5654   -218       C  
+ATOM    399  CG1 VAL A  62      -3.109  27.376 -28.433  1.00118.28           C  
+ANISOU  399  CG1 VAL A  62    14536  17771  12634  -3205   5740   -501       C  
+ATOM    400  CG2 VAL A  62      -2.646  29.664 -29.316  1.00101.05           C  
+ANISOU  400  CG2 VAL A  62    12708  15589  10097  -3754   5811   -113       C  
+ATOM    401  N   SER A  63      -4.139  31.787 -27.452  1.00108.50           N  
+ANISOU  401  N   SER A  63    13923  16186  11115  -3675   5130    554       N  
+ATOM    402  CA  SER A  63      -3.979  33.151 -26.972  1.00102.84           C  
+ANISOU  402  CA  SER A  63    13273  15357  10447  -3821   4991    819       C  
+ATOM    403  C   SER A  63      -5.005  33.429 -25.883  1.00104.80           C  
+ANISOU  403  C   SER A  63    13584  15442  10791  -3616   4645   1009       C  
+ATOM    404  O   SER A  63      -4.711  34.103 -24.897  1.00103.30           O  
+ANISOU  404  O   SER A  63    13246  15154  10850  -3588   4540   1124       O  
+ATOM    405  CB  SER A  63      -4.118  34.155 -28.117  1.00104.50           C  
+ANISOU  405  CB  SER A  63    13890  15556  10259  -4161   4977   1017       C  
+ATOM    406  OG  SER A  63      -5.400  34.075 -28.714  1.00119.63           O  
+ANISOU  406  OG  SER A  63    16203  17416  11834  -4149   4755   1136       O  
+ATOM    407  N   LEU A  64      -6.212  32.903 -26.070  1.00 86.00           N  
+ANISOU  407  N   LEU A  64    11426  13035   8215  -3479   4468   1035       N  
+ATOM    408  CA  LEU A  64      -7.261  33.042 -25.068  1.00 98.06           C  
+ANISOU  408  CA  LEU A  64    13011  14424   9823  -3276   4156   1183       C  
+ATOM    409  C   LEU A  64      -6.910  32.267 -23.804  1.00104.90           C  
+ANISOU  409  C   LEU A  64    13474  15288  11094  -3010   4198   1008       C  
+ATOM    410  O   LEU A  64      -7.101  32.756 -22.691  1.00104.21           O  
+ANISOU  410  O   LEU A  64    13308  15082  11205  -2918   4024   1130       O  
+ATOM    411  CB  LEU A  64      -8.603  32.557 -25.621  1.00 87.40           C  
+ANISOU  411  CB  LEU A  64    11966  13060   8183  -3197   3975   1219       C  
+ATOM    412  CG  LEU A  64      -9.743  32.478 -24.603  1.00 82.28           C  
+ANISOU  412  CG  LEU A  64    11346  12293   7621  -2967   3680   1322       C  
+ATOM    413  CD1 LEU A  64     -10.044  33.852 -24.023  1.00 74.93           C  
+ANISOU  413  CD1 LEU A  64    10565  11199   6706  -3046   3413   1609       C  
+ATOM    414  CD2 LEU A  64     -10.991  31.858 -25.218  1.00 88.58           C  
+ANISOU  414  CD2 LEU A  64    12405  13096   8155  -2891   3530   1317       C  
+ATOM    415  N   ALA A  65      -6.402  31.053 -23.984  1.00109.40           N  
+ANISOU  415  N   ALA A  65    13806  15975  11784  -2891   4413    715       N  
+ATOM    416  CA  ALA A  65      -6.007  30.205 -22.867  1.00104.65           C  
+ANISOU  416  CA  ALA A  65    12830  15358  11574  -2638   4440    513       C  
+ATOM    417  C   ALA A  65      -4.870  30.827 -22.063  1.00100.83           C  
+ANISOU  417  C   ALA A  65    12048  14828  11435  -2685   4504    511       C  
+ATOM    418  O   ALA A  65      -4.857  30.752 -20.834  1.00 92.07           O  
+ANISOU  418  O   ALA A  65    10740  13615  10628  -2515   4384    498       O  
+ATOM    419  CB  ALA A  65      -5.607  28.825 -23.366  1.00106.23           C  
+ANISOU  419  CB  ALA A  65    12861  15677  11825  -2525   4639    193       C  
+ATOM    420  N   GLN A  66      -3.917  31.443 -22.758  1.00 92.14           N  
+ANISOU  420  N   GLN A  66    10921  13795  10292  -2926   4690    519       N  
+ATOM    421  CA  GLN A  66      -2.769  32.046 -22.088  1.00100.16           C  
+ANISOU  421  CA  GLN A  66    11641  14773  11642  -2995   4759    509       C  
+ATOM    422  C   GLN A  66      -3.093  33.429 -21.523  1.00105.52           C  
+ANISOU  422  C   GLN A  66    12488  15305  12299  -3116   4541    836       C  
+ATOM    423  O   GLN A  66      -2.417  33.907 -20.613  1.00115.68           O  
+ANISOU  423  O   GLN A  66    13538  16507  13908  -3113   4506    859       O  
+ATOM    424  CB  GLN A  66      -1.576  32.129 -23.043  1.00104.62           C  
+ANISOU  424  CB  GLN A  66    12089  15476  12188  -3216   5062    370       C  
+ATOM    425  CG  GLN A  66      -1.035  30.769 -23.459  1.00110.64           C  
+ANISOU  425  CG  GLN A  66    12618  16364  13057  -3088   5283      9       C  
+ATOM    426  CD  GLN A  66      -0.457  29.992 -22.292  1.00112.76           C  
+ANISOU  426  CD  GLN A  66    12467  16568  13809  -2821   5244   -221       C  
+ATOM    427  OE1 GLN A  66      -1.108  29.104 -21.740  1.00116.87           O  
+ANISOU  427  OE1 GLN A  66    12961  17033  14410  -2565   5105   -313       O  
+ATOM    428  NE2 GLN A  66       0.772  30.321 -21.911  1.00112.72           N  
+ANISOU  428  NE2 GLN A  66    12137  16556  14133  -2884   5349   -320       N  
+ATOM    429  N   TYR A  67      -4.127  34.067 -22.064  1.00 99.56           N  
+ANISOU  429  N   TYR A  67    12147  14502  11178  -3220   4370   1079       N  
+ATOM    430  CA  TYR A  67      -4.645  35.303 -21.488  1.00 87.93           C  
+ANISOU  430  CA  TYR A  67    10880  12860   9671  -3294   4096   1387       C  
+ATOM    431  C   TYR A  67      -5.354  34.979 -20.181  1.00 74.15           C  
+ANISOU  431  C   TYR A  67     9044  11000   8131  -3035   3886   1399       C  
+ATOM    432  O   TYR A  67      -5.171  35.657 -19.171  1.00 72.65           O  
+ANISOU  432  O   TYR A  67     8764  10675   8165  -3027   3748   1517       O  
+ATOM    433  CB  TYR A  67      -5.597  36.012 -22.456  1.00 82.98           C  
+ANISOU  433  CB  TYR A  67    10730  12192   8608  -3455   3924   1618       C  
+ATOM    434  CG  TYR A  67      -6.244  37.254 -21.877  1.00 81.62           C  
+ANISOU  434  CG  TYR A  67    10795  11820   8398  -3501   3579   1927       C  
+ATOM    435  CD1 TYR A  67      -5.591  38.479 -21.903  1.00 88.67           C  
+ANISOU  435  CD1 TYR A  67    11747  12624   9320  -3726   3534   2105       C  
+ATOM    436  CD2 TYR A  67      -7.509  37.199 -21.305  1.00 84.61           C  
+ANISOU  436  CD2 TYR A  67    11338  12093   8718  -3316   3281   2036       C  
+ATOM    437  CE1 TYR A  67      -6.180  39.616 -21.374  1.00 91.89           C  
+ANISOU  437  CE1 TYR A  67    12383  12828   9705  -3750   3177   2380       C  
+ATOM    438  CE2 TYR A  67      -8.104  38.328 -20.773  1.00 83.04           C  
+ANISOU  438  CE2 TYR A  67    11352  11702   8499  -3338   2930   2308       C  
+ATOM    439  CZ  TYR A  67      -7.437  39.533 -20.810  1.00 88.32           C  
+ANISOU  439  CZ  TYR A  67    12085  12269   9203  -3547   2867   2477       C  
+ATOM    440  OH  TYR A  67      -8.029  40.658 -20.282  1.00 95.44           O  
+ANISOU  440  OH  TYR A  67    13202  12957  10103  -3543   2476   2738       O  
+ATOM    441  N   TYR A  68      -6.178  33.939 -20.222  1.00 72.14           N  
+ANISOU  441  N   TYR A  68     8829  10793   7790  -2835   3861   1275       N  
+ATOM    442  CA  TYR A  68      -6.938  33.495 -19.062  1.00 84.06           C  
+ANISOU  442  CA  TYR A  68    10273  12195   9472  -2560   3654   1259       C  
+ATOM    443  C   TYR A  68      -6.028  33.008 -17.943  1.00 91.71           C  
+ANISOU  443  C   TYR A  68    10834  13096  10914  -2355   3679   1068       C  
+ATOM    444  O   TYR A  68      -6.285  33.259 -16.766  1.00100.77           O  
+ANISOU  444  O   TYR A  68    11928  14061  12299  -2125   3380   1139       O  
+ATOM    445  CB  TYR A  68      -7.905  32.381 -19.467  1.00 74.34           C  
+ANISOU  445  CB  TYR A  68     9152  11042   8053  -2405   3650   1138       C  
+ATOM    446  CG  TYR A  68      -8.783  31.890 -18.342  1.00 66.72           C  
+ANISOU  446  CG  TYR A  68     8137   9934   7279  -2039   3337   1119       C  
+ATOM    447  CD1 TYR A  68      -9.927  32.583 -17.973  1.00 70.09           C  
+ANISOU  447  CD1 TYR A  68     8799  10222   7610  -1940   2985   1334       C  
+ATOM    448  CD2 TYR A  68      -8.468  30.728 -17.648  1.00 71.11           C  
+ANISOU  448  CD2 TYR A  68     8415  10488   8115  -1804   3391    875       C  
+ATOM    449  CE1 TYR A  68     -10.731  32.134 -16.944  1.00 69.21           C  
+ANISOU  449  CE1 TYR A  68     8637   9998   7663  -1634   2739   1300       C  
+ATOM    450  CE2 TYR A  68      -9.266  30.271 -16.617  1.00 75.16           C  
+ANISOU  450  CE2 TYR A  68     8914  10872   8773  -1509   3120    865       C  
+ATOM    451  CZ  TYR A  68     -10.397  30.978 -16.269  1.00 71.94           C  
+ANISOU  451  CZ  TYR A  68     8732  10352   8251  -1434   2816   1075       C  
+ATOM    452  OH  TYR A  68     -11.196  30.527 -15.244  1.00 81.06           O  
+ANISOU  452  OH  TYR A  68     9867  11395   9538  -1168   2585   1048       O  
+ATOM    453  N   CYS A  69      -4.960  32.314 -18.320  1.00 87.93           N  
+ANISOU  453  N   CYS A  69    10076  12757  10576  -2435   4021    815       N  
+ATOM    454  CA  CYS A  69      -4.030  31.753 -17.349  1.00 83.51           C  
+ANISOU  454  CA  CYS A  69     9116  12127  10489  -2249   4043    599       C  
+ATOM    455  C   CYS A  69      -2.842  32.680 -17.111  1.00 89.46           C  
+ANISOU  455  C   CYS A  69     9669  12838  11483  -2436   4126    645       C  
+ATOM    456  O   CYS A  69      -1.768  32.236 -16.705  1.00 87.37           O  
+ANISOU  456  O   CYS A  69     9039  12564  11592  -2366   4228    424       O  
+ATOM    457  CB  CYS A  69      -3.544  30.379 -17.812  1.00 70.19           C  
+ANISOU  457  CB  CYS A  69     7212  10572   8884  -2138   4251    265       C  
+ATOM    458  SG  CYS A  69      -4.835  29.113 -17.845  1.00 86.65           S  
+ANISOU  458  SG  CYS A  69     9458  12675  10790  -1898   4158    167       S  
+ATOM    459  N   ASN A  70      -3.041  33.969 -17.367  1.00 91.83           N  
+ANISOU  459  N   ASN A  70    10218  13095  11580  -2657   4029    935       N  
+ATOM    460  CA  ASN A  70      -1.998  34.959 -17.135  1.00 83.06           C  
+ANISOU  460  CA  ASN A  70     8955  11927  10676  -2858   4073   1019       C  
+ATOM    461  C   ASN A  70      -1.855  35.236 -15.642  1.00 83.15           C  
+ANISOU  461  C   ASN A  70     8817  11691  11086  -2585   3718   1064       C  
+ATOM    462  O   ASN A  70      -2.820  35.104 -14.888  1.00 82.33           O  
+ANISOU  462  O   ASN A  70     8865  11448  10969  -2313   3396   1146       O  
+ATOM    463  CB  ASN A  70      -2.311  36.249 -17.900  1.00 85.61           C  
+ANISOU  463  CB  ASN A  70     9642  12248  10638  -3153   4003   1330       C  
+ATOM    464  CG  ASN A  70      -1.252  37.315 -17.712  1.00 88.67           C  
+ANISOU  464  CG  ASN A  70     9901  12569  11220  -3371   4021   1438       C  
+ATOM    465  OD1 ASN A  70      -1.267  38.056 -16.730  1.00 94.31           O  
+ANISOU  465  OD1 ASN A  70    10609  13085  12140  -3312   3759   1590       O  
+ATOM    466  ND2 ASN A  70      -0.325  37.400 -18.659  1.00 82.19           N  
+ANISOU  466  ND2 ASN A  70     8991  11893  10344  -3564   4264   1356       N  
+ATOM    467  N   GLU A  71      -0.648  35.603 -15.220  1.00 91.60           N  
+ANISOU  467  N   GLU A  71     9587  12707  12510  -2669   3785   1000       N  
+ATOM    468  CA  GLU A  71      -0.368  35.891 -13.813  1.00 95.32           C  
+ANISOU  468  CA  GLU A  71     9916  12931  13370  -2436   3450   1034       C  
+ATOM    469  C   GLU A  71      -1.324  36.928 -13.228  1.00 97.28           C  
+ANISOU  469  C   GLU A  71    10507  12993  13463  -2362   3058   1348       C  
+ATOM    470  O   GLU A  71      -1.751  36.810 -12.079  1.00 99.06           O  
+ANISOU  470  O   GLU A  71    10752  13031  13857  -2071   2740   1364       O  
+ATOM    471  CB  GLU A  71       1.077  36.364 -13.644  1.00 97.46           C  
+ANISOU  471  CB  GLU A  71     9848  13175  14006  -2612   3582    959       C  
+ATOM    472  N   ASN A  72      -1.656  37.941 -14.022  1.00 90.24           N  
+ANISOU  472  N   ASN A  72     9897  12144  12245  -2633   3077   1586       N  
+ATOM    473  CA  ASN A  72      -2.621  38.947 -13.601  1.00 89.23           C  
+ANISOU  473  CA  ASN A  72    10105  11841  11959  -2567   2701   1867       C  
+ATOM    474  C   ASN A  72      -4.012  38.327 -13.511  1.00 94.09           C  
+ANISOU  474  C   ASN A  72    10934  12458  12359  -2314   2541   1860       C  
+ATOM    475  O   ASN A  72      -4.599  37.950 -14.526  1.00 99.09           O  
+ANISOU  475  O   ASN A  72    11734  13248  12667  -2414   2694   1853       O  
+ATOM    476  CB  ASN A  72      -2.615  40.134 -14.567  1.00 97.56           C  
+ANISOU  476  CB  ASN A  72    11427  12928  12714  -2937   2742   2115       C  
+ATOM    477  CG  ASN A  72      -3.264  41.370 -13.977  1.00108.42           C  
+ANISOU  477  CG  ASN A  72    13074  14071  14050  -2881   2320   2390       C  
+ATOM    478  OD1 ASN A  72      -3.658  41.382 -12.811  1.00112.27           O  
+ANISOU  478  OD1 ASN A  72    13533  14383  14743  -2572   2023   2384       O  
+ATOM    479  ND2 ASN A  72      -3.368  42.423 -14.779  1.00110.55           N  
+ANISOU  479  ND2 ASN A  72    13627  14329  14050  -3188   2285   2625       N  
+ATOM    480  N   GLN A  73      -4.536  38.230 -12.293  1.00 89.85           N  
+ANISOU  480  N   GLN A  73    10395  11744  12000  -2000   2234   1858       N  
+ATOM    481  CA  GLN A  73      -5.785  37.514 -12.044  1.00 89.22           C  
+ANISOU  481  CA  GLN A  73    10454  11665  11779  -1747   2102   1810       C  
+ATOM    482  C   GLN A  73      -7.009  38.305 -12.501  1.00 94.43           C  
+ANISOU  482  C   GLN A  73    11468  12295  12116  -1785   1904   2025       C  
+ATOM    483  O   GLN A  73      -8.119  37.770 -12.556  1.00 99.87           O  
+ANISOU  483  O   GLN A  73    12283  13015  12647  -1628   1825   1992       O  
+ATOM    484  CB  GLN A  73      -5.911  37.174 -10.557  1.00 72.26           C  
+ANISOU  484  CB  GLN A  73     8203   9338   9916  -1433   1858   1732       C  
+ATOM    485  N   GLY A  74      -6.799  39.578 -12.825  1.00 80.53           N  
+ANISOU  485  N   GLY A  74     9862  10459  10275  -1997   1805   2239       N  
+ATOM    486  CA  GLY A  74      -7.848  40.415 -13.381  1.00 82.19           C  
+ANISOU  486  CA  GLY A  74    10418  10618  10192  -2066   1592   2445       C  
+ATOM    487  C   GLY A  74      -8.427  39.839 -14.660  1.00 93.82           C  
+ANISOU  487  C   GLY A  74    12053  12275  11319  -2199   1771   2421       C  
+ATOM    488  O   GLY A  74      -9.632  39.920 -14.898  1.00 88.18           O  
+ANISOU  488  O   GLY A  74    11566  11528  10410  -2105   1573   2488       O  
+ATOM    489  N   ASN A  75      -7.554  39.271 -15.488  1.00 97.61           N  
+ANISOU  489  N   ASN A  75    12411  12943  11733  -2421   2144   2312       N  
+ATOM    490  CA  ASN A  75      -7.957  38.576 -16.707  1.00 84.99           C  
+ANISOU  490  CA  ASN A  75    10949  11535   9807  -2554   2363   2250       C  
+ATOM    491  C   ASN A  75      -8.976  37.482 -16.410  1.00 71.47           C  
+ANISOU  491  C   ASN A  75     9216   9853   8084  -2251   2291   2102       C  
+ATOM    492  O   ASN A  75     -10.100  37.477 -16.936  1.00 79.36           O  
+ANISOU  492  O   ASN A  75    10469  10856   8829  -2225   2146   2175       O  
+ATOM    493  CB  ASN A  75      -6.735  37.963 -17.394  1.00 80.42           C  
+ANISOU  493  CB  ASN A  75    10155  11157   9243  -2784   2813   2078       C  
+ATOM    494  CG  ASN A  75      -5.764  39.009 -17.901  1.00 78.62           C  
+ANISOU  494  CG  ASN A  75     9968  10935   8968  -3155   2941   2222       C  
+ATOM    495  OD1 ASN A  75      -5.926  40.201 -17.642  1.00 94.75           O  
+ANISOU  495  OD1 ASN A  75    12193  12808  10998  -3227   2667   2459       O  
+ATOM    496  ND2 ASN A  75      -4.741  38.566 -18.623  1.00 77.46           N  
+ANISOU  496  ND2 ASN A  75     9647  10983   8802  -3401   3365   2067       N  
+ATOM    497  N   ARG A  76      -8.547  36.555 -15.557  1.00 71.34           N  
+ANISOU  497  N   ARG A  76     8898   9848   8359  -2032   2378   1893       N  
+ATOM    498  CA  ARG A  76      -9.369  35.458 -15.071  1.00 69.17           C  
+ANISOU  498  CA  ARG A  76     8569   9584   8128  -1745   2311   1740       C  
+ATOM    499  C   ARG A  76     -10.717  35.957 -14.567  1.00 77.92           C  
+ANISOU  499  C   ARG A  76     9883  10554   9168  -1564   1955   1874       C  
+ATOM    500  O   ARG A  76     -11.764  35.428 -14.939  1.00 83.12           O  
+ANISOU  500  O   ARG A  76    10668  11264   9649  -1480   1902   1843       O  
+ATOM    501  CB  ARG A  76      -8.632  34.717 -13.955  1.00 59.90           C  
+ANISOU  501  CB  ARG A  76     7079   8357   7323  -1543   2350   1551       C  
+ATOM    502  CG  ARG A  76      -9.368  33.526 -13.380  1.00 66.63           C  
+ANISOU  502  CG  ARG A  76     7878   9207   8230  -1273   2286   1391       C  
+ATOM    503  CD  ARG A  76      -8.553  32.903 -12.263  1.00 84.47           C  
+ANISOU  503  CD  ARG A  76     9869  11375  10852  -1103   2278   1228       C  
+ATOM    504  NE  ARG A  76      -8.676  31.452 -12.254  1.00 93.59           N  
+ANISOU  504  NE  ARG A  76    10915  12602  12043   -966   2385   1006       N  
+ATOM    505  CZ  ARG A  76      -7.841  30.643 -12.897  1.00102.05           C  
+ANISOU  505  CZ  ARG A  76    11803  13800  13170  -1044   2657    812       C  
+ATOM    506  NH1 ARG A  76      -6.830  31.150 -13.590  1.00102.76           N  
+ANISOU  506  NH1 ARG A  76    11787  13975  13281  -1270   2877    808       N  
+ATOM    507  NH2 ARG A  76      -8.011  29.333 -12.849  1.00104.01           N  
+ANISOU  507  NH2 ARG A  76    11973  14089  13459   -903   2712    611       N  
+ATOM    508  N   GLY A  77     -10.678  36.988 -13.727  1.00 71.01           N  
+ANISOU  508  N   GLY A  77     9031   9500   8448  -1505   1712   2007       N  
+ATOM    509  CA  GLY A  77     -11.886  37.571 -13.173  1.00 66.36           C  
+ANISOU  509  CA  GLY A  77     8607   8770   7838  -1327   1376   2107       C  
+ATOM    510  C   GLY A  77     -12.837  38.117 -14.223  1.00 73.58           C  
+ANISOU  510  C   GLY A  77     9813   9697   8449  -1447   1245   2250       C  
+ATOM    511  O   GLY A  77     -14.050  37.923 -14.132  1.00 66.52           O  
+ANISOU  511  O   GLY A  77     9009   8775   7489  -1282   1069   2230       O  
+ATOM    512  N   ARG A  78     -12.287  38.801 -15.223  1.00 69.80           N  
+ANISOU  512  N   ARG A  78     9486   9249   7787  -1746   1322   2392       N  
+ATOM    513  CA  ARG A  78     -13.095  39.402 -16.280  1.00 59.35           C  
+ANISOU  513  CA  ARG A  78     8489   7903   6156  -1899   1161   2551       C  
+ATOM    514  C   ARG A  78     -13.766  38.347 -17.156  1.00 65.68           C  
+ANISOU  514  C   ARG A  78     9367   8863   6727  -1902   1293   2443       C  
+ATOM    515  O   ARG A  78     -14.978  38.405 -17.402  1.00 81.09           O  
+ANISOU  515  O   ARG A  78    11490  10760   8561  -1803   1053   2480       O  
+ATOM    516  CB  ARG A  78     -12.238  40.329 -17.144  1.00 62.69           C  
+ANISOU  516  CB  ARG A  78     9084   8323   6411  -2267   1238   2732       C  
+ATOM    517  N   ILE A  79     -12.978  37.379 -17.619  1.00 62.12           N  
+ANISOU  517  N   ILE A  79     8774   8598   6231  -2009   1662   2294       N  
+ATOM    518  CA  ILE A  79     -13.510  36.331 -18.488  1.00 69.27           C  
+ANISOU  518  CA  ILE A  79     9754   9655   6910  -2025   1807   2178       C  
+ATOM    519  C   ILE A  79     -14.550  35.501 -17.733  1.00 60.41           C  
+ANISOU  519  C   ILE A  79     8520   8508   5924  -1694   1662   2045       C  
+ATOM    520  O   ILE A  79     -15.633  35.194 -18.264  1.00 71.33           O  
+ANISOU  520  O   ILE A  79    10066   9905   7132  -1648   1534   2046       O  
+ATOM    521  CB  ILE A  79     -12.393  35.420 -19.026  1.00 67.89           C  
+ANISOU  521  CB  ILE A  79     9410   9681   6705  -2177   2243   2002       C  
+ATOM    522  CG1 ILE A  79     -11.498  36.204 -19.987  1.00 69.38           C  
+ANISOU  522  CG1 ILE A  79     9748   9926   6687  -2561   2426   2127       C  
+ATOM    523  CG2 ILE A  79     -12.979  34.215 -19.744  1.00 73.66           C  
+ANISOU  523  CG2 ILE A  79    10191  10553   7243  -2136   2374   1848       C  
+ATOM    524  CD1 ILE A  79     -10.422  35.368 -20.636  1.00 84.57           C  
+ANISOU  524  CD1 ILE A  79    11506  12064   8564  -2739   2886   1930       C  
+ATOM    525  N   ASN A  80     -14.220  35.162 -16.488  1.00 55.14           N  
+ANISOU  525  N   ASN A  80     7589   7793   5568  -1481   1671   1935       N  
+ATOM    526  CA  ASN A  80     -15.158  34.473 -15.613  1.00 56.97           C  
+ANISOU  526  CA  ASN A  80     7723   7985   5937  -1192   1534   1821       C  
+ATOM    527  C   ASN A  80     -16.448  35.265 -15.501  1.00 53.06           C  
+ANISOU  527  C   ASN A  80     7406   7363   5392  -1096   1190   1942       C  
+ATOM    528  O   ASN A  80     -17.530  34.700 -15.567  1.00 56.79           O  
+ANISOU  528  O   ASN A  80     7909   7856   5812   -969   1096   1872       O  
+ATOM    529  CB  ASN A  80     -14.566  34.250 -14.220  1.00 53.75           C  
+ANISOU  529  CB  ASN A  80     7069   7502   5852  -1014   1545   1725       C  
+ATOM    530  CG  ASN A  80     -13.608  33.077 -14.172  1.00 66.05           C  
+ANISOU  530  CG  ASN A  80     8411   9170   7516  -1013   1832   1533       C  
+ATOM    531  OD1 ASN A  80     -13.212  32.542 -15.205  1.00 78.50           O  
+ANISOU  531  OD1 ASN A  80     9999  10892   8936  -1167   2063   1467       O  
+ATOM    532  ND2 ASN A  80     -13.240  32.664 -12.964  1.00 70.71           N  
+ANISOU  532  ND2 ASN A  80     8814   9679   8374   -838   1803   1431       N  
+ATOM    533  N   GLN A  81     -16.323  36.579 -15.343  1.00 53.56           N  
+ANISOU  533  N   GLN A  81     7576   7285   5489  -1157    991   2112       N  
+ATOM    534  CA  GLN A  81     -17.490  37.441 -15.213  1.00 57.32           C  
+ANISOU  534  CA  GLN A  81     8207   7615   5959  -1054    632   2210       C  
+ATOM    535  C   GLN A  81     -18.376  37.370 -16.452  1.00 66.39           C  
+ANISOU  535  C   GLN A  81     9591   8797   6836  -1156    527   2264       C  
+ATOM    536  O   GLN A  81     -19.592  37.226 -16.338  1.00 55.19           O  
+ANISOU  536  O   GLN A  81     8194   7335   5441   -990    321   2213       O  
+ATOM    537  CB  GLN A  81     -17.068  38.888 -14.957  1.00 65.80           C  
+ANISOU  537  CB  GLN A  81     9380   8519   7103  -1132    431   2389       C  
+ATOM    538  CG  GLN A  81     -18.202  39.801 -14.509  1.00 82.30           C  
+ANISOU  538  CG  GLN A  81    11566  10424   9279   -960     38   2445       C  
+ATOM    539  CD  GLN A  81     -18.889  39.318 -13.244  1.00 77.03           C  
+ANISOU  539  CD  GLN A  81    10690   9735   8843   -657     -7   2271       C  
+ATOM    540  OE1 GLN A  81     -18.493  39.680 -12.136  1.00 89.46           O  
+ANISOU  540  OE1 GLN A  81    12147  11221  10624   -545    -37   2247       O  
+ATOM    541  NE2 GLN A  81     -19.937  38.516 -13.403  1.00 73.79           N  
+ANISOU  541  NE2 GLN A  81    10248   9400   8391   -539    -16   2149       N  
+ATOM    542  N   ILE A  82     -17.767  37.480 -17.629  1.00 56.75           N  
+ANISOU  542  N   ILE A  82     8552   7651   5360  -1439    666   2359       N  
+ATOM    543  CA  ILE A  82     -18.516  37.407 -18.884  1.00 58.64           C  
+ANISOU  543  CA  ILE A  82     9066   7912   5302  -1572    561   2421       C  
+ATOM    544  C   ILE A  82     -19.273  36.081 -19.035  1.00 65.40           C  
+ANISOU  544  C   ILE A  82     9834   8891   6125  -1429    652   2239       C  
+ATOM    545  O   ILE A  82     -20.504  36.061 -19.224  1.00 80.78           O  
+ANISOU  545  O   ILE A  82    11874  10773   8046  -1315    391   2233       O  
+ATOM    546  CB  ILE A  82     -17.582  37.589 -20.098  1.00 62.88           C  
+ANISOU  546  CB  ILE A  82     9815   8540   5538  -1936    778   2526       C  
+ATOM    547  CG1 ILE A  82     -17.070  39.029 -20.165  1.00 63.64           C  
+ANISOU  547  CG1 ILE A  82    10086   8485   5609  -2125    611   2749       C  
+ATOM    548  CG2 ILE A  82     -18.299  37.218 -21.388  1.00 68.78           C  
+ANISOU  548  CG2 ILE A  82    10849   9335   5949  -2073    724   2551       C  
+ATOM    549  CD1 ILE A  82     -15.880  39.211 -21.081  1.00 66.59           C  
+ANISOU  549  CD1 ILE A  82    10590   8967   5744  -2504    910   2831       C  
+ATOM    550  N   ILE A  83     -18.540  34.977 -18.907  1.00 61.02           N  
+ANISOU  550  N   ILE A  83     9084   8500   5601  -1426   1001   2080       N  
+ATOM    551  CA  ILE A  83     -19.119  33.645 -19.093  1.00 55.35           C  
+ANISOU  551  CA  ILE A  83     8291   7899   4841  -1316   1108   1905       C  
+ATOM    552  C   ILE A  83     -20.222  33.369 -18.065  1.00 57.77           C  
+ANISOU  552  C   ILE A  83     8443   8130   5375  -1025    903   1816       C  
+ATOM    553  O   ILE A  83     -21.314  32.884 -18.403  1.00 58.49           O  
+ANISOU  553  O   ILE A  83     8591   8230   5401   -948    772   1764       O  
+ATOM    554  CB  ILE A  83     -18.024  32.562 -19.009  1.00 54.96           C  
+ANISOU  554  CB  ILE A  83     8038   8009   4836  -1347   1497   1736       C  
+ATOM    555  CG1 ILE A  83     -17.152  32.609 -20.267  1.00 77.15           C  
+ANISOU  555  CG1 ILE A  83    11009  10935   7369  -1653   1744   1771       C  
+ATOM    556  CG2 ILE A  83     -18.634  31.180 -18.807  1.00 53.29           C  
+ANISOU  556  CG2 ILE A  83     7700   7876   4670  -1172   1561   1543       C  
+ATOM    557  CD1 ILE A  83     -15.879  31.805 -20.169  1.00 80.91           C  
+ANISOU  557  CD1 ILE A  83    11252  11551   7939  -1700   2127   1598       C  
+ATOM    558  N   LEU A  84     -19.932  33.706 -16.814  1.00 55.84           N  
+ANISOU  558  N   LEU A  84     8012   7810   5396   -879    876   1796       N  
+ATOM    559  CA  LEU A  84     -20.878  33.553 -15.717  1.00 61.45           C  
+ANISOU  559  CA  LEU A  84     8577   8451   6320   -628    715   1706       C  
+ATOM    560  C   LEU A  84     -22.148  34.335 -16.012  1.00 67.87           C  
+ANISOU  560  C   LEU A  84     9530   9150   7108   -572    373   1780       C  
+ATOM    561  O   LEU A  84     -23.246  33.806 -15.884  1.00 65.61           O  
+ANISOU  561  O   LEU A  84     9187   8875   6867   -439    275   1677       O  
+ATOM    562  CB  LEU A  84     -20.273  34.003 -14.388  1.00 57.93           C  
+ANISOU  562  CB  LEU A  84     7968   7919   6123   -518    722   1697       C  
+ATOM    563  CG  LEU A  84     -19.385  32.952 -13.718  1.00 63.18           C  
+ANISOU  563  CG  LEU A  84     8437   8662   6905   -475    987   1558       C  
+ATOM    564  CD1 LEU A  84     -19.092  33.318 -12.275  1.00 74.04           C  
+ANISOU  564  CD1 LEU A  84     9680   9925   8527   -332    927   1535       C  
+ATOM    565  CD2 LEU A  84     -20.026  31.585 -13.810  1.00 54.79           C  
+ANISOU  565  CD2 LEU A  84     7313   7705   5800   -397   1083   1401       C  
+ATOM    566  N   ASP A  85     -21.991  35.605 -16.377  1.00 65.01           N  
+ANISOU  566  N   ASP A  85     9341   8665   6695   -674    176   1951       N  
+ATOM    567  CA  ASP A  85     -23.128  36.448 -16.733  1.00 63.56           C  
+ANISOU  567  CA  ASP A  85     9308   8337   6503   -625   -200   2025       C  
+ATOM    568  C   ASP A  85     -23.992  35.826 -17.824  1.00 76.49           C  
+ANISOU  568  C   ASP A  85    11086  10027   7949   -677   -279   1999       C  
+ATOM    569  O   ASP A  85     -25.222  35.857 -17.726  1.00 71.28           O  
+ANISOU  569  O   ASP A  85    10393   9297   7392   -525   -527   1932       O  
+ATOM    570  CB  ASP A  85     -22.653  37.829 -17.188  1.00 58.90           C  
+ANISOU  570  CB  ASP A  85     8946   7601   5831   -786   -397   2237       C  
+ATOM    571  CG  ASP A  85     -22.211  38.705 -16.034  1.00 61.77           C  
+ANISOU  571  CG  ASP A  85     9190   7846   6434   -680   -468   2264       C  
+ATOM    572  OD1 ASP A  85     -22.581  38.403 -14.880  1.00 63.97           O  
+ANISOU  572  OD1 ASP A  85     9239   8125   6944   -453   -446   2117       O  
+ATOM    573  OD2 ASP A  85     -21.491  39.695 -16.282  1.00 59.89           O  
+ANISOU  573  OD2 ASP A  85     9103   7512   6140   -839   -545   2434       O  
+ATOM    574  N   GLU A  86     -23.369  35.268 -18.861  1.00 77.97           N  
+ANISOU  574  N   GLU A  86    11423  10334   7869   -890    -71   2036       N  
+ATOM    575  CA  GLU A  86     -24.160  34.599 -19.896  1.00 65.70           C  
+ANISOU  575  CA  GLU A  86    10020   8828   6117   -943   -141   2002       C  
+ATOM    576  C   GLU A  86     -24.953  33.424 -19.308  1.00 64.86           C  
+ANISOU  576  C   GLU A  86     9672   8807   6166   -734    -73   1798       C  
+ATOM    577  O   GLU A  86     -26.165  33.274 -19.561  1.00 68.19           O  
+ANISOU  577  O   GLU A  86    10114   9176   6616   -641   -312   1750       O  
+ATOM    578  CB  GLU A  86     -23.257  34.110 -21.029  1.00 62.56           C  
+ANISOU  578  CB  GLU A  86     9812   8563   5394  -1211    130   2044       C  
+ATOM    579  N   PHE A  87     -24.269  32.617 -18.498  1.00 57.61           N  
+ANISOU  579  N   PHE A  87     8525   8002   5363   -667    233   1678       N  
+ATOM    580  CA  PHE A  87     -24.908  31.494 -17.812  1.00 71.14           C  
+ANISOU  580  CA  PHE A  87    10020   9787   7222   -494    313   1493       C  
+ATOM    581  C   PHE A  87     -26.145  31.943 -17.035  1.00 74.50           C  
+ANISOU  581  C   PHE A  87    10323  10105   7877   -297     46   1441       C  
+ATOM    582  O   PHE A  87     -27.233  31.397 -17.207  1.00 74.90           O  
+ANISOU  582  O   PHE A  87    10333  10170   7957   -222    -65   1348       O  
+ATOM    583  CB  PHE A  87     -23.924  30.805 -16.865  1.00 72.61           C  
+ANISOU  583  CB  PHE A  87    10001  10055   7534   -446    614   1395       C  
+ATOM    584  CG  PHE A  87     -23.088  29.745 -17.522  1.00 82.40           C  
+ANISOU  584  CG  PHE A  87    11260  11435   8613   -566    901   1326       C  
+ATOM    585  CD1 PHE A  87     -22.748  29.839 -18.862  1.00 99.34           C  
+ANISOU  585  CD1 PHE A  87    13628  13633  10485   -767    952   1400       C  
+ATOM    586  CD2 PHE A  87     -22.653  28.646 -16.801  1.00 84.54           C  
+ANISOU  586  CD2 PHE A  87    11343  11777   9004   -482   1111   1175       C  
+ATOM    587  CE1 PHE A  87     -21.980  28.861 -19.467  1.00107.82           C  
+ANISOU  587  CE1 PHE A  87    14706  14844  11418   -871   1236   1303       C  
+ATOM    588  CE2 PHE A  87     -21.888  27.664 -17.400  1.00 92.77           C  
+ANISOU  588  CE2 PHE A  87    12385  12935   9928   -571   1358   1083       C  
+ATOM    589  CZ  PHE A  87     -21.551  27.772 -18.735  1.00104.51           C  
+ANISOU  589  CZ  PHE A  87    14066  14490  11154   -760   1434   1136       C  
+ATOM    590  N   SER A  88     -25.957  32.948 -16.186  1.00 65.79           N  
+ANISOU  590  N   SER A  88     9155   8896   6946   -219    -51   1489       N  
+ATOM    591  CA  SER A  88     -27.024  33.512 -15.369  1.00 64.24           C  
+ANISOU  591  CA  SER A  88     8828   8595   6986    -30   -283   1417       C  
+ATOM    592  C   SER A  88     -28.168  34.044 -16.220  1.00 77.14           C  
+ANISOU  592  C   SER A  88    10585  10126   8599    -16   -632   1449       C  
+ATOM    593  O   SER A  88     -29.333  33.961 -15.830  1.00 86.18           O  
+ANISOU  593  O   SER A  88    11581  11240   9926    137   -785   1317       O  
+ATOM    594  CB  SER A  88     -26.476  34.627 -14.478  1.00 63.33           C  
+ANISOU  594  CB  SER A  88     8676   8366   7021     27   -343   1480       C  
+ATOM    595  OG  SER A  88     -25.430  34.146 -13.653  1.00 84.29           O  
+ANISOU  595  OG  SER A  88    11218  11090   9717     22    -58   1447       O  
+ATOM    596  N   ARG A  89     -27.834  34.598 -17.381  1.00 77.22           N  
+ANISOU  596  N   ARG A  89    10872  10077   8392   -187   -766   1617       N  
+ATOM    597  CA  ARG A  89     -28.856  35.111 -18.280  1.00 77.03           C  
+ANISOU  597  CA  ARG A  89    11017   9924   8328   -194  -1146   1665       C  
+ATOM    598  C   ARG A  89     -29.547  33.975 -19.026  1.00 80.32           C  
+ANISOU  598  C   ARG A  89    11454  10436   8629   -220  -1121   1576       C  
+ATOM    599  O   ARG A  89     -30.532  34.199 -19.730  1.00 88.66           O  
+ANISOU  599  O   ARG A  89    12619  11386   9681   -204  -1448   1582       O  
+ATOM    600  CB  ARG A  89     -28.250  36.100 -19.279  1.00 67.14           C  
+ANISOU  600  CB  ARG A  89    10111   8556   6845   -403  -1316   1893       C  
+ATOM    601  N   LYS A  90     -29.042  32.754 -18.860  1.00 73.35           N  
+ANISOU  601  N   LYS A  90    10468   9735   7669   -253   -763   1487       N  
+ATOM    602  CA  LYS A  90     -29.626  31.607 -19.561  1.00 68.56           C  
+ANISOU  602  CA  LYS A  90     9888   9219   6944   -285   -728   1400       C  
+ATOM    603  C   LYS A  90     -30.248  30.515 -18.672  1.00 73.72           C  
+ANISOU  603  C   LYS A  90    10243   9972   7793   -133   -579   1198       C  
+ATOM    604  O   LYS A  90     -30.710  29.501 -19.191  1.00 85.32           O  
+ANISOU  604  O   LYS A  90    11723  11516   9178   -160   -543   1120       O  
+ATOM    605  CB  LYS A  90     -28.568  30.964 -20.460  1.00 66.34           C  
+ANISOU  605  CB  LYS A  90     9804   9058   6343   -493   -460   1462       C  
+ATOM    606  N   VAL A  91     -30.292  30.715 -17.357  1.00 72.35           N  
+ANISOU  606  N   VAL A  91     9829   9794   7867      9   -502   1114       N  
+ATOM    607  CA  VAL A  91     -30.778  29.661 -16.460  1.00 69.23           C  
+ANISOU  607  CA  VAL A  91     9186   9497   7622    109   -328    934       C  
+ATOM    608  C   VAL A  91     -32.113  30.008 -15.807  1.00 73.50           C  
+ANISOU  608  C   VAL A  91     9518   9973   8435    267   -529    803       C  
+ATOM    609  O   VAL A  91     -32.462  31.180 -15.679  1.00 75.56           O  
+ANISOU  609  O   VAL A  91     9776  10106   8829    344   -769    834       O  
+ATOM    610  CB  VAL A  91     -29.761  29.351 -15.338  1.00 65.61           C  
+ANISOU  610  CB  VAL A  91     8611   9102   7216    127    -27    904       C  
+ATOM    611  CG1 VAL A  91     -28.480  28.773 -15.916  1.00 62.25           C  
+ANISOU  611  CG1 VAL A  91     8320   8759   6571    -14    206    973       C  
+ATOM    612  CG2 VAL A  91     -29.476  30.598 -14.514  1.00 66.76           C  
+ANISOU  612  CG2 VAL A  91     8711   9141   7512    204   -109    956       C  
+ATOM    613  N   ASP A  92     -32.844  28.981 -15.370  1.00 74.41           N  
+ANISOU  613  N   ASP A  92     9451  10175   8645    310   -425    643       N  
+ATOM    614  CA  ASP A  92     -34.116  29.187 -14.680  1.00 78.39           C  
+ANISOU  614  CA  ASP A  92     9713  10649   9424    443   -552    480       C  
+ATOM    615  C   ASP A  92     -34.444  28.064 -13.702  1.00 78.15           C  
+ANISOU  615  C   ASP A  92     9476  10739   9478    453   -293    318       C  
+ATOM    616  O   ASP A  92     -33.879  26.974 -13.774  1.00 74.49           O  
+ANISOU  616  O   ASP A  92     9074  10369   8860    362    -79    329       O  
+ATOM    617  CB  ASP A  92     -35.263  29.266 -15.698  1.00 81.20           C  
+ANISOU  617  CB  ASP A  92    10088  10937   9828    458   -873    449       C  
+ATOM    618  CG  ASP A  92     -35.184  30.484 -16.590  1.00 91.17           C  
+ANISOU  618  CG  ASP A  92    11564  12039  11038    452  -1207    597       C  
+ATOM    619  OD1 ASP A  92     -35.189  31.616 -16.064  1.00105.07           O  
+ANISOU  619  OD1 ASP A  92    13275  13692  12956    548  -1340    606       O  
+ATOM    620  OD2 ASP A  92     -35.116  30.304 -17.825  1.00 81.65           O  
+ANISOU  620  OD2 ASP A  92    10599  10804   9621    342  -1345    705       O  
+ATOM    621  N   LEU A  93     -35.377  28.341 -12.797  1.00 80.31           N  
+ANISOU  621  N   LEU A  93     9511  11004   9999    555   -319    156       N  
+ATOM    622  CA  LEU A  93     -35.783  27.371 -11.789  1.00 77.38           C  
+ANISOU  622  CA  LEU A  93     8957  10740   9704    536    -74     -1       C  
+ATOM    623  C   LEU A  93     -36.787  26.418 -12.428  1.00 79.12           C  
+ANISOU  623  C   LEU A  93     9098  11016   9946    489   -137    -93       C  
+ATOM    624  O   LEU A  93     -37.633  26.845 -13.214  1.00 82.50           O  
+ANISOU  624  O   LEU A  93     9490  11379  10477    537   -414   -119       O  
+ATOM    625  CB  LEU A  93     -36.380  28.065 -10.563  1.00 76.38           C  
+ANISOU  625  CB  LEU A  93     8611  10595   9817    641    -42   -156       C  
+ATOM    626  CG  LEU A  93     -36.669  27.205  -9.330  1.00 80.65           C  
+ANISOU  626  CG  LEU A  93     9002  11240  10402    589    248   -310       C  
+ATOM    627  CD1 LEU A  93     -35.374  26.778  -8.651  1.00 75.38           C  
+ANISOU  627  CD1 LEU A  93     8496  10591   9555    518    481   -208       C  
+ATOM    628  CD2 LEU A  93     -37.565  27.952  -8.354  1.00 83.29           C  
+ANISOU  628  CD2 LEU A  93     9095  11562  10988    689    249   -507       C  
+ATOM    629  N   THR A  94     -36.702  25.133 -12.102  1.00 79.82           N  
+ANISOU  629  N   THR A  94     9173  11207   9948    392     88   -142       N  
+ATOM    630  CA  THR A  94     -37.607  24.157 -12.696  1.00 76.51           C  
+ANISOU  630  CA  THR A  94     8690  10838   9543    332     30   -223       C  
+ATOM    631  C   THR A  94     -38.329  23.333 -11.637  1.00 72.59           C  
+ANISOU  631  C   THR A  94     7983  10430   9169    279    231   -395       C  
+ATOM    632  O   THR A  94     -37.941  23.326 -10.467  1.00 67.65           O  
+ANISOU  632  O   THR A  94     7320   9833   8551    264    447   -431       O  
+ATOM    633  CB  THR A  94     -36.863  23.195 -13.650  1.00 75.80           C  
+ANISOU  633  CB  THR A  94     8835  10777   9189    230     71   -108       C  
+ATOM    634  OG1 THR A  94     -36.030  22.312 -12.890  1.00 72.40           O  
+ANISOU  634  OG1 THR A  94     8451  10408   8648    160    349   -105       O  
+ATOM    635  CG2 THR A  94     -36.006  23.970 -14.641  1.00 77.13           C  
+ANISOU  635  CG2 THR A  94     9239  10877   9190    238    -62     64       C  
+ATOM    636  N   GLU A  95     -39.383  22.643 -12.064  1.00 74.88           N  
+ANISOU  636  N   GLU A  95     8151  10755   9545    234    150   -498       N  
+ATOM    637  CA  GLU A  95     -40.143  21.746 -11.199  1.00 71.86           C  
+ANISOU  637  CA  GLU A  95     7578  10463   9261    140    340   -659       C  
+ATOM    638  C   GLU A  95     -39.257  20.643 -10.631  1.00 73.87           C  
+ANISOU  638  C   GLU A  95     7996  10768   9304     13    596   -598       C  
+ATOM    639  O   GLU A  95     -39.518  20.128  -9.543  1.00 89.86           O  
+ANISOU  639  O   GLU A  95     9931  12848  11363    -78    804   -696       O  
+ATOM    640  CB  GLU A  95     -41.320  21.135 -11.961  1.00 75.55           C  
+ANISOU  640  CB  GLU A  95     7914  10946   9844     99    176   -755       C  
+ATOM    641  CG  GLU A  95     -42.684  21.572 -11.456  1.00 96.26           C  
+ANISOU  641  CG  GLU A  95    10186  13591  12796    140    131   -974       C  
+ATOM    642  CD  GLU A  95     -43.050  20.915 -10.138  1.00 99.47           C  
+ANISOU  642  CD  GLU A  95    10429  14109  13255     12    454  -1121       C  
+ATOM    643  OE1 GLU A  95     -42.882  19.683 -10.023  1.00104.54           O  
+ANISOU  643  OE1 GLU A  95    11171  14806  13742   -145    603  -1090       O  
+ATOM    644  OE2 GLU A  95     -43.511  21.628  -9.222  1.00 89.96           O  
+ANISOU  644  OE2 GLU A  95     9010  12932  12240     59    556  -1272       O  
+ATOM    645  N   ASN A  96     -38.232  20.260 -11.389  1.00 66.37           N  
+ANISOU  645  N   ASN A  96     7292   9789   8135     -1    571   -448       N  
+ATOM    646  CA  ASN A  96     -37.241  19.300 -10.912  1.00 60.72           C  
+ANISOU  646  CA  ASN A  96     6738   9089   7242    -90    769   -394       C  
+ATOM    647  C   ASN A  96     -36.602  19.749  -9.601  1.00 60.47           C  
+ANISOU  647  C   ASN A  96     6709   9043   7225    -79    945   -392       C  
+ATOM    648  O   ASN A  96     -36.502  18.968  -8.651  1.00 70.64           O  
+ANISOU  648  O   ASN A  96     8018  10348   8475   -181   1115   -437       O  
+ATOM    649  CB  ASN A  96     -36.152  19.080 -11.965  1.00 59.97           C  
+ANISOU  649  CB  ASN A  96     6876   8964   6945    -78    715   -258       C  
+ATOM    650  CG  ASN A  96     -36.675  18.409 -13.219  1.00 64.59           C  
+ANISOU  650  CG  ASN A  96     7518   9561   7463   -116    564   -263       C  
+ATOM    651  OD1 ASN A  96     -37.613  17.617 -13.165  1.00 66.50           O  
+ANISOU  651  OD1 ASN A  96     7659   9834   7774   -185    546   -359       O  
+ATOM    652  ND2 ASN A  96     -36.054  18.709 -14.355  1.00 73.11           N  
+ANISOU  652  ND2 ASN A  96     8772  10612   8393    -87    459   -161       N  
+ATOM    653  N   HIS A  97     -36.179  21.011  -9.559  1.00 56.62           N  
+ANISOU  653  N   HIS A  97     6223   8508   6783     35    883   -334       N  
+ATOM    654  CA  HIS A  97     -35.573  21.590  -8.362  1.00 54.73           C  
+ANISOU  654  CA  HIS A  97     5994   8236   6564     62   1015   -329       C  
+ATOM    655  C   HIS A  97     -36.526  21.547  -7.176  1.00 53.68           C  
+ANISOU  655  C   HIS A  97     5687   8149   6561     12   1147   -493       C  
+ATOM    656  O   HIS A  97     -36.116  21.274  -6.051  1.00 52.70           O  
+ANISOU  656  O   HIS A  97     5626   8016   6382    -55   1318   -510       O  
+ATOM    657  CB  HIS A  97     -35.140  23.040  -8.607  1.00 55.73           C  
+ANISOU  657  CB  HIS A  97     6134   8296   6745    194    887   -249       C  
+ATOM    658  CG  HIS A  97     -34.052  23.193  -9.625  1.00 58.90           C  
+ANISOU  658  CG  HIS A  97     6724   8657   6997    209    807    -85       C  
+ATOM    659  ND1 HIS A  97     -34.271  23.733 -10.874  1.00 61.84           N  
+ANISOU  659  ND1 HIS A  97     7138   9006   7351    248    603    -19       N  
+ATOM    660  CD2 HIS A  97     -32.732  22.896  -9.570  1.00 52.94           C  
+ANISOU  660  CD2 HIS A  97     6126   7880   6109    179    909     14       C  
+ATOM    661  CE1 HIS A  97     -33.135  23.753 -11.548  1.00 59.56           C  
+ANISOU  661  CE1 HIS A  97     7032   8698   6898    222    614    115       C  
+ATOM    662  NE2 HIS A  97     -32.186  23.250 -10.780  1.00 53.60           N  
+ANISOU  662  NE2 HIS A  97     6326   7948   6090    189    803    127       N  
+ATOM    663  N   LYS A  98     -37.797  21.828  -7.438  1.00 60.24           N  
+ANISOU  663  N   LYS A  98     6301   9021   7566     39   1061   -621       N  
+ATOM    664  CA  LYS A  98     -38.814  21.872  -6.393  1.00 57.94           C  
+ANISOU  664  CA  LYS A  98     5798   8792   7425    -13   1204   -814       C  
+ATOM    665  C   LYS A  98     -39.122  20.485  -5.827  1.00 69.81           C  
+ANISOU  665  C   LYS A  98     7326  10363   8837   -215   1397   -873       C  
+ATOM    666  O   LYS A  98     -39.183  20.299  -4.607  1.00 83.73           O  
+ANISOU  666  O   LYS A  98     9091  12152  10569   -320   1608   -951       O  
+ATOM    667  CB  LYS A  98     -40.084  22.522  -6.943  1.00 59.65           C  
+ANISOU  667  CB  LYS A  98     5745   9026   7894     80   1033   -955       C  
+ATOM    668  CG  LYS A  98     -39.919  24.009  -7.211  1.00 69.24           C  
+ANISOU  668  CG  LYS A  98     6926  10151   9230    271    838   -929       C  
+ATOM    669  CD  LYS A  98     -41.062  24.579  -8.031  1.00 77.13           C  
+ANISOU  669  CD  LYS A  98     7706  11124  10477    377    576  -1040       C  
+ATOM    670  CE  LYS A  98     -41.010  26.100  -8.044  1.00 88.05           C  
+ANISOU  670  CE  LYS A  98     9040  12401  12013    563    382  -1050       C  
+ATOM    671  NZ  LYS A  98     -42.046  26.696  -8.932  1.00 97.12           N  
+ANISOU  671  NZ  LYS A  98    10008  13481  13411    681     55  -1145       N  
+ATOM    672  N   ILE A  99     -39.306  19.515  -6.720  1.00 54.18           N  
+ANISOU  672  N   ILE A  99     5390   8401   6797   -282   1314   -833       N  
+ATOM    673  CA  ILE A  99     -39.534  18.130  -6.320  1.00 53.60           C  
+ANISOU  673  CA  ILE A  99     5375   8368   6624   -481   1454   -866       C  
+ATOM    674  C   ILE A  99     -38.347  17.609  -5.520  1.00 61.44           C  
+ANISOU  674  C   ILE A  99     6628   9301   7414   -557   1585   -763       C  
+ATOM    675  O   ILE A  99     -38.521  16.989  -4.471  1.00 62.31           O  
+ANISOU  675  O   ILE A  99     6786   9427   7464   -723   1759   -820       O  
+ATOM    676  CB  ILE A  99     -39.770  17.218  -7.536  1.00 57.58           C  
+ANISOU  676  CB  ILE A  99     5918   8874   7084   -515   1302   -822       C  
+ATOM    677  CG1 ILE A  99     -41.021  17.657  -8.296  1.00 60.20           C  
+ANISOU  677  CG1 ILE A  99     5995   9243   7634   -454   1137   -932       C  
+ATOM    678  CG2 ILE A  99     -39.891  15.764  -7.102  1.00 54.07           C  
+ANISOU  678  CG2 ILE A  99     5570   8448   6527   -724   1424   -840       C  
+ATOM    679  CD1 ILE A  99     -41.163  16.993  -9.640  1.00 64.07           C  
+ANISOU  679  CD1 ILE A  99     6560   9712   8072   -454    934   -872       C  
+ATOM    680  N   LEU A 100     -37.142  17.872  -6.017  1.00 59.33           N  
+ANISOU  680  N   LEU A 100     6535   8959   7047   -446   1494   -617       N  
+ATOM    681  CA  LEU A 100     -35.925  17.475  -5.316  1.00 60.00           C  
+ANISOU  681  CA  LEU A 100     6850   8964   6984   -486   1575   -527       C  
+ATOM    682  C   LEU A 100     -35.848  18.134  -3.943  1.00 57.91           C  
+ANISOU  682  C   LEU A 100     6586   8679   6738   -507   1713   -573       C  
+ATOM    683  O   LEU A 100     -35.404  17.522  -2.973  1.00 61.53           O  
+ANISOU  683  O   LEU A 100     7210   9083   7085   -630   1816   -561       O  
+ATOM    684  CB  LEU A 100     -34.682  17.830  -6.134  1.00 49.10           C  
+ANISOU  684  CB  LEU A 100     5597   7519   5540   -352   1462   -390       C  
+ATOM    685  CG  LEU A 100     -34.382  16.956  -7.352  1.00 47.31           C  
+ANISOU  685  CG  LEU A 100     5457   7294   5226   -357   1365   -340       C  
+ATOM    686  CD1 LEU A 100     -33.281  17.578  -8.196  1.00 47.51           C  
+ANISOU  686  CD1 LEU A 100     5566   7282   5202   -233   1288   -231       C  
+ATOM    687  CD2 LEU A 100     -33.997  15.556  -6.907  1.00 41.85           C  
+ANISOU  687  CD2 LEU A 100     4918   6555   4430   -486   1422   -348       C  
+ATOM    688  N   ALA A 101     -36.277  19.389  -3.873  1.00 51.41           N  
+ANISOU  688  N   ALA A 101     5597   7883   6054   -388   1693   -630       N  
+ATOM    689  CA  ALA A 101     -36.254  20.133  -2.621  1.00 56.52           C  
+ANISOU  689  CA  ALA A 101     6238   8513   6725   -389   1819   -694       C  
+ATOM    690  C   ALA A 101     -37.264  19.583  -1.616  1.00 66.34           C  
+ANISOU  690  C   ALA A 101     7407   9832   7966   -579   2022   -855       C  
+ATOM    691  O   ALA A 101     -37.047  19.672  -0.408  1.00 64.61           O  
+ANISOU  691  O   ALA A 101     7299   9583   7665   -667   2170   -890       O  
+ATOM    692  CB  ALA A 101     -36.514  21.609  -2.882  1.00 44.23           C  
+ANISOU  692  CB  ALA A 101     4513   6957   5337   -201   1721   -732       C  
+ATOM    693  N   ARG A 102     -38.362  19.010  -2.107  1.00 66.45           N  
+ANISOU  693  N   ARG A 102     7247   9940   8063   -660   2032   -955       N  
+ATOM    694  CA  ARG A 102     -39.351  18.413  -1.208  1.00 65.10           C  
+ANISOU  694  CA  ARG A 102     6992   9855   7887   -878   2248  -1113       C  
+ATOM    695  C   ARG A 102     -38.950  17.004  -0.754  1.00 76.18           C  
+ANISOU  695  C   ARG A 102     8659  11213   9072  -1108   2323  -1034       C  
+ATOM    696  O   ARG A 102     -39.481  16.491   0.230  1.00 80.29           O  
+ANISOU  696  O   ARG A 102     9216  11774   9515  -1334   2522  -1127       O  
+ATOM    697  CB  ARG A 102     -40.742  18.367  -1.857  1.00 55.73           C  
+ANISOU  697  CB  ARG A 102     5482   8782   6910   -889   2226  -1270       C  
+ATOM    698  CG  ARG A 102     -41.387  19.733  -2.084  1.00 51.88           C  
+ANISOU  698  CG  ARG A 102     4704   8329   6678   -688   2154  -1406       C  
+ATOM    699  CD  ARG A 102     -42.839  19.593  -2.543  1.00 56.09           C  
+ANISOU  699  CD  ARG A 102     4896   8965   7450   -723   2140  -1599       C  
+ATOM    700  NE  ARG A 102     -42.970  19.180  -3.937  1.00 66.28           N  
+ANISOU  700  NE  ARG A 102     6166  10228   8788   -656   1885  -1507       N  
+ATOM    701  CZ  ARG A 102     -43.040  20.018  -4.965  1.00 59.29           C  
+ANISOU  701  CZ  ARG A 102     5186   9290   8051   -440   1618  -1478       C  
+ATOM    702  NH1 ARG A 102     -42.997  21.325  -4.762  1.00 64.64           N  
+ANISOU  702  NH1 ARG A 102     5764   9929   8866   -261   1555  -1533       N  
+ATOM    703  NH2 ARG A 102     -43.162  19.545  -6.198  1.00 60.90           N  
+ANISOU  703  NH2 ARG A 102     5417   9465   8256   -413   1397  -1394       N  
+ATOM    704  N   LEU A 103     -38.011  16.386  -1.464  1.00 71.97           N  
+ANISOU  704  N   LEU A 103     8317  10590   8438  -1059   2163   -871       N  
+ATOM    705  CA  LEU A 103     -37.540  15.046  -1.114  1.00 54.51           C  
+ANISOU  705  CA  LEU A 103     6369   8301   6043  -1247   2176   -796       C  
+ATOM    706  C   LEU A 103     -36.550  15.076   0.048  1.00 57.77           C  
+ANISOU  706  C   LEU A 103     7057   8591   6303  -1303   2230   -727       C  
+ATOM    707  O   LEU A 103     -35.820  16.052   0.221  1.00 52.97           O  
+ANISOU  707  O   LEU A 103     6471   7932   5725  -1140   2193   -682       O  
+ATOM    708  CB  LEU A 103     -36.901  14.369  -2.330  1.00 55.54           C  
+ANISOU  708  CB  LEU A 103     6584   8374   6144  -1157   1978   -682       C  
+ATOM    709  CG  LEU A 103     -37.843  14.025  -3.484  1.00 53.16           C  
+ANISOU  709  CG  LEU A 103     6088   8163   5945  -1146   1893   -734       C  
+ATOM    710  CD1 LEU A 103     -37.084  13.364  -4.625  1.00 44.88           C  
+ANISOU  710  CD1 LEU A 103     5170   7050   4831  -1060   1714   -629       C  
+ATOM    711  CD2 LEU A 103     -38.977  13.134  -2.999  1.00 54.83           C  
+ANISOU  711  CD2 LEU A 103     6238   8442   6155  -1396   2013   -841       C  
+ATOM    712  N   PRO A 104     -36.523  14.002   0.857  1.00 62.85           N  
+ANISOU  712  N   PRO A 104     7930   9168   6782  -1546   2295   -714       N  
+ATOM    713  CA  PRO A 104     -35.597  13.937   1.994  1.00 58.15           C  
+ANISOU  713  CA  PRO A 104     7639   8424   6030  -1622   2306   -645       C  
+ATOM    714  C   PRO A 104     -34.148  13.681   1.578  1.00 57.69           C  
+ANISOU  714  C   PRO A 104     7771   8200   5948  -1472   2089   -500       C  
+ATOM    715  O   PRO A 104     -33.485  12.811   2.144  1.00 62.63           O  
+ANISOU  715  O   PRO A 104     8682   8669   6444  -1592   2009   -434       O  
+ATOM    716  CB  PRO A 104     -36.140  12.765   2.815  1.00 52.69           C  
+ANISOU  716  CB  PRO A 104     7144   7706   5168  -1953   2408   -673       C  
+ATOM    717  CG  PRO A 104     -36.799  11.887   1.811  1.00 56.55           C  
+ANISOU  717  CG  PRO A 104     7503   8267   5718  -2001   2349   -690       C  
+ATOM    718  CD  PRO A 104     -37.394  12.814   0.787  1.00 65.88           C  
+ANISOU  718  CD  PRO A 104     8316   9599   7115  -1781   2344   -763       C  
+ATOM    719  N   ILE A 105     -33.668  14.438   0.597  1.00 55.30           N  
+ANISOU  719  N   ILE A 105     7309   7926   5776  -1220   1988   -461       N  
+ATOM    720  CA  ILE A 105     -32.281  14.353   0.162  1.00 45.62           C  
+ANISOU  720  CA  ILE A 105     6208   6567   4558  -1070   1819   -351       C  
+ATOM    721  C   ILE A 105     -31.450  15.419   0.868  1.00 55.09           C  
+ANISOU  721  C   ILE A 105     7468   7686   5778   -961   1814   -309       C  
+ATOM    722  O   ILE A 105     -31.780  16.604   0.817  1.00 65.94           O  
+ANISOU  722  O   ILE A 105     8671   9144   7239   -851   1875   -340       O  
+ATOM    723  CB  ILE A 105     -32.158  14.521  -1.363  1.00 58.41           C  
+ANISOU  723  CB  ILE A 105     7650   8264   6280   -891   1725   -328       C  
+ATOM    724  CG1 ILE A 105     -32.852  13.360  -2.078  1.00 62.32           C  
+ANISOU  724  CG1 ILE A 105     8123   8809   6745   -994   1695   -364       C  
+ATOM    725  CG2 ILE A 105     -30.695  14.625  -1.777  1.00 39.28           C  
+ANISOU  725  CG2 ILE A 105     5317   5728   3881   -737   1599   -241       C  
+ATOM    726  CD1 ILE A 105     -32.914  13.515  -3.578  1.00 72.09           C  
+ANISOU  726  CD1 ILE A 105     9207  10128   8054   -847   1609   -355       C  
+ATOM    727  N   HIS A 106     -30.374  14.999   1.525  1.00 45.51           N  
+ANISOU  727  N   HIS A 106     6501   6290   4500   -988   1715   -242       N  
+ATOM    728  CA  HIS A 106     -29.568  15.918   2.321  1.00 52.84           C  
+ANISOU  728  CA  HIS A 106     7519   7114   5443   -909   1689   -201       C  
+ATOM    729  C   HIS A 106     -28.199  16.206   1.708  1.00 54.34           C  
+ANISOU  729  C   HIS A 106     7698   7206   5743   -714   1532   -119       C  
+ATOM    730  O   HIS A 106     -27.418  16.979   2.264  1.00 50.22           O  
+ANISOU  730  O   HIS A 106     7236   6586   5261   -635   1484    -76       O  
+ATOM    731  CB  HIS A 106     -29.399  15.373   3.741  1.00 47.94           C  
+ANISOU  731  CB  HIS A 106     7209   6337   4668  -1107   1685   -196       C  
+ATOM    732  CG  HIS A 106     -30.688  14.974   4.388  1.00 62.00           C  
+ANISOU  732  CG  HIS A 106     9026   8215   6316  -1347   1868   -283       C  
+ATOM    733  ND1 HIS A 106     -31.659  15.889   4.735  1.00 64.04           N  
+ANISOU  733  ND1 HIS A 106     9116   8626   6588  -1365   2068   -383       N  
+ATOM    734  CD2 HIS A 106     -31.170  13.760   4.748  1.00 67.24           C  
+ANISOU  734  CD2 HIS A 106     9865   8843   6839  -1589   1886   -296       C  
+ATOM    735  CE1 HIS A 106     -32.682  15.257   5.282  1.00 60.79           C  
+ANISOU  735  CE1 HIS A 106     8755   8286   6054  -1615   2229   -466       C  
+ATOM    736  NE2 HIS A 106     -32.411  13.965   5.301  1.00 56.47           N  
+ANISOU  736  NE2 HIS A 106     8428   7626   5401  -1766   2121   -402       N  
+ATOM    737  N   THR A 107     -27.905  15.591   0.566  1.00 45.87           N  
+ANISOU  737  N   THR A 107     6546   6161   4721   -646   1462   -108       N  
+ATOM    738  CA  THR A 107     -26.616  15.811  -0.081  1.00 44.61           C  
+ANISOU  738  CA  THR A 107     6351   5930   4669   -482   1351    -57       C  
+ATOM    739  C   THR A 107     -26.734  16.129  -1.571  1.00 54.03           C  
+ANISOU  739  C   THR A 107     7331   7274   5922   -363   1377    -56       C  
+ATOM    740  O   THR A 107     -27.211  15.317  -2.375  1.00 63.10           O  
+ANISOU  740  O   THR A 107     8443   8495   7037   -398   1378    -93       O  
+ATOM    741  CB  THR A 107     -25.686  14.600   0.093  1.00 41.76           C  
+ANISOU  741  CB  THR A 107     6168   5389   4311   -514   1202    -59       C  
+ATOM    742  OG1 THR A 107     -25.486  14.351   1.490  1.00 53.90           O  
+ANISOU  742  OG1 THR A 107     7949   6751   5778   -633   1135    -43       O  
+ATOM    743  CG2 THR A 107     -24.339  14.873  -0.559  1.00 37.13           C  
+ANISOU  743  CG2 THR A 107     5499   4741   3868   -344   1114    -40       C  
+ATOM    744  N   TYR A 108     -26.274  17.324  -1.921  1.00 57.16           N  
+ANISOU  744  N   TYR A 108     7616   7705   6399   -234   1384     -8       N  
+ATOM    745  CA  TYR A 108     -26.213  17.773  -3.303  1.00 46.98           C  
+ANISOU  745  CA  TYR A 108     6173   6533   5146   -136   1393     13       C  
+ATOM    746  C   TYR A 108     -24.777  18.091  -3.678  1.00 46.57           C  
+ANISOU  746  C   TYR A 108     6112   6409   5175    -39   1347     59       C  
+ATOM    747  O   TYR A 108     -24.112  18.862  -3.001  1.00 52.10           O  
+ANISOU  747  O   TYR A 108     6834   7022   5942      5   1319    104       O  
+ATOM    748  CB  TYR A 108     -27.079  19.016  -3.529  1.00 41.80           C  
+ANISOU  748  CB  TYR A 108     5383   5989   4511    -90   1435     30       C  
+ATOM    749  CG  TYR A 108     -28.572  18.794  -3.459  1.00 53.75           C  
+ANISOU  749  CG  TYR A 108     6827   7605   5988   -168   1489    -43       C  
+ATOM    750  CD1 TYR A 108     -29.247  18.841  -2.247  1.00 60.40           C  
+ANISOU  750  CD1 TYR A 108     7706   8432   6813   -256   1559   -100       C  
+ATOM    751  CD2 TYR A 108     -29.311  18.566  -4.613  1.00 41.83           C  
+ANISOU  751  CD2 TYR A 108     5216   6210   4468   -164   1473    -65       C  
+ATOM    752  CE1 TYR A 108     -30.615  18.649  -2.184  1.00 38.16           C  
+ANISOU  752  CE1 TYR A 108     4789   5722   3989   -339   1632   -190       C  
+ATOM    753  CE2 TYR A 108     -30.679  18.374  -4.560  1.00 53.27           C  
+ANISOU  753  CE2 TYR A 108     6570   7747   5922   -233   1510   -145       C  
+ATOM    754  CZ  TYR A 108     -31.326  18.417  -3.344  1.00 52.62           C  
+ANISOU  754  CZ  TYR A 108     6489   7659   5844   -321   1599   -214       C  
+ATOM    755  OH  TYR A 108     -32.687  18.225  -3.288  1.00 50.51           O  
+ANISOU  755  OH  TYR A 108     6094   7492   5606   -403   1659   -317       O  
+ATOM    756  N   TRP A 109     -24.302  17.475  -4.749  1.00 51.49           N  
+ANISOU  756  N   TRP A 109     6698   7069   5796    -13   1345     33       N  
+ATOM    757  CA  TRP A 109     -23.053  17.860  -5.381  1.00 44.05           C  
+ANISOU  757  CA  TRP A 109     5696   6109   4931     67   1348     53       C  
+ATOM    758  C   TRP A 109     -23.381  18.518  -6.705  1.00 54.91           C  
+ANISOU  758  C   TRP A 109     6977   7638   6247     87   1408     90       C  
+ATOM    759  O   TRP A 109     -24.305  18.097  -7.398  1.00 63.04           O  
+ANISOU  759  O   TRP A 109     8001   8767   7185     52   1420     62       O  
+ATOM    760  CB  TRP A 109     -22.139  16.652  -5.588  1.00 45.37           C  
+ANISOU  760  CB  TRP A 109     5897   6191   5149     77   1310    -34       C  
+ATOM    761  CG  TRP A 109     -21.468  16.205  -4.336  1.00 54.45           C  
+ANISOU  761  CG  TRP A 109     7155   7144   6392     73   1199    -54       C  
+ATOM    762  CD1 TRP A 109     -21.975  15.376  -3.379  1.00 57.45           C  
+ANISOU  762  CD1 TRP A 109     7690   7417   6720    -11   1119    -76       C  
+ATOM    763  CD2 TRP A 109     -20.157  16.573  -3.896  1.00 44.14           C  
+ANISOU  763  CD2 TRP A 109     5824   5703   5242    140   1136    -51       C  
+ATOM    764  NE1 TRP A 109     -21.058  15.204  -2.370  1.00 50.70           N  
+ANISOU  764  NE1 TRP A 109     6939   6357   5966      2    990    -80       N  
+ATOM    765  CE2 TRP A 109     -19.933  15.928  -2.665  1.00 47.86           C  
+ANISOU  765  CE2 TRP A 109     6457   5974   5752    105    990    -70       C  
+ATOM    766  CE3 TRP A 109     -19.149  17.383  -4.428  1.00 43.23           C  
+ANISOU  766  CE3 TRP A 109     5573   5612   5241    211   1182    -33       C  
+ATOM    767  CZ2 TRP A 109     -18.745  16.072  -1.953  1.00 54.27           C  
+ANISOU  767  CZ2 TRP A 109     7293   6597   6729    159    862    -76       C  
+ATOM    768  CZ3 TRP A 109     -17.970  17.525  -3.721  1.00 49.41           C  
+ANISOU  768  CZ3 TRP A 109     6348   6223   6202    260   1081    -46       C  
+ATOM    769  CH2 TRP A 109     -17.778  16.872  -2.497  1.00 60.05           C  
+ANISOU  769  CH2 TRP A 109     7854   7361   7602    244    910    -69       C  
+ATOM    770  N   THR A 110     -22.638  19.559  -7.055  1.00 52.54           N  
+ANISOU  770  N   THR A 110     6621   7348   5994    131   1429    157       N  
+ATOM    771  CA  THR A 110     -22.865  20.221  -8.329  1.00 44.47           C  
+ANISOU  771  CA  THR A 110     5555   6450   4890    125   1467    208       C  
+ATOM    772  C   THR A 110     -21.622  20.946  -8.820  1.00 57.24           C  
+ANISOU  772  C   THR A 110     7131   8063   6556    136   1517    257       C  
+ATOM    773  O   THR A 110     -20.761  21.341  -8.032  1.00 44.12           O  
+ANISOU  773  O   THR A 110     5445   6298   5019    167   1499    278       O  
+ATOM    774  CB  THR A 110     -24.032  21.223  -8.241  1.00 47.80           C  
+ANISOU  774  CB  THR A 110     5963   6917   5283    131   1412    275       C  
+ATOM    775  OG1 THR A 110     -24.239  21.828  -9.523  1.00 55.86           O  
+ANISOU  775  OG1 THR A 110     6981   8029   6215    115   1403    333       O  
+ATOM    776  CG2 THR A 110     -23.731  22.307  -7.218  1.00 42.51           C  
+ANISOU  776  CG2 THR A 110     5282   6157   4713    174   1372    337       C  
+ATOM    777  N   THR A 111     -21.535  21.109 -10.133  1.00 51.10           N  
+ANISOU  777  N   THR A 111     6353   7393   5671     94   1580    273       N  
+ATOM    778  CA  THR A 111     -20.479  21.903 -10.737  1.00 45.75           C  
+ANISOU  778  CA  THR A 111     5643   6736   5005     62   1654    328       C  
+ATOM    779  C   THR A 111     -21.069  23.201 -11.272  1.00 44.83           C  
+ANISOU  779  C   THR A 111     5576   6662   4796     26   1595    466       C  
+ATOM    780  O   THR A 111     -20.395  23.969 -11.958  1.00 71.44           O  
+ANISOU  780  O   THR A 111     8959  10061   8124    -38   1646    539       O  
+ATOM    781  CB  THR A 111     -19.772  21.141 -11.871  1.00 55.03           C  
+ANISOU  781  CB  THR A 111     6805   7997   6106     12   1793    231       C  
+ATOM    782  OG1 THR A 111     -20.747  20.660 -12.805  1.00 47.26           O  
+ANISOU  782  OG1 THR A 111     5905   7110   4942    -27   1786    212       O  
+ATOM    783  CG2 THR A 111     -18.992  19.962 -11.311  1.00 49.47           C  
+ANISOU  783  CG2 THR A 111     6034   7217   5545     66   1820     81       C  
+ATOM    784  N   ASN A 112     -22.336  23.439 -10.945  1.00 41.62           N  
+ANISOU  784  N   ASN A 112     5197   6250   4368     60   1478    493       N  
+ATOM    785  CA  ASN A 112     -23.017  24.658 -11.362  1.00 48.62           C  
+ANISOU  785  CA  ASN A 112     6125   7144   5203     51   1366    605       C  
+ATOM    786  C   ASN A 112     -22.621  25.845 -10.496  1.00 54.73           C  
+ANISOU  786  C   ASN A 112     6873   7819   6103     93   1301    690       C  
+ATOM    787  O   ASN A 112     -22.273  25.687  -9.325  1.00 54.71           O  
+ANISOU  787  O   ASN A 112     6824   7738   6226    148   1311    651       O  
+ATOM    788  CB  ASN A 112     -24.534  24.466 -11.322  1.00 40.31           C  
+ANISOU  788  CB  ASN A 112     5071   6115   4128     85   1256    568       C  
+ATOM    789  CG  ASN A 112     -25.002  23.353 -12.234  1.00 42.72           C  
+ANISOU  789  CG  ASN A 112     5416   6508   4308     38   1290    495       C  
+ATOM    790  OD1 ASN A 112     -24.298  22.962 -13.164  1.00 52.10           O  
+ANISOU  790  OD1 ASN A 112     6661   7749   5384    -26   1381    488       O  
+ATOM    791  ND2 ASN A 112     -26.200  22.840 -11.977  1.00 54.33           N  
+ANISOU  791  ND2 ASN A 112     6851   7994   5797     63   1223    427       N  
+ATOM    792  N   TYR A 113     -22.677  27.035 -11.083  1.00 48.95           N  
+ANISOU  792  N   TYR A 113     6197   7075   5327     60   1212    809       N  
+ATOM    793  CA  TYR A 113     -22.350  28.259 -10.368  1.00 55.23           C  
+ANISOU  793  CA  TYR A 113     6984   7766   6236     99   1121    896       C  
+ATOM    794  C   TYR A 113     -23.611  28.895  -9.796  1.00 52.61           C  
+ANISOU  794  C   TYR A 113     6637   7384   5969    193    955    887       C  
+ATOM    795  O   TYR A 113     -23.570  29.580  -8.774  1.00 50.31           O  
+ANISOU  795  O   TYR A 113     6314   6999   5800    265    893    894       O  
+ATOM    796  CB  TYR A 113     -21.649  29.241 -11.304  1.00 56.88           C  
+ANISOU  796  CB  TYR A 113     7275   7970   6365     -6   1103   1035       C  
+ATOM    797  CG  TYR A 113     -20.529  28.619 -12.105  1.00 50.93           C  
+ANISOU  797  CG  TYR A 113     6524   7300   5528   -123   1299   1017       C  
+ATOM    798  CD1 TYR A 113     -19.267  28.428 -11.557  1.00 46.34           C  
+ANISOU  798  CD1 TYR A 113     5847   6688   5074   -130   1421    982       C  
+ATOM    799  CD2 TYR A 113     -20.741  28.217 -13.417  1.00 56.62           C  
+ANISOU  799  CD2 TYR A 113     7339   8126   6049   -227   1357   1015       C  
+ATOM    800  CE1 TYR A 113     -18.247  27.856 -12.299  1.00 52.57           C  
+ANISOU  800  CE1 TYR A 113     6599   7557   5816   -230   1615    928       C  
+ATOM    801  CE2 TYR A 113     -19.732  27.649 -14.164  1.00 43.84           C  
+ANISOU  801  CE2 TYR A 113     5715   6595   4348   -338   1564    968       C  
+ATOM    802  CZ  TYR A 113     -18.488  27.469 -13.602  1.00 50.97           C  
+ANISOU  802  CZ  TYR A 113     6488   7476   5403   -335   1702    914       C  
+ATOM    803  OH  TYR A 113     -17.484  26.900 -14.351  1.00 59.93           O  
+ANISOU  803  OH  TYR A 113     7580   8703   6486   -439   1921    831       O  
+ATOM    804  N   ASP A 114     -24.731  28.658 -10.474  1.00 48.49           N  
+ANISOU  804  N   ASP A 114     6131   6921   5374    194    881    854       N  
+ATOM    805  CA  ASP A 114     -26.022  29.217 -10.085  1.00 51.89           C  
+ANISOU  805  CA  ASP A 114     6510   7313   5891    285    720    810       C  
+ATOM    806  C   ASP A 114     -26.472  28.758  -8.700  1.00 54.48           C  
+ANISOU  806  C   ASP A 114     6732   7630   6340    362    789    681       C  
+ATOM    807  O   ASP A 114     -25.956  27.781  -8.156  1.00 46.67           O  
+ANISOU  807  O   ASP A 114     5734   6661   5338    334    936    627       O  
+ATOM    808  CB  ASP A 114     -27.088  28.862 -11.130  1.00 53.90           C  
+ANISOU  808  CB  ASP A 114     6786   7631   6063    263    625    782       C  
+ATOM    809  CG  ASP A 114     -27.339  27.367 -11.234  1.00 58.30           C  
+ANISOU  809  CG  ASP A 114     7308   8288   6557    228    766    674       C  
+ATOM    810  OD1 ASP A 114     -27.943  26.791 -10.305  1.00 66.20           O  
+ANISOU  810  OD1 ASP A 114     8205   9301   7647    274    819    558       O  
+ATOM    811  OD2 ASP A 114     -26.934  26.766 -12.251  1.00 68.14           O  
+ANISOU  811  OD2 ASP A 114     8642   9596   7653    141    826    701       O  
+ATOM    812  N   ARG A 115     -27.446  29.469  -8.142  1.00 54.08           N  
+ANISOU  812  N   ARG A 115     6610   7536   6402    450    674    622       N  
+ATOM    813  CA  ARG A 115     -27.955  29.169  -6.810  1.00 53.04           C  
+ANISOU  813  CA  ARG A 115     6392   7398   6363    500    755    488       C  
+ATOM    814  C   ARG A 115     -29.345  28.546  -6.842  1.00 62.02           C  
+ANISOU  814  C   ARG A 115     7419   8617   7530    507    762    346       C  
+ATOM    815  O   ARG A 115     -30.125  28.730  -5.911  1.00 68.19           O  
+ANISOU  815  O   ARG A 115     8101   9394   8413    555    786    220       O  
+ATOM    816  CB  ARG A 115     -28.011  30.437  -5.956  1.00 56.52           C  
+ANISOU  816  CB  ARG A 115     6811   7734   6930    594    658    483       C  
+ATOM    817  CG  ARG A 115     -26.685  31.100  -5.643  1.00 57.04           C  
+ANISOU  817  CG  ARG A 115     6971   7700   7001    589    645    608       C  
+ATOM    818  CD  ARG A 115     -26.889  32.082  -4.497  1.00 59.91           C  
+ANISOU  818  CD  ARG A 115     7312   7962   7488    687    577    554       C  
+ATOM    819  NE  ARG A 115     -25.737  32.944  -4.256  1.00 60.40           N  
+ANISOU  819  NE  ARG A 115     7461   7906   7581    692    509    681       N  
+ATOM    820  CZ  ARG A 115     -24.730  32.632  -3.448  1.00 78.41           C  
+ANISOU  820  CZ  ARG A 115     9797  10133   9861    663    599    703       C  
+ATOM    821  NH1 ARG A 115     -24.729  31.474  -2.802  1.00 91.62           N  
+ANISOU  821  NH1 ARG A 115    11473  11847  11489    623    749    614       N  
+ATOM    822  NH2 ARG A 115     -23.724  33.478  -3.283  1.00 72.66           N  
+ANISOU  822  NH2 ARG A 115     9130   9292   9185    666    517    816       N  
+ATOM    823  N   LEU A 116     -29.657  27.815  -7.907  1.00 57.40           N  
+ANISOU  823  N   LEU A 116     6847   8107   6857    450    750    355       N  
+ATOM    824  CA  LEU A 116     -30.996  27.252  -8.070  1.00 58.36           C  
+ANISOU  824  CA  LEU A 116     6852   8298   7022    449    729    226       C  
+ATOM    825  C   LEU A 116     -31.349  26.217  -6.999  1.00 61.32           C  
+ANISOU  825  C   LEU A 116     7165   8726   7408    397    913     97       C  
+ATOM    826  O   LEU A 116     -32.462  26.218  -6.470  1.00 56.38           O  
+ANISOU  826  O   LEU A 116     6400   8135   6887    413    929    -44       O  
+ATOM    827  CB  LEU A 116     -31.136  26.626  -9.458  1.00 59.55           C  
+ANISOU  827  CB  LEU A 116     7066   8504   7056    387    667    275       C  
+ATOM    828  CG  LEU A 116     -31.084  27.611 -10.626  1.00 61.30           C  
+ANISOU  828  CG  LEU A 116     7377   8673   7242    405    455    394       C  
+ATOM    829  CD1 LEU A 116     -31.307  26.885 -11.937  1.00 61.93           C  
+ANISOU  829  CD1 LEU A 116     7546   8808   7178    328    404    423       C  
+ATOM    830  CD2 LEU A 116     -32.108  28.720 -10.440  1.00 67.81           C  
+ANISOU  830  CD2 LEU A 116     8090   9425   8248    514    245    335       C  
+ATOM    831  N   ILE A 117     -30.400  25.341  -6.682  1.00 57.76           N  
+ANISOU  831  N   ILE A 117     6820   8272   6853    326   1047    136       N  
+ATOM    832  CA  ILE A 117     -30.625  24.289  -5.693  1.00 45.98           C  
+ANISOU  832  CA  ILE A 117     5328   6803   5338    248   1196     38       C  
+ATOM    833  C   ILE A 117     -30.904  24.868  -4.306  1.00 44.22           C  
+ANISOU  833  C   ILE A 117     5070   6538   5193    270   1258    -42       C  
+ATOM    834  O   ILE A 117     -31.914  24.537  -3.678  1.00 52.50           O  
+ANISOU  834  O   ILE A 117     6031   7640   6277    221   1342   -177       O  
+ATOM    835  CB  ILE A 117     -29.427  23.324  -5.615  1.00 40.54           C  
+ANISOU  835  CB  ILE A 117     4780   6078   4546    184   1274     98       C  
+ATOM    836  CG1 ILE A 117     -29.301  22.538  -6.921  1.00 43.23           C  
+ANISOU  836  CG1 ILE A 117     5149   6477   4798    149   1249    128       C  
+ATOM    837  CG2 ILE A 117     -29.589  22.366  -4.446  1.00 41.99           C  
+ANISOU  837  CG2 ILE A 117     5013   6241   4699     94   1386     15       C  
+ATOM    838  CD1 ILE A 117     -28.028  21.728  -7.032  1.00 40.14           C  
+ANISOU  838  CD1 ILE A 117     4867   6046   4340    116   1307    166       C  
+ATOM    839  N   GLU A 118     -30.008  25.731  -3.833  1.00 44.24           N  
+ANISOU  839  N   GLU A 118     5143   6447   5219    330   1226     33       N  
+ATOM    840  CA  GLU A 118     -30.168  26.349  -2.521  1.00 54.92           C  
+ANISOU  840  CA  GLU A 118     6495   7746   6627    356   1276    -41       C  
+ATOM    841  C   GLU A 118     -31.431  27.207  -2.466  1.00 51.23           C  
+ANISOU  841  C   GLU A 118     5852   7321   6292    433   1231   -170       C  
+ATOM    842  O   GLU A 118     -32.092  27.285  -1.427  1.00 62.85           O  
+ANISOU  842  O   GLU A 118     7270   8810   7801    413   1340   -314       O  
+ATOM    843  CB  GLU A 118     -28.937  27.185  -2.155  1.00 65.34           C  
+ANISOU  843  CB  GLU A 118     7922   8942   7961    416   1211     73       C  
+ATOM    844  CG  GLU A 118     -28.368  28.023  -3.288  1.00 66.09           C  
+ANISOU  844  CG  GLU A 118     8012   9012   8089    485   1065    208       C  
+ATOM    845  CD  GLU A 118     -27.194  27.353  -3.981  1.00 57.59           C  
+ANISOU  845  CD  GLU A 118     7025   7930   6929    427   1087    323       C  
+ATOM    846  OE1 GLU A 118     -27.378  26.253  -4.543  1.00 58.33           O  
+ANISOU  846  OE1 GLU A 118     7117   8099   6947    361   1147    297       O  
+ATOM    847  OE2 GLU A 118     -26.086  27.930  -3.962  1.00 60.87           O  
+ANISOU  847  OE2 GLU A 118     7500   8262   7365    446   1044    426       O  
+ATOM    848  N   LYS A 119     -31.766  27.842  -3.587  1.00 59.28           N  
+ANISOU  848  N   LYS A 119     6789   8350   7385    514   1066   -128       N  
+ATOM    849  CA  LYS A 119     -32.988  28.637  -3.680  1.00 60.29           C  
+ANISOU  849  CA  LYS A 119     6732   8497   7680    607    969   -263       C  
+ATOM    850  C   LYS A 119     -34.216  27.761  -3.487  1.00 55.36           C  
+ANISOU  850  C   LYS A 119     5953   7987   7095    534   1089   -440       C  
+ATOM    851  O   LYS A 119     -35.112  28.092  -2.708  1.00 57.14           O  
+ANISOU  851  O   LYS A 119     6025   8244   7443    558   1162   -627       O  
+ATOM    852  CB  LYS A 119     -33.084  29.353  -5.026  1.00 61.73           C  
+ANISOU  852  CB  LYS A 119     6900   8641   7914    687    723   -166       C  
+ATOM    853  CG  LYS A 119     -32.580  30.781  -5.018  1.00 80.78           C  
+ANISOU  853  CG  LYS A 119     9365  10929  10401    798    549    -83       C  
+ATOM    854  CD  LYS A 119     -33.069  31.515  -6.254  1.00 85.63           C  
+ANISOU  854  CD  LYS A 119     9955  11494  11089    866    274    -31       C  
+ATOM    855  CE  LYS A 119     -34.592  31.522  -6.298  1.00 79.25           C  
+ANISOU  855  CE  LYS A 119     8920  10725  10465    933    198   -238       C  
+ATOM    856  NZ  LYS A 119     -35.133  32.515  -7.264  1.00 82.73           N  
+ANISOU  856  NZ  LYS A 119     9336  11062  11035   1035   -139   -214       N  
+ATOM    857  N   ALA A 120     -34.246  26.643  -4.207  1.00 55.80           N  
+ANISOU  857  N   ALA A 120     6044   8107   7052    437   1116   -393       N  
+ATOM    858  CA  ALA A 120     -35.347  25.695  -4.110  1.00 56.08           C  
+ANISOU  858  CA  ALA A 120     5946   8248   7116    341   1222   -541       C  
+ATOM    859  C   ALA A 120     -35.459  25.190  -2.677  1.00 57.48           C  
+ANISOU  859  C   ALA A 120     6146   8455   7240    226   1462   -651       C  
+ATOM    860  O   ALA A 120     -36.560  25.039  -2.148  1.00 55.96           O  
+ANISOU  860  O   ALA A 120     5783   8341   7137    173   1577   -838       O  
+ATOM    861  CB  ALA A 120     -35.149  24.536  -5.077  1.00 50.71           C  
+ANISOU  861  CB  ALA A 120     5350   7607   6310    251   1201   -451       C  
+ATOM    862  N   LEU A 121     -34.311  24.926  -2.059  1.00 50.12           N  
+ANISOU  862  N   LEU A 121     5430   7453   6161    177   1533   -541       N  
+ATOM    863  CA  LEU A 121     -34.275  24.494  -0.665  1.00 49.39           C  
+ANISOU  863  CA  LEU A 121     5432   7353   5980     54   1728   -619       C  
+ATOM    864  C   LEU A 121     -34.871  25.535   0.291  1.00 60.91           C  
+ANISOU  864  C   LEU A 121     6782   8815   7546    112   1801   -777       C  
+ATOM    865  O   LEU A 121     -35.633  25.179   1.190  1.00 76.44           O  
+ANISOU  865  O   LEU A 121     8701  10850   9494    -10   1994   -940       O  
+ATOM    866  CB  LEU A 121     -32.842  24.151  -0.249  1.00 44.81           C  
+ANISOU  866  CB  LEU A 121     5114   6659   5254     19   1722   -464       C  
+ATOM    867  CG  LEU A 121     -32.291  22.849  -0.832  1.00 39.94           C  
+ANISOU  867  CG  LEU A 121     4619   6036   4522    -75   1706   -366       C  
+ATOM    868  CD1 LEU A 121     -30.816  22.685  -0.501  1.00 42.67           C  
+ANISOU  868  CD1 LEU A 121     5177   6249   4787    -68   1659   -233       C  
+ATOM    869  CD2 LEU A 121     -33.098  21.655  -0.331  1.00 41.05           C  
+ANISOU  869  CD2 LEU A 121     4775   6241   4582   -262   1848   -467       C  
+ATOM    870  N   GLU A 122     -34.537  26.812   0.103  1.00 58.13           N  
+ANISOU  870  N   GLU A 122     6397   8389   7302    285   1653   -741       N  
+ATOM    871  CA  GLU A 122     -35.038  27.847   1.010  1.00 59.41           C  
+ANISOU  871  CA  GLU A 122     6462   8536   7575    362   1703   -905       C  
+ATOM    872  C   GLU A 122     -36.517  28.121   0.782  1.00 65.48           C  
+ANISOU  872  C   GLU A 122     6924   9409   8546    407   1722  -1132       C  
+ATOM    873  O   GLU A 122     -37.245  28.450   1.719  1.00 75.30           O  
+ANISOU  873  O   GLU A 122     8050  10699   9860    391   1880  -1350       O  
+ATOM    874  CB  GLU A 122     -34.266  29.161   0.854  1.00 60.15           C  
+ANISOU  874  CB  GLU A 122     6611   8500   7743    538   1507   -801       C  
+ATOM    875  CG  GLU A 122     -32.880  29.189   1.463  1.00 76.81           C  
+ANISOU  875  CG  GLU A 122     8984  10491   9708    510   1507   -640       C  
+ATOM    876  CD  GLU A 122     -32.044  30.309   0.881  1.00 95.33           C  
+ANISOU  876  CD  GLU A 122    11374  12719  12128    658   1280   -487       C  
+ATOM    877  OE1 GLU A 122     -32.643  31.278   0.364  1.00 86.09           O  
+ANISOU  877  OE1 GLU A 122    10053  11538  11120    792   1131   -542       O  
+ATOM    878  OE2 GLU A 122     -30.799  30.228   0.941  1.00100.04           O  
+ANISOU  878  OE2 GLU A 122    12152  13224  12633    636   1238   -318       O  
+ATOM    879  N   GLU A 123     -36.958  27.984  -0.464  1.00 54.92           N  
+ANISOU  879  N   GLU A 123     5456   8102   7307    460   1558  -1096       N  
+ATOM    880  CA  GLU A 123     -38.369  28.153  -0.793  1.00 53.84           C  
+ANISOU  880  CA  GLU A 123     5011   8049   7396    505   1532  -1312       C  
+ATOM    881  C   GLU A 123     -39.218  27.054  -0.157  1.00 63.15           C  
+ANISOU  881  C   GLU A 123     6090   9368   8537    305   1807  -1481       C  
+ATOM    882  O   GLU A 123     -40.427  27.213   0.018  1.00 68.59           O  
+ANISOU  882  O   GLU A 123     6494  10142   9424    310   1878  -1726       O  
+ATOM    883  CB  GLU A 123     -38.564  28.174  -2.310  1.00 65.45           C  
+ANISOU  883  CB  GLU A 123     6420   9497   8952    587   1260  -1208       C  
+ATOM    884  CG  GLU A 123     -38.750  29.575  -2.878  1.00 91.38           C  
+ANISOU  884  CG  GLU A 123     9605  12672  12442    801    969  -1222       C  
+ATOM    885  CD  GLU A 123     -38.959  29.581  -4.379  1.00108.47           C  
+ANISOU  885  CD  GLU A 123    11759  14797  14657    855    681  -1110       C  
+ATOM    886  OE1 GLU A 123     -39.631  28.662  -4.892  1.00115.25           O  
+ANISOU  886  OE1 GLU A 123    12524  15740  15528    768    704  -1159       O  
+ATOM    887  OE2 GLU A 123     -38.450  30.506  -5.047  1.00104.34           O  
+ANISOU  887  OE2 GLU A 123    11344  14150  14151    970    425   -969       O  
+ATOM    888  N   GLU A 124     -38.580  25.938   0.180  1.00 66.82           N  
+ANISOU  888  N   GLU A 124     6785   9846   8757    121   1951  -1357       N  
+ATOM    889  CA  GLU A 124     -39.254  24.849   0.878  1.00 64.41           C  
+ANISOU  889  CA  GLU A 124     6453   9652   8367   -111   2213  -1485       C  
+ATOM    890  C   GLU A 124     -39.022  24.954   2.383  1.00 70.52           C  
+ANISOU  890  C   GLU A 124     7373  10419   9002   -226   2455  -1569       C  
+ATOM    891  O   GLU A 124     -39.275  24.004   3.125  1.00 78.10           O  
+ANISOU  891  O   GLU A 124     8429  11440   9807   -463   2680  -1623       O  
+ATOM    892  CB  GLU A 124     -38.764  23.495   0.362  1.00 66.69           C  
+ANISOU  892  CB  GLU A 124     6931   9939   8468   -258   2199  -1309       C  
+ATOM    893  CG  GLU A 124     -39.867  22.470   0.167  1.00 68.18           C  
+ANISOU  893  CG  GLU A 124     6960  10249   8695   -430   2309  -1432       C  
+ATOM    894  CD  GLU A 124     -40.977  22.981  -0.729  1.00 85.91           C  
+ANISOU  894  CD  GLU A 124     8862  12556  11224   -300   2171  -1573       C  
+ATOM    895  OE1 GLU A 124     -40.680  23.390  -1.872  1.00104.14           O  
+ANISOU  895  OE1 GLU A 124    11168  14800  13602   -133   1904  -1451       O  
+ATOM    896  OE2 GLU A 124     -42.147  22.975  -0.293  1.00 91.74           O  
+ANISOU  896  OE2 GLU A 124     9338  13402  12119   -375   2324  -1813       O  
+ATOM    897  N   ASN A 125     -38.533  26.115   2.817  1.00 65.65           N  
+ANISOU  897  N   ASN A 125     6799   9714   8428    -69   2392  -1574       N  
+ATOM    898  CA  ASN A 125     -38.231  26.378   4.224  1.00 73.67           C  
+ANISOU  898  CA  ASN A 125     7985  10698   9306   -153   2585  -1649       C  
+ATOM    899  C   ASN A 125     -37.224  25.389   4.807  1.00 72.00           C  
+ANISOU  899  C   ASN A 125     8147  10412   8800   -343   2651  -1464       C  
+ATOM    900  O   ASN A 125     -37.309  25.014   5.977  1.00 89.32           O  
+ANISOU  900  O   ASN A 125    10502  12615  10821   -534   2869  -1546       O  
+ATOM    901  CB  ASN A 125     -39.511  26.384   5.067  1.00 71.13           C  
+ANISOU  901  CB  ASN A 125     7451  10518   9056   -274   2871  -1963       C  
+ATOM    902  CG  ASN A 125     -40.371  27.607   4.809  1.00 83.39           C  
+ANISOU  902  CG  ASN A 125     8651  12105  10929    -51   2797  -2191       C  
+ATOM    903  OD1 ASN A 125     -39.858  28.702   4.573  1.00 86.17           O  
+ANISOU  903  OD1 ASN A 125     9015  12341  11384    175   2582  -2132       O  
+ATOM    904  ND2 ASN A 125     -41.686  27.428   4.861  1.00 92.79           N  
+ANISOU  904  ND2 ASN A 125     9519  13443  12295   -117   2962  -2462       N  
+ATOM    905  N   LYS A 126     -36.271  24.972   3.980  1.00 53.39           N  
+ANISOU  905  N   LYS A 126     5931   7970   6386   -294   2454  -1225       N  
+ATOM    906  CA  LYS A 126     -35.174  24.132   4.441  1.00 56.07           C  
+ANISOU  906  CA  LYS A 126     6609   8199   6497   -425   2448  -1050       C  
+ATOM    907  C   LYS A 126     -33.898  24.958   4.504  1.00 60.35           C  
+ANISOU  907  C   LYS A 126     7308   8585   7037   -265   2271   -896       C  
+ATOM    908  O   LYS A 126     -33.716  25.893   3.724  1.00 59.18           O  
+ANISOU  908  O   LYS A 126     7023   8417   7046    -64   2107   -849       O  
+ATOM    909  CB  LYS A 126     -34.970  22.929   3.517  1.00 59.40           C  
+ANISOU  909  CB  LYS A 126     7071   8634   6865   -499   2367   -921       C  
+ATOM    910  CG  LYS A 126     -36.083  21.898   3.542  1.00 53.82           C  
+ANISOU  910  CG  LYS A 126     6268   8055   6125   -702   2530  -1042       C  
+ATOM    911  CD  LYS A 126     -35.680  20.665   2.748  1.00 54.87           C  
+ANISOU  911  CD  LYS A 126     6509   8163   6178   -775   2426   -899       C  
+ATOM    912  CE  LYS A 126     -36.769  19.608   2.758  1.00 54.29           C  
+ANISOU  912  CE  LYS A 126     6353   8202   6072   -992   2567  -1007       C  
+ATOM    913  NZ  LYS A 126     -36.346  18.387   2.016  1.00 54.17           N  
+ANISOU  913  NZ  LYS A 126     6466   8143   5973  -1058   2447   -873       N  
+ATOM    914  N   ILE A 127     -33.014  24.610   5.429  1.00 50.81           N  
+ANISOU  914  N   ILE A 127     6399   7252   5655   -366   2287   -813       N  
+ATOM    915  CA  ILE A 127     -31.763  25.337   5.583  1.00 44.39           C  
+ANISOU  915  CA  ILE A 127     5736   6278   4852   -234   2118   -672       C  
+ATOM    916  C   ILE A 127     -30.648  24.641   4.808  1.00 45.27           C  
+ANISOU  916  C   ILE A 127     5954   6304   4942   -215   1953   -473       C  
+ATOM    917  O   ILE A 127     -30.356  23.468   5.040  1.00 47.10           O  
+ANISOU  917  O   ILE A 127     6358   6494   5044   -365   1972   -426       O  
+ATOM    918  CB  ILE A 127     -31.369  25.475   7.062  1.00 56.23           C  
+ANISOU  918  CB  ILE A 127     7506   7661   6197   -337   2192   -705       C  
+ATOM    919  CG1 ILE A 127     -32.343  26.412   7.782  1.00 46.21           C  
+ANISOU  919  CG1 ILE A 127     6115   6471   4971   -314   2353   -923       C  
+ATOM    920  CG2 ILE A 127     -29.945  25.983   7.187  1.00 42.42           C  
+ANISOU  920  CG2 ILE A 127     5934   5723   4462   -223   1985   -537       C  
+ATOM    921  CD1 ILE A 127     -32.383  26.218   9.282  1.00 47.41           C  
+ANISOU  921  CD1 ILE A 127     6540   6568   4907   -504   2520  -1015       C  
+ATOM    922  N   ALA A 128     -30.030  25.373   3.889  1.00 41.58           N  
+ANISOU  922  N   ALA A 128     5387   5807   4605    -37   1790   -365       N  
+ATOM    923  CA  ALA A 128     -28.997  24.809   3.028  1.00 49.78           C  
+ANISOU  923  CA  ALA A 128     6479   6790   5646    -10   1661   -207       C  
+ATOM    924  C   ALA A 128     -27.600  25.228   3.469  1.00 52.76           C  
+ANISOU  924  C   ALA A 128     7020   6993   6033     47   1536    -88       C  
+ATOM    925  O   ALA A 128     -27.306  26.418   3.581  1.00 53.41           O  
+ANISOU  925  O   ALA A 128     7067   7023   6201    165   1463    -63       O  
+ATOM    926  CB  ALA A 128     -29.236  25.222   1.585  1.00 49.73           C  
+ANISOU  926  CB  ALA A 128     6264   6878   5755    109   1580   -166       C  
+ATOM    927  N   ASP A 129     -26.743  24.243   3.718  1.00 46.16           N  
+ANISOU  927  N   ASP A 129     6360   6053   5127    -34   1489    -21       N  
+ATOM    928  CA  ASP A 129     -25.338  24.508   3.995  1.00 42.61           C  
+ANISOU  928  CA  ASP A 129     6032   5428   4728     23   1343     86       C  
+ATOM    929  C   ASP A 129     -24.571  24.526   2.679  1.00 46.47           C  
+ANISOU  929  C   ASP A 129     6384   5946   5328    118   1262    180       C  
+ATOM    930  O   ASP A 129     -24.193  23.476   2.160  1.00 44.74           O  
+ANISOU  930  O   ASP A 129     6178   5727   5094     76   1248    195       O  
+ATOM    931  CB  ASP A 129     -24.762  23.449   4.940  1.00 42.96           C  
+ANISOU  931  CB  ASP A 129     6336   5318   4671   -105   1296     94       C  
+ATOM    932  CG  ASP A 129     -23.411  23.841   5.513  1.00 53.31           C  
+ANISOU  932  CG  ASP A 129     7784   6419   6054    -48   1125    177       C  
+ATOM    933  OD1 ASP A 129     -22.778  24.780   4.987  1.00 72.73           O  
+ANISOU  933  OD1 ASP A 129    10115   8867   8652     85   1053    242       O  
+ATOM    934  OD2 ASP A 129     -22.979  23.201   6.495  1.00 49.66           O  
+ANISOU  934  OD2 ASP A 129     7571   5790   5510   -147   1046    179       O  
+ATOM    935  N   VAL A 130     -24.347  25.720   2.142  1.00 43.84           N  
+ANISOU  935  N   VAL A 130     5930   5631   5097    235   1209    235       N  
+ATOM    936  CA  VAL A 130     -23.715  25.852   0.835  1.00 41.49           C  
+ANISOU  936  CA  VAL A 130     5510   5380   4873    295   1162    321       C  
+ATOM    937  C   VAL A 130     -22.208  26.041   0.961  1.00 41.77           C  
+ANISOU  937  C   VAL A 130     5598   5272   5003    327   1061    408       C  
+ATOM    938  O   VAL A 130     -21.740  26.993   1.586  1.00 59.53           O  
+ANISOU  938  O   VAL A 130     7890   7413   7316    374    983    450       O  
+ATOM    939  CB  VAL A 130     -24.309  27.031   0.040  1.00 50.52           C  
+ANISOU  939  CB  VAL A 130     6511   6616   6068    377   1141    346       C  
+ATOM    940  CG1 VAL A 130     -23.721  27.076  -1.360  1.00 42.86           C  
+ANISOU  940  CG1 VAL A 130     5458   5703   5123    394   1112    437       C  
+ATOM    941  CG2 VAL A 130     -25.827  26.922  -0.015  1.00 47.73           C  
+ANISOU  941  CG2 VAL A 130     6073   6389   5672    362   1218    234       C  
+ATOM    942  N   LYS A 131     -21.456  25.124   0.362  1.00 42.14           N  
+ANISOU  942  N   LYS A 131     5625   5312   5072    302   1059    419       N  
+ATOM    943  CA  LYS A 131     -20.000  25.143   0.430  1.00 43.21           C  
+ANISOU  943  CA  LYS A 131     5769   5315   5335    329    970    467       C  
+ATOM    944  C   LYS A 131     -19.392  25.255  -0.966  1.00 48.29           C  
+ANISOU  944  C   LYS A 131     6255   6056   6037    348   1015    508       C  
+ATOM    945  O   LYS A 131     -19.589  24.374  -1.803  1.00 47.08           O  
+ANISOU  945  O   LYS A 131     6053   6005   5830    319   1089    462       O  
+ATOM    946  CB  LYS A 131     -19.483  23.888   1.136  1.00 43.71           C  
+ANISOU  946  CB  LYS A 131     5960   5244   5405    282    908    410       C  
+ATOM    947  CG  LYS A 131     -20.223  23.550   2.424  1.00 43.57           C  
+ANISOU  947  CG  LYS A 131     6142   5149   5265    210    892    366       C  
+ATOM    948  CD  LYS A 131     -19.562  22.394   3.161  1.00 44.83           C  
+ANISOU  948  CD  LYS A 131     6476   5124   5433    152    771    333       C  
+ATOM    949  CE  LYS A 131     -20.261  22.105   4.482  1.00 44.21           C  
+ANISOU  949  CE  LYS A 131     6646   4958   5194     41    759    302       C  
+ATOM    950  NZ  LYS A 131     -20.151  23.244   5.435  1.00 46.09           N  
+ANISOU  950  NZ  LYS A 131     6979   5102   5431     65    713    334       N  
+ATOM    951  N   TYR A 132     -18.651  26.332  -1.217  1.00 46.38           N  
+ANISOU  951  N   TYR A 132     5949   5780   5892    382    974    591       N  
+ATOM    952  CA  TYR A 132     -17.943  26.483  -2.486  1.00 48.61           C  
+ANISOU  952  CA  TYR A 132     6104   6149   6217    364   1037    630       C  
+ATOM    953  C   TYR A 132     -16.482  26.882  -2.277  1.00 50.66           C  
+ANISOU  953  C   TYR A 132     6307   6284   6656    372    979    664       C  
+ATOM    954  O   TYR A 132     -15.711  26.964  -3.232  1.00 60.89           O  
+ANISOU  954  O   TYR A 132     7486   7644   8006    336   1055    677       O  
+ATOM    955  CB  TYR A 132     -18.644  27.500  -3.391  1.00 46.23           C  
+ANISOU  955  CB  TYR A 132     5765   5971   5831    356   1064    710       C  
+ATOM    956  CG  TYR A 132     -19.124  28.750  -2.694  1.00 48.57           C  
+ANISOU  956  CG  TYR A 132     6111   6197   6146    404    961    770       C  
+ATOM    957  CD1 TYR A 132     -18.263  29.816  -2.470  1.00 48.42           C  
+ANISOU  957  CD1 TYR A 132     6087   6073   6236    415    876    861       C  
+ATOM    958  CD2 TYR A 132     -20.442  28.873  -2.276  1.00 46.55           C  
+ANISOU  958  CD2 TYR A 132     5894   5978   5813    437    949    720       C  
+ATOM    959  CE1 TYR A 132     -18.699  30.966  -1.839  1.00 51.06           C  
+ANISOU  959  CE1 TYR A 132     6475   6330   6593    470    765    904       C  
+ATOM    960  CE2 TYR A 132     -20.888  30.019  -1.645  1.00 47.83           C  
+ANISOU  960  CE2 TYR A 132     6088   6076   6010    495    858    743       C  
+ATOM    961  CZ  TYR A 132     -20.012  31.062  -1.429  1.00 49.77           C  
+ANISOU  961  CZ  TYR A 132     6349   6206   6356    517    758    837       C  
+ATOM    962  OH  TYR A 132     -20.449  32.205  -0.801  1.00 51.60           O  
+ANISOU  962  OH  TYR A 132     6620   6359   6626    585    650    848       O  
+ATOM    963  N   THR A 133     -16.105  27.128  -1.026  1.00 50.03           N  
+ANISOU  963  N   THR A 133     6314   6027   6668    407    849    671       N  
+ATOM    964  CA  THR A 133     -14.705  27.373  -0.694  1.00 52.87           C  
+ANISOU  964  CA  THR A 133     6617   6238   7233    419    759    686       C  
+ATOM    965  C   THR A 133     -14.157  26.201   0.112  1.00 54.53           C  
+ANISOU  965  C   THR A 133     6888   6293   7536    437    661    586       C  
+ATOM    966  O   THR A 133     -14.921  25.409   0.662  1.00 64.34           O  
+ANISOU  966  O   THR A 133     8271   7518   8658    428    644    534       O  
+ATOM    967  CB  THR A 133     -14.517  28.674   0.112  1.00 52.54           C  
+ANISOU  967  CB  THR A 133     6640   6067   7254    447    630    780       C  
+ATOM    968  OG1 THR A 133     -15.007  28.491   1.446  1.00 51.08           O  
+ANISOU  968  OG1 THR A 133     6642   5750   7015    476    522    748       O  
+ATOM    969  CG2 THR A 133     -15.255  29.828  -0.546  1.00 51.50           C  
+ANISOU  969  CG2 THR A 133     6490   6056   7022    439    676    873       C  
+ATOM    970  N   VAL A 134     -12.834  26.091   0.175  1.00 56.71           N  
+ANISOU  970  N   VAL A 134     7062   6448   8038    454    585    556       N  
+ATOM    971  CA  VAL A 134     -12.195  25.019   0.929  1.00 56.90           C  
+ANISOU  971  CA  VAL A 134     7144   6283   8194    483    434    455       C  
+ATOM    972  C   VAL A 134     -12.476  25.165   2.427  1.00 53.78           C  
+ANISOU  972  C   VAL A 134     7001   5683   7750    491    241    491       C  
+ATOM    973  O   VAL A 134     -12.739  24.178   3.116  1.00 52.78           O  
+ANISOU  973  O   VAL A 134     7045   5446   7561    475    144    432       O  
+ATOM    974  CB  VAL A 134     -10.664  24.973   0.662  1.00 58.74           C  
+ANISOU  974  CB  VAL A 134     7170   6417   8731    510    377    393       C  
+ATOM    975  CG1 VAL A 134     -10.017  26.331   0.902  1.00 73.71           C  
+ANISOU  975  CG1 VAL A 134     9005   8244  10756    506    317    498       C  
+ATOM    976  CG2 VAL A 134      -9.998  23.896   1.504  1.00 58.18           C  
+ANISOU  976  CG2 VAL A 134     7168   6107   8831    558    158    282       C  
+ATOM    977  N   LYS A 135     -12.428  26.399   2.923  1.00 61.79           N  
+ANISOU  977  N   LYS A 135     8059   6641   8777    502    181    588       N  
+ATOM    978  CA  LYS A 135     -12.644  26.676   4.340  1.00 54.97           C  
+ANISOU  978  CA  LYS A 135     7449   5584   7855    503      9    616       C  
+ATOM    979  C   LYS A 135     -14.049  26.299   4.815  1.00 52.98           C  
+ANISOU  979  C   LYS A 135     7395   5408   7325    455     91    594       C  
+ATOM    980  O   LYS A 135     -14.222  25.843   5.945  1.00 56.66           O  
+ANISOU  980  O   LYS A 135     8107   5714   7707    417    -29    569       O  
+ATOM    981  CB  LYS A 135     -12.375  28.153   4.638  1.00 47.90           C  
+ANISOU  981  CB  LYS A 135     6545   4633   7022    530    -54    714       C  
+ATOM    982  CG  LYS A 135     -10.901  28.524   4.615  1.00 54.10           C  
+ANISOU  982  CG  LYS A 135     7189   5267   8101    556   -196    734       C  
+ATOM    983  CD  LYS A 135     -10.688  29.986   4.968  1.00 64.75           C  
+ANISOU  983  CD  LYS A 135     8557   6544   9501    572   -280    840       C  
+ATOM    984  CE  LYS A 135      -9.229  30.386   4.812  1.00 84.33           C  
+ANISOU  984  CE  LYS A 135    10856   8897  12290    578   -398    860       C  
+ATOM    985  NZ  LYS A 135      -8.973  31.758   5.333  1.00 98.32           N  
+ANISOU  985  NZ  LYS A 135    12687  10551  14121    588   -530    967       N  
+ATOM    986  N   GLN A 136     -15.045  26.484   3.952  1.00 49.13           N  
+ANISOU  986  N   GLN A 136     6809   5159   6699    444    292    600       N  
+ATOM    987  CA  GLN A 136     -16.433  26.176   4.306  1.00 49.03           C  
+ANISOU  987  CA  GLN A 136     6930   5244   6455    394    394    561       C  
+ATOM    988  C   GLN A 136     -16.673  24.696   4.605  1.00 49.53           C  
+ANISOU  988  C   GLN A 136     7121   5267   6430    323    384    484       C  
+ATOM    989  O   GLN A 136     -17.704  24.336   5.169  1.00 49.47           O  
+ANISOU  989  O   GLN A 136     7267   5296   6234    248    448    446       O  
+ATOM    990  CB  GLN A 136     -17.390  26.638   3.204  1.00 49.51           C  
+ANISOU  990  CB  GLN A 136     6829   5554   6430    405    575    573       C  
+ATOM    991  CG  GLN A 136     -17.661  28.133   3.214  1.00 49.17           C  
+ANISOU  991  CG  GLN A 136     6745   5535   6401    457    567    639       C  
+ATOM    992  CD  GLN A 136     -18.538  28.580   2.061  1.00 49.46           C  
+ANISOU  992  CD  GLN A 136     6635   5783   6376    471    690    654       C  
+ATOM    993  OE1 GLN A 136     -18.391  28.112   0.932  1.00 49.20           O  
+ANISOU  993  OE1 GLN A 136     6480   5866   6347    452    767    662       O  
+ATOM    994  NE2 GLN A 136     -19.472  29.480   2.346  1.00 49.72           N  
+ANISOU  994  NE2 GLN A 136     6688   5853   6352    506    697    646       N  
+ATOM    995  N   LEU A 137     -15.737  23.838   4.216  1.00 50.31           N  
+ANISOU  995  N   LEU A 137     7152   5290   6672    339    304    449       N  
+ATOM    996  CA  LEU A 137     -15.853  22.418   4.523  1.00 50.32           C  
+ANISOU  996  CA  LEU A 137     7295   5210   6615    277    241    377       C  
+ATOM    997  C   LEU A 137     -15.612  22.173   6.009  1.00 48.24           C  
+ANISOU  997  C   LEU A 137     7336   4683   6311    220     31    383       C  
+ATOM    998  O   LEU A 137     -16.034  21.156   6.559  1.00 48.16           O  
+ANISOU  998  O   LEU A 137     7539   4592   6166    123    -23    346       O  
+ATOM    999  CB  LEU A 137     -14.865  21.602   3.690  1.00 51.88           C  
+ANISOU  999  CB  LEU A 137     7322   5381   7010    330    192    311       C  
+ATOM   1000  CG  LEU A 137     -15.107  21.580   2.182  1.00 53.92           C  
+ANISOU 1000  CG  LEU A 137     7330   5894   7265    356    404    287       C  
+ATOM   1001  CD1 LEU A 137     -13.958  20.892   1.472  1.00 60.86           C  
+ANISOU 1001  CD1 LEU A 137     8033   6728   8363    413    363    195       C  
+ATOM   1002  CD2 LEU A 137     -16.419  20.889   1.866  1.00 53.70           C  
+ANISOU 1002  CD2 LEU A 137     7368   6023   7013    287    535    260       C  
+ATOM   1003  N   ALA A 138     -14.929  23.114   6.652  1.00 46.64           N  
+ANISOU 1003  N   ALA A 138     7176   4333   6212    266    -99    435       N  
+ATOM   1004  CA  ALA A 138     -14.605  23.000   8.069  1.00 52.66           C  
+ANISOU 1004  CA  ALA A 138     8254   4820   6933    211   -326    448       C  
+ATOM   1005  C   ALA A 138     -15.767  23.399   8.976  1.00 63.03           C  
+ANISOU 1005  C   ALA A 138     9811   6175   7961    109   -223    459       C  
+ATOM   1006  O   ALA A 138     -15.739  23.126  10.176  1.00 86.65           O  
+ANISOU 1006  O   ALA A 138    13129   8961  10833     16   -373    460       O  
+ATOM   1007  CB  ALA A 138     -13.380  23.840   8.395  1.00 47.43           C  
+ANISOU 1007  CB  ALA A 138     7540   3971   6510    300   -524    491       C  
+ATOM   1008  N   THR A 139     -16.783  24.044   8.411  1.00 51.45           N  
+ANISOU 1008  N   THR A 139     8192   4966   6390    121     25    454       N  
+ATOM   1009  CA  THR A 139     -17.909  24.518   9.212  1.00 50.82           C  
+ANISOU 1009  CA  THR A 139     8283   4948   6078     39    153    428       C  
+ATOM   1010  C   THR A 139     -19.141  23.637   9.045  1.00 57.04           C  
+ANISOU 1010  C   THR A 139     9103   5907   6663    -83    348    360       C  
+ATOM   1011  O   THR A 139     -19.297  22.942   8.042  1.00 50.06           O  
+ANISOU 1011  O   THR A 139     8045   5153   5823    -71    421    346       O  
+ATOM   1012  CB  THR A 139     -18.291  25.975   8.860  1.00 59.78           C  
+ANISOU 1012  CB  THR A 139     9232   6225   7257    142    267    445       C  
+ATOM   1013  OG1 THR A 139     -19.223  26.474   9.827  1.00 87.36           O  
+ANISOU 1013  OG1 THR A 139    12904   9734  10557     77    361    387       O  
+ATOM   1014  CG2 THR A 139     -18.920  26.054   7.480  1.00 58.42           C  
+ANISOU 1014  CG2 THR A 139     8759   6317   7121    195    452    435       C  
+ATOM   1015  N   THR A 140     -20.007  23.666  10.052  1.00 51.27           N  
+ANISOU 1015  N   THR A 140     8603   5172   5707   -212    437    311       N  
+ATOM   1016  CA  THR A 140     -21.265  22.935  10.006  1.00 46.29           C  
+ANISOU 1016  CA  THR A 140     7996   4710   4881   -355    646    236       C  
+ATOM   1017  C   THR A 140     -22.425  23.847  10.383  1.00 53.11           C  
+ANISOU 1017  C   THR A 140     8817   5736   5625   -378    868    151       C  
+ATOM   1018  O   THR A 140     -22.568  24.226  11.544  1.00 77.62           O  
+ANISOU 1018  O   THR A 140    12165   8739   8586   -460    873    115       O  
+ATOM   1019  CB  THR A 140     -21.245  21.720  10.956  1.00 63.97           C  
+ANISOU 1019  CB  THR A 140    10602   6773   6932   -560    552    230       C  
+ATOM   1020  OG1 THR A 140     -20.138  20.869  10.630  1.00 67.14           O  
+ANISOU 1020  OG1 THR A 140    11033   6994   7482   -516    307    286       O  
+ATOM   1021  CG2 THR A 140     -22.543  20.930  10.852  1.00 65.35           C  
+ANISOU 1021  CG2 THR A 140    10786   7130   6914   -731    778    157       C  
+ATOM   1022  N   LYS A 141     -23.249  24.204   9.402  1.00 49.85           N  
+ANISOU 1022  N   LYS A 141     8100   5565   5277   -302   1041    106       N  
+ATOM   1023  CA  LYS A 141     -24.363  25.113   9.654  1.00 46.18           C  
+ANISOU 1023  CA  LYS A 141     7536   5253   4757   -291   1232     -3       C  
+ATOM   1024  C   LYS A 141     -25.415  24.496  10.559  1.00 57.66           C  
+ANISOU 1024  C   LYS A 141     9170   6763   5975   -508   1423   -122       C  
+ATOM   1025  O   LYS A 141     -25.854  23.365  10.340  1.00 62.43           O  
+ANISOU 1025  O   LYS A 141     9802   7429   6489   -648   1494   -136       O  
+ATOM   1026  CB  LYS A 141     -25.025  25.561   8.355  1.00 42.14           C  
+ANISOU 1026  CB  LYS A 141     6665   4962   4386   -165   1329    -28       C  
+ATOM   1027  CG  LYS A 141     -25.904  26.787   8.546  1.00 52.01           C  
+ANISOU 1027  CG  LYS A 141     7778   6317   5668    -84   1440   -138       C  
+ATOM   1028  CD  LYS A 141     -26.579  27.225   7.267  1.00 61.25           C  
+ANISOU 1028  CD  LYS A 141     8618   7671   6983     38   1484   -160       C  
+ATOM   1029  CE  LYS A 141     -27.170  28.617   7.423  1.00 73.22           C  
+ANISOU 1029  CE  LYS A 141    10001   9228   8592    166   1504   -255       C  
+ATOM   1030  NZ  LYS A 141     -26.205  29.568   8.034  1.00 89.41           N  
+ANISOU 1030  NZ  LYS A 141    12190  11096  10685    255   1350   -184       N  
+ATOM   1031  N   VAL A 142     -25.811  25.250  11.578  1.00 57.99           N  
+ANISOU 1031  N   VAL A 142     9338   6783   5911   -547   1513   -215       N  
+ATOM   1032  CA  VAL A 142     -26.792  24.782  12.545  1.00 57.54           C  
+ANISOU 1032  CA  VAL A 142     9469   6784   5609   -781   1732   -348       C  
+ATOM   1033  C   VAL A 142     -28.151  24.527  11.892  1.00 54.64           C  
+ANISOU 1033  C   VAL A 142     8812   6687   5263   -826   1984   -480       C  
+ATOM   1034  O   VAL A 142     -28.592  25.289  11.029  1.00 52.06           O  
+ANISOU 1034  O   VAL A 142     8145   6505   5130   -644   2021   -528       O  
+ATOM   1035  CB  VAL A 142     -26.950  25.780  13.716  1.00 59.13           C  
+ANISOU 1035  CB  VAL A 142     9841   6924   5703   -795   1800   -451       C  
+ATOM   1036  CG1 VAL A 142     -25.651  25.887  14.497  1.00 47.29           C  
+ANISOU 1036  CG1 VAL A 142     8683   5131   4154   -792   1533   -324       C  
+ATOM   1037  CG2 VAL A 142     -27.386  27.143  13.213  1.00 74.18           C  
+ANISOU 1037  CG2 VAL A 142    11417   8958   7812   -566   1856   -542       C  
+ATOM   1038  N   LYS A 143     -28.785  23.426  12.290  1.00 46.95           N  
+ANISOU 1038  N   LYS A 143     7984   5761   4093  -1078   2130   -530       N  
+ATOM   1039  CA  LYS A 143     -30.140  23.087  11.859  1.00 68.17           C  
+ANISOU 1039  CA  LYS A 143    10423   8694   6784  -1170   2385   -673       C  
+ATOM   1040  C   LYS A 143     -30.260  22.920  10.347  1.00 62.75           C  
+ANISOU 1040  C   LYS A 143     9390   8129   6321  -1005   2312   -620       C  
+ATOM   1041  O   LYS A 143     -31.341  23.089   9.783  1.00 67.54           O  
+ANISOU 1041  O   LYS A 143     9699   8938   7027   -981   2469   -746       O  
+ATOM   1042  CB  LYS A 143     -31.136  24.146  12.340  1.00 56.21           C  
+ANISOU 1042  CB  LYS A 143     8740   7325   5291  -1141   2620   -889       C  
+ATOM   1043  CG  LYS A 143     -31.153  24.340  13.845  1.00 58.07           C  
+ANISOU 1043  CG  LYS A 143     9322   7468   5275  -1326   2741   -977       C  
+ATOM   1044  CD  LYS A 143     -32.222  25.336  14.258  1.00 75.04           C  
+ANISOU 1044  CD  LYS A 143    11261   9784   7465  -1292   3005  -1236       C  
+ATOM   1045  CE  LYS A 143     -32.310  25.447  15.770  1.00 85.52           C  
+ANISOU 1045  CE  LYS A 143    12957  11037   8498  -1512   3170  -1347       C  
+ATOM   1046  NZ  LYS A 143     -32.427  24.109  16.412  1.00101.21           N  
+ANISOU 1046  NZ  LYS A 143    15272  12977  10206  -1863   3238  -1288       N  
+ATOM   1047  N   ARG A 144     -29.150  22.594   9.693  1.00 48.75           N  
+ANISOU 1047  N   ARG A 144     7658   6229   4634   -894   2071   -447       N  
+ATOM   1048  CA  ARG A 144     -29.162  22.402   8.250  1.00 53.64           C  
+ANISOU 1048  CA  ARG A 144     7997   6953   5432   -754   2001   -392       C  
+ATOM   1049  C   ARG A 144     -29.990  21.174   7.888  1.00 50.65           C  
+ANISOU 1049  C   ARG A 144     7581   6688   4975   -929   2113   -436       C  
+ATOM   1050  O   ARG A 144     -30.030  20.196   8.635  1.00 59.02           O  
+ANISOU 1050  O   ARG A 144     8905   7672   5846  -1155   2147   -432       O  
+ATOM   1051  CB  ARG A 144     -27.735  22.266   7.708  1.00 43.26           C  
+ANISOU 1051  CB  ARG A 144     6745   5479   4214   -623   1750   -223       C  
+ATOM   1052  CG  ARG A 144     -27.022  20.989   8.126  1.00 53.79           C  
+ANISOU 1052  CG  ARG A 144     8367   6640   5429   -770   1628   -145       C  
+ATOM   1053  CD  ARG A 144     -25.549  21.026   7.754  1.00 39.89           C  
+ANISOU 1053  CD  ARG A 144     6644   4707   3807   -622   1382    -19       C  
+ATOM   1054  NE  ARG A 144     -24.890  19.747   8.002  1.00 50.86           N  
+ANISOU 1054  NE  ARG A 144     8267   5923   5134   -733   1229     34       N  
+ATOM   1055  CZ  ARG A 144     -23.605  19.509   7.759  1.00 50.35           C  
+ANISOU 1055  CZ  ARG A 144     8242   5686   5202   -630   1005    112       C  
+ATOM   1056  NH1 ARG A 144     -22.832  20.464   7.260  1.00 55.99           N  
+ANISOU 1056  NH1 ARG A 144     8779   6393   6101   -437    935    158       N  
+ATOM   1057  NH2 ARG A 144     -23.090  18.314   8.015  1.00 40.52           N  
+ANISOU 1057  NH2 ARG A 144     7209   4269   3918   -726    844    136       N  
+ATOM   1058  N   ASP A 145     -30.655  21.232   6.740  1.00 52.04           N  
+ANISOU 1058  N   ASP A 145     7448   7033   5292   -835   2150   -473       N  
+ATOM   1059  CA  ASP A 145     -31.424  20.099   6.246  1.00 53.17           C  
+ANISOU 1059  CA  ASP A 145     7529   7283   5392   -980   2228   -509       C  
+ATOM   1060  C   ASP A 145     -30.686  19.419   5.103  1.00 54.42           C  
+ANISOU 1060  C   ASP A 145     7660   7397   5621   -887   2045   -381       C  
+ATOM   1061  O   ASP A 145     -30.858  18.225   4.862  1.00 74.67           O  
+ANISOU 1061  O   ASP A 145    10298   9961   8114  -1021   2035   -367       O  
+ATOM   1062  CB  ASP A 145     -32.816  20.542   5.793  1.00 66.66           C  
+ANISOU 1062  CB  ASP A 145     8910   9207   7212   -961   2395   -667       C  
+ATOM   1063  CG  ASP A 145     -33.628  21.153   6.918  1.00 82.56           C  
+ANISOU 1063  CG  ASP A 145    10916  11284   9169  -1062   2614   -841       C  
+ATOM   1064  OD1 ASP A 145     -34.121  20.392   7.777  1.00108.71           O  
+ANISOU 1064  OD1 ASP A 145    14393  14612  12300  -1325   2782   -910       O  
+ATOM   1065  OD2 ASP A 145     -33.775  22.393   6.943  1.00 72.66           O  
+ANISOU 1065  OD2 ASP A 145     9499  10061   8047   -888   2620   -916       O  
+ATOM   1066  N   ALA A 146     -29.861  20.188   4.400  1.00 42.30           N  
+ANISOU 1066  N   ALA A 146     6024   5824   4224   -668   1906   -298       N  
+ATOM   1067  CA  ALA A 146     -29.094  19.653   3.284  1.00 55.06           C  
+ANISOU 1067  CA  ALA A 146     7601   7410   5908   -575   1761   -199       C  
+ATOM   1068  C   ALA A 146     -27.753  20.362   3.124  1.00 50.71           C  
+ANISOU 1068  C   ALA A 146     7080   6735   5452   -411   1612    -95       C  
+ATOM   1069  O   ALA A 146     -27.623  21.548   3.429  1.00 56.68           O  
+ANISOU 1069  O   ALA A 146     7788   7478   6269   -312   1609    -91       O  
+ATOM   1070  CB  ALA A 146     -29.898  19.755   1.998  1.00 39.02           C  
+ANISOU 1070  CB  ALA A 146     5302   5553   3969   -500   1790   -234       C  
+ATOM   1071  N   VAL A 147     -26.758  19.620   2.648  1.00 47.65           N  
+ANISOU 1071  N   VAL A 147     6762   6253   5089   -385   1487    -24       N  
+ATOM   1072  CA  VAL A 147     -25.473  20.197   2.277  1.00 52.13           C  
+ANISOU 1072  CA  VAL A 147     7302   6726   5777   -236   1362     60       C  
+ATOM   1073  C   VAL A 147     -25.366  20.325   0.760  1.00 54.73           C  
+ANISOU 1073  C   VAL A 147     7424   7178   6191   -129   1359     87       C  
+ATOM   1074  O   VAL A 147     -25.697  19.391   0.029  1.00 45.53           O  
+ANISOU 1074  O   VAL A 147     6224   6083   4991   -171   1377     58       O  
+ATOM   1075  CB  VAL A 147     -24.299  19.346   2.800  1.00 57.38           C  
+ANISOU 1075  CB  VAL A 147     8169   7185   6450   -270   1215     96       C  
+ATOM   1076  CG1 VAL A 147     -22.968  19.980   2.424  1.00 54.15           C  
+ANISOU 1076  CG1 VAL A 147     7688   6687   6199   -123   1102    161       C  
+ATOM   1077  CG2 VAL A 147     -24.407  19.163   4.305  1.00 41.82           C  
+ANISOU 1077  CG2 VAL A 147     6464   5069   4357   -406   1192     82       C  
+ATOM   1078  N   VAL A 148     -24.910  21.480   0.287  1.00 67.30           N  
+ANISOU 1078  N   VAL A 148     8902   8790   7879     -4   1330    144       N  
+ATOM   1079  CA  VAL A 148     -24.722  21.681  -1.144  1.00 52.85           C  
+ANISOU 1079  CA  VAL A 148     6920   7063   6097     71   1327    181       C  
+ATOM   1080  C   VAL A 148     -23.268  22.009  -1.475  1.00 56.85           C  
+ANISOU 1080  C   VAL A 148     7418   7482   6703    144   1256    252       C  
+ATOM   1081  O   VAL A 148     -22.813  23.136  -1.282  1.00 63.97           O  
+ANISOU 1081  O   VAL A 148     8293   8339   7674    207   1217    313       O  
+ATOM   1082  CB  VAL A 148     -25.632  22.804  -1.679  1.00 45.30           C  
+ANISOU 1082  CB  VAL A 148     5823   6228   5161    130   1352    187       C  
+ATOM   1083  CG1 VAL A 148     -25.459  22.958  -3.181  1.00 49.61           C  
+ANISOU 1083  CG1 VAL A 148     6267   6865   5716    176   1331    237       C  
+ATOM   1084  CG2 VAL A 148     -27.083  22.511  -1.339  1.00 49.98           C  
+ANISOU 1084  CG2 VAL A 148     6376   6912   5700     62   1430     86       C  
+ATOM   1085  N   TYR A 149     -22.550  21.007  -1.974  1.00 43.33           N  
+ANISOU 1085  N   TYR A 149     5715   5741   5007    133   1239    229       N  
+ATOM   1086  CA  TYR A 149     -21.178  21.170  -2.439  1.00 45.72           C  
+ANISOU 1086  CA  TYR A 149     5962   5983   5425    192   1202    259       C  
+ATOM   1087  C   TYR A 149     -21.134  21.726  -3.855  1.00 52.43           C  
+ANISOU 1087  C   TYR A 149     6678   6980   6262    220   1272    296       C  
+ATOM   1088  O   TYR A 149     -21.523  21.050  -4.812  1.00 49.46           O  
+ANISOU 1088  O   TYR A 149     6269   6713   5811    195   1328    255       O  
+ATOM   1089  CB  TYR A 149     -20.421  19.839  -2.406  1.00 45.82           C  
+ANISOU 1089  CB  TYR A 149     6024   5899   5485    177   1151    183       C  
+ATOM   1090  CG  TYR A 149     -20.322  19.169  -1.054  1.00 45.79           C  
+ANISOU 1090  CG  TYR A 149     6202   5712   5483    129   1037    156       C  
+ATOM   1091  CD1 TYR A 149     -19.295  19.486  -0.176  1.00 51.36           C  
+ANISOU 1091  CD1 TYR A 149     6974   6230   6312    163    912    178       C  
+ATOM   1092  CD2 TYR A 149     -21.238  18.198  -0.667  1.00 52.72           C  
+ANISOU 1092  CD2 TYR A 149     7205   6591   6235     32   1039    110       C  
+ATOM   1093  CE1 TYR A 149     -19.191  18.868   1.056  1.00 47.40           C  
+ANISOU 1093  CE1 TYR A 149     6685   5535   5790    103    778    162       C  
+ATOM   1094  CE2 TYR A 149     -21.140  17.573   0.564  1.00 46.56           C  
+ANISOU 1094  CE2 TYR A 149     6637   5629   5423    -46    927     97       C  
+ATOM   1095  CZ  TYR A 149     -20.115  17.914   1.421  1.00 46.51           C  
+ANISOU 1095  CZ  TYR A 149     6721   5427   5523     -9    788    125       C  
+ATOM   1096  OH  TYR A 149     -20.010  17.300   2.648  1.00 63.38           O  
+ANISOU 1096  OH  TYR A 149     9114   7360   7608   -101    647    120       O  
+ATOM   1097  N   LYS A 150     -20.662  22.960  -3.985  1.00 61.36           N  
+ANISOU 1097  N   LYS A 150     7757   8103   7454    258   1259    380       N  
+ATOM   1098  CA  LYS A 150     -20.466  23.563  -5.294  1.00 51.27           C  
+ANISOU 1098  CA  LYS A 150     6393   6940   6148    254   1314    434       C  
+ATOM   1099  C   LYS A 150     -18.972  23.613  -5.600  1.00 48.17           C  
+ANISOU 1099  C   LYS A 150     5936   6496   5870    255   1340    438       C  
+ATOM   1100  O   LYS A 150     -18.298  24.599  -5.300  1.00 57.81           O  
+ANISOU 1100  O   LYS A 150     7133   7649   7185    270   1301    512       O  
+ATOM   1101  CB  LYS A 150     -21.096  24.956  -5.342  1.00 43.03           C  
+ANISOU 1101  CB  LYS A 150     5343   5923   5084    274   1267    527       C  
+ATOM   1102  CG  LYS A 150     -22.544  24.960  -4.869  1.00 43.57           C  
+ANISOU 1102  CG  LYS A 150     5435   6028   5093    285   1242    486       C  
+ATOM   1103  CD  LYS A 150     -23.150  26.351  -4.853  1.00 41.05           C  
+ANISOU 1103  CD  LYS A 150     5093   5711   4796    331   1166    548       C  
+ATOM   1104  CE  LYS A 150     -23.371  26.885  -6.256  1.00 41.05           C  
+ANISOU 1104  CE  LYS A 150     5065   5800   4733    314   1138    617       C  
+ATOM   1105  NZ  LYS A 150     -24.201  28.122  -6.232  1.00 44.68           N  
+ANISOU 1105  NZ  LYS A 150     5509   6242   5226    369   1018    654       N  
+HETATM 1106  N   MSE A 151     -18.472  22.527  -6.185  1.00 41.58           N  
+ANISOU 1106  N   MSE A 151     5064   5694   5042    240   1405    342       N  
+HETATM 1107  CA  MSE A 151     -17.045  22.332  -6.440  1.00 48.35           C  
+ANISOU 1107  CA  MSE A 151     5822   6504   6045    247   1446    289       C  
+HETATM 1108  C   MSE A 151     -16.412  23.482  -7.208  1.00 47.32           C  
+ANISOU 1108  C   MSE A 151     5613   6441   5927    202   1524    376       C  
+HETATM 1109  O   MSE A 151     -15.354  23.989  -6.836  1.00 76.24           O  
+ANISOU 1109  O   MSE A 151     9201  10014   9754    209   1504    392       O  
+HETATM 1110  CB  MSE A 151     -16.818  21.039  -7.228  1.00 60.06           C  
+ANISOU 1110  CB  MSE A 151     7264   8049   7506    239   1528    149       C  
+HETATM 1111  CG  MSE A 151     -17.409  19.789  -6.609  1.00 65.96           C  
+ANISOU 1111  CG  MSE A 151     8106   8725   8231    261   1442     63       C  
+HETATM 1112 SE   MSE A 151     -17.105  18.239  -7.750  1.00 92.94          SE  
+ANISOU 1112 SE   MSE A 151    11473  12215  11625    262   1528   -124      SE  
+HETATM 1113  CE  MSE A 151     -15.196  18.027  -7.439  1.00 68.09           C  
+ANISOU 1113  CE  MSE A 151     8164   8918   8791    331   1505   -253       C  
+ATOM   1114  N   HIS A 152     -17.073  23.881  -8.287  1.00 49.04           N  
+ANISOU 1114  N   HIS A 152     5860   6805   5969    141   1598    434       N  
+ATOM   1115  CA  HIS A 152     -16.494  24.811  -9.245  1.00 57.95           C  
+ANISOU 1115  CA  HIS A 152     6952   8010   7056     55   1688    514       C  
+ATOM   1116  C   HIS A 152     -16.747  26.264  -8.865  1.00 47.21           C  
+ANISOU 1116  C   HIS A 152     5642   6594   5702     50   1578    674       C  
+ATOM   1117  O   HIS A 152     -16.508  27.173  -9.659  1.00 49.18           O  
+ANISOU 1117  O   HIS A 152     5911   6896   5881    -41   1614    775       O  
+ATOM   1118  CB  HIS A 152     -17.032  24.514 -10.644  1.00 40.52           C  
+ANISOU 1118  CB  HIS A 152     4798   5964   4632    -26   1794    502       C  
+ATOM   1119  CG  HIS A 152     -16.424  23.297 -11.269  1.00 55.87           C  
+ANISOU 1119  CG  HIS A 152     6675   7974   6578    -41   1939    336       C  
+ATOM   1120  ND1 HIS A 152     -16.749  22.863 -12.536  1.00 75.35           N  
+ANISOU 1120  ND1 HIS A 152     9199  10582   8848   -117   2052    293       N  
+ATOM   1121  CD2 HIS A 152     -15.505  22.422 -10.797  1.00 54.98           C  
+ANISOU 1121  CD2 HIS A 152     6447   7791   6651     17   1971    189       C  
+ATOM   1122  CE1 HIS A 152     -16.058  21.773 -12.816  1.00 74.43           C  
+ANISOU 1122  CE1 HIS A 152     8997  10490   8792   -101   2167    116       C  
+ATOM   1123  NE2 HIS A 152     -15.295  21.484 -11.778  1.00 62.00           N  
+ANISOU 1123  NE2 HIS A 152     7309   8786   7464    -15   2112     47       N  
+ATOM   1124  N   GLY A 153     -17.237  26.478  -7.648  1.00 43.24           N  
+ANISOU 1124  N   GLY A 153     5179   5977   5274    137   1441    693       N  
+ATOM   1125  CA  GLY A 153     -17.413  27.823  -7.138  1.00 44.21           C  
+ANISOU 1125  CA  GLY A 153     5343   6021   5433    155   1322    816       C  
+ATOM   1126  C   GLY A 153     -18.834  28.343  -7.185  1.00 50.56           C  
+ANISOU 1126  C   GLY A 153     6227   6861   6124    186   1230    862       C  
+ATOM   1127  O   GLY A 153     -19.774  27.598  -7.461  1.00 51.42           O  
+ANISOU 1127  O   GLY A 153     6355   7048   6134    196   1252    795       O  
+ATOM   1128  N   ASP A 154     -18.991  29.634  -6.910  1.00 54.89           N  
+ANISOU 1128  N   ASP A 154     6811   7338   6706    205   1110    965       N  
+ATOM   1129  CA  ASP A 154     -20.312  30.244  -6.847  1.00 45.96           C  
+ANISOU 1129  CA  ASP A 154     5729   6213   5522    260    993    983       C  
+ATOM   1130  C   ASP A 154     -20.385  31.506  -7.706  1.00 48.04           C  
+ANISOU 1130  C   ASP A 154     6048   6468   5736    211    887   1119       C  
+ATOM   1131  O   ASP A 154     -19.393  32.217  -7.880  1.00 48.67           O  
+ANISOU 1131  O   ASP A 154     6141   6495   5856    146    880   1219       O  
+ATOM   1132  CB  ASP A 154     -20.675  30.563  -5.395  1.00 47.06           C  
+ANISOU 1132  CB  ASP A 154     5876   6240   5765    360    908    937       C  
+ATOM   1133  CG  ASP A 154     -22.060  31.162  -5.255  1.00 50.05           C  
+ANISOU 1133  CG  ASP A 154     6262   6628   6126    430    804    909       C  
+ATOM   1134  OD1 ASP A 154     -23.049  30.404  -5.348  1.00 64.66           O  
+ANISOU 1134  OD1 ASP A 154     8084   8564   7920    441    850    812       O  
+ATOM   1135  OD2 ASP A 154     -22.160  32.389  -5.045  1.00 51.92           O  
+ANISOU 1135  OD2 ASP A 154     6523   6780   6425    476    668    971       O  
+ATOM   1136  N   VAL A 155     -21.571  31.762  -8.247  1.00 49.38           N  
+ANISOU 1136  N   VAL A 155     6256   6679   5827    232    789   1121       N  
+ATOM   1137  CA  VAL A 155     -21.818  32.875  -9.160  1.00 51.73           C  
+ANISOU 1137  CA  VAL A 155     6646   6950   6059    180    640   1248       C  
+ATOM   1138  C   VAL A 155     -21.539  34.244  -8.524  1.00 53.49           C  
+ANISOU 1138  C   VAL A 155     6900   7024   6400    224    476   1338       C  
+ATOM   1139  O   VAL A 155     -21.134  35.183  -9.210  1.00 54.12           O  
+ANISOU 1139  O   VAL A 155     7074   7054   6434    134    378   1480       O  
+ATOM   1140  CB  VAL A 155     -23.274  32.834  -9.695  1.00 53.73           C  
+ANISOU 1140  CB  VAL A 155     6919   7243   6252    227    513   1203       C  
+ATOM   1141  CG1 VAL A 155     -24.276  32.904  -8.553  1.00 55.61           C  
+ANISOU 1141  CG1 VAL A 155     7062   7436   6629    380    441   1078       C  
+ATOM   1142  CG2 VAL A 155     -23.518  33.949 -10.704  1.00 56.03           C  
+ANISOU 1142  CG2 VAL A 155     7344   7476   6468    165    310   1342       C  
+ATOM   1143  N   GLU A 156     -21.719  34.347  -7.209  1.00 61.08           N  
+ANISOU 1143  N   GLU A 156     7802   7909   7498    347    446   1257       N  
+ATOM   1144  CA  GLU A 156     -21.453  35.598  -6.497  1.00 57.84           C  
+ANISOU 1144  CA  GLU A 156     7425   7347   7207    404    287   1320       C  
+ATOM   1145  C   GLU A 156     -19.972  35.790  -6.161  1.00 60.62           C  
+ANISOU 1145  C   GLU A 156     7779   7631   7622    333    349   1403       C  
+ATOM   1146  O   GLU A 156     -19.603  36.714  -5.435  1.00 53.12           O  
+ANISOU 1146  O   GLU A 156     6857   6544   6783    377    226   1450       O  
+ATOM   1147  CB  GLU A 156     -22.279  35.646  -5.210  1.00 62.18           C  
+ANISOU 1147  CB  GLU A 156     7925   7842   7861    557    242   1179       C  
+ATOM   1148  CG  GLU A 156     -22.852  37.008  -4.869  1.00 81.14           C  
+ANISOU 1148  CG  GLU A 156    10356  10113  10358    658     14   1191       C  
+ATOM   1149  CD  GLU A 156     -24.123  37.308  -5.636  1.00 83.94           C  
+ANISOU 1149  CD  GLU A 156    10696  10498  10698    706   -128   1153       C  
+ATOM   1150  OE1 GLU A 156     -24.660  36.384  -6.283  1.00 71.35           O  
+ANISOU 1150  OE1 GLU A 156     9062   9032   9014    666    -34   1103       O  
+ATOM   1151  OE2 GLU A 156     -24.590  38.465  -5.583  1.00 81.59           O  
+ANISOU 1151  OE2 GLU A 156    10427  10082  10492    788   -357   1166       O  
+ATOM   1152  N   HIS A 157     -19.133  34.913  -6.699  1.00 52.17           N  
+ANISOU 1152  N   HIS A 157     6670   6653   6500    227    532   1404       N  
+ATOM   1153  CA  HIS A 157     -17.687  34.970  -6.500  1.00 52.44           C  
+ANISOU 1153  CA  HIS A 157     6663   6638   6625    150    607   1454       C  
+ATOM   1154  C   HIS A 157     -16.981  34.573  -7.792  1.00 55.73           C  
+ANISOU 1154  C   HIS A 157     7062   7176   6935    -17    771   1498       C  
+ATOM   1155  O   HIS A 157     -16.306  33.544  -7.840  1.00 49.94           O  
+ANISOU 1155  O   HIS A 157     6234   6510   6230    -46    945   1407       O  
+ATOM   1156  CB  HIS A 157     -17.244  34.063  -5.349  1.00 50.85           C  
+ANISOU 1156  CB  HIS A 157     6388   6392   6539    229    680   1333       C  
+ATOM   1157  CG  HIS A 157     -17.766  34.482  -4.008  1.00 54.38           C  
+ANISOU 1157  CG  HIS A 157     6879   6712   7069    360    546   1287       C  
+ATOM   1158  ND1 HIS A 157     -17.139  35.430  -3.232  1.00 65.90           N  
+ANISOU 1158  ND1 HIS A 157     8371   8013   8654    388    415   1351       N  
+ATOM   1159  CD2 HIS A 157     -18.853  34.078  -3.308  1.00 51.33           C  
+ANISOU 1159  CD2 HIS A 157     6514   6338   6649    458    536   1174       C  
+ATOM   1160  CE1 HIS A 157     -17.815  35.593  -2.107  1.00 56.68           C  
+ANISOU 1160  CE1 HIS A 157     7257   6765   7515    504    332   1272       C  
+ATOM   1161  NE2 HIS A 157     -18.860  34.786  -2.130  1.00 53.05           N  
+ANISOU 1161  NE2 HIS A 157     6785   6413   6958    541    416   1161       N  
+ATOM   1162  N   PRO A 158     -17.140  35.391  -8.846  1.00 51.63           N  
+ANISOU 1162  N   PRO A 158     6648   6678   6290   -134    709   1628       N  
+ATOM   1163  CA  PRO A 158     -16.723  35.027 -10.206  1.00 51.06           C  
+ANISOU 1163  CA  PRO A 158     6610   6742   6050   -316    874   1662       C  
+ATOM   1164  C   PRO A 158     -15.232  34.735 -10.352  1.00 50.81           C  
+ANISOU 1164  C   PRO A 158     6463   6748   6093   -441   1080   1646       C  
+ATOM   1165  O   PRO A 158     -14.870  33.836 -11.108  1.00 53.44           O  
+ANISOU 1165  O   PRO A 158     6747   7218   6339   -527   1292   1564       O  
+ATOM   1166  CB  PRO A 158     -17.106  36.262 -11.038  1.00 57.64           C  
+ANISOU 1166  CB  PRO A 158     7626   7524   6752   -427    697   1836       C  
+ATOM   1167  CG  PRO A 158     -18.041  37.051 -10.181  1.00 55.08           C  
+ANISOU 1167  CG  PRO A 158     7337   7056   6533   -254    430   1849       C  
+ATOM   1168  CD  PRO A 158     -17.630  36.778  -8.779  1.00 52.72           C  
+ANISOU 1168  CD  PRO A 158     6902   6690   6438   -114    462   1752       C  
+ATOM   1169  N   SER A 159     -14.385  35.471  -9.642  1.00 51.80           N  
+ANISOU 1169  N   SER A 159     6536   6750   6394   -447   1017   1706       N  
+ATOM   1170  CA  SER A 159     -12.942  35.322  -9.804  1.00 52.28           C  
+ANISOU 1170  CA  SER A 159     6460   6838   6567   -576   1197   1685       C  
+ATOM   1171  C   SER A 159     -12.426  33.998  -9.241  1.00 51.76           C  
+ANISOU 1171  C   SER A 159     6211   6803   6651   -474   1338   1491       C  
+ATOM   1172  O   SER A 159     -11.379  33.504  -9.661  1.00 69.13           O  
+ANISOU 1172  O   SER A 159     8268   9074   8925   -573   1536   1410       O  
+ATOM   1173  CB  SER A 159     -12.217  36.489  -9.136  1.00 56.75           C  
+ANISOU 1173  CB  SER A 159     7017   7241   7305   -604   1053   1803       C  
+ATOM   1174  OG  SER A 159     -12.464  36.502  -7.741  1.00 59.41           O  
+ANISOU 1174  OG  SER A 159     7328   7431   7814   -399    882   1752       O  
+ATOM   1175  N   GLU A 160     -13.163  33.428  -8.293  1.00 51.27           N  
+ANISOU 1175  N   GLU A 160     6159   6682   6640   -285   1231   1406       N  
+ATOM   1176  CA  GLU A 160     -12.769  32.165  -7.678  1.00 54.91           C  
+ANISOU 1176  CA  GLU A 160     6494   7135   7234   -188   1308   1234       C  
+ATOM   1177  C   GLU A 160     -13.366  30.963  -8.406  1.00 51.78           C  
+ANISOU 1177  C   GLU A 160     6100   6891   6682   -184   1449   1118       C  
+ATOM   1178  O   GLU A 160     -13.061  29.816  -8.077  1.00 56.92           O  
+ANISOU 1178  O   GLU A 160     6660   7543   7425   -117   1513    967       O  
+ATOM   1179  CB  GLU A 160     -13.182  32.137  -6.203  1.00 52.09           C  
+ANISOU 1179  CB  GLU A 160     6180   6620   6993    -20   1121   1205       C  
+ATOM   1180  CG  GLU A 160     -12.559  33.238  -5.356  1.00 54.05           C  
+ANISOU 1180  CG  GLU A 160     6434   6695   7407     -5    961   1300       C  
+ATOM   1181  CD  GLU A 160     -11.066  33.052  -5.155  1.00 74.30           C  
+ANISOU 1181  CD  GLU A 160     8836   9191  10203    -53   1010   1253       C  
+ATOM   1182  OE1 GLU A 160     -10.576  31.916  -5.324  1.00 92.35           O  
+ANISOU 1182  OE1 GLU A 160    11001  11528  12559    -45   1134   1110       O  
+ATOM   1183  OE2 GLU A 160     -10.382  34.045  -4.828  1.00 90.97           O  
+ANISOU 1183  OE2 GLU A 160    10930  11188  12445    -95    911   1349       O  
+ATOM   1184  N   ALA A 161     -14.216  31.231  -9.391  1.00 48.01           N  
+ANISOU 1184  N   ALA A 161     5743   6522   5978   -255   1467   1188       N  
+ATOM   1185  CA  ALA A 161     -14.926  30.173 -10.102  1.00 49.04           C  
+ANISOU 1185  CA  ALA A 161     5903   6785   5944   -250   1567   1091       C  
+ATOM   1186  C   ALA A 161     -13.984  29.273 -10.897  1.00 49.30           C  
+ANISOU 1186  C   ALA A 161     5823   6932   5976   -341   1804    965       C  
+ATOM   1187  O   ALA A 161     -12.997  29.738 -11.469  1.00 47.18           O  
+ANISOU 1187  O   ALA A 161     5495   6701   5729   -481   1932    994       O  
+ATOM   1188  CB  ALA A 161     -15.976  30.775 -11.024  1.00 47.11           C  
+ANISOU 1188  CB  ALA A 161     5823   6606   5469   -316   1498   1203       C  
+ATOM   1189  N   VAL A 162     -14.296  27.981 -10.923  1.00 45.78           N  
+ANISOU 1189  N   VAL A 162     5345   6539   5512   -267   1866    814       N  
+ATOM   1190  CA  VAL A 162     -13.537  27.020 -11.715  1.00 58.58           C  
+ANISOU 1190  CA  VAL A 162     6860   8269   7127   -329   2084    657       C  
+ATOM   1191  C   VAL A 162     -14.251  26.719 -13.029  1.00 57.99           C  
+ANISOU 1191  C   VAL A 162     6914   8351   6766   -427   2185    657       C  
+ATOM   1192  O   VAL A 162     -15.334  26.133 -13.037  1.00 53.60           O  
+ANISOU 1192  O   VAL A 162     6449   7814   6102   -353   2103    634       O  
+ATOM   1193  CB  VAL A 162     -13.314  25.705 -10.947  1.00 64.92           C  
+ANISOU 1193  CB  VAL A 162     7555   9006   8105   -188   2065    473       C  
+ATOM   1194  CG1 VAL A 162     -12.548  24.712 -11.808  1.00 55.19           C  
+ANISOU 1194  CG1 VAL A 162     6202   7881   6887   -234   2280    282       C  
+ATOM   1195  CG2 VAL A 162     -12.578  25.972  -9.644  1.00 69.50           C  
+ANISOU 1195  CG2 VAL A 162     8041   9407   8961    -99   1934    473       C  
+ATOM   1196  N   LEU A 163     -13.645  27.129 -14.138  1.00 52.70           N  
+ANISOU 1196  N   LEU A 163     6265   7792   5968   -608   2363    682       N  
+ATOM   1197  CA  LEU A 163     -14.243  26.929 -15.454  1.00 66.62           C  
+ANISOU 1197  CA  LEU A 163     8193   9693   7427   -730   2454    693       C  
+ATOM   1198  C   LEU A 163     -13.602  25.760 -16.197  1.00 76.12           C  
+ANISOU 1198  C   LEU A 163     9303  11023   8598   -773   2707    475       C  
+ATOM   1199  O   LEU A 163     -14.291  24.986 -16.860  1.00 76.64           O  
+ANISOU 1199  O   LEU A 163     9472  11166   8481   -768   2732    405       O  
+ATOM   1200  CB  LEU A 163     -14.152  28.205 -16.298  1.00 71.25           C  
+ANISOU 1200  CB  LEU A 163     8942  10312   7819   -941   2468    881       C  
+ATOM   1201  CG  LEU A 163     -15.141  29.348 -16.022  1.00 69.99           C  
+ANISOU 1201  CG  LEU A 163     8956  10043   7593   -918   2184   1097       C  
+ATOM   1202  CD1 LEU A 163     -15.095  29.862 -14.586  1.00 60.34           C  
+ANISOU 1202  CD1 LEU A 163     7622   8664   6640   -758   2004   1142       C  
+ATOM   1203  CD2 LEU A 163     -14.910  30.483 -17.002  1.00 69.29           C  
+ANISOU 1203  CD2 LEU A 163     9054   9978   7294  -1158   2200   1272       C  
+ATOM   1204  N   ILE A 164     -12.284  25.633 -16.084  1.00 73.56           N  
+ANISOU 1204  N   ILE A 164     8771  10711   8469   -809   2887    352       N  
+ATOM   1205  CA  ILE A 164     -11.565  24.584 -16.799  1.00 68.99           C  
+ANISOU 1205  CA  ILE A 164     8067  10251   7894   -846   3145    109       C  
+ATOM   1206  C   ILE A 164     -10.871  23.625 -15.837  1.00 86.47           C  
+ANISOU 1206  C   ILE A 164    10031  12366  10459   -657   3117    -99       C  
+ATOM   1207  O   ILE A 164     -10.593  23.972 -14.688  1.00 86.50           O  
+ANISOU 1207  O   ILE A 164     9939  12216  10710   -553   2950    -45       O  
+ATOM   1208  CB  ILE A 164     -10.520  25.176 -17.763  1.00 63.74           C  
+ANISOU 1208  CB  ILE A 164     7354   9716   7147  -1089   3435     88       C  
+ATOM   1209  CG1 ILE A 164      -9.561  26.100 -17.010  1.00 57.21           C  
+ANISOU 1209  CG1 ILE A 164     6355   8796   6587  -1120   3415    161       C  
+ATOM   1210  CG2 ILE A 164     -11.206  25.931 -18.889  1.00 72.95           C  
+ANISOU 1210  CG2 ILE A 164     8825  10978   7914  -1304   3462    274       C  
+ATOM   1211  CD1 ILE A 164      -8.586  26.836 -17.909  1.00 79.25           C  
+ANISOU 1211  CD1 ILE A 164     9108  11711   9292  -1398   3696    172       C  
+ATOM   1212  N   LYS A 165     -10.605  22.413 -16.318  1.00 87.41           N  
+ANISOU 1212  N   LYS A 165    10685  12058  10471   -897   1335    786       N  
+ATOM   1213  CA  LYS A 165      -9.935  21.378 -15.533  1.00 85.27           C  
+ANISOU 1213  CA  LYS A 165    10338  11839  10223   -758   1313    607       C  
+ATOM   1214  C   LYS A 165      -8.559  21.815 -15.033  1.00 83.51           C  
+ANISOU 1214  C   LYS A 165     9910  11705  10113   -803   1351    541       C  
+ATOM   1215  O   LYS A 165      -8.070  21.307 -14.022  1.00 86.51           O  
+ANISOU 1215  O   LYS A 165    10209  12107  10553   -690   1291    417       O  
+ATOM   1216  CB  LYS A 165      -9.800  20.096 -16.358  1.00 80.02           C  
+ANISOU 1216  CB  LYS A 165     9706  11305   9394   -658   1392    527       C  
+ATOM   1217  N   ASP A 166      -7.948  22.755 -15.750  1.00 62.98           N  
+ANISOU 1217  N   ASP A 166     7223   9172   7533   -973   1455    629       N  
+ATOM   1218  CA  ASP A 166      -6.617  23.265 -15.425  1.00 62.18           C  
+ANISOU 1218  CA  ASP A 166     6906   9185   7537  -1065   1513    562       C  
+ATOM   1219  C   ASP A 166      -6.448  23.656 -13.959  1.00 68.92           C  
+ANISOU 1219  C   ASP A 166     7684   9956   8547  -1060   1396    465       C  
+ATOM   1220  O   ASP A 166      -5.369  23.483 -13.394  1.00 71.04           O  
+ANISOU 1220  O   ASP A 166     7753  10375   8862  -1039   1395    338       O  
+ATOM   1221  CB  ASP A 166      -6.284  24.468 -16.311  1.00 54.68           C  
+ANISOU 1221  CB  ASP A 166     5923   8241   6612  -1294   1641    705       C  
+ATOM   1222  CG  ASP A 166      -6.133  24.092 -17.771  1.00 87.27           C  
+ANISOU 1222  CG  ASP A 166    10073  12525  10562  -1311   1778    784       C  
+ATOM   1223  OD1 ASP A 166      -5.008  24.209 -18.303  1.00 92.93           O  
+ANISOU 1223  OD1 ASP A 166    10624  13422  11262  -1400   1912    760       O  
+ATOM   1224  OD2 ASP A 166      -7.135  23.666 -18.383  1.00 86.50           O  
+ANISOU 1224  OD2 ASP A 166    10146  12392  10330  -1242   1753    859       O  
+ATOM   1225  N   ASP A 167      -7.507  24.179 -13.347  1.00 65.54           N  
+ANISOU 1225  N   ASP A 167     7402   9313   8188  -1075   1297    517       N  
+ATOM   1226  CA  ASP A 167      -7.448  24.588 -11.946  1.00 59.93           C  
+ANISOU 1226  CA  ASP A 167     6638   8524   7610  -1079   1187    415       C  
+ATOM   1227  C   ASP A 167      -7.093  23.417 -11.039  1.00 53.15           C  
+ANISOU 1227  C   ASP A 167     5708   7781   6704   -871   1096    269       C  
+ATOM   1228  O   ASP A 167      -6.245  23.551 -10.152  1.00 58.15           O  
+ANISOU 1228  O   ASP A 167     6169   8525   7402   -874   1050    150       O  
+ATOM   1229  CB  ASP A 167      -8.775  25.204 -11.508  1.00 69.09           C  
+ANISOU 1229  CB  ASP A 167     7985   9434   8832  -1097   1107    494       C  
+ATOM   1230  CG  ASP A 167      -8.997  26.575 -12.099  1.00 68.01           C  
+ANISOU 1230  CG  ASP A 167     7900   9153   8787  -1294   1191    636       C  
+ATOM   1231  OD1 ASP A 167      -8.025  27.146 -12.636  1.00 58.71           O  
+ANISOU 1231  OD1 ASP A 167     6602   8058   7649  -1449   1309    654       O  
+ATOM   1232  OD2 ASP A 167     -10.133  27.087 -12.023  1.00 88.31           O  
+ANISOU 1232  OD2 ASP A 167    10632  11527  11396  -1288   1150    736       O  
+ATOM   1233  N   TYR A 168      -7.718  22.267 -11.289  1.00 58.67           N  
+ANISOU 1233  N   TYR A 168     6539   8466   7288   -693   1077    280       N  
+ATOM   1234  CA  TYR A 168      -7.398  21.039 -10.564  1.00 55.98           C  
+ANISOU 1234  CA  TYR A 168     6164   8209   6895   -470   1020    172       C  
+ATOM   1235  C   TYR A 168      -5.901  20.760 -10.601  1.00 61.14           C  
+ANISOU 1235  C   TYR A 168     6575   9109   7546   -426   1076     82       C  
+ATOM   1236  O   TYR A 168      -5.332  20.238  -9.644  1.00 60.65           O  
+ANISOU 1236  O   TYR A 168     6403   9151   7490   -277   1003    -11       O  
+ATOM   1237  CB  TYR A 168      -8.153  19.843 -11.149  1.00 51.06           C  
+ANISOU 1237  CB  TYR A 168     5721   7530   6150   -324   1048    194       C  
+ATOM   1238  CG  TYR A 168      -9.643  19.818 -10.894  1.00 52.96           C  
+ANISOU 1238  CG  TYR A 168     6178   7566   6378   -321    974    251       C  
+ATOM   1239  CD1 TYR A 168     -10.529  20.454 -11.753  1.00 52.05           C  
+ANISOU 1239  CD1 TYR A 168     6171   7365   6240   -453   1001    363       C  
+ATOM   1240  CD2 TYR A 168     -10.167  19.121  -9.812  1.00 64.85           C  
+ANISOU 1240  CD2 TYR A 168     7772   8983   7884   -175    883    200       C  
+ATOM   1241  CE1 TYR A 168     -11.895  20.419 -11.526  1.00 65.12           C  
+ANISOU 1241  CE1 TYR A 168     7995   8867   7882   -442    931    408       C  
+ATOM   1242  CE2 TYR A 168     -11.529  19.079  -9.578  1.00 67.73           C  
+ANISOU 1242  CE2 TYR A 168     8317   9181   8238   -182    827    242       C  
+ATOM   1243  CZ  TYR A 168     -12.388  19.729 -10.437  1.00 70.11           C  
+ANISOU 1243  CZ  TYR A 168     8701   9415   8524   -315    848    338       C  
+ATOM   1244  OH  TYR A 168     -13.744  19.688 -10.203  1.00 64.97           O  
+ANISOU 1244  OH  TYR A 168     8199   8628   7860   -315    790    374       O  
+ATOM   1245  N   GLU A 169      -5.274  21.112 -11.718  1.00 66.57           N  
+ANISOU 1245  N   GLU A 169     7171   9908   8216   -551   1208    117       N  
+ATOM   1246  CA  GLU A 169      -3.848  20.892 -11.904  1.00 68.71           C  
+ANISOU 1246  CA  GLU A 169     7188  10437   8481   -526   1283     32       C  
+ATOM   1247  C   GLU A 169      -3.014  21.965 -11.209  1.00 64.59           C  
+ANISOU 1247  C   GLU A 169     6445  10016   8080   -698   1253    -33       C  
+ATOM   1248  O   GLU A 169      -1.935  21.679 -10.691  1.00 82.18           O  
+ANISOU 1248  O   GLU A 169     8436  12471  10317   -620   1233   -146       O  
+ATOM   1249  CB  GLU A 169      -3.510  20.859 -13.395  1.00 69.64           C  
+ANISOU 1249  CB  GLU A 169     7291  10650   8520   -609   1454     88       C  
+ATOM   1250  CG  GLU A 169      -4.443  19.992 -14.221  1.00 78.15           C  
+ANISOU 1250  CG  GLU A 169     8599  11628   9469   -506   1493    142       C  
+ATOM   1251  CD  GLU A 169      -4.275  20.223 -15.708  1.00 72.04           C  
+ANISOU 1251  CD  GLU A 169     7830  10944   8598   -637   1652    216       C  
+ATOM   1252  OE1 GLU A 169      -3.315  20.922 -16.096  1.00 76.91           O  
+ANISOU 1252  OE1 GLU A 169     8262  11710   9250   -784   1749    224       O  
+ATOM   1253  OE2 GLU A 169      -5.109  19.720 -16.488  1.00 54.25           O  
+ANISOU 1253  OE2 GLU A 169     5761   8626   6224   -605   1684    262       O  
+ATOM   1254  N   LYS A 170      -3.516  23.198 -11.193  1.00 62.75           N  
+ANISOU 1254  N   LYS A 170     6285   9617   7940   -928   1252     31       N  
+ATOM   1255  CA  LYS A 170      -2.748  24.311 -10.638  1.00 79.86           C  
+ANISOU 1255  CA  LYS A 170     8258  11850  10234  -1142   1252    -47       C  
+ATOM   1256  C   LYS A 170      -2.984  24.469  -9.144  1.00 72.68           C  
+ANISOU 1256  C   LYS A 170     7334  10896   9385  -1096   1088   -153       C  
+ATOM   1257  O   LYS A 170      -2.046  24.676  -8.374  1.00 76.84           O  
+ANISOU 1257  O   LYS A 170     7626  11618   9951  -1136   1041   -294       O  
+ATOM   1258  CB  LYS A 170      -3.096  25.622 -11.347  1.00 91.96           C  
+ANISOU 1258  CB  LYS A 170     9885  13202  11855  -1421   1359     73       C  
+ATOM   1259  CG  LYS A 170      -3.078  25.556 -12.861  1.00 88.80           C  
+ANISOU 1259  CG  LYS A 170     9545  12827  11368  -1474   1519    214       C  
+ATOM   1260  CD  LYS A 170      -3.794  26.759 -13.449  1.00 84.79           C  
+ANISOU 1260  CD  LYS A 170     9209  12080  10929  -1682   1594    384       C  
+ATOM   1261  CE  LYS A 170      -3.545  26.886 -14.939  1.00 89.30           C  
+ANISOU 1261  CE  LYS A 170     9798  12726  11406  -1777   1769    529       C  
+ATOM   1262  NZ  LYS A 170      -4.274  28.054 -15.502  1.00 92.18           N  
+ANISOU 1262  NZ  LYS A 170    10344  12852  11829  -1948   1840    729       N  
+ATOM   1263  N   TYR A 171      -4.244  24.369  -8.741  1.00 79.26           N  
+ANISOU 1263  N   TYR A 171     8408  11495  10212  -1016   1002    -92       N  
+ATOM   1264  CA  TYR A 171      -4.619  24.595  -7.354  1.00 87.22           C  
+ANISOU 1264  CA  TYR A 171     9434  12439  11266   -987    858   -184       C  
+ATOM   1265  C   TYR A 171      -5.313  23.372  -6.775  1.00 78.88           C  
+ANISOU 1265  C   TYR A 171     8516  11352  10104   -706    754   -174       C  
+ATOM   1266  O   TYR A 171      -6.533  23.347  -6.623  1.00 71.86           O  
+ANISOU 1266  O   TYR A 171     7849  10244   9212   -671    713   -104       O  
+ATOM   1267  CB  TYR A 171      -5.517  25.829  -7.245  1.00 78.02           C  
+ANISOU 1267  CB  TYR A 171     8426  10999  10221  -1183    866   -131       C  
+ATOM   1268  CG  TYR A 171      -5.171  26.910  -8.245  1.00 66.06           C  
+ANISOU 1268  CG  TYR A 171     6884   9419   8799  -1439   1019    -55       C  
+ATOM   1269  CD1 TYR A 171      -4.020  27.673  -8.097  1.00 66.28           C  
+ANISOU 1269  CD1 TYR A 171     6686   9581   8917  -1651   1080   -166       C  
+ATOM   1270  CD2 TYR A 171      -5.986  27.160  -9.343  1.00 74.43           C  
+ANISOU 1270  CD2 TYR A 171     8138  10296   9845  -1474   1107    133       C  
+ATOM   1271  CE1 TYR A 171      -3.693  28.661  -9.007  1.00 75.10           C  
+ANISOU 1271  CE1 TYR A 171     7792  10619  10122  -1898   1242    -84       C  
+ATOM   1272  CE2 TYR A 171      -5.666  28.146 -10.260  1.00 84.17           C  
+ANISOU 1272  CE2 TYR A 171     9363  11467  11151  -1696   1256    233       C  
+ATOM   1273  CZ  TYR A 171      -4.519  28.893 -10.087  1.00 84.89           C  
+ANISOU 1273  CZ  TYR A 171     9248  11662  11345  -1911   1332    128       C  
+ATOM   1274  OH  TYR A 171      -4.198  29.874 -10.997  1.00 94.70           O  
+ANISOU 1274  OH  TYR A 171    10495  12822  12664  -2146   1503    239       O  
+ATOM   1275  N   SER A 172      -4.520  22.355  -6.456  1.00 83.06           N  
+ANISOU 1275  N   SER A 172     8907  12103  10550   -503    721   -238       N  
+ATOM   1276  CA  SER A 172      -5.047  21.125  -5.885  1.00 75.79           C  
+ANISOU 1276  CA  SER A 172     8117  11149   9532   -228    643   -221       C  
+ATOM   1277  C   SER A 172      -5.395  21.325  -4.416  1.00 67.77           C  
+ANISOU 1277  C   SER A 172     7114  10113   8521   -188    497   -288       C  
+ATOM   1278  O   SER A 172      -6.248  20.629  -3.872  1.00 69.10           O  
+ANISOU 1278  O   SER A 172     7464  10160   8632    -29    437   -248       O  
+ATOM   1279  CB  SER A 172      -4.039  19.984  -6.038  1.00 86.36           C  
+ANISOU 1279  CB  SER A 172     9309  12717  10787      2    672   -253       C  
+ATOM   1280  OG  SER A 172      -3.485  19.960  -7.341  1.00101.34           O  
+ANISOU 1280  OG  SER A 172    11135  14688  12680    -65    817   -226       O  
+ATOM   1281  N   ILE A 173      -4.736  22.290  -3.784  1.00 67.10           N  
+ANISOU 1281  N   ILE A 173     6839  10155   8503   -352    450   -400       N  
+ATOM   1282  CA  ILE A 173      -4.948  22.566  -2.368  1.00 69.22           C  
+ANISOU 1282  CA  ILE A 173     7091  10450   8760   -337    312   -493       C  
+ATOM   1283  C   ILE A 173      -6.380  23.025  -2.083  1.00 70.03           C  
+ANISOU 1283  C   ILE A 173     7454  10249   8908   -404    291   -443       C  
+ATOM   1284  O   ILE A 173      -6.886  22.848  -0.974  1.00 69.28           O  
+ANISOU 1284  O   ILE A 173     7426  10134   8763   -314    187   -483       O  
+ATOM   1285  CB  ILE A 173      -3.940  23.626  -1.849  1.00 73.72           C  
+ANISOU 1285  CB  ILE A 173     7392  11219   9398   -553    283   -656       C  
+ATOM   1286  CG1 ILE A 173      -3.923  23.658  -0.319  1.00 79.55           C  
+ANISOU 1286  CG1 ILE A 173     8065  12087  10071   -489    126   -779       C  
+ATOM   1287  CG2 ILE A 173      -4.239  25.004  -2.431  1.00 72.12           C  
+ANISOU 1287  CG2 ILE A 173     7243  10808   9352   -874    382   -660       C  
+ATOM   1288  CD1 ILE A 173      -2.731  24.384   0.261  1.00 90.86           C  
+ANISOU 1288  CD1 ILE A 173     9182  13819  11524   -654     78   -970       C  
+ATOM   1289  N   LYS A 174      -7.036  23.608  -3.083  1.00 66.92           N  
+ANISOU 1289  N   LYS A 174     7197   9635   8596   -552    390   -350       N  
+ATOM   1290  CA  LYS A 174      -8.418  24.044  -2.918  1.00 65.98           C  
+ANISOU 1290  CA  LYS A 174     7307   9241   8521   -597    377   -291       C  
+ATOM   1291  C   LYS A 174      -9.421  23.069  -3.537  1.00 62.83           C  
+ANISOU 1291  C   LYS A 174     7119   8709   8044   -441    403   -157       C  
+ATOM   1292  O   LYS A 174     -10.614  23.128  -3.238  1.00 61.43           O  
+ANISOU 1292  O   LYS A 174     7119   8350   7872   -422    373   -115       O  
+ATOM   1293  CB  LYS A 174      -8.609  25.445  -3.509  1.00 72.11           C  
+ANISOU 1293  CB  LYS A 174     8105   9849   9445   -854    462   -265       C  
+ATOM   1294  CG  LYS A 174      -9.117  25.486  -4.942  1.00 64.74           C  
+ANISOU 1294  CG  LYS A 174     7297   8782   8521   -891    573    -96       C  
+ATOM   1295  CD  LYS A 174      -9.519  26.906  -5.321  1.00 63.92           C  
+ANISOU 1295  CD  LYS A 174     7258   8466   8563  -1108    648    -42       C  
+ATOM   1296  CE  LYS A 174     -10.201  26.966  -6.678  1.00 67.46           C  
+ANISOU 1296  CE  LYS A 174     7849   8790   8994  -1118    739    153       C  
+ATOM   1297  NZ  LYS A 174     -10.650  28.351  -7.002  1.00 58.73           N  
+ANISOU 1297  NZ  LYS A 174     6826   7458   8031  -1292    814    237       N  
+HETATM 1298  N   MSE A 175      -8.939  22.170  -4.391  1.00 60.96           N  
+ANISOU 1298  N   MSE A 175     6856   8571   7734   -337    466   -107       N  
+HETATM 1299  CA  MSE A 175      -9.826  21.247  -5.099  1.00 57.41           C  
+ANISOU 1299  CA  MSE A 175     6599   8005   7209   -224    509     -8       C  
+HETATM 1300  C   MSE A 175      -9.834  19.839  -4.506  1.00 58.56           C  
+ANISOU 1300  C   MSE A 175     6802   8198   7250     22    471    -25       C  
+HETATM 1301  O   MSE A 175     -10.857  19.157  -4.534  1.00 59.61           O  
+ANISOU 1301  O   MSE A 175     7127   8188   7334    101    475     25       O  
+HETATM 1302  CB  MSE A 175      -9.445  21.173  -6.580  1.00 54.67           C  
+ANISOU 1302  CB  MSE A 175     6227   7701   6843   -285    631     58       C  
+HETATM 1303  CG  MSE A 175      -9.569  22.492  -7.325  1.00 59.30           C  
+ANISOU 1303  CG  MSE A 175     6802   8209   7519   -515    693    123       C  
+HETATM 1304 SE   MSE A 175     -11.304  23.347  -7.071  1.00 93.70          SE  
+ANISOU 1304 SE   MSE A 175    11377  12280  11943   -595    643    209      SE  
+HETATM 1305  CE  MSE A 175     -12.457  21.931  -7.747  1.00 49.51           C  
+ANISOU 1305  CE  MSE A 175     5980   6634   6196   -433    652    282       C  
+ATOM   1306  N   ASP A 176      -8.693  19.406  -3.980  1.00 61.14           N  
+ANISOU 1306  N   ASP A 176     6960   8729   7543    144    440    -90       N  
+ATOM   1307  CA  ASP A 176      -8.564  18.063  -3.409  1.00 61.96           C  
+ANISOU 1307  CA  ASP A 176     7115   8878   7550    409    416    -84       C  
+ATOM   1308  C   ASP A 176      -9.522  17.746  -2.247  1.00 62.52           C  
+ANISOU 1308  C   ASP A 176     7348   8828   7580    496    331    -70       C  
+ATOM   1309  O   ASP A 176     -10.047  16.634  -2.190  1.00 61.84           O  
+ANISOU 1309  O   ASP A 176     7430   8638   7429    657    362    -17       O  
+ATOM   1310  CB  ASP A 176      -7.121  17.812  -2.961  1.00 64.54           C  
+ANISOU 1310  CB  ASP A 176     7195   9482   7846    537    382   -148       C  
+ATOM   1311  CG  ASP A 176      -6.195  17.521  -4.127  1.00 62.73           C  
+ANISOU 1311  CG  ASP A 176     6839   9377   7620    554    496   -150       C  
+ATOM   1312  OD1 ASP A 176      -6.638  17.657  -5.287  1.00 61.36           O  
+ANISOU 1312  OD1 ASP A 176     6765   9082   7468    434    598   -106       O  
+ATOM   1313  OD2 ASP A 176      -5.028  17.149  -3.885  1.00 69.83           O  
+ANISOU 1313  OD2 ASP A 176     7529  10513   8488    694    485   -195       O  
+ATOM   1314  N   PRO A 177      -9.732  18.690  -1.305  1.00 63.12           N  
+ANISOU 1314  N   PRO A 177     7377   8916   7691    387    237   -125       N  
+ATOM   1315  CA  PRO A 177     -10.689  18.355  -0.241  1.00 62.34           C  
+ANISOU 1315  CA  PRO A 177     7437   8710   7538    469    173   -110       C  
+ATOM   1316  C   PRO A 177     -12.089  18.017  -0.766  1.00 60.30           C  
+ANISOU 1316  C   PRO A 177     7419   8204   7287    437    235    -34       C  
+ATOM   1317  O   PRO A 177     -12.738  17.090  -0.264  1.00 59.05           O  
+ANISOU 1317  O   PRO A 177     7420   7960   7058    569    237      7       O  
+ATOM   1318  CB  PRO A 177     -10.724  19.631   0.605  1.00 62.08           C  
+ANISOU 1318  CB  PRO A 177     7310   8716   7559    307     88   -205       C  
+ATOM   1319  CG  PRO A 177      -9.390  20.248   0.395  1.00 63.75           C  
+ANISOU 1319  CG  PRO A 177     7269   9140   7813    222     80   -286       C  
+ATOM   1320  CD  PRO A 177      -9.063  19.979  -1.043  1.00 64.39           C  
+ANISOU 1320  CD  PRO A 177     7340   9195   7929    200    194   -220       C  
+ATOM   1321  N   TYR A 178     -12.531  18.742  -1.789  1.00 58.77           N  
+ANISOU 1321  N   TYR A 178     7248   7911   7171    261    290    -11       N  
+ATOM   1322  CA  TYR A 178     -13.821  18.469  -2.412  1.00 54.93           C  
+ANISOU 1322  CA  TYR A 178     6952   7241   6680    221    341     55       C  
+ATOM   1323  C   TYR A 178     -13.827  17.111  -3.107  1.00 54.32           C  
+ANISOU 1323  C   TYR A 178     6976   7139   6525    347    424     91       C  
+ATOM   1324  O   TYR A 178     -14.815  16.382  -3.053  1.00 59.20           O  
+ANISOU 1324  O   TYR A 178     7765   7628   7099    384    452    117       O  
+ATOM   1325  CB  TYR A 178     -14.179  19.572  -3.411  1.00 51.74           C  
+ANISOU 1325  CB  TYR A 178     6528   6772   6359     29    377     92       C  
+ATOM   1326  CG  TYR A 178     -14.761  20.804  -2.762  1.00 51.38           C  
+ANISOU 1326  CG  TYR A 178     6477   6641   6402    -91    322     70       C  
+ATOM   1327  CD1 TYR A 178     -13.950  21.868  -2.390  1.00 58.50           C  
+ANISOU 1327  CD1 TYR A 178     7232   7607   7388   -195    296      5       C  
+ATOM   1328  CD2 TYR A 178     -16.121  20.894  -2.502  1.00 48.27           C  
+ANISOU 1328  CD2 TYR A 178     6222   6104   6013   -103    306    100       C  
+ATOM   1329  CE1 TYR A 178     -14.481  22.993  -1.789  1.00 54.77           C  
+ANISOU 1329  CE1 TYR A 178     6771   7030   7009   -304    264    -34       C  
+ATOM   1330  CE2 TYR A 178     -16.660  22.013  -1.902  1.00 52.06           C  
+ANISOU 1330  CE2 TYR A 178     6700   6497   6582   -192    269     72       C  
+ATOM   1331  CZ  TYR A 178     -15.836  23.058  -1.547  1.00 52.48           C  
+ANISOU 1331  CZ  TYR A 178     6626   6588   6724   -289    252      3       C  
+ATOM   1332  OH  TYR A 178     -16.375  24.170  -0.947  1.00 58.58           O  
+ANISOU 1332  OH  TYR A 178     7413   7248   7597   -378    234    -43       O  
+ATOM   1333  N   ILE A 179     -12.719  16.782  -3.761  1.00 55.63           N  
+ANISOU 1333  N   ILE A 179     7031   7428   6677    401    477     80       N  
+ATOM   1334  CA  ILE A 179     -12.566  15.495  -4.427  1.00 55.42           C  
+ANISOU 1334  CA  ILE A 179     7092   7378   6585    532    574     91       C  
+ATOM   1335  C   ILE A 179     -12.588  14.348  -3.422  1.00 57.58           C  
+ANISOU 1335  C   ILE A 179     7469   7608   6802    747    564     99       C  
+ATOM   1336  O   ILE A 179     -13.222  13.317  -3.657  1.00 56.88           O  
+ANISOU 1336  O   ILE A 179     7563   7376   6672    812    642    115       O  
+ATOM   1337  CB  ILE A 179     -11.270  15.461  -5.252  1.00 56.12           C  
+ANISOU 1337  CB  ILE A 179     7015   7633   6677    560    637     67       C  
+ATOM   1338  CG1 ILE A 179     -11.436  16.365  -6.472  1.00 52.86           C  
+ANISOU 1338  CG1 ILE A 179     6562   7228   6296    348    686     88       C  
+ATOM   1339  CG2 ILE A 179     -10.939  14.046  -5.696  1.00 56.40           C  
+ANISOU 1339  CG2 ILE A 179     7131   7647   6650    746    741     57       C  
+ATOM   1340  CD1 ILE A 179     -10.157  16.706  -7.167  1.00 75.56           C  
+ANISOU 1340  CD1 ILE A 179     9239  10284   9186    317    742     66       C  
+ATOM   1341  N   LYS A 180     -11.893  14.539  -2.305  1.00 59.39           N  
+ANISOU 1341  N   LYS A 180     7581   7963   7021    850    474     87       N  
+ATOM   1342  CA  LYS A 180     -11.889  13.567  -1.216  1.00 60.26           C  
+ANISOU 1342  CA  LYS A 180     7783   8052   7060   1069    451    123       C  
+ATOM   1343  C   LYS A 180     -13.305  13.325  -0.698  1.00 59.23           C  
+ANISOU 1343  C   LYS A 180     7873   7723   6910   1020    454    156       C  
+ATOM   1344  O   LYS A 180     -13.765  12.173  -0.608  1.00 61.48           O  
+ANISOU 1344  O   LYS A 180     8345   7863   7151   1135    533    199       O  
+ATOM   1345  CB  LYS A 180     -10.984  14.046  -0.077  1.00 59.42           C  
+ANISOU 1345  CB  LYS A 180     7486   8165   6924   1153    328     99       C  
+ATOM   1346  CG  LYS A 180      -9.498  13.981  -0.395  1.00 60.36           C  
+ANISOU 1346  CG  LYS A 180     7374   8516   7043   1260    329     70       C  
+ATOM   1347  CD  LYS A 180      -8.665  14.671   0.672  1.00 61.72           C  
+ANISOU 1347  CD  LYS A 180     7321   8947   7184   1281    192     16       C  
+ATOM   1348  CE  LYS A 180      -7.195  14.298   0.549  1.00 73.10           C  
+ANISOU 1348  CE  LYS A 180     8528  10649   8597   1456    189     -2       C  
+ATOM   1349  NZ  LYS A 180      -6.455  14.623   1.799  1.00 81.91           N  
+ANISOU 1349  NZ  LYS A 180     9442  12043   9635   1543     42    -43       N  
+ATOM   1350  N   ALA A 181     -13.991  14.422  -0.382  1.00 56.87           N  
+ANISOU 1350  N   ALA A 181     7549   7409   6651    842    382    130       N  
+ATOM   1351  CA  ALA A 181     -15.362  14.371   0.117  1.00 56.46           C  
+ANISOU 1351  CA  ALA A 181     7668   7199   6587    776    381    148       C  
+ATOM   1352  C   ALA A 181     -16.279  13.636  -0.861  1.00 55.84           C  
+ANISOU 1352  C   ALA A 181     7758   6950   6507    718    492    167       C  
+ATOM   1353  O   ALA A 181     -17.082  12.785  -0.465  1.00 59.77           O  
+ANISOU 1353  O   ALA A 181     8432   7315   6963    760    544    192       O  
+ATOM   1354  CB  ALA A 181     -15.881  15.778   0.375  1.00 53.58           C  
+ANISOU 1354  CB  ALA A 181     7226   6846   6287    594    304    106       C  
+ATOM   1355  N   LEU A 182     -16.143  13.968  -2.141  1.00 52.71           N  
+ANISOU 1355  N   LEU A 182     7306   6573   6150    609    535    150       N  
+ATOM   1356  CA  LEU A 182     -16.950  13.358  -3.191  1.00 50.48           C  
+ANISOU 1356  CA  LEU A 182     7154   6178   5848    530    632    144       C  
+ATOM   1357  C   LEU A 182     -16.686  11.862  -3.328  1.00 51.88           C  
+ANISOU 1357  C   LEU A 182     7468   6270   5976    679    745    138       C  
+ATOM   1358  O   LEU A 182     -17.616  11.080  -3.515  1.00 53.23           O  
+ANISOU 1358  O   LEU A 182     7809   6297   6120    638    823    123       O  
+ATOM   1359  CB  LEU A 182     -16.688  14.051  -4.528  1.00 47.90           C  
+ANISOU 1359  CB  LEU A 182     6722   5931   5546    400    652    136       C  
+ATOM   1360  CG  LEU A 182     -17.449  13.504  -5.737  1.00 50.08           C  
+ANISOU 1360  CG  LEU A 182     7105   6149   5776    305    741    116       C  
+ATOM   1361  CD1 LEU A 182     -18.946  13.429  -5.452  1.00 42.95           C  
+ANISOU 1361  CD1 LEU A 182     6322   5138   4859    210    728    116       C  
+ATOM   1362  CD2 LEU A 182     -17.167  14.353  -6.966  1.00 49.89           C  
+ANISOU 1362  CD2 LEU A 182     6966   6235   5754    182    747    133       C  
+ATOM   1363  N   SER A 183     -15.418  11.473  -3.250  1.00 54.44           N  
+ANISOU 1363  N   SER A 183     7711   6681   6293    850    761    143       N  
+ATOM   1364  CA  SER A 183     -15.042  10.067  -3.325  1.00 56.21           C  
+ANISOU 1364  CA  SER A 183     8063   6807   6485   1033    879    146       C  
+ATOM   1365  C   SER A 183     -15.706   9.290  -2.196  1.00 66.64           C  
+ANISOU 1365  C   SER A 183     9570   7974   7775   1129    896    198       C  
+ATOM   1366  O   SER A 183     -16.350   8.254  -2.424  1.00 58.69           O  
+ANISOU 1366  O   SER A 183     8768   6776   6756   1131   1020    187       O  
+ATOM   1367  CB  SER A 183     -13.523   9.908  -3.259  1.00 57.86           C  
+ANISOU 1367  CB  SER A 183     8117   7173   6695   1234    874    156       C  
+ATOM   1368  OG  SER A 183     -12.904  10.449  -4.412  1.00 75.87           O  
+ANISOU 1368  OG  SER A 183    10246   9582   8999   1140    897    105       O  
+ATOM   1369  N   GLY A 184     -15.560   9.815  -0.980  1.00 67.61           N  
+ANISOU 1369  N   GLY A 184     9624   8186   7880   1192    780    248       N  
+ATOM   1370  CA  GLY A 184     -16.179   9.205   0.183  1.00 53.69           C  
+ANISOU 1370  CA  GLY A 184     8024   6307   6068   1278    789    314       C  
+ATOM   1371  C   GLY A 184     -17.682   9.063   0.021  1.00 51.72           C  
+ANISOU 1371  C   GLY A 184     7942   5884   5826   1085    849    288       C  
+ATOM   1372  O   GLY A 184     -18.252   8.003   0.296  1.00 51.02           O  
+ANISOU 1372  O   GLY A 184     8061   5611   5713   1128    961    318       O  
+ATOM   1373  N   ASP A 185     -18.324  10.137  -0.430  1.00 50.60           N  
+ANISOU 1373  N   ASP A 185     7704   5801   5721    873    782    235       N  
+ATOM   1374  CA  ASP A 185     -19.769  10.137  -0.635  1.00 48.23           C  
+ANISOU 1374  CA  ASP A 185     7512   5387   5425    686    821    204       C  
+ATOM   1375  C   ASP A 185     -20.206   9.108  -1.676  1.00 58.16           C  
+ANISOU 1375  C   ASP A 185     8912   6507   6678    620    967    153       C  
+ATOM   1376  O   ASP A 185     -21.234   8.452  -1.515  1.00 70.88           O  
+ANISOU 1376  O   ASP A 185    10679   7978   8272    536   1049    135       O  
+ATOM   1377  CB  ASP A 185     -20.247  11.530  -1.043  1.00 49.02           C  
+ANISOU 1377  CB  ASP A 185     7463   5593   5571    509    722    172       C  
+ATOM   1378  CG  ASP A 185     -20.402  12.461   0.143  1.00 56.53           C  
+ANISOU 1378  CG  ASP A 185     8338   6612   6530    514    610    190       C  
+ATOM   1379  OD1 ASP A 185     -20.229  11.995   1.290  1.00 56.69           O  
+ANISOU 1379  OD1 ASP A 185     8423   6619   6499    641    605    228       O  
+ATOM   1380  OD2 ASP A 185     -20.698  13.655  -0.070  1.00 51.81           O  
+ANISOU 1380  OD2 ASP A 185     7623   6077   5984    396    536    168       O  
+ATOM   1381  N   LEU A 186     -19.423   8.970  -2.742  1.00 49.72           N  
+ANISOU 1381  N   LEU A 186     7785   5487   5619    643   1006    114       N  
+ATOM   1382  CA  LEU A 186     -19.723   7.998  -3.787  1.00 51.35           C  
+ANISOU 1382  CA  LEU A 186     8120   5580   5811    578   1151     36       C  
+ATOM   1383  C   LEU A 186     -19.506   6.579  -3.283  1.00 53.37           C  
+ANISOU 1383  C   LEU A 186     8581   5635   6060    740   1292     54       C  
+ATOM   1384  O   LEU A 186     -20.068   5.626  -3.822  1.00 52.32           O  
+ANISOU 1384  O   LEU A 186     8616   5340   5923    661   1436    -21       O  
+ATOM   1385  CB  LEU A 186     -18.876   8.257  -5.034  1.00 52.16           C  
+ANISOU 1385  CB  LEU A 186     8100   5807   5913    570   1164    -13       C  
+ATOM   1386  CG  LEU A 186     -19.357   9.399  -5.929  1.00 49.58           C  
+ANISOU 1386  CG  LEU A 186     7633   5628   5576    368   1083    -35       C  
+ATOM   1387  CD1 LEU A 186     -18.297   9.772  -6.945  1.00 48.63           C  
+ANISOU 1387  CD1 LEU A 186     7376   5653   5449    388   1091    -50       C  
+ATOM   1388  CD2 LEU A 186     -20.644   8.996  -6.629  1.00 60.15           C  
+ANISOU 1388  CD2 LEU A 186     9077   6907   6870    176   1145   -113       C  
+ATOM   1389  N   VAL A 187     -18.683   6.440  -2.249  1.00 52.80           N  
+ANISOU 1389  N   VAL A 187     8498   5576   5986    968   1254    154       N  
+ATOM   1390  CA  VAL A 187     -18.552   5.154  -1.578  1.00 52.64           C  
+ANISOU 1390  CA  VAL A 187     8689   5353   5957   1151   1383    216       C  
+ATOM   1391  C   VAL A 187     -19.773   4.881  -0.694  1.00 58.40           C  
+ANISOU 1391  C   VAL A 187     9583   5942   6665   1050   1415    253       C  
+ATOM   1392  O   VAL A 187     -20.277   3.758  -0.648  1.00 53.59           O  
+ANISOU 1392  O   VAL A 187     9202   5096   6062   1041   1580    248       O  
+ATOM   1393  CB  VAL A 187     -17.267   5.082  -0.726  1.00 55.30           C  
+ANISOU 1393  CB  VAL A 187     8948   5789   6275   1454   1322    330       C  
+ATOM   1394  CG1 VAL A 187     -17.270   3.839   0.153  1.00 51.48           C  
+ANISOU 1394  CG1 VAL A 187     8699   5091   5769   1661   1444    440       C  
+ATOM   1395  CG2 VAL A 187     -16.037   5.106  -1.621  1.00 67.18           C  
+ANISOU 1395  CG2 VAL A 187    10306   7414   7805   1570   1332    286       C  
+ATOM   1396  N   SER A 188     -20.267   5.916  -0.017  1.00 73.81           N  
+ANISOU 1396  N   SER A 188    11418   8029   8596    959   1272    280       N  
+ATOM   1397  CA  SER A 188     -21.268   5.721   1.031  1.00 61.20           C  
+ANISOU 1397  CA  SER A 188     9949   6337   6965    904   1295    332       C  
+ATOM   1398  C   SER A 188     -22.716   6.011   0.622  1.00 57.66           C  
+ANISOU 1398  C   SER A 188     9518   5859   6532    617   1317    239       C  
+ATOM   1399  O   SER A 188     -23.639   5.371   1.126  1.00 65.61           O  
+ANISOU 1399  O   SER A 188    10687   6718   7521    536   1419    248       O  
+ATOM   1400  CB  SER A 188     -20.915   6.590   2.240  1.00 66.64           C  
+ANISOU 1400  CB  SER A 188    10511   7200   7607   1010   1138    415       C  
+ATOM   1401  OG  SER A 188     -19.662   6.221   2.788  1.00 78.06           O  
+ANISOU 1401  OG  SER A 188    11942   8702   9017   1286   1114    511       O  
+ATOM   1402  N   LYS A 189     -22.920   6.965  -0.281  1.00 51.08           N  
+ANISOU 1402  N   LYS A 189     8511   5172   5724    467   1225    158       N  
+ATOM   1403  CA  LYS A 189     -24.273   7.369  -0.672  1.00 49.84           C  
+ANISOU 1403  CA  LYS A 189     8327   5040   5571    221   1219     81       C  
+ATOM   1404  C   LYS A 189     -24.620   6.979  -2.105  1.00 53.06           C  
+ANISOU 1404  C   LYS A 189     8747   5432   5981     63   1297    -35       C  
+ATOM   1405  O   LYS A 189     -23.764   7.014  -2.987  1.00 62.64           O  
+ANISOU 1405  O   LYS A 189     9901   6700   7199    115   1293    -61       O  
+ATOM   1406  CB  LYS A 189     -24.448   8.879  -0.502  1.00 46.75           C  
+ANISOU 1406  CB  LYS A 189     7726   4838   5196    172   1049     94       C  
+ATOM   1407  CG  LYS A 189     -24.079   9.402   0.874  1.00 46.82           C  
+ANISOU 1407  CG  LYS A 189     7698   4899   5192    306    961    174       C  
+ATOM   1408  CD  LYS A 189     -24.256  10.909   0.948  1.00 50.17           C  
+ANISOU 1408  CD  LYS A 189     7930   5479   5653    241    816    160       C  
+ATOM   1409  CE  LYS A 189     -23.613  11.480   2.200  1.00 46.96           C  
+ANISOU 1409  CE  LYS A 189     7464   5151   5227    374    724    206       C  
+ATOM   1410  NZ  LYS A 189     -24.358  11.098   3.430  1.00 71.17           N  
+ANISOU 1410  NZ  LYS A 189    10645   8163   8234    388    762    236       N  
+ATOM   1411  N   THR A 190     -25.880   6.618  -2.338  1.00 50.25           N  
+ANISOU 1411  N   THR A 190     8456   5026   5610   -141   1368   -114       N  
+ATOM   1412  CA  THR A 190     -26.335   6.303  -3.688  1.00 48.74           C  
+ANISOU 1412  CA  THR A 190     8257   4867   5396   -321   1427   -246       C  
+ATOM   1413  C   THR A 190     -26.671   7.589  -4.440  1.00 49.99           C  
+ANISOU 1413  C   THR A 190     8192   5265   5537   -419   1275   -255       C  
+ATOM   1414  O   THR A 190     -27.570   8.335  -4.052  1.00 51.39           O  
+ANISOU 1414  O   THR A 190     8275   5534   5718   -500   1192   -234       O  
+ATOM   1415  CB  THR A 190     -27.566   5.375  -3.679  1.00 49.11           C  
+ANISOU 1415  CB  THR A 190     8444   4790   5425   -524   1568   -348       C  
+ATOM   1416  OG1 THR A 190     -27.205   4.103  -3.125  1.00 49.78           O  
+ANISOU 1416  OG1 THR A 190     8769   4611   5534   -435   1742   -332       O  
+ATOM   1417  CG2 THR A 190     -28.088   5.168  -5.093  1.00 55.91           C  
+ANISOU 1417  CG2 THR A 190     9260   5744   6239   -733   1605   -507       C  
+ATOM   1418  N   PHE A 191     -25.942   7.830  -5.525  1.00 57.61           N  
+ANISOU 1418  N   PHE A 191     9078   6329   6483   -400   1251   -280       N  
+ATOM   1419  CA  PHE A 191     -26.063   9.059  -6.304  1.00 52.02           C  
+ANISOU 1419  CA  PHE A 191     8173   5837   5755   -462   1118   -255       C  
+ATOM   1420  C   PHE A 191     -26.989   8.951  -7.509  1.00 47.48           C  
+ANISOU 1420  C   PHE A 191     7555   5388   5098   -665   1134   -359       C  
+ATOM   1421  O   PHE A 191     -27.092   7.899  -8.140  1.00 46.37           O  
+ANISOU 1421  O   PHE A 191     7523   5188   4907   -754   1258   -483       O  
+ATOM   1422  CB  PHE A 191     -24.684   9.510  -6.790  1.00 50.06           C  
+ANISOU 1422  CB  PHE A 191     7844   5656   5519   -330   1080   -203       C  
+ATOM   1423  CG  PHE A 191     -23.929  10.347  -5.801  1.00 47.03           C  
+ANISOU 1423  CG  PHE A 191     7382   5283   5205   -177    981    -91       C  
+ATOM   1424  CD1 PHE A 191     -23.396   9.785  -4.653  1.00 46.13           C  
+ANISOU 1424  CD1 PHE A 191     7361   5044   5121    -25   1014    -54       C  
+ATOM   1425  CD2 PHE A 191     -23.738  11.699  -6.031  1.00 45.73           C  
+ANISOU 1425  CD2 PHE A 191     7049   5257   5068   -188    861    -24       C  
+ATOM   1426  CE1 PHE A 191     -22.693  10.560  -3.750  1.00 46.36           C  
+ANISOU 1426  CE1 PHE A 191     7299   5122   5192    101    915     27       C  
+ATOM   1427  CE2 PHE A 191     -23.039  12.479  -5.133  1.00 46.57           C  
+ANISOU 1427  CE2 PHE A 191     7081   5376   5240    -77    779     48       C  
+ATOM   1428  CZ  PHE A 191     -22.515  11.909  -3.990  1.00 46.39           C  
+ANISOU 1428  CZ  PHE A 191     7132   5262   5231     62    800     62       C  
+ATOM   1429  N   LEU A 192     -27.672  10.050  -7.812  1.00 47.08           N  
+ANISOU 1429  N   LEU A 192     7343   5515   5029   -732   1010   -310       N  
+ATOM   1430  CA  LEU A 192     -28.323  10.209  -9.104  1.00 47.95           C  
+ANISOU 1430  CA  LEU A 192     7362   5820   5037   -884    986   -372       C  
+ATOM   1431  C   LEU A 192     -27.632  11.323  -9.883  1.00 50.02           C  
+ANISOU 1431  C   LEU A 192     7487   6237   5282   -817    887   -265       C  
+ATOM   1432  O   LEU A 192     -27.710  12.493  -9.509  1.00 46.96           O  
+ANISOU 1432  O   LEU A 192     6991   5899   4953   -753    778   -141       O  
+ATOM   1433  CB  LEU A 192     -29.813  10.520  -8.949  1.00 47.41           C  
+ANISOU 1433  CB  LEU A 192     7209   5862   4944  -1015    931   -394       C  
+ATOM   1434  CG  LEU A 192     -30.517  10.966 -10.235  1.00 47.11           C  
+ANISOU 1434  CG  LEU A 192     7024   6090   4784  -1138    860   -419       C  
+ATOM   1435  CD1 LEU A 192     -30.395   9.903 -11.320  1.00 47.33           C  
+ANISOU 1435  CD1 LEU A 192     7125   6165   4694  -1271    964   -582       C  
+ATOM   1436  CD2 LEU A 192     -31.975  11.304  -9.977  1.00 47.84           C  
+ANISOU 1436  CD2 LEU A 192     7004   6312   4859  -1237    799   -431       C  
+ATOM   1437  N   PHE A 193     -26.954  10.957 -10.966  1.00 64.58           N  
+ANISOU 1437  N   PHE A 193     9342   8148   7046   -836    941   -316       N  
+ATOM   1438  CA  PHE A 193     -26.350  11.950 -11.845  1.00 63.78           C  
+ANISOU 1438  CA  PHE A 193     9117   8210   6906   -801    870   -214       C  
+ATOM   1439  C   PHE A 193     -27.386  12.447 -12.845  1.00 48.69           C  
+ANISOU 1439  C   PHE A 193     7095   6536   4870   -928    797   -203       C  
+ATOM   1440  O   PHE A 193     -28.025  11.655 -13.534  1.00 51.06           O  
+ANISOU 1440  O   PHE A 193     7421   6930   5050  -1067    847   -342       O  
+ATOM   1441  CB  PHE A 193     -25.137  11.373 -12.582  1.00 51.03           C  
+ANISOU 1441  CB  PHE A 193     7551   6591   5247   -759    967   -270       C  
+ATOM   1442  CG  PHE A 193     -23.944  11.118 -11.700  1.00 51.19           C  
+ANISOU 1442  CG  PHE A 193     7630   6436   5383   -593   1013   -242       C  
+ATOM   1443  CD1 PHE A 193     -23.912  10.033 -10.838  1.00 52.24           C  
+ANISOU 1443  CD1 PHE A 193     7911   6367   5570   -538   1103   -318       C  
+ATOM   1444  CD2 PHE A 193     -22.846  11.963 -11.745  1.00 50.46           C  
+ANISOU 1444  CD2 PHE A 193     7440   6392   5340   -491    970   -134       C  
+ATOM   1445  CE1 PHE A 193     -22.809   9.801 -10.032  1.00 52.96           C  
+ANISOU 1445  CE1 PHE A 193     8041   6332   5748   -359   1133   -275       C  
+ATOM   1446  CE2 PHE A 193     -21.742  11.737 -10.943  1.00 47.60           C  
+ANISOU 1446  CE2 PHE A 193     7100   5917   5070   -337    999   -117       C  
+ATOM   1447  CZ  PHE A 193     -21.724  10.655 -10.086  1.00 47.19           C  
+ANISOU 1447  CZ  PHE A 193     7185   5688   5056   -258   1073   -182       C  
+ATOM   1448  N   VAL A 194     -27.558  13.761 -12.917  1.00 47.81           N  
+ANISOU 1448  N   VAL A 194     6858   6524   4784   -879    683    -40       N  
+ATOM   1449  CA  VAL A 194     -28.530  14.342 -13.833  1.00 48.99           C  
+ANISOU 1449  CA  VAL A 194     6887   6915   4811   -957    601     11       C  
+ATOM   1450  C   VAL A 194     -28.071  15.723 -14.298  1.00 49.34           C  
+ANISOU 1450  C   VAL A 194     6833   7042   4872   -869    523    217       C  
+ATOM   1451  O   VAL A 194     -27.481  16.487 -13.533  1.00 49.53           O  
+ANISOU 1451  O   VAL A 194     6854   6916   5047   -764    502    321       O  
+ATOM   1452  CB  VAL A 194     -29.935  14.428 -13.182  1.00 49.38           C  
+ANISOU 1452  CB  VAL A 194     6886   6990   4887  -1002    542     -9       C  
+ATOM   1453  CG1 VAL A 194     -29.915  15.332 -11.958  1.00 49.12           C  
+ANISOU 1453  CG1 VAL A 194     6834   6799   5031   -875    487    109       C  
+ATOM   1454  CG2 VAL A 194     -30.975  14.899 -14.191  1.00 55.97           C  
+ANISOU 1454  CG2 VAL A 194     7575   8118   5572  -1072    453     32       C  
+ATOM   1455  N   GLY A 195     -28.327  16.029 -15.566  1.00 49.85           N  
+ANISOU 1455  N   GLY A 195     6821   7346   4773   -921    490    272       N  
+ATOM   1456  CA  GLY A 195     -27.905  17.288 -16.147  1.00 52.75           C  
+ANISOU 1456  CA  GLY A 195     7113   7791   5137   -847    439    486       C  
+ATOM   1457  C   GLY A 195     -26.556  17.167 -16.827  1.00 51.87           C  
+ANISOU 1457  C   GLY A 195     7040   7686   4983   -846    523    494       C  
+ATOM   1458  O   GLY A 195     -25.931  18.169 -17.173  1.00 50.85           O  
+ANISOU 1458  O   GLY A 195     6871   7568   4883   -793    514    666       O  
+ATOM   1459  N   PHE A 196     -26.104  15.931 -17.014  1.00 50.58           N  
+ANISOU 1459  N   PHE A 196     6956   7506   4756   -905    620    303       N  
+ATOM   1460  CA  PHE A 196     -24.852  15.673 -17.712  1.00 57.44           C  
+ANISOU 1460  CA  PHE A 196     7851   8404   5569   -902    716    280       C  
+ATOM   1461  C   PHE A 196     -25.090  14.984 -19.051  1.00 56.99           C  
+ANISOU 1461  C   PHE A 196     7794   8591   5270  -1017    762    170       C  
+ATOM   1462  O   PHE A 196     -25.808  13.987 -19.129  1.00 54.52           O  
+ANISOU 1462  O   PHE A 196     7526   8313   4876  -1112    788    -16       O  
+ATOM   1463  CB  PHE A 196     -23.918  14.814 -16.855  1.00 66.05           C  
+ANISOU 1463  CB  PHE A 196     9034   9270   6790   -841    811    150       C  
+ATOM   1464  CG  PHE A 196     -23.436  15.494 -15.605  1.00 56.96           C  
+ANISOU 1464  CG  PHE A 196     7872   7921   5849   -730    770    246       C  
+ATOM   1465  CD1 PHE A 196     -22.413  16.427 -15.658  1.00 50.12           C  
+ANISOU 1465  CD1 PHE A 196     6941   7046   5056   -675    771    376       C  
+ATOM   1466  CD2 PHE A 196     -23.992  15.186 -14.375  1.00 57.25           C  
+ANISOU 1466  CD2 PHE A 196     7961   7792   6000   -696    741    194       C  
+ATOM   1467  CE1 PHE A 196     -21.963  17.049 -14.508  1.00 60.80           C  
+ANISOU 1467  CE1 PHE A 196     8274   8236   6592   -596    734    434       C  
+ATOM   1468  CE2 PHE A 196     -23.547  15.804 -13.222  1.00 50.67           C  
+ANISOU 1468  CE2 PHE A 196     7112   6804   5335   -601    701    265       C  
+ATOM   1469  CZ  PHE A 196     -22.530  16.736 -13.288  1.00 62.69           C  
+ANISOU 1469  CZ  PHE A 196     8564   8328   6929   -554    694    375       C  
+ATOM   1470  N   SER A 197     -24.479  15.522 -20.101  1.00 53.65           N  
+ANISOU 1470  N   SER A 197     7320   8339   4725  -1021    783    276       N  
+ATOM   1471  CA  SER A 197     -24.500  14.892 -21.414  1.00 50.50           C  
+ANISOU 1471  CA  SER A 197     6921   8192   4076  -1127    842    164       C  
+ATOM   1472  C   SER A 197     -23.076  14.484 -21.771  1.00 54.56           C  
+ANISOU 1472  C   SER A 197     7477   8663   4591  -1099    983     97       C  
+ATOM   1473  O   SER A 197     -22.145  14.766 -21.016  1.00 56.85           O  
+ANISOU 1473  O   SER A 197     7775   8756   5070   -999   1016    156       O  
+ATOM   1474  CB  SER A 197     -25.081  15.835 -22.469  1.00 51.04           C  
+ANISOU 1474  CB  SER A 197     6887   8557   3949  -1155    751    353       C  
+ATOM   1475  OG  SER A 197     -24.306  17.014 -22.582  1.00 65.40           O  
+ANISOU 1475  OG  SER A 197     8667  10344   5838  -1069    750    600       O  
+ATOM   1476  N   PHE A 198     -22.897  13.817 -22.907  1.00 53.02           N  
+ANISOU 1476  N   PHE A 198     7297   8669   4180  -1187   1068    -38       N  
+ATOM   1477  CA  PHE A 198     -21.574  13.314 -23.266  1.00 56.54           C  
+ANISOU 1477  CA  PHE A 198     7777   9083   4621  -1154   1220   -131       C  
+ATOM   1478  C   PHE A 198     -20.629  14.442 -23.680  1.00 64.91           C  
+ANISOU 1478  C   PHE A 198     8752  10226   5687  -1102   1231     96       C  
+ATOM   1479  O   PHE A 198     -19.425  14.231 -23.826  1.00 75.24           O  
+ANISOU 1479  O   PHE A 198    10056  11503   7029  -1057   1351     53       O  
+ATOM   1480  CB  PHE A 198     -21.674  12.252 -24.373  1.00 53.42           C  
+ANISOU 1480  CB  PHE A 198     7429   8879   3988  -1271   1326   -369       C  
+ATOM   1481  CG  PHE A 198     -22.249  12.754 -25.670  1.00 57.21           C  
+ANISOU 1481  CG  PHE A 198     7830   9728   4178  -1379   1269   -293       C  
+ATOM   1482  CD1 PHE A 198     -21.452  13.403 -26.600  1.00 56.56           C  
+ANISOU 1482  CD1 PHE A 198     7688   9840   3961  -1368   1317   -152       C  
+ATOM   1483  CD2 PHE A 198     -23.585  12.546 -25.973  1.00 56.13           C  
+ANISOU 1483  CD2 PHE A 198     7671   9766   3887  -1494   1171   -363       C  
+ATOM   1484  CE1 PHE A 198     -21.981  13.852 -27.797  1.00 64.93           C  
+ANISOU 1484  CE1 PHE A 198     8683  11258   4729  -1454   1265    -62       C  
+ATOM   1485  CE2 PHE A 198     -24.120  12.993 -27.168  1.00 58.16           C  
+ANISOU 1485  CE2 PHE A 198     7843  10404   3852  -1577   1105   -286       C  
+ATOM   1486  CZ  PHE A 198     -23.316  13.647 -28.081  1.00 59.39           C  
+ANISOU 1486  CZ  PHE A 198     7955  10746   3866  -1549   1151   -126       C  
+ATOM   1487  N   THR A 199     -21.180  15.638 -23.866  1.00 54.15           N  
+ANISOU 1487  N   THR A 199     7319   8963   4293  -1105   1116    337       N  
+ATOM   1488  CA  THR A 199     -20.381  16.804 -24.227  1.00 55.20           C  
+ANISOU 1488  CA  THR A 199     7387   9142   4446  -1074   1136    576       C  
+ATOM   1489  C   THR A 199     -19.948  17.616 -23.006  1.00 58.71           C  
+ANISOU 1489  C   THR A 199     7812   9314   5181   -984   1097    705       C  
+ATOM   1490  O   THR A 199     -19.333  18.674 -23.148  1.00 64.51           O  
+ANISOU 1490  O   THR A 199     8498  10041   5974   -974   1115    903       O  
+ATOM   1491  CB  THR A 199     -21.140  17.727 -25.198  1.00 54.05           C  
+ANISOU 1491  CB  THR A 199     7190   9249   4099  -1115   1055    798       C  
+ATOM   1492  OG1 THR A 199     -22.468  17.951 -24.710  1.00 62.88           O  
+ANISOU 1492  OG1 THR A 199     8298  10346   5247  -1097    908    844       O  
+ATOM   1493  CG2 THR A 199     -21.214  17.097 -26.581  1.00 62.99           C  
+ANISOU 1493  CG2 THR A 199     8319  10709   4906  -1212   1116    692       C  
+ATOM   1494  N   ASP A 200     -20.275  17.130 -21.811  1.00 52.87           N  
+ANISOU 1494  N   ASP A 200     7115   8356   4616   -933   1051    590       N  
+ATOM   1495  CA  ASP A 200     -19.911  17.829 -20.579  1.00 52.48           C  
+ANISOU 1495  CA  ASP A 200     7047   8068   4824   -854   1008    678       C  
+ATOM   1496  C   ASP A 200     -18.391  17.865 -20.449  1.00 61.90           C  
+ANISOU 1496  C   ASP A 200     8199   9208   6113   -821   1114    659       C  
+ATOM   1497  O   ASP A 200     -17.731  16.832 -20.569  1.00 70.03           O  
+ANISOU 1497  O   ASP A 200     9248  10252   7107   -798   1210    484       O  
+ATOM   1498  CB  ASP A 200     -20.545  17.157 -19.359  1.00 57.06           C  
+ANISOU 1498  CB  ASP A 200     7687   8456   5535   -807    950    544       C  
+ATOM   1499  CG  ASP A 200     -20.413  17.992 -18.096  1.00 57.39           C  
+ANISOU 1499  CG  ASP A 200     7707   8289   5811   -736    884    640       C  
+ATOM   1500  OD1 ASP A 200     -19.324  17.983 -17.483  1.00 56.16           O  
+ANISOU 1500  OD1 ASP A 200     7529   8026   5784   -684    931    607       O  
+ATOM   1501  OD2 ASP A 200     -21.399  18.659 -17.717  1.00 58.45           O  
+ANISOU 1501  OD2 ASP A 200     7835   8381   5992   -731    785    738       O  
+ATOM   1502  N   PRO A 201     -17.831  19.059 -20.200  1.00 67.17           N  
+ANISOU 1502  N   PRO A 201     8802   9813   6907   -819   1107    832       N  
+ATOM   1503  CA  PRO A 201     -16.379  19.272 -20.233  1.00 60.30           C  
+ANISOU 1503  CA  PRO A 201     7856   8947   6110   -819   1211    831       C  
+ATOM   1504  C   PRO A 201     -15.619  18.763 -19.009  1.00 60.33           C  
+ANISOU 1504  C   PRO A 201     7834   8794   6296   -730   1216    690       C  
+ATOM   1505  O   PRO A 201     -14.396  18.654 -19.089  1.00 67.94           O  
+ANISOU 1505  O   PRO A 201     8715   9806   7292   -716   1308    644       O  
+ATOM   1506  CB  PRO A 201     -16.259  20.796 -20.320  1.00 55.82           C  
+ANISOU 1506  CB  PRO A 201     7241   8342   5625   -874   1196   1066       C  
+ATOM   1507  CG  PRO A 201     -17.473  21.294 -19.626  1.00 56.32           C  
+ANISOU 1507  CG  PRO A 201     7357   8269   5775   -841   1065   1141       C  
+ATOM   1508  CD  PRO A 201     -18.566  20.308 -19.935  1.00 60.32           C  
+ANISOU 1508  CD  PRO A 201     7927   8872   6121   -825   1011   1035       C  
+ATOM   1509  N   ASN A 202     -16.305  18.456 -17.910  1.00 57.88           N  
+ANISOU 1509  N   ASN A 202     7580   8321   6090   -667   1123    627       N  
+ATOM   1510  CA  ASN A 202     -15.596  18.113 -16.674  1.00 55.02           C  
+ANISOU 1510  CA  ASN A 202     7189   7826   5889   -571   1113    529       C  
+ATOM   1511  C   ASN A 202     -15.947  16.782 -16.008  1.00 54.24           C  
+ANISOU 1511  C   ASN A 202     7186   7634   5789   -472   1108    366       C  
+ATOM   1512  O   ASN A 202     -15.168  16.286 -15.196  1.00 57.06           O  
+ANISOU 1512  O   ASN A 202     7518   7927   6237   -366   1126    285       O  
+ATOM   1513  CB  ASN A 202     -15.780  19.227 -15.641  1.00 55.43           C  
+ANISOU 1513  CB  ASN A 202     7207   7737   6115   -579   1018    625       C  
+ATOM   1514  CG  ASN A 202     -15.316  20.570 -16.152  1.00 56.56           C  
+ANISOU 1514  CG  ASN A 202     7271   7917   6301   -678   1047    784       C  
+ATOM   1515  OD1 ASN A 202     -16.104  21.504 -16.295  1.00 72.65           O  
+ANISOU 1515  OD1 ASN A 202     9341   9902   8360   -728    997    926       O  
+ATOM   1516  ND2 ASN A 202     -14.029  20.665 -16.457  1.00 57.92           N  
+ANISOU 1516  ND2 ASN A 202     7339   8179   6487   -705   1140    765       N  
+ATOM   1517  N   LEU A 203     -17.097  16.201 -16.338  1.00 53.01           N  
+ANISOU 1517  N   LEU A 203     7134   7478   5529   -507   1088    320       N  
+ATOM   1518  CA  LEU A 203     -17.570  15.010 -15.627  1.00 52.03           C  
+ANISOU 1518  CA  LEU A 203     7121   7226   5421   -439   1092    178       C  
+ATOM   1519  C   LEU A 203     -16.621  13.810 -15.692  1.00 59.22           C  
+ANISOU 1519  C   LEU A 203     8065   8119   6318   -338   1215     34       C  
+ATOM   1520  O   LEU A 203     -16.371  13.163 -14.676  1.00 70.98           O  
+ANISOU 1520  O   LEU A 203     9602   9466   7901   -217   1219    -25       O  
+ATOM   1521  CB  LEU A 203     -18.941  14.584 -16.151  1.00 50.94           C  
+ANISOU 1521  CB  LEU A 203     7072   7124   5159   -533   1070    134       C  
+ATOM   1522  CG  LEU A 203     -19.510  13.357 -15.433  1.00 50.24           C  
+ANISOU 1522  CG  LEU A 203     7113   6883   5093   -496   1096    -13       C  
+ATOM   1523  CD1 LEU A 203     -19.715  13.663 -13.954  1.00 51.37           C  
+ANISOU 1523  CD1 LEU A 203     7266   6856   5395   -417   1013     38       C  
+ATOM   1524  CD2 LEU A 203     -20.808  12.893 -16.076  1.00 50.02           C  
+ANISOU 1524  CD2 LEU A 203     7150   6926   4929   -625   1090    -89       C  
+ATOM   1525  N   ASP A 204     -16.100  13.507 -16.877  1.00 58.03           N  
+ANISOU 1525  N   ASP A 204     7891   8114   6043   -374   1320    -17       N  
+ATOM   1526  CA  ASP A 204     -15.233  12.342 -17.030  1.00 53.33           C  
+ANISOU 1526  CA  ASP A 204     7331   7500   5434   -265   1455   -165       C  
+ATOM   1527  C   ASP A 204     -13.936  12.516 -16.244  1.00 58.11           C  
+ANISOU 1527  C   ASP A 204     7823   8081   6175   -117   1463   -135       C  
+ATOM   1528  O   ASP A 204     -13.421  11.554 -15.674  1.00 57.73           O  
+ANISOU 1528  O   ASP A 204     7819   7934   6183     42   1523   -226       O  
+ATOM   1529  CB  ASP A 204     -14.931  12.069 -18.508  1.00 53.67           C  
+ANISOU 1529  CB  ASP A 204     7360   7729   5303   -342   1575   -235       C  
+ATOM   1530  CG  ASP A 204     -14.285  13.248 -19.205  1.00 56.38           C  
+ANISOU 1530  CG  ASP A 204     7552   8262   5607   -415   1572    -94       C  
+ATOM   1531  OD1 ASP A 204     -14.397  14.383 -18.693  1.00 71.14           O  
+ANISOU 1531  OD1 ASP A 204     9350  10109   7570   -449   1465     64       O  
+ATOM   1532  OD2 ASP A 204     -13.664  13.038 -20.267  1.00 60.39           O  
+ANISOU 1532  OD2 ASP A 204     8021   8935   5992   -443   1690   -146       O  
+ATOM   1533  N   TYR A 205     -13.414  13.739 -16.213  1.00 56.06           N  
+ANISOU 1533  N   TYR A 205     7415   7917   5968   -168   1407     -9       N  
+ATOM   1534  CA  TYR A 205     -12.224  14.030 -15.421  1.00 56.90           C  
+ANISOU 1534  CA  TYR A 205     7382   8037   6200    -59   1397      9       C  
+ATOM   1535  C   TYR A 205     -12.480  13.807 -13.935  1.00 56.63           C  
+ANISOU 1535  C   TYR A 205     7394   7840   6284     56   1298      6       C  
+ATOM   1536  O   TYR A 205     -11.735  13.088 -13.266  1.00 56.43           O  
+ANISOU 1536  O   TYR A 205     7346   7787   6309    229   1325    -53       O  
+ATOM   1537  CB  TYR A 205     -11.745  15.467 -15.641  1.00 57.40           C  
+ANISOU 1537  CB  TYR A 205     7291   8212   6307   -182   1361    136       C  
+ATOM   1538  CG  TYR A 205     -10.656  15.862 -14.669  1.00 58.93           C  
+ANISOU 1538  CG  TYR A 205     7327   8427   6636   -105   1327    136       C  
+ATOM   1539  CD1 TYR A 205      -9.367  15.367 -14.810  1.00 62.12           C  
+ANISOU 1539  CD1 TYR A 205     7600   8961   7043      2   1419     60       C  
+ATOM   1540  CD2 TYR A 205     -10.922  16.702 -13.595  1.00 58.76           C  
+ANISOU 1540  CD2 TYR A 205     7277   8316   6734   -136   1203    196       C  
+ATOM   1541  CE1 TYR A 205      -8.369  15.709 -13.921  1.00 60.44           C  
+ANISOU 1541  CE1 TYR A 205     7213   8812   6938     71   1376     49       C  
+ATOM   1542  CE2 TYR A 205      -9.929  17.049 -12.698  1.00 59.86           C  
+ANISOU 1542  CE2 TYR A 205     7259   8507   6977    -81   1164    171       C  
+ATOM   1543  CZ  TYR A 205      -8.653  16.550 -12.867  1.00 60.91           C  
+ANISOU 1543  CZ  TYR A 205     7246   8794   7102     20   1245    100       C  
+ATOM   1544  OH  TYR A 205      -7.655  16.887 -11.982  1.00 62.48           O  
+ANISOU 1544  OH  TYR A 205     7259   9090   7389     72   1196     67       O  
+ATOM   1545  N   ILE A 206     -13.536  14.439 -13.429  1.00 54.98           N  
+ANISOU 1545  N   ILE A 206     7243   7537   6108    -30   1187     77       N  
+ATOM   1546  CA  ILE A 206     -13.915  14.328 -12.024  1.00 54.54           C  
+ANISOU 1546  CA  ILE A 206     7237   7340   6145     55   1093     80       C  
+ATOM   1547  C   ILE A 206     -14.116  12.873 -11.617  1.00 53.74           C  
+ANISOU 1547  C   ILE A 206     7283   7117   6020    196   1152    -14       C  
+ATOM   1548  O   ILE A 206     -13.587  12.429 -10.599  1.00 53.80           O  
+ANISOU 1548  O   ILE A 206     7284   7071   6087    357   1135    -26       O  
+ATOM   1549  CB  ILE A 206     -15.203  15.121 -11.726  1.00 56.04           C  
+ANISOU 1549  CB  ILE A 206     7485   7452   6357    -65    989    155       C  
+ATOM   1550  CG1 ILE A 206     -14.976  16.615 -11.966  1.00 54.62           C  
+ANISOU 1550  CG1 ILE A 206     7180   7343   6232   -182    941    263       C  
+ATOM   1551  CG2 ILE A 206     -15.661  14.883 -10.298  1.00 53.06           C  
+ANISOU 1551  CG2 ILE A 206     7172   6936   6051     21    911    142       C  
+ATOM   1552  CD1 ILE A 206     -16.231  17.450 -11.848  1.00 54.06           C  
+ANISOU 1552  CD1 ILE A 206     7160   7197   6181   -280    856    348       C  
+ATOM   1553  N   LEU A 207     -14.869  12.136 -12.427  1.00 52.74           N  
+ANISOU 1553  N   LEU A 207     7289   6950   5799    133   1228    -80       N  
+ATOM   1554  CA  LEU A 207     -15.117  10.721 -12.175  1.00 62.28           C  
+ANISOU 1554  CA  LEU A 207     8664   8007   6991    237   1318   -182       C  
+ATOM   1555  C   LEU A 207     -13.814   9.934 -12.191  1.00 59.00           C  
+ANISOU 1555  C   LEU A 207     8214   7607   6596    432   1425   -238       C  
+ATOM   1556  O   LEU A 207     -13.624   9.009 -11.401  1.00 53.27           O  
+ANISOU 1556  O   LEU A 207     7585   6740   5915    605   1466   -262       O  
+ATOM   1557  CB  LEU A 207     -16.095  10.157 -13.202  1.00 54.08           C  
+ANISOU 1557  CB  LEU A 207     7752   6955   5840     92   1392   -273       C  
+ATOM   1558  CG  LEU A 207     -17.540  10.615 -13.016  1.00 51.00           C  
+ANISOU 1558  CG  LEU A 207     7415   6532   5430    -63   1294   -235       C  
+ATOM   1559  CD1 LEU A 207     -18.419  10.000 -14.076  1.00 54.24           C  
+ANISOU 1559  CD1 LEU A 207     7920   6978   5710   -211   1366   -348       C  
+ATOM   1560  CD2 LEU A 207     -18.041  10.253 -11.627  1.00 49.69           C  
+ANISOU 1560  CD2 LEU A 207     7345   6181   5353     14   1250   -218       C  
+ATOM   1561  N   SER A 208     -12.919  10.308 -13.099  1.00 54.28           N  
+ANISOU 1561  N   SER A 208     7476   7187   5961    412   1478   -248       N  
+ATOM   1562  CA  SER A 208     -11.605   9.685 -13.182  1.00 55.28           C  
+ANISOU 1562  CA  SER A 208     7524   7371   6108    604   1580   -301       C  
+ATOM   1563  C   SER A 208     -10.792  10.007 -11.933  1.00 55.98           C  
+ANISOU 1563  C   SER A 208     7481   7489   6298    767   1486   -227       C  
+ATOM   1564  O   SER A 208      -9.834   9.308 -11.606  1.00 56.77           O  
+ANISOU 1564  O   SER A 208     7535   7607   6429    988   1546   -256       O  
+ATOM   1565  CB  SER A 208     -10.856  10.146 -14.434  1.00 56.31           C  
+ANISOU 1565  CB  SER A 208     7510   7716   6169    519   1658   -325       C  
+ATOM   1566  OG  SER A 208     -10.417  11.488 -14.301  1.00 57.18           O  
+ANISOU 1566  OG  SER A 208     7429   7976   6321    425   1560   -217       O  
+ATOM   1567  N   ARG A 209     -11.178  11.074 -11.239  1.00 56.78           N  
+ANISOU 1567  N   ARG A 209     7518   7610   6447    664   1338   -138       N  
+ATOM   1568  CA  ARG A 209     -10.481  11.484 -10.027  1.00 56.88           C  
+ANISOU 1568  CA  ARG A 209     7396   7679   6537    783   1234    -87       C  
+ATOM   1569  C   ARG A 209     -11.109  10.879  -8.772  1.00 58.44           C  
+ANISOU 1569  C   ARG A 209     7743   7704   6757    906   1175    -61       C  
+ATOM   1570  O   ARG A 209     -10.467  10.816  -7.724  1.00 68.94           O  
+ANISOU 1570  O   ARG A 209     8992   9082   8121   1070   1109    -30       O  
+ATOM   1571  CB  ARG A 209     -10.490  13.012  -9.905  1.00 56.96           C  
+ANISOU 1571  CB  ARG A 209     7256   7794   6591    597   1122    -23       C  
+ATOM   1572  CG  ARG A 209      -9.465  13.739 -10.758  1.00 58.21           C  
+ANISOU 1572  CG  ARG A 209     7210   8155   6752    510   1171    -25       C  
+ATOM   1573  CD  ARG A 209      -8.041  13.444 -10.326  1.00 65.46           C  
+ANISOU 1573  CD  ARG A 209     7937   9235   7702    689   1188    -65       C  
+ATOM   1574  NE  ARG A 209      -7.787  13.785  -8.929  1.00 68.67           N  
+ANISOU 1574  NE  ARG A 209     8255   9667   8168    767   1054    -46       N  
+ATOM   1575  CZ  ARG A 209      -7.503  15.009  -8.495  1.00 65.18           C  
+ANISOU 1575  CZ  ARG A 209     7656   9322   7786    622    963    -31       C  
+ATOM   1576  NH1 ARG A 209      -7.457  16.025  -9.347  1.00 73.07           N  
+ANISOU 1576  NH1 ARG A 209     8584  10373   8808    398    999     -8       N  
+ATOM   1577  NH2 ARG A 209      -7.277  15.221  -7.205  1.00 60.66           N  
+ANISOU 1577  NH2 ARG A 209     7009   8793   7247    697    843    -39       N  
+ATOM   1578  N   VAL A 210     -12.359  10.434  -8.873  1.00 54.34           N  
+ANISOU 1578  N   VAL A 210     7432   7006   6210    821   1199    -73       N  
+ATOM   1579  CA  VAL A 210     -13.067   9.935  -7.696  1.00 57.22           C  
+ANISOU 1579  CA  VAL A 210     7946   7204   6591    902   1155    -39       C  
+ATOM   1580  C   VAL A 210     -13.537   8.486  -7.796  1.00 71.82           C  
+ANISOU 1580  C   VAL A 210    10029   8845   8414    994   1292    -89       C  
+ATOM   1581  O   VAL A 210     -14.098   7.955  -6.837  1.00 69.65           O  
+ANISOU 1581  O   VAL A 210     9898   8416   8150   1065   1283    -52       O  
+ATOM   1582  CB  VAL A 210     -14.305  10.797  -7.378  1.00 58.31           C  
+ANISOU 1582  CB  VAL A 210     8124   7293   6737    705   1051     -2       C  
+ATOM   1583  CG1 VAL A 210     -13.890  12.216  -7.018  1.00 53.51           C  
+ANISOU 1583  CG1 VAL A 210     7319   6834   6178    628    924     48       C  
+ATOM   1584  CG2 VAL A 210     -15.270  10.794  -8.549  1.00 55.40           C  
+ANISOU 1584  CG2 VAL A 210     7841   6892   6316    511   1107    -46       C  
+ATOM   1585  N   ARG A 211     -13.324   7.839  -8.938  1.00 76.57           N  
+ANISOU 1585  N   ARG A 211    10679   9434   8981    983   1431   -179       N  
+ATOM   1586  CA  ARG A 211     -13.788   6.464  -9.073  1.00 67.46           C  
+ANISOU 1586  CA  ARG A 211     9763   8054   7814   1046   1583   -252       C  
+ATOM   1587  C   ARG A 211     -12.730   5.557  -9.702  1.00 74.43           C  
+ANISOU 1587  C   ARG A 211    10649   8931   8698   1232   1741   -327       C  
+ATOM   1588  O   ARG A 211     -11.909   6.003 -10.504  1.00 81.12           O  
+ANISOU 1588  O   ARG A 211    11325   9973   9524   1223   1756   -359       O  
+ATOM   1589  CB  ARG A 211     -15.071   6.423  -9.907  1.00 53.69           C  
+ANISOU 1589  CB  ARG A 211     8139   6248   6012    783   1622   -338       C  
+ATOM   1590  CG  ARG A 211     -16.292   6.976  -9.177  1.00 64.90           C  
+ANISOU 1590  CG  ARG A 211     9603   7616   7439    637   1503   -278       C  
+ATOM   1591  CD  ARG A 211     -16.686   6.179  -7.945  1.00 69.99           C  
+ANISOU 1591  CD  ARG A 211    10420   8046   8126    756   1530   -234       C  
+ATOM   1592  NE  ARG A 211     -17.745   5.209  -8.197  1.00 71.44           N  
+ANISOU 1592  NE  ARG A 211    10825   8031   8289    636   1656   -329       N  
+ATOM   1593  CZ  ARG A 211     -18.291   4.453  -7.251  1.00 75.27           C  
+ANISOU 1593  CZ  ARG A 211    11492   8302   8804    688   1711   -297       C  
+ATOM   1594  NH1 ARG A 211     -17.883   4.569  -5.994  1.00 60.42           N  
+ANISOU 1594  NH1 ARG A 211     9599   6401   6958    874   1640   -163       N  
+ATOM   1595  NH2 ARG A 211     -19.253   3.593  -7.556  1.00 78.38           N  
+ANISOU 1595  NH2 ARG A 211    12079   8518   9185    541   1842   -402       N  
+ATOM   1596  N   SER A 212     -12.759   4.281  -9.330  1.00 68.52           N  
+ANISOU 1596  N   SER A 212    10105   7950   7980   1404   1874   -350       N  
+ATOM   1597  CA  SER A 212     -11.848   3.290  -9.891  1.00 77.03           C  
+ANISOU 1597  CA  SER A 212    11223   8972   9073   1607   2051   -429       C  
+ATOM   1598  C   SER A 212     -12.556   2.494 -10.983  1.00 78.87           C  
+ANISOU 1598  C   SER A 212    11654   9048   9266   1444   2228   -603       C  
+ATOM   1599  O   SER A 212     -13.741   2.184 -10.864  1.00 88.08           O  
+ANISOU 1599  O   SER A 212    13004  10042  10422   1271   2249   -642       O  
+ATOM   1600  CB  SER A 212     -11.324   2.353  -8.800  1.00 87.88           C  
+ANISOU 1600  CB  SER A 212    12705  10174  10511   1938   2105   -335       C  
+ATOM   1601  OG  SER A 212     -10.444   3.030  -7.920  1.00 98.31           O  
+ANISOU 1601  OG  SER A 212    13803  11706  11845   2113   1949   -202       O  
+ATOM   1602  N   ALA A 213     -11.829   2.166 -12.046  1.00 77.08           N  
+ANISOU 1602  N   ALA A 213    11377   8898   9011   1487   2360   -724       N  
+ATOM   1603  CA  ALA A 213     -12.413   1.454 -13.179  1.00 79.16           C  
+ANISOU 1603  CA  ALA A 213    11806   9055   9215   1317   2532   -922       C  
+ATOM   1604  C   ALA A 213     -12.335  -0.059 -13.002  1.00 78.04           C  
+ANISOU 1604  C   ALA A 213    11927   8579   9146   1502   2754  -1010       C  
+ATOM   1605  O   ALA A 213     -11.314  -0.590 -12.565  1.00 90.64           O  
+ANISOU 1605  O   ALA A 213    13511  10112  10817   1824   2827   -952       O  
+ATOM   1606  CB  ALA A 213     -11.724   1.867 -14.470  1.00 81.02           C  
+ANISOU 1606  CB  ALA A 213    11869   9548   9365   1250   2579  -1023       C  
+ATOM   1607  N   TYR A 214     -13.438  -0.734 -13.328  1.00 75.72           N  
+ANISOU 1607  N   TYR A 214    11867   8073   8831   1296   2864  -1148       N  
+ATOM   1608  CA  TYR A 214     -13.576  -2.190 -13.209  1.00 80.95           C  
+ANISOU 1608  CA  TYR A 214    12826   8361   9570   1406   3104  -1253       C  
+ATOM   1609  C   TYR A 214     -13.479  -2.693 -11.763  1.00 88.91           C  
+ANISOU 1609  C   TYR A 214    13968   9120  10694   1664   3102  -1061       C  
+ATOM   1610  O   TYR A 214     -13.623  -3.890 -11.508  1.00101.69           O  
+ANISOU 1610  O   TYR A 214    15858  10387  12392   1774   3305  -1106       O  
+ATOM   1611  CB  TYR A 214     -12.536  -2.902 -14.080  1.00 78.95           C  
+ANISOU 1611  CB  TYR A 214    12581   8087   9328   1590   3309  -1401       C  
+ATOM   1612  N   GLU A 215     -13.236  -1.773 -10.832  1.00 79.07           N  
+ANISOU 1612  N   GLU A 215    12538   8057   9449   1755   2881   -850       N  
+ATOM   1613  CA  GLU A 215     -13.231  -2.058  -9.398  1.00 81.28           C  
+ANISOU 1613  CA  GLU A 215    12914   8172   9796   1971   2837   -649       C  
+ATOM   1614  C   GLU A 215     -14.520  -2.756  -8.985  1.00 90.93           C  
+ANISOU 1614  C   GLU A 215    14430   9076  11043   1794   2936   -678       C  
+ATOM   1615  O   GLU A 215     -15.611  -2.240  -9.219  1.00109.50           O  
+ANISOU 1615  O   GLU A 215    16772  11494  13339   1466   2856   -745       O  
+ATOM   1616  CB  GLU A 215     -13.049  -0.770  -8.594  1.00 84.06           C  
+ANISOU 1616  CB  GLU A 215    13012   8815  10114   1979   2565   -472       C  
+ATOM   1617  N   ARG A 216     -14.403  -3.927  -8.370  1.00 88.50           N  
+ANISOU 1617  N   ARG A 216    14379   8426  10819   2014   3116   -621       N  
+ATOM   1618  CA  ARG A 216     -15.584  -4.736  -8.106  1.00 92.66           C  
+ANISOU 1618  CA  ARG A 216    15211   8613  11382   1825   3265   -676       C  
+ATOM   1619  C   ARG A 216     -16.257  -4.382  -6.783  1.00102.00           C  
+ANISOU 1619  C   ARG A 216    16428   9774  12556   1803   3130   -474       C  
+ATOM   1620  O   ARG A 216     -15.652  -3.765  -5.903  1.00102.99           O  
+ANISOU 1620  O   ARG A 216    16391  10079  12660   2020   2955   -272       O  
+ATOM   1621  CB  ARG A 216     -15.219  -6.221  -8.115  1.00 90.14           C  
+ANISOU 1621  CB  ARG A 216    15198   7882  11169   2048   3563   -716       C  
+ATOM   1622  N   ASP A 217     -17.530  -4.761  -6.684  1.00 96.27           N  
+ANISOU 1622  N   ASP A 217    15898   8846  11834   1520   3217   -550       N  
+ATOM   1623  CA  ASP A 217     -18.371  -4.513  -5.513  1.00 81.82           C  
+ANISOU 1623  CA  ASP A 217    14125   6973   9989   1442   3128   -394       C  
+ATOM   1624  C   ASP A 217     -18.569  -3.035  -5.173  1.00 80.16           C  
+ANISOU 1624  C   ASP A 217    13616   7145   9696   1339   2831   -309       C  
+ATOM   1625  O   ASP A 217     -18.887  -2.702  -4.031  1.00 94.33           O  
+ANISOU 1625  O   ASP A 217    15408   8961  11471   1384   2727   -141       O  
+ATOM   1626  CB  ASP A 217     -17.820  -5.257  -4.292  1.00 81.40           C  
+ANISOU 1626  CB  ASP A 217    14255   6685   9989   1803   3212   -157       C  
+ATOM   1627  CG  ASP A 217     -17.702  -6.752  -4.526  1.00 91.18           C  
+ANISOU 1627  CG  ASP A 217    15831   7483  11330   1917   3532   -217       C  
+ATOM   1628  OD1 ASP A 217     -18.752  -7.423  -4.619  1.00101.91           O  
+ANISOU 1628  OD1 ASP A 217    17403   8598  12720   1639   3688   -319       O  
+ATOM   1629  OD2 ASP A 217     -16.564  -7.259  -4.609  1.00 93.88           O  
+ANISOU 1629  OD2 ASP A 217    16183   7768  11720   2260   3607   -155       O  
+ATOM   1630  N   GLN A 218     -18.388  -2.149  -6.149  1.00 86.73           N  
+ANISOU 1630  N   GLN A 218    14206   8269  10477   1203   2706   -424       N  
+ATOM   1631  CA  GLN A 218     -18.613  -0.728  -5.899  1.00 64.09           C  
+ANISOU 1631  CA  GLN A 218    11074   5728   7548   1093   2447   -353       C  
+ATOM   1632  C   GLN A 218     -20.101  -0.455  -5.712  1.00 57.83           C  
+ANISOU 1632  C   GLN A 218    10328   4918   6725    775   2411   -399       C  
+ATOM   1633  O   GLN A 218     -20.944  -1.216  -6.187  1.00 69.12           O  
+ANISOU 1633  O   GLN A 218    11934   6165   8164    567   2570   -546       O  
+ATOM   1634  CB  GLN A 218     -18.086   0.131  -7.052  1.00 60.58           C  
+ANISOU 1634  CB  GLN A 218    10382   5577   7058   1016   2347   -450       C  
+ATOM   1635  CG  GLN A 218     -16.577   0.206  -7.187  1.00 79.11           C  
+ANISOU 1635  CG  GLN A 218    12591   8043   9423   1310   2333   -394       C  
+ATOM   1636  CD  GLN A 218     -16.155   1.073  -8.361  1.00 99.15           C  
+ANISOU 1636  CD  GLN A 218    14896  10868  11908   1192   2255   -489       C  
+ATOM   1637  OE1 GLN A 218     -16.548   0.827  -9.502  1.00 99.73           O  
+ANISOU 1637  OE1 GLN A 218    15013  10940  11941   1000   2351   -660       O  
+ATOM   1638  NE2 GLN A 218     -15.360   2.102  -8.085  1.00 94.81           N  
+ANISOU 1638  NE2 GLN A 218    14098  10576  11351   1292   2085   -382       N  
+ATOM   1639  N   ARG A 219     -20.418   0.633  -5.018  1.00 73.47           N  
+ANISOU 1639  N   ARG A 219    12143   7098   8674    734   2208   -288       N  
+ATOM   1640  CA  ARG A 219     -21.801   1.074  -4.887  1.00 64.97           C  
+ANISOU 1640  CA  ARG A 219    11055   6064   7567    447   2152   -332       C  
+ATOM   1641  C   ARG A 219     -22.362   1.454  -6.250  1.00 60.93           C  
+ANISOU 1641  C   ARG A 219    10436   5709   7008    178   2133   -512       C  
+ATOM   1642  O   ARG A 219     -21.694   2.128  -7.034  1.00 73.00           O  
+ANISOU 1642  O   ARG A 219    11786   7444   8506    208   2045   -532       O  
+ATOM   1643  CB  ARG A 219     -21.902   2.251  -3.919  1.00 53.47           C  
+ANISOU 1643  CB  ARG A 219     9425   4801   6090    486   1940   -187       C  
+ATOM   1644  CG  ARG A 219     -23.280   2.882  -3.848  1.00 57.25           C  
+ANISOU 1644  CG  ARG A 219     9844   5368   6540    213   1865   -232       C  
+ATOM   1645  CD  ARG A 219     -23.367   3.855  -2.691  1.00 60.26           C  
+ANISOU 1645  CD  ARG A 219    10107   5877   6913    284   1699    -93       C  
+ATOM   1646  NE  ARG A 219     -23.167   3.182  -1.412  1.00 61.43           N  
+ANISOU 1646  NE  ARG A 219    10419   5858   7064    464   1765     36       N  
+ATOM   1647  CZ  ARG A 219     -24.154   2.776  -0.622  1.00 52.95           C  
+ANISOU 1647  CZ  ARG A 219     9486   4654   5979    367   1839     63       C  
+ATOM   1648  NH1 ARG A 219     -25.415   2.975  -0.980  1.00 52.23           N  
+ANISOU 1648  NH1 ARG A 219     9371   4592   5881     89   1851    -44       N  
+ATOM   1649  NH2 ARG A 219     -23.881   2.168   0.524  1.00 53.28           N  
+ANISOU 1649  NH2 ARG A 219     9682   4554   6006    552   1903    205       N  
+ATOM   1650  N   ARG A 220     -23.589   1.033  -6.536  1.00 58.95           N  
+ANISOU 1650  N   ARG A 220    10282   5379   6736    -89   2218   -639       N  
+ATOM   1651  CA  ARG A 220     -24.197   1.376  -7.812  1.00 63.40           C  
+ANISOU 1651  CA  ARG A 220    10732   6130   7226   -345   2188   -808       C  
+ATOM   1652  C   ARG A 220     -24.898   2.732  -7.734  1.00 61.54           C  
+ANISOU 1652  C   ARG A 220    10267   6172   6944   -466   1971   -743       C  
+ATOM   1653  O   ARG A 220     -25.674   3.001  -6.816  1.00 64.05           O  
+ANISOU 1653  O   ARG A 220    10586   6471   7281   -516   1919   -671       O  
+ATOM   1654  CB  ARG A 220     -25.147   0.260  -8.253  1.00 63.96           C  
+ANISOU 1654  CB  ARG A 220    10994   6019   7288   -589   2383  -1005       C  
+ATOM   1655  CG  ARG A 220     -25.853   0.488  -9.578  1.00 75.74           C  
+ANISOU 1655  CG  ARG A 220    12371   7731   8676   -870   2358  -1203       C  
+ATOM   1656  CD  ARG A 220     -26.396  -0.839 -10.093  1.00 94.22           C  
+ANISOU 1656  CD  ARG A 220    14927   9855  11017  -1073   2596  -1437       C  
+ATOM   1657  NE  ARG A 220     -27.786  -0.802 -10.532  1.00101.88           N  
+ANISOU 1657  NE  ARG A 220    15835  10967  11909  -1418   2582  -1598       N  
+ATOM   1658  CZ  ARG A 220     -28.323  -1.714 -11.336  1.00103.46           C  
+ANISOU 1658  CZ  ARG A 220    16145  11097  12066  -1668   2749  -1858       C  
+ATOM   1659  NH1 ARG A 220     -27.578  -2.712 -11.796  1.00 95.28           N  
+ANISOU 1659  NH1 ARG A 220    15305   9828  11069  -1601   2952  -1984       N  
+ATOM   1660  NH2 ARG A 220     -29.597  -1.626 -11.691  1.00105.04           N  
+ANISOU 1660  NH2 ARG A 220    16252  11474  12185  -1983   2717  -2004       N  
+ATOM   1661  N   HIS A 221     -24.613   3.576  -8.721  1.00 61.33           N  
+ANISOU 1661  N   HIS A 221    10050   6396   6855   -505   1859   -766       N  
+ATOM   1662  CA  HIS A 221     -25.226   4.893  -8.847  1.00 47.96           C  
+ANISOU 1662  CA  HIS A 221     8144   4960   5121   -606   1668   -701       C  
+ATOM   1663  C   HIS A 221     -26.012   4.964 -10.148  1.00 59.16           C  
+ANISOU 1663  C   HIS A 221     9486   6564   6428   -846   1664   -848       C  
+ATOM   1664  O   HIS A 221     -25.963   4.039 -10.955  1.00 65.56           O  
+ANISOU 1664  O   HIS A 221    10402   7318   7191   -936   1805  -1013       O  
+ATOM   1665  CB  HIS A 221     -24.162   5.991  -8.799  1.00 47.65           C  
+ANISOU 1665  CB  HIS A 221     7936   5067   5103   -428   1528   -559       C  
+ATOM   1666  CG  HIS A 221     -23.234   5.882  -7.627  1.00 66.17           C  
+ANISOU 1666  CG  HIS A 221    10329   7281   7531   -185   1526   -436       C  
+ATOM   1667  ND1 HIS A 221     -23.569   6.327  -6.368  1.00 52.86           N  
+ANISOU 1667  ND1 HIS A 221     8632   5562   5889   -130   1442   -325       N  
+ATOM   1668  CD2 HIS A 221     -21.985   5.367  -7.525  1.00 69.76           C  
+ANISOU 1668  CD2 HIS A 221    10831   7654   8019     26   1594   -409       C  
+ATOM   1669  CE1 HIS A 221     -22.564   6.098  -5.540  1.00 53.48           C  
+ANISOU 1669  CE1 HIS A 221     8750   5560   6011     98   1450   -234       C  
+ATOM   1670  NE2 HIS A 221     -21.592   5.515  -6.217  1.00 58.37           N  
+ANISOU 1670  NE2 HIS A 221     9399   6151   6630    204   1539   -277       N  
+ATOM   1671  N   TYR A 222     -26.752   6.048 -10.349  1.00 50.79           N  
+ANISOU 1671  N   TYR A 222     8245   5732   5321   -943   1507   -793       N  
+ATOM   1672  CA  TYR A 222     -27.600   6.150 -11.529  1.00 48.37           C  
+ANISOU 1672  CA  TYR A 222     7847   5646   4886  -1161   1483   -914       C  
+ATOM   1673  C   TYR A 222     -27.426   7.486 -12.242  1.00 54.62           C  
+ANISOU 1673  C   TYR A 222     8427   6713   5612  -1131   1317   -797       C  
+ATOM   1674  O   TYR A 222     -27.158   8.508 -11.612  1.00 55.14           O  
+ANISOU 1674  O   TYR A 222     8399   6800   5752  -1003   1200   -627       O  
+ATOM   1675  CB  TYR A 222     -29.063   5.943 -11.137  1.00 50.52           C  
+ANISOU 1675  CB  TYR A 222     8115   5935   5145  -1352   1482   -985       C  
+ATOM   1676  CG  TYR A 222     -29.303   4.638 -10.413  1.00 56.12           C  
+ANISOU 1676  CG  TYR A 222     9048   6353   5922  -1406   1666  -1089       C  
+ATOM   1677  CD1 TYR A 222     -29.424   3.446 -11.114  1.00 58.06           C  
+ANISOU 1677  CD1 TYR A 222     9436   6501   6121  -1561   1840  -1301       C  
+ATOM   1678  CD2 TYR A 222     -29.398   4.597  -9.028  1.00 50.42           C  
+ANISOU 1678  CD2 TYR A 222     8407   5445   5307  -1305   1678   -974       C  
+ATOM   1679  CE1 TYR A 222     -29.637   2.250 -10.456  1.00 60.86           C  
+ANISOU 1679  CE1 TYR A 222    10019   6550   6553  -1614   2032  -1385       C  
+ATOM   1680  CE2 TYR A 222     -29.612   3.405  -8.362  1.00 55.83           C  
+ANISOU 1680  CE2 TYR A 222     9313   5850   6048  -1348   1860  -1040       C  
+ATOM   1681  CZ  TYR A 222     -29.731   2.235  -9.081  1.00 65.43           C  
+ANISOU 1681  CZ  TYR A 222    10680   6943   7236  -1502   2042  -1240       C  
+ATOM   1682  OH  TYR A 222     -29.944   1.046  -8.421  1.00 74.75           O  
+ANISOU 1682  OH  TYR A 222    12105   7809   8488  -1550   2247  -1297       O  
+ATOM   1683  N   CYS A 223     -27.579   7.467 -13.562  1.00 60.75           N  
+ANISOU 1683  N   CYS A 223     9139   7699   6246  -1256   1319   -892       N  
+ATOM   1684  CA  CYS A 223     -27.495   8.683 -14.363  1.00 52.53           C  
+ANISOU 1684  CA  CYS A 223     7912   6927   5118  -1240   1178   -768       C  
+ATOM   1685  C   CYS A 223     -28.608   8.732 -15.402  1.00 53.87           C  
+ANISOU 1685  C   CYS A 223     7981   7375   5113  -1441   1130   -863       C  
+ATOM   1686  O   CYS A 223     -28.785   7.791 -16.163  1.00 48.54           O  
+ANISOU 1686  O   CYS A 223     7371   6746   4326  -1588   1233  -1063       O  
+ATOM   1687  CB  CYS A 223     -26.133   8.780 -15.052  1.00 47.94           C  
+ANISOU 1687  CB  CYS A 223     7331   6374   4512  -1131   1223   -738       C  
+ATOM   1688  SG  CYS A 223     -26.004  10.128 -16.251  1.00 56.76           S  
+ANISOU 1688  SG  CYS A 223     8252   7821   5493  -1143   1093   -591       S  
+ATOM   1689  N   LEU A 224     -29.348   9.835 -15.442  1.00 52.21           N  
+ANISOU 1689  N   LEU A 224     7606   7359   4873  -1442    975   -724       N  
+ATOM   1690  CA  LEU A 224     -30.441   9.976 -16.399  1.00 53.78           C  
+ANISOU 1690  CA  LEU A 224     7673   7870   4889  -1606    903   -787       C  
+ATOM   1691  C   LEU A 224     -30.038  10.843 -17.585  1.00 54.43           C  
+ANISOU 1691  C   LEU A 224     7636   8220   4825  -1564    820   -664       C  
+ATOM   1692  O   LEU A 224     -29.624  11.990 -17.407  1.00 55.00           O  
+ANISOU 1692  O   LEU A 224     7636   8295   4965  -1415    730   -440       O  
+ATOM   1693  CB  LEU A 224     -31.673  10.580 -15.722  1.00 53.10           C  
+ANISOU 1693  CB  LEU A 224     7470   7857   4850  -1624    790   -711       C  
+ATOM   1694  CG  LEU A 224     -32.285   9.830 -14.538  1.00 56.61           C  
+ANISOU 1694  CG  LEU A 224     8009   8082   5418  -1687    867   -816       C  
+ATOM   1695  CD1 LEU A 224     -33.430  10.633 -13.937  1.00 50.95           C  
+ANISOU 1695  CD1 LEU A 224     7140   7477   4741  -1677    748   -720       C  
+ATOM   1696  CD2 LEU A 224     -32.758   8.449 -14.961  1.00 64.28           C  
+ANISOU 1696  CD2 LEU A 224     9075   9049   6300  -1915   1004  -1086       C  
+ATOM   1697  N   ILE A 225     -30.160  10.305 -18.795  1.00 51.00           N  
+ANISOU 1697  N   ILE A 225     7186   8009   4184  -1706    859   -812       N  
+ATOM   1698  CA  ILE A 225     -29.892  11.114 -19.986  1.00 54.92           C  
+ANISOU 1698  CA  ILE A 225     7565   8801   4502  -1679    781   -685       C  
+ATOM   1699  C   ILE A 225     -31.027  10.983 -20.993  1.00 68.09           C  
+ANISOU 1699  C   ILE A 225     9105  10847   5918  -1853    709   -789       C  
+ATOM   1700  O   ILE A 225     -31.936  10.183 -20.802  1.00 69.65           O  
+ANISOU 1700  O   ILE A 225     9307  11068   6089  -2017    736   -992       O  
+ATOM   1701  CB  ILE A 225     -28.556  10.732 -20.669  1.00 50.59           C  
+ANISOU 1701  CB  ILE A 225     7109   8211   3902  -1645    903   -737       C  
+ATOM   1702  CG1 ILE A 225     -28.604   9.300 -21.206  1.00 52.40           C  
+ANISOU 1702  CG1 ILE A 225     7450   8439   4022  -1817   1052  -1054       C  
+ATOM   1703  CG2 ILE A 225     -27.382  10.925 -19.715  1.00 49.43           C  
+ANISOU 1703  CG2 ILE A 225     7050   7744   3987  -1463    958   -627       C  
+ATOM   1704  CD1 ILE A 225     -27.388   8.925 -22.029  1.00 53.34           C  
+ANISOU 1704  CD1 ILE A 225     7639   8569   4060  -1786   1178  -1125       C  
+ATOM   1705  N   LYS A 226     -30.983  11.784 -22.053  1.00 60.91           N  
+ANISOU 1705  N   LYS A 226     8075  10249   4819  -1822    618   -643       N  
+ATOM   1706  CA  LYS A 226     -31.975  11.688 -23.119  1.00 55.95           C  
+ANISOU 1706  CA  LYS A 226     7307  10043   3910  -1973    536   -731       C  
+ATOM   1707  C   LYS A 226     -31.383  10.998 -24.340  1.00 57.94           C  
+ANISOU 1707  C   LYS A 226     7610  10475   3931  -2093    635   -909       C  
+ATOM   1708  O   LYS A 226     -30.241  11.261 -24.716  1.00 64.30           O  
+ANISOU 1708  O   LYS A 226     8478  11218   4734  -1994    698   -812       O  
+ATOM   1709  CB  LYS A 226     -32.505  13.069 -23.514  1.00 60.05           C  
+ANISOU 1709  CB  LYS A 226     7643  10837   4335  -1844    356   -429       C  
+ATOM   1710  CG  LYS A 226     -33.500  13.019 -24.670  1.00 69.99           C  
+ANISOU 1710  CG  LYS A 226     8732  12592   5269  -1974    252   -494       C  
+ATOM   1711  CD  LYS A 226     -33.896  14.400 -25.163  1.00 76.46           C  
+ANISOU 1711  CD  LYS A 226     9387  13684   5981  -1804     84   -155       C  
+ATOM   1712  CE  LYS A 226     -34.518  14.320 -26.549  1.00 99.65           C  
+ANISOU 1712  CE  LYS A 226    12173  17154   8534  -1912     -5   -201       C  
+ATOM   1713  NZ  LYS A 226     -35.001  15.641 -27.037  1.00116.57           N  
+ANISOU 1713  NZ  LYS A 226    14153  19579  10558  -1724   -172    153       N  
+ATOM   1714  N   LYS A 227     -32.162  10.108 -24.948  1.00 66.42           N  
+ANISOU 1714  N   LYS A 227     8649  11778   4809  -2319    656  -1186       N  
+ATOM   1715  CA  LYS A 227     -31.730   9.414 -26.153  1.00 74.49           C  
+ANISOU 1715  CA  LYS A 227     9711  13007   5584  -2458    752  -1398       C  
+ATOM   1716  C   LYS A 227     -31.429  10.395 -27.273  1.00 63.70           C  
+ANISOU 1716  C   LYS A 227     8226  12003   3975  -2369    652  -1170       C  
+ATOM   1717  O   LYS A 227     -32.186  11.337 -27.507  1.00 75.24           O  
+ANISOU 1717  O   LYS A 227     9516  13745   5328  -2305    476   -951       O  
+ATOM   1718  CB  LYS A 227     -32.806   8.427 -26.611  1.00 78.05           C  
+ANISOU 1718  CB  LYS A 227    10113  13694   5850  -2741    768  -1739       C  
+ATOM   1719  CG  LYS A 227     -32.432   7.614 -27.839  1.00 85.46           C  
+ANISOU 1719  CG  LYS A 227    11100  14847   6523  -2917    882  -2015       C  
+ATOM   1720  CD  LYS A 227     -33.049   6.227 -27.789  1.00 98.70           C  
+ANISOU 1720  CD  LYS A 227    12859  16458   8184  -3202   1014  -2438       C  
+ATOM   1721  CE  LYS A 227     -32.371   5.285 -28.769  1.00103.09           C  
+ANISOU 1721  CE  LYS A 227    13509  16978   8684  -3291   1171  -2678       C  
+ATOM   1722  NZ  LYS A 227     -33.182   4.057 -29.002  1.00 94.72           N  
+ANISOU 1722  NZ  LYS A 227    12446  15886   7655  -3558   1256  -3025       N  
+ATOM   1723  N   GLU A 228     -30.317  10.173 -27.963  1.00 67.37           N  
+ANISOU 1723  N   GLU A 228     8783  12461   4354  -2353    774  -1211       N  
+ATOM   1724  CA  GLU A 228     -29.982  10.996 -29.110  1.00 65.84           C  
+ANISOU 1724  CA  GLU A 228     8494  12622   3899  -2294    710  -1010       C  
+ATOM   1725  C   GLU A 228     -30.930  10.654 -30.252  1.00 69.17           C  
+ANISOU 1725  C   GLU A 228     8786  13552   3942  -2489    634  -1185       C  
+ATOM   1726  O   GLU A 228     -31.119   9.484 -30.581  1.00 74.71           O  
+ANISOU 1726  O   GLU A 228     9540  14274   4573  -2690    735  -1546       O  
+ATOM   1727  CB  GLU A 228     -28.526  10.787 -29.526  1.00 65.78           C  
+ANISOU 1727  CB  GLU A 228     8612  12484   3898  -2239    881  -1032       C  
+ATOM   1728  CG  GLU A 228     -27.818  12.063 -29.955  1.00 65.55           C  
+ANISOU 1728  CG  GLU A 228     8526  12558   3823  -2067    831   -663       C  
+ATOM   1729  CD  GLU A 228     -27.516  12.990 -28.790  1.00 80.06           C  
+ANISOU 1729  CD  GLU A 228    10375  14050   5994  -1871    779   -376       C  
+ATOM   1730  OE1 GLU A 228     -27.541  12.524 -27.631  1.00 85.06           O  
+ANISOU 1730  OE1 GLU A 228    11086  14331   6901  -1850    815   -481       O  
+ATOM   1731  OE2 GLU A 228     -27.253  14.187 -29.033  1.00 75.34           O  
+ANISOU 1731  OE2 GLU A 228     9716  13532   5379  -1743    711    -48       O  
+ATOM   1732  N   GLU A 229     -31.523  11.676 -30.857  1.00 70.67           N  
+ANISOU 1732  N   GLU A 229     8803  14125   3925  -2415    456   -920       N  
+ATOM   1733  CA  GLU A 229     -32.470  11.467 -31.945  1.00 73.87           C  
+ANISOU 1733  CA  GLU A 229     9030  14945   4093  -2529    342  -1025       C  
+ATOM   1734  C   GLU A 229     -31.989  12.143 -33.221  1.00 76.05           C  
+ANISOU 1734  C   GLU A 229     9240  15497   4159  -2429    303   -811       C  
+ATOM   1735  O   GLU A 229     -31.196  13.083 -33.177  1.00 81.58           O  
+ANISOU 1735  O   GLU A 229     9991  16114   4892  -2250    314   -496       O  
+ATOM   1736  CB  GLU A 229     -33.862  11.966 -31.556  1.00 78.94           C  
+ANISOU 1736  CB  GLU A 229     9481  15800   4714  -2514    146   -919       C  
+ATOM   1737  CG  GLU A 229     -33.870  13.155 -30.619  1.00 93.81           C  
+ANISOU 1737  CG  GLU A 229    11358  17543   6743  -2291     56   -550       C  
+ATOM   1738  CD  GLU A 229     -35.124  13.200 -29.769  1.00112.39           C  
+ANISOU 1738  CD  GLU A 229    13581  19893   9228  -2302    -63   -575       C  
+ATOM   1739  OE1 GLU A 229     -35.506  12.144 -29.222  1.00113.36           O  
+ANISOU 1739  OE1 GLU A 229    13750  19867   9453  -2494     16   -906       O  
+ATOM   1740  OE2 GLU A 229     -35.731  14.285 -29.652  1.00125.08           O  
+ANISOU 1740  OE2 GLU A 229    15044  21640  10840  -2118   -223   -264       O  
+ATOM   1741  N   ARG A 230     -32.471  11.654 -34.359  1.00 79.49           N  
+ANISOU 1741  N   ARG A 230     9563  16258   4383  -2558    268   -985       N  
+ATOM   1742  CA  ARG A 230     -32.037  12.166 -35.650  1.00 82.05           C  
+ANISOU 1742  CA  ARG A 230     9831  16860   4482  -2487    245   -820       C  
+ATOM   1743  C   ARG A 230     -32.534  13.583 -35.906  1.00 82.75           C  
+ANISOU 1743  C   ARG A 230     9774  17194   4474  -2280     60   -383       C  
+ATOM   1744  O   ARG A 230     -33.687  13.911 -35.627  1.00103.62           O  
+ANISOU 1744  O   ARG A 230    12259  20008   7104  -2253    -99   -309       O  
+ATOM   1745  CB  ARG A 230     -32.540  11.255 -36.773  1.00100.21           C  
+ANISOU 1745  CB  ARG A 230    12034  19472   6570  -2689    247  -1133       C  
+ATOM   1746  CG  ARG A 230     -32.067   9.815 -36.708  1.00101.46           C  
+ANISOU 1746  CG  ARG A 230    12340  19391   6817  -2893    446  -1571       C  
+ATOM   1747  CD  ARG A 230     -32.620   9.023 -37.886  1.00 98.04           C  
+ANISOU 1747  CD  ARG A 230    11793  19296   6162  -3096    441  -1856       C  
+ATOM   1748  NE  ARG A 230     -31.615   8.164 -38.500  1.00 98.40           N  
+ANISOU 1748  NE  ARG A 230    11987  19218   6183  -3182    637  -2104       N  
+ATOM   1749  CZ  ARG A 230     -31.395   6.898 -38.163  1.00109.14           C  
+ANISOU 1749  CZ  ARG A 230    13487  20287   7695  -3346    813  -2478       C  
+ATOM   1750  NH1 ARG A 230     -32.118   6.322 -37.211  1.00108.91           N  
+ANISOU 1750  NH1 ARG A 230    13476  20053   7852  -3461    823  -2650       N  
+ATOM   1751  NH2 ARG A 230     -30.453   6.202 -38.787  1.00114.01           N  
+ANISOU 1751  NH2 ARG A 230    14230  20807   8281  -3390    990  -2675       N  
+ATOM   1752  N   ARG A 231     -31.651  14.420 -36.438  1.00 93.71           N  
+ANISOU 1752  N   ARG A 231    11218  18583   5806  -2128     93    -90       N  
+ATOM   1753  CA  ARG A 231     -32.023  15.770 -36.831  1.00 95.10           C  
+ANISOU 1753  CA  ARG A 231    11283  18960   5891  -1920    -53    342       C  
+ATOM   1754  C   ARG A 231     -32.491  15.743 -38.283  1.00 97.06           C  
+ANISOU 1754  C   ARG A 231    11386  19663   5829  -1959   -131    329       C  
+ATOM   1755  O   ARG A 231     -32.009  14.928 -39.071  1.00 97.54           O  
+ANISOU 1755  O   ARG A 231    11487  19818   5756  -2109    -28     71       O  
+ATOM   1756  CB  ARG A 231     -30.861  16.748 -36.623  1.00 86.58           C  
+ANISOU 1756  CB  ARG A 231    10343  17621   4932  -1746     38    684       C  
+ATOM   1757  CG  ARG A 231     -30.734  17.228 -35.179  1.00 82.09           C  
+ANISOU 1757  CG  ARG A 231     9854  16685   4653  -1645     46    832       C  
+ATOM   1758  CD  ARG A 231     -29.303  17.547 -34.772  1.00 78.78           C  
+ANISOU 1758  CD  ARG A 231     9607  15923   4403  -1590    219    953       C  
+ATOM   1759  NE  ARG A 231     -29.212  17.824 -33.339  1.00 93.10           N  
+ANISOU 1759  NE  ARG A 231    11490  17397   6489  -1529    234   1033       N  
+ATOM   1760  CZ  ARG A 231     -28.085  18.118 -32.698  1.00 92.33           C  
+ANISOU 1760  CZ  ARG A 231    11519  16968   6595  -1483    371   1132       C  
+ATOM   1761  NH1 ARG A 231     -26.938  18.176 -33.360  1.00 94.72           N  
+ANISOU 1761  NH1 ARG A 231    11890  17253   6847  -1495    513   1166       N  
+ATOM   1762  NH2 ARG A 231     -28.106  18.356 -31.394  1.00 81.98           N  
+ANISOU 1762  NH2 ARG A 231    10247  15238   5664  -1397    359   1162       N  
+ATOM   1763  N   PRO A 232     -33.436  16.628 -38.639  1.00103.92           N  
+ANISOU 1763  N   PRO A 232    12083  20819   6583  -1815   -309    606       N  
+ATOM   1764  CA  PRO A 232     -33.980  16.661 -40.002  1.00108.33           C  
+ANISOU 1764  CA  PRO A 232    12480  21848   6830  -1835   -399    617       C  
+ATOM   1765  C   PRO A 232     -32.911  16.902 -41.065  1.00115.74           C  
+ANISOU 1765  C   PRO A 232    13522  22847   7609  -1810   -292    729       C  
+ATOM   1766  O   PRO A 232     -32.697  16.038 -41.916  1.00117.49           O  
+ANISOU 1766  O   PRO A 232    13735  23257   7649  -1984   -226    443       O  
+ATOM   1767  CB  PRO A 232     -34.977  17.827 -39.955  1.00105.49           C  
+ANISOU 1767  CB  PRO A 232    11958  21678   6445  -1606   -587    993       C  
+ATOM   1768  CG  PRO A 232     -34.568  18.646 -38.771  1.00105.53           C  
+ANISOU 1768  CG  PRO A 232    12092  21262   6742  -1430   -560   1265       C  
+ATOM   1769  CD  PRO A 232     -34.039  17.661 -37.781  1.00100.02           C  
+ANISOU 1769  CD  PRO A 232    11534  20221   6247  -1608   -430    932       C  
+ATOM   1770  N   ASP A 233     -32.247  18.051 -41.013  1.00115.23           N  
+ANISOU 1770  N   ASP A 233    13553  22612   7616  -1604   -264   1133       N  
+ATOM   1771  CA  ASP A 233     -31.205  18.361 -41.983  1.00116.63           C  
+ANISOU 1771  CA  ASP A 233    13830  22833   7653  -1580   -150   1265       C  
+ATOM   1772  C   ASP A 233     -29.841  17.920 -41.476  1.00125.66           C  
+ANISOU 1772  C   ASP A 233    15175  23591   8980  -1656     61   1125       C  
+ATOM   1773  O   ASP A 233     -29.031  18.746 -41.055  1.00130.06           O  
+ANISOU 1773  O   ASP A 233    15850  23866   9700  -1529    142   1405       O  
+ATOM   1774  CB  ASP A 233     -31.188  19.859 -42.289  1.00111.69           C  
+ANISOU 1774  CB  ASP A 233    13206  22224   7006  -1330   -208   1781       C  
+ATOM   1775  N   GLU A 234     -29.585  16.617 -41.524  1.00123.34           N  
+ANISOU 1775  N   GLU A 234    14915  23281   8667  -1862    160    689       N  
+ATOM   1776  CA  GLU A 234     -28.258  16.103 -41.215  1.00110.75           C  
+ANISOU 1776  CA  GLU A 234    13496  21369   7215  -1925    373    531       C  
+ATOM   1777  C   GLU A 234     -28.003  14.720 -41.802  1.00102.33           C  
+ANISOU 1777  C   GLU A 234    12452  20396   6033  -2133    485     74       C  
+ATOM   1778  O   GLU A 234     -28.931  13.934 -42.001  1.00 95.86           O  
+ANISOU 1778  O   GLU A 234    11533  19773   5117  -2274    408   -204       O  
+ATOM   1779  CB  GLU A 234     -28.064  16.057 -39.698  1.00 88.35           C  
+ANISOU 1779  CB  GLU A 234    10750  18112   4706  -1893    415    513       C  
+ATOM   1780  CG  GLU A 234     -28.667  14.825 -39.038  1.00 87.10           C  
+ANISOU 1780  CG  GLU A 234    10585  17873   4637  -2059    414    100       C  
+ATOM   1781  CD  GLU A 234     -28.237  14.656 -37.595  1.00103.01           C  
+ANISOU 1781  CD  GLU A 234    12722  19456   6962  -2037    498     54       C  
+ATOM   1782  OE1 GLU A 234     -27.510  15.531 -37.081  1.00102.74           O  
+ANISOU 1782  OE1 GLU A 234    12760  19202   7076  -1896    544    345       O  
+ATOM   1783  OE2 GLU A 234     -28.625  13.642 -36.977  1.00 81.82           O  
+ANISOU 1783  OE2 GLU A 234    10064  16648   4377  -2170    526   -276       O  
+ATOM   1784  N   LEU A 235     -26.737  14.435 -42.090  1.00 96.98           N  
+ANISOU 1784  N   LEU A 235    11900  19575   5373  -2155    677     -5       N  
+ATOM   1785  CA  LEU A 235     -26.358  13.158 -42.677  1.00 95.87           C  
+ANISOU 1785  CA  LEU A 235    11801  19487   5140  -2328    811   -426       C  
+ATOM   1786  C   LEU A 235     -26.516  12.090 -41.605  1.00105.71           C  
+ANISOU 1786  C   LEU A 235    13118  20423   6623  -2434    875   -770       C  
+ATOM   1787  O   LEU A 235     -26.580  12.404 -40.416  1.00102.90           O  
+ANISOU 1787  O   LEU A 235    12805  19787   6505  -2357    852   -658       O  
+ATOM   1788  CB  LEU A 235     -24.934  13.193 -43.228  1.00 99.68           C  
+ANISOU 1788  CB  LEU A 235    12390  19892   5592  -2296   1009   -400       C  
+ATOM   1789  CG  LEU A 235     -24.726  14.173 -44.384  1.00 99.60           C  
+ANISOU 1789  CG  LEU A 235    12328  20186   5330  -2213    973    -78       C  
+ATOM   1790  CD1 LEU A 235     -23.280  14.165 -44.852  1.00110.77           C  
+ANISOU 1790  CD1 LEU A 235    13845  21509   6734  -2197   1188    -71       C  
+ATOM   1791  CD2 LEU A 235     -25.666  13.840 -45.534  1.00103.84           C  
+ANISOU 1791  CD2 LEU A 235    12732  21178   5545  -2315    852   -204       C  
+ATOM   1792  N   GLU A 236     -26.570  10.831 -42.014  1.00 94.99           N  
+ANISOU 1792  N   GLU A 236    11784  19102   5207  -2610    965  -1187       N  
+ATOM   1793  CA  GLU A 236     -26.909   9.774 -41.077  1.00 94.63           C  
+ANISOU 1793  CA  GLU A 236    11805  18776   5374  -2726   1021  -1518       C  
+ATOM   1794  C   GLU A 236     -25.649   9.401 -40.293  1.00 93.82           C  
+ANISOU 1794  C   GLU A 236    11886  18239   5523  -2656   1229  -1593       C  
+ATOM   1795  O   GLU A 236     -25.712   8.821 -39.201  1.00 94.54           O  
+ANISOU 1795  O   GLU A 236    12067  18000   5856  -2679   1286  -1751       O  
+ATOM   1796  CB  GLU A 236     -27.479   8.570 -41.824  1.00 96.53           C  
+ANISOU 1796  CB  GLU A 236    12006  19198   5474  -2949   1051  -1932       C  
+ATOM   1797  CG  GLU A 236     -28.666   7.928 -41.134  1.00109.69           C  
+ANISOU 1797  CG  GLU A 236    13620  20808   7249  -3094    973  -2151       C  
+ATOM   1798  CD  GLU A 236     -29.911   8.810 -41.218  1.00125.12           C  
+ANISOU 1798  CD  GLU A 236    15367  23103   9072  -3062    726  -1907       C  
+ATOM   1799  OE1 GLU A 236     -29.863   9.867 -41.884  1.00126.85           O  
+ANISOU 1799  OE1 GLU A 236    15494  23598   9107  -2924    619  -1574       O  
+ATOM   1800  OE2 GLU A 236     -30.947   8.445 -40.629  1.00123.42           O  
+ANISOU 1800  OE2 GLU A 236    15076  22880   8939  -3168    646  -2041       O  
+ATOM   1801  N   ALA A 237     -24.505   9.782 -40.855  1.00 93.47           N  
+ANISOU 1801  N   ALA A 237    11886  18211   5419  -2564   1344  -1462       N  
+ATOM   1802  CA  ALA A 237     -23.207   9.542 -40.241  1.00 88.79           C  
+ANISOU 1802  CA  ALA A 237    11430  17266   5040  -2476   1546  -1501       C  
+ATOM   1803  C   ALA A 237     -23.042  10.435 -39.021  1.00 84.97           C  
+ANISOU 1803  C   ALA A 237    10966  16538   4782  -2334   1499  -1201       C  
+ATOM   1804  O   ALA A 237     -22.379  10.062 -38.057  1.00 82.48           O  
+ANISOU 1804  O   ALA A 237    10751  15880   4706  -2283   1626  -1287       O  
+ATOM   1805  CB  ALA A 237     -22.086   9.785 -41.241  1.00 90.86           C  
+ANISOU 1805  CB  ALA A 237    11702  17661   5159  -2425   1676  -1428       C  
+ATOM   1806  N   ASP A 238     -23.626  11.627 -39.083  1.00 84.80           N  
+ANISOU 1806  N   ASP A 238    10846  16694   4680  -2261   1324   -844       N  
+ATOM   1807  CA  ASP A 238     -23.592  12.557 -37.960  1.00 85.96           C  
+ANISOU 1807  CA  ASP A 238    11002  16625   5032  -2134   1266   -544       C  
+ATOM   1808  C   ASP A 238     -24.425  12.014 -36.800  1.00 87.34           C  
+ANISOU 1808  C   ASP A 238    11201  16599   5384  -2183   1203   -709       C  
+ATOM   1809  O   ASP A 238     -24.007  12.062 -35.634  1.00 92.76           O  
+ANISOU 1809  O   ASP A 238    11964  16968   6311  -2119   1264   -676       O  
+ATOM   1810  CB  ASP A 238     -24.112  13.931 -38.387  1.00 90.43           C  
+ANISOU 1810  CB  ASP A 238    11465  17423   5472  -2035   1097   -125       C  
+ATOM   1811  CG  ASP A 238     -23.336  14.511 -39.554  1.00103.00           C  
+ANISOU 1811  CG  ASP A 238    13045  19208   6882  -1993   1165     59       C  
+ATOM   1812  OD1 ASP A 238     -22.516  13.780 -40.147  1.00104.15           O  
+ANISOU 1812  OD1 ASP A 238    13240  19370   6962  -2057   1325   -169       O  
+ATOM   1813  OD2 ASP A 238     -23.550  15.698 -39.882  1.00111.34           O  
+ANISOU 1813  OD2 ASP A 238    14049  20391   7866  -1891   1067    433       O  
+ATOM   1814  N   PHE A 239     -25.602  11.489 -37.129  1.00 80.89           N  
+ANISOU 1814  N   PHE A 239    10310  15980   4445  -2306   1086   -894       N  
+ATOM   1815  CA  PHE A 239     -26.472  10.895 -36.123  1.00 79.21           C  
+ANISOU 1815  CA  PHE A 239    10112  15600   4384  -2384   1037  -1079       C  
+ATOM   1816  C   PHE A 239     -25.798   9.697 -35.478  1.00 78.15           C  
+ANISOU 1816  C   PHE A 239    10141  15103   4448  -2443   1239  -1413       C  
+ATOM   1817  O   PHE A 239     -25.791   9.572 -34.255  1.00 75.17           O  
+ANISOU 1817  O   PHE A 239     9843  14421   4296  -2409   1270  -1426       O  
+ATOM   1818  CB  PHE A 239     -27.812  10.476 -36.726  1.00 87.38           C  
+ANISOU 1818  CB  PHE A 239    11014  16944   5241  -2534    896  -1247       C  
+ATOM   1819  CG  PHE A 239     -28.670   9.680 -35.783  1.00 89.25           C  
+ANISOU 1819  CG  PHE A 239    11272  17004   5636  -2656    881  -1496       C  
+ATOM   1820  CD1 PHE A 239     -29.187  10.261 -34.637  1.00 92.06           C  
+ANISOU 1820  CD1 PHE A 239    11612  17220   6148  -2578    783  -1317       C  
+ATOM   1821  CD2 PHE A 239     -28.949   8.347 -36.038  1.00 82.44           C  
+ANISOU 1821  CD2 PHE A 239    10452  16099   4773  -2855    979  -1909       C  
+ATOM   1822  CE1 PHE A 239     -29.972   9.529 -33.765  1.00 76.94           C  
+ANISOU 1822  CE1 PHE A 239     9718  15139   4375  -2699    782  -1546       C  
+ATOM   1823  CE2 PHE A 239     -29.734   7.610 -35.170  1.00 82.46           C  
+ANISOU 1823  CE2 PHE A 239    10483  15914   4934  -2982    985  -2131       C  
+ATOM   1824  CZ  PHE A 239     -30.247   8.202 -34.033  1.00 78.79           C  
+ANISOU 1824  CZ  PHE A 239     9998  15323   4614  -2905    886  -1949       C  
+ATOM   1825  N   GLU A 240     -25.216   8.825 -36.296  1.00 84.79           N  
+ANISOU 1825  N   GLU A 240    11037  15970   5209  -2518   1385  -1673       N  
+ATOM   1826  CA  GLU A 240     -24.544   7.650 -35.753  1.00 93.31           C  
+ANISOU 1826  CA  GLU A 240    12278  16688   6485  -2546   1592  -1984       C  
+ATOM   1827  C   GLU A 240     -23.290   8.059 -34.988  1.00 87.36           C  
+ANISOU 1827  C   GLU A 240    11612  15658   5924  -2368   1717  -1818       C  
+ATOM   1828  O   GLU A 240     -22.827   7.333 -34.109  1.00 93.08           O  
+ANISOU 1828  O   GLU A 240    12465  16030   6870  -2334   1858  -1985       O  
+ATOM   1829  CB  GLU A 240     -24.204   6.647 -36.857  1.00 82.91           C  
+ANISOU 1829  CB  GLU A 240    10996  15466   5039  -2653   1725  -2294       C  
+ATOM   1830  CG  GLU A 240     -25.374   5.751 -37.241  1.00 95.33           C  
+ANISOU 1830  CG  GLU A 240    12532  17160   6529  -2871   1672  -2594       C  
+ATOM   1831  CD  GLU A 240     -25.777   4.806 -36.119  1.00102.91           C  
+ANISOU 1831  CD  GLU A 240    13615  17738   7747  -2945   1750  -2828       C  
+ATOM   1832  OE1 GLU A 240     -24.950   4.559 -35.215  1.00103.03           O  
+ANISOU 1832  OE1 GLU A 240    13776  17374   7994  -2822   1891  -2832       O  
+ATOM   1833  OE2 GLU A 240     -26.924   4.313 -36.137  1.00115.95           O  
+ANISOU 1833  OE2 GLU A 240    15212  19474   9371  -3126   1675  -3002       O  
+ATOM   1834  N   TYR A 241     -22.744   9.223 -35.328  1.00 76.57           N  
+ANISOU 1834  N   TYR A 241    10168  14449   4475  -2255   1672  -1485       N  
+ATOM   1835  CA  TYR A 241     -21.648   9.800 -34.561  1.00 74.12           C  
+ANISOU 1835  CA  TYR A 241     9898  13916   4347  -2104   1767  -1287       C  
+ATOM   1836  C   TYR A 241     -22.096  10.147 -33.150  1.00 77.02           C  
+ANISOU 1836  C   TYR A 241    10292  14052   4921  -2058   1692  -1170       C  
+ATOM   1837  O   TYR A 241     -21.462   9.734 -32.178  1.00 72.76           O  
+ANISOU 1837  O   TYR A 241     9840  13157   4649  -1974   1798  -1244       O  
+ATOM   1838  CB  TYR A 241     -21.085  11.046 -35.252  1.00 74.83           C  
+ANISOU 1838  CB  TYR A 241     9896  14223   4314  -2022   1731   -934       C  
+ATOM   1839  CG  TYR A 241     -20.131  11.839 -34.383  1.00 72.33           C  
+ANISOU 1839  CG  TYR A 241     9586  13700   4197  -1894   1797   -686       C  
+ATOM   1840  CD1 TYR A 241     -18.788  11.499 -34.294  1.00 86.91           C  
+ANISOU 1840  CD1 TYR A 241    11470  15400   6151  -1830   1999   -775       C  
+ATOM   1841  CD2 TYR A 241     -20.576  12.941 -33.659  1.00 70.36           C  
+ANISOU 1841  CD2 TYR A 241     9291  13410   4032  -1836   1660   -366       C  
+ATOM   1842  CE1 TYR A 241     -17.918  12.225 -33.497  1.00 84.89           C  
+ANISOU 1842  CE1 TYR A 241    11189  14947   6118  -1716   2042   -556       C  
+ATOM   1843  CE2 TYR A 241     -19.716  13.670 -32.863  1.00 76.48           C  
+ANISOU 1843  CE2 TYR A 241    10058  13903   5098  -1703   1687   -145       C  
+ATOM   1844  CZ  TYR A 241     -18.389  13.311 -32.786  1.00 82.99           C  
+ANISOU 1844  CZ  TYR A 241    10904  14587   6041  -1652   1872   -244       C  
+ATOM   1845  OH  TYR A 241     -17.533  14.042 -31.993  1.00 81.42           O  
+ANISOU 1845  OH  TYR A 241    10673  14138   6125  -1537   1891    -43       O  
+ATOM   1846  N   ARG A 242     -23.181  10.910 -33.033  1.00 70.50           N  
+ANISOU 1846  N   ARG A 242     9377  13384   4026  -2076   1491   -968       N  
+ATOM   1847  CA  ARG A 242     -23.677  11.269 -31.706  1.00 67.63           C  
+ANISOU 1847  CA  ARG A 242     9020  12730   3948  -1995   1383   -838       C  
+ATOM   1848  C   ARG A 242     -24.105  10.033 -30.919  1.00 76.34           C  
+ANISOU 1848  C   ARG A 242    10228  13557   5222  -2070   1442  -1166       C  
+ATOM   1849  O   ARG A 242     -23.893   9.960 -29.707  1.00 70.70           O  
+ANISOU 1849  O   ARG A 242     9575  12459   4829  -1964   1451  -1129       O  
+ATOM   1850  CB  ARG A 242     -24.839  12.260 -31.783  1.00 67.76           C  
+ANISOU 1850  CB  ARG A 242     8912  12977   3858  -1988   1161   -579       C  
+ATOM   1851  CG  ARG A 242     -24.405  13.715 -31.848  1.00 67.22           C  
+ANISOU 1851  CG  ARG A 242     8778  12935   3826  -1837   1093   -155       C  
+ATOM   1852  CD  ARG A 242     -25.601  14.651 -31.933  1.00 67.70           C  
+ANISOU 1852  CD  ARG A 242     8724  13213   3787  -1800    883    101       C  
+ATOM   1853  NE  ARG A 242     -26.710  14.086 -32.694  1.00 70.09           N  
+ANISOU 1853  NE  ARG A 242     8951  13906   3773  -1948    796    -85       N  
+ATOM   1854  CZ  ARG A 242     -26.971  14.371 -33.964  1.00 93.52           C  
+ANISOU 1854  CZ  ARG A 242    11824  17204   6505  -1953    726     -7       C  
+ATOM   1855  NH1 ARG A 242     -26.202  15.223 -34.628  1.00 93.23           N  
+ANISOU 1855  NH1 ARG A 242    11785  17235   6404  -1853    761    265       N  
+ATOM   1856  NH2 ARG A 242     -28.007  13.807 -34.570  1.00101.02           N  
+ANISOU 1856  NH2 ARG A 242    12677  18419   7286  -2067    626   -202       N  
+ATOM   1857  N   VAL A 243     -24.712   9.070 -31.608  1.00 69.20           N  
+ANISOU 1857  N   VAL A 243     9347  12853   4092  -2260   1489  -1486       N  
+ATOM   1858  CA  VAL A 243     -25.111   7.815 -30.978  1.00 76.83           C  
+ANISOU 1858  CA  VAL A 243    10435  13551   5205  -2363   1581  -1820       C  
+ATOM   1859  C   VAL A 243     -23.891   7.083 -30.428  1.00 73.14           C  
+ANISOU 1859  C   VAL A 243    10122  12682   4984  -2248   1791  -1943       C  
+ATOM   1860  O   VAL A 243     -23.913   6.581 -29.305  1.00 69.83           O  
+ANISOU 1860  O   VAL A 243     9805  11879   4849  -2189   1831  -1999       O  
+ATOM   1861  CB  VAL A 243     -25.863   6.893 -31.964  1.00 80.41           C  
+ANISOU 1861  CB  VAL A 243    10860  14200   5493  -2560   1579  -2121       C  
+ATOM   1862  CG1 VAL A 243     -26.062   5.508 -31.365  1.00 72.57           C  
+ANISOU 1862  CG1 VAL A 243    10024  12863   4687  -2666   1727  -2469       C  
+ATOM   1863  CG2 VAL A 243     -27.200   7.504 -32.347  1.00 75.38           C  
+ANISOU 1863  CG2 VAL A 243    10042  13919   4680  -2650   1350  -2007       C  
+ATOM   1864  N   ARG A 244     -22.827   7.031 -31.224  1.00 70.57           N  
+ANISOU 1864  N   ARG A 244     9808  12464   4541  -2204   1926  -1976       N  
+ATOM   1865  CA  ARG A 244     -21.586   6.393 -30.801  1.00 69.04           C  
+ANISOU 1865  CA  ARG A 244     9730  11940   4563  -2065   2126  -2078       C  
+ATOM   1866  C   ARG A 244     -20.969   7.106 -29.597  1.00 69.26           C  
+ANISOU 1866  C   ARG A 244     9736  11664   4914  -1845   2066  -1787       C  
+ATOM   1867  O   ARG A 244     -20.489   6.460 -28.666  1.00 69.41           O  
+ANISOU 1867  O   ARG A 244     9862  11317   5195  -1730   2162  -1868       O  
+ATOM   1868  CB  ARG A 244     -20.584   6.345 -31.956  1.00 71.26           C  
+ANISOU 1868  CB  ARG A 244     9980  12428   4667  -2043   2256  -2130       C  
+ATOM   1869  CG  ARG A 244     -19.245   5.729 -31.586  1.00 71.10           C  
+ANISOU 1869  CG  ARG A 244    10055  12133   4827  -1888   2482  -2243       C  
+ATOM   1870  CD  ARG A 244     -19.420   4.347 -30.975  1.00 71.50           C  
+ANISOU 1870  CD  ARG A 244    10283  11815   5069  -1893   2615  -2550       C  
+ATOM   1871  NE  ARG A 244     -18.142   3.732 -30.632  1.00 82.82           N  
+ANISOU 1871  NE  ARG A 244    11801  12983   6683  -1704   2829  -2643       N  
+ATOM   1872  CZ  ARG A 244     -18.018   2.577 -29.986  1.00 79.70           C  
+ANISOU 1872  CZ  ARG A 244    11577  12209   6498  -1636   2976  -2856       C  
+ATOM   1873  NH1 ARG A 244     -19.098   1.908 -29.604  1.00 81.32           N  
+ANISOU 1873  NH1 ARG A 244    11890  12242   6766  -1770   2939  -3000       N  
+ATOM   1874  NH2 ARG A 244     -16.814   2.091 -29.715  1.00 76.04           N  
+ANISOU 1874  NH2 ARG A 244    11165  11532   6197  -1423   3156  -2904       N  
+ATOM   1875  N   LYS A 245     -20.985   8.436 -29.621  1.00 64.83           N  
+ANISOU 1875  N   LYS A 245     9043  11261   4329  -1785   1911  -1450       N  
+ATOM   1876  CA  LYS A 245     -20.455   9.227 -28.512  1.00 67.84           C  
+ANISOU 1876  CA  LYS A 245     9390  11384   5000  -1606   1844  -1183       C  
+ATOM   1877  C   LYS A 245     -21.235   8.989 -27.224  1.00 68.32           C  
+ANISOU 1877  C   LYS A 245     9510  11153   5296  -1581   1755  -1191       C  
+ATOM   1878  O   LYS A 245     -20.651   8.852 -26.145  1.00 68.87           O  
+ANISOU 1878  O   LYS A 245     9630  10905   5633  -1437   1789  -1153       O  
+ATOM   1879  CB  LYS A 245     -20.488  10.718 -28.854  1.00 61.76           C  
+ANISOU 1879  CB  LYS A 245     8484  10834   4149  -1579   1706   -834       C  
+ATOM   1880  CG  LYS A 245     -19.436  11.171 -29.848  1.00 71.91           C  
+ANISOU 1880  CG  LYS A 245     9709  12336   5277  -1562   1809   -743       C  
+ATOM   1881  CD  LYS A 245     -18.879  12.532 -29.456  1.00 77.11           C  
+ANISOU 1881  CD  LYS A 245    10278  12940   6079  -1456   1740   -392       C  
+ATOM   1882  CE  LYS A 245     -17.946  12.443 -28.259  1.00 64.09           C  
+ANISOU 1882  CE  LYS A 245     8646  10939   4766  -1311   1794   -386       C  
+ATOM   1883  NZ  LYS A 245     -16.656  11.789 -28.610  1.00 61.43           N  
+ANISOU 1883  NZ  LYS A 245     8314  10596   4430  -1260   1993   -544       N  
+ATOM   1884  N   GLN A 246     -22.557   8.928 -27.347  1.00 69.47           N  
+ANISOU 1884  N   GLN A 246     9639  11432   5325  -1722   1642  -1244       N  
+ATOM   1885  CA  GLN A 246     -23.422   8.661 -26.206  1.00 71.87           C  
+ANISOU 1885  CA  GLN A 246     9991  11495   5820  -1728   1568  -1270       C  
+ATOM   1886  C   GLN A 246     -23.180   7.250 -25.681  1.00 69.92           C  
+ANISOU 1886  C   GLN A 246     9917  10937   5712  -1738   1742  -1555       C  
+ATOM   1887  O   GLN A 246     -23.209   7.012 -24.476  1.00 57.57           O  
+ANISOU 1887  O   GLN A 246     8428   9055   4393  -1648   1743  -1527       O  
+ATOM   1888  CB  GLN A 246     -24.892   8.857 -26.585  1.00 59.80           C  
+ANISOU 1888  CB  GLN A 246     8379  10232   4109  -1893   1423  -1289       C  
+ATOM   1889  CG  GLN A 246     -25.859   8.715 -25.420  1.00 58.25           C  
+ANISOU 1889  CG  GLN A 246     8205   9827   4101  -1908   1341  -1293       C  
+ATOM   1890  CD  GLN A 246     -27.268   9.152 -25.772  1.00 60.59           C  
+ANISOU 1890  CD  GLN A 246     8365  10430   4225  -2037   1174  -1258       C  
+ATOM   1891  OE1 GLN A 246     -27.935   8.531 -26.599  1.00 61.41           O  
+ANISOU 1891  OE1 GLN A 246     8446  10787   4100  -2228   1189  -1481       O  
+ATOM   1892  NE2 GLN A 246     -27.725  10.232 -25.148  1.00 57.49           N  
+ANISOU 1892  NE2 GLN A 246     7873  10030   3939  -1929   1016   -986       N  
+ATOM   1893  N   GLU A 247     -22.936   6.320 -26.599  1.00 69.61           N  
+ANISOU 1893  N   GLU A 247     9950  10988   5510  -1842   1899  -1827       N  
+ATOM   1894  CA  GLU A 247     -22.659   4.933 -26.244  1.00 70.42           C  
+ANISOU 1894  CA  GLU A 247    10240  10781   5737  -1847   2098  -2110       C  
+ATOM   1895  C   GLU A 247     -21.346   4.807 -25.473  1.00 70.75           C  
+ANISOU 1895  C   GLU A 247    10344  10513   6023  -1595   2202  -2018       C  
+ATOM   1896  O   GLU A 247     -21.260   4.070 -24.489  1.00 75.50           O  
+ANISOU 1896  O   GLU A 247    11082  10763   6841  -1509   2282  -2081       O  
+ATOM   1897  CB  GLU A 247     -22.613   4.069 -27.506  1.00 65.77           C  
+ANISOU 1897  CB  GLU A 247     9707  10379   4905  -2011   2255  -2428       C  
+ATOM   1898  CG  GLU A 247     -22.191   2.632 -27.270  1.00 86.59           C  
+ANISOU 1898  CG  GLU A 247    12555  12673   7672  -2000   2499  -2729       C  
+ATOM   1899  CD  GLU A 247     -22.133   1.825 -28.554  1.00 94.38           C  
+ANISOU 1899  CD  GLU A 247    13586  13836   8438  -2158   2647  -3046       C  
+ATOM   1900  OE1 GLU A 247     -22.359   2.405 -29.637  1.00 84.73           O  
+ANISOU 1900  OE1 GLU A 247    12208  13014   6972  -2255   2534  -2998       O  
+ATOM   1901  OE2 GLU A 247     -21.867   0.607 -28.480  1.00103.32           O  
+ANISOU 1901  OE2 GLU A 247    14876  14663   9717  -2142   2825  -3274       O  
+ATOM   1902  N   LEU A 248     -20.329   5.534 -25.924  1.00 71.01           N  
+ANISOU 1902  N   LEU A 248    10269  10697   6013  -1477   2202  -1861       N  
+ATOM   1903  CA  LEU A 248     -19.041   5.565 -25.239  1.00 63.22           C  
+ANISOU 1903  CA  LEU A 248     9288   9491   5240  -1239   2277  -1758       C  
+ATOM   1904  C   LEU A 248     -19.165   6.213 -23.865  1.00 57.50           C  
+ANISOU 1904  C   LEU A 248     8533   8563   4753  -1114   2132  -1521       C  
+ATOM   1905  O   LEU A 248     -18.526   5.785 -22.904  1.00 56.77           O  
+ANISOU 1905  O   LEU A 248     8506   8192   4872   -939   2192  -1509       O  
+ATOM   1906  CB  LEU A 248     -18.006   6.312 -26.081  1.00 60.91           C  
+ANISOU 1906  CB  LEU A 248     8859   9452   4834  -1182   2303  -1640       C  
+ATOM   1907  CG  LEU A 248     -17.580   5.630 -27.382  1.00 66.82           C  
+ANISOU 1907  CG  LEU A 248     9636  10392   5359  -1261   2483  -1880       C  
+ATOM   1908  CD1 LEU A 248     -16.561   6.478 -28.127  1.00 66.71           C  
+ANISOU 1908  CD1 LEU A 248     9474  10635   5238  -1206   2507  -1726       C  
+ATOM   1909  CD2 LEU A 248     -17.020   4.248 -27.092  1.00 65.12           C  
+ANISOU 1909  CD2 LEU A 248     9584   9882   5277  -1157   2699  -2143       C  
+ATOM   1910  N   PHE A 249     -19.989   7.253 -23.787  1.00 56.22           N  
+ANISOU 1910  N   PHE A 249     8265   8553   4542  -1196   1942  -1332       N  
+ATOM   1911  CA  PHE A 249     -20.262   7.931 -22.526  1.00 54.78           C  
+ANISOU 1911  CA  PHE A 249     8051   8200   4562  -1104   1800  -1127       C  
+ATOM   1912  C   PHE A 249     -20.910   6.971 -21.527  1.00 65.24           C  
+ANISOU 1912  C   PHE A 249     9525   9234   6029  -1106   1835  -1256       C  
+ATOM   1913  O   PHE A 249     -20.496   6.884 -20.365  1.00 52.36           O  
+ANISOU 1913  O   PHE A 249     7938   7352   4605   -950   1834  -1178       O  
+ATOM   1914  CB  PHE A 249     -21.156   9.148 -22.776  1.00 58.72           C  
+ANISOU 1914  CB  PHE A 249     8422   8925   4964  -1197   1612   -929       C  
+ATOM   1915  CG  PHE A 249     -21.517   9.913 -21.535  1.00 57.28           C  
+ANISOU 1915  CG  PHE A 249     8204   8581   4979  -1114   1472   -734       C  
+ATOM   1916  CD1 PHE A 249     -20.553  10.621 -20.837  1.00 66.25           C  
+ANISOU 1916  CD1 PHE A 249     9284   9602   6285   -959   1448   -562       C  
+ATOM   1917  CD2 PHE A 249     -22.826   9.953 -21.086  1.00 59.64           C  
+ANISOU 1917  CD2 PHE A 249     8511   8866   5285  -1202   1368   -736       C  
+ATOM   1918  CE1 PHE A 249     -20.884  11.336 -19.701  1.00 50.19           C  
+ANISOU 1918  CE1 PHE A 249     7220   7429   4421   -893   1326   -407       C  
+ATOM   1919  CE2 PHE A 249     -23.164  10.667 -19.952  1.00 59.57           C  
+ANISOU 1919  CE2 PHE A 249     8468   8717   5449  -1123   1251   -570       C  
+ATOM   1920  CZ  PHE A 249     -22.191  11.359 -19.259  1.00 49.61           C  
+ANISOU 1920  CZ  PHE A 249     7167   7330   4353   -969   1231   -410       C  
+ATOM   1921  N   ILE A 250     -21.924   6.248 -21.995  1.00 61.69           N  
+ANISOU 1921  N   ILE A 250     9150   8834   5455  -1295   1872  -1457       N  
+ATOM   1922  CA  ILE A 250     -22.608   5.241 -21.189  1.00 59.29           C  
+ANISOU 1922  CA  ILE A 250     9004   8258   5266  -1343   1939  -1606       C  
+ATOM   1923  C   ILE A 250     -21.651   4.137 -20.741  1.00 61.94           C  
+ANISOU 1923  C   ILE A 250     9508   8277   5749  -1189   2137  -1726       C  
+ATOM   1924  O   ILE A 250     -21.705   3.692 -19.598  1.00 58.12           O  
+ANISOU 1924  O   ILE A 250     9135   7501   5448  -1091   2165  -1694       O  
+ATOM   1925  CB  ILE A 250     -23.791   4.612 -21.959  1.00 56.68           C  
+ANISOU 1925  CB  ILE A 250     8708   8073   4753  -1611   1968  -1844       C  
+ATOM   1926  CG1 ILE A 250     -24.897   5.646 -22.173  1.00 55.95           C  
+ANISOU 1926  CG1 ILE A 250     8445   8275   4538  -1733   1757  -1706       C  
+ATOM   1927  CG2 ILE A 250     -24.357   3.420 -21.205  1.00 57.32           C  
+ANISOU 1927  CG2 ILE A 250     8979   7836   4962  -1682   2093  -2030       C  
+ATOM   1928  CD1 ILE A 250     -26.044   5.144 -23.023  1.00 58.10           C  
+ANISOU 1928  CD1 ILE A 250     8698   8780   4595  -2001   1758  -1935       C  
+ATOM   1929  N   SER A 251     -20.777   3.700 -21.644  1.00 61.02           N  
+ANISOU 1929  N   SER A 251     9410   8228   5546  -1154   2279  -1857       N  
+ATOM   1930  CA  SER A 251     -19.800   2.661 -21.324  1.00 65.47           C  
+ANISOU 1930  CA  SER A 251    10122   8509   6246   -974   2480  -1968       C  
+ATOM   1931  C   SER A 251     -18.835   3.123 -20.232  1.00 69.43           C  
+ANISOU 1931  C   SER A 251    10570   8866   6946   -698   2424  -1735       C  
+ATOM   1932  O   SER A 251     -18.564   2.394 -19.269  1.00 71.22           O  
+ANISOU 1932  O   SER A 251    10931   8786   7343   -541   2506  -1735       O  
+ATOM   1933  CB  SER A 251     -19.022   2.257 -22.578  1.00 67.46           C  
+ANISOU 1933  CB  SER A 251    10369   8911   6352   -982   2636  -2147       C  
+ATOM   1934  OG  SER A 251     -18.064   1.256 -22.284  1.00 92.06           O  
+ANISOU 1934  OG  SER A 251    13621  11751   9607   -779   2840  -2253       O  
+ATOM   1935  N   ASP A 252     -18.325   4.341 -20.389  1.00 62.67           N  
+ANISOU 1935  N   ASP A 252     9516   8238   6058   -647   2288  -1534       N  
+ATOM   1936  CA  ASP A 252     -17.419   4.934 -19.412  1.00 63.41           C  
+ANISOU 1936  CA  ASP A 252     9520   8256   6319   -424   2215  -1325       C  
+ATOM   1937  C   ASP A 252     -18.099   5.052 -18.056  1.00 68.17           C  
+ANISOU 1937  C   ASP A 252    10177   8659   7066   -389   2104  -1209       C  
+ATOM   1938  O   ASP A 252     -17.487   4.789 -17.021  1.00 75.74           O  
+ANISOU 1938  O   ASP A 252    11172   9426   8178   -186   2120  -1134       O  
+ATOM   1939  CB  ASP A 252     -16.928   6.304 -19.879  1.00 68.21           C  
+ANISOU 1939  CB  ASP A 252     9912   9145   6862   -438   2093  -1144       C  
+ATOM   1940  CG  ASP A 252     -15.766   6.207 -20.846  1.00 83.76           C  
+ANISOU 1940  CG  ASP A 252    11805  11272   8748   -377   2223  -1209       C  
+ATOM   1941  OD1 ASP A 252     -15.436   5.080 -21.271  1.00 89.33           O  
+ANISOU 1941  OD1 ASP A 252    12625  11888   9428   -333   2405  -1415       O  
+ATOM   1942  OD2 ASP A 252     -15.175   7.257 -21.173  1.00 91.70           O  
+ANISOU 1942  OD2 ASP A 252    12640  12480   9721   -375   2157  -1058       O  
+ATOM   1943  N   LEU A 253     -19.366   5.455 -18.069  1.00 69.84           N  
+ANISOU 1943  N   LEU A 253    10382   8940   7214   -581   1992  -1191       N  
+ATOM   1944  CA  LEU A 253     -20.134   5.564 -16.836  1.00 72.69           C  
+ANISOU 1944  CA  LEU A 253    10792   9133   7694   -573   1898  -1098       C  
+ATOM   1945  C   LEU A 253     -20.314   4.183 -16.210  1.00 68.97           C  
+ANISOU 1945  C   LEU A 253    10543   8348   7313   -528   2054  -1235       C  
+ATOM   1946  O   LEU A 253     -20.316   4.037 -14.988  1.00 69.86           O  
+ANISOU 1946  O   LEU A 253    10722   8260   7561   -404   2032  -1136       O  
+ATOM   1947  CB  LEU A 253     -21.498   6.202 -17.108  1.00 72.06           C  
+ANISOU 1947  CB  LEU A 253    10647   9218   7515   -789   1765  -1077       C  
+ATOM   1948  CG  LEU A 253     -21.541   7.725 -17.249  1.00 70.48           C  
+ANISOU 1948  CG  LEU A 253    10251   9244   7284   -797   1583   -867       C  
+ATOM   1949  CD1 LEU A 253     -22.969   8.238 -17.146  1.00 62.80           C  
+ANISOU 1949  CD1 LEU A 253     9231   8367   6262   -950   1454   -828       C  
+ATOM   1950  CD2 LEU A 253     -20.658   8.386 -16.215  1.00 64.27           C  
+ANISOU 1950  CD2 LEU A 253     9402   8355   6661   -602   1519   -690       C  
+ATOM   1951  N   SER A 254     -20.462   3.175 -17.064  1.00 55.77           N  
+ANISOU 1951  N   SER A 254     8994   6635   5559   -633   2221  -1462       N  
+ATOM   1952  CA  SER A 254     -20.638   1.796 -16.627  1.00 58.96           C  
+ANISOU 1952  CA  SER A 254     9639   6712   6051   -612   2409  -1613       C  
+ATOM   1953  C   SER A 254     -19.377   1.268 -15.959  1.00 64.48           C  
+ANISOU 1953  C   SER A 254    10413   7192   6894   -301   2513  -1543       C  
+ATOM   1954  O   SER A 254     -19.444   0.434 -15.055  1.00 61.55           O  
+ANISOU 1954  O   SER A 254    10223   6516   6646   -195   2612  -1535       O  
+ATOM   1955  CB  SER A 254     -21.019   0.902 -17.810  1.00 59.36           C  
+ANISOU 1955  CB  SER A 254     9795   6783   5975   -814   2575  -1902       C  
+ATOM   1956  OG  SER A 254     -21.197  -0.442 -17.398  1.00 75.96           O  
+ANISOU 1956  OG  SER A 254    12152   8530   8180   -808   2783  -2056       O  
+ATOM   1957  N   ARG A 255     -18.226   1.750 -16.418  1.00 81.40           N  
+ANISOU 1957  N   ARG A 255    12410   9503   9017   -152   2497  -1485       N  
+ATOM   1958  CA  ARG A 255     -16.945   1.335 -15.854  1.00 82.69           C  
+ANISOU 1958  CA  ARG A 255    12592   9526   9302    163   2580  -1415       C  
+ATOM   1959  C   ARG A 255     -16.816   1.731 -14.382  1.00 75.84           C  
+ANISOU 1959  C   ARG A 255    11696   8557   8562    336   2451  -1191       C  
+ATOM   1960  O   ARG A 255     -16.050   1.125 -13.633  1.00 75.43           O  
+ANISOU 1960  O   ARG A 255    11717   8326   8618    599   2526  -1130       O  
+ATOM   1961  CB  ARG A 255     -15.789   1.932 -16.660  1.00 79.65           C  
+ANISOU 1961  CB  ARG A 255    12007   9400   8856    254   2572  -1396       C  
+ATOM   1962  N   PHE A 256     -17.571   2.747 -13.974  1.00 69.41           N  
+ANISOU 1962  N   PHE A 256    10775   7870   7727    199   2259  -1071       N  
+ATOM   1963  CA  PHE A 256     -17.539   3.218 -12.594  1.00 70.61           C  
+ANISOU 1963  CA  PHE A 256    10892   7958   7978    331   2128   -878       C  
+ATOM   1964  C   PHE A 256     -18.770   2.749 -11.822  1.00 70.93           C  
+ANISOU 1964  C   PHE A 256    11106   7795   8051    219   2138   -885       C  
+ATOM   1965  O   PHE A 256     -19.116   3.319 -10.785  1.00 59.03           O  
+ANISOU 1965  O   PHE A 256     9559   6282   6589    245   2008   -742       O  
+ATOM   1966  CB  PHE A 256     -17.457   4.743 -12.559  1.00 63.77           C  
+ANISOU 1966  CB  PHE A 256     9787   7358   7087    273   1920   -737       C  
+ATOM   1967  CG  PHE A 256     -16.241   5.302 -13.239  1.00 62.04           C  
+ANISOU 1967  CG  PHE A 256     9384   7346   6843    361   1913   -713       C  
+ATOM   1968  CD1 PHE A 256     -14.983   4.778 -12.990  1.00 67.64           C  
+ANISOU 1968  CD1 PHE A 256    10075   8012   7615    614   1999   -706       C  
+ATOM   1969  CD2 PHE A 256     -16.358   6.355 -14.131  1.00 54.90           C  
+ANISOU 1969  CD2 PHE A 256     8321   6689   5850    196   1827   -688       C  
+ATOM   1970  CE1 PHE A 256     -13.865   5.296 -13.618  1.00 74.90           C  
+ANISOU 1970  CE1 PHE A 256    10805   9143   8511    680   2002   -694       C  
+ATOM   1971  CE2 PHE A 256     -15.245   6.877 -14.761  1.00 69.42           C  
+ANISOU 1971  CE2 PHE A 256     9995   8719   7664    255   1838   -662       C  
+ATOM   1972  CZ  PHE A 256     -13.997   6.347 -14.504  1.00 67.47           C  
+ANISOU 1972  CZ  PHE A 256     9715   8438   7482    487   1927   -674       C  
+ATOM   1973  N   ASN A 257     -19.422   1.712 -12.343  1.00 69.12           N  
+ANISOU 1973  N   ASN A 257    11065   7405   7794     80   2303  -1065       N  
+ATOM   1974  CA  ASN A 257     -20.649   1.164 -11.767  1.00 58.77           C  
+ANISOU 1974  CA  ASN A 257     9921   5901   6506    -75   2348  -1107       C  
+ATOM   1975  C   ASN A 257     -21.749   2.219 -11.647  1.00 68.14           C  
+ANISOU 1975  C   ASN A 257    10966   7289   7637   -286   2160  -1049       C  
+ATOM   1976  O   ASN A 257     -22.530   2.215 -10.695  1.00 76.88           O  
+ANISOU 1976  O   ASN A 257    12132   8291   8788   -330   2125   -982       O  
+ATOM   1977  CB  ASN A 257     -20.374   0.528 -10.400  1.00 63.55           C  
+ANISOU 1977  CB  ASN A 257    10686   6227   7232    146   2410   -977       C  
+ATOM   1978  CG  ASN A 257     -21.465  -0.441  -9.977  1.00 79.80           C  
+ANISOU 1978  CG  ASN A 257    12985   8013   9324     -7   2552  -1059       C  
+ATOM   1979  OD1 ASN A 257     -22.150  -1.028 -10.816  1.00 79.95           O  
+ANISOU 1979  OD1 ASN A 257    13097   7983   9296   -241   2674  -1268       O  
+ATOM   1980  ND2 ASN A 257     -21.633  -0.610  -8.671  1.00 84.12           N  
+ANISOU 1980  ND2 ASN A 257    13630   8392   9941    110   2543   -903       N  
+ATOM   1981  N   ILE A 258     -21.800   3.127 -12.616  1.00 55.25           N  
+ANISOU 1981  N   ILE A 258     9144   5946   5901   -403   2049  -1065       N  
+ATOM   1982  CA  ILE A 258     -22.900   4.079 -12.705  1.00 51.35           C  
+ANISOU 1982  CA  ILE A 258     8517   5652   5343   -597   1888  -1023       C  
+ATOM   1983  C   ILE A 258     -23.817   3.681 -13.856  1.00 57.79           C  
+ANISOU 1983  C   ILE A 258     9350   6584   6025   -864   1946  -1225       C  
+ATOM   1984  O   ILE A 258     -23.474   3.855 -15.025  1.00 55.49           O  
+ANISOU 1984  O   ILE A 258     8979   6485   5619   -918   1954  -1301       O  
+ATOM   1985  CB  ILE A 258     -22.401   5.521 -12.912  1.00 50.87           C  
+ANISOU 1985  CB  ILE A 258     8225   5843   5258   -535   1707   -862       C  
+ATOM   1986  CG1 ILE A 258     -21.465   5.933 -11.774  1.00 64.48           C  
+ANISOU 1986  CG1 ILE A 258     9912   7483   7105   -296   1646   -692       C  
+ATOM   1987  CG2 ILE A 258     -23.576   6.481 -13.014  1.00 47.85           C  
+ANISOU 1987  CG2 ILE A 258     7718   5645   4819   -707   1554   -808       C  
+ATOM   1988  CD1 ILE A 258     -20.918   7.338 -11.911  1.00 65.74           C  
+ANISOU 1988  CD1 ILE A 258     9858   7856   7263   -253   1491   -550       C  
+ATOM   1989  N   LYS A 259     -24.986   3.149 -13.518  1.00 52.81           N  
+ANISOU 1989  N   LYS A 259     8814   5856   5397  -1041   1989  -1318       N  
+ATOM   1990  CA  LYS A 259     -25.926   2.681 -14.526  1.00 63.82           C  
+ANISOU 1990  CA  LYS A 259    10217   7371   6659  -1318   2047  -1539       C  
+ATOM   1991  C   LYS A 259     -26.623   3.861 -15.191  1.00 71.38           C  
+ANISOU 1991  C   LYS A 259    10938   8699   7482  -1445   1850  -1480       C  
+ATOM   1992  O   LYS A 259     -27.151   4.749 -14.517  1.00 62.23           O  
+ANISOU 1992  O   LYS A 259     9666   7614   6364  -1421   1699  -1319       O  
+ATOM   1993  CB  LYS A 259     -26.950   1.728 -13.907  1.00 55.23           C  
+ANISOU 1993  CB  LYS A 259     9295   6064   5626  -1484   2167  -1662       C  
+ATOM   1994  CG  LYS A 259     -27.987   1.204 -14.887  1.00 59.56           C  
+ANISOU 1994  CG  LYS A 259     9839   6752   6038  -1806   2230  -1922       C  
+ATOM   1995  CD  LYS A 259     -29.020   0.342 -14.184  1.00 58.97           C  
+ANISOU 1995  CD  LYS A 259     9912   6461   6032  -1991   2353  -2034       C  
+ATOM   1996  CE  LYS A 259     -29.771  -0.536 -15.171  1.00 62.51           C  
+ANISOU 1996  CE  LYS A 259    10415   6969   6367  -2313   2487  -2356       C  
+ATOM   1997  NZ  LYS A 259     -30.782  -1.397 -14.496  1.00 78.53           N  
+ANISOU 1997  NZ  LYS A 259    12589   8778   8472  -2527   2629  -2479       N  
+ATOM   1998  N   THR A 260     -26.616   3.866 -16.519  1.00 74.19           N  
+ANISOU 1998  N   THR A 260    11226   9292   7673  -1568   1859  -1608       N  
+ATOM   1999  CA  THR A 260     -27.237   4.939 -17.280  1.00 72.46           C  
+ANISOU 1999  CA  THR A 260    10789   9445   7299  -1670   1680  -1538       C  
+ATOM   2000  C   THR A 260     -28.622   4.543 -17.772  1.00 64.19           C  
+ANISOU 2000  C   THR A 260     9705   8564   6119  -1951   1676  -1727       C  
+ATOM   2001  O   THR A 260     -28.802   3.505 -18.408  1.00 68.57           O  
+ANISOU 2001  O   THR A 260    10365   9097   6593  -2122   1823  -1984       O  
+ATOM   2002  CB  THR A 260     -26.375   5.351 -18.487  1.00 74.18           C  
+ANISOU 2002  CB  THR A 260    10920   9887   7377  -1626   1671  -1527       C  
+ATOM   2003  OG1 THR A 260     -25.074   5.744 -18.035  1.00 76.26           O  
+ANISOU 2003  OG1 THR A 260    11189  10020   7765  -1380   1676  -1362       O  
+ATOM   2004  CG2 THR A 260     -27.022   6.509 -19.229  1.00 80.43           C  
+ANISOU 2004  CG2 THR A 260    11499  11054   8005  -1704   1485  -1409       C  
+ATOM   2005  N   ILE A 261     -29.597   5.388 -17.463  1.00 56.03           N  
+ANISOU 2005  N   ILE A 261     8514   7707   5068  -1997   1510  -1607       N  
+ATOM   2006  CA  ILE A 261     -30.955   5.219 -17.940  1.00 64.47           C  
+ANISOU 2006  CA  ILE A 261     9483   9016   5996  -2251   1467  -1758       C  
+ATOM   2007  C   ILE A 261     -31.239   6.244 -19.032  1.00 63.81           C  
+ANISOU 2007  C   ILE A 261     9175   9362   5708  -2270   1294  -1666       C  
+ATOM   2008  O   ILE A 261     -31.054   7.460 -18.850  1.00 73.53           O  
+ANISOU 2008  O   ILE A 261    10281  10688   6970  -2100   1144  -1405       O  
+ATOM   2009  CB  ILE A 261     -31.957   5.361 -16.791  1.00 62.40           C  
+ANISOU 2009  CB  ILE A 261     9192   8662   5855  -2286   1418  -1699       C  
+ATOM   2010  CG1 ILE A 261     -31.627   4.340 -15.702  1.00 61.52           C  
+ANISOU 2010  CG1 ILE A 261     9322   8122   5931  -2253   1599  -1759       C  
+ATOM   2011  CG2 ILE A 261     -33.383   5.203 -17.297  1.00 54.32           C  
+ANISOU 2011  CG2 ILE A 261     8028   7928   4682  -2554   1368  -1864       C  
+ATOM   2012  CD1 ILE A 261     -31.945   4.817 -14.322  1.00 71.93           C  
+ANISOU 2012  CD1 ILE A 261    10633   9290   7408  -2138   1538  -1579       C  
+ATOM   2013  N   VAL A 262     -31.667   5.728 -20.178  1.00 71.90           N  
+ANISOU 2013  N   VAL A 262    10159  10642   6516  -2479   1326  -1886       N  
+ATOM   2014  CA  VAL A 262     -31.866   6.534 -21.370  1.00 73.27           C  
+ANISOU 2014  CA  VAL A 262    10140  11251   6449  -2503   1183  -1815       C  
+ATOM   2015  C   VAL A 262     -33.346   6.799 -21.618  1.00 72.20           C  
+ANISOU 2015  C   VAL A 262     9806  11456   6170  -2674   1046  -1862       C  
+ATOM   2016  O   VAL A 262     -34.118   5.884 -21.903  1.00 64.36           O  
+ANISOU 2016  O   VAL A 262     8821  10551   5083  -2929   1117  -2144       O  
+ATOM   2017  CB  VAL A 262     -31.249   5.856 -22.601  1.00 64.44           C  
+ANISOU 2017  CB  VAL A 262     9087  10258   5140  -2605   1300  -2024       C  
+ATOM   2018  CG1 VAL A 262     -31.322   6.776 -23.795  1.00 61.89           C  
+ANISOU 2018  CG1 VAL A 262     8573  10387   4556  -2595   1151  -1902       C  
+ATOM   2019  CG2 VAL A 262     -29.806   5.469 -22.317  1.00 58.43           C  
+ANISOU 2019  CG2 VAL A 262     8512   9155   4532  -2431   1455  -2005       C  
+ATOM   2020  N   LEU A 263     -33.727   8.064 -21.504  1.00 69.20           N  
+ANISOU 2020  N   LEU A 263     9245  11267   5780  -2532    856  -1589       N  
+ATOM   2021  CA  LEU A 263     -35.114   8.479 -21.637  1.00 65.29           C  
+ANISOU 2021  CA  LEU A 263     8531  11106   5168  -2632    706  -1582       C  
+ATOM   2022  C   LEU A 263     -35.401   8.991 -23.044  1.00 60.75           C  
+ANISOU 2022  C   LEU A 263     7772  11028   4282  -2673    578  -1549       C  
+ATOM   2023  O   LEU A 263     -34.481   9.295 -23.803  1.00 65.47           O  
+ANISOU 2023  O   LEU A 263     8408  11689   4779  -2581    589  -1458       O  
+ATOM   2024  CB  LEU A 263     -35.433   9.556 -20.600  1.00 61.37           C  
+ANISOU 2024  CB  LEU A 263     7949  10508   4860  -2428    585  -1301       C  
+ATOM   2025  CG  LEU A 263     -35.051   9.175 -19.167  1.00 63.63           C  
+ANISOU 2025  CG  LEU A 263     8415  10326   5435  -2356    699  -1295       C  
+ATOM   2026  CD1 LEU A 263     -35.242  10.348 -18.218  1.00 53.20           C  
+ANISOU 2026  CD1 LEU A 263     7010   8924   4281  -2144    579  -1021       C  
+ATOM   2027  CD2 LEU A 263     -35.853   7.966 -18.705  1.00 55.38           C  
+ANISOU 2027  CD2 LEU A 263     7439   9181   4424  -2598    821  -1574       C  
+ATOM   2028  N   ASN A 264     -36.682   9.088 -23.385  1.00 66.32           N  
+ANISOU 2028  N   ASN A 264     8267  12106   4824  -2808    458  -1618       N  
+ATOM   2029  CA  ASN A 264     -37.090   9.568 -24.699  1.00 68.07           C  
+ANISOU 2029  CA  ASN A 264     8290  12855   4719  -2841    317  -1578       C  
+ATOM   2030  C   ASN A 264     -37.011  11.086 -24.776  1.00 72.98           C  
+ANISOU 2030  C   ASN A 264     8782  13608   5340  -2553    144  -1167       C  
+ATOM   2031  O   ASN A 264     -36.791  11.658 -25.844  1.00 85.12           O  
+ANISOU 2031  O   ASN A 264    10235  15464   6644  -2487     60  -1030       O  
+ATOM   2032  CB  ASN A 264     -38.508   9.096 -25.021  1.00 67.87           C  
+ANISOU 2032  CB  ASN A 264     8062  13215   4510  -3090    245  -1811       C  
+ATOM   2033  CG  ASN A 264     -38.677   7.602 -24.844  1.00 69.02           C  
+ANISOU 2033  CG  ASN A 264     8349  13186   4691  -3401    437  -2226       C  
+ATOM   2034  OD1 ASN A 264     -38.195   6.811 -25.654  1.00 90.38           O  
+ANISOU 2034  OD1 ASN A 264    11159  15935   7246  -3562    552  -2466       O  
+ATOM   2035  ND2 ASN A 264     -39.361   7.206 -23.777  1.00 75.09           N  
+ANISOU 2035  ND2 ASN A 264     9130  13741   5661  -3491    490  -2316       N  
+ATOM   2036  N   ASN A 265     -37.188  11.730 -23.628  1.00 63.80           N  
+ANISOU 2036  N   ASN A 265     7616  12187   4438  -2383    105   -974       N  
+ATOM   2037  CA  ASN A 265     -37.120  13.181 -23.526  1.00 62.94           C  
+ANISOU 2037  CA  ASN A 265     7412  12116   4385  -2105    -31   -593       C  
+ATOM   2038  C   ASN A 265     -36.830  13.600 -22.092  1.00 63.14           C  
+ANISOU 2038  C   ASN A 265     7541  11693   4758  -1944      8   -459       C  
+ATOM   2039  O   ASN A 265     -37.028  12.824 -21.157  1.00 67.35           O  
+ANISOU 2039  O   ASN A 265     8162  11974   5454  -2049    103   -644       O  
+ATOM   2040  CB  ASN A 265     -38.417  13.822 -24.021  1.00 75.85           C  
+ANISOU 2040  CB  ASN A 265     8768  14221   5829  -2078   -220   -490       C  
+ATOM   2041  CG  ASN A 265     -39.645  13.249 -23.345  1.00 92.41           C  
+ANISOU 2041  CG  ASN A 265    10746  16385   7982  -2234   -235   -699       C  
+ATOM   2042  OD1 ASN A 265     -39.844  12.035 -23.323  1.00103.14           O  
+ANISOU 2042  OD1 ASN A 265    12163  17720   9306  -2500   -125  -1034       O  
+ATOM   2043  ND2 ASN A 265     -40.481  14.122 -22.797  1.00102.47           N  
+ANISOU 2043  ND2 ASN A 265    11851  17739   9346  -2072   -357   -508       N  
+ATOM   2044  N   TYR A 266     -36.351  14.827 -21.923  1.00 65.49           N  
+ANISOU 2044  N   TYR A 266     7834  11890   5160  -1699    -56   -140       N  
+ATOM   2045  CA  TYR A 266     -35.944  15.316 -20.611  1.00 62.48           C  
+ANISOU 2045  CA  TYR A 266     7553  11095   5093  -1545    -18    -15       C  
+ATOM   2046  C   TYR A 266     -37.119  15.446 -19.644  1.00 58.88           C  
+ANISOU 2046  C   TYR A 266     6985  10626   4760  -1534    -74    -38       C  
+ATOM   2047  O   TYR A 266     -36.945  15.325 -18.431  1.00 64.36           O  
+ANISOU 2047  O   TYR A 266     7783  10984   5689  -1499     -5    -67       O  
+ATOM   2048  CB  TYR A 266     -35.213  16.653 -20.755  1.00 57.41           C  
+ANISOU 2048  CB  TYR A 266     6922  10371   4521  -1312    -67    315       C  
+ATOM   2049  CG  TYR A 266     -33.831  16.506 -21.354  1.00 65.51           C  
+ANISOU 2049  CG  TYR A 266     8089  11297   5505  -1316     30    332       C  
+ATOM   2050  CD1 TYR A 266     -32.798  15.928 -20.626  1.00 61.27           C  
+ANISOU 2050  CD1 TYR A 266     7729  10400   5150  -1332    163    221       C  
+ATOM   2051  CD2 TYR A 266     -33.561  16.933 -22.648  1.00 60.33           C  
+ANISOU 2051  CD2 TYR A 266     7380  10929   4616  -1298     -9    463       C  
+ATOM   2052  CE1 TYR A 266     -31.533  15.784 -21.167  1.00 57.09           C  
+ANISOU 2052  CE1 TYR A 266     7305   9801   4586  -1327    256    228       C  
+ATOM   2053  CE2 TYR A 266     -32.296  16.794 -23.198  1.00 61.23           C  
+ANISOU 2053  CE2 TYR A 266     7611  10966   4687  -1309     94    471       C  
+ATOM   2054  CZ  TYR A 266     -31.287  16.219 -22.453  1.00 68.19           C  
+ANISOU 2054  CZ  TYR A 266     8652  11490   5766  -1323    227    346       C  
+ATOM   2055  OH  TYR A 266     -30.028  16.077 -22.994  1.00 61.27           O  
+ANISOU 2055  OH  TYR A 266     7869  10560   4852  -1325    333    347       O  
+ATOM   2056  N   ASN A 267     -38.317  15.665 -20.180  1.00 66.77           N  
+ANISOU 2056  N   ASN A 267     7764  12018   5588  -1565   -196    -31       N  
+ATOM   2057  CA  ASN A 267     -39.503  15.813 -19.343  1.00 68.90           C  
+ANISOU 2057  CA  ASN A 267     7891  12331   5957  -1553   -249    -57       C  
+ATOM   2058  C   ASN A 267     -39.763  14.570 -18.500  1.00 63.04           C  
+ANISOU 2058  C   ASN A 267     7242  11395   5314  -1774   -120   -356       C  
+ATOM   2059  O   ASN A 267     -40.284  14.662 -17.384  1.00 64.54           O  
+ANISOU 2059  O   ASN A 267     7416  11423   5684  -1741   -101   -363       O  
+ATOM   2060  CB  ASN A 267     -40.735  16.102 -20.205  1.00 83.11           C  
+ANISOU 2060  CB  ASN A 267     9409  14653   7515  -1570   -402    -33       C  
+ATOM   2061  CG  ASN A 267     -40.798  17.539 -20.673  1.00 91.66           C  
+ANISOU 2061  CG  ASN A 267    10377  15887   8562  -1285   -538    325       C  
+ATOM   2062  OD1 ASN A 267     -39.895  18.333 -20.409  1.00100.06           O  
+ANISOU 2062  OD1 ASN A 267    11580  16656   9782  -1100   -507    545       O  
+ATOM   2063  ND2 ASN A 267     -41.874  17.886 -21.369  1.00 94.39           N  
+ANISOU 2063  ND2 ASN A 267    10465  16699   8701  -1247   -684    388       N  
+ATOM   2064  N   GLU A 268     -39.355  13.415 -19.019  1.00 62.95           N  
+ANISOU 2064  N   GLU A 268     7347  11380   5191  -1992    -15   -597       N  
+ATOM   2065  CA  GLU A 268     -39.509  12.161 -18.296  1.00 64.06           C  
+ANISOU 2065  CA  GLU A 268     7617  11296   5427  -2208    138   -875       C  
+ATOM   2066  C   GLU A 268     -38.794  12.213 -16.952  1.00 57.14           C  
+ANISOU 2066  C   GLU A 268     6938   9939   4833  -2079    236   -795       C  
+ATOM   2067  O   GLU A 268     -39.285  11.649 -15.970  1.00 57.25           O  
+ANISOU 2067  O   GLU A 268     6999   9783   4972  -2171    319   -914       O  
+ATOM   2068  CB  GLU A 268     -38.993  10.986 -19.130  1.00 57.14           C  
+ANISOU 2068  CB  GLU A 268     6870  10439   4403  -2428    256  -1129       C  
+ATOM   2069  CG  GLU A 268     -39.812  10.727 -20.385  1.00 60.31           C  
+ANISOU 2069  CG  GLU A 268     7072  11341   4500  -2617    173  -1281       C  
+ATOM   2070  CD  GLU A 268     -39.539   9.368 -21.000  1.00 61.91           C  
+ANISOU 2070  CD  GLU A 268     7409  11530   4582  -2896    324  -1618       C  
+ATOM   2071  OE1 GLU A 268     -38.469   8.787 -20.724  1.00 78.58           O  
+ANISOU 2071  OE1 GLU A 268     9775  13264   6819  -2881    481  -1672       O  
+ATOM   2072  OE2 GLU A 268     -40.399   8.877 -21.761  1.00 64.72           O  
+ANISOU 2072  OE2 GLU A 268     7612  12263   4718  -3130    290  -1837       O  
+ATOM   2073  N   ILE A 269     -37.664  12.919 -16.905  1.00 59.04           N  
+ANISOU 2073  N   ILE A 269     7284   9988   5163  -1872    227   -591       N  
+ATOM   2074  CA  ILE A 269     -36.970  13.152 -15.642  1.00 67.65           C  
+ANISOU 2074  CA  ILE A 269     8526  10676   6502  -1727    290   -494       C  
+ATOM   2075  C   ILE A 269     -37.964  13.655 -14.609  1.00 62.63           C  
+ANISOU 2075  C   ILE A 269     7780  10024   5990  -1669    240   -439       C  
+ATOM   2076  O   ILE A 269     -38.145  13.030 -13.558  1.00 66.38           O  
+ANISOU 2076  O   ILE A 269     8352  10280   6590  -1735    338   -548       O  
+ATOM   2077  CB  ILE A 269     -35.817  14.167 -15.777  1.00 60.25           C  
+ANISOU 2077  CB  ILE A 269     7641   9616   5635  -1507    250   -256       C  
+ATOM   2078  CG1 ILE A 269     -34.725  13.628 -16.702  1.00 56.06           C  
+ANISOU 2078  CG1 ILE A 269     7225   9079   4995  -1558    323   -317       C  
+ATOM   2079  CG2 ILE A 269     -35.234  14.493 -14.412  1.00 53.71           C  
+ANISOU 2079  CG2 ILE A 269     6930   8427   5050  -1368    294   -172       C  
+ATOM   2080  CD1 ILE A 269     -33.571  14.588 -16.905  1.00 52.70           C  
+ANISOU 2080  CD1 ILE A 269     6837   8557   4629  -1374    299    -95       C  
+ATOM   2081  N   THR A 270     -38.636  14.757 -14.939  1.00 58.51           N  
+ANISOU 2081  N   THR A 270     7057   9748   5425  -1542     98   -268       N  
+ATOM   2082  CA  THR A 270     -39.633  15.343 -14.051  1.00 68.83           C  
+ANISOU 2082  CA  THR A 270     8232  11078   6843  -1462     48   -211       C  
+ATOM   2083  C   THR A 270     -40.624  14.282 -13.619  1.00 65.26           C  
+ANISOU 2083  C   THR A 270     7736  10696   6363  -1691    120   -455       C  
+ATOM   2084  O   THR A 270     -40.871  14.103 -12.420  1.00 61.79           O  
+ANISOU 2084  O   THR A 270     7355  10046   6077  -1694    194   -497       O  
+ATOM   2085  CB  THR A 270     -40.393  16.497 -14.726  1.00 63.20           C  
+ANISOU 2085  CB  THR A 270     7281  10693   6041  -1309   -112    -20       C  
+ATOM   2086  OG1 THR A 270     -39.459  17.461 -15.227  1.00 61.59           O  
+ANISOU 2086  OG1 THR A 270     7133  10414   5853  -1119   -160    214       O  
+ATOM   2087  CG2 THR A 270     -41.332  17.170 -13.734  1.00 64.13           C  
+ANISOU 2087  CG2 THR A 270     7268  10796   6301  -1189   -148     44       C  
+ATOM   2088  N   GLU A 271     -41.121  13.530 -14.598  1.00 60.54           N  
+ANISOU 2088  N   GLU A 271     7052  10387   5564  -1902    115   -629       N  
+ATOM   2089  CA  GLU A 271     -42.142  12.531 -14.340  1.00 64.07           C  
+ANISOU 2089  CA  GLU A 271     7432  10944   5968  -2161    188   -880       C  
+ATOM   2090  C   GLU A 271     -41.606  11.559 -13.310  1.00 64.39           C  
+ANISOU 2090  C   GLU A 271     7735  10564   6166  -2261    376  -1007       C  
+ATOM   2091  O   GLU A 271     -42.241  11.319 -12.276  1.00 66.94           O  
+ANISOU 2091  O   GLU A 271     8053  10781   6599  -2317    444  -1064       O  
+ATOM   2092  CB  GLU A 271     -42.523  11.801 -15.633  1.00 70.82           C  
+ANISOU 2092  CB  GLU A 271     8188  12147   6572  -2397    171  -1078       C  
+ATOM   2093  CG  GLU A 271     -43.650  10.794 -15.490  1.00 81.79           C  
+ANISOU 2093  CG  GLU A 271     9480  13696   7902  -2706    246  -1363       C  
+ATOM   2094  CD  GLU A 271     -43.980  10.104 -16.804  1.00 95.46           C  
+ANISOU 2094  CD  GLU A 271    11110  15790   9373  -2955    226  -1585       C  
+ATOM   2095  OE1 GLU A 271     -43.428  10.513 -17.848  1.00 90.24           O  
+ANISOU 2095  OE1 GLU A 271    10428  15303   8557  -2861    133  -1490       O  
+ATOM   2096  OE2 GLU A 271     -44.785   9.149 -16.792  1.00 99.37           O  
+ANISOU 2096  OE2 GLU A 271    11547  16398   9810  -3259    312  -1863       O  
+ATOM   2097  N   ILE A 272     -40.386  11.088 -13.557  1.00 57.78           N  
+ANISOU 2097  N   ILE A 272     7124   9487   5342  -2250    458  -1021       N  
+ATOM   2098  CA  ILE A 272     -39.743  10.143 -12.660  1.00 56.18           C  
+ANISOU 2098  CA  ILE A 272     7186   8882   5277  -2307    637  -1113       C  
+ATOM   2099  C   ILE A 272     -39.696  10.732 -11.263  1.00 55.82           C  
+ANISOU 2099  C   ILE A 272     7183   8602   5424  -2130    639   -963       C  
+ATOM   2100  O   ILE A 272     -40.162  10.107 -10.300  1.00 55.79           O  
+ANISOU 2100  O   ILE A 272     7252   8444   5503  -2232    751  -1054       O  
+ATOM   2101  CB  ILE A 272     -38.316   9.795 -13.129  1.00 54.93           C  
+ANISOU 2101  CB  ILE A 272     7235   8519   5117  -2240    701  -1099       C  
+ATOM   2102  CG1 ILE A 272     -38.367   8.968 -14.416  1.00 64.87           C  
+ANISOU 2102  CG1 ILE A 272     8491   9972   6184  -2454    744  -1307       C  
+ATOM   2103  CG2 ILE A 272     -37.559   9.049 -12.041  1.00 54.95           C  
+ANISOU 2103  CG2 ILE A 272     7500   8096   5285  -2207    861  -1123       C  
+ATOM   2104  CD1 ILE A 272     -37.063   8.948 -15.181  1.00 71.75           C  
+ANISOU 2104  CD1 ILE A 272     9486  10769   7009  -2357    765  -1265       C  
+ATOM   2105  N   LEU A 273     -39.217  11.970 -11.173  1.00 55.60           N  
+ANISOU 2105  N   LEU A 273     7099   8569   5458  -1879    520   -737       N  
+ATOM   2106  CA  LEU A 273     -39.084  12.622  -9.882  1.00 65.90           C  
+ANISOU 2106  CA  LEU A 273     8443   9659   6937  -1706    518   -606       C  
+ATOM   2107  C   LEU A 273     -40.440  12.677  -9.208  1.00 71.46           C  
+ANISOU 2107  C   LEU A 273     8997  10490   7663  -1780    519   -665       C  
+ATOM   2108  O   LEU A 273     -40.571  12.303  -8.036  1.00 55.94           O  
+ANISOU 2108  O   LEU A 273     7133   8322   5802  -1802    619   -703       O  
+ATOM   2109  CB  LEU A 273     -38.492  14.024 -10.031  1.00 67.83           C  
+ANISOU 2109  CB  LEU A 273     8626   9910   7238  -1456    392   -376       C  
+ATOM   2110  CG  LEU A 273     -37.029  14.070 -10.475  1.00 59.27           C  
+ANISOU 2110  CG  LEU A 273     7690   8667   6162  -1368    406   -303       C  
+ATOM   2111  CD1 LEU A 273     -36.533  15.503 -10.566  1.00 57.86           C  
+ANISOU 2111  CD1 LEU A 273     7446   8483   6054  -1150    299    -81       C  
+ATOM   2112  CD2 LEU A 273     -36.166  13.260  -9.521  1.00 51.71           C  
+ANISOU 2112  CD2 LEU A 273     6958   7382   5308  -1370    535   -366       C  
+ATOM   2113  N   GLN A 274     -41.454  13.074  -9.976  1.00 69.76           N  
+ANISOU 2113  N   GLN A 274     8535  10634   7335  -1825    415   -677       N  
+ATOM   2114  CA  GLN A 274     -42.800  13.179  -9.437  1.00 68.64           C  
+ANISOU 2114  CA  GLN A 274     8203  10671   7205  -1889    408   -737       C  
+ATOM   2115  C   GLN A 274     -43.184  11.852  -8.815  1.00 70.44           C  
+ANISOU 2115  C   GLN A 274     8546  10772   7444  -2149    582   -952       C  
+ATOM   2116  O   GLN A 274     -43.585  11.794  -7.646  1.00 63.36           O  
+ANISOU 2116  O   GLN A 274     7678   9741   6653  -2148    660   -960       O  
+ATOM   2117  CB  GLN A 274     -43.799  13.580 -10.525  1.00 69.42           C  
+ANISOU 2117  CB  GLN A 274     8008  11225   7144  -1925    273   -747       C  
+ATOM   2118  CG  GLN A 274     -43.934  15.082 -10.714  1.00 77.48           C  
+ANISOU 2118  CG  GLN A 274     8862  12381   8197  -1634    115   -505       C  
+ATOM   2119  CD  GLN A 274     -44.551  15.460 -12.045  1.00 83.09           C  
+ANISOU 2119  CD  GLN A 274     9328  13531   8712  -1626    -32   -465       C  
+ATOM   2120  OE1 GLN A 274     -44.893  14.597 -12.854  1.00 82.78           O  
+ANISOU 2120  OE1 GLN A 274     9227  13728   8498  -1858    -25   -642       O  
+ATOM   2121  NE2 GLN A 274     -44.699  16.759 -12.279  1.00 83.72           N  
+ANISOU 2121  NE2 GLN A 274     9271  13725   8816  -1357   -160   -231       N  
+ATOM   2122  N   ARG A 275     -42.977  10.781  -9.578  1.00 65.37           N  
+ANISOU 2122  N   ARG A 275     7998  10144   6697  -2367    659  -1121       N  
+ATOM   2123  CA  ARG A 275     -43.352   9.454  -9.123  1.00 60.71           C  
+ANISOU 2123  CA  ARG A 275     7535   9415   6116  -2641    846  -1335       C  
+ATOM   2124  C   ARG A 275     -42.649   9.147  -7.816  1.00 59.71           C  
+ANISOU 2124  C   ARG A 275     7672   8868   6149  -2549    978  -1264       C  
+ATOM   2125  O   ARG A 275     -43.282   8.697  -6.856  1.00 71.77           O  
+ANISOU 2125  O   ARG A 275     9230  10302   7736  -2658   1096  -1327       O  
+ATOM   2126  CB  ARG A 275     -43.026   8.400 -10.181  1.00 59.57           C  
+ANISOU 2126  CB  ARG A 275     7492   9291   5850  -2863    922  -1527       C  
+ATOM   2127  CG  ARG A 275     -43.907   8.504 -11.413  1.00 68.85           C  
+ANISOU 2127  CG  ARG A 275     8393  10933   6832  -3017    808  -1648       C  
+ATOM   2128  CD  ARG A 275     -44.238   7.138 -11.978  1.00 79.58           C  
+ANISOU 2128  CD  ARG A 275     9821  12325   8093  -3378    954  -1953       C  
+ATOM   2129  NE  ARG A 275     -44.388   6.136 -10.929  1.00 71.81           N  
+ANISOU 2129  NE  ARG A 275     9041  11004   7240  -3548   1176  -2069       N  
+ATOM   2130  CZ  ARG A 275     -44.294   4.828 -11.135  1.00 60.72           C  
+ANISOU 2130  CZ  ARG A 275     7829   9420   5822  -3822   1371  -2303       C  
+ATOM   2131  NH1 ARG A 275     -44.066   4.369 -12.356  1.00 61.70           N  
+ANISOU 2131  NH1 ARG A 275     7953   9689   5801  -3965   1367  -2471       N  
+ATOM   2132  NH2 ARG A 275     -44.437   3.979 -10.127  1.00 63.89           N  
+ANISOU 2132  NH2 ARG A 275     8430   9494   6350  -3953   1581  -2370       N  
+ATOM   2133  N   ILE A 276     -41.353   9.441  -7.766  1.00 56.06           N  
+ANISOU 2133  N   ILE A 276     7379   8178   5744  -2342    955  -1125       N  
+ATOM   2134  CA  ILE A 276     -40.578   9.155  -6.571  1.00 57.21           C  
+ANISOU 2134  CA  ILE A 276     7765   7957   6016  -2233   1063  -1049       C  
+ATOM   2135  C   ILE A 276     -41.214   9.877  -5.394  1.00 59.74           C  
+ANISOU 2135  C   ILE A 276     7992   8287   6422  -2131   1037   -959       C  
+ATOM   2136  O   ILE A 276     -41.481   9.263  -4.355  1.00 60.68           O  
+ANISOU 2136  O   ILE A 276     8230   8235   6591  -2206   1174   -998       O  
+ATOM   2137  CB  ILE A 276     -39.104   9.571  -6.721  1.00 56.20           C  
+ANISOU 2137  CB  ILE A 276     7770   7653   5931  -2004   1009   -904       C  
+ATOM   2138  CG1 ILE A 276     -38.408   8.688  -7.760  1.00 57.60           C  
+ANISOU 2138  CG1 ILE A 276     8074   7781   6031  -2104   1075  -1012       C  
+ATOM   2139  CG2 ILE A 276     -38.385   9.477  -5.385  1.00 50.79           C  
+ANISOU 2139  CG2 ILE A 276     7278   6659   5362  -1858   1083   -806       C  
+ATOM   2140  CD1 ILE A 276     -37.036   9.183  -8.165  1.00 55.84           C  
+ANISOU 2140  CD1 ILE A 276     7920   7471   5825  -1896   1009   -882       C  
+ATOM   2141  N   GLU A 277     -41.525  11.159  -5.588  1.00 55.27           N  
+ANISOU 2141  N   GLU A 277     7210   7927   5863  -1969    874   -843       N  
+ATOM   2142  CA  GLU A 277     -42.106  11.954  -4.516  1.00 55.19           C  
+ANISOU 2142  CA  GLU A 277     7102   7930   5939  -1849    850   -767       C  
+ATOM   2143  C   GLU A 277     -43.388  11.297  -4.046  1.00 61.15           C  
+ANISOU 2143  C   GLU A 277     7768   8799   6668  -2067    958   -913       C  
+ATOM   2144  O   GLU A 277     -43.635  11.190  -2.840  1.00 59.44           O  
+ANISOU 2144  O   GLU A 277     7618   8448   6516  -2060   1053   -907       O  
+ATOM   2145  CB  GLU A 277     -42.381  13.390  -4.961  1.00 56.66           C  
+ANISOU 2145  CB  GLU A 277     7060   8330   6137  -1651    675   -636       C  
+ATOM   2146  CG  GLU A 277     -43.026  14.232  -3.869  1.00 57.25           C  
+ANISOU 2146  CG  GLU A 277     7030   8414   6309  -1520    664   -578       C  
+ATOM   2147  CD  GLU A 277     -43.242  15.673  -4.277  1.00 60.45           C  
+ANISOU 2147  CD  GLU A 277     7240   8978   6752  -1298    511   -436       C  
+ATOM   2148  OE1 GLU A 277     -43.194  15.967  -5.490  1.00 72.26           O  
+ANISOU 2148  OE1 GLU A 277     8633  10652   8169  -1276    407   -385       O  
+ATOM   2149  OE2 GLU A 277     -43.467  16.512  -3.380  1.00 82.68           O  
+ANISOU 2149  OE2 GLU A 277    10010  11733   9671  -1141    504   -374       O  
+ATOM   2150  N   ASN A 278     -44.187  10.837  -5.006  1.00 57.69           N  
+ANISOU 2150  N   ASN A 278     7176   8621   6123  -2276    949  -1053       N  
+ATOM   2151  CA  ASN A 278     -45.439  10.176  -4.688  1.00 59.17           C  
+ANISOU 2151  CA  ASN A 278     7250   8955   6279  -2526   1056  -1218       C  
+ATOM   2152  C   ASN A 278     -45.159   9.032  -3.728  1.00 74.50           C  
+ANISOU 2152  C   ASN A 278     9472  10562   8274  -2671   1274  -1285       C  
+ATOM   2153  O   ASN A 278     -45.716   8.985  -2.625  1.00 80.64           O  
+ANISOU 2153  O   ASN A 278    10252  11285   9104  -2697   1369  -1283       O  
+ATOM   2154  CB  ASN A 278     -46.125   9.669  -5.956  1.00 60.74           C  
+ANISOU 2154  CB  ASN A 278     7275   9468   6337  -2765   1025  -1390       C  
+ATOM   2155  CG  ASN A 278     -47.556   9.249  -5.712  1.00 75.19           C  
+ANISOU 2155  CG  ASN A 278     8898  11543   8130  -3015   1100  -1561       C  
+ATOM   2156  OD1 ASN A 278     -48.409  10.080  -5.409  1.00 74.15           O  
+ANISOU 2156  OD1 ASN A 278     8509  11652   8012  -2913   1016  -1510       O  
+ATOM   2157  ND2 ASN A 278     -47.828   7.955  -5.840  1.00 75.87           N  
+ANISOU 2157  ND2 ASN A 278     9089  11563   8174  -3345   1270  -1771       N  
+ATOM   2158  N   ASN A 279     -44.234   8.161  -4.131  1.00 62.08           N  
+ANISOU 2158  N   ASN A 279     8144   8757   6686  -2735   1355  -1323       N  
+ATOM   2159  CA  ASN A 279     -43.879   6.981  -3.351  1.00 58.36           C  
+ANISOU 2159  CA  ASN A 279     7971   7942   6262  -2855   1574  -1369       C  
+ATOM   2160  C   ASN A 279     -43.537   7.347  -1.916  1.00 69.36           C  
+ANISOU 2160  C   ASN A 279     9486   9126   7743  -2660   1611  -1210       C  
+ATOM   2161  O   ASN A 279     -43.767   6.569  -0.990  1.00 80.79           O  
+ANISOU 2161  O   ASN A 279    11094  10384   9216  -2772   1792  -1234       O  
+ATOM   2162  CB  ASN A 279     -42.704   6.244  -3.992  1.00 63.84           C  
+ANISOU 2162  CB  ASN A 279     8909   8401   6947  -2846   1627  -1386       C  
+ATOM   2163  CG  ASN A 279     -43.092   5.512  -5.261  1.00 68.30           C  
+ANISOU 2163  CG  ASN A 279     9418   9119   7414  -3113   1662  -1600       C  
+ATOM   2164  OD1 ASN A 279     -44.273   5.345  -5.561  1.00 71.34           O  
+ANISOU 2164  OD1 ASN A 279     9605   9762   7738  -3351   1676  -1755       O  
+ATOM   2165  ND2 ASN A 279     -42.092   5.067  -6.013  1.00 73.01           N  
+ANISOU 2165  ND2 ASN A 279    10177   9575   7988  -3080   1679  -1623       N  
+ATOM   2166  N   ILE A 280     -42.984   8.543  -1.741  1.00 59.73           N  
+ANISOU 2166  N   ILE A 280     8191   7942   6561  -2375   1447  -1051       N  
+ATOM   2167  CA  ILE A 280     -42.621   9.011  -0.418  1.00 68.83           C  
+ANISOU 2167  CA  ILE A 280     9438   8935   7781  -2184   1461   -918       C  
+ATOM   2168  C   ILE A 280     -43.852   9.550   0.305  1.00 80.40           C  
+ANISOU 2168  C   ILE A 280    10701  10590   9256  -2220   1470   -944       C  
+ATOM   2169  O   ILE A 280     -44.196   9.092   1.401  1.00 92.88           O  
+ANISOU 2169  O   ILE A 280    12382  12062  10847  -2286   1614   -951       O  
+ATOM   2170  CB  ILE A 280     -41.542  10.111  -0.489  1.00 64.15           C  
+ANISOU 2170  CB  ILE A 280     8840   8302   7232  -1889   1295   -763       C  
+ATOM   2171  CG1 ILE A 280     -40.337   9.631  -1.305  1.00 60.07           C  
+ANISOU 2171  CG1 ILE A 280     8484   7640   6699  -1852   1283   -744       C  
+ATOM   2172  CG2 ILE A 280     -41.147  10.570   0.908  1.00 57.81           C  
+ANISOU 2172  CG2 ILE A 280     8131   7352   6482  -1712   1311   -655       C  
+ATOM   2173  CD1 ILE A 280     -39.626   8.440  -0.709  1.00 71.06           C  
+ANISOU 2173  CD1 ILE A 280    10171   8729   8098  -1883   1450   -743       C  
+ATOM   2174  N   LYS A 281     -44.549  10.482  -0.340  1.00 78.57           N  
+ANISOU 2174  N   LYS A 281    10181  10656   9015  -2176   1325   -956       N  
+ATOM   2175  CA  LYS A 281     -45.579  11.255   0.348  1.00 72.40           C  
+ANISOU 2175  CA  LYS A 281     9185  10062   8263  -2126   1307   -955       C  
+ATOM   2176  C   LYS A 281     -46.788  10.405   0.711  1.00 79.95           C  
+ANISOU 2176  C   LYS A 281    10068  11129   9180  -2406   1469  -1106       C  
+ATOM   2177  O   LYS A 281     -47.503  10.706   1.666  1.00 80.83           O  
+ANISOU 2177  O   LYS A 281    10092  11305   9316  -2393   1531  -1111       O  
+ATOM   2178  CB  LYS A 281     -46.017  12.452  -0.499  1.00 68.64           C  
+ANISOU 2178  CB  LYS A 281     8418   9872   7788  -1981   1116   -913       C  
+ATOM   2179  CG  LYS A 281     -45.146  13.686  -0.310  1.00 74.10           C  
+ANISOU 2179  CG  LYS A 281     9138  10456   8560  -1670    986   -748       C  
+ATOM   2180  CD  LYS A 281     -45.687  14.882  -1.077  1.00 83.92           C  
+ANISOU 2180  CD  LYS A 281    10107  11961   9817  -1515    823   -684       C  
+ATOM   2181  CE  LYS A 281     -46.954  15.420  -0.429  1.00 79.75           C  
+ANISOU 2181  CE  LYS A 281     9348  11631   9321  -1482    844   -725       C  
+ATOM   2182  NZ  LYS A 281     -46.684  16.078   0.882  1.00 75.01           N  
+ANISOU 2182  NZ  LYS A 281     8838  10843   8821  -1310    890   -670       N  
+ATOM   2183  N   THR A 282     -46.996   9.325  -0.031  1.00 71.46           N  
+ANISOU 2183  N   THR A 282     9036  10070   8044  -2673   1554  -1240       N  
+ATOM   2184  CA  THR A 282     -48.126   8.447   0.225  1.00 64.71           C  
+ANISOU 2184  CA  THR A 282     8115   9317   7156  -2987   1725  -1405       C  
+ATOM   2185  C   THR A 282     -47.850   7.483   1.372  1.00 69.01           C  
+ANISOU 2185  C   THR A 282     8964   9529   7727  -3088   1954  -1389       C  
+ATOM   2186  O   THR A 282     -48.697   6.654   1.702  1.00 75.24           O  
+ANISOU 2186  O   THR A 282     9751  10337   8497  -3368   2138  -1514       O  
+ATOM   2187  CB  THR A 282     -48.499   7.630  -1.024  1.00 69.49           C  
+ANISOU 2187  CB  THR A 282     8649  10071   7682  -3271   1743  -1588       C  
+ATOM   2188  OG1 THR A 282     -47.372   6.847  -1.438  1.00 91.92           O  
+ANISOU 2188  OG1 THR A 282    11792  12611  10523  -3292   1800  -1580       O  
+ATOM   2189  CG2 THR A 282     -48.916   8.550  -2.156  1.00 76.70           C  
+ANISOU 2189  CG2 THR A 282     9234  11372   8535  -3180   1517  -1597       C  
+ATOM   2190  N   LYS A 283     -46.672   7.585   1.982  1.00 71.11           N  
+ANISOU 2190  N   LYS A 283     9487   9501   8030  -2865   1949  -1232       N  
+ATOM   2191  CA  LYS A 283     -46.354   6.699   3.096  1.00 74.74           C  
+ANISOU 2191  CA  LYS A 283    10244   9655   8497  -2919   2157  -1180       C  
+ATOM   2192  C   LYS A 283     -46.524   7.390   4.448  1.00 74.81           C  
+ANISOU 2192  C   LYS A 283    10235   9673   8518  -2751   2169  -1074       C  
+ATOM   2193  O   LYS A 283     -46.358   6.768   5.497  1.00 74.25           O  
+ANISOU 2193  O   LYS A 283    10388   9395   8430  -2778   2336  -1012       O  
+ATOM   2194  CB  LYS A 283     -44.946   6.127   2.947  1.00 64.44           C  
+ANISOU 2194  CB  LYS A 283     9254   8026   7206  -2801   2174  -1085       C  
+ATOM   2195  CG  LYS A 283     -44.977   4.706   2.407  1.00 75.39           C  
+ANISOU 2195  CG  LYS A 283    10830   9233   8582  -3075   2362  -1206       C  
+ATOM   2196  CD  LYS A 283     -43.607   4.068   2.324  1.00 83.90           C  
+ANISOU 2196  CD  LYS A 283    12225   9974   9680  -2938   2405  -1109       C  
+ATOM   2197  CE  LYS A 283     -43.679   2.749   1.566  1.00 97.03           C  
+ANISOU 2197  CE  LYS A 283    14052  11470  11344  -3210   2584  -1263       C  
+ATOM   2198  NZ  LYS A 283     -42.388   2.010   1.572  1.00 89.25           N  
+ANISOU 2198  NZ  LYS A 283    13394  10128  10388  -3067   2665  -1168       N  
+ATOM   2199  N   THR A 284     -46.845   8.680   4.416  1.00 68.35           N  
+ANISOU 2199  N   THR A 284     9157   9090   7721  -2571   1998  -1051       N  
+ATOM   2200  CA  THR A 284     -47.239   9.391   5.626  1.00 62.65           C  
+ANISOU 2200  CA  THR A 284     8368   8428   7008  -2444   2020  -1001       C  
+ATOM   2201  C   THR A 284     -48.717   9.754   5.520  1.00 72.21           C  
+ANISOU 2201  C   THR A 284     9248   9970   8217  -2576   2035  -1126       C  
+ATOM   2202  O   THR A 284     -49.113  10.531   4.652  1.00 63.06           O  
+ANISOU 2202  O   THR A 284     7824   9055   7080  -2506   1874  -1161       O  
+ATOM   2203  CB  THR A 284     -46.397  10.659   5.853  1.00 64.11           C  
+ANISOU 2203  CB  THR A 284     8533   8589   7238  -2108   1836   -880       C  
+ATOM   2204  OG1 THR A 284     -45.038  10.289   6.117  1.00 75.36           O  
+ANISOU 2204  OG1 THR A 284    10248   9733   8654  -1989   1834   -769       O  
+ATOM   2205  CG2 THR A 284     -46.935  11.452   7.034  1.00 52.56           C  
+ANISOU 2205  CG2 THR A 284     6971   7219   5782  -1993   1863   -869       C  
+ATOM   2206  N   VAL A 285     -49.525   9.185   6.408  1.00 77.66           N  
+ANISOU 2206  N   VAL A 285     9951  10682   8876  -2759   2233  -1184       N  
+ATOM   2207  CA  VAL A 285     -50.975   9.327   6.329  1.00 74.62           C  
+ANISOU 2207  CA  VAL A 285     9246  10625   8483  -2930   2282  -1323       C  
+ATOM   2208  C   VAL A 285     -51.532  10.289   7.377  1.00 80.14           C  
+ANISOU 2208  C   VAL A 285     9787  11464   9196  -2760   2288  -1299       C  
+ATOM   2209  O   VAL A 285     -51.115  10.272   8.534  1.00 71.46           O  
+ANISOU 2209  O   VAL A 285     8888  10187   8075  -2671   2383  -1217       O  
+ATOM   2210  CB  VAL A 285     -51.667   7.959   6.489  1.00 72.77           C  
+ANISOU 2210  CB  VAL A 285     9093  10351   8205  -3317   2531  -1443       C  
+ATOM   2211  CG1 VAL A 285     -53.164   8.087   6.271  1.00 62.28           C  
+ANISOU 2211  CG1 VAL A 285     7392   9409   6864  -3519   2570  -1610       C  
+ATOM   2212  CG2 VAL A 285     -51.071   6.950   5.522  1.00 76.21           C  
+ANISOU 2212  CG2 VAL A 285     9722  10602   8632  -3489   2555  -1485       C  
+ATOM   2213  N   PHE A 286     -52.475  11.129   6.960  1.00 72.87           N  
+ANISOU 2213  N   PHE A 286     8504  10877   8304  -2705   2188  -1373       N  
+ATOM   2214  CA  PHE A 286     -53.199  11.990   7.887  1.00 59.30           C  
+ANISOU 2214  CA  PHE A 286     6599   9326   6608  -2567   2221  -1386       C  
+ATOM   2215  C   PHE A 286     -54.550  11.379   8.241  1.00 71.06           C  
+ANISOU 2215  C   PHE A 286     7894  11051   8055  -2855   2413  -1532       C  
+ATOM   2216  O   PHE A 286     -55.374  11.127   7.362  1.00 63.65           O  
+ANISOU 2216  O   PHE A 286     6701  10378   7107  -3037   2389  -1651       O  
+ATOM   2217  CB  PHE A 286     -53.392  13.385   7.292  1.00 59.04           C  
+ANISOU 2217  CB  PHE A 286     6285   9500   6647  -2278   2004  -1360       C  
+ATOM   2218  CG  PHE A 286     -54.248  14.288   8.133  1.00 72.21           C  
+ANISOU 2218  CG  PHE A 286     7727  11358   8351  -2130   2046  -1398       C  
+ATOM   2219  CD1 PHE A 286     -53.787  14.762   9.350  1.00 75.35           C  
+ANISOU 2219  CD1 PHE A 286     8293  11579   8759  -1961   2108  -1345       C  
+ATOM   2220  CD2 PHE A 286     -55.508  14.668   7.706  1.00 69.75           C  
+ANISOU 2220  CD2 PHE A 286     7026  11420   8055  -2152   2023  -1496       C  
+ATOM   2221  CE1 PHE A 286     -54.569  15.594  10.127  1.00 70.26           C  
+ANISOU 2221  CE1 PHE A 286     7447  11104   8146  -1822   2162  -1400       C  
+ATOM   2222  CE2 PHE A 286     -56.294  15.503   8.478  1.00 73.36           C  
+ANISOU 2222  CE2 PHE A 286     7269  12050   8553  -1994   2073  -1536       C  
+ATOM   2223  CZ  PHE A 286     -55.825  15.964   9.691  1.00 62.13           C  
+ANISOU 2223  CZ  PHE A 286     6033  10426   7147  -1832   2150  -1494       C  
+ATOM   2224  N   LEU A 287     -54.773  11.136   9.529  1.00 91.28           N  
+ANISOU 2224  N   LEU A 287    10568  13536  10579  -2907   2606  -1527       N  
+ATOM   2225  CA  LEU A 287     -56.046  10.588   9.984  1.00 65.72           C  
+ANISOU 2225  CA  LEU A 287     7151  10520   7301  -3186   2814  -1661       C  
+ATOM   2226  C   LEU A 287     -56.970  11.693  10.477  1.00 69.62           C  
+ANISOU 2226  C   LEU A 287     7307  11321   7826  -3008   2793  -1717       C  
+ATOM   2227  O   LEU A 287     -56.785  12.242  11.563  1.00 77.56           O  
+ANISOU 2227  O   LEU A 287     8397  12249   8822  -2825   2847  -1663       O  
+ATOM   2228  CB  LEU A 287     -55.832   9.550  11.087  1.00 66.53           C  
+ANISOU 2228  CB  LEU A 287     7581  10367   7329  -3382   3076  -1617       C  
+ATOM   2229  CG  LEU A 287     -55.157   8.245  10.665  1.00 74.49           C  
+ANISOU 2229  CG  LEU A 287     8915  11074   8313  -3612   3167  -1584       C  
+ATOM   2230  CD1 LEU A 287     -55.061   7.288  11.841  1.00 71.31           C  
+ANISOU 2230  CD1 LEU A 287     8825  10433   7835  -3777   3444  -1515       C  
+ATOM   2231  CD2 LEU A 287     -55.918   7.607   9.514  1.00 74.68           C  
+ANISOU 2231  CD2 LEU A 287     8736  11287   8354  -3926   3181  -1753       C  
+ATOM   2232  N   SER A 288     -57.966  12.014   9.660  1.00 68.45           N  
+ANISOU 2232  N   SER A 288     6767  11535   7705  -3054   2713  -1831       N  
+ATOM   2233  CA  SER A 288     -58.932  13.054   9.977  1.00 69.88           C  
+ANISOU 2233  CA  SER A 288     6583  12041   7927  -2869   2688  -1890       C  
+ATOM   2234  C   SER A 288     -60.201  12.450  10.561  1.00 73.15           C  
+ANISOU 2234  C   SER A 288     6787  12716   8290  -3166   2924  -2042       C  
+ATOM   2235  O   SER A 288     -60.725  11.471  10.031  1.00 96.60           O  
+ANISOU 2235  O   SER A 288     9681  15804  11218  -3520   3012  -2152       O  
+ATOM   2236  CB  SER A 288     -59.271  13.864   8.726  1.00 70.06           C  
+ANISOU 2236  CB  SER A 288     6273  12340   8006  -2689   2445  -1900       C  
+ATOM   2237  OG  SER A 288     -60.305  14.797   8.987  1.00 71.96           O  
+ANISOU 2237  OG  SER A 288     6137  12914   8292  -2508   2436  -1959       O  
+ATOM   2238  N   GLY A 289     -60.694  13.028  11.652  1.00 74.10           N  
+ANISOU 2238  N   GLY A 289     6813  12929   8413  -3038   3040  -2063       N  
+ATOM   2239  CA  GLY A 289     -61.956  12.584  12.212  1.00 90.94           C  
+ANISOU 2239  CA  GLY A 289     8701  15351  10500  -3298   3267  -2211       C  
+ATOM   2240  C   GLY A 289     -62.167  12.807  13.697  1.00 93.76           C  
+ANISOU 2240  C   GLY A 289     9139  15670  10814  -3239   3474  -2210       C  
+ATOM   2241  O   GLY A 289     -61.228  12.753  14.489  1.00 95.78           O  
+ANISOU 2241  O   GLY A 289     9766  15596  11028  -3142   3520  -2093       O  
+ATOM   2242  N   SER A 290     -63.418  13.075  14.060  1.00 94.19           N  
+ANISOU 2242  N   SER A 290     8846  16069  10874  -3271   3569  -2335       N  
+ATOM   2243  CA  SER A 290     -63.843  13.174  15.453  1.00 91.30           C  
+ANISOU 2243  CA  SER A 290     8542  15690  10457  -3242   3754  -2348       C  
+ATOM   2244  C   SER A 290     -65.228  12.543  15.578  1.00 97.53           C  
+ANISOU 2244  C   SER A 290     9112  16715  11229  -3494   3845  -2465       C  
+ATOM   2245  O   SER A 290     -65.993  12.557  14.614  1.00 95.15           O  
+ANISOU 2245  O   SER A 290     8488  16692  10973  -3555   3723  -2559       O  
+ATOM   2246  CB  SER A 290     -63.863  14.632  15.910  1.00 89.85           C  
+ANISOU 2246  CB  SER A 290     8165  15644  10330  -2840   3713  -2368       C  
+ATOM   2247  OG  SER A 290     -64.701  15.407  15.068  1.00 86.63           O  
+ANISOU 2247  OG  SER A 290     7308  15586  10022  -2672   3561  -2447       O  
+ATOM   2248  N   ALA A 291     -65.566  11.994  16.742  1.00103.31           N  
+ANISOU 2248  N   ALA A 291    10009  17358  11885  -3639   4052  -2461       N  
+ATOM   2249  CA  ALA A 291     -66.868  11.342  16.887  1.00 92.24           C  
+ANISOU 2249  CA  ALA A 291     8411  16170  10465  -3904   4158  -2577       C  
+ATOM   2250  C   ALA A 291     -67.364  11.262  18.326  1.00 94.37           C  
+ANISOU 2250  C   ALA A 291     8754  16438  10663  -3930   4377  -2576       C  
+ATOM   2251  O   ALA A 291     -66.609  10.947  19.232  1.00 95.90           O  
+ANISOU 2251  O   ALA A 291     9315  16346  10777  -3932   4499  -2458       O  
+ATOM   2252  CB  ALA A 291     -66.814   9.944  16.293  1.00 93.05           C  
+ANISOU 2252  CB  ALA A 291     8710  16104  10540  -4288   4194  -2590       C  
+ATOM   2253  N   VAL A 292     -68.646  11.547  18.518  1.00108.82           N  
+ANISOU 2253  N   VAL A 292    10226  18608  12511  -3944   4421  -2703       N  
+ATOM   2254  CA  VAL A 292     -69.339  11.261  19.770  1.00115.45           C  
+ANISOU 2254  CA  VAL A 292    11098  19491  13276  -4051   4646  -2725       C  
+ATOM   2255  C   VAL A 292     -70.322  10.129  19.495  1.00104.15           C  
+ANISOU 2255  C   VAL A 292     9575  18168  11828  -4449   4740  -2825       C  
+ATOM   2256  O   VAL A 292     -70.617   9.291  20.354  1.00106.36           O  
+ANISOU 2256  O   VAL A 292    10041  18338  12033  -4687   4951  -2805       O  
+ATOM   2257  CB  VAL A 292     -70.071  12.487  20.322  1.00102.00           C  
+ANISOU 2257  CB  VAL A 292     9061  18087  11606  -3750   4653  -2805       C  
+ATOM   2258  CG1 VAL A 292     -70.852  12.122  21.580  1.00105.34           C  
+ANISOU 2258  CG1 VAL A 292     9503  18579  11942  -3891   4894  -2838       C  
+ATOM   2259  CG2 VAL A 292     -69.071  13.588  20.623  1.00105.26           C  
+ANISOU 2259  CG2 VAL A 292     9593  18363  12039  -3366   4575  -2730       C  
+ATOM   2260  N   GLU A 293     -70.838  10.151  18.269  1.00104.92           N  
+ANISOU 2260  N   GLU A 293     9375  18500  11991  -4510   4576  -2936       N  
+ATOM   2261  CA  GLU A 293     -71.736   9.139  17.731  1.00121.06           C  
+ANISOU 2261  CA  GLU A 293    11298  20680  14021  -4886   4620  -3068       C  
+ATOM   2262  C   GLU A 293     -71.065   8.398  16.580  1.00112.98           C  
+ANISOU 2262  C   GLU A 293    10452  19466  13010  -5064   4500  -3063       C  
+ATOM   2263  O   GLU A 293     -70.205   8.945  15.885  1.00103.24           O  
+ANISOU 2263  O   GLU A 293     9254  18156  11817  -4850   4318  -2992       O  
+ATOM   2264  CB  GLU A 293     -73.026   9.778  17.224  1.00111.34           C  
+ANISOU 2264  CB  GLU A 293     9531  19945  12828  -4811   4520  -3230       C  
+ATOM   2265  CG  GLU A 293     -74.305   9.163  17.747  1.00119.94           C  
+ANISOU 2265  CG  GLU A 293    10448  21249  13873  -5094   4703  -3364       C  
+ATOM   2266  CD  GLU A 293     -75.487   9.503  16.872  1.00129.75           C  
+ANISOU 2266  CD  GLU A 293    11185  22973  15140  -5095   4565  -3535       C  
+ATOM   2267  OE1 GLU A 293     -75.677  10.697  16.563  1.00128.17           O  
+ANISOU 2267  OE1 GLU A 293    10676  23028  14997  -4727   4402  -3530       O  
+ATOM   2268  OE2 GLU A 293     -76.224   8.574  16.485  1.00144.54           O  
+ANISOU 2268  OE2 GLU A 293    12976  24970  16973  -5454   4621  -3674       O  
+ATOM   2269  N   TYR A 294     -71.507   7.166  16.365  1.00119.47           N  
+ANISOU 2269  N   TYR A 294    11370  20225  13798  -5458   4610  -3153       N  
+ATOM   2270  CA  TYR A 294     -70.943   6.298  15.345  1.00115.28           C  
+ANISOU 2270  CA  TYR A 294    11039  19489  13271  -5670   4538  -3175       C  
+ATOM   2271  C   TYR A 294     -72.044   5.857  14.404  1.00111.93           C  
+ANISOU 2271  C   TYR A 294    10292  19402  12834  -5928   4480  -3396       C  
+ATOM   2272  O   TYR A 294     -71.986   4.770  13.836  1.00113.13           O  
+ANISOU 2272  O   TYR A 294    10618  19402  12965  -6242   4525  -3479       O  
+ATOM   2273  CB  TYR A 294     -70.245   5.087  15.980  1.00118.28           C  
+ANISOU 2273  CB  TYR A 294    11936  19387  13618  -5904   4748  -3070       C  
+ATOM   2274  CG  TYR A 294     -69.028   5.492  16.770  1.00104.46           C  
+ANISOU 2274  CG  TYR A 294    10521  17312  11858  -5638   4773  -2844       C  
+ATOM   2275  CD1 TYR A 294     -69.120   5.805  18.119  1.00104.98           C  
+ANISOU 2275  CD1 TYR A 294    10664  17349  11875  -5522   4928  -2748       C  
+ATOM   2276  CD2 TYR A 294     -67.791   5.592  16.158  1.00106.46           C  
+ANISOU 2276  CD2 TYR A 294    11002  17313  12137  -5498   4636  -2736       C  
+ATOM   2277  CE1 TYR A 294     -68.005   6.195  18.833  1.00101.85           C  
+ANISOU 2277  CE1 TYR A 294    10567  16687  11444  -5274   4940  -2556       C  
+ATOM   2278  CE2 TYR A 294     -66.674   5.978  16.860  1.00108.87           C  
+ANISOU 2278  CE2 TYR A 294    11602  17346  12419  -5254   4651  -2540       C  
+ATOM   2279  CZ  TYR A 294     -66.785   6.279  18.198  1.00112.17           C  
+ANISOU 2279  CZ  TYR A 294    12093  17749  12776  -5142   4799  -2454       C  
+ATOM   2280  OH  TYR A 294     -65.665   6.665  18.897  1.00 99.19           O  
+ANISOU 2280  OH  TYR A 294    10742  15861  11086  -4898   4805  -2272       O  
+ATOM   2281  N   HIS A 296     -73.164   2.977  12.765  1.00119.36           N  
+ANISOU 2281  N   HIS A 296    11338  20324  13688  -6904   4633  -3820       N  
+ATOM   2282  CA  HIS A 296     -74.130   2.200  13.533  1.00129.72           C  
+ANISOU 2282  CA  HIS A 296    12646  21671  14972  -7217   4884  -3925       C  
+ATOM   2283  C   HIS A 296     -73.480   0.998  14.209  1.00129.03           C  
+ANISOU 2283  C   HIS A 296    13090  21044  14890  -7446   5136  -3828       C  
+ATOM   2284  O   HIS A 296     -74.026  -0.103  14.174  1.00136.23           O  
+ANISOU 2284  O   HIS A 296    14096  21884  15780  -7819   5315  -3967       O  
+ATOM   2285  CB  HIS A 296     -75.260   1.708  12.626  1.00145.95           C  
+ANISOU 2285  CB  HIS A 296    14380  24099  16975  -7520   4853  -4203       C  
+ATOM   2286  CG  HIS A 296     -76.045   2.803  11.975  1.00147.41           C  
+ANISOU 2286  CG  HIS A 296    14020  24852  17138  -7304   4615  -4299       C  
+ATOM   2287  ND1 HIS A 296     -77.182   3.343  12.537  1.00140.19           N  
+ANISOU 2287  ND1 HIS A 296    12728  24326  16212  -7254   4657  -4366       N  
+ATOM   2288  CD2 HIS A 296     -75.864   3.449  10.799  1.00142.88           C  
+ANISOU 2288  CD2 HIS A 296    13216  24526  16547  -7110   4336  -4327       C  
+ATOM   2289  CE1 HIS A 296     -77.664   4.277  11.738  1.00144.42           C  
+ANISOU 2289  CE1 HIS A 296    12826  25316  16730  -7023   4412  -4427       C  
+ATOM   2290  NE2 HIS A 296     -76.882   4.363  10.677  1.00145.20           N  
+ANISOU 2290  NE2 HIS A 296    13007  25342  16822  -6931   4212  -4398       N  
+ATOM   2291  N   TRP A 297     -72.329   1.209  14.840  1.00126.24           N  
+ANISOU 2291  N   TRP A 297    13083  20318  14563  -7215   5157  -3586       N  
+ATOM   2292  CA  TRP A 297     -71.634   0.115  15.506  1.00124.60           C  
+ANISOU 2292  CA  TRP A 297    13394  19593  14357  -7374   5384  -3454       C  
+ATOM   2293  C   TRP A 297     -71.572   0.401  16.999  1.00124.79           C  
+ANISOU 2293  C   TRP A 297    13548  19511  14356  -7232   5548  -3264       C  
+ATOM   2294  O   TRP A 297     -71.797   1.533  17.426  1.00126.83           O  
+ANISOU 2294  O   TRP A 297    13544  20041  14606  -6962   5460  -3222       O  
+ATOM   2295  CB  TRP A 297     -70.215  -0.082  14.958  1.00116.34           C  
+ANISOU 2295  CB  TRP A 297    12709  18155  13341  -7241   5284  -3319       C  
+ATOM   2296  CG  TRP A 297     -70.119  -0.441  13.503  1.00124.39           C  
+ANISOU 2296  CG  TRP A 297    13663  19228  14372  -7376   5138  -3491       C  
+ATOM   2297  CD1 TRP A 297     -71.117  -0.416  12.572  1.00119.03           C  
+ANISOU 2297  CD1 TRP A 297    12599  18962  13665  -7551   5040  -3744       C  
+ATOM   2298  CD2 TRP A 297     -68.969  -0.973  12.839  1.00120.56           C  
+ANISOU 2298  CD2 TRP A 297    13527  18369  13912  -7362   5093  -3428       C  
+ATOM   2299  NE1 TRP A 297     -70.642  -0.843  11.356  1.00125.41           N  
+ANISOU 2299  NE1 TRP A 297    13490  19693  14469  -7638   4928  -3842       N  
+ATOM   2300  CE2 TRP A 297     -69.326  -1.201  11.497  1.00120.39           C  
+ANISOU 2300  CE2 TRP A 297    13305  18566  13873  -7528   4964  -3656       C  
+ATOM   2301  CE3 TRP A 297     -67.663  -1.262  13.248  1.00113.98           C  
+ANISOU 2301  CE3 TRP A 297    13147  17053  13106  -7210   5145  -3200       C  
+ATOM   2302  CZ2 TRP A 297     -68.427  -1.704  10.561  1.00117.26           C  
+ANISOU 2302  CZ2 TRP A 297    13151  17914  13489  -7552   4898  -3669       C  
+ATOM   2303  CZ3 TRP A 297     -66.774  -1.760  12.320  1.00109.26           C  
+ANISOU 2303  CZ3 TRP A 297    12785  16197  12533  -7226   5076  -3209       C  
+ATOM   2304  CH2 TRP A 297     -67.158  -1.976  10.991  1.00110.50           C  
+ANISOU 2304  CH2 TRP A 297    12738  16571  12675  -7399   4959  -3446       C  
+ATOM   2305  N   GLU A 298     -71.255  -0.612  17.799  1.00123.61           N  
+ANISOU 2305  N   GLU A 298    13809  18970  14187  -7397   5790  -3145       N  
+ATOM   2306  CA  GLU A 298     -71.101  -0.377  19.224  1.00122.82           C  
+ANISOU 2306  CA  GLU A 298    13866  18765  14037  -7251   5943  -2943       C  
+ATOM   2307  C   GLU A 298     -69.824   0.433  19.397  1.00116.85           C  
+ANISOU 2307  C   GLU A 298    13285  17837  13275  -6857   5790  -2730       C  
+ATOM   2308  O   GLU A 298     -68.827   0.161  18.728  1.00113.85           O  
+ANISOU 2308  O   GLU A 298    13147  17182  12929  -6800   5690  -2665       O  
+ATOM   2309  CB  GLU A 298     -71.035  -1.691  20.004  1.00124.65           C  
+ANISOU 2309  CB  GLU A 298    14506  18616  14240  -7509   6236  -2843       C  
+ATOM   2310  N   THR A 299     -69.874   1.451  20.251  1.00115.36           N  
+ANISOU 2310  N   THR A 299    12959  17831  13043  -6588   5771  -2641       N  
+ATOM   2311  CA  THR A 299     -68.747   2.363  20.452  1.00118.57           C  
+ANISOU 2311  CA  THR A 299    13485  18133  13434  -6206   5625  -2468       C  
+ATOM   2312  C   THR A 299     -67.421   1.635  20.688  1.00122.32           C  
+ANISOU 2312  C   THR A 299    14483  18111  13883  -6162   5676  -2248       C  
+ATOM   2313  O   THR A 299     -66.415   1.990  20.091  1.00119.51           O  
+ANISOU 2313  O   THR A 299    14235  17617  13558  -5969   5505  -2179       O  
+ATOM   2314  CB  THR A 299     -69.026   3.345  21.610  1.00118.98           C  
+ANISOU 2314  CB  THR A 299    13392  18398  13417  -5964   5673  -2405       C  
+ATOM   2315  OG1 THR A 299     -69.931   4.363  21.156  1.00122.54           O  
+ANISOU 2315  OG1 THR A 299    13341  19302  13916  -5861   5541  -2588       O  
+ATOM   2316  CG2 THR A 299     -67.742   4.002  22.090  1.00117.18           C  
+ANISOU 2316  CG2 THR A 299    13413  17969  13140  -5617   5590  -2203       C  
+ATOM   2317  N   GLU A 300     -67.424   0.616  21.543  1.00111.39           N  
+ANISOU 2317  N   GLU A 300    13416  16464  12443  -6334   5912  -2132       N  
+ATOM   2318  CA  GLU A 300     -66.197  -0.122  21.850  1.00114.95           C  
+ANISOU 2318  CA  GLU A 300    14367  16446  12863  -6267   5972  -1901       C  
+ATOM   2319  C   GLU A 300     -65.661  -0.824  20.595  1.00118.87           C  
+ANISOU 2319  C   GLU A 300    15011  16701  13455  -6388   5886  -1966       C  
+ATOM   2320  O   GLU A 300     -64.445  -0.855  20.344  1.00118.19           O  
+ANISOU 2320  O   GLU A 300    15197  16336  13376  -6201   5790  -1820       O  
+ATOM   2321  CB  GLU A 300     -66.450  -1.134  22.969  1.00113.76           C  
+ANISOU 2321  CB  GLU A 300    14500  16087  12637  -6440   6256  -1767       C  
+ATOM   2322  CG  GLU A 300     -65.224  -1.924  23.393  1.00112.91           C  
+ANISOU 2322  CG  GLU A 300    14907  15508  12486  -6340   6329  -1501       C  
+ATOM   2323  CD  GLU A 300     -65.468  -2.723  24.657  1.00133.40           C  
+ANISOU 2323  CD  GLU A 300    17754  17950  14981  -6446   6601  -1330       C  
+ATOM   2324  OE1 GLU A 300     -66.643  -2.833  25.067  1.00133.57           O  
+ANISOU 2324  OE1 GLU A 300    17567  18199  14987  -6663   6752  -1446       O  
+ATOM   2325  OE2 GLU A 300     -64.492  -3.239  25.240  1.00142.99           O  
+ANISOU 2325  OE2 GLU A 300    19369  18832  16128  -6305   6663  -1073       O  
+ATOM   2326  N   HIS A 301     -66.580  -1.364  19.799  1.00111.76           N  
+ANISOU 2326  N   HIS A 301    13916  15930  12616  -6699   5918  -2199       N  
+ATOM   2327  CA  HIS A 301     -66.227  -2.048  18.559  1.00111.40           C  
+ANISOU 2327  CA  HIS A 301    13975  15704  12648  -6847   5849  -2309       C  
+ATOM   2328  C   HIS A 301     -65.602  -1.058  17.579  1.00112.74           C  
+ANISOU 2328  C   HIS A 301    13964  16017  12855  -6603   5560  -2343       C  
+ATOM   2329  O   HIS A 301     -64.602  -1.361  16.930  1.00104.83           O  
+ANISOU 2329  O   HIS A 301    13202  14740  11888  -6533   5479  -2283       O  
+ATOM   2330  CB  HIS A 301     -67.456  -2.715  17.935  1.00115.62           C  
+ANISOU 2330  CB  HIS A 301    14287  16429  13215  -7232   5937  -2585       C  
+ATOM   2331  N   ALA A 302     -66.211   0.120  17.471  1.00112.86           N  
+ANISOU 2331  N   ALA A 302    13552  16465  12866  -6469   5414  -2439       N  
+ATOM   2332  CA  ALA A 302     -65.708   1.186  16.609  1.00102.45           C  
+ANISOU 2332  CA  ALA A 302    12022  15321  11582  -6217   5145  -2460       C  
+ATOM   2333  C   ALA A 302     -64.334   1.673  17.073  1.00 98.43           C  
+ANISOU 2333  C   ALA A 302    11801  14547  11050  -5889   5080  -2217       C  
+ATOM   2334  O   ALA A 302     -63.462   1.992  16.259  1.00118.21           O  
+ANISOU 2334  O   ALA A 302    14356  16966  13591  -5743   4909  -2186       O  
+ATOM   2335  CB  ALA A 302     -66.695   2.337  16.571  1.00102.94           C  
+ANISOU 2335  CB  ALA A 302    11579  15889  11645  -6110   5034  -2590       C  
+ATOM   2336  N   GLU A 303     -64.150   1.719  18.389  1.00 98.77           N  
+ANISOU 2336  N   GLU A 303    12029  14478  11019  -5780   5220  -2048       N  
+ATOM   2337  CA  GLU A 303     -62.885   2.108  18.994  1.00 98.73           C  
+ANISOU 2337  CA  GLU A 303    12314  14238  10961  -5479   5180  -1816       C  
+ATOM   2338  C   GLU A 303     -61.835   1.099  18.570  1.00103.90           C  
+ANISOU 2338  C   GLU A 303    13384  14454  11640  -5525   5200  -1701       C  
+ATOM   2339  O   GLU A 303     -60.670   1.446  18.353  1.00 91.37           O  
+ANISOU 2339  O   GLU A 303    11969  12698  10050  -5291   5074  -1573       O  
+ATOM   2340  CB  GLU A 303     -62.996   2.155  20.520  1.00 96.99           C  
+ANISOU 2340  CB  GLU A 303    12226  13997  10627  -5396   5349  -1669       C  
+ATOM   2341  CG  GLU A 303     -63.841   3.289  21.077  1.00101.31           C  
+ANISOU 2341  CG  GLU A 303    12398  14954  11140  -5274   5331  -1762       C  
+ATOM   2342  CD  GLU A 303     -63.982   3.224  22.590  1.00110.11           C  
+ANISOU 2342  CD  GLU A 303    13661  16051  12125  -5222   5517  -1627       C  
+ATOM   2343  OE1 GLU A 303     -63.554   2.213  23.185  1.00111.10           O  
+ANISOU 2343  OE1 GLU A 303    14161  15865  12188  -5313   5670  -1461       O  
+ATOM   2344  OE2 GLU A 303     -64.513   4.185  23.186  1.00109.30           O  
+ANISOU 2344  OE2 GLU A 303    13303  16248  11979  -5078   5513  -1685       O  
+ATOM   2345  N   GLN A 304     -62.258  -0.159  18.456  1.00 97.95           N  
+ANISOU 2345  N   GLN A 304    12790  13513  10912  -5823   5368  -1754       N  
+ATOM   2346  CA  GLN A 304     -61.362  -1.221  18.005  1.00101.30           C  
+ANISOU 2346  CA  GLN A 304    13604  13510  11374  -5878   5412  -1672       C  
+ATOM   2347  C   GLN A 304     -61.095  -1.133  16.503  1.00 95.95           C  
+ANISOU 2347  C   GLN A 304    12807  12868  10782  -5917   5231  -1830       C  
+ATOM   2348  O   GLN A 304     -60.028  -1.527  16.026  1.00 94.16           O  
+ANISOU 2348  O   GLN A 304    12858  12334  10583  -5825   5183  -1740       O  
+ATOM   2349  CB  GLN A 304     -61.942  -2.593  18.343  1.00108.68           C  
+ANISOU 2349  CB  GLN A 304    14748  14230  12316  -6186   5669  -1698       C  
+ATOM   2350  CG  GLN A 304     -60.979  -3.734  18.086  1.00114.41           C  
+ANISOU 2350  CG  GLN A 304    15919  14473  13078  -6200   5754  -1583       C  
+ATOM   2351  CD  GLN A 304     -61.630  -5.100  18.162  1.00128.76           C  
+ANISOU 2351  CD  GLN A 304    17911  16087  14926  -6536   6009  -1663       C  
+ATOM   2352  OE1 GLN A 304     -62.838  -5.236  17.960  1.00131.17           O  
+ANISOU 2352  OE1 GLN A 304    17955  16639  15247  -6818   6081  -1882       O  
+ATOM   2353  NE2 GLN A 304     -60.835  -6.119  18.468  1.00137.15           N  
+ANISOU 2353  NE2 GLN A 304    19414  16701  15997  -6498   6152  -1486       N  
+ATOM   2354  N   PHE A 305     -62.063  -0.603  15.761  1.00 96.59           N  
+ANISOU 2354  N   PHE A 305    12465  13343  10893  -6040   5126  -2061       N  
+ATOM   2355  CA  PHE A 305     -61.880  -0.413  14.330  1.00102.12           C  
+ANISOU 2355  CA  PHE A 305    13006  14146  11649  -6066   4936  -2212       C  
+ATOM   2356  C   PHE A 305     -60.804   0.628  14.099  1.00 93.76           C  
+ANISOU 2356  C   PHE A 305    11945  13086  10594  -5724   4732  -2075       C  
+ATOM   2357  O   PHE A 305     -59.873   0.409  13.329  1.00 88.54           O  
+ANISOU 2357  O   PHE A 305    11461  12215   9964  -5664   4643  -2041       O  
+ATOM   2358  CB  PHE A 305     -63.175   0.016  13.643  1.00 96.96           C  
+ANISOU 2358  CB  PHE A 305    11869  13968  11004  -6233   4850  -2469       C  
+ATOM   2359  CG  PHE A 305     -62.952   0.692  12.319  1.00102.38           C  
+ANISOU 2359  CG  PHE A 305    12305  14876  11717  -6143   4598  -2575       C  
+ATOM   2360  CD1 PHE A 305     -62.343   0.014  11.274  1.00 98.88           C  
+ANISOU 2360  CD1 PHE A 305    12040  14230  11299  -6242   4552  -2636       C  
+ATOM   2361  CD2 PHE A 305     -63.334   2.009  12.124  1.00100.24           C  
+ANISOU 2361  CD2 PHE A 305    11625  15016  11445  -5943   4413  -2607       C  
+ATOM   2362  CE1 PHE A 305     -62.127   0.635  10.056  1.00 92.27           C  
+ANISOU 2362  CE1 PHE A 305    10974  13614  10471  -6159   4321  -2722       C  
+ATOM   2363  CE2 PHE A 305     -63.122   2.635  10.907  1.00 97.09           C  
+ANISOU 2363  CE2 PHE A 305    10996  14829  11065  -5846   4180  -2681       C  
+ATOM   2364  CZ  PHE A 305     -62.518   1.947   9.872  1.00 90.87           C  
+ANISOU 2364  CZ  PHE A 305    10387  13853  10288  -5962   4131  -2736       C  
+ATOM   2365  N   ILE A 306     -60.954   1.769  14.762  1.00 89.12           N  
+ANISOU 2365  N   ILE A 306    11149  12741   9971  -5503   4667  -2010       N  
+ATOM   2366  CA  ILE A 306     -59.965   2.835  14.688  1.00 92.61           C  
+ANISOU 2366  CA  ILE A 306    11587  13191  10408  -5171   4497  -1883       C  
+ATOM   2367  C   ILE A 306     -58.605   2.309  15.162  1.00 91.62           C  
+ANISOU 2367  C   ILE A 306    11941  12619  10253  -5030   4552  -1655       C  
+ATOM   2368  O   ILE A 306     -57.571   2.546  14.525  1.00 86.16           O  
+ANISOU 2368  O   ILE A 306    11362  11789   9584  -4877   4419  -1587       O  
+ATOM   2369  CB  ILE A 306     -60.402   4.053  15.531  1.00 89.36           C  
+ANISOU 2369  CB  ILE A 306    10916  13082   9955  -4960   4470  -1862       C  
+ATOM   2370  CG1 ILE A 306     -61.808   4.499  15.118  1.00 92.72           C  
+ANISOU 2370  CG1 ILE A 306    10863  13952  10412  -5082   4427  -2079       C  
+ATOM   2371  CG2 ILE A 306     -59.425   5.198  15.367  1.00 85.92           C  
+ANISOU 2371  CG2 ILE A 306    10457  12671   9518  -4629   4299  -1766       C  
+ATOM   2372  CD1 ILE A 306     -62.345   5.679  15.904  1.00 96.99           C  
+ANISOU 2372  CD1 ILE A 306    11124  14800  10928  -4867   4414  -2084       C  
+ATOM   2373  N   HIS A 307     -58.633   1.587  16.280  1.00 94.58           N  
+ANISOU 2373  N   HIS A 307    12583  12785  10569  -5078   4747  -1531       N  
+ATOM   2374  CA  HIS A 307     -57.450   0.979  16.886  1.00 87.52           C  
+ANISOU 2374  CA  HIS A 307    12141  11485   9628  -4934   4817  -1294       C  
+ATOM   2375  C   HIS A 307     -56.641   0.131  15.904  1.00 95.14           C  
+ANISOU 2375  C   HIS A 307    13354  12129  10664  -4986   4788  -1288       C  
+ATOM   2376  O   HIS A 307     -55.457   0.387  15.668  1.00104.57           O  
+ANISOU 2376  O   HIS A 307    14721  13155  11856  -4760   4675  -1159       O  
+ATOM   2377  CB  HIS A 307     -57.879   0.123  18.084  1.00 87.98           C  
+ANISOU 2377  CB  HIS A 307    12409  11399   9619  -5047   5054  -1193       C  
+ATOM   2378  CG  HIS A 307     -56.742  -0.500  18.832  1.00 87.71           C  
+ANISOU 2378  CG  HIS A 307    12819  10988   9519  -4871   5128   -926       C  
+ATOM   2379  ND1 HIS A 307     -56.294  -0.007  20.040  1.00 92.06           N  
+ANISOU 2379  ND1 HIS A 307    13478  11562   9939  -4632   5142   -732       N  
+ATOM   2380  CD2 HIS A 307     -55.978  -1.584  18.564  1.00 88.33           C  
+ANISOU 2380  CD2 HIS A 307    13253  10674   9634  -4885   5194   -824       C  
+ATOM   2381  CE1 HIS A 307     -55.296  -0.751  20.475  1.00 95.96           C  
+ANISOU 2381  CE1 HIS A 307    14362  11713  10385  -4501   5197   -508       C  
+ATOM   2382  NE2 HIS A 307     -55.083  -1.717  19.598  1.00 91.44           N  
+ANISOU 2382  NE2 HIS A 307    13948  10873   9922  -4641   5234   -555       N  
+ATOM   2383  N   GLN A 308     -57.283  -0.872  15.315  1.00 91.54           N  
+ANISOU 2383  N   GLN A 308    12912  11601  10268  -5285   4893  -1444       N  
+ATOM   2384  CA  GLN A 308     -56.551  -1.788  14.454  1.00 95.86           C  
+ANISOU 2384  CA  GLN A 308    13721  11823  10877  -5340   4901  -1455       C  
+ATOM   2385  C   GLN A 308     -56.316  -1.198  13.077  1.00 95.15           C  
+ANISOU 2385  C   GLN A 308    13411  11901  10841  -5323   4689  -1601       C  
+ATOM   2386  O   GLN A 308     -55.413  -1.632  12.364  1.00101.42           O  
+ANISOU 2386  O   GLN A 308    14414  12448  11674  -5269   4646  -1575       O  
+ATOM   2387  CB  GLN A 308     -57.276  -3.127  14.336  1.00 99.55           C  
+ANISOU 2387  CB  GLN A 308    14315  12130  11380  -5667   5114  -1583       C  
+ATOM   2388  CG  GLN A 308     -57.280  -3.936  15.618  1.00 93.64           C  
+ANISOU 2388  CG  GLN A 308    13874  11118  10586  -5675   5346  -1400       C  
+ATOM   2389  CD  GLN A 308     -58.300  -5.047  15.580  1.00124.33           C  
+ANISOU 2389  CD  GLN A 308    17792  14944  14505  -6035   5567  -1560       C  
+ATOM   2390  OE1 GLN A 308     -59.304  -4.959  14.872  1.00140.85           O  
+ANISOU 2390  OE1 GLN A 308    19577  17316  16624  -6284   5542  -1821       O  
+ATOM   2391  NE2 GLN A 308     -58.026  -6.125  16.305  1.00145.64           N  
+ANISOU 2391  NE2 GLN A 308    20863  17277  17195  -6060   5787  -1406       N  
+ATOM   2392  N   LEU A 309     -57.115  -0.203  12.706  1.00 93.45           N  
+ANISOU 2392  N   LEU A 309    12770  12115  10624  -5350   4556  -1746       N  
+ATOM   2393  CA  LEU A 309     -56.824   0.557  11.500  1.00 86.75           C  
+ANISOU 2393  CA  LEU A 309    11689  11463   9808  -5275   4333  -1840       C  
+ATOM   2394  C   LEU A 309     -55.466   1.218  11.666  1.00 87.03           C  
+ANISOU 2394  C   LEU A 309    11900  11334   9831  -4947   4221  -1627       C  
+ATOM   2395  O   LEU A 309     -54.600   1.106  10.799  1.00 90.43           O  
+ANISOU 2395  O   LEU A 309    12448  11616  10296  -4886   4126  -1614       O  
+ATOM   2396  CB  LEU A 309     -57.893   1.610  11.217  1.00 85.11           C  
+ANISOU 2396  CB  LEU A 309    10983  11761   9594  -5296   4208  -1992       C  
+ATOM   2397  CG  LEU A 309     -57.551   2.535  10.043  1.00 78.78           C  
+ANISOU 2397  CG  LEU A 309     9926  11190   8817  -5170   3966  -2049       C  
+ATOM   2398  CD1 LEU A 309     -57.378   1.735   8.757  1.00 85.88           C  
+ANISOU 2398  CD1 LEU A 309    10889  12002   9741  -5361   3925  -2191       C  
+ATOM   2399  CD2 LEU A 309     -58.597   3.621   9.867  1.00 89.22           C  
+ANISOU 2399  CD2 LEU A 309    10750  13015  10134  -5131   3844  -2168       C  
+ATOM   2400  N   SER A 310     -55.285   1.897  12.794  1.00 76.44           N  
+ANISOU 2400  N   SER A 310    10581  10031   8432  -4738   4239  -1472       N  
+ATOM   2401  CA  SER A 310     -54.006   2.523  13.106  1.00 76.70           C  
+ANISOU 2401  CA  SER A 310    10795   9920   8429  -4423   4147  -1272       C  
+ATOM   2402  C   SER A 310     -52.888   1.484  13.180  1.00 76.95           C  
+ANISOU 2402  C   SER A 310    11275   9501   8462  -4364   4219  -1114       C  
+ATOM   2403  O   SER A 310     -51.787   1.704  12.660  1.00 70.75           O  
+ANISOU 2403  O   SER A 310    10615   8576   7690  -4189   4104  -1030       O  
+ATOM   2404  CB  SER A 310     -54.108   3.302  14.414  1.00 75.31           C  
+ANISOU 2404  CB  SER A 310    10581   9871   8163  -4236   4182  -1161       C  
+ATOM   2405  OG  SER A 310     -55.075   4.329  14.288  1.00 80.09           O  
+ANISOU 2405  OG  SER A 310    10762  10890   8781  -4245   4111  -1310       O  
+ATOM   2406  N   LYS A 311     -53.174   0.350  13.817  1.00 76.11           N  
+ANISOU 2406  N   LYS A 311    11403   9170   8344  -4499   4413  -1073       N  
+ATOM   2407  CA  LYS A 311     -52.152  -0.674  14.032  1.00 76.58           C  
+ANISOU 2407  CA  LYS A 311    11892   8800   8405  -4405   4502   -903       C  
+ATOM   2408  C   LYS A 311     -51.664  -1.325  12.748  1.00 86.38           C  
+ANISOU 2408  C   LYS A 311    13232   9851   9736  -4488   4465  -1003       C  
+ATOM   2409  O   LYS A 311     -50.476  -1.637  12.600  1.00 88.22           O  
+ANISOU 2409  O   LYS A 311    13735   9805   9979  -4295   4435   -862       O  
+ATOM   2410  CB  LYS A 311     -52.665  -1.799  14.930  1.00 80.31           C  
+ANISOU 2410  CB  LYS A 311    12580   9079   8854  -4549   4738   -847       C  
+ATOM   2411  CG  LYS A 311     -51.593  -2.863  15.124  1.00 92.63           C  
+ANISOU 2411  CG  LYS A 311    14573  10199  10422  -4417   4831   -661       C  
+ATOM   2412  CD  LYS A 311     -52.120  -4.242  15.442  1.00102.45           C  
+ANISOU 2412  CD  LYS A 311    16035  11197  11694  -4632   5078   -676       C  
+ATOM   2413  CE  LYS A 311     -51.095  -5.284  15.009  1.00108.71           C  
+ANISOU 2413  CE  LYS A 311    17183  11577  12545  -4534   5139   -589       C  
+ATOM   2414  NZ  LYS A 311     -51.420  -6.637  15.524  1.00116.04           N  
+ANISOU 2414  NZ  LYS A 311    18386  12215  13491  -4677   5402   -544       N  
+ATOM   2415  N   GLU A 312     -52.574  -1.477  11.795  1.00 87.30           N  
+ANISOU 2415  N   GLU A 312    13110  10152   9908  -4762   4456  -1255       N  
+ATOM   2416  CA  GLU A 312     -52.248  -2.197  10.583  1.00 87.13           C  
+ANISOU 2416  CA  GLU A 312    13180   9974   9953  -4879   4447  -1387       C  
+ATOM   2417  C   GLU A 312     -51.948  -1.160   9.512  1.00 98.63           C  
+ANISOU 2417  C   GLU A 312    14371  11682  11424  -4803   4212  -1467       C  
+ATOM   2418  O   GLU A 312     -51.612  -1.484   8.374  1.00115.37           O  
+ANISOU 2418  O   GLU A 312    16506  13746  13583  -4872   4156  -1582       O  
+ATOM   2419  CB  GLU A 312     -53.425  -3.113  10.204  1.00 93.79           C  
+ANISOU 2419  CB  GLU A 312    13945  10869  10821  -5243   4596  -1626       C  
+ATOM   2420  CG  GLU A 312     -53.308  -3.886   8.901  1.00101.29           C  
+ANISOU 2420  CG  GLU A 312    14949  11719  11818  -5415   4607  -1822       C  
+ATOM   2421  CD  GLU A 312     -52.257  -4.979   8.959  1.00105.65           C  
+ANISOU 2421  CD  GLU A 312    15944  11789  12408  -5309   4744  -1700       C  
+ATOM   2422  OE1 GLU A 312     -51.806  -5.323  10.073  1.00109.81           O  
+ANISOU 2422  OE1 GLU A 312    16741  12061  12923  -5146   4858  -1471       O  
+ATOM   2423  OE2 GLU A 312     -51.884  -5.498   7.887  1.00100.40           O  
+ANISOU 2423  OE2 GLU A 312    15351  11018  11778  -5376   4738  -1831       O  
+ATOM   2424  N   LEU A 313     -52.031   0.104   9.911  1.00 80.49           N  
+ANISOU 2424  N   LEU A 313    11837   9658   9088  -4643   4084  -1398       N  
+ATOM   2425  CA  LEU A 313     -51.357   1.177   9.196  1.00 69.53           C  
+ANISOU 2425  CA  LEU A 313    10292   8421   7705  -4463   3875  -1371       C  
+ATOM   2426  C   LEU A 313     -49.877   1.132   9.543  1.00 87.92           C  
+ANISOU 2426  C   LEU A 313    12961  10423  10020  -4180   3855  -1139       C  
+ATOM   2427  O   LEU A 313     -49.014   1.186   8.670  1.00 84.23           O  
+ANISOU 2427  O   LEU A 313    12556   9859   9588  -4073   3730  -1131       O  
+ATOM   2428  CB  LEU A 313     -51.956   2.540   9.546  1.00 76.26           C  
+ANISOU 2428  CB  LEU A 313    10783   9669   8522  -4369   3769  -1383       C  
+ATOM   2429  CG  LEU A 313     -53.108   3.034   8.669  1.00 72.75           C  
+ANISOU 2429  CG  LEU A 313     9894   9647   8100  -4550   3670  -1609       C  
+ATOM   2430  CD1 LEU A 313     -53.661   4.336   9.212  1.00 72.53           C  
+ANISOU 2430  CD1 LEU A 313     9549   9953   8054  -4334   3534  -1593       C  
+ATOM   2431  CD2 LEU A 313     -52.616   3.231   7.246  1.00 67.78           C  
+ANISOU 2431  CD2 LEU A 313     9176   9071   7506  -4492   3450  -1684       C  
+ATOM   2432  N   ILE A 314     -49.597   1.001  10.836  1.00 87.67           N  
+ANISOU 2432  N   ILE A 314    13140  10241   9930  -4029   3952   -954       N  
+ATOM   2433  CA  ILE A 314     -48.224   0.955  11.324  1.00 78.71           C  
+ANISOU 2433  CA  ILE A 314    12315   8834   8756  -3733   3927   -719       C  
+ATOM   2434  C   ILE A 314     -47.515  -0.340  10.930  1.00 77.60           C  
+ANISOU 2434  C   ILE A 314    12507   8306   8671  -3739   4017   -679       C  
+ATOM   2435  O   ILE A 314     -46.323  -0.335  10.610  1.00 69.20           O  
+ANISOU 2435  O   ILE A 314    11615   7063   7616  -3528   3938   -565       O  
+ATOM   2436  CB  ILE A 314     -48.184   1.108  12.858  1.00 72.63           C  
+ANISOU 2436  CB  ILE A 314    11667   8049   7880  -3572   4003   -537       C  
+ATOM   2437  CG1 ILE A 314     -48.646   2.508  13.267  1.00 72.82           C  
+ANISOU 2437  CG1 ILE A 314    11371   8441   7855  -3454   3859   -579       C  
+ATOM   2438  CG2 ILE A 314     -46.793   0.834  13.387  1.00 69.37           C  
+ANISOU 2438  CG2 ILE A 314    11588   7356   7412  -3273   3983   -294       C  
+ATOM   2439  CD1 ILE A 314     -47.741   3.619  12.781  1.00 61.89           C  
+ANISOU 2439  CD1 ILE A 314     9859   7153   6504  -3120   3538   -557       C  
+ATOM   2440  N   ARG A 315     -48.259  -1.441  10.923  1.00 85.71           N  
+ANISOU 2440  N   ARG A 315    13615   9214   9736  -3979   4190   -787       N  
+ATOM   2441  CA  ARG A 315     -47.699  -2.742  10.573  1.00 92.46           C  
+ANISOU 2441  CA  ARG A 315    14785   9698  10646  -3995   4314   -775       C  
+ATOM   2442  C   ARG A 315     -47.173  -2.759   9.141  1.00 94.99           C  
+ANISOU 2442  C   ARG A 315    15066   9992  11033  -4022   4209   -910       C  
+ATOM   2443  O   ARG A 315     -46.201  -3.451   8.837  1.00 97.42           O  
+ANISOU 2443  O   ARG A 315    15636  10002  11376  -3887   4245   -838       O  
+ATOM   2444  CB  ARG A 315     -48.745  -3.843  10.762  1.00 76.46           C  
+ANISOU 2444  CB  ARG A 315    12819   7588   8646  -4287   4533   -905       C  
+ATOM   2445  N   LYS A 316     -47.816  -1.993   8.265  1.00 89.24           N  
+ANISOU 2445  N   LYS A 316    13997   9594  10314  -4185   4078  -1102       N  
+ATOM   2446  CA  LYS A 316     -47.398  -1.919   6.869  1.00 80.92           C  
+ANISOU 2446  CA  LYS A 316    12868   8574   9304  -4229   3964  -1239       C  
+ATOM   2447  C   LYS A 316     -46.532  -0.692   6.595  1.00 82.42           C  
+ANISOU 2447  C   LYS A 316    12947   8890   9478  -3991   3753  -1121       C  
+ATOM   2448  O   LYS A 316     -46.632  -0.079   5.532  1.00105.69           O  
+ANISOU 2448  O   LYS A 316    15637  12085  12436  -4000   3556  -1257       O  
+ATOM   2449  CB  LYS A 316     -48.620  -1.910   5.950  1.00 85.58           C  
+ANISOU 2449  CB  LYS A 316    13145   9475   9898  -4560   3942  -1529       C  
+ATOM   2450  N   ASP A 317     -45.692  -0.342   7.566  1.00 78.16           N  
+ANISOU 2450  N   ASP A 317    12564   8231   8901  -3667   3705   -880       N  
+ATOM   2451  CA  ASP A 317     -44.663   0.687   7.403  1.00 74.69           C  
+ANISOU 2451  CA  ASP A 317    12038   7888   8452  -3291   3419   -770       C  
+ATOM   2452  C   ASP A 317     -45.203   2.069   7.031  1.00 70.95           C  
+ANISOU 2452  C   ASP A 317    11163   7824   7972  -3228   3169   -860       C  
+ATOM   2453  O   ASP A 317     -44.496   2.863   6.411  1.00 71.59           O  
+ANISOU 2453  O   ASP A 317    11132   8000   8069  -3009   2937   -837       O  
+ATOM   2454  CB  ASP A 317     -43.639   0.247   6.352  1.00 87.79           C  
+ANISOU 2454  CB  ASP A 317    13836   9358  10162  -3208   3365   -790       C  
+ATOM   2455  CG  ASP A 317     -42.670  -0.790   6.881  1.00104.55           C  
+ANISOU 2455  CG  ASP A 317    16364  11068  12292  -3080   3541   -619       C  
+ATOM   2456  OD1 ASP A 317     -41.755  -0.414   7.644  1.00106.05           O  
+ANISOU 2456  OD1 ASP A 317    16652  11202  12440  -2755   3449   -411       O  
+ATOM   2457  OD2 ASP A 317     -42.823  -1.980   6.536  1.00109.32           O  
+ANISOU 2457  OD2 ASP A 317    17185  11408  12945  -3299   3772   -696       O  
+ATOM   2458  N   PHE A 318     -46.444   2.361   7.405  1.00 75.88           N  
+ANISOU 2458  N   PHE A 318    11569   8685   8575  -3412   3225   -954       N  
+ATOM   2459  CA  PHE A 318     -46.986   3.697   7.183  1.00 66.92           C  
+ANISOU 2459  CA  PHE A 318    10062   7926   7440  -3311   3004  -1015       C  
+ATOM   2460  C   PHE A 318     -46.709   4.605   8.370  1.00 63.76           C  
+ANISOU 2460  C   PHE A 318     9648   7576   7000  -3034   2927   -863       C  
+ATOM   2461  O   PHE A 318     -46.431   4.138   9.476  1.00 64.98           O  
+ANISOU 2461  O   PHE A 318    10040   7546   7103  -2989   3074   -735       O  
+ATOM   2462  CB  PHE A 318     -48.491   3.650   6.915  1.00 70.09           C  
+ANISOU 2462  CB  PHE A 318    10183   8609   7839  -3625   3084  -1210       C  
+ATOM   2463  CG  PHE A 318     -48.849   3.155   5.547  1.00 79.07           C  
+ANISOU 2463  CG  PHE A 318    11210   9834   8997  -3874   3072  -1403       C  
+ATOM   2464  CD1 PHE A 318     -49.186   1.828   5.342  1.00 75.75           C  
+ANISOU 2464  CD1 PHE A 318    10967   9229   8588  -4216   3318  -1520       C  
+ATOM   2465  CD2 PHE A 318     -48.859   4.020   4.466  1.00 80.15           C  
+ANISOU 2465  CD2 PHE A 318    11072  10243   9138  -3774   2823  -1470       C  
+ATOM   2466  CE1 PHE A 318     -49.520   1.371   4.082  1.00 78.79           C  
+ANISOU 2466  CE1 PHE A 318    11245   9714   8979  -4466   3310  -1729       C  
+ATOM   2467  CE2 PHE A 318     -49.190   3.569   3.204  1.00 75.29           C  
+ANISOU 2467  CE2 PHE A 318    10346   9747   8512  -4004   2805  -1653       C  
+ATOM   2468  CZ  PHE A 318     -49.522   2.243   3.011  1.00 81.06           C  
+ANISOU 2468  CZ  PHE A 318    11244  10310   9247  -4357   3045  -1797       C  
+ATOM   2469  N   ASN A 319     -46.788   5.907   8.129  1.00 61.41           N  
+ANISOU 2469  N   ASN A 319     9079   7531   6724  -2849   2703   -881       N  
+ATOM   2470  CA  ASN A 319     -46.636   6.890   9.187  1.00 55.22           C  
+ANISOU 2470  CA  ASN A 319     8244   6826   5911  -2608   2627   -785       C  
+ATOM   2471  C   ASN A 319     -47.947   7.634   9.402  1.00 74.95           C  
+ANISOU 2471  C   ASN A 319    10420   9642   8416  -2683   2624   -898       C  
+ATOM   2472  O   ASN A 319     -48.665   7.920   8.445  1.00 90.54           O  
+ANISOU 2472  O   ASN A 319    12132  11836  10433  -2788   2546  -1024       O  
+ATOM   2473  CB  ASN A 319     -45.511   7.861   8.845  1.00 55.44           C  
+ANISOU 2473  CB  ASN A 319     8252   6838   5973  -2298   2385   -701       C  
+ATOM   2474  CG  ASN A 319     -44.194   7.152   8.591  1.00 75.06           C  
+ANISOU 2474  CG  ASN A 319    11023   9042   8453  -2207   2382   -596       C  
+ATOM   2475  OD1 ASN A 319     -43.833   6.216   9.306  1.00 75.09           O  
+ANISOU 2475  OD1 ASN A 319    11298   8827   8406  -2233   2545   -505       O  
+ATOM   2476  ND2 ASN A 319     -43.459   7.608   7.584  1.00 73.27           N  
+ANISOU 2476  ND2 ASN A 319    10737   8823   8278  -2085   2203   -595       N  
+ATOM   2477  N   ILE A 320     -48.259   7.950  10.653  1.00 66.35           N  
+ANISOU 2477  N   ILE A 320     9339   8597   7274  -2619   2708   -855       N  
+ATOM   2478  CA  ILE A 320     -49.528   8.595  10.962  1.00 61.73           C  
+ANISOU 2478  CA  ILE A 320     8452   8310   6694  -2684   2737   -967       C  
+ATOM   2479  C   ILE A 320     -49.330   9.985  11.555  1.00 58.98           C  
+ANISOU 2479  C   ILE A 320     7973   8077   6358  -2384   2589   -934       C  
+ATOM   2480  O   ILE A 320     -48.554  10.170  12.491  1.00 57.04           O  
+ANISOU 2480  O   ILE A 320     7919   7697   6056  -2213   2591   -829       O  
+ATOM   2481  CB  ILE A 320     -50.366   7.744  11.942  1.00 61.79           C  
+ANISOU 2481  CB  ILE A 320     8539   8312   6625  -2926   3016   -990       C  
+ATOM   2482  CG1 ILE A 320     -50.749   6.410  11.299  1.00 61.37           C  
+ANISOU 2482  CG1 ILE A 320     8583   8154   6581  -3271   3187  -1062       C  
+ATOM   2483  CG2 ILE A 320     -51.613   8.496  12.380  1.00 63.80           C  
+ANISOU 2483  CG2 ILE A 320     8470   8893   6881  -2957   3048  -1104       C  
+ATOM   2484  CD1 ILE A 320     -51.499   5.479  12.228  1.00 64.19           C  
+ANISOU 2484  CD1 ILE A 320     9059   8458   6871  -3537   3490  -1069       C  
+ATOM   2485  N   VAL A 321     -50.041  10.959  10.997  1.00 65.47           N  
+ANISOU 2485  N   VAL A 321     8468   9155   7251  -2318   2465  -1027       N  
+ATOM   2486  CA  VAL A 321     -50.119  12.290  11.582  1.00 66.57           C  
+ANISOU 2486  CA  VAL A 321     8458   9415   7422  -2063   2368  -1029       C  
+ATOM   2487  C   VAL A 321     -51.560  12.536  12.005  1.00 80.45           C  
+ANISOU 2487  C   VAL A 321     9942  11450   9176  -2166   2485  -1150       C  
+ATOM   2488  O   VAL A 321     -52.480  12.421  11.194  1.00 79.91           O  
+ANISOU 2488  O   VAL A 321     9624  11593   9143  -2311   2480  -1247       O  
+ATOM   2489  CB  VAL A 321     -49.660  13.381  10.598  1.00 56.32           C  
+ANISOU 2489  CB  VAL A 321     7014   8157   6228  -1839   2123  -1010       C  
+ATOM   2490  CG1 VAL A 321     -49.914  14.763  11.180  1.00 55.40           C  
+ANISOU 2490  CG1 VAL A 321     6729   8153   6166  -1596   2055  -1035       C  
+ATOM   2491  CG2 VAL A 321     -48.189  13.205  10.260  1.00 58.85           C  
+ANISOU 2491  CG2 VAL A 321     7590   8218   6550  -1730   2015   -895       C  
+ATOM   2492  N   SER A 322     -51.760  12.879  13.273  1.00 72.02           N  
+ANISOU 2492  N   SER A 322     8904  10408   8053  -2090   2591  -1154       N  
+ATOM   2493  CA  SER A 322     -53.110  13.001  13.808  1.00 63.60           C  
+ANISOU 2493  CA  SER A 322     7595   9603   6968  -2201   2741  -1271       C  
+ATOM   2494  C   SER A 322     -53.344  14.321  14.534  1.00 68.78           C  
+ANISOU 2494  C   SER A 322     8096  10383   7656  -1940   2697  -1316       C  
+ATOM   2495  O   SER A 322     -52.471  14.821  15.243  1.00 71.83           O  
+ANISOU 2495  O   SER A 322     8662  10617   8012  -1747   2651  -1257       O  
+ATOM   2496  CB  SER A 322     -53.409  11.835  14.752  1.00 61.87           C  
+ANISOU 2496  CB  SER A 322     7567   9317   6622  -2454   3005  -1257       C  
+ATOM   2497  OG  SER A 322     -54.669  11.999  15.379  1.00 69.53           O  
+ANISOU 2497  OG  SER A 322     8304  10548   7566  -2557   3165  -1372       O  
+ATOM   2498  N   GLY A 323     -54.535  14.876  14.342  1.00 69.42           N  
+ANISOU 2498  N   GLY A 323     7830  10750   7795  -1935   2715  -1432       N  
+ATOM   2499  CA  GLY A 323     -54.937  16.098  15.012  1.00 64.91           C  
+ANISOU 2499  CA  GLY A 323     7086  10308   7269  -1696   2707  -1499       C  
+ATOM   2500  C   GLY A 323     -55.592  15.802  16.347  1.00 77.16           C  
+ANISOU 2500  C   GLY A 323     8650  11960   8705  -1805   2948  -1567       C  
+ATOM   2501  O   GLY A 323     -56.088  16.707  17.019  1.00 85.14           O  
+ANISOU 2501  O   GLY A 323     9506  13108   9737  -1640   2990  -1653       O  
+ATOM   2502  N   PHE A 324     -55.588  14.525  16.722  1.00 70.03           N  
+ANISOU 2502  N   PHE A 324     7946  10982   7683  -2083   3120  -1526       N  
+ATOM   2503  CA  PHE A 324     -56.119  14.074  18.006  1.00 67.27           C  
+ANISOU 2503  CA  PHE A 324     7660  10703   7195  -2221   3373  -1558       C  
+ATOM   2504  C   PHE A 324     -57.584  14.470  18.199  1.00 70.33           C  
+ANISOU 2504  C   PHE A 324     7671  11439   7614  -2277   3496  -1717       C  
+ATOM   2505  O   PHE A 324     -57.930  15.181  19.143  1.00 70.95           O  
+ANISOU 2505  O   PHE A 324     7667  11634   7657  -2137   3578  -1787       O  
+ATOM   2506  CB  PHE A 324     -55.267  14.603  19.165  1.00 66.41           C  
+ANISOU 2506  CB  PHE A 324     7783  10459   6991  -2008   3371  -1506       C  
+ATOM   2507  CG  PHE A 324     -55.555  13.933  20.481  1.00 80.54           C  
+ANISOU 2507  CG  PHE A 324     9729  12279   8592  -2161   3628  -1489       C  
+ATOM   2508  CD1 PHE A 324     -55.338  12.574  20.640  1.00 76.82           C  
+ANISOU 2508  CD1 PHE A 324     9518  11657   8011  -2412   3777  -1370       C  
+ATOM   2509  CD2 PHE A 324     -56.040  14.659  21.556  1.00 84.62           C  
+ANISOU 2509  CD2 PHE A 324    10143  12968   9039  -2050   3734  -1588       C  
+ATOM   2510  CE1 PHE A 324     -55.603  11.950  21.845  1.00 78.52           C  
+ANISOU 2510  CE1 PHE A 324     9894  11897   8045  -2548   4025  -1327       C  
+ATOM   2511  CE2 PHE A 324     -56.305  14.042  22.765  1.00 71.96           C  
+ANISOU 2511  CE2 PHE A 324     8688  11413   7240  -2193   3977  -1563       C  
+ATOM   2512  CZ  PHE A 324     -56.086  12.685  22.909  1.00 72.63           C  
+ANISOU 2512  CZ  PHE A 324     9036  11350   7210  -2442   4122  -1420       C  
+ATOM   2513  N   GLY A 325     -58.434  14.019  17.282  1.00 73.71           N  
+ANISOU 2513  N   GLY A 325     7854  12049   8102  -2479   3508  -1786       N  
+ATOM   2514  CA  GLY A 325     -59.862  14.257  17.381  1.00 74.03           C  
+ANISOU 2514  CA  GLY A 325     7504  12457   8167  -2563   3628  -1940       C  
+ATOM   2515  C   GLY A 325     -60.379  13.543  18.615  1.00 88.59           C  
+ANISOU 2515  C   GLY A 325     9443  14352   9866  -2793   3932  -1969       C  
+ATOM   2516  O   GLY A 325     -59.881  12.476  18.972  1.00 98.43           O  
+ANISOU 2516  O   GLY A 325    11015  15378  11006  -3007   4060  -1870       O  
+ATOM   2517  N   LEU A 326     -61.373  14.137  19.267  1.00 82.91           N  
+ANISOU 2517  N   LEU A 326     8444  13920   9139  -2737   4057  -2097       N  
+ATOM   2518  CA  LEU A 326     -61.883  13.633  20.541  1.00 85.44           C  
+ANISOU 2518  CA  LEU A 326     8872  14260   9333  -2876   4280  -2097       C  
+ATOM   2519  C   LEU A 326     -62.347  12.179  20.504  1.00 94.19           C  
+ANISOU 2519  C   LEU A 326    10107  15284  10396  -3250   4394  -2048       C  
+ATOM   2520  O   LEU A 326     -61.937  11.370  21.336  1.00111.99           O  
+ANISOU 2520  O   LEU A 326    12702  17317  12531  -3368   4524  -1929       O  
+ATOM   2521  CB  LEU A 326     -63.039  14.517  21.016  1.00 97.75           C  
+ANISOU 2521  CB  LEU A 326    10066  16138  10937  -2731   4325  -2243       C  
+ATOM   2522  N   GLY A 327     -63.190  11.849  19.537  1.00 84.39           N  
+ANISOU 2522  N   GLY A 327     8594  14220   9250  -3425   4341  -2141       N  
+ATOM   2523  CA  GLY A 327     -63.703  10.500  19.390  1.00 86.61           C  
+ANISOU 2523  CA  GLY A 327     8971  14428   9510  -3791   4446  -2138       C  
+ATOM   2524  C   GLY A 327     -62.808   9.513  18.670  1.00100.05           C  
+ANISOU 2524  C   GLY A 327    10986  15815  11215  -3962   4405  -2041       C  
+ATOM   2525  O   GLY A 327     -63.136   8.330  18.577  1.00 86.92           O  
+ANISOU 2525  O   GLY A 327     9454  14033   9540  -4263   4508  -2041       O  
+ATOM   2526  N   VAL A 328     -61.680   9.991  18.157  1.00 86.08           N  
+ANISOU 2526  N   VAL A 328     9340  13899   9467  -3769   4265  -1965       N  
+ATOM   2527  CA  VAL A 328     -60.809   9.152  17.342  1.00 80.01           C  
+ANISOU 2527  CA  VAL A 328     8839  12846   8714  -3901   4209  -1883       C  
+ATOM   2528  C   VAL A 328     -59.367   9.049  17.847  1.00 85.92           C  
+ANISOU 2528  C   VAL A 328    10013  13246   9385  -3751   4217  -1698       C  
+ATOM   2529  O   VAL A 328     -58.811   7.952  17.914  1.00 88.16           O  
+ANISOU 2529  O   VAL A 328    10643  13223   9632  -3899   4289  -1585       O  
+ATOM   2530  CB  VAL A 328     -60.782   9.673  15.888  1.00 78.57           C  
+ANISOU 2530  CB  VAL A 328     8384  12831   8637  -3848   4002  -1969       C  
+ATOM   2531  CG1 VAL A 328     -59.807   8.870  15.044  1.00 78.68           C  
+ANISOU 2531  CG1 VAL A 328     8683  12548   8663  -3964   3944  -1891       C  
+ATOM   2532  CG2 VAL A 328     -62.176   9.626  15.284  1.00 91.64           C  
+ANISOU 2532  CG2 VAL A 328     9630  14840  10349  -4008   3972  -2144       C  
+ATOM   2533  N   GLY A 329     -58.773  10.181  18.210  1.00 88.08           N  
+ANISOU 2533  N   GLY A 329    10264  13568   9634  -3448   4143  -1675       N  
+ATOM   2534  CA  GLY A 329     -57.359  10.249  18.547  1.00 72.81           C  
+ANISOU 2534  CA  GLY A 329     8703  11312   7650  -3226   4033  -1503       C  
+ATOM   2535  C   GLY A 329     -56.803   9.236  19.537  1.00 75.34           C  
+ANISOU 2535  C   GLY A 329     9432  11381   7814  -3347   4241  -1347       C  
+ATOM   2536  O   GLY A 329     -55.757   8.628  19.283  1.00 72.17           O  
+ANISOU 2536  O   GLY A 329     9346  10678   7397  -3324   4184  -1204       O  
+ATOM   2537  N   SER A 330     -57.494   9.046  20.657  1.00 76.09           N  
+ANISOU 2537  N   SER A 330     9528  11562   7822  -3403   4397  -1347       N  
+ATOM   2538  CA  SER A 330     -56.999   8.189  21.735  1.00 83.21           C  
+ANISOU 2538  CA  SER A 330    10808  12229   8579  -3430   4527  -1164       C  
+ATOM   2539  C   SER A 330     -56.819   6.742  21.277  1.00 90.40           C  
+ANISOU 2539  C   SER A 330    11972  12849   9527  -3666   4596  -1062       C  
+ATOM   2540  O   SER A 330     -55.902   6.039  21.715  1.00 97.71           O  
+ANISOU 2540  O   SER A 330    13267  13489  10368  -3617   4633   -870       O  
+ATOM   2541  CB  SER A 330     -57.961   8.233  22.925  1.00 86.69           C  
+ANISOU 2541  CB  SER A 330    11154  12857   8928  -3477   4690  -1199       C  
+ATOM   2542  OG  SER A 330     -58.516   9.527  23.096  1.00 79.97           O  
+ANISOU 2542  OG  SER A 330     9969  12316   8099  -3311   4640  -1362       O  
+ATOM   2543  N   PHE A 331     -57.687   6.319  20.369  1.00 79.46           N  
+ANISOU 2543  N   PHE A 331    10379  11545   8268  -3907   4606  -1201       N  
+ATOM   2544  CA  PHE A 331     -57.711   4.942  19.902  1.00 81.01           C  
+ANISOU 2544  CA  PHE A 331    10782  11484   8514  -4163   4691  -1163       C  
+ATOM   2545  C   PHE A 331     -56.717   4.745  18.762  1.00 88.70           C  
+ANISOU 2545  C   PHE A 331    11893  12246   9565  -4122   4550  -1130       C  
+ATOM   2546  O   PHE A 331     -56.183   3.651  18.573  1.00101.92           O  
+ANISOU 2546  O   PHE A 331    13875  13598  11252  -4217   4610  -1031       O  
+ATOM   2547  CB  PHE A 331     -59.133   4.569  19.489  1.00 90.05           C  
+ANISOU 2547  CB  PHE A 331    11638  12839   9739  -4456   4768  -1356       C  
+ATOM   2548  CG  PHE A 331     -60.175   5.068  20.451  1.00 97.98           C  
+ANISOU 2548  CG  PHE A 331    12410  14132  10684  -4458   4872  -1425       C  
+ATOM   2549  CD1 PHE A 331     -60.246   4.559  21.737  1.00 88.29           C  
+ANISOU 2549  CD1 PHE A 331    11406  12802   9337  -4481   5056  -1294       C  
+ATOM   2550  CD2 PHE A 331     -61.058   6.070  20.083  1.00101.33           C  
+ANISOU 2550  CD2 PHE A 331    12393  14939  11167  -4413   4786  -1609       C  
+ATOM   2551  CE1 PHE A 331     -61.188   5.025  22.633  1.00 90.44           C  
+ANISOU 2551  CE1 PHE A 331    11469  13346   9548  -4481   5159  -1360       C  
+ATOM   2552  CE2 PHE A 331     -62.005   6.540  20.975  1.00 88.47           C  
+ANISOU 2552  CE2 PHE A 331    10551  13574   9489  -4395   4887  -1676       C  
+ATOM   2553  CZ  PHE A 331     -62.069   6.017  22.252  1.00 90.51           C  
+ANISOU 2553  CZ  PHE A 331    11039  13725   9626  -4438   5077  -1558       C  
+ATOM   2554  N   VAL A 332     -56.474   5.812  18.005  1.00 84.28           N  
+ANISOU 2554  N   VAL A 332    11101  11864   9058  -3969   4371  -1213       N  
+ATOM   2555  CA  VAL A 332     -55.372   5.830  17.052  1.00 75.37           C  
+ANISOU 2555  CA  VAL A 332    10109  10551   7977  -3874   4229  -1158       C  
+ATOM   2556  C   VAL A 332     -54.069   5.619  17.810  1.00 76.93           C  
+ANISOU 2556  C   VAL A 332    10706  10453   8069  -3666   4242   -933       C  
+ATOM   2557  O   VAL A 332     -53.239   4.779  17.439  1.00 89.46           O  
+ANISOU 2557  O   VAL A 332    12585  11732   9674  -3681   4240   -822       O  
+ATOM   2558  CB  VAL A 332     -55.303   7.157  16.266  1.00 76.98           C  
+ANISOU 2558  CB  VAL A 332     9994  11002   8252  -3674   4003  -1259       C  
+ATOM   2559  CG1 VAL A 332     -54.034   7.218  15.427  1.00 67.89           C  
+ANISOU 2559  CG1 VAL A 332     9020   9613   7161  -3481   3775  -1166       C  
+ATOM   2560  CG2 VAL A 332     -56.534   7.329  15.396  1.00 73.54           C  
+ANISOU 2560  CG2 VAL A 332     9147  10890   7903  -3874   3990  -1467       C  
+ATOM   2561  N   ILE A 333     -53.909   6.383  18.888  1.00 79.83           N  
+ANISOU 2561  N   ILE A 333    11078  10933   8322  -3463   4252   -877       N  
+ATOM   2562  CA  ILE A 333     -52.740   6.263  19.751  1.00 78.83           C  
+ANISOU 2562  CA  ILE A 333    11297  10595   8059  -3249   4250   -671       C  
+ATOM   2563  C   ILE A 333     -52.607   4.847  20.304  1.00 84.06           C  
+ANISOU 2563  C   ILE A 333    12289  10973   8676  -3365   4402   -506       C  
+ATOM   2564  O   ILE A 333     -51.529   4.257  20.250  1.00 72.22           O  
+ANISOU 2564  O   ILE A 333    11096   9192   7150  -3257   4373   -339       O  
+ATOM   2565  CB  ILE A 333     -52.794   7.268  20.917  1.00 77.67           C  
+ANISOU 2565  CB  ILE A 333    11069  10656   7784  -3038   4236   -677       C  
+ATOM   2566  CG1 ILE A 333     -52.657   8.697  20.388  1.00 75.22           C  
+ANISOU 2566  CG1 ILE A 333    10470  10520   7590  -2782   3953   -809       C  
+ATOM   2567  CG2 ILE A 333     -51.694   6.980  21.923  1.00 70.44           C  
+ANISOU 2567  CG2 ILE A 333    10512   9563   6691  -2852   4253   -463       C  
+ATOM   2568  CD1 ILE A 333     -52.575   9.747  21.475  1.00 68.54           C  
+ANISOU 2568  CD1 ILE A 333     9562   9839   6640  -2549   3913   -838       C  
+ATOM   2569  N   ASN A 334     -53.703   4.305  20.830  1.00 84.25           N  
+ANISOU 2569  N   ASN A 334    12246  11072   8695  -3572   4567   -553       N  
+ATOM   2570  CA  ASN A 334     -53.692   2.943  21.360  1.00 88.46           C  
+ANISOU 2570  CA  ASN A 334    13082  11335   9194  -3697   4737   -405       C  
+ATOM   2571  C   ASN A 334     -53.245   1.925  20.313  1.00 96.76           C  
+ANISOU 2571  C   ASN A 334    14317  12077  10371  -3815   4733   -392       C  
+ATOM   2572  O   ASN A 334     -52.379   1.080  20.574  1.00106.81           O  
+ANISOU 2572  O   ASN A 334    15934  13038  11609  -3726   4777   -201       O  
+ATOM   2573  CB  ASN A 334     -55.075   2.562  21.890  1.00 87.60           C  
+ANISOU 2573  CB  ASN A 334    12824  11378   9084  -3946   4919   -501       C  
+ATOM   2574  CG  ASN A 334     -55.427   3.281  23.175  1.00 83.03           C  
+ANISOU 2574  CG  ASN A 334    12155  11041   8351  -3822   4973   -469       C  
+ATOM   2575  OD1 ASN A 334     -54.551   3.619  23.971  1.00 82.05           O  
+ANISOU 2575  OD1 ASN A 334    12209  10883   8081  -3574   4929   -312       O  
+ATOM   2576  ND2 ASN A 334     -56.716   3.515  23.388  1.00 85.08           N  
+ANISOU 2576  ND2 ASN A 334    12130  11562   8633  -3991   5066   -628       N  
+ATOM   2577  N   GLY A 335     -53.836   2.021  19.125  1.00 96.81           N  
+ANISOU 2577  N   GLY A 335    14082  12186  10517  -4001   4676   -601       N  
+ATOM   2578  CA  GLY A 335     -53.502   1.138  18.023  1.00 89.50           C  
+ANISOU 2578  CA  GLY A 335    13288  11009   9707  -4131   4667   -641       C  
+ATOM   2579  C   GLY A 335     -52.044   1.215  17.617  1.00 82.61           C  
+ANISOU 2579  C   GLY A 335    12643   9912   8834  -3886   4535   -499       C  
+ATOM   2580  O   GLY A 335     -51.429   0.199  17.291  1.00 87.98           O  
+ANISOU 2580  O   GLY A 335    13602  10267   9558  -3901   4585   -419       O  
+ATOM   2581  N   VAL A 336     -51.488   2.422  17.635  1.00 75.47           N  
+ANISOU 2581  N   VAL A 336    11616   9179   7879  -3653   4373   -476       N  
+ATOM   2582  CA  VAL A 336     -50.075   2.612  17.318  1.00 70.01           C  
+ANISOU 2582  CA  VAL A 336    11122   8306   7171  -3403   4239   -340       C  
+ATOM   2583  C   VAL A 336     -49.188   1.979  18.395  1.00 79.26           C  
+ANISOU 2583  C   VAL A 336    12657   9234   8224  -3207   4305    -85       C  
+ATOM   2584  O   VAL A 336     -48.227   1.257  18.094  1.00 90.78           O  
+ANISOU 2584  O   VAL A 336    14381  10401   9708  -3106   4290     42       O  
+ATOM   2585  CB  VAL A 336     -49.728   4.108  17.172  1.00 67.65           C  
+ANISOU 2585  CB  VAL A 336    10595   8262   6848  -3180   4034   -390       C  
+ATOM   2586  CG1 VAL A 336     -48.224   4.309  17.132  1.00 64.73           C  
+ANISOU 2586  CG1 VAL A 336    10423   7713   6457  -2852   3838   -235       C  
+ATOM   2587  CG2 VAL A 336     -50.377   4.685  15.923  1.00 68.07           C  
+ANISOU 2587  CG2 VAL A 336    10293   8523   7048  -3281   3884   -609       C  
+ATOM   2588  N   LEU A 337     -49.526   2.248  19.652  1.00 79.60           N  
+ANISOU 2588  N   LEU A 337    12698   9416   8131  -3144   4376    -12       N  
+ATOM   2589  CA  LEU A 337     -48.723   1.790  20.780  1.00 83.87           C  
+ANISOU 2589  CA  LEU A 337    13540   9803   8522  -2935   4419    238       C  
+ATOM   2590  C   LEU A 337     -48.723   0.274  20.913  1.00 86.26           C  
+ANISOU 2590  C   LEU A 337    14126   9784   8867  -3043   4588    360       C  
+ATOM   2591  O   LEU A 337     -47.753  -0.306  21.403  1.00 76.90           O  
+ANISOU 2591  O   LEU A 337    13225   8386   7607  -2838   4592    581       O  
+ATOM   2592  CB  LEU A 337     -49.220   2.407  22.087  1.00 87.84           C  
+ANISOU 2592  CB  LEU A 337    13954  10565   8857  -2875   4470    263       C  
+ATOM   2593  CG  LEU A 337     -49.080   3.918  22.258  1.00 82.99           C  
+ANISOU 2593  CG  LEU A 337    13113  10254   8165  -2706   4321    160       C  
+ATOM   2594  CD1 LEU A 337     -49.730   4.364  23.559  1.00 81.36           C  
+ANISOU 2594  CD1 LEU A 337    12820  10293   7800  -2686   4409    154       C  
+ATOM   2595  CD2 LEU A 337     -47.624   4.336  22.201  1.00 69.50           C  
+ANISOU 2595  CD2 LEU A 337    11563   8465   6379  -2410   4148    282       C  
+ATOM   2596  N   GLU A 338     -49.816  -0.363  20.501  1.00 95.09           N  
+ANISOU 2596  N   GLU A 338    15158  10875  10098  -3356   4730    210       N  
+ATOM   2597  CA  GLU A 338     -49.879  -1.822  20.517  1.00 98.67           C  
+ANISOU 2597  CA  GLU A 338    15878  11002  10609  -3486   4910    286       C  
+ATOM   2598  C   GLU A 338     -48.730  -2.431  19.716  1.00 99.19           C  
+ANISOU 2598  C   GLU A 338    16176  10753  10759  -3349   4847    363       C  
+ATOM   2599  O   GLU A 338     -48.115  -3.408  20.141  1.00118.50           O  
+ANISOU 2599  O   GLU A 338    18931  12913  13183  -3236   4943    553       O  
+ATOM   2600  CB  GLU A 338     -51.223  -2.317  19.974  1.00 83.79           C  
+ANISOU 2600  CB  GLU A 338    13828   9164   8843  -3866   5049     56       C  
+ATOM   2601  CG  GLU A 338     -51.337  -3.835  19.926  1.00 89.97           C  
+ANISOU 2601  CG  GLU A 338    14892   9598   9695  -4025   5256     99       C  
+ATOM   2602  CD  GLU A 338     -52.765  -4.315  19.744  1.00107.26           C  
+ANISOU 2602  CD  GLU A 338    16924  11876  11954  -4406   5423   -112       C  
+ATOM   2603  OE1 GLU A 338     -53.687  -3.658  20.272  1.00113.77           O  
+ANISOU 2603  OE1 GLU A 338    17496  13011  12720  -4502   5439   -189       O  
+ATOM   2604  OE2 GLU A 338     -52.964  -5.353  19.077  1.00115.59           O  
+ANISOU 2604  OE2 GLU A 338    18105  12697  13117  -4606   5543   -212       O  
+ATOM   2605  N   GLU A 339     -48.448  -1.846  18.556  1.00 88.86           N  
+ANISOU 2605  N   GLU A 339    14711   9507   9545  -3348   4689    216       N  
+ATOM   2606  CA  GLU A 339     -47.371  -2.330  17.699  1.00 92.26           C  
+ANISOU 2606  CA  GLU A 339    15327   9669  10057  -3219   4621    262       C  
+ATOM   2607  C   GLU A 339     -45.991  -1.775  18.065  1.00103.30           C  
+ANISOU 2607  C   GLU A 339    16846  11047  11356  -2841   4458    469       C  
+ATOM   2608  O   GLU A 339     -44.987  -2.467  17.901  1.00113.50           O  
+ANISOU 2608  O   GLU A 339    18383  12070  12670  -2663   4454    606       O  
+ATOM   2609  CB  GLU A 339     -47.679  -2.001  16.236  1.00 96.25           C  
+ANISOU 2609  CB  GLU A 339    15611  10262  10698  -3401   4528     11       C  
+ATOM   2610  N   LEU A 340     -45.930  -0.541  18.563  1.00101.86           N  
+ANISOU 2610  N   LEU A 340    16486  11156  11061  -2709   4328    480       N  
+ATOM   2611  CA  LEU A 340     -44.625   0.071  18.837  1.00 94.51           C  
+ANISOU 2611  CA  LEU A 340    15641  10243  10026  -2364   4157    641       C  
+ATOM   2612  C   LEU A 340     -43.979  -0.345  20.157  1.00107.09           C  
+ANISOU 2612  C   LEU A 340    17469  11769  11450  -2122   4193    903       C  
+ATOM   2613  O   LEU A 340     -42.753  -0.411  20.253  1.00116.41           O  
+ANISOU 2613  O   LEU A 340    18804  12852  12574  -1839   4086   1067       O  
+ATOM   2614  CB  LEU A 340     -44.721   1.601  18.818  1.00 67.15           C  
+ANISOU 2614  CB  LEU A 340    11904   7115   6496  -2303   4001    531       C  
+ATOM   2615  CG  LEU A 340     -44.533   2.341  17.491  1.00 70.87           C  
+ANISOU 2615  CG  LEU A 340    12156   7666   7107  -2311   3813    356       C  
+ATOM   2616  CD1 LEU A 340     -45.474   1.827  16.428  1.00 77.15           C  
+ANISOU 2616  CD1 LEU A 340    12848   8413   8051  -2651   3930    172       C  
+ATOM   2617  CD2 LEU A 340     -44.686   3.845  17.678  1.00 73.94           C  
+ANISOU 2617  CD2 LEU A 340    12222   8390   7481  -2167   3581    233       C  
+ATOM   2618  N   TYR A 341     -44.791  -0.628  21.169  1.00100.53           N  
+ANISOU 2618  N   TYR A 341    16612   8823  12763   2091    677   -559       N  
+ATOM   2619  CA  TYR A 341     -44.253  -0.971  22.483  1.00100.83           C  
+ANISOU 2619  CA  TYR A 341    17094   8480  12738   2372    277   -383       C  
+ATOM   2620  C   TYR A 341     -43.980  -2.462  22.652  1.00111.63           C  
+ANISOU 2620  C   TYR A 341    19122   9199  14092   2660     55   -422       C  
+ATOM   2621  O   TYR A 341     -43.740  -2.931  23.765  1.00122.69           O  
+ANISOU 2621  O   TYR A 341    21076  10178  15361   2836   -283   -231       O  
+ATOM   2622  CB  TYR A 341     -45.198  -0.489  23.585  1.00100.23           C  
+ANISOU 2622  CB  TYR A 341    17358   8386  12338   1954    321    -90       C  
+ATOM   2623  CG  TYR A 341     -45.096   0.994  23.867  1.00101.56           C  
+ANISOU 2623  CG  TYR A 341    16988   9061  12540   1871    335    -33       C  
+ATOM   2624  CD1 TYR A 341     -44.061   1.753  23.335  1.00101.38           C  
+ANISOU 2624  CD1 TYR A 341    16293   9402  12826   2167    234   -186       C  
+ATOM   2625  CD2 TYR A 341     -46.026   1.633  24.677  1.00103.32           C  
+ANISOU 2625  CD2 TYR A 341    17382   9388  12485   1490    454    160       C  
+ATOM   2626  CE1 TYR A 341     -43.961   3.108  23.593  1.00 91.67           C  
+ANISOU 2626  CE1 TYR A 341    14623   8572  11636   2060    222   -130       C  
+ATOM   2627  CE2 TYR A 341     -45.933   2.987  24.943  1.00 96.34           C  
+ANISOU 2627  CE2 TYR A 341    16056   8911  11637   1442    438    185       C  
+ATOM   2628  CZ  TYR A 341     -44.899   3.719  24.397  1.00 88.85           C  
+ANISOU 2628  CZ  TYR A 341    14490   8262  11006   1717    305     50       C  
+ATOM   2629  OH  TYR A 341     -44.805   5.067  24.658  1.00 79.32           O  
+ANISOU 2629  OH  TYR A 341    12892   7401   9843   1636    267     80       O  
+HETATM 2630  N   MSE A 342     -44.008  -3.203  21.549  1.00104.95           N  
+ANISOU 2630  N   MSE A 342    18261   8251  13364   2722    221   -673       N  
+HETATM 2631  CA  MSE A 342     -43.730  -4.634  21.590  1.00109.94           C  
+ANISOU 2631  CA  MSE A 342    19532   8224  14016   3028      2   -757       C  
+HETATM 2632  C   MSE A 342     -42.229  -4.901  21.625  1.00119.56           C  
+ANISOU 2632  C   MSE A 342    20526   9360  15540   3798   -383   -949       C  
+HETATM 2633  O   MSE A 342     -41.459  -4.110  22.171  1.00116.65           O  
+ANISOU 2633  O   MSE A 342    19745   9286  15290   4050   -604   -890       O  
+HETATM 2634  CB  MSE A 342     -44.363  -5.339  20.389  1.00107.67           C  
+ANISOU 2634  CB  MSE A 342    19342   7838  13728   2800    313   -997       C  
+ATOM   2635  N   THR A 346     -39.695   4.868  23.294  1.00 87.01           N  
+ANISOU 2635  N   THR A 346    12215   8758  12087   3123   -572   -515       N  
+ATOM   2636  CA  THR A 346     -39.685   3.807  22.295  1.00 90.83           C  
+ANISOU 2636  CA  THR A 346    12734   9140  12638   3276   -348   -691       C  
+ATOM   2637  C   THR A 346     -40.517   4.185  21.074  1.00 93.65           C  
+ANISOU 2637  C   THR A 346    12872   9787  12923   2867    160   -732       C  
+ATOM   2638  O   THR A 346     -40.614   3.418  20.116  1.00105.72           O  
+ANISOU 2638  O   THR A 346    14415  11283  14471   2929    393   -900       O  
+ATOM   2639  CB  THR A 346     -40.211   2.483  22.874  1.00 91.84           C  
+ANISOU 2639  CB  THR A 346    13668   8692  12533   3399   -474   -615       C  
+ATOM   2640  N   ILE A 347     -41.113   5.374  21.107  1.00 90.92           N  
+ANISOU 2640  N   ILE A 347    12348   9712  12487   2475    301   -592       N  
+ATOM   2641  CA  ILE A 347     -41.877   5.858  19.967  1.00 93.81           C  
+ANISOU 2641  CA  ILE A 347    12494  10369  12781   2109    717   -613       C  
+ATOM   2642  C   ILE A 347     -40.935   6.561  19.007  1.00 99.50           C  
+ANISOU 2642  C   ILE A 347    12526  11520  13760   2151    837   -739       C  
+ATOM   2643  O   ILE A 347     -40.366   7.607  19.321  1.00 96.40           O  
+ANISOU 2643  O   ILE A 347    11771  11343  13515   2099    699   -674       O  
+ATOM   2644  CB  ILE A 347     -43.010   6.822  20.374  1.00 92.00           C  
+ANISOU 2644  CB  ILE A 347    12395  10222  12340   1696    810   -418       C  
+ATOM   2645  CG1 ILE A 347     -44.107   6.073  21.127  1.00 98.26           C  
+ANISOU 2645  CG1 ILE A 347    13831  10663  12841   1561    823   -312       C  
+ATOM   2646  CG2 ILE A 347     -43.640   7.448  19.143  1.00 84.22           C  
+ANISOU 2646  CG2 ILE A 347    11114   9566  11321   1379   1161   -442       C  
+ATOM   2647  CD1 ILE A 347     -45.234   6.970  21.599  1.00 89.42           C  
+ANISOU 2647  CD1 ILE A 347    12807   9653  11517   1203    930   -166       C  
+ATOM   2648  N   ASP A 348     -40.779   5.970  17.830  1.00103.27           N  
+ANISOU 2648  N   ASP A 348    12847  12118  14272   2218   1108   -928       N  
+ATOM   2649  CA  ASP A 348     -40.025   6.586  16.754  1.00103.46           C  
+ANISOU 2649  CA  ASP A 348    12252  12594  14464   2183   1331  -1046       C  
+ATOM   2650  C   ASP A 348     -40.816   7.807  16.308  1.00103.68           C  
+ANISOU 2650  C   ASP A 348    12167  12878  14349   1709   1531   -863       C  
+ATOM   2651  O   ASP A 348     -42.043   7.760  16.216  1.00109.21           O  
+ANISOU 2651  O   ASP A 348    13223  13467  14805   1460   1645   -770       O  
+ATOM   2652  CB  ASP A 348     -39.796   5.599  15.605  1.00104.60           C  
+ANISOU 2652  CB  ASP A 348    12345  12796  14602   2369   1600  -1313       C  
+ATOM   2653  CG  ASP A 348     -38.733   6.072  14.629  1.00108.88           C  
+ANISOU 2653  CG  ASP A 348    12218  13820  15331   2423   1825  -1475       C  
+ATOM   2654  OD1 ASP A 348     -38.536   7.297  14.499  1.00104.44           O  
+ANISOU 2654  OD1 ASP A 348    11283  13576  14823   2132   1885  -1326       O  
+ATOM   2655  OD2 ASP A 348     -38.085   5.211  13.996  1.00112.67           O  
+ANISOU 2655  OD2 ASP A 348    12556  14354  15900   2751   1952  -1759       O  
+ATOM   2656  N   ASP A 349     -40.114   8.898  16.029  1.00105.62           N  
+ANISOU 2656  N   ASP A 349    11914  13458  14757   1582   1557   -815       N  
+ATOM   2657  CA  ASP A 349     -40.766  10.175  15.767  1.00101.82           C  
+ANISOU 2657  CA  ASP A 349    11368  13150  14169   1168   1654   -612       C  
+ATOM   2658  C   ASP A 349     -41.335  10.239  14.367  1.00 93.47           C  
+ANISOU 2658  C   ASP A 349    10271  12325  12919    934   2027   -633       C  
+ATOM   2659  O   ASP A 349     -42.182  11.081  14.065  1.00 86.56           O  
+ANISOU 2659  O   ASP A 349     9479  11522  11887    621   2097   -469       O  
+ATOM   2660  CB  ASP A 349     -39.773  11.321  15.950  1.00103.53           C  
+ANISOU 2660  CB  ASP A 349    11110  13594  14632   1073   1532   -540       C  
+ATOM   2661  CG  ASP A 349     -39.179  11.359  17.332  1.00110.07           C  
+ANISOU 2661  CG  ASP A 349    11962  14220  15641   1292   1110   -531       C  
+ATOM   2662  OD1 ASP A 349     -39.547  12.280  18.082  1.00110.35           O  
+ANISOU 2662  OD1 ASP A 349    12122  14159  15646   1112    910   -371       O  
+ATOM   2663  OD2 ASP A 349     -38.351  10.484  17.668  1.00109.48           O  
+ANISOU 2663  OD2 ASP A 349    11797  14074  15727   1665    955   -696       O  
+ATOM   2664  N   ASP A 350     -40.873   9.337  13.514  1.00 87.50           N  
+ANISOU 2664  N   ASP A 350     9410  11678  12159   1115   2242   -853       N  
+ATOM   2665  CA  ASP A 350     -41.344   9.312  12.145  1.00 85.30           C  
+ANISOU 2665  CA  ASP A 350     9124  11633  11651    914   2587   -904       C  
+ATOM   2666  C   ASP A 350     -42.584   8.456  11.969  1.00 92.39           C  
+ANISOU 2666  C   ASP A 350    10514  12293  12297    873   2633   -960       C  
+ATOM   2667  O   ASP A 350     -43.140   8.404  10.882  1.00109.58           O  
+ANISOU 2667  O   ASP A 350    12749  14636  14249    696   2865  -1007       O  
+ATOM   2668  CB  ASP A 350     -40.231   8.772  11.244  1.00 88.82           C  
+ANISOU 2668  CB  ASP A 350     9208  12355  12185   1124   2836  -1160       C  
+ATOM   2669  CG  ASP A 350     -38.913   9.476  11.475  1.00 97.82           C  
+ANISOU 2669  CG  ASP A 350     9787  13754  13624   1169   2794  -1149       C  
+ATOM   2670  OD1 ASP A 350     -38.909  10.725  11.469  1.00111.92           O  
+ANISOU 2670  OD1 ASP A 350    11396  15701  15429    831   2783   -917       O  
+ATOM   2671  OD2 ASP A 350     -37.887   8.784  11.661  1.00 91.08           O  
+ANISOU 2671  OD2 ASP A 350     8669  12934  13004   1543   2752  -1381       O  
+ATOM   2672  N   ARG A 351     -43.048   7.821  13.040  1.00 77.80           N  
+ANISOU 2672  N   ARG A 351     9032  10063  10466    998   2406   -942       N  
+ATOM   2673  CA  ARG A 351     -44.191   6.924  12.912  1.00 71.77           C  
+ANISOU 2673  CA  ARG A 351     8722   9059   9488    913   2459  -1005       C  
+ATOM   2674  C   ARG A 351     -45.515   7.555  13.333  1.00 72.60           C  
+ANISOU 2674  C   ARG A 351     9034   9114   9437    587   2404   -805       C  
+ATOM   2675  O   ARG A 351     -46.547   7.326  12.704  1.00 73.97           O  
+ANISOU 2675  O   ARG A 351     9376   9317   9412    372   2531   -840       O  
+ATOM   2676  CB  ARG A 351     -43.942   5.645  13.711  1.00 70.26           C  
+ANISOU 2676  CB  ARG A 351     8872   8450   9374   1222   2290  -1124       C  
+ATOM   2677  CG  ARG A 351     -42.615   4.986  13.368  1.00 73.69           C  
+ANISOU 2677  CG  ARG A 351     9079   8917  10002   1634   2302  -1363       C  
+ATOM   2678  CD  ARG A 351     -42.501   4.694  11.878  1.00 72.07           C  
+ANISOU 2678  CD  ARG A 351     8713   8987   9684   1614   2632  -1592       C  
+ATOM   2679  NE  ARG A 351     -43.595   3.878  11.363  1.00 71.04           N  
+ANISOU 2679  NE  ARG A 351     9024   8658   9311   1454   2735  -1691       N  
+ATOM   2680  CZ  ARG A 351     -43.620   2.551  11.406  1.00 74.04           C  
+ANISOU 2680  CZ  ARG A 351     9782   8664   9685   1682   2685  -1903       C  
+ATOM   2681  NH1 ARG A 351     -42.604   1.886  11.938  1.00 77.98           N  
+ANISOU 2681  NH1 ARG A 351    10278   8942  10407   2135   2519  -2035       N  
+ATOM   2682  NH2 ARG A 351     -44.656   1.890  10.910  1.00 73.16           N  
+ANISOU 2682  NH2 ARG A 351    10056   8383   9357   1460   2772  -1992       N  
+ATOM   2683  N   LEU A 352     -45.481   8.351  14.396  1.00 75.45           N  
+ANISOU 2683  N   LEU A 352     9362   9415   9890    566   2203   -623       N  
+ATOM   2684  CA  LEU A 352     -46.687   9.000  14.895  1.00 60.12           C  
+ANISOU 2684  CA  LEU A 352     7580   7445   7819    313   2155   -469       C  
+ATOM   2685  C   LEU A 352     -46.397  10.432  15.314  1.00 64.41           C  
+ANISOU 2685  C   LEU A 352     7878   8127   8467    248   2020   -300       C  
+ATOM   2686  O   LEU A 352     -45.592  10.675  16.212  1.00 75.32           O  
+ANISOU 2686  O   LEU A 352     9200   9412  10005    406   1821   -258       O  
+ATOM   2687  CB  LEU A 352     -47.279   8.218  16.070  1.00 62.37           C  
+ANISOU 2687  CB  LEU A 352     8282   7383   8032    344   2041   -451       C  
+ATOM   2688  CG  LEU A 352     -48.523   8.823  16.728  1.00 62.80           C  
+ANISOU 2688  CG  LEU A 352     8473   7436   7951    104   2027   -329       C  
+ATOM   2689  CD1 LEU A 352     -49.633   9.029  15.707  1.00 59.18           C  
+ANISOU 2689  CD1 LEU A 352     7934   7191   7360   -157   2205   -368       C  
+ATOM   2690  CD2 LEU A 352     -49.008   7.957  17.882  1.00 63.01           C  
+ANISOU 2690  CD2 LEU A 352     8933   7141   7869    101   1970   -306       C  
+ATOM   2691  N   ILE A 353     -47.062  11.377  14.661  1.00 64.24           N  
+ANISOU 2691  N   ILE A 353     7741   8309   8359     22   2093   -210       N  
+ATOM   2692  CA  ILE A 353     -46.933  12.781  15.019  1.00 55.83           C  
+ANISOU 2692  CA  ILE A 353     6515   7315   7382    -62   1948    -49       C  
+ATOM   2693  C   ILE A 353     -48.295  13.317  15.438  1.00 60.32           C  
+ANISOU 2693  C   ILE A 353     7256   7839   7822   -194   1895     15       C  
+ATOM   2694  O   ILE A 353     -49.240  13.342  14.645  1.00 64.03           O  
+ANISOU 2694  O   ILE A 353     7747   8433   8150   -335   2005      1       O  
+ATOM   2695  CB  ILE A 353     -46.364  13.617  13.858  1.00 63.37           C  
+ANISOU 2695  CB  ILE A 353     7175   8535   8369   -195   2050     25       C  
+ATOM   2696  CG1 ILE A 353     -44.861  13.370  13.720  1.00 66.07           C  
+ANISOU 2696  CG1 ILE A 353     7237   8965   8900    -64   2085    -40       C  
+ATOM   2697  CG2 ILE A 353     -46.660  15.098  14.060  1.00 60.82           C  
+ANISOU 2697  CG2 ILE A 353     6802   8224   8081   -347   1896    207       C  
+ATOM   2698  CD1 ILE A 353     -44.060  13.813  14.924  1.00 71.10           C  
+ANISOU 2698  CD1 ILE A 353     7778   9469   9769     51   1821      3       C  
+ATOM   2699  N   LEU A 354     -48.392  13.729  16.696  1.00 59.56           N  
+ANISOU 2699  N   LEU A 354     7273   7585   7771   -130   1716     61       N  
+ATOM   2700  CA  LEU A 354     -49.646  14.220  17.247  1.00 54.35           C  
+ANISOU 2700  CA  LEU A 354     6750   6901   6997   -210   1686     78       C  
+ATOM   2701  C   LEU A 354     -49.702  15.741  17.288  1.00 53.53           C  
+ANISOU 2701  C   LEU A 354     6521   6846   6972   -246   1530    179       C  
+ATOM   2702  O   LEU A 354     -48.785  16.400  17.780  1.00 58.65           O  
+ANISOU 2702  O   LEU A 354     7102   7417   7764   -189   1356    238       O  
+ATOM   2703  CB  LEU A 354     -49.862  13.649  18.648  1.00 60.71           C  
+ANISOU 2703  CB  LEU A 354     7833   7500   7733   -123   1625     42       C  
+ATOM   2704  CG  LEU A 354     -50.008  12.128  18.710  1.00 56.41           C  
+ANISOU 2704  CG  LEU A 354     7520   6827   7087   -118   1759    -36       C  
+ATOM   2705  CD1 LEU A 354     -49.649  11.602  20.090  1.00 59.92           C  
+ANISOU 2705  CD1 LEU A 354     8267   7018   7480     14   1629    -15       C  
+ATOM   2706  CD2 LEU A 354     -51.421  11.719  18.324  1.00 50.65           C  
+ANISOU 2706  CD2 LEU A 354     6864   6184   6199   -324   1954   -100       C  
+ATOM   2707  N   ARG A 355     -50.792  16.290  16.766  1.00 51.44           N  
+ANISOU 2707  N   ARG A 355     6231   6694   6622   -337   1564    187       N  
+ATOM   2708  CA  ARG A 355     -51.009  17.729  16.781  1.00 57.29           C  
+ANISOU 2708  CA  ARG A 355     6915   7426   7428   -340   1388    273       C  
+ATOM   2709  C   ARG A 355     -52.379  18.075  17.353  1.00 59.11           C  
+ANISOU 2709  C   ARG A 355     7222   7664   7571   -291   1364    185       C  
+ATOM   2710  O   ARG A 355     -53.266  18.504  16.614  1.00 54.70           O  
+ANISOU 2710  O   ARG A 355     6586   7231   6967   -323   1359    183       O  
+ATOM   2711  CB  ARG A 355     -50.876  18.306  15.370  1.00 59.99           C  
+ANISOU 2711  CB  ARG A 355     7124   7905   7766   -461   1403    391       C  
+ATOM   2712  CG  ARG A 355     -49.485  18.186  14.776  1.00 57.74           C  
+ANISOU 2712  CG  ARG A 355     6704   7666   7569   -534   1463    473       C  
+ATOM   2713  CD  ARG A 355     -48.518  19.145  15.448  1.00 57.78           C  
+ANISOU 2713  CD  ARG A 355     6654   7530   7771   -537   1264    565       C  
+ATOM   2714  NE  ARG A 355     -47.174  19.048  14.885  1.00 58.29           N  
+ANISOU 2714  NE  ARG A 355     6507   7693   7949   -633   1344    624       N  
+ATOM   2715  CZ  ARG A 355     -46.785  19.658  13.770  1.00 72.79           C  
+ANISOU 2715  CZ  ARG A 355     8231   9660   9768   -831   1423    769       C  
+ATOM   2716  NH1 ARG A 355     -47.638  20.411  13.089  1.00 75.50           N  
+ANISOU 2716  NH1 ARG A 355     8702  10007   9977   -927   1379    888       N  
+ATOM   2717  NH2 ARG A 355     -45.542  19.512  13.333  1.00 74.93           N  
+ANISOU 2717  NH2 ARG A 355     8259  10068  10143   -929   1546    792       N  
+ATOM   2718  N   PRO A 356     -52.564  17.874  18.670  1.00 69.05           N  
+ANISOU 2718  N   PRO A 356     8629   8813   8793   -202   1349    100       N  
+ATOM   2719  CA  PRO A 356     -53.835  18.256  19.293  1.00 57.81           C  
+ANISOU 2719  CA  PRO A 356     7239   7443   7283   -147   1369    -17       C  
+ATOM   2720  C   PRO A 356     -54.065  19.757  19.169  1.00 62.62           C  
+ANISOU 2720  C   PRO A 356     7785   8014   7992    -43   1150      6       C  
+ATOM   2721  O   PRO A 356     -53.110  20.531  19.237  1.00 77.14           O  
+ANISOU 2721  O   PRO A 356     9657   9695   9955    -20    955    109       O  
+ATOM   2722  CB  PRO A 356     -53.657  17.836  20.756  1.00 57.52           C  
+ANISOU 2722  CB  PRO A 356     7425   7277   7154    -81   1387    -82       C  
+ATOM   2723  CG  PRO A 356     -52.184  17.791  20.964  1.00 63.16           C  
+ANISOU 2723  CG  PRO A 356     8199   7825   7976    -39   1228     18       C  
+ATOM   2724  CD  PRO A 356     -51.605  17.344  19.656  1.00 71.21           C  
+ANISOU 2724  CD  PRO A 356     9047   8925   9084   -133   1298    101       C  
+ATOM   2725  N   PHE A 357     -55.316  20.162  18.993  1.00 62.61           N  
+ANISOU 2725  N   PHE A 357     7691   8145   7955     19   1164    -97       N  
+ATOM   2726  CA  PHE A 357     -55.633  21.567  18.777  1.00 68.52           C  
+ANISOU 2726  CA  PHE A 357     8410   8821   8803    165    922    -84       C  
+ATOM   2727  C   PHE A 357     -55.665  22.347  20.082  1.00 72.44           C  
+ANISOU 2727  C   PHE A 357     9048   9155   9322    349    797   -204       C  
+ATOM   2728  O   PHE A 357     -56.243  21.892  21.069  1.00 71.59           O  
+ANISOU 2728  O   PHE A 357     8980   9128   9091    404    957   -374       O  
+ATOM   2729  CB  PHE A 357     -56.976  21.706  18.059  1.00 69.19           C  
+ANISOU 2729  CB  PHE A 357     8312   9120   8859    222    936   -178       C  
+ATOM   2730  CG  PHE A 357     -56.925  21.341  16.605  1.00 70.38           C  
+ANISOU 2730  CG  PHE A 357     8370   9394   8976     72    947    -47       C  
+ATOM   2731  CD1 PHE A 357     -56.859  20.015  16.211  1.00 61.91           C  
+ANISOU 2731  CD1 PHE A 357     7254   8466   7802   -118   1182    -65       C  
+ATOM   2732  CD2 PHE A 357     -56.945  22.325  15.632  1.00 78.20           C  
+ANISOU 2732  CD2 PHE A 357     9369  10333  10012    121    709     92       C  
+ATOM   2733  CE1 PHE A 357     -56.811  19.677  14.875  1.00 62.47           C  
+ANISOU 2733  CE1 PHE A 357     7271   8660   7806   -246   1194     21       C  
+ATOM   2734  CE2 PHE A 357     -56.898  21.993  14.294  1.00 72.84           C  
+ANISOU 2734  CE2 PHE A 357     8651   9786   9240    -24    723    213       C  
+ATOM   2735  CZ  PHE A 357     -56.832  20.666  13.916  1.00 66.31           C  
+ANISOU 2735  CZ  PHE A 357     7759   9135   8300   -202    973    161       C  
+ATOM   2736  N   PRO A 358     -55.041  23.534  20.088  1.00 77.46           N  
+ANISOU 2736  N   PRO A 358     9785   9552  10093    420    516   -120       N  
+ATOM   2737  CA  PRO A 358     -55.108  24.414  21.256  1.00 81.25           C  
+ANISOU 2737  CA  PRO A 358    10432   9846  10594    616    349   -268       C  
+ATOM   2738  C   PRO A 358     -56.490  25.045  21.394  1.00 79.77           C  
+ANISOU 2738  C   PRO A 358    10171   9749  10390    867    329   -478       C  
+ATOM   2739  O   PRO A 358     -57.014  25.611  20.435  1.00 81.66           O  
+ANISOU 2739  O   PRO A 358    10308  10004  10716    937    198   -427       O  
+ATOM   2740  CB  PRO A 358     -54.038  25.470  20.961  1.00 81.23           C  
+ANISOU 2740  CB  PRO A 358    10549   9545  10772    557     39    -97       C  
+ATOM   2741  CG  PRO A 358     -53.952  25.507  19.475  1.00 81.94           C  
+ANISOU 2741  CG  PRO A 358    10515   9701  10916    404     38    120       C  
+ATOM   2742  CD  PRO A 358     -54.209  24.100  19.011  1.00 80.15           C  
+ANISOU 2742  CD  PRO A 358    10120   9775  10558    286    351    117       C  
+ATOM   2743  N   GLN A 359     -57.070  24.941  22.585  1.00 78.60           N  
+ANISOU 2743  N   GLN A 359    10075   9673  10116   1016    455   -722       N  
+ATOM   2744  CA  GLN A 359     -58.411  25.454  22.827  1.00 82.13           C  
+ANISOU 2744  CA  GLN A 359    10385  10272  10548   1282    491   -983       C  
+ATOM   2745  C   GLN A 359     -58.355  26.882  23.354  1.00 80.48           C  
+ANISOU 2745  C   GLN A 359    10369   9769  10442   1573    176  -1113       C  
+ATOM   2746  O   GLN A 359     -57.414  27.262  24.050  1.00 80.49           O  
+ANISOU 2746  O   GLN A 359    10640   9501  10443   1550     18  -1084       O  
+ATOM   2747  CB  GLN A 359     -59.162  24.551  23.807  1.00 84.28           C  
+ANISOU 2747  CB  GLN A 359    10590  10833  10599   1261    865  -1200       C  
+ATOM   2748  CG  GLN A 359     -59.204  23.089  23.387  1.00 76.71           C  
+ANISOU 2748  CG  GLN A 359     9514  10096   9536    947   1164  -1080       C  
+ATOM   2749  CD  GLN A 359     -59.845  22.885  22.027  1.00 79.59           C  
+ANISOU 2749  CD  GLN A 359     9578  10651  10011    879   1163  -1022       C  
+ATOM   2750  OE1 GLN A 359     -60.806  23.567  21.669  1.00 82.06           O  
+ANISOU 2750  OE1 GLN A 359     9673  11090  10418   1088   1068  -1171       O  
+ATOM   2751  NE2 GLN A 359     -59.309  21.944  21.257  1.00 81.01           N  
+ANISOU 2751  NE2 GLN A 359     9753  10850  10176    613   1243   -826       N  
+ATOM   2752  N   GLY A 360     -59.369  27.670  23.015  1.00 84.43           N  
+ANISOU 2752  N   GLY A 360    10732  10307  11041   1862     53  -1273       N  
+ATOM   2753  CA  GLY A 360     -59.409  29.066  23.406  1.00 88.06           C  
+ANISOU 2753  CA  GLY A 360    11400  10439  11620   2184   -281  -1416       C  
+ATOM   2754  C   GLY A 360     -59.391  29.954  22.180  1.00 87.49           C  
+ANISOU 2754  C   GLY A 360    11360  10125  11755   2254   -642  -1217       C  
+ATOM   2755  O   GLY A 360     -59.225  29.469  21.061  1.00101.56           O  
+ANISOU 2755  O   GLY A 360    13021  12013  13555   2024   -616   -955       O  
+ATOM   2756  N   LYS A 361     -59.569  31.255  22.387  1.00 83.93           N  
+ANISOU 2756  N   LYS A 361    11119   9333  11439   2575   -986  -1343       N  
+ATOM   2757  CA  LYS A 361     -59.625  32.209  21.285  1.00 86.32           C  
+ANISOU 2757  CA  LYS A 361    11541   9338  11920   2675  -1376  -1146       C  
+ATOM   2758  C   LYS A 361     -58.310  32.263  20.510  1.00 93.58           C  
+ANISOU 2758  C   LYS A 361    12676   9993  12885   2245  -1509   -712       C  
+ATOM   2759  O   LYS A 361     -58.307  32.201  19.280  1.00 95.85           O  
+ANISOU 2759  O   LYS A 361    12919  10313  13187   2101  -1581   -438       O  
+ATOM   2760  CB  LYS A 361     -59.982  33.603  21.806  1.00 88.64           C  
+ANISOU 2760  CB  LYS A 361    12099   9229  12352   3114  -1743  -1384       C  
+ATOM   2761  N   LYS A 362     -57.200  32.361  21.236  1.00102.06           N  
+ANISOU 2761  N   LYS A 362    13968  10840  13969   2034  -1535   -665       N  
+ATOM   2762  CA  LYS A 362     -55.876  32.458  20.624  1.00100.68           C  
+ANISOU 2762  CA  LYS A 362    13942  10444  13868   1608  -1641   -295       C  
+ATOM   2763  C   LYS A 362     -55.515  31.235  19.779  1.00 95.36           C  
+ANISOU 2763  C   LYS A 362    13004  10140  13090   1272  -1326    -60       C  
+ATOM   2764  O   LYS A 362     -54.832  31.358  18.762  1.00100.64           O  
+ANISOU 2764  O   LYS A 362    13718  10722  13797    983  -1388    263       O  
+ATOM   2765  CB  LYS A 362     -54.812  32.670  21.704  1.00 90.13           C  
+ANISOU 2765  CB  LYS A 362    12804   8872  12570   1466  -1723   -361       C  
+ATOM   2766  N   GLY A 363     -55.967  30.058  20.205  1.00 84.04           N  
+ANISOU 2766  N   GLY A 363    11319   9104  11509   1298   -979   -226       N  
+ATOM   2767  CA  GLY A 363     -55.738  28.837  19.452  1.00 84.14           C  
+ANISOU 2767  CA  GLY A 363    11106   9444  11418   1026   -686    -60       C  
+ATOM   2768  C   GLY A 363     -56.538  28.821  18.163  1.00 88.78           C  
+ANISOU 2768  C   GLY A 363    11563  10192  11976   1061   -709     48       C  
+ATOM   2769  O   GLY A 363     -56.004  28.576  17.072  1.00 99.23           O  
+ANISOU 2769  O   GLY A 363    12877  11559  13268    802   -682    317       O  
+ATOM   2770  N   GLU A 364     -57.830  29.110  18.289  1.00 86.88           N  
+ANISOU 2770  N   GLU A 364    11215  10058  11737   1397   -770   -183       N  
+ATOM   2771  CA  GLU A 364     -58.719  29.115  17.138  1.00 88.45           C  
+ANISOU 2771  CA  GLU A 364    11268  10430  11909   1486   -855   -126       C  
+ATOM   2772  C   GLU A 364     -58.330  30.202  16.153  1.00 95.07           C  
+ANISOU 2772  C   GLU A 364    12386  10922  12813   1462  -1224    170       C  
+ATOM   2773  O   GLU A 364     -58.709  30.142  14.984  1.00104.85           O  
+ANISOU 2773  O   GLU A 364    13589  12273  13974   1428  -1313    330       O  
+ATOM   2774  CB  GLU A 364     -60.169  29.326  17.565  1.00 90.57           C  
+ANISOU 2774  CB  GLU A 364    11315  10884  12212   1896   -888   -474       C  
+ATOM   2775  CG  GLU A 364     -60.719  28.267  18.485  1.00 97.57           C  
+ANISOU 2775  CG  GLU A 364    11923  12148  13003   1881   -488   -759       C  
+ATOM   2776  CD  GLU A 364     -62.192  28.469  18.763  1.00104.32           C  
+ANISOU 2776  CD  GLU A 364    12470  13264  13902   2251   -484  -1110       C  
+ATOM   2777  OE1 GLU A 364     -62.863  29.145  17.954  1.00106.27           O  
+ANISOU 2777  OE1 GLU A 364    12645  13485  14247   2501   -791  -1109       O  
+ATOM   2778  OE2 GLU A 364     -62.679  27.949  19.788  1.00 99.58           O  
+ANISOU 2778  OE2 GLU A 364    11697  12910  13231   2292   -175  -1388       O  
+ATOM   2779  N   GLU A 365     -57.597  31.210  16.620  1.00101.22           N  
+ANISOU 2779  N   GLU A 365    13477  11266  13716   1462  -1459    246       N  
+ATOM   2780  CA  GLU A 365     -57.128  32.237  15.699  1.00107.24           C  
+ANISOU 2780  CA  GLU A 365    14566  11650  14528   1353  -1793    575       C  
+ATOM   2781  C   GLU A 365     -56.160  31.648  14.686  1.00 99.83           C  
+ANISOU 2781  C   GLU A 365    13622  10841  13468    878  -1606    926       C  
+ATOM   2782  O   GLU A 365     -56.118  32.089  13.539  1.00102.08           O  
+ANISOU 2782  O   GLU A 365    14088  11024  13675    763  -1772   1214       O  
+ATOM   2783  CB  GLU A 365     -56.432  33.388  16.441  1.00110.03           C  
+ANISOU 2783  CB  GLU A 365    15271  11481  15053   1364  -2071    586       C  
+ATOM   2784  CG  GLU A 365     -57.337  34.259  17.295  1.00110.94           C  
+ANISOU 2784  CG  GLU A 365    15498  11364  15289   1874  -2336    249       C  
+ATOM   2785  CD  GLU A 365     -56.616  35.463  17.886  1.00115.61           C  
+ANISOU 2785  CD  GLU A 365    16512  11368  16046   1857  -2668    272       C  
+ATOM   2786  OE1 GLU A 365     -55.366  35.476  17.893  1.00114.76           O  
+ANISOU 2786  OE1 GLU A 365    16528  11103  15972   1416  -2634    501       O  
+ATOM   2787  OE2 GLU A 365     -57.303  36.405  18.336  1.00116.87           O  
+ANISOU 2787  OE2 GLU A 365    16868  11222  16314   2290  -2974     41       O  
+ATOM   2788  N   GLN A 366     -55.443  30.599  15.080  1.00 93.00           N  
+ANISOU 2788  N   GLN A 366    12552  10224  12560    630  -1254    887       N  
+ATOM   2789  CA  GLN A 366     -54.428  30.033  14.202  1.00 92.13           C  
+ANISOU 2789  CA  GLN A 366    12403  10249  12353    211  -1048   1167       C  
+ATOM   2790  C   GLN A 366     -54.656  28.540  13.931  1.00 87.41           C  
+ANISOU 2790  C   GLN A 366    11497  10116  11598    143   -676   1062       C  
+ATOM   2791  O   GLN A 366     -53.734  27.827  13.511  1.00 85.60           O  
+ANISOU 2791  O   GLN A 366    11179  10040  11306   -153   -435   1189       O  
+ATOM   2792  CB  GLN A 366     -53.027  30.232  14.805  1.00 91.62           C  
+ANISOU 2792  CB  GLN A 366    12399   9988  12425    -68  -1016   1255       C  
+ATOM   2793  CG  GLN A 366     -52.598  31.684  15.087  1.00104.65           C  
+ANISOU 2793  CG  GLN A 366    14383  11131  14249   -105  -1384   1370       C  
+ATOM   2794  CD  GLN A 366     -52.569  32.581  13.859  1.00117.15           C  
+ANISOU 2794  CD  GLN A 366    16249  12484  15779   -269  -1596   1719       C  
+ATOM   2795  OE1 GLN A 366     -53.534  33.288  13.574  1.00116.60           O  
+ANISOU 2795  OE1 GLN A 366    16387  12224  15691     22  -1881   1714       O  
+ATOM   2796  NE2 GLN A 366     -51.468  32.545  13.120  1.00117.09           N  
+ANISOU 2796  NE2 GLN A 366    16251  12505  15732   -729  -1454   2020       N  
+ATOM   2797  N   TRP A 367     -55.884  28.074  14.149  1.00 89.18           N  
+ANISOU 2797  N   TRP A 367    11551  10562  11771    411   -632    814       N  
+ATOM   2798  CA  TRP A 367     -56.235  26.676  13.876  1.00 89.67           C  
+ANISOU 2798  CA  TRP A 367    11356  11022  11691    326   -312    701       C  
+ATOM   2799  C   TRP A 367     -56.053  26.284  12.410  1.00 93.33           C  
+ANISOU 2799  C   TRP A 367    11827  11659  11976    104   -249    915       C  
+ATOM   2800  O   TRP A 367     -55.716  25.138  12.107  1.00101.28           O  
+ANISOU 2800  O   TRP A 367    12702  12906  12873    -81     40    890       O  
+ATOM   2801  CB  TRP A 367     -57.683  26.392  14.281  1.00 91.08           C  
+ANISOU 2801  CB  TRP A 367    11332  11413  11862    609   -303    403       C  
+ATOM   2802  CG  TRP A 367     -57.857  25.913  15.685  1.00 89.19           C  
+ANISOU 2802  CG  TRP A 367    10990  11229  11671    704   -108    138       C  
+ATOM   2803  CD1 TRP A 367     -56.894  25.807  16.645  1.00 87.21           C  
+ANISOU 2803  CD1 TRP A 367    10853  10819  11465    615    -19    139       C  
+ATOM   2804  CD2 TRP A 367     -59.076  25.468  16.288  1.00 88.86           C  
+ANISOU 2804  CD2 TRP A 367    10717  11437  11608    886     23   -164       C  
+ATOM   2805  NE1 TRP A 367     -57.439  25.325  17.811  1.00 84.68           N  
+ANISOU 2805  NE1 TRP A 367    10450  10614  11112    739    154   -124       N  
+ATOM   2806  CE2 TRP A 367     -58.779  25.109  17.617  1.00 91.68           C  
+ANISOU 2806  CE2 TRP A 367    11114  11762  11959    886    214   -312       C  
+ATOM   2807  CE3 TRP A 367     -60.391  25.340  15.832  1.00 87.23           C  
+ANISOU 2807  CE3 TRP A 367    10256  11503  11384   1036     -6   -329       C  
+ATOM   2808  CZ2 TRP A 367     -59.749  24.631  18.495  1.00 93.25           C  
+ANISOU 2808  CZ2 TRP A 367    11137  12191  12105    998    426   -598       C  
+ATOM   2809  CZ3 TRP A 367     -61.351  24.866  16.703  1.00 83.73           C  
+ANISOU 2809  CZ3 TRP A 367     9566  11308  10937   1145    203   -638       C  
+ATOM   2810  CH2 TRP A 367     -61.026  24.517  18.019  1.00 87.93           C  
+ANISOU 2810  CH2 TRP A 367    10172  11802  11433   1110    442   -761       C  
+ATOM   2811  N   ASP A 368     -56.285  27.229  11.504  1.00 90.70           N  
+ANISOU 2811  N   ASP A 368    11688  11185  11589    136   -532   1118       N  
+ATOM   2812  CA  ASP A 368     -56.187  26.952  10.074  1.00 91.08           C  
+ANISOU 2812  CA  ASP A 368    11804  11403  11401    -64   -498   1329       C  
+ATOM   2813  C   ASP A 368     -54.740  26.681   9.674  1.00 86.99           C  
+ANISOU 2813  C   ASP A 368    11348  10886  10819   -438   -251   1547       C  
+ATOM   2814  O   ASP A 368     -54.440  25.672   9.027  1.00 83.64           O  
+ANISOU 2814  O   ASP A 368    10812  10744  10222   -615     26   1538       O  
+ATOM   2815  CB  ASP A 368     -56.752  28.118   9.261  1.00101.49           C  
+ANISOU 2815  CB  ASP A 368    13391  12522  12650     71   -905   1529       C  
+ATOM   2816  CG  ASP A 368     -56.817  27.817   7.775  1.00106.75           C  
+ANISOU 2816  CG  ASP A 368    14165  13393  13001   -107   -901   1730       C  
+ATOM   2817  OD1 ASP A 368     -57.659  26.987   7.372  1.00 99.11           O  
+ANISOU 2817  OD1 ASP A 368    13000  12750  11906    -22   -851   1547       O  
+ATOM   2818  OD2 ASP A 368     -56.028  28.409   7.009  1.00106.74           O  
+ANISOU 2818  OD2 ASP A 368    14459  13235  12861   -358   -943   2068       O  
+ATOM   2819  N   LYS A 369     -53.848  27.583  10.074  1.00 85.52           N  
+ANISOU 2819  N   LYS A 369    11320  10389  10783   -555   -353   1714       N  
+ATOM   2820  CA  LYS A 369     -52.423  27.425   9.816  1.00 83.91           C  
+ANISOU 2820  CA  LYS A 369    11100  10205  10578   -918   -120   1895       C  
+ATOM   2821  C   LYS A 369     -51.919  26.162  10.501  1.00 85.01           C  
+ANISOU 2821  C   LYS A 369    10941  10572  10787   -932    204   1663       C  
+ATOM   2822  O   LYS A 369     -51.056  25.460   9.973  1.00 77.94           O  
+ANISOU 2822  O   LYS A 369     9923   9884   9808  -1153    487   1714       O  
+ATOM   2823  CB  LYS A 369     -51.643  28.649  10.301  1.00 81.84           C  
+ANISOU 2823  CB  LYS A 369    11027   9548  10520  -1051   -330   2070       C  
+ATOM   2824  N   TYR A 370     -52.468  25.879  11.679  1.00 80.89           N  
+ANISOU 2824  N   TYR A 370    10324  10007  10402   -680    163   1404       N  
+ATOM   2825  CA  TYR A 370     -52.133  24.659  12.409  1.00 74.46           C  
+ANISOU 2825  CA  TYR A 370     9305   9360   9628   -660    423   1194       C  
+ATOM   2826  C   TYR A 370     -52.471  23.412  11.572  1.00 76.26           C  
+ANISOU 2826  C   TYR A 370     9414   9910   9650   -711    682   1117       C  
+ATOM   2827  O   TYR A 370     -51.638  22.503  11.419  1.00 73.36           O  
+ANISOU 2827  O   TYR A 370     8933   9680   9259   -834    932   1088       O  
+ATOM   2828  CB  TYR A 370     -52.871  24.641  13.750  1.00 77.04           C  
+ANISOU 2828  CB  TYR A 370     9620   9592  10060   -395    333    951       C  
+ATOM   2829  CG  TYR A 370     -52.306  23.693  14.784  1.00 72.87           C  
+ANISOU 2829  CG  TYR A 370     8994   9104   9591   -384    513    794       C  
+ATOM   2830  CD1 TYR A 370     -51.041  23.891  15.322  1.00 72.32           C  
+ANISOU 2830  CD1 TYR A 370     8919   8894   9665   -488    477    856       C  
+ATOM   2831  CD2 TYR A 370     -53.052  22.618  15.246  1.00 70.01           C  
+ANISOU 2831  CD2 TYR A 370     8557   8904   9139   -281    690    587       C  
+ATOM   2832  CE1 TYR A 370     -50.526  23.031  16.275  1.00 70.16           C  
+ANISOU 2832  CE1 TYR A 370     8586   8639   9431   -437    579    720       C  
+ATOM   2833  CE2 TYR A 370     -52.547  21.753  16.198  1.00 68.56           C  
+ANISOU 2833  CE2 TYR A 370     8364   8710   8976   -266    821    477       C  
+ATOM   2834  CZ  TYR A 370     -51.284  21.965  16.709  1.00 67.59           C  
+ANISOU 2834  CZ  TYR A 370     8256   8441   8984   -317    746    545       C  
+ATOM   2835  OH  TYR A 370     -50.776  21.108  17.658  1.00 66.02           O  
+ANISOU 2835  OH  TYR A 370     8076   8216   8793   -265    818    443       O  
+ATOM   2836  N   ARG A 371     -53.675  23.396  10.999  1.00 76.56           N  
+ANISOU 2836  N   ARG A 371     9477  10062   9549   -604    593   1066       N  
+ATOM   2837  CA  ARG A 371     -54.117  22.274  10.169  1.00 78.84           C  
+ANISOU 2837  CA  ARG A 371     9682  10638   9635   -666    784    968       C  
+ATOM   2838  C   ARG A 371     -53.277  22.120   8.909  1.00 79.85           C  
+ANISOU 2838  C   ARG A 371     9872  10895   9572   -900    931   1150       C  
+ATOM   2839  O   ARG A 371     -52.840  21.018   8.578  1.00 84.81           O  
+ANISOU 2839  O   ARG A 371    10414  11702  10106   -991   1199   1048       O  
+ATOM   2840  CB  ARG A 371     -55.589  22.427   9.756  1.00 75.27           C  
+ANISOU 2840  CB  ARG A 371     9216  10296   9086   -515    594    874       C  
+ATOM   2841  CG  ARG A 371     -56.625  22.135  10.827  1.00 76.82           C  
+ANISOU 2841  CG  ARG A 371     9256  10523   9409   -317    578    608       C  
+ATOM   2842  CD  ARG A 371     -58.017  22.065  10.204  1.00 81.59           C  
+ANISOU 2842  CD  ARG A 371     9748  11336   9917   -213    429    484       C  
+ATOM   2843  NE  ARG A 371     -59.061  21.680  11.151  1.00 81.47           N  
+ANISOU 2843  NE  ARG A 371     9514  11429  10011    -76    481    203       N  
+ATOM   2844  CZ  ARG A 371     -59.860  22.540  11.771  1.00 87.31           C  
+ANISOU 2844  CZ  ARG A 371    10169  12118  10887    186    282     98       C  
+ATOM   2845  NH1 ARG A 371     -59.731  23.840  11.549  1.00 92.49           N  
+ANISOU 2845  NH1 ARG A 371    10989  12553  11601    358    -28    258       N  
+ATOM   2846  NH2 ARG A 371     -60.786  22.102  12.614  1.00 91.50           N  
+ANISOU 2846  NH2 ARG A 371    10466  12811  11491    270    404   -174       N  
+ATOM   2847  N   ARG A 372     -53.047  23.227   8.212  1.00 75.56           N  
+ANISOU 2847  N   ARG A 372     9505  10249   8956   -998    761   1415       N  
+ATOM   2848  CA  ARG A 372     -52.244  23.198   6.995  1.00 74.99           C  
+ANISOU 2848  CA  ARG A 372     9518  10320   8654  -1259    931   1614       C  
+ATOM   2849  C   ARG A 372     -50.849  22.671   7.306  1.00 81.73           C  
+ANISOU 2849  C   ARG A 372    10195  11232   9626  -1414   1239   1590       C  
+ATOM   2850  O   ARG A 372     -50.265  21.905   6.532  1.00 82.24           O  
+ANISOU 2850  O   ARG A 372    10190  11540   9517  -1547   1527   1559       O  
+ATOM   2851  CB  ARG A 372     -52.167  24.594   6.378  1.00 73.92           C  
+ANISOU 2851  CB  ARG A 372     9656   9993   8436  -1375    684   1947       C  
+ATOM   2852  CG  ARG A 372     -53.527  25.170   6.017  1.00 79.64           C  
+ANISOU 2852  CG  ARG A 372    10560  10645   9053  -1160    316   1971       C  
+ATOM   2853  CD  ARG A 372     -53.406  26.447   5.204  1.00 89.74           C  
+ANISOU 2853  CD  ARG A 372    12201  11715  10182  -1287     61   2340       C  
+ATOM   2854  NE  ARG A 372     -54.661  26.784   4.540  1.00 95.55           N  
+ANISOU 2854  NE  ARG A 372    13114  12459  10732  -1072   -289   2364       N  
+ATOM   2855  CZ  ARG A 372     -55.064  26.259   3.389  1.00101.60           C  
+ANISOU 2855  CZ  ARG A 372    13962  13502  11140  -1130   -264   2384       C  
+ATOM   2856  NH1 ARG A 372     -54.307  25.369   2.763  1.00103.50           N  
+ANISOU 2856  NH1 ARG A 372    14141  14027  11158  -1392    131   2371       N  
+ATOM   2857  NH2 ARG A 372     -56.224  26.625   2.862  1.00101.83           N  
+ANISOU 2857  NH2 ARG A 372    14130  13529  11031   -902   -654   2393       N  
+ATOM   2858  N   ASP A 373     -50.344  23.069   8.469  1.00 78.47           N  
+ANISOU 2858  N   ASP A 373     9700  10604   9511  -1366   1156   1570       N  
+ATOM   2859  CA  ASP A 373     -49.024  22.666   8.928  1.00 68.08           C  
+ANISOU 2859  CA  ASP A 373     8176   9325   8367  -1469   1364   1530       C  
+ATOM   2860  C   ASP A 373     -48.962  21.160   9.178  1.00 64.05           C  
+ANISOU 2860  C   ASP A 373     7498   8994   7846  -1332   1601   1256       C  
+ATOM   2861  O   ASP A 373     -47.999  20.505   8.781  1.00 57.32           O  
+ANISOU 2861  O   ASP A 373     6485   8318   6976  -1418   1860   1210       O  
+ATOM   2862  CB  ASP A 373     -48.655  23.437  10.197  1.00 71.29           C  
+ANISOU 2862  CB  ASP A 373     8567   9441   9078  -1417   1141   1540       C  
+ATOM   2863  CG  ASP A 373     -47.204  23.257  10.599  1.00 85.58           C  
+ANISOU 2863  CG  ASP A 373    10141  11286  11088  -1555   1276   1532       C  
+ATOM   2864  OD1 ASP A 373     -46.480  22.463   9.964  1.00 94.04           O  
+ANISOU 2864  OD1 ASP A 373    11023  12621  12087  -1647   1571   1489       O  
+ATOM   2865  OD2 ASP A 373     -46.784  23.927  11.561  1.00 93.13           O  
+ANISOU 2865  OD2 ASP A 373    11088  12014  12282  -1555   1071   1544       O  
+HETATM 2866  N   MSE A 374     -49.978  20.602   9.834  1.00 74.49           N  
+ANISOU 2866  N   MSE A 374     8860  10265   9179  -1124   1521   1067       N  
+HETATM 2867  CA  MSE A 374     -49.936  19.167  10.121  1.00 71.51           C  
+ANISOU 2867  CA  MSE A 374     8396   9984   8792  -1022   1723    829       C  
+HETATM 2868  C   MSE A 374     -50.244  18.307   8.887  1.00 74.79           C  
+ANISOU 2868  C   MSE A 374     8841  10636   8940  -1088   1919    749       C  
+HETATM 2869  O   MSE A 374     -49.769  17.176   8.786  1.00 70.71           O  
+ANISOU 2869  O   MSE A 374     8262  10202   8402  -1052   2131    582       O  
+HETATM 2870  CB  MSE A 374     -50.898  18.808  11.259  1.00 55.38           C  
+ANISOU 2870  CB  MSE A 374     6406   7810   6827   -845   1613    666       C  
+HETATM 2871  CG  MSE A 374     -52.310  18.464  10.821  1.00 66.89           C  
+ANISOU 2871  CG  MSE A 374     7923   9376   8115   -820   1590    562       C  
+HETATM 2872 SE   MSE A 374     -53.488  18.182  12.341  1.00 85.33          SE  
+ANISOU 2872 SE   MSE A 374    10272  11596  10554   -658   1513    367      SE  
+HETATM 2873  CE  MSE A 374     -53.488  19.999  13.028  1.00 59.57           C  
+ANISOU 2873  CE  MSE A 374     7049   8128   7456   -540   1204    514       C  
+ATOM   2874  N   ILE A 375     -51.022  18.843   7.949  1.00 68.71           N  
+ANISOU 2874  N   ILE A 375     8191   9956   7957  -1164   1819    853       N  
+ATOM   2875  CA  ILE A 375     -51.412  18.087   6.758  1.00 69.75           C  
+ANISOU 2875  CA  ILE A 375     8391  10318   7794  -1231   1954    762       C  
+ATOM   2876  C   ILE A 375     -50.330  18.145   5.674  1.00 73.01           C  
+ANISOU 2876  C   ILE A 375     8802  10917   8022  -1404   2187    874       C  
+ATOM   2877  O   ILE A 375     -50.220  17.238   4.846  1.00 60.38           O  
+ANISOU 2877  O   ILE A 375     7226   9515   6201  -1434   2399    725       O  
+ATOM   2878  CB  ILE A 375     -52.763  18.592   6.192  1.00 68.62           C  
+ANISOU 2878  CB  ILE A 375     8378  10220   7475  -1218   1702    807       C  
+ATOM   2879  CG1 ILE A 375     -53.864  18.435   7.241  1.00 65.53           C  
+ANISOU 2879  CG1 ILE A 375     7916   9719   7264  -1056   1539    643       C  
+ATOM   2880  CG2 ILE A 375     -53.172  17.813   4.950  1.00 60.97           C  
+ANISOU 2880  CG2 ILE A 375     7499   9493   6174  -1300   1797    695       C  
+ATOM   2881  CD1 ILE A 375     -55.238  18.831   6.750  1.00 63.01           C  
+ANISOU 2881  CD1 ILE A 375     7629   9487   6823  -1000   1280    624       C  
+ATOM   2882  N   THR A 376     -49.509  19.193   5.704  1.00 69.85           N  
+ANISOU 2882  N   THR A 376     8372  10458   7711  -1533   2167   1117       N  
+ATOM   2883  CA  THR A 376     -48.424  19.346   4.732  1.00 65.98           C  
+ANISOU 2883  CA  THR A 376     7841  10177   7053  -1752   2435   1242       C  
+ATOM   2884  C   THR A 376     -47.463  18.159   4.800  1.00 74.92           C  
+ANISOU 2884  C   THR A 376     8738  11472   8258  -1678   2766    990       C  
+ATOM   2885  O   THR A 376     -46.864  17.759   3.800  1.00 77.14           O  
+ANISOU 2885  O   THR A 376     8983  12021   8307  -1782   3064    944       O  
+ATOM   2886  CB  THR A 376     -47.639  20.653   4.965  1.00 67.30           C  
+ANISOU 2886  CB  THR A 376     7979  10214   7378  -1952   2357   1537       C  
+ATOM   2887  OG1 THR A 376     -48.547  21.761   4.977  1.00 77.66           O  
+ANISOU 2887  OG1 THR A 376     9552  11304   8652  -1961   2004   1753       O  
+ATOM   2888  CG2 THR A 376     -46.607  20.867   3.868  1.00 63.78           C  
+ANISOU 2888  CG2 THR A 376     7490  10029   6714  -2250   2675   1691       C  
+ATOM   2889  N   ARG A 377     -47.345  17.593   5.995  1.00 84.80           N  
+ANISOU 2889  N   ARG A 377     9852  12552   9815  -1473   2701    816       N  
+ATOM   2890  CA  ARG A 377     -46.474  16.455   6.255  1.00 86.24           C  
+ANISOU 2890  CA  ARG A 377     9835  12807  10123  -1323   2927    567       C  
+ATOM   2891  C   ARG A 377     -46.923  15.188   5.532  1.00 90.21           C  
+ANISOU 2891  C   ARG A 377    10458  13433  10383  -1225   3098    308       C  
+ATOM   2892  O   ARG A 377     -46.149  14.242   5.382  1.00 94.05           O  
+ANISOU 2892  O   ARG A 377    10819  14016  10901  -1099   3325     88       O  
+ATOM   2893  CB  ARG A 377     -46.426  16.195   7.757  1.00 77.71           C  
+ANISOU 2893  CB  ARG A 377     8688  11459   9378  -1119   2736    478       C  
+ATOM   2894  CG  ARG A 377     -46.167  17.447   8.568  1.00 81.78           C  
+ANISOU 2894  CG  ARG A 377     9144  11808  10119  -1201   2505    692       C  
+ATOM   2895  CD  ARG A 377     -46.106  17.137  10.044  1.00 84.55           C  
+ANISOU 2895  CD  ARG A 377     9471  11917  10737   -991   2318    585       C  
+ATOM   2896  NE  ARG A 377     -45.004  16.234  10.338  1.00 86.98           N  
+ANISOU 2896  NE  ARG A 377     9566  12279  11204   -839   2447    412       N  
+ATOM   2897  CZ  ARG A 377     -43.821  16.638  10.782  1.00 89.15           C  
+ANISOU 2897  CZ  ARG A 377     9571  12576  11726   -853   2406    445       C  
+ATOM   2898  NH1 ARG A 377     -43.597  17.928  10.990  1.00 89.41           N  
+ANISOU 2898  NH1 ARG A 377     9554  12552  11868  -1057   2252    653       N  
+ATOM   2899  NH2 ARG A 377     -42.865  15.753  11.030  1.00100.38           N  
+ANISOU 2899  NH2 ARG A 377    10775  14061  13305   -655   2491    256       N  
+ATOM   2900  N   THR A 378     -48.175  15.176   5.084  1.00 87.50           N  
+ANISOU 2900  N   THR A 378    10354  13080   9812  -1271   2963    312       N  
+ATOM   2901  CA  THR A 378     -48.787  13.968   4.541  1.00 78.13           C  
+ANISOU 2901  CA  THR A 378     9314  11952   8421  -1203   3051     45       C  
+ATOM   2902  C   THR A 378     -49.102  14.069   3.051  1.00 81.62           C  
+ANISOU 2902  C   THR A 378     9917  12659   8436  -1360   3145     64       C  
+ATOM   2903  O   THR A 378     -49.092  15.156   2.472  1.00 80.31           O  
+ANISOU 2903  O   THR A 378     9805  12600   8108  -1528   3090    331       O  
+ATOM   2904  CB  THR A 378     -50.088  13.633   5.289  1.00 73.09           C  
+ANISOU 2904  CB  THR A 378     8797  11106   7866  -1142   2809    -37       C  
+ATOM   2905  OG1 THR A 378     -51.092  14.603   4.964  1.00 74.59           O  
+ANISOU 2905  OG1 THR A 378     9075  11337   7930  -1249   2575    142       O  
+ATOM   2906  CG2 THR A 378     -49.850  13.639   6.790  1.00 71.92           C  
+ANISOU 2906  CG2 THR A 378     8554  10701   8070  -1006   2706    -24       C  
+ATOM   2907  N   GLY A 379     -49.375  12.921   2.438  1.00 79.89           N  
+ANISOU 2907  N   GLY A 379     9822  12519   8015  -1309   3267   -220       N  
+ATOM   2908  CA  GLY A 379     -49.715  12.859   1.028  1.00 75.80           C  
+ANISOU 2908  CA  GLY A 379     9501  12256   7042  -1440   3339   -258       C  
+ATOM   2909  C   GLY A 379     -51.021  12.126   0.783  1.00 75.60           C  
+ANISOU 2909  C   GLY A 379     9676  12179   6870  -1444   3142   -465       C  
+ATOM   2910  O   GLY A 379     -51.537  12.113  -0.335  1.00 75.12           O  
+ANISOU 2910  O   GLY A 379     9810  12313   6419  -1553   3100   -501       O  
+ATOM   2911  N   VAL A 380     -51.554  11.511   1.835  1.00 81.80           N  
+ANISOU 2911  N   VAL A 380    10419  12708   7953  -1349   3017   -599       N  
+ATOM   2912  CA  VAL A 380     -52.840  10.825   1.769  1.00 75.35           C  
+ANISOU 2912  CA  VAL A 380     9735  11829   7066  -1408   2829   -794       C  
+ATOM   2913  C   VAL A 380     -53.649  11.121   3.026  1.00 76.19           C  
+ANISOU 2913  C   VAL A 380     9726  11728   7494  -1394   2609   -709       C  
+ATOM   2914  O   VAL A 380     -53.138  11.006   4.141  1.00 68.78           O  
+ANISOU 2914  O   VAL A 380     8695  10584   6854  -1286   2670   -679       O  
+ATOM   2915  CB  VAL A 380     -52.668   9.292   1.621  1.00 69.60           C  
+ANISOU 2915  CB  VAL A 380     9146  10995   6305  -1353   2997  -1163       C  
+ATOM   2916  CG1 VAL A 380     -53.996   8.576   1.828  1.00 69.05           C  
+ANISOU 2916  CG1 VAL A 380     9182  10799   6257  -1474   2795  -1349       C  
+ATOM   2917  CG2 VAL A 380     -52.072   8.938   0.266  1.00 71.49           C  
+ANISOU 2917  CG2 VAL A 380     9525  11478   6161  -1358   3212  -1320       C  
+ATOM   2918  N   SER A 381     -54.911  11.500   2.850  1.00 72.25           N  
+ANISOU 2918  N   SER A 381     9225  11304   6923  -1488   2347   -687       N  
+ATOM   2919  CA  SER A 381     -55.761  11.816   3.992  1.00 63.29           C  
+ANISOU 2919  CA  SER A 381     7946  10035   6067  -1471   2172   -641       C  
+ATOM   2920  C   SER A 381     -56.941  10.856   4.085  1.00 79.94           C  
+ANISOU 2920  C   SER A 381    10064  12129   8180  -1603   2093   -901       C  
+ATOM   2921  O   SER A 381     -57.767  10.787   3.178  1.00 78.18           O  
+ANISOU 2921  O   SER A 381     9866  12093   7745  -1711   1930  -1003       O  
+ATOM   2922  CB  SER A 381     -56.264  13.259   3.900  1.00 62.00           C  
+ANISOU 2922  CB  SER A 381     7692   9969   5898  -1435   1913   -392       C  
+ATOM   2923  OG  SER A 381     -55.184  14.175   3.869  1.00 73.98           O  
+ANISOU 2923  OG  SER A 381     9221  11458   7431  -1376   1980   -135       O  
+ATOM   2924  N   ILE A 382     -57.019  10.122   5.191  1.00 69.22           N  
+ANISOU 2924  N   ILE A 382     8697  10549   7056  -1617   2196  -1000       N  
+ATOM   2925  CA  ILE A 382     -58.143   9.225   5.436  1.00 72.20           C  
+ANISOU 2925  CA  ILE A 382     9073  10888   7472  -1811   2152  -1222       C  
+ATOM   2926  C   ILE A 382     -59.159   9.899   6.350  1.00 75.89           C  
+ANISOU 2926  C   ILE A 382     9295  11408   8129  -1836   2019  -1152       C  
+ATOM   2927  O   ILE A 382     -58.790  10.491   7.360  1.00 67.94           O  
+ANISOU 2927  O   ILE A 382     8225  10289   7302  -1701   2060   -993       O  
+ATOM   2928  CB  ILE A 382     -57.682   7.894   6.062  1.00 70.99           C  
+ANISOU 2928  CB  ILE A 382     9128  10426   7418  -1856   2357  -1375       C  
+ATOM   2929  CG1 ILE A 382     -56.624   7.229   5.179  1.00 60.15           C  
+ANISOU 2929  CG1 ILE A 382     7973   9004   5879  -1759   2500  -1493       C  
+ATOM   2930  CG2 ILE A 382     -58.864   6.960   6.277  1.00 61.98           C  
+ANISOU 2930  CG2 ILE A 382     8017   9226   6307  -2140   2325  -1588       C  
+ATOM   2931  CD1 ILE A 382     -56.040   5.966   5.772  1.00 62.01           C  
+ANISOU 2931  CD1 ILE A 382     8447   8885   6229  -1717   2658  -1642       C  
+ATOM   2932  N   PHE A 383     -60.437   9.811   5.995  1.00 80.80           N  
+ANISOU 2932  N   PHE A 383     9763  12223   8713  -2000   1854  -1299       N  
+ATOM   2933  CA  PHE A 383     -61.472  10.522   6.742  1.00 73.13           C  
+ANISOU 2933  CA  PHE A 383     8489  11379   7920  -1988   1729  -1277       C  
+ATOM   2934  C   PHE A 383     -62.443   9.581   7.451  1.00 71.25           C  
+ANISOU 2934  C   PHE A 383     8143  11123   7806  -2263   1835  -1485       C  
+ATOM   2935  O   PHE A 383     -63.091   8.746   6.820  1.00 79.41           O  
+ANISOU 2935  O   PHE A 383     9179  12238   8757  -2515   1790  -1699       O  
+ATOM   2936  CB  PHE A 383     -62.232  11.465   5.808  1.00 72.14           C  
+ANISOU 2936  CB  PHE A 383     8176  11548   7687  -1906   1403  -1258       C  
+ATOM   2937  CG  PHE A 383     -61.357  12.496   5.156  1.00 71.97           C  
+ANISOU 2937  CG  PHE A 383     8295  11527   7525  -1685   1298  -1006       C  
+ATOM   2938  CD1 PHE A 383     -60.717  12.224   3.958  1.00 75.43           C  
+ANISOU 2938  CD1 PHE A 383     8975  12011   7675  -1725   1309   -991       C  
+ATOM   2939  CD2 PHE A 383     -61.157  13.729   5.751  1.00 71.33           C  
+ANISOU 2939  CD2 PHE A 383     8130  11389   7585  -1463   1207   -789       C  
+ATOM   2940  CE1 PHE A 383     -59.903  13.167   3.361  1.00 85.12           C  
+ANISOU 2940  CE1 PHE A 383    10340  13253   8748  -1586   1258   -738       C  
+ATOM   2941  CE2 PHE A 383     -60.343  14.676   5.160  1.00 71.54           C  
+ANISOU 2941  CE2 PHE A 383     8314  11381   7486  -1327   1117   -536       C  
+ATOM   2942  CZ  PHE A 383     -59.716  14.393   3.962  1.00 80.80           C  
+ANISOU 2942  CZ  PHE A 383     9713  12625   8363  -1408   1158   -496       C  
+ATOM   2943  N   LEU A 384     -62.533   9.725   8.770  1.00 62.49           N  
+ANISOU 2943  N   LEU A 384     6959   9909   6876  -2243   1982  -1423       N  
+ATOM   2944  CA  LEU A 384     -63.386   8.867   9.588  1.00 75.04           C  
+ANISOU 2944  CA  LEU A 384     8475  11475   8563  -2545   2148  -1577       C  
+ATOM   2945  C   LEU A 384     -64.439   9.677  10.344  1.00 90.57           C  
+ANISOU 2945  C   LEU A 384    10039  13698  10677  -2513   2118  -1610       C  
+ATOM   2946  O   LEU A 384     -64.106  10.638  11.035  1.00 95.24           O  
+ANISOU 2946  O   LEU A 384    10581  14265  11341  -2240   2114  -1464       O  
+ATOM   2947  CB  LEU A 384     -62.535   8.065  10.575  1.00 67.80           C  
+ANISOU 2947  CB  LEU A 384     7909  10178   7672  -2590   2405  -1493       C  
+ATOM   2948  CG  LEU A 384     -61.307   7.359   9.995  1.00 66.27           C  
+ANISOU 2948  CG  LEU A 384     8095   9708   7376  -2506   2445  -1467       C  
+ATOM   2949  CD1 LEU A 384     -60.489   6.702  11.097  1.00 71.42           C  
+ANISOU 2949  CD1 LEU A 384     9069   9981   8084  -2470   2631  -1370       C  
+ATOM   2950  CD2 LEU A 384     -61.717   6.337   8.947  1.00 65.52           C  
+ANISOU 2950  CD2 LEU A 384     8111   9619   7164  -2763   2405  -1696       C  
+ATOM   2951  N   TYR A 385     -65.702   9.277  10.213  1.00 85.03           N  
+ANISOU 2951  N   TYR A 385     9035  13247  10027  -2794   2098  -1831       N  
+ATOM   2952  CA  TYR A 385     -66.811   9.882  10.957  1.00 79.18           C  
+ANISOU 2952  CA  TYR A 385     7841  12803   9441  -2791   2122  -1933       C  
+ATOM   2953  C   TYR A 385     -66.883  11.398  10.766  1.00 71.19           C  
+ANISOU 2953  C   TYR A 385     6590  11970   8487  -2344   1853  -1853       C  
+ATOM   2954  O   TYR A 385     -67.034  11.877   9.643  1.00 75.76           O  
+ANISOU 2954  O   TYR A 385     7085  12694   9008  -2200   1532  -1862       O  
+ATOM   2955  CB  TYR A 385     -66.706   9.528  12.444  1.00 73.16           C  
+ANISOU 2955  CB  TYR A 385     7196  11875   8724  -2918   2479  -1878       C  
+ATOM   2956  CG  TYR A 385     -66.643   8.036  12.694  1.00 76.99           C  
+ANISOU 2956  CG  TYR A 385     7994  12114   9146  -3367   2724  -1922       C  
+ATOM   2957  CD1 TYR A 385     -67.799   7.267  12.692  1.00 74.73           C  
+ANISOU 2957  CD1 TYR A 385     7463  12019   8910  -3829   2832  -2138       C  
+ATOM   2958  CD2 TYR A 385     -65.430   7.396  12.916  1.00 79.75           C  
+ANISOU 2958  CD2 TYR A 385     8878  12023   9399  -3330   2825  -1757       C  
+ATOM   2959  CE1 TYR A 385     -67.752   5.903  12.909  1.00 81.34           C  
+ANISOU 2959  CE1 TYR A 385     8646  12568   9689  -4274   3037  -2165       C  
+ATOM   2960  CE2 TYR A 385     -65.372   6.030  13.136  1.00 80.81           C  
+ANISOU 2960  CE2 TYR A 385     9359  11866   9480  -3707   3006  -1795       C  
+ATOM   2961  CZ  TYR A 385     -66.537   5.289  13.131  1.00 82.89           C  
+ANISOU 2961  CZ  TYR A 385     9437  12278   9780  -4193   3112  -1987       C  
+ATOM   2962  OH  TYR A 385     -66.490   3.931  13.350  1.00 79.91           O  
+ANISOU 2962  OH  TYR A 385     9463  11550   9349  -4604   3277  -2010       O  
+ATOM   2963  N   GLY A 386     -66.787  12.146  11.860  1.00 71.69           N  
+ANISOU 2963  N   GLY A 386     6592  12002   8645  -2124   1965  -1776       N  
+ATOM   2964  CA  GLY A 386     -66.802  13.596  11.790  1.00 79.76           C  
+ANISOU 2964  CA  GLY A 386     7457  13110   9739  -1686   1704  -1702       C  
+ATOM   2965  C   GLY A 386     -68.018  14.242  12.431  1.00 97.92           C  
+ANISOU 2965  C   GLY A 386     9263  15736  12208  -1559   1693  -1910       C  
+ATOM   2966  O   GLY A 386     -68.703  15.052  11.800  1.00104.71           O  
+ANISOU 2966  O   GLY A 386     9810  16828  13146  -1311   1365  -2000       O  
+ATOM   2967  N   ASN A 387     -68.295  13.879  13.680  1.00 91.44           N  
+ANISOU 2967  N   ASN A 387     8375  14940  11426  -1713   2049  -1994       N  
+ATOM   2968  CA  ASN A 387     -69.398  14.474  14.427  1.00 85.70           C  
+ANISOU 2968  CA  ASN A 387     7164  14553  10845  -1584   2125  -2223       C  
+ATOM   2969  C   ASN A 387     -68.958  14.959  15.806  1.00 90.23           C  
+ANISOU 2969  C   ASN A 387     7917  14972  11394  -1405   2369  -2159       C  
+ATOM   2970  O   ASN A 387     -68.017  14.417  16.389  1.00 91.32           O  
+ANISOU 2970  O   ASN A 387     8510  14787  11399  -1549   2576  -1975       O  
+ATOM   2971  CB  ASN A 387     -70.551  13.477  14.571  1.00 87.75           C  
+ANISOU 2971  CB  ASN A 387     7033  15154  11156  -2045   2371  -2482       C  
+ATOM   2972  CG  ASN A 387     -70.204  12.301  15.473  1.00 95.77           C  
+ANISOU 2972  CG  ASN A 387     8451  15900  12036  -2462   2773  -2376       C  
+ATOM   2973  OD1 ASN A 387     -70.063  12.448  16.687  1.00101.73           O  
+ANISOU 2973  OD1 ASN A 387     9400  16515  12738  -2380   2984  -2298       O  
+ATOM   2974  ND2 ASN A 387     -70.088  11.118  14.879  1.00 93.05           N  
+ANISOU 2974  ND2 ASN A 387     8314  15419  11620  -2870   2805  -2355       N  
+ATOM   2975  N   LYS A 388     -69.648  15.961  16.343  1.00 93.12           N  
+ANISOU 2975  N   LYS A 388     7932  15568  11881  -1072   2327  -2336       N  
+ATOM   2976  CA  LYS A 388     -69.295  16.488  17.658  1.00 82.59           C  
+ANISOU 2976  CA  LYS A 388     6775  14108  10497   -878   2541  -2322       C  
+ATOM   2977  C   LYS A 388     -70.534  16.963  18.405  1.00 91.05           C  
+ANISOU 2977  C   LYS A 388     7323  15598  11673   -738   2708  -2653       C  
+ATOM   2978  O   LYS A 388     -71.630  16.996  17.845  1.00101.55           O  
+ANISOU 2978  O   LYS A 388     8176  17255  13152   -731   2568  -2853       O  
+ATOM   2979  CB  LYS A 388     -68.296  17.638  17.518  1.00 85.16           C  
+ANISOU 2979  CB  LYS A 388     7433  14084  10840   -431   2207  -2121       C  
+ATOM   2980  CG  LYS A 388     -68.843  18.836  16.750  1.00 84.58           C  
+ANISOU 2980  CG  LYS A 388     7064  14132  10939      8   1774  -2216       C  
+ATOM   2981  CD  LYS A 388     -67.827  19.963  16.641  1.00 84.51           C  
+ANISOU 2981  CD  LYS A 388     7445  13722  10941    377   1458  -1990       C  
+ATOM   2982  CE  LYS A 388     -68.421  21.143  15.885  1.00 91.68           C  
+ANISOU 2982  CE  LYS A 388     8128  14698  12009    814    999  -2064       C  
+ATOM   2983  NZ  LYS A 388     -67.455  22.261  15.713  1.00 95.59           N  
+ANISOU 2983  NZ  LYS A 388     9042  14762  12515   1115    676  -1819       N  
+ATOM   2984  N   ILE A 389     -70.361  17.328  19.672  1.00 93.75           N  
+ANISOU 2984  N   ILE A 389     7872  15826  11921   -599   2918  -2656       N  
+ATOM   2985  CA  ILE A 389     -71.476  17.844  20.458  1.00 99.27           C  
+ANISOU 2985  CA  ILE A 389     8235  16796  12688   -411   3021  -2904       C  
+ATOM   2986  C   ILE A 389     -71.538  19.370  20.441  1.00104.19           C  
+ANISOU 2986  C   ILE A 389     8647  17474  13465    231   2742  -3091       C  
+ATOM   2987  O   ILE A 389     -70.598  20.038  20.871  1.00102.87           O  
+ANISOU 2987  O   ILE A 389     8812  17043  13233    503   2694  -3021       O  
+ATOM   2988  CB  ILE A 389     -71.391  17.364  21.921  1.00 96.07           C  
+ANISOU 2988  CB  ILE A 389     8169  16276  12057   -620   3419  -2833       C  
+ATOM   2989  N   ASP A 390     -72.640  19.914  19.936  1.00110.88           N  
+ANISOU 2989  N   ASP A 390     8970  18633  14528    490   2517  -3335       N  
+ATOM   2990  CA  ASP A 390     -72.849  21.360  19.918  1.00108.12           C  
+ANISOU 2990  CA  ASP A 390     8439  18290  14351   1152   2189  -3528       C  
+ATOM   2991  C   ASP A 390     -74.213  21.691  20.515  1.00116.43           C  
+ANISOU 2991  C   ASP A 390     9065  19667  15506   1311   2289  -3833       C  
+ATOM   2992  O   ASP A 390     -74.360  22.593  21.346  1.00132.02           O  
+ANISOU 2992  O   ASP A 390    11073  21598  17493   1708   2311  -3997       O  
+ATOM   2993  CB  ASP A 390     -72.725  21.913  18.500  1.00108.30           C  
+ANISOU 2993  CB  ASP A 390     8321  18275  14552   1448   1642  -3476       C  
+ATOM   2994  N   LYS A 391     -75.207  20.923  20.080  1.00110.76           N  
+ANISOU 2994  N   LYS A 391     7947  19278  14858    982   2356  -3923       N  
+ATOM   2995  CA  LYS A 391     -76.576  21.090  20.535  1.00116.63           C  
+ANISOU 2995  CA  LYS A 391     8202  20396  15715   1065   2475  -4224       C  
+ATOM   2996  C   LYS A 391     -76.765  20.392  21.866  1.00117.58           C  
+ANISOU 2996  C   LYS A 391     8471  20581  15623    678   3040  -4213       C  
+ATOM   2997  O   LYS A 391     -76.744  19.167  21.926  1.00121.18           O  
+ANISOU 2997  O   LYS A 391     9048  21048  15948     96   3310  -4058       O  
+ATOM   2998  CB  LYS A 391     -77.557  20.522  19.507  1.00109.97           C  
+ANISOU 2998  CB  LYS A 391     6860  19887  15036    848   2297  -4337       C  
+ATOM   2999  N   VAL A 394     -75.977  16.209  18.816  1.00113.78           N  
+ANISOU 2999  N   VAL A 394     8333  19899  15000  -1151   2954  -3596       N  
+ATOM   3000  CA  VAL A 394     -75.025  15.703  17.835  1.00103.73           C  
+ANISOU 3000  CA  VAL A 394     7377  18373  13662  -1329   2768  -3384       C  
+ATOM   3001  C   VAL A 394     -75.035  16.554  16.569  1.00 94.41           C  
+ANISOU 3001  C   VAL A 394     5899  17325  12648   -927   2261  -3470       C  
+ATOM   3002  O   VAL A 394     -76.077  16.726  15.936  1.00103.37           O  
+ANISOU 3002  O   VAL A 394     6529  18792  13953   -837   2017  -3693       O  
+ATOM   3003  CB  VAL A 394     -75.331  14.238  17.466  1.00103.55           C  
+ANISOU 3003  CB  VAL A 394     7418  18350  13575  -1961   2911  -3343       C  
+ATOM   3004  CG1 VAL A 394     -74.446  13.779  16.315  1.00101.00           C  
+ANISOU 3004  CG1 VAL A 394     7367  17813  13196  -2105   2686  -3184       C  
+ATOM   3005  CG2 VAL A 394     -75.160  13.335  18.681  1.00 98.38           C  
+ANISOU 3005  CG2 VAL A 394     7165  17487  12728  -2354   3360  -3198       C  
+ATOM   3006  N   VAL A 395     -73.872  17.085  16.202  1.00 90.17           N  
+ANISOU 3006  N   VAL A 395     5677  16529  12055   -678   2083  -3286       N  
+ATOM   3007  CA  VAL A 395     -73.755  17.941  15.025  1.00 99.00           C  
+ANISOU 3007  CA  VAL A 395     6581  17738  13296   -270   1566  -3316       C  
+ATOM   3008  C   VAL A 395     -72.563  17.510  14.170  1.00109.03           C  
+ANISOU 3008  C   VAL A 395     8485  18567  14373   -451   1396  -2944       C  
+ATOM   3009  O   VAL A 395     -71.546  17.060  14.699  1.00119.55           O  
+ANISOU 3009  O   VAL A 395    10325  19554  15545   -650   1666  -2717       O  
+ATOM   3010  CB  VAL A 395     -73.595  19.433  15.428  1.00109.52           C  
+ANISOU 3010  CB  VAL A 395     7969  18921  14722    403   1323  -3331       C  
+ATOM   3011  CG1 VAL A 395     -73.459  20.328  14.202  1.00112.46           C  
+ANISOU 3011  CG1 VAL A 395     8446  19130  15153    820    678  -3197       C  
+ATOM   3012  CG2 VAL A 395     -74.769  19.888  16.282  1.00109.28           C  
+ANISOU 3012  CG2 VAL A 395     7505  19180  14836    624   1455  -3646       C  
+ATOM   3013  N   LYS A 396     -72.696  17.635  12.852  1.00109.51           N  
+ANISOU 3013  N   LYS A 396     8508  18664  14438   -372    947  -2900       N  
+ATOM   3014  CA  LYS A 396     -71.601  17.342  11.933  1.00 99.38           C  
+ANISOU 3014  CA  LYS A 396     7794  17015  12950   -494    779  -2576       C  
+ATOM   3015  C   LYS A 396     -70.408  18.252  12.222  1.00 94.77           C  
+ANISOU 3015  C   LYS A 396     7725  15988  12296   -166    705  -2277       C  
+ATOM   3016  O   LYS A 396     -70.581  19.439  12.499  1.00 96.09           O  
+ANISOU 3016  O   LYS A 396     7811  16119  12581    292    486  -2304       O  
+ATOM   3017  CB  LYS A 396     -72.056  17.504  10.481  1.00 94.12           C  
+ANISOU 3017  CB  LYS A 396     6994  16506  12259   -404    275  -2600       C  
+ATOM   3018  N   ALA A 397     -69.202  17.698  12.157  1.00 97.12           N  
+ANISOU 3018  N   ALA A 397     8538  15944  12419   -398    872  -2013       N  
+ATOM   3019  CA  ALA A 397     -67.996  18.458  12.476  1.00 94.01           C  
+ANISOU 3019  CA  ALA A 397     8598  15146  11974   -168    832  -1737       C  
+ATOM   3020  C   ALA A 397     -67.386  19.105  11.233  1.00 83.20           C  
+ANISOU 3020  C   ALA A 397     7513  13596  10505     -3    434  -1488       C  
+ATOM   3021  O   ALA A 397     -66.748  18.432  10.423  1.00 82.23           O  
+ANISOU 3021  O   ALA A 397     7646  13388  10208   -251    457  -1342       O  
+ATOM   3022  CB  ALA A 397     -66.976  17.559  13.160  1.00 87.87           C  
+ANISOU 3022  CB  ALA A 397     8188  14116  11083   -471   1219  -1599       C  
+ATOM   3023  N   LYS A 398     -67.597  20.412  11.091  1.00 87.65           N  
+ANISOU 3023  N   LYS A 398     8052  14092  11160    418     76  -1446       N  
+ATOM   3024  CA  LYS A 398     -67.087  21.186   9.956  1.00 95.35           C  
+ANISOU 3024  CA  LYS A 398     9338  14872  12019    580   -323  -1177       C  
+ATOM   3025  C   LYS A 398     -65.568  21.108   9.802  1.00 97.97           C  
+ANISOU 3025  C   LYS A 398    10174  14854  12195    400   -180   -848       C  
+ATOM   3026  O   LYS A 398     -65.039  21.213   8.690  1.00 96.79           O  
+ANISOU 3026  O   LYS A 398    10293  14625  11859    328   -355   -625       O  
+ATOM   3027  CB  LYS A 398     -67.513  22.652  10.087  1.00 94.75           C  
+ANISOU 3027  CB  LYS A 398     9220  14684  12096   1079   -715  -1180       C  
+ATOM   3028  N   GLY A 399     -64.873  20.932  10.922  1.00 87.96           N  
+ANISOU 3028  N   GLY A 399     9022  13405  10993    331    137   -829       N  
+ATOM   3029  CA  GLY A 399     -63.423  20.856  10.927  1.00 84.52           C  
+ANISOU 3029  CA  GLY A 399     8980  12670  10464    182    275   -560       C  
+ATOM   3030  C   GLY A 399     -62.869  19.772  10.025  1.00 84.45           C  
+ANISOU 3030  C   GLY A 399     9107  12722  10257   -143    429   -479       C  
+ATOM   3031  O   GLY A 399     -61.864  19.971   9.337  1.00 95.03           O  
+ANISOU 3031  O   GLY A 399    10730  13908  11470   -211    394   -238       O  
+ATOM   3032  N   VAL A 400     -63.533  18.622  10.015  1.00 84.40           N  
+ANISOU 3032  N   VAL A 400     8901  12945  10221   -357    611   -698       N  
+ATOM   3033  CA  VAL A 400     -63.097  17.499   9.196  1.00 83.02           C  
+ANISOU 3033  CA  VAL A 400     8870  12812   9862   -650    755   -685       C  
+ATOM   3034  C   VAL A 400     -63.198  17.807   7.704  1.00 90.81           C  
+ANISOU 3034  C   VAL A 400     9948  13908  10649   -634    462   -589       C  
+ATOM   3035  O   VAL A 400     -62.291  17.474   6.935  1.00 94.42           O  
+ANISOU 3035  O   VAL A 400    10673  14292  10909   -768    539   -447       O  
+ATOM   3036  CB  VAL A 400     -63.930  16.240   9.517  1.00 80.37           C  
+ANISOU 3036  CB  VAL A 400     8318  12667   9552   -910    971   -958       C  
+ATOM   3037  CG1 VAL A 400     -63.495  15.059   8.659  1.00 73.01           C  
+ANISOU 3037  CG1 VAL A 400     7580  11728   8433  -1193   1092   -982       C  
+ATOM   3038  CG2 VAL A 400     -63.839  15.915  11.003  1.00 73.22           C  
+ANISOU 3038  CG2 VAL A 400     7389  11650   8780   -953   1275  -1023       C  
+ATOM   3039  N   GLN A 401     -64.284  18.469   7.306  1.00 95.22           N  
+ANISOU 3039  N   GLN A 401    10289  14650  11242   -449    121   -671       N  
+ATOM   3040  CA  GLN A 401     -64.466  18.878   5.912  1.00103.64           C  
+ANISOU 3040  CA  GLN A 401    11483  15812  12084   -397   -232   -560       C  
+ATOM   3041  C   GLN A 401     -63.449  19.945   5.549  1.00106.68           C  
+ANISOU 3041  C   GLN A 401    12240  15928  12365   -268   -356   -205       C  
+ATOM   3042  O   GLN A 401     -62.974  19.994   4.419  1.00112.80           O  
+ANISOU 3042  O   GLN A 401    13292  16709  12856   -364   -450    -26       O  
+ATOM   3043  CB  GLN A 401     -65.887  19.378   5.639  1.00103.87           C  
+ANISOU 3043  CB  GLN A 401    11173  16091  12203   -175   -630   -740       C  
+ATOM   3044  CG  GLN A 401     -66.154  19.663   4.156  1.00104.39           C  
+ANISOU 3044  CG  GLN A 401    11402  16274  11988   -132  -1042   -638       C  
+ATOM   3045  CD  GLN A 401     -67.620  19.537   3.803  1.00111.96           C  
+ANISOU 3045  CD  GLN A 401    11939  17582  13019    -36  -1381   -928       C  
+ATOM   3046  OE1 GLN A 401     -68.343  18.775   4.441  1.00115.86           O  
+ANISOU 3046  OE1 GLN A 401    12021  18289  13709   -178  -1190  -1236       O  
+ATOM   3047  NE2 GLN A 401     -68.060  20.246   2.766  1.00119.08           N  
+ANISOU 3047  NE2 GLN A 401    12941  18552  13751    180  -1891   -830       N  
+ATOM   3048  N   SER A 402     -63.133  20.816   6.501  1.00101.58           N  
+ANISOU 3048  N   SER A 402    11615  15051  11932    -74   -355   -111       N  
+ATOM   3049  CA  SER A 402     -62.081  21.797   6.280  1.00100.74           C  
+ANISOU 3049  CA  SER A 402    11864  14649  11763    -26   -440    227       C  
+ATOM   3050  C   SER A 402     -60.770  21.074   5.988  1.00 95.06           C  
+ANISOU 3050  C   SER A 402    11360  13875  10884   -328    -87    362       C  
+ATOM   3051  O   SER A 402     -60.021  21.461   5.090  1.00 93.46           O  
+ANISOU 3051  O   SER A 402    11440  13606  10465   -428   -129    620       O  
+ATOM   3052  CB  SER A 402     -61.919  22.707   7.494  1.00104.08           C  
+ANISOU 3052  CB  SER A 402    12270  14812  12462    196   -470    247       C  
+ATOM   3053  OG  SER A 402     -63.124  23.386   7.793  1.00115.31           O  
+ANISOU 3053  OG  SER A 402    13469  16296  14046    528   -777     78       O  
+ATOM   3054  N   GLU A 403     -60.495  20.022   6.755  1.00 87.96           N  
+ANISOU 3054  N   GLU A 403    10330  13006  10085   -466    265    184       N  
+ATOM   3055  CA  GLU A 403     -59.292  19.221   6.546  1.00 81.53           C  
+ANISOU 3055  CA  GLU A 403     9670  12150   9159   -690    592    249       C  
+ATOM   3056  C   GLU A 403     -59.335  18.535   5.182  1.00 81.55           C  
+ANISOU 3056  C   GLU A 403     9781  12359   8844   -858    607    222       C  
+ATOM   3057  O   GLU A 403     -58.298  18.325   4.548  1.00 81.32           O  
+ANISOU 3057  O   GLU A 403     9943  12321   8635   -993    786    349       O  
+ATOM   3058  CB  GLU A 403     -59.124  18.200   7.673  1.00 71.69           C  
+ANISOU 3058  CB  GLU A 403     8300  10858   8081   -759    898     53       C  
+ATOM   3059  CG  GLU A 403     -58.657  18.828   8.978  1.00 72.03           C  
+ANISOU 3059  CG  GLU A 403     8335  10673   8362   -627    931    116       C  
+ATOM   3060  CD  GLU A 403     -58.874  17.940  10.186  1.00 77.38           C  
+ANISOU 3060  CD  GLU A 403     8906  11326   9169   -659   1159    -85       C  
+ATOM   3061  OE1 GLU A 403     -59.088  16.725  10.007  1.00 69.59           O  
+ANISOU 3061  OE1 GLU A 403     7899  10438   8105   -827   1341   -236       O  
+ATOM   3062  OE2 GLU A 403     -58.827  18.462  11.321  1.00 79.51           O  
+ANISOU 3062  OE2 GLU A 403     9154  11457   9598   -528   1150    -89       O  
+ATOM   3063  N   PHE A 404     -60.543  18.212   4.728  1.00 85.81           N  
+ANISOU 3063  N   PHE A 404    10183  13109   9311   -846    414     35       N  
+ATOM   3064  CA  PHE A 404     -60.744  17.678   3.384  1.00 93.76           C  
+ANISOU 3064  CA  PHE A 404    11317  14322   9984   -984    340    -12       C  
+ATOM   3065  C   PHE A 404     -60.321  18.695   2.337  1.00 92.97           C  
+ANISOU 3065  C   PHE A 404    11510  14203   9612   -943    125    297       C  
+ATOM   3066  O   PHE A 404     -59.522  18.390   1.446  1.00 90.30           O  
+ANISOU 3066  O   PHE A 404    11414  13923   8972  -1105    289    393       O  
+ATOM   3067  CB  PHE A 404     -62.213  17.287   3.178  1.00101.49           C  
+ANISOU 3067  CB  PHE A 404    12045  15537  10981   -971     94   -280       C  
+ATOM   3068  CG  PHE A 404     -62.555  16.910   1.761  1.00100.09           C  
+ANISOU 3068  CG  PHE A 404    12014  15576  10438  -1083    -95   -336       C  
+ATOM   3069  CD1 PHE A 404     -63.046  17.866   0.884  1.00101.54           C  
+ANISOU 3069  CD1 PHE A 404    12307  15846  10428   -929   -527   -180       C  
+ATOM   3070  CD2 PHE A 404     -62.399  15.614   1.306  1.00 93.95           C  
+ANISOU 3070  CD2 PHE A 404    11308  14895   9496  -1325    123   -551       C  
+ATOM   3071  CE1 PHE A 404     -63.364  17.540  -0.419  1.00105.69           C  
+ANISOU 3071  CE1 PHE A 404    13009  16580  10569  -1025   -735   -228       C  
+ATOM   3072  CE2 PHE A 404     -62.723  15.284  -0.001  1.00 95.99           C  
+ANISOU 3072  CE2 PHE A 404    11732  15356   9384  -1423    -72   -630       C  
+ATOM   3073  CZ  PHE A 404     -63.202  16.248  -0.862  1.00101.75           C  
+ANISOU 3073  CZ  PHE A 404    12568  16202   9892  -1279   -500   -465       C  
+ATOM   3074  N   ASN A 405     -60.863  19.903   2.458  1.00 96.17           N  
+ANISOU 3074  N   ASN A 405    11910  14516  10112   -723   -235    446       N  
+ATOM   3075  CA  ASN A 405     -60.531  20.992   1.556  1.00101.85           C  
+ANISOU 3075  CA  ASN A 405    12970  15145  10584   -684   -489    787       C  
+ATOM   3076  C   ASN A 405     -59.027  21.235   1.494  1.00100.90           C  
+ANISOU 3076  C   ASN A 405    13095  14863  10381   -872   -171   1054       C  
+ATOM   3077  O   ASN A 405     -58.434  21.187   0.417  1.00104.78           O  
+ANISOU 3077  O   ASN A 405    13860  15450  10502  -1054    -83   1220       O  
+ATOM   3078  CB  ASN A 405     -61.261  22.272   1.980  1.00110.19           C  
+ANISOU 3078  CB  ASN A 405    13993  16024  11849   -370   -918    888       C  
+ATOM   3079  CG  ASN A 405     -62.775  22.128   1.928  1.00113.90           C  
+ANISOU 3079  CG  ASN A 405    14160  16713  12404   -155  -1266    612       C  
+ATOM   3080  OD1 ASN A 405     -63.310  21.385   1.104  1.00112.38           O  
+ANISOU 3080  OD1 ASN A 405    13923  16793  11984   -260  -1345    459       O  
+ATOM   3081  ND2 ASN A 405     -63.472  22.844   2.805  1.00118.64           N  
+ANISOU 3081  ND2 ASN A 405    14532  17211  13336    150  -1480    521       N  
+ATOM   3082  N   ILE A 406     -58.407  21.427   2.657  1.00 94.76           N  
+ANISOU 3082  N   ILE A 406    12193  13876   9934   -844     21   1068       N  
+ATOM   3083  CA  ILE A 406     -56.967  21.669   2.724  1.00 90.80           C  
+ANISOU 3083  CA  ILE A 406    11833  13239   9426  -1026    308   1289       C  
+ATOM   3084  C   ILE A 406     -56.188  20.523   2.089  1.00 94.48           C  
+ANISOU 3084  C   ILE A 406    12313  13923   9661  -1247    703   1187       C  
+ATOM   3085  O   ILE A 406     -55.205  20.748   1.381  1.00 90.32           O  
+ANISOU 3085  O   ILE A 406    11968  13436   8913  -1436    886   1394       O  
+ATOM   3086  CB  ILE A 406     -56.480  21.854   4.175  1.00 83.99           C  
+ANISOU 3086  CB  ILE A 406    10793  12150   8970   -950    430   1242       C  
+ATOM   3087  CG1 ILE A 406     -57.186  23.034   4.843  1.00 86.82           C  
+ANISOU 3087  CG1 ILE A 406    11161  12273   9554   -703     58   1306       C  
+ATOM   3088  CG2 ILE A 406     -54.974  22.059   4.212  1.00 85.32           C  
+ANISOU 3088  CG2 ILE A 406    11043  12220   9157  -1155    701   1440       C  
+ATOM   3089  CD1 ILE A 406     -56.947  23.111   6.338  1.00 85.49           C  
+ANISOU 3089  CD1 ILE A 406    10819  11918   9745   -594    152   1182       C  
+ATOM   3090  N   SER A 407     -56.632  19.297   2.347  1.00 84.50           N  
+ANISOU 3090  N   SER A 407    10862  12795   8449  -1230    843    858       N  
+ATOM   3091  CA  SER A 407     -56.016  18.121   1.743  1.00 76.76           C  
+ANISOU 3091  CA  SER A 407     9917  11990   7258  -1385   1180    698       C  
+ATOM   3092  C   SER A 407     -56.066  18.182   0.218  1.00 85.11           C  
+ANISOU 3092  C   SER A 407    11242  13264   7831  -1508   1123    788       C  
+ATOM   3093  O   SER A 407     -55.083  17.864  -0.453  1.00 77.97           O  
+ANISOU 3093  O   SER A 407    10460  12478   6687  -1655   1429    828       O  
+ATOM   3094  CB  SER A 407     -56.684  16.840   2.244  1.00 69.99           C  
+ANISOU 3094  CB  SER A 407     8882  11180   6530  -1358   1260    335       C  
+ATOM   3095  OG  SER A 407     -56.374  16.616   3.610  1.00 70.88           O  
+ANISOU 3095  OG  SER A 407     8819  11100   7010  -1284   1401    267       O  
+ATOM   3096  N   PHE A 408     -57.206  18.596  -0.328  1.00 88.56           N  
+ANISOU 3096  N   PHE A 408    11765  13774   8109  -1433    728    809       N  
+ATOM   3097  CA  PHE A 408     -57.374  18.596  -1.780  1.00 89.66           C  
+ANISOU 3097  CA  PHE A 408    12202  14129   7737  -1538    615    878       C  
+ATOM   3098  C   PHE A 408     -56.657  19.762  -2.470  1.00 95.42           C  
+ANISOU 3098  C   PHE A 408    13260  14800   8193  -1640    583   1305       C  
+ATOM   3099  O   PHE A 408     -56.198  19.623  -3.606  1.00107.82           O  
+ANISOU 3099  O   PHE A 408    15110  16562   9295  -1813    725   1393       O  
+ATOM   3100  CB  PHE A 408     -58.862  18.611  -2.138  1.00 95.39           C  
+ANISOU 3100  CB  PHE A 408    12892  14965   8386  -1410    144    739       C  
+ATOM   3101  CG  PHE A 408     -59.131  18.850  -3.596  1.00104.32           C  
+ANISOU 3101  CG  PHE A 408    14382  16287   8969  -1477    -98    861       C  
+ATOM   3102  CD1 PHE A 408     -58.979  17.831  -4.522  1.00105.16           C  
+ANISOU 3102  CD1 PHE A 408    14637  16636   8684  -1638     82    649       C  
+ATOM   3103  CD2 PHE A 408     -59.534  20.098  -4.042  1.00107.41           C  
+ANISOU 3103  CD2 PHE A 408    15011  16591   9210  -1364   -529   1184       C  
+ATOM   3104  CE1 PHE A 408     -59.226  18.053  -5.865  1.00107.97           C  
+ANISOU 3104  CE1 PHE A 408    15368  17181   8476  -1703   -151    757       C  
+ATOM   3105  CE2 PHE A 408     -59.781  20.326  -5.383  1.00113.24           C  
+ANISOU 3105  CE2 PHE A 408    16141  17493   9394  -1423   -784   1324       C  
+ATOM   3106  CZ  PHE A 408     -59.628  19.302  -6.295  1.00114.74           C  
+ANISOU 3106  CZ  PHE A 408    16472  17962   9164  -1601   -589   1110       C  
+ATOM   3107  N   GLU A 409     -56.545  20.906  -1.798  1.00 91.64           N  
+ANISOU 3107  N   GLU A 409    12781  14053   7985  -1558    412   1568       N  
+ATOM   3108  CA  GLU A 409     -55.807  22.044  -2.365  1.00 97.82           C  
+ANISOU 3108  CA  GLU A 409    13905  14717   8546  -1715    392   2002       C  
+ATOM   3109  C   GLU A 409     -54.297  21.801  -2.284  1.00 88.10           C  
+ANISOU 3109  C   GLU A 409    12617  13533   7324  -1969    931   2072       C  
+ATOM   3110  O   GLU A 409     -53.495  22.538  -2.861  1.00 98.80           O  
+ANISOU 3110  O   GLU A 409    14222  14865   8451  -2204   1051   2407       O  
+ATOM   3111  CB  GLU A 409     -56.155  23.342  -1.636  1.00108.69           C  
+ANISOU 3111  CB  GLU A 409    15324  15735  10237  -1547     15   2233       C  
+ATOM   3112  CG  GLU A 409     -57.619  23.508  -1.258  1.00113.11           C  
+ANISOU 3112  CG  GLU A 409    15745  16244  10989  -1205   -469   2055       C  
+ATOM   3113  CD  GLU A 409     -57.847  24.618  -0.234  1.00120.90           C  
+ANISOU 3113  CD  GLU A 409    16684  16865  12387   -983   -745   2168       C  
+ATOM   3114  OE1 GLU A 409     -56.882  25.041   0.437  1.00120.59           O  
+ANISOU 3114  OE1 GLU A 409    16644  16608  12567  -1101   -531   2307       O  
+ATOM   3115  OE2 GLU A 409     -59.001  25.087  -0.119  1.00127.74           O  
+ANISOU 3115  OE2 GLU A 409    17509  17668  13357   -676  -1199   2097       O  
+ATOM   3116  N   GLN A 410     -53.928  20.766  -1.538  1.00 86.21           N  
+ANISOU 3116  N   GLN A 410    12037  13355   7365  -1922   1243   1752       N  
+ATOM   3117  CA  GLN A 410     -52.535  20.418  -1.314  1.00 86.01           C  
+ANISOU 3117  CA  GLN A 410    11856  13388   7434  -2084   1720   1740       C  
+ATOM   3118  C   GLN A 410     -52.160  19.223  -2.189  1.00 87.03           C  
+ANISOU 3118  C   GLN A 410    12000  13846   7222  -2164   2079   1488       C  
+ATOM   3119  O   GLN A 410     -51.090  18.629  -2.034  1.00 86.87           O  
+ANISOU 3119  O   GLN A 410    11789  13930   7288  -2224   2494   1360       O  
+ATOM   3120  CB  GLN A 410     -52.299  20.107   0.170  1.00 77.75           C  
+ANISOU 3120  CB  GLN A 410    10460  12148   6935  -1930   1783   1561       C  
+ATOM   3121  CG  GLN A 410     -50.848  20.095   0.608  1.00 88.78           C  
+ANISOU 3121  CG  GLN A 410    11661  13539   8531  -2059   2147   1607       C  
+ATOM   3122  CD  GLN A 410     -50.691  19.587   2.023  1.00 89.02           C  
+ANISOU 3122  CD  GLN A 410    11392  13399   9034  -1873   2170   1389       C  
+ATOM   3123  OE1 GLN A 410     -50.957  20.306   2.984  1.00 85.57           O  
+ANISOU 3123  OE1 GLN A 410    10913  12705   8897  -1782   1925   1479       O  
+ATOM   3124  NE2 GLN A 410     -50.275  18.333   2.158  1.00 82.64           N  
+ANISOU 3124  NE2 GLN A 410    10416  12716   8269  -1800   2450   1092       N  
+ATOM   3125  N   ASN A 411     -53.043  18.895  -3.129  1.00 89.26           N  
+ANISOU 3125  N   ASN A 411    12512  14292   7111  -2147   1893   1398       N  
+ATOM   3126  CA  ASN A 411     -52.890  17.716  -3.981  1.00 92.58           C  
+ANISOU 3126  CA  ASN A 411    12999  15000   7178  -2193   2165   1098       C  
+ATOM   3127  C   ASN A 411     -52.570  16.439  -3.208  1.00 87.98           C  
+ANISOU 3127  C   ASN A 411    12112  14390   6926  -2067   2434    700       C  
+ATOM   3128  O   ASN A 411     -51.575  15.771  -3.485  1.00 91.22           O  
+ANISOU 3128  O   ASN A 411    12461  14951   7247  -2108   2853    545       O  
+ATOM   3129  CB  ASN A 411     -51.806  17.961  -5.034  1.00 93.38           C  
+ANISOU 3129  CB  ASN A 411    13304  15346   6831  -2435   2542   1277       C  
+ATOM   3130  N   ASN A 412     -53.407  16.119  -2.227  1.00 84.59           N  
+ANISOU 3130  N   ASN A 412    11502  13765   6875  -1906   2195    538       N  
+ATOM   3131  CA  ASN A 412     -53.307  14.848  -1.522  1.00 81.48           C  
+ANISOU 3131  CA  ASN A 412    10915  13296   6748  -1800   2381    176       C  
+ATOM   3132  C   ASN A 412     -54.378  13.873  -1.974  1.00 84.18           C  
+ANISOU 3132  C   ASN A 412    11355  13713   6918  -1794   2223   -142       C  
+ATOM   3133  O   ASN A 412     -55.472  14.281  -2.363  1.00 91.27           O  
+ANISOU 3133  O   ASN A 412    12339  14667   7671  -1811   1860    -92       O  
+ATOM   3134  CB  ASN A 412     -53.427  15.042  -0.007  1.00 86.96           C  
+ANISOU 3134  CB  ASN A 412    11357  13711   7971  -1674   2282    202       C  
+ATOM   3135  CG  ASN A 412     -52.184  15.643   0.611  1.00101.28           C  
+ANISOU 3135  CG  ASN A 412    13027  15429  10025  -1676   2482    402       C  
+ATOM   3136  OD1 ASN A 412     -51.224  15.973  -0.084  1.00 96.87           O  
+ANISOU 3136  OD1 ASN A 412    12514  15026   9266  -1798   2715    539       O  
+ATOM   3137  ND2 ASN A 412     -52.192  15.777   1.933  1.00102.56           N  
+ANISOU 3137  ND2 ASN A 412    13007  15355  10607  -1561   2399    407       N  
+ATOM   3138  N   TYR A 413     -54.059  12.585  -1.924  1.00 76.78           N  
+ANISOU 3138  N   TYR A 413    10404  12761   6008  -1764   2468   -480       N  
+ATOM   3139  CA  TYR A 413     -55.036  11.560  -2.248  1.00 82.63           C  
+ANISOU 3139  CA  TYR A 413    11242  13519   6636  -1800   2323   -813       C  
+ATOM   3140  C   TYR A 413     -56.079  11.534  -1.137  1.00 88.61           C  
+ANISOU 3140  C   TYR A 413    11797  14082   7789  -1776   2063   -847       C  
+ATOM   3141  O   TYR A 413     -55.736  11.455   0.045  1.00 85.61           O  
+ANISOU 3141  O   TYR A 413    11247  13487   7795  -1694   2171   -817       O  
+ATOM   3142  CB  TYR A 413     -54.370  10.196  -2.406  1.00 79.59           C  
+ANISOU 3142  CB  TYR A 413    10938  13091   6211  -1761   2646  -1169       C  
+ATOM   3143  CG  TYR A 413     -53.441  10.103  -3.594  1.00 80.65           C  
+ANISOU 3143  CG  TYR A 413    11256  13480   5905  -1776   2939  -1221       C  
+ATOM   3144  CD1 TYR A 413     -53.914  10.285  -4.886  1.00 81.61           C  
+ANISOU 3144  CD1 TYR A 413    11646  13863   5499  -1897   2814  -1234       C  
+ATOM   3145  CD2 TYR A 413     -52.093   9.820  -3.425  1.00 82.49           C  
+ANISOU 3145  CD2 TYR A 413    11387  13720   6237  -1661   3342  -1274       C  
+ATOM   3146  CE1 TYR A 413     -53.070  10.197  -5.976  1.00 87.83           C  
+ANISOU 3146  CE1 TYR A 413    12615  14879   5875  -1903   3097  -1274       C  
+ATOM   3147  CE2 TYR A 413     -51.244   9.728  -4.507  1.00 87.97           C  
+ANISOU 3147  CE2 TYR A 413    12177  14586   6659  -1599   3557  -1297       C  
+ATOM   3148  CZ  TYR A 413     -51.735   9.918  -5.780  1.00 94.93           C  
+ANISOU 3148  CZ  TYR A 413    13344  15699   7025  -1723   3454  -1291       C  
+ATOM   3149  OH  TYR A 413     -50.890   9.828  -6.862  1.00100.33           O  
+ANISOU 3149  OH  TYR A 413    14138  16561   7422  -1660   3695  -1311       O  
+ATOM   3150  N   VAL A 414     -57.349  11.609  -1.517  1.00 84.70           N  
+ANISOU 3150  N   VAL A 414    11309  13690   7183  -1847   1719   -920       N  
+ATOM   3151  CA  VAL A 414     -58.426  11.695  -0.540  1.00 89.01           C  
+ANISOU 3151  CA  VAL A 414    11608  14132   8080  -1839   1487   -959       C  
+ATOM   3152  C   VAL A 414     -59.165  10.371  -0.379  1.00 89.39           C  
+ANISOU 3152  C   VAL A 414    11633  14126   8205  -1983   1486  -1328       C  
+ATOM   3153  O   VAL A 414     -59.716   9.836  -1.340  1.00 91.65           O  
+ANISOU 3153  O   VAL A 414    12050  14563   8208  -2107   1344  -1541       O  
+ATOM   3154  CB  VAL A 414     -59.436  12.784  -0.929  1.00 92.86           C  
+ANISOU 3154  CB  VAL A 414    12026  14779   8480  -1798   1062   -795       C  
+ATOM   3155  CG1 VAL A 414     -60.668  12.681  -0.061  1.00104.69           C  
+ANISOU 3155  CG1 VAL A 414    13214  16253  10312  -1800    851   -939       C  
+ATOM   3156  CG2 VAL A 414     -58.800  14.163  -0.815  1.00 80.26           C  
+ANISOU 3156  CG2 VAL A 414    10466  13128   6900  -1670   1029   -403       C  
+ATOM   3157  N   VAL A 415     -59.169   9.845   0.843  1.00 74.13           N  
+ANISOU 3157  N   VAL A 415     9566  11963   6636  -1991   1633  -1399       N  
+ATOM   3158  CA  VAL A 415     -59.791   8.555   1.122  1.00 75.38           C  
+ANISOU 3158  CA  VAL A 415     9747  12001   6893  -2179   1669  -1714       C  
+ATOM   3159  C   VAL A 415     -60.823   8.654   2.248  1.00 83.12           C  
+ANISOU 3159  C   VAL A 415    10440  12934   8206  -2267   1566  -1721       C  
+ATOM   3160  O   VAL A 415     -60.499   8.438   3.419  1.00 90.80           O  
+ANISOU 3160  O   VAL A 415    11378  13679   9443  -2239   1756  -1665       O  
+ATOM   3161  CB  VAL A 415     -58.736   7.495   1.499  1.00 79.74           C  
+ANISOU 3161  CB  VAL A 415    10511  12269   7518  -2142   2000  -1837       C  
+ATOM   3162  CG1 VAL A 415     -59.384   6.123   1.621  1.00 76.61           C  
+ANISOU 3162  CG1 VAL A 415    10241  11694   7174  -2372   2006  -2160       C  
+ATOM   3163  CG2 VAL A 415     -57.617   7.464   0.467  1.00 78.70           C  
+ANISOU 3163  CG2 VAL A 415    10594  12230   7079  -2017   2167  -1849       C  
+ATOM   3164  N   PRO A 416     -62.066   9.019   1.900  1.00 89.94           N  
+ANISOU 3164  N   PRO A 416    11087  14040   9046  -2360   1260  -1794       N  
+ATOM   3165  CA  PRO A 416     -63.171   9.079   2.863  1.00 88.31           C  
+ANISOU 3165  CA  PRO A 416    10541  13874   9138  -2465   1183  -1860       C  
+ATOM   3166  C   PRO A 416     -63.883   7.736   3.047  1.00 95.54           C  
+ANISOU 3166  C   PRO A 416    11453  14717  10130  -2817   1254  -2168       C  
+ATOM   3167  O   PRO A 416     -64.414   7.172   2.091  1.00 98.30           O  
+ANISOU 3167  O   PRO A 416    11859  15195  10298  -3004   1080  -2396       O  
+ATOM   3168  CB  PRO A 416     -64.106  10.116   2.244  1.00 91.12           C  
+ANISOU 3168  CB  PRO A 416    10644  14553   9425  -2362    789  -1819       C  
+ATOM   3169  CG  PRO A 416     -63.902   9.948   0.782  1.00 95.68           C  
+ANISOU 3169  CG  PRO A 416    11486  15260   9609  -2388    623  -1879       C  
+ATOM   3170  CD  PRO A 416     -62.442   9.606   0.602  1.00 95.55           C  
+ANISOU 3170  CD  PRO A 416    11837  15031   9437  -2321    950  -1779       C  
+ATOM   3171  N   VAL A 417     -63.896   7.237   4.279  1.00 94.51           N  
+ANISOU 3171  N   VAL A 417    11290  14369  10251  -2930   1496  -2168       N  
+ATOM   3172  CA  VAL A 417     -64.586   5.991   4.596  1.00 89.78           C  
+ANISOU 3172  CA  VAL A 417    10717  13651   9744  -3321   1589  -2416       C  
+ATOM   3173  C   VAL A 417     -66.066   6.264   4.849  1.00 92.71           C  
+ANISOU 3173  C   VAL A 417    10609  14340  10277  -3532   1424  -2545       C  
+ATOM   3174  O   VAL A 417     -66.456   6.645   5.954  1.00 87.63           O  
+ANISOU 3174  O   VAL A 417     9709  13735   9852  -3531   1552  -2463       O  
+ATOM   3175  CB  VAL A 417     -63.978   5.297   5.822  1.00 83.83           C  
+ANISOU 3175  CB  VAL A 417    10192  12508   9152  -3380   1916  -2337       C  
+ATOM   3176  N   GLY A 418     -66.884   6.054   3.821  1.00 96.98           N  
+ANISOU 3176  N   GLY A 418    11017  15130  10702  -3707   1140  -2772       N  
+ATOM   3177  CA  GLY A 418     -68.303   6.364   3.879  1.00 99.81           C  
+ANISOU 3177  CA  GLY A 418    10841  15863  11219  -3872    920  -2934       C  
+ATOM   3178  C   GLY A 418     -69.111   5.459   4.790  1.00102.59           C  
+ANISOU 3178  C   GLY A 418    11000  16172  11807  -4335   1142  -3109       C  
+ATOM   3179  O   GLY A 418     -70.273   5.742   5.080  1.00107.33           O  
+ANISOU 3179  O   GLY A 418    11071  17115  12597  -4481   1047  -3244       O  
+ATOM   3180  N   ALA A 419     -68.493   4.374   5.245  1.00102.28           N  
+ANISOU 3180  N   ALA A 419    11393  15712  11757  -4565   1439  -3105       N  
+ATOM   3181  CA  ALA A 419     -69.140   3.438   6.157  1.00 94.77           C  
+ANISOU 3181  CA  ALA A 419    10385  14635  10989  -5056   1690  -3216       C  
+ATOM   3182  C   ALA A 419     -69.316   4.128   7.500  1.00 90.34           C  
+ANISOU 3182  C   ALA A 419     9545  14166  10615  -4946   1935  -3030       C  
+ATOM   3183  O   ALA A 419     -70.305   3.926   8.204  1.00 86.35           O  
+ANISOU 3183  O   ALA A 419     8681  13846  10280  -5295   2080  -3136       O  
+ATOM   3184  CB  ALA A 419     -68.325   2.167   6.302  1.00 92.02           C  
+ANISOU 3184  CB  ALA A 419    10668  13737  10559  -5256   1903  -3220       C  
+ATOM   3185  N   THR A 420     -68.328   4.947   7.837  1.00 92.01           N  
+ANISOU 3185  N   THR A 420     9922  14258  10780  -4470   1990  -2766       N  
+ATOM   3186  CA  THR A 420     -68.340   5.744   9.051  1.00 93.10           C  
+ANISOU 3186  CA  THR A 420     9860  14464  11052  -4275   2181  -2590       C  
+ATOM   3187  C   THR A 420     -68.929   7.117   8.757  1.00101.88           C  
+ANISOU 3187  C   THR A 420    10464  16011  12237  -3930   1916  -2600       C  
+ATOM   3188  O   THR A 420     -68.223   8.123   8.780  1.00113.20           O  
+ANISOU 3188  O   THR A 420    11971  17405  13634  -3483   1829  -2398       O  
+ATOM   3189  CB  THR A 420     -66.922   5.907   9.623  1.00 84.89           C  
+ANISOU 3189  CB  THR A 420     9280  13035   9941  -3949   2341  -2313       C  
+ATOM   3190  OG1 THR A 420     -66.156   6.767   8.770  1.00 83.19           O  
+ANISOU 3190  OG1 THR A 420     9128  12863   9619  -3522   2111  -2197       O  
+ATOM   3191  CG2 THR A 420     -66.232   4.556   9.731  1.00 74.45           C  
+ANISOU 3191  CG2 THR A 420     8506  11244   8539  -4187   2518  -2315       C  
+ATOM   3192  N   GLY A 421     -70.222   7.138   8.449  1.00 94.00           N  
+ANISOU 3192  N   GLY A 421     8953  15412  11350  -4143   1760  -2847       N  
+ATOM   3193  CA  GLY A 421     -70.901   8.345   8.010  1.00 84.63           C  
+ANISOU 3193  CA  GLY A 421     7276  14639  10241  -3799   1423  -2906       C  
+ATOM   3194  C   GLY A 421     -70.777   9.528   8.951  1.00 88.84           C  
+ANISOU 3194  C   GLY A 421     7631  15231  10891  -3383   1508  -2752       C  
+ATOM   3195  O   GLY A 421     -70.622  10.666   8.507  1.00 91.49           O  
+ANISOU 3195  O   GLY A 421     7894  15657  11211  -2929   1209  -2653       O  
+ATOM   3196  N   ILE A 423     -69.899  13.012   8.196  1.00 99.91           N  
+ANISOU 3196  N   ILE A 423     9037  16670  12253  -2023    765  -2324       N  
+ATOM   3197  CA  ILE A 423     -69.234  13.922   7.271  1.00101.30           C  
+ANISOU 3197  CA  ILE A 423     9490  16729  12271  -1670    421  -2099       C  
+ATOM   3198  C   ILE A 423     -68.343  13.164   6.292  1.00103.93           C  
+ANISOU 3198  C   ILE A 423    10293  16867  12327  -1869    433  -1994       C  
+ATOM   3199  O   ILE A 423     -68.186  13.575   5.140  1.00 99.46           O  
+ANISOU 3199  O   ILE A 423     9883  16348  11560  -1733    108  -1908       O  
+ATOM   3200  CB  ILE A 423     -68.390  14.970   8.017  1.00 85.62           C  
+ANISOU 3200  CB  ILE A 423     7711  14483  10338  -1312    491  -1844       C  
+ATOM   3201  N   ALA A 424     -67.749  12.071   6.762  1.00 97.48           N  
+ANISOU 3201  N   ALA A 424     9730  15826  11483  -2170    808  -2003       N  
+ATOM   3202  CA  ALA A 424     -66.987  11.172   5.900  1.00 94.56           C  
+ANISOU 3202  CA  ALA A 424     9773  15282  10875  -2362    860  -1988       C  
+ATOM   3203  C   ALA A 424     -67.834  10.710   4.722  1.00101.80           C  
+ANISOU 3203  C   ALA A 424    10563  16458  11659  -2555    563  -2219       C  
+ATOM   3204  O   ALA A 424     -67.402  10.761   3.571  1.00105.10           O  
+ANISOU 3204  O   ALA A 424    11249  16878  11805  -2491    366  -2168       O  
+ATOM   3205  CB  ALA A 424     -66.484   9.974   6.693  1.00 96.74           C  
+ANISOU 3205  CB  ALA A 424    10286  15274  11195  -2650   1263  -2026       C  
+ATOM   3206  N   LYS A 425     -69.044  10.254   5.027  1.00105.72           N  
+ANISOU 3206  N   LYS A 425    10642  17194  12333  -2812    539  -2484       N  
+ATOM   3207  CA  LYS A 425     -69.992   9.820   4.011  1.00104.97           C  
+ANISOU 3207  CA  LYS A 425    10339  17384  12160  -3026    214  -2749       C  
+ATOM   3208  C   LYS A 425     -70.312  10.937   3.025  1.00108.99           C  
+ANISOU 3208  C   LYS A 425    10734  18139  12541  -2659   -290  -2686       C  
+ATOM   3209  O   LYS A 425     -70.339  10.716   1.814  1.00116.89           O  
+ANISOU 3209  O   LYS A 425    11921  19222  13271  -2710   -583  -2751       O  
+ATOM   3210  CB  LYS A 425     -71.279   9.314   4.661  1.00110.94           C  
+ANISOU 3210  CB  LYS A 425    10554  18405  13195  -3363    288  -3038       C  
+ATOM   3211  N   ASP A 426     -70.559  12.134   3.550  1.00108.65           N  
+ANISOU 3211  N   ASP A 426    10424  18189  12670  -2282   -407  -2563       N  
+ATOM   3212  CA  ASP A 426     -70.853  13.305   2.723  1.00119.31           C  
+ANISOU 3212  CA  ASP A 426    11713  19701  13916  -1880   -918  -2462       C  
+ATOM   3213  C   ASP A 426     -69.771  13.562   1.676  1.00117.58           C  
+ANISOU 3213  C   ASP A 426    12095  19275  13303  -1765  -1035  -2190       C  
+ATOM   3214  O   ASP A 426     -70.066  13.856   0.511  1.00125.44           O  
+ANISOU 3214  O   ASP A 426    13188  20429  14046  -1671  -1468  -2188       O  
+ATOM   3215  CB  ASP A 426     -71.004  14.556   3.598  1.00117.83           C  
+ANISOU 3215  CB  ASP A 426    11286  19505  13977  -1458   -956  -2336       C  
+ATOM   3216  CG  ASP A 426     -72.271  14.545   4.432  1.00123.78           C  
+ANISOU 3216  CG  ASP A 426    11356  20586  15088  -1481   -929  -2644       C  
+ATOM   3217  OD1 ASP A 426     -72.807  13.449   4.684  1.00133.59           O  
+ANISOU 3217  OD1 ASP A 426    12357  21981  16422  -1920   -704  -2897       O  
+ATOM   3218  OD2 ASP A 426     -72.725  15.636   4.839  1.00122.96           O  
+ANISOU 3218  OD2 ASP A 426    10963  20583  15175  -1065  -1121  -2641       O  
+ATOM   3219  N   LEU A 427     -68.514  13.458   2.091  1.00111.98           N  
+ANISOU 3219  N   LEU A 427    11784  18234  12529  -1774   -649  -1963       N  
+ATOM   3220  CA  LEU A 427     -67.393  13.684   1.181  1.00114.05           C  
+ANISOU 3220  CA  LEU A 427    12576  18329  12430  -1699   -663  -1710       C  
+ATOM   3221  C   LEU A 427     -67.197  12.509   0.228  1.00110.28           C  
+ANISOU 3221  C   LEU A 427    12366  17885  11650  -2008   -611  -1889       C  
+ATOM   3222  O   LEU A 427     -66.715  12.678  -0.895  1.00111.19           O  
+ANISOU 3222  O   LEU A 427    12840  18025  11382  -1963   -762  -1779       O  
+ATOM   3223  CB  LEU A 427     -66.100  13.946   1.966  1.00109.36           C  
+ANISOU 3223  CB  LEU A 427    12242  17405  11904  -1610   -271  -1447       C  
+ATOM   3224  CG  LEU A 427     -66.233  15.020   3.038  1.00107.02           C  
+ANISOU 3224  CG  LEU A 427    11724  17028  11911  -1328   -287  -1309       C  
+ATOM   3225  CD1 LEU A 427     -65.030  15.077   4.002  1.00 97.48           C  
+ANISOU 3225  CD1 LEU A 427    10721  15503  10813  -1302    109  -1118       C  
+ATOM   3226  CD2 LEU A 427     -66.469  16.330   2.326  1.00114.57           C  
+ANISOU 3226  CD2 LEU A 427    12736  18042  12753  -1008   -743  -1114       C  
+ATOM   3227  N   TRP A 428     -67.528  11.312   0.702  1.00106.57           N  
+ANISOU 3227  N   TRP A 428    11768  17392  11333  -2335   -376  -2162       N  
+ATOM   3228  CA  TRP A 428     -67.469  10.146  -0.151  1.00104.52           C  
+ANISOU 3228  CA  TRP A 428    11757  17133  10821  -2635   -361  -2393       C  
+ATOM   3229  C   TRP A 428     -68.488  10.286  -1.270  1.00107.41           C  
+ANISOU 3229  C   TRP A 428    11984  17836  10990  -2663   -880  -2572       C  
+ATOM   3230  O   TRP A 428     -68.252   9.833  -2.383  1.00111.37           O  
+ANISOU 3230  O   TRP A 428    12824  18377  11115  -2761  -1007  -2663       O  
+ATOM   3231  CB  TRP A 428     -67.731   8.865   0.630  1.00107.22           C  
+ANISOU 3231  CB  TRP A 428    12008  17336  11395  -3006    -52  -2644       C  
+ATOM   3232  CG  TRP A 428     -67.526   7.650  -0.204  1.00114.63           C  
+ANISOU 3232  CG  TRP A 428    13290  18182  12082  -3292    -21  -2885       C  
+ATOM   3233  CD1 TRP A 428     -66.398   6.890  -0.262  1.00114.73           C  
+ANISOU 3233  CD1 TRP A 428    13758  17879  11956  -3328    307  -2875       C  
+ATOM   3234  CD2 TRP A 428     -68.468   7.041  -1.102  1.00115.01           C  
+ANISOU 3234  CD2 TRP A 428    13257  18447  11993  -3562   -352  -3210       C  
+ATOM   3235  NE1 TRP A 428     -66.571   5.849  -1.139  1.00111.96           N  
+ANISOU 3235  NE1 TRP A 428    13650  17510  11380  -3586    218  -3179       N  
+ATOM   3236  CE2 TRP A 428     -67.832   5.918  -1.668  1.00115.97           C  
+ANISOU 3236  CE2 TRP A 428    13848  18338  11876  -3757   -190  -3385       C  
+ATOM   3237  CE3 TRP A 428     -69.785   7.331  -1.478  1.00120.67           C  
+ANISOU 3237  CE3 TRP A 428    13533  19537  12778  -3642   -792  -3394       C  
+ATOM   3238  CZ2 TRP A 428     -68.465   5.088  -2.589  1.00115.89           C  
+ANISOU 3238  CZ2 TRP A 428    13926  18431  11673  -4055   -452  -3735       C  
+ATOM   3239  CZ3 TRP A 428     -70.410   6.504  -2.401  1.00125.17           C  
+ANISOU 3239  CZ3 TRP A 428    14153  20239  13168  -3951  -1069  -3732       C  
+ATOM   3240  CH2 TRP A 428     -69.748   5.397  -2.942  1.00115.90           C  
+ANISOU 3240  CH2 TRP A 428    13495  18803  11737  -4168   -896  -3898       C  
+ATOM   3241  N   ASN A 429     -69.634  10.890  -0.975  1.00112.21           N  
+ANISOU 3241  N   ASN A 429    12083  18705  11846  -2564  -1193  -2651       N  
+ATOM   3242  CA  ASN A 429     -70.634  11.138  -2.008  1.00122.80           C  
+ANISOU 3242  CA  ASN A 429    13244  20387  13027  -2527  -1767  -2815       C  
+ATOM   3243  C   ASN A 429     -70.243  12.309  -2.897  1.00121.54           C  
+ANISOU 3243  C   ASN A 429    13399  20253  12530  -2141  -2122  -2507       C  
+ATOM   3244  O   ASN A 429     -70.574  12.326  -4.083  1.00124.03           O  
+ANISOU 3244  O   ASN A 429    13883  20753  12489  -2136  -2546  -2575       O  
+ATOM   3245  CB  ASN A 429     -72.011  11.381  -1.384  1.00126.36           C  
+ANISOU 3245  CB  ASN A 429    12977  21142  13892  -2521  -1992  -3039       C  
+ATOM   3246  CG  ASN A 429     -72.576  10.139  -0.713  1.00124.47           C  
+ANISOU 3246  CG  ASN A 429    12431  20937  13925  -3013  -1695  -3369       C  
+ATOM   3247  OD1 ASN A 429     -73.067  10.194   0.412  1.00127.87           O  
+ANISOU 3247  OD1 ASN A 429    12417  21430  14736  -3066  -1464  -3433       O  
+ATOM   3248  ND2 ASN A 429     -72.521   9.011  -1.416  1.00120.69           N  
+ANISOU 3248  ND2 ASN A 429    12218  20409  13231  -3393  -1698  -3585       N  
+ATOM   3249  N   LYS A 430     -69.542  13.288  -2.330  1.00119.35           N  
+ANISOU 3249  N   LYS A 430    13234  19774  12340  -1842  -1964  -2164       N  
+ATOM   3250  CA  LYS A 430     -69.052  14.405  -3.132  1.00127.15           C  
+ANISOU 3250  CA  LYS A 430    14602  20713  12995  -1533  -2251  -1818       C  
+ATOM   3251  C   LYS A 430     -67.968  13.958  -4.115  1.00127.61           C  
+ANISOU 3251  C   LYS A 430    15272  20670  12544  -1689  -2062  -1700       C  
+ATOM   3252  O   LYS A 430     -67.804  14.548  -5.183  1.00133.74           O  
+ANISOU 3252  O   LYS A 430    16409  21513  12892  -1567  -2371  -1509       O  
+ATOM   3253  CB  LYS A 430     -68.513  15.521  -2.232  1.00116.04           C  
+ANISOU 3253  CB  LYS A 430    13189  19069  11831  -1231  -2105  -1493       C  
+ATOM   3254  CG  LYS A 430     -67.965  16.715  -3.004  1.00112.68           C  
+ANISOU 3254  CG  LYS A 430    13205  18531  11079   -962  -2384  -1095       C  
+ATOM   3255  CD  LYS A 430     -67.396  17.789  -2.092  1.00110.58           C  
+ANISOU 3255  CD  LYS A 430    12963  17981  11071   -708  -2245   -795       C  
+ATOM   3256  CE  LYS A 430     -67.227  19.101  -2.847  1.00115.31           C  
+ANISOU 3256  CE  LYS A 430    13940  18468  11405   -430  -2669   -422       C  
+ATOM   3257  NZ  LYS A 430     -67.663  20.285  -2.056  1.00120.16           N  
+ANISOU 3257  NZ  LYS A 430    14342  18930  12385    -44  -2920   -315       N  
+ATOM   3258  N   VAL A 431     -67.242  12.903  -3.758  1.00118.42           N  
+ANISOU 3258  N   VAL A 431    14237  19348  11411  -1950  -1555  -1824       N  
+ATOM   3259  CA  VAL A 431     -66.156  12.405  -4.599  1.00115.85           C  
+ANISOU 3259  CA  VAL A 431    14440  18940  10640  -2070  -1302  -1770       C  
+ATOM   3260  C   VAL A 431     -66.599  11.285  -5.545  1.00124.18           C  
+ANISOU 3260  C   VAL A 431    15634  20158  11390  -2334  -1442  -2139       C  
+ATOM   3261  O   VAL A 431     -66.217  11.276  -6.713  1.00127.21           O  
+ANISOU 3261  O   VAL A 431    16442  20639  11253  -2342  -1546  -2107       O  
+ATOM   3262  CB  VAL A 431     -64.975  11.919  -3.732  1.00113.11           C  
+ANISOU 3262  CB  VAL A 431    14193  18300  10482  -2133   -694  -1704       C  
+ATOM   3263  CG1 VAL A 431     -64.039  11.028  -4.534  1.00108.70           C  
+ANISOU 3263  CG1 VAL A 431    14067  17699   9536  -2283   -401  -1817       C  
+ATOM   3264  CG2 VAL A 431     -64.219  13.114  -3.173  1.00120.40           C  
+ANISOU 3264  CG2 VAL A 431    15151  19065  11530  -1887   -575  -1299       C  
+ATOM   3265  N   ASN A 432     -67.423  10.361  -5.053  1.00121.87           N  
+ANISOU 3265  N   ASN A 432    15006  19899  11402  -2571  -1451  -2493       N  
+ATOM   3266  CA  ASN A 432     -67.895   9.247  -5.873  1.00117.95           C  
+ANISOU 3266  CA  ASN A 432    14633  19516  10665  -2867  -1606  -2882       C  
+ATOM   3267  C   ASN A 432     -68.662   9.777  -7.069  1.00123.74           C  
+ANISOU 3267  C   ASN A 432    15419  20572  11023  -2778  -2227  -2915       C  
+ATOM   3268  O   ASN A 432     -68.508   9.281  -8.184  1.00132.53           O  
+ANISOU 3268  O   ASN A 432    16931  21774  11651  -2891  -2356  -3070       O  
+ATOM   3269  CB  ASN A 432     -68.780   8.297  -5.058  1.00112.69           C  
+ANISOU 3269  CB  ASN A 432    13544  18829  10443  -3185  -1550  -3224       C  
+ATOM   3270  CG  ASN A 432     -69.320   7.141  -5.885  1.00125.19           C  
+ANISOU 3270  CG  ASN A 432    15257  20497  11813  -3536  -1750  -3649       C  
+ATOM   3271  OD1 ASN A 432     -68.576   6.482  -6.612  1.00123.91           O  
+ANISOU 3271  OD1 ASN A 432    15600  20207  11273  -3610  -1597  -3754       O  
+ATOM   3272  ND2 ASN A 432     -70.621   6.891  -5.776  1.00131.78           N  
+ANISOU 3272  ND2 ASN A 432    15617  21557  12896  -3758  -2093  -3922       N  
+ATOM   3273  N   GLU A 433     -69.493  10.785  -6.831  1.00126.73           N  
+ANISOU 3273  N   GLU A 433    15412  21124  11616  -2548  -2631  -2784       N  
+ATOM   3274  CA  GLU A 433     -70.077  11.559  -7.915  1.00135.16           C  
+ANISOU 3274  CA  GLU A 433    16586  22451  12316  -2347  -3266  -2705       C  
+ATOM   3275  C   GLU A 433     -69.001  12.533  -8.347  1.00135.57           C  
+ANISOU 3275  C   GLU A 433    17157  22361  11990  -2090  -3156  -2238       C  
+ATOM   3276  O   GLU A 433     -68.295  13.085  -7.500  1.00130.23           O  
+ANISOU 3276  O   GLU A 433    16454  21457  11570  -1953  -2791  -1957       O  
+ATOM   3277  CB  GLU A 433     -71.346  12.292  -7.480  1.00133.43           C  
+ANISOU 3277  CB  GLU A 433    15749  22451  12496  -2138  -3758  -2754       C  
+ATOM   3278  N   GLU A 434     -68.871  12.744  -9.651  1.00137.35           N  
+ANISOU 3278  N   GLU A 434    17867  22724  11594  -2057  -3466  -2156       N  
+ATOM   3279  CA  GLU A 434     -67.832  13.622 -10.187  1.00136.36           C  
+ANISOU 3279  CA  GLU A 434    18292  22486  11032  -1896  -3335  -1702       C  
+ATOM   3280  C   GLU A 434     -66.466  13.076  -9.784  1.00127.83           C  
+ANISOU 3280  C   GLU A 434    17433  21182   9955  -2048  -2573  -1646       C  
+ATOM   3281  O   GLU A 434     -65.634  13.805  -9.244  1.00112.72           O  
+ANISOU 3281  O   GLU A 434    15581  19072   8175  -1924  -2264  -1292       O  
+ATOM   3282  CB  GLU A 434     -67.979  15.062  -9.666  1.00134.03           C  
+ANISOU 3282  CB  GLU A 434    17857  22075  10992  -1550  -3574  -1296       C  
+ATOM   3283  CG  GLU A 434     -69.409  15.611  -9.500  1.00132.66           C  
+ANISOU 3283  CG  GLU A 434    17205  22074  11127  -1305  -4253  -1410       C  
+ATOM   3284  CD  GLU A 434     -70.434  15.023 -10.457  1.00145.31           C  
+ANISOU 3284  CD  GLU A 434    18750  24007  12455  -1404  -4813  -1764       C  
+ATOM   3285  OE1 GLU A 434     -70.245  15.119 -11.688  1.00150.68           O  
+ANISOU 3285  OE1 GLU A 434    19983  24789  12480  -1418  -5087  -1661       O  
+ATOM   3286  OE2 GLU A 434     -71.447  14.479  -9.969  1.00148.85           O  
+ANISOU 3286  OE2 GLU A 434    18592  24629  13335  -1485  -4987  -2149       O  
+ATOM   3287  N   PHE A 435     -66.260  11.786 -10.023  1.00130.23           N  
+ANISOU 3287  N   PHE A 435    17837  21504  10141  -2307  -2303  -2020       N  
+ATOM   3288  CA  PHE A 435     -65.092  11.065  -9.522  1.00120.59           C  
+ANISOU 3288  CA  PHE A 435    16732  20063   9025  -2420  -1616  -2070       C  
+ATOM   3289  C   PHE A 435     -63.786  11.275 -10.301  1.00121.60           C  
+ANISOU 3289  C   PHE A 435    17392  20196   8615  -2398  -1248  -1849       C  
+ATOM   3290  O   PHE A 435     -62.700  11.010  -9.780  1.00115.25           O  
+ANISOU 3290  O   PHE A 435    16615  19217   7958  -2405   -690  -1795       O  
+ATOM   3291  CB  PHE A 435     -65.428   9.573  -9.468  1.00125.78           C  
+ANISOU 3291  CB  PHE A 435    17317  20687   9786  -2685  -1506  -2582       C  
+ATOM   3292  CG  PHE A 435     -64.336   8.718  -8.893  1.00118.08           C  
+ANISOU 3292  CG  PHE A 435    16449  19446   8971  -2759   -867  -2683       C  
+ATOM   3293  CD1 PHE A 435     -64.155   8.629  -7.522  1.00109.31           C  
+ANISOU 3293  CD1 PHE A 435    14994  18087   8452  -2739   -570  -2616       C  
+ATOM   3294  CD2 PHE A 435     -63.505   7.984  -9.724  1.00110.60           C  
+ANISOU 3294  CD2 PHE A 435    15953  18501   7568  -2823   -583  -2870       C  
+ATOM   3295  CE1 PHE A 435     -63.155   7.836  -6.992  1.00100.79           C  
+ANISOU 3295  CE1 PHE A 435    14030  16746   7517  -2768    -47  -2707       C  
+ATOM   3296  CE2 PHE A 435     -62.507   7.191  -9.201  1.00107.71           C  
+ANISOU 3296  CE2 PHE A 435    15664  17885   7375  -2829    -37  -2991       C  
+ATOM   3297  CZ  PHE A 435     -62.331   7.115  -7.836  1.00107.41           C  
+ANISOU 3297  CZ  PHE A 435    15291  17581   7939  -2796    208  -2899       C  
+ATOM   3298  N   GLU A 436     -63.884  11.780 -11.526  1.00133.32           N  
+ANISOU 3298  N   GLU A 436    19285  21897   9474  -2372  -1561  -1715       N  
+ATOM   3299  CA  GLU A 436     -62.704  11.969 -12.368  1.00128.91           C  
+ANISOU 3299  CA  GLU A 436    19244  21409   8329  -2402  -1190  -1519       C  
+ATOM   3300  C   GLU A 436     -61.841  13.142 -11.909  1.00130.81           C  
+ANISOU 3300  C   GLU A 436    19503  21511   8690  -2290   -933   -995       C  
+ATOM   3301  O   GLU A 436     -60.684  13.268 -12.314  1.00139.38           O  
+ANISOU 3301  O   GLU A 436    20889  22631   9440  -2353   -474   -826       O  
+ATOM   3302  CB  GLU A 436     -63.121  12.170 -13.826  1.00128.97           C  
+ANISOU 3302  CB  GLU A 436    19741  21697   7566  -2437  -1620  -1514       C  
+ATOM   3303  N   THR A 437     -62.401  13.990 -11.054  1.00121.56           N  
+ANISOU 3303  N   THR A 437    17993  20189   8006  -2133  -1220   -766       N  
+ATOM   3304  CA  THR A 437     -61.706  15.188 -10.595  1.00117.29           C  
+ANISOU 3304  CA  THR A 437    17486  19472   7608  -2032  -1074   -275       C  
+ATOM   3305  C   THR A 437     -60.784  14.897  -9.413  1.00113.75           C  
+ANISOU 3305  C   THR A 437    16733  18805   7683  -2049   -497   -289       C  
+ATOM   3306  O   THR A 437     -60.032  15.768  -8.975  1.00108.83           O  
+ANISOU 3306  O   THR A 437    16123  18026   7202  -2009   -299     74       O  
+ATOM   3307  CB  THR A 437     -62.700  16.291 -10.189  1.00117.27           C  
+ANISOU 3307  CB  THR A 437    17289  19372   7895  -1803  -1666    -43       C  
+ATOM   3308  N   TYR A 438     -60.849  13.675  -8.898  1.00113.94           N  
+ANISOU 3308  N   TYR A 438    16507  18795   7990  -2116   -262   -706       N  
+ATOM   3309  CA  TYR A 438     -60.068  13.299  -7.726  1.00108.77           C  
+ANISOU 3309  CA  TYR A 438    15574  17916   7838  -2103    215   -747       C  
+ATOM   3310  C   TYR A 438     -59.106  12.156  -8.044  1.00104.88           C  
+ANISOU 3310  C   TYR A 438    15239  17454   7158  -2207    723  -1027       C  
+ATOM   3311  O   TYR A 438     -57.987  12.115  -7.533  1.00 87.60           O  
+ANISOU 3311  O   TYR A 438    12984  15152   5147  -2179   1177   -942       O  
+ATOM   3312  CB  TYR A 438     -60.994  12.915  -6.570  1.00104.78           C  
+ANISOU 3312  CB  TYR A 438    14619  17269   7925  -2060     49   -957       C  
+ATOM   3313  CG  TYR A 438     -61.867  14.057  -6.100  1.00110.18           C  
+ANISOU 3313  CG  TYR A 438    15075  17922   8868  -1894   -393   -723       C  
+ATOM   3314  CD1 TYR A 438     -61.458  14.891  -5.069  1.00105.60           C  
+ANISOU 3314  CD1 TYR A 438    14314  17127   8681  -1760   -274   -450       C  
+ATOM   3315  CD2 TYR A 438     -63.098  14.305  -6.694  1.00116.56           C  
+ANISOU 3315  CD2 TYR A 438    15846  18913   9529  -1846   -956   -803       C  
+ATOM   3316  CE1 TYR A 438     -62.252  15.939  -4.639  1.00106.20           C  
+ANISOU 3316  CE1 TYR A 438    14203  17154   8994  -1565   -679   -277       C  
+ATOM   3317  CE2 TYR A 438     -63.898  15.350  -6.272  1.00114.50           C  
+ANISOU 3317  CE2 TYR A 438    15356  18625   9526  -1630  -1376   -625       C  
+ATOM   3318  CZ  TYR A 438     -63.470  16.163  -5.244  1.00113.91           C  
+ANISOU 3318  CZ  TYR A 438    15129  18316   9837  -1482  -1223   -369       C  
+ATOM   3319  OH  TYR A 438     -64.264  17.204  -4.820  1.00120.40           O  
+ANISOU 3319  OH  TYR A 438    15742  19089  10916  -1225  -1642   -231       O  
+ATOM   3320  N   TYR A 439     -59.551  11.229  -8.887  1.00105.81           N  
+ANISOU 3320  N   TYR A 439    15556  17720   6927  -2306    618  -1387       N  
+ATOM   3321  CA  TYR A 439     -58.727  10.092  -9.289  1.00102.29           C  
+ANISOU 3321  CA  TYR A 439    15303  17293   6268  -2363   1056  -1720       C  
+ATOM   3322  C   TYR A 439     -58.806   9.812 -10.787  1.00118.84           C  
+ANISOU 3322  C   TYR A 439    17852  19674   7628  -2453    962  -1887       C  
+ATOM   3323  O   TYR A 439     -59.557   8.937 -11.219  1.00119.50           O  
+ANISOU 3323  O   TYR A 439    18035  19799   7571  -2539    723  -2276       O  
+ATOM   3324  CB  TYR A 439     -59.125   8.832  -8.517  1.00 95.18           C  
+ANISOU 3324  CB  TYR A 439    14198  16168   5799  -2404   1103  -2134       C  
+ATOM   3325  CG  TYR A 439     -58.906   8.919  -7.025  1.00 98.42           C  
+ANISOU 3325  CG  TYR A 439    14232  16294   6869  -2323   1272  -2009       C  
+ATOM   3326  CD1 TYR A 439     -59.867   9.472  -6.188  1.00 92.49           C  
+ANISOU 3326  CD1 TYR A 439    13157  15467   6517  -2317    947  -1870       C  
+ATOM   3327  CD2 TYR A 439     -57.734   8.446  -6.454  1.00 96.93           C  
+ANISOU 3327  CD2 TYR A 439    14012  15929   6889  -2231   1748  -2051       C  
+ATOM   3328  CE1 TYR A 439     -59.663   9.548  -4.823  1.00 87.17           C  
+ANISOU 3328  CE1 TYR A 439    12185  14549   6387  -2247   1114  -1767       C  
+ATOM   3329  CE2 TYR A 439     -57.522   8.520  -5.096  1.00 96.71           C  
+ANISOU 3329  CE2 TYR A 439    13687  15641   7416  -2153   1866  -1934       C  
+ATOM   3330  CZ  TYR A 439     -58.487   9.070  -4.285  1.00 93.38           C  
+ANISOU 3330  CZ  TYR A 439    12996  15148   7338  -2174   1559  -1789       C  
+ATOM   3331  OH  TYR A 439     -58.267   9.138  -2.931  1.00 94.42           O  
+ANISOU 3331  OH  TYR A 439    12875  15035   7965  -2100   1691  -1684       O  
+ATOM   3332  N   PRO A 440     -58.029  10.558 -11.587  1.00114.24           N  
+ANISOU 3332  N   PRO A 440    17559  19279   6569  -2452   1150  -1590       N  
+ATOM   3333  CA  PRO A 440     -57.990  10.316 -13.032  1.00117.06           C  
+ANISOU 3333  CA  PRO A 440    18322  19782   6375  -2428   1090  -1681       C  
+ATOM   3334  C   PRO A 440     -57.388   8.950 -13.364  1.00130.85           C  
+ANISOU 3334  C   PRO A 440    20137  21446   8134  -2350   1461  -2135       C  
+ATOM   3335  O   PRO A 440     -56.175   8.820 -13.527  1.00141.51           O  
+ANISOU 3335  O   PRO A 440    21488  22773   9505  -2228   1956  -2093       O  
+ATOM   3336  CB  PRO A 440     -57.112  11.456 -13.555  1.00115.85           C  
+ANISOU 3336  CB  PRO A 440    18344  19699   5973  -2393   1302  -1186       C  
+ATOM   3337  CG  PRO A 440     -56.261  11.839 -12.392  1.00108.91           C  
+ANISOU 3337  CG  PRO A 440    17111  18657   5611  -2370   1677   -978       C  
+ATOM   3338  CD  PRO A 440     -57.135  11.658 -11.185  1.00103.17           C  
+ANISOU 3338  CD  PRO A 440    16070  17829   5301  -2412   1411  -1112       C  
+ATOM   3339  N   GLY A 441     -58.253   7.946 -13.463  1.00135.30           N  
+ANISOU 3339  N   GLY A 441    20744  21962   8702  -2416   1187  -2575       N  
+ATOM   3340  CA  GLY A 441     -57.847   6.577 -13.727  1.00134.15           C  
+ANISOU 3340  CA  GLY A 441    20708  21676   8588  -2340   1445  -3040       C  
+ATOM   3341  C   GLY A 441     -58.913   5.619 -13.231  1.00134.58           C  
+ANISOU 3341  C   GLY A 441    20667  21564   8905  -2496   1120  -3451       C  
+ATOM   3342  O   GLY A 441     -59.887   6.044 -12.609  1.00135.08           O  
+ANISOU 3342  O   GLY A 441    20503  21661   9161  -2656    750  -3374       O  
+ATOM   3343  N   ALA A 442     -58.739   4.327 -13.495  1.00135.82           N  
+ANISOU 3343  N   ALA A 442    20984  21536   9085  -2454   1248  -3895       N  
+ATOM   3344  CA  ALA A 442     -59.751   3.346 -13.111  1.00135.87           C  
+ANISOU 3344  CA  ALA A 442    20946  21339   9341  -2654    937  -4294       C  
+ATOM   3345  C   ALA A 442     -59.178   2.050 -12.540  1.00141.81           C  
+ANISOU 3345  C   ALA A 442    21725  21703  10455  -2580   1265  -4643       C  
+ATOM   3346  O   ALA A 442     -59.931   1.143 -12.184  1.00143.90           O  
+ANISOU 3346  O   ALA A 442    21992  21723  10960  -2774   1050  -4968       O  
+ATOM   3347  CB  ALA A 442     -60.641   3.033 -14.306  1.00123.52           C  
+ANISOU 3347  CB  ALA A 442    19672  19925   7334  -2754    476  -4537       C  
+ATOM   3348  N   ASP A 443     -57.855   1.956 -12.454  1.00144.25           N  
+ANISOU 3348  N   ASP A 443    22046  21941  10820  -2300   1757  -4572       N  
+ATOM   3349  CA  ASP A 443     -57.222   0.749 -11.931  1.00138.27           C  
+ANISOU 3349  CA  ASP A 443    21337  20803  10397  -2151   2034  -4891       C  
+ATOM   3350  C   ASP A 443     -55.817   1.022 -11.407  1.00133.18           C  
+ANISOU 3350  C   ASP A 443    20500  20128   9974  -1847   2526  -4682       C  
+ATOM   3351  O   ASP A 443     -55.148   0.119 -10.901  1.00130.40           O  
+ANISOU 3351  O   ASP A 443    20159  19469   9919  -1652   2755  -4905       O  
+ATOM   3352  CB  ASP A 443     -57.173  -0.336 -13.010  1.00122.40           C  
+ANISOU 3352  CB  ASP A 443    19724  18723   8060  -2051   1985  -5333       C  
+ATOM   3353  N   ARG A 445     -59.692  -2.433 -10.112  1.00122.26           N  
+ANISOU 3353  N   ARG A 445    19482  17594   9378  -2903   1372  -5839       N  
+ATOM   3354  CA  ARG A 445     -59.685  -2.623  -8.666  1.00121.58           C  
+ANISOU 3354  CA  ARG A 445    19205  17168   9821  -3008   1513  -5736       C  
+ATOM   3355  C   ARG A 445     -59.966  -1.320  -7.929  1.00120.69           C  
+ANISOU 3355  C   ARG A 445    18677  17353   9827  -3109   1511  -5336       C  
+ATOM   3356  O   ARG A 445     -60.696  -1.302  -6.938  1.00123.86           O  
+ANISOU 3356  O   ARG A 445    18846  17614  10601  -3370   1396  -5256       O  
+ATOM   3357  CB  ARG A 445     -58.341  -3.196  -8.208  1.00117.57           C  
+ANISOU 3357  CB  ARG A 445    18828  16330   9511  -2617   1923  -5772       C  
+ATOM   3358  CG  ARG A 445     -58.416  -4.617  -7.672  1.00123.45           C  
+ANISOU 3358  CG  ARG A 445    19858  16468  10580  -2679   1894  -6079       C  
+ATOM   3359  CD  ARG A 445     -59.096  -4.657  -6.311  1.00125.06           C  
+ANISOU 3359  CD  ARG A 445    19897  16387  11234  -3020   1834  -5930       C  
+ATOM   3360  NE  ARG A 445     -59.073  -5.995  -5.725  1.00133.57           N  
+ANISOU 3360  NE  ARG A 445    21299  16825  12627  -3077   1825  -6146       N  
+ATOM   3361  CZ  ARG A 445     -59.767  -6.351  -4.649  1.00123.50           C  
+ANISOU 3361  CZ  ARG A 445    20000  15204  11719  -3443   1747  -6065       C  
+ATOM   3362  NH1 ARG A 445     -60.545  -5.470  -4.037  1.00112.68           N  
+ANISOU 3362  NH1 ARG A 445    18249  14107  10457  -3765   1684  -5821       N  
+ATOM   3363  NH2 ARG A 445     -59.684  -7.591  -4.184  1.00123.82           N  
+ANISOU 3363  NH2 ARG A 445    20403  14630  12014  -3481   1727  -6222       N  
+HETATM 3364  N   MSE A 446     -59.384  -0.233  -8.426  1.00121.02           N  
+ANISOU 3364  N   MSE A 446    18616  17786   9580  -2882   1629  -5049       N  
+HETATM 3365  CA  MSE A 446     -59.425   1.053  -7.740  1.00115.45           C  
+ANISOU 3365  CA  MSE A 446    17531  17307   9028  -2866   1645  -4601       C  
+HETATM 3366  C   MSE A 446     -60.840   1.609  -7.596  1.00115.71           C  
+ANISOU 3366  C   MSE A 446    17274  17511   9178  -3137   1180  -4469       C  
+HETATM 3367  O   MSE A 446     -61.214   2.093  -6.528  1.00107.86           O  
+ANISOU 3367  O   MSE A 446    15913  16442   8627  -3172   1142  -4197       O  
+HETATM 3368  CB  MSE A 446     -58.543   2.066  -8.472  1.00117.51           C  
+ANISOU 3368  CB  MSE A 446    17816  17935   8898  -2623   1839  -4330       C  
+HETATM 3369  CG  MSE A 446     -58.309   3.354  -7.701  1.00101.62           C  
+ANISOU 3369  CG  MSE A 446    15435  16035   7141  -2525   1896  -3813       C  
+HETATM 3370 SE   MSE A 446     -57.063   4.548  -8.606  1.00182.12          SE  
+ANISOU 3370 SE   MSE A 446    25706  26623  16867  -2297   2199  -3457      SE  
+HETATM 3371  CE  MSE A 446     -55.522   3.356  -8.694  1.00102.34           C  
+ANISOU 3371  CE  MSE A 446    15720  16245   6919  -1950   2704  -3724       C  
+ATOM   3372  N   LYS A 447     -61.622   1.539  -8.668  1.00124.70           N  
+ANISOU 3372  N   LYS A 447    18566  18899   9915  -3308    820  -4686       N  
+ATOM   3373  CA  LYS A 447     -62.979   2.073  -8.647  1.00121.48           C  
+ANISOU 3373  CA  LYS A 447    17841  18710   9606  -3527    330  -4605       C  
+ATOM   3374  C   LYS A 447     -63.893   1.233  -7.758  1.00123.60           C  
+ANISOU 3374  C   LYS A 447    17891  18700  10370  -3851    209  -4813       C  
+ATOM   3375  O   LYS A 447     -64.759   1.766  -7.064  1.00123.08           O  
+ANISOU 3375  O   LYS A 447    17380  18734  10652  -3967      9  -4636       O  
+ATOM   3376  CB  LYS A 447     -63.548   2.146 -10.066  1.00123.26           C  
+ANISOU 3376  CB  LYS A 447    18313  19274   9245  -3618    -70  -4813       C  
+ATOM   3377  N   LYS A 448     -63.695  -0.081  -7.785  1.00123.02           N  
+ANISOU 3377  N   LYS A 448    18146  18274  10323  -4001    343  -5196       N  
+ATOM   3378  CA  LYS A 448     -64.464  -0.994  -6.945  1.00117.17           C  
+ANISOU 3378  CA  LYS A 448    17290  17202  10029  -4369    279  -5385       C  
+ATOM   3379  C   LYS A 448     -64.100  -0.838  -5.470  1.00123.63           C  
+ANISOU 3379  C   LYS A 448    17867  17749  11358  -4290    600  -5068       C  
+ATOM   3380  O   LYS A 448     -64.973  -0.839  -4.597  1.00133.64           O  
+ANISOU 3380  O   LYS A 448    18790  18977  13011  -4563    509  -4993       O  
+ATOM   3381  CB  LYS A 448     -64.244  -2.441  -7.389  1.00114.15           C  
+ANISOU 3381  CB  LYS A 448    17408  16420   9543  -4503    329  -5835       C  
+ATOM   3382  N   LEU A 449     -62.805  -0.697  -5.202  1.00114.95           N  
+ANISOU 3382  N   LEU A 449    16938  16494  10244  -3919    977  -4894       N  
+ATOM   3383  CA  LEU A 449     -62.305  -0.575  -3.837  1.00 97.93           C  
+ANISOU 3383  CA  LEU A 449    14620  14065   8522  -3797   1266  -4605       C  
+ATOM   3384  C   LEU A 449     -62.802   0.705  -3.179  1.00102.28           C  
+ANISOU 3384  C   LEU A 449    14664  14915   9285  -3760   1173  -4209       C  
+ATOM   3385  O   LEU A 449     -63.178   0.702  -2.006  1.00102.39           O  
+ANISOU 3385  O   LEU A 449    14442  14771   9689  -3886   1243  -4063       O  
+ATOM   3386  CB  LEU A 449     -60.776  -0.614  -3.819  1.00 93.49           C  
+ANISOU 3386  CB  LEU A 449    14297  13346   7879  -3375   1637  -4531       C  
+ATOM   3387  N   PHE A 450     -62.789   1.798  -3.937  1.00102.09           N  
+ANISOU 3387  N   PHE A 450    14510  15302   8976  -3580   1019  -4038       N  
+ATOM   3388  CA  PHE A 450     -63.291   3.075  -3.446  1.00 96.90           C  
+ANISOU 3388  CA  PHE A 450    13414  14915   8491  -3500    871  -3690       C  
+ATOM   3389  C   PHE A 450     -64.764   2.952  -3.074  1.00105.26           C  
+ANISOU 3389  C   PHE A 450    14113  16083   9799  -3834    571  -3814       C  
+ATOM   3390  O   PHE A 450     -65.195   3.436  -2.028  1.00107.18           O  
+ANISOU 3390  O   PHE A 450    13986  16337  10401  -3851    606  -3624       O  
+ATOM   3391  CB  PHE A 450     -63.095   4.173  -4.493  1.00 96.19           C  
+ANISOU 3391  CB  PHE A 450    13352  15201   7995  -3282    692  -3509       C  
+ATOM   3392  N   GLY A 451     -65.527   2.299  -3.944  1.00111.77           N  
+ANISOU 3392  N   GLY A 451    15032  17009  10425  -4107    283  -4160       N  
+ATOM   3393  CA  GLY A 451     -66.941   2.070  -3.713  1.00113.87           C  
+ANISOU 3393  CA  GLY A 451    14920  17420  10926  -4478    -14  -4343       C  
+ATOM   3394  C   GLY A 451     -67.223   1.140  -2.549  1.00109.75           C  
+ANISOU 3394  C   GLY A 451    14333  16548  10819  -4812    230  -4433       C  
+ATOM   3395  O   GLY A 451     -68.296   1.193  -1.947  1.00112.40           O  
+ANISOU 3395  O   GLY A 451    14227  17026  11455  -5095    118  -4469       O  
+ATOM   3396  N   GLU A 452     -66.258   0.286  -2.226  1.00107.48           N  
+ANISOU 3396  N   GLU A 452    14490  15806  10543  -4777    566  -4469       N  
+ATOM   3397  CA  GLU A 452     -66.437  -0.691  -1.157  1.00113.43           C  
+ANISOU 3397  CA  GLU A 452    15319  16144  11635  -5101    789  -4531       C  
+ATOM   3398  C   GLU A 452     -66.299  -0.087   0.242  1.00120.30           C  
+ANISOU 3398  C   GLU A 452    15905  16964  12838  -4986   1047  -4173       C  
+ATOM   3399  O   GLU A 452     -66.489  -0.782   1.240  1.00124.35           O  
+ANISOU 3399  O   GLU A 452    16476  17160  13609  -5262   1244  -4163       O  
+ATOM   3400  CB  GLU A 452     -65.433  -1.835  -1.321  1.00114.98           C  
+ANISOU 3400  CB  GLU A 452    16143  15825  11719  -5043   1003  -4707       C  
+ATOM   3401  N   LEU A 453     -65.962   1.198   0.315  1.00122.32           N  
+ANISOU 3401  N   LEU A 453    15903  17508  13063  -4594   1040  -3877       N  
+ATOM   3402  CA  LEU A 453     -65.784   1.867   1.604  1.00112.75           C  
+ANISOU 3402  CA  LEU A 453    14446  16262  12133  -4443   1259  -3557       C  
+ATOM   3403  C   LEU A 453     -67.044   2.525   2.176  1.00118.71           C  
+ANISOU 3403  C   LEU A 453    14617  17364  13125  -4618   1126  -3518       C  
+ATOM   3404  O   LEU A 453     -67.120   2.773   3.378  1.00121.70           O  
+ANISOU 3404  O   LEU A 453    14814  17675  13749  -4622   1342  -3341       O  
+ATOM   3405  CB  LEU A 453     -64.678   2.918   1.491  1.00102.96           C  
+ANISOU 3405  CB  LEU A 453    13255  15096  10770  -3935   1339  -3261       C  
+ATOM   3406  N   ASN A 454     -68.034   2.798   1.331  1.00117.66           N  
+ANISOU 3406  N   ASN A 454    14180  17615  12909  -4744    766  -3704       N  
+ATOM   3407  CA  ASN A 454     -69.249   3.463   1.799  1.00106.56           C  
+ANISOU 3407  CA  ASN A 454    12146  16594  11746  -4849    613  -3714       C  
+ATOM   3408  C   ASN A 454     -70.409   2.495   1.970  1.00103.73           C  
+ANISOU 3408  C   ASN A 454    11554  16288  11571  -5437    572  -4025       C  
+ATOM   3409  O   ASN A 454     -71.560   2.913   2.082  1.00109.55           O  
+ANISOU 3409  O   ASN A 454    11705  17429  12489  -5577    383  -4138       O  
+ATOM   3410  CB  ASN A 454     -69.658   4.581   0.840  1.00109.93           C  
+ANISOU 3410  CB  ASN A 454    12301  17457  12010  -4546    182  -3691       C  
+ATOM   3411  N   ALA A 457     -70.604  -1.723   4.838  1.00133.11           N  
+ANISOU 3411  N   ALA A 457    16249  18527  15798  -7131   1640  -4209       N  
+ATOM   3412  CA  ALA A 457     -70.815  -2.303   6.160  1.00133.55           C  
+ANISOU 3412  CA  ALA A 457    16417  18303  16023  -7407   2000  -4017       C  
+ATOM   3413  C   ALA A 457     -70.349  -3.756   6.206  1.00129.18           C  
+ANISOU 3413  C   ALA A 457    16597  17077  15410  -7644   2092  -4042       C  
+ATOM   3414  O   ALA A 457     -71.151  -4.690   6.276  1.00110.48           O  
+ANISOU 3414  O   ALA A 457    14278  14584  13114  -8043   2082  -4109       O  
+ATOM   3415  CB  ALA A 457     -72.272  -2.194   6.561  1.00131.34           C  
+ANISOU 3415  CB  ALA A 457    15529  18446  15928  -7660   2001  -4038       C  
+ATOM   3416  N   LEU A 458     -69.033  -3.918   6.153  1.00129.50           N  
+ANISOU 3416  N   LEU A 458    17202  16677  15324  -7367   2164  -3996       N  
+ATOM   3417  CA  LEU A 458     -68.362  -5.201   6.320  1.00123.65           C  
+ANISOU 3417  CA  LEU A 458    17213  15230  14536  -7431   2251  -3985       C  
+ATOM   3418  C   LEU A 458     -67.843  -5.306   7.747  1.00120.26           C  
+ANISOU 3418  C   LEU A 458    17057  14455  14182  -7359   2569  -3636       C  
+ATOM   3419  O   LEU A 458     -68.247  -4.537   8.622  1.00122.50           O  
+ANISOU 3419  O   LEU A 458    16923  15071  14550  -7352   2737  -3425       O  
+ATOM   3420  CB  LEU A 458     -67.215  -5.359   5.316  1.00119.94           C  
+ANISOU 3420  CB  LEU A 458    17198  14510  13865  -7017   2106  -4166       C  
+ATOM   3421  N   SER A 459     -66.936  -6.248   7.973  1.00112.80           N  
+ANISOU 3421  N   SER A 459    16825  12848  13187  -7243   2622  -3582       N  
+ATOM   3422  CA  SER A 459     -66.354  -6.454   9.290  1.00107.91           C  
+ANISOU 3422  CA  SER A 459    16565  11837  12597  -7132   2857  -3246       C  
+ATOM   3423  C   SER A 459     -65.233  -5.442   9.483  1.00105.00           C  
+ANISOU 3423  C   SER A 459    16139  11560  12198  -6533   2909  -3094       C  
+ATOM   3424  O   SER A 459     -65.008  -4.592   8.621  1.00105.63           O  
+ANISOU 3424  O   SER A 459    15850  12067  12218  -6150   2767  -3183       O  
+ATOM   3425  CB  SER A 459     -65.813  -7.876   9.442  1.00106.90           C  
+ANISOU 3425  CB  SER A 459    17215  10965  12438  -7144   2818  -3225       C  
+ATOM   3426  OG  SER A 459     -64.454  -7.937   9.035  1.00113.79           O  
+ANISOU 3426  OG  SER A 459    18515  11470  13251  -6624   2749  -3309       O  
+ATOM   3427  N   ILE A 460     -64.540  -5.518  10.614  1.00100.63           N  
+ANISOU 3427  N   ILE A 460    15916  10663  11654  -6335   3070  -2800       N  
+ATOM   3428  CA  ILE A 460     -63.457  -4.582  10.893  1.00 93.54           C  
+ANISOU 3428  CA  ILE A 460    14911   9896  10734  -5655   3076  -2592       C  
+ATOM   3429  C   ILE A 460     -62.233  -4.938  10.058  1.00100.46           C  
+ANISOU 3429  C   ILE A 460    16134  10485  11550  -5143   2928  -2730       C  
+ATOM   3430  O   ILE A 460     -61.637  -4.069   9.413  1.00104.89           O  
+ANISOU 3430  O   ILE A 460    16386  11399  12068  -4681   2858  -2750       O  
+ATOM   3431  CB  ILE A 460     -63.079  -4.575  12.386  1.00 88.38           C  
+ANISOU 3431  CB  ILE A 460    14521   8968  10090  -5596   3253  -2252       C  
+ATOM   3432  N   GLU A 461     -61.867  -6.217  10.073  1.00102.79           N  
+ANISOU 3432  N   GLU A 461    17078  10135  11840  -5231   2890  -2833       N  
+ATOM   3433  CA  GLU A 461     -60.757  -6.707   9.266  1.00104.69           C  
+ANISOU 3433  CA  GLU A 461    17666  10079  12034  -4748   2766  -3035       C  
+ATOM   3434  C   GLU A 461     -60.967  -6.400   7.785  1.00109.07           C  
+ANISOU 3434  C   GLU A 461    17912  11054  12475  -4698   2649  -3355       C  
+ATOM   3435  O   GLU A 461     -60.034  -5.992   7.094  1.00114.34           O  
+ANISOU 3435  O   GLU A 461    18496  11884  13063  -4176   2619  -3436       O  
+ATOM   3436  CB  GLU A 461     -60.574  -8.215   9.457  1.00113.02           C  
+ANISOU 3436  CB  GLU A 461    19496  10337  13111  -4922   2709  -3151       C  
+ATOM   3437  CG  GLU A 461     -59.631  -8.848   8.439  1.00120.21           C  
+ANISOU 3437  CG  GLU A 461    20749  10957  13969  -4471   2575  -3479       C  
+ATOM   3438  CD  GLU A 461     -59.122 -10.213   8.862  1.00124.62           C  
+ANISOU 3438  CD  GLU A 461    22019  10740  14591  -4348   2462  -3464       C  
+ATOM   3439  OE1 GLU A 461     -59.940 -11.149   8.973  1.00117.10           O  
+ANISOU 3439  OE1 GLU A 461    21306   9530  13659  -4802   2377  -3440       O  
+ATOM   3440  OE2 GLU A 461     -57.900 -10.350   9.080  1.00133.89           O  
+ANISOU 3440  OE2 GLU A 461    23439  11625  15808  -3741   2423  -3444       O  
+ATOM   3441  N   GLU A 462     -62.193  -6.586   7.304  1.00112.62           N  
+ANISOU 3441  N   GLU A 462    18185  11701  12903  -5256   2582  -3536       N  
+ATOM   3442  CA  GLU A 462     -62.492  -6.395   5.886  1.00117.19           C  
+ANISOU 3442  CA  GLU A 462    18544  12650  13333  -5258   2417  -3855       C  
+ATOM   3443  C   GLU A 462     -62.404  -4.929   5.464  1.00112.87           C  
+ANISOU 3443  C   GLU A 462    17381  12796  12708  -4923   2397  -3731       C  
+ATOM   3444  O   GLU A 462     -61.820  -4.607   4.426  1.00110.83           O  
+ANISOU 3444  O   GLU A 462    17088  12751  12273  -4570   2323  -3877       O  
+ATOM   3445  CB  GLU A 462     -63.882  -6.947   5.559  1.00121.02           C  
+ANISOU 3445  CB  GLU A 462    18955  13187  13840  -5970   2303  -4079       C  
+ATOM   3446  N   LEU A 463     -62.975  -4.044   6.277  1.00109.41           N  
+ANISOU 3446  N   LEU A 463    16493  12693  12386  -5034   2473  -3465       N  
+ATOM   3447  CA  LEU A 463     -62.953  -2.614   5.987  1.00105.36           C  
+ANISOU 3447  CA  LEU A 463    15434  12772  11826  -4727   2428  -3322       C  
+ATOM   3448  C   LEU A 463     -61.526  -2.081   6.051  1.00 95.71           C  
+ANISOU 3448  C   LEU A 463    14304  11499  10562  -4116   2512  -3148       C  
+ATOM   3449  O   LEU A 463     -61.096  -1.305   5.187  1.00 91.11           O  
+ANISOU 3449  O   LEU A 463    13520  11260   9836  -3807   2445  -3161       O  
+ATOM   3450  CB  LEU A 463     -63.852  -1.848   6.959  1.00104.59           C  
+ANISOU 3450  CB  LEU A 463    14874  12982  11883  -4946   2502  -3107       C  
+ATOM   3451  CG  LEU A 463     -64.097  -0.379   6.609  1.00 97.09           C  
+ANISOU 3451  CG  LEU A 463    13356  12628  10906  -4687   2393  -3001       C  
+ATOM   3452  CD1 LEU A 463     -64.696  -0.255   5.217  1.00 97.47           C  
+ANISOU 3452  CD1 LEU A 463    13216  13019  10799  -4782   2130  -3261       C  
+ATOM   3453  CD2 LEU A 463     -64.994   0.282   7.644  1.00 90.48           C  
+ANISOU 3453  CD2 LEU A 463    12084  12055  10237  -4872   2484  -2844       C  
+ATOM   3454  N   ILE A 464     -60.797  -2.506   7.080  1.00 96.09           N  
+ANISOU 3454  N   ILE A 464    14664  11119  10729  -3964   2650  -2981       N  
+ATOM   3455  CA  ILE A 464     -59.403  -2.115   7.236  1.00 97.73           C  
+ANISOU 3455  CA  ILE A 464    14940  11251  10941  -3402   2714  -2841       C  
+ATOM   3456  C   ILE A 464     -58.602  -2.580   6.024  1.00102.25           C  
+ANISOU 3456  C   ILE A 464    15729  11762  11358  -3124   2679  -3116       C  
+ATOM   3457  O   ILE A 464     -57.800  -1.824   5.481  1.00 93.56           O  
+ANISOU 3457  O   ILE A 464    14424  10952  10172  -2747   2711  -3076       O  
+ATOM   3458  CB  ILE A 464     -58.787  -2.688   8.529  1.00 93.30           C  
+ANISOU 3458  CB  ILE A 464    14742  10184  10523  -3292   2803  -2656       C  
+ATOM   3459  CG1 ILE A 464     -59.313  -1.927   9.747  1.00 86.48           C  
+ANISOU 3459  CG1 ILE A 464    13619   9484   9756  -3436   2878  -2352       C  
+ATOM   3460  CG2 ILE A 464     -57.270  -2.603   8.488  1.00 85.48           C  
+ANISOU 3460  CG2 ILE A 464    13867   9057   9555  -2703   2822  -2622       C  
+ATOM   3461  CD1 ILE A 464     -58.966  -2.576  11.068  1.00 87.11           C  
+ANISOU 3461  CD1 ILE A 464    14122   9065   9913  -3446   2948  -2161       C  
+ATOM   3462  N   ASN A 465     -58.838  -3.815   5.592  1.00102.05           N  
+ANISOU 3462  N   ASN A 465    16126  11364  11284  -3333   2627  -3407       N  
+ATOM   3463  CA  ASN A 465     -58.173  -4.342   4.404  1.00105.79           C  
+ANISOU 3463  CA  ASN A 465    16839  11778  11579  -3081   2604  -3736       C  
+ATOM   3464  C   ASN A 465     -58.489  -3.517   3.159  1.00108.13           C  
+ANISOU 3464  C   ASN A 465    16791  12667  11627  -3086   2535  -3844       C  
+ATOM   3465  O   ASN A 465     -57.606  -3.257   2.335  1.00107.72           O  
+ANISOU 3465  O   ASN A 465    16728  12802  11397  -2717   2604  -3947       O  
+ATOM   3466  CB  ASN A 465     -58.573  -5.800   4.169  1.00101.76           C  
+ANISOU 3466  CB  ASN A 465    16869  10739  11058  -3374   2518  -4057       C  
+ATOM   3467  CG  ASN A 465     -57.906  -6.754   5.140  1.00109.05           C  
+ANISOU 3467  CG  ASN A 465    18291  10979  12164  -3216   2560  -3997       C  
+ATOM   3468  OD1 ASN A 465     -56.842  -6.462   5.684  1.00114.24           O  
+ANISOU 3468  OD1 ASN A 465    18923  11567  12914  -2740   2640  -3823       O  
+ATOM   3469  ND2 ASN A 465     -58.533  -7.903   5.364  1.00111.89           N  
+ANISOU 3469  ND2 ASN A 465    19122  10816  12577  -3627   2478  -4136       N  
+ATOM   3470  N   THR A 466     -59.745  -3.090   3.039  1.00 96.31           N  
+ANISOU 3470  N   THR A 466    15005  11479  10110  -3499   2401  -3815       N  
+ATOM   3471  CA  THR A 466     -60.163  -2.231   1.934  1.00 89.86           C  
+ANISOU 3471  CA  THR A 466    13872  11220   9052  -3508   2268  -3872       C  
+ATOM   3472  C   THR A 466     -59.367  -0.929   1.912  1.00 94.73           C  
+ANISOU 3472  C   THR A 466    14174  12198   9621  -3101   2360  -3582       C  
+ATOM   3473  O   THR A 466     -58.750  -0.580   0.899  1.00 96.26           O  
+ANISOU 3473  O   THR A 466    14384  12637   9554  -2859   2384  -3659       O  
+ATOM   3474  CB  THR A 466     -61.666  -1.898   2.015  1.00 91.72           C  
+ANISOU 3474  CB  THR A 466    13766  11737   9347  -3972   2075  -3859       C  
+ATOM   3475  OG1 THR A 466     -62.429  -3.111   2.018  1.00103.81           O  
+ANISOU 3475  OG1 THR A 466    15567  12941  10935  -4431   1993  -4132       O  
+ATOM   3476  CG2 THR A 466     -62.088  -1.039   0.831  1.00 92.31           C  
+ANISOU 3476  CG2 THR A 466    13566  12354   9153  -3935   1866  -3919       C  
+ATOM   3477  N   ILE A 467     -59.379  -0.222   3.040  1.00 92.60           N  
+ANISOU 3477  N   ILE A 467    13645  11952   9586  -3052   2421  -3254       N  
+ATOM   3478  CA  ILE A 467     -58.666   1.048   3.162  1.00 86.46           C  
+ANISOU 3478  CA  ILE A 467    12578  11464   8810  -2715   2486  -2962       C  
+ATOM   3479  C   ILE A 467     -57.173   0.884   2.869  1.00 88.40           C  
+ANISOU 3479  C   ILE A 467    13000  11598   8990  -2308   2667  -2992       C  
+ATOM   3480  O   ILE A 467     -56.612   1.589   2.024  1.00 86.30           O  
+ANISOU 3480  O   ILE A 467    12615  11656   8520  -2115   2709  -2956       O  
+ATOM   3481  CB  ILE A 467     -58.845   1.663   4.562  1.00 84.14           C  
+ANISOU 3481  CB  ILE A 467    12058  11121   8791  -2718   2526  -2653       C  
+ATOM   3482  CG1 ILE A 467     -60.296   2.104   4.762  1.00 85.53           C  
+ANISOU 3482  CG1 ILE A 467    11925  11549   9024  -3058   2374  -2626       C  
+ATOM   3483  CG2 ILE A 467     -57.916   2.852   4.746  1.00 82.93           C  
+ANISOU 3483  CG2 ILE A 467    11683  11162   8665  -2361   2588  -2378       C  
+ATOM   3484  CD1 ILE A 467     -60.622   2.512   6.182  1.00 83.64           C  
+ANISOU 3484  CD1 ILE A 467    11506  11246   9026  -3110   2451  -2396       C  
+ATOM   3485  N   ILE A 468     -56.545  -0.052   3.575  1.00 89.80           N  
+ANISOU 3485  N   ILE A 468    13460  11322   9339  -2182   2771  -3058       N  
+ATOM   3486  CA  ILE A 468     -55.111  -0.298   3.460  1.00 82.97           C  
+ANISOU 3486  CA  ILE A 468    12711  10331   8484  -1753   2933  -3118       C  
+ATOM   3487  C   ILE A 468     -54.703  -0.625   2.024  1.00 94.67           C  
+ANISOU 3487  C   ILE A 468    14323  11990   9656  -1634   3001  -3434       C  
+ATOM   3488  O   ILE A 468     -53.723  -0.079   1.507  1.00 96.50           O  
+ANISOU 3488  O   ILE A 468    14399  12489   9778  -1343   3157  -3406       O  
+ATOM   3489  CB  ILE A 468     -54.670  -1.465   4.377  1.00 78.22           C  
+ANISOU 3489  CB  ILE A 468    12476   9141   8102  -1638   2956  -3197       C  
+ATOM   3490  CG1 ILE A 468     -54.777  -1.074   5.853  1.00 78.54           C  
+ANISOU 3490  CG1 ILE A 468    12418   9027   8396  -1673   2928  -2859       C  
+ATOM   3491  CG2 ILE A 468     -53.261  -1.928   4.031  1.00 85.84           C  
+ANISOU 3491  CG2 ILE A 468    13567   9980   9069  -1160   3088  -3381       C  
+ATOM   3492  CD1 ILE A 468     -53.992   0.149   6.215  1.00 76.43           C  
+ANISOU 3492  CD1 ILE A 468    11771   9058   8210  -1393   2983  -2584       C  
+ATOM   3493  N   GLU A 469     -55.470  -1.494   1.371  1.00 99.61           N  
+ANISOU 3493  N   GLU A 469    15233  12489  10125  -1889   2894  -3742       N  
+ATOM   3494  CA  GLU A 469     -55.142  -1.901   0.008  1.00 99.34           C  
+ANISOU 3494  CA  GLU A 469    15393  12602   9751  -1785   2949  -4091       C  
+ATOM   3495  C   GLU A 469     -55.408  -0.782  -1.000  1.00 97.26           C  
+ANISOU 3495  C   GLU A 469    14869  12928   9158  -1858   2917  -3987       C  
+ATOM   3496  O   GLU A 469     -54.739  -0.699  -2.031  1.00103.13           O  
+ANISOU 3496  O   GLU A 469    15676  13922   9588  -1667   3061  -4148       O  
+ATOM   3497  CB  GLU A 469     -55.922  -3.162  -0.376  1.00100.88           C  
+ANISOU 3497  CB  GLU A 469    16006  12453   9869  -2065   2798  -4470       C  
+ATOM   3498  CG  GLU A 469     -57.131  -2.920  -1.264  1.00104.20           C  
+ANISOU 3498  CG  GLU A 469    16369  13198  10024  -2461   2578  -4581       C  
+ATOM   3499  CD  GLU A 469     -57.710  -4.202  -1.823  1.00122.97           C  
+ANISOU 3499  CD  GLU A 469    19186  15248  12289  -2716   2432  -5023       C  
+ATOM   3500  OE1 GLU A 469     -57.204  -5.287  -1.468  1.00130.06           O  
+ANISOU 3500  OE1 GLU A 469    20469  15616  13332  -2588   2505  -5226       O  
+ATOM   3501  OE2 GLU A 469     -58.671  -4.126  -2.617  1.00129.93           O  
+ANISOU 3501  OE2 GLU A 469    20044  16381  12941  -3039   2213  -5176       O  
+ATOM   3502  N   PHE A 470     -56.373   0.082  -0.697  1.00 91.85           N  
+ANISOU 3502  N   PHE A 470    13905  12463   8528  -2118   2732  -3719       N  
+ATOM   3503  CA  PHE A 470     -56.644   1.235  -1.549  1.00 88.90           C  
+ANISOU 3503  CA  PHE A 470    13314  12599   7865  -2158   2644  -3560       C  
+ATOM   3504  C   PHE A 470     -55.460   2.201  -1.486  1.00 91.70           C  
+ANISOU 3504  C   PHE A 470    13463  13163   8214  -1849   2869  -3284       C  
+ATOM   3505  O   PHE A 470     -54.949   2.667  -2.517  1.00 97.02           O  
+ANISOU 3505  O   PHE A 470    14158  14166   8539  -1755   2976  -3292       O  
+ATOM   3506  CB  PHE A 470     -57.942   1.928  -1.123  1.00 86.71           C  
+ANISOU 3506  CB  PHE A 470    12762  12471   7715  -2443   2367  -3356       C  
+ATOM   3507  CG  PHE A 470     -58.315   3.108  -1.978  1.00 83.04           C  
+ANISOU 3507  CG  PHE A 470    12118  12471   6962  -2459   2196  -3184       C  
+ATOM   3508  CD1 PHE A 470     -57.974   4.396  -1.601  1.00 77.34           C  
+ANISOU 3508  CD1 PHE A 470    11128  11932   6325  -2306   2221  -2797       C  
+ATOM   3509  CD2 PHE A 470     -59.024   2.926  -3.156  1.00 89.64           C  
+ANISOU 3509  CD2 PHE A 470    13096  13531   7433  -2630   1972  -3409       C  
+ATOM   3510  CE1 PHE A 470     -58.324   5.480  -2.388  1.00 80.03           C  
+ANISOU 3510  CE1 PHE A 470    11377  12638   6395  -2315   2029  -2615       C  
+ATOM   3511  CE2 PHE A 470     -59.375   4.005  -3.946  1.00 89.91           C  
+ANISOU 3511  CE2 PHE A 470    13024  13964   7174  -2625   1767  -3228       C  
+ATOM   3512  CZ  PHE A 470     -59.025   5.283  -3.561  1.00 85.79           C  
+ANISOU 3512  CZ  PHE A 470    12266  13587   6744  -2463   1797  -2818       C  
+ATOM   3513  N   VAL A 471     -55.011   2.469  -0.263  1.00 79.48           N  
+ANISOU 3513  N   VAL A 471    11737  11421   7041  -1720   2948  -3045       N  
+ATOM   3514  CA  VAL A 471     -53.907   3.391  -0.035  1.00 77.31           C  
+ANISOU 3514  CA  VAL A 471    11228  11312   6836  -1472   3130  -2778       C  
+ATOM   3515  C   VAL A 471     -52.618   2.828  -0.637  1.00 93.56           C  
+ANISOU 3515  C   VAL A 471    13396  13389   8764  -1189   3421  -3010       C  
+ATOM   3516  O   VAL A 471     -51.781   3.575  -1.147  1.00105.40           O  
+ANISOU 3516  O   VAL A 471    14729  15204  10114  -1069   3609  -2887       O  
+ATOM   3517  CB  VAL A 471     -53.716   3.659   1.478  1.00 73.61           C  
+ANISOU 3517  CB  VAL A 471    10581  10591   6795  -1392   3113  -2527       C  
+ATOM   3518  CG1 VAL A 471     -52.394   4.359   1.752  1.00 72.46           C  
+ANISOU 3518  CG1 VAL A 471    10215  10551   6764  -1122   3301  -2332       C  
+ATOM   3519  CG2 VAL A 471     -54.878   4.477   2.023  1.00 75.55           C  
+ANISOU 3519  CG2 VAL A 471    10641  10922   7143  -1623   2881  -2286       C  
+ATOM   3520  N   GLU A 472     -52.476   1.507  -0.601  1.00 84.99           N  
+ANISOU 3520  N   GLU A 472    12594  11966   7731  -1092   3463  -3361       N  
+ATOM   3521  CA  GLU A 472     -51.325   0.851  -1.216  1.00 84.38           C  
+ANISOU 3521  CA  GLU A 472    12628  11899   7534   -774   3730  -3667       C  
+ATOM   3522  C   GLU A 472     -51.375   0.949  -2.738  1.00 95.38           C  
+ANISOU 3522  C   GLU A 472    14125  13668   8447   -824   3788  -3829       C  
+ATOM   3523  O   GLU A 472     -50.354   1.176  -3.388  1.00 88.29           O  
+ANISOU 3523  O   GLU A 472    13090  13023   7435   -576   3982  -3807       O  
+ATOM   3524  CB  GLU A 472     -51.237  -0.610  -0.782  1.00 92.13           C  
+ANISOU 3524  CB  GLU A 472    13950  12348   8706   -628   3696  -4004       C  
+ATOM   3525  CG  GLU A 472     -50.434  -0.805   0.491  1.00 92.60           C  
+ANISOU 3525  CG  GLU A 472    13907  12078   9198   -341   3723  -3872       C  
+ATOM   3526  CD  GLU A 472     -50.551  -2.206   1.048  1.00109.92           C  
+ANISOU 3526  CD  GLU A 472    16521  13659  11585   -251   3607  -4126       C  
+ATOM   3527  OE1 GLU A 472     -51.289  -3.022   0.458  1.00125.53           O  
+ANISOU 3527  OE1 GLU A 472    18859  15455  13383   -451   3513  -4413       O  
+ATOM   3528  OE2 GLU A 472     -49.907  -2.489   2.080  1.00106.85           O  
+ANISOU 3528  OE2 GLU A 472    16131  12947  11520     11   3583  -4035       O  
+ATOM   3529  N   ILE A 473     -52.569   0.772  -3.297  1.00103.62           N  
+ANISOU 3529  N   ILE A 473    15390  14745   9236  -1140   3569  -3953       N  
+ATOM   3530  CA  ILE A 473     -52.781   0.921  -4.733  1.00105.89           C  
+ANISOU 3530  CA  ILE A 473    15802  15372   9060  -1201   3516  -4041       C  
+ATOM   3531  C   ILE A 473     -52.433   2.339  -5.182  1.00104.16           C  
+ANISOU 3531  C   ILE A 473    15321  15603   8653  -1212   3587  -3641       C  
+ATOM   3532  O   ILE A 473     -51.979   2.547  -6.307  1.00 93.29           O  
+ANISOU 3532  O   ILE A 473    14008  14511   6928  -1124   3687  -3644       O  
+ATOM   3533  CB  ILE A 473     -54.235   0.602  -5.134  1.00 97.60           C  
+ANISOU 3533  CB  ILE A 473    14986  14297   7801  -1575   3192  -4223       C  
+ATOM   3534  N   LEU A 474     -52.651   3.307  -4.294  1.00 98.61           N  
+ANISOU 3534  N   LEU A 474    14358  14936   8172  -1326   3533  -3292       N  
+ATOM   3535  CA  LEU A 474     -52.313   4.706  -4.574  1.00100.59           C  
+ANISOU 3535  CA  LEU A 474    14389  15525   8305  -1353   3570  -2875       C  
+ATOM   3536  C   LEU A 474     -50.824   4.956  -4.842  1.00115.79           C  
+ANISOU 3536  C   LEU A 474    16138  17580  10276  -1085   3881  -2762       C  
+ATOM   3537  O   LEU A 474     -50.471   5.766  -5.701  1.00121.69           O  
+ANISOU 3537  O   LEU A 474    16865  18632  10740  -1123   3956  -2545       O  
+ATOM   3538  CB  LEU A 474     -52.774   5.595  -3.421  1.00 97.90           C  
+ANISOU 3538  CB  LEU A 474    13806  15114   8276  -1473   3429  -2547       C  
+ATOM   3539  CG  LEU A 474     -54.257   5.953  -3.468  1.00 92.22           C  
+ANISOU 3539  CG  LEU A 474    13118  14418   7505  -1713   3020  -2454       C  
+ATOM   3540  CD1 LEU A 474     -54.690   6.637  -2.183  1.00 77.41           C  
+ANISOU 3540  CD1 LEU A 474    10965  12374   6072  -1731   2847  -2153       C  
+ATOM   3541  CD2 LEU A 474     -54.535   6.829  -4.678  1.00 96.02           C  
+ANISOU 3541  CD2 LEU A 474    13708  15280   7494  -1828   2907  -2303       C  
+ATOM   3542  N   SER A 475     -49.957   4.256  -4.118  1.00115.49           N  
+ANISOU 3542  N   SER A 475    15983  17317  10582   -824   4055  -2915       N  
+ATOM   3543  CA  SER A 475     -48.517   4.421  -4.282  1.00107.35           C  
+ANISOU 3543  CA  SER A 475    14712  16438   9636   -560   4343  -2858       C  
+ATOM   3544  C   SER A 475     -48.017   3.610  -5.474  1.00106.55           C  
+ANISOU 3544  C   SER A 475    14799  16474   9212   -375   4523  -3184       C  
+ATOM   3545  O   SER A 475     -47.314   2.615  -5.310  1.00104.05           O  
+ANISOU 3545  O   SER A 475    14485  15998   9050    -66   4661  -3499       O  
+ATOM   3546  CB  SER A 475     -47.778   3.999  -3.009  1.00109.15           C  
+ANISOU 3546  CB  SER A 475    14725  16394  10355   -315   4418  -2915       C  
+ATOM   3547  OG  SER A 475     -47.325   2.657  -3.099  1.00119.81           O  
+ANISOU 3547  OG  SER A 475    16230  17536  11757    -18   4514  -3342       O  
+ATOM   3548  N   ASN A 476     -48.422   4.034  -6.670  1.00108.15           N  
+ANISOU 3548  N   ASN A 476    15188  16956   8949   -546   4500  -3120       N  
+ATOM   3549  CA  ASN A 476     -48.091   3.353  -7.921  1.00115.53           C  
+ANISOU 3549  CA  ASN A 476    16357  18053   9487   -403   4656  -3420       C  
+ATOM   3550  C   ASN A 476     -46.608   3.043  -8.112  1.00127.26           C  
+ANISOU 3550  C   ASN A 476    17626  19668  11060    -58   5031  -3536       C  
+ATOM   3551  O   ASN A 476     -46.260   2.130  -8.861  1.00133.26           O  
+ANISOU 3551  O   ASN A 476    18574  20457  11602    169   5171  -3902       O  
+ATOM   3552  CB  ASN A 476     -48.580   4.192  -9.102  1.00120.86           C  
+ANISOU 3552  CB  ASN A 476    17221  19059   9641   -650   4596  -3210       C  
+ATOM   3553  CG  ASN A 476     -50.052   4.529  -9.004  1.00123.56           C  
+ANISOU 3553  CG  ASN A 476    17751  19329   9866   -964   4197  -3116       C  
+ATOM   3554  OD1 ASN A 476     -50.899   3.642  -8.898  1.00121.18           O  
+ANISOU 3554  OD1 ASN A 476    17662  18814   9568  -1016   3981  -3430       O  
+ATOM   3555  ND2 ASN A 476     -50.364   5.820  -9.011  1.00122.54           N  
+ANISOU 3555  ND2 ASN A 476    17542  19368   9648  -1181   4084  -2689       N  
+ATOM   3556  OXT ASN A 476     -45.727   3.680  -7.532  1.00129.95           O  
+ANISOU 3556  OXT ASN A 476    17594  20091  11688      7   5194  -3291       O  
+TER    3557      ASN A 476                                                      
+ATOM   3558  N   HIS B   2     -15.661  24.859  34.089  1.00 84.11           N  
+ANISOU 3558  N   HIS B   2    11814  13512   6633    145    432  -2624       N  
+ATOM   3559  CA  HIS B   2     -15.097  24.199  35.261  1.00 96.17           C  
+ANISOU 3559  CA  HIS B   2    13722  15254   7565    -67    381  -2442       C  
+ATOM   3560  C   HIS B   2     -13.703  23.654  34.966  1.00 99.14           C  
+ANISOU 3560  C   HIS B   2    14149  15465   8054   -139    -54  -1921       C  
+ATOM   3561  O   HIS B   2     -12.740  23.974  35.664  1.00 97.45           O  
+ANISOU 3561  O   HIS B   2    14179  15214   7635   -215   -442  -1877       O  
+ATOM   3562  CB  HIS B   2     -16.015  23.073  35.737  1.00 94.54           C  
+ANISOU 3562  CB  HIS B   2    13593  15361   6966   -227    875  -2361       C  
+HETATM 3563  N   MSE B   3     -13.601  22.831  33.927  1.00 90.56           N  
+ANISOU 3563  N   MSE B   3    12817  14274   7316   -114      6  -1553       N  
+HETATM 3564  CA  MSE B   3     -12.314  22.290  33.500  1.00 77.43           C  
+ANISOU 3564  CA  MSE B   3    11112  12442   5865   -147   -353  -1102       C  
+HETATM 3565  C   MSE B   3     -11.472  23.380  32.841  1.00 74.83           C  
+ANISOU 3565  C   MSE B   3    10610  11847   5975    -49   -724  -1167       C  
+HETATM 3566  O   MSE B   3     -11.926  24.515  32.690  1.00 84.50           O  
+ANISOU 3566  O   MSE B   3    11778  12990   7338     46   -728  -1534       O  
+HETATM 3567  CB  MSE B   3     -12.517  21.116  32.540  1.00 65.63           C  
+ANISOU 3567  CB  MSE B   3     9406  10908   4621   -139   -134   -757       C  
+HETATM 3568  CG  MSE B   3     -12.828  19.794  33.229  1.00 69.56           C  
+ANISOU 3568  CG  MSE B   3    10120  11594   4715   -295     61   -507       C  
+HETATM 3569 SE   MSE B   3     -13.601  18.469  32.020  1.00 96.90          SE  
+ANISOU 3569 SE   MSE B   3    13319  15012   8484   -279    449   -237      SE  
+HETATM 3570  CE  MSE B   3     -12.797  16.861  32.773  1.00 82.08           C  
+ANISOU 3570  CE  MSE B   3    11737  13141   6309   -454    258    297       C  
+ATOM   3571  N   ASN B   4     -10.247  23.038  32.453  1.00 71.81           N  
+ANISOU 3571  N   ASN B   4    10131  11319   5836    -80  -1039   -817       N  
+ATOM   3572  CA  ASN B   4      -9.364  23.999  31.799  1.00 74.01           C  
+ANISOU 3572  CA  ASN B   4    10226  11358   6537    -45  -1370   -830       C  
+ATOM   3573  C   ASN B   4      -9.913  24.413  30.429  1.00 71.78           C  
+ANISOU 3573  C   ASN B   4     9668  10924   6681     48  -1174   -896       C  
+ATOM   3574  O   ASN B   4     -10.577  23.620  29.760  1.00 68.93           O  
+ANISOU 3574  O   ASN B   4     9189  10612   6390     82   -850   -780       O  
+ATOM   3575  CB  ASN B   4      -7.945  23.424  31.678  1.00 90.76           C  
+ANISOU 3575  CB  ASN B   4    12241  13385   8858   -109  -1695   -446       C  
+ATOM   3576  CG  ASN B   4      -7.873  22.235  30.752  1.00 95.75           C  
+ANISOU 3576  CG  ASN B   4    12650  13996   9733    -78  -1468   -122       C  
+ATOM   3577  OD1 ASN B   4      -8.858  21.529  30.563  1.00116.26           O  
+ANISOU 3577  OD1 ASN B   4    15277  16699  12197    -51  -1103   -114       O  
+ATOM   3578  ND2 ASN B   4      -6.703  22.005  30.168  1.00 85.87           N  
+ANISOU 3578  ND2 ASN B   4    11160  12607   8861    -88  -1676    126       N  
+ATOM   3579  N   PRO B   5      -9.643  25.666  30.017  1.00 79.57           N  
+ANISOU 3579  N   PRO B   5    10582  11707   7943     68  -1408  -1072       N  
+ATOM   3580  CA  PRO B   5     -10.206  26.290  28.809  1.00 77.10           C  
+ANISOU 3580  CA  PRO B   5    10087  11211   7997    133  -1313  -1161       C  
+ATOM   3581  C   PRO B   5     -10.116  25.467  27.519  1.00 75.20           C  
+ANISOU 3581  C   PRO B   5     9627  10925   8019    111  -1116   -841       C  
+ATOM   3582  O   PRO B   5     -11.039  25.537  26.705  1.00 69.67           O  
+ANISOU 3582  O   PRO B   5     8845  10167   7459    171   -917   -916       O  
+ATOM   3583  CB  PRO B   5      -9.382  27.582  28.668  1.00 84.50           C  
+ANISOU 3583  CB  PRO B   5    11019  11905   9184     76  -1725  -1243       C  
+ATOM   3584  CG  PRO B   5      -8.231  27.443  29.628  1.00 89.44           C  
+ANISOU 3584  CG  PRO B   5    11748  12593   9641    -24  -2024  -1130       C  
+ATOM   3585  CD  PRO B   5      -8.756  26.598  30.731  1.00 80.06           C  
+ANISOU 3585  CD  PRO B   5    10771  11672   7974      5  -1837  -1186       C  
+ATOM   3586  N   ILE B   6      -9.040  24.710  27.331  1.00 75.58           N  
+ANISOU 3586  N   ILE B   6     9580  10988   8150     32  -1183   -515       N  
+ATOM   3587  CA  ILE B   6      -8.888  23.905  26.121  1.00 69.94           C  
+ANISOU 3587  CA  ILE B   6     8670  10233   7671     11   -973   -254       C  
+ATOM   3588  C   ILE B   6      -9.951  22.810  26.043  1.00 66.31           C  
+ANISOU 3588  C   ILE B   6     8243   9912   7040     78   -610   -226       C  
+ATOM   3589  O   ILE B   6     -10.631  22.655  25.019  1.00 65.06           O  
+ANISOU 3589  O   ILE B   6     7997   9695   7026     97   -403   -219       O  
+ATOM   3590  CB  ILE B   6      -7.488  23.266  26.043  1.00 74.48           C  
+ANISOU 3590  CB  ILE B   6     9096  10798   8406    -58  -1105     37       C  
+ATOM   3591  CG1 ILE B   6      -6.410  24.352  26.011  1.00 76.89           C  
+ANISOU 3591  CG1 ILE B   6     9314  10963   8940   -163  -1454     24       C  
+ATOM   3592  CG2 ILE B   6      -7.376  22.375  24.817  1.00 70.59           C  
+ANISOU 3592  CG2 ILE B   6     8414  10275   8133    -65   -834    246       C  
+ATOM   3593  CD1 ILE B   6      -4.998  23.814  25.933  1.00 77.70           C  
+ANISOU 3593  CD1 ILE B   6     9189  11053   9280   -229  -1596    274       C  
+ATOM   3594  N   VAL B   7     -10.106  22.069  27.136  1.00 65.11           N  
+ANISOU 3594  N   VAL B   7     8239   9933   6566     86   -559   -201       N  
+ATOM   3595  CA  VAL B   7     -11.116  21.021  27.211  1.00 61.93           C  
+ANISOU 3595  CA  VAL B   7     7886   9668   5976    106   -223   -164       C  
+ATOM   3596  C   VAL B   7     -12.511  21.606  27.051  1.00 61.83           C  
+ANISOU 3596  C   VAL B   7     7869   9689   5934    164    -14   -471       C  
+ATOM   3597  O   VAL B   7     -13.353  21.015  26.393  1.00 58.80           O  
+ANISOU 3597  O   VAL B   7     7398   9320   5624    181    246   -442       O  
+ATOM   3598  CB  VAL B   7     -11.029  20.230  28.538  1.00 62.09           C  
+ANISOU 3598  CB  VAL B   7     8128   9865   5597     50   -238    -73       C  
+ATOM   3599  CG1 VAL B   7     -12.264  19.359  28.744  1.00 58.19           C  
+ANISOU 3599  CG1 VAL B   7     7711   9529   4868     24    132    -88       C  
+ATOM   3600  CG2 VAL B   7      -9.757  19.397  28.576  1.00 63.78           C  
+ANISOU 3600  CG2 VAL B   7     8303  10008   5922     23   -455    267       C  
+ATOM   3601  N   GLU B   8     -12.750  22.769  27.646  1.00 61.83           N  
+ANISOU 3601  N   GLU B   8     7947   9683   5863    204   -149   -785       N  
+ATOM   3602  CA  GLU B   8     -14.050  23.421  27.531  1.00 60.97           C  
+ANISOU 3602  CA  GLU B   8     7785   9576   5803    298     15  -1130       C  
+ATOM   3603  C   GLU B   8     -14.356  23.807  26.084  1.00 65.73           C  
+ANISOU 3603  C   GLU B   8     8204   9954   6815    343    -16  -1099       C  
+ATOM   3604  O   GLU B   8     -15.476  23.610  25.601  1.00 66.72           O  
+ANISOU 3604  O   GLU B   8     8222  10088   7040    398    192  -1203       O  
+ATOM   3605  CB  GLU B   8     -14.107  24.653  28.432  1.00 64.06           C  
+ANISOU 3605  CB  GLU B   8     8300   9957   6085    353   -167  -1504       C  
+ATOM   3606  CG  GLU B   8     -13.937  24.334  29.908  1.00 65.10           C  
+ANISOU 3606  CG  GLU B   8     8677  10329   5730    281   -128  -1578       C  
+ATOM   3607  CD  GLU B   8     -15.132  23.608  30.492  1.00 64.48           C  
+ANISOU 3607  CD  GLU B   8     8634  10517   5348    260    305  -1711       C  
+ATOM   3608  OE1 GLU B   8     -16.211  23.618  29.861  1.00 71.39           O  
+ANISOU 3608  OE1 GLU B   8     9303  11380   6440    343    550  -1861       O  
+ATOM   3609  OE2 GLU B   8     -14.994  23.015  31.583  1.00 71.98           O  
+ANISOU 3609  OE2 GLU B   8     9821  11687   5842    138    386  -1654       O  
+ATOM   3610  N   LEU B   9     -13.355  24.354  25.399  1.00 63.67           N  
+ANISOU 3610  N   LEU B   9     7915   9494   6783    292   -286   -948       N  
+ATOM   3611  CA  LEU B   9     -13.495  24.716  23.992  1.00 64.13           C  
+ANISOU 3611  CA  LEU B   9     7867   9335   7165    274   -343   -864       C  
+ATOM   3612  C   LEU B   9     -13.830  23.479  23.161  1.00 61.70           C  
+ANISOU 3612  C   LEU B   9     7480   9086   6876    238    -69   -635       C  
+ATOM   3613  O   LEU B   9     -14.745  23.502  22.323  1.00 59.38           O  
+ANISOU 3613  O   LEU B   9     7127   8706   6728    265      8   -685       O  
+ATOM   3614  CB  LEU B   9     -12.218  25.380  23.474  1.00 66.87           C  
+ANISOU 3614  CB  LEU B   9     8211   9502   7695    157   -628   -697       C  
+ATOM   3615  CG  LEU B   9     -12.138  26.900  23.639  1.00 69.77           C  
+ANISOU 3615  CG  LEU B   9     8645   9659   8206    168   -966   -922       C  
+ATOM   3616  CD1 LEU B   9     -10.788  27.428  23.175  1.00 71.05           C  
+ANISOU 3616  CD1 LEU B   9     8788   9670   8537     -6  -1220   -711       C  
+ATOM   3617  CD2 LEU B   9     -13.270  27.583  22.888  1.00 69.91           C  
+ANISOU 3617  CD2 LEU B   9     8648   9482   8435    249  -1013  -1098       C  
+ATOM   3618  N   PHE B  10     -13.090  22.399  23.406  1.00 57.60           N  
+ANISOU 3618  N   PHE B  10     6967   8688   6229    182     39   -392       N  
+ATOM   3619  CA  PHE B  10     -13.370  21.128  22.746  1.00 58.12           C  
+ANISOU 3619  CA  PHE B  10     6983   8798   6302    156    295   -195       C  
+ATOM   3620  C   PHE B  10     -14.794  20.660  23.017  1.00 68.60           C  
+ANISOU 3620  C   PHE B  10     8307  10240   7519    207    532   -341       C  
+ATOM   3621  O   PHE B  10     -15.478  20.179  22.117  1.00 73.76           O  
+ANISOU 3621  O   PHE B  10     8897  10840   8288    194    670   -296       O  
+ATOM   3622  CB  PHE B  10     -12.392  20.043  23.195  1.00 52.30           C  
+ANISOU 3622  CB  PHE B  10     6259   8148   5467    122    332     51       C  
+ATOM   3623  CG  PHE B  10     -12.894  18.647  22.947  1.00 60.57           C  
+ANISOU 3623  CG  PHE B  10     7305   9252   6458    117    593    197       C  
+ATOM   3624  CD1 PHE B  10     -12.969  18.144  21.660  1.00 51.21           C  
+ANISOU 3624  CD1 PHE B  10     6047   7956   5455     89    721    301       C  
+ATOM   3625  CD2 PHE B  10     -13.304  17.844  23.999  1.00 57.57           C  
+ANISOU 3625  CD2 PHE B  10     7028   9025   5820    111    704    229       C  
+ATOM   3626  CE1 PHE B  10     -13.437  16.865  21.424  1.00 55.19           C  
+ANISOU 3626  CE1 PHE B  10     6565   8481   5925     79    935    417       C  
+ATOM   3627  CE2 PHE B  10     -13.773  16.563  23.769  1.00 43.63           C  
+ANISOU 3627  CE2 PHE B  10     5277   7278   4024     81    918    379       C  
+ATOM   3628  CZ  PHE B  10     -13.839  16.074  22.480  1.00 44.87           C  
+ANISOU 3628  CZ  PHE B  10     5344   7302   4403     77   1024    463       C  
+ATOM   3629  N   ILE B  11     -15.222  20.789  24.268  1.00 59.62           N  
+ANISOU 3629  N   ILE B  11     7237   9269   6146    241    586   -522       N  
+ATOM   3630  CA  ILE B  11     -16.557  20.384  24.678  1.00 58.11           C  
+ANISOU 3630  CA  ILE B  11     7009   9230   5839    259    859   -690       C  
+ATOM   3631  C   ILE B  11     -17.593  21.163  23.886  1.00 59.18           C  
+ANISOU 3631  C   ILE B  11     6991   9235   6259    345    838   -927       C  
+ATOM   3632  O   ILE B  11     -18.588  20.598  23.452  1.00 61.71           O  
+ANISOU 3632  O   ILE B  11     7198   9583   6664    338   1029   -946       O  
+ATOM   3633  CB  ILE B  11     -16.782  20.581  26.194  1.00 58.18           C  
+ANISOU 3633  CB  ILE B  11     7142   9460   5506    253    939   -896       C  
+ATOM   3634  CG1 ILE B  11     -16.010  19.523  26.984  1.00 52.84           C  
+ANISOU 3634  CG1 ILE B  11     6647   8913   4516    138    963   -610       C  
+ATOM   3635  CG2 ILE B  11     -18.256  20.469  26.540  1.00 61.98           C  
+ANISOU 3635  CG2 ILE B  11     7518  10102   5928    268   1254  -1162       C  
+ATOM   3636  CD1 ILE B  11     -16.068  19.714  28.484  1.00 54.42           C  
+ANISOU 3636  CD1 ILE B  11     7054   9329   4295     81    996   -768       C  
+ATOM   3637  N   LYS B  12     -17.345  22.450  23.666  1.00 55.31           N  
+ANISOU 3637  N   LYS B  12     6498   8571   5948    416    563  -1090       N  
+ATOM   3638  CA  LYS B  12     -18.308  23.275  22.944  1.00 56.56           C  
+ANISOU 3638  CA  LYS B  12     6526   8550   6415    513    455  -1312       C  
+ATOM   3639  C   LYS B  12     -18.375  22.908  21.463  1.00 61.61           C  
+ANISOU 3639  C   LYS B  12     7133   9010   7267    444    392  -1072       C  
+ATOM   3640  O   LYS B  12     -19.467  22.712  20.906  1.00 81.44           O  
+ANISOU 3640  O   LYS B  12     9520  11477   9945    478    454  -1152       O  
+ATOM   3641  CB  LYS B  12     -17.949  24.755  23.087  1.00 59.96           C  
+ANISOU 3641  CB  LYS B  12     7005   8785   6993    593    119  -1521       C  
+ATOM   3642  CG  LYS B  12     -18.789  25.511  24.096  1.00 61.19           C  
+ANISOU 3642  CG  LYS B  12     7097   9007   7145    749    160  -1976       C  
+ATOM   3643  CD  LYS B  12     -18.374  26.970  24.168  1.00 64.93           C  
+ANISOU 3643  CD  LYS B  12     7645   9226   7801    829   -222  -2180       C  
+ATOM   3644  CE  LYS B  12     -19.327  27.766  25.042  1.00 82.13           C  
+ANISOU 3644  CE  LYS B  12     9733  11428  10047   1023   -176  -2705       C  
+ATOM   3645  NZ  LYS B  12     -19.509  27.138  26.380  1.00 93.75           N  
+ANISOU 3645  NZ  LYS B  12    11250  13275  11096    998    198  -2867       N  
+ATOM   3646  N   ASP B  13     -17.208  22.771  20.838  1.00 55.66           N  
+ANISOU 3646  N   ASP B  13     6486   8165   6499    332    283   -789       N  
+ATOM   3647  CA  ASP B  13     -17.150  22.460  19.412  1.00 56.77           C  
+ANISOU 3647  CA  ASP B  13     6649   8147   6773    232    244   -574       C  
+ATOM   3648  C   ASP B  13     -17.765  21.088  19.138  1.00 67.77           C  
+ANISOU 3648  C   ASP B  13     7996   9657   8096    199    526   -467       C  
+ATOM   3649  O   ASP B  13     -18.600  20.927  18.240  1.00 71.57           O  
+ANISOU 3649  O   ASP B  13     8445  10035   8715    179    509   -470       O  
+ATOM   3650  CB  ASP B  13     -15.703  22.507  18.908  1.00 57.43           C  
+ANISOU 3650  CB  ASP B  13     6827   8164   6831    100    158   -325       C  
+ATOM   3651  CG  ASP B  13     -15.582  22.178  17.427  1.00 71.44           C  
+ANISOU 3651  CG  ASP B  13     8664   9804   8677    -39    171   -126       C  
+ATOM   3652  OD1 ASP B  13     -16.597  22.262  16.704  1.00 85.59           O  
+ANISOU 3652  OD1 ASP B  13    10469  11483  10568    -36    111   -180       O  
+ATOM   3653  OD2 ASP B  13     -14.466  21.830  16.985  1.00 56.26           O  
+ANISOU 3653  OD2 ASP B  13     6774   7890   6713   -157    240     71       O  
+ATOM   3654  N   PHE B  14     -17.360  20.105  19.934  1.00 65.73           N  
+ANISOU 3654  N   PHE B  14     7751   9591   7630    182    744   -364       N  
+ATOM   3655  CA  PHE B  14     -17.813  18.735  19.746  1.00 56.64           C  
+ANISOU 3655  CA  PHE B  14     6585   8524   6413    129    993   -233       C  
+ATOM   3656  C   PHE B  14     -19.281  18.577  20.136  1.00 54.04           C  
+ANISOU 3656  C   PHE B  14     6129   8292   6113    167   1138   -433       C  
+ATOM   3657  O   PHE B  14     -19.987  17.746  19.568  1.00 46.39           O  
+ANISOU 3657  O   PHE B  14     5114   7308   5206    109   1262   -369       O  
+ATOM   3658  CB  PHE B  14     -16.942  17.770  20.551  1.00 57.32           C  
+ANISOU 3658  CB  PHE B  14     6742   8743   6294     98   1123    -49       C  
+ATOM   3659  CG  PHE B  14     -16.981  16.359  20.048  1.00 49.68           C  
+ANISOU 3659  CG  PHE B  14     5801   7759   5317     32   1303    152       C  
+ATOM   3660  CD1 PHE B  14     -16.458  16.042  18.805  1.00 37.86           C  
+ANISOU 3660  CD1 PHE B  14     4331   6108   3947    -13   1286    281       C  
+ATOM   3661  CD2 PHE B  14     -17.542  15.350  20.810  1.00 47.87           C  
+ANISOU 3661  CD2 PHE B  14     5590   7659   4940     -7   1495    203       C  
+ATOM   3662  CE1 PHE B  14     -16.491  14.745  18.333  1.00 43.18           C  
+ANISOU 3662  CE1 PHE B  14     5042   6739   4626    -60   1445    423       C  
+ATOM   3663  CE2 PHE B  14     -17.578  14.050  20.344  1.00 59.02           C  
+ANISOU 3663  CE2 PHE B  14     7043   9009   6372    -71   1625    385       C  
+ATOM   3664  CZ  PHE B  14     -17.051  13.748  19.104  1.00 52.85           C  
+ANISOU 3664  CZ  PHE B  14     6281   8056   5745    -79   1593    478       C  
+ATOM   3665  N   THR B  15     -19.736  19.366  21.108  1.00 57.39           N  
+ANISOU 3665  N   THR B  15     6484   8818   6504    255   1134   -698       N  
+ATOM   3666  CA  THR B  15     -21.156  19.398  21.450  1.00 52.22           C  
+ANISOU 3666  CA  THR B  15     5640   8261   5940    301   1291   -956       C  
+ATOM   3667  C   THR B  15     -21.951  19.872  20.249  1.00 49.37           C  
+ANISOU 3667  C   THR B  15     5150   7678   5931    347   1096  -1038       C  
+ATOM   3668  O   THR B  15     -22.976  19.281  19.903  1.00 55.48           O  
+ANISOU 3668  O   THR B  15     5774   8472   6836    314   1214  -1071       O  
+ATOM   3669  CB  THR B  15     -21.462  20.318  22.647  1.00 64.22           C  
+ANISOU 3669  CB  THR B  15     7100   9915   7384    407   1327  -1299       C  
+ATOM   3670  OG1 THR B  15     -20.919  19.745  23.843  1.00 71.44           O  
+ANISOU 3670  OG1 THR B  15     8166  11065   7912    324   1521  -1221       O  
+ATOM   3671  CG2 THR B  15     -22.964  20.494  22.817  1.00 50.71           C  
+ANISOU 3671  CG2 THR B  15     5115   8281   5872    476   1493  -1626       C  
+ATOM   3672  N   LYS B  16     -21.477  20.943  19.617  1.00 53.83           N  
+ANISOU 3672  N   LYS B  16     5787   8015   6652    401    766  -1054       N  
+ATOM   3673  CA  LYS B  16     -22.132  21.431  18.409  1.00 57.27           C  
+ANISOU 3673  CA  LYS B  16     6171   8195   7396    417    496  -1078       C  
+ATOM   3674  C   LYS B  16     -22.161  20.345  17.339  1.00 55.13           C  
+ANISOU 3674  C   LYS B  16     5983   7873   7090    267    557   -808       C  
+ATOM   3675  O   LYS B  16     -23.188  20.121  16.698  1.00 57.11           O  
+ANISOU 3675  O   LYS B  16     6121   8038   7539    257    493   -857       O  
+ATOM   3676  CB  LYS B  16     -21.444  22.679  17.859  1.00 60.75           C  
+ANISOU 3676  CB  LYS B  16     6756   8377   7951    435    115  -1057       C  
+ATOM   3677  CG  LYS B  16     -22.092  23.172  16.574  1.00 65.89           C  
+ANISOU 3677  CG  LYS B  16     7422   8732   8881    416   -224  -1030       C  
+ATOM   3678  CD  LYS B  16     -21.438  24.421  16.022  1.00 78.50           C  
+ANISOU 3678  CD  LYS B  16     9203  10047  10575    386   -623   -973       C  
+ATOM   3679  CE  LYS B  16     -22.020  24.758  14.659  1.00 72.54           C  
+ANISOU 3679  CE  LYS B  16     8546   8990  10028    310   -985   -868       C  
+ATOM   3680  NZ  LYS B  16     -21.324  25.897  14.007  1.00 72.15           N  
+ANISOU 3680  NZ  LYS B  16     8741   8648  10024    206  -1380   -736       N  
+ATOM   3681  N   GLU B  17     -21.029  19.671  17.154  1.00 51.95           N  
+ANISOU 3681  N   GLU B  17     5767   7514   6460    155    667   -546       N  
+ATOM   3682  CA  GLU B  17     -20.925  18.631  16.134  1.00 51.38           C  
+ANISOU 3682  CA  GLU B  17     5804   7381   6337     19    743   -324       C  
+ATOM   3683  C   GLU B  17     -21.805  17.417  16.432  1.00 56.78           C  
+ANISOU 3683  C   GLU B  17     6372   8196   7004    -14    998   -328       C  
+ATOM   3684  O   GLU B  17     -22.367  16.816  15.517  1.00 49.17           O  
+ANISOU 3684  O   GLU B  17     5432   7131   6121   -100    971   -263       O  
+ATOM   3685  CB  GLU B  17     -19.470  18.193  15.975  1.00 49.25           C  
+ANISOU 3685  CB  GLU B  17     5703   7132   5876    -60    835    -99       C  
+ATOM   3686  CG  GLU B  17     -18.580  19.269  15.386  1.00 60.89           C  
+ANISOU 3686  CG  GLU B  17     7298   8460   7377   -106    602    -46       C  
+ATOM   3687  CD  GLU B  17     -19.000  19.661  13.983  1.00 66.71           C  
+ANISOU 3687  CD  GLU B  17     8165   8977   8206   -217    382      2       C  
+ATOM   3688  OE1 GLU B  17     -18.893  20.858  13.643  1.00 64.31           O  
+ANISOU 3688  OE1 GLU B  17     7931   8510   7995   -237     92    -25       O  
+ATOM   3689  OE2 GLU B  17     -19.440  18.774  13.221  1.00 61.83           O  
+ANISOU 3689  OE2 GLU B  17     7607   8328   7556   -299    468     74       O  
+ATOM   3690  N   VAL B  18     -21.924  17.059  17.707  1.00 58.84           N  
+ANISOU 3690  N   VAL B  18     6538   8676   7142     23   1232   -397       N  
+ATOM   3691  CA  VAL B  18     -22.777  15.942  18.103  1.00 51.47           C  
+ANISOU 3691  CA  VAL B  18     5499   7876   6179    -53   1490   -386       C  
+ATOM   3692  C   VAL B  18     -24.251  16.279  17.899  1.00 56.89           C  
+ANISOU 3692  C   VAL B  18     5928   8544   7142    -25   1446   -618       C  
+ATOM   3693  O   VAL B  18     -25.003  15.496  17.319  1.00 59.10           O  
+ANISOU 3693  O   VAL B  18     6141   8776   7537   -123   1484   -566       O  
+ATOM   3694  CB  VAL B  18     -22.547  15.543  19.575  1.00 48.47           C  
+ANISOU 3694  CB  VAL B  18     5125   7746   5546    -66   1746   -387       C  
+ATOM   3695  CG1 VAL B  18     -23.701  14.686  20.086  1.00 46.92           C  
+ANISOU 3695  CG1 VAL B  18     4778   7705   5345   -175   2017   -435       C  
+ATOM   3696  CG2 VAL B  18     -21.225  14.807  19.722  1.00 43.06           C  
+ANISOU 3696  CG2 VAL B  18     4662   7051   4647   -112   1775   -112       C  
+HETATM 3697  N   MSE B  19     -24.653  17.453  18.376  1.00 64.65           N  
+ANISOU 3697  N   MSE B  19     6750   9546   8267    118   1345   -892       N  
+HETATM 3698  CA  MSE B  19     -26.036  17.897  18.256  1.00 56.38           C  
+ANISOU 3698  CA  MSE B  19     5388   8468   7564    191   1282  -1166       C  
+HETATM 3699  C   MSE B  19     -26.441  18.064  16.798  1.00 55.19           C  
+ANISOU 3699  C   MSE B  19     5255   8026   7686    171    922  -1094       C  
+HETATM 3700  O   MSE B  19     -27.619  17.967  16.454  1.00 57.32           O  
+ANISOU 3700  O   MSE B  19     5274   8245   8260    175    852  -1228       O  
+HETATM 3701  CB  MSE B  19     -26.245  19.214  19.003  1.00 56.22           C  
+ANISOU 3701  CB  MSE B  19     5212   8474   7675    385   1206  -1508       C  
+HETATM 3702  CG  MSE B  19     -27.686  19.472  19.395  1.00 74.67           C  
+ANISOU 3702  CG  MSE B  19     7136  10895  10342    476   1315  -1869       C  
+HETATM 3703 SE   MSE B  19     -27.921  21.222  20.206  1.00197.07          SE  
+ANISOU 3703 SE   MSE B  19    22445  26355  26077    771   1176  -2371      SE  
+HETATM 3704  CE  MSE B  19     -26.551  21.130  21.589  1.00 58.82           C  
+ANISOU 3704  CE  MSE B  19     5276   9122   7950    705   1467  -2289       C  
+ATOM   3705  N   GLU B  20     -25.457  18.320  15.946  1.00 59.19           N  
+ANISOU 3705  N   GLU B  20     6063   8347   8079    130    690   -883       N  
+ATOM   3706  CA  GLU B  20     -25.725  18.521  14.536  1.00 62.96           C  
+ANISOU 3706  CA  GLU B  20     6654   8549   8721     66    332   -787       C  
+ATOM   3707  C   GLU B  20     -25.587  17.194  13.807  1.00 62.15           C  
+ANISOU 3707  C   GLU B  20     6723   8441   8452   -121    461   -551       C  
+ATOM   3708  O   GLU B  20     -25.688  17.131  12.579  1.00 67.24           O  
+ANISOU 3708  O   GLU B  20     7543   8877   9127   -226    208   -438       O  
+ATOM   3709  CB  GLU B  20     -24.773  19.565  13.950  1.00 66.88           C  
+ANISOU 3709  CB  GLU B  20     7409   8845   9155     72     26   -691       C  
+ATOM   3710  CG  GLU B  20     -25.185  21.001  14.237  1.00 69.07           C  
+ANISOU 3710  CG  GLU B  20     7544   8979   9719    251   -281   -933       C  
+ATOM   3711  CD  GLU B  20     -26.523  21.361  13.627  1.00 71.23           C  
+ANISOU 3711  CD  GLU B  20     7613   9048  10403    318   -612  -1087       C  
+ATOM   3712  OE1 GLU B  20     -26.871  20.793  12.569  1.00 73.37           O  
+ANISOU 3712  OE1 GLU B  20     7997   9193  10688    174   -765   -923       O  
+ATOM   3713  OE2 GLU B  20     -27.228  22.214  14.204  1.00 70.06           O  
+ANISOU 3713  OE2 GLU B  20     7184   8853  10581    521   -736  -1391       O  
+ATOM   3714  N   GLU B  21     -25.351  16.140  14.584  1.00 56.54           N  
+ANISOU 3714  N   GLU B  21     5990   7943   7550   -173    838   -481       N  
+ATOM   3715  CA  GLU B  21     -25.314  14.770  14.081  1.00 64.91           C  
+ANISOU 3715  CA  GLU B  21     7180   8988   8493   -332    987   -295       C  
+ATOM   3716  C   GLU B  21     -24.242  14.612  13.005  1.00 54.43           C  
+ANISOU 3716  C   GLU B  21     6195   7503   6981   -414    884   -101       C  
+ATOM   3717  O   GLU B  21     -24.424  13.894  12.022  1.00 55.42           O  
+ANISOU 3717  O   GLU B  21     6472   7499   7087   -542    830    -13       O  
+ATOM   3718  CB  GLU B  21     -26.694  14.350  13.563  1.00 59.88           C  
+ANISOU 3718  CB  GLU B  21     6358   8275   8120   -408    883   -377       C  
+ATOM   3719  CG  GLU B  21     -27.798  14.512  14.606  1.00 76.80           C  
+ANISOU 3719  CG  GLU B  21     8097  10600  10482   -344   1042   -606       C  
+ATOM   3720  CD  GLU B  21     -29.058  13.744  14.258  1.00 74.79           C  
+ANISOU 3720  CD  GLU B  21     7621  10319  10479   -470   1039   -649       C  
+ATOM   3721  OE1 GLU B  21     -30.118  14.039  14.850  1.00 89.01           O  
+ANISOU 3721  OE1 GLU B  21     9027  12235  12559   -421   1113   -881       O  
+ATOM   3722  OE2 GLU B  21     -28.993  12.855  13.382  1.00 71.47           O  
+ANISOU 3722  OE2 GLU B  21     7404   9758   9993   -621    965   -473       O  
+ATOM   3723  N   ASN B  22     -23.123  15.303  13.204  1.00 52.06           N  
+ANISOU 3723  N   ASN B  22     6012   7221   6547   -355    871    -57       N  
+ATOM   3724  CA  ASN B  22     -22.003  15.255  12.273  1.00 50.72           C  
+ANISOU 3724  CA  ASN B  22     6123   6944   6205   -446    837    100       C  
+ATOM   3725  C   ASN B  22     -20.689  14.888  12.957  1.00 48.34           C  
+ANISOU 3725  C   ASN B  22     5864   6771   5734   -407   1079    200       C  
+ATOM   3726  O   ASN B  22     -19.610  15.096  12.404  1.00 59.59           O  
+ANISOU 3726  O   ASN B  22     7441   8147   7055   -457   1079    290       O  
+ATOM   3727  CB  ASN B  22     -21.859  16.607  11.568  1.00 57.76           C  
+ANISOU 3727  CB  ASN B  22     7123   7675   7147   -464    505     82       C  
+ATOM   3728  CG  ASN B  22     -21.032  16.524  10.302  1.00 56.42           C  
+ANISOU 3728  CG  ASN B  22     7268   7382   6788   -640    465    235       C  
+ATOM   3729  OD1 ASN B  22     -21.252  15.659   9.455  1.00 55.23           O  
+ANISOU 3729  OD1 ASN B  22     7268   7165   6551   -762    513    286       O  
+ATOM   3730  ND2 ASN B  22     -20.063  17.422  10.173  1.00 55.85           N  
+ANISOU 3730  ND2 ASN B  22     7301   7282   6636   -676    393    295       N  
+ATOM   3731  N   ALA B  23     -20.779  14.325  14.157  1.00 59.00           N  
+ANISOU 3731  N   ALA B  23     7075   8286   7058   -336   1277    188       N  
+ATOM   3732  CA  ALA B  23     -19.582  13.922  14.884  1.00 47.65           C  
+ANISOU 3732  CA  ALA B  23     5674   6946   5487   -292   1438    297       C  
+ATOM   3733  C   ALA B  23     -19.210  12.479  14.574  1.00 50.71           C  
+ANISOU 3733  C   ALA B  23     6160   7284   5824   -347   1619    433       C  
+ATOM   3734  O   ALA B  23     -20.077  11.655  14.284  1.00 58.81           O  
+ANISOU 3734  O   ALA B  23     7194   8260   6892   -418   1673    435       O  
+ATOM   3735  CB  ALA B  23     -19.783  14.105  16.380  1.00 37.48           C  
+ANISOU 3735  CB  ALA B  23     4251   5844   4144   -209   1515    233       C  
+ATOM   3736  N   ALA B  24     -17.918  12.179  14.637  1.00 55.05           N  
+ANISOU 3736  N   ALA B  24     6766   7828   6324   -311   1694    531       N  
+ATOM   3737  CA  ALA B  24     -17.445  10.816  14.438  1.00 55.25           C  
+ANISOU 3737  CA  ALA B  24     6865   7773   6354   -318   1848    633       C  
+ATOM   3738  C   ALA B  24     -16.493  10.412  15.556  1.00 54.47           C  
+ANISOU 3738  C   ALA B  24     6713   7742   6239   -220   1893    742       C  
+ATOM   3739  O   ALA B  24     -15.828  11.260  16.152  1.00 61.50           O  
+ANISOU 3739  O   ALA B  24     7535   8727   7106   -160   1807    738       O  
+ATOM   3740  CB  ALA B  24     -16.767  10.682  13.084  1.00 49.54           C  
+ANISOU 3740  CB  ALA B  24     6263   6920   5642   -372   1893    615       C  
+ATOM   3741  N   ILE B  25     -16.436   9.116  15.841  1.00 44.15           N  
+ANISOU 3741  N   ILE B  25     5455   6360   4959   -213   1981    847       N  
+ATOM   3742  CA  ILE B  25     -15.509   8.594  16.839  1.00 39.74           C  
+ANISOU 3742  CA  ILE B  25     4879   5812   4410   -123   1958    983       C  
+ATOM   3743  C   ILE B  25     -14.535   7.613  16.196  1.00 61.56           C  
+ANISOU 3743  C   ILE B  25     7662   8385   7342    -49   2017   1022       C  
+ATOM   3744  O   ILE B  25     -14.967   6.736  15.466  1.00 53.89           O  
+ANISOU 3744  O   ILE B  25     6783   7266   6427    -94   2106    998       O  
+ATOM   3745  CB  ILE B  25     -16.258   7.869  17.983  1.00 42.97           C  
+ANISOU 3745  CB  ILE B  25     5346   6274   4706   -185   1971   1106       C  
+ATOM   3746  CG1 ILE B  25     -17.222   8.817  18.704  1.00 40.12           C  
+ANISOU 3746  CG1 ILE B  25     4929   6129   4187   -249   1972   1013       C  
+ATOM   3747  CG2 ILE B  25     -15.274   7.235  18.958  1.00 41.90           C  
+ANISOU 3747  CG2 ILE B  25     5252   6098   4571   -110   1876   1289       C  
+ATOM   3748  CD1 ILE B  25     -16.538   9.912  19.488  1.00 44.13           C  
+ANISOU 3748  CD1 ILE B  25     5387   6780   4600   -171   1857    971       C  
+ATOM   3749  N   PHE B  26     -13.237   7.732  16.453  1.00 40.64           N  
+ANISOU 3749  N   PHE B  26     4911   5724   4805     67   1964   1057       N  
+ATOM   3750  CA  PHE B  26     -12.348   6.640  16.068  1.00 53.03           C  
+ANISOU 3750  CA  PHE B  26     6453   7098   6597    175   2018   1075       C  
+ATOM   3751  C   PHE B  26     -11.753   6.071  17.340  1.00 53.21           C  
+ANISOU 3751  C   PHE B  26     6449   7075   6692    277   1837   1260       C  
+ATOM   3752  O   PHE B  26     -11.075   6.766  18.093  1.00 50.00           O  
+ANISOU 3752  O   PHE B  26     5943   6781   6274    326   1688   1311       O  
+ATOM   3753  CB  PHE B  26     -11.255   7.069  15.072  1.00 47.91           C  
+ANISOU 3753  CB  PHE B  26     5668   6436   6101    224   2133    932       C  
+ATOM   3754  CG  PHE B  26     -10.539   5.901  14.396  1.00 57.71           C  
+ANISOU 3754  CG  PHE B  26     6870   7465   7592    336   2270    854       C  
+ATOM   3755  CD1 PHE B  26     -10.370   5.880  13.020  1.00 63.06           C  
+ANISOU 3755  CD1 PHE B  26     7577   8102   8281    280   2507    658       C  
+ATOM   3756  CD2 PHE B  26     -10.122   4.790  15.119  1.00 68.60           C  
+ANISOU 3756  CD2 PHE B  26     8221   8666   9180    484   2152    967       C  
+ATOM   3757  CE1 PHE B  26      -9.751   4.806  12.392  1.00 61.44           C  
+ANISOU 3757  CE1 PHE B  26     7338   7702   8306    393   2667    526       C  
+ATOM   3758  CE2 PHE B  26      -9.494   3.725  14.499  1.00 76.24           C  
+ANISOU 3758  CE2 PHE B  26     9138   9400  10429    618   2261    856       C  
+ATOM   3759  CZ  PHE B  26      -9.316   3.731  13.136  1.00 71.64           C  
+ANISOU 3759  CZ  PHE B  26     8555   8797   9867    582   2541    611       C  
+ATOM   3760  N   ALA B  27     -12.018   4.789  17.565  1.00 57.01           N  
+ANISOU 3760  N   ALA B  27     7048   7366   7246    291   1812   1372       N  
+ATOM   3761  CA  ALA B  27     -11.678   4.153  18.829  1.00 60.01           C  
+ANISOU 3761  CA  ALA B  27     7490   7672   7640    337   1588   1602       C  
+ATOM   3762  C   ALA B  27     -10.466   3.239  18.677  1.00 63.04           C  
+ANISOU 3762  C   ALA B  27     7769   7786   8398    540   1480   1628       C  
+ATOM   3763  O   ALA B  27     -10.437   2.358  17.818  1.00 65.66           O  
+ANISOU 3763  O   ALA B  27     8114   7896   8939    602   1597   1530       O  
+ATOM   3764  CB  ALA B  27     -12.862   3.372  19.363  1.00 57.00           C  
+ANISOU 3764  CB  ALA B  27     7335   7249   7074    172   1591   1756       C  
+ATOM   3765  N   GLY B  28      -9.464   3.469  19.519  1.00 68.21           N  
+ANISOU 3765  N   GLY B  28     8308   8450   9158    652   1236   1738       N  
+ATOM   3766  CA  GLY B  28      -8.291   2.619  19.577  1.00 76.28           C  
+ANISOU 3766  CA  GLY B  28     9186   9201  10597    870   1058   1777       C  
+ATOM   3767  C   GLY B  28      -8.456   1.552  20.641  1.00 77.34           C  
+ANISOU 3767  C   GLY B  28     9548   9116  10722    861    750   2074       C  
+ATOM   3768  O   GLY B  28      -9.506   1.458  21.276  1.00 81.44           O  
+ANISOU 3768  O   GLY B  28    10341   9725  10877    652    741   2240       O  
+ATOM   3769  N   ALA B  29      -7.419   0.742  20.828  1.00 81.57           N  
+ANISOU 3769  N   ALA B  29     9966   9355  11673   1076    495   2141       N  
+ATOM   3770  CA  ALA B  29      -7.478  -0.387  21.750  1.00 82.86           C  
+ANISOU 3770  CA  ALA B  29    10374   9225  11884   1074    140   2450       C  
+ATOM   3771  C   ALA B  29      -7.664   0.054  23.200  1.00 81.66           C  
+ANISOU 3771  C   ALA B  29    10450   9246  11330    899   -159   2751       C  
+ATOM   3772  O   ALA B  29      -8.188  -0.699  24.020  1.00 86.20           O  
+ANISOU 3772  O   ALA B  29    11359   9687  11704    747   -362   3045       O  
+ATOM   3773  CB  ALA B  29      -6.221  -1.230  21.619  1.00 86.49           C  
+ANISOU 3773  CB  ALA B  29    10607   9305  12951   1385   -123   2427       C  
+ATOM   3774  N   GLY B  30      -7.226   1.270  23.513  1.00 81.10           N  
+ANISOU 3774  N   GLY B  30    10225   9465  11124    897   -185   2675       N  
+ATOM   3775  CA  GLY B  30      -7.333   1.800  24.860  1.00 80.21           C  
+ANISOU 3775  CA  GLY B  30    10336   9538  10602    734   -457   2901       C  
+ATOM   3776  C   GLY B  30      -8.757   1.930  25.370  1.00 80.07           C  
+ANISOU 3776  C   GLY B  30    10665   9746  10012    425   -254   2995       C  
+ATOM   3777  O   GLY B  30      -9.016   1.766  26.562  1.00 75.59           O  
+ANISOU 3777  O   GLY B  30    10411   9225   9084    244   -479   3257       O  
+ATOM   3778  N   LEU B  31      -9.682   2.227  24.462  1.00 80.31           N  
+ANISOU 3778  N   LEU B  31    10635   9919   9958    349    170   2775       N  
+ATOM   3779  CA  LEU B  31     -11.083   2.415  24.826  1.00 66.46           C  
+ANISOU 3779  CA  LEU B  31     9112   8397   7743     72    408   2802       C  
+ATOM   3780  C   LEU B  31     -11.740   1.100  25.243  1.00 70.51           C  
+ANISOU 3780  C   LEU B  31     9926   8698   8165   -102    351   3076       C  
+ATOM   3781  O   LEU B  31     -12.741   1.097  25.960  1.00 69.81           O  
+ANISOU 3781  O   LEU B  31    10072   8793   7659   -379    467   3194       O  
+ATOM   3782  CB  LEU B  31     -11.856   3.044  23.663  1.00 61.20           C  
+ANISOU 3782  CB  LEU B  31     8270   7887   7096     57    806   2497       C  
+ATOM   3783  CG  LEU B  31     -13.245   3.606  23.980  1.00 55.47           C  
+ANISOU 3783  CG  LEU B  31     7652   7456   5967   -184   1060   2432       C  
+ATOM   3784  CD1 LEU B  31     -13.138   4.836  24.867  1.00 54.37           C  
+ANISOU 3784  CD1 LEU B  31     7518   7617   5524   -223   1001   2366       C  
+ATOM   3785  CD2 LEU B  31     -14.006   3.932  22.708  1.00 51.32           C  
+ANISOU 3785  CD2 LEU B  31     6967   6974   5559   -184   1360   2174       C  
+ATOM   3786  N   SER B  32     -11.167  -0.014  24.801  1.00 71.12           N  
+ANISOU 3786  N   SER B  32     9990   8382   8651     53    179   3165       N  
+ATOM   3787  CA  SER B  32     -11.701  -1.330  25.133  1.00 72.54           C  
+ANISOU 3787  CA  SER B  32    10469   8283   8811   -108     70   3443       C  
+ATOM   3788  C   SER B  32     -11.110  -1.862  26.434  1.00 75.76           C  
+ANISOU 3788  C   SER B  32    11156   8524   9106   -168   -402   3827       C  
+ATOM   3789  O   SER B  32     -11.425  -2.972  26.862  1.00 76.28           O  
+ANISOU 3789  O   SER B  32    11523   8316   9143   -325   -582   4126       O  
+ATOM   3790  CB  SER B  32     -11.437  -2.316  23.995  1.00 74.81           C  
+ANISOU 3790  CB  SER B  32    10639   8177   9608     90     94   3327       C  
+ATOM   3791  OG  SER B  32     -11.875  -1.791  22.755  1.00 72.27           O  
+ANISOU 3791  OG  SER B  32    10094   8003   9361    138    487   2974       O  
+HETATM 3792  N   MSE B  33     -10.249  -1.063  27.055  1.00 78.84           N  
+ANISOU 3792  N   MSE B  33    11467   9059   9430    -64   -638   3832       N  
+HETATM 3793  CA  MSE B  33      -9.650  -1.422  28.334  1.00 84.83           C  
+ANISOU 3793  CA  MSE B  33    12515   9684  10033   -137  -1145   4197       C  
+HETATM 3794  C   MSE B  33     -10.249  -0.571  29.449  1.00 89.19           C  
+ANISOU 3794  C   MSE B  33    13336  10656   9895   -446  -1073   4279       C  
+HETATM 3795  O   MSE B  33     -10.427   0.637  29.287  1.00 96.32           O  
+ANISOU 3795  O   MSE B  33    14048  11921  10627   -429   -805   3992       O  
+HETATM 3796  CB  MSE B  33      -8.131  -1.246  28.286  1.00 81.95           C  
+ANISOU 3796  CB  MSE B  33    11865   9125  10146    210  -1552   4152       C  
+HETATM 3797  CG  MSE B  33      -7.454  -1.995  27.148  1.00 84.66           C  
+ANISOU 3797  CG  MSE B  33    11878   9084  11205    548  -1563   3984       C  
+HETATM 3798 SE   MSE B  33      -7.466  -3.931  27.381  1.00127.97          SE  
+ANISOU 3798 SE   MSE B  33    17692  13922  17008    553  -1975   4358      SE  
+HETATM 3799  CE  MSE B  33      -5.982  -4.091  28.635  1.00112.80           C  
+ANISOU 3799  CE  MSE B  33    15824  11724  15313    719  -2829   4697       C  
+ATOM   3800  N   SER B  34     -10.566  -1.204  30.574  1.00 89.99           N  
+ANISOU 3800  N   SER B  34    13901  10699   9591   -741  -1308   4661       N  
+ATOM   3801  CA  SER B  34     -11.127  -0.491  31.716  1.00 91.06           C  
+ANISOU 3801  CA  SER B  34    14346  11236   9015  -1068  -1221   4733       C  
+ATOM   3802  C   SER B  34     -10.128   0.522  32.259  1.00101.46           C  
+ANISOU 3802  C   SER B  34    15583  12700  10268   -917  -1530   4645       C  
+ATOM   3803  O   SER B  34     -10.505   1.605  32.708  1.00107.68           O  
+ANISOU 3803  O   SER B  34    16403  13889  10620  -1042  -1312   4452       O  
+ATOM   3804  CB  SER B  34     -11.541  -1.471  32.816  1.00 98.34           C  
+ANISOU 3804  CB  SER B  34    15827  12034   9503  -1446  -1445   5196       C  
+ATOM   3805  OG  SER B  34     -12.614  -2.291  32.387  1.00106.91           O  
+ANISOU 3805  OG  SER B  34    16953  13048  10620  -1625  -1083   5202       O  
+ATOM   3806  N   VAL B  35      -8.849   0.163  32.213  1.00 98.46           N  
+ANISOU 3806  N   VAL B  35    15076  11971  10361   -642  -2051   4767       N  
+ATOM   3807  CA  VAL B  35      -7.789   1.047  32.678  1.00 92.69           C  
+ANISOU 3807  CA  VAL B  35    14223  11326   9669   -490  -2414   4698       C  
+ATOM   3808  C   VAL B  35      -7.468   2.114  31.634  1.00 85.59           C  
+ANISOU 3808  C   VAL B  35    12783  10605   9135   -221  -2104   4249       C  
+ATOM   3809  O   VAL B  35      -6.755   3.077  31.918  1.00 83.13           O  
+ANISOU 3809  O   VAL B  35    12327  10435   8823   -133  -2293   4122       O  
+ATOM   3810  CB  VAL B  35      -6.509   0.260  33.019  1.00 95.36           C  
+ANISOU 3810  CB  VAL B  35    14568  11208  10456   -290  -3128   4992       C  
+ATOM   3811  CG1 VAL B  35      -6.752  -0.651  34.211  1.00103.27           C  
+ANISOU 3811  CG1 VAL B  35    16186  12037  11017   -601  -3531   5476       C  
+ATOM   3812  CG2 VAL B  35      -6.042  -0.543  31.815  1.00102.84           C  
+ANISOU 3812  CG2 VAL B  35    15107  11769  12199     53  -3098   4885       C  
+ATOM   3813  N   GLY B  36      -7.997   1.938  30.426  1.00 80.96           N  
+ANISOU 3813  N   GLY B  36    11925   9995   8839   -118  -1650   4024       N  
+ATOM   3814  CA  GLY B  36      -7.890   2.950  29.390  1.00 78.22           C  
+ANISOU 3814  CA  GLY B  36    11145   9837   8741     61  -1304   3622       C  
+ATOM   3815  C   GLY B  36      -6.673   2.812  28.494  1.00 82.14           C  
+ANISOU 3815  C   GLY B  36    11196  10077   9937    405  -1453   3495       C  
+ATOM   3816  O   GLY B  36      -6.475   3.614  27.581  1.00 86.83           O  
+ANISOU 3816  O   GLY B  36    11438  10806  10746    529  -1177   3186       O  
+ATOM   3817  N   TYR B  37      -5.855   1.797  28.750  1.00100.68           N  
+ANISOU 3817  N   TYR B  37    13556  12047  12652    548  -1891   3728       N  
+ATOM   3818  CA  TYR B  37      -4.629   1.589  27.985  1.00 95.19           C  
+ANISOU 3818  CA  TYR B  37    12394  11097  12679    891  -2040   3585       C  
+ATOM   3819  C   TYR B  37      -4.241   0.116  27.907  1.00 92.51           C  
+ANISOU 3819  C   TYR B  37    12089  10270  12790   1054  -2340   3782       C  
+ATOM   3820  O   TYR B  37      -4.829  -0.726  28.583  1.00100.02           O  
+ANISOU 3820  O   TYR B  37    13475  11060  13470    875  -2528   4096       O  
+ATOM   3821  CB  TYR B  37      -3.485   2.404  28.594  1.00 95.29           C  
+ANISOU 3821  CB  TYR B  37    12208  11178  12820    983  -2450   3588       C  
+ATOM   3822  CG  TYR B  37      -3.111   1.983  29.999  1.00 94.28           C  
+ANISOU 3822  CG  TYR B  37    12441  10894  12488    887  -3098   3974       C  
+ATOM   3823  CD1 TYR B  37      -2.143   1.012  30.223  1.00 94.43           C  
+ANISOU 3823  CD1 TYR B  37    12363  10476  13040   1102  -3643   4180       C  
+ATOM   3824  CD2 TYR B  37      -3.730   2.555  31.101  1.00101.65           C  
+ANISOU 3824  CD2 TYR B  37    13827  12105  12691    577  -3178   4122       C  
+ATOM   3825  CE1 TYR B  37      -1.802   0.626  31.506  1.00108.40           C  
+ANISOU 3825  CE1 TYR B  37    14509  12074  14604    993  -4304   4568       C  
+ATOM   3826  CE2 TYR B  37      -3.395   2.177  32.387  1.00106.01           C  
+ANISOU 3826  CE2 TYR B  37    14777  12524  12978    445  -3779   4488       C  
+ATOM   3827  CZ  TYR B  37      -2.432   1.212  32.584  1.00114.48           C  
+ANISOU 3827  CZ  TYR B  37    15779  13146  14574    645  -4368   4734       C  
+ATOM   3828  OH  TYR B  37      -2.095   0.830  33.863  1.00126.49           O  
+ANISOU 3828  OH  TYR B  37    17739  14505  15817    494  -5037   5133       O  
+ATOM   3829  N   VAL B  38      -3.244  -0.185  27.079  1.00101.35           N  
+ANISOU 3829  N   VAL B  38    12747  11148  14612   1384  -2378   3584       N  
+ATOM   3830  CA  VAL B  38      -2.740  -1.549  26.947  1.00103.68           C  
+ANISOU 3830  CA  VAL B  38    13004  10932  15457   1609  -2692   3704       C  
+ATOM   3831  C   VAL B  38      -1.255  -1.619  27.287  1.00 96.53           C  
+ANISOU 3831  C   VAL B  38    11735   9781  15162   1901  -3238   3733       C  
+ATOM   3832  O   VAL B  38      -0.825  -2.479  28.056  1.00124.66           O  
+ANISOU 3832  O   VAL B  38    15472  12960  18933   1974  -3839   4045       O  
+ATOM   3833  CB  VAL B  38      -2.944  -2.098  25.522  1.00101.16           C  
+ANISOU 3833  CB  VAL B  38    12437  10471  15527   1780  -2208   3377       C  
+ATOM   3834  CG1 VAL B  38      -4.361  -1.828  25.044  1.00 91.03           C  
+ANISOU 3834  CG1 VAL B  38    11420   9473  13696   1501  -1661   3291       C  
+ATOM   3835  CG2 VAL B  38      -1.931  -1.482  24.567  1.00102.62           C  
+ANISOU 3835  CG2 VAL B  38    12015  10747  16228   2045  -1974   2979       C  
+ATOM   3836  N   LEU B  84      -4.292 -10.360  19.937  1.00126.45           N  
+ANISOU 3836  N   LEU B  84    15924  10715  21405   2806  -1514   2288       N  
+ATOM   3837  CA  LEU B  84      -4.880 -11.210  18.909  1.00123.88           C  
+ANISOU 3837  CA  LEU B  84    15748  10111  21211   2819  -1235   2007       C  
+ATOM   3838  C   LEU B  84      -6.051 -12.013  19.469  1.00125.04           C  
+ANISOU 3838  C   LEU B  84    16468  10010  21030   2476  -1480   2427       C  
+ATOM   3839  O   LEU B  84      -7.087 -11.449  19.822  1.00114.34           O  
+ANISOU 3839  O   LEU B  84    15381   9045  19018   2069  -1312   2667       O  
+ATOM   3840  CB  LEU B  84      -3.824 -12.150  18.323  1.00124.93           C  
+ANISOU 3840  CB  LEU B  84    15569   9700  22198   3303  -1366   1642       C  
+ATOM   3841  N   ASP B  85      -5.884 -13.331  19.533  1.00129.69           N  
+ANISOU 3841  N   ASP B  85    17225   9939  22111   2636  -1869   2497       N  
+ATOM   3842  CA  ASP B  85      -6.884 -14.219  20.120  1.00128.89           C  
+ANISOU 3842  CA  ASP B  85    17676   9519  21779   2298  -2170   2937       C  
+ATOM   3843  C   ASP B  85      -7.170 -13.851  21.576  1.00137.28           C  
+ANISOU 3843  C   ASP B  85    19031  10781  22350   1966  -2538   3551       C  
+ATOM   3844  O   ASP B  85      -8.321 -13.824  22.011  1.00134.99           O  
+ANISOU 3844  O   ASP B  85    19128  10682  21481   1504  -2450   3869       O  
+ATOM   3845  CB  ASP B  85      -6.426 -15.676  20.024  1.00117.39           C  
+ANISOU 3845  CB  ASP B  85    16319   7340  20943   2556  -2587   2884       C  
+ATOM   3846  N   GLU B  86      -6.100 -13.572  22.314  1.00140.99           N  
+ANISOU 3846  N   GLU B  86    19299  11209  23060   2197  -2943   3693       N  
+ATOM   3847  CA  GLU B  86      -6.158 -13.161  23.718  1.00131.86           C  
+ANISOU 3847  CA  GLU B  86    18404  10294  21402   1910  -3303   4204       C  
+ATOM   3848  C   GLU B  86      -6.946 -11.870  23.963  1.00126.67           C  
+ANISOU 3848  C   GLU B  86    17801  10343  19983   1548  -2874   4279       C  
+ATOM   3849  O   GLU B  86      -7.654 -11.745  24.971  1.00135.39           O  
+ANISOU 3849  O   GLU B  86    19313  11628  20502   1135  -3007   4720       O  
+ATOM   3850  CB  GLU B  86      -4.740 -12.999  24.269  1.00125.77           C  
+ANISOU 3850  CB  GLU B  86    17302   9494  20993   2244  -3714   4154       C  
+ATOM   3851  N   PHE B  87      -6.797 -10.912  23.051  1.00116.27           N  
+ANISOU 3851  N   PHE B  87    16072   9456  18650   1691  -2340   3811       N  
+ATOM   3852  CA  PHE B  87      -7.473  -9.617  23.147  1.00115.06           C  
+ANISOU 3852  CA  PHE B  87    15902   9984  17832   1404  -1907   3776       C  
+ATOM   3853  C   PHE B  87      -8.962  -9.741  23.458  1.00120.64           C  
+ANISOU 3853  C   PHE B  87    17040  10869  17931    916  -1709   4029       C  
+ATOM   3854  O   PHE B  87      -9.453  -9.111  24.395  1.00121.65           O  
+ANISOU 3854  O   PHE B  87    17367  11360  17493    604  -1716   4305       O  
+ATOM   3855  CB  PHE B  87      -7.285  -8.831  21.847  1.00106.08           C  
+ANISOU 3855  CB  PHE B  87    14336   9158  16813   1594  -1345   3225       C  
+ATOM   3856  N   SER B  88      -9.677 -10.540  22.673  1.00120.59           N  
+ANISOU 3856  N   SER B  88    17159  10613  18049    842  -1520   3908       N  
+ATOM   3857  CA  SER B  88     -11.100 -10.764  22.910  1.00123.06           C  
+ANISOU 3857  CA  SER B  88    17830  11052  17874    370  -1340   4135       C  
+ATOM   3858  C   SER B  88     -11.334 -11.357  24.295  1.00125.74           C  
+ANISOU 3858  C   SER B  88    18615  11210  17951     60  -1786   4720       C  
+ATOM   3859  O   SER B  88     -12.329 -11.057  24.955  1.00128.24           O  
+ANISOU 3859  O   SER B  88    19180  11860  17687   -380  -1623   4970       O  
+ATOM   3860  CB  SER B  88     -11.685 -11.688  21.844  1.00130.22           C  
+ANISOU 3860  CB  SER B  88    18807  11611  19059    365  -1176   3921       C  
+ATOM   3861  N   ARG B  89     -10.403 -12.202  24.726  1.00124.07           N  
+ANISOU 3861  N   ARG B  89    18500  10460  18179    284  -2354   4929       N  
+ATOM   3862  CA  ARG B  89     -10.488 -12.847  26.029  1.00120.99           C  
+ANISOU 3862  CA  ARG B  89    18532   9925  17512     11  -2792   5412       C  
+ATOM   3863  C   ARG B  89     -10.108 -11.921  27.183  1.00126.50           C  
+ANISOU 3863  C   ARG B  89    19272  11049  17744    -95  -2938   5618       C  
+ATOM   3864  O   ARG B  89     -10.222 -12.308  28.347  1.00136.25           O  
+ANISOU 3864  O   ARG B  89    20831  12332  18607   -358  -3192   5918       O  
+ATOM   3865  CB  ARG B  89      -9.599 -14.093  26.058  1.00119.05           C  
+ANISOU 3865  CB  ARG B  89    18297   9082  17855    320  -3287   5395       C  
+ATOM   3866  N   LYS B  90      -9.653 -10.708  26.879  1.00115.71           N  
+ANISOU 3866  N   LYS B  90    17571  10011  16383     99  -2763   5422       N  
+ATOM   3867  CA  LYS B  90      -9.248  -9.803  27.954  1.00121.71           C  
+ANISOU 3867  CA  LYS B  90    18388  11137  16721      5  -2948   5611       C  
+ATOM   3868  C   LYS B  90     -10.100  -8.519  28.061  1.00124.47           C  
+ANISOU 3868  C   LYS B  90    18685  12199  16410   -273  -2389   5457       C  
+ATOM   3869  O   LYS B  90      -9.938  -7.743  29.004  1.00131.57           O  
+ANISOU 3869  O   LYS B  90    19695  13428  16867   -412  -2497   5605       O  
+ATOM   3870  CB  LYS B  90      -7.764  -9.444  27.753  1.00122.65           C  
+ANISOU 3870  CB  LYS B  90    18078  11119  17404    507  -3258   5401       C  
+ATOM   3871  CG  LYS B  90      -7.113  -8.571  28.821  1.00117.03           C  
+ANISOU 3871  CG  LYS B  90    17389  10695  16383    474  -3568   5570       C  
+ATOM   3872  CD  LYS B  90      -6.981  -9.295  30.147  1.00126.78           C  
+ANISOU 3872  CD  LYS B  90    19032  11816  17320    252  -4019   5884       C  
+ATOM   3873  CE  LYS B  90      -6.339  -8.397  31.193  1.00131.74           C  
+ANISOU 3873  CE  LYS B  90    19686  12755  17612    206  -4299   5977       C  
+ATOM   3874  NZ  LYS B  90      -4.937  -8.039  30.837  1.00134.71           N  
+ANISOU 3874  NZ  LYS B  90    19569  12969  18644    679  -4619   5771       N  
+ATOM   3875  N   VAL B  91     -11.037  -8.310  27.138  1.00116.29           N  
+ANISOU 3875  N   VAL B  91    17501  11382  15301   -363  -1823   5159       N  
+ATOM   3876  CA  VAL B  91     -11.832  -7.075  27.161  1.00111.61           C  
+ANISOU 3876  CA  VAL B  91    16802  11426  14180   -572  -1319   4964       C  
+ATOM   3877  C   VAL B  91     -13.354  -7.244  27.303  1.00118.32           C  
+ANISOU 3877  C   VAL B  91    17891  12493  14573  -1038   -943   5069       C  
+ATOM   3878  O   VAL B  91     -13.915  -8.274  26.926  1.00128.04           O  
+ANISOU 3878  O   VAL B  91    19275  13399  15975  -1170   -938   5171       O  
+ATOM   3879  CB  VAL B  91     -11.572  -6.238  25.894  1.00103.63           C  
+ANISOU 3879  CB  VAL B  91    15299  10619  13459   -253   -939   4439       C  
+ATOM   3880  CG1 VAL B  91     -10.119  -5.798  25.845  1.00110.19           C  
+ANISOU 3880  CG1 VAL B  91    15826  11373  14666    145  -1215   4306       C  
+ATOM   3881  CG2 VAL B  91     -11.930  -7.031  24.650  1.00 98.67           C  
+ANISOU 3881  CG2 VAL B  91    14574   9688  13227   -153   -739   4217       C  
+ATOM   3882  N   ASP B  92     -14.007  -6.214  27.844  1.00107.85           N  
+ANISOU 3882  N   ASP B  92    16570  11711  12697  -1280   -630   5018       N  
+ATOM   3883  CA  ASP B  92     -15.472  -6.128  27.908  1.00107.73           C  
+ANISOU 3883  CA  ASP B  92    16644  12000  12286  -1690   -182   5013       C  
+ATOM   3884  C   ASP B  92     -15.904  -4.654  28.069  1.00111.90           C  
+ANISOU 3884  C   ASP B  92    16953  13132  12433  -1732    207   4722       C  
+ATOM   3885  O   ASP B  92     -15.064  -3.756  28.129  1.00 99.17           O  
+ANISOU 3885  O   ASP B  92    15164  11670  10847  -1467    107   4556       O  
+ATOM   3886  CB  ASP B  92     -16.074  -7.037  28.992  1.00110.85           C  
+ANISOU 3886  CB  ASP B  92    17428  12325  12364  -2060   -276   5336       C  
+ATOM   3887  CG  ASP B  92     -15.629  -6.685  30.386  1.00130.09           C  
+ANISOU 3887  CG  ASP B  92    20082  14970  14377  -2138   -489   5489       C  
+ATOM   3888  OD1 ASP B  92     -14.412  -6.522  30.604  1.00130.03           O  
+ANISOU 3888  OD1 ASP B  92    20098  14786  14522  -1884   -923   5590       O  
+ATOM   3889  OD2 ASP B  92     -16.505  -6.601  31.272  1.00140.70           O  
+ANISOU 3889  OD2 ASP B  92    21559  16638  15261  -2455   -236   5500       O  
+ATOM   3890  N   LEU B  93     -17.213  -4.427  28.146  1.00114.70           N  
+ANISOU 3890  N   LEU B  93    17305  13805  12470  -2066    632   4656       N  
+ATOM   3891  CA  LEU B  93     -17.837  -3.099  28.043  1.00 97.90           C  
+ANISOU 3891  CA  LEU B  93    14901  12192  10104  -2076   1045   4301       C  
+ATOM   3892  C   LEU B  93     -17.654  -2.106  29.208  1.00 93.37           C  
+ANISOU 3892  C   LEU B  93    14398  12005   9073  -2111   1062   4242       C  
+ATOM   3893  O   LEU B  93     -17.636  -2.490  30.378  1.00106.05           O  
+ANISOU 3893  O   LEU B  93    16287  13622  10386  -2269    923   4434       O  
+ATOM   3894  CB  LEU B  93     -19.338  -3.321  27.825  1.00 76.43           C  
+ANISOU 3894  CB  LEU B  93    12059   9630   7350  -2314   1457   4136       C  
+ATOM   3895  CG  LEU B  93     -20.286  -2.184  27.465  1.00 73.30           C  
+ANISOU 3895  CG  LEU B  93    11308   9656   6887  -2305   1881   3729       C  
+ATOM   3896  CD1 LEU B  93     -20.034  -1.757  26.041  1.00 72.96           C  
+ANISOU 3896  CD1 LEU B  93    10997   9531   7193  -2078   1915   3504       C  
+ATOM   3897  CD2 LEU B  93     -21.723  -2.647  27.636  1.00 77.79           C  
+ANISOU 3897  CD2 LEU B  93    11789  10327   7441  -2557   2171   3669       C  
+ATOM   3898  N   THR B  94     -17.514  -0.823  28.854  1.00 85.37           N  
+ANISOU 3898  N   THR B  94    13113  11292   8032  -1939   1222   3932       N  
+ATOM   3899  CA  THR B  94     -17.291   0.274  29.809  1.00 84.67           C  
+ANISOU 3899  CA  THR B  94    13071  11559   7540  -1947   1234   3821       C  
+ATOM   3900  C   THR B  94     -18.324   1.405  29.663  1.00 87.43           C  
+ANISOU 3900  C   THR B  94    13130  12309   7782  -1951   1687   3381       C  
+ATOM   3901  O   THR B  94     -19.066   1.455  28.683  1.00 91.92           O  
+ANISOU 3901  O   THR B  94    13428  12883   8615  -1920   1941   3179       O  
+ATOM   3902  CB  THR B  94     -15.882   0.889  29.652  1.00 78.23           C  
+ANISOU 3902  CB  THR B  94    12146  10642   6936  -1589    875   3757       C  
+ATOM   3903  OG1 THR B  94     -15.816   1.642  28.434  1.00 81.76           O  
+ANISOU 3903  OG1 THR B  94    12179  11122   7762  -1301   1045   3383       O  
+ATOM   3904  CG2 THR B  94     -14.811  -0.192  29.641  1.00 77.92           C  
+ANISOU 3904  CG2 THR B  94    12259  10137   7212  -1449    397   4075       C  
+ATOM   3905  N   GLU B  95     -18.363   2.304  30.649  1.00 80.70           N  
+ANISOU 3905  N   GLU B  95    12339  11754   6568  -1977   1745   3229       N  
+ATOM   3906  CA  GLU B  95     -19.279   3.454  30.649  1.00 71.64           C  
+ANISOU 3906  CA  GLU B  95    10923  10944   5352  -1941   2115   2800       C  
+ATOM   3907  C   GLU B  95     -19.119   4.415  29.464  1.00 66.48           C  
+ANISOU 3907  C   GLU B  95     9921  10344   4995  -1704   2179   2513       C  
+ATOM   3908  O   GLU B  95     -20.101   5.009  29.006  1.00 65.04           O  
+ANISOU 3908  O   GLU B  95     9455  10295   4961  -1660   2464   2189       O  
+ATOM   3909  CB  GLU B  95     -19.112   4.240  31.957  1.00 74.64           C  
+ANISOU 3909  CB  GLU B  95    11489  11586   5284  -1995   2095   2706       C  
+ATOM   3910  CG  GLU B  95     -20.041   5.445  32.118  1.00 94.89           C  
+ANISOU 3910  CG  GLU B  95    13803  14469   7781  -1947   2447   2255       C  
+ATOM   3911  CD  GLU B  95     -21.510   5.071  32.229  1.00113.48           C  
+ANISOU 3911  CD  GLU B  95    16002  16921  10193  -2104   2822   2142       C  
+ATOM   3912  OE1 GLU B  95     -21.817   3.878  32.439  1.00123.38           O  
+ANISOU 3912  OE1 GLU B  95    17407  18043  11428  -2305   2823   2427       O  
+ATOM   3913  OE2 GLU B  95     -22.361   5.977  32.107  1.00107.01           O  
+ANISOU 3913  OE2 GLU B  95    14897  16302   9458  -2030   3094   1771       O  
+ATOM   3914  N   ASN B  96     -17.893   4.568  28.973  1.00 69.56           N  
+ANISOU 3914  N   ASN B  96    10288  10573   5568  -1491   1867   2601       N  
+ATOM   3915  CA  ASN B  96     -17.645   5.384  27.785  1.00 74.05           C  
+ANISOU 3915  CA  ASN B  96    10511  11089   6537  -1194   1874   2303       C  
+ATOM   3916  C   ASN B  96     -18.481   4.914  26.601  1.00 75.37           C  
+ANISOU 3916  C   ASN B  96    10476  11133   7026  -1200   2081   2214       C  
+ATOM   3917  O   ASN B  96     -19.105   5.719  25.908  1.00 76.48           O  
+ANISOU 3917  O   ASN B  96    10362  11389   7310  -1125   2257   1917       O  
+ATOM   3918  CB  ASN B  96     -16.161   5.375  27.413  1.00 58.49           C  
+ANISOU 3918  CB  ASN B  96     8512   8867   4846   -926   1503   2393       C  
+ATOM   3919  CG  ASN B  96     -15.294   6.068  28.448  1.00 76.14           C  
+ANISOU 3919  CG  ASN B  96    10885  11221   6825   -890   1247   2424       C  
+ATOM   3920  OD1 ASN B  96     -15.730   7.008  29.111  1.00 75.05           O  
+ANISOU 3920  OD1 ASN B  96    10778  11372   6365   -972   1374   2235       O  
+ATOM   3921  ND2 ASN B  96     -14.055   5.611  28.583  1.00 61.25           N  
+ANISOU 3921  ND2 ASN B  96     9067   9096   5108   -759    867   2640       N  
+ATOM   3922  N   HIS B  97     -18.490   3.602  26.389  1.00 59.09           N  
+ANISOU 3922  N   HIS B  97     8553   8812   5088  -1296   2016   2476       N  
+ATOM   3923  CA  HIS B  97     -19.261   2.987  25.316  1.00 71.38           C  
+ANISOU 3923  CA  HIS B  97     9975  10214   6933  -1336   2168   2420       C  
+ATOM   3924  C   HIS B  97     -20.742   3.298  25.451  1.00 73.91           C  
+ANISOU 3924  C   HIS B  97    10159  10805   7120  -1566   2514   2254       C  
+ATOM   3925  O   HIS B  97     -21.424   3.540  24.461  1.00 70.58           O  
+ANISOU 3925  O   HIS B  97     9499  10369   6951  -1520   2634   2040       O  
+ATOM   3926  CB  HIS B  97     -19.065   1.475  25.318  1.00 69.29           C  
+ANISOU 3926  CB  HIS B  97     9939   9613   6775  -1445   2020   2747       C  
+ATOM   3927  CG  HIS B  97     -17.659   1.045  25.050  1.00 67.33           C  
+ANISOU 3927  CG  HIS B  97     9758   9047   6778  -1185   1681   2870       C  
+ATOM   3928  ND1 HIS B  97     -16.850   0.500  26.025  1.00 76.51           N  
+ANISOU 3928  ND1 HIS B  97    11179  10076   7814  -1208   1385   3176       N  
+ATOM   3929  CD2 HIS B  97     -16.917   1.074  23.919  1.00 57.57           C  
+ANISOU 3929  CD2 HIS B  97     8348   7599   5926   -902   1594   2716       C  
+ATOM   3930  CE1 HIS B  97     -15.671   0.215  25.506  1.00 78.86           C  
+ANISOU 3930  CE1 HIS B  97    11408  10083   8471   -921   1119   3187       C  
+ATOM   3931  NE2 HIS B  97     -15.684   0.554  24.228  1.00 64.71           N  
+ANISOU 3931  NE2 HIS B  97     9351   8255   6980   -738   1276   2899       N  
+ATOM   3932  N   LYS B  98     -21.231   3.272  26.687  1.00 78.72           N  
+ANISOU 3932  N   LYS B  98    10897  11580   7434  -1722   2612   2294       N  
+ATOM   3933  CA  LYS B  98     -22.641   3.514  26.973  1.00 72.48           C  
+ANISOU 3933  CA  LYS B  98     9911  10979   6649  -1824   2893   2082       C  
+ATOM   3934  C   LYS B  98     -23.036   4.963  26.718  1.00 74.08           C  
+ANISOU 3934  C   LYS B  98     9819  11402   6925  -1647   3011   1684       C  
+ATOM   3935  O   LYS B  98     -24.072   5.229  26.101  1.00 78.39           O  
+ANISOU 3935  O   LYS B  98    10077  11996   7714  -1640   3157   1472       O  
+ATOM   3936  CB  LYS B  98     -22.959   3.126  28.419  1.00 68.75           C  
+ANISOU 3936  CB  LYS B  98     9664  10639   5819  -2034   2972   2227       C  
+ATOM   3937  CG  LYS B  98     -22.952   1.626  28.651  1.00 72.39           C  
+ANISOU 3937  CG  LYS B  98    10383  10864   6259  -2256   2876   2607       C  
+ATOM   3938  CD  LYS B  98     -22.185   1.245  29.907  1.00 75.39           C  
+ANISOU 3938  CD  LYS B  98    11159  11231   6253  -2369   2685   2889       C  
+ATOM   3939  CE  LYS B  98     -22.370  -0.230  30.233  1.00 90.52           C  
+ANISOU 3939  CE  LYS B  98    13332  12906   8154  -2618   2591   3255       C  
+ATOM   3940  NZ  LYS B  98     -21.510  -0.669  31.367  1.00 96.55           N  
+ANISOU 3940  NZ  LYS B  98    14514  13593   8578  -2717   2306   3569       N  
+ATOM   3941  N   ILE B  99     -22.216   5.897  27.195  1.00 66.23           N  
+ANISOU 3941  N   ILE B  99     8899  10531   5734  -1519   2913   1590       N  
+ATOM   3942  CA  ILE B  99     -22.450   7.314  26.934  1.00 64.14           C  
+ANISOU 3942  CA  ILE B  99     8386  10431   5555  -1343   2972   1218       C  
+ATOM   3943  C   ILE B  99     -22.425   7.590  25.433  1.00 60.26           C  
+ANISOU 3943  C   ILE B  99     7661   9801   5435  -1198   2902   1104       C  
+ATOM   3944  O   ILE B  99     -23.295   8.283  24.905  1.00 61.02           O  
+ANISOU 3944  O   ILE B  99     7483   9958   5743  -1133   2995    831       O  
+ATOM   3945  CB  ILE B  99     -21.412   8.207  27.638  1.00 65.98           C  
+ANISOU 3945  CB  ILE B  99     8766  10796   5509  -1248   2826   1168       C  
+ATOM   3946  CG1 ILE B  99     -21.537   8.073  29.156  1.00 63.53           C  
+ANISOU 3946  CG1 ILE B  99     8710  10647   4782  -1407   2897   1232       C  
+ATOM   3947  CG2 ILE B  99     -21.598   9.662  27.234  1.00 57.14           C  
+ANISOU 3947  CG2 ILE B  99     7387   9801   4522  -1062   2850    785       C  
+ATOM   3948  CD1 ILE B  99     -20.399   8.712  29.918  1.00 65.61           C  
+ANISOU 3948  CD1 ILE B  99     9199  11013   4718  -1364   2682   1259       C  
+ATOM   3949  N   LEU B 100     -21.428   7.034  24.753  1.00 58.54           N  
+ANISOU 3949  N   LEU B 100     7549   9398   5295  -1153   2721   1321       N  
+ATOM   3950  CA  LEU B 100     -21.309   7.188  23.306  1.00 64.19           C  
+ANISOU 3950  CA  LEU B 100     8110   9898   6381   -983   2608   1218       C  
+ATOM   3951  C   LEU B 100     -22.525   6.618  22.581  1.00 58.11           C  
+ANISOU 3951  C   LEU B 100     7198   9070   5810  -1123   2754   1169       C  
+ATOM   3952  O   LEU B 100     -22.997   7.190  21.600  1.00 73.72           O  
+ANISOU 3952  O   LEU B 100     8983  10999   8029  -1034   2721    965       O  
+ATOM   3953  CB  LEU B 100     -20.035   6.511  22.797  1.00 65.16           C  
+ANISOU 3953  CB  LEU B 100     8386   9742   6631   -856   2382   1428       C  
+ATOM   3954  CG  LEU B 100     -18.714   7.217  23.108  1.00 62.59           C  
+ANISOU 3954  CG  LEU B 100     8104   9420   6258   -670   2176   1432       C  
+ATOM   3955  CD1 LEU B 100     -17.528   6.324  22.772  1.00 53.60           C  
+ANISOU 3955  CD1 LEU B 100     7072   8010   5282   -566   1988   1645       C  
+ATOM   3956  CD2 LEU B 100     -18.625   8.538  22.362  1.00 45.40           C  
+ANISOU 3956  CD2 LEU B 100     5739   7288   4224   -513   2134   1165       C  
+ATOM   3957  N   ALA B 101     -23.023   5.488  23.071  1.00 53.21           N  
+ANISOU 3957  N   ALA B 101     6689   8422   5104  -1348   2865   1373       N  
+ATOM   3958  CA  ALA B 101     -24.183   4.834  22.479  1.00 53.84           C  
+ANISOU 3958  CA  ALA B 101     6632   8424   5401  -1497   2961   1353       C  
+ATOM   3959  C   ALA B 101     -25.446   5.654  22.704  1.00 77.48           C  
+ANISOU 3959  C   ALA B 101     9319  11642   8479  -1508   3115   1072       C  
+ATOM   3960  O   ALA B 101     -26.369   5.617  21.896  1.00 72.66           O  
+ANISOU 3960  O   ALA B 101     8487  10996   8125  -1575   3151    943       O  
+ATOM   3961  CB  ALA B 101     -24.349   3.431  23.047  1.00 61.07           C  
+ANISOU 3961  CB  ALA B 101     7752   9221   6231  -1718   2986   1658       C  
+ATOM   3962  N   ARG B 102     -25.481   6.400  23.804  1.00 62.81           N  
+ANISOU 3962  N   ARG B 102     7451  10001   6412  -1456   3205    958       N  
+ATOM   3963  CA  ARG B 102     -26.619   7.270  24.089  1.00 69.19           C  
+ANISOU 3963  CA  ARG B 102     7955  11017   7315  -1440   3368    648       C  
+ATOM   3964  C   ARG B 102     -26.556   8.589  23.333  1.00 77.89           C  
+ANISOU 3964  C   ARG B 102     8839  12143   8612  -1228   3269    339       C  
+ATOM   3965  O   ARG B 102     -27.558   9.296  23.230  1.00 84.18           O  
+ANISOU 3965  O   ARG B 102     9323  13050   9613  -1194   3355     51       O  
+ATOM   3966  CB  ARG B 102     -26.726   7.531  25.589  1.00 64.14           C  
+ANISOU 3966  CB  ARG B 102     7418  10594   6357  -1490   3531    614       C  
+ATOM   3967  CG  ARG B 102     -27.151   6.301  26.358  1.00 69.15           C  
+ANISOU 3967  CG  ARG B 102     8209  11241   6824  -1752   3669    877       C  
+ATOM   3968  CD  ARG B 102     -27.351   6.582  27.833  1.00 70.13           C  
+ANISOU 3968  CD  ARG B 102     8448  11604   6596  -1841   3858    823       C  
+ATOM   3969  NE  ARG B 102     -26.067   6.671  28.513  1.00 75.88           N  
+ANISOU 3969  NE  ARG B 102     9536  12315   6980  -1791   3699    979       N  
+ATOM   3970  CZ  ARG B 102     -25.807   7.458  29.551  1.00 81.95           C  
+ANISOU 3970  CZ  ARG B 102    10422  13280   7436  -1759   3756    835       C  
+ATOM   3971  NH1 ARG B 102     -26.749   8.242  30.057  1.00104.98           N  
+ANISOU 3971  NH1 ARG B 102    13124  16422  10342  -1756   4000    510       N  
+ATOM   3972  NH2 ARG B 102     -24.595   7.451  30.087  1.00 78.42           N  
+ANISOU 3972  NH2 ARG B 102    10307  12799   6690  -1739   3558   1008       N  
+ATOM   3973  N   LEU B 103     -25.378   8.930  22.825  1.00 52.87           N  
+ANISOU 3973  N   LEU B 103     5820   8870   5398  -1092   3083    394       N  
+ATOM   3974  CA  LEU B 103     -25.225  10.143  22.032  1.00 62.14           C  
+ANISOU 3974  CA  LEU B 103     6831  10015   6763   -896   2930    146       C  
+ATOM   3975  C   LEU B 103     -25.704   9.895  20.605  1.00 62.82           C  
+ANISOU 3975  C   LEU B 103     6812   9864   7193   -884   2768    139       C  
+ATOM   3976  O   LEU B 103     -25.587   8.780  20.097  1.00 59.21           O  
+ANISOU 3976  O   LEU B 103     6492   9245   6760   -998   2749    357       O  
+ATOM   3977  CB  LEU B 103     -23.767  10.614  22.028  1.00 48.28           C  
+ANISOU 3977  CB  LEU B 103     5299   8167   4878   -725   2709    241       C  
+ATOM   3978  CG  LEU B 103     -23.180  11.114  23.349  1.00 60.39           C  
+ANISOU 3978  CG  LEU B 103     6955   9904   6084   -704   2763    212       C  
+ATOM   3979  CD1 LEU B 103     -21.731  11.541  23.164  1.00 54.60           C  
+ANISOU 3979  CD1 LEU B 103     6391   9039   5316   -543   2494    315       C  
+ATOM   3980  CD2 LEU B 103     -24.014  12.256  23.902  1.00 58.35           C  
+ANISOU 3980  CD2 LEU B 103     6476   9856   5839   -646   2889   -158       C  
+ATOM   3981  N   PRO B 104     -26.250  10.934  19.952  1.00 62.57           N  
+ANISOU 3981  N   PRO B 104     6560   9786   7426   -748   2617   -115       N  
+ATOM   3982  CA  PRO B 104     -26.711  10.812  18.563  1.00 57.72           C  
+ANISOU 3982  CA  PRO B 104     5888   8937   7108   -749   2397   -123       C  
+ATOM   3983  C   PRO B 104     -25.553  10.789  17.566  1.00 60.80           C  
+ANISOU 3983  C   PRO B 104     6561   9094   7447   -669   2162     37       C  
+ATOM   3984  O   PRO B 104     -25.567  11.532  16.585  1.00 69.77           O  
+ANISOU 3984  O   PRO B 104     7694  10077   8739   -584   1911    -51       O  
+ATOM   3985  CB  PRO B 104     -27.574  12.061  18.372  1.00 51.22           C  
+ANISOU 3985  CB  PRO B 104     4759   8134   6570   -616   2265   -441       C  
+ATOM   3986  CG  PRO B 104     -26.992  13.054  19.309  1.00 60.44           C  
+ANISOU 3986  CG  PRO B 104     5942   9453   7570   -467   2314   -578       C  
+ATOM   3987  CD  PRO B 104     -26.535  12.268  20.510  1.00 64.65           C  
+ANISOU 3987  CD  PRO B 104     6630  10197   7738   -596   2618   -421       C  
+ATOM   3988  N   ILE B 105     -24.569   9.934  17.824  1.00 51.77           N  
+ANISOU 3988  N   ILE B 105     5658   7919   6094   -707   2245    265       N  
+ATOM   3989  CA  ILE B 105     -23.419   9.776  16.943  1.00 47.43           C  
+ANISOU 3989  CA  ILE B 105     5337   7174   5510   -639   2100    391       C  
+ATOM   3990  C   ILE B 105     -23.660   8.647  15.944  1.00 41.85           C  
+ANISOU 3990  C   ILE B 105     4746   6261   4894   -756   2079    490       C  
+ATOM   3991  O   ILE B 105     -23.988   7.526  16.331  1.00 57.82           O  
+ANISOU 3991  O   ILE B 105     6801   8271   6899   -884   2211    610       O  
+ATOM   3992  CB  ILE B 105     -22.137   9.490  17.751  1.00 53.45           C  
+ANISOU 3992  CB  ILE B 105     6255   7986   6067   -579   2164    551       C  
+ATOM   3993  CG1 ILE B 105     -21.800  10.680  18.653  1.00 62.02           C  
+ANISOU 3993  CG1 ILE B 105     7268   9250   7044   -470   2136    435       C  
+ATOM   3994  CG2 ILE B 105     -20.979   9.149  16.824  1.00 45.55           C  
+ANISOU 3994  CG2 ILE B 105     5428   6789   5089   -518   2074    654       C  
+ATOM   3995  CD1 ILE B 105     -20.638  10.430  19.590  1.00 71.41           C  
+ANISOU 3995  CD1 ILE B 105     8600  10502   8033   -430   2151    592       C  
+ATOM   3996  N   HIS B 106     -23.493   8.948  14.660  1.00 43.58           N  
+ANISOU 3996  N   HIS B 106     5061   6309   5189   -735   1901    442       N  
+ATOM   3997  CA  HIS B 106     -23.816   7.992  13.607  1.00 44.15           C  
+ANISOU 3997  CA  HIS B 106     5269   6177   5330   -855   1853    481       C  
+ATOM   3998  C   HIS B 106     -22.587   7.414  12.910  1.00 49.53           C  
+ANISOU 3998  C   HIS B 106     6209   6702   5910   -818   1881    564       C  
+ATOM   3999  O   HIS B 106     -22.718   6.567  12.028  1.00 58.67           O  
+ANISOU 3999  O   HIS B 106     7523   7675   7094   -908   1861    569       O  
+ATOM   4000  CB  HIS B 106     -24.714   8.648  12.555  1.00 43.20           C  
+ANISOU 4000  CB  HIS B 106     5101   5960   5354   -904   1611    346       C  
+ATOM   4001  CG  HIS B 106     -25.890   9.376  13.125  1.00 46.76           C  
+ANISOU 4001  CG  HIS B 106     5234   6543   5991   -893   1556    206       C  
+ATOM   4002  ND1 HIS B 106     -26.931   8.733  13.760  1.00 55.07           N  
+ANISOU 4002  ND1 HIS B 106     6067   7686   7172  -1006   1695    187       N  
+ATOM   4003  CD2 HIS B 106     -26.195  10.696  13.149  1.00 55.67           C  
+ANISOU 4003  CD2 HIS B 106     6207   7715   7232   -783   1384     56       C  
+ATOM   4004  CE1 HIS B 106     -27.823   9.624  14.153  1.00 59.81           C  
+ANISOU 4004  CE1 HIS B 106     6355   8405   7962   -953   1646      3       C  
+ATOM   4005  NE2 HIS B 106     -27.400  10.823  13.794  1.00 66.99           N  
+ANISOU 4005  NE2 HIS B 106     7302   9270   8879   -800   1437    -85       N  
+ATOM   4006  N   THR B 107     -21.395   7.856  13.301  1.00 52.12           N  
+ANISOU 4006  N   THR B 107     6565   7097   6141   -690   1930    604       N  
+ATOM   4007  CA  THR B 107     -20.188   7.363  12.647  1.00 42.00           C  
+ANISOU 4007  CA  THR B 107     5457   5685   4816   -641   1990    640       C  
+ATOM   4008  C   THR B 107     -19.104   6.901  13.616  1.00 49.10           C  
+ANISOU 4008  C   THR B 107     6333   6622   5701   -523   2095    759       C  
+ATOM   4009  O   THR B 107     -18.550   7.688  14.391  1.00 59.48           O  
+ANISOU 4009  O   THR B 107     7551   8083   6967   -435   2071    781       O  
+ATOM   4010  CB  THR B 107     -19.590   8.437  11.720  1.00 41.83           C  
+ANISOU 4010  CB  THR B 107     5504   5659   4732   -627   1907    557       C  
+ATOM   4011  OG1 THR B 107     -20.568   8.823  10.746  1.00 39.02           O  
+ANISOU 4011  OG1 THR B 107     5221   5223   4381   -749   1740    474       O  
+ATOM   4012  CG2 THR B 107     -18.356   7.901  11.011  1.00 38.67           C  
+ANISOU 4012  CG2 THR B 107     5243   5156   4295   -597   2041    552       C  
+ATOM   4013  N   TYR B 108     -18.800   5.610  13.538  1.00 44.77           N  
+ANISOU 4013  N   TYR B 108     5887   5907   5215   -522   2169    831       N  
+ATOM   4014  CA  TYR B 108     -17.733   4.998  14.312  1.00 43.32           C  
+ANISOU 4014  CA  TYR B 108     5700   5681   5077   -400   2204    954       C  
+ATOM   4015  C   TYR B 108     -16.720   4.356  13.378  1.00 52.73           C  
+ANISOU 4015  C   TYR B 108     6973   6675   6387   -309   2275    880       C  
+ATOM   4016  O   TYR B 108     -17.076   3.542  12.536  1.00 52.96           O  
+ANISOU 4016  O   TYR B 108     7137   6520   6465   -371   2318    808       O  
+ATOM   4017  CB  TYR B 108     -18.284   3.940  15.269  1.00 46.77           C  
+ANISOU 4017  CB  TYR B 108     6183   6062   5525   -473   2202   1125       C  
+ATOM   4018  CG  TYR B 108     -19.126   4.486  16.394  1.00 57.33           C  
+ANISOU 4018  CG  TYR B 108     7428   7633   6722   -569   2203   1188       C  
+ATOM   4019  CD1 TYR B 108     -20.485   4.708  16.221  1.00 42.86           C  
+ANISOU 4019  CD1 TYR B 108     5522   5882   4879   -721   2238   1108       C  
+ATOM   4020  CD2 TYR B 108     -18.566   4.772  17.631  1.00 52.87           C  
+ANISOU 4020  CD2 TYR B 108     6840   7208   6040   -514   2172   1304       C  
+ATOM   4021  CE1 TYR B 108     -21.262   5.201  17.247  1.00 58.69           C  
+ANISOU 4021  CE1 TYR B 108     7404   8119   6777   -804   2297   1112       C  
+ATOM   4022  CE2 TYR B 108     -19.335   5.267  18.664  1.00 50.73           C  
+ANISOU 4022  CE2 TYR B 108     6509   7171   5595   -616   2220   1319       C  
+ATOM   4023  CZ  TYR B 108     -20.683   5.480  18.466  1.00 52.95           C  
+ANISOU 4023  CZ  TYR B 108     6688   7546   5884   -756   2311   1207       C  
+ATOM   4024  OH  TYR B 108     -21.456   5.973  19.491  1.00 55.99           O  
+ANISOU 4024  OH  TYR B 108     6974   8182   6118   -854   2415   1170       O  
+ATOM   4025  N   TRP B 109     -15.464   4.753  13.519  1.00 59.13           N  
+ANISOU 4025  N   TRP B 109     7686   7528   7252   -168   2294    870       N  
+ATOM   4026  CA  TRP B 109     -14.339   4.079  12.894  1.00 52.65           C  
+ANISOU 4026  CA  TRP B 109     6862   6538   6603    -45   2397    785       C  
+ATOM   4027  C   TRP B 109     -13.519   3.416  14.002  1.00 55.06           C  
+ANISOU 4027  C   TRP B 109     7074   6761   7086    115   2300    938       C  
+ATOM   4028  O   TRP B 109     -13.377   3.977  15.089  1.00 63.70           O  
+ANISOU 4028  O   TRP B 109     8085   8005   8112    135   2172   1077       O  
+ATOM   4029  CB  TRP B 109     -13.486   5.074  12.101  1.00 53.80           C  
+ANISOU 4029  CB  TRP B 109     6925   6798   6719    -34   2501    642       C  
+ATOM   4030  CG  TRP B 109     -14.104   5.539  10.810  1.00 54.89           C  
+ANISOU 4030  CG  TRP B 109     7225   6948   6680   -204   2573    500       C  
+ATOM   4031  CD1 TRP B 109     -15.006   6.551  10.652  1.00 51.32           C  
+ANISOU 4031  CD1 TRP B 109     6826   6617   6054   -343   2454    514       C  
+ATOM   4032  CD2 TRP B 109     -13.837   5.033   9.494  1.00 46.99           C  
+ANISOU 4032  CD2 TRP B 109     6376   5822   5655   -258   2753    316       C  
+ATOM   4033  NE1 TRP B 109     -15.332   6.693   9.325  1.00 55.13           N  
+ANISOU 4033  NE1 TRP B 109     7504   7042   6401   -492   2499    390       N  
+ATOM   4034  CE2 TRP B 109     -14.625   5.776   8.593  1.00 45.87           C  
+ANISOU 4034  CE2 TRP B 109     6414   5735   5279   -460   2702    263       C  
+ATOM   4035  CE3 TRP B 109     -13.010   4.023   8.992  1.00 49.62           C  
+ANISOU 4035  CE3 TRP B 109     6715   5991   6147   -152   2945    170       C  
+ATOM   4036  CZ2 TRP B 109     -14.619   5.536   7.220  1.00 52.22           C  
+ANISOU 4036  CZ2 TRP B 109     7454   6454   5935   -594   2834     92       C  
+ATOM   4037  CZ3 TRP B 109     -13.006   3.785   7.628  1.00 63.94           C  
+ANISOU 4037  CZ3 TRP B 109     8734   7731   7828   -267   3128    -44       C  
+ATOM   4038  CH2 TRP B 109     -13.804   4.540   6.758  1.00 67.90           C  
+ANISOU 4038  CH2 TRP B 109     9461   8309   8027   -504   3071    -70       C  
+ATOM   4039  N   THR B 110     -12.990   2.225  13.750  1.00 51.32           N  
+ANISOU 4039  N   THR B 110     6632   6026   6840    228   2327    909       N  
+ATOM   4040  CA  THR B 110     -12.149   1.576  14.752  1.00 58.28           C  
+ANISOU 4040  CA  THR B 110     7430   6774   7939    396   2164   1066       C  
+ATOM   4041  C   THR B 110     -11.187   0.561  14.138  1.00 67.03           C  
+ANISOU 4041  C   THR B 110     8477   7591   9400    593   2226    920       C  
+ATOM   4042  O   THR B 110     -11.454   0.002  13.075  1.00 67.66           O  
+ANISOU 4042  O   THR B 110     8669   7523   9517    568   2392    725       O  
+ATOM   4043  CB  THR B 110     -12.996   0.880  15.837  1.00 58.85           C  
+ANISOU 4043  CB  THR B 110     7669   6772   7920    292   1986   1329       C  
+ATOM   4044  OG1 THR B 110     -12.134   0.316  16.833  1.00 65.00           O  
+ANISOU 4044  OG1 THR B 110     8411   7405   8880    436   1761   1518       O  
+ATOM   4045  CG2 THR B 110     -13.868  -0.209  15.230  1.00 60.06           C  
+ANISOU 4045  CG2 THR B 110     8018   6686   8114    187   2039   1298       C  
+ATOM   4046  N   THR B 111     -10.068   0.329  14.818  1.00 74.03           N  
+ANISOU 4046  N   THR B 111     9182   8386  10561    796   2074    995       N  
+ATOM   4047  CA  THR B 111      -9.128  -0.713  14.417  1.00 78.11           C  
+ANISOU 4047  CA  THR B 111     9588   8585  11505   1031   2087    851       C  
+ATOM   4048  C   THR B 111      -9.186  -1.885  15.384  1.00 81.71           C  
+ANISOU 4048  C   THR B 111    10171   8721  12156   1114   1763   1101       C  
+ATOM   4049  O   THR B 111      -8.373  -2.805  15.312  1.00 91.45           O  
+ANISOU 4049  O   THR B 111    11302   9630  13813   1348   1666   1028       O  
+ATOM   4050  CB  THR B 111      -7.677  -0.193  14.356  1.00 76.55           C  
+ANISOU 4050  CB  THR B 111     9023   8464  11598   1230   2130    717       C  
+ATOM   4051  OG1 THR B 111      -7.346   0.452  15.592  1.00 78.08           O  
+ANISOU 4051  OG1 THR B 111     9117   8805  11743   1237   1844    972       O  
+ATOM   4052  CG2 THR B 111      -7.509   0.794  13.218  1.00 69.56           C  
+ANISOU 4052  CG2 THR B 111     8040   7838  10550   1124   2486    455       C  
+ATOM   4053  N   ASN B 112     -10.154  -1.843  16.292  1.00 79.59           N  
+ANISOU 4053  N   ASN B 112    10122   8533  11584    911   1596   1392       N  
+ATOM   4054  CA  ASN B 112     -10.345  -2.919  17.251  1.00 80.35           C  
+ANISOU 4054  CA  ASN B 112    10414   8341  11775    901   1285   1687       C  
+ATOM   4055  C   ASN B 112     -11.072  -4.113  16.641  1.00 84.01           C  
+ANISOU 4055  C   ASN B 112    11106   8477  12338    834   1330   1640       C  
+ATOM   4056  O   ASN B 112     -11.862  -3.965  15.708  1.00 80.01           O  
+ANISOU 4056  O   ASN B 112    10676   8056  11668    695   1582   1450       O  
+ATOM   4057  CB  ASN B 112     -11.119  -2.415  18.471  1.00 76.45           C  
+ANISOU 4057  CB  ASN B 112    10086   8094  10869    659   1144   2004       C  
+ATOM   4058  CG  ASN B 112     -10.406  -1.289  19.190  1.00 76.31           C  
+ANISOU 4058  CG  ASN B 112     9890   8362  10744    717   1042   2057       C  
+ATOM   4059  OD1 ASN B 112      -9.197  -1.110  19.043  1.00 79.92           O  
+ANISOU 4059  OD1 ASN B 112    10096   8761  11509    950    966   1950       O  
+ATOM   4060  ND2 ASN B 112     -11.153  -0.522  19.977  1.00 71.72           N  
+ANISOU 4060  ND2 ASN B 112     9420   8086   9743    501   1044   2198       N  
+ATOM   4061  N   TYR B 113     -10.797  -5.296  17.179  1.00 90.88           N  
+ANISOU 4061  N   TYR B 113    12099   8942  13488    926   1038   1823       N  
+ATOM   4062  CA  TYR B 113     -11.472  -6.522  16.765  1.00 98.06           C  
+ANISOU 4062  CA  TYR B 113    13260   9477  14522    846   1006   1824       C  
+ATOM   4063  C   TYR B 113     -12.687  -6.814  17.628  1.00101.15           C  
+ANISOU 4063  C   TYR B 113    13949   9900  14582    494    880   2190       C  
+ATOM   4064  O   TYR B 113     -13.626  -7.472  17.181  1.00103.73           O  
+ANISOU 4064  O   TYR B 113    14473  10068  14872    305    946   2178       O  
+ATOM   4065  CB  TYR B 113     -10.509  -7.712  16.787  1.00107.29           C  
+ANISOU 4065  CB  TYR B 113    14407  10118  16240   1144    740   1798       C  
+ATOM   4066  CG  TYR B 113      -9.376  -7.595  15.798  1.00113.45           C  
+ANISOU 4066  CG  TYR B 113    14863  10839  17404   1485    940   1363       C  
+ATOM   4067  CD1 TYR B 113      -9.562  -7.988  14.482  1.00116.96           C  
+ANISOU 4067  CD1 TYR B 113    15338  11156  17946   1527   1242    971       C  
+ATOM   4068  CD2 TYR B 113      -8.141  -7.072  16.158  1.00120.61           C  
+ANISOU 4068  CD2 TYR B 113    15431  11837  18558   1736    850   1326       C  
+ATOM   4069  CE1 TYR B 113      -8.552  -7.896  13.560  1.00125.96           C  
+ANISOU 4069  CE1 TYR B 113    16194  12272  19395   1802   1493    544       C  
+ATOM   4070  CE2 TYR B 113      -7.116  -6.966  15.230  1.00127.73           C  
+ANISOU 4070  CE2 TYR B 113    15993  12713  19825   2018   1095    904       C  
+ATOM   4071  CZ  TYR B 113      -7.332  -7.380  13.930  1.00131.28           C  
+ANISOU 4071  CZ  TYR B 113    16492  13053  20335   2044   1444    508       C  
+ATOM   4072  OH  TYR B 113      -6.330  -7.285  12.991  1.00137.94           O  
+ANISOU 4072  OH  TYR B 113    17011  13901  21498   2290   1753     60       O  
+ATOM   4073  N   ASP B 114     -12.662  -6.330  18.866  1.00 95.12           N  
+ANISOU 4073  N   ASP B 114    13221   9349  13573    385    707   2503       N  
+ATOM   4074  CA  ASP B 114     -13.772  -6.547  19.783  1.00 85.74           C  
+ANISOU 4074  CA  ASP B 114    12304   8247  12025     17    642   2847       C  
+ATOM   4075  C   ASP B 114     -15.050  -5.931  19.224  1.00 73.08           C  
+ANISOU 4075  C   ASP B 114    10681   6975  10112   -241    990   2696       C  
+ATOM   4076  O   ASP B 114     -15.005  -5.075  18.340  1.00 70.83           O  
+ANISOU 4076  O   ASP B 114    10192   6917   9803   -142   1230   2382       O  
+ATOM   4077  CB  ASP B 114     -13.449  -5.968  21.163  1.00 82.79           C  
+ANISOU 4077  CB  ASP B 114    11975   8106  11374    -55    444   3146       C  
+ATOM   4078  CG  ASP B 114     -13.265  -4.461  21.140  1.00 74.23           C  
+ANISOU 4078  CG  ASP B 114    10642   7508  10054      0    651   2953       C  
+ATOM   4079  OD1 ASP B 114     -14.268  -3.733  20.982  1.00 71.13           O  
+ANISOU 4079  OD1 ASP B 114    10227   7457   9344   -209    931   2859       O  
+ATOM   4080  OD2 ASP B 114     -12.112  -4.003  21.277  1.00 76.15           O  
+ANISOU 4080  OD2 ASP B 114    10696   7770  10468    253    510   2892       O  
+ATOM   4081  N   ARG B 115     -16.189  -6.364  19.749  1.00 74.72           N  
+ANISOU 4081  N   ARG B 115    11095   7199  10096   -588   1001   2930       N  
+ATOM   4082  CA  ARG B 115     -17.474  -5.891  19.256  1.00 70.84           C  
+ANISOU 4082  CA  ARG B 115    10548   6979   9387   -838   1288   2792       C  
+ATOM   4083  C   ARG B 115     -18.162  -4.983  20.267  1.00 68.62           C  
+ANISOU 4083  C   ARG B 115    10229   7155   8690  -1076   1415   2934       C  
+ATOM   4084  O   ARG B 115     -19.387  -4.938  20.334  1.00 81.14           O  
+ANISOU 4084  O   ARG B 115    11816   8909  10106  -1373   1589   2955       O  
+ATOM   4085  CB  ARG B 115     -18.374  -7.080  18.910  1.00 80.25           C  
+ANISOU 4085  CB  ARG B 115    11938   7849  10703  -1076   1258   2878       C  
+ATOM   4086  CG  ARG B 115     -17.818  -7.962  17.803  1.00 80.05           C  
+ANISOU 4086  CG  ARG B 115    11967   7367  11081   -846   1166   2660       C  
+ATOM   4087  CD  ARG B 115     -18.875  -8.885  17.211  1.00 80.32           C  
+ANISOU 4087  CD  ARG B 115    12166   7141  11210  -1101   1176   2647       C  
+ATOM   4088  NE  ARG B 115     -19.908  -9.254  18.176  1.00 97.73           N  
+ANISOU 4088  NE  ARG B 115    14514   9410  13210  -1514   1148   3005       N  
+ATOM   4089  CZ  ARG B 115     -21.177  -8.864  18.097  1.00103.85           C  
+ANISOU 4089  CZ  ARG B 115    15199  10473  13788  -1830   1353   2983       C  
+ATOM   4090  NH1 ARG B 115     -21.572  -8.098  17.091  1.00100.78           N  
+ANISOU 4090  NH1 ARG B 115    14608  10297  13385  -1766   1536   2644       N  
+ATOM   4091  NH2 ARG B 115     -22.050  -9.247  19.019  1.00104.24           N  
+ANISOU 4091  NH2 ARG B 115    15355  10589  13664  -2224   1368   3303       N  
+ATOM   4092  N   LEU B 116     -17.366  -4.263  21.051  1.00 63.76           N  
+ANISOU 4092  N   LEU B 116     9560   6735   7930   -945   1327   3002       N  
+ATOM   4093  CA  LEU B 116     -17.893  -3.423  22.123  1.00 68.37           C  
+ANISOU 4093  CA  LEU B 116    10146   7735   8097  -1153   1434   3113       C  
+ATOM   4094  C   LEU B 116     -18.780  -2.282  21.624  1.00 62.65           C  
+ANISOU 4094  C   LEU B 116     9181   7393   7232  -1214   1742   2823       C  
+ATOM   4095  O   LEU B 116     -19.798  -1.976  22.241  1.00 73.89           O  
+ANISOU 4095  O   LEU B 116    10597   9090   8387  -1482   1920   2869       O  
+ATOM   4096  CB  LEU B 116     -16.748  -2.860  22.966  1.00 63.85           C  
+ANISOU 4096  CB  LEU B 116     9578   7256   7424   -972   1228   3208       C  
+ATOM   4097  CG  LEU B 116     -15.978  -3.910  23.768  1.00 68.58           C  
+ANISOU 4097  CG  LEU B 116    10443   7505   8110   -960    850   3562       C  
+ATOM   4098  CD1 LEU B 116     -14.918  -3.259  24.641  1.00 68.71           C  
+ANISOU 4098  CD1 LEU B 116    10454   7642   8009   -808    608   3652       C  
+ATOM   4099  CD2 LEU B 116     -16.934  -4.744  24.609  1.00 71.69           C  
+ANISOU 4099  CD2 LEU B 116    11155   7850   8233  -1369    843   3903       C  
+ATOM   4100  N   ILE B 117     -18.387  -1.642  20.527  1.00 61.97           N  
+ANISOU 4100  N   ILE B 117     8895   7320   7331   -974   1799   2523       N  
+ATOM   4101  CA  ILE B 117     -19.162  -0.529  19.984  1.00 58.38           C  
+ANISOU 4101  CA  ILE B 117     8230   7167   6783  -1009   2010   2260       C  
+ATOM   4102  C   ILE B 117     -20.560  -0.973  19.553  1.00 71.56           C  
+ANISOU 4102  C   ILE B 117     9888   8824   8478  -1267   2149   2224       C  
+ATOM   4103  O   ILE B 117     -21.565  -0.402  19.987  1.00 67.67           O  
+ANISOU 4103  O   ILE B 117     9276   8618   7819  -1451   2309   2182       O  
+ATOM   4104  CB  ILE B 117     -18.449   0.126  18.785  1.00 55.06           C  
+ANISOU 4104  CB  ILE B 117     7664   6712   6545   -750   2016   1985       C  
+ATOM   4105  CG1 ILE B 117     -17.151   0.795  19.240  1.00 52.41           C  
+ANISOU 4105  CG1 ILE B 117     7261   6456   6197   -526   1904   1992       C  
+ATOM   4106  CG2 ILE B 117     -19.359   1.143  18.110  1.00 53.98           C  
+ANISOU 4106  CG2 ILE B 117     7363   6803   6344   -814   2161   1748       C  
+ATOM   4107  CD1 ILE B 117     -16.279   1.273  18.100  1.00 48.94           C  
+ANISOU 4107  CD1 ILE B 117     6688   5956   5952   -305   1930   1758       C  
+ATOM   4108  N   GLU B 118     -20.619  -1.991  18.700  1.00 87.19           N  
+ANISOU 4108  N   GLU B 118    11971  10463  10693  -1276   2085   2217       N  
+ATOM   4109  CA  GLU B 118     -21.894  -2.510  18.214  1.00 76.22           C  
+ANISOU 4109  CA  GLU B 118    10576   9011   9375  -1531   2164   2187       C  
+ATOM   4110  C   GLU B 118     -22.730  -3.088  19.355  1.00 70.25           C  
+ANISOU 4110  C   GLU B 118     9898   8330   8463  -1869   2228   2460       C  
+ATOM   4111  O   GLU B 118     -23.958  -2.985  19.351  1.00 81.40           O  
+ANISOU 4111  O   GLU B 118    11173   9903   9852  -2120   2379   2414       O  
+ATOM   4112  CB  GLU B 118     -21.667  -3.568  17.130  1.00 72.00           C  
+ANISOU 4112  CB  GLU B 118    10192   8054   9111  -1473   2049   2120       C  
+ATOM   4113  CG  GLU B 118     -20.538  -4.541  17.423  1.00 82.84           C  
+ANISOU 4113  CG  GLU B 118    11767   9078  10629  -1314   1870   2283       C  
+ATOM   4114  CD  GLU B 118     -19.234  -4.142  16.757  1.00 78.92           C  
+ANISOU 4114  CD  GLU B 118    11205   8514  10267   -951   1838   2073       C  
+ATOM   4115  OE1 GLU B 118     -18.715  -3.048  17.066  1.00 62.92           O  
+ANISOU 4115  OE1 GLU B 118     9024   6776   8106   -819   1887   2018       O  
+ATOM   4116  OE2 GLU B 118     -18.724  -4.925  15.929  1.00 74.81           O  
+ANISOU 4116  OE2 GLU B 118    10780   7650   9995   -811   1777   1947       O  
+ATOM   4117  N   LYS B 119     -22.054  -3.687  20.332  1.00 71.43           N  
+ANISOU 4117  N   LYS B 119    10264   8365   8513  -1889   2106   2748       N  
+ATOM   4118  CA  LYS B 119     -22.716  -4.242  21.510  1.00 73.02           C  
+ANISOU 4118  CA  LYS B 119    10613   8643   8489  -2252   2165   3057       C  
+ATOM   4119  C   LYS B 119     -23.408  -3.142  22.307  1.00 78.46           C  
+ANISOU 4119  C   LYS B 119    11113   9837   8860  -2397   2430   2974       C  
+ATOM   4120  O   LYS B 119     -24.582  -3.260  22.665  1.00 81.56           O  
+ANISOU 4120  O   LYS B 119    11374  10408   9206  -2641   2605   2967       O  
+ATOM   4121  CB  LYS B 119     -21.700  -4.967  22.396  1.00 68.51           C  
+ANISOU 4121  CB  LYS B 119    10352   7835   7846  -2216   1907   3392       C  
+ATOM   4122  CG  LYS B 119     -21.580  -6.461  22.139  1.00 71.67           C  
+ANISOU 4122  CG  LYS B 119    11012   7716   8505  -2299   1676   3612       C  
+ATOM   4123  CD  LYS B 119     -20.815  -7.147  23.262  1.00 75.44           C  
+ANISOU 4123  CD  LYS B 119    11817   7982   8866  -2350   1390   4011       C  
+ATOM   4124  CE  LYS B 119     -20.298  -8.511  22.829  1.00 78.22           C  
+ANISOU 4124  CE  LYS B 119    12397   7721   9602  -2261   1063   4156       C  
+ATOM   4125  NZ  LYS B 119     -19.451  -9.149  23.876  1.00100.22           N  
+ANISOU 4125  NZ  LYS B 119    15500  10242  12337  -2264    692   4551       N  
+ATOM   4126  N   ALA B 120     -22.663  -2.074  22.577  1.00 77.33           N  
+ANISOU 4126  N   ALA B 120    10888   9912   8582  -2145   2414   2844       N  
+ATOM   4127  CA  ALA B 120     -23.178  -0.923  23.308  1.00 73.61           C  
+ANISOU 4127  CA  ALA B 120    10233   9891   7844  -2193   2631   2693       C  
+ATOM   4128  C   ALA B 120     -24.337  -0.281  22.558  1.00 73.55           C  
+ANISOU 4128  C   ALA B 120     9872  10060   8016  -2201   2812   2374       C  
+ATOM   4129  O   ALA B 120     -25.338   0.106  23.161  1.00 70.75           O  
+ANISOU 4129  O   ALA B 120     9319   9968   7594  -2293   2982   2263       O  
+ATOM   4130  CB  ALA B 120     -22.072   0.092  23.545  1.00 60.68           C  
+ANISOU 4130  CB  ALA B 120     8587   8379   6089  -1908   2524   2595       C  
+ATOM   4131  N   LEU B 121     -24.188  -0.160  21.242  1.00 68.98           N  
+ANISOU 4131  N   LEU B 121     9212   9295   7703  -2050   2735   2201       N  
+ATOM   4132  CA  LEU B 121     -25.248   0.384  20.399  1.00 72.47           C  
+ANISOU 4132  CA  LEU B 121     9364   9836   8337  -2082   2831   1930       C  
+ATOM   4133  C   LEU B 121     -26.518  -0.459  20.474  1.00 72.49           C  
+ANISOU 4133  C   LEU B 121     9289   9816   8439  -2421   2944   2012       C  
+ATOM   4134  O   LEU B 121     -27.619   0.082  20.545  1.00 79.70           O  
+ANISOU 4134  O   LEU B 121     9891  10961   9431  -2494   3070   1830       O  
+ATOM   4135  CB  LEU B 121     -24.782   0.506  18.949  1.00 60.91           C  
+ANISOU 4135  CB  LEU B 121     7900   8125   7119  -1845   2642   1761       C  
+ATOM   4136  CG  LEU B 121     -23.786   1.631  18.661  1.00 58.28           C  
+ANISOU 4136  CG  LEU B 121     7528   7873   6741  -1531   2558   1603       C  
+ATOM   4137  CD1 LEU B 121     -23.271   1.536  17.232  1.00 49.53           C  
+ANISOU 4137  CD1 LEU B 121     6487   6509   5823  -1367   2413   1475       C  
+ATOM   4138  CD2 LEU B 121     -24.414   2.993  18.923  1.00 50.61           C  
+ANISOU 4138  CD2 LEU B 121     6292   7226   5712  -1499   2656   1383       C  
+ATOM   4139  N   GLU B 122     -26.371  -1.780  20.451  1.00 62.64           N  
+ANISOU 4139  N   GLU B 122     8299   8259   7243  -2590   2855   2271       N  
+ATOM   4140  CA  GLU B 122     -27.542  -2.646  20.484  1.00 74.90           C  
+ANISOU 4140  CA  GLU B 122     9771   9751   8936  -2892   2902   2357       C  
+ATOM   4141  C   GLU B 122     -28.200  -2.649  21.855  1.00 83.07           C  
+ANISOU 4141  C   GLU B 122    10713  11070   9782  -3033   3073   2458       C  
+ATOM   4142  O   GLU B 122     -29.420  -2.764  21.968  1.00 83.08           O  
+ANISOU 4142  O   GLU B 122    10472  11198   9899  -3237   3220   2394       O  
+ATOM   4143  CB  GLU B 122     -27.180  -4.084  20.113  1.00 70.90           C  
+ANISOU 4143  CB  GLU B 122     9601   8782   8554  -3032   2727   2608       C  
+ATOM   4144  CG  GLU B 122     -28.407  -4.936  19.857  1.00 98.35           C  
+ANISOU 4144  CG  GLU B 122    12980  12145  12244  -3348   2743   2654       C  
+ATOM   4145  CD  GLU B 122     -28.086  -6.395  19.604  1.00111.49           C  
+ANISOU 4145  CD  GLU B 122    14996  13318  14045  -3488   2536   2903       C  
+ATOM   4146  OE1 GLU B 122     -26.921  -6.710  19.279  1.00117.06           O  
+ANISOU 4146  OE1 GLU B 122    15990  13718  14770  -3274   2354   2959       O  
+ATOM   4147  OE2 GLU B 122     -28.999  -7.230  19.767  1.00 96.40           O  
+ANISOU 4147  OE2 GLU B 122    13053  11314  12261  -3769   2541   3021       O  
+ATOM   4148  N   GLU B 123     -27.388  -2.513  22.897  1.00 70.25           N  
+ANISOU 4148  N   GLU B 123     9293   9532   7867  -2938   3062   2601       N  
+ATOM   4149  CA  GLU B 123     -27.903  -2.442  24.260  1.00 74.10           C  
+ANISOU 4149  CA  GLU B 123     9772  10280   8102  -3073   3246   2669       C  
+ATOM   4150  C   GLU B 123     -28.711  -1.158  24.469  1.00 82.55           C  
+ANISOU 4150  C   GLU B 123    10464  11742   9158  -2988   3474   2330       C  
+ATOM   4151  O   GLU B 123     -29.521  -1.064  25.392  1.00 77.53           O  
+ANISOU 4151  O   GLU B 123     9723  11343   8393  -3143   3698   2302       O  
+ATOM   4152  CB  GLU B 123     -26.752  -2.562  25.257  1.00 74.96           C  
+ANISOU 4152  CB  GLU B 123    10238  10357   7888  -3000   3125   2891       C  
+ATOM   4153  CG  GLU B 123     -26.643  -3.967  25.833  1.00 92.66           C  
+ANISOU 4153  CG  GLU B 123    12822  12327  10059  -3246   3007   3266       C  
+ATOM   4154  CD  GLU B 123     -25.508  -4.125  26.819  1.00108.77           C  
+ANISOU 4154  CD  GLU B 123    15231  14304  11792  -3193   2816   3509       C  
+ATOM   4155  OE1 GLU B 123     -25.246  -3.178  27.588  1.00117.80           O  
+ANISOU 4155  OE1 GLU B 123    16358  15747  12655  -3093   2896   3396       O  
+ATOM   4156  OE2 GLU B 123     -24.878  -5.204  26.822  1.00108.67           O  
+ANISOU 4156  OE2 GLU B 123    15533  13917  11838  -3251   2551   3811       O  
+ATOM   4157  N   GLU B 124     -28.479  -0.171  23.608  1.00 71.75           N  
+ANISOU 4157  N   GLU B 124     8905  10424   7932  -2748   3414   2068       N  
+ATOM   4158  CA  GLU B 124     -29.271   1.056  23.610  1.00 71.02           C  
+ANISOU 4158  CA  GLU B 124     8438  10629   7917  -2646   3572   1723       C  
+ATOM   4159  C   GLU B 124     -30.403   0.958  22.592  1.00 75.24           C  
+ANISOU 4159  C   GLU B 124     8643  11120   8825  -2770   3595   1565       C  
+ATOM   4160  O   GLU B 124     -31.015   1.963  22.228  1.00 76.62           O  
+ANISOU 4160  O   GLU B 124     8478  11459   9174  -2664   3648   1257       O  
+ATOM   4161  CB  GLU B 124     -28.398   2.276  23.318  1.00 70.22           C  
+ANISOU 4161  CB  GLU B 124     8321  10597   7762  -2329   3468   1522       C  
+ATOM   4162  CG  GLU B 124     -27.832   2.927  24.562  1.00 83.52           C  
+ANISOU 4162  CG  GLU B 124    10143  12482   9108  -2221   3533   1509       C  
+ATOM   4163  CD  GLU B 124     -28.915   3.562  25.411  1.00 88.00           C  
+ANISOU 4163  CD  GLU B 124    10466  13351   9618  -2285   3793   1288       C  
+ATOM   4164  OE1 GLU B 124     -29.867   4.126  24.833  1.00 86.64           O  
+ANISOU 4164  OE1 GLU B 124     9926  13265   9727  -2258   3871   1022       O  
+ATOM   4165  OE2 GLU B 124     -28.820   3.491  26.654  1.00112.52           O  
+ANISOU 4165  OE2 GLU B 124    13749  16601  12401  -2373   3916   1371       O  
+ATOM   4166  N   ASN B 125     -30.655  -0.265  22.134  1.00 70.84           N  
+ANISOU 4166  N   ASN B 125     8198  10311   8408  -3002   3524   1774       N  
+ATOM   4167  CA  ASN B 125     -31.701  -0.568  21.159  1.00 72.84           C  
+ANISOU 4167  CA  ASN B 125     8186  10467   9024  -3181   3502   1666       C  
+ATOM   4168  C   ASN B 125     -31.553   0.191  19.844  1.00 74.51           C  
+ANISOU 4168  C   ASN B 125     8264  10589   9458  -3020   3349   1412       C  
+ATOM   4169  O   ASN B 125     -32.547   0.534  19.206  1.00 78.43           O  
+ANISOU 4169  O   ASN B 125     8410  11126  10262  -3103   3351   1196       O  
+ATOM   4170  CB  ASN B 125     -33.082  -0.281  21.755  1.00 75.78           C  
+ANISOU 4170  CB  ASN B 125     8155  11123   9514  -3333   3742   1519       C  
+ATOM   4171  CG  ASN B 125     -33.464  -1.262  22.843  1.00 95.89           C  
+ANISOU 4171  CG  ASN B 125    10836  13704  11895  -3602   3913   1785       C  
+ATOM   4172  OD1 ASN B 125     -33.774  -0.869  23.967  1.00109.56           O  
+ANISOU 4172  OD1 ASN B 125    12496  15714  13416  -3617   4150   1741       O  
+ATOM   4173  ND2 ASN B 125     -33.440  -2.549  22.516  1.00 97.23           N  
+ANISOU 4173  ND2 ASN B 125    11224  13567  12151  -3832   3793   2054       N  
+ATOM   4174  N   LYS B 126     -30.315   0.452  19.438  1.00 64.05           N  
+ANISOU 4174  N   LYS B 126     7212   9126   7998  -2803   3215   1434       N  
+ATOM   4175  CA  LYS B 126     -30.064   1.056  18.135  1.00 83.03           C  
+ANISOU 4175  CA  LYS B 126     9583  11370  10596  -2590   2994   1229       C  
+ATOM   4176  C   LYS B 126     -29.415   0.067  17.169  1.00 83.69           C  
+ANISOU 4176  C   LYS B 126    10008  11045  10746  -2559   2748   1363       C  
+ATOM   4177  O   LYS B 126     -28.713  -0.855  17.583  1.00 89.57           O  
+ANISOU 4177  O   LYS B 126    11052  11626  11355  -2611   2753   1605       O  
+ATOM   4178  CB  LYS B 126     -29.221   2.324  18.268  1.00 68.90           C  
+ANISOU 4178  CB  LYS B 126     7793   9731   8655  -2258   2956   1080       C  
+ATOM   4179  CG  LYS B 126     -29.977   3.460  18.945  1.00 68.73           C  
+ANISOU 4179  CG  LYS B 126     7398  10063   8654  -2235   3145    839       C  
+ATOM   4180  CD  LYS B 126     -29.239   4.782  18.848  1.00 56.08           C  
+ANISOU 4180  CD  LYS B 126     5790   8539   6979  -1904   3029    660       C  
+ATOM   4181  CE  LYS B 126     -27.838   4.684  19.400  1.00 63.65           C  
+ANISOU 4181  CE  LYS B 126     7090   9478   7617  -1782   3018    846       C  
+ATOM   4182  NZ  LYS B 126     -27.213   6.032  19.529  1.00 72.15           N  
+ANISOU 4182  NZ  LYS B 126     8122  10675   8616  -1512   2943    666       N  
+ATOM   4183  N   ILE B 127     -29.656   0.278  15.879  1.00 73.05           N  
+ANISOU 4183  N   ILE B 127     8626   9521   9609  -2472   2518   1189       N  
+ATOM   4184  CA  ILE B 127     -29.163  -0.613  14.835  1.00 59.61           C  
+ANISOU 4184  CA  ILE B 127     7239   7440   7971  -2453   2307   1237       C  
+ATOM   4185  C   ILE B 127     -27.817  -0.168  14.270  1.00 60.33           C  
+ANISOU 4185  C   ILE B 127     7568   7435   7921  -2137   2206   1175       C  
+ATOM   4186  O   ILE B 127     -27.668   0.957  13.792  1.00 65.94           O  
+ANISOU 4186  O   ILE B 127     8183   8261   8611  -1962   2130   1000       O  
+ATOM   4187  CB  ILE B 127     -30.177  -0.713  13.679  1.00 60.49           C  
+ANISOU 4187  CB  ILE B 127     7240   7399   8346  -2581   2094   1079       C  
+ATOM   4188  CG1 ILE B 127     -31.439  -1.445  14.139  1.00 66.49           C  
+ANISOU 4188  CG1 ILE B 127     7775   8184   9303  -2939   2183   1164       C  
+ATOM   4189  CG2 ILE B 127     -29.556  -1.409  12.477  1.00 58.33           C  
+ANISOU 4189  CG2 ILE B 127     7334   6755   8073  -2519   1878   1051       C  
+ATOM   4190  CD1 ILE B 127     -32.660  -1.137  13.301  1.00 66.07           C  
+ANISOU 4190  CD1 ILE B 127     7431   8110   9564  -3058   1983    972       C  
+ATOM   4191  N   ALA B 128     -26.837  -1.065  14.335  1.00 54.85           N  
+ANISOU 4191  N   ALA B 128     7169   6515   7157  -2075   2199   1319       N  
+ATOM   4192  CA  ALA B 128     -25.485  -0.766  13.882  1.00 57.76           C  
+ANISOU 4192  CA  ALA B 128     7719   6799   7429  -1790   2151   1258       C  
+ATOM   4193  C   ALA B 128     -25.200  -1.402  12.525  1.00 64.12           C  
+ANISOU 4193  C   ALA B 128     8761   7278   8326  -1757   2015   1131       C  
+ATOM   4194  O   ALA B 128     -25.346  -2.612  12.348  1.00 60.39           O  
+ANISOU 4194  O   ALA B 128     8459   6522   7965  -1878   1964   1202       O  
+ATOM   4195  CB  ALA B 128     -24.468  -1.237  14.909  1.00 53.01           C  
+ANISOU 4195  CB  ALA B 128     7245   6171   6724  -1696   2222   1467       C  
+ATOM   4196  N   ASP B 129     -24.797  -0.573  11.568  1.00 67.21           N  
+ANISOU 4196  N   ASP B 129     9185   7702   8651  -1612   1955    938       N  
+ATOM   4197  CA  ASP B 129     -24.353  -1.056  10.268  1.00 61.61           C  
+ANISOU 4197  CA  ASP B 129     8740   6726   7943  -1574   1877    782       C  
+ATOM   4198  C   ASP B 129     -22.851  -1.325  10.331  1.00 66.12           C  
+ANISOU 4198  C   ASP B 129     9444   7205   8471  -1337   1992    775       C  
+ATOM   4199  O   ASP B 129     -22.041  -0.405  10.219  1.00 64.69           O  
+ANISOU 4199  O   ASP B 129     9212   7186   8180  -1173   2057    707       O  
+ATOM   4200  CB  ASP B 129     -24.686  -0.042   9.171  1.00 64.73           C  
+ANISOU 4200  CB  ASP B 129     9145   7201   8248  -1589   1750    594       C  
+ATOM   4201  CG  ASP B 129     -24.564  -0.625   7.774  1.00 69.17           C  
+ANISOU 4201  CG  ASP B 129    10024   7496   8762  -1649   1656    421       C  
+ATOM   4202  OD1 ASP B 129     -23.965  -1.710   7.623  1.00 76.14           O  
+ANISOU 4202  OD1 ASP B 129    11102   8138   9687  -1605   1734    397       O  
+ATOM   4203  OD2 ASP B 129     -25.075   0.004   6.822  1.00 57.34           O  
+ANISOU 4203  OD2 ASP B 129     8598   6011   7179  -1742   1483    301       O  
+ATOM   4204  N   VAL B 130     -22.488  -2.592  10.508  1.00 61.50           N  
+ANISOU 4204  N   VAL B 130     9012   6340   8015  -1324   1998    844       N  
+ATOM   4205  CA  VAL B 130     -21.095  -2.976  10.717  1.00 68.74           C  
+ANISOU 4205  CA  VAL B 130     9996   7133   8990  -1079   2077    844       C  
+ATOM   4206  C   VAL B 130     -20.388  -3.320   9.409  1.00 66.06           C  
+ANISOU 4206  C   VAL B 130     9851   6581   8669   -966   2132    565       C  
+ATOM   4207  O   VAL B 130     -20.834  -4.187   8.657  1.00 65.92           O  
+ANISOU 4207  O   VAL B 130    10037   6293   8717  -1074   2068    448       O  
+ATOM   4208  CB  VAL B 130     -20.986  -4.178  11.673  1.00 58.77           C  
+ANISOU 4208  CB  VAL B 130     8802   5634   7895  -1098   2015   1073       C  
+ATOM   4209  CG1 VAL B 130     -19.529  -4.481  11.979  1.00 61.63           C  
+ANISOU 4209  CG1 VAL B 130     9176   5864   8377   -811   2037   1079       C  
+ATOM   4210  CG2 VAL B 130     -21.755  -3.904  12.952  1.00 55.76           C  
+ANISOU 4210  CG2 VAL B 130     8274   5482   7429  -1275   2007   1342       C  
+ATOM   4211  N   LYS B 131     -19.279  -2.633   9.150  1.00 74.84           N  
+ANISOU 4211  N   LYS B 131    10898   7823   9716   -768   2265    445       N  
+ATOM   4212  CA  LYS B 131     -18.535  -2.801   7.907  1.00 70.58           C  
+ANISOU 4212  CA  LYS B 131    10517   7156   9144   -680   2397    148       C  
+ATOM   4213  C   LYS B 131     -17.127  -3.335   8.159  1.00 69.67           C  
+ANISOU 4213  C   LYS B 131    10329   6900   9245   -401   2525     78       C  
+ATOM   4214  O   LYS B 131     -16.321  -2.676   8.815  1.00 68.53           O  
+ANISOU 4214  O   LYS B 131     9966   6945   9128   -252   2577    168       O  
+ATOM   4215  CB  LYS B 131     -18.432  -1.465   7.166  1.00 61.11           C  
+ANISOU 4215  CB  LYS B 131     9302   6238   7681   -733   2473     30       C  
+ATOM   4216  CG  LYS B 131     -19.719  -0.659   7.089  1.00 58.01           C  
+ANISOU 4216  CG  LYS B 131     8895   6014   7133   -953   2295    119       C  
+ATOM   4217  CD  LYS B 131     -20.723  -1.261   6.128  1.00 63.55           C  
+ANISOU 4217  CD  LYS B 131     9843   6515   7789  -1164   2155      3       C  
+ATOM   4218  CE  LYS B 131     -21.790  -0.239   5.771  1.00 60.48           C  
+ANISOU 4218  CE  LYS B 131     9425   6295   7259  -1350   1955     34       C  
+ATOM   4219  NZ  LYS B 131     -22.836  -0.798   4.873  1.00 61.58           N  
+ANISOU 4219  NZ  LYS B 131     9785   6234   7378  -1574   1749    -62       N  
+ATOM   4220  N   TYR B 132     -16.828  -4.526   7.647  1.00 74.55           N  
+ANISOU 4220  N   TYR B 132    11111   7165  10050   -322   2552    -98       N  
+ATOM   4221  CA  TYR B 132     -15.462  -5.041   7.713  1.00 78.39           C  
+ANISOU 4221  CA  TYR B 132    11492   7484  10807    -25   2676   -240       C  
+ATOM   4222  C   TYR B 132     -14.994  -5.613   6.375  1.00 79.51           C  
+ANISOU 4222  C   TYR B 132    11816   7423  10972     39   2884   -662       C  
+ATOM   4223  O   TYR B 132     -13.820  -5.949   6.216  1.00 80.35           O  
+ANISOU 4223  O   TYR B 132    11796   7418  11316    294   3055   -874       O  
+ATOM   4224  CB  TYR B 132     -15.326  -6.092   8.821  1.00 87.35           C  
+ANISOU 4224  CB  TYR B 132    12594   8319  12276     96   2461     -7       C  
+ATOM   4225  CG  TYR B 132     -16.477  -7.068   8.933  1.00 85.96           C  
+ANISOU 4225  CG  TYR B 132    12655   7864  12142   -114   2258    124       C  
+ATOM   4226  CD1 TYR B 132     -16.539  -8.199   8.130  1.00 94.02           C  
+ANISOU 4226  CD1 TYR B 132    13910   8480  13332    -96   2242   -117       C  
+ATOM   4227  CD2 TYR B 132     -17.491  -6.867   9.861  1.00 75.28           C  
+ANISOU 4227  CD2 TYR B 132    11283   6650  10670   -344   2095    472       C  
+ATOM   4228  CE1 TYR B 132     -17.588  -9.095   8.238  1.00 96.55           C  
+ANISOU 4228  CE1 TYR B 132    14445   8525  13713   -317   2032     15       C  
+ATOM   4229  CE2 TYR B 132     -18.542  -7.756   9.977  1.00 76.51           C  
+ANISOU 4229  CE2 TYR B 132    11623   6564  10883   -577   1930    602       C  
+ATOM   4230  CZ  TYR B 132     -18.586  -8.869   9.163  1.00 92.08           C  
+ANISOU 4230  CZ  TYR B 132    13831   8117  13038   -570   1879    388       C  
+ATOM   4231  OH  TYR B 132     -19.632  -9.757   9.275  1.00 95.12           O  
+ANISOU 4231  OH  TYR B 132    14398   8241  13501   -829   1691    528       O  
+ATOM   4232  N   THR B 133     -15.909  -5.726   5.416  1.00 79.15           N  
+ANISOU 4232  N   THR B 133    12058   7327  10686   -197   2867   -803       N  
+ATOM   4233  CA  THR B 133     -15.544  -6.105   4.053  1.00 80.05           C  
+ANISOU 4233  CA  THR B 133    12409   7309  10697   -196   3089  -1231       C  
+ATOM   4234  C   THR B 133     -15.804  -4.957   3.079  1.00 77.07           C  
+ANISOU 4234  C   THR B 133    12166   7257   9858   -423   3215  -1337       C  
+ATOM   4235  O   THR B 133     -16.545  -4.025   3.389  1.00 75.67           O  
+ANISOU 4235  O   THR B 133    11938   7327   9487   -597   3050  -1082       O  
+ATOM   4236  CB  THR B 133     -16.305  -7.356   3.575  1.00 81.45           C  
+ANISOU 4236  CB  THR B 133    12908   7077  10963   -298   2930  -1362       C  
+ATOM   4237  OG1 THR B 133     -17.677  -7.023   3.333  1.00 84.13           O  
+ANISOU 4237  OG1 THR B 133    13425   7503  11038   -627   2706  -1211       O  
+ATOM   4238  CG2 THR B 133     -16.223  -8.465   4.613  1.00 82.87           C  
+ANISOU 4238  CG2 THR B 133    13001   6900  11587   -135   2724  -1174       C  
+ATOM   4239  N   VAL B 134     -15.189  -5.032   1.903  1.00 76.92           N  
+ANISOU 4239  N   VAL B 134    12333   7227   9667   -428   3503  -1721       N  
+ATOM   4240  CA  VAL B 134     -15.373  -4.019   0.868  1.00 75.12           C  
+ANISOU 4240  CA  VAL B 134    12317   7272   8952   -685   3615  -1822       C  
+ATOM   4241  C   VAL B 134     -16.803  -4.019   0.323  1.00 76.16           C  
+ANISOU 4241  C   VAL B 134    12792   7331   8815   -997   3295  -1748       C  
+ATOM   4242  O   VAL B 134     -17.402  -2.959   0.126  1.00 75.75           O  
+ANISOU 4242  O   VAL B 134    12792   7512   8477  -1209   3143  -1578       O  
+ATOM   4243  CB  VAL B 134     -14.373  -4.227  -0.295  1.00 77.66           C  
+ANISOU 4243  CB  VAL B 134    12803   7593   9110   -658   4045  -2280       C  
+ATOM   4244  CG1 VAL B 134     -14.894  -3.608  -1.588  1.00 74.87           C  
+ANISOU 4244  CG1 VAL B 134    12884   7385   8177  -1017   4074  -2410       C  
+ATOM   4245  CG2 VAL B 134     -13.011  -3.650   0.068  1.00 73.76           C  
+ANISOU 4245  CG2 VAL B 134    11919   7328   8776   -451   4375  -2319       C  
+ATOM   4246  N   LYS B 135     -17.351  -5.210   0.099  1.00 80.76           N  
+ANISOU 4246  N   LYS B 135    13591   7561   9531  -1021   3157  -1874       N  
+ATOM   4247  CA  LYS B 135     -18.688  -5.347  -0.473  1.00 80.80           C  
+ANISOU 4247  CA  LYS B 135    13912   7456   9335  -1324   2829  -1838       C  
+ATOM   4248  C   LYS B 135     -19.768  -4.735   0.419  1.00 87.73           C  
+ANISOU 4248  C   LYS B 135    14561   8473  10300  -1441   2486  -1424       C  
+ATOM   4249  O   LYS B 135     -20.731  -4.143  -0.073  1.00 91.29           O  
+ANISOU 4249  O   LYS B 135    15155   9011  10519  -1695   2236  -1350       O  
+ATOM   4250  CB  LYS B 135     -19.008  -6.823  -0.729  1.00 80.56           C  
+ANISOU 4250  CB  LYS B 135    14116   6984   9511  -1313   2730  -2040       C  
+ATOM   4251  CG  LYS B 135     -20.429  -7.077  -1.212  1.00 80.79           C  
+ANISOU 4251  CG  LYS B 135    14426   6860   9411  -1634   2340  -1985       C  
+ATOM   4252  CD  LYS B 135     -20.586  -8.470  -1.798  1.00 96.66           C  
+ANISOU 4252  CD  LYS B 135    16771   8423  11534  -1658   2281  -2288       C  
+ATOM   4253  CE  LYS B 135     -22.055  -8.845  -1.924  1.00103.47           C  
+ANISOU 4253  CE  LYS B 135    17795   9098  12421  -1964   1829  -2146       C  
+ATOM   4254  NZ  LYS B 135     -22.286  -9.905  -2.944  1.00108.45           N  
+ANISOU 4254  NZ  LYS B 135    18892   9342  12972  -2087   1738  -2515       N  
+ATOM   4255  N   GLN B 136     -19.591  -4.863   1.732  1.00 79.09           N  
+ANISOU 4255  N   GLN B 136    13110   7400   9542  -1257   2473  -1170       N  
+ATOM   4256  CA  GLN B 136     -20.564  -4.352   2.694  1.00 74.15           C  
+ANISOU 4256  CA  GLN B 136    12239   6924   9012  -1357   2222   -814       C  
+ATOM   4257  C   GLN B 136     -20.714  -2.834   2.637  1.00 71.59           C  
+ANISOU 4257  C   GLN B 136    11792   6964   8446  -1432   2189   -700       C  
+ATOM   4258  O   GLN B 136     -21.694  -2.285   3.139  1.00 68.41           O  
+ANISOU 4258  O   GLN B 136    11226   6687   8081  -1550   1964   -488       O  
+ATOM   4259  CB  GLN B 136     -20.182  -4.779   4.114  1.00 73.38           C  
+ANISOU 4259  CB  GLN B 136    11839   6792   9248  -1158   2254   -578       C  
+ATOM   4260  CG  GLN B 136     -20.513  -6.227   4.442  1.00 74.85           C  
+ANISOU 4260  CG  GLN B 136    12129   6588   9723  -1168   2132   -550       C  
+ATOM   4261  CD  GLN B 136     -20.014  -6.645   5.812  1.00 74.81           C  
+ANISOU 4261  CD  GLN B 136    11891   6529  10006   -987   2137   -294       C  
+ATOM   4262  OE1 GLN B 136     -18.916  -6.272   6.224  1.00 75.49           O  
+ANISOU 4262  OE1 GLN B 136    11803   6737  10143   -746   2297   -292       O  
+ATOM   4263  NE2 GLN B 136     -20.819  -7.427   6.523  1.00 74.56           N  
+ANISOU 4263  NE2 GLN B 136    11866   6308  10158  -1130   1942    -64       N  
+ATOM   4264  N   LEU B 137     -19.743  -2.161   2.029  1.00 72.58           N  
+ANISOU 4264  N   LEU B 137    11984   7247   8345  -1371   2419   -852       N  
+ATOM   4265  CA  LEU B 137     -19.814  -0.715   1.863  1.00 69.28           C  
+ANISOU 4265  CA  LEU B 137    11508   7126   7688  -1464   2365   -748       C  
+ATOM   4266  C   LEU B 137     -20.835  -0.327   0.798  1.00 69.97           C  
+ANISOU 4266  C   LEU B 137    11907   7182   7497  -1755   2084   -794       C  
+ATOM   4267  O   LEU B 137     -21.329   0.800   0.783  1.00 77.59           O  
+ANISOU 4267  O   LEU B 137    12811   8318   8351  -1858   1881   -649       O  
+ATOM   4268  CB  LEU B 137     -18.442  -0.144   1.500  1.00 65.97           C  
+ANISOU 4268  CB  LEU B 137    11080   6875   7112  -1362   2702   -882       C  
+ATOM   4269  CG  LEU B 137     -17.353  -0.242   2.570  1.00 69.70           C  
+ANISOU 4269  CG  LEU B 137    11190   7419   7874  -1071   2920   -813       C  
+ATOM   4270  CD1 LEU B 137     -16.010   0.201   2.010  1.00 63.14           C  
+ANISOU 4270  CD1 LEU B 137    10343   6731   6917  -1008   3275  -1003       C  
+ATOM   4271  CD2 LEU B 137     -17.725   0.581   3.792  1.00 71.84           C  
+ANISOU 4271  CD2 LEU B 137    11143   7883   8272  -1019   2738   -502       C  
+ATOM   4272  N   ALA B 138     -21.149  -1.263  -0.092  1.00 72.83           N  
+ANISOU 4272  N   ALA B 138    12614   7296   7764  -1885   2035  -1003       N  
+ATOM   4273  CA  ALA B 138     -22.090  -0.989  -1.173  1.00 73.08           C  
+ANISOU 4273  CA  ALA B 138    12993   7261   7512  -2180   1718  -1057       C  
+ATOM   4274  C   ALA B 138     -23.534  -1.077  -0.693  1.00 72.40           C  
+ANISOU 4274  C   ALA B 138    12735   7093   7679  -2294   1301   -864       C  
+ATOM   4275  O   ALA B 138     -24.452  -0.615  -1.371  1.00 74.79           O  
+ANISOU 4275  O   ALA B 138    13205   7369   7842  -2518    940   -840       O  
+ATOM   4276  CB  ALA B 138     -21.859  -1.947  -2.329  1.00 74.92           C  
+ANISOU 4276  CB  ALA B 138    13691   7261   7515  -2293   1819  -1386       C  
+ATOM   4277  N   THR B 139     -23.731  -1.671   0.478  1.00 70.92           N  
+ANISOU 4277  N   THR B 139    12209   6865   7872  -2155   1344   -723       N  
+ATOM   4278  CA  THR B 139     -25.069  -1.836   1.029  1.00 69.35           C  
+ANISOU 4278  CA  THR B 139    11789   6614   7945  -2280   1030   -552       C  
+ATOM   4279  C   THR B 139     -25.275  -0.844   2.171  1.00 66.71           C  
+ANISOU 4279  C   THR B 139    11006   6562   7776  -2170   1034   -318       C  
+ATOM   4280  O   THR B 139     -24.315  -0.402   2.802  1.00 71.89           O  
+ANISOU 4280  O   THR B 139    11509   7393   8412  -1967   1294   -263       O  
+ATOM   4281  CB  THR B 139     -25.305  -3.280   1.527  1.00 80.71           C  
+ANISOU 4281  CB  THR B 139    13207   7787   9671  -2281   1062   -547       C  
+ATOM   4282  OG1 THR B 139     -24.763  -4.208   0.579  1.00 89.12           O  
+ANISOU 4282  OG1 THR B 139    14683   8584  10595  -2296   1152   -818       O  
+ATOM   4283  CG2 THR B 139     -26.792  -3.562   1.700  1.00 82.26           C  
+ANISOU 4283  CG2 THR B 139    13265   7890  10099  -2515    717   -431       C  
+ATOM   4284  N   THR B 140     -26.531  -0.504   2.435  1.00 68.04           N  
+ANISOU 4284  N   THR B 140    10953   6771   8129  -2305    741   -207       N  
+ATOM   4285  CA  THR B 140     -26.883   0.384   3.533  1.00 67.35           C  
+ANISOU 4285  CA  THR B 140    10426   6939   8223  -2211    749    -38       C  
+ATOM   4286  C   THR B 140     -27.976  -0.253   4.379  1.00 67.87           C  
+ANISOU 4286  C   THR B 140    10185   6975   8626  -2319    679     74       C  
+ATOM   4287  O   THR B 140     -29.109  -0.405   3.926  1.00 67.66           O  
+ANISOU 4287  O   THR B 140    10122   6841   8744  -2520    381     45       O  
+ATOM   4288  CB  THR B 140     -27.355   1.760   3.028  1.00 67.17           C  
+ANISOU 4288  CB  THR B 140    10360   7042   8119  -2254    467    -42       C  
+ATOM   4289  OG1 THR B 140     -26.328   2.356   2.226  1.00 78.97           O  
+ANISOU 4289  OG1 THR B 140    12172   8568   9263  -2212    548   -117       O  
+ATOM   4290  CG2 THR B 140     -27.671   2.677   4.198  1.00 64.45           C  
+ANISOU 4290  CG2 THR B 140     9555   6948   7984  -2123    504     76       C  
+ATOM   4291  N   LYS B 141     -27.629  -0.630   5.606  1.00 72.96           N  
+ANISOU 4291  N   LYS B 141    10615   7715   9391  -2213    945    209       N  
+ATOM   4292  CA  LYS B 141     -28.564  -1.326   6.482  1.00 68.54           C  
+ANISOU 4292  CA  LYS B 141     9798   7140   9103  -2362    950    339       C  
+ATOM   4293  C   LYS B 141     -29.756  -0.441   6.817  1.00 68.19           C  
+ANISOU 4293  C   LYS B 141     9357   7302   9250  -2451    796    355       C  
+ATOM   4294  O   LYS B 141     -29.599   0.713   7.217  1.00 64.79           O  
+ANISOU 4294  O   LYS B 141     8724   7114   8778  -2301    841    350       O  
+ATOM   4295  CB  LYS B 141     -27.864  -1.769   7.766  1.00 63.44           C  
+ANISOU 4295  CB  LYS B 141     9052   6578   8476  -2244   1252    508       C  
+ATOM   4296  CG  LYS B 141     -28.576  -2.874   8.529  1.00 64.61           C  
+ANISOU 4296  CG  LYS B 141     9100   6615   8832  -2452   1287    667       C  
+ATOM   4297  CD  LYS B 141     -27.816  -3.231   9.797  1.00 62.51           C  
+ANISOU 4297  CD  LYS B 141     8801   6423   8528  -2348   1535    867       C  
+ATOM   4298  CE  LYS B 141     -28.285  -4.559  10.371  1.00 61.50           C  
+ANISOU 4298  CE  LYS B 141     8725   6081   8562  -2579   1543   1051       C  
+ATOM   4299  NZ  LYS B 141     -29.769  -4.689  10.353  1.00 76.13           N  
+ANISOU 4299  NZ  LYS B 141    10344   7969  10611  -2896   1441   1067       N  
+ATOM   4300  N   VAL B 142     -30.948  -1.003   6.647  1.00 73.17           N  
+ANISOU 4300  N   VAL B 142     9859   7816  10126  -2693    605    353       N  
+ATOM   4301  CA  VAL B 142     -32.196  -0.281   6.853  1.00 77.35           C  
+ANISOU 4301  CA  VAL B 142     9959   8502  10929  -2789    432    323       C  
+ATOM   4302  C   VAL B 142     -32.354   0.176   8.302  1.00 80.58           C  
+ANISOU 4302  C   VAL B 142     9945   9231  11441  -2719    741    411       C  
+ATOM   4303  O   VAL B 142     -32.063  -0.578   9.231  1.00 83.39           O  
+ANISOU 4303  O   VAL B 142    10298   9625  11760  -2769   1028    558       O  
+ATOM   4304  CB  VAL B 142     -33.404  -1.159   6.449  1.00 74.79           C  
+ANISOU 4304  CB  VAL B 142     9548   7974  10894  -3095    190    310       C  
+ATOM   4305  CG1 VAL B 142     -34.718  -0.474   6.787  1.00 76.33           C  
+ANISOU 4305  CG1 VAL B 142     9195   8345  11462  -3186     47    262       C  
+ATOM   4306  CG2 VAL B 142     -33.340  -1.497   4.967  1.00 80.08           C  
+ANISOU 4306  CG2 VAL B 142    10663   8334  11432  -3180   -166    188       C  
+ATOM   4307  N   LYS B 143     -32.806   1.417   8.477  1.00 70.23           N  
+ANISOU 4307  N   LYS B 143     8309   8131  10246  -2607    661    315       N  
+ATOM   4308  CA  LYS B 143     -33.130   1.972   9.791  1.00 71.67           C  
+ANISOU 4308  CA  LYS B 143     8060   8633  10539  -2551    943    326       C  
+ATOM   4309  C   LYS B 143     -31.930   1.998  10.736  1.00 71.18           C  
+ANISOU 4309  C   LYS B 143     8152   8723  10171  -2387   1292    443       C  
+ATOM   4310  O   LYS B 143     -32.094   1.978  11.956  1.00 89.38           O  
+ANISOU 4310  O   LYS B 143    10224  11259  12477  -2421   1589    507       O  
+ATOM   4311  CB  LYS B 143     -34.282   1.190  10.432  1.00 84.16           C  
+ANISOU 4311  CB  LYS B 143     9294  10270  12411  -2832   1069    372       C  
+ATOM   4312  N   ARG B 144     -30.728   2.036  10.169  1.00 62.05           N  
+ANISOU 4312  N   ARG B 144     7387   7442   8748  -2226   1255    464       N  
+ATOM   4313  CA  ARG B 144     -29.510   2.068  10.970  1.00 65.88           C  
+ANISOU 4313  CA  ARG B 144     8008   8037   8984  -2057   1521    570       C  
+ATOM   4314  C   ARG B 144     -29.403   3.376  11.748  1.00 70.27           C  
+ANISOU 4314  C   ARG B 144     8308   8888   9504  -1881   1617    505       C  
+ATOM   4315  O   ARG B 144     -29.879   4.419  11.296  1.00 82.32           O  
+ANISOU 4315  O   ARG B 144     9671  10461  11147  -1810   1420    355       O  
+ATOM   4316  CB  ARG B 144     -28.269   1.887  10.093  1.00 62.27           C  
+ANISOU 4316  CB  ARG B 144     7959   7389   8311  -1922   1466    560       C  
+ATOM   4317  CG  ARG B 144     -27.967   3.071   9.189  1.00 57.09           C  
+ANISOU 4317  CG  ARG B 144     7381   6750   7559  -1796   1274    426       C  
+ATOM   4318  CD  ARG B 144     -26.857   2.753   8.204  1.00 60.30           C  
+ANISOU 4318  CD  ARG B 144     8191   6976   7745  -1737   1269    391       C  
+ATOM   4319  NE  ARG B 144     -26.446   3.937   7.457  1.00 69.83           N  
+ANISOU 4319  NE  ARG B 144     9499   8230   8804  -1655   1130    306       N  
+ATOM   4320  CZ  ARG B 144     -25.488   3.946   6.536  1.00 70.00           C  
+ANISOU 4320  CZ  ARG B 144     9849   8153   8596  -1628   1154    249       C  
+ATOM   4321  NH1 ARG B 144     -24.837   2.828   6.243  1.00 73.54           N  
+ANISOU 4321  NH1 ARG B 144    10528   8442   8972  -1633   1317    225       N  
+ATOM   4322  NH2 ARG B 144     -25.179   5.073   5.909  1.00 62.05           N  
+ANISOU 4322  NH2 ARG B 144     8939   7197   7439  -1606   1024    207       N  
+ATOM   4323  N   ASP B 145     -28.789   3.313  12.924  1.00 54.49           N  
+ANISOU 4323  N   ASP B 145     6293   7061   7350  -1817   1884    615       N  
+ATOM   4324  CA  ASP B 145     -28.548   4.507  13.724  1.00 51.64           C  
+ANISOU 4324  CA  ASP B 145     5745   6966   6911  -1648   1983    539       C  
+ATOM   4325  C   ASP B 145     -27.082   4.924  13.658  1.00 49.57           C  
+ANISOU 4325  C   ASP B 145     5734   6684   6417  -1435   1982    583       C  
+ATOM   4326  O   ASP B 145     -26.755   6.101  13.810  1.00 54.53           O  
+ANISOU 4326  O   ASP B 145     6278   7441   6998  -1274   1940    485       O  
+ATOM   4327  CB  ASP B 145     -28.971   4.271  15.174  1.00 52.21           C  
+ANISOU 4327  CB  ASP B 145     5615   7286   6938  -1759   2280    607       C  
+ATOM   4328  CG  ASP B 145     -30.448   3.956  15.303  1.00 66.17           C  
+ANISOU 4328  CG  ASP B 145     7055   9120   8966  -1991   2336    537       C  
+ATOM   4329  OD1 ASP B 145     -31.267   4.892  15.194  1.00 85.46           O  
+ANISOU 4329  OD1 ASP B 145     9160  11681  11627  -1935   2266    317       O  
+ATOM   4330  OD2 ASP B 145     -30.792   2.772  15.498  1.00 85.77           O  
+ANISOU 4330  OD2 ASP B 145     9601  11517  11470  -2233   2433    697       O  
+ATOM   4331  N   ALA B 146     -26.202   3.954  13.425  1.00 53.24           N  
+ANISOU 4331  N   ALA B 146     6483   6970   6777  -1434   2020    718       N  
+ATOM   4332  CA  ALA B 146     -24.774   4.232  13.329  1.00 63.40           C  
+ANISOU 4332  CA  ALA B 146     7958   8230   7902  -1242   2036    749       C  
+ATOM   4333  C   ALA B 146     -24.073   3.272  12.371  1.00 62.27           C  
+ANISOU 4333  C   ALA B 146     8101   7809   7750  -1237   2001    771       C  
+ATOM   4334  O   ALA B 146     -24.472   2.117  12.229  1.00 64.88           O  
+ANISOU 4334  O   ALA B 146     8528   7959   8164  -1371   2004    832       O  
+ATOM   4335  CB  ALA B 146     -24.130   4.164  14.706  1.00 45.11           C  
+ANISOU 4335  CB  ALA B 146     5614   6071   5456  -1176   2199    887       C  
+ATOM   4336  N   VAL B 147     -23.024   3.762  11.718  1.00 46.39           N  
+ANISOU 4336  N   VAL B 147     6219   5761   5645  -1095   1983    702       N  
+ATOM   4337  CA  VAL B 147     -22.161   2.913  10.908  1.00 50.26           C  
+ANISOU 4337  CA  VAL B 147     6954   6024   6120  -1054   2022    673       C  
+ATOM   4338  C   VAL B 147     -20.884   2.614  11.678  1.00 53.42           C  
+ANISOU 4338  C   VAL B 147     7353   6432   6512   -881   2148    772       C  
+ATOM   4339  O   VAL B 147     -20.277   3.518  12.242  1.00 49.54           O  
+ANISOU 4339  O   VAL B 147     6742   6125   5954   -766   2171    795       O  
+ATOM   4340  CB  VAL B 147     -21.799   3.578   9.569  1.00 49.96           C  
+ANISOU 4340  CB  VAL B 147     7068   5942   5972  -1049   1957    514       C  
+ATOM   4341  CG1 VAL B 147     -20.968   2.633   8.714  1.00 45.41           C  
+ANISOU 4341  CG1 VAL B 147     6738   5145   5371  -1020   2060    425       C  
+ATOM   4342  CG2 VAL B 147     -23.053   3.985   8.832  1.00 72.11           C  
+ANISOU 4342  CG2 VAL B 147     9883   8722   8793  -1215   1743    437       C  
+ATOM   4343  N   VAL B 148     -20.470   1.352  11.704  1.00 55.58           N  
+ANISOU 4343  N   VAL B 148     7757   6477   6883   -858   2190    826       N  
+ATOM   4344  CA  VAL B 148     -19.232   0.994  12.382  1.00 46.26           C  
+ANISOU 4344  CA  VAL B 148     6563   5252   5761   -674   2246    918       C  
+ATOM   4345  C   VAL B 148     -18.240   0.357  11.415  1.00 52.31           C  
+ANISOU 4345  C   VAL B 148     7461   5785   6629   -547   2317    762       C  
+ATOM   4346  O   VAL B 148     -18.361  -0.815  11.059  1.00 52.60           O  
+ANISOU 4346  O   VAL B 148     7650   5544   6792   -571   2305    732       O  
+ATOM   4347  CB  VAL B 148     -19.488   0.035  13.560  1.00 53.21           C  
+ANISOU 4347  CB  VAL B 148     7462   6045   6709   -731   2203   1152       C  
+ATOM   4348  CG1 VAL B 148     -18.186  -0.267  14.287  1.00 56.75           C  
+ANISOU 4348  CG1 VAL B 148     7901   6424   7238   -531   2177   1266       C  
+ATOM   4349  CG2 VAL B 148     -20.501   0.639  14.520  1.00 47.46           C  
+ANISOU 4349  CG2 VAL B 148     6599   5582   5851   -887   2207   1265       C  
+ATOM   4350  N   TYR B 149     -17.261   1.150  10.996  1.00 52.18           N  
+ANISOU 4350  N   TYR B 149     7375   5882   6567   -421   2405    644       N  
+ATOM   4351  CA  TYR B 149     -16.176   0.682  10.149  1.00 55.52           C  
+ANISOU 4351  CA  TYR B 149     7858   6146   7091   -289   2546    457       C  
+ATOM   4352  C   TYR B 149     -15.104   0.012  10.992  1.00 59.50           C  
+ANISOU 4352  C   TYR B 149     8241   6526   7842    -70   2536    546       C  
+ATOM   4353  O   TYR B 149     -14.398   0.679  11.747  1.00 64.33           O  
+ANISOU 4353  O   TYR B 149     8666   7303   8474     37   2506    644       O  
+ATOM   4354  CB  TYR B 149     -15.551   1.845   9.381  1.00 51.25           C  
+ANISOU 4354  CB  TYR B 149     7271   5800   6401   -291   2667    311       C  
+ATOM   4355  CG  TYR B 149     -16.498   2.635   8.511  1.00 47.21           C  
+ANISOU 4355  CG  TYR B 149     6904   5388   5647   -503   2609    244       C  
+ATOM   4356  CD1 TYR B 149     -16.748   2.258   7.199  1.00 47.74           C  
+ANISOU 4356  CD1 TYR B 149     7224   5320   5597   -627   2669     55       C  
+ATOM   4357  CD2 TYR B 149     -17.137   3.767   9.000  1.00 43.95           C  
+ANISOU 4357  CD2 TYR B 149     6386   5183   5130   -576   2466    358       C  
+ATOM   4358  CE1 TYR B 149     -17.608   2.986   6.399  1.00 50.55           C  
+ANISOU 4358  CE1 TYR B 149     7737   5739   5731   -832   2542     20       C  
+ATOM   4359  CE2 TYR B 149     -17.997   4.502   8.208  1.00 43.42           C  
+ANISOU 4359  CE2 TYR B 149     6436   5162   4900   -749   2346    304       C  
+ATOM   4360  CZ  TYR B 149     -18.230   4.106   6.909  1.00 48.69           C  
+ANISOU 4360  CZ  TYR B 149     7368   5685   5447   -883   2362    155       C  
+ATOM   4361  OH  TYR B 149     -19.089   4.833   6.117  1.00 58.15           O  
+ANISOU 4361  OH  TYR B 149     8711   6901   6483  -1067   2171    127       O  
+ATOM   4362  N   LYS B 150     -14.977  -1.302  10.868  1.00 64.39           N  
+ANISOU 4362  N   LYS B 150     8971   6824   8670     -1   2518    511       N  
+ATOM   4363  CA  LYS B 150     -13.912  -2.013  11.558  1.00 70.58           C  
+ANISOU 4363  CA  LYS B 150     9644   7420   9754    234   2453    580       C  
+ATOM   4364  C   LYS B 150     -12.860  -2.454  10.544  1.00 75.42           C  
+ANISOU 4364  C   LYS B 150    10217   7860  10581    421   2647    260       C  
+ATOM   4365  O   LYS B 150     -12.945  -3.538   9.966  1.00 78.01           O  
+ANISOU 4365  O   LYS B 150    10700   7875  11065    460   2673    105       O  
+ATOM   4366  CB  LYS B 150     -14.487  -3.187  12.349  1.00 71.49           C  
+ANISOU 4366  CB  LYS B 150     9903   7260   9998    185   2244    807       C  
+ATOM   4367  CG  LYS B 150     -15.654  -2.750  13.230  1.00 67.82           C  
+ANISOU 4367  CG  LYS B 150     9477   7010   9282    -56   2140   1073       C  
+ATOM   4368  CD  LYS B 150     -16.280  -3.887  14.010  1.00 66.80           C  
+ANISOU 4368  CD  LYS B 150     9511   6635   9234   -181   1966   1327       C  
+ATOM   4369  CE  LYS B 150     -15.354  -4.367  15.112  1.00 71.11           C  
+ANISOU 4369  CE  LYS B 150    10033   7035   9952    -19   1771   1555       C  
+ATOM   4370  NZ  LYS B 150     -16.051  -5.290  16.050  1.00 81.71           N  
+ANISOU 4370  NZ  LYS B 150    11575   8194  11278   -219   1585   1881       N  
+HETATM 4371  N   MSE B 151     -11.871  -1.587  10.339  1.00 72.47           N  
+ANISOU 4371  N   MSE B 151     9624   7696  10217    524   2799    144       N  
+HETATM 4372  CA  MSE B 151     -10.903  -1.718   9.253  1.00 74.62           C  
+ANISOU 4372  CA  MSE B 151     9817   7915  10619    644   3086   -206       C  
+HETATM 4373  C   MSE B 151     -10.060  -2.985   9.325  1.00 84.27           C  
+ANISOU 4373  C   MSE B 151    10946   8774  12300    924   3078   -347       C  
+HETATM 4374  O   MSE B 151     -10.013  -3.761   8.370  1.00108.87           O  
+ANISOU 4374  O   MSE B 151    14197  11671  15499    962   3253   -647       O  
+HETATM 4375  CB  MSE B 151      -9.976  -0.501   9.232  1.00 75.81           C  
+ANISOU 4375  CB  MSE B 151     9700   8377  10726    670   3230   -244       C  
+HETATM 4376  CG  MSE B 151     -10.700   0.832   9.265  1.00 66.90           C  
+ANISOU 4376  CG  MSE B 151     8643   7570   9207    429   3184    -97       C  
+HETATM 4377 SE   MSE B 151      -9.467   2.343   9.273  1.00125.77          SE  
+ANISOU 4377 SE   MSE B 151    15777  15363  16648    435   3325   -125      SE  
+HETATM 4378  CE  MSE B 151      -8.788   2.185   7.452  1.00 62.85           C  
+ANISOU 4378  CE  MSE B 151     7879   7391   8609    355   3807   -554       C  
+ATOM   4379  N   HIS B 152      -9.395  -3.196  10.456  1.00 77.55           N  
+ANISOU 4379  N   HIS B 152     9877   7834  11755   1122   2847   -144       N  
+ATOM   4380  CA  HIS B 152      -8.464  -4.312  10.583  1.00 89.57           C  
+ANISOU 4380  CA  HIS B 152    11253   8985  13796   1430   2778   -273       C  
+ATOM   4381  C   HIS B 152      -9.176  -5.651  10.734  1.00 89.76           C  
+ANISOU 4381  C   HIS B 152    11566   8585  13956   1433   2561   -196       C  
+ATOM   4382  O   HIS B 152      -8.532  -6.681  10.917  1.00103.16           O  
+ANISOU 4382  O   HIS B 152    13189   9893  16115   1692   2422   -271       O  
+ATOM   4383  CB  HIS B 152      -7.540  -4.090  11.784  1.00 95.08           C  
+ANISOU 4383  CB  HIS B 152    11646   9696  14786   1626   2509    -42       C  
+ATOM   4384  CG  HIS B 152      -6.473  -3.069  11.546  1.00 97.80           C  
+ANISOU 4384  CG  HIS B 152    11621  10338  15202   1702   2721   -200       C  
+ATOM   4385  ND1 HIS B 152      -6.359  -2.374  10.363  1.00 97.14           N  
+ANISOU 4385  ND1 HIS B 152    11506  10504  14897   1575   3143   -500       N  
+ATOM   4386  CD2 HIS B 152      -5.472  -2.625  12.344  1.00101.26           C  
+ANISOU 4386  CD2 HIS B 152    11715  10855  15903   1860   2549    -86       C  
+ATOM   4387  CE1 HIS B 152      -5.332  -1.544  10.439  1.00 97.91           C  
+ANISOU 4387  CE1 HIS B 152    11244  10829  15130   1640   3252   -560       C  
+ATOM   4388  NE2 HIS B 152      -4.779  -1.678  11.631  1.00106.83           N  
+ANISOU 4388  NE2 HIS B 152    12160  11858  16572   1822   2889   -322       N  
+ATOM   4389  N   GLY B 153     -10.495  -5.642  10.580  1.00 83.14           N  
+ANISOU 4389  N   GLY B 153    11040   7796  12752   1144   2528    -71       N  
+ATOM   4390  CA  GLY B 153     -11.282  -6.856  10.663  1.00 84.67           C  
+ANISOU 4390  CA  GLY B 153    11522   7604  13044   1076   2332     13       C  
+ATOM   4391  C   GLY B 153     -11.985  -6.956  12.004  1.00 86.82           C  
+ANISOU 4391  C   GLY B 153    11894   7876  13217    920   1998    492       C  
+ATOM   4392  O   GLY B 153     -11.962  -6.016  12.798  1.00 91.84           O  
+ANISOU 4392  O   GLY B 153    12400   8842  13652    855   1944    720       O  
+ATOM   4393  N   ASP B 154     -12.610  -8.101  12.253  1.00 92.88           N  
+ANISOU 4393  N   ASP B 154    12911   8269  14112    837   1783    635       N  
+ATOM   4394  CA  ASP B 154     -13.412  -8.311  13.453  1.00 97.62           C  
+ANISOU 4394  CA  ASP B 154    13662   8862  14567    609   1511   1090       C  
+ATOM   4395  C   ASP B 154     -13.025  -9.621  14.134  1.00 95.52           C  
+ANISOU 4395  C   ASP B 154    13525   8076  14690    734   1161   1292       C  
+ATOM   4396  O   ASP B 154     -12.545 -10.538  13.467  1.00106.63           O  
+ANISOU 4396  O   ASP B 154    14972   9068  16475    944   1138   1035       O  
+ATOM   4397  CB  ASP B 154     -14.903  -8.304  13.091  1.00102.75           C  
+ANISOU 4397  CB  ASP B 154    14524   9612  14904    246   1587   1134       C  
+ATOM   4398  CG  ASP B 154     -15.802  -8.475  14.296  1.00101.40           C  
+ANISOU 4398  CG  ASP B 154    14479   9491  14556    -40   1391   1576       C  
+ATOM   4399  OD1 ASP B 154     -15.938  -7.512  15.080  1.00 97.36           O  
+ANISOU 4399  OD1 ASP B 154    13846   9371  13774   -130   1422   1759       O  
+ATOM   4400  OD2 ASP B 154     -16.367  -9.575  14.465  1.00 99.64           O  
+ANISOU 4400  OD2 ASP B 154    14486   8913  14460   -193   1219   1729       O  
+ATOM   4401  N   VAL B 155     -13.195  -9.700  15.456  1.00 89.27           N  
+ANISOU 4401  N   VAL B 155    12817   7295  13807    606    881   1738       N  
+ATOM   4402  CA  VAL B 155     -12.806 -10.899  16.203  1.00 92.86           C  
+ANISOU 4402  CA  VAL B 155    13438   7235  14609    696    473   2002       C  
+ATOM   4403  C   VAL B 155     -13.575 -12.099  15.652  1.00107.19           C  
+ANISOU 4403  C   VAL B 155    15545   8607  16576    552    407   1958       C  
+ATOM   4404  O   VAL B 155     -13.063 -13.219  15.609  1.00116.71           O  
+ANISOU 4404  O   VAL B 155    16854   9258  18230    748    143   1935       O  
+ATOM   4405  CB  VAL B 155     -13.056 -10.743  17.724  1.00 94.11           C  
+ANISOU 4405  CB  VAL B 155    13731   7521  14503    472    196   2531       C  
+ATOM   4406  CG1 VAL B 155     -14.524 -10.446  18.014  1.00 97.98           C  
+ANISOU 4406  CG1 VAL B 155    14403   8318  14506      8    356   2736       C  
+ATOM   4407  CG2 VAL B 155     -12.593 -11.982  18.470  1.00 92.34           C  
+ANISOU 4407  CG2 VAL B 155    13723   6725  14637    553   -288   2837       C  
+ATOM   4408  N   GLU B 156     -14.806 -11.851  15.220  1.00111.45           N  
+ANISOU 4408  N   GLU B 156    16201   9370  16774    215    620   1934       N  
+ATOM   4409  CA  GLU B 156     -15.550 -12.836  14.461  1.00105.02           C  
+ANISOU 4409  CA  GLU B 156    15628   8183  16090     70    600   1804       C  
+ATOM   4410  C   GLU B 156     -15.089 -12.572  13.041  1.00113.22           C  
+ANISOU 4410  C   GLU B 156    16536   9253  17228    314    894   1247       C  
+ATOM   4411  O   GLU B 156     -14.971 -11.411  12.653  1.00116.54           O  
+ANISOU 4411  O   GLU B 156    16751  10145  17384    339   1176   1074       O  
+ATOM   4412  CB  GLU B 156     -17.062 -12.681  14.615  1.00 96.86           C  
+ANISOU 4412  CB  GLU B 156    14737   7377  14688   -407    677   2013       C  
+ATOM   4413  CG  GLU B 156     -17.548 -12.645  16.053  1.00103.50           C  
+ANISOU 4413  CG  GLU B 156    15667   8358  15302   -702    514   2540       C  
+ATOM   4414  CD  GLU B 156     -19.000 -12.225  16.158  1.00104.40           C  
+ANISOU 4414  CD  GLU B 156    15793   8823  15052  -1149    698   2662       C  
+ATOM   4415  OE1 GLU B 156     -19.468 -11.477  15.274  1.00100.61           O  
+ANISOU 4415  OE1 GLU B 156    15158   8640  14430  -1168    952   2358       O  
+ATOM   4416  OE2 GLU B 156     -19.675 -12.644  17.121  1.00106.30           O  
+ANISOU 4416  OE2 GLU B 156    16192   9038  15159  -1493    583   3062       O  
+ATOM   4417  N   HIS B 157     -14.816 -13.639  12.293  1.00112.44           N  
+ANISOU 4417  N   HIS B 157    16579   8648  17496    477    826    967       N  
+ATOM   4418  CA  HIS B 157     -14.284 -13.580  10.927  1.00114.93           C  
+ANISOU 4418  CA  HIS B 157    16821   8930  17916    712   1119    394       C  
+ATOM   4419  C   HIS B 157     -12.792 -13.251  11.040  1.00108.23           C  
+ANISOU 4419  C   HIS B 157    15642   8121  17360   1141   1193    214       C  
+ATOM   4420  O   HIS B 157     -12.350 -12.202  10.572  1.00103.72           O  
+ANISOU 4420  O   HIS B 157    14836   7983  16589   1215   1513     -5       O  
+ATOM   4421  CB  HIS B 157     -14.994 -12.525  10.068  1.00111.87           C  
+ANISOU 4421  CB  HIS B 157    16416   9041  17047    484   1455    202       C  
+ATOM   4422  CG  HIS B 157     -16.472 -12.725   9.956  1.00112.45           C  
+ANISOU 4422  CG  HIS B 157    16734   9122  16870     65   1371    366       C  
+ATOM   4423  ND1 HIS B 157     -17.371 -12.029  10.735  1.00102.42           N  
+ANISOU 4423  ND1 HIS B 157    15407   8224  15283   -241   1337    740       N  
+ATOM   4424  CD2 HIS B 157     -17.212 -13.526   9.153  1.00115.62           C  
+ANISOU 4424  CD2 HIS B 157    17410   9209  17312   -104   1315    186       C  
+ATOM   4425  CE1 HIS B 157     -18.600 -12.399  10.425  1.00107.50           C  
+ANISOU 4425  CE1 HIS B 157    16240   8788  15818   -578   1270    789       C  
+ATOM   4426  NE2 HIS B 157     -18.531 -13.305   9.466  1.00111.82           N  
+ANISOU 4426  NE2 HIS B 157    17001   8914  16571   -511   1234    471       N  
+ATOM   4427  N   PRO B 158     -12.014 -14.150  11.672  1.00110.85           N  
+ANISOU 4427  N   PRO B 158    15945   7980  18194   1411    868    319       N  
+ATOM   4428  CA  PRO B 158     -10.623 -13.885  12.071  1.00109.57           C  
+ANISOU 4428  CA  PRO B 158    15423   7824  18386   1805    822    250       C  
+ATOM   4429  C   PRO B 158      -9.667 -13.597  10.915  1.00120.40           C  
+ANISOU 4429  C   PRO B 158    16508   9288  19953   2119   1234   -359       C  
+ATOM   4430  O   PRO B 158      -8.769 -12.766  11.059  1.00123.73           O  
+ANISOU 4430  O   PRO B 158    16565  10026  20422   2299   1381   -430       O  
+ATOM   4431  CB  PRO B 158     -10.205 -15.181  12.783  1.00110.15           C  
+ANISOU 4431  CB  PRO B 158    15612   7225  19016   2003    318    450       C  
+ATOM   4432  CG  PRO B 158     -11.473 -15.921  13.057  1.00110.68           C  
+ANISOU 4432  CG  PRO B 158    16119   7040  18894   1618     90    776       C  
+ATOM   4433  CD  PRO B 158     -12.402 -15.540  11.959  1.00109.33           C  
+ANISOU 4433  CD  PRO B 158    16067   7155  18320   1361    487    483       C  
+ATOM   4434  N   SER B 159      -9.861 -14.272   9.787  1.00124.31           N  
+ANISOU 4434  N   SER B 159    17175   9515  20544   2158   1427   -799       N  
+ATOM   4435  CA  SER B 159      -8.934 -14.178   8.663  1.00121.26           C  
+ANISOU 4435  CA  SER B 159    16556   9164  20354   2446   1850  -1424       C  
+ATOM   4436  C   SER B 159      -8.967 -12.811   7.986  1.00118.93           C  
+ANISOU 4436  C   SER B 159    16130   9530  19526   2266   2324  -1586       C  
+ATOM   4437  O   SER B 159      -8.007 -12.416   7.325  1.00124.18           O  
+ANISOU 4437  O   SER B 159    16506  10370  20308   2474   2697  -1998       O  
+ATOM   4438  CB  SER B 159      -9.236 -15.273   7.638  1.00126.61           C  
+ANISOU 4438  CB  SER B 159    17530   9380  21197   2490   1929  -1865       C  
+ATOM   4439  OG  SER B 159     -10.532 -15.113   7.090  1.00131.01           O  
+ANISOU 4439  OG  SER B 159    18472  10099  21209   2067   2009  -1811       O  
+ATOM   4440  N   GLU B 160     -10.072 -12.092   8.152  1.00109.49           N  
+ANISOU 4440  N   GLU B 160    15140   8691  17769   1870   2305  -1264       N  
+ATOM   4441  CA  GLU B 160     -10.217 -10.774   7.548  1.00112.42           C  
+ANISOU 4441  CA  GLU B 160    15439   9644  17633   1671   2671  -1363       C  
+ATOM   4442  C   GLU B 160      -9.702  -9.684   8.482  1.00111.54           C  
+ANISOU 4442  C   GLU B 160    14996   9927  17456   1702   2623  -1049       C  
+ATOM   4443  O   GLU B 160      -8.622  -9.809   9.060  1.00111.09           O  
+ANISOU 4443  O   GLU B 160    14623   9762  17823   2005   2525  -1039       O  
+ATOM   4444  CB  GLU B 160     -11.679 -10.507   7.184  1.00112.05           C  
+ANISOU 4444  CB  GLU B 160    15750   9756  17067   1251   2647  -1219       C  
+ATOM   4445  N   ILE B 173      -3.469  -2.730   0.726  1.00120.01           N  
+ANISOU 4445  N   ILE B 173    14790  14113  16694    874   6063  -3318       N  
+ATOM   4446  CA  ILE B 173      -3.966  -3.796  -0.136  1.00129.68           C  
+ANISOU 4446  CA  ILE B 173    16376  15097  17799    880   6173  -3638       C  
+ATOM   4447  C   ILE B 173      -5.199  -3.341  -0.912  1.00126.54           C  
+ANISOU 4447  C   ILE B 173    16563  14789  16727    481   6145  -3539       C  
+ATOM   4448  O   ILE B 173      -5.187  -2.289  -1.553  1.00124.06           O  
+ANISOU 4448  O   ILE B 173    16377  14801  15958    150   6232  -3432       O  
+ATOM   4449  CB  ILE B 173      -4.314  -5.060   0.673  1.00123.93           C  
+ANISOU 4449  CB  ILE B 173    15628  13882  17577   1243   5939  -3681       C  
+ATOM   4450  N   LYS B 174      -6.262  -4.136  -0.847  1.00112.75           N  
+ANISOU 4450  N   LYS B 174    15178  12720  14942    509   5984  -3564       N  
+ATOM   4451  CA  LYS B 174      -7.514  -3.797  -1.511  1.00 93.12           C  
+ANISOU 4451  CA  LYS B 174    13250  10269  11864    145   5889  -3470       C  
+ATOM   4452  C   LYS B 174      -8.489  -3.184  -0.513  1.00 93.28           C  
+ANISOU 4452  C   LYS B 174    13347  10274  11819     79   5598  -3058       C  
+ATOM   4453  O   LYS B 174      -9.695  -3.426  -0.572  1.00100.27           O  
+ANISOU 4453  O   LYS B 174    14642  10982  12475    -61   5424  -2993       O  
+ATOM   4454  CB  LYS B 174      -8.129  -5.032  -2.171  1.00 96.14           C  
+ANISOU 4454  CB  LYS B 174    14023  10305  12201    167   5881  -3779       C  
+HETATM 4455  N   MSE B 175      -7.949  -2.393   0.408  1.00 88.22           N  
+ANISOU 4455  N   MSE B 175    12309   9825  11386    176   5541  -2793       N  
+HETATM 4456  CA  MSE B 175      -8.745  -1.700   1.413  1.00 82.15           C  
+ANISOU 4456  CA  MSE B 175    11543   9111  10559    122   5246  -2375       C  
+HETATM 4457  C   MSE B 175      -8.953  -0.245   1.007  1.00 78.23           C  
+ANISOU 4457  C   MSE B 175    11153   8985   9586   -221   5215  -2168       C  
+HETATM 4458  O   MSE B 175      -9.105   0.634   1.855  1.00 73.87           O  
+ANISOU 4458  O   MSE B 175    10432   8586   9047   -238   5030  -1847       O  
+HETATM 4459  CB  MSE B 175      -8.061  -1.777   2.779  1.00 96.40           C  
+ANISOU 4459  CB  MSE B 175    12857  10869  12902    444   5061  -2160       C  
+HETATM 4460  CG  MSE B 175      -7.979  -3.178   3.363  1.00108.73           C  
+ANISOU 4460  CG  MSE B 175    14332  12015  14965    769   4883  -2225       C  
+HETATM 4461 SE   MSE B 175      -9.715  -3.845   3.941  1.00186.87          SE  
+ANISOU 4461 SE   MSE B 175    24630  21636  24734    644   4351  -1877      SE  
+HETATM 4462  CE  MSE B 175     -10.066  -2.538   5.344  1.00 76.74           C  
+ANISOU 4462  CE  MSE B 175    10456   8014  10689    559   4009  -1313       C  
+ATOM   4463  N   ASP B 176      -8.964  -0.006  -0.300  1.00 86.26           N  
+ANISOU 4463  N   ASP B 176    12458  10120  10195   -496   5322  -2328       N  
+ATOM   4464  CA  ASP B 176      -8.965   1.345  -0.851  1.00 88.58           C  
+ANISOU 4464  CA  ASP B 176    12851  10715  10089   -815   5243  -2141       C  
+ATOM   4465  C   ASP B 176     -10.254   2.118  -0.577  1.00 86.05           C  
+ANISOU 4465  C   ASP B 176    12803  10419   9472  -1022   4900  -1823       C  
+ATOM   4466  O   ASP B 176     -10.209   3.304  -0.249  1.00 76.09           O  
+ANISOU 4466  O   ASP B 176    11423   9355   8131  -1125   4729  -1561       O  
+ATOM   4467  CB  ASP B 176      -8.708   1.296  -2.358  1.00 89.47           C  
+ANISOU 4467  CB  ASP B 176    13260  10900   9834  -1065   5448  -2391       C  
+ATOM   4468  CG  ASP B 176      -8.380   2.657  -2.936  1.00109.77           C  
+ANISOU 4468  CG  ASP B 176    15876  13753  12079  -1363   5421  -2220       C  
+ATOM   4469  OD1 ASP B 176      -7.746   3.467  -2.226  1.00103.40           O  
+ANISOU 4469  OD1 ASP B 176    14709  13110  11469  -1292   5377  -2030       O  
+ATOM   4470  OD2 ASP B 176      -8.752   2.918  -4.099  1.00125.52           O  
+ANISOU 4470  OD2 ASP B 176    18285  15785  13624  -1677   5427  -2274       O  
+ATOM   4471  N   PRO B 177     -11.409   1.451  -0.723  1.00 68.78           N  
+ANISOU 4471  N   PRO B 177     7452  10955   7726    730   1333  -2213       N  
+ATOM   4472  CA  PRO B 177     -12.711   2.080  -0.471  1.00 67.08           C  
+ANISOU 4472  CA  PRO B 177     7435  10580   7473    675   1325  -1944       C  
+ATOM   4473  C   PRO B 177     -12.847   2.626   0.952  1.00 58.76           C  
+ANISOU 4473  C   PRO B 177     6618   9158   6552    605   1352  -1551       C  
+ATOM   4474  O   PRO B 177     -13.422   3.702   1.153  1.00 56.17           O  
+ANISOU 4474  O   PRO B 177     6471   8823   6046    512   1391  -1254       O  
+ATOM   4475  CB  PRO B 177     -13.698   0.936  -0.714  1.00 61.44           C  
+ANISOU 4475  CB  PRO B 177     6596   9674   7076    790   1213  -2229       C  
+ATOM   4476  N   TYR B 178     -12.300   1.900   1.922  1.00 57.85           N  
+ANISOU 4476  N   TYR B 178     6475   8757   6747    649   1324  -1556       N  
+ATOM   4477  CA  TYR B 178     -12.309   2.348   3.309  1.00 61.04           C  
+ANISOU 4477  CA  TYR B 178     7066   8874   7252    591   1348  -1211       C  
+ATOM   4478  C   TYR B 178     -11.471   3.611   3.471  1.00 64.29           C  
+ANISOU 4478  C   TYR B 178     7599   9474   7354    484   1442   -983       C  
+ATOM   4479  O   TYR B 178     -11.830   4.510   4.230  1.00 57.83           O  
+ANISOU 4479  O   TYR B 178     6962   8538   6471    410   1473   -691       O  
+ATOM   4480  CB  TYR B 178     -11.798   1.243   4.237  1.00 60.18           C  
+ANISOU 4480  CB  TYR B 178     6860   8476   7531    657   1288  -1257       C  
+ATOM   4481  CG  TYR B 178     -12.841   0.203   4.581  1.00 61.93           C  
+ANISOU 4481  CG  TYR B 178     7009   8382   8139    733   1185  -1307       C  
+ATOM   4482  CD1 TYR B 178     -12.953  -0.968   3.842  1.00 64.25           C  
+ANISOU 4482  CD1 TYR B 178     7066   8644   8700    841   1089  -1667       C  
+ATOM   4483  CD2 TYR B 178     -13.713   0.392   5.646  1.00 68.27           C  
+ANISOU 4483  CD2 TYR B 178     7957   8928   9055    700   1178  -1003       C  
+ATOM   4484  CE1 TYR B 178     -13.906  -1.920   4.153  1.00 65.63           C  
+ANISOU 4484  CE1 TYR B 178     7153   8505   9279    908    980  -1698       C  
+ATOM   4485  CE2 TYR B 178     -14.668  -0.555   5.965  1.00 63.99           C  
+ANISOU 4485  CE2 TYR B 178     7330   8105   8877    762   1083  -1011       C  
+ATOM   4486  CZ  TYR B 178     -14.759  -1.709   5.214  1.00 65.25           C  
+ANISOU 4486  CZ  TYR B 178     7256   8204   9332    865    980  -1347       C  
+ATOM   4487  OH  TYR B 178     -15.707  -2.656   5.523  1.00 76.59           O  
+ANISOU 4487  OH  TYR B 178     8586   9334  11180    926    870  -1343       O  
+ATOM   4488  N   ILE B 179     -10.352   3.668   2.755  1.00 62.14           N  
+ANISOU 4488  N   ILE B 179     7205   9495   6911    481   1481  -1131       N  
+ATOM   4489  CA  ILE B 179      -9.487   4.843   2.770  1.00 58.85           C  
+ANISOU 4489  CA  ILE B 179     6864   9276   6220    380   1561   -922       C  
+ATOM   4490  C   ILE B 179     -10.225   6.059   2.208  1.00 60.91           C  
+ANISOU 4490  C   ILE B 179     7228   9704   6210    286   1589   -714       C  
+ATOM   4491  O   ILE B 179     -10.149   7.158   2.765  1.00 60.19           O  
+ANISOU 4491  O   ILE B 179     7277   9553   6039    195   1621   -426       O  
+ATOM   4492  CB  ILE B 179      -8.191   4.598   1.968  1.00 57.09           C  
+ANISOU 4492  CB  ILE B 179     6454   9381   5857    397   1598  -1135       C  
+ATOM   4493  CG1 ILE B 179      -7.306   3.575   2.685  1.00 58.38           C  
+ANISOU 4493  CG1 ILE B 179     6525   9341   6317    471   1567  -1286       C  
+ATOM   4494  CG2 ILE B 179      -7.435   5.899   1.749  1.00 58.79           C  
+ANISOU 4494  CG2 ILE B 179     6721   9846   5769    283   1676   -894       C  
+ATOM   4495  CD1 ILE B 179      -7.050   3.900   4.141  1.00 57.45           C  
+ANISOU 4495  CD1 ILE B 179     6571   8912   6345    429   1572  -1000       C  
+ATOM   4496  N   LYS B 180     -10.952   5.846   1.112  1.00 53.38           N  
+ANISOU 4496  N   LYS B 180     6185   8955   5143    311   1565   -869       N  
+ATOM   4497  CA  LYS B 180     -11.778   6.890   0.512  1.00 58.09           C  
+ANISOU 4497  CA  LYS B 180     6854   9703   5514    225   1572   -669       C  
+ATOM   4498  C   LYS B 180     -12.796   7.411   1.521  1.00 56.42           C  
+ANISOU 4498  C   LYS B 180     6849   9125   5461    189   1549   -422       C  
+ATOM   4499  O   LYS B 180     -12.906   8.624   1.757  1.00 67.70           O  
+ANISOU 4499  O   LYS B 180     8388  10543   6792     88   1569   -140       O  
+ATOM   4500  CB  LYS B 180     -12.510   6.355  -0.724  1.00 54.70           C  
+ANISOU 4500  CB  LYS B 180     6285   9524   4976    279   1533   -913       C  
+ATOM   4501  CG  LYS B 180     -11.633   6.089  -1.936  1.00 56.24           C  
+ANISOU 4501  CG  LYS B 180     6246  10209   4913    299   1561  -1151       C  
+ATOM   4502  CD  LYS B 180     -12.415   5.340  -3.010  1.00 68.95           C  
+ANISOU 4502  CD  LYS B 180     7696  12037   6466    382   1505  -1472       C  
+ATOM   4503  CE  LYS B 180     -12.478   6.118  -4.315  1.00 84.17           C  
+ANISOU 4503  CE  LYS B 180     9510  14509   7963    305   1533  -1395       C  
+ATOM   4504  NZ  LYS B 180     -11.321   5.815  -5.203  1.00 78.42           N  
+ANISOU 4504  NZ  LYS B 180     8532  14280   6987    332   1578  -1637       N  
+ATOM   4505  N   ALA B 181     -13.528   6.475   2.121  1.00 52.41           N  
+ANISOU 4505  N   ALA B 181     6368   8321   5224    273   1500   -535       N  
+ATOM   4506  CA  ALA B 181     -14.554   6.804   3.103  1.00 53.12           C  
+ANISOU 4506  CA  ALA B 181     6626   8089   5469    254   1481   -334       C  
+ATOM   4507  C   ALA B 181     -13.991   7.607   4.274  1.00 51.95           C  
+ANISOU 4507  C   ALA B 181     6601   7799   5337    191   1520    -95       C  
+ATOM   4508  O   ALA B 181     -14.567   8.620   4.677  1.00 52.97           O  
+ANISOU 4508  O   ALA B 181     6854   7844   5430    122   1525    115       O  
+ATOM   4509  CB  ALA B 181     -15.221   5.533   3.609  1.00 55.95           C  
+ANISOU 4509  CB  ALA B 181     6948   8174   6137    357   1422   -479       C  
+ATOM   4510  N   LEU B 182     -12.861   7.155   4.810  1.00 51.94           N  
+ANISOU 4510  N   LEU B 182     6552   7777   5407    218   1538   -147       N  
+ATOM   4511  CA  LEU B 182     -12.229   7.829   5.938  1.00 52.29           C  
+ANISOU 4511  CA  LEU B 182     6690   7710   5466    169   1567     44       C  
+ATOM   4512  C   LEU B 182     -11.737   9.228   5.571  1.00 53.22           C  
+ANISOU 4512  C   LEU B 182     6845   8005   5372     65   1602    210       C  
+ATOM   4513  O   LEU B 182     -11.879  10.162   6.358  1.00 54.17           O  
+ANISOU 4513  O   LEU B 182     7068   8004   5510     10   1604    392       O  
+ATOM   4514  CB  LEU B 182     -11.072   6.991   6.485  1.00 58.78           C  
+ANISOU 4514  CB  LEU B 182     7431   8492   6411    221   1571    -52       C  
+ATOM   4515  CG  LEU B 182     -10.323   7.604   7.670  1.00 59.30           C  
+ANISOU 4515  CG  LEU B 182     7577   8470   6485    178   1595    122       C  
+ATOM   4516  CD1 LEU B 182     -11.297   8.019   8.764  1.00 50.88           C  
+ANISOU 4516  CD1 LEU B 182     6636   7204   5494    164   1581    289       C  
+ATOM   4517  CD2 LEU B 182      -9.305   6.625   8.217  1.00 51.97           C  
+ANISOU 4517  CD2 LEU B 182     6555   7482   5709    234   1584     33       C  
+ATOM   4518  N   SER B 183     -11.146   9.367   4.388  1.00 47.29           N  
+ANISOU 4518  N   SER B 183     5983   7551   4435     39   1623    146       N  
+ATOM   4519  CA  SER B 183     -10.682  10.672   3.927  1.00 46.78           C  
+ANISOU 4519  CA  SER B 183     5912   7670   4191    -69   1644    346       C  
+ATOM   4520  C   SER B 183     -11.847  11.656   3.845  1.00 51.78           C  
+ANISOU 4520  C   SER B 183     6633   8222   4819   -137   1610    537       C  
+ATOM   4521  O   SER B 183     -11.782  12.773   4.384  1.00 58.11           O  
+ANISOU 4521  O   SER B 183     7498   8919   5664   -212   1598    739       O  
+ATOM   4522  CB  SER B 183      -9.994  10.549   2.567  1.00 48.09           C  
+ANISOU 4522  CB  SER B 183     5910   8232   4131    -85   1672    255       C  
+ATOM   4523  OG  SER B 183      -8.786   9.816   2.675  1.00 69.97           O  
+ANISOU 4523  OG  SER B 183     8588  11081   6918    -32   1705     86       O  
+ATOM   4524  N   GLY B 184     -12.918  11.224   3.182  1.00 47.20           N  
+ANISOU 4524  N   GLY B 184     6042   7675   4218   -107   1583    453       N  
+ATOM   4525  CA  GLY B 184     -14.118  12.034   3.065  1.00 47.12           C  
+ANISOU 4525  CA  GLY B 184     6106   7573   4225   -164   1543    614       C  
+ATOM   4526  C   GLY B 184     -14.672  12.434   4.421  1.00 54.79           C  
+ANISOU 4526  C   GLY B 184     7218   8202   5398   -162   1527    707       C  
+ATOM   4527  O   GLY B 184     -15.008  13.602   4.654  1.00 55.91           O  
+ANISOU 4527  O   GLY B 184     7405   8259   5578   -240   1499    893       O  
+ATOM   4528  N   ASP B 185     -14.760  11.459   5.321  1.00 46.13           N  
+ANISOU 4528  N   ASP B 185     6163   6922   4440    -74   1536    577       N  
+ATOM   4529  CA  ASP B 185     -15.272  11.697   6.664  1.00 45.82           C  
+ANISOU 4529  CA  ASP B 185     6230   6623   4557    -62   1528    648       C  
+ATOM   4530  C   ASP B 185     -14.417  12.711   7.417  1.00 45.19           C  
+ANISOU 4530  C   ASP B 185     6172   6518   4479   -119   1538    767       C  
+ATOM   4531  O   ASP B 185     -14.938  13.557   8.142  1.00 51.35           O  
+ANISOU 4531  O   ASP B 185     7013   7158   5339   -151   1516    856       O  
+ATOM   4532  CB  ASP B 185     -15.339  10.389   7.452  1.00 57.03           C  
+ANISOU 4532  CB  ASP B 185     7647   7905   6116     36   1533    528       C  
+ATOM   4533  CG  ASP B 185     -16.565   9.567   7.113  1.00 59.07           C  
+ANISOU 4533  CG  ASP B 185     7901   8074   6469     93   1502    444       C  
+ATOM   4534  OD1 ASP B 185     -17.411  10.053   6.333  1.00 56.18           O  
+ANISOU 4534  OD1 ASP B 185     7554   7751   6042     59   1481    471       O  
+ATOM   4535  OD2 ASP B 185     -16.684   8.437   7.631  1.00 52.32           O  
+ANISOU 4535  OD2 ASP B 185     7010   7099   5771    170   1490    366       O  
+ATOM   4536  N   LEU B 186     -13.102  12.623   7.243  1.00 44.46           N  
+ANISOU 4536  N   LEU B 186     6015   6563   4314   -128   1565    745       N  
+ATOM   4537  CA  LEU B 186     -12.186  13.551   7.893  1.00 45.20           C  
+ANISOU 4537  CA  LEU B 186     6112   6638   4424   -179   1566    845       C  
+ATOM   4538  C   LEU B 186     -12.286  14.945   7.292  1.00 57.17           C  
+ANISOU 4538  C   LEU B 186     7600   8204   5920   -283   1530   1017       C  
+ATOM   4539  O   LEU B 186     -11.938  15.933   7.940  1.00 55.75           O  
+ANISOU 4539  O   LEU B 186     7422   7929   5831   -328   1502   1105       O  
+ATOM   4540  CB  LEU B 186     -10.748  13.043   7.804  1.00 43.08           C  
+ANISOU 4540  CB  LEU B 186     5771   6503   4095   -161   1603    779       C  
+ATOM   4541  CG  LEU B 186     -10.395  11.935   8.795  1.00 45.23           C  
+ANISOU 4541  CG  LEU B 186     6057   6669   4459    -75   1618    665       C  
+ATOM   4542  CD1 LEU B 186      -9.073  11.301   8.430  1.00 50.18           C  
+ANISOU 4542  CD1 LEU B 186     6589   7436   5039    -54   1647    573       C  
+ATOM   4543  CD2 LEU B 186     -10.344  12.493  10.206  1.00 44.05           C  
+ANISOU 4543  CD2 LEU B 186     5972   6372   4392    -79   1604    735       C  
+ATOM   4544  N   VAL B 187     -12.755  15.033   6.052  1.00 44.53           N  
+ANISOU 4544  N   VAL B 187     5946   6754   4217   -323   1519   1069       N  
+ATOM   4545  CA  VAL B 187     -13.038  16.345   5.480  1.00 49.91           C  
+ANISOU 4545  CA  VAL B 187     6581   7463   4919   -430   1466   1281       C  
+ATOM   4546  C   VAL B 187     -14.339  16.927   6.042  1.00 48.53           C  
+ANISOU 4546  C   VAL B 187     6485   7043   4911   -439   1412   1321       C  
+ATOM   4547  O   VAL B 187     -14.405  18.114   6.370  1.00 50.67           O  
+ANISOU 4547  O   VAL B 187     6732   7188   5331   -506   1353   1450       O  
+ATOM   4548  CB  VAL B 187     -13.126  16.287   3.940  1.00 46.96           C  
+ANISOU 4548  CB  VAL B 187     6101   7386   4354   -479   1466   1356       C  
+ATOM   4549  CG1 VAL B 187     -13.644  17.606   3.381  1.00 47.58           C  
+ANISOU 4549  CG1 VAL B 187     6119   7467   4491   -597   1392   1623       C  
+ATOM   4550  CG2 VAL B 187     -11.767  15.956   3.346  1.00 46.76           C  
+ANISOU 4550  CG2 VAL B 187     5963   7647   4158   -486   1518   1333       C  
+ATOM   4551  N   SER B 188     -15.361  16.087   6.183  1.00 49.51           N  
+ANISOU 4551  N   SER B 188     6683   7088   5041   -367   1424   1197       N  
+ATOM   4552  CA  SER B 188     -16.705  16.585   6.486  1.00 47.42           C  
+ANISOU 4552  CA  SER B 188     6476   6630   4910   -378   1376   1234       C  
+ATOM   4553  C   SER B 188     -17.138  16.448   7.950  1.00 54.68           C  
+ANISOU 4553  C   SER B 188     7478   7333   5965   -313   1385   1131       C  
+ATOM   4554  O   SER B 188     -17.902  17.274   8.449  1.00 50.62           O  
+ANISOU 4554  O   SER B 188     6980   6662   5591   -337   1339   1164       O  
+ATOM   4555  CB  SER B 188     -17.731  15.888   5.589  1.00 50.34           C  
+ANISOU 4555  CB  SER B 188     6857   7065   5206   -352   1372   1191       C  
+ATOM   4556  OG  SER B 188     -17.499  16.188   4.223  1.00 55.60           O  
+ANISOU 4556  OG  SER B 188     7424   7975   5724   -423   1353   1303       O  
+ATOM   4557  N   LYS B 189     -16.654  15.418   8.638  1.00 49.76           N  
+ANISOU 4557  N   LYS B 189     6882   6721   5304   -233   1438   1011       N  
+ATOM   4558  CA  LYS B 189     -17.085  15.159  10.011  1.00 43.02           C  
+ANISOU 4558  CA  LYS B 189     6081   5729   4537   -172   1451    940       C  
+ATOM   4559  C   LYS B 189     -15.977  15.444  11.023  1.00 49.39           C  
+ANISOU 4559  C   LYS B 189     6866   6550   5349   -165   1463    918       C  
+ATOM   4560  O   LYS B 189     -14.802  15.198  10.754  1.00 54.72           O  
+ANISOU 4560  O   LYS B 189     7504   7331   5955   -171   1484    918       O  
+ATOM   4561  CB  LYS B 189     -17.549  13.707  10.160  1.00 48.00           C  
+ANISOU 4561  CB  LYS B 189     6734   6346   5159    -87   1484    858       C  
+ATOM   4562  CG  LYS B 189     -18.592  13.259   9.145  1.00 51.51           C  
+ANISOU 4562  CG  LYS B 189     7186   6780   5604    -79   1467    844       C  
+ATOM   4563  CD  LYS B 189     -18.963  11.796   9.360  1.00 62.81           C  
+ANISOU 4563  CD  LYS B 189     8608   8164   7091     11   1482    757       C  
+ATOM   4564  CE  LYS B 189     -19.767  11.240   8.194  1.00 54.97           C  
+ANISOU 4564  CE  LYS B 189     7596   7191   6099     28   1456    698       C  
+ATOM   4565  NZ  LYS B 189     -21.139  11.807   8.131  1.00 76.65           N  
+ANISOU 4565  NZ  LYS B 189    10395   9826   8902      4   1427    755       N  
+ATOM   4566  N   THR B 190     -16.357  15.964  12.187  1.00 49.53           N  
+ANISOU 4566  N   THR B 190     6894   6481   5444   -149   1448    881       N  
+ATOM   4567  CA  THR B 190     -15.407  16.211  13.269  1.00 42.50           C  
+ANISOU 4567  CA  THR B 190     5973   5625   4551   -132   1453    834       C  
+ATOM   4568  C   THR B 190     -15.148  14.946  14.079  1.00 45.53           C  
+ANISOU 4568  C   THR B 190     6365   6069   4865    -56   1502    799       C  
+ATOM   4569  O   THR B 190     -16.065  14.379  14.674  1.00 49.44           O  
+ANISOU 4569  O   THR B 190     6876   6539   5370    -10   1517    790       O  
+ATOM   4570  CB  THR B 190     -15.897  17.319  14.214  1.00 44.97           C  
+ANISOU 4570  CB  THR B 190     6255   5861   4969   -138   1407    769       C  
+ATOM   4571  OG1 THR B 190     -15.978  18.559  13.500  1.00 46.47           O  
+ANISOU 4571  OG1 THR B 190     6401   5964   5290   -215   1338    822       O  
+ATOM   4572  CG2 THR B 190     -14.948  17.476  15.397  1.00 45.31           C  
+ANISOU 4572  CG2 THR B 190     6252   5979   4986   -107   1409    688       C  
+ATOM   4573  N   PHE B 191     -13.892  14.513  14.101  1.00 41.07           N  
+ANISOU 4573  N   PHE B 191     5773   5583   4248    -49   1521    799       N  
+ATOM   4574  CA  PHE B 191     -13.517  13.267  14.758  1.00 49.93           C  
+ANISOU 4574  CA  PHE B 191     6877   6751   5343     12   1552    796       C  
+ATOM   4575  C   PHE B 191     -13.023  13.454  16.189  1.00 47.12           C  
+ANISOU 4575  C   PHE B 191     6485   6461   4957     36   1550    782       C  
+ATOM   4576  O   PHE B 191     -12.365  14.444  16.509  1.00 41.95           O  
+ANISOU 4576  O   PHE B 191     5809   5833   4296      7   1527    741       O  
+ATOM   4577  CB  PHE B 191     -12.432  12.559  13.946  1.00 48.38           C  
+ANISOU 4577  CB  PHE B 191     6650   6609   5125     13   1568    789       C  
+ATOM   4578  CG  PHE B 191     -12.964  11.715  12.828  1.00 48.20           C  
+ANISOU 4578  CG  PHE B 191     6623   6569   5120     31   1574    764       C  
+ATOM   4579  CD1 PHE B 191     -13.513  12.302  11.700  1.00 50.85           C  
+ANISOU 4579  CD1 PHE B 191     6978   6916   5425    -13   1564    768       C  
+ATOM   4580  CD2 PHE B 191     -12.898  10.335  12.897  1.00 41.84           C  
+ANISOU 4580  CD2 PHE B 191     5770   5741   4385     93   1577    733       C  
+ATOM   4581  CE1 PHE B 191     -13.997  11.525  10.666  1.00 52.98           C  
+ANISOU 4581  CE1 PHE B 191     7228   7206   5695     10   1563    715       C  
+ATOM   4582  CE2 PHE B 191     -13.379   9.553  11.866  1.00 45.60           C  
+ANISOU 4582  CE2 PHE B 191     6218   6200   4908    120   1569    663       C  
+ATOM   4583  CZ  PHE B 191     -13.930  10.148  10.749  1.00 45.53           C  
+ANISOU 4583  CZ  PHE B 191     6237   6235   4829     82   1565    641       C  
+ATOM   4584  N   LEU B 192     -13.352  12.492  17.045  1.00 48.63           N  
+ANISOU 4584  N   LEU B 192     6649   6690   5138     87   1565    825       N  
+ATOM   4585  CA  LEU B 192     -12.694  12.360  18.337  1.00 41.79           C  
+ANISOU 4585  CA  LEU B 192     5723   5947   4211    112   1565    841       C  
+ATOM   4586  C   LEU B 192     -11.891  11.067  18.359  1.00 50.17           C  
+ANISOU 4586  C   LEU B 192     6736   7022   5305    138   1570    920       C  
+ATOM   4587  O   LEU B 192     -12.460   9.975  18.362  1.00 68.36           O  
+ANISOU 4587  O   LEU B 192     9007   9282   7684    169   1570   1002       O  
+ATOM   4588  CB  LEU B 192     -13.708  12.377  19.483  1.00 49.53           C  
+ANISOU 4588  CB  LEU B 192     6665   7015   5140    143   1570    862       C  
+ATOM   4589  CG  LEU B 192     -13.181  11.961  20.862  1.00 51.98           C  
+ANISOU 4589  CG  LEU B 192     6881   7517   5353    173   1571    920       C  
+ATOM   4590  CD1 LEU B 192     -12.022  12.849  21.297  1.00 42.03           C  
+ANISOU 4590  CD1 LEU B 192     5597   6344   4030    159   1548    813       C  
+ATOM   4591  CD2 LEU B 192     -14.294  11.984  21.899  1.00 50.16           C  
+ANISOU 4591  CD2 LEU B 192     6589   7429   5040    200   1583    947       C  
+ATOM   4592  N   PHE B 193     -10.570  11.191  18.375  1.00 47.47           N  
+ANISOU 4592  N   PHE B 193     6371   6723   4941    125   1564    895       N  
+ATOM   4593  CA  PHE B 193      -9.708  10.027  18.505  1.00 41.22           C  
+ANISOU 4593  CA  PHE B 193     5514   5941   4208    150   1558    959       C  
+ATOM   4594  C   PHE B 193      -9.528   9.696  19.980  1.00 41.72           C  
+ANISOU 4594  C   PHE B 193     5498   6135   4218    172   1544   1059       C  
+ATOM   4595  O   PHE B 193      -9.163  10.557  20.779  1.00 46.39           O  
+ANISOU 4595  O   PHE B 193     6081   6850   4696    164   1538   1014       O  
+ATOM   4596  CB  PHE B 193      -8.353  10.269  17.836  1.00 41.53           C  
+ANISOU 4596  CB  PHE B 193     5551   5980   4248    125   1561    890       C  
+ATOM   4597  CG  PHE B 193      -8.420  10.353  16.335  1.00 41.69           C  
+ANISOU 4597  CG  PHE B 193     5607   5938   4297    104   1577    819       C  
+ATOM   4598  CD1 PHE B 193      -8.904  11.491  15.709  1.00 40.68           C  
+ANISOU 4598  CD1 PHE B 193     5538   5800   4118     60   1581    786       C  
+ATOM   4599  CD2 PHE B 193      -7.998   9.293  15.549  1.00 44.14           C  
+ANISOU 4599  CD2 PHE B 193     5862   6217   4691    129   1579    781       C  
+ATOM   4600  CE1 PHE B 193      -8.965  11.570  14.330  1.00 47.57           C  
+ANISOU 4600  CE1 PHE B 193     6420   6670   4984     33   1593    751       C  
+ATOM   4601  CE2 PHE B 193      -8.057   9.365  14.169  1.00 45.95           C  
+ANISOU 4601  CE2 PHE B 193     6097   6457   4905    113   1595    695       C  
+ATOM   4602  CZ  PHE B 193      -8.541  10.505  13.559  1.00 45.76           C  
+ANISOU 4602  CZ  PHE B 193     6137   6460   4790     62   1605    698       C  
+ATOM   4603  N   VAL B 194      -9.799   8.449  20.344  1.00 42.60           N  
+ANISOU 4603  N   VAL B 194     5529   6232   4425    200   1528   1200       N  
+ATOM   4604  CA  VAL B 194      -9.678   8.030  21.733  1.00 44.13           C  
+ANISOU 4604  CA  VAL B 194     5617   6590   4562    213   1508   1353       C  
+ATOM   4605  C   VAL B 194      -9.291   6.555  21.807  1.00 51.42           C  
+ANISOU 4605  C   VAL B 194     6422   7439   5678    230   1466   1520       C  
+ATOM   4606  O   VAL B 194      -9.742   5.739  21.002  1.00 48.27           O  
+ANISOU 4606  O   VAL B 194     6005   6861   5472    247   1450   1529       O  
+ATOM   4607  CB  VAL B 194     -10.994   8.291  22.516  1.00 43.51           C  
+ANISOU 4607  CB  VAL B 194     5518   6632   4380    223   1524   1417       C  
+ATOM   4608  CG1 VAL B 194     -12.157   7.512  21.913  1.00 50.87           C  
+ANISOU 4608  CG1 VAL B 194     6452   7409   5467    237   1525   1495       C  
+ATOM   4609  CG2 VAL B 194     -10.824   7.977  23.996  1.00 65.91           C  
+ANISOU 4609  CG2 VAL B 194     8220   9727   7097    231   1508   1582       C  
+ATOM   4610  N   GLY B 195      -8.437   6.223  22.770  1.00 47.65           N  
+ANISOU 4610  N   GLY B 195     5843   7093   5170    227   1435   1643       N  
+ATOM   4611  CA  GLY B 195      -7.948   4.866  22.922  1.00 54.59           C  
+ANISOU 4611  CA  GLY B 195     6578   7889   6273    236   1376   1820       C  
+ATOM   4612  C   GLY B 195      -6.635   4.646  22.195  1.00 62.42           C  
+ANISOU 4612  C   GLY B 195     7572   8759   7385    236   1358   1697       C  
+ATOM   4613  O   GLY B 195      -6.196   3.509  22.025  1.00 72.22           O  
+ANISOU 4613  O   GLY B 195     8692   9869   8880    250   1300   1779       O  
+ATOM   4614  N   PHE B 196      -6.006   5.737  21.768  1.00 67.54           N  
+ANISOU 4614  N   PHE B 196     8339   9447   7877    221   1401   1502       N  
+ATOM   4615  CA  PHE B 196      -4.706   5.664  21.105  1.00 58.70           C  
+ANISOU 4615  CA  PHE B 196     7217   8254   6833    217   1396   1383       C  
+ATOM   4616  C   PHE B 196      -3.582   6.256  21.950  1.00 51.72           C  
+ANISOU 4616  C   PHE B 196     6319   7520   5812    198   1387   1395       C  
+ATOM   4617  O   PHE B 196      -3.695   7.367  22.469  1.00 62.00           O  
+ANISOU 4617  O   PHE B 196     7685   8961   6910    184   1410   1340       O  
+ATOM   4618  CB  PHE B 196      -4.745   6.376  19.748  1.00 56.72           C  
+ANISOU 4618  CB  PHE B 196     7082   7928   6541    207   1446   1169       C  
+ATOM   4619  CG  PHE B 196      -5.612   5.699  18.724  1.00 52.74           C  
+ANISOU 4619  CG  PHE B 196     6572   7283   6183    231   1446   1114       C  
+ATOM   4620  CD1 PHE B 196      -5.153   4.582  18.045  1.00 54.79           C  
+ANISOU 4620  CD1 PHE B 196     6725   7421   6670    261   1410   1055       C  
+ATOM   4621  CD2 PHE B 196      -6.873   6.187  18.424  1.00 56.83           C  
+ANISOU 4621  CD2 PHE B 196     7176   7790   6628    227   1473   1094       C  
+ATOM   4622  CE1 PHE B 196      -5.938   3.956  17.098  1.00 57.01           C  
+ANISOU 4622  CE1 PHE B 196     6980   7585   7097    292   1398    962       C  
+ATOM   4623  CE2 PHE B 196      -7.663   5.565  17.475  1.00 50.44           C  
+ANISOU 4623  CE2 PHE B 196     6355   6859   5952    252   1466   1030       C  
+ATOM   4624  CZ  PHE B 196      -7.192   4.448  16.812  1.00 54.81           C  
+ANISOU 4624  CZ  PHE B 196     6796   7305   6724    287   1427    956       C  
+ATOM   4625  N   SER B 197      -2.498   5.499  22.078  1.00 56.37           N  
+ANISOU 4625  N   SER B 197     6809   8071   6540    201   1345   1448       N  
+ATOM   4626  CA  SER B 197      -1.290   5.975  22.740  1.00 58.10           C  
+ANISOU 4626  CA  SER B 197     7009   8409   6658    186   1330   1444       C  
+ATOM   4627  C   SER B 197      -0.161   6.051  21.719  1.00 68.68           C  
+ANISOU 4627  C   SER B 197     8369   9638   8086    180   1346   1279       C  
+ATOM   4628  O   SER B 197      -0.340   5.672  20.562  1.00 55.29           O  
+ANISOU 4628  O   SER B 197     6684   7810   6512    192   1367   1170       O  
+ATOM   4629  CB  SER B 197      -0.906   5.061  23.906  1.00 61.61           C  
+ANISOU 4629  CB  SER B 197     7295   8938   7175    187   1259   1681       C  
+ATOM   4630  OG  SER B 197      -0.646   3.742  23.459  1.00 82.00           O  
+ANISOU 4630  OG  SER B 197     9758  11330  10068    200   1206   1759       O  
+ATOM   4631  N   PHE B 198       1.000   6.542  22.142  1.00 83.05           N  
+ANISOU 4631  N   PHE B 198    10181  11537   9838    165   1336   1251       N  
+ATOM   4632  CA  PHE B 198       2.114   6.750  21.220  1.00 67.91           C  
+ANISOU 4632  CA  PHE B 198     8275   9550   7977    155   1359   1102       C  
+ATOM   4633  C   PHE B 198       2.753   5.439  20.771  1.00 62.45           C  
+ANISOU 4633  C   PHE B 198     7459   8730   7539    177   1324   1106       C  
+ATOM   4634  O   PHE B 198       3.573   5.424  19.852  1.00 65.72           O  
+ANISOU 4634  O   PHE B 198     7858   9098   8016    176   1349    960       O  
+ATOM   4635  CB  PHE B 198       3.165   7.670  21.852  1.00 57.72           C  
+ANISOU 4635  CB  PHE B 198     6999   8369   6565    134   1350   1074       C  
+ATOM   4636  CG  PHE B 198       3.800   7.122  23.098  1.00 61.63           C  
+ANISOU 4636  CG  PHE B 198     7388   8950   7080    140   1283   1221       C  
+ATOM   4637  CD1 PHE B 198       4.874   6.249  23.027  1.00 64.88           C  
+ANISOU 4637  CD1 PHE B 198     7696   9284   7672    143   1244   1257       C  
+ATOM   4638  CD2 PHE B 198       3.324   7.490  24.344  1.00 65.46           C  
+ANISOU 4638  CD2 PHE B 198     7857   9618   7398    142   1255   1318       C  
+ATOM   4639  CE1 PHE B 198       5.458   5.753  24.177  1.00 63.25           C  
+ANISOU 4639  CE1 PHE B 198     7378   9163   7490    142   1172   1422       C  
+ATOM   4640  CE2 PHE B 198       3.901   6.997  25.496  1.00 66.40           C  
+ANISOU 4640  CE2 PHE B 198     7859   9869   7504    142   1189   1476       C  
+ATOM   4641  CZ  PHE B 198       4.969   6.127  25.413  1.00 63.20           C  
+ANISOU 4641  CZ  PHE B 198     7357   9367   7290    139   1145   1545       C  
+ATOM   4642  N   THR B 199       2.375   4.341  21.415  1.00 61.38           N  
+ANISOU 4642  N   THR B 199     7209   8544   7568    195   1259   1275       N  
+ATOM   4643  CA  THR B 199       2.904   3.034  21.050  1.00 65.57           C  
+ANISOU 4643  CA  THR B 199     7583   8914   8415    220   1199   1277       C  
+ATOM   4644  C   THR B 199       2.011   2.329  20.033  1.00 67.41           C  
+ANISOU 4644  C   THR B 199     7784   8999   8828    254   1200   1174       C  
+ATOM   4645  O   THR B 199       2.284   1.192  19.646  1.00 70.57           O  
+ANISOU 4645  O   THR B 199     8028   9242   9543    285   1137   1133       O  
+ATOM   4646  CB  THR B 199       3.066   2.129  22.286  1.00 70.11           C  
+ANISOU 4646  CB  THR B 199     8002   9489   9149    215   1099   1552       C  
+ATOM   4647  OG1 THR B 199       1.870   2.175  23.075  1.00 64.39           O  
+ANISOU 4647  OG1 THR B 199     7289   8861   8314    208   1091   1748       O  
+ATOM   4648  CG2 THR B 199       4.238   2.593  23.135  1.00 68.81           C  
+ANISOU 4648  CG2 THR B 199     7826   9457   8862    189   1081   1614       C  
+ATOM   4649  N   ASP B 200       0.943   2.999  19.609  1.00 79.96           N  
+ANISOU 4649  N   ASP B 200     9504  10634  10243    250   1261   1118       N  
+ATOM   4650  CA  ASP B 200       0.029   2.418  18.630  1.00 75.80           C  
+ANISOU 4650  CA  ASP B 200     8954   9988   9859    284   1261   1006       C  
+ATOM   4651  C   ASP B 200       0.725   2.256  17.281  1.00 86.46           C  
+ANISOU 4651  C   ASP B 200    10263  11308  11279    306   1289    732       C  
+ATOM   4652  O   ASP B 200       1.302   3.208  16.756  1.00 78.32           O  
+ANISOU 4652  O   ASP B 200     9323  10400  10033    280   1360    618       O  
+ATOM   4653  CB  ASP B 200      -1.229   3.275  18.480  1.00 72.47           C  
+ANISOU 4653  CB  ASP B 200     8685   9635   9217    270   1320   1010       C  
+ATOM   4654  CG  ASP B 200      -2.311   2.583  17.671  1.00 84.48           C  
+ANISOU 4654  CG  ASP B 200    10169  11031  10898    307   1305    935       C  
+ATOM   4655  OD1 ASP B 200      -3.251   2.030  18.281  1.00 92.92           O  
+ANISOU 4655  OD1 ASP B 200    11191  12034  12080    318   1260   1104       O  
+ATOM   4656  OD2 ASP B 200      -2.215   2.578  16.426  1.00 84.52           O  
+ANISOU 4656  OD2 ASP B 200    10175  11024  10914    325   1334    710       O  
+ATOM   4657  N   PRO B 201       0.672   1.040  16.720  1.00 94.02           N  
+ANISOU 4657  N   PRO B 201    11056  12114  12553    357   1226    624       N  
+ATOM   4658  CA  PRO B 201       1.395   0.669  15.499  1.00 90.63           C  
+ANISOU 4658  CA  PRO B 201    10526  11684  12224    392   1238    328       C  
+ATOM   4659  C   PRO B 201       0.744   1.121  14.190  1.00 81.89           C  
+ANISOU 4659  C   PRO B 201     9487  10684  10945    404   1309    109       C  
+ATOM   4660  O   PRO B 201       1.409   1.067  13.155  1.00 84.94           O  
+ANISOU 4660  O   PRO B 201     9799  11167  11308    424   1341   -137       O  
+ATOM   4661  CB  PRO B 201       1.417  -0.859  15.565  1.00 88.28           C  
+ANISOU 4661  CB  PRO B 201     9992  11162  12387    449   1116    296       C  
+ATOM   4662  CG  PRO B 201       0.185  -1.208  16.313  1.00 77.38           C  
+ANISOU 4662  CG  PRO B 201     8619   9672  11109    446   1062    538       C  
+ATOM   4663  CD  PRO B 201      -0.010  -0.117  17.328  1.00 85.28           C  
+ANISOU 4663  CD  PRO B 201     9807  10830  11767    384   1123    788       C  
+ATOM   4664  N   ASN B 202      -0.511   1.560  14.218  1.00 77.08           N  
+ANISOU 4664  N   ASN B 202     9000  10082  10206    392   1332    197       N  
+ATOM   4665  CA  ASN B 202      -1.231   1.775  12.964  1.00 77.09           C  
+ANISOU 4665  CA  ASN B 202     9029  10165  10095    408   1375      1       C  
+ATOM   4666  C   ASN B 202      -1.807   3.167  12.713  1.00 81.62           C  
+ANISOU 4666  C   ASN B 202     9799  10894  10318    349   1460     72       C  
+ATOM   4667  O   ASN B 202      -2.077   3.522  11.566  1.00 92.31           O  
+ANISOU 4667  O   ASN B 202    11165  12380  11529    347   1505    -79       O  
+ATOM   4668  CB  ASN B 202      -2.378   0.766  12.874  1.00 80.43           C  
+ANISOU 4668  CB  ASN B 202     9364  10412  10784    463   1299    -23       C  
+ATOM   4669  CG  ASN B 202      -1.910  -0.665  13.036  1.00 91.94           C  
+ANISOU 4669  CG  ASN B 202    10585  11674  12674    524   1188    -99       C  
+ATOM   4670  OD1 ASN B 202      -0.891  -1.064  12.473  1.00 95.95           O  
+ANISOU 4670  OD1 ASN B 202    10959  12215  13284    553   1177   -316       O  
+ATOM   4671  ND2 ASN B 202      -2.648  -1.445  13.818  1.00 91.73           N  
+ANISOU 4671  ND2 ASN B 202    10484  11442  12928    540   1098     90       N  
+ATOM   4672  N   LEU B 203      -1.986   3.954  13.768  1.00 67.15           N  
+ANISOU 4672  N   LEU B 203     8096   9061   8358    303   1474    294       N  
+ATOM   4673  CA  LEU B 203      -2.662   5.244  13.645  1.00 59.11           C  
+ANISOU 4673  CA  LEU B 203     7238   8139   7082    251   1530    362       C  
+ATOM   4674  C   LEU B 203      -1.941   6.192  12.683  1.00 81.06           C  
+ANISOU 4674  C   LEU B 203    10044  11093   9661    206   1593    272       C  
+ATOM   4675  O   LEU B 203      -2.566   6.815  11.820  1.00 85.19           O  
+ANISOU 4675  O   LEU B 203    10619  11707  10043    180   1627    240       O  
+ATOM   4676  CB  LEU B 203      -2.801   5.898  15.021  1.00 53.95           C  
+ANISOU 4676  CB  LEU B 203     6675   7472   6351    219   1523    564       C  
+ATOM   4677  CG  LEU B 203      -3.527   7.243  15.079  1.00 52.13           C  
+ANISOU 4677  CG  LEU B 203     6585   7306   5916    172   1560    621       C  
+ATOM   4678  CD1 LEU B 203      -4.966   7.086  14.616  1.00 53.84           C  
+ANISOU 4678  CD1 LEU B 203     6842   7468   6148    186   1560    611       C  
+ATOM   4679  CD2 LEU B 203      -3.479   7.816  16.486  1.00 62.88           C  
+ANISOU 4679  CD2 LEU B 203     7990   8689   7213    155   1544    756       C  
+ATOM   4680  N   ASP B 204      -0.622   6.274  12.821  1.00 84.78           N  
+ANISOU 4680  N   ASP B 204    10462  11620  10129    194   1603    252       N  
+ATOM   4681  CA  ASP B 204       0.190   7.185  12.019  1.00 76.44           C  
+ANISOU 4681  CA  ASP B 204     9406  10740   8898    143   1659    212       C  
+ATOM   4682  C   ASP B 204       0.181   6.818  10.534  1.00 66.13           C  
+ANISOU 4682  C   ASP B 204     7998   9591   7536    161   1692     24       C  
+ATOM   4683  O   ASP B 204       0.154   7.694   9.670  1.00 63.96           O  
+ANISOU 4683  O   ASP B 204     7740   9496   7068    109   1739     42       O  
+ATOM   4684  CB  ASP B 204       1.626   7.202  12.551  1.00 80.01           C  
+ANISOU 4684  CB  ASP B 204     9805  11203   9391    134   1656    226       C  
+ATOM   4685  CG  ASP B 204       2.495   8.229  11.857  1.00 87.90           C  
+ANISOU 4685  CG  ASP B 204    10796  12377  10226     74   1710    231       C  
+ATOM   4686  OD1 ASP B 204       1.951   9.247  11.381  1.00 84.82           O  
+ANISOU 4686  OD1 ASP B 204    10471  12066   9692     20   1735    309       O  
+ATOM   4687  OD2 ASP B 204       3.724   8.020  11.794  1.00109.29           O  
+ANISOU 4687  OD2 ASP B 204    13415  15139  12969     76   1721    175       O  
+ATOM   4688  N   TYR B 205       0.199   5.520  10.247  1.00 62.60           N  
+ANISOU 4688  N   TYR B 205     7422   9091   7273    235   1658   -156       N  
+ATOM   4689  CA  TYR B 205       0.109   5.017   8.878  1.00 68.98           C  
+ANISOU 4689  CA  TYR B 205     8099  10067   8043    272   1676   -397       C  
+ATOM   4690  C   TYR B 205      -1.214   5.388   8.212  1.00 79.91           C  
+ANISOU 4690  C   TYR B 205     9552  11514   9297    260   1687   -387       C  
+ATOM   4691  O   TYR B 205      -1.245   6.006   7.134  1.00 84.64           O  
+ANISOU 4691  O   TYR B 205    10127  12365   9667    223   1737   -426       O  
+ATOM   4692  CB  TYR B 205       0.288   3.496   8.882  1.00 73.18           C  
+ANISOU 4692  CB  TYR B 205     8457  10465   8883    365   1608   -613       C  
+ATOM   4693  CG  TYR B 205      -0.049   2.807   7.579  1.00 84.23           C  
+ANISOU 4693  CG  TYR B 205     9698  12011  10297    427   1602   -920       C  
+ATOM   4694  CD1 TYR B 205       0.791   2.899   6.478  1.00 92.83           C  
+ANISOU 4694  CD1 TYR B 205    10648  13404  11219    431   1657  -1131       C  
+ATOM   4695  CD2 TYR B 205      -1.207   2.047   7.458  1.00 80.77           C  
+ANISOU 4695  CD2 TYR B 205     9225  11426  10038    486   1537  -1009       C  
+ATOM   4696  CE1 TYR B 205       0.483   2.261   5.288  1.00 90.14           C  
+ANISOU 4696  CE1 TYR B 205    10134  13250  10866    496   1648  -1450       C  
+ATOM   4697  CE2 TYR B 205      -1.523   1.406   6.275  1.00 78.33           C  
+ANISOU 4697  CE2 TYR B 205     8751  11259   9751    552   1519  -1328       C  
+ATOM   4698  CZ  TYR B 205      -0.676   1.515   5.193  1.00 90.04           C  
+ANISOU 4698  CZ  TYR B 205    10092  13075  11043    560   1575  -1561       C  
+ATOM   4699  OH  TYR B 205      -0.990   0.878   4.014  1.00 97.82           O  
+ANISOU 4699  OH  TYR B 205    10888  14256  12024    633   1555  -1914       O  
+ATOM   4700  N   ILE B 206      -2.302   5.020   8.882  1.00 75.22           N  
+ANISOU 4700  N   ILE B 206     9032  10702   8848    286   1637   -310       N  
+ATOM   4701  CA  ILE B 206      -3.645   5.294   8.398  1.00 69.30           C  
+ANISOU 4701  CA  ILE B 206     8352   9963   8015    280   1636   -292       C  
+ATOM   4702  C   ILE B 206      -3.819   6.784   8.147  1.00 71.44           C  
+ANISOU 4702  C   ILE B 206     8748  10376   8022    188   1689   -116       C  
+ATOM   4703  O   ILE B 206      -4.270   7.192   7.076  1.00 64.09           O  
+ANISOU 4703  O   ILE B 206     7799   9629   6924    163   1712   -155       O  
+ATOM   4704  CB  ILE B 206      -4.711   4.812   9.399  1.00 62.87           C  
+ANISOU 4704  CB  ILE B 206     7607   8883   7397    310   1579   -177       C  
+ATOM   4705  CG1 ILE B 206      -4.631   3.295   9.578  1.00 64.40           C  
+ANISOU 4705  CG1 ILE B 206     7641   8910   7920    397   1503   -319       C  
+ATOM   4706  CG2 ILE B 206      -6.096   5.223   8.942  1.00 59.61           C  
+ANISOU 4706  CG2 ILE B 206     7280   8475   6892    297   1582   -143       C  
+ATOM   4707  CD1 ILE B 206      -5.540   2.760  10.666  1.00 60.97           C  
+ANISOU 4707  CD1 ILE B 206     7238   8228   7702    418   1442   -148       C  
+ATOM   4708  N   LEU B 207      -3.421   7.589   9.128  1.00 59.65           N  
+ANISOU 4708  N   LEU B 207     7355   8803   6508    137   1696     73       N  
+ATOM   4709  CA  LEU B 207      -3.508   9.041   9.014  1.00 55.03           C  
+ANISOU 4709  CA  LEU B 207     6859   8300   5750     50   1722    242       C  
+ATOM   4710  C   LEU B 207      -2.666   9.573   7.861  1.00 62.69           C  
+ANISOU 4710  C   LEU B 207     7734   9540   6547     -1   1768    223       C  
+ATOM   4711  O   LEU B 207      -3.069  10.512   7.174  1.00 67.68           O  
+ANISOU 4711  O   LEU B 207     8380  10299   7038    -69   1780    336       O  
+ATOM   4712  CB  LEU B 207      -3.083   9.706  10.320  1.00 55.60           C  
+ANISOU 4712  CB  LEU B 207     7014   8242   5870     21   1707    390       C  
+ATOM   4713  CG  LEU B 207      -4.090   9.579  11.461  1.00 65.31           C  
+ANISOU 4713  CG  LEU B 207     8338   9282   7197     47   1670    464       C  
+ATOM   4714  CD1 LEU B 207      -3.561  10.272  12.693  1.00 57.78           C  
+ANISOU 4714  CD1 LEU B 207     7432   8270   6251     24   1654    568       C  
+ATOM   4715  CD2 LEU B 207      -5.437  10.154  11.055  1.00 70.84           C  
+ANISOU 4715  CD2 LEU B 207     9112   9962   7841     23   1666    512       C  
+ATOM   4716  N   SER B 208      -1.495   8.980   7.656  1.00 58.88           N  
+ANISOU 4716  N   SER B 208     7135   9156   6081     27   1789     98       N  
+ATOM   4717  CA  SER B 208      -0.632   9.384   6.553  1.00 70.54           C  
+ANISOU 4717  CA  SER B 208     8488  10936   7376    -17   1840     73       C  
+ATOM   4718  C   SER B 208      -1.279   9.051   5.213  1.00 73.49           C  
+ANISOU 4718  C   SER B 208     8764  11555   7604     -1   1857    -62       C  
+ATOM   4719  O   SER B 208      -0.963   9.665   4.193  1.00 82.99           O  
+ANISOU 4719  O   SER B 208     9873  13068   8592    -60   1898     -7       O  
+ATOM   4720  CB  SER B 208       0.738   8.709   6.658  1.00 67.86           C  
+ANISOU 4720  CB  SER B 208     8031  10649   7104     22   1858    -67       C  
+ATOM   4721  OG  SER B 208       0.657   7.331   6.335  1.00 69.50           O  
+ANISOU 4721  OG  SER B 208     8124  10851   7433    118   1839   -341       O  
+ATOM   4722  N   ARG B 209      -2.193   8.084   5.221  1.00 64.20           N  
+ANISOU 4722  N   ARG B 209     7590  10256   6546     78   1819   -227       N  
+ATOM   4723  CA  ARG B 209      -2.890   7.701   3.995  1.00 60.03           C  
+ANISOU 4723  CA  ARG B 209     6962   9954   5895    106   1822   -393       C  
+ATOM   4724  C   ARG B 209      -4.231   8.419   3.799  1.00 59.19           C  
+ANISOU 4724  C   ARG B 209     6972   9813   5706     58   1803   -227       C  
+ATOM   4725  O   ARG B 209      -4.766   8.434   2.690  1.00 57.43           O  
+ANISOU 4725  O   ARG B 209     6667   9838   5315     53   1809   -298       O  
+ATOM   4726  CB  ARG B 209      -3.085   6.181   3.965  1.00 62.45           C  
+ANISOU 4726  CB  ARG B 209     7159  10153   6417    227   1775   -709       C  
+ATOM   4727  CG  ARG B 209      -1.845   5.448   3.461  1.00 77.54           C  
+ANISOU 4727  CG  ARG B 209     8864  12254   8342    279   1795   -969       C  
+ATOM   4728  CD  ARG B 209      -2.066   3.960   3.217  1.00 89.38           C  
+ANISOU 4728  CD  ARG B 209    10201  13668  10093    403   1730  -1329       C  
+ATOM   4729  NE  ARG B 209      -2.861   3.668   2.028  1.00105.57           N  
+ANISOU 4729  NE  ARG B 209    12137  15960  12015    444   1720  -1551       N  
+ATOM   4730  CZ  ARG B 209      -3.345   2.464   1.741  1.00107.70           C  
+ANISOU 4730  CZ  ARG B 209    12262  16137  12522    554   1644  -1873       C  
+ATOM   4731  NH1 ARG B 209      -3.103   1.440   2.550  1.00100.73           N  
+ANISOU 4731  NH1 ARG B 209    11321  14912  12039    627   1569  -1977       N  
+ATOM   4732  NH2 ARG B 209      -4.064   2.276   0.641  1.00110.25           N  
+ANISOU 4732  NH2 ARG B 209    12476  16712  12704    591   1632  -2087       N  
+ATOM   4733  N   VAL B 210      -4.775   9.015   4.859  1.00 65.46           N  
+ANISOU 4733  N   VAL B 210     7937  10323   6611     24   1778    -19       N  
+ATOM   4734  CA  VAL B 210      -6.095   9.643   4.759  1.00 77.88           C  
+ANISOU 4734  CA  VAL B 210     9615  11826   8151    -15   1752    119       C  
+ATOM   4735  C   VAL B 210      -6.111  11.150   5.035  1.00 79.32           C  
+ANISOU 4735  C   VAL B 210     9884  11982   8273   -123   1751    407       C  
+ATOM   4736  O   VAL B 210      -7.163  11.782   4.947  1.00 75.22           O  
+ANISOU 4736  O   VAL B 210     9436  11396   7748   -163   1723    530       O  
+ATOM   4737  CB  VAL B 210      -7.110   8.983   5.713  1.00 75.68           C  
+ANISOU 4737  CB  VAL B 210     9441  11225   8088     51   1707     84       C  
+ATOM   4738  CG1 VAL B 210      -7.338   7.531   5.320  1.00 78.12           C  
+ANISOU 4738  CG1 VAL B 210     9639  11524   8517    155   1681   -186       C  
+ATOM   4739  CG2 VAL B 210      -6.645   9.093   7.153  1.00 62.48           C  
+ANISOU 4739  CG2 VAL B 210     7856   9323   6561     52   1699    190       C  
+ATOM   4740  N   ARG B 211      -4.961  11.730   5.367  1.00 72.12           N  
+ANISOU 4740  N   ARG B 211     8948  11104   7351   -169   1771    505       N  
+ATOM   4741  CA  ARG B 211      -4.906  13.167   5.630  1.00 60.02           C  
+ANISOU 4741  CA  ARG B 211     7460   9521   5825   -269   1750    761       C  
+ATOM   4742  C   ARG B 211      -3.739  13.839   4.918  1.00 66.05           C  
+ANISOU 4742  C   ARG B 211     8092  10539   6465   -346   1779    883       C  
+ATOM   4743  O   ARG B 211      -2.678  13.240   4.739  1.00 68.56           O  
+ANISOU 4743  O   ARG B 211     8321  10999   6732   -314   1822    763       O  
+ATOM   4744  CB  ARG B 211      -4.794  13.426   7.137  1.00 68.61           C  
+ANISOU 4744  CB  ARG B 211     8661  10312   7094   -251   1721    797       C  
+ATOM   4745  CG  ARG B 211      -6.100  13.321   7.910  1.00 71.73           C  
+ANISOU 4745  CG  ARG B 211     9180  10474   7599   -215   1684    785       C  
+ATOM   4746  CD  ARG B 211      -7.083  14.422   7.538  1.00 65.19           C  
+ANISOU 4746  CD  ARG B 211     8382   9616   6771   -287   1646    940       C  
+ATOM   4747  NE  ARG B 211      -7.010  15.551   8.463  1.00 55.17           N  
+ANISOU 4747  NE  ARG B 211     7153   8177   5632   -331   1601   1053       N  
+ATOM   4748  CZ  ARG B 211      -7.797  16.621   8.403  1.00 76.04           C  
+ANISOU 4748  CZ  ARG B 211     9808  10728   8356   -392   1547   1179       C  
+ATOM   4749  NH1 ARG B 211      -8.726  16.712   7.461  1.00 84.23           N  
+ANISOU 4749  NH1 ARG B 211    10834  11832   9337   -424   1535   1241       N  
+ATOM   4750  NH2 ARG B 211      -7.658  17.599   9.288  1.00 74.15           N  
+ANISOU 4750  NH2 ARG B 211     9575  10328   8271   -419   1494   1227       N  
+ATOM   4751  N   SER B 212      -3.944  15.088   4.511  1.00 75.87           N  
+ANISOU 4751  N   SER B 212     9304  11835   7686   -451   1749   1135       N  
+ATOM   4752  CA  SER B 212      -2.885  15.875   3.892  1.00 77.82           C  
+ANISOU 4752  CA  SER B 212     9408  12309   7851   -541   1763   1322       C  
+ATOM   4753  C   SER B 212      -2.316  16.864   4.905  1.00 81.74           C  
+ANISOU 4753  C   SER B 212     9943  12556   8558   -587   1715   1470       C  
+ATOM   4754  O   SER B 212      -3.060  17.471   5.674  1.00 98.16           O  
+ANISOU 4754  O   SER B 212    12121  14361  10814   -596   1651   1525       O  
+ATOM   4755  CB  SER B 212      -3.406  16.610   2.656  1.00 71.82           C  
+ANISOU 4755  CB  SER B 212     8531  11809   6947   -639   1746   1549       C  
+ATOM   4756  OG  SER B 212      -2.362  17.310   2.002  1.00 81.67           O  
+ANISOU 4756  OG  SER B 212     9606  13318   8107   -733   1761   1765       O  
+ATOM   4757  N   ALA B 213      -0.996  17.019   4.904  1.00 75.43           N  
+ANISOU 4757  N   ALA B 213     9050  11860   7749   -611   1741   1510       N  
+ATOM   4758  CA  ALA B 213      -0.329  17.921   5.836  1.00 69.58           C  
+ANISOU 4758  CA  ALA B 213     8321  10897   7218   -647   1689   1622       C  
+ATOM   4759  C   ALA B 213      -0.122  19.309   5.242  1.00 82.78           C  
+ANISOU 4759  C   ALA B 213     9853  12633   8966   -778   1632   1948       C  
+ATOM   4760  O   ALA B 213       0.505  20.169   5.862  1.00 97.46           O  
+ANISOU 4760  O   ALA B 213    11677  14322  11033   -818   1573   2056       O  
+ATOM   4761  CB  ALA B 213       1.001  17.335   6.268  1.00 51.00           C  
+ANISOU 4761  CB  ALA B 213     5942   8580   4857   -600   1735   1492       C  
+ATOM   4762  N   TYR B 214      -0.647  19.523   4.042  1.00 77.22           N  
+ANISOU 4762  N   TYR B 214     9048  12179   8112   -845   1638   2113       N  
+ATOM   4763  CA  TYR B 214      -0.455  20.793   3.362  1.00 81.01           C  
+ANISOU 4763  CA  TYR B 214     9355  12756   8670   -982   1576   2480       C  
+ATOM   4764  C   TYR B 214      -1.687  21.698   3.414  1.00 88.64           C  
+ANISOU 4764  C   TYR B 214    10344  13506   9830  -1040   1471   2650       C  
+ATOM   4765  O   TYR B 214      -1.633  22.837   2.952  1.00 99.86           O  
+ANISOU 4765  O   TYR B 214    11607  14937  11399  -1161   1389   2982       O  
+ATOM   4766  CB  TYR B 214      -0.054  20.537   1.906  1.00 82.33           C  
+ANISOU 4766  CB  TYR B 214     9334  13425   8523  -1039   1646   2614       C  
+ATOM   4767  CG  TYR B 214       1.120  19.591   1.762  1.00 93.45           C  
+ANISOU 4767  CG  TYR B 214    10694  15074   9739   -975   1752   2408       C  
+ATOM   4768  CD1 TYR B 214       2.422  20.033   1.953  1.00 93.69           C  
+ANISOU 4768  CD1 TYR B 214    10618  15129   9851  -1018   1758   2524       C  
+ATOM   4769  CD2 TYR B 214       0.923  18.249   1.460  1.00101.66           C  
+ANISOU 4769  CD2 TYR B 214    11781  16291  10555   -868   1834   2081       C  
+ATOM   4770  CE1 TYR B 214       3.496  19.170   1.830  1.00 99.19           C  
+ANISOU 4770  CE1 TYR B 214    11262  16036  10389   -958   1852   2326       C  
+ATOM   4771  CE2 TYR B 214       1.990  17.377   1.337  1.00108.54           C  
+ANISOU 4771  CE2 TYR B 214    12585  17361  11295   -806   1917   1867       C  
+ATOM   4772  CZ  TYR B 214       3.275  17.844   1.522  1.00107.65           C  
+ANISOU 4772  CZ  TYR B 214    12373  17281  11246   -852   1930   1992       C  
+ATOM   4773  OH  TYR B 214       4.345  16.986   1.403  1.00115.98           O  
+ANISOU 4773  OH  TYR B 214    13353  18527  12187   -790   2010   1773       O  
+ATOM   4774  N   GLU B 215      -2.794  21.201   3.963  1.00 82.65           N  
+ANISOU 4774  N   GLU B 215     9761  12548   9095   -960   1465   2439       N  
+ATOM   4775  CA  GLU B 215      -3.971  22.050   4.170  1.00 93.29           C  
+ANISOU 4775  CA  GLU B 215    11138  13649  10661  -1003   1362   2556       C  
+ATOM   4776  C   GLU B 215      -4.127  22.490   5.627  1.00111.20           C  
+ANISOU 4776  C   GLU B 215    13511  15510  13230   -952   1293   2408       C  
+ATOM   4777  O   GLU B 215      -4.298  21.657   6.522  1.00105.49           O  
+ANISOU 4777  O   GLU B 215    12945  14675  12462   -841   1340   2127       O  
+ATOM   4778  CB  GLU B 215      -5.235  21.328   3.724  1.00 96.40           C  
+ANISOU 4778  CB  GLU B 215    11628  14113  10885   -957   1393   2443       C  
+ATOM   4779  CG  GLU B 215      -5.036  20.437   2.527  1.00 95.88           C  
+ANISOU 4779  CG  GLU B 215    11490  14473  10467   -949   1484   2413       C  
+ATOM   4780  CD  GLU B 215      -6.192  19.481   2.365  1.00117.50           C  
+ANISOU 4780  CD  GLU B 215    14349  17220  13075   -865   1515   2195       C  
+ATOM   4781  OE1 GLU B 215      -7.007  19.394   3.306  1.00122.52           O  
+ANISOU 4781  OE1 GLU B 215    15140  17530  13882   -806   1483   2062       O  
+ATOM   4782  OE2 GLU B 215      -6.266  18.788   1.329  1.00115.88           O  
+ANISOU 4782  OE2 GLU B 215    14070  17360  12599   -852   1570   2138       O  
+ATOM   4783  N   ARG B 216      -4.072  23.795   5.860  1.00115.16           N  
+ANISOU 4783  N   ARG B 216    13900  15808  14048  -1033   1173   2599       N  
+ATOM   4784  CA  ARG B 216      -4.126  24.321   7.213  1.00106.40           C  
+ANISOU 4784  CA  ARG B 216    12843  14353  13233   -983   1096   2431       C  
+ATOM   4785  C   ARG B 216      -5.556  24.684   7.596  1.00 93.73           C  
+ANISOU 4785  C   ARG B 216    11303  12520  11789   -967   1024   2360       C  
+ATOM   4786  O   ARG B 216      -5.914  24.664   8.772  1.00 83.52           O  
+ANISOU 4786  O   ARG B 216    10102  11017  10613   -885   1001   2114       O  
+ATOM   4787  CB  ARG B 216      -3.204  25.537   7.353  1.00103.96           C  
+ANISOU 4787  CB  ARG B 216    12346  13915  13239  -1065    987   2620       C  
+ATOM   4788  N   ASP B 217      -6.375  25.001   6.597  1.00 85.88           N  
+ANISOU 4788  N   ASP B 217    10247  11598  10786  -1044    991   2576       N  
+ATOM   4789  CA  ASP B 217      -7.745  25.435   6.844  1.00 87.05           C  
+ANISOU 4789  CA  ASP B 217    10433  11526  11116  -1042    913   2539       C  
+ATOM   4790  C   ASP B 217      -8.743  24.283   6.881  1.00 80.03           C  
+ANISOU 4790  C   ASP B 217     9734  10710   9964   -951   1008   2332       C  
+ATOM   4791  O   ASP B 217      -9.952  24.496   6.779  1.00 83.39           O  
+ANISOU 4791  O   ASP B 217    10189  11022  10472   -958    963   2340       O  
+ATOM   4792  CB  ASP B 217      -8.175  26.423   5.758  1.00 88.13           C  
+ANISOU 4792  CB  ASP B 217    10387  11680  11419  -1181    807   2908       C  
+ATOM   4793  CG  ASP B 217      -7.218  27.585   5.613  1.00107.84           C  
+ANISOU 4793  CG  ASP B 217    12655  14097  14223  -1286    695   3174       C  
+ATOM   4794  OD1 ASP B 217      -6.511  27.637   4.585  1.00115.70           O  
+ANISOU 4794  OD1 ASP B 217    13514  15371  15074  -1376    720   3468       O  
+ATOM   4795  OD2 ASP B 217      -7.159  28.436   6.525  1.00119.41           O  
+ANISOU 4795  OD2 ASP B 217    14056  15238  16077  -1276    579   3081       O  
+ATOM   4796  N   GLN B 218      -8.237  23.067   7.037  1.00 60.85           N  
+ANISOU 4796  N   GLN B 218     7417   8449   7253   -866   1131   2151       N  
+ATOM   4797  CA  GLN B 218      -9.096  21.894   7.131  1.00 66.71           C  
+ANISOU 4797  CA  GLN B 218     8316   9238   7791   -774   1211   1953       C  
+ATOM   4798  C   GLN B 218      -9.802  21.822   8.480  1.00 68.75           C  
+ANISOU 4798  C   GLN B 218     8690   9248   8185   -688   1193   1726       C  
+ATOM   4799  O   GLN B 218      -9.425  22.501   9.436  1.00 59.47           O  
+ANISOU 4799  O   GLN B 218     7481   7908   7208   -678   1136   1657       O  
+ATOM   4800  CB  GLN B 218      -8.317  20.606   6.859  1.00 90.30           C  
+ANISOU 4800  CB  GLN B 218    11349  12464  10497   -710   1328   1832       C  
+ATOM   4801  CG  GLN B 218      -6.974  20.490   7.530  1.00 99.13           C  
+ANISOU 4801  CG  GLN B 218    12449  13586  11629   -683   1355   1758       C  
+ATOM   4802  CD  GLN B 218      -6.177  19.326   6.977  1.00 98.77           C  
+ANISOU 4802  CD  GLN B 218    12398  13798  11332   -640   1456   1672       C  
+ATOM   4803  OE1 GLN B 218      -6.592  18.680   6.014  1.00 90.47           O  
+ANISOU 4803  OE1 GLN B 218    11334  12944  10097   -635   1499   1663       O  
+ATOM   4804  NE2 GLN B 218      -5.025  19.056   7.577  1.00104.90           N  
+ANISOU 4804  NE2 GLN B 218    13168  14577  12113   -606   1486   1589       N  
+ATOM   4805  N   ARG B 219     -10.837  20.994   8.530  1.00 63.10           N  
+ANISOU 4805  N   ARG B 219     8089   8530   7357   -624   1238   1607       N  
+ATOM   4806  CA  ARG B 219     -11.600  20.743   9.743  1.00 49.16           C  
+ANISOU 4806  CA  ARG B 219     6422   6595   5662   -540   1239   1407       C  
+ATOM   4807  C   ARG B 219     -10.709  20.232  10.874  1.00 49.48           C  
+ANISOU 4807  C   ARG B 219     6499   6644   5659   -465   1283   1246       C  
+ATOM   4808  O   ARG B 219      -9.833  19.394  10.660  1.00 55.25           O  
+ANISOU 4808  O   ARG B 219     7241   7519   6232   -440   1350   1229       O  
+ATOM   4809  CB  ARG B 219     -12.704  19.733   9.430  1.00 46.74           C  
+ANISOU 4809  CB  ARG B 219     6217   6327   5217   -487   1292   1341       C  
+ATOM   4810  CG  ARG B 219     -13.520  19.247  10.604  1.00 45.83           C  
+ANISOU 4810  CG  ARG B 219     6193   6091   5131   -398   1311   1165       C  
+ATOM   4811  CD  ARG B 219     -14.706  18.456  10.081  1.00 54.71           C  
+ANISOU 4811  CD  ARG B 219     7387   7225   6176   -368   1340   1151       C  
+ATOM   4812  NE  ARG B 219     -15.579  19.276   9.245  1.00 54.18           N  
+ANISOU 4812  NE  ARG B 219     7284   7100   6201   -442   1276   1277       N  
+ATOM   4813  CZ  ARG B 219     -16.691  19.865   9.674  1.00 47.36           C  
+ANISOU 4813  CZ  ARG B 219     6433   6067   5496   -444   1224   1251       C  
+ATOM   4814  NH1 ARG B 219     -17.077  19.717  10.933  1.00 47.08           N  
+ANISOU 4814  NH1 ARG B 219     6438   5938   5511   -373   1239   1093       N  
+ATOM   4815  NH2 ARG B 219     -17.420  20.594   8.840  1.00 48.69           N  
+ANISOU 4815  NH2 ARG B 219     6554   6181   5766   -518   1155   1389       N  
+ATOM   4816  N   ARG B 220     -10.946  20.745  12.079  1.00 51.54           N  
+ANISOU 4816  N   ARG B 220     6757   6765   6060   -428   1238   1117       N  
+ATOM   4817  CA  ARG B 220     -10.176  20.361  13.258  1.00 60.82           C  
+ANISOU 4817  CA  ARG B 220     7949   7972   7190   -359   1265    970       C  
+ATOM   4818  C   ARG B 220     -10.702  19.075  13.881  1.00 55.46           C  
+ANISOU 4818  C   ARG B 220     7369   7355   6348   -270   1341    865       C  
+ATOM   4819  O   ARG B 220     -11.908  18.910  14.060  1.00 59.75           O  
+ANISOU 4819  O   ARG B 220     7957   7846   6899   -244   1343    827       O  
+ATOM   4820  CB  ARG B 220     -10.204  21.475  14.311  1.00 73.08           C  
+ANISOU 4820  CB  ARG B 220     9422   9396   8949   -351   1177    849       C  
+ATOM   4821  CG  ARG B 220      -9.444  21.125  15.587  1.00 73.77           C  
+ANISOU 4821  CG  ARG B 220     9507   9557   8964   -279   1197    689       C  
+ATOM   4822  CD  ARG B 220      -9.288  22.311  16.531  1.00 87.66           C  
+ANISOU 4822  CD  ARG B 220    11150  11222  10934   -269   1096    534       C  
+ATOM   4823  NE  ARG B 220      -8.310  23.297  16.083  1.00106.05           N  
+ANISOU 4823  NE  ARG B 220    13364  13461  13470   -338   1015    616       N  
+ATOM   4824  CZ  ARG B 220      -7.994  24.389  16.774  1.00101.24           C  
+ANISOU 4824  CZ  ARG B 220    12618  12740  13106   -334    905    478       C  
+ATOM   4825  NH1 ARG B 220      -8.577  24.627  17.942  1.00 94.11           N  
+ANISOU 4825  NH1 ARG B 220    11679  11842  12238   -260    871    223       N  
+ATOM   4826  NH2 ARG B 220      -7.094  25.240  16.303  1.00 96.40           N  
+ANISOU 4826  NH2 ARG B 220    11885  12028  12713   -403    825    587       N  
+ATOM   4827  N   HIS B 221      -9.793  18.163  14.207  1.00 50.37           N  
+ANISOU 4827  N   HIS B 221     6742   6815   5582   -228   1396    835       N  
+ATOM   4828  CA  HIS B 221     -10.170  16.941  14.901  1.00 45.42           C  
+ANISOU 4828  CA  HIS B 221     6172   6237   4849   -150   1449    772       C  
+ATOM   4829  C   HIS B 221      -9.481  16.884  16.259  1.00 50.87           C  
+ANISOU 4829  C   HIS B 221     6831   6982   5517   -104   1443    690       C  
+ATOM   4830  O   HIS B 221      -8.596  17.691  16.546  1.00 48.18           O  
+ANISOU 4830  O   HIS B 221     6432   6640   5235   -127   1403    659       O  
+ATOM   4831  CB  HIS B 221      -9.818  15.717  14.056  1.00 43.59           C  
+ANISOU 4831  CB  HIS B 221     5961   6079   4522   -134   1505    813       C  
+ATOM   4832  CG  HIS B 221     -10.323  15.796  12.647  1.00 52.58           C  
+ANISOU 4832  CG  HIS B 221     7105   7228   5645   -179   1508    877       C  
+ATOM   4833  ND1 HIS B 221     -11.632  15.522  12.312  1.00 56.11           N  
+ANISOU 4833  ND1 HIS B 221     7597   7623   6100   -166   1508    878       N  
+ATOM   4834  CD2 HIS B 221      -9.699  16.125  11.495  1.00 50.60           C  
+ANISOU 4834  CD2 HIS B 221     6803   7067   5356   -239   1510    952       C  
+ATOM   4835  CE1 HIS B 221     -11.789  15.677  11.010  1.00 58.51           C  
+ANISOU 4835  CE1 HIS B 221     7881   7986   6366   -214   1505    941       C  
+ATOM   4836  NE2 HIS B 221     -10.634  16.041  10.489  1.00 59.61           N  
+ANISOU 4836  NE2 HIS B 221     7955   8230   6465   -260   1508    994       N  
+ATOM   4837  N   TYR B 222      -9.887  15.935  17.095  1.00 44.95           N  
+ANISOU 4837  N   TYR B 222     6099   6291   4688    -42   1476    668       N  
+ATOM   4838  CA  TYR B 222      -9.357  15.857  18.450  1.00 45.06           C  
+ANISOU 4838  CA  TYR B 222     6064   6409   4648      1   1467    609       C  
+ATOM   4839  C   TYR B 222      -8.937  14.452  18.864  1.00 51.55           C  
+ANISOU 4839  C   TYR B 222     6879   7316   5391     44   1506    681       C  
+ATOM   4840  O   TYR B 222      -9.518  13.457  18.429  1.00 53.22           O  
+ANISOU 4840  O   TYR B 222     7118   7493   5611     61   1535    750       O  
+ATOM   4841  CB  TYR B 222     -10.384  16.400  19.448  1.00 46.92           C  
+ANISOU 4841  CB  TYR B 222     6269   6684   4875     31   1444    515       C  
+ATOM   4842  CG  TYR B 222     -10.811  17.822  19.167  1.00 50.75           C  
+ANISOU 4842  CG  TYR B 222     6726   7056   5500     -7   1383    420       C  
+ATOM   4843  CD1 TYR B 222     -10.122  18.894  19.720  1.00 55.41           C  
+ANISOU 4843  CD1 TYR B 222     7229   7649   6176    -13   1317    295       C  
+ATOM   4844  CD2 TYR B 222     -11.902  18.095  18.350  1.00 51.43           C  
+ANISOU 4844  CD2 TYR B 222     6853   7020   5667    -36   1378    456       C  
+ATOM   4845  CE1 TYR B 222     -10.504  20.197  19.467  1.00 60.28           C  
+ANISOU 4845  CE1 TYR B 222     7786   8128   6992    -48   1239    210       C  
+ATOM   4846  CE2 TYR B 222     -12.291  19.396  18.091  1.00 54.79           C  
+ANISOU 4846  CE2 TYR B 222     7229   7319   6268    -76   1305    392       C  
+ATOM   4847  CZ  TYR B 222     -11.589  20.442  18.653  1.00 59.99           C  
+ANISOU 4847  CZ  TYR B 222     7786   7961   7047    -82   1232    270       C  
+ATOM   4848  OH  TYR B 222     -11.975  21.738  18.398  1.00 64.94           O  
+ANISOU 4848  OH  TYR B 222     8330   8428   7917   -123   1138    207       O  
+ATOM   4849  N   CYS B 223      -7.918  14.391  19.715  1.00 52.23           N  
+ANISOU 4849  N   CYS B 223     6911   7501   5432     60   1492    664       N  
+ATOM   4850  CA  CYS B 223      -7.447  13.137  20.282  1.00 52.38           C  
+ANISOU 4850  CA  CYS B 223     6892   7602   5406     95   1509    754       C  
+ATOM   4851  C   CYS B 223      -7.189  13.329  21.772  1.00 52.33           C  
+ANISOU 4851  C   CYS B 223     6808   7777   5298    125   1484    730       C  
+ATOM   4852  O   CYS B 223      -6.454  14.230  22.164  1.00 48.37           O  
+ANISOU 4852  O   CYS B 223     6273   7322   4781    117   1451    625       O  
+ATOM   4853  CB  CYS B 223      -6.178  12.660  19.574  1.00 43.16           C  
+ANISOU 4853  CB  CYS B 223     5718   6393   4289     79   1516    779       C  
+ATOM   4854  SG  CYS B 223      -5.398  11.224  20.343  1.00 45.36           S  
+ANISOU 4854  SG  CYS B 223     5916   6743   4576    117   1510    887       S  
+ATOM   4855  N   LEU B 224      -7.785  12.479  22.601  1.00 50.69           N  
+ANISOU 4855  N   LEU B 224     6550   7688   5023    158   1494    834       N  
+ATOM   4856  CA  LEU B 224      -7.611  12.586  24.046  1.00 47.30           C  
+ANISOU 4856  CA  LEU B 224     6018   7504   4449    185   1473    831       C  
+ATOM   4857  C   LEU B 224      -6.621  11.549  24.553  1.00 53.68           C  
+ANISOU 4857  C   LEU B 224     6753   8399   5244    192   1459    985       C  
+ATOM   4858  O   LEU B 224      -6.803  10.352  24.328  1.00 60.46           O  
+ANISOU 4858  O   LEU B 224     7591   9193   6188    195   1466   1159       O  
+ATOM   4859  CB  LEU B 224      -8.954  12.421  24.762  1.00 57.49           C  
+ANISOU 4859  CB  LEU B 224     7261   8937   5645    211   1490    875       C  
+ATOM   4860  CG  LEU B 224     -10.052  13.423  24.400  1.00 47.99           C  
+ANISOU 4860  CG  LEU B 224     6109   7658   4467    209   1497    718       C  
+ATOM   4861  CD1 LEU B 224     -11.351  13.076  25.109  1.00 45.00           C  
+ANISOU 4861  CD1 LEU B 224     5671   7436   3993    236   1523    782       C  
+ATOM   4862  CD2 LEU B 224      -9.618  14.839  24.739  1.00 47.89           C  
+ANISOU 4862  CD2 LEU B 224     6062   7690   4443    210   1453    479       C  
+ATOM   4863  N   ILE B 225      -5.568  11.999  25.232  1.00 59.66           N  
+ANISOU 4863  N   ILE B 225     7455   9286   5927    195   1426    918       N  
+ATOM   4864  CA  ILE B 225      -4.626  11.054  25.833  1.00 57.06           C  
+ANISOU 4864  CA  ILE B 225     7039   9058   5584    199   1402   1077       C  
+ATOM   4865  C   ILE B 225      -4.354  11.411  27.287  1.00 55.83           C  
+ANISOU 4865  C   ILE B 225     6761   9227   5226    221   1368   1055       C  
+ATOM   4866  O   ILE B 225      -4.791  12.450  27.759  1.00 50.69           O  
+ANISOU 4866  O   ILE B 225     6091   8707   4460    239   1361    866       O  
+ATOM   4867  CB  ILE B 225      -3.285  11.002  25.069  1.00 53.88           C  
+ANISOU 4867  CB  ILE B 225     6677   8488   5309    177   1392   1040       C  
+ATOM   4868  CG1 ILE B 225      -2.573  12.353  25.134  1.00 51.41           C  
+ANISOU 4868  CG1 ILE B 225     6381   8193   4959    169   1368    834       C  
+ATOM   4869  CG2 ILE B 225      -3.501  10.567  23.623  1.00 48.27           C  
+ANISOU 4869  CG2 ILE B 225     6053   7522   4766    160   1426   1047       C  
+ATOM   4870  CD1 ILE B 225      -1.181  12.331  24.545  1.00 52.03           C  
+ANISOU 4870  CD1 ILE B 225     6474   8154   5142    147   1358    817       C  
+ATOM   4871  N   LYS B 226      -3.645  10.539  27.998  1.00 60.71           N  
+ANISOU 4871  N   LYS B 226     7274   9986   5807    220   1337   1240       N  
+ATOM   4872  CA  LYS B 226      -3.259  10.814  29.379  1.00 54.94           C  
+ANISOU 4872  CA  LYS B 226     6405   9613   4855    239   1298   1232       C  
+ATOM   4873  C   LYS B 226      -1.778  11.160  29.472  1.00 55.94           C  
+ANISOU 4873  C   LYS B 226     6523   9723   5007    234   1254   1139       C  
+ATOM   4874  O   LYS B 226      -0.948  10.535  28.811  1.00 63.78           O  
+ANISOU 4874  O   LYS B 226     7556  10504   6175    211   1249   1234       O  
+ATOM   4875  CB  LYS B 226      -3.572   9.621  30.287  1.00 63.65           C  
+ANISOU 4875  CB  LYS B 226     7357  10954   5873    235   1283   1555       C  
+ATOM   4876  CG  LYS B 226      -3.151   9.831  31.739  1.00 64.41           C  
+ANISOU 4876  CG  LYS B 226     7281  11493   5698    250   1240   1577       C  
+ATOM   4877  CD  LYS B 226      -3.326   8.573  32.574  1.00 71.61           C  
+ANISOU 4877  CD  LYS B 226     8016  12644   6550    230   1213   1972       C  
+ATOM   4878  CE  LYS B 226      -2.103   7.675  32.481  1.00 82.24           C  
+ANISOU 4878  CE  LYS B 226     9318  13854   8076    200   1155   2180       C  
+ATOM   4879  NZ  LYS B 226      -0.897   8.320  33.071  1.00 81.43           N  
+ANISOU 4879  NZ  LYS B 226     9177  13926   7836    210   1111   2026       N  
+ATOM   4880  N   LYS B 227      -1.454  12.164  30.282  1.00 65.29           N  
+ANISOU 4880  N   LYS B 227     7642  11133   6032    260   1219    930       N  
+ATOM   4881  CA  LYS B 227      -0.066  12.548  30.503  1.00 63.55           C  
+ANISOU 4881  CA  LYS B 227     7393  10922   5830    259   1167    833       C  
+ATOM   4882  C   LYS B 227       0.722  11.380  31.086  1.00 70.10           C  
+ANISOU 4882  C   LYS B 227     8123  11878   6632    244   1135   1107       C  
+ATOM   4883  O   LYS B 227       0.220  10.628  31.925  1.00 70.69           O  
+ANISOU 4883  O   LYS B 227     8077  12217   6564    246   1127   1326       O  
+ATOM   4884  CB  LYS B 227       0.028  13.769  31.427  1.00 65.39           C  
+ANISOU 4884  CB  LYS B 227     7530  11416   5898    301   1117    542       C  
+ATOM   4885  CG  LYS B 227      -0.325  13.496  32.882  1.00 78.19           C  
+ANISOU 4885  CG  LYS B 227     8968  13524   7217    333   1093    600       C  
+ATOM   4886  CD  LYS B 227       0.034  14.672  33.778  1.00 82.15           C  
+ANISOU 4886  CD  LYS B 227     9346  14295   7572    384   1028    258       C  
+ATOM   4887  CE  LYS B 227      -0.433  14.439  35.207  1.00 81.77           C  
+ANISOU 4887  CE  LYS B 227     9090  14807   7170    420   1012    292       C  
+ATOM   4888  NZ  LYS B 227       0.702  14.484  36.172  1.00 97.24           N  
+ANISOU 4888  NZ  LYS B 227    10904  17071   8971    439    936    254       N  
+ATOM   4889  N   GLU B 228       1.949  11.212  30.609  1.00 69.39           N  
+ANISOU 4889  N   GLU B 228     8071  11597   6699    225   1112   1115       N  
+ATOM   4890  CA  GLU B 228       2.822  10.174  31.130  1.00 73.91           C  
+ANISOU 4890  CA  GLU B 228     8538  12253   7291    208   1066   1358       C  
+ATOM   4891  C   GLU B 228       3.235  10.527  32.555  1.00 73.76           C  
+ANISOU 4891  C   GLU B 228     8364  12648   7014    230   1004   1332       C  
+ATOM   4892  O   GLU B 228       3.646  11.655  32.828  1.00 67.68           O  
+ANISOU 4892  O   GLU B 228     7593  11960   6161    257    977   1051       O  
+ATOM   4893  CB  GLU B 228       4.050  10.003  30.233  1.00 66.13           C  
+ANISOU 4893  CB  GLU B 228     7624  10964   6540    186   1060   1329       C  
+ATOM   4894  CG  GLU B 228       4.483   8.559  30.041  1.00 74.73           C  
+ANISOU 4894  CG  GLU B 228     8649  11930   7815    162   1038   1607       C  
+ATOM   4895  CD  GLU B 228       3.527   7.776  29.159  1.00 76.85           C  
+ANISOU 4895  CD  GLU B 228     8967  11980   8252    155   1083   1713       C  
+ATOM   4896  OE1 GLU B 228       2.734   8.407  28.428  1.00 78.52           O  
+ANISOU 4896  OE1 GLU B 228     9299  12082   8452    163   1142   1551       O  
+ATOM   4897  OE2 GLU B 228       3.567   6.528  29.197  1.00 85.47           O  
+ANISOU 4897  OE2 GLU B 228     9961  13001   9513    142   1047   1957       O  
+ATOM   4898  N   GLU B 229       3.124   9.561  33.462  1.00 72.57           N  
+ANISOU 4898  N   GLU B 229     8059  12767   6748    218    970   1631       N  
+ATOM   4899  CA  GLU B 229       3.463   9.798  34.860  1.00 73.68           C  
+ANISOU 4899  CA  GLU B 229     8020  13378   6597    236    909   1640       C  
+ATOM   4900  C   GLU B 229       4.617   8.903  35.282  1.00 70.08           C  
+ANISOU 4900  C   GLU B 229     7455  12964   6209    204    837   1904       C  
+ATOM   4901  O   GLU B 229       4.822   7.832  34.712  1.00 77.17           O  
+ANISOU 4901  O   GLU B 229     8364  13592   7364    166    831   2162       O  
+ATOM   4902  CB  GLU B 229       2.251   9.556  35.762  1.00 75.74           C  
+ANISOU 4902  CB  GLU B 229     8140  14047   6590    245    924   1786       C  
+ATOM   4903  CG  GLU B 229       1.169  10.614  35.651  1.00 79.63           C  
+ANISOU 4903  CG  GLU B 229     8694  14601   6961    288    979   1471       C  
+ATOM   4904  CD  GLU B 229      -0.067  10.259  36.451  1.00100.83           C  
+ANISOU 4904  CD  GLU B 229    11235  17680   9397    294   1007   1639       C  
+ATOM   4905  OE1 GLU B 229      -0.745   9.278  36.083  1.00110.96           O  
+ANISOU 4905  OE1 GLU B 229    12526  18826  10806    259   1038   1952       O  
+ATOM   4906  OE2 GLU B 229      -0.359  10.958  37.444  1.00101.59           O  
+ANISOU 4906  OE2 GLU B 229    11189  18231   9178    337    993   1449       O  
+ATOM   4907  N   ARG B 230       5.373   9.349  36.280  1.00 72.39           N  
+ANISOU 4907  N   ARG B 230     7625  13591   6289    221    771   1822       N  
+ATOM   4908  CA  ARG B 230       6.543   8.607  36.718  1.00 77.16           C  
+ANISOU 4908  CA  ARG B 230     8119  14243   6956    190    692   2056       C  
+ATOM   4909  C   ARG B 230       6.071   7.342  37.425  1.00 84.68           C  
+ANISOU 4909  C   ARG B 230     8881  15442   7849    147    657   2530       C  
+ATOM   4910  O   ARG B 230       5.098   7.373  38.179  1.00 78.25           O  
+ANISOU 4910  O   ARG B 230     7949  15021   6762    156    672   2619       O  
+ATOM   4911  CB  ARG B 230       7.422   9.445  37.657  1.00 75.49           C  
+ANISOU 4911  CB  ARG B 230     7808  14364   6511    223    623   1837       C  
+ATOM   4912  CG  ARG B 230       7.873  10.806  37.120  1.00 87.77           C  
+ANISOU 4912  CG  ARG B 230     9500  15709   8137    267    634   1371       C  
+ATOM   4913  CD  ARG B 230       8.929  11.433  38.037  1.00 88.59           C  
+ANISOU 4913  CD  ARG B 230     9481  16097   8082    298    542   1188       C  
+ATOM   4914  NE  ARG B 230       9.367  12.836  37.865  1.00 92.35           N  
+ANISOU 4914  NE  ARG B 230    10010  16474   8603    348    517    730       N  
+ATOM   4915  CZ  ARG B 230       9.069  13.699  36.888  1.00100.15           C  
+ANISOU 4915  CZ  ARG B 230    11152  17105   9796    361    563    465       C  
+ATOM   4916  NH1 ARG B 230       8.142  13.463  35.971  1.00108.49           N  
+ANISOU 4916  NH1 ARG B 230    12343  17899  10979    338    651    548       N  
+ATOM   4917  NH2 ARG B 230       9.631  14.899  36.913  1.00 99.56           N  
+ANISOU 4917  NH2 ARG B 230    11065  16971   9792    402    508    100       N  
+ATOM   4918  N   ARG B 231       6.754   6.232  37.178  1.00 95.99           N  
+ANISOU 4918  N   ARG B 231    10262  16648   9561    100    603   2839       N  
+ATOM   4919  CA  ARG B 231       6.422   4.979  37.837  1.00 92.48           C  
+ANISOU 4919  CA  ARG B 231     9602  16395   9144     49    543   3339       C  
+ATOM   4920  C   ARG B 231       7.177   4.916  39.155  1.00 91.43           C  
+ANISOU 4920  C   ARG B 231     9248  16745   8747     32    447   3515       C  
+ATOM   4921  O   ARG B 231       8.275   5.463  39.260  1.00 86.23           O  
+ANISOU 4921  O   ARG B 231     8624  16077   8061     50    410   3300       O  
+ATOM   4922  CB  ARG B 231       6.789   3.788  36.951  1.00 90.00           C  
+ANISOU 4922  CB  ARG B 231     9297  15585   9314      9    508   3577       C  
+ATOM   4923  CG  ARG B 231       5.799   3.505  35.835  1.00 91.61           C  
+ANISOU 4923  CG  ARG B 231     9636  15413   9760     17    584   3525       C  
+ATOM   4924  CD  ARG B 231       6.524   2.930  34.630  1.00 97.59           C  
+ANISOU 4924  CD  ARG B 231    10485  15630  10965     11    573   3459       C  
+ATOM   4925  NE  ARG B 231       5.670   2.827  33.451  1.00101.40           N  
+ANISOU 4925  NE  ARG B 231    11112  15767  11648     30    649   3320       N  
+ATOM   4926  CZ  ARG B 231       6.086   2.378  32.270  1.00 96.68           C  
+ANISOU 4926  CZ  ARG B 231    10592  14733  11410     36    657   3203       C  
+ATOM   4927  NH1 ARG B 231       7.345   1.993  32.113  1.00 91.49           N  
+ANISOU 4927  NH1 ARG B 231     9882  13913  10966     24    597   3206       N  
+ATOM   4928  NH2 ARG B 231       5.245   2.316  31.247  1.00 94.86           N  
+ANISOU 4928  NH2 ARG B 231    10477  14250  11317     56    723   3069       N  
+ATOM   4929  N   PRO B 232       6.586   4.273  40.175  1.00 97.63           N  
+ANISOU 4929  N   PRO B 232     9789  17978   9326     -3    402   3913       N  
+ATOM   4930  CA  PRO B 232       7.287   4.168  41.458  1.00 90.83           C  
+ANISOU 4930  CA  PRO B 232     8688  17640   8184    -26    304   4119       C  
+ATOM   4931  C   PRO B 232       8.606   3.431  41.274  1.00 94.57           C  
+ANISOU 4931  C   PRO B 232     9119  17817   8995    -70    204   4320       C  
+ATOM   4932  O   PRO B 232       8.609   2.324  40.734  1.00 99.64           O  
+ANISOU 4932  O   PRO B 232     9723  18084  10051   -119    165   4642       O  
+ATOM   4933  CB  PRO B 232       6.315   3.371  42.337  1.00 85.22           C  
+ANISOU 4933  CB  PRO B 232     7713  17381   7287    -75    279   4612       C  
+ATOM   4934  CG  PRO B 232       5.400   2.680  41.373  1.00 90.93           C  
+ANISOU 4934  CG  PRO B 232     8530  17643   8376    -95    330   4763       C  
+ATOM   4935  CD  PRO B 232       5.267   3.620  40.214  1.00 99.89           C  
+ANISOU 4935  CD  PRO B 232     9990  18342   9623    -29    436   4213       C  
+ATOM   4936  N   ASP B 233       9.702   4.058  41.692  1.00 95.06           N  
+ANISOU 4936  N   ASP B 233     9180  18028   8913    -47    156   4104       N  
+ATOM   4937  CA  ASP B 233      11.040   3.485  41.574  1.00105.48           C  
+ANISOU 4937  CA  ASP B 233    10458  19093  10528    -83     60   4249       C  
+ATOM   4938  C   ASP B 233      11.400   3.188  40.120  1.00107.21           C  
+ANISOU 4938  C   ASP B 233    10891  18590  11254    -81    102   4102       C  
+ATOM   4939  O   ASP B 233      11.358   2.039  39.677  1.00117.55           O  
+ANISOU 4939  O   ASP B 233    12130  19582  12952   -128     59   4423       O  
+ATOM   4940  CB  ASP B 233      11.160   2.213  42.421  1.00106.79           C  
+ANISOU 4940  CB  ASP B 233    10315  19504  10757   -166    -65   4878       C  
+ATOM   4941  N   GLU B 234      11.750   4.238  39.385  1.00104.07           N  
+ANISOU 4941  N   GLU B 234    10729  17954  10859    -26    178   3611       N  
+ATOM   4942  CA  GLU B 234      12.303   4.102  38.043  1.00 97.67           C  
+ANISOU 4942  CA  GLU B 234    10102  16542  10465    -21    218   3432       C  
+ATOM   4943  C   GLU B 234      13.117   5.352  37.740  1.00 84.93           C  
+ANISOU 4943  C   GLU B 234     8651  14854   8766     26    253   2974       C  
+ATOM   4944  O   GLU B 234      12.848   6.423  38.288  1.00 76.56           O  
+ANISOU 4944  O   GLU B 234     7610  14109   7370     68    273   2719       O  
+ATOM   4945  CB  GLU B 234      11.206   3.902  36.992  1.00 97.46           C  
+ANISOU 4945  CB  GLU B 234    10215  16196  10619    -12    316   3374       C  
+ATOM   4946  CG  GLU B 234      10.550   5.184  36.496  1.00 99.43           C  
+ANISOU 4946  CG  GLU B 234    10673  16438  10667     42    429   2948       C  
+ATOM   4947  CD  GLU B 234       9.695   4.967  35.259  1.00106.64           C  
+ANISOU 4947  CD  GLU B 234    11740  16967  11812     48    519   2872       C  
+ATOM   4948  OE1 GLU B 234       9.568   3.805  34.817  1.00113.71           O  
+ANISOU 4948  OE1 GLU B 234    12570  17615  13021     18    491   3126       O  
+ATOM   4949  OE2 GLU B 234       9.163   5.961  34.720  1.00 94.52           O  
+ANISOU 4949  OE2 GLU B 234    10373  15373  10169     84    605   2552       O  
+ATOM   4950  N   LEU B 235      14.116   5.217  36.876  1.00 79.50           N  
+ANISOU 4950  N   LEU B 235     8053  13752   8400     20    253   2865       N  
+ATOM   4951  CA  LEU B 235      15.047   6.308  36.621  1.00 81.48           C  
+ANISOU 4951  CA  LEU B 235     8420  13920   8618     54    268   2496       C  
+ATOM   4952  C   LEU B 235      14.348   7.443  35.881  1.00 81.03           C  
+ANISOU 4952  C   LEU B 235     8558  13750   8482     96    376   2129       C  
+ATOM   4953  O   LEU B 235      13.305   7.236  35.262  1.00 79.70           O  
+ANISOU 4953  O   LEU B 235     8468  13450   8364     95    450   2152       O  
+ATOM   4954  CB  LEU B 235      16.243   5.802  35.815  1.00 84.09           C  
+ANISOU 4954  CB  LEU B 235     8781  13844   9325     33    250   2498       C  
+ATOM   4955  CG  LEU B 235      17.081   4.724  36.508  1.00 84.41           C  
+ANISOU 4955  CG  LEU B 235     8617  13946   9509    -11    125   2845       C  
+ATOM   4956  CD1 LEU B 235      18.225   4.263  35.618  1.00 92.82           C  
+ANISOU 4956  CD1 LEU B 235     9710  14587  10970    -24    115   2792       C  
+ATOM   4957  CD2 LEU B 235      17.601   5.220  37.847  1.00 83.79           C  
+ANISOU 4957  CD2 LEU B 235     8408  14320   9106     -5     34   2873       C  
+ATOM   4958  N   GLU B 236      14.918   8.641  35.945  1.00 82.02           N  
+ANISOU 4958  N   GLU B 236     8743  13912   8510    131    372   1800       N  
+ATOM   4959  CA  GLU B 236      14.258   9.812  35.383  1.00 81.45           C  
+ANISOU 4959  CA  GLU B 236     8813  13757   8378    167    448   1469       C  
+ATOM   4960  C   GLU B 236      14.511   9.918  33.885  1.00 83.16           C  
+ANISOU 4960  C   GLU B 236     9196  13504   8896    152    528   1356       C  
+ATOM   4961  O   GLU B 236      13.737  10.532  33.150  1.00 81.74           O  
+ANISOU 4961  O   GLU B 236     9136  13190   8730    163    603   1193       O  
+ATOM   4962  CB  GLU B 236      14.734  11.084  36.103  1.00 82.22           C  
+ANISOU 4962  CB  GLU B 236     8864  14082   8294    212    389   1156       C  
+ATOM   4963  CG  GLU B 236      14.044  12.369  35.660  1.00 93.27           C  
+ANISOU 4963  CG  GLU B 236    10362  15405   9669    251    437    810       C  
+ATOM   4964  CD  GLU B 236      12.581  12.442  36.063  1.00 94.56           C  
+ANISOU 4964  CD  GLU B 236    10502  15822   9604    272    474    808       C  
+ATOM   4965  OE1 GLU B 236      12.106  11.550  36.797  1.00 89.00           O  
+ANISOU 4965  OE1 GLU B 236     9687  15408   8720    259    461   1080       O  
+ATOM   4966  OE2 GLU B 236      11.901  13.399  35.636  1.00103.08           O  
+ANISOU 4966  OE2 GLU B 236    11658  16808  10700    299    512    549       O  
+ATOM   4967  N   ALA B 237      15.578   9.271  33.433  1.00 84.17           N  
+ANISOU 4967  N   ALA B 237     9312  13407   9262    125    510   1456       N  
+ATOM   4968  CA  ALA B 237      15.930   9.287  32.022  1.00 84.36           C  
+ANISOU 4968  CA  ALA B 237     9457  13046   9549    110    587   1355       C  
+ATOM   4969  C   ALA B 237      14.972   8.428  31.206  1.00 82.94           C  
+ANISOU 4969  C   ALA B 237     9327  12699   9488     97    656   1482       C  
+ATOM   4970  O   ALA B 237      14.622   8.771  30.074  1.00 81.27           O  
+ANISOU 4970  O   ALA B 237     9235  12279   9366     96    741   1343       O  
+ATOM   4971  CB  ALA B 237      17.358   8.816  31.832  1.00 86.10           C  
+ANISOU 4971  CB  ALA B 237     9622  13108   9982     91    545   1402       C  
+ATOM   4972  N   ASP B 238      14.532   7.322  31.796  1.00 82.93           N  
+ANISOU 4972  N   ASP B 238     9214  12803   9492     84    611   1758       N  
+ATOM   4973  CA  ASP B 238      13.581   6.432  31.144  1.00 81.43           C  
+ANISOU 4973  CA  ASP B 238     9038  12457   9444     76    655   1889       C  
+ATOM   4974  C   ASP B 238      12.231   7.125  31.027  1.00 79.42           C  
+ANISOU 4974  C   ASP B 238     8886  12300   8990     95    725   1783       C  
+ATOM   4975  O   ASP B 238      11.564   7.082  29.978  1.00 79.68           O  
+ANISOU 4975  O   ASP B 238     9022  12128   9127     98    801   1704       O  
+ATOM   4976  CB  ASP B 238      13.443   5.123  31.924  1.00 81.93           C  
+ANISOU 4976  CB  ASP B 238     8918  12615   9597     52    566   2249       C  
+ATOM   4977  CG  ASP B 238      14.767   4.403  32.096  1.00 87.15           C  
+ANISOU 4977  CG  ASP B 238     9453  13169  10489     31    479   2371       C  
+ATOM   4978  OD1 ASP B 238      15.818   4.997  31.775  1.00 87.33           O  
+ANISOU 4978  OD1 ASP B 238     9534  13102  10547     37    490   2169       O  
+ATOM   4979  OD2 ASP B 238      14.756   3.239  32.550  1.00 98.55           O  
+ANISOU 4979  OD2 ASP B 238    10726  14612  12108      4    393   2682       O  
+ATOM   4980  N   PHE B 239      11.841   7.789  32.109  1.00 77.62           N  
+ANISOU 4980  N   PHE B 239     8616  12403   8472    111    694   1762       N  
+ATOM   4981  CA  PHE B 239      10.590   8.518  32.114  1.00 74.54           C  
+ANISOU 4981  CA  PHE B 239     8301  12128   7892    133    751   1636       C  
+ATOM   4982  C   PHE B 239      10.625   9.627  31.074  1.00 74.36           C  
+ANISOU 4982  C   PHE B 239     8437  11881   7934    144    818   1333       C  
+ATOM   4983  O   PHE B 239       9.667   9.816  30.326  1.00 71.66           O  
+ANISOU 4983  O   PHE B 239     8194  11417   7616    145    887   1271       O  
+ATOM   4984  CB  PHE B 239      10.295   9.146  33.468  1.00 74.33           C  
+ANISOU 4984  CB  PHE B 239     8173  12531   7540    158    701   1596       C  
+ATOM   4985  CG  PHE B 239       9.069   9.996  33.450  1.00 72.04           C  
+ANISOU 4985  CG  PHE B 239     7947  12344   7080    187    755   1411       C  
+ATOM   4986  CD1 PHE B 239       7.824   9.410  33.325  1.00 68.71           C  
+ANISOU 4986  CD1 PHE B 239     7531  11945   6632    180    801   1571       C  
+ATOM   4987  CD2 PHE B 239       9.158  11.376  33.433  1.00 72.32           C  
+ANISOU 4987  CD2 PHE B 239     8033  12400   7045    220    754   1070       C  
+ATOM   4988  CE1 PHE B 239       6.687  10.179  33.268  1.00 66.57           C  
+ANISOU 4988  CE1 PHE B 239     7317  11751   6225    206    851   1397       C  
+ATOM   4989  CE2 PHE B 239       8.020  12.148  33.366  1.00 71.85           C  
+ANISOU 4989  CE2 PHE B 239     8018  12400   6881    246    794    891       C  
+ATOM   4990  CZ  PHE B 239       6.780  11.546  33.293  1.00 67.39           C  
+ANISOU 4990  CZ  PHE B 239     7464  11885   6256    239    847   1053       C  
+ATOM   4991  N   GLU B 240      11.734  10.362  31.031  1.00 77.10           N  
+ANISOU 4991  N   GLU B 240     8792  12179   8322    147    790   1166       N  
+ATOM   4992  CA  GLU B 240      11.862  11.475  30.098  1.00 76.88           C  
+ANISOU 4992  CA  GLU B 240     8878  11953   8381    147    836    922       C  
+ATOM   4993  C   GLU B 240      11.896  10.962  28.668  1.00 75.07           C  
+ANISOU 4993  C   GLU B 240     8738  11422   8364    119    914    961       C  
+ATOM   4994  O   GLU B 240      11.507  11.664  27.730  1.00 73.61           O  
+ANISOU 4994  O   GLU B 240     8647  11096   8226    110    972    835       O  
+ATOM   4995  CB  GLU B 240      13.132  12.282  30.382  1.00 79.95           C  
+ANISOU 4995  CB  GLU B 240     9227  12344   8809    152    776    769       C  
+ATOM   4996  CG  GLU B 240      13.022  13.288  31.513  1.00 85.68           C  
+ANISOU 4996  CG  GLU B 240     9874  13335   9346    192    702    586       C  
+ATOM   4997  CD  GLU B 240      14.360  13.923  31.846  1.00 86.38           C  
+ANISOU 4997  CD  GLU B 240     9898  13415   9506    200    626    450       C  
+ATOM   4998  OE1 GLU B 240      15.332  13.684  31.098  1.00 83.94           O  
+ANISOU 4998  OE1 GLU B 240     9623  12875   9395    169    645    501       O  
+ATOM   4999  OE2 GLU B 240      14.443  14.655  32.854  1.00 98.44           O  
+ANISOU 4999  OE2 GLU B 240    11329  15180  10895    240    545    278       O  
+ATOM   5000  N   TYR B 241      12.341   9.721  28.515  1.00 75.42           N  
+ANISOU 5000  N   TYR B 241     8727  11385   8544    106    906   1136       N  
+ATOM   5001  CA  TYR B 241      12.316   9.047  27.228  1.00 73.92           C  
+ANISOU 5001  CA  TYR B 241     8581  10953   8553     92    971   1150       C  
+ATOM   5002  C   TYR B 241      10.862   8.862  26.791  1.00 73.19           C  
+ANISOU 5002  C   TYR B 241     8553  10838   8417     99   1025   1175       C  
+ATOM   5003  O   TYR B 241      10.471   9.259  25.680  1.00 83.09           O  
+ANISOU 5003  O   TYR B 241     9900  11962   9710     92   1096   1060       O  
+ATOM   5004  CB  TYR B 241      13.050   7.706  27.322  1.00 75.89           C  
+ANISOU 5004  CB  TYR B 241     8715  11123   8996     86    924   1312       C  
+ATOM   5005  CG  TYR B 241      12.991   6.850  26.080  1.00 75.37           C  
+ANISOU 5005  CG  TYR B 241     8648  10831   9157     85    974   1292       C  
+ATOM   5006  CD1 TYR B 241      13.913   7.027  25.058  1.00 82.22           C  
+ANISOU 5006  CD1 TYR B 241     9530  11562  10147     78   1020   1142       C  
+ATOM   5007  CD2 TYR B 241      12.031   5.856  25.932  1.00 74.51           C  
+ANISOU 5007  CD2 TYR B 241     8500  10663   9147     95    970   1412       C  
+ATOM   5008  CE1 TYR B 241      13.880   6.248  23.920  1.00 78.65           C  
+ANISOU 5008  CE1 TYR B 241     9048  10954   9880     86   1064   1079       C  
+ATOM   5009  CE2 TYR B 241      11.988   5.070  24.793  1.00 79.85           C  
+ANISOU 5009  CE2 TYR B 241     9150  11141  10048    105   1003   1344       C  
+ATOM   5010  CZ  TYR B 241      12.916   5.272  23.790  1.00 83.97           C  
+ANISOU 5010  CZ  TYR B 241     9680  11563  10660    103   1051   1161       C  
+ATOM   5011  OH  TYR B 241      12.884   4.497  22.653  1.00 75.60           O  
+ANISOU 5011  OH  TYR B 241     8566  10357   9799    121   1083   1050       O  
+ATOM   5012  N   ARG B 242      10.057   8.287  27.684  1.00 70.46           N  
+ANISOU 5012  N   ARG B 242     8147  10643   7982    109    988   1339       N  
+ATOM   5013  CA  ARG B 242       8.639   8.067  27.389  1.00 68.50           C  
+ANISOU 5013  CA  ARG B 242     7947  10383   7696    116   1032   1381       C  
+ATOM   5014  C   ARG B 242       7.885   9.381  27.126  1.00 68.41           C  
+ANISOU 5014  C   ARG B 242     8052  10410   7531    123   1082   1189       C  
+ATOM   5015  O   ARG B 242       7.039   9.456  26.224  1.00 65.39           O  
+ANISOU 5015  O   ARG B 242     7754   9904   7187    120   1142   1140       O  
+ATOM   5016  CB  ARG B 242       7.984   7.283  28.534  1.00 67.55           C  
+ANISOU 5016  CB  ARG B 242     7710  10462   7495    120    977   1625       C  
+ATOM   5017  CG  ARG B 242       8.106   5.771  28.369  1.00 69.29           C  
+ANISOU 5017  CG  ARG B 242     7815  10538   7974    110    935   1852       C  
+ATOM   5018  CD  ARG B 242       7.574   4.982  29.563  1.00 79.63           C  
+ANISOU 5018  CD  ARG B 242     8967  12060   9228    100    863   2163       C  
+ATOM   5019  NE  ARG B 242       6.592   5.711  30.360  1.00 90.99           N  
+ANISOU 5019  NE  ARG B 242    10424  13795  10352    110    886   2160       N  
+ATOM   5020  CZ  ARG B 242       6.742   5.979  31.654  1.00 85.01           C  
+ANISOU 5020  CZ  ARG B 242     9560  13392   9350    109    835   2256       C  
+ATOM   5021  NH1 ARG B 242       7.833   5.577  32.292  1.00 86.22           N  
+ANISOU 5021  NH1 ARG B 242     9589  13631   9538     92    755   2391       N  
+ATOM   5022  NH2 ARG B 242       5.803   6.645  32.312  1.00 76.91           N  
+ANISOU 5022  NH2 ARG B 242     8531  12652   8037    127    860   2207       N  
+ATOM   5023  N   VAL B 243       8.206  10.416  27.898  1.00 66.95           N  
+ANISOU 5023  N   VAL B 243     7852  10386   7198    132   1046   1071       N  
+ATOM   5024  CA  VAL B 243       7.617  11.740  27.698  1.00 66.37           C  
+ANISOU 5024  CA  VAL B 243     7853  10321   7046    139   1068    868       C  
+ATOM   5025  C   VAL B 243       7.962  12.315  26.341  1.00 69.32           C  
+ANISOU 5025  C   VAL B 243     8315  10451   7572    112   1117    759       C  
+ATOM   5026  O   VAL B 243       7.101  12.854  25.644  1.00 70.11           O  
+ANISOU 5026  O   VAL B 243     8490  10467   7680    103   1159    692       O  
+ATOM   5027  CB  VAL B 243       8.081  12.731  28.767  1.00 69.00           C  
+ANISOU 5027  CB  VAL B 243     8114  10853   7251    162    997    718       C  
+ATOM   5028  CG1 VAL B 243       7.642  14.151  28.419  1.00 69.53           C  
+ANISOU 5028  CG1 VAL B 243     8228  10852   7337    168    998    484       C  
+ATOM   5029  CG2 VAL B 243       7.530  12.321  30.089  1.00 68.63           C  
+ANISOU 5029  CG2 VAL B 243     7961  11126   6988    190    958    810       C  
+ATOM   5030  N   ARG B 244       9.230  12.184  25.969  1.00 74.66           N  
+ANISOU 5030  N   ARG B 244     8969  11034   8366     95   1109    757       N  
+ATOM   5031  CA  ARG B 244       9.693  12.678  24.686  1.00 67.50           C  
+ANISOU 5031  CA  ARG B 244     8112   9949   7585     63   1158    686       C  
+ATOM   5032  C   ARG B 244       8.946  11.992  23.557  1.00 64.43           C  
+ANISOU 5032  C   ARG B 244     7780   9455   7246     52   1232    739       C  
+ATOM   5033  O   ARG B 244       8.514  12.641  22.599  1.00 62.86           O  
+ANISOU 5033  O   ARG B 244     7638   9181   7063     28   1277    684       O  
+ATOM   5034  CB  ARG B 244      11.198  12.449  24.538  1.00 69.37           C  
+ANISOU 5034  CB  ARG B 244     8291  10133   7931     50   1142    693       C  
+ATOM   5035  CG  ARG B 244      11.765  12.872  23.196  1.00 68.70           C  
+ANISOU 5035  CG  ARG B 244     8228   9917   7958     12   1199    647       C  
+ATOM   5036  CD  ARG B 244      11.435  14.316  22.874  1.00 69.45           C  
+ANISOU 5036  CD  ARG B 244     8352   9979   8058    -13   1192    564       C  
+ATOM   5037  NE  ARG B 244      12.007  14.720  21.594  1.00 68.77           N  
+ANISOU 5037  NE  ARG B 244     8255   9808   8067    -60   1243    575       N  
+ATOM   5038  CZ  ARG B 244      11.790  15.896  21.015  1.00 69.59           C  
+ANISOU 5038  CZ  ARG B 244     8357   9857   8225   -100   1239    561       C  
+ATOM   5039  NH1 ARG B 244      11.008  16.792  21.602  1.00 71.55           N  
+ANISOU 5039  NH1 ARG B 244     8616  10095   8472    -91   1181    496       N  
+ATOM   5040  NH2 ARG B 244      12.354  16.176  19.849  1.00 83.47           N  
+ANISOU 5040  NH2 ARG B 244    10078  11585  10051   -151   1288    617       N  
+ATOM   5041  N   LYS B 245       8.773  10.681  23.679  1.00 63.83           N  
+ANISOU 5041  N   LYS B 245     7667   9373   7210     70   1234    849       N  
+ATOM   5042  CA  LYS B 245       8.046   9.943  22.652  1.00 63.19           C  
+ANISOU 5042  CA  LYS B 245     7616   9192   7200     72   1290    868       C  
+ATOM   5043  C   LYS B 245       6.567  10.363  22.580  1.00 70.80           C  
+ANISOU 5043  C   LYS B 245     8658  10178   8065     75   1315    861       C  
+ATOM   5044  O   LYS B 245       6.007  10.476  21.484  1.00 62.94           O  
+ANISOU 5044  O   LYS B 245     7717   9106   7091     63   1368    814       O  
+ATOM   5045  CB  LYS B 245       8.201   8.441  22.878  1.00 63.00           C  
+ANISOU 5045  CB  LYS B 245     7500   9126   7311     93   1259    982       C  
+ATOM   5046  CG  LYS B 245       9.633   8.000  22.586  1.00 72.83           C  
+ANISOU 5046  CG  LYS B 245     8665  10308   8700     88   1246    952       C  
+ATOM   5047  CD  LYS B 245       9.746   6.705  21.813  1.00 79.85           C  
+ANISOU 5047  CD  LYS B 245     9468  11068   9802    107   1250    943       C  
+ATOM   5048  CE  LYS B 245      10.594   6.928  20.567  1.00 84.18           C  
+ANISOU 5048  CE  LYS B 245    10006  11577  10401     97   1311    779       C  
+ATOM   5049  NZ  LYS B 245      12.046   6.984  20.901  1.00 84.19           N  
+ANISOU 5049  NZ  LYS B 245     9938  11582  10470     86   1282    770       N  
+ATOM   5050  N   GLN B 246       5.938  10.606  23.730  1.00 65.45           N  
+ANISOU 5050  N   GLN B 246     7972   9628   7268     92   1276    902       N  
+ATOM   5051  CA  GLN B 246       4.551  11.083  23.722  1.00 57.50           C  
+ANISOU 5051  CA  GLN B 246     7029   8650   6171     98   1298    876       C  
+ATOM   5052  C   GLN B 246       4.459  12.461  23.061  1.00 57.89           C  
+ANISOU 5052  C   GLN B 246     7143   8639   6215     72   1315    736       C  
+ATOM   5053  O   GLN B 246       3.498  12.761  22.347  1.00 55.89           O  
+ANISOU 5053  O   GLN B 246     6952   8320   5963     61   1351    713       O  
+ATOM   5054  CB  GLN B 246       3.968  11.147  25.137  1.00 57.63           C  
+ANISOU 5054  CB  GLN B 246     6992   8868   6036    124   1254    924       C  
+ATOM   5055  CG  GLN B 246       2.496  11.556  25.166  1.00 55.87           C  
+ANISOU 5055  CG  GLN B 246     6818   8682   5726    134   1279    892       C  
+ATOM   5056  CD  GLN B 246       1.856  11.393  26.532  1.00 61.90           C  
+ANISOU 5056  CD  GLN B 246     7500   9697   6321    162   1247    960       C  
+ATOM   5057  OE1 GLN B 246       2.223  12.076  27.488  1.00 71.85           O  
+ANISOU 5057  OE1 GLN B 246     8696  11148   7457    178   1203    867       O  
+ATOM   5058  NE2 GLN B 246       0.884  10.492  26.626  1.00 53.77           N  
+ANISOU 5058  NE2 GLN B 246     6453   8692   5287    169   1266   1119       N  
+ATOM   5059  N   GLU B 247       5.473  13.288  23.296  1.00 60.48           N  
+ANISOU 5059  N   GLU B 247     7438   8978   6564     60   1279    658       N  
+ATOM   5060  CA  GLU B 247       5.539  14.624  22.713  1.00 61.72           C  
+ANISOU 5060  CA  GLU B 247     7615   9056   6781     27   1272    557       C  
+ATOM   5061  C   GLU B 247       5.659  14.550  21.193  1.00 59.87           C  
+ANISOU 5061  C   GLU B 247     7418   8706   6626    -15   1334    600       C  
+ATOM   5062  O   GLU B 247       5.004  15.305  20.466  1.00 62.51           O  
+ANISOU 5062  O   GLU B 247     7784   8979   6988    -47   1347    588       O  
+ATOM   5063  CB  GLU B 247       6.723  15.398  23.301  1.00 71.59           C  
+ANISOU 5063  CB  GLU B 247     8794  10328   8079     25   1207    476       C  
+ATOM   5064  CG  GLU B 247       6.970  16.758  22.669  1.00 90.74           C  
+ANISOU 5064  CG  GLU B 247    11201  12639  10639    -16   1180    405       C  
+ATOM   5065  CD  GLU B 247       8.171  17.469  23.268  1.00 95.48           C  
+ANISOU 5065  CD  GLU B 247    11712  13241  11326    -13   1104    321       C  
+ATOM   5066  OE1 GLU B 247       8.847  16.874  24.134  1.00 82.72           O  
+ANISOU 5066  OE1 GLU B 247    10060  11730   9639     20   1080    316       O  
+ATOM   5067  OE2 GLU B 247       8.437  18.624  22.875  1.00108.53           O  
+ANISOU 5067  OE2 GLU B 247    13316  14783  13138    -46   1058    273       O  
+ATOM   5068  N   LEU B 248       6.485  13.621  20.719  1.00 58.63           N  
+ANISOU 5068  N   LEU B 248     7234   8537   6505    -16   1368    647       N  
+ATOM   5069  CA  LEU B 248       6.636  13.394  19.285  1.00 56.82           C  
+ANISOU 5069  CA  LEU B 248     7009   8265   6315    -47   1432    663       C  
+ATOM   5070  C   LEU B 248       5.327  12.889  18.684  1.00 62.06           C  
+ANISOU 5070  C   LEU B 248     7727   8913   6938    -37   1473    678       C  
+ATOM   5071  O   LEU B 248       4.974  13.238  17.557  1.00 52.61           O  
+ANISOU 5071  O   LEU B 248     6547   7712   5731    -70   1513    680       O  
+ATOM   5072  CB  LEU B 248       7.766  12.402  19.012  1.00 57.16           C  
+ANISOU 5072  CB  LEU B 248     6986   8316   6417    -36   1453    664       C  
+ATOM   5073  CG  LEU B 248       9.176  12.894  19.341  1.00 59.78           C  
+ANISOU 5073  CG  LEU B 248     7257   8655   6801    -53   1423    652       C  
+ATOM   5074  CD1 LEU B 248      10.206  11.823  19.021  1.00 60.16           C  
+ANISOU 5074  CD1 LEU B 248     7230   8704   6924    -39   1445    641       C  
+ATOM   5075  CD2 LEU B 248       9.481  14.179  18.591  1.00 61.11           C  
+ANISOU 5075  CD2 LEU B 248     7412   8815   6992   -110   1433    656       C  
+ATOM   5076  N   PHE B 249       4.616  12.062  19.444  1.00 53.45           N  
+ANISOU 5076  N   PHE B 249     6651   7830   5827      6   1457    707       N  
+ATOM   5077  CA  PHE B 249       3.304  11.571  19.033  1.00 51.52           C  
+ANISOU 5077  CA  PHE B 249     6453   7557   5565     21   1483    724       C  
+ATOM   5078  C   PHE B 249       2.329  12.730  18.838  1.00 57.75           C  
+ANISOU 5078  C   PHE B 249     7307   8335   6299     -6   1484    704       C  
+ATOM   5079  O   PHE B 249       1.627  12.812  17.820  1.00 51.84           O  
+ANISOU 5079  O   PHE B 249     6593   7557   5545    -24   1519    703       O  
+ATOM   5080  CB  PHE B 249       2.770  10.589  20.075  1.00 51.96           C  
+ANISOU 5080  CB  PHE B 249     6484   7631   5626     65   1452    799       C  
+ATOM   5081  CG  PHE B 249       1.400  10.051  19.773  1.00 50.56           C  
+ANISOU 5081  CG  PHE B 249     6342   7414   5455     84   1470    830       C  
+ATOM   5082  CD1 PHE B 249       1.194   9.201  18.700  1.00 60.50           C  
+ANISOU 5082  CD1 PHE B 249     7582   8598   6807     95   1498    799       C  
+ATOM   5083  CD2 PHE B 249       0.325  10.368  20.587  1.00 50.56           C  
+ANISOU 5083  CD2 PHE B 249     6373   7464   5372     95   1455    871       C  
+ATOM   5084  CE1 PHE B 249      -0.065   8.696  18.430  1.00 55.34           C  
+ANISOU 5084  CE1 PHE B 249     6952   7895   6181    115   1505    820       C  
+ATOM   5085  CE2 PHE B 249      -0.935   9.865  20.323  1.00 58.51           C  
+ANISOU 5085  CE2 PHE B 249     7406   8428   6397    111   1471    910       C  
+ATOM   5086  CZ  PHE B 249      -1.130   9.028  19.243  1.00 53.67           C  
+ANISOU 5086  CZ  PHE B 249     6783   7713   5894    120   1493    890       C  
+ATOM   5087  N   ILE B 250       2.304  13.631  19.817  1.00 52.10           N  
+ANISOU 5087  N   ILE B 250     6589   7651   5556     -5   1436    675       N  
+ATOM   5088  CA  ILE B 250       1.467  14.823  19.749  1.00 52.78           C  
+ANISOU 5088  CA  ILE B 250     6705   7704   5645    -27   1415    630       C  
+ATOM   5089  C   ILE B 250       1.829  15.673  18.532  1.00 55.69           C  
+ANISOU 5089  C   ILE B 250     7064   8006   6088    -89   1424    649       C  
+ATOM   5090  O   ILE B 250       0.950  16.196  17.847  1.00 56.81           O  
+ANISOU 5090  O   ILE B 250     7234   8100   6249   -119   1430    671       O  
+ATOM   5091  CB  ILE B 250       1.595  15.671  21.033  1.00 56.35           C  
+ANISOU 5091  CB  ILE B 250     7112   8214   6086     -7   1346    539       C  
+ATOM   5092  CG1 ILE B 250       1.046  14.902  22.236  1.00 60.48           C  
+ANISOU 5092  CG1 ILE B 250     7620   8869   6489     48   1339    550       C  
+ATOM   5093  CG2 ILE B 250       0.880  17.005  20.876  1.00 58.71           C  
+ANISOU 5093  CG2 ILE B 250     7405   8440   6461    -31   1304    460       C  
+ATOM   5094  CD1 ILE B 250       1.244  15.611  23.558  1.00 58.58           C  
+ANISOU 5094  CD1 ILE B 250     7305   8762   6190     78   1272    433       C  
+ATOM   5095  N   SER B 251       3.126  15.800  18.264  1.00 64.08           N  
+ANISOU 5095  N   SER B 251     8073   9080   7197   -113   1424    663       N  
+ATOM   5096  CA  SER B 251       3.601  16.564  17.112  1.00 64.32           C  
+ANISOU 5096  CA  SER B 251     8059   9089   7289   -180   1434    726       C  
+ATOM   5097  C   SER B 251       3.112  15.956  15.797  1.00 60.61           C  
+ANISOU 5097  C   SER B 251     7609   8670   6750   -200   1505    781       C  
+ATOM   5098  O   SER B 251       2.605  16.661  14.910  1.00 59.20           O  
+ANISOU 5098  O   SER B 251     7418   8490   6583   -254   1507    854       O  
+ATOM   5099  CB  SER B 251       5.128  16.633  17.118  1.00 58.33           C  
+ANISOU 5099  CB  SER B 251     7227   8357   6580   -196   1429    736       C  
+ATOM   5100  OG  SER B 251       5.611  17.360  16.001  1.00 76.03           O  
+ANISOU 5100  OG  SER B 251     9401  10612   8876   -268   1442    832       O  
+ATOM   5101  N   ASP B 252       3.251  14.637  15.696  1.00 50.24           N  
+ANISOU 5101  N   ASP B 252     6305   7405   5378   -154   1552    743       N  
+ATOM   5102  CA  ASP B 252       2.826  13.895  14.516  1.00 50.74           C  
+ANISOU 5102  CA  ASP B 252     6362   7535   5382   -153   1610    735       C  
+ATOM   5103  C   ASP B 252       1.337  14.081  14.278  1.00 56.18           C  
+ANISOU 5103  C   ASP B 252     7120   8185   6042   -155   1607    754       C  
+ATOM   5104  O   ASP B 252       0.901  14.269  13.142  1.00 64.87           O  
+ANISOU 5104  O   ASP B 252     8206   9350   7090   -190   1635    787       O  
+ATOM   5105  CB  ASP B 252       3.149  12.407  14.667  1.00 57.79           C  
+ANISOU 5105  CB  ASP B 252     7228   8438   6292    -89   1632    657       C  
+ATOM   5106  CG  ASP B 252       4.592  12.085  14.336  1.00 55.18           C  
+ANISOU 5106  CG  ASP B 252     6805   8176   5986    -94   1653    620       C  
+ATOM   5107  OD1 ASP B 252       5.384  13.028  14.130  1.00 56.05           O  
+ANISOU 5107  OD1 ASP B 252     6879   8329   6089   -146   1654    672       O  
+ATOM   5108  OD2 ASP B 252       4.933  10.885  14.280  1.00 75.93           O  
+ANISOU 5108  OD2 ASP B 252     9378  10804   8669    -45   1663    539       O  
+ATOM   5109  N   LEU B 253       0.558  14.023  15.353  1.00 51.80           N  
+ANISOU 5109  N   LEU B 253     6625   7549   5506   -117   1573    736       N  
+ATOM   5110  CA  LEU B 253      -0.878  14.232  15.240  1.00 46.58           C  
+ANISOU 5110  CA  LEU B 253     6027   6842   4830   -116   1567    748       C  
+ATOM   5111  C   LEU B 253      -1.186  15.668  14.822  1.00 55.99           C  
+ANISOU 5111  C   LEU B 253     7211   7999   6062   -183   1534    803       C  
+ATOM   5112  O   LEU B 253      -2.134  15.921  14.076  1.00 65.22           O  
+ANISOU 5112  O   LEU B 253     8404   9157   7219   -210   1539    844       O  
+ATOM   5113  CB  LEU B 253      -1.571  13.918  16.564  1.00 45.92           C  
+ANISOU 5113  CB  LEU B 253     5982   6719   4747    -64   1539    723       C  
+ATOM   5114  CG  LEU B 253      -1.811  12.440  16.873  1.00 54.97           C  
+ANISOU 5114  CG  LEU B 253     7123   7869   5895     -6   1557    726       C  
+ATOM   5115  CD1 LEU B 253      -2.815  12.282  18.005  1.00 44.46           C  
+ANISOU 5115  CD1 LEU B 253     5816   6534   4542     30   1534    752       C  
+ATOM   5116  CD2 LEU B 253      -2.263  11.694  15.636  1.00 44.05           C  
+ANISOU 5116  CD2 LEU B 253     5738   6475   4524      0   1593    706       C  
+ATOM   5117  N   SER B 254      -0.376  16.602  15.310  1.00 51.41           N  
+ANISOU 5117  N   SER B 254     6582   7392   5560   -210   1487    809       N  
+ATOM   5118  CA  SER B 254      -0.558  18.018  15.010  1.00 57.85           C  
+ANISOU 5118  CA  SER B 254     7351   8136   6494   -275   1429    871       C  
+ATOM   5119  C   SER B 254      -0.302  18.332  13.541  1.00 62.85           C  
+ANISOU 5119  C   SER B 254     7924   8841   7115   -352   1453   1014       C  
+ATOM   5120  O   SER B 254      -0.919  19.237  12.979  1.00 63.63           O  
+ANISOU 5120  O   SER B 254     7989   8892   7295   -412   1412   1115       O  
+ATOM   5121  CB  SER B 254       0.352  18.875  15.893  1.00 56.18           C  
+ANISOU 5121  CB  SER B 254     7070   7868   6408   -279   1359    824       C  
+ATOM   5122  OG  SER B 254      -0.012  18.766  17.258  1.00 91.63           O  
+ANISOU 5122  OG  SER B 254    11588  12342  10885   -212   1326    686       O  
+ATOM   5123  N   ARG B 255       0.615  17.591  12.923  1.00 56.42           N  
+ANISOU 5123  N   ARG B 255     7076   8161   6201   -351   1516   1028       N  
+ATOM   5124  CA  ARG B 255       0.927  17.810  11.511  1.00 52.36           C  
+ANISOU 5124  CA  ARG B 255     6475   7797   5623   -422   1551   1160       C  
+ATOM   5125  C   ARG B 255      -0.284  17.533  10.609  1.00 67.21           C  
+ANISOU 5125  C   ARG B 255     8387   9744   7405   -431   1576   1190       C  
+ATOM   5126  O   ARG B 255      -0.373  18.053   9.496  1.00 78.56           O  
+ANISOU 5126  O   ARG B 255     9743  11308   8798   -505   1580   1338       O  
+ATOM   5127  CB  ARG B 255       2.118  16.946  11.084  1.00 48.13           C  
+ANISOU 5127  CB  ARG B 255     5880   7422   4984   -403   1619   1113       C  
+ATOM   5128  CG  ARG B 255       2.667  17.286   9.703  1.00 60.04           C  
+ANISOU 5128  CG  ARG B 255     7258   9151   6402   -480   1657   1253       C  
+ATOM   5129  CD  ARG B 255       3.852  16.408   9.333  1.00 63.36           C  
+ANISOU 5129  CD  ARG B 255     7603   9747   6724   -451   1727   1163       C  
+ATOM   5130  NE  ARG B 255       4.126  16.435   7.898  1.00 76.98           N  
+ANISOU 5130  NE  ARG B 255     9193  11769   8288   -506   1784   1250       N  
+ATOM   5131  CZ  ARG B 255       3.790  15.464   7.055  1.00 73.54           C  
+ANISOU 5131  CZ  ARG B 255     8724  11535   7684   -466   1845   1120       C  
+ATOM   5132  NH1 ARG B 255       3.164  14.383   7.500  1.00 68.43           N  
+ANISOU 5132  NH1 ARG B 255     8171  10774   7055   -373   1848    915       N  
+ATOM   5133  NH2 ARG B 255       4.078  15.574   5.765  1.00 71.92           N  
+ANISOU 5133  NH2 ARG B 255     8368  11659   7300   -518   1895   1195       N  
+ATOM   5134  N   PHE B 256      -1.217  16.721  11.098  1.00 60.34           N  
+ANISOU 5134  N   PHE B 256     7620   8804   6504   -360   1589   1067       N  
+ATOM   5135  CA  PHE B 256      -2.427  16.394  10.347  1.00 65.79           C  
+ANISOU 5135  CA  PHE B 256     8346   9533   7119   -358   1606   1072       C  
+ATOM   5136  C   PHE B 256      -3.640  17.162  10.866  1.00 61.73           C  
+ANISOU 5136  C   PHE B 256     7895   8848   6710   -370   1545   1105       C  
+ATOM   5137  O   PHE B 256      -4.783  16.758  10.642  1.00 50.34           O  
+ANISOU 5137  O   PHE B 256     6512   7384   5232   -346   1553   1075       O  
+ATOM   5138  CB  PHE B 256      -2.699  14.890  10.397  1.00 67.56           C  
+ANISOU 5138  CB  PHE B 256     8613   9787   7270   -270   1654    914       C  
+ATOM   5139  CG  PHE B 256      -1.624  14.059   9.762  1.00 64.07           C  
+ANISOU 5139  CG  PHE B 256     8083   9514   6748   -250   1706    837       C  
+ATOM   5140  CD1 PHE B 256      -1.131  14.385   8.509  1.00 61.28           C  
+ANISOU 5140  CD1 PHE B 256     7620   9386   6278   -308   1738    902       C  
+ATOM   5141  CD2 PHE B 256      -1.106  12.953  10.414  1.00 59.36           C  
+ANISOU 5141  CD2 PHE B 256     7487   8868   6199   -175   1718    706       C  
+ATOM   5142  CE1 PHE B 256      -0.144  13.623   7.917  1.00 70.87           C  
+ANISOU 5142  CE1 PHE B 256     8730  10787   7409   -283   1789    797       C  
+ATOM   5143  CE2 PHE B 256      -0.117  12.187   9.828  1.00 64.28           C  
+ANISOU 5143  CE2 PHE B 256     8008   9633   6784   -151   1758    605       C  
+ATOM   5144  CZ  PHE B 256       0.365  12.522   8.577  1.00 65.97           C  
+ANISOU 5144  CZ  PHE B 256     8116  10084   6866   -201   1798    630       C  
+ATOM   5145  N   ASN B 257      -3.373  18.262  11.564  1.00 51.83           N  
+ANISOU 5145  N   ASN B 257     6614   7471   5608   -403   1479   1147       N  
+ATOM   5146  CA  ASN B 257      -4.408  19.105  12.161  1.00 48.50           C  
+ANISOU 5146  CA  ASN B 257     6218   6881   5328   -409   1408   1137       C  
+ATOM   5147  C   ASN B 257      -5.310  18.333  13.124  1.00 49.31           C  
+ANISOU 5147  C   ASN B 257     6424   6926   5385   -322   1428    990       C  
+ATOM   5148  O   ASN B 257      -6.511  18.590  13.211  1.00 47.71           O  
+ANISOU 5148  O   ASN B 257     6259   6642   5225   -319   1403    977       O  
+ATOM   5149  CB  ASN B 257      -5.250  19.777  11.069  1.00 56.60           C  
+ANISOU 5149  CB  ASN B 257     7205   7907   6393   -485   1377   1290       C  
+ATOM   5150  CG  ASN B 257      -5.997  21.000  11.575  1.00 71.67           C  
+ANISOU 5150  CG  ASN B 257     9081   9616   8534   -516   1275   1305       C  
+ATOM   5151  OD1 ASN B 257      -5.567  21.656  12.524  1.00 84.13           O  
+ANISOU 5151  OD1 ASN B 257    10615  11079  10271   -502   1215   1224       O  
+ATOM   5152  ND2 ASN B 257      -7.120  21.313  10.939  1.00 87.64           N  
+ANISOU 5152  ND2 ASN B 257    11107  11598  10593   -554   1248   1390       N  
+ATOM   5153  N   ILE B 258      -4.724  17.382  13.843  1.00 48.36           N  
+ANISOU 5153  N   ILE B 258     6333   6854   5187   -257   1468    898       N  
+ATOM   5154  CA  ILE B 258      -5.434  16.699  14.916  1.00 45.49           C  
+ANISOU 5154  CA  ILE B 258     6031   6462   4792   -183   1476    803       C  
+ATOM   5155  C   ILE B 258      -4.924  17.194  16.262  1.00 53.81           C  
+ANISOU 5155  C   ILE B 258     7052   7503   5891   -156   1432    721       C  
+ATOM   5156  O   ILE B 258      -3.812  16.862  16.673  1.00 62.21           O  
+ANISOU 5156  O   ILE B 258     8085   8622   6929   -139   1439    705       O  
+ATOM   5157  CB  ILE B 258      -5.276  15.170  14.838  1.00 49.71           C  
+ANISOU 5157  CB  ILE B 258     6590   7062   5234   -127   1535    783       C  
+ATOM   5158  CG1 ILE B 258      -5.813  14.647  13.506  1.00 44.89           C  
+ANISOU 5158  CG1 ILE B 258     5990   6486   4579   -140   1570    809       C  
+ATOM   5159  CG2 ILE B 258      -6.004  14.501  15.994  1.00 42.72           C  
+ANISOU 5159  CG2 ILE B 258     5738   6158   4335    -62   1534    744       C  
+ATOM   5160  CD1 ILE B 258      -5.693  13.150  13.352  1.00 49.58           C  
+ANISOU 5160  CD1 ILE B 258     6575   7116   5148    -79   1607    752       C  
+ATOM   5161  N   LYS B 259      -5.739  17.992  16.944  1.00 56.31           N  
+ANISOU 5161  N   LYS B 259     7359   7759   6279   -147   1382    651       N  
+ATOM   5162  CA  LYS B 259      -5.336  18.559  18.223  1.00 54.63           C  
+ANISOU 5162  CA  LYS B 259     7086   7570   6102   -115   1329    526       C  
+ATOM   5163  C   LYS B 259      -5.390  17.523  19.332  1.00 52.82           C  
+ANISOU 5163  C   LYS B 259     6873   7473   5722    -43   1365    484       C  
+ATOM   5164  O   LYS B 259      -6.399  16.845  19.517  1.00 62.46           O  
+ANISOU 5164  O   LYS B 259     8137   8725   6869    -12   1399    505       O  
+ATOM   5165  CB  LYS B 259      -6.213  19.758  18.590  1.00 59.20           C  
+ANISOU 5165  CB  LYS B 259     7613   8059   6823   -121   1254    421       C  
+ATOM   5166  CG  LYS B 259      -5.884  20.346  19.952  1.00 64.08           C  
+ANISOU 5166  CG  LYS B 259     8140   8737   7471    -73   1192    231       C  
+ATOM   5167  CD  LYS B 259      -4.652  21.230  19.896  1.00 83.36           C  
+ANISOU 5167  CD  LYS B 259    10488  11112  10075   -106   1121    204       C  
+ATOM   5168  CE  LYS B 259      -4.451  21.961  21.211  1.00 94.15           C  
+ANISOU 5168  CE  LYS B 259    11737  12533  11505    -51   1038    -37       C  
+ATOM   5169  NZ  LYS B 259      -3.095  22.569  21.309  1.00 90.53           N  
+ANISOU 5169  NZ  LYS B 259    11186  12028  11183    -70    972    -68       N  
+ATOM   5170  N   THR B 260      -4.292  17.407  20.070  1.00 54.02           N  
+ANISOU 5170  N   THR B 260     6977   7710   5840    -22   1350    446       N  
+ATOM   5171  CA  THR B 260      -4.222  16.464  21.171  1.00 52.71           C  
+ANISOU 5171  CA  THR B 260     6795   7697   5534     35   1370    447       C  
+ATOM   5172  C   THR B 260      -4.453  17.175  22.496  1.00 57.53           C  
+ANISOU 5172  C   THR B 260     7323   8434   6101     75   1316    292       C  
+ATOM   5173  O   THR B 260      -3.774  18.149  22.819  1.00 71.25           O  
+ANISOU 5173  O   THR B 260     8990  10162   7920     70   1253    166       O  
+ATOM   5174  CB  THR B 260      -2.865  15.738  21.217  1.00 52.09           C  
+ANISOU 5174  CB  THR B 260     6697   7664   5431     37   1383    512       C  
+ATOM   5175  OG1 THR B 260      -2.647  15.051  19.979  1.00 63.17           O  
+ANISOU 5175  OG1 THR B 260     8148   8981   6871      9   1431    610       O  
+ATOM   5176  CG2 THR B 260      -2.845  14.731  22.352  1.00 53.62           C  
+ANISOU 5176  CG2 THR B 260     6852   8018   5504     86   1389    563       C  
+ATOM   5177  N   ILE B 261      -5.417  16.677  23.259  1.00 54.53           N  
+ANISOU 5177  N   ILE B 261     6931   8189   5598    116   1338    294       N  
+ATOM   5178  CA  ILE B 261      -5.662  17.176  24.599  1.00 55.81           C  
+ANISOU 5178  CA  ILE B 261     6987   8559   5659    164   1298    136       C  
+ATOM   5179  C   ILE B 261      -5.164  16.158  25.617  1.00 53.81           C  
+ANISOU 5179  C   ILE B 261     6676   8549   5221    198   1314    237       C  
+ATOM   5180  O   ILE B 261      -5.502  14.962  25.565  1.00 50.95           O  
+ANISOU 5180  O   ILE B 261     6342   8220   4797    200   1363    435       O  
+ATOM   5181  CB  ILE B 261      -7.148  17.487  24.839  1.00 55.82           C  
+ANISOU 5181  CB  ILE B 261     6976   8598   5635    186   1306     57       C  
+ATOM   5182  CG1 ILE B 261      -7.610  18.597  23.894  1.00 58.33           C  
+ANISOU 5182  CG1 ILE B 261     7324   8667   6170    147   1268    -37       C  
+ATOM   5183  CG2 ILE B 261      -7.369  17.934  26.269  1.00 57.52           C  
+ANISOU 5183  CG2 ILE B 261     7049   9096   5709    244   1270   -134       C  
+ATOM   5184  CD1 ILE B 261      -9.065  18.507  23.506  1.00 56.98           C  
+ANISOU 5184  CD1 ILE B 261     7203   8431   6017    145   1299     -8       C  
+ATOM   5185  N   VAL B 262      -4.328  16.649  26.524  1.00 55.78           N  
+ANISOU 5185  N   VAL B 262     6825   8960   5410    223   1261    107       N  
+ATOM   5186  CA  VAL B 262      -3.661  15.811  27.501  1.00 61.57           C  
+ANISOU 5186  CA  VAL B 262     7481   9940   5973    246   1259    212       C  
+ATOM   5187  C   VAL B 262      -4.347  15.937  28.854  1.00 58.73           C  
+ANISOU 5187  C   VAL B 262     6986   9937   5392    297   1245    120       C  
+ATOM   5188  O   VAL B 262      -4.332  16.994  29.484  1.00 57.90           O  
+ANISOU 5188  O   VAL B 262     6782   9959   5258    331   1189   -151       O  
+ATOM   5189  CB  VAL B 262      -2.176  16.183  27.637  1.00 61.38           C  
+ANISOU 5189  CB  VAL B 262     7421   9900   6003    240   1207    141       C  
+ATOM   5190  CG1 VAL B 262      -1.471  15.197  28.538  1.00 57.08           C  
+ANISOU 5190  CG1 VAL B 262     6800   9589   5300    255   1201    295       C  
+ATOM   5191  CG2 VAL B 262      -1.514  16.219  26.268  1.00 57.87           C  
+ANISOU 5191  CG2 VAL B 262     7084   9139   5763    188   1224    211       C  
+ATOM   5192  N   LEU B 263      -4.951  14.839  29.286  1.00 56.27           N  
+ANISOU 5192  N   LEU B 263     6645   9797   4938    302   1289    344       N  
+ATOM   5193  CA  LEU B 263      -5.717  14.792  30.516  1.00 59.21           C  
+ANISOU 5193  CA  LEU B 263     6871  10560   5064    343   1292    318       C  
+ATOM   5194  C   LEU B 263      -4.842  14.252  31.640  1.00 67.40           C  
+ANISOU 5194  C   LEU B 263     7767  11938   5902    356   1260    429       C  
+ATOM   5195  O   LEU B 263      -3.792  13.660  31.389  1.00 74.61           O  
+ANISOU 5195  O   LEU B 263     8714  12736   6897    329   1244    584       O  
+ATOM   5196  CB  LEU B 263      -6.961  13.920  30.330  1.00 65.32           C  
+ANISOU 5196  CB  LEU B 263     7670  11334   5814    333   1354    543       C  
+ATOM   5197  CG  LEU B 263      -7.837  14.245  29.115  1.00 66.26           C  
+ANISOU 5197  CG  LEU B 263     7937  11105   6135    313   1387    487       C  
+ATOM   5198  CD1 LEU B 263      -8.949  13.218  28.953  1.00 64.57           C  
+ANISOU 5198  CD1 LEU B 263     7737  10882   5913    305   1440    733       C  
+ATOM   5199  CD2 LEU B 263      -8.412  15.650  29.217  1.00 59.57           C  
+ANISOU 5199  CD2 LEU B 263     7062  10264   5308    340   1360    153       C  
+ATOM   5200  N   ASN B 264      -5.277  14.456  32.877  1.00 65.79           N  
+ANISOU 5200  N   ASN B 264     7390  12178   5431    397   1248    346       N  
+ATOM   5201  CA  ASN B 264      -4.529  13.988  34.036  1.00 66.67           C  
+ANISOU 5201  CA  ASN B 264     7335  12690   5307    408   1211    461       C  
+ATOM   5202  C   ASN B 264      -4.746  12.498  34.262  1.00 62.55           C  
+ANISOU 5202  C   ASN B 264     6764  12277   4725    370   1241    919       C  
+ATOM   5203  O   ASN B 264      -3.886  11.807  34.809  1.00 65.32           O  
+ANISOU 5203  O   ASN B 264     7023  12791   5006    352   1203   1135       O  
+ATOM   5204  CB  ASN B 264      -4.925  14.782  35.280  1.00 74.79           C  
+ANISOU 5204  CB  ASN B 264     8159  14215   6042    471   1183    183       C  
+ATOM   5205  CG  ASN B 264      -4.829  16.279  35.067  1.00 74.29           C  
+ANISOU 5205  CG  ASN B 264     8107  14010   6110    514   1133   -295       C  
+ATOM   5206  OD1 ASN B 264      -3.735  16.842  35.016  1.00 74.37           O  
+ANISOU 5206  OD1 ASN B 264     8120  13911   6225    522   1067   -465       O  
+ATOM   5207  ND2 ASN B 264      -5.977  16.932  34.935  1.00 72.99           N  
+ANISOU 5207  ND2 ASN B 264     7933  13827   5974    542   1154   -506       N  
+ATOM   5208  N   ASN B 265      -5.905  12.013  33.831  1.00 57.28           N  
+ANISOU 5208  N   ASN B 265     6144  11502   4119    356   1297   1072       N  
+ATOM   5209  CA  ASN B 265      -6.251  10.605  33.962  1.00 70.08           C  
+ANISOU 5209  CA  ASN B 265     7700  13170   5759    319   1313   1514       C  
+ATOM   5210  C   ASN B 265      -7.320  10.209  32.951  1.00 65.50           C  
+ANISOU 5210  C   ASN B 265     7248  12247   5393    302   1365   1605       C  
+ATOM   5211  O   ASN B 265      -8.023  11.063  32.412  1.00 85.81           O  
+ANISOU 5211  O   ASN B 265     9925  14670   8008    322   1397   1343       O  
+ATOM   5212  CB  ASN B 265      -6.721  10.301  35.387  1.00 71.64           C  
+ANISOU 5212  CB  ASN B 265     7649  13960   5613    330   1309   1682       C  
+ATOM   5213  CG  ASN B 265      -7.827  11.229  35.847  1.00 71.17           C  
+ANISOU 5213  CG  ASN B 265     7524  14179   5336    378   1350   1399       C  
+ATOM   5214  OD1 ASN B 265      -8.990  11.058  35.483  1.00 70.37           O  
+ANISOU 5214  OD1 ASN B 265     7462  13977   5298    374   1400   1460       O  
+ATOM   5215  ND2 ASN B 265      -7.466  12.228  36.645  1.00 62.97           N  
+ANISOU 5215  ND2 ASN B 265     6376  13479   4071    427   1317   1060       N  
+ATOM   5216  N   TYR B 266      -7.431   8.910  32.693  1.00 58.92           N  
+ANISOU 5216  N   TYR B 266     6388  11277   4720    267   1360   1974       N  
+ATOM   5217  CA  TYR B 266      -8.349   8.401  31.680  1.00 61.54           C  
+ANISOU 5217  CA  TYR B 266     6830  11260   5292    254   1395   2064       C  
+ATOM   5218  C   TYR B 266      -9.806   8.642  32.054  1.00 64.10           C  
+ANISOU 5218  C   TYR B 266     7100  11783   5471    272   1444   2057       C  
+ATOM   5219  O   TYR B 266     -10.662   8.800  31.182  1.00 66.78           O  
+ANISOU 5219  O   TYR B 266     7567  11847   5959    275   1480   1967       O  
+ATOM   5220  CB  TYR B 266      -8.108   6.909  31.453  1.00 60.09           C  
+ANISOU 5220  CB  TYR B 266     6576  10904   5350    219   1355   2449       C  
+ATOM   5221  CG  TYR B 266      -6.821   6.613  30.720  1.00 56.19           C  
+ANISOU 5221  CG  TYR B 266     6164  10102   5084    206   1315   2413       C  
+ATOM   5222  CD1 TYR B 266      -6.686   6.908  29.369  1.00 54.13           C  
+ANISOU 5222  CD1 TYR B 266     6094   9442   5031    211   1339   2193       C  
+ATOM   5223  CD2 TYR B 266      -5.737   6.051  31.380  1.00 56.98           C  
+ANISOU 5223  CD2 TYR B 266     6132  10337   5178    187   1252   2601       C  
+ATOM   5224  CE1 TYR B 266      -5.509   6.642  28.695  1.00 56.74           C  
+ANISOU 5224  CE1 TYR B 266     6478   9532   5548    200   1309   2147       C  
+ATOM   5225  CE2 TYR B 266      -4.557   5.783  30.715  1.00 55.62           C  
+ANISOU 5225  CE2 TYR B 266     6024   9887   5222    177   1217   2552       C  
+ATOM   5226  CZ  TYR B 266      -4.448   6.080  29.373  1.00 61.25           C  
+ANISOU 5226  CZ  TYR B 266     6923  10222   6128    186   1250   2316       C  
+ATOM   5227  OH  TYR B 266      -3.273   5.814  28.708  1.00 65.64           O  
+ANISOU 5227  OH  TYR B 266     7521  10542   6878    178   1222   2257       O  
+ATOM   5228  N   ASN B 267     -10.079   8.700  33.354  1.00 57.48           N  
+ANISOU 5228  N   ASN B 267     6061  11450   4328    283   1445   2142       N  
+ATOM   5229  CA  ASN B 267     -11.438   8.914  33.834  1.00 58.48           C  
+ANISOU 5229  CA  ASN B 267     6104  11816   4301    301   1486   2126       C  
+ATOM   5230  C   ASN B 267     -12.005  10.238  33.342  1.00 68.91           C  
+ANISOU 5230  C   ASN B 267     7556  13029   5598    341   1531   1691       C  
+ATOM   5231  O   ASN B 267     -13.212  10.359  33.115  1.00 65.40           O  
+ANISOU 5231  O   ASN B 267     7132  12544   5173    350   1575   1660       O  
+ATOM   5232  CB  ASN B 267     -11.471   8.870  35.363  1.00 67.58           C  
+ANISOU 5232  CB  ASN B 267     7017  13457   5205    309   1410   2174       C  
+ATOM   5233  CG  ASN B 267     -12.877   8.967  35.921  1.00 91.63           C  
+ANISOU 5233  CG  ASN B 267     9954  16711   8150    325   1417   2158       C  
+ATOM   5234  OD1 ASN B 267     -13.432  10.058  36.055  1.00102.45           O  
+ANISOU 5234  OD1 ASN B 267    11339  18206   9380    367   1451   1799       O  
+ATOM   5235  ND2 ASN B 267     -13.459   7.822  36.258  1.00110.18           N  
+ANISOU 5235  ND2 ASN B 267    12172  19102  10592    292   1378   2548       N  
+ATOM   5236  N   GLU B 268     -11.124  11.211  33.127  1.00 79.52           N  
+ANISOU 5236  N   GLU B 268     8984  14272   6956    360   1500   1362       N  
+ATOM   5237  CA  GLU B 268     -11.539  12.510  32.614  1.00 71.30           C  
+ANISOU 5237  CA  GLU B 268     8049  13059   5983    389   1508    954       C  
+ATOM   5238  C   GLU B 268     -12.237  12.378  31.266  1.00 68.73           C  
+ANISOU 5238  C   GLU B 268     7916  12255   5941    365   1536    985       C  
+ATOM   5239  O   GLU B 268     -13.182  13.124  30.989  1.00 63.71           O  
+ANISOU 5239  O   GLU B 268     7319  11547   5340    383   1556    777       O  
+ATOM   5240  CB  GLU B 268     -10.347  13.463  32.509  1.00 63.61           C  
+ANISOU 5240  CB  GLU B 268     7119  11995   5054    403   1452    658       C  
+ATOM   5241  CG  GLU B 268      -9.757  13.832  33.861  1.00 68.25           C  
+ANISOU 5241  CG  GLU B 268     7502  13080   5349    441   1414    527       C  
+ATOM   5242  CD  GLU B 268      -8.844  15.042  33.804  1.00 80.95           C  
+ANISOU 5242  CD  GLU B 268     9128  14599   7031    469   1349    143       C  
+ATOM   5243  OE1 GLU B 268      -8.628  15.668  34.864  1.00 89.66           O  
+ANISOU 5243  OE1 GLU B 268    10051  16104   7914    519   1310   -101       O  
+ATOM   5244  OE2 GLU B 268      -8.340  15.366  32.710  1.00 75.17           O  
+ANISOU 5244  OE2 GLU B 268     8568  13415   6578    441   1331     84       O  
+ATOM   5245  N   ILE B 269     -11.801  11.411  30.455  1.00 52.07           N  
+ANISOU 5245  N   ILE B 269     5906   9841   4036    328   1532   1233       N  
+ATOM   5246  CA  ILE B 269     -12.488  11.112  29.201  1.00 61.77           C  
+ANISOU 5246  CA  ILE B 269     7289  10670   5510    308   1556   1281       C  
+ATOM   5247  C   ILE B 269     -13.975  10.976  29.478  1.00 64.77           C  
+ANISOU 5247  C   ILE B 269     7613  11167   5830    321   1597   1345       C  
+ATOM   5248  O   ILE B 269     -14.793  11.727  28.930  1.00 60.05           O  
+ANISOU 5248  O   ILE B 269     7102  10417   5299    330   1616   1145       O  
+ATOM   5249  CB  ILE B 269     -11.977   9.817  28.536  1.00 49.51           C  
+ANISOU 5249  CB  ILE B 269     5775   8871   4166    279   1540   1562       C  
+ATOM   5250  CG1 ILE B 269     -10.510   9.957  28.125  1.00 57.38           C  
+ANISOU 5250  CG1 ILE B 269     6835   9726   5242    265   1505   1481       C  
+ATOM   5251  CG2 ILE B 269     -12.829   9.468  27.325  1.00 48.02           C  
+ANISOU 5251  CG2 ILE B 269     5710   8331   4204    269   1561   1587       C  
+ATOM   5252  CD1 ILE B 269      -9.933   8.703  27.495  1.00 48.42           C  
+ANISOU 5252  CD1 ILE B 269     5708   8360   4329    245   1482   1706       C  
+ATOM   5253  N   THR B 270     -14.302  10.060  30.388  1.00 62.40           N  
+ANISOU 5253  N   THR B 270     7145  11162   5403    319   1607   1636       N  
+ATOM   5254  CA  THR B 270     -15.684   9.815  30.768  1.00 62.17           C  
+ANISOU 5254  CA  THR B 270     7026  11295   5300    328   1649   1750       C  
+ATOM   5255  C   THR B 270     -16.371  11.118  31.135  1.00 70.89           C  
+ANISOU 5255  C   THR B 270     8112  12585   6239    366   1676   1393       C  
+ATOM   5256  O   THR B 270     -17.451  11.424  30.615  1.00 63.57           O  
+ANISOU 5256  O   THR B 270     7253  11493   5407    372   1704   1300       O  
+ATOM   5257  CB  THR B 270     -15.779   8.840  31.957  1.00 55.68           C  
+ANISOU 5257  CB  THR B 270     5965  10888   4300    316   1648   2118       C  
+ATOM   5258  OG1 THR B 270     -15.055   7.641  31.654  1.00 55.49           O  
+ANISOU 5258  OG1 THR B 270     5929  10667   4489    281   1600   2444       O  
+ATOM   5259  CG2 THR B 270     -17.228   8.494  32.252  1.00 56.59           C  
+ANISOU 5259  CG2 THR B 270     5994  11091   4418    317   1663   2246       C  
+ATOM   5260  N   GLU B 271     -15.708  11.913  31.973  1.00 55.08           N  
+ANISOU 5260  N   GLU B 271     6010  10895   4022    394   1656   1165       N  
+ATOM   5261  CA  GLU B 271     -16.313  13.142  32.463  1.00 63.08           C  
+ANISOU 5261  CA  GLU B 271     6950  12123   4895    440   1664    787       C  
+ATOM   5262  C   GLU B 271     -16.659  14.026  31.282  1.00 69.58           C  
+ANISOU 5262  C   GLU B 271     7963  12483   5993    437   1649    524       C  
+ATOM   5263  O   GLU B 271     -17.788  14.514  31.174  1.00 71.43           O  
+ANISOU 5263  O   GLU B 271     8189  12694   6258    455   1672    380       O  
+ATOM   5264  CB  GLU B 271     -15.386  13.880  33.431  1.00 68.68           C  
+ANISOU 5264  CB  GLU B 271     7520  13191   5384    477   1622    534       C  
+ATOM   5265  CG  GLU B 271     -14.579  12.979  34.343  1.00100.21           C  
+ANISOU 5265  CG  GLU B 271    11369  17534   9172    462   1605    828       C  
+ATOM   5266  CD  GLU B 271     -13.794  13.759  35.380  1.00111.84           C  
+ANISOU 5266  CD  GLU B 271    12689  19367  10437    502   1538    539       C  
+ATOM   5267  OE1 GLU B 271     -13.842  15.007  35.349  1.00112.34           O  
+ANISOU 5267  OE1 GLU B 271    12738  19465  10481    554   1538     97       O  
+ATOM   5268  OE2 GLU B 271     -13.123  13.125  36.220  1.00112.11           O  
+ANISOU 5268  OE2 GLU B 271    12599  19647  10351    485   1477    745       O  
+ATOM   5269  N   ILE B 272     -15.704  14.173  30.367  1.00 53.49           N  
+ANISOU 5269  N   ILE B 272     6083  10082   4160    409   1610    495       N  
+ATOM   5270  CA  ILE B 272     -15.922  14.999  29.192  1.00 52.40           C  
+ANISOU 5270  CA  ILE B 272     6105   9523   4282    393   1587    300       C  
+ATOM   5271  C   ILE B 272     -17.163  14.504  28.465  1.00 49.65           C  
+ANISOU 5271  C   ILE B 272     5843   8965   4056    376   1629    449       C  
+ATOM   5272  O   ILE B 272     -18.085  15.283  28.193  1.00 49.52           O  
+ANISOU 5272  O   ILE B 272     5842   8849   4122    385   1627    258       O  
+ATOM   5273  CB  ILE B 272     -14.706  14.977  28.249  1.00 61.21           C  
+ANISOU 5273  CB  ILE B 272     7362  10319   5575    355   1551    338       C  
+ATOM   5274  CG1 ILE B 272     -13.527  15.714  28.890  1.00 50.20           C  
+ANISOU 5274  CG1 ILE B 272     5886   9083   4106    374   1498    134       C  
+ATOM   5275  CG2 ILE B 272     -15.061  15.594  26.909  1.00 47.55           C  
+ANISOU 5275  CG2 ILE B 272     5786   8179   4103    323   1535    244       C  
+ATOM   5276  CD1 ILE B 272     -12.189  15.393  28.259  1.00 68.36           C  
+ANISOU 5276  CD1 ILE B 272     8281  11178   6514    339   1474    242       C  
+ATOM   5277  N   LEU B 273     -17.217  13.194  28.237  1.00 49.17           N  
+ANISOU 5277  N   LEU B 273     5810   8851   4021    354   1657    785       N  
+ATOM   5278  CA  LEU B 273     -18.338  12.606  27.523  1.00 70.26           C  
+ANISOU 5278  CA  LEU B 273     8553  11308   6834    341   1687    937       C  
+ATOM   5279  C   LEU B 273     -19.621  12.936  28.264  1.00 62.93           C  
+ANISOU 5279  C   LEU B 273     7508  10626   5777    370   1723    865       C  
+ATOM   5280  O   LEU B 273     -20.595  13.396  27.657  1.00 62.22           O  
+ANISOU 5280  O   LEU B 273     7489  10339   5811    370   1730    753       O  
+ATOM   5281  CB  LEU B 273     -18.166  11.093  27.383  1.00 57.73           C  
+ANISOU 5281  CB  LEU B 273     6951   9664   5319    322   1693   1299       C  
+ATOM   5282  CG  LEU B 273     -17.030  10.631  26.468  1.00 63.69           C  
+ANISOU 5282  CG  LEU B 273     7817  10138   6245    298   1658   1357       C  
+ATOM   5283  CD1 LEU B 273     -16.976   9.112  26.396  1.00 71.05           C  
+ANISOU 5283  CD1 LEU B 273     8690  11002   7305    288   1646   1688       C  
+ATOM   5284  CD2 LEU B 273     -17.189  11.233  25.080  1.00 52.43           C  
+ANISOU 5284  CD2 LEU B 273     6567   8352   5002    280   1649   1183       C  
+ATOM   5285  N   GLN B 274     -19.588  12.762  29.584  1.00 61.30           N  
+ANISOU 5285  N   GLN B 274     7108  10875   5308    395   1743    917       N  
+ATOM   5286  CA  GLN B 274     -20.751  13.035  30.414  1.00 61.92           C  
+ANISOU 5286  CA  GLN B 274     7034  11279   5215    427   1785    846       C  
+ATOM   5287  C   GLN B 274     -21.219  14.456  30.166  1.00 53.01           C  
+ANISOU 5287  C   GLN B 274     5936  10044   4160    454   1765    424       C  
+ATOM   5288  O   GLN B 274     -22.400  14.692  29.881  1.00 62.26           O  
+ANISOU 5288  O   GLN B 274     7122  11119   5415    461   1788    361       O  
+ATOM   5289  CB  GLN B 274     -20.429  12.829  31.896  1.00 55.82           C  
+ANISOU 5289  CB  GLN B 274     6019  11089   4101    452   1802    912       C  
+ATOM   5290  CG  GLN B 274     -20.613  11.402  32.382  1.00 76.54           C  
+ANISOU 5290  CG  GLN B 274     8528  13895   6659    422   1820   1386       C  
+ATOM   5291  CD  GLN B 274     -19.885  11.130  33.685  1.00 86.88           C  
+ANISOU 5291  CD  GLN B 274     9650  15591   7768    419   1743   1462       C  
+ATOM   5292  OE1 GLN B 274     -19.233  12.014  34.241  1.00 88.56           O  
+ANISOU 5292  OE1 GLN B 274     9805  16028   7814    451   1718   1163       O  
+ATOM   5293  NE2 GLN B 274     -19.994   9.902  34.178  1.00 90.61           N  
+ANISOU 5293  NE2 GLN B 274    10006  16149   8274    384   1695   1864       N  
+ATOM   5294  N   ARG B 275     -20.270  15.388  30.215  1.00 53.11           N  
+ANISOU 5294  N   ARG B 275     5955  10035   4188    467   1710    146       N  
+ATOM   5295  CA  ARG B 275     -20.586  16.796  30.047  1.00 53.32           C  
+ANISOU 5295  CA  ARG B 275     5969   9948   4343    492   1663   -264       C  
+ATOM   5296  C   ARG B 275     -21.277  16.988  28.711  1.00 60.43           C  
+ANISOU 5296  C   ARG B 275     7051  10364   5544    453   1651   -238       C  
+ATOM   5297  O   ARG B 275     -22.321  17.644  28.633  1.00 60.84           O  
+ANISOU 5297  O   ARG B 275     7067  10361   5687    469   1646   -423       O  
+ATOM   5298  CB  ARG B 275     -19.328  17.658  30.146  1.00 53.62           C  
+ANISOU 5298  CB  ARG B 275     5990   9957   4427    501   1588   -512       C  
+ATOM   5299  CG  ARG B 275     -18.735  17.690  31.544  1.00 90.04           C  
+ANISOU 5299  CG  ARG B 275    10391  15091   8730    550   1586   -625       C  
+ATOM   5300  CD  ARG B 275     -18.157  19.051  31.886  1.00 85.98           C  
+ANISOU 5300  CD  ARG B 275     9768  14608   8292    593   1496  -1077       C  
+ATOM   5301  NE  ARG B 275     -18.930  20.140  31.300  1.00 82.71           N  
+ANISOU 5301  NE  ARG B 275     9366  13894   8167    601   1446  -1368       N  
+ATOM   5302  CZ  ARG B 275     -18.459  21.368  31.114  1.00 77.12           C  
+ANISOU 5302  CZ  ARG B 275     8608  12987   7706    615   1341  -1711       C  
+ATOM   5303  NH1 ARG B 275     -17.221  21.662  31.484  1.00 61.92           N  
+ANISOU 5303  NH1 ARG B 275     6628  11146   5754    629   1282  -1824       N  
+ATOM   5304  NH2 ARG B 275     -19.226  22.304  30.571  1.00 75.71           N  
+ANISOU 5304  NH2 ARG B 275     8419  12519   7829    615   1283  -1933       N  
+ATOM   5305  N   ILE B 276     -20.722  16.364  27.675  1.00 49.42           N  
+ANISOU 5305  N   ILE B 276     5835   8647   4295    404   1646     -4       N  
+ATOM   5306  CA  ILE B 276     -21.275  16.499  26.340  1.00 48.76           C  
+ANISOU 5306  CA  ILE B 276     5916   8142   4469    364   1630     36       C  
+ATOM   5307  C   ILE B 276     -22.727  16.049  26.370  1.00 52.66           C  
+ANISOU 5307  C   ILE B 276     6392   8657   4958    375   1680    132       C  
+ATOM   5308  O   ILE B 276     -23.620  16.780  25.923  1.00 50.30           O  
+ANISOU 5308  O   ILE B 276     6115   8185   4810    372   1659    -22       O  
+ATOM   5309  CB  ILE B 276     -20.486  15.674  25.305  1.00 48.07           C  
+ANISOU 5309  CB  ILE B 276     5985   7795   4483    320   1629    278       C  
+ATOM   5310  CG1 ILE B 276     -19.074  16.239  25.138  1.00 58.30           C  
+ANISOU 5310  CG1 ILE B 276     7303   9033   5813    303   1579    174       C  
+ATOM   5311  CG2 ILE B 276     -21.216  15.651  23.972  1.00 47.26           C  
+ANISOU 5311  CG2 ILE B 276     6026   7337   4593    284   1620    339       C  
+ATOM   5312  CD1 ILE B 276     -18.146  15.339  24.351  1.00 54.76           C  
+ANISOU 5312  CD1 ILE B 276     6966   8427   5413    270   1585    393       C  
+ATOM   5313  N   GLU B 277     -22.964  14.886  26.975  1.00 58.21           N  
+ANISOU 5313  N   GLU B 277     7028   9588   5502    386   1737    393       N  
+ATOM   5314  CA  GLU B 277     -24.310  14.336  27.036  1.00 71.31           C  
+ANISOU 5314  CA  GLU B 277     8654  11277   7166    394   1784    532       C  
+ATOM   5315  C   GLU B 277     -25.223  15.337  27.720  1.00 67.96           C  
+ANISOU 5315  C   GLU B 277     8098  11054   6668    432   1793    245       C  
+ATOM   5316  O   GLU B 277     -26.325  15.618  27.233  1.00 72.30           O  
+ANISOU 5316  O   GLU B 277     8688  11425   7360    430   1797    186       O  
+ATOM   5317  CB  GLU B 277     -24.331  12.996  27.775  1.00 49.54           C  
+ANISOU 5317  CB  GLU B 277     5784   8784   4256    397   1830    877       C  
+ATOM   5318  CG  GLU B 277     -25.722  12.390  27.904  1.00 51.92           C  
+ANISOU 5318  CG  GLU B 277     6022   9131   4575    403   1876   1054       C  
+ATOM   5319  CD  GLU B 277     -25.712  11.030  28.575  1.00 60.56           C  
+ANISOU 5319  CD  GLU B 277     6978  10453   5578    395   1903   1453       C  
+ATOM   5320  OE1 GLU B 277     -26.722  10.303  28.462  1.00 82.68           O  
+ANISOU 5320  OE1 GLU B 277     9742  13199   8474    389   1925   1674       O  
+ATOM   5321  OE2 GLU B 277     -24.698  10.689  29.220  1.00 71.98           O  
+ANISOU 5321  OE2 GLU B 277     8339  12127   6882    391   1893   1563       O  
+ATOM   5322  N   ASN B 278     -24.730  15.913  28.816  1.00 51.79           N  
+ANISOU 5322  N   ASN B 278     5885   9378   4415    470   1789     37       N  
+ATOM   5323  CA  ASN B 278     -25.496  16.901  29.559  1.00 53.59           C  
+ANISOU 5323  CA  ASN B 278     5945   9847   4569    520   1789   -304       C  
+ATOM   5324  C   ASN B 278     -25.929  18.000  28.608  1.00 55.35           C  
+ANISOU 5324  C   ASN B 278     6268   9652   5112    507   1722   -564       C  
+ATOM   5325  O   ASN B 278     -27.128  18.269  28.461  1.00 59.07           O  
+ANISOU 5325  O   ASN B 278     6715  10054   5677    516   1735   -645       O  
+ATOM   5326  CB  ASN B 278     -24.674  17.475  30.717  1.00 61.15           C  
+ANISOU 5326  CB  ASN B 278     6712  11226   5296    567   1768   -557       C  
+ATOM   5327  CG  ASN B 278     -25.511  18.296  31.680  1.00 83.85           C  
+ANISOU 5327  CG  ASN B 278     9352  14469   8038    633   1778   -917       C  
+ATOM   5328  OD1 ASN B 278     -26.379  17.767  32.375  1.00 81.75           O  
+ANISOU 5328  OD1 ASN B 278     8948  14559   7555    653   1854   -803       O  
+ATOM   5329  ND2 ASN B 278     -25.253  19.598  31.727  1.00 97.82           N  
+ANISOU 5329  ND2 ASN B 278    11051  16159   9957    667   1694  -1361       N  
+ATOM   5330  N   ASN B 279     -24.950  18.566  27.903  1.00 54.12           N  
+ANISOU 5330  N   ASN B 279     6220   9204   5138    477   1648   -648       N  
+ATOM   5331  CA  ASN B 279     -25.191  19.680  26.995  1.00 63.49           C  
+ANISOU 5331  CA  ASN B 279     7472   9997   6653    452   1563   -856       C  
+ATOM   5332  C   ASN B 279     -26.312  19.389  26.012  1.00 68.64           C  
+ANISOU 5332  C   ASN B 279     8253  10346   7479    416   1579   -694       C  
+ATOM   5333  O   ASN B 279     -27.036  20.295  25.599  1.00 76.72           O  
+ANISOU 5333  O   ASN B 279     9258  11156   8735    409   1522   -883       O  
+ATOM   5334  CB  ASN B 279     -23.916  20.039  26.231  1.00 59.71           C  
+ANISOU 5334  CB  ASN B 279     7104   9251   6331    407   1493   -834       C  
+ATOM   5335  CG  ASN B 279     -22.894  20.743  27.098  1.00 60.02           C  
+ANISOU 5335  CG  ASN B 279     6997   9506   6302    445   1441  -1095       C  
+ATOM   5336  OD1 ASN B 279     -23.201  21.182  28.207  1.00 65.86           O  
+ANISOU 5336  OD1 ASN B 279     7537  10576   6911    509   1440  -1366       O  
+ATOM   5337  ND2 ASN B 279     -21.673  20.866  26.592  1.00 66.00           N  
+ANISOU 5337  ND2 ASN B 279     7837  10095   7145    409   1395  -1032       N  
+ATOM   5338  N   ILE B 280     -26.460  18.122  25.643  1.00 62.45           N  
+ANISOU 5338  N   ILE B 280     7583   9536   6611    394   1644   -351       N  
+ATOM   5339  CA  ILE B 280     -27.513  17.756  24.715  1.00 64.17           C  
+ANISOU 5339  CA  ILE B 280     7915   9479   6987    366   1654   -200       C  
+ATOM   5340  C   ILE B 280     -28.836  17.633  25.462  1.00 74.64           C  
+ANISOU 5340  C   ILE B 280     9114  11018   8228    406   1710   -244       C  
+ATOM   5341  O   ILE B 280     -29.816  18.327  25.154  1.00 91.22           O  
+ANISOU 5341  O   ILE B 280    11201  12962  10499    406   1681   -402       O  
+ATOM   5342  CB  ILE B 280     -27.197  16.428  23.996  1.00 58.97           C  
+ANISOU 5342  CB  ILE B 280     7399   8690   6318    335   1687    148       C  
+ATOM   5343  CG1 ILE B 280     -25.834  16.505  23.301  1.00 57.99           C  
+ANISOU 5343  CG1 ILE B 280     7379   8406   6248    299   1643    182       C  
+ATOM   5344  CG2 ILE B 280     -28.302  16.070  23.013  1.00 50.87           C  
+ANISOU 5344  CG2 ILE B 280     6478   7386   5463    313   1687    271       C  
+ATOM   5345  CD1 ILE B 280     -25.757  17.552  22.217  1.00 53.41           C  
+ANISOU 5345  CD1 ILE B 280     6884   7509   5900    253   1565     56       C  
+ATOM   5346  N   LYS B 281     -28.828  16.814  26.508  1.00 73.65           N  
+ANISOU 5346  N   LYS B 281     8867  11279   7836    439   1783   -109       N  
+ATOM   5347  CA  LYS B 281     -30.070  16.378  27.131  1.00 73.38           C  
+ANISOU 5347  CA  LYS B 281     8713  11470   7698    467   1851    -37       C  
+ATOM   5348  C   LYS B 281     -30.779  17.528  27.829  1.00 68.91           C  
+ANISOU 5348  C   LYS B 281     7974  11097   7111    513   1843   -419       C  
+ATOM   5349  O   LYS B 281     -32.001  17.523  27.966  1.00 75.69           O  
+ANISOU 5349  O   LYS B 281     8767  12000   7993    529   1878   -441       O  
+ATOM   5350  CB  LYS B 281     -29.795  15.245  28.124  1.00 68.50           C  
+ANISOU 5350  CB  LYS B 281     7968  11261   6798    481   1922    244       C  
+ATOM   5351  CG  LYS B 281     -29.741  13.862  27.487  1.00 64.36           C  
+ANISOU 5351  CG  LYS B 281     7557  10532   6365    444   1935    662       C  
+ATOM   5352  CD  LYS B 281     -29.555  12.766  28.527  1.00 73.15           C  
+ANISOU 5352  CD  LYS B 281     8499  12044   7249    451   1988    977       C  
+ATOM   5353  CE  LYS B 281     -30.818  12.556  29.342  1.00 72.45           C  
+ANISOU 5353  CE  LYS B 281     8222  12279   7027    474   2055   1056       C  
+ATOM   5354  NZ  LYS B 281     -31.899  11.933  28.529  1.00 78.41           N  
+ANISOU 5354  NZ  LYS B 281     9065  12702   8025    455   2058   1251       N  
+ATOM   5355  N   THR B 282     -30.011  18.531  28.236  1.00 65.45           N  
+ANISOU 5355  N   THR B 282     7452  10755   6663    537   1786   -741       N  
+ATOM   5356  CA  THR B 282     -30.575  19.678  28.933  1.00 68.76           C  
+ANISOU 5356  CA  THR B 282     7669  11358   7100    592   1758  -1172       C  
+ATOM   5357  C   THR B 282     -31.180  20.731  28.007  1.00 63.71           C  
+ANISOU 5357  C   THR B 282     7092  10262   6852    571   1667  -1394       C  
+ATOM   5358  O   THR B 282     -31.670  21.754  28.484  1.00 75.97           O  
+ANISOU 5358  O   THR B 282     8466  11897   8504    617   1621  -1783       O  
+ATOM   5359  CB  THR B 282     -29.512  20.367  29.812  1.00 72.32           C  
+ANISOU 5359  CB  THR B 282     7960  12104   7413    637   1715  -1474       C  
+ATOM   5360  OG1 THR B 282     -28.414  20.791  28.995  1.00 81.62           O  
+ANISOU 5360  OG1 THR B 282     9289  12913   8811    594   1627  -1479       O  
+ATOM   5361  CG2 THR B 282     -29.004  19.413  30.880  1.00 75.41           C  
+ANISOU 5361  CG2 THR B 282     8240  13022   7390    660   1800  -1272       C  
+ATOM   5362  N   LYS B 283     -31.156  20.502  26.695  1.00 67.47           N  
+ANISOU 5362  N   LYS B 283     7796  10277   7561    504   1631  -1159       N  
+ATOM   5363  CA  LYS B 283     -31.726  21.505  25.794  1.00 85.47           C  
+ANISOU 5363  CA  LYS B 283    10118  12140  10216    472   1533  -1321       C  
+ATOM   5364  C   LYS B 283     -33.125  21.129  25.301  1.00 82.86           C  
+ANISOU 5364  C   LYS B 283     9846  11654   9983    458   1568  -1188       C  
+ATOM   5365  O   LYS B 283     -33.773  21.898  24.587  1.00 76.96           O  
+ANISOU 5365  O   LYS B 283     9118  10579   9544    431   1489  -1298       O  
+ATOM   5366  CB  LYS B 283     -30.789  21.768  24.616  1.00 81.96           C  
+ANISOU 5366  CB  LYS B 283     9847  11306   9987    402   1448  -1192       C  
+ATOM   5367  CG  LYS B 283     -30.586  23.260  24.354  1.00 87.36           C  
+ANISOU 5367  CG  LYS B 283    10433  11746  11014    388   1309  -1499       C  
+ATOM   5368  CD  LYS B 283     -29.690  23.522  23.158  1.00 87.97           C  
+ANISOU 5368  CD  LYS B 283    10659  11470  11297    308   1227  -1319       C  
+ATOM   5369  CE  LYS B 283     -30.292  22.956  21.886  1.00 91.40           C  
+ANISOU 5369  CE  LYS B 283    11286  11623  11818    242   1238  -1004       C  
+ATOM   5370  NZ  LYS B 283     -31.447  23.742  21.385  1.00 99.85           N  
+ANISOU 5370  NZ  LYS B 283    12309  12431  13198    218   1160  -1102       N  
+ATOM   5371  N   THR B 284     -33.586  19.943  25.684  1.00 74.14           N  
+ANISOU 5371  N   THR B 284     8753  10778   8638    474   1677   -933       N  
+ATOM   5372  CA  THR B 284     -34.969  19.549  25.441  1.00 69.73           C  
+ANISOU 5372  CA  THR B 284     8208  10139   8147    474   1719   -826       C  
+ATOM   5373  C   THR B 284     -35.711  19.470  26.772  1.00 70.23           C  
+ANISOU 5373  C   THR B 284     8035  10675   7975    540   1803   -963       C  
+ATOM   5374  O   THR B 284     -35.369  18.665  27.639  1.00 62.64           O  
+ANISOU 5374  O   THR B 284     6985  10113   6702    564   1886   -804       O  
+ATOM   5375  CB  THR B 284     -35.062  18.204  24.708  1.00 62.81           C  
+ANISOU 5375  CB  THR B 284     7511   9110   7245    436   1764   -401       C  
+ATOM   5376  OG1 THR B 284     -34.520  18.342  23.389  1.00 67.12           O  
+ANISOU 5376  OG1 THR B 284     8254   9246   8002    377   1686   -311       O  
+ATOM   5377  CG2 THR B 284     -36.510  17.756  24.607  1.00 58.30           C  
+ANISOU 5377  CG2 THR B 284     6923   8493   6736    443   1808   -295       C  
+ATOM   5378  N   VAL B 285     -36.722  20.317  26.930  1.00 66.76           N  
+ANISOU 5378  N   VAL B 285     7472  10207   7687    567   1778  -1253       N  
+ATOM   5379  CA  VAL B 285     -37.422  20.454  28.202  1.00 66.05           C  
+ANISOU 5379  CA  VAL B 285     7116  10604   7375    637   1851  -1469       C  
+ATOM   5380  C   VAL B 285     -38.787  19.773  28.186  1.00 67.31           C  
+ANISOU 5380  C   VAL B 285     7259  10798   7517    638   1931  -1272       C  
+ATOM   5381  O   VAL B 285     -39.527  19.872  27.208  1.00 70.21           O  
+ANISOU 5381  O   VAL B 285     7763  10740   8172    602   1887  -1205       O  
+ATOM   5382  CB  VAL B 285     -37.615  21.942  28.565  1.00 71.74           C  
+ANISOU 5382  CB  VAL B 285     7644  11329   8287    684   1763  -2011       C  
+ATOM   5383  CG1 VAL B 285     -38.215  22.084  29.956  1.00 81.88           C  
+ANISOU 5383  CG1 VAL B 285     8618  13206   9289    769   1843  -2288       C  
+ATOM   5384  CG2 VAL B 285     -36.292  22.685  28.475  1.00 77.20           C  
+ANISOU 5384  CG2 VAL B 285     8346  11913   9075    679   1663  -2204       C  
+ATOM   5385  N   PHE B 286     -39.114  19.078  29.273  1.00 68.11           N  
+ANISOU 5385  N   PHE B 286     7179  11423   7278    676   2044  -1160       N  
+ATOM   5386  CA  PHE B 286     -40.447  18.515  29.450  1.00 65.61           C  
+ANISOU 5386  CA  PHE B 286     6786  11213   6929    684   2123  -1000       C  
+ATOM   5387  C   PHE B 286     -41.288  19.431  30.333  1.00 69.65           C  
+ANISOU 5387  C   PHE B 286     7019  12064   7381    752   2147  -1437       C  
+ATOM   5388  O   PHE B 286     -40.927  19.708  31.477  1.00 65.29           O  
+ANISOU 5388  O   PHE B 286     6226  12052   6528    807   2187  -1663       O  
+ATOM   5389  CB  PHE B 286     -40.372  17.113  30.057  1.00 63.13           C  
+ANISOU 5389  CB  PHE B 286     6411  11265   6309    674   2229   -541       C  
+ATOM   5390  CG  PHE B 286     -41.713  16.529  30.401  1.00 62.13           C  
+ANISOU 5390  CG  PHE B 286     6154  11322   6129    683   2315   -358       C  
+ATOM   5391  CD1 PHE B 286     -42.601  16.162  29.404  1.00 59.50           C  
+ANISOU 5391  CD1 PHE B 286     5987  10523   6096    648   2292   -171       C  
+ATOM   5392  CD2 PHE B 286     -42.082  16.338  31.722  1.00 69.22           C  
+ANISOU 5392  CD2 PHE B 286     6748  12884   6667    725   2416   -362       C  
+ATOM   5393  CE1 PHE B 286     -43.835  15.625  29.717  1.00 60.16           C  
+ANISOU 5393  CE1 PHE B 286     5944  10761   6154    656   2368      5       C  
+ATOM   5394  CE2 PHE B 286     -43.314  15.798  32.041  1.00 69.82           C  
+ANISOU 5394  CE2 PHE B 286     6686  13147   6695    729   2498   -167       C  
+ATOM   5395  CZ  PHE B 286     -44.192  15.443  31.037  1.00 63.06           C  
+ANISOU 5395  CZ  PHE B 286     6006  11782   6172    694   2473     17       C  
+ATOM   5396  N   LEU B 287     -42.408  19.902  29.795  1.00 71.30           N  
+ANISOU 5396  N   LEU B 287     7245  11969   7875    750   2116  -1573       N  
+ATOM   5397  CA  LEU B 287     -43.304  20.771  30.548  1.00 64.20           C  
+ANISOU 5397  CA  LEU B 287     6073  11350   6972    817   2131  -2013       C  
+ATOM   5398  C   LEU B 287     -44.453  19.977  31.160  1.00 76.16           C  
+ANISOU 5398  C   LEU B 287     7435  13235   8267    834   2262  -1802       C  
+ATOM   5399  O   LEU B 287     -45.388  19.577  30.466  1.00 81.65           O  
+ANISOU 5399  O   LEU B 287     8249  13604   9169    800   2269  -1582       O  
+ATOM   5400  CB  LEU B 287     -43.845  21.886  29.653  1.00 64.32           C  
+ANISOU 5400  CB  LEU B 287     6155  10812   7470    804   2002  -2323       C  
+ATOM   5401  CG  LEU B 287     -42.814  22.912  29.177  1.00 62.91           C  
+ANISOU 5401  CG  LEU B 287     6042  10308   7553    791   1856  -2593       C  
+ATOM   5402  CD1 LEU B 287     -43.476  24.006  28.351  1.00 63.02           C  
+ANISOU 5402  CD1 LEU B 287     6071   9800   8075    772   1720  -2857       C  
+ATOM   5403  CD2 LEU B 287     -42.057  23.503  30.357  1.00 68.11           C  
+ANISOU 5403  CD2 LEU B 287     6440  11461   7978    866   1857  -2991       C  
+ATOM   5404  N   SER B 288     -44.370  19.751  32.467  1.00 77.72           N  
+ANISOU 5404  N   SER B 288     7352  14138   8039    887   2363  -1859       N  
+ATOM   5405  CA  SER B 288     -45.383  18.993  33.191  1.00 78.43           C  
+ANISOU 5405  CA  SER B 288     7244  14688   7870    901   2496  -1629       C  
+ATOM   5406  C   SER B 288     -46.378  19.906  33.894  1.00 77.61           C  
+ANISOU 5406  C   SER B 288     6838  14915   7735    977   2525  -2130       C  
+ATOM   5407  O   SER B 288     -45.986  20.875  34.542  1.00 77.21           O  
+ANISOU 5407  O   SER B 288     6663  15022   7652   1015   2418  -2581       O  
+ATOM   5408  CB  SER B 288     -44.721  18.070  34.213  1.00 72.02           C  
+ANISOU 5408  CB  SER B 288     6307  14453   6606    890   2562  -1289       C  
+ATOM   5409  OG  SER B 288     -45.689  17.421  35.018  1.00 74.41           O  
+ANISOU 5409  OG  SER B 288     6449  15104   6719    876   2602  -1037       O  
+ATOM   5410  N   GLY B 289     -47.666  19.599  33.768  1.00 61.30           N  
+ANISOU 5410  N   GLY B 289     6881  11168   5244   -776   1340  -1894       N  
+ATOM   5411  CA  GLY B 289     -48.672  20.350  34.494  1.00 68.37           C  
+ANISOU 5411  CA  GLY B 289     7733  12028   6216   -593   1660  -2100       C  
+ATOM   5412  C   GLY B 289     -50.066  20.390  33.898  1.00 70.12           C  
+ANISOU 5412  C   GLY B 289     7669  12127   6846   -490   1838  -1938       C  
+ATOM   5413  O   GLY B 289     -50.243  20.369  32.681  1.00 75.16           O  
+ANISOU 5413  O   GLY B 289     8130  12596   7832   -523   1668  -1753       O  
+ATOM   5414  N   SER B 290     -51.059  20.429  34.781  1.00 69.87           N  
+ANISOU 5414  N   SER B 290     7593  12194   6760   -345   2185  -2008       N  
+ATOM   5415  CA  SER B 290     -52.451  20.636  34.400  1.00 76.72           C  
+ANISOU 5415  CA  SER B 290     8195  12934   8019   -221   2397  -1917       C  
+ATOM   5416  C   SER B 290     -53.096  21.537  35.448  1.00 75.21           C  
+ANISOU 5416  C   SER B 290     8068  12748   7759    -35   2714  -2203       C  
+ATOM   5417  O   SER B 290     -52.681  21.530  36.604  1.00 72.55           O  
+ANISOU 5417  O   SER B 290     7946  12610   7010     17   2830  -2382       O  
+ATOM   5418  CB  SER B 290     -53.198  19.308  34.289  1.00 83.52           C  
+ANISOU 5418  CB  SER B 290     8853  13940   8939   -246   2519  -1583       C  
+ATOM   5419  OG  SER B 290     -53.124  18.582  35.504  1.00 87.75           O  
+ANISOU 5419  OG  SER B 290     9517  14759   9067   -224   2744  -1560       O  
+ATOM   5420  N   ALA B 291     -54.101  22.315  35.059  1.00 68.64           N  
+ANISOU 5420  N   ALA B 291     7055  11711   7313     86   2848  -2255       N  
+ATOM   5421  CA  ALA B 291     -54.730  23.227  36.011  1.00 70.21           C  
+ANISOU 5421  CA  ALA B 291     7309  11904   7464    274   3141  -2538       C  
+ATOM   5422  C   ALA B 291     -56.153  23.631  35.642  1.00 75.45           C  
+ANISOU 5422  C   ALA B 291     7711  12408   8548    408   3367  -2481       C  
+ATOM   5423  O   ALA B 291     -56.455  23.903  34.481  1.00 74.30           O  
+ANISOU 5423  O   ALA B 291     7381  12039   8812    383   3220  -2374       O  
+ATOM   5424  CB  ALA B 291     -53.870  24.466  36.181  1.00 72.42           C  
+ANISOU 5424  CB  ALA B 291     7783  12034   7698    288   2982  -2901       C  
+ATOM   5425  N   VAL B 292     -57.019  23.669  36.650  1.00 75.10           N  
+ANISOU 5425  N   VAL B 292     7653  12492   8389    572   3730  -2552       N  
+ATOM   5426  CA  VAL B 292     -58.346  24.257  36.511  1.00 81.70           C  
+ANISOU 5426  CA  VAL B 292     8276  13176   9590    725   3977  -2572       C  
+ATOM   5427  C   VAL B 292     -58.361  25.578  37.277  1.00 99.35           C  
+ANISOU 5427  C   VAL B 292    10668  15347  11734    884   4103  -2968       C  
+ATOM   5428  O   VAL B 292     -58.967  26.560  36.850  1.00 97.62           O  
+ANISOU 5428  O   VAL B 292    10335  14893  11864    968   4143  -3094       O  
+ATOM   5429  CB  VAL B 292     -59.446  23.310  37.034  1.00 81.99           C  
+ANISOU 5429  CB  VAL B 292     8137  13382   9635    811   4325  -2331       C  
+ATOM   5430  CG1 VAL B 292     -60.808  23.984  36.986  1.00 81.43           C  
+ANISOU 5430  CG1 VAL B 292     7883  13129   9929    984   4554  -2344       C  
+ATOM   5431  CG2 VAL B 292     -59.461  22.020  36.227  1.00 75.82           C  
+ANISOU 5431  CG2 VAL B 292     7164  12629   9014    657   4179  -1962       C  
+ATOM   5432  N   GLU B 293     -57.656  25.595  38.402  1.00103.78           N  
+ANISOU 5432  N   GLU B 293    11491  16121  11821    933   4147  -3178       N  
+ATOM   5433  CA  GLU B 293     -57.465  26.812  39.179  1.00 98.66           C  
+ANISOU 5433  CA  GLU B 293    11019  15422  11045   1086   4196  -3595       C  
+ATOM   5434  C   GLU B 293     -55.981  27.113  39.126  1.00 95.16           C  
+ANISOU 5434  C   GLU B 293    10793  14951  10410    960   3853  -3812       C  
+ATOM   5435  O   GLU B 293     -55.170  26.212  38.915  1.00 85.80           O  
+ANISOU 5435  O   GLU B 293     9680  13891   9029    799   3663  -3629       O  
+ATOM   5436  CB  GLU B 293     -57.943  26.653  40.621  1.00 99.44           C  
+ANISOU 5436  CB  GLU B 293    11298  15702  10783   1307   4439  -3579       C  
+ATOM   5437  N   TYR B 294     -55.609  28.374  39.281  1.00103.45           N  
+ANISOU 5437  N   TYR B 294    11935  15815  11556   1027   3758  -4192       N  
+ATOM   5438  CA  TYR B 294     -54.204  28.712  39.132  1.00 91.42           C  
+ANISOU 5438  CA  TYR B 294    10582  14206   9949    897   3413  -4386       C  
+ATOM   5439  C   TYR B 294     -53.612  29.459  40.316  1.00 97.70           C  
+ANISOU 5439  C   TYR B 294    11619  15056  10447   1040   3377  -4821       C  
+ATOM   5440  O   TYR B 294     -53.229  30.616  40.183  1.00100.32           O  
+ANISOU 5440  O   TYR B 294    11961  15139  11017   1061   3247  -5156       O  
+ATOM   5441  CB  TYR B 294     -54.013  29.541  37.871  1.00 82.33           C  
+ANISOU 5441  CB  TYR B 294     9291  12666   9326    791   3195  -4366       C  
+ATOM   5442  CG  TYR B 294     -54.393  28.830  36.591  1.00 81.03           C  
+ANISOU 5442  CG  TYR B 294     8915  12419   9453    661   3122  -3922       C  
+ATOM   5443  CD1 TYR B 294     -53.450  28.124  35.855  1.00 85.76           C  
+ANISOU 5443  CD1 TYR B 294     9544  13030  10012    466   2834  -3696       C  
+ATOM   5444  CD2 TYR B 294     -55.694  28.879  36.112  1.00 80.55           C  
+ANISOU 5444  CD2 TYR B 294     8620  12270   9713    751   3328  -3748       C  
+ATOM   5445  CE1 TYR B 294     -53.789  27.495  34.673  1.00 89.34           C  
+ANISOU 5445  CE1 TYR B 294     9802  13418  10727    380   2744  -3319       C  
+ATOM   5446  CE2 TYR B 294     -56.048  28.243  34.936  1.00 78.82           C  
+ANISOU 5446  CE2 TYR B 294     8199  11981   9769    662   3233  -3380       C  
+ATOM   5447  CZ  TYR B 294     -55.092  27.551  34.222  1.00 86.42           C  
+ANISOU 5447  CZ  TYR B 294     9197  12966  10673    485   2937  -3173       C  
+ATOM   5448  OH  TYR B 294     -55.442  26.920  33.052  1.00 83.92           O  
+ANISOU 5448  OH  TYR B 294     8677  12593  10616    429   2823  -2833       O  
+ATOM   5449  N   ASN B 295     -53.509  28.780  41.454  1.00 95.83           N  
+ANISOU 5449  N   ASN B 295    11590  15076   9744   1139   3432  -4724       N  
+ATOM   5450  CA  ASN B 295     -52.924  29.363  42.656  1.00101.46           C  
+ANISOU 5450  CA  ASN B 295    12569  15817  10164   1294   3333  -5023       C  
+ATOM   5451  C   ASN B 295     -53.459  30.739  43.065  1.00 99.54           C  
+ANISOU 5451  C   ASN B 295    12312  15387  10122   1489   3421  -5381       C  
+ATOM   5452  O   ASN B 295     -54.577  30.866  43.576  1.00104.49           O  
+ANISOU 5452  O   ASN B 295    12902  16072  10728   1683   3714  -5330       O  
+ATOM   5453  CB  ASN B 295     -51.409  29.463  42.480  1.00107.79           C  
+ANISOU 5453  CB  ASN B 295    13509  16546  10901   1128   2948  -5183       C  
+ATOM   5454  N   HIS B 296     -52.635  31.763  42.856  1.00100.31           N  
+ANISOU 5454  N   HIS B 296    12438  15244  10432   1438   3161  -5732       N  
+ATOM   5455  CA  HIS B 296     -52.981  33.116  43.265  1.00104.20           C  
+ANISOU 5455  CA  HIS B 296    12924  15529  11138   1609   3190  -6093       C  
+ATOM   5456  C   HIS B 296     -53.053  34.099  42.102  1.00 99.96           C  
+ANISOU 5456  C   HIS B 296    12159  14618  11204   1503   3122  -6233       C  
+ATOM   5457  O   HIS B 296     -52.915  35.308  42.291  1.00106.58           O  
+ANISOU 5457  O   HIS B 296    12995  15210  12292   1583   3032  -6565       O  
+ATOM   5458  CB  HIS B 296     -51.968  33.615  44.297  1.00111.06           C  
+ANISOU 5458  CB  HIS B 296    14035  16403  11759   1695   2948  -6415       C  
+ATOM   5459  N   TRP B 297     -53.244  33.576  40.896  1.00 95.94           N  
+ANISOU 5459  N   TRP B 297    11455  14050  10948   1333   3161  -5964       N  
+ATOM   5460  CA  TRP B 297     -53.361  34.418  39.714  1.00100.89           C  
+ANISOU 5460  CA  TRP B 297    11860  14306  12168   1256   3127  -6023       C  
+ATOM   5461  C   TRP B 297     -54.719  34.239  39.060  1.00115.64           C  
+ANISOU 5461  C   TRP B 297    13506  16137  14295   1299   3392  -5713       C  
+ATOM   5462  O   TRP B 297     -55.423  33.262  39.318  1.00118.31           O  
+ANISOU 5462  O   TRP B 297    13823  16749  14378   1334   3596  -5456       O  
+ATOM   5463  CB  TRP B 297     -52.241  34.104  38.723  1.00 93.62           C  
+ANISOU 5463  CB  TRP B 297    10926  13240  11405   1012   2819  -5839       C  
+ATOM   5464  CG  TRP B 297     -51.023  34.917  38.983  1.00 97.76           C  
+ANISOU 5464  CG  TRP B 297    11557  13572  12015    978   2555  -6231       C  
+ATOM   5465  CD1 TRP B 297     -50.932  35.988  39.819  1.00105.68           C  
+ANISOU 5465  CD1 TRP B 297    12633  14448  13074   1124   2517  -6623       C  
+ATOM   5466  CD2 TRP B 297     -49.706  34.703  38.457  1.00 97.07           C  
+ANISOU 5466  CD2 TRP B 297    11525  13379  11977    777   2237  -6164       C  
+ATOM   5467  NE1 TRP B 297     -49.652  36.478  39.824  1.00110.31           N  
+ANISOU 5467  NE1 TRP B 297    13289  14841  13784   1025   2205  -6833       N  
+ATOM   5468  CE2 TRP B 297     -48.879  35.706  39.002  1.00 95.70           C  
+ANISOU 5468  CE2 TRP B 297    11427  13008  11929    820   2058  -6621       C  
+ATOM   5469  CE3 TRP B 297     -49.150  33.773  37.574  1.00 98.79           C  
+ANISOU 5469  CE3 TRP B 297    11729  13641  12166    570   2074  -5747       C  
+ATOM   5470  CZ2 TRP B 297     -47.523  35.803  38.692  1.00 96.60           C  
+ANISOU 5470  CZ2 TRP B 297    11589  12959  12155    659   1745  -6684       C  
+ATOM   5471  CZ3 TRP B 297     -47.800  33.873  37.268  1.00 96.17           C  
+ANISOU 5471  CZ3 TRP B 297    11463  13165  11912    417   1770  -5808       C  
+ATOM   5472  CH2 TRP B 297     -47.004  34.880  37.827  1.00102.79           C  
+ANISOU 5472  CH2 TRP B 297    12364  13800  12891    459   1620  -6286       C  
+ATOM   5473  N   GLU B 298     -55.078  35.205  38.223  1.00121.85           N  
+ANISOU 5473  N   GLU B 298    14120  16564  15613   1303   3380  -5719       N  
+ATOM   5474  CA  GLU B 298     -56.292  35.162  37.423  1.00116.72           C  
+ANISOU 5474  CA  GLU B 298    13244  15816  15287   1338   3568  -5413       C  
+ATOM   5475  C   GLU B 298     -56.094  34.173  36.284  1.00 99.20           C  
+ANISOU 5475  C   GLU B 298    10928  13615  13149   1156   3420  -4942       C  
+ATOM   5476  O   GLU B 298     -55.005  34.093  35.721  1.00 97.14           O  
+ANISOU 5476  O   GLU B 298    10719  13254  12936   1004   3144  -4877       O  
+ATOM   5477  CB  GLU B 298     -56.646  36.554  36.891  1.00123.89           C  
+ANISOU 5477  CB  GLU B 298    14011  16334  16728   1418   3586  -5582       C  
+ATOM   5478  CG  GLU B 298     -58.063  36.685  36.351  1.00124.05           C  
+ANISOU 5478  CG  GLU B 298    13813  16278  17043   1522   3830  -5372       C  
+ATOM   5479  CD  GLU B 298     -58.756  37.959  36.812  1.00134.93           C  
+ANISOU 5479  CD  GLU B 298    15169  17465  18636   1694   3964  -5643       C  
+ATOM   5480  OE1 GLU B 298     -58.295  39.064  36.442  1.00136.14           O  
+ANISOU 5480  OE1 GLU B 298    15288  17291  19148   1690   3832  -5828       O  
+ATOM   5481  OE2 GLU B 298     -59.771  37.858  37.536  1.00143.45           O  
+ANISOU 5481  OE2 GLU B 298    16267  18708  19529   1830   4179  -5616       O  
+ATOM   5482  N   THR B 299     -57.138  33.412  35.967  1.00 88.80           N  
+ANISOU 5482  N   THR B 299     9462  12424  11852   1183   3600  -4625       N  
+ATOM   5483  CA  THR B 299     -57.059  32.347  34.966  1.00 88.37           C  
+ANISOU 5483  CA  THR B 299     9302  12427  11847   1039   3464  -4194       C  
+ATOM   5484  C   THR B 299     -56.363  32.839  33.705  1.00 88.70           C  
+ANISOU 5484  C   THR B 299     9274  12176  12253    944   3189  -4081       C  
+ATOM   5485  O   THR B 299     -55.446  32.193  33.180  1.00 87.60           O  
+ANISOU 5485  O   THR B 299     9187  12081  12016    792   2945  -3892       O  
+ATOM   5486  CB  THR B 299     -58.453  31.823  34.570  1.00 87.25           C  
+ANISOU 5486  CB  THR B 299     8930  12336  11883   1117   3684  -3920       C  
+ATOM   5487  OG1 THR B 299     -58.956  30.964  35.598  1.00 93.75           O  
+ANISOU 5487  OG1 THR B 299     9803  13472  12344   1168   3920  -3888       O  
+ATOM   5488  CG2 THR B 299     -58.375  31.032  33.252  1.00 78.85           C  
+ANISOU 5488  CG2 THR B 299     7711  11232  11016   1001   3480  -3526       C  
+ATOM   5489  N   GLU B 300     -56.788  34.008  33.239  1.00 95.45           N  
+ANISOU 5489  N   GLU B 300    10010  12731  13527   1049   3241  -4191       N  
+ATOM   5490  CA  GLU B 300     -56.224  34.580  32.032  1.00100.56           C  
+ANISOU 5490  CA  GLU B 300    10571  13082  14556   1006   3030  -4060       C  
+ATOM   5491  C   GLU B 300     -54.746  34.897  32.278  1.00 95.01           C  
+ANISOU 5491  C   GLU B 300    10046  12297  13756    885   2796  -4245       C  
+ATOM   5492  O   GLU B 300     -53.892  34.553  31.471  1.00 87.39           O  
+ANISOU 5492  O   GLU B 300     9087  11278  12840    768   2564  -4024       O  
+ATOM   5493  CB  GLU B 300     -57.019  35.824  31.606  1.00111.83           C  
+ANISOU 5493  CB  GLU B 300    11835  14205  16449   1166   3173  -4157       C  
+ATOM   5494  CG  GLU B 300     -58.523  35.574  31.235  1.00112.87           C  
+ANISOU 5494  CG  GLU B 300    11762  14385  16740   1297   3391  -3970       C  
+ATOM   5495  CD  GLU B 300     -59.454  35.240  32.420  1.00125.72           C  
+ANISOU 5495  CD  GLU B 300    13418  16249  18099   1376   3674  -4123       C  
+ATOM   5496  OE1 GLU B 300     -58.982  35.149  33.578  1.00130.23           O  
+ANISOU 5496  OE1 GLU B 300    14184  16988  18312   1354   3713  -4372       O  
+ATOM   5497  OE2 GLU B 300     -60.668  35.029  32.186  1.00124.57           O  
+ANISOU 5497  OE2 GLU B 300    13095  16133  18101   1478   3860  -3983       O  
+ATOM   5498  N   HIS B 301     -54.443  35.430  33.455  1.00 98.49           N  
+ANISOU 5498  N   HIS B 301    10638  12765  14017    922   2853  -4652       N  
+ATOM   5499  CA  HIS B 301     -53.085  35.826  33.809  1.00 92.99           C  
+ANISOU 5499  CA  HIS B 301    10097  11973  13261    828   2632  -4902       C  
+ATOM   5500  C   HIS B 301     -52.136  34.622  33.821  1.00 88.44           C  
+ANISOU 5500  C   HIS B 301     9661  11647  12297    654   2429  -4717       C  
+ATOM   5501  O   HIS B 301     -50.993  34.702  33.358  1.00 92.99           O  
+ANISOU 5501  O   HIS B 301    10282  12087  12961    530   2182  -4680       O  
+ATOM   5502  CB  HIS B 301     -53.100  36.524  35.174  1.00 88.00           C  
+ANISOU 5502  CB  HIS B 301     9594  11379  12464    945   2738  -5408       C  
+ATOM   5503  CG  HIS B 301     -51.942  37.447  35.396  1.00 91.10           C  
+ANISOU 5503  CG  HIS B 301    10059  11518  13037    906   2531  -5754       C  
+ATOM   5504  ND1 HIS B 301     -51.027  37.244  36.395  1.00 95.37           N  
+ANISOU 5504  ND1 HIS B 301    10802  12224  13209    874   2394  -6067       N  
+ATOM   5505  CD2 HIS B 301     -51.615  38.613  34.798  1.00 93.07           C  
+ANISOU 5505  CD2 HIS B 301    10189  11352  13822    916   2454  -5855       C  
+ATOM   5506  CE1 HIS B 301     -50.145  38.234  36.382  1.00 92.94           C  
+ANISOU 5506  CE1 HIS B 301    10488  11599  13225    852   2216  -6362       C  
+ATOM   5507  NE2 HIS B 301     -50.481  39.077  35.427  1.00 93.90           N  
+ANISOU 5507  NE2 HIS B 301    10411  11358  13908    872   2260  -6230       N  
+ATOM   5508  N   ALA B 302     -52.613  33.520  34.391  1.00 86.26           N  
+ANISOU 5508  N   ALA B 302     9445  11727  11601    653   2546  -4602       N  
+ATOM   5509  CA  ALA B 302     -51.833  32.300  34.407  1.00 89.30           C  
+ANISOU 5509  CA  ALA B 302     9949  12366  11614    497   2379  -4400       C  
+ATOM   5510  C   ALA B 302     -51.622  31.887  32.963  1.00 87.98           C  
+ANISOU 5510  C   ALA B 302     9645  12077  11707    391   2202  -3987       C  
+ATOM   5511  O   ALA B 302     -50.529  31.452  32.590  1.00 81.88           O  
+ANISOU 5511  O   ALA B 302     8954  11318  10838    244   1956  -3870       O  
+ATOM   5512  CB  ALA B 302     -52.533  31.215  35.176  1.00 87.90           C  
+ANISOU 5512  CB  ALA B 302     9816  12561  11021    536   2579  -4300       C  
+ATOM   5513  N   GLU B 303     -52.656  32.086  32.142  1.00 91.61           N  
+ANISOU 5513  N   GLU B 303     9894  12412  12503    486   2321  -3782       N  
+ATOM   5514  CA  GLU B 303     -52.541  31.738  30.732  1.00 83.53           C  
+ANISOU 5514  CA  GLU B 303     8729  11285  11723    442   2153  -3400       C  
+ATOM   5515  C   GLU B 303     -51.451  32.559  30.032  1.00 85.53           C  
+ANISOU 5515  C   GLU B 303     8999  11242  12259    397   1939  -3414       C  
+ATOM   5516  O   GLU B 303     -50.705  32.020  29.198  1.00 76.94           O  
+ANISOU 5516  O   GLU B 303     7911  10159  11166    303   1719  -3143       O  
+ATOM   5517  CB  GLU B 303     -53.878  31.913  30.003  1.00 90.88           C  
+ANISOU 5517  CB  GLU B 303     9424  12127  12980    593   2315  -3223       C  
+ATOM   5518  CG  GLU B 303     -54.962  30.884  30.363  1.00 97.19           C  
+ANISOU 5518  CG  GLU B 303    10143  13199  13587    625   2494  -3091       C  
+ATOM   5519  CD  GLU B 303     -56.258  31.142  29.612  1.00 96.90           C  
+ANISOU 5519  CD  GLU B 303     9857  13042  13918    782   2633  -2948       C  
+ATOM   5520  OE1 GLU B 303     -56.339  32.178  28.919  1.00 94.85           O  
+ANISOU 5520  OE1 GLU B 303     9509  12506  14024    881   2615  -2975       O  
+ATOM   5521  OE2 GLU B 303     -57.193  30.320  29.709  1.00 94.73           O  
+ANISOU 5521  OE2 GLU B 303     9463  12941  13590    815   2764  -2808       O  
+ATOM   5522  N   GLN B 304     -51.304  33.831  30.400  1.00 94.01           N  
+ANISOU 5522  N   GLN B 304    10084  12056  13580    464   2002  -3729       N  
+ATOM   5523  CA  GLN B 304     -50.245  34.628  29.797  1.00 91.93           C  
+ANISOU 5523  CA  GLN B 304     9814  11481  13632    422   1821  -3741       C  
+ATOM   5524  C   GLN B 304     -48.895  34.147  30.334  1.00 83.51           C  
+ANISOU 5524  C   GLN B 304     8947  10529  12255    247   1603  -3853       C  
+ATOM   5525  O   GLN B 304     -47.911  34.082  29.582  1.00 82.52           O  
+ANISOU 5525  O   GLN B 304     8822  10281  12251    156   1394  -3665       O  
+ATOM   5526  CB  GLN B 304     -50.448  36.139  30.074  1.00 97.99           C  
+ANISOU 5526  CB  GLN B 304    10517  11911  14803    540   1945  -4067       C  
+ATOM   5527  CG  GLN B 304     -51.893  36.591  30.347  1.00106.36           C  
+ANISOU 5527  CG  GLN B 304    11464  12967  15979    711   2225  -4170       C  
+ATOM   5528  CD  GLN B 304     -52.026  38.126  30.386  1.00122.24           C  
+ANISOU 5528  CD  GLN B 304    13384  14598  18464    829   2322  -4441       C  
+ATOM   5529  OE1 GLN B 304     -51.722  38.815  29.419  1.00131.33           O  
+ANISOU 5529  OE1 GLN B 304    14409  15438  20051    864   2266  -4282       O  
+ATOM   5530  NE2 GLN B 304     -52.499  38.652  31.505  1.00127.34           N  
+ANISOU 5530  NE2 GLN B 304    14086  15272  19026    909   2478  -4841       N  
+ATOM   5531  N   PHE B 305     -48.876  33.677  31.582  1.00 83.72           N  
+ANISOU 5531  N   PHE B 305     9138  10826  11846    214   1654  -4113       N  
+ATOM   5532  CA  PHE B 305     -47.617  33.190  32.158  1.00 85.64           C  
+ANISOU 5532  CA  PHE B 305     9578  11204  11759     65   1445  -4241       C  
+ATOM   5533  C   PHE B 305     -47.118  31.942  31.426  1.00 83.05           C  
+ANISOU 5533  C   PHE B 305     9272  11064  11217    -77   1268  -3831       C  
+ATOM   5534  O   PHE B 305     -45.978  31.920  30.945  1.00 75.48           O  
+ANISOU 5534  O   PHE B 305     8358   9996  10327   -193   1039  -3745       O  
+ATOM   5535  CB  PHE B 305     -47.755  32.892  33.661  1.00 89.27           C  
+ANISOU 5535  CB  PHE B 305    10215  11954  11749    104   1550  -4590       C  
+ATOM   5536  CG  PHE B 305     -46.701  31.950  34.194  1.00 89.02           C  
+ANISOU 5536  CG  PHE B 305    10383  12184  11255    -37   1362  -4608       C  
+ATOM   5537  CD1 PHE B 305     -45.356  32.288  34.160  1.00 91.36           C  
+ANISOU 5537  CD1 PHE B 305    10765  12323  11625   -147   1107  -4760       C  
+ATOM   5538  CD2 PHE B 305     -47.058  30.715  34.705  1.00 81.86           C  
+ANISOU 5538  CD2 PHE B 305     9566  11671   9867    -55   1449  -4458       C  
+ATOM   5539  CE1 PHE B 305     -44.389  31.412  34.636  1.00 90.14           C  
+ANISOU 5539  CE1 PHE B 305    10795  12415  11041   -273    928  -4777       C  
+ATOM   5540  CE2 PHE B 305     -46.099  29.836  35.183  1.00 80.99           C  
+ANISOU 5540  CE2 PHE B 305     9639  11807   9328   -176   1284  -4460       C  
+ATOM   5541  CZ  PHE B 305     -44.762  30.186  35.148  1.00 83.26           C  
+ANISOU 5541  CZ  PHE B 305    10024  11949   9664   -285   1017  -4626       C  
+ATOM   5542  N   ILE B 306     -47.974  30.930  31.309  1.00 71.50           N  
+ANISOU 5542  N   ILE B 306     7763   9867   9536    -61   1374  -3577       N  
+ATOM   5543  CA  ILE B 306     -47.626  29.712  30.587  1.00 72.76           C  
+ANISOU 5543  CA  ILE B 306     7919  10208   9519   -178   1208  -3192       C  
+ATOM   5544  C   ILE B 306     -47.261  30.011  29.135  1.00 72.19           C  
+ANISOU 5544  C   ILE B 306     7711   9888   9830   -173   1044  -2894       C  
+ATOM   5545  O   ILE B 306     -46.235  29.529  28.619  1.00 67.07           O  
+ANISOU 5545  O   ILE B 306     7123   9258   9103   -292    812  -2712       O  
+ATOM   5546  CB  ILE B 306     -48.784  28.698  30.613  1.00 72.47           C  
+ANISOU 5546  CB  ILE B 306     7791  10435   9309   -133   1370  -2976       C  
+ATOM   5547  CG1 ILE B 306     -49.221  28.425  32.054  1.00 72.81           C  
+ANISOU 5547  CG1 ILE B 306     7956  10727   8980    -97   1581  -3232       C  
+ATOM   5548  CG2 ILE B 306     -48.366  27.402  29.940  1.00 68.63           C  
+ANISOU 5548  CG2 ILE B 306     7300  10139   8639   -256   1175  -2616       C  
+ATOM   5549  CD1 ILE B 306     -50.372  27.453  32.167  1.00 67.67           C  
+ANISOU 5549  CD1 ILE B 306     7196  10311   8205    -49   1776  -3018       C  
+ATOM   5550  N   HIS B 307     -48.098  30.817  28.485  1.00 78.34           N  
+ANISOU 5550  N   HIS B 307     8308  10442  11014    -16   1173  -2838       N  
+ATOM   5551  CA  HIS B 307     -47.856  31.197  27.098  1.00 76.06           C  
+ANISOU 5551  CA  HIS B 307     7880   9920  11099     50   1056  -2545       C  
+ATOM   5552  C   HIS B 307     -46.445  31.748  26.869  1.00 77.97           C  
+ANISOU 5552  C   HIS B 307     8201   9941  11483    -40    867  -2580       C  
+ATOM   5553  O   HIS B 307     -45.678  31.192  26.069  1.00 74.94           O  
+ANISOU 5553  O   HIS B 307     7827   9587  11059   -103    664  -2291       O  
+ATOM   5554  CB  HIS B 307     -48.905  32.220  26.648  1.00 78.54           C  
+ANISOU 5554  CB  HIS B 307     8008   9994  11838    252   1252  -2563       C  
+ATOM   5555  CG  HIS B 307     -48.773  32.646  25.217  1.00 82.00           C  
+ANISOU 5555  CG  HIS B 307     8294  10208  12654    375   1167  -2245       C  
+ATOM   5556  ND1 HIS B 307     -47.689  33.354  24.746  1.00 85.51           N  
+ANISOU 5556  ND1 HIS B 307     8752  10386  13350    357   1049  -2202       N  
+ATOM   5557  CD2 HIS B 307     -49.598  32.474  24.156  1.00 83.15           C  
+ANISOU 5557  CD2 HIS B 307     8262  10358  12973    545   1189  -1953       C  
+ATOM   5558  CE1 HIS B 307     -47.848  33.596  23.457  1.00 89.72           C  
+ANISOU 5558  CE1 HIS B 307     9133  10781  14176    521   1021  -1871       C  
+ATOM   5559  NE2 HIS B 307     -48.999  33.072  23.075  1.00 87.37           N  
+ANISOU 5559  NE2 HIS B 307     8723  10653  13822    645   1093  -1728       N  
+ATOM   5560  N   GLN B 308     -46.075  32.811  27.577  1.00 86.33           N  
+ANISOU 5560  N   GLN B 308     9308  10777  12716    -43    923  -2939       N  
+ATOM   5561  CA  GLN B 308     -44.795  33.437  27.261  1.00 92.39           C  
+ANISOU 5561  CA  GLN B 308    10099  11272  13734   -112    757  -2960       C  
+ATOM   5562  C   GLN B 308     -43.592  32.716  27.879  1.00 94.20           C  
+ANISOU 5562  C   GLN B 308    10526  11676  13590   -312    547  -3063       C  
+ATOM   5563  O   GLN B 308     -42.460  32.860  27.392  1.00106.68           O  
+ANISOU 5563  O   GLN B 308    12121  13093  15321   -392    367  -2957       O  
+ATOM   5564  CB  GLN B 308     -44.822  34.909  27.664  1.00 99.01           C  
+ANISOU 5564  CB  GLN B 308    10872  11750  14997    -31    877  -3303       C  
+ATOM   5565  CG  GLN B 308     -45.862  35.692  26.867  1.00105.73           C  
+ANISOU 5565  CG  GLN B 308    11516  12384  16273    171   1068  -3149       C  
+ATOM   5566  CD  GLN B 308     -45.339  37.007  26.327  1.00116.84           C  
+ANISOU 5566  CD  GLN B 308    12794  13332  18268    242   1081  -3166       C  
+ATOM   5567  OE1 GLN B 308     -44.130  37.229  26.271  1.00123.18           O  
+ANISOU 5567  OE1 GLN B 308    13635  13964  19205    139    924  -3190       O  
+ATOM   5568  NE2 GLN B 308     -46.249  37.882  25.912  1.00124.19           N  
+ANISOU 5568  NE2 GLN B 308    13559  14049  19578    425   1277  -3139       N  
+ATOM   5569  N   LEU B 309     -43.832  31.919  28.920  1.00 90.83           N  
+ANISOU 5569  N   LEU B 309    10245  11584  12680   -378    578  -3242       N  
+ATOM   5570  CA  LEU B 309     -42.791  31.023  29.414  1.00 90.46           C  
+ANISOU 5570  CA  LEU B 309    10387  11766  12219   -553    380  -3272       C  
+ATOM   5571  C   LEU B 309     -42.397  30.085  28.287  1.00 82.84           C  
+ANISOU 5571  C   LEU B 309     9388  10900  11189   -623    210  -2804       C  
+ATOM   5572  O   LEU B 309     -41.211  29.900  28.001  1.00 77.88           O  
+ANISOU 5572  O   LEU B 309     8829  10220  10540   -742     -1  -2720       O  
+ATOM   5573  CB  LEU B 309     -43.255  30.220  30.628  1.00 88.40           C  
+ANISOU 5573  CB  LEU B 309    10272  11880  11434   -573    478  -3467       C  
+ATOM   5574  CG  LEU B 309     -42.264  29.143  31.081  1.00 74.07           C  
+ANISOU 5574  CG  LEU B 309     8649  10344   9151   -740    286  -3443       C  
+ATOM   5575  CD1 LEU B 309     -40.934  29.764  31.478  1.00 75.99           C  
+ANISOU 5575  CD1 LEU B 309     8999  10405   9469   -826     93  -3735       C  
+ATOM   5576  CD2 LEU B 309     -42.835  28.310  32.219  1.00 79.08           C  
+ANISOU 5576  CD2 LEU B 309     9409  11360   9276   -723    427  -3571       C  
+ATOM   5577  N   SER B 310     -43.403  29.487  27.656  1.00 78.13           N  
+ANISOU 5577  N   SER B 310     8677  10445  10565   -537    297  -2512       N  
+ATOM   5578  CA  SER B 310     -43.157  28.626  26.505  1.00 76.44           C  
+ANISOU 5578  CA  SER B 310     8405  10326  10315   -558    129  -2077       C  
+ATOM   5579  C   SER B 310     -42.460  29.397  25.385  1.00 76.99           C  
+ANISOU 5579  C   SER B 310     8379  10073  10802   -495     22  -1877       C  
+ATOM   5580  O   SER B 310     -41.513  28.900  24.761  1.00 75.93           O  
+ANISOU 5580  O   SER B 310     8284   9965  10599   -572   -186  -1638       O  
+ATOM   5581  CB  SER B 310     -44.466  28.031  25.987  1.00 66.66           C  
+ANISOU 5581  CB  SER B 310     7016   9243   9069   -434    241  -1849       C  
+ATOM   5582  OG  SER B 310     -45.090  27.230  26.974  1.00 74.11           O  
+ANISOU 5582  OG  SER B 310     8028  10480   9650   -488    357  -1977       O  
+ATOM   5583  N   LYS B 311     -42.923  30.623  25.148  1.00 74.42           N  
+ANISOU 5583  N   LYS B 311     7922   9440  10913   -346    177  -1967       N  
+ATOM   5584  CA  LYS B 311     -42.430  31.408  24.020  1.00 77.18           C  
+ANISOU 5584  CA  LYS B 311     8147   9470  11707   -239    131  -1729       C  
+ATOM   5585  C   LYS B 311     -40.942  31.773  24.178  1.00 86.15           C  
+ANISOU 5585  C   LYS B 311     9374  10416  12945   -380    -28  -1813       C  
+ATOM   5586  O   LYS B 311     -40.214  31.841  23.183  1.00 90.42           O  
+ANISOU 5586  O   LYS B 311     9858  10817  13681   -344   -141  -1499       O  
+ATOM   5587  CB  LYS B 311     -43.276  32.670  23.834  1.00 82.94           C  
+ANISOU 5587  CB  LYS B 311     8715   9904  12896    -48    355  -1826       C  
+ATOM   5588  CG  LYS B 311     -42.917  33.483  22.591  1.00 87.81           C  
+ANISOU 5588  CG  LYS B 311     9177  10194  13992    113    353  -1525       C  
+ATOM   5589  CD  LYS B 311     -43.355  34.933  22.712  1.00 98.33           C  
+ANISOU 5589  CD  LYS B 311    10382  11160  15821    243    564  -1723       C  
+ATOM   5590  CE  LYS B 311     -42.566  35.825  21.763  1.00109.50           C  
+ANISOU 5590  CE  LYS B 311    11674  12197  17733    346    555  -1482       C  
+ATOM   5591  NZ  LYS B 311     -43.186  37.169  21.591  1.00123.59           N  
+ANISOU 5591  NZ  LYS B 311    13289  13628  20040    527    781  -1566       N  
+ATOM   5592  N   GLU B 312     -40.456  31.992  25.399  1.00 85.78           N  
+ANISOU 5592  N   GLU B 312     9462  10365  12768   -522    -45  -2228       N  
+ATOM   5593  CA  GLU B 312     -39.024  32.296  25.501  1.00 85.83           C  
+ANISOU 5593  CA  GLU B 312     9533  10181  12899   -653   -219  -2311       C  
+ATOM   5594  C   GLU B 312     -38.258  31.043  25.978  1.00 83.98           C  
+ANISOU 5594  C   GLU B 312     9497  10286  12127   -849   -425  -2306       C  
+ATOM   5595  O   GLU B 312     -37.031  31.044  26.121  1.00 98.22           O  
+ANISOU 5595  O   GLU B 312    11380  12003  13937   -982   -600  -2369       O  
+ATOM   5596  CB  GLU B 312     -38.775  33.516  26.417  1.00 94.94           C  
+ANISOU 5596  CB  GLU B 312    10677  11033  14362   -662   -149  -2792       C  
+ATOM   5597  CG  GLU B 312     -37.298  33.776  26.787  1.00100.58           C  
+ANISOU 5597  CG  GLU B 312    11464  11569  15184   -815   -348  -2985       C  
+ATOM   5598  CD  GLU B 312     -37.033  35.132  27.417  1.00109.59           C  
+ANISOU 5598  CD  GLU B 312    12527  12322  16790   -786   -295  -3423       C  
+ATOM   5599  OE1 GLU B 312     -37.752  36.094  27.083  1.00123.22           O  
+ANISOU 5599  OE1 GLU B 312    14087  13783  18949   -633   -108  -3424       O  
+ATOM   5600  OE2 GLU B 312     -36.105  35.230  28.254  1.00117.52           O  
+ANISOU 5600  OE2 GLU B 312    13631  13286  17736   -909   -452  -3781       O  
+ATOM   5601  N   LEU B 313     -38.971  29.932  26.124  1.00 82.93           N  
+ANISOU 5601  N   LEU B 313     9425  10529  11555   -862   -406  -2192       N  
+ATOM   5602  CA  LEU B 313     -38.279  28.653  26.125  1.00 76.23           C  
+ANISOU 5602  CA  LEU B 313     8716   9983  10267  -1016   -606  -2023       C  
+ATOM   5603  C   LEU B 313     -37.839  28.428  24.689  1.00 85.34           C  
+ANISOU 5603  C   LEU B 313     9770  11051  11605   -965   -736  -1556       C  
+ATOM   5604  O   LEU B 313     -36.702  28.045  24.428  1.00 72.44           O  
+ANISOU 5604  O   LEU B 313     8213   9424   9887  -1081   -934  -1427       O  
+ATOM   5605  CB  LEU B 313     -39.157  27.516  26.640  1.00 69.22           C  
+ANISOU 5605  CB  LEU B 313     7893   9495   8913  -1037   -540  -2005       C  
+ATOM   5606  CG  LEU B 313     -39.041  27.320  28.154  1.00 73.89           C  
+ANISOU 5606  CG  LEU B 313     8665  10277   9133  -1133   -497  -2415       C  
+ATOM   5607  CD1 LEU B 313     -39.984  26.233  28.640  1.00 80.08           C  
+ANISOU 5607  CD1 LEU B 313     9485  11434   9509  -1128   -382  -2353       C  
+ATOM   5608  CD2 LEU B 313     -37.599  27.009  28.545  1.00 57.54           C  
+ANISOU 5608  CD2 LEU B 313     6763   8246   6853  -1308   -728  -2518       C  
+ATOM   5609  N   ILE B 314     -38.742  28.698  23.754  1.00 84.34           N  
+ANISOU 5609  N   ILE B 314     9470  10844  11732   -767   -623  -1306       N  
+ATOM   5610  CA  ILE B 314     -38.414  28.553  22.342  1.00 74.92           C  
+ANISOU 5610  CA  ILE B 314     8173   9581  10712   -651   -731   -858       C  
+ATOM   5611  C   ILE B 314     -37.415  29.633  21.903  1.00 79.16           C  
+ANISOU 5611  C   ILE B 314     8654   9725  11699   -623   -749   -812       C  
+ATOM   5612  O   ILE B 314     -36.537  29.371  21.077  1.00 82.52           O  
+ANISOU 5612  O   ILE B 314     9075  10116  12163   -618   -899   -500       O  
+ATOM   5613  CB  ILE B 314     -39.684  28.610  21.467  1.00 70.05           C  
+ANISOU 5613  CB  ILE B 314     7377   8986  10252   -406   -606   -629       C  
+ATOM   5614  CG1 ILE B 314     -40.562  27.388  21.743  1.00 63.78           C  
+ANISOU 5614  CG1 ILE B 314     6608   8571   9053   -438   -622   -611       C  
+ATOM   5615  CG2 ILE B 314     -39.333  28.682  19.987  1.00 59.67           C  
+ANISOU 5615  CG2 ILE B 314     5947   7568   9158   -218   -700   -186       C  
+ATOM   5616  CD1 ILE B 314     -39.915  26.072  21.354  1.00 49.20           C  
+ANISOU 5616  CD1 ILE B 314     4844   7001   6849   -542   -866   -363       C  
+ATOM   5617  N   ARG B 315     -37.525  30.833  22.472  1.00 79.65           N  
+ANISOU 5617  N   ARG B 315     8663   9485  12114   -602   -596  -1123       N  
+ATOM   5618  CA  ARG B 315     -36.618  31.925  22.103  1.00 80.39           C  
+ANISOU 5618  CA  ARG B 315     8669   9159  12718   -574   -591  -1096       C  
+ATOM   5619  C   ARG B 315     -35.139  31.657  22.415  1.00 86.99           C  
+ANISOU 5619  C   ARG B 315     9623   9957  13471   -781   -801  -1157       C  
+ATOM   5620  O   ARG B 315     -34.263  32.112  21.682  1.00105.51           O  
+ANISOU 5620  O   ARG B 315    11886  12036  16168   -746   -848   -924       O  
+ATOM   5621  CB  ARG B 315     -37.042  33.225  22.787  1.00 81.63           C  
+ANISOU 5621  CB  ARG B 315     8742   9002  13273   -527   -400  -1481       C  
+ATOM   5622  N   LYS B 316     -34.852  30.927  23.490  1.00 89.02           N  
+ANISOU 5622  N   LYS B 316     9442  13081  11301  -1426   2226  -1353       N  
+ATOM   5623  CA  LYS B 316     -33.461  30.614  23.816  1.00 84.41           C  
+ANISOU 5623  CA  LYS B 316     8609  12823  10639  -1473   2251  -1336       C  
+ATOM   5624  C   LYS B 316     -33.119  29.210  23.307  1.00 82.04           C  
+ANISOU 5624  C   LYS B 316     8326  12752  10095  -1242   2364  -1159       C  
+ATOM   5625  O   LYS B 316     -32.417  28.442  23.966  1.00 80.32           O  
+ANISOU 5625  O   LYS B 316     7956  12830   9732  -1129   2351  -1189       O  
+ATOM   5626  CB  LYS B 316     -33.197  30.745  25.326  1.00 91.69           C  
+ANISOU 5626  CB  LYS B 316     9376  13931  11532  -1511   2119  -1601       C  
+ATOM   5627  CG  LYS B 316     -31.716  30.651  25.728  1.00108.26           C  
+ANISOU 5627  CG  LYS B 316    11168  16373  13594  -1600   2097  -1604       C  
+ATOM   5628  CD  LYS B 316     -31.015  31.997  25.681  1.00108.19           C  
+ANISOU 5628  CD  LYS B 316    10998  16264  13846  -1931   2049  -1677       C  
+ATOM   5629  CE  LYS B 316     -29.499  31.825  25.637  1.00111.99           C  
+ANISOU 5629  CE  LYS B 316    11147  17099  14306  -2027   2074  -1591       C  
+ATOM   5630  NZ  LYS B 316     -29.059  30.731  24.718  1.00119.48           N  
+ANISOU 5630  NZ  LYS B 316    12065  18240  15091  -1811   2241  -1328       N  
+ATOM   5631  N   ASP B 317     -33.653  28.876  22.135  1.00 78.33           N  
+ANISOU 5631  N   ASP B 317     8054  12131   9578  -1159   2462   -981       N  
+ATOM   5632  CA  ASP B 317     -33.262  27.664  21.421  1.00 78.75           C  
+ANISOU 5632  CA  ASP B 317     8146  12353   9423   -959   2591   -822       C  
+ATOM   5633  C   ASP B 317     -33.515  26.373  22.211  1.00 77.32           C  
+ANISOU 5633  C   ASP B 317     8017  12316   9046   -715   2556   -888       C  
+ATOM   5634  O   ASP B 317     -32.832  25.372  22.001  1.00 84.13           O  
+ANISOU 5634  O   ASP B 317     8833  13370   9764   -536   2637   -805       O  
+ATOM   5635  CB  ASP B 317     -31.782  27.753  21.029  1.00 84.03           C  
+ANISOU 5635  CB  ASP B 317     8554  13272  10100  -1028   2697   -722       C  
+ATOM   5636  CG  ASP B 317     -31.435  26.880  19.839  1.00 93.39           C  
+ANISOU 5636  CG  ASP B 317     9810  14556  11118   -866   2877   -544       C  
+ATOM   5637  OD1 ASP B 317     -32.281  26.739  18.930  1.00 92.90           O  
+ANISOU 5637  OD1 ASP B 317    10010  14294  10994   -827   2922   -456       O  
+ATOM   5638  OD2 ASP B 317     -30.314  26.331  19.820  1.00 97.98           O  
+ANISOU 5638  OD2 ASP B 317    10175  15428  11626   -768   2969   -506       O  
+ATOM   5639  N   PHE B 318     -34.493  26.384  23.113  1.00 76.59           N  
+ANISOU 5639  N   PHE B 318     8022  12128   8951   -700   2445  -1030       N  
+ATOM   5640  CA  PHE B 318     -34.854  25.155  23.819  1.00 72.35           C  
+ANISOU 5640  CA  PHE B 318     7571  11697   8220   -498   2419  -1052       C  
+ATOM   5641  C   PHE B 318     -35.908  24.370  23.054  1.00 68.15           C  
+ANISOU 5641  C   PHE B 318     7317  10978   7599   -381   2470   -963       C  
+ATOM   5642  O   PHE B 318     -36.602  24.903  22.187  1.00 67.43           O  
+ANISOU 5642  O   PHE B 318     7349  10675   7596   -462   2487   -924       O  
+ATOM   5643  CB  PHE B 318     -35.358  25.440  25.240  1.00 63.34           C  
+ANISOU 5643  CB  PHE B 318     6387  10609   7069   -548   2294  -1243       C  
+ATOM   5644  CG  PHE B 318     -34.269  25.776  26.220  1.00 65.39           C  
+ANISOU 5644  CG  PHE B 318     6388  11134   7323   -613   2214  -1343       C  
+ATOM   5645  CD1 PHE B 318     -33.558  24.768  26.851  1.00 71.41           C  
+ANISOU 5645  CD1 PHE B 318     7061  12168   7904   -448   2186  -1288       C  
+ATOM   5646  CD2 PHE B 318     -33.972  27.093  26.528  1.00 75.63           C  
+ANISOU 5646  CD2 PHE B 318     7536  12399   8801   -839   2148  -1495       C  
+ATOM   5647  CE1 PHE B 318     -32.558  25.066  27.758  1.00 82.83           C  
+ANISOU 5647  CE1 PHE B 318     8249  13894   9329   -506   2083  -1375       C  
+ATOM   5648  CE2 PHE B 318     -32.971  27.398  27.437  1.00 78.84           C  
+ANISOU 5648  CE2 PHE B 318     7696  13067   9194   -925   2052  -1607       C  
+ATOM   5649  CZ  PHE B 318     -32.264  26.382  28.052  1.00 82.79           C  
+ANISOU 5649  CZ  PHE B 318     8084  13881   9491   -757   2013  -1545       C  
+ATOM   5650  N   ASN B 319     -36.014  23.090  23.386  1.00 67.19           N  
+ANISOU 5650  N   ASN B 319     7294  10931   7305   -197   2479   -924       N  
+ATOM   5651  CA  ASN B 319     -37.021  22.228  22.794  1.00 61.15           C  
+ANISOU 5651  CA  ASN B 319     6793   9991   6450   -108   2509   -863       C  
+ATOM   5652  C   ASN B 319     -38.031  21.795  23.849  1.00 62.93           C  
+ANISOU 5652  C   ASN B 319     7105  10195   6610   -103   2432   -938       C  
+ATOM   5653  O   ASN B 319     -37.667  21.548  24.998  1.00 62.79           O  
+ANISOU 5653  O   ASN B 319     6987  10353   6517    -67   2381   -982       O  
+ATOM   5654  CB  ASN B 319     -36.358  21.014  22.148  1.00 73.02           C  
+ANISOU 5654  CB  ASN B 319     8385  11544   7817     94   2603   -747       C  
+ATOM   5655  CG  ASN B 319     -35.319  21.403  21.112  1.00 77.88           C  
+ANISOU 5655  CG  ASN B 319     8888  12236   8465     94   2715   -676       C  
+ATOM   5656  OD1 ASN B 319     -35.529  22.325  20.322  1.00 86.03           O  
+ANISOU 5656  OD1 ASN B 319     9927  13172   9587    -59   2741   -652       O  
+ATOM   5657  ND2 ASN B 319     -34.206  20.679  21.086  1.00 73.99           N  
+ANISOU 5657  ND2 ASN B 319     8291  11924   7897    274   2787   -627       N  
+ATOM   5658  N   ILE B 320     -39.296  21.697  23.456  1.00 54.92           N  
+ANISOU 5658  N   ILE B 320     6263   8995   5610   -147   2421   -944       N  
+ATOM   5659  CA  ILE B 320     -40.358  21.377  24.403  1.00 62.19           C  
+ANISOU 5659  CA  ILE B 320     7238   9913   6480   -177   2371  -1015       C  
+ATOM   5660  C   ILE B 320     -41.057  20.056  24.092  1.00 60.63           C  
+ANISOU 5660  C   ILE B 320     7268   9611   6159   -107   2392   -920       C  
+ATOM   5661  O   ILE B 320     -41.462  19.802  22.958  1.00 57.01           O  
+ANISOU 5661  O   ILE B 320     6956   8994   5712   -104   2414   -864       O  
+ATOM   5662  CB  ILE B 320     -41.417  22.502  24.449  1.00 65.27           C  
+ANISOU 5662  CB  ILE B 320     7581  10193   7027   -314   2326  -1140       C  
+ATOM   5663  CG1 ILE B 320     -40.801  23.793  24.992  1.00 64.00           C  
+ANISOU 5663  CG1 ILE B 320     7217  10100   7000   -400   2290  -1272       C  
+ATOM   5664  CG2 ILE B 320     -42.602  22.093  25.309  1.00 51.20           C  
+ANISOU 5664  CG2 ILE B 320     5839   8436   5180   -342   2307  -1211       C  
+ATOM   5665  CD1 ILE B 320     -41.753  24.972  24.985  1.00 55.47           C  
+ANISOU 5665  CD1 ILE B 320     6098   8865   6113   -498   2245  -1407       C  
+ATOM   5666  N   VAL B 321     -41.193  19.220  25.117  1.00 51.83           N  
+ANISOU 5666  N   VAL B 321     6191   8586   4915    -66   2378   -898       N  
+ATOM   5667  CA  VAL B 321     -42.013  18.019  25.039  1.00 59.32           C  
+ANISOU 5667  CA  VAL B 321     7358   9414   5768    -53   2387   -814       C  
+ATOM   5668  C   VAL B 321     -43.179  18.167  26.011  1.00 66.06           C  
+ANISOU 5668  C   VAL B 321     8174  10324   6600   -188   2366   -883       C  
+ATOM   5669  O   VAL B 321     -42.974  18.421  27.197  1.00 76.52           O  
+ANISOU 5669  O   VAL B 321     9375  11842   7855   -204   2352   -934       O  
+ATOM   5670  CB  VAL B 321     -41.206  16.753  25.373  1.00 59.07           C  
+ANISOU 5670  CB  VAL B 321     7437   9408   5598    113   2400   -683       C  
+ATOM   5671  CG1 VAL B 321     -42.125  15.543  25.464  1.00 57.88           C  
+ANISOU 5671  CG1 VAL B 321     7526   9099   5365     83   2400   -595       C  
+ATOM   5672  CG2 VAL B 321     -40.119  16.531  24.335  1.00 53.33           C  
+ANISOU 5672  CG2 VAL B 321     6735   8636   4891    273   2450   -636       C  
+ATOM   5673  N   SER B 322     -44.401  18.011  25.510  1.00 62.89           N  
+ANISOU 5673  N   SER B 322     7865   9784   6246   -288   2363   -893       N  
+ATOM   5674  CA  SER B 322     -45.585  18.263  26.325  1.00 60.48           C  
+ANISOU 5674  CA  SER B 322     7477   9559   5944   -421   2365   -975       C  
+ATOM   5675  C   SER B 322     -46.595  17.121  26.289  1.00 56.35           C  
+ANISOU 5675  C   SER B 322     7117   8945   5348   -511   2378   -881       C  
+ATOM   5676  O   SER B 322     -46.832  16.518  25.242  1.00 62.85           O  
+ANISOU 5676  O   SER B 322     8107   9577   6196   -516   2357   -816       O  
+ATOM   5677  CB  SER B 322     -46.263  19.558  25.871  1.00 57.48           C  
+ANISOU 5677  CB  SER B 322     6950   9137   5752   -484   2337  -1118       C  
+ATOM   5678  OG  SER B 322     -47.484  19.765  26.560  1.00 54.08           O  
+ANISOU 5678  OG  SER B 322     6418   8790   5340   -586   2353  -1214       O  
+ATOM   5679  N   GLY B 323     -47.184  16.828  27.445  1.00 60.97           N  
+ANISOU 5679  N   GLY B 323     7655   9680   5831   -602   2414   -878       N  
+ATOM   5680  CA  GLY B 323     -48.219  15.816  27.541  1.00 59.17           C  
+ANISOU 5680  CA  GLY B 323     7550   9386   5545   -741   2436   -782       C  
+ATOM   5681  C   GLY B 323     -49.600  16.406  27.325  1.00 60.46           C  
+ANISOU 5681  C   GLY B 323     7565   9577   5832   -885   2440   -900       C  
+ATOM   5682  O   GLY B 323     -50.608  15.706  27.435  1.00 58.69           O  
+ANISOU 5682  O   GLY B 323     7380   9339   5581  -1043   2462   -842       O  
+ATOM   5683  N   PHE B 324     -49.633  17.701  27.017  1.00 57.01           N  
+ANISOU 5683  N   PHE B 324     6947   9171   5544   -831   2413  -1058       N  
+ATOM   5684  CA  PHE B 324     -50.866  18.420  26.704  1.00 53.38           C  
+ANISOU 5684  CA  PHE B 324     6318   8722   5243   -908   2393  -1178       C  
+ATOM   5685  C   PHE B 324     -51.898  18.281  27.823  1.00 55.35           C  
+ANISOU 5685  C   PHE B 324     6415   9188   5426  -1036   2483  -1234       C  
+ATOM   5686  O   PHE B 324     -53.038  17.880  27.587  1.00 64.59           O  
+ANISOU 5686  O   PHE B 324     7543  10359   6640  -1170   2485  -1212       O  
+ATOM   5687  CB  PHE B 324     -51.446  17.924  25.374  1.00 55.39           C  
+ANISOU 5687  CB  PHE B 324     6699   8775   5573   -965   2310  -1099       C  
+ATOM   5688  CG  PHE B 324     -52.526  18.806  24.810  1.00 61.66           C  
+ANISOU 5688  CG  PHE B 324     7308   9565   6556   -993   2243  -1203       C  
+ATOM   5689  CD1 PHE B 324     -52.254  20.116  24.451  1.00 65.83           C  
+ANISOU 5689  CD1 PHE B 324     7716  10054   7240   -872   2194  -1301       C  
+ATOM   5690  CD2 PHE B 324     -53.811  18.320  24.624  1.00 57.35           C  
+ANISOU 5690  CD2 PHE B 324     6703   9045   6043  -1144   2216  -1191       C  
+ATOM   5691  CE1 PHE B 324     -53.244  20.927  23.929  1.00 58.86           C  
+ANISOU 5691  CE1 PHE B 324     6670   9146   6546   -865   2113  -1375       C  
+ATOM   5692  CE2 PHE B 324     -54.804  19.126  24.102  1.00 60.28           C  
+ANISOU 5692  CE2 PHE B 324     6874   9432   6597  -1142   2135  -1278       C  
+ATOM   5693  CZ  PHE B 324     -54.521  20.431  23.753  1.00 61.06           C  
+ANISOU 5693  CZ  PHE B 324     6868   9478   6852   -984   2079  -1365       C  
+ATOM   5694  N   GLY B 325     -51.487  18.603  29.046  1.00 55.62           N  
+ANISOU 5694  N   GLY B 325     6358   9436   5340  -1007   2559  -1309       N  
+ATOM   5695  CA  GLY B 325     -52.394  18.571  30.179  1.00 60.55           C  
+ANISOU 5695  CA  GLY B 325     6825  10319   5863  -1120   2673  -1381       C  
+ATOM   5696  C   GLY B 325     -53.443  19.663  30.103  1.00 63.93           C  
+ANISOU 5696  C   GLY B 325     6986  10820   6486  -1110   2693  -1603       C  
+ATOM   5697  O   GLY B 325     -53.155  20.780  29.668  1.00 74.02           O  
+ANISOU 5697  O   GLY B 325     8181  11999   7945   -978   2627  -1749       O  
+ATOM   5698  N   LEU B 326     -54.663  19.338  30.519  1.00 59.90           N  
+ANISOU 5698  N   LEU B 326     6333  10476   5951  -1248   2783  -1618       N  
+ATOM   5699  CA  LEU B 326     -55.772  20.285  30.474  1.00 61.09           C  
+ANISOU 5699  CA  LEU B 326     6192  10721   6297  -1217   2810  -1828       C  
+ATOM   5700  C   LEU B 326     -55.480  21.516  31.327  1.00 61.82           C  
+ANISOU 5700  C   LEU B 326     6122  10958   6409  -1071   2873  -2100       C  
+ATOM   5701  O   LEU B 326     -55.222  21.403  32.525  1.00 63.40           O  
+ANISOU 5701  O   LEU B 326     6304  11406   6379  -1106   2993  -2161       O  
+ATOM   5702  CB  LEU B 326     -57.070  19.618  30.935  1.00 67.58           C  
+ANISOU 5702  CB  LEU B 326     6857  11765   7056  -1411   2928  -1791       C  
+ATOM   5703  CG  LEU B 326     -58.331  20.484  30.869  1.00 65.14           C  
+ANISOU 5703  CG  LEU B 326     6198  11588   6963  -1366   2962  -2000       C  
+ATOM   5704  CD1 LEU B 326     -58.584  20.962  29.447  1.00 63.98           C  
+ANISOU 5704  CD1 LEU B 326     6036  11170   7102  -1268   2767  -1992       C  
+ATOM   5705  CD2 LEU B 326     -59.534  19.722  31.395  1.00 67.76           C  
+ANISOU 5705  CD2 LEU B 326     6352  12189   7205  -1592   3103  -1944       C  
+ATOM   5706  N   GLY B 327     -55.518  22.688  30.703  1.00 61.40           N  
+ANISOU 5706  N   GLY B 327     5967  10739   6623   -914   2782  -2261       N  
+ATOM   5707  CA  GLY B 327     -55.280  23.933  31.409  1.00 62.46           C  
+ANISOU 5707  CA  GLY B 327     5963  10941   6827   -775   2823  -2551       C  
+ATOM   5708  C   GLY B 327     -53.881  24.474  31.196  1.00 66.96           C  
+ANISOU 5708  C   GLY B 327     6696  11324   7424   -690   2723  -2560       C  
+ATOM   5709  O   GLY B 327     -53.566  25.585  31.620  1.00 66.36           O  
+ANISOU 5709  O   GLY B 327     6537  11229   7448   -589   2721  -2804       O  
+ATOM   5710  N   VAL B 328     -53.029  23.674  30.561  1.00 73.22           N  
+ANISOU 5710  N   VAL B 328     7712  11979   8128   -737   2645  -2307       N  
+ATOM   5711  CA  VAL B 328     -51.647  24.070  30.309  1.00 60.68           C  
+ANISOU 5711  CA  VAL B 328     6252  10250   6555   -673   2561  -2285       C  
+ATOM   5712  C   VAL B 328     -51.258  23.908  28.840  1.00 65.77           C  
+ANISOU 5712  C   VAL B 328     7044  10607   7337   -648   2442  -2083       C  
+ATOM   5713  O   VAL B 328     -50.677  24.814  28.241  1.00 64.23           O  
+ANISOU 5713  O   VAL B 328     6859  10228   7318   -578   2363  -2122       O  
+ATOM   5714  CB  VAL B 328     -50.665  23.264  31.182  1.00 58.69           C  
+ANISOU 5714  CB  VAL B 328     6116  10183   6001   -723   2603  -2191       C  
+ATOM   5715  CG1 VAL B 328     -49.226  23.604  30.824  1.00 56.45           C  
+ANISOU 5715  CG1 VAL B 328     5924   9776   5748   -662   2510  -2151       C  
+ATOM   5716  CG2 VAL B 328     -50.931  23.525  32.657  1.00 59.71           C  
+ANISOU 5716  CG2 VAL B 328     6114  10629   5946   -752   2713  -2399       C  
+ATOM   5717  N   GLY B 329     -51.582  22.749  28.272  1.00 75.00           N  
+ANISOU 5717  N   GLY B 329     8339  11743   8414   -721   2434  -1872       N  
+ATOM   5718  CA  GLY B 329     -51.153  22.382  26.932  1.00 65.88           C  
+ANISOU 5718  CA  GLY B 329     7359  10359   7312   -705   2338  -1686       C  
+ATOM   5719  C   GLY B 329     -51.424  23.381  25.822  1.00 60.51           C  
+ANISOU 5719  C   GLY B 329     6637   9475   6880   -638   2232  -1710       C  
+ATOM   5720  O   GLY B 329     -50.527  23.704  25.040  1.00 59.03           O  
+ANISOU 5720  O   GLY B 329     6555   9134   6738   -591   2175  -1629       O  
+ATOM   5721  N   SER B 330     -52.658  23.874  25.753  1.00 57.89           N  
+ANISOU 5721  N   SER B 330     6138   9152   6704   -629   2206  -1807       N  
+ATOM   5722  CA  SER B 330     -53.076  24.763  24.672  1.00 68.41           C  
+ANISOU 5722  CA  SER B 330     7432  10287   8274   -552   2078  -1793       C  
+ATOM   5723  C   SER B 330     -52.276  26.061  24.673  1.00 72.82           C  
+ANISOU 5723  C   SER B 330     7971  10698   8997   -455   2047  -1885       C  
+ATOM   5724  O   SER B 330     -52.018  26.648  23.622  1.00 76.05           O  
+ANISOU 5724  O   SER B 330     8455  10899   9540   -413   1942  -1779       O  
+ATOM   5725  CB  SER B 330     -54.571  25.072  24.782  1.00 68.29           C  
+ANISOU 5725  CB  SER B 330     7190  10346   8411   -531   2057  -1899       C  
+ATOM   5726  OG  SER B 330     -55.300  23.934  25.208  1.00 78.69           O  
+ANISOU 5726  OG  SER B 330     8471  11859   9570   -664   2129  -1862       O  
+ATOM   5727  N   PHE B 331     -51.879  26.498  25.863  1.00 72.13           N  
+ANISOU 5727  N   PHE B 331     7794  10725   8886   -440   2137  -2078       N  
+ATOM   5728  CA  PHE B 331     -51.188  27.769  26.023  1.00 73.60           C  
+ANISOU 5728  CA  PHE B 331     7949  10767   9248   -379   2106  -2212       C  
+ATOM   5729  C   PHE B 331     -49.691  27.600  25.794  1.00 74.28           C  
+ANISOU 5729  C   PHE B 331     8182  10814   9226   -433   2103  -2091       C  
+ATOM   5730  O   PHE B 331     -49.014  28.524  25.337  1.00 71.50           O  
+ANISOU 5730  O   PHE B 331     7857  10273   9037   -425   2045  -2084       O  
+ATOM   5731  CB  PHE B 331     -51.470  28.340  27.410  1.00 67.58           C  
+ANISOU 5731  CB  PHE B 331     7020  10159   8498   -345   2195  -2518       C  
+ATOM   5732  CG  PHE B 331     -52.903  28.196  27.831  1.00 67.11           C  
+ANISOU 5732  CG  PHE B 331     6784  10248   8467   -304   2253  -2637       C  
+ATOM   5733  CD1 PHE B 331     -53.902  28.889  27.168  1.00 65.57           C  
+ANISOU 5733  CD1 PHE B 331     6475   9894   8544   -192   2171  -2666       C  
+ATOM   5734  CD2 PHE B 331     -53.256  27.356  28.873  1.00 68.03           C  
+ANISOU 5734  CD2 PHE B 331     6834  10679   8334   -378   2389  -2698       C  
+ATOM   5735  CE1 PHE B 331     -55.224  28.753  27.541  1.00 65.92           C  
+ANISOU 5735  CE1 PHE B 331     6309  10110   8628   -148   2229  -2778       C  
+ATOM   5736  CE2 PHE B 331     -54.578  27.219  29.253  1.00 61.59           C  
+ANISOU 5736  CE2 PHE B 331     5825  10035   7542   -362   2466  -2800       C  
+ATOM   5737  CZ  PHE B 331     -55.562  27.917  28.585  1.00 62.92           C  
+ANISOU 5737  CZ  PHE B 331     5847  10063   7999   -244   2389  -2851       C  
+ATOM   5738  N   VAL B 332     -49.182  26.414  26.114  1.00 75.27           N  
+ANISOU 5738  N   VAL B 332     8393  11117   9090   -489   2167  -1986       N  
+ATOM   5739  CA  VAL B 332     -47.829  26.043  25.725  1.00 69.82           C  
+ANISOU 5739  CA  VAL B 332     7826  10411   8291   -512   2165  -1837       C  
+ATOM   5740  C   VAL B 332     -47.739  26.076  24.206  1.00 65.54           C  
+ANISOU 5740  C   VAL B 332     7407   9664   7832   -502   2099  -1637       C  
+ATOM   5741  O   VAL B 332     -46.826  26.678  23.635  1.00 61.40           O  
+ANISOU 5741  O   VAL B 332     6914   9029   7386   -511   2076  -1572       O  
+ATOM   5742  CB  VAL B 332     -47.439  24.642  26.240  1.00 59.59           C  
+ANISOU 5742  CB  VAL B 332     6616   9310   6715   -533   2232  -1734       C  
+ATOM   5743  CG1 VAL B 332     -46.096  24.218  25.664  1.00 52.94           C  
+ANISOU 5743  CG1 VAL B 332     5883   8443   5789   -512   2230  -1574       C  
+ATOM   5744  CG2 VAL B 332     -47.400  24.623  27.759  1.00 63.65           C  
+ANISOU 5744  CG2 VAL B 332     7024  10063   7097   -552   2291  -1901       C  
+ATOM   5745  N   ILE B 333     -48.713  25.438  23.564  1.00 60.21           N  
+ANISOU 5745  N   ILE B 333     6792   8958   7127   -502   2067  -1542       N  
+ATOM   5746  CA  ILE B 333     -48.801  25.412  22.110  1.00 63.18           C  
+ANISOU 5746  CA  ILE B 333     7296   9173   7537   -498   1989  -1364       C  
+ATOM   5747  C   ILE B 333     -48.888  26.820  21.527  1.00 68.07           C  
+ANISOU 5747  C   ILE B 333     7863   9597   8405   -466   1901  -1366       C  
+ATOM   5748  O   ILE B 333     -48.160  27.147  20.596  1.00 71.01           O  
+ANISOU 5748  O   ILE B 333     8336   9856   8788   -480   1876  -1218       O  
+ATOM   5749  CB  ILE B 333     -50.010  24.583  21.633  1.00 63.51           C  
+ANISOU 5749  CB  ILE B 333     7380   9231   7520   -524   1940  -1305       C  
+ATOM   5750  CG1 ILE B 333     -49.804  23.106  21.971  1.00 59.35           C  
+ANISOU 5750  CG1 ILE B 333     6973   8823   6755   -575   2017  -1252       C  
+ATOM   5751  CG2 ILE B 333     -50.218  24.749  20.137  1.00 67.75           C  
+ANISOU 5751  CG2 ILE B 333     8034   9620   8089   -519   1827  -1147       C  
+ATOM   5752  CD1 ILE B 333     -50.885  22.197  21.430  1.00 67.76           C  
+ANISOU 5752  CD1 ILE B 333     8107   9880   7758   -646   1962  -1190       C  
+ATOM   5753  N   ASN B 334     -49.778  27.645  22.072  1.00 70.01           N  
+ANISOU 5753  N   ASN B 334     7953   9800   8848   -418   1862  -1527       N  
+ATOM   5754  CA  ASN B 334     -49.924  29.026  21.613  1.00 75.72           C  
+ANISOU 5754  CA  ASN B 334     8636  10288   9846   -364   1766  -1535       C  
+ATOM   5755  C   ASN B 334     -48.618  29.808  21.720  1.00 76.90           C  
+ANISOU 5755  C   ASN B 334     8819  10332  10068   -415   1795  -1540       C  
+ATOM   5756  O   ASN B 334     -48.195  30.474  20.767  1.00 81.70           O  
+ANISOU 5756  O   ASN B 334     9514  10746  10783   -438   1732  -1376       O  
+ATOM   5757  CB  ASN B 334     -51.017  29.744  22.407  1.00 82.00           C  
+ANISOU 5757  CB  ASN B 334     9239  11066  10849   -270   1745  -1765       C  
+ATOM   5758  CG  ASN B 334     -52.410  29.264  22.052  1.00 78.19           C  
+ANISOU 5758  CG  ASN B 334     8679  10655  10377   -220   1682  -1732       C  
+ATOM   5759  OD1 ASN B 334     -52.665  28.842  20.925  1.00 80.63           O  
+ANISOU 5759  OD1 ASN B 334     9091  10919  10627   -241   1587  -1522       O  
+ATOM   5760  ND2 ASN B 334     -53.321  29.327  23.017  1.00 83.19           N  
+ANISOU 5760  ND2 ASN B 334     9113  11424  11071   -165   1737  -1949       N  
+ATOM   5761  N   GLY B 335     -47.982  29.713  22.885  1.00 73.11           N  
+ANISOU 5761  N   GLY B 335     8265  10000   9514   -451   1885  -1717       N  
+ATOM   5762  CA  GLY B 335     -46.719  30.384  23.128  1.00 74.49           C  
+ANISOU 5762  CA  GLY B 335     8434  10123   9748   -529   1905  -1751       C  
+ATOM   5763  C   GLY B 335     -45.639  29.944  22.162  1.00 77.99           C  
+ANISOU 5763  C   GLY B 335     8993  10577  10062   -598   1933  -1501       C  
+ATOM   5764  O   GLY B 335     -44.832  30.755  21.706  1.00 85.60           O  
+ANISOU 5764  O   GLY B 335     9971  11401  11151   -676   1917  -1424       O  
+ATOM   5765  N   VAL B 336     -45.626  28.654  21.845  1.00 79.43           N  
+ANISOU 5765  N   VAL B 336     9258  10923   9999   -573   1982  -1378       N  
+ATOM   5766  CA  VAL B 336     -44.671  28.118  20.883  1.00 73.17           C  
+ANISOU 5766  CA  VAL B 336     8576  10165   9060   -603   2030  -1165       C  
+ATOM   5767  C   VAL B 336     -44.953  28.644  19.478  1.00 80.08           C  
+ANISOU 5767  C   VAL B 336     9564  10847  10016   -618   1964   -968       C  
+ATOM   5768  O   VAL B 336     -44.040  29.086  18.781  1.00 79.32           O  
+ANISOU 5768  O   VAL B 336     9504  10701   9933   -687   1995   -825       O  
+ATOM   5769  CB  VAL B 336     -44.686  26.575  20.868  1.00 66.13           C  
+ANISOU 5769  CB  VAL B 336     7776   9450   7900   -550   2092  -1107       C  
+ATOM   5770  CG1 VAL B 336     -43.921  26.040  19.669  1.00 64.28           C  
+ANISOU 5770  CG1 VAL B 336     7678   9224   7523   -545   2143   -909       C  
+ATOM   5771  CG2 VAL B 336     -44.099  26.030  22.160  1.00 76.00           C  
+ANISOU 5771  CG2 VAL B 336     8937  10903   9038   -536   2155  -1231       C  
+ATOM   5772  N   LEU B 337     -46.218  28.604  19.071  1.00 85.69           N  
+ANISOU 5772  N   LEU B 337    10316  11472  10769   -563   1871   -948       N  
+ATOM   5773  CA  LEU B 337     -46.603  28.990  17.717  1.00 91.82           C  
+ANISOU 5773  CA  LEU B 337    11212  12099  11577   -564   1778   -740       C  
+ATOM   5774  C   LEU B 337     -46.381  30.473  17.456  1.00 96.56           C  
+ANISOU 5774  C   LEU B 337    11787  12459  12441   -603   1712   -680       C  
+ATOM   5775  O   LEU B 337     -46.093  30.868  16.328  1.00 94.80           O  
+ANISOU 5775  O   LEU B 337    11682  12134  12205   -650   1678   -449       O  
+ATOM   5776  CB  LEU B 337     -48.071  28.646  17.450  1.00 83.63           C  
+ANISOU 5776  CB  LEU B 337    10180  11048  10545   -495   1661   -750       C  
+ATOM   5777  CG  LEU B 337     -48.473  27.171  17.422  1.00 79.04           C  
+ANISOU 5777  CG  LEU B 337     9668  10647   9717   -493   1695   -766       C  
+ATOM   5778  CD1 LEU B 337     -49.980  27.035  17.266  1.00 82.16           C  
+ANISOU 5778  CD1 LEU B 337    10009  11034  10176   -458   1564   -796       C  
+ATOM   5779  CD2 LEU B 337     -47.744  26.432  16.317  1.00 77.49           C  
+ANISOU 5779  CD2 LEU B 337     9668  10500   9275   -526   1740   -594       C  
+ATOM   5780  N   GLU B 338     -46.525  31.294  18.493  1.00 97.77           N  
+ANISOU 5780  N   GLU B 338    11806  12516  12827   -589   1694   -886       N  
+ATOM   5781  CA  GLU B 338     -46.251  32.723  18.361  1.00 97.33           C  
+ANISOU 5781  CA  GLU B 338    11743  12180  13058   -637   1630   -857       C  
+ATOM   5782  C   GLU B 338     -44.825  32.988  17.878  1.00 96.89           C  
+ANISOU 5782  C   GLU B 338    11740  12121  12954   -798   1713   -693       C  
+ATOM   5783  O   GLU B 338     -44.598  33.846  17.025  1.00101.26           O  
+ANISOU 5783  O   GLU B 338    12380  12458  13635   -872   1661   -486       O  
+ATOM   5784  CB  GLU B 338     -46.504  33.450  19.683  1.00 96.81           C  
+ANISOU 5784  CB  GLU B 338    11531  12032  13220   -601   1621  -1171       C  
+ATOM   5785  CG  GLU B 338     -46.164  34.934  19.635  1.00103.29           C  
+ANISOU 5785  CG  GLU B 338    12366  12514  14368   -664   1552  -1178       C  
+ATOM   5786  CD  GLU B 338     -46.771  35.718  20.780  1.00104.02           C  
+ANISOU 5786  CD  GLU B 338    12341  12470  14713   -574   1514  -1518       C  
+ATOM   5787  OE1 GLU B 338     -47.910  35.400  21.180  1.00106.64           O  
+ANISOU 5787  OE1 GLU B 338    12591  12885  15043   -412   1494  -1662       O  
+ATOM   5788  OE2 GLU B 338     -46.106  36.647  21.286  1.00104.74           O  
+ANISOU 5788  OE2 GLU B 338    12414  12382  14999   -673   1510  -1656       O  
+ATOM   5789  N   GLU B 339     -43.871  32.245  18.428  1.00 92.45           N  
+ANISOU 5789  N   GLU B 339    11112  11807  12207   -852   1840   -771       N  
+ATOM   5790  CA  GLU B 339     -42.468  32.395  18.055  1.00 92.48           C  
+ANISOU 5790  CA  GLU B 339    11105  11875  12156  -1000   1938   -638       C  
+ATOM   5791  C   GLU B 339     -42.105  31.603  16.800  1.00 93.36           C  
+ANISOU 5791  C   GLU B 339    11343  12124  12005   -999   2015   -378       C  
+ATOM   5792  O   GLU B 339     -41.227  32.006  16.037  1.00101.67           O  
+ANISOU 5792  O   GLU B 339    12422  13167  13043  -1124   2080   -183       O  
+ATOM   5793  CB  GLU B 339     -41.565  31.968  19.215  1.00 87.44           C  
+ANISOU 5793  CB  GLU B 339    10309  11469  11443  -1035   2023   -838       C  
+ATOM   5794  N   LEU B 340     -42.777  30.475  16.591  1.00 90.22           N  
+ANISOU 5794  N   LEU B 340    11026  11861  11394   -872   2014   -386       N  
+ATOM   5795  CA  LEU B 340     -42.441  29.583  15.486  1.00 83.40           C  
+ANISOU 5795  CA  LEU B 340    10297  11142  10249   -853   2094   -205       C  
+ATOM   5796  C   LEU B 340     -43.113  29.980  14.170  1.00 90.81           C  
+ANISOU 5796  C   LEU B 340    11404  11942  11160   -865   1999     21       C  
+ATOM   5797  O   LEU B 340     -42.560  29.745  13.096  1.00 94.08           O  
+ANISOU 5797  O   LEU B 340    11930  12444  11373   -908   2077    213       O  
+ATOM   5798  CB  LEU B 340     -42.808  28.141  15.843  1.00 82.58           C  
+ANISOU 5798  CB  LEU B 340    10230  11217   9928   -730   2129   -324       C  
+ATOM   5799  CG  LEU B 340     -41.748  27.363  16.629  1.00 78.57           C  
+ANISOU 5799  CG  LEU B 340     9623  10924   9308   -700   2261   -427       C  
+ATOM   5800  CD1 LEU B 340     -41.982  25.863  16.524  1.00 72.22           C  
+ANISOU 5800  CD1 LEU B 340     8936  10246   8259   -581   2305   -455       C  
+ATOM   5801  CD2 LEU B 340     -40.343  27.728  16.167  1.00 74.59           C  
+ANISOU 5801  CD2 LEU B 340     9049  10512   8779   -784   2384   -308       C  
+ATOM   5802  N   TYR B 341     -44.300  30.576  14.249  1.00 98.15           N  
+ANISOU 5802  N   TYR B 341    12342  12676  12275   -814   1831     -2       N  
+ATOM   5803  CA  TYR B 341     -45.017  30.985  13.043  1.00100.40           C  
+ANISOU 5803  CA  TYR B 341    12775  12833  12539   -807   1698    226       C  
+ATOM   5804  C   TYR B 341     -44.607  32.388  12.615  1.00102.48           C  
+ANISOU 5804  C   TYR B 341    13062  12858  13018   -914   1656    422       C  
+ATOM   5805  O   TYR B 341     -45.170  32.950  11.676  1.00108.58           O  
+ANISOU 5805  O   TYR B 341    13957  13485  13816   -908   1522    647       O  
+ATOM   5806  CB  TYR B 341     -46.534  30.930  13.248  1.00 99.44           C  
+ANISOU 5806  CB  TYR B 341    12629  12632  12523   -682   1518    132       C  
+ATOM   5807  CG  TYR B 341     -47.133  29.544  13.149  1.00 95.82           C  
+ANISOU 5807  CG  TYR B 341    12218  12378  11812   -621   1518     45       C  
+ATOM   5808  CD1 TYR B 341     -46.390  28.475  12.666  1.00 97.19           C  
+ANISOU 5808  CD1 TYR B 341    12508  12745  11675   -653   1652     81       C  
+ATOM   5809  CD2 TYR B 341     -48.452  29.311  13.519  1.00 97.38           C  
+ANISOU 5809  CD2 TYR B 341    12339  12567  12095   -537   1386    -77       C  
+ATOM   5810  CE1 TYR B 341     -46.939  27.210  12.568  1.00 91.41           C  
+ANISOU 5810  CE1 TYR B 341    11848  12147  10734   -611   1642     -7       C  
+ATOM   5811  CE2 TYR B 341     -49.009  28.051  13.424  1.00 97.03           C  
+ANISOU 5811  CE2 TYR B 341    12341  12688  11836   -524   1380   -148       C  
+ATOM   5812  CZ  TYR B 341     -48.249  27.004  12.947  1.00 94.66           C  
+ANISOU 5812  CZ  TYR B 341    12192  12533  11240   -567   1501   -114       C  
+ATOM   5813  OH  TYR B 341     -48.801  25.746  12.852  1.00 92.11           O  
+ANISOU 5813  OH  TYR B 341    11946  12325  10727   -567   1486   -196       O  
+HETATM 5814  N   MSE B 342     -43.625  32.950  13.312  1.00103.67           N  
+ANISOU 5814  N   MSE B 342    13098  12966  13326  -1023   1757    346       N  
+HETATM 5815  CA  MSE B 342     -43.105  34.267  12.973  1.00111.11           C  
+ANISOU 5815  CA  MSE B 342    14064  13659  14493  -1172   1734    528       C  
+HETATM 5816  C   MSE B 342     -42.349  34.208  11.649  1.00110.48           C  
+ANISOU 5816  C   MSE B 342    14118  13687  14173  -1301   1832    859       C  
+HETATM 5817  O   MSE B 342     -41.589  33.269  11.406  1.00104.16           O  
+ANISOU 5817  O   MSE B 342    13303  13188  13086  -1319   2002    856       O  
+HETATM 5818  CB  MSE B 342     -42.193  34.787  14.087  1.00113.96           C  
+ANISOU 5818  CB  MSE B 342    14255  13982  15063  -1291   1815    331       C  
+HETATM 5819  CG  MSE B 342     -42.041  36.300  14.122  1.00118.81           C  
+ANISOU 5819  CG  MSE B 342    14885  14221  16036  -1427   1729    412       C  
+HETATM 5820 SE   MSE B 342     -43.651  37.202  14.756  1.00187.57          SE  
+ANISOU 5820 SE   MSE B 342    23607  22531  25131  -1220   1487    222      SE  
+HETATM 5821  CE  MSE B 342     -42.912  38.985  15.036  1.00126.06           C  
+ANISOU 5821  CE  MSE B 342    15832  14270  17796  -1446   1440    252       C  
+ATOM   5822  N   ASN B 343     -42.570  35.211  10.802  1.00113.68           N  
+ANISOU 5822  N   ASN B 343    14656  13848  14690  -1378   1728   1146       N  
+ATOM   5823  CA  ASN B 343     -41.943  35.287   9.483  1.00112.57           C  
+ANISOU 5823  CA  ASN B 343    14660  13807  14303  -1517   1817   1499       C  
+ATOM   5824  C   ASN B 343     -42.208  34.044   8.637  1.00110.04           C  
+ANISOU 5824  C   ASN B 343    14457  13805  13549  -1412   1863   1541       C  
+ATOM   5825  O   ASN B 343     -41.361  33.156   8.537  1.00109.04           O  
+ANISOU 5825  O   ASN B 343    14289  13980  13160  -1434   2067   1476       O  
+ATOM   5826  CB  ASN B 343     -40.435  35.513   9.619  1.00106.21           C  
+ANISOU 5826  CB  ASN B 343    13736  13120  13497  -1741   2040   1543       C  
+ATOM   5827  N   THR B 346     -43.822  26.796   9.614  1.00 91.26           N  
+ANISOU 5827  N   THR B 346    12209  12450  10014   -747   2044    454       N  
+ATOM   5828  CA  THR B 346     -44.145  25.410   9.936  1.00 86.15           C  
+ANISOU 5828  CA  THR B 346    11621  11895   9217   -654   2065    254       C  
+ATOM   5829  C   THR B 346     -43.520  24.993  11.263  1.00 85.91           C  
+ANISOU 5829  C   THR B 346    11426  11904   9311   -601   2184     74       C  
+ATOM   5830  O   THR B 346     -42.572  25.619  11.738  1.00 98.47           O  
+ANISOU 5830  O   THR B 346    12867  13518  11028   -637   2287     96       O  
+ATOM   5831  CB  THR B 346     -43.670  24.447   8.832  1.00 80.28           C  
+ANISOU 5831  CB  THR B 346    11084  11314   8104   -625   2178    278       C  
+ATOM   5832  N   ILE B 347     -44.058  23.932  11.856  1.00 79.76           N  
+ANISOU 5832  N   ILE B 347    10676  11138   8489   -532   2158    -93       N  
+ATOM   5833  CA  ILE B 347     -43.534  23.408  13.111  1.00 77.13           C  
+ANISOU 5833  CA  ILE B 347    10216  10858   8232   -471   2252   -240       C  
+ATOM   5834  C   ILE B 347     -42.426  22.388  12.892  1.00 87.51           C  
+ANISOU 5834  C   ILE B 347    11601  12308   9340   -375   2429   -267       C  
+ATOM   5835  O   ILE B 347     -42.670  21.296  12.380  1.00 90.30           O  
+ANISOU 5835  O   ILE B 347    12143  12666   9499   -313   2441   -316       O  
+ATOM   5836  CB  ILE B 347     -44.638  22.738  13.960  1.00 77.72           C  
+ANISOU 5836  CB  ILE B 347    10285  10879   8364   -454   2150   -382       C  
+ATOM   5837  CG1 ILE B 347     -45.690  23.758  14.392  1.00 77.51           C  
+ANISOU 5837  CG1 ILE B 347    10127  10748   8574   -511   1999   -396       C  
+ATOM   5838  CG2 ILE B 347     -44.036  22.061  15.186  1.00 63.33           C  
+ANISOU 5838  CG2 ILE B 347     8374   9133   6556   -387   2249   -496       C  
+ATOM   5839  CD1 ILE B 347     -46.826  23.145  15.184  1.00 67.59           C  
+ANISOU 5839  CD1 ILE B 347     8831   9483   7366   -513   1921   -527       C  
+ATOM   5840  N   ASP B 348     -41.203  22.754  13.255  1.00 88.32           N  
+ANISOU 5840  N   ASP B 348    11545  12517   9495   -359   2562   -244       N  
+ATOM   5841  CA  ASP B 348     -40.121  21.784  13.290  1.00 95.97           C  
+ANISOU 5841  CA  ASP B 348    12517  13631  10318   -224   2727   -290       C  
+ATOM   5842  C   ASP B 348     -40.415  20.859  14.466  1.00 92.38           C  
+ANISOU 5842  C   ASP B 348    12052  13146   9902   -131   2685   -424       C  
+ATOM   5843  O   ASP B 348     -40.748  21.332  15.552  1.00 89.96           O  
+ANISOU 5843  O   ASP B 348    11602  12812   9767   -184   2604   -474       O  
+ATOM   5844  CB  ASP B 348     -38.762  22.477  13.442  1.00 98.34           C  
+ANISOU 5844  CB  ASP B 348    12594  14085  10688   -248   2862   -226       C  
+ATOM   5845  CG  ASP B 348     -37.590  21.551  13.160  1.00 98.71           C  
+ANISOU 5845  CG  ASP B 348    12623  14316  10565    -85   3050   -249       C  
+ATOM   5846  OD1 ASP B 348     -37.726  20.324  13.347  1.00 98.37           O  
+ANISOU 5846  OD1 ASP B 348    12709  14250  10416     78   3061   -350       O  
+ATOM   5847  OD2 ASP B 348     -36.524  22.056  12.750  1.00102.57           O  
+ANISOU 5847  OD2 ASP B 348    12962  14968  11041   -118   3191   -164       O  
+ATOM   5848  N   ASP B 349     -40.287  19.550  14.269  1.00 78.48           N  
+ANISOU 5848  N   ASP B 349    10456  11384   7979      6   2743   -483       N  
+ATOM   5849  CA  ASP B 349     -40.666  18.623  15.330  1.00 71.66           C  
+ANISOU 5849  CA  ASP B 349     9626  10458   7144     74   2692   -569       C  
+ATOM   5850  C   ASP B 349     -39.557  18.434  16.345  1.00 82.05           C  
+ANISOU 5850  C   ASP B 349    10758  11908   8511    193   2767   -581       C  
+ATOM   5851  O   ASP B 349     -39.746  17.753  17.351  1.00 89.04           O  
+ANISOU 5851  O   ASP B 349    11652  12766   9414    250   2724   -618       O  
+ATOM   5852  CB  ASP B 349     -41.078  17.261  14.775  1.00 72.78           C  
+ANISOU 5852  CB  ASP B 349    10050  10483   7122    158   2695   -627       C  
+ATOM   5853  CG  ASP B 349     -42.272  17.342  13.859  1.00 97.20           C  
+ANISOU 5853  CG  ASP B 349    13318  13463  10150     23   2582   -632       C  
+ATOM   5854  OD1 ASP B 349     -42.848  18.442  13.714  1.00112.42           O  
+ANISOU 5854  OD1 ASP B 349    15142  15397  12176   -111   2490   -574       O  
+ATOM   5855  OD2 ASP B 349     -42.654  16.288  13.318  1.00 97.72           O  
+ANISOU 5855  OD2 ASP B 349    13626  13425  10079     55   2567   -700       O  
+ATOM   5856  N   ASP B 350     -38.395  19.023  16.091  1.00 69.05           N  
+ANISOU 5856  N   ASP B 350     8936  10422   6879    222   2875   -534       N  
+ATOM   5857  CA  ASP B 350     -37.344  18.936  17.086  1.00 68.60           C  
+ANISOU 5857  CA  ASP B 350     8658  10527   6881    322   2915   -544       C  
+ATOM   5858  C   ASP B 350     -37.523  20.100  18.048  1.00 74.27           C  
+ANISOU 5858  C   ASP B 350     9164  11282   7775    155   2817   -563       C  
+ATOM   5859  O   ASP B 350     -36.786  20.229  19.015  1.00 82.68           O  
+ANISOU 5859  O   ASP B 350    10025  12495   8896    187   2807   -588       O  
+ATOM   5860  CB  ASP B 350     -35.960  18.970  16.435  1.00 68.42           C  
+ANISOU 5860  CB  ASP B 350     8499  10696   6801    428   3082   -500       C  
+ATOM   5861  N   ARG B 351     -38.531  20.928  17.781  1.00 60.28           N  
+ANISOU 5861  N   ARG B 351     7443   9373   6087    -12   2731   -564       N  
+ATOM   5862  CA  ARG B 351     -38.841  22.086  18.615  1.00 61.75           C  
+ANISOU 5862  CA  ARG B 351     7460   9544   6456   -159   2637   -616       C  
+ATOM   5863  C   ARG B 351     -39.996  21.820  19.576  1.00 59.20           C  
+ANISOU 5863  C   ARG B 351     7186   9145   6164   -178   2530   -711       C  
+ATOM   5864  O   ARG B 351     -39.963  22.232  20.736  1.00 57.63           O  
+ANISOU 5864  O   ARG B 351     6837   9018   6041   -217   2481   -800       O  
+ATOM   5865  CB  ARG B 351     -39.167  23.295  17.736  1.00 68.12           C  
+ANISOU 5865  CB  ARG B 351     8272  10237   7374   -310   2612   -549       C  
+ATOM   5866  CG  ARG B 351     -38.066  23.672  16.760  1.00 77.40           C  
+ANISOU 5866  CG  ARG B 351     9392  11506   8509   -339   2737   -428       C  
+ATOM   5867  CD  ARG B 351     -36.799  24.056  17.504  1.00 68.82           C  
+ANISOU 5867  CD  ARG B 351     8039  10603   7508   -363   2791   -455       C  
+ATOM   5868  NE  ARG B 351     -37.065  25.147  18.439  1.00 62.85           N  
+ANISOU 5868  NE  ARG B 351     7143   9774   6963   -511   2677   -544       N  
+ATOM   5869  CZ  ARG B 351     -36.142  25.741  19.188  1.00 64.74           C  
+ANISOU 5869  CZ  ARG B 351     7145  10141   7312   -594   2674   -601       C  
+ATOM   5870  NH1 ARG B 351     -34.877  25.351  19.121  1.00 89.07           N  
+ANISOU 5870  NH1 ARG B 351    10065  13455  10322   -540   2778   -555       N  
+ATOM   5871  NH2 ARG B 351     -36.487  26.726  20.005  1.00 66.66           N  
+ANISOU 5871  NH2 ARG B 351     7301  10287   7740   -728   2563   -720       N  
+ATOM   5872  N   LEU B 352     -41.016  21.124  19.082  1.00 62.44           N  
+ANISOU 5872  N   LEU B 352     7800   9429   6497   -164   2496   -698       N  
+ATOM   5873  CA  LEU B 352     -42.196  20.815  19.881  1.00 61.72           C  
+ANISOU 5873  CA  LEU B 352     7744   9282   6426   -206   2414   -771       C  
+ATOM   5874  C   LEU B 352     -42.706  19.402  19.617  1.00 71.15           C  
+ANISOU 5874  C   LEU B 352     9160  10401   7474   -147   2418   -745       C  
+ATOM   5875  O   LEU B 352     -43.071  19.065  18.490  1.00 80.86           O  
+ANISOU 5875  O   LEU B 352    10559  11528   8636   -153   2412   -708       O  
+ATOM   5876  CB  LEU B 352     -43.310  21.830  19.608  1.00 59.54           C  
+ANISOU 5876  CB  LEU B 352     7433   8893   6296   -325   2321   -804       C  
+ATOM   5877  CG  LEU B 352     -44.633  21.599  20.343  1.00 56.49           C  
+ANISOU 5877  CG  LEU B 352     7038   8481   5945   -375   2252   -888       C  
+ATOM   5878  CD1 LEU B 352     -44.418  21.553  21.852  1.00 53.39           C  
+ANISOU 5878  CD1 LEU B 352     6509   8228   5547   -369   2276   -984       C  
+ATOM   5879  CD2 LEU B 352     -45.654  22.666  19.976  1.00 58.43           C  
+ANISOU 5879  CD2 LEU B 352     7217   8624   6362   -447   2157   -919       C  
+ATOM   5880  N   ILE B 353     -42.728  18.579  20.658  1.00 62.83           N  
+ANISOU 5880  N   ILE B 353     8119   9393   6361   -104   2422   -760       N  
+ATOM   5881  CA  ILE B 353     -43.282  17.237  20.549  1.00 66.55           C  
+ANISOU 5881  CA  ILE B 353     8814   9749   6723    -80   2417   -730       C  
+ATOM   5882  C   ILE B 353     -44.453  17.090  21.513  1.00 76.25           C  
+ANISOU 5882  C   ILE B 353    10015  10979   7978   -206   2360   -763       C  
+ATOM   5883  O   ILE B 353     -44.289  17.185  22.731  1.00 73.77           O  
+ANISOU 5883  O   ILE B 353     9578  10795   7655   -206   2368   -777       O  
+ATOM   5884  CB  ILE B 353     -42.224  16.153  20.833  1.00 52.00           C  
+ANISOU 5884  CB  ILE B 353     7059   7925   4774    101   2482   -673       C  
+ATOM   5885  CG1 ILE B 353     -41.322  15.965  19.613  1.00 70.52           C  
+ANISOU 5885  CG1 ILE B 353     9485  10244   7063    234   2562   -657       C  
+ATOM   5886  CG2 ILE B 353     -42.887  14.829  21.190  1.00 52.68           C  
+ANISOU 5886  CG2 ILE B 353     7363   7868   4785     95   2457   -636       C  
+ATOM   5887  CD1 ILE B 353     -42.051  15.451  18.391  1.00 71.40           C  
+ANISOU 5887  CD1 ILE B 353     9844  10179   7106    190   2549   -679       C  
+ATOM   5888  N   LEU B 354     -45.639  16.872  20.956  1.00 64.07           N  
+ANISOU 5888  N   LEU B 354     8571   9321   6452   -323   2303   -777       N  
+ATOM   5889  CA  LEU B 354     -46.848  16.739  21.758  1.00 54.42           C  
+ANISOU 5889  CA  LEU B 354     7292   8125   5261   -464   2266   -808       C  
+ATOM   5890  C   LEU B 354     -47.227  15.276  21.938  1.00 51.85           C  
+ANISOU 5890  C   LEU B 354     7180   7690   4830   -509   2273   -740       C  
+ATOM   5891  O   LEU B 354     -47.301  14.519  20.971  1.00 52.69           O  
+ANISOU 5891  O   LEU B 354     7502   7630   4889   -507   2250   -721       O  
+ATOM   5892  CB  LEU B 354     -48.005  17.507  21.115  1.00 54.06           C  
+ANISOU 5892  CB  LEU B 354     7162   8047   5331   -578   2184   -864       C  
+ATOM   5893  CG  LEU B 354     -47.837  19.023  21.001  1.00 53.38           C  
+ANISOU 5893  CG  LEU B 354     6877   8015   5389   -548   2160   -922       C  
+ATOM   5894  CD1 LEU B 354     -48.717  19.577  19.891  1.00 55.91           C  
+ANISOU 5894  CD1 LEU B 354     7199   8246   5798   -603   2055   -918       C  
+ATOM   5895  CD2 LEU B 354     -48.153  19.695  22.329  1.00 52.32           C  
+ANISOU 5895  CD2 LEU B 354     6522   8020   5336   -577   2184  -1024       C  
+ATOM   5896  N   ARG B 355     -47.465  14.885  23.185  1.00 52.37           N  
+ANISOU 5896  N   ARG B 355     7201   7846   4854   -562   2303   -706       N  
+ATOM   5897  CA  ARG B 355     -47.880  13.522  23.491  1.00 58.07           C  
+ANISOU 5897  CA  ARG B 355     8129   8444   5491   -639   2309   -610       C  
+ATOM   5898  C   ARG B 355     -49.132  13.490  24.362  1.00 63.09           C  
+ANISOU 5898  C   ARG B 355     8652   9185   6136   -852   2316   -610       C  
+ATOM   5899  O   ARG B 355     -49.056  13.149  25.543  1.00 58.30           O  
+ANISOU 5899  O   ARG B 355     8020   8692   5438   -877   2368   -535       O  
+ATOM   5900  CB  ARG B 355     -46.747  12.763  24.185  1.00 60.94           C  
+ANISOU 5900  CB  ARG B 355     8601   8803   5749   -476   2352   -498       C  
+ATOM   5901  CG  ARG B 355     -45.516  12.557  23.323  1.00 64.55           C  
+ANISOU 5901  CG  ARG B 355     9169   9162   6194   -251   2367   -495       C  
+ATOM   5902  CD  ARG B 355     -45.782  11.537  22.229  1.00 56.74           C  
+ANISOU 5902  CD  ARG B 355     8472   7896   5190   -257   2349   -495       C  
+ATOM   5903  NE  ARG B 355     -44.605  11.312  21.396  1.00 58.53           N  
+ANISOU 5903  NE  ARG B 355     8798   8053   5386    -21   2392   -516       N  
+ATOM   5904  CZ  ARG B 355     -43.609  10.493  21.718  1.00 75.39           C  
+ANISOU 5904  CZ  ARG B 355    11043  10126   7477    194   2430   -440       C  
+ATOM   5905  NH1 ARG B 355     -43.646   9.815  22.858  1.00 82.55           N  
+ANISOU 5905  NH1 ARG B 355    12000  11013   8353    195   2412   -312       N  
+ATOM   5906  NH2 ARG B 355     -42.576  10.349  20.899  1.00 79.97           N  
+ANISOU 5906  NH2 ARG B 355    11673  10675   8035    419   2489   -482       N  
+ATOM   5907  N   PRO B 356     -50.288  13.860  23.787  1.00 64.06           N  
+ANISOU 5907  N   PRO B 356     8688   9298   6355  -1003   2265   -686       N  
+ATOM   5908  CA  PRO B 356     -51.541  13.798  24.547  1.00 56.10           C  
+ANISOU 5908  CA  PRO B 356     7534   8418   5365  -1211   2288   -693       C  
+ATOM   5909  C   PRO B 356     -51.867  12.370  24.973  1.00 65.87           C  
+ANISOU 5909  C   PRO B 356     8981   9540   6505  -1364   2315   -550       C  
+ATOM   5910  O   PRO B 356     -51.599  11.431  24.224  1.00 75.28           O  
+ANISOU 5910  O   PRO B 356    10447  10480   7677  -1358   2268   -492       O  
+ATOM   5911  CB  PRO B 356     -52.583  14.328  23.556  1.00 57.65           C  
+ANISOU 5911  CB  PRO B 356     7620   8589   5695  -1308   2194   -788       C  
+ATOM   5912  CG  PRO B 356     -51.981  14.106  22.212  1.00 60.21           C  
+ANISOU 5912  CG  PRO B 356     8161   8706   6009  -1211   2115   -781       C  
+ATOM   5913  CD  PRO B 356     -50.507  14.291  22.395  1.00 56.96           C  
+ANISOU 5913  CD  PRO B 356     7815   8291   5535   -990   2178   -754       C  
+ATOM   5914  N   PHE B 357     -52.442  12.215  26.160  1.00 58.60           N  
+ANISOU 5914  N   PHE B 357     7945   8799   5522  -1505   2396   -495       N  
+ATOM   5915  CA  PHE B 357     -52.740  10.892  26.695  1.00 60.81           C  
+ANISOU 5915  CA  PHE B 357     8428   8972   5706  -1677   2431   -317       C  
+ATOM   5916  C   PHE B 357     -54.031  10.330  26.117  1.00 69.55           C  
+ANISOU 5916  C   PHE B 357     9555   9973   6899  -1958   2386   -319       C  
+ATOM   5917  O   PHE B 357     -55.037  11.034  26.027  1.00 66.02           O  
+ANISOU 5917  O   PHE B 357     8833   9708   6544  -2077   2382   -432       O  
+ATOM   5918  CB  PHE B 357     -52.829  10.935  28.223  1.00 71.47           C  
+ANISOU 5918  CB  PHE B 357     9650  10591   6913  -1740   2547   -231       C  
+ATOM   5919  CG  PHE B 357     -51.497  11.048  28.907  1.00 61.98           C  
+ANISOU 5919  CG  PHE B 357     8507   9460   5582  -1503   2564   -170       C  
+ATOM   5920  CD1 PHE B 357     -50.806  12.248  28.922  1.00 59.56           C  
+ANISOU 5920  CD1 PHE B 357     8009   9314   5305  -1305   2554   -330       C  
+ATOM   5921  CD2 PHE B 357     -50.937   9.950  29.538  1.00 63.24           C  
+ANISOU 5921  CD2 PHE B 357     8909   9519   5600  -1486   2574     57       C  
+ATOM   5922  CE1 PHE B 357     -49.579  12.349  29.553  1.00 66.59           C  
+ANISOU 5922  CE1 PHE B 357     8924  10298   6079  -1111   2551   -281       C  
+ATOM   5923  CE2 PHE B 357     -49.712  10.044  30.170  1.00 63.09           C  
+ANISOU 5923  CE2 PHE B 357     8916   9596   5461  -1257   2564    122       C  
+ATOM   5924  CZ  PHE B 357     -49.032  11.246  30.178  1.00 66.45           C  
+ANISOU 5924  CZ  PHE B 357     9123  10216   5910  -1078   2550    -56       C  
+ATOM   5925  N   PRO B 358     -54.003   9.049  25.720  1.00 65.93           N  
+ANISOU 5925  N   PRO B 358     9417   9211   6423  -2063   2342   -202       N  
+ATOM   5926  CA  PRO B 358     -55.213   8.371  25.250  1.00 73.11           C  
+ANISOU 5926  CA  PRO B 358    10365  10004   7407  -2382   2288   -196       C  
+ATOM   5927  C   PRO B 358     -56.168   8.073  26.401  1.00 83.15           C  
+ANISOU 5927  C   PRO B 358    11479  11478   8636  -2670   2397    -75       C  
+ATOM   5928  O   PRO B 358     -55.754   7.512  27.416  1.00 82.64           O  
+ANISOU 5928  O   PRO B 358    11536  11420   8443  -2680   2489    108       O  
+ATOM   5929  CB  PRO B 358     -54.672   7.080  24.630  1.00 71.70           C  
+ANISOU 5929  CB  PRO B 358    10621   9408   7214  -2375   2221   -115       C  
+ATOM   5930  CG  PRO B 358     -53.398   6.823  25.356  1.00 70.42           C  
+ANISOU 5930  CG  PRO B 358    10614   9198   6944  -2115   2289     17       C  
+ATOM   5931  CD  PRO B 358     -52.817   8.176  25.662  1.00 66.49           C  
+ANISOU 5931  CD  PRO B 358     9825   9016   6421  -1876   2332    -85       C  
+ATOM   5932  N   GLN B 359     -57.432   8.448  26.241  1.00 83.04           N  
+ANISOU 5932  N   GLN B 359    11184  11649   8720  -2899   2388   -165       N  
+ATOM   5933  CA  GLN B 359     -58.420   8.255  27.295  1.00 85.05           C  
+ANISOU 5933  CA  GLN B 359    11226  12157   8932  -3185   2520    -69       C  
+ATOM   5934  C   GLN B 359     -59.148   6.924  27.134  1.00 90.48           C  
+ANISOU 5934  C   GLN B 359    12114  12616   9650  -3562   2490     80       C  
+ATOM   5935  O   GLN B 359     -59.362   6.450  26.018  1.00 89.21           O  
+ANISOU 5935  O   GLN B 359    12118  12182   9594  -3652   2338     15       O  
+ATOM   5936  CB  GLN B 359     -59.424   9.411  27.309  1.00 77.10           C  
+ANISOU 5936  CB  GLN B 359     9751  11513   8031  -3216   2546   -254       C  
+ATOM   5937  CG  GLN B 359     -58.792  10.794  27.429  1.00 68.75           C  
+ANISOU 5937  CG  GLN B 359     8500  10639   6982  -2866   2564   -422       C  
+ATOM   5938  CD  GLN B 359     -57.961  10.962  28.691  1.00 68.24           C  
+ANISOU 5938  CD  GLN B 359     8463  10733   6732  -2726   2709   -352       C  
+ATOM   5939  OE1 GLN B 359     -56.939  11.649  28.686  1.00 75.72           O  
+ANISOU 5939  OE1 GLN B 359     9444  11672   7653  -2437   2688   -429       O  
+ATOM   5940  NE2 GLN B 359     -58.405  10.347  29.782  1.00 82.25           N  
+ANISOU 5940  NE2 GLN B 359    10214  12673   8363  -2948   2855   -201       N  
+ATOM   5941  N   GLY B 360     -59.526   6.332  28.261  1.00 88.40           N  
+ANISOU 5941  N   GLY B 360    11841  12467   9279  -3800   2635    282       N  
+ATOM   5942  CA  GLY B 360     -60.186   5.039  28.272  1.00 81.33           C  
+ANISOU 5942  CA  GLY B 360    11150  11340   8413  -4198   2626    465       C  
+ATOM   5943  C   GLY B 360     -59.334   4.018  28.999  1.00 82.86           C  
+ANISOU 5943  C   GLY B 360    11748  11271   8466  -4175   2678    744       C  
+ATOM   5944  O   GLY B 360     -58.182   4.291  29.332  1.00 80.86           O  
+ANISOU 5944  O   GLY B 360    11615  11006   8102  -3824   2691    772       O  
+ATOM   5945  N   LYS B 361     -59.891   2.835  29.232  1.00 86.74           N  
+ANISOU 5945  N   LYS B 361    12446  11540   8971  -4553   2695    961       N  
+ATOM   5946  CA  LYS B 361     -59.186   1.792  29.972  1.00 93.66           C  
+ANISOU 5946  CA  LYS B 361    13721  12137   9727  -4555   2735   1275       C  
+ATOM   5947  C   LYS B 361     -57.918   1.354  29.238  1.00 87.48           C  
+ANISOU 5947  C   LYS B 361    13354  10894   8990  -4191   2590   1242       C  
+ATOM   5948  O   LYS B 361     -56.840   1.247  29.837  1.00 89.59           O  
+ANISOU 5948  O   LYS B 361    13796  11114   9129  -3895   2613   1388       O  
+ATOM   5949  CB  LYS B 361     -60.105   0.591  30.209  1.00107.64           C  
+ANISOU 5949  CB  LYS B 361    15656  13693  11549  -5071   2763   1511       C  
+ATOM   5950  N   LYS B 362     -58.050   1.120  27.937  1.00 88.62           N  
+ANISOU 5950  N   LYS B 362    13635  10732   9304  -4206   2438   1039       N  
+ATOM   5951  CA  LYS B 362     -56.935   0.656  27.117  1.00 98.68           C  
+ANISOU 5951  CA  LYS B 362    15297  11571  10625  -3875   2317    967       C  
+ATOM   5952  C   LYS B 362     -55.754   1.635  27.074  1.00 85.48           C  
+ANISOU 5952  C   LYS B 362    13511  10097   8869  -3372   2328    846       C  
+ATOM   5953  O   LYS B 362     -54.599   1.212  26.988  1.00 86.36           O  
+ANISOU 5953  O   LYS B 362    13909   9949   8955  -3052   2296    902       O  
+ATOM   5954  CB  LYS B 362     -57.422   0.372  25.695  1.00 94.33           C  
+ANISOU 5954  CB  LYS B 362    14863  10746  10231  -4011   2161    722       C  
+ATOM   5955  N   GLY B 363     -56.050   2.933  27.098  1.00 81.92           N  
+ANISOU 5955  N   GLY B 363    12638  10091   8398  -3304   2370    674       N  
+ATOM   5956  CA  GLY B 363     -55.031   3.974  27.144  1.00 88.85           C  
+ANISOU 5956  CA  GLY B 363    13363  11188   9208  -2891   2388    561       C  
+ATOM   5957  C   GLY B 363     -54.327   4.066  28.485  1.00 87.45           C  
+ANISOU 5957  C   GLY B 363    13157  11211   8858  -2740   2492    762       C  
+ATOM   5958  O   GLY B 363     -53.082   4.118  28.585  1.00 86.05           O  
+ANISOU 5958  O   GLY B 363    13101  10973   8620  -2390   2470    792       O  
+ATOM   5959  N   GLU B 364     -55.144   4.088  29.536  1.00 93.28           N  
+ANISOU 5959  N   GLU B 364    13715  12226   9501  -3014   2607    898       N  
+ATOM   5960  CA  GLU B 364     -54.632   4.198  30.894  1.00 90.60           C  
+ANISOU 5960  CA  GLU B 364    13332  12145   8948  -2922   2708   1091       C  
+ATOM   5961  C   GLU B 364     -53.796   2.966  31.210  1.00 93.31           C  
+ANISOU 5961  C   GLU B 364    14105  12119   9230  -2826   2658   1381       C  
+ATOM   5962  O   GLU B 364     -52.944   2.989  32.102  1.00104.18           O  
+ANISOU 5962  O   GLU B 364    15521  13628  10434  -2618   2677   1541       O  
+ATOM   5963  CB  GLU B 364     -55.774   4.358  31.908  1.00 85.28           C  
+ANISOU 5963  CB  GLU B 364    12399  11846   8159  -3271   2863   1182       C  
+ATOM   5964  CG  GLU B 364     -56.621   5.630  31.743  1.00 88.24           C  
+ANISOU 5964  CG  GLU B 364    12309  12618   8599  -3323   2925    892       C  
+ATOM   5965  CD  GLU B 364     -57.651   5.764  32.858  1.00 98.14           C  
+ANISOU 5965  CD  GLU B 364    13292  14286   9712  -3627   3113    978       C  
+ATOM   5966  OE1 GLU B 364     -57.390   5.236  33.964  1.00106.33           O  
+ANISOU 5966  OE1 GLU B 364    14459  15421  10522  -3696   3207   1240       O  
+ATOM   5967  OE2 GLU B 364     -58.700   6.413  32.649  1.00 98.74           O  
+ANISOU 5967  OE2 GLU B 364    13015  14612   9891  -3780   3170    789       O  
+ATOM   5968  N   GLU B 365     -54.024   1.898  30.452  1.00 87.92           N  
+ANISOU 5968  N   GLU B 365    13747  10960   8697  -2964   2577   1438       N  
+ATOM   5969  CA  GLU B 365     -53.233   0.682  30.594  1.00 88.57           C  
+ANISOU 5969  CA  GLU B 365    14275  10601   8778  -2838   2511   1689       C  
+ATOM   5970  C   GLU B 365     -51.751   0.905  30.269  1.00 87.73           C  
+ANISOU 5970  C   GLU B 365    14260  10406   8666  -2322   2435   1612       C  
+ATOM   5971  O   GLU B 365     -50.883   0.210  30.803  1.00 91.09           O  
+ANISOU 5971  O   GLU B 365    14935  10648   9027  -2111   2398   1850       O  
+ATOM   5972  CB  GLU B 365     -53.801  -0.408  29.684  1.00 90.13           C  
+ANISOU 5972  CB  GLU B 365    14800  10274   9170  -3082   2430   1681       C  
+ATOM   5973  N   GLN B 366     -51.463   1.880  29.409  1.00 93.05           N  
+ANISOU 5973  N   GLN B 366    14718  11226   9410  -2122   2410   1297       N  
+ATOM   5974  CA  GLN B 366     -50.085   2.171  29.012  1.00 98.75           C  
+ANISOU 5974  CA  GLN B 366    15476  11909  10137  -1663   2358   1203       C  
+ATOM   5975  C   GLN B 366     -49.707   3.630  29.213  1.00 90.63           C  
+ANISOU 5975  C   GLN B 366    14044  11356   9035  -1494   2397   1023       C  
+ATOM   5976  O   GLN B 366     -48.766   4.139  28.586  1.00 93.03           O  
+ANISOU 5976  O   GLN B 366    14291  11674   9381  -1182   2362    866       O  
+ATOM   5977  CB  GLN B 366     -49.836   1.758  27.556  1.00 97.23           C  
+ANISOU 5977  CB  GLN B 366    15508  11323  10111  -1539   2283   1001       C  
+ATOM   5978  CG  GLN B 366     -49.903   0.257  27.325  1.00105.80           C  
+ANISOU 5978  CG  GLN B 366    17054  11859  11288  -1615   2227   1148       C  
+ATOM   5979  CD  GLN B 366     -49.975  -0.127  25.862  1.00113.72           C  
+ANISOU 5979  CD  GLN B 366    18271  12503  12435  -1590   2160    892       C  
+ATOM   5980  OE1 GLN B 366     -49.002  -0.629  25.293  1.00121.86           O  
+ANISOU 5980  OE1 GLN B 366    19543  13245  13514  -1255   2127    831       O  
+ATOM   5981  NE2 GLN B 366     -51.126   0.101  25.244  1.00119.04           N  
+ANISOU 5981  NE2 GLN B 366    18850  13215  13167  -1938   2138    730       N  
+ATOM   5982  N   TRP B 367     -50.449   4.303  30.084  1.00 83.28           N  
+ANISOU 5982  N   TRP B 367    12834  10811   7998  -1710   2478   1038       N  
+ATOM   5983  CA  TRP B 367     -50.132   5.688  30.417  1.00 79.86           C  
+ANISOU 5983  CA  TRP B 367    12037  10809   7497  -1569   2515    861       C  
+ATOM   5984  C   TRP B 367     -48.737   5.828  31.024  1.00 85.30           C  
+ANISOU 5984  C   TRP B 367    12731  11614   8066  -1229   2478    948       C  
+ATOM   5985  O   TRP B 367     -48.054   6.830  30.800  1.00 78.31           O  
+ANISOU 5985  O   TRP B 367    11632  10924   7199  -1021   2463    762       O  
+ATOM   5986  CB  TRP B 367     -51.162   6.252  31.389  1.00 78.60           C  
+ANISOU 5986  CB  TRP B 367    11606  11035   7222  -1844   2624    864       C  
+ATOM   5987  CG  TRP B 367     -52.336   6.890  30.736  1.00 85.04           C  
+ANISOU 5987  CG  TRP B 367    12194  11937   8180  -2059   2654    645       C  
+ATOM   5988  CD1 TRP B 367     -52.619   6.932  29.401  1.00 88.46           C  
+ANISOU 5988  CD1 TRP B 367    12669  12137   8807  -2068   2575    479       C  
+ATOM   5989  CD2 TRP B 367     -53.394   7.584  31.394  1.00 86.66           C  
+ANISOU 5989  CD2 TRP B 367    12079  12513   8334  -2281   2765    565       C  
+ATOM   5990  NE1 TRP B 367     -53.792   7.617  29.190  1.00 89.92           N  
+ANISOU 5990  NE1 TRP B 367    12571  12520   9075  -2277   2608    321       N  
+ATOM   5991  CE2 TRP B 367     -54.288   8.026  30.400  1.00 89.86           C  
+ANISOU 5991  CE2 TRP B 367    12328  12880   8936  -2401   2733    362       C  
+ATOM   5992  CE3 TRP B 367     -53.673   7.876  32.731  1.00 82.75           C  
+ANISOU 5992  CE3 TRP B 367    11410  12400   7633  -2380   2892    637       C  
+ATOM   5993  CZ2 TRP B 367     -55.441   8.745  30.702  1.00 81.94           C  
+ANISOU 5993  CZ2 TRP B 367    10979  12193   7962  -2591   2821    233       C  
+ATOM   5994  CZ3 TRP B 367     -54.816   8.587  33.029  1.00 80.50           C  
+ANISOU 5994  CZ3 TRP B 367    10793  12433   7360  -2576   3004    487       C  
+ATOM   5995  CH2 TRP B 367     -55.686   9.014  32.021  1.00 75.04           C  
+ANISOU 5995  CH2 TRP B 367     9930  11682   6900  -2669   2968    287       C  
+ATOM   5996  N   ASP B 368     -48.315   4.816  31.778  1.00 92.86           N  
+ANISOU 5996  N   ASP B 368    13930  12445   8909  -1184   2453   1242       N  
+ATOM   5997  CA  ASP B 368     -47.023   4.838  32.458  1.00 84.62           C  
+ANISOU 5997  CA  ASP B 368    12883  11535   7735   -866   2393   1365       C  
+ATOM   5998  C   ASP B 368     -45.852   4.772  31.482  1.00 85.69           C  
+ANISOU 5998  C   ASP B 368    13090  11451   8015   -501   2315   1257       C  
+ATOM   5999  O   ASP B 368     -44.939   5.607  31.531  1.00 91.50           O  
+ANISOU 5999  O   ASP B 368    13600  12439   8726   -270   2290   1135       O  
+ATOM   6000  CB  ASP B 368     -46.936   3.678  33.451  1.00 80.90           C  
+ANISOU 6000  CB  ASP B 368    12682  10945   7112   -906   2365   1749       C  
+ATOM   6001  CG  ASP B 368     -45.680   3.727  34.294  1.00 83.28           C  
+ANISOU 6001  CG  ASP B 368    12945  11452   7244   -592   2278   1901       C  
+ATOM   6002  OD1 ASP B 368     -45.582   4.626  35.157  1.00 84.00           O  
+ANISOU 6002  OD1 ASP B 368    12763  12010   7142   -615   2300   1842       O  
+ATOM   6003  OD2 ASP B 368     -44.788   2.874  34.097  1.00 88.39           O  
+ANISOU 6003  OD2 ASP B 368    13828  11803   7955   -312   2180   2066       O  
+ATOM   6004  N   LYS B 369     -45.889   3.781  30.595  1.00 83.37           N  
+ANISOU 6004  N   LYS B 369    13107  10698   7874   -464   2286   1288       N  
+ATOM   6005  CA  LYS B 369     -44.866   3.626  29.566  1.00 79.99           C  
+ANISOU 6005  CA  LYS B 369    12764  10051   7578   -123   2244   1161       C  
+ATOM   6006  C   LYS B 369     -44.874   4.842  28.654  1.00 75.71           C  
+ANISOU 6006  C   LYS B 369    11949   9704   7113   -112   2282    842       C  
+ATOM   6007  O   LYS B 369     -43.828   5.285  28.179  1.00 75.52           O  
+ANISOU 6007  O   LYS B 369    11811   9757   7126    173   2273    730       O  
+ATOM   6008  CB  LYS B 369     -45.088   2.348  28.755  1.00 85.41           C  
+ANISOU 6008  CB  LYS B 369    13855  10193   8404   -127   2218   1203       C  
+ATOM   6009  N   TYR B 370     -46.071   5.367  28.408  1.00 74.46           N  
+ANISOU 6009  N   TYR B 370    11680   9625   6985   -429   2324    715       N  
+ATOM   6010  CA  TYR B 370     -46.241   6.579  27.617  1.00 74.05           C  
+ANISOU 6010  CA  TYR B 370    11372   9757   7008   -449   2346    447       C  
+ATOM   6011  C   TYR B 370     -45.492   7.757  28.255  1.00 65.89           C  
+ANISOU 6011  C   TYR B 370    10014   9120   5903   -304   2358    383       C  
+ATOM   6012  O   TYR B 370     -44.740   8.480  27.581  1.00 63.82           O  
+ANISOU 6012  O   TYR B 370     9615   8929   5704   -124   2355    233       O  
+ATOM   6013  CB  TYR B 370     -47.736   6.884  27.477  1.00 70.62           C  
+ANISOU 6013  CB  TYR B 370    10851   9369   6614   -809   2372    364       C  
+ATOM   6014  CG  TYR B 370     -48.114   7.832  26.364  1.00 64.45           C  
+ANISOU 6014  CG  TYR B 370     9907   8638   5943   -844   2362    118       C  
+ATOM   6015  CD1 TYR B 370     -47.906   7.493  25.033  1.00 65.41           C  
+ANISOU 6015  CD1 TYR B 370    10212   8496   6147   -759   2322     12       C  
+ATOM   6016  CD2 TYR B 370     -48.742   9.037  26.641  1.00 62.80           C  
+ANISOU 6016  CD2 TYR B 370     9378   8734   5750   -966   2389     -6       C  
+ATOM   6017  CE1 TYR B 370     -48.271   8.352  24.012  1.00 62.77           C  
+ANISOU 6017  CE1 TYR B 370     9744   8224   5883   -799   2299   -178       C  
+ATOM   6018  CE2 TYR B 370     -49.112   9.901  25.630  1.00 64.91           C  
+ANISOU 6018  CE2 TYR B 370     9510   9026   6127   -987   2360   -195       C  
+ATOM   6019  CZ  TYR B 370     -48.875   9.554  24.317  1.00 61.55           C  
+ANISOU 6019  CZ  TYR B 370     9272   8356   5759   -912   2309   -263       C  
+ATOM   6020  OH  TYR B 370     -49.245  10.412  23.308  1.00 62.91           O  
+ANISOU 6020  OH  TYR B 370     9323   8569   6010   -937   2267   -417       O  
+ATOM   6021  N   ARG B 371     -45.672   7.922  29.564  1.00 66.40           N  
+ANISOU 6021  N   ARG B 371     9964   9443   5823   -398   2371    498       N  
+ATOM   6022  CA  ARG B 371     -45.030   9.010  30.295  1.00 74.48           C  
+ANISOU 6022  CA  ARG B 371    10693  10848   6760   -298   2367    417       C  
+ATOM   6023  C   ARG B 371     -43.511   8.865  30.322  1.00 78.47           C  
+ANISOU 6023  C   ARG B 371    11194  11376   7244     33   2303    478       C  
+ATOM   6024  O   ARG B 371     -42.793   9.820  30.012  1.00 70.48           O  
+ANISOU 6024  O   ARG B 371     9959  10533   6286    156   2295    317       O  
+ATOM   6025  CB  ARG B 371     -45.571   9.087  31.725  1.00 68.36           C  
+ANISOU 6025  CB  ARG B 371     9832  10357   5786   -474   2398    525       C  
+ATOM   6026  N   ARG B 372     -43.015   7.677  30.667  1.00 75.03           N  
+ANISOU 6026  N   ARG B 372    10994  10763   6749    180   2255    716       N  
+ATOM   6027  CA  ARG B 372     -41.566   7.455  30.640  1.00 75.25           C  
+ANISOU 6027  CA  ARG B 372    10998  10811   6780    533   2188    778       C  
+ATOM   6028  C   ARG B 372     -40.987   7.681  29.250  1.00 73.25           C  
+ANISOU 6028  C   ARG B 372    10723  10405   6704    708   2221    593       C  
+ATOM   6029  O   ARG B 372     -39.866   8.170  29.105  1.00 71.77           O  
+ANISOU 6029  O   ARG B 372    10337  10391   6539    932   2203    530       O  
+ATOM   6030  CB  ARG B 372     -41.193   6.056  31.140  1.00 77.13           C  
+ANISOU 6030  CB  ARG B 372    11527  10819   6960    694   2120   1078       C  
+ATOM   6031  CG  ARG B 372     -41.474   5.817  32.612  1.00 83.79           C  
+ANISOU 6031  CG  ARG B 372    12385  11873   7577    570   2074   1318       C  
+ATOM   6032  CD  ARG B 372     -40.839   4.511  33.076  1.00 94.95           C  
+ANISOU 6032  CD  ARG B 372    14072  13060   8946    803   1977   1645       C  
+ATOM   6033  NE  ARG B 372     -40.619   4.472  34.521  1.00 95.31           N  
+ANISOU 6033  NE  ARG B 372    14061  13423   8731    792   1895   1885       N  
+ATOM   6034  CZ  ARG B 372     -41.575   4.372  35.439  1.00 99.36           C  
+ANISOU 6034  CZ  ARG B 372    14637  14064   9049    484   1934   2032       C  
+ATOM   6035  NH1 ARG B 372     -42.847   4.306  35.080  1.00103.62           N  
+ANISOU 6035  NH1 ARG B 372    15273  14444   9653    153   2055   1963       N  
+ATOM   6036  NH2 ARG B 372     -41.254   4.346  36.726  1.00 98.48           N  
+ANISOU 6036  NH2 ARG B 372    14478  14277   8663    502   1853   2250       N  
+ATOM   6037  N   ASP B 373     -41.754   7.312  28.232  1.00 74.03           N  
+ANISOU 6037  N   ASP B 373    11017  10200   6910    591   2271    509       N  
+ATOM   6038  CA  ASP B 373     -41.320   7.483  26.855  1.00 77.04           C  
+ANISOU 6038  CA  ASP B 373    11412  10445   7415    730   2314    332       C  
+ATOM   6039  C   ASP B 373     -41.161   8.963  26.522  1.00 72.49           C  
+ANISOU 6039  C   ASP B 373    10508  10162   6872    669   2347    139       C  
+ATOM   6040  O   ASP B 373     -40.139   9.367  25.966  1.00 78.90           O  
+ANISOU 6040  O   ASP B 373    11184  11065   7727    870   2372     62       O  
+ATOM   6041  CB  ASP B 373     -42.312   6.826  25.900  1.00 86.56           C  
+ANISOU 6041  CB  ASP B 373    12900  11297   8693    566   2337    269       C  
+ATOM   6042  CG  ASP B 373     -41.807   6.771  24.474  1.00 93.95           C  
+ANISOU 6042  CG  ASP B 373    13917  12075   9706    737   2383    101       C  
+ATOM   6043  OD1 ASP B 373     -40.724   7.321  24.175  1.00 98.86           O  
+ANISOU 6043  OD1 ASP B 373    14349  12878  10337    964   2419     36       O  
+ATOM   6044  OD2 ASP B 373     -42.502   6.164  23.642  1.00 93.19           O  
+ANISOU 6044  OD2 ASP B 373    14072  11686   9648    627   2385     29       O  
+HETATM 6045  N   MSE B 374     -42.159   9.776  26.857  1.00 69.15           N  
+ANISOU 6045  N   MSE B 374     9951   9883   6439    395   2353     63       N  
+HETATM 6046  CA  MSE B 374     -42.067  11.197  26.522  1.00 66.80           C  
+ANISOU 6046  CA  MSE B 374     9374   9802   6204    336   2373   -116       C  
+HETATM 6047  C   MSE B 374     -41.016  11.920  27.371  1.00 70.85           C  
+ANISOU 6047  C   MSE B 374     9621  10630   6668    453   2344   -119       C  
+HETATM 6048  O   MSE B 374     -40.406  12.886  26.912  1.00 66.98           O  
+ANISOU 6048  O   MSE B 374     8929  10268   6253    494   2359   -240       O  
+HETATM 6049  CB  MSE B 374     -43.426  11.888  26.670  1.00 61.79           C  
+ANISOU 6049  CB  MSE B 374     8656   9223   5597     49   2381   -212       C  
+HETATM 6050  CG  MSE B 374     -43.792  12.289  28.086  1.00 67.28           C  
+ANISOU 6050  CG  MSE B 374     9196  10178   6190    -71   2374   -190       C  
+HETATM 6051 SE   MSE B 374     -45.586  13.029  28.172  1.00 72.88          SE  
+ANISOU 6051 SE   MSE B 374     9787  10947   6958   -392   2411   -329      SE  
+HETATM 6052  CE  MSE B 374     -46.555  11.467  27.551  1.00 61.51           C  
+ANISOU 6052  CE  MSE B 374     8688   9155   5527   -529   2412   -183       C  
+ATOM   6053  N   ILE B 375     -40.796  11.450  28.598  1.00 72.61           N  
+ANISOU 6053  N   ILE B 375     9849  10983   6758    491   2293     22       N  
+ATOM   6054  CA  ILE B 375     -39.824  12.091  29.485  1.00 70.88           C  
+ANISOU 6054  CA  ILE B 375     9376  11093   6464    584   2234     13       C  
+ATOM   6055  C   ILE B 375     -38.390  11.679  29.132  1.00 80.33           C  
+ANISOU 6055  C   ILE B 375    10527  12300   7693    890   2206     82       C  
+ATOM   6056  O   ILE B 375     -37.442  12.427  29.381  1.00 75.85           O  
+ANISOU 6056  O   ILE B 375     9692  11994   7131    964   2168     17       O  
+ATOM   6057  CB  ILE B 375     -40.122  11.769  30.970  1.00 65.38           C  
+ANISOU 6057  CB  ILE B 375     8693  10584   5565    508   2178    146       C  
+ATOM   6058  CG1 ILE B 375     -41.513  12.281  31.347  1.00 65.92           C  
+ANISOU 6058  CG1 ILE B 375     8744  10702   5598    213   2235     47       C  
+ATOM   6059  CG2 ILE B 375     -39.109  12.427  31.894  1.00 64.22           C  
+ANISOU 6059  CG2 ILE B 375     8286  10802   5312    594   2090    117       C  
+ATOM   6060  CD1 ILE B 375     -41.867  12.081  32.804  1.00 70.82           C  
+ANISOU 6060  CD1 ILE B 375     9360  11565   5985    107   2213    155       C  
+ATOM   6061  N   THR B 376     -38.241  10.506  28.521  1.00 82.24           N  
+ANISOU 6061  N   THR B 376    11022  12257   7970   1065   2227    195       N  
+ATOM   6062  CA  THR B 376     -36.927  10.006  28.114  1.00 82.51           C  
+ANISOU 6062  CA  THR B 376    11018  12282   8051   1398   2221    249       C  
+ATOM   6063  C   THR B 376     -36.266  10.966  27.128  1.00 77.80           C  
+ANISOU 6063  C   THR B 376    10188  11806   7566   1430   2297     69       C  
+ATOM   6064  O   THR B 376     -35.042  11.106  27.095  1.00 75.58           O  
+ANISOU 6064  O   THR B 376     9693  11713   7312   1640   2289     75       O  
+ATOM   6065  CB  THR B 376     -37.025   8.601  27.484  1.00 88.23           C  
+ANISOU 6065  CB  THR B 376    12093  12612   8817   1576   2250    350       C  
+ATOM   6066  OG1 THR B 376     -37.704   7.718  28.386  1.00 95.86           O  
+ANISOU 6066  OG1 THR B 376    13298  13435   9691   1500   2182    546       O  
+ATOM   6067  CG2 THR B 376     -35.640   8.041  27.194  1.00 90.59           C  
+ANISOU 6067  CG2 THR B 376    12333  12922   9165   1972   2247    401       C  
+ATOM   6068  N   ARG B 377     -37.096  11.644  26.344  1.00 82.04           N  
+ANISOU 6068  N   ARG B 377    10753  12250   8167   1208   2367    -74       N  
+ATOM   6069  CA  ARG B 377     -36.636  12.605  25.351  1.00 82.62           C  
+ANISOU 6069  CA  ARG B 377    10645  12411   8336   1186   2445   -214       C  
+ATOM   6070  C   ARG B 377     -35.970  13.828  25.968  1.00 83.38           C  
+ANISOU 6070  C   ARG B 377    10387  12840   8456   1108   2403   -279       C  
+ATOM   6071  O   ARG B 377     -35.238  14.553  25.294  1.00 84.01           O  
+ANISOU 6071  O   ARG B 377    10273  13031   8615   1122   2462   -351       O  
+ATOM   6072  CB  ARG B 377     -37.815  13.064  24.501  1.00 65.03           C  
+ANISOU 6072  CB  ARG B 377     8546  10006   6157    952   2492   -319       C  
+ATOM   6073  CG  ARG B 377     -38.643  11.943  23.922  1.00 63.43           C  
+ANISOU 6073  CG  ARG B 377     8690   9479   5931    954   2510   -286       C  
+ATOM   6074  CD  ARG B 377     -39.768  12.524  23.104  1.00 78.23           C  
+ANISOU 6074  CD  ARG B 377    10632  11243   7850    717   2526   -391       C  
+ATOM   6075  NE  ARG B 377     -39.241  13.337  22.017  1.00 81.65           N  
+ANISOU 6075  NE  ARG B 377    10949  11746   8329    739   2594   -477       N  
+ATOM   6076  CZ  ARG B 377     -39.089  12.905  20.774  1.00 76.46           C  
+ANISOU 6076  CZ  ARG B 377    10456  10948   7645    827   2664   -517       C  
+ATOM   6077  NH1 ARG B 377     -39.423  11.661  20.459  1.00 74.15           N  
+ANISOU 6077  NH1 ARG B 377    10461  10410   7304    907   2665   -507       N  
+ATOM   6078  NH2 ARG B 377     -38.602  13.713  19.842  1.00 84.04           N  
+ANISOU 6078  NH2 ARG B 377    11299  12012   8620    824   2737   -568       N  
+ATOM   6079  N   THR B 378     -36.227  14.051  27.251  1.00 75.21           N  
+ANISOU 6079  N   THR B 378     9272  11966   7338   1008   2304   -256       N  
+ATOM   6080  CA  THR B 378     -35.801  15.277  27.912  1.00 66.73           C  
+ANISOU 6080  CA  THR B 378     7893  11181   6278    880   2246   -365       C  
+ATOM   6081  C   THR B 378     -34.760  15.026  28.997  1.00 70.88           C  
+ANISOU 6081  C   THR B 378     8239  11991   6699   1029   2132   -281       C  
+ATOM   6082  O   THR B 378     -34.547  13.890  29.423  1.00 77.73           O  
+ANISOU 6082  O   THR B 378     9243  12824   7468   1225   2084   -111       O  
+ATOM   6083  CB  THR B 378     -37.002  16.009  28.532  1.00 65.85           C  
+ANISOU 6083  CB  THR B 378     7798  11078   6145    613   2223   -475       C  
+ATOM   6084  OG1 THR B 378     -37.496  15.261  29.649  1.00 73.09           O  
+ANISOU 6084  OG1 THR B 378     8837  12044   6890    611   2164   -371       O  
+ATOM   6085  CG2 THR B 378     -38.111  16.165  27.501  1.00 56.69           C  
+ANISOU 6085  CG2 THR B 378     6807   9647   5086    484   2306   -534       C  
+ATOM   6086  N   GLY B 379     -34.110  16.099  29.433  1.00 63.43           N  
+ANISOU 6086  N   GLY B 379     6995  11321   5783    930   2073   -397       N  
+ATOM   6087  CA  GLY B 379     -33.113  16.022  30.484  1.00 67.31           C  
+ANISOU 6087  CA  GLY B 379     7271  12136   6166   1036   1933   -344       C  
+ATOM   6088  C   GLY B 379     -33.434  16.992  31.604  1.00 79.77           C  
+ANISOU 6088  C   GLY B 379     8716  13941   7653    800   1833   -494       C  
+ATOM   6089  O   GLY B 379     -32.798  16.974  32.657  1.00 89.10           O  
+ANISOU 6089  O   GLY B 379     9743  15421   8689    841   1689   -468       O  
+ATOM   6090  N   VAL B 380     -34.424  17.848  31.367  1.00 87.66           N  
+ANISOU 6090  N   VAL B 380     9773  14802   8730    564   1903   -662       N  
+ATOM   6091  CA  VAL B 380     -34.896  18.783  32.381  1.00 86.61           C  
+ANISOU 6091  CA  VAL B 380     9549  14839   8521    348   1835   -850       C  
+ATOM   6092  C   VAL B 380     -36.421  18.887  32.344  1.00 85.42           C  
+ANISOU 6092  C   VAL B 380     9605  14481   8369    204   1925   -920       C  
+ATOM   6093  O   VAL B 380     -37.020  19.044  31.279  1.00 79.07           O  
+ANISOU 6093  O   VAL B 380     8904  13407   7733    163   2027   -939       O  
+ATOM   6094  CB  VAL B 380     -34.261  20.183  32.196  1.00 76.71           C  
+ANISOU 6094  CB  VAL B 380     8026  13685   7435    188   1806  -1064       C  
+ATOM   6095  CG1 VAL B 380     -34.360  20.636  30.746  1.00 84.77           C  
+ANISOU 6095  CG1 VAL B 380     9072  14432   8704    147   1934  -1078       C  
+ATOM   6096  CG2 VAL B 380     -34.899  21.197  33.136  1.00 67.27           C  
+ANISOU 6096  CG2 VAL B 380     6781  12590   6188    -31   1754  -1312       C  
+ATOM   6097  N   SER B 381     -37.045  18.781  33.513  1.00 84.77           N  
+ANISOU 6097  N   SER B 381     9572  14557   8080    127   1887   -952       N  
+ATOM   6098  CA  SER B 381     -38.498  18.842  33.613  1.00 71.10           C  
+ANISOU 6098  CA  SER B 381     7990  12693   6332     -8   1981  -1020       C  
+ATOM   6099  C   SER B 381     -38.959  20.033  34.446  1.00 76.82           C  
+ANISOU 6099  C   SER B 381     8576  13590   7023   -186   1967  -1306       C  
+ATOM   6100  O   SER B 381     -38.609  20.148  35.619  1.00 80.98           O  
+ANISOU 6100  O   SER B 381     9018  14422   7330   -212   1883  -1368       O  
+ATOM   6101  CB  SER B 381     -39.045  17.546  34.214  1.00 62.30           C  
+ANISOU 6101  CB  SER B 381     7087  11592   4992     44   1994   -793       C  
+ATOM   6102  OG  SER B 381     -38.685  16.425  33.426  1.00 82.06           O  
+ANISOU 6102  OG  SER B 381     9752  13877   7550    217   2007   -556       O  
+ATOM   6103  N   ILE B 382     -39.743  20.917  33.838  1.00 78.07           N  
+ANISOU 6103  N   ILE B 382     8719  13552   7393   -295   2043  -1486       N  
+ATOM   6104  CA  ILE B 382     -40.320  22.042  34.565  1.00 75.00           C  
+ANISOU 6104  CA  ILE B 382     8221  13269   7007   -436   2049  -1786       C  
+ATOM   6105  C   ILE B 382     -41.749  21.701  34.975  1.00 77.14           C  
+ANISOU 6105  C   ILE B 382     8599  13540   7172   -493   2157  -1804       C  
+ATOM   6106  O   ILE B 382     -42.532  21.206  34.165  1.00 85.55           O  
+ANISOU 6106  O   ILE B 382     9783  14376   8345   -483   2234  -1679       O  
+ATOM   6107  CB  ILE B 382     -40.308  23.333  33.725  1.00 64.68           C  
+ANISOU 6107  CB  ILE B 382     6816  11738   6022   -508   2055  -1983       C  
+ATOM   6108  CG1 ILE B 382     -38.883  23.659  33.272  1.00 60.70           C  
+ANISOU 6108  CG1 ILE B 382     6184  11250   5627   -488   1969  -1944       C  
+ATOM   6109  CG2 ILE B 382     -40.887  24.496  34.517  1.00 61.63           C  
+ANISOU 6109  CG2 ILE B 382     6332  11424   5660   -624   2056  -2322       C  
+ATOM   6110  CD1 ILE B 382     -38.795  24.853  32.347  1.00 60.09           C  
+ANISOU 6110  CD1 ILE B 382     6037  10925   5870   -580   1980  -2071       C  
+ATOM   6111  N   PHE B 383     -42.088  21.971  36.232  1.00 72.25           N  
+ANISOU 6111  N   PHE B 383     7923  13201   6329   -564   2164  -1967       N  
+ATOM   6112  CA  PHE B 383     -43.389  21.580  36.770  1.00 71.97           C  
+ANISOU 6112  CA  PHE B 383     7955  13245   6145   -630   2288  -1971       C  
+ATOM   6113  C   PHE B 383     -44.265  22.776  37.122  1.00 68.98           C  
+ANISOU 6113  C   PHE B 383     7452  12893   5865   -709   2359  -2328       C  
+ATOM   6114  O   PHE B 383     -43.882  23.632  37.919  1.00 77.01           O  
+ANISOU 6114  O   PHE B 383     8361  14086   6814   -743   2303  -2589       O  
+ATOM   6115  CB  PHE B 383     -43.205  20.687  37.999  1.00 66.01           C  
+ANISOU 6115  CB  PHE B 383     7266  12825   4989   -639   2272  -1815       C  
+ATOM   6116  CG  PHE B 383     -42.456  19.419  37.712  1.00 81.57           C  
+ANISOU 6116  CG  PHE B 383     9382  14731   6879   -527   2198  -1444       C  
+ATOM   6117  CD1 PHE B 383     -41.083  19.354  37.879  1.00 75.90           C  
+ANISOU 6117  CD1 PHE B 383     8604  14132   6103   -421   2046  -1374       C  
+ATOM   6118  CD2 PHE B 383     -43.125  18.294  37.261  1.00 76.30           C  
+ANISOU 6118  CD2 PHE B 383     8902  13875   6214   -524   2275  -1176       C  
+ATOM   6119  CE1 PHE B 383     -40.392  18.189  37.608  1.00 77.89           C  
+ANISOU 6119  CE1 PHE B 383     8977  14312   6304   -273   1980  -1044       C  
+ATOM   6120  CE2 PHE B 383     -42.441  17.127  36.986  1.00 73.10           C  
+ANISOU 6120  CE2 PHE B 383     8653  13361   5759   -397   2207   -856       C  
+ATOM   6121  CZ  PHE B 383     -41.072  17.075  37.160  1.00 66.18           C  
+ANISOU 6121  CZ  PHE B 383     7712  12601   4831   -251   2063   -790       C  
+ATOM   6122  N   LEU B 384     -45.447  22.823  36.517  1.00 65.43           N  
+ANISOU 6122  N   LEU B 384     7025  12220   5614   -724   2444  -2324       N  
+ATOM   6123  CA  LEU B 384     -46.377  23.923  36.729  1.00 70.55           C  
+ANISOU 6123  CA  LEU B 384     7560  12810   6436   -747   2483  -2619       C  
+ATOM   6124  C   LEU B 384     -47.697  23.437  37.313  1.00 74.86           C  
+ANISOU 6124  C   LEU B 384     8120  13437   6888   -788   2571  -2559       C  
+ATOM   6125  O   LEU B 384     -48.316  22.516  36.782  1.00 81.59           O  
+ANISOU 6125  O   LEU B 384     9052  14198   7749   -813   2629  -2323       O  
+ATOM   6126  CB  LEU B 384     -46.642  24.667  35.417  1.00 66.01           C  
+ANISOU 6126  CB  LEU B 384     6936  11925   6219   -713   2506  -2715       C  
+ATOM   6127  CG  LEU B 384     -45.444  25.080  34.562  1.00 67.54           C  
+ANISOU 6127  CG  LEU B 384     7144  11921   6596   -682   2395  -2667       C  
+ATOM   6128  CD1 LEU B 384     -45.921  25.693  33.254  1.00 61.26           C  
+ANISOU 6128  CD1 LEU B 384     6352  10766   6159   -651   2384  -2660       C  
+ATOM   6129  CD2 LEU B 384     -44.553  26.052  35.317  1.00 77.32           C  
+ANISOU 6129  CD2 LEU B 384     8280  13286   7812   -717   2315  -2929       C  
+ATOM   6130  N   TYR B 385     -48.117  24.069  38.407  1.00 68.07           N  
+ANISOU 6130  N   TYR B 385     7171  12761   5933   -809   2591  -2791       N  
+ATOM   6131  CA  TYR B 385     -49.425  23.820  39.015  1.00 78.25           C  
+ANISOU 6131  CA  TYR B 385     8421  14159   7151   -849   2699  -2790       C  
+ATOM   6132  C   TYR B 385     -49.661  22.351  39.352  1.00 78.41           C  
+ANISOU 6132  C   TYR B 385     8571  14307   6915   -928   2750  -2436       C  
+ATOM   6133  O   TYR B 385     -48.910  21.754  40.120  1.00 83.51           O  
+ANISOU 6133  O   TYR B 385     9310  15151   7269   -953   2706  -2298       O  
+ATOM   6134  CB  TYR B 385     -50.528  24.321  38.084  1.00 68.89           C  
+ANISOU 6134  CB  TYR B 385     7133  12749   6293   -811   2763  -2888       C  
+ATOM   6135  CG  TYR B 385     -50.342  25.761  37.682  1.00 74.67           C  
+ANISOU 6135  CG  TYR B 385     7757  13310   7305   -725   2722  -3220       C  
+ATOM   6136  CD1 TYR B 385     -50.724  26.792  38.529  1.00 71.61           C  
+ANISOU 6136  CD1 TYR B 385     7254  13015   6938   -687   2747  -3560       C  
+ATOM   6137  CD2 TYR B 385     -49.762  26.091  36.465  1.00 72.59           C  
+ANISOU 6137  CD2 TYR B 385     7517  12786   7280   -684   2668  -3202       C  
+ATOM   6138  CE1 TYR B 385     -50.548  28.112  38.167  1.00 71.99           C  
+ANISOU 6138  CE1 TYR B 385     7224  12866   7264   -608   2713  -3878       C  
+ATOM   6139  CE2 TYR B 385     -49.580  27.408  36.095  1.00 78.58           C  
+ANISOU 6139  CE2 TYR B 385     8188  13364   8306   -620   2642  -3499       C  
+ATOM   6140  CZ  TYR B 385     -49.975  28.415  36.950  1.00 80.02           C  
+ANISOU 6140  CZ  TYR B 385     8268  13608   8530   -581   2660  -3841       C  
+ATOM   6141  OH  TYR B 385     -49.799  29.730  36.590  1.00 85.30           O  
+ANISOU 6141  OH  TYR B 385     8870  14049   9492   -514   2636  -4156       O  
+ATOM   6142  N   GLY B 386     -50.708  21.776  38.764  1.00 69.55           N  
+ANISOU 6142  N   GLY B 386     7449  13076   5901   -977   2839  -2292       N  
+ATOM   6143  CA  GLY B 386     -51.032  20.376  38.977  1.00 70.15           C  
+ANISOU 6143  CA  GLY B 386     7655  13229   5769  -1084   2904  -1961       C  
+ATOM   6144  C   GLY B 386     -52.348  20.133  39.702  1.00 78.12           C  
+ANISOU 6144  C   GLY B 386     8577  14417   6689  -1191   3039  -1958       C  
+ATOM   6145  O   GLY B 386     -52.384  19.464  40.731  1.00 75.24           O  
+ANISOU 6145  O   GLY B 386     8282  14278   6027  -1276   3089  -1811       O  
+ATOM   6146  N   ASN B 387     -53.432  20.683  39.170  1.00 73.45           N  
+ANISOU 6146  N   ASN B 387     7817  13744   6346  -1187   3103  -2116       N  
+ATOM   6147  CA  ASN B 387     -54.747  20.498  39.759  1.00 78.52           C  
+ANISOU 6147  CA  ASN B 387     8327  14573   6933  -1285   3245  -2130       C  
+ATOM   6148  C   ASN B 387     -55.736  20.008  38.695  1.00 76.88           C  
+ANISOU 6148  C   ASN B 387     8049  14224   6937  -1373   3298  -2017       C  
+ATOM   6149  O   ASN B 387     -55.506  20.185  37.496  1.00 71.63           O  
+ANISOU 6149  O   ASN B 387     7400  13314   6501  -1318   3223  -2025       O  
+ATOM   6150  CB  ASN B 387     -55.190  21.785  40.473  1.00 77.71           C  
+ANISOU 6150  CB  ASN B 387     8030  14612   6883  -1184   3283  -2498       C  
+ATOM   6151  CG  ASN B 387     -55.511  22.906  39.524  1.00 76.27           C  
+ANISOU 6151  CG  ASN B 387     7696  14213   7070  -1047   3243  -2757       C  
+ATOM   6152  OD1 ASN B 387     -56.478  22.829  38.769  1.00 91.53           O  
+ANISOU 6152  OD1 ASN B 387     9503  16067   9206  -1063   3293  -2738       O  
+ATOM   6153  ND2 ASN B 387     -54.689  23.949  39.535  1.00 75.69           N  
+ANISOU 6153  ND2 ASN B 387     7629  14044   7087   -922   3148  -2996       N  
+ATOM   6154  N   LYS B 388     -56.829  19.397  39.141  1.00 77.80           N  
+ANISOU 6154  N   LYS B 388     8079  14517   6966  -1526   3429  -1914       N  
+ATOM   6155  CA  LYS B 388     -57.752  18.713  38.248  1.00 76.47           C  
+ANISOU 6155  CA  LYS B 388     7849  14262   6946  -1673   3479  -1768       C  
+ATOM   6156  C   LYS B 388     -59.185  18.997  38.652  1.00 98.44           C  
+ANISOU 6156  C   LYS B 388    10351  17261   9791  -1735   3613  -1896       C  
+ATOM   6157  O   LYS B 388     -59.513  20.091  39.098  1.00100.67           O  
+ANISOU 6157  O   LYS B 388    10449  17651  10148  -1584   3641  -2185       O  
+ATOM   6158  CB  LYS B 388     -57.505  17.197  38.305  1.00 80.19           C  
+ANISOU 6158  CB  LYS B 388     8555  14705   7207  -1881   3505  -1391       C  
+ATOM   6159  CG  LYS B 388     -57.679  16.452  37.002  1.00 85.04           C  
+ANISOU 6159  CG  LYS B 388     9251  15081   7978  -2007   3473  -1227       C  
+ATOM   6160  CD  LYS B 388     -57.790  14.946  37.247  1.00100.36           C  
+ANISOU 6160  CD  LYS B 388    11399  17015   9717  -2265   3536   -866       C  
+ATOM   6161  CE  LYS B 388     -56.740  14.439  38.225  1.00104.09           C  
+ANISOU 6161  CE  LYS B 388    12115  17550   9884  -2222   3517   -679       C  
+ATOM   6162  NZ  LYS B 388     -56.566  12.953  38.180  1.00104.56           N  
+ANISOU 6162  NZ  LYS B 388    12456  17487   9785  -2434   3541   -295       N  
+ATOM   6163  N   ILE B 389     -60.033  18.001  38.462  1.00 89.45           N  
+ANISOU 6163  N   ILE B 389     9178  16178   8632  -1964   3698  -1682       N  
+ATOM   6164  CA  ILE B 389     -61.436  18.043  38.815  1.00 97.55           C  
+ANISOU 6164  CA  ILE B 389     9923  17437   9705  -2068   3838  -1746       C  
+ATOM   6165  C   ILE B 389     -61.738  16.569  38.988  1.00 98.47           C  
+ANISOU 6165  C   ILE B 389    10172  17596   9646  -2379   3913  -1388       C  
+ATOM   6166  O   ILE B 389     -61.363  15.764  38.133  1.00101.46           O  
+ANISOU 6166  O   ILE B 389    10736  17744  10068  -2502   3838  -1182       O  
+ATOM   6167  CB  ILE B 389     -62.313  18.677  37.737  1.00 87.68           C  
+ANISOU 6167  CB  ILE B 389     8397  16114   8803  -2005   3808  -1927       C  
+ATOM   6168  CG1 ILE B 389     -62.339  20.208  37.866  1.00 85.83           C  
+ANISOU 6168  CG1 ILE B 389     7981  15892   8738  -1704   3781  -2296       C  
+ATOM   6169  CG2 ILE B 389     -63.722  18.144  37.865  1.00 96.26           C  
+ANISOU 6169  CG2 ILE B 389     9235  17418   9921  -2217   3938  -1851       C  
+ATOM   6170  CD1 ILE B 389     -63.195  20.744  39.002  1.00 94.21           C  
+ANISOU 6170  CD1 ILE B 389     8815  17259   9720  -1652   3933  -2484       C  
+ATOM   6171  N   ASP B 390     -62.324  16.207  40.125  1.00 89.79           N  
+ANISOU 6171  N   ASP B 390     9010  16775   8332  -2509   4062  -1309       N  
+ATOM   6172  CA  ASP B 390     -62.616  14.813  40.439  1.00104.89           C  
+ANISOU 6172  CA  ASP B 390    11063  18727  10065  -2822   4145   -946       C  
+ATOM   6173  C   ASP B 390     -64.103  14.560  40.636  1.00106.39           C  
+ANISOU 6173  C   ASP B 390    10961  19148  10316  -3035   4301   -931       C  
+ATOM   6174  O   ASP B 390     -64.625  13.509  40.268  1.00122.76           O  
+ANISOU 6174  O   ASP B 390    13070  21157  12416  -3331   4330   -675       O  
+ATOM   6175  CB  ASP B 390     -61.857  14.402  41.702  1.00116.56           C  
+ANISOU 6175  CB  ASP B 390    12773  20337  11175  -2827   4188   -782       C  
+ATOM   6176  CG  ASP B 390     -61.647  12.902  41.800  1.00128.16           C  
+ANISOU 6176  CG  ASP B 390    14525  21700  12472  -3099   4205   -349       C  
+ATOM   6177  OD1 ASP B 390     -62.422  12.132  41.194  1.00131.75           O  
+ANISOU 6177  OD1 ASP B 390    14942  22061  13057  -3357   4242   -182       O  
+ATOM   6178  OD2 ASP B 390     -60.694  12.488  42.496  1.00131.27           O  
+ANISOU 6178  OD2 ASP B 390    15182  22095  12599  -3061   4173   -169       O  
+ATOM   6179  N   LYS B 391     -64.781  15.516  41.256  1.00 98.36           N  
+ANISOU 6179  N   LYS B 391     9656  18399   9318  -2892   4404  -1206       N  
+ATOM   6180  CA  LYS B 391     -66.209  15.354  41.485  1.00127.25           C  
+ANISOU 6180  CA  LYS B 391    12996  22316  13037  -3066   4566  -1212       C  
+ATOM   6181  C   LYS B 391     -66.954  16.668  41.718  1.00111.04           C  
+ANISOU 6181  C   LYS B 391    10583  20478  11130  -2820   4639  -1597       C  
+ATOM   6182  O   LYS B 391     -68.014  16.687  42.344  1.00114.54           O  
+ANISOU 6182  O   LYS B 391    10763  21226  11532  -2905   4817  -1640       O  
+ATOM   6183  CB  LYS B 391     -66.421  14.436  42.687  1.00130.69           C  
+ANISOU 6183  CB  LYS B 391    13534  22983  13140  -3309   4734   -947       C  
+ATOM   6184  N   GLY B 392     -66.424  17.751  41.157  1.00103.97           N  
+ANISOU 6184  N   GLY B 392     9672  19407  10426  -2518   4504  -1868       N  
+ATOM   6185  CA  GLY B 392     -67.013  19.075  41.293  1.00102.70           C  
+ANISOU 6185  CA  GLY B 392     9209  19374  10437  -2246   4549  -2243       C  
+ATOM   6186  C   GLY B 392     -65.997  20.016  41.915  1.00111.66           C  
+ANISOU 6186  C   GLY B 392    10509  20458  11457  -1984   4497  -2472       C  
+ATOM   6187  O   GLY B 392     -66.074  21.237  41.770  1.00113.83           O  
+ANISOU 6187  O   GLY B 392    10637  20688  11925  -1713   4462  -2799       O  
+ATOM   6188  N   GLN B 393     -65.021  19.418  42.594  1.00109.16           N  
+ANISOU 6188  N   GLN B 393    10506  20138  10833  -2074   4480  -2288       N  
+ATOM   6189  CA  GLN B 393     -64.008  20.172  43.311  1.00108.84           C  
+ANISOU 6189  CA  GLN B 393    10627  20093  10633  -1880   4425  -2476       C  
+ATOM   6190  C   GLN B 393     -62.620  20.070  42.695  1.00108.98           C  
+ANISOU 6190  C   GLN B 393    10942  19792  10671  -1817   4220  -2379       C  
+ATOM   6191  O   GLN B 393     -62.307  19.154  41.932  1.00105.60           O  
+ANISOU 6191  O   GLN B 393    10669  19174  10281  -1957   4142  -2101       O  
+ATOM   6192  CB  GLN B 393     -63.952  19.707  44.771  1.00107.22           C  
+ANISOU 6192  CB  GLN B 393    10513  20209  10016  -2003   4572  -2378       C  
+ATOM   6193  N   VAL B 394     -61.801  21.054  43.031  1.00 94.89           N  
+ANISOU 6193  N   VAL B 394     9226  17958   8870  -1609   4137  -2630       N  
+ATOM   6194  CA  VAL B 394     -60.422  21.112  42.598  1.00 91.04           C  
+ANISOU 6194  CA  VAL B 394     8989  17216   8387  -1532   3951  -2581       C  
+ATOM   6195  C   VAL B 394     -59.589  20.145  43.421  1.00 91.64           C  
+ANISOU 6195  C   VAL B 394     9325  17404   8091  -1667   3945  -2305       C  
+ATOM   6196  O   VAL B 394     -59.617  20.190  44.651  1.00109.94           O  
+ANISOU 6196  O   VAL B 394    11647  20003  10121  -1695   4036  -2353       O  
+ATOM   6197  CB  VAL B 394     -59.870  22.525  42.737  1.00 95.00           C  
+ANISOU 6197  CB  VAL B 394     9453  17642   9002  -1293   3869  -2954       C  
+ATOM   6198  CG1 VAL B 394     -58.379  22.534  42.483  1.00 87.43           C  
+ANISOU 6198  CG1 VAL B 394     8740  16483   7995  -1245   3692  -2892       C  
+ATOM   6199  CG2 VAL B 394     -60.612  23.457  41.801  1.00 90.03           C  
+ANISOU 6199  CG2 VAL B 394     8593  16846   8767  -1137   3855  -3192       C  
+ATOM   6200  N   VAL B 395     -58.878  19.249  42.747  1.00 91.36           N  
+ANISOU 6200  N   VAL B 395     9504  17158   8050  -1747   3843  -2013       N  
+ATOM   6201  CA  VAL B 395     -58.058  18.256  43.428  1.00 89.37           C  
+ANISOU 6201  CA  VAL B 395     9511  16981   7465  -1855   3823  -1715       C  
+ATOM   6202  C   VAL B 395     -56.664  18.211  42.799  1.00 99.62           C  
+ANISOU 6202  C   VAL B 395    11019  18028   8803  -1747   3637  -1645       C  
+ATOM   6203  O   VAL B 395     -56.516  18.437  41.597  1.00101.35           O  
+ANISOU 6203  O   VAL B 395    11227  17976   9305  -1679   3552  -1689       O  
+ATOM   6204  CB  VAL B 395     -58.718  16.856  43.377  1.00102.58           C  
+ANISOU 6204  CB  VAL B 395    11256  18680   9040  -2113   3928  -1340       C  
+ATOM   6205  CG1 VAL B 395     -57.860  15.821  44.085  1.00109.24           C  
+ANISOU 6205  CG1 VAL B 395    12388  19576   9543  -2206   3902  -1005       C  
+ATOM   6206  CG2 VAL B 395     -60.101  16.899  44.002  1.00 94.96           C  
+ANISOU 6206  CG2 VAL B 395    10051  17992   8037  -2235   4124  -1405       C  
+ATOM   6207  N   LYS B 396     -55.652  17.930  43.619  1.00 94.99           N  
+ANISOU 6207  N   LYS B 396    10613  17558   7923  -1729   3575  -1539       N  
+ATOM   6208  CA  LYS B 396     -54.279  17.797  43.146  1.00 83.60           C  
+ANISOU 6208  CA  LYS B 396     9354  15935   6477  -1629   3407  -1450       C  
+ATOM   6209  C   LYS B 396     -54.163  16.702  42.091  1.00 81.27           C  
+ANISOU 6209  C   LYS B 396     9218  15376   6283  -1709   3383  -1135       C  
+ATOM   6210  O   LYS B 396     -54.786  15.646  42.203  1.00 94.78           O  
+ANISOU 6210  O   LYS B 396    11008  17110   7895  -1891   3480   -860       O  
+ATOM   6211  CB  LYS B 396     -53.330  17.507  44.314  1.00 85.83           C  
+ANISOU 6211  CB  LYS B 396     9783  16449   6378  -1621   3351  -1343       C  
+ATOM   6212  CG  LYS B 396     -52.972  18.729  45.150  1.00 87.39           C  
+ANISOU 6212  CG  LYS B 396     9861  16853   6490  -1512   3307  -1704       C  
+ATOM   6213  CD  LYS B 396     -52.172  18.347  46.386  1.00 95.96           C  
+ANISOU 6213  CD  LYS B 396    11079  18231   7152  -1537   3255  -1581       C  
+ATOM   6214  CE  LYS B 396     -51.472  19.556  46.989  1.00107.78           C  
+ANISOU 6214  CE  LYS B 396    12483  19883   8584  -1429   3153  -1951       C  
+ATOM   6215  NZ  LYS B 396     -52.419  20.668  47.278  1.00111.88           N  
+ANISOU 6215  NZ  LYS B 396    12795  20477   9235  -1403   3265  -2338       N  
+ATOM   6216  N   ALA B 397     -53.353  16.966  41.070  1.00 88.82           N  
+ANISOU 6216  N   ALA B 397    10229  16084   7433  -1585   3260  -1181       N  
+ATOM   6217  CA  ALA B 397     -53.194  16.059  39.938  1.00 85.75           C  
+ANISOU 6217  CA  ALA B 397     9994  15428   7160  -1640   3236   -941       C  
+ATOM   6218  C   ALA B 397     -52.051  15.069  40.146  1.00 85.95           C  
+ANISOU 6218  C   ALA B 397    10284  15429   6943  -1624   3166   -637       C  
+ATOM   6219  O   ALA B 397     -50.878  15.432  40.064  1.00 78.15           O  
+ANISOU 6219  O   ALA B 397     9340  14425   5928  -1463   3047   -698       O  
+ATOM   6220  CB  ALA B 397     -52.977  16.851  38.659  1.00 72.09           C  
+ANISOU 6220  CB  ALA B 397     8182  13450   5759  -1513   3158  -1146       C  
+ATOM   6221  N   LYS B 398     -52.414  13.821  40.427  1.00 96.17           N  
+ANISOU 6221  N   LYS B 398    11747  16728   8063  -1798   3239   -302       N  
+ATOM   6222  CA  LYS B 398     -51.454  12.743  40.661  1.00 89.22           C  
+ANISOU 6222  CA  LYS B 398    11148  15814   6939  -1790   3179     44       C  
+ATOM   6223  C   LYS B 398     -50.475  12.559  39.498  1.00 92.23           C  
+ANISOU 6223  C   LYS B 398    11656  15936   7451  -1655   3079     84       C  
+ATOM   6224  O   LYS B 398     -49.328  12.149  39.696  1.00102.92           O  
+ANISOU 6224  O   LYS B 398    13161  17320   8623  -1531   2983    252       O  
+ATOM   6225  CB  LYS B 398     -52.212  11.437  40.919  1.00 81.23           C  
+ANISOU 6225  CB  LYS B 398    10311  14756   5799  -2040   3283    408       C  
+ATOM   6226  CG  LYS B 398     -51.346  10.233  41.250  1.00 84.09           C  
+ANISOU 6226  CG  LYS B 398    10999  15054   5897  -2044   3220    826       C  
+ATOM   6227  CD  LYS B 398     -52.168   8.952  41.192  1.00 99.69           C  
+ANISOU 6227  CD  LYS B 398    13178  16855   7846  -2328   3316   1184       C  
+ATOM   6228  CE  LYS B 398     -51.526   7.835  42.000  1.00102.12           C  
+ANISOU 6228  CE  LYS B 398    13799  17164   7838  -2348   3262   1634       C  
+ATOM   6229  NZ  LYS B 398     -50.145   7.528  41.539  1.00104.86           N  
+ANISOU 6229  NZ  LYS B 398    14349  17302   8193  -2080   3072   1756       N  
+ATOM   6230  N   GLY B 399     -50.935  12.872  38.289  1.00 78.78           N  
+ANISOU 6230  N   GLY B 399     9878  14006   6049  -1673   3101    -72       N  
+ATOM   6231  CA  GLY B 399     -50.124  12.742  37.092  1.00 72.32           C  
+ANISOU 6231  CA  GLY B 399     9184  12824   5469  -1500   2962    -55       C  
+ATOM   6232  C   GLY B 399     -48.829  13.531  37.135  1.00 69.69           C  
+ANISOU 6232  C   GLY B 399     8781  12561   5138  -1252   2839   -206       C  
+ATOM   6233  O   GLY B 399     -47.785  13.050  36.692  1.00 67.99           O  
+ANISOU 6233  O   GLY B 399     8719  12142   4971  -1080   2712    -62       O  
+ATOM   6234  N   VAL B 400     -48.899  14.747  37.669  1.00 68.64           N  
+ANISOU 6234  N   VAL B 400     8405  12716   4961  -1237   2880   -510       N  
+ATOM   6235  CA  VAL B 400     -47.728  15.611  37.777  1.00 72.18           C  
+ANISOU 6235  CA  VAL B 400     8756  13252   5417  -1053   2763   -687       C  
+ATOM   6236  C   VAL B 400     -46.711  15.011  38.748  1.00 79.53           C  
+ANISOU 6236  C   VAL B 400     9797  14386   6033   -977   2669   -476       C  
+ATOM   6237  O   VAL B 400     -45.503  15.080  38.517  1.00 69.20           O  
+ANISOU 6237  O   VAL B 400     8503  13022   4769   -799   2525   -449       O  
+ATOM   6238  CB  VAL B 400     -48.117  17.031  38.232  1.00 76.80           C  
+ANISOU 6238  CB  VAL B 400     9105  13948   6127  -1040   2753  -1046       C  
+ATOM   6239  CG1 VAL B 400     -46.890  17.930  38.282  1.00 67.23           C  
+ANISOU 6239  CG1 VAL B 400     7799  12806   4939   -902   2631  -1235       C  
+ATOM   6240  CG2 VAL B 400     -49.160  17.617  37.292  1.00 72.35           C  
+ANISOU 6240  CG2 VAL B 400     8427  13176   5886  -1081   2814  -1217       C  
+ATOM   6241  N   GLN B 401     -47.211  14.419  39.830  1.00 72.79           N  
+ANISOU 6241  N   GLN B 401     9016  13751   4890  -1103   2733   -308       N  
+ATOM   6242  CA  GLN B 401     -46.361  13.741  40.807  1.00 75.43           C  
+ANISOU 6242  CA  GLN B 401     9476  14321   4863  -1049   2647    -52       C  
+ATOM   6243  C   GLN B 401     -45.690  12.508  40.213  1.00 90.11           C  
+ANISOU 6243  C   GLN B 401    11589  15842   6806   -920   2533    314       C  
+ATOM   6244  O   GLN B 401     -44.505  12.247  40.461  1.00 85.60           O  
+ANISOU 6244  O   GLN B 401    11066  15316   6142   -728   2371    448       O  
+ATOM   6245  CB  GLN B 401     -47.187  13.335  42.032  1.00 78.93           C  
+ANISOU 6245  CB  GLN B 401     9972  14958   5057  -1215   2723     81       C  
+ATOM   6246  CG  GLN B 401     -46.392  12.653  43.139  1.00 82.27           C  
+ANISOU 6246  CG  GLN B 401    10538  15640   5080  -1169   2618    370       C  
+ATOM   6247  CD  GLN B 401     -45.467  13.591  43.879  1.00 88.63           C  
+ANISOU 6247  CD  GLN B 401    11181  16752   5743  -1046   2474    131       C  
+ATOM   6248  OE1 GLN B 401     -45.812  14.741  44.144  1.00 88.59           O  
+ANISOU 6248  OE1 GLN B 401    10976  16841   5842  -1078   2499   -247       O  
+ATOM   6249  NE2 GLN B 401     -44.280  13.102  44.221  1.00 92.76           N  
+ANISOU 6249  NE2 GLN B 401    11785  17437   6022   -902   2308    358       N  
+ATOM   6250  N   SER B 402     -46.446  11.766  39.410  1.00 89.68           N  
+ANISOU 6250  N   SER B 402    11688  15440   6948  -1015   2606    455       N  
+ATOM   6251  CA  SER B 402     -45.901  10.614  38.704  1.00 78.06           C  
+ANISOU 6251  CA  SER B 402    10479  13570   5611   -883   2509    747       C  
+ATOM   6252  C   SER B 402     -44.799  11.040  37.744  1.00 74.68           C  
+ANISOU 6252  C   SER B 402     9985  12960   5430   -621   2386    605       C  
+ATOM   6253  O   SER B 402     -43.738  10.419  37.684  1.00 72.92           O  
+ANISOU 6253  O   SER B 402     9878  12633   5196   -400   2258    795       O  
+ATOM   6254  CB  SER B 402     -47.007   9.877  37.944  1.00 75.67           C  
+ANISOU 6254  CB  SER B 402    10334  12924   5491  -1072   2609    848       C  
+ATOM   6255  OG  SER B 402     -46.479   8.801  37.188  1.00 89.72           O  
+ANISOU 6255  OG  SER B 402    12387  14279   7423   -934   2516   1075       O  
+ATOM   6256  N   GLU B 403     -45.056  12.112  37.002  1.00 76.65           N  
+ANISOU 6256  N   GLU B 403    10037  13183   5902   -641   2430    281       N  
+ATOM   6257  CA  GLU B 403     -44.082  12.641  36.056  1.00 71.72           C  
+ANISOU 6257  CA  GLU B 403     9327  12415   5507   -436   2342    138       C  
+ATOM   6258  C   GLU B 403     -42.834  13.168  36.760  1.00 74.47           C  
+ANISOU 6258  C   GLU B 403     9520  13058   5717   -279   2221     87       C  
+ATOM   6259  O   GLU B 403     -41.732  13.095  36.215  1.00 75.68           O  
+ANISOU 6259  O   GLU B 403     9653  13116   5985    -71   2124    119       O  
+ATOM   6260  CB  GLU B 403     -44.721  13.733  35.197  1.00 64.35           C  
+ANISOU 6260  CB  GLU B 403     8226  11403   4823   -522   2412   -168       C  
+ATOM   6261  CG  GLU B 403     -45.676  13.180  34.146  1.00 63.25           C  
+ANISOU 6261  CG  GLU B 403     8232  10927   4875   -622   2477   -118       C  
+ATOM   6262  CD  GLU B 403     -46.613  14.230  33.581  1.00 69.18           C  
+ANISOU 6262  CD  GLU B 403     8802  11671   5813   -741   2544   -386       C  
+ATOM   6263  OE1 GLU B 403     -46.331  15.433  33.746  1.00 62.82           O  
+ANISOU 6263  OE1 GLU B 403     7784  11030   5055   -702   2532   -621       O  
+ATOM   6264  OE2 GLU B 403     -47.635  13.849  32.972  1.00 80.57           O  
+ANISOU 6264  OE2 GLU B 403    10315  12934   7365   -876   2595   -360       O  
+ATOM   6265  N   PHE B 404     -43.005  13.696  37.969  1.00 80.70           N  
+ANISOU 6265  N   PHE B 404    10186  14227   6249   -383   2227     -4       N  
+ATOM   6266  CA  PHE B 404     -41.862  14.115  38.775  1.00 84.89           C  
+ANISOU 6266  CA  PHE B 404    10577  15078   6598   -266   2086    -44       C  
+ATOM   6267  C   PHE B 404     -41.014  12.912  39.168  1.00 88.40           C  
+ANISOU 6267  C   PHE B 404    11190  15519   6880    -87   1955    325       C  
+ATOM   6268  O   PHE B 404     -39.792  12.909  38.970  1.00 94.83           O  
+ANISOU 6268  O   PHE B 404    11921  16357   7754    126   1814    360       O  
+ATOM   6269  CB  PHE B 404     -42.311  14.872  40.026  1.00 84.74           C  
+ANISOU 6269  CB  PHE B 404    10423  15480   6294   -428   2123   -238       C  
+ATOM   6270  CG  PHE B 404     -41.178  15.250  40.944  1.00 83.43           C  
+ANISOU 6270  CG  PHE B 404    10125  15679   5894   -338   1953   -284       C  
+ATOM   6271  CD1 PHE B 404     -40.811  14.428  41.999  1.00 90.93           C  
+ANISOU 6271  CD1 PHE B 404    11187  16882   6481   -297   1856      2       C  
+ATOM   6272  CD2 PHE B 404     -40.482  16.431  40.751  1.00 74.30           C  
+ANISOU 6272  CD2 PHE B 404     8736  14613   4881   -310   1876   -602       C  
+ATOM   6273  CE1 PHE B 404     -39.768  14.777  42.838  1.00 88.22           C  
+ANISOU 6273  CE1 PHE B 404    10707  16906   5907   -217   1670    -42       C  
+ATOM   6274  CE2 PHE B 404     -39.441  16.786  41.588  1.00 77.76           C  
+ANISOU 6274  CE2 PHE B 404     9035  15402   5109   -256   1699   -663       C  
+ATOM   6275  CZ  PHE B 404     -39.084  15.958  42.633  1.00 79.77           C  
+ANISOU 6275  CZ  PHE B 404     9384  15937   4987   -204   1589   -389       C  
+ATOM   6276  N   ASN B 405     -41.666  11.899  39.736  1.00 89.34           N  
+ANISOU 6276  N   ASN B 405    11534  15612   6801   -174   2002    611       N  
+ATOM   6277  CA  ASN B 405     -40.971  10.675  40.123  1.00 85.63           C  
+ANISOU 6277  CA  ASN B 405    11267  15080   6188      1   1874   1006       C  
+ATOM   6278  C   ASN B 405     -40.189  10.094  38.951  1.00 84.63           C  
+ANISOU 6278  C   ASN B 405    11227  14561   6369    259   1809   1096       C  
+ATOM   6279  O   ASN B 405     -38.988   9.841  39.061  1.00 94.20           O  
+ANISOU 6279  O   ASN B 405    12389  15840   7564    519   1651   1212       O  
+ATOM   6280  CB  ASN B 405     -41.955   9.638  40.668  1.00 84.30           C  
+ANISOU 6280  CB  ASN B 405    11370  14827   5833   -176   1964   1315       C  
+ATOM   6281  CG  ASN B 405     -42.664  10.109  41.923  1.00 86.26           C  
+ANISOU 6281  CG  ASN B 405    11534  15523   5717   -417   2047   1257       C  
+ATOM   6282  OD1 ASN B 405     -42.108  10.872  42.713  1.00 93.10           O  
+ANISOU 6282  OD1 ASN B 405    12212  16800   6363   -384   1963   1100       O  
+ATOM   6283  ND2 ASN B 405     -43.894   9.649  42.116  1.00 85.33           N  
+ANISOU 6283  ND2 ASN B 405    11549  15348   5525   -671   2216   1372       N  
+ATOM   6284  N   ILE B 406     -40.872   9.918  37.824  1.00 75.33           N  
+ANISOU 6284  N   ILE B 406    10157  13003   5463    193   1930   1024       N  
+ATOM   6285  CA  ILE B 406     -40.245   9.399  36.612  1.00 83.51           C  
+ANISOU 6285  CA  ILE B 406    11288  13665   6777    421   1902   1060       C  
+ATOM   6286  C   ILE B 406     -39.075  10.273  36.171  1.00 84.52           C  
+ANISOU 6286  C   ILE B 406    11139  13944   7032    614   1829    851       C  
+ATOM   6287  O   ILE B 406     -38.033   9.764  35.754  1.00 77.67           O  
+ANISOU 6287  O   ILE B 406    10282  12970   6260    894   1746    958       O  
+ATOM   6288  CB  ILE B 406     -41.262   9.287  35.464  1.00 83.64           C  
+ANISOU 6288  CB  ILE B 406    11433  13315   7031    270   2041    949       C  
+ATOM   6289  CG1 ILE B 406     -42.362   8.290  35.834  1.00 78.46           C  
+ANISOU 6289  CG1 ILE B 406    11053  12480   6280     64   2106   1181       C  
+ATOM   6290  CG2 ILE B 406     -40.577   8.837  34.190  1.00 86.06           C  
+ANISOU 6290  CG2 ILE B 406    11834  13277   7588    509   2023    938       C  
+ATOM   6291  CD1 ILE B 406     -43.543   8.301  34.890  1.00 72.87           C  
+ANISOU 6291  CD1 ILE B 406    10418  11502   5766   -156   2229   1046       C  
+ATOM   6292  N   SER B 407     -39.250  11.586  36.273  1.00 88.90           N  
+ANISOU 6292  N   SER B 407    11437  14742   7598    460   1864    551       N  
+ATOM   6293  CA  SER B 407     -38.182  12.519  35.944  1.00 78.00           C  
+ANISOU 6293  CA  SER B 407     9778  13524   6334    576   1796    352       C  
+ATOM   6294  C   SER B 407     -36.942  12.251  36.795  1.00 81.93           C  
+ANISOU 6294  C   SER B 407    10161  14311   6657    780   1616    501       C  
+ATOM   6295  O   SER B 407     -35.823  12.267  36.285  1.00 88.47           O  
+ANISOU 6295  O   SER B 407    10849  15146   7621    996   1546    501       O  
+ATOM   6296  CB  SER B 407     -38.643  13.966  36.128  1.00 73.93           C  
+ANISOU 6296  CB  SER B 407     9039  13209   5841    353   1846     18       C  
+ATOM   6297  OG  SER B 407     -39.602  14.328  35.150  1.00 82.05           O  
+ANISOU 6297  OG  SER B 407    10122  13969   7086    220   1984   -127       O  
+ATOM   6298  N   PHE B 408     -37.136  12.002  38.088  1.00 88.87           N  
+ANISOU 6298  N   PHE B 408    11087  15458   7222    711   1540    636       N  
+ATOM   6299  CA  PHE B 408     -35.993  11.827  38.984  1.00 89.62           C  
+ANISOU 6299  CA  PHE B 408    11053  15884   7113    891   1335    776       C  
+ATOM   6300  C   PHE B 408     -35.349  10.440  38.859  1.00 91.13           C  
+ANISOU 6300  C   PHE B 408    11433  15873   7320   1200   1239   1148       C  
+ATOM   6301  O   PHE B 408     -34.141  10.299  39.064  1.00 91.61           O  
+ANISOU 6301  O   PHE B 408    11329  16114   7364   1450   1070   1239       O  
+ATOM   6302  CB  PHE B 408     -36.403  12.084  40.436  1.00 95.83           C  
+ANISOU 6302  CB  PHE B 408    11829  17070   7511    709   1277    787       C  
+ATOM   6303  CG  PHE B 408     -35.334  11.736  41.432  1.00102.02           C  
+ANISOU 6303  CG  PHE B 408    12527  18206   8030    888   1039    990       C  
+ATOM   6304  CD1 PHE B 408     -34.259  12.587  41.635  1.00 93.10           C  
+ANISOU 6304  CD1 PHE B 408    11068  17404   6902    948    883    790       C  
+ATOM   6305  CD2 PHE B 408     -35.404  10.566  42.168  1.00111.86           C  
+ANISOU 6305  CD2 PHE B 408    14019  19456   9027    985    956   1392       C  
+ATOM   6306  CE1 PHE B 408     -33.269  12.272  42.545  1.00 99.00           C  
+ANISOU 6306  CE1 PHE B 408    11708  18508   7400   1115    635    976       C  
+ATOM   6307  CE2 PHE B 408     -34.420  10.246  43.081  1.00114.35           C  
+ANISOU 6307  CE2 PHE B 408    14252  20108   9088   1169    709   1603       C  
+ATOM   6308  CZ  PHE B 408     -33.350  11.100  43.271  1.00113.38           C  
+ANISOU 6308  CZ  PHE B 408    13776  20342   8961   1240    541   1388       C  
+ATOM   6309  N   GLU B 409     -36.146   9.426  38.523  1.00 99.15           N  
+ANISOU 6309  N   GLU B 409    12782  16506   8383   1186   1338   1355       N  
+ATOM   6310  CA  GLU B 409     -35.607   8.081  38.324  1.00103.53           C  
+ANISOU 6310  CA  GLU B 409    13563  16776   8998   1488   1256   1691       C  
+ATOM   6311  C   GLU B 409     -34.841   7.995  37.015  1.00101.32           C  
+ANISOU 6311  C   GLU B 409    13206  16241   9051   1746   1291   1578       C  
+ATOM   6312  O   GLU B 409     -34.134   7.019  36.763  1.00108.89           O  
+ANISOU 6312  O   GLU B 409    14279  16995  10098   2072   1216   1791       O  
+ATOM   6313  CB  GLU B 409     -36.708   7.014  38.337  1.00107.33           C  
+ANISOU 6313  CB  GLU B 409    14446  16885   9450   1360   1351   1934       C  
+ATOM   6314  CG  GLU B 409     -37.688   7.091  39.491  1.00116.77           C  
+ANISOU 6314  CG  GLU B 409    15729  18316  10323   1046   1386   2035       C  
+ATOM   6315  CD  GLU B 409     -38.905   6.220  39.259  1.00116.91           C  
+ANISOU 6315  CD  GLU B 409    16091  17947  10381    841   1525   2207       C  
+ATOM   6316  OE1 GLU B 409     -39.056   5.724  38.124  1.00115.20           O  
+ANISOU 6316  OE1 GLU B 409    16031  17282  10458    912   1594   2173       O  
+ATOM   6317  OE2 GLU B 409     -39.708   6.038  40.199  1.00120.27           O  
+ANISOU 6317  OE2 GLU B 409    16625  18533  10539    593   1570   2364       O  
+ATOM   6318  N   GLN B 410     -34.979   9.027  36.190  1.00 92.77           N  
+ANISOU 6318  N   GLN B 410    11931  15172   8144   1610   1410   1246       N  
+ATOM   6319  CA  GLN B 410     -34.318   9.076  34.892  1.00 90.66           C  
+ANISOU 6319  CA  GLN B 410    11577  14709   8162   1808   1478   1116       C  
+ATOM   6320  C   GLN B 410     -33.102   9.999  34.959  1.00 99.74           C  
+ANISOU 6320  C   GLN B 410    12312  16239   9345   1910   1389    963       C  
+ATOM   6321  O   GLN B 410     -32.478  10.308  33.942  1.00 98.09           O  
+ANISOU 6321  O   GLN B 410    11947  15972   9349   2027   1461    823       O  
+ATOM   6322  CB  GLN B 410     -35.307   9.561  33.832  1.00 82.63           C  
+ANISOU 6322  CB  GLN B 410    10646  13433   7316   1574   1667    889       C  
+ATOM   6323  CG  GLN B 410     -34.893   9.322  32.398  1.00 89.35           C  
+ANISOU 6323  CG  GLN B 410    11532  14002   8415   1757   1767    800       C  
+ATOM   6324  CD  GLN B 410     -35.818  10.010  31.422  1.00 90.24           C  
+ANISOU 6324  CD  GLN B 410    11681  13948   8659   1506   1918    570       C  
+ATOM   6325  OE1 GLN B 410     -35.405  10.913  30.696  1.00 87.11           O  
+ANISOU 6325  OE1 GLN B 410    11067  13645   8386   1486   1974    375       O  
+ATOM   6326  NE2 GLN B 410     -37.079   9.588  31.399  1.00 74.62           N  
+ANISOU 6326  NE2 GLN B 410     9968  11730   6654   1302   1976    609       N  
+ATOM   6327  N   ASN B 411     -32.759  10.394  36.183  1.00107.36           N  
+ANISOU 6327  N   ASN B 411    13103  17609  10080   1855   1230    999       N  
+ATOM   6328  CA  ASN B 411     -31.699  11.360  36.456  1.00105.69           C  
+ANISOU 6328  CA  ASN B 411    12483  17809   9867   1873   1115    836       C  
+ATOM   6329  C   ASN B 411     -31.873  12.591  35.551  1.00 88.24           C  
+ANISOU 6329  C   ASN B 411    10093  15566   7870   1654   1261    500       C  
+ATOM   6330  O   ASN B 411     -30.987  12.957  34.778  1.00 87.56           O  
+ANISOU 6330  O   ASN B 411     9772  15518   7978   1764   1286    404       O  
+ATOM   6331  CB  ASN B 411     -30.323  10.696  36.282  1.00114.94           C  
+ANISOU 6331  CB  ASN B 411    13492  19059  11122   2272    991   1005       C  
+ATOM   6332  CG  ASN B 411     -29.157  11.664  36.443  1.00119.38           C  
+ANISOU 6332  CG  ASN B 411    13587  20053  11721   2279    875    837       C  
+ATOM   6333  OD1 ASN B 411     -29.319  12.794  36.908  1.00122.57           O  
+ANISOU 6333  OD1 ASN B 411    13812  20715  12044   1983    843    612       O  
+ATOM   6334  ND2 ASN B 411     -27.967  11.211  36.071  1.00119.05           N  
+ANISOU 6334  ND2 ASN B 411    13339  20088  11809   2618    809    936       N  
+ATOM   6335  N   ASN B 412     -33.063  13.179  35.611  1.00 92.28           N  
+ANISOU 6335  N   ASN B 412    10726  15987   8350   1351   1368    344       N  
+ATOM   6336  CA  ASN B 412     -33.329  14.455  34.961  1.00 82.17           C  
+ANISOU 6336  CA  ASN B 412     9288  14689   7245   1123   1474     40       C  
+ATOM   6337  C   ASN B 412     -33.372  15.568  35.993  1.00 77.40           C  
+ANISOU 6337  C   ASN B 412     8483  14433   6494    892   1380   -170       C  
+ATOM   6338  O   ASN B 412     -33.750  15.339  37.141  1.00 81.07           O  
+ANISOU 6338  O   ASN B 412     9026  15092   6687    831   1300   -105       O  
+ATOM   6339  CB  ASN B 412     -34.650  14.428  34.185  1.00 82.65           C  
+ANISOU 6339  CB  ASN B 412     9600  14385   7417    967   1654    -22       C  
+ATOM   6340  CG  ASN B 412     -34.562  13.640  32.898  1.00 83.36           C  
+ANISOU 6340  CG  ASN B 412     9855  14123   7694   1147   1760     78       C  
+ATOM   6341  OD1 ASN B 412     -33.526  13.057  32.581  1.00 88.86           O  
+ANISOU 6341  OD1 ASN B 412    10489  14830   8443   1416   1721    194       O  
+ATOM   6342  ND2 ASN B 412     -35.651  13.630  32.139  1.00 74.20           N  
+ANISOU 6342  ND2 ASN B 412     8894  12666   6631   1007   1892     16       N  
+ATOM   6343  N   TYR B 413     -32.987  16.771  35.585  1.00 76.18           N  
+ANISOU 6343  N   TYR B 413     8083  14352   6509    754   1394   -423       N  
+ATOM   6344  CA  TYR B 413     -33.044  17.918  36.478  1.00 76.88           C  
+ANISOU 6344  CA  TYR B 413     7997  14719   6496    520   1310   -678       C  
+ATOM   6345  C   TYR B 413     -34.501  18.286  36.739  1.00 77.81           C  
+ANISOU 6345  C   TYR B 413     8305  14705   6554    311   1428   -820       C  
+ATOM   6346  O   TYR B 413     -35.279  18.463  35.800  1.00 80.28           O  
+ANISOU 6346  O   TYR B 413     8735  14698   7068    248   1581   -872       O  
+ATOM   6347  CB  TYR B 413     -32.285  19.102  35.882  1.00 83.46           C  
+ANISOU 6347  CB  TYR B 413     8545  15594   7571    405   1303   -902       C  
+ATOM   6348  CG  TYR B 413     -30.793  18.879  35.763  1.00 96.70           C  
+ANISOU 6348  CG  TYR B 413     9951  17496   9296    578   1182   -797       C  
+ATOM   6349  CD1 TYR B 413     -30.016  18.648  36.889  1.00101.48           C  
+ANISOU 6349  CD1 TYR B 413    10392  18495   9672    652    966   -738       C  
+ATOM   6350  CD2 TYR B 413     -30.162  18.909  34.525  1.00 88.12           C  
+ANISOU 6350  CD2 TYR B 413     8752  16260   8469    668   1285   -756       C  
+ATOM   6351  CE1 TYR B 413     -28.652  18.445  36.788  1.00103.50           C  
+ANISOU 6351  CE1 TYR B 413    10354  18986   9985    824    844   -641       C  
+ATOM   6352  CE2 TYR B 413     -28.797  18.708  34.413  1.00 88.02           C  
+ANISOU 6352  CE2 TYR B 413     8447  16488   8509    834   1195   -669       C  
+ATOM   6353  CZ  TYR B 413     -28.048  18.477  35.548  1.00 95.61           C  
+ANISOU 6353  CZ  TYR B 413     9223  17837   9269    917    969   -612       C  
+ATOM   6354  OH  TYR B 413     -26.691  18.277  35.445  1.00 99.58           O  
+ANISOU 6354  OH  TYR B 413     9392  18607   9836   1095    867   -524       O  
+ATOM   6355  N   VAL B 414     -34.868  18.398  38.012  1.00 86.18           N  
+ANISOU 6355  N   VAL B 414     9381  16038   7325    209   1356   -882       N  
+ATOM   6356  CA  VAL B 414     -36.253  18.664  38.384  1.00 81.32           C  
+ANISOU 6356  CA  VAL B 414     8919  15360   6621     32   1483  -1012       C  
+ATOM   6357  C   VAL B 414     -36.431  20.116  38.811  1.00 91.34           C  
+ANISOU 6357  C   VAL B 414    10017  16768   7920   -177   1473  -1407       C  
+ATOM   6358  O   VAL B 414     -35.790  20.578  39.755  1.00103.19           O  
+ANISOU 6358  O   VAL B 414    11365  18609   9233   -230   1326  -1543       O  
+ATOM   6359  CB  VAL B 414     -36.722  17.737  39.521  1.00 73.59           C  
+ANISOU 6359  CB  VAL B 414     8109  14585   5265     48   1456   -807       C  
+ATOM   6360  N   VAL B 415     -37.303  20.833  38.108  1.00 79.85           N  
+ANISOU 6360  N   VAL B 415     8594  15038   6707   -289   1615  -1595       N  
+ATOM   6361  CA  VAL B 415     -37.524  22.251  38.370  1.00 73.88           C  
+ANISOU 6361  CA  VAL B 415     7701  14318   6050   -463   1615  -1981       C  
+ATOM   6362  C   VAL B 415     -39.001  22.549  38.631  1.00 74.04           C  
+ANISOU 6362  C   VAL B 415     7829  14261   6041   -561   1769  -2146       C  
+ATOM   6363  O   VAL B 415     -39.749  22.881  37.707  1.00 78.82           O  
+ANISOU 6363  O   VAL B 415     8482  14547   6918   -582   1884  -2193       O  
+ATOM   6364  CB  VAL B 415     -37.026  23.128  37.202  1.00 78.36           C  
+ANISOU 6364  CB  VAL B 415     8151  14615   7007   -501   1621  -2087       C  
+ATOM   6365  CG1 VAL B 415     -37.116  24.602  37.568  1.00 72.39           C  
+ANISOU 6365  CG1 VAL B 415     7267  13872   6366   -682   1589  -2482       C  
+ATOM   6366  CG2 VAL B 415     -35.595  22.763  36.835  1.00 82.27           C  
+ANISOU 6366  CG2 VAL B 415     8507  15203   7547   -396   1506  -1907       C  
+ATOM   6367  N   PRO B 416     -39.430  22.404  39.894  1.00 77.27           N  
+ANISOU 6367  N   PRO B 416     8266  14989   6103   -616   1771  -2223       N  
+ATOM   6368  CA  PRO B 416     -40.798  22.713  40.322  1.00 79.96           C  
+ANISOU 6368  CA  PRO B 416     8662  15347   6373   -708   1933  -2410       C  
+ATOM   6369  C   PRO B 416     -40.986  24.195  40.657  1.00 90.50           C  
+ANISOU 6369  C   PRO B 416     9860  16706   7820   -815   1935  -2876       C  
+ATOM   6370  O   PRO B 416     -40.332  24.724  41.555  1.00 89.62           O  
+ANISOU 6370  O   PRO B 416     9654  16877   7520   -876   1817  -3091       O  
+ATOM   6371  CB  PRO B 416     -40.970  21.839  41.563  1.00 74.37           C  
+ANISOU 6371  CB  PRO B 416     8040  15020   5198   -718   1931  -2255       C  
+ATOM   6372  CG  PRO B 416     -39.596  21.762  42.134  1.00 76.42           C  
+ANISOU 6372  CG  PRO B 416     8215  15548   5273   -672   1713  -2201       C  
+ATOM   6373  CD  PRO B 416     -38.656  21.741  40.959  1.00 81.37           C  
+ANISOU 6373  CD  PRO B 416     8778  15895   6246   -571   1628  -2071       C  
+ATOM   6374  N   VAL B 417     -41.895  24.846  39.936  1.00 86.23           N  
+ANISOU 6374  N   VAL B 417     9317  15860   7586   -832   2058  -3035       N  
+ATOM   6375  CA  VAL B 417     -42.200  26.261  40.139  1.00 78.65           C  
+ANISOU 6375  CA  VAL B 417     8254  14830   6798   -902   2073  -3476       C  
+ATOM   6376  C   VAL B 417     -43.226  26.515  41.242  1.00 81.88           C  
+ANISOU 6376  C   VAL B 417     8680  15365   7066   -929   2122  -3647       C  
+ATOM   6377  O   VAL B 417     -44.434  26.443  41.008  1.00 74.37           O  
+ANISOU 6377  O   VAL B 417     7767  14234   6256   -895   2237  -3603       O  
+ATOM   6378  CB  VAL B 417     -42.716  26.901  38.838  1.00 72.35           C  
+ANISOU 6378  CB  VAL B 417     7455  13570   6462   -874   2131  -3509       C  
+ATOM   6379  CG1 VAL B 417     -42.872  28.411  39.009  1.00 73.17           C  
+ANISOU 6379  CG1 VAL B 417     7470  13538   6792   -930   2116  -3950       C  
+ATOM   6380  CG2 VAL B 417     -41.770  26.587  37.691  1.00 67.98           C  
+ANISOU 6380  CG2 VAL B 417     6919  12787   6123   -839   2041  -3223       C  
+ATOM   6381  N   GLY B 418     -42.738  26.811  42.443  1.00 89.94           N  
+ANISOU 6381  N   GLY B 418     9657  16711   7806   -990   2030  -3839       N  
+ATOM   6382  CA  GLY B 418     -43.605  27.035  43.585  1.00 98.32           C  
+ANISOU 6382  CA  GLY B 418    10729  17932   8697  -1014   2080  -3996       C  
+ATOM   6383  C   GLY B 418     -44.354  28.350  43.480  1.00 82.11           C  
+ANISOU 6383  C   GLY B 418     8605  15648   6945  -1009   2148  -4402       C  
+ATOM   6384  O   GLY B 418     -45.580  28.371  43.374  1.00 82.86           O  
+ANISOU 6384  O   GLY B 418     8709  15606   7169   -955   2280  -4391       O  
+ATOM   6385  N   ILE B 423     -49.464  21.222  43.382  1.00 94.24           N  
+ANISOU 6385  N   ILE B 423    10685  17265   7856  -1105   2805  -2292       N  
+ATOM   6386  CA  ILE B 423     -48.552  20.086  43.322  1.00 95.61           C  
+ANISOU 6386  CA  ILE B 423    11032  17467   7828  -1111   2729  -1940       C  
+ATOM   6387  C   ILE B 423     -47.127  20.544  43.029  1.00 93.29           C  
+ANISOU 6387  C   ILE B 423    10726  17163   7557  -1017   2563  -2032       C  
+ATOM   6388  O   ILE B 423     -46.162  19.933  43.490  1.00 86.14           O  
+ANISOU 6388  O   ILE B 423     9907  16439   6383   -998   2464  -1845       O  
+ATOM   6389  CB  ILE B 423     -48.988  19.064  42.257  1.00 76.56           C  
+ANISOU 6389  CB  ILE B 423     8730  14793   5567  -1140   2791  -1636       C  
+ATOM   6390  N   ALA B 424     -47.006  21.607  42.238  1.00 82.56           N  
+ANISOU 6390  N   ALA B 424     9250  15600   6518   -962   2533  -2306       N  
+ATOM   6391  CA  ALA B 424     -45.718  22.247  41.981  1.00 76.99           C  
+ANISOU 6391  CA  ALA B 424     8487  14902   5862   -905   2394  -2456       C  
+ATOM   6392  C   ALA B 424     -45.020  22.651  43.277  1.00 89.39           C  
+ANISOU 6392  C   ALA B 424    10008  16836   7120   -936   2295  -2626       C  
+ATOM   6393  O   ALA B 424     -43.842  22.350  43.482  1.00 78.47           O  
+ANISOU 6393  O   ALA B 424     8635  15632   5546   -910   2164  -2531       O  
+ATOM   6394  CB  ALA B 424     -45.906  23.458  41.085  1.00 72.99           C  
+ANISOU 6394  CB  ALA B 424     7863  14125   5744   -874   2404  -2755       C  
+ATOM   6395  N   LYS B 425     -45.761  23.331  44.146  1.00 86.19           N  
+ANISOU 6395  N   LYS B 425     9536  16559   6652   -984   2354  -2885       N  
+ATOM   6396  CA  LYS B 425     -45.247  23.752  45.444  1.00 87.44           C  
+ANISOU 6396  CA  LYS B 425     9653  17075   6494  -1028   2270  -3081       C  
+ATOM   6397  C   LYS B 425     -44.775  22.558  46.277  1.00 92.91           C  
+ANISOU 6397  C   LYS B 425    10467  18075   6759  -1050   2212  -2733       C  
+ATOM   6398  O   LYS B 425     -43.706  22.606  46.886  1.00 95.43           O  
+ANISOU 6398  O   LYS B 425    10766  18666   6827  -1051   2053  -2761       O  
+ATOM   6399  CB  LYS B 425     -46.309  24.549  46.207  1.00 90.16           C  
+ANISOU 6399  CB  LYS B 425     9925  17495   6838  -1061   2386  -3392       C  
+ATOM   6400  CG  LYS B 425     -45.960  26.023  46.392  1.00 99.52           C  
+ANISOU 6400  CG  LYS B 425    10987  18663   8165  -1059   2320  -3879       C  
+ATOM   6401  CD  LYS B 425     -46.951  26.729  47.304  1.00 91.89           C  
+ANISOU 6401  CD  LYS B 425     9959  17816   7138  -1068   2437  -4184       C  
+ATOM   6402  CE  LYS B 425     -46.599  28.200  47.461  1.00 93.59           C  
+ANISOU 6402  CE  LYS B 425    10078  17965   7518  -1061   2372  -4686       C  
+ATOM   6403  NZ  LYS B 425     -47.291  29.060  46.462  1.00101.56           N  
+ANISOU 6403  NZ  LYS B 425    11018  18575   8996   -980   2449  -4886       N  
+ATOM   6404  N   ASP B 426     -45.578  21.495  46.295  1.00 86.18           N  
+ANISOU 6404  N   ASP B 426     9737  17183   5825  -1073   2333  -2403       N  
+ATOM   6405  CA  ASP B 426     -45.245  20.269  47.024  1.00 94.24           C  
+ANISOU 6405  CA  ASP B 426    10908  18442   6456  -1096   2293  -2020       C  
+ATOM   6406  C   ASP B 426     -43.880  19.711  46.612  1.00104.91           C  
+ANISOU 6406  C   ASP B 426    12308  19824   7729  -1004   2117  -1795       C  
+ATOM   6407  O   ASP B 426     -43.063  19.322  47.459  1.00116.33           O  
+ANISOU 6407  O   ASP B 426    13792  21589   8820   -988   1975  -1660       O  
+ATOM   6408  CB  ASP B 426     -46.327  19.207  46.805  1.00 88.01           C  
+ANISOU 6408  CB  ASP B 426    10249  17509   5681  -1154   2462  -1694       C  
+ATOM   6409  CG  ASP B 426     -47.625  19.533  47.524  1.00 90.53           C  
+ANISOU 6409  CG  ASP B 426    10508  17939   5952  -1250   2635  -1848       C  
+ATOM   6410  OD1 ASP B 426     -47.872  20.723  47.826  1.00 91.46           O  
+ANISOU 6410  OD1 ASP B 426    10474  18118   6160  -1238   2652  -2252       O  
+ATOM   6411  OD2 ASP B 426     -48.394  18.589  47.806  1.00 91.98           O  
+ANISOU 6411  OD2 ASP B 426    10793  18154   6000  -1339   2761  -1564       O  
+ATOM   6412  N   LEU B 427     -43.632  19.709  45.305  1.00 87.66           N  
+ANISOU 6412  N   LEU B 427    10108  17329   5871   -932   2121  -1763       N  
+ATOM   6413  CA  LEU B 427     -42.385  19.195  44.763  1.00 86.28           C  
+ANISOU 6413  CA  LEU B 427     9952  17174   5658   -818   1982  -1561       C  
+ATOM   6414  C   LEU B 427     -41.263  20.174  45.051  1.00 90.93           C  
+ANISOU 6414  C   LEU B 427    10358  17994   6195   -799   1811  -1860       C  
+ATOM   6415  O   LEU B 427     -40.115  19.769  45.236  1.00 96.67           O  
+ANISOU 6415  O   LEU B 427    11060  18959   6709   -715   1646  -1707       O  
+ATOM   6416  CB  LEU B 427     -42.506  18.946  43.260  1.00 80.07           C  
+ANISOU 6416  CB  LEU B 427     9196  15995   5232   -752   2062  -1463       C  
+ATOM   6417  CG  LEU B 427     -43.626  18.009  42.806  1.00 83.34           C  
+ANISOU 6417  CG  LEU B 427     9778  16154   5732   -798   2222  -1201       C  
+ATOM   6418  CD1 LEU B 427     -43.752  18.059  41.295  1.00 73.53           C  
+ANISOU 6418  CD1 LEU B 427     8534  14536   4868   -747   2285  -1210       C  
+ATOM   6419  CD2 LEU B 427     -43.392  16.577  43.282  1.00 83.70           C  
+ANISOU 6419  CD2 LEU B 427    10027  16320   5456   -775   2197   -755       C  
+ATOM   6420  N   TRP B 428     -41.591  21.463  45.093  1.00 83.12           N  
+ANISOU 6420  N   TRP B 428     9236  16947   5399   -874   1842  -2288       N  
+ATOM   6421  CA  TRP B 428     -40.586  22.449  45.460  1.00 96.40           C  
+ANISOU 6421  CA  TRP B 428    10751  18853   7022   -904   1680  -2616       C  
+ATOM   6422  C   TRP B 428     -40.138  22.257  46.900  1.00 95.06           C  
+ANISOU 6422  C   TRP B 428    10585  19136   6396   -943   1538  -2600       C  
+ATOM   6423  O   TRP B 428     -38.980  22.494  47.216  1.00 95.06           O  
+ANISOU 6423  O   TRP B 428    10473  19415   6229   -938   1338  -2682       O  
+ATOM   6424  CB  TRP B 428     -41.070  23.885  45.253  1.00 90.65           C  
+ANISOU 6424  CB  TRP B 428     9909  17935   6597   -982   1744  -3087       C  
+ATOM   6425  CG  TRP B 428     -39.956  24.854  45.527  1.00 90.98           C  
+ANISOU 6425  CG  TRP B 428     9792  18175   6599  -1044   1571  -3428       C  
+ATOM   6426  CD1 TRP B 428     -39.096  25.390  44.615  1.00 90.61           C  
+ANISOU 6426  CD1 TRP B 428     9627  18017   6783  -1050   1509  -3561       C  
+ATOM   6427  CD2 TRP B 428     -39.579  25.394  46.800  1.00 90.14           C  
+ANISOU 6427  CD2 TRP B 428     9625  18424   6200  -1132   1438  -3687       C  
+ATOM   6428  NE1 TRP B 428     -38.200  26.222  45.241  1.00 98.02           N  
+ANISOU 6428  NE1 TRP B 428    10431  19193   7621  -1153   1324  -3879       N  
+ATOM   6429  CE2 TRP B 428     -38.475  26.241  46.584  1.00 96.81           C  
+ANISOU 6429  CE2 TRP B 428    10312  19346   7124  -1203   1276  -3980       C  
+ATOM   6430  CE3 TRP B 428     -40.067  25.243  48.102  1.00 93.75           C  
+ANISOU 6430  CE3 TRP B 428    10144  19148   6327  -1171   1444  -3704       C  
+ATOM   6431  CZ2 TRP B 428     -37.858  26.941  47.618  1.00 94.75           C  
+ANISOU 6431  CZ2 TRP B 428     9958  19397   6643  -1316   1098  -4296       C  
+ATOM   6432  CZ3 TRP B 428     -39.450  25.930  49.127  1.00 97.72           C  
+ANISOU 6432  CZ3 TRP B 428    10564  19972   6595  -1262   1284  -4007       C  
+ATOM   6433  CH2 TRP B 428     -38.360  26.772  48.880  1.00107.84           C  
+ANISOU 6433  CH2 TRP B 428    11692  21302   7981  -1335   1104  -4303       C  
+ATOM   6434  N   ASN B 429     -41.043  21.840  47.779  1.00 91.19           N  
+ANISOU 6434  N   ASN B 429    10211  18742   5695   -990   1635  -2496       N  
+ATOM   6435  CA  ASN B 429     -40.637  21.568  49.152  1.00 95.67           C  
+ANISOU 6435  CA  ASN B 429    10805  19743   5801  -1026   1505  -2434       C  
+ATOM   6436  C   ASN B 429     -39.865  20.255  49.236  1.00 96.34           C  
+ANISOU 6436  C   ASN B 429    10998  19992   5615   -923   1371  -1942       C  
+ATOM   6437  O   ASN B 429     -38.889  20.135  49.998  1.00 99.42           O  
+ANISOU 6437  O   ASN B 429    11342  20750   5682   -898   1149  -1885       O  
+ATOM   6438  CB  ASN B 429     -41.853  21.525  50.079  1.00111.36           C  
+ANISOU 6438  CB  ASN B 429    12881  21804   7626  -1112   1673  -2468       C  
+ATOM   6439  CG  ASN B 429     -42.540  22.870  50.204  1.00108.78           C  
+ANISOU 6439  CG  ASN B 429    12435  21386   7509  -1178   1778  -2973       C  
+ATOM   6440  OD1 ASN B 429     -41.893  23.915  50.167  1.00111.95           O  
+ANISOU 6440  OD1 ASN B 429    12704  21817   8014  -1199   1664  -3341       O  
+ATOM   6441  ND2 ASN B 429     -43.857  22.850  50.371  1.00105.53           N  
+ANISOU 6441  ND2 ASN B 429    12067  20870   7161  -1211   1992  -2993       N  
+ATOM   6442  N   LYS B 430     -40.248  19.306  48.386  1.00 96.22           N  
+ANISOU 6442  N   LYS B 430    11117  19689   5753   -851   1485  -1594       N  
+ATOM   6443  CA  LYS B 430     -39.550  18.028  48.318  1.00 98.40           C  
+ANISOU 6443  CA  LYS B 430    11516  20048   5822   -719   1368  -1109       C  
+ATOM   6444  C   LYS B 430     -38.121  18.225  47.821  1.00110.10           C  
+ANISOU 6444  C   LYS B 430    12834  21671   7328   -582   1153  -1134       C  
+ATOM   6445  O   LYS B 430     -37.227  17.440  48.140  1.00117.07           O  
+ANISOU 6445  O   LYS B 430    13743  22791   7947   -445    960   -810       O  
+ATOM   6446  CB  LYS B 430     -40.297  17.050  47.407  1.00 91.48           C  
+ANISOU 6446  CB  LYS B 430    10824  18787   5147   -683   1549   -782       C  
+ATOM   6447  CG  LYS B 430     -39.622  15.692  47.257  1.00 93.72           C  
+ANISOU 6447  CG  LYS B 430    11268  19092   5248   -521   1440   -265       C  
+ATOM   6448  CD  LYS B 430     -40.381  14.792  46.298  1.00 94.96           C  
+ANISOU 6448  CD  LYS B 430    11616  18838   5625   -511   1624      9       C  
+ATOM   6449  CE  LYS B 430     -40.903  13.551  47.000  1.00108.69           C  
+ANISOU 6449  CE  LYS B 430    13622  20585   7092   -561   1658    456       C  
+ATOM   6450  NZ  LYS B 430     -39.820  12.554  47.228  1.00113.47           N  
+ANISOU 6450  NZ  LYS B 430    14343  21315   7457   -350   1441    895       N  
+ATOM   6451  N   VAL B 431     -37.903  19.293  47.062  1.00108.29           N  
+ANISOU 6451  N   VAL B 431    12424  21309   7414   -616   1177  -1514       N  
+ATOM   6452  CA  VAL B 431     -36.582  19.569  46.517  1.00 99.60           C  
+ANISOU 6452  CA  VAL B 431    11136  20185   6523   -507    968  -1539       C  
+ATOM   6453  C   VAL B 431     -35.787  20.467  47.464  1.00112.64           C  
+ANISOU 6453  C   VAL B 431    12592  22279   7928   -605    752  -1865       C  
+ATOM   6454  O   VAL B 431     -34.612  20.229  47.713  1.00123.78           O  
+ANISOU 6454  O   VAL B 431    13875  23911   9246   -509    495  -1726       O  
+ATOM   6455  CB  VAL B 431     -36.681  20.236  45.125  1.00 87.60           C  
+ANISOU 6455  CB  VAL B 431     9530  18188   5566   -509   1083  -1724       C  
+ATOM   6456  CG1 VAL B 431     -35.372  20.914  44.749  1.00 86.57           C  
+ANISOU 6456  CG1 VAL B 431     9150  18082   5660   -483    883  -1871       C  
+ATOM   6457  CG2 VAL B 431     -37.075  19.210  44.072  1.00 85.14           C  
+ANISOU 6457  CG2 VAL B 431     9388  17459   5502   -373   1214  -1359       C  
+ATOM   6458  N   ASN B 432     -36.447  21.483  48.008  1.00103.97           N  
+ANISOU 6458  N   ASN B 432    11467  21286   6752   -790    846  -2301       N  
+ATOM   6459  CA  ASN B 432     -35.823  22.431  48.927  1.00 99.39           C  
+ANISOU 6459  CA  ASN B 432    10727  21041   5996   -915    650  -2669       C  
+ATOM   6460  C   ASN B 432     -35.331  21.824  50.238  1.00107.97           C  
+ANISOU 6460  C   ASN B 432    11846  22576   6602   -891    438  -2454       C  
+ATOM   6461  O   ASN B 432     -34.283  22.226  50.744  1.00116.60           O  
+ANISOU 6461  O   ASN B 432    12764  24011   7528   -925    173  -2598       O  
+ATOM   6462  CB  ASN B 432     -36.776  23.587  49.234  1.00101.11           C  
+ANISOU 6462  CB  ASN B 432    10949  21082   6387  -1074    808  -3128       C  
+ATOM   6463  CG  ASN B 432     -36.173  24.597  50.197  1.00109.27           C  
+ANISOU 6463  CG  ASN B 432    11843  22420   7254  -1214    617  -3540       C  
+ATOM   6464  OD1 ASN B 432     -36.230  24.424  51.415  1.00112.55           O  
+ANISOU 6464  OD1 ASN B 432    12312  23145   7307  -1248    542  -3517       O  
+ATOM   6465  ND2 ASN B 432     -35.563  25.642  49.650  1.00110.35           N  
+ANISOU 6465  ND2 ASN B 432    11810  22466   7653  -1309    534  -3914       N  
+ATOM   6466  N   GLU B 433     -36.063  20.860  50.792  1.00105.51           N  
+ANISOU 6466  N   GLU B 433    11752  22265   6072   -846    540  -2103       N  
+ATOM   6467  CA  GLU B 433     -35.541  20.180  51.982  1.00108.96           C  
+ANISOU 6467  CA  GLU B 433    12243  23113   6046   -807    330  -1831       C  
+ATOM   6468  C   GLU B 433     -34.371  19.242  51.680  1.00112.79           C  
+ANISOU 6468  C   GLU B 433    12677  23763   6414   -598     83  -1409       C  
+ATOM   6469  O   GLU B 433     -33.341  19.301  52.352  1.00121.33           O  
+ANISOU 6469  O   GLU B 433    13617  25232   7251   -566   -214  -1396       O  
+ATOM   6470  CB  GLU B 433     -36.661  19.408  52.690  1.00115.90           C  
+ANISOU 6470  CB  GLU B 433    13379  23946   6711   -841    515  -1562       C  
+ATOM   6471  CG  GLU B 433     -37.577  20.222  53.629  1.00122.02           C  
+ANISOU 6471  CG  GLU B 433    14178  24807   7377  -1019    662  -1930       C  
+ATOM   6472  CD  GLU B 433     -38.175  21.503  53.047  1.00124.99           C  
+ANISOU 6472  CD  GLU B 433    14435  24910   8145  -1116    833  -2452       C  
+ATOM   6473  OE1 GLU B 433     -38.013  21.797  51.846  1.00126.66           O  
+ANISOU 6473  OE1 GLU B 433    14562  24823   8741  -1072    871  -2537       O  
+ATOM   6474  OE2 GLU B 433     -38.830  22.231  53.822  1.00128.28           O  
+ANISOU 6474  OE2 GLU B 433    14850  25414   8476  -1227    932  -2777       O  
+ATOM   6475  N   GLU B 434     -34.517  18.388  50.676  1.00111.23           N  
+ANISOU 6475  N   GLU B 434    12585  23276   6402   -442    193  -1068       N  
+ATOM   6476  CA  GLU B 434     -33.457  17.449  50.328  1.00115.00           C  
+ANISOU 6476  CA  GLU B 434    13023  23806   6867   -185    -28   -640       C  
+ATOM   6477  C   GLU B 434     -32.679  17.983  49.130  1.00110.46           C  
+ANISOU 6477  C   GLU B 434    12205  22909   6857   -105    -68   -806       C  
+ATOM   6478  O   GLU B 434     -32.504  17.283  48.135  1.00108.03           O  
+ANISOU 6478  O   GLU B 434    11942  22210   6895     88     -8   -523       O  
+ATOM   6479  CB  GLU B 434     -34.029  16.063  50.026  1.00114.60           C  
+ANISOU 6479  CB  GLU B 434    13266  23455   6824    -36    104   -109       C  
+ATOM   6480  N   PHE B 435     -32.209  19.223  49.238  1.00106.09           N  
+ANISOU 6480  N   PHE B 435    11402  22524   6382   -267   -164  -1268       N  
+ATOM   6481  CA  PHE B 435     -31.651  19.936  48.091  1.00105.38           C  
+ANISOU 6481  CA  PHE B 435    11091  22116   6834   -272   -146  -1479       C  
+ATOM   6482  C   PHE B 435     -30.259  19.460  47.696  1.00112.97           C  
+ANISOU 6482  C   PHE B 435    11822  23143   7957    -54   -385  -1220       C  
+ATOM   6483  O   PHE B 435     -29.812  19.700  46.574  1.00103.72           O  
+ANISOU 6483  O   PHE B 435    10501  21665   7243      0   -326  -1254       O  
+ATOM   6484  CB  PHE B 435     -31.626  21.441  48.382  1.00103.56           C  
+ANISOU 6484  CB  PHE B 435    10687  22015   6644   -545   -173  -2058       C  
+ATOM   6485  CG  PHE B 435     -31.167  22.277  47.222  1.00106.14           C  
+ANISOU 6485  CG  PHE B 435    10814  21992   7525   -604   -130  -2275       C  
+ATOM   6486  CD1 PHE B 435     -32.041  22.588  46.194  1.00102.48           C  
+ANISOU 6486  CD1 PHE B 435    10468  21026   7444   -639    153  -2363       C  
+ATOM   6487  CD2 PHE B 435     -29.870  22.761  47.160  1.00112.36           C  
+ANISOU 6487  CD2 PHE B 435    11285  22969   8439   -639   -375  -2378       C  
+ATOM   6488  CE1 PHE B 435     -31.632  23.356  45.122  1.00101.64           C  
+ANISOU 6488  CE1 PHE B 435    10199  20602   7819   -703    194  -2526       C  
+ATOM   6489  CE2 PHE B 435     -29.453  23.531  46.089  1.00113.20           C  
+ANISOU 6489  CE2 PHE B 435    11209  22759   9042   -724   -317  -2549       C  
+ATOM   6490  CZ  PHE B 435     -30.336  23.829  45.070  1.00107.20           C  
+ANISOU 6490  CZ  PHE B 435    10600  21489   8642   -754    -29  -2613       C  
+ATOM   6491  N   GLU B 436     -29.575  18.773  48.604  1.00125.09           N  
+ANISOU 6491  N   GLU B 436    13320  25096   9113     83   -652   -950       N  
+ATOM   6492  CA  GLU B 436     -28.250  18.260  48.289  1.00125.26           C  
+ANISOU 6492  CA  GLU B 436    13094  25218   9282    333   -891   -689       C  
+ATOM   6493  C   GLU B 436     -28.390  17.036  47.391  1.00129.11           C  
+ANISOU 6493  C   GLU B 436    13764  25274  10017    638   -749   -244       C  
+ATOM   6494  O   GLU B 436     -27.439  16.622  46.728  1.00131.65           O  
+ANISOU 6494  O   GLU B 436    13894  25518  10608    881   -842    -61       O  
+ATOM   6495  CB  GLU B 436     -27.482  17.910  49.564  1.00124.79           C  
+ANISOU 6495  CB  GLU B 436    12930  25753   8734    406  -1253   -527       C  
+ATOM   6496  N   THR B 437     -29.592  16.467  47.376  1.00122.06           N  
+ANISOU 6496  N   THR B 437    13236  24110   9032    617   -518    -92       N  
+ATOM   6497  CA  THR B 437     -29.873  15.261  46.606  1.00115.15           C  
+ANISOU 6497  CA  THR B 437    12597  22799   8358    868   -381    312       C  
+ATOM   6498  C   THR B 437     -30.297  15.558  45.169  1.00111.96           C  
+ANISOU 6498  C   THR B 437    12213  21870   8457    841   -106    154       C  
+ATOM   6499  O   THR B 437     -30.417  14.643  44.355  1.00116.18           O  
+ANISOU 6499  O   THR B 437    12913  22018   9213   1049      5    427       O  
+ATOM   6500  CB  THR B 437     -30.974  14.418  47.276  1.00113.77           C  
+ANISOU 6500  CB  THR B 437    12811  22576   7841    829   -271    590       C  
+ATOM   6501  N   TYR B 438     -30.526  16.830  44.856  1.00111.49           N  
+ANISOU 6501  N   TYR B 438    12002  21787   8571    586     -5   -285       N  
+ATOM   6502  CA  TYR B 438     -31.012  17.195  43.529  1.00103.41           C  
+ANISOU 6502  CA  TYR B 438    11014  20288   7989    536    248   -429       C  
+ATOM   6503  C   TYR B 438     -30.054  18.123  42.787  1.00104.06           C  
+ANISOU 6503  C   TYR B 438    10758  20371   8410    495    199   -673       C  
+ATOM   6504  O   TYR B 438     -29.868  17.991  41.577  1.00 98.87           O  
+ANISOU 6504  O   TYR B 438    10073  19382   8109    600    329   -617       O  
+ATOM   6505  CB  TYR B 438     -32.390  17.855  43.629  1.00 96.24           C  
+ANISOU 6505  CB  TYR B 438    10281  19238   7047    268    468   -698       C  
+ATOM   6506  CG  TYR B 438     -33.471  16.955  44.185  1.00 94.32           C  
+ANISOU 6506  CG  TYR B 438    10362  18954   6521    266    580   -456       C  
+ATOM   6507  CD1 TYR B 438     -33.945  15.872  43.456  1.00 87.00           C  
+ANISOU 6507  CD1 TYR B 438     9676  17637   5742    412    715   -134       C  
+ATOM   6508  CD2 TYR B 438     -34.024  17.194  45.436  1.00100.89           C  
+ANISOU 6508  CD2 TYR B 438    11261  20144   6928     98    558   -560       C  
+ATOM   6509  CE1 TYR B 438     -34.935  15.048  43.961  1.00 93.22           C  
+ANISOU 6509  CE1 TYR B 438    10755  18377   6288    368    819    100       C  
+ATOM   6510  CE2 TYR B 438     -35.014  16.376  45.949  1.00 95.75           C  
+ANISOU 6510  CE2 TYR B 438    10891  19482   6008     65    681   -318       C  
+ATOM   6511  CZ  TYR B 438     -35.465  15.306  45.208  1.00 93.25           C  
+ANISOU 6511  CZ  TYR B 438    10801  18759   5870    188    808     22       C  
+ATOM   6512  OH  TYR B 438     -36.451  14.490  45.716  1.00 94.00           O  
+ANISOU 6512  OH  TYR B 438    11170  18833   5714    114    932    275       O  
+ATOM   6513  N   TYR B 439     -29.446  19.056  43.511  1.00115.49           N  
+ANISOU 6513  N   TYR B 439    11950  22198   9733    324     13   -946       N  
+ATOM   6514  CA  TYR B 439     -28.501  19.987  42.901  1.00111.83           C  
+ANISOU 6514  CA  TYR B 439    11146  21762   9582    231    -47  -1175       C  
+ATOM   6515  C   TYR B 439     -27.257  20.182  43.763  1.00119.63           C  
+ANISOU 6515  C   TYR B 439    11806  23272  10377    234   -374  -1208       C  
+ATOM   6516  O   TYR B 439     -27.150  21.175  44.483  1.00116.31           O  
+ANISOU 6516  O   TYR B 439    11254  23115   9823    -29   -499  -1547       O  
+ATOM   6517  CB  TYR B 439     -29.168  21.345  42.652  1.00104.99           C  
+ANISOU 6517  CB  TYR B 439    10284  20712   8896    -93     94  -1605       C  
+ATOM   6518  CG  TYR B 439     -30.340  21.307  41.695  1.00 98.07           C  
+ANISOU 6518  CG  TYR B 439     9671  19337   8256   -106    393  -1599       C  
+ATOM   6519  CD1 TYR B 439     -30.168  21.572  40.343  1.00101.06           C  
+ANISOU 6519  CD1 TYR B 439     9988  19363   9045    -92    538  -1595       C  
+ATOM   6520  CD2 TYR B 439     -31.620  21.007  42.146  1.00 91.69           C  
+ANISOU 6520  CD2 TYR B 439     9158  18439   7242   -144    528  -1592       C  
+ATOM   6521  CE1 TYR B 439     -31.237  21.539  39.466  1.00102.60           C  
+ANISOU 6521  CE1 TYR B 439    10418  19130   9435   -106    781  -1585       C  
+ATOM   6522  CE2 TYR B 439     -32.695  20.973  41.276  1.00 88.21           C  
+ANISOU 6522  CE2 TYR B 439     8924  17571   7020   -162    777  -1588       C  
+ATOM   6523  CZ  TYR B 439     -32.497  21.239  39.937  1.00 98.78           C  
+ANISOU 6523  CZ  TYR B 439    10206  18565   8762   -139    889  -1586       C  
+ATOM   6524  OH  TYR B 439     -33.563  21.206  39.067  1.00 89.76           O  
+ANISOU 6524  OH  TYR B 439     9265  17024   7817   -158   1107  -1578       O  
+ATOM   6525  N   PRO B 440     -26.310  19.233  43.693  1.00128.99           N  
+ANISOU 6525  N   PRO B 440    12851  24608  11552    539   -523   -868       N  
+ATOM   6526  CA  PRO B 440     -25.055  19.369  44.440  1.00128.85           C  
+ANISOU 6526  CA  PRO B 440    12469  25111  11375    570   -859   -872       C  
+ATOM   6527  C   PRO B 440     -24.202  20.527  43.927  1.00129.07           C  
+ANISOU 6527  C   PRO B 440    12100  25223  11719    346   -904  -1186       C  
+ATOM   6528  O   PRO B 440     -23.373  20.339  43.036  1.00127.67           O  
+ANISOU 6528  O   PRO B 440    11674  24981  11853    497   -872  -1063       O  
+ATOM   6529  CB  PRO B 440     -24.354  18.028  44.197  1.00124.87           C  
+ANISOU 6529  CB  PRO B 440    11923  24628  10893   1005   -948   -414       C  
+ATOM   6530  CG  PRO B 440     -25.454  17.082  43.842  1.00129.54           C  
+ANISOU 6530  CG  PRO B 440    12967  24783  11468   1160   -712   -164       C  
+ATOM   6531  CD  PRO B 440     -26.435  17.907  43.066  1.00129.01           C  
+ANISOU 6531  CD  PRO B 440    13054  24323  11642    888   -412   -459       C  
+ATOM   6532  N   GLY B 441     -24.408  21.711  44.495  1.00131.56           N  
+ANISOU 6532  N   GLY B 441    12361  25675  11952    -17   -968  -1592       N  
+ATOM   6533  CA  GLY B 441     -23.687  22.901  44.082  1.00130.82           C  
+ANISOU 6533  CA  GLY B 441    11927  25621  12158   -297  -1013  -1910       C  
+ATOM   6534  C   GLY B 441     -24.479  24.153  44.402  1.00135.61           C  
+ANISOU 6534  C   GLY B 441    12674  26090  12762   -679   -942  -2367       C  
+ATOM   6535  O   GLY B 441     -25.621  24.072  44.852  1.00143.26           O  
+ANISOU 6535  O   GLY B 441    13987  26933  13512   -700   -822  -2435       O  
+ATOM   6536  N   ALA B 442     -23.879  25.314  44.163  1.00132.11           N  
+ANISOU 6536  N   ALA B 442    11960  25660  12574   -982  -1006  -2682       N  
+ATOM   6537  CA  ALA B 442     -24.532  26.582  44.464  1.00129.08           C  
+ANISOU 6537  CA  ALA B 442    11698  25114  12232  -1340   -961  -3149       C  
+ATOM   6538  C   ALA B 442     -24.301  27.601  43.353  1.00126.76           C  
+ANISOU 6538  C   ALA B 442    11269  24442  12451  -1577   -818  -3321       C  
+ATOM   6539  O   ALA B 442     -24.651  28.773  43.491  1.00125.38           O  
+ANISOU 6539  O   ALA B 442    11149  24088  12399  -1890   -804  -3716       O  
+ATOM   6540  CB  ALA B 442     -24.041  27.128  45.795  1.00127.37           C  
+ANISOU 6540  CB  ALA B 442    11327  25395  11674  -1554  -1286  -3457       C  
+HETATM 6541  N   MSE B 446     -27.476  29.840  41.870  1.00122.93           N  
+ANISOU 6541  N   MSE B 446    11565  22500  12641  -1960   -142  -3943       N  
+HETATM 6542  CA  MSE B 446     -28.403  28.720  41.749  1.00121.81           C  
+ANISOU 6542  CA  MSE B 446    11691  22278  12314  -1653     32  -3652       C  
+HETATM 6543  C   MSE B 446     -29.374  28.649  42.920  1.00124.21           C  
+ANISOU 6543  C   MSE B 446    12223  22743  12229  -1639     25  -3855       C  
+HETATM 6544  O   MSE B 446     -30.590  28.628  42.729  1.00115.97           O  
+ANISOU 6544  O   MSE B 446    11440  21417  11208  -1577    236  -3888       O  
+HETATM 6545  CB  MSE B 446     -27.639  27.400  41.638  1.00123.21           C  
+ANISOU 6545  CB  MSE B 446    11742  22735  12338  -1374    -39  -3217       C  
+HETATM 6546  CG  MSE B 446     -27.642  26.805  40.246  1.00115.86           C  
+ANISOU 6546  CG  MSE B 446    10847  21474  11701  -1186    171  -2880       C  
+HETATM 6547 SE   MSE B 446     -26.821  25.039  40.157  1.00145.60          SE  
+ANISOU 6547 SE   MSE B 446    14515  25532  15276   -764    102  -2360      SE  
+HETATM 6548  CE  MSE B 446     -24.956  25.565  40.365  1.00135.08           C  
+ANISOU 6548  CE  MSE B 446    12623  24661  14040   -903   -181  -2433       C  
+ATOM   6549  N   LYS B 447     -28.826  28.607  44.131  1.00123.79           N  
+ANISOU 6549  N   LYS B 447    12054  23178  11804  -1699   -218  -3987       N  
+ATOM   6550  CA  LYS B 447     -29.626  28.451  45.341  1.00110.22           C  
+ANISOU 6550  CA  LYS B 447    10533  21715   9631  -1685   -232  -4155       C  
+ATOM   6551  C   LYS B 447     -30.625  29.588  45.526  1.00106.98           C  
+ANISOU 6551  C   LYS B 447    10288  21036   9324  -1869    -95  -4628       C  
+ATOM   6552  O   LYS B 447     -31.741  29.371  45.997  1.00108.64           O  
+ANISOU 6552  O   LYS B 447    10727  21247   9304  -1792     60  -4695       O  
+ATOM   6553  CB  LYS B 447     -28.718  28.353  46.568  1.00109.26           C  
+ANISOU 6553  CB  LYS B 447    10231  22193   9092  -1753   -554  -4244       C  
+ATOM   6554  N   LYS B 448     -30.221  30.799  45.156  1.00109.33           N  
+ANISOU 6554  N   LYS B 448    10463  21098   9978  -2111   -148  -4950       N  
+ATOM   6555  CA  LYS B 448     -31.104  31.956  45.255  1.00111.89           C  
+ANISOU 6555  CA  LYS B 448    10943  21098  10471  -2264    -31  -5412       C  
+ATOM   6556  C   LYS B 448     -32.263  31.870  44.265  1.00110.56           C  
+ANISOU 6556  C   LYS B 448    10983  20427  10598  -2114    270  -5267       C  
+ATOM   6557  O   LYS B 448     -33.404  32.175  44.608  1.00118.31           O  
+ANISOU 6557  O   LYS B 448    12153  21288  11513  -2078    423  -5506       O  
+ATOM   6558  CB  LYS B 448     -30.317  33.248  45.027  1.00105.00           C  
+ANISOU 6558  CB  LYS B 448     9902  20038   9955  -2572   -177  -5751       C  
+ATOM   6559  N   LEU B 449     -31.962  31.453  43.039  1.00110.45           N  
+ANISOU 6559  N   LEU B 449    10919  20150  10898  -2024    351  -4886       N  
+ATOM   6560  CA  LEU B 449     -32.969  31.342  41.988  1.00105.87           C  
+ANISOU 6560  CA  LEU B 449    10519  19106  10601  -1892    604  -4718       C  
+ATOM   6561  C   LEU B 449     -33.996  30.253  42.293  1.00109.43           C  
+ANISOU 6561  C   LEU B 449    11161  19675  10742  -1661    757  -4506       C  
+ATOM   6562  O   LEU B 449     -35.202  30.440  42.090  1.00105.97           O  
+ANISOU 6562  O   LEU B 449    10891  18981  10392  -1603    945  -4599       O  
+ATOM   6563  CB  LEU B 449     -32.299  31.067  40.641  1.00100.27           C  
+ANISOU 6563  CB  LEU B 449     9709  18160  10230  -1854    644  -4353       C  
+ATOM   6564  N   PHE B 450     -33.505  29.117  42.784  1.00106.80           N  
+ANISOU 6564  N   PHE B 450    10790  19730  10059  -1534    667  -4211       N  
+ATOM   6565  CA  PHE B 450     -34.363  27.996  43.149  1.00 95.99           C  
+ANISOU 6565  CA  PHE B 450     9604  18494   8372  -1348    790  -3966       C  
+ATOM   6566  C   PHE B 450     -35.357  28.406  44.225  1.00 94.82           C  
+ANISOU 6566  C   PHE B 450     9577  18514   7937  -1411    863  -4312       C  
+ATOM   6567  O   PHE B 450     -36.537  28.061  44.154  1.00 95.01           O  
+ANISOU 6567  O   PHE B 450     9762  18418   7917  -1325   1070  -4258       O  
+ATOM   6568  CB  PHE B 450     -33.524  26.811  43.631  1.00 90.51           C  
+ANISOU 6568  CB  PHE B 450     8849  18197   7345  -1214    634  -3608       C  
+ATOM   6569  N   GLY B 451     -34.876  29.145  45.219  1.00 96.86           N  
+ANISOU 6569  N   GLY B 451     9741  19068   7994  -1570    696  -4684       N  
+ATOM   6570  CA  GLY B 451     -35.751  29.677  46.246  1.00100.46           C  
+ANISOU 6570  CA  GLY B 451    10299  19696   8177  -1637    773  -5090       C  
+ATOM   6571  C   GLY B 451     -36.663  30.753  45.686  1.00102.78           C  
+ANISOU 6571  C   GLY B 451    10658  19523   8872  -1680    952  -5431       C  
+ATOM   6572  O   GLY B 451     -37.769  30.964  46.181  1.00112.09           O  
+ANISOU 6572  O   GLY B 451    11945  20700   9944  -1640   1118  -5638       O  
+ATOM   6573  N   GLU B 452     -36.202  31.422  44.632  1.00 93.10           N  
+ANISOU 6573  N   GLU B 452     9357  17873   8142  -1746    916  -5436       N  
+ATOM   6574  CA  GLU B 452     -36.967  32.499  44.018  1.00 91.84           C  
+ANISOU 6574  CA  GLU B 452     9263  17223   8410  -1778   1048  -5722       C  
+ATOM   6575  C   GLU B 452     -38.063  31.954  43.114  1.00106.03           C  
+ANISOU 6575  C   GLU B 452    11178  18719  10390  -1594   1281  -5434       C  
+ATOM   6576  O   GLU B 452     -38.894  32.708  42.607  1.00107.54           O  
+ANISOU 6576  O   GLU B 452    11430  18523  10907  -1568   1404  -5622       O  
+ATOM   6577  CB  GLU B 452     -36.046  33.429  43.226  1.00 92.15           C  
+ANISOU 6577  CB  GLU B 452     9193  16920   8900  -1947    916  -5797       C  
+ATOM   6578  N   LEU B 453     -38.022  30.643  42.888  1.00 95.50           N  
+ANISOU 6578  N   LEU B 453     9874  17550   8863  -1466   1319  -4974       N  
+ATOM   6579  CA  LEU B 453     -39.036  29.952  42.103  1.00 90.31           C  
+ANISOU 6579  CA  LEU B 453     9330  16663   8320  -1313   1518  -4681       C  
+ATOM   6580  C   LEU B 453     -40.284  29.667  42.931  1.00 89.25           C  
+ANISOU 6580  C   LEU B 453     9284  16736   7889  -1252   1689  -4810       C  
+ATOM   6581  O   LEU B 453     -41.349  29.381  42.380  1.00 84.47           O  
+ANISOU 6581  O   LEU B 453     8750  15922   7423  -1157   1864  -4685       O  
+ATOM   6582  CB  LEU B 453     -38.476  28.649  41.534  1.00 89.77           C  
+ANISOU 6582  CB  LEU B 453     9276  16656   8176  -1209   1489  -4161       C  
+ATOM   6583  N   ASN B 454     -40.145  29.730  44.253  1.00 89.91           N  
+ANISOU 6583  N   ASN B 454     9354  17204   7602  -1310   1613  -4998       N  
+ATOM   6584  CA  ASN B 454     -41.257  29.447  45.153  1.00 93.61           C  
+ANISOU 6584  CA  ASN B 454     9900  17770   7897  -1254   1713  -4953       C  
+ATOM   6585  C   ASN B 454     -41.883  30.684  45.775  1.00 91.36           C  
+ANISOU 6585  C   ASN B 454     9592  17386   7733  -1288   1750  -5417       C  
+ATOM   6586  O   ASN B 454     -42.833  30.574  46.551  1.00 93.28           O  
+ANISOU 6586  O   ASN B 454     9875  17734   7832  -1242   1852  -5433       O  
+ATOM   6587  CB  ASN B 454     -40.804  28.511  46.271  1.00 93.39           C  
+ANISOU 6587  CB  ASN B 454     9901  18210   7374  -1267   1612  -4729       C  
+ATOM   6588  N   LEU B 458     -43.251  36.417  42.961  1.00113.08           N  
+ANISOU 6588  N   LEU B 458    12324  18090  12550  -1246   1869  -6969       N  
+ATOM   6589  CA  LEU B 458     -42.800  37.465  42.054  1.00116.51           C  
+ANISOU 6589  CA  LEU B 458    12789  18032  13449  -1327   1798  -7190       C  
+ATOM   6590  C   LEU B 458     -43.775  37.683  40.904  1.00111.29           C  
+ANISOU 6590  C   LEU B 458    12161  16919  13204  -1151   1920  -7053       C  
+ATOM   6591  O   LEU B 458     -44.847  37.077  40.854  1.00102.42           O  
+ANISOU 6591  O   LEU B 458    11018  15896  12000   -972   2065  -6862       O  
+ATOM   6592  CB  LEU B 458     -41.413  37.121  41.497  1.00109.26           C  
+ANISOU 6592  CB  LEU B 458    11833  17130  12549  -1518   1626  -6882       C  
+ATOM   6593  N   SER B 459     -43.342  38.487  39.940  1.00102.43           N  
+ANISOU 6593  N   SER B 459    11084  15285  12550  -1221   1809  -6982       N  
+ATOM   6594  CA  SER B 459     -44.148  38.838  38.781  1.00 93.24           C  
+ANISOU 6594  CA  SER B 459     9965  13641  11820  -1065   1865  -6798       C  
+ATOM   6595  C   SER B 459     -44.012  37.773  37.702  1.00105.02           C  
+ANISOU 6595  C   SER B 459    11452  15164  13286  -1047   1881  -6199       C  
+ATOM   6596  O   SER B 459     -43.340  36.764  37.910  1.00112.22           O  
+ANISOU 6596  O   SER B 459    12327  16452  13859  -1130   1863  -5953       O  
+ATOM   6597  CB  SER B 459     -43.735  40.205  38.239  1.00 95.27           C  
+ANISOU 6597  CB  SER B 459    10301  13318  12578  -1162   1735  -6968       C  
+ATOM   6598  OG  SER B 459     -42.703  40.073  37.273  1.00107.83           O  
+ANISOU 6598  OG  SER B 459    11904  14747  14319  -1344   1620  -6562       O  
+ATOM   6599  N   ILE B 460     -44.650  37.995  36.556  1.00109.07           N  
+ANISOU 6599  N   ILE B 460    12009  15281  14152   -927   1905  -5974       N  
+ATOM   6600  CA  ILE B 460     -44.607  37.035  35.455  1.00103.71           C  
+ANISOU 6600  CA  ILE B 460    11346  14605  13454   -903   1922  -5441       C  
+ATOM   6601  C   ILE B 460     -43.263  37.074  34.732  1.00105.10           C  
+ANISOU 6601  C   ILE B 460    11547  14658  13727  -1102   1799  -5168       C  
+ATOM   6602  O   ILE B 460     -42.633  36.032  34.522  1.00104.83           O  
+ANISOU 6602  O   ILE B 460    11487  14898  13446  -1151   1801  -4851       O  
+ATOM   6603  CB  ILE B 460     -45.733  37.305  34.427  1.00 99.71           C  
+ANISOU 6603  CB  ILE B 460    10875  13734  13277   -717   1964  -5292       C  
+ATOM   6604  CG1 ILE B 460     -47.080  36.797  34.945  1.00 95.45           C  
+ANISOU 6604  CG1 ILE B 460    10257  13438  12574   -519   2114  -5409       C  
+ATOM   6605  CG2 ILE B 460     -45.413  36.660  33.084  1.00 87.01           C  
+ANISOU 6605  CG2 ILE B 460     9321  12009  11729   -748   1930  -4774       C  
+ATOM   6606  CD1 ILE B 460     -48.180  36.794  33.897  1.00 87.47           C  
+ANISOU 6606  CD1 ILE B 460     9239  12168  11827   -340   2139  -5195       C  
+ATOM   6607  N   GLU B 461     -42.831  38.272  34.349  1.00110.67           N  
+ANISOU 6607  N   GLU B 461    12298  14948  14802  -1214   1699  -5289       N  
+ATOM   6608  CA  GLU B 461     -41.533  38.452  33.708  1.00106.75           C  
+ANISOU 6608  CA  GLU B 461    11797  14343  14421  -1440   1597  -5060       C  
+ATOM   6609  C   GLU B 461     -40.421  37.934  34.616  1.00106.41           C  
+ANISOU 6609  C   GLU B 461    11642  14754  14036  -1602   1539  -5140       C  
+ATOM   6610  O   GLU B 461     -39.480  37.278  34.159  1.00106.94           O  
+ANISOU 6610  O   GLU B 461    11645  14996  13991  -1697   1513  -4820       O  
+ATOM   6611  CB  GLU B 461     -41.301  39.924  33.366  1.00106.35           C  
+ANISOU 6611  CB  GLU B 461    11820  13765  14823  -1570   1498  -5235       C  
+ATOM   6612  N   GLU B 462     -40.549  38.226  35.907  1.00106.83           N  
+ANISOU 6612  N   GLU B 462    11664  15017  13912  -1616   1519  -5574       N  
+ATOM   6613  CA  GLU B 462     -39.540  37.855  36.892  1.00110.56           C  
+ANISOU 6613  CA  GLU B 462    12028  15937  14045  -1770   1430  -5698       C  
+ATOM   6614  C   GLU B 462     -39.478  36.342  37.080  1.00106.16           C  
+ANISOU 6614  C   GLU B 462    11418  15857  13061  -1659   1492  -5380       C  
+ATOM   6615  O   GLU B 462     -38.394  35.764  37.149  1.00102.44           O  
+ANISOU 6615  O   GLU B 462    10848  15664  12410  -1760   1409  -5190       O  
+ATOM   6616  CB  GLU B 462     -39.825  38.540  38.231  1.00104.54           C  
+ANISOU 6616  CB  GLU B 462    11271  15293  13156  -1798   1398  -6263       C  
+ATOM   6617  N   LEU B 463     -40.643  35.707  37.166  1.00 94.24           N  
+ANISOU 6617  N   LEU B 463     9966  14434  11406  -1450   1634  -5321       N  
+ATOM   6618  CA  LEU B 463     -40.710  34.259  37.336  1.00 91.62           C  
+ANISOU 6618  CA  LEU B 463     9621  14495  10695  -1349   1700  -5011       C  
+ATOM   6619  C   LEU B 463     -40.174  33.538  36.101  1.00101.89           C  
+ANISOU 6619  C   LEU B 463    10930  15689  12093  -1334   1699  -4529       C  
+ATOM   6620  O   LEU B 463     -39.406  32.579  36.214  1.00106.28           O  
+ANISOU 6620  O   LEU B 463    11438  16545  12400  -1337   1664  -4288       O  
+ATOM   6621  CB  LEU B 463     -42.146  33.816  37.626  1.00 91.37           C  
+ANISOU 6621  CB  LEU B 463     9641  14541  10533  -1167   1863  -5055       C  
+ATOM   6622  CG  LEU B 463     -42.331  32.362  38.061  1.00 88.02           C  
+ANISOU 6622  CG  LEU B 463     9225  14532   9686  -1093   1937  -4791       C  
+ATOM   6623  CD1 LEU B 463     -41.497  32.063  39.298  1.00 85.14           C  
+ANISOU 6623  CD1 LEU B 463     8806  14621   8923  -1186   1846  -4915       C  
+ATOM   6624  CD2 LEU B 463     -43.801  32.057  38.314  1.00 75.12           C  
+ANISOU 6624  CD2 LEU B 463     7617  12956   7969   -958   2110  -4852       C  
+ATOM   6625  N   ILE B 464     -40.579  34.010  34.925  1.00 97.85           N  
+ANISOU 6625  N   ILE B 464    10484  14755  11938  -1302   1734  -4393       N  
+ATOM   6626  CA  ILE B 464     -40.115  33.434  33.668  1.00 88.07           C  
+ANISOU 6626  CA  ILE B 464     9269  13401  10793  -1292   1747  -3967       C  
+ATOM   6627  C   ILE B 464     -38.597  33.551  33.534  1.00 90.21           C  
+ANISOU 6627  C   ILE B 464     9428  13769  11079  -1463   1645  -3876       C  
+ATOM   6628  O   ILE B 464     -37.916  32.577  33.191  1.00 91.73           O  
+ANISOU 6628  O   ILE B 464     9577  14169  11107  -1427   1655  -3579       O  
+ATOM   6629  CB  ILE B 464     -40.798  34.114  32.460  1.00 83.33           C  
+ANISOU 6629  CB  ILE B 464     8764  12331  10566  -1252   1779  -3864       C  
+ATOM   6630  CG1 ILE B 464     -42.248  33.646  32.333  1.00 77.96           C  
+ANISOU 6630  CG1 ILE B 464     8156  11618   9846  -1058   1881  -3830       C  
+ATOM   6631  CG2 ILE B 464     -40.059  33.808  31.176  1.00 85.36           C  
+ANISOU 6631  CG2 ILE B 464     9039  12469  10924  -1300   1778  -3479       C  
+ATOM   6632  CD1 ILE B 464     -43.058  34.440  31.332  1.00 84.42           C  
+ANISOU 6632  CD1 ILE B 464     9050  11998  11029   -992   1880  -3786       C  
+ATOM   6633  N   ASN B 465     -38.069  34.737  33.823  1.00 97.04           N  
+ANISOU 6633  N   ASN B 465    10236  14484  12150  -1649   1548  -4143       N  
+ATOM   6634  CA  ASN B 465     -36.625  34.951  33.796  1.00104.05           C  
+ANISOU 6634  CA  ASN B 465    10974  15492  13068  -1854   1441  -4096       C  
+ATOM   6635  C   ASN B 465     -35.894  34.075  34.809  1.00102.30           C  
+ANISOU 6635  C   ASN B 465    10619  15796  12455  -1843   1370  -4112       C  
+ATOM   6636  O   ASN B 465     -34.809  33.565  34.530  1.00104.22           O  
+ANISOU 6636  O   ASN B 465    10723  16246  12631  -1889   1326  -3885       O  
+ATOM   6637  CB  ASN B 465     -36.295  36.424  34.041  1.00106.22           C  
+ANISOU 6637  CB  ASN B 465    11227  15490  13642  -2088   1336  -4427       C  
+ATOM   6638  CG  ASN B 465     -36.573  37.291  32.829  1.00109.83           C  
+ANISOU 6638  CG  ASN B 465    11793  15416  14523  -2146   1373  -4292       C  
+ATOM   6639  OD1 ASN B 465     -36.574  36.810  31.695  1.00107.86           O  
+ANISOU 6639  OD1 ASN B 465    11580  15075  14325  -2078   1454  -3910       O  
+ATOM   6640  ND2 ASN B 465     -36.806  38.577  33.061  1.00113.40           N  
+ANISOU 6640  ND2 ASN B 465    12310  15506  15269  -2268   1306  -4606       N  
+ATOM   6641  N   THR B 466     -36.494  33.911  35.984  1.00 93.82           N  
+ANISOU 6641  N   THR B 466     9578  14951  11116  -1773   1360  -4372       N  
+ATOM   6642  CA  THR B 466     -35.946  33.039  37.018  1.00 92.35           C  
+ANISOU 6642  CA  THR B 466     9299  15277  10515  -1741   1284  -4363       C  
+ATOM   6643  C   THR B 466     -35.805  31.606  36.512  1.00 94.42           C  
+ANISOU 6643  C   THR B 466     9574  15712  10591  -1557   1352  -3921       C  
+ATOM   6644  O   THR B 466     -34.714  31.022  36.548  1.00100.11           O  
+ANISOU 6644  O   THR B 466    10155  16697  11187  -1561   1266  -3734       O  
+ATOM   6645  CB  THR B 466     -36.833  33.042  38.280  1.00 88.63           C  
+ANISOU 6645  CB  THR B 466     8902  15017   9757  -1680   1306  -4682       C  
+ATOM   6646  OG1 THR B 466     -36.976  34.382  38.768  1.00 90.74           O  
+ANISOU 6646  OG1 THR B 466     9172  15104  10199  -1829   1248  -5142       O  
+ATOM   6647  CG2 THR B 466     -36.228  32.167  39.367  1.00 88.35           C  
+ANISOU 6647  CG2 THR B 466     8784  15525   9261  -1660   1207  -4641       C  
+ATOM   6648  N   ILE B 467     -36.915  31.063  36.018  1.00 89.65           N  
+ANISOU 6648  N   ILE B 467     9130  14943   9990  -1391   1500  -3765       N  
+ATOM   6649  CA  ILE B 467     -36.956  29.697  35.510  1.00 79.12           C  
+ANISOU 6649  CA  ILE B 467     7858  13705   8500  -1217   1574  -3376       C  
+ATOM   6650  C   ILE B 467     -35.935  29.494  34.401  1.00 81.82           C  
+ANISOU 6650  C   ILE B 467     8118  13955   9013  -1225   1564  -3097       C  
+ATOM   6651  O   ILE B 467     -35.076  28.608  34.473  1.00 90.65           O  
+ANISOU 6651  O   ILE B 467     9152  15330   9959  -1146   1521  -2887       O  
+ATOM   6652  CB  ILE B 467     -38.352  29.348  34.955  1.00 80.30           C  
+ANISOU 6652  CB  ILE B 467     8183  13618   8707  -1091   1726  -3281       C  
+ATOM   6653  CG1 ILE B 467     -39.399  29.360  36.068  1.00 87.70           C  
+ANISOU 6653  CG1 ILE B 467     9173  14714   9435  -1063   1774  -3522       C  
+ATOM   6654  CG2 ILE B 467     -38.327  28.003  34.241  1.00 72.31           C  
+ANISOU 6654  CG2 ILE B 467     7256  12626   7591   -941   1793  -2890       C  
+ATOM   6655  CD1 ILE B 467     -40.818  29.269  35.554  1.00 87.08           C  
+ANISOU 6655  CD1 ILE B 467     9211  14405   9472   -970   1914  -3492       C  
+ATOM   6656  N   ILE B 468     -36.044  30.331  33.375  1.00 89.76           N  
+ANISOU 6656  N   ILE B 468     9149  14599  10356  -1311   1609  -3093       N  
+ATOM   6657  CA  ILE B 468     -35.186  30.239  32.203  1.00 90.96           C  
+ANISOU 6657  CA  ILE B 468     9235  14651  10674  -1336   1638  -2830       C  
+ATOM   6658  C   ILE B 468     -33.702  30.386  32.531  1.00 96.23           C  
+ANISOU 6658  C   ILE B 468     9656  15590  11318  -1461   1526  -2840       C  
+ATOM   6659  O   ILE B 468     -32.887  29.629  32.016  1.00101.84           O  
+ANISOU 6659  O   ILE B 468    10269  16454  11970  -1375   1552  -2586       O  
+ATOM   6660  CB  ILE B 468     -35.601  31.270  31.145  1.00 85.29           C  
+ANISOU 6660  CB  ILE B 468     8599  13501  10308  -1441   1692  -2831       C  
+ATOM   6661  CG1 ILE B 468     -36.884  30.789  30.470  1.00 85.95           C  
+ANISOU 6661  CG1 ILE B 468     8890  13368  10398  -1273   1803  -2694       C  
+ATOM   6662  CG2 ILE B 468     -34.519  31.435  30.092  1.00 87.08           C  
+ANISOU 6662  CG2 ILE B 468     8716  13677  10693  -1542   1717  -2607       C  
+ATOM   6663  CD1 ILE B 468     -37.578  31.828  29.655  1.00 97.08           C  
+ANISOU 6663  CD1 ILE B 468    10401  14362  12122  -1337   1825  -2727       C  
+ATOM   6664  N   GLU B 469     -33.341  31.339  33.386  1.00101.65           N  
+ANISOU 6664  N   GLU B 469    10226  16346  12048  -1658   1398  -3147       N  
+ATOM   6665  CA  GLU B 469     -31.927  31.525  33.703  1.00100.12           C  
+ANISOU 6665  CA  GLU B 469     9765  16432  11845  -1809   1268  -3169       C  
+ATOM   6666  C   GLU B 469     -31.418  30.374  34.570  1.00104.92           C  
+ANISOU 6666  C   GLU B 469    10269  17509  12088  -1643   1182  -3076       C  
+ATOM   6667  O   GLU B 469     -30.250  29.994  34.486  1.00110.27           O  
+ANISOU 6667  O   GLU B 469    10717  18451  12728  -1640   1115  -2929       O  
+ATOM   6668  CB  GLU B 469     -31.686  32.869  34.403  1.00104.67           C  
+ANISOU 6668  CB  GLU B 469    10258  16944  12569  -2093   1132  -3551       C  
+ATOM   6669  CG  GLU B 469     -30.348  32.959  35.131  1.00112.38           C  
+ANISOU 6669  CG  GLU B 469    10941  18316  13442  -2255    948  -3646       C  
+ATOM   6670  CD  GLU B 469     -30.143  34.277  35.852  1.00119.66           C  
+ANISOU 6670  CD  GLU B 469    11805  19158  14503  -2561    798  -4063       C  
+ATOM   6671  OE1 GLU B 469     -30.711  35.297  35.409  1.00127.92           O  
+ANISOU 6671  OE1 GLU B 469    12997  19753  15855  -2692    853  -4209       O  
+ATOM   6672  OE2 GLU B 469     -29.409  34.292  36.863  1.00114.50           O  
+ANISOU 6672  OE2 GLU B 469    10968  18885  13652  -2666    613  -4247       O  
+ATOM   6673  N   PHE B 470     -32.306  29.787  35.367  1.00101.10           N  
+ANISOU 6673  N   PHE B 470     9948  17129  11337  -1494   1190  -3134       N  
+ATOM   6674  CA  PHE B 470     -31.936  28.624  36.169  1.00 94.44           C  
+ANISOU 6674  CA  PHE B 470     9057  16693  10134  -1320   1110  -2990       C  
+ATOM   6675  C   PHE B 470     -31.619  27.437  35.256  1.00 92.97           C  
+ANISOU 6675  C   PHE B 470     8889  16495   9941  -1089   1207  -2593       C  
+ATOM   6676  O   PHE B 470     -30.579  26.772  35.395  1.00 96.10           O  
+ANISOU 6676  O   PHE B 470     9105  17181  10225   -986   1119  -2425       O  
+ATOM   6677  CB  PHE B 470     -33.060  28.273  37.145  1.00 90.26           C  
+ANISOU 6677  CB  PHE B 470     8724  16251   9321  -1238   1132  -3110       C  
+ATOM   6678  CG  PHE B 470     -32.753  27.103  38.032  1.00 88.98           C  
+ANISOU 6678  CG  PHE B 470     8551  16490   8769  -1075   1043  -2935       C  
+ATOM   6679  CD1 PHE B 470     -32.049  27.281  39.211  1.00 93.75           C  
+ANISOU 6679  CD1 PHE B 470     8997  17499   9123  -1159    841  -3098       C  
+ATOM   6680  CD2 PHE B 470     -33.180  25.829  37.697  1.00 83.99           C  
+ANISOU 6680  CD2 PHE B 470     8079  15820   8014   -846   1144  -2605       C  
+ATOM   6681  CE1 PHE B 470     -31.767  26.210  40.034  1.00 93.71           C  
+ANISOU 6681  CE1 PHE B 470     8994  17865   8745   -999    739  -2901       C  
+ATOM   6682  CE2 PHE B 470     -32.901  24.753  38.517  1.00 84.37           C  
+ANISOU 6682  CE2 PHE B 470     8142  16195   7719   -693   1052  -2413       C  
+ATOM   6683  CZ  PHE B 470     -32.194  24.944  39.687  1.00 89.21           C  
+ANISOU 6683  CZ  PHE B 470     8598  17222   8077   -761    847  -2545       C  
+ATOM   6684  N   VAL B 471     -32.510  27.205  34.297  1.00 88.53           N  
+ANISOU 6684  N   VAL B 471     8537  15592   9509  -1002   1380  -2462       N  
+ATOM   6685  CA  VAL B 471     -32.362  26.108  33.348  1.00 90.17           C  
+ANISOU 6685  CA  VAL B 471     8814  15731   9715   -787   1490  -2130       C  
+ATOM   6686  C   VAL B 471     -31.126  26.361  32.485  1.00 98.38           C  
+ANISOU 6686  C   VAL B 471     9626  16806  10948   -832   1500  -2021       C  
+ATOM   6687  O   VAL B 471     -30.431  25.429  32.073  1.00103.17           O  
+ANISOU 6687  O   VAL B 471    10161  17545  11496   -640   1530  -1790       O  
+ATOM   6688  CB  VAL B 471     -33.621  25.965  32.461  1.00 75.92           C  
+ANISOU 6688  CB  VAL B 471     7278  13552   8017   -733   1654  -2056       C  
+ATOM   6689  CG1 VAL B 471     -33.365  25.033  31.286  1.00 77.49           C  
+ANISOU 6689  CG1 VAL B 471     7546  13642   8254   -554   1768  -1763       C  
+ATOM   6690  CG2 VAL B 471     -34.794  25.465  33.288  1.00 71.09           C  
+ANISOU 6690  CG2 VAL B 471     6856  12963   7191   -666   1668  -2110       C  
+ATOM   6691  N   GLU B 472     -30.845  27.639  32.252  1.00 96.14           N  
+ANISOU 6691  N   GLU B 472     9222  16407  10900  -1091   1478  -2196       N  
+ATOM   6692  CA  GLU B 472     -29.677  28.064  31.493  1.00 97.02           C  
+ANISOU 6692  CA  GLU B 472     9088  16568  11207  -1207   1496  -2110       C  
+ATOM   6693  C   GLU B 472     -28.402  27.719  32.242  1.00 98.74           C  
+ANISOU 6693  C   GLU B 472     8988  17234  11293  -1183   1343  -2102       C  
+ATOM   6694  O   GLU B 472     -27.429  27.255  31.648  1.00108.16           O  
+ANISOU 6694  O   GLU B 472     9978  18593  12524  -1089   1389  -1910       O  
+ATOM   6695  CB  GLU B 472     -29.725  29.571  31.234  1.00 99.08           C  
+ANISOU 6695  CB  GLU B 472     9313  16578  11754  -1532   1484  -2307       C  
+ATOM   6696  CG  GLU B 472     -30.476  29.989  29.983  1.00 99.83           C  
+ANISOU 6696  CG  GLU B 472     9618  16247  12064  -1564   1647  -2199       C  
+ATOM   6697  CD  GLU B 472     -30.711  31.487  29.932  1.00111.67           C  
+ANISOU 6697  CD  GLU B 472    11141  17445  13845  -1860   1604  -2406       C  
+ATOM   6698  OE1 GLU B 472     -30.307  32.185  30.888  1.00120.58           O  
+ANISOU 6698  OE1 GLU B 472    12130  18687  14998  -2048   1455  -2667       O  
+ATOM   6699  OE2 GLU B 472     -31.303  31.968  28.943  1.00110.51           O  
+ANISOU 6699  OE2 GLU B 472    11160  16937  13890  -1902   1707  -2310       O  
+ATOM   6700  N   ILE B 473     -28.413  27.960  33.550  1.00 93.86           N  
+ANISOU 6700  N   ILE B 473     8318  16835  10509  -1262   1160  -2320       N  
+ATOM   6701  CA  ILE B 473     -27.286  27.600  34.397  1.00 98.38           C  
+ANISOU 6701  CA  ILE B 473     8595  17872  10911  -1228    970  -2315       C  
+ATOM   6702  C   ILE B 473     -27.091  26.090  34.377  1.00107.28           C  
+ANISOU 6702  C   ILE B 473     9753  19181  11826   -856    991  -2016       C  
+ATOM   6703  O   ILE B 473     -25.955  25.603  34.370  1.00122.31           O  
+ANISOU 6703  O   ILE B 473    11375  21391  13706   -738    916  -1876       O  
+ATOM   6704  CB  ILE B 473     -27.486  28.098  35.849  1.00102.67           C  
+ANISOU 6704  CB  ILE B 473     9133  18624  11254  -1374    763  -2618       C  
+ATOM   6705  CG1 ILE B 473     -26.795  29.448  36.059  1.00106.86           C  
+ANISOU 6705  CG1 ILE B 473     9427  19190  11985  -1743    636  -2900       C  
+ATOM   6706  CG2 ILE B 473     -26.919  27.107  36.845  1.00105.25           C  
+ANISOU 6706  CG2 ILE B 473     9338  19411  11241  -1172    585  -2507       C  
+ATOM   6707  CD1 ILE B 473     -27.177  30.522  35.065  1.00112.92           C  
+ANISOU 6707  CD1 ILE B 473    10290  19493  13121  -1968    784  -2980       C  
+ATOM   6708  N   LEU B 474     -28.193  25.345  34.335  1.00102.29           N  
+ANISOU 6708  N   LEU B 474     9456  18346  11064   -670   1094  -1916       N  
+ATOM   6709  CA  LEU B 474     -28.077  23.897  34.215  1.00 96.27           C  
+ANISOU 6709  CA  LEU B 474     8775  17664  10139   -324   1127  -1625       C  
+ATOM   6710  C   LEU B 474     -27.432  23.530  32.879  1.00 99.63           C  
+ANISOU 6710  C   LEU B 474     9104  17987  10763   -190   1284  -1427       C  
+ATOM   6711  O   LEU B 474     -26.560  22.665  32.814  1.00 96.51           O  
+ANISOU 6711  O   LEU B 474     8550  17808  10312     56   1253  -1243       O  
+ATOM   6712  CB  LEU B 474     -29.446  23.230  34.343  1.00 90.58           C  
+ANISOU 6712  CB  LEU B 474     8440  16703   9273   -209   1221  -1562       C  
+ATOM   6713  CG  LEU B 474     -29.969  23.037  35.766  1.00 94.92           C  
+ANISOU 6713  CG  LEU B 474     9090  17461   9515   -223   1083  -1649       C  
+ATOM   6714  CD1 LEU B 474     -31.419  22.583  35.740  1.00 86.12           C  
+ANISOU 6714  CD1 LEU B 474     8327  16080   8314   -181   1219  -1610       C  
+ATOM   6715  CD2 LEU B 474     -29.099  22.047  36.527  1.00 96.62           C  
+ANISOU 6715  CD2 LEU B 474     9181  18041   9487     -1    912  -1450       C  
+ATOM   6716  N   SER B 475     -27.871  24.199  31.816  1.00102.62           N  
+ANISOU 6716  N   SER B 475     9581  18045  11366   -340   1454  -1467       N  
+ATOM   6717  CA  SER B 475     -27.319  23.987  30.480  1.00103.17           C  
+ANISOU 6717  CA  SER B 475     9573  18027  11599   -254   1630  -1303       C  
+ATOM   6718  C   SER B 475     -26.131  24.913  30.225  1.00102.26           C  
+ANISOU 6718  C   SER B 475     9072  18112  11671   -477   1606  -1365       C  
+ATOM   6719  O   SER B 475     -26.213  25.811  29.386  1.00 93.35           O  
+ANISOU 6719  O   SER B 475     7944  16776  10748   -706   1722  -1400       O  
+ATOM   6720  CB  SER B 475     -28.398  24.188  29.414  1.00 90.69           C  
+ANISOU 6720  CB  SER B 475     8305  16023  10131   -304   1817  -1277       C  
+ATOM   6721  OG  SER B 475     -28.380  25.508  28.903  1.00 95.01           O  
+ANISOU 6721  OG  SER B 475     8776  16420  10902   -613   1858  -1392       O  
+ATOM   6722  N   ASN B 476     -25.044  24.705  30.963  1.00105.85           N  
+ANISOU 6722  N   ASN B 476     9193  18973  12051   -424   1445  -1364       N  
+ATOM   6723  CA  ASN B 476     -23.854  25.553  30.873  1.00107.92           C  
+ANISOU 6723  CA  ASN B 476     9034  19488  12484   -664   1392  -1432       C  
+ATOM   6724  C   ASN B 476     -23.347  25.763  29.447  1.00116.78           C  
+ANISOU 6724  C   ASN B 476    10036  20522  13814   -711   1631  -1298       C  
+ATOM   6725  O   ASN B 476     -22.649  26.737  29.161  1.00125.11           O  
+ANISOU 6725  O   ASN B 476    10817  21659  15059  -1018   1641  -1358       O  
+ATOM   6726  CB  ASN B 476     -22.732  24.970  31.732  1.00104.50           C  
+ANISOU 6726  CB  ASN B 476     8241  19545  11918   -500   1192  -1388       C  
+ATOM   6727  OXT ASN B 476     -23.626  24.967  28.549  1.00114.39           O  
+ANISOU 6727  OXT ASN B 476     9914  20068  13480   -459   1822  -1129       O  
+TER    6728      ASN B 476                                                      
+ATOM   6729  N   HIS C   2     -46.936  64.707  14.798  1.00107.48           N  
+ANISOU 6729  N   HIS C   2    11164  14632  15042   4451   3831  -1596       N  
+ATOM   6730  CA  HIS C   2     -47.169  63.568  15.678  1.00109.67           C  
+ANISOU 6730  CA  HIS C   2    11344  15200  15126   4315   4037  -1486       C  
+ATOM   6731  C   HIS C   2     -46.082  63.459  16.742  1.00107.50           C  
+ANISOU 6731  C   HIS C   2    11416  14916  14515   4258   4097  -1652       C  
+ATOM   6732  O   HIS C   2     -46.373  63.308  17.928  1.00113.62           O  
+ANISOU 6732  O   HIS C   2    12220  15860  15091   4313   4305  -1714       O  
+ATOM   6733  CB  HIS C   2     -47.238  62.271  14.870  1.00102.66           C  
+ANISOU 6733  CB  HIS C   2    10240  14435  14332   4056   3974  -1194       C  
+HETATM 6734  N   MSE C   3     -44.829  63.539  16.306  1.00 88.59           N  
+ANISOU 6734  N   MSE C   3     9282  12322  12057   4149   3910  -1715       N  
+HETATM 6735  CA  MSE C   3     -43.689  63.403  17.204  1.00 85.13           C  
+ANISOU 6735  CA  MSE C   3     9174  11861  11313   4074   3921  -1861       C  
+HETATM 6736  C   MSE C   3     -43.032  64.763  17.443  1.00 89.30           C  
+ANISOU 6736  C   MSE C   3    10012  12110  11807   4234   3813  -2150       C  
+HETATM 6737  O   MSE C   3     -43.488  65.776  16.913  1.00 94.28           O  
+ANISOU 6737  O   MSE C   3    10600  12564  12658   4402   3741  -2227       O  
+HETATM 6738  CB  MSE C   3     -42.684  62.400  16.631  1.00 83.45           C  
+ANISOU 6738  CB  MSE C   3     9029  11638  11039   3814   3795  -1717       C  
+HETATM 6739  CG  MSE C   3     -43.321  61.076  16.215  1.00 87.41           C  
+ANISOU 6739  CG  MSE C   3     9225  12363  11625   3635   3866  -1418       C  
+HETATM 6740 SE   MSE C   3     -42.146  59.899  15.193  1.00119.48          SE  
+ANISOU 6740 SE   MSE C   3    13347  16358  15693   3324   3689  -1226      SE  
+HETATM 6741  CE  MSE C   3     -41.278  58.970  16.671  1.00 74.38           C  
+ANISOU 6741  CE  MSE C   3     7868  10822   9571   3191   3814  -1265       C  
+ATOM   6742  N   ASN C   4     -41.970  64.786  18.245  1.00 85.61           N  
+ANISOU 6742  N   ASN C   4     9859  11593  11075   4177   3788  -2305       N  
+ATOM   6743  CA  ASN C   4     -41.305  66.042  18.590  1.00 91.04           C  
+ANISOU 6743  CA  ASN C   4    10861  12011  11718   4304   3679  -2585       C  
+ATOM   6744  C   ASN C   4     -40.616  66.664  17.373  1.00 86.76           C  
+ANISOU 6744  C   ASN C   4    10414  11156  11395   4264   3421  -2602       C  
+ATOM   6745  O   ASN C   4     -40.170  65.943  16.481  1.00 95.09           O  
+ANISOU 6745  O   ASN C   4    11399  12212  12519   4090   3316  -2428       O  
+ATOM   6746  CB  ASN C   4     -40.299  65.822  19.729  1.00 91.27           C  
+ANISOU 6746  CB  ASN C   4    11198  12078  11404   4230   3688  -2728       C  
+ATOM   6747  CG  ASN C   4     -39.112  64.977  19.313  1.00 91.64           C  
+ANISOU 6747  CG  ASN C   4    11349  12108  11362   3988   3538  -2631       C  
+ATOM   6748  OD1 ASN C   4     -38.212  65.446  18.615  1.00104.10           O  
+ANISOU 6748  OD1 ASN C   4    13085  13434  13035   3929   3324  -2697       O  
+ATOM   6749  ND2 ASN C   4     -39.098  63.724  19.750  1.00109.70           N  
+ANISOU 6749  ND2 ASN C   4    13551  14658  13473   3846   3653  -2469       N  
+ATOM   6750  N   PRO C   5     -40.540  68.008  17.331  1.00 98.00           N  
+ANISOU 6750  N   PRO C   5    12004  12299  12933   4425   3325  -2802       N  
+ATOM   6751  CA  PRO C   5     -40.025  68.774  16.187  1.00 97.84           C  
+ANISOU 6751  CA  PRO C   5    12074  11950  13151   4413   3088  -2814       C  
+ATOM   6752  C   PRO C   5     -38.678  68.295  15.642  1.00 87.56           C  
+ANISOU 6752  C   PRO C   5    10943  10540  11788   4187   2903  -2765       C  
+ATOM   6753  O   PRO C   5     -38.463  68.376  14.433  1.00 94.62           O  
+ANISOU 6753  O   PRO C   5    11788  11275  12887   4128   2751  -2644       O  
+ATOM   6754  CB  PRO C   5     -39.901  70.202  16.746  1.00109.63           C  
+ANISOU 6754  CB  PRO C   5    13818  13174  14663   4587   3043  -3081       C  
+ATOM   6755  CG  PRO C   5     -40.078  70.076  18.235  1.00105.68           C  
+ANISOU 6755  CG  PRO C   5    13413  12868  13873   4662   3236  -3229       C  
+ATOM   6756  CD  PRO C   5     -40.976  68.904  18.414  1.00104.52           C  
+ANISOU 6756  CD  PRO C   5    12952  13095  13664   4633   3447  -3026       C  
+ATOM   6757  N   ILE C   6     -37.786  67.820  16.507  1.00 92.26           N  
+ANISOU 6757  N   ILE C   6    11734  11215  12105   4070   2912  -2852       N  
+ATOM   6758  CA  ILE C   6     -36.486  67.331  16.057  1.00 84.13           C  
+ANISOU 6758  CA  ILE C   6    10858  10096  11013   3861   2742  -2812       C  
+ATOM   6759  C   ILE C   6     -36.646  66.087  15.184  1.00 87.67           C  
+ANISOU 6759  C   ILE C   6    11066  10724  11522   3714   2781  -2529       C  
+ATOM   6760  O   ILE C   6     -36.104  66.009  14.074  1.00 86.28           O  
+ANISOU 6760  O   ILE C   6    10894  10391  11499   3589   2626  -2416       O  
+ATOM   6761  CB  ILE C   6     -35.562  66.999  17.247  1.00 78.41           C  
+ANISOU 6761  CB  ILE C   6    10372   9455   9965   3774   2743  -2954       C  
+ATOM   6762  CG1 ILE C   6     -35.318  68.244  18.103  1.00 81.61           C  
+ANISOU 6762  CG1 ILE C   6    11046   9660  10303   3903   2683  -3238       C  
+ATOM   6763  CG2 ILE C   6     -34.242  66.423  16.756  1.00 73.47           C  
+ANISOU 6763  CG2 ILE C   6     9871   8756   9289   3561   2569  -2902       C  
+ATOM   6764  CD1 ILE C   6     -34.414  68.001  19.294  1.00 80.94           C  
+ANISOU 6764  CD1 ILE C   6    11212   9647   9895   3830   2654  -3389       C  
+ATOM   6765  N   VAL C   7     -37.417  65.128  15.688  1.00 79.40           N  
+ANISOU 6765  N   VAL C   7     9808   9993  10369   3698   2981  -2398       N  
+ATOM   6766  CA  VAL C   7     -37.689  63.891  14.966  1.00 79.93           C  
+ANISOU 6766  CA  VAL C   7     9634  10239  10499   3545   3034  -2120       C  
+ATOM   6767  C   VAL C   7     -38.424  64.169  13.657  1.00 78.94           C  
+ANISOU 6767  C   VAL C   7     9291  10009  10693   3592   2975  -1968       C  
+ATOM   6768  O   VAL C   7     -38.112  63.573  12.627  1.00 70.21           O  
+ANISOU 6768  O   VAL C   7     8105   8864   9706   3373   2840  -1782       O  
+ATOM   6769  CB  VAL C   7     -38.512  62.911  15.830  1.00 83.46           C  
+ANISOU 6769  CB  VAL C   7     9887  11027  10796   3523   3258  -2008       C  
+ATOM   6770  CG1 VAL C   7     -38.966  61.716  15.006  1.00 80.98           C  
+ANISOU 6770  CG1 VAL C   7     9295  10868  10606   3364   3297  -1713       C  
+ATOM   6771  CG2 VAL C   7     -37.691  62.448  17.021  1.00 90.48           C  
+ANISOU 6771  CG2 VAL C   7    10995  12025  11359   3446   3302  -2107       C  
+ATOM   6772  N   GLU C   8     -39.380  65.094  13.697  1.00 73.84           N  
+ANISOU 6772  N   GLU C   8     8551   9314  10191   3800   3003  -2045       N  
+ATOM   6773  CA  GLU C   8     -40.140  65.475  12.508  1.00 81.21           C  
+ANISOU 6773  CA  GLU C   8     9282  10144  11430   3873   2927  -1909       C  
+ATOM   6774  C   GLU C   8     -39.226  66.091  11.452  1.00 90.35           C  
+ANISOU 6774  C   GLU C   8    10625  10972  12731   3790   2684  -1913       C  
+ATOM   6775  O   GLU C   8     -39.320  65.777  10.258  1.00105.61           O  
+ANISOU 6775  O   GLU C   8    12426  12859  14841   3628   2536  -1713       O  
+ATOM   6776  CB  GLU C   8     -41.252  66.464  12.876  1.00 88.30           C  
+ANISOU 6776  CB  GLU C   8    10077  11031  12442   4127   2992  -2023       C  
+ATOM   6777  CG  GLU C   8     -42.306  65.921  13.833  1.00 89.55           C  
+ANISOU 6777  CG  GLU C   8    10017  11509  12501   4188   3230  -1992       C  
+ATOM   6778  CD  GLU C   8     -43.226  64.904  13.183  1.00 90.84           C  
+ANISOU 6778  CD  GLU C   8     9816  11896  12803   4097   3289  -1708       C  
+ATOM   6779  OE1 GLU C   8     -43.937  64.188  13.919  1.00 81.17           O  
+ANISOU 6779  OE1 GLU C   8     8412  10947  11484   4077   3480  -1635       O  
+ATOM   6780  OE2 GLU C   8     -43.255  64.834  11.937  1.00 98.60           O  
+ANISOU 6780  OE2 GLU C   8    10696  12769  14000   4038   3140  -1551       O  
+ATOM   6781  N   LEU C   9     -38.333  66.964  11.910  1.00 82.94           N  
+ANISOU 6781  N   LEU C   9     9995   9812  11706   3836   2592  -2140       N  
+ATOM   6782  CA  LEU C   9     -37.360  67.613  11.042  1.00 80.47           C  
+ANISOU 6782  CA  LEU C   9     9873   9186  11517   3682   2321  -2149       C  
+ATOM   6783  C   LEU C   9     -36.482  66.573  10.365  1.00 74.96           C  
+ANISOU 6783  C   LEU C   9     9162   8544  10774   3332   2198  -1965       C  
+ATOM   6784  O   LEU C   9     -36.247  66.634   9.152  1.00 91.57           O  
+ANISOU 6784  O   LEU C   9    11235  10510  13045   3185   2026  -1813       O  
+ATOM   6785  CB  LEU C   9     -36.499  68.596  11.837  1.00 90.18           C  
+ANISOU 6785  CB  LEU C   9    11432  10192  12641   3764   2250  -2431       C  
+ATOM   6786  CG  LEU C   9     -35.457  69.382  11.039  1.00 87.58           C  
+ANISOU 6786  CG  LEU C   9    11305   9517  12456   3606   1977  -2447       C  
+ATOM   6787  CD1 LEU C   9     -36.107  70.082   9.854  1.00 90.80           C  
+ANISOU 6787  CD1 LEU C   9    11604   9738  13158   3685   1876  -2317       C  
+ATOM   6788  CD2 LEU C   9     -34.735  70.382  11.929  1.00 91.26           C  
+ANISOU 6788  CD2 LEU C   9    12083   9758  12834   3702   1905  -2742       C  
+ATOM   6789  N   PHE C  10     -35.999  65.617  11.155  1.00 68.45           N  
+ANISOU 6789  N   PHE C  10     8370   7923   9714   3212   2292  -1976       N  
+ATOM   6790  CA  PHE C  10     -35.220  64.514  10.607  1.00 66.25           C  
+ANISOU 6790  CA  PHE C  10     8068   7722   9383   2905   2202  -1804       C  
+ATOM   6791  C   PHE C  10     -36.017  63.756   9.557  1.00 66.10           C  
+ANISOU 6791  C   PHE C  10     7783   7815   9516   2816   2200  -1551       C  
+ATOM   6792  O   PHE C  10     -35.481  63.372   8.516  1.00 63.17           O  
+ANISOU 6792  O   PHE C  10     7413   7371   9219   2605   2045  -1407       O  
+ATOM   6793  CB  PHE C  10     -34.783  63.546  11.699  1.00 71.30           C  
+ANISOU 6793  CB  PHE C  10     8755   8584   9750   2828   2326  -1839       C  
+ATOM   6794  CG  PHE C  10     -34.373  62.198  11.174  1.00 66.44           C  
+ANISOU 6794  CG  PHE C  10     8042   8104   9097   2559   2289  -1628       C  
+ATOM   6795  CD1 PHE C  10     -33.184  62.049  10.478  1.00 65.82           C  
+ANISOU 6795  CD1 PHE C  10     8083   7885   9042   2335   2099  -1581       C  
+ATOM   6796  CD2 PHE C  10     -35.174  61.085  11.367  1.00 72.32           C  
+ANISOU 6796  CD2 PHE C  10     8574   9109   9794   2534   2449  -1475       C  
+ATOM   6797  CE1 PHE C  10     -32.801  60.817   9.987  1.00 74.15           C  
+ANISOU 6797  CE1 PHE C  10     9062   9052  10060   2112   2070  -1402       C  
+ATOM   6798  CE2 PHE C  10     -34.794  59.848  10.878  1.00 77.34           C  
+ANISOU 6798  CE2 PHE C  10     9143   9840  10405   2293   2402  -1293       C  
+ATOM   6799  CZ  PHE C  10     -33.606  59.715  10.188  1.00 80.93           C  
+ANISOU 6799  CZ  PHE C  10     9732  10147  10869   2092   2213  -1265       C  
+ATOM   6800  N   ILE C  11     -37.294  63.527   9.851  1.00 78.24           N  
+ANISOU 6800  N   ILE C  11     9093   9539  11096   2979   2374  -1498       N  
+ATOM   6801  CA  ILE C  11     -38.168  62.804   8.940  1.00 82.85           C  
+ANISOU 6801  CA  ILE C  11     9402  10240  11836   2902   2363  -1264       C  
+ATOM   6802  C   ILE C  11     -38.226  63.533   7.603  1.00 83.69           C  
+ANISOU 6802  C   ILE C  11     9509  10118  12170   2890   2151  -1190       C  
+ATOM   6803  O   ILE C  11     -38.136  62.904   6.551  1.00 72.16           O  
+ANISOU 6803  O   ILE C  11     7976   8659  10781   2699   2020  -1011       O  
+ATOM   6804  CB  ILE C  11     -39.592  62.636   9.518  1.00 71.68           C  
+ANISOU 6804  CB  ILE C  11     7718   9049  10468   3107   2586  -1226       C  
+ATOM   6805  CG1 ILE C  11     -39.585  61.628  10.669  1.00 75.24           C  
+ANISOU 6805  CG1 ILE C  11     8135   9764  10688   3063   2799  -1222       C  
+ATOM   6806  CG2 ILE C  11     -40.560  62.170   8.444  1.00 65.32           C  
+ANISOU 6806  CG2 ILE C  11     6622   8310   9886   3047   2519   -998       C  
+ATOM   6807  CD1 ILE C  11     -40.919  61.499  11.379  1.00 68.59           C  
+ANISOU 6807  CD1 ILE C  11     7033   9157   9870   3273   3060  -1185       C  
+ATOM   6808  N   LYS C  12     -38.312  64.861   7.642  1.00 66.43           N  
+ANISOU 6808  N   LYS C  12     7432   7723  10084   3094   2109  -1329       N  
+ATOM   6809  CA  LYS C  12     -38.408  65.629   6.403  1.00 73.14           C  
+ANISOU 6809  CA  LYS C  12     8293   8346  11152   3102   1911  -1246       C  
+ATOM   6810  C   LYS C  12     -37.099  65.624   5.622  1.00 70.16           C  
+ANISOU 6810  C   LYS C  12     8124   7787  10746   2854   1715  -1200       C  
+ATOM   6811  O   LYS C  12     -37.086  65.379   4.410  1.00 86.01           O  
+ANISOU 6811  O   LYS C  12    10081   9747  12850   2720   1571  -1021       O  
+ATOM   6812  CB  LYS C  12     -38.794  67.081   6.687  1.00 86.03           C  
+ANISOU 6812  CB  LYS C  12    10009   9771  12908   3390   1913  -1409       C  
+ATOM   6813  CG  LYS C  12     -39.026  67.898   5.423  1.00 85.62           C  
+ANISOU 6813  CG  LYS C  12     9954   9486  13093   3424   1713  -1299       C  
+ATOM   6814  CD  LYS C  12     -39.376  69.340   5.734  1.00 83.79           C  
+ANISOU 6814  CD  LYS C  12     9823   9020  12993   3716   1708  -1464       C  
+ATOM   6815  CE  LYS C  12     -38.116  70.114   6.101  1.00 96.28           C  
+ANISOU 6815  CE  LYS C  12    11741  10338  14501   3655   1616  -1644       C  
+ATOM   6816  NZ  LYS C  12     -38.366  71.555   6.375  1.00107.90           N  
+ANISOU 6816  NZ  LYS C  12    13353  11532  16110   3926   1583  -1818       N  
+ATOM   6817  N   ASP C  13     -35.997  65.867   6.326  1.00 72.47           N  
+ANISOU 6817  N   ASP C  13     8646   7991  10898   2794   1712  -1357       N  
+ATOM   6818  CA  ASP C  13     -34.692  65.948   5.678  1.00 70.13           C  
+ANISOU 6818  CA  ASP C  13     8536   7522  10588   2570   1544  -1320       C  
+ATOM   6819  C   ASP C  13     -34.303  64.616   5.044  1.00 61.62           C  
+ANISOU 6819  C   ASP C  13     7377   6605   9429   2318   1518  -1136       C  
+ATOM   6820  O   ASP C  13     -33.902  64.560   3.873  1.00 64.78           O  
+ANISOU 6820  O   ASP C  13     7805   6907   9902   2175   1378   -992       O  
+ATOM   6821  CB  ASP C  13     -33.631  66.390   6.687  1.00 69.98           C  
+ANISOU 6821  CB  ASP C  13     8747   7403  10439   2553   1544  -1530       C  
+ATOM   6822  CG  ASP C  13     -33.875  67.794   7.209  1.00 82.60           C  
+ANISOU 6822  CG  ASP C  13    10476   8782  12124   2789   1531  -1730       C  
+ATOM   6823  OD1 ASP C  13     -34.502  68.597   6.486  1.00 83.06           O  
+ANISOU 6823  OD1 ASP C  13    10496   8680  12382   2914   1463  -1678       O  
+ATOM   6824  OD2 ASP C  13     -33.441  68.095   8.340  1.00 95.50           O  
+ANISOU 6824  OD2 ASP C  13    12264  10398  13625   2855   1578  -1943       O  
+ATOM   6825  N   PHE C  14     -34.438  63.541   5.812  1.00 60.59           N  
+ANISOU 6825  N   PHE C  14     7159   6719   9143   2273   1656  -1138       N  
+ATOM   6826  CA  PHE C  14     -34.059  62.228   5.314  1.00 71.30           C  
+ANISOU 6826  CA  PHE C  14     8456   8215  10419   2045   1634   -981       C  
+ATOM   6827  C   PHE C  14     -35.050  61.729   4.268  1.00 72.00           C  
+ANISOU 6827  C   PHE C  14     8344   8377  10634   2023   1589   -790       C  
+ATOM   6828  O   PHE C  14     -34.669  60.986   3.366  1.00 68.17           O  
+ANISOU 6828  O   PHE C  14     7860   7904  10135   1839   1494   -653       O  
+ATOM   6829  CB  PHE C  14     -33.932  61.219   6.455  1.00 68.17           C  
+ANISOU 6829  CB  PHE C  14     8033   8041   9827   2004   1786  -1024       C  
+ATOM   6830  CG  PHE C  14     -33.106  60.017   6.097  1.00 65.83           C  
+ANISOU 6830  CG  PHE C  14     7762   7823   9429   1764   1741   -910       C  
+ATOM   6831  CD1 PHE C  14     -31.753  60.149   5.826  1.00 59.02           C  
+ANISOU 6831  CD1 PHE C  14     7077   6828   8521   1625   1631   -937       C  
+ATOM   6832  CD2 PHE C  14     -33.679  58.759   6.026  1.00 55.40           C  
+ANISOU 6832  CD2 PHE C  14     6281   6697   8073   1679   1807   -774       C  
+ATOM   6833  CE1 PHE C  14     -30.988  59.049   5.490  1.00 53.91           C  
+ANISOU 6833  CE1 PHE C  14     6447   6250   7785   1429   1599   -836       C  
+ATOM   6834  CE2 PHE C  14     -32.916  57.654   5.696  1.00 61.60           C  
+ANISOU 6834  CE2 PHE C  14     7105   7531   8769   1475   1762   -680       C  
+ATOM   6835  CZ  PHE C  14     -31.572  57.800   5.422  1.00 57.11           C  
+ANISOU 6835  CZ  PHE C  14     6715   6837   8147   1362   1663   -714       C  
+ATOM   6836  N   THR C  15     -36.316  62.128   4.385  1.00 70.48           N  
+ANISOU 6836  N   THR C  15     7980   8234  10564   2216   1651   -786       N  
+ATOM   6837  CA  THR C  15     -37.286  61.811   3.340  1.00 69.69           C  
+ANISOU 6837  CA  THR C  15     7684   8181  10613   2204   1567   -608       C  
+ATOM   6838  C   THR C  15     -36.829  62.436   2.030  1.00 66.60           C  
+ANISOU 6838  C   THR C  15     7416   7572  10317   2142   1360   -529       C  
+ATOM   6839  O   THR C  15     -36.844  61.787   0.983  1.00 63.17           O  
+ANISOU 6839  O   THR C  15     6947   7161   9895   1996   1242   -375       O  
+ATOM   6840  CB  THR C  15     -38.705  62.314   3.671  1.00 70.09           C  
+ANISOU 6840  CB  THR C  15     7514   8304  10813   2448   1658   -616       C  
+ATOM   6841  OG1 THR C  15     -39.236  61.567   4.772  1.00 80.93           O  
+ANISOU 6841  OG1 THR C  15     8736   9918  12096   2487   1868   -641       O  
+ATOM   6842  CG2 THR C  15     -39.623  62.156   2.471  1.00 65.47           C  
+ANISOU 6842  CG2 THR C  15     6740   7729  10407   2434   1516   -432       C  
+ATOM   6843  N   LYS C  16     -36.420  63.700   2.101  1.00 63.86           N  
+ANISOU 6843  N   LYS C  16     7228   7008  10029   2255   1316   -635       N  
+ATOM   6844  CA  LYS C  16     -35.897  64.399   0.934  1.00 68.62           C  
+ANISOU 6844  CA  LYS C  16     7970   7386  10717   2197   1136   -552       C  
+ATOM   6845  C   LYS C  16     -34.682  63.681   0.350  1.00 72.31           C  
+ANISOU 6845  C   LYS C  16     8572   7848  11054   1941   1070   -475       C  
+ATOM   6846  O   LYS C  16     -34.598  63.479  -0.862  1.00 72.66           O  
+ANISOU 6846  O   LYS C  16     8635   7852  11121   1840    945   -320       O  
+ATOM   6847  CB  LYS C  16     -35.532  65.841   1.292  1.00 64.18           C  
+ANISOU 6847  CB  LYS C  16     7575   6574  10237   2340   1111   -691       C  
+ATOM   6848  N   GLU C  17     -33.745  63.295   1.213  1.00 70.52           N  
+ANISOU 6848  N   GLU C  17     8442   7666  10684   1849   1156   -582       N  
+ATOM   6849  CA  GLU C  17     -32.532  62.620   0.752  1.00 59.58           C  
+ANISOU 6849  CA  GLU C  17     7172   6281   9184   1626   1111   -518       C  
+ATOM   6850  C   GLU C  17     -32.809  61.225   0.191  1.00 59.37           C  
+ANISOU 6850  C   GLU C  17     7037   6440   9081   1495   1109   -382       C  
+ATOM   6851  O   GLU C  17     -32.174  60.803  -0.776  1.00 75.41           O  
+ANISOU 6851  O   GLU C  17     9144   8440  11067   1350   1027   -273       O  
+ATOM   6852  CB  GLU C  17     -31.503  62.534   1.880  1.00 61.12           C  
+ANISOU 6852  CB  GLU C  17     7478   6488   9256   1572   1189   -667       C  
+ATOM   6853  CG  GLU C  17     -30.942  63.883   2.297  1.00 73.65           C  
+ANISOU 6853  CG  GLU C  17     9219   7852  10915   1648   1146   -803       C  
+ATOM   6854  CD  GLU C  17     -30.209  64.585   1.167  1.00 73.43           C  
+ANISOU 6854  CD  GLU C  17     9308   7606  10986   1552   1010   -698       C  
+ATOM   6855  OE1 GLU C  17     -29.550  63.896   0.360  1.00 76.39           O  
+ANISOU 6855  OE1 GLU C  17     9700   8022  11302   1381    975   -564       O  
+ATOM   6856  OE2 GLU C  17     -30.294  65.828   1.085  1.00 95.27           O  
+ANISOU 6856  OE2 GLU C  17    12157  10155  13888   1654    944   -746       O  
+ATOM   6857  N   VAL C  18     -33.750  60.509   0.798  1.00 59.34           N  
+ANISOU 6857  N   VAL C  18     6861   6623   9062   1546   1202   -387       N  
+ATOM   6858  CA  VAL C  18     -34.114  59.179   0.321  1.00 59.27           C  
+ANISOU 6858  CA  VAL C  18     6743   6771   9005   1419   1186   -263       C  
+ATOM   6859  C   VAL C  18     -34.832  59.260  -1.025  1.00 67.93           C  
+ANISOU 6859  C   VAL C  18     7778   7823  10210   1417   1033   -119       C  
+ATOM   6860  O   VAL C  18     -34.609  58.433  -1.911  1.00 64.69           O  
+ANISOU 6860  O   VAL C  18     7399   7441   9741   1274    944    -14       O  
+ATOM   6861  CB  VAL C  18     -35.004  58.435   1.342  1.00 59.79           C  
+ANISOU 6861  CB  VAL C  18     6623   7044   9052   1466   1329   -284       C  
+ATOM   6862  CG1 VAL C  18     -35.648  57.217   0.705  1.00 59.71           C  
+ANISOU 6862  CG1 VAL C  18     6472   7159   9056   1345   1276   -138       C  
+ATOM   6863  CG2 VAL C  18     -34.181  57.999   2.533  1.00 60.93           C  
+ANISOU 6863  CG2 VAL C  18     6853   7263   9036   1422   1460   -390       C  
+HETATM 6864  N   MSE C  19     -35.680  60.273  -1.181  1.00 87.08           N  
+ANISOU 6864  N   MSE C  19    10127  10171  12787   1588    992   -119       N  
+HETATM 6865  CA  MSE C  19     -36.519  60.400  -2.372  1.00 81.38           C  
+ANISOU 6865  CA  MSE C  19     9322   9419  12178   1613    832     20       C  
+HETATM 6866  C   MSE C  19     -35.716  60.642  -3.652  1.00 77.25           C  
+ANISOU 6866  C   MSE C  19     8996   8749  11606   1511    681    114       C  
+HETATM 6867  O   MSE C  19     -36.104  60.175  -4.723  1.00 76.38           O  
+ANISOU 6867  O   MSE C  19     8865   8665  11493   1447    543    241       O  
+HETATM 6868  CB  MSE C  19     -37.546  61.518  -2.175  1.00 84.12           C  
+ANISOU 6868  CB  MSE C  19     9547   9705  12708   1845    827     -5       C  
+HETATM 6869  CG  MSE C  19     -38.746  61.410  -3.099  1.00 92.00           C  
+ANISOU 6869  CG  MSE C  19    10366  10747  13842   1891    680    139       C  
+HETATM 6870 SE   MSE C  19     -40.368  62.156  -2.317  1.00155.93          SE  
+ANISOU 6870 SE   MSE C  19    18160  18914  22171   2186    768    100      SE  
+HETATM 6871  CE  MSE C  19     -39.713  63.948  -1.919  1.00104.80           C  
+ANISOU 6871  CE  MSE C  19    11914  12158  15748   2389    801    -49       C  
+ATOM   6872  N   GLU C  20     -34.604  61.367  -3.545  1.00 63.20           N  
+ANISOU 6872  N   GLU C  20     7408   6820   9787   1493    706     56       N  
+ATOM   6873  CA  GLU C  20     -33.654  61.489  -4.656  1.00 62.72           C  
+ANISOU 6873  CA  GLU C  20     7534   6642   9655   1375    609    155       C  
+ATOM   6874  C   GLU C  20     -32.811  60.245  -4.865  1.00 68.73           C  
+ANISOU 6874  C   GLU C  20     8361   7509  10242   1189    642    180       C  
+ATOM   6875  O   GLU C  20     -31.885  60.245  -5.680  1.00 74.54           O  
+ANISOU 6875  O   GLU C  20     9253   8174  10896   1090    602    252       O  
+ATOM   6876  CB  GLU C  20     -32.715  62.675  -4.464  1.00 75.79           C  
+ANISOU 6876  CB  GLU C  20     9350   8095  11350   1399    626    101       C  
+ATOM   6877  CG  GLU C  20     -33.114  63.900  -5.257  1.00 87.11           C  
+ANISOU 6877  CG  GLU C  20    10838   9339  12922   1511    504    186       C  
+ATOM   6878  CD  GLU C  20     -32.982  63.681  -6.761  1.00102.88           C  
+ANISOU 6878  CD  GLU C  20    12923  11313  14854   1423    373    375       C  
+ATOM   6879  OE1 GLU C  20     -32.431  62.640  -7.184  1.00111.51           O  
+ANISOU 6879  OE1 GLU C  20    14059  12518  15791   1274    388    421       O  
+ATOM   6880  OE2 GLU C  20     -33.430  64.556  -7.528  1.00 88.57           O  
+ANISOU 6880  OE2 GLU C  20    11148   9365  13138   1513    254    477       O  
+ATOM   6881  N   GLU C  21     -33.110  59.205  -4.098  1.00 65.96           N  
+ANISOU 6881  N   GLU C  21     7895   7327   9840   1150    727    126       N  
+ATOM   6882  CA  GLU C  21     -32.508  57.893  -4.289  1.00 67.60           C  
+ANISOU 6882  CA  GLU C  21     8146   7637   9899    990    746    154       C  
+ATOM   6883  C   GLU C  21     -30.985  57.873  -4.160  1.00 72.17           C  
+ANISOU 6883  C   GLU C  21     8891   8160  10370    895    811    118       C  
+ATOM   6884  O   GLU C  21     -30.319  57.095  -4.839  1.00 75.04           O  
+ANISOU 6884  O   GLU C  21     9344   8548  10621    782    791    178       O  
+ATOM   6885  CB  GLU C  21     -32.911  57.355  -5.662  1.00 68.69           C  
+ANISOU 6885  CB  GLU C  21     8310   7786  10003    929    596    285       C  
+ATOM   6886  CG  GLU C  21     -34.408  57.325  -5.892  1.00 79.30           C  
+ANISOU 6886  CG  GLU C  21     9472   9189  11470   1006    497    338       C  
+ATOM   6887  CD  GLU C  21     -34.801  56.438  -7.052  1.00 82.00           C  
+ANISOU 6887  CD  GLU C  21     9832   9574  11751    912    338    442       C  
+ATOM   6888  OE1 GLU C  21     -33.962  55.622  -7.484  1.00 82.17           O  
+ANISOU 6888  OE1 GLU C  21     9997   9605  11618    790    339    451       O  
+ATOM   6889  OE2 GLU C  21     -35.944  56.562  -7.538  1.00 81.34           O  
+ANISOU 6889  OE2 GLU C  21     9623   9510  11773    968    203    510       O  
+ATOM   6890  N   ASN C  22     -30.435  58.714  -3.289  1.00 74.19           N  
+ANISOU 6890  N   ASN C  22     9183   8340  10665    945    884     16       N  
+ATOM   6891  CA  ASN C  22     -28.989  58.719  -3.078  1.00 66.78           C  
+ANISOU 6891  CA  ASN C  22     8369   7353   9650    848    934    -17       C  
+ATOM   6892  C   ASN C  22     -28.629  58.624  -1.596  1.00 62.43           C  
+ANISOU 6892  C   ASN C  22     7791   6861   9070    863   1039   -162       C  
+ATOM   6893  O   ASN C  22     -27.519  58.967  -1.190  1.00 62.26           O  
+ANISOU 6893  O   ASN C  22     7855   6773   9027    813   1062   -218       O  
+ATOM   6894  CB  ASN C  22     -28.353  59.962  -3.701  1.00 65.56           C  
+ANISOU 6894  CB  ASN C  22     8334   7006   9572    854    878     26       C  
+ATOM   6895  CG  ASN C  22     -26.865  59.789  -3.949  1.00 67.65           C  
+ANISOU 6895  CG  ASN C  22     8706   7235   9763    722    910     58       C  
+ATOM   6896  OD1 ASN C  22     -26.431  58.781  -4.508  1.00 72.45           O  
+ANISOU 6896  OD1 ASN C  22     9338   7935  10256    634    928    126       O  
+ATOM   6897  ND2 ASN C  22     -26.077  60.771  -3.532  1.00 67.80           N  
+ANISOU 6897  ND2 ASN C  22     8786   7117   9859    711    916      8       N  
+ATOM   6898  N   ALA C  23     -29.574  58.155  -0.790  1.00 64.20           N  
+ANISOU 6898  N   ALA C  23     7891   7214   9289    931   1099   -216       N  
+ATOM   6899  CA  ALA C  23     -29.349  58.001   0.642  1.00 54.47           C  
+ANISOU 6899  CA  ALA C  23     6641   6061   7995    960   1206   -346       C  
+ATOM   6900  C   ALA C  23     -28.773  56.621   0.934  1.00 58.15           C  
+ANISOU 6900  C   ALA C  23     7107   6662   8325    837   1256   -320       C  
+ATOM   6901  O   ALA C  23     -29.005  55.674   0.183  1.00 60.92           O  
+ANISOU 6901  O   ALA C  23     7428   7074   8647    761   1225   -215       O  
+ATOM   6902  CB  ALA C  23     -30.639  58.216   1.412  1.00 54.58           C  
+ANISOU 6902  CB  ALA C  23     6521   6156   8062   1108   1274   -405       C  
+ATOM   6903  N   ALA C  24     -28.018  56.511   2.022  1.00 60.56           N  
+ANISOU 6903  N   ALA C  24     7458   7005   8546    823   1320   -418       N  
+ATOM   6904  CA  ALA C  24     -27.435  55.233   2.411  1.00 53.88           C  
+ANISOU 6904  CA  ALA C  24     6617   6280   7576    723   1365   -392       C  
+ATOM   6905  C   ALA C  24     -27.744  54.889   3.863  1.00 57.04           C  
+ANISOU 6905  C   ALA C  24     6973   6811   7888    779   1468   -478       C  
+ATOM   6906  O   ALA C  24     -27.980  55.773   4.685  1.00 53.18           O  
+ANISOU 6906  O   ALA C  24     6496   6302   7407    890   1505   -594       O  
+ATOM   6907  CB  ALA C  24     -25.935  55.250   2.183  1.00 48.70           C  
+ANISOU 6907  CB  ALA C  24     6070   5551   6881    627   1327   -392       C  
+ATOM   6908  N   ILE C  25     -27.743  53.596   4.168  1.00 52.87           N  
+ANISOU 6908  N   ILE C  25     6410   6412   7268    708   1517   -418       N  
+ATOM   6909  CA  ILE C  25     -27.978  53.133   5.531  1.00 50.13           C  
+ANISOU 6909  CA  ILE C  25     6033   6203   6812    749   1623   -468       C  
+ATOM   6910  C   ILE C  25     -26.745  52.426   6.076  1.00 54.78           C  
+ANISOU 6910  C   ILE C  25     6713   6826   7276    666   1619   -478       C  
+ATOM   6911  O   ILE C  25     -26.177  51.595   5.392  1.00 44.90           O  
+ANISOU 6911  O   ILE C  25     5484   5560   6018    563   1574   -391       O  
+ATOM   6912  CB  ILE C  25     -29.178  52.164   5.595  1.00 48.70           C  
+ANISOU 6912  CB  ILE C  25     5711   6154   6639    738   1694   -365       C  
+ATOM   6913  CG1 ILE C  25     -30.454  52.854   5.108  1.00 47.65           C  
+ANISOU 6913  CG1 ILE C  25     5454   6005   6646    831   1693   -348       C  
+ATOM   6914  CG2 ILE C  25     -29.346  51.599   7.000  1.00 55.91           C  
+ANISOU 6914  CG2 ILE C  25     6602   7221   7420    769   1823   -387       C  
+ATOM   6915  CD1 ILE C  25     -30.935  53.959   6.015  1.00 48.99           C  
+ANISOU 6915  CD1 ILE C  25     5605   6188   6822   1000   1777   -472       C  
+ATOM   6916  N   PHE C  26     -26.328  52.738   7.299  1.00 53.00           N  
+ANISOU 6916  N   PHE C  26     6545   6645   6946    720   1657   -587       N  
+ATOM   6917  CA  PHE C  26     -25.298  51.928   7.945  1.00 57.90           C  
+ANISOU 6917  CA  PHE C  26     7233   7327   7441    651   1649   -580       C  
+ATOM   6918  C   PHE C  26     -25.899  51.259   9.172  1.00 58.82           C  
+ANISOU 6918  C   PHE C  26     7322   7609   7416    699   1764   -575       C  
+ATOM   6919  O   PHE C  26     -26.313  51.925  10.123  1.00 56.17           O  
+ANISOU 6919  O   PHE C  26     7007   7325   7010    812   1828   -681       O  
+ATOM   6920  CB  PHE C  26     -24.075  52.772   8.327  1.00 59.62           C  
+ANISOU 6920  CB  PHE C  26     7557   7456   7640    650   1563   -697       C  
+ATOM   6921  CG  PHE C  26     -22.851  51.958   8.703  1.00 67.83           C  
+ANISOU 6921  CG  PHE C  26     8646   8537   8590    567   1519   -668       C  
+ATOM   6922  CD1 PHE C  26     -22.851  50.574   8.624  1.00 77.17           C  
+ANISOU 6922  CD1 PHE C  26     9797   9809   9714    509   1557   -545       C  
+ATOM   6923  CD2 PHE C  26     -21.698  52.588   9.139  1.00 67.48           C  
+ANISOU 6923  CD2 PHE C  26     8675   8431   8534    549   1425   -762       C  
+ATOM   6924  CE1 PHE C  26     -21.730  49.839   8.975  1.00 70.56           C  
+ANISOU 6924  CE1 PHE C  26     9001   9002   8805    453   1512   -515       C  
+ATOM   6925  CE2 PHE C  26     -20.574  51.857   9.490  1.00 71.81           C  
+ANISOU 6925  CE2 PHE C  26     9247   9023   9015    483   1372   -729       C  
+ATOM   6926  CZ  PHE C  26     -20.593  50.482   9.406  1.00 67.37           C  
+ANISOU 6926  CZ  PHE C  26     8653   8554   8392    445   1421   -604       C  
+ATOM   6927  N   ALA C  27     -25.921  49.931   9.143  1.00 50.45           N  
+ANISOU 6927  N   ALA C  27     6231   6629   6311    617   1793   -448       N  
+ATOM   6928  CA  ALA C  27     -26.640  49.145  10.136  1.00 48.23           C  
+ANISOU 6928  CA  ALA C  27     5904   6505   5917    641   1915   -389       C  
+ATOM   6929  C   ALA C  27     -25.701  48.451  11.113  1.00 58.20           C  
+ANISOU 6929  C   ALA C  27     7264   7838   7010    615   1910   -384       C  
+ATOM   6930  O   ALA C  27     -24.787  47.733  10.710  1.00 50.71           O  
+ANISOU 6930  O   ALA C  27     6357   6841   6067    526   1830   -324       O  
+ATOM   6931  CB  ALA C  27     -27.526  48.121   9.447  1.00 52.40           C  
+ANISOU 6931  CB  ALA C  27     6317   7061   6533    560   1945   -231       C  
+ATOM   6932  N   GLY C  28     -25.937  48.669  12.402  1.00 75.30           N  
+ANISOU 6932  N   GLY C  28     9469  10122   9018    705   1997   -446       N  
+ATOM   6933  CA  GLY C  28     -25.195  47.978  13.438  1.00 63.10           C  
+ANISOU 6933  CA  GLY C  28     8020   8667   7288    693   1994   -426       C  
+ATOM   6934  C   GLY C  28     -25.927  46.728  13.884  1.00 54.66           C  
+ANISOU 6934  C   GLY C  28     6891   7726   6150    656   2116   -256       C  
+ATOM   6935  O   GLY C  28     -26.985  46.398  13.349  1.00 59.76           O  
+ANISOU 6935  O   GLY C  28     7409   8386   6910    626   2192   -157       O  
+ATOM   6936  N   ALA C  29     -25.362  46.033  14.865  1.00 54.06           N  
+ANISOU 6936  N   ALA C  29     6905   7740   5895    651   2123   -211       N  
+ATOM   6937  CA  ALA C  29     -25.908  44.761  15.328  1.00 48.88           C  
+ANISOU 6937  CA  ALA C  29     6212   7189   5171    599   2228    -24       C  
+ATOM   6938  C   ALA C  29     -27.291  44.922  15.958  1.00 56.82           C  
+ANISOU 6938  C   ALA C  29     7124   8341   6125    671   2426     17       C  
+ATOM   6939  O   ALA C  29     -28.081  43.978  15.987  1.00 58.74           O  
+ANISOU 6939  O   ALA C  29     7269   8647   6401    603   2527    195       O  
+ATOM   6940  CB  ALA C  29     -24.951  44.110  16.312  1.00 49.94           C  
+ANISOU 6940  CB  ALA C  29     6479   7386   5108    599   2183     13       C  
+ATOM   6941  N   GLY C  30     -27.572  46.118  16.467  1.00 70.85           N  
+ANISOU 6941  N   GLY C  30     8927  10164   7827    810   2483   -147       N  
+ATOM   6942  CA  GLY C  30     -28.845  46.409  17.102  1.00 59.80           C  
+ANISOU 6942  CA  GLY C  30     7436   8913   6371    915   2690   -130       C  
+ATOM   6943  C   GLY C  30     -30.035  46.243  16.175  1.00 59.30           C  
+ANISOU 6943  C   GLY C  30     7156   8831   6543    865   2758    -20       C  
+ATOM   6944  O   GLY C  30     -31.123  45.864  16.609  1.00 59.88           O  
+ANISOU 6944  O   GLY C  30     7099   9046   6608    884   2939    102       O  
+ATOM   6945  N   LEU C  31     -29.830  46.528  14.893  1.00 65.09           N  
+ANISOU 6945  N   LEU C  31     7848   9397   7487    799   2611    -54       N  
+ATOM   6946  CA  LEU C  31     -30.903  46.432  13.908  1.00 57.96           C  
+ANISOU 6946  CA  LEU C  31     6751   8460   6812    749   2629     37       C  
+ATOM   6947  C   LEU C  31     -31.313  44.982  13.649  1.00 52.84           C  
+ANISOU 6947  C   LEU C  31     6007   7835   6233    588   2645    259       C  
+ATOM   6948  O   LEU C  31     -32.426  44.717  13.198  1.00 66.78           O  
+ANISOU 6948  O   LEU C  31     7587   9628   8157    543   2698    370       O  
+ATOM   6949  CB  LEU C  31     -30.484  47.100  12.596  1.00 49.71           C  
+ANISOU 6949  CB  LEU C  31     5720   7228   5941    722   2453    -53       C  
+ATOM   6950  CG  LEU C  31     -31.610  47.360  11.592  1.00 48.69           C  
+ANISOU 6950  CG  LEU C  31     5408   7060   6032    713   2447     -1       C  
+ATOM   6951  CD1 LEU C  31     -32.553  48.427  12.122  1.00 53.53           C  
+ANISOU 6951  CD1 LEU C  31     5927   7759   6653    889   2582    -87       C  
+ATOM   6952  CD2 LEU C  31     -31.053  47.757  10.233  1.00 55.87           C  
+ANISOU 6952  CD2 LEU C  31     6365   7784   7081    659   2260    -51       C  
+ATOM   6953  N   SER C  32     -30.417  44.046  13.946  1.00 63.23           N  
+ANISOU 6953  N   SER C  32     7449   9132   7445    502   2588    326       N  
+ATOM   6954  CA  SER C  32     -30.700  42.629  13.744  1.00 61.45           C  
+ANISOU 6954  CA  SER C  32     7167   8897   7285    348   2587    532       C  
+ATOM   6955  C   SER C  32     -31.362  42.020  14.977  1.00 58.08           C  
+ANISOU 6955  C   SER C  32     6690   8652   6725    357   2782    680       C  
+ATOM   6956  O   SER C  32     -31.587  40.811  15.042  1.00 65.85           O  
+ANISOU 6956  O   SER C  32     7642   9636   7744    227   2799    870       O  
+ATOM   6957  CB  SER C  32     -29.416  41.868  13.407  1.00 62.14           C  
+ANISOU 6957  CB  SER C  32     7413   8858   7340    263   2430    544       C  
+ATOM   6958  OG  SER C  32     -28.714  42.493  12.345  1.00 58.95           O  
+ANISOU 6958  OG  SER C  32     7061   8307   7032    269   2276    412       O  
+HETATM 6959  N   MSE C  33     -31.674  42.869  15.951  1.00 53.16           N  
+ANISOU 6959  N   MSE C  33     6072   8178   5947    514   2934    592       N  
+HETATM 6960  CA  MSE C  33     -32.320  42.431  17.182  1.00 63.54           C  
+ANISOU 6960  CA  MSE C  33     7348   9694   7100    552   3153    726       C  
+HETATM 6961  C   MSE C  33     -33.746  42.968  17.276  1.00 75.07           C  
+ANISOU 6961  C   MSE C  33     8585  11284   8656    630   3345    757       C  
+HETATM 6962  O   MSE C  33     -34.026  44.088  16.846  1.00 75.15           O  
+ANISOU 6962  O   MSE C  33     8542  11261   8750    744   3329    596       O  
+HETATM 6963  CB  MSE C  33     -31.510  42.879  18.401  1.00 73.71           C  
+ANISOU 6963  CB  MSE C  33     8847  11080   8078    690   3194    607       C  
+HETATM 6964  CG  MSE C  33     -30.068  42.395  18.407  1.00 67.72           C  
+ANISOU 6964  CG  MSE C  33     8291  10213   7226    629   3001    579       C  
+HETATM 6965 SE   MSE C  33     -29.944  40.453  18.436  1.00200.79          SE  
+ANISOU 6965 SE   MSE C  33    25145  27035  24111    428   2982    886      SE  
+HETATM 6966  CE  MSE C  33     -28.063  40.246  18.899  1.00 78.37           C  
+ANISOU 6966  CE  MSE C  33     9914  11459   8405    455   2777    796       C  
+ATOM   6967  N   SER C  34     -34.645  42.165  17.837  1.00 80.66           N  
+ANISOU 6967  N   SER C  34     9150  12134   9362    572   3529    977       N  
+ATOM   6968  CA  SER C  34     -36.031  42.581  18.015  1.00 69.77           C  
+ANISOU 6968  CA  SER C  34     7524  10903   8080    647   3734   1035       C  
+ATOM   6969  C   SER C  34     -36.137  43.680  19.066  1.00 70.52           C  
+ANISOU 6969  C   SER C  34     7715  11125   7955    865   3843    839       C  
+ATOM   6970  O   SER C  34     -36.960  44.588  18.948  1.00 86.52           O  
+ANISOU 6970  O   SER C  34     9606  13192  10078    985   3908    741       O  
+ATOM   6971  CB  SER C  34     -36.907  41.391  18.408  1.00 73.90           C  
+ANISOU 6971  CB  SER C  34     7897  11509   8672    482   3822   1297       C  
+ATOM   6972  OG  SER C  34     -36.990  40.449  17.354  1.00 84.55           O  
+ANISOU 6972  OG  SER C  34     9135  12721  10268    276   3707   1467       O  
+ATOM   6973  N   VAL C  35     -35.300  43.589  20.094  1.00 74.04           N  
+ANISOU 6973  N   VAL C  35     8399  11628   8106    920   3854    783       N  
+ATOM   6974  CA  VAL C  35     -35.286  44.584  21.159  1.00 75.73           C  
+ANISOU 6974  CA  VAL C  35     8743  11948   8081   1120   3940    586       C  
+ATOM   6975  C   VAL C  35     -34.528  45.842  20.740  1.00 79.77           C  
+ANISOU 6975  C   VAL C  35     9392  12342   8573   1268   3822    312       C  
+ATOM   6976  O   VAL C  35     -34.587  46.864  21.422  1.00 99.35           O  
+ANISOU 6976  O   VAL C  35    11971  14870  10909   1444   3868    112       O  
+ATOM   6977  CB  VAL C  35     -34.664  44.020  22.451  1.00 79.05           C  
+ANISOU 6977  CB  VAL C  35     9380  12474   8180   1123   3978    629       C  
+ATOM   6978  CG1 VAL C  35     -35.551  42.927  23.034  1.00 68.14           C  
+ANISOU 6978  CG1 VAL C  35     7869  11217   6804   1002   4126    891       C  
+ATOM   6979  CG2 VAL C  35     -33.259  43.502  22.184  1.00 72.01           C  
+ANISOU 6979  CG2 VAL C  35     8682  11472   7205   1050   3805    638       C  
+ATOM   6980  N   GLY C  36     -33.819  45.763  19.618  1.00 72.31           N  
+ANISOU 6980  N   GLY C  36     8462  11230   7781   1189   3664    301       N  
+ATOM   6981  CA  GLY C  36     -33.183  46.933  19.040  1.00 70.74           C  
+ANISOU 6981  CA  GLY C  36     8369  10865   7644   1270   3487     51       C  
+ATOM   6982  C   GLY C  36     -31.756  47.212  19.477  1.00 71.83           C  
+ANISOU 6982  C   GLY C  36     8782  10926   7584   1288   3320   -111       C  
+ATOM   6983  O   GLY C  36     -31.156  48.193  19.038  1.00 64.12           O  
+ANISOU 6983  O   GLY C  36     7897   9803   6664   1339   3166   -311       O  
+ATOM   6984  N   TYR C  37     -31.204  46.363  20.338  1.00 77.78           N  
+ANISOU 6984  N   TYR C  37     9663  11775   8116   1243   3339    -15       N  
+ATOM   6985  CA  TYR C  37     -29.845  46.580  20.829  1.00 74.15           C  
+ANISOU 6985  CA  TYR C  37     9450  11259   7466   1261   3166   -156       C  
+ATOM   6986  C   TYR C  37     -29.122  45.276  21.155  1.00 78.08           C  
+ANISOU 6986  C   TYR C  37    10027  11781   7860   1127   3100     25       C  
+ATOM   6987  O   TYR C  37     -29.737  44.210  21.217  1.00 80.82           O  
+ANISOU 6987  O   TYR C  37    10265  12206   8237   1036   3220    260       O  
+ATOM   6988  CB  TYR C  37     -29.871  47.472  22.072  1.00 67.13           C  
+ANISOU 6988  CB  TYR C  37     8724  10499   6284   1470   3267   -340       C  
+ATOM   6989  CG  TYR C  37     -30.568  46.838  23.256  1.00 70.84           C  
+ANISOU 6989  CG  TYR C  37     9198  11206   6512   1528   3504   -195       C  
+ATOM   6990  CD1 TYR C  37     -31.950  46.885  23.380  1.00 68.07           C  
+ANISOU 6990  CD1 TYR C  37     8648  10946   6268   1545   3685   -118       C  
+ATOM   6991  CD2 TYR C  37     -29.843  46.190  24.248  1.00 75.72           C  
+ANISOU 6991  CD2 TYR C  37    10004  11917   6850   1511   3469   -136       C  
+ATOM   6992  CE1 TYR C  37     -32.590  46.304  24.456  1.00 74.71           C  
+ANISOU 6992  CE1 TYR C  37     9479  11962   6945   1540   3843     14       C  
+ATOM   6993  CE2 TYR C  37     -30.475  45.607  25.329  1.00 66.30           C  
+ANISOU 6993  CE2 TYR C  37     8813  10893   5485   1507   3618     -1       C  
+ATOM   6994  CZ  TYR C  37     -31.849  45.667  25.428  1.00 73.94           C  
+ANISOU 6994  CZ  TYR C  37     9582  11945   6566   1519   3813     74       C  
+ATOM   6995  OH  TYR C  37     -32.484  45.089  26.502  1.00 85.73           O  
+ANISOU 6995  OH  TYR C  37    11075  13608   7890   1515   3977    216       O  
+ATOM   6996  N   VAL C  38     -27.811  45.375  21.363  1.00 70.54           N  
+ANISOU 6996  N   VAL C  38     9256  10750   6798   1115   2900    -80       N  
+ATOM   6997  CA  VAL C  38     -26.990  44.225  21.733  1.00 72.01           C  
+ANISOU 6997  CA  VAL C  38     9535  10948   6875   1017   2813     72       C  
+ATOM   6998  C   VAL C  38     -26.194  44.455  23.020  1.00 72.50           C  
+ANISOU 6998  C   VAL C  38     9825  11115   6605   1121   2759    -27       C  
+ATOM   6999  O   VAL C  38     -25.456  45.436  23.134  1.00 82.93           O  
+ANISOU 6999  O   VAL C  38    11264  12370   7876   1191   2610   -254       O  
+ATOM   7000  CB  VAL C  38     -26.003  43.863  20.610  1.00 74.09           C  
+ANISOU 7000  CB  VAL C  38     9782  11009   7361    879   2584     81       C  
+ATOM   7001  CG1 VAL C  38     -25.138  42.684  21.024  1.00 73.26           C  
+ANISOU 7001  CG1 VAL C  38     9773  10911   7151    803   2493    234       C  
+ATOM   7002  CG2 VAL C  38     -26.755  43.543  19.335  1.00 77.23           C  
+ANISOU 7002  CG2 VAL C  38     9984  11303   8056    773   2615    181       C  
+ATOM   7003  N   SER C  39     -26.345  43.555  23.986  1.00 72.50           N  
+ANISOU 7003  N   SER C  39     9894  11272   6380   1126   2869    149       N  
+ATOM   7004  CA  SER C  39     -25.535  43.608  25.199  1.00 81.71           C  
+ANISOU 7004  CA  SER C  39    11291  12542   7212   1214   2792     85       C  
+ATOM   7005  C   SER C  39     -24.227  42.863  24.940  1.00 88.07           C  
+ANISOU 7005  C   SER C  39    12162  13231   8071   1102   2542    153       C  
+ATOM   7006  O   SER C  39     -24.153  41.641  25.072  1.00 93.12           O  
+ANISOU 7006  O   SER C  39    12794  13893   8694   1017   2560    390       O  
+ATOM   7007  CB  SER C  39     -26.286  43.011  26.390  1.00 84.76           C  
+ANISOU 7007  CB  SER C  39    11736  13162   7305   1285   3032    256       C  
+ATOM   7008  OG  SER C  39     -25.463  42.959  27.543  1.00107.13           O  
+ANISOU 7008  OG  SER C  39    14812  16097   9795   1365   2934    213       O  
+ATOM   7009  N   TRP C  40     -23.204  43.620  24.559  1.00 79.65           N  
+ANISOU 7009  N   TRP C  40    11149  12031   7082   1103   2310    -49       N  
+ATOM   7010  CA  TRP C  40     -21.937  43.076  24.071  1.00 84.34           C  
+ANISOU 7010  CA  TRP C  40    11753  12494   7799   1002   2071     -7       C  
+ATOM   7011  C   TRP C  40     -21.218  42.148  25.056  1.00 81.17           C  
+ANISOU 7011  C   TRP C  40    11494  12186   7159   1008   1988    132       C  
+ATOM   7012  O   TRP C  40     -20.538  41.209  24.639  1.00 70.49           O  
+ANISOU 7012  O   TRP C  40    10108  10748   5928    919   1875    277       O  
+ATOM   7013  CB  TRP C  40     -21.022  44.224  23.649  1.00 83.26           C  
+ANISOU 7013  CB  TRP C  40    11642  12225   7767   1014   1859   -255       C  
+ATOM   7014  CG  TRP C  40     -21.545  44.920  22.427  1.00 76.30           C  
+ANISOU 7014  CG  TRP C  40    10608  11207   7174    977   1904   -338       C  
+ATOM   7015  CD1 TRP C  40     -22.253  46.085  22.390  1.00 71.16           C  
+ANISOU 7015  CD1 TRP C  40     9949  10552   6537   1064   1988   -513       C  
+ATOM   7016  CD2 TRP C  40     -21.429  44.477  21.066  1.00 71.52           C  
+ANISOU 7016  CD2 TRP C  40     9849  10451   6874    856   1866   -245       C  
+ATOM   7017  NE1 TRP C  40     -22.576  46.403  21.093  1.00 66.12           N  
+ANISOU 7017  NE1 TRP C  40     9156   9769   6196    999   1995   -522       N  
+ATOM   7018  CE2 TRP C  40     -22.081  45.433  20.260  1.00 67.27           C  
+ANISOU 7018  CE2 TRP C  40     9217   9829   6513    869   1922   -362       C  
+ATOM   7019  CE3 TRP C  40     -20.831  43.372  20.451  1.00 63.75           C  
+ANISOU 7019  CE3 TRP C  40     8811   9390   6020    751   1789    -80       C  
+ATOM   7020  CZ2 TRP C  40     -22.152  45.318  18.872  1.00 69.85           C  
+ANISOU 7020  CZ2 TRP C  40     9406  10012   7123    775   1898   -313       C  
+ATOM   7021  CZ3 TRP C  40     -20.904  43.259  19.070  1.00 59.85           C  
+ANISOU 7021  CZ3 TRP C  40     8186   8749   5805    664   1775    -48       C  
+ATOM   7022  CH2 TRP C  40     -21.559  44.227  18.298  1.00 62.78           C  
+ANISOU 7022  CH2 TRP C  40     8473   9052   6329    673   1827   -161       C  
+ATOM   7023  N   ALA C  41     -21.350  42.422  26.351  1.00 74.55           N  
+ANISOU 7023  N   ALA C  41    10827  11522   5979   1127   2038     84       N  
+ATOM   7024  CA  ALA C  41     -20.764  41.562  27.381  1.00 69.27           C  
+ANISOU 7024  CA  ALA C  41    10312  10963   5043   1148   1967    230       C  
+ATOM   7025  C   ALA C  41     -21.308  40.136  27.276  1.00 77.82           C  
+ANISOU 7025  C   ALA C  41    11320  12069   6178   1061   2115    553       C  
+ATOM   7026  O   ALA C  41     -20.542  39.163  27.249  1.00 93.28           O  
+ANISOU 7026  O   ALA C  41    13303  13969   8170   1000   1979    711       O  
+ATOM   7027  CB  ALA C  41     -21.033  42.133  28.765  1.00 72.76           C  
+ANISOU 7027  CB  ALA C  41    10961  11606   5079   1303   2038    125       C  
+ATOM   7028  N   LYS C  42     -22.632  40.021  27.216  1.00 75.08           N  
+ANISOU 7028  N   LYS C  42    10874  11799   5854   1057   2389    652       N  
+ATOM   7029  CA  LYS C  42     -23.292  38.725  27.101  1.00 80.60           C  
+ANISOU 7029  CA  LYS C  42    11486  12508   6629    955   2542    962       C  
+ATOM   7030  C   LYS C  42     -22.846  38.026  25.820  1.00 84.39           C  
+ANISOU 7030  C   LYS C  42    11835  12762   7468    810   2403   1041       C  
+ATOM   7031  O   LYS C  42     -22.810  36.798  25.748  1.00 76.33           O  
+ANISOU 7031  O   LYS C  42    10805  11689   6509    720   2404   1281       O  
+ATOM   7032  CB  LYS C  42     -24.813  38.888  27.118  1.00 82.53           C  
+ANISOU 7032  CB  LYS C  42    11599  12864   6893    965   2849   1032       C  
+ATOM   7033  N   LEU C  43     -22.511  38.825  24.812  1.00 88.26           N  
+ANISOU 7033  N   LEU C  43    12236  13112   8186    793   2288    837       N  
+ATOM   7034  CA  LEU C  43     -21.989  38.312  23.553  1.00 87.48           C  
+ANISOU 7034  CA  LEU C  43    12032  12805   8402    681   2152    871       C  
+ATOM   7035  C   LEU C  43     -20.603  37.721  23.785  1.00 84.24           C  
+ANISOU 7035  C   LEU C  43    11727  12336   7945    684   1928    912       C  
+ATOM   7036  O   LEU C  43     -20.241  36.707  23.191  1.00 84.91           O  
+ANISOU 7036  O   LEU C  43    11775  12291   8196    606   1862   1058       O  
+ATOM   7037  CB  LEU C  43     -21.937  39.413  22.491  1.00 75.88           C  
+ANISOU 7037  CB  LEU C  43    10459  11221   7152    677   2092    646       C  
+ATOM   7038  N   LEU C  44     -19.823  38.377  24.640  1.00 73.19           N  
+ANISOU 7038  N   LEU C  44    10459  11024   6326    780   1801    774       N  
+ATOM   7039  CA  LEU C  44     -18.479  37.911  24.967  1.00 74.46           C  
+ANISOU 7039  CA  LEU C  44    10708  11151   6433    797   1570    806       C  
+ATOM   7040  C   LEU C  44     -18.504  36.665  25.858  1.00 83.40           C  
+ANISOU 7040  C   LEU C  44    11950  12363   7374    803   1602   1069       C  
+ATOM   7041  O   LEU C  44     -17.535  35.905  25.901  1.00 86.92           O  
+ANISOU 7041  O   LEU C  44    12434  12743   7850    799   1432   1171       O  
+ATOM   7042  CB  LEU C  44     -17.686  39.029  25.653  1.00 78.94           C  
+ANISOU 7042  CB  LEU C  44    11382  11789   6822    888   1400    576       C  
+ATOM   7043  CG  LEU C  44     -16.238  38.738  26.059  1.00 80.82           C  
+ANISOU 7043  CG  LEU C  44    11692  12009   7004    912   1127    582       C  
+ATOM   7044  CD1 LEU C  44     -15.366  38.533  24.830  1.00 79.65           C  
+ANISOU 7044  CD1 LEU C  44    11390  11674   7198    840    990    573       C  
+ATOM   7045  CD2 LEU C  44     -15.681  39.845  26.945  1.00 74.89           C  
+ANISOU 7045  CD2 LEU C  44    11072  11354   6030    995    968    359       C  
+ATOM   7046  N   GLU C  45     -19.616  36.451  26.558  1.00 78.31           N  
+ANISOU 7046  N   GLU C  45    11349  11860   6545    817   1827   1191       N  
+ATOM   7047  CA  GLU C  45     -19.719  35.343  27.516  1.00 80.32           C  
+ANISOU 7047  CA  GLU C  45    11725  12208   6586    825   1880   1458       C  
+ATOM   7048  C   GLU C  45     -19.474  33.917  26.970  1.00 77.97           C  
+ANISOU 7048  C   GLU C  45    11384  11746   6496    725   1831   1709       C  
+ATOM   7049  O   GLU C  45     -18.822  33.122  27.647  1.00 64.15           O  
+ANISOU 7049  O   GLU C  45     9757  10011   4606    756   1723   1869       O  
+ATOM   7050  CB  GLU C  45     -21.085  35.382  28.213  1.00 74.54           C  
+ANISOU 7050  CB  GLU C  45    11006  11654   5660    843   2176   1564       C  
+ATOM   7051  CG  GLU C  45     -21.173  36.420  29.320  1.00 79.61           C  
+ANISOU 7051  CG  GLU C  45    11798  12507   5943    990   2220   1391       C  
+ATOM   7052  CD  GLU C  45     -22.462  36.327  30.110  1.00 95.51           C  
+ANISOU 7052  CD  GLU C  45    13834  14722   7735   1030   2537   1530       C  
+ATOM   7053  OE1 GLU C  45     -23.289  35.443  29.802  1.00 95.40           O  
+ANISOU 7053  OE1 GLU C  45    13699  14681   7866    923   2714   1777       O  
+ATOM   7054  OE2 GLU C  45     -22.646  37.134  31.045  1.00110.92           O  
+ANISOU 7054  OE2 GLU C  45    15922  16858   9366   1169   2609   1392       O  
+ATOM   7055  N   PRO C  46     -19.990  33.575  25.769  1.00 79.46           N  
+ANISOU 7055  N   PRO C  46    11412  11771   7008    614   1899   1742       N  
+ATOM   7056  CA  PRO C  46     -19.720  32.219  25.262  1.00 77.05           C  
+ANISOU 7056  CA  PRO C  46    11095  11288   6893    532   1836   1958       C  
+ATOM   7057  C   PRO C  46     -18.237  31.877  25.095  1.00 84.12           C  
+ANISOU 7057  C   PRO C  46    12044  12072   7846    585   1576   1928       C  
+ATOM   7058  O   PRO C  46     -17.893  30.707  24.930  1.00 78.98           O  
+ANISOU 7058  O   PRO C  46    11426  11289   7296    555   1511   2116       O  
+ATOM   7059  CB  PRO C  46     -20.415  32.217  23.900  1.00 79.21           C  
+ANISOU 7059  CB  PRO C  46    11198  11406   7493    421   1911   1912       C  
+ATOM   7060  CG  PRO C  46     -21.544  33.148  24.075  1.00 92.18           C  
+ANISOU 7060  CG  PRO C  46    12765  13195   9065    424   2108   1821       C  
+ATOM   7061  CD  PRO C  46     -21.019  34.250  24.956  1.00 91.44           C  
+ANISOU 7061  CD  PRO C  46    12772  13268   8702    560   2056   1630       C  
+ATOM   7062  N   ILE C  47     -17.378  32.889  25.137  1.00 89.35           N  
+ANISOU 7062  N   ILE C  47    12709  12781   8460    665   1427   1697       N  
+ATOM   7063  CA  ILE C  47     -15.938  32.682  25.124  1.00 85.54           C  
+ANISOU 7063  CA  ILE C  47    12255  12231   8015    727   1178   1668       C  
+ATOM   7064  C   ILE C  47     -15.409  32.826  26.554  1.00 92.30           C  
+ANISOU 7064  C   ILE C  47    13275  13265   8529    826   1069   1695       C  
+ATOM   7065  O   ILE C  47     -14.387  32.249  26.925  1.00101.87           O  
+ANISOU 7065  O   ILE C  47    14548  14454   9705    882    877   1783       O  
+ATOM   7066  CB  ILE C  47     -15.238  33.683  24.183  1.00 89.24           C  
+ANISOU 7066  CB  ILE C  47    12600  12623   8685    732   1062   1412       C  
+ATOM   7067  CG1 ILE C  47     -15.797  33.562  22.763  1.00 80.55           C  
+ANISOU 7067  CG1 ILE C  47    11359  11358   7888    642   1170   1386       C  
+ATOM   7068  CG2 ILE C  47     -13.747  33.451  24.167  1.00 93.07           C  
+ANISOU 7068  CG2 ILE C  47    13079  13051   9233    794    816   1400       C  
+ATOM   7069  CD1 ILE C  47     -15.582  32.202  22.138  1.00 67.37           C  
+ANISOU 7069  CD1 ILE C  47     9680   9513   6404    608   1147   1570       C  
+ATOM   7070  N   ALA C  48     -16.141  33.595  27.352  1.00 93.49           N  
+ANISOU 7070  N   ALA C  48    13502  13596   8423    858   1193   1618       N  
+ATOM   7071  CA  ALA C  48     -15.832  33.827  28.762  1.00 87.62           C  
+ANISOU 7071  CA  ALA C  48    12947  13046   7300    960   1116   1624       C  
+ATOM   7072  C   ALA C  48     -16.407  32.757  29.696  1.00 97.75           C  
+ANISOU 7072  C   ALA C  48    14366  14424   8352    966   1246   1926       C  
+ATOM   7073  O   ALA C  48     -16.125  32.760  30.894  1.00 84.83           O  
+ANISOU 7073  O   ALA C  48    12910  12948   6373   1056   1179   1976       O  
+ATOM   7074  CB  ALA C  48     -16.330  35.203  29.181  1.00 91.18           C  
+ANISOU 7074  CB  ALA C  48    13437  13641   7565   1013   1194   1378       C  
+ATOM   7075  N   GLN C  49     -17.208  31.846  29.150  1.00107.19           N  
+ANISOU 7075  N   GLN C  49    15482  15515   9729    867   1422   2132       N  
+ATOM   7076  CA  GLN C  49     -17.881  30.828  29.960  1.00 92.36           C  
+ANISOU 7076  CA  GLN C  49    13713  13712   7670    845   1575   2445       C  
+ATOM   7077  C   GLN C  49     -16.970  29.763  30.575  1.00 97.11           C  
+ANISOU 7077  C   GLN C  49    14454  14273   8170    890   1388   2668       C  
+ATOM   7078  O   GLN C  49     -17.318  29.185  31.605  1.00113.24           O  
+ANISOU 7078  O   GLN C  49    16647  16439   9941    913   1474   2900       O  
+ATOM   7079  CB  GLN C  49     -18.961  30.138  29.122  1.00 85.33           C  
+ANISOU 7079  CB  GLN C  49    12682  12689   7052    702   1784   2602       C  
+ATOM   7080  CG  GLN C  49     -20.325  30.800  29.220  1.00 96.62           C  
+ANISOU 7080  CG  GLN C  49    14034  14261   8417    669   2068   2559       C  
+ATOM   7081  CD  GLN C  49     -21.208  30.502  28.025  1.00 98.15           C  
+ANISOU 7081  CD  GLN C  49    14028  14294   8970    524   2196   2596       C  
+ATOM   7082  OE1 GLN C  49     -20.859  29.692  27.167  1.00103.32           O  
+ANISOU 7082  OE1 GLN C  49    14631  14725   9901    443   2086   2671       O  
+ATOM   7083  NE2 GLN C  49     -22.361  31.157  27.965  1.00 94.39           N  
+ANISOU 7083  NE2 GLN C  49    13443  13930   8490    500   2423   2538       N  
+ATOM   7084  N   GLU C  50     -15.819  29.492  29.968  1.00 90.45           N  
+ANISOU 7084  N   GLU C  50    13561  13265   7541    912   1143   2614       N  
+ATOM   7085  CA  GLU C  50     -14.895  28.531  30.566  1.00 88.91           C  
+ANISOU 7085  CA  GLU C  50    13491  13032   7260    978    946   2817       C  
+ATOM   7086  C   GLU C  50     -14.181  29.173  31.755  1.00 93.83           C  
+ANISOU 7086  C   GLU C  50    14271  13865   7517   1106    772   2729       C  
+ATOM   7087  O   GLU C  50     -14.485  28.869  32.909  1.00 97.49           O  
+ANISOU 7087  O   GLU C  50    14917  14488   7636   1153    826   2904       O  
+ATOM   7088  CB  GLU C  50     -13.879  28.013  29.539  1.00 73.07           C  
+ANISOU 7088  CB  GLU C  50    11369  10789   5606    982    750   2790       C  
+ATOM   7089  CG  GLU C  50     -13.386  29.031  28.518  1.00 81.27           C  
+ANISOU 7089  CG  GLU C  50    12234  11767   6877    978    671   2478       C  
+ATOM   7090  CD  GLU C  50     -14.261  29.096  27.283  1.00 82.21           C  
+ANISOU 7090  CD  GLU C  50    12205  11749   7283    862    862   2412       C  
+ATOM   7091  OE1 GLU C  50     -15.404  28.595  27.331  1.00 94.65           O  
+ANISOU 7091  OE1 GLU C  50    13801  13317   8846    777   1071   2570       O  
+ATOM   7092  OE2 GLU C  50     -13.799  29.638  26.258  1.00 86.80           O  
+ANISOU 7092  OE2 GLU C  50    12645  12232   8105    854    797   2212       O  
+ATOM   7093  N   ILE C  51     -13.233  30.057  31.467  1.00 95.60           N  
+ANISOU 7093  N   ILE C  51    14425  14085   7813   1157    557   2464       N  
+ATOM   7094  CA  ILE C  51     -12.549  30.828  32.496  1.00 94.50           C  
+ANISOU 7094  CA  ILE C  51    14421  14129   7356   1263    358   2327       C  
+ATOM   7095  C   ILE C  51     -12.688  32.314  32.186  1.00 90.59           C  
+ANISOU 7095  C   ILE C  51    13853  13692   6877   1255    373   1980       C  
+ATOM   7096  O   ILE C  51     -12.179  32.793  31.173  1.00 88.05           O  
+ANISOU 7096  O   ILE C  51    13352  13236   6868   1214    283   1803       O  
+ATOM   7097  CB  ILE C  51     -11.059  30.454  32.599  1.00 99.32           C  
+ANISOU 7097  CB  ILE C  51    15022  14675   8039   1337     12   2354       C  
+ATOM   7098  N   GLY C  52     -13.389  33.038  33.053  1.00 99.77           N  
+ANISOU 7098  N   GLY C  52    15160  15049   7699   1300    496   1889       N  
+ATOM   7099  CA  GLY C  52     -13.593  34.463  32.864  1.00 91.50           C  
+ANISOU 7099  CA  GLY C  52    14076  14049   6643   1308    515   1560       C  
+ATOM   7100  C   GLY C  52     -12.796  35.313  33.834  1.00 93.64           C  
+ANISOU 7100  C   GLY C  52    14511  14453   6616   1406    256   1363       C  
+ATOM   7101  O   GLY C  52     -11.731  34.909  34.300  1.00 91.23           O  
+ANISOU 7101  O   GLY C  52    14267  14155   6241   1451    -24   1432       O  
+ATOM   7102  N   ASN C  59      -6.398  41.190  32.003  1.00100.91           N  
+ANISOU 7102  N   ASN C  59    14819  14908   8614   1199  -1518   -106       N  
+ATOM   7103  CA  ASN C  59      -5.512  40.284  32.723  1.00106.85           C  
+ANISOU 7103  CA  ASN C  59    15612  15743   9245   1259  -1761     76       C  
+ATOM   7104  C   ASN C  59      -5.537  38.876  32.137  1.00112.55           C  
+ANISOU 7104  C   ASN C  59    16206  16415  10142   1273  -1605    382       C  
+ATOM   7105  O   ASN C  59      -4.528  38.382  31.636  1.00113.15           O  
+ANISOU 7105  O   ASN C  59    16084  16414  10494   1258  -1767    486       O  
+ATOM   7106  CB  ASN C  59      -5.888  40.238  34.205  1.00104.77           C  
+ANISOU 7106  CB  ASN C  59    15681  15670   8457   1368  -1821     70       C  
+ATOM   7107  N   ASP C  60      -6.699  38.236  32.208  1.00118.42           N  
+ANISOU 7107  N   ASP C  60    17062  17198  10733   1305  -1290    526       N  
+ATOM   7108  CA  ASP C  60      -6.896  36.914  31.625  1.00112.29           C  
+ANISOU 7108  CA  ASP C  60    16192  16347  10125   1307  -1120    805       C  
+ATOM   7109  C   ASP C  60      -7.236  37.035  30.142  1.00110.16           C  
+ANISOU 7109  C   ASP C  60    15695  15908  10253   1217   -911    765       C  
+ATOM   7110  O   ASP C  60      -7.193  36.056  29.397  1.00107.03           O  
+ANISOU 7110  O   ASP C  60    15181  15405  10082   1207   -812    949       O  
+ATOM   7111  CB  ASP C  60      -8.001  36.158  32.367  1.00114.18           C  
+ANISOU 7111  CB  ASP C  60    16647  16696  10039   1360   -884    994       C  
+ATOM   7112  CG  ASP C  60      -7.739  34.667  32.442  1.00117.50           C  
+ANISOU 7112  CG  ASP C  60    17070  17081  10494   1399   -892   1316       C  
+ATOM   7113  OD1 ASP C  60      -6.853  34.179  31.709  1.00120.83           O  
+ANISOU 7113  OD1 ASP C  60    17305  17371  11235   1390  -1020   1384       O  
+ATOM   7114  OD2 ASP C  60      -8.419  33.982  33.236  1.00118.63           O  
+ANISOU 7114  OD2 ASP C  60    17404  17324  10347   1445   -762   1508       O  
+ATOM   7115  N   LEU C  61      -7.575  38.251  29.728  1.00108.40           N  
+ANISOU 7115  N   LEU C  61    15428  15654  10104   1158   -854    521       N  
+ATOM   7116  CA  LEU C  61      -8.016  38.529  28.364  1.00102.21           C  
+ANISOU 7116  CA  LEU C  61    14457  14726   9652   1075   -652    465       C  
+ATOM   7117  C   LEU C  61      -6.891  38.438  27.332  1.00101.38           C  
+ANISOU 7117  C   LEU C  61    14103  14484   9931   1030   -789    474       C  
+ATOM   7118  O   LEU C  61      -7.146  38.199  26.151  1.00 98.92           O  
+ANISOU 7118  O   LEU C  61    13644  14051   9892    983   -616    513       O  
+ATOM   7119  CB  LEU C  61      -8.662  39.915  28.302  1.00104.41           C  
+ANISOU 7119  CB  LEU C  61    14777  15009   9885   1040   -574    204       C  
+ATOM   7120  CG  LEU C  61      -9.854  40.124  29.239  1.00101.33           C  
+ANISOU 7120  CG  LEU C  61    14615  14759   9126   1103   -394    171       C  
+ATOM   7121  CD1 LEU C  61     -10.520  41.468  28.983  1.00 95.37           C  
+ANISOU 7121  CD1 LEU C  61    13873  13976   8388   1082   -295    -87       C  
+ATOM   7122  CD2 LEU C  61     -10.857  38.987  29.102  1.00 99.69           C  
+ANISOU 7122  CD2 LEU C  61    14427  14572   8880   1111   -110    415       C  
+ATOM   7123  N   VAL C  62      -5.653  38.630  27.777  1.00107.83           N  
+ANISOU 7123  N   VAL C  62    14872  15332  10768   1048  -1098    440       N  
+ATOM   7124  CA  VAL C  62      -4.507  38.575  26.875  1.00108.78           C  
+ANISOU 7124  CA  VAL C  62    14733  15347  11252   1015  -1229    458       C  
+ATOM   7125  C   VAL C  62      -4.238  37.142  26.425  1.00104.31           C  
+ANISOU 7125  C   VAL C  62    14087  14723  10824   1077  -1161    708       C  
+ATOM   7126  O   VAL C  62      -3.732  36.918  25.326  1.00105.70           O  
+ANISOU 7126  O   VAL C  62    14054  14785  11320   1060  -1116    743       O  
+ATOM   7127  CB  VAL C  62      -3.233  39.149  27.526  1.00 99.90           C  
+ANISOU 7127  CB  VAL C  62    13552  14277  10128   1013  -1599    367       C  
+ATOM   7128  CG1 VAL C  62      -3.346  40.660  27.670  1.00103.28           C  
+ANISOU 7128  CG1 VAL C  62    14015  14701  10525    930  -1682     94       C  
+ATOM   7129  CG2 VAL C  62      -2.971  38.492  28.869  1.00 92.37           C  
+ANISOU 7129  CG2 VAL C  62    12786  13460   8850   1111  -1791    482       C  
+ATOM   7130  N   SER C  63      -4.580  36.177  27.274  1.00 92.16           N  
+ANISOU 7130  N   SER C  63    12726  13255   9037   1155  -1148    884       N  
+ATOM   7131  CA  SER C  63      -4.436  34.773  26.914  1.00 94.74           C  
+ANISOU 7131  CA  SER C  63    13015  13502   9479   1218  -1079   1126       C  
+ATOM   7132  C   SER C  63      -5.391  34.440  25.776  1.00 88.89           C  
+ANISOU 7132  C   SER C  63    12229  12632   8911   1165   -767   1155       C  
+ATOM   7133  O   SER C  63      -5.037  33.724  24.837  1.00 83.39           O  
+ANISOU 7133  O   SER C  63    11401  11807   8476   1186   -710   1247       O  
+ATOM   7134  CB  SER C  63      -4.708  33.868  28.119  1.00 97.04           C  
+ANISOU 7134  CB  SER C  63    13532  13891   9450   1300  -1124   1320       C  
+ATOM   7135  OG  SER C  63      -4.150  32.581  27.928  1.00101.84           O  
+ANISOU 7135  OG  SER C  63    14090  14414  10192   1380  -1171   1548       O  
+ATOM   7136  N   LEU C  64      -6.596  34.992  25.858  1.00 83.98           N  
+ANISOU 7136  N   LEU C  64    11717  12048   8143   1104   -572   1065       N  
+ATOM   7137  CA  LEU C  64      -7.596  34.819  24.812  1.00 87.89           C  
+ANISOU 7137  CA  LEU C  64    12169  12434   8792   1040   -295   1072       C  
+ATOM   7138  C   LEU C  64      -7.180  35.530  23.533  1.00 89.06           C  
+ANISOU 7138  C   LEU C  64    12112  12474   9252    985   -277    924       C  
+ATOM   7139  O   LEU C  64      -7.339  34.996  22.434  1.00 85.04           O  
+ANISOU 7139  O   LEU C  64    11511  11835   8964    969   -141    980       O  
+ATOM   7140  CB  LEU C  64      -8.957  35.337  25.276  1.00 91.52           C  
+ANISOU 7140  CB  LEU C  64    12771  12979   9023    999   -105   1009       C  
+ATOM   7141  CG  LEU C  64     -10.040  35.382  24.196  1.00 83.37           C  
+ANISOU 7141  CG  LEU C  64    11673  11847   8157    922    157    987       C  
+ATOM   7142  CD1 LEU C  64     -10.306  33.989  23.647  1.00 76.81           C  
+ANISOU 7142  CD1 LEU C  64    10833  10895   7455    919    264   1204       C  
+ATOM   7143  CD2 LEU C  64     -11.310  36.008  24.746  1.00 78.56           C  
+ANISOU 7143  CD2 LEU C  64    11177  11345   7327    899    330    916       C  
+ATOM   7144  N   ALA C  65      -6.653  36.741  23.687  1.00 90.89           N  
+ANISOU 7144  N   ALA C  65    12284  12754   9494    954   -418    735       N  
+ATOM   7145  CA  ALA C  65      -6.201  37.536  22.553  1.00 89.82           C  
+ANISOU 7145  CA  ALA C  65    11956  12526   9646    892   -410    604       C  
+ATOM   7146  C   ALA C  65      -5.074  36.836  21.803  1.00 90.85           C  
+ANISOU 7146  C   ALA C  65    11902  12574  10041    935   -483    710       C  
+ATOM   7147  O   ALA C  65      -5.022  36.869  20.574  1.00 88.72           O  
+ANISOU 7147  O   ALA C  65    11499  12200  10012    907   -358    694       O  
+ATOM   7148  CB  ALA C  65      -5.754  38.913  23.019  1.00 88.58           C  
+ANISOU 7148  CB  ALA C  65    11782  12427   9448    845   -586    401       C  
+ATOM   7149  N   GLN C  66      -4.174  36.201  22.549  1.00 90.78           N  
+ANISOU 7149  N   GLN C  66    11892  12621   9981   1015   -683    821       N  
+ATOM   7150  CA  GLN C  66      -3.042  35.507  21.946  1.00 94.77           C  
+ANISOU 7150  CA  GLN C  66    12212  13060  10734   1085   -761    929       C  
+ATOM   7151  C   GLN C  66      -3.435  34.127  21.429  1.00 97.04           C  
+ANISOU 7151  C   GLN C  66    12553  13243  11077   1157   -596   1104       C  
+ATOM   7152  O   GLN C  66      -2.762  33.571  20.562  1.00 98.76           O  
+ANISOU 7152  O   GLN C  66    12625  13369  11531   1219   -569   1166       O  
+ATOM   7153  CB  GLN C  66      -1.887  35.386  22.943  1.00 98.33           C  
+ANISOU 7153  CB  GLN C  66    12624  13608  11130   1153  -1064    982       C  
+ATOM   7154  CG  GLN C  66      -1.255  36.715  23.324  1.00106.61           C  
+ANISOU 7154  CG  GLN C  66    13583  14731  12192   1074  -1275    806       C  
+ATOM   7155  CD  GLN C  66      -0.572  37.389  22.150  1.00117.78           C  
+ANISOU 7155  CD  GLN C  66    14732  16071  13947   1011  -1245    727       C  
+ATOM   7156  OE1 GLN C  66      -1.124  38.302  21.535  1.00124.27           O  
+ANISOU 7156  OE1 GLN C  66    15543  16846  14827    911  -1112    589       O  
+ATOM   7157  NE2 GLN C  66       0.635  36.936  21.828  1.00113.87           N  
+ANISOU 7157  NE2 GLN C  66    14016  15567  13681   1076  -1361    827       N  
+ATOM   7158  N   TYR C  67      -4.523  33.574  21.957  1.00 91.46           N  
+ANISOU 7158  N   TYR C  67    12052  12544  10154   1151   -482   1184       N  
+ATOM   7159  CA  TYR C  67      -5.067  32.343  21.394  1.00 80.51           C  
+ANISOU 7159  CA  TYR C  67    10728  11029   8835   1186   -317   1335       C  
+ATOM   7160  C   TYR C  67      -5.693  32.638  20.036  1.00 78.74           C  
+ANISOU 7160  C   TYR C  67    10433  10691   8791   1115   -104   1239       C  
+ATOM   7161  O   TYR C  67      -5.451  31.930  19.059  1.00 81.04           O  
+ANISOU 7161  O   TYR C  67    10662  10851   9279   1160    -28   1291       O  
+ATOM   7162  CB  TYR C  67      -6.103  31.713  22.330  1.00 78.35           C  
+ANISOU 7162  CB  TYR C  67    10679  10795   8297   1175   -248   1465       C  
+ATOM   7163  CG  TYR C  67      -6.766  30.474  21.760  1.00 76.68           C  
+ANISOU 7163  CG  TYR C  67    10539  10428   8168   1182    -86   1620       C  
+ATOM   7164  CD1 TYR C  67      -6.165  29.227  21.874  1.00 77.41           C  
+ANISOU 7164  CD1 TYR C  67    10662  10426   8325   1287   -168   1804       C  
+ATOM   7165  CD2 TYR C  67      -7.991  30.552  21.107  1.00 81.17           C  
+ANISOU 7165  CD2 TYR C  67    11146  10932   8763   1082    132   1582       C  
+ATOM   7166  CE1 TYR C  67      -6.763  28.092  21.353  1.00 75.76           C  
+ANISOU 7166  CE1 TYR C  67    10535  10046   8203   1287    -38   1938       C  
+ATOM   7167  CE2 TYR C  67      -8.597  29.423  20.582  1.00 73.52           C  
+ANISOU 7167  CE2 TYR C  67    10245   9805   7883   1071    253   1717       C  
+ATOM   7168  CZ  TYR C  67      -7.979  28.196  20.709  1.00 74.56           C  
+ANISOU 7168  CZ  TYR C  67    10422   9830   8077   1170    166   1890       C  
+ATOM   7169  OH  TYR C  67      -8.578  27.070  20.190  1.00 76.33           O  
+ANISOU 7169  OH  TYR C  67    10731   9871   8400   1153    269   2016       O  
+ATOM   7170  N   TYR C  68      -6.498  33.693  19.989  1.00 79.30           N  
+ANISOU 7170  N   TYR C  68    10528  10815   8786   1013    -14   1094       N  
+ATOM   7171  CA  TYR C  68      -7.194  34.096  18.774  1.00 84.41           C  
+ANISOU 7171  CA  TYR C  68    11123  11371   9577    940    173   1000       C  
+ATOM   7172  C   TYR C  68      -6.217  34.543  17.687  1.00 87.23           C  
+ANISOU 7172  C   TYR C  68    11286  11669  10188    953    150    920       C  
+ATOM   7173  O   TYR C  68      -6.424  34.271  16.504  1.00 92.75           O  
+ANISOU 7173  O   TYR C  68    11942  12256  11043    949    288    916       O  
+ATOM   7174  CB  TYR C  68      -8.192  35.214  19.089  1.00 81.93           C  
+ANISOU 7174  CB  TYR C  68    10871  11137   9123    849    249    864       C  
+ATOM   7175  CG  TYR C  68      -9.057  35.626  17.921  1.00 70.87           C  
+ANISOU 7175  CG  TYR C  68     9429   9649   7848    775    434    782       C  
+ATOM   7176  CD1 TYR C  68     -10.177  34.883  17.570  1.00 65.72           C  
+ANISOU 7176  CD1 TYR C  68     8859   8929   7183    743    596    867       C  
+ATOM   7177  CD2 TYR C  68      -8.767  36.763  17.179  1.00 72.28           C  
+ANISOU 7177  CD2 TYR C  68     9490   9810   8163    729    434    630       C  
+ATOM   7178  CE1 TYR C  68     -10.976  35.254  16.507  1.00 69.29           C  
+ANISOU 7178  CE1 TYR C  68     9274   9306   7746    677    738    795       C  
+ATOM   7179  CE2 TYR C  68      -9.562  37.143  16.112  1.00 64.28           C  
+ANISOU 7179  CE2 TYR C  68     8452   8720   7253    669    590    567       C  
+ATOM   7180  CZ  TYR C  68     -10.666  36.384  15.781  1.00 64.64           C  
+ANISOU 7180  CZ  TYR C  68     8579   8708   7274    647    735    645       C  
+ATOM   7181  OH  TYR C  68     -11.462  36.754  14.722  1.00 60.36           O  
+ANISOU 7181  OH  TYR C  68     8011   8093   6832    588    864    584       O  
+ATOM   7182  N   CYS C  69      -5.156  35.234  18.094  1.00 82.59           N  
+ANISOU 7182  N   CYS C  69    10583  11162   9637    966    -26    861       N  
+ATOM   7183  CA  CYS C  69      -4.169  35.751  17.151  1.00 91.92           C  
+ANISOU 7183  CA  CYS C  69    11554  12308  11065    967    -47    802       C  
+ATOM   7184  C   CYS C  69      -2.980  34.806  16.987  1.00 88.88           C  
+ANISOU 7184  C   CYS C  69    11049  11894  10826   1092   -131    928       C  
+ATOM   7185  O   CYS C  69      -1.890  35.228  16.599  1.00 84.43           O  
+ANISOU 7185  O   CYS C  69    10281  11350  10447   1110   -207    906       O  
+ATOM   7186  CB  CYS C  69      -3.675  37.128  17.602  1.00 95.78           C  
+ANISOU 7186  CB  CYS C  69    11954  12883  11555    889   -197    665       C  
+ATOM   7187  SG  CYS C  69      -4.928  38.431  17.555  1.00 79.71           S  
+ANISOU 7187  SG  CYS C  69    10024  10852   9411    762    -88    488       S  
+ATOM   7188  N   ASN C  70      -3.195  33.529  17.285  1.00 91.60           N  
+ANISOU 7188  N   ASN C  70    11513  12190  11101   1182   -115   1069       N  
+ATOM   7189  CA  ASN C  70      -2.155  32.517  17.130  1.00 88.58           C  
+ANISOU 7189  CA  ASN C  70    11039  11760  10857   1328   -185   1196       C  
+ATOM   7190  C   ASN C  70      -1.961  32.140  15.664  1.00 87.96           C  
+ANISOU 7190  C   ASN C  70    10869  11557  10994   1383     -9   1188       C  
+ATOM   7191  O   ASN C  70      -2.887  32.264  14.860  1.00 84.35           O  
+ANISOU 7191  O   ASN C  70    10493  11023  10533   1315    169   1124       O  
+ATOM   7192  CB  ASN C  70      -2.493  31.275  17.961  1.00 88.38           C  
+ANISOU 7192  CB  ASN C  70    11197  11701  10682   1405   -231   1357       C  
+ATOM   7193  CG  ASN C  70      -1.429  30.198  17.864  1.00 84.51           C  
+ANISOU 7193  CG  ASN C  70    10627  11147  10338   1577   -316   1494       C  
+ATOM   7194  OD1 ASN C  70      -1.418  29.401  16.926  1.00 87.87           O  
+ANISOU 7194  OD1 ASN C  70    11052  11430  10903   1658   -186   1532       O  
+ATOM   7195  ND2 ASN C  70      -0.525  30.171  18.836  1.00 85.46           N  
+ANISOU 7195  ND2 ASN C  70    10680  11369  10421   1644   -545   1563       N  
+ATOM   7196  N   GLU C  71      -0.750  31.704  15.321  1.00 89.52           N  
+ANISOU 7196  N   GLU C  71    10897  11742  11374   1515    -62   1250       N  
+ATOM   7197  CA  GLU C  71      -0.418  31.292  13.959  1.00 94.02           C  
+ANISOU 7197  CA  GLU C  71    11381  12207  12136   1604    109   1244       C  
+ATOM   7198  C   GLU C  71      -1.401  30.251  13.428  1.00 96.61           C  
+ANISOU 7198  C   GLU C  71    11929  12373  12407   1636    260   1276       C  
+ATOM   7199  O   GLU C  71      -1.772  30.278  12.254  1.00 91.77           O  
+ANISOU 7199  O   GLU C  71    11335  11673  11862   1627    434   1207       O  
+ATOM   7200  CB  GLU C  71       1.008  30.739  13.900  1.00 96.90           C  
+ANISOU 7200  CB  GLU C  71    11547  12586  12683   1780     23   1336       C  
+ATOM   7201  N   ASN C  72      -1.816  29.335  14.298  1.00 98.37           N  
+ANISOU 7201  N   ASN C  72    12322  12550  12505   1668    182   1387       N  
+ATOM   7202  CA  ASN C  72      -2.826  28.346  13.942  1.00 99.45           C  
+ANISOU 7202  CA  ASN C  72    12674  12521  12590   1666    296   1431       C  
+ATOM   7203  C   ASN C  72      -4.186  29.006  13.747  1.00 96.13           C  
+ANISOU 7203  C   ASN C  72    12363  12109  12054   1484    409   1339       C  
+ATOM   7204  O   ASN C  72      -4.790  29.497  14.701  1.00 97.63           O  
+ANISOU 7204  O   ASN C  72    12616  12401  12080   1379    355   1344       O  
+ATOM   7205  CB  ASN C  72      -2.915  27.260  15.016  1.00100.13           C  
+ANISOU 7205  CB  ASN C  72    12907  12561  12576   1729    178   1599       C  
+ATOM   7206  CG  ASN C  72      -3.643  26.021  14.535  1.00109.36           C  
+ANISOU 7206  CG  ASN C  72    14271  13516  13766   1760    273   1669       C  
+ATOM   7207  OD1 ASN C  72      -3.870  25.845  13.338  1.00112.88           O  
+ANISOU 7207  OD1 ASN C  72    14734  13839  14317   1774    408   1586       O  
+ATOM   7208  ND2 ASN C  72      -4.014  25.153  15.470  1.00116.11           N  
+ANISOU 7208  ND2 ASN C  72    15284  14318  14515   1766    194   1826       N  
+ATOM   7209  N   GLN C  73      -4.665  29.015  12.507  1.00 92.54           N  
+ANISOU 7209  N   GLN C  73    11934  11551  11678   1460    565   1256       N  
+ATOM   7210  CA  GLN C  73      -5.887  29.736  12.165  1.00 87.92           C  
+ANISOU 7210  CA  GLN C  73    11416  10976  11015   1297    668   1162       C  
+ATOM   7211  C   GLN C  73      -7.132  28.979  12.618  1.00 85.30           C  
+ANISOU 7211  C   GLN C  73    11279  10562  10568   1220    693   1243       C  
+ATOM   7212  O   GLN C  73      -8.242  29.518  12.595  1.00 90.79           O  
+ANISOU 7212  O   GLN C  73    12025  11286  11186   1084    763   1192       O  
+ATOM   7213  CB  GLN C  73      -5.943  30.007  10.661  1.00 80.18           C  
+ANISOU 7213  CB  GLN C  73    10398   9918  10150   1302    809   1055       C  
+ATOM   7214  CG  GLN C  73      -6.328  31.438  10.315  1.00 89.71           C  
+ANISOU 7214  CG  GLN C  73    11522  11226  11340   1174    863    932       C  
+ATOM   7215  CD  GLN C  73      -5.357  32.462  10.881  1.00 96.01           C  
+ANISOU 7215  CD  GLN C  73    12138  12175  12166   1170    767    902       C  
+ATOM   7216  OE1 GLN C  73      -4.183  32.168  11.106  1.00102.00           O  
+ANISOU 7216  OE1 GLN C  73    12781  12965  13010   1281    687    958       O  
+ATOM   7217  NE2 GLN C  73      -5.849  33.672  11.121  1.00 95.88           N  
+ANISOU 7217  NE2 GLN C  73    12093  12247  12091   1043    762    814       N  
+ATOM   7218  N   GLY C  74      -6.938  27.727  13.023  1.00 73.23           N  
+ANISOU 7218  N   GLY C  74     9851   8927   9045   1308    636   1380       N  
+ATOM   7219  CA  GLY C  74      -8.008  26.928  13.593  1.00 82.98           C  
+ANISOU 7219  CA  GLY C  74    11262  10083  10184   1230    645   1497       C  
+ATOM   7220  C   GLY C  74      -8.608  27.611  14.807  1.00 87.32           C  
+ANISOU 7220  C   GLY C  74    11825  10808  10544   1121    617   1529       C  
+ATOM   7221  O   GLY C  74      -9.817  27.553  15.028  1.00101.27           O  
+ANISOU 7221  O   GLY C  74    13683  12568  12227    999    692   1564       O  
+ATOM   7222  N   ASN C  75      -7.748  28.243  15.602  1.00 75.40           N  
+ANISOU 7222  N   ASN C  75    10224   9458   8969   1172    504   1517       N  
+ATOM   7223  CA  ASN C  75      -8.172  29.043  16.746  1.00 78.88           C  
+ANISOU 7223  CA  ASN C  75    10684  10080   9209   1092    465   1510       C  
+ATOM   7224  C   ASN C  75      -9.177  30.116  16.336  1.00 71.69           C  
+ANISOU 7224  C   ASN C  75     9749   9225   8263    960    590   1368       C  
+ATOM   7225  O   ASN C  75     -10.305  30.170  16.846  1.00 68.57           O  
+ANISOU 7225  O   ASN C  75     9444   8874   7736    869    666   1405       O  
+ATOM   7226  CB  ASN C  75      -6.957  29.691  17.411  1.00 73.92           C  
+ANISOU 7226  CB  ASN C  75     9943   9593   8551   1166    300   1473       C  
+ATOM   7227  CG  ASN C  75      -6.021  28.675  18.035  1.00 75.62           C  
+ANISOU 7227  CG  ASN C  75    10180   9779   8773   1303    153   1631       C  
+ATOM   7228  OD1 ASN C  75      -6.203  27.468  17.877  1.00 75.64           O  
+ANISOU 7228  OD1 ASN C  75    10285   9633   8822   1355    182   1764       O  
+ATOM   7229  ND2 ASN C  75      -5.009  29.160  18.745  1.00 77.85           N  
+ANISOU 7229  ND2 ASN C  75    10368  10193   9019   1362    -22   1619       N  
+ATOM   7230  N   ARG C  76      -8.742  30.975  15.417  1.00 68.76           N  
+ANISOU 7230  N   ARG C  76     9249   8858   8019    958    614   1218       N  
+ATOM   7231  CA  ARG C  76      -9.591  32.006  14.832  1.00 72.17           C  
+ANISOU 7231  CA  ARG C  76     9648   9318   8456    850    723   1082       C  
+ATOM   7232  C   ARG C  76     -10.922  31.457  14.339  1.00 77.50           C  
+ANISOU 7232  C   ARG C  76    10421   9892   9134    768    854   1122       C  
+ATOM   7233  O   ARG C  76     -11.981  32.005  14.648  1.00 74.48           O  
+ANISOU 7233  O   ARG C  76    10065   9577   8657    675    926   1092       O  
+ATOM   7234  CB  ARG C  76      -8.871  32.695  13.674  1.00 67.69           C  
+ANISOU 7234  CB  ARG C  76     8942   8719   8057    871    743    960       C  
+ATOM   7235  CG  ARG C  76      -9.726  33.737  12.983  1.00 63.28           C  
+ANISOU 7235  CG  ARG C  76     8359   8171   7515    769    848    832       C  
+ATOM   7236  CD  ARG C  76      -9.002  34.394  11.829  1.00 68.92           C  
+ANISOU 7236  CD  ARG C  76     8947   8853   8385    788    876    738       C  
+ATOM   7237  NE  ARG C  76      -9.415  35.784  11.691  1.00 78.59           N  
+ANISOU 7237  NE  ARG C  76    10119  10142   9600    699    903    615       N  
+ATOM   7238  CZ  ARG C  76      -8.803  36.802  12.283  1.00 90.48           C  
+ANISOU 7238  CZ  ARG C  76    11541  11745  11093    682    810    547       C  
+ATOM   7239  NH1 ARG C  76      -7.749  36.589  13.058  1.00 90.71           N  
+ANISOU 7239  NH1 ARG C  76    11517  11834  11115    742    675    592       N  
+ATOM   7240  NH2 ARG C  76      -9.253  38.033  12.105  1.00 96.04           N  
+ANISOU 7240  NH2 ARG C  76    12218  12475  11799    605    836    434       N  
+ATOM   7241  N   GLY C  77     -10.856  30.372  13.574  1.00 77.62           N  
+ANISOU 7241  N   GLY C  77    10487   9740   9265    807    877   1186       N  
+ATOM   7242  CA  GLY C  77     -12.048  29.746  13.034  1.00 75.78           C  
+ANISOU 7242  CA  GLY C  77    10346   9384   9064    720    968   1225       C  
+ATOM   7243  C   GLY C  77     -13.007  29.295  14.118  1.00 66.13           C  
+ANISOU 7243  C   GLY C  77     9214   8205   7709    642    989   1363       C  
+ATOM   7244  O   GLY C  77     -14.217  29.472  13.998  1.00 66.97           O  
+ANISOU 7244  O   GLY C  77     9333   8316   7797    528   1079   1363       O  
+ATOM   7245  N   ARG C  78     -12.460  28.714  15.181  1.00 61.69           N  
+ANISOU 7245  N   ARG C  78     8706   7681   7053    707    907   1494       N  
+ATOM   7246  CA  ARG C  78     -13.267  28.206  16.284  1.00 61.33           C  
+ANISOU 7246  CA  ARG C  78     8758   7685   6861    645    934   1658       C  
+ATOM   7247  C   ARG C  78     -13.961  29.332  17.047  1.00 70.71           C  
+ANISOU 7247  C   ARG C  78     9911   9079   7877    580   1000   1597       C  
+ATOM   7248  O   ARG C  78     -15.172  29.274  17.293  1.00 84.16           O  
+ANISOU 7248  O   ARG C  78    11641  10811   9525    480   1113   1661       O  
+ATOM   7249  CB  ARG C  78     -12.401  27.384  17.241  1.00 63.61           C  
+ANISOU 7249  CB  ARG C  78     9121   7974   7073    748    815   1814       C  
+ATOM   7250  N   ILE C  79     -13.195  30.357  17.412  1.00 68.41           N  
+ANISOU 7250  N   ILE C  79     9555   8925   7511    641    929   1472       N  
+ATOM   7251  CA  ILE C  79     -13.745  31.473  18.177  1.00 73.87           C  
+ANISOU 7251  CA  ILE C  79    10237   9802   8029    605    976   1388       C  
+ATOM   7252  C   ILE C  79     -14.808  32.208  17.356  1.00 61.30           C  
+ANISOU 7252  C   ILE C  79     8577   8197   6517    514   1111   1273       C  
+ATOM   7253  O   ILE C  79     -15.910  32.516  17.851  1.00 55.87           O  
+ANISOU 7253  O   ILE C  79     7905   7601   5720    456   1224   1293       O  
+ATOM   7254  CB  ILE C  79     -12.636  32.463  18.598  1.00 62.35           C  
+ANISOU 7254  CB  ILE C  79     8725   8457   6510    679    841   1253       C  
+ATOM   7255  CG1 ILE C  79     -11.628  31.781  19.528  1.00 64.99           C  
+ANISOU 7255  CG1 ILE C  79     9119   8826   6747    772    685   1375       C  
+ATOM   7256  CG2 ILE C  79     -13.234  33.711  19.233  1.00 60.79           C  
+ANISOU 7256  CG2 ILE C  79     8531   8417   6149    648    887   1125       C  
+ATOM   7257  CD1 ILE C  79     -12.238  31.226  20.796  1.00 64.92           C  
+ANISOU 7257  CD1 ILE C  79     9254   8913   6499    770    712   1539       C  
+ATOM   7258  N   ASN C  80     -14.476  32.455  16.090  1.00 61.68           N  
+ANISOU 7258  N   ASN C  80     8547   8134   6755    512   1102   1164       N  
+ATOM   7259  CA  ASN C  80     -15.407  33.057  15.145  1.00 62.52           C  
+ANISOU 7259  CA  ASN C  80     8593   8203   6958    433   1205   1066       C  
+ATOM   7260  C   ASN C  80     -16.688  32.248  15.046  1.00 61.61           C  
+ANISOU 7260  C   ASN C  80     8519   8026   6865    340   1306   1191       C  
+ATOM   7261  O   ASN C  80     -17.789  32.799  15.062  1.00 61.72           O  
+ANISOU 7261  O   ASN C  80     8491   8104   6857    272   1407   1163       O  
+ATOM   7262  CB  ASN C  80     -14.774  33.170  13.756  1.00 57.51           C  
+ANISOU 7262  CB  ASN C  80     7899   7442   6510    455   1176    969       C  
+ATOM   7263  CG  ASN C  80     -13.811  34.334  13.641  1.00 58.85           C  
+ANISOU 7263  CG  ASN C  80     7981   7682   6696    504   1113    825       C  
+ATOM   7264  OD1 ASN C  80     -13.441  34.951  14.637  1.00 57.61           O  
+ANISOU 7264  OD1 ASN C  80     7820   7651   6419    530   1054    792       O  
+ATOM   7265  ND2 ASN C  80     -13.399  34.641  12.416  1.00 67.03           N  
+ANISOU 7265  ND2 ASN C  80     8955   8635   7880    512   1122    742       N  
+ATOM   7266  N   GLN C  81     -16.531  30.932  14.956  1.00 53.95           N  
+ANISOU 7266  N   GLN C  81     7623   6923   5951    339   1272   1334       N  
+ATOM   7267  CA  GLN C  81     -17.665  30.033  14.819  1.00 53.79           C  
+ANISOU 7267  CA  GLN C  81     7642   6810   5986    233   1343   1471       C  
+ATOM   7268  C   GLN C  81     -18.584  30.137  16.026  1.00 64.83           C  
+ANISOU 7268  C   GLN C  81     9046   8363   7222    179   1441   1587       C  
+ATOM   7269  O   GLN C  81     -19.797  30.271  15.876  1.00 52.75           O  
+ANISOU 7269  O   GLN C  81     7461   6855   5727     79   1547   1614       O  
+ATOM   7270  CB  GLN C  81     -17.194  28.590  14.636  1.00 59.43           C  
+ANISOU 7270  CB  GLN C  81     8458   7336   6786    253   1268   1606       C  
+ATOM   7271  CG  GLN C  81     -18.274  27.635  14.147  1.00 78.34           C  
+ANISOU 7271  CG  GLN C  81    10893   9569   9302    126   1306   1718       C  
+ATOM   7272  CD  GLN C  81     -18.881  28.064  12.821  1.00 76.17           C  
+ANISOU 7272  CD  GLN C  81    10557   9215   9168     59   1327   1577       C  
+ATOM   7273  OE1 GLN C  81     -18.401  27.680  11.754  1.00 75.31           O  
+ANISOU 7273  OE1 GLN C  81    10493   8944   9179     97   1263   1499       O  
+ATOM   7274  NE2 GLN C  81     -19.952  28.849  12.882  1.00 67.02           N  
+ANISOU 7274  NE2 GLN C  81     9301   8175   7990    -29   1418   1546       N  
+ATOM   7275  N   ILE C  82     -18.000  30.082  17.219  1.00 53.80           N  
+ANISOU 7275  N   ILE C  82     7713   7083   5644    252   1406   1658       N  
+ATOM   7276  CA  ILE C  82     -18.777  30.185  18.450  1.00 53.59           C  
+ANISOU 7276  CA  ILE C  82     7716   7228   5420    226   1512   1773       C  
+ATOM   7277  C   ILE C  82     -19.564  31.499  18.526  1.00 52.18           C  
+ANISOU 7277  C   ILE C  82     7446   7206   5175    212   1625   1626       C  
+ATOM   7278  O   ILE C  82     -20.797  31.496  18.690  1.00 79.77           O  
+ANISOU 7278  O   ILE C  82    10891  10757   8661    133   1771   1702       O  
+ATOM   7279  CB  ILE C  82     -17.870  30.066  19.694  1.00 55.69           C  
+ANISOU 7279  CB  ILE C  82     8084   7607   5468    329   1428   1840       C  
+ATOM   7280  CG1 ILE C  82     -17.330  28.640  19.828  1.00 57.11           C  
+ANISOU 7280  CG1 ILE C  82     8363   7640   5698    343   1340   2040       C  
+ATOM   7281  CG2 ILE C  82     -18.628  30.466  20.951  1.00 55.38           C  
+ANISOU 7281  CG2 ILE C  82     8083   7782   5175    328   1552   1909       C  
+ATOM   7282  CD1 ILE C  82     -16.164  28.515  20.784  1.00 59.32           C  
+ANISOU 7282  CD1 ILE C  82     8729   7998   5812    467   1201   2085       C  
+ATOM   7283  N   ILE C  83     -18.858  32.619  18.369  1.00 52.13           N  
+ANISOU 7283  N   ILE C  83     7407   7258   5142    289   1557   1421       N  
+ATOM   7284  CA  ILE C  83     -19.503  33.929  18.492  1.00 56.16           C  
+ANISOU 7284  CA  ILE C  83     7851   7900   5588    298   1647   1268       C  
+ATOM   7285  C   ILE C  83     -20.585  34.166  17.426  1.00 55.01           C  
+ANISOU 7285  C   ILE C  83     7592   7681   5628    211   1743   1229       C  
+ATOM   7286  O   ILE C  83     -21.711  34.586  17.744  1.00 51.21           O  
+ANISOU 7286  O   ILE C  83     7052   7304   5100    184   1883   1241       O  
+ATOM   7287  CB  ILE C  83     -18.449  35.052  18.437  1.00 51.28           C  
+ANISOU 7287  CB  ILE C  83     7225   7315   4942    382   1527   1059       C  
+ATOM   7288  CG1 ILE C  83     -17.683  35.096  19.762  1.00 57.12           C  
+ANISOU 7288  CG1 ILE C  83     8072   8185   5445    467   1442   1079       C  
+ATOM   7289  CG2 ILE C  83     -19.100  36.397  18.152  1.00 49.59           C  
+ANISOU 7289  CG2 ILE C  83     6937   7161   4744    383   1602    881       C  
+ATOM   7290  CD1 ILE C  83     -16.443  35.951  19.737  1.00 79.67           C  
+ANISOU 7290  CD1 ILE C  83    10918  11048   8305    532   1275    907       C  
+ATOM   7291  N   LEU C  84     -20.254  33.875  16.171  1.00 61.48           N  
+ANISOU 7291  N   LEU C  84     8379   8329   6652    176   1667   1187       N  
+ATOM   7292  CA  LEU C  84     -21.221  34.004  15.080  1.00 53.82           C  
+ANISOU 7292  CA  LEU C  84     7316   7276   5856     92   1722   1155       C  
+ATOM   7293  C   LEU C  84     -22.436  33.117  15.323  1.00 59.79           C  
+ANISOU 7293  C   LEU C  84     8048   8025   6644    -15   1823   1343       C  
+ATOM   7294  O   LEU C  84     -23.558  33.545  15.089  1.00 65.91           O  
+ANISOU 7294  O   LEU C  84     8718   8847   7479    -71   1918   1334       O  
+ATOM   7295  CB  LEU C  84     -20.592  33.717  13.714  1.00 52.12           C  
+ANISOU 7295  CB  LEU C  84     7105   6878   5821     83   1618   1087       C  
+ATOM   7296  CG  LEU C  84     -19.924  34.932  13.047  1.00 50.75           C  
+ANISOU 7296  CG  LEU C  84     6886   6711   5684    144   1570    891       C  
+ATOM   7297  CD1 LEU C  84     -18.774  35.524  13.857  1.00 62.64           C  
+ANISOU 7297  CD1 LEU C  84     8423   8312   7067    239   1505    820       C  
+ATOM   7298  CD2 LEU C  84     -19.484  34.609  11.623  1.00 45.28           C  
+ANISOU 7298  CD2 LEU C  84     6199   5851   5155    135   1504    843       C  
+ATOM   7299  N   ASP C  85     -22.212  31.876  15.745  1.00 58.00           N  
+ANISOU 7299  N   ASP C  85     7907   7729   6402    -46   1795   1520       N  
+ATOM   7300  CA  ASP C  85     -23.322  30.988  16.092  1.00 55.98           C  
+ANISOU 7300  CA  ASP C  85     7627   7463   6180   -164   1890   1729       C  
+ATOM   7301  C   ASP C  85     -24.229  31.622  17.144  1.00 69.96           C  
+ANISOU 7301  C   ASP C  85     9329   9460   7794   -156   2063   1778       C  
+ATOM   7302  O   ASP C  85     -25.458  31.534  17.036  1.00 64.31           O  
+ANISOU 7302  O   ASP C  85     8498   8772   7164   -254   2176   1866       O  
+ATOM   7303  CB  ASP C  85     -22.813  29.635  16.592  1.00 50.04           C  
+ANISOU 7303  CB  ASP C  85     7002   6608   5404   -181   1832   1924       C  
+ATOM   7304  CG  ASP C  85     -22.323  28.746  15.468  1.00 69.44           C  
+ANISOU 7304  CG  ASP C  85     9518   8809   8058   -213   1695   1914       C  
+ATOM   7305  OD1 ASP C  85     -22.680  29.011  14.301  1.00 62.95           O  
+ANISOU 7305  OD1 ASP C  85     8633   7891   7392   -260   1666   1796       O  
+ATOM   7306  OD2 ASP C  85     -21.582  27.782  15.752  1.00 71.10           O  
+ANISOU 7306  OD2 ASP C  85     9847   8912   8257   -179   1615   2022       O  
+ATOM   7307  N   GLU C  86     -23.638  32.257  18.156  1.00 55.26           N  
+ANISOU 7307  N   GLU C  86     7535   7760   5702    -36   2081   1719       N  
+ATOM   7308  CA  GLU C  86     -24.454  32.944  19.160  1.00 56.43           C  
+ANISOU 7308  CA  GLU C  86     7640   8131   5670      3   2255   1734       C  
+ATOM   7309  C   GLU C  86     -25.311  34.028  18.490  1.00 55.94           C  
+ANISOU 7309  C   GLU C  86     7426   8108   5718      1   2331   1580       C  
+ATOM   7310  O   GLU C  86     -26.530  34.123  18.733  1.00 62.42           O  
+ANISOU 7310  O   GLU C  86     8131   9030   6555    -42   2497   1665       O  
+ATOM   7311  CB  GLU C  86     -23.564  33.561  20.243  1.00 66.29           C  
+ANISOU 7311  CB  GLU C  86     9014   9528   6646    145   2221   1645       C  
+ATOM   7312  CG  GLU C  86     -24.313  34.131  21.439  1.00 78.24           C  
+ANISOU 7312  CG  GLU C  86    10535  11279   7916    211   2405   1670       C  
+ATOM   7313  CD  GLU C  86     -24.686  33.069  22.455  1.00 89.85           C  
+ANISOU 7313  CD  GLU C  86    12074  12832   9235    173   2514   1947       C  
+ATOM   7314  OE1 GLU C  86     -24.174  31.935  22.346  1.00 84.30           O  
+ANISOU 7314  OE1 GLU C  86    11439  11992   8598    110   2411   2106       O  
+ATOM   7315  OE2 GLU C  86     -25.484  33.370  23.367  1.00 98.48           O  
+ANISOU 7315  OE2 GLU C  86    13156  14123  10141    213   2708   2011       O  
+ATOM   7316  N   PHE C  87     -24.680  34.818  17.621  1.00 48.85           N  
+ANISOU 7316  N   PHE C  87     6521   7128   4912     47   2212   1369       N  
+ATOM   7317  CA  PHE C  87     -25.412  35.820  16.842  1.00 51.82           C  
+ANISOU 7317  CA  PHE C  87     6765   7507   5416     47   2255   1228       C  
+ATOM   7318  C   PHE C  87     -26.598  35.231  16.079  1.00 66.15           C  
+ANISOU 7318  C   PHE C  87     8444   9249   7442    -87   2307   1350       C  
+ATOM   7319  O   PHE C  87     -27.724  35.712  16.196  1.00 82.61           O  
+ANISOU 7319  O   PHE C  87    10394  11437   9557    -95   2440   1365       O  
+ATOM   7320  CB  PHE C  87     -24.485  36.532  15.853  1.00 61.01           C  
+ANISOU 7320  CB  PHE C  87     7951   8555   6677     89   2103   1029       C  
+ATOM   7321  CG  PHE C  87     -23.837  37.768  16.404  1.00 72.74           C  
+ANISOU 7321  CG  PHE C  87     9486  10136   8017    212   2081    844       C  
+ATOM   7322  CD1 PHE C  87     -24.554  38.951  16.482  1.00 74.90           C  
+ANISOU 7322  CD1 PHE C  87     9688  10495   8275    270   2169    719       C  
+ATOM   7323  CD2 PHE C  87     -22.517  37.760  16.820  1.00 78.07           C  
+ANISOU 7323  CD2 PHE C  87    10274  10802   8587    270   1958    793       C  
+ATOM   7324  CE1 PHE C  87     -23.973  40.100  16.978  1.00 80.33           C  
+ANISOU 7324  CE1 PHE C  87    10439  11243   8841    378   2132    537       C  
+ATOM   7325  CE2 PHE C  87     -21.928  38.910  17.317  1.00 85.04           C  
+ANISOU 7325  CE2 PHE C  87    11203  11757   9352    365   1911    618       C  
+ATOM   7326  CZ  PHE C  87     -22.659  40.081  17.396  1.00 87.57           C  
+ANISOU 7326  CZ  PHE C  87    11472  12145   9654    416   1996    485       C  
+ATOM   7327  N   SER C  88     -26.328  34.187  15.303  1.00 58.55           N  
+ANISOU 7327  N   SER C  88     7518   8102   6628   -186   2193   1432       N  
+ATOM   7328  CA  SER C  88     -27.341  33.526  14.492  1.00 54.37           C  
+ANISOU 7328  CA  SER C  88     6881   7465   6312   -330   2191   1538       C  
+ATOM   7329  C   SER C  88     -28.491  33.003  15.337  1.00 65.44           C  
+ANISOU 7329  C   SER C  88     8183   8981   7699   -413   2354   1752       C  
+ATOM   7330  O   SER C  88     -29.646  33.040  14.914  1.00 72.87           O  
+ANISOU 7330  O   SER C  88     8958   9931   8796   -503   2409   1807       O  
+ATOM   7331  CB  SER C  88     -26.714  32.378  13.698  1.00 50.54           C  
+ANISOU 7331  CB  SER C  88     6503   6752   5949   -405   2033   1586       C  
+ATOM   7332  OG  SER C  88     -25.657  32.843  12.878  1.00 67.56           O  
+ANISOU 7332  OG  SER C  88     8736   8816   8119   -323   1908   1402       O  
+ATOM   7333  N   ARG C  89     -28.177  32.514  16.532  1.00 62.05           N  
+ANISOU 7333  N   ARG C  89     7846   8645   7085   -383   2430   1886       N  
+ATOM   7334  CA  ARG C  89     -29.218  32.033  17.428  1.00 63.33           C  
+ANISOU 7334  CA  ARG C  89     7918   8937   7207   -455   2614   2113       C  
+ATOM   7335  C   ARG C  89     -29.922  33.194  18.127  1.00 67.55           C  
+ANISOU 7335  C   ARG C  89     8342   9717   7605   -346   2808   2043       C  
+ATOM   7336  O   ARG C  89     -30.925  32.993  18.812  1.00 78.16           O  
+ANISOU 7336  O   ARG C  89     9571  11204   8922   -387   2999   2217       O  
+ATOM   7337  CB  ARG C  89     -28.638  31.069  18.466  1.00 67.31           C  
+ANISOU 7337  CB  ARG C  89     8579   9455   7541   -456   2630   2301       C  
+ATOM   7338  N   LYS C  90     -29.412  34.410  17.939  1.00 72.52           N  
+ANISOU 7338  N   LYS C  90     9004  10390   8161   -205   2764   1793       N  
+ATOM   7339  CA  LYS C  90     -30.009  35.566  18.609  1.00 66.82           C  
+ANISOU 7339  CA  LYS C  90     8207   9879   7303    -74   2937   1697       C  
+ATOM   7340  C   LYS C  90     -30.632  36.635  17.698  1.00 73.79           C  
+ANISOU 7340  C   LYS C  90     8935  10745   8355    -40   2931   1527       C  
+ATOM   7341  O   LYS C  90     -31.117  37.648  18.198  1.00 84.44           O  
+ANISOU 7341  O   LYS C  90    10226  12249   9608     87   3068   1428       O  
+ATOM   7342  CB  LYS C  90     -28.960  36.235  19.500  1.00 65.45           C  
+ANISOU 7342  CB  LYS C  90     8222   9801   6846     89   2913   1549       C  
+ATOM   7343  N   VAL C  91     -30.654  36.419  16.385  1.00 64.96           N  
+ANISOU 7343  N   VAL C  91     7760   9441   7480   -141   2776   1493       N  
+ATOM   7344  CA  VAL C  91     -31.150  37.455  15.471  1.00 57.79           C  
+ANISOU 7344  CA  VAL C  91     6728   8506   6724   -101   2744   1335       C  
+ATOM   7345  C   VAL C  91     -32.454  37.082  14.768  1.00 57.48           C  
+ANISOU 7345  C   VAL C  91     6468   8439   6932   -230   2769   1461       C  
+ATOM   7346  O   VAL C  91     -32.771  35.903  14.613  1.00 66.06           O  
+ANISOU 7346  O   VAL C  91     7522   9450   8129   -389   2740   1648       O  
+ATOM   7347  CB  VAL C  91     -30.110  37.795  14.381  1.00 61.00           C  
+ANISOU 7347  CB  VAL C  91     7247   8731   7201    -89   2530   1158       C  
+ATOM   7348  CG1 VAL C  91     -28.867  38.416  14.998  1.00 60.80           C  
+ANISOU 7348  CG1 VAL C  91     7395   8738   6968     42   2491   1009       C  
+ATOM   7349  CG2 VAL C  91     -29.758  36.556  13.572  1.00 58.74           C  
+ANISOU 7349  CG2 VAL C  91     7016   8255   7048   -234   2382   1260       C  
+ATOM   7350  N   ASP C  92     -33.192  38.101  14.328  1.00 57.39           N  
+ANISOU 7350  N   ASP C  92     6306   8477   7020   -162   2805   1358       N  
+ATOM   7351  CA  ASP C  92     -34.421  37.900  13.562  1.00 62.96           C  
+ANISOU 7351  CA  ASP C  92     6782   9158   7980   -273   2796   1457       C  
+ATOM   7352  C   ASP C  92     -34.730  39.077  12.648  1.00 60.17           C  
+ANISOU 7352  C   ASP C  92     6343   8772   7748   -186   2722   1284       C  
+ATOM   7353  O   ASP C  92     -34.186  40.170  12.809  1.00 67.73           O  
+ANISOU 7353  O   ASP C  92     7392   9757   8587    -27   2732   1099       O  
+ATOM   7354  CB  ASP C  92     -35.621  37.701  14.497  1.00 66.34           C  
+ANISOU 7354  CB  ASP C  92     7004   9786   8414   -285   3036   1644       C  
+ATOM   7355  CG  ASP C  92     -35.575  36.393  15.254  1.00 87.87           C  
+ANISOU 7355  CG  ASP C  92     9776  12530  11079   -414   3106   1876       C  
+ATOM   7356  OD1 ASP C  92     -35.516  35.328  14.605  1.00104.15           O  
+ANISOU 7356  OD1 ASP C  92    11857  14420  13296   -595   2956   1987       O  
+ATOM   7357  OD2 ASP C  92     -35.601  36.431  16.503  1.00 90.29           O  
+ANISOU 7357  OD2 ASP C  92    10113  13017  11175   -329   3310   1949       O  
+ATOM   7358  N   LEU C  93     -35.621  38.841  11.691  1.00 67.77           N  
+ANISOU 7358  N   LEU C  93     7133   9665   8952   -299   2633   1352       N  
+ATOM   7359  CA  LEU C  93     -36.002  39.854  10.719  1.00 65.23           C  
+ANISOU 7359  CA  LEU C  93     6723   9299   8763   -231   2538   1219       C  
+ATOM   7360  C   LEU C  93     -37.041  40.764  11.369  1.00 67.50           C  
+ANISOU 7360  C   LEU C  93     6799   9780   9069    -95   2739   1222       C  
+ATOM   7361  O   LEU C  93     -37.907  40.290  12.103  1.00 75.61           O  
+ANISOU 7361  O   LEU C  93     7653  10950  10127   -135   2911   1392       O  
+ATOM   7362  CB  LEU C  93     -36.547  39.205   9.445  1.00 67.08           C  
+ANISOU 7362  CB  LEU C  93     6867   9386   9235   -402   2340   1291       C  
+ATOM   7363  CG  LEU C  93     -36.798  40.090   8.223  1.00 73.36           C  
+ANISOU 7363  CG  LEU C  93     7615  10098  10159   -353   2184   1166       C  
+ATOM   7364  CD1 LEU C  93     -35.478  40.533   7.613  1.00 61.42           C  
+ANISOU 7364  CD1 LEU C  93     6360   8451   8527   -285   2054    989       C  
+ATOM   7365  CD2 LEU C  93     -37.641  39.353   7.194  1.00 83.26           C  
+ANISOU 7365  CD2 LEU C  93     8736  11252  11645   -531   2010   1274       C  
+ATOM   7366  N   THR C  94     -36.966  42.062  11.103  1.00 69.55           N  
+ANISOU 7366  N   THR C  94     7068  10040   9316     72   2727   1042       N  
+ATOM   7367  CA  THR C  94     -37.898  43.004  11.715  1.00 70.23           C  
+ANISOU 7367  CA  THR C  94     6974  10296   9416    238   2920   1019       C  
+ATOM   7368  C   THR C  94     -38.611  43.846  10.665  1.00 74.13           C  
+ANISOU 7368  C   THR C  94     7311  10730  10124    290   2810    956       C  
+ATOM   7369  O   THR C  94     -38.217  43.867   9.498  1.00 77.36           O  
+ANISOU 7369  O   THR C  94     7800  10968  10625    218   2584    900       O  
+ATOM   7370  CB  THR C  94     -37.189  43.944  12.716  1.00 66.67           C  
+ANISOU 7370  CB  THR C  94     6698   9923   8712    443   3047    845       C  
+ATOM   7371  OG1 THR C  94     -36.362  44.874  12.005  1.00 81.22           O  
+ANISOU 7371  OG1 THR C  94     8701  11612  10546    519   2880    644       O  
+ATOM   7372  CG2 THR C  94     -36.333  43.151  13.697  1.00 58.88           C  
+ANISOU 7372  CG2 THR C  94     5899   8982   7492    399   3112    896       C  
+ATOM   7373  N   GLU C  95     -39.671  44.528  11.091  1.00 68.89           N  
+ANISOU 7373  N   GLU C  95     6425  10216   9535    425   2978    973       N  
+ATOM   7374  CA  GLU C  95     -40.425  45.421  10.219  1.00 68.95           C  
+ANISOU 7374  CA  GLU C  95     6265  10184   9747    510   2890    921       C  
+ATOM   7375  C   GLU C  95     -39.519  46.516   9.662  1.00 73.16           C  
+ANISOU 7375  C   GLU C  95     7022  10566  10211    632   2750    700       C  
+ATOM   7376  O   GLU C  95     -39.742  47.016   8.560  1.00 83.91           O  
+ANISOU 7376  O   GLU C  95     8341  11813  11729    636   2576    663       O  
+ATOM   7377  CB  GLU C  95     -41.611  46.036  10.971  1.00 74.21           C  
+ANISOU 7377  CB  GLU C  95     6668  11053  10476    681   3133    962       C  
+ATOM   7378  CG  GLU C  95     -42.504  46.944  10.129  1.00 83.69           C  
+ANISOU 7378  CG  GLU C  95     7660  12225  11913    787   3049    928       C  
+ATOM   7379  CD  GLU C  95     -43.244  46.209   9.022  1.00 93.13           C  
+ANISOU 7379  CD  GLU C  95     8648  13359  13379    584   2848   1091       C  
+ATOM   7380  OE1 GLU C  95     -43.284  44.961   9.043  1.00 92.52           O  
+ANISOU 7380  OE1 GLU C  95     8538  13285  13331    364   2818   1249       O  
+ATOM   7381  OE2 GLU C  95     -43.784  46.887   8.123  1.00 95.66           O  
+ANISOU 7381  OE2 GLU C  95     8847  13617  13882    645   2705   1060       O  
+ATOM   7382  N   ASN C  96     -38.503  46.887  10.437  1.00 69.93           N  
+ANISOU 7382  N   ASN C  96     6847  10156   9566    726   2821    565       N  
+ATOM   7383  CA  ASN C  96     -37.501  47.849   9.993  1.00 52.20           C  
+ANISOU 7383  CA  ASN C  96     4824   7756   7253    812   2688    370       C  
+ATOM   7384  C   ASN C  96     -36.847  47.425   8.682  1.00 78.70           C  
+ANISOU 7384  C   ASN C  96     8287  10925  10689    652   2437    383       C  
+ATOM   7385  O   ASN C  96     -36.741  48.218   7.745  1.00 80.49           O  
+ANISOU 7385  O   ASN C  96     8548  11028  11008    697   2297    304       O  
+ATOM   7386  CB  ASN C  96     -36.425  48.029  11.066  1.00 51.70           C  
+ANISOU 7386  CB  ASN C  96     4994   7721   6927    884   2773    250       C  
+ATOM   7387  CG  ASN C  96     -36.967  48.647  12.337  1.00 71.78           C  
+ANISOU 7387  CG  ASN C  96     7488  10436   9348   1080   3014    190       C  
+ATOM   7388  OD1 ASN C  96     -37.905  49.440  12.303  1.00 73.58           O  
+ANISOU 7388  OD1 ASN C  96     7555  10712   9688   1227   3097    159       O  
+ATOM   7389  ND2 ASN C  96     -36.380  48.282  13.470  1.00 88.31           N  
+ANISOU 7389  ND2 ASN C  96     9726  12626  11201   1097   3127    174       N  
+ATOM   7390  N   HIS C  97     -36.425  46.165   8.623  1.00 61.31           N  
+ANISOU 7390  N   HIS C  97     6145   8703   8445    475   2388    489       N  
+ATOM   7391  CA  HIS C  97     -35.803  45.608   7.426  1.00 51.19           C  
+ANISOU 7391  CA  HIS C  97     4978   7253   7217    331   2169    503       C  
+ATOM   7392  C   HIS C  97     -36.732  45.658   6.221  1.00 52.48           C  
+ANISOU 7392  C   HIS C  97     4985   7356   7596    276   2023    566       C  
+ATOM   7393  O   HIS C  97     -36.302  45.958   5.111  1.00 52.21           O  
+ANISOU 7393  O   HIS C  97     5057   7183   7598    257   1848    509       O  
+ATOM   7394  CB  HIS C  97     -35.366  44.162   7.668  1.00 50.97           C  
+ANISOU 7394  CB  HIS C  97     5023   7217   7125    165   2158    617       C  
+ATOM   7395  CG  HIS C  97     -34.302  44.014   8.710  1.00 61.23           C  
+ANISOU 7395  CG  HIS C  97     6502   8556   8207    206   2252    565       C  
+ATOM   7396  ND1 HIS C  97     -34.546  43.466   9.950  1.00 70.18           N  
+ANISOU 7396  ND1 HIS C  97     7596   9836   9234    207   2427    655       N  
+ATOM   7397  CD2 HIS C  97     -32.986  44.332   8.691  1.00 50.93           C  
+ANISOU 7397  CD2 HIS C  97     5411   7168   6772    244   2186    443       C  
+ATOM   7398  CE1 HIS C  97     -33.427  43.457  10.653  1.00 70.67           C  
+ANISOU 7398  CE1 HIS C  97     7853   9901   9099    250   2449    583       C  
+ATOM   7399  NE2 HIS C  97     -32.466  43.977   9.912  1.00 58.05           N  
+ANISOU 7399  NE2 HIS C  97     6397   8163   7494    270   2301    452       N  
+ATOM   7400  N   LYS C  98     -38.005  45.355   6.448  1.00 59.31           N  
+ANISOU 7400  N   LYS C  98     5596   8336   8605    250   2096    692       N  
+ATOM   7401  CA  LYS C  98     -38.995  45.320   5.376  1.00 68.20           C  
+ANISOU 7401  CA  LYS C  98     6540   9420   9951    186   1941    769       C  
+ATOM   7402  C   LYS C  98     -39.291  46.722   4.839  1.00 71.84           C  
+ANISOU 7402  C   LYS C  98     6960   9847  10487    359   1890    666       C  
+ATOM   7403  O   LYS C  98     -39.334  46.938   3.622  1.00 73.69           O  
+ANISOU 7403  O   LYS C  98     7227   9961  10811    325   1682    654       O  
+ATOM   7404  CB  LYS C  98     -40.274  44.645   5.878  1.00 58.62           C  
+ANISOU 7404  CB  LYS C  98     5031   8353   8890    110   2045    946       C  
+ATOM   7405  CG  LYS C  98     -40.099  43.151   6.120  1.00 57.41           C  
+ANISOU 7405  CG  LYS C  98     4912   8185   8716   -102   2035   1081       C  
+ATOM   7406  CD  LYS C  98     -41.256  42.548   6.901  1.00 70.06           C  
+ANISOU 7406  CD  LYS C  98     6225   9952  10443   -171   2198   1271       C  
+ATOM   7407  CE  LYS C  98     -41.184  41.027   6.886  1.00 73.71           C  
+ANISOU 7407  CE  LYS C  98     6716  10349  10941   -415   2129   1424       C  
+ATOM   7408  NZ  LYS C  98     -42.231  40.398   7.739  1.00 77.46           N  
+ANISOU 7408  NZ  LYS C  98     6914  10985  11532   -500   2311   1636       N  
+ATOM   7409  N   ILE C  99     -39.484  47.672   5.751  1.00 61.31           N  
+ANISOU 7409  N   ILE C  99     5574   8613   9108    552   2078    590       N  
+ATOM   7410  CA  ILE C  99     -39.698  49.067   5.376  1.00 68.06           C  
+ANISOU 7410  CA  ILE C  99     6414   9416  10029    738   2044    481       C  
+ATOM   7411  C   ILE C  99     -38.501  49.613   4.605  1.00 71.80           C  
+ANISOU 7411  C   ILE C  99     7164   9704  10411    741   1886    358       C  
+ATOM   7412  O   ILE C  99     -38.662  50.243   3.560  1.00 87.16           O  
+ANISOU 7412  O   ILE C  99     9115  11542  12459    774   1726    343       O  
+ATOM   7413  CB  ILE C  99     -39.948  49.957   6.607  1.00 67.09           C  
+ANISOU 7413  CB  ILE C  99     6242   9413   9835    958   2284    390       C  
+ATOM   7414  CG1 ILE C  99     -41.238  49.544   7.315  1.00 64.95           C  
+ANISOU 7414  CG1 ILE C  99     5663   9344   9670    983   2469    525       C  
+ATOM   7415  CG2 ILE C  99     -40.035  51.418   6.200  1.00 58.72           C  
+ANISOU 7415  CG2 ILE C  99     5211   8256   8844   1155   2231    262       C  
+ATOM   7416  CD1 ILE C  99     -41.413  50.191   8.670  1.00 60.00           C  
+ANISOU 7416  CD1 ILE C  99     5017   8863   8918   1195   2743    441       C  
+ATOM   7417  N   LEU C 100     -37.302  49.357   5.122  1.00 70.72           N  
+ANISOU 7417  N   LEU C 100     7248   9537  10084    706   1931    285       N  
+ATOM   7418  CA  LEU C 100     -36.074  49.789   4.462  1.00 66.54           C  
+ANISOU 7418  CA  LEU C 100     6963   8847   9471    693   1803    187       C  
+ATOM   7419  C   LEU C 100     -35.950  49.163   3.078  1.00 68.83           C  
+ANISOU 7419  C   LEU C 100     7302   9028   9823    546   1596    262       C  
+ATOM   7420  O   LEU C 100     -35.508  49.810   2.128  1.00 74.41           O  
+ANISOU 7420  O   LEU C 100     8123   9607  10543    568   1467    218       O  
+ATOM   7421  CB  LEU C 100     -34.848  49.436   5.307  1.00 67.02           C  
+ANISOU 7421  CB  LEU C 100     7215   8917   9335    663   1882    119       C  
+ATOM   7422  CG  LEU C 100     -34.599  50.268   6.566  1.00 59.49           C  
+ANISOU 7422  CG  LEU C 100     6309   8027   8266    820   2040     -6       C  
+ATOM   7423  CD1 LEU C 100     -33.501  49.639   7.410  1.00 55.43           C  
+ANISOU 7423  CD1 LEU C 100     5956   7546   7559    761   2092    -36       C  
+ATOM   7424  CD2 LEU C 100     -34.250  51.701   6.202  1.00 50.70           C  
+ANISOU 7424  CD2 LEU C 100     5290   6785   7190    949   1975   -141       C  
+ATOM   7425  N   ALA C 101     -36.345  47.899   2.973  1.00 66.94           N  
+ANISOU 7425  N   ALA C 101     6986   8833   9615    395   1566    378       N  
+ATOM   7426  CA  ALA C 101     -36.277  47.177   1.709  1.00 63.60           C  
+ANISOU 7426  CA  ALA C 101     6625   8305   9234    255   1364    437       C  
+ATOM   7427  C   ALA C 101     -37.279  47.716   0.691  1.00 63.54           C  
+ANISOU 7427  C   ALA C 101     6486   8265   9392    284   1213    478       C  
+ATOM   7428  O   ALA C 101     -37.031  47.650  -0.512  1.00 66.43           O  
+ANISOU 7428  O   ALA C 101     6968   8519   9755    230   1028    481       O  
+ATOM   7429  CB  ALA C 101     -36.504  45.691   1.938  1.00 56.70           C  
+ANISOU 7429  CB  ALA C 101     5707   7468   8368     86   1361    544       C  
+ATOM   7430  N   ARG C 102     -38.403  48.251   1.163  1.00 60.38           N  
+ANISOU 7430  N   ARG C 102     5845   7968   9127    381   1291    514       N  
+ATOM   7431  CA  ARG C 102     -39.383  48.836   0.245  1.00 73.98           C  
+ANISOU 7431  CA  ARG C 102     7420   9666  11022    429   1140    560       C  
+ATOM   7432  C   ARG C 102     -39.003  50.258  -0.178  1.00 72.50           C  
+ANISOU 7432  C   ARG C 102     7346   9383  10819    597   1105    463       C  
+ATOM   7433  O   ARG C 102     -39.528  50.777  -1.162  1.00 66.08           O  
+ANISOU 7433  O   ARG C 102     6489   8508  10111    634    939    497       O  
+ATOM   7434  CB  ARG C 102     -40.793  48.840   0.850  1.00 73.21           C  
+ANISOU 7434  CB  ARG C 102     6987   9720  11109    476   1234    652       C  
+ATOM   7435  CG  ARG C 102     -41.409  47.457   1.034  1.00 67.97           C  
+ANISOU 7435  CG  ARG C 102     6166   9135  10524    283   1223    789       C  
+ATOM   7436  CD  ARG C 102     -42.876  47.548   1.441  1.00 66.19           C  
+ANISOU 7436  CD  ARG C 102     5569   9060  10519    325   1297    905       C  
+ATOM   7437  NE  ARG C 102     -43.066  47.936   2.834  1.00 65.68           N  
+ANISOU 7437  NE  ARG C 102     5393   9150  10414    468   1597    887       N  
+ATOM   7438  CZ  ARG C 102     -43.138  47.082   3.848  1.00 68.62           C  
+ANISOU 7438  CZ  ARG C 102     5695   9641  10736    385   1782    965       C  
+ATOM   7439  NH1 ARG C 102     -43.039  45.780   3.627  1.00 65.25           N  
+ANISOU 7439  NH1 ARG C 102     5292   9179  10320    154   1689   1068       N  
+ATOM   7440  NH2 ARG C 102     -43.315  47.531   5.083  1.00 68.16           N  
+ANISOU 7440  NH2 ARG C 102     5555   9730  10611    541   2059    940       N  
+ATOM   7441  N   LEU C 103     -38.090  50.881   0.562  1.00 65.76           N  
+ANISOU 7441  N   LEU C 103     6641   8508   9838    690   1246    350       N  
+ATOM   7442  CA  LEU C 103     -37.638  52.232   0.237  1.00 61.83           C  
+ANISOU 7442  CA  LEU C 103     6265   7893   9333    833   1215    259       C  
+ATOM   7443  C   LEU C 103     -36.635  52.224  -0.911  1.00 67.54           C  
+ANISOU 7443  C   LEU C 103     7226   8470   9968    748   1057    254       C  
+ATOM   7444  O   LEU C 103     -35.887  51.261  -1.079  1.00 80.86           O  
+ANISOU 7444  O   LEU C 103     9036  10146  11540    610   1036    266       O  
+ATOM   7445  CB  LEU C 103     -37.013  52.901   1.465  1.00 58.94           C  
+ANISOU 7445  CB  LEU C 103     5979   7546   8869    951   1404    131       C  
+ATOM   7446  CG  LEU C 103     -37.941  53.235   2.632  1.00 65.71           C  
+ANISOU 7446  CG  LEU C 103     6640   8543   9785   1097   1591    107       C  
+ATOM   7447  CD1 LEU C 103     -37.159  53.886   3.761  1.00 56.93           C  
+ANISOU 7447  CD1 LEU C 103     5671   7426   8533   1208   1743    -44       C  
+ATOM   7448  CD2 LEU C 103     -39.070  54.140   2.167  1.00 66.67           C  
+ANISOU 7448  CD2 LEU C 103     6582   8649  10100   1247   1537    135       C  
+ATOM   7449  N   PRO C 104     -36.616  53.302  -1.714  1.00 66.14           N  
+ANISOU 7449  N   PRO C 104     7112   8176   9843    839    951    244       N  
+ATOM   7450  CA  PRO C 104     -35.672  53.381  -2.833  1.00 65.45           C  
+ANISOU 7450  CA  PRO C 104     7248   7958   9661    771    822    256       C  
+ATOM   7451  C   PRO C 104     -34.241  53.669  -2.381  1.00 71.68           C  
+ANISOU 7451  C   PRO C 104     8234   8684  10318    761    923    167       C  
+ATOM   7452  O   PRO C 104     -33.583  54.549  -2.936  1.00 79.90           O  
+ANISOU 7452  O   PRO C 104     9414   9602  11344    799    877    152       O  
+ATOM   7453  CB  PRO C 104     -36.218  54.543  -3.665  1.00 64.98           C  
+ANISOU 7453  CB  PRO C 104     7173   7804   9713    888    698    292       C  
+ATOM   7454  CG  PRO C 104     -36.907  55.413  -2.670  1.00 64.48           C  
+ANISOU 7454  CG  PRO C 104     6951   7778   9771   1056    819    233       C  
+ATOM   7455  CD  PRO C 104     -37.504  54.477  -1.655  1.00 64.00           C  
+ANISOU 7455  CD  PRO C 104     6706   7888   9723   1018    949    236       C  
+ATOM   7456  N   ILE C 105     -33.773  52.930  -1.381  1.00 64.49           N  
+ANISOU 7456  N   ILE C 105     7327   7857   9321    707   1051    121       N  
+ATOM   7457  CA  ILE C 105     -32.400  53.052  -0.914  1.00 58.99           C  
+ANISOU 7457  CA  ILE C 105     6795   7115   8503    683   1128     43       C  
+ATOM   7458  C   ILE C 105     -31.547  51.995  -1.603  1.00 62.10           C  
+ANISOU 7458  C   ILE C 105     7318   7491   8786    543   1073     90       C  
+ATOM   7459  O   ILE C 105     -31.858  50.805  -1.551  1.00 74.79           O  
+ANISOU 7459  O   ILE C 105     8880   9171  10367    455   1066    136       O  
+ATOM   7460  CB  ILE C 105     -32.309  52.908   0.615  1.00 53.63           C  
+ANISOU 7460  CB  ILE C 105     6064   6538   7775    722   1290    -37       C  
+ATOM   7461  CG1 ILE C 105     -33.017  54.083   1.294  1.00 54.57           C  
+ANISOU 7461  CG1 ILE C 105     6092   6659   7982    891   1358   -111       C  
+ATOM   7462  CG2 ILE C 105     -30.858  52.836   1.060  1.00 51.30           C  
+ANISOU 7462  CG2 ILE C 105     5931   6206   7353    674   1334   -105       C  
+ATOM   7463  CD1 ILE C 105     -33.112  53.961   2.799  1.00 60.84           C  
+ANISOU 7463  CD1 ILE C 105     6837   7574   8707    953   1525   -191       C  
+ATOM   7464  N   HIS C 106     -30.469  52.432  -2.243  1.00 56.43           N  
+ANISOU 7464  N   HIS C 106     6761   6671   8010    527   1040     81       N  
+ATOM   7465  CA  HIS C 106     -29.647  51.535  -3.046  1.00 55.84           C  
+ANISOU 7465  CA  HIS C 106     6816   6573   7827    424    997    124       C  
+ATOM   7466  C   HIS C 106     -28.292  51.242  -2.410  1.00 57.39           C  
+ANISOU 7466  C   HIS C 106     7101   6775   7929    387   1093     73       C  
+ATOM   7467  O   HIS C 106     -27.495  50.486  -2.967  1.00 58.10           O  
+ANISOU 7467  O   HIS C 106     7294   6851   7931    321   1083    101       O  
+ATOM   7468  CB  HIS C 106     -29.439  52.122  -4.445  1.00 56.67           C  
+ANISOU 7468  CB  HIS C 106     7033   6576   7923    432    892    183       C  
+ATOM   7469  CG  HIS C 106     -30.704  52.568  -5.109  1.00 63.20           C  
+ANISOU 7469  CG  HIS C 106     7780   7387   8846    484    771    239       C  
+ATOM   7470  ND1 HIS C 106     -31.685  51.687  -5.513  1.00 67.55           N  
+ANISOU 7470  ND1 HIS C 106     8254   7994   9416    436    672    288       N  
+ATOM   7471  CD2 HIS C 106     -31.150  53.803  -5.442  1.00 61.57           C  
+ANISOU 7471  CD2 HIS C 106     7552   7107   8734    578    720    259       C  
+ATOM   7472  CE1 HIS C 106     -32.678  52.359  -6.064  1.00 63.26           C  
+ANISOU 7472  CE1 HIS C 106     7634   7427   8975    501    561    336       C  
+ATOM   7473  NE2 HIS C 106     -32.379  53.646  -6.034  1.00 62.17           N  
+ANISOU 7473  NE2 HIS C 106     7531   7210   8881    596    591    322       N  
+ATOM   7474  N   THR C 107     -28.027  51.832  -1.250  1.00 51.02           N  
+ANISOU 7474  N   THR C 107     6257   5988   7139    437   1180     -6       N  
+ATOM   7475  CA  THR C 107     -26.743  51.618  -0.595  1.00 53.63           C  
+ANISOU 7475  CA  THR C 107     6660   6327   7391    403   1247    -55       C  
+ATOM   7476  C   THR C 107     -26.879  51.246   0.879  1.00 50.64           C  
+ANISOU 7476  C   THR C 107     6217   6052   6973    422   1336   -118       C  
+ATOM   7477  O   THR C 107     -27.369  52.027   1.704  1.00 56.20           O  
+ANISOU 7477  O   THR C 107     6866   6774   7712    505   1379   -188       O  
+ATOM   7478  CB  THR C 107     -25.844  52.861  -0.716  1.00 50.20           C  
+ANISOU 7478  CB  THR C 107     6297   5785   6993    429   1239    -94       C  
+ATOM   7479  OG1 THR C 107     -25.642  53.169  -2.101  1.00 53.05           O  
+ANISOU 7479  OG1 THR C 107     6729   6059   7369    408   1174    -12       O  
+ATOM   7480  CG2 THR C 107     -24.495  52.608  -0.062  1.00 46.37           C  
+ANISOU 7480  CG2 THR C 107     5861   5314   6443    383   1286   -136       C  
+ATOM   7481  N   TYR C 108     -26.414  50.042   1.191  1.00 54.84           N  
+ANISOU 7481  N   TYR C 108     6771   6647   7420    355   1364    -91       N  
+ATOM   7482  CA  TYR C 108     -26.376  49.532   2.553  1.00 59.02           C  
+ANISOU 7482  CA  TYR C 108     7266   7278   7881    362   1447   -126       C  
+ATOM   7483  C   TYR C 108     -24.948  49.193   2.955  1.00 57.94           C  
+ANISOU 7483  C   TYR C 108     7216   7137   7661    327   1456   -151       C  
+ATOM   7484  O   TYR C 108     -24.258  48.458   2.263  1.00 61.48           O  
+ANISOU 7484  O   TYR C 108     7722   7553   8083    269   1427    -98       O  
+ATOM   7485  CB  TYR C 108     -27.257  48.287   2.704  1.00 51.69           C  
+ANISOU 7485  CB  TYR C 108     6264   6432   6941    311   1468    -46       C  
+ATOM   7486  CG  TYR C 108     -28.746  48.536   2.620  1.00 60.49           C  
+ANISOU 7486  CG  TYR C 108     7244   7589   8152    345   1472    -14       C  
+ATOM   7487  CD1 TYR C 108     -29.499  48.739   3.771  1.00 45.43           C  
+ANISOU 7487  CD1 TYR C 108     5231   5789   6243    410   1578    -36       C  
+ATOM   7488  CD2 TYR C 108     -29.403  48.558   1.397  1.00 56.91           C  
+ANISOU 7488  CD2 TYR C 108     6762   7076   7784    320   1371     43       C  
+ATOM   7489  CE1 TYR C 108     -30.861  48.960   3.705  1.00 46.87           C  
+ANISOU 7489  CE1 TYR C 108     5258   6021   6529    451   1596      4       C  
+ATOM   7490  CE2 TYR C 108     -30.767  48.779   1.322  1.00 50.24           C  
+ANISOU 7490  CE2 TYR C 108     5768   6275   7048    353   1360     81       C  
+ATOM   7491  CZ  TYR C 108     -31.490  48.980   2.480  1.00 49.75           C  
+ANISOU 7491  CZ  TYR C 108     5576   6323   7004    419   1479     65       C  
+ATOM   7492  OH  TYR C 108     -32.847  49.201   2.415  1.00 59.32           O  
+ANISOU 7492  OH  TYR C 108     6608   7590   8340    462   1482    113       O  
+ATOM   7493  N   TRP C 109     -24.512  49.765   4.068  1.00 52.77           N  
+ANISOU 7493  N   TRP C 109     6572   6513   6965    371   1491   -237       N  
+ATOM   7494  CA  TRP C 109     -23.282  49.381   4.736  1.00 46.70           C  
+ANISOU 7494  CA  TRP C 109     5860   5769   6115    344   1491   -261       C  
+ATOM   7495  C   TRP C 109     -23.643  48.678   6.034  1.00 51.47           C  
+ANISOU 7495  C   TRP C 109     6444   6498   6613    364   1557   -265       C  
+ATOM   7496  O   TRP C 109     -24.619  49.042   6.693  1.00 58.83           O  
+ANISOU 7496  O   TRP C 109     7327   7493   7531    425   1617   -300       O  
+ATOM   7497  CB  TRP C 109     -22.403  50.599   5.015  1.00 53.46           C  
+ANISOU 7497  CB  TRP C 109     6758   6555   7000    367   1449   -357       C  
+ATOM   7498  CG  TRP C 109     -21.717  51.130   3.801  1.00 58.48           C  
+ANISOU 7498  CG  TRP C 109     7420   7073   7727    326   1397   -321       C  
+ATOM   7499  CD1 TRP C 109     -22.226  52.005   2.887  1.00 62.22           C  
+ANISOU 7499  CD1 TRP C 109     7892   7453   8295    344   1371   -307       C  
+ATOM   7500  CD2 TRP C 109     -20.393  50.816   3.362  1.00 58.40           C  
+ANISOU 7500  CD2 TRP C 109     7435   7033   7720    267   1373   -278       C  
+ATOM   7501  NE1 TRP C 109     -21.298  52.257   1.907  1.00 54.18           N  
+ANISOU 7501  NE1 TRP C 109     6909   6351   7324    293   1340   -251       N  
+ATOM   7502  CE2 TRP C 109     -20.163  51.539   2.177  1.00 59.14           C  
+ANISOU 7502  CE2 TRP C 109     7545   7023   7903    246   1350   -234       C  
+ATOM   7503  CE3 TRP C 109     -19.377  49.996   3.858  1.00 43.90           C  
+ANISOU 7503  CE3 TRP C 109     5603   5254   5823    237   1373   -262       C  
+ATOM   7504  CZ2 TRP C 109     -18.961  51.462   1.478  1.00 63.96           C  
+ANISOU 7504  CZ2 TRP C 109     8168   7596   8540    196   1348   -172       C  
+ATOM   7505  CZ3 TRP C 109     -18.185  49.923   3.163  1.00 48.58           C  
+ANISOU 7505  CZ3 TRP C 109     6196   5804   6458    195   1361   -210       C  
+ATOM   7506  CH2 TRP C 109     -17.986  50.650   1.989  1.00 63.41           C  
+ANISOU 7506  CH2 TRP C 109     8082   7590   8421    174   1358   -165       C  
+ATOM   7507  N   THR C 110     -22.873  47.659   6.394  1.00 53.60           N  
+ANISOU 7507  N   THR C 110     6750   6808   6805    320   1554   -220       N  
+ATOM   7508  CA  THR C 110     -23.112  46.966   7.649  1.00 41.43           C  
+ANISOU 7508  CA  THR C 110     5209   5385   5148    336   1613   -203       C  
+ATOM   7509  C   THR C 110     -21.856  46.278   8.166  1.00 51.46           C  
+ANISOU 7509  C   THR C 110     6541   6675   6335    312   1575   -186       C  
+ATOM   7510  O   THR C 110     -20.959  45.929   7.396  1.00 46.59           O  
+ANISOU 7510  O   THR C 110     5947   5989   5766    273   1521   -152       O  
+ATOM   7511  CB  THR C 110     -24.239  45.924   7.508  1.00 48.21           C  
+ANISOU 7511  CB  THR C 110     6007   6294   6017    298   1670    -91       C  
+ATOM   7512  OG1 THR C 110     -24.471  45.296   8.774  1.00 50.95           O  
+ANISOU 7512  OG1 THR C 110     6354   6760   6245    311   1744    -54       O  
+ATOM   7513  CG2 THR C 110     -23.872  44.866   6.473  1.00 37.59           C  
+ANISOU 7513  CG2 THR C 110     4691   4872   4719    219   1614     -1       C  
+ATOM   7514  N   THR C 111     -21.790  46.103   9.480  1.00 51.29           N  
+ANISOU 7514  N   THR C 111     6549   6756   6185    348   1604   -206       N  
+ATOM   7515  CA  THR C 111     -20.724  45.326  10.091  1.00 45.36           C  
+ANISOU 7515  CA  THR C 111     5851   6039   5346    333   1559   -170       C  
+ATOM   7516  C   THR C 111     -21.300  44.020  10.620  1.00 43.51           C  
+ANISOU 7516  C   THR C 111     5620   5881   5030    313   1625    -45       C  
+ATOM   7517  O   THR C 111     -20.616  43.251  11.295  1.00 59.01           O  
+ANISOU 7517  O   THR C 111     7633   7885   6902    313   1598      8       O  
+ATOM   7518  CB  THR C 111     -20.037  46.097  11.230  1.00 47.00           C  
+ANISOU 7518  CB  THR C 111     6112   6298   5449    385   1509   -282       C  
+ATOM   7519  OG1 THR C 111     -21.022  46.548  12.168  1.00 62.14           O  
+ANISOU 7519  OG1 THR C 111     8044   8308   7260    452   1592   -338       O  
+ATOM   7520  CG2 THR C 111     -19.282  47.297  10.677  1.00 43.70           C  
+ANISOU 7520  CG2 THR C 111     5690   5776   5139    378   1421   -388       C  
+ATOM   7521  N   ASN C 112     -22.567  43.775  10.298  1.00 41.91           N  
+ANISOU 7521  N   ASN C 112     5356   5691   4875    292   1702     14       N  
+ATOM   7522  CA  ASN C 112     -23.244  42.552  10.708  1.00 42.75           C  
+ANISOU 7522  CA  ASN C 112     5448   5854   4940    249   1767    152       C  
+ATOM   7523  C   ASN C 112     -22.842  41.383   9.819  1.00 45.29           C  
+ANISOU 7523  C   ASN C 112     5798   6071   5341    175   1706    249       C  
+ATOM   7524  O   ASN C 112     -22.490  41.570   8.654  1.00 61.60           O  
+ANISOU 7524  O   ASN C 112     7868   8032   7508    158   1644    214       O  
+ATOM   7525  CB  ASN C 112     -24.760  42.744  10.686  1.00 44.99           C  
+ANISOU 7525  CB  ASN C 112     5629   6192   5273    244   1867    187       C  
+ATOM   7526  CG  ASN C 112     -25.215  43.855  11.610  1.00 52.64           C  
+ANISOU 7526  CG  ASN C 112     6579   7267   6154    345   1949     85       C  
+ATOM   7527  OD1 ASN C 112     -24.496  44.242  12.529  1.00 48.38           O  
+ANISOU 7527  OD1 ASN C 112     6124   6781   5476    407   1937      8       O  
+ATOM   7528  ND2 ASN C 112     -26.414  44.373  11.371  1.00 57.79           N  
+ANISOU 7528  ND2 ASN C 112     7123   7948   6887    371   2024     80       N  
+ATOM   7529  N   TYR C 113     -22.896  40.179  10.375  1.00 44.47           N  
+ANISOU 7529  N   TYR C 113     5725   5990   5182    139   1727    372       N  
+ATOM   7530  CA  TYR C 113     -22.547  38.982   9.626  1.00 49.05           C  
+ANISOU 7530  CA  TYR C 113     6352   6453   5832     80   1666    458       C  
+ATOM   7531  C   TYR C 113     -23.802  38.373   9.018  1.00 54.06           C  
+ANISOU 7531  C   TYR C 113     6930   7039   6570     -9   1688    544       C  
+ATOM   7532  O   TYR C 113     -23.751  37.708   7.983  1.00 51.53           O  
+ANISOU 7532  O   TYR C 113     6647   6592   6342    -59   1619    566       O  
+ATOM   7533  CB  TYR C 113     -21.853  37.977  10.541  1.00 55.13           C  
+ANISOU 7533  CB  TYR C 113     7198   7245   6503     91   1655    552       C  
+ATOM   7534  CG  TYR C 113     -20.786  38.617  11.393  1.00 61.19           C  
+ANISOU 7534  CG  TYR C 113     8004   8093   7154    173   1623    476       C  
+ATOM   7535  CD1 TYR C 113     -19.526  38.899  10.884  1.00 48.79           C  
+ANISOU 7535  CD1 TYR C 113     6454   6461   5624    212   1535    403       C  
+ATOM   7536  CD2 TYR C 113     -21.051  38.951  12.714  1.00 53.32           C  
+ANISOU 7536  CD2 TYR C 113     7018   7237   6004    212   1679    478       C  
+ATOM   7537  CE1 TYR C 113     -18.560  39.497  11.672  1.00 51.55           C  
+ANISOU 7537  CE1 TYR C 113     6821   6880   5888    271   1481    336       C  
+ATOM   7538  CE2 TYR C 113     -20.096  39.543  13.507  1.00 52.98           C  
+ANISOU 7538  CE2 TYR C 113     7023   7261   5846    282   1620    396       C  
+ATOM   7539  CZ  TYR C 113     -18.853  39.814  12.984  1.00 57.27           C  
+ANISOU 7539  CZ  TYR C 113     7572   7732   6455    303   1510    326       C  
+ATOM   7540  OH  TYR C 113     -17.904  40.409  13.781  1.00 51.81           O  
+ANISOU 7540  OH  TYR C 113     6913   7104   5670    357   1427    247       O  
+ATOM   7541  N   ASP C 114     -24.931  38.610   9.681  1.00 44.47           N  
+ANISOU 7541  N   ASP C 114     5626   5931   5340    -24   1782    588       N  
+ATOM   7542  CA  ASP C 114     -26.217  38.076   9.251  1.00 46.75           C  
+ANISOU 7542  CA  ASP C 114     5822   6196   5745   -120   1803    686       C  
+ATOM   7543  C   ASP C 114     -26.621  38.572   7.867  1.00 48.66           C  
+ANISOU 7543  C   ASP C 114     6022   6345   6123   -143   1724    614       C  
+ATOM   7544  O   ASP C 114     -26.097  39.571   7.372  1.00 41.32           O  
+ANISOU 7544  O   ASP C 114     5113   5397   5189    -73   1691    492       O  
+ATOM   7545  CB  ASP C 114     -27.302  38.432  10.273  1.00 41.27           C  
+ANISOU 7545  CB  ASP C 114     5010   5663   5008   -108   1945    743       C  
+ATOM   7546  CG  ASP C 114     -27.535  39.929  10.387  1.00 46.32           C  
+ANISOU 7546  CG  ASP C 114     5589   6386   5624     -2   1995    602       C  
+ATOM   7547  OD1 ASP C 114     -28.116  40.522   9.454  1.00 57.66           O  
+ANISOU 7547  OD1 ASP C 114     6947   7775   7188     -7   1957    551       O  
+ATOM   7548  OD2 ASP C 114     -27.134  40.516  11.414  1.00 64.13           O  
+ANISOU 7548  OD2 ASP C 114     7887   8747   7731     92   2062    541       O  
+ATOM   7549  N   ARG C 115     -27.568  37.870   7.255  1.00 52.61           N  
+ANISOU 7549  N   ARG C 115     6463   6781   6743   -248   1684    701       N  
+ATOM   7550  CA  ARG C 115     -28.034  38.208   5.915  1.00 55.40           C  
+ANISOU 7550  CA  ARG C 115     6789   7046   7215   -277   1585    647       C  
+ATOM   7551  C   ARG C 115     -29.446  38.783   5.893  1.00 55.98           C  
+ANISOU 7551  C   ARG C 115     6680   7199   7391   -301   1623    678       C  
+ATOM   7552  O   ARG C 115     -30.183  38.596   4.927  1.00 67.00           O  
+ANISOU 7552  O   ARG C 115     8025   8523   8911   -373   1524    699       O  
+ATOM   7553  CB  ARG C 115     -27.953  36.981   5.002  1.00 64.18           C  
+ANISOU 7553  CB  ARG C 115     7995   7995   8395   -375   1461    695       C  
+ATOM   7554  CG  ARG C 115     -26.532  36.519   4.740  1.00 62.93           C  
+ANISOU 7554  CG  ARG C 115     8012   7744   8156   -322   1417    645       C  
+ATOM   7555  CD  ARG C 115     -26.472  35.609   3.528  1.00 68.75           C  
+ANISOU 7555  CD  ARG C 115     8862   8306   8953   -381   1286    639       C  
+ATOM   7556  NE  ARG C 115     -25.118  35.115   3.287  1.00 72.77           N  
+ANISOU 7556  NE  ARG C 115     9529   8731   9390   -309   1265    595       N  
+ATOM   7557  CZ  ARG C 115     -24.820  34.069   2.523  1.00 77.31           C  
+ANISOU 7557  CZ  ARG C 115    10241   9147   9986   -332   1175    594       C  
+ATOM   7558  NH1 ARG C 115     -25.784  33.380   1.929  1.00 65.27           N  
+ANISOU 7558  NH1 ARG C 115     8729   7518   8554   -445   1075    630       N  
+ATOM   7559  NH2 ARG C 115     -23.553  33.715   2.352  1.00 80.04           N  
+ANISOU 7559  NH2 ARG C 115    10709   9434  10268   -238   1179    551       N  
+ATOM   7560  N   LEU C 116     -29.814  39.482   6.962  1.00 54.78           N  
+ANISOU 7560  N   LEU C 116     6432   7198   7183   -229   1762    677       N  
+ATOM   7561  CA  LEU C 116     -31.160  40.027   7.108  1.00 45.34           C  
+ANISOU 7561  CA  LEU C 116     5040   6101   6085   -224   1831    714       C  
+ATOM   7562  C   LEU C 116     -31.498  41.089   6.062  1.00 57.55           C  
+ANISOU 7562  C   LEU C 116     6538   7602   7725   -171   1748    616       C  
+ATOM   7563  O   LEU C 116     -32.604  41.106   5.526  1.00 70.55           O  
+ANISOU 7563  O   LEU C 116     8038   9252   9516   -220   1706    670       O  
+ATOM   7564  CB  LEU C 116     -31.337  40.611   8.508  1.00 52.12           C  
+ANISOU 7564  CB  LEU C 116     5841   7134   6828   -121   2014    710       C  
+ATOM   7565  CG  LEU C 116     -31.290  39.580   9.634  1.00 48.70           C  
+ANISOU 7565  CG  LEU C 116     5429   6777   6298   -174   2117    846       C  
+ATOM   7566  CD1 LEU C 116     -31.559  40.240  10.972  1.00 49.08           C  
+ANISOU 7566  CD1 LEU C 116     5429   7013   6205    -55   2306    832       C  
+ATOM   7567  CD2 LEU C 116     -32.282  38.456   9.371  1.00 45.45           C  
+ANISOU 7567  CD2 LEU C 116     4896   6334   6037   -335   2101   1025       C  
+ATOM   7568  N   ILE C 117     -30.548  41.978   5.785  1.00 60.43           N  
+ANISOU 7568  N   ILE C 117     7018   7925   8018    -75   1718    484       N  
+ATOM   7569  CA  ILE C 117     -30.760  43.047   4.813  1.00 57.02           C  
+ANISOU 7569  CA  ILE C 117     6563   7438   7662    -18   1640    401       C  
+ATOM   7570  C   ILE C 117     -31.016  42.475   3.421  1.00 55.96           C  
+ANISOU 7570  C   ILE C 117     6456   7183   7623   -114   1479    438       C  
+ATOM   7571  O   ILE C 117     -32.006  42.815   2.768  1.00 59.02           O  
+ANISOU 7571  O   ILE C 117     6730   7565   8130   -125   1412    461       O  
+ATOM   7572  CB  ILE C 117     -29.563  44.018   4.762  1.00 46.97           C  
+ANISOU 7572  CB  ILE C 117     5423   6123   6301     78   1633    272       C  
+ATOM   7573  CG1 ILE C 117     -29.457  44.796   6.076  1.00 41.90           C  
+ANISOU 7573  CG1 ILE C 117     4759   5591   5571    185   1764    206       C  
+ATOM   7574  CG2 ILE C 117     -29.713  44.988   3.602  1.00 43.87           C  
+ANISOU 7574  CG2 ILE C 117     5031   5646   5990    118   1539    216       C  
+ATOM   7575  CD1 ILE C 117     -28.188  45.613   6.207  1.00 40.87           C  
+ANISOU 7575  CD1 ILE C 117     4759   5412   5358    252   1741     85       C  
+ATOM   7576  N   GLU C 118     -30.117  41.605   2.976  1.00 48.16           N  
+ANISOU 7576  N   GLU C 118     5625   6098   6577   -171   1409    440       N  
+ATOM   7577  CA  GLU C 118     -30.224  40.984   1.663  1.00 57.82           C  
+ANISOU 7577  CA  GLU C 118     6922   7195   7851   -250   1253    455       C  
+ATOM   7578  C   GLU C 118     -31.495  40.139   1.552  1.00 52.45           C  
+ANISOU 7578  C   GLU C 118     6117   6513   7300   -373   1189    562       C  
+ATOM   7579  O   GLU C 118     -32.148  40.102   0.502  1.00 70.84           O  
+ANISOU 7579  O   GLU C 118     8424   8776   9715   -423   1045    568       O  
+ATOM   7580  CB  GLU C 118     -28.985  40.127   1.401  1.00 63.52           C  
+ANISOU 7580  CB  GLU C 118     7836   7821   8476   -265   1222    433       C  
+ATOM   7581  CG  GLU C 118     -27.684  40.801   1.830  1.00 80.82           C  
+ANISOU 7581  CG  GLU C 118    10110  10040  10559   -162   1303    355       C  
+ATOM   7582  CD  GLU C 118     -27.163  40.310   3.170  1.00 73.48           C  
+ANISOU 7582  CD  GLU C 118     9184   9179   9555   -153   1405    388       C  
+ATOM   7583  OE1 GLU C 118     -26.498  39.254   3.197  1.00 48.98           O  
+ANISOU 7583  OE1 GLU C 118     6183   6014   6412   -184   1382    421       O  
+ATOM   7584  OE2 GLU C 118     -27.405  40.986   4.193  1.00 76.42           O  
+ANISOU 7584  OE2 GLU C 118     9470   9666   9901   -103   1503    377       O  
+ATOM   7585  N   LYS C 119     -31.855  39.495   2.658  1.00 52.89           N  
+ANISOU 7585  N   LYS C 119     6084   6644   7369   -424   1292    654       N  
+ATOM   7586  CA  LYS C 119     -33.070  38.693   2.737  1.00 51.65           C  
+ANISOU 7586  CA  LYS C 119     5774   6497   7355   -558   1256    783       C  
+ATOM   7587  C   LYS C 119     -34.307  39.561   2.537  1.00 60.03           C  
+ANISOU 7587  C   LYS C 119     6614   7646   8550   -534   1252    803       C  
+ATOM   7588  O   LYS C 119     -35.194  39.225   1.752  1.00 61.89           O  
+ANISOU 7588  O   LYS C 119     6759   7830   8927   -632   1107    855       O  
+ATOM   7589  CB  LYS C 119     -33.142  37.974   4.085  1.00 52.89           C  
+ANISOU 7589  CB  LYS C 119     5876   6739   7481   -601   1407    896       C  
+ATOM   7590  CG  LYS C 119     -34.207  36.897   4.174  1.00 72.52           C  
+ANISOU 7590  CG  LYS C 119     8228   9205  10120   -773   1367   1057       C  
+ATOM   7591  CD  LYS C 119     -34.141  36.180   5.513  1.00 68.21           C  
+ANISOU 7591  CD  LYS C 119     7659   8739   9518   -810   1529   1186       C  
+ATOM   7592  CE  LYS C 119     -35.110  35.013   5.563  1.00 79.00           C  
+ANISOU 7592  CE  LYS C 119     8905  10058  11055  -1007   1482   1368       C  
+ATOM   7593  NZ  LYS C 119     -35.229  34.333   4.242  1.00 84.59           N  
+ANISOU 7593  NZ  LYS C 119     9698  10561  11881  -1130   1233   1339       N  
+ATOM   7594  N   ALA C 120     -34.359  40.672   3.265  1.00 67.77           N  
+ANISOU 7594  N   ALA C 120     7509   8752   9487   -396   1401    757       N  
+ATOM   7595  CA  ALA C 120     -35.467  41.615   3.166  1.00 69.55           C  
+ANISOU 7595  CA  ALA C 120     7524   9065   9837   -331   1419    764       C  
+ATOM   7596  C   ALA C 120     -35.571  42.194   1.759  1.00 74.26           C  
+ANISOU 7596  C   ALA C 120     8164   9557  10494   -313   1228    700       C  
+ATOM   7597  O   ALA C 120     -36.668  42.342   1.219  1.00 79.13           O  
+ANISOU 7597  O   ALA C 120     8611  10187  11266   -345   1133    755       O  
+ATOM   7598  CB  ALA C 120     -35.310  42.726   4.190  1.00 62.35           C  
+ANISOU 7598  CB  ALA C 120     6573   8278   8839   -162   1609    694       C  
+ATOM   7599  N   LEU C 121     -34.423  42.526   1.175  1.00 65.97           N  
+ANISOU 7599  N   LEU C 121     7336   8411   9321   -260   1173    594       N  
+ATOM   7600  CA  LEU C 121     -34.380  43.036  -0.192  1.00 58.34           C  
+ANISOU 7600  CA  LEU C 121     6451   7343   8373   -240   1002    543       C  
+ATOM   7601  C   LEU C 121     -34.953  42.033  -1.180  1.00 58.86           C  
+ANISOU 7601  C   LEU C 121     6527   7320   8517   -383    803    603       C  
+ATOM   7602  O   LEU C 121     -35.710  42.395  -2.081  1.00 61.75           O  
+ANISOU 7602  O   LEU C 121     6828   7661   8975   -389    653    616       O  
+ATOM   7603  CB  LEU C 121     -32.947  43.377  -0.597  1.00 58.06           C  
+ANISOU 7603  CB  LEU C 121     6653   7225   8182   -176   1003    444       C  
+ATOM   7604  CG  LEU C 121     -32.317  44.626   0.017  1.00 56.69           C  
+ANISOU 7604  CG  LEU C 121     6498   7096   7947    -37   1131    362       C  
+ATOM   7605  CD1 LEU C 121     -30.843  44.708  -0.344  1.00 49.98           C  
+ANISOU 7605  CD1 LEU C 121     5860   6166   6964    -12   1130    293       C  
+ATOM   7606  CD2 LEU C 121     -33.055  45.864  -0.458  1.00 58.19           C  
+ANISOU 7606  CD2 LEU C 121     6589   7289   8231     55   1086    345       C  
+ATOM   7607  N   GLU C 122     -34.583  40.769  -1.010  1.00 57.84           N  
+ANISOU 7607  N   GLU C 122     6493   7133   8352   -496    788    636       N  
+ATOM   7608  CA  GLU C 122     -35.014  39.726  -1.937  1.00 60.77           C  
+ANISOU 7608  CA  GLU C 122     6916   7388   8786   -638    582    672       C  
+ATOM   7609  C   GLU C 122     -36.484  39.351  -1.754  1.00 71.15           C  
+ANISOU 7609  C   GLU C 122     7972   8754  10309   -757    518    793       C  
+ATOM   7610  O   GLU C 122     -37.151  38.938  -2.706  1.00 83.57           O  
+ANISOU 7610  O   GLU C 122     9531  10246  11975   -857    300    814       O  
+ATOM   7611  CB  GLU C 122     -34.123  38.495  -1.798  1.00 58.79           C  
+ANISOU 7611  CB  GLU C 122     6860   7034   8442   -709    584    665       C  
+ATOM   7612  CG  GLU C 122     -32.751  38.713  -2.416  1.00 75.47           C  
+ANISOU 7612  CG  GLU C 122     9230   9069  10377   -610    585    550       C  
+ATOM   7613  CD  GLU C 122     -31.671  37.804  -1.857  1.00101.56           C  
+ANISOU 7613  CD  GLU C 122    12686  12322  13582   -615    669    542       C  
+ATOM   7614  OE1 GLU C 122     -32.002  36.748  -1.279  1.00107.24           O  
+ANISOU 7614  OE1 GLU C 122    13370  13012  14366   -723    669    624       O  
+ATOM   7615  OE2 GLU C 122     -30.482  38.161  -1.995  1.00101.00           O  
+ANISOU 7615  OE2 GLU C 122    12760  12236  13378   -510    735    464       O  
+ATOM   7616  N   GLU C 123     -36.978  39.465  -0.525  1.00 69.18           N  
+ANISOU 7616  N   GLU C 123     7516   8643  10126   -747    705    876       N  
+ATOM   7617  CA  GLU C 123     -38.392  39.242  -0.252  1.00 62.79           C  
+ANISOU 7617  CA  GLU C 123     6412   7915   9530   -844    687   1009       C  
+ATOM   7618  C   GLU C 123     -39.234  40.334  -0.905  1.00 67.29           C  
+ANISOU 7618  C   GLU C 123     6819   8537  10210   -759    597    993       C  
+ATOM   7619  O   GLU C 123     -40.427  40.152  -1.148  1.00 86.59           O  
+ANISOU 7619  O   GLU C 123     9030  11014  12854   -848    491   1091       O  
+ATOM   7620  CB  GLU C 123     -38.652  39.193   1.254  1.00 65.35           C  
+ANISOU 7620  CB  GLU C 123     6566   8397   9867   -824    949   1104       C  
+ATOM   7621  N   GLU C 124     -38.604  41.472  -1.178  1.00 69.69           N  
+ANISOU 7621  N   GLU C 124     7239   8842  10397   -589    633    878       N  
+ATOM   7622  CA  GLU C 124     -39.254  42.572  -1.881  1.00 68.73           C  
+ANISOU 7622  CA  GLU C 124     7010   8742  10362   -488    533    858       C  
+ATOM   7623  C   GLU C 124     -38.946  42.523  -3.374  1.00 72.26           C  
+ANISOU 7623  C   GLU C 124     7661   9044  10749   -519    277    799       C  
+ATOM   7624  O   GLU C 124     -39.161  43.500  -4.092  1.00 72.31           O  
+ANISOU 7624  O   GLU C 124     7665   9041  10770   -416    184    768       O  
+ATOM   7625  CB  GLU C 124     -38.821  43.918  -1.296  1.00 66.06           C  
+ANISOU 7625  CB  GLU C 124     6678   8476   9946   -282    718    777       C  
+ATOM   7626  CG  GLU C 124     -39.949  44.930  -1.178  1.00 74.46           C  
+ANISOU 7626  CG  GLU C 124     7478   9640  11175   -165    742    814       C  
+ATOM   7627  CD  GLU C 124     -41.143  44.390  -0.417  1.00 90.83           C  
+ANISOU 7627  CD  GLU C 124     9236  11847  13430   -237    827    947       C  
+ATOM   7628  OE1 GLU C 124     -42.261  44.412  -0.973  1.00 96.10           O  
+ANISOU 7628  OE1 GLU C 124     9683  12537  14293   -277    683   1031       O  
+ATOM   7629  OE2 GLU C 124     -40.965  43.949   0.738  1.00101.31           O  
+ANISOU 7629  OE2 GLU C 124    10528  13261  14704   -253   1038    979       O  
+ATOM   7630  N   ASN C 125     -38.429  41.382  -3.821  1.00 70.06           N  
+ANISOU 7630  N   ASN C 125     7575   8650  10394   -649    168    784       N  
+ATOM   7631  CA  ASN C 125     -38.077  41.164  -5.223  1.00 74.42           C  
+ANISOU 7631  CA  ASN C 125     8359   9064  10852   -678    -66    719       C  
+ATOM   7632  C   ASN C 125     -37.061  42.167  -5.761  1.00 75.00           C  
+ANISOU 7632  C   ASN C 125     8643   9107  10746   -520    -23    621       C  
+ATOM   7633  O   ASN C 125     -37.132  42.572  -6.921  1.00 82.07           O  
+ANISOU 7633  O   ASN C 125     9646   9944  11595   -488   -197    594       O  
+ATOM   7634  CB  ASN C 125     -39.332  41.174  -6.098  1.00 76.50           C  
+ANISOU 7634  CB  ASN C 125     8474   9315  11277   -751   -323    778       C  
+ATOM   7635  CG  ASN C 125     -40.193  39.946  -5.889  1.00 89.54           C  
+ANISOU 7635  CG  ASN C 125     9976  10944  13101   -955   -434    871       C  
+ATOM   7636  OD1 ASN C 125     -39.682  38.849  -5.663  1.00 91.92           O  
+ANISOU 7636  OD1 ASN C 125    10417  11159  13348  -1063   -421    863       O  
+ATOM   7637  ND2 ASN C 125     -41.506  40.122  -5.965  1.00 93.68           N  
+ANISOU 7637  ND2 ASN C 125    10207  11537  13850  -1010   -549    970       N  
+ATOM   7638  N   LYS C 126     -36.119  42.566  -4.914  1.00 69.21           N  
+ANISOU 7638  N   LYS C 126     7967   8416   9914   -428    203    577       N  
+ATOM   7639  CA  LYS C 126     -35.023  43.416  -5.355  1.00 67.68           C  
+ANISOU 7639  CA  LYS C 126     7970   8182   9562   -304    255    495       C  
+ATOM   7640  C   LYS C 126     -33.749  42.583  -5.428  1.00 64.70           C  
+ANISOU 7640  C   LYS C 126     7833   7730   9021   -334    303    440       C  
+ATOM   7641  O   LYS C 126     -33.573  41.638  -4.659  1.00 62.89           O  
+ANISOU 7641  O   LYS C 126     7591   7506   8799   -407    376    458       O  
+ATOM   7642  CB  LYS C 126     -34.834  44.604  -4.408  1.00 65.54           C  
+ANISOU 7642  CB  LYS C 126     7593   8000   9310   -171    450    475       C  
+ATOM   7643  CG  LYS C 126     -35.969  45.616  -4.434  1.00 67.83           C  
+ANISOU 7643  CG  LYS C 126     7671   8350   9753    -94    414    514       C  
+ATOM   7644  CD  LYS C 126     -35.619  46.853  -3.622  1.00 65.22           C  
+ANISOU 7644  CD  LYS C 126     7298   8067   9414     57    594    463       C  
+ATOM   7645  CE  LYS C 126     -36.748  47.871  -3.647  1.00 67.08           C  
+ANISOU 7645  CE  LYS C 126     7328   8349   9809    161    564    496       C  
+ATOM   7646  NZ  LYS C 126     -36.398  49.105  -2.889  1.00 64.74           N  
+ANISOU 7646  NZ  LYS C 126     7022   8071   9504    319    725    427       N  
+ATOM   7647  N   ILE C 127     -32.862  42.932  -6.353  1.00 64.27           N  
+ANISOU 7647  N   ILE C 127     7992   7607   8822   -270    268    383       N  
+ATOM   7648  CA  ILE C 127     -31.620  42.190  -6.520  1.00 61.69           C  
+ANISOU 7648  CA  ILE C 127     7883   7213   8342   -273    321    330       C  
+ATOM   7649  C   ILE C 127     -30.495  42.867  -5.745  1.00 57.97           C  
+ANISOU 7649  C   ILE C 127     7429   6788   7807   -180    526    298       C  
+ATOM   7650  O   ILE C 127     -30.190  44.038  -5.970  1.00 58.10           O  
+ANISOU 7650  O   ILE C 127     7452   6821   7804    -92    567    284       O  
+ATOM   7651  CB  ILE C 127     -31.236  42.062  -8.004  1.00 62.39           C  
+ANISOU 7651  CB  ILE C 127     8204   7210   8293   -254    181    291       C  
+ATOM   7652  CG1 ILE C 127     -32.214  41.127  -8.720  1.00 65.83           C  
+ANISOU 7652  CG1 ILE C 127     8663   7577   8772   -366    -49    302       C  
+ATOM   7653  CG2 ILE C 127     -29.818  41.541  -8.143  1.00 59.93           C  
+ANISOU 7653  CG2 ILE C 127     8099   6848   7821   -212    285    235       C  
+ATOM   7654  CD1 ILE C 127     -32.276  41.332 -10.217  1.00 68.25           C  
+ANISOU 7654  CD1 ILE C 127     9156   7820   8955   -334   -229    273       C  
+ATOM   7655  N   ALA C 128     -29.881  42.121  -4.832  1.00 55.37           N  
+ANISOU 7655  N   ALA C 128     7111   6473   7454   -205    637    291       N  
+ATOM   7656  CA  ALA C 128     -28.843  42.671  -3.970  1.00 53.40           C  
+ANISOU 7656  CA  ALA C 128     6862   6274   7154   -130    808    260       C  
+ATOM   7657  C   ALA C 128     -27.442  42.248  -4.399  1.00 51.67           C  
+ANISOU 7657  C   ALA C 128     6832   5996   6805    -96    849    220       C  
+ATOM   7658  O   ALA C 128     -27.151  41.058  -4.516  1.00 51.16           O  
+ANISOU 7658  O   ALA C 128     6866   5876   6698   -139    821    218       O  
+ATOM   7659  CB  ALA C 128     -29.093  42.258  -2.526  1.00 50.94           C  
+ANISOU 7659  CB  ALA C 128     6417   6040   6896   -162    914    290       C  
+ATOM   7660  N   ASP C 129     -26.581  43.233  -4.634  1.00 48.89           N  
+ANISOU 7660  N   ASP C 129     6524   5652   6402    -17    918    194       N  
+ATOM   7661  CA  ASP C 129     -25.170  42.973  -4.888  1.00 47.16           C  
+ANISOU 7661  CA  ASP C 129     6435   5403   6080     27    991    169       C  
+ATOM   7662  C   ASP C 129     -24.441  42.960  -3.553  1.00 45.47           C  
+ANISOU 7662  C   ASP C 129     6146   5248   5881     41   1111    158       C  
+ATOM   7663  O   ASP C 129     -24.082  44.011  -3.022  1.00 52.49           O  
+ANISOU 7663  O   ASP C 129     6966   6179   6798     80   1177    142       O  
+ATOM   7664  CB  ASP C 129     -24.578  44.034  -5.819  1.00 49.13           C  
+ANISOU 7664  CB  ASP C 129     6754   5632   6279     89   1009    169       C  
+ATOM   7665  CG  ASP C 129     -23.215  43.644  -6.363  1.00 58.49           C  
+ANISOU 7665  CG  ASP C 129     8073   6792   7357    135   1083    159       C  
+ATOM   7666  OD1 ASP C 129     -22.592  42.706  -5.822  1.00 65.33           O  
+ANISOU 7666  OD1 ASP C 129     8960   7661   8203    135   1133    143       O  
+ATOM   7667  OD2 ASP C 129     -22.767  44.283  -7.338  1.00 61.90           O  
+ANISOU 7667  OD2 ASP C 129     8587   7205   7728    178   1098    179       O  
+ATOM   7668  N   VAL C 130     -24.226  41.765  -3.014  1.00 43.91           N  
+ANISOU 7668  N   VAL C 130     5976   5043   5666     10   1124    167       N  
+ATOM   7669  CA  VAL C 130     -23.654  41.627  -1.682  1.00 45.07           C  
+ANISOU 7669  CA  VAL C 130     6058   5253   5816     21   1215    169       C  
+ATOM   7670  C   VAL C 130     -22.143  41.449  -1.737  1.00 44.57           C  
+ANISOU 7670  C   VAL C 130     6070   5175   5689     80   1276    151       C  
+ATOM   7671  O   VAL C 130     -21.643  40.499  -2.339  1.00 60.88           O  
+ANISOU 7671  O   VAL C 130     8247   7177   7706     94   1262    153       O  
+ATOM   7672  CB  VAL C 130     -24.273  40.433  -0.945  1.00 49.65           C  
+ANISOU 7672  CB  VAL C 130     6612   5834   6419    -45   1197    215       C  
+ATOM   7673  CG1 VAL C 130     -23.818  40.412   0.504  1.00 44.11           C  
+ANISOU 7673  CG1 VAL C 130     5844   5216   5701    -28   1288    229       C  
+ATOM   7674  CG2 VAL C 130     -25.782  40.511  -1.021  1.00 45.68           C  
+ANISOU 7674  CG2 VAL C 130     6011   5345   5999   -112   1134    250       C  
+ATOM   7675  N   LYS C 131     -21.420  42.363  -1.100  1.00 50.72           N  
+ANISOU 7675  N   LYS C 131     6783   6010   6477    117   1341    131       N  
+ATOM   7676  CA  LYS C 131     -19.963  42.335  -1.115  1.00 48.75           C  
+ANISOU 7676  CA  LYS C 131     6564   5762   6198    166   1395    125       C  
+ATOM   7677  C   LYS C 131     -19.392  42.212   0.296  1.00 47.49           C  
+ANISOU 7677  C   LYS C 131     6336   5668   6038    174   1428    122       C  
+ATOM   7678  O   LYS C 131     -19.605  43.089   1.133  1.00 42.65           O  
+ANISOU 7678  O   LYS C 131     5645   5111   5448    168   1436     93       O  
+ATOM   7679  CB  LYS C 131     -19.417  43.587  -1.804  1.00 54.80           C  
+ANISOU 7679  CB  LYS C 131     7319   6520   6984    192   1421    115       C  
+ATOM   7680  CG  LYS C 131     -20.115  43.916  -3.117  1.00 58.29           C  
+ANISOU 7680  CG  LYS C 131     7830   6909   7411    188   1379    127       C  
+ATOM   7681  CD  LYS C 131     -19.434  45.063  -3.845  1.00 53.55           C  
+ANISOU 7681  CD  LYS C 131     7234   6292   6822    213   1418    145       C  
+ATOM   7682  CE  LYS C 131     -20.094  45.332  -5.189  1.00 53.83           C  
+ANISOU 7682  CE  LYS C 131     7361   6279   6815    218   1369    171       C  
+ATOM   7683  NZ  LYS C 131     -19.952  44.182  -6.124  1.00 58.26           N  
+ANISOU 7683  NZ  LYS C 131     8061   6807   7268    244   1359    174       N  
+ATOM   7684  N   TYR C 132     -18.668  41.128   0.559  1.00 41.34           N  
+ANISOU 7684  N   TYR C 132     5600   4881   5228    198   1438    147       N  
+ATOM   7685  CA  TYR C 132     -17.983  40.969   1.840  1.00 44.10           C  
+ANISOU 7685  CA  TYR C 132     5897   5295   5565    215   1452    154       C  
+ATOM   7686  C   TYR C 132     -16.524  40.551   1.651  1.00 51.47           C  
+ANISOU 7686  C   TYR C 132     6842   6217   6497    278   1474    169       C  
+ATOM   7687  O   TYR C 132     -15.770  40.453   2.618  1.00 58.25           O  
+ANISOU 7687  O   TYR C 132     7652   7129   7351    301   1467    179       O  
+ATOM   7688  CB  TYR C 132     -18.720  39.974   2.744  1.00 41.09           C  
+ANISOU 7688  CB  TYR C 132     5529   4930   5154    182   1436    198       C  
+ATOM   7689  CG  TYR C 132     -19.233  38.728   2.063  1.00 44.39           C  
+ANISOU 7689  CG  TYR C 132     6037   5254   5573    158   1406    239       C  
+ATOM   7690  CD1 TYR C 132     -18.408  37.629   1.866  1.00 43.89           C  
+ANISOU 7690  CD1 TYR C 132     6056   5126   5494    204   1400    265       C  
+ATOM   7691  CD2 TYR C 132     -20.552  38.643   1.637  1.00 44.41           C  
+ANISOU 7691  CD2 TYR C 132     6043   5227   5605     90   1371    249       C  
+ATOM   7692  CE1 TYR C 132     -18.880  36.485   1.252  1.00 42.99           C  
+ANISOU 7692  CE1 TYR C 132     6049   4901   5385    182   1357    287       C  
+ATOM   7693  CE2 TYR C 132     -21.033  37.504   1.023  1.00 41.88           C  
+ANISOU 7693  CE2 TYR C 132     5811   4804   5297     51   1316    279       C  
+ATOM   7694  CZ  TYR C 132     -20.193  36.428   0.833  1.00 44.58           C  
+ANISOU 7694  CZ  TYR C 132     6259   5065   5615     96   1307    291       C  
+ATOM   7695  OH  TYR C 132     -20.669  35.291   0.221  1.00 48.81           O  
+ANISOU 7695  OH  TYR C 132     6906   5473   6166     58   1237    306       O  
+ATOM   7696  N   THR C 133     -16.132  40.301   0.406  1.00 52.48           N  
+ANISOU 7696  N   THR C 133     7033   6283   6623    316   1501    173       N  
+ATOM   7697  CA  THR C 133     -14.728  40.057   0.093  1.00 41.69           C  
+ANISOU 7697  CA  THR C 133     5653   4920   5269    392   1549    190       C  
+ATOM   7698  C   THR C 133     -14.189  41.231  -0.721  1.00 49.18           C  
+ANISOU 7698  C   THR C 133     6553   5883   6253    395   1599    185       C  
+ATOM   7699  O   THR C 133     -14.961  42.016  -1.272  1.00 69.04           O  
+ANISOU 7699  O   THR C 133     9087   8378   8767    351   1590    170       O  
+ATOM   7700  CB  THR C 133     -14.524  38.743  -0.689  1.00 40.12           C  
+ANISOU 7700  CB  THR C 133     5576   4641   5028    461   1567    202       C  
+ATOM   7701  OG1 THR C 133     -14.991  38.901  -2.034  1.00 48.99           O  
+ANISOU 7701  OG1 THR C 133     6795   5708   6111    464   1583    179       O  
+ATOM   7702  CG2 THR C 133     -15.269  37.595  -0.020  1.00 41.76           C  
+ANISOU 7702  CG2 THR C 133     5850   4801   5217    433   1505    220       C  
+ATOM   7703  N   VAL C 134     -12.868  41.360  -0.784  1.00 44.05           N  
+ANISOU 7703  N   VAL C 134     5827   5265   5645    446   1651    213       N  
+ATOM   7704  CA  VAL C 134     -12.241  42.433  -1.551  1.00 50.37           C  
+ANISOU 7704  CA  VAL C 134     6567   6079   6494    439   1712    236       C  
+ATOM   7705  C   VAL C 134     -12.502  42.276  -3.046  1.00 52.68           C  
+ANISOU 7705  C   VAL C 134     6978   6323   6717    479   1780    250       C  
+ATOM   7706  O   VAL C 134     -12.801  43.249  -3.741  1.00 64.76           O  
+ANISOU 7706  O   VAL C 134     8516   7839   8249    441   1797    265       O  
+ATOM   7707  CB  VAL C 134     -10.720  42.487  -1.294  1.00 56.12           C  
+ANISOU 7707  CB  VAL C 134     7161   6860   7302    481   1758    281       C  
+ATOM   7708  CG1 VAL C 134      -9.987  43.154  -2.451  1.00 66.02           C  
+ANISOU 7708  CG1 VAL C 134     8374   8120   8591    498   1868    338       C  
+ATOM   7709  CG2 VAL C 134     -10.443  43.216  -0.003  1.00 64.30           C  
+ANISOU 7709  CG2 VAL C 134     8075   7943   8415    414   1670    261       C  
+ATOM   7710  N   LYS C 135     -12.407  41.042  -3.528  1.00 44.61           N  
+ANISOU 7710  N   LYS C 135     6063   5265   5622    560   1808    244       N  
+ATOM   7711  CA  LYS C 135     -12.581  40.753  -4.946  1.00 43.15           C  
+ANISOU 7711  CA  LYS C 135     6022   5034   5338    618   1865    241       C  
+ATOM   7712  C   LYS C 135     -13.981  41.124  -5.439  1.00 44.86           C  
+ANISOU 7712  C   LYS C 135     6340   5203   5501    546   1783    212       C  
+ATOM   7713  O   LYS C 135     -14.144  41.584  -6.571  1.00 50.49           O  
+ANISOU 7713  O   LYS C 135     7134   5902   6148    561   1816    227       O  
+ATOM   7714  CB  LYS C 135     -12.285  39.277  -5.221  1.00 41.26           C  
+ANISOU 7714  CB  LYS C 135     5900   4743   5032    726   1886    215       C  
+ATOM   7715  CG  LYS C 135     -10.802  38.934  -5.136  1.00 40.82           C  
+ANISOU 7715  CG  LYS C 135     5751   4737   5021    837   1996    255       C  
+ATOM   7716  CD  LYS C 135     -10.534  37.472  -5.454  1.00 57.99           C  
+ANISOU 7716  CD  LYS C 135     8060   6841   7133    968   2019    220       C  
+ATOM   7717  CE  LYS C 135      -9.073  37.116  -5.226  1.00 71.41           C  
+ANISOU 7717  CE  LYS C 135     9636   8597   8902   1094   2122    266       C  
+ATOM   7718  NZ  LYS C 135      -8.750  35.744  -5.707  1.00 83.23           N  
+ANISOU 7718  NZ  LYS C 135    11280  10011  10334   1254   2164    226       N  
+ATOM   7719  N   GLN C 136     -14.985  40.941  -4.584  1.00 48.53           N  
+ANISOU 7719  N   GLN C 136     6793   5652   5996    473   1678    182       N  
+ATOM   7720  CA  GLN C 136     -16.367  41.255  -4.946  1.00 56.16           C  
+ANISOU 7720  CA  GLN C 136     7817   6580   6939    405   1589    161       C  
+ATOM   7721  C   GLN C 136     -16.592  42.738  -5.240  1.00 62.79           C  
+ANISOU 7721  C   GLN C 136     8595   7445   7818    365   1595    184       C  
+ATOM   7722  O   GLN C 136     -17.601  43.109  -5.841  1.00 71.88           O  
+ANISOU 7722  O   GLN C 136     9802   8565   8944    333   1530    180       O  
+ATOM   7723  CB  GLN C 136     -17.330  40.812  -3.842  1.00 43.70           C  
+ANISOU 7723  CB  GLN C 136     6198   5001   5406    337   1503    144       C  
+ATOM   7724  CG  GLN C 136     -17.621  39.324  -3.818  1.00 44.29           C  
+ANISOU 7724  CG  GLN C 136     6376   5008   5444    346   1457    132       C  
+ATOM   7725  CD  GLN C 136     -18.502  38.927  -2.650  1.00 54.12           C  
+ANISOU 7725  CD  GLN C 136     7559   6264   6741    269   1394    146       C  
+ATOM   7726  OE1 GLN C 136     -18.338  39.423  -1.534  1.00 50.41           O  
+ANISOU 7726  OE1 GLN C 136     6971   5869   6312    251   1418    159       O  
+ATOM   7727  NE2 GLN C 136     -19.461  38.045  -2.906  1.00 53.57           N  
+ANISOU 7727  NE2 GLN C 136     7569   6119   6665    219   1312    144       N  
+ATOM   7728  N   LEU C 137     -15.658  43.584  -4.817  1.00 55.81           N  
+ANISOU 7728  N   LEU C 137     7595   6606   7004    363   1658    212       N  
+ATOM   7729  CA  LEU C 137     -15.750  45.013  -5.093  1.00 44.83           C  
+ANISOU 7729  CA  LEU C 137     6153   5212   5668    323   1662    240       C  
+ATOM   7730  C   LEU C 137     -15.477  45.293  -6.565  1.00 51.44           C  
+ANISOU 7730  C   LEU C 137     7086   6028   6430    361   1725    297       C  
+ATOM   7731  O   LEU C 137     -15.871  46.332  -7.093  1.00 59.53           O  
+ANISOU 7731  O   LEU C 137     8121   7027   7470    332   1708    333       O  
+ATOM   7732  CB  LEU C 137     -14.770  45.800  -4.220  1.00 36.40           C  
+ANISOU 7732  CB  LEU C 137     4939   4180   4710    295   1692    253       C  
+ATOM   7733  CG  LEU C 137     -15.032  45.797  -2.713  1.00 47.88           C  
+ANISOU 7733  CG  LEU C 137     6311   5664   6219    260   1624    194       C  
+ATOM   7734  CD1 LEU C 137     -13.882  46.459  -1.973  1.00 54.14           C  
+ANISOU 7734  CD1 LEU C 137     6978   6486   7106    236   1634    200       C  
+ATOM   7735  CD2 LEU C 137     -16.346  46.489  -2.392  1.00 46.19           C  
+ANISOU 7735  CD2 LEU C 137     6101   5425   6022    220   1551    152       C  
+ATOM   7736  N   ALA C 138     -14.800  44.356  -7.221  1.00 62.34           N  
+ANISOU 7736  N   ALA C 138     8548   7418   7720    438   1802    306       N  
+ATOM   7737  CA  ALA C 138     -14.446  44.502  -8.629  1.00 56.19           C  
+ANISOU 7737  CA  ALA C 138     7881   6637   6833    497   1887    360       C  
+ATOM   7738  C   ALA C 138     -15.614  44.165  -9.553  1.00 63.45           C  
+ANISOU 7738  C   ALA C 138     8982   7505   7623    506   1794    328       C  
+ATOM   7739  O   ALA C 138     -15.570  44.453 -10.748  1.00 83.78           O  
+ANISOU 7739  O   ALA C 138    11675  10077  10083    547   1835    372       O  
+ATOM   7740  CB  ALA C 138     -13.244  43.630  -8.964  1.00 40.82           C  
+ANISOU 7740  CB  ALA C 138     5953   4727   4832    601   2020    373       C  
+ATOM   7741  N   THR C 139     -16.657  43.555  -8.998  1.00 49.38           N  
+ANISOU 7741  N   THR C 139     7218   5686   5858    464   1663    259       N  
+ATOM   7742  CA  THR C 139     -17.794  43.117  -9.801  1.00 61.34           C  
+ANISOU 7742  CA  THR C 139     8887   7147   7273    458   1543    224       C  
+ATOM   7743  C   THR C 139     -19.015  44.021  -9.671  1.00 62.60           C  
+ANISOU 7743  C   THR C 139     8991   7293   7502    381   1422    238       C  
+ATOM   7744  O   THR C 139     -19.182  44.729  -8.679  1.00 61.74           O  
+ANISOU 7744  O   THR C 139     8728   7207   7526    331   1418    245       O  
+ATOM   7745  CB  THR C 139     -18.223  41.687  -9.424  1.00 62.55           C  
+ANISOU 7745  CB  THR C 139     9106   7252   7409    455   1464    150       C  
+ATOM   7746  OG1 THR C 139     -18.898  41.707  -8.159  1.00 63.66           O  
+ANISOU 7746  OG1 THR C 139     9105   7402   7682    371   1395    140       O  
+ATOM   7747  CG2 THR C 139     -17.013  40.768  -9.341  1.00 52.40           C  
+ANISOU 7747  CG2 THR C 139     7856   5970   6085    546   1579    133       C  
+ATOM   7748  N   THR C 140     -19.862  43.986 -10.694  1.00 63.35           N  
+ANISOU 7748  N   THR C 140     9218   7351   7502    383   1319    237       N  
+ATOM   7749  CA  THR C 140     -21.123  44.717 -10.687  1.00 49.64           C  
+ANISOU 7749  CA  THR C 140     7430   5599   5834    327   1185    253       C  
+ATOM   7750  C   THR C 140     -22.254  43.773 -11.079  1.00 51.18           C  
+ANISOU 7750  C   THR C 140     7716   5748   5982    295   1017    203       C  
+ATOM   7751  O   THR C 140     -22.362  43.374 -12.238  1.00 55.97           O  
+ANISOU 7751  O   THR C 140     8506   6321   6438    330    955    191       O  
+ATOM   7752  CB  THR C 140     -21.092  45.919 -11.655  1.00 60.89           C  
+ANISOU 7752  CB  THR C 140     8906   7021   7210    353   1193    333       C  
+ATOM   7753  OG1 THR C 140     -20.004  46.787 -11.314  1.00 60.36           O  
+ANISOU 7753  OG1 THR C 140     8748   6979   7206    363   1342    389       O  
+ATOM   7754  CG2 THR C 140     -22.400  46.698 -11.593  1.00 66.03           C  
+ANISOU 7754  CG2 THR C 140     9488   7649   7951    313   1048    352       C  
+ATOM   7755  N   LYS C 141     -23.093  43.414 -10.111  1.00 53.71           N  
+ANISOU 7755  N   LYS C 141     7911   6068   6428    225    942    176       N  
+ATOM   7756  CA  LYS C 141     -24.172  42.460 -10.353  1.00 56.23           C  
+ANISOU 7756  CA  LYS C 141     8283   6338   6745    167    776    141       C  
+ATOM   7757  C   LYS C 141     -25.219  43.020 -11.306  1.00 67.32           C  
+ANISOU 7757  C   LYS C 141     9728   7724   8125    153    615    167       C  
+ATOM   7758  O   LYS C 141     -25.690  44.146 -11.140  1.00 67.62           O  
+ANISOU 7758  O   LYS C 141     9646   7795   8250    153    604    216       O  
+ATOM   7759  CB  LYS C 141     -24.841  42.041  -9.044  1.00 52.62           C  
+ANISOU 7759  CB  LYS C 141     7651   5899   6442     88    755    137       C  
+ATOM   7760  CG  LYS C 141     -25.647  40.752  -9.161  1.00 54.83           C  
+ANISOU 7760  CG  LYS C 141     7988   6112   6734     13    612    108       C  
+ATOM   7761  CD  LYS C 141     -26.321  40.379  -7.852  1.00 60.03           C  
+ANISOU 7761  CD  LYS C 141     8462   6801   7547    -71    615    134       C  
+ATOM   7762  CE  LYS C 141     -26.817  38.937  -7.869  1.00 63.29           C  
+ANISOU 7762  CE  LYS C 141     8941   7124   7980   -157    500    119       C  
+ATOM   7763  NZ  LYS C 141     -25.788  37.981  -8.353  1.00 84.25           N  
+ANISOU 7763  NZ  LYS C 141    11808   9694  10509   -101    528     61       N  
+ATOM   7764  N   VAL C 142     -25.573  42.219 -12.306  1.00 63.11           N  
+ANISOU 7764  N   VAL C 142     9376   7131   7472    148    478    128       N  
+ATOM   7765  CA  VAL C 142     -26.529  42.618 -13.329  1.00 64.02           C  
+ANISOU 7765  CA  VAL C 142     9560   7227   7537    138    292    150       C  
+ATOM   7766  C   VAL C 142     -27.903  42.875 -12.706  1.00 64.50           C  
+ANISOU 7766  C   VAL C 142     9407   7304   7796     51    155    181       C  
+ATOM   7767  O   VAL C 142     -28.351  42.115 -11.848  1.00 74.93           O  
+ANISOU 7767  O   VAL C 142    10613   8618   9239    -28    134    162       O  
+ATOM   7768  CB  VAL C 142     -26.634  41.538 -14.428  1.00 65.10           C  
+ANISOU 7768  CB  VAL C 142     9951   7287   7498    144    149     79       C  
+ATOM   7769  CG1 VAL C 142     -27.684  41.913 -15.457  1.00 66.97           C  
+ANISOU 7769  CG1 VAL C 142    10259   7506   7679    126    -81    100       C  
+ATOM   7770  CG2 VAL C 142     -25.291  41.354 -15.107  1.00 74.53           C  
+ANISOU 7770  CG2 VAL C 142    11354   8481   8484    259    309     51       C  
+ATOM   7771  N   LYS C 143     -28.553  43.956 -13.138  1.00 63.00           N  
+ANISOU 7771  N   LYS C 143     9159   7137   7640     73     74    242       N  
+ATOM   7772  CA  LYS C 143     -29.918  44.294 -12.725  1.00 77.07           C  
+ANISOU 7772  CA  LYS C 143    10733   8943   9609     16    -63    280       C  
+ATOM   7773  C   LYS C 143     -30.048  44.509 -11.218  1.00 78.13           C  
+ANISOU 7773  C   LYS C 143    10621   9134   9932     -8     77    289       C  
+ATOM   7774  O   LYS C 143     -31.137  44.361 -10.662  1.00 79.32           O  
+ANISOU 7774  O   LYS C 143    10585   9312  10242    -69     -2    311       O  
+ATOM   7775  CB  LYS C 143     -30.907  43.204 -13.158  1.00 73.73           C  
+ANISOU 7775  CB  LYS C 143    10340   8471   9203    -80   -294    251       C  
+ATOM   7776  CG  LYS C 143     -30.943  42.916 -14.648  1.00 71.67           C  
+ANISOU 7776  CG  LYS C 143    10340   8151   8741    -58   -475    223       C  
+ATOM   7777  CD  LYS C 143     -31.447  44.102 -15.446  1.00 85.64           C  
+ANISOU 7777  CD  LYS C 143    12111   9946  10483      4   -582    298       C  
+ATOM   7778  CE  LYS C 143     -31.652  43.718 -16.902  1.00 96.84           C  
+ANISOU 7778  CE  LYS C 143    13794  11312  11687     16   -800    271       C  
+ATOM   7779  NZ  LYS C 143     -32.545  42.532 -17.033  1.00 95.66           N  
+ANISOU 7779  NZ  LYS C 143    13651  11103  11592   -102  -1040    208       N  
+ATOM   7780  N   ARG C 144     -28.948  44.859 -10.559  1.00 71.71           N  
+ANISOU 7780  N   ARG C 144     9805   8345   9096     40    282    276       N  
+ATOM   7781  CA  ARG C 144     -28.977  45.080  -9.118  1.00 62.03           C  
+ANISOU 7781  CA  ARG C 144     8381   7177   8011     29    414    273       C  
+ATOM   7782  C   ARG C 144     -29.811  46.307  -8.764  1.00 61.32           C  
+ANISOU 7782  C   ARG C 144     8115   7124   8060     69    400    312       C  
+ATOM   7783  O   ARG C 144     -29.859  47.278  -9.519  1.00 77.44           O  
+ANISOU 7783  O   ARG C 144    10204   9139  10081    129    352    346       O  
+ATOM   7784  CB  ARG C 144     -27.557  45.227  -8.562  1.00 58.32           C  
+ANISOU 7784  CB  ARG C 144     7959   6719   7480     72    606    247       C  
+ATOM   7785  CG  ARG C 144     -26.843  46.499  -8.984  1.00 53.61           C  
+ANISOU 7785  CG  ARG C 144     7407   6113   6848    146    678    274       C  
+ATOM   7786  CD  ARG C 144     -25.379  46.469  -8.587  1.00 50.77           C  
+ANISOU 7786  CD  ARG C 144     7094   5762   6432    171    844    255       C  
+ATOM   7787  NE  ARG C 144     -24.725  47.750  -8.835  1.00 51.05           N  
+ANISOU 7787  NE  ARG C 144     7138   5783   6476    219    915    294       N  
+ATOM   7788  CZ  ARG C 144     -23.446  48.000  -8.577  1.00 47.69           C  
+ANISOU 7788  CZ  ARG C 144     6726   5363   6031    235   1048    297       C  
+ATOM   7789  NH1 ARG C 144     -22.672  47.054  -8.064  1.00 51.80           N  
+ANISOU 7789  NH1 ARG C 144     7254   5912   6515    225   1125    259       N  
+ATOM   7790  NH2 ARG C 144     -22.940  49.198  -8.836  1.00 47.37           N  
+ANISOU 7790  NH2 ARG C 144     6683   5293   6021    258   1097    346       N  
+ATOM   7791  N   ASP C 145     -30.477  46.251  -7.615  1.00 59.63           N  
+ANISOU 7791  N   ASP C 145     7702   6969   7984     46    447    311       N  
+ATOM   7792  CA  ASP C 145     -31.246  47.384  -7.117  1.00 60.92           C  
+ANISOU 7792  CA  ASP C 145     7689   7173   8286    108    464    332       C  
+ATOM   7793  C   ASP C 145     -30.528  48.057  -5.955  1.00 58.74           C  
+ANISOU 7793  C   ASP C 145     7361   6929   8029    165    650    289       C  
+ATOM   7794  O   ASP C 145     -30.697  49.253  -5.715  1.00 61.44           O  
+ANISOU 7794  O   ASP C 145     7637   7264   8441    248    683    283       O  
+ATOM   7795  CB  ASP C 145     -32.645  46.940  -6.685  1.00 66.57           C  
+ANISOU 7795  CB  ASP C 145     8199   7946   9148     58    389    368       C  
+ATOM   7796  CG  ASP C 145     -33.445  46.345  -7.825  1.00 72.29           C  
+ANISOU 7796  CG  ASP C 145     8959   8631   9877     -9    165    408       C  
+ATOM   7797  OD1 ASP C 145     -33.590  45.105  -7.869  1.00 67.67           O  
+ANISOU 7797  OD1 ASP C 145     8404   8031   9278   -117    101    407       O  
+ATOM   7798  OD2 ASP C 145     -33.926  47.117  -8.682  1.00 95.00           O  
+ANISOU 7798  OD2 ASP C 145    11843  11481  12771     44     38    442       O  
+ATOM   7799  N   ALA C 146     -29.724  47.281  -5.235  1.00 56.38           N  
+ANISOU 7799  N   ALA C 146     7101   6655   7667    125    756    254       N  
+ATOM   7800  CA  ALA C 146     -28.983  47.806  -4.096  1.00 54.61           C  
+ANISOU 7800  CA  ALA C 146     6841   6464   7443    170    908    206       C  
+ATOM   7801  C   ALA C 146     -27.650  47.090  -3.902  1.00 63.47           C  
+ANISOU 7801  C   ALA C 146     8084   7577   8455    139    984    181       C  
+ATOM   7802  O   ALA C 146     -27.518  45.904  -4.206  1.00 69.57           O  
+ANISOU 7802  O   ALA C 146     8926   8337   9169     80    950    195       O  
+ATOM   7803  CB  ALA C 146     -29.823  47.702  -2.833  1.00 52.76           C  
+ANISOU 7803  CB  ALA C 146     6431   6322   7295    175    977    198       C  
+ATOM   7804  N   VAL C 147     -26.666  47.823  -3.392  1.00 51.10           N  
+ANISOU 7804  N   VAL C 147     6539   6007   6871    182   1077    142       N  
+ATOM   7805  CA  VAL C 147     -25.396  47.234  -2.990  1.00 54.79           C  
+ANISOU 7805  CA  VAL C 147     7076   6483   7260    164   1154    121       C  
+ATOM   7806  C   VAL C 147     -25.347  47.088  -1.474  1.00 58.06           C  
+ANISOU 7806  C   VAL C 147     7401   6972   7687    168   1236     82       C  
+ATOM   7807  O   VAL C 147     -25.698  48.014  -0.745  1.00 48.40           O  
+ANISOU 7807  O   VAL C 147     6100   5775   6516    214   1269     43       O  
+ATOM   7808  CB  VAL C 147     -24.200  48.086  -3.460  1.00 57.94           C  
+ANISOU 7808  CB  VAL C 147     7550   6830   7634    194   1192    117       C  
+ATOM   7809  CG1 VAL C 147     -22.883  47.436  -3.052  1.00 50.38           C  
+ANISOU 7809  CG1 VAL C 147     6634   5891   6615    182   1265    104       C  
+ATOM   7810  CG2 VAL C 147     -24.258  48.294  -4.963  1.00 51.76           C  
+ANISOU 7810  CG2 VAL C 147     6869   5984   6812    201   1127    170       C  
+ATOM   7811  N   VAL C 148     -24.919  45.922  -1.001  1.00 59.12           N  
+ANISOU 7811  N   VAL C 148     7562   7136   7763    130   1265     93       N  
+ATOM   7812  CA  VAL C 148     -24.779  45.702   0.433  1.00 53.86           C  
+ANISOU 7812  CA  VAL C 148     6836   6548   7079    135   1339     70       C  
+ATOM   7813  C   VAL C 148     -23.335  45.354   0.784  1.00 57.56           C  
+ANISOU 7813  C   VAL C 148     7374   7016   7482    141   1377     54       C  
+ATOM   7814  O   VAL C 148     -22.889  44.224   0.592  1.00 54.65           O  
+ANISOU 7814  O   VAL C 148     7066   6631   7069    114   1371     88       O  
+ATOM   7815  CB  VAL C 148     -25.713  44.580   0.933  1.00 53.88           C  
+ANISOU 7815  CB  VAL C 148     6783   6601   7089     82   1341    123       C  
+ATOM   7816  CG1 VAL C 148     -25.572  44.401   2.440  1.00 49.60           C  
+ANISOU 7816  CG1 VAL C 148     6193   6153   6501     97   1431    115       C  
+ATOM   7817  CG2 VAL C 148     -27.156  44.881   0.559  1.00 43.09           C  
+ANISOU 7817  CG2 VAL C 148     5314   5245   5812     71   1296    153       C  
+ATOM   7818  N   TYR C 149     -22.616  46.342   1.307  1.00 41.10           N  
+ANISOU 7818  N   TYR C 149     5274   4939   5402    178   1405      0       N  
+ATOM   7819  CA  TYR C 149     -21.255  46.163   1.790  1.00 51.63           C  
+ANISOU 7819  CA  TYR C 149     6637   6284   6695    182   1427    -16       C  
+ATOM   7820  C   TYR C 149     -21.254  45.575   3.195  1.00 51.60           C  
+ANISOU 7820  C   TYR C 149     6607   6367   6630    186   1456    -26       C  
+ATOM   7821  O   TYR C 149     -21.683  46.229   4.149  1.00 56.64           O  
+ANISOU 7821  O   TYR C 149     7204   7059   7258    214   1477    -78       O  
+ATOM   7822  CB  TYR C 149     -20.495  47.492   1.799  1.00 50.02           C  
+ANISOU 7822  CB  TYR C 149     6422   6044   6539    201   1420    -66       C  
+ATOM   7823  CG  TYR C 149     -20.386  48.198   0.466  1.00 55.15           C  
+ANISOU 7823  CG  TYR C 149     7103   6608   7243    197   1402    -36       C  
+ATOM   7824  CD1 TYR C 149     -19.358  47.897  -0.416  1.00 51.26           C  
+ANISOU 7824  CD1 TYR C 149     6656   6084   6738    186   1420     14       C  
+ATOM   7825  CD2 TYR C 149     -21.288  49.192   0.106  1.00 63.89           C  
+ANISOU 7825  CD2 TYR C 149     8195   7671   8411    216   1375    -50       C  
+ATOM   7826  CE1 TYR C 149     -19.243  48.548  -1.630  1.00 53.44           C  
+ANISOU 7826  CE1 TYR C 149     6971   6293   7041    185   1418     58       C  
+ATOM   7827  CE2 TYR C 149     -21.179  49.851  -1.105  1.00 48.50           C  
+ANISOU 7827  CE2 TYR C 149     6286   5642   6499    215   1353     -4       C  
+ATOM   7828  CZ  TYR C 149     -20.155  49.524  -1.969  1.00 56.00           C  
+ANISOU 7828  CZ  TYR C 149     7292   6569   7418    195   1378     53       C  
+ATOM   7829  OH  TYR C 149     -20.043  50.175  -3.176  1.00 61.06           O  
+ANISOU 7829  OH  TYR C 149     7984   7142   8074    196   1371    115       O  
+ATOM   7830  N   LYS C 150     -20.780  44.343   3.328  1.00 47.01           N  
+ANISOU 7830  N   LYS C 150     6064   5797   6001    169   1459     25       N  
+ATOM   7831  CA  LYS C 150     -20.647  43.743   4.648  1.00 37.67           C  
+ANISOU 7831  CA  LYS C 150     4873   4694   4747    175   1482     37       C  
+ATOM   7832  C   LYS C 150     -19.178  43.741   5.039  1.00 42.11           C  
+ANISOU 7832  C   LYS C 150     5453   5263   5282    199   1461     19       C  
+ATOM   7833  O   LYS C 150     -18.462  42.758   4.851  1.00 57.20           O  
+ANISOU 7833  O   LYS C 150     7400   7154   7179    202   1452     71       O  
+ATOM   7834  CB  LYS C 150     -21.237  42.332   4.670  1.00 43.05           C  
+ANISOU 7834  CB  LYS C 150     5578   5372   5406    136   1488    123       C  
+ATOM   7835  CG  LYS C 150     -22.661  42.287   4.131  1.00 43.28           C  
+ANISOU 7835  CG  LYS C 150     5568   5386   5492     94   1486    151       C  
+ATOM   7836  CD  LYS C 150     -23.240  40.883   4.093  1.00 38.20           C  
+ANISOU 7836  CD  LYS C 150     4945   4716   4853     31   1472    243       C  
+ATOM   7837  CE  LYS C 150     -23.508  40.352   5.492  1.00 38.36           C  
+ANISOU 7837  CE  LYS C 150     4933   4828   4815     20   1532    301       C  
+ATOM   7838  NZ  LYS C 150     -24.321  39.101   5.480  1.00 47.24           N  
+ANISOU 7838  NZ  LYS C 150     6055   5919   5974    -64   1522    410       N  
+HETATM 7839  N   MSE C 151     -18.749  44.871   5.586  1.00 52.10           N  
+ANISOU 7839  N   MSE C 151     6691   6551   6554    218   1443    -56       N  
+HETATM 7840  CA  MSE C 151     -17.344  45.147   5.851  1.00 53.43           C  
+ANISOU 7840  CA  MSE C 151     6848   6718   6734    227   1399    -79       C  
+HETATM 7841  C   MSE C 151     -16.648  44.102   6.714  1.00 53.76           C  
+ANISOU 7841  C   MSE C 151     6905   6820   6702    244   1378    -35       C  
+HETATM 7842  O   MSE C 151     -15.457  43.859   6.552  1.00 57.35           O  
+ANISOU 7842  O   MSE C 151     7339   7264   7189    254   1346    -12       O  
+HETATM 7843  CB  MSE C 151     -17.220  46.515   6.512  1.00 73.54           C  
+ANISOU 7843  CB  MSE C 151     9375   9272   9296    233   1361   -181       C  
+HETATM 7844  CG  MSE C 151     -17.303  47.684   5.551  1.00112.01           C  
+ANISOU 7844  CG  MSE C 151    14229  14052  14277    216   1355   -212       C  
+HETATM 7845 SE   MSE C 151     -17.486  49.336   6.547  1.00146.12          SE  
+ANISOU 7845 SE   MSE C 151    18556  18352  18613    237   1300   -359      SE  
+HETATM 7846  CE  MSE C 151     -16.798  48.690   8.246  1.00 48.53           C  
+ANISOU 7846  CE  MSE C 151     6220   6112   6106    258   1248   -399       C  
+ATOM   7847  N   HIS C 152     -17.389  43.486   7.625  1.00 44.46           N  
+ANISOU 7847  N   HIS C 152     5755   5708   5429    251   1400    -10       N  
+ATOM   7848  CA  HIS C 152     -16.795  42.563   8.591  1.00 47.11           C  
+ANISOU 7848  CA  HIS C 152     6118   6104   5678    272   1372     42       C  
+ATOM   7849  C   HIS C 152     -17.018  41.098   8.217  1.00 47.30           C  
+ANISOU 7849  C   HIS C 152     6183   6090   5700    264   1399    153       C  
+ATOM   7850  O   HIS C 152     -16.790  40.201   9.028  1.00 54.05           O  
+ANISOU 7850  O   HIS C 152     7072   6983   6481    280   1384    222       O  
+ATOM   7851  CB  HIS C 152     -17.331  42.856   9.993  1.00 41.58           C  
+ANISOU 7851  CB  HIS C 152     5442   5509   4849    292   1379      8       C  
+ATOM   7852  CG  HIS C 152     -16.726  44.078  10.610  1.00 49.55           C  
+ANISOU 7852  CG  HIS C 152     6444   6546   5838    313   1312   -111       C  
+ATOM   7853  ND1 HIS C 152     -17.047  44.519  11.876  1.00 59.44           N  
+ANISOU 7853  ND1 HIS C 152     7742   7890   6953    350   1305   -177       N  
+ATOM   7854  CD2 HIS C 152     -15.810  44.951  10.130  1.00 46.41           C  
+ANISOU 7854  CD2 HIS C 152     6006   6087   5542    298   1242   -176       C  
+ATOM   7855  CE1 HIS C 152     -16.359  45.614  12.146  1.00 61.69           C  
+ANISOU 7855  CE1 HIS C 152     8027   8156   7257    356   1215   -294       C  
+ATOM   7856  NE2 HIS C 152     -15.599  45.897  11.102  1.00 57.96           N  
+ANISOU 7856  NE2 HIS C 152     7493   7588   6942    315   1174   -287       N  
+ATOM   7857  N   GLY C 153     -17.468  40.863   6.988  1.00 44.81           N  
+ANISOU 7857  N   GLY C 153     5875   5689   5461    239   1426    171       N  
+ATOM   7858  CA  GLY C 153     -17.619  39.510   6.482  1.00 51.09           C  
+ANISOU 7858  CA  GLY C 153     6729   6415   6270    229   1431    255       C  
+ATOM   7859  C   GLY C 153     -19.041  38.986   6.461  1.00 55.68           C  
+ANISOU 7859  C   GLY C 153     7324   6983   6850    169   1459    305       C  
+ATOM   7860  O   GLY C 153     -19.995  39.732   6.681  1.00 59.07           O  
+ANISOU 7860  O   GLY C 153     7701   7464   7279    143   1491    276       O  
+ATOM   7861  N   ASP C 154     -19.177  37.691   6.192  1.00 58.26           N  
+ANISOU 7861  N   ASP C 154     7714   7231   7190    147   1444    384       N  
+ATOM   7862  CA  ASP C 154     -20.484  37.063   6.055  1.00 42.39           C  
+ANISOU 7862  CA  ASP C 154     5710   5186   5212     67   1452    448       C  
+ATOM   7863  C   ASP C 154     -20.585  35.823   6.939  1.00 42.37           C  
+ANISOU 7863  C   ASP C 154     5751   5173   5172     40   1453    566       C  
+ATOM   7864  O   ASP C 154     -19.594  35.131   7.178  1.00 46.01           O  
+ANISOU 7864  O   ASP C 154     6277   5597   5608     92   1424    599       O  
+ATOM   7865  CB  ASP C 154     -20.740  36.701   4.589  1.00 44.89           C  
+ANISOU 7865  CB  ASP C 154     6081   5372   5602     41   1406    425       C  
+ATOM   7866  CG  ASP C 154     -22.095  36.057   4.368  1.00 61.58           C  
+ANISOU 7866  CG  ASP C 154     8188   7436   7772    -61   1381    488       C  
+ATOM   7867  OD1 ASP C 154     -23.111  36.783   4.379  1.00 71.55           O  
+ANISOU 7867  OD1 ASP C 154     9357   8761   9067   -103   1400    479       O  
+ATOM   7868  OD2 ASP C 154     -22.141  34.825   4.169  1.00 58.77           O  
+ANISOU 7868  OD2 ASP C 154     7917   6971   7444    -98   1335    548       O  
+ATOM   7869  N   VAL C 155     -21.793  35.563   7.428  1.00 45.49           N  
+ANISOU 7869  N   VAL C 155     6103   5606   5576    -39   1490    643       N  
+ATOM   7870  CA  VAL C 155     -22.061  34.475   8.366  1.00 47.39           C  
+ANISOU 7870  CA  VAL C 155     6374   5849   5781    -82   1509    784       C  
+ATOM   7871  C   VAL C 155     -21.738  33.087   7.795  1.00 58.05           C  
+ANISOU 7871  C   VAL C 155     7836   7023   7197   -108   1434    851       C  
+ATOM   7872  O   VAL C 155     -21.345  32.182   8.535  1.00 46.20           O  
+ANISOU 7872  O   VAL C 155     6399   5497   5658    -99   1426    955       O  
+ATOM   7873  CB  VAL C 155     -23.537  34.516   8.843  1.00 53.51           C  
+ANISOU 7873  CB  VAL C 155     7052   6700   6579   -175   1581    868       C  
+ATOM   7874  CG1 VAL C 155     -24.495  34.394   7.666  1.00 52.51           C  
+ANISOU 7874  CG1 VAL C 155     6884   6473   6593   -264   1532    857       C  
+ATOM   7875  CG2 VAL C 155     -23.806  33.433   9.883  1.00 44.05           C  
+ANISOU 7875  CG2 VAL C 155     5882   5516   5337   -227   1619   1040       C  
+ATOM   7876  N   GLU C 156     -21.868  32.923   6.481  1.00 61.68           N  
+ANISOU 7876  N   GLU C 156     8338   7354   7745   -129   1373    787       N  
+ATOM   7877  CA  GLU C 156     -21.541  31.645   5.849  1.00 53.90           C  
+ANISOU 7877  CA  GLU C 156     7484   6180   6815   -136   1295    819       C  
+ATOM   7878  C   GLU C 156     -20.046  31.491   5.582  1.00 50.89           C  
+ANISOU 7878  C   GLU C 156     7183   5755   6396      1   1278    759       C  
+ATOM   7879  O   GLU C 156     -19.605  30.480   5.036  1.00 57.02           O  
+ANISOU 7879  O   GLU C 156     8082   6375   7210     36   1224    765       O  
+ATOM   7880  CB  GLU C 156     -22.318  31.484   4.543  1.00 51.43           C  
+ANISOU 7880  CB  GLU C 156     7205   5744   6592   -209   1224    765       C  
+ATOM   7881  CG  GLU C 156     -23.815  31.685   4.686  1.00 53.14           C  
+ANISOU 7881  CG  GLU C 156     7307   6008   6878   -346   1228    825       C  
+ATOM   7882  CD  GLU C 156     -24.501  30.542   5.392  1.00 69.13           C  
+ANISOU 7882  CD  GLU C 156     9335   7969   8961   -462   1216    985       C  
+ATOM   7883  OE1 GLU C 156     -24.206  29.372   5.067  1.00 71.40           O  
+ANISOU 7883  OE1 GLU C 156     9760   8074   9295   -482   1135   1019       O  
+ATOM   7884  OE2 GLU C 156     -25.342  30.818   6.270  1.00 70.40           O  
+ANISOU 7884  OE2 GLU C 156     9364   8258   9126   -530   1296   1081       O  
+ATOM   7885  N   HIS C 157     -19.276  32.500   5.974  1.00 50.50           N  
+ANISOU 7885  N   HIS C 157     7063   5843   6284     82   1322    701       N  
+ATOM   7886  CA  HIS C 157     -17.823  32.474   5.839  1.00 47.98           C  
+ANISOU 7886  CA  HIS C 157     6772   5514   5945    210   1313    659       C  
+ATOM   7887  C   HIS C 157     -17.188  32.885   7.167  1.00 48.73           C  
+ANISOU 7887  C   HIS C 157     6801   5751   5962    254   1327    697       C  
+ATOM   7888  O   HIS C 157     -16.520  33.916   7.243  1.00 48.86           O  
+ANISOU 7888  O   HIS C 157     6743   5866   5957    303   1338    621       O  
+ATOM   7889  CB  HIS C 157     -17.349  33.399   4.714  1.00 47.26           C  
+ANISOU 7889  CB  HIS C 157     6653   5430   5873    260   1331    538       C  
+ATOM   7890  CG  HIS C 157     -17.817  32.991   3.352  1.00 48.17           C  
+ANISOU 7890  CG  HIS C 157     6861   5411   6032    239   1305    491       C  
+ATOM   7891  ND1 HIS C 157     -17.154  32.055   2.586  1.00 50.29           N  
+ANISOU 7891  ND1 HIS C 157     7251   5543   6315    320   1283    473       N  
+ATOM   7892  CD2 HIS C 157     -18.877  33.396   2.612  1.00 50.52           C  
+ANISOU 7892  CD2 HIS C 157     7155   5687   6352    157   1287    452       C  
+ATOM   7893  CE1 HIS C 157     -17.786  31.900   1.437  1.00 58.17           C  
+ANISOU 7893  CE1 HIS C 157     8335   6442   7326    285   1249    416       C  
+ATOM   7894  NE2 HIS C 157     -18.836  32.703   1.428  1.00 60.27           N  
+ANISOU 7894  NE2 HIS C 157     8521   6777   7601    181   1242    408       N  
+ATOM   7895  N   PRO C 158     -17.402  32.077   8.222  1.00 48.90           N  
+ANISOU 7895  N   PRO C 158     6859   5780   5939    232   1316    819       N  
+ATOM   7896  CA  PRO C 158     -17.045  32.464   9.594  1.00 49.25           C  
+ANISOU 7896  CA  PRO C 158     6862   5975   5874    262   1322    862       C  
+ATOM   7897  C   PRO C 158     -15.556  32.730   9.805  1.00 50.89           C  
+ANISOU 7897  C   PRO C 158     7046   6226   6065    379   1270    821       C  
+ATOM   7898  O   PRO C 158     -15.210  33.620  10.579  1.00 58.02           O  
+ANISOU 7898  O   PRO C 158     7888   7267   6890    398   1259    780       O  
+ATOM   7899  CB  PRO C 158     -17.494  31.256  10.426  1.00 61.25           C  
+ANISOU 7899  CB  PRO C 158     8459   7452   7360    221   1315   1028       C  
+ATOM   7900  CG  PRO C 158     -17.508  30.121   9.474  1.00 51.05           C  
+ANISOU 7900  CG  PRO C 158     7260   5953   6183    212   1274   1058       C  
+ATOM   7901  CD  PRO C 158     -17.938  30.706   8.167  1.00 49.86           C  
+ANISOU 7901  CD  PRO C 158     7081   5754   6109    178   1288    930       C  
+ATOM   7902  N   SER C 159     -14.692  31.968   9.142  1.00 52.79           N  
+ANISOU 7902  N   SER C 159     7330   6349   6380    458   1234    829       N  
+ATOM   7903  CA  SER C 159     -13.254  32.089   9.363  1.00 55.43           C  
+ANISOU 7903  CA  SER C 159     7613   6726   6723    575   1184    815       C  
+ATOM   7904  C   SER C 159     -12.687  33.394   8.805  1.00 54.10           C  
+ANISOU 7904  C   SER C 159     7330   6635   6590    590   1203    690       C  
+ATOM   7905  O   SER C 159     -11.650  33.873   9.262  1.00 56.09           O  
+ANISOU 7905  O   SER C 159     7498   6970   6842    647   1153    674       O  
+ATOM   7906  CB  SER C 159     -12.522  30.896   8.745  1.00 57.72           C  
+ANISOU 7906  CB  SER C 159     7972   6864   7094    676   1161    859       C  
+ATOM   7907  OG  SER C 159     -12.696  30.866   7.339  1.00 60.14           O  
+ANISOU 7907  OG  SER C 159     8313   7063   7476    681   1210    775       O  
+ATOM   7908  N   GLU C 160     -13.376  33.970   7.824  1.00 51.29           N  
+ANISOU 7908  N   GLU C 160     6969   6246   6272    531   1262    612       N  
+ATOM   7909  CA  GLU C 160     -12.931  35.216   7.208  1.00 49.46           C  
+ANISOU 7909  CA  GLU C 160     6641   6068   6082    534   1286    512       C  
+ATOM   7910  C   GLU C 160     -13.515  36.429   7.923  1.00 48.93           C  
+ANISOU 7910  C   GLU C 160     6519   6114   5959    461   1283    458       C  
+ATOM   7911  O   GLU C 160     -13.188  37.570   7.596  1.00 60.15           O  
+ANISOU 7911  O   GLU C 160     7863   7573   7417    450   1288    379       O  
+ATOM   7912  CB  GLU C 160     -13.320  35.255   5.727  1.00 48.33           C  
+ANISOU 7912  CB  GLU C 160     6538   5828   5997    523   1345    460       C  
+ATOM   7913  CG  GLU C 160     -12.731  34.136   4.875  1.00 58.85           C  
+ANISOU 7913  CG  GLU C 160     7948   7039   7373    615   1358    482       C  
+ATOM   7914  CD  GLU C 160     -11.232  34.267   4.683  1.00 72.04           C  
+ANISOU 7914  CD  GLU C 160     9530   8744   9096    730   1372    479       C  
+ATOM   7915  OE1 GLU C 160     -10.700  35.382   4.867  1.00 74.81           O  
+ANISOU 7915  OE1 GLU C 160     9756   9197   9471    713   1374    448       O  
+ATOM   7916  OE2 GLU C 160     -10.586  33.256   4.337  1.00 81.51           O  
+ANISOU 7916  OE2 GLU C 160    10781   9862  10328    839   1380    511       O  
+ATOM   7917  N   ALA C 161     -14.386  36.173   8.895  1.00 48.73           N  
+ANISOU 7917  N   ALA C 161     6536   6136   5843    415   1282    505       N  
+ATOM   7918  CA  ALA C 161     -15.095  37.235   9.601  1.00 46.45           C  
+ANISOU 7918  CA  ALA C 161     6214   5952   5484    366   1299    448       C  
+ATOM   7919  C   ALA C 161     -14.149  38.118  10.407  1.00 46.92           C  
+ANISOU 7919  C   ALA C 161     6218   6108   5500    402   1229    386       C  
+ATOM   7920  O   ALA C 161     -13.167  37.641  10.977  1.00 51.54           O  
+ANISOU 7920  O   ALA C 161     6801   6718   6063    456   1155    433       O  
+ATOM   7921  CB  ALA C 161     -16.163  36.644  10.508  1.00 49.97           C  
+ANISOU 7921  CB  ALA C 161     6714   6441   5832    325   1335    532       C  
+ATOM   7922  N   VAL C 162     -14.461  39.408  10.450  1.00 45.47           N  
+ANISOU 7922  N   VAL C 162     5994   5969   5314    373   1237    281       N  
+ATOM   7923  CA  VAL C 162     -13.696  40.367  11.236  1.00 49.94           C  
+ANISOU 7923  CA  VAL C 162     6522   6609   5843    389   1152    201       C  
+ATOM   7924  C   VAL C 162     -14.384  40.608  12.574  1.00 57.74           C  
+ANISOU 7924  C   VAL C 162     7573   7704   6660    393   1151    180       C  
+ATOM   7925  O   VAL C 162     -15.488  41.148  12.624  1.00 71.48           O  
+ANISOU 7925  O   VAL C 162     9329   9466   8366    371   1229    133       O  
+ATOM   7926  CB  VAL C 162     -13.532  41.705  10.494  1.00 57.71           C  
+ANISOU 7926  CB  VAL C 162     7438   7554   6933    357   1150     92       C  
+ATOM   7927  CG1 VAL C 162     -12.760  42.698  11.350  1.00 50.72           C  
+ANISOU 7927  CG1 VAL C 162     6523   6725   6023    357   1038      2       C  
+ATOM   7928  CG2 VAL C 162     -12.839  41.487   9.157  1.00 55.92           C  
+ANISOU 7928  CG2 VAL C 162     7155   7241   6851    360   1175    125       C  
+ATOM   7929  N   LEU C 163     -13.728  40.202  13.656  1.00 55.29           N  
+ANISOU 7929  N   LEU C 163     7301   7469   6240    433   1064    218       N  
+ATOM   7930  CA  LEU C 163     -14.315  40.323  14.984  1.00 55.47           C  
+ANISOU 7930  CA  LEU C 163     7408   7608   6061    453   1070    210       C  
+ATOM   7931  C   LEU C 163     -13.764  41.528  15.739  1.00 57.86           C  
+ANISOU 7931  C   LEU C 163     7720   7974   6292    471    959     66       C  
+ATOM   7932  O   LEU C 163     -14.508  42.258  16.393  1.00 63.10           O  
+ANISOU 7932  O   LEU C 163     8442   8703   6832    485    999    -23       O  
+ATOM   7933  CB  LEU C 163     -14.051  39.053  15.794  1.00 65.76           C  
+ANISOU 7933  CB  LEU C 163     8780   8956   7249    488   1038    359       C  
+ATOM   7934  CG  LEU C 163     -14.837  37.783  15.460  1.00 69.42           C  
+ANISOU 7934  CG  LEU C 163     9278   9365   7734    464   1143    514       C  
+ATOM   7935  CD1 LEU C 163     -14.924  36.888  16.682  1.00 57.14           C  
+ANISOU 7935  CD1 LEU C 163     7820   7890   5999    494   1131    651       C  
+ATOM   7936  CD2 LEU C 163     -16.219  38.089  14.920  1.00 64.76           C  
+ANISOU 7936  CD2 LEU C 163     8667   8756   7183    406   1284    492       C  
+ATOM   7937  N   ILE C 164     -12.455  41.730  15.639  1.00 72.03           N  
+ANISOU 7937  N   ILE C 164     9452   9743   8172    473    816     40       N  
+ATOM   7938  CA  ILE C 164     -11.784  42.805  16.362  1.00 73.46           C  
+ANISOU 7938  CA  ILE C 164     9639   9965   8307    474    668    -94       C  
+ATOM   7939  C   ILE C 164     -11.085  43.786  15.425  1.00 84.43           C  
+ANISOU 7939  C   ILE C 164    10910  11258   9913    419    613   -180       C  
+ATOM   7940  O   ILE C 164     -10.776  43.455  14.280  1.00 84.46           O  
+ANISOU 7940  O   ILE C 164    10818  11183  10088    398    670   -112       O  
+ATOM   7941  CB  ILE C 164     -10.760  42.242  17.364  1.00 62.51           C  
+ANISOU 7941  CB  ILE C 164     8279   8657   6817    515    501    -40       C  
+ATOM   7942  CG1 ILE C 164      -9.784  41.303  16.654  1.00 63.48           C  
+ANISOU 7942  CG1 ILE C 164     8290   8723   7105    527    467     90       C  
+ATOM   7943  CG2 ILE C 164     -11.469  41.496  18.481  1.00 62.81           C  
+ANISOU 7943  CG2 ILE C 164     8460   8803   6601    569    547     38       C  
+ATOM   7944  CD1 ILE C 164      -8.832  40.587  17.588  1.00 67.26           C  
+ANISOU 7944  CD1 ILE C 164     8784   9275   7498    584    304    174       C  
+ATOM   7945  N   LYS C 165     -10.850  44.997  15.924  1.00 82.37           N  
+ANISOU 7945  N   LYS C 165    10666  10996   9633    396    503   -329       N  
+ATOM   7946  CA  LYS C 165     -10.167  46.047  15.171  1.00 74.52           C  
+ANISOU 7946  CA  LYS C 165     9566   9902   8848    327    434   -405       C  
+ATOM   7947  C   LYS C 165      -8.773  45.622  14.711  1.00 69.79           C  
+ANISOU 7947  C   LYS C 165     8816   9285   8416    303    340   -312       C  
+ATOM   7948  O   LYS C 165      -8.249  46.152  13.729  1.00 64.45           O  
+ANISOU 7948  O   LYS C 165     8018   8526   7944    246    352   -307       O  
+ATOM   7949  CB  LYS C 165     -10.069  47.322  16.012  1.00 64.98           C  
+ANISOU 7949  CB  LYS C 165     8426   8686   7578    307    293   -583       C  
+ATOM   7950  N   ASP C 166      -8.181  44.673  15.432  1.00 66.57           N  
+ANISOU 7950  N   ASP C 166     8414   8960   7919    354    253   -229       N  
+ATOM   7951  CA  ASP C 166      -6.841  44.167  15.140  1.00 69.16           C  
+ANISOU 7951  CA  ASP C 166     8588   9290   8399    358    158   -132       C  
+ATOM   7952  C   ASP C 166      -6.632  43.800  13.672  1.00 67.08           C  
+ANISOU 7952  C   ASP C 166     8203   8949   8335    355    308    -40       C  
+ATOM   7953  O   ASP C 166      -5.543  43.989  13.135  1.00 72.86           O  
+ANISOU 7953  O   ASP C 166     8769   9659   9254    331    259     -2       O  
+ATOM   7954  CB  ASP C 166      -6.537  42.948  16.013  1.00 72.66           C  
+ANISOU 7954  CB  ASP C 166     9083   9823   8702    443     88    -26       C  
+ATOM   7955  CG  ASP C 166      -6.437  43.295  17.485  1.00 86.52           C  
+ANISOU 7955  CG  ASP C 166    10950  11672  10252    454    -96   -105       C  
+ATOM   7956  OD1 ASP C 166      -5.332  43.167  18.053  1.00102.45           O  
+ANISOU 7956  OD1 ASP C 166    12897  13736  12293    466   -297    -80       O  
+ATOM   7957  OD2 ASP C 166      -7.461  43.707  18.071  1.00 91.66           O  
+ANISOU 7957  OD2 ASP C 166    11759  12354  10716    459    -43   -195       O  
+ATOM   7958  N   ASP C 167      -7.675  43.285  13.027  1.00 63.22           N  
+ANISOU 7958  N   ASP C 167     7795   8424   7803    378    490     -2       N  
+ATOM   7959  CA  ASP C 167      -7.589  42.896  11.622  1.00 60.51           C  
+ANISOU 7959  CA  ASP C 167     7378   8007   7608    386    632     72       C  
+ATOM   7960  C   ASP C 167      -7.216  44.078  10.739  1.00 67.55           C  
+ANISOU 7960  C   ASP C 167     8161   8834   8671    311    649     20       C  
+ATOM   7961  O   ASP C 167      -6.372  43.954   9.849  1.00 80.04           O  
+ANISOU 7961  O   ASP C 167     9614  10390  10409    316    692     90       O  
+ATOM   7962  CB  ASP C 167      -8.912  42.298  11.148  1.00 55.96           C  
+ANISOU 7962  CB  ASP C 167     6923   7394   6946    404    790     97       C  
+ATOM   7963  CG  ASP C 167      -9.165  40.927  11.722  1.00 67.61           C  
+ANISOU 7963  CG  ASP C 167     8484   8902   8302    471    799    193       C  
+ATOM   7964  OD1 ASP C 167      -8.219  40.333  12.281  1.00 75.80           O  
+ANISOU 7964  OD1 ASP C 167     9481   9980   9339    523    698    255       O  
+ATOM   7965  OD2 ASP C 167     -10.307  40.434  11.612  1.00 83.07           O  
+ANISOU 7965  OD2 ASP C 167    10544  10840  10180    468    900    217       O  
+ATOM   7966  N   TYR C 168      -7.843  45.222  11.002  1.00 58.55           N  
+ANISOU 7966  N   TYR C 168     7078   7666   7502    248    622    -95       N  
+ATOM   7967  CA  TYR C 168      -7.521  46.464  10.307  1.00 58.87           C  
+ANISOU 7967  CA  TYR C 168     7034   7628   7706    164    614   -143       C  
+ATOM   7968  C   TYR C 168      -6.027  46.759  10.385  1.00 63.18           C  
+ANISOU 7968  C   TYR C 168     7406   8186   8414    120    485   -108       C  
+ATOM   7969  O   TYR C 168      -5.437  47.300   9.450  1.00 63.71           O  
+ANISOU 7969  O   TYR C 168     7346   8198   8663     65    529    -64       O  
+ATOM   7970  CB  TYR C 168      -8.312  47.632  10.896  1.00 60.00           C  
+ANISOU 7970  CB  TYR C 168     7280   7735   7784    120    559   -288       C  
+ATOM   7971  CG  TYR C 168      -9.799  47.590  10.625  1.00 57.99           C  
+ANISOU 7971  CG  TYR C 168     7150   7461   7424    155    699   -316       C  
+ATOM   7972  CD1 TYR C 168     -10.662  46.919  11.482  1.00 67.13           C  
+ANISOU 7972  CD1 TYR C 168     8424   8697   8387    217    728   -329       C  
+ATOM   7973  CD2 TYR C 168     -10.342  48.231   9.519  1.00 57.69           C  
+ANISOU 7973  CD2 TYR C 168     7104   7331   7485    123    800   -317       C  
+ATOM   7974  CE1 TYR C 168     -12.024  46.882  11.242  1.00 65.22           C  
+ANISOU 7974  CE1 TYR C 168     8263   8446   8073    242    856   -342       C  
+ATOM   7975  CE2 TYR C 168     -11.703  48.199   9.270  1.00 57.48           C  
+ANISOU 7975  CE2 TYR C 168     7170   7292   7379    155    909   -338       C  
+ATOM   7976  CZ  TYR C 168     -12.538  47.524  10.134  1.00 58.54           C  
+ANISOU 7976  CZ  TYR C 168     7394   7508   7340    212    937   -351       C  
+ATOM   7977  OH  TYR C 168     -13.892  47.490   9.889  1.00 58.17           O  
+ANISOU 7977  OH  TYR C 168     7407   7457   7239    237   1046   -358       O  
+ATOM   7978  N   GLU C 169      -5.425  46.391  11.511  1.00 67.82           N  
+ANISOU 7978  N   GLU C 169     7982   8852   8935    145    325   -117       N  
+ATOM   7979  CA  GLU C 169      -4.006  46.616  11.740  1.00 70.53           C  
+ANISOU 7979  CA  GLU C 169     8143   9219   9435    103    167    -82       C  
+ATOM   7980  C   GLU C 169      -3.167  45.558  11.026  1.00 70.13           C  
+ANISOU 7980  C   GLU C 169     7943   9206   9495    177    255     73       C  
+ATOM   7981  O   GLU C 169      -2.065  45.843  10.559  1.00 71.61           O  
+ANISOU 7981  O   GLU C 169     7927   9395   9889    138    227    138       O  
+ATOM   7982  CB  GLU C 169      -3.702  46.613  13.239  1.00 75.00           C  
+ANISOU 7982  CB  GLU C 169     8766   9858   9871    110    -62   -153       C  
+ATOM   7983  CG  GLU C 169      -4.658  47.463  14.062  1.00 79.88           C  
+ANISOU 7983  CG  GLU C 169     9578  10455  10319     81   -125   -319       C  
+ATOM   7984  CD  GLU C 169      -4.528  47.211  15.551  1.00 81.46           C  
+ANISOU 7984  CD  GLU C 169     9887  10750  10315    124   -317   -379       C  
+ATOM   7985  OE1 GLU C 169      -3.580  46.507  15.956  1.00 87.51           O  
+ANISOU 7985  OE1 GLU C 169    10559  11590  11102    157   -440   -292       O  
+ATOM   7986  OE2 GLU C 169      -5.380  47.708  16.316  1.00 78.62           O  
+ANISOU 7986  OE2 GLU C 169     9710  10397   9764    136   -341   -511       O  
+ATOM   7987  N   LYS C 170      -3.690  44.336  10.949  1.00 72.95           N  
+ANISOU 7987  N   LYS C 170     8401   9591   9726    287    364    134       N  
+ATOM   7988  CA  LYS C 170      -2.943  43.228  10.361  1.00 80.49           C  
+ANISOU 7988  CA  LYS C 170     9248  10570  10765    387    443    266       C  
+ATOM   7989  C   LYS C 170      -3.154  43.126   8.854  1.00 84.65           C  
+ANISOU 7989  C   LYS C 170     9753  11033  11377    406    665    314       C  
+ATOM   7990  O   LYS C 170      -2.202  42.925   8.099  1.00 86.41           O  
+ANISOU 7990  O   LYS C 170     9811  11265  11754    445    733    401       O  
+ATOM   7991  CB  LYS C 170      -3.333  41.900  11.015  1.00 82.87           C  
+ANISOU 7991  CB  LYS C 170     9681  10906  10898    499    435    314       C  
+ATOM   7992  CG  LYS C 170      -3.330  41.906  12.532  1.00 81.50           C  
+ANISOU 7992  CG  LYS C 170     9584  10806  10577    495    235    274       C  
+ATOM   7993  CD  LYS C 170      -4.089  40.707  13.075  1.00 82.35           C  
+ANISOU 7993  CD  LYS C 170     9868  10931  10491    583    275    329       C  
+ATOM   7994  CE  LYS C 170      -3.857  40.528  14.564  1.00 81.45           C  
+ANISOU 7994  CE  LYS C 170     9820  10907  10222    605     76    327       C  
+ATOM   7995  NZ  LYS C 170      -4.622  39.369  15.099  1.00 81.03           N  
+ANISOU 7995  NZ  LYS C 170     9940  10866   9980    680    128    407       N  
+ATOM   7996  N   TYR C 171      -4.402  43.272   8.420  1.00 78.63           N  
+ANISOU 7996  N   TYR C 171     9153  10212  10509    385    777    262       N  
+ATOM   7997  CA  TYR C 171      -4.737  43.077   7.015  1.00 73.83           C  
+ANISOU 7997  CA  TYR C 171     8569   9546   9939    413    971    302       C  
+ATOM   7998  C   TYR C 171      -5.378  44.322   6.415  1.00 64.88           C  
+ANISOU 7998  C   TYR C 171     7466   8350   8837    310   1020    240       C  
+ATOM   7999  O   TYR C 171      -6.595  44.368   6.242  1.00 59.74           O  
+ANISOU 7999  O   TYR C 171     6965   7657   8077    300   1076    190       O  
+ATOM   8000  CB  TYR C 171      -5.694  41.896   6.848  1.00 75.14           C  
+ANISOU 8000  CB  TYR C 171     8907   9683   9960    494   1059    316       C  
+ATOM   8001  CG  TYR C 171      -5.540  40.813   7.889  1.00 67.89           C  
+ANISOU 8001  CG  TYR C 171     8033   8808   8954    570    967    354       C  
+ATOM   8002  CD1 TYR C 171      -4.436  39.970   7.897  1.00 66.38           C  
+ANISOU 8002  CD1 TYR C 171     7739   8644   8840    671    947    440       C  
+ATOM   8003  CD2 TYR C 171      -6.515  40.626   8.860  1.00 75.43           C  
+ANISOU 8003  CD2 TYR C 171     9132   9778   9748    548    910    316       C  
+ATOM   8004  CE1 TYR C 171      -4.305  38.979   8.854  1.00 72.43           C  
+ANISOU 8004  CE1 TYR C 171     8557   9438   9526    746    853    489       C  
+ATOM   8005  CE2 TYR C 171      -6.394  39.642   9.814  1.00 82.23           C  
+ANISOU 8005  CE2 TYR C 171    10048  10678  10518    613    831    371       C  
+ATOM   8006  CZ  TYR C 171      -5.290  38.821   9.809  1.00 88.01           C  
+ANISOU 8006  CZ  TYR C 171    10688  11422  11329    711    793    459       C  
+ATOM   8007  OH  TYR C 171      -5.174  37.839  10.765  1.00 99.87           O  
+ANISOU 8007  OH  TYR C 171    12254  12953  12740    781    704    528       O  
+ATOM   8008  N   SER C 172      -4.574  45.330   6.098  1.00 65.32           N  
+ANISOU 8008  N   SER C 172     7371   8393   9053    231    995    255       N  
+ATOM   8009  CA  SER C 172      -5.124  46.542   5.502  1.00 68.04           C  
+ANISOU 8009  CA  SER C 172     7748   8660   9443    135   1035    213       C  
+ATOM   8010  C   SER C 172      -5.473  46.260   4.048  1.00 62.58           C  
+ANISOU 8010  C   SER C 172     7101   7932   8745    179   1231    280       C  
+ATOM   8011  O   SER C 172      -6.344  46.904   3.470  1.00 66.59           O  
+ANISOU 8011  O   SER C 172     7704   8374   9225    137   1285    249       O  
+ATOM   8012  CB  SER C 172      -4.140  47.710   5.607  1.00 76.70           C  
+ANISOU 8012  CB  SER C 172     8676   9736  10730     20    939    222       C  
+ATOM   8013  OG  SER C 172      -3.576  47.793   6.903  1.00 89.84           O  
+ANISOU 8013  OG  SER C 172    10285  11446  12405     -8    736    169       O  
+ATOM   8014  N   ILE C 173      -4.796  45.273   3.471  1.00 65.69           N  
+ANISOU 8014  N   ILE C 173     7435   8368   9158    277   1331    368       N  
+ATOM   8015  CA  ILE C 173      -5.013  44.887   2.082  1.00 67.79           C  
+ANISOU 8015  CA  ILE C 173     7759   8607   9391    340   1516    425       C  
+ATOM   8016  C   ILE C 173      -6.432  44.358   1.864  1.00 63.65           C  
+ANISOU 8016  C   ILE C 173     7453   8032   8698    373   1548    364       C  
+ATOM   8017  O   ILE C 173      -6.956  44.402   0.751  1.00 65.67           O  
+ANISOU 8017  O   ILE C 173     7798   8245   8908    388   1658    379       O  
+ATOM   8018  CB  ILE C 173      -3.982  43.822   1.635  1.00 65.82           C  
+ANISOU 8018  CB  ILE C 173     7416   8412   9181    469   1613    512       C  
+ATOM   8019  CG1 ILE C 173      -3.977  43.671   0.113  1.00 76.49           C  
+ANISOU 8019  CG1 ILE C 173     8813   9745  10507    534   1814    570       C  
+ATOM   8020  CG2 ILE C 173      -4.244  42.486   2.321  1.00 63.25           C  
+ANISOU 8020  CG2 ILE C 173     7187   8097   8748    574   1561    487       C  
+ATOM   8021  CD1 ILE C 173      -2.769  42.936  -0.418  1.00 84.68           C  
+ANISOU 8021  CD1 ILE C 173     9717  10844  11614    663   1938    662       C  
+ATOM   8022  N   LYS C 174      -7.053  43.869   2.934  1.00 54.80           N  
+ANISOU 8022  N   LYS C 174     6414   6923   7485    380   1445    304       N  
+ATOM   8023  CA  LYS C 174      -8.418  43.358   2.860  1.00 45.84           C  
+ANISOU 8023  CA  LYS C 174     5455   5747   6215    393   1464    260       C  
+ATOM   8024  C   LYS C 174      -9.462  44.357   3.363  1.00 45.45           C  
+ANISOU 8024  C   LYS C 174     5461   5676   6132    306   1401    180       C  
+ATOM   8025  O   LYS C 174     -10.646  44.231   3.053  1.00 62.97           O  
+ANISOU 8025  O   LYS C 174     7794   7859   8274    301   1432    153       O  
+ATOM   8026  CB  LYS C 174      -8.535  42.051   3.648  1.00 47.07           C  
+ANISOU 8026  CB  LYS C 174     5673   5926   6287    463   1421    270       C  
+HETATM 8027  N   MSE C 175      -9.024  45.348   4.134  1.00 44.53           N  
+ANISOU 8027  N   MSE C 175     5262   5576   6081    241   1305    138       N  
+HETATM 8028  CA  MSE C 175      -9.954  46.274   4.777  1.00 45.51           C  
+ANISOU 8028  CA  MSE C 175     5447   5677   6167    184   1239     44       C  
+HETATM 8029  C   MSE C 175      -9.967  47.663   4.139  1.00 52.76           C  
+ANISOU 8029  C   MSE C 175     6333   6520   7193    111   1246     26       C  
+HETATM 8030  O   MSE C 175     -11.023  48.287   4.028  1.00 68.47           O  
+ANISOU 8030  O   MSE C 175     8403   8462   9153     94   1252    -28       O  
+HETATM 8031  CB  MSE C 175      -9.625  46.395   6.267  1.00 50.79           C  
+ANISOU 8031  CB  MSE C 175     6097   6404   6797    173   1103    -18       C  
+HETATM 8032  CG  MSE C 175      -9.797  45.102   7.052  1.00 60.07           C  
+ANISOU 8032  CG  MSE C 175     7329   7649   7844    242   1088      8       C  
+HETATM 8033 SE   MSE C 175     -11.609  44.383   6.936  1.00100.80          SE  
+ANISOU 8033 SE   MSE C 175    12646  12796  12857    269   1185      4      SE  
+HETATM 8034  CE  MSE C 175     -11.219  42.718   5.999  1.00 80.02           C  
+ANISOU 8034  CE  MSE C 175    10033  10138  10231    342   1269    121       C  
+ATOM   8035  N   ASP C 176      -8.796  48.141   3.727  1.00 47.32           N  
+ANISOU 8035  N   ASP C 176     5519   5820   6642     70   1244     83       N  
+ATOM   8036  CA  ASP C 176      -8.664  49.483   3.154  1.00 50.51           C  
+ANISOU 8036  CA  ASP C 176     5883   6139   7171    -15   1243     90       C  
+ATOM   8037  C   ASP C 176      -9.610  49.792   1.983  1.00 55.40           C  
+ANISOU 8037  C   ASP C 176     6599   6691   7760     -6   1348    119       C  
+ATOM   8038  O   ASP C 176     -10.157  50.893   1.930  1.00 63.44           O  
+ANISOU 8038  O   ASP C 176     7655   7626   8824    -56   1310     76       O  
+ATOM   8039  CB  ASP C 176      -7.218  49.733   2.713  1.00 55.83           C  
+ANISOU 8039  CB  ASP C 176     6385   6823   8007    -61   1261    190       C  
+ATOM   8040  CG  ASP C 176      -6.296  50.021   3.880  1.00 57.46           C  
+ANISOU 8040  CG  ASP C 176     6474   7057   8300   -117   1099    149       C  
+ATOM   8041  OD1 ASP C 176      -6.740  49.886   5.040  1.00 56.96           O  
+ANISOU 8041  OD1 ASP C 176     6488   7019   8137   -100    982     41       O  
+ATOM   8042  OD2 ASP C 176      -5.127  50.386   3.639  1.00 69.39           O  
+ANISOU 8042  OD2 ASP C 176     7815   8572   9977   -178   1087    229       O  
+ATOM   8043  N   PRO C 177      -9.793  48.849   1.032  1.00 45.64           N  
+ANISOU 8043  N   PRO C 177     5411   5483   6447     64   1466    188       N  
+ATOM   8044  CA  PRO C 177     -10.743  49.169  -0.044  1.00 54.10           C  
+ANISOU 8044  CA  PRO C 177     6587   6494   7475     71   1534    209       C  
+ATOM   8045  C   PRO C 177     -12.154  49.468   0.468  1.00 50.93           C  
+ANISOU 8045  C   PRO C 177     6284   6060   7009     72   1469    115       C  
+ATOM   8046  O   PRO C 177     -12.816  50.374  -0.045  1.00 51.40           O  
+ANISOU 8046  O   PRO C 177     6387   6045   7098     48   1466    112       O  
+ATOM   8047  CB  PRO C 177     -10.734  47.901  -0.902  1.00 44.34           C  
+ANISOU 8047  CB  PRO C 177     5411   5298   6137    156   1637    266       C  
+ATOM   8048  CG  PRO C 177      -9.389  47.318  -0.679  1.00 41.68           C  
+ANISOU 8048  CG  PRO C 177     4958   5026   5855    186   1668    316       C  
+ATOM   8049  CD  PRO C 177      -9.087  47.580   0.766  1.00 41.74           C  
+ANISOU 8049  CD  PRO C 177     4886   5059   5915    142   1537    250       C  
+ATOM   8050  N   TYR C 178     -12.596  48.726   1.478  1.00 46.46           N  
+ANISOU 8050  N   TYR C 178     5744   5550   6358    105   1424     51       N  
+ATOM   8051  CA  TYR C 178     -13.893  48.979   2.093  1.00 41.88           C  
+ANISOU 8051  CA  TYR C 178     5230   4963   5721    114   1383    -31       C  
+ATOM   8052  C   TYR C 178     -13.893  50.327   2.813  1.00 43.62           C  
+ANISOU 8052  C   TYR C 178     5428   5133   6014     74   1303   -115       C  
+ATOM   8053  O   TYR C 178     -14.884  51.057   2.781  1.00 71.17           O  
+ANISOU 8053  O   TYR C 178     8963   8570   9509     83   1292   -164       O  
+ATOM   8054  CB  TYR C 178     -14.268  47.845   3.052  1.00 40.10           C  
+ANISOU 8054  CB  TYR C 178     5032   4819   5385    153   1370    -57       C  
+ATOM   8055  CG  TYR C 178     -14.839  46.637   2.343  1.00 40.09           C  
+ANISOU 8055  CG  TYR C 178     5092   4827   5312    188   1430      0       C  
+ATOM   8056  CD1 TYR C 178     -16.193  46.562   2.039  1.00 51.74           C  
+ANISOU 8056  CD1 TYR C 178     6625   6285   6751    191   1440    -10       C  
+ATOM   8057  CD2 TYR C 178     -14.025  45.578   1.964  1.00 52.07           C  
+ANISOU 8057  CD2 TYR C 178     6610   6362   6812    221   1466     61       C  
+ATOM   8058  CE1 TYR C 178     -16.720  45.466   1.385  1.00 46.80           C  
+ANISOU 8058  CE1 TYR C 178     6060   5651   6072    206   1466     35       C  
+ATOM   8059  CE2 TYR C 178     -14.543  44.475   1.309  1.00 41.15           C  
+ANISOU 8059  CE2 TYR C 178     5308   4962   5366    253   1503     97       C  
+ATOM   8060  CZ  TYR C 178     -15.891  44.426   1.023  1.00 52.97           C  
+ANISOU 8060  CZ  TYR C 178     6867   6433   6827    235   1494     82       C  
+ATOM   8061  OH  TYR C 178     -16.411  43.333   0.371  1.00 68.67           O  
+ANISOU 8061  OH  TYR C 178     8939   8388   8764    250   1504    111       O  
+ATOM   8062  N   ILE C 179     -12.775  50.650   3.457  1.00 44.81           N  
+ANISOU 8062  N   ILE C 179     5508   5291   6228     34   1237   -134       N  
+ATOM   8063  CA  ILE C 179     -12.611  51.935   4.127  1.00 48.14           C  
+ANISOU 8063  CA  ILE C 179     5919   5641   6730    -15   1137   -224       C  
+ATOM   8064  C   ILE C 179     -12.675  53.079   3.122  1.00 52.29           C  
+ANISOU 8064  C   ILE C 179     6444   6040   7383    -63   1153   -183       C  
+ATOM   8065  O   ILE C 179     -13.329  54.099   3.359  1.00 56.84           O  
+ANISOU 8065  O   ILE C 179     7074   6526   7997    -64   1104   -263       O  
+ATOM   8066  CB  ILE C 179     -11.272  51.996   4.889  1.00 50.87           C  
+ANISOU 8066  CB  ILE C 179     6175   6015   7138    -66   1038   -237       C  
+ATOM   8067  CG1 ILE C 179     -11.322  51.085   6.114  1.00 50.62           C  
+ANISOU 8067  CG1 ILE C 179     6171   6097   6965    -12    989   -294       C  
+ATOM   8068  CG2 ILE C 179     -10.957  53.418   5.320  1.00 55.22           C  
+ANISOU 8068  CG2 ILE C 179     6717   6455   7809   -140    919   -321       C  
+ATOM   8069  CD1 ILE C 179     -12.521  51.335   7.003  1.00 50.53           C  
+ANISOU 8069  CD1 ILE C 179     6272   6100   6829     40    970   -413       C  
+ATOM   8070  N   LYS C 180     -11.994  52.892   1.995  1.00 54.62           N  
+ANISOU 8070  N   LYS C 180     6685   6327   7739    -92   1231    -53       N  
+ATOM   8071  CA  LYS C 180     -12.011  53.858   0.901  1.00 57.26           C  
+ANISOU 8071  CA  LYS C 180     7027   6552   8177   -137   1267     25       C  
+ATOM   8072  C   LYS C 180     -13.425  54.090   0.381  1.00 55.63           C  
+ANISOU 8072  C   LYS C 180     6930   6299   7907    -81   1293      7       C  
+ATOM   8073  O   LYS C 180     -13.888  55.235   0.281  1.00 72.82           O  
+ANISOU 8073  O   LYS C 180     9144   8359  10165    -99   1246    -19       O  
+ATOM   8074  CB  LYS C 180     -11.101  53.387  -0.237  1.00 49.87           C  
+ANISOU 8074  CB  LYS C 180     6027   5653   7268   -151   1381    178       C  
+ATOM   8075  CG  LYS C 180      -9.617  53.483   0.078  1.00 50.15           C  
+ANISOU 8075  CG  LYS C 180     5912   5713   7429   -222   1359    228       C  
+ATOM   8076  CD  LYS C 180      -8.771  52.803  -0.985  1.00 66.38           C  
+ANISOU 8076  CD  LYS C 180     7896   7839   9485   -199   1506    376       C  
+ATOM   8077  CE  LYS C 180      -7.311  53.209  -0.865  1.00 72.75           C  
+ANISOU 8077  CE  LYS C 180     8517   8655  10471   -286   1495    459       C  
+ATOM   8078  NZ  LYS C 180      -6.566  52.894  -2.114  1.00 79.15           N  
+ANISOU 8078  NZ  LYS C 180     9257   9516  11299   -265   1674    625       N  
+ATOM   8079  N   ALA C 181     -14.105  52.991   0.064  1.00 45.50           N  
+ANISOU 8079  N   ALA C 181     5695   5100   6493    -12   1354     23       N  
+ATOM   8080  CA  ALA C 181     -15.473  53.033  -0.439  1.00 48.22           C  
+ANISOU 8080  CA  ALA C 181     6121   5420   6780     39   1365     16       C  
+ATOM   8081  C   ALA C 181     -16.396  53.760   0.539  1.00 52.19           C  
+ANISOU 8081  C   ALA C 181     6644   5886   7301     68   1294   -106       C  
+ATOM   8082  O   ALA C 181     -17.205  54.604   0.142  1.00 56.27           O  
+ANISOU 8082  O   ALA C 181     7197   6316   7865     91   1274   -112       O  
+ATOM   8083  CB  ALA C 181     -15.979  51.625  -0.703  1.00 41.97           C  
+ANISOU 8083  CB  ALA C 181     5366   4722   5858     90   1414     37       C  
+ATOM   8084  N   LEU C 182     -16.261  53.429   1.820  1.00 47.00           N  
+ANISOU 8084  N   LEU C 182     5966   5296   6597     80   1260   -202       N  
+ATOM   8085  CA  LEU C 182     -17.076  54.044   2.860  1.00 56.07           C  
+ANISOU 8085  CA  LEU C 182     7143   6430   7732    127   1212   -330       C  
+ATOM   8086  C   LEU C 182     -16.806  55.540   2.973  1.00 58.71           C  
+ANISOU 8086  C   LEU C 182     7493   6618   8195    100   1137   -390       C  
+ATOM   8087  O   LEU C 182     -17.732  56.328   3.157  1.00 67.20           O  
+ANISOU 8087  O   LEU C 182     8611   7624   9297    158   1118   -462       O  
+ATOM   8088  CB  LEU C 182     -16.827  53.364   4.208  1.00 66.22           C  
+ANISOU 8088  CB  LEU C 182     8421   7826   8914    146   1192   -409       C  
+ATOM   8089  CG  LEU C 182     -17.611  53.926   5.396  1.00 62.91           C  
+ANISOU 8089  CG  LEU C 182     8045   7417   8441    213   1163   -551       C  
+ATOM   8090  CD1 LEU C 182     -19.097  53.997   5.077  1.00 57.40           C  
+ANISOU 8090  CD1 LEU C 182     7358   6724   7726    288   1226   -550       C  
+ATOM   8091  CD2 LEU C 182     -17.371  53.085   6.638  1.00 49.30           C  
+ANISOU 8091  CD2 LEU C 182     6330   5825   6577    234   1156   -599       C  
+ATOM   8092  N   SER C 183     -15.536  55.925   2.882  1.00 53.79           N  
+ANISOU 8092  N   SER C 183     6830   5941   7667     11   1092   -357       N  
+ATOM   8093  CA  SER C 183     -15.162  57.334   2.933  1.00 57.13           C  
+ANISOU 8093  CA  SER C 183     7267   6198   8241    -43   1005   -398       C  
+ATOM   8094  C   SER C 183     -15.827  58.104   1.797  1.00 61.66           C  
+ANISOU 8094  C   SER C 183     7882   6650   8897    -29   1034   -319       C  
+ATOM   8095  O   SER C 183     -16.471  59.143   2.017  1.00 62.80           O  
+ANISOU 8095  O   SER C 183     8086   6667   9108     10    979   -398       O  
+ATOM   8096  CB  SER C 183     -13.641  57.489   2.861  1.00 59.08           C  
+ANISOU 8096  CB  SER C 183     7431   6419   8600   -162    960   -335       C  
+ATOM   8097  OG  SER C 183     -13.021  56.966   4.023  1.00 66.43           O  
+ANISOU 8097  OG  SER C 183     8328   7443   9469   -171    892   -421       O  
+ATOM   8098  N   GLY C 184     -15.684  57.572   0.584  1.00 55.33           N  
+ANISOU 8098  N   GLY C 184     7060   5885   8078    -49   1120   -163       N  
+ATOM   8099  CA  GLY C 184     -16.300  58.172  -0.586  1.00 54.52           C  
+ANISOU 8099  CA  GLY C 184     7006   5686   8022    -32   1144    -65       C  
+ATOM   8100  C   GLY C 184     -17.803  58.316  -0.435  1.00 54.38           C  
+ANISOU 8100  C   GLY C 184     7042   5661   7958     79   1129   -138       C  
+ATOM   8101  O   GLY C 184     -18.365  59.378  -0.715  1.00 54.68           O  
+ANISOU 8101  O   GLY C 184     7126   5561   8089    110   1084   -142       O  
+ATOM   8102  N   ASP C 185     -18.454  57.245   0.011  1.00 53.27           N  
+ANISOU 8102  N   ASP C 185     6888   5667   7687    140   1167   -187       N  
+ATOM   8103  CA  ASP C 185     -19.900  57.258   0.209  1.00 52.64           C  
+ANISOU 8103  CA  ASP C 185     6821   5608   7571    243   1166   -244       C  
+ATOM   8104  C   ASP C 185     -20.331  58.282   1.254  1.00 57.38           C  
+ANISOU 8104  C   ASP C 185     7442   6127   8233    307   1114   -392       C  
+ATOM   8105  O   ASP C 185     -21.349  58.953   1.090  1.00 54.14           O  
+ANISOU 8105  O   ASP C 185     7048   5648   7875    393   1098   -415       O  
+ATOM   8106  CB  ASP C 185     -20.400  55.869   0.608  1.00 51.97           C  
+ANISOU 8106  CB  ASP C 185     6702   5694   7350    273   1220   -256       C  
+ATOM   8107  CG  ASP C 185     -20.577  54.952  -0.584  1.00 50.15           C  
+ANISOU 8107  CG  ASP C 185     6481   5515   7060    253   1254   -131       C  
+ATOM   8108  OD1 ASP C 185     -20.405  55.426  -1.727  1.00 54.59           O  
+ANISOU 8108  OD1 ASP C 185     7081   5996   7666    232   1244    -35       O  
+ATOM   8109  OD2 ASP C 185     -20.896  53.762  -0.380  1.00 51.41           O  
+ANISOU 8109  OD2 ASP C 185     6622   5788   7124    259   1286   -127       O  
+ATOM   8110  N   LEU C 186     -19.555  58.405   2.326  1.00 57.16           N  
+ANISOU 8110  N   LEU C 186     7418   6105   8195    276   1081   -498       N  
+ATOM   8111  CA  LEU C 186     -19.872  59.367   3.373  1.00 65.89           C  
+ANISOU 8111  CA  LEU C 186     8573   7129   9335    343   1024   -664       C  
+ATOM   8112  C   LEU C 186     -19.658  60.791   2.882  1.00 68.12           C  
+ANISOU 8112  C   LEU C 186     8907   7184   9790    320    944   -661       C  
+ATOM   8113  O   LEU C 186     -20.252  61.730   3.409  1.00 65.17           O  
+ANISOU 8113  O   LEU C 186     8593   6699   9469    410    901   -785       O  
+ATOM   8114  CB  LEU C 186     -19.036  59.104   4.628  1.00 67.91           C  
+ANISOU 8114  CB  LEU C 186     8839   7448   9515    310    983   -779       C  
+ATOM   8115  CG  LEU C 186     -19.528  57.951   5.504  1.00 61.82           C  
+ANISOU 8115  CG  LEU C 186     8047   6879   8563    373   1054   -823       C  
+ATOM   8116  CD1 LEU C 186     -18.486  57.566   6.541  1.00 53.71           C  
+ANISOU 8116  CD1 LEU C 186     7032   5922   7455    321    998   -892       C  
+ATOM   8117  CD2 LEU C 186     -20.834  58.338   6.177  1.00 59.99           C  
+ANISOU 8117  CD2 LEU C 186     7846   6667   8281    518   1098   -937       C  
+ATOM   8118  N   VAL C 187     -18.815  60.955   1.869  1.00 64.40           N  
+ANISOU 8118  N   VAL C 187     8421   6639   9409    207    933   -515       N  
+ATOM   8119  CA  VAL C 187     -18.698  62.257   1.224  1.00 57.46           C  
+ANISOU 8119  CA  VAL C 187     7591   5538   8702    177    868   -466       C  
+ATOM   8120  C   VAL C 187     -19.905  62.515   0.316  1.00 63.63           C  
+ANISOU 8120  C   VAL C 187     8397   6279   9499    276    895   -387       C  
+ATOM   8121  O   VAL C 187     -20.436  63.626   0.276  1.00 59.24           O  
+ANISOU 8121  O   VAL C 187     7900   5549   9058    341    836   -426       O  
+ATOM   8122  CB  VAL C 187     -17.395  62.377   0.406  1.00 57.73           C  
+ANISOU 8122  CB  VAL C 187     7590   5514   8829     18    865   -307       C  
+ATOM   8123  CG1 VAL C 187     -17.404  63.644  -0.439  1.00 57.88           C  
+ANISOU 8123  CG1 VAL C 187     7664   5307   9020    -16    816   -209       C  
+ATOM   8124  CG2 VAL C 187     -16.187  62.363   1.331  1.00 58.92           C  
+ANISOU 8124  CG2 VAL C 187     7700   5671   9015    -84    801   -387       C  
+ATOM   8125  N   SER C 188     -20.357  61.479  -0.387  1.00 71.00           N  
+ANISOU 8125  N   SER C 188     9289   7366  10321    295    971   -282       N  
+ATOM   8126  CA  SER C 188     -21.335  61.665  -1.458  1.00 69.80           C  
+ANISOU 8126  CA  SER C 188     9155   7180  10185    362    972   -173       C  
+ATOM   8127  C   SER C 188     -22.786  61.335  -1.087  1.00 66.99           C  
+ANISOU 8127  C   SER C 188     8762   6915   9776    503    987   -248       C  
+ATOM   8128  O   SER C 188     -23.711  61.954  -1.611  1.00 66.53           O  
+ANISOU 8128  O   SER C 188     8715   6775   9787    592    949   -211       O  
+ATOM   8129  CB  SER C 188     -20.927  60.825  -2.673  1.00 87.85           C  
+ANISOU 8129  CB  SER C 188    11436   9556  12388    290   1025      2       C  
+ATOM   8130  OG  SER C 188     -19.673  61.240  -3.186  1.00100.86           O  
+ANISOU 8130  OG  SER C 188    13102  11119  14101    172   1033    105       O  
+ATOM   8131  N   LYS C 189     -22.991  60.369  -0.196  1.00 71.30           N  
+ANISOU 8131  N   LYS C 189     9253   7630  10207    525   1042   -337       N  
+ATOM   8132  CA  LYS C 189     -24.348  59.948   0.159  1.00 55.23           C  
+ANISOU 8132  CA  LYS C 189     7154   5704   8128    642   1076   -383       C  
+ATOM   8133  C   LYS C 189     -24.716  60.347   1.583  1.00 61.47           C  
+ANISOU 8133  C   LYS C 189     7938   6508   8910    742   1100   -564       C  
+ATOM   8134  O   LYS C 189     -23.870  60.330   2.476  1.00 61.06           O  
+ANISOU 8134  O   LYS C 189     7923   6466   8811    698   1100   -661       O  
+ATOM   8135  CB  LYS C 189     -24.509  58.433  -0.001  1.00 52.65           C  
+ANISOU 8135  CB  LYS C 189     6768   5568   7670    596   1132   -319       C  
+ATOM   8136  CG  LYS C 189     -24.114  57.883  -1.362  1.00 56.02           C  
+ANISOU 8136  CG  LYS C 189     7224   5998   8065    511   1117   -164       C  
+ATOM   8137  CD  LYS C 189     -24.296  56.372  -1.403  1.00 57.26           C  
+ANISOU 8137  CD  LYS C 189     7339   6318   8098    474   1160   -129       C  
+ATOM   8138  CE  LYS C 189     -23.647  55.756  -2.633  1.00 54.94           C  
+ANISOU 8138  CE  LYS C 189     7105   6028   7743    396   1156     -6       C  
+ATOM   8139  NZ  LYS C 189     -24.377  56.100  -3.884  1.00 62.02           N  
+ANISOU 8139  NZ  LYS C 189     8037   6867   8663    425   1091     94       N  
+ATOM   8140  N   THR C 190     -25.981  60.702   1.794  1.00 59.64           N  
+ANISOU 8140  N   THR C 190     7659   6285   8718    885   1119   -608       N  
+ATOM   8141  CA  THR C 190     -26.461  61.023   3.133  1.00 56.19           C  
+ANISOU 8141  CA  THR C 190     7217   5886   8246   1010   1171   -780       C  
+ATOM   8142  C   THR C 190     -26.798  59.734   3.877  1.00 59.72           C  
+ANISOU 8142  C   THR C 190     7583   6566   8541   1006   1273   -788       C  
+ATOM   8143  O   THR C 190     -27.685  58.982   3.472  1.00 65.11           O  
+ANISOU 8143  O   THR C 190     8158   7366   9213   1019   1316   -693       O  
+ATOM   8144  CB  THR C 190     -27.697  61.943   3.091  1.00 62.15           C  
+ANISOU 8144  CB  THR C 190     7939   6562   9114   1189   1171   -822       C  
+ATOM   8145  OG1 THR C 190     -27.334  63.207   2.523  1.00 66.70           O  
+ANISOU 8145  OG1 THR C 190     8612   6893   9836   1197   1068   -821       O  
+ATOM   8146  CG2 THR C 190     -28.245  62.166   4.493  1.00 62.64           C  
+ANISOU 8146  CG2 THR C 190     7995   6693   9111   1340   1258  -1003       C  
+ATOM   8147  N   PHE C 191     -26.085  59.494   4.973  1.00 61.51           N  
+ANISOU 8147  N   PHE C 191     7863   6851   8655    981   1299   -896       N  
+ATOM   8148  CA  PHE C 191     -26.211  58.256   5.736  1.00 69.05           C  
+ANISOU 8148  CA  PHE C 191     8764   8017   9454    961   1391   -888       C  
+ATOM   8149  C   PHE C 191     -27.157  58.342   6.928  1.00 61.39           C  
+ANISOU 8149  C   PHE C 191     7763   7160   8404   1115   1499  -1001       C  
+ATOM   8150  O   PHE C 191     -27.264  59.379   7.582  1.00 52.54           O  
+ANISOU 8150  O   PHE C 191     6715   5954   7296   1233   1494  -1153       O  
+ATOM   8151  CB  PHE C 191     -24.834  57.805   6.231  1.00 69.46           C  
+ANISOU 8151  CB  PHE C 191     8890   8089   9410    845   1353   -915       C  
+ATOM   8152  CG  PHE C 191     -24.068  56.985   5.236  1.00 59.72           C  
+ANISOU 8152  CG  PHE C 191     7638   6865   8190    700   1319   -766       C  
+ATOM   8153  CD1 PHE C 191     -23.532  57.565   4.098  1.00 50.47           C  
+ANISOU 8153  CD1 PHE C 191     6494   5546   7139    633   1246   -692       C  
+ATOM   8154  CD2 PHE C 191     -23.873  55.630   5.447  1.00 54.30           C  
+ANISOU 8154  CD2 PHE C 191     6915   6329   7390    638   1369   -697       C  
+ATOM   8155  CE1 PHE C 191     -22.822  56.806   3.186  1.00 49.83           C  
+ANISOU 8155  CE1 PHE C 191     6402   5484   7048    521   1237   -561       C  
+ATOM   8156  CE2 PHE C 191     -23.166  54.867   4.540  1.00 52.74           C  
+ANISOU 8156  CE2 PHE C 191     6710   6131   7196    528   1345   -576       C  
+ATOM   8157  CZ  PHE C 191     -22.638  55.455   3.408  1.00 59.42           C  
+ANISOU 8157  CZ  PHE C 191     7583   6845   8147    475   1286   -513       C  
+ATOM   8158  N   LEU C 192     -27.845  57.236   7.196  1.00 65.66           N  
+ANISOU 8158  N   LEU C 192     8198   7889   8862   1113   1602   -922       N  
+ATOM   8159  CA  LEU C 192     -28.540  57.045   8.463  1.00 57.06           C  
+ANISOU 8159  CA  LEU C 192     7077   6953   7649   1233   1737  -1002       C  
+ATOM   8160  C   LEU C 192     -27.882  55.921   9.257  1.00 54.12           C  
+ANISOU 8160  C   LEU C 192     6740   6726   7097   1144   1777   -978       C  
+ATOM   8161  O   LEU C 192     -27.931  54.756   8.861  1.00 61.66           O  
+ANISOU 8161  O   LEU C 192     7622   7769   8036   1036   1796   -833       O  
+ATOM   8162  CB  LEU C 192     -30.019  56.733   8.241  1.00 58.09           C  
+ANISOU 8162  CB  LEU C 192     7031   7193   7847   1314   1841   -911       C  
+ATOM   8163  CG  LEU C 192     -30.795  56.244   9.467  1.00 56.39           C  
+ANISOU 8163  CG  LEU C 192     6745   7182   7499   1414   2018   -935       C  
+ATOM   8164  CD1 LEU C 192     -30.733  57.269  10.593  1.00 60.02           C  
+ANISOU 8164  CD1 LEU C 192     7322   7620   7862   1587   2073  -1141       C  
+ATOM   8165  CD2 LEU C 192     -32.237  55.925   9.105  1.00 50.77           C  
+ANISOU 8165  CD2 LEU C 192     5818   6574   6900   1470   2109   -816       C  
+ATOM   8166  N   PHE C 193     -27.263  56.277  10.377  1.00 67.02           N  
+ANISOU 8166  N   PHE C 193     8498   8373   8594   1192   1777  -1122       N  
+ATOM   8167  CA  PHE C 193     -26.692  55.284  11.277  1.00 60.62           C  
+ANISOU 8167  CA  PHE C 193     7731   7707   7594   1134   1811  -1103       C  
+ATOM   8168  C   PHE C 193     -27.750  54.755  12.239  1.00 68.32           C  
+ANISOU 8168  C   PHE C 193     8642   8883   8433   1239   1992  -1086       C  
+ATOM   8169  O   PHE C 193     -28.424  55.528  12.919  1.00 63.82           O  
+ANISOU 8169  O   PHE C 193     8091   8340   7819   1404   2079  -1209       O  
+ATOM   8170  CB  PHE C 193     -25.520  55.876  12.065  1.00 62.24           C  
+ANISOU 8170  CB  PHE C 193     8103   7844   7701   1131   1705  -1261       C  
+ATOM   8171  CG  PHE C 193     -24.295  56.146  11.235  1.00 61.31           C  
+ANISOU 8171  CG  PHE C 193     8025   7564   7707    993   1540  -1241       C  
+ATOM   8172  CD1 PHE C 193     -24.243  57.227  10.369  1.00 61.76           C  
+ANISOU 8172  CD1 PHE C 193     8091   7427   7948    993   1458  -1272       C  
+ATOM   8173  CD2 PHE C 193     -23.185  55.324  11.336  1.00 63.97           C  
+ANISOU 8173  CD2 PHE C 193     8384   7945   7979    869   1473  -1178       C  
+ATOM   8174  CE1 PHE C 193     -23.111  57.473   9.612  1.00 58.31           C  
+ANISOU 8174  CE1 PHE C 193     7678   6852   7623    860   1328  -1231       C  
+ATOM   8175  CE2 PHE C 193     -22.051  55.567  10.585  1.00 61.48           C  
+ANISOU 8175  CE2 PHE C 193     8080   7497   7784    749   1343  -1147       C  
+ATOM   8176  CZ  PHE C 193     -22.014  56.642   9.721  1.00 50.69           C  
+ANISOU 8176  CZ  PHE C 193     6716   5947   6596    739   1278  -1170       C  
+ATOM   8177  N   VAL C 194     -27.896  53.435  12.290  1.00 66.70           N  
+ANISOU 8177  N   VAL C 194     8361   8815   8166   1148   2056   -929       N  
+ATOM   8178  CA  VAL C 194     -28.868  52.813  13.182  1.00 62.50           C  
+ANISOU 8178  CA  VAL C 194     7753   8482   7511   1221   2240   -871       C  
+ATOM   8179  C   VAL C 194     -28.376  51.431  13.618  1.00 51.62           C  
+ANISOU 8179  C   VAL C 194     6394   7220   6000   1102   2257   -740       C  
+ATOM   8180  O   VAL C 194     -27.766  50.699  12.837  1.00 47.86           O  
+ANISOU 8180  O   VAL C 194     5909   6679   5598    957   2157   -636       O  
+ATOM   8181  CB  VAL C 194     -30.263  52.706  12.515  1.00 49.99           C  
+ANISOU 8181  CB  VAL C 194     5965   6938   6091   1252   2335   -759       C  
+ATOM   8182  CG1 VAL C 194     -30.209  51.829  11.272  1.00 46.86           C  
+ANISOU 8182  CG1 VAL C 194     5479   6485   5842   1080   2241   -590       C  
+ATOM   8183  CG2 VAL C 194     -31.299  52.188  13.506  1.00 55.51           C  
+ANISOU 8183  CG2 VAL C 194     6562   7852   6678   1336   2549   -694       C  
+ATOM   8184  N   GLY C 195     -28.627  51.090  14.878  1.00 51.15           N  
+ANISOU 8184  N   GLY C 195     6374   7327   5733   1176   2389   -746       N  
+ATOM   8185  CA  GLY C 195     -28.177  49.827  15.435  1.00 48.02           C  
+ANISOU 8185  CA  GLY C 195     6014   7040   5193   1081   2408   -617       C  
+ATOM   8186  C   GLY C 195     -26.829  49.951  16.119  1.00 47.97           C  
+ANISOU 8186  C   GLY C 195     6198   7008   5021   1073   2283   -723       C  
+ATOM   8187  O   GLY C 195     -26.194  48.949  16.448  1.00 50.10           O  
+ANISOU 8187  O   GLY C 195     6514   7330   5191    988   2248   -621       O  
+ATOM   8188  N   PHE C 196     -26.389  51.188  16.330  1.00 54.12           N  
+ANISOU 8188  N   PHE C 196     7085   7695   5783   1161   2199   -927       N  
+ATOM   8189  CA  PHE C 196     -25.137  51.447  17.031  1.00 59.60           C  
+ANISOU 8189  CA  PHE C 196     7953   8360   6332   1155   2055  -1049       C  
+ATOM   8190  C   PHE C 196     -25.385  52.115  18.382  1.00 67.66           C  
+ANISOU 8190  C   PHE C 196     9116   9481   7112   1322   2125  -1218       C  
+ATOM   8191  O   PHE C 196     -26.103  53.111  18.467  1.00 78.16           O  
+ANISOU 8191  O   PHE C 196    10451  10780   8468   1457   2196  -1351       O  
+ATOM   8192  CB  PHE C 196     -24.219  52.326  16.178  1.00 67.27           C  
+ANISOU 8192  CB  PHE C 196     8956   9119   7485   1092   1861  -1152       C  
+ATOM   8193  CG  PHE C 196     -23.749  51.671  14.909  1.00 63.95           C  
+ANISOU 8193  CG  PHE C 196     8433   8608   7256    938   1785  -1000       C  
+ATOM   8194  CD1 PHE C 196     -22.713  50.751  14.927  1.00 60.31           C  
+ANISOU 8194  CD1 PHE C 196     7995   8164   6755    831   1696   -908       C  
+ATOM   8195  CD2 PHE C 196     -24.337  51.986  13.694  1.00 66.69           C  
+ANISOU 8195  CD2 PHE C 196     8671   8853   7816    914   1800   -951       C  
+ATOM   8196  CE1 PHE C 196     -22.277  50.152  13.759  1.00 66.50           C  
+ANISOU 8196  CE1 PHE C 196     8699   8866   7702    713   1641   -782       C  
+ATOM   8197  CE2 PHE C 196     -23.905  51.391  12.522  1.00 54.87           C  
+ANISOU 8197  CE2 PHE C 196     7106   7278   6464    787   1734   -822       C  
+ATOM   8198  CZ  PHE C 196     -22.873  50.473  12.555  1.00 52.26           C  
+ANISOU 8198  CZ  PHE C 196     6805   6967   6086    690   1663   -744       C  
+ATOM   8199  N   SER C 197     -24.786  51.564  19.432  1.00 63.82           N  
+ANISOU 8199  N   SER C 197     8755   9112   6382   1325   2100  -1215       N  
+ATOM   8200  CA  SER C 197     -24.834  52.175  20.758  1.00 55.46           C  
+ANISOU 8200  CA  SER C 197     7875   8147   5049   1482   2135  -1392       C  
+ATOM   8201  C   SER C 197     -23.429  52.580  21.188  1.00 66.07           C  
+ANISOU 8201  C   SER C 197     9392   9401   6308   1440   1882  -1538       C  
+ATOM   8202  O   SER C 197     -22.461  52.321  20.473  1.00 72.69           O  
+ANISOU 8202  O   SER C 197    10184  10125   7309   1290   1710  -1478       O  
+ATOM   8203  CB  SER C 197     -25.457  51.219  21.778  1.00 57.08           C  
+ANISOU 8203  CB  SER C 197     8097   8596   4994   1543   2333  -1259       C  
+ATOM   8204  OG  SER C 197     -24.702  50.027  21.896  1.00 71.71           O  
+ANISOU 8204  OG  SER C 197     9961  10501   6785   1411   2255  -1087       O  
+ATOM   8205  N   PHE C 198     -23.310  53.217  22.350  1.00 58.60           N  
+ANISOU 8205  N   PHE C 198     8644   8511   5110   1573   1857  -1732       N  
+ATOM   8206  CA  PHE C 198     -22.012  53.719  22.792  1.00 60.51           C  
+ANISOU 8206  CA  PHE C 198     9052   8657   5284   1531   1587  -1893       C  
+ATOM   8207  C   PHE C 198     -21.078  52.586  23.217  1.00 66.42           C  
+ANISOU 8207  C   PHE C 198     9825   9507   5902   1425   1478  -1747       C  
+ATOM   8208  O   PHE C 198     -19.885  52.803  23.426  1.00 84.98           O  
+ANISOU 8208  O   PHE C 198    12261  11782   8246   1355   1230  -1830       O  
+ATOM   8209  CB  PHE C 198     -22.177  54.739  23.930  1.00 62.41           C  
+ANISOU 8209  CB  PHE C 198     9523   8915   5273   1712   1570  -2164       C  
+ATOM   8210  CG  PHE C 198     -22.805  54.186  25.183  1.00 64.81           C  
+ANISOU 8210  CG  PHE C 198     9944   9474   5206   1859   1759  -2139       C  
+ATOM   8211  CD1 PHE C 198     -22.043  53.513  26.126  1.00 65.94           C  
+ANISOU 8211  CD1 PHE C 198    10230   9747   5078   1836   1652  -2104       C  
+ATOM   8212  CD2 PHE C 198     -24.154  54.376  25.434  1.00 69.87           C  
+ANISOU 8212  CD2 PHE C 198    10552  10230   5765   2031   2047  -2147       C  
+ATOM   8213  CE1 PHE C 198     -22.620  53.020  27.283  1.00 75.66           C  
+ANISOU 8213  CE1 PHE C 198    11583  11218   5946   1974   1835  -2065       C  
+ATOM   8214  CE2 PHE C 198     -24.736  53.885  26.589  1.00 71.58           C  
+ANISOU 8214  CE2 PHE C 198    10871  10694   5631   2170   2247  -2109       C  
+ATOM   8215  CZ  PHE C 198     -23.967  53.207  27.514  1.00 73.42           C  
+ANISOU 8215  CZ  PHE C 198    11264  11055   5578   2139   2144  -2065       C  
+ATOM   8216  N   THR C 199     -21.627  51.381  23.340  1.00 60.39           N  
+ANISOU 8216  N   THR C 199     8982   8909   5054   1413   1655  -1522       N  
+ATOM   8217  CA  THR C 199     -20.837  50.210  23.704  1.00 61.47           C  
+ANISOU 8217  CA  THR C 199     9139   9136   5083   1324   1569  -1354       C  
+ATOM   8218  C   THR C 199     -20.342  49.441  22.478  1.00 70.15           C  
+ANISOU 8218  C   THR C 199    10053  10128   6472   1156   1506  -1168       C  
+ATOM   8219  O   THR C 199     -19.717  48.389  22.614  1.00 63.38           O  
+ANISOU 8219  O   THR C 199     9187   9322   5571   1084   1444  -1010       O  
+ATOM   8220  CB  THR C 199     -21.637  49.248  24.602  1.00 65.44           C  
+ANISOU 8220  CB  THR C 199     9680   9869   5316   1399   1788  -1194       C  
+ATOM   8221  OG1 THR C 199     -22.932  49.025  24.032  1.00 74.26           O  
+ANISOU 8221  OG1 THR C 199    10632  11023   6562   1415   2043  -1075       O  
+ATOM   8222  CG2 THR C 199     -21.794  49.826  26.002  1.00 73.81           C  
+ANISOU 8222  CG2 THR C 199    10971  11065   6010   1570   1816  -1368       C  
+ATOM   8223  N   ASP C 200     -20.623  49.962  21.286  1.00 58.16           N  
+ANISOU 8223  N   ASP C 200     8401   8459   5238   1106   1523  -1188       N  
+ATOM   8224  CA  ASP C 200     -20.212  49.297  20.051  1.00 59.96           C  
+ANISOU 8224  CA  ASP C 200     8471   8585   5726    964   1479  -1028       C  
+ATOM   8225  C   ASP C 200     -18.688  49.259  19.966  1.00 70.01           C  
+ANISOU 8225  C   ASP C 200     9768   9777   7057    875   1235  -1050       C  
+ATOM   8226  O   ASP C 200     -18.029  50.287  20.123  1.00 87.67           O  
+ANISOU 8226  O   ASP C 200    12069  11919   9320    877   1074  -1227       O  
+ATOM   8227  CB  ASP C 200     -20.802  50.003  18.828  1.00 60.35           C  
+ANISOU 8227  CB  ASP C 200     8398   8493   6038    942   1531  -1060       C  
+ATOM   8228  CG  ASP C 200     -20.629  49.201  17.550  1.00 59.62           C  
+ANISOU 8228  CG  ASP C 200     8158   8324   6171    816   1529   -882       C  
+ATOM   8229  OD1 ASP C 200     -19.519  49.216  16.978  1.00 57.50           O  
+ANISOU 8229  OD1 ASP C 200     7867   7950   6029    729   1375   -878       O  
+ATOM   8230  OD2 ASP C 200     -21.607  48.554  17.119  1.00 66.03           O  
+ANISOU 8230  OD2 ASP C 200     8875   9181   7033    807   1682   -749       O  
+ATOM   8231  N   PRO C 201     -18.126  48.068  19.713  1.00 70.77           N  
+ANISOU 8231  N   PRO C 201     9803   9899   7188    796   1204   -866       N  
+ATOM   8232  CA  PRO C 201     -16.674  47.864  19.782  1.00 58.35           C  
+ANISOU 8232  CA  PRO C 201     8235   8284   5650    731    986   -860       C  
+ATOM   8233  C   PRO C 201     -15.880  48.384  18.582  1.00 56.96           C  
+ANISOU 8233  C   PRO C 201     7939   7938   5766    634    874   -885       C  
+ATOM   8234  O   PRO C 201     -14.661  48.503  18.697  1.00 63.26           O  
+ANISOU 8234  O   PRO C 201     8726   8697   6612    586    684   -912       O  
+ATOM   8235  CB  PRO C 201     -16.548  46.341  19.874  1.00 55.64           C  
+ANISOU 8235  CB  PRO C 201     7863   8025   5252    706   1032   -638       C  
+ATOM   8236  CG  PRO C 201     -17.750  45.829  19.164  1.00 52.97           C  
+ANISOU 8236  CG  PRO C 201     7440   7686   4999    693   1246   -519       C  
+ATOM   8237  CD  PRO C 201     -18.851  46.812  19.451  1.00 70.06           C  
+ANISOU 8237  CD  PRO C 201     9641   9883   7097    773   1370   -652       C  
+ATOM   8238  N   ASN C 202     -16.532  48.687  17.463  1.00 54.90           N  
+ANISOU 8238  N   ASN C 202     7584   7583   5694    607    986   -866       N  
+ATOM   8239  CA  ASN C 202     -15.788  49.053  16.256  1.00 55.28           C  
+ANISOU 8239  CA  ASN C 202     7521   7482   6002    515    906   -852       C  
+ATOM   8240  C   ASN C 202     -16.169  50.381  15.595  1.00 56.84           C  
+ANISOU 8240  C   ASN C 202     7703   7544   6351    510    912   -976       C  
+ATOM   8241  O   ASN C 202     -15.383  50.922  14.821  1.00 59.97           O  
+ANISOU 8241  O   ASN C 202     8031   7816   6938    432    817   -986       O  
+ATOM   8242  CB  ASN C 202     -15.892  47.932  15.217  1.00 52.13           C  
+ANISOU 8242  CB  ASN C 202     7016   7071   5720    466   1003   -664       C  
+ATOM   8243  CG  ASN C 202     -15.387  46.602  15.743  1.00 55.66           C  
+ANISOU 8243  CG  ASN C 202     7476   7613   6060    469    980   -530       C  
+ATOM   8244  OD1 ASN C 202     -14.351  46.541  16.407  1.00 55.67           O  
+ANISOU 8244  OD1 ASN C 202     7503   7646   6003    468    832   -550       O  
+ATOM   8245  ND2 ASN C 202     -16.105  45.528  15.436  1.00 60.75           N  
+ANISOU 8245  ND2 ASN C 202     8101   8292   6689    469   1111   -387       N  
+ATOM   8246  N   LEU C 203     -17.350  50.912  15.901  1.00 58.34           N  
+ANISOU 8246  N   LEU C 203     7948   7756   6463    596   1026  -1058       N  
+ATOM   8247  CA  LEU C 203     -17.854  52.096  15.201  1.00 55.59           C  
+ANISOU 8247  CA  LEU C 203     7582   7268   6270    607   1044  -1155       C  
+ATOM   8248  C   LEU C 203     -16.947  53.325  15.309  1.00 62.63           C  
+ANISOU 8248  C   LEU C 203     8524   8018   7253    570    859  -1310       C  
+ATOM   8249  O   LEU C 203     -16.694  54.002  14.312  1.00 65.13           O  
+ANISOU 8249  O   LEU C 203     8778   8183   7785    504    820  -1304       O  
+ATOM   8250  CB  LEU C 203     -19.248  52.467  15.711  1.00 53.09           C  
+ANISOU 8250  CB  LEU C 203     7318   7016   5840    736   1194  -1230       C  
+ATOM   8251  CG  LEU C 203     -19.837  53.699  15.015  1.00 53.28           C  
+ANISOU 8251  CG  LEU C 203     7326   6889   6030    771   1210  -1326       C  
+ATOM   8252  CD1 LEU C 203     -20.016  53.445  13.524  1.00 56.56           C  
+ANISOU 8252  CD1 LEU C 203     7607   7221   6661    690   1252  -1179       C  
+ATOM   8253  CD2 LEU C 203     -21.146  54.128  15.656  1.00 53.82           C  
+ANISOU 8253  CD2 LEU C 203     7440   7027   5981    926   1356  -1418       C  
+ATOM   8254  N   ASP C 204     -16.461  53.612  16.511  1.00 63.22           N  
+ANISOU 8254  N   ASP C 204     8720   8136   7165    605    738  -1443       N  
+ATOM   8255  CA  ASP C 204     -15.635  54.797  16.723  1.00 64.69           C  
+ANISOU 8255  CA  ASP C 204     8967   8174   7437    560    536  -1607       C  
+ATOM   8256  C   ASP C 204     -14.309  54.711  15.965  1.00 68.27           C  
+ANISOU 8256  C   ASP C 204     9293   8539   8106    407    394  -1510       C  
+ATOM   8257  O   ASP C 204     -13.819  55.717  15.448  1.00 65.73           O  
+ANISOU 8257  O   ASP C 204     8946   8046   7982    330    287  -1569       O  
+ATOM   8258  CB  ASP C 204     -15.390  55.018  18.219  1.00 64.57           C  
+ANISOU 8258  CB  ASP C 204     9124   8236   7171    633    416  -1775       C  
+ATOM   8259  CG  ASP C 204     -14.746  53.822  18.895  1.00 66.33           C  
+ANISOU 8259  CG  ASP C 204     9345   8629   7227    615    365  -1666       C  
+ATOM   8260  OD1 ASP C 204     -14.816  52.706  18.339  1.00 77.32           O  
+ANISOU 8260  OD1 ASP C 204    10622  10101   8658    584    479  -1466       O  
+ATOM   8261  OD2 ASP C 204     -14.174  54.001  19.991  1.00 66.91           O  
+ANISOU 8261  OD2 ASP C 204     9546   8749   7129    638    200  -1785       O  
+ATOM   8262  N   TYR C 205     -13.734  53.514  15.897  1.00 62.76           N  
+ANISOU 8262  N   TYR C 205     8512   7956   7379    367    402  -1353       N  
+ATOM   8263  CA  TYR C 205     -12.513  53.296  15.127  1.00 63.95           C  
+ANISOU 8263  CA  TYR C 205     8516   8049   7733    244    307  -1238       C  
+ATOM   8264  C   TYR C 205     -12.736  53.567  13.641  1.00 61.83           C  
+ANISOU 8264  C   TYR C 205     8138   7665   7690    189    418  -1140       C  
+ATOM   8265  O   TYR C 205     -12.008  54.342  13.005  1.00 72.46           O  
+ANISOU 8265  O   TYR C 205     9413   8877   9243     93    331  -1140       O  
+ATOM   8266  CB  TYR C 205     -12.004  51.866  15.314  1.00 63.49           C  
+ANISOU 8266  CB  TYR C 205     8397   8136   7590    247    323  -1085       C  
+ATOM   8267  CG  TYR C 205     -10.885  51.516  14.365  1.00 66.45           C  
+ANISOU 8267  CG  TYR C 205     8601   8466   8181    151    283   -947       C  
+ATOM   8268  CD1 TYR C 205      -9.610  52.028  14.553  1.00 68.39           C  
+ANISOU 8268  CD1 TYR C 205     8773   8660   8551     64     84   -979       C  
+ATOM   8269  CD2 TYR C 205     -11.106  50.689  13.270  1.00 70.85           C  
+ANISOU 8269  CD2 TYR C 205     9069   9032   8819    150    443   -787       C  
+ATOM   8270  CE1 TYR C 205      -8.583  51.722  13.686  1.00 69.43           C  
+ANISOU 8270  CE1 TYR C 205     8726   8767   8888    -13     71   -842       C  
+ATOM   8271  CE2 TYR C 205     -10.084  50.379  12.396  1.00 70.07           C  
+ANISOU 8271  CE2 TYR C 205     8822   8902   8900     86    430   -667       C  
+ATOM   8272  CZ  TYR C 205      -8.824  50.898  12.610  1.00 69.69           C  
+ANISOU 8272  CZ  TYR C 205     8683   8819   8979      8    256   -688       C  
+ATOM   8273  OH  TYR C 205      -7.798  50.594  11.745  1.00 71.56           O  
+ANISOU 8273  OH  TYR C 205     8749   9040   9401    -46    265   -557       O  
+ATOM   8274  N   ILE C 206     -13.760  52.910  13.107  1.00 58.20           N  
+ANISOU 8274  N   ILE C 206     7668   7260   7185    247    606  -1049       N  
+ATOM   8275  CA  ILE C 206     -14.137  53.020  11.706  1.00 58.05           C  
+ANISOU 8275  CA  ILE C 206     7569   7154   7332    214    716   -950       C  
+ATOM   8276  C   ILE C 206     -14.376  54.477  11.329  1.00 61.46           C  
+ANISOU 8276  C   ILE C 206     8033   7419   7902    197    674  -1053       C  
+ATOM   8277  O   ILE C 206     -13.879  54.956  10.309  1.00 67.91           O  
+ANISOU 8277  O   ILE C 206     8775   8120   8909    115    658   -985       O  
+ATOM   8278  CB  ILE C 206     -15.397  52.187  11.418  1.00 53.91           C  
+ANISOU 8278  CB  ILE C 206     7053   6714   6715    286    893   -872       C  
+ATOM   8279  CG1 ILE C 206     -15.124  50.710  11.713  1.00 51.32           C  
+ANISOU 8279  CG1 ILE C 206     6702   6520   6275    292    929   -753       C  
+ATOM   8280  CG2 ILE C 206     -15.861  52.391   9.985  1.00 50.62           C  
+ANISOU 8280  CG2 ILE C 206     6576   6205   6453    259    981   -787       C  
+ATOM   8281  CD1 ILE C 206     -16.344  49.824  11.624  1.00 48.18           C  
+ANISOU 8281  CD1 ILE C 206     6317   6205   5784    345   1081   -675       C  
+ATOM   8282  N   LEU C 207     -15.143  55.175  12.162  1.00 58.12           N  
+ANISOU 8282  N   LEU C 207     7725   6981   7376    283    664  -1211       N  
+ATOM   8283  CA  LEU C 207     -15.406  56.592  11.955  1.00 59.68           C  
+ANISOU 8283  CA  LEU C 207     7978   7000   7698    287    609  -1330       C  
+ATOM   8284  C   LEU C 207     -14.112  57.389  12.012  1.00 63.14           C  
+ANISOU 8284  C   LEU C 207     8402   7303   8284    167    413  -1382       C  
+ATOM   8285  O   LEU C 207     -13.934  58.348  11.262  1.00 63.99           O  
+ANISOU 8285  O   LEU C 207     8490   7234   8590    102    371  -1376       O  
+ATOM   8286  CB  LEU C 207     -16.394  57.129  12.992  1.00 59.80           C  
+ANISOU 8286  CB  LEU C 207     8133   7036   7553    428    634  -1511       C  
+ATOM   8287  CG  LEU C 207     -17.859  56.726  12.832  1.00 60.69           C  
+ANISOU 8287  CG  LEU C 207     8237   7242   7582    550    833  -1471       C  
+ATOM   8288  CD1 LEU C 207     -18.699  57.354  13.933  1.00 58.09           C  
+ANISOU 8288  CD1 LEU C 207     8039   6937   7096    703    864  -1660       C  
+ATOM   8289  CD2 LEU C 207     -18.369  57.135  11.459  1.00 56.61           C  
+ANISOU 8289  CD2 LEU C 207     7640   6603   7264    528    897  -1375       C  
+ATOM   8290  N   SER C 208     -13.210  56.993  12.905  1.00 64.92           N  
+ANISOU 8290  N   SER C 208     8635   7610   8422    131    284  -1419       N  
+ATOM   8291  CA  SER C 208     -11.930  57.677  13.017  1.00 68.36           C  
+ANISOU 8291  CA  SER C 208     9031   7929   9013      0     76  -1459       C  
+ATOM   8292  C   SER C 208     -11.111  57.488  11.745  1.00 68.81           C  
+ANISOU 8292  C   SER C 208     8907   7939   9300   -126    109  -1262       C  
+ATOM   8293  O   SER C 208     -10.235  58.297  11.442  1.00 71.42           O  
+ANISOU 8293  O   SER C 208     9173   8128   9834   -251    -19  -1257       O  
+ATOM   8294  CB  SER C 208     -11.146  57.172  14.231  1.00 70.39           C  
+ANISOU 8294  CB  SER C 208     9320   8306   9119     -5    -81  -1524       C  
+ATOM   8295  OG  SER C 208     -10.636  55.869  14.007  1.00 69.94           O  
+ANISOU 8295  OG  SER C 208     9140   8405   9031    -21    -21  -1349       O  
+ATOM   8296  N   ARG C 209     -11.392  56.421  11.000  1.00 67.60           N  
+ANISOU 8296  N   ARG C 209     8673   7899   9112    -93    282  -1098       N  
+ATOM   8297  CA  ARG C 209     -10.688  56.205   9.738  1.00 66.39           C  
+ANISOU 8297  CA  ARG C 209     8366   7714   9143   -185    344   -914       C  
+ATOM   8298  C   ARG C 209     -11.424  56.703   8.488  1.00 64.67           C  
+ANISOU 8298  C   ARG C 209     8152   7390   9031   -181    476   -840       C  
+ATOM   8299  O   ARG C 209     -10.809  56.829   7.429  1.00 65.65           O  
+ANISOU 8299  O   ARG C 209     8172   7458   9314   -264    516   -701       O  
+ATOM   8300  CB  ARG C 209     -10.334  54.730   9.545  1.00 64.23           C  
+ANISOU 8300  CB  ARG C 209     8006   7609   8790   -156    434   -775       C  
+ATOM   8301  CG  ARG C 209      -9.073  54.315  10.282  1.00 67.28           C  
+ANISOU 8301  CG  ARG C 209     8308   8069   9185   -205    287   -766       C  
+ATOM   8302  CD  ARG C 209      -8.554  52.993   9.763  1.00 66.20           C  
+ANISOU 8302  CD  ARG C 209     8059   8054   9042   -180    386   -600       C  
+ATOM   8303  NE  ARG C 209      -7.957  53.183   8.443  1.00 65.54           N  
+ANISOU 8303  NE  ARG C 209     7841   7907   9156   -250    471   -461       N  
+ATOM   8304  CZ  ARG C 209      -7.611  52.200   7.620  1.00 62.75           C  
+ANISOU 8304  CZ  ARG C 209     7398   7623   8818   -218    601   -314       C  
+ATOM   8305  NH1 ARG C 209      -7.793  50.938   7.978  1.00 72.91           N  
+ANISOU 8305  NH1 ARG C 209     8715   9029   9957   -125    647   -284       N  
+ATOM   8306  NH2 ARG C 209      -7.079  52.483   6.439  1.00 67.41           N  
+ANISOU 8306  NH2 ARG C 209     7881   8162   9571   -273    690   -194       N  
+ATOM   8307  N   VAL C 210     -12.721  56.980   8.587  1.00 66.80           N  
+ANISOU 8307  N   VAL C 210     8534   7639   9209    -81    546   -920       N  
+ATOM   8308  CA  VAL C 210     -13.481  57.348   7.392  1.00 65.20           C  
+ANISOU 8308  CA  VAL C 210     8332   7351   9092    -64    659   -837       C  
+ATOM   8309  C   VAL C 210     -14.042  58.768   7.448  1.00 66.46           C  
+ANISOU 8309  C   VAL C 210     8583   7325   9345    -46    597   -952       C  
+ATOM   8310  O   VAL C 210     -14.622  59.254   6.477  1.00 63.35           O  
+ANISOU 8310  O   VAL C 210     8196   6834   9041    -34    662   -882       O  
+ATOM   8311  CB  VAL C 210     -14.648  56.369   7.153  1.00 61.27           C  
+ANISOU 8311  CB  VAL C 210     7855   6981   8445     43    811   -789       C  
+ATOM   8312  N   ARG C 211     -13.862  59.426   8.586  1.00 66.31           N  
+ANISOU 8312  N   ARG C 211     8647   7249   9298    -37    461  -1130       N  
+ATOM   8313  CA  ARG C 211     -14.262  60.821   8.752  1.00 64.96           C  
+ANISOU 8313  CA  ARG C 211     8582   6873   9226    -15    376  -1265       C  
+ATOM   8314  C   ARG C 211     -13.212  61.651   9.468  1.00 72.14           C  
+ANISOU 8314  C   ARG C 211     9525   7649  10234   -120    164  -1384       C  
+ATOM   8315  O   ARG C 211     -12.479  61.155  10.323  1.00 81.74           O  
+ANISOU 8315  O   ARG C 211    10727   8970  11362   -155     68  -1436       O  
+ATOM   8316  CB  ARG C 211     -15.603  60.929   9.480  1.00 64.58           C  
+ANISOU 8316  CB  ARG C 211     8654   6868   9014    164    442  -1416       C  
+ATOM   8317  CG  ARG C 211     -16.790  60.919   8.541  1.00 64.37           C  
+ANISOU 8317  CG  ARG C 211     8608   6835   9016    252    593  -1325       C  
+ATOM   8318  CD  ARG C 211     -16.713  62.213   7.737  1.00 88.69           C  
+ANISOU 8318  CD  ARG C 211    11715   9664  12319    203    525  -1306       C  
+ATOM   8319  NE  ARG C 211     -17.912  62.533   6.974  1.00 85.16           N  
+ANISOU 8319  NE  ARG C 211    11278   9165  11913    308    623  -1256       N  
+ATOM   8320  CZ  ARG C 211     -17.987  62.490   5.648  1.00 94.95           C  
+ANISOU 8320  CZ  ARG C 211    12454  10365  13259    258    679  -1069       C  
+ATOM   8321  NH1 ARG C 211     -16.929  62.139   4.929  1.00 91.08           N  
+ANISOU 8321  NH1 ARG C 211    11885   9884  12838    111    673   -915       N  
+ATOM   8322  NH2 ARG C 211     -19.119  62.812   5.043  1.00102.72           N  
+ANISOU 8322  NH2 ARG C 211    13451  11303  14273    364    741  -1034       N  
+ATOM   8323  N   SER C 212     -13.147  62.927   9.104  1.00 77.57           N  
+ANISOU 8323  N   SER C 212    10262   8096  11115   -175     76  -1421       N  
+ATOM   8324  CA  SER C 212     -12.220  63.848   9.739  1.00 85.05           C  
+ANISOU 8324  CA  SER C 212    11252   8873  12189   -289   -151  -1544       C  
+ATOM   8325  C   SER C 212     -12.946  64.710  10.765  1.00 91.79           C  
+ANISOU 8325  C   SER C 212    12314   9608  12954   -163   -246  -1811       C  
+ATOM   8326  O   SER C 212     -14.079  65.140  10.545  1.00100.50           O  
+ANISOU 8326  O   SER C 212    13506  10646  14034    -24   -146  -1860       O  
+ATOM   8327  CB  SER C 212     -11.530  64.721   8.693  1.00 91.79           C  
+ANISOU 8327  CB  SER C 212    12025   9511  13339   -457   -204  -1401       C  
+ATOM   8328  OG  SER C 212     -10.543  65.535   9.297  1.00105.59           O  
+ANISOU 8328  OG  SER C 212    13791  11094  15237   -600   -441  -1502       O  
+ATOM   8329  N   ALA C 213     -12.281  64.954  11.889  1.00 93.41           N  
+ANISOU 8329  N   ALA C 213    12598   9789  13104   -203   -444  -1986       N  
+ATOM   8330  CA  ALA C 213     -12.856  65.726  12.982  1.00 90.33           C  
+ANISOU 8330  CA  ALA C 213    12431   9297  12593    -73   -547  -2268       C  
+ATOM   8331  C   ALA C 213     -12.550  67.219  12.880  1.00 89.71           C  
+ANISOU 8331  C   ALA C 213    12454   8876  12755   -158   -740  -2380       C  
+ATOM   8332  O   ALA C 213     -11.485  67.608  12.403  1.00 95.76           O  
+ANISOU 8332  O   ALA C 213    13115   9504  13763   -369   -878  -2276       O  
+ATOM   8333  CB  ALA C 213     -12.355  65.182  14.309  1.00 89.99           C  
+ANISOU 8333  CB  ALA C 213    12456   9412  12323    -55   -675  -2415       C  
+ATOM   8334  N   TYR C 214     -13.504  68.037  13.324  1.00 94.11           N  
+ANISOU 8334  N   TYR C 214    13209   9294  13253     12   -739  -2586       N  
+ATOM   8335  CA  TYR C 214     -13.403  69.503  13.336  1.00103.47           C  
+ANISOU 8335  CA  TYR C 214    14541  10124  14650    -28   -923  -2731       C  
+ATOM   8336  C   TYR C 214     -13.280  70.169  11.960  1.00107.26           C  
+ANISOU 8336  C   TYR C 214    14919  10382  15452   -154   -896  -2518       C  
+ATOM   8337  O   TYR C 214     -13.244  71.396  11.865  1.00109.88           O  
+ANISOU 8337  O   TYR C 214    15371  10394  15985   -191  -1040  -2609       O  
+ATOM   8338  CB  TYR C 214     -12.222  69.939  14.209  1.00 95.30           C  
+ANISOU 8338  CB  TYR C 214    13576   8970  13663   -186  -1229  -2889       C  
+ATOM   8339  N   GLU C 215     -13.223  69.369  10.901  1.00 99.62           N  
+ANISOU 8339  N   GLU C 215    13750   9576  14525   -216   -717  -2238       N  
+ATOM   8340  CA  GLU C 215     -13.219  69.899   9.540  1.00100.13           C  
+ANISOU 8340  CA  GLU C 215    13730   9471  14845   -309   -657  -2014       C  
+ATOM   8341  C   GLU C 215     -14.637  70.178   9.057  1.00 98.12           C  
+ANISOU 8341  C   GLU C 215    13554   9177  14550    -98   -495  -2015       C  
+ATOM   8342  O   GLU C 215     -15.503  69.304   9.062  1.00101.41           O  
+ANISOU 8342  O   GLU C 215    13934   9833  14763     60   -310  -1992       O  
+ATOM   8343  CB  GLU C 215     -12.486  68.962   8.582  1.00 97.38           C  
+ANISOU 8343  CB  GLU C 215    13147   9306  14547   -460   -542  -1719       C  
+ATOM   8344  CG  GLU C 215     -11.123  68.507   9.084  1.00103.56           C  
+ANISOU 8344  CG  GLU C 215    13813  10180  15357   -641   -679  -1703       C  
+ATOM   8345  CD  GLU C 215     -10.343  69.612   9.784  1.00114.45           C  
+ANISOU 8345  CD  GLU C 215    15282  11292  16911   -779   -966  -1867       C  
+ATOM   8346  OE1 GLU C 215     -10.067  70.652   9.147  1.00120.97           O  
+ANISOU 8346  OE1 GLU C 215    16114  11839  18010   -906  -1047  -1791       O  
+ATOM   8347  OE2 GLU C 215      -9.991  69.437  10.968  1.00115.88           O  
+ANISOU 8347  OE2 GLU C 215    15533  11536  16958   -768  -1123  -2067       O  
+ATOM   8348  N   ARG C 216     -14.844  71.426   8.647  1.00103.07           N  
+ANISOU 8348  N   ARG C 216    14284   9486  15394   -104   -581  -2034       N  
+ATOM   8349  CA  ARG C 216     -16.158  71.980   8.330  1.00102.63           C  
+ANISOU 8349  CA  ARG C 216    14329   9324  15342    110   -484  -2076       C  
+ATOM   8350  C   ARG C 216     -16.598  71.773   6.883  1.00102.09           C  
+ANISOU 8350  C   ARG C 216    14138   9287  15365    102   -326  -1786       C  
+ATOM   8351  O   ARG C 216     -15.789  71.432   6.016  1.00 97.78           O  
+ANISOU 8351  O   ARG C 216    13453   8783  14916    -88   -301  -1548       O  
+ATOM   8352  CB  ARG C 216     -16.172  73.479   8.644  1.00 95.74           C  
+ANISOU 8352  CB  ARG C 216    13652   8059  14664    125   -677  -2252       C  
+ATOM   8353  N   ASP C 217     -17.903  71.948   6.669  1.00 93.72           N  
+ANISOU 8353  N   ASP C 217    13131   8225  14255    324   -216  -1815       N  
+ATOM   8354  CA  ASP C 217     -18.582  71.785   5.380  1.00 83.34           C  
+ANISOU 8354  CA  ASP C 217    11729   6945  12993    367    -81  -1574       C  
+ATOM   8355  C   ASP C 217     -18.745  70.317   5.013  1.00 86.40           C  
+ANISOU 8355  C   ASP C 217    11955   7689  13185    365     93  -1428       C  
+ATOM   8356  O   ASP C 217     -18.949  69.979   3.846  1.00 97.85           O  
+ANISOU 8356  O   ASP C 217    13315   9197  14664    334    186  -1197       O  
+ATOM   8357  CB  ASP C 217     -17.850  72.529   4.255  1.00 87.58           C  
+ANISOU 8357  CB  ASP C 217    12248   7243  13787    174   -156  -1349       C  
+ATOM   8358  CG  ASP C 217     -17.682  74.007   4.546  1.00100.09           C  
+ANISOU 8358  CG  ASP C 217    13998   8435  15596    157   -342  -1474       C  
+ATOM   8359  OD1 ASP C 217     -18.698  74.734   4.530  1.00 98.34           O  
+ANISOU 8359  OD1 ASP C 217    13890   8051  15422    353   -346  -1559       O  
+ATOM   8360  OD2 ASP C 217     -16.536  74.441   4.787  1.00105.93           O  
+ANISOU 8360  OD2 ASP C 217    14750   9020  16478    -51   -493  -1486       O  
+ATOM   8361  N   GLN C 218     -18.654  69.441   6.008  1.00 85.60           N  
+ANISOU 8361  N   GLN C 218    11830   7818  12878    400    130  -1561       N  
+ATOM   8362  CA  GLN C 218     -18.875  68.026   5.763  1.00 66.43           C  
+ANISOU 8362  CA  GLN C 218     9265   5708  10266    410    287  -1440       C  
+ATOM   8363  C   GLN C 218     -20.360  67.790   5.527  1.00 63.01           C  
+ANISOU 8363  C   GLN C 218     8817   5375   9751    619    421  -1433       C  
+ATOM   8364  O   GLN C 218     -21.200  68.573   5.974  1.00 71.97           O  
+ANISOU 8364  O   GLN C 218    10044   6389  10912    789    405  -1584       O  
+ATOM   8365  CB  GLN C 218     -18.385  67.183   6.942  1.00 75.73           C  
+ANISOU 8365  CB  GLN C 218    10434   7090  11251    395    279  -1574       C  
+ATOM   8366  CG  GLN C 218     -16.877  67.155   7.116  1.00 84.84           C  
+ANISOU 8366  CG  GLN C 218    11553   8205  12479    180    150  -1546       C  
+ATOM   8367  CD  GLN C 218     -16.445  66.325   8.311  1.00 98.51           C  
+ANISOU 8367  CD  GLN C 218    13283  10138  14007    183    124  -1676       C  
+ATOM   8368  OE1 GLN C 218     -16.860  66.583   9.443  1.00 93.81           O  
+ANISOU 8368  OE1 GLN C 218    12813   9545  13285    308     80  -1902       O  
+ATOM   8369  NE2 GLN C 218     -15.612  65.322   8.065  1.00102.44           N  
+ANISOU 8369  NE2 GLN C 218    13648  10808  14466     59    155  -1532       N  
+ATOM   8370  N   ARG C 219     -20.679  66.712   4.822  1.00 68.39           N  
+ANISOU 8370  N   ARG C 219     9375   6270  10341    607    546  -1261       N  
+ATOM   8371  CA  ARG C 219     -22.059  66.286   4.646  1.00 61.29           C  
+ANISOU 8371  CA  ARG C 219     8425   5504   9359    781    665  -1242       C  
+ATOM   8372  C   ARG C 219     -22.674  65.894   5.986  1.00 60.57           C  
+ANISOU 8372  C   ARG C 219     8352   5570   9093    929    731  -1441       C  
+ATOM   8373  O   ARG C 219     -22.019  65.246   6.803  1.00 76.20           O  
+ANISOU 8373  O   ARG C 219    10335   7681  10936    866    729  -1510       O  
+ATOM   8374  CB  ARG C 219     -22.135  65.126   3.654  1.00 59.05           C  
+ANISOU 8374  CB  ARG C 219     8019   5411   9009    709    758  -1027       C  
+ATOM   8375  CG  ARG C 219     -23.510  64.503   3.529  1.00 58.32           C  
+ANISOU 8375  CG  ARG C 219     7848   5482   8831    856    865  -1001       C  
+ATOM   8376  CD  ARG C 219     -23.572  63.554   2.349  1.00 57.93           C  
+ANISOU 8376  CD  ARG C 219     7710   5554   8746    775    914   -788       C  
+ATOM   8377  NE  ARG C 219     -23.351  64.246   1.083  1.00 59.99           N  
+ANISOU 8377  NE  ARG C 219     8005   5646   9145    717    853   -633       N  
+ATOM   8378  CZ  ARG C 219     -24.325  64.657   0.277  1.00 57.67           C  
+ANISOU 8378  CZ  ARG C 219     7701   5288   8922    812    839   -549       C  
+ATOM   8379  NH1 ARG C 219     -25.592  64.445   0.605  1.00 61.16           N  
+ANISOU 8379  NH1 ARG C 219     8078   5827   9332    967    883   -606       N  
+ATOM   8380  NH2 ARG C 219     -24.034  65.280  -0.856  1.00 57.84           N  
+ANISOU 8380  NH2 ARG C 219     7771   5156   9048    752    782   -394       N  
+ATOM   8381  N   ARG C 220     -23.924  66.280   6.221  1.00 60.55           N  
+ANISOU 8381  N   ARG C 220     8355   5561   9088   1132    793  -1522       N  
+ATOM   8382  CA  ARG C 220     -24.578  65.897   7.464  1.00 65.50           C  
+ANISOU 8382  CA  ARG C 220     8991   6360   9537   1287    890  -1691       C  
+ATOM   8383  C   ARG C 220     -25.164  64.498   7.345  1.00 63.65           C  
+ANISOU 8383  C   ARG C 220     8605   6415   9162   1287   1034  -1563       C  
+ATOM   8384  O   ARG C 220     -25.851  64.175   6.376  1.00 71.57           O  
+ANISOU 8384  O   ARG C 220     9499   7462  10232   1296   1080  -1403       O  
+ATOM   8385  CB  ARG C 220     -25.684  66.885   7.847  1.00 70.88           C  
+ANISOU 8385  CB  ARG C 220     9729   6928  10275   1527    919  -1838       C  
+ATOM   8386  CG  ARG C 220     -26.421  66.476   9.121  1.00 71.10           C  
+ANISOU 8386  CG  ARG C 220     9758   7157  10100   1706   1056  -2000       C  
+ATOM   8387  CD  ARG C 220     -27.343  67.556   9.670  1.00 89.15           C  
+ANISOU 8387  CD  ARG C 220    12126   9316  12429   1964   1087  -2188       C  
+ATOM   8388  NE  ARG C 220     -26.624  68.650  10.314  1.00 94.06           N  
+ANISOU 8388  NE  ARG C 220    12965   9692  13083   1978    942  -2407       N  
+ATOM   8389  CZ  ARG C 220     -27.219  69.680  10.907  1.00104.70           C  
+ANISOU 8389  CZ  ARG C 220    14438  10886  14458   2203    944  -2616       C  
+ATOM   8390  NH1 ARG C 220     -28.543  69.753  10.943  1.00110.49           N  
+ANISOU 8390  NH1 ARG C 220    15079  11706  15195   2442   1100  -2624       N  
+ATOM   8391  NH2 ARG C 220     -26.492  70.634  11.472  1.00113.05           N  
+ANISOU 8391  NH2 ARG C 220    15710  11698  15546   2194    784  -2821       N  
+ATOM   8392  N   HIS C 221     -24.882  63.674   8.346  1.00 59.21           N  
+ANISOU 8392  N   HIS C 221     8781   5045   8671    951   1404  -2025       N  
+ATOM   8393  CA  HIS C 221     -25.451  62.339   8.441  1.00 63.16           C  
+ANISOU 8393  CA  HIS C 221     9106   5751   9142    973   1529  -1830       C  
+ATOM   8394  C   HIS C 221     -26.264  62.248   9.720  1.00 63.29           C  
+ANISOU 8394  C   HIS C 221     8999   6070   8979   1192   1541  -1864       C  
+ATOM   8395  O   HIS C 221     -26.240  63.165  10.540  1.00 57.78           O  
+ANISOU 8395  O   HIS C 221     8344   5428   8182   1326   1454  -2052       O  
+ATOM   8396  CB  HIS C 221     -24.357  61.273   8.406  1.00 61.56           C  
+ANISOU 8396  CB  HIS C 221     8807   5586   8997    812   1594  -1706       C  
+ATOM   8397  CG  HIS C 221     -23.413  61.421   7.255  1.00 71.06           C  
+ANISOU 8397  CG  HIS C 221    10111   6538  10353    595   1583  -1703       C  
+ATOM   8398  ND1 HIS C 221     -23.720  60.991   5.982  1.00 72.77           N  
+ANISOU 8398  ND1 HIS C 221    10359   6611  10681    483   1640  -1585       N  
+ATOM   8399  CD2 HIS C 221     -22.170  61.953   7.183  1.00 72.54           C  
+ANISOU 8399  CD2 HIS C 221    10362   6612  10587    464   1525  -1808       C  
+ATOM   8400  CE1 HIS C 221     -22.707  61.252   5.175  1.00 71.37           C  
+ANISOU 8400  CE1 HIS C 221    10261   6252  10602    295   1624  -1614       C  
+ATOM   8401  NE2 HIS C 221     -21.754  61.835   5.878  1.00 75.96           N  
+ANISOU 8401  NE2 HIS C 221    10861   6850  11152    272   1557  -1746       N  
+ATOM   8402  N   TYR C 222     -26.988  61.151   9.893  1.00 59.57           N  
+ANISOU 8402  N   TYR C 222     8374   5798   8461   1223   1648  -1688       N  
+ATOM   8403  CA  TYR C 222     -27.863  61.032  11.047  1.00 55.79           C  
+ANISOU 8403  CA  TYR C 222     7764   5637   7797   1416   1677  -1701       C  
+ATOM   8404  C   TYR C 222     -27.673  59.699  11.755  1.00 63.76           C  
+ANISOU 8404  C   TYR C 222     8604   6885   8736   1375   1774  -1504       C  
+ATOM   8405  O   TYR C 222     -27.374  58.682  11.127  1.00 68.73           O  
+ANISOU 8405  O   TYR C 222     9201   7432   9481   1223   1840  -1321       O  
+ATOM   8406  CB  TYR C 222     -29.321  61.203  10.619  1.00 56.80           C  
+ANISOU 8406  CB  TYR C 222     7869   5807   7905   1527   1703  -1691       C  
+ATOM   8407  CG  TYR C 222     -29.582  62.497   9.881  1.00 62.47           C  
+ANISOU 8407  CG  TYR C 222     8768   6272   8695   1586   1592  -1869       C  
+ATOM   8408  CD1 TYR C 222     -29.854  63.672  10.571  1.00 69.01           C  
+ANISOU 8408  CD1 TYR C 222     9659   7139   9420   1784   1488  -2101       C  
+ATOM   8409  CD2 TYR C 222     -29.548  62.546   8.493  1.00 57.71           C  
+ANISOU 8409  CD2 TYR C 222     8282   5386   8258   1448   1584  -1805       C  
+ATOM   8410  CE1 TYR C 222     -30.088  64.858   9.898  1.00 66.94           C  
+ANISOU 8410  CE1 TYR C 222     9585   6615   9235   1844   1369  -2255       C  
+ATOM   8411  CE2 TYR C 222     -29.781  63.726   7.812  1.00 59.49           C  
+ANISOU 8411  CE2 TYR C 222     8690   5369   8544   1499   1473  -1943       C  
+ATOM   8412  CZ  TYR C 222     -30.051  64.878   8.519  1.00 70.35           C  
+ANISOU 8412  CZ  TYR C 222    10138   6760   9829   1697   1361  -2163       C  
+ATOM   8413  OH  TYR C 222     -30.283  66.054   7.842  1.00 72.39           O  
+ANISOU 8413  OH  TYR C 222    10600   6747  10158   1753   1234  -2293       O  
+ATOM   8414  N   CYS C 223     -27.850  59.714  13.070  1.00 63.26           N  
+ANISOU 8414  N   CYS C 223     8440   7117   8477   1518   1776  -1544       N  
+ATOM   8415  CA  CYS C 223     -27.769  58.501  13.867  1.00 60.74           C  
+ANISOU 8415  CA  CYS C 223     7970   7049   8060   1497   1859  -1343       C  
+ATOM   8416  C   CYS C 223     -28.914  58.472  14.862  1.00 62.78           C  
+ANISOU 8416  C   CYS C 223     8093   7661   8098   1666   1911  -1334       C  
+ATOM   8417  O   CYS C 223     -29.108  59.416  15.620  1.00 58.11           O  
+ANISOU 8417  O   CYS C 223     7507   7212   7358   1835   1850  -1540       O  
+ATOM   8418  CB  CYS C 223     -26.428  58.412  14.597  1.00 61.84           C  
+ANISOU 8418  CB  CYS C 223     8112   7225   8160   1468   1804  -1378       C  
+ATOM   8419  SG  CYS C 223     -26.329  57.058  15.790  1.00 71.17           S  
+ANISOU 8419  SG  CYS C 223     9124   8738   9178   1484   1878  -1139       S  
+ATOM   8420  N   LEU C 224     -29.669  57.382  14.862  1.00 58.80           N  
+ANISOU 8420  N   LEU C 224     7465   7307   7571   1615   2022  -1102       N  
+ATOM   8421  CA  LEU C 224     -30.800  57.252  15.767  1.00 66.81           C  
+ANISOU 8421  CA  LEU C 224     8326   8690   8368   1745   2091  -1067       C  
+ATOM   8422  C   LEU C 224     -30.449  56.351  16.942  1.00 61.40           C  
+ANISOU 8422  C   LEU C 224     7527   8286   7515   1733   2141   -893       C  
+ATOM   8423  O   LEU C 224     -30.059  55.199  16.750  1.00 56.88           O  
+ANISOU 8423  O   LEU C 224     6934   7647   7031   1581   2189   -652       O  
+ATOM   8424  CB  LEU C 224     -32.009  56.695  15.018  1.00 62.17           C  
+ANISOU 8424  CB  LEU C 224     7661   8113   7849   1687   2183   -925       C  
+ATOM   8425  CG  LEU C 224     -32.529  57.485  13.817  1.00 68.93           C  
+ANISOU 8425  CG  LEU C 224     8616   8720   8855   1707   2136  -1066       C  
+ATOM   8426  CD1 LEU C 224     -33.664  56.735  13.137  1.00 66.44           C  
+ANISOU 8426  CD1 LEU C 224     8197   8447   8599   1631   2230   -900       C  
+ATOM   8427  CD2 LEU C 224     -32.981  58.872  14.240  1.00 79.81           C  
+ANISOU 8427  CD2 LEU C 224    10028  10186  10112   1935   2053  -1351       C  
+ATOM   8428  N   ILE C 225     -30.585  56.865  18.161  1.00 63.92           N  
+ANISOU 8428  N   ILE C 225     7778   8919   7589   1899   2123  -1014       N  
+ATOM   8429  CA  ILE C 225     -30.361  56.022  19.334  1.00 69.03           C  
+ANISOU 8429  CA  ILE C 225     8313   9876   8040   1897   2172   -832       C  
+ATOM   8430  C   ILE C 225     -31.499  56.153  20.332  1.00 64.96           C  
+ANISOU 8430  C   ILE C 225     7637   9803   7242   2041   2245   -846       C  
+ATOM   8431  O   ILE C 225     -32.374  56.994  20.172  1.00 73.28           O  
+ANISOU 8431  O   ILE C 225     8666  10924   8254   2170   2243  -1038       O  
+ATOM   8432  CB  ILE C 225     -29.036  56.361  20.053  1.00 67.53           C  
+ANISOU 8432  CB  ILE C 225     8186   9686   7786   1943   2068   -948       C  
+ATOM   8433  CG1 ILE C 225     -29.083  57.776  20.637  1.00 62.94           C  
+ANISOU 8433  CG1 ILE C 225     7635   9217   7062   2142   1978  -1291       C  
+ATOM   8434  CG2 ILE C 225     -27.846  56.176  19.119  1.00 64.50           C  
+ANISOU 8434  CG2 ILE C 225     7934   8909   7666   1793   2003   -932       C  
+ATOM   8435  CD1 ILE C 225     -27.887  58.115  21.500  1.00 63.84           C  
+ANISOU 8435  CD1 ILE C 225     7784   9397   7075   2195   1876  -1418       C  
+ATOM   8436  N   LYS C 226     -31.491  55.299  21.350  1.00 65.65           N  
+ANISOU 8436  N   LYS C 226     7611  10199   7132   2020   2309   -636       N  
+ATOM   8437  CA  LYS C 226     -32.460  55.383  22.436  1.00 71.53           C  
+ANISOU 8437  CA  LYS C 226     8188  11423   7568   2147   2387   -638       C  
+ATOM   8438  C   LYS C 226     -31.782  55.928  23.688  1.00 69.45           C  
+ANISOU 8438  C   LYS C 226     7917  11413   7059   2304   2315   -796       C  
+ATOM   8439  O   LYS C 226     -30.678  55.503  24.028  1.00 69.21           O  
+ANISOU 8439  O   LYS C 226     7946  11311   7038   2246   2258   -704       O  
+ATOM   8440  CB  LYS C 226     -33.075  54.008  22.705  1.00 68.49           C  
+ANISOU 8440  CB  LYS C 226     7673  11241   7108   1992   2523   -263       C  
+ATOM   8441  CG  LYS C 226     -34.039  53.956  23.876  1.00 74.40           C  
+ANISOU 8441  CG  LYS C 226     8228  12529   7511   2088   2622   -220       C  
+ATOM   8442  CD  LYS C 226     -34.470  52.523  24.137  1.00 80.73           C  
+ANISOU 8442  CD  LYS C 226     8929  13488   8257   1890   2745    190       C  
+ATOM   8443  CE  LYS C 226     -35.052  52.349  25.523  1.00 88.80           C  
+ANISOU 8443  CE  LYS C 226     9776  15070   8893   1959   2834    281       C  
+ATOM   8444  NZ  LYS C 226     -34.013  52.519  26.576  1.00 96.74           N  
+ANISOU 8444  NZ  LYS C 226    10831  16217   9707   2063   2751    238       N  
+ATOM   8445  N   LYS C 227     -32.430  56.871  24.368  1.00 79.03           N  
+ANISOU 8445  N   LYS C 227     9051  12926   8050   2512   2307  -1048       N  
+ATOM   8446  CA  LYS C 227     -31.875  57.420  25.604  1.00 76.57           C  
+ANISOU 8446  CA  LYS C 227     8719  12893   7480   2674   2237  -1224       C  
+ATOM   8447  C   LYS C 227     -31.739  56.349  26.676  1.00 75.45           C  
+ANISOU 8447  C   LYS C 227     8463  13111   7094   2614   2314   -928       C  
+ATOM   8448  O   LYS C 227     -32.607  55.487  26.817  1.00 83.01           O  
+ANISOU 8448  O   LYS C 227     9292  14291   7957   2523   2449   -661       O  
+ATOM   8449  CB  LYS C 227     -32.715  58.580  26.145  1.00 86.30           C  
+ANISOU 8449  CB  LYS C 227     9873  14410   8508   2925   2221  -1557       C  
+ATOM   8450  CG  LYS C 227     -32.070  59.216  27.371  1.00 93.52           C  
+ANISOU 8450  CG  LYS C 227    10780  15586   9167   3097   2130  -1780       C  
+ATOM   8451  CD  LYS C 227     -32.292  60.711  27.454  1.00 98.64           C  
+ANISOU 8451  CD  LYS C 227    11479  16216   9785   3336   2018  -2227       C  
+ATOM   8452  CE  LYS C 227     -31.269  61.342  28.390  1.00101.39           C  
+ANISOU 8452  CE  LYS C 227    11883  16655   9986   3452   1886  -2460       C  
+ATOM   8453  NZ  LYS C 227     -31.010  60.494  29.588  1.00101.54           N  
+ANISOU 8453  NZ  LYS C 227    11772  17106   9704   3435   1950  -2249       N  
+ATOM   8454  N   GLU C 228     -30.643  56.406  27.424  1.00 75.87           N  
+ANISOU 8454  N   GLU C 228     8564  13218   7043   2656   2221   -971       N  
+ATOM   8455  CA  GLU C 228     -30.426  55.490  28.533  1.00 79.54           C  
+ANISOU 8455  CA  GLU C 228     8938  14035   7249   2626   2268   -707       C  
+ATOM   8456  C   GLU C 228     -31.436  55.779  29.639  1.00 84.89           C  
+ANISOU 8456  C   GLU C 228     9436  15274   7543   2781   2354   -774       C  
+ATOM   8457  O   GLU C 228     -31.640  56.932  30.021  1.00 85.10           O  
+ANISOU 8457  O   GLU C 228     9442  15453   7440   2987   2298  -1134       O  
+ATOM   8458  CB  GLU C 228     -28.997  55.620  29.062  1.00 81.81           C  
+ANISOU 8458  CB  GLU C 228     9315  14259   7510   2663   2128   -784       C  
+ATOM   8459  CG  GLU C 228     -27.939  55.117  28.097  1.00 75.27           C  
+ANISOU 8459  CG  GLU C 228     8630  12948   7023   2499   2058   -669       C  
+ATOM   8460  CD  GLU C 228     -28.106  53.650  27.767  1.00 91.45           C  
+ANISOU 8460  CD  GLU C 228    10662  14917   9169   2305   2150   -238       C  
+ATOM   8461  OE1 GLU C 228     -28.275  52.844  28.705  1.00 99.64           O  
+ANISOU 8461  OE1 GLU C 228    11614  16279   9966   2293   2205     20       O  
+ATOM   8462  OE2 GLU C 228     -28.070  53.304  26.567  1.00 94.80           O  
+ANISOU 8462  OE2 GLU C 228    11163  14950   9906   2164   2164   -158       O  
+ATOM   8463  N   GLU C 229     -32.070  54.723  30.141  1.00 82.56           N  
+ANISOU 8463  N   GLU C 229     9014  15287   7069   2675   2489   -427       N  
+ATOM   8464  CA  GLU C 229     -33.099  54.849  31.167  1.00 85.78           C  
+ANISOU 8464  CA  GLU C 229     9224  16272   7095   2788   2600   -443       C  
+ATOM   8465  C   GLU C 229     -32.684  54.104  32.437  1.00 94.91           C  
+ANISOU 8465  C   GLU C 229    10320  17814   7928   2768   2620   -193       C  
+ATOM   8466  O   GLU C 229     -31.899  53.159  32.378  1.00 99.27           O  
+ANISOU 8466  O   GLU C 229    10963  18174   8583   2617   2588    105       O  
+ATOM   8467  CB  GLU C 229     -34.431  54.310  30.641  1.00 93.25           C  
+ANISOU 8467  CB  GLU C 229    10042  17306   8081   2665   2762   -250       C  
+ATOM   8468  CG  GLU C 229     -35.065  55.167  29.550  1.00 98.06           C  
+ANISOU 8468  CG  GLU C 229    10675  17653   8930   2734   2746   -527       C  
+ATOM   8469  CD  GLU C 229     -36.289  54.518  28.936  1.00102.49           C  
+ANISOU 8469  CD  GLU C 229    11111  18268   9564   2586   2895   -314       C  
+ATOM   8470  OE1 GLU C 229     -37.409  55.034  29.135  1.00106.09           O  
+ANISOU 8470  OE1 GLU C 229    11399  19055   9855   2710   2972   -476       O  
+ATOM   8471  OE2 GLU C 229     -36.129  53.485  28.254  1.00 91.66           O  
+ANISOU 8471  OE2 GLU C 229     9800  16611   8414   2348   2930      3       O  
+ATOM   8472  N   ARG C 230     -33.209  54.523  33.583  1.00102.01           N  
+ANISOU 8472  N   ARG C 230    11066  19264   8430   2931   2669   -316       N  
+ATOM   8473  CA  ARG C 230     -32.831  53.902  34.848  1.00 99.55           C  
+ANISOU 8473  CA  ARG C 230    10695  19360   7769   2929   2683    -93       C  
+ATOM   8474  C   ARG C 230     -33.400  52.490  34.976  1.00100.88           C  
+ANISOU 8474  C   ARG C 230    10788  19676   7865   2690   2833    423       C  
+ATOM   8475  O   ARG C 230     -34.538  52.221  34.586  1.00101.94           O  
+ANISOU 8475  O   ARG C 230    10807  19906   8020   2591   2975    533       O  
+ATOM   8476  CB  ARG C 230     -33.290  54.762  36.035  1.00 97.66           C  
+ANISOU 8476  CB  ARG C 230    10301  19705   7102   3173   2700   -382       C  
+ATOM   8477  CG  ARG C 230     -32.731  56.180  36.056  1.00 99.00           C  
+ANISOU 8477  CG  ARG C 230    10547  19755   7313   3419   2538   -907       C  
+ATOM   8478  CD  ARG C 230     -33.176  56.992  37.278  1.00102.44           C  
+ANISOU 8478  CD  ARG C 230    10859  20631   7433   3606   2473  -1177       C  
+ATOM   8479  NE  ARG C 230     -33.507  58.369  36.907  1.00100.48           N  
+ANISOU 8479  NE  ARG C 230    10646  20181   7353   3775   2351  -1643       N  
+ATOM   8480  CZ  ARG C 230     -32.888  59.444  37.388  1.00106.40           C  
+ANISOU 8480  CZ  ARG C 230    11461  20899   8066   3958   2173  -2026       C  
+ATOM   8481  NH1 ARG C 230     -31.889  59.309  38.249  1.00107.98           N  
+ANISOU 8481  NH1 ARG C 230    11687  21277   8064   4003   2097  -2021       N  
+ATOM   8482  NH2 ARG C 230     -33.250  60.655  36.991  1.00107.55           N  
+ANISOU 8482  NH2 ARG C 230    11655  20821   8389   4090   2059  -2409       N  
+ATOM   8483  N   ARG C 231     -32.591  51.589  35.520  1.00104.07           N  
+ANISOU 8483  N   ARG C 231    11262  20089   8189   2594   2789    739       N  
+ATOM   8484  CA  ARG C 231     -33.024  50.222  35.761  1.00107.84           C  
+ANISOU 8484  CA  ARG C 231    11696  20697   8581   2364   2908   1252       C  
+ATOM   8485  C   ARG C 231     -33.682  50.093  37.139  1.00114.78           C  
+ANISOU 8485  C   ARG C 231    12392  22275   8945   2413   3021   1372       C  
+ATOM   8486  O   ARG C 231     -33.320  50.806  38.079  1.00120.91           O  
+ANISOU 8486  O   ARG C 231    13125  23393   9423   2625   2957   1130       O  
+ATOM   8487  CB  ARG C 231     -31.842  49.261  35.642  1.00102.82           C  
+ANISOU 8487  CB  ARG C 231    11240  19706   8123   2243   2794   1553       C  
+ATOM   8488  N   PRO C 232     -34.667  49.190  37.257  1.00113.00           N  
+ANISOU 8488  N   PRO C 232    12051  22277   8608   2208   3190   1743       N  
+ATOM   8489  CA  PRO C 232     -35.386  48.954  38.515  1.00116.06           C  
+ANISOU 8489  CA  PRO C 232    12288  23162   8647   2167   3228   1872       C  
+ATOM   8490  C   PRO C 232     -34.473  48.490  39.649  1.00123.80           C  
+ANISOU 8490  C   PRO C 232    13330  24370   9338   2203   3148   2082       C  
+ATOM   8491  O   PRO C 232     -33.863  47.424  39.560  1.00131.53           O  
+ANISOU 8491  O   PRO C 232    14433  25180  10363   2054   3145   2494       O  
+ATOM   8492  CB  PRO C 232     -36.398  47.861  38.144  1.00116.73           C  
+ANISOU 8492  CB  PRO C 232    12313  23189   8850   1856   3359   2270       C  
+ATOM   8493  CG  PRO C 232     -35.862  47.241  36.897  1.00115.73           C  
+ANISOU 8493  CG  PRO C 232    12341  22560   9072   1726   3379   2470       C  
+ATOM   8494  CD  PRO C 232     -35.187  48.350  36.165  1.00110.35           C  
+ANISOU 8494  CD  PRO C 232    11752  21562   8615   1950   3267   2015       C  
+ATOM   8495  N   ASP C 233     -34.397  49.308  40.696  1.00129.12           N  
+ANISOU 8495  N   ASP C 233    13920  25412   9728   2409   3069   1792       N  
+ATOM   8496  CA  ASP C 233     -33.591  49.043  41.889  1.00131.88           C  
+ANISOU 8496  CA  ASP C 233    14301  26040   9766   2480   2978   1923       C  
+ATOM   8497  C   ASP C 233     -32.090  48.873  41.600  1.00130.17           C  
+ANISOU 8497  C   ASP C 233    14280  25561   9618   2566   2866   1969       C  
+ATOM   8498  O   ASP C 233     -31.567  47.761  41.609  1.00133.49           O  
+ANISOU 8498  O   ASP C 233    14812  25862  10047   2421   2862   2410       O  
+ATOM   8499  CB  ASP C 233     -34.123  47.801  42.611  1.00123.61           C  
+ANISOU 8499  CB  ASP C 233    13207  25213   8547   2235   3054   2435       C  
+ATOM   8500  N   GLU C 234     -31.416  49.992  41.347  1.00123.68           N  
+ANISOU 8500  N   GLU C 234    13502  24637   8854   2802   2764   1504       N  
+ATOM   8501  CA  GLU C 234     -29.959  50.059  41.235  1.00121.31           C  
+ANISOU 8501  CA  GLU C 234    13376  23996   8721   2882   2561   1419       C  
+ATOM   8502  C   GLU C 234     -29.528  51.501  41.475  1.00125.61           C  
+ANISOU 8502  C   GLU C 234    13900  24628   9199   3152   2443    842       C  
+ATOM   8503  O   GLU C 234     -30.328  52.423  41.308  1.00125.17           O  
+ANISOU 8503  O   GLU C 234    13741  24707   9112   3260   2512    503       O  
+ATOM   8504  CB  GLU C 234     -29.464  49.542  39.875  1.00115.35           C  
+ANISOU 8504  CB  GLU C 234    12790  22531   8506   2719   2502   1542       C  
+ATOM   8505  CG  GLU C 234     -29.573  50.516  38.708  1.00120.63           C  
+ANISOU 8505  CG  GLU C 234    13495  22796   9544   2771   2477   1132       C  
+ATOM   8506  CD  GLU C 234     -28.769  50.038  37.508  1.00125.37           C  
+ANISOU 8506  CD  GLU C 234    14273  22730  10632   2639   2383   1227       C  
+ATOM   8507  OE1 GLU C 234     -28.262  48.898  37.569  1.00131.99           O  
+ANISOU 8507  OE1 GLU C 234    15195  23429  11528   2507   2351   1619       O  
+ATOM   8508  OE2 GLU C 234     -28.658  50.784  36.509  1.00108.59           O  
+ANISOU 8508  OE2 GLU C 234    12205  20228   8825   2668   2340    917       O  
+ATOM   8509  N   LEU C 235     -28.275  51.690  41.877  1.00121.07           N  
+ANISOU 8509  N   LEU C 235    13419  23978   8602   3262   2259    725       N  
+ATOM   8510  CA  LEU C 235     -27.805  53.005  42.297  1.00116.14           C  
+ANISOU 8510  CA  LEU C 235    12774  23491   7863   3509   2133    195       C  
+ATOM   8511  C   LEU C 235     -27.795  53.998  41.141  1.00112.76           C  
+ANISOU 8511  C   LEU C 235    12416  22587   7841   3548   2083   -211       C  
+ATOM   8512  O   LEU C 235     -27.786  53.621  39.967  1.00107.37           O  
+ANISOU 8512  O   LEU C 235    11830  21401   7566   3387   2103    -81       O  
+ATOM   8513  CB  LEU C 235     -26.412  52.907  42.925  1.00115.87           C  
+ANISOU 8513  CB  LEU C 235    12824  23459   7742   3592   1937    182       C  
+ATOM   8514  CG  LEU C 235     -26.255  52.100  44.219  1.00119.69           C  
+ANISOU 8514  CG  LEU C 235    13251  24451   7773   3606   1941    526       C  
+ATOM   8515  CD1 LEU C 235     -26.172  50.598  43.962  1.00114.26           C  
+ANISOU 8515  CD1 LEU C 235    12647  23561   7204   3378   1986   1123       C  
+ATOM   8516  CD2 LEU C 235     -25.042  52.579  45.006  1.00124.57           C  
+ANISOU 8516  CD2 LEU C 235    13899  25212   8219   3789   1733    284       C  
+ATOM   8517  N   GLU C 236     -27.784  55.275  41.503  1.00107.29           N  
+ANISOU 8517  N   GLU C 236    11679  22062   7023   3767   2010   -706       N  
+ATOM   8518  CA  GLU C 236     -28.007  56.358  40.560  1.00106.08           C  
+ANISOU 8518  CA  GLU C 236    11578  21548   7179   3832   1974  -1115       C  
+ATOM   8519  C   GLU C 236     -26.720  56.738  39.821  1.00102.02           C  
+ANISOU 8519  C   GLU C 236    11241  20480   7043   3804   1787  -1298       C  
+ATOM   8520  O   GLU C 236     -26.754  57.335  38.734  1.00101.38           O  
+ANISOU 8520  O   GLU C 236    11251  19947   7323   3772   1758  -1505       O  
+ATOM   8521  CB  GLU C 236     -28.566  57.565  41.309  1.00107.47           C  
+ANISOU 8521  CB  GLU C 236    11648  22047   7140   4046   1924  -1550       C  
+ATOM   8522  CG  GLU C 236     -29.684  58.295  40.594  1.00118.87           C  
+ANISOU 8522  CG  GLU C 236    13059  23296   8810   4059   1968  -1762       C  
+ATOM   8523  CD  GLU C 236     -30.983  57.498  40.617  1.00129.95           C  
+ANISOU 8523  CD  GLU C 236    14321  24924  10131   3922   2156  -1415       C  
+ATOM   8524  OE1 GLU C 236     -31.019  56.421  41.252  1.00139.44           O  
+ANISOU 8524  OE1 GLU C 236    15457  26425  11100   3808   2245  -1013       O  
+ATOM   8525  OE2 GLU C 236     -31.977  57.953  40.017  1.00133.13           O  
+ANISOU 8525  OE2 GLU C 236    14680  25200  10703   3921   2203  -1542       O  
+ATOM   8526  N   ALA C 237     -25.587  56.353  40.405  1.00102.82           N  
+ANISOU 8526  N   ALA C 237    11386  20629   7053   3807   1662  -1203       N  
+ATOM   8527  CA  ALA C 237     -24.275  56.645  39.839  1.00107.24           C  
+ANISOU 8527  CA  ALA C 237    12083  20736   7926   3775   1483  -1365       C  
+ATOM   8528  C   ALA C 237     -24.038  55.828  38.578  1.00106.12           C  
+ANISOU 8528  C   ALA C 237    12051  20057   8213   3554   1516  -1070       C  
+ATOM   8529  O   ALA C 237     -23.382  56.291  37.646  1.00 99.94           O  
+ANISOU 8529  O   ALA C 237    11376  18809   7787   3501   1424  -1262       O  
+ATOM   8530  CB  ALA C 237     -23.184  56.371  40.863  1.00102.75           C  
+ANISOU 8530  CB  ALA C 237    11505  20421   7114   3849   1343  -1325       C  
+ATOM   8531  N   ASP C 238     -24.572  54.612  38.555  1.00106.50           N  
+ANISOU 8531  N   ASP C 238    12069  20175   8220   3418   1646   -606       N  
+ATOM   8532  CA  ASP C 238     -24.456  53.757  37.381  1.00100.64           C  
+ANISOU 8532  CA  ASP C 238    11423  18947   7870   3211   1686   -317       C  
+ATOM   8533  C   ASP C 238     -25.261  54.350  36.229  1.00103.09           C  
+ANISOU 8533  C   ASP C 238    11758  18945   8468   3157   1769   -495       C  
+ATOM   8534  O   ASP C 238     -24.803  54.377  35.080  1.00112.02           O  
+ANISOU 8534  O   ASP C 238    12998  19575   9988   3051   1726   -534       O  
+ATOM   8535  CB  ASP C 238     -24.938  52.339  37.693  1.00 98.97           C  
+ANISOU 8535  CB  ASP C 238    11177  18896   7531   3076   1802    215       C  
+ATOM   8536  CG  ASP C 238     -24.185  51.708  38.847  1.00113.18           C  
+ANISOU 8536  CG  ASP C 238    12964  21009   9029   3134   1714    427       C  
+ATOM   8537  OD1 ASP C 238     -23.417  52.427  39.520  1.00114.68           O  
+ANISOU 8537  OD1 ASP C 238    13141  21375   9056   3296   1577    136       O  
+ATOM   8538  OD2 ASP C 238     -24.361  50.494  39.083  1.00126.30           O  
+ANISOU 8538  OD2 ASP C 238    14634  22737  10619   3016   1773    885       O  
+ATOM   8539  N   PHE C 239     -26.463  54.826  36.543  1.00 93.41           N  
+ANISOU 8539  N   PHE C 239    10421  18035   7035   3239   1886   -605       N  
+ATOM   8540  CA  PHE C 239     -27.306  55.457  35.539  1.00 97.27           C  
+ANISOU 8540  CA  PHE C 239    10921  18278   7759   3223   1955   -793       C  
+ATOM   8541  C   PHE C 239     -26.682  56.718  34.972  1.00105.66           C  
+ANISOU 8541  C   PHE C 239    12091  19008   9048   3316   1810  -1245       C  
+ATOM   8542  O   PHE C 239     -26.649  56.898  33.759  1.00102.72           O  
+ANISOU 8542  O   PHE C 239    11819  18172   9038   3216   1802  -1294       O  
+ATOM   8543  CB  PHE C 239     -28.680  55.803  36.105  1.00 93.82           C  
+ANISOU 8543  CB  PHE C 239    10323  18303   7022   3330   2093   -868       C  
+ATOM   8544  CG  PHE C 239     -29.506  56.646  35.176  1.00 99.81           C  
+ANISOU 8544  CG  PHE C 239    11088  18843   7994   3371   2131  -1134       C  
+ATOM   8545  CD1 PHE C 239     -29.950  56.133  33.969  1.00 96.16           C  
+ANISOU 8545  CD1 PHE C 239    10672  18006   7858   3192   2209   -938       C  
+ATOM   8546  CD2 PHE C 239     -29.816  57.959  35.498  1.00 94.82           C  
+ANISOU 8546  CD2 PHE C 239    10422  18366   7240   3598   2073  -1590       C  
+ATOM   8547  CE1 PHE C 239     -30.702  56.907  33.105  1.00 88.32           C  
+ANISOU 8547  CE1 PHE C 239     9689  16815   7053   3239   2232  -1176       C  
+ATOM   8548  CE2 PHE C 239     -30.568  58.738  34.637  1.00 92.25           C  
+ANISOU 8548  CE2 PHE C 239    10115  17822   7114   3653   2090  -1830       C  
+ATOM   8549  CZ  PHE C 239     -31.013  58.210  33.440  1.00 89.64           C  
+ANISOU 8549  CZ  PHE C 239     9828  17134   7097   3474   2170  -1615       C  
+ATOM   8550  N   GLU C 240     -26.183  57.590  35.844  1.00107.63           N  
+ANISOU 8550  N   GLU C 240    12324  19490   9080   3497   1692  -1573       N  
+ATOM   8551  CA  GLU C 240     -25.581  58.829  35.363  1.00104.87           C  
+ANISOU 8551  CA  GLU C 240    12085  18821   8940   3572   1544  -2008       C  
+ATOM   8552  C   GLU C 240     -24.271  58.519  34.639  1.00 93.68           C  
+ANISOU 8552  C   GLU C 240    10798  16950   7845   3419   1432  -1936       C  
+ATOM   8553  O   GLU C 240     -23.817  59.292  33.794  1.00 90.44           O  
+ANISOU 8553  O   GLU C 240    10503  16136   7725   3385   1344  -2186       O  
+ATOM   8554  CB  GLU C 240     -25.372  59.822  36.506  1.00101.68           C  
+ANISOU 8554  CB  GLU C 240    11629  18782   8224   3799   1437  -2390       C  
+ATOM   8555  CG  GLU C 240     -25.766  61.247  36.129  1.00109.01           C  
+ANISOU 8555  CG  GLU C 240    12613  19547   9260   3937   1369  -2858       C  
+ATOM   8556  CD  GLU C 240     -27.264  61.407  35.896  1.00124.78           C  
+ANISOU 8556  CD  GLU C 240    14524  21691  11198   4009   1516  -2865       C  
+ATOM   8557  OE1 GLU C 240     -28.045  60.558  36.378  1.00130.87           O  
+ANISOU 8557  OE1 GLU C 240    15152  22840  11732   3990   1671  -2570       O  
+ATOM   8558  OE2 GLU C 240     -27.660  62.380  35.219  1.00127.78           O  
+ANISOU 8558  OE2 GLU C 240    14977  21804  11768   4081   1472  -3161       O  
+ATOM   8559  N   TYR C 241     -23.674  57.378  34.972  1.00 88.41           N  
+ANISOU 8559  N   TYR C 241    10112  16358   7121   3328   1436  -1590       N  
+ATOM   8560  CA  TYR C 241     -22.525  56.869  34.232  1.00 93.90           C  
+ANISOU 8560  CA  TYR C 241    10907  16646   8125   3180   1352  -1468       C  
+ATOM   8561  C   TYR C 241     -22.910  56.557  32.792  1.00 95.71           C  
+ANISOU 8561  C   TYR C 241    11215  16419   8732   3009   1437  -1334       C  
+ATOM   8562  O   TYR C 241     -22.259  57.020  31.854  1.00 80.86           O  
+ANISOU 8562  O   TYR C 241     9436  14128   7160   2932   1361  -1501       O  
+ATOM   8563  CB  TYR C 241     -21.955  55.618  34.908  1.00 87.41           C  
+ANISOU 8563  CB  TYR C 241    10045  16014   7151   3141   1342  -1096       C  
+ATOM   8564  CG  TYR C 241     -20.966  54.854  34.056  1.00 93.37           C  
+ANISOU 8564  CG  TYR C 241    10885  16355   8234   2989   1284   -907       C  
+ATOM   8565  CD1 TYR C 241     -19.627  55.213  34.008  1.00 93.62           C  
+ANISOU 8565  CD1 TYR C 241    10958  16231   8381   3001   1120  -1106       C  
+ATOM   8566  CD2 TYR C 241     -21.377  53.752  33.312  1.00 88.18           C  
+ANISOU 8566  CD2 TYR C 241    10257  15478   7768   2834   1391   -538       C  
+ATOM   8567  CE1 TYR C 241     -18.728  54.507  33.226  1.00 82.91           C  
+ANISOU 8567  CE1 TYR C 241     9659  14526   7316   2875   1071   -950       C  
+ATOM   8568  CE2 TYR C 241     -20.488  53.043  32.533  1.00 81.77           C  
+ANISOU 8568  CE2 TYR C 241     9517  14299   7252   2714   1336   -387       C  
+ATOM   8569  CZ  TYR C 241     -19.166  53.422  32.493  1.00 81.73           C  
+ANISOU 8569  CZ  TYR C 241     9542  14162   7349   2742   1179   -594       C  
+ATOM   8570  OH  TYR C 241     -18.281  52.710  31.715  1.00 94.70           O  
+ANISOU 8570  OH  TYR C 241    11237  15467   9278   2635   1127   -459       O  
+ATOM   8571  N   ARG C 242     -23.968  55.770  32.622  1.00 99.25           N  
+ANISOU 8571  N   ARG C 242    11610  16953   9146   2940   1593  -1033       N  
+ATOM   8572  CA  ARG C 242     -24.441  55.426  31.284  1.00 86.07           C  
+ANISOU 8572  CA  ARG C 242    10004  14886   7813   2781   1678   -901       C  
+ATOM   8573  C   ARG C 242     -24.879  56.673  30.512  1.00 84.22           C  
+ANISOU 8573  C   ARG C 242     9826  14427   7745   2828   1662  -1258       C  
+ATOM   8574  O   ARG C 242     -24.657  56.773  29.304  1.00 76.32           O  
+ANISOU 8574  O   ARG C 242     8927  12994   7079   2710   1649  -1285       O  
+ATOM   8575  CB  ARG C 242     -25.574  54.400  31.363  1.00 80.86           C  
+ANISOU 8575  CB  ARG C 242     9259  14411   7053   2699   1846   -532       C  
+ATOM   8576  CG  ARG C 242     -25.062  52.965  31.390  1.00 80.78           C  
+ANISOU 8576  CG  ARG C 242     9270  14326   7098   2560   1856   -111       C  
+ATOM   8577  CD  ARG C 242     -26.171  51.942  31.573  1.00 84.21           C  
+ANISOU 8577  CD  ARG C 242     9625  14957   7414   2459   2014    267       C  
+ATOM   8578  NE  ARG C 242     -27.221  52.407  32.472  1.00100.60           N  
+ANISOU 8578  NE  ARG C 242    11565  17521   9138   2573   2108    189       N  
+ATOM   8579  CZ  ARG C 242     -28.210  51.640  32.918  1.00102.62           C  
+ANISOU 8579  CZ  ARG C 242    11716  18077   9197   2499   2250    493       C  
+ATOM   8580  NH1 ARG C 242     -28.283  50.368  32.548  1.00110.38           N  
+ANISOU 8580  NH1 ARG C 242    12734  18890  10316   2306   2305    901       N  
+ATOM   8581  NH2 ARG C 242     -29.126  52.142  33.735  1.00103.80           N  
+ANISOU 8581  NH2 ARG C 242    11724  18701   9013   2615   2335    385       N  
+ATOM   8582  N   VAL C 243     -25.501  57.616  31.215  1.00 91.09           N  
+ANISOU 8582  N   VAL C 243    10634  15597   8377   3008   1657  -1531       N  
+ATOM   8583  CA  VAL C 243     -25.904  58.885  30.619  1.00 88.83           C  
+ANISOU 8583  CA  VAL C 243    10414  15113   8224   3090   1615  -1895       C  
+ATOM   8584  C   VAL C 243     -24.686  59.651  30.111  1.00 87.03           C  
+ANISOU 8584  C   VAL C 243    10329  14509   8231   3054   1452  -2153       C  
+ATOM   8585  O   VAL C 243     -24.694  60.182  28.999  1.00 87.13           O  
+ANISOU 8585  O   VAL C 243    10453  14120   8533   2981   1427  -2272       O  
+ATOM   8586  CB  VAL C 243     -26.681  59.765  31.624  1.00 83.09           C  
+ANISOU 8586  CB  VAL C 243     9590  14810   7170   3324   1616  -2173       C  
+ATOM   8587  CG1 VAL C 243     -26.890  61.167  31.069  1.00 82.69           C  
+ANISOU 8587  CG1 VAL C 243     9637  14509   7272   3432   1524  -2586       C  
+ATOM   8588  CG2 VAL C 243     -28.011  59.126  31.966  1.00 84.38           C  
+ANISOU 8588  CG2 VAL C 243     9598  15339   7122   3344   1792  -1945       C  
+ATOM   8589  N   ARG C 244     -23.638  59.694  30.929  1.00 80.19           N  
+ANISOU 8589  N   ARG C 244     9452  13785   7231   3096   1341  -2231       N  
+ATOM   8590  CA  ARG C 244     -22.398  60.366  30.556  1.00 79.32           C  
+ANISOU 8590  CA  ARG C 244     9452  13366   7322   3043   1185  -2470       C  
+ATOM   8591  C   ARG C 244     -21.767  59.698  29.337  1.00 84.34           C  
+ANISOU 8591  C   ARG C 244    10167  13573   8306   2825   1200  -2260       C  
+ATOM   8592  O   ARG C 244     -21.281  60.378  28.431  1.00 84.11           O  
+ANISOU 8592  O   ARG C 244    10251  13167   8541   2736   1132  -2443       O  
+ATOM   8593  CB  ARG C 244     -21.414  60.382  31.728  1.00 81.50           C  
+ANISOU 8593  CB  ARG C 244     9671  13929   7364   3127   1068  -2561       C  
+ATOM   8594  CG  ARG C 244     -20.078  61.031  31.403  1.00 81.07           C  
+ANISOU 8594  CG  ARG C 244     9706  13592   7507   3055    905  -2806       C  
+ATOM   8595  CD  ARG C 244     -20.253  62.433  30.841  1.00 80.60           C  
+ANISOU 8595  CD  ARG C 244     9762  13255   7607   3077    830  -3185       C  
+ATOM   8596  NE  ARG C 244     -18.970  63.066  30.550  1.00 80.62           N  
+ANISOU 8596  NE  ARG C 244     9846  12997   7791   2978    676  -3412       N  
+ATOM   8597  CZ  ARG C 244     -18.835  64.243  29.947  1.00 86.12           C  
+ANISOU 8597  CZ  ARG C 244    10671  13373   8678   2941    586  -3718       C  
+ATOM   8598  NH1 ARG C 244     -19.908  64.919  29.559  1.00 87.80           N  
+ANISOU 8598  NH1 ARG C 244    10954  13477   8930   3019    625  -3837       N  
+ATOM   8599  NH2 ARG C 244     -17.627  64.741  29.724  1.00 90.32           N  
+ANISOU 8599  NH2 ARG C 244    11260  13694   9363   2822    453  -3899       N  
+ATOM   8600  N   LYS C 245     -21.782  58.368  29.315  1.00 75.86           N  
+ANISOU 8600  N   LYS C 245     9037  12557   7227   2736   1288  -1878       N  
+ATOM   8601  CA  LYS C 245     -21.264  57.625  28.170  1.00 77.31           C  
+ANISOU 8601  CA  LYS C 245     9285  12360   7731   2545   1311  -1673       C  
+ATOM   8602  C   LYS C 245     -22.029  57.905  26.888  1.00 83.65           C  
+ANISOU 8602  C   LYS C 245    10165  12832   8788   2453   1388  -1687       C  
+ATOM   8603  O   LYS C 245     -21.431  58.075  25.822  1.00 81.83           O  
+ANISOU 8603  O   LYS C 245    10027  12222   8842   2321   1352  -1740       O  
+ATOM   8604  CB  LYS C 245     -21.295  56.122  28.447  1.00 73.50           C  
+ANISOU 8604  CB  LYS C 245     8734  12007   7184   2487   1386  -1257       C  
+ATOM   8605  CG  LYS C 245     -20.172  55.614  29.312  1.00 74.94           C  
+ANISOU 8605  CG  LYS C 245     8876  12367   7233   2527   1284  -1185       C  
+ATOM   8606  CD  LYS C 245     -18.895  55.645  28.490  1.00 83.70           C  
+ANISOU 8606  CD  LYS C 245    10049  13122   8632   2417   1185  -1273       C  
+ATOM   8607  CE  LYS C 245     -17.765  54.911  29.167  1.00 81.38           C  
+ANISOU 8607  CE  LYS C 245     9705  12962   8253   2446   1086  -1150       C  
+ATOM   8608  NZ  LYS C 245     -16.599  54.769  28.253  1.00 75.23           N  
+ANISOU 8608  NZ  LYS C 245     8966  11846   7773   2327   1012  -1201       N  
+ATOM   8609  N   GLN C 246     -23.350  57.969  26.997  1.00 83.03           N  
+ANISOU 8609  N   GLN C 246    10038  12917   8592   2523   1493  -1646       N  
+ATOM   8610  CA  GLN C 246     -24.180  58.270  25.843  1.00 75.67           C  
+ANISOU 8610  CA  GLN C 246     9168  11710   7872   2460   1560  -1668       C  
+ATOM   8611  C   GLN C 246     -23.914  59.692  25.362  1.00 75.48           C  
+ANISOU 8611  C   GLN C 246     9264  11438   7977   2501   1449  -2042       C  
+ATOM   8612  O   GLN C 246     -23.892  59.954  24.161  1.00 81.58           O  
+ANISOU 8612  O   GLN C 246    10141  11838   9018   2389   1447  -2071       O  
+ATOM   8613  CB  GLN C 246     -25.659  58.070  26.178  1.00 70.99           C  
+ANISOU 8613  CB  GLN C 246     8472  11403   7098   2545   1688  -1566       C  
+ATOM   8614  CG  GLN C 246     -26.592  58.240  24.993  1.00 69.28           C  
+ANISOU 8614  CG  GLN C 246     8299  10935   7090   2483   1760  -1557       C  
+ATOM   8615  CD  GLN C 246     -28.005  57.783  25.298  1.00 71.99           C  
+ANISOU 8615  CD  GLN C 246     8507  11583   7263   2531   1901  -1399       C  
+ATOM   8616  OE1 GLN C 246     -28.696  58.373  26.128  1.00 85.38           O  
+ANISOU 8616  OE1 GLN C 246    10115  13616   8709   2707   1913  -1561       O  
+ATOM   8617  NE2 GLN C 246     -28.439  56.721  24.629  1.00 69.12           N  
+ANISOU 8617  NE2 GLN C 246     8117  11113   7033   2371   2006  -1091       N  
+ATOM   8618  N   GLU C 247     -23.696  60.603  26.305  1.00 80.00           N  
+ANISOU 8618  N   GLU C 247     9826  12214   8355   2658   1351  -2325       N  
+ATOM   8619  CA  GLU C 247     -23.408  61.995  25.974  1.00 81.42           C  
+ANISOU 8619  CA  GLU C 247    10133  12156   8647   2700   1226  -2693       C  
+ATOM   8620  C   GLU C 247     -22.072  62.134  25.246  1.00 79.10           C  
+ANISOU 8620  C   GLU C 247     9946  11502   8608   2521   1132  -2740       C  
+ATOM   8621  O   GLU C 247     -21.959  62.882  24.273  1.00 72.30           O  
+ANISOU 8621  O   GLU C 247     9218  10279   7975   2438   1083  -2883       O  
+ATOM   8622  CB  GLU C 247     -23.408  62.856  27.239  1.00 74.66           C  
+ANISOU 8622  CB  GLU C 247     9235  11618   7515   2909   1132  -2991       C  
+ATOM   8623  N   LEU C 248     -21.065  61.405  25.719  1.00 76.68           N  
+ANISOU 8623  N   LEU C 248     9574  11307   8254   2462   1104  -2616       N  
+ATOM   8624  CA  LEU C 248     -19.759  61.395  25.068  1.00 78.39           C  
+ANISOU 8624  CA  LEU C 248     9852  11235   8695   2289   1027  -2643       C  
+ATOM   8625  C   LEU C 248     -19.832  60.770  23.677  1.00 77.49           C  
+ANISOU 8625  C   LEU C 248     9794  10786   8864   2106   1115  -2427       C  
+ATOM   8626  O   LEU C 248     -19.163  61.223  22.749  1.00 68.20           O  
+ANISOU 8626  O   LEU C 248     8712   9282   7917   1962   1065  -2528       O  
+ATOM   8627  CB  LEU C 248     -18.738  60.645  25.926  1.00 70.20           C  
+ANISOU 8627  CB  LEU C 248     8713  10433   7529   2296    978  -2543       C  
+ATOM   8628  CG  LEU C 248     -18.342  61.316  27.242  1.00 76.71           C  
+ANISOU 8628  CG  LEU C 248     9486  11567   8091   2451    860  -2793       C  
+ATOM   8629  CD1 LEU C 248     -17.329  60.469  27.995  1.00 73.83           C  
+ANISOU 8629  CD1 LEU C 248     9019  11426   7609   2454    808  -2659       C  
+ATOM   8630  CD2 LEU C 248     -17.791  62.708  26.981  1.00 81.30           C  
+ANISOU 8630  CD2 LEU C 248    10176  11922   8791   2418    725  -3172       C  
+ATOM   8631  N   PHE C 249     -20.640  59.723  23.545  1.00 77.48           N  
+ANISOU 8631  N   PHE C 249     9728  10875   8835   2105   1244  -2131       N  
+ATOM   8632  CA  PHE C 249     -20.864  59.073  22.257  1.00 67.44           C  
+ANISOU 8632  CA  PHE C 249     8499   9311   7812   1947   1332  -1928       C  
+ATOM   8633  C   PHE C 249     -21.496  60.039  21.255  1.00 68.31           C  
+ANISOU 8633  C   PHE C 249     8731   9143   8082   1915   1334  -2088       C  
+ATOM   8634  O   PHE C 249     -21.034  60.172  20.112  1.00 62.97           O  
+ANISOU 8634  O   PHE C 249     8146   8134   7647   1760   1324  -2098       O  
+ATOM   8635  CB  PHE C 249     -21.749  57.842  22.451  1.00 65.29           C  
+ANISOU 8635  CB  PHE C 249     8133   9219   7454   1961   1462  -1601       C  
+ATOM   8636  CG  PHE C 249     -22.069  57.107  21.182  1.00 61.68           C  
+ANISOU 8636  CG  PHE C 249     7712   8484   7239   1808   1551  -1394       C  
+ATOM   8637  CD1 PHE C 249     -21.080  56.426  20.492  1.00 64.57           C  
+ANISOU 8637  CD1 PHE C 249     8098   8629   7804   1666   1535  -1286       C  
+ATOM   8638  CD2 PHE C 249     -23.365  57.072  20.696  1.00 63.13           C  
+ANISOU 8638  CD2 PHE C 249     7895   8649   7442   1815   1649  -1319       C  
+ATOM   8639  CE1 PHE C 249     -21.374  55.740  19.330  1.00 62.65           C  
+ANISOU 8639  CE1 PHE C 249     7886   8142   7775   1533   1613  -1115       C  
+ATOM   8640  CE2 PHE C 249     -23.665  56.387  19.535  1.00 70.79           C  
+ANISOU 8640  CE2 PHE C 249     8893   9375   8628   1674   1723  -1141       C  
+ATOM   8641  CZ  PHE C 249     -22.668  55.720  18.851  1.00 63.16           C  
+ANISOU 8641  CZ  PHE C 249     7958   8182   7858   1532   1705  -1041       C  
+ATOM   8642  N   ILE C 250     -22.545  60.723  21.706  1.00 66.98           N  
+ANISOU 8642  N   ILE C 250     8560   9124   7764   2073   1342  -2218       N  
+ATOM   8643  CA  ILE C 250     -23.234  61.724  20.899  1.00 73.41           C  
+ANISOU 8643  CA  ILE C 250     9493   9702   8699   2091   1322  -2388       C  
+ATOM   8644  C   ILE C 250     -22.266  62.828  20.496  1.00 78.49           C  
+ANISOU 8644  C   ILE C 250    10279  10057   9486   2016   1186  -2649       C  
+ATOM   8645  O   ILE C 250     -22.290  63.302  19.361  1.00 80.45           O  
+ANISOU 8645  O   ILE C 250    10655   9968   9944   1907   1170  -2688       O  
+ATOM   8646  CB  ILE C 250     -24.435  62.333  21.656  1.00 74.07           C  
+ANISOU 8646  CB  ILE C 250     9530  10047   8567   2316   1331  -2530       C  
+ATOM   8647  CG1 ILE C 250     -25.526  61.283  21.862  1.00 71.47           C  
+ANISOU 8647  CG1 ILE C 250     9058   9979   8117   2352   1482  -2259       C  
+ATOM   8648  CG2 ILE C 250     -25.010  63.518  20.897  1.00 65.40           C  
+ANISOU 8648  CG2 ILE C 250     8574   8682   7595   2365   1270  -2751       C  
+ATOM   8649  CD1 ILE C 250     -26.685  61.766  22.705  1.00 67.66           C  
+ANISOU 8649  CD1 ILE C 250     8487   9833   7389   2575   1508  -2388       C  
+ATOM   8650  N   SER C 251     -21.412  63.228  21.433  1.00 81.20           N  
+ANISOU 8650  N   SER C 251    10600  10543   9710   2065   1084  -2823       N  
+ATOM   8651  CA  SER C 251     -20.416  64.258  21.169  1.00 77.69           C  
+ANISOU 8651  CA  SER C 251    10277   9851   9390   1974    947  -3076       C  
+ATOM   8652  C   SER C 251     -19.439  63.814  20.082  1.00 81.50           C  
+ANISOU 8652  C   SER C 251    10799  10050  10116   1725    964  -2948       C  
+ATOM   8653  O   SER C 251     -19.140  64.572  19.155  1.00 93.29           O  
+ANISOU 8653  O   SER C 251    12432  11216  11799   1593    913  -3058       O  
+ATOM   8654  CB  SER C 251     -19.656  64.605  22.450  1.00 81.32           C  
+ANISOU 8654  CB  SER C 251    10674  10563   9659   2067    839  -3270       C  
+ATOM   8655  OG  SER C 251     -18.675  65.597  22.208  1.00 96.10           O  
+ANISOU 8655  OG  SER C 251    12657  12197  11659   1956    703  -3519       O  
+ATOM   8656  N   ASP C 252     -18.950  62.583  20.199  1.00 73.30           N  
+ANISOU 8656  N   ASP C 252     9639   9145   9067   1667   1031  -2715       N  
+ATOM   8657  CA  ASP C 252     -18.025  62.025  19.217  1.00 70.05           C  
+ANISOU 8657  CA  ASP C 252     9234   8512   8869   1455   1054  -2594       C  
+ATOM   8658  C   ASP C 252     -18.642  61.946  17.824  1.00 77.70           C  
+ANISOU 8658  C   ASP C 252    10297   9188  10038   1340   1137  -2478       C  
+ATOM   8659  O   ASP C 252     -17.982  62.265  16.836  1.00 78.39           O  
+ANISOU 8659  O   ASP C 252    10466   9005  10315   1161   1116  -2521       O  
+ATOM   8660  CB  ASP C 252     -17.544  60.640  19.654  1.00 74.11           C  
+ANISOU 8660  CB  ASP C 252     9602   9231   9327   1457   1106  -2357       C  
+ATOM   8661  CG  ASP C 252     -16.401  60.709  20.647  1.00 96.06           C  
+ANISOU 8661  CG  ASP C 252    12300  12208  11989   1491    999  -2479       C  
+ATOM   8662  OD1 ASP C 252     -16.081  61.826  21.107  1.00105.77           O  
+ANISOU 8662  OD1 ASP C 252    13578  13449  13160   1522    891  -2754       O  
+ATOM   8663  OD2 ASP C 252     -15.817  59.651  20.962  1.00108.98           O  
+ANISOU 8663  OD2 ASP C 252    13828  13983  13596   1491   1014  -2306       O  
+ATOM   8664  N   LEU C 253     -19.893  61.504  17.734  1.00 82.00           N  
+ANISOU 8664  N   LEU C 253    10820   9803  10532   1433   1231  -2328       N  
+ATOM   8665  CA  LEU C 253     -20.556  61.469  16.430  1.00 76.07           C  
+ANISOU 8665  CA  LEU C 253    10154   8792   9955   1339   1300  -2232       C  
+ATOM   8666  C   LEU C 253     -20.789  62.883  15.899  1.00 70.28           C  
+ANISOU 8666  C   LEU C 253     9590   7815   9298   1333   1216  -2459       C  
+ATOM   8667  O   LEU C 253     -20.707  63.123  14.696  1.00 71.37           O  
+ANISOU 8667  O   LEU C 253     9836   7665   9618   1186   1224  -2438       O  
+ATOM   8668  CB  LEU C 253     -21.873  60.689  16.493  1.00 67.24           C  
+ANISOU 8668  CB  LEU C 253     8960   7826   8762   1437   1414  -2031       C  
+ATOM   8669  CG  LEU C 253     -21.802  59.160  16.360  1.00 65.75           C  
+ANISOU 8669  CG  LEU C 253     8659   7716   8607   1366   1515  -1736       C  
+ATOM   8670  CD1 LEU C 253     -20.731  58.526  17.242  1.00 69.59           C  
+ANISOU 8670  CD1 LEU C 253     9051   8380   9010   1371   1479  -1687       C  
+ATOM   8671  CD2 LEU C 253     -23.162  58.537  16.635  1.00 61.34           C  
+ANISOU 8671  CD2 LEU C 253     8020   7346   7940   1463   1617  -1564       C  
+ATOM   8672  N   SER C 254     -21.062  63.819  16.803  1.00 70.77           N  
+ANISOU 8672  N   SER C 254     9681   7991   9216   1493   1127  -2680       N  
+ATOM   8673  CA  SER C 254     -21.291  65.211  16.429  1.00 78.85           C  
+ANISOU 8673  CA  SER C 254    10881   8774  10306   1514   1022  -2913       C  
+ATOM   8674  C   SER C 254     -20.010  65.802  15.852  1.00 81.80           C  
+ANISOU 8674  C   SER C 254    11363   8878  10840   1298    936  -3022       C  
+ATOM   8675  O   SER C 254     -20.043  66.689  14.998  1.00 68.23           O  
+ANISOU 8675  O   SER C 254     9815   6849   9259   1207    877  -3112       O  
+ATOM   8676  CB  SER C 254     -21.762  66.030  17.632  1.00 87.20           C  
+ANISOU 8676  CB  SER C 254    11933  10033  11167   1747    935  -3151       C  
+ATOM   8677  OG  SER C 254     -21.989  67.381  17.270  1.00107.32           O  
+ANISOU 8677  OG  SER C 254    14668  12316  13793   1780    815  -3384       O  
+ATOM   8678  N   ARG C 255     -18.884  65.296  16.342  1.00 87.97           N  
+ANISOU 8678  N   ARG C 255    12038   9792  11595   1215    926  -3009       N  
+ATOM   8679  CA  ARG C 255     -17.563  65.721  15.899  1.00 89.70           C  
+ANISOU 8679  CA  ARG C 255    12310   9824  11948    996    856  -3107       C  
+ATOM   8680  C   ARG C 255     -17.325  65.435  14.415  1.00 91.23           C  
+ANISOU 8680  C   ARG C 255    12568   9746  12350    774    926  -2955       C  
+ATOM   8681  O   ARG C 255     -16.515  66.096  13.765  1.00 92.94           O  
+ANISOU 8681  O   ARG C 255    12881   9736  12695    575    870  -3049       O  
+ATOM   8682  CB  ARG C 255     -16.503  65.009  16.739  1.00 92.19           C  
+ANISOU 8682  CB  ARG C 255    12456  10394  12177    983    846  -3091       C  
+ATOM   8683  CG  ARG C 255     -15.083  65.484  16.557  1.00 90.42           C  
+ANISOU 8683  CG  ARG C 255    12243  10060  12052    781    759  -3235       C  
+ATOM   8684  CD  ARG C 255     -14.164  64.648  17.430  1.00101.36           C  
+ANISOU 8684  CD  ARG C 255    13438  11738  13335    811    750  -3202       C  
+ATOM   8685  NE  ARG C 255     -14.314  63.226  17.130  1.00106.11           N  
+ANISOU 8685  NE  ARG C 255    13923  12440  13954    825    874  -2919       N  
+ATOM   8686  CZ  ARG C 255     -13.803  62.244  17.866  1.00103.17           C  
+ANISOU 8686  CZ  ARG C 255    13390  12325  13483    898    883  -2816       C  
+ATOM   8687  NH1 ARG C 255     -13.995  60.979  17.514  1.00 95.01           N  
+ANISOU 8687  NH1 ARG C 255    12279  11332  12490    906    986  -2557       N  
+ATOM   8688  NH2 ARG C 255     -13.105  62.526  18.956  1.00106.95           N  
+ANISOU 8688  NH2 ARG C 255    13795  13016  13825    968    778  -2973       N  
+ATOM   8689  N   PHE C 256     -18.041  64.448  13.885  1.00 79.60           N  
+ANISOU 8689  N   PHE C 256    11037   8305  10901    799   1050  -2723       N  
+ATOM   8690  CA  PHE C 256     -17.920  64.063  12.482  1.00 79.04           C  
+ANISOU 8690  CA  PHE C 256    11013   8011  11008    610   1126  -2574       C  
+ATOM   8691  C   PHE C 256     -19.103  64.551  11.652  1.00 76.70           C  
+ANISOU 8691  C   PHE C 256    10858   7519  10766    647   1143  -2542       C  
+ATOM   8692  O   PHE C 256     -19.387  64.002  10.586  1.00 82.73           O  
+ANISOU 8692  O   PHE C 256    11634   8165  11635    551   1227  -2379       O  
+ATOM   8693  CB  PHE C 256     -17.786  62.544  12.358  1.00 77.54           C  
+ANISOU 8693  CB  PHE C 256    10661   7970  10830    594   1241  -2341       C  
+ATOM   8694  CG  PHE C 256     -16.573  61.986  13.044  1.00 76.79           C  
+ANISOU 8694  CG  PHE C 256    10427   8051  10698    561   1217  -2356       C  
+ATOM   8695  CD1 PHE C 256     -15.331  62.569  12.863  1.00 87.88           C  
+ANISOU 8695  CD1 PHE C 256    11849   9368  12172    398   1145  -2506       C  
+ATOM   8696  CD2 PHE C 256     -16.675  60.880  13.872  1.00 66.92           C  
+ANISOU 8696  CD2 PHE C 256     9028   7058   9339    689   1260  -2214       C  
+ATOM   8697  CE1 PHE C 256     -14.211  62.060  13.493  1.00 84.79           C  
+ANISOU 8697  CE1 PHE C 256    11314   9158  11745    380   1113  -2532       C  
+ATOM   8698  CE2 PHE C 256     -15.559  60.366  14.506  1.00 68.45           C  
+ANISOU 8698  CE2 PHE C 256     9098   7414   9495    679   1222  -2225       C  
+ATOM   8699  CZ  PHE C 256     -14.325  60.957  14.315  1.00 71.17           C  
+ANISOU 8699  CZ  PHE C 256     9446   7683   9910    533   1147  -2393       C  
+ATOM   8700  N   ASN C 257     -19.790  65.574  12.157  1.00 75.05           N  
+ANISOU 8700  N   ASN C 257    10749   7285  10480    800   1055  -2709       N  
+ATOM   8701  CA  ASN C 257     -20.990  66.120  11.525  1.00 70.22           C  
+ANISOU 8701  CA  ASN C 257    10267   6513   9900    886   1048  -2705       C  
+ATOM   8702  C   ASN C 257     -22.068  65.050  11.371  1.00 74.29           C  
+ANISOU 8702  C   ASN C 257    10663   7191  10374    990   1175  -2497       C  
+ATOM   8703  O   ASN C 257     -22.814  65.031  10.391  1.00 72.48           O  
+ANISOU 8703  O   ASN C 257    10501   6813  10225    969   1212  -2405       O  
+ATOM   8704  CB  ASN C 257     -20.656  66.743  10.164  1.00 69.95           C  
+ANISOU 8704  CB  ASN C 257    10413   6124  10041    676   1017  -2696       C  
+ATOM   8705  CG  ASN C 257     -21.724  67.710   9.685  1.00 81.99           C  
+ANISOU 8705  CG  ASN C 257    12118   7444  11589    785    946  -2765       C  
+ATOM   8706  OD1 ASN C 257     -22.439  68.311  10.487  1.00 74.55           O  
+ANISOU 8706  OD1 ASN C 257    11200   6582  10545   1009    873  -2913       O  
+ATOM   8707  ND2 ASN C 257     -21.840  67.861   8.371  1.00 92.77           N  
+ANISOU 8707  ND2 ASN C 257    13594   8600  13055    640    932  -2625       N  
+ATOM   8708  N   ILE C 258     -22.138  64.156  12.352  1.00 77.35           N  
+ANISOU 8708  N   ILE C 258    10871   7887  10629   1093   1236  -2420       N  
+ATOM   8709  CA  ILE C 258     -23.213  63.176  12.425  1.00 66.52           C  
+ANISOU 8709  CA  ILE C 258     9377   6703   9194   1195   1350  -2232       C  
+ATOM   8710  C   ILE C 258     -24.181  63.566  13.535  1.00 73.41           C  
+ANISOU 8710  C   ILE C 258    10196   7825   9873   1444   1327  -2338       C  
+ATOM   8711  O   ILE C 258     -23.871  63.428  14.719  1.00 73.19           O  
+ANISOU 8711  O   ILE C 258    10070   8049   9691   1538   1311  -2392       O  
+ATOM   8712  CB  ILE C 258     -22.678  61.755  12.682  1.00 65.87           C  
+ANISOU 8712  CB  ILE C 258     9134   6792   9103   1122   1444  -2026       C  
+ATOM   8713  CG1 ILE C 258     -21.665  61.359  11.606  1.00 71.55           C  
+ANISOU 8713  CG1 ILE C 258     9889   7291  10007    892   1464  -1950       C  
+ATOM   8714  CG2 ILE C 258     -23.825  60.757  12.759  1.00 67.78           C  
+ANISOU 8714  CG2 ILE C 258     9260   7208   9285   1202   1556  -1823       C  
+ATOM   8715  CD1 ILE C 258     -21.076  59.978  11.801  1.00 69.04           C  
+ANISOU 8715  CD1 ILE C 258     9425   7107   9700    835   1536  -1766       C  
+ATOM   8716  N   LYS C 259     -25.355  64.052  13.148  1.00 60.16           N  
+ANISOU 8716  N   LYS C 259     8571   6094   8192   1559   1324  -2375       N  
+ATOM   8717  CA  LYS C 259     -26.343  64.502  14.117  1.00 73.68           C  
+ANISOU 8717  CA  LYS C 259    10224   8051   9719   1810   1303  -2503       C  
+ATOM   8718  C   LYS C 259     -27.017  63.303  14.774  1.00 82.77           C  
+ANISOU 8718  C   LYS C 259    11164   9557  10726   1876   1435  -2307       C  
+ATOM   8719  O   LYS C 259     -27.524  62.412  14.092  1.00 67.42           O  
+ANISOU 8719  O   LYS C 259     9160   7602   8855   1792   1538  -2092       O  
+ATOM   8720  CB  LYS C 259     -27.376  65.403  13.435  1.00 75.25           C  
+ANISOU 8720  CB  LYS C 259    10543   8078   9971   1922   1247  -2611       C  
+ATOM   8721  CG  LYS C 259     -28.482  65.919  14.338  1.00 62.74           C  
+ANISOU 8721  CG  LYS C 259     8888   6749   8202   2204   1222  -2769       C  
+ATOM   8722  CD  LYS C 259     -29.494  66.716  13.529  1.00 63.61           C  
+ANISOU 8722  CD  LYS C 259     9113   6671   8386   2318   1161  -2857       C  
+ATOM   8723  CE  LYS C 259     -30.345  67.610  14.414  1.00 81.18           C  
+ANISOU 8723  CE  LYS C 259    11316   9079  10449   2620   1082  -3111       C  
+ATOM   8724  NZ  LYS C 259     -31.328  68.396  13.616  1.00 88.73           N  
+ANISOU 8724  NZ  LYS C 259    12386   9843  11483   2754   1005  -3203       N  
+ATOM   8725  N   THR C 260     -27.022  63.288  16.103  1.00 83.34           N  
+ANISOU 8725  N   THR C 260    11127   9948  10590   2019   1429  -2381       N  
+ATOM   8726  CA  THR C 260     -27.635  62.194  16.846  1.00 71.69           C  
+ANISOU 8726  CA  THR C 260     9456   8833   8950   2073   1551  -2186       C  
+ATOM   8727  C   THR C 260     -29.017  62.582  17.349  1.00 75.22           C  
+ANISOU 8727  C   THR C 260     9818   9534   9228   2292   1577  -2277       C  
+ATOM   8728  O   THR C 260     -29.188  63.602  18.017  1.00 76.77           O  
+ANISOU 8728  O   THR C 260    10044   9821   9304   2477   1488  -2536       O  
+ATOM   8729  CB  THR C 260     -26.765  61.757  18.039  1.00 78.18           C  
+ANISOU 8729  CB  THR C 260    10188   9901   9616   2084   1543  -2167       C  
+ATOM   8730  OG1 THR C 260     -25.465  61.378  17.572  1.00 78.08           O  
+ANISOU 8730  OG1 THR C 260    10233   9673   9761   1893   1515  -2095       O  
+ATOM   8731  CG2 THR C 260     -27.404  60.580  18.760  1.00 67.57           C  
+ANISOU 8731  CG2 THR C 260     8657   8913   8102   2116   1669  -1925       C  
+ATOM   8732  N   ILE C 261     -30.001  61.754  17.021  1.00 68.14           N  
+ANISOU 8732  N   ILE C 261     8806   8759   8325   2269   1698  -2072       N  
+ATOM   8733  CA  ILE C 261     -31.357  61.932  17.510  1.00 65.72           C  
+ANISOU 8733  CA  ILE C 261     8371   8754   7845   2460   1748  -2127       C  
+ATOM   8734  C   ILE C 261     -31.679  60.889  18.572  1.00 72.62           C  
+ANISOU 8734  C   ILE C 261     9038  10054   8501   2468   1869  -1933       C  
+ATOM   8735  O   ILE C 261     -31.518  59.675  18.363  1.00 75.07           O  
+ANISOU 8735  O   ILE C 261     9285  10372   8866   2292   1964  -1647       O  
+ATOM   8736  CB  ILE C 261     -32.363  61.858  16.362  1.00 64.49           C  
+ANISOU 8736  CB  ILE C 261     8223   8453   7827   2433   1789  -2055       C  
+ATOM   8737  CG1 ILE C 261     -32.035  62.944  15.339  1.00 64.72           C  
+ANISOU 8737  CG1 ILE C 261     8475   8063   8053   2429   1658  -2235       C  
+ATOM   8738  CG2 ILE C 261     -33.784  62.009  16.885  1.00 62.72           C  
+ANISOU 8738  CG2 ILE C 261     7834   8579   7417   2633   1845  -2118       C  
+ATOM   8739  CD1 ILE C 261     -32.364  62.562  13.936  1.00 76.40           C  
+ANISOU 8739  CD1 ILE C 261    10010   9281   9737   2284   1693  -2084       C  
+ATOM   8740  N   VAL C 262     -32.118  61.384  19.723  1.00 68.62           N  
+ANISOU 8740  N   VAL C 262     8434   9898   7742   2674   1859  -2097       N  
+ATOM   8741  CA  VAL C 262     -32.345  60.551  20.889  1.00 68.17           C  
+ANISOU 8741  CA  VAL C 262     8189  10281   7431   2694   1961  -1937       C  
+ATOM   8742  C   VAL C 262     -33.833  60.284  21.109  1.00 69.38           C  
+ANISOU 8742  C   VAL C 262     8155  10777   7430   2786   2079  -1876       C  
+ATOM   8743  O   VAL C 262     -34.601  61.192  21.423  1.00 84.24           O  
+ANISOU 8743  O   VAL C 262     9991  12828   9188   3005   2046  -2125       O  
+ATOM   8744  CB  VAL C 262     -31.745  61.205  22.140  1.00 68.81           C  
+ANISOU 8744  CB  VAL C 262     8266  10586   7294   2853   1878  -2155       C  
+ATOM   8745  CG1 VAL C 262     -31.821  60.262  23.304  1.00 70.33           C  
+ANISOU 8745  CG1 VAL C 262     8284  11217   7223   2847   1979  -1952       C  
+ATOM   8746  CG2 VAL C 262     -30.300  61.600  21.880  1.00 67.64           C  
+ANISOU 8746  CG2 VAL C 262     8296  10098   7307   2763   1750  -2254       C  
+ATOM   8747  N   LEU C 263     -34.223  59.025  20.942  1.00 71.05           N  
+ANISOU 8747  N   LEU C 263     8253  11090   7654   2614   2212  -1549       N  
+ATOM   8748  CA  LEU C 263     -35.613  58.599  21.041  1.00 72.28           C  
+ANISOU 8748  CA  LEU C 263     8213  11562   7687   2640   2339  -1443       C  
+ATOM   8749  C   LEU C 263     -35.940  58.007  22.408  1.00 72.94           C  
+ANISOU 8749  C   LEU C 263     8102  12162   7448   2674   2443  -1314       C  
+ATOM   8750  O   LEU C 263     -35.045  57.667  23.182  1.00 74.21           O  
+ANISOU 8750  O   LEU C 263     8288  12403   7506   2640   2424  -1234       O  
+ATOM   8751  CB  LEU C 263     -35.931  57.580  19.948  1.00 71.24           C  
+ANISOU 8751  CB  LEU C 263     8076  11214   7777   2408   2420  -1163       C  
+ATOM   8752  CG  LEU C 263     -35.565  57.987  18.521  1.00 68.16           C  
+ANISOU 8752  CG  LEU C 263     7875  10322   7700   2338   2332  -1240       C  
+ATOM   8753  CD1 LEU C 263     -35.791  56.829  17.568  1.00 64.06           C  
+ANISOU 8753  CD1 LEU C 263     7337   9631   7374   2100   2416   -952       C  
+ATOM   8754  CD2 LEU C 263     -36.365  59.204  18.087  1.00 65.01           C  
+ANISOU 8754  CD2 LEU C 263     7503   9884   7315   2540   2262  -1528       C  
+ATOM   8755  N   ASN C 264     -37.232  57.882  22.694  1.00 75.92           N  
+ANISOU 8755  N   ASN C 264     8280  12907   7659   2740   2551  -1291       N  
+ATOM   8756  CA  ASN C 264     -37.694  57.331  23.962  1.00 83.55           C  
+ANISOU 8756  CA  ASN C 264     9041  14410   8295   2760   2668  -1158       C  
+ATOM   8757  C   ASN C 264     -37.632  55.803  24.001  1.00 83.14           C  
+ANISOU 8757  C   ASN C 264     8929  14400   8260   2483   2787   -720       C  
+ATOM   8758  O   ASN C 264     -37.454  55.209  25.065  1.00 94.76           O  
+ANISOU 8758  O   ASN C 264    10314  16196   9495   2447   2847   -546       O  
+ATOM   8759  CB  ASN C 264     -39.122  57.802  24.240  1.00 78.13           C  
+ANISOU 8759  CB  ASN C 264     8143  14128   7415   2932   2744  -1313       C  
+ATOM   8760  CG  ASN C 264     -39.268  59.308  24.135  1.00 81.14           C  
+ANISOU 8760  CG  ASN C 264     8594  14435   7800   3225   2611  -1753       C  
+ATOM   8761  OD1 ASN C 264     -38.445  60.061  24.656  1.00 89.23           O  
+ANISOU 8761  OD1 ASN C 264     9737  15400   8768   3363   2494  -1974       O  
+ATOM   8762  ND2 ASN C 264     -40.314  59.755  23.450  1.00 78.87           N  
+ANISOU 8762  ND2 ASN C 264     8238  14142   7587   3323   2617  -1885       N  
+ATOM   8763  N   ASN C 265     -37.782  55.176  22.838  1.00 80.97           N  
+ANISOU 8763  N   ASN C 265     8708  13790   8265   2290   2811   -545       N  
+ATOM   8764  CA  ASN C 265     -37.721  53.721  22.722  1.00 83.61           C  
+ANISOU 8764  CA  ASN C 265     9013  14085   8668   2019   2904   -141       C  
+ATOM   8765  C   ASN C 265     -37.409  53.292  21.292  1.00 81.65           C  
+ANISOU 8765  C   ASN C 265     8908  13324   8790   1844   2866    -48       C  
+ATOM   8766  O   ASN C 265     -37.586  54.068  20.353  1.00 68.57           O  
+ANISOU 8766  O   ASN C 265     7327  11419   7306   1918   2802   -265       O  
+ATOM   8767  CB  ASN C 265     -39.030  53.079  23.189  1.00 78.63           C  
+ANISOU 8767  CB  ASN C 265     8139  13899   7839   1946   3066     47       C  
+ATOM   8768  CG  ASN C 265     -40.246  53.667  22.504  1.00 98.13           C  
+ANISOU 8768  CG  ASN C 265    10494  16436  10356   2031   3098   -137       C  
+ATOM   8769  OD1 ASN C 265     -40.446  54.881  22.507  1.00112.92           O  
+ANISOU 8769  OD1 ASN C 265    12374  18351  12178   2278   3024   -482       O  
+ATOM   8770  ND2 ASN C 265     -41.063  52.807  21.907  1.00108.19           N  
+ANISOU 8770  ND2 ASN C 265    11663  17712  11733   1831   3197     87       N  
+ATOM   8771  N   TYR C 266     -36.940  52.058  21.131  1.00 71.81           N  
+ANISOU 8771  N   TYR C 266     7704  11920   7659   1618   2900    273       N  
+ATOM   8772  CA  TYR C 266     -36.522  51.563  19.822  1.00 66.67           C  
+ANISOU 8772  CA  TYR C 266     7192  10791   7351   1452   2860    361       C  
+ATOM   8773  C   TYR C 266     -37.673  51.423  18.822  1.00 66.17           C  
+ANISOU 8773  C   TYR C 266     7047  10670   7424   1370   2922    375       C  
+ATOM   8774  O   TYR C 266     -37.455  51.520  17.618  1.00 71.25           O  
+ANISOU 8774  O   TYR C 266     7808  10934   8330   1313   2866    313       O  
+ATOM   8775  CB  TYR C 266     -35.786  50.227  19.969  1.00 66.48           C  
+ANISOU 8775  CB  TYR C 266     7223  10631   7406   1251   2873    694       C  
+ATOM   8776  CG  TYR C 266     -34.400  50.374  20.562  1.00 66.21           C  
+ANISOU 8776  CG  TYR C 266     7312  10510   7334   1323   2773    653       C  
+ATOM   8777  CD1 TYR C 266     -33.375  50.969  19.836  1.00 63.97           C  
+ANISOU 8777  CD1 TYR C 266     7194   9857   7254   1366   2656    456       C  
+ATOM   8778  CD2 TYR C 266     -34.113  49.915  21.841  1.00 72.27           C  
+ANISOU 8778  CD2 TYR C 266     8024  11580   7855   1341   2794    816       C  
+ATOM   8779  CE1 TYR C 266     -32.106  51.110  20.369  1.00 65.80           C  
+ANISOU 8779  CE1 TYR C 266     7518  10029   7452   1425   2563    406       C  
+ATOM   8780  CE2 TYR C 266     -32.844  50.049  22.382  1.00 77.88           C  
+ANISOU 8780  CE2 TYR C 266     8836  12228   8527   1415   2692    770       C  
+ATOM   8781  CZ  TYR C 266     -31.847  50.648  21.642  1.00 76.01           C  
+ANISOU 8781  CZ  TYR C 266     8749  11627   8504   1456   2577    558       C  
+ATOM   8782  OH  TYR C 266     -30.585  50.785  22.175  1.00 78.01           O  
+ANISOU 8782  OH  TYR C 266     9083  11836   8720   1522   2474    501       O  
+ATOM   8783  N   ASN C 267     -38.891  51.200  19.308  1.00 78.21           N  
+ANISOU 8783  N   ASN C 267     8364  12589   8764   1361   3037    452       N  
+ATOM   8784  CA  ASN C 267     -40.034  51.066  18.406  1.00 83.39           C  
+ANISOU 8784  CA  ASN C 267     8916  13233   9534   1286   3093    457       C  
+ATOM   8785  C   ASN C 267     -40.248  52.332  17.584  1.00 72.42           C  
+ANISOU 8785  C   ASN C 267     7593  11675   8247   1479   3002    117       C  
+ATOM   8786  O   ASN C 267     -40.722  52.279  16.446  1.00 68.88           O  
+ANISOU 8786  O   ASN C 267     7160  11012   7998   1410   2991     98       O  
+ATOM   8787  CB  ASN C 267     -41.310  50.741  19.187  1.00 82.06           C  
+ANISOU 8787  CB  ASN C 267     8483  13582   9112   1263   3233    564       C  
+ATOM   8788  CG  ASN C 267     -41.393  49.284  19.590  1.00 91.65           C  
+ANISOU 8788  CG  ASN C 267     9633  14887  10302    990   3334    963       C  
+ATOM   8789  OD1 ASN C 267     -40.473  48.505  19.341  1.00 90.98           O  
+ANISOU 8789  OD1 ASN C 267     9706  14475  10387    842   3290   1153       O  
+ATOM   8790  ND2 ASN C 267     -42.508  48.904  20.204  1.00 95.35           N  
+ANISOU 8790  ND2 ASN C 267     9867  15800  10561    920   3467   1091       N  
+ATOM   8791  N   GLU C 268     -39.859  53.465  18.160  1.00 68.10           N  
+ANISOU 8791  N   GLU C 268     7100  11210   7566   1717   2924   -150       N  
+ATOM   8792  CA  GLU C 268     -39.955  54.747  17.478  1.00 66.46           C  
+ANISOU 8792  CA  GLU C 268     6988  10814   7448   1915   2814   -475       C  
+ATOM   8793  C   GLU C 268     -39.163  54.731  16.176  1.00 67.42           C  
+ANISOU 8793  C   GLU C 268     7329  10401   7886   1801   2723   -473       C  
+ATOM   8794  O   GLU C 268     -39.577  55.356  15.195  1.00 64.03           O  
+ANISOU 8794  O   GLU C 268     6955   9779   7594   1863   2665   -626       O  
+ATOM   8795  CB  GLU C 268     -39.477  55.877  18.394  1.00 67.59           C  
+ANISOU 8795  CB  GLU C 268     7180  11092   7408   2165   2731   -747       C  
+ATOM   8796  CG  GLU C 268     -40.376  56.070  19.607  1.00 70.72           C  
+ANISOU 8796  CG  GLU C 268     7348  12050   7473   2319   2816   -810       C  
+ATOM   8797  CD  GLU C 268     -40.142  57.385  20.325  1.00 82.15           C  
+ANISOU 8797  CD  GLU C 268     8838  13620   8757   2612   2715  -1158       C  
+ATOM   8798  OE1 GLU C 268     -39.054  57.974  20.163  1.00 85.88           O  
+ANISOU 8798  OE1 GLU C 268     9520  13768   9341   2656   2588  -1294       O  
+ATOM   8799  OE2 GLU C 268     -41.052  57.828  21.056  1.00 92.14           O  
+ANISOU 8799  OE2 GLU C 268     9917  15315   9778   2797   2762  -1305       O  
+ATOM   8800  N   ILE C 269     -38.050  53.993  16.162  1.00 74.61           N  
+ANISOU 8800  N   ILE C 269     8355  11090   8903   1640   2711   -297       N  
+ATOM   8801  CA  ILE C 269     -37.293  53.788  14.930  1.00 65.40           C  
+ANISOU 8801  CA  ILE C 269     7368   9454   8026   1504   2646   -267       C  
+ATOM   8802  C   ILE C 269     -38.254  53.363  13.836  1.00 65.91           C  
+ANISOU 8802  C   ILE C 269     7373   9430   8240   1394   2691   -192       C  
+ATOM   8803  O   ILE C 269     -38.403  54.052  12.820  1.00 77.09           O  
+ANISOU 8803  O   ILE C 269     8882  10616   9795   1446   2621   -352       O  
+ATOM   8804  CB  ILE C 269     -36.206  52.701  15.073  1.00 68.27           C  
+ANISOU 8804  CB  ILE C 269     7802   9658   8478   1322   2656    -32       C  
+ATOM   8805  CG1 ILE C 269     -35.181  53.079  16.143  1.00 76.39           C  
+ANISOU 8805  CG1 ILE C 269     8887  10777   9360   1427   2600   -104       C  
+ATOM   8806  CG2 ILE C 269     -35.538  52.432  13.727  1.00 58.03           C  
+ANISOU 8806  CG2 ILE C 269     6662   7913   7475   1183   2602    -11       C  
+ATOM   8807  CD1 ILE C 269     -34.237  54.150  15.717  1.00 72.68           C  
+ANISOU 8807  CD1 ILE C 269     8593  10030   8991   1520   2474   -356       C  
+ATOM   8808  N   THR C 270     -38.947  52.255  14.095  1.00 63.21           N  
+ANISOU 8808  N   THR C 270     6872   9292   7854   1243   2804     52       N  
+ATOM   8809  CA  THR C 270     -39.924  51.712  13.164  1.00 63.63           C  
+ANISOU 8809  CA  THR C 270     6836   9306   8034   1114   2855    141       C  
+ATOM   8810  C   THR C 270     -40.903  52.796  12.768  1.00 76.14           C  
+ANISOU 8810  C   THR C 270     8357  11001   9571   1304   2822   -106       C  
+ATOM   8811  O   THR C 270     -41.138  53.028  11.577  1.00 85.75           O  
+ANISOU 8811  O   THR C 270     9643  11974  10965   1286   2770   -182       O  
+ATOM   8812  CB  THR C 270     -40.694  50.528  13.773  1.00 66.03           C  
+ANISOU 8812  CB  THR C 270     6943   9907   8237    944   2986    415       C  
+ATOM   8813  OG1 THR C 270     -39.767  49.551  14.262  1.00 76.31           O  
+ANISOU 8813  OG1 THR C 270     8318  11110   9566    794   3001    651       O  
+ATOM   8814  CG2 THR C 270     -41.607  49.894  12.735  1.00 61.47           C  
+ANISOU 8814  CG2 THR C 270     6283   9251   7822    779   3028    507       C  
+ATOM   8815  N   GLU C 271     -41.405  53.504  13.776  1.00 62.43           N  
+ANISOU 8815  N   GLU C 271     6501   9628   7590   1504   2840   -246       N  
+ATOM   8816  CA  GLU C 271     -42.418  54.518  13.558  1.00 76.39           C  
+ANISOU 8816  CA  GLU C 271     8183  11556   9287   1719   2807   -490       C  
+ATOM   8817  C   GLU C 271     -41.867  55.535  12.579  1.00 70.19           C  
+ANISOU 8817  C   GLU C 271     7627  10365   8676   1833   2659   -706       C  
+ATOM   8818  O   GLU C 271     -42.492  55.822  11.552  1.00 80.32           O  
+ANISOU 8818  O   GLU C 271     8920  11519  10079   1856   2617   -781       O  
+ATOM   8819  CB  GLU C 271     -42.806  55.176  14.888  1.00 82.63           C  
+ANISOU 8819  CB  GLU C 271     8835  12782   9781   1942   2834   -639       C  
+ATOM   8820  CG  GLU C 271     -43.926  56.195  14.802  1.00 85.91           C  
+ANISOU 8820  CG  GLU C 271     9129  13415  10096   2197   2800   -906       C  
+ATOM   8821  CD  GLU C 271     -44.265  56.796  16.157  1.00 98.14           C  
+ANISOU 8821  CD  GLU C 271    10532  15416  11340   2424   2829  -1067       C  
+ATOM   8822  OE1 GLU C 271     -43.705  56.334  17.176  1.00102.31           O  
+ANISOU 8822  OE1 GLU C 271    11036  16120  11719   2359   2890   -941       O  
+ATOM   8823  OE2 GLU C 271     -45.078  57.743  16.202  1.00 95.04           O  
+ANISOU 8823  OE2 GLU C 271    10052  15207  10854   2679   2783  -1329       O  
+ATOM   8824  N   ILE C 272     -40.650  55.998  12.853  1.00 62.98           N  
+ANISOU 8824  N   ILE C 272     6903   9242   7784   1875   2580   -782       N  
+ATOM   8825  CA  ILE C 272     -40.000  56.973  11.989  1.00 67.70           C  
+ANISOU 8825  CA  ILE C 272     7735   9449   8540   1952   2440   -970       C  
+ATOM   8826  C   ILE C 272     -39.926  56.429  10.573  1.00 57.54           C  
+ANISOU 8826  C   ILE C 272     6535   7829   7497   1761   2432   -850       C  
+ATOM   8827  O   ILE C 272     -40.361  57.089   9.621  1.00 70.04           O  
+ANISOU 8827  O   ILE C 272     8190   9247   9176   1836   2356   -977       O  
+ATOM   8828  CB  ILE C 272     -38.586  57.329  12.487  1.00 72.95           C  
+ANISOU 8828  CB  ILE C 272     8573   9938   9207   1959   2372  -1027       C  
+ATOM   8829  CG1 ILE C 272     -38.669  58.155  13.773  1.00 63.50           C  
+ANISOU 8829  CG1 ILE C 272     7319   9037   7770   2191   2345  -1221       C  
+ATOM   8830  CG2 ILE C 272     -37.820  58.097  11.420  1.00 69.58           C  
+ANISOU 8830  CG2 ILE C 272     8391   9067   8979   1950   2246  -1155       C  
+ATOM   8831  CD1 ILE C 272     -37.379  58.190  14.558  1.00 68.87           C  
+ANISOU 8831  CD1 ILE C 272     8099   9668   8402   2170   2309  -1227       C  
+ATOM   8832  N   LEU C 273     -39.446  55.194  10.452  1.00 60.71           N  
+ANISOU 8832  N   LEU C 273     6922   8153   7991   1524   2506   -605       N  
+ATOM   8833  CA  LEU C 273     -39.294  54.578   9.144  1.00 72.02           C  
+ANISOU 8833  CA  LEU C 273     8434   9278   9651   1336   2500   -497       C  
+ATOM   8834  C   LEU C 273     -40.640  54.555   8.449  1.00 62.60           C  
+ANISOU 8834  C   LEU C 273     7114   8194   8478   1353   2521   -514       C  
+ATOM   8835  O   LEU C 273     -40.747  54.943   7.279  1.00 69.25           O  
+ANISOU 8835  O   LEU C 273     8060   8795   9458   1354   2450   -592       O  
+ATOM   8836  CB  LEU C 273     -38.720  53.165   9.261  1.00 60.88           C  
+ANISOU 8836  CB  LEU C 273     6998   7812   8320   1100   2577   -235       C  
+ATOM   8837  CG  LEU C 273     -37.268  53.081   9.733  1.00 64.15           C  
+ANISOU 8837  CG  LEU C 273     7549   8072   8755   1067   2542   -210       C  
+ATOM   8838  CD1 LEU C 273     -36.800  51.636   9.788  1.00 61.41           C  
+ANISOU 8838  CD1 LEU C 273     7176   7659   8498    854   2605     50       C  
+ATOM   8839  CD2 LEU C 273     -36.372  53.903   8.822  1.00 52.24           C  
+ANISOU 8839  CD2 LEU C 273     6251   6209   7388   1090   2434   -372       C  
+ATOM   8840  N   GLN C 274     -41.671  54.164   9.197  1.00 62.46           N  
+ANISOU 8840  N   GLN C 274     6865   8561   8305   1375   2614   -450       N  
+ATOM   8841  CA  GLN C 274     -43.012  54.081   8.642  1.00 70.28           C  
+ANISOU 8841  CA  GLN C 274     7692   9715   9297   1387   2642   -466       C  
+ATOM   8842  C   GLN C 274     -43.372  55.417   8.018  1.00 68.59           C  
+ANISOU 8842  C   GLN C 274     7566   9402   9093   1622   2520   -728       C  
+ATOM   8843  O   GLN C 274     -43.759  55.477   6.844  1.00 74.67           O  
+ANISOU 8843  O   GLN C 274     8377   9994   9998   1590   2469   -752       O  
+ATOM   8844  CB  GLN C 274     -44.028  53.684   9.716  1.00 60.31           C  
+ANISOU 8844  CB  GLN C 274     6153   8938   7822   1407   2759   -398       C  
+ATOM   8845  CG  GLN C 274     -44.176  52.180   9.892  1.00 68.87           C  
+ANISOU 8845  CG  GLN C 274     7116  10110   8943   1121   2881    -98       C  
+ATOM   8846  CD  GLN C 274     -44.813  51.796  11.213  1.00 84.80           C  
+ANISOU 8846  CD  GLN C 274     8901  12601  10718   1117   3003      4       C  
+ATOM   8847  OE1 GLN C 274     -45.158  52.654  12.024  1.00103.33           O  
+ANISOU 8847  OE1 GLN C 274    11163  15242  12857   1344   3001   -166       O  
+ATOM   8848  NE2 GLN C 274     -44.973  50.496  11.435  1.00 77.75           N  
+ANISOU 8848  NE2 GLN C 274     7909  11785   9848    857   3105    284       N  
+ATOM   8849  N   ARG C 275     -43.149  56.489   8.776  1.00 58.73           N  
+ANISOU 8849  N   ARG C 275     6371   8234   7709   1855   2458   -923       N  
+ATOM   8850  CA  ARG C 275     -43.500  57.821   8.310  1.00 59.18           C  
+ANISOU 8850  CA  ARG C 275     6527   8193   7768   2104   2325  -1178       C  
+ATOM   8851  C   ARG C 275     -42.817  58.095   6.985  1.00 73.46           C  
+ANISOU 8851  C   ARG C 275     8583   9536   9791   2020   2222  -1185       C  
+ATOM   8852  O   ARG C 275     -43.468  58.507   6.019  1.00 87.61           O  
+ANISOU 8852  O   ARG C 275    10402  11232  11655   2087   2151  -1260       O  
+ATOM   8853  CB  ARG C 275     -43.108  58.885   9.337  1.00 60.40           C  
+ANISOU 8853  CB  ARG C 275     6746   8433   7771   2341   2259  -1386       C  
+ATOM   8854  CG  ARG C 275     -43.944  58.877  10.604  1.00 69.81           C  
+ANISOU 8854  CG  ARG C 275     7683  10127   8714   2489   2344  -1443       C  
+ATOM   8855  CD  ARG C 275     -45.236  59.652  10.401  1.00 67.65           C  
+ANISOU 8855  CD  ARG C 275     7281  10057   8366   2741   2292  -1648       C  
+ATOM   8856  NE  ARG C 275     -44.981  61.034  10.003  1.00 73.47           N  
+ANISOU 8856  NE  ARG C 275     8241  10517   9159   2979   2112  -1906       N  
+ATOM   8857  CZ  ARG C 275     -44.759  62.029  10.856  1.00 87.93           C  
+ANISOU 8857  CZ  ARG C 275    10128  12418  10863   3222   2034  -2135       C  
+ATOM   8858  NH1 ARG C 275     -44.763  61.798  12.162  1.00 90.34           N  
+ANISOU 8858  NH1 ARG C 275    10272  13093  10960   3267   2127  -2144       N  
+ATOM   8859  NH2 ARG C 275     -44.534  63.256  10.406  1.00 89.88           N  
+ANISOU 8859  NH2 ARG C 275    10599  12364  11187   3417   1858  -2355       N  
+ATOM   8860  N   ILE C 276     -41.523  57.794   6.923  1.00 64.98           N  
+ANISOU 8860  N   ILE C 276     7676   8200   8812   1862   2220  -1096       N  
+ATOM   8861  CA  ILE C 276     -40.764  58.064   5.714  1.00 57.02           C  
+ANISOU 8861  CA  ILE C 276     6900   6775   7989   1768   2133  -1103       C  
+ATOM   8862  C   ILE C 276     -41.403  57.333   4.547  1.00 64.47           C  
+ANISOU 8862  C   ILE C 276     7784   7654   9056   1623   2162   -986       C  
+ATOM   8863  O   ILE C 276     -41.688  57.945   3.510  1.00 67.85           O  
+ANISOU 8863  O   ILE C 276     8320   7900   9560   1681   2068  -1071       O  
+ATOM   8864  CB  ILE C 276     -39.288  57.652   5.852  1.00 65.36           C  
+ANISOU 8864  CB  ILE C 276     8095   7614   9125   1596   2147  -1009       C  
+ATOM   8865  CG1 ILE C 276     -38.577  58.569   6.849  1.00 65.10           C  
+ANISOU 8865  CG1 ILE C 276     8154   7597   8985   1745   2087  -1162       C  
+ATOM   8866  CG2 ILE C 276     -38.590  57.719   4.505  1.00 65.95           C  
+ANISOU 8866  CG2 ILE C 276     8366   7305   9385   1458   2086   -988       C  
+ATOM   8867  CD1 ILE C 276     -37.198  58.090   7.246  1.00 64.74           C  
+ANISOU 8867  CD1 ILE C 276     8188   7430   8980   1595   2111  -1073       C  
+ATOM   8868  N   GLU C 277     -41.703  56.050   4.748  1.00 68.72           N  
+ANISOU 8868  N   GLU C 277     8148   8357   9604   1445   2283   -796       N  
+ATOM   8869  CA  GLU C 277     -42.279  55.255   3.672  1.00 71.66           C  
+ANISOU 8869  CA  GLU C 277     8457   8669  10101   1286   2311   -689       C  
+ATOM   8870  C   GLU C 277     -43.566  55.911   3.215  1.00 75.71           C  
+ANISOU 8870  C   GLU C 277     8875   9326  10563   1458   2255   -820       C  
+ATOM   8871  O   GLU C 277     -43.798  56.070   2.011  1.00 87.19           O  
+ANISOU 8871  O   GLU C 277    10408  10597  12124   1436   2187   -849       O  
+ATOM   8872  CB  GLU C 277     -42.546  53.814   4.111  1.00 69.50           C  
+ANISOU 8872  CB  GLU C 277     7997   8576   9835   1078   2443   -472       C  
+ATOM   8873  CG  GLU C 277     -43.191  52.969   3.018  1.00 70.76           C  
+ANISOU 8873  CG  GLU C 277     8081   8676  10128    906   2465   -378       C  
+ATOM   8874  CD  GLU C 277     -43.395  51.523   3.424  1.00 82.65           C  
+ANISOU 8874  CD  GLU C 277     9429  10310  11663    678   2583   -156       C  
+ATOM   8875  OE1 GLU C 277     -43.337  51.228   4.636  1.00 95.50           O  
+ANISOU 8875  OE1 GLU C 277    10962  12156  13169    677   2657    -70       O  
+ATOM   8876  OE2 GLU C 277     -43.619  50.681   2.528  1.00 85.55           O  
+ANISOU 8876  OE2 GLU C 277     9774  10557  12174    496   2595    -67       O  
+ATOM   8877  N   ASN C 278     -44.371  56.337   4.186  1.00 69.62           N  
+ANISOU 8877  N   ASN C 278     7937   8895   9619   1644   2278   -913       N  
+ATOM   8878  CA  ASN C 278     -45.631  56.987   3.881  1.00 82.61           C  
+ANISOU 8878  CA  ASN C 278     9464  10724  11200   1844   2222  -1059       C  
+ATOM   8879  C   ASN C 278     -45.362  58.160   2.955  1.00 86.66           C  
+ANISOU 8879  C   ASN C 278    10221  10919  11788   1999   2057  -1219       C  
+ATOM   8880  O   ASN C 278     -45.898  58.219   1.842  1.00 83.45           O  
+ANISOU 8880  O   ASN C 278     9833  10412  11464   1994   1995  -1232       O  
+ATOM   8881  CB  ASN C 278     -46.333  57.445   5.161  1.00 79.52           C  
+ANISOU 8881  CB  ASN C 278     8881  10738  10594   2059   2259  -1176       C  
+ATOM   8882  CG  ASN C 278     -47.772  57.854   4.925  1.00 92.62           C  
+ANISOU 8882  CG  ASN C 278    10342  12670  12177   2246   2227  -1309       C  
+ATOM   8883  OD1 ASN C 278     -48.616  57.024   4.589  1.00 94.45           O  
+ANISOU 8883  OD1 ASN C 278    10369  13092  12428   2112   2303  -1204       O  
+ATOM   8884  ND2 ASN C 278     -48.060  59.137   5.104  1.00101.69           N  
+ANISOU 8884  ND2 ASN C 278    11551  13843  13244   2561   2107  -1549       N  
+ATOM   8885  N   ASN C 279     -44.458  59.038   3.391  1.00 72.08           N  
+ANISOU 8885  N   ASN C 279     8573   8896   9917   2110   1984  -1325       N  
+ATOM   8886  CA  ASN C 279     -44.129  60.250   2.650  1.00 61.01           C  
+ANISOU 8886  CA  ASN C 279     7428   7177   8577   2254   1820  -1472       C  
+ATOM   8887  C   ASN C 279     -43.762  59.942   1.207  1.00 75.13           C  
+ANISOU 8887  C   ASN C 279     9367   8649  10531   2068   1782  -1369       C  
+ATOM   8888  O   ASN C 279     -44.025  60.737   0.305  1.00 91.95           O  
+ANISOU 8888  O   ASN C 279    11637  10596  12702   2177   1654  -1455       O  
+ATOM   8889  CB  ASN C 279     -42.983  61.001   3.331  1.00 70.42           C  
+ANISOU 8889  CB  ASN C 279     8817   8194   9746   2310   1766  -1561       C  
+ATOM   8890  CG  ASN C 279     -43.412  61.680   4.616  1.00 84.09           C  
+ANISOU 8890  CG  ASN C 279    10444  10203  11302   2568   1752  -1735       C  
+ATOM   8891  OD1 ASN C 279     -44.603  61.804   4.900  1.00100.92           O  
+ANISOU 8891  OD1 ASN C 279    12378  12640  13329   2745   1760  -1821       O  
+ATOM   8892  ND2 ASN C 279     -42.438  62.127   5.402  1.00 80.24           N  
+ANISOU 8892  ND2 ASN C 279    10079   9631  10776   2593   1729  -1802       N  
+ATOM   8893  N   ILE C 280     -43.156  58.779   0.996  1.00 74.50           N  
+ANISOU 8893  N   ILE C 280     9260   8509  10539   1793   1889  -1185       N  
+ATOM   8894  CA  ILE C 280     -42.772  58.368  -0.343  1.00 74.88           C  
+ANISOU 8894  CA  ILE C 280     9429   8288  10733   1606   1868  -1093       C  
+ATOM   8895  C   ILE C 280     -43.959  57.769  -1.082  1.00 79.01           C  
+ANISOU 8895  C   ILE C 280     9779   8963  11280   1571   1886  -1050       C  
+ATOM   8896  O   ILE C 280     -44.286  58.191  -2.194  1.00 90.07           O  
+ANISOU 8896  O   ILE C 280    11273  10222  12728   1610   1790  -1093       O  
+ATOM   8897  CB  ILE C 280     -41.613  57.367  -0.316  1.00 72.26           C  
+ANISOU 8897  CB  ILE C 280     9141   7819  10495   1344   1962   -940       C  
+ATOM   8898  CG1 ILE C 280     -40.408  58.003   0.377  1.00 72.97           C  
+ANISOU 8898  CG1 ILE C 280     9396   7767  10562   1377   1933   -996       C  
+ATOM   8899  CG2 ILE C 280     -41.243  56.944  -1.732  1.00 61.66           C  
+ANISOU 8899  CG2 ILE C 280     7911   6225   9293   1163   1941   -868       C  
+ATOM   8900  CD1 ILE C 280     -39.096  57.358   0.036  1.00 76.78           C  
+ANISOU 8900  CD1 ILE C 280     9989   8026  11157   1149   1975   -889       C  
+ATOM   8901  N   LYS C 281     -44.627  56.813  -0.445  1.00 84.21           N  
+ANISOU 8901  N   LYS C 281    10181   9921  11895   1498   2004   -964       N  
+ATOM   8902  CA  LYS C 281     -45.596  55.986  -1.152  1.00 80.81           C  
+ANISOU 8902  CA  LYS C 281     9573   9620  11512   1388   2041   -894       C  
+ATOM   8903  C   LYS C 281     -46.797  56.810  -1.592  1.00 89.12           C  
+ANISOU 8903  C   LYS C 281    10553  10812  12499   1617   1939  -1042       C  
+ATOM   8904  O   LYS C 281     -47.445  56.498  -2.588  1.00 85.91           O  
+ANISOU 8904  O   LYS C 281    10089  10405  12150   1562   1907  -1028       O  
+ATOM   8905  CB  LYS C 281     -46.050  54.821  -0.268  1.00 75.37           C  
+ANISOU 8905  CB  LYS C 281     8626   9227  10784   1244   2189   -761       C  
+ATOM   8906  N   THR C 282     -47.059  57.892  -0.870  1.00 94.49           N  
+ANISOU 8906  N   THR C 282    11244  11600  13058   1888   1876  -1196       N  
+ATOM   8907  CA  THR C 282     -48.183  58.766  -1.177  1.00 92.14           C  
+ANISOU 8907  CA  THR C 282    10879  11440  12690   2155   1763  -1360       C  
+ATOM   8908  C   THR C 282     -47.885  59.779  -2.284  1.00 89.53           C  
+ANISOU 8908  C   THR C 282    10829  10765  12424   2270   1588  -1442       C  
+ATOM   8909  O   THR C 282     -48.743  60.599  -2.618  1.00 87.16           O  
+ANISOU 8909  O   THR C 282    10516  10527  12074   2515   1464  -1579       O  
+ATOM   8910  CB  THR C 282     -48.632  59.529   0.082  1.00 93.85           C  
+ANISOU 8910  CB  THR C 282    10986  11927  12745   2426   1756  -1516       C  
+ATOM   8911  OG1 THR C 282     -47.530  60.287   0.595  1.00 95.80           O  
+ANISOU 8911  OG1 THR C 282    11474  11942  12986   2497   1706  -1576       O  
+ATOM   8912  CG2 THR C 282     -49.109  58.559   1.151  1.00 93.59           C  
+ANISOU 8912  CG2 THR C 282    10649  12295  12617   2320   1930  -1428       C  
+ATOM   8913  N   LYS C 283     -46.684  59.727  -2.858  1.00 89.96           N  
+ANISOU 8913  N   LYS C 283    11133  10466  12582   2096   1574  -1356       N  
+ATOM   8914  CA  LYS C 283     -46.317  60.690  -3.897  1.00 86.34           C  
+ANISOU 8914  CA  LYS C 283    10957   9676  12173   2173   1416  -1409       C  
+ATOM   8915  C   LYS C 283     -46.442  60.113  -5.304  1.00 83.67           C  
+ANISOU 8915  C   LYS C 283    10650   9218  11924   2000   1399  -1311       C  
+ATOM   8916  O   LYS C 283     -46.265  60.821  -6.298  1.00 80.74           O  
+ANISOU 8916  O   LYS C 283    10496   8603  11579   2047   1270  -1332       O  
+ATOM   8917  CB  LYS C 283     -44.892  61.202  -3.683  1.00 87.53           C  
+ANISOU 8917  CB  LYS C 283    11377   9516  12363   2103   1396  -1398       C  
+ATOM   8918  CG  LYS C 283     -44.858  62.561  -3.000  1.00 93.36           C  
+ANISOU 8918  CG  LYS C 283    12250  10195  13028   2378   1275  -1568       C  
+ATOM   8919  CD  LYS C 283     -44.705  63.712  -3.979  1.00 99.39           C  
+ANISOU 8919  CD  LYS C 283    13303  10633  13828   2488   1089  -1627       C  
+ATOM   8920  CE  LYS C 283     -45.207  65.012  -3.340  1.00105.06           C  
+ANISOU 8920  CE  LYS C 283    14088  11363  14467   2833    944  -1828       C  
+ATOM   8921  NZ  LYS C 283     -45.356  66.138  -4.310  1.00102.20           N  
+ANISOU 8921  NZ  LYS C 283    13990  10709  14134   2982    739  -1883       N  
+ATOM   8922  N   THR C 284     -46.738  58.821  -5.384  1.00 84.70           N  
+ANISOU 8922  N   THR C 284    10569   9517  12096   1794   1525  -1203       N  
+ATOM   8923  CA  THR C 284     -47.070  58.196  -6.657  1.00 83.42           C  
+ANISOU 8923  CA  THR C 284    10384   9305  12006   1648   1509  -1138       C  
+ATOM   8924  C   THR C 284     -48.536  57.795  -6.615  1.00 85.78           C  
+ANISOU 8924  C   THR C 284    10386   9951  12257   1725   1520  -1179       C  
+ATOM   8925  O   THR C 284     -48.938  56.944  -5.820  1.00 81.64           O  
+ANISOU 8925  O   THR C 284     9617   9684  11716   1633   1647  -1129       O  
+ATOM   8926  CB  THR C 284     -46.192  56.971  -6.947  1.00 79.52           C  
+ANISOU 8926  CB  THR C 284     9900   8691  11623   1327   1628   -992       C  
+ATOM   8927  OG1 THR C 284     -44.835  57.390  -7.136  1.00 79.75           O  
+ANISOU 8927  OG1 THR C 284    10197   8410  11694   1257   1609   -968       O  
+ATOM   8928  CG2 THR C 284     -46.673  56.259  -8.200  1.00 75.06           C  
+ANISOU 8928  CG2 THR C 284     9276   8119  11123   1187   1612   -951       C  
+ATOM   8929  N   VAL C 285     -49.331  58.417  -7.476  1.00 83.67           N  
+ANISOU 8929  N   VAL C 285    10136   9695  11959   1890   1383  -1264       N  
+ATOM   8930  CA  VAL C 285     -50.778  58.256  -7.446  1.00 77.62           C  
+ANISOU 8930  CA  VAL C 285     9083   9277  11132   2013   1366  -1338       C  
+ATOM   8931  C   VAL C 285     -51.307  57.370  -8.570  1.00 79.63           C  
+ANISOU 8931  C   VAL C 285     9225   9577  11452   1833   1367  -1280       C  
+ATOM   8932  O   VAL C 285     -50.863  57.464  -9.713  1.00 82.32           O  
+ANISOU 8932  O   VAL C 285     9763   9668  11845   1761   1288  -1248       O  
+ATOM   8933  CB  VAL C 285     -51.477  59.628  -7.521  1.00 77.10           C  
+ANISOU 8933  CB  VAL C 285     9078   9245  10973   2382   1191  -1505       C  
+ATOM   8934  CG1 VAL C 285     -52.977  59.479  -7.342  1.00 76.33           C  
+ANISOU 8934  CG1 VAL C 285     8644   9558  10799   2532   1181  -1603       C  
+ATOM   8935  CG2 VAL C 285     -50.906  60.562  -6.465  1.00 77.44           C  
+ANISOU 8935  CG2 VAL C 285     9258   9207  10960   2565   1171  -1585       C  
+ATOM   8936  N   PHE C 286     -52.257  56.507  -8.227  1.00 83.84           N  
+ANISOU 8936  N   PHE C 286     9437  10444  11976   1752   1456  -1270       N  
+ATOM   8937  CA  PHE C 286     -52.978  55.706  -9.205  1.00 85.39           C  
+ANISOU 8937  CA  PHE C 286     9479  10740  12225   1605   1444  -1248       C  
+ATOM   8938  C   PHE C 286     -54.314  56.364  -9.533  1.00 87.53           C  
+ANISOU 8938  C   PHE C 286     9585  11269  12404   1868   1316  -1393       C  
+ATOM   8939  O   PHE C 286     -55.150  56.552  -8.651  1.00 81.05           O  
+ANISOU 8939  O   PHE C 286     8526  10774  11495   2020   1347  -1473       O  
+ATOM   8940  CB  PHE C 286     -53.196  54.288  -8.673  1.00 78.09           C  
+ANISOU 8940  CB  PHE C 286     8302  10009  11361   1319   1614  -1139       C  
+ATOM   8941  CG  PHE C 286     -54.070  53.438  -9.546  1.00 79.10           C  
+ANISOU 8941  CG  PHE C 286     8230  10280  11543   1163   1602  -1136       C  
+ATOM   8942  CD1 PHE C 286     -53.624  52.999 -10.780  1.00 81.24           C  
+ANISOU 8942  CD1 PHE C 286     8648  10307  11911   1000   1552  -1100       C  
+ATOM   8943  CD2 PHE C 286     -55.338  53.070  -9.127  1.00 80.75           C  
+ANISOU 8943  CD2 PHE C 286     8093  10888  11700   1172   1643  -1178       C  
+ATOM   8944  CE1 PHE C 286     -54.428  52.215 -11.581  1.00 79.54           C  
+ANISOU 8944  CE1 PHE C 286     8250  10228  11745    857   1532  -1115       C  
+ATOM   8945  CE2 PHE C 286     -56.144  52.284  -9.925  1.00 81.21           C  
+ANISOU 8945  CE2 PHE C 286     7960  11083  11814   1015   1626  -1185       C  
+ATOM   8946  CZ  PHE C 286     -55.690  51.857 -11.154  1.00 78.57           C  
+ANISOU 8946  CZ  PHE C 286     7785  10487  11582    859   1566  -1157       C  
+ATOM   8947  N   LEU C 287     -54.516  56.711 -10.800  1.00 88.57           N  
+ANISOU 8947  N   LEU C 287     9835  11272  12547   1928   1171  -1430       N  
+ATOM   8948  CA  LEU C 287     -55.771  57.322 -11.227  1.00 78.67           C  
+ANISOU 8948  CA  LEU C 287     8433  10250  11209   2188   1027  -1568       C  
+ATOM   8949  C   LEU C 287     -56.714  56.289 -11.824  1.00 77.83           C  
+ANISOU 8949  C   LEU C 287     8037  10399  11136   2013   1055  -1565       C  
+ATOM   8950  O   LEU C 287     -56.525  55.834 -12.952  1.00 76.30           O  
+ANISOU 8950  O   LEU C 287     7931  10055  11005   1853   1010  -1520       O  
+ATOM   8951  CB  LEU C 287     -55.521  58.443 -12.239  1.00 71.27           C  
+ANISOU 8951  CB  LEU C 287     7804   9035  10242   2397    823  -1613       C  
+ATOM   8952  CG  LEU C 287     -54.834  59.710 -11.730  1.00 73.35           C  
+ANISOU 8952  CG  LEU C 287     8350   9058  10462   2630    744  -1653       C  
+ATOM   8953  CD1 LEU C 287     -54.721  60.732 -12.849  1.00 72.58           C  
+ANISOU 8953  CD1 LEU C 287     8545   8694  10336   2808    531  -1675       C  
+ATOM   8954  CD2 LEU C 287     -55.594  60.292 -10.548  1.00 76.45           C  
+ANISOU 8954  CD2 LEU C 287     8547   9735  10764   2912    741  -1793       C  
+ATOM   8955  N   SER C 288     -57.733  55.924 -11.055  1.00 82.44           N  
+ANISOU 8955  N   SER C 288     8268  11385  11672   2038   1130  -1621       N  
+ATOM   8956  CA  SER C 288     -58.711  54.942 -11.495  1.00 83.13           C  
+ANISOU 8956  CA  SER C 288     8043  11753  11791   1859   1162  -1627       C  
+ATOM   8957  C   SER C 288     -59.947  55.629 -12.049  1.00 87.85           C  
+ANISOU 8957  C   SER C 288     8477  12608  12295   2145    995  -1792       C  
+ATOM   8958  O   SER C 288     -60.463  56.569 -11.447  1.00105.37           O  
+ANISOU 8958  O   SER C 288    10627  15002  14407   2468    931  -1916       O  
+ATOM   8959  CB  SER C 288     -59.102  54.019 -10.342  1.00 91.55           C  
+ANISOU 8959  CB  SER C 288     8798  13128  12859   1664   1356  -1568       C  
+ATOM   8960  OG  SER C 288     -60.150  53.145 -10.722  1.00 99.66           O  
+ANISOU 8960  OG  SER C 288     9501  14452  13912   1495   1379  -1585       O  
+ATOM   8961  N   GLY C 289     -60.420  55.162 -13.199  1.00 85.46           N  
+ANISOU 8961  N   GLY C 289     8107  12332  12031   2040    914  -1807       N  
+ATOM   8962  CA  GLY C 289     -61.654  55.678 -13.755  1.00 85.42           C  
+ANISOU 8962  CA  GLY C 289     7910  12607  11940   2291    753  -1963       C  
+ATOM   8963  C   GLY C 289     -61.798  55.559 -15.257  1.00 84.15           C  
+ANISOU 8963  C   GLY C 289     7843  12326  11803   2249    603  -1977       C  
+ATOM   8964  O   GLY C 289     -60.829  55.666 -16.009  1.00 82.01           O  
+ANISOU 8964  O   GLY C 289     7906  11679  11575   2170    558  -1893       O  
+ATOM   8965  N   SER C 290     -63.034  55.330 -15.682  1.00 86.00           N  
+ANISOU 8965  N   SER C 290     7765  12912  11999   2299    529  -2089       N  
+ATOM   8966  CA  SER C 290     -63.409  55.319 -17.088  1.00 87.45           C  
+ANISOU 8966  CA  SER C 290     7987  13068  12173   2317    359  -2136       C  
+ATOM   8967  C   SER C 290     -64.775  55.978 -17.194  1.00 96.19           C  
+ANISOU 8967  C   SER C 290     8825  14558  13164   2651    202  -2316       C  
+ATOM   8968  O   SER C 290     -65.541  55.964 -16.234  1.00 99.35           O  
+ANISOU 8968  O   SER C 290     8909  15317  13522   2735    276  -2398       O  
+ATOM   8969  CB  SER C 290     -63.441  53.897 -17.646  1.00 87.08           C  
+ANISOU 8969  CB  SER C 290     7794  13055  12236   1903    452  -2078       C  
+ATOM   8970  OG  SER C 290     -64.320  53.077 -16.896  1.00 88.32           O  
+ANISOU 8970  OG  SER C 290     7538  13599  12419   1741    581  -2110       O  
+ATOM   8971  N   ALA C 291     -65.092  56.561 -18.343  1.00 89.65           N  
+ANISOU 8971  N   ALA C 291     8112  13675  12275   2850    -17  -2380       N  
+ATOM   8972  CA  ALA C 291     -66.373  57.245 -18.464  1.00 88.36           C  
+ANISOU 8972  CA  ALA C 291     7704  13868  12000   3206   -189  -2560       C  
+ATOM   8973  C   ALA C 291     -66.899  57.331 -19.888  1.00 97.87           C  
+ANISOU 8973  C   ALA C 291     8924  15106  13158   3283   -402  -2617       C  
+ATOM   8974  O   ALA C 291     -66.158  57.607 -20.829  1.00 97.74           O  
+ANISOU 8974  O   ALA C 291     9264  14737  13137   3269   -503  -2529       O  
+ATOM   8975  CB  ALA C 291     -66.266  58.645 -17.872  1.00 99.37           C  
+ANISOU 8975  CB  ALA C 291     9284  15162  13310   3636   -297  -2623       C  
+ATOM   8976  N   VAL C 292     -68.198  57.086 -20.022  1.00108.01           N  
+ANISOU 8976  N   VAL C 292     9803  16840  14394   3361   -467  -2767       N  
+ATOM   8977  CA  VAL C 292     -68.922  57.375 -21.249  1.00103.73           C  
+ANISOU 8977  CA  VAL C 292     9225  16413  13775   3538   -705  -2863       C  
+ATOM   8978  C   VAL C 292     -69.787  58.587 -20.959  1.00110.60           C  
+ANISOU 8978  C   VAL C 292     9998  17502  14523   4050   -892  -3023       C  
+ATOM   8979  O   VAL C 292     -69.980  59.456 -21.806  1.00125.06           O  
+ANISOU 8979  O   VAL C 292    12017  19233  16267   4360  -1139  -3064       O  
+ATOM   8980  CB  VAL C 292     -69.784  56.187 -21.711  1.00 96.66           C  
+ANISOU 8980  CB  VAL C 292     7931  15878  12919   3251   -666  -2934       C  
+ATOM   8981  N   GLU C 293     -70.292  58.636 -19.733  1.00103.51           N  
+ANISOU 8981  N   GLU C 293     8810  16905  13615   4140   -772  -3113       N  
+ATOM   8982  CA  GLU C 293     -71.027  59.790 -19.239  1.00103.72           C  
+ANISOU 8982  CA  GLU C 293     8738  17138  13533   4639   -922  -3284       C  
+ATOM   8983  C   GLU C 293     -70.236  60.376 -18.074  1.00 97.46           C  
+ANISOU 8983  C   GLU C 293     8156  16121  12754   4740   -807  -3236       C  
+ATOM   8984  O   GLU C 293     -69.457  59.671 -17.430  1.00113.08           O  
+ANISOU 8984  O   GLU C 293    10182  17968  14816   4397   -572  -3102       O  
+ATOM   8985  CB  GLU C 293     -72.441  59.413 -18.804  1.00114.75           C  
+ANISOU 8985  CB  GLU C 293     9557  19166  14876   4704   -896  -3477       C  
+ATOM   8986  N   TYR C 294     -70.412  61.669 -17.825  1.00106.26           N  
+ANISOU 8986  N   TYR C 294     9411  17176  13789   5215   -985  -3348       N  
+ATOM   8987  CA  TYR C 294     -69.671  62.369 -16.778  1.00107.37           C  
+ANISOU 8987  CA  TYR C 294     9778  17082  13935   5356   -915  -3330       C  
+ATOM   8988  C   TYR C 294     -70.648  63.035 -15.822  1.00111.85           C  
+ANISOU 8988  C   TYR C 294    10033  18058  14408   5759   -958  -3564       C  
+ATOM   8989  O   TYR C 294     -70.726  64.264 -15.767  1.00104.30           O  
+ANISOU 8989  O   TYR C 294     9283  16953  13393   6192  -1161  -3667       O  
+ATOM   8990  CB  TYR C 294     -68.737  63.424 -17.371  1.00104.02           C  
+ANISOU 8990  CB  TYR C 294     9914  16094  13517   5551  -1102  -3236       C  
+ATOM   8991  CG  TYR C 294     -67.641  62.897 -18.270  1.00106.53           C  
+ANISOU 8991  CG  TYR C 294    10575  15991  13911   5178  -1056  -3008       C  
+ATOM   8992  CD1 TYR C 294     -66.419  62.496 -17.746  1.00 95.76           C  
+ANISOU 8992  CD1 TYR C 294     9429  14322  12634   4864   -850  -2846       C  
+ATOM   8993  CD2 TYR C 294     -67.815  62.837 -19.645  1.00113.78           C  
+ANISOU 8993  CD2 TYR C 294    11600  16829  14804   5159  -1226  -2964       C  
+ATOM   8994  CE1 TYR C 294     -65.409  62.029 -18.564  1.00104.83           C  
+ANISOU 8994  CE1 TYR C 294    10876  15108  13846   4541   -808  -2657       C  
+ATOM   8995  CE2 TYR C 294     -66.810  62.371 -20.474  1.00110.34           C  
+ANISOU 8995  CE2 TYR C 294    11468  16035  14421   4829  -1181  -2772       C  
+ATOM   8996  CZ  TYR C 294     -65.609  61.969 -19.927  1.00106.36           C  
+ANISOU 8996  CZ  TYR C 294    11163  15242  14008   4524   -970  -2624       C  
+ATOM   8997  OH  TYR C 294     -64.607  61.506 -20.745  1.00107.85           O  
+ANISOU 8997  OH  TYR C 294    11634  15100  14243   4210   -923  -2451       O  
+ATOM   8998  N   ASN C 295     -71.364  62.216 -15.056  1.00106.65           N  
+ANISOU 8998  N   ASN C 295     8894  17899  13729   5591   -763  -3639       N  
+ATOM   8999  CA  ASN C 295     -72.400  62.688 -14.146  1.00108.21           C  
+ANISOU 8999  CA  ASN C 295     8853  18473  13788   5775   -768  -3791       C  
+ATOM   9000  C   ASN C 295     -73.337  63.644 -14.881  1.00119.81           C  
+ANISOU 9000  C   ASN C 295    10367  20004  15153   6155  -1071  -3935       C  
+ATOM   9001  O   ASN C 295     -74.038  63.239 -15.810  1.00129.50           O  
+ANISOU 9001  O   ASN C 295    11390  21442  16372   6133  -1170  -3980       O  
+ATOM   9002  CB  ASN C 295     -71.774  63.373 -12.925  1.00104.04           C  
+ANISOU 9002  CB  ASN C 295     8552  17754  13226   5868   -686  -3777       C  
+ATOM   9003  CG  ASN C 295     -72.750  63.527 -11.771  1.00109.39           C  
+ANISOU 9003  CG  ASN C 295     8938  18866  13759   5919   -609  -3902       C  
+ATOM   9004  OD1 ASN C 295     -73.909  63.897 -11.961  1.00110.73           O  
+ANISOU 9004  OD1 ASN C 295     8917  19337  13819   6115   -749  -4053       O  
+ATOM   9005  ND2 ASN C 295     -72.278  63.247 -10.562  1.00112.95           N  
+ANISOU 9005  ND2 ASN C 295     9358  19360  14200   5747   -388  -3842       N  
+ATOM   9006  N   HIS C 296     -73.326  64.915 -14.491  1.00114.76           N  
+ANISOU 9006  N   HIS C 296    10003  19167  14434   6497  -1226  -4008       N  
+ATOM   9007  CA  HIS C 296     -74.192  65.904 -15.123  1.00120.83           C  
+ANISOU 9007  CA  HIS C 296    10843  19968  15100   6874  -1520  -4145       C  
+ATOM   9008  C   HIS C 296     -73.446  67.121 -15.677  1.00118.10           C  
+ANISOU 9008  C   HIS C 296    11038  19061  14775   7164  -1763  -4093       C  
+ATOM   9009  O   HIS C 296     -73.967  68.234 -15.617  1.00119.87           O  
+ANISOU 9009  O   HIS C 296    11399  19241  14903   7499  -1970  -4210       O  
+ATOM   9010  CB  HIS C 296     -75.265  66.375 -14.138  1.00120.84           C  
+ANISOU 9010  CB  HIS C 296    10600  20362  14953   7045  -1518  -4333       C  
+ATOM   9011  N   TRP C 297     -72.243  66.937 -16.217  1.00125.98           N  
+ANISOU 9011  N   TRP C 297    12351  19624  15892   7032  -1744  -3918       N  
+ATOM   9012  CA  TRP C 297     -71.522  68.092 -16.747  1.00124.81           C  
+ANISOU 9012  CA  TRP C 297    12737  18927  15757   7268  -1971  -3844       C  
+ATOM   9013  C   TRP C 297     -71.353  67.932 -18.254  1.00123.29           C  
+ANISOU 9013  C   TRP C 297    12699  18547  15599   7287  -2145  -3745       C  
+ATOM   9014  O   TRP C 297     -71.504  66.831 -18.784  1.00118.17           O  
+ANISOU 9014  O   TRP C 297    11770  18134  14995   7070  -2050  -3722       O  
+ATOM   9015  CB  TRP C 297     -70.137  68.261 -16.104  1.00116.44           C  
+ANISOU 9015  CB  TRP C 297    12019  17434  14790   7127  -1836  -3710       C  
+ATOM   9016  CG  TRP C 297     -70.110  68.473 -14.612  1.00114.45           C  
+ANISOU 9016  CG  TRP C 297    11674  17309  14503   7104  -1674  -3787       C  
+ATOM   9017  CD1 TRP C 297     -71.178  68.551 -13.766  1.00119.90           C  
+ANISOU 9017  CD1 TRP C 297    12023  18452  15081   7202  -1635  -3960       C  
+ATOM   9018  CD2 TRP C 297     -68.946  68.726 -13.810  1.00106.28           C  
+ANISOU 9018  CD2 TRP C 297    10920  15932  13530   6994  -1553  -3698       C  
+ATOM   9019  NE1 TRP C 297     -70.747  68.776 -12.479  1.00117.77           N  
+ANISOU 9019  NE1 TRP C 297    11790  18161  14798   7155  -1489  -3980       N  
+ATOM   9020  CE2 TRP C 297     -69.382  68.898 -12.482  1.00107.51           C  
+ANISOU 9020  CE2 TRP C 297    10868  16375  13605   7030  -1441  -3823       C  
+ATOM   9021  CE3 TRP C 297     -67.577  68.805 -14.087  1.00100.48           C  
+ANISOU 9021  CE3 TRP C 297    10587  14687  12904   6858  -1526  -3526       C  
+ATOM   9022  CZ2 TRP C 297     -68.498  69.144 -11.432  1.00103.70           C  
+ANISOU 9022  CZ2 TRP C 297    10560  15693  13148   6942  -1312  -3784       C  
+ATOM   9023  CZ3 TRP C 297     -66.702  69.049 -13.044  1.00102.41           C  
+ANISOU 9023  CZ3 TRP C 297    11002  14731  13179   6760  -1393  -3489       C  
+ATOM   9024  CH2 TRP C 297     -67.166  69.216 -11.733  1.00101.04           C  
+ANISOU 9024  CH2 TRP C 297    10608  14857  12924   6807  -1291  -3619       C  
+ATOM   9025  N   GLU C 298     -71.035  69.020 -18.948  1.00124.16           N  
+ANISOU 9025  N   GLU C 298    13255  18237  15684   7530  -2404  -3684       N  
+ATOM   9026  CA  GLU C 298     -70.761  68.908 -20.373  1.00120.64           C  
+ANISOU 9026  CA  GLU C 298    13006  17579  15254   7542  -2575  -3562       C  
+ATOM   9027  C   GLU C 298     -69.407  68.234 -20.538  1.00110.27           C  
+ANISOU 9027  C   GLU C 298    11914  15928  14057   7194  -2396  -3361       C  
+ATOM   9028  O   GLU C 298     -68.467  68.523 -19.796  1.00102.46           O  
+ANISOU 9028  O   GLU C 298    11171  14630  13130   7112  -2280  -3291       O  
+ATOM   9029  CB  GLU C 298     -70.806  70.269 -21.076  1.00121.61           C  
+ANISOU 9029  CB  GLU C 298    13567  17339  15301   7861  -2899  -3521       C  
+ATOM   9030  CG  GLU C 298     -70.223  71.426 -20.297  1.00119.66           C  
+ANISOU 9030  CG  GLU C 298    13699  16705  15061   7975  -2937  -3500       C  
+ATOM   9031  CD  GLU C 298     -70.684  72.767 -20.838  1.00129.39           C  
+ANISOU 9031  CD  GLU C 298    15234  17726  16201   8316  -3259  -3525       C  
+ATOM   9032  OE1 GLU C 298     -71.424  72.781 -21.845  1.00126.34           O  
+ANISOU 9032  OE1 GLU C 298    14779  17485  15739   8468  -3451  -3546       O  
+ATOM   9033  OE2 GLU C 298     -70.309  73.805 -20.258  1.00133.30           O  
+ANISOU 9033  OE2 GLU C 298    16032  17915  16701   8426  -3325  -3527       O  
+ATOM   9034  N   THR C 299     -69.331  67.329 -21.510  1.00108.61           N  
+ANISOU 9034  N   THR C 299    11657  15765  13845   6851  -2345  -3236       N  
+ATOM   9035  CA  THR C 299     -68.158  66.489 -21.736  1.00100.60           C  
+ANISOU 9035  CA  THR C 299    10838  14478  12907   6335  -2122  -3014       C  
+ATOM   9036  C   THR C 299     -66.830  67.254 -21.710  1.00100.00           C  
+ANISOU 9036  C   THR C 299    11309  13815  12870   6306  -2142  -2840       C  
+ATOM   9037  O   THR C 299     -65.887  66.843 -21.029  1.00 94.33           O  
+ANISOU 9037  O   THR C 299    10678  12929  12235   6011  -1911  -2747       O  
+ATOM   9038  CB  THR C 299     -68.295  65.735 -23.081  1.00109.68           C  
+ANISOU 9038  CB  THR C 299    11959  15692  14023   6089  -2167  -2922       C  
+ATOM   9039  OG1 THR C 299     -69.209  64.641 -22.926  1.00121.04           O  
+ANISOU 9039  OG1 THR C 299    12875  17644  15472   5917  -2039  -3046       O  
+ATOM   9040  CG2 THR C 299     -66.963  65.200 -23.542  1.00 95.82           C  
+ANISOU 9040  CG2 THR C 299    10529  13551  12326   5652  -2016  -2690       C  
+ATOM   9041  N   GLU C 300     -66.773  68.385 -22.406  1.00 99.11           N  
+ANISOU 9041  N   GLU C 300    11560  13401  12697   6616  -2425  -2798       N  
+ATOM   9042  CA  GLU C 300     -65.544  69.170 -22.482  1.00106.38           C  
+ANISOU 9042  CA  GLU C 300    13014  13757  13649   6578  -2467  -2624       C  
+ATOM   9043  C   GLU C 300     -65.130  69.685 -21.105  1.00111.64           C  
+ANISOU 9043  C   GLU C 300    13730  14302  14387   6693  -2370  -2706       C  
+ATOM   9044  O   GLU C 300     -63.944  69.694 -20.763  1.00109.19           O  
+ANISOU 9044  O   GLU C 300    13693  13650  14144   6444  -2230  -2569       O  
+ATOM   9045  CB  GLU C 300     -65.716  70.341 -23.452  1.00108.49           C  
+ANISOU 9045  CB  GLU C 300    13644  13746  13831   6923  -2815  -2569       C  
+ATOM   9046  N   HIS C 301     -66.117  70.094 -20.314  1.00105.73           N  
+ANISOU 9046  N   HIS C 301    12698  13861  13615   7071  -2443  -2942       N  
+ATOM   9047  CA  HIS C 301     -65.866  70.618 -18.977  1.00105.10           C  
+ANISOU 9047  CA  HIS C 301    12643  13727  13564   7134  -2346  -3028       C  
+ATOM   9048  C   HIS C 301     -65.278  69.551 -18.050  1.00105.39           C  
+ANISOU 9048  C   HIS C 301    12455  13903  13686   6814  -2012  -3020       C  
+ATOM   9049  O   HIS C 301     -64.276  69.789 -17.369  1.00107.96           O  
+ANISOU 9049  O   HIS C 301    13016  13931  14071   6696  -1903  -2954       O  
+ATOM   9050  CB  HIS C 301     -67.168  71.169 -18.386  1.00111.92           C  
+ANISOU 9050  CB  HIS C 301    13231  14967  14327   7405  -2441  -3238       C  
+ATOM   9051  CG  HIS C 301     -66.967  72.151 -17.273  1.00121.02           C  
+ANISOU 9051  CG  HIS C 301    14546  15971  15466   7503  -2445  -3306       C  
+ATOM   9052  ND1 HIS C 301     -66.056  73.177 -17.341  1.00124.39           N  
+ANISOU 9052  ND1 HIS C 301    15467  15872  15924   7520  -2562  -3190       N  
+ATOM   9053  CD2 HIS C 301     -67.579  72.263 -16.067  1.00123.17           C  
+ANISOU 9053  CD2 HIS C 301    14540  16570  15689   7582  -2352  -3482       C  
+ATOM   9054  CE1 HIS C 301     -66.107  73.885 -16.222  1.00122.24           C  
+ANISOU 9054  CE1 HIS C 301    15209  15605  15633   7614  -2547  -3304       C  
+ATOM   9055  NE2 HIS C 301     -67.019  73.347 -15.436  1.00123.58           N  
+ANISOU 9055  NE2 HIS C 301    14920  16287  15749   7663  -2422  -3482       N  
+ATOM   9056  N   ALA C 302     -65.890  68.369 -18.044  1.00100.49           N  
+ANISOU 9056  N   ALA C 302    11398  13727  13056   6583  -1839  -3052       N  
+ATOM   9057  CA  ALA C 302     -65.414  67.264 -17.215  1.00 97.21           C  
+ANISOU 9057  CA  ALA C 302    10769  13462  12703   6177  -1510  -2997       C  
+ATOM   9058  C   ALA C 302     -64.037  66.776 -17.647  1.00 99.86           C  
+ANISOU 9058  C   ALA C 302    11437  13389  13116   5744  -1375  -2749       C  
+ATOM   9059  O   ALA C 302     -63.178  66.462 -16.809  1.00101.16           O  
+ANISOU 9059  O   ALA C 302    11661  13433  13344   5520  -1170  -2684       O  
+ATOM   9060  CB  ALA C 302     -66.406  66.117 -17.255  1.00 93.78           C  
+ANISOU 9060  CB  ALA C 302     9821  13564  12249   6012  -1384  -3070       C  
+ATOM   9061  N   GLU C 303     -63.832  66.720 -18.959  1.00100.76           N  
+ANISOU 9061  N   GLU C 303    11760  13309  13214   5639  -1494  -2619       N  
+ATOM   9062  CA  GLU C 303     -62.553  66.302 -19.514  1.00 96.26           C  
+ANISOU 9062  CA  GLU C 303    11504  12369  12699   5250  -1385  -2396       C  
+ATOM   9063  C   GLU C 303     -61.477  67.303 -19.125  1.00102.30           C  
+ANISOU 9063  C   GLU C 303    12705  12670  13496   5326  -1430  -2320       C  
+ATOM   9064  O   GLU C 303     -60.321  66.936 -18.907  1.00 95.03           O  
+ANISOU 9064  O   GLU C 303    11960  11505  12642   5007  -1258  -2183       O  
+ATOM   9065  CB  GLU C 303     -62.637  66.153 -21.034  1.00 99.73           C  
+ANISOU 9065  CB  GLU C 303    12076  12731  13085   5167  -1528  -2293       C  
+ATOM   9066  CG  GLU C 303     -63.457  64.948 -21.474  1.00109.30           C  
+ANISOU 9066  CG  GLU C 303    12879  14361  14289   4975  -1444  -2345       C  
+ATOM   9067  CD  GLU C 303     -63.594  64.834 -22.982  1.00108.91           C  
+ANISOU 9067  CD  GLU C 303    12950  14264  14168   4920  -1601  -2267       C  
+ATOM   9068  OE1 GLU C 303     -63.159  65.760 -23.697  1.00109.29           O  
+ANISOU 9068  OE1 GLU C 303    13391  13978  14156   5067  -1791  -2167       O  
+ATOM   9069  OE2 GLU C 303     -64.168  63.826 -23.449  1.00 98.03           O  
+ANISOU 9069  OE2 GLU C 303    11270  13190  12788   4731  -1542  -2306       O  
+ATOM   9070  N   GLN C 304     -61.856  68.573 -19.045  1.00109.83           N  
+ANISOU 9070  N   GLN C 304    13832  13494  14405   5753  -1671  -2415       N  
+ATOM   9071  CA  GLN C 304     -60.903  69.594 -18.644  1.00112.59           C  
+ANISOU 9071  CA  GLN C 304    14595  13393  14791   5841  -1737  -2361       C  
+ATOM   9072  C   GLN C 304     -60.651  69.492 -17.130  1.00106.63           C  
+ANISOU 9072  C   GLN C 304    13684  12741  14090   5835  -1549  -2472       C  
+ATOM   9073  O   GLN C 304     -59.573  69.861 -16.654  1.00100.67           O  
+ANISOU 9073  O   GLN C 304    13209  11649  13390   5723  -1488  -2398       O  
+ATOM   9074  CB  GLN C 304     -61.390  70.989 -19.047  1.00109.97           C  
+ANISOU 9074  CB  GLN C 304    14521  12858  14406   6303  -2073  -2428       C  
+ATOM   9075  CG  GLN C 304     -60.345  72.087 -18.879  1.00111.30           C  
+ANISOU 9075  CG  GLN C 304    15180  12496  14613   6328  -2168  -2329       C  
+ATOM   9076  CD  GLN C 304     -60.900  73.478 -19.132  1.00132.81           C  
+ANISOU 9076  CD  GLN C 304    18119  15084  17261   6602  -2451  -2351       C  
+ATOM   9077  OE1 GLN C 304     -61.989  73.817 -18.670  1.00136.95           O  
+ANISOU 9077  OE1 GLN C 304    18394  15912  17728   6864  -2533  -2533       O  
+ATOM   9078  NE2 GLN C 304     -60.168  74.277 -19.905  1.00141.95           N  
+ANISOU 9078  NE2 GLN C 304    19736  15790  18409   6535  -2600  -2163       N  
+ATOM   9079  N   PHE C 305     -61.635  68.983 -16.381  1.00100.18           N  
+ANISOU 9079  N   PHE C 305    12414  12404  13247   5943  -1455  -2647       N  
+ATOM   9080  CA  PHE C 305     -61.448  68.747 -14.944  1.00 98.71           C  
+ANISOU 9080  CA  PHE C 305    12037  12381  13086   5907  -1254  -2743       C  
+ATOM   9081  C   PHE C 305     -60.388  67.679 -14.742  1.00 91.31           C  
+ANISOU 9081  C   PHE C 305    11115  11356  12222   5409   -979  -2563       C  
+ATOM   9082  O   PHE C 305     -59.455  67.862 -13.962  1.00 84.42           O  
+ANISOU 9082  O   PHE C 305    10410  10272  11394   5313   -875  -2527       O  
+ATOM   9083  CB  PHE C 305     -62.746  68.310 -14.255  1.00 96.56           C  
+ANISOU 9083  CB  PHE C 305    11246  12690  12754   6079  -1190  -2946       C  
+ATOM   9084  CG  PHE C 305     -62.525  67.569 -12.954  1.00 99.39           C  
+ANISOU 9084  CG  PHE C 305    11340  13298  13126   5876   -909  -2974       C  
+ATOM   9085  CD1 PHE C 305     -61.880  68.179 -11.887  1.00 98.60           C  
+ANISOU 9085  CD1 PHE C 305    11404  13031  13028   5928   -863  -3006       C  
+ATOM   9086  CD2 PHE C 305     -62.951  66.255 -12.806  1.00 95.81           C  
+ANISOU 9086  CD2 PHE C 305    10495  13236  12674   5574   -694  -2936       C  
+ATOM   9087  CE1 PHE C 305     -61.672  67.498 -10.700  1.00 94.31           C  
+ANISOU 9087  CE1 PHE C 305    10623  12728  12482   5759   -614  -3027       C  
+ATOM   9088  CE2 PHE C 305     -62.745  65.571 -11.617  1.00 88.82           C  
+ANISOU 9088  CE2 PHE C 305     9384  12572  11793   5380   -443  -2936       C  
+ATOM   9089  CZ  PHE C 305     -62.105  66.195 -10.565  1.00 87.59           C  
+ANISOU 9089  CZ  PHE C 305     9382  12268  11631   5496   -404  -2988       C  
+ATOM   9090  N   ILE C 306     -60.551  66.556 -15.436  1.00 88.02           N  
+ANISOU 9090  N   ILE C 306    10516  11110  11820   5104   -869  -2463       N  
+ATOM   9091  CA  ILE C 306     -59.557  65.488 -15.378  1.00 83.55           C  
+ANISOU 9091  CA  ILE C 306     9973  10443  11330   4638   -629  -2293       C  
+ATOM   9092  C   ILE C 306     -58.190  66.006 -15.801  1.00 83.21           C  
+ANISOU 9092  C   ILE C 306    10400   9883  11331   4503   -663  -2135       C  
+ATOM   9093  O   ILE C 306     -57.176  65.761 -15.132  1.00 85.28           O  
+ANISOU 9093  O   ILE C 306    10765   9984  11653   4288   -500  -2061       O  
+ATOM   9094  CB  ILE C 306     -59.945  64.301 -16.282  1.00 81.49           C  
+ANISOU 9094  CB  ILE C 306     9496  10384  11081   4356   -557  -2220       C  
+ATOM   9095  CG1 ILE C 306     -61.393  63.880 -16.024  1.00 90.36           C  
+ANISOU 9095  CG1 ILE C 306    10153  12026  12155   4498   -557  -2380       C  
+ATOM   9096  CG2 ILE C 306     -58.958  63.149 -16.129  1.00 78.00           C  
+ANISOU 9096  CG2 ILE C 306     9057   9850  10730   3898   -310  -2066       C  
+ATOM   9097  CD1 ILE C 306     -61.845  62.708 -16.862  1.00 89.59           C  
+ANISOU 9097  CD1 ILE C 306     9822  12141  12076   4219   -495  -2330       C  
+ATOM   9098  N   HIS C 307     -58.193  66.743 -16.909  1.00 85.18           N  
+ANISOU 9098  N   HIS C 307    10929   9892  11543   4634   -882  -2084       N  
+ATOM   9099  CA  HIS C 307     -56.994  67.352 -17.465  1.00 84.71           C  
+ANISOU 9099  CA  HIS C 307    11327   9353  11506   4519   -945  -1927       C  
+ATOM   9100  C   HIS C 307     -56.224  68.138 -16.408  1.00 87.87           C  
+ANISOU 9100  C   HIS C 307    11935   9504  11949   4606   -927  -1959       C  
+ATOM   9101  O   HIS C 307     -55.043  67.871 -16.161  1.00 86.62           O  
+ANISOU 9101  O   HIS C 307    11936   9125  11849   4320   -781  -1846       O  
+ATOM   9102  CB  HIS C 307     -57.369  68.260 -18.644  1.00 93.50           C  
+ANISOU 9102  CB  HIS C 307    12694  10285  12547   4749  -1227  -1893       C  
+ATOM   9103  CG  HIS C 307     -56.198  68.892 -19.327  1.00 90.38           C  
+ANISOU 9103  CG  HIS C 307    12769   9415  12158   4610  -1299  -1711       C  
+ATOM   9104  ND1 HIS C 307     -55.363  69.798 -18.708  1.00 92.40           N  
+ANISOU 9104  ND1 HIS C 307    13326   9326  12456   4666  -1333  -1694       N  
+ATOM   9105  CD2 HIS C 307     -55.720  68.751 -20.590  1.00 87.42           C  
+ANISOU 9105  CD2 HIS C 307    12607   8866  11741   4404  -1342  -1539       C  
+ATOM   9106  CE1 HIS C 307     -54.425  70.185 -19.552  1.00 90.02           C  
+ANISOU 9106  CE1 HIS C 307    13399   8659  12145   4487  -1390  -1511       C  
+ATOM   9107  NE2 HIS C 307     -54.622  69.562 -20.703  1.00 90.08           N  
+ANISOU 9107  NE2 HIS C 307    13359   8773  12094   4329  -1392  -1412       N  
+ATOM   9108  N   GLN C 308     -56.881  69.096 -15.764  1.00 93.64           N  
+ANISOU 9108  N   GLN C 308    12652  10278  12649   5005  -1079  -2130       N  
+ATOM   9109  CA  GLN C 308     -56.142  69.947 -14.842  1.00 95.45           C  
+ANISOU 9109  CA  GLN C 308    13113  10238  12916   5105  -1095  -2176       C  
+ATOM   9110  C   GLN C 308     -55.908  69.259 -13.494  1.00 93.76           C  
+ANISOU 9110  C   GLN C 308    12635  10260  12731   4973   -848  -2247       C  
+ATOM   9111  O   GLN C 308     -55.017  69.658 -12.743  1.00 98.71           O  
+ANISOU 9111  O   GLN C 308    13442  10666  13398   4928   -798  -2247       O  
+ATOM   9112  CB  GLN C 308     -56.850  71.287 -14.639  1.00 90.60           C  
+ANISOU 9112  CB  GLN C 308    12598   9577  12247   5490  -1341  -2303       C  
+ATOM   9113  CG  GLN C 308     -56.991  72.108 -15.909  1.00 92.85           C  
+ANISOU 9113  CG  GLN C 308    13193   9592  12495   5600  -1599  -2202       C  
+ATOM   9114  CD  GLN C 308     -57.085  73.592 -15.629  1.00102.32           C  
+ANISOU 9114  CD  GLN C 308    14626  10592  13660   5773  -1800  -2230       C  
+ATOM   9115  OE1 GLN C 308     -56.083  74.232 -15.308  1.00116.09           O  
+ANISOU 9115  OE1 GLN C 308    16649  12014  15445   5613  -1789  -2145       O  
+ATOM   9116  NE2 GLN C 308     -58.293  74.142 -15.712  1.00120.63           N  
+ANISOU 9116  NE2 GLN C 308    16815  13116  15905   6097  -1982  -2364       N  
+ATOM   9117  N   LEU C 309     -56.696  68.232 -13.187  1.00 86.34           N  
+ANISOU 9117  N   LEU C 309    11271   9769  11767   4903   -697  -2300       N  
+ATOM   9118  CA  LEU C 309     -56.398  67.395 -12.031  1.00 82.10           C  
+ANISOU 9118  CA  LEU C 309    10491   9453  11251   4704   -443  -2312       C  
+ATOM   9119  C   LEU C 309     -55.035  66.750 -12.221  1.00 80.58           C  
+ANISOU 9119  C   LEU C 309    10488   8992  11137   4284   -281  -2112       C  
+ATOM   9120  O   LEU C 309     -54.182  66.822 -11.339  1.00 83.54           O  
+ANISOU 9120  O   LEU C 309    10952   9247  11543   4194   -176  -2102       O  
+ATOM   9121  CB  LEU C 309     -57.464  66.319 -11.816  1.00 80.62           C  
+ANISOU 9121  CB  LEU C 309     9828   9776  11027   4643   -309  -2366       C  
+ATOM   9122  CG  LEU C 309     -57.116  65.308 -10.717  1.00 77.62           C  
+ANISOU 9122  CG  LEU C 309     9210   9614  10668   4379    -37  -2329       C  
+ATOM   9123  CD1 LEU C 309     -56.927  66.018  -9.384  1.00 86.96           C  
+ANISOU 9123  CD1 LEU C 309    10408  10823  11811   4595    -21  -2463       C  
+ATOM   9124  CD2 LEU C 309     -58.184  64.228 -10.611  1.00 74.81           C  
+ANISOU 9124  CD2 LEU C 309     8399   9743  10281   4281     87  -2358       C  
+ATOM   9125  N   SER C 310     -54.834  66.125 -13.377  1.00 80.52           N  
+ANISOU 9125  N   SER C 310    10534   8904  11154   4039   -267  -1967       N  
+ATOM   9126  CA  SER C 310     -53.540  65.530 -13.700  1.00 77.34           C  
+ANISOU 9126  CA  SER C 310    10315   8248  10822   3656   -130  -1789       C  
+ATOM   9127  C   SER C 310     -52.429  66.580 -13.727  1.00 80.69           C  
+ANISOU 9127  C   SER C 310    11159   8232  11269   3676   -223  -1737       C  
+ATOM   9128  O   SER C 310     -51.344  66.374 -13.167  1.00 78.65           O  
+ANISOU 9128  O   SER C 310    10999   7821  11062   3468    -89  -1674       O  
+ATOM   9129  CB  SER C 310     -53.604  64.807 -15.048  1.00 71.95           C  
+ANISOU 9129  CB  SER C 310     9629   7564  10146   3438   -133  -1672       C  
+ATOM   9130  OG  SER C 310     -54.538  63.743 -15.012  1.00 84.83           O  
+ANISOU 9130  OG  SER C 310    10873   9585  11773   3365    -34  -1715       O  
+ATOM   9131  N   LYS C 311     -52.724  67.717 -14.351  1.00 78.98           N  
+ANISOU 9131  N   LYS C 311    11185   7813  11012   3933   -462  -1765       N  
+ATOM   9132  CA  LYS C 311     -51.723  68.756 -14.567  1.00 79.55           C  
+ANISOU 9132  CA  LYS C 311    11683   7437  11106   3932   -577  -1694       C  
+ATOM   9133  C   LYS C 311     -51.243  69.381 -13.257  1.00 81.58           C  
+ANISOU 9133  C   LYS C 311    12009   7594  11394   4046   -555  -1802       C  
+ATOM   9134  O   LYS C 311     -50.065  69.735 -13.122  1.00 85.98           O  
+ANISOU 9134  O   LYS C 311    12833   7838  11999   3878   -529  -1724       O  
+ATOM   9135  CB  LYS C 311     -52.280  69.846 -15.490  1.00 84.70           C  
+ANISOU 9135  CB  LYS C 311    12576   7902  11705   4208   -859  -1698       C  
+ATOM   9136  CG  LYS C 311     -51.277  70.934 -15.858  1.00 81.82           C  
+ANISOU 9136  CG  LYS C 311    12678   7049  11361   4177   -995  -1594       C  
+ATOM   9137  CD  LYS C 311     -51.966  72.217 -16.295  1.00 89.78           C  
+ANISOU 9137  CD  LYS C 311    13844   7959  12307   4437  -1262  -1606       C  
+ATOM   9138  CE  LYS C 311     -51.033  73.413 -16.175  1.00106.55           C  
+ANISOU 9138  CE  LYS C 311    16293   9742  14448   4304  -1339  -1504       C  
+ATOM   9139  NZ  LYS C 311     -50.595  73.655 -14.775  1.00114.99           N  
+ANISOU 9139  NZ  LYS C 311    17268  10857  15565   4265  -1228  -1605       N  
+ATOM   9140  N   GLU C 312     -52.137  69.478 -12.275  1.00 81.05           N  
+ANISOU 9140  N   GLU C 312    11683   7818  11294   4319   -557  -1988       N  
+ATOM   9141  CA  GLU C 312     -51.757  70.108 -11.019  1.00 88.78           C  
+ANISOU 9141  CA  GLU C 312    12683   8775  12273   4367   -529  -2073       C  
+ATOM   9142  C   GLU C 312     -51.505  69.024  -9.959  1.00 94.10           C  
+ANISOU 9142  C   GLU C 312    13088   9701  12964   4253   -283  -2124       C  
+ATOM   9143  O   GLU C 312     -51.155  69.316  -8.814  1.00108.57           O  
+ANISOU 9143  O   GLU C 312    14887  11581  14785   4247   -219  -2184       O  
+ATOM   9144  CB  GLU C 312     -52.861  71.091 -10.579  1.00 93.91           C  
+ANISOU 9144  CB  GLU C 312    13239   9595  12848   4701   -699  -2227       C  
+ATOM   9145  CG  GLU C 312     -52.626  71.840  -9.268  1.00 98.41           C  
+ANISOU 9145  CG  GLU C 312    13809  10185  13397   4762   -692  -2331       C  
+ATOM   9146  CD  GLU C 312     -51.495  72.858  -9.369  1.00111.69           C  
+ANISOU 9146  CD  GLU C 312    15867  11441  15129   4613   -781  -2233       C  
+ATOM   9147  OE1 GLU C 312     -51.079  73.184 -10.503  1.00115.37           O  
+ANISOU 9147  OE1 GLU C 312    16598  11611  15626   4506   -883  -2088       O  
+ATOM   9148  OE2 GLU C 312     -51.016  73.325  -8.315  1.00121.09           O  
+ANISOU 9148  OE2 GLU C 312    17077  12609  16321   4595   -746  -2300       O  
+ATOM   9149  N   LEU C 313     -51.634  67.762 -10.361  1.00 77.12           N  
+ANISOU 9149  N   LEU C 313    10710   7769  10824   3985   -118  -2009       N  
+ATOM   9150  CA  LEU C 313     -51.019  66.672  -9.613  1.00 78.62           C  
+ANISOU 9150  CA  LEU C 313    10721   8106  11045   3692    131  -1938       C  
+ATOM   9151  C   LEU C 313     -49.531  66.681  -9.896  1.00 93.30           C  
+ANISOU 9151  C   LEU C 313    12879   9595  12977   3409    180  -1794       C  
+ATOM   9152  O   LEU C 313     -48.704  66.634  -8.987  1.00 97.29           O  
+ANISOU 9152  O   LEU C 313    13418  10043  13503   3313    282  -1798       O  
+ATOM   9153  CB  LEU C 313     -51.618  65.313  -9.987  1.00 75.95           C  
+ANISOU 9153  CB  LEU C 313    10063   8082  10711   3489    275  -1862       C  
+ATOM   9154  CG  LEU C 313     -52.821  64.797  -9.196  1.00 74.69           C  
+ANISOU 9154  CG  LEU C 313     9494   8398  10489   3622    355  -1978       C  
+ATOM   9155  CD1 LEU C 313     -53.299  63.479  -9.784  1.00 70.13           C  
+ANISOU 9155  CD1 LEU C 313     8657   8051   9937   3370    475  -1879       C  
+ATOM   9156  CD2 LEU C 313     -52.466  64.629  -7.726  1.00 71.57           C  
+ANISOU 9156  CD2 LEU C 313     8978   8147  10069   3610    502  -2026       C  
+ATOM   9157  N   ILE C 314     -49.203  66.782 -11.179  1.00 88.93           N  
+ANISOU 9157  N   ILE C 314    12539   8804  12447   3283    100  -1673       N  
+ATOM   9158  CA  ILE C 314     -47.812  66.801 -11.601  1.00 73.89           C  
+ANISOU 9158  CA  ILE C 314    10908   6568  10597   3002    144  -1534       C  
+ATOM   9159  C   ILE C 314     -47.129  68.102 -11.192  1.00 77.77           C  
+ANISOU 9159  C   ILE C 314    11717   6734  11100   3129     14  -1585       C  
+ATOM   9160  O   ILE C 314     -45.948  68.102 -10.831  1.00 76.84           O  
+ANISOU 9160  O   ILE C 314    11735   6433  11028   2928     97  -1532       O  
+ATOM   9161  CB  ILE C 314     -47.692  66.596 -13.117  1.00 72.10           C  
+ANISOU 9161  CB  ILE C 314    10818   6207  10370   2840     91  -1396       C  
+ATOM   9162  CG1 ILE C 314     -48.138  65.175 -13.477  1.00 72.15           C  
+ANISOU 9162  CG1 ILE C 314    10521   6505  10387   2651    241  -1346       C  
+ATOM   9163  CG2 ILE C 314     -46.275  66.859 -13.572  1.00 73.95           C  
+ANISOU 9163  CG2 ILE C 314    11359   6095  10642   2588    111  -1269       C  
+ATOM   9164  CD1 ILE C 314     -47.262  64.479 -14.495  1.00 74.87           C  
+ANISOU 9164  CD1 ILE C 314    10970   6712  10766   2317    324  -1196       C  
+ATOM   9165  N   ARG C 315     -47.878  69.201 -11.210  1.00 76.13           N  
+ANISOU 9165  N   ARG C 315    11600   6475  10852   3442   -189  -1688       N  
+ATOM   9166  CA  ARG C 315     -47.316  70.492 -10.821  1.00 76.25           C  
+ANISOU 9166  CA  ARG C 315    11818   6283  10872   3430   -297  -1682       C  
+ATOM   9167  C   ARG C 315     -46.825  70.447  -9.374  1.00 85.85           C  
+ANISOU 9167  C   ARG C 315    12916   7603  12101   3398   -176  -1772       C  
+ATOM   9168  O   ARG C 315     -45.860  71.124  -9.016  1.00 94.12           O  
+ANISOU 9168  O   ARG C 315    14125   8454  13181   3255   -188  -1738       O  
+ATOM   9169  CB  ARG C 315     -48.344  71.608 -10.998  1.00 75.49           C  
+ANISOU 9169  CB  ARG C 315    11766   6197  10719   3737   -521  -1765       C  
+ATOM   9170  N   LYS C 316     -47.491  69.645  -8.548  1.00 79.06           N  
+ANISOU 9170  N   LYS C 316    12655   8207   9179    935   -185  -1810       N  
+ATOM   9171  CA  LYS C 316     -47.094  69.486  -7.154  1.00 87.93           C  
+ANISOU 9171  CA  LYS C 316    13708   9575  10126    774   -197  -1928       C  
+ATOM   9172  C   LYS C 316     -46.255  68.224  -6.963  1.00 85.99           C  
+ANISOU 9172  C   LYS C 316    13056   9728   9889    597   -222  -1718       C  
+ATOM   9173  O   LYS C 316     -46.370  67.539  -5.948  1.00 84.63           O  
+ANISOU 9173  O   LYS C 316    12688   9862   9606    632   -201  -1705       O  
+ATOM   9174  CB  LYS C 316     -48.323  69.439  -6.246  1.00 91.04           C  
+ANISOU 9174  CB  LYS C 316    14096  10065  10429   1095   -103  -2100       C  
+ATOM   9175  N   ASP C 317     -45.422  67.925  -7.957  1.00 93.32           N  
+ANISOU 9175  N   ASP C 317    13863  10651  10942    431   -255  -1542       N  
+ATOM   9176  CA  ASP C 317     -44.413  66.868  -7.877  1.00 91.32           C  
+ANISOU 9176  CA  ASP C 317    13244  10731  10722    266   -287  -1354       C  
+ATOM   9177  C   ASP C 317     -44.974  65.466  -7.607  1.00 87.04           C  
+ANISOU 9177  C   ASP C 317    12373  10426  10273    504   -215  -1215       C  
+ATOM   9178  O   ASP C 317     -44.268  64.613  -7.070  1.00 97.02           O  
+ANISOU 9178  O   ASP C 317    13370  11968  11524    425   -246  -1068       O  
+ATOM   9179  CB  ASP C 317     -43.373  67.208  -6.802  1.00 94.82           C  
+ANISOU 9179  CB  ASP C 317    13679  11382  10965    -49   -397  -1417       C  
+ATOM   9180  CG  ASP C 317     -42.390  68.270  -7.254  1.00104.86           C  
+ANISOU 9180  CG  ASP C 317    15149  12482  12211   -416   -469  -1489       C  
+ATOM   9181  OD1 ASP C 317     -41.496  67.946  -8.064  1.00107.25           O  
+ANISOU 9181  OD1 ASP C 317    15252  12880  12617   -582   -475  -1330       O  
+ATOM   9182  OD2 ASP C 317     -42.495  69.422  -6.779  1.00114.59           O  
+ANISOU 9182  OD2 ASP C 317    16733  13484  13321   -554   -506  -1715       O  
+ATOM   9183  N   PHE C 318     -46.221  65.215  -7.995  1.00 76.04           N  
+ANISOU 9183  N   PHE C 318    10986   8920   8985    789   -123  -1246       N  
+ATOM   9184  CA  PHE C 318     -46.783  63.872  -7.856  1.00 73.77           C  
+ANISOU 9184  CA  PHE C 318    10396   8805   8829    960    -36  -1116       C  
+ATOM   9185  C   PHE C 318     -46.498  63.018  -9.084  1.00 72.50           C  
+ANISOU 9185  C   PHE C 318    10032   8615   8900    982    -12   -998       C  
+ATOM   9186  O   PHE C 318     -46.188  63.534 -10.157  1.00 70.34           O  
+ANISOU 9186  O   PHE C 318     9866   8202   8659    929    -41  -1030       O  
+ATOM   9187  CB  PHE C 318     -48.296  63.917  -7.617  1.00 73.55           C  
+ANISOU 9187  CB  PHE C 318    10403   8736   8808   1221     61  -1229       C  
+ATOM   9188  CG  PHE C 318     -48.690  64.328  -6.227  1.00 77.66           C  
+ANISOU 9188  CG  PHE C 318    11022   9388   9098   1247     94  -1334       C  
+ATOM   9189  CD1 PHE C 318     -49.021  65.642  -5.943  1.00 73.60           C  
+ANISOU 9189  CD1 PHE C 318    10825   8712   8428   1295     74  -1572       C  
+ATOM   9190  CD2 PHE C 318     -48.746  63.393  -5.206  1.00 80.62           C  
+ANISOU 9190  CD2 PHE C 318    11189  10041   9403   1235    158  -1192       C  
+ATOM   9191  CE1 PHE C 318     -49.392  66.018  -4.666  1.00 80.92           C  
+ANISOU 9191  CE1 PHE C 318    11845   9785   9115   1330    123  -1722       C  
+ATOM   9192  CE2 PHE C 318     -49.116  63.761  -3.928  1.00 79.44           C  
+ANISOU 9192  CE2 PHE C 318    11126  10074   8982   1256    204  -1292       C  
+ATOM   9193  CZ  PHE C 318     -49.439  65.076  -3.657  1.00 84.50           C  
+ANISOU 9193  CZ  PHE C 318    12070  10586   9452   1304    190  -1584       C  
+ATOM   9194  N   ASN C 319     -46.608  61.705  -8.913  1.00 79.53           N  
+ANISOU 9194  N   ASN C 319    10647   9629   9942   1057     54   -863       N  
+ATOM   9195  CA  ASN C 319     -46.446  60.772 -10.018  1.00 70.40           C  
+ANISOU 9195  CA  ASN C 319     9298   8428   9021   1103    100   -808       C  
+ATOM   9196  C   ASN C 319     -47.762  60.069 -10.330  1.00 67.16           C  
+ANISOU 9196  C   ASN C 319     8786   7959   8774   1280    195   -864       C  
+ATOM   9197  O   ASN C 319     -48.525  59.740  -9.423  1.00 74.47           O  
+ANISOU 9197  O   ASN C 319     9659   8948   9688   1344    259   -834       O  
+ATOM   9198  CB  ASN C 319     -45.360  59.749  -9.690  1.00 74.78           C  
+ANISOU 9198  CB  ASN C 319     9613   9121   9678   1039     98   -618       C  
+ATOM   9199  CG  ASN C 319     -44.026  60.399  -9.370  1.00 80.01           C  
+ANISOU 9199  CG  ASN C 319    10298   9923  10178    841    -11   -571       C  
+ATOM   9200  OD1 ASN C 319     -43.610  61.350 -10.033  1.00 79.62           O  
+ANISOU 9200  OD1 ASN C 319    10396   9812  10045    706    -54   -669       O  
+ATOM   9201  ND2 ASN C 319     -43.339  59.878  -8.360  1.00 85.60           N  
+ANISOU 9201  ND2 ASN C 319    10848  10838  10836    808    -61   -402       N  
+ATOM   9202  N   ILE C 320     -48.025  59.838 -11.612  1.00 64.16           N  
+ANISOU 9202  N   ILE C 320     8361   7495   8524   1336    207   -954       N  
+ATOM   9203  CA  ILE C 320     -49.289  59.240 -12.025  1.00 62.29           C  
+ANISOU 9203  CA  ILE C 320     8003   7233   8433   1466    270  -1054       C  
+ATOM   9204  C   ILE C 320     -49.104  57.895 -12.722  1.00 66.31           C  
+ANISOU 9204  C   ILE C 320     8290   7705   9201   1450    336  -1053       C  
+ATOM   9205  O   ILE C 320     -48.300  57.768 -13.644  1.00 67.30           O  
+ANISOU 9205  O   ILE C 320     8400   7813   9356   1412    318  -1083       O  
+ATOM   9206  CB  ILE C 320     -50.067  60.184 -12.966  1.00 67.49           C  
+ANISOU 9206  CB  ILE C 320     8804   7849   8991   1583    204  -1215       C  
+ATOM   9207  CG1 ILE C 320     -50.449  61.473 -12.235  1.00 64.20           C  
+ANISOU 9207  CG1 ILE C 320     8625   7398   8368   1655    161  -1250       C  
+ATOM   9208  CG2 ILE C 320     -51.308  59.497 -13.518  1.00 68.48           C  
+ANISOU 9208  CG2 ILE C 320     8735   8020   9264   1695    241  -1342       C  
+ATOM   9209  CD1 ILE C 320     -51.135  62.493 -13.118  1.00 58.26           C  
+ANISOU 9209  CD1 ILE C 320     8052   6562   7524   1821     82  -1357       C  
+ATOM   9210  N   VAL C 321     -49.856  56.895 -12.274  1.00 64.87           N  
+ANISOU 9210  N   VAL C 321     7942   7501   9206   1467    432  -1030       N  
+ATOM   9211  CA  VAL C 321     -49.944  55.621 -12.975  1.00 73.92           C  
+ANISOU 9211  CA  VAL C 321     8908   8543  10638   1448    506  -1093       C  
+ATOM   9212  C   VAL C 321     -51.382  55.427 -13.451  1.00 86.70           C  
+ANISOU 9212  C   VAL C 321    10422  10182  12337   1473    530  -1289       C  
+ATOM   9213  O   VAL C 321     -52.316  55.488 -12.651  1.00 88.97           O  
+ANISOU 9213  O   VAL C 321    10657  10536  12611   1480    582  -1257       O  
+ATOM   9214  CB  VAL C 321     -49.511  54.447 -12.080  1.00 70.49           C  
+ANISOU 9214  CB  VAL C 321     8360   8009  10414   1408    607   -873       C  
+ATOM   9215  CG1 VAL C 321     -49.759  53.125 -12.781  1.00 68.21           C  
+ANISOU 9215  CG1 VAL C 321     7923   7526  10466   1385    702   -976       C  
+ATOM   9216  CG2 VAL C 321     -48.043  54.581 -11.711  1.00 67.85           C  
+ANISOU 9216  CG2 VAL C 321     8063   7718  10001   1409    554   -689       C  
+ATOM   9217  N   SER C 322     -51.562  55.192 -14.747  1.00 89.85           N  
+ANISOU 9217  N   SER C 322    10765  10574  12798   1480    492  -1504       N  
+ATOM   9218  CA  SER C 322     -52.906  55.132 -15.316  1.00 79.71           C  
+ANISOU 9218  CA  SER C 322     9352   9387  11546   1502    466  -1719       C  
+ATOM   9219  C   SER C 322     -53.152  53.884 -16.158  1.00 81.43           C  
+ANISOU 9219  C   SER C 322     9393   9519  12027   1399    517  -1926       C  
+ATOM   9220  O   SER C 322     -52.276  53.436 -16.898  1.00 81.59           O  
+ANISOU 9220  O   SER C 322     9441   9451  12107   1381    526  -1998       O  
+ATOM   9221  CB  SER C 322     -53.171  56.379 -16.162  1.00 69.46           C  
+ANISOU 9221  CB  SER C 322     8183   8242   9969   1638    315  -1825       C  
+ATOM   9222  OG  SER C 322     -54.418  56.288 -16.827  1.00 69.60           O  
+ANISOU 9222  OG  SER C 322     8033   8412   9999   1688    254  -2037       O  
+ATOM   9223  N   GLY C 323     -54.352  53.324 -16.031  1.00 76.24           N  
+ANISOU 9223  N   GLY C 323     8540   8899  11529   1318    562  -2045       N  
+ATOM   9224  CA  GLY C 323     -54.749  52.165 -16.811  1.00 76.35           C  
+ANISOU 9224  CA  GLY C 323     8383   8821  11803   1171    603  -2298       C  
+ATOM   9225  C   GLY C 323     -55.386  52.575 -18.121  1.00 81.66           C  
+ANISOU 9225  C   GLY C 323     8978   9743  12304   1217    445  -2609       C  
+ATOM   9226  O   GLY C 323     -55.856  51.732 -18.887  1.00 90.21           O  
+ANISOU 9226  O   GLY C 323     9905  10825  13548   1081    442  -2897       O  
+ATOM   9227  N   PHE C 324     -55.395  53.882 -18.364  1.00 72.03           N  
+ANISOU 9227  N   PHE C 324     7886   8733  10750   1408    306  -2546       N  
+ATOM   9228  CA  PHE C 324     -55.894  54.461 -19.607  1.00 75.41           C  
+ANISOU 9228  CA  PHE C 324     8286   9428  10937   1512    125  -2756       C  
+ATOM   9229  C   PHE C 324     -57.333  54.035 -19.898  1.00 83.20           C  
+ANISOU 9229  C   PHE C 324     8963  10635  12015   1446     65  -3006       C  
+ATOM   9230  O   PHE C 324     -57.634  53.521 -20.975  1.00 96.22           O  
+ANISOU 9230  O   PHE C 324    10482  12420  13657   1364    -20  -3299       O  
+ATOM   9231  CB  PHE C 324     -54.973  54.077 -20.770  1.00 73.73           C  
+ANISOU 9231  CB  PHE C 324     8160   9190  10663   1469    109  -2909       C  
+ATOM   9232  CG  PHE C 324     -55.210  54.869 -22.024  1.00 79.38           C  
+ANISOU 9232  CG  PHE C 324     8928  10208  11025   1601    -78  -3030       C  
+ATOM   9233  CD1 PHE C 324     -55.021  56.240 -22.038  1.00 68.08           C  
+ANISOU 9233  CD1 PHE C 324     7715   8860   9291   1793   -180  -2800       C  
+ATOM   9234  CD2 PHE C 324     -55.605  54.239 -23.194  1.00 72.78           C  
+ANISOU 9234  CD2 PHE C 324     7944   9563  10146   1525   -154  -3369       C  
+ATOM   9235  CE1 PHE C 324     -55.235  56.972 -23.190  1.00 72.60           C  
+ANISOU 9235  CE1 PHE C 324     8365   9693   9526   1929   -352  -2845       C  
+ATOM   9236  CE2 PHE C 324     -55.819  54.965 -24.350  1.00 73.38           C  
+ANISOU 9236  CE2 PHE C 324     8072   9968   9841   1658   -340  -3444       C  
+ATOM   9237  CZ  PHE C 324     -55.633  56.333 -24.348  1.00 73.83           C  
+ANISOU 9237  CZ  PHE C 324     8357  10097   9599   1871   -437  -3151       C  
+ATOM   9238  N   GLY C 325     -58.217  54.240 -18.927  1.00 84.74           N  
+ANISOU 9238  N   GLY C 325     9016  10902  12278   1468    113  -2910       N  
+ATOM   9239  CA  GLY C 325     -59.625  53.942 -19.112  1.00 81.34           C  
+ANISOU 9239  CA  GLY C 325     8233  10748  11926   1404     60  -3130       C  
+ATOM   9240  C   GLY C 325     -60.271  54.902 -20.092  1.00 84.89           C  
+ANISOU 9240  C   GLY C 325     8621  11570  12062   1653   -190  -3254       C  
+ATOM   9241  O   GLY C 325     -59.949  56.090 -20.108  1.00 87.29           O  
+ANISOU 9241  O   GLY C 325     9165  11898  12104   1931   -281  -3069       O  
+ATOM   9242  N   LEU C 326     -61.177  54.383 -20.916  1.00 85.75           N  
+ANISOU 9242  N   LEU C 326     8417  11965  12199   1548   -309  -3562       N  
+ATOM   9243  CA  LEU C 326     -61.850  55.189 -21.930  1.00 84.50           C  
+ANISOU 9243  CA  LEU C 326     8158  12225  11723   1798   -582  -3678       C  
+ATOM   9244  C   LEU C 326     -62.643  56.333 -21.304  1.00 90.46           C  
+ANISOU 9244  C   LEU C 326     8846  13176  12348   2136   -644  -3498       C  
+ATOM   9245  O   LEU C 326     -63.492  56.113 -20.441  1.00 98.22           O  
+ANISOU 9245  O   LEU C 326     9546  14260  13515   2083   -535  -3516       O  
+ATOM   9246  CB  LEU C 326     -62.771  54.318 -22.787  1.00 90.44           C  
+ANISOU 9246  CB  LEU C 326     8515  13304  12544   1579   -704  -4075       C  
+ATOM   9247  CG  LEU C 326     -63.486  55.035 -23.935  1.00 94.06           C  
+ANISOU 9247  CG  LEU C 326     8825  14277  12639   1834  -1027  -4207       C  
+ATOM   9248  CD1 LEU C 326     -62.481  55.666 -24.888  1.00 95.12           C  
+ANISOU 9248  CD1 LEU C 326     9350  14373  12420   2019  -1144  -4096       C  
+ATOM   9249  CD2 LEU C 326     -64.400  54.076 -24.679  1.00 97.89           C  
+ANISOU 9249  CD2 LEU C 326     8875  15117  13203   1553  -1151  -4645       C  
+ATOM   9250  N   GLY C 327     -62.358  57.554 -21.744  1.00 85.55           N  
+ANISOU 9250  N   GLY C 327     8495  12598  11414   2485   -802  -3325       N  
+ATOM   9251  CA  GLY C 327     -63.057  58.723 -21.247  1.00 86.98           C  
+ANISOU 9251  CA  GLY C 327     8668  12907  11471   2872   -870  -3171       C  
+ATOM   9252  C   GLY C 327     -62.283  59.453 -20.168  1.00 83.69           C  
+ANISOU 9252  C   GLY C 327     8631  12105  11065   2976   -704  -2895       C  
+ATOM   9253  O   GLY C 327     -62.670  60.543 -19.747  1.00 89.14           O  
+ANISOU 9253  O   GLY C 327     9422  12805  11643   3320   -743  -2772       O  
+ATOM   9254  N   VAL C 328     -61.196  58.843 -19.705  1.00 86.09           N  
+ANISOU 9254  N   VAL C 328     9135  12072  11504   2688   -523  -2818       N  
+ATOM   9255  CA  VAL C 328     -60.375  59.438 -18.656  1.00 81.50           C  
+ANISOU 9255  CA  VAL C 328     8887  11163  10915   2727   -379  -2582       C  
+ATOM   9256  C   VAL C 328     -58.898  59.490 -19.050  1.00 86.24           C  
+ANISOU 9256  C   VAL C 328     9848  11483  11435   2597   -366  -2452       C  
+ATOM   9257  O   VAL C 328     -58.251  60.530 -18.928  1.00 92.05           O  
+ANISOU 9257  O   VAL C 328    10928  12041  12004   2736   -396  -2271       O  
+ATOM   9258  CB  VAL C 328     -60.513  58.666 -17.328  1.00 73.31           C  
+ANISOU 9258  CB  VAL C 328     7690  10043  10122   2513   -139  -2559       C  
+ATOM   9259  CG1 VAL C 328     -59.558  59.222 -16.281  1.00 64.26           C  
+ANISOU 9259  CG1 VAL C 328     6887   8608   8920   2525    -18  -2336       C  
+ATOM   9260  CG2 VAL C 328     -61.951  58.711 -16.832  1.00 73.71           C  
+ANISOU 9260  CG2 VAL C 328     7366  10407  10233   2634   -108  -2671       C  
+ATOM   9261  N   GLY C 329     -58.381  58.360 -19.527  1.00 80.03           N  
+ANISOU 9261  N   GLY C 329     8970  10656  10783   2324   -312  -2562       N  
+ATOM   9262  CA  GLY C 329     -56.965  58.200 -19.818  1.00 74.67           C  
+ANISOU 9262  CA  GLY C 329     8546   9753  10073   2185   -256  -2466       C  
+ATOM   9263  C   GLY C 329     -56.326  59.246 -20.715  1.00 84.65           C  
+ANISOU 9263  C   GLY C 329    10110  11024  11031   2327   -385  -2351       C  
+ATOM   9264  O   GLY C 329     -55.265  59.790 -20.393  1.00 88.43           O  
+ANISOU 9264  O   GLY C 329    10866  11292  11440   2291   -327  -2158       O  
+ATOM   9265  N   SER C 330     -56.972  59.527 -21.843  1.00 72.74           N  
+ANISOU 9265  N   SER C 330     8536   9779   9324   2470   -564  -2456       N  
+ATOM   9266  CA  SER C 330     -56.419  60.427 -22.851  1.00 76.57           C  
+ANISOU 9266  CA  SER C 330     9304  10303   9486   2587   -683  -2319       C  
+ATOM   9267  C   SER C 330     -56.230  61.833 -22.295  1.00 75.42           C  
+ANISOU 9267  C   SER C 330     9493   9940   9221   2784   -707  -2043       C  
+ATOM   9268  O   SER C 330     -55.306  62.558 -22.672  1.00 77.37           O  
+ANISOU 9268  O   SER C 330    10065  10042   9292   2758   -706  -1849       O  
+ATOM   9269  CB  SER C 330     -57.334  60.471 -24.079  1.00 84.01           C  
+ANISOU 9269  CB  SER C 330    10087  11629  10206   2742   -899  -2463       C  
+ATOM   9270  OG  SER C 330     -57.896  59.199 -24.348  1.00 89.96           O  
+ANISOU 9270  OG  SER C 330    10470  12588  11124   2563   -894  -2792       O  
+ATOM   9271  N   PHE C 331     -57.118  62.199 -21.382  1.00 73.31           N  
+ANISOU 9271  N   PHE C 331     9143   9649   9063   2964   -710  -2045       N  
+ATOM   9272  CA  PHE C 331     -57.161  63.538 -20.821  1.00 73.89           C  
+ANISOU 9272  CA  PHE C 331     9524   9504   9049   3200   -736  -1855       C  
+ATOM   9273  C   PHE C 331     -56.206  63.657 -19.639  1.00 69.67           C  
+ANISOU 9273  C   PHE C 331     9188   8654   8630   3005   -561  -1761       C  
+ATOM   9274  O   PHE C 331     -55.679  64.735 -19.355  1.00 69.76           O  
+ANISOU 9274  O   PHE C 331     9559   8403   8544   3060   -563  -1603       O  
+ATOM   9275  CB  PHE C 331     -58.600  63.855 -20.442  1.00 78.12           C  
+ANISOU 9275  CB  PHE C 331     9839  10216   9628   3524   -813  -1948       C  
+ATOM   9276  CG  PHE C 331     -59.584  63.386 -21.473  1.00 80.01           C  
+ANISOU 9276  CG  PHE C 331     9736  10868   9794   3640   -986  -2101       C  
+ATOM   9277  CD1 PHE C 331     -59.623  63.973 -22.726  1.00 85.28           C  
+ANISOU 9277  CD1 PHE C 331    10546  11670  10185   3827  -1192  -1998       C  
+ATOM   9278  CD2 PHE C 331     -60.421  62.314 -21.216  1.00 89.16           C  
+ANISOU 9278  CD2 PHE C 331    10431  12300  11145   3520   -945  -2343       C  
+ATOM   9279  CE1 PHE C 331     -60.508  63.528 -23.689  1.00 96.66           C  
+ANISOU 9279  CE1 PHE C 331    11655  13557  11514   3922  -1381  -2157       C  
+ATOM   9280  CE2 PHE C 331     -61.307  61.865 -22.177  1.00 90.73           C  
+ANISOU 9280  CE2 PHE C 331    10290  12913  11271   3577  -1123  -2525       C  
+ATOM   9281  CZ  PHE C 331     -61.350  62.472 -23.413  1.00 96.31           C  
+ANISOU 9281  CZ  PHE C 331    11124  13796  11672   3787  -1354  -2445       C  
+ATOM   9282  N   VAL C 332     -55.995  62.539 -18.952  1.00 70.72           N  
+ANISOU 9282  N   VAL C 332     9088   8813   8970   2769   -418  -1858       N  
+ATOM   9283  CA  VAL C 332     -54.922  62.436 -17.974  1.00 69.02           C  
+ANISOU 9283  CA  VAL C 332     9015   8377   8834   2551   -277  -1757       C  
+ATOM   9284  C   VAL C 332     -53.599  62.678 -18.689  1.00 74.00           C  
+ANISOU 9284  C   VAL C 332     9876   8895   9344   2382   -286  -1634       C  
+ATOM   9285  O   VAL C 332     -52.766  63.476 -18.243  1.00 77.35           O  
+ANISOU 9285  O   VAL C 332    10579   9117   9694   2304   -262  -1496       O  
+ATOM   9286  CB  VAL C 332     -54.894  61.057 -17.285  1.00 62.97           C  
+ANISOU 9286  CB  VAL C 332     7953   7665   8307   2345   -134  -1833       C  
+ATOM   9287  CG1 VAL C 332     -53.650  60.917 -16.423  1.00 60.34           C  
+ANISOU 9287  CG1 VAL C 332     7754   7157   8017   2142    -27  -1692       C  
+ATOM   9288  CG2 VAL C 332     -56.154  60.843 -16.460  1.00 64.23           C  
+ANISOU 9288  CG2 VAL C 332     7876   7956   8573   2456    -81  -1924       C  
+ATOM   9289  N   ILE C 333     -53.429  61.991 -19.816  1.00 67.51           N  
+ANISOU 9289  N   ILE C 333     8923   8232   8495   2309   -313  -1710       N  
+ATOM   9290  CA  ILE C 333     -52.241  62.145 -20.647  1.00 67.29           C  
+ANISOU 9290  CA  ILE C 333     9060   8182   8327   2156   -297  -1615       C  
+ATOM   9291  C   ILE C 333     -52.073  63.597 -21.081  1.00 78.25           C  
+ANISOU 9291  C   ILE C 333    10814   9452   9468   2259   -388  -1419       C  
+ATOM   9292  O   ILE C 333     -50.987  64.158 -20.962  1.00 84.69           O  
+ANISOU 9292  O   ILE C 333    11855  10107  10216   2085   -331  -1265       O  
+ATOM   9293  CB  ILE C 333     -52.294  61.238 -21.893  1.00 69.43           C  
+ANISOU 9293  CB  ILE C 333     9133   8694   8553   2112   -315  -1783       C  
+ATOM   9294  CG1 ILE C 333     -52.219  59.765 -21.487  1.00 66.18           C  
+ANISOU 9294  CG1 ILE C 333     8421   8292   8433   1967   -193  -1968       C  
+ATOM   9295  CG2 ILE C 333     -51.161  61.572 -22.848  1.00 72.60           C  
+ANISOU 9295  CG2 ILE C 333     9712   9136   8736   1991   -285  -1676       C  
+ATOM   9296  CD1 ILE C 333     -52.150  58.813 -22.662  1.00 67.58           C  
+ANISOU 9296  CD1 ILE C 333     8429   8656   8592   1897   -185  -2198       C  
+ATOM   9297  N   ASN C 334     -53.150  64.202 -21.576  1.00 77.49           N  
+ANISOU 9297  N   ASN C 334    10766   9430   9246   2538   -533  -1414       N  
+ATOM   9298  CA  ASN C 334     -53.114  65.603 -21.994  1.00 88.28           C  
+ANISOU 9298  CA  ASN C 334    12517  10624  10401   2688   -627  -1192       C  
+ATOM   9299  C   ASN C 334     -52.673  66.537 -20.866  1.00 99.61           C  
+ANISOU 9299  C   ASN C 334    14248  11688  11912   2643   -563  -1085       C  
+ATOM   9300  O   ASN C 334     -51.786  67.384 -21.048  1.00104.65           O  
+ANISOU 9300  O   ASN C 334    15223  12098  12443   2494   -540   -898       O  
+ATOM   9301  CB  ASN C 334     -54.486  66.037 -22.512  1.00 89.84           C  
+ANISOU 9301  CB  ASN C 334    12670  10969  10496   3076   -808  -1206       C  
+ATOM   9302  CG  ASN C 334     -54.825  65.420 -23.853  1.00 90.91           C  
+ANISOU 9302  CG  ASN C 334    12603  11492  10449   3111   -919  -1281       C  
+ATOM   9303  OD1 ASN C 334     -53.940  65.136 -24.659  1.00 91.06           O  
+ANISOU 9303  OD1 ASN C 334    12679  11600  10318   2896   -870  -1237       O  
+ATOM   9304  ND2 ASN C 334     -56.113  65.210 -24.099  1.00 97.94           N  
+ANISOU 9304  ND2 ASN C 334    13228  12653  11330   3378  -1068  -1418       N  
+ATOM   9305  N   GLY C 335     -53.289  66.363 -19.699  1.00 92.75           N  
+ANISOU 9305  N   GLY C 335    13246  10778  11216   2740   -525  -1221       N  
+ATOM   9306  CA  GLY C 335     -52.968  67.159 -18.528  1.00 85.05           C  
+ANISOU 9306  CA  GLY C 335    12522   9502  10292   2702   -464  -1195       C  
+ATOM   9307  C   GLY C 335     -51.514  67.024 -18.127  1.00 86.33           C  
+ANISOU 9307  C   GLY C 335    12772   9559  10469   2308   -364  -1129       C  
+ATOM   9308  O   GLY C 335     -50.880  67.995 -17.713  1.00 86.57           O  
+ANISOU 9308  O   GLY C 335    13130   9311  10451   2186   -352  -1048       O  
+ATOM   9309  N   VAL C 336     -50.983  65.813 -18.251  1.00 78.15           N  
+ANISOU 9309  N   VAL C 336    11432   8746   9514   2109   -293  -1176       N  
+ATOM   9310  CA  VAL C 336     -49.576  65.563 -17.958  1.00 79.58           C  
+ANISOU 9310  CA  VAL C 336    11614   8907   9716   1772   -208  -1108       C  
+ATOM   9311  C   VAL C 336     -48.665  66.262 -18.969  1.00 79.71           C  
+ANISOU 9311  C   VAL C 336    11864   8855   9566   1601   -214   -945       C  
+ATOM   9312  O   VAL C 336     -47.692  66.934 -18.599  1.00 84.55           O  
+ANISOU 9312  O   VAL C 336    12673   9311  10140   1354   -181   -850       O  
+ATOM   9313  CB  VAL C 336     -49.269  64.051 -17.955  1.00 84.47           C  
+ANISOU 9313  CB  VAL C 336    11850   9759  10488   1671   -127  -1191       C  
+ATOM   9314  CG1 VAL C 336     -47.768  63.802 -17.980  1.00 77.64           C  
+ANISOU 9314  CG1 VAL C 336    10945   8931   9623   1383    -52  -1105       C  
+ATOM   9315  CG2 VAL C 336     -49.918  63.377 -16.753  1.00 71.58           C  
+ANISOU 9315  CG2 VAL C 336    10018   8160   9020   1745    -85  -1284       C  
+ATOM   9316  N   LEU C 337     -48.996  66.110 -20.247  1.00 77.08           N  
+ANISOU 9316  N   LEU C 337    11502   8670   9114   1711   -254   -914       N  
+ATOM   9317  CA  LEU C 337     -48.160  66.628 -21.322  1.00 85.06           C  
+ANISOU 9317  CA  LEU C 337    12698   9694   9926   1540   -230   -738       C  
+ATOM   9318  C   LEU C 337     -48.105  68.149 -21.338  1.00 86.94           C  
+ANISOU 9318  C   LEU C 337    13397   9590  10046   1533   -279   -534       C  
+ATOM   9319  O   LEU C 337     -47.091  68.727 -21.728  1.00 91.75           O  
+ANISOU 9319  O   LEU C 337    14201  10113  10548   1251   -214   -361       O  
+ATOM   9320  CB  LEU C 337     -48.662  66.128 -22.679  1.00 86.25           C  
+ANISOU 9320  CB  LEU C 337    12724  10129   9919   1690   -275   -766       C  
+ATOM   9321  CG  LEU C 337     -48.580  64.625 -22.955  1.00 85.27           C  
+ANISOU 9321  CG  LEU C 337    12191  10309   9899   1653   -207   -991       C  
+ATOM   9322  CD1 LEU C 337     -49.224  64.289 -24.293  1.00 89.15           C  
+ANISOU 9322  CD1 LEU C 337    12600  11086  10188   1807   -284  -1067       C  
+ATOM   9323  CD2 LEU C 337     -47.148  64.136 -22.897  1.00 82.80           C  
+ANISOU 9323  CD2 LEU C 337    11759  10066   9636   1355    -49   -978       C  
+ATOM   9324  N   GLU C 338     -49.194  68.797 -20.932  1.00 85.12           N  
+ANISOU 9324  N   GLU C 338    13339   9155   9848   1842   -381   -556       N  
+ATOM   9325  CA  GLU C 338     -49.194  70.256 -20.830  1.00 87.67           C  
+ANISOU 9325  CA  GLU C 338    14141   9055  10112   1875   -422   -387       C  
+ATOM   9326  C   GLU C 338     -48.100  70.757 -19.889  1.00 89.95           C  
+ANISOU 9326  C   GLU C 338    14603   9091  10483   1496   -334   -394       C  
+ATOM   9327  O   GLU C 338     -47.420  71.742 -20.180  1.00 94.30           O  
+ANISOU 9327  O   GLU C 338    15512   9357  10959   1270   -308   -209       O  
+ATOM   9328  CB  GLU C 338     -50.555  70.784 -20.373  1.00 92.49           C  
+ANISOU 9328  CB  GLU C 338    14860   9494  10788   2323   -528   -467       C  
+ATOM   9329  CG  GLU C 338     -50.570  72.300 -20.197  1.00100.48           C  
+ANISOU 9329  CG  GLU C 338    16408   9984  11787   2399   -559   -321       C  
+ATOM   9330  CD  GLU C 338     -51.966  72.882 -20.123  1.00105.42           C  
+ANISOU 9330  CD  GLU C 338    17144  10469  12443   2945   -675   -352       C  
+ATOM   9331  OE1 GLU C 338     -52.863  72.371 -20.825  1.00109.69           O  
+ANISOU 9331  OE1 GLU C 338    17423  11340  12912   3258   -776   -348       O  
+ATOM   9332  OE2 GLU C 338     -52.165  73.854 -19.364  1.00109.59           O  
+ANISOU 9332  OE2 GLU C 338    18005  10569  13066   3067   -666   -404       O  
+ATOM   9333  N   GLU C 339     -47.930  70.068 -18.766  1.00 89.05           N  
+ANISOU 9333  N   GLU C 339    14228   9097  10510   1407   -292   -597       N  
+ATOM   9334  CA  GLU C 339     -46.939  70.460 -17.770  1.00 96.51           C  
+ANISOU 9334  CA  GLU C 339    15276   9888  11505   1055   -242   -643       C  
+ATOM   9335  C   GLU C 339     -45.529  69.960 -18.091  1.00102.14           C  
+ANISOU 9335  C   GLU C 339    15787  10834  12189    639   -158   -559       C  
+ATOM   9336  O   GLU C 339     -44.547  70.625 -17.758  1.00100.65           O  
+ANISOU 9336  O   GLU C 339    15760  10499  11981    276   -129   -513       O  
+ATOM   9337  CB  GLU C 339     -47.362  69.953 -16.387  1.00 90.79           C  
+ANISOU 9337  CB  GLU C 339    14356   9248  10890   1156   -242   -868       C  
+ATOM   9338  CG  GLU C 339     -46.519  70.481 -15.234  1.00 94.45           C  
+ANISOU 9338  CG  GLU C 339    14956   9573  11357    839   -229   -957       C  
+ATOM   9339  CD  GLU C 339     -46.806  71.937 -14.916  1.00102.58           C  
+ANISOU 9339  CD  GLU C 339    16489  10125  12363    873   -264  -1005       C  
+ATOM   9340  OE1 GLU C 339     -47.975  72.356 -15.048  1.00103.40           O  
+ANISOU 9340  OE1 GLU C 339    16756  10046  12484   1279   -297  -1041       O  
+ATOM   9341  OE2 GLU C 339     -45.863  72.661 -14.533  1.00109.92           O  
+ANISOU 9341  OE2 GLU C 339    17640  10856  13268    495   -258  -1020       O  
+ATOM   9342  N   LEU C 340     -45.419  68.803 -18.740  1.00103.06           N  
+ANISOU 9342  N   LEU C 340    15537  11313  12308    685   -114   -563       N  
+ATOM   9343  CA  LEU C 340     -44.096  68.223 -18.999  1.00 97.85           C  
+ANISOU 9343  CA  LEU C 340    14623  10914  11640    355    -17   -516       C  
+ATOM   9344  C   LEU C 340     -43.422  68.722 -20.275  1.00100.92           C  
+ANISOU 9344  C   LEU C 340    15151  11340  11855    150     56   -317       C  
+ATOM   9345  O   LEU C 340     -42.194  68.792 -20.340  1.00106.78           O  
+ANISOU 9345  O   LEU C 340    15799  12203  12571   -212    146   -247       O  
+ATOM   9346  CB  LEU C 340     -44.170  66.693 -19.047  1.00 91.66           C  
+ANISOU 9346  CB  LEU C 340    13387  10472  10968    495     25   -639       C  
+ATOM   9347  CG  LEU C 340     -43.998  65.950 -17.720  1.00 89.55           C  
+ANISOU 9347  CG  LEU C 340    12869  10288  10868    487     19   -752       C  
+ATOM   9348  CD1 LEU C 340     -44.966  66.458 -16.685  1.00 91.34           C  
+ANISOU 9348  CD1 LEU C 340    13283  10300  11123    655    -61   -835       C  
+ATOM   9349  CD2 LEU C 340     -44.145  64.448 -17.904  1.00 88.22           C  
+ANISOU 9349  CD2 LEU C 340    12314  10365  10841    645     73   -840       C  
+ATOM   9350  N   TYR C 341     -44.211  69.072 -21.285  1.00 99.73           N  
+ANISOU 9350  N   TYR C 341    15201  11127  11564    376     18   -211       N  
+ATOM   9351  CA  TYR C 341     -43.642  69.509 -22.556  1.00107.42           C  
+ANISOU 9351  CA  TYR C 341    16318  12181  12317    199     98     15       C  
+ATOM   9352  C   TYR C 341     -43.362  71.009 -22.574  1.00113.48           C  
+ANISOU 9352  C   TYR C 341    17581  12525  13012    -18     95    249       C  
+ATOM   9353  O   TYR C 341     -43.612  71.682 -23.574  1.00108.06           O  
+ANISOU 9353  O   TYR C 341    17193  11733  12133     36     92    493       O  
+ATOM   9354  CB  TYR C 341     -44.572  69.144 -23.715  1.00109.91           C  
+ANISOU 9354  CB  TYR C 341    16611  12690  12459    536     44     41       C  
+ATOM   9355  CG  TYR C 341     -44.520  67.687 -24.118  1.00110.04           C  
+ANISOU 9355  CG  TYR C 341    16168  13144  12496    620    100   -172       C  
+ATOM   9356  CD1 TYR C 341     -43.532  66.842 -23.626  1.00108.66           C  
+ANISOU 9356  CD1 TYR C 341    15653  13158  12474    411    219   -304       C  
+ATOM   9357  CD2 TYR C 341     -45.453  67.159 -25.001  1.00111.85           C  
+ANISOU 9357  CD2 TYR C 341    16305  13594  12597    917     27   -254       C  
+ATOM   9358  CE1 TYR C 341     -43.482  65.509 -23.995  1.00106.68           C  
+ANISOU 9358  CE1 TYR C 341    15022  13231  12282    516    283   -510       C  
+ATOM   9359  CE2 TYR C 341     -45.409  65.830 -25.378  1.00113.73           C  
+ANISOU 9359  CE2 TYR C 341    16158  14178  12876    969     86   -495       C  
+ATOM   9360  CZ  TYR C 341     -44.423  65.010 -24.872  1.00106.58           C  
+ANISOU 9360  CZ  TYR C 341    14959  13381  12156    778    225   -622       C  
+ATOM   9361  OH  TYR C 341     -44.378  63.685 -25.244  1.00 89.55           O  
+ANISOU 9361  OH  TYR C 341    12455  11493  10077    858    296   -872       O  
+HETATM 9362  N   MSE C 342     -42.837  71.526 -21.468  1.00117.10           N  
+ANISOU 9362  N   MSE C 342    18139  12736  13617   -275     93    179       N  
+HETATM 9363  CA  MSE C 342     -42.524  72.946 -21.362  1.00115.98           C  
+ANISOU 9363  CA  MSE C 342    18489  12119  13459   -538     99    349       C  
+HETATM 9364  C   MSE C 342     -41.032  73.200 -21.553  1.00125.21           C  
+ANISOU 9364  C   MSE C 342    19590  13404  14581  -1126    241    468       C  
+HETATM 9365  O   MSE C 342     -40.252  72.266 -21.738  1.00128.38           O  
+ANISOU 9365  O   MSE C 342    19537  14280  14960  -1277    333    410       O  
+HETATM 9366  CB  MSE C 342     -42.981  73.495 -20.009  1.00103.05           C  
+ANISOU 9366  CB  MSE C 342    17056  10101  11996   -460      0    142       C  
+ATOM   9367  N   THR C 346     -39.335  63.913 -23.702  1.00 98.67           N  
+ANISOU 9367  N   THR C 346    13060  12952  11478   -177    760   -585       N  
+ATOM   9368  CA  THR C 346     -39.034  64.708 -22.518  1.00102.99           C  
+ANISOU 9368  CA  THR C 346    13733  13274  12124   -384    665   -469       C  
+ATOM   9369  C   THR C 346     -39.865  64.256 -21.322  1.00110.76           C  
+ANISOU 9369  C   THR C 346    14701  14049  13335   -148    516   -584       C  
+ATOM   9370  O   THR C 346     -39.919  64.938 -20.298  1.00120.91           O  
+ANISOU 9370  O   THR C 346    16149  15124  14667   -257    412   -534       O  
+ATOM   9371  CB  THR C 346     -39.283  66.206 -22.767  1.00103.07           C  
+ANISOU 9371  CB  THR C 346    14212  13009  11941   -582    615   -260       C  
+ATOM   9372  N   ILE C 347     -40.506  63.100 -21.454  1.00104.71           N  
+ANISOU 9372  N   ILE C 347    13741  13344  12699    153    519   -752       N  
+ATOM   9373  CA  ILE C 347     -41.290  62.547 -20.358  1.00 96.14           C  
+ANISOU 9373  CA  ILE C 347    12606  12095  11827    356    415   -838       C  
+ATOM   9374  C   ILE C 347     -40.396  61.713 -19.460  1.00 94.70           C  
+ANISOU 9374  C   ILE C 347    12092  12043  11846    325    447   -844       C  
+ATOM   9375  O   ILE C 347     -39.843  60.697 -19.881  1.00 87.65           O  
+ANISOU 9375  O   ILE C 347    10903  11337  11064    411    555   -922       O  
+ATOM   9376  CB  ILE C 347     -42.457  61.674 -20.855  1.00 95.71           C  
+ANISOU 9376  CB  ILE C 347    12497  12020  11848    651    402  -1008       C  
+ATOM   9377  CG1 ILE C 347     -43.479  62.522 -21.608  1.00 99.90           C  
+ANISOU 9377  CG1 ILE C 347    13332  12454  12169    738    319   -984       C  
+ATOM   9378  CG2 ILE C 347     -43.139  60.979 -19.687  1.00 94.22           C  
+ANISOU 9378  CG2 ILE C 347    12205  11695  11899    809    341  -1070       C  
+ATOM   9379  CD1 ILE C 347     -44.629  61.711 -22.165  1.00103.35           C  
+ANISOU 9379  CD1 ILE C 347    13675  12943  12651    990    282  -1176       C  
+ATOM   9380  N   ASP C 348     -40.261  62.153 -18.216  1.00101.85           N  
+ANISOU 9380  N   ASP C 348    13053  12857  12786    227    347   -768       N  
+ATOM   9381  CA  ASP C 348     -39.564  61.372 -17.213  1.00104.33           C  
+ANISOU 9381  CA  ASP C 348    13067  13309  13263    244    331   -736       C  
+ATOM   9382  C   ASP C 348     -40.428  60.145 -16.943  1.00107.44           C  
+ANISOU 9382  C   ASP C 348    13344  13610  13870    553    342   -812       C  
+ATOM   9383  O   ASP C 348     -41.652  60.241 -16.859  1.00111.42           O  
+ANISOU 9383  O   ASP C 348    14034  13925  14375    680    300   -873       O  
+ATOM   9384  CB  ASP C 348     -39.314  62.194 -15.945  1.00104.17           C  
+ANISOU 9384  CB  ASP C 348    13164  13249  13166     52    202   -659       C  
+ATOM   9385  CG  ASP C 348     -38.295  61.552 -15.019  1.00108.31           C  
+ANISOU 9385  CG  ASP C 348    13346  14025  13780     16    162   -582       C  
+ATOM   9386  OD1 ASP C 348     -38.156  60.312 -15.041  1.00108.61           O  
+ANISOU 9386  OD1 ASP C 348    13104  14157  14007    250    218   -570       O  
+ATOM   9387  OD2 ASP C 348     -37.623  62.295 -14.272  1.00108.15           O  
+ANISOU 9387  OD2 ASP C 348    13340  14107  13644   -244     65   -537       O  
+ATOM   9388  N   ASP C 349     -39.777  58.994 -16.821  1.00102.63           N  
+ANISOU 9388  N   ASP C 349    12413  13127  13454    672    407   -805       N  
+ATOM   9389  CA  ASP C 349     -40.450  57.704 -16.729  1.00104.08           C  
+ANISOU 9389  CA  ASP C 349    12481  13179  13886    934    455   -875       C  
+ATOM   9390  C   ASP C 349     -41.294  57.561 -15.468  1.00104.87           C  
+ANISOU 9390  C   ASP C 349    12670  13124  14052   1005    367   -787       C  
+ATOM   9391  O   ASP C 349     -42.404  57.030 -15.516  1.00114.61           O  
+ANISOU 9391  O   ASP C 349    13959  14185  15402   1137    392   -869       O  
+ATOM   9392  CB  ASP C 349     -39.429  56.567 -16.798  1.00 99.43           C  
+ANISOU 9392  CB  ASP C 349    11553  12715  13512   1066    547   -858       C  
+ATOM   9393  N   ASP C 350     -40.774  58.030 -14.340  1.00 97.76           N  
+ANISOU 9393  N   ASP C 350    11765  12323  13055    896    270   -634       N  
+ATOM   9394  CA  ASP C 350     -41.505  57.906 -13.084  1.00101.04           C  
+ANISOU 9394  CA  ASP C 350    12258  12657  13475    957    204   -543       C  
+ATOM   9395  C   ASP C 350     -42.555  58.986 -12.844  1.00 93.18           C  
+ANISOU 9395  C   ASP C 350    11571  11541  12294    894    150   -627       C  
+ATOM   9396  O   ASP C 350     -43.110  59.055 -11.754  1.00104.48           O  
+ANISOU 9396  O   ASP C 350    13070  12957  13669    923    110   -573       O  
+ATOM   9397  CB  ASP C 350     -40.533  57.886 -11.900  1.00111.67           C  
+ANISOU 9397  CB  ASP C 350    13459  14217  14755    890    107   -355       C  
+ATOM   9398  CG  ASP C 350     -39.500  56.786 -12.015  1.00120.34           C  
+ANISOU 9398  CG  ASP C 350    14223  15445  16057   1025    148   -240       C  
+ATOM   9399  OD1 ASP C 350     -39.895  55.631 -12.289  1.00122.74           O  
+ANISOU 9399  OD1 ASP C 350    14439  15576  16620   1243    249   -236       O  
+ATOM   9400  OD2 ASP C 350     -38.300  57.066 -11.807  1.00121.16           O  
+ANISOU 9400  OD2 ASP C 350    14141  15819  16075    916     78   -161       O  
+ATOM   9401  N   ARG C 351     -42.829  59.830 -13.834  1.00 78.73           N  
+ANISOU 9401  N   ARG C 351     9926   9635  10353    832    155   -746       N  
+ATOM   9402  CA  ARG C 351     -43.857  60.848 -13.645  1.00 75.23           C  
+ANISOU 9402  CA  ARG C 351     9776   9045   9764    843    102   -821       C  
+ATOM   9403  C   ARG C 351     -45.189  60.327 -14.172  1.00 73.12           C  
+ANISOU 9403  C   ARG C 351     9503   8673   9606   1051    149   -929       C  
+ATOM   9404  O   ARG C 351     -46.241  60.581 -13.587  1.00 78.25           O  
+ANISOU 9404  O   ARG C 351    10249   9254  10228   1151    132   -972       O  
+ATOM   9405  CB  ARG C 351     -43.496  62.163 -14.333  1.00 75.08           C  
+ANISOU 9405  CB  ARG C 351    10005   8961   9559    676     64   -846       C  
+ATOM   9406  CG  ARG C 351     -42.152  62.731 -13.932  1.00 80.36           C  
+ANISOU 9406  CG  ARG C 351    10656   9749  10127    395     22   -768       C  
+ATOM   9407  CD  ARG C 351     -42.072  62.930 -12.428  1.00 81.71           C  
+ANISOU 9407  CD  ARG C 351    10847   9970  10229    333    -64   -750       C  
+ATOM   9408  NE  ARG C 351     -43.167  63.733 -11.891  1.00 79.63           N  
+ANISOU 9408  NE  ARG C 351    10886   9505   9864    416    -99   -852       N  
+ATOM   9409  CZ  ARG C 351     -43.190  65.061 -11.864  1.00 79.36           C  
+ANISOU 9409  CZ  ARG C 351    11182   9284   9689    275   -148   -929       C  
+ATOM   9410  NH1 ARG C 351     -42.175  65.758 -12.355  1.00 89.15           N  
+ANISOU 9410  NH1 ARG C 351    12498  10509  10865    -15   -166   -895       N  
+ATOM   9411  NH2 ARG C 351     -44.234  65.692 -11.346  1.00 74.71           N  
+ANISOU 9411  NH2 ARG C 351    10843   8511   9033    422   -163  -1045       N  
+ATOM   9412  N   LEU C 352     -45.135  59.596 -15.280  1.00 70.30           N  
+ANISOU 9412  N   LEU C 352     9008   8338   9363   1108    211  -1000       N  
+ATOM   9413  CA  LEU C 352     -46.333  59.014 -15.868  1.00 63.99           C  
+ANISOU 9413  CA  LEU C 352     8160   7483   8670   1262    240  -1141       C  
+ATOM   9414  C   LEU C 352     -46.052  57.605 -16.372  1.00 67.46           C  
+ANISOU 9414  C   LEU C 352     8354   7932   9348   1306    336  -1210       C  
+ATOM   9415  O   LEU C 352     -45.217  57.406 -17.254  1.00 78.13           O  
+ANISOU 9415  O   LEU C 352     9637   9361  10689   1272    382  -1258       O  
+ATOM   9416  CB  LEU C 352     -46.866  59.882 -17.010  1.00 63.72           C  
+ANISOU 9416  CB  LEU C 352     8305   7451   8455   1301    184  -1235       C  
+ATOM   9417  CG  LEU C 352     -48.099  59.321 -17.727  1.00 63.10           C  
+ANISOU 9417  CG  LEU C 352     8133   7394   8448   1449    177  -1409       C  
+ATOM   9418  CD1 LEU C 352     -49.234  59.071 -16.743  1.00 59.52           C  
+ANISOU 9418  CD1 LEU C 352     7613   6892   8110   1541    176  -1431       C  
+ATOM   9419  CD2 LEU C 352     -48.551  60.245 -18.845  1.00 74.58           C  
+ANISOU 9419  CD2 LEU C 352     9765   8901   9671   1519     89  -1452       C  
+ATOM   9420  N   ILE C 353     -46.755  56.629 -15.810  1.00 61.84           N  
+ANISOU 9420  N   ILE C 353     7515   7128   8853   1376    386  -1224       N  
+ATOM   9421  CA  ILE C 353     -46.644  55.255 -16.269  1.00 67.69           C  
+ANISOU 9421  CA  ILE C 353     8066   7784   9870   1421    486  -1319       C  
+ATOM   9422  C   ILE C 353     -48.010  54.797 -16.759  1.00 71.74           C  
+ANISOU 9422  C   ILE C 353     8537   8236  10486   1451    497  -1526       C  
+ATOM   9423  O   ILE C 353     -48.970  54.727 -15.989  1.00 70.28           O  
+ANISOU 9423  O   ILE C 353     8338   8008  10357   1451    499  -1483       O  
+ATOM   9424  CB  ILE C 353     -46.131  54.314 -15.160  1.00 75.05           C  
+ANISOU 9424  CB  ILE C 353     8874   8614  11026   1448    548  -1116       C  
+ATOM   9425  CG1 ILE C 353     -44.627  54.504 -14.956  1.00 85.77           C  
+ANISOU 9425  CG1 ILE C 353    10174  10094  12321   1438    530   -963       C  
+ATOM   9426  CG2 ILE C 353     -46.454  52.862 -15.489  1.00 61.22           C  
+ANISOU 9426  CG2 ILE C 353     6983   6654   9622   1505    663  -1224       C  
+ATOM   9427  CD1 ILE C 353     -43.796  54.123 -16.161  1.00 89.67           C  
+ANISOU 9427  CD1 ILE C 353    10557  10636  12876   1474    601  -1116       C  
+ATOM   9428  N   LEU C 354     -48.094  54.506 -18.051  1.00 70.43           N  
+ANISOU 9428  N   LEU C 354     8330   8113  10317   1461    507  -1764       N  
+ATOM   9429  CA  LEU C 354     -49.349  54.092 -18.657  1.00 69.46           C  
+ANISOU 9429  CA  LEU C 354     8135   7996  10262   1461    487  -2007       C  
+ATOM   9430  C   LEU C 354     -49.393  52.582 -18.838  1.00 76.72           C  
+ANISOU 9430  C   LEU C 354     8895   8721  11534   1424    607  -2173       C  
+ATOM   9431  O   LEU C 354     -48.466  51.983 -19.383  1.00 83.92           O  
+ANISOU 9431  O   LEU C 354     9770   9575  12542   1451    686  -2260       O  
+ATOM   9432  CB  LEU C 354     -49.550  54.800 -19.996  1.00 66.18           C  
+ANISOU 9432  CB  LEU C 354     7792   7793   9561   1491    391  -2186       C  
+ATOM   9433  CG  LEU C 354     -49.664  56.324 -19.896  1.00 60.67           C  
+ANISOU 9433  CG  LEU C 354     7297   7210   8543   1541    272  -2017       C  
+ATOM   9434  CD1 LEU C 354     -49.296  56.988 -21.212  1.00 62.48           C  
+ANISOU 9434  CD1 LEU C 354     7643   7621   8476   1556    215  -2077       C  
+ATOM   9435  CD2 LEU C 354     -51.064  56.729 -19.458  1.00 64.58           C  
+ANISOU 9435  CD2 LEU C 354     7779   7738   9019   1620    185  -2037       C  
+ATOM   9436  N   ARG C 355     -50.480  51.975 -18.376  1.00 79.12           N  
+ANISOU 9436  N   ARG C 355     9103   8916  12042   1357    635  -2225       N  
+ATOM   9437  CA  ARG C 355     -50.669  50.538 -18.515  1.00 74.43           C  
+ANISOU 9437  CA  ARG C 355     8391   8064  11825   1277    755  -2390       C  
+ATOM   9438  C   ARG C 355     -52.025  50.217 -19.137  1.00 73.99           C  
+ANISOU 9438  C   ARG C 355     8212   8077  11825   1155    713  -2705       C  
+ATOM   9439  O   ARG C 355     -52.917  49.717 -18.451  1.00 79.17           O  
+ANISOU 9439  O   ARG C 355     8767   8624  12690   1033    769  -2666       O  
+ATOM   9440  CB  ARG C 355     -50.547  49.852 -17.152  1.00 66.67           C  
+ANISOU 9440  CB  ARG C 355     7394   6821  11116   1251    869  -2084       C  
+ATOM   9441  CG  ARG C 355     -49.172  49.960 -16.510  1.00 71.03           C  
+ANISOU 9441  CG  ARG C 355     8015   7329  11647   1375    893  -1782       C  
+ATOM   9442  CD  ARG C 355     -48.148  49.092 -17.223  1.00 70.00           C  
+ANISOU 9442  CD  ARG C 355     7846   7026  11724   1466    978  -1916       C  
+ATOM   9443  NE  ARG C 355     -46.831  49.183 -16.599  1.00 76.92           N  
+ANISOU 9443  NE  ARG C 355     8722   7921  12584   1603    987  -1622       N  
+ATOM   9444  CZ  ARG C 355     -46.464  48.488 -15.527  1.00 81.43           C  
+ANISOU 9444  CZ  ARG C 355     9272   8288  13380   1671   1044  -1311       C  
+ATOM   9445  NH1 ARG C 355     -47.317  47.647 -14.955  1.00 78.61           N  
+ANISOU 9445  NH1 ARG C 355     8924   7652  13291   1591   1127  -1234       N  
+ATOM   9446  NH2 ARG C 355     -45.245  48.632 -15.024  1.00 83.98           N  
+ANISOU 9446  NH2 ARG C 355     9553   8709  13647   1809   1016  -1059       N  
+ATOM   9447  N   PRO C 356     -52.190  50.515 -20.437  1.00 73.82           N  
+ANISOU 9447  N   PRO C 356     8178   8281  11590   1171    613  -3010       N  
+ATOM   9448  CA  PRO C 356     -53.446  50.189 -21.121  1.00 78.26           C  
+ANISOU 9448  CA  PRO C 356     8581   8979  12173   1048    537  -3349       C  
+ATOM   9449  C   PRO C 356     -53.705  48.687 -21.130  1.00 78.70           C  
+ANISOU 9449  C   PRO C 356     8527   8708  12668    855    674  -3582       C  
+ATOM   9450  O   PRO C 356     -52.764  47.899 -21.231  1.00 85.59           O  
+ANISOU 9450  O   PRO C 356     9473   9289  13757    880    804  -3620       O  
+ATOM   9451  CB  PRO C 356     -53.227  50.718 -22.542  1.00 91.40           C  
+ANISOU 9451  CB  PRO C 356    10290  10953  13484   1126    411  -3595       C  
+ATOM   9452  CG  PRO C 356     -51.750  50.762 -22.707  1.00 90.39           C  
+ANISOU 9452  CG  PRO C 356    10309  10731  13305   1226    508  -3481       C  
+ATOM   9453  CD  PRO C 356     -51.200  51.102 -21.357  1.00 80.73           C  
+ANISOU 9453  CD  PRO C 356     9164   9329  12179   1282    572  -3058       C  
+ATOM   9454  N   PHE C 357     -54.971  48.303 -21.025  1.00 86.48           N  
+ANISOU 9454  N   PHE C 357     9331   9732  13797    665    652  -3742       N  
+ATOM   9455  CA  PHE C 357     -55.337  46.896 -20.938  1.00 87.29           C  
+ANISOU 9455  CA  PHE C 357     9343   9470  14354    416    794  -3948       C  
+ATOM   9456  C   PHE C 357     -55.377  46.227 -22.304  1.00 89.26           C  
+ANISOU 9456  C   PHE C 357     9549   9734  14633    311    756  -4487       C  
+ATOM   9457  O   PHE C 357     -55.922  46.782 -23.257  1.00 93.37           O  
+ANISOU 9457  O   PHE C 357     9970  10682  14823    316    572  -4759       O  
+ATOM   9458  CB  PHE C 357     -56.693  46.745 -20.251  1.00 89.66           C  
+ANISOU 9458  CB  PHE C 357     9431   9836  14802    194    807  -3909       C  
+ATOM   9459  CG  PHE C 357     -56.651  47.014 -18.781  1.00 99.64           C  
+ANISOU 9459  CG  PHE C 357    10741  10993  16123    241    920  -3416       C  
+ATOM   9460  CD1 PHE C 357     -56.573  48.313 -18.308  1.00100.20           C  
+ANISOU 9460  CD1 PHE C 357    10868  11374  15830    467    823  -3147       C  
+ATOM   9461  CD2 PHE C 357     -56.672  45.973 -17.871  1.00 95.54           C  
+ANISOU 9461  CD2 PHE C 357    10236  10058  16009     59   1126  -3220       C  
+ATOM   9462  CE1 PHE C 357     -56.527  48.571 -16.957  1.00 92.99           C  
+ANISOU 9462  CE1 PHE C 357    10004  10405  14924    506    925  -2741       C  
+ATOM   9463  CE2 PHE C 357     -56.626  46.226 -16.518  1.00 95.39           C  
+ANISOU 9463  CE2 PHE C 357    10262  10004  15976    104   1227  -2756       C  
+ATOM   9464  CZ  PHE C 357     -56.553  47.528 -16.061  1.00 90.55           C  
+ANISOU 9464  CZ  PHE C 357     9687   9751  14967    326   1124  -2540       C  
+ATOM   9465  N   PRO C 358     -54.796  45.023 -22.400  1.00 87.38           N  
+ANISOU 9465  N   PRO C 358     9393   9028  14780    234    926  -4647       N  
+ATOM   9466  CA  PRO C 358     -54.882  44.235 -23.631  1.00 85.93           C  
+ANISOU 9466  CA  PRO C 358     9178   8799  14672    101    921  -5232       C  
+ATOM   9467  C   PRO C 358     -56.286  43.668 -23.815  1.00 98.51           C  
+ANISOU 9467  C   PRO C 358    10553  10430  16446   -266    866  -5572       C  
+ATOM   9468  O   PRO C 358     -56.832  43.066 -22.890  1.00106.49           O  
+ANISOU 9468  O   PRO C 358    11506  11116  17839   -482    990  -5399       O  
+ATOM   9469  CB  PRO C 358     -53.854  43.124 -23.409  1.00 88.16           C  
+ANISOU 9469  CB  PRO C 358     9630   8479  15387    166   1150  -5234       C  
+ATOM   9470  CG  PRO C 358     -53.785  42.972 -21.927  1.00 85.45           C  
+ANISOU 9470  CG  PRO C 358     9336   7805  15329    175   1270  -4680       C  
+ATOM   9471  CD  PRO C 358     -53.997  44.348 -21.361  1.00 86.20           C  
+ANISOU 9471  CD  PRO C 358     9381   8366  15005    299   1128  -4291       C  
+ATOM   9472  N   GLN C 359     -56.864  43.863 -24.995  1.00 97.91           N  
+ANISOU 9472  N   GLN C 359    10341  10782  16077   -354    682  -6040       N  
+ATOM   9473  CA  GLN C 359     -58.227  43.412 -25.249  1.00 91.08           C  
+ANISOU 9473  CA  GLN C 359     9206  10067  15334   -720    588  -6401       C  
+ATOM   9474  C   GLN C 359     -58.241  42.009 -25.845  1.00100.69           C  
+ANISOU 9474  C   GLN C 359    10452  10859  16947  -1024    704  -6955       C  
+ATOM   9475  O   GLN C 359     -57.336  41.630 -26.589  1.00100.69           O  
+ANISOU 9475  O   GLN C 359    10637  10701  16919   -892    767  -7235       O  
+ATOM   9476  CB  GLN C 359     -58.947  44.390 -26.180  1.00 89.71           C  
+ANISOU 9476  CB  GLN C 359     8833  10643  14609   -650    285  -6607       C  
+ATOM   9477  CG  GLN C 359     -58.929  45.836 -25.702  1.00 88.70           C  
+ANISOU 9477  CG  GLN C 359     8720  10892  14091   -318    164  -6098       C  
+ATOM   9478  CD  GLN C 359     -59.555  46.015 -24.332  1.00 95.21           C  
+ANISOU 9478  CD  GLN C 359     9428  11601  15148   -378    252  -5685       C  
+ATOM   9479  OE1 GLN C 359     -60.539  45.358 -23.993  1.00109.56           O  
+ANISOU 9479  OE1 GLN C 359    11003  13364  17261   -701    294  -5831       O  
+ATOM   9480  NE2 GLN C 359     -58.983  46.910 -23.534  1.00 93.40           N  
+ANISOU 9480  NE2 GLN C 359     9365  11354  14769    -90    290  -5182       N  
+ATOM   9481  N   GLY C 360     -59.275  41.244 -25.514  1.00108.60           N  
+ANISOU 9481  N   GLY C 360    11266  11674  18324  -1442    748  -7130       N  
+ATOM   9482  CA  GLY C 360     -59.397  39.874 -25.979  1.00109.72           C  
+ANISOU 9482  CA  GLY C 360    11452  11348  18886  -1785    871  -7619       C  
+ATOM   9483  C   GLY C 360     -59.369  38.884 -24.831  1.00112.31           C  
+ANISOU 9483  C   GLY C 360    11904  10920  19848  -1991   1154  -7300       C  
+ATOM   9484  O   GLY C 360     -59.106  39.260 -23.689  1.00103.44           O  
+ANISOU 9484  O   GLY C 360    10847   9632  18824  -1838   1261  -6729       O  
+ATOM   9485  N   LYS C 361     -59.640  37.617 -25.133  1.00119.50           N  
+ANISOU 9485  N   LYS C 361    12870  11453  21081  -2290   1268  -7528       N  
+ATOM   9486  CA  LYS C 361     -59.686  36.577 -24.109  1.00121.24           C  
+ANISOU 9486  CA  LYS C 361    13237  10939  21890  -2510   1535  -7209       C  
+ATOM   9487  C   LYS C 361     -58.318  36.402 -23.458  1.00118.67           C  
+ANISOU 9487  C   LYS C 361    13256  10100  21733  -2093   1716  -6734       C  
+ATOM   9488  O   LYS C 361     -58.196  36.376 -22.228  1.00124.12           O  
+ANISOU 9488  O   LYS C 361    14023  10426  22711  -2077   1873  -6217       O  
+ATOM   9489  CB  LYS C 361     -60.159  35.252 -24.710  1.00124.33           C  
+ANISOU 9489  CB  LYS C 361    13674  11017  22550  -2878   1602  -7592       C  
+ATOM   9490  N   LYS C 362     -57.291  36.294 -24.297  1.00117.11           N  
+ANISOU 9490  N   LYS C 362    13239   9931  21324  -1756   1690  -6896       N  
+ATOM   9491  CA  LYS C 362     -55.922  36.124 -23.829  1.00118.88           C  
+ANISOU 9491  CA  LYS C 362    13737   9781  21650  -1327   1829  -6486       C  
+ATOM   9492  C   LYS C 362     -55.496  37.332 -23.003  1.00109.63           C  
+ANISOU 9492  C   LYS C 362    12529   8851  20274  -1033   1790  -6021       C  
+ATOM   9493  O   LYS C 362     -54.730  37.206 -22.048  1.00111.04           O  
+ANISOU 9493  O   LYS C 362    12869   8669  20654   -796   1923  -5512       O  
+ATOM   9494  CB  LYS C 362     -54.969  35.921 -25.010  1.00114.79           C  
+ANISOU 9494  CB  LYS C 362    13345   9401  20869  -1046   1794  -6805       C  
+ATOM   9495  N   GLY C 363     -56.000  38.503 -23.380  1.00102.46           N  
+ANISOU 9495  N   GLY C 363    11414   8570  18946  -1035   1593  -6197       N  
+ATOM   9496  CA  GLY C 363     -55.727  39.722 -22.642  1.00109.08           C  
+ANISOU 9496  CA  GLY C 363    12220   9732  19495   -768   1525  -5733       C  
+ATOM   9497  C   GLY C 363     -56.400  39.728 -21.281  1.00105.16           C  
+ANISOU 9497  C   GLY C 363    11654   9110  19192   -944   1608  -5208       C  
+ATOM   9498  O   GLY C 363     -55.758  39.994 -20.268  1.00 96.86           O  
+ANISOU 9498  O   GLY C 363    10723   7935  18145   -710   1687  -4640       O  
+ATOM   9499  N   GLU C 364     -57.697  39.432 -21.259  1.00109.33           N  
+ANISOU 9499  N   GLU C 364    11966   9719  19856  -1371   1591  -5408       N  
+ATOM   9500  CA  GLU C 364     -58.471  39.411 -20.018  1.00109.41           C  
+ANISOU 9500  CA  GLU C 364    11864   9679  20027  -1591   1698  -4952       C  
+ATOM   9501  C   GLU C 364     -58.040  38.294 -19.064  1.00104.79           C  
+ANISOU 9501  C   GLU C 364    11515   8311  19991  -1679   1974  -4579       C  
+ATOM   9502  O   GLU C 364     -58.377  38.322 -17.879  1.00103.79           O  
+ANISOU 9502  O   GLU C 364    11365   8128  19942  -1770   2095  -4060       O  
+ATOM   9503  CB  GLU C 364     -59.969  39.277 -20.306  1.00117.47           C  
+ANISOU 9503  CB  GLU C 364    12543  11000  21090  -2064   1631  -5303       C  
+ATOM   9504  CG  GLU C 364     -60.568  40.418 -21.111  1.00118.29           C  
+ANISOU 9504  CG  GLU C 364    12372  11929  20645  -1958   1339  -5584       C  
+ATOM   9505  CD  GLU C 364     -62.078  40.312 -21.233  1.00127.80           C  
+ANISOU 9505  CD  GLU C 364    13167  13495  21894  -2398   1266  -5863       C  
+ATOM   9506  OE1 GLU C 364     -62.691  39.613 -20.398  1.00127.82           O  
+ANISOU 9506  OE1 GLU C 364    13080  13195  22290  -2769   1470  -5683       O  
+ATOM   9507  OE2 GLU C 364     -62.650  40.925 -22.159  1.00133.62           O  
+ANISOU 9507  OE2 GLU C 364    13659  14845  22266  -2375   1007  -6242       O  
+ATOM   9508  N   GLU C 365     -57.318  37.304 -19.583  1.00113.20           N  
+ANISOU 9508  N   GLU C 365    12811   8775  21425  -1638   2081  -4840       N  
+ATOM   9509  CA  GLU C 365     -56.838  36.195 -18.757  1.00118.67           C  
+ANISOU 9509  CA  GLU C 365    13768   8652  22671  -1659   2335  -4475       C  
+ATOM   9510  C   GLU C 365     -55.897  36.619 -17.621  1.00117.55           C  
+ANISOU 9510  C   GLU C 365    13776   8485  22401  -1241   2384  -3732       C  
+ATOM   9511  O   GLU C 365     -55.784  35.916 -16.617  1.00129.10           O  
+ANISOU 9511  O   GLU C 365    15397   9436  24218  -1292   2572  -3247       O  
+ATOM   9512  CB  GLU C 365     -56.141  35.155 -19.643  1.00118.71           C  
+ANISOU 9512  CB  GLU C 365    13984   8335  22785  -1525   2356  -4766       C  
+ATOM   9513  N   GLN C 366     -55.229  37.760 -17.775  1.00101.30           N  
+ANISOU 9513  N   GLN C 366    11674   6984  19832   -849   2211  -3637       N  
+ATOM   9514  CA  GLN C 366     -54.286  38.255 -16.765  1.00 99.53           C  
+ANISOU 9514  CA  GLN C 366    11563   6824  19432   -467   2219  -2999       C  
+ATOM   9515  C   GLN C 366     -54.576  39.685 -16.292  1.00109.64           C  
+ANISOU 9515  C   GLN C 366    12682   8837  20140   -377   2058  -2744       C  
+ATOM   9516  O   GLN C 366     -53.674  40.374 -15.801  1.00112.42           O  
+ANISOU 9516  O   GLN C 366    13103   9397  20215    -36   1993  -2388       O  
+ATOM   9517  CB  GLN C 366     -52.854  38.193 -17.301  1.00 98.30           C  
+ANISOU 9517  CB  GLN C 366    11552   6534  19265    -22   2195  -3080       C  
+ATOM   9518  CG  GLN C 366     -52.340  36.795 -17.608  1.00111.77           C  
+ANISOU 9518  CG  GLN C 366    13453   7555  21461     20   2348  -3212       C  
+ATOM   9519  CD  GLN C 366     -52.249  35.912 -16.378  1.00128.87           C  
+ANISOU 9519  CD  GLN C 366    15791   9156  24020      4   2519  -2614       C  
+ATOM   9520  OE1 GLN C 366     -53.153  35.128 -16.091  1.00136.53           O  
+ANISOU 9520  OE1 GLN C 366    16800   9758  25318   -387   2645  -2597       O  
+ATOM   9521  NE2 GLN C 366     -51.148  36.034 -15.645  1.00123.78           N  
+ANISOU 9521  NE2 GLN C 366    15238   8481  23311    420   2513  -2099       N  
+ATOM   9522  N   TRP C 367     -55.817  40.136 -16.444  1.00111.57           N  
+ANISOU 9522  N   TRP C 367    12703   9473  20216   -673   1992  -2946       N  
+ATOM   9523  CA  TRP C 367     -56.187  41.495 -16.041  1.00103.41           C  
+ANISOU 9523  CA  TRP C 367    11524   9098  18670   -564   1849  -2757       C  
+ATOM   9524  C   TRP C 367     -55.993  41.756 -14.544  1.00102.37           C  
+ANISOU 9524  C   TRP C 367    11463   8981  18451   -469   1945  -2108       C  
+ATOM   9525  O   TRP C 367     -55.648  42.874 -14.144  1.00103.17           O  
+ANISOU 9525  O   TRP C 367    11569   9502  18131   -222   1831  -1893       O  
+ATOM   9526  CB  TRP C 367     -57.635  41.787 -16.444  1.00106.97           C  
+ANISOU 9526  CB  TRP C 367    11682   9940  19020   -882   1778  -3092       C  
+ATOM   9527  CG  TRP C 367     -57.748  42.328 -17.840  1.00110.70           C  
+ANISOU 9527  CG  TRP C 367    12051  10786  19224   -811   1559  -3633       C  
+ATOM   9528  CD1 TRP C 367     -56.741  42.445 -18.753  1.00106.49           C  
+ANISOU 9528  CD1 TRP C 367    11671  10224  18568   -554   1471  -3858       C  
+ATOM   9529  CD2 TRP C 367     -58.928  42.835 -18.479  1.00113.99           C  
+ANISOU 9529  CD2 TRP C 367    12175  11711  19427   -983   1401  -3992       C  
+ATOM   9530  NE1 TRP C 367     -57.218  42.986 -19.921  1.00103.52           N  
+ANISOU 9530  NE1 TRP C 367    11145  10296  17890   -571   1273  -4316       N  
+ATOM   9531  CE2 TRP C 367     -58.558  43.235 -19.779  1.00108.71           C  
+ANISOU 9531  CE2 TRP C 367    11527  11288  18489   -816   1208  -4401       C  
+ATOM   9532  CE3 TRP C 367     -60.259  42.987 -18.080  1.00110.31           C  
+ANISOU 9532  CE3 TRP C 367    11403  11555  18956  -1249   1406  -3999       C  
+ATOM   9533  CZ2 TRP C 367     -59.470  43.778 -20.682  1.00108.91           C  
+ANISOU 9533  CZ2 TRP C 367    11301  11850  18231   -890    994  -4787       C  
+ATOM   9534  CZ3 TRP C 367     -61.165  43.526 -18.980  1.00106.38           C  
+ANISOU 9534  CZ3 TRP C 367    10619  11595  18207  -1310   1192  -4408       C  
+ATOM   9535  CH2 TRP C 367     -60.765  43.914 -20.265  1.00108.28           C  
+ANISOU 9535  CH2 TRP C 367    10910  12062  18171  -1122    975  -4784       C  
+ATOM   9536  N   ASP C 368     -56.193  40.729 -13.724  1.00103.97           N  
+ANISOU 9536  N   ASP C 368    11741   8722  19040   -674   2157  -1798       N  
+ATOM   9537  CA  ASP C 368     -56.064  40.881 -12.279  1.00110.04           C  
+ANISOU 9537  CA  ASP C 368    12579   9533  19697   -611   2260  -1165       C  
+ATOM   9538  C   ASP C 368     -54.615  41.151 -11.893  1.00112.16           C  
+ANISOU 9538  C   ASP C 368    13048   9753  19813   -181   2187   -829       C  
+ATOM   9539  O   ASP C 368     -54.317  42.130 -11.206  1.00112.45           O  
+ANISOU 9539  O   ASP C 368    13080  10213  19432     10   2097   -552       O  
+ATOM   9540  CB  ASP C 368     -56.570  39.630 -11.556  1.00125.40           C  
+ANISOU 9540  CB  ASP C 368    14588  10955  22104   -943   2517   -872       C  
+ATOM   9541  CG  ASP C 368     -56.561  39.783 -10.045  1.00125.29           C  
+ANISOU 9541  CG  ASP C 368    14632  11064  21910   -912   2637   -202       C  
+ATOM   9542  OD1 ASP C 368     -57.392  40.550  -9.514  1.00119.37           O  
+ANISOU 9542  OD1 ASP C 368    13692  10837  20825  -1029   2647   -135       O  
+ATOM   9543  OD2 ASP C 368     -55.717  39.136  -9.389  1.00126.11           O  
+ANISOU 9543  OD2 ASP C 368    14966  10761  22187   -745   2719    255       O  
+ATOM   9544  N   LYS C 369     -53.717  40.295 -12.370  1.00113.14           N  
+ANISOU 9544  N   LYS C 369    13329   9378  20279    -29   2221   -894       N  
+ATOM   9545  CA  LYS C 369     -52.291  40.459 -12.121  1.00107.32           C  
+ANISOU 9545  CA  LYS C 369    12723   8612  19440    391   2147   -619       C  
+ATOM   9546  C   LYS C 369     -51.790  41.766 -12.716  1.00101.52           C  
+ANISOU 9546  C   LYS C 369    11905   8444  18226    609   1934   -853       C  
+ATOM   9547  O   LYS C 369     -50.927  42.430 -12.140  1.00 97.66           O  
+ANISOU 9547  O   LYS C 369    11448   8213  17446    864   1839   -544       O  
+ATOM   9548  CB  LYS C 369     -51.503  39.280 -12.695  1.00116.31           C  
+ANISOU 9548  CB  LYS C 369    14007   9118  21068    541   2237   -743       C  
+ATOM   9549  N   TYR C 370     -52.334  42.129 -13.874  1.00102.62           N  
+ANISOU 9549  N   TYR C 370    11938   8779  18276    490   1855  -1392       N  
+ATOM   9550  CA  TYR C 370     -51.981  43.388 -14.522  1.00 90.54           C  
+ANISOU 9550  CA  TYR C 370    10350   7761  16288    660   1664  -1603       C  
+ATOM   9551  C   TYR C 370     -52.308  44.585 -13.628  1.00101.04           C  
+ANISOU 9551  C   TYR C 370    11641   9560  17189    682   1576  -1311       C  
+ATOM   9552  O   TYR C 370     -51.471  45.469 -13.421  1.00111.26           O  
+ANISOU 9552  O   TYR C 370    12986  11123  18166    899   1463  -1156       O  
+ATOM   9553  CB  TYR C 370     -52.709  43.507 -15.861  1.00 87.37           C  
+ANISOU 9553  CB  TYR C 370     9841   7509  15847    504   1592  -2189       C  
+ATOM   9554  CG  TYR C 370     -52.114  44.514 -16.822  1.00 84.94           C  
+ANISOU 9554  CG  TYR C 370     9528   7597  15149    704   1426  -2432       C  
+ATOM   9555  CD1 TYR C 370     -50.845  44.326 -17.355  1.00 77.54           C  
+ANISOU 9555  CD1 TYR C 370     8670   6554  14239    939   1437  -2496       C  
+ATOM   9556  CD2 TYR C 370     -52.831  45.635 -17.220  1.00 85.24           C  
+ANISOU 9556  CD2 TYR C 370     9475   8115  14797    664   1272  -2586       C  
+ATOM   9557  CE1 TYR C 370     -50.298  45.237 -18.242  1.00 75.88           C  
+ANISOU 9557  CE1 TYR C 370     8454   6721  13658   1079   1315  -2690       C  
+ATOM   9558  CE2 TYR C 370     -52.294  46.551 -18.108  1.00 88.58           C  
+ANISOU 9558  CE2 TYR C 370     9929   8867  14862    829   1133  -2756       C  
+ATOM   9559  CZ  TYR C 370     -51.028  46.346 -18.616  1.00 82.36           C  
+ANISOU 9559  CZ  TYR C 370     9224   7979  14089   1010   1164  -2802       C  
+ATOM   9560  OH  TYR C 370     -50.492  47.256 -19.499  1.00 84.71           O  
+ANISOU 9560  OH  TYR C 370     9549   8622  14017   1134   1054  -2942       O  
+ATOM   9561  N   ARG C 371     -53.519  44.593 -13.079  1.00102.90           N  
+ANISOU 9561  N   ARG C 371    11779   9890  17427    443   1642  -1253       N  
+ATOM   9562  CA  ARG C 371     -53.970  45.678 -12.209  1.00103.19           C  
+ANISOU 9562  CA  ARG C 371    11772  10363  17074    467   1592  -1030       C  
+ATOM   9563  C   ARG C 371     -53.181  45.734 -10.910  1.00 99.38           C  
+ANISOU 9563  C   ARG C 371    11416   9869  16476    610   1631   -508       C  
+ATOM   9564  O   ARG C 371     -52.792  46.812 -10.461  1.00 98.09           O  
+ANISOU 9564  O   ARG C 371    11294  10052  15923    764   1518   -387       O  
+ATOM   9565  CB  ARG C 371     -55.451  45.523 -11.908  1.00105.16           C  
+ANISOU 9565  CB  ARG C 371    11841  10726  17389    181   1695  -1096       C  
+ATOM   9566  CG  ARG C 371     -56.305  45.889 -13.083  1.00104.61           C  
+ANISOU 9566  CG  ARG C 371    11595  10888  17266     88   1583  -1599       C  
+ATOM   9567  CD  ARG C 371     -57.766  45.886 -12.745  1.00106.41           C  
+ANISOU 9567  CD  ARG C 371    11574  11341  17514   -168   1666  -1665       C  
+ATOM   9568  NE  ARG C 371     -58.570  46.061 -13.948  1.00113.04           N  
+ANISOU 9568  NE  ARG C 371    12208  12401  18341   -263   1534  -2161       N  
+ATOM   9569  CZ  ARG C 371     -59.799  45.583 -14.093  1.00112.89           C  
+ANISOU 9569  CZ  ARG C 371    11915  12473  18506   -576   1600  -2370       C  
+ATOM   9570  NH1 ARG C 371     -60.367  44.917 -13.097  1.00121.16           N  
+ANISOU 9570  NH1 ARG C 371    12876  13386  19772   -842   1827  -2106       N  
+ATOM   9571  NH2 ARG C 371     -60.463  45.777 -15.225  1.00116.81           N  
+ANISOU 9571  NH2 ARG C 371    12207  13230  18947   -637   1437  -2829       N  
+ATOM   9572  N   ARG C 372     -52.970  44.571 -10.298  1.00100.15           N  
+ANISOU 9572  N   ARG C 372    11582   9563  16906    551   1785   -197       N  
+ATOM   9573  CA  ARG C 372     -52.187  44.490  -9.070  1.00 99.42           C  
+ANISOU 9573  CA  ARG C 372    11604   9471  16702    705   1805    338       C  
+ATOM   9574  C   ARG C 372     -50.791  45.046  -9.326  1.00102.28           C  
+ANISOU 9574  C   ARG C 372    12024   9961  16875   1012   1630    349       C  
+ATOM   9575  O   ARG C 372     -50.203  45.729  -8.479  1.00108.25           O  
+ANISOU 9575  O   ARG C 372    12818  11019  17293   1144   1538    633       O  
+ATOM   9576  CB  ARG C 372     -52.101  43.045  -8.572  1.00100.98           C  
+ANISOU 9576  CB  ARG C 372    11892   9132  17342    632   1988    677       C  
+ATOM   9577  CG  ARG C 372     -53.445  42.399  -8.274  1.00105.77           C  
+ANISOU 9577  CG  ARG C 372    12434   9578  18174    259   2194    705       C  
+ATOM   9578  CD  ARG C 372     -53.289  41.064  -7.561  1.00115.38           C  
+ANISOU 9578  CD  ARG C 372    13800  10252  19788    187   2387   1170       C  
+ATOM   9579  NE  ARG C 372     -54.543  40.637  -6.945  1.00119.33           N  
+ANISOU 9579  NE  ARG C 372    14232  10720  20388   -204   2605   1332       N  
+ATOM   9580  CZ  ARG C 372     -54.986  41.063  -5.767  1.00120.25           C  
+ANISOU 9580  CZ  ARG C 372    14313  11221  20156   -280   2687   1718       C  
+ATOM   9581  NH1 ARG C 372     -54.278  41.937  -5.066  1.00118.73           N  
+ANISOU 9581  NH1 ARG C 372    14167  11455  19489      4   2546   1957       N  
+ATOM   9582  NH2 ARG C 372     -56.141  40.618  -5.293  1.00122.29           N  
+ANISOU 9582  NH2 ARG C 372    14476  11461  20528   -663   2918   1842       N  
+ATOM   9583  N   ASP C 373     -50.280  44.754 -10.519  1.00 98.01           N  
+ANISOU 9583  N   ASP C 373    11475   9225  16540   1101   1591      9       N  
+ATOM   9584  CA  ASP C 373     -48.968  45.214 -10.951  1.00 93.87           C  
+ANISOU 9584  CA  ASP C 373    10958   8834  15872   1361   1456    -35       C  
+ATOM   9585  C   ASP C 373     -48.976  46.735 -11.048  1.00 83.26           C  
+ANISOU 9585  C   ASP C 373     9596   7999  14041   1366   1296   -165       C  
+ATOM   9586  O   ASP C 373     -48.015  47.398 -10.652  1.00 76.31           O  
+ANISOU 9586  O   ASP C 373     8731   7358  12904   1509   1183      8       O  
+ATOM   9587  CB  ASP C 373     -48.603  44.587 -12.300  1.00 97.64           C  
+ANISOU 9587  CB  ASP C 373    11416   9036  16647   1425   1489   -439       C  
+ATOM   9588  CG  ASP C 373     -47.167  44.847 -12.707  1.00 99.24           C  
+ANISOU 9588  CG  ASP C 373    11590   9357  16760   1701   1403   -449       C  
+ATOM   9589  OD1 ASP C 373     -46.451  45.581 -11.994  1.00 98.31           O  
+ANISOU 9589  OD1 ASP C 373    11455   9552  16345   1813   1293   -163       O  
+ATOM   9590  OD2 ASP C 373     -46.754  44.317 -13.758  1.00 97.55           O  
+ANISOU 9590  OD2 ASP C 373    11352   8949  16762   1791   1454   -772       O  
+HETATM 9591  N   MSE C 374     -50.068  47.283 -11.574  1.00 84.38           N  
+ANISOU 9591  N   MSE C 374     9699   8295  14068   1207   1282   -471       N  
+HETATM 9592  CA  MSE C 374     -50.228  48.733 -11.642  1.00 91.18           C  
+ANISOU 9592  CA  MSE C 374    10578   9567  14500   1227   1144   -579       C  
+HETATM 9593  C   MSE C 374     -50.207  49.375 -10.260  1.00 95.21           C  
+ANISOU 9593  C   MSE C 374    11143  10312  14722   1243   1121   -241       C  
+HETATM 9594  O   MSE C 374     -49.384  50.246  -9.974  1.00 93.28           O  
+ANISOU 9594  O   MSE C 374    10965  10286  14191   1339   1001   -156       O  
+HETATM 9595  CB  MSE C 374     -51.538  49.107 -12.334  1.00 85.75           C  
+ANISOU 9595  CB  MSE C 374     9816   9001  13766   1097   1133   -918       C  
+HETATM 9596  CG  MSE C 374     -51.727  48.544 -13.721  1.00100.33           C  
+ANISOU 9596  CG  MSE C 374    11598  10698  15826   1047   1133  -1309       C  
+HETATM 9597 SE   MSE C 374     -53.202  49.481 -14.553  1.00101.35          SE  
+ANISOU 9597 SE   MSE C 374    11612  11179  15718    963   1020  -1689      SE  
+HETATM 9598  CE  MSE C 374     -52.489  51.263 -14.267  1.00111.06           C  
+ANISOU 9598  CE  MSE C 374    13014  12739  16446   1174    858  -1532       C  
+ATOM   9599  N   ILE C 375     -51.127  48.927  -9.414  1.00 84.88           N  
+ANISOU 9599  N   ILE C 375     9800   8970  13479   1119   1250    -68       N  
+ATOM   9600  CA  ILE C 375     -51.397  49.553  -8.128  1.00 84.86           C  
+ANISOU 9600  CA  ILE C 375     9837   9250  13155   1108   1261    185       C  
+ATOM   9601  C   ILE C 375     -50.227  49.387  -7.158  1.00 87.52           C  
+ANISOU 9601  C   ILE C 375    10252   9625  13376   1222   1213    581       C  
+ATOM   9602  O   ILE C 375     -50.031  50.213  -6.265  1.00 89.31           O  
+ANISOU 9602  O   ILE C 375    10539  10165  13229   1252   1144    713       O  
+ATOM   9603  CB  ILE C 375     -52.692  48.968  -7.513  1.00 94.32           C  
+ANISOU 9603  CB  ILE C 375    10943  10424  14468    922   1454    284       C  
+ATOM   9604  CG1 ILE C 375     -53.854  49.124  -8.498  1.00 92.82           C  
+ANISOU 9604  CG1 ILE C 375    10614  10263  14391    809   1472   -128       C  
+ATOM   9605  CG2 ILE C 375     -53.028  49.624  -6.182  1.00 94.78           C  
+ANISOU 9605  CG2 ILE C 375    11034  10830  14149    919   1497    514       C  
+ATOM   9606  CD1 ILE C 375     -55.184  48.646  -7.966  1.00 94.49           C  
+ANISOU 9606  CD1 ILE C 375    10669  10525  14708    592   1664    -79       C  
+ATOM   9607  N   THR C 376     -49.435  48.333  -7.348  1.00 88.50           N  
+ANISOU 9607  N   THR C 376    10368   9445  13813   1304   1238    749       N  
+ATOM   9608  CA  THR C 376     -48.274  48.103  -6.489  1.00 93.24           C  
+ANISOU 9608  CA  THR C 376    10998  10108  14319   1458   1164   1144       C  
+ATOM   9609  C   THR C 376     -47.272  49.256  -6.587  1.00 94.54           C  
+ANISOU 9609  C   THR C 376    11167  10610  14144   1553    961   1039       C  
+ATOM   9610  O   THR C 376     -46.611  49.604  -5.608  1.00 90.45           O  
+ANISOU 9610  O   THR C 376    10663  10361  13342   1608    859   1305       O  
+ATOM   9611  CB  THR C 376     -47.567  46.780  -6.842  1.00 99.83           C  
+ANISOU 9611  CB  THR C 376    11811  10521  15600   1596   1223   1302       C  
+ATOM   9612  OG1 THR C 376     -48.517  45.707  -6.810  1.00 99.62           O  
+ANISOU 9612  OG1 THR C 376    11810  10109  15931   1454   1423   1373       O  
+ATOM   9613  CG2 THR C 376     -46.446  46.485  -5.854  1.00 98.45           C  
+ANISOU 9613  CG2 THR C 376    11634  10448  15324   1797   1134   1772       C  
+ATOM   9614  N   ARG C 377     -47.182  49.858  -7.771  1.00 95.19           N  
+ANISOU 9614  N   ARG C 377    11236  10696  14235   1545    901    652       N  
+ATOM   9615  CA  ARG C 377     -46.281  50.983  -7.999  1.00 89.64           C  
+ANISOU 9615  CA  ARG C 377    10548  10270  13240   1575    734    533       C  
+ATOM   9616  C   ARG C 377     -46.726  52.221  -7.223  1.00 90.00           C  
+ANISOU 9616  C   ARG C 377    10704  10624  12869   1478    662    505       C  
+ATOM   9617  O   ARG C 377     -45.944  53.149  -7.019  1.00 94.50           O  
+ANISOU 9617  O   ARG C 377    11313  11427  13164   1462    521    482       O  
+ATOM   9618  CB  ARG C 377     -46.193  51.307  -9.494  1.00 91.66           C  
+ANISOU 9618  CB  ARG C 377    10789  10446  13590   1570    718    155       C  
+ATOM   9619  CG  ARG C 377     -45.899  50.102 -10.376  1.00 99.67           C  
+ANISOU 9619  CG  ARG C 377    11710  11151  15010   1663    816     74       C  
+ATOM   9620  CD  ARG C 377     -45.798  50.491 -11.846  1.00 99.61           C  
+ANISOU 9620  CD  ARG C 377    11691  11152  15005   1650    801   -311       C  
+ATOM   9621  NE  ARG C 377     -44.692  51.409 -12.109  1.00 91.84           N  
+ANISOU 9621  NE  ARG C 377    10692  10432  13773   1669    690   -328       N  
+ATOM   9622  CZ  ARG C 377     -43.510  51.034 -12.588  1.00 90.63           C  
+ANISOU 9622  CZ  ARG C 377    10409  10298  13726   1783    698   -327       C  
+ATOM   9623  NH1 ARG C 377     -43.280  49.757 -12.862  1.00 92.33           N  
+ANISOU 9623  NH1 ARG C 377    10531  10247  14304   1934    809   -325       N  
+ATOM   9624  NH2 ARG C 377     -42.560  51.934 -12.800  1.00 92.72           N  
+ANISOU 9624  NH2 ARG C 377    10636  10842  13751   1742    609   -339       N  
+ATOM   9625  N   THR C 378     -47.984  52.226  -6.792  1.00 96.26           N  
+ANISOU 9625  N   THR C 378    11534  11416  13623   1406    771    485       N  
+ATOM   9626  CA  THR C 378     -48.582  53.407  -6.176  1.00 88.94           C  
+ANISOU 9626  CA  THR C 378    10713  10750  12328   1353    739    378       C  
+ATOM   9627  C   THR C 378     -48.920  53.184  -4.703  1.00100.98           C  
+ANISOU 9627  C   THR C 378    12253  12467  13648   1324    813    668       C  
+ATOM   9628  O   THR C 378     -48.950  52.048  -4.227  1.00115.16           O  
+ANISOU 9628  O   THR C 378    13981  14152  15621   1326    916    976       O  
+ATOM   9629  CB  THR C 378     -49.861  53.836  -6.919  1.00 80.61           C  
+ANISOU 9629  CB  THR C 378     9661   9640  11326   1328    805     59       C  
+ATOM   9630  OG1 THR C 378     -50.893  52.865  -6.703  1.00 84.79           O  
+ANISOU 9630  OG1 THR C 378    10075  10066  12076   1267    981    140       O  
+ATOM   9631  CG2 THR C 378     -49.594  53.952  -8.409  1.00 75.24           C  
+ANISOU 9631  CG2 THR C 378     8969   8803  10816   1355    737   -200       C  
+ATOM   9632  N   GLY C 379     -49.179  54.277  -3.991  1.00 97.37           N  
+ANISOU 9632  N   GLY C 379    11904  12287  12807   1301    771    568       N  
+ATOM   9633  CA  GLY C 379     -49.525  54.212  -2.582  1.00 99.90           C  
+ANISOU 9633  CA  GLY C 379    12248  12871  12839   1272    850    795       C  
+ATOM   9634  C   GLY C 379     -50.824  54.920  -2.241  1.00 98.06           C  
+ANISOU 9634  C   GLY C 379    12052  12793  12413   1257    979    572       C  
+ATOM   9635  O   GLY C 379     -51.307  54.833  -1.113  1.00101.18           O  
+ANISOU 9635  O   GLY C 379    12448  13437  12559   1227   1098    729       O  
+ATOM   9636  N   VAL C 380     -51.372  55.651  -3.206  1.00 92.03           N  
+ANISOU 9636  N   VAL C 380    11312  11915  11739   1301    956    213       N  
+ATOM   9637  CA  VAL C 380     -52.675  56.291  -3.045  1.00 89.63           C  
+ANISOU 9637  CA  VAL C 380    10996  11743  11316   1349   1078    -22       C  
+ATOM   9638  C   VAL C 380     -53.460  56.207  -4.359  1.00 87.22           C  
+ANISOU 9638  C   VAL C 380    10578  11236  11326   1391   1095   -259       C  
+ATOM   9639  O   VAL C 380     -52.925  56.503  -5.424  1.00 82.76           O  
+ANISOU 9639  O   VAL C 380    10074  10488  10884   1426    951   -400       O  
+ATOM   9640  CB  VAL C 380     -52.538  57.762  -2.586  1.00 89.97           C  
+ANISOU 9640  CB  VAL C 380    11249  11955  10980   1425    984   -267       C  
+ATOM   9641  CG1 VAL C 380     -51.523  58.510  -3.441  1.00 91.19           C  
+ANISOU 9641  CG1 VAL C 380    11560  11924  11162   1428    768   -416       C  
+ATOM   9642  CG2 VAL C 380     -53.892  58.460  -2.596  1.00 87.86           C  
+ANISOU 9642  CG2 VAL C 380    10955  11783  10643   1554   1107   -548       C  
+ATOM   9643  N   SER C 381     -54.722  55.797  -4.285  1.00 91.33           N  
+ANISOU 9643  N   SER C 381    10912  11833  11954   1371   1271   -300       N  
+ATOM   9644  CA  SER C 381     -55.552  55.657  -5.479  1.00 88.79           C  
+ANISOU 9644  CA  SER C 381    10433  11396  11906   1395   1270   -534       C  
+ATOM   9645  C   SER C 381     -56.742  56.614  -5.466  1.00 96.43           C  
+ANISOU 9645  C   SER C 381    11332  12583  12724   1551   1313   -807       C  
+ATOM   9646  O   SER C 381     -57.581  56.562  -4.571  1.00105.03           O  
+ANISOU 9646  O   SER C 381    12293  13920  13693   1542   1497   -774       O  
+ATOM   9647  CB  SER C 381     -56.045  54.215  -5.617  1.00 89.53           C  
+ANISOU 9647  CB  SER C 381    10304  11371  12343   1209   1424   -383       C  
+ATOM   9648  OG  SER C 381     -54.958  53.310  -5.707  1.00 94.46           O  
+ANISOU 9648  OG  SER C 381    11000  11739  13151   1126   1386   -144       O  
+ATOM   9649  N   ILE C 382     -56.811  57.479  -6.474  1.00 91.79           N  
+ANISOU 9649  N   ILE C 382    10821  11915  12139   1713   1153  -1061       N  
+ATOM   9650  CA  ILE C 382     -57.931  58.403  -6.630  1.00 77.17           C  
+ANISOU 9650  CA  ILE C 382     8898  10235  10186   1934   1163  -1317       C  
+ATOM   9651  C   ILE C 382     -58.953  57.839  -7.613  1.00 78.82           C  
+ANISOU 9651  C   ILE C 382     8794  10496  10659   1924   1169  -1454       C  
+ATOM   9652  O   ILE C 382     -58.587  57.344  -8.679  1.00 74.25           O  
+ANISOU 9652  O   ILE C 382     8196   9738  10277   1841   1053  -1479       O  
+ATOM   9653  CB  ILE C 382     -57.457  59.787  -7.118  1.00 69.15           C  
+ANISOU 9653  CB  ILE C 382     8185   9088   9000   2147    973  -1484       C  
+ATOM   9654  CG1 ILE C 382     -56.394  60.351  -6.174  1.00 68.93           C  
+ANISOU 9654  CG1 ILE C 382     8457   9016   8718   2096    946  -1395       C  
+ATOM   9655  CG2 ILE C 382     -58.631  60.748  -7.243  1.00 66.73           C  
+ANISOU 9655  CG2 ILE C 382     7819   8926   8611   2446    982  -1728       C  
+ATOM   9656  CD1 ILE C 382     -55.797  61.660  -6.644  1.00 65.60           C  
+ANISOU 9656  CD1 ILE C 382     8365   8395   8166   2221    772  -1541       C  
+ATOM   9657  N   PHE C 383     -60.232  57.912  -7.254  1.00 82.96           N  
+ANISOU 9657  N   PHE C 383     9048  11304  11167   2002   1307  -1566       N  
+ATOM   9658  CA  PHE C 383     -61.280  57.292  -8.061  1.00 81.73           C  
+ANISOU 9658  CA  PHE C 383     8522  11275  11256   1940   1318  -1704       C  
+ATOM   9659  C   PHE C 383     -62.238  58.304  -8.689  1.00 86.78           C  
+ANISOU 9659  C   PHE C 383     9034  12122  11818   2273   1204  -1973       C  
+ATOM   9660  O   PHE C 383     -62.881  59.093  -7.990  1.00 92.35           O  
+ANISOU 9660  O   PHE C 383     9696  13050  12343   2509   1296  -2060       O  
+ATOM   9661  CB  PHE C 383     -62.059  56.289  -7.209  1.00 78.72           C  
+ANISOU 9661  CB  PHE C 383     7826  11097  10987   1689   1589  -1584       C  
+ATOM   9662  CG  PHE C 383     -61.204  55.193  -6.643  1.00 88.18           C  
+ANISOU 9662  CG  PHE C 383     9144  12065  12297   1385   1698  -1271       C  
+ATOM   9663  CD1 PHE C 383     -60.655  55.310  -5.377  1.00 91.65           C  
+ANISOU 9663  CD1 PHE C 383     9775  12552  12497   1371   1818  -1030       C  
+ATOM   9664  CD2 PHE C 383     -60.934  54.055  -7.383  1.00 94.41           C  
+ANISOU 9664  CD2 PHE C 383     9865  12588  13419   1138   1671  -1223       C  
+ATOM   9665  CE1 PHE C 383     -59.860  54.308  -4.856  1.00101.42           C  
+ANISOU 9665  CE1 PHE C 383    11118  13592  13825   1142   1894   -696       C  
+ATOM   9666  CE2 PHE C 383     -60.139  53.050  -6.868  1.00 90.42           C  
+ANISOU 9666  CE2 PHE C 383     9485  11824  13045    919   1769   -915       C  
+ATOM   9667  CZ  PHE C 383     -59.601  53.178  -5.602  1.00 99.16           C  
+ANISOU 9667  CZ  PHE C 383    10769  12997  13910    934   1872   -625       C  
+ATOM   9668  N   LEU C 384     -62.319  58.265 -10.017  1.00 75.77           N  
+ANISOU 9668  N   LEU C 384     7578  10667  10546   2316   1001  -2103       N  
+ATOM   9669  CA  LEU C 384     -63.155  59.178 -10.789  1.00 83.86           C  
+ANISOU 9669  CA  LEU C 384     8487  11881  11496   2662    839  -2313       C  
+ATOM   9670  C   LEU C 384     -64.190  58.423 -11.624  1.00 86.07           C  
+ANISOU 9670  C   LEU C 384     8300  12429  11973   2552    792  -2478       C  
+ATOM   9671  O   LEU C 384     -63.839  57.517 -12.378  1.00 91.45           O  
+ANISOU 9671  O   LEU C 384     8937  12982  12827   2281    725  -2492       O  
+ATOM   9672  CB  LEU C 384     -62.288  60.041 -11.710  1.00 85.68           C  
+ANISOU 9672  CB  LEU C 384     9104  11844  11606   2851    594  -2309       C  
+ATOM   9673  CG  LEU C 384     -61.059  60.720 -11.103  1.00 83.47           C  
+ANISOU 9673  CG  LEU C 384     9297  11258  11161   2865    599  -2165       C  
+ATOM   9674  CD1 LEU C 384     -60.249  61.424 -12.183  1.00 72.84           C  
+ANISOU 9674  CD1 LEU C 384     8277   9664   9733   2969    375  -2146       C  
+ATOM   9675  CD2 LEU C 384     -61.468  61.699 -10.017  1.00 78.91           C  
+ANISOU 9675  CD2 LEU C 384     8822  10763  10398   3117    709  -2218       C  
+ATOM   9676  N   TYR C 385     -65.457  58.807 -11.486  1.00 84.43           N  
+ANISOU 9676  N   TYR C 385     7731  12609  11739   2769    825  -2629       N  
+ATOM   9677  CA  TYR C 385     -66.547  58.273 -12.307  1.00 85.89           C  
+ANISOU 9677  CA  TYR C 385     7417  13141  12076   2701    739  -2825       C  
+ATOM   9678  C   TYR C 385     -66.615  56.745 -12.271  1.00 84.01           C  
+ANISOU 9678  C   TYR C 385     6929  12875  12115   2159    883  -2815       C  
+ATOM   9679  O   TYR C 385     -66.763  56.149 -11.204  1.00 91.45           O  
+ANISOU 9679  O   TYR C 385     7770  13837  13140   1913   1161  -2686       O  
+ATOM   9680  CB  TYR C 385     -66.402  58.760 -13.752  1.00 86.08           C  
+ANISOU 9680  CB  TYR C 385     7539  13143  12025   2919    403  -2933       C  
+ATOM   9681  CG  TYR C 385     -66.285  60.264 -13.883  1.00 86.87           C  
+ANISOU 9681  CG  TYR C 385     7947  13178  11883   3444    252  -2899       C  
+ATOM   9682  CD1 TYR C 385     -67.410  61.078 -13.836  1.00 94.96           C  
+ANISOU 9682  CD1 TYR C 385     8701  14551  12829   3875    203  -3018       C  
+ATOM   9683  CD2 TYR C 385     -65.045  60.869 -14.047  1.00 85.82           C  
+ANISOU 9683  CD2 TYR C 385     8369  12619  11621   3509    168  -2748       C  
+ATOM   9684  CE1 TYR C 385     -67.303  62.452 -13.954  1.00 96.33           C  
+ANISOU 9684  CE1 TYR C 385     9201  14583  12819   4379     73  -2978       C  
+ATOM   9685  CE2 TYR C 385     -64.929  62.242 -14.165  1.00 90.95           C  
+ANISOU 9685  CE2 TYR C 385     9339  13136  12080   3947     45  -2708       C  
+ATOM   9686  CZ  TYR C 385     -66.061  63.028 -14.119  1.00 91.95           C  
+ANISOU 9686  CZ  TYR C 385     9240  13545  12150   4392     -3  -2820       C  
+ATOM   9687  OH  TYR C 385     -65.948  64.395 -14.235  1.00 98.98           O  
+ANISOU 9687  OH  TYR C 385    10493  14227  12889   4852   -119  -2772       O  
+ATOM   9688  N   GLY C 386     -66.511  56.118 -13.440  1.00 78.33           N  
+ANISOU 9688  N   GLY C 386     6134  12100  11530   1974    702  -2951       N  
+ATOM   9689  CA  GLY C 386     -66.509  54.668 -13.535  1.00 81.77           C  
+ANISOU 9689  CA  GLY C 386     6394  12410  12266   1461    822  -2983       C  
+ATOM   9690  C   GLY C 386     -67.715  54.062 -14.234  1.00103.89           C  
+ANISOU 9690  C   GLY C 386     8645  15595  15233   1255    753  -3272       C  
+ATOM   9691  O   GLY C 386     -68.365  53.170 -13.682  1.00109.11           O  
+ANISOU 9691  O   GLY C 386     8977  16357  16123    879    974  -3282       O  
+ATOM   9692  N   ASN C 387     -68.028  54.541 -15.437  1.00106.00           N  
+ANISOU 9692  N   ASN C 387     8802  16100  15374   1478    446  -3496       N  
+ATOM   9693  CA  ASN C 387     -69.143  53.984 -16.203  1.00104.82           C  
+ANISOU 9693  CA  ASN C 387     8105  16375  15347   1276    323  -3810       C  
+ATOM   9694  C   ASN C 387     -68.793  53.645 -17.653  1.00101.70           C  
+ANISOU 9694  C   ASN C 387     7781  15940  14922   1186     37  -4046       C  
+ATOM   9695  O   ASN C 387     -67.963  54.315 -18.271  1.00 88.66           O  
+ANISOU 9695  O   ASN C 387     6529  14117  13042   1480   -145  -3973       O  
+ATOM   9696  CB  ASN C 387     -70.314  54.967 -16.189  1.00101.04           C  
+ANISOU 9696  CB  ASN C 387     7220  16481  14688   1694    211  -3902       C  
+ATOM   9697  CG  ASN C 387     -70.025  56.228 -16.991  1.00103.14           C  
+ANISOU 9697  CG  ASN C 387     7755  16799  14636   2265   -104  -3878       C  
+ATOM   9698  OD1 ASN C 387     -69.968  56.204 -18.221  1.00110.31           O  
+ANISOU 9698  OD1 ASN C 387     8652  17816  15443   2297   -393  -4033       O  
+ATOM   9699  ND2 ASN C 387     -69.831  57.336 -16.294  1.00106.21           N  
+ANISOU 9699  ND2 ASN C 387     8407  17097  14851   2705    -41  -3682       N  
+ATOM   9700  N   LYS C 388     -69.464  52.644 -18.215  1.00 96.92           N  
+ANISOU 9700  N   LYS C 388     6775  15528  14523    772     -3  -4346       N  
+ATOM   9701  CA  LYS C 388     -69.212  52.254 -19.601  1.00 97.18           C  
+ANISOU 9701  CA  LYS C 388     6842  15583  14499    657   -269  -4638       C  
+ATOM   9702  C   LYS C 388     -70.504  51.697 -20.188  1.00111.80           C  
+ANISOU 9702  C   LYS C 388     8054  17974  16450    376   -406  -5023       C  
+ATOM   9703  O   LYS C 388     -71.524  51.645 -19.502  1.00122.71           O  
+ANISOU 9703  O   LYS C 388     8975  19692  17958    281   -277  -5030       O  
+ATOM   9704  CB  LYS C 388     -68.091  51.222 -19.702  1.00 95.94           C  
+ANISOU 9704  CB  LYS C 388     7072  14813  14566    292   -125  -4641       C  
+ATOM   9705  N   ILE C 389     -70.477  51.328 -21.465  1.00117.94           N  
+ANISOU 9705  N   ILE C 389     8777  18895  17140    248   -671  -5358       N  
+ATOM   9706  CA  ILE C 389     -71.618  50.700 -22.131  1.00125.23           C  
+ANISOU 9706  CA  ILE C 389     9096  20338  18148    -93   -837  -5789       C  
+ATOM   9707  C   ILE C 389     -71.489  49.193 -21.938  1.00121.04           C  
+ANISOU 9707  C   ILE C 389     8547  19378  18066   -796   -594  -5997       C  
+ATOM   9708  O   ILE C 389     -70.431  48.626 -22.190  1.00113.26           O  
+ANISOU 9708  O   ILE C 389     8025  17828  17180   -943   -515  -6011       O  
+ATOM   9709  CB  ILE C 389     -71.688  51.051 -23.635  1.00131.59           C  
+ANISOU 9709  CB  ILE C 389     9847  21566  18584    110  -1267  -6077       C  
+ATOM   9710  N   ASP C 390     -72.561  48.541 -21.506  1.00126.50           N  
+ANISOU 9710  N   ASP C 390     8698  20324  19041  -1230   -467  -6160       N  
+ATOM   9711  CA  ASP C 390     -72.479  47.118 -21.218  1.00125.49           C  
+ANISOU 9711  CA  ASP C 390     8584  19711  19387  -1923   -200  -6309       C  
+ATOM   9712  C   ASP C 390     -73.285  46.300 -22.224  1.00130.10           C  
+ANISOU 9712  C   ASP C 390     8708  20636  20087  -2424   -406  -6894       C  
+ATOM   9713  O   ASP C 390     -72.788  45.315 -22.763  1.00139.77           O  
+ANISOU 9713  O   ASP C 390    10165  21412  21530  -2825   -380  -7183       O  
+ATOM   9714  CB  ASP C 390     -72.965  46.822 -19.800  1.00128.44           C  
+ANISOU 9714  CB  ASP C 390     8766  19979  20057  -2170    190  -5998       C  
+ATOM   9715  N   LYS C 391     -74.516  46.700 -22.499  1.00127.47           N  
+ANISOU 9715  N   LYS C 391     7831  21045  19555  -2356   -601  -7031       N  
+ATOM   9716  CA  LYS C 391     -75.288  45.997 -23.507  1.00135.93           C  
+ANISOU 9716  CA  LYS C 391     8689  22386  20572  -2727   -797  -7451       C  
+ATOM   9717  C   LYS C 391     -76.140  46.990 -24.278  1.00142.79           C  
+ANISOU 9717  C   LYS C 391     9234  24082  20938  -2252  -1183  -7507       C  
+ATOM   9718  O   LYS C 391     -77.217  46.655 -24.772  1.00141.12           O  
+ANISOU 9718  O   LYS C 391     8642  24320  20658  -2487  -1316  -7741       O  
+ATOM   9719  CB  LYS C 391     -76.159  44.911 -22.872  1.00141.80           C  
+ANISOU 9719  CB  LYS C 391     9159  22999  21718  -3389   -508  -7488       C  
+ATOM   9720  N   GLY C 392     -75.643  48.216 -24.372  1.00139.60           N  
+ANISOU 9720  N   GLY C 392     9000  23851  20192  -1573  -1360  -7269       N  
+ATOM   9721  CA  GLY C 392     -76.318  49.256 -25.115  1.00144.04           C  
+ANISOU 9721  CA  GLY C 392     9358  25106  20267  -1034  -1727  -7243       C  
+ATOM   9722  C   GLY C 392     -76.632  50.475 -24.274  1.00147.33           C  
+ANISOU 9722  C   GLY C 392     9689  25743  20546   -431  -1678  -6817       C  
+ATOM   9723  O   GLY C 392     -76.794  51.579 -24.796  1.00149.47           O  
+ANISOU 9723  O   GLY C 392     9991  26387  20414    180  -1961  -6677       O  
+ATOM   9724  N   GLN C 393     -76.741  50.261 -22.968  1.00145.64           N  
+ANISOU 9724  N   GLN C 393     9397  25277  20662   -605  -1298  -6599       N  
+ATOM   9725  CA  GLN C 393     -77.066  51.317 -22.014  1.00137.45           C  
+ANISOU 9725  CA  GLN C 393     8305  24396  19523    -81  -1173  -6219       C  
+ATOM   9726  C   GLN C 393     -75.888  51.595 -21.082  1.00135.38           C  
+ANISOU 9726  C   GLN C 393     8480  23561  19398     90   -902  -5924       C  
+ATOM   9727  O   GLN C 393     -74.986  50.768 -20.952  1.00145.56           O  
+ANISOU 9727  O   GLN C 393    10006  24332  20966   -314   -734  -5996       O  
+ATOM   9728  CB  GLN C 393     -78.308  50.939 -21.208  1.00140.78           C  
+ANISOU 9728  CB  GLN C 393     8231  25122  20136   -380   -939  -6190       C  
+ATOM   9729  N   VAL C 394     -75.893  52.756 -20.433  1.00128.17           N  
+ANISOU 9729  N   VAL C 394     7694  22711  18295    692   -852  -5598       N  
+ATOM   9730  CA  VAL C 394     -74.820  53.094 -19.505  1.00120.28           C  
+ANISOU 9730  CA  VAL C 394     7118  21202  17381    883   -590  -5316       C  
+ATOM   9731  C   VAL C 394     -74.946  52.305 -18.205  1.00118.69           C  
+ANISOU 9731  C   VAL C 394     6807  20767  17522    414   -128  -5189       C  
+ATOM   9732  O   VAL C 394     -75.972  52.351 -17.524  1.00125.64           O  
+ANISOU 9732  O   VAL C 394     7324  21987  18426    366     38  -5121       O  
+ATOM   9733  CB  VAL C 394     -74.797  54.600 -19.180  1.00120.33           C  
+ANISOU 9733  CB  VAL C 394     7377  21280  17063   1655   -662  -5017       C  
+ATOM   9734  CG1 VAL C 394     -73.762  54.887 -18.103  1.00115.46           C  
+ANISOU 9734  CG1 VAL C 394     7297  20079  16494   1769   -355  -4698       C  
+ATOM   9735  CG2 VAL C 394     -74.499  55.407 -20.432  1.00115.17           C  
+ANISOU 9735  CG2 VAL C 394     6952  20743  16063   2120  -1089  -5044       C  
+ATOM   9736  N   VAL C 395     -73.881  51.579 -17.879  1.00110.19           N  
+ANISOU 9736  N   VAL C 395     6257  18985  16625     74     80  -5038       N  
+ATOM   9737  CA  VAL C 395     -73.812  50.726 -16.700  1.00116.24           C  
+ANISOU 9737  CA  VAL C 395     7049  19416  17701   -395    511  -4845       C  
+ATOM   9738  C   VAL C 395     -72.500  50.982 -15.949  1.00114.40           C  
+ANISOU 9738  C   VAL C 395     7529  18535  17404   -201    694  -4451       C  
+ATOM   9739  O   VAL C 395     -71.469  51.280 -16.562  1.00115.40           O  
+ANISOU 9739  O   VAL C 395     8150  18308  17387     25    510  -4413       O  
+ATOM   9740  CB  VAL C 395     -73.923  49.227 -17.091  1.00128.15           C  
+ANISOU 9740  CB  VAL C 395     8409  20688  19595  -1154    587  -5093       C  
+ATOM   9741  CG1 VAL C 395     -73.810  48.321 -15.873  1.00134.77           C  
+ANISOU 9741  CG1 VAL C 395     9331  21114  20761  -1638   1041  -4819       C  
+ATOM   9742  CG2 VAL C 395     -75.227  48.963 -17.833  1.00125.48           C  
+ANISOU 9742  CG2 VAL C 395     7327  21038  19311  -1405    386  -5523       C  
+ATOM   9743  N   LYS C 396     -72.552  50.864 -14.625  1.00116.35           N  
+ANISOU 9743  N   LYS C 396     7797  18680  17731   -304   1057  -4160       N  
+ATOM   9744  CA  LYS C 396     -71.385  51.036 -13.761  1.00110.66           C  
+ANISOU 9744  CA  LYS C 396     7685  17422  16940   -169   1243  -3780       C  
+ATOM   9745  C   LYS C 396     -70.245  50.071 -14.091  1.00108.14           C  
+ANISOU 9745  C   LYS C 396     7823  16427  16836   -496   1257  -3716       C  
+ATOM   9746  O   LYS C 396     -70.475  48.902 -14.401  1.00116.16           O  
+ANISOU 9746  O   LYS C 396     8678  17277  18180  -1018   1327  -3869       O  
+ATOM   9747  CB  LYS C 396     -71.795  50.868 -12.296  1.00106.05           C  
+ANISOU 9747  CB  LYS C 396     6960  16935  16401   -324   1645  -3506       C  
+ATOM   9748  N   ALA C 397     -69.016  50.575 -14.019  1.00 96.71           N  
+ANISOU 9748  N   ALA C 397     6939  14590  15217   -184   1195  -3506       N  
+ATOM   9749  CA  ALA C 397     -67.832  49.792 -14.363  1.00105.07           C  
+ANISOU 9749  CA  ALA C 397     8432  15041  16448   -382   1193  -3444       C  
+ATOM   9750  C   ALA C 397     -67.238  49.081 -13.148  1.00111.23           C  
+ANISOU 9750  C   ALA C 397     9467  15387  17409   -620   1521  -3057       C  
+ATOM   9751  O   ALA C 397     -66.604  49.707 -12.298  1.00113.13           O  
+ANISOU 9751  O   ALA C 397    10003  15543  17438   -348   1602  -2747       O  
+ATOM   9752  CB  ALA C 397     -66.782  50.682 -15.015  1.00 97.99           C  
+ANISOU 9752  CB  ALA C 397     7964  13997  15269     56    946  -3424       C  
+ATOM   9753  N   LYS C 398     -67.464  47.772 -13.075  1.00110.24           N  
+ANISOU 9753  N   LYS C 398     9226  14990  17670  -1137   1699  -3078       N  
+ATOM   9754  CA  LYS C 398     -66.965  46.932 -11.985  1.00104.44           C  
+ANISOU 9754  CA  LYS C 398     8725  13811  17145  -1398   2010  -2675       C  
+ATOM   9755  C   LYS C 398     -65.445  47.002 -11.821  1.00103.69           C  
+ANISOU 9755  C   LYS C 398     9189  13231  16978  -1145   1969  -2408       C  
+ATOM   9756  O   LYS C 398     -64.922  46.798 -10.723  1.00105.34           O  
+ANISOU 9756  O   LYS C 398     9625  13224  17175  -1151   2172  -1989       O  
+ATOM   9757  CB  LYS C 398     -67.392  45.479 -12.206  1.00109.44           C  
+ANISOU 9757  CB  LYS C 398     9199  14122  18259  -2000   2167  -2790       C  
+ATOM   9758  N   GLY C 399     -64.747  47.276 -12.919  1.00101.36           N  
+ANISOU 9758  N   GLY C 399     9087  12812  16615   -931   1708  -2648       N  
+ATOM   9759  CA  GLY C 399     -63.296  47.358 -12.917  1.00100.37           C  
+ANISOU 9759  CA  GLY C 399     9426  12286  16425   -696   1653  -2449       C  
+ATOM   9760  C   GLY C 399     -62.759  48.352 -11.905  1.00109.16           C  
+ANISOU 9760  C   GLY C 399    10752  13529  17193   -357   1683  -2096       C  
+ATOM   9761  O   GLY C 399     -61.746  48.100 -11.252  1.00112.69           O  
+ANISOU 9761  O   GLY C 399    11506  13656  17654   -306   1768  -1769       O  
+ATOM   9762  N   VAL C 400     -63.442  49.485 -11.777  1.00110.19           N  
+ANISOU 9762  N   VAL C 400    10716  14138  17015   -113   1604  -2179       N  
+ATOM   9763  CA  VAL C 400     -63.049  50.521 -10.829  1.00102.82           C  
+ANISOU 9763  CA  VAL C 400     9980  13350  15739    201   1630  -1926       C  
+ATOM   9764  C   VAL C 400     -63.196  50.004  -9.396  1.00106.18           C  
+ANISOU 9764  C   VAL C 400    10393  13753  16197      8   1931  -1563       C  
+ATOM   9765  O   VAL C 400     -62.364  50.288  -8.530  1.00107.03           O  
+ANISOU 9765  O   VAL C 400    10788  13762  16116    145   1982  -1263       O  
+ATOM   9766  CB  VAL C 400     -63.890  51.800 -11.013  1.00 92.74           C  
+ANISOU 9766  CB  VAL C 400     8512  12557  14169    519   1504  -2130       C  
+ATOM   9767  CG1 VAL C 400     -63.432  52.884 -10.050  1.00 91.91           C  
+ANISOU 9767  CG1 VAL C 400     8662  12537  13723    835   1536  -1925       C  
+ATOM   9768  CG2 VAL C 400     -63.797  52.292 -12.450  1.00 85.66           C  
+ANISOU 9768  CG2 VAL C 400     7631  11708  13208    709   1202  -2434       C  
+ATOM   9769  N   GLN C 401     -64.252  49.228  -9.162  1.00105.76           N  
+ANISOU 9769  N   GLN C 401     9996  13819  16368   -335   2126  -1588       N  
+ATOM   9770  CA  GLN C 401     -64.498  48.614  -7.859  1.00109.60           C  
+ANISOU 9770  CA  GLN C 401    10446  14301  16896   -582   2446  -1216       C  
+ATOM   9771  C   GLN C 401     -63.423  47.587  -7.509  1.00113.02           C  
+ANISOU 9771  C   GLN C 401    11221  14171  17550   -748   2533   -864       C  
+ATOM   9772  O   GLN C 401     -62.960  47.512  -6.363  1.00119.48           O  
+ANISOU 9772  O   GLN C 401    12229  14953  18213   -723   2687   -452       O  
+ATOM   9773  CB  GLN C 401     -65.877  47.946  -7.854  1.00113.65           C  
+ANISOU 9773  CB  GLN C 401    10485  15048  17648   -979   2639  -1343       C  
+ATOM   9774  CG  GLN C 401     -66.300  47.342  -6.524  1.00120.12           C  
+ANISOU 9774  CG  GLN C 401    11219  15936  18484  -1276   3009   -947       C  
+ATOM   9775  CD  GLN C 401     -66.645  48.386  -5.487  1.00119.73           C  
+ANISOU 9775  CD  GLN C 401    11101  16408  17983   -993   3127   -831       C  
+ATOM   9776  OE1 GLN C 401     -65.946  48.535  -4.486  1.00129.89           O  
+ANISOU 9776  OE1 GLN C 401    12690  17637  19025   -877   3228   -474       O  
+ATOM   9777  NE2 GLN C 401     -67.734  49.111  -5.717  1.00106.90           N  
+ANISOU 9777  NE2 GLN C 401     9066  15319  16233   -865   3110  -1150       N  
+ATOM   9778  N   SER C 402     -63.019  46.809  -8.509  1.00107.40           N  
+ANISOU 9778  N   SER C 402    10585  13041  17181   -886   2426  -1037       N  
+ATOM   9779  CA  SER C 402     -61.930  45.851  -8.349  1.00110.82           C  
+ANISOU 9779  CA  SER C 402    11347  12897  17864   -960   2479   -752       C  
+ATOM   9780  C   SER C 402     -60.622  46.559  -8.021  1.00108.96           C  
+ANISOU 9780  C   SER C 402    11453  12619  17325   -566   2335   -540       C  
+ATOM   9781  O   SER C 402     -59.876  46.137  -7.132  1.00113.58           O  
+ANISOU 9781  O   SER C 402    12261  12990  17904   -545   2437   -111       O  
+ATOM   9782  CB  SER C 402     -61.773  45.004  -9.612  1.00116.60           C  
+ANISOU 9782  CB  SER C 402    12084  13221  18998  -1130   2381  -1089       C  
+ATOM   9783  OG  SER C 402     -62.970  44.299  -9.896  1.00134.45           O  
+ANISOU 9783  OG  SER C 402    14018  15513  21554  -1557   2506  -1308       O  
+ATOM   9784  N   GLU C 403     -60.359  47.647  -8.739  1.00103.48           N  
+ANISOU 9784  N   GLU C 403    10791  12152  16376   -266   2092   -829       N  
+ATOM   9785  CA  GLU C 403     -59.160  48.443  -8.519  1.00101.02           C  
+ANISOU 9785  CA  GLU C 403    10772  11842  15771     64   1942   -686       C  
+ATOM   9786  C   GLU C 403     -59.167  49.050  -7.124  1.00 99.82           C  
+ANISOU 9786  C   GLU C 403    10684  11974  15268    162   2049   -368       C  
+ATOM   9787  O   GLU C 403     -58.117  49.218  -6.509  1.00 98.65           O  
+ANISOU 9787  O   GLU C 403    10779  11753  14951    305   2006    -96       O  
+ATOM   9788  CB  GLU C 403     -59.047  49.537  -9.584  1.00 99.15           C  
+ANISOU 9788  CB  GLU C 403    10547  11796  15329    315   1687  -1053       C  
+ATOM   9789  CG  GLU C 403     -58.642  49.017 -10.954  1.00 99.87           C  
+ANISOU 9789  CG  GLU C 403    10661  11622  15663    278   1555  -1336       C  
+ATOM   9790  CD  GLU C 403     -58.930  50.008 -12.063  1.00102.18           C  
+ANISOU 9790  CD  GLU C 403    10892  12185  15747    463   1331  -1697       C  
+ATOM   9791  OE1 GLU C 403     -59.100  51.207 -11.762  1.00105.66           O  
+ANISOU 9791  OE1 GLU C 403    11368  12919  15858    690   1252  -1681       O  
+ATOM   9792  OE2 GLU C 403     -58.984  49.586 -13.238  1.00101.96           O  
+ANISOU 9792  OE2 GLU C 403    10799  12069  15874    389   1235  -1998       O  
+ATOM   9793  N   PHE C 404     -60.359  49.364  -6.626  1.00100.95           N  
+ANISOU 9793  N   PHE C 404    10585  12483  15290     82   2190   -423       N  
+ATOM   9794  CA  PHE C 404     -60.522  49.834  -5.255  1.00101.80           C  
+ANISOU 9794  CA  PHE C 404    10723  12903  15052    141   2344   -154       C  
+ATOM   9795  C   PHE C 404     -60.146  48.745  -4.250  1.00106.30           C  
+ANISOU 9795  C   PHE C 404    11402  13264  15724    -75   2552    338       C  
+ATOM   9796  O   PHE C 404     -59.344  48.976  -3.334  1.00111.79           O  
+ANISOU 9796  O   PHE C 404    12321  14017  16139     55   2545    647       O  
+ATOM   9797  CB  PHE C 404     -61.961  50.305  -5.023  1.00111.10           C  
+ANISOU 9797  CB  PHE C 404    11559  14539  16113    104   2486   -353       C  
+ATOM   9798  CG  PHE C 404     -62.253  50.700  -3.603  1.00114.31           C  
+ANISOU 9798  CG  PHE C 404    11964  15313  16157    141   2698   -115       C  
+ATOM   9799  CD1 PHE C 404     -62.803  49.792  -2.713  1.00115.12           C  
+ANISOU 9799  CD1 PHE C 404    11924  15487  16328   -173   3005    205       C  
+ATOM   9800  CD2 PHE C 404     -61.997  51.988  -3.165  1.00112.63           C  
+ANISOU 9800  CD2 PHE C 404    11901  15371  15522    474   2603   -223       C  
+ATOM   9801  CE1 PHE C 404     -63.076  50.157  -1.409  1.00118.24           C  
+ANISOU 9801  CE1 PHE C 404    12315  16280  16332   -140   3218    420       C  
+ATOM   9802  CE2 PHE C 404     -62.269  52.359  -1.863  1.00108.60           C  
+ANISOU 9802  CE2 PHE C 404    11395  15227  14641    512   2805    -60       C  
+ATOM   9803  CZ  PHE C 404     -62.809  51.442  -0.984  1.00111.70           C  
+ANISOU 9803  CZ  PHE C 404    11630  15752  15060    213   3114    263       C  
+ATOM   9804  N   ASN C 405     -60.734  47.563  -4.427  1.00109.01           N  
+ANISOU 9804  N   ASN C 405    11590  13365  16463   -415   2728    414       N  
+ATOM   9805  CA  ASN C 405     -60.444  46.423  -3.560  1.00114.73           C  
+ANISOU 9805  CA  ASN C 405    12439  13805  17349   -637   2940    922       C  
+ATOM   9806  C   ASN C 405     -58.948  46.135  -3.485  1.00120.38           C  
+ANISOU 9806  C   ASN C 405    13496  14156  18087   -432   2787   1196       C  
+ATOM   9807  O   ASN C 405     -58.368  46.045  -2.396  1.00119.30           O  
+ANISOU 9807  O   ASN C 405    13531  14085  17714   -359   2845   1643       O  
+ATOM   9808  CB  ASN C 405     -61.185  45.177  -4.050  1.00117.55           C  
+ANISOU 9808  CB  ASN C 405    12624  13811  18226  -1051   3114    885       C  
+ATOM   9809  CG  ASN C 405     -62.690  45.351  -4.039  1.00124.60           C  
+ANISOU 9809  CG  ASN C 405    13109  15119  19113  -1304   3286    652       C  
+ATOM   9810  OD1 ASN C 405     -63.238  46.074  -3.206  1.00124.22           O  
+ANISOU 9810  OD1 ASN C 405    12928  15588  18683  -1228   3405    721       O  
+ATOM   9811  ND2 ASN C 405     -63.368  44.687  -4.968  1.00127.43           N  
+ANISOU 9811  ND2 ASN C 405    13247  15282  19889  -1605   3300    344       N  
+ATOM   9812  N   ILE C 406     -58.332  45.996  -4.655  1.00122.92           N  
+ANISOU 9812  N   ILE C 406    13888  14145  18670   -330   2589    917       N  
+ATOM   9813  CA  ILE C 406     -56.899  45.756  -4.751  1.00117.25           C  
+ANISOU 9813  CA  ILE C 406    13430  13115  18003   -106   2435   1106       C  
+ATOM   9814  C   ILE C 406     -56.116  46.893  -4.096  1.00111.60           C  
+ANISOU 9814  C   ILE C 406    12847  12779  16778    186   2276   1212       C  
+ATOM   9815  O   ILE C 406     -55.114  46.656  -3.420  1.00113.30           O  
+ANISOU 9815  O   ILE C 406    13234  12923  16891    317   2231   1589       O  
+ATOM   9816  CB  ILE C 406     -56.453  45.591  -6.220  1.00117.56           C  
+ANISOU 9816  CB  ILE C 406    13482  12842  18344    -32   2264    695       C  
+ATOM   9817  CG1 ILE C 406     -57.174  44.405  -6.864  1.00119.53           C  
+ANISOU 9817  CG1 ILE C 406    13622  12687  19108   -351   2412    542       C  
+ATOM   9818  CG2 ILE C 406     -54.948  45.398  -6.308  1.00116.03           C  
+ANISOU 9818  CG2 ILE C 406    13506  12396  18186    229   2123    874       C  
+ATOM   9819  CD1 ILE C 406     -56.999  44.323  -8.365  1.00116.26           C  
+ANISOU 9819  CD1 ILE C 406    13175  12076  18921   -317   2256     34       C  
+ATOM   9820  N   SER C 407     -56.582  48.123  -4.299  1.00112.31           N  
+ANISOU 9820  N   SER C 407    12853  13265  16556    290   2183    873       N  
+ATOM   9821  CA  SER C 407     -55.946  49.293  -3.698  1.00111.58           C  
+ANISOU 9821  CA  SER C 407    12897  13509  15987    523   2041    898       C  
+ATOM   9822  C   SER C 407     -55.893  49.208  -2.176  1.00114.18           C  
+ANISOU 9822  C   SER C 407    13296  14093  15995    493   2178   1328       C  
+ATOM   9823  O   SER C 407     -54.858  49.492  -1.575  1.00111.51           O  
+ANISOU 9823  O   SER C 407    13126  13848  15396    639   2050   1543       O  
+ATOM   9824  CB  SER C 407     -56.671  50.575  -4.114  1.00103.75           C  
+ANISOU 9824  CB  SER C 407    11817  12843  14760    632   1964    470       C  
+ATOM   9825  OG  SER C 407     -56.475  50.850  -5.490  1.00102.43           O  
+ANISOU 9825  OG  SER C 407    11643  12503  14773    714   1783    117       O  
+ATOM   9826  N   PHE C 408     -57.000  48.822  -1.547  1.00117.60           N  
+ANISOU 9826  N   PHE C 408    13579  14684  16418    291   2436   1455       N  
+ATOM   9827  CA  PHE C 408     -57.021  48.785  -0.085  1.00119.93           C  
+ANISOU 9827  CA  PHE C 408    13937  15295  16335    256   2590   1864       C  
+ATOM   9828  C   PHE C 408     -56.340  47.539   0.469  1.00118.96           C  
+ANISOU 9828  C   PHE C 408    13949  14865  16385    172   2659   2434       C  
+ATOM   9829  O   PHE C 408     -55.783  47.568   1.568  1.00121.77           O  
+ANISOU 9829  O   PHE C 408    14438  15451  16377    246   2656   2821       O  
+ATOM   9830  CB  PHE C 408     -58.443  48.864   0.466  1.00125.29           C  
+ANISOU 9830  CB  PHE C 408    14390  16328  16888     71   2878   1820       C  
+ATOM   9831  CG  PHE C 408     -58.523  48.618   1.951  1.00132.85           C  
+ANISOU 9831  CG  PHE C 408    15405  17608  17464    -14   3090   2289       C  
+ATOM   9832  CD1 PHE C 408     -58.163  49.611   2.848  1.00131.00           C  
+ANISOU 9832  CD1 PHE C 408    15292  17833  16650    179   3023   2274       C  
+ATOM   9833  CD2 PHE C 408     -58.948  47.396   2.448  1.00136.32           C  
+ANISOU 9833  CD2 PHE C 408    15796  17891  18109   -303   3358   2744       C  
+ATOM   9834  CE1 PHE C 408     -58.227  49.393   4.214  1.00132.99           C  
+ANISOU 9834  CE1 PHE C 408    15600  18446  16485    104   3212   2694       C  
+ATOM   9835  CE2 PHE C 408     -59.014  47.172   3.813  1.00136.61           C  
+ANISOU 9835  CE2 PHE C 408    15899  18261  17746   -382   3560   3220       C  
+ATOM   9836  CZ  PHE C 408     -58.654  48.171   4.696  1.00135.66           C  
+ANISOU 9836  CZ  PHE C 408    15883  18661  16999   -169   3483   3190       C  
+ATOM   9837  N   GLU C 409     -56.366  46.449  -0.291  1.00119.84           N  
+ANISOU 9837  N   GLU C 409    14038  14452  17044     35   2709   2481       N  
+ATOM   9838  CA  GLU C 409     -55.735  45.221   0.175  1.00125.87           C  
+ANISOU 9838  CA  GLU C 409    14956  14828  18040     -6   2781   3033       C  
+ATOM   9839  C   GLU C 409     -54.212  45.386   0.149  1.00128.88           C  
+ANISOU 9839  C   GLU C 409    15515  15129  18324    318   2500   3164       C  
+ATOM   9840  O   GLU C 409     -53.481  44.623   0.781  1.00139.02           O  
+ANISOU 9840  O   GLU C 409    16937  16241  19644    402   2498   3680       O  
+ATOM   9841  CB  GLU C 409     -56.202  44.026  -0.677  1.00127.22           C  
+ANISOU 9841  CB  GLU C 409    15074  14400  18862   -247   2920   2978       C  
+ATOM   9842  CG  GLU C 409     -55.139  42.991  -1.032  1.00134.44           C  
+ANISOU 9842  CG  GLU C 409    16181  14704  20195   -118   2840   3232       C  
+ATOM   9843  CD  GLU C 409     -55.686  41.862  -1.883  1.00140.64           C  
+ANISOU 9843  CD  GLU C 409    16936  14876  21623   -385   2993   3090       C  
+ATOM   9844  OE1 GLU C 409     -56.921  41.798  -2.059  1.00147.11           O  
+ANISOU 9844  OE1 GLU C 409    17565  15780  22550   -723   3174   2872       O  
+ATOM   9845  OE2 GLU C 409     -54.883  41.042  -2.377  1.00136.35           O  
+ANISOU 9845  OE2 GLU C 409    16544  13780  21483   -256   2934   3169       O  
+ATOM   9846  N   GLN C 410     -53.742  46.435  -0.516  1.00121.88           N  
+ANISOU 9846  N   GLN C 410    14612  14417  17281    504   2264   2726       N  
+ATOM   9847  CA  GLN C 410     -52.309  46.697  -0.607  1.00119.79           C  
+ANISOU 9847  CA  GLN C 410    14457  14144  16914    773   1999   2793       C  
+ATOM   9848  C   GLN C 410     -51.935  47.843   0.332  1.00125.61           C  
+ANISOU 9848  C   GLN C 410    15246  15455  17026    880   1868   2819       C  
+ATOM   9849  O   GLN C 410     -50.831  48.392   0.275  1.00125.09           O  
+ANISOU 9849  O   GLN C 410    15231  15514  16781   1060   1626   2770       O  
+ATOM   9850  CB  GLN C 410     -51.907  47.030  -2.039  1.00115.14           C  
+ANISOU 9850  CB  GLN C 410    13828  13332  16588    870   1834   2309       C  
+ATOM   9851  N   ASN C 411     -52.886  48.173   1.200  1.00129.41           N  
+ANISOU 9851  N   ASN C 411    15698  16292  17181    746   2046   2874       N  
+ATOM   9852  CA  ASN C 411     -52.831  49.302   2.113  1.00128.28           C  
+ANISOU 9852  CA  ASN C 411    15605  16708  16427    808   1979   2797       C  
+ATOM   9853  C   ASN C 411     -52.424  50.574   1.328  1.00115.49           C  
+ANISOU 9853  C   ASN C 411    14009  15165  14706    937   1745   2260       C  
+ATOM   9854  O   ASN C 411     -51.378  51.190   1.569  1.00114.52           O  
+ANISOU 9854  O   ASN C 411    13980  15219  14313   1055   1517   2245       O  
+ATOM   9855  CB  ASN C 411     -51.887  48.994   3.289  1.00136.87           C  
+ANISOU 9855  CB  ASN C 411    16805  18034  17164    896   1887   3316       C  
+ATOM   9856  CG  ASN C 411     -51.582  50.208   4.139  1.00137.82           C  
+ANISOU 9856  CG  ASN C 411    16996  18727  16640    962   1752   3159       C  
+ATOM   9857  OD1 ASN C 411     -52.359  51.162   4.171  1.00135.52           O  
+ANISOU 9857  OD1 ASN C 411    16688  18678  16124    921   1830   2754       O  
+ATOM   9858  ND2 ASN C 411     -50.436  50.194   4.811  1.00136.79           N  
+ANISOU 9858  ND2 ASN C 411    16939  18818  16218   1076   1539   3453       N  
+ATOM   9859  N   ASN C 412     -53.200  50.901   0.299  1.00112.35           N  
+ANISOU 9859  N   ASN C 412    13521  14604  14562    901   1789   1838       N  
+ATOM   9860  CA  ASN C 412     -53.031  52.201  -0.356  1.00110.26           C  
+ANISOU 9860  CA  ASN C 412    13308  14431  14156   1015   1608   1365       C  
+ATOM   9861  C   ASN C 412     -54.185  53.114   0.101  1.00116.96           C  
+ANISOU 9861  C   ASN C 412    14119  15618  14704   1013   1744   1096       C  
+ATOM   9862  O   ASN C 412     -55.287  52.638   0.360  1.00121.25           O  
+ANISOU 9862  O   ASN C 412    14511  16236  15324    904   1983   1155       O  
+ATOM   9863  CB  ASN C 412     -52.968  52.030  -1.887  1.00108.32           C  
+ANISOU 9863  CB  ASN C 412    13003  13803  14351   1036   1523   1086       C  
+ATOM   9864  CG  ASN C 412     -51.754  51.194  -2.337  1.00115.38           C  
+ANISOU 9864  CG  ASN C 412    13928  14388  15524   1084   1404   1302       C  
+ATOM   9865  OD1 ASN C 412     -50.946  50.752  -1.510  1.00118.58           O  
+ANISOU 9865  OD1 ASN C 412    14384  14859  15811   1126   1362   1682       O  
+ATOM   9866  ND2 ASN C 412     -51.584  51.049  -3.649  1.00120.22           N  
+ANISOU 9866  ND2 ASN C 412    14500  14709  16467   1110   1335   1044       N  
+ATOM   9867  N   TYR C 413     -53.933  54.415   0.235  1.00112.50           N  
+ANISOU 9867  N   TYR C 413    13685  15256  13805   1131   1607    799       N  
+ATOM   9868  CA  TYR C 413     -54.997  55.328   0.670  1.00105.89           C  
+ANISOU 9868  CA  TYR C 413    12825  14714  12693   1194   1740    509       C  
+ATOM   9869  C   TYR C 413     -56.013  55.489  -0.446  1.00102.27           C  
+ANISOU 9869  C   TYR C 413    12208  14093  12555   1243   1791    191       C  
+ATOM   9870  O   TYR C 413     -55.663  55.809  -1.579  1.00108.98           O  
+ANISOU 9870  O   TYR C 413    13105  14681  13622   1312   1613    -14       O  
+ATOM   9871  CB  TYR C 413     -54.453  56.698   1.103  1.00110.52           C  
+ANISOU 9871  CB  TYR C 413    13636  15489  12866   1311   1582    242       C  
+ATOM   9872  CG  TYR C 413     -53.634  56.673   2.381  1.00115.16           C  
+ANISOU 9872  CG  TYR C 413    14347  16382  13025   1253   1534    493       C  
+ATOM   9873  CD1 TYR C 413     -54.199  56.292   3.598  1.00121.44           C  
+ANISOU 9873  CD1 TYR C 413    15087  17552  13503   1197   1752    717       C  
+ATOM   9874  CD2 TYR C 413     -52.291  57.021   2.368  1.00111.65           C  
+ANISOU 9874  CD2 TYR C 413    14051  15900  12469   1241   1268    515       C  
+ATOM   9875  CE1 TYR C 413     -53.440  56.268   4.762  1.00122.94           C  
+ANISOU 9875  CE1 TYR C 413    15390  18079  13244   1151   1683    958       C  
+ATOM   9876  CE2 TYR C 413     -51.533  56.997   3.519  1.00114.09           C  
+ANISOU 9876  CE2 TYR C 413    14439  16548  12362   1187   1186    734       C  
+ATOM   9877  CZ  TYR C 413     -52.108  56.621   4.713  1.00119.61           C  
+ANISOU 9877  CZ  TYR C 413    15103  17624  12720   1153   1382    958       C  
+ATOM   9878  OH  TYR C 413     -51.335  56.603   5.853  1.00122.76           O  
+ANISOU 9878  OH  TYR C 413    15580  18414  12650   1107   1275   1185       O  
+ATOM   9879  N   VAL C 414     -57.281  55.279  -0.124  1.00100.96           N  
+ANISOU 9879  N   VAL C 414    11833  14135  12394   1203   2034    156       N  
+ATOM   9880  CA  VAL C 414     -58.313  55.308  -1.147  1.00100.64           C  
+ANISOU 9880  CA  VAL C 414    11570  14010  12657   1237   2073   -122       C  
+ATOM   9881  C   VAL C 414     -59.075  56.627  -1.099  1.00 99.95           C  
+ANISOU 9881  C   VAL C 414    11475  14168  12334   1483   2083   -511       C  
+ATOM   9882  O   VAL C 414     -59.682  56.981  -0.088  1.00100.43           O  
+ANISOU 9882  O   VAL C 414    11484  14585  12090   1534   2274   -543       O  
+ATOM   9883  CB  VAL C 414     -59.292  54.124  -0.999  1.00104.36           C  
+ANISOU 9883  CB  VAL C 414    11742  14536  13376   1004   2335     69       C  
+ATOM   9884  CG1 VAL C 414     -58.691  52.857  -1.595  1.00103.96           C  
+ANISOU 9884  CG1 VAL C 414    11696  14070  13733    806   2288    322       C  
+ATOM   9885  CG2 VAL C 414     -59.666  53.905   0.460  1.00114.20           C  
+ANISOU 9885  CG2 VAL C 414    12948  16153  14289    906   2598    335       C  
+ATOM   9886  N   VAL C 415     -59.042  57.346  -2.215  1.00 87.48           N  
+ANISOU 9886  N   VAL C 415     9954  12392  10892   1656   1884   -802       N  
+ATOM   9887  CA  VAL C 415     -59.653  58.664  -2.312  1.00 83.63           C  
+ANISOU 9887  CA  VAL C 415     9514  12033  10227   1950   1852  -1160       C  
+ATOM   9888  C   VAL C 415     -60.664  58.706  -3.456  1.00 90.10           C  
+ANISOU 9888  C   VAL C 415    10071  12837  11326   2071   1816  -1379       C  
+ATOM   9889  O   VAL C 415     -60.325  59.075  -4.584  1.00 92.59           O  
+ANISOU 9889  O   VAL C 415    10492  12902  11785   2170   1594  -1500       O  
+ATOM   9890  CB  VAL C 415     -58.589  59.763  -2.524  1.00 84.50           C  
+ANISOU 9890  CB  VAL C 415    10014  11918  10173   2085   1613  -1292       C  
+ATOM   9891  CG1 VAL C 415     -59.222  61.147  -2.448  1.00 82.96           C  
+ANISOU 9891  CG1 VAL C 415     9929  11798   9793   2406   1609  -1643       C  
+ATOM   9892  CG2 VAL C 415     -57.486  59.634  -1.489  1.00 91.62           C  
+ANISOU 9892  CG2 VAL C 415    11132  12871  10810   1929   1597  -1078       C  
+ATOM   9893  N   PRO C 416     -61.911  58.304  -3.170  1.00 97.35           N  
+ANISOU 9893  N   PRO C 416    10620  14067  12300   2046   2036  -1420       N  
+ATOM   9894  CA  PRO C 416     -62.986  58.338  -4.165  1.00 94.02           C  
+ANISOU 9894  CA  PRO C 416     9870  13740  12112   2161   1997  -1645       C  
+ATOM   9895  C   PRO C 416     -63.668  59.701  -4.256  1.00 88.09           C  
+ANISOU 9895  C   PRO C 416     9125  13154  11193   2595   1950  -1963       C  
+ATOM   9896  O   PRO C 416     -64.241  60.181  -3.277  1.00 80.10           O  
+ANISOU 9896  O   PRO C 416     8044  12442   9947   2746   2150  -2055       O  
+ATOM   9897  CB  PRO C 416     -63.956  57.277  -3.648  1.00 87.52           C  
+ANISOU 9897  CB  PRO C 416     8627  13215  11411   1894   2281  -1524       C  
+ATOM   9898  CG  PRO C 416     -63.789  57.337  -2.165  1.00 90.92           C  
+ANISOU 9898  CG  PRO C 416     9171  13863  11511   1845   2514  -1350       C  
+ATOM   9899  CD  PRO C 416     -62.330  57.636  -1.926  1.00 93.77           C  
+ANISOU 9899  CD  PRO C 416    10002  13921  11704   1853   2336  -1210       C  
+ATOM   9900  N   VAL C 417     -63.606  60.314  -5.434  1.00 86.08           N  
+ANISOU 9900  N   VAL C 417     8959  12700  11048   2814   1694  -2123       N  
+ATOM   9901  CA  VAL C 417     -64.262  61.596  -5.664  1.00 79.37           C  
+ANISOU 9901  CA  VAL C 417     8133  11935  10088   3276   1621  -2391       C  
+ATOM   9902  C   VAL C 417     -65.716  61.379  -6.061  1.00 87.13           C  
+ANISOU 9902  C   VAL C 417     8578  13310  11217   3412   1690  -2546       C  
+ATOM   9903  O   VAL C 417     -66.018  61.175  -7.238  1.00 93.12           O  
+ANISOU 9903  O   VAL C 417     9160  14051  12170   3436   1497  -2600       O  
+ATOM   9904  CB  VAL C 417     -63.550  62.399  -6.759  1.00 84.65           C  
+ANISOU 9904  CB  VAL C 417     9159  12219  10786   3462   1314  -2439       C  
+ATOM   9905  CG1 VAL C 417     -64.144  63.803  -6.862  1.00 97.06           C  
+ANISOU 9905  CG1 VAL C 417    10845  13792  12241   3973   1249  -2672       C  
+ATOM   9906  CG2 VAL C 417     -62.060  62.464  -6.469  1.00 69.28           C  
+ANISOU 9906  CG2 VAL C 417     7666   9924   8735   3247   1241  -2278       C  
+ATOM   9907  N   GLY C 418     -66.614  61.424  -5.080  1.00 99.97           N  
+ANISOU 9907  N   GLY C 418     9920  15338  12726   3493   1964  -2629       N  
+ATOM   9908  CA  GLY C 418     -68.015  61.142  -5.334  1.00 96.80           C  
+ANISOU 9908  CA  GLY C 418     8925  15392  12461   3576   2063  -2771       C  
+ATOM   9909  C   GLY C 418     -68.803  62.205  -6.078  1.00 99.28           C  
+ANISOU 9909  C   GLY C 418     9105  15829  12788   4123   1887  -3031       C  
+ATOM   9910  O   GLY C 418     -69.892  61.923  -6.580  1.00109.78           O  
+ANISOU 9910  O   GLY C 418     9936  17509  14267   4153   1868  -3118       O  
+ATOM   9911  N   ALA C 419     -68.267  63.420  -6.171  1.00102.51           N  
+ANISOU 9911  N   ALA C 419    10007  15888  13055   4476   1725  -3090       N  
+ATOM   9912  CA  ALA C 419     -68.976  64.474  -6.889  1.00102.13           C  
+ANISOU 9912  CA  ALA C 419     9999  15767  13037   4859   1503  -3162       C  
+ATOM   9913  C   ALA C 419     -68.920  64.218  -8.388  1.00100.46           C  
+ANISOU 9913  C   ALA C 419     9707  15469  12996   4850   1186  -3111       C  
+ATOM   9914  O   ALA C 419     -69.919  64.350  -9.095  1.00109.51           O  
+ANISOU 9914  O   ALA C 419    10523  16864  14222   5019   1049  -3160       O  
+ATOM   9915  CB  ALA C 419     -68.387  65.838  -6.559  1.00 93.13           C  
+ANISOU 9915  CB  ALA C 419     9453  14198  11732   5144   1431  -3198       C  
+ATOM   9916  N   THR C 420     -67.737  63.844  -8.859  1.00 99.80           N  
+ANISOU 9916  N   THR C 420     9918  15062  12940   4657   1068  -3024       N  
+ATOM   9917  CA  THR C 420     -67.536  63.459 -10.246  1.00120.30           C  
+ANISOU 9917  CA  THR C 420    12448  17593  15666   4596    794  -2994       C  
+ATOM   9918  C   THR C 420     -67.547  61.944 -10.339  1.00104.21           C  
+ANISOU 9918  C   THR C 420    10068  15716  13810   4057    886  -2938       C  
+ATOM   9919  O   THR C 420     -66.523  61.337 -10.655  1.00 78.51           O  
+ANISOU 9919  O   THR C 420     7074  12143  10612   3712    826  -2796       O  
+ATOM   9920  CB  THR C 420     -66.206  64.003 -10.807  1.00120.43           C  
+ANISOU 9920  CB  THR C 420    13071  17080  15606   4600    596  -2867       C  
+ATOM   9921  N   GLY C 421     -68.686  61.323 -10.053  1.00103.46           N  
+ANISOU 9921  N   GLY C 421     9397  16090  13822   3961   1044  -3042       N  
+ATOM   9922  CA  GLY C 421     -68.686  59.879  -9.966  1.00106.14           C  
+ANISOU 9922  CA  GLY C 421     9471  16498  14358   3388   1180  -2965       C  
+ATOM   9923  C   GLY C 421     -69.972  59.082  -9.923  1.00100.90           C  
+ANISOU 9923  C   GLY C 421     8127  16347  13865   3181   1319  -3091       C  
+ATOM   9924  O   GLY C 421     -71.032  59.550  -9.509  1.00 91.59           O  
+ANISOU 9924  O   GLY C 421     6562  15611  12627   3457   1432  -3228       O  
+ATOM   9925  N   TYR C 422     -69.829  57.841 -10.371  1.00110.62           N  
+ANISOU 9925  N   TYR C 422     9212  17495  15323   2672   1316  -3055       N  
+ATOM   9926  CA  TYR C 422     -70.859  56.814 -10.350  1.00110.31           C  
+ANISOU 9926  CA  TYR C 422     8569  17837  15506   2284   1464  -3152       C  
+ATOM   9927  C   TYR C 422     -70.418  55.733  -9.374  1.00110.40           C  
+ANISOU 9927  C   TYR C 422     8680  17624  15642   1763   1785  -2911       C  
+ATOM   9928  O   TYR C 422     -70.927  55.647  -8.254  1.00115.73           O  
+ANISOU 9928  O   TYR C 422     9160  18558  16255   1687   2101  -2820       O  
+ATOM   9929  CB  TYR C 422     -71.095  56.234 -11.747  1.00100.62           C  
+ANISOU 9929  CB  TYR C 422     7109  16662  14459   2096   1182  -3344       C  
+ATOM   9930  CG  TYR C 422     -71.532  57.242 -12.787  1.00 96.84           C  
+ANISOU 9930  CG  TYR C 422     6527  16439  13827   2612    833  -3532       C  
+ATOM   9931  CD1 TYR C 422     -70.668  58.224 -13.265  1.00 95.64           C  
+ANISOU 9931  CD1 TYR C 422     6910  15955  13472   3018    606  -3451       C  
+ATOM   9932  CD2 TYR C 422     -72.814  57.188 -13.314  1.00100.19           C  
+ANISOU 9932  CD2 TYR C 422     6303  17454  14309   2677    723  -3772       C  
+ATOM   9933  CE1 TYR C 422     -71.088  59.137 -14.214  1.00 99.11           C  
+ANISOU 9933  CE1 TYR C 422     7281  16612  13766   3500    291  -3564       C  
+ATOM   9934  CE2 TYR C 422     -73.235  58.087 -14.265  1.00106.89           C  
+ANISOU 9934  CE2 TYR C 422     7128  18506  14980   3142    376  -3858       C  
+ATOM   9935  CZ  TYR C 422     -72.370  59.057 -14.713  1.00103.89           C  
+ANISOU 9935  CZ  TYR C 422     7299  17773  14402   3569    167  -3748       C  
+ATOM   9936  OH  TYR C 422     -72.798  59.950 -15.663  1.00107.17           O  
+ANISOU 9936  OH  TYR C 422     7759  18337  14623   3997   -169  -3754       O  
+ATOM   9937  N   ILE C 423     -69.475  54.907  -9.817  1.00104.95           N  
+ANISOU 9937  N   ILE C 423     8294  16466  15117   1425   1709  -2799       N  
+ATOM   9938  CA  ILE C 423     -68.856  53.912  -8.955  1.00107.16           C  
+ANISOU 9938  CA  ILE C 423     8769  16428  15518    998   1971  -2510       C  
+ATOM   9939  C   ILE C 423     -68.013  54.647  -7.917  1.00104.45           C  
+ANISOU 9939  C   ILE C 423     8879  15927  14881   1254   2068  -2279       C  
+ATOM   9940  O   ILE C 423     -67.915  54.231  -6.762  1.00101.49           O  
+ANISOU 9940  O   ILE C 423     8548  15563  14450   1055   2352  -2032       O  
+ATOM   9941  CB  ILE C 423     -67.986  52.922  -9.775  1.00 97.64           C  
+ANISOU 9941  CB  ILE C 423     7800  14727  14573    668   1839  -2478       C  
+ATOM   9942  CG1 ILE C 423     -68.864  51.855 -10.451  1.00100.81           C  
+ANISOU 9942  CG1 ILE C 423     7741  15256  15307    233   1852  -2687       C  
+ATOM   9943  CG2 ILE C 423     -66.875  52.318  -8.924  1.00 91.59           C  
+ANISOU 9943  CG2 ILE C 423     7451  13511  13838    467   2013  -2116       C  
+ATOM   9944  CD1 ILE C 423     -69.422  50.825  -9.501  1.00107.29           C  
+ANISOU 9944  CD1 ILE C 423     8308  16118  16339   -251   2216  -2504       C  
+ATOM   9945  N   ALA C 424     -67.433  55.765  -8.342  1.00105.25           N  
+ANISOU 9945  N   ALA C 424     9311  15902  14776   1682   1828  -2362       N  
+ATOM   9946  CA  ALA C 424     -66.716  56.673  -7.450  1.00100.51           C  
+ANISOU 9946  CA  ALA C 424     9123  15189  13876   1954   1877  -2235       C  
+ATOM   9947  C   ALA C 424     -67.586  57.104  -6.274  1.00100.70           C  
+ANISOU 9947  C   ALA C 424     8916  15642  13703   2093   2156  -2257       C  
+ATOM   9948  O   ALA C 424     -67.152  57.064  -5.126  1.00 98.61           O  
+ANISOU 9948  O   ALA C 424     8854  15360  13252   2013   2361  -2063       O  
+ATOM   9949  CB  ALA C 424     -66.223  57.888  -8.214  1.00 97.83           C  
+ANISOU 9949  CB  ALA C 424     9104  14681  13384   2383   1580  -2372       C  
+ATOM   9950  N   LYS C 425     -68.810  57.528  -6.572  1.00106.53           N  
+ANISOU 9950  N   LYS C 425     9213  16807  14458   2322   2159  -2503       N  
+ATOM   9951  CA  LYS C 425     -69.770  57.904  -5.539  1.00114.11           C  
+ANISOU 9951  CA  LYS C 425     9859  18251  15245   2476   2450  -2574       C  
+ATOM   9952  C   LYS C 425     -70.024  56.726  -4.599  1.00126.42           C  
+ANISOU 9952  C   LYS C 425    11191  19971  16870   1962   2807  -2338       C  
+ATOM   9953  O   LYS C 425     -70.051  56.883  -3.374  1.00126.83           O  
+ANISOU 9953  O   LYS C 425    11303  20215  16671   1971   3088  -2221       O  
+ATOM   9954  CB  LYS C 425     -71.082  58.381  -6.166  1.00100.06           C  
+ANISOU 9954  CB  LYS C 425     7544  16940  13536   2788   2375  -2872       C  
+ATOM   9955  N   ASP C 426     -70.208  55.548  -5.192  1.00127.93           N  
+ANISOU 9955  N   ASP C 426    11143  20074  17392   1504   2797  -2272       N  
+ATOM   9956  CA  ASP C 426     -70.426  54.307  -4.452  1.00119.73           C  
+ANISOU 9956  CA  ASP C 426     9919  19081  16491    954   3122  -2008       C  
+ATOM   9957  C   ASP C 426     -69.308  54.063  -3.440  1.00109.00           C  
+ANISOU 9957  C   ASP C 426     9067  17402  14947    834   3256  -1637       C  
+ATOM   9958  O   ASP C 426     -69.558  53.639  -2.311  1.00118.90           O  
+ANISOU 9958  O   ASP C 426    10236  18872  16067    613   3593  -1396       O  
+ATOM   9959  CB  ASP C 426     -70.543  53.122  -5.415  1.00113.11           C  
+ANISOU 9959  CB  ASP C 426     8888  18012  16077    490   3024  -2026       C  
+ATOM   9960  CG  ASP C 426     -71.845  53.129  -6.198  1.00116.56           C  
+ANISOU 9960  CG  ASP C 426     8691  18911  16684    475   2956  -2367       C  
+ATOM   9961  OD1 ASP C 426     -72.460  54.210  -6.346  1.00118.09           O  
+ANISOU 9961  OD1 ASP C 426     8674  19507  16687    958   2859  -2609       O  
+ATOM   9962  OD2 ASP C 426     -72.265  52.045  -6.655  1.00123.00           O  
+ANISOU 9962  OD2 ASP C 426     9211  19690  17832    -20   2996  -2399       O  
+ATOM   9963  N   LEU C 427     -68.076  54.330  -3.865  1.00 97.26           N  
+ANISOU 9963  N   LEU C 427     8082  15440  13431    978   2987  -1582       N  
+ATOM   9964  CA  LEU C 427     -66.903  54.161  -3.018  1.00103.08           C  
+ANISOU 9964  CA  LEU C 427     9290  15891  13987    907   3040  -1249       C  
+ATOM   9965  C   LEU C 427     -66.829  55.273  -1.980  1.00106.25           C  
+ANISOU 9965  C   LEU C 427     9866  16575  13929   1251   3137  -1290       C  
+ATOM   9966  O   LEU C 427     -66.284  55.077  -0.897  1.00107.28           O  
+ANISOU 9966  O   LEU C 427    10223  16724  13817   1143   3297  -1011       O  
+ATOM   9967  CB  LEU C 427     -65.630  54.130  -3.864  1.00 99.93           C  
+ANISOU 9967  CB  LEU C 427     9303  14954  13710    955   2719  -1217       C  
+ATOM   9968  CG  LEU C 427     -65.575  53.066  -4.962  1.00 98.62           C  
+ANISOU 9968  CG  LEU C 427     9025  14468  13978    651   2607  -1238       C  
+ATOM   9969  CD1 LEU C 427     -64.377  53.310  -5.860  1.00100.62           C  
+ANISOU 9969  CD1 LEU C 427     9657  14296  14277    802   2294  -1285       C  
+ATOM   9970  CD2 LEU C 427     -65.531  51.659  -4.379  1.00 99.92           C  
+ANISOU 9970  CD2 LEU C 427     9141  14453  14370    180   2857   -892       C  
+ATOM   9971  N   TRP C 428     -67.350  56.447  -2.326  1.00108.84           N  
+ANISOU 9971  N   TRP C 428    10112  17110  14133   1681   3027  -1644       N  
+ATOM   9972  CA  TRP C 428     -67.419  57.553  -1.379  1.00103.44           C  
+ANISOU 9972  CA  TRP C 428     9577  16687  13040   2034   3138  -1772       C  
+ATOM   9973  C   TRP C 428     -68.342  57.180  -0.222  1.00105.96           C  
+ANISOU 9973  C   TRP C 428     9543  17538  13180   1881   3556  -1685       C  
+ATOM   9974  O   TRP C 428     -68.083  57.531   0.928  1.00107.00           O  
+ANISOU 9974  O   TRP C 428     9871  17856  12928   1946   3738  -1611       O  
+ATOM   9975  CB  TRP C 428     -67.902  58.832  -2.068  1.00 95.36           C  
+ANISOU 9975  CB  TRP C 428     8518  15727  11989   2554   2947  -2168       C  
+ATOM   9976  N   ASN C 429     -69.410  56.451  -0.534  1.00113.60           N  
+ANISOU 9976  N   ASN C 429     9977  18777  14408   1647   3712  -1699       N  
+ATOM   9977  CA  ASN C 429     -70.292  55.932   0.502  1.00115.11           C  
+ANISOU 9977  CA  ASN C 429     9788  19481  14467   1404   4143  -1564       C  
+ATOM   9978  C   ASN C 429     -69.669  54.730   1.205  1.00114.82           C  
+ANISOU 9978  C   ASN C 429     9940  19251  14437    891   4323  -1066       C  
+ATOM   9979  O   ASN C 429     -69.919  54.489   2.383  1.00115.71           O  
+ANISOU 9979  O   ASN C 429     9990  19716  14258    737   4668   -847       O  
+ATOM   9980  CB  ASN C 429     -71.658  55.556  -0.077  1.00120.62           C  
+ANISOU 9980  CB  ASN C 429     9808  20565  15458   1281   4251  -1751       C  
+ATOM   9981  CG  ASN C 429     -72.451  56.764  -0.531  1.00125.94           C  
+ANISOU 9981  CG  ASN C 429    10215  21572  16064   1853   4137  -2203       C  
+ATOM   9982  OD1 ASN C 429     -72.326  57.850   0.036  1.00129.16           O  
+ANISOU 9982  OD1 ASN C 429    10845  22095  16137   2309   4167  -2372       O  
+ATOM   9983  ND2 ASN C 429     -73.266  56.584  -1.564  1.00122.90           N  
+ANISOU 9983  ND2 ASN C 429     9361  21337  15997   1844   3994  -2409       N  
+ATOM   9984  N   LYS C 430     -68.857  53.970   0.481  1.00113.88           N  
+ANISOU 9984  N   LYS C 430    10056  18575  14639    647   4096   -877       N  
+ATOM   9985  CA  LYS C 430     -68.154  52.845   1.085  1.00121.59           C  
+ANISOU 9985  CA  LYS C 430    11266  19275  15656    232   4226   -378       C  
+ATOM   9986  C   LYS C 430     -67.120  53.327   2.101  1.00124.24           C  
+ANISOU 9986  C   LYS C 430    12077  19596  15533    411   4212   -170       C  
+ATOM   9987  O   LYS C 430     -66.774  52.606   3.037  1.00122.72           O  
+ANISOU 9987  O   LYS C 430    12018  19425  15186    148   4412    269       O  
+ATOM   9988  CB  LYS C 430     -67.478  51.992   0.010  1.00119.05           C  
+ANISOU 9988  CB  LYS C 430    11100  18335  15801      8   3971   -286       C  
+ATOM   9989  N   VAL C 431     -66.633  54.550   1.909  1.00126.43           N  
+ANISOU 9989  N   VAL C 431    12611  19840  15587    848   3967   -481       N  
+ATOM   9990  CA  VAL C 431     -65.621  55.127   2.788  1.00120.28           C  
+ANISOU 9990  CA  VAL C 431    12276  19058  14368   1013   3903   -373       C  
+ATOM   9991  C   VAL C 431     -66.227  55.963   3.913  1.00123.70           C  
+ANISOU 9991  C   VAL C 431    12636  20068  14296   1228   4164   -548       C  
+ATOM   9992  O   VAL C 431     -65.780  55.883   5.056  1.00126.76           O  
+ANISOU 9992  O   VAL C 431    13227  20667  14270   1150   4305   -306       O  
+ATOM   9993  CB  VAL C 431     -64.630  56.002   1.997  1.00104.46           C  
+ANISOU 9993  CB  VAL C 431    10642  16650  12397   1311   3497   -612       C  
+ATOM   9994  N   ASN C 432     -67.234  56.771   3.589  1.00117.52           N  
+ANISOU 9994  N   ASN C 432    11561  19562  13528   1525   4223   -979       N  
+ATOM   9995  CA  ASN C 432     -67.896  57.596   4.595  1.00119.63           C  
+ANISOU 9995  CA  ASN C 432    11725  20385  13343   1784   4497  -1218       C  
+ATOM   9996  C   ASN C 432     -68.550  56.698   5.638  1.00127.47           C  
+ANISOU 9996  C   ASN C 432    12419  21870  14144   1427   4940   -885       C  
+ATOM   9997  O   ASN C 432     -68.519  56.984   6.834  1.00122.41           O  
+ANISOU 9997  O   ASN C 432    11885  21634  12991   1470   5175   -841       O  
+ATOM   9998  CB  ASN C 432     -68.928  58.527   3.955  1.00115.30           C  
+ANISOU 9998  CB  ASN C 432    10859  20026  12923   2204   4480  -1718       C  
+ATOM   9999  CG  ASN C 432     -69.643  59.395   4.974  1.00121.97           C  
+ANISOU 9999  CG  ASN C 432    11581  21437  13323   2527   4787  -2016       C  
+ATOM  10000  OD1 ASN C 432     -70.614  58.968   5.600  1.00116.37           O  
+ANISOU10000  OD1 ASN C 432    10432  21281  12504   2388   5173  -1959       O  
+ATOM  10001  ND2 ASN C 432     -69.162  60.621   5.149  1.00123.55           N  
+ANISOU10001  ND2 ASN C 432    12174  21500  13269   2946   4633  -2352       N  
+ATOM  10002  N   GLU C 433     -69.139  55.606   5.161  1.00130.05           N  
+ANISOU10002  N   GLU C 433    12377  22158  14877   1049   5056   -657       N  
+ATOM  10003  CA  GLU C 433     -69.607  54.539   6.031  1.00128.03           C  
+ANISOU10003  CA  GLU C 433    11892  22226  14528    593   5460   -223       C  
+ATOM  10004  C   GLU C 433     -68.385  53.743   6.469  1.00135.96           C  
+ANISOU10004  C   GLU C 433    13357  22843  15460    317   5363    312       C  
+ATOM  10005  O   GLU C 433     -67.493  53.491   5.656  1.00130.21           O  
+ANISOU10005  O   GLU C 433    12902  21520  15050    303   5014    382       O  
+ATOM  10006  CB  GLU C 433     -70.613  53.633   5.310  1.00120.74           C  
+ANISOU10006  CB  GLU C 433    10437  21322  14116    235   5596   -181       C  
+ATOM  10007  CG  GLU C 433     -72.050  54.169   5.134  1.00122.84           C  
+ANISOU10007  CG  GLU C 433    10083  22175  14414    416   5803   -606       C  
+ATOM  10008  CD  GLU C 433     -72.166  55.555   4.491  1.00126.39           C  
+ANISOU10008  CD  GLU C 433    10552  22642  14827   1053   5522  -1175       C  
+ATOM  10009  OE1 GLU C 433     -71.154  56.140   4.051  1.00123.69           O  
+ANISOU10009  OE1 GLU C 433    10704  21820  14474   1323   5151  -1271       O  
+ATOM  10010  OE2 GLU C 433     -73.304  56.062   4.410  1.00135.17           O  
+ANISOU10010  OE2 GLU C 433    11179  24234  15943   1284   5671  -1512       O  
+ATOM  10011  N   GLU C 434     -68.344  53.356   7.742  1.00145.04           N  
+ANISOU10011  N   GLU C 434    14576  24360  16172    123   5673    695       N  
+ATOM  10012  CA  GLU C 434     -67.197  52.642   8.302  1.00139.41           C  
+ANISOU10012  CA  GLU C 434    14290  23366  15314    -82   5584   1248       C  
+ATOM  10013  C   GLU C 434     -65.911  53.427   8.052  1.00132.76           C  
+ANISOU10013  C   GLU C 434    13920  22184  14338    255   5143   1067       C  
+ATOM  10014  O   GLU C 434     -64.932  52.892   7.532  1.00119.38           O  
+ANISOU10014  O   GLU C 434    12486  19946  12927    170   4859   1313       O  
+ATOM  10015  CB  GLU C 434     -67.089  51.231   7.715  1.00129.61           C  
+ANISOU10015  CB  GLU C 434    13000  21603  14642   -520   5580   1695       C  
+ATOM  10016  N   PHE C 435     -65.932  54.703   8.424  1.00134.90           N  
+ANISOU10016  N   PHE C 435    14290  22778  14189    632   5101    617       N  
+ATOM  10017  CA  PHE C 435     -64.857  55.631   8.092  1.00114.86           C  
+ANISOU10017  CA  PHE C 435    12157  19928  11557    941   4694    336       C  
+ATOM  10018  C   PHE C 435     -63.630  55.407   8.970  1.00114.60           C  
+ANISOU10018  C   PHE C 435    12523  19903  11116    851   4569    716       C  
+ATOM  10019  O   PHE C 435     -62.527  55.841   8.637  1.00114.68           O  
+ANISOU10019  O   PHE C 435    12860  19579  11133    983   4203    627       O  
+ATOM  10020  CB  PHE C 435     -65.359  57.073   8.223  1.00115.78           C  
+ANISOU10020  CB  PHE C 435    12260  20343  11387   1361   4718   -290       C  
+ATOM  10021  CG  PHE C 435     -64.346  58.112   7.837  1.00114.64           C  
+ANISOU10021  CG  PHE C 435    12534  19841  11182   1645   4322   -616       C  
+ATOM  10022  CD1 PHE C 435     -64.120  58.417   6.505  1.00107.56           C  
+ANISOU10022  CD1 PHE C 435    11680  18418  10769   1782   4009   -829       C  
+ATOM  10023  CD2 PHE C 435     -63.638  58.802   8.806  1.00116.24           C  
+ANISOU10023  CD2 PHE C 435    13082  20260  10823   1749   4271   -721       C  
+ATOM  10024  CE1 PHE C 435     -63.194  59.379   6.146  1.00101.95           C  
+ANISOU10024  CE1 PHE C 435    11355  17374  10006   2000   3673  -1099       C  
+ATOM  10025  CE2 PHE C 435     -62.711  59.765   8.455  1.00108.97           C  
+ANISOU10025  CE2 PHE C 435    12537  18999   9868   1950   3918  -1032       C  
+ATOM  10026  CZ  PHE C 435     -62.489  60.054   7.123  1.00103.50           C  
+ANISOU10026  CZ  PHE C 435    11888  17754   9683   2068   3631  -1204       C  
+ATOM  10027  N   GLU C 436     -63.827  54.716  10.088  1.00130.80           N  
+ANISOU10027  N   GLU C 436    14527  22369  12800    617   4872   1159       N  
+ATOM  10028  CA  GLU C 436     -62.738  54.422  11.010  1.00136.92           C  
+ANISOU10028  CA  GLU C 436    15641  23250  13133    537   4760   1584       C  
+ATOM  10029  C   GLU C 436     -61.847  53.313  10.457  1.00142.75           C  
+ANISOU10029  C   GLU C 436    16512  23405  14319    341   4531   2104       C  
+ATOM  10030  O   GLU C 436     -60.725  53.112  10.921  1.00145.57           O  
+ANISOU10030  O   GLU C 436    17155  23719  14435    345   4312   2427       O  
+ATOM  10031  CB  GLU C 436     -63.287  54.026  12.382  1.00130.76           C  
+ANISOU10031  CB  GLU C 436    14767  23139  11775    361   5175   1933       C  
+ATOM  10032  N   THR C 437     -62.361  52.596   9.463  1.00140.72           N  
+ANISOU10032  N   THR C 437    16031  22722  14713    182   4578   2160       N  
+ATOM  10033  CA  THR C 437     -61.653  51.464   8.880  1.00138.13           C  
+ANISOU10033  CA  THR C 437    15809  21799  14875     -1   4414   2610       C  
+ATOM  10034  C   THR C 437     -60.697  51.926   7.777  1.00126.36           C  
+ANISOU10034  C   THR C 437    14499  19800  13711    216   3973   2301       C  
+ATOM  10035  O   THR C 437     -59.856  51.161   7.303  1.00121.24           O  
+ANISOU10035  O   THR C 437    13987  18674  13406    153   3779   2606       O  
+ATOM  10036  CB  THR C 437     -62.657  50.431   8.306  1.00131.38           C  
+ANISOU10036  CB  THR C 437    14637  20703  14577   -323   4680   2771       C  
+ATOM  10037  OG1 THR C 437     -63.688  50.179   9.268  1.00135.65           O  
+ANISOU10037  OG1 THR C 437    14947  21789  14804   -536   5127   2970       O  
+ATOM  10038  CG2 THR C 437     -61.970  49.113   7.967  1.00132.29           C  
+ANISOU10038  CG2 THR C 437    14903  20214  15147   -540   4592   3310       C  
+ATOM  10039  N   TYR C 438     -60.803  53.195   7.394  1.00125.72           N  
+ANISOU10039  N   TYR C 438    14432  19824  13512    485   3828   1706       N  
+ATOM  10040  CA  TYR C 438     -59.999  53.710   6.291  1.00125.21           C  
+ANISOU10040  CA  TYR C 438    14523  19302  13748    666   3446   1403       C  
+ATOM  10041  C   TYR C 438     -59.092  54.872   6.693  1.00126.63           C  
+ANISOU10041  C   TYR C 438    14997  19635  13483    895   3194   1140       C  
+ATOM  10042  O   TYR C 438     -57.954  54.964   6.230  1.00118.76           O  
+ANISOU10042  O   TYR C 438    14201  18324  12601    947   2876   1164       O  
+ATOM  10043  CB  TYR C 438     -60.906  54.151   5.138  1.00119.87           C  
+ANISOU10043  CB  TYR C 438    13614  18464  13468    763   3446    928       C  
+ATOM  10044  CG  TYR C 438     -61.716  53.037   4.511  1.00120.80           C  
+ANISOU10044  CG  TYR C 438    13428  18375  14095    502   3624   1096       C  
+ATOM  10045  CD1 TYR C 438     -62.848  52.534   5.140  1.00121.89           C  
+ANISOU10045  CD1 TYR C 438    13270  18873  14168    292   4008   1247       C  
+ATOM  10046  CD2 TYR C 438     -61.355  52.495   3.285  1.00123.69           C  
+ANISOU10046  CD2 TYR C 438    13793  18206  14997    440   3419   1074       C  
+ATOM  10047  CE1 TYR C 438     -63.593  51.519   4.570  1.00125.30           C  
+ANISOU10047  CE1 TYR C 438    13415  19109  15083     -8   4169   1374       C  
+ATOM  10048  CE2 TYR C 438     -62.095  51.480   2.706  1.00125.50           C  
+ANISOU10048  CE2 TYR C 438    13757  18234  15693    167   3572   1169       C  
+ATOM  10049  CZ  TYR C 438     -63.212  50.996   3.353  1.00125.48           C  
+ANISOU10049  CZ  TYR C 438    13464  18570  15643    -73   3940   1318       C  
+ATOM  10050  OH  TYR C 438     -63.952  49.986   2.782  1.00123.76           O  
+ANISOU10050  OH  TYR C 438    12972  18145  15906   -404   4092   1390       O  
+ATOM  10051  N   TYR C 439     -59.590  55.753   7.556  1.00131.62           N  
+ANISOU10051  N   TYR C 439    15644  20756  13611   1016   3347    867       N  
+ATOM  10052  CA  TYR C 439     -58.809  56.910   7.986  1.00126.58           C  
+ANISOU10052  CA  TYR C 439    15296  20259  12541   1197   3127    548       C  
+ATOM  10053  C   TYR C 439     -58.900  57.166   9.490  1.00132.18           C  
+ANISOU10053  C   TYR C 439    16085  21598  12541   1181   3314    607       C  
+ATOM  10054  O   TYR C 439     -59.664  58.027   9.927  1.00130.46           O  
+ANISOU10054  O   TYR C 439    15831  21719  12020   1337   3501    188       O  
+ATOM  10055  CB  TYR C 439     -59.265  58.168   7.240  1.00115.71           C  
+ANISOU10055  CB  TYR C 439    13941  18730  11293   1459   3048    -89       C  
+ATOM  10056  CG  TYR C 439     -59.105  58.111   5.736  1.00104.34           C  
+ANISOU10056  CG  TYR C 439    12463  16725  10455   1503   2828   -195       C  
+ATOM  10057  CD1 TYR C 439     -57.974  58.627   5.117  1.00101.66           C  
+ANISOU10057  CD1 TYR C 439    12382  16028  10215   1556   2481   -314       C  
+ATOM  10058  CD2 TYR C 439     -60.090  57.549   4.935  1.00107.62           C  
+ANISOU10058  CD2 TYR C 439    12568  17011  11313   1470   2971   -190       C  
+ATOM  10059  CE1 TYR C 439     -57.828  58.580   3.744  1.00100.86           C  
+ANISOU10059  CE1 TYR C 439    12250  15462  10609   1593   2301   -404       C  
+ATOM  10060  CE2 TYR C 439     -59.953  57.498   3.562  1.00108.49           C  
+ANISOU10060  CE2 TYR C 439    12645  16662  11913   1509   2763   -306       C  
+ATOM  10061  CZ  TYR C 439     -58.820  58.015   2.972  1.00108.81           C  
+ANISOU10061  CZ  TYR C 439    12967  16362  12015   1581   2437   -404       C  
+ATOM  10062  OH  TYR C 439     -58.675  57.968   1.606  1.00107.95           O  
+ANISOU10062  OH  TYR C 439    12831  15844  12341   1617   2249   -511       O  
+ATOM  10063  N   PRO C 440     -58.121  56.420  10.287  1.00130.91           N  
+ANISOU10063  N   PRO C 440    16030  21614  12096   1020   3262   1126       N  
+ATOM  10064  CA  PRO C 440     -58.082  56.631  11.739  1.00134.43           C  
+ANISOU10064  CA  PRO C 440    16574  22714  11788    994   3401   1218       C  
+ATOM  10065  C   PRO C 440     -57.462  57.977  12.119  1.00133.78           C  
+ANISOU10065  C   PRO C 440    16756  22817  11256   1154   3175    678       C  
+ATOM  10066  O   PRO C 440     -56.245  58.063  12.282  1.00133.66           O  
+ANISOU10066  O   PRO C 440    16940  22767  11078   1114   2844    785       O  
+ATOM  10067  CB  PRO C 440     -57.218  55.469  12.238  1.00132.05           C  
+ANISOU10067  CB  PRO C 440    16338  22437  11396    816   3300   1950       C  
+ATOM  10068  CG  PRO C 440     -56.366  55.107  11.069  1.00124.77           C  
+ANISOU10068  CG  PRO C 440    15455  20860  11091    829   2974   2042       C  
+ATOM  10069  CD  PRO C 440     -57.231  55.326   9.864  1.00121.36           C  
+ANISOU10069  CD  PRO C 440    14851  20015  11243    884   3067   1660       C  
+ATOM  10070  N   GLY C 441     -58.286  59.011  12.261  1.00135.09           N  
+ANISOU10070  N   GLY C 441    16914  23176  11237   1332   3352     94       N  
+ATOM  10071  CA  GLY C 441     -57.779  60.334  12.579  1.00136.91           C  
+ANISOU10071  CA  GLY C 441    17428  23496  11094   1475   3162   -482       C  
+ATOM  10072  C   GLY C 441     -58.694  61.473  12.171  1.00134.39           C  
+ANISOU10072  C   GLY C 441    17104  23060  10897   1750   3302  -1159       C  
+ATOM  10073  O   GLY C 441     -59.749  61.257  11.574  1.00137.65           O  
+ANISOU10073  O   GLY C 441    17247  23357  11695   1851   3527  -1191       O  
+ATOM  10074  N   ALA C 442     -58.287  62.694  12.506  1.00128.63           N  
+ANISOU10074  N   ALA C 442    16672  22361   9842   1874   3161  -1708       N  
+ATOM  10075  CA  ALA C 442     -59.083  63.880  12.218  1.00124.63           C  
+ANISOU10075  CA  ALA C 442    16226  21709   9417   2189   3283  -2374       C  
+ATOM  10076  C   ALA C 442     -58.210  65.016  11.693  1.00123.12           C  
+ANISOU10076  C   ALA C 442    16410  21021   9350   2253   2929  -2822       C  
+ATOM  10077  O   ALA C 442     -58.713  66.073  11.313  1.00124.54           O  
+ANISOU10077  O   ALA C 442    16717  20927   9675   2532   2968  -3359       O  
+ATOM  10078  CB  ALA C 442     -59.837  64.326  13.461  1.00130.43           C  
+ANISOU10078  CB  ALA C 442    16947  23096   9514   2315   3634  -2696       C  
+HETATM10079  N   MSE C 446     -59.694  67.707   8.459  1.00104.46           N  
+ANISOU10079  N   MSE C 446    14280  16997   8415   3189   2774  -3983       N  
+HETATM10080  CA  MSE C 446     -59.404  66.722   7.424  1.00 98.99           C  
+ANISOU10080  CA  MSE C 446    13374  16050   8190   3003   2612  -3477       C  
+HETATM10081  C   MSE C 446     -60.667  65.942   7.060  1.00103.80           C  
+ANISOU10081  C   MSE C 446    13508  16871   9062   3135   2874  -3278       C  
+HETATM10082  O   MSE C 446     -60.847  65.530   5.913  1.00112.11           O  
+ANISOU10082  O   MSE C 446    14388  17609  10601   3147   2766  -3087       O  
+HETATM10083  CB  MSE C 446     -58.284  65.783   7.886  1.00110.82           C  
+ANISOU10083  CB  MSE C 446    14882  17731   9492   2589   2462  -3016       C  
+HETATM10084  CG  MSE C 446     -58.415  64.337   7.439  1.00115.53           C  
+ANISOU10084  CG  MSE C 446    15123  18380  10392   2406   2507  -2432       C  
+HETATM10085 SE   MSE C 446     -56.797  63.322   7.833  1.00162.78          SE  
+ANISOU10085 SE   MSE C 446    21190  24437  16220   1986   2236  -1865      SE  
+HETATM10086  CE  MSE C 446     -57.536  61.523   7.735  1.00101.47           C  
+ANISOU10086  CE  MSE C 446    12974  16851   8729   1841   2493  -1209       C  
+ATOM  10087  N   LYS C 447     -61.546  65.760   8.041  1.00117.22           N  
+ANISOU10087  N   LYS C 447    14985  19137  10417   3214   3224  -3347       N  
+ATOM  10088  CA  LYS C 447     -62.856  65.161   7.804  1.00115.32           C  
+ANISOU10088  CA  LYS C 447    14257  19170  10390   3334   3513  -3239       C  
+ATOM  10089  C   LYS C 447     -63.676  66.028   6.851  1.00116.77           C  
+ANISOU10089  C   LYS C 447    14369  19050  10947   3771   3486  -3622       C  
+ATOM  10090  O   LYS C 447     -64.448  65.520   6.036  1.00114.31           O  
+ANISOU10090  O   LYS C 447    13679  18726  11028   3832   3529  -3481       O  
+ATOM  10091  CB  LYS C 447     -63.607  64.965   9.122  1.00118.25           C  
+ANISOU10091  CB  LYS C 447    14422  20255  10254   3343   3923  -3289       C  
+ATOM  10092  N   LYS C 448     -63.501  67.341   6.967  1.00119.86           N  
+ANISOU10092  N   LYS C 448    15140  19155  11248   4034   3384  -4075       N  
+ATOM  10093  CA  LYS C 448     -64.183  68.300   6.106  1.00121.98           C  
+ANISOU10093  CA  LYS C 448    15439  18954  11953   4369   3270  -4313       C  
+ATOM  10094  C   LYS C 448     -63.705  68.179   4.662  1.00119.13           C  
+ANISOU10094  C   LYS C 448    15137  18108  12020   4397   2967  -4158       C  
+ATOM  10095  O   LYS C 448     -64.501  68.270   3.723  1.00126.84           O  
+ANISOU10095  O   LYS C 448    15878  18921  13395   4602   2912  -4126       O  
+ATOM  10096  CB  LYS C 448     -63.965  69.726   6.616  1.00110.99           C  
+ANISOU10096  CB  LYS C 448    14509  17229  10433   4515   3207  -4730       C  
+ATOM  10097  N   LEU C 449     -62.402  67.974   4.492  1.00101.82           N  
+ANISOU10097  N   LEU C 449    13249  15677   9761   4127   2739  -4010       N  
+ATOM  10098  CA  LEU C 449     -61.815  67.858   3.164  1.00107.46           C  
+ANISOU10098  CA  LEU C 449    14056  15878  10896   4035   2427  -3794       C  
+ATOM  10099  C   LEU C 449     -62.381  66.630   2.462  1.00113.92           C  
+ANISOU10099  C   LEU C 449    14390  16866  12029   3909   2469  -3425       C  
+ATOM  10100  O   LEU C 449     -62.690  66.670   1.272  1.00107.85           O  
+ANISOU10100  O   LEU C 449    13515  15834  11628   4054   2322  -3391       O  
+ATOM  10101  CB  LEU C 449     -60.290  67.774   3.248  1.00 90.05           C  
+ANISOU10101  CB  LEU C 449    12205  13419   8590   3642   2177  -3622       C  
+ATOM  10102  N   PHE C 450     -62.503  65.536   3.208  1.00114.64           N  
+ANISOU10102  N   PHE C 450    14204  17392  11961   3620   2666  -3146       N  
+ATOM  10103  CA  PHE C 450     -63.103  64.315   2.686  1.00107.73           C  
+ANISOU10103  CA  PHE C 450    12870  16680  11381   3448   2752  -2821       C  
+ATOM  10104  C   PHE C 450     -64.550  64.565   2.274  1.00 99.42           C  
+ANISOU10104  C   PHE C 450    11422  15843  10508   3794   2912  -3048       C  
+ATOM  10105  O   PHE C 450     -64.992  64.120   1.214  1.00 90.51           O  
+ANISOU10105  O   PHE C 450    10022  14614   9754   3798   2813  -2951       O  
+ATOM  10106  CB  PHE C 450     -63.035  63.189   3.723  1.00109.03           C  
+ANISOU10106  CB  PHE C 450    12854  17263  11309   3089   2980  -2475       C  
+ATOM  10107  CG  PHE C 450     -63.661  61.901   3.263  1.00102.09           C  
+ANISOU10107  CG  PHE C 450    11532  16505  10754   2856   3098  -2147       C  
+ATOM  10108  CD1 PHE C 450     -62.897  60.930   2.639  1.00 91.31           C  
+ANISOU10108  CD1 PHE C 450    10194  14829   9670   2541   2920  -1783       C  
+ATOM  10109  CD2 PHE C 450     -65.012  61.657   3.463  1.00102.17           C  
+ANISOU10109  CD2 PHE C 450    11085  16939  10795   2941   3399  -2226       C  
+ATOM  10110  CE1 PHE C 450     -63.469  59.745   2.214  1.00 93.71           C  
+ANISOU10110  CE1 PHE C 450    10126  15185  10296   2303   3033  -1523       C  
+ATOM  10111  CE2 PHE C 450     -65.588  60.477   3.039  1.00107.71           C  
+ANISOU10111  CE2 PHE C 450    11378  17733  11812   2665   3507  -1950       C  
+ATOM  10112  CZ  PHE C 450     -64.816  59.520   2.416  1.00104.17           C  
+ANISOU10112  CZ  PHE C 450    11009  16915  11656   2338   3322  -1607       C  
+ATOM  10113  N   GLY C 451     -65.282  65.279   3.124  1.00 97.12           N  
+ANISOU10113  N   GLY C 451    11082  15887   9932   4093   3157  -3373       N  
+ATOM  10114  CA  GLY C 451     -66.675  65.595   2.865  1.00100.66           C  
+ANISOU10114  CA  GLY C 451    11143  16549  10555   4410   3295  -3566       C  
+ATOM  10115  C   GLY C 451     -66.870  66.496   1.663  1.00104.62           C  
+ANISOU10115  C   GLY C 451    11786  16547  11418   4711   2984  -3697       C  
+ATOM  10116  O   GLY C 451     -67.934  66.497   1.044  1.00116.44           O  
+ANISOU10116  O   GLY C 451    12918  18142  13181   4871   2973  -3705       O  
+ATOM  10117  N   GLU C 452     -65.840  67.266   1.331  1.00109.72           N  
+ANISOU10117  N   GLU C 452    12958  16676  12053   4766   2728  -3776       N  
+ATOM  10118  CA  GLU C 452     -65.913  68.192   0.207  1.00108.31           C  
+ANISOU10118  CA  GLU C 452    12983  15991  12179   5020   2439  -3839       C  
+ATOM  10119  C   GLU C 452     -65.755  67.475  -1.133  1.00104.31           C  
+ANISOU10119  C   GLU C 452    12296  15357  11982   4931   2222  -3606       C  
+ATOM  10120  O   GLU C 452     -65.839  68.099  -2.191  1.00114.91           O  
+ANISOU10120  O   GLU C 452    13763  16345  13553   5114   1975  -3592       O  
+ATOM  10121  CB  GLU C 452     -64.848  69.282   0.345  1.00114.21           C  
+ANISOU10121  CB  GLU C 452    14363  16219  12812   5042   2268  -3989       C  
+ATOM  10122  N   LEU C 453     -65.525  66.166  -1.086  1.00 97.77           N  
+ANISOU10122  N   LEU C 453    11177  14825  11146   4645   2325  -3418       N  
+ATOM  10123  CA  LEU C 453     -65.340  65.379  -2.303  1.00 98.55           C  
+ANISOU10123  CA  LEU C 453    11111  14771  11561   4444   2117  -3181       C  
+ATOM  10124  C   LEU C 453     -66.658  64.860  -2.873  1.00112.44           C  
+ANISOU10124  C   LEU C 453    12270  16909  13544   4563   2189  -3211       C  
+ATOM  10125  O   LEU C 453     -66.730  64.496  -4.047  1.00117.12           O  
+ANISOU10125  O   LEU C 453    12722  17385  14395   4517   1977  -3120       O  
+ATOM  10126  CB  LEU C 453     -64.397  64.204  -2.036  1.00 91.18           C  
+ANISOU10126  CB  LEU C 453    10224  13796  10626   3893   2122  -2842       C  
+ATOM  10127  N   ASN C 454     -67.699  64.828  -2.047  1.00107.87           N  
+ANISOU10127  N   ASN C 454    11361  16757  12869   4614   2456  -3292       N  
+ATOM  10128  CA  ASN C 454     -68.997  64.323  -2.482  1.00 95.22           C  
+ANISOU10128  CA  ASN C 454     9170  15528  11479   4616   2518  -3284       C  
+ATOM  10129  C   ASN C 454     -69.982  65.452  -2.765  1.00108.81           C  
+ANISOU10129  C   ASN C 454    10858  17227  13258   5034   2418  -3450       C  
+ATOM  10130  O   ASN C 454     -69.586  66.606  -2.934  1.00105.36           O  
+ANISOU10130  O   ASN C 454    10876  16379  12775   5312   2246  -3541       O  
+ATOM  10131  CB  ASN C 454     -69.582  63.373  -1.435  1.00 98.03           C  
+ANISOU10131  CB  ASN C 454     9094  16433  11719   4334   2910  -3214       C  
+ATOM  10132  N   SER C 459     -67.166  73.126  -7.787  1.00100.53           N  
+ANISOU10132  N   SER C 459    12874  12736  12587   6700    717  -3307       N  
+ATOM  10133  CA  SER C 459     -66.347  73.774  -8.805  1.00 99.32           C  
+ANISOU10133  CA  SER C 459    13178  12081  12478   6714    475  -3121       C  
+ATOM  10134  C   SER C 459     -65.253  72.843  -9.320  1.00111.36           C  
+ANISOU10134  C   SER C 459    14770  13575  13966   6301    377  -2962       C  
+ATOM  10135  O   SER C 459     -65.110  71.728  -8.829  1.00121.52           O  
+ANISOU10135  O   SER C 459    15772  15188  15210   6017    499  -3002       O  
+ATOM  10136  CB  SER C 459     -65.719  75.042  -8.227  1.00115.59           C  
+ANISOU10136  CB  SER C 459    15817  13580  14522   6769    526  -3237       C  
+ATOM  10137  OG  SER C 459     -64.738  75.577  -9.093  1.00118.85           O  
+ANISOU10137  OG  SER C 459    16701  13491  14965   6673    331  -3045       O  
+ATOM  10138  N   ILE C 460     -64.501  73.280 -10.327  1.00103.90           N  
+ANISOU10138  N   ILE C 460    14191  12245  13041   6279    168  -2771       N  
+ATOM  10139  CA  ILE C 460     -63.387  72.479 -10.830  1.00 99.07           C  
+ANISOU10139  CA  ILE C 460    13676  11573  12394   5904     85  -2634       C  
+ATOM  10140  C   ILE C 460     -62.092  72.739 -10.055  1.00 95.78           C  
+ANISOU10140  C   ILE C 460    13706  10789  11899   5580    171  -2698       C  
+ATOM  10141  O   ILE C 460     -61.460  71.813  -9.538  1.00 90.85           O  
+ANISOU10141  O   ILE C 460    12980  10324  11214   5257    260  -2735       O  
+ATOM  10142  CB  ILE C 460     -63.147  72.732 -12.331  1.00100.32           C  
+ANISOU10142  CB  ILE C 460    13997  11551  12569   6013   -170  -2392       C  
+ATOM  10143  CG1 ILE C 460     -64.181  71.972 -13.165  1.00 99.62           C  
+ANISOU10143  CG1 ILE C 460    13373  11968  12512   6188   -283  -2348       C  
+ATOM  10144  CG2 ILE C 460     -61.740  72.299 -12.732  1.00 91.66           C  
+ANISOU10144  CG2 ILE C 460    13181  10222  11425   5636   -228  -2272       C  
+ATOM  10145  CD1 ILE C 460     -63.869  71.947 -14.638  1.00 93.67           C  
+ANISOU10145  CD1 ILE C 460    12723  11155  11713   6252   -534  -2130       C  
+ATOM  10146  N   GLU C 461     -61.716  74.014  -9.976  1.00103.52           N  
+ANISOU10146  N   GLU C 461    15173  11277  12884   5671    140  -2716       N  
+ATOM  10147  CA  GLU C 461     -60.528  74.437  -9.241  1.00 99.93           C  
+ANISOU10147  CA  GLU C 461    15161  10457  12352   5358    201  -2818       C  
+ATOM  10148  C   GLU C 461     -60.623  74.041  -7.777  1.00102.97           C  
+ANISOU10148  C   GLU C 461    15388  11117  12618   5236    416  -3081       C  
+ATOM  10149  O   GLU C 461     -59.659  73.555  -7.183  1.00 96.88           O  
+ANISOU10149  O   GLU C 461    14725  10363  11723   4890    461  -3137       O  
+ATOM  10150  CB  GLU C 461     -60.330  75.950  -9.367  1.00 94.01           C  
+ANISOU10150  CB  GLU C 461    14925   9129  11664   5500    151  -2832       C  
+ATOM  10151  N   GLU C 462     -61.807  74.240  -7.209  1.00105.16           N  
+ANISOU10151  N   GLU C 462    15400  11645  12909   5537    549  -3237       N  
+ATOM  10152  CA  GLU C 462     -62.043  73.969  -5.799  1.00 98.19           C  
+ANISOU10152  CA  GLU C 462    14374  11060  11875   5474    781  -3492       C  
+ATOM  10153  C   GLU C 462     -61.989  72.472  -5.520  1.00100.81           C  
+ANISOU10153  C   GLU C 462    14293  11893  12118   5243    866  -3426       C  
+ATOM  10154  O   GLU C 462     -61.425  72.043  -4.515  1.00105.30           O  
+ANISOU10154  O   GLU C 462    14905  12611  12494   5007    994  -3540       O  
+ATOM  10155  CB  GLU C 462     -63.386  74.551  -5.357  1.00102.37           C  
+ANISOU10155  CB  GLU C 462    14694  11754  12450   5877    918  -3664       C  
+ATOM  10156  CG  GLU C 462     -63.409  75.041  -3.915  1.00108.94           C  
+ANISOU10156  CG  GLU C 462    15668  12612  13114   5866   1143  -3994       C  
+ATOM  10157  CD  GLU C 462     -62.629  76.332  -3.714  1.00110.70           C  
+ANISOU10157  CD  GLU C 462    16485  12228  13348   5822   1093  -4149       C  
+ATOM  10158  OE1 GLU C 462     -63.258  77.355  -3.372  1.00122.07           O  
+ANISOU10158  OE1 GLU C 462    18051  13473  14856   6125   1181  -4353       O  
+ATOM  10159  OE2 GLU C 462     -61.390  76.326  -3.882  1.00100.37           O  
+ANISOU10159  OE2 GLU C 462    15511  10634  11990   5474    974  -4083       O  
+ATOM  10160  N   LEU C 463     -62.585  71.681  -6.407  1.00 95.45           N  
+ANISOU10160  N   LEU C 463    13216  11481  11569   5313    794  -3248       N  
+ATOM  10161  CA  LEU C 463     -62.596  70.229  -6.253  1.00 96.46           C  
+ANISOU10161  CA  LEU C 463    12933  12044  11672   5093    882  -3179       C  
+ATOM  10162  C   LEU C 463     -61.180  69.666  -6.357  1.00 92.61           C  
+ANISOU10162  C   LEU C 463    12685  11382  11122   4744    806  -3077       C  
+ATOM  10163  O   LEU C 463     -60.776  68.811  -5.559  1.00 95.71           O  
+ANISOU10163  O   LEU C 463    12950  12020  11396   4475    936  -3064       O  
+ATOM  10164  CB  LEU C 463     -63.500  69.586  -7.307  1.00 94.16           C  
+ANISOU10164  CB  LEU C 463    12190  12029  11559   5215    789  -3048       C  
+ATOM  10165  CG  LEU C 463     -63.826  68.101  -7.149  1.00 96.04           C  
+ANISOU10165  CG  LEU C 463    11916  12741  11833   5012    915  -3012       C  
+ATOM  10166  CD1 LEU C 463     -64.474  67.846  -5.800  1.00 82.50           C  
+ANISOU10166  CD1 LEU C 463     9952  11405   9990   5015   1210  -3159       C  
+ATOM  10167  CD2 LEU C 463     -64.729  67.630  -8.280  1.00 98.92           C  
+ANISOU10167  CD2 LEU C 463    11861  13348  12377   5119    785  -2937       C  
+ATOM  10168  N   ILE C 464     -60.430  70.152  -7.343  1.00 84.12           N  
+ANISOU10168  N   ILE C 464    11938   9900  10123   4696    596  -2947       N  
+ATOM  10169  CA  ILE C 464     -59.042  69.737  -7.519  1.00 85.05           C  
+ANISOU10169  CA  ILE C 464    12270   9840  10206   4285    509  -2801       C  
+ATOM  10170  C   ILE C 464     -58.215  70.097  -6.284  1.00 88.92           C  
+ANISOU10170  C   ILE C 464    13049  10240  10496   4044    595  -2929       C  
+ATOM  10171  O   ILE C 464     -57.433  69.278  -5.786  1.00 89.55           O  
+ANISOU10171  O   ILE C 464    13030  10497  10499   3651    622  -2805       O  
+ATOM  10172  CB  ILE C 464     -58.416  70.375  -8.775  1.00 84.29           C  
+ANISOU10172  CB  ILE C 464    12504   9325  10197   4284    297  -2649       C  
+ATOM  10173  CG1 ILE C 464     -58.947  69.692 -10.036  1.00 83.76           C  
+ANISOU10173  CG1 ILE C 464    12107   9449  10269   4376    186  -2480       C  
+ATOM  10174  CG2 ILE C 464     -56.905  70.262  -8.742  1.00 69.74           C  
+ANISOU10174  CG2 ILE C 464    10914   7285   8301   3800    235  -2516       C  
+ATOM  10175  CD1 ILE C 464     -58.585  70.406 -11.318  1.00 83.83           C  
+ANISOU10175  CD1 ILE C 464    12423   9117  10311   4471    -10  -2322       C  
+ATOM  10176  N   ASN C 465     -58.406  71.316  -5.783  1.00 92.29           N  
+ANISOU10176  N   ASN C 465    13830  10401  10835   4298    629  -3190       N  
+ATOM  10177  CA  ASN C 465     -57.721  71.757  -4.572  1.00 97.56           C  
+ANISOU10177  CA  ASN C 465    14781  11011  11276   4085    703  -3393       C  
+ATOM  10178  C   ASN C 465     -58.064  70.870  -3.380  1.00101.53           C  
+ANISOU10178  C   ASN C 465    14936  12060  11582   3980    900  -3442       C  
+ATOM  10179  O   ASN C 465     -57.201  70.551  -2.559  1.00103.01           O  
+ANISOU10179  O   ASN C 465    15186  12383  11569   3618    912  -3420       O  
+ATOM  10180  CB  ASN C 465     -58.074  73.212  -4.254  1.00 83.90           C  
+ANISOU10180  CB  ASN C 465    13387   8932   9559   4289    727  -3625       C  
+ATOM  10181  CG  ASN C 465     -57.375  74.197  -5.169  1.00103.57           C  
+ANISOU10181  CG  ASN C 465    16317  10832  12201   4212    545  -3527       C  
+ATOM  10182  OD1 ASN C 465     -56.322  73.899  -5.732  1.00116.07           O  
+ANISOU10182  OD1 ASN C 465    18064  12252  13784   3927    415  -3374       O  
+ATOM  10183  ND2 ASN C 465     -57.959  75.381  -5.320  1.00102.98           N  
+ANISOU10183  ND2 ASN C 465    16439  10434  12256   4469    550  -3609       N  
+ATOM  10184  N   THR C 466     -59.330  70.471  -3.301  1.00 94.72           N  
+ANISOU10184  N   THR C 466    13687  11538  10765   4290   1053  -3487       N  
+ATOM  10185  CA  THR C 466     -59.798  69.556  -2.267  1.00 87.49           C  
+ANISOU10185  CA  THR C 466    12399  11167   9678   4186   1274  -3477       C  
+ATOM  10186  C   THR C 466     -59.044  68.233  -2.318  1.00 87.88           C  
+ANISOU10186  C   THR C 466    12231  11406   9755   3724   1232  -3122       C  
+ATOM  10187  O   THR C 466     -58.467  67.794  -1.317  1.00 91.72           O  
+ANISOU10187  O   THR C 466    12728  12115  10007   3447   1304  -3061       O  
+ATOM  10188  CB  THR C 466     -61.307  69.277  -2.404  1.00 82.79           C  
+ANISOU10188  CB  THR C 466    11354  10915   9188   4556   1438  -3546       C  
+ATOM  10189  OG1 THR C 466     -62.034  70.509  -2.329  1.00106.10           O  
+ANISOU10189  OG1 THR C 466    14443  13672  12197   4846   1450  -3733       O  
+ATOM  10190  CG2 THR C 466     -61.776  68.350  -1.300  1.00 83.89           C  
+ANISOU10190  CG2 THR C 466    11122  11617   9136   4398   1702  -3508       C  
+ATOM  10191  N   ILE C 467     -59.043  67.613  -3.496  1.00 78.44           N  
+ANISOU10191  N   ILE C 467    10848  10122   8834   3666   1108  -2893       N  
+ATOM  10192  CA  ILE C 467     -58.377  66.329  -3.687  1.00 84.28           C  
+ANISOU10192  CA  ILE C 467    11382  10977   9663   3282   1072  -2575       C  
+ATOM  10193  C   ILE C 467     -56.898  66.413  -3.317  1.00 87.01           C  
+ANISOU10193  C   ILE C 467    12026  11163   9869   2951    953  -2477       C  
+ATOM  10194  O   ILE C 467     -56.405  65.656  -2.469  1.00 96.93           O  
+ANISOU10194  O   ILE C 467    13185  12663  10983   2699   1018  -2321       O  
+ATOM  10195  CB  ILE C 467     -58.485  65.856  -5.149  1.00 77.82           C  
+ANISOU10195  CB  ILE C 467    10402  10019   9146   3288    929  -2425       C  
+ATOM  10196  CG1 ILE C 467     -59.940  65.584  -5.531  1.00 77.35           C  
+ANISOU10196  CG1 ILE C 467     9953  10210   9227   3559   1021  -2506       C  
+ATOM  10197  CG2 ILE C 467     -57.619  64.626  -5.379  1.00 75.83           C  
+ANISOU10197  CG2 ILE C 467    10015   9793   9003   2909    887  -2141       C  
+ATOM  10198  CD1 ILE C 467     -60.132  65.359  -7.015  1.00 73.63           C  
+ANISOU10198  CD1 ILE C 467     9360   9624   8993   3619    845  -2431       C  
+ATOM  10199  N   ILE C 468     -56.201  67.346  -3.961  1.00 84.96           N  
+ANISOU10199  N   ILE C 468    12119  10513   9649   2952    776  -2550       N  
+ATOM  10200  CA  ILE C 468     -54.766  67.517  -3.765  1.00 84.06           C  
+ANISOU10200  CA  ILE C 468    12255  10252   9432   2614    642  -2476       C  
+ATOM  10201  C   ILE C 468     -54.389  67.821  -2.315  1.00 87.55           C  
+ANISOU10201  C   ILE C 468    12839  10888   9538   2487    707  -2627       C  
+ATOM  10202  O   ILE C 468     -53.434  67.249  -1.792  1.00 85.62           O  
+ANISOU10202  O   ILE C 468    12546  10817   9167   2182    652  -2462       O  
+ATOM  10203  CB  ILE C 468     -54.207  68.620  -4.683  1.00 88.06           C  
+ANISOU10203  CB  ILE C 468    13134  10292  10032   2626    476  -2550       C  
+ATOM  10204  CG1 ILE C 468     -54.123  68.100  -6.118  1.00 81.89           C  
+ANISOU10204  CG1 ILE C 468    12208   9398   9507   2616    377  -2323       C  
+ATOM  10205  CG2 ILE C 468     -52.821  69.046  -4.237  1.00 99.01           C  
+ANISOU10205  CG2 ILE C 468    14789  11562  11268   2264    364  -2566       C  
+ATOM  10206  CD1 ILE C 468     -53.894  69.177  -7.141  1.00 88.08           C  
+ANISOU10206  CD1 ILE C 468    13333   9757  10376   2703    248  -2351       C  
+ATOM  10207  N   GLU C 469     -55.124  68.710  -1.654  1.00 90.87           N  
+ANISOU10207  N   GLU C 469    13423  11308   9795   2738    818  -2949       N  
+ATOM  10208  CA  GLU C 469     -54.764  69.035  -0.279  1.00 92.52           C  
+ANISOU10208  CA  GLU C 469    13785  11736   9634   2608    877  -3144       C  
+ATOM  10209  C   GLU C 469     -55.107  67.865   0.644  1.00 95.47           C  
+ANISOU10209  C   GLU C 469    13799  12655   9821   2530   1043  -2951       C  
+ATOM  10210  O   GLU C 469     -54.468  67.683   1.679  1.00106.58           O  
+ANISOU10210  O   GLU C 469    15249  14340  10907   2307   1038  -2933       O  
+ATOM  10211  CB  GLU C 469     -55.442  70.324   0.200  1.00 94.51           C  
+ANISOU10211  CB  GLU C 469    14335  11821   9752   2915    973  -3594       C  
+ATOM  10212  CG  GLU C 469     -56.622  70.133   1.136  1.00 95.14           C  
+ANISOU10212  CG  GLU C 469    14193  12327   9628   3187   1240  -3763       C  
+ATOM  10213  CD  GLU C 469     -57.047  71.434   1.791  1.00113.92           C  
+ANISOU10213  CD  GLU C 469    16912  14553  11818   3460   1336  -4266       C  
+ATOM  10214  OE1 GLU C 469     -56.458  72.485   1.461  1.00116.72           O  
+ANISOU10214  OE1 GLU C 469    17701  14403  12245   3432   1187  -4468       O  
+ATOM  10215  OE2 GLU C 469     -57.960  71.406   2.643  1.00129.05           O  
+ANISOU10215  OE2 GLU C 469    18670  16846  13518   3694   1578  -4466       O  
+ATOM  10216  N   PHE C 470     -56.101  67.065   0.265  1.00 84.38           N  
+ANISOU10216  N   PHE C 470    12038  11414   8607   2692   1184  -2790       N  
+ATOM  10217  CA  PHE C 470     -56.433  65.872   1.041  1.00 91.60           C  
+ANISOU10217  CA  PHE C 470    12616  12790   9396   2573   1360  -2541       C  
+ATOM  10218  C   PHE C 470     -55.298  64.845   0.979  1.00 94.38           C  
+ANISOU10218  C   PHE C 470    12887  13174   9798   2229   1225  -2148       C  
+ATOM  10219  O   PHE C 470     -54.828  64.351   2.016  1.00 96.85           O  
+ANISOU10219  O   PHE C 470    13170  13807   9822   2048   1261  -1987       O  
+ATOM  10220  CB  PHE C 470     -57.744  65.260   0.534  1.00 92.60           C  
+ANISOU10220  CB  PHE C 470    12367  13045   9772   2770   1534  -2474       C  
+ATOM  10221  CG  PHE C 470     -58.178  64.029   1.281  1.00 87.53           C  
+ANISOU10221  CG  PHE C 470    11384  12831   9041   2614   1748  -2197       C  
+ATOM  10222  CD1 PHE C 470     -58.904  64.137   2.456  1.00 87.73           C  
+ANISOU10222  CD1 PHE C 470    11320  13280   8732   2700   2004  -2319       C  
+ATOM  10223  CD2 PHE C 470     -57.886  62.765   0.793  1.00 88.90           C  
+ANISOU10223  CD2 PHE C 470    11338  12968   9472   2383   1715  -1816       C  
+ATOM  10224  CE1 PHE C 470     -59.312  63.007   3.142  1.00 91.88           C  
+ANISOU10224  CE1 PHE C 470    11547  14197   9166   2526   2225  -2015       C  
+ATOM  10225  CE2 PHE C 470     -58.293  61.632   1.474  1.00 91.30           C  
+ANISOU10225  CE2 PHE C 470    11368  13596   9727   2221   1925  -1527       C  
+ATOM  10226  CZ  PHE C 470     -59.007  61.754   2.649  1.00 88.95           C  
+ANISOU10226  CZ  PHE C 470    10986  13730   9081   2278   2182  -1602       C  
+ATOM  10227  N   VAL C 471     -54.833  64.550  -0.233  1.00 89.87           N  
+ANISOU10227  N   VAL C 471    12287  12289   9571   2165   1067  -1995       N  
+ATOM  10228  CA  VAL C 471     -53.752  63.579  -0.397  1.00 95.54           C  
+ANISOU10228  CA  VAL C 471    12910  13009  10383   1896    948  -1647       C  
+ATOM  10229  C   VAL C 471     -52.449  64.126   0.194  1.00 95.20           C  
+ANISOU10229  C   VAL C 471    13109  12989  10072   1692    771  -1685       C  
+ATOM  10230  O   VAL C 471     -51.603  63.361   0.657  1.00 87.89           O  
+ANISOU10230  O   VAL C 471    12083  12254   9059   1501    703  -1407       O  
+ATOM  10231  CB  VAL C 471     -53.545  63.171  -1.879  1.00 88.51           C  
+ANISOU10231  CB  VAL C 471    11928  11801   9900   1887    837  -1529       C  
+ATOM  10232  CG1 VAL C 471     -54.830  62.589  -2.452  1.00 85.05           C  
+ANISOU10232  CG1 VAL C 471    11215  11390   9708   2048    984  -1519       C  
+ATOM  10233  CG2 VAL C 471     -53.068  64.339  -2.719  1.00 94.63           C  
+ANISOU10233  CG2 VAL C 471    12992  12232  10731   1926    667  -1740       C  
+ATOM  10234  N   GLU C 472     -52.286  65.447   0.165  1.00 90.52           N  
+ANISOU10234  N   GLU C 472    12832  12197   9366   1733    689  -2028       N  
+ATOM  10235  CA  GLU C 472     -51.119  66.085   0.766  1.00 88.80           C  
+ANISOU10235  CA  GLU C 472    12845  12012   8881   1495    521  -2140       C  
+ATOM  10236  C   GLU C 472     -51.151  65.927   2.282  1.00 93.98           C  
+ANISOU10236  C   GLU C 472    13482  13138   9089   1436    599  -2170       C  
+ATOM  10237  O   GLU C 472     -50.126  65.660   2.910  1.00 93.70           O  
+ANISOU10237  O   GLU C 472    13428  13348   8825   1199    458  -2035       O  
+ATOM  10238  CB  GLU C 472     -51.054  67.569   0.397  1.00 89.32           C  
+ANISOU10238  CB  GLU C 472    13293  11689   8957   1536    444  -2526       C  
+ATOM  10239  CG  GLU C 472     -50.309  67.863  -0.895  1.00 97.47           C  
+ANISOU10239  CG  GLU C 472    14424  12319  10291   1414    281  -2444       C  
+ATOM  10240  CD  GLU C 472     -50.477  69.302  -1.344  1.00110.04           C  
+ANISOU10240  CD  GLU C 472    16418  13454  11940   1500    245  -2770       C  
+ATOM  10241  OE1 GLU C 472     -51.203  70.057  -0.663  1.00123.53           O  
+ANISOU10241  OE1 GLU C 472    18321  15131  13481   1694    347  -3091       O  
+ATOM  10242  OE2 GLU C 472     -49.885  69.679  -2.377  1.00103.36           O  
+ANISOU10242  OE2 GLU C 472    15700  12269  11302   1383    129  -2699       O  
+ATOM  10243  N   ILE C 473     -52.337  66.102   2.859  1.00101.71           N  
+ANISOU10243  N   ILE C 473    14443  14283   9918   1663    823  -2349       N  
+ATOM  10244  CA  ILE C 473     -52.547  65.890   4.288  1.00 99.28           C  
+ANISOU10244  CA  ILE C 473    14095  14484   9144   1634    951  -2367       C  
+ATOM  10245  C   ILE C 473     -52.254  64.436   4.655  1.00102.69           C  
+ANISOU10245  C   ILE C 473    14223  15248   9545   1495    975  -1843       C  
+ATOM  10246  O   ILE C 473     -51.738  64.152   5.739  1.00110.37           O  
+ANISOU10246  O   ILE C 473    15190  16635  10112   1353    941  -1715       O  
+ATOM  10247  CB  ILE C 473     -53.984  66.288   4.711  1.00 93.65           C  
+ANISOU10247  CB  ILE C 473    13361  13904   8317   1936   1237  -2649       C  
+ATOM  10248  CG1 ILE C 473     -53.990  67.702   5.300  1.00 98.65           C  
+ANISOU10248  CG1 ILE C 473    14360  14468   8653   2018   1230  -3199       C  
+ATOM  10249  CG2 ILE C 473     -54.532  65.349   5.770  1.00 91.71           C  
+ANISOU10249  CG2 ILE C 473    12860  14219   7767   1919   1464  -2405       C  
+ATOM  10250  CD1 ILE C 473     -53.356  68.761   4.423  1.00 95.85           C  
+ANISOU10250  CD1 ILE C 473    14336  13537   8546   1980   1013  -3444       C  
+ATOM  10251  N   LEU C 474     -52.546  63.522   3.732  1.00105.22           N  
+ANISOU10251  N   LEU C 474    14311  15374  10295   1538   1018  -1541       N  
+ATOM  10252  CA  LEU C 474     -52.232  62.110   3.949  1.00108.18           C  
+ANISOU10252  CA  LEU C 474    14435  15936  10734   1418   1040  -1031       C  
+ATOM  10253  C   LEU C 474     -50.731  61.888   4.144  1.00116.24           C  
+ANISOU10253  C   LEU C 474    15495  17024  11647   1217    775   -820       C  
+ATOM  10254  O   LEU C 474     -50.321  61.051   4.950  1.00114.81           O  
+ANISOU10254  O   LEU C 474    15197  17168  11255   1135    765   -458       O  
+ATOM  10255  CB  LEU C 474     -52.737  61.257   2.785  1.00 96.86           C  
+ANISOU10255  CB  LEU C 474    12783  14196   9825   1479   1112   -831       C  
+ATOM  10256  CG  LEU C 474     -54.217  60.879   2.826  1.00 98.88           C  
+ANISOU10256  CG  LEU C 474    12838  14553  10178   1611   1400   -845       C  
+ATOM  10257  CD1 LEU C 474     -54.636  60.246   1.513  1.00 93.83           C  
+ANISOU10257  CD1 LEU C 474    12010  13580  10060   1643   1409   -761       C  
+ATOM  10258  CD2 LEU C 474     -54.486  59.937   3.991  1.00101.80           C  
+ANISOU10258  CD2 LEU C 474    13058  15331  10289   1512   1594   -497       C  
+ATOM  10259  N   SER C 475     -49.918  62.634   3.403  1.00115.84           N  
+ANISOU10259  N   SER C 475    15591  16686  11738   1141    561  -1024       N  
+ATOM  10260  CA  SER C 475     -48.467  62.522   3.512  1.00105.25           C  
+ANISOU10260  CA  SER C 475    14237  15441  10312    939    302   -870       C  
+ATOM  10261  C   SER C 475     -47.931  63.367   4.662  1.00108.32           C  
+ANISOU10261  C   SER C 475    14807  16178  10173    793    179  -1115       C  
+ATOM  10262  O   SER C 475     -47.037  64.192   4.475  1.00106.74           O  
+ANISOU10262  O   SER C 475    14748  15885   9925    614    -27  -1347       O  
+ATOM  10263  CB  SER C 475     -47.798  62.944   2.203  1.00102.57           C  
+ANISOU10263  CB  SER C 475    13948  14684  10340    872    150   -975       C  
+TER   10264      SER C 475                                                      
+ATOM  10265  N   HIS D   2     -14.494  42.266 -34.534  1.00105.67           N  
+ANISOU10265  N   HIS D   2    12727  18164   9258    508    331  -3347       N  
+ATOM  10266  CA  HIS D   2     -14.327  43.286 -35.553  1.00110.79           C  
+ANISOU10266  CA  HIS D   2    13371  19426   9296    593    238  -3029       C  
+ATOM  10267  C   HIS D   2     -12.999  43.988 -35.322  1.00101.69           C  
+ANISOU10267  C   HIS D   2    12307  18270   8061    656    473  -2537       C  
+ATOM  10268  O   HIS D   2     -12.018  43.746 -36.039  1.00107.32           O  
+ANISOU10268  O   HIS D   2    13023  19216   8537    727    636  -2585       O  
+ATOM  10269  CB  HIS D   2     -15.488  44.282 -35.519  1.00113.30           C  
+ANISOU10269  CB  HIS D   2    13648  19849   9551    568    -46  -2705       C  
+ATOM  10270  CG  HIS D   2     -15.422  45.332 -36.586  1.00120.61           C  
+ANISOU10270  CG  HIS D   2    14573  21379   9876    674   -152  -2332       C  
+ATOM  10271  ND1 HIS D   2     -16.551  45.955 -37.078  1.00126.89           N  
+ANISOU10271  ND1 HIS D   2    15290  22435  10488    703   -441  -2194       N  
+ATOM  10272  CD2 HIS D   2     -14.377  45.880 -37.251  1.00124.66           C  
+ANISOU10272  CD2 HIS D   2    15141  22097  10126    747      4  -1971       C  
+ATOM  10273  CE1 HIS D   2     -16.206  46.820 -38.012  1.00129.73           C  
+ANISOU10273  CE1 HIS D   2    15672  23127  10491    801   -446  -1770       C  
+ATOM  10274  NE2 HIS D   2     -14.889  46.799 -38.134  1.00130.55           N  
+ANISOU10274  NE2 HIS D   2    15859  23201  10544    816   -176  -1631       N  
+HETATM10275  N   MSE D   3     -12.989  44.871 -34.325  1.00 87.99           N  
+ANISOU10275  N   MSE D   3    10626  16178   6626    611    474  -2032       N  
+HETATM10276  CA  MSE D   3     -11.763  45.482 -33.847  1.00 80.35           C  
+ANISOU10276  CA  MSE D   3     9720  15092   5715    627    694  -1600       C  
+HETATM10277  C   MSE D   3     -10.955  44.434 -33.085  1.00 89.68           C  
+ANISOU10277  C   MSE D   3    10908  15887   7279    635    924  -1868       C  
+HETATM10278  O   MSE D   3     -11.435  43.321 -32.854  1.00 89.44           O  
+ANISOU10278  O   MSE D   3    10857  15612   7515    622    911  -2331       O  
+HETATM10279  CB  MSE D   3     -12.051  46.698 -32.956  1.00 73.62           C  
+ANISOU10279  CB  MSE D   3     8919  13947   5105    567    614  -1052       C  
+HETATM10280  CG  MSE D   3     -12.889  47.799 -33.623  1.00 74.95           C  
+ANISOU10280  CG  MSE D   3     9089  14434   4955    590    389   -728       C  
+HETATM10281 SE   MSE D   3     -13.136  49.411 -32.533  1.00131.25          SE  
+ANISOU10281 SE   MSE D   3    16298  21153  12418    536    324    -42      SE  
+HETATM10282  CE  MSE D   3     -11.414  50.287 -32.844  1.00 91.23           C  
+ANISOU10282  CE  MSE D   3    11283  16262   7120    520    608    444       C  
+ATOM  10283  N   ASN D   4      -9.731  44.782 -32.698  1.00 93.57           N  
+ANISOU10283  N   ASN D   4    11418  16322   7814    660   1136  -1571       N  
+ATOM  10284  CA  ASN D   4      -8.862  43.812 -32.046  1.00 91.69           C  
+ANISOU10284  CA  ASN D   4    11166  15782   7889    712   1358  -1791       C  
+ATOM  10285  C   ASN D   4      -9.463  43.345 -30.717  1.00 81.07           C  
+ANISOU10285  C   ASN D   4     9851  13838   7116    662   1314  -1851       C  
+ATOM  10286  O   ASN D   4     -10.144  44.115 -30.037  1.00 72.60           O  
+ANISOU10286  O   ASN D   4     8805  12563   6216    580   1171  -1558       O  
+ATOM  10287  CB  ASN D   4      -7.457  44.397 -31.854  1.00 98.98           C  
+ANISOU10287  CB  ASN D   4    12065  16805   8740    741   1571  -1424       C  
+ATOM  10288  CG  ASN D   4      -7.425  45.547 -30.870  1.00107.10           C  
+ANISOU10288  CG  ASN D   4    13122  17575   9997    641   1521   -910       C  
+ATOM  10289  OD1 ASN D   4      -7.507  45.346 -29.658  1.00111.28           O  
+ANISOU10289  OD1 ASN D   4    13666  17657  10959    619   1524   -878       O  
+ATOM  10290  ND2 ASN D   4      -7.288  46.762 -31.387  1.00113.20           N  
+ANISOU10290  ND2 ASN D   4    13904  18630  10478    584   1485   -503       N  
+ATOM  10291  N   PRO D   5      -9.217  42.074 -30.354  1.00 84.18           N  
+ANISOU10291  N   PRO D   5    10237  13946   7801    725   1452  -2227       N  
+ATOM  10292  CA  PRO D   5      -9.823  41.410 -29.191  1.00 82.49           C  
+ANISOU10292  CA  PRO D   5    10047  13175   8118    689   1441  -2328       C  
+ATOM  10293  C   PRO D   5      -9.751  42.193 -27.879  1.00 78.34           C  
+ANISOU10293  C   PRO D   5     9547  12345   7874    647   1429  -1866       C  
+ATOM  10294  O   PRO D   5     -10.693  42.125 -27.086  1.00 78.35           O  
+ANISOU10294  O   PRO D   5     9566  12016   8187    577   1328  -1849       O  
+ATOM  10295  CB  PRO D   5      -9.019  40.114 -29.083  1.00 84.84           C  
+ANISOU10295  CB  PRO D   5    10338  13279   8618    817   1674  -2661       C  
+ATOM  10296  CG  PRO D   5      -8.644  39.814 -30.487  1.00 89.17           C  
+ANISOU10296  CG  PRO D   5    10852  14295   8734    883   1718  -2986       C  
+ATOM  10297  CD  PRO D   5      -8.371  41.146 -31.126  1.00 87.24           C  
+ANISOU10297  CD  PRO D   5    10590  14541   8016    849   1640  -2598       C  
+ATOM  10298  N   ILE D   6      -8.662  42.919 -27.656  1.00 70.73           N  
+ANISOU10298  N   ILE D   6     8570  11506   6799    681   1534  -1519       N  
+ATOM  10299  CA  ILE D   6      -8.510  43.704 -26.436  1.00 67.52           C  
+ANISOU10299  CA  ILE D   6     8175  10850   6631    636   1519  -1122       C  
+ATOM  10300  C   ILE D   6      -9.549  44.822 -26.394  1.00 69.46           C  
+ANISOU10300  C   ILE D   6     8456  11112   6824    519   1299   -881       C  
+ATOM  10301  O   ILE D   6     -10.257  45.004 -25.394  1.00 69.56           O  
+ANISOU10301  O   ILE D   6     8491  10806   7134    473   1216   -781       O  
+ATOM  10302  CB  ILE D   6      -7.093  44.303 -26.325  1.00 64.08           C  
+ANISOU10302  CB  ILE D   6     7686  10594   6068    669   1668   -836       C  
+ATOM  10303  CG1 ILE D   6      -6.044  43.188 -26.312  1.00 74.73           C  
+ANISOU10303  CG1 ILE D   6     8976  11933   7487    822   1888  -1064       C  
+ATOM  10304  CG2 ILE D   6      -6.973  45.169 -25.080  1.00 61.64           C  
+ANISOU10304  CG2 ILE D   6     7377  10050   5992    603   1629   -475       C  
+ATOM  10305  CD1 ILE D   6      -4.618  43.687 -26.209  1.00 81.51           C  
+ANISOU10305  CD1 ILE D   6     9736  13003   8231    858   2042   -816       C  
+ATOM  10306  N   VAL D   7      -9.646  45.553 -27.500  1.00 69.91           N  
+ANISOU10306  N   VAL D   7     8513  11557   6491    491   1215   -783       N  
+ATOM  10307  CA  VAL D   7     -10.611  46.636 -27.634  1.00 66.79           C  
+ANISOU10307  CA  VAL D   7     8149  11217   6010    418   1008   -538       C  
+ATOM  10308  C   VAL D   7     -12.039  46.109 -27.524  1.00 70.19           C  
+ANISOU10308  C   VAL D   7     8570  11490   6608    394    835   -805       C  
+ATOM  10309  O   VAL D   7     -12.884  46.736 -26.894  1.00 73.35           O  
+ANISOU10309  O   VAL D   7     8982  11699   7189    349    699   -628       O  
+ATOM  10310  CB  VAL D   7     -10.431  47.385 -28.972  1.00 68.85           C  
+ANISOU10310  CB  VAL D   7     8410  11967   5783    426    965   -379       C  
+ATOM  10311  CG1 VAL D   7     -11.582  48.355 -29.212  1.00 69.02           C  
+ANISOU10311  CG1 VAL D   7     8457  12049   5717    395    732   -159       C  
+ATOM  10312  CG2 VAL D   7      -9.098  48.120 -28.991  1.00 66.47           C  
+ANISOU10312  CG2 VAL D   7     8101  11794   5362    409   1138    -39       C  
+ATOM  10313  N   GLU D   8     -12.302  44.952 -28.126  1.00 73.26           N  
+ANISOU10313  N   GLU D   8     8926  11957   6954    419    848  -1250       N  
+ATOM  10314  CA  GLU D   8     -13.628  44.340 -28.058  1.00 76.22           C  
+ANISOU10314  CA  GLU D   8     9260  12185   7516    365    698  -1556       C  
+ATOM  10315  C   GLU D   8     -13.999  43.959 -26.625  1.00 81.41           C  
+ANISOU10315  C   GLU D   8     9925  12324   8683    326    750  -1526       C  
+ATOM  10316  O   GLU D   8     -15.129  44.194 -26.178  1.00 86.81           O  
+ANISOU10316  O   GLU D   8    10576  12860   9549    263    605  -1498       O  
+ATOM  10317  CB  GLU D   8     -13.698  43.110 -28.965  1.00 70.10           C  
+ANISOU10317  CB  GLU D   8     8442  11562   6629    381    731  -2090       C  
+ATOM  10318  CG  GLU D   8     -13.519  43.419 -30.443  1.00 76.10           C  
+ANISOU10318  CG  GLU D   8     9178  12906   6831    427    658  -2173       C  
+ATOM  10319  CD  GLU D   8     -14.718  44.133 -31.041  1.00 79.22           C  
+ANISOU10319  CD  GLU D   8     9521  13588   6992    391    378  -2108       C  
+ATOM  10320  OE1 GLU D   8     -15.797  44.114 -30.412  1.00 82.04           O  
+ANISOU10320  OE1 GLU D   8     9834  13685   7652    318    241  -2141       O  
+ATOM  10321  OE2 GLU D   8     -14.585  44.712 -32.140  1.00 89.54           O  
+ANISOU10321  OE2 GLU D   8    10817  15400   7803    448    301  -2008       O  
+ATOM  10322  N   LEU D   9     -13.038  43.378 -25.911  1.00 76.85           N  
+ANISOU10322  N   LEU D   9     9379  11502   8318    381    961  -1516       N  
+ATOM  10323  CA  LEU D   9     -13.234  43.013 -24.512  1.00 72.64           C  
+ANISOU10323  CA  LEU D   9     8858  10517   8224    374   1037  -1435       C  
+ATOM  10324  C   LEU D   9     -13.566  44.252 -23.691  1.00 69.36           C  
+ANISOU10324  C   LEU D   9     8458  10029   7867    337    934  -1036       C  
+ATOM  10325  O   LEU D   9     -14.510  44.249 -22.887  1.00 74.76           O  
+ANISOU10325  O   LEU D   9     9124  10465   8818    291    871  -1010       O  
+ATOM  10326  CB  LEU D   9     -11.989  42.321 -23.952  1.00 71.28           C  
+ANISOU10326  CB  LEU D   9     8709  10178   8197    482   1273  -1425       C  
+ATOM  10327  CG  LEU D   9     -11.929  40.800 -24.092  1.00 72.78           C  
+ANISOU10327  CG  LEU D   9     8897  10157   8601    534   1417  -1823       C  
+ATOM  10328  CD1 LEU D   9     -10.598  40.269 -23.587  1.00 70.28           C  
+ANISOU10328  CD1 LEU D   9     8591   9727   8387    688   1643  -1749       C  
+ATOM  10329  CD2 LEU D   9     -13.081  40.162 -23.335  1.00 72.00           C  
+ANISOU10329  CD2 LEU D   9     8789   9665   8902    454   1393  -1940       C  
+ATOM  10330  N   PHE D  10     -12.793  45.314 -23.908  1.00 64.49           N  
+ANISOU10330  N   PHE D  10     7866   9625   7011    353    930   -737       N  
+ATOM  10331  CA  PHE D  10     -13.071  46.584 -23.251  1.00 68.03           C  
+ANISOU10331  CA  PHE D  10     8336  10004   7509    314    832   -384       C  
+ATOM  10332  C   PHE D  10     -14.475  47.080 -23.569  1.00 65.61           C  
+ANISOU10332  C   PHE D  10     8008   9743   7179    272    619   -390       C  
+ATOM  10333  O   PHE D  10     -15.181  47.564 -22.688  1.00 66.15           O  
+ANISOU10333  O   PHE D  10     8071   9598   7465    253    549   -258       O  
+ATOM  10334  CB  PHE D  10     -12.060  47.654 -23.658  1.00 64.82           C  
+ANISOU10334  CB  PHE D  10     7953   9825   6849    309    863    -86       C  
+ATOM  10335  CG  PHE D  10     -12.542  49.055 -23.408  1.00 64.43           C  
+ANISOU10335  CG  PHE D  10     7936   9743   6802    262    729    235       C  
+ATOM  10336  CD1 PHE D  10     -12.635  49.548 -22.117  1.00 61.18           C  
+ANISOU10336  CD1 PHE D  10     7537   9041   6669    243    730    389       C  
+ATOM  10337  CD2 PHE D  10     -12.918  49.875 -24.461  1.00 70.82           C  
+ANISOU10337  CD2 PHE D  10     8763  10814   7333    254    606    380       C  
+ATOM  10338  CE1 PHE D  10     -13.086  50.832 -21.880  1.00 62.13           C  
+ANISOU10338  CE1 PHE D  10     7690   9094   6823    211    616    648       C  
+ATOM  10339  CE2 PHE D  10     -13.369  51.161 -24.229  1.00 70.11           C  
+ANISOU10339  CE2 PHE D  10     8710  10645   7285    234    494    688       C  
+ATOM  10340  CZ  PHE D  10     -13.453  51.640 -22.937  1.00 62.57           C  
+ANISOU10340  CZ  PHE D  10     7770   9360   6642    209    503    804       C  
+ATOM  10341  N   ILE D  11     -14.867  46.972 -24.834  1.00 67.25           N  
+ANISOU10341  N   ILE D  11     8187  10263   7101    272    513   -549       N  
+ATOM  10342  CA  ILE D  11     -16.182  47.423 -25.266  1.00 69.24           C  
+ANISOU10342  CA  ILE D  11     8388  10635   7286    256    290   -562       C  
+ATOM  10343  C   ILE D  11     -17.283  46.672 -24.531  1.00 72.11           C  
+ANISOU10343  C   ILE D  11     8677  10719   8001    206    249   -797       C  
+ATOM  10344  O   ILE D  11     -18.254  47.280 -24.093  1.00 75.49           O  
+ANISOU10344  O   ILE D  11     9062  11066   8556    198    118   -674       O  
+ATOM  10345  CB  ILE D  11     -16.364  47.271 -26.791  1.00 74.45           C  
+ANISOU10345  CB  ILE D  11     9008  11744   7534    278    181   -742       C  
+ATOM  10346  CG1 ILE D  11     -15.535  48.329 -27.521  1.00 79.92           C  
+ANISOU10346  CG1 ILE D  11     9766  12740   7861    327    197   -392       C  
+ATOM  10347  CG2 ILE D  11     -17.824  47.429 -27.181  1.00 73.58           C  
+ANISOU10347  CG2 ILE D  11     8800  11766   7391    269    -62   -850       C  
+ATOM  10348  CD1 ILE D  11     -15.543  48.190 -29.026  1.00 82.73           C  
+ANISOU10348  CD1 ILE D  11    10089  13602   7743    372    121   -531       C  
+ATOM  10349  N   LYS D  12     -17.122  45.364 -24.355  1.00 72.49           N  
+ANISOU10349  N   LYS D  12     8707  10601   8234    176    380  -1120       N  
+ATOM  10350  CA  LYS D  12     -18.164  44.586 -23.692  1.00 72.65           C  
+ANISOU10350  CA  LYS D  12     8649  10341   8615    103    372  -1334       C  
+ATOM  10351  C   LYS D  12     -18.227  44.909 -22.198  1.00 70.54           C  
+ANISOU10351  C   LYS D  12     8408   9728   8666    113    458  -1069       C  
+ATOM  10352  O   LYS D  12     -19.312  45.125 -21.641  1.00 72.23           O  
+ANISOU10352  O   LYS D  12     8548   9825   9073     73    373  -1040       O  
+ATOM  10353  CB  LYS D  12     -17.943  43.087 -23.900  1.00 72.78           C  
+ANISOU10353  CB  LYS D  12     8651  10215   8786     66    514  -1737       C  
+ATOM  10354  CG  LYS D  12     -19.159  42.365 -24.464  1.00 84.30           C  
+ANISOU10354  CG  LYS D  12     9981  11713  10335    -48    389  -2138       C  
+ATOM  10355  CD  LYS D  12     -18.903  40.877 -24.650  1.00 88.49           C  
+ANISOU10355  CD  LYS D  12    10511  12038  11075    -96    551  -2560       C  
+ATOM  10356  CE  LYS D  12     -20.210  40.110 -24.804  1.00 94.61           C  
+ANISOU10356  CE  LYS D  12    11138  12708  12100   -258    461  -2943       C  
+ATOM  10357  NZ  LYS D  12     -21.169  40.397 -23.698  1.00 85.97           N  
+ANISOU10357  NZ  LYS D  12     9970  11361  11335   -327    440  -2732       N  
+ATOM  10358  N   ASP D  13     -17.061  44.972 -21.559  1.00 62.56           N  
+ANISOU10358  N   ASP D  13     7486   8598   7688    175    624   -882       N  
+ATOM  10359  CA  ASP D  13     -17.000  45.239 -20.124  1.00 61.00           C  
+ANISOU10359  CA  ASP D  13     7310   8123   7743    200    710   -651       C  
+ATOM  10360  C   ASP D  13     -17.561  46.625 -19.798  1.00 61.29           C  
+ANISOU10360  C   ASP D  13     7342   8213   7732    203    561   -388       C  
+ATOM  10361  O   ASP D  13     -18.406  46.783 -18.905  1.00 60.85           O  
+ANISOU10361  O   ASP D  13     7242   7983   7897    194    540   -334       O  
+ATOM  10362  CB  ASP D  13     -15.555  45.121 -19.628  1.00 77.34           C  
+ANISOU10362  CB  ASP D  13     9449  10141   9794    277    884   -512       C  
+ATOM  10363  CG  ASP D  13     -15.416  45.405 -18.142  1.00 89.22           C  
+ANISOU10363  CG  ASP D  13    10967  11426  11507    316    961   -287       C  
+ATOM  10364  OD1 ASP D  13     -16.431  45.346 -17.416  1.00105.02           O  
+ANISOU10364  OD1 ASP D  13    12930  13258  13717    289    936   -282       O  
+ATOM  10365  OD2 ASP D  13     -14.283  45.690 -17.699  1.00 76.38           O  
+ANISOU10365  OD2 ASP D  13     9374   9828   9820    375   1047   -124       O  
+ATOM  10366  N   PHE D  14     -17.107  47.625 -20.545  1.00 66.37           N  
+ANISOU10366  N   PHE D  14     8029   9092   8096    223    471   -221       N  
+ATOM  10367  CA  PHE D  14     -17.513  48.999 -20.295  1.00 73.03           C  
+ANISOU10367  CA  PHE D  14     8887   9946   8914    242    347     46       C  
+ATOM  10368  C   PHE D  14     -18.967  49.207 -20.699  1.00 68.04           C  
+ANISOU10368  C   PHE D  14     8165   9390   8297    241    160    -31       C  
+ATOM  10369  O   PHE D  14     -19.667  50.028 -20.107  1.00 65.66           O  
+ANISOU10369  O   PHE D  14     7842   8989   8117    274     80    120       O  
+ATOM  10370  CB  PHE D  14     -16.609  49.979 -21.043  1.00 66.46           C  
+ANISOU10370  CB  PHE D  14     8128   9318   7806    255    326    274       C  
+ATOM  10371  CG  PHE D  14     -16.609  51.361 -20.459  1.00 63.65           C  
+ANISOU10371  CG  PHE D  14     7818   8850   7515    267    276    573       C  
+ATOM  10372  CD1 PHE D  14     -16.065  51.593 -19.206  1.00 60.00           C  
+ANISOU10372  CD1 PHE D  14     7381   8164   7250    259    380    658       C  
+ATOM  10373  CD2 PHE D  14     -17.165  52.424 -21.150  1.00 64.68           C  
+ANISOU10373  CD2 PHE D  14     7963   9097   7515    299    124    759       C  
+ATOM  10374  CE1 PHE D  14     -16.063  52.860 -18.658  1.00 57.58           C  
+ANISOU10374  CE1 PHE D  14     7116   7736   7025    260    336    876       C  
+ATOM  10375  CE2 PHE D  14     -17.168  53.695 -20.606  1.00 61.66           C  
+ANISOU10375  CE2 PHE D  14     7634   8554   7241    315     93   1017       C  
+ATOM  10376  CZ  PHE D  14     -16.616  53.912 -19.358  1.00 64.19           C  
+ANISOU10376  CZ  PHE D  14     7981   8634   7775    284    200   1051       C  
+ATOM  10377  N   THR D  15     -19.419  48.465 -21.708  1.00 67.04           N  
+ANISOU10377  N   THR D  15     7970   9458   8045    210     87   -289       N  
+ATOM  10378  CA  THR D  15     -20.830  48.484 -22.080  1.00 69.90           C  
+ANISOU10378  CA  THR D  15     8200   9927   8434    200    -98   -418       C  
+ATOM  10379  C   THR D  15     -21.665  48.005 -20.905  1.00 70.40           C  
+ANISOU10379  C   THR D  15     8176   9697   8874    156    -39   -505       C  
+ATOM  10380  O   THR D  15     -22.673  48.624 -20.558  1.00 68.89           O  
+ANISOU10380  O   THR D  15     7898   9491   8787    187   -153   -421       O  
+ATOM  10381  CB  THR D  15     -21.128  47.602 -23.308  1.00 70.27           C  
+ANISOU10381  CB  THR D  15     8164  10244   8292    152   -181   -760       C  
+ATOM  10382  OG1 THR D  15     -20.518  48.173 -24.472  1.00 72.66           O  
+ANISOU10382  OG1 THR D  15     8528  10894   8185    213   -255   -648       O  
+ATOM  10383  CG2 THR D  15     -22.626  47.479 -23.534  1.00 71.32           C  
+ANISOU10383  CG2 THR D  15     8115  10478   8507    118   -371   -943       C  
+ATOM  10384  N   LYS D  16     -21.240  46.903 -20.291  1.00 65.30           N  
+ANISOU10384  N   LYS D  16     7550   8825   8436     99    152   -655       N  
+ATOM  10385  CA  LYS D  16     -21.930  46.398 -19.110  1.00 61.14           C  
+ANISOU10385  CA  LYS D  16     6951   8016   8263     58    253   -689       C  
+ATOM  10386  C   LYS D  16     -21.948  47.445 -18.001  1.00 62.61           C  
+ANISOU10386  C   LYS D  16     7177   8083   8528    138    270   -387       C  
+ATOM  10387  O   LYS D  16     -22.980  47.669 -17.367  1.00 62.10           O  
+ANISOU10387  O   LYS D  16     7009   7943   8643    139    236   -367       O  
+ATOM  10388  CB  LYS D  16     -21.293  45.108 -18.592  1.00 58.19           C  
+ANISOU10388  CB  LYS D  16     6624   7397   8090     18    483   -818       C  
+ATOM  10389  CG  LYS D  16     -21.978  44.592 -17.333  1.00 60.80           C  
+ANISOU10389  CG  LYS D  16     6886   7442   8774    -19    616   -792       C  
+ATOM  10390  CD  LYS D  16     -21.374  43.302 -16.814  1.00 65.43           C  
+ANISOU10390  CD  LYS D  16     7524   7760   9578    -35    855   -869       C  
+ATOM  10391  CE  LYS D  16     -21.982  42.937 -15.468  1.00 59.92           C  
+ANISOU10391  CE  LYS D  16     6772   6803   9193    -49   1008   -748       C  
+ATOM  10392  NZ  LYS D  16     -21.329  41.751 -14.849  1.00 58.46           N  
+ANISOU10392  NZ  LYS D  16     6654   6338   9221    -27   1259   -735       N  
+ATOM  10393  N   GLU D  17     -20.806  48.087 -17.771  1.00 58.53           N  
+ANISOU10393  N   GLU D  17     6795   7563   7882    201    327   -177       N  
+ATOM  10394  CA  GLU D  17     -20.711  49.082 -16.703  1.00 56.47           C  
+ANISOU10394  CA  GLU D  17     6576   7186   7695    266    346     60       C  
+ATOM  10395  C   GLU D  17     -21.584  50.310 -16.967  1.00 59.86           C  
+ANISOU10395  C   GLU D  17     6963   7702   8077    321    161    178       C  
+ATOM  10396  O   GLU D  17     -22.144  50.894 -16.039  1.00 62.90           O  
+ANISOU10396  O   GLU D  17     7316   7967   8615    372    161    265       O  
+ATOM  10397  CB  GLU D  17     -19.258  49.509 -16.504  1.00 62.37           C  
+ANISOU10397  CB  GLU D  17     7449   7932   8316    294    432    221       C  
+ATOM  10398  CG  GLU D  17     -18.366  48.411 -15.943  1.00 70.99           C  
+ANISOU10398  CG  GLU D  17     8570   8918   9485    293    626    156       C  
+ATOM  10399  CD  GLU D  17     -18.798  47.966 -14.555  1.00 67.37           C  
+ANISOU10399  CD  GLU D  17     8072   8259   9267    321    744    176       C  
+ATOM  10400  OE1 GLU D  17     -18.681  46.761 -14.248  1.00 72.72           O  
+ANISOU10400  OE1 GLU D  17     8735   8817  10078    316    890     83       O  
+ATOM  10401  OE2 GLU D  17     -19.250  48.824 -13.766  1.00 58.45           O  
+ANISOU10401  OE2 GLU D  17     6928   7088   8193    356    703    292       O  
+ATOM  10402  N   VAL D  18     -21.687  50.700 -18.235  1.00 62.48           N  
+ANISOU10402  N   VAL D  18     7294   8257   8188    330      9    187       N  
+ATOM  10403  CA  VAL D  18     -22.515  51.837 -18.640  1.00 64.62           C  
+ANISOU10403  CA  VAL D  18     7524   8629   8400    415   -178    330       C  
+ATOM  10404  C   VAL D  18     -23.988  51.503 -18.462  1.00 68.06           C  
+ANISOU10404  C   VAL D  18     7774   9082   9003    422   -267    174       C  
+ATOM  10405  O   VAL D  18     -24.776  52.311 -17.960  1.00 76.88           O  
+ANISOU10405  O   VAL D  18     8832  10140  10241    512   -335    281       O  
+ATOM  10406  CB  VAL D  18     -22.260  52.230 -20.109  1.00 68.84           C  
+ANISOU10406  CB  VAL D  18     8093   9450   8614    441   -313    403       C  
+ATOM  10407  CG1 VAL D  18     -23.399  53.070 -20.662  1.00 70.77           C  
+ANISOU10407  CG1 VAL D  18     8245   9845   8801    550   -528    505       C  
+ATOM  10408  CG2 VAL D  18     -20.939  52.953 -20.246  1.00 68.03           C  
+ANISOU10408  CG2 VAL D  18     8153   9326   8368    443   -234    639       C  
+HETATM10409  N   MSE D  19     -24.345  50.297 -18.888  1.00 78.47           N  
+ANISOU10409  N   MSE D  19     8989  10480  10346    323   -258    -98       N  
+HETATM10410  CA  MSE D  19     -25.722  49.843 -18.859  1.00 72.83           C  
+ANISOU10410  CA  MSE D  19     8061   9815   9796    286   -342   -289       C  
+HETATM10411  C   MSE D  19     -26.190  49.681 -17.427  1.00 68.90           C  
+ANISOU10411  C   MSE D  19     7506   9060   9614    276   -191   -265       C  
+HETATM10412  O   MSE D  19     -27.376  49.809 -17.137  1.00 70.04           O  
+ANISOU10412  O   MSE D  19     7470   9231   9912    293   -256   -313       O  
+HETATM10413  CB  MSE D  19     -25.858  48.521 -19.600  1.00 75.81           C  
+ANISOU10413  CB  MSE D  19     8351  10292  10163    145   -339   -624       C  
+HETATM10414  CG  MSE D  19     -27.212  48.269 -20.213  1.00 75.22           C  
+ANISOU10414  CG  MSE D  19     8031  10431  10120    100   -524   -847       C  
+HETATM10415 SE   MSE D  19     -26.971  47.155 -21.799  1.00329.30          SE  
+ANISOU10415 SE   MSE D  19    40166  42901  42050    -25   -621  -1249      SE  
+HETATM10416  CE  MSE D  19     -25.905  45.701 -21.040  1.00 95.70           C  
+ANISOU10416  CE  MSE D  19    10727  12902  12735   -165   -278  -1412       C  
+ATOM  10417  N   GLU D  20     -25.248  49.398 -16.535  1.00 65.72           N  
+ANISOU10417  N   GLU D  20     7241   8443   9287    262     11   -186       N  
+ATOM  10418  CA  GLU D  20     -25.579  49.183 -15.144  1.00 58.77           C  
+ANISOU10418  CA  GLU D  20     6318   7356   8656    265    176   -144       C  
+ATOM  10419  C   GLU D  20     -25.410  50.503 -14.383  1.00 57.38           C  
+ANISOU10419  C   GLU D  20     6220   7127   8455    402    160     81       C  
+ATOM  10420  O   GLU D  20     -25.540  50.558 -13.153  1.00 59.13           O  
+ANISOU10420  O   GLU D  20     6430   7216   8820    439    293    138       O  
+ATOM  10421  CB  GLU D  20     -24.702  48.082 -14.559  1.00 53.84           C  
+ANISOU10421  CB  GLU D  20     5782   6554   8120    198    401   -180       C  
+ATOM  10422  CG  GLU D  20     -25.137  46.670 -14.964  1.00 54.40           C  
+ANISOU10422  CG  GLU D  20     5750   6571   8350     55    469   -430       C  
+ATOM  10423  CD  GLU D  20     -26.521  46.308 -14.471  1.00 64.99           C  
+ANISOU10423  CD  GLU D  20     6879   7860   9952    -17    495   -523       C  
+ATOM  10424  OE1 GLU D  20     -26.924  46.829 -13.409  1.00 72.62           O  
+ANISOU10424  OE1 GLU D  20     7809   8768  11015     57    563   -366       O  
+ATOM  10425  OE2 GLU D  20     -27.199  45.485 -15.126  1.00 74.38           O  
+ANISOU10425  OE2 GLU D  20     7927   9078  11257   -154    457   -771       O  
+ATOM  10426  N   GLU D  21     -25.115  51.552 -15.151  1.00 62.80           N  
+ANISOU10426  N   GLU D  21     6985   7921   8954    476      4    204       N  
+ATOM  10427  CA  GLU D  21     -25.048  52.919 -14.667  1.00 70.91           C  
+ANISOU10427  CA  GLU D  21     8083   8876   9983    599    -40    394       C  
+ATOM  10428  C   GLU D  21     -23.984  53.058 -13.582  1.00 63.65           C  
+ANISOU10428  C   GLU D  21     7299   7794   9092    596    125    471       C  
+ATOM  10429  O   GLU D  21     -24.168  53.769 -12.598  1.00 77.51           O  
+ANISOU10429  O   GLU D  21     9060   9443  10948    675    163    526       O  
+ATOM  10430  CB  GLU D  21     -26.426  53.371 -14.173  1.00 72.24           C  
+ANISOU10430  CB  GLU D  21     8086   9040  10321    695   -100    373       C  
+ATOM  10431  CG  GLU D  21     -27.534  53.142 -15.210  1.00 75.57           C  
+ANISOU10431  CG  GLU D  21     8324   9671  10717    697   -279    272       C  
+ATOM  10432  CD  GLU D  21     -28.776  53.962 -14.943  1.00 73.91           C  
+ANISOU10432  CD  GLU D  21     7954   9496  10633    846   -383    310       C  
+ATOM  10433  OE1 GLU D  21     -29.805  53.748 -15.623  1.00 91.70           O  
+ANISOU10433  OE1 GLU D  21    10005  11947  12891    857   -530    212       O  
+ATOM  10434  OE2 GLU D  21     -28.711  54.854 -14.074  1.00 78.79           O  
+ANISOU10434  OE2 GLU D  21     8639   9958  11341    961   -326    424       O  
+ATOM  10435  N   ASN D  22     -22.874  52.351 -13.779  1.00 52.37           N  
+ANISOU10435  N   ASN D  22     5961   6372   7564    515    219    453       N  
+ATOM  10436  CA  ASN D  22     -21.757  52.352 -12.846  1.00 49.86           C  
+ANISOU10436  CA  ASN D  22     5745   5959   7241    513    362    516       C  
+ATOM  10437  C   ASN D  22     -20.432  52.703 -13.525  1.00 57.84           C  
+ANISOU10437  C   ASN D  22     6880   7027   8069    473    348    607       C  
+ATOM  10438  O   ASN D  22     -19.357  52.449 -12.980  1.00 65.10           O  
+ANISOU10438  O   ASN D  22     7857   7922   8957    454    462    630       O  
+ATOM  10439  CB  ASN D  22     -21.638  50.978 -12.165  1.00 52.33           C  
+ANISOU10439  CB  ASN D  22     6018   6217   7650    474    538    425       C  
+ATOM  10440  CG  ASN D  22     -20.801  51.018 -10.894  1.00 50.53           C  
+ANISOU10440  CG  ASN D  22     5847   5925   7428    520    676    503       C  
+ATOM  10441  OD1 ASN D  22     -21.004  51.869 -10.027  1.00 64.57           O  
+ANISOU10441  OD1 ASN D  22     7623   7673   9237    586    669    550       O  
+ATOM  10442  ND2 ASN D  22     -19.849  50.097 -10.785  1.00 48.89           N  
+ANISOU10442  ND2 ASN D  22     5681   5714   7180    501    799    504       N  
+ATOM  10443  N   ALA D  23     -20.506  53.294 -14.713  1.00 61.91           N  
+ANISOU10443  N   ALA D  23     7422   7645   8454    469    213    673       N  
+ATOM  10444  CA  ALA D  23     -19.298  53.706 -15.415  1.00 53.15           C  
+ANISOU10444  CA  ALA D  23     6417   6610   7168    423    216    788       C  
+ATOM  10445  C   ALA D  23     -18.944  55.151 -15.084  1.00 51.26           C  
+ANISOU10445  C   ALA D  23     6255   6258   6965    443    179    965       C  
+ATOM  10446  O   ALA D  23     -19.824  55.969 -14.818  1.00 51.47           O  
+ANISOU10446  O   ALA D  23     6264   6184   7107    520     95   1011       O  
+ATOM  10447  CB  ALA D  23     -19.468  53.530 -16.915  1.00 56.92           C  
+ANISOU10447  CB  ALA D  23     6886   7291   7448    408    113    786       C  
+ATOM  10448  N   ALA D  24     -17.653  55.464 -15.109  1.00 50.61           N  
+ANISOU10448  N   ALA D  24     6245   6180   6805    372    249   1051       N  
+ATOM  10449  CA  ALA D  24     -17.196  56.830 -14.882  1.00 52.66           C  
+ANISOU10449  CA  ALA D  24     6577   6306   7127    349    227   1202       C  
+ATOM  10450  C   ALA D  24     -16.213  57.258 -15.966  1.00 55.31           C  
+ANISOU10450  C   ALA D  24     6975   6743   7299    262    237   1374       C  
+ATOM  10451  O   ALA D  24     -15.531  56.422 -16.558  1.00 65.08           O  
+ANISOU10451  O   ALA D  24     8195   8164   8367    216    301   1338       O  
+ATOM  10452  CB  ALA D  24     -16.560  56.959 -13.506  1.00 48.10           C  
+ANISOU10452  CB  ALA D  24     5993   5618   6664    323    318   1119       C  
+ATOM  10453  N   ILE D  25     -16.138  58.559 -16.220  1.00 53.75           N  
+ANISOU10453  N   ILE D  25     6847   6414   7163    245    192   1566       N  
+ATOM  10454  CA  ILE D  25     -15.182  59.090 -17.186  1.00 53.81           C  
+ANISOU10454  CA  ILE D  25     6911   6499   7036    147    229   1777       C  
+ATOM  10455  C   ILE D  25     -14.195  60.012 -16.482  1.00 59.41           C  
+ANISOU10455  C   ILE D  25     7652   7016   7906     21    307   1831       C  
+ATOM  10456  O   ILE D  25     -14.609  60.858 -15.708  1.00 62.05           O  
+ANISOU10456  O   ILE D  25     8015   7098   8462     45    271   1812       O  
+ATOM  10457  CB  ILE D  25     -15.891  59.864 -18.320  1.00 52.12           C  
+ANISOU10457  CB  ILE D  25     6753   6305   6746    224    121   2022       C  
+ATOM  10458  CG1 ILE D  25     -16.818  58.936 -19.109  1.00 53.87           C  
+ANISOU10458  CG1 ILE D  25     6913   6782   6774    331     24   1933       C  
+ATOM  10459  CG2 ILE D  25     -14.876  60.518 -19.246  1.00 52.47           C  
+ANISOU10459  CG2 ILE D  25     6861   6414   6662    116    191   2293       C  
+ATOM  10460  CD1 ILE D  25     -16.089  57.876 -19.905  1.00 54.40           C  
+ANISOU10460  CD1 ILE D  25     6949   7148   6573    268     93   1850       C  
+ATOM  10461  N   PHE D  26     -12.899  59.863 -16.743  1.00 52.98           N  
+ANISOU10461  N   PHE D  26     6816   6325   6990   -116    414   1875       N  
+ATOM  10462  CA  PHE D  26     -11.940  60.857 -16.270  1.00 52.23           C  
+ANISOU10462  CA  PHE D  26     6728   6062   7053   -272    479   1941       C  
+ATOM  10463  C   PHE D  26     -11.333  61.510 -17.506  1.00 54.70           C  
+ANISOU10463  C   PHE D  26     7088   6430   7266   -377    532   2239       C  
+ATOM  10464  O   PHE D  26     -10.692  60.843 -18.316  1.00 64.02           O  
+ANISOU10464  O   PHE D  26     8226   7891   8206   -411    604   2290       O  
+ATOM  10465  CB  PHE D  26     -10.843  60.233 -15.396  1.00 50.71           C  
+ANISOU10465  CB  PHE D  26     6431   5985   6851   -359    568   1747       C  
+ATOM  10466  CG  PHE D  26     -10.070  61.235 -14.558  1.00 67.08           C  
+ANISOU10466  CG  PHE D  26     8478   7877   9133   -515    597   1708       C  
+ATOM  10467  CD1 PHE D  26     -10.058  62.586 -14.877  1.00 80.49           C  
+ANISOU10467  CD1 PHE D  26    10254   9316  11014   -623    592   1884       C  
+ATOM  10468  CD2 PHE D  26      -9.339  60.813 -13.458  1.00 74.73           C  
+ANISOU10468  CD2 PHE D  26     9335   8938  10119   -553    631   1491       C  
+ATOM  10469  CE1 PHE D  26      -9.353  63.495 -14.108  1.00 86.19           C  
+ANISOU10469  CE1 PHE D  26    10942   9846  11960   -793    621   1800       C  
+ATOM  10470  CE2 PHE D  26      -8.625  61.718 -12.688  1.00 77.56           C  
+ANISOU10470  CE2 PHE D  26     9645   9168  10656   -710    640   1405       C  
+ATOM  10471  CZ  PHE D  26      -8.634  63.060 -13.015  1.00 82.36           C  
+ANISOU10471  CZ  PHE D  26    10329   9490  11472   -845    636   1537       C  
+ATOM  10472  N   ALA D  27     -11.532  62.817 -17.643  1.00 52.93           N  
+ANISOU10472  N   ALA D  27     6949   5930   7230   -421    513   2444       N  
+ATOM  10473  CA  ALA D  27     -11.171  63.509 -18.874  1.00 55.18           C  
+ANISOU10473  CA  ALA D  27     7297   6245   7425   -491    568   2801       C  
+ATOM  10474  C   ALA D  27      -9.926  64.374 -18.718  1.00 64.93           C  
+ANISOU10474  C   ALA D  27     8513   7327   8832   -741    702   2913       C  
+ATOM  10475  O   ALA D  27      -9.854  65.228 -17.834  1.00 61.02           O  
+ANISOU10475  O   ALA D  27     8036   6496   8653   -829    698   2832       O  
+ATOM  10476  CB  ALA D  27     -12.335  64.359 -19.355  1.00 58.16           C  
+ANISOU10476  CB  ALA D  27     7788   6421   7888   -339    463   3031       C  
+ATOM  10477  N   GLY D  28      -8.949  64.140 -19.587  1.00 69.62           N  
+ANISOU10477  N   GLY D  28     9054   8181   9217   -860    826   3078       N  
+ATOM  10478  CA  GLY D  28      -7.758  64.965 -19.651  1.00 65.81           C  
+ANISOU10478  CA  GLY D  28     8529   7592   8884  -1121    973   3235       C  
+ATOM  10479  C   GLY D  28      -7.903  66.049 -20.702  1.00 72.81           C  
+ANISOU10479  C   GLY D  28     9541   8333   9791  -1145   1017   3621       C  
+ATOM  10480  O   GLY D  28      -8.948  66.164 -21.342  1.00 78.72           O  
+ANISOU10480  O   GLY D  28    10403   9083  10425   -939    916   3767       O  
+ATOM  10481  N   ALA D  29      -6.855  66.848 -20.875  1.00 76.52           N  
+ANISOU10481  N   ALA D  29     9989   8700  10384  -1374   1151   3707       N  
+ATOM  10482  CA  ALA D  29      -6.893  67.981 -21.794  1.00 70.50           C  
+ANISOU10482  CA  ALA D  29     9362   7766   9660  -1397   1201   4002       C  
+ATOM  10483  C   ALA D  29      -7.049  67.538 -23.247  1.00 76.86           C  
+ANISOU10483  C   ALA D  29    10205   8958  10042  -1251   1220   4231       C  
+ATOM  10484  O   ALA D  29      -7.559  68.288 -24.080  1.00 97.00           O  
+ANISOU10484  O   ALA D  29    12888  11418  12551  -1156   1203   4502       O  
+ATOM  10485  CB  ALA D  29      -5.638  68.828 -21.636  1.00 66.05           C  
+ANISOU10485  CB  ALA D  29     8744   7032   9322  -1707   1363   4026       C  
+ATOM  10486  N   GLY D  30      -6.605  66.321 -23.545  1.00 76.24           N  
+ANISOU10486  N   GLY D  30    10004   9317   9646  -1225   1255   4110       N  
+ATOM  10487  CA  GLY D  30      -6.673  65.786 -24.893  1.00 82.06           C  
+ANISOU10487  CA  GLY D  30    10754  10466   9960  -1093   1276   4256       C  
+ATOM  10488  C   GLY D  30      -8.086  65.676 -25.435  1.00 79.62           C  
+ANISOU10488  C   GLY D  30    10553  10214   9484   -825   1102   4357       C  
+ATOM  10489  O   GLY D  30      -8.316  65.839 -26.633  1.00 78.10           O  
+ANISOU10489  O   GLY D  30    10418  10235   9021   -722   1100   4577       O  
+ATOM  10490  N   LEU D  31      -9.034  65.397 -24.546  1.00 70.48           N  
+ANISOU10490  N   LEU D  31     9408   8888   8483   -710    954   4195       N  
+ATOM  10491  CA  LEU D  31     -10.431  65.241 -24.932  1.00 62.86           C  
+ANISOU10491  CA  LEU D  31     8511   7988   7387   -453    773   4255       C  
+ATOM  10492  C   LEU D  31     -11.044  66.573 -25.352  1.00 76.13           C  
+ANISOU10492  C   LEU D  31    10329   9378   9219   -372    723   4538       C  
+ATOM  10493  O   LEU D  31     -12.036  66.608 -26.080  1.00 70.37           O  
+ANISOU10493  O   LEU D  31     9646   8789   8304   -156    593   4673       O  
+ATOM  10494  CB  LEU D  31     -11.236  64.630 -23.782  1.00 60.19           C  
+ANISOU10494  CB  LEU D  31     8133   7519   7218   -361    648   4005       C  
+ATOM  10495  CG  LEU D  31     -12.635  64.107 -24.119  1.00 63.98           C  
+ANISOU10495  CG  LEU D  31     8621   8167   7520   -102    457   3995       C  
+ATOM  10496  CD1 LEU D  31     -12.549  62.879 -25.011  1.00 61.45           C  
+ANISOU10496  CD1 LEU D  31     8225   8373   6752    -41    448   3874       C  
+ATOM  10497  CD2 LEU D  31     -13.412  63.798 -22.849  1.00 58.03           C  
+ANISOU10497  CD2 LEU D  31     7837   7173   7039    -30    343   3646       C  
+ATOM  10498  N   SER D  32     -10.442  67.666 -24.896  1.00 86.14           N  
+ANISOU10498  N   SER D  32    11653  10252  10825   -546    827   4618       N  
+ATOM  10499  CA  SER D  32     -10.930  69.002 -25.217  1.00 79.66           C  
+ANISOU10499  CA  SER D  32    10974   9096  10196   -483    808   4883       C  
+ATOM  10500  C   SER D  32     -10.319  69.534 -26.508  1.00 89.27           C  
+ANISOU10500  C   SER D  32    12244  10472  11202   -537    934   5216       C  
+ATOM  10501  O   SER D  32     -10.550  70.682 -26.889  1.00 92.91           O  
+ANISOU10501  O   SER D  32    12829  10664  11810   -506    953   5487       O  
+ATOM  10502  CB  SER D  32     -10.634  69.965 -24.067  1.00 69.91           C  
+ANISOU10502  CB  SER D  32     9784   7326   9454   -646    860   4778       C  
+ATOM  10503  OG  SER D  32     -11.091  69.438 -22.833  1.00 65.79           O  
+ANISOU10503  OG  SER D  32     9199   6684   9112   -607    763   4455       O  
+HETATM10504  N   MSE D  33      -9.538  68.694 -27.179  1.00 89.10           N  
+ANISOU10504  N   MSE D  33    12127  10889  10838   -607   1027   5194       N  
+HETATM10505  CA  MSE D  33      -8.899  69.079 -28.430  1.00 87.93           C  
+ANISOU10505  CA  MSE D  33    12008  10952  10449   -655   1162   5492       C  
+HETATM10506  C   MSE D  33      -9.371  68.197 -29.580  1.00 85.44           C  
+ANISOU10506  C   MSE D  33    11655  11183   9625   -446   1080   5535       C  
+HETATM10507  O   MSE D  33      -9.440  66.974 -29.448  1.00 75.25           O  
+ANISOU10507  O   MSE D  33    10260  10214   8120   -395   1023   5260       O  
+HETATM10508  CB  MSE D  33      -7.377  69.005 -28.296  1.00 87.59           C  
+ANISOU10508  CB  MSE D  33    11869  10955  10455   -945   1380   5428       C  
+HETATM10509  CG  MSE D  33      -6.814  69.810 -27.134  1.00 89.77           C  
+ANISOU10509  CG  MSE D  33    12148  10740  11221  -1185   1456   5330       C  
+HETATM10510 SE   MSE D  33      -7.019  71.733 -27.377  1.00139.63          SE  
+ANISOU10510 SE   MSE D  33    18665  16487  17901  -1247   1518   5715      SE  
+HETATM10511  CE  MSE D  33      -6.279  72.335 -25.677  1.00109.40           C  
+ANISOU10511  CE  MSE D  33    14782  12128  14658  -1571   1582   5395       C  
+ATOM  10512  N   SER D  34      -9.700  68.827 -30.704  1.00 88.21           N  
+ANISOU10512  N   SER D  34    12091  11640   9783   -326   1076   5874       N  
+ATOM  10513  CA  SER D  34     -10.126  68.109 -31.900  1.00 94.14           C  
+ANISOU10513  CA  SER D  34    12802  12938  10027   -131    997   5923       C  
+ATOM  10514  C   SER D  34      -9.026  67.179 -32.400  1.00100.05           C  
+ANISOU10514  C   SER D  34    13433  14113  10468   -251   1148   5775       C  
+ATOM  10515  O   SER D  34      -9.301  66.098 -32.921  1.00110.48           O  
+ANISOU10515  O   SER D  34    14673  15890  11414   -124   1069   5585       O  
+ATOM  10516  CB  SER D  34     -10.532  69.089 -33.002  1.00100.02           C  
+ANISOU10516  CB  SER D  34    13657  13710  10637      3    991   6353       C  
+ATOM  10517  OG  SER D  34     -11.692  69.816 -32.635  1.00 96.96           O  
+ANISOU10517  OG  SER D  34    13362  12992  10486    174    826   6464       O  
+ATOM  10518  N   VAL D  35      -7.778  67.607 -32.237  1.00 97.14           N  
+ANISOU10518  N   VAL D  35    13045  13595  10267   -496   1366   5842       N  
+ATOM  10519  CA  VAL D  35      -6.631  66.813 -32.660  1.00101.78           C  
+ANISOU10519  CA  VAL D  35    13507  14558  10608   -612   1530   5704       C  
+ATOM  10520  C   VAL D  35      -6.353  65.696 -31.650  1.00 98.50           C  
+ANISOU10520  C   VAL D  35    12967  14185  10274   -670   1506   5272       C  
+ATOM  10521  O   VAL D  35      -5.565  64.787 -31.911  1.00105.68           O  
+ANISOU10521  O   VAL D  35    13755  15434  10964   -711   1606   5076       O  
+ATOM  10522  CB  VAL D  35      -5.376  67.696 -32.839  1.00100.89           C  
+ANISOU10522  CB  VAL D  35    13394  14280  10660   -861   1779   5934       C  
+ATOM  10523  CG1 VAL D  35      -4.708  67.957 -31.497  1.00103.02           C  
+ANISOU10523  CG1 VAL D  35    13613  14142  11387  -1103   1851   5749       C  
+ATOM  10524  CG2 VAL D  35      -4.400  67.051 -33.813  1.00102.75           C  
+ANISOU10524  CG2 VAL D  35    13518  15008  10516   -896   1944   5921       C  
+ATOM  10525  N   GLY D  36      -7.014  65.772 -30.498  1.00 90.58           N  
+ANISOU10525  N   GLY D  36    11993  12835   9588   -658   1376   5128       N  
+ATOM  10526  CA  GLY D  36      -6.977  64.709 -29.508  1.00 86.96           C  
+ANISOU10526  CA  GLY D  36    11431  12411   9199   -674   1327   4748       C  
+ATOM  10527  C   GLY D  36      -5.894  64.817 -28.450  1.00 90.12           C  
+ANISOU10527  C   GLY D  36    11743  12576   9923   -914   1460   4600       C  
+ATOM  10528  O   GLY D  36      -5.810  63.972 -27.559  1.00 93.45           O  
+ANISOU10528  O   GLY D  36    12073  13017  10417   -925   1428   4303       O  
+ATOM  10529  N   TYR D  37      -5.064  65.850 -28.542  1.00 95.37           N  
+ANISOU10529  N   TYR D  37    12425  13029  10781  -1110   1612   4805       N  
+ATOM  10530  CA  TYR D  37      -3.990  66.049 -27.572  1.00 87.82           C  
+ANISOU10530  CA  TYR D  37    11361  11872  10135  -1361   1735   4661       C  
+ATOM  10531  C   TYR D  37      -3.657  67.530 -27.445  1.00 86.18           C  
+ANISOU10531  C   TYR D  37    11237  11241  10268  -1556   1827   4905       C  
+ATOM  10532  O   TYR D  37      -4.136  68.351 -28.226  1.00 83.42           O  
+ANISOU10532  O   TYR D  37    11029  10787   9881  -1488   1824   5216       O  
+ATOM  10533  CB  TYR D  37      -2.740  65.249 -27.956  1.00 82.51           C  
+ANISOU10533  CB  TYR D  37    10517  11591   9244  -1448   1899   4531       C  
+ATOM  10534  CG  TYR D  37      -2.078  65.690 -29.240  1.00 93.73           C  
+ANISOU10534  CG  TYR D  37    11946  13221  10446  -1499   2065   4805       C  
+ATOM  10535  CD1 TYR D  37      -0.981  66.544 -29.220  1.00 99.79           C  
+ANISOU10535  CD1 TYR D  37    12660  13836  11421  -1757   2257   4946       C  
+ATOM  10536  CD2 TYR D  37      -2.539  65.246 -30.471  1.00 95.45           C  
+ANISOU10536  CD2 TYR D  37    12214  13807  10244  -1297   2035   4913       C  
+ATOM  10537  CE1 TYR D  37      -0.369  66.948 -30.390  1.00107.09           C  
+ANISOU10537  CE1 TYR D  37    13589  14955  12146  -1809   2428   5217       C  
+ATOM  10538  CE2 TYR D  37      -1.933  65.645 -31.647  1.00100.69           C  
+ANISOU10538  CE2 TYR D  37    12882  14687  10689  -1335   2193   5174       C  
+ATOM  10539  CZ  TYR D  37      -0.849  66.495 -31.600  1.00107.49           C  
+ANISOU10539  CZ  TYR D  37    13696  15377  11766  -1589   2396   5339       C  
+ATOM  10540  OH  TYR D  37      -0.242  66.895 -32.769  1.00115.88           O  
+ANISOU10540  OH  TYR D  37    14760  16658  12609  -1633   2572   5620       O  
+ATOM  10541  N   VAL D  38      -2.828  67.866 -26.463  1.00 88.96           N  
+ANISOU10541  N   VAL D  38    11492  11358  10950  -1800   1909   4757       N  
+ATOM  10542  CA  VAL D  38      -2.399  69.246 -26.274  1.00 93.53           C  
+ANISOU10542  CA  VAL D  38    12133  11520  11883  -2031   2013   4933       C  
+ATOM  10543  C   VAL D  38      -0.881  69.348 -26.366  1.00 99.01           C  
+ANISOU10543  C   VAL D  38    12658  12342  12619  -2312   2233   4912       C  
+ATOM  10544  O   VAL D  38      -0.157  68.658 -25.649  1.00111.04           O  
+ANISOU10544  O   VAL D  38    13989  14021  14179  -2411   2259   4625       O  
+ATOM  10545  CB  VAL D  38      -2.866  69.805 -24.917  1.00 80.00           C  
+ANISOU10545  CB  VAL D  38    10459   9333  10606  -2102   1900   4749       C  
+ATOM  10546  N   SER D  39      -0.409  70.215 -27.256  1.00100.08           N  
+ANISOU10546  N   SER D  39    12855  12422  12750  -2434   2395   5228       N  
+ATOM  10547  CA  SER D  39       1.019  70.470 -27.404  1.00108.19           C  
+ANISOU10547  CA  SER D  39    13721  13539  13848  -2725   2625   5243       C  
+ATOM  10548  C   SER D  39       1.504  71.530 -26.421  1.00120.93           C  
+ANISOU10548  C   SER D  39    15308  14680  15961  -3046   2678   5163       C  
+ATOM  10549  O   SER D  39       2.525  71.351 -25.756  1.00125.58           O  
+ANISOU10549  O   SER D  39    15681  15332  16699  -3278   2763   4923       O  
+ATOM  10550  CB  SER D  39       1.338  70.900 -28.837  1.00102.14           C  
+ANISOU10550  CB  SER D  39    13023  12948  12836  -2724   2795   5631       C  
+ATOM  10551  N   ILE D  82      -2.282  82.394 -16.764  1.00116.70           N  
+ANISOU10551  N   ILE D  82    15778   8364  20200  -4081   1862   3322       N  
+ATOM  10552  CA  ILE D  82      -1.920  83.007 -18.037  1.00130.54           C  
+ANISOU10552  CA  ILE D  82    17646  10019  21935  -4183   2044   3844       C  
+ATOM  10553  C   ILE D  82      -2.138  82.039 -19.197  1.00135.32           C  
+ANISOU10553  C   ILE D  82    18264  11120  22034  -3952   2086   4246       C  
+ATOM  10554  O   ILE D  82      -2.821  82.362 -20.169  1.00145.95           O  
+ANISOU10554  O   ILE D  82    19805  12377  23273  -3715   2125   4673       O  
+ATOM  10555  CB  ILE D  82      -0.452  83.475 -18.037  1.00133.20           C  
+ANISOU10555  CB  ILE D  82    17815  10336  22459  -4686   2191   3799       C  
+ATOM  10556  N   ILE D  83      -1.547  80.855 -19.085  1.00128.31           N  
+ANISOU10556  N   ILE D  83    17155  10766  20832  -4014   2075   4094       N  
+ATOM  10557  CA  ILE D  83      -1.639  79.822 -20.113  1.00128.21           C  
+ANISOU10557  CA  ILE D  83    17119  11272  20324  -3812   2117   4396       C  
+ATOM  10558  C   ILE D  83      -3.077  79.343 -20.302  1.00128.63           C  
+ANISOU10558  C   ILE D  83    17325  11381  20169  -3345   1962   4490       C  
+ATOM  10559  O   ILE D  83      -3.545  79.147 -21.430  1.00134.94           O  
+ANISOU10559  O   ILE D  83    18231  12367  20671  -3118   1992   4880       O  
+ATOM  10560  CB  ILE D  83      -0.749  78.611 -19.775  1.00122.79           C  
+ANISOU10560  CB  ILE D  83    16150  11122  19383  -3951   2124   4141       C  
+ATOM  10561  N   LEU D  84      -3.764  79.155 -19.180  1.00120.34           N  
+ANISOU10561  N   LEU D  84    16265  10191  19268  -3208   1794   4114       N  
+ATOM  10562  CA  LEU D  84      -5.140  78.671 -19.166  1.00114.59           C  
+ANISOU10562  CA  LEU D  84    15646   9516  18378  -2786   1636   4131       C  
+ATOM  10563  C   LEU D  84      -6.103  79.533 -19.980  1.00121.36           C  
+ANISOU10563  C   LEU D  84    16743  10081  19286  -2536   1631   4512       C  
+ATOM  10564  O   LEU D  84      -7.064  79.012 -20.534  1.00127.41           O  
+ANISOU10564  O   LEU D  84    17576  11061  19774  -2198   1538   4692       O  
+ATOM  10565  CB  LEU D  84      -5.643  78.568 -17.724  1.00111.31           C  
+ANISOU10565  CB  LEU D  84    15182   8918  18193  -2723   1486   3643       C  
+ATOM  10566  N   ASP D  85      -5.885  80.844 -20.015  1.00120.84           N  
+ANISOU10566  N   ASP D  85    16800   9529  19586  -2692   1721   4620       N  
+ATOM  10567  CA  ASP D  85      -6.718  81.713 -20.845  1.00127.40           C  
+ANISOU10567  CA  ASP D  85    17854  10077  20475  -2458   1733   5027       C  
+ATOM  10568  C   ASP D  85      -6.642  81.313 -22.321  1.00139.84           C  
+ANISOU10568  C   ASP D  85    19458  12047  21629  -2352   1811   5520       C  
+ATOM  10569  O   ASP D  85      -7.668  81.168 -22.998  1.00148.52           O  
+ANISOU10569  O   ASP D  85    20659  13266  22505  -2000   1720   5775       O  
+ATOM  10570  CB  ASP D  85      -6.299  83.175 -20.676  1.00123.51           C  
+ANISOU10570  CB  ASP D  85    17476   8988  20463  -2696   1849   5079       C  
+ATOM  10571  N   GLU D  86      -5.418  81.114 -22.804  1.00138.56           N  
+ANISOU10571  N   GLU D  86    19184  12118  21342  -2656   1975   5628       N  
+ATOM  10572  CA  GLU D  86      -5.187  80.663 -24.172  1.00139.07           C  
+ANISOU10572  CA  GLU D  86    19247  12615  20977  -2583   2070   6045       C  
+ATOM  10573  C   GLU D  86      -5.792  79.282 -24.386  1.00137.71           C  
+ANISOU10573  C   GLU D  86    18989  12989  20345  -2293   1928   5963       C  
+ATOM  10574  O   GLU D  86      -6.429  79.023 -25.411  1.00145.52           O  
+ANISOU10574  O   GLU D  86    20051  14242  21001  -2022   1888   6280       O  
+ATOM  10575  CB  GLU D  86      -3.690  80.642 -24.489  1.00135.81           C  
+ANISOU10575  CB  GLU D  86    18696  12371  20533  -2981   2283   6097       C  
+ATOM  10576  N   PHE D  87      -5.575  78.401 -23.412  1.00124.35           N  
+ANISOU10576  N   PHE D  87    17135  11472  18640  -2359   1850   5532       N  
+ATOM  10577  CA  PHE D  87      -6.143  77.055 -23.435  1.00126.20           C  
+ANISOU10577  CA  PHE D  87    17279  12176  18494  -2108   1712   5401       C  
+ATOM  10578  C   PHE D  87      -7.652  77.101 -23.660  1.00135.60           C  
+ANISOU10578  C   PHE D  87    18609  13306  19608  -1709   1536   5516       C  
+ATOM  10579  O   PHE D  87      -8.178  76.444 -24.558  1.00136.45           O  
+ANISOU10579  O   PHE D  87    18721  13803  19322  -1473   1475   5713       O  
+ATOM  10580  CB  PHE D  87      -5.826  76.318 -22.133  1.00119.56           C  
+ANISOU10580  CB  PHE D  87    16269  11397  17760  -2226   1643   4915       C  
+ATOM  10581  N   SER D  88      -8.335  77.881 -22.828  1.00137.36           N  
+ANISOU10581  N   SER D  88    18929  13056  20207  -1636   1452   5366       N  
+ATOM  10582  CA  SER D  88      -9.778  78.068 -22.916  1.00128.42           C  
+ANISOU10582  CA  SER D  88    17913  11813  19066  -1261   1290   5447       C  
+ATOM  10583  C   SER D  88     -10.168  78.645 -24.270  1.00126.31           C  
+ANISOU10583  C   SER D  88    17782  11582  18629  -1091   1322   5953       C  
+ATOM  10584  O   SER D  88     -11.214  78.308 -24.823  1.00126.08           O  
+ANISOU10584  O   SER D  88    17783  11770  18350   -764   1185   6098       O  
+ATOM  10585  CB  SER D  88     -10.267  78.984 -21.792  1.00133.11           C  
+ANISOU10585  CB  SER D  88    18588  11850  20137  -1246   1236   5193       C  
+ATOM  10586  OG  SER D  88     -11.417  79.712 -22.188  1.00143.35           O  
+ANISOU10586  OG  SER D  88    20042  12916  21510   -937   1154   5423       O  
+ATOM  10587  N   ARG D  89      -9.316  79.518 -24.799  1.00128.41           N  
+ANISOU10587  N   ARG D  89    18116  11644  19029  -1320   1503   6221       N  
+ATOM  10588  CA  ARG D  89      -9.549  80.122 -26.107  1.00124.93           C  
+ANISOU10588  CA  ARG D  89    17804  11235  18430  -1184   1561   6740       C  
+ATOM  10589  C   ARG D  89      -9.217  79.152 -27.243  1.00123.60           C  
+ANISOU10589  C   ARG D  89    17544  11703  17716  -1139   1595   6946       C  
+ATOM  10590  O   ARG D  89      -9.422  79.464 -28.416  1.00132.45           O  
+ANISOU10590  O   ARG D  89    18744  12971  18608  -1001   1631   7371       O  
+ATOM  10591  CB  ARG D  89      -8.729  81.405 -26.258  1.00118.53           C  
+ANISOU10591  CB  ARG D  89    17098   9964  17975  -1462   1762   6966       C  
+ATOM  10592  N   LYS D  90      -8.713  77.974 -26.887  1.00115.30           N  
+ANISOU10592  N   LYS D  90    16322  11035  16453  -1242   1582   6638       N  
+ATOM  10593  CA  LYS D  90      -8.277  76.989 -27.875  1.00122.49           C  
+ANISOU10593  CA  LYS D  90    17128  12551  16859  -1222   1628   6759       C  
+ATOM  10594  C   LYS D  90      -9.090  75.689 -27.898  1.00123.16           C  
+ANISOU10594  C   LYS D  90    17120  13093  16583   -958   1435   6558       C  
+ATOM  10595  O   LYS D  90      -8.732  74.751 -28.611  1.00116.58           O  
+ANISOU10595  O   LYS D  90    16187  12774  15335   -941   1461   6577       O  
+ATOM  10596  CB  LYS D  90      -6.801  76.652 -27.647  1.00122.58           C  
+ANISOU10596  CB  LYS D  90    17000  12690  16886  -1588   1815   6605       C  
+ATOM  10597  N   VAL D  91     -10.174  75.622 -27.130  1.00121.18           N  
+ANISOU10597  N   VAL D  91    16894  12658  16489   -756   1250   6354       N  
+ATOM  10598  CA  VAL D  91     -10.943  74.381 -27.032  1.00114.57           C  
+ANISOU10598  CA  VAL D  91    15956  12218  15358   -538   1072   6134       C  
+ATOM  10599  C   VAL D  91     -12.319  74.481 -27.691  1.00121.53           C  
+ANISOU10599  C   VAL D  91    16905  13212  16060   -176    891   6331       C  
+ATOM  10600  O   VAL D  91     -12.869  75.572 -27.849  1.00129.67           O  
+ANISOU10600  O   VAL D  91    18067  13901  17299    -58    872   6564       O  
+ATOM  10601  CB  VAL D  91     -11.137  73.956 -25.563  1.00105.38           C  
+ANISOU10601  CB  VAL D  91    14719  10855  14465   -583    989   5692       C  
+ATOM  10602  CG1 VAL D  91      -9.797  73.632 -24.921  1.00108.68           C  
+ANISOU10602  CG1 VAL D  91    15026  11277  14991   -920   1138   5464       C  
+ATOM  10603  CG2 VAL D  91     -11.863  75.044 -24.784  1.00 97.23           C  
+ANISOU10603  CG2 VAL D  91    13805   9268  13872   -501    927   5648       C  
+ATOM  10604  N   ASP D  92     -12.867  73.330 -28.073  1.00108.86           N  
+ANISOU10604  N   ASP D  92    15199  12094  14071     -1    757   6227       N  
+ATOM  10605  CA  ASP D  92     -14.204  73.262 -28.657  1.00110.19           C  
+ANISOU10605  CA  ASP D  92    15383  12446  14039    338    558   6355       C  
+ATOM  10606  C   ASP D  92     -14.848  71.892 -28.446  1.00100.05           C  
+ANISOU10606  C   ASP D  92    13956  11564  12496    471    392   6051       C  
+ATOM  10607  O   ASP D  92     -14.184  70.935 -28.048  1.00 91.69           O  
+ANISOU10607  O   ASP D  92    12796  10696  11348    310    447   5793       O  
+ATOM  10608  CB  ASP D  92     -14.150  73.587 -30.151  1.00114.68           C  
+ANISOU10608  CB  ASP D  92    16002  13313  14258    436    594   6772       C  
+ATOM  10609  N   LEU D  93     -16.147  71.811 -28.719  1.00105.71           N  
+ANISOU10609  N   LEU D  93    14656  12409  13099    765    189   6087       N  
+ATOM  10610  CA  LEU D  93     -16.926  70.604 -28.463  1.00 90.91           C  
+ANISOU10610  CA  LEU D  93    12642  10869  11032    900     14   5797       C  
+ATOM  10611  C   LEU D  93     -16.673  69.552 -29.543  1.00 99.45           C  
+ANISOU10611  C   LEU D  93    13627  12575  11583    910     -5   5802       C  
+ATOM  10612  O   LEU D  93     -16.537  69.882 -30.722  1.00109.19           O  
+ANISOU10612  O   LEU D  93    14900  14050  12538    969     22   6091       O  
+ATOM  10613  CB  LEU D  93     -18.417  70.945 -28.390  1.00 86.33           C  
+ANISOU10613  CB  LEU D  93    12052  10218  10532   1206   -199   5823       C  
+ATOM  10614  CG  LEU D  93     -19.372  69.864 -27.887  1.00 81.29           C  
+ANISOU10614  CG  LEU D  93    11258   9817   9811   1345   -386   5502       C  
+ATOM  10615  CD1 LEU D  93     -19.184  69.681 -26.393  1.00 80.52           C  
+ANISOU10615  CD1 LEU D  93    11141   9354  10097   1216   -332   5184       C  
+ATOM  10616  CD2 LEU D  93     -20.813  70.217 -28.207  1.00 81.30           C  
+ANISOU10616  CD2 LEU D  93    11219   9882   9790   1664   -601   5592       C  
+ATOM  10617  N   THR D  94     -16.619  68.285 -29.143  1.00 99.74           N  
+ANISOU10617  N   THR D  94    13540  12877  11479    861    -46   5474       N  
+ATOM  10618  CA  THR D  94     -16.331  67.203 -30.080  1.00104.57           C  
+ANISOU10618  CA  THR D  94    14057  14074  11600    859    -55   5401       C  
+ATOM  10619  C   THR D  94     -17.431  66.144 -30.023  1.00 92.57           C  
+ANISOU10619  C   THR D  94    12404  12885   9883   1036   -277   5139       C  
+ATOM  10620  O   THR D  94     -18.245  66.137 -29.099  1.00 90.75           O  
+ANISOU10620  O   THR D  94    12140  12416   9926   1122   -393   4994       O  
+ATOM  10621  CB  THR D  94     -14.961  66.550 -29.783  1.00105.79           C  
+ANISOU10621  CB  THR D  94    14177  14292  11725    593    145   5232       C  
+ATOM  10622  OG1 THR D  94     -14.049  67.544 -29.302  1.00112.33           O  
+ANISOU10622  OG1 THR D  94    15100  14680  12902    395    329   5373       O  
+ATOM  10623  CG2 THR D  94     -14.376  65.903 -31.036  1.00109.11           C  
+ANISOU10623  CG2 THR D  94    14548  15254  11657    578    209   5266       C  
+ATOM  10624  N   GLU D  95     -17.455  65.261 -31.019  1.00 82.98           N  
+ANISOU10624  N   GLU D  95    11103  12229   8198   1088   -334   5057       N  
+ATOM  10625  CA  GLU D  95     -18.432  64.181 -31.070  1.00 77.27           C  
+ANISOU10625  CA  GLU D  95    10233  11874   7253   1227   -545   4767       C  
+ATOM  10626  C   GLU D  95     -18.325  63.278 -29.846  1.00 74.93           C  
+ANISOU10626  C   GLU D  95     9868  11441   7160   1118   -529   4433       C  
+ATOM  10627  O   GLU D  95     -19.318  62.704 -29.418  1.00 80.18           O  
+ANISOU10627  O   GLU D  95    10422  12187   7855   1235   -708   4223       O  
+ATOM  10628  CB  GLU D  95     -18.265  63.352 -32.347  1.00 79.07           C  
+ANISOU10628  CB  GLU D  95    10382  12724   6936   1258   -577   4670       C  
+ATOM  10629  CG  GLU D  95     -19.400  63.539 -33.348  1.00100.89           C  
+ANISOU10629  CG  GLU D  95    13080  15834   9417   1498   -801   4761       C  
+ATOM  10630  CD  GLU D  95     -20.726  62.977 -32.863  1.00109.54           C  
+ANISOU10630  CD  GLU D  95    14028  17019  10573   1643  -1055   4490       C  
+ATOM  10631  OE1 GLU D  95     -20.754  61.831 -32.364  1.00 98.09           O  
+ANISOU10631  OE1 GLU D  95    12472  15715   9084   1566  -1092   4112       O  
+ATOM  10632  OE2 GLU D  95     -21.744  63.696 -32.970  1.00118.97           O  
+ANISOU10632  OE2 GLU D  95    15203  18134  11867   1836  -1214   4655       O  
+ATOM  10633  N   ASN D  96     -17.119  63.148 -29.298  1.00 68.42           N  
+ANISOU10633  N   ASN D  96     9093  10429   6474    897   -314   4387       N  
+ATOM  10634  CA  ASN D  96     -16.905  62.386 -28.070  1.00 70.58           C  
+ANISOU10634  CA  ASN D  96     9315  10536   6966    790   -271   4115       C  
+ATOM  10635  C   ASN D  96     -17.790  62.884 -26.935  1.00 72.45           C  
+ANISOU10635  C   ASN D  96     9553  10322   7650    863   -370   4034       C  
+ATOM  10636  O   ASN D  96     -18.436  62.098 -26.242  1.00 69.10           O  
+ANISOU10636  O   ASN D  96     9033   9873   7350    882   -458   3639       O  
+ATOM  10637  CB  ASN D  96     -15.438  62.456 -27.647  1.00 80.92           C  
+ANISOU10637  CB  ASN D  96    10675  11662   8408    543    -21   4115       C  
+ATOM  10638  CG  ASN D  96     -14.514  61.786 -28.641  1.00 77.57           C  
+ANISOU10638  CG  ASN D  96    10217  11674   7583    463    100   4062       C  
+ATOM  10639  OD1 ASN D  96     -14.892  60.822 -29.305  1.00 85.46           O  
+ANISOU10639  OD1 ASN D  96    11139  13119   8214    556     10   3876       O  
+ATOM  10640  ND2 ASN D  96     -13.295  62.300 -28.755  1.00 64.90           N  
+ANISOU10640  ND2 ASN D  96     8657   9949   6052    288    306   4192       N  
+ATOM  10641  N   HIS D  97     -17.816  64.201 -26.762  1.00 73.90           N  
+ANISOU10641  N   HIS D  97     9847  10123   8107    889   -335   4326       N  
+ATOM  10642  CA  HIS D  97     -18.635  64.832 -25.736  1.00 70.40           C  
+ANISOU10642  CA  HIS D  97     9416   9250   8082    988   -413   4290       C  
+ATOM  10643  C   HIS D  97     -20.116  64.515 -25.928  1.00 83.89           C  
+ANISOU10643  C   HIS D  97    11005  11168   9700   1245   -655   4218       C  
+ATOM  10644  O   HIS D  97     -20.829  64.278 -24.955  1.00 84.65           O  
+ANISOU10644  O   HIS D  97    11025  11077  10059   1291   -721   3942       O  
+ATOM  10645  CB  HIS D  97     -18.404  66.340 -25.732  1.00 77.10           C  
+ANISOU10645  CB  HIS D  97    10413   9676   9206    970   -330   4540       C  
+ATOM  10646  CG  HIS D  97     -17.007  66.730 -25.364  1.00 71.73           C  
+ANISOU10646  CG  HIS D  97     9814   8748   8690    699   -106   4566       C  
+ATOM  10647  ND1 HIS D  97     -16.110  67.239 -26.278  1.00 91.15           N  
+ANISOU10647  ND1 HIS D  97    12349  11289  10996    586     26   4808       N  
+ATOM  10648  CD2 HIS D  97     -16.352  66.680 -24.180  1.00 62.74           C  
+ANISOU10648  CD2 HIS D  97     8673   7311   7854    519      3   4368       C  
+ATOM  10649  CE1 HIS D  97     -14.962  67.486 -25.672  1.00102.39           C  
+ANISOU10649  CE1 HIS D  97    13799  12472  12631    338    205   4752       C  
+ATOM  10650  NE2 HIS D  97     -15.082  67.156 -24.399  1.00 87.06           N  
+ANISOU10650  NE2 HIS D  97    11811  10306  10960    293    187   4480       N  
+ATOM  10651  N   LYS D  98     -20.582  64.522 -27.175  1.00 81.53           N  
+ANISOU10651  N   LYS D  98    10675  11257   9044   1382   -773   4351       N  
+ATOM  10652  CA  LYS D  98     -21.983  64.205 -27.456  1.00 72.06           C  
+ANISOU10652  CA  LYS D  98     9325  10324   7729   1617  -1021   4256       C  
+ATOM  10653  C   LYS D  98     -22.299  62.728 -27.209  1.00 81.36           C  
+ANISOU10653  C   LYS D  98    10331  11811   8772   1555  -1101   3798       C  
+ATOM  10654  O   LYS D  98     -23.303  62.410 -26.578  1.00 90.06           O  
+ANISOU10654  O   LYS D  98    11301  12848  10068   1630  -1219   3533       O  
+ATOM  10655  CB  LYS D  98     -22.368  64.591 -28.886  1.00 79.85           C  
+ANISOU10655  CB  LYS D  98    10315  11669   8357   1763  -1130   4473       C  
+ATOM  10656  CG  LYS D  98     -22.549  66.086 -29.122  1.00 88.62           C  
+ANISOU10656  CG  LYS D  98    11566  12439   9667   1874  -1102   4827       C  
+ATOM  10657  CD  LYS D  98     -23.319  66.322 -30.421  1.00 90.55           C  
+ANISOU10657  CD  LYS D  98    11756  13087   9562   2088  -1274   5008       C  
+ATOM  10658  CE  LYS D  98     -23.848  67.748 -30.522  1.00106.30           C  
+ANISOU10658  CE  LYS D  98    13857  14738  11794   2267  -1298   5337       C  
+ATOM  10659  NZ  LYS D  98     -24.752  68.100 -29.387  1.00110.55           N  
+ANISOU10659  NZ  LYS D  98    14348  14896  12759   2388  -1380   5199       N  
+ATOM  10660  N   ILE D  99     -21.432  61.835 -27.672  1.00 85.70           N  
+ANISOU10660  N   ILE D  99    10883  12638   9040   1386  -1002   3624       N  
+ATOM  10661  CA  ILE D  99     -21.620  60.417 -27.437  1.00 79.69           C  
+ANISOU10661  CA  ILE D  99     9988  12071   8221   1280  -1029   3105       C  
+ATOM  10662  C   ILE D  99     -21.713  60.163 -25.931  1.00 71.95           C  
+ANISOU10662  C   ILE D  99     8992  10648   7696   1178   -944   2825       C  
+ATOM  10663  O   ILE D  99     -22.641  59.507 -25.463  1.00 76.62           O  
+ANISOU10663  O   ILE D  99     9441  11258   8413   1206  -1043   2514       O  
+ATOM  10664  CB  ILE D  99     -20.441  59.576 -27.969  1.00 84.01           C  
+ANISOU10664  CB  ILE D  99    10571  12866   8482   1108   -876   2962       C  
+ATOM  10665  CG1 ILE D  99     -20.252  59.703 -29.475  1.00 80.64           C  
+ANISOU10665  CG1 ILE D  99    10152  12947   7539   1199   -932   3199       C  
+ATOM  10666  CG2 ILE D  99     -20.650  58.125 -27.602  1.00 72.94           C  
+ANISOU10666  CG2 ILE D  99     9046  11558   7110   1005   -883   2421       C  
+ATOM  10667  CD1 ILE D  99     -18.932  59.120 -29.896  1.00 97.92           C  
+ANISOU10667  CD1 ILE D  99    12396  15316   9493   1036   -730   3123       C  
+ATOM  10668  N   LEU D 100     -20.769  60.725 -25.177  1.00 74.92           N  
+ANISOU10668  N   LEU D 100     9502  10648   8315   1059   -759   2949       N  
+ATOM  10669  CA  LEU D 100     -20.739  60.578 -23.722  1.00 69.54           C  
+ANISOU10669  CA  LEU D 100     8816   9582   8024    972   -669   2711       C  
+ATOM  10670  C   LEU D 100     -21.972  61.171 -23.032  1.00 63.62           C  
+ANISOU10670  C   LEU D 100     8005   8605   7561   1137   -789   2711       C  
+ATOM  10671  O   LEU D 100     -22.501  60.600 -22.076  1.00 63.26           O  
+ANISOU10671  O   LEU D 100     7866   8447   7723   1119   -786   2410       O  
+ATOM  10672  CB  LEU D 100     -19.465  61.215 -23.166  1.00 66.78           C  
+ANISOU10672  CB  LEU D 100     8606   8926   7841    820   -473   2860       C  
+ATOM  10673  CG  LEU D 100     -18.201  60.407 -23.479  1.00 65.02           C  
+ANISOU10673  CG  LEU D 100     8398   8897   7409    642   -322   2755       C  
+ATOM  10674  CD1 LEU D 100     -16.930  61.186 -23.139  1.00 71.09           C  
+ANISOU10674  CD1 LEU D 100     9273   9425   8313    488   -144   2956       C  
+ATOM  10675  CD2 LEU D 100     -18.212  59.054 -22.781  1.00 60.06           C  
+ANISOU10675  CD2 LEU D 100     7675   8312   6831    571   -283   2326       C  
+ATOM  10676  N   ALA D 101     -22.424  62.318 -23.529  1.00 65.19           N  
+ANISOU10676  N   ALA D 101     8253   8744   7773   1311   -882   3066       N  
+ATOM  10677  CA  ALA D 101     -23.589  62.992 -22.973  1.00 69.35           C  
+ANISOU10677  CA  ALA D 101     8718   9062   8571   1510   -994   3098       C  
+ATOM  10678  C   ALA D 101     -24.857  62.186 -23.232  1.00 81.11           C  
+ANISOU10678  C   ALA D 101     9987  10885   9946   1628  -1181   2860       C  
+ATOM  10679  O   ALA D 101     -25.813  62.265 -22.462  1.00 72.50           O  
+ANISOU10679  O   ALA D 101     8782   9657   9107   1732  -1237   2714       O  
+ATOM  10680  CB  ALA D 101     -23.728  64.391 -23.561  1.00 65.36           C  
+ANISOU10680  CB  ALA D 101     8321   8411   8102   1694  -1043   3572       C  
+ATOM  10681  N   ARG D 102     -24.866  61.426 -24.325  1.00 92.58           N  
+ANISOU10681  N   ARG D 102    11365  12791  11021   1607  -1274   2806       N  
+ATOM  10682  CA  ARG D 102     -26.012  60.591 -24.666  1.00 85.05           C  
+ANISOU10682  CA  ARG D 102    10178  12190   9946   1678  -1460   2535       C  
+ATOM  10683  C   ARG D 102     -26.018  59.268 -23.912  1.00 89.15           C  
+ANISOU10683  C   ARG D 102    10596  12686  10589   1478  -1373   2066       C  
+ATOM  10684  O   ARG D 102     -27.059  58.624 -23.778  1.00 95.54           O  
+ANISOU10684  O   ARG D 102    11198  13645  11459   1502  -1485   1800       O  
+ATOM  10685  CB  ARG D 102     -26.043  60.357 -26.177  1.00 81.14           C  
+ANISOU10685  CB  ARG D 102     9637  12216   8976   1744  -1609   2641       C  
+ATOM  10686  CG  ARG D 102     -26.383  61.627 -26.961  1.00 81.39           C  
+ANISOU10686  CG  ARG D 102     9719  12331   8874   2006  -1736   3138       C  
+ATOM  10687  CD  ARG D 102     -26.399  61.421 -28.488  1.00 82.68           C  
+ANISOU10687  CD  ARG D 102     9833  13084   8498   2096  -1887   3273       C  
+ATOM  10688  NE  ARG D 102     -25.054  61.342 -29.071  1.00102.16           N  
+ANISOU10688  NE  ARG D 102    12480  15633  10702   1947  -1713   3419       N  
+ATOM  10689  CZ  ARG D 102     -24.767  60.690 -30.188  1.00107.31           C  
+ANISOU10689  CZ  ARG D 102    13091  16806  10877   1920  -1767   3339       C  
+ATOM  10690  NH1 ARG D 102     -25.716  60.012 -30.814  1.00123.82           N  
+ANISOU10690  NH1 ARG D 102    14965  19369  12711   2007  -2000   3073       N  
+ATOM  10691  NH2 ARG D 102     -23.533  60.681 -30.647  1.00114.25           N  
+ANISOU10691  NH2 ARG D 102    14123  17746  11540   1795  -1583   3486       N  
+ATOM  10692  N   LEU D 103     -24.858  58.888 -23.390  1.00 72.95           N  
+ANISOU10692  N   LEU D 103     8683  10437   8598   1286  -1165   1983       N  
+ATOM  10693  CA  LEU D 103     -24.737  57.660 -22.620  1.00 70.05           C  
+ANISOU10693  CA  LEU D 103     8248  10001   8365   1114  -1051   1599       C  
+ATOM  10694  C   LEU D 103     -25.221  57.886 -21.196  1.00 67.89           C  
+ANISOU10694  C   LEU D 103     7939   9378   8476   1133   -977   1516       C  
+ATOM  10695  O   LEU D 103     -25.096  58.987 -20.663  1.00 66.15           O  
+ANISOU10695  O   LEU D 103     7819   8887   8427   1217   -942   1732       O  
+ATOM  10696  CB  LEU D 103     -23.289  57.167 -22.629  1.00 68.60           C  
+ANISOU10696  CB  LEU D 103     8209   9776   8079    940   -862   1563       C  
+ATOM  10697  CG  LEU D 103     -22.770  56.718 -23.996  1.00 70.49           C  
+ANISOU10697  CG  LEU D 103     8465  10402   7917    909   -899   1568       C  
+ATOM  10698  CD1 LEU D 103     -21.325  56.261 -23.896  1.00 69.02           C  
+ANISOU10698  CD1 LEU D 103     8400  10158   7667    754   -691   1529       C  
+ATOM  10699  CD2 LEU D 103     -23.651  55.621 -24.571  1.00 73.97           C  
+ANISOU10699  CD2 LEU D 103     8720  11159   8225    900  -1035   1227       C  
+ATOM  10700  N   PRO D 104     -25.781  56.841 -20.575  1.00 68.54           N  
+ANISOU10700  N   PRO D 104     7877   9463   8701   1052   -942   1197       N  
+ATOM  10701  CA  PRO D 104     -26.257  56.918 -19.192  1.00 66.36           C  
+ANISOU10701  CA  PRO D 104     7549   8911   8753   1067   -848   1103       C  
+ATOM  10702  C   PRO D 104     -25.106  56.922 -18.187  1.00 74.04           C  
+ANISOU10702  C   PRO D 104     8685   9606   9841    960   -637   1110       C  
+ATOM  10703  O   PRO D 104     -25.116  56.145 -17.234  1.00 81.67           O  
+ANISOU10703  O   PRO D 104     9605  10470  10957    878   -507    919       O  
+ATOM  10704  CB  PRO D 104     -27.114  55.659 -19.051  1.00 67.88           C  
+ANISOU10704  CB  PRO D 104     7531   9242   9019    982   -859    785       C  
+ATOM  10705  CG  PRO D 104     -26.526  54.702 -20.025  1.00 70.30           C  
+ANISOU10705  CG  PRO D 104     7858   9771   9082    851   -867    647       C  
+ATOM  10706  CD  PRO D 104     -26.067  55.531 -21.188  1.00 71.62           C  
+ANISOU10706  CD  PRO D 104     8132  10127   8953    943   -986    901       C  
+ATOM  10707  N   ILE D 105     -24.127  57.794 -18.411  1.00 64.34           N  
+ANISOU10707  N   ILE D 105     7633   8274   8540    960   -602   1340       N  
+ATOM  10708  CA  ILE D 105     -22.997  57.947 -17.503  1.00 58.42           C  
+ANISOU10708  CA  ILE D 105     7015   7294   7889    860   -428   1348       C  
+ATOM  10709  C   ILE D 105     -23.289  59.053 -16.497  1.00 56.80           C  
+ANISOU10709  C   ILE D 105     6845   6804   7933    956   -409   1418       C  
+ATOM  10710  O   ILE D 105     -23.625  60.175 -16.876  1.00 62.81           O  
+ANISOU10710  O   ILE D 105     7649   7474   8740   1078   -500   1622       O  
+ATOM  10711  CB  ILE D 105     -21.698  58.270 -18.265  1.00 58.53           C  
+ANISOU10711  CB  ILE D 105     7174   7354   7711    772   -381   1530       C  
+ATOM  10712  CG1 ILE D 105     -21.299  57.093 -19.157  1.00 60.09           C  
+ANISOU10712  CG1 ILE D 105     7337   7837   7656    682   -368   1406       C  
+ATOM  10713  CG2 ILE D 105     -20.577  58.615 -17.294  1.00 57.66           C  
+ANISOU10713  CG2 ILE D 105     7167   7015   7729    672   -226   1541       C  
+ATOM  10714  CD1 ILE D 105     -20.115  57.380 -20.050  1.00 71.61           C  
+ANISOU10714  CD1 ILE D 105     8909   9414   8887    613   -318   1591       C  
+ATOM  10715  N   HIS D 106     -23.161  58.732 -15.214  1.00 54.80           N  
+ANISOU10715  N   HIS D 106     6574   6412   7836    916   -284   1250       N  
+ATOM  10716  CA  HIS D 106     -23.533  59.664 -14.157  1.00 53.86           C  
+ANISOU10716  CA  HIS D 106     6466   6056   7942   1015   -258   1239       C  
+ATOM  10717  C   HIS D 106     -22.333  60.237 -13.407  1.00 52.47           C  
+ANISOU10717  C   HIS D 106     6425   5686   7826    924   -146   1248       C  
+ATOM  10718  O   HIS D 106     -22.500  61.065 -12.512  1.00 59.24           O  
+ANISOU10718  O   HIS D 106     7306   6339   8863    991   -119   1200       O  
+ATOM  10719  CB  HIS D 106     -24.472  58.976 -13.163  1.00 53.44           C  
+ANISOU10719  CB  HIS D 106     6260   6033   8010   1064   -204   1029       C  
+ATOM  10720  CG  HIS D 106     -25.611  58.253 -13.808  1.00 55.20           C  
+ANISOU10720  CG  HIS D 106     6311   6463   8201   1106   -301    968       C  
+ATOM  10721  ND1 HIS D 106     -26.623  58.905 -14.481  1.00 57.32           N  
+ANISOU10721  ND1 HIS D 106     6492   6792   8495   1261   -462   1061       N  
+ATOM  10722  CD2 HIS D 106     -25.900  56.932 -13.887  1.00 61.00           C  
+ANISOU10722  CD2 HIS D 106     6928   7356   8894   1009   -260    811       C  
+ATOM  10723  CE1 HIS D 106     -27.484  58.018 -14.945  1.00 59.29           C  
+ANISOU10723  CE1 HIS D 106     6559   7265   8702   1245   -532    943       C  
+ATOM  10724  NE2 HIS D 106     -27.068  56.812 -14.598  1.00 68.34           N  
+ANISOU10724  NE2 HIS D 106     7689   8452   9823   1080   -405    781       N  
+ATOM  10725  N   THR D 107     -21.127  59.809 -13.769  1.00 51.56           N  
+ANISOU10725  N   THR D 107     6380   5648   7561    772    -82   1285       N  
+ATOM  10726  CA  THR D 107     -19.934  60.293 -13.078  1.00 50.71           C  
+ANISOU10726  CA  THR D 107     6361   5402   7503    665     15   1272       C  
+ATOM  10727  C   THR D 107     -18.821  60.765 -14.011  1.00 58.90           C  
+ANISOU10727  C   THR D 107     7500   6443   8438    543     24   1468       C  
+ATOM  10728  O   THR D 107     -18.264  59.991 -14.796  1.00 72.97           O  
+ANISOU10728  O   THR D 107     9274   8432  10019    467     48   1508       O  
+ATOM  10729  CB  THR D 107     -19.359  59.211 -12.148  1.00 50.14           C  
+ANISOU10729  CB  THR D 107     6237   5437   7375    595    135   1088       C  
+ATOM  10730  OG1 THR D 107     -20.354  58.825 -11.193  1.00 56.32           O  
+ANISOU10730  OG1 THR D 107     6927   6216   8256    699    158    937       O  
+ATOM  10731  CG2 THR D 107     -18.140  59.742 -11.410  1.00 49.85           C  
+ANISOU10731  CG2 THR D 107     6257   5312   7372    492    209   1053       C  
+ATOM  10732  N   TYR D 108     -18.499  62.049 -13.898  1.00 59.51           N  
+ANISOU10732  N   TYR D 108     7664   6276   8670    521     22   1581       N  
+ATOM  10733  CA  TYR D 108     -17.402  62.654 -14.636  1.00 56.05           C  
+ANISOU10733  CA  TYR D 108     7314   5796   8188    380     62   1786       C  
+ATOM  10734  C   TYR D 108     -16.393  63.270 -13.673  1.00 61.23           C  
+ANISOU10734  C   TYR D 108     7996   6264   9005    235    149   1679       C  
+ATOM  10735  O   TYR D 108     -16.750  64.081 -12.827  1.00 64.22           O  
+ANISOU10735  O   TYR D 108     8397   6391   9611    281    137   1573       O  
+ATOM  10736  CB  TYR D 108     -17.918  63.724 -15.601  1.00 64.40           C  
+ANISOU10736  CB  TYR D 108     8453   6708   9307    467    -16   2080       C  
+ATOM  10737  CG  TYR D 108     -18.730  63.187 -16.756  1.00 63.08           C  
+ANISOU10737  CG  TYR D 108     8246   6801   8919    593   -121   2212       C  
+ATOM  10738  CD1 TYR D 108     -20.094  62.964 -16.626  1.00 71.25           C  
+ANISOU10738  CD1 TYR D 108     9196   7880   9994    781   -232   2124       C  
+ATOM  10739  CD2 TYR D 108     -18.136  62.912 -17.981  1.00 53.82           C  
+ANISOU10739  CD2 TYR D 108     7100   5864   7485    525   -111   2407       C  
+ATOM  10740  CE1 TYR D 108     -20.842  62.478 -17.679  1.00 73.48           C  
+ANISOU10740  CE1 TYR D 108     9414   8437  10070    885   -349   2208       C  
+ATOM  10741  CE2 TYR D 108     -18.876  62.426 -19.040  1.00 55.20           C  
+ANISOU10741  CE2 TYR D 108     7227   6322   7426    642   -223   2488       C  
+ATOM  10742  CZ  TYR D 108     -20.229  62.210 -18.883  1.00 68.23           C  
+ANISOU10742  CZ  TYR D 108     8784   8013   9128    817   -351   2380       C  
+ATOM  10743  OH  TYR D 108     -20.972  61.725 -19.934  1.00 70.53           O  
+ANISOU10743  OH  TYR D 108     8998   8620   9180    923   -482   2426       O  
+ATOM  10744  N   TRP D 109     -15.139  62.859 -13.797  1.00 64.92           N  
+ANISOU10744  N   TRP D 109     8442   6875   9349     66    233   1678       N  
+ATOM  10745  CA  TRP D 109     -14.021  63.513 -13.137  1.00 59.66           C  
+ANISOU10745  CA  TRP D 109     7777   6077   8816   -110    305   1606       C  
+ATOM  10746  C   TRP D 109     -13.203  64.197 -14.222  1.00 60.70           C  
+ANISOU10746  C   TRP D 109     7966   6157   8942   -264    354   1887       C  
+ATOM  10747  O   TRP D 109     -13.066  63.659 -15.320  1.00 75.84           O  
+ANISOU10747  O   TRP D 109     9884   8298  10634   -258    368   2067       O  
+ATOM  10748  CB  TRP D 109     -13.169  62.504 -12.365  1.00 53.58           C  
+ANISOU10748  CB  TRP D 109     6897   5548   7911   -176    369   1394       C  
+ATOM  10749  CG  TRP D 109     -13.817  62.009 -11.112  1.00 54.05           C  
+ANISOU10749  CG  TRP D 109     6904   5634   7999    -47    350   1144       C  
+ATOM  10750  CD1 TRP D 109     -14.712  60.985 -11.005  1.00 59.27           C  
+ANISOU10750  CD1 TRP D 109     7527   6433   8559    106    336   1087       C  
+ATOM  10751  CD2 TRP D 109     -13.627  62.517  -9.787  1.00 56.46           C  
+ANISOU10751  CD2 TRP D 109     7176   5842   8434    -65    355    915       C  
+ATOM  10752  NE1 TRP D 109     -15.091  60.824  -9.695  1.00 63.47           N  
+ANISOU10752  NE1 TRP D 109     8008   6962   9145    189    348    878       N  
+ATOM  10753  CE2 TRP D 109     -14.437  61.751  -8.926  1.00 56.29           C  
+ANISOU10753  CE2 TRP D 109     7102   5932   8353     99    354    760       C  
+ATOM  10754  CE3 TRP D 109     -12.846  63.542  -9.244  1.00 59.03           C  
+ANISOU10754  CE3 TRP D 109     7500   6009   8918   -215    363    811       C  
+ATOM  10755  CZ2 TRP D 109     -14.495  61.982  -7.554  1.00 65.16           C  
+ANISOU10755  CZ2 TRP D 109     8180   7051   9527    143    362    521       C  
+ATOM  10756  CZ3 TRP D 109     -12.906  63.770  -7.881  1.00 61.88           C  
+ANISOU10756  CZ3 TRP D 109     7811   6358   9341   -180    353    527       C  
+ATOM  10757  CH2 TRP D 109     -13.723  62.992  -7.052  1.00 63.73           C  
+ANISOU10757  CH2 TRP D 109     8001   6745   9469     10    352    393       C  
+ATOM  10758  N   THR D 110     -12.669  65.379 -13.938  1.00 55.34           N  
+ANISOU10758  N   THR D 110     7330   5187   8509   -406    392   1921       N  
+ATOM  10759  CA  THR D 110     -11.832  66.047 -14.926  1.00 56.90           C  
+ANISOU10759  CA  THR D 110     7573   5322   8726   -580    472   2217       C  
+ATOM  10760  C   THR D 110     -10.843  67.017 -14.292  1.00 70.43           C  
+ANISOU10760  C   THR D 110     9267   6778  10715   -823    547   2130       C  
+ATOM  10761  O   THR D 110     -11.085  67.560 -13.214  1.00 75.70           O  
+ANISOU10761  O   THR D 110     9938   7207  11618   -820    510   1878       O  
+ATOM  10762  CB  THR D 110     -12.688  66.810 -15.962  1.00 57.03           C  
+ANISOU10762  CB  THR D 110     7718   5155   8795   -454    430   2564       C  
+ATOM  10763  OG1 THR D 110     -11.835  67.420 -16.939  1.00 60.70           O  
+ANISOU10763  OG1 THR D 110     8226   5582   9255   -626    534   2897       O  
+ATOM  10764  CG2 THR D 110     -13.527  67.881 -15.285  1.00 65.84           C  
+ANISOU10764  CG2 THR D 110     8916   5841  10258   -351    373   2503       C  
+ATOM  10765  N   THR D 111      -9.722  67.224 -14.976  1.00 69.00           N  
+ANISOU10765  N   THR D 111     9051   6667  10499  -1042    656   2322       N  
+ATOM  10766  CA  THR D 111      -8.741  68.220 -14.571  1.00 73.26           C  
+ANISOU10766  CA  THR D 111     9555   6951  11328  -1320    740   2277       C  
+ATOM  10767  C   THR D 111      -8.735  69.391 -15.545  1.00 79.78           C  
+ANISOU10767  C   THR D 111    10509   7444  12361  -1415    819   2678       C  
+ATOM  10768  O   THR D 111      -7.878  70.271 -15.470  1.00 76.26           O  
+ANISOU10768  O   THR D 111    10040   6755  12181  -1685    921   2721       O  
+ATOM  10769  CB  THR D 111      -7.327  67.620 -14.482  1.00 64.76           C  
+ANISOU10769  CB  THR D 111     8296   6208  10103  -1535    828   2179       C  
+ATOM  10770  OG1 THR D 111      -7.006  66.962 -15.713  1.00 79.01           O  
+ANISOU10770  OG1 THR D 111    10086   8329  11606  -1516    903   2466       O  
+ATOM  10771  CG2 THR D 111      -7.249  66.618 -13.341  1.00 63.55           C  
+ANISOU10771  CG2 THR D 111     8016   6327   9802  -1440    755   1792       C  
+ATOM  10772  N   ASN D 112      -9.701  69.397 -16.458  1.00 79.44           N  
+ANISOU10772  N   ASN D 112    10589   7395  12198  -1194    775   2980       N  
+ATOM  10773  CA  ASN D 112      -9.827  70.475 -17.429  1.00 85.14           C  
+ANISOU10773  CA  ASN D 112    11458   7929  12960  -1185    812   3277       C  
+ATOM  10774  C   ASN D 112     -10.450  71.717 -16.810  1.00 93.28           C  
+ANISOU10774  C   ASN D 112    12612   8461  14371  -1134    767   3177       C  
+ATOM  10775  O   ASN D 112     -11.216  71.627 -15.850  1.00105.63           O  
+ANISOU10775  O   ASN D 112    14170   9875  16088   -993    673   2919       O  
+ATOM  10776  CB  ASN D 112     -10.663  70.029 -18.631  1.00 75.13           C  
+ANISOU10776  CB  ASN D 112    10262   6932  11352   -931    747   3559       C  
+ATOM  10777  CG  ASN D 112     -10.056  68.849 -19.360  1.00 80.98           C  
+ANISOU10777  CG  ASN D 112    10897   8176  11695   -968    799   3638       C  
+ATOM  10778  OD1 ASN D 112      -8.864  68.573 -19.236  1.00 84.35           O  
+ANISOU10778  OD1 ASN D 112    11213   8747  12091  -1197    916   3572       O  
+ATOM  10779  ND2 ASN D 112     -10.877  68.148 -20.133  1.00 79.49           N  
+ANISOU10779  ND2 ASN D 112    10728   8277  11197   -738    710   3757       N  
+ATOM  10780  N   TYR D 113     -10.118  72.877 -17.364  1.00101.48           N  
+ANISOU10780  N   TYR D 113    13759   9242  15557  -1243    846   3376       N  
+ATOM  10781  CA  TYR D 113     -10.690  74.131 -16.898  1.00105.58           C  
+ANISOU10781  CA  TYR D 113    14409   9271  16435  -1185    819   3307       C  
+ATOM  10782  C   TYR D 113     -11.931  74.455 -17.721  1.00113.99           C  
+ANISOU10782  C   TYR D 113    15614  10299  17397   -860    736   3589       C  
+ATOM  10783  O   TYR D 113     -12.849  75.126 -17.247  1.00117.93           O  
+ANISOU10783  O   TYR D 113    16199  10490  18120   -677    663   3494       O  
+ATOM  10784  CB  TYR D 113      -9.665  75.264 -16.990  1.00 91.44           C  
+ANISOU10784  CB  TYR D 113    12661   7179  14904  -1489    954   3364       C  
+ATOM  10785  N   ASP D 114     -11.945  73.972 -18.960  1.00100.99           N  
+ANISOU10785  N   ASP D 114    13975   8998  15399   -782    745   3920       N  
+ATOM  10786  CA  ASP D 114     -13.070  74.178 -19.865  1.00 88.52           C  
+ANISOU10786  CA  ASP D 114    12495   7475  13664   -477    651   4204       C  
+ATOM  10787  C   ASP D 114     -14.345  73.539 -19.318  1.00 80.81           C  
+ANISOU10787  C   ASP D 114    11472   6590  12643   -188    484   4007       C  
+ATOM  10788  O   ASP D 114     -14.290  72.677 -18.440  1.00 85.05           O  
+ANISOU10788  O   ASP D 114    11894   7247  13174   -222    453   3704       O  
+ATOM  10789  CB  ASP D 114     -12.739  73.618 -21.253  1.00 86.98           C  
+ANISOU10789  CB  ASP D 114    12284   7716  13051   -468    688   4534       C  
+ATOM  10790  CG  ASP D 114     -12.512  72.115 -21.242  1.00 80.02           C  
+ANISOU10790  CG  ASP D 114    11249   7312  11842   -479    657   4384       C  
+ATOM  10791  OD1 ASP D 114     -11.346  71.691 -21.382  1.00 79.84           O  
+ANISOU10791  OD1 ASP D 114    11146   7483  11706   -715    780   4368       O  
+ATOM  10792  OD2 ASP D 114     -13.492  71.358 -21.082  1.00 86.53           O  
+ANISOU10792  OD2 ASP D 114    12027   8317  12533   -253    515   4276       O  
+ATOM  10793  N   ARG D 115     -15.491  73.959 -19.845  1.00 81.59           N  
+ANISOU10793  N   ARG D 115    11646   6645  12709     98    381   4189       N  
+ATOM  10794  CA  ARG D 115     -16.774  73.441 -19.385  1.00 83.05           C  
+ANISOU10794  CA  ARG D 115    11769   6922  12864    381    224   4015       C  
+ATOM  10795  C   ARG D 115     -17.419  72.549 -20.435  1.00 87.49           C  
+ANISOU10795  C   ARG D 115    12266   7957  13018    573    112   4213       C  
+ATOM  10796  O   ARG D 115     -18.643  72.485 -20.519  1.00 82.63           O  
+ANISOU10796  O   ARG D 115    11623   7406  12365    850    -29   4215       O  
+ATOM  10797  CB  ARG D 115     -17.750  74.570 -19.058  1.00 85.35           C  
+ANISOU10797  CB  ARG D 115    12160   6824  13446    596    168   4009       C  
+ATOM  10798  CG  ARG D 115     -17.334  75.546 -17.978  1.00 93.75           C  
+ANISOU10798  CG  ARG D 115    13292   7395  14931    452    257   3766       C  
+ATOM  10799  CD  ARG D 115     -18.591  76.221 -17.464  1.00 86.67           C  
+ANISOU10799  CD  ARG D 115    12441   6238  14251    744    167   3652       C  
+ATOM  10800  NE  ARG D 115     -18.353  77.431 -16.690  1.00107.45           N  
+ANISOU10800  NE  ARG D 115    15179   8357  17290    660    247   3483       N  
+ATOM  10801  CZ  ARG D 115     -19.293  78.341 -16.459  1.00116.65           C  
+ANISOU10801  CZ  ARG D 115    16428   9217  18676    902    204   3464       C  
+ATOM  10802  NH1 ARG D 115     -20.520  78.154 -16.929  1.00119.27           N  
+ANISOU10802  NH1 ARG D 115    16731   9727  18857   1238     76   3607       N  
+ATOM  10803  NH2 ARG D 115     -19.017  79.428 -15.754  1.00112.64           N  
+ANISOU10803  NH2 ARG D 115    16021   8237  18542    811    284   3286       N  
+ATOM  10804  N   LEU D 116     -16.609  71.862 -21.231  1.00 86.54           N  
+ANISOU10804  N   LEU D 116    12106   8185  12588    429    173   4355       N  
+ATOM  10805  CA  LEU D 116     -17.133  71.087 -22.352  1.00 81.84           C  
+ANISOU10805  CA  LEU D 116    11455   8062  11578    595     71   4538       C  
+ATOM  10806  C   LEU D 116     -18.075  69.969 -21.913  1.00 83.99           C  
+ANISOU10806  C   LEU D 116    11590   8584  11738    765    -78   4302       C  
+ATOM  10807  O   LEU D 116     -19.093  69.723 -22.560  1.00 94.09           O  
+ANISOU10807  O   LEU D 116    12824  10107  12820   1001   -227   4399       O  
+ATOM  10808  CB  LEU D 116     -15.986  70.506 -23.181  1.00 69.95           C  
+ANISOU10808  CB  LEU D 116     9922   6896   9760    393    186   4669       C  
+ATOM  10809  CG  LEU D 116     -15.128  71.537 -23.917  1.00 77.88           C  
+ANISOU10809  CG  LEU D 116    11042   7749  10800    246    334   4971       C  
+ATOM  10810  CD1 LEU D 116     -14.081  70.848 -24.772  1.00 76.75           C  
+ANISOU10810  CD1 LEU D 116    10843   8013  10305     81    446   5073       C  
+ATOM  10811  CD2 LEU D 116     -15.997  72.455 -24.763  1.00 77.91           C  
+ANISOU10811  CD2 LEU D 116    11152   7669  10782    480    256   5292       C  
+ATOM  10812  N   ILE D 117     -17.735  69.292 -20.821  1.00 70.82           N  
+ANISOU10812  N   ILE D 117     9845   6869  10196    644    -40   3994       N  
+ATOM  10813  CA  ILE D 117     -18.550  68.190 -20.321  1.00 68.92           C  
+ANISOU10813  CA  ILE D 117     9469   6839   9880    781   -155   3768       C  
+ATOM  10814  C   ILE D 117     -19.956  68.643 -19.912  1.00 81.32           C  
+ANISOU10814  C   ILE D 117    11015   8248  11634   1050   -290   3690       C  
+ATOM  10815  O   ILE D 117     -20.955  68.113 -20.404  1.00 76.87           O  
+ANISOU10815  O   ILE D 117    10354   7967  10886   1255   -436   3722       O  
+ATOM  10816  CB  ILE D 117     -17.874  67.512 -19.114  1.00 60.75           C  
+ANISOU10816  CB  ILE D 117     8368   5731   8982    602    -69   3456       C  
+ATOM  10817  CG1 ILE D 117     -16.553  66.863 -19.535  1.00 65.44           C  
+ANISOU10817  CG1 ILE D 117     8944   6585   9335    358     52   3464       C  
+ATOM  10818  CG2 ILE D 117     -18.809  66.493 -18.477  1.00 56.49           C  
+ANISOU10818  CG2 ILE D 117     7699   5396   8370    731   -171   3100       C  
+ATOM  10819  CD1 ILE D 117     -15.720  66.371 -18.372  1.00 55.14           C  
+ANISOU10819  CD1 ILE D 117     7578   5240   8132    165    144   3099       C  
+ATOM  10820  N   GLU D 118     -20.027  69.627 -19.018  1.00 90.38           N  
+ANISOU10820  N   GLU D 118    12237   8965  13141   1050   -241   3568       N  
+ATOM  10821  CA  GLU D 118     -21.310  70.147 -18.547  1.00 88.08           C  
+ANISOU10821  CA  GLU D 118    11922   8505  13041   1310   -342   3466       C  
+ATOM  10822  C   GLU D 118     -22.106  70.801 -19.676  1.00 87.59           C  
+ANISOU10822  C   GLU D 118    11904   8514  12861   1533   -450   3776       C  
+ATOM  10823  O   GLU D 118     -23.337  70.735 -19.699  1.00 78.48           O  
+ANISOU10823  O   GLU D 118    10657   7463  11698   1790   -588   3740       O  
+ATOM  10824  CB  GLU D 118     -21.103  71.142 -17.402  1.00 82.32           C  
+ANISOU10824  CB  GLU D 118    11277   7302  12697   1253   -251   3257       C  
+ATOM  10825  CG  GLU D 118     -19.948  72.100 -17.605  1.00 90.42           C  
+ANISOU10825  CG  GLU D 118    12455   8040  13859   1025   -117   3398       C  
+ATOM  10826  CD  GLU D 118     -18.680  71.634 -16.920  1.00 86.73           C  
+ANISOU10826  CD  GLU D 118    11959   7557  13439    720      3   3204       C  
+ATOM  10827  OE1 GLU D 118     -18.190  72.353 -16.025  1.00 96.51           O  
+ANISOU10827  OE1 GLU D 118    13246   8450  14972    588     83   3004       O  
+ATOM  10828  OE2 GLU D 118     -18.174  70.549 -17.276  1.00 80.57           O  
+ANISOU10828  OE2 GLU D 118    11097   7119  12397    617     13   3240       O  
+ATOM  10829  N   LYS D 119     -21.395  71.438 -20.604  1.00 78.91           N  
+ANISOU10829  N   LYS D 119    10935   7376  11674   1437   -383   4083       N  
+ATOM  10830  CA  LYS D 119     -22.022  72.054 -21.770  1.00 81.00           C  
+ANISOU10830  CA  LYS D 119    11251   7736  11791   1641   -475   4421       C  
+ATOM  10831  C   LYS D 119     -22.695  70.993 -22.631  1.00 80.01           C  
+ANISOU10831  C   LYS D 119    10974   8157  11270   1786   -636   4479       C  
+ATOM  10832  O   LYS D 119     -23.848  71.146 -23.038  1.00 77.76           O  
+ANISOU10832  O   LYS D 119    10621   8005  10921   2053   -796   4554       O  
+ATOM  10833  CB  LYS D 119     -20.991  72.831 -22.594  1.00 76.97           C  
+ANISOU10833  CB  LYS D 119    10897   7109  11240   1476   -344   4742       C  
+ATOM  10834  N   ALA D 120     -21.960  69.922 -22.912  1.00 89.03           N  
+ANISOU10834  N   ALA D 120    12053   9627  12146   1609   -595   4430       N  
+ATOM  10835  CA  ALA D 120     -22.481  68.811 -23.697  1.00 89.43           C  
+ANISOU10835  CA  ALA D 120    11953  10218  11807   1709   -740   4429       C  
+ATOM  10836  C   ALA D 120     -23.679  68.171 -23.002  1.00 87.80           C  
+ANISOU10836  C   ALA D 120    11566  10104  11689   1886   -889   4160       C  
+ATOM  10837  O   ALA D 120     -24.677  67.841 -23.645  1.00 79.51           O  
+ANISOU10837  O   ALA D 120    10384   9391  10435   2086  -1070   4191       O  
+ATOM  10838  CB  ALA D 120     -21.392  67.777 -23.942  1.00 74.60           C  
+ANISOU10838  CB  ALA D 120    10050   8625   9671   1475   -643   4371       C  
+ATOM  10839  N   LEU D 121     -23.575  67.999 -21.687  1.00 76.49           N  
+ANISOU10839  N   LEU D 121    10110   8394  10558   1805   -811   3884       N  
+ATOM  10840  CA  LEU D 121     -24.674  67.446 -20.900  1.00 76.93           C  
+ANISOU10840  CA  LEU D 121     9984   8502  10743   1959   -914   3616       C  
+ATOM  10841  C   LEU D 121     -25.935  68.307 -20.973  1.00 84.13           C  
+ANISOU10841  C   LEU D 121    10860   9316  11788   2241  -1039   3668       C  
+ATOM  10842  O   LEU D 121     -27.041  67.788 -21.131  1.00 79.91           O  
+ANISOU10842  O   LEU D 121    10130   9067  11167   2421  -1197   3580       O  
+ATOM  10843  CB  LEU D 121     -24.251  67.281 -19.437  1.00 69.32           C  
+ANISOU10843  CB  LEU D 121     9026   7227  10084   1822   -778   3321       C  
+ATOM  10844  CG  LEU D 121     -23.269  66.151 -19.136  1.00 71.69           C  
+ANISOU10844  CG  LEU D 121     9309   7706  10224   1546   -672   3085       C  
+ATOM  10845  CD1 LEU D 121     -22.804  66.219 -17.691  1.00 68.16           C  
+ANISOU10845  CD1 LEU D 121     8891   6958  10049   1414   -536   2786       C  
+ATOM  10846  CD2 LEU D 121     -23.915  64.809 -19.434  1.00 72.42           C  
+ANISOU10846  CD2 LEU D 121     9220   8241  10054   1560   -771   2859       C  
+ATOM  10847  N   GLU D 122     -25.759  69.621 -20.862  1.00 82.52           N  
+ANISOU10847  N   GLU D 122    10835   8716  11804   2275   -966   3802       N  
+ATOM  10848  CA  GLU D 122     -26.885  70.554 -20.826  1.00 83.40           C  
+ANISOU10848  CA  GLU D 122    10936   8668  12083   2554  -1063   3850       C  
+ATOM  10849  C   GLU D 122     -27.503  70.705 -22.221  1.00 98.14           C  
+ANISOU10849  C   GLU D 122    12763  10863  13662   2745  -1233   4154       C  
+ATOM  10850  O   GLU D 122     -28.698  70.982 -22.347  1.00104.21           O  
+ANISOU10850  O   GLU D 122    13417  11713  14465   3010  -1383   4158       O  
+ATOM  10851  CB  GLU D 122     -26.445  71.905 -20.256  1.00 88.21           C  
+ANISOU10851  CB  GLU D 122    11756   8732  13029   2523   -926   3885       C  
+ATOM  10852  CG  GLU D 122     -27.591  72.794 -19.759  1.00108.61           C  
+ANISOU10852  CG  GLU D 122    14322  11075  15869   2807   -990   3810       C  
+ATOM  10853  CD  GLU D 122     -27.089  74.124 -19.223  1.00119.87           C  
+ANISOU10853  CD  GLU D 122    15965  11952  17628   2764   -850   3828       C  
+ATOM  10854  OE1 GLU D 122     -25.927  74.170 -18.765  1.00121.41           O  
+ANISOU10854  OE1 GLU D 122    16269  11942  17919   2484   -694   3745       O  
+ATOM  10855  OE2 GLU D 122     -27.864  75.105 -19.214  1.00115.49           O  
+ANISOU10855  OE2 GLU D 122    15458  11171  17251   3008   -898   3899       O  
+ATOM  10856  N   GLU D 123     -26.685  70.554 -23.263  1.00 94.89           N  
+ANISOU10856  N   GLU D 123    12437  10656  12960   2614  -1205   4404       N  
+ATOM  10857  CA  GLU D 123     -27.196  70.522 -24.633  1.00 96.43           C  
+ANISOU10857  CA  GLU D 123    12575  11258  12806   2776  -1366   4665       C  
+ATOM  10858  C   GLU D 123     -28.044  69.280 -24.866  1.00 93.60           C  
+ANISOU10858  C   GLU D 123    11947  11422  12193   2860  -1554   4459       C  
+ATOM  10859  O   GLU D 123     -28.879  69.244 -25.769  1.00 99.92           O  
+ANISOU10859  O   GLU D 123    12628  12577  12759   3052  -1742   4570       O  
+ATOM  10860  CB  GLU D 123     -26.061  70.528 -25.664  1.00 98.38           C  
+ANISOU10860  CB  GLU D 123    12958  11660  12761   2598  -1268   4937       C  
+ATOM  10861  CG  GLU D 123     -25.816  71.842 -26.387  1.00109.09           C  
+ANISOU10861  CG  GLU D 123    14507  12783  14159   2669  -1211   5329       C  
+ATOM  10862  CD  GLU D 123     -24.733  71.719 -27.453  1.00116.57           C  
+ANISOU10862  CD  GLU D 123    15548  13964  14778   2494  -1106   5583       C  
+ATOM  10863  OE1 GLU D 123     -24.671  70.663 -28.119  1.00112.79           O  
+ANISOU10863  OE1 GLU D 123    14949  14004  13903   2457  -1180   5519       O  
+ATOM  10864  OE2 GLU D 123     -23.952  72.678 -27.633  1.00121.64           O  
+ANISOU10864  OE2 GLU D 123    16378  14282  15557   2392   -946   5832       O  
+ATOM  10865  N   GLU D 124     -27.815  68.262 -24.046  1.00 92.95           N  
+ANISOU10865  N   GLU D 124    11760  11391  12164   2708  -1504   4153       N  
+ATOM  10866  CA  GLU D 124     -28.561  67.015 -24.127  1.00 91.49           C  
+ANISOU10866  CA  GLU D 124    11305  11668  11791   2749  -1661   3913       C  
+ATOM  10867  C   GLU D 124     -29.738  67.008 -23.162  1.00 89.13           C  
+ANISOU10867  C   GLU D 124    10818  11258  11789   2912  -1731   3666       C  
+ATOM  10868  O   GLU D 124     -30.294  65.952 -22.858  1.00 93.40           O  
+ANISOU10868  O   GLU D 124    11117  12081  12291   2899  -1809   3403       O  
+ATOM  10869  CB  GLU D 124     -27.639  65.826 -23.849  1.00 89.00           C  
+ANISOU10869  CB  GLU D 124    10964  11500  11350   2497  -1561   3738       C  
+ATOM  10870  CG  GLU D 124     -26.944  65.285 -25.090  1.00 95.67           C  
+ANISOU10870  CG  GLU D 124    11846  12766  11739   2392  -1585   3871       C  
+ATOM  10871  CD  GLU D 124     -27.909  64.650 -26.069  1.00109.51           C  
+ANISOU10871  CD  GLU D 124    13378  15089  13141   2532  -1826   3793       C  
+ATOM  10872  OE1 GLU D 124     -28.872  63.995 -25.618  1.00116.08           O  
+ANISOU10872  OE1 GLU D 124    13966  16084  14055   2606  -1954   3520       O  
+ATOM  10873  OE2 GLU D 124     -27.704  64.804 -27.291  1.00122.73           O  
+ANISOU10873  OE2 GLU D 124    15108  17062  14461   2557  -1880   3984       O  
+ATOM  10874  N   ASN D 125     -30.091  68.194 -22.673  1.00 86.85           N  
+ANISOU10874  N   ASN D 125    10637  10559  11802   3056  -1690   3738       N  
+ATOM  10875  CA  ASN D 125     -31.200  68.373 -21.740  1.00 80.11           C  
+ANISOU10875  CA  ASN D 125     9625   9576  11238   3232  -1731   3508       C  
+ATOM  10876  C   ASN D 125     -31.022  67.576 -20.450  1.00 79.59           C  
+ANISOU10876  C   ASN D 125     9467   9407  11368   3082  -1600   3166       C  
+ATOM  10877  O   ASN D 125     -31.993  67.080 -19.877  1.00 77.26           O  
+ANISOU10877  O   ASN D 125     8930   9249  11178   3175  -1656   2923       O  
+ATOM  10878  CB  ASN D 125     -32.524  67.992 -22.409  1.00 79.31           C  
+ANISOU10878  CB  ASN D 125     9240   9924  10970   3441  -1976   3476       C  
+ATOM  10879  CG  ASN D 125     -32.937  68.976 -23.485  1.00100.29           C  
+ANISOU10879  CG  ASN D 125    11970  12629  13506   3654  -2110   3805       C  
+ATOM  10880  OD1 ASN D 125     -32.708  70.179 -23.363  1.00104.66           O  
+ANISOU10880  OD1 ASN D 125    12742  12768  14254   3742  -2027   4000       O  
+ATOM  10881  ND2 ASN D 125     -33.548  68.467 -24.549  1.00109.80           N  
+ANISOU10881  ND2 ASN D 125    12985  14346  14386   3735  -2319   3859       N  
+ATOM  10882  N   LYS D 126     -29.778  67.456 -19.999  1.00 70.91           N  
+ANISOU10882  N   LYS D 126     8547   8077  10319   2843  -1418   3150       N  
+ATOM  10883  CA  LYS D 126     -29.486  66.814 -18.722  1.00 82.95           C  
+ANISOU10883  CA  LYS D 126    10017   9458  12041   2697  -1276   2847       C  
+ATOM  10884  C   LYS D 126     -29.061  67.822 -17.660  1.00 80.54           C  
+ANISOU10884  C   LYS D 126     9903   8651  12047   2666  -1109   2753       C  
+ATOM  10885  O   LYS D 126     -28.481  68.862 -17.972  1.00 84.21           O  
+ANISOU10885  O   LYS D 126    10589   8843  12563   2648  -1058   2948       O  
+ATOM  10886  CB  LYS D 126     -28.397  65.752 -18.887  1.00 80.04           C  
+ANISOU10886  CB  LYS D 126     9691   9260  11460   2403  -1195   2774       C  
+ATOM  10887  CG  LYS D 126     -28.826  64.533 -19.680  1.00 81.68           C  
+ANISOU10887  CG  LYS D 126     9712   9979  11343   2344  -1323   2648       C  
+ATOM  10888  CD  LYS D 126     -27.766  63.448 -19.615  1.00 69.54           C  
+ANISOU10888  CD  LYS D 126     8240   8550   9630   2030  -1198   2448       C  
+ATOM  10889  CE  LYS D 126     -28.190  62.216 -20.392  1.00 67.32           C  
+ANISOU10889  CE  LYS D 126     7780   8734   9063   1962  -1315   2272       C  
+ATOM  10890  NZ  LYS D 126     -27.175  61.132 -20.296  1.00 68.28           N  
+ANISOU10890  NZ  LYS D 126     7967   8925   9052   1685  -1178   2064       N  
+ATOM  10891  N   ILE D 127     -29.352  67.502 -16.404  1.00 72.87           N  
+ANISOU10891  N   ILE D 127     8834   7580  11273   2653  -1018   2438       N  
+ATOM  10892  CA  ILE D 127     -29.000  68.375 -15.292  1.00 67.67           C  
+ANISOU10892  CA  ILE D 127     8327   6511  10875   2626   -868   2275       C  
+ATOM  10893  C   ILE D 127     -27.662  67.946 -14.702  1.00 66.55           C  
+ANISOU10893  C   ILE D 127     8295   6242  10749   2342   -718   2171       C  
+ATOM  10894  O   ILE D 127     -27.504  66.808 -14.260  1.00 67.58           O  
+ANISOU10894  O   ILE D 127     8307   6571  10800   2220   -676   1991       O  
+ATOM  10895  CB  ILE D 127     -30.081  68.358 -14.195  1.00 68.97           C  
+ANISOU10895  CB  ILE D 127     8325   6673  11206   2789   -840   1974       C  
+ATOM  10896  CG1 ILE D 127     -31.351  69.054 -14.690  1.00 78.99           C  
+ANISOU10896  CG1 ILE D 127     9507   8003  12504   3093   -977   2073       C  
+ATOM  10897  CG2 ILE D 127     -29.571  69.035 -12.933  1.00 70.30           C  
+ANISOU10897  CG2 ILE D 127     8634   6489  11588   2725   -674   1744       C  
+ATOM  10898  CD1 ILE D 127     -32.602  68.647 -13.943  1.00 79.97           C  
+ANISOU10898  CD1 ILE D 127     9369   8314  12702   3255   -985   1815       C  
+ATOM  10899  N   ALA D 128     -26.702  68.865 -14.698  1.00 72.44           N  
+ANISOU10899  N   ALA D 128     9265   6673  11588   2223   -633   2265       N  
+ATOM  10900  CA  ALA D 128     -25.356  68.564 -14.225  1.00 65.33           C  
+ANISOU10900  CA  ALA D 128     8458   5662  10701   1948   -503   2183       C  
+ATOM  10901  C   ALA D 128     -25.090  69.146 -12.842  1.00 66.35           C  
+ANISOU10901  C   ALA D 128     8643   5487  11080   1904   -384   1876       C  
+ATOM  10902  O   ALA D 128     -25.238  70.348 -12.625  1.00 76.29           O  
+ANISOU10902  O   ALA D 128    10015   6444  12527   1981   -363   1863       O  
+ATOM  10903  CB  ALA D 128     -24.324  69.077 -15.216  1.00 59.82           C  
+ANISOU10903  CB  ALA D 128     7936   4878   9916   1793   -481   2488       C  
+ATOM  10904  N   ASP D 129     -24.697  68.286 -11.910  1.00 65.28           N  
+ANISOU10904  N   ASP D 129     8424   5444  10934   1788   -306   1623       N  
+ATOM  10905  CA  ASP D 129     -24.254  68.734 -10.596  1.00 66.65           C  
+ANISOU10905  CA  ASP D 129     8641   5391  11291   1722   -195   1314       C  
+ATOM  10906  C   ASP D 129     -22.751  68.989 -10.642  1.00 64.90           C  
+ANISOU10906  C   ASP D 129     8558   5033  11066   1435   -122   1341       C  
+ATOM  10907  O   ASP D 129     -21.951  68.058 -10.545  1.00 68.41           O  
+ANISOU10907  O   ASP D 129     8971   5740  11280   1236    -81   1269       O  
+ATOM  10908  CB  ASP D 129     -24.598  67.703  -9.520  1.00 80.27           C  
+ANISOU10908  CB  ASP D 129    10214   7406  12878   1718   -139    991       C  
+ATOM  10909  CG  ASP D 129     -24.461  68.256  -8.111  1.00 81.11           C  
+ANISOU10909  CG  ASP D 129    10334   7332  13151   1736    -43    652       C  
+ATOM  10910  OD1 ASP D 129     -23.845  69.329  -7.938  1.00 86.49           O  
+ANISOU10910  OD1 ASP D 129    11150   7662  14048   1678    -17    615       O  
+ATOM  10911  OD2 ASP D 129     -24.979  67.617  -7.171  1.00 77.07           O  
+ANISOU10911  OD2 ASP D 129     9692   7038  12552   1803     12    415       O  
+ATOM  10912  N   VAL D 130     -22.375  70.254 -10.788  1.00 58.55           N  
+ANISOU10912  N   VAL D 130     7902   3862  10484   1400    -99   1422       N  
+ATOM  10913  CA  VAL D 130     -20.976  70.628 -10.966  1.00 65.88           C  
+ANISOU10913  CA  VAL D 130     8941   4619  11473   1119    -27   1493       C  
+ATOM  10914  C   VAL D 130     -20.303  70.943  -9.634  1.00 67.66           C  
+ANISOU10914  C   VAL D 130     9166   4658  11883    982     56   1106       C  
+ATOM  10915  O   VAL D 130     -20.765  71.795  -8.876  1.00 80.50           O  
+ANISOU10915  O   VAL D 130    10823   6053  13710   1087     70    872       O  
+ATOM  10916  CB  VAL D 130     -20.834  71.842 -11.902  1.00 67.07           C  
+ANISOU10916  CB  VAL D 130     9250   4513  11719   1102    -30   1781       C  
+ATOM  10917  CG1 VAL D 130     -19.366  72.128 -12.177  1.00 62.10           C  
+ANISOU10917  CG1 VAL D 130     8703   3762  11132    782     60   1877       C  
+ATOM  10918  CG2 VAL D 130     -21.583  71.598 -13.202  1.00 64.20           C  
+ANISOU10918  CG2 VAL D 130     8879   4373  11142   1274   -129   2138       C  
+ATOM  10919  N   LYS D 131     -19.204  70.246  -9.359  1.00 68.47           N  
+ANISOU10919  N   LYS D 131     9227   5004  11786    732    102    989       N  
+ATOM  10920  CA  LYS D 131     -18.494  70.387  -8.093  1.00 75.68           C  
+ANISOU10920  CA  LYS D 131    10106   5894  12756    588    157    592       C  
+ATOM  10921  C   LYS D 131     -17.084  70.935  -8.292  1.00 79.04           C  
+ANISOU10921  C   LYS D 131    10587   6152  13293    273    210    622       C  
+ATOM  10922  O   LYS D 131     -16.257  70.303  -8.949  1.00 88.41           O  
+ANISOU10922  O   LYS D 131    11747   7574  14271    102    229    810       O  
+ATOM  10923  CB  LYS D 131     -18.399  69.034  -7.380  1.00 71.68           C  
+ANISOU10923  CB  LYS D 131     9459   5865  11910    584    166    393       C  
+ATOM  10924  CG  LYS D 131     -19.684  68.223  -7.330  1.00 75.01           C  
+ANISOU10924  CG  LYS D 131     9795   6522  12185    834    133    411       C  
+ATOM  10925  CD  LYS D 131     -20.687  68.807  -6.354  1.00 70.78           C  
+ANISOU10925  CD  LYS D 131     9229   5839  11826   1052    142    150       C  
+ATOM  10926  CE  LYS D 131     -21.755  67.781  -6.013  1.00 58.61           C  
+ANISOU10926  CE  LYS D 131     7549   4625  10096   1241    145    103       C  
+ATOM  10927  NZ  LYS D 131     -22.793  68.329  -5.099  1.00 59.00           N  
+ANISOU10927  NZ  LYS D 131     7544   4573  10300   1473    171   -140       N  
+ATOM  10928  N   TYR D 132     -16.808  72.109  -7.731  1.00 72.72           N  
+ANISOU10928  N   TYR D 132     9850   4943  12835    192    244    419       N  
+ATOM  10929  CA  TYR D 132     -15.448  72.636  -7.749  1.00 80.99           C  
+ANISOU10929  CA  TYR D 132    10913   5837  14022   -145    301    376       C  
+ATOM  10930  C   TYR D 132     -15.009  73.148  -6.375  1.00 85.57           C  
+ANISOU10930  C   TYR D 132    11440   6316  14758   -257    312   -147       C  
+ATOM  10931  O   TYR D 132     -13.840  73.481  -6.179  1.00 99.22           O  
+ANISOU10931  O   TYR D 132    13129   7992  16579   -557    345   -281       O  
+ATOM  10932  CB  TYR D 132     -15.305  73.743  -8.804  1.00 81.91           C  
+ANISOU10932  CB  TYR D 132    11178   5539  14406   -222    343    733       C  
+ATOM  10933  CG  TYR D 132     -16.455  74.724  -8.880  1.00 75.66           C  
+ANISOU10933  CG  TYR D 132    10507   4484  13756     39    312    770       C  
+ATOM  10934  CD1 TYR D 132     -17.464  74.569  -9.823  1.00 73.89           C  
+ANISOU10934  CD1 TYR D 132    10332   4358  13385    297    258   1123       C  
+ATOM  10935  CD2 TYR D 132     -16.523  75.816  -8.024  1.00 97.25           C  
+ANISOU10935  CD2 TYR D 132    13296   6889  16766     28    333    440       C  
+ATOM  10936  CE1 TYR D 132     -18.514  75.468  -9.904  1.00 91.36           C  
+ANISOU10936  CE1 TYR D 132    12638   6343  15731    546    228   1163       C  
+ATOM  10937  CE2 TYR D 132     -17.570  76.720  -8.096  1.00101.39           C  
+ANISOU10937  CE2 TYR D 132    13930   7164  17431    280    316    483       C  
+ATOM  10938  CZ  TYR D 132     -18.563  76.541  -9.038  1.00 95.25           C  
+ANISOU10938  CZ  TYR D 132    13193   6484  16512    542    264    854       C  
+ATOM  10939  OH  TYR D 132     -19.606  77.436  -9.114  1.00 91.03           O  
+ANISOU10939  OH  TYR D 132    12753   5714  16121    805    243    899       O  
+ATOM  10940  N   THR D 133     -15.942  73.213  -5.429  1.00 77.44           N  
+ANISOU10940  N   THR D 133    10389   5288  13745    -18    284   -456       N  
+ATOM  10941  CA  THR D 133     -15.599  73.525  -4.043  1.00 85.14           C  
+ANISOU10941  CA  THR D 133    11292   6292  14766    -86    284   -997       C  
+ATOM  10942  C   THR D 133     -15.885  72.337  -3.122  1.00 86.01           C  
+ANISOU10942  C   THR D 133    11260   6967  14454     62    258  -1209       C  
+ATOM  10943  O   THR D 133     -16.626  71.424  -3.487  1.00 77.79           O  
+ANISOU10943  O   THR D 133    10193   6186  13180    254    249   -973       O  
+ATOM  10944  CB  THR D 133     -16.359  74.760  -3.522  1.00 89.10           C  
+ANISOU10944  CB  THR D 133    11888   6309  15659     65    300  -1258       C  
+ATOM  10945  OG1 THR D 133     -17.736  74.427  -3.315  1.00 89.65           O  
+ANISOU10945  OG1 THR D 133    11946   6504  15613    430    284  -1242       O  
+ATOM  10946  CG2 THR D 133     -16.254  75.915  -4.509  1.00 87.56           C  
+ANISOU10946  CG2 THR D 133    11854   5718  15696    -23    326   -923       C  
+ATOM  10947  N   VAL D 134     -15.292  72.357  -1.932  1.00 84.57           N  
+ANISOU10947  N   VAL D 134    10977   6979  14177    -34    248  -1651       N  
+ATOM  10948  CA  VAL D 134     -15.508  71.308  -0.938  1.00 74.42           C  
+ANISOU10948  CA  VAL D 134     9557   6229  12489    114    239  -1848       C  
+ATOM  10949  C   VAL D 134     -16.944  71.311  -0.411  1.00 78.51           C  
+ANISOU10949  C   VAL D 134    10086   6744  13000    449    263  -1956       C  
+ATOM  10950  O   VAL D 134     -17.566  70.257  -0.261  1.00 69.70           O  
+ANISOU10950  O   VAL D 134     8898   5990  11594    627    283  -1830       O  
+ATOM  10951  CB  VAL D 134     -14.524  71.458   0.249  1.00 73.48           C  
+ANISOU10951  CB  VAL D 134     9319   6344  12256    -51    210  -2312       C  
+ATOM  10952  CG1 VAL D 134     -15.074  70.797   1.506  1.00 73.66           C  
+ANISOU10952  CG1 VAL D 134     9236   6814  11939    182    217  -2588       C  
+ATOM  10953  CG2 VAL D 134     -13.167  70.875  -0.110  1.00 74.73           C  
+ANISOU10953  CG2 VAL D 134     9383   6768  12242   -317    186  -2174       C  
+ATOM  10954  N   LYS D 135     -17.467  72.505  -0.149  1.00 84.53           N  
+ANISOU10954  N   LYS D 135    10929   7079  14110    533    275  -2186       N  
+ATOM  10955  CA  LYS D 135     -18.805  72.660   0.415  1.00 80.43           C  
+ANISOU10955  CA  LYS D 135    10400   6539  13620    861    310  -2340       C  
+ATOM  10956  C   LYS D 135     -19.879  72.106  -0.519  1.00 84.49           C  
+ANISOU10956  C   LYS D 135    10929   7068  14105   1074    314  -1900       C  
+ATOM  10957  O   LYS D 135     -20.872  71.531  -0.067  1.00 83.74           O  
+ANISOU10957  O   LYS D 135    10745   7233  13840   1316    348  -1934       O  
+ATOM  10958  CB  LYS D 135     -19.074  74.135   0.731  1.00 76.07           C  
+ANISOU10958  CB  LYS D 135     9946   5450  13508    908    327  -2660       C  
+ATOM  10959  CG  LYS D 135     -20.475  74.435   1.241  1.00 77.19           C  
+ANISOU10959  CG  LYS D 135    10081   5635  13612   1242    365  -2744       C  
+ATOM  10960  CD  LYS D 135     -20.536  75.813   1.887  1.00 79.93           C  
+ANISOU10960  CD  LYS D 135    10511   5692  14168   1235    380  -3080       C  
+ATOM  10961  CE  LYS D 135     -21.969  76.285   2.077  1.00 88.74           C  
+ANISOU10961  CE  LYS D 135    11651   6744  15322   1568    424  -3061       C  
+ATOM  10962  NZ  LYS D 135     -22.066  77.319   3.147  1.00 92.64           N  
+ANISOU10962  NZ  LYS D 135    12172   7120  15908   1606    459  -3529       N  
+ATOM  10963  N   GLN D 136     -19.668  72.264  -1.823  1.00 88.69           N  
+ANISOU10963  N   GLN D 136    11556   7353  14790    975    282  -1492       N  
+ATOM  10964  CA  GLN D 136     -20.620  71.784  -2.820  1.00 73.83           C  
+ANISOU10964  CA  GLN D 136     9677   5506  12870   1159    259  -1082       C  
+ATOM  10965  C   GLN D 136     -20.766  70.264  -2.797  1.00 65.28           C  
+ANISOU10965  C   GLN D 136     8468   4959  11378   1181    263   -952       C  
+ATOM  10966  O   GLN D 136     -21.740  69.721  -3.319  1.00 81.26           O  
+ANISOU10966  O   GLN D 136    10442   7098  13333   1356    248   -730       O  
+ATOM  10967  CB  GLN D 136     -20.199  72.239  -4.219  1.00 76.18           C  
+ANISOU10967  CB  GLN D 136    10099   5494  13352   1029    224   -669       C  
+ATOM  10968  CG  GLN D 136     -20.503  73.696  -4.524  1.00 76.56           C  
+ANISOU10968  CG  GLN D 136    10290   5072  13727   1080    225   -625       C  
+ATOM  10969  CD  GLN D 136     -19.954  74.136  -5.868  1.00 80.32           C  
+ANISOU10969  CD  GLN D 136    10890   5344  14282    922    209   -188       C  
+ATOM  10970  OE1 GLN D 136     -18.845  73.761  -6.252  1.00 89.19           O  
+ANISOU10970  OE1 GLN D 136    12009   6510  15368    660    225    -77       O  
+ATOM  10971  NE2 GLN D 136     -20.728  74.937  -6.590  1.00 70.20           N  
+ANISOU10971  NE2 GLN D 136     9713   3866  13095   1090    185     67       N  
+ATOM  10972  N   LEU D 137     -19.797  69.581  -2.194  1.00 68.39           N  
+ANISOU10972  N   LEU D 137     8799   5672  11515   1005    282  -1094       N  
+ATOM  10973  CA  LEU D 137     -19.859  68.130  -2.054  1.00 65.71           C  
+ANISOU10973  CA  LEU D 137     8347   5802  10816   1029    307   -984       C  
+ATOM  10974  C   LEU D 137     -20.877  67.717  -1.000  1.00 63.67           C  
+ANISOU10974  C   LEU D 137     7979   5783  10428   1264    370  -1186       C  
+ATOM  10975  O   LEU D 137     -21.364  66.587  -1.005  1.00 64.41           O  
+ANISOU10975  O   LEU D 137     7982   6180  10310   1340    410  -1041       O  
+ATOM  10976  CB  LEU D 137     -18.484  67.559  -1.705  1.00 66.32           C  
+ANISOU10976  CB  LEU D 137     8384   6146  10670    805    312  -1052       C  
+ATOM  10977  CG  LEU D 137     -17.408  67.679  -2.785  1.00 70.39           C  
+ANISOU10977  CG  LEU D 137     8965   6533  11246    559    275   -813       C  
+ATOM  10978  CD1 LEU D 137     -16.057  67.243  -2.246  1.00 68.55           C  
+ANISOU10978  CD1 LEU D 137     8653   6578  10815    362    279   -949       C  
+ATOM  10979  CD2 LEU D 137     -17.787  66.861  -4.010  1.00 63.69           C  
+ANISOU10979  CD2 LEU D 137     8132   5764  10302    595    265   -419       C  
+ATOM  10980  N   ALA D 138     -21.198  68.637  -0.095  1.00 67.61           N  
+ANISOU10980  N   ALA D 138     8482   6140  11067   1372    394  -1530       N  
+ATOM  10981  CA  ALA D 138     -22.149  68.342   0.970  1.00 67.47           C  
+ANISOU10981  CA  ALA D 138     8350   6372  10915   1603    476  -1744       C  
+ATOM  10982  C   ALA D 138     -23.579  68.443   0.455  1.00 77.55           C  
+ANISOU10982  C   ALA D 138     9590   7520  12356   1840    488  -1584       C  
+ATOM  10983  O   ALA D 138     -24.516  67.977   1.102  1.00 91.65           O  
+ANISOU10983  O   ALA D 138    11249   9552  14024   2030    571  -1661       O  
+ATOM  10984  CB  ALA D 138     -21.938  69.281   2.146  1.00 65.76           C  
+ANISOU10984  CB  ALA D 138     8137   6091  10756   1642    500  -2218       C  
+ATOM  10985  N   THR D 139     -23.737  69.056  -0.713  1.00 77.81           N  
+ANISOU10985  N   THR D 139     9720   7192  12654   1832    409  -1346       N  
+ATOM  10986  CA  THR D 139     -25.053  69.244  -1.307  1.00 66.00           C  
+ANISOU10986  CA  THR D 139     8175   5576  11324   2070    390  -1176       C  
+ATOM  10987  C   THR D 139     -25.241  68.280  -2.479  1.00 68.75           C  
+ANISOU10987  C   THR D 139     8486   6086  11548   2011    331   -777       C  
+ATOM  10988  O   THR D 139     -24.267  67.845  -3.096  1.00 85.33           O  
+ANISOU10988  O   THR D 139    10657   8231  13535   1788    293   -602       O  
+ATOM  10989  CB  THR D 139     -25.248  70.702  -1.781  1.00 80.96           C  
+ANISOU10989  CB  THR D 139    10215   7012  13535   2134    335  -1152       C  
+ATOM  10990  OG1 THR D 139     -24.719  71.601  -0.799  1.00 98.05           O  
+ANISOU10990  OG1 THR D 139    12451   9008  15797   2084    378  -1533       O  
+ATOM  10991  CG2 THR D 139     -26.723  71.015  -2.004  1.00 78.47           C  
+ANISOU10991  CG2 THR D 139     9844   6727  13244   2396    324  -1044       C  
+ATOM  10992  N   THR D 140     -26.494  67.953  -2.783  1.00 69.38           N  
+ANISOU10992  N   THR D 140     8438   6272  11651   2210    324   -660       N  
+ATOM  10993  CA  THR D 140     -26.831  67.101  -3.921  1.00 66.78           C  
+ANISOU10993  CA  THR D 140     8050   6100  11223   2172    252   -334       C  
+ATOM  10994  C   THR D 140     -27.921  67.758  -4.771  1.00 79.14           C  
+ANISOU10994  C   THR D 140     9594   7536  12940   2368    153   -158       C  
+ATOM  10995  O   THR D 140     -29.061  67.885  -4.334  1.00 76.42           O  
+ANISOU10995  O   THR D 140     9132   7308  12596   2557    180   -256       O  
+ATOM  10996  CB  THR D 140     -27.302  65.709  -3.469  1.00 69.48           C  
+ANISOU10996  CB  THR D 140     8216   6853  11330   2156    334   -354       C  
+ATOM  10997  OG1 THR D 140     -26.274  65.085  -2.689  1.00 77.49           O  
+ANISOU10997  OG1 THR D 140     9268   8042  12132   1982    420   -472       O  
+ATOM  10998  CG2 THR D 140     -27.606  64.840  -4.676  1.00 71.80           C  
+ANISOU10998  CG2 THR D 140     8449   7289  11545   2090    252    -75       C  
+ATOM  10999  N   LYS D 141     -27.553  68.179  -5.977  1.00 80.00           N  
+ANISOU10999  N   LYS D 141     9825   7463  13109   2309     43    117       N  
+ATOM  11000  CA  LYS D 141     -28.441  68.914  -6.865  1.00 73.14           C  
+ANISOU11000  CA  LYS D 141     8974   6503  12314   2484    -63    319       C  
+ATOM  11001  C   LYS D 141     -29.605  68.011  -7.277  1.00 81.59           C  
+ANISOU11001  C   LYS D 141     9821   7912  13268   2606   -119    404       C  
+ATOM  11002  O   LYS D 141     -29.398  66.867  -7.680  1.00 69.83           O  
+ANISOU11002  O   LYS D 141     8236   6647  11650   2483   -134    491       O  
+ATOM  11003  CB  LYS D 141     -27.644  69.409  -8.083  1.00 65.16           C  
+ANISOU11003  CB  LYS D 141     8138   5287  11334   2368   -149    626       C  
+ATOM  11004  CG  LYS D 141     -28.156  70.690  -8.742  1.00 80.02           C  
+ANISOU11004  CG  LYS D 141    10134   6918  13350   2537   -220    799       C  
+ATOM  11005  CD  LYS D 141     -27.343  71.006  -9.998  1.00 88.18           C  
+ANISOU11005  CD  LYS D 141    11325   7822  14358   2404   -284   1146       C  
+ATOM  11006  CE  LYS D 141     -27.479  72.471 -10.381  1.00 82.56           C  
+ANISOU11006  CE  LYS D 141    10785   6755  13830   2520   -301   1282       C  
+ATOM  11007  NZ  LYS D 141     -27.395  73.366  -9.193  1.00 87.82           N  
+ANISOU11007  NZ  LYS D 141    11526   7119  14721   2545   -197    966       N  
+ATOM  11008  N   VAL D 142     -30.826  68.519  -7.143  1.00 89.11           N  
+ANISOU11008  N   VAL D 142    10677   8899  14281   2845   -141    359       N  
+ATOM  11009  CA  VAL D 142     -32.027  67.742  -7.444  1.00 85.01           C  
+ANISOU11009  CA  VAL D 142     9907   8710  13685   2962   -191    398       C  
+ATOM  11010  C   VAL D 142     -32.140  67.338  -8.919  1.00 91.45           C  
+ANISOU11010  C   VAL D 142    10674   9647  14423   2944   -359    694       C  
+ATOM  11011  O   VAL D 142     -31.808  68.114  -9.818  1.00 99.92           O  
+ANISOU11011  O   VAL D 142    11906  10537  15521   2979   -459    917       O  
+ATOM  11012  CB  VAL D 142     -33.304  68.505  -7.028  1.00 75.52           C  
+ANISOU11012  CB  VAL D 142     8603   7517  12572   3247   -180    298       C  
+ATOM  11013  CG1 VAL D 142     -33.334  68.704  -5.520  1.00 75.31           C  
+ANISOU11013  CG1 VAL D 142     8573   7470  12570   3276     -2    -15       C  
+ATOM  11014  CG2 VAL D 142     -33.401  69.843  -7.753  1.00 79.08           C  
+ANISOU11014  CG2 VAL D 142     9223   7675  13150   3417   -281    472       C  
+ATOM  11015  N   LYS D 143     -32.580  66.101  -9.145  1.00 77.44           N  
+ANISOU11015  N   LYS D 143     8678   8194  12551   2878   -381    690       N  
+ATOM  11016  CA  LYS D 143     -32.872  65.582 -10.485  1.00 74.03           C  
+ANISOU11016  CA  LYS D 143     8136   7963  12029   2878   -553    914       C  
+ATOM  11017  C   LYS D 143     -31.650  65.584 -11.395  1.00 78.15           C  
+ANISOU11017  C   LYS D 143     8860   8373  12462   2720   -614   1144       C  
+ATOM  11018  O   LYS D 143     -31.781  65.628 -12.619  1.00 94.72           O  
+ANISOU11018  O   LYS D 143    10944  10583  14460   2768   -773   1382       O  
+ATOM  11019  CB  LYS D 143     -34.004  66.382 -11.138  1.00 65.32           C  
+ANISOU11019  CB  LYS D 143     6946   6913  10960   3152   -700   1029       C  
+ATOM  11020  N   ARG D 144     -30.465  65.538 -10.795  1.00 68.96           N  
+ANISOU11020  N   ARG D 144     7872   7029  11300   2533   -486   1070       N  
+ATOM  11021  CA  ARG D 144     -29.229  65.529 -11.564  1.00 60.91           C  
+ANISOU11021  CA  ARG D 144     7059   5946  10137   2332   -508   1250       C  
+ATOM  11022  C   ARG D 144     -29.105  64.235 -12.362  1.00 59.81           C  
+ANISOU11022  C   ARG D 144     6836   6159   9728   2159   -562   1285       C  
+ATOM  11023  O   ARG D 144     -29.571  63.181 -11.931  1.00 65.58           O  
+ANISOU11023  O   ARG D 144     7401   7115  10402   2093   -513   1100       O  
+ATOM  11024  CB  ARG D 144     -28.018  65.709 -10.645  1.00 61.74           C  
+ANISOU11024  CB  ARG D 144     7339   5844  10276   2148   -358   1105       C  
+ATOM  11025  CG  ARG D 144     -27.731  64.529  -9.726  1.00 56.03           C  
+ANISOU11025  CG  ARG D 144     6538   5333   9417   1982   -231    865       C  
+ATOM  11026  CD  ARG D 144     -26.663  64.889  -8.705  1.00 69.69           C  
+ANISOU11026  CD  ARG D 144     8408   6887  11186   1862   -106    703       C  
+ATOM  11027  NE  ARG D 144     -26.232  63.737  -7.919  1.00 72.21           N  
+ANISOU11027  NE  ARG D 144     8670   7432  11336   1714     10    540       N  
+ATOM  11028  CZ  ARG D 144     -25.305  63.786  -6.967  1.00 85.88           C  
+ANISOU11028  CZ  ARG D 144    10478   9122  13030   1607    111    383       C  
+ATOM  11029  NH1 ARG D 144     -24.707  64.934  -6.678  1.00 98.09           N  
+ANISOU11029  NH1 ARG D 144    12155  10399  14716   1600    109    324       N  
+ATOM  11030  NH2 ARG D 144     -24.972  62.686  -6.307  1.00 76.76           N  
+ANISOU11030  NH2 ARG D 144     9262   8196  11708   1510    213    287       N  
+ATOM  11031  N   ASP D 145     -28.480  64.326 -13.530  1.00 66.30           N  
+ANISOU11031  N   ASP D 145     7774   7022  10394   2086   -649   1520       N  
+ATOM  11032  CA  ASP D 145     -28.236  63.152 -14.356  1.00 72.16           C  
+ANISOU11032  CA  ASP D 145     8460   8088  10869   1921   -695   1524       C  
+ATOM  11033  C   ASP D 145     -26.773  62.734 -14.273  1.00 67.55           C  
+ANISOU11033  C   ASP D 145     8048   7459  10160   1669   -576   1508       C  
+ATOM  11034  O   ASP D 145     -26.440  61.562 -14.446  1.00 65.30           O  
+ANISOU11034  O   ASP D 145     7717   7387   9706   1508   -540   1399       O  
+ATOM  11035  CB  ASP D 145     -28.631  63.426 -15.808  1.00 71.31           C  
+ANISOU11035  CB  ASP D 145     8324   8162  10607   2037   -884   1782       C  
+ATOM  11036  CG  ASP D 145     -30.102  63.767 -15.957  1.00 84.65           C  
+ANISOU11036  CG  ASP D 145     9803   9960  12400   2305  -1026   1801       C  
+ATOM  11037  OD1 ASP D 145     -30.938  62.842 -15.879  1.00 86.38           O  
+ANISOU11037  OD1 ASP D 145     9789  10450  12581   2288  -1066   1604       O  
+ATOM  11038  OD2 ASP D 145     -30.423  64.959 -16.148  1.00 98.24           O  
+ANISOU11038  OD2 ASP D 145    11579  11485  14261   2534  -1090   2015       O  
+ATOM  11039  N   ALA D 146     -25.902  63.702 -14.006  1.00 70.14           N  
+ANISOU11039  N   ALA D 146     8559   7496  10592   1636   -511   1607       N  
+ATOM  11040  CA  ALA D 146     -24.474  63.433 -13.886  1.00 72.52           C  
+ANISOU11040  CA  ALA D 146     8997   7760  10796   1403   -400   1594       C  
+ATOM  11041  C   ALA D 146     -23.809  64.387 -12.902  1.00 78.17           C  
+ANISOU11041  C   ALA D 146     9835   8143  11724   1366   -299   1526       C  
+ATOM  11042  O   ALA D 146     -24.222  65.538 -12.763  1.00 92.69           O  
+ANISOU11042  O   ALA D 146    11724   9712  13782   1511   -328   1596       O  
+ATOM  11043  CB  ALA D 146     -23.803  63.527 -15.247  1.00 71.08           C  
+ANISOU11043  CB  ALA D 146     8910   7680  10418   1328   -455   1861       C  
+ATOM  11044  N   VAL D 147     -22.774  63.901 -12.225  1.00 60.13           N  
+ANISOU11044  N   VAL D 147     7587   5881   9379   1179   -185   1375       N  
+ATOM  11045  CA  VAL D 147     -21.937  64.748 -11.383  1.00 61.61           C  
+ANISOU11045  CA  VAL D 147     7877   5805   9728   1094   -102   1282       C  
+ATOM  11046  C   VAL D 147     -20.638  65.060 -12.114  1.00 64.22           C  
+ANISOU11046  C   VAL D 147     8327   6079   9995    898    -74   1466       C  
+ATOM  11047  O   VAL D 147     -20.014  64.166 -12.679  1.00 56.84           O  
+ANISOU11047  O   VAL D 147     7375   5390   8834    775    -54   1522       O  
+ATOM  11048  CB  VAL D 147     -21.622  64.076 -10.035  1.00 68.88           C  
+ANISOU11048  CB  VAL D 147     8732   6829  10611   1031      0    986       C  
+ATOM  11049  CG1 VAL D 147     -20.803  65.008  -9.154  1.00 70.17           C  
+ANISOU11049  CG1 VAL D 147     8976   6756  10927    947     60    841       C  
+ATOM  11050  CG2 VAL D 147     -22.905  63.678  -9.336  1.00 73.95           C  
+ANISOU11050  CG2 VAL D 147     9239   7565  11295   1211      3    830       C  
+ATOM  11051  N   VAL D 148     -20.227  66.323 -12.105  1.00 60.52           N  
+ANISOU11051  N   VAL D 148     7972   5277   9743    865    -58   1556       N  
+ATOM  11052  CA  VAL D 148     -18.978  66.708 -12.751  1.00 57.57           C  
+ANISOU11052  CA  VAL D 148     7696   4831   9347    654     -6   1742       C  
+ATOM  11053  C   VAL D 148     -17.996  67.325 -11.759  1.00 63.60           C  
+ANISOU11053  C   VAL D 148     8495   5375  10294    477     81   1536       C  
+ATOM  11054  O   VAL D 148     -18.136  68.481 -11.358  1.00 59.31           O  
+ANISOU11054  O   VAL D 148     8024   4464  10046    505     90   1493       O  
+ATOM  11055  CB  VAL D 148     -19.218  67.699 -13.904  1.00 62.09           C  
+ANISOU11055  CB  VAL D 148     8375   5198  10017    727    -51   2117       C  
+ATOM  11056  CG1 VAL D 148     -17.902  68.045 -14.586  1.00 69.60           C  
+ANISOU11056  CG1 VAL D 148     9411   6101  10934    488     33   2336       C  
+ATOM  11057  CG2 VAL D 148     -20.203  67.116 -14.905  1.00 60.17           C  
+ANISOU11057  CG2 VAL D 148     8073   5232   9558    913   -165   2302       C  
+ATOM  11058  N   TYR D 149     -17.006  66.531 -11.369  1.00 56.37           N  
+ANISOU11058  N   TYR D 149     7517   4695   9207    303    141   1392       N  
+ATOM  11059  CA  TYR D 149     -15.931  66.983 -10.501  1.00 57.85           C  
+ANISOU11059  CA  TYR D 149     7698   4772   9511    109    207   1185       C  
+ATOM  11060  C   TYR D 149     -14.867  67.714 -11.309  1.00 68.83           C  
+ANISOU11060  C   TYR D 149     9157   6001  10994   -113    260   1413       C  
+ATOM  11061  O   TYR D 149     -14.152  67.109 -12.112  1.00 69.96           O  
+ANISOU11061  O   TYR D 149     9273   6381  10925   -226    297   1591       O  
+ATOM  11062  CB  TYR D 149     -15.302  65.802  -9.764  1.00 60.42           C  
+ANISOU11062  CB  TYR D 149     7905   5454   9599     44    243    970       C  
+ATOM  11063  CG  TYR D 149     -16.267  64.997  -8.924  1.00 57.57           C  
+ANISOU11063  CG  TYR D 149     7468   5266   9140    239    226    777       C  
+ATOM  11064  CD1 TYR D 149     -16.540  65.353  -7.610  1.00 59.17           C  
+ANISOU11064  CD1 TYR D 149     7637   5402   9442    305    235    484       C  
+ATOM  11065  CD2 TYR D 149     -16.904  63.880  -9.447  1.00 55.49           C  
+ANISOU11065  CD2 TYR D 149     7158   5239   8685    348    211    880       C  
+ATOM  11066  CE1 TYR D 149     -17.419  64.616  -6.840  1.00 61.18           C  
+ANISOU11066  CE1 TYR D 149     7814   5836   9597    480    246    341       C  
+ATOM  11067  CE2 TYR D 149     -17.784  63.138  -8.686  1.00 54.96           C  
+ANISOU11067  CE2 TYR D 149     7011   5313   8560    499    219    726       C  
+ATOM  11068  CZ  TYR D 149     -18.039  63.510  -7.384  1.00 65.38           C  
+ANISOU11068  CZ  TYR D 149     8298   6576   9969    568    244    479       C  
+ATOM  11069  OH  TYR D 149     -18.917  62.773  -6.622  1.00 69.28           O  
+ANISOU11069  OH  TYR D 149     8700   7229  10393    717    278    358       O  
+ATOM  11070  N   LYS D 150     -14.771  69.019 -11.087  1.00 66.24           N  
+ANISOU11070  N   LYS D 150     8912   5258  10998   -177    280   1401       N  
+ATOM  11071  CA  LYS D 150     -13.751  69.838 -11.721  1.00 61.10           C  
+ANISOU11071  CA  LYS D 150     8319   4391  10506   -421    357   1608       C  
+ATOM  11072  C   LYS D 150     -12.691  70.186 -10.684  1.00 78.56           C  
+ANISOU11072  C   LYS D 150    10456   6530  12864   -666    405   1272       C  
+ATOM  11073  O   LYS D 150     -12.589  71.331 -10.243  1.00 96.44           O  
+ANISOU11073  O   LYS D 150    12777   8384  15480   -757    428   1149       O  
+ATOM  11074  CB  LYS D 150     -14.377  71.099 -12.314  1.00 74.12           C  
+ANISOU11074  CB  LYS D 150    10118   5574  12470   -332    359   1874       C  
+ATOM  11075  CG  LYS D 150     -15.588  70.814 -13.192  1.00 72.39           C  
+ANISOU11075  CG  LYS D 150     9944   5457  12103    -40    276   2161       C  
+ATOM  11076  CD  LYS D 150     -15.338  71.168 -14.645  1.00 72.13           C  
+ANISOU11076  CD  LYS D 150     9998   5485  11925    -76    302   2591       C  
+ATOM  11077  CE  LYS D 150     -15.254  72.671 -14.831  1.00 78.40           C  
+ANISOU11077  CE  LYS D 150    10930   5879  12977   -120    346   2685       C  
+ATOM  11078  NZ  LYS D 150     -15.403  73.060 -16.259  1.00 94.29           N  
+ANISOU11078  NZ  LYS D 150    13039   7965  14821    -51    349   3115       N  
+HETATM11079  N   MSE D 151     -11.903  69.185 -10.302  1.00 80.51           N  
+ANISOU11079  N   MSE D 151    10565   7181  12844   -765    416   1113       N  
+HETATM11080  CA  MSE D 151     -11.006  69.292  -9.154  1.00 90.00           C  
+ANISOU11080  CA  MSE D 151    11649   8445  14101   -943    426    739       C  
+HETATM11081  C   MSE D 151      -9.843  70.262  -9.357  1.00 89.13           C  
+ANISOU11081  C   MSE D 151    11519   8096  14249  -1274    499    762       C  
+HETATM11082  O   MSE D 151      -9.056  70.487  -8.437  1.00 99.71           O  
+ANISOU11082  O   MSE D 151    12742   9476  15666  -1452    494    427       O  
+HETATM11083  CB  MSE D 151     -10.465  67.908  -8.788  1.00 85.50           C  
+ANISOU11083  CB  MSE D 151    10929   8394  13164   -924    419    628       C  
+HETATM11084  CG  MSE D 151      -9.660  67.234  -9.885  1.00 82.23           C  
+ANISOU11084  CG  MSE D 151    10469   8234  12542  -1032    483    918       C  
+HETATM11085 SE   MSE D 151      -9.394  65.331  -9.544  1.00116.12          SE  
+ANISOU11085 SE   MSE D 151    14613  13110  16396   -887    478    823      SE  
+HETATM11086  CE  MSE D 151      -8.742  65.436  -7.710  1.00 68.22           C  
+ANISOU11086  CE  MSE D 151     8390   7178  10354   -950    435    354       C  
+ATOM  11087  N   HIS D 152      -9.728  70.833 -10.551  1.00 87.25           N  
+ANISOU11087  N   HIS D 152    11381   7631  14138  -1361    570   1157       N  
+ATOM  11088  CA  HIS D 152      -8.728  71.867 -10.784  1.00 91.46           C  
+ANISOU11088  CA  HIS D 152    11906   7862  14983  -1690    667   1220       C  
+ATOM  11089  C   HIS D 152      -9.397  73.189 -11.141  1.00 99.11           C  
+ANISOU11089  C   HIS D 152    13064   8232  16359  -1656    698   1401       C  
+ATOM  11090  O   HIS D 152      -8.729  74.160 -11.494  1.00 99.16           O  
+ANISOU11090  O   HIS D 152    13117   8032  16528  -1870    770   1485       O  
+ATOM  11091  CB  HIS D 152      -7.763  71.444 -11.893  1.00 87.06           C  
+ANISOU11091  CB  HIS D 152    11281   7564  14234  -1868    769   1568       C  
+ATOM  11092  N   GLY D 153     -10.723  73.220 -11.043  1.00 99.85           N  
+ANISOU11092  N   GLY D 153    13274   8215  16449  -1328    617   1409       N  
+ATOM  11093  CA  GLY D 153     -11.475  74.445 -11.234  1.00 98.08           C  
+ANISOU11093  CA  GLY D 153    13228   7606  16430  -1190    603   1481       C  
+ATOM  11094  C   GLY D 153     -12.084  74.611 -12.614  1.00109.70           C  
+ANISOU11094  C   GLY D 153    14837   9106  17740  -1009    605   1975       C  
+ATOM  11095  O   GLY D 153     -12.042  73.705 -13.446  1.00123.78           O  
+ANISOU11095  O   GLY D 153    16580  11239  19212   -961    604   2245       O  
+ATOM  11096  N   ASP D 154     -12.653  75.790 -12.845  1.00112.32           N  
+ANISOU11096  N   ASP D 154    15324   9077  18277   -903    606   2074       N  
+ATOM  11097  CA  ASP D 154     -13.311  76.126 -14.102  1.00103.47           C  
+ANISOU11097  CA  ASP D 154    14333   7948  17031   -707    598   2523       C  
+ATOM  11098  C   ASP D 154     -12.789  77.484 -14.554  1.00104.16           C  
+ANISOU11098  C   ASP D 154    14555   7649  17373   -873    697   2702       C  
+ATOM  11099  O   ASP D 154     -12.424  78.309 -13.717  1.00114.75           O  
+ANISOU11099  O   ASP D 154    15914   8644  19042  -1029    734   2415       O  
+ATOM  11100  CB  ASP D 154     -14.831  76.148 -13.944  1.00102.08           C  
+ANISOU11100  CB  ASP D 154    14209   7732  16845   -322    482   2495       C  
+ATOM  11101  N   VAL D 155     -12.731  77.714 -15.863  1.00 97.65           N  
+ANISOU11101  N   VAL D 155    13818   6888  16396   -847    744   3162       N  
+ATOM  11102  CA  VAL D 155     -12.153  78.955 -16.373  1.00100.60           C  
+ANISOU11102  CA  VAL D 155    14317   6902  17004  -1024    860   3382       C  
+ATOM  11103  C   VAL D 155     -12.914  80.188 -15.874  1.00123.03           C  
+ANISOU11103  C   VAL D 155    17302   9228  20217   -876    837   3276       C  
+ATOM  11104  O   VAL D 155     -12.310  81.219 -15.576  1.00126.66           O  
+ANISOU11104  O   VAL D 155    17826   9286  21011  -1095    927   3194       O  
+ATOM  11105  CB  VAL D 155     -12.110  78.952 -17.925  1.00116.41           C  
+ANISOU11105  CB  VAL D 155    16394   9100  18735   -964    910   3923       C  
+ATOM  11106  CG1 VAL D 155     -13.500  78.737 -18.520  1.00119.69           C  
+ANISOU11106  CG1 VAL D 155    16873   9655  18949   -552    780   4136       C  
+ATOM  11107  CG2 VAL D 155     -11.464  80.228 -18.456  1.00123.77           C  
+ANISOU11107  CG2 VAL D 155    17455   9651  19919  -1162   1051   4180       C  
+ATOM  11108  N   GLU D 156     -14.235  80.076 -15.766  1.00129.83           N  
+ANISOU11108  N   GLU D 156    18201  10104  21024   -507    719   3260       N  
+ATOM  11109  CA  GLU D 156     -15.043  81.127 -15.159  1.00129.03           C  
+ANISOU11109  CA  GLU D 156    18212   9554  21257   -326    691   3099       C  
+ATOM  11110  C   GLU D 156     -15.203  80.881 -13.662  1.00117.66           C  
+ANISOU11110  C   GLU D 156    16673   8073  19961   -331    643   2528       C  
+ATOM  11111  O   GLU D 156     -16.297  81.038 -13.124  1.00109.54           O  
+ANISOU11111  O   GLU D 156    15665   6953  19002    -40    566   2353       O  
+ATOM  11112  CB  GLU D 156     -16.408  81.221 -15.836  1.00123.64           C  
+ANISOU11112  CB  GLU D 156    17607   8920  20449     88    591   3381       C  
+ATOM  11113  N   HIS D 157     -14.087  80.589 -12.998  1.00113.71           N  
+ANISOU11113  N   HIS D 157    16061   7630  19511   -663    694   2238       N  
+ATOM  11114  CA  HIS D 157     -14.011  80.236 -11.574  1.00108.13           C  
+ANISOU11114  CA  HIS D 157    15232   6964  18889   -715    652   1679       C  
+ATOM  11115  C   HIS D 157     -12.544  80.102 -11.181  1.00104.17           C  
+ANISOU11115  C   HIS D 157    14613   6521  18448  -1136    720   1475       C  
+ATOM  11116  O   HIS D 157     -12.095  79.011 -10.828  1.00111.25           O  
+ANISOU11116  O   HIS D 157    15347   7791  19132  -1228    692   1320       O  
+ATOM  11117  CB  HIS D 157     -14.710  78.898 -11.247  1.00111.52           C  
+ANISOU11117  CB  HIS D 157    15533   7829  19011   -490    552   1567       C  
+ATOM  11118  CG  HIS D 157     -16.192  78.888 -11.465  1.00123.63           C  
+ANISOU11118  CG  HIS D 157    17125   9380  20467    -80    467   1688       C  
+ATOM  11119  ND1 HIS D 157     -16.772  78.363 -12.601  1.00121.40           N  
+ANISOU11119  ND1 HIS D 157    16860   9355  19913    112    417   2107       N  
+ATOM  11120  CD2 HIS D 157     -17.211  79.323 -10.689  1.00130.68           C  
+ANISOU11120  CD2 HIS D 157    18045  10103  21506    176    421   1425       C  
+ATOM  11121  CE1 HIS D 157     -18.085  78.484 -12.518  1.00122.10           C  
+ANISOU11121  CE1 HIS D 157    16971   9426  19996    460    335   2101       C  
+ATOM  11122  NE2 HIS D 157     -18.378  79.062 -11.368  1.00131.36           N  
+ANISOU11122  NE2 HIS D 157    18151  10338  21420    509    344   1701       N  
+ATOM  11123  N   PRO D 158     -11.789  81.212 -11.249  1.00103.98           N  
+ANISOU11123  N   PRO D 158    14659   6128  18721  -1396    811   1476       N  
+ATOM  11124  CA  PRO D 158     -10.329  81.185 -11.103  1.00110.17           C  
+ANISOU11124  CA  PRO D 158    15319   6980  19562  -1824    883   1356       C  
+ATOM  11125  C   PRO D 158      -9.876  80.656  -9.745  1.00115.88           C  
+ANISOU11125  C   PRO D 158    15850   7888  20290  -1960    820    776       C  
+ATOM  11126  O   PRO D 158      -8.672  80.632  -9.489  1.00120.92           O  
+ANISOU11126  O   PRO D 158    16351   8617  20978  -2312    858    610       O  
+ATOM  11127  CB  PRO D 158      -9.932  82.656 -11.267  1.00108.42           C  
+ANISOU11127  CB  PRO D 158    15230   6237  19727  -2012    977   1410       C  
+ATOM  11128  CG  PRO D 158     -11.155  83.419 -10.897  1.00114.71           C  
+ANISOU11128  CG  PRO D 158    16183   6674  20726  -1691    930   1310       C  
+ATOM  11129  CD  PRO D 158     -12.301  82.588 -11.376  1.00109.38           C  
+ANISOU11129  CD  PRO D 158    15533   6293  19734  -1298    848   1556       C  
+ATOM  11130  N   ILE D 173      -6.141  69.709   2.545  1.00 99.47           N  
+ANISOU11130  N   ILE D 173    11456  11873  14464  -1431   -143  -3257       N  
+ATOM  11131  CA  ILE D 173      -6.676  71.065   2.520  1.00108.20           C  
+ANISOU11131  CA  ILE D 173    12709  12391  16012  -1544   -125  -3503       C  
+ATOM  11132  C   ILE D 173      -8.022  71.100   1.809  1.00114.20           C  
+ANISOU11132  C   ILE D 173    13725  12742  16926  -1315    -32  -3169       C  
+ATOM  11133  O   ILE D 173      -9.016  70.574   2.310  1.00113.32           O  
+ANISOU11133  O   ILE D 173    13668  12797  16591  -1000    -20  -3167       O  
+ATOM  11134  CB  ILE D 173      -5.710  72.041   1.823  1.00107.98           C  
+ANISOU11134  CB  ILE D 173    12642  11977  16408  -1963   -109  -3531       C  
+ATOM  11135  N   LYS D 174      -8.045  71.715   0.632  1.00116.92           N  
+ANISOU11135  N   LYS D 174    14206  12577  17641  -1473     38  -2871       N  
+ATOM  11136  CA  LYS D 174      -9.253  71.769  -0.178  1.00109.58           C  
+ANISOU11136  CA  LYS D 174    13497  11285  16854  -1260    109  -2516       C  
+ATOM  11137  C   LYS D 174      -9.158  70.675  -1.226  1.00104.10           C  
+ANISOU11137  C   LYS D 174    12811  10810  15932  -1202    152  -1992       C  
+ATOM  11138  O   LYS D 174      -9.689  70.794  -2.330  1.00 95.83           O  
+ANISOU11138  O   LYS D 174    11913   9460  15036  -1158    209  -1608       O  
+ATOM  11139  CB  LYS D 174      -9.423  73.139  -0.835  1.00106.96           C  
+ANISOU11139  CB  LYS D 174    13322  10258  17058  -1424    162  -2479       C  
+HETATM11140  N   MSE D 175      -8.461  69.606  -0.858  1.00 99.73           N  
+ANISOU11140  N   MSE D 175    12089  10801  15003  -1188    122  -1993       N  
+HETATM11141  CA  MSE D 175      -8.224  68.479  -1.743  1.00 91.54           C  
+ANISOU11141  CA  MSE D 175    11035  10012  13735  -1137    166  -1567       C  
+HETATM11142  C   MSE D 175      -8.837  67.215  -1.156  1.00 88.49           C  
+ANISOU11142  C   MSE D 175    10615  10038  12967   -828    161  -1526       C  
+HETATM11143  O   MSE D 175      -9.313  66.347  -1.884  1.00 91.17           O  
+ANISOU11143  O   MSE D 175    11020  10438  13183   -686    210  -1187       O  
+HETATM11144  CB  MSE D 175      -6.721  68.274  -1.955  1.00 93.91           C  
+ANISOU11144  CB  MSE D 175    11148  10567  13967  -1400    160  -1554       C  
+HETATM11145  CG  MSE D 175      -5.898  69.550  -1.867  1.00109.73           C  
+ANISOU11145  CG  MSE D 175    13088  12289  16316  -1747    145  -1808       C  
+HETATM11146 SE   MSE D 175      -4.066  69.338  -2.500  1.00220.25          SE  
+ANISOU11146 SE   MSE D 175    26835  26561  30289  -2110    175  -1682      SE  
+HETATM11147  CE  MSE D 175      -3.833  67.438  -2.121  1.00 98.69           C  
+ANISOU11147  CE  MSE D 175    11288  11906  14304  -1796    143  -1546       C  
+ATOM  11148  N   ASP D 176      -8.833  67.138   0.173  1.00 92.35           N  
+ANISOU11148  N   ASP D 176    11000  10811  13276   -731    108  -1882       N  
+ATOM  11149  CA  ASP D 176      -9.095  65.890   0.889  1.00 87.13           C  
+ANISOU11149  CA  ASP D 176    10262  10621  12221   -474    116  -1840       C  
+ATOM  11150  C   ASP D 176     -10.479  65.256   0.647  1.00 80.65           C  
+ANISOU11150  C   ASP D 176     9574   9721  11346   -204    187  -1603       C  
+ATOM  11151  O   ASP D 176     -10.554  64.046   0.437  1.00 80.47           O  
+ANISOU11151  O   ASP D 176     9527   9947  11101    -73    235  -1345       O  
+ATOM  11152  CB  ASP D 176      -8.884  66.113   2.395  1.00 90.25           C  
+ANISOU11152  CB  ASP D 176    10525  11337  12428   -417     47  -2281       C  
+ATOM  11153  CG  ASP D 176      -8.819  64.816   3.176  1.00105.86           C  
+ANISOU11153  CG  ASP D 176    12388  13867  13967   -181     58  -2201       C  
+ATOM  11154  OD1 ASP D 176      -8.040  63.924   2.784  1.00113.55           O  
+ANISOU11154  OD1 ASP D 176    13274  15087  14784   -198     69  -1957       O  
+ATOM  11155  OD2 ASP D 176      -9.545  64.690   4.184  1.00108.33           O  
+ANISOU11155  OD2 ASP D 176    12697  14365  14097     32     70  -2370       O  
+ATOM  11156  N   PRO D 177     -11.574  66.047   0.686  1.00 78.47           N  
+ANISOU11156  N   PRO D 177     9423   9102  11290   -117    199  -1700       N  
+ATOM  11157  CA  PRO D 177     -12.865  65.414   0.378  1.00 76.39           C  
+ANISOU11157  CA  PRO D 177     9246   8794  10985    120    262  -1465       C  
+ATOM  11158  C   PRO D 177     -12.928  64.846  -1.042  1.00 74.83           C  
+ANISOU11158  C   PRO D 177     9119   8474  10837     81    291  -1048       C  
+ATOM  11159  O   PRO D 177     -13.472  63.760  -1.273  1.00 73.68           O  
+ANISOU11159  O   PRO D 177     8971   8494  10531    229    340   -834       O  
+ATOM  11160  CB  PRO D 177     -13.865  66.561   0.545  1.00 74.95           C  
+ANISOU11160  CB  PRO D 177     9165   8232  11081    196    258  -1652       C  
+ATOM  11161  CG  PRO D 177     -13.219  67.474   1.518  1.00 76.31           C  
+ANISOU11161  CG  PRO D 177     9277   8409  11309     81    206  -2092       C  
+ATOM  11162  CD  PRO D 177     -11.758  67.426   1.178  1.00 77.96           C  
+ANISOU11162  CD  PRO D 177     9401   8726  11495   -192    161  -2061       C  
+ATOM  11163  N   TYR D 178     -12.339  65.581  -1.980  1.00 74.40           N  
+ANISOU11163  N   TYR D 178     9123   8142  11005   -128    269   -945       N  
+ATOM  11164  CA  TYR D 178     -12.278  65.159  -3.374  1.00 72.99           C  
+ANISOU11164  CA  TYR D 178     9007   7880  10846   -180    295   -569       C  
+ATOM  11165  C   TYR D 178     -11.431  63.901  -3.543  1.00 73.77           C  
+ANISOU11165  C   TYR D 178     9002   8359  10668   -203    326   -431       C  
+ATOM  11166  O   TYR D 178     -11.762  63.023  -4.341  1.00 71.72           O  
+ANISOU11166  O   TYR D 178     8774   8166  10310   -124    362   -176       O  
+ATOM  11167  CB  TYR D 178     -11.727  66.289  -4.249  1.00 71.94           C  
+ANISOU11167  CB  TYR D 178     8947   7392  10996   -408    287   -478       C  
+ATOM  11168  CG  TYR D 178     -12.755  67.339  -4.612  1.00 69.98           C  
+ANISOU11168  CG  TYR D 178     8844   6699  11046   -332    277   -436       C  
+ATOM  11169  CD1 TYR D 178     -12.921  68.478  -3.833  1.00 77.05           C  
+ANISOU11169  CD1 TYR D 178     9768   7318  12189   -355    257   -744       C  
+ATOM  11170  CD2 TYR D 178     -13.572  67.181  -5.723  1.00 71.45           C  
+ANISOU11170  CD2 TYR D 178     9129   6755  11262   -218    282   -104       C  
+ATOM  11171  CE1 TYR D 178     -13.864  69.436  -4.161  1.00 69.61           C  
+ANISOU11171  CE1 TYR D 178     8959   5945  11545   -251    256   -695       C  
+ATOM  11172  CE2 TYR D 178     -14.515  68.131  -6.058  1.00 69.44           C  
+ANISOU11172  CE2 TYR D 178     8992   6117  11274   -111    264    -38       C  
+ATOM  11173  CZ  TYR D 178     -14.658  69.255  -5.274  1.00 71.92           C  
+ANISOU11173  CZ  TYR D 178     9341   6126  11858   -119    258   -321       C  
+ATOM  11174  OH  TYR D 178     -15.600  70.199  -5.609  1.00 84.52           O  
+ANISOU11174  OH  TYR D 178    11054   7316  13743     20    249   -244       O  
+ATOM  11175  N   ILE D 179     -10.337  63.825  -2.791  1.00 76.60           N  
+ANISOU11175  N   ILE D 179     9226   8971  10909   -303    306   -618       N  
+ATOM  11176  CA  ILE D 179      -9.464  62.658  -2.813  1.00 77.58           C  
+ANISOU11176  CA  ILE D 179     9229   9470  10776   -290    335   -506       C  
+ATOM  11177  C   ILE D 179     -10.218  61.426  -2.328  1.00 76.57           C  
+ANISOU11177  C   ILE D 179     9098   9565  10431    -30    383   -426       C  
+ATOM  11178  O   ILE D 179     -10.118  60.346  -2.919  1.00 73.63           O  
+ANISOU11178  O   ILE D 179     8721   9314   9941     35    439   -203       O  
+ATOM  11179  CB  ILE D 179      -8.216  62.881  -1.937  1.00 79.07           C  
+ANISOU11179  CB  ILE D 179     9242   9931  10872   -415    284   -753       C  
+ATOM  11180  CG1 ILE D 179      -7.320  63.955  -2.556  1.00 78.99           C  
+ANISOU11180  CG1 ILE D 179     9206   9707  11101   -721    263   -794       C  
+ATOM  11181  CG2 ILE D 179      -7.454  61.580  -1.731  1.00 77.24           C  
+ANISOU11181  CG2 ILE D 179     8872  10127  10350   -314    312   -641       C  
+ATOM  11182  CD1 ILE D 179      -6.993  63.710  -4.013  1.00 76.91           C  
+ANISOU11182  CD1 ILE D 179     8993   9336  10893   -823    331   -451       C  
+ATOM  11183  N   LYS D 180     -10.980  61.604  -1.251  1.00 76.58           N  
+ANISOU11183  N   LYS D 180     9099   9606  10392    115    374   -618       N  
+ATOM  11184  CA  LYS D 180     -11.828  60.547  -0.715  1.00 72.72           C  
+ANISOU11184  CA  LYS D 180     8606   9295   9730    351    444   -533       C  
+ATOM  11185  C   LYS D 180     -12.834  60.068  -1.753  1.00 70.40           C  
+ANISOU11185  C   LYS D 180     8417   8790   9543    412    493   -288       C  
+ATOM  11186  O   LYS D 180     -12.945  58.863  -2.019  1.00 72.62           O  
+ANISOU11186  O   LYS D 180     8683   9200   9711    499    563   -101       O  
+ATOM  11187  CB  LYS D 180     -12.563  61.027   0.540  1.00 72.86           C  
+ANISOU11187  CB  LYS D 180     8606   9372   9704    483    440   -789       C  
+ATOM  11188  CG  LYS D 180     -11.682  61.178   1.768  1.00 73.95           C  
+ANISOU11188  CG  LYS D 180     8610   9853   9633    484    393  -1047       C  
+ATOM  11189  CD  LYS D 180     -12.432  61.850   2.907  1.00 80.96           C  
+ANISOU11189  CD  LYS D 180     9493  10780  10488    602    387  -1349       C  
+ATOM  11190  CE  LYS D 180     -11.705  61.674   4.231  1.00 95.08           C  
+ANISOU11190  CE  LYS D 180    11130  13036  11958    670    351  -1573       C  
+ATOM  11191  NZ  LYS D 180     -12.617  61.950   5.377  1.00 92.16           N  
+ANISOU11191  NZ  LYS D 180    10752  12803  11462    858    388  -1804       N  
+ATOM  11192  N   ALA D 181     -13.553  61.020  -2.342  1.00 70.95           N  
+ANISOU11192  N   ALA D 181     8584   8534   9840    370    454   -298       N  
+ATOM  11193  CA  ALA D 181     -14.559  60.716  -3.354  1.00 67.09           C  
+ANISOU11193  CA  ALA D 181     8173   7871   9447    430    469    -90       C  
+ATOM  11194  C   ALA D 181     -13.974  59.941  -4.536  1.00 65.39           C  
+ANISOU11194  C   ALA D 181     7970   7706   9169    345    487    142       C  
+ATOM  11195  O   ALA D 181     -14.538  58.934  -4.977  1.00 67.69           O  
+ANISOU11195  O   ALA D 181     8262   8056   9400    430    532    276       O  
+ATOM  11196  CB  ALA D 181     -15.211  62.000  -3.840  1.00 65.69           C  
+ANISOU11196  CB  ALA D 181     8089   7348   9521    404    408   -117       C  
+ATOM  11197  N   LEU D 182     -12.837  60.411  -5.041  1.00 68.18           N  
+ANISOU11197  N   LEU D 182     8322   8042   9543    170    461    169       N  
+ATOM  11198  CA  LEU D 182     -12.182  59.763  -6.172  1.00 65.05           C  
+ANISOU11198  CA  LEU D 182     7926   7722   9069     91    490    368       C  
+ATOM  11199  C   LEU D 182     -11.691  58.361  -5.817  1.00 63.60           C  
+ANISOU11199  C   LEU D 182     7655   7826   8685    179    562    396       C  
+ATOM  11200  O   LEU D 182     -11.807  57.438  -6.623  1.00 61.62           O  
+ANISOU11200  O   LEU D 182     7422   7617   8375    217    607    536       O  
+ATOM  11201  CB  LEU D 182     -11.020  60.619  -6.684  1.00 64.90           C  
+ANISOU11201  CB  LEU D 182     7895   7645   9119   -125    471    390       C  
+ATOM  11202  CG  LEU D 182     -10.244  60.047  -7.873  1.00 61.51           C  
+ANISOU11202  CG  LEU D 182     7451   7329   8591   -210    519    589       C  
+ATOM  11203  CD1 LEU D 182     -11.193  59.652  -8.995  1.00 56.96           C  
+ANISOU11203  CD1 LEU D 182     6974   6668   8002   -129    519    768       C  
+ATOM  11204  CD2 LEU D 182      -9.226  61.054  -8.373  1.00 62.59           C  
+ANISOU11204  CD2 LEU D 182     7570   7380   8831   -441    519    632       C  
+ATOM  11205  N   SER D 183     -11.132  58.207  -4.619  1.00 65.22           N  
+ANISOU11205  N   SER D 183     7765   8232   8786    224    570    259       N  
+ATOM  11206  CA  SER D 183     -10.662  56.902  -4.161  1.00 61.55           C  
+ANISOU11206  CA  SER D 183     7216   8033   8137    347    644    317       C  
+ATOM  11207  C   SER D 183     -11.808  55.894  -4.129  1.00 58.02           C  
+ANISOU11207  C   SER D 183     6816   7544   7686    509    720    413       C  
+ATOM  11208  O   SER D 183     -11.707  54.790  -4.688  1.00 59.20           O  
+ANISOU11208  O   SER D 183     6966   7731   7795    558    793    544       O  
+ATOM  11209  CB  SER D 183     -10.025  57.020  -2.776  1.00 63.20           C  
+ANISOU11209  CB  SER D 183     7307   8495   8209    399    623    159       C  
+ATOM  11210  OG  SER D 183      -8.828  57.777  -2.829  1.00 78.71           O  
+ANISOU11210  OG  SER D 183     9187  10539  10182    226    557     55       O  
+ATOM  11211  N   GLY D 184     -12.904  56.294  -3.487  1.00 60.85           N  
+ANISOU11211  N   GLY D 184     7202   7813   8104    585    711    331       N  
+ATOM  11212  CA  GLY D 184     -14.096  55.468  -3.417  1.00 56.16           C  
+ANISOU11212  CA  GLY D 184     6627   7170   7542    710    789    408       C  
+ATOM  11213  C   GLY D 184     -14.607  55.098  -4.797  1.00 55.07           C  
+ANISOU11213  C   GLY D 184     6550   6867   7509    655    783    522       C  
+ATOM  11214  O   GLY D 184     -14.932  53.936  -5.064  1.00 52.81           O  
+ANISOU11214  O   GLY D 184     6254   6593   7217    709    866    610       O  
+ATOM  11215  N   ASP D 185     -14.673  56.094  -5.676  1.00 54.86           N  
+ANISOU11215  N   ASP D 185     6584   6685   7577    547    687    517       N  
+ATOM  11216  CA  ASP D 185     -15.146  55.881  -7.039  1.00 51.42           C  
+ANISOU11216  CA  ASP D 185     6198   6144   7194    502    657    621       C  
+ATOM  11217  C   ASP D 185     -14.268  54.881  -7.786  1.00 49.14           C  
+ANISOU11217  C   ASP D 185     5900   5970   6800    462    713    701       C  
+ATOM  11218  O   ASP D 185     -14.767  54.047  -8.539  1.00 55.11           O  
+ANISOU11218  O   ASP D 185     6665   6713   7561    480    738    740       O  
+ATOM  11219  CB  ASP D 185     -15.194  57.205  -7.803  1.00 58.35           C  
+ANISOU11219  CB  ASP D 185     7145   6860   8166    411    552    650       C  
+ATOM  11220  CG  ASP D 185     -16.435  58.013  -7.488  1.00 54.64           C  
+ANISOU11220  CG  ASP D 185     6694   6226   7840    492    495    596       C  
+ATOM  11221  OD1 ASP D 185     -17.305  57.503  -6.753  1.00 66.22           O  
+ANISOU11221  OD1 ASP D 185     8107   7733   9322    606    541    530       O  
+ATOM  11222  OD2 ASP D 185     -16.542  59.157  -7.979  1.00 59.74           O  
+ANISOU11222  OD2 ASP D 185     7403   6699   8597    450    419    633       O  
+ATOM  11223  N   LEU D 186     -12.959  54.967  -7.574  1.00 50.20           N  
+ANISOU11223  N   LEU D 186     5999   6229   6846    409    732    701       N  
+ATOM  11224  CA  LEU D 186     -12.030  54.042  -8.210  1.00 55.38           C  
+ANISOU11224  CA  LEU D 186     6627   7013   7402    397    799    764       C  
+ATOM  11225  C   LEU D 186     -12.140  52.644  -7.615  1.00 65.94           C  
+ANISOU11225  C   LEU D 186     7925   8422   8709    539    910    775       C  
+ATOM  11226  O   LEU D 186     -11.763  51.663  -8.255  1.00 67.41           O  
+ANISOU11226  O   LEU D 186     8106   8644   8862    565    981    813       O  
+ATOM  11227  CB  LEU D 186     -10.596  54.556  -8.101  1.00 49.61           C  
+ANISOU11227  CB  LEU D 186     5833   6419   6598    304    791    760       C  
+ATOM  11228  CG  LEU D 186     -10.277  55.662  -9.107  1.00 54.89           C  
+ANISOU11228  CG  LEU D 186     6546   7004   7308    134    730    812       C  
+ATOM  11229  CD1 LEU D 186      -8.969  56.330  -8.771  1.00 62.91           C  
+ANISOU11229  CD1 LEU D 186     7470   8129   8302      9    724    778       C  
+ATOM  11230  CD2 LEU D 186     -10.235  55.093 -10.515  1.00 63.41           C  
+ANISOU11230  CD2 LEU D 186     7663   8114   8317    114    764    913       C  
+ATOM  11231  N   VAL D 187     -12.646  52.548  -6.390  1.00 49.14           N  
+ANISOU11231  N   VAL D 187     5769   6310   6594    639    940    748       N  
+ATOM  11232  CA  VAL D 187     -12.939  51.232  -5.832  1.00 46.36           C  
+ANISOU11232  CA  VAL D 187     5391   5980   6243    777   1068    809       C  
+ATOM  11233  C   VAL D 187     -14.216  50.633  -6.430  1.00 51.50           C  
+ANISOU11233  C   VAL D 187     6080   6454   7033    770   1102    811       C  
+ATOM  11234  O   VAL D 187     -14.255  49.448  -6.766  1.00 63.51           O  
+ANISOU11234  O   VAL D 187     7603   7925   8604    808   1203    848       O  
+ATOM  11235  CB  VAL D 187     -13.077  51.285  -4.295  1.00 52.85           C  
+ANISOU11235  CB  VAL D 187     6160   6923   6999    898   1108    809       C  
+ATOM  11236  CG1 VAL D 187     -13.617  49.964  -3.755  1.00 44.30           C  
+ANISOU11236  CG1 VAL D 187     5064   5817   5952   1035   1264    925       C  
+ATOM  11237  CG2 VAL D 187     -11.740  51.623  -3.652  1.00 47.10           C  
+ANISOU11237  CG2 VAL D 187     5357   6428   6111    919   1073    789       C  
+ATOM  11238  N   SER D 188     -15.248  51.458  -6.594  1.00 61.41           N  
+ANISOU11238  N   SER D 188     7355   7610   8368    722   1017    755       N  
+ATOM  11239  CA  SER D 188     -16.576  50.941  -6.931  1.00 65.42           C  
+ANISOU11239  CA  SER D 188     7853   7994   9011    723   1041    738       C  
+ATOM  11240  C   SER D 188     -16.984  51.081  -8.401  1.00 70.09           C  
+ANISOU11240  C   SER D 188     8474   8518   9639    627    942    699       C  
+ATOM  11241  O   SER D 188     -17.733  50.250  -8.916  1.00 54.21           O  
+ANISOU11241  O   SER D 188     6436   6446   7717    608    973    660       O  
+ATOM  11242  CB  SER D 188     -17.630  51.617  -6.051  1.00 60.82           C  
+ANISOU11242  CB  SER D 188     7233   7385   8491    774   1025    702       C  
+ATOM  11243  OG  SER D 188     -17.416  51.315  -4.684  1.00 68.75           O  
+ANISOU11243  OG  SER D 188     8199   8495   9430    880   1135    738       O  
+ATOM  11244  N   LYS D 189     -16.502  52.120  -9.077  1.00 71.15           N  
+ANISOU11244  N   LYS D 189     8656   8674   9703    561    826    710       N  
+ATOM  11245  CA  LYS D 189     -16.913  52.371 -10.458  1.00 55.01           C  
+ANISOU11245  CA  LYS D 189     6639   6614   7647    495    723    708       C  
+ATOM  11246  C   LYS D 189     -15.782  52.092 -11.442  1.00 50.97           C  
+ANISOU11246  C   LYS D 189     6165   6202   7000    433    735    737       C  
+ATOM  11247  O   LYS D 189     -14.618  52.354 -11.150  1.00 59.73           O  
+ANISOU11247  O   LYS D 189     7282   7378   8036    414    772    780       O  
+ATOM  11248  CB  LYS D 189     -17.383  53.819 -10.627  1.00 58.93           C  
+ANISOU11248  CB  LYS D 189     7166   7046   8177    484    592    747       C  
+ATOM  11249  CG  LYS D 189     -18.450  54.277  -9.646  1.00 49.09           C  
+ANISOU11249  CG  LYS D 189     5877   5716   7061    566    581    701       C  
+ATOM  11250  CD  LYS D 189     -18.805  55.737  -9.897  1.00 50.35           C  
+ANISOU11250  CD  LYS D 189     6078   5773   7278    577    459    740       C  
+ATOM  11251  CE  LYS D 189     -19.637  56.324  -8.768  1.00 55.09           C  
+ANISOU11251  CE  LYS D 189     6638   6294   8001    676    466    664       C  
+ATOM  11252  NZ  LYS D 189     -21.018  55.774  -8.736  1.00 75.02           N  
+ANISOU11252  NZ  LYS D 189     9060   8833  10613    750    472    622       N  
+ATOM  11253  N   THR D 190     -16.132  51.562 -12.610  1.00 46.99           N  
+ANISOU11253  N   THR D 190     5663   5738   6453    402    704    693       N  
+ATOM  11254  CA  THR D 190     -15.153  51.321 -13.665  1.00 48.23           C  
+ANISOU11254  CA  THR D 190     5849   6024   6453    355    721    704       C  
+ATOM  11255  C   THR D 190     -14.901  52.594 -14.464  1.00 53.99           C  
+ANISOU11255  C   THR D 190     6627   6813   7074    293    616    828       C  
+ATOM  11256  O   THR D 190     -15.814  53.145 -15.081  1.00 49.69           O  
+ANISOU11256  O   THR D 190     6095   6260   6525    296    499    861       O  
+ATOM  11257  CB  THR D 190     -15.603  50.202 -14.618  1.00 53.81           C  
+ANISOU11257  CB  THR D 190     6537   6776   7134    351    735    566       C  
+ATOM  11258  OG1 THR D 190     -15.670  48.963 -13.902  1.00 61.04           O  
+ANISOU11258  OG1 THR D 190     7418   7588   8185    398    868    475       O  
+ATOM  11259  CG2 THR D 190     -14.625  50.058 -15.774  1.00 52.22           C  
+ANISOU11259  CG2 THR D 190     6361   6748   6731    317    754    561       C  
+ATOM  11260  N   PHE D 191     -13.654  53.050 -14.449  1.00 53.69           N  
+ANISOU11260  N   PHE D 191     6602   6841   6958    241    663    913       N  
+ATOM  11261  CA  PHE D 191     -13.279  54.307 -15.085  1.00 54.20           C  
+ANISOU11261  CA  PHE D 191     6713   6924   6959    160    601   1069       C  
+ATOM  11262  C   PHE D 191     -12.750  54.139 -16.503  1.00 56.14           C  
+ANISOU11262  C   PHE D 191     6973   7363   6995    117    616   1133       C  
+ATOM  11263  O   PHE D 191     -12.092  53.149 -16.823  1.00 53.26           O  
+ANISOU11263  O   PHE D 191     6572   7136   6527    131    710   1043       O  
+ATOM  11264  CB  PHE D 191     -12.223  55.023 -14.241  1.00 55.04           C  
+ANISOU11264  CB  PHE D 191     6800   6992   7121     92    647   1118       C  
+ATOM  11265  CG  PHE D 191     -12.793  55.873 -13.146  1.00 53.14           C  
+ANISOU11265  CG  PHE D 191     6572   6564   7053    108    590   1095       C  
+ATOM  11266  CD1 PHE D 191     -13.387  55.298 -12.035  1.00 51.27           C  
+ANISOU11266  CD1 PHE D 191     6300   6281   6901    206    609    973       C  
+ATOM  11267  CD2 PHE D 191     -12.716  57.254 -13.220  1.00 47.99           C  
+ANISOU11267  CD2 PHE D 191     5968   5779   6487     29    532   1196       C  
+ATOM  11268  CE1 PHE D 191     -13.906  56.086 -11.025  1.00 55.61           C  
+ANISOU11268  CE1 PHE D 191     6853   6695   7582    235    567    926       C  
+ATOM  11269  CE2 PHE D 191     -13.231  58.046 -12.215  1.00 54.45           C  
+ANISOU11269  CE2 PHE D 191     6799   6414   7475     55    486   1132       C  
+ATOM  11270  CZ  PHE D 191     -13.827  57.463 -11.116  1.00 48.75           C  
+ANISOU11270  CZ  PHE D 191     6033   5689   6801    163    501    983       C  
+ATOM  11271  N   LEU D 192     -13.054  55.116 -17.351  1.00 49.93           N  
+ANISOU11271  N   LEU D 192     6240   6591   6142     83    532   1297       N  
+ATOM  11272  CA  LEU D 192     -12.368  55.262 -18.625  1.00 50.84           C  
+ANISOU11272  CA  LEU D 192     6371   6918   6029     30    565   1423       C  
+ATOM  11273  C   LEU D 192     -11.537  56.538 -18.596  1.00 50.20           C  
+ANISOU11273  C   LEU D 192     6319   6766   5990    -85    600   1649       C  
+ATOM  11274  O   LEU D 192     -12.078  57.644 -18.582  1.00 53.96           O  
+ANISOU11274  O   LEU D 192     6856   7070   6575    -95    521   1805       O  
+ATOM  11275  CB  LEU D 192     -13.360  55.298 -19.789  1.00 55.23           C  
+ANISOU11275  CB  LEU D 192     6957   7603   6426     92    448   1468       C  
+ATOM  11276  CG  LEU D 192     -12.786  55.734 -21.141  1.00 60.41           C  
+ANISOU11276  CG  LEU D 192     7643   8501   6809     54    470   1667       C  
+ATOM  11277  CD1 LEU D 192     -11.645  54.819 -21.567  1.00 57.24           C  
+ANISOU11277  CD1 LEU D 192     7191   8329   6228     19    618   1554       C  
+ATOM  11278  CD2 LEU D 192     -13.872  55.778 -22.208  1.00 56.83           C  
+ANISOU11278  CD2 LEU D 192     7204   8217   6170    145    324   1706       C  
+ATOM  11279  N   PHE D 193     -10.220  56.378 -18.583  1.00 49.89           N  
+ANISOU11279  N   PHE D 193     6222   6844   5889   -173    727   1660       N  
+ATOM  11280  CA  PHE D 193      -9.319  57.517 -18.663  1.00 50.35           C  
+ANISOU11280  CA  PHE D 193     6279   6857   5995   -325    784   1864       C  
+ATOM  11281  C   PHE D 193      -9.095  57.862 -20.129  1.00 51.18           C  
+ANISOU11281  C   PHE D 193     6419   7158   5868   -362    820   2094       C  
+ATOM  11282  O   PHE D 193      -8.725  57.001 -20.925  1.00 51.71           O  
+ANISOU11282  O   PHE D 193     6447   7508   5693   -322    887   2036       O  
+ATOM  11283  CB  PHE D 193      -7.990  57.212 -17.968  1.00 57.08           C  
+ANISOU11283  CB  PHE D 193     7013   7790   6886   -409    901   1771       C  
+ATOM  11284  CG  PHE D 193      -8.097  57.078 -16.473  1.00 52.28           C  
+ANISOU11284  CG  PHE D 193     6364   7024   6476   -376    864   1590       C  
+ATOM  11285  CD1 PHE D 193      -8.638  55.938 -15.900  1.00 48.70           C  
+ANISOU11285  CD1 PHE D 193     5897   6586   6020   -224    850   1403       C  
+ATOM  11286  CD2 PHE D 193      -7.642  58.087 -15.640  1.00 50.28           C  
+ANISOU11286  CD2 PHE D 193     6080   6615   6407   -501    853   1603       C  
+ATOM  11287  CE1 PHE D 193      -8.732  55.811 -14.526  1.00 58.37           C  
+ANISOU11287  CE1 PHE D 193     7082   7708   7387   -177    830   1272       C  
+ATOM  11288  CE2 PHE D 193      -7.732  57.964 -14.265  1.00 52.43           C  
+ANISOU11288  CE2 PHE D 193     6307   6803   6810   -456    815   1421       C  
+ATOM  11289  CZ  PHE D 193      -8.278  56.825 -13.708  1.00 57.76           C  
+ANISOU11289  CZ  PHE D 193     6973   7530   7444   -284    806   1275       C  
+ATOM  11290  N   VAL D 194      -9.328  59.118 -20.491  1.00 51.59           N  
+ANISOU11290  N   VAL D 194     6549   7061   5991   -425    786   2361       N  
+ATOM  11291  CA  VAL D 194      -9.157  59.540 -21.875  1.00 56.61           C  
+ANISOU11291  CA  VAL D 194     7227   7894   6389   -447    829   2644       C  
+ATOM  11292  C   VAL D 194      -8.750  61.011 -21.943  1.00 59.21           C  
+ANISOU11292  C   VAL D 194     7608   7995   6892   -597    882   2967       C  
+ATOM  11293  O   VAL D 194      -9.208  61.833 -21.148  1.00 56.39           O  
+ANISOU11293  O   VAL D 194     7307   7285   6835   -616    813   2980       O  
+ATOM  11294  CB  VAL D 194     -10.450  59.297 -22.698  1.00 58.88           C  
+ANISOU11294  CB  VAL D 194     7582   8300   6490   -269    684   2674       C  
+ATOM  11295  CG1 VAL D 194     -11.611  60.113 -22.147  1.00 53.62           C  
+ANISOU11295  CG1 VAL D 194     6992   7310   6072   -192    536   2739       C  
+ATOM  11296  CG2 VAL D 194     -10.223  59.599 -24.173  1.00 74.88           C  
+ANISOU11296  CG2 VAL D 194     9639  10624   8188   -263    729   2961       C  
+ATOM  11297  N   GLY D 195      -7.867  61.334 -22.883  1.00 54.55           N  
+ANISOU11297  N   GLY D 195     6996   7600   6129   -708   1022   3219       N  
+ATOM  11298  CA  GLY D 195      -7.373  62.690 -23.022  1.00 58.89           C  
+ANISOU11298  CA  GLY D 195     7589   7918   6867   -879   1106   3534       C  
+ATOM  11299  C   GLY D 195      -6.090  62.912 -22.247  1.00 69.75           C  
+ANISOU11299  C   GLY D 195     8841   9207   8455  -1110   1236   3427       C  
+ATOM  11300  O   GLY D 195      -5.656  64.048 -22.061  1.00 70.26           O  
+ANISOU11300  O   GLY D 195     8932   8991   8773  -1278   1286   3541       O  
+ATOM  11301  N   PHE D 196      -5.479  61.820 -21.797  1.00 70.37           N  
+ANISOU11301  N   PHE D 196     8780   9523   8434  -1102   1279   3154       N  
+ATOM  11302  CA  PHE D 196      -4.212  61.893 -21.079  1.00 57.36           C  
+ANISOU11302  CA  PHE D 196     6967   7886   6939  -1298   1390   3038       C  
+ATOM  11303  C   PHE D 196      -3.078  61.309 -21.916  1.00 63.35           C  
+ANISOU11303  C   PHE D 196     7599   9037   7434  -1336   1548   3044       C  
+ATOM  11304  O   PHE D 196      -3.191  60.204 -22.446  1.00 84.88           O  
+ANISOU11304  O   PHE D 196    10307  12069   9875  -1169   1558   2935       O  
+ATOM  11305  CB  PHE D 196      -4.305  61.155 -19.739  1.00 58.88           C  
+ANISOU11305  CB  PHE D 196     7090   8025   7256  -1215   1295   2656       C  
+ATOM  11306  CG  PHE D 196      -5.254  61.786 -18.755  1.00 70.03           C  
+ANISOU11306  CG  PHE D 196     8607   9054   8949  -1180   1147   2559       C  
+ATOM  11307  CD1 PHE D 196      -4.876  62.899 -18.022  1.00 73.91           C  
+ANISOU11307  CD1 PHE D 196     9077   9254   9753  -1373   1153   2560       C  
+ATOM  11308  CD2 PHE D 196      -6.521  61.259 -18.556  1.00 58.74           C  
+ANISOU11308  CD2 PHE D 196     7279   7560   7478   -959   1012   2440       C  
+ATOM  11309  CE1 PHE D 196      -5.744  63.480 -17.114  1.00 62.35           C  
+ANISOU11309  CE1 PHE D 196     7705   7447   8536  -1323   1028   2436       C  
+ATOM  11310  CE2 PHE D 196      -7.394  61.836 -17.649  1.00 65.74           C  
+ANISOU11310  CE2 PHE D 196     8244   8123   8612   -911    894   2344       C  
+ATOM  11311  CZ  PHE D 196      -7.005  62.947 -16.927  1.00 60.92           C  
+ANISOU11311  CZ  PHE D 196     7624   7231   8293  -1081    903   2337       C  
+ATOM  11312  N   SER D 197      -1.985  62.057 -22.026  1.00 69.46           N  
+ANISOU11312  N   SER D 197     8287   9779   8324  -1547   1667   3123       N  
+ATOM  11313  CA  SER D 197      -0.783  61.575 -22.698  1.00 75.39           C  
+ANISOU11313  CA  SER D 197     8895  10875   8876  -1584   1820   3085       C  
+ATOM  11314  C   SER D 197       0.342  61.444 -21.677  1.00 72.91           C  
+ANISOU11314  C   SER D 197     8351  10608   8744  -1733   1879   2891       C  
+ATOM  11315  O   SER D 197       0.164  61.801 -20.513  1.00 67.44           O  
+ANISOU11315  O   SER D 197     7618   9690   8315  -1825   1799   2800       O  
+ATOM  11316  CB  SER D 197      -0.382  62.514 -23.837  1.00 80.09           C  
+ANISOU11316  CB  SER D 197     9556  11459   9417  -1697   1934   3363       C  
+ATOM  11317  OG  SER D 197      -0.108  63.816 -23.351  1.00110.33           O  
+ANISOU11317  OG  SER D 197    13399  14932  13591  -1936   1965   3486       O  
+ATOM  11318  N   PHE D 198       1.495  60.932 -22.099  1.00 66.02           N  
+ANISOU11318  N   PHE D 198     7311  10046   7728  -1747   2009   2818       N  
+ATOM  11319  CA  PHE D 198       2.569  60.661 -21.146  1.00 69.08           C  
+ANISOU11319  CA  PHE D 198     7446  10548   8251  -1841   2046   2615       C  
+ATOM  11320  C   PHE D 198       3.248  61.933 -20.641  1.00 73.69           C  
+ANISOU11320  C   PHE D 198     7928  10917   9155  -2159   2091   2681       C  
+ATOM  11321  O   PHE D 198       4.030  61.885 -19.692  1.00 75.47           O  
+ANISOU11321  O   PHE D 198     7928  11215   9533  -2269   2084   2499       O  
+ATOM  11322  CB  PHE D 198       3.613  59.707 -21.747  1.00 75.77           C  
+ANISOU11322  CB  PHE D 198     8132  11785   8870  -1731   2167   2507       C  
+ATOM  11323  CG  PHE D 198       4.357  60.252 -22.936  1.00 70.89           C  
+ANISOU11323  CG  PHE D 198     7497  11280   8157  -1848   2330   2698       C  
+ATOM  11324  CD1 PHE D 198       5.462  61.072 -22.764  1.00 68.14           C  
+ANISOU11324  CD1 PHE D 198     6972  10911   8006  -2107   2443   2752       C  
+ATOM  11325  CD2 PHE D 198       3.979  59.909 -24.223  1.00 64.77           C  
+ANISOU11325  CD2 PHE D 198     6862  10661   7088  -1703   2377   2810       C  
+ATOM  11326  CE1 PHE D 198       6.158  61.560 -23.851  1.00 69.88           C  
+ANISOU11326  CE1 PHE D 198     7170  11239   8142  -2217   2618   2944       C  
+ATOM  11327  CE2 PHE D 198       4.673  60.395 -25.316  1.00 69.58           C  
+ANISOU11327  CE2 PHE D 198     7447  11405   7584  -1800   2538   2999       C  
+ATOM  11328  CZ  PHE D 198       5.763  61.222 -25.128  1.00 70.12           C  
+ANISOU11328  CZ  PHE D 198     7351  11430   7860  -2057   2668   3079       C  
+ATOM  11329  N   THR D 199       2.951  63.065 -21.270  1.00 81.44           N  
+ANISOU11329  N   THR D 199     9067  11635  10240  -2301   2135   2928       N  
+ATOM  11330  CA  THR D 199       3.529  64.333 -20.844  1.00 78.90           C  
+ANISOU11330  CA  THR D 199     8676  11040  10264  -2620   2194   2979       C  
+ATOM  11331  C   THR D 199       2.626  65.057 -19.852  1.00 68.52           C  
+ANISOU11331  C   THR D 199     7477   9304   9254  -2696   2045   2933       C  
+ATOM  11332  O   THR D 199       2.935  66.170 -19.423  1.00 79.40           O  
+ANISOU11332  O   THR D 199     8830  10377  10960  -2961   2071   2934       O  
+ATOM  11333  CB  THR D 199       3.796  65.267 -22.042  1.00 73.15           C  
+ANISOU11333  CB  THR D 199     8059  10211   9525  -2750   2352   3280       C  
+ATOM  11334  OG1 THR D 199       2.630  65.333 -22.873  1.00 76.33           O  
+ANISOU11334  OG1 THR D 199     8735  10518   9747  -2554   2289   3496       O  
+ATOM  11335  CG2 THR D 199       4.973  64.763 -22.861  1.00 73.67           C  
+ANISOU11335  CG2 THR D 199     7948  10672   9373  -2756   2529   3298       C  
+ATOM  11336  N   ASP D 200       1.511  64.426 -19.493  1.00 74.51           N  
+ANISOU11336  N   ASP D 200     8359  10032   9919  -2464   1894   2875       N  
+ATOM  11337  CA  ASP D 200       0.559  65.032 -18.567  1.00 92.41           C  
+ANISOU11337  CA  ASP D 200    10741  11903  12469  -2490   1749   2825       C  
+ATOM  11338  C   ASP D 200       1.172  65.187 -17.177  1.00 92.11           C  
+ANISOU11338  C   ASP D 200    10476  11830  12691  -2680   1692   2540       C  
+ATOM  11339  O   ASP D 200       1.698  64.229 -16.611  1.00 94.95           O  
+ANISOU11339  O   ASP D 200    10658  12523  12895  -2577   1656   2291       O  
+ATOM  11340  CB  ASP D 200      -0.727  64.208 -18.494  1.00 95.71           C  
+ANISOU11340  CB  ASP D 200    11310  12339  12715  -2186   1614   2804       C  
+ATOM  11341  CG  ASP D 200      -1.841  64.935 -17.769  1.00 99.56           C  
+ANISOU11341  CG  ASP D 200    11982  12378  13467  -2132   1459   2725       C  
+ATOM  11342  OD1 ASP D 200      -1.830  64.954 -16.520  1.00 91.46           O  
+ANISOU11342  OD1 ASP D 200    10893  11248  12610  -2143   1356   2406       O  
+ATOM  11343  OD2 ASP D 200      -2.725  65.495 -18.450  1.00107.29           O  
+ANISOU11343  OD2 ASP D 200    13162  13133  14471  -2060   1442   2983       O  
+ATOM  11344  N   PRO D 201       1.099  66.405 -16.626  1.00 94.73           N  
+ANISOU11344  N   PRO D 201    10846  11745  13402  -2904   1661   2503       N  
+ATOM  11345  CA  PRO D 201       1.758  66.794 -15.372  1.00 96.68           C  
+ANISOU11345  CA  PRO D 201    10898  11935  13900  -3102   1590   2146       C  
+ATOM  11346  C   PRO D 201       1.079  66.361 -14.065  1.00 95.51           C  
+ANISOU11346  C   PRO D 201    10790  11760  13742  -2885   1382   1762       C  
+ATOM  11347  O   PRO D 201       1.710  66.470 -13.015  1.00 97.08           O  
+ANISOU11347  O   PRO D 201    10790  12046  14049  -3007   1311   1439       O  
+ATOM  11348  CB  PRO D 201       1.779  68.322 -15.464  1.00 99.03           C  
+ANISOU11348  CB  PRO D 201    11283  11733  14611  -3404   1652   2258       C  
+ATOM  11349  CG  PRO D 201       0.600  68.663 -16.302  1.00 96.57           C  
+ANISOU11349  CG  PRO D 201    11314  11137  14241  -3195   1645   2544       C  
+ATOM  11350  CD  PRO D 201       0.477  67.556 -17.307  1.00 94.25           C  
+ANISOU11350  CD  PRO D 201    11051  11255  13505  -2945   1695   2744       C  
+ATOM  11351  N   ASN D 202      -0.164  65.895 -14.111  1.00 86.72           N  
+ANISOU11351  N   ASN D 202     9904  10554  12493  -2579   1287   1792       N  
+ATOM  11352  CA  ASN D 202      -0.909  65.682 -12.874  1.00 81.46           C  
+ANISOU11352  CA  ASN D 202     9290   9803  11858  -2398   1116   1466       C  
+ATOM  11353  C   ASN D 202      -1.463  64.272 -12.665  1.00 80.70           C  
+ANISOU11353  C   ASN D 202     9222  10002  11439  -2054   1048   1385       C  
+ATOM  11354  O   ASN D 202      -1.787  63.895 -11.538  1.00 90.34           O  
+ANISOU11354  O   ASN D 202    10416  11275  12633  -1914    934   1113       O  
+ATOM  11355  CB  ASN D 202      -2.074  66.676 -12.815  1.00 86.09           C  
+ANISOU11355  CB  ASN D 202    10124   9888  12700  -2370   1055   1518       C  
+ATOM  11356  CG  ASN D 202      -1.625  68.126 -12.931  1.00109.97           C  
+ANISOU11356  CG  ASN D 202    13149  12518  16115  -2703   1129   1586       C  
+ATOM  11357  OD1 ASN D 202      -2.041  68.839 -13.845  1.00116.28           O  
+ANISOU11357  OD1 ASN D 202    14119  13014  17049  -2745   1208   1920       O  
+ATOM  11358  ND2 ASN D 202      -0.803  68.577 -11.988  1.00115.06           N  
+ANISOU11358  ND2 ASN D 202    13604  13160  16954  -2937   1102   1268       N  
+ATOM  11359  N   LEU D 203      -1.580  63.500 -13.741  1.00 75.22           N  
+ANISOU11359  N   LEU D 203     9523   8199  10858   -973    540   1195       N  
+ATOM  11360  CA  LEU D 203      -2.250  62.201 -13.669  1.00 72.25           C  
+ANISOU11360  CA  LEU D 203     9257   8007  10189   -758    522   1168       C  
+ATOM  11361  C   LEU D 203      -1.575  61.235 -12.692  1.00 90.34           C  
+ANISOU11361  C   LEU D 203    11436  10604  12285   -687    527    985       C  
+ATOM  11362  O   LEU D 203      -2.248  60.611 -11.869  1.00 94.89           O  
+ANISOU11362  O   LEU D 203    12045  11247  12763   -551    478    840       O  
+ATOM  11363  CB  LEU D 203      -2.335  61.569 -15.064  1.00 70.48           C  
+ANISOU11363  CB  LEU D 203     9133   7876   9768   -684    591   1439       C  
+ATOM  11364  CG  LEU D 203      -3.053  60.221 -15.153  1.00 62.66           C  
+ANISOU11364  CG  LEU D 203     8244   7036   8530   -474    586   1401       C  
+ATOM  11365  CD1 LEU D 203      -4.504  60.350 -14.718  1.00 61.85           C  
+ANISOU11365  CD1 LEU D 203     8260   6735   8505   -376    497   1298       C  
+ATOM  11366  CD2 LEU D 203      -2.976  59.658 -16.562  1.00 66.95           C  
+ANISOU11366  CD2 LEU D 203     8837   7717   8885   -421    658   1611       C  
+ATOM  11367  N   ASP D 204      -0.250  61.136 -12.766  1.00 88.35           N  
+ANISOU11367  N   ASP D 204    11037  10548  11983   -777    590   1010       N  
+ATOM  11368  CA  ASP D 204       0.504  60.207 -11.923  1.00 87.72           C  
+ANISOU11368  CA  ASP D 204    10828  10786  11714   -695    596    880       C  
+ATOM  11369  C   ASP D 204       0.442  60.566 -10.438  1.00 84.14           C  
+ANISOU11369  C   ASP D 204    10255  10394  11320   -708    510    598       C  
+ATOM  11370  O   ASP D 204       0.373  59.685  -9.580  1.00 73.90           O  
+ANISOU11370  O   ASP D 204     8916   9325   9838   -560    486    510       O  
+ATOM  11371  CB  ASP D 204       1.964  60.145 -12.376  1.00 92.25           C  
+ANISOU11371  CB  ASP D 204    11249  11559  12242   -798    678    960       C  
+ATOM  11372  CG  ASP D 204       2.769  59.106 -11.614  1.00 98.49           C  
+ANISOU11372  CG  ASP D 204    11899  12693  12831   -682    685    866       C  
+ATOM  11373  OD1 ASP D 204       2.489  57.899 -11.774  1.00 99.75           O  
+ANISOU11373  OD1 ASP D 204    12129  12962  12811   -492    712    940       O  
+ATOM  11374  OD2 ASP D 204       3.683  59.498 -10.859  1.00107.27           O  
+ANISOU11374  OD2 ASP D 204    12813  13962  13981   -778    664    715       O  
+ATOM  11375  N   TYR D 205       0.471  61.862 -10.147  1.00 80.74           N  
+ANISOU11375  N   TYR D 205     9751   9770  11156   -882    470    458       N  
+ATOM  11376  CA  TYR D 205       0.350  62.357  -8.779  1.00 86.94           C  
+ANISOU11376  CA  TYR D 205    10398  10618  12017   -911    384    131       C  
+ATOM  11377  C   TYR D 205      -0.998  61.973  -8.179  1.00 84.59           C  
+ANISOU11377  C   TYR D 205    10222  10283  11636   -745    320     46       C  
+ATOM  11378  O   TYR D 205      -1.074  61.351  -7.108  1.00 81.26           O  
+ANISOU11378  O   TYR D 205     9718  10138  11018   -629    283    -99       O  
+ATOM  11379  CB  TYR D 205       0.528  63.878  -8.765  1.00 81.01           C  
+ANISOU11379  CB  TYR D 205     9549   9583  11647  -1138    366    -14       C  
+ATOM  11380  CG  TYR D 205       0.198  64.550  -7.451  1.00 93.00           C  
+ANISOU11380  CG  TYR D 205    10924  11116  13297  -1176    273   -409       C  
+ATOM  11381  CD1 TYR D 205       1.053  64.452  -6.362  1.00104.72           C  
+ANISOU11381  CD1 TYR D 205    12163  12962  14666  -1204    237   -686       C  
+ATOM  11382  CD2 TYR D 205      -0.967  65.293  -7.305  1.00 90.95           C  
+ANISOU11382  CD2 TYR D 205    10751  10537  13269  -1176    217   -523       C  
+ATOM  11383  CE1 TYR D 205       0.756  65.072  -5.162  1.00106.84           C  
+ANISOU11383  CE1 TYR D 205    12268  13301  15024  -1236    151  -1086       C  
+ATOM  11384  CE2 TYR D 205      -1.274  65.915  -6.108  1.00 94.21           C  
+ANISOU11384  CE2 TYR D 205    11008  10985  13802  -1208    136   -928       C  
+ATOM  11385  CZ  TYR D 205      -0.409  65.801  -5.041  1.00107.49           C  
+ANISOU11385  CZ  TYR D 205    12440  13057  15344  -1241    104  -1218       C  
+ATOM  11386  OH  TYR D 205      -0.708  66.418  -3.848  1.00121.53           O  
+ANISOU11386  OH  TYR D 205    14035  14930  17212  -1270     22  -1658       O  
+ATOM  11387  N   ILE D 206      -2.058  62.337  -8.894  1.00 72.90           N  
+ANISOU11387  N   ILE D 206     8925   8478  10294   -731    313    160       N  
+ATOM  11388  CA  ILE D 206      -3.420  62.040  -8.479  1.00 77.22           C  
+ANISOU11388  CA  ILE D 206     9594   8953  10792   -586    260     91       C  
+ATOM  11389  C   ILE D 206      -3.611  60.543  -8.266  1.00 73.39           C  
+ANISOU11389  C   ILE D 206     9162   8731   9993   -388    291    188       C  
+ATOM  11390  O   ILE D 206      -4.116  60.122  -7.226  1.00 72.52           O  
+ANISOU11390  O   ILE D 206     9011   8779   9764   -284    255     46       O  
+ATOM  11391  CB  ILE D 206      -4.442  62.547  -9.513  1.00 73.23           C  
+ANISOU11391  CB  ILE D 206     9277   8086  10463   -584    253    253       C  
+ATOM  11392  CG1 ILE D 206      -4.371  64.071  -9.629  1.00 71.35           C  
+ANISOU11392  CG1 ILE D 206     8977   7529  10602   -764    224    175       C  
+ATOM  11393  CG2 ILE D 206      -5.846  62.109  -9.136  1.00 69.19           C  
+ANISOU11393  CG2 ILE D 206     8882   7528   9880   -425    205    183       C  
+ATOM  11394  CD1 ILE D 206      -5.229  64.640 -10.738  1.00 73.89           C  
+ANISOU11394  CD1 ILE D 206     9461   7506  11108   -759    221    403       C  
+ATOM  11395  N   LEU D 207      -3.171  59.745  -9.238  1.00 71.41           N  
+ANISOU11395  N   LEU D 207     8979   8534   9620   -340    367    426       N  
+ATOM  11396  CA  LEU D 207      -3.286  58.291  -9.145  1.00 66.84           C  
+ANISOU11396  CA  LEU D 207     8436   8151   8811   -156    413    524       C  
+ATOM  11397  C   LEU D 207      -2.523  57.742  -7.947  1.00 71.50           C  
+ANISOU11397  C   LEU D 207     8845   9077   9245    -97    408    429       C  
+ATOM  11398  O   LEU D 207      -2.986  56.820  -7.275  1.00 71.08           O  
+ANISOU11398  O   LEU D 207     8793   9162   9052     60    415    445       O  
+ATOM  11399  CB  LEU D 207      -2.779  57.626 -10.425  1.00 68.05           C  
+ANISOU11399  CB  LEU D 207     8647   8315   8892   -131    498    743       C  
+ATOM  11400  CG  LEU D 207      -3.661  57.747 -11.666  1.00 70.15           C  
+ANISOU11400  CG  LEU D 207     9089   8353   9213   -121    510    874       C  
+ATOM  11401  CD1 LEU D 207      -3.024  57.022 -12.842  1.00 72.91           C  
+ANISOU11401  CD1 LEU D 207     9447   8809   9446    -91    600   1041       C  
+ATOM  11402  CD2 LEU D 207      -5.057  57.213 -11.385  1.00 57.84           C  
+ANISOU11402  CD2 LEU D 207     7647   6696   7633     19    479    823       C  
+ATOM  11403  N   SER D 208      -1.350  58.310  -7.686  1.00 79.03           N  
+ANISOU11403  N   SER D 208     9630  10174  10226   -222    399    346       N  
+ATOM  11404  CA  SER D 208      -0.552  57.906  -6.537  1.00 77.69           C  
+ANISOU11404  CA  SER D 208     9253  10373   9891   -168    379    244       C  
+ATOM  11405  C   SER D 208      -1.250  58.283  -5.237  1.00 86.22           C  
+ANISOU11405  C   SER D 208    10259  11561  10939   -140    298     13       C  
+ATOM  11406  O   SER D 208      -0.985  57.697  -4.187  1.00 93.65           O  
+ANISOU11406  O   SER D 208    11057  12851  11676    -29    280    -28       O  
+ATOM  11407  CB  SER D 208       0.839  58.542  -6.590  1.00 71.49           C  
+ANISOU11407  CB  SER D 208     8281   9720   9162   -328    381    165       C  
+ATOM  11408  OG  SER D 208       0.779  59.927  -6.298  1.00 74.41           O  
+ANISOU11408  OG  SER D 208     8578   9942   9752   -517    323    -70       O  
+ATOM  11409  N   ARG D 209      -2.148  59.262  -5.311  1.00 82.29           N  
+ANISOU11409  N   ARG D 209     9846  10785  10638   -231    251   -130       N  
+ATOM  11410  CA  ARG D 209      -2.878  59.700  -4.126  1.00 78.00           C  
+ANISOU11410  CA  ARG D 209     9220  10338  10078   -211    177   -392       C  
+ATOM  11411  C   ARG D 209      -4.232  59.009  -3.928  1.00 78.48           C  
+ANISOU11411  C   ARG D 209     9429  10343  10048    -49    185   -314       C  
+ATOM  11412  O   ARG D 209      -4.779  59.029  -2.826  1.00 86.23           O  
+ANISOU11412  O   ARG D 209    10319  11520  10923     12    144   -485       O  
+ATOM  11413  CB  ARG D 209      -3.087  61.216  -4.176  1.00 79.64           C  
+ANISOU11413  CB  ARG D 209     9394  10270  10597   -398    119   -645       C  
+ATOM  11414  N   VAL D 210      -4.773  58.395  -4.977  1.00 74.52           N  
+ANISOU11414  N   VAL D 210     9131   9605   9578     17    242    -73       N  
+ATOM  11415  CA  VAL D 210      -6.109  57.805  -4.876  1.00 73.30           C  
+ANISOU11415  CA  VAL D 210     9108   9358   9383    148    253    -21       C  
+ATOM  11416  C   VAL D 210      -6.157  56.294  -5.115  1.00 76.38           C  
+ANISOU11416  C   VAL D 210     9560   9841   9621    312    341    233       C  
+ATOM  11417  O   VAL D 210      -7.216  55.678  -4.992  1.00 68.68           O  
+ANISOU11417  O   VAL D 210     8672   8801   8623    419    367    284       O  
+ATOM  11418  CB  VAL D 210      -7.084  58.477  -5.857  1.00 71.53           C  
+ANISOU11418  CB  VAL D 210     9066   8735   9378     93    231    -16       C  
+ATOM  11419  CG1 VAL D 210      -7.283  59.941  -5.487  1.00 74.92           C  
+ANISOU11419  CG1 VAL D 210     9429   9017  10019    -42    149   -277       C  
+ATOM  11420  CG2 VAL D 210      -6.581  58.336  -7.280  1.00 68.25           C  
+ANISOU11420  CG2 VAL D 210     8756   8153   9021     52    281    202       C  
+ATOM  11421  N   ARG D 211      -5.020  55.698  -5.455  1.00 72.15           N  
+ANISOU11421  N   ARG D 211     8964   9440   9011    331    392    378       N  
+ATOM  11422  CA  ARG D 211      -4.963  54.254  -5.664  1.00 62.37           C  
+ANISOU11422  CA  ARG D 211     7752   8264   7680    491    481    601       C  
+ATOM  11423  C   ARG D 211      -3.758  53.620  -4.985  1.00 66.38           C  
+ANISOU11423  C   ARG D 211     8074   9114   8035    565    507    686       C  
+ATOM  11424  O   ARG D 211      -2.705  54.241  -4.846  1.00 73.55           O  
+ANISOU11424  O   ARG D 211     8853  10178   8916    468    468    599       O  
+ATOM  11425  CB  ARG D 211      -4.945  53.912  -7.156  1.00 59.69           C  
+ANISOU11425  CB  ARG D 211     7554   7686   7441    480    539    725       C  
+ATOM  11426  CG  ARG D 211      -6.311  53.918  -7.820  1.00 62.36           C  
+ANISOU11426  CG  ARG D 211     8069   7743   7882    497    538    716       C  
+ATOM  11427  CD  ARG D 211      -6.415  52.781  -8.830  1.00 66.98           C  
+ANISOU11427  CD  ARG D 211     8729   8236   8485    592    627    852       C  
+ATOM  11428  NE  ARG D 211      -7.539  51.893  -8.544  1.00 75.62           N  
+ANISOU11428  NE  ARG D 211     9876   9246   9609    715    669    874       N  
+ATOM  11429  CZ  ARG D 211      -7.770  50.749  -9.179  1.00 83.28           C  
+ANISOU11429  CZ  ARG D 211    10878  10131  10633    813    756    951       C  
+ATOM  11430  NH1 ARG D 211      -6.953  50.343 -10.141  1.00 74.14           N  
+ANISOU11430  NH1 ARG D 211     9703   8986   9480    816    806   1000       N  
+ATOM  11431  NH2 ARG D 211      -8.821  50.008  -8.852  1.00 80.32           N  
+ANISOU11431  NH2 ARG D 211    10534   9660  10323    904    800    960       N  
+ATOM  11432  N   SER D 212      -3.929  52.371  -4.566  1.00 72.66           N  
+ANISOU11432  N   SER D 212     8842  10016   8749    742    575    867       N  
+ATOM  11433  CA  SER D 212      -2.852  51.613  -3.952  1.00 66.79           C  
+ANISOU11433  CA  SER D 212     7919   9588   7869    855    605   1008       C  
+ATOM  11434  C   SER D 212      -2.227  50.667  -4.964  1.00 71.15           C  
+ANISOU11434  C   SER D 212     8503  10021   8508    926    694   1180       C  
+ATOM  11435  O   SER D 212      -2.924  50.066  -5.783  1.00 82.96           O  
+ANISOU11435  O   SER D 212    10143  11244  10134    969    761   1246       O  
+ATOM  11436  CB  SER D 212      -3.363  50.826  -2.745  1.00 62.92           C  
+ANISOU11436  CB  SER D 212     7342   9318   7248   1022    631   1141       C  
+ATOM  11437  OG  SER D 212      -2.303  50.144  -2.100  1.00 74.55           O  
+ANISOU11437  OG  SER D 212     8620  11127   8579   1149    650   1307       O  
+ATOM  11438  N   ALA D 213      -0.908  50.542  -4.908  1.00 69.63           N  
+ANISOU11438  N   ALA D 213     8156  10053   8245    940    695   1222       N  
+ATOM  11439  CA  ALA D 213      -0.194  49.673  -5.828  1.00 71.04           C  
+ANISOU11439  CA  ALA D 213     8330  10157   8504   1012    781   1353       C  
+ATOM  11440  C   ALA D 213      -0.067  48.278  -5.236  1.00 81.89           C  
+ANISOU11440  C   ALA D 213     9606  11636   9872   1244    856   1587       C  
+ATOM  11441  O   ALA D 213       0.377  47.348  -5.911  1.00 81.74           O  
+ANISOU11441  O   ALA D 213     9571  11520   9965   1343    941   1696       O  
+ATOM  11442  CB  ALA D 213       1.175  50.244  -6.147  1.00 62.39           C  
+ANISOU11442  CB  ALA D 213     7106   9237   7362    907    754   1280       C  
+ATOM  11443  N   TYR D 214      -0.465  48.130  -3.975  1.00 83.68           N  
+ANISOU11443  N   TYR D 214     9752  12065   9979   1335    830   1668       N  
+ATOM  11444  CA  TYR D 214      -0.344  46.840  -3.314  1.00 81.05           C  
+ANISOU11444  CA  TYR D 214     9306  11844   9646   1564    907   1951       C  
+ATOM  11445  C   TYR D 214      -1.631  46.026  -3.371  1.00 71.75           C  
+ANISOU11445  C   TYR D 214     8256  10376   8630   1650    998   2078       C  
+ATOM  11446  O   TYR D 214      -1.638  44.848  -3.014  1.00 83.16           O  
+ANISOU11446  O   TYR D 214     9626  11806  10165   1836   1091   2341       O  
+ATOM  11447  CB  TYR D 214       0.053  47.037  -1.848  1.00 77.87           C  
+ANISOU11447  CB  TYR D 214     8697  11908   8983   1638    838   2022       C  
+ATOM  11448  CG  TYR D 214       1.266  47.913  -1.627  1.00 81.29           C  
+ANISOU11448  CG  TYR D 214     8966  12671   9250   1541    737   1850       C  
+ATOM  11449  CD1 TYR D 214       2.548  47.413  -1.797  1.00 85.73           C  
+ANISOU11449  CD1 TYR D 214     9372  13400   9801   1631    754   1957       C  
+ATOM  11450  CD2 TYR D 214       1.126  49.240  -1.240  1.00 90.18           C  
+ANISOU11450  CD2 TYR D 214    10074  13932  10259   1358    629   1560       C  
+ATOM  11451  CE1 TYR D 214       3.660  48.210  -1.588  1.00 89.98           C  
+ANISOU11451  CE1 TYR D 214     9740  14251  10199   1532    665   1784       C  
+ATOM  11452  CE2 TYR D 214       2.230  50.045  -1.030  1.00 89.79           C  
+ANISOU11452  CE2 TYR D 214     9852  14166  10099   1252    544   1373       C  
+ATOM  11453  CZ  TYR D 214       3.494  49.525  -1.205  1.00 88.84           C  
+ANISOU11453  CZ  TYR D 214     9577  14227   9953   1335    563   1488       C  
+ATOM  11454  OH  TYR D 214       4.594  50.325  -0.997  1.00 94.50           O  
+ANISOU11454  OH  TYR D 214    10102  15234  10570   1219    482   1286       O  
+ATOM  11455  N   GLU D 215      -2.720  46.643  -3.815  1.00 72.02           N  
+ANISOU11455  N   GLU D 215     8469  10171   8726   1517    975   1899       N  
+ATOM  11456  CA  GLU D 215      -3.952  45.896  -4.029  1.00 78.85           C  
+ANISOU11456  CA  GLU D 215     9452  10738   9771   1577   1064   1976       C  
+ATOM  11457  C   GLU D 215      -4.005  45.373  -5.463  1.00 98.97           C  
+ANISOU11457  C   GLU D 215    12108  12943  12552   1563   1135   1911       C  
+ATOM  11458  O   GLU D 215      -4.062  46.156  -6.412  1.00106.54           O  
+ANISOU11458  O   GLU D 215    13178  13788  13514   1418   1083   1707       O  
+ATOM  11459  CB  GLU D 215      -5.166  46.767  -3.714  1.00 76.08           C  
+ANISOU11459  CB  GLU D 215     9212  10335   9361   1463   1002   1810       C  
+ATOM  11460  N   ARG D 216      -3.997  44.054  -5.619  1.00106.14           N  
+ANISOU11460  N   ARG D 216    12966  13697  13664   1716   1256   2084       N  
+ATOM  11461  CA  ARG D 216      -3.925  43.438  -6.943  1.00105.18           C  
+ANISOU11461  CA  ARG D 216    12897  13298  13767   1722   1331   1986       C  
+ATOM  11462  C   ARG D 216      -5.302  43.082  -7.503  1.00105.79           C  
+ANISOU11462  C   ARG D 216    13105  13051  14041   1695   1387   1883       C  
+ATOM  11463  O   ARG D 216      -5.516  43.091  -8.717  1.00 99.90           O  
+ANISOU11463  O   ARG D 216    12438  12129  13389   1631   1398   1688       O  
+ATOM  11464  CB  ARG D 216      -3.043  42.190  -6.900  1.00101.57           C  
+ANISOU11464  CB  ARG D 216    12282  12829  13479   1906   1436   2178       C  
+ATOM  11465  N   ASP D 217      -6.226  42.759  -6.604  1.00 94.43           N  
+ANISOU11465  N   ASP D 217    11665  11568  12645   1746   1424   2014       N  
+ATOM  11466  CA  ASP D 217      -7.574  42.338  -6.976  1.00 85.73           C  
+ANISOU11466  CA  ASP D 217    10654  10170  11747   1727   1487   1930       C  
+ATOM  11467  C   ASP D 217      -8.541  43.509  -7.115  1.00 72.60           C  
+ANISOU11467  C   ASP D 217     9137   8509   9938   1575   1379   1723       C  
+ATOM  11468  O   ASP D 217      -9.755  43.338  -7.009  1.00 77.80           O  
+ANISOU11468  O   ASP D 217     9852   9009  10701   1560   1411   1682       O  
+ATOM  11469  CB  ASP D 217      -8.108  41.336  -5.952  1.00 91.78           C  
+ANISOU11469  CB  ASP D 217    11329  10875  12669   1857   1605   2202       C  
+ATOM  11470  CG  ASP D 217      -7.190  40.144  -5.778  1.00101.69           C  
+ANISOU11470  CG  ASP D 217    12427  12092  14119   2030   1718   2449       C  
+ATOM  11471  OD1 ASP D 217      -6.551  40.035  -4.711  1.00116.34           O  
+ANISOU11471  OD1 ASP D 217    14159  14210  15834   2134   1715   2724       O  
+ATOM  11472  OD2 ASP D 217      -7.094  39.325  -6.717  1.00103.89           O  
+ANISOU11472  OD2 ASP D 217    12686  12094  14692   2070   1806   2356       O  
+ATOM  11473  N   GLN D 218      -7.996  44.697  -7.355  1.00 61.99           N  
+ANISOU11473  N   GLN D 218     7841   7331   8382   1463   1256   1595       N  
+ATOM  11474  CA  GLN D 218      -8.812  45.892  -7.525  1.00 62.08           C  
+ANISOU11474  CA  GLN D 218     7978   7321   8289   1327   1149   1407       C  
+ATOM  11475  C   GLN D 218      -9.629  45.858  -8.801  1.00 71.21           C  
+ANISOU11475  C   GLN D 218     9250   8229   9576   1276   1154   1228       C  
+ATOM  11476  O   GLN D 218      -9.342  45.094  -9.723  1.00 79.65           O  
+ANISOU11476  O   GLN D 218    10300   9187  10776   1317   1223   1194       O  
+ATOM  11477  CB  GLN D 218      -7.943  47.148  -7.543  1.00 86.34           C  
+ANISOU11477  CB  GLN D 218    11052  10587  11167   1216   1031   1327       C  
+ATOM  11478  CG  GLN D 218      -7.332  47.520  -6.221  1.00104.81           C  
+ANISOU11478  CG  GLN D 218    13269  13224  13331   1234    988   1414       C  
+ATOM  11479  CD  GLN D 218      -6.476  48.767  -6.315  1.00105.07           C  
+ANISOU11479  CD  GLN D 218    13283  13409  13229   1103    880   1288       C  
+ATOM  11480  OE1 GLN D 218      -5.543  48.835  -7.115  1.00108.13           O  
+ANISOU11480  OE1 GLN D 218    13658  13801  13627   1064    884   1280       O  
+ATOM  11481  NE2 GLN D 218      -6.789  49.762  -5.494  1.00101.75           N  
+ANISOU11481  NE2 GLN D 218    12844  13116  12700   1028    791   1173       N  
+ATOM  11482  N   ARG D 219     -10.663  46.691  -8.830  1.00 60.28           N  
+ANISOU11482  N   ARG D 219     7967   6785   8153   1194   1076   1099       N  
+ATOM  11483  CA  ARG D 219     -11.464  46.879 -10.025  1.00 50.38           C  
+ANISOU11483  CA  ARG D 219     6815   5357   6971   1144   1050    926       C  
+ATOM  11484  C   ARG D 219     -10.546  47.385 -11.129  1.00 52.85           C  
+ANISOU11484  C   ARG D 219     7150   5732   7198   1082   1006    876       C  
+ATOM  11485  O   ARG D 219      -9.705  48.255 -10.896  1.00 59.41           O  
+ANISOU11485  O   ARG D 219     7972   6705   7897   1015    941    917       O  
+ATOM  11486  CB  ARG D 219     -12.601  47.864  -9.750  1.00 54.22           C  
+ANISOU11486  CB  ARG D 219     7389   5800   7412   1075    955    818       C  
+ATOM  11487  CG  ARG D 219     -13.426  48.266 -10.956  1.00 48.67           C  
+ANISOU11487  CG  ARG D 219     6784   4965   6745   1030    899    657       C  
+ATOM  11488  CD  ARG D 219     -14.653  49.042 -10.505  1.00 49.32           C  
+ANISOU11488  CD  ARG D 219     6927   4987   6827    997    821    564       C  
+ATOM  11489  NE  ARG D 219     -15.537  48.238  -9.666  1.00 49.53           N  
+ANISOU11489  NE  ARG D 219     6904   4958   6955   1057    902    577       N  
+ATOM  11490  CZ  ARG D 219     -16.621  47.612 -10.110  1.00 46.99           C  
+ANISOU11490  CZ  ARG D 219     6590   4489   6776   1085    947    478       C  
+ATOM  11491  NH1 ARG D 219     -16.965  47.707 -11.387  1.00 49.20           N  
+ANISOU11491  NH1 ARG D 219     6919   4695   7081   1069    905    340       N  
+ATOM  11492  NH2 ARG D 219     -17.367  46.899  -9.277  1.00 51.28           N  
+ANISOU11492  NH2 ARG D 219     7074   4983   7427   1126   1037    518       N  
+ATOM  11493  N   ARG D 220     -10.709  46.843 -12.329  1.00 51.88           N  
+ANISOU11493  N   ARG D 220     7039   5524   7151   1101   1047    775       N  
+ATOM  11494  CA  ARG D 220      -9.877  47.239 -13.456  1.00 59.39           C  
+ANISOU11494  CA  ARG D 220     7992   6575   7998   1049   1023    737       C  
+ATOM  11495  C   ARG D 220     -10.416  48.496 -14.118  1.00 53.92           C  
+ANISOU11495  C   ARG D 220     7407   5886   7195    948    909    679       C  
+ATOM  11496  O   ARG D 220     -11.616  48.613 -14.366  1.00 57.54           O  
+ANISOU11496  O   ARG D 220     7929   6238   7696    953    872    584       O  
+ATOM  11497  CB  ARG D 220      -9.788  46.112 -14.487  1.00 71.23           C  
+ANISOU11497  CB  ARG D 220     9425   8036   9604   1120   1118    626       C  
+ATOM  11498  CG  ARG D 220      -8.930  46.452 -15.698  1.00 79.17           C  
+ANISOU11498  CG  ARG D 220    10408   9203  10469   1073   1106    581       C  
+ATOM  11499  CD  ARG D 220      -8.675  45.231 -16.568  1.00 92.14           C  
+ANISOU11499  CD  ARG D 220    11940  10846  12222   1158   1213    434       C  
+ATOM  11500  NE  ARG D 220      -7.739  44.287 -15.967  1.00105.69           N  
+ANISOU11500  NE  ARG D 220    13538  12544  14077   1248   1312    514       N  
+ATOM  11501  CZ  ARG D 220      -7.339  43.164 -16.555  1.00101.53           C  
+ANISOU11501  CZ  ARG D 220    12885  11989  13703   1336   1418    389       C  
+ATOM  11502  NH1 ARG D 220      -7.791  42.852 -17.763  1.00 92.80           N  
+ANISOU11502  NH1 ARG D 220    11749  10906  12606   1336   1438    145       N  
+ATOM  11503  NH2 ARG D 220      -6.487  42.355 -15.942  1.00 99.73           N  
+ANISOU11503  NH2 ARG D 220    12544  11726  13623   1434   1503    495       N  
+ATOM  11504  N   HIS D 221      -9.525  49.437 -14.404  1.00 50.23           N  
+ANISOU11504  N   HIS D 221     6946   5535   6603    860    858    750       N  
+ATOM  11505  CA  HIS D 221      -9.912  50.636 -15.129  1.00 50.07           C  
+ANISOU11505  CA  HIS D 221     7013   5504   6509    770    764    749       C  
+ATOM  11506  C   HIS D 221      -9.173  50.673 -16.456  1.00 51.41           C  
+ANISOU11506  C   HIS D 221     7151   5814   6567    741    791    776       C  
+ATOM  11507  O   HIS D 221      -8.265  49.876 -16.694  1.00 50.80           O  
+ANISOU11507  O   HIS D 221     6982   5848   6472    778    877    772       O  
+ATOM  11508  CB  HIS D 221      -9.614  51.892 -14.311  1.00 52.84           C  
+ANISOU11508  CB  HIS D 221     7386   5841   6850    671    684    816       C  
+ATOM  11509  CG  HIS D 221     -10.149  51.841 -12.916  1.00 62.38           C  
+ANISOU11509  CG  HIS D 221     8586   6994   8122    702    665    775       C  
+ATOM  11510  ND1 HIS D 221     -11.472  52.079 -12.614  1.00 52.44           N  
+ANISOU11510  ND1 HIS D 221     7392   5605   6927    723    616    691       N  
+ATOM  11511  CD2 HIS D 221      -9.537  51.581 -11.735  1.00 59.39           C  
+ANISOU11511  CD2 HIS D 221     8122   6715   7729    721    691    809       C  
+ATOM  11512  CE1 HIS D 221     -11.653  51.965 -11.311  1.00 58.14           C  
+ANISOU11512  CE1 HIS D 221     8070   6353   7667    748    620    672       C  
+ATOM  11513  NE2 HIS D 221     -10.493  51.665 -10.755  1.00 48.64           N  
+ANISOU11513  NE2 HIS D 221     6774   5302   6406    750    663    750       N  
+ATOM  11514  N   TYR D 222      -9.562  51.602 -17.320  1.00 56.31           N  
+ANISOU11514  N   TYR D 222     7835   6448   7112    682    722    816       N  
+ATOM  11515  CA  TYR D 222      -8.991  51.663 -18.656  1.00 55.73           C  
+ANISOU11515  CA  TYR D 222     7721   6560   6892    659    751    861       C  
+ATOM  11516  C   TYR D 222      -8.560  53.072 -19.032  1.00 60.96           C  
+ANISOU11516  C   TYR D 222     8418   7252   7492    537    695   1050       C  
+ATOM  11517  O   TYR D 222      -9.163  54.058 -18.608  1.00 57.08           O  
+ANISOU11517  O   TYR D 222     8004   6599   7086    490    609   1106       O  
+ATOM  11518  CB  TYR D 222      -9.992  51.128 -19.688  1.00 53.60           C  
+ANISOU11518  CB  TYR D 222     7456   6345   6566    741    746    730       C  
+ATOM  11519  CG  TYR D 222     -10.456  49.712 -19.419  1.00 55.19           C  
+ANISOU11519  CG  TYR D 222     7602   6481   6888    848    817    523       C  
+ATOM  11520  CD1 TYR D 222     -11.485  49.450 -18.523  1.00 59.90           C  
+ANISOU11520  CD1 TYR D 222     8246   6872   7642    889    795    449       C  
+ATOM  11521  CD2 TYR D 222      -9.860  48.635 -20.063  1.00 55.98           C  
+ANISOU11521  CD2 TYR D 222     7584   6713   6972    906    916    399       C  
+ATOM  11522  CE1 TYR D 222     -11.906  48.156 -18.275  1.00 65.98           C  
+ANISOU11522  CE1 TYR D 222     8952   7551   8567    976    878    291       C  
+ATOM  11523  CE2 TYR D 222     -10.274  47.339 -19.822  1.00 61.40           C  
+ANISOU11523  CE2 TYR D 222     8203   7288   7838   1000    994    210       C  
+ATOM  11524  CZ  TYR D 222     -11.297  47.105 -18.928  1.00 63.63           C  
+ANISOU11524  CZ  TYR D 222     8538   7345   8293   1030    978    174       C  
+ATOM  11525  OH  TYR D 222     -11.711  45.815 -18.687  1.00 71.10           O  
+ANISOU11525  OH  TYR D 222     9404   8150   9459   1113   1071     15       O  
+ATOM  11526  N   CYS D 223      -7.509  53.149 -19.839  1.00 70.50           N  
+ANISOU11526  N   CYS D 223     9554   8660   8574    486    753   1146       N  
+ATOM  11527  CA  CYS D 223      -7.022  54.419 -20.353  1.00 72.75           C  
+ANISOU11527  CA  CYS D 223     9849   8981   8813    362    727   1363       C  
+ATOM  11528  C   CYS D 223      -6.730  54.264 -21.837  1.00 69.60           C  
+ANISOU11528  C   CYS D 223     9389   8861   8195    373    778   1438       C  
+ATOM  11529  O   CYS D 223      -5.994  53.369 -22.235  1.00 63.04           O  
+ANISOU11529  O   CYS D 223     8455   8236   7261    409    867   1348       O  
+ATOM  11530  CB  CYS D 223      -5.770  54.873 -19.601  1.00 51.61           C  
+ANISOU11530  CB  CYS D 223     7108   6292   6210    247    759   1435       C  
+ATOM  11531  SG  CYS D 223      -4.971  56.332 -20.307  1.00 59.30           S  
+ANISOU11531  SG  CYS D 223     8054   7303   7176     69    767   1711       S  
+ATOM  11532  N   LEU D 224      -7.298  55.143 -22.655  1.00 61.99           N  
+ANISOU11532  N   LEU D 224     8470   7925   7158    350    723   1609       N  
+ATOM  11533  CA  LEU D 224      -7.098  55.067 -24.096  1.00 61.83           C  
+ANISOU11533  CA  LEU D 224     8376   8236   6880    369    765   1707       C  
+ATOM  11534  C   LEU D 224      -6.065  56.083 -24.546  1.00 56.49           C  
+ANISOU11534  C   LEU D 224     7653   7655   6157    227    813   2011       C  
+ATOM  11535  O   LEU D 224      -6.203  57.277 -24.278  1.00 59.87           O  
+ANISOU11535  O   LEU D 224     8143   7867   6737    137    761   2228       O  
+ATOM  11536  CB  LEU D 224      -8.415  55.294 -24.841  1.00 57.90           C  
+ANISOU11536  CB  LEU D 224     7928   7785   6285    460    678   1729       C  
+ATOM  11537  CG  LEU D 224      -9.556  54.322 -24.538  1.00 55.51           C  
+ANISOU11537  CG  LEU D 224     7654   7403   6035    591    634   1421       C  
+ATOM  11538  CD1 LEU D 224     -10.817  54.730 -25.282  1.00 56.76           C  
+ANISOU11538  CD1 LEU D 224     7844   7628   6093    672    534   1464       C  
+ATOM  11539  CD2 LEU D 224      -9.161  52.900 -24.891  1.00 62.99           C  
+ANISOU11539  CD2 LEU D 224     8483   8564   6885    664    729   1148       C  
+ATOM  11540  N   ILE D 225      -5.026  55.613 -25.228  1.00 53.74           N  
+ANISOU11540  N   ILE D 225     7178   7618   5623    204    919   2020       N  
+ATOM  11541  CA  ILE D 225      -4.036  56.536 -25.771  1.00 54.95           C  
+ANISOU11541  CA  ILE D 225     7263   7900   5714     61    984   2326       C  
+ATOM  11542  C   ILE D 225      -3.800  56.245 -27.241  1.00 66.69           C  
+ANISOU11542  C   ILE D 225     8634   9848   6856    100   1055   2410       C  
+ATOM  11543  O   ILE D 225      -4.304  55.260 -27.773  1.00 60.19           O  
+ANISOU11543  O   ILE D 225     7769   9245   5857    236   1054   2171       O  
+ATOM  11544  CB  ILE D 225      -2.685  56.459 -25.023  1.00 56.44           C  
+ANISOU11544  CB  ILE D 225     7373   8050   6022    -51   1063   2289       C  
+ATOM  11545  CG1 ILE D 225      -2.025  55.095 -25.235  1.00 54.21           C  
+ANISOU11545  CG1 ILE D 225     6970   8037   5591     39   1151   2037       C  
+ATOM  11546  CG2 ILE D 225      -2.860  56.786 -23.541  1.00 57.53           C  
+ANISOU11546  CG2 ILE D 225     7594   7802   6463    -90    991   2194       C  
+ATOM  11547  CD1 ILE D 225      -0.624  55.003 -24.671  1.00 54.89           C  
+ANISOU11547  CD1 ILE D 225     6945   8158   5752    -54   1232   2023       C  
+ATOM  11548  N   LYS D 226      -3.043  57.115 -27.898  1.00 81.44           N  
+ANISOU11548  N   LYS D 226    10434  11876   8635    -23   1123   2742       N  
+ATOM  11549  CA  LYS D 226      -2.686  56.904 -29.292  1.00 74.58           C  
+ANISOU11549  CA  LYS D 226     9426  11513   7399      2   1207   2853       C  
+ATOM  11550  C   LYS D 226      -1.240  56.446 -29.401  1.00 77.27           C  
+ANISOU11550  C   LYS D 226     9610  12092   7656    -77   1346   2788       C  
+ATOM  11551  O   LYS D 226      -0.360  56.974 -28.721  1.00 77.84           O  
+ANISOU11551  O   LYS D 226     9672  11968   7935   -221   1389   2898       O  
+ATOM  11552  CB  LYS D 226      -2.903  58.181 -30.106  1.00 65.58           C  
+ANISOU11552  CB  LYS D 226     8291  10450   6176    -66   1201   3329       C  
+ATOM  11553  N   LYS D 227      -1.007  55.451 -30.250  1.00 79.50           N  
+ANISOU11553  N   LYS D 227     9753  12808   7644     21   1415   2576       N  
+ATOM  11554  CA  LYS D 227       0.336  54.937 -30.485  1.00 80.62           C  
+ANISOU11554  CA  LYS D 227     9720  13231   7681    -30   1552   2487       C  
+ATOM  11555  C   LYS D 227       1.247  56.023 -31.036  1.00 82.60           C  
+ANISOU11555  C   LYS D 227     9886  13658   7840   -207   1649   2909       C  
+ATOM  11556  O   LYS D 227       0.844  56.798 -31.903  1.00 92.86           O  
+ANISOU11556  O   LYS D 227    11184  15139   8959   -231   1647   3243       O  
+ATOM  11557  CB  LYS D 227       0.285  53.750 -31.451  1.00 84.15           C  
+ANISOU11557  CB  LYS D 227    10010  14142   7820    118   1607   2167       C  
+ATOM  11558  CG  LYS D 227       1.626  53.085 -31.715  1.00 96.80           C  
+ANISOU11558  CG  LYS D 227    11410  16049   9320     94   1749   2009       C  
+ATOM  11559  CD  LYS D 227       1.455  51.589 -31.936  1.00 99.14           C  
+ANISOU11559  CD  LYS D 227    11594  16509   9564    271   1771   1508       C  
+ATOM  11560  CE  LYS D 227       2.773  50.847 -31.787  1.00 96.19           C  
+ANISOU11560  CE  LYS D 227    11044  16270   9234    269   1894   1307       C  
+ATOM  11561  NZ  LYS D 227       3.899  51.597 -32.406  1.00 99.33           N  
+ANISOU11561  NZ  LYS D 227    11307  17011   9421    119   2008   1604       N  
+ATOM  11562  N   GLU D 228       2.475  56.081 -30.531  1.00 71.27           N  
+ANISOU11562  N   GLU D 228     8366  12176   6537   -330   1736   2912       N  
+ATOM  11563  CA  GLU D 228       3.441  57.033 -31.055  1.00 71.29           C  
+ANISOU11563  CA  GLU D 228     8256  12355   6477   -516   1853   3291       C  
+ATOM  11564  C   GLU D 228       3.847  56.628 -32.461  1.00 81.74           C  
+ANISOU11564  C   GLU D 228     9387  14312   7360   -475   1972   3330       C  
+ATOM  11565  O   GLU D 228       4.203  55.478 -32.717  1.00 90.13           O  
+ANISOU11565  O   GLU D 228    10323  15666   8256   -363   2021   2967       O  
+ATOM  11566  CB  GLU D 228       4.668  57.129 -30.148  1.00 85.27           C  
+ANISOU11566  CB  GLU D 228     9955  13948   8495   -656   1915   3231       C  
+ATOM  11567  CG  GLU D 228       4.406  57.830 -28.828  1.00 83.04           C  
+ANISOU11567  CG  GLU D 228     9821  13104   8625   -742   1812   3257       C  
+ATOM  11568  CD  GLU D 228       3.968  59.270 -29.019  1.00 86.69           C  
+ANISOU11568  CD  GLU D 228    10366  13335   9238   -879   1789   3679       C  
+ATOM  11569  OE1 GLU D 228       4.631  59.994 -29.793  1.00 93.86           O  
+ANISOU11569  OE1 GLU D 228    11158  14441  10064  -1024   1907   4024       O  
+ATOM  11570  OE2 GLU D 228       2.965  59.679 -28.397  1.00 82.74           O  
+ANISOU11570  OE2 GLU D 228    10035  12449   8955   -841   1661   3674       O  
+ATOM  11571  N   GLU D 229       3.792  57.591 -33.369  1.00 77.61           N  
+ANISOU11571  N   GLU D 229     8824  14007   6658   -560   2022   3778       N  
+ATOM  11572  CA  GLU D 229       4.116  57.349 -34.763  1.00 89.15           C  
+ANISOU11572  CA  GLU D 229    10087  16137   7649   -524   2137   3875       C  
+ATOM  11573  C   GLU D 229       5.276  58.226 -35.186  1.00 88.34           C  
+ANISOU11573  C   GLU D 229     9872  16081   7612   -714   2231   4177       C  
+ATOM  11574  O   GLU D 229       5.524  59.272 -34.585  1.00 84.57           O  
+ANISOU11574  O   GLU D 229     9474  15188   7472   -882   2233   4473       O  
+ATOM  11575  CB  GLU D 229       2.901  57.613 -35.652  1.00 98.00           C  
+ANISOU11575  CB  GLU D 229    11267  17416   8552   -394   2025   4007       C  
+ATOM  11576  CG  GLU D 229       1.797  56.583 -35.503  1.00 96.85           C  
+ANISOU11576  CG  GLU D 229    11188  17304   8305   -186   1922   3595       C  
+ATOM  11577  CD  GLU D 229       0.545  56.956 -36.271  1.00105.15           C  
+ANISOU11577  CD  GLU D 229    12288  18537   9128    -68   1818   3784       C  
+ATOM  11578  OE1 GLU D 229       0.228  56.267 -37.263  1.00105.51           O  
+ANISOU11578  OE1 GLU D 229    12193  19078   8818     70   1803   3542       O  
+ATOM  11579  OE2 GLU D 229      -0.118  57.942 -35.886  1.00104.11           O  
+ANISOU11579  OE2 GLU D 229    12323  18008   9228   -107   1727   4120       O  
+ATOM  11580  N   ARG D 230       5.998  57.797 -36.212  1.00 87.38           N  
+ANISOU11580  N   ARG D 230     9549  16462   7188   -689   2314   4077       N  
+ATOM  11581  CA  ARG D 230       7.136  58.571 -36.671  1.00103.62           C  
+ANISOU11581  CA  ARG D 230    11481  18607   9283   -864   2419   4356       C  
+ATOM  11582  C   ARG D 230       6.697  59.859 -37.339  1.00105.01           C  
+ANISOU11582  C   ARG D 230    11714  18691   9493   -925   2382   4851       C  
+ATOM  11583  O   ARG D 230       5.739  59.893 -38.113  1.00106.91           O  
+ANISOU11583  O   ARG D 230    11979  19133   9508   -787   2297   4934       O  
+ATOM  11584  CB  ARG D 230       8.003  57.742 -37.618  1.00 93.36           C  
+ANISOU11584  CB  ARG D 230     9941  17891   7642   -810   2514   4109       C  
+ATOM  11585  CG  ARG D 230       8.654  56.558 -36.939  1.00107.24           C  
+ANISOU11585  CG  ARG D 230    11611  19698   9437   -761   2571   3639       C  
+ATOM  11586  CD  ARG D 230       9.517  55.751 -37.889  1.00100.73           C  
+ANISOU11586  CD  ARG D 230    10537  19425   8313   -700   2658   3368       C  
+ATOM  11587  NE  ARG D 230      10.087  54.587 -37.216  1.00102.68           N  
+ANISOU11587  NE  ARG D 230    10694  19678   8642   -625   2707   2903       N  
+ATOM  11588  CZ  ARG D 230       9.503  53.397 -37.119  1.00102.78           C  
+ANISOU11588  CZ  ARG D 230    10691  19780   8579   -428   2669   2458       C  
+ATOM  11589  NH1 ARG D 230       8.301  53.191 -37.639  1.00111.52           N  
+ANISOU11589  NH1 ARG D 230    11868  20997   9506   -294   2576   2389       N  
+ATOM  11590  NH2 ARG D 230      10.122  52.413 -36.480  1.00 96.22           N  
+ANISOU11590  NH2 ARG D 230     9763  18912   7883   -360   2726   2074       N  
+ATOM  11591  N   ARG D 231       7.422  60.922 -37.020  1.00110.34           N  
+ANISOU11591  N   ARG D 231    12391  19061  10474  -1131   2450   5170       N  
+ATOM  11592  CA  ARG D 231       7.176  62.225 -37.598  1.00105.01           C  
+ANISOU11592  CA  ARG D 231    11747  18245   9907  -1206   2444   5660       C  
+ATOM  11593  C   ARG D 231       7.969  62.303 -38.890  1.00110.70           C  
+ANISOU11593  C   ARG D 231    12254  19497  10311  -1227   2551   5817       C  
+ATOM  11594  O   ARG D 231       9.024  61.678 -39.005  1.00104.81           O  
+ANISOU11594  O   ARG D 231    11349  19042   9431  -1273   2655   5595       O  
+ATOM  11595  CB  ARG D 231       7.565  63.333 -36.616  1.00100.86           C  
+ANISOU11595  CB  ARG D 231    11307  17109   9905  -1423   2474   5891       C  
+ATOM  11596  CG  ARG D 231       6.510  63.576 -35.545  1.00 95.59           C  
+ANISOU11596  CG  ARG D 231    10857  15904   9559  -1388   2340   5848       C  
+ATOM  11597  CD  ARG D 231       7.121  64.030 -34.229  1.00 93.68           C  
+ANISOU11597  CD  ARG D 231    10647  15157   9789  -1587   2374   5793       C  
+ATOM  11598  NE  ARG D 231       6.127  64.058 -33.159  1.00107.79           N  
+ANISOU11598  NE  ARG D 231    12621  16491  11842  -1535   2242   5678       N  
+ATOM  11599  CZ  ARG D 231       6.387  64.393 -31.900  1.00108.18           C  
+ANISOU11599  CZ  ARG D 231    12708  16089  12307  -1677   2233   5583       C  
+ATOM  11600  NH1 ARG D 231       7.618  64.733 -31.541  1.00115.37           N  
+ANISOU11600  NH1 ARG D 231    13477  16939  13419  -1886   2349   5582       N  
+ATOM  11601  NH2 ARG D 231       5.416  64.385 -30.996  1.00 96.80           N  
+ANISOU11601  NH2 ARG D 231    11428  14274  11077  -1612   2107   5474       N  
+ATOM  11602  N   PRO D 232       7.456  63.054 -39.877  1.00120.13           N  
+ANISOU11602  N   PRO D 232    13429  20838  11377  -1183   2525   6199       N  
+ATOM  11603  CA  PRO D 232       8.148  63.133 -41.166  1.00113.61           C  
+ANISOU11603  CA  PRO D 232    12383  20566  10217  -1190   2624   6375       C  
+ATOM  11604  C   PRO D 232       9.570  63.652 -41.034  1.00115.84           C  
+ANISOU11604  C   PRO D 232    12551  20772  10690  -1417   2788   6524       C  
+ATOM  11605  O   PRO D 232       9.785  64.797 -40.631  1.00121.94           O  
+ANISOU11605  O   PRO D 232    13390  21090  11853  -1585   2832   6870       O  
+ATOM  11606  CB  PRO D 232       7.285  64.110 -41.972  1.00117.48           C  
+ANISOU11606  CB  PRO D 232    12900  21070  10666  -1126   2562   6846       C  
+ATOM  11607  CG  PRO D 232       6.489  64.862 -40.954  1.00116.18           C  
+ANISOU11607  CG  PRO D 232    12971  20212  10961  -1163   2471   6986       C  
+ATOM  11608  CD  PRO D 232       6.240  63.882 -39.853  1.00112.60           C  
+ANISOU11608  CD  PRO D 232    12636  19558  10587  -1117   2405   6497       C  
+ATOM  11609  N   ASP D 233      10.524  62.786 -41.356  1.00116.26           N  
+ANISOU11609  N   ASP D 233    12424  21264  10487  -1419   2878   6232       N  
+ATOM  11610  CA  ASP D 233      11.940  63.121 -41.311  1.00121.44           C  
+ANISOU11610  CA  ASP D 233    12936  21938  11267  -1622   3040   6317       C  
+ATOM  11611  C   ASP D 233      12.420  63.531 -39.921  1.00124.04           C  
+ANISOU11611  C   ASP D 233    13368  21663  12099  -1809   3074   6266       C  
+ATOM  11612  O   ASP D 233      12.562  64.716 -39.623  1.00130.92           O  
+ANISOU11612  O   ASP D 233    14293  22113  13336  -1980   3116   6622       O  
+ATOM  11613  CB  ASP D 233      12.254  64.221 -42.326  1.00129.59           C  
+ANISOU11613  CB  ASP D 233    13863  23122  12253  -1716   3130   6852       C  
+ATOM  11614  CG  ASP D 233      11.804  63.857 -43.725  1.00134.61           C  
+ANISOU11614  CG  ASP D 233    14361  24413  12372  -1532   3095   6920       C  
+ATOM  11615  OD1 ASP D 233      12.213  62.785 -44.215  1.00139.76           O  
+ANISOU11615  OD1 ASP D 233    14852  25590  12660  -1437   3114   6553       O  
+ATOM  11616  OD2 ASP D 233      11.044  64.638 -44.334  1.00136.81           O  
+ANISOU11616  OD2 ASP D 233    14675  24690  12618  -1478   3046   7327       O  
+ATOM  11617  N   GLU D 234      12.672  62.534 -39.080  1.00124.69           N  
+ANISOU11617  N   GLU D 234    13456  21716  12207  -1770   3054   5808       N  
+ATOM  11618  CA  GLU D 234      13.329  62.755 -37.800  1.00119.54           C  
+ANISOU11618  CA  GLU D 234    12830  20619  11970  -1944   3096   5698       C  
+ATOM  11619  C   GLU D 234      14.035  61.452 -37.460  1.00114.80           C  
+ANISOU11619  C   GLU D 234    12104  20308  11209  -1872   3127   5207       C  
+ATOM  11620  O   GLU D 234      13.637  60.383 -37.927  1.00105.04           O  
+ANISOU11620  O   GLU D 234    10836  19440   9634  -1667   3077   4916       O  
+ATOM  11621  CB  GLU D 234      12.343  63.162 -36.699  1.00104.93           C  
+ANISOU11621  CB  GLU D 234    11207  18182  10478  -1947   2972   5720       C  
+ATOM  11622  CG  GLU D 234      11.730  62.011 -35.906  1.00115.96           C  
+ANISOU11622  CG  GLU D 234    12696  19551  11812  -1782   2866   5290       C  
+ATOM  11623  CD  GLU D 234      10.944  62.505 -34.702  1.00124.56           C  
+ANISOU11623  CD  GLU D 234    13984  20044  13298  -1824   2761   5321       C  
+ATOM  11624  OE1 GLU D 234      10.746  63.735 -34.588  1.00139.29           O  
+ANISOU11624  OE1 GLU D 234    15923  21522  15478  -1958   2755   5662       O  
+ATOM  11625  OE2 GLU D 234      10.592  61.678 -33.832  1.00 98.97           O  
+ANISOU11625  OE2 GLU D 234    10808  16713  10084  -1730   2693   4997       O  
+ATOM  11626  N   LEU D 235      15.096  61.539 -36.667  1.00105.52           N  
+ANISOU11626  N   LEU D 235    10832  18970  10289  -2036   3212   5100       N  
+ATOM  11627  CA  LEU D 235      15.941  60.378 -36.426  1.00104.05           C  
+ANISOU11627  CA  LEU D 235    10484  19083   9966  -1969   3257   4667       C  
+ATOM  11628  C   LEU D 235      15.209  59.301 -35.634  1.00 99.14           C  
+ANISOU11628  C   LEU D 235     9965  18373   9330  -1778   3143   4280       C  
+ATOM  11629  O   LEU D 235      14.194  59.570 -34.992  1.00 99.97           O  
+ANISOU11629  O   LEU D 235    10268  18108   9609  -1750   3037   4349       O  
+ATOM  11630  CB  LEU D 235      17.221  60.792 -35.700  1.00104.73           C  
+ANISOU11630  CB  LEU D 235    10430  19010  10353  -2190   3365   4654       C  
+ATOM  11631  CG  LEU D 235      18.129  61.754 -36.469  1.00109.93           C  
+ANISOU11631  CG  LEU D 235    10949  19783  11038  -2390   3510   4994       C  
+ATOM  11632  CD1 LEU D 235      19.356  62.110 -35.647  1.00110.39           C  
+ANISOU11632  CD1 LEU D 235    10854  19667  11420  -2612   3611   4923       C  
+ATOM  11633  CD2 LEU D 235      18.528  61.165 -37.814  1.00113.23           C  
+ANISOU11633  CD2 LEU D 235    11207  20814  11001  -2277   3576   4952       C  
+ATOM  11634  N   GLU D 236      15.728  58.079 -35.685  1.00 98.24           N  
+ANISOU11634  N   GLU D 236     9708  18589   9028  -1642   3169   3871       N  
+ATOM  11635  CA  GLU D 236      15.027  56.944 -35.105  1.00 94.26           C  
+ANISOU11635  CA  GLU D 236     9277  18049   8487  -1431   3079   3493       C  
+ATOM  11636  C   GLU D 236      15.252  56.897 -33.600  1.00 90.92           C  
+ANISOU11636  C   GLU D 236     8890  17243   8414  -1493   3054   3372       C  
+ATOM  11637  O   GLU D 236      14.474  56.290 -32.866  1.00 87.32           O  
+ANISOU11637  O   GLU D 236     8547  16608   8023  -1356   2969   3179       O  
+ATOM  11638  CB  GLU D 236      15.493  55.633 -35.748  1.00 95.06           C  
+ANISOU11638  CB  GLU D 236     9193  18621   8304  -1248   3119   3078       C  
+ATOM  11639  CG  GLU D 236      15.182  55.505 -37.233  1.00107.31           C  
+ANISOU11639  CG  GLU D 236    10679  20621   9472  -1158   3124   3118       C  
+ATOM  11640  CD  GLU D 236      13.698  55.587 -37.533  1.00116.42           C  
+ANISOU11640  CD  GLU D 236    12019  21706  10511  -1041   3008   3206       C  
+ATOM  11641  OE1 GLU D 236      12.901  55.026 -36.752  1.00104.52           O  
+ANISOU11641  OE1 GLU D 236    10641  19951   9118   -924   2929   2993       O  
+ATOM  11642  OE2 GLU D 236      13.329  56.211 -38.550  1.00119.23           O  
+ANISOU11642  OE2 GLU D 236    12377  22267  10660  -1059   2997   3494       O  
+ATOM  11643  N   ALA D 237      16.308  57.562 -33.143  1.00 92.15           N  
+ANISOU11643  N   ALA D 237     8931  17288   8793  -1701   3128   3488       N  
+ATOM  11644  CA  ALA D 237      16.623  57.610 -31.721  1.00 89.52           C  
+ANISOU11644  CA  ALA D 237     8583  16643   8787  -1781   3100   3375       C  
+ATOM  11645  C   ALA D 237      15.657  58.512 -30.956  1.00 97.75           C  
+ANISOU11645  C   ALA D 237     9835  17198  10106  -1880   3007   3613       C  
+ATOM  11646  O   ALA D 237      15.296  58.220 -29.815  1.00 99.14           O  
+ANISOU11646  O   ALA D 237    10106  17072  10493  -1814   2892   3410       O  
+ATOM  11647  CB  ALA D 237      18.053  58.074 -31.516  1.00 91.92           C  
+ANISOU11647  CB  ALA D 237     8670  17009   9247  -1983   3205   3399       C  
+ATOM  11648  N   ASP D 238      15.237  59.604 -31.588  1.00 89.97           N  
+ANISOU11648  N   ASP D 238     8956  16062   9167  -1999   3012   3985       N  
+ATOM  11649  CA  ASP D 238      14.278  60.518 -30.975  1.00 90.94           C  
+ANISOU11649  CA  ASP D 238     9278  15697   9581  -2082   2919   4214       C  
+ATOM  11650  C   ASP D 238      12.909  59.853 -30.874  1.00 85.52           C  
+ANISOU11650  C   ASP D 238     8788  14955   8750  -1854   2795   4106       C  
+ATOM  11651  O   ASP D 238      12.226  59.931 -29.841  1.00 86.09           O  
+ANISOU11651  O   ASP D 238     9033  14588   9089  -1808   2647   3969       O  
+ATOM  11652  CB  ASP D 238      14.183  61.818 -31.778  1.00 92.54           C  
+ANISOU11652  CB  ASP D 238     9527  15755   9879  -2232   2960   4642       C  
+ATOM  11653  CG  ASP D 238      15.524  62.516 -31.922  1.00105.73           C  
+ANISOU11653  CG  ASP D 238    10998  17464  11710  -2469   3102   4763       C  
+ATOM  11654  OD1 ASP D 238      16.555  61.910 -31.559  1.00100.09           O  
+ANISOU11654  OD1 ASP D 238    10096  16967  10966  -2497   3165   4500       O  
+ATOM  11655  OD2 ASP D 238      15.548  63.672 -32.397  1.00115.40           O  
+ANISOU11655  OD2 ASP D 238    12244  18498  13104  -2620   3153   5118       O  
+ATOM  11656  N   PHE D 239      12.523  59.183 -31.955  1.00 91.27           N  
+ANISOU11656  N   PHE D 239     9524  16052   9104  -1670   2796   4041       N  
+ATOM  11657  CA  PHE D 239      11.264  58.458 -31.998  1.00 89.80           C  
+ANISOU11657  CA  PHE D 239     9491  15879   8751  -1447   2693   3895       C  
+ATOM  11658  C   PHE D 239      11.263  57.347 -30.960  1.00 80.08           C  
+ANISOU11658  C   PHE D 239     8296  14482   7647  -1284   2595   3412       C  
+ATOM  11659  O   PHE D 239      10.282  57.165 -30.245  1.00 77.15           O  
+ANISOU11659  O   PHE D 239     8128  13747   7439  -1168   2442   3271       O  
+ATOM  11660  CB  PHE D 239      11.005  57.886 -33.392  1.00 85.88           C  
+ANISOU11660  CB  PHE D 239     8940  15853   7838  -1287   2709   3832       C  
+ATOM  11661  CG  PHE D 239       9.814  56.975 -33.457  1.00 91.56           C  
+ANISOU11661  CG  PHE D 239     9768  16644   8377  -1053   2617   3592       C  
+ATOM  11662  CD1 PHE D 239       8.538  57.466 -33.244  1.00 82.05           C  
+ANISOU11662  CD1 PHE D 239     8775  15143   7255  -1014   2502   3769       C  
+ATOM  11663  CD2 PHE D 239       9.971  55.627 -33.733  1.00 92.41           C  
+ANISOU11663  CD2 PHE D 239     9752  17098   8261   -870   2649   3168       C  
+ATOM  11664  CE1 PHE D 239       7.440  56.629 -33.299  1.00 79.98           C  
+ANISOU11664  CE1 PHE D 239     8624  14881   6883   -792   2386   3481       C  
+ATOM  11665  CE2 PHE D 239       8.876  54.786 -33.793  1.00 80.90           C  
+ANISOU11665  CE2 PHE D 239     8393  15634   6709   -655   2549   2885       C  
+ATOM  11666  CZ  PHE D 239       7.609  55.289 -33.577  1.00 79.44           C  
+ANISOU11666  CZ  PHE D 239     8437  15124   6622   -619   2411   3035       C  
+ATOM  11667  N   GLU D 240      12.368  56.611 -30.874  1.00 80.48           N  
+ANISOU11667  N   GLU D 240     8146  14792   7640  -1264   2680   3164       N  
+ATOM  11668  CA  GLU D 240      12.471  55.515 -29.916  1.00 90.27           C  
+ANISOU11668  CA  GLU D 240     9397  15883   9019  -1089   2593   2735       C  
+ATOM  11669  C   GLU D 240      12.497  56.055 -28.488  1.00 86.36           C  
+ANISOU11669  C   GLU D 240     9006  14894   8911  -1176   2480   2723       C  
+ATOM  11670  O   GLU D 240      12.081  55.376 -27.545  1.00 77.86           O  
+ANISOU11670  O   GLU D 240     8029  13573   7980  -1020   2360   2461       O  
+ATOM  11671  CB  GLU D 240      13.728  54.684 -30.187  1.00 79.00           C  
+ANISOU11671  CB  GLU D 240     7701  14856   7461  -1047   2717   2506       C  
+ATOM  11672  CG  GLU D 240      13.588  53.676 -31.320  1.00 80.26           C  
+ANISOU11672  CG  GLU D 240     7748  15475   7274   -867   2792   2302       C  
+ATOM  11673  CD  GLU D 240      14.905  53.007 -31.677  1.00102.92           C  
+ANISOU11673  CD  GLU D 240    10321  18763  10022   -848   2934   2099       C  
+ATOM  11674  OE1 GLU D 240      15.895  53.210 -30.946  1.00 82.40           O  
+ANISOU11674  OE1 GLU D 240     7614  16074   7621   -949   2957   2093       O  
+ATOM  11675  OE2 GLU D 240      14.954  52.285 -32.695  1.00107.37           O  
+ANISOU11675  OE2 GLU D 240    10756  19730  10309   -725   3002   1910       O  
+ATOM  11676  N   TYR D 241      12.963  57.293 -28.343  1.00 77.20           N  
+ANISOU11676  N   TYR D 241     7809  13601   7923  -1428   2525   3009       N  
+ATOM  11677  CA  TYR D 241      12.935  57.987 -27.062  1.00 75.82           C  
+ANISOU11677  CA  TYR D 241     7713  12978   8118  -1539   2421   2991       C  
+ATOM  11678  C   TYR D 241      11.483  58.218 -26.642  1.00 73.45           C  
+ANISOU11678  C   TYR D 241     7684  12289   7936  -1447   2267   3011       C  
+ATOM  11679  O   TYR D 241      11.073  57.856 -25.530  1.00 70.74           O  
+ANISOU11679  O   TYR D 241     7441  11678   7759  -1343   2136   2776       O  
+ATOM  11680  CB  TYR D 241      13.703  59.312 -27.158  1.00 83.50           C  
+ANISOU11680  CB  TYR D 241     8562  13883   9280  -1846   2522   3287       C  
+ATOM  11681  CG  TYR D 241      13.648  60.187 -25.925  1.00 85.12           C  
+ANISOU11681  CG  TYR D 241     8820  13630   9894  -1989   2422   3251       C  
+ATOM  11682  CD1 TYR D 241      14.556  60.005 -24.889  1.00 86.67           C  
+ANISOU11682  CD1 TYR D 241     8866  13814  10250  -2032   2393   2985       C  
+ATOM  11683  CD2 TYR D 241      12.707  61.203 -25.800  1.00 83.13           C  
+ANISOU11683  CD2 TYR D 241     8741  12980   9866  -2076   2355   3463       C  
+ATOM  11684  CE1 TYR D 241      14.526  60.801 -23.761  1.00 89.78           C  
+ANISOU11684  CE1 TYR D 241     9273  13846  10994  -2164   2300   2901       C  
+ATOM  11685  CE2 TYR D 241      12.668  62.004 -24.671  1.00 96.80           C  
+ANISOU11685  CE2 TYR D 241    10491  14304  11984  -2208   2268   3374       C  
+ATOM  11686  CZ  TYR D 241      13.581  61.798 -23.655  1.00101.33           C  
+ANISOU11686  CZ  TYR D 241    10906  14908  12689  -2255   2241   3078       C  
+ATOM  11687  OH  TYR D 241      13.551  62.588 -22.529  1.00101.77           O  
+ANISOU11687  OH  TYR D 241    10949  14613  13106  -2385   2150   2940       O  
+ATOM  11688  N   ARG D 242      10.704  58.803 -27.550  1.00 74.71           N  
+ANISOU11688  N   ARG D 242     7945  12449   7990  -1475   2285   3304       N  
+ATOM  11689  CA  ARG D 242       9.288  59.067 -27.285  1.00 79.50           C  
+ANISOU11689  CA  ARG D 242     8795  12717   8695  -1384   2145   3343       C  
+ATOM  11690  C   ARG D 242       8.493  57.780 -27.032  1.00 71.57           C  
+ANISOU11690  C   ARG D 242     7899  11733   7560  -1114   2044   3007       C  
+ATOM  11691  O   ARG D 242       7.637  57.728 -26.137  1.00 67.24           O  
+ANISOU11691  O   ARG D 242     7516  10841   7193  -1032   1908   2875       O  
+ATOM  11692  CB  ARG D 242       8.677  59.849 -28.452  1.00 75.27           C  
+ANISOU11692  CB  ARG D 242     8311  12264   8024  -1439   2193   3745       C  
+ATOM  11693  CG  ARG D 242       8.827  61.358 -28.320  1.00 99.01           C  
+ANISOU11693  CG  ARG D 242    11317  14955  11346  -1684   2225   4109       C  
+ATOM  11694  CD  ARG D 242       8.326  62.107 -29.549  1.00 99.90           C  
+ANISOU11694  CD  ARG D 242    11450  15192  11313  -1725   2292   4581       C  
+ATOM  11695  NE  ARG D 242       7.351  61.347 -30.326  1.00 94.83           N  
+ANISOU11695  NE  ARG D 242    10901  14828  10304  -1491   2236   4533       N  
+ATOM  11696  CZ  ARG D 242       7.554  60.939 -31.575  1.00 91.78           C  
+ANISOU11696  CZ  ARG D 242    10393  14983   9496  -1432   2342   4659       C  
+ATOM  11697  NH1 ARG D 242       8.694  61.225 -32.190  1.00 93.46           N  
+ANISOU11697  NH1 ARG D 242    10432  15433   9645  -1558   2465   4763       N  
+ATOM  11698  NH2 ARG D 242       6.616  60.251 -32.212  1.00 91.37           N  
+ANISOU11698  NH2 ARG D 242    10408  15179   9130  -1219   2276   4555       N  
+ATOM  11699  N   VAL D 243       8.801  56.741 -27.803  1.00 70.27           N  
+ANISOU11699  N   VAL D 243     7623  11972   7104   -981   2120   2856       N  
+ATOM  11700  CA  VAL D 243       8.172  55.435 -27.633  1.00 67.93           C  
+ANISOU11700  CA  VAL D 243     7386  11697   6728   -733   2053   2517       C  
+ATOM  11701  C   VAL D 243       8.477  54.880 -26.247  1.00 66.99           C  
+ANISOU11701  C   VAL D 243     7272  11327   6852   -667   1980   2259       C  
+ATOM  11702  O   VAL D 243       7.588  54.363 -25.564  1.00 63.07           O  
+ANISOU11702  O   VAL D 243     6918  10582   6462   -523   1871   2094       O  
+ATOM  11703  CB  VAL D 243       8.639  54.428 -28.707  1.00 69.52           C  
+ANISOU11703  CB  VAL D 243     7411  12387   6616   -617   2167   2354       C  
+ATOM  11704  CG1 VAL D 243       8.147  53.026 -28.379  1.00 67.37           C  
+ANISOU11704  CG1 VAL D 243     7164  12067   6366   -373   2111   1963       C  
+ATOM  11705  CG2 VAL D 243       8.150  54.853 -30.081  1.00 74.73           C  
+ANISOU11705  CG2 VAL D 243     8062  13361   6972   -640   2221   2584       C  
+ATOM  11706  N   ARG D 244       9.734  55.004 -25.832  1.00 66.53           N  
+ANISOU11706  N   ARG D 244     7045  11362   6873   -772   2043   2242       N  
+ATOM  11707  CA  ARG D 244      10.149  54.537 -24.514  1.00 71.42           C  
+ANISOU11707  CA  ARG D 244     7631  11814   7691   -708   1975   2032       C  
+ATOM  11708  C   ARG D 244       9.397  55.281 -23.412  1.00 73.09           C  
+ANISOU11708  C   ARG D 244     8013  11614   8144   -764   1840   2072       C  
+ATOM  11709  O   ARG D 244       8.958  54.672 -22.431  1.00 60.88           O  
+ANISOU11709  O   ARG D 244     6539   9893   6701   -621   1744   1893       O  
+ATOM  11710  CB  ARG D 244      11.659  54.704 -24.332  1.00 66.67           C  
+ANISOU11710  CB  ARG D 244     6790  11423   7117   -832   2064   2025       C  
+ATOM  11711  CG  ARG D 244      12.171  54.269 -22.966  1.00 65.36           C  
+ANISOU11711  CG  ARG D 244     6556  11151   7127   -759   1987   1828       C  
+ATOM  11712  CD  ARG D 244      11.764  52.837 -22.648  1.00 72.27           C  
+ANISOU11712  CD  ARG D 244     7463  12019   7978   -474   1945   1600       C  
+ATOM  11713  NE  ARG D 244      12.275  52.393 -21.353  1.00 68.85           N  
+ANISOU11713  NE  ARG D 244     6946  11526   7687   -383   1876   1466       N  
+ATOM  11714  CZ  ARG D 244      11.980  51.225 -20.793  1.00 70.12           C  
+ANISOU11714  CZ  ARG D 244     7122  11624   7896   -140   1832   1315       C  
+ATOM  11715  NH1 ARG D 244      11.175  50.373 -21.413  1.00 80.43           N  
+ANISOU11715  NH1 ARG D 244     8520  12886   9153     23   1854   1236       N  
+ATOM  11716  NH2 ARG D 244      12.491  50.905 -19.612  1.00 75.59           N  
+ANISOU11716  NH2 ARG D 244     7719  12306   8695    -58   1770   1248       N  
+ATOM  11717  N   LYS D 245       9.242  56.592 -23.575  1.00 64.30           N  
+ANISOU11717  N   LYS D 245     6950  10348   7134   -969   1839   2310       N  
+ATOM  11718  CA  LYS D 245       8.492  57.376 -22.594  1.00 69.78           C  
+ANISOU11718  CA  LYS D 245     7789  10648   8076  -1027   1714   2320       C  
+ATOM  11719  C   LYS D 245       7.025  56.947 -22.511  1.00 73.94           C  
+ANISOU11719  C   LYS D 245     8532  10983   8577   -849   1611   2257       C  
+ATOM  11720  O   LYS D 245       6.460  56.847 -21.414  1.00 62.83           O  
+ANISOU11720  O   LYS D 245     7215   9339   7317   -781   1501   2111       O  
+ATOM  11721  CB  LYS D 245       8.585  58.869 -22.914  1.00 65.31           C  
+ANISOU11721  CB  LYS D 245     7219   9921   7675  -1276   1749   2597       C  
+ATOM  11722  CG  LYS D 245       9.931  59.481 -22.571  1.00 68.26           C  
+ANISOU11722  CG  LYS D 245     7379  10361   8197  -1489   1824   2609       C  
+ATOM  11723  CD  LYS D 245      10.103  59.563 -21.063  1.00 66.16           C  
+ANISOU11723  CD  LYS D 245     7079   9908   8149  -1498   1713   2352       C  
+ATOM  11724  CE  LYS D 245      11.321  60.382 -20.682  1.00 93.85           C  
+ANISOU11724  CE  LYS D 245    10365  13441  11853  -1740   1772   2343       C  
+ATOM  11725  NZ  LYS D 245      12.582  59.609 -20.850  1.00 92.74           N  
+ANISOU11725  NZ  LYS D 245    10007  13688  11541  -1712   1862   2247       N  
+ATOM  11726  N   GLN D 246       6.414  56.671 -23.661  1.00 65.04           N  
+ANISOU11726  N   GLN D 246     7468   9997   7248   -771   1647   2352       N  
+ATOM  11727  CA  GLN D 246       5.030  56.201 -23.668  1.00 65.17           C  
+ANISOU11727  CA  GLN D 246     7664   9866   7232   -602   1555   2266       C  
+ATOM  11728  C   GLN D 246       4.904  54.840 -22.989  1.00 63.20           C  
+ANISOU11728  C   GLN D 246     7411   9621   6983   -399   1523   1968       C  
+ATOM  11729  O   GLN D 246       3.939  54.573 -22.264  1.00 55.01           O  
+ANISOU11729  O   GLN D 246     6506   8343   6052   -296   1426   1860       O  
+ATOM  11730  CB  GLN D 246       4.497  56.109 -25.099  1.00 60.53           C  
+ANISOU11730  CB  GLN D 246     7097   9509   6391   -552   1603   2396       C  
+ATOM  11731  CG  GLN D 246       3.031  55.711 -25.185  1.00 66.34           C  
+ANISOU11731  CG  GLN D 246     7999  10110   7096   -392   1504   2303       C  
+ATOM  11732  CD  GLN D 246       2.468  55.848 -26.586  1.00 78.31           C  
+ANISOU11732  CD  GLN D 246     9520  11883   8352   -358   1534   2457       C  
+ATOM  11733  OE1 GLN D 246       2.882  55.140 -27.504  1.00 93.58           O  
+ANISOU11733  OE1 GLN D 246    11324  14198  10033   -295   1622   2376       O  
+ATOM  11734  NE2 GLN D 246       1.513  56.754 -26.755  1.00 62.11           N  
+ANISOU11734  NE2 GLN D 246     7599   9646   6353   -388   1456   2670       N  
+ATOM  11735  N   GLU D 247       5.899  53.991 -23.217  1.00 59.23           N  
+ANISOU11735  N   GLU D 247     6740   9386   6380   -341   1613   1851       N  
+ATOM  11736  CA  GLU D 247       5.926  52.649 -22.649  1.00 57.42           C  
+ANISOU11736  CA  GLU D 247     6472   9159   6187   -140   1605   1602       C  
+ATOM  11737  C   GLU D 247       6.051  52.709 -21.122  1.00 66.61           C  
+ANISOU11737  C   GLU D 247     7652  10106   7553   -130   1521   1546       C  
+ATOM  11738  O   GLU D 247       5.373  51.967 -20.397  1.00 53.20           O  
+ANISOU11738  O   GLU D 247     6028   8247   5940     25   1462   1426       O  
+ATOM  11739  CB  GLU D 247       7.068  51.852 -23.288  1.00 69.59           C  
+ANISOU11739  CB  GLU D 247     7801  11040   7602    -88   1727   1502       C  
+ATOM  11740  CG  GLU D 247       7.274  50.440 -22.774  1.00 86.87           C  
+ANISOU11740  CG  GLU D 247     9908  13226   9873    127   1740   1266       C  
+ATOM  11741  CD  GLU D 247       8.415  49.738 -23.492  1.00103.28           C  
+ANISOU11741  CD  GLU D 247    11758  15640  11844    176   1864   1154       C  
+ATOM  11742  OE1 GLU D 247       9.065  50.383 -24.344  1.00 91.83           O  
+ANISOU11742  OE1 GLU D 247    10211  14450  10228     30   1942   1266       O  
+ATOM  11743  OE2 GLU D 247       8.655  48.545 -23.214  1.00111.90           O  
+ANISOU11743  OE2 GLU D 247    12754  16733  13029    364   1891    962       O  
+ATOM  11744  N   LEU D 248       6.899  53.614 -20.637  1.00 69.00           N  
+ANISOU11744  N   LEU D 248     7867  10421   7927   -301   1518   1633       N  
+ATOM  11745  CA  LEU D 248       7.032  53.838 -19.198  1.00 61.87           C  
+ANISOU11745  CA  LEU D 248     6952   9372   7183   -312   1429   1565       C  
+ATOM  11746  C   LEU D 248       5.743  54.401 -18.601  1.00 57.78           C  
+ANISOU11746  C   LEU D 248     6629   8546   6778   -319   1317   1575       C  
+ATOM  11747  O   LEU D 248       5.378  54.067 -17.473  1.00 55.82           O  
+ANISOU11747  O   LEU D 248     6409   8193   6606   -223   1240   1471       O  
+ATOM  11748  CB  LEU D 248       8.205  54.771 -18.895  1.00 56.84           C  
+ANISOU11748  CB  LEU D 248     6153   8830   6612   -517   1452   1614       C  
+ATOM  11749  CG  LEU D 248       9.602  54.206 -19.151  1.00 73.84           C  
+ANISOU11749  CG  LEU D 248     8076  11301   8678   -504   1548   1568       C  
+ATOM  11750  CD1 LEU D 248      10.664  55.235 -18.803  1.00 60.30           C  
+ANISOU11750  CD1 LEU D 248     6196   9657   7058   -732   1564   1602       C  
+ATOM  11751  CD2 LEU D 248       9.807  52.930 -18.349  1.00 73.14           C  
+ANISOU11751  CD2 LEU D 248     7918  11288   8585   -269   1519   1414       C  
+ATOM  11752  N   PHE D 249       5.065  55.262 -19.356  1.00 57.86           N  
+ANISOU11752  N   PHE D 249     6757   8434   6793   -425   1311   1714       N  
+ATOM  11753  CA  PHE D 249       3.772  55.800 -18.935  1.00 53.94           C  
+ANISOU11753  CA  PHE D 249     6440   7645   6409   -418   1209   1721       C  
+ATOM  11754  C   PHE D 249       2.763  54.672 -18.735  1.00 52.93           C  
+ANISOU11754  C   PHE D 249     6418   7458   6234   -201   1172   1594       C  
+ATOM  11755  O   PHE D 249       2.065  54.603 -17.707  1.00 53.17           O  
+ANISOU11755  O   PHE D 249     6523   7315   6364   -138   1089   1504       O  
+ATOM  11756  CB  PHE D 249       3.258  56.794 -19.974  1.00 54.64           C  
+ANISOU11756  CB  PHE D 249     6616   7647   6497   -536   1220   1930       C  
+ATOM  11757  CG  PHE D 249       1.904  57.367 -19.663  1.00 55.31           C  
+ANISOU11757  CG  PHE D 249     6876   7434   6705   -516   1115   1944       C  
+ATOM  11758  CD1 PHE D 249       1.726  58.230 -18.595  1.00 65.49           C  
+ANISOU11758  CD1 PHE D 249     8181   8482   8220   -608   1035   1885       C  
+ATOM  11759  CD2 PHE D 249       0.811  57.054 -20.455  1.00 58.85           C  
+ANISOU11759  CD2 PHE D 249     7450   7866   7046   -403   1096   1988       C  
+ATOM  11760  CE1 PHE D 249       0.479  58.762 -18.316  1.00 67.09           C  
+ANISOU11760  CE1 PHE D 249     8529   8415   8547   -583    942   1878       C  
+ATOM  11761  CE2 PHE D 249      -0.437  57.582 -20.181  1.00 58.14           C  
+ANISOU11761  CE2 PHE D 249     7505   7513   7072   -377    997   1996       C  
+ATOM  11762  CZ  PHE D 249      -0.603  58.436 -19.111  1.00 58.36           C  
+ANISOU11762  CZ  PHE D 249     7554   7285   7335   -464    923   1946       C  
+ATOM  11763  N   ILE D 250       2.715  53.778 -19.720  1.00 55.12           N  
+ANISOU11763  N   ILE D 250     6681   7897   6367    -92   1243   1571       N  
+ATOM  11764  CA  ILE D 250       1.850  52.607 -19.664  1.00 53.89           C  
+ANISOU11764  CA  ILE D 250     6589   7684   6202    105   1233   1428       C  
+ATOM  11765  C   ILE D 250       2.193  51.772 -18.436  1.00 55.39           C  
+ANISOU11765  C   ILE D 250     6712   7842   6490    222   1222   1319       C  
+ATOM  11766  O   ILE D 250       1.304  51.257 -17.759  1.00 58.48           O  
+ANISOU11766  O   ILE D 250     7186   8068   6965    335   1176   1251       O  
+ATOM  11767  CB  ILE D 250       1.977  51.747 -20.937  1.00 52.45           C  
+ANISOU11767  CB  ILE D 250     6340   7723   5866    194   1325   1363       C  
+ATOM  11768  CG1 ILE D 250       1.454  52.514 -22.153  1.00 53.99           C  
+ANISOU11768  CG1 ILE D 250     6599   7996   5917    110   1325   1493       C  
+ATOM  11769  CG2 ILE D 250       1.230  50.432 -20.781  1.00 51.64           C  
+ANISOU11769  CG2 ILE D 250     6262   7534   5825    392   1330   1171       C  
+ATOM  11770  CD1 ILE D 250       1.657  51.787 -23.464  1.00 52.79           C  
+ANISOU11770  CD1 ILE D 250     6346   8151   5562    181   1417   1412       C  
+ATOM  11771  N   SER D 251       3.485  51.651 -18.149  1.00 56.81           N  
+ANISOU11771  N   SER D 251     6728   8200   6657    196   1268   1322       N  
+ATOM  11772  CA  SER D 251       3.931  50.910 -16.973  1.00 63.42           C  
+ANISOU11772  CA  SER D 251     7471   9058   7567    317   1254   1263       C  
+ATOM  11773  C   SER D 251       3.411  51.542 -15.678  1.00 67.28           C  
+ANISOU11773  C   SER D 251     8026   9400   8136    279   1147   1269       C  
+ATOM  11774  O   SER D 251       2.904  50.844 -14.789  1.00 58.84           O  
+ANISOU11774  O   SER D 251     6978   8260   7120    422   1118   1237       O  
+ATOM  11775  CB  SER D 251       5.458  50.837 -16.943  1.00 53.59           C  
+ANISOU11775  CB  SER D 251     6018   8064   6279    282   1310   1269       C  
+ATOM  11776  OG  SER D 251       5.912  50.131 -15.802  1.00 59.77           O  
+ANISOU11776  OG  SER D 251     6693   8902   7116    418   1289   1240       O  
+ATOM  11777  N   ASP D 252       3.530  52.865 -15.585  1.00 63.50           N  
+ANISOU11777  N   ASP D 252     7564   8882   7681     86   1098   1307       N  
+ATOM  11778  CA  ASP D 252       3.063  53.598 -14.411  1.00 54.92           C  
+ANISOU11778  CA  ASP D 252     6514   7674   6678     31    997   1260       C  
+ATOM  11779  C   ASP D 252       1.567  53.417 -14.186  1.00 54.76           C  
+ANISOU11779  C   ASP D 252     6671   7434   6701    122    944   1234       C  
+ATOM  11780  O   ASP D 252       1.133  53.203 -13.054  1.00 68.07           O  
+ANISOU11780  O   ASP D 252     8358   9094   8413    199    889   1175       O  
+ATOM  11781  CB  ASP D 252       3.390  55.087 -14.537  1.00 56.28           C  
+ANISOU11781  CB  ASP D 252     6667   7785   6933   -204    968   1284       C  
+ATOM  11782  CG  ASP D 252       4.813  55.408 -14.129  1.00 61.04           C  
+ANISOU11782  CG  ASP D 252     7056   8597   7538   -309    988   1248       C  
+ATOM  11783  OD1 ASP D 252       5.593  54.463 -13.887  1.00 80.45           O  
+ANISOU11783  OD1 ASP D 252     9386  11276   9906   -189   1025   1225       O  
+ATOM  11784  OD2 ASP D 252       5.151  56.608 -14.045  1.00 67.26           O  
+ANISOU11784  OD2 ASP D 252     7792   9319   8443   -511    968   1236       O  
+ATOM  11785  N   LEU D 253       0.776  53.506 -15.252  1.00 53.01           N  
+ANISOU11785  N   LEU D 253     6580   7089   6471    115    961   1279       N  
+ATOM  11786  CA  LEU D 253      -0.662  53.272 -15.106  1.00 53.24           C  
+ANISOU11786  CA  LEU D 253     6762   6924   6543    206    914   1238       C  
+ATOM  11787  C   LEU D 253      -0.944  51.815 -14.748  1.00 61.28           C  
+ANISOU11787  C   LEU D 253     7761   7963   7559    404    957   1185       C  
+ATOM  11788  O   LEU D 253      -1.886  51.516 -14.012  1.00 61.76           O  
+ANISOU11788  O   LEU D 253     7889   7900   7676    485    921   1145       O  
+ATOM  11789  CB  LEU D 253      -1.431  53.663 -16.371  1.00 51.50           C  
+ANISOU11789  CB  LEU D 253     6660   6610   6295    169    915   1296       C  
+ATOM  11790  CG  LEU D 253      -1.826  55.132 -16.571  1.00 54.41           C  
+ANISOU11790  CG  LEU D 253     7105   6826   6742     14    849   1379       C  
+ATOM  11791  CD1 LEU D 253      -0.677  56.098 -16.310  1.00 59.91           C  
+ANISOU11791  CD1 LEU D 253     7688   7572   7501   -161    857   1433       C  
+ATOM  11792  CD2 LEU D 253      -2.406  55.341 -17.964  1.00 59.57           C  
+ANISOU11792  CD2 LEU D 253     7840   7476   7319     10    865   1488       C  
+ATOM  11793  N   SER D 254      -0.121  50.913 -15.273  1.00 53.53           N  
+ANISOU11793  N   SER D 254     6675   7130   6535    480   1045   1187       N  
+ATOM  11794  CA  SER D 254      -0.283  49.486 -15.026  1.00 51.35           C  
+ANISOU11794  CA  SER D 254     6355   6836   6319    670   1105   1146       C  
+ATOM  11795  C   SER D 254      -0.049  49.145 -13.560  1.00 57.92           C  
+ANISOU11795  C   SER D 254     7113   7702   7193    754   1080   1190       C  
+ATOM  11796  O   SER D 254      -0.659  48.217 -13.027  1.00 56.96           O  
+ANISOU11796  O   SER D 254     7001   7483   7160    899   1106   1202       O  
+ATOM  11797  CB  SER D 254       0.673  48.681 -15.908  1.00 53.48           C  
+ANISOU11797  CB  SER D 254     6498   7262   6560    731   1206   1116       C  
+ATOM  11798  OG  SER D 254       0.526  47.290 -15.681  1.00 73.98           O  
+ANISOU11798  OG  SER D 254     9036   9793   9281    920   1273   1071       O  
+ATOM  11799  N   ARG D 255       0.840  49.892 -12.913  1.00 65.27           N  
+ANISOU11799  N   ARG D 255     7949   8789   8062    663   1034   1218       N  
+ATOM  11800  CA  ARG D 255       1.129  49.666 -11.499  1.00 58.87           C  
+ANISOU11800  CA  ARG D 255     7035   8096   7237    742    997   1255       C  
+ATOM  11801  C   ARG D 255      -0.102  49.928 -10.620  1.00 71.23           C  
+ANISOU11801  C   ARG D 255     8705   9534   8824    757    932   1236       C  
+ATOM  11802  O   ARG D 255      -0.210  49.396  -9.514  1.00 74.65           O  
+ANISOU11802  O   ARG D 255     9070  10053   9240    875    925   1294       O  
+ATOM  11803  CB  ARG D 255       2.308  50.535 -11.051  1.00 54.19           C  
+ANISOU11803  CB  ARG D 255     6297   7726   6565    618    951   1233       C  
+ATOM  11804  CG  ARG D 255       2.840  50.197  -9.666  1.00 55.84           C  
+ANISOU11804  CG  ARG D 255     6344   8162   6709    722    914   1266       C  
+ATOM  11805  CD  ARG D 255       4.021  51.080  -9.291  1.00 57.77           C  
+ANISOU11805  CD  ARG D 255     6419   8649   6882    587    864   1194       C  
+ATOM  11806  NE  ARG D 255       4.285  51.064  -7.855  1.00 61.86           N  
+ANISOU11806  NE  ARG D 255     6786   9419   7300    659    794   1181       N  
+ATOM  11807  CZ  ARG D 255       3.941  52.042  -7.023  1.00 65.26           C  
+ANISOU11807  CZ  ARG D 255     7197   9904   7694    550    702   1046       C  
+ATOM  11808  NH1 ARG D 255       3.318  53.118  -7.484  1.00 64.67           N  
+ANISOU11808  NH1 ARG D 255     7255   9597   7720    367    671    931       N  
+ATOM  11809  NH2 ARG D 255       4.219  51.945  -5.730  1.00 62.40           N  
+ANISOU11809  NH2 ARG D 255     6665   9845   7197    633    641   1022       N  
+ATOM  11810  N   PHE D 256      -1.030  50.741 -11.120  1.00 52.26           N  
+ANISOU11810  N   PHE D 256     6455   6948   6455    646    889   1170       N  
+ATOM  11811  CA  PHE D 256      -2.260  51.049 -10.393  1.00 52.63           C  
+ANISOU11811  CA  PHE D 256     6598   6867   6532    654    829   1125       C  
+ATOM  11812  C   PHE D 256      -3.449  50.274 -10.955  1.00 63.49           C  
+ANISOU11812  C   PHE D 256     8099   8035   7989    749    874   1126       C  
+ATOM  11813  O   PHE D 256      -4.602  50.665 -10.760  1.00 61.10           O  
+ANISOU11813  O   PHE D 256     7903   7589   7725    729    827   1071       O  
+ATOM  11814  CB  PHE D 256      -2.557  52.551 -10.430  1.00 53.74           C  
+ANISOU11814  CB  PHE D 256     6801   6925   6693    475    739   1033       C  
+ATOM  11815  CG  PHE D 256      -1.512  53.397  -9.761  1.00 56.27           C  
+ANISOU11815  CG  PHE D 256     6977   7424   6978    361    691    976       C  
+ATOM  11816  CD1 PHE D 256      -1.036  53.066  -8.503  1.00 58.35           C  
+ANISOU11816  CD1 PHE D 256     7091   7926   7153    436    670    957       C  
+ATOM  11817  CD2 PHE D 256      -1.014  54.529 -10.384  1.00 57.68           C  
+ANISOU11817  CD2 PHE D 256     7151   7546   7217    179    669    946       C  
+ATOM  11818  CE1 PHE D 256      -0.079  53.845  -7.882  1.00 69.11           C  
+ANISOU11818  CE1 PHE D 256     8293   9488   8477    328    619    860       C  
+ATOM  11819  CE2 PHE D 256      -0.057  55.312  -9.768  1.00 61.09           C  
+ANISOU11819  CE2 PHE D 256     7428   8127   7657     57    631    859       C  
+ATOM  11820  CZ  PHE D 256       0.411  54.970  -8.515  1.00 69.54           C  
+ANISOU11820  CZ  PHE D 256     8340   9454   8627    131    601    791       C  
+ATOM  11821  N   ASN D 257      -3.152  49.186 -11.661  1.00 54.32           N  
+ANISOU11821  N   ASN D 257     6906   6864   6871    850    966   1161       N  
+ATOM  11822  CA  ASN D 257      -4.163  48.342 -12.299  1.00 60.59           C  
+ANISOU11822  CA  ASN D 257     7779   7472   7771    936   1021   1117       C  
+ATOM  11823  C   ASN D 257      -5.050  49.114 -13.275  1.00 53.90           C  
+ANISOU11823  C   ASN D 257     7071   6503   6907    837    970   1029       C  
+ATOM  11824  O   ASN D 257      -6.247  48.849 -13.392  1.00 55.77           O  
+ANISOU11824  O   ASN D 257     7390   6585   7215    877    966    967       O  
+ATOM  11825  CB  ASN D 257      -5.027  47.643 -11.243  1.00 60.01           C  
+ANISOU11825  CB  ASN D 257     7708   7306   7786   1048   1042   1163       C  
+ATOM  11826  CG  ASN D 257      -5.752  46.428 -11.794  1.00 73.80           C  
+ANISOU11826  CG  ASN D 257     9470   8868   9704   1159   1136   1124       C  
+ATOM  11827  OD1 ASN D 257      -5.293  45.796 -12.747  1.00 76.27           O  
+ANISOU11827  OD1 ASN D 257     9735   9169  10075   1197   1203   1067       O  
+ATOM  11828  ND2 ASN D 257      -6.890  46.094 -11.196  1.00 91.31           N  
+ANISOU11828  ND2 ASN D 257    11732  10946  12015   1205   1148   1131       N  
+ATOM  11829  N   ILE D 258      -4.456  50.075 -13.974  1.00 50.68           N  
+ANISOU11829  N   ILE D 258     6671   6174   6410    711    935   1040       N  
+ATOM  11830  CA  ILE D 258      -5.155  50.758 -15.053  1.00 49.59           C  
+ANISOU11830  CA  ILE D 258     6641   5960   6242    637    896   1011       C  
+ATOM  11831  C   ILE D 258      -4.618  50.266 -16.387  1.00 50.60           C  
+ANISOU11831  C   ILE D 258     6719   6211   6296    653    969    996       C  
+ATOM  11832  O   ILE D 258      -3.502  50.606 -16.785  1.00 60.73           O  
+ANISOU11832  O   ILE D 258     7926   7652   7499    581    996   1059       O  
+ATOM  11833  CB  ILE D 258      -5.007  52.286 -14.966  1.00 52.51           C  
+ANISOU11833  CB  ILE D 258     7052   6308   6592    479    811   1067       C  
+ATOM  11834  CG1 ILE D 258      -5.542  52.796 -13.628  1.00 59.33           C  
+ANISOU11834  CG1 ILE D 258     7938   7079   7527    465    738   1023       C  
+ATOM  11835  CG2 ILE D 258      -5.736  52.958 -16.121  1.00 53.50           C  
+ANISOU11835  CG2 ILE D 258     7277   6360   6691    428    775   1096       C  
+ATOM  11836  CD1 ILE D 258      -5.427  54.289 -13.463  1.00 66.94           C  
+ANISOU11836  CD1 ILE D 258     8919   7978   8539    312    659   1030       C  
+ATOM  11837  N   LYS D 259      -5.419  49.464 -17.077  1.00 58.98           N  
+ANISOU11837  N   LYS D 259     7803   7221   7384    743   1003    888       N  
+ATOM  11838  CA  LYS D 259      -4.997  48.888 -18.344  1.00 57.70           C  
+ANISOU11838  CA  LYS D 259     7567   7215   7143    774   1075    814       C  
+ATOM  11839  C   LYS D 259      -5.038  49.945 -19.435  1.00 59.93           C  
+ANISOU11839  C   LYS D 259     7894   7622   7256    667   1031    887       C  
+ATOM  11840  O   LYS D 259      -6.044  50.636 -19.614  1.00 56.10           O  
+ANISOU11840  O   LYS D 259     7516   7042   6758    636    952    913       O  
+ATOM  11841  CB  LYS D 259      -5.882  47.699 -18.722  1.00 53.68           C  
+ANISOU11841  CB  LYS D 259     7039   6618   6738    899   1125    627       C  
+ATOM  11842  CG  LYS D 259      -5.531  47.055 -20.055  1.00 59.65           C  
+ANISOU11842  CG  LYS D 259     7689   7564   7413    940   1198    477       C  
+ATOM  11843  CD  LYS D 259      -4.356  46.098 -19.923  1.00 85.68           C  
+ANISOU11843  CD  LYS D 259    10833  10930  10792   1014   1304    435       C  
+ATOM  11844  CE  LYS D 259      -4.153  45.291 -21.199  1.00 97.00           C  
+ANISOU11844  CE  LYS D 259    12134  12537  12184   1075   1386    209       C  
+ATOM  11845  NZ  LYS D 259      -2.846  44.578 -21.207  1.00 91.68           N  
+ANISOU11845  NZ  LYS D 259    11297  11971  11565   1135   1485    176       N  
+ATOM  11846  N   THR D 260      -3.934  50.070 -20.159  1.00 70.54           N  
+ANISOU11846  N   THR D 260     9143   9187   8473    616   1088    941       N  
+ATOM  11847  CA  THR D 260      -3.850  51.040 -21.235  1.00 70.32           C  
+ANISOU11847  CA  THR D 260     9132   9313   8273    514   1068   1067       C  
+ATOM  11848  C   THR D 260      -4.083  50.363 -22.575  1.00 64.17           C  
+ANISOU11848  C   THR D 260     8282   8762   7337    589   1120    938       C  
+ATOM  11849  O   THR D 260      -3.413  49.390 -22.921  1.00 64.20           O  
+ANISOU11849  O   THR D 260     8156   8919   7320    656   1212    793       O  
+ATOM  11850  CB  THR D 260      -2.484  51.753 -21.262  1.00 60.88           C  
+ANISOU11850  CB  THR D 260     7856   8258   7017    385   1107   1231       C  
+ATOM  11851  OG1 THR D 260      -2.249  52.396 -20.003  1.00 62.62           O  
+ANISOU11851  OG1 THR D 260     8112   8298   7384    312   1053   1300       O  
+ATOM  11852  CG2 THR D 260      -2.452  52.796 -22.366  1.00 55.14           C  
+ANISOU11852  CG2 THR D 260     7144   7674   6135    276   1100   1421       C  
+ATOM  11853  N   ILE D 261      -5.036  50.894 -23.330  1.00 53.93           N  
+ANISOU11853  N   ILE D 261     7054   7505   5930    583   1057    976       N  
+ATOM  11854  CA  ILE D 261      -5.272  50.424 -24.679  1.00 55.28           C  
+ANISOU11854  CA  ILE D 261     7137   7972   5895    645   1092    854       C  
+ATOM  11855  C   ILE D 261      -4.722  51.456 -25.652  1.00 60.53           C  
+ANISOU11855  C   ILE D 261     7770   8908   6319    543   1100   1111       C  
+ATOM  11856  O   ILE D 261      -5.036  52.657 -25.584  1.00 61.71           O  
+ANISOU11856  O   ILE D 261     8020   8953   6474    458   1028   1369       O  
+ATOM  11857  CB  ILE D 261      -6.761  50.159 -24.950  1.00 62.99           C  
+ANISOU11857  CB  ILE D 261     8173   8878   6882    734   1019    700       C  
+ATOM  11858  CG1 ILE D 261      -7.271  49.048 -24.031  1.00 57.02           C  
+ANISOU11858  CG1 ILE D 261     7423   7855   6386    826   1039    459       C  
+ATOM  11859  CG2 ILE D 261      -6.969  49.741 -26.392  1.00 63.24           C  
+ANISOU11859  CG2 ILE D 261     8081   9286   6661    796   1045    551       C  
+ATOM  11860  CD1 ILE D 261      -8.731  49.173 -23.669  1.00 57.64           C  
+ANISOU11860  CD1 ILE D 261     7610   7720   6571    865    948    397       C  
+ATOM  11861  N   VAL D 262      -3.867  50.965 -26.539  1.00 60.88           N  
+ANISOU11861  N   VAL D 262     7657   9297   6175    554   1198   1042       N  
+ATOM  11862  CA  VAL D 262      -3.136  51.800 -27.469  1.00 64.94           C  
+ANISOU11862  CA  VAL D 262     8103  10125   6448    454   1242   1298       C  
+ATOM  11863  C   VAL D 262      -3.774  51.708 -28.849  1.00 61.76           C  
+ANISOU11863  C   VAL D 262     7626  10100   5738    524   1233   1256       C  
+ATOM  11864  O   VAL D 262      -3.755  50.655 -29.484  1.00 61.82           O  
+ANISOU11864  O   VAL D 262     7496  10368   5627    624   1289    948       O  
+ATOM  11865  CB  VAL D 262      -1.659  51.381 -27.535  1.00 60.27           C  
+ANISOU11865  CB  VAL D 262     7357   9728   5816    412   1365   1260       C  
+ATOM  11866  CG1 VAL D 262      -0.871  52.362 -28.363  1.00 62.80           C  
+ANISOU11866  CG1 VAL D 262     7605  10339   5916    280   1422   1573       C  
+ATOM  11867  CG2 VAL D 262      -1.079  51.295 -26.132  1.00 58.04           C  
+ANISOU11867  CG2 VAL D 262     7117   9117   5819    377   1363   1254       C  
+ATOM  11868  N   LEU D 263      -4.339  52.820 -29.302  1.00 58.45           N  
+ANISOU11868  N   LEU D 263     7285   9720   5205    477   1163   1560       N  
+ATOM  11869  CA  LEU D 263      -5.064  52.859 -30.564  1.00 65.92           C  
+ANISOU11869  CA  LEU D 263     8161  11052   5834    557   1131   1568       C  
+ATOM  11870  C   LEU D 263      -4.186  53.365 -31.701  1.00 84.22           C  
+ANISOU11870  C   LEU D 263    10336  13847   7818    491   1221   1831       C  
+ATOM  11871  O   LEU D 263      -3.124  53.945 -31.471  1.00 80.34           O  
+ANISOU11871  O   LEU D 263     9832  13312   7384    358   1296   2076       O  
+ATOM  11872  CB  LEU D 263      -6.309  53.736 -30.429  1.00 70.47           C  
+ANISOU11872  CB  LEU D 263     8887  11412   6475    578    994   1768       C  
+ATOM  11873  CG  LEU D 263      -7.229  53.404 -29.251  1.00 69.16           C  
+ANISOU11873  CG  LEU D 263     8865  10776   6637    627    906   1554       C  
+ATOM  11874  CD1 LEU D 263      -8.342  54.431 -29.131  1.00 64.34           C  
+ANISOU11874  CD1 LEU D 263     8388   9960   6097    638    776   1782       C  
+ATOM  11875  CD2 LEU D 263      -7.803  52.001 -29.391  1.00 62.59           C  
+ANISOU11875  CD2 LEU D 263     7951  10034   5798    759    916   1091       C  
+ATOM  11876  N   ASN D 264      -4.640  53.140 -32.930  1.00 96.78           N  
+ANISOU11876  N   ASN D 264    11800  15921   9049    583   1217   1772       N  
+ATOM  11877  CA  ASN D 264      -3.904  53.565 -34.113  1.00 87.54           C  
+ANISOU11877  CA  ASN D 264    10468  15296   7497    538   1307   2026       C  
+ATOM  11878  C   ASN D 264      -4.091  55.053 -34.380  1.00 71.78           C  
+ANISOU11878  C   ASN D 264     8558  13263   5452    454   1267   2610       C  
+ATOM  11879  O   ASN D 264      -3.212  55.709 -34.939  1.00 77.41           O  
+ANISOU11879  O   ASN D 264     9183  14230   6001    349   1366   2965       O  
+ATOM  11880  CB  ASN D 264      -4.348  52.755 -35.332  1.00 82.73           C  
+ANISOU11880  CB  ASN D 264     9661  15281   6490    680   1314   1722       C  
+ATOM  11881  CG  ASN D 264      -4.292  51.261 -35.089  1.00 82.91           C  
+ANISOU11881  CG  ASN D 264     9585  15282   6636    773   1353   1111       C  
+ATOM  11882  OD1 ASN D 264      -3.216  50.665 -35.048  1.00 84.17           O  
+ANISOU11882  OD1 ASN D 264     9625  15536   6820    743   1474    941       O  
+ATOM  11883  ND2 ASN D 264      -5.458  50.646 -34.922  1.00 73.96           N  
+ANISOU11883  ND2 ASN D 264     8487  14003   5610    887   1257    782       N  
+ATOM  11884  N   ASN D 265      -5.239  55.579 -33.965  1.00 70.58           N  
+ANISOU11884  N   ASN D 265     8567  12778   5471    501   1129   2714       N  
+ATOM  11885  CA  ASN D 265      -5.548  56.995 -34.132  1.00 74.19           C  
+ANISOU11885  CA  ASN D 265     9111  13110   5966    442   1079   3260       C  
+ATOM  11886  C   ASN D 265      -6.617  57.436 -33.136  1.00 78.51           C  
+ANISOU11886  C   ASN D 265     9862  13084   6883    471    936   3252       C  
+ATOM  11887  O   ASN D 265      -7.353  56.606 -32.603  1.00 94.45           O  
+ANISOU11887  O   ASN D 265    11934  14939   9013    567    865   2841       O  
+ATOM  11888  CB  ASN D 265      -6.001  57.276 -35.569  1.00 79.47           C  
+ANISOU11888  CB  ASN D 265     9644  14379   6171    541   1063   3503       C  
+ATOM  11889  CG  ASN D 265      -7.137  56.372 -36.013  1.00 82.32           C  
+ANISOU11889  CG  ASN D 265     9949  15009   6320    731    961   3090       C  
+ATOM  11890  OD1 ASN D 265      -8.295  56.596 -35.661  1.00 85.84           O  
+ANISOU11890  OD1 ASN D 265    10513  15187   6917    813    823   3067       O  
+ATOM  11891  ND2 ASN D 265      -6.810  55.343 -36.788  1.00 78.83           N  
+ANISOU11891  ND2 ASN D 265     9306  15103   5544    798   1031   2731       N  
+ATOM  11892  N   TYR D 266      -6.695  58.740 -32.881  1.00 73.21           N  
+ANISOU11892  N   TYR D 266     9289  12101   6425    385    903   3699       N  
+ATOM  11893  CA  TYR D 266      -7.620  59.274 -31.881  1.00 78.90           C  
+ANISOU11893  CA  TYR D 266    10188  12263   7527    400    776   3691       C  
+ATOM  11894  C   TYR D 266      -9.085  59.106 -32.246  1.00 78.63           C  
+ANISOU11894  C   TYR D 266    10183  12317   7375    582    635   3587       C  
+ATOM  11895  O   TYR D 266      -9.935  59.004 -31.365  1.00 82.23           O  
+ANISOU11895  O   TYR D 266    10759  12388   8096    629    536   3367       O  
+ATOM  11896  CB  TYR D 266      -7.339  60.753 -31.635  1.00 70.06           C  
+ANISOU11896  CB  TYR D 266     9131  10798   6690    269    783   4185       C  
+ATOM  11897  CG  TYR D 266      -6.084  61.004 -30.850  1.00 73.84           C  
+ANISOU11897  CG  TYR D 266     9608  11014   7433     74    890   4199       C  
+ATOM  11898  CD1 TYR D 266      -6.021  60.685 -29.503  1.00 70.33           C  
+ANISOU11898  CD1 TYR D 266     9257  10156   7311     30    858   3861       C  
+ATOM  11899  CD2 TYR D 266      -4.963  61.556 -31.451  1.00 72.11           C  
+ANISOU11899  CD2 TYR D 266     9276  10992   7129    -66   1024   4552       C  
+ATOM  11900  CE1 TYR D 266      -4.879  60.910 -28.773  1.00 68.09           C  
+ANISOU11900  CE1 TYR D 266     8947   9677   7248   -139    943   3851       C  
+ATOM  11901  CE2 TYR D 266      -3.813  61.786 -30.730  1.00 81.24           C  
+ANISOU11901  CE2 TYR D 266    10409  11923   8534   -250   1118   4538       C  
+ATOM  11902  CZ  TYR D 266      -3.777  61.461 -29.390  1.00 80.88           C  
+ANISOU11902  CZ  TYR D 266    10452  11483   8798   -281   1070   4176       C  
+ATOM  11903  OH  TYR D 266      -2.633  61.687 -28.665  1.00 83.64           O  
+ANISOU11903  OH  TYR D 266    10753  11653   9371   -455   1152   4142       O  
+ATOM  11904  N   ASN D 267      -9.385  59.101 -33.538  1.00 74.27           N  
+ANISOU11904  N   ASN D 267     9505  12302   6413    685    626   3747       N  
+ATOM  11905  CA  ASN D 267     -10.759  58.916 -33.986  1.00 72.17           C  
+ANISOU11905  CA  ASN D 267     9229  12201   5990    867    487   3634       C  
+ATOM  11906  C   ASN D 267     -11.302  57.551 -33.586  1.00 88.05           C  
+ANISOU11906  C   ASN D 267    11229  14213   8011    951    454   3004       C  
+ATOM  11907  O   ASN D 267     -12.515  57.360 -33.495  1.00 95.73           O  
+ANISOU11907  O   ASN D 267    12234  15121   9016   1072    332   2817       O  
+ATOM  11908  CB  ASN D 267     -10.881  59.117 -35.492  1.00 78.41           C  
+ANISOU11908  CB  ASN D 267     9847  13666   6281    967    487   3914       C  
+ATOM  11909  CG  ASN D 267     -10.903  60.577 -35.887  1.00101.63           C  
+ANISOU11909  CG  ASN D 267    12813  16537   9264    944    471   4598       C  
+ATOM  11910  OD1 ASN D 267     -10.504  60.939 -36.994  1.00109.50           O  
+ANISOU11910  OD1 ASN D 267    13665  18012   9927    954    528   4941       O  
+ATOM  11911  ND2 ASN D 267     -11.362  61.428 -34.977  1.00102.25           N  
+ANISOU11911  ND2 ASN D 267    13059  15988   9802    908    396   4763       N  
+ATOM  11912  N   GLU D 268     -10.401  56.588 -33.405  1.00 68.11           N  
+ANISOU11912  N   GLU D 268     8638  11776   5463    892    570   2686       N  
+ATOM  11913  CA  GLU D 268     -10.793  55.273 -32.914  1.00 85.33           C  
+ANISOU11913  CA  GLU D 268    10804  13872   7746    956    565   2114       C  
+ATOM  11914  C   GLU D 268     -11.452  55.383 -31.540  1.00 81.86           C  
+ANISOU11914  C   GLU D 268    10550  12809   7743    938    490   2004       C  
+ATOM  11915  O   GLU D 268     -12.254  54.530 -31.175  1.00 74.69           O  
+ANISOU11915  O   GLU D 268     9646  11795   6937   1017    447   1615       O  
+ATOM  11916  CB  GLU D 268      -9.610  54.305 -32.852  1.00 78.85           C  
+ANISOU11916  CB  GLU D 268     9881  13180   6899    896    710   1845       C  
+ATOM  11917  CG  GLU D 268      -9.021  53.907 -34.195  1.00 80.56           C  
+ANISOU11917  CG  GLU D 268     9875  14066   6669    932    794   1804       C  
+ATOM  11918  CD  GLU D 268      -8.152  52.670 -34.082  1.00 83.40           C  
+ANISOU11918  CD  GLU D 268    10113  14517   7057    921    918   1380       C  
+ATOM  11919  OE1 GLU D 268      -7.695  52.373 -32.959  1.00 77.27           O  
+ANISOU11919  OE1 GLU D 268     9437  13287   6635    856    957   1279       O  
+ATOM  11920  OE2 GLU D 268      -7.941  51.982 -35.103  1.00 81.42           O  
+ANISOU11920  OE2 GLU D 268     9652  14803   6479    989    974   1138       O  
+ATOM  11921  N   ILE D 269     -11.040  56.362 -30.738  1.00 77.52           N  
+ANISOU11921  N   ILE D 269    10132  11855   7467    823    491   2312       N  
+ATOM  11922  CA  ILE D 269     -11.748  56.672 -29.493  1.00 74.26           C  
+ANISOU11922  CA  ILE D 269     9879  10905   7433    813    408   2243       C  
+ATOM  11923  C   ILE D 269     -13.237  56.893 -29.777  1.00 75.97           C  
+ANISOU11923  C   ILE D 269    10121  11128   7618    948    267   2216       C  
+ATOM  11924  O   ILE D 269     -14.111  56.241 -29.188  1.00 76.30           O  
+ANISOU11924  O   ILE D 269    10199  10994   7799   1014    214   1880       O  
+ATOM  11925  CB  ILE D 269     -11.187  57.918 -28.792  1.00 68.60           C  
+ANISOU11925  CB  ILE D 269     9263   9812   6991    676    414   2595       C  
+ATOM  11926  CG1 ILE D 269      -9.734  57.698 -28.368  1.00 70.07           C  
+ANISOU11926  CG1 ILE D 269     9413   9971   7238    537    544   2586       C  
+ATOM  11927  CG2 ILE D 269     -12.039  58.266 -27.587  1.00 59.24           C  
+ANISOU11927  CG2 ILE D 269     8213   8136   6158    684    318   2488       C  
+ATOM  11928  CD1 ILE D 269      -9.113  58.909 -27.701  1.00 70.26           C  
+ANISOU11928  CD1 ILE D 269     9503   9646   7547    385    557   2886       C  
+ATOM  11929  N   THR D 270     -13.508  57.844 -30.670  1.00 71.05           N  
+ANISOU11929  N   THR D 270     9468  10706   6820    990    211   2599       N  
+ATOM  11930  CA  THR D 270     -14.867  58.161 -31.101  1.00 69.46           C  
+ANISOU11930  CA  THR D 270     9263  10583   6546   1138     69   2636       C  
+ATOM  11931  C   THR D 270     -15.584  56.903 -31.585  1.00 68.54           C  
+ANISOU11931  C   THR D 270     9031  10809   6203   1260     41   2172       C  
+ATOM  11932  O   THR D 270     -16.758  56.703 -31.286  1.00 64.30           O  
+ANISOU11932  O   THR D 270     8519  10142   5769   1352    -61   1956       O  
+ATOM  11933  CB  THR D 270     -14.888  59.241 -32.207  1.00 75.41           C  
+ANISOU11933  CB  THR D 270     9956  11628   7070   1186     32   3162       C  
+ATOM  11934  OG1 THR D 270     -14.196  60.410 -31.752  1.00 75.95           O  
+ANISOU11934  OG1 THR D 270    10114  11326   7417   1055     73   3583       O  
+ATOM  11935  CG2 THR D 270     -16.316  59.630 -32.534  1.00 68.47           C  
+ANISOU11935  CG2 THR D 270     9072  10791   6154   1354   -130   3217       C  
+ATOM  11936  N   GLU D 271     -14.889  56.093 -32.380  1.00 64.28           N  
+ANISOU11936  N   GLU D 271     8342  10721   5359   1260    135   2011       N  
+ATOM  11937  CA  GLU D 271     -15.460  54.871 -32.951  1.00 73.24           C  
+ANISOU11937  CA  GLU D 271     9324  12216   6288   1366    124   1529       C  
+ATOM  11938  C   GLU D 271     -15.894  53.895 -31.854  1.00 69.21           C  
+ANISOU11938  C   GLU D 271     8876  11295   6124   1352    139   1068       C  
+ATOM  11939  O   GLU D 271     -16.960  53.276 -31.935  1.00 67.12           O  
+ANISOU11939  O   GLU D 271     8551  11081   5872   1444     72    729       O  
+ATOM  11940  CB  GLU D 271     -14.465  54.200 -33.892  1.00 70.34           C  
+ANISOU11940  CB  GLU D 271     8774  12367   5583   1352    243   1413       C  
+ATOM  11941  CG  GLU D 271     -15.041  53.011 -34.632  1.00 85.88           C  
+ANISOU11941  CG  GLU D 271    10541  14761   7328   1463    231    891       C  
+ATOM  11942  CD  GLU D 271     -14.027  52.367 -35.545  1.00111.38           C  
+ANISOU11942  CD  GLU D 271    13570  18514  10235   1452    353    741       C  
+ATOM  11943  OE1 GLU D 271     -12.980  53.000 -35.804  1.00112.41           O  
+ANISOU11943  OE1 GLU D 271    13708  18770  10231   1372    432   1125       O  
+ATOM  11944  OE2 GLU D 271     -14.283  51.241 -36.019  1.00119.76           O  
+ANISOU11944  OE2 GLU D 271    14448  19865  11190   1520    376    222       O  
+ATOM  11945  N   ILE D 272     -15.020  53.721 -30.867  1.00 64.55           N  
+ANISOU11945  N   ILE D 272     8383  10338   5805   1236    237   1062       N  
+ATOM  11946  CA  ILE D 272     -15.288  52.881 -29.704  1.00 65.10           C  
+ANISOU11946  CA  ILE D 272     8517   9999   6218   1215    268    724       C  
+ATOM  11947  C   ILE D 272     -16.539  53.366 -28.966  1.00 65.59           C  
+ANISOU11947  C   ILE D 272     8698   9716   6507   1254    149    734       C  
+ATOM  11948  O   ILE D 272     -17.429  52.578 -28.618  1.00 67.01           O  
+ANISOU11948  O   ILE D 272     8852   9786   6822   1307    130    389       O  
+ATOM  11949  CB  ILE D 272     -14.088  52.868 -28.737  1.00 66.43           C  
+ANISOU11949  CB  ILE D 272     8769   9865   6605   1093    375    820       C  
+ATOM  11950  CG1 ILE D 272     -12.905  52.111 -29.345  1.00 70.91           C  
+ANISOU11950  CG1 ILE D 272     9198  10745   6999   1068    505    705       C  
+ATOM  11951  CG2 ILE D 272     -14.474  52.235 -27.418  1.00 64.05           C  
+ANISOU11951  CG2 ILE D 272     8549   9131   6655   1082    391    581       C  
+ATOM  11952  CD1 ILE D 272     -11.578  52.402 -28.663  1.00 72.99           C  
+ANISOU11952  CD1 ILE D 272     9517  10825   7391    947    596    905       C  
+ATOM  11953  N   LEU D 273     -16.584  54.672 -28.714  1.00 70.55           N  
+ANISOU11953  N   LEU D 273     9443  10158   7206   1222     80   1125       N  
+ATOM  11954  CA  LEU D 273     -17.716  55.292 -28.024  1.00 75.94           C  
+ANISOU11954  CA  LEU D 273    10229  10514   8112   1263    -35   1157       C  
+ATOM  11955  C   LEU D 273     -19.023  55.078 -28.801  1.00 78.77           C  
+ANISOU11955  C   LEU D 273    10492  11133   8303   1407   -146    995       C  
+ATOM  11956  O   LEU D 273     -20.070  54.790 -28.216  1.00 88.72           O  
+ANISOU11956  O   LEU D 273    11775  12191   9744   1453   -203    758       O  
+ATOM  11957  CB  LEU D 273     -17.449  56.781 -27.804  1.00 63.39           C  
+ANISOU11957  CB  LEU D 273     8745   8705   6636   1210    -84   1607       C  
+ATOM  11958  CG  LEU D 273     -16.332  57.135 -26.821  1.00 63.89           C  
+ANISOU11958  CG  LEU D 273     8897   8447   6932   1060      3   1726       C  
+ATOM  11959  CD1 LEU D 273     -16.186  58.645 -26.680  1.00 65.25           C  
+ANISOU11959  CD1 LEU D 273     9144   8382   7267   1006    -48   2132       C  
+ATOM  11960  CD2 LEU D 273     -16.592  56.488 -25.472  1.00 60.45           C  
+ANISOU11960  CD2 LEU D 273     8524   7678   6765   1031     26   1413       C  
+ATOM  11961  N   GLN D 274     -18.950  55.277 -30.116  1.00 68.98           N  
+ANISOU11961  N   GLN D 274     9133  10373   6705   1478   -178   1141       N  
+ATOM  11962  CA  GLN D 274     -20.069  55.056 -31.033  1.00 75.39           C  
+ANISOU11962  CA  GLN D 274     9808  11559   7276   1625   -287    985       C  
+ATOM  11963  C   GLN D 274     -20.571  53.624 -30.898  1.00 72.69           C  
+ANISOU11963  C   GLN D 274     9361  11267   6991   1646   -247    409       C  
+ATOM  11964  O   GLN D 274     -21.775  53.371 -30.880  1.00 81.46           O  
+ANISOU11964  O   GLN D 274    10421  12379   8153   1730   -336    168       O  
+ATOM  11965  CB  GLN D 274     -19.666  55.336 -32.487  1.00 71.40           C  
+ANISOU11965  CB  GLN D 274     9155  11658   6316   1690   -298   1215       C  
+ATOM  11966  CG  GLN D 274     -19.822  56.788 -32.938  1.00 76.86           C  
+ANISOU11966  CG  GLN D 274     9893  12396   6916   1745   -392   1791       C  
+ATOM  11967  CD  GLN D 274     -19.040  57.105 -34.206  1.00 90.12           C  
+ANISOU11967  CD  GLN D 274    11441  14633   8166   1764   -349   2121       C  
+ATOM  11968  OE1 GLN D 274     -18.366  56.240 -34.765  1.00 99.05           O  
+ANISOU11968  OE1 GLN D 274    12441  16146   9046   1738   -252   1884       O  
+ATOM  11969  NE2 GLN D 274     -19.144  58.346 -34.674  1.00 85.95           N  
+ANISOU11969  NE2 GLN D 274    10932  14163   7561   1818   -416   2677       N  
+ATOM  11970  N   ARG D 275     -19.623  52.692 -30.882  1.00 71.75           N  
+ANISOU11970  N   ARG D 275     9186  11205   6870   1573   -108    194       N  
+ATOM  11971  CA  ARG D 275     -19.908  51.266 -30.755  1.00 78.10           C  
+ANISOU11971  CA  ARG D 275     9872  12010   7791   1580    -37   -342       C  
+ATOM  11972  C   ARG D 275     -20.681  50.981 -29.469  1.00 78.60           C  
+ANISOU11972  C   ARG D 275    10046  11556   8264   1552    -41   -508       C  
+ATOM  11973  O   ARG D 275     -21.654  50.221 -29.468  1.00 78.66           O  
+ANISOU11973  O   ARG D 275     9954  11562   8371   1598    -60   -883       O  
+ATOM  11974  CB  ARG D 275     -18.605  50.467 -30.779  1.00 72.22           C  
+ANISOU11974  CB  ARG D 275     9073  11315   7051   1505    122   -463       C  
+ATOM  11975  CG  ARG D 275     -18.782  48.967 -30.651  1.00 76.87           C  
+ANISOU11975  CG  ARG D 275     9525  11854   7827   1511    216  -1002       C  
+ATOM  11976  CD  ARG D 275     -18.915  48.303 -32.010  1.00 73.80           C  
+ANISOU11976  CD  ARG D 275     8880  12036   7125   1589    214  -1347       C  
+ATOM  11977  NE  ARG D 275     -18.918  46.847 -31.901  1.00 73.85           N  
+ANISOU11977  NE  ARG D 275     8733  11952   7373   1583    327  -1880       N  
+ATOM  11978  CZ  ARG D 275     -17.823  46.099 -31.807  1.00 84.84           C  
+ANISOU11978  CZ  ARG D 275    10069  13294   8871   1539    472  -2007       C  
+ATOM  11979  NH1 ARG D 275     -16.624  46.666 -31.811  1.00 88.85           N  
+ANISOU11979  NH1 ARG D 275    10659  13865   9236   1490    520  -1652       N  
+ATOM  11980  NH2 ARG D 275     -17.925  44.780 -31.709  1.00106.18           N  
+ANISOU11980  NH2 ARG D 275    12619  15870  11854   1545    574  -2491       N  
+ATOM  11981  N   ILE D 276     -20.203  51.569 -28.373  1.00 79.82           N  
+ANISOU11981  N   ILE D 276    10383  11294   8651   1468    -12   -240       N  
+ATOM  11982  CA  ILE D 276     -20.830  51.427 -27.057  1.00 79.75           C  
+ANISOU11982  CA  ILE D 276    10480  10823   8998   1436     -7   -339       C  
+ATOM  11983  C   ILE D 276     -22.265  51.961 -27.086  1.00 73.68           C  
+ANISOU11983  C   ILE D 276     9715  10029   8252   1520   -150   -366       C  
+ATOM  11984  O   ILE D 276     -23.203  51.309 -26.605  1.00 72.94           O  
+ANISOU11984  O   ILE D 276     9580   9784   8348   1538   -148   -665       O  
+ATOM  11985  CB  ILE D 276     -20.018  52.163 -25.972  1.00 69.64           C  
+ANISOU11985  CB  ILE D 276     9371   9193   7897   1339     29    -31       C  
+ATOM  11986  CG1 ILE D 276     -18.661  51.483 -25.781  1.00 68.67           C  
+ANISOU11986  CG1 ILE D 276     9229   9070   7793   1263    173    -51       C  
+ATOM  11987  CG2 ILE D 276     -20.784  52.211 -24.655  1.00 70.09           C  
+ANISOU11987  CG2 ILE D 276     9521   8848   8261   1321     13   -106       C  
+ATOM  11988  CD1 ILE D 276     -17.690  52.276 -24.946  1.00 66.47           C  
+ANISOU11988  CD1 ILE D 276     9079   8561   7618   1166    202    255       C  
+ATOM  11989  N   GLU D 277     -22.420  53.158 -27.655  1.00 71.76           N  
+ANISOU11989  N   GLU D 277     9507   9928   7831   1574   -267    -35       N  
+ATOM  11990  CA  GLU D 277     -23.724  53.809 -27.771  1.00 70.72           C  
+ANISOU11990  CA  GLU D 277     9369   9795   7708   1677   -417     -5       C  
+ATOM  11991  C   GLU D 277     -24.683  52.926 -28.549  1.00 72.47           C  
+ANISOU11991  C   GLU D 277     9401  10348   7787   1770   -460   -397       C  
+ATOM  11992  O   GLU D 277     -25.856  52.808 -28.203  1.00 73.17           O  
+ANISOU11992  O   GLU D 277     9460  10324   8018   1819   -528   -599       O  
+ATOM  11993  CB  GLU D 277     -23.602  55.166 -28.463  1.00 68.94           C  
+ANISOU11993  CB  GLU D 277     9176   9718   7298   1738   -524    454       C  
+ATOM  11994  CG  GLU D 277     -24.940  55.870 -28.651  1.00 68.90           C  
+ANISOU11994  CG  GLU D 277     9147   9728   7304   1872   -688    512       C  
+ATOM  11995  CD  GLU D 277     -24.809  57.235 -29.298  1.00 84.58           C  
+ANISOU11995  CD  GLU D 277    11161  11813   9163   1944   -785   1022       C  
+ATOM  11996  OE1 GLU D 277     -25.768  58.030 -29.206  1.00 88.55           O  
+ANISOU11996  OE1 GLU D 277    11677  12196   9771   2048   -915   1150       O  
+ATOM  11997  OE2 GLU D 277     -23.748  57.512 -29.897  1.00101.96           O  
+ANISOU11997  OE2 GLU D 277    13360  14203  11177   1899   -725   1307       O  
+ATOM  11998  N   ASN D 278     -24.176  52.359 -29.639  1.00 73.04           N  
+ANISOU11998  N   ASN D 278     9324  10860   7566   1793   -424   -512       N  
+ATOM  11999  CA  ASN D 278     -24.923  51.413 -30.452  1.00 76.69           C  
+ANISOU11999  CA  ASN D 278     9566  11690   7883   1867   -449   -955       C  
+ATOM  12000  C   ASN D 278     -25.393  50.267 -29.576  1.00 76.06           C  
+ANISOU12000  C   ASN D 278     9459  11274   8165   1802   -354  -1390       C  
+ATOM  12001  O   ASN D 278     -26.568  49.897 -29.589  1.00 91.25           O  
+ANISOU12001  O   ASN D 278    11278  13218  10175   1852   -413  -1691       O  
+ATOM  12002  CB  ASN D 278     -24.068  50.885 -31.598  1.00 73.86           C  
+ANISOU12002  CB  ASN D 278     9046  11828   7188   1878   -389  -1056       C  
+ATOM  12003  CG  ASN D 278     -24.873  50.104 -32.612  1.00 83.77           C  
+ANISOU12003  CG  ASN D 278    10035  13563   8229   1972   -443  -1512       C  
+ATOM  12004  OD1 ASN D 278     -25.707  50.659 -33.328  1.00 90.15           O  
+ANISOU12004  OD1 ASN D 278    10750  14720   8784   2094   -594  -1445       O  
+ATOM  12005  ND2 ASN D 278     -24.650  48.796 -32.655  1.00 94.25           N  
+ANISOU12005  ND2 ASN D 278    11221  14904   9684   1920   -322  -1997       N  
+ATOM  12006  N   ASN D 279     -24.444  49.681 -28.850  1.00 73.90           N  
+ANISOU12006  N   ASN D 279     9262  10712   8105   1694   -200  -1411       N  
+ATOM  12007  CA  ASN D 279     -24.740  48.575 -27.953  1.00 76.00           C  
+ANISOU12007  CA  ASN D 279     9505  10629   8744   1629    -83  -1744       C  
+ATOM  12008  C   ASN D 279     -25.859  48.936 -26.983  1.00 72.72           C  
+ANISOU12008  C   ASN D 279     9176   9880   8575   1630   -142  -1729       C  
+ATOM  12009  O   ASN D 279     -26.645  48.075 -26.597  1.00 71.43           O  
+ANISOU12009  O   ASN D 279     8921   9566   8654   1613    -91  -2063       O  
+ATOM  12010  CB  ASN D 279     -23.492  48.139 -27.178  1.00 82.43           C  
+ANISOU12010  CB  ASN D 279    10416  11162   9744   1531     74  -1637       C  
+ATOM  12011  CG  ASN D 279     -22.505  47.374 -28.040  1.00 83.55           C  
+ANISOU12011  CG  ASN D 279    10418  11590   9737   1527    169  -1805       C  
+ATOM  12012  OD1 ASN D 279     -22.828  46.959 -29.153  1.00 95.92           O  
+ANISOU12012  OD1 ASN D 279    11792  13555  11099   1588    136  -2090       O  
+ATOM  12013  ND2 ASN D 279     -21.302  47.162 -27.518  1.00 84.98           N  
+ANISOU12013  ND2 ASN D 279    10676  11595  10019   1460    287  -1656       N  
+ATOM  12014  N   ILE D 280     -25.949  50.208 -26.601  1.00 73.71           N  
+ANISOU12014  N   ILE D 280     9459   9888   8658   1649   -242  -1354       N  
+ATOM  12015  CA  ILE D 280     -27.012  50.598 -25.683  1.00 72.67           C  
+ANISOU12015  CA  ILE D 280     9393   9464   8753   1659   -300  -1361       C  
+ATOM  12016  C   ILE D 280     -28.341  50.770 -26.417  1.00 76.83           C  
+ANISOU12016  C   ILE D 280     9784  10246   9163   1773   -443  -1542       C  
+ATOM  12017  O   ILE D 280     -29.343  50.167 -26.037  1.00 90.92           O  
+ANISOU12017  O   ILE D 280    11480  11922  11141   1770   -431  -1850       O  
+ATOM  12018  CB  ILE D 280     -26.696  51.903 -24.936  1.00 74.70           C  
+ANISOU12018  CB  ILE D 280     9845   9473   9065   1642   -355   -953       C  
+ATOM  12019  CG1 ILE D 280     -25.387  51.769 -24.158  1.00 72.12           C  
+ANISOU12019  CG1 ILE D 280     9634   8924   8844   1530   -223   -791       C  
+ATOM  12020  CG2 ILE D 280     -27.842  52.254 -23.999  1.00 70.77           C  
+ANISOU12020  CG2 ILE D 280     9385   8707   8798   1660   -410  -1019       C  
+ATOM  12021  CD1 ILE D 280     -25.423  50.707 -23.071  1.00 76.56           C  
+ANISOU12021  CD1 ILE D 280    10191   9213   9686   1456    -82  -1008       C  
+ATOM  12022  N   LYS D 281     -28.355  51.593 -27.460  1.00 74.62           N  
+ANISOU12022  N   LYS D 281     9469  10315   8567   1875   -577  -1335       N  
+ATOM  12023  CA  LYS D 281     -29.612  51.975 -28.090  1.00 76.30           C  
+ANISOU12023  CA  LYS D 281     9561  10779   8652   2008   -740  -1425       C  
+ATOM  12024  C   LYS D 281     -30.258  50.833 -28.866  1.00 74.04           C  
+ANISOU12024  C   LYS D 281     9026  10830   8276   2039   -734  -1924       C  
+ATOM  12025  O   LYS D 281     -31.475  50.818 -29.043  1.00 81.41           O  
+ANISOU12025  O   LYS D 281     9835  11876   9222   2118   -837  -2139       O  
+ATOM  12026  CB  LYS D 281     -29.411  53.184 -29.010  1.00 87.30           C  
+ANISOU12026  CB  LYS D 281    10972  12474   9726   2124   -880  -1006       C  
+ATOM  12027  CG  LYS D 281     -30.420  54.291 -28.722  1.00 94.82           C  
+ANISOU12027  CG  LYS D 281    11974  13284  10769   2231  -1035   -800       C  
+ATOM  12028  CD  LYS D 281     -30.137  55.566 -29.499  1.00 94.86           C  
+ANISOU12028  CD  LYS D 281    12013  13491  10540   2343  -1155   -297       C  
+ATOM  12029  CE  LYS D 281     -31.071  56.691 -29.069  1.00 91.39           C  
+ANISOU12029  CE  LYS D 281    11631  12811  10283   2450  -1296    -84       C  
+ATOM  12030  NZ  LYS D 281     -30.783  57.944 -29.821  1.00 99.27           N  
+ANISOU12030  NZ  LYS D 281    12653  13956  11109   2564  -1401    453       N  
+ATOM  12031  N   THR D 282     -29.455  49.872 -29.314  1.00 74.32           N  
+ANISOU12031  N   THR D 282     8970  11023   8246   1978   -614  -2139       N  
+ATOM  12032  CA  THR D 282     -29.985  48.752 -30.089  1.00 77.26           C  
+ANISOU12032  CA  THR D 282     9075  11715   8563   1998   -597  -2669       C  
+ATOM  12033  C   THR D 282     -30.621  47.675 -29.217  1.00 76.21           C  
+ANISOU12033  C   THR D 282     8883  11206   8868   1902   -478  -3074       C  
+ATOM  12034  O   THR D 282     -31.064  46.643 -29.722  1.00 81.92           O  
+ANISOU12034  O   THR D 282     9373  12102   9651   1892   -437  -3563       O  
+ATOM  12035  CB  THR D 282     -28.896  48.086 -30.959  1.00 82.70           C  
+ANISOU12035  CB  THR D 282     9651  12733   9039   1975   -506  -2803       C  
+ATOM  12036  OG1 THR D 282     -27.821  47.630 -30.125  1.00 91.07           O  
+ANISOU12036  OG1 THR D 282    10853  13393  10358   1851   -331  -2714       O  
+ATOM  12037  CG2 THR D 282     -28.357  49.062 -31.997  1.00 80.40           C  
+ANISOU12037  CG2 THR D 282     9361  12918   8268   2074   -617  -2427       C  
+ATOM  12038  N   LYS D 283     -30.659  47.914 -27.910  1.00 72.26           N  
+ANISOU12038  N   LYS D 283     8574  10204   8678   1830   -415  -2874       N  
+ATOM  12039  CA  LYS D 283     -31.253  46.963 -26.978  1.00 82.43           C  
+ANISOU12039  CA  LYS D 283     9814  11120  10384   1736   -286  -3171       C  
+ATOM  12040  C   LYS D 283     -32.667  47.368 -26.565  1.00 94.05           C  
+ANISOU12040  C   LYS D 283    11254  12512  11970   1777   -386  -3250       C  
+ATOM  12041  O   LYS D 283     -33.346  46.627 -25.854  1.00102.20           O  
+ANISOU12041  O   LYS D 283    12216  13280  13337   1703   -287  -3502       O  
+ATOM  12042  CB  LYS D 283     -30.370  46.817 -25.736  1.00 67.97           C  
+ANISOU12042  CB  LYS D 283     8180   8833   8814   1628   -130  -2920       C  
+ATOM  12043  N   THR D 284     -33.101  48.551 -26.990  1.00 84.25           N  
+ANISOU12043  N   THR D 284    10054  11487  10469   1899   -575  -3015       N  
+ATOM  12044  CA  THR D 284     -34.490  48.963 -26.810  1.00 75.18           C  
+ANISOU12044  CA  THR D 284     8833  10344   9387   1970   -696  -3124       C  
+ATOM  12045  C   THR D 284     -35.199  49.108 -28.156  1.00 77.84           C  
+ANISOU12045  C   THR D 284     8948  11225   9401   2112   -869  -3316       C  
+ATOM  12046  O   THR D 284     -34.819  49.944 -28.977  1.00 71.89           O  
+ANISOU12046  O   THR D 284     8223  10793   8297   2226   -997  -3024       O  
+ATOM  12047  CB  THR D 284     -34.593  50.285 -26.029  1.00 70.99           C  
+ANISOU12047  CB  THR D 284     8515   9568   8890   2016   -783  -2698       C  
+ATOM  12048  OG1 THR D 284     -34.121  50.086 -24.690  1.00 81.40           O  
+ANISOU12048  OG1 THR D 284     9994  10429  10504   1887   -627  -2592       O  
+ATOM  12049  CG2 THR D 284     -36.032  50.760 -25.978  1.00 68.26           C  
+ANISOU12049  CG2 THR D 284     8070   9278   8589   2116   -923  -2819       C  
+ATOM  12050  N   VAL D 285     -36.226  48.294 -28.381  1.00 80.90           N  
+ANISOU12050  N   VAL D 285     9099  11733   9906   2105   -869  -3799       N  
+ATOM  12051  CA  VAL D 285     -36.899  48.258 -29.675  1.00 70.73           C  
+ANISOU12051  CA  VAL D 285     7552  11022   8303   2235  -1027  -4067       C  
+ATOM  12052  C   VAL D 285     -38.254  48.964 -29.633  1.00 75.73           C  
+ANISOU12052  C   VAL D 285     8106  11749   8918   2358  -1202  -4078       C  
+ATOM  12053  O   VAL D 285     -39.021  48.808 -28.684  1.00 73.32           O  
+ANISOU12053  O   VAL D 285     7815  11093   8950   2295  -1151  -4203       O  
+ATOM  12054  CB  VAL D 285     -37.097  46.805 -30.159  1.00 70.55           C  
+ANISOU12054  CB  VAL D 285     7250  11153   8403   2148   -918  -4689       C  
+ATOM  12055  CG1 VAL D 285     -37.676  46.779 -31.566  1.00 80.42           C  
+ANISOU12055  CG1 VAL D 285     8203  13088   9265   2287  -1089  -4993       C  
+ATOM  12056  CG2 VAL D 285     -35.779  46.049 -30.112  1.00 70.88           C  
+ANISOU12056  CG2 VAL D 285     7357  11046   8529   2032   -732  -4700       C  
+ATOM  12057  N   PHE D 286     -38.532  49.742 -30.675  1.00 80.20           N  
+ANISOU12057  N   PHE D 286     8578  12812   9081   2544  -1407  -3927       N  
+ATOM  12058  CA  PHE D 286     -39.831  50.374 -30.868  1.00 70.65           C  
+ANISOU12058  CA  PHE D 286     7240  11798   7805   2699  -1598  -3962       C  
+ATOM  12059  C   PHE D 286     -40.680  49.557 -31.832  1.00 86.68           C  
+ANISOU12059  C   PHE D 286     8905  14349   9682   2748  -1672  -4532       C  
+ATOM  12060  O   PHE D 286     -40.294  49.336 -32.982  1.00 81.62           O  
+ANISOU12060  O   PHE D 286     8101  14244   8666   2817  -1729  -4634       O  
+ATOM  12061  CB  PHE D 286     -39.652  51.803 -31.388  1.00 71.84           C  
+ANISOU12061  CB  PHE D 286     7500  12166   7632   2895  -1785  -3392       C  
+ATOM  12062  CG  PHE D 286     -40.935  52.479 -31.773  1.00 74.37           C  
+ANISOU12062  CG  PHE D 286     7657  12764   7836   3097  -2004  -3396       C  
+ATOM  12063  CD1 PHE D 286     -41.864  52.838 -30.812  1.00 78.87           C  
+ANISOU12063  CD1 PHE D 286     8274  12955   8738   3103  -2028  -3427       C  
+ATOM  12064  CD2 PHE D 286     -41.200  52.783 -33.098  1.00 78.30           C  
+ANISOU12064  CD2 PHE D 286     7942  13935   7874   3293  -2188  -3354       C  
+ATOM  12065  CE1 PHE D 286     -43.042  53.468 -31.169  1.00 75.55           C  
+ANISOU12065  CE1 PHE D 286     7691  12792   8223   3302  -2233  -3434       C  
+ATOM  12066  CE2 PHE D 286     -42.374  53.416 -33.458  1.00 86.72           C  
+ANISOU12066  CE2 PHE D 286     8845  15278   8828   3500  -2398  -3332       C  
+ATOM  12067  CZ  PHE D 286     -43.296  53.757 -32.492  1.00 79.46           C  
+ANISOU12067  CZ  PHE D 286     7975  13943   8272   3505  -2422  -3378       C  
+ATOM  12068  N   LEU D 287     -41.838  49.106 -31.360  1.00 90.10           N  
+ANISOU12068  N   LEU D 287     9187  14648  10400   2708  -1666  -4922       N  
+ATOM  12069  CA  LEU D 287     -42.744  48.332 -32.197  1.00 85.93           C  
+ANISOU12069  CA  LEU D 287     8282  14591   9777   2742  -1736  -5517       C  
+ATOM  12070  C   LEU D 287     -43.833  49.222 -32.786  1.00 89.43           C  
+ANISOU12070  C   LEU D 287     8568  15469   9941   2975  -1998  -5442       C  
+ATOM  12071  O   LEU D 287     -44.778  49.611 -32.101  1.00 99.59           O  
+ANISOU12071  O   LEU D 287     9865  16516  11458   3005  -2048  -5434       O  
+ATOM  12072  CB  LEU D 287     -43.364  47.183 -31.400  1.00 83.68           C  
+ANISOU12072  CB  LEU D 287     7876  13918  10000   2542  -1555  -6035       C  
+ATOM  12073  CG  LEU D 287     -42.381  46.089 -30.975  1.00 84.85           C  
+ANISOU12073  CG  LEU D 287     8096  13681  10462   2301  -1296  -6114       C  
+ATOM  12074  CD1 LEU D 287     -43.095  44.964 -30.245  1.00 83.70           C  
+ANISOU12074  CD1 LEU D 287     7801  13121  10882   2014  -1129  -6274       C  
+ATOM  12075  CD2 LEU D 287     -41.613  45.555 -32.174  1.00 77.59           C  
+ANISOU12075  CD2 LEU D 287     7012  13215   9254   2307  -1300  -6272       C  
+ATOM  12076  N   SER D 288     -43.683  49.534 -34.068  1.00 83.80           N  
+ANISOU12076  N   SER D 288     7693  15425   8720   3148  -2163  -5381       N  
+ATOM  12077  CA  SER D 288     -44.618  50.390 -34.786  1.00 87.04           C  
+ANISOU12077  CA  SER D 288     7930  16344   8798   3405  -2428  -5255       C  
+ATOM  12078  C   SER D 288     -45.617  49.556 -35.575  1.00 90.83           C  
+ANISOU12078  C   SER D 288     7975  17383   9154   3441  -2516  -5946       C  
+ATOM  12079  O   SER D 288     -45.235  48.591 -36.229  1.00116.75           O  
+ANISOU12079  O   SER D 288    11059  20975  12327   3352  -2434  -6380       O  
+ATOM  12080  CB  SER D 288     -43.862  51.329 -35.726  1.00 88.92           C  
+ANISOU12080  CB  SER D 288     8238  17027   8521   3596  -2562  -4691       C  
+ATOM  12081  OG  SER D 288     -44.756  52.080 -36.527  1.00 92.72           O  
+ANISOU12081  OG  SER D 288     8512  18069   8651   3866  -2820  -4561       O  
+ATOM  12082  N   GLY D 289     -46.895  49.920 -35.514  1.00 96.43           N  
+ANISOU12082  N   GLY D 289     8517  18218   9905   3567  -2673  -6070       N  
+ATOM  12083  CA  GLY D 289     -47.891  49.226 -36.307  1.00 96.44           C  
+ANISOU12083  CA  GLY D 289     8114  18689   9840   3601  -2680  -6615       C  
+ATOM  12084  C   GLY D 289     -49.317  49.269 -35.794  1.00110.17           C  
+ANISOU12084  C   GLY D 289     9704  20283  11871   3628  -2726  -6870       C  
+ATOM  12085  O   GLY D 289     -49.564  49.304 -34.589  1.00112.61           O  
+ANISOU12085  O   GLY D 289    10166  20033  12588   3511  -2693  -6898       O  
+ATOM  12086  N   SER D 290     -50.259  49.269 -36.733  1.00101.47           N  
+ANISOU12086  N   SER D 290     8305  19710  10541   3782  -2786  -7062       N  
+ATOM  12087  CA  SER D 290     -51.681  49.185 -36.423  1.00123.28           C  
+ANISOU12087  CA  SER D 290    10869  22425  13546   3811  -2807  -7380       C  
+ATOM  12088  C   SER D 290     -52.373  48.270 -37.427  1.00123.82           C  
+ANISOU12088  C   SER D 290    10512  22981  13553   3816  -2706  -7911       C  
+ATOM  12089  O   SER D 290     -51.908  48.116 -38.555  1.00127.11           O  
+ANISOU12089  O   SER D 290    10795  23918  13581   3896  -2702  -7915       O  
+ATOM  12090  CB  SER D 290     -52.325  50.574 -36.436  1.00114.92           C  
+ANISOU12090  CB  SER D 290     9920  21496  12249   4074  -3056  -6918       C  
+ATOM  12091  OG  SER D 290     -52.127  51.218 -37.682  1.00126.19           O  
+ANISOU12091  OG  SER D 290    11300  23531  13116   4298  -3179  -6568       O  
+ATOM  12092  N   ALA D 291     -53.474  47.651 -37.016  1.00103.32           N  
+ANISOU12092  N   ALA D 291     8891  18115  12252   1644  -1091  -5968       N  
+ATOM  12093  CA  ALA D 291     -54.189  46.727 -37.890  1.00105.97           C  
+ANISOU12093  CA  ALA D 291     8790  18956  12519   1394  -1219  -6663       C  
+ATOM  12094  C   ALA D 291     -55.660  46.612 -37.505  1.00107.69           C  
+ANISOU12094  C   ALA D 291     8480  19516  12922   1290  -1323  -6975       C  
+ATOM  12095  O   ALA D 291     -55.991  46.315 -36.357  1.00107.12           O  
+ANISOU12095  O   ALA D 291     8369  18996  13335   1066  -1085  -6935       O  
+ATOM  12096  CB  ALA D 291     -53.527  45.357 -37.864  1.00104.48           C  
+ANISOU12096  CB  ALA D 291     8696  18302  12701    930   -921  -7057       C  
+ATOM  12097  N   HIS D 296     -51.382  37.387 -47.104  1.00142.73           N  
+ANISOU12097  N   HIS D 296    13168  24360  16702  -1100   -146 -11194       N  
+ATOM  12098  CA  HIS D 296     -51.620  37.785 -45.721  1.00142.17           C  
+ANISOU12098  CA  HIS D 296    13104  23891  17021  -1045   -120 -10867       C  
+ATOM  12099  C   HIS D 296     -52.294  36.663 -44.935  1.00141.43           C  
+ANISOU12099  C   HIS D 296    12823  23302  17611  -1513    190 -11219       C  
+ATOM  12100  O   HIS D 296     -52.703  35.653 -45.503  1.00140.28           O  
+ANISOU12100  O   HIS D 296    12499  23202  17599  -1871    350 -11734       O  
+ATOM  12101  CB  HIS D 296     -52.425  39.082 -45.679  1.00146.67           C  
+ANISOU12101  CB  HIS D 296    13451  25141  17136   -691   -561 -10601       C  
+ATOM  12102  CG  HIS D 296     -51.704  40.241 -46.295  1.00147.37           C  
+ANISOU12102  CG  HIS D 296    13804  25601  16587   -207   -805 -10146       C  
+ATOM  12103  ND1 HIS D 296     -52.348  41.373 -46.745  1.00151.33           N  
+ANISOU12103  ND1 HIS D 296    14147  26845  16507    176  -1215  -9914       N  
+ATOM  12104  CD2 HIS D 296     -50.385  40.439 -46.529  1.00135.81           C  
+ANISOU12104  CD2 HIS D 296    12769  23846  14988    -34   -657  -9853       C  
+ATOM  12105  CE1 HIS D 296     -51.456  42.217 -47.235  1.00143.65           C  
+ANISOU12105  CE1 HIS D 296    13525  25998  15060    547  -1297  -9485       C  
+ATOM  12106  NE2 HIS D 296     -50.258  41.675 -47.115  1.00133.37           N  
+ANISOU12106  NE2 HIS D 296    12568  24092  14016    411   -958  -9459       N  
+ATOM  12107  N   TRP D 297     -52.414  36.862 -43.627  1.00138.18           N  
+ANISOU12107  N   TRP D 297    12470  22417  17614  -1512    292 -10933       N  
+ATOM  12108  CA  TRP D 297     -52.846  35.811 -42.709  1.00140.52           C  
+ANISOU12108  CA  TRP D 297    12707  22080  18603  -1931    671 -11138       C  
+ATOM  12109  C   TRP D 297     -54.165  36.058 -41.977  1.00147.29           C  
+ANISOU12109  C   TRP D 297    13186  23152  19624  -2060    579 -11227       C  
+ATOM  12110  O   TRP D 297     -54.672  37.177 -41.943  1.00149.01           O  
+ANISOU12110  O   TRP D 297    13219  23930  19468  -1758    204 -11031       O  
+ATOM  12111  CB  TRP D 297     -51.724  35.609 -41.690  1.00130.23           C  
+ANISOU12111  CB  TRP D 297    11867  19875  17738  -1854    985 -10701       C  
+ATOM  12112  CG  TRP D 297     -50.450  35.149 -42.326  1.00134.15           C  
+ANISOU12112  CG  TRP D 297    12707  20075  18190  -1768   1166 -10655       C  
+ATOM  12113  CD1 TRP D 297     -50.306  34.587 -43.562  1.00141.60           C  
+ANISOU12113  CD1 TRP D 297    13598  21308  18897  -1887   1187 -11052       C  
+ATOM  12114  CD2 TRP D 297     -49.125  35.337 -41.818  1.00127.92           C  
+ANISOU12114  CD2 TRP D 297    12345  18730  17530  -1497   1323 -10174       C  
+ATOM  12115  NE1 TRP D 297     -48.980  34.347 -43.823  1.00134.13           N  
+ANISOU12115  NE1 TRP D 297    13025  19971  17968  -1727   1380 -10864       N  
+ATOM  12116  CE2 TRP D 297     -48.232  34.806 -42.770  1.00122.22           C  
+ANISOU12116  CE2 TRP D 297    11797  17956  16682  -1476   1462 -10318       C  
+ATOM  12117  CE3 TRP D 297     -48.607  35.875 -40.636  1.00121.96           C  
+ANISOU12117  CE3 TRP D 297    11827  17520  16992  -1271   1377  -9645       C  
+ATOM  12118  CZ2 TRP D 297     -46.852  34.797 -42.577  1.00118.89           C  
+ANISOU12118  CZ2 TRP D 297    11746  17065  16363  -1225   1652  -9949       C  
+ATOM  12119  CZ3 TRP D 297     -47.239  35.866 -40.447  1.00117.13           C  
+ANISOU12119  CZ3 TRP D 297    11578  16456  16469  -1024   1553  -9272       C  
+ATOM  12120  CH2 TRP D 297     -46.377  35.331 -41.411  1.00119.24           C  
+ANISOU12120  CH2 TRP D 297    11981  16701  16624   -998   1688  -9424       C  
+ATOM  12121  N   GLU D 298     -54.701  34.996 -41.381  1.00146.30           N  
+ANISOU12121  N   GLU D 298    12965  22557  20065  -2497    953 -11504       N  
+ATOM  12122  CA  GLU D 298     -55.914  35.082 -40.576  1.00138.29           C  
+ANISOU12122  CA  GLU D 298    11617  21634  19292  -2675    971 -11598       C  
+ATOM  12123  C   GLU D 298     -55.623  35.829 -39.276  1.00131.32           C  
+ANISOU12123  C   GLU D 298    10958  20332  18606  -2458    971 -11054       C  
+ATOM  12124  O   GLU D 298     -54.552  35.671 -38.689  1.00132.91           O  
+ANISOU12124  O   GLU D 298    11605  19842  19054  -2375   1188 -10695       O  
+ATOM  12125  CB  GLU D 298     -56.476  33.690 -40.280  1.00141.83           C  
+ANISOU12125  CB  GLU D 298    11970  21623  20296  -3217   1446 -12016       C  
+ATOM  12126  N   THR D 299     -56.576  36.656 -38.855  1.00129.64           N  
+ANISOU12126  N   THR D 299    10430  20564  18264  -2343    722 -10992       N  
+ATOM  12127  CA  THR D 299     -56.419  37.551 -37.706  1.00126.29           C  
+ANISOU12127  CA  THR D 299    10163  19886  17936  -2111    649 -10508       C  
+ATOM  12128  C   THR D 299     -55.814  36.920 -36.449  1.00126.95           C  
+ANISOU12128  C   THR D 299    10645  18966  18624  -2308   1108 -10240       C  
+ATOM  12129  O   THR D 299     -54.917  37.502 -35.839  1.00122.58           O  
+ANISOU12129  O   THR D 299    10469  18044  18062  -2031   1089  -9782       O  
+ATOM  12130  CB  THR D 299     -57.776  38.168 -37.313  1.00127.39           C  
+ANISOU12130  CB  THR D 299     9837  20545  18021  -2096    451 -10580       C  
+ATOM  12131  N   GLU D 300     -56.304  35.748 -36.054  1.00131.39           N  
+ANISOU12131  N   GLU D 300    11150  19090  19682  -2754   1538 -10497       N  
+ATOM  12132  CA  GLU D 300     -55.811  35.096 -34.843  1.00126.86           C  
+ANISOU12132  CA  GLU D 300    10972  17565  19664  -2914   1999 -10183       C  
+ATOM  12133  C   GLU D 300     -54.343  34.700 -35.007  1.00122.21           C  
+ANISOU12133  C   GLU D 300    10886  16424  19126  -2737   2146  -9903       C  
+ATOM  12134  O   GLU D 300     -53.531  34.860 -34.086  1.00119.28           O  
+ANISOU12134  O   GLU D 300    10916  15462  18943  -2549   2289  -9407       O  
+ATOM  12135  CB  GLU D 300     -56.672  33.870 -34.506  1.00134.28           C  
+ANISOU12135  CB  GLU D 300    11765  18182  21075  -3419   2457 -10521       C  
+ATOM  12136  CG  GLU D 300     -56.307  33.135 -33.209  1.00141.16           C  
+ANISOU12136  CG  GLU D 300    13051  18082  22502  -3582   2972 -10157       C  
+ATOM  12137  CD  GLU D 300     -55.105  32.214 -33.343  1.00150.28           C  
+ANISOU12137  CD  GLU D 300    14674  18562  23865  -3550   3265  -9983       C  
+ATOM  12138  OE1 GLU D 300     -54.824  31.757 -34.470  1.00160.42           O  
+ANISOU12138  OE1 GLU D 300    15895  20065  24993  -3591   3212 -10321       O  
+ATOM  12139  OE2 GLU D 300     -54.442  31.949 -32.318  1.00149.51           O  
+ANISOU12139  OE2 GLU D 300    15006  17731  24072  -3462   3547  -9495       O  
+ATOM  12140  N   HIS D 301     -54.009  34.201 -36.194  1.00126.67           N  
+ANISOU12140  N   HIS D 301    11412  17216  19500  -2774   2109 -10215       N  
+ATOM  12141  CA  HIS D 301     -52.653  33.757 -36.496  1.00126.02           C  
+ANISOU12141  CA  HIS D 301    11748  16677  19456  -2611   2258 -10009       C  
+ATOM  12142  C   HIS D 301     -51.678  34.925 -36.460  1.00114.92           C  
+ANISOU12142  C   HIS D 301    10580  15399  17684  -2115   1957  -9546       C  
+ATOM  12143  O   HIS D 301     -50.592  34.821 -35.890  1.00108.97           O  
+ANISOU12143  O   HIS D 301    10226  14064  17114  -1913   2136  -9117       O  
+ATOM  12144  CB  HIS D 301     -52.605  33.069 -37.862  1.00128.68           C  
+ANISOU12144  CB  HIS D 301    11952  17330  19612  -2767   2260 -10499       C  
+ATOM  12145  N   ALA D 302     -52.068  36.033 -37.082  1.00118.12           N  
+ANISOU12145  N   ALA D 302    10736  16589  17554  -1895   1511  -9616       N  
+ATOM  12146  CA  ALA D 302     -51.249  37.238 -37.083  1.00112.75           C  
+ANISOU12146  CA  ALA D 302    10273  16093  16475  -1419   1239  -9187       C  
+ATOM  12147  C   ALA D 302     -51.102  37.795 -35.671  1.00102.22           C  
+ANISOU12147  C   ALA D 302     9148  14315  15374  -1256   1319  -8643       C  
+ATOM  12148  O   ALA D 302     -50.034  38.286 -35.293  1.00105.65           O  
+ANISOU12148  O   ALA D 302     9916  14482  15745   -928   1323  -8059       O  
+ATOM  12149  CB  ALA D 302     -51.847  38.283 -38.010  1.00116.53           C  
+ANISOU12149  CB  ALA D 302    10446  17513  16317  -1206    761  -9336       C  
+ATOM  12150  N   GLU D 303     -52.178  37.713 -34.893  1.00105.60           N  
+ANISOU12150  N   GLU D 303     9362  14698  16061  -1488   1385  -8705       N  
+ATOM  12151  CA  GLU D 303     -52.147  38.185 -33.515  1.00110.27           C  
+ANISOU12151  CA  GLU D 303    10147  14893  16858  -1356   1481  -8071       C  
+ATOM  12152  C   GLU D 303     -51.159  37.371 -32.690  1.00108.45           C  
+ANISOU12152  C   GLU D 303    10348  13795  17063  -1388   1878  -7765       C  
+ATOM  12153  O   GLU D 303     -50.446  37.919 -31.841  1.00101.46           O  
+ANISOU12153  O   GLU D 303     9755  12628  16165  -1105   1875  -7119       O  
+ATOM  12154  CB  GLU D 303     -53.544  38.114 -32.890  1.00102.35           C  
+ANISOU12154  CB  GLU D 303     8805  14009  16073  -1647   1541  -8279       C  
+ATOM  12155  N   GLN D 304     -51.096  36.068 -32.952  1.00106.80           N  
+ANISOU12155  N   GLN D 304    10180  13169  17229  -1717   2220  -8235       N  
+ATOM  12156  CA  GLN D 304     -50.141  35.222 -32.238  1.00113.41           C  
+ANISOU12156  CA  GLN D 304    11431  13191  18470  -1684   2597  -7878       C  
+ATOM  12157  C   GLN D 304     -48.730  35.455 -32.787  1.00113.17           C  
+ANISOU12157  C   GLN D 304    11638  13143  18216  -1306   2494  -7625       C  
+ATOM  12158  O   GLN D 304     -47.741  35.254 -32.085  1.00111.87           O  
+ANISOU12158  O   GLN D 304    11801  12452  18252  -1090   2667  -7163       O  
+ATOM  12159  CB  GLN D 304     -50.535  33.745 -32.309  1.00113.83           C  
+ANISOU12159  CB  GLN D 304    11474  12833  18943  -2100   2995  -8172       C  
+ATOM  12160  CG  GLN D 304     -49.718  32.868 -31.368  1.00110.72           C  
+ANISOU12160  CG  GLN D 304    11518  11580  18973  -2037   3400  -7721       C  
+ATOM  12161  CD  GLN D 304     -49.937  31.379 -31.562  1.00132.48           C  
+ANISOU12161  CD  GLN D 304    14326  13904  22108  -2381   3822  -7991       C  
+ATOM  12162  OE1 GLN D 304     -50.332  30.930 -32.638  1.00139.02           O  
+ANISOU12162  OE1 GLN D 304    14910  15054  22856  -2615   3807  -8526       O  
+ATOM  12163  NE2 GLN D 304     -49.706  30.606 -30.505  1.00140.33           N  
+ANISOU12163  NE2 GLN D 304    15649  14174  23496  -2403   4213  -7614       N  
+ATOM  12164  N   PHE D 305     -48.643  35.892 -34.041  1.00111.07           N  
+ANISOU12164  N   PHE D 305    11191  13491  17518  -1216   2213  -7914       N  
+ATOM  12165  CA  PHE D 305     -47.351  36.227 -34.632  1.00100.73           C  
+ANISOU12165  CA  PHE D 305    10073  12248  15953   -872   2122  -7692       C  
+ATOM  12166  C   PHE D 305     -46.758  37.398 -33.868  1.00 90.18           C  
+ANISOU12166  C   PHE D 305     8895  10948  14421   -499   1929  -7005       C  
+ATOM  12167  O   PHE D 305     -45.596  37.357 -33.441  1.00 91.74           O  
+ANISOU12167  O   PHE D 305     9350  10780  14729   -265   2036  -6583       O  
+ATOM  12168  CB  PHE D 305     -47.487  36.582 -36.113  1.00107.96           C  
+ANISOU12168  CB  PHE D 305    10772  13883  16366   -853   1847  -8082       C  
+ATOM  12169  CG  PHE D 305     -46.351  37.418 -36.640  1.00105.34           C  
+ANISOU12169  CG  PHE D 305    10594  13793  15637   -458   1684  -7795       C  
+ATOM  12170  CD1 PHE D 305     -45.053  36.930 -36.654  1.00110.37           C  
+ANISOU12170  CD1 PHE D 305    11483  14005  16446   -307   1903  -7564       C  
+ATOM  12171  CD2 PHE D 305     -46.580  38.706 -37.095  1.00 93.75           C  
+ANISOU12171  CD2 PHE D 305     9017  12982  13621   -230   1312  -7641       C  
+ATOM  12172  CE1 PHE D 305     -44.009  37.706 -37.131  1.00105.82           C  
+ANISOU12172  CE1 PHE D 305    11012  13672  15524     23   1787  -7313       C  
+ATOM  12173  CE2 PHE D 305     -45.541  39.487 -37.571  1.00 94.31           C  
+ANISOU12173  CE2 PHE D 305     9250  13255  13329     94   1197  -7290       C  
+ATOM  12174  CZ  PHE D 305     -44.255  38.986 -37.589  1.00102.29           C  
+ANISOU12174  CZ  PHE D 305    10476  13857  14533    200   1446  -7170       C  
+ATOM  12175  N   ILE D 306     -47.566  38.441 -33.707  1.00 87.94           N  
+ANISOU12175  N   ILE D 306     8440  11135  13837   -447   1632  -6853       N  
+ATOM  12176  CA  ILE D 306     -47.168  39.605 -32.929  1.00 88.88           C  
+ANISOU12176  CA  ILE D 306     8711  11295  13763   -148   1451  -6181       C  
+ATOM  12177  C   ILE D 306     -46.822  39.159 -31.511  1.00 90.87           C  
+ANISOU12177  C   ILE D 306     9207  10887  14433   -170   1705  -5769       C  
+ATOM  12178  O   ILE D 306     -45.800  39.568 -30.944  1.00 93.02           O  
+ANISOU12178  O   ILE D 306     9709  10961  14671     75   1686  -5258       O  
+ATOM  12179  CB  ILE D 306     -48.278  40.671 -32.890  1.00 82.46           C  
+ANISOU12179  CB  ILE D 306     7675  11013  12644   -106   1159  -6134       C  
+ATOM  12180  CG1 ILE D 306     -48.710  41.040 -34.311  1.00 92.09           C  
+ANISOU12180  CG1 ILE D 306     8640  12930  13419    -59    890  -6542       C  
+ATOM  12181  CG2 ILE D 306     -47.798  41.907 -32.158  1.00 79.60           C  
+ANISOU12181  CG2 ILE D 306     7511  10658  12075    196   1004  -5478       C  
+ATOM  12182  CD1 ILE D 306     -49.818  42.069 -34.369  1.00 95.78           C  
+ANISOU12182  CD1 ILE D 306     8857  13960  13575     53    589  -6497       C  
+ATOM  12183  N   HIS D 307     -47.684  38.309 -30.957  1.00 91.32           N  
+ANISOU12183  N   HIS D 307     9202  10630  14866   -478   1949  -6006       N  
+ATOM  12184  CA  HIS D 307     -47.497  37.756 -29.619  1.00 93.82           C  
+ANISOU12184  CA  HIS D 307     9769  10308  15571   -524   2234  -5639       C  
+ATOM  12185  C   HIS D 307     -46.112  37.142 -29.407  1.00 94.85           C  
+ANISOU12185  C   HIS D 307    10196   9946  15897   -320   2415  -5356       C  
+ATOM  12186  O   HIS D 307     -45.406  37.526 -28.482  1.00 99.30           O  
+ANISOU12186  O   HIS D 307    10972  10316  16442    -92   2382  -4789       O  
+ATOM  12187  CB  HIS D 307     -48.576  36.711 -29.319  1.00112.47           C  
+ANISOU12187  CB  HIS D 307    12029  12362  18343   -941   2556  -6047       C  
+ATOM  12188  CG  HIS D 307     -48.480  36.119 -27.946  1.00112.95           C  
+ANISOU12188  CG  HIS D 307    12379  11761  18776   -995   2886  -5651       C  
+ATOM  12189  ND1 HIS D 307     -49.317  36.489 -26.915  1.00111.92           N  
+ANISOU12189  ND1 HIS D 307    12233  11616  18677  -1107   2930  -5426       N  
+ATOM  12190  CD2 HIS D 307     -47.649  35.179 -27.438  1.00109.00           C  
+ANISOU12190  CD2 HIS D 307    12203  10603  18611   -925   3199  -5423       C  
+ATOM  12191  CE1 HIS D 307     -49.001  35.806 -25.829  1.00108.41           C  
+ANISOU12191  CE1 HIS D 307    12110  10542  18538  -1122   3254  -5068       C  
+ATOM  12192  NE2 HIS D 307     -47.992  35.005 -26.118  1.00107.07           N  
+ANISOU12192  NE2 HIS D 307    12152   9971  18559   -994   3411  -5042       N  
+ATOM  12193  N   GLN D 308     -45.725  36.191 -30.253  1.00 87.59           N  
+ANISOU12193  N   GLN D 308     9277   8845  15160   -391   2606  -5766       N  
+ATOM  12194  CA  GLN D 308     -44.480  35.458 -30.029  1.00 96.43           C  
+ANISOU12194  CA  GLN D 308    10652   9446  16539   -178   2833  -5529       C  
+ATOM  12195  C   GLN D 308     -43.241  36.232 -30.481  1.00103.04           C  
+ANISOU12195  C   GLN D 308    11510  10590  17052    186   2592  -5240       C  
+ATOM  12196  O   GLN D 308     -42.144  36.057 -29.916  1.00110.32           O  
+ANISOU12196  O   GLN D 308    12611  11201  18106    454   2668  -4815       O  
+ATOM  12197  CB  GLN D 308     -44.539  34.109 -30.751  1.00 93.01           C  
+ANISOU12197  CB  GLN D 308    10229   8710  16402   -402   3140  -6000       C  
+ATOM  12198  N   LEU D 309     -43.440  37.147 -31.433  1.00100.06           N  
+ANISOU12198  N   LEU D 309    10939  10846  16233    205   2297  -5430       N  
+ATOM  12199  CA  LEU D 309     -42.389  38.087 -31.813  1.00 93.34           C  
+ANISOU12199  CA  LEU D 309    10107  10328  15029    505   2073  -5122       C  
+ATOM  12200  C   LEU D 309     -42.009  38.893 -30.591  1.00 87.29           C  
+ANISOU12200  C   LEU D 309     9474   9488  14205    676   1937  -4477       C  
+ATOM  12201  O   LEU D 309     -40.837  38.968 -30.217  1.00 85.89           O  
+ANISOU12201  O   LEU D 309     9405   9164  14066    905   1947  -4109       O  
+ATOM  12202  CB  LEU D 309     -42.849  39.022 -32.936  1.00 98.67           C  
+ANISOU12202  CB  LEU D 309    10598  11685  15207    492   1791  -5372       C  
+ATOM  12203  CG  LEU D 309     -41.870  40.150 -33.276  1.00 85.31           C  
+ANISOU12203  CG  LEU D 309     8954  10333  13125    764   1584  -5010       C  
+ATOM  12204  CD1 LEU D 309     -40.547  39.577 -33.743  1.00 86.52           C  
+ANISOU12204  CD1 LEU D 309     9169  10307  13397    916   1768  -5031       C  
+ATOM  12205  CD2 LEU D 309     -42.446  41.103 -34.315  1.00 81.71           C  
+ANISOU12205  CD2 LEU D 309     8367  10520  12159    778   1323  -5190       C  
+ATOM  12206  N   SER D 310     -43.025  39.466 -29.953  1.00 83.81           N  
+ANISOU12206  N   SER D 310     9003   9164  13676    553   1820  -4373       N  
+ATOM  12207  CA  SER D 310     -42.837  40.203 -28.711  1.00 87.81           C  
+ANISOU12207  CA  SER D 310     9652   9590  14120    664   1716  -3820       C  
+ATOM  12208  C   SER D 310     -42.248  39.312 -27.620  1.00 88.85           C  
+ANISOU12208  C   SER D 310     9988   9155  14618    725   1946  -3512       C  
+ATOM  12209  O   SER D 310     -41.335  39.721 -26.890  1.00 83.69           O  
+ANISOU12209  O   SER D 310     9457   8447  13894    929   1858  -3048       O  
+ATOM  12210  CB  SER D 310     -44.166  40.795 -28.234  1.00 91.65           C  
+ANISOU12210  CB  SER D 310    10063  10257  14504    505   1624  -3843       C  
+ATOM  12211  OG  SER D 310     -44.693  41.709 -29.177  1.00 93.16           O  
+ANISOU12211  OG  SER D 310    10073  10996  14329    527   1382  -4048       O  
+ATOM  12212  N   LYS D 311     -42.753  38.082 -27.544  1.00 87.53           N  
+ANISOU12212  N   LYS D 311     9855   8573  14831    550   2247  -3779       N  
+ATOM  12213  CA  LYS D 311     -42.423  37.186 -26.448  1.00 98.95           C  
+ANISOU12213  CA  LYS D 311    11535   9435  16628    606   2506  -3463       C  
+ATOM  12214  C   LYS D 311     -40.956  36.804 -26.416  1.00100.96           C  
+ANISOU12214  C   LYS D 311    11891   9488  16983    934   2544  -3185       C  
+ATOM  12215  O   LYS D 311     -40.349  36.802 -25.335  1.00116.93           O  
+ANISOU12215  O   LYS D 311    14079  11309  19042   1131   2533  -2677       O  
+ATOM  12216  CB  LYS D 311     -43.263  35.904 -26.542  1.00 93.66           C  
+ANISOU12216  CB  LYS D 311    10896   8315  16373    322   2882  -3863       C  
+ATOM  12217  N   GLU D 312     -40.350  36.543 -27.578  1.00 83.83           N  
+ANISOU12217  N   GLU D 312     9604   7428  14820   1015   2570  -3502       N  
+ATOM  12218  CA  GLU D 312     -38.929  36.200 -27.510  1.00 96.22           C  
+ANISOU12218  CA  GLU D 312    11224   8832  16504   1356   2617  -3228       C  
+ATOM  12219  C   GLU D 312     -38.063  37.346 -28.033  1.00 94.21           C  
+ANISOU12219  C   GLU D 312    10811   9123  15862   1519   2313  -3100       C  
+ATOM  12220  O   GLU D 312     -36.845  37.206 -28.176  1.00106.21           O  
+ANISOU12220  O   GLU D 312    12286  10637  17434   1785   2325  -2940       O  
+ATOM  12221  CB  GLU D 312     -38.632  34.825 -28.156  1.00 98.31           C  
+ANISOU12221  CB  GLU D 312    11535   8644  17176   1395   2984  -3580       C  
+ATOM  12222  CG  GLU D 312     -37.769  34.651 -29.396  1.00 92.66           C  
+ANISOU12222  CG  GLU D 312    10679   8095  16432   1539   3031  -3898       C  
+ATOM  12223  CD  GLU D 312     -37.259  33.206 -29.448  1.00118.60           C  
+ANISOU12223  CD  GLU D 312    14120  10858  20085   1645   3356  -3907       C  
+ATOM  12224  OE1 GLU D 312     -37.248  32.582 -28.367  1.00125.49           O  
+ANISOU12224  OE1 GLU D 312    15196  11261  21223   1745   3503  -3535       O  
+ATOM  12225  OE2 GLU D 312     -36.892  32.684 -30.524  1.00133.08           O  
+ANISOU12225  OE2 GLU D 312    15901  12755  21908   1627   3462  -4243       O  
+ATOM  12226  N   LEU D 313     -38.690  38.495 -28.277  1.00 93.21           N  
+ANISOU12226  N   LEU D 313    10600   9455  15360   1368   2061  -3151       N  
+ATOM  12227  CA  LEU D 313     -37.926  39.733 -28.248  1.00 88.77           C  
+ANISOU12227  CA  LEU D 313     9979   9303  14445   1502   1788  -2846       C  
+ATOM  12228  C   LEU D 313     -37.574  39.950 -26.782  1.00 88.76           C  
+ANISOU12228  C   LEU D 313    10107   9137  14479   1607   1707  -2319       C  
+ATOM  12229  O   LEU D 313     -36.445  40.302 -26.436  1.00 83.64           O  
+ANISOU12229  O   LEU D 313     9425   8594  13759   1800   1595  -2003       O  
+ATOM  12230  CB  LEU D 313     -38.709  40.932 -28.789  1.00 81.01           C  
+ANISOU12230  CB  LEU D 313     8929   8788  13065   1352   1568  -2977       C  
+ATOM  12231  CG  LEU D 313     -38.646  41.336 -30.263  1.00 84.18           C  
+ANISOU12231  CG  LEU D 313     9199   9593  13194   1339   1510  -3322       C  
+ATOM  12232  CD1 LEU D 313     -39.595  42.504 -30.562  1.00 69.21           C  
+ANISOU12232  CD1 LEU D 313     7276   8104  10917   1241   1290  -3358       C  
+ATOM  12233  CD2 LEU D 313     -37.219  41.709 -30.620  1.00 79.34           C  
+ANISOU12233  CD2 LEU D 313     8542   9131  12473   1529   1487  -3137       C  
+ATOM  12234  N   ILE D 314     -38.564  39.742 -25.918  1.00 90.17           N  
+ANISOU12234  N   ILE D 314    10419   9093  14749   1462   1767  -2245       N  
+ATOM  12235  CA  ILE D 314     -38.350  39.888 -24.486  1.00 87.31           C  
+ANISOU12235  CA  ILE D 314    10214   8580  14377   1544   1710  -1761       C  
+ATOM  12236  C   ILE D 314     -37.455  38.765 -23.963  1.00 91.56           C  
+ANISOU12236  C   ILE D 314    10842   8719  15229   1795   1880  -1517       C  
+ATOM  12237  O   ILE D 314     -36.613  38.990 -23.089  1.00 84.62           O  
+ANISOU12237  O   ILE D 314    10003   7883  14264   1995   1745  -1088       O  
+ATOM  12238  CB  ILE D 314     -39.689  39.895 -23.718  1.00 89.40           C  
+ANISOU12238  CB  ILE D 314    10607   8699  14660   1317   1787  -1761       C  
+ATOM  12239  CG1 ILE D 314     -40.486  41.159 -24.046  1.00 81.76           C  
+ANISOU12239  CG1 ILE D 314     9547   8159  13359   1156   1584  -1902       C  
+ATOM  12240  CG2 ILE D 314     -39.461  39.802 -22.215  1.00 86.93           C  
+ANISOU12240  CG2 ILE D 314    10505   8176  14348   1411   1792  -1269       C  
+ATOM  12241  CD1 ILE D 314     -39.823  42.440 -23.586  1.00 76.12           C  
+ANISOU12241  CD1 ILE D 314     8862   7758  12302   1252   1319  -1572       C  
+ATOM  12242  N   ARG D 315     -37.615  37.564 -24.511  1.00 97.65           N  
+ANISOU12242  N   ARG D 315    11637   9109  16354   1797   2176  -1798       N  
+ATOM  12243  CA  ARG D 315     -36.785  36.436 -24.084  1.00 99.64           C  
+ANISOU12243  CA  ARG D 315    11997   8919  16942   2089   2382  -1563       C  
+ATOM  12244  C   ARG D 315     -35.301  36.656 -24.388  1.00 97.99           C  
+ANISOU12244  C   ARG D 315    11608   8953  16672   2419   2235  -1393       C  
+ATOM  12245  O   ARG D 315     -34.437  36.161 -23.665  1.00100.22           O  
+ANISOU12245  O   ARG D 315    11936   9052  17091   2740   2252  -1004       O  
+ATOM  12246  CB  ARG D 315     -37.254  35.134 -24.731  1.00101.15           C  
+ANISOU12246  CB  ARG D 315    12266   8618  17550   2002   2776  -1966       C  
+ATOM  12247  N   LYS D 316     -35.007  37.392 -25.457  1.00 93.74           N  
+ANISOU12247  N   LYS D 316    10854   8844  15919   2350   2099  -1674       N  
+ATOM  12248  CA  LYS D 316     -33.623  37.654 -25.845  1.00 92.62           C  
+ANISOU12248  CA  LYS D 316    10499   8973  15720   2611   1995  -1567       C  
+ATOM  12249  C   LYS D 316     -33.118  39.002 -25.332  1.00 97.58           C  
+ANISOU12249  C   LYS D 316    11023  10086  15966   2588   1649  -1259       C  
+ATOM  12250  O   LYS D 316     -32.371  39.699 -26.020  1.00 90.21           O  
+ANISOU12250  O   LYS D 316     9886   9534  14854   2603   1540  -1338       O  
+ATOM  12251  CB  LYS D 316     -33.479  37.594 -27.368  1.00 90.61           C  
+ANISOU12251  CB  LYS D 316    10087   8881  15458   2550   2114  -2059       C  
+ATOM  12252  N   ASP D 317     -33.538  39.351 -24.119  1.00104.88           N  
+ANISOU12252  N   ASP D 317    12104  10978  16767   2527   1510   -929       N  
+ATOM  12253  CA  ASP D 317     -33.017  40.505 -23.381  1.00 96.90           C  
+ANISOU12253  CA  ASP D 317    11035  10358  15426   2506   1205   -617       C  
+ATOM  12254  C   ASP D 317     -33.219  41.852 -24.084  1.00 89.19           C  
+ANISOU12254  C   ASP D 317     9976   9800  14114   2257   1051   -815       C  
+ATOM  12255  O   ASP D 317     -32.461  42.795 -23.858  1.00 87.67           O  
+ANISOU12255  O   ASP D 317     9672   9948  13692   2240    852   -652       O  
+ATOM  12256  CB  ASP D 317     -31.527  40.299 -23.085  1.00 97.64           C  
+ANISOU12256  CB  ASP D 317    10919  10595  15583   2824   1107   -347       C  
+ATOM  12257  CG  ASP D 317     -31.056  41.086 -21.877  1.00113.24           C  
+ANISOU12257  CG  ASP D 317    12884  12859  17283   2828    813     39       C  
+ATOM  12258  OD1 ASP D 317     -31.845  41.234 -20.920  1.00117.51           O  
+ANISOU12258  OD1 ASP D 317    13667  13283  17699   2712    765    213       O  
+ATOM  12259  OD2 ASP D 317     -29.900  41.558 -21.885  1.00122.48           O  
+ANISOU12259  OD2 ASP D 317    13790  14391  18354   2928    642    142       O  
+ATOM  12260  N   PHE D 318     -34.235  41.944 -24.936  1.00 78.37           N  
+ANISOU12260  N   PHE D 318     8658   8407  12711   2066   1150  -1165       N  
+ATOM  12261  CA  PHE D 318     -34.587  43.223 -25.551  1.00 80.24           C  
+ANISOU12261  CA  PHE D 318     8872   9003  12611   1872   1016  -1300       C  
+ATOM  12262  C   PHE D 318     -35.627  43.977 -24.727  1.00 82.28           C  
+ANISOU12262  C   PHE D 318     9308   9274  12680   1694    907  -1182       C  
+ATOM  12263  O   PHE D 318     -36.324  43.392 -23.898  1.00 80.08           O  
+ANISOU12263  O   PHE D 318     9165   8721  12541   1670    980  -1097       O  
+ATOM  12264  CB  PHE D 318     -35.106  43.025 -26.977  1.00 85.04           C  
+ANISOU12264  CB  PHE D 318     9418   9681  13214   1801   1141  -1733       C  
+ATOM  12265  CG  PHE D 318     -34.032  42.728 -27.982  1.00 84.53           C  
+ANISOU12265  CG  PHE D 318     9176   9739  13204   1936   1236  -1882       C  
+ATOM  12266  CD1 PHE D 318     -33.730  41.423 -28.333  1.00 86.79           C  
+ANISOU12266  CD1 PHE D 318     9408   9744  13825   2085   1458  -2060       C  
+ATOM  12267  CD2 PHE D 318     -33.326  43.759 -28.579  1.00 82.55           C  
+ANISOU12267  CD2 PHE D 318     8825   9860  12679   1909   1146  -1853       C  
+ATOM  12268  CE1 PHE D 318     -32.742  41.152 -29.262  1.00 88.05           C  
+ANISOU12268  CE1 PHE D 318     9396  10022  14036   2223   1577  -2219       C  
+ATOM  12269  CE2 PHE D 318     -32.338  43.495 -29.507  1.00 81.99           C  
+ANISOU12269  CE2 PHE D 318     8580   9922  12651   2021   1271  -1998       C  
+ATOM  12270  CZ  PHE D 318     -32.045  42.190 -29.849  1.00 88.84           C  
+ANISOU12270  CZ  PHE D 318     9373  10537  13845   2188   1481  -2189       C  
+ATOM  12271  N   ASN D 319     -35.723  45.281 -24.965  1.00 86.68           N  
+ANISOU12271  N   ASN D 319     9878  10129  12925   1575    767  -1175       N  
+ATOM  12272  CA  ASN D 319     -36.745  46.109 -24.336  1.00 75.46           C  
+ANISOU12272  CA  ASN D 319     8620   8734  11318   1428    690  -1109       C  
+ATOM  12273  C   ASN D 319     -37.722  46.617 -25.388  1.00 78.39           C  
+ANISOU12273  C   ASN D 319     8979   9261  11545   1350    704  -1393       C  
+ATOM  12274  O   ASN D 319     -37.326  46.923 -26.513  1.00 78.67           O  
+ANISOU12274  O   ASN D 319     8924   9504  11464   1382    701  -1540       O  
+ATOM  12275  CB  ASN D 319     -36.114  47.283 -23.586  1.00 79.77           C  
+ANISOU12275  CB  ASN D 319     9233   9461  11616   1369    528   -843       C  
+ATOM  12276  CG  ASN D 319     -35.126  46.836 -22.528  1.00 86.26           C  
+ANISOU12276  CG  ASN D 319    10026  10230  12517   1459    459   -564       C  
+ATOM  12277  OD1 ASN D 319     -35.373  45.879 -21.797  1.00 97.51           O  
+ANISOU12277  OD1 ASN D 319    11517  11412  14121   1545    521   -452       O  
+ATOM  12278  ND2 ASN D 319     -34.000  47.534 -22.437  1.00 85.57           N  
+ANISOU12278  ND2 ASN D 319     9836  10386  12289   1441    334   -444       N  
+ATOM  12279  N   ILE D 320     -38.998  46.704 -25.027  1.00 82.12           N  
+ANISOU12279  N   ILE D 320     9528   9664  12009   1264    722  -1464       N  
+ATOM  12280  CA  ILE D 320     -40.021  47.103 -25.986  1.00 69.77           C  
+ANISOU12280  CA  ILE D 320     7905   8292  10311   1230    707  -1735       C  
+ATOM  12281  C   ILE D 320     -40.712  48.406 -25.595  1.00 69.80           C  
+ANISOU12281  C   ILE D 320     8026   8432  10063   1202    610  -1609       C  
+ATOM  12282  O   ILE D 320     -41.169  48.567 -24.464  1.00 74.62           O  
+ANISOU12282  O   ILE D 320     8747   8901  10703   1143    624  -1458       O  
+ATOM  12283  CB  ILE D 320     -41.085  45.997 -26.149  1.00 68.88           C  
+ANISOU12283  CB  ILE D 320     7701   8031  10441   1154    837  -2032       C  
+ATOM  12284  CG1 ILE D 320     -40.451  44.736 -26.740  1.00 70.24           C  
+ANISOU12284  CG1 ILE D 320     7781   8040  10867   1188    975  -2222       C  
+ATOM  12285  CG2 ILE D 320     -42.232  46.475 -27.025  1.00 68.15           C  
+ANISOU12285  CG2 ILE D 320     7497   8221  10176   1126    772  -2313       C  
+ATOM  12286  CD1 ILE D 320     -41.403  43.568 -26.854  1.00 78.97           C  
+ANISOU12286  CD1 ILE D 320     8819   8929  12258   1061   1153  -2544       C  
+ATOM  12287  N   VAL D 321     -40.786  49.331 -26.547  1.00 71.14           N  
+ANISOU12287  N   VAL D 321     8192   8862   9976   1263    536  -1666       N  
+ATOM  12288  CA  VAL D 321     -41.588  50.536 -26.391  1.00 80.36           C  
+ANISOU12288  CA  VAL D 321     9470  10141  10921   1294    473  -1583       C  
+ATOM  12289  C   VAL D 321     -42.702  50.515 -27.433  1.00 86.75           C  
+ANISOU12289  C   VAL D 321    10134  11190  11637   1379    434  -1853       C  
+ATOM  12290  O   VAL D 321     -42.436  50.399 -28.630  1.00 73.14           O  
+ANISOU12290  O   VAL D 321     8324   9675   9790   1447    405  -2006       O  
+ATOM  12291  CB  VAL D 321     -40.734  51.808 -26.542  1.00 76.01           C  
+ANISOU12291  CB  VAL D 321     9086   9675  10120   1319    433  -1359       C  
+ATOM  12292  CG1 VAL D 321     -41.614  53.044 -26.530  1.00 71.03           C  
+ANISOU12292  CG1 VAL D 321     8597   9115   9274   1400    406  -1283       C  
+ATOM  12293  CG2 VAL D 321     -39.700  51.883 -25.430  1.00 72.72           C  
+ANISOU12293  CG2 VAL D 321     8765   9092   9773   1206    437  -1132       C  
+ATOM  12294  N   SER D 322     -43.947  50.632 -26.980  1.00 91.18           N  
+ANISOU12294  N   SER D 322    10649  11762  12235   1378    432  -1922       N  
+ATOM  12295  CA  SER D 322     -45.090  50.484 -27.879  1.00 78.67           C  
+ANISOU12295  CA  SER D 322     8847  10460  10585   1451    369  -2216       C  
+ATOM  12296  C   SER D 322     -46.092  51.627 -27.766  1.00 78.39           C  
+ANISOU12296  C   SER D 322     8836  10590  10360   1610    298  -2128       C  
+ATOM  12297  O   SER D 322     -46.365  52.126 -26.675  1.00 78.60           O  
+ANISOU12297  O   SER D 322     8993  10431  10439   1587    361  -1947       O  
+ATOM  12298  CB  SER D 322     -45.800  49.155 -27.617  1.00 72.02           C  
+ANISOU12298  CB  SER D 322     7796   9508  10058   1280    466  -2513       C  
+ATOM  12299  OG  SER D 322     -46.982  49.048 -28.392  1.00 73.52           O  
+ANISOU12299  OG  SER D 322     7724  10024  10187   1312    389  -2838       O  
+ATOM  12300  N   GLY D 323     -46.634  52.040 -28.909  1.00 79.57           N  
+ANISOU12300  N   GLY D 323     8862  11102  10267   1796    172  -2254       N  
+ATOM  12301  CA  GLY D 323     -47.643  53.082 -28.943  1.00 71.75           C  
+ANISOU12301  CA  GLY D 323     7860  10306   9097   2025     96  -2171       C  
+ATOM  12302  C   GLY D 323     -49.034  52.505 -28.795  1.00 74.81           C  
+ANISOU12302  C   GLY D 323     7906  10874   9644   1994     72  -2471       C  
+ATOM  12303  O   GLY D 323     -50.028  53.228 -28.876  1.00 80.85           O  
+ANISOU12303  O   GLY D 323     8563  11867  10290   2214     -3  -2458       O  
+ATOM  12304  N   PHE D 324     -49.089  51.194 -28.576  1.00 75.17           N  
+ANISOU12304  N   PHE D 324     7778  10806   9978   1724    158  -2742       N  
+ATOM  12305  CA  PHE D 324     -50.334  50.475 -28.331  1.00 78.24           C  
+ANISOU12305  CA  PHE D 324     7831  11307  10590   1589    199  -3069       C  
+ATOM  12306  C   PHE D 324     -51.342  50.705 -29.457  1.00 87.61           C  
+ANISOU12306  C   PHE D 324     8675  13052  11560   1774     -8  -3344       C  
+ATOM  12307  O   PHE D 324     -52.485  51.094 -29.217  1.00102.50           O  
+ANISOU12307  O   PHE D 324    10334  15154  13457   1882    -47  -3413       O  
+ATOM  12308  CB  PHE D 324     -50.922  50.893 -26.979  1.00 81.11           C  
+ANISOU12308  CB  PHE D 324     8270  11441  11106   1561    342  -2889       C  
+ATOM  12309  CG  PHE D 324     -52.027  50.001 -26.491  1.00 81.99           C  
+ANISOU12309  CG  PHE D 324     8073  11559  11519   1334    476  -3199       C  
+ATOM  12310  CD1 PHE D 324     -51.791  48.663 -26.231  1.00 78.34           C  
+ANISOU12310  CD1 PHE D 324     7577  10829  11361   1011    647  -3389       C  
+ATOM  12311  CD2 PHE D 324     -53.297  50.508 -26.272  1.00 76.10           C  
+ANISOU12311  CD2 PHE D 324     7074  11066  10775   1446    466  -3292       C  
+ATOM  12312  CE1 PHE D 324     -52.806  47.842 -25.780  1.00 78.49           C  
+ANISOU12312  CE1 PHE D 324     7334  10812  11676    758    825  -3676       C  
+ATOM  12313  CE2 PHE D 324     -54.315  49.692 -25.818  1.00 77.92           C  
+ANISOU12313  CE2 PHE D 324     6991  11316  11301   1196    626  -3597       C  
+ATOM  12314  CZ  PHE D 324     -54.068  48.358 -25.570  1.00 78.98           C  
+ANISOU12314  CZ  PHE D 324     7115  11159  11734    827    816  -3791       C  
+ATOM  12315  N   GLY D 325     -50.900  50.469 -30.688  1.00 78.34           N  
+ANISOU12315  N   GLY D 325     7450  12145  10168   1827   -144  -3502       N  
+ATOM  12316  CA  GLY D 325     -51.765  50.584 -31.847  1.00 82.18           C  
+ANISOU12316  CA  GLY D 325     7606  13230  10387   2000   -376  -3786       C  
+ATOM  12317  C   GLY D 325     -52.813  49.490 -31.894  1.00 92.09           C  
+ANISOU12317  C   GLY D 325     8411  14686  11894   1728   -364  -4312       C  
+ATOM  12318  O   GLY D 325     -52.542  48.349 -31.519  1.00 99.88           O  
+ANISOU12318  O   GLY D 325     9388  15343  13221   1371   -166  -4534       O  
+ATOM  12319  N   LEU D 326     -54.014  49.844 -32.342  1.00 90.58           N  
+ANISOU12319  N   LEU D 326     7839  15029  11547   1900   -561  -4509       N  
+ATOM  12320  CA  LEU D 326     -55.121  48.895 -32.419  1.00 96.20           C  
+ANISOU12320  CA  LEU D 326     8049  16013  12489   1618   -560  -5056       C  
+ATOM  12321  C   LEU D 326     -54.774  47.729 -33.340  1.00100.04           C  
+ANISOU12321  C   LEU D 326     8414  16609  12986   1322   -569  -5533       C  
+ATOM  12322  O   LEU D 326     -54.402  47.931 -34.496  1.00 99.04           O  
+ANISOU12322  O   LEU D 326     8310  16857  12466   1500   -778  -5596       O  
+ATOM  12323  CB  LEU D 326     -56.395  49.590 -32.905  1.00 97.38           C  
+ANISOU12323  CB  LEU D 326     7763  16841  12398   1925   -832  -5177       C  
+ATOM  12324  N   GLY D 327     -54.891  46.512 -32.822  1.00100.53           N  
+ANISOU12324  N   GLY D 327     8381  16322  13494    870   -309  -5865       N  
+ATOM  12325  CA  GLY D 327     -54.610  45.325 -33.607  1.00104.91           C  
+ANISOU12325  CA  GLY D 327     8837  16895  14129    552   -251  -6369       C  
+ATOM  12326  C   GLY D 327     -53.198  44.810 -33.408  1.00104.49           C  
+ANISOU12326  C   GLY D 327     9242  16235  14226    461    -24  -6161       C  
+ATOM  12327  O   GLY D 327     -52.847  43.736 -33.895  1.00108.91           O  
+ANISOU12327  O   GLY D 327     9788  16655  14937    192    110  -6550       O  
+ATOM  12328  N   VAL D 328     -52.380  45.590 -32.709  1.00105.98           N  
+ANISOU12328  N   VAL D 328     9820  16077  14371    694     22  -5568       N  
+ATOM  12329  CA  VAL D 328     -50.994  45.211 -32.458  1.00 99.70           C  
+ANISOU12329  CA  VAL D 328     9417  14761  13702    658    208  -5323       C  
+ATOM  12330  C   VAL D 328     -50.662  45.289 -30.969  1.00104.39           C  
+ANISOU12330  C   VAL D 328    10279  14783  14600    612    424  -4896       C  
+ATOM  12331  O   VAL D 328     -50.099  44.354 -30.399  1.00101.33           O  
+ANISOU12331  O   VAL D 328    10051  13897  14554    408    674  -4889       O  
+ATOM  12332  CB  VAL D 328     -50.012  46.105 -33.244  1.00 86.75           C  
+ANISOU12332  CB  VAL D 328     8013  13320  11627    982     35  -5023       C  
+ATOM  12333  CG1 VAL D 328     -48.576  45.748 -32.898  1.00 79.08           C  
+ANISOU12333  CG1 VAL D 328     7385  11845  10817    947    230  -4767       C  
+ATOM  12334  CG2 VAL D 328     -50.248  45.969 -34.741  1.00 91.31           C  
+ANISOU12334  CG2 VAL D 328     8373  14474  11845   1034   -164  -5431       C  
+ATOM  12335  N   GLY D 329     -51.025  46.411 -30.352  1.00107.10           N  
+ANISOU12335  N   GLY D 329    10682  15210  14802    822    331  -4540       N  
+ATOM  12336  CA  GLY D 329     -50.668  46.705 -28.973  1.00 91.41           C  
+ANISOU12336  CA  GLY D 329     8978  12763  12989    816    496  -4113       C  
+ATOM  12337  C   GLY D 329     -51.010  45.641 -27.947  1.00 83.25           C  
+ANISOU12337  C   GLY D 329     7935  11303  12395    496    788  -4214       C  
+ATOM  12338  O   GLY D 329     -50.163  45.258 -27.138  1.00 84.43           O  
+ANISOU12338  O   GLY D 329     8377  10985  12716    435    959  -3940       O  
+ATOM  12339  N   SER D 330     -52.249  45.160 -27.983  1.00 81.74           N  
+ANISOU12339  N   SER D 330     7397  11287  12375    295    852  -4600       N  
+ATOM  12340  CA  SER D 330     -52.735  44.210 -26.987  1.00 89.60           C  
+ANISOU12340  CA  SER D 330     8380  11877  13786    -35   1180  -4694       C  
+ATOM  12341  C   SER D 330     -51.938  42.912 -27.038  1.00 88.47           C  
+ANISOU12341  C   SER D 330     8414  11268  13932   -254   1408  -4806       C  
+ATOM  12342  O   SER D 330     -51.721  42.255 -26.019  1.00 94.29           O  
+ANISOU12342  O   SER D 330     9376  11490  14960   -409   1696  -4619       O  
+ATOM  12343  CB  SER D 330     -54.222  43.918 -27.205  1.00100.16           C  
+ANISOU12343  CB  SER D 330     9241  13557  15258   -250   1211  -5169       C  
+ATOM  12344  OG  SER D 330     -54.921  45.082 -27.614  1.00 90.96           O  
+ANISOU12344  OG  SER D 330     7829  12957  13774     38    924  -5152       O  
+ATOM  12345  N   PHE D 331     -51.494  42.561 -28.240  1.00 85.50           N  
+ANISOU12345  N   PHE D 331     7955  11076  13453   -236   1290  -5097       N  
+ATOM  12346  CA  PHE D 331     -50.797  41.306 -28.476  1.00 89.14           C  
+ANISOU12346  CA  PHE D 331     8549  11122  14196   -419   1519  -5286       C  
+ATOM  12347  C   PHE D 331     -49.303  41.440 -28.196  1.00 89.98           C  
+ANISOU12347  C   PHE D 331     9037  10904  14246   -179   1522  -4822       C  
+ATOM  12348  O   PHE D 331     -48.650  40.473 -27.794  1.00 92.14           O  
+ANISOU12348  O   PHE D 331     9517  10668  14825   -262   1777  -4755       O  
+ATOM  12349  CB  PHE D 331     -51.055  40.843 -29.907  1.00 89.18           C  
+ANISOU12349  CB  PHE D 331     8273  11504  14107   -531   1413  -5878       C  
+ATOM  12350  CG  PHE D 331     -52.486  41.003 -30.332  1.00 98.09           C  
+ANISOU12350  CG  PHE D 331     8947  13158  15166   -693   1285  -6323       C  
+ATOM  12351  CD1 PHE D 331     -53.482  40.238 -29.749  1.00102.36           C  
+ANISOU12351  CD1 PHE D 331     9291  13511  16090  -1072   1551  -6620       C  
+ATOM  12352  CD2 PHE D 331     -52.843  41.938 -31.289  1.00 96.69           C  
+ANISOU12352  CD2 PHE D 331     8528  13676  14533   -453    908  -6422       C  
+ATOM  12353  CE1 PHE D 331     -54.803  40.386 -30.126  1.00 99.06           C  
+ANISOU12353  CE1 PHE D 331     8385  13631  15622  -1230   1426  -7055       C  
+ATOM  12354  CE2 PHE D 331     -54.164  42.092 -31.669  1.00 96.73           C  
+ANISOU12354  CE2 PHE D 331     8064  14227  14461   -557    757  -6821       C  
+ATOM  12355  CZ  PHE D 331     -55.144  41.315 -31.087  1.00100.52           C  
+ANISOU12355  CZ  PHE D 331     8293  14555  15345   -953   1008  -7157       C  
+ATOM  12356  N   VAL D 332     -48.768  42.640 -28.406  1.00 82.25           N  
+ANISOU12356  N   VAL D 332     8143  10222  12888    123   1253  -4502       N  
+ATOM  12357  CA  VAL D 332     -47.423  42.960 -27.945  1.00 83.27           C  
+ANISOU12357  CA  VAL D 332     8589  10099  12953    328   1243  -4029       C  
+ATOM  12358  C   VAL D 332     -47.392  42.798 -26.435  1.00 83.17           C  
+ANISOU12358  C   VAL D 332     8791   9656  13154    273   1422  -3660       C  
+ATOM  12359  O   VAL D 332     -46.502  42.153 -25.879  1.00 91.08           O  
+ANISOU12359  O   VAL D 332    10009  10253  14346    296   1572  -3433       O  
+ATOM  12360  CB  VAL D 332     -46.996  44.394 -28.319  1.00 75.74           C  
+ANISOU12360  CB  VAL D 332     7694   9520  11565    604    963  -3753       C  
+ATOM  12361  CG1 VAL D 332     -45.676  44.748 -27.652  1.00 70.77           C  
+ANISOU12361  CG1 VAL D 332     7354   8635  10902    747    969  -3284       C  
+ATOM  12362  CG2 VAL D 332     -46.895  44.549 -29.825  1.00 90.85           C  
+ANISOU12362  CG2 VAL D 332     9452  11858  13210    691    800  -4054       C  
+ATOM  12363  N   ILE D 333     -48.393  43.381 -25.785  1.00 81.41           N  
+ANISOU12363  N   ILE D 333     8498   9551  12881    221   1410  -3601       N  
+ATOM  12364  CA  ILE D 333     -48.552  43.290 -24.341  1.00 82.32           C  
+ANISOU12364  CA  ILE D 333     8812   9322  13145    148   1595  -3283       C  
+ATOM  12365  C   ILE D 333     -48.656  41.839 -23.861  1.00 81.21           C  
+ANISOU12365  C   ILE D 333     8744   8692  13418    -90   1938  -3388       C  
+ATOM  12366  O   ILE D 333     -47.912  41.419 -22.966  1.00 79.21           O  
+ANISOU12366  O   ILE D 333     8779   8041  13275    -41   2077  -3029       O  
+ATOM  12367  CB  ILE D 333     -49.796  44.089 -23.895  1.00 77.85           C  
+ANISOU12367  CB  ILE D 333     8094   9007  12476    113   1567  -3315       C  
+ATOM  12368  CG1 ILE D 333     -49.535  45.588 -24.043  1.00 75.33           C  
+ANISOU12368  CG1 ILE D 333     7838   9015  11769    393   1292  -3069       C  
+ATOM  12369  CG2 ILE D 333     -50.141  43.813 -22.462  1.00 79.82           C  
+ANISOU12369  CG2 ILE D 333     8523   8909  12895    -24   1825  -3078       C  
+ATOM  12370  CD1 ILE D 333     -50.648  46.456 -23.502  1.00 81.14           C  
+ANISOU12370  CD1 ILE D 333     8469   9949  12410    428   1288  -3045       C  
+ATOM  12371  N   ASN D 334     -49.542  41.069 -24.488  1.00 84.13           N  
+ANISOU12371  N   ASN D 334     8859   9098  14010   -343   2076  -3884       N  
+ATOM  12372  CA  ASN D 334     -49.721  39.661 -24.137  1.00 94.41           C  
+ANISOU12372  CA  ASN D 334    10240   9888  15743   -613   2459  -4041       C  
+ATOM  12373  C   ASN D 334     -48.416  38.883 -24.264  1.00103.76           C  
+ANISOU12373  C   ASN D 334    11684  10668  17070   -476   2555  -3878       C  
+ATOM  12374  O   ASN D 334     -48.015  38.145 -23.351  1.00107.78           O  
+ANISOU12374  O   ASN D 334    12478  10657  17816   -481   2819  -3581       O  
+ATOM  12375  CB  ASN D 334     -50.794  39.021 -25.021  1.00 97.71           C  
+ANISOU12375  CB  ASN D 334    10297  10477  16352   -938   2560  -4699       C  
+ATOM  12376  CG  ASN D 334     -52.192  39.506 -24.688  1.00 95.77           C  
+ANISOU12376  CG  ASN D 334     9757  10547  16085  -1114   2563  -4871       C  
+ATOM  12377  OD1 ASN D 334     -52.487  39.851 -23.543  1.00 90.66           O  
+ANISOU12377  OD1 ASN D 334     9248   9754  15445  -1109   2682  -4530       O  
+ATOM  12378  ND2 ASN D 334     -53.062  39.539 -25.691  1.00104.92           N  
+ANISOU12378  ND2 ASN D 334    10489  12177  17198  -1261   2430  -5414       N  
+ATOM  12379  N   GLY D 335     -47.752  39.071 -25.400  1.00105.70           N  
+ANISOU12379  N   GLY D 335    11833  11175  17154   -324   2346  -4055       N  
+ATOM  12380  CA  GLY D 335     -46.483  38.425 -25.664  1.00103.38           C  
+ANISOU12380  CA  GLY D 335    11725  10578  16979   -154   2420  -3941       C  
+ATOM  12381  C   GLY D 335     -45.419  38.780 -24.646  1.00 98.40           C  
+ANISOU12381  C   GLY D 335    11374   9753  16259    123   2361  -3314       C  
+ATOM  12382  O   GLY D 335     -44.625  37.926 -24.251  1.00103.67           O  
+ANISOU12382  O   GLY D 335    12246   9978  17165    230   2552  -3109       O  
+ATOM  12383  N   VAL D 336     -45.401  40.037 -24.211  1.00 89.76           N  
+ANISOU12383  N   VAL D 336    10289   8995  14822    247   2099  -3017       N  
+ATOM  12384  CA  VAL D 336     -44.439  40.463 -23.201  1.00 90.09           C  
+ANISOU12384  CA  VAL D 336    10569   8928  14734    465   2013  -2465       C  
+ATOM  12385  C   VAL D 336     -44.719  39.813 -21.847  1.00 90.30           C  
+ANISOU12385  C   VAL D 336    10830   8520  14960    390   2267  -2172       C  
+ATOM  12386  O   VAL D 336     -43.809  39.259 -21.228  1.00 81.63           O  
+ANISOU12386  O   VAL D 336     9941   7114  13961    560   2345  -1828       O  
+ATOM  12387  CB  VAL D 336     -44.428  41.995 -23.036  1.00 83.59           C  
+ANISOU12387  CB  VAL D 336     9723   8535  13502    564   1712  -2268       C  
+ATOM  12388  CG1 VAL D 336     -43.639  42.391 -21.797  1.00 79.56           C  
+ANISOU12388  CG1 VAL D 336     9453   7914  12861    702   1650  -1754       C  
+ATOM  12389  CG2 VAL D 336     -43.838  42.655 -24.270  1.00 84.90           C  
+ANISOU12389  CG2 VAL D 336     9744   9075  13440    695   1484  -2419       C  
+ATOM  12390  N   LEU D 337     -45.969  39.864 -21.386  1.00 93.21           N  
+ANISOU12390  N   LEU D 337    11159   8879  15379    154   2407  -2294       N  
+ATOM  12391  CA  LEU D 337     -46.280  39.293 -20.072  1.00 97.47           C  
+ANISOU12391  CA  LEU D 337    11950   9016  16067     66   2685  -1995       C  
+ATOM  12392  C   LEU D 337     -46.135  37.778 -20.031  1.00103.89           C  
+ANISOU12392  C   LEU D 337    12912   9259  17304     -9   3054  -2043       C  
+ATOM  12393  O   LEU D 337     -45.909  37.219 -18.957  1.00110.11           O  
+ANISOU12393  O   LEU D 337    13998   9653  18186     45   3266  -1649       O  
+ATOM  12394  CB  LEU D 337     -47.674  39.686 -19.579  1.00 99.26           C  
+ANISOU12394  CB  LEU D 337    12081   9366  16268   -186   2802  -2132       C  
+ATOM  12395  CG  LEU D 337     -47.868  41.144 -19.165  1.00102.19           C  
+ANISOU12395  CG  LEU D 337    12424  10159  16245    -84   2536  -1959       C  
+ATOM  12396  CD1 LEU D 337     -48.852  41.838 -20.052  1.00 97.71           C  
+ANISOU12396  CD1 LEU D 337    11506  10022  15597   -174   2400  -2376       C  
+ATOM  12397  CD2 LEU D 337     -48.315  41.217 -17.710  1.00106.42           C  
+ANISOU12397  CD2 LEU D 337    13196  10514  16723   -163   2736  -1635       C  
+ATOM  12398  N   GLU D 338     -46.303  37.109 -21.172  1.00104.34           N  
+ANISOU12398  N   GLU D 338    12786   9255  17604   -136   3154  -2524       N  
+ATOM  12399  CA  GLU D 338     -46.069  35.665 -21.206  1.00 99.61           C  
+ANISOU12399  CA  GLU D 338    12361   8051  17436   -192   3537  -2594       C  
+ATOM  12400  C   GLU D 338     -44.669  35.363 -20.677  1.00 97.24           C  
+ANISOU12400  C   GLU D 338    12335   7483  17128    204   3505  -2069       C  
+ATOM  12401  O   GLU D 338     -44.474  34.434 -19.892  1.00101.57           O  
+ANISOU12401  O   GLU D 338    13181   7488  17921    264   3815  -1769       O  
+ATOM  12402  CB  GLU D 338     -46.224  35.104 -22.619  1.00 92.70           C  
+ANISOU12402  CB  GLU D 338    11251   7210  16761   -347   3598  -3218       C  
+ATOM  12403  CG  GLU D 338     -45.923  33.614 -22.705  1.00104.36           C  
+ANISOU12403  CG  GLU D 338    12938   8003  18712   -397   4032  -3325       C  
+ATOM  12404  CD  GLU D 338     -46.404  32.984 -23.995  1.00115.29           C  
+ANISOU12404  CD  GLU D 338    14092   9394  20318   -685   4172  -4057       C  
+ATOM  12405  OE1 GLU D 338     -45.722  32.065 -24.496  1.00106.58           O  
+ANISOU12405  OE1 GLU D 338    13094   7989  19412   -596   4338  -4131       O  
+ATOM  12406  OE2 GLU D 338     -47.465  33.401 -24.503  1.00121.97           O  
+ANISOU12406  OE2 GLU D 338    14626  10656  21059   -994   4069  -4506       O  
+ATOM  12407  N   GLU D 339     -43.701  36.163 -21.110  1.00 93.90           N  
+ANISOU12407  N   GLU D 339    11801   7460  16419    480   3134  -1951       N  
+ATOM  12408  CA  GLU D 339     -42.325  36.046 -20.647  1.00 94.55           C  
+ANISOU12408  CA  GLU D 339    12044   7433  16448    869   3030  -1475       C  
+ATOM  12409  C   GLU D 339     -42.162  36.823 -19.345  1.00100.14           C  
+ANISOU12409  C   GLU D 339    12912   8306  16830    980   2847   -948       C  
+ATOM  12410  O   GLU D 339     -41.330  36.481 -18.503  1.00103.67           O  
+ANISOU12410  O   GLU D 339    13566   8562  17262   1251   2850   -474       O  
+ATOM  12411  CB  GLU D 339     -41.345  36.557 -21.705  1.00 95.18           C  
+ANISOU12411  CB  GLU D 339    11901   7887  16375   1070   2748  -1619       C  
+ATOM  12412  N   LEU D 340     -42.959  37.884 -19.214  1.00 98.25           N  
+ANISOU12412  N   LEU D 340    12566   8449  16314    785   2682  -1051       N  
+ATOM  12413  CA  LEU D 340     -42.908  38.812 -18.083  1.00 94.04           C  
+ANISOU12413  CA  LEU D 340    12165   8141  15423    839   2499   -655       C  
+ATOM  12414  C   LEU D 340     -41.569  39.537 -18.022  1.00 95.70           C  
+ANISOU12414  C   LEU D 340    12344   8668  15351   1125   2146   -372       C  
+ATOM  12415  O   LEU D 340     -41.430  40.644 -18.546  1.00 84.51           O  
+ANISOU12415  O   LEU D 340    10755   7675  13681   1107   1877   -507       O  
+ATOM  12416  CB  LEU D 340     -43.180  38.086 -16.761  1.00 87.65           C  
+ANISOU12416  CB  LEU D 340    11681   6922  14698    829   2779   -276       C  
+ATOM  12417  N   ILE D 347     -43.573  43.840 -11.103  1.00 98.64           N  
+ANISOU12417  N   ILE D 347    13823   9886  13768    699   1935    955       N  
+ATOM  12418  CA  ILE D 347     -43.371  42.719 -12.014  1.00101.56           C  
+ANISOU12418  CA  ILE D 347    14058   9976  14554    780   2042    865       C  
+ATOM  12419  C   ILE D 347     -42.726  43.184 -13.317  1.00112.18           C  
+ANISOU12419  C   ILE D 347    15105  11544  15975    860   1776    603       C  
+ATOM  12420  O   ILE D 347     -41.764  42.582 -13.796  1.00124.55           O  
+ANISOU12420  O   ILE D 347    16597  13042  17686   1049   1686    682       O  
+ATOM  12421  CB  ILE D 347     -44.700  42.002 -12.327  1.00 97.06           C  
+ANISOU12421  CB  ILE D 347    13442   9097  14338    557   2432    598       C  
+ATOM  12422  N   ASP D 348     -43.304  44.219 -13.917  1.00103.38           N  
+ANISOU12422  N   ASP D 348    13826  10679  14774    733   1685    295       N  
+ATOM  12423  CA  ASP D 348     -42.707  44.888 -15.071  1.00100.23           C  
+ANISOU12423  CA  ASP D 348    13197  10536  14351    802   1435     89       C  
+ATOM  12424  C   ASP D 348     -41.508  45.785 -14.752  1.00103.70           C  
+ANISOU12424  C   ASP D 348    13671  11259  14470    902   1132    288       C  
+ATOM  12425  O   ASP D 348     -41.539  46.563 -13.799  1.00107.94           O  
+ANISOU12425  O   ASP D 348    14375  11933  14705    837   1066    428       O  
+ATOM  12426  CB  ASP D 348     -43.780  45.703 -15.791  1.00 92.79           C  
+ANISOU12426  CB  ASP D 348    12096   9759  13403    672   1454   -263       C  
+ATOM  12427  CG  ASP D 348     -44.955  44.852 -16.206  1.00 98.92           C  
+ANISOU12427  CG  ASP D 348    12750  10339  14497    538   1723   -531       C  
+ATOM  12428  OD1 ASP D 348     -44.989  43.675 -15.792  1.00100.38           O  
+ANISOU12428  OD1 ASP D 348    13038  10197  14907    508   1945   -426       O  
+ATOM  12429  OD2 ASP D 348     -45.836  45.346 -16.937  1.00100.55           O  
+ANISOU12429  OD2 ASP D 348    12756  10718  14730    466   1720   -845       O  
+ATOM  12430  N   ASP D 349     -40.453  45.664 -15.552  1.00 94.96           N  
+ANISOU12430  N   ASP D 349    12397  10249  13435   1035    970    268       N  
+ATOM  12431  CA  ASP D 349     -39.242  46.457 -15.359  1.00 99.05           C  
+ANISOU12431  CA  ASP D 349    12882  11058  13695   1094    696    412       C  
+ATOM  12432  C   ASP D 349     -39.173  47.540 -16.430  1.00102.05           C  
+ANISOU12432  C   ASP D 349    13112  11664  14001   1021    587    153       C  
+ATOM  12433  O   ASP D 349     -40.181  48.151 -16.782  1.00 95.21           O  
+ANISOU12433  O   ASP D 349    12263  10808  13106    916    666    -48       O  
+ATOM  12434  CB  ASP D 349     -37.987  45.579 -15.407  1.00106.79           C  
+ANISOU12434  CB  ASP D 349    13759  12020  14798   1317    605    612       C  
+ATOM  12435  CG  ASP D 349     -36.866  46.106 -14.523  1.00115.03           C  
+ANISOU12435  CG  ASP D 349    14815  13355  15535   1371    344    875       C  
+ATOM  12436  OD1 ASP D 349     -36.948  47.267 -14.067  1.00113.55           O  
+ANISOU12436  OD1 ASP D 349    14708  13391  15045   1195    229    837       O  
+ATOM  12437  OD2 ASP D 349     -35.905  45.349 -14.275  1.00117.73           O  
+ANISOU12437  OD2 ASP D 349    15079  13709  15943   1597    258   1106       O  
+ATOM  12438  N   ASP D 350     -37.959  47.757 -16.928  1.00108.87           N  
+ANISOU12438  N   ASP D 350    13823  12714  14831   1096    418    180       N  
+ATOM  12439  CA  ASP D 350     -37.650  48.675 -18.024  1.00103.05           C  
+ANISOU12439  CA  ASP D 350    12953  12174  14027   1044    341    -18       C  
+ATOM  12440  C   ASP D 350     -37.785  47.958 -19.366  1.00 94.61           C  
+ANISOU12440  C   ASP D 350    11703  11030  13213   1138    441   -240       C  
+ATOM  12441  O   ASP D 350     -37.272  48.414 -20.388  1.00 91.93           O  
+ANISOU12441  O   ASP D 350    11232  10857  12840   1147    393   -369       O  
+ATOM  12442  CB  ASP D 350     -36.248  49.274 -17.871  1.00116.02           C  
+ANISOU12442  CB  ASP D 350    14503  14074  15506   1031    147     99       C  
+ATOM  12443  CG  ASP D 350     -36.023  49.890 -16.502  1.00123.36           C  
+ANISOU12443  CG  ASP D 350    15595  15118  16157    918     28    280       C  
+ATOM  12444  OD1 ASP D 350     -37.013  50.065 -15.758  1.00129.25           O  
+ANISOU12444  OD1 ASP D 350    16560  15743  16806    842    117    300       O  
+ATOM  12445  OD2 ASP D 350     -34.864  50.235 -16.189  1.00121.53           O  
+ANISOU12445  OD2 ASP D 350    15257  15127  15791    888   -149    372       O  
+ATOM  12446  N   ARG D 351     -38.483  46.827 -19.339  1.00 90.59           N  
+ANISOU12446  N   ARG D 351    11206  10265  12949   1183    607   -295       N  
+ATOM  12447  CA  ARG D 351     -38.645  45.944 -20.487  1.00 86.55           C  
+ANISOU12447  CA  ARG D 351    10540   9644  12699   1246    730   -543       C  
+ATOM  12448  C   ARG D 351     -39.796  46.384 -21.393  1.00 81.87           C  
+ANISOU12448  C   ARG D 351     9891   9141  12077   1142    781   -861       C  
+ATOM  12449  O   ARG D 351     -39.740  46.204 -22.611  1.00 82.26           O  
+ANISOU12449  O   ARG D 351     9789   9282  12183   1174    795  -1108       O  
+ATOM  12450  CB  ARG D 351     -38.908  44.514 -20.010  1.00 86.43           C  
+ANISOU12450  CB  ARG D 351    10587   9270  12982   1305    924   -483       C  
+ATOM  12451  CG  ARG D 351     -37.882  43.963 -19.036  1.00 84.68           C  
+ANISOU12451  CG  ARG D 351    10440   8950  12783   1478    876   -115       C  
+ATOM  12452  CD  ARG D 351     -36.489  43.924 -19.634  1.00 83.57           C  
+ANISOU12452  CD  ARG D 351    10102   8984  12669   1655    748    -80       C  
+ATOM  12453  NE  ARG D 351     -36.457  43.150 -20.872  1.00 81.08           N  
+ANISOU12453  NE  ARG D 351     9642   8540  12626   1721    903   -369       N  
+ATOM  12454  CZ  ARG D 351     -36.335  41.827 -20.928  1.00 86.45           C  
+ANISOU12454  CZ  ARG D 351    10340   8874  13634   1872   1102   -365       C  
+ATOM  12455  NH1 ARG D 351     -36.233  41.117 -19.812  1.00 83.77           N  
+ANISOU12455  NH1 ARG D 351    10168   8274  13388   2002   1169    -35       N  
+ATOM  12456  NH2 ARG D 351     -36.317  41.212 -22.101  1.00103.75           N  
+ANISOU12456  NH2 ARG D 351    12407  10967  16046   1899   1253   -691       N  
+ATOM  12457  N   LEU D 352     -40.843  46.951 -20.803  1.00 78.32           N  
+ANISOU12457  N   LEU D 352     9547   8693  11518   1035    807   -860       N  
+ATOM  12458  CA  LEU D 352     -41.998  47.378 -21.583  1.00 73.97           C  
+ANISOU12458  CA  LEU D 352     8902   8270  10932    982    834  -1140       C  
+ATOM  12459  C   LEU D 352     -42.492  48.759 -21.168  1.00 73.52           C  
+ANISOU12459  C   LEU D 352     8960   8367  10609    955    758  -1059       C  
+ATOM  12460  O   LEU D 352     -42.897  48.974 -20.026  1.00 74.71           O  
+ANISOU12460  O   LEU D 352     9259   8418  10708    889    814   -914       O  
+ATOM  12461  CB  LEU D 352     -43.133  46.359 -21.447  1.00 73.77           C  
+ANISOU12461  CB  LEU D 352     8817   8048  11165    883   1030  -1331       C  
+ATOM  12462  CG  LEU D 352     -44.449  46.702 -22.150  1.00 73.71           C  
+ANISOU12462  CG  LEU D 352     8641   8228  11136    823   1044  -1647       C  
+ATOM  12463  CD1 LEU D 352     -44.218  46.948 -23.633  1.00 79.94           C  
+ANISOU12463  CD1 LEU D 352     9262   9287  11826    911    917  -1880       C  
+ATOM  12464  CD2 LEU D 352     -45.484  45.606 -21.931  1.00 73.55           C  
+ANISOU12464  CD2 LEU D 352     8529   8008  11411    662   1268  -1862       C  
+ATOM  12465  N   ILE D 353     -42.452  49.688 -22.117  1.00 75.96           N  
+ANISOU12465  N   ILE D 353     9220   8901  10739   1019    658  -1150       N  
+ATOM  12466  CA  ILE D 353     -42.965  51.036 -21.918  1.00 71.94           C  
+ANISOU12466  CA  ILE D 353     8835   8500  10001   1036    620  -1092       C  
+ATOM  12467  C   ILE D 353     -44.089  51.280 -22.912  1.00 76.23           C  
+ANISOU12467  C   ILE D 353     9225   9224  10517   1130    615  -1328       C  
+ATOM  12468  O   ILE D 353     -43.876  51.266 -24.128  1.00 82.88           O  
+ANISOU12468  O   ILE D 353     9950  10242  11300   1215    547  -1457       O  
+ATOM  12469  CB  ILE D 353     -41.868  52.105 -22.094  1.00 73.04           C  
+ANISOU12469  CB  ILE D 353     9103   8729   9919   1046    524   -933       C  
+ATOM  12470  CG1 ILE D 353     -41.036  52.225 -20.818  1.00 75.73           C  
+ANISOU12470  CG1 ILE D 353     9598   8965  10211    933    500   -710       C  
+ATOM  12471  CG2 ILE D 353     -42.484  53.462 -22.404  1.00 72.43           C  
+ANISOU12471  CG2 ILE D 353     9144   8742   9633   1117    523   -932       C  
+ATOM  12472  CD1 ILE D 353     -41.827  52.706 -19.619  1.00 76.55           C  
+ANISOU12472  CD1 ILE D 353     9885   8970  10231    865    569   -640       C  
+ATOM  12473  N   LEU D 354     -45.292  51.477 -22.389  1.00 72.35           N  
+ANISOU12473  N   LEU D 354     8715   8722  10052   1124    689  -1389       N  
+ATOM  12474  CA  LEU D 354     -46.459  51.699 -23.226  1.00 69.41           C  
+ANISOU12474  CA  LEU D 354     8139   8578   9654   1237    662  -1615       C  
+ATOM  12475  C   LEU D 354     -46.794  53.181 -23.271  1.00 69.66           C  
+ANISOU12475  C   LEU D 354     8309   8715   9444   1409    619  -1490       C  
+ATOM  12476  O   LEU D 354     -46.898  53.835 -22.233  1.00 75.71           O  
+ANISOU12476  O   LEU D 354     9273   9330  10162   1380    700  -1335       O  
+ATOM  12477  CB  LEU D 354     -47.649  50.893 -22.706  1.00 69.96           C  
+ANISOU12477  CB  LEU D 354     8030   8599   9953   1126    797  -1804       C  
+ATOM  12478  CG  LEU D 354     -47.444  49.376 -22.729  1.00 71.89           C  
+ANISOU12478  CG  LEU D 354     8163   8677  10475    951    897  -1951       C  
+ATOM  12479  CD1 LEU D 354     -48.352  48.688 -21.721  1.00 72.34           C  
+ANISOU12479  CD1 LEU D 354     8184   8545  10757    776   1113  -2007       C  
+ATOM  12480  CD2 LEU D 354     -47.670  48.823 -24.128  1.00 77.90           C  
+ANISOU12480  CD2 LEU D 354     8655   9664  11278    974    818  -2283       C  
+ATOM  12481  N   ARG D 355     -46.957  53.708 -24.478  1.00 69.17           N  
+ANISOU12481  N   ARG D 355     8164   8902   9215   1600    507  -1555       N  
+ATOM  12482  CA  ARG D 355     -47.325  55.106 -24.656  1.00 69.64           C  
+ANISOU12482  CA  ARG D 355     8374   9034   9053   1823    489  -1414       C  
+ATOM  12483  C   ARG D 355     -48.529  55.224 -25.585  1.00 71.70           C  
+ANISOU12483  C   ARG D 355     8366   9633   9243   2064    395  -1594       C  
+ATOM  12484  O   ARG D 355     -48.393  55.668 -26.726  1.00 77.33           O  
+ANISOU12484  O   ARG D 355     9074  10571   9738   2263    281  -1571       O  
+ATOM  12485  CB  ARG D 355     -46.142  55.906 -25.207  1.00 69.97           C  
+ANISOU12485  CB  ARG D 355     8664   9037   8885   1864    456  -1212       C  
+ATOM  12486  CG  ARG D 355     -44.945  55.975 -24.268  1.00 70.39           C  
+ANISOU12486  CG  ARG D 355     8943   8824   8977   1632    521  -1044       C  
+ATOM  12487  CD  ARG D 355     -45.222  56.874 -23.072  1.00 74.01           C  
+ANISOU12487  CD  ARG D 355     9646   9075   9401   1594    631   -913       C  
+ATOM  12488  NE  ARG D 355     -44.078  56.950 -22.166  1.00 78.31           N  
+ANISOU12488  NE  ARG D 355    10379   9438   9937   1355    658   -786       N  
+ATOM  12489  CZ  ARG D 355     -43.034  57.754 -22.341  1.00 75.71           C  
+ANISOU12489  CZ  ARG D 355    10243   9052   9471   1277    665   -661       C  
+ATOM  12490  NH1 ARG D 355     -42.041  57.753 -21.462  1.00 85.24           N  
+ANISOU12490  NH1 ARG D 355    11555  10163  10671   1043    661   -586       N  
+ATOM  12491  NH2 ARG D 355     -42.982  58.562 -23.392  1.00 73.22           N  
+ANISOU12491  NH2 ARG D 355    10012   8793   9014   1429    682   -610       N  
+ATOM  12492  N   PRO D 356     -49.713  54.811 -25.102  1.00 72.33           N  
+ANISOU12492  N   PRO D 356     8206   9785   9492   2047    446  -1775       N  
+ATOM  12493  CA  PRO D 356     -50.939  54.916 -25.901  1.00 81.01           C  
+ANISOU12493  CA  PRO D 356     8971  11276  10533   2278    335  -1975       C  
+ATOM  12494  C   PRO D 356     -51.261  56.362 -26.252  1.00 79.20           C  
+ANISOU12494  C   PRO D 356     8894  11150  10049   2660    286  -1756       C  
+ATOM  12495  O   PRO D 356     -51.020  57.259 -25.445  1.00 86.24           O  
+ANISOU12495  O   PRO D 356    10104  11748  10914   2700    421  -1520       O  
+ATOM  12496  CB  PRO D 356     -52.013  54.322 -24.983  1.00 79.84           C  
+ANISOU12496  CB  PRO D 356     8581  11101  10654   2129    471  -2168       C  
+ATOM  12497  CG  PRO D 356     -51.462  54.467 -23.609  1.00 76.45           C  
+ANISOU12497  CG  PRO D 356     8483  10248  10316   1944    666  -1952       C  
+ATOM  12498  CD  PRO D 356     -49.982  54.300 -23.747  1.00 72.65           C  
+ANISOU12498  CD  PRO D 356     8271   9569   9762   1818    622  -1786       C  
+ATOM  12499  N   PHE D 357     -51.806  56.580 -27.443  1.00 76.53           N  
+ANISOU12499  N   PHE D 357     8342  11223   9512   2947    102  -1837       N  
+ATOM  12500  CA  PHE D 357     -52.082  57.929 -27.915  1.00 82.31           C  
+ANISOU12500  CA  PHE D 357     9245  12050   9980   3377     56  -1581       C  
+ATOM  12501  C   PHE D 357     -53.382  58.483 -27.346  1.00 85.35           C  
+ANISOU12501  C   PHE D 357     9456  12521  10453   3630    111  -1599       C  
+ATOM  12502  O   PHE D 357     -54.405  57.798 -27.337  1.00 91.90           O  
+ANISOU12502  O   PHE D 357     9831  13658  11430   3604     49  -1895       O  
+ATOM  12503  CB  PHE D 357     -52.132  57.955 -29.443  1.00 86.47           C  
+ANISOU12503  CB  PHE D 357     9630  13027  10199   3633   -176  -1619       C  
+ATOM  12504  CG  PHE D 357     -50.785  57.839 -30.093  1.00 85.83           C  
+ANISOU12504  CG  PHE D 357     9818  12839   9955   3491   -179  -1507       C  
+ATOM  12505  CD1 PHE D 357     -50.127  56.621 -30.143  1.00 84.94           C  
+ANISOU12505  CD1 PHE D 357     9588  12690   9997   3123   -178  -1742       C  
+ATOM  12506  CD2 PHE D 357     -50.176  58.948 -30.653  1.00 89.53           C  
+ANISOU12506  CD2 PHE D 357    10662  13222  10135   3732   -147  -1164       C  
+ATOM  12507  CE1 PHE D 357     -48.887  56.512 -30.738  1.00 86.40           C  
+ANISOU12507  CE1 PHE D 357     9982  12797  10049   3012   -160  -1653       C  
+ATOM  12508  CE2 PHE D 357     -48.937  58.846 -31.251  1.00 89.52           C  
+ANISOU12508  CE2 PHE D 357    10879  13142   9994   3579   -115  -1075       C  
+ATOM  12509  CZ  PHE D 357     -48.291  57.625 -31.293  1.00 86.67           C  
+ANISOU12509  CZ  PHE D 357    10355  12787   9788   3226   -129  -1328       C  
+ATOM  12510  N   PRO D 358     -53.341  59.736 -26.869  1.00 86.12           N  
+ANISOU12510  N   PRO D 358     9909  12337  10477   3864    256  -1303       N  
+ATOM  12511  CA  PRO D 358     -54.530  60.449 -26.394  1.00 86.65           C  
+ANISOU12511  CA  PRO D 358     9855  12461  10609   4194    339  -1282       C  
+ATOM  12512  C   PRO D 358     -55.431  60.887 -27.547  1.00 89.56           C  
+ANISOU12512  C   PRO D 358     9935  13333  10761   4717    117  -1264       C  
+ATOM  12513  O   PRO D 358     -54.956  61.501 -28.503  1.00 94.98           O  
+ANISOU12513  O   PRO D 358    10852  14085  11153   4983     13  -1028       O  
+ATOM  12514  CB  PRO D 358     -53.944  61.658 -25.661  1.00 81.23           C  
+ANISOU12514  CB  PRO D 358     9728  11252   9882   4256    582   -969       C  
+ATOM  12515  CG  PRO D 358     -52.630  61.892 -26.320  1.00 80.71           C  
+ANISOU12515  CG  PRO D 358    10024  11028   9616   4152    541   -769       C  
+ATOM  12516  CD  PRO D 358     -52.113  60.534 -26.705  1.00 77.40           C  
+ANISOU12516  CD  PRO D 358     9347  10812   9250   3795    385   -998       C  
+ATOM  12517  N   GLN D 359     -56.718  60.570 -27.451  1.00 94.45           N  
+ANISOU12517  N   GLN D 359    10045  14331  11512   4863     50  -1508       N  
+ATOM  12518  CA  GLN D 359     -57.665  60.896 -28.511  1.00 96.41           C  
+ANISOU12518  CA  GLN D 359     9918  15164  11547   5376   -209  -1528       C  
+ATOM  12519  C   GLN D 359     -58.349  62.237 -28.265  1.00103.22           C  
+ANISOU12519  C   GLN D 359    10917  15939  12363   5950    -98  -1241       C  
+ATOM  12520  O   GLN D 359     -58.571  62.635 -27.121  1.00102.34           O  
+ANISOU12520  O   GLN D 359    10957  15444  12483   5899    185  -1207       O  
+ATOM  12521  CB  GLN D 359     -58.708  59.786 -28.653  1.00 95.80           C  
+ANISOU12521  CB  GLN D 359     9130  15632  11638   5217   -368  -1998       C  
+ATOM  12522  CG  GLN D 359     -58.102  58.408 -28.871  1.00 92.94           C  
+ANISOU12522  CG  GLN D 359     8644  15302  11368   4650   -429  -2314       C  
+ATOM  12523  CD  GLN D 359     -57.219  58.348 -30.103  1.00 91.10           C  
+ANISOU12523  CD  GLN D 359     8599  15224  10790   4703   -643  -2221       C  
+ATOM  12524  OE1 GLN D 359     -57.513  58.969 -31.125  1.00 92.76           O  
+ANISOU12524  OE1 GLN D 359     8748  15841  10656   5166   -869  -2086       O  
+ATOM  12525  NE2 GLN D 359     -56.124  57.602 -30.009  1.00 96.69           N  
+ANISOU12525  NE2 GLN D 359     9543  15621  11574   4254   -560  -2278       N  
+ATOM  12526  N   GLY D 360     -58.683  62.927 -29.350  1.00108.13           N  
+ANISOU12526  N   GLY D 360    11501  16918  12667   6518   -310  -1031       N  
+ATOM  12527  CA  GLY D 360     -59.294  64.240 -29.270  1.00100.89           C  
+ANISOU12527  CA  GLY D 360    10749  15901  11684   7157   -206   -705       C  
+ATOM  12528  C   GLY D 360     -58.401  65.283 -29.909  1.00100.15           C  
+ANISOU12528  C   GLY D 360    11304  15471  11278   7446   -146   -229       C  
+ATOM  12529  O   GLY D 360     -57.263  64.990 -30.271  1.00 93.81           O  
+ANISOU12529  O   GLY D 360    10817  14484  10342   7091   -152   -172       O  
+ATOM  12530  N   LYS D 361     -58.912  66.501 -30.047  1.00105.60           N  
+ANISOU12530  N   LYS D 361    12231  16026  11865   7950    -54    115       N  
+ATOM  12531  CA  LYS D 361     -58.168  67.572 -30.702  1.00111.25           C  
+ANISOU12531  CA  LYS D 361    13584  16402  12284   8246     50    594       C  
+ATOM  12532  C   LYS D 361     -56.891  67.923 -29.941  1.00115.60           C  
+ANISOU12532  C   LYS D 361    14772  16182  12970   7917    411    724       C  
+ATOM  12533  O   LYS D 361     -55.814  68.028 -30.532  1.00116.77           O  
+ANISOU12533  O   LYS D 361    15310  16150  12905   7729    430    910       O  
+ATOM  12534  CB  LYS D 361     -59.046  68.816 -30.853  1.00112.37           C  
+ANISOU12534  CB  LYS D 361    13874  16467  12353   8753    141    909       C  
+ATOM  12535  N   LYS D 362     -57.021  68.098 -28.629  1.00117.37           N  
+ANISOU12535  N   LYS D 362    15099  15966  13531   7687    701    593       N  
+ATOM  12536  CA  LYS D 362     -55.892  68.461 -27.777  1.00108.31           C  
+ANISOU12536  CA  LYS D 362    14537  14107  12510   7199   1034    654       C  
+ATOM  12537  C   LYS D 362     -54.788  67.401 -27.770  1.00 98.69           C  
+ANISOU12537  C   LYS D 362    13292  12913  11292   6508    927    452       C  
+ATOM  12538  O   LYS D 362     -53.606  67.730 -27.679  1.00 97.15           O  
+ANISOU12538  O   LYS D 362    13574  12290  11047   6187   1092    591       O  
+ATOM  12539  CB  LYS D 362     -56.374  68.716 -26.347  1.00 97.50           C  
+ANISOU12539  CB  LYS D 362    13204  12380  11463   7081   1328    486       C  
+ATOM  12540  N   GLY D 363     -55.177  66.133 -27.858  1.00102.00           N  
+ANISOU12540  N   GLY D 363    13143  13825  11788   6280    671    113       N  
+ATOM  12541  CA  GLY D 363     -54.219  65.042 -27.918  1.00 98.61           C  
+ANISOU12541  CA  GLY D 363    12648  13441  11378   5697    567    -82       C  
+ATOM  12542  C   GLY D 363     -53.460  65.014 -29.232  1.00 98.09           C  
+ANISOU12542  C   GLY D 363    12712  13567  10992   5761    401     82       C  
+ATOM  12543  O   GLY D 363     -52.225  64.934 -29.265  1.00 94.65           O  
+ANISOU12543  O   GLY D 363    12594  12852  10514   5391    491    151       O  
+ATOM  12544  N   GLU D 364     -54.212  65.090 -30.326  1.00 99.15           N  
+ANISOU12544  N   GLU D 364    12578  14219  10875   6244    157    138       N  
+ATOM  12545  CA  GLU D 364     -53.635  65.061 -31.662  1.00100.96           C  
+ANISOU12545  CA  GLU D 364    12909  14721  10731   6363    -12    290       C  
+ATOM  12546  C   GLU D 364     -52.775  66.304 -31.865  1.00104.37           C  
+ANISOU12546  C   GLU D 364    14024  14640  10992   6505    255    744       C  
+ATOM  12547  O   GLU D 364     -51.911  66.342 -32.742  1.00105.04           O  
+ANISOU12547  O   GLU D 364    14344  14756  10810   6438    243    901       O  
+ATOM  12548  CB  GLU D 364     -54.736  64.974 -32.719  1.00102.49           C  
+ANISOU12548  CB  GLU D 364    12668  15626  10646   6902   -344    264       C  
+ATOM  12549  CG  GLU D 364     -55.599  63.726 -32.590  1.00104.22           C  
+ANISOU12549  CG  GLU D 364    12178  16379  11043   6704   -592   -240       C  
+ATOM  12550  CD  GLU D 364     -56.616  63.583 -33.706  1.00113.57           C  
+ANISOU12550  CD  GLU D 364    12878  18360  11914   7183   -964   -326       C  
+ATOM  12551  OE1 GLU D 364     -56.421  64.196 -34.776  1.00117.74           O  
+ANISOU12551  OE1 GLU D 364    13634  19094  12009   7596  -1080    -10       O  
+ATOM  12552  OE2 GLU D 364     -57.614  62.858 -33.509  1.00114.93           O  
+ANISOU12552  OE2 GLU D 364    12437  18975  12259   7135  -1135   -715       O  
+ATOM  12553  N   GLU D 365     -53.034  67.325 -31.052  1.00110.11           N  
+ANISOU12553  N   GLU D 365    15075  14882  11881   6689    530    937       N  
+ATOM  12554  CA  GLU D 365     -52.218  68.532 -31.042  1.00113.91           C  
+ANISOU12554  CA  GLU D 365    16241  14757  12281   6736    863   1320       C  
+ATOM  12555  C   GLU D 365     -50.801  68.211 -30.571  1.00112.43           C  
+ANISOU12555  C   GLU D 365    16313  14193  12212   6038   1029   1218       C  
+ATOM  12556  O   GLU D 365     -49.853  68.920 -30.906  1.00120.69           O  
+ANISOU12556  O   GLU D 365    17846  14879  13131   5942   1249   1478       O  
+ATOM  12557  CB  GLU D 365     -52.846  69.608 -30.151  1.00102.97           C  
+ANISOU12557  CB  GLU D 365    15125  12904  11096   7034   1151   1462       C  
+ATOM  12558  N   GLN D 366     -50.659  67.129 -29.808  1.00 99.35           N  
+ANISOU12558  N   GLN D 366    14314  12636  10799   5559    930    846       N  
+ATOM  12559  CA  GLN D 366     -49.356  66.742 -29.275  1.00101.13           C  
+ANISOU12559  CA  GLN D 366    14710  12567  11148   4934   1048    738       C  
+ATOM  12560  C   GLN D 366     -48.959  65.320 -29.669  1.00103.84           C  
+ANISOU12560  C   GLN D 366    14637  13322  11495   4612    793    462       C  
+ATOM  12561  O   GLN D 366     -48.028  64.752 -29.093  1.00 96.18           O  
+ANISOU12561  O   GLN D 366    13679  12186  10679   4120    842    320       O  
+ATOM  12562  CB  GLN D 366     -49.365  66.845 -27.746  1.00 97.30           C  
+ANISOU12562  CB  GLN D 366    14314  11690  10966   4623   1236    583       C  
+ATOM  12563  CG  GLN D 366     -49.612  68.236 -27.186  1.00108.66           C  
+ANISOU12563  CG  GLN D 366    16217  12624  12447   4842   1554    790       C  
+ATOM  12564  CD  GLN D 366     -48.509  69.209 -27.541  1.00116.46           C  
+ANISOU12564  CD  GLN D 366    17763  13178  13309   4715   1810   1053       C  
+ATOM  12565  OE1 GLN D 366     -47.451  69.216 -26.913  1.00107.43           O  
+ANISOU12565  OE1 GLN D 366    16817  11744  12259   4191   1949    962       O  
+ATOM  12566  NE2 GLN D 366     -48.754  70.047 -28.541  1.00124.93           N  
+ANISOU12566  NE2 GLN D 366    19090  14214  14162   5193   1883   1386       N  
+ATOM  12567  N   TRP D 367     -49.630  64.768 -30.676  1.00106.92           N  
+ANISOU12567  N   TRP D 367    14669  14252  11703   4902    527    383       N  
+ATOM  12568  CA  TRP D 367     -49.306  63.424 -31.158  1.00101.70           C  
+ANISOU12568  CA  TRP D 367    13632  13969  11039   4618    312     88       C  
+ATOM  12569  C   TRP D 367     -47.893  63.324 -31.740  1.00 99.55           C  
+ANISOU12569  C   TRP D 367    13603  13590  10631   4334    393    178       C  
+ATOM  12570  O   TRP D 367     -47.232  62.290 -31.619  1.00 99.51           O  
+ANISOU12570  O   TRP D 367    13407  13641  10761   3948    342    -57       O  
+ATOM  12571  CB  TRP D 367     -50.321  62.965 -32.211  1.00 98.08           C  
+ANISOU12571  CB  TRP D 367    12760  14145  10361   4986     15    -43       C  
+ATOM  12572  CG  TRP D 367     -51.522  62.275 -31.638  1.00 98.48           C  
+ANISOU12572  CG  TRP D 367    12316  14455  10648   5006   -125   -363       C  
+ATOM  12573  CD1 TRP D 367     -51.842  62.144 -30.319  1.00 96.20           C  
+ANISOU12573  CD1 TRP D 367    11972  13869  10711   4795     18   -482       C  
+ATOM  12574  CD2 TRP D 367     -52.552  61.596 -32.369  1.00105.96           C  
+ANISOU12574  CD2 TRP D 367    12738  16035  11488   5211   -417   -630       C  
+ATOM  12575  NE1 TRP D 367     -53.014  61.441 -30.182  1.00 94.18           N  
+ANISOU12575  NE1 TRP D 367    11196  13993  10595   4855   -134   -788       N  
+ATOM  12576  CE2 TRP D 367     -53.470  61.091 -31.426  1.00102.29           C  
+ANISOU12576  CE2 TRP D 367    11906  15600  11359   5096   -411   -903       C  
+ATOM  12577  CE3 TRP D 367     -52.791  61.372 -33.728  1.00113.18           C  
+ANISOU12577  CE3 TRP D 367    13450  17522  12032   5465   -680   -684       C  
+ATOM  12578  CZ2 TRP D 367     -54.606  60.375 -31.798  1.00107.00           C  
+ANISOU12578  CZ2 TRP D 367    11916  16767  11973   5196   -646  -1244       C  
+ATOM  12579  CZ3 TRP D 367     -53.920  60.661 -34.096  1.00113.77           C  
+ANISOU12579  CZ3 TRP D 367    12941  18194  12094   5576   -950  -1037       C  
+ATOM  12580  CH2 TRP D 367     -54.813  60.172 -33.135  1.00112.39           C  
+ANISOU12580  CH2 TRP D 367    12382  18024  12299   5428   -927  -1322       C  
+ATOM  12581  N   ASP D 368     -47.439  64.403 -32.372  1.00100.61           N  
+ANISOU12581  N   ASP D 368    14159  13557  10510   4538    548    528       N  
+ATOM  12582  CA  ASP D 368     -46.133  64.429 -33.028  1.00100.94           C  
+ANISOU12582  CA  ASP D 368    14434  13523  10397   4294    667    635       C  
+ATOM  12583  C   ASP D 368     -44.985  64.376 -32.016  1.00 99.27           C  
+ANISOU12583  C   ASP D 368    14375  12874  10467   3761    869    574       C  
+ATOM  12584  O   ASP D 368     -44.087  63.526 -32.110  1.00104.25           O  
+ANISOU12584  O   ASP D 368    14844  13596  11170   3413    836    401       O  
+ATOM  12585  CB  ASP D 368     -46.020  65.685 -33.899  1.00109.29           C  
+ANISOU12585  CB  ASP D 368    15947  14465  11114   4653    838   1059       C  
+ATOM  12586  CG  ASP D 368     -44.757  65.711 -34.735  1.00111.17           C  
+ANISOU12586  CG  ASP D 368    16403  14691  11147   4426    985   1174       C  
+ATOM  12587  OD1 ASP D 368     -44.657  64.913 -35.691  1.00117.53           O  
+ANISOU12587  OD1 ASP D 368    16963  15961  11733   4454    806   1036       O  
+ATOM  12588  OD2 ASP D 368     -43.868  66.538 -34.444  1.00106.70           O  
+ANISOU12588  OD2 ASP D 368    16247  13657  10637   4201   1301   1379       O  
+ATOM  12589  N   LYS D 369     -45.033  65.282 -31.043  1.00102.10           N  
+ANISOU12589  N   LYS D 369    15030  12782  10980   3715   1074    700       N  
+ATOM  12590  CA  LYS D 369     -44.052  65.323 -29.965  1.00100.64           C  
+ANISOU12590  CA  LYS D 369    14979  12226  11035   3219   1238    620       C  
+ATOM  12591  C   LYS D 369     -44.127  64.034 -29.159  1.00 93.80           C  
+ANISOU12591  C   LYS D 369    13699  11523  10417   2952   1048    298       C  
+ATOM  12592  O   LYS D 369     -43.110  63.516 -28.687  1.00 86.30           O  
+ANISOU12592  O   LYS D 369    12690  10499   9601   2550   1065    189       O  
+ATOM  12593  CB  LYS D 369     -44.283  66.537 -29.063  1.00 94.08           C  
+ANISOU12593  CB  LYS D 369    14540  10910  10297   3245   1488    761       C  
+ATOM  12594  N   TYR D 370     -45.348  63.525 -29.014  1.00 88.55           N  
+ANISOU12594  N   TYR D 370    12743  11087   9815   3191    879    157       N  
+ATOM  12595  CA  TYR D 370     -45.583  62.264 -28.326  1.00 80.86           C  
+ANISOU12595  CA  TYR D 370    11391  10255   9076   2970    732   -133       C  
+ATOM  12596  C   TYR D 370     -44.793  61.153 -29.025  1.00 80.38           C  
+ANISOU12596  C   TYR D 370    11095  10440   9006   2772    611   -282       C  
+ATOM  12597  O   TYR D 370     -44.075  60.387 -28.374  1.00 78.27           O  
+ANISOU12597  O   TYR D 370    10725  10082   8931   2439    610   -405       O  
+ATOM  12598  CB  TYR D 370     -47.081  61.949 -28.308  1.00 79.55           C  
+ANISOU12598  CB  TYR D 370    10924  10345   8956   3271    598   -269       C  
+ATOM  12599  CG  TYR D 370     -47.529  60.949 -27.267  1.00 76.14           C  
+ANISOU12599  CG  TYR D 370    10206   9917   8806   3040    556   -524       C  
+ATOM  12600  CD1 TYR D 370     -47.437  61.241 -25.912  1.00 74.46           C  
+ANISOU12600  CD1 TYR D 370    10169   9365   8756   2839    712   -503       C  
+ATOM  12601  CD2 TYR D 370     -48.076  59.729 -27.638  1.00 80.20           C  
+ANISOU12601  CD2 TYR D 370    10295  10768   9408   3014    385   -792       C  
+ATOM  12602  CE1 TYR D 370     -47.857  60.336 -24.956  1.00 72.58           C  
+ANISOU12602  CE1 TYR D 370     9710   9127   8741   2641    704   -696       C  
+ATOM  12603  CE2 TYR D 370     -48.500  58.818 -26.689  1.00 80.68           C  
+ANISOU12603  CE2 TYR D 370    10133  10784   9737   2792    400   -999       C  
+ATOM  12604  CZ  TYR D 370     -48.388  59.127 -25.349  1.00 72.01           C  
+ANISOU12604  CZ  TYR D 370     9235   9350   8776   2619    562   -926       C  
+ATOM  12605  OH  TYR D 370     -48.808  58.224 -24.399  1.00 70.71           O  
+ANISOU12605  OH  TYR D 370     8886   9137   8843   2406    605  -1094       O  
+ATOM  12606  N   ARG D 371     -44.888  61.106 -30.355  1.00 86.93           N  
+ANISOU12606  N   ARG D 371    11861  11580   9589   3001    522   -258       N  
+ATOM  12607  CA  ARG D 371     -44.173  60.100 -31.141  1.00 86.24           C  
+ANISOU12607  CA  ARG D 371    11568  11736   9464   2846    439   -424       C  
+ATOM  12608  C   ARG D 371     -42.658  60.245 -31.053  1.00 83.75           C  
+ANISOU12608  C   ARG D 371    11441  11203   9178   2536    600   -323       C  
+ATOM  12609  O   ARG D 371     -41.946  59.254 -30.850  1.00 81.71           O  
+ANISOU12609  O   ARG D 371    10982  10968   9094   2281    571   -496       O  
+ATOM  12610  CB  ARG D 371     -44.587  60.151 -32.619  1.00 88.11           C  
+ANISOU12610  CB  ARG D 371    11741  12382   9353   3166    325   -414       C  
+ATOM  12611  CG  ARG D 371     -45.948  59.555 -32.946  1.00 87.68           C  
+ANISOU12611  CG  ARG D 371    11324  12723   9268   3405     93   -649       C  
+ATOM  12612  CD  ARG D 371     -46.123  59.431 -34.455  1.00 91.26           C  
+ANISOU12612  CD  ARG D 371    11689  13656   9331   3654    -49   -692       C  
+ATOM  12613  NE  ARG D 371     -47.364  58.764 -34.841  1.00 94.01           N  
+ANISOU12613  NE  ARG D 371    11622  14464   9633   3830   -300   -990       N  
+ATOM  12614  CZ  ARG D 371     -48.472  59.401 -35.196  1.00108.02           C  
+ANISOU12614  CZ  ARG D 371    13325  16525  11192   4248   -444   -891       C  
+ATOM  12615  NH1 ARG D 371     -48.497  60.725 -35.201  1.00108.03           N  
+ANISOU12615  NH1 ARG D 371    13698  16333  11018   4562   -333   -470       N  
+ATOM  12616  NH2 ARG D 371     -49.556  58.717 -35.539  1.00118.90           N  
+ANISOU12616  NH2 ARG D 371    14254  18378  12544   4356   -685  -1219       N  
+ATOM  12617  N   ARG D 372     -42.159  61.468 -31.212  1.00 87.13           N  
+ANISOU12617  N   ARG D 372    12242  11414   9449   2560    787    -48       N  
+ATOM  12618  CA  ARG D 372     -40.718  61.678 -31.117  1.00 88.57           C  
+ANISOU12618  CA  ARG D 372    12566  11415   9672   2226    960     23       C  
+ATOM  12619  C   ARG D 372     -40.192  61.260 -29.751  1.00 86.08           C  
+ANISOU12619  C   ARG D 372    12152  10893   9662   1882    953    -94       C  
+ATOM  12620  O   ARG D 372     -39.109  60.679 -29.653  1.00 86.99           O  
+ANISOU12620  O   ARG D 372    12125  11041   9886   1618    964   -175       O  
+ATOM  12621  CB  ARG D 372     -40.347  63.132 -31.413  1.00 94.66           C  
+ANISOU12621  CB  ARG D 372    13785  11926  10257   2262   1212    325       C  
+ATOM  12622  CG  ARG D 372     -40.729  63.570 -32.817  1.00102.80           C  
+ANISOU12622  CG  ARG D 372    14962  13170  10929   2626   1237    508       C  
+ATOM  12623  CD  ARG D 372     -40.074  64.882 -33.201  1.00111.81           C  
+ANISOU12623  CD  ARG D 372    16575  14010  11899   2593   1556    826       C  
+ATOM  12624  NE  ARG D 372     -40.119  65.087 -34.646  1.00115.46           N  
+ANISOU12624  NE  ARG D 372    17162  14731  11978   2880   1597   1008       N  
+ATOM  12625  CZ  ARG D 372     -39.135  65.641 -35.345  1.00120.04           C  
+ANISOU12625  CZ  ARG D 372    18010  15215  12385   2737   1873   1196       C  
+ATOM  12626  NH1 ARG D 372     -38.028  66.027 -34.727  1.00118.89           N  
+ANISOU12626  NH1 ARG D 372    17985  14737  12450   2286   2119   1192       N  
+ATOM  12627  NH2 ARG D 372     -39.248  65.795 -36.658  1.00126.62           N  
+ANISOU12627  NH2 ARG D 372    18975  16316  12820   3027   1907   1376       N  
+ATOM  12628  N   ASP D 373     -40.963  61.536 -28.702  1.00 85.18           N  
+ANISOU12628  N   ASP D 373    12100  10596   9667   1910    935    -99       N  
+ATOM  12629  CA  ASP D 373     -40.559  61.140 -27.359  1.00 83.25           C  
+ANISOU12629  CA  ASP D 373    11785  10194   9652   1611    915   -196       C  
+ATOM  12630  C   ASP D 373     -40.534  59.622 -27.241  1.00 79.73           C  
+ANISOU12630  C   ASP D 373    10962   9950   9380   1552    744   -398       C  
+ATOM  12631  O   ASP D 373     -39.616  59.056 -26.643  1.00 80.12           O  
+ANISOU12631  O   ASP D 373    10905   9968   9571   1305    723   -443       O  
+ATOM  12632  CB  ASP D 373     -41.488  61.722 -26.300  1.00 91.63           C  
+ANISOU12632  CB  ASP D 373    13004  11040  10772   1672    958   -177       C  
+ATOM  12633  CG  ASP D 373     -40.983  61.471 -24.895  1.00112.33           C  
+ANISOU12633  CG  ASP D 373    15620  13511  13548   1350    956   -249       C  
+ATOM  12634  OD1 ASP D 373     -39.775  61.195 -24.735  1.00123.08           O  
+ANISOU12634  OD1 ASP D 373    16920  14896  14947   1077    943   -262       O  
+ATOM  12635  OD2 ASP D 373     -41.794  61.525 -23.953  1.00110.01           O  
+ANISOU12635  OD2 ASP D 373    15364  13113  13321   1383    963   -294       O  
+HETATM12636  N   MSE D 374     -41.558  58.973 -27.796  1.00 77.48           N  
+ANISOU12636  N   MSE D 374    10476   9872   9092   1784    630   -524       N  
+HETATM12637  CA  MSE D 374     -41.585  57.515 -27.869  1.00 75.38           C  
+ANISOU12637  CA  MSE D 374     9879   9760   9000   1727    515   -743       C  
+HETATM12638  C   MSE D 374     -40.299  56.965 -28.454  1.00 76.78           C  
+ANISOU12638  C   MSE D 374     9962  10018   9193   1589    536   -776       C  
+HETATM12639  O   MSE D 374     -39.550  56.243 -27.797  1.00 76.53           O  
+ANISOU12639  O   MSE D 374     9816   9906   9356   1406    526   -813       O  
+HETATM12640  CB  MSE D 374     -42.747  57.022 -28.729  1.00 75.96           C  
+ANISOU12640  CB  MSE D 374     9745  10104   9011   1967    407   -918       C  
+HETATM12641  CG  MSE D 374     -44.123  57.303 -28.200  1.00 99.39           C  
+ANISOU12641  CG  MSE D 374    12679  13069  12015   2122    374   -947       C  
+HETATM12642 SE   MSE D 374     -45.328  56.001 -28.968  1.00106.30          SE  
+ANISOU12642 SE   MSE D 374    13108  14320  12961   2232    215  -1319      SE  
+HETATM12643  CE  MSE D 374     -44.466  54.443 -28.195  1.00 92.93           C  
+ANISOU12643  CE  MSE D 374    11274  12407  11629   1874    272  -1479       C  
+ATOM  12644  N   ILE D 375     -40.058  57.335 -29.704  1.00 78.48           N  
+ANISOU12644  N   ILE D 375    10228  10409   9182   1708    573   -745       N  
+ATOM  12645  CA  ILE D 375     -38.984  56.767 -30.499  1.00 83.07           C  
+ANISOU12645  CA  ILE D 375    10687  11127   9748   1623    619   -818       C  
+ATOM  12646  C   ILE D 375     -37.608  57.143 -29.938  1.00 86.66           C  
+ANISOU12646  C   ILE D 375    11214  11427  10287   1367    731   -687       C  
+ATOM  12647  O   ILE D 375     -36.629  56.424 -30.148  1.00 85.89           O  
+ANISOU12647  O   ILE D 375    10928  11407  10300   1262    757   -770       O  
+ATOM  12648  CB  ILE D 375     -39.126  57.217 -31.970  1.00 85.06           C  
+ANISOU12648  CB  ILE D 375    11025  11624   9668   1820    657   -790       C  
+ATOM  12649  CG1 ILE D 375     -40.518  56.843 -32.487  1.00 80.50           C  
+ANISOU12649  CG1 ILE D 375    10318  11282   8986   2073    499   -951       C  
+ATOM  12650  CG2 ILE D 375     -38.044  56.612 -32.846  1.00 82.14           C  
+ANISOU12650  CG2 ILE D 375    10528  11418   9263   1735    742   -895       C  
+ATOM  12651  CD1 ILE D 375     -40.751  57.168 -33.940  1.00 84.02           C  
+ANISOU12651  CD1 ILE D 375    10821  12054   9049   2304    485   -939       C  
+ATOM  12652  N   THR D 376     -37.543  58.254 -29.206  1.00 88.74           N  
+ANISOU12652  N   THR D 376    11727  11481  10509   1265    803   -509       N  
+ATOM  12653  CA  THR D 376     -36.282  58.704 -28.615  1.00 87.69           C  
+ANISOU12653  CA  THR D 376    11641  11235  10441    973    898   -426       C  
+ATOM  12654  C   THR D 376     -35.701  57.674 -27.643  1.00 89.88           C  
+ANISOU12654  C   THR D 376    11656  11525  10971    830    778   -520       C  
+ATOM  12655  O   THR D 376     -34.482  57.519 -27.545  1.00 90.94           O  
+ANISOU12655  O   THR D 376    11647  11727  11179    652    808   -520       O  
+ATOM  12656  CB  THR D 376     -36.457  60.051 -27.884  1.00 89.04           C  
+ANISOU12656  CB  THR D 376    12147  11149  10536    861   1004   -278       C  
+ATOM  12657  OG1 THR D 376     -37.040  61.007 -28.777  1.00 89.81           O  
+ANISOU12657  OG1 THR D 376    12522  11196  10407   1059   1132   -142       O  
+ATOM  12658  CG2 THR D 376     -35.116  60.581 -27.396  1.00 93.35           C  
+ANISOU12658  CG2 THR D 376    12720  11623  11125    505   1112   -244       C  
+ATOM  12659  N   ARG D 377     -36.576  56.955 -26.947  1.00 94.58           N  
+ANISOU12659  N   ARG D 377    12176  12066  11694    925    653   -588       N  
+ATOM  12660  CA  ARG D 377     -36.145  55.924 -26.006  1.00 93.90           C  
+ANISOU12660  CA  ARG D 377    11888  11962  11827    845    550   -627       C  
+ATOM  12661  C   ARG D 377     -35.509  54.729 -26.716  1.00 96.99           C  
+ANISOU12661  C   ARG D 377    11999  12492  12362    919    541   -744       C  
+ATOM  12662  O   ARG D 377     -34.807  53.931 -26.095  1.00101.67           O  
+ANISOU12662  O   ARG D 377    12416  13081  13135    880    485   -734       O  
+ATOM  12663  CB  ARG D 377     -37.323  55.452 -25.149  1.00 87.70           C  
+ANISOU12663  CB  ARG D 377    11130  11056  11134    923    478   -659       C  
+ATOM  12664  CG  ARG D 377     -38.108  56.577 -24.493  1.00 85.23           C  
+ANISOU12664  CG  ARG D 377    11089  10604  10692    897    518   -578       C  
+ATOM  12665  CD  ARG D 377     -39.240  56.035 -23.631  1.00 92.49           C  
+ANISOU12665  CD  ARG D 377    11998  11429  11716    960    481   -624       C  
+ATOM  12666  NE  ARG D 377     -38.752  55.220 -22.521  1.00 97.26           N  
+ANISOU12666  NE  ARG D 377    12524  11979  12451    842    421   -583       N  
+ATOM  12667  CZ  ARG D 377     -38.608  55.664 -21.276  1.00100.53           C  
+ANISOU12667  CZ  ARG D 377    13092  12308  12799    698    410   -490       C  
+ATOM  12668  NH1 ARG D 377     -38.916  56.919 -20.977  1.00107.06           N  
+ANISOU12668  NH1 ARG D 377    14163  13049  13467    631    484   -464       N  
+ATOM  12669  NH2 ARG D 377     -38.158  54.853 -20.327  1.00 99.72           N  
+ANISOU12669  NH2 ARG D 377    12916  12201  12774    635    336   -422       N  
+ATOM  12670  N   THR D 378     -35.756  54.614 -28.018  1.00 91.73           N  
+ANISOU12670  N   THR D 378    11300  11954  11598   1050    602   -852       N  
+ATOM  12671  CA  THR D 378     -35.355  53.433 -28.774  1.00 81.59           C  
+ANISOU12671  CA  THR D 378     9774  10783  10443   1138    624  -1024       C  
+ATOM  12672  C   THR D 378     -34.282  53.743 -29.814  1.00 85.51           C  
+ANISOU12672  C   THR D 378    10216  11455  10821   1103    754  -1032       C  
+ATOM  12673  O   THR D 378     -34.038  54.904 -30.144  1.00 85.83           O  
+ANISOU12673  O   THR D 378    10436  11530  10647   1022    841   -904       O  
+ATOM  12674  CB  THR D 378     -36.560  52.798 -29.491  1.00 79.86           C  
+ANISOU12674  CB  THR D 378     9516  10621  10204   1300    596  -1232       C  
+ATOM  12675  OG1 THR D 378     -36.980  53.644 -30.568  1.00 82.02           O  
+ANISOU12675  OG1 THR D 378     9924  11071  10170   1391    629  -1231       O  
+ATOM  12676  CG2 THR D 378     -37.712  52.606 -28.521  1.00 74.50           C  
+ANISOU12676  CG2 THR D 378     8885   9786   9635   1311    511  -1233       C  
+ATOM  12677  N   GLY D 379     -33.645  52.693 -30.325  1.00 87.59           N  
+ANISOU12677  N   GLY D 379    10243  11802  11234   1164    804  -1183       N  
+ATOM  12678  CA  GLY D 379     -32.614  52.833 -31.338  1.00 84.39           C  
+ANISOU12678  CA  GLY D 379     9746  11584  10735   1138    963  -1225       C  
+ATOM  12679  C   GLY D 379     -32.877  51.981 -32.565  1.00 82.24           C  
+ANISOU12679  C   GLY D 379     9380  11450  10416   1291   1040  -1483       C  
+ATOM  12680  O   GLY D 379     -32.189  52.105 -33.579  1.00 83.66           O  
+ANISOU12680  O   GLY D 379     9518  11815  10453   1290   1200  -1545       O  
+ATOM  12681  N   VAL D 380     -33.880  51.113 -32.473  1.00 84.95           N  
+ANISOU12681  N   VAL D 380     9693  11712  10871   1396    947  -1658       N  
+ATOM  12682  CA  VAL D 380     -34.290  50.275 -33.596  1.00 81.49           C  
+ANISOU12682  CA  VAL D 380     9173  11409  10379   1505   1006  -1973       C  
+ATOM  12683  C   VAL D 380     -35.811  50.217 -33.663  1.00 83.53           C  
+ANISOU12683  C   VAL D 380     9512  11687  10540   1560    870  -2100       C  
+ATOM  12684  O   VAL D 380     -36.467  49.965 -32.657  1.00 81.82           O  
+ANISOU12684  O   VAL D 380     9297  11267  10523   1533    773  -2059       O  
+ATOM  12685  CB  VAL D 380     -33.729  48.838 -33.473  1.00 77.66           C  
+ANISOU12685  CB  VAL D 380     8463  10787  10257   1554   1092  -2173       C  
+ATOM  12686  CG1 VAL D 380     -34.377  47.917 -34.496  1.00 76.20           C  
+ANISOU12686  CG1 VAL D 380     8222  10688  10042   1622   1153  -2566       C  
+ATOM  12687  CG2 VAL D 380     -32.216  48.833 -33.626  1.00 86.17           C  
+ANISOU12687  CG2 VAL D 380     9389  11932  11419   1547   1238  -2095       C  
+ATOM  12688  N   SER D 381     -36.368  50.446 -34.848  1.00 79.12           N  
+ANISOU12688  N   SER D 381     9001  11407   9656   1642    864  -2257       N  
+ATOM  12689  CA  SER D 381     -37.817  50.440 -35.021  1.00 79.86           C  
+ANISOU12689  CA  SER D 381     9106  11616   9623   1711    711  -2403       C  
+ATOM  12690  C   SER D 381     -38.272  49.341 -35.976  1.00 76.85           C  
+ANISOU12690  C   SER D 381     8557  11421   9223   1731    722  -2850       C  
+ATOM  12691  O   SER D 381     -37.877  49.319 -37.140  1.00 76.10           O  
+ANISOU12691  O   SER D 381     8464  11593   8858   1781    799  -2995       O  
+ATOM  12692  CB  SER D 381     -38.297  51.801 -35.531  1.00 77.57           C  
+ANISOU12692  CB  SER D 381     9020  11546   8906   1828    640  -2183       C  
+ATOM  12693  OG  SER D 381     -37.943  52.839 -34.634  1.00 89.42           O  
+ANISOU12693  OG  SER D 381    10704  12831  10439   1778    661  -1817       O  
+ATOM  12694  N   ILE D 382     -39.105  48.431 -35.481  1.00 78.71           N  
+ANISOU12694  N   ILE D 382     8659  11513   9736   1667    670  -3087       N  
+ATOM  12695  CA  ILE D 382     -39.679  47.394 -36.332  1.00 87.63           C  
+ANISOU12695  CA  ILE D 382     9627  12805  10866   1631    685  -3573       C  
+ATOM  12696  C   ILE D 382     -41.085  47.801 -36.764  1.00 85.73           C  
+ANISOU12696  C   ILE D 382     9326  12909  10339   1682    478  -3720       C  
+ATOM  12697  O   ILE D 382     -41.888  48.240 -35.942  1.00 87.41           O  
+ANISOU12697  O   ILE D 382     9541  13039  10631   1689    365  -3558       O  
+ATOM  12698  CB  ILE D 382     -39.722  46.030 -35.619  1.00 85.92           C  
+ANISOU12698  CB  ILE D 382     9291  12196  11158   1497    808  -3797       C  
+ATOM  12699  CG1 ILE D 382     -38.321  45.630 -35.153  1.00 71.02           C  
+ANISOU12699  CG1 ILE D 382     7434   9999   9552   1518    987  -3613       C  
+ATOM  12700  CG2 ILE D 382     -40.297  44.963 -36.538  1.00 83.07           C  
+ANISOU12700  CG2 ILE D 382     8777  11973  10812   1408    863  -4360       C  
+ATOM  12701  CD1 ILE D 382     -38.288  44.353 -34.345  1.00 69.99           C  
+ANISOU12701  CD1 ILE D 382     7243   9425   9923   1451   1126  -3725       C  
+ATOM  12702  N   PHE D 383     -41.383  47.652 -38.051  1.00 90.90           N  
+ANISOU12702  N   PHE D 383     9909  13984  10645   1731    427  -4036       N  
+ATOM  12703  CA  PHE D 383     -42.660  48.120 -38.587  1.00 88.92           C  
+ANISOU12703  CA  PHE D 383     9565  14173  10047   1834    189  -4160       C  
+ATOM  12704  C   PHE D 383     -43.544  46.974 -39.069  1.00 92.74           C  
+ANISOU12704  C   PHE D 383     9774  14850  10612   1677    139  -4762       C  
+ATOM  12705  O   PHE D 383     -43.159  46.194 -39.935  1.00 86.03           O  
+ANISOU12705  O   PHE D 383     8871  14124   9694   1593    242  -5144       O  
+ATOM  12706  CB  PHE D 383     -42.418  49.120 -39.719  1.00 88.36           C  
+ANISOU12706  CB  PHE D 383     9651  14541   9381   2056    116  -3981       C  
+ATOM  12707  CG  PHE D 383     -41.659  50.342 -39.288  1.00 95.91           C  
+ANISOU12707  CG  PHE D 383    10890  15302  10250   2173    191  -3412       C  
+ATOM  12708  CD1 PHE D 383     -40.273  50.353 -39.280  1.00100.20           C  
+ANISOU12708  CD1 PHE D 383    11565  15622  10885   2099    419  -3251       C  
+ATOM  12709  CD2 PHE D 383     -42.335  51.475 -38.874  1.00 94.29           C  
+ANISOU12709  CD2 PHE D 383    10803  15129   9895   2346     52  -3062       C  
+ATOM  12710  CE1 PHE D 383     -39.579  51.477 -38.875  1.00 95.42           C  
+ANISOU12710  CE1 PHE D 383    11197  14843  10216   2145    503  -2778       C  
+ATOM  12711  CE2 PHE D 383     -41.648  52.599 -38.467  1.00 91.98           C  
+ANISOU12711  CE2 PHE D 383    10794  14611   9543   2411    157  -2581       C  
+ATOM  12712  CZ  PHE D 383     -40.268  52.600 -38.467  1.00 91.71           C  
+ANISOU12712  CZ  PHE D 383    10882  14366   9596   2284    381  -2451       C  
+ATOM  12713  N   LEU D 384     -44.736  46.885 -38.490  1.00101.73           N  
+ANISOU12713  N   LEU D 384    10732  16014  11906   1616      5  -4871       N  
+ATOM  12714  CA  LEU D 384     -45.678  45.814 -38.791  1.00101.64           C  
+ANISOU12714  CA  LEU D 384    10424  16159  12035   1399    -27  -5466       C  
+ATOM  12715  C   LEU D 384     -47.003  46.347 -39.326  1.00105.46           C  
+ANISOU12715  C   LEU D 384    10669  17252  12148   1516   -334  -5625       C  
+ATOM  12716  O   LEU D 384     -47.591  47.247 -38.729  1.00110.00           O  
+ANISOU12716  O   LEU D 384    11246  17869  12681   1686   -469  -5281       O  
+ATOM  12717  CB  LEU D 384     -45.932  44.973 -37.539  1.00 96.54           C  
+ANISOU12717  CB  LEU D 384     9716  14961  12005   1154    149  -5527       C  
+ATOM  12718  CG  LEU D 384     -44.707  44.509 -36.750  1.00 90.69           C  
+ANISOU12718  CG  LEU D 384     9197  13602  11659   1101    418  -5271       C  
+ATOM  12719  CD1 LEU D 384     -45.138  43.809 -35.476  1.00 92.88           C  
+ANISOU12719  CD1 LEU D 384     9440  13386  12463    905    564  -5261       C  
+ATOM  12720  CD2 LEU D 384     -43.839  43.593 -37.593  1.00 88.27           C  
+ANISOU12720  CD2 LEU D 384     8914  13235  11391   1031    607  -5605       C  
+ATOM  12721  N   TYR D 385     -47.461  45.799 -40.449  1.00112.13           N  
+ANISOU12721  N   TYR D 385    11300  18588  12717   1440   -444  -6156       N  
+ATOM  12722  CA  TYR D 385     -48.785  46.126 -40.977  1.00103.73           C  
+ANISOU12722  CA  TYR D 385     9919  18180  11315   1534   -766  -6394       C  
+ATOM  12723  C   TYR D 385     -48.977  47.626 -41.206  1.00106.21           C  
+ANISOU12723  C   TYR D 385    10363  18853  11140   1979  -1005  -5854       C  
+ATOM  12724  O   TYR D 385     -48.216  48.244 -41.949  1.00106.32           O  
+ANISOU12724  O   TYR D 385    10643  19026  10728   2202  -1009  -5590       O  
+ATOM  12725  CB  TYR D 385     -49.852  45.594 -40.016  1.00 95.37           C  
+ANISOU12725  CB  TYR D 385     8558  16943  10735   1290   -753  -6624       C  
+ATOM  12726  CG  TYR D 385     -49.728  44.114 -39.728  1.00 94.44           C  
+ANISOU12726  CG  TYR D 385     8354  16391  11138    845   -469  -7127       C  
+ATOM  12727  CD1 TYR D 385     -50.279  43.170 -40.585  1.00 99.60           C  
+ANISOU12727  CD1 TYR D 385     8716  17397  11729    571   -502  -7851       C  
+ATOM  12728  CD2 TYR D 385     -48.989  43.661 -38.643  1.00 90.92           C  
+ANISOU12728  CD2 TYR D 385     8146  15177  11220    711   -153  -6875       C  
+ATOM  12729  CE1 TYR D 385     -50.152  41.816 -40.331  1.00103.84           C  
+ANISOU12729  CE1 TYR D 385     9222  17461  12772    158   -188  -8316       C  
+ATOM  12730  CE2 TYR D 385     -48.847  42.313 -38.388  1.00100.36           C  
+ANISOU12730  CE2 TYR D 385     9314  15922  12896    354    140  -7282       C  
+ATOM  12731  CZ  TYR D 385     -49.430  41.395 -39.233  1.00104.76           C  
+ANISOU12731  CZ  TYR D 385     9607  16767  13431     72    144  -8002       C  
+ATOM  12732  OH  TYR D 385     -49.284  40.054 -38.971  1.00103.90           O  
+ANISOU12732  OH  TYR D 385     9515  16130  13834   -291    489  -8409       O  
+ATOM  12733  N   GLY D 386     -49.983  48.212 -40.562  1.00111.89           N  
+ANISOU12733  N   GLY D 386    10911  19669  11932   2113  -1165  -5683       N  
+ATOM  12734  CA  GLY D 386     -50.228  49.638 -40.699  1.00115.48           C  
+ANISOU12734  CA  GLY D 386    11509  20389  11978   2568  -1356  -5157       C  
+ATOM  12735  C   GLY D 386     -51.530  49.959 -41.412  1.00119.81           C  
+ANISOU12735  C   GLY D 386    11683  21718  12121   2810  -1723  -5367       C  
+ATOM  12736  O   GLY D 386     -51.536  50.698 -42.398  1.00126.18           O  
+ANISOU12736  O   GLY D 386    12587  23027  12330   3172  -1923  -5179       O  
+ATOM  12737  N   ASN D 387     -52.635  49.400 -40.927  1.00117.09           N  
+ANISOU12737  N   ASN D 387    10898  21502  12088   2618  -1806  -5751       N  
+ATOM  12738  CA  ASN D 387     -53.937  49.679 -41.521  1.00120.40           C  
+ANISOU12738  CA  ASN D 387    10867  22716  12163   2846  -2176  -5981       C  
+ATOM  12739  C   ASN D 387     -54.971  50.131 -40.498  1.00126.91           C  
+ANISOU12739  C   ASN D 387    11434  23479  13307   2955  -2219  -5832       C  
+ATOM  12740  O   ASN D 387     -54.935  49.724 -39.336  1.00126.97           O  
+ANISOU12740  O   ASN D 387    11466  22889  13887   2659  -1954  -5827       O  
+ATOM  12741  CB  ASN D 387     -54.450  48.440 -42.258  1.00109.57           C  
+ANISOU12741  CB  ASN D 387     9058  21810  10765   2466  -2284  -6794       C  
+ATOM  12742  N   LYS D 388     -55.912  50.953 -40.947  1.00122.87           N  
+ANISOU12742  N   LYS D 388    10666  23615  12405   3401  -2549  -5713       N  
+ATOM  12743  CA  LYS D 388     -56.929  51.491 -40.058  1.00117.42           C  
+ANISOU12743  CA  LYS D 388     9709  22930  11976   3583  -2591  -5557       C  
+ATOM  12744  C   LYS D 388     -58.245  51.733 -40.785  1.00125.75           C  
+ANISOU12744  C   LYS D 388    10178  24937  12665   3897  -3013  -5817       C  
+ATOM  12745  O   LYS D 388     -58.290  51.715 -42.014  1.00127.44           O  
+ANISOU12745  O   LYS D 388    10383  25677  12362   4034  -3204  -5931       O  
+ATOM  12746  CB  LYS D 388     -56.411  52.794 -39.446  1.00115.56           C  
+ANISOU12746  CB  LYS D 388     9989  22206  11712   3995  -2451  -4786       C  
+ATOM  12747  CG  LYS D 388     -56.111  53.861 -40.496  1.00122.16           C  
+ANISOU12747  CG  LYS D 388    11116  23420  11880   4557  -2658  -4348       C  
+ATOM  12748  CD  LYS D 388     -55.582  55.147 -39.885  1.00120.19           C  
+ANISOU12748  CD  LYS D 388    11408  22617  11642   4913  -2464  -3618       C  
+ATOM  12749  CE  LYS D 388     -56.632  55.844 -39.050  1.00127.63           C  
+ANISOU12749  CE  LYS D 388    12137  23552  12805   5214  -2494  -3433       C  
+ATOM  12750  NZ  LYS D 388     -56.111  57.129 -38.513  1.00126.91           N  
+ANISOU12750  NZ  LYS D 388    12611  22905  12705   5556  -2283  -2758       N  
+ATOM  12751  N   ILE D 389     -59.311  51.968 -40.026  1.00125.96           N  
+ANISOU12751  N   ILE D 389     9871  24993  12995   3964  -3001  -5815       N  
+ATOM  12752  CA  ILE D 389     -60.610  52.279 -40.615  1.00131.91           C  
+ANISOU12752  CA  ILE D 389    10283  26360  13478   4214  -3205  -5904       C  
+ATOM  12753  C   ILE D 389     -60.881  53.784 -40.668  1.00136.10           C  
+ANISOU12753  C   ILE D 389    11052  26977  13682   4931  -3318  -5219       C  
+ATOM  12754  O   ILE D 389     -60.896  54.450 -39.629  1.00136.61           O  
+ANISOU12754  O   ILE D 389    11266  26590  14048   5108  -3161  -4841       O  
+ATOM  12755  CB  ILE D 389     -61.744  51.567 -39.832  1.00125.61           C  
+ANISOU12755  CB  ILE D 389     8979  25556  13193   3809  -3086  -6362       C  
+ATOM  12756  CG1 ILE D 389     -61.795  50.081 -40.209  1.00127.77           C  
+ANISOU12756  CG1 ILE D 389     8971  25925  13651   3151  -3003  -7106       C  
+ATOM  12757  CG2 ILE D 389     -63.082  52.263 -40.037  1.00134.69           C  
+ANISOU12757  CG2 ILE D 389     9813  27217  14146   4200  -3273  -6260       C  
+ATOM  12758  CD1 ILE D 389     -62.893  49.295 -39.526  1.00130.50           C  
+ANISOU12758  CD1 ILE D 389     8850  26252  14484   2699  -2842  -7584       C  
+ATOM  12759  N   ASP D 390     -61.077  54.329 -41.867  1.00138.24           N  
+ANISOU12759  N   ASP D 390    11390  27780  13355   5344  -3549  -5046       N  
+ATOM  12760  CA  ASP D 390     -61.409  55.748 -41.988  1.00139.25           C  
+ANISOU12760  CA  ASP D 390    11759  27971  13180   6034  -3626  -4398       C  
+ATOM  12761  C   ASP D 390     -62.655  55.918 -42.874  1.00141.73           C  
+ANISOU12761  C   ASP D 390    11668  29042  13140   6310  -3892  -4543       C  
+ATOM  12762  O   ASP D 390     -62.680  55.432 -44.009  1.00146.34           O  
+ANISOU12762  O   ASP D 390    12113  30152  13337   6237  -4065  -4835       O  
+ATOM  12763  CB  ASP D 390     -60.224  56.552 -42.530  1.00143.19           C  
+ANISOU12763  CB  ASP D 390    12896  28245  13265   6393  -3590  -3830       C  
+ATOM  12764  CG  ASP D 390     -60.331  58.038 -42.211  1.00149.16           C  
+ANISOU12764  CG  ASP D 390    14038  28717  13918   7018  -3513  -3100       C  
+ATOM  12765  OD1 ASP D 390     -61.457  58.519 -41.975  1.00149.38           O  
+ANISOU12765  OD1 ASP D 390    13803  28936  14018   7288  -3578  -3033       O  
+ATOM  12766  OD2 ASP D 390     -59.284  58.721 -42.175  1.00147.60           O  
+ANISOU12766  OD2 ASP D 390    14420  28075  13588   7219  -3360  -2602       O  
+ATOM  12767  N   LYS D 391     -63.676  56.599 -42.357  1.00144.60           N  
+ANISOU12767  N   LYS D 391    11833  29467  13639   6626  -3917  -4348       N  
+ATOM  12768  CA  LYS D 391     -64.912  56.849 -43.103  1.00161.44           C  
+ANISOU12768  CA  LYS D 391    13549  32328  15461   6942  -4181  -4448       C  
+ATOM  12769  C   LYS D 391     -65.566  55.560 -43.602  1.00165.33           C  
+ANISOU12769  C   LYS D 391    13447  33386  15984   6429  -4321  -5235       C  
+ATOM  12770  O   LYS D 391     -66.133  55.528 -44.691  1.00166.04           O  
+ANISOU12770  O   LYS D 391    13281  34174  15632   6614  -4578  -5391       O  
+ATOM  12771  CB  LYS D 391     -64.658  57.796 -44.285  1.00166.54           C  
+ANISOU12771  CB  LYS D 391    14542  33291  15446   7558  -4349  -3950       C  
+ATOM  12772  CG  LYS D 391     -65.020  59.259 -44.022  1.00167.35           C  
+ANISOU12772  CG  LYS D 391    14923  33206  15458   8252  -4314  -3254       C  
+ATOM  12773  CD  LYS D 391     -64.162  59.857 -42.904  1.00160.47           C  
+ANISOU12773  CD  LYS D 391    14583  31439  14949   8274  -3986  -2806       C  
+ATOM  12774  CE  LYS D 391     -64.243  61.378 -42.870  1.00158.47           C  
+ANISOU12774  CE  LYS D 391    14775  30914  14524   8971  -3894  -2065       C  
+ATOM  12775  NZ  LYS D 391     -63.414  61.955 -41.772  1.00152.43           N  
+ANISOU12775  NZ  LYS D 391    14533  29260  14122   8956  -3547  -1668       N  
+ATOM  12776  N   GLY D 392     -65.448  54.487 -42.832  1.00161.39           N  
+ANISOU12776  N   GLY D 392    12753  32566  16001   5774  -4129  -5729       N  
+ATOM  12777  CA  GLY D 392     -66.062  53.240 -43.233  1.00163.23           C  
+ANISOU12777  CA  GLY D 392    12461  33235  16325   5237  -4189  -6492       C  
+ATOM  12778  C   GLY D 392     -65.023  52.149 -43.308  1.00157.25           C  
+ANISOU12778  C   GLY D 392    11877  32140  15731   4656  -4013  -6870       C  
+ATOM  12779  O   GLY D 392     -65.362  50.971 -43.301  1.00155.52           O  
+ANISOU12779  O   GLY D 392    11303  32008  15780   4075  -3926  -7524       O  
+ATOM  12780  N   VAL D 394     -60.865  49.775 -45.272  1.00146.86           N  
+ANISOU12780  N   VAL D 394    11604  30148  14048   3604  -3662  -7491       N  
+ATOM  12781  CA  VAL D 394     -59.484  49.674 -44.815  1.00143.80           C  
+ANISOU12781  CA  VAL D 394    11696  29107  13836   3456  -3448  -7290       C  
+ATOM  12782  C   VAL D 394     -58.587  50.657 -45.571  1.00144.22           C  
+ANISOU12782  C   VAL D 394    12252  29238  13306   3957  -3547  -6701       C  
+ATOM  12783  O   VAL D 394     -58.526  50.638 -46.801  1.00140.71           O  
+ANISOU12783  O   VAL D 394    11831  29263  12367   4079  -3674  -6762       O  
+ATOM  12784  CB  VAL D 394     -58.943  48.241 -44.983  1.00144.20           C  
+ANISOU12784  CB  VAL D 394    11702  28905  14181   2798  -3221  -7915       C  
+ATOM  12785  CG1 VAL D 394     -57.476  48.181 -44.588  1.00130.73           C  
+ANISOU12785  CG1 VAL D 394    10511  26554  12605   2690  -3011  -7691       C  
+ATOM  12786  CG2 VAL D 394     -59.751  47.273 -44.128  1.00144.90           C  
+ANISOU12786  CG2 VAL D 394    11375  28781  14901   2274  -3039  -8443       C  
+ATOM  12787  N   VAL D 395     -57.883  51.506 -44.827  1.00139.17           N  
+ANISOU12787  N   VAL D 395    12026  28121  12732   4227  -3464  -6130       N  
+ATOM  12788  CA  VAL D 395     -57.033  52.535 -45.421  1.00137.82           C  
+ANISOU12788  CA  VAL D 395    12390  27932  12045   4700  -3492  -5506       C  
+ATOM  12789  C   VAL D 395     -55.643  52.530 -44.779  1.00131.18           C  
+ANISOU12789  C   VAL D 395    12033  26429  11379   4536  -3259  -5292       C  
+ATOM  12790  O   VAL D 395     -55.492  52.174 -43.609  1.00133.78           O  
+ANISOU12790  O   VAL D 395    12334  26212  12282   4236  -3076  -5373       O  
+ATOM  12791  CB  VAL D 395     -57.679  53.938 -45.282  1.00138.47           C  
+ANISOU12791  CB  VAL D 395    12566  28138  11909   5356  -3621  -4870       C  
+ATOM  12792  CG1 VAL D 395     -57.623  54.421 -43.839  1.00127.36           C  
+ANISOU12792  CG1 VAL D 395    11262  26145  10985   5413  -3482  -4563       C  
+ATOM  12793  CG2 VAL D 395     -57.017  54.940 -46.220  1.00140.01           C  
+ANISOU12793  CG2 VAL D 395    13275  28427  11495   5841  -3641  -4276       C  
+ATOM  12794  N   LYS D 396     -54.624  52.887 -45.558  1.00132.86           N  
+ANISOU12794  N   LYS D 396    12717  26614  11151   4685  -3184  -4997       N  
+ATOM  12795  CA  LYS D 396     -53.258  52.959 -45.045  1.00127.72           C  
+ANISOU12795  CA  LYS D 396    12592  25240  10697   4513  -2846  -4716       C  
+ATOM  12796  C   LYS D 396     -53.141  53.939 -43.877  1.00122.15           C  
+ANISOU12796  C   LYS D 396    12176  23872  10364   4713  -2650  -4091       C  
+ATOM  12797  O   LYS D 396     -53.736  55.017 -43.896  1.00129.30           O  
+ANISOU12797  O   LYS D 396    13124  24983  11019   5224  -2809  -3657       O  
+ATOM  12798  CB  LYS D 396     -52.291  53.356 -46.163  1.00125.35           C  
+ANISOU12798  CB  LYS D 396    12737  25112   9780   4705  -2793  -4457       C  
+ATOM  12799  N   ALA D 397     -52.377  53.551 -42.858  1.00110.67           N  
+ANISOU12799  N   ALA D 397    10920  21629   9499   4322  -2303  -4057       N  
+ATOM  12800  CA  ALA D 397     -52.220  54.368 -41.657  1.00111.89           C  
+ANISOU12800  CA  ALA D 397    11342  21137  10032   4422  -2098  -3550       C  
+ATOM  12801  C   ALA D 397     -50.991  55.270 -41.745  1.00112.28           C  
+ANISOU12801  C   ALA D 397    12007  20747   9908   4565  -1854  -2971       C  
+ATOM  12802  O   ALA D 397     -49.872  54.827 -41.488  1.00109.25           O  
+ANISOU12802  O   ALA D 397    11852  19896   9760   4222  -1588  -2990       O  
+ATOM  12803  CB  ALA D 397     -52.136  53.476 -40.427  1.00111.56           C  
+ANISOU12803  CB  ALA D 397    11162  20529  10696   3930  -1875  -3820       C  
+ATOM  12804  N   LYS D 398     -51.216  56.546 -42.045  1.00115.10           N  
+ANISOU12804  N   LYS D 398    12618  21226   9887   5073  -1924  -2451       N  
+ATOM  12805  CA  LYS D 398     -50.138  57.524 -42.207  1.00115.01           C  
+ANISOU12805  CA  LYS D 398    13205  20817   9676   5218  -1671  -1886       C  
+ATOM  12806  C   LYS D 398     -49.220  57.623 -40.988  1.00115.37           C  
+ANISOU12806  C   LYS D 398    13531  20033  10270   4874  -1319  -1702       C  
+ATOM  12807  O   LYS D 398     -48.038  57.950 -41.117  1.00109.41           O  
+ANISOU12807  O   LYS D 398    13175  18936   9461   4755  -1065  -1445       O  
+ATOM  12808  CB  LYS D 398     -50.724  58.902 -42.524  1.00115.92           C  
+ANISOU12808  CB  LYS D 398    13547  21103   9395   5841  -1771  -1344       C  
+ATOM  12809  N   GLY D 399     -49.772  57.341 -39.812  1.00112.98           N  
+ANISOU12809  N   GLY D 399    13004  19450  10474   4708  -1305  -1844       N  
+ATOM  12810  CA  GLY D 399     -49.023  57.397 -38.569  1.00109.67           C  
+ANISOU12810  CA  GLY D 399    12810  18313  10545   4393  -1017  -1696       C  
+ATOM  12811  C   GLY D 399     -47.783  56.522 -38.556  1.00110.32           C  
+ANISOU12811  C   GLY D 399    12968  18130  10819   3952   -830  -1885       C  
+ATOM  12812  O   GLY D 399     -46.747  56.921 -38.029  1.00115.12           O  
+ANISOU12812  O   GLY D 399    13903  18253  11584   3797   -587  -1612       O  
+ATOM  12813  N   VAL D 400     -47.891  55.326 -39.128  1.00106.29           N  
+ANISOU12813  N   VAL D 400    12136  17943  10305   3751   -936  -2372       N  
+ATOM  12814  CA  VAL D 400     -46.764  54.400 -39.187  1.00 99.72           C  
+ANISOU12814  CA  VAL D 400    11344  16880   9668   3381   -751  -2587       C  
+ATOM  12815  C   VAL D 400     -45.653  54.968 -40.068  1.00100.76           C  
+ANISOU12815  C   VAL D 400    11827  17039   9418   3470   -608  -2315       C  
+ATOM  12816  O   VAL D 400     -44.467  54.836 -39.755  1.00 93.20           O  
+ANISOU12816  O   VAL D 400    11050  15697   8664   3239   -368  -2218       O  
+ATOM  12817  CB  VAL D 400     -47.192  53.019 -39.721  1.00 99.20           C  
+ANISOU12817  CB  VAL D 400    10882  17152   9658   3166   -866  -3205       C  
+ATOM  12818  CG1 VAL D 400     -46.011  52.062 -39.730  1.00 95.80           C  
+ANISOU12818  CG1 VAL D 400    10510  16415   9473   2831   -634  -3409       C  
+ATOM  12819  CG2 VAL D 400     -48.325  52.454 -38.880  1.00 98.52           C  
+ANISOU12819  CG2 VAL D 400    10436  17041   9956   3038   -966  -3488       C  
+ATOM  12820  N   GLN D 401     -46.047  55.611 -41.163  1.00106.00           N  
+ANISOU12820  N   GLN D 401    12576  18181   9518   3817   -751  -2180       N  
+ATOM  12821  CA  GLN D 401     -45.096  56.258 -42.060  1.00104.62           C  
+ANISOU12821  CA  GLN D 401    12772  18059   8919   3931   -588  -1875       C  
+ATOM  12822  C   GLN D 401     -44.418  57.429 -41.356  1.00105.49           C  
+ANISOU12822  C   GLN D 401    13298  17624   9159   3962   -339  -1330       C  
+ATOM  12823  O   GLN D 401     -43.222  57.672 -41.540  1.00101.86           O  
+ANISOU12823  O   GLN D 401    13105  16928   8668   3805    -73  -1151       O  
+ATOM  12824  CB  GLN D 401     -45.796  56.736 -43.335  1.00100.92           C  
+ANISOU12824  CB  GLN D 401    12328  18245   7774   4346   -812  -1802       C  
+ATOM  12825  N   SER D 402     -45.191  58.150 -40.549  1.00115.75           N  
+ANISOU12825  N   SER D 402    14636  18731  10611   4146   -407  -1098       N  
+ATOM  12826  CA  SER D 402     -44.648  59.231 -39.735  1.00113.62           C  
+ANISOU12826  CA  SER D 402    14750  17900  10519   4130   -162   -652       C  
+ATOM  12827  C   SER D 402     -43.611  58.697 -38.753  1.00108.48           C  
+ANISOU12827  C   SER D 402    14084  16772  10362   3664     40   -765       C  
+ATOM  12828  O   SER D 402     -42.546  59.285 -38.581  1.00110.99           O  
+ANISOU12828  O   SER D 402    14702  16752  10716   3509    297   -508       O  
+ATOM  12829  CB  SER D 402     -45.767  59.955 -38.981  1.00106.56           C  
+ANISOU12829  CB  SER D 402    13853  16893   9741   4408   -269   -472       C  
+ATOM  12830  N   GLU D 403     -43.930  57.576 -38.113  1.00101.20           N  
+ANISOU12830  N   GLU D 403    12802  15838   9812   3442    -71  -1149       N  
+ATOM  12831  CA  GLU D 403     -43.012  56.939 -37.177  1.00102.87           C  
+ANISOU12831  CA  GLU D 403    12965  15648  10474   3054     83  -1255       C  
+ATOM  12832  C   GLU D 403     -41.752  56.438 -37.880  1.00 99.13           C  
+ANISOU12832  C   GLU D 403    12518  15217   9929   2866    242  -1347       C  
+ATOM  12833  O   GLU D 403     -40.675  56.414 -37.287  1.00 86.50           O  
+ANISOU12833  O   GLU D 403    10997  13288   8582   2621    425  -1259       O  
+ATOM  12834  CB  GLU D 403     -43.709  55.794 -36.438  1.00101.94           C  
+ANISOU12834  CB  GLU D 403    12484  15512  10737   2896    -47  -1625       C  
+ATOM  12835  CG  GLU D 403     -44.687  56.277 -35.376  1.00 97.62           C  
+ANISOU12835  CG  GLU D 403    11920  14789  10383   2984   -112  -1513       C  
+ATOM  12836  CD  GLU D 403     -45.657  55.205 -34.923  1.00 98.82           C  
+ANISOU12836  CD  GLU D 403    11690  15042  10814   2878   -241  -1893       C  
+ATOM  12837  OE1 GLU D 403     -45.390  54.013 -35.170  1.00100.76           O  
+ANISOU12837  OE1 GLU D 403    11726  15348  11209   2665   -237  -2233       O  
+ATOM  12838  OE2 GLU D 403     -46.688  55.558 -34.311  1.00102.42           O  
+ANISOU12838  OE2 GLU D 403    12061  15497  11358   3001   -313  -1861       O  
+ATOM  12839  N   PHE D 404     -41.890  56.037 -39.141  1.00105.33           N  
+ANISOU12839  N   PHE D 404    13217  16444  10358   2987    171  -1544       N  
+ATOM  12840  CA  PHE D 404     -40.734  55.660 -39.950  1.00 95.64           C  
+ANISOU12840  CA  PHE D 404    12037  15303   8998   2852    357  -1628       C  
+ATOM  12841  C   PHE D 404     -39.842  56.877 -40.169  1.00 91.43           C  
+ANISOU12841  C   PHE D 404    11890  14599   8251   2878    599  -1180       C  
+ATOM  12842  O   PHE D 404     -38.629  56.825 -39.944  1.00 90.36           O  
+ANISOU12842  O   PHE D 404    11803  14227   8302   2633    831  -1128       O  
+ATOM  12843  CB  PHE D 404     -41.173  55.061 -41.289  1.00 93.82           C  
+ANISOU12843  CB  PHE D 404    11667  15625   8356   2989    231  -1947       C  
+ATOM  12844  CG  PHE D 404     -40.031  54.725 -42.212  1.00 99.92           C  
+ANISOU12844  CG  PHE D 404    12508  16520   8935   2878    454  -2044       C  
+ATOM  12845  CD1 PHE D 404     -39.596  55.631 -43.168  1.00108.02           C  
+ANISOU12845  CD1 PHE D 404    13846  17740   9456   3037    594  -1739       C  
+ATOM  12846  CD2 PHE D 404     -39.398  53.496 -42.128  1.00 99.27           C  
+ANISOU12846  CD2 PHE D 404    12193  16345   9180   2630    557  -2432       C  
+ATOM  12847  CE1 PHE D 404     -38.547  55.318 -44.015  1.00109.46           C  
+ANISOU12847  CE1 PHE D 404    14082  18051   9455   2923    837  -1841       C  
+ATOM  12848  CE2 PHE D 404     -38.350  53.177 -42.972  1.00106.02           C  
+ANISOU12848  CE2 PHE D 404    13089  17319   9875   2547    791  -2542       C  
+ATOM  12849  CZ  PHE D 404     -37.925  54.090 -43.916  1.00107.48           C  
+ANISOU12849  CZ  PHE D 404    13561  17729   9546   2680    933  -2258       C  
+ATOM  12850  N   ASN D 405     -40.458  57.966 -40.621  1.00 94.47           N  
+ANISOU12850  N   ASN D 405    12537  15108   8248   3182    557   -859       N  
+ATOM  12851  CA  ASN D 405     -39.751  59.223 -40.844  1.00102.48           C  
+ANISOU12851  CA  ASN D 405    13979  15907   9051   3218    825   -403       C  
+ATOM  12852  C   ASN D 405     -38.985  59.679 -39.605  1.00104.41           C  
+ANISOU12852  C   ASN D 405    14333  15601   9737   2921   1019   -237       C  
+ATOM  12853  O   ASN D 405     -37.789  59.976 -39.674  1.00 95.57           O  
+ANISOU12853  O   ASN D 405    13352  14302   8657   2682   1297   -120       O  
+ATOM  12854  CB  ASN D 405     -40.735  60.311 -41.276  1.00108.37           C  
+ANISOU12854  CB  ASN D 405    14998  16783   9396   3649    732    -56       C  
+ATOM  12855  CG  ASN D 405     -41.439  59.976 -42.575  1.00109.44           C  
+ANISOU12855  CG  ASN D 405    15036  17547   9000   3969    517   -185       C  
+ATOM  12856  OD1 ASN D 405     -40.880  59.307 -43.444  1.00104.55           O  
+ANISOU12856  OD1 ASN D 405    14331  17225   8167   3861    571   -412       O  
+ATOM  12857  ND2 ASN D 405     -42.677  60.436 -42.713  1.00115.19           N  
+ANISOU12857  ND2 ASN D 405    15757  18511   9499   4374    269    -59       N  
+ATOM  12858  N   ILE D 406     -39.688  59.739 -38.477  1.00105.33           N  
+ANISOU12858  N   ILE D 406    14368  15485  10166   2925    877   -249       N  
+ATOM  12859  CA  ILE D 406     -39.083  60.117 -37.205  1.00 97.52           C  
+ANISOU12859  CA  ILE D 406    13463  14024   9568   2642   1015   -141       C  
+ATOM  12860  C   ILE D 406     -37.955  59.157 -36.839  1.00 94.55           C  
+ANISOU12860  C   ILE D 406    12830  13587   9506   2286   1086   -378       C  
+ATOM  12861  O   ILE D 406     -36.908  59.578 -36.349  1.00 96.58           O  
+ANISOU12861  O   ILE D 406    13185  13587   9922   2020   1284   -257       O  
+ATOM  12862  CB  ILE D 406     -40.126  60.148 -36.068  1.00 94.23           C  
+ANISOU12862  CB  ILE D 406    12961  13433   9408   2715    837   -177       C  
+ATOM  12863  CG1 ILE D 406     -41.222  61.169 -36.378  1.00 95.08           C  
+ANISOU12863  CG1 ILE D 406    13304  13585   9236   3116    785     80       C  
+ATOM  12864  CG2 ILE D 406     -39.465  60.484 -34.741  1.00 92.45           C  
+ANISOU12864  CG2 ILE D 406    12823  12767   9537   2402    967   -101       C  
+ATOM  12865  CD1 ILE D 406     -42.416  61.081 -35.454  1.00 94.49           C  
+ANISOU12865  CD1 ILE D 406    13072  13452   9378   3247    602    -11       C  
+ATOM  12866  N   SER D 407     -38.174  57.868 -37.088  1.00 95.12           N  
+ANISOU12866  N   SER D 407    12566  13901   9675   2288    931   -728       N  
+ATOM  12867  CA  SER D 407     -37.161  56.848 -36.827  1.00 96.96           C  
+ANISOU12867  CA  SER D 407    12545  14084  10211   2033   1001   -953       C  
+ATOM  12868  C   SER D 407     -35.869  57.127 -37.590  1.00 91.09           C  
+ANISOU12868  C   SER D 407    11889  13404   9317   1906   1266   -868       C  
+ATOM  12869  O   SER D 407     -34.779  57.014 -37.031  1.00 90.46           O  
+ANISOU12869  O   SER D 407    11714  13153   9502   1660   1399   -857       O  
+ATOM  12870  CB  SER D 407     -37.686  55.457 -37.191  1.00 93.84           C  
+ANISOU12870  CB  SER D 407    11834  13921   9902   2089    844  -1354       C  
+ATOM  12871  OG  SER D 407     -38.706  55.046 -36.297  1.00 86.79           O  
+ANISOU12871  OG  SER D 407    10806  12917   9252   2114    652  -1463       O  
+ATOM  12872  N   PHE D 408     -35.989  57.496 -38.862  1.00 91.73           N  
+ANISOU12872  N   PHE D 408    12135  13763   8955   2077   1345   -805       N  
+ATOM  12873  CA  PHE D 408     -34.798  57.711 -39.679  1.00 99.15           C  
+ANISOU12873  CA  PHE D 408    13156  14794   9722   1952   1640   -741       C  
+ATOM  12874  C   PHE D 408     -34.146  59.056 -39.371  1.00 99.79           C  
+ANISOU12874  C   PHE D 408    13556  14587   9771   1798   1892   -362       C  
+ATOM  12875  O   PHE D 408     -32.928  59.200 -39.480  1.00 98.75           O  
+ANISOU12875  O   PHE D 408    13399  14403   9718   1548   2157   -330       O  
+ATOM  12876  CB  PHE D 408     -35.132  57.624 -41.171  1.00107.68           C  
+ANISOU12876  CB  PHE D 408    14334  16294  10284   2181   1662   -802       C  
+ATOM  12877  CG  PHE D 408     -34.001  58.052 -42.067  1.00111.63           C  
+ANISOU12877  CG  PHE D 408    14997  16887  10530   2070   2018   -671       C  
+ATOM  12878  CD1 PHE D 408     -32.934  57.202 -42.309  1.00114.67           C  
+ANISOU12878  CD1 PHE D 408    15119  17357  11093   1876   2193   -933       C  
+ATOM  12879  CD2 PHE D 408     -34.005  59.301 -42.668  1.00114.86           C  
+ANISOU12879  CD2 PHE D 408    15828  17281  10532   2172   2210   -276       C  
+ATOM  12880  CE1 PHE D 408     -31.890  57.589 -43.129  1.00117.03           C  
+ANISOU12880  CE1 PHE D 408    15538  17761  11168   1757   2555   -829       C  
+ATOM  12881  CE2 PHE D 408     -32.964  59.694 -43.490  1.00120.01           C  
+ANISOU12881  CE2 PHE D 408    16643  18005  10949   2039   2586   -148       C  
+ATOM  12882  CZ  PHE D 408     -31.905  58.837 -43.720  1.00120.36           C  
+ANISOU12882  CZ  PHE D 408    16387  18170  11173   1817   2760   -438       C  
+ATOM  12883  N   GLU D 409     -34.953  60.040 -38.986  1.00108.11           N  
+ANISOU12883  N   GLU D 409    14899  15448  10730   1938   1832    -96       N  
+ATOM  12884  CA  GLU D 409     -34.417  61.349 -38.626  1.00111.05           C  
+ANISOU12884  CA  GLU D 409    15618  15472  11104   1772   2098    239       C  
+ATOM  12885  C   GLU D 409     -33.747  61.311 -37.250  1.00105.80           C  
+ANISOU12885  C   GLU D 409    14791  14500  10907   1419   2107    163       C  
+ATOM  12886  O   GLU D 409     -33.052  62.250 -36.859  1.00103.20           O  
+ANISOU12886  O   GLU D 409    14668  13894  10649   1161   2349    341       O  
+ATOM  12887  CB  GLU D 409     -35.526  62.405 -38.651  1.00109.02           C  
+ANISOU12887  CB  GLU D 409    15741  15072  10610   2080   2055    542       C  
+ATOM  12888  N   GLN D 410     -33.979  60.221 -36.523  1.00103.88           N  
+ANISOU12888  N   GLN D 410    14189  14315  10966   1403   1848   -105       N  
+ATOM  12889  CA  GLN D 410     -33.438  60.012 -35.179  1.00102.98           C  
+ANISOU12889  CA  GLN D 410    13890  13984  11255   1126   1791   -183       C  
+ATOM  12890  C   GLN D 410     -32.285  58.993 -35.177  1.00109.52           C  
+ANISOU12890  C   GLN D 410    14330  14970  12314    941   1824   -401       C  
+ATOM  12891  O   GLN D 410     -31.930  58.445 -34.132  1.00112.83           O  
+ANISOU12891  O   GLN D 410    14506  15308  13057    803   1699   -504       O  
+ATOM  12892  CB  GLN D 410     -34.546  59.552 -34.231  1.00103.65           C  
+ANISOU12892  CB  GLN D 410    13885  13981  11518   1264   1502   -275       C  
+ATOM  12893  CG  GLN D 410     -34.212  59.684 -32.759  1.00107.18           C  
+ANISOU12893  CG  GLN D 410    14278  14173  12271   1017   1450   -270       C  
+ATOM  12894  CD  GLN D 410     -35.225  58.994 -31.885  1.00109.46           C  
+ANISOU12894  CD  GLN D 410    14438  14415  12736   1142   1198   -386       C  
+ATOM  12895  OE1 GLN D 410     -36.364  59.440 -31.753  1.00107.84           O  
+ANISOU12895  OE1 GLN D 410    14405  14135  12434   1333   1127   -317       O  
+ATOM  12896  NE2 GLN D 410     -34.821  57.871 -31.302  1.00108.63           N  
+ANISOU12896  NE2 GLN D 410    14022  14357  12897   1055   1082   -554       N  
+ATOM  12897  N   ASN D 411     -31.748  58.720 -36.364  1.00112.31           N  
+ANISOU12897  N   ASN D 411    14628  15564  12480    979   1994   -464       N  
+ATOM  12898  CA  ASN D 411     -30.735  57.682 -36.610  1.00111.33           C  
+ANISOU12898  CA  ASN D 411    14129  15626  12545    888   2060   -694       C  
+ATOM  12899  C   ASN D 411     -31.073  56.324 -35.993  1.00103.01           C  
+ANISOU12899  C   ASN D 411    12753  14585  11801    998   1805   -942       C  
+ATOM  12900  O   ASN D 411     -30.229  55.660 -35.397  1.00110.39           O  
+ANISOU12900  O   ASN D 411    13385  15504  13052    888   1796  -1042       O  
+ATOM  12901  CB  ASN D 411     -29.333  58.165 -36.148  1.00127.74           C  
+ANISOU12901  CB  ASN D 411    16086  17637  14814    543   2271   -624       C  
+ATOM  12902  CG  ASN D 411     -29.195  58.332 -34.623  1.00127.96           C  
+ANISOU12902  CG  ASN D 411    16017  17451  15152    357   2100   -588       C  
+ATOM  12903  OD1 ASN D 411     -29.253  57.369 -33.856  1.00130.40           O  
+ANISOU12903  OD1 ASN D 411    16052  17766  15727    422   1875   -722       O  
+ATOM  12904  ND2 ASN D 411     -29.006  59.571 -34.190  1.00134.79           N  
+ANISOU12904  ND2 ASN D 411    17135  18116  15963    119   2229   -405       N  
+ATOM  12905  N   ASN D 412     -32.289  55.858 -36.238  1.00 96.21           N  
+ANISOU12905  N   ASN D 412    11942  13776  10839   1231   1618  -1051       N  
+ATOM  12906  CA  ASN D 412     -32.635  54.520 -35.802  1.00 89.75           C  
+ANISOU12906  CA  ASN D 412    10850  12942  10309   1314   1443  -1307       C  
+ATOM  12907  C   ASN D 412     -32.631  53.542 -36.953  1.00 88.06           C  
+ANISOU12907  C   ASN D 412    10492  12969   9997   1443   1507  -1603       C  
+ATOM  12908  O   ASN D 412     -32.954  53.891 -38.089  1.00101.31           O  
+ANISOU12908  O   ASN D 412    12326  14881  11288   1546   1575  -1624       O  
+ATOM  12909  CB  ASN D 412     -34.005  54.503 -35.122  1.00 89.86           C  
+ANISOU12909  CB  ASN D 412    10951  12830  10361   1423   1205  -1300       C  
+ATOM  12910  CG  ASN D 412     -33.975  55.120 -33.743  1.00 88.84           C  
+ANISOU12910  CG  ASN D 412    10905  12433  10418   1286   1135  -1091       C  
+ATOM  12911  OD1 ASN D 412     -32.942  55.619 -33.296  1.00 93.10           O  
+ANISOU12911  OD1 ASN D 412    11437  12895  11040   1091   1240   -958       O  
+ATOM  12912  ND2 ASN D 412     -35.103  55.069 -33.049  1.00 85.60           N  
+ANISOU12912  ND2 ASN D 412    10549  11903  10070   1367    963  -1091       N  
+ATOM  12913  N   TYR D 413     -32.264  52.306 -36.639  1.00 85.47           N  
+ANISOU12913  N   TYR D 413     9886  12580  10010   1449   1494  -1830       N  
+ATOM  12914  CA  TYR D 413     -32.261  51.241 -37.619  1.00 89.11           C  
+ANISOU12914  CA  TYR D 413    10205  13210  10444   1553   1577  -2176       C  
+ATOM  12915  C   TYR D 413     -33.703  50.909 -37.959  1.00 94.63           C  
+ANISOU12915  C   TYR D 413    10976  13995  10984   1670   1394  -2373       C  
+ATOM  12916  O   TYR D 413     -34.519  50.674 -37.067  1.00 90.12           O  
+ANISOU12916  O   TYR D 413    10387  13237  10619   1673   1213  -2366       O  
+ATOM  12917  CB  TYR D 413     -31.528  50.014 -37.080  1.00 86.48           C  
+ANISOU12917  CB  TYR D 413     9582  12709  10569   1557   1633  -2344       C  
+ATOM  12918  CG  TYR D 413     -30.047  50.230 -36.863  1.00 92.18           C  
+ANISOU12918  CG  TYR D 413    10137  13443  11445   1470   1806  -2202       C  
+ATOM  12919  CD1 TYR D 413     -29.211  50.553 -37.923  1.00 94.30           C  
+ANISOU12919  CD1 TYR D 413    10384  13952  11492   1435   2061  -2246       C  
+ATOM  12920  CD2 TYR D 413     -29.482  50.102 -35.599  1.00 93.58           C  
+ANISOU12920  CD2 TYR D 413    10155  13428  11971   1421   1716  -2034       C  
+ATOM  12921  CE1 TYR D 413     -27.856  50.748 -37.732  1.00 95.05           C  
+ANISOU12921  CE1 TYR D 413    10267  14096  11751   1333   2235  -2146       C  
+ATOM  12922  CE2 TYR D 413     -28.127  50.294 -35.398  1.00 96.92           C  
+ANISOU12922  CE2 TYR D 413    10358  13934  12533   1339   1846  -1933       C  
+ATOM  12923  CZ  TYR D 413     -27.319  50.617 -36.469  1.00 97.48           C  
+ANISOU12923  CZ  TYR D 413    10374  14244  12421   1285   2111  -2001       C  
+ATOM  12924  OH  TYR D 413     -25.970  50.810 -36.283  1.00104.91           O  
+ANISOU12924  OH  TYR D 413    11039  15301  13519   1181   2257  -1928       O  
+ATOM  12925  N   VAL D 414     -34.019  50.895 -39.246  1.00 97.26           N  
+ANISOU12925  N   VAL D 414    11375  14647  10933   1759   1442  -2558       N  
+ATOM  12926  CA  VAL D 414     -35.389  50.675 -39.672  1.00 93.82           C  
+ANISOU12926  CA  VAL D 414    10966  14396  10284   1866   1241  -2766       C  
+ATOM  12927  C   VAL D 414     -35.558  49.251 -40.182  1.00 93.21           C  
+ANISOU12927  C   VAL D 414    10682  14384  10350   1856   1278  -3266       C  
+ATOM  12928  O   VAL D 414     -34.876  48.818 -41.111  1.00101.12           O  
+ANISOU12928  O   VAL D 414    11641  15557  11224   1860   1471  -3484       O  
+ATOM  12929  CB  VAL D 414     -35.812  51.688 -40.756  1.00 93.53           C  
+ANISOU12929  CB  VAL D 414    11160  14728   9647   2001   1217  -2629       C  
+ATOM  12930  CG1 VAL D 414     -36.187  53.017 -40.115  1.00 88.92           C  
+ANISOU12930  CG1 VAL D 414    10809  14010   8968   2050   1128  -2182       C  
+ATOM  12931  CG2 VAL D 414     -34.700  51.875 -41.779  1.00 91.79           C  
+ANISOU12931  CG2 VAL D 414    11015  14703   9160   1981   1495  -2615       C  
+ATOM  12932  N   VAL D 415     -36.464  48.520 -39.541  1.00 81.68           N  
+ANISOU12932  N   VAL D 415     9103  12759   9174   1823   1128  -3462       N  
+ATOM  12933  CA  VAL D 415     -36.705  47.127 -39.880  1.00 84.26           C  
+ANISOU12933  CA  VAL D 415     9253  13051   9712   1769   1192  -3960       C  
+ATOM  12934  C   VAL D 415     -38.182  46.973 -40.207  1.00 81.20           C  
+ANISOU12934  C   VAL D 415     8812  12906   9136   1764    972  -4239       C  
+ATOM  12935  O   VAL D 415     -38.984  46.600 -39.349  1.00 83.94           O  
+ANISOU12935  O   VAL D 415     9073  13037   9785   1692    864  -4290       O  
+ATOM  12936  CB  VAL D 415     -36.317  46.173 -38.723  1.00 83.18           C  
+ANISOU12936  CB  VAL D 415     8998  12419  10188   1696   1283  -3968       C  
+ATOM  12937  CG1 VAL D 415     -36.434  44.716 -39.163  1.00 85.15           C  
+ANISOU12937  CG1 VAL D 415     9112  12558  10682   1641   1431  -4488       C  
+ATOM  12938  CG2 VAL D 415     -34.907  46.471 -38.228  1.00 75.40           C  
+ANISOU12938  CG2 VAL D 415     8011  11255   9382   1723   1431  -3636       C  
+ATOM  12939  N   PRO D 416     -38.555  47.280 -41.454  1.00 89.76           N  
+ANISOU12939  N   PRO D 416     9932  14479   9693   1844    904  -4419       N  
+ATOM  12940  CA  PRO D 416     -39.951  47.095 -41.852  1.00 94.51           C  
+ANISOU12940  CA  PRO D 416    10414  15412  10083   1847    664  -4735       C  
+ATOM  12941  C   PRO D 416     -40.230  45.671 -42.309  1.00 86.74           C  
+ANISOU12941  C   PRO D 416     9235  14441   9282   1675    747  -5381       C  
+ATOM  12942  O   PRO D 416     -39.542  45.160 -43.202  1.00 88.12           O  
+ANISOU12942  O   PRO D 416     9425  14738   9319   1654    934  -5662       O  
+ATOM  12943  CB  PRO D 416     -40.116  48.098 -42.998  1.00100.42           C  
+ANISOU12943  CB  PRO D 416    11308  16713  10136   2044    550  -4597       C  
+ATOM  12944  CG  PRO D 416     -38.761  48.165 -43.623  1.00102.10           C  
+ANISOU12944  CG  PRO D 416    11662  16918  10214   2051    831  -4515       C  
+ATOM  12945  CD  PRO D 416     -37.785  48.017 -42.476  1.00 95.23           C  
+ANISOU12945  CD  PRO D 416    10790  15484   9909   1952   1019  -4259       C  
+ATOM  12946  N   VAL D 417     -41.179  45.006 -41.658  1.00 91.10           N  
+ANISOU12946  N   VAL D 417     9616  14819  10177   1529    659  -5625       N  
+ATOM  12947  CA  VAL D 417     -41.536  43.677 -42.099  1.00 98.70           C  
+ANISOU12947  CA  VAL D 417    10410  15766  11326   1320    763  -6276       C  
+ATOM  12948  C   VAL D 417     -42.602  43.820 -43.183  1.00107.76           C  
+ANISOU12948  C   VAL D 417    11414  17589  11940   1317    510  -6669       C  
+ATOM  12949  O   VAL D 417     -43.808  43.888 -42.923  1.00115.52           O  
+ANISOU12949  O   VAL D 417    12210  18760  12921   1259    282  -6796       O  
+ATOM  12950  CB  VAL D 417     -42.028  42.793 -40.950  1.00 91.64           C  
+ANISOU12950  CB  VAL D 417     9408  14348  11065   1120    846  -6396       C  
+ATOM  12951  CG1 VAL D 417     -42.173  41.374 -41.432  1.00 91.56           C  
+ANISOU12951  CG1 VAL D 417     9282  14207  11301    883   1050  -7068       C  
+ATOM  12952  CG2 VAL D 417     -41.038  42.849 -39.812  1.00 83.41           C  
+ANISOU12952  CG2 VAL D 417     8510  12734  10448   1187   1018  -5909       C  
+ATOM  12953  N   GLY D 418     -42.111  43.865 -44.412  1.00107.91           N  
+ANISOU12953  N   GLY D 418    11505  18007  11488   1389    559  -6863       N  
+ATOM  12954  CA  GLY D 418     -42.916  44.039 -45.601  1.00108.83           C  
+ANISOU12954  CA  GLY D 418    11519  18829  11001   1420    310  -7167       C  
+ATOM  12955  C   GLY D 418     -43.714  42.802 -45.955  1.00116.31           C  
+ANISOU12955  C   GLY D 418    12207  19798  12186   1089    280  -7752       C  
+ATOM  12956  O   GLY D 418     -44.540  42.848 -46.862  1.00118.82           O  
+ANISOU12956  O   GLY D 418    12361  20696  12087   1068     33  -7996       O  
+ATOM  12957  N   ALA D 419     -43.481  41.700 -45.240  1.00120.58           N  
+ANISOU12957  N   ALA D 419    12710  19708  13396    837    542  -7955       N  
+ATOM  12958  CA  ALA D 419     -44.124  40.421 -45.559  1.00119.68           C  
+ANISOU12958  CA  ALA D 419    12392  19514  13568    482    607  -8512       C  
+ATOM  12959  C   ALA D 419     -45.635  40.524 -45.408  1.00133.95           C  
+ANISOU12959  C   ALA D 419    13881  21698  15314    361    305  -8741       C  
+ATOM  12960  O   ALA D 419     -46.344  40.669 -46.405  1.00156.93           O  
+ANISOU12960  O   ALA D 419    16606  25257  17762    353     59  -8986       O  
+ATOM  12961  CB  ALA D 419     -43.585  39.309 -44.664  1.00107.64           C  
+ANISOU12961  CB  ALA D 419    10942  17166  12791    286    972  -8567       C  
+ATOM  12962  N   THR D 420     -46.134  40.465 -44.176  1.00132.41           N  
+ANISOU12962  N   THR D 420    13606  21130  15574    280    327  -8653       N  
+ATOM  12963  CA  THR D 420     -47.557  40.687 -43.955  1.00141.59           C  
+ANISOU12963  CA  THR D 420    14439  22677  16680    195     49  -8837       C  
+ATOM  12964  C   THR D 420     -47.682  42.170 -43.630  1.00138.95           C  
+ANISOU12964  C   THR D 420    14180  22680  15935    598   -227  -8362       C  
+ATOM  12965  O   THR D 420     -48.048  42.562 -42.520  1.00130.28           O  
+ANISOU12965  O   THR D 420    13064  21328  15108    646   -250  -8108       O  
+ATOM  12966  CB  THR D 420     -48.135  39.800 -42.830  1.00140.22           C  
+ANISOU12966  CB  THR D 420    14131  21936  17208   -139    253  -9026       C  
+ATOM  12967  N   GLY D 421     -47.336  42.982 -44.631  1.00144.38           N  
+ANISOU12967  N   GLY D 421    14988  23892  15979    888   -402  -8164       N  
+ATOM  12968  CA  GLY D 421     -47.287  44.431 -44.516  1.00132.72           C  
+ANISOU12968  CA  GLY D 421    13669  22706  14052   1310   -616  -7617       C  
+ATOM  12969  C   GLY D 421     -48.198  45.218 -45.458  1.00118.92           C  
+ANISOU12969  C   GLY D 421    11752  21808  11625   1567  -1021  -7604       C  
+ATOM  12970  O   GLY D 421     -48.547  44.769 -46.557  1.00113.61           O  
+ANISOU12970  O   GLY D 421    10905  21574  10686   1469  -1125  -7926       O  
+ATOM  12971  N   TYR D 422     -48.586  46.417 -45.033  1.00121.01           N  
+ANISOU12971  N   TYR D 422    12073  22208  11697   1911  -1225  -7067       N  
+ATOM  12972  CA  TYR D 422     -49.335  47.301 -45.926  1.00123.85           C  
+ANISOU12972  CA  TYR D 422    12332  23380  11347   2274  -1606  -6962       C  
+ATOM  12973  C   TYR D 422     -48.444  48.500 -46.192  1.00118.03           C  
+ANISOU12973  C   TYR D 422    12050  22576  10219   2658  -1541  -6252       C  
+ATOM  12974  O   TYR D 422     -47.803  48.597 -47.234  1.00110.82           O  
+ANISOU12974  O   TYR D 422    11339  21948   8819   2751  -1494  -6254       O  
+ATOM  12975  CB  TYR D 422     -50.677  47.750 -45.342  1.00123.32           C  
+ANISOU12975  CB  TYR D 422    11921  23563  11370   2408  -1896  -6896       C  
+ATOM  12976  CG  TYR D 422     -51.516  46.638 -44.758  1.00121.38           C  
+ANISOU12976  CG  TYR D 422    11244  23208  11666   1972  -1871  -7506       C  
+ATOM  12977  CD1 TYR D 422     -52.610  46.127 -45.442  1.00119.26           C  
+ANISOU12977  CD1 TYR D 422    10514  23483  11317   1837  -2062  -7944       C  
+ATOM  12978  CD2 TYR D 422     -51.189  46.079 -43.537  1.00116.36           C  
+ANISOU12978  CD2 TYR D 422    10688  21760  11764   1674  -1547  -7453       C  
+ATOM  12979  CE1 TYR D 422     -53.370  45.100 -44.907  1.00119.58           C  
+ANISOU12979  CE1 TYR D 422    10175  23351  11907   1395  -1956  -8457       C  
+ATOM  12980  CE2 TYR D 422     -51.939  45.065 -42.988  1.00127.10           C  
+ANISOU12980  CE2 TYR D 422    11702  22964  13628   1261  -1465  -7976       C  
+ATOM  12981  CZ  TYR D 422     -53.029  44.572 -43.677  1.00138.50           C  
+ANISOU12981  CZ  TYR D 422    12678  25013  14931   1100  -1670  -8519       C  
+ATOM  12982  OH  TYR D 422     -53.772  43.552 -43.128  1.00135.45           O  
+ANISOU12982  OH  TYR D 422    11961  24396  15107    648  -1508  -8981       O  
+ATOM  12983  N   ILE D 423     -48.409  49.417 -45.233  1.00121.59           N  
+ANISOU12983  N   ILE D 423    12673  22621  10904   2854  -1503  -5643       N  
+ATOM  12984  CA  ILE D 423     -47.475  50.542 -45.275  1.00118.08           C  
+ANISOU12984  CA  ILE D 423    12693  21946  10227   3134  -1356  -4963       C  
+ATOM  12985  C   ILE D 423     -46.063  50.009 -45.006  1.00114.46           C  
+ANISOU12985  C   ILE D 423    12474  20897  10120   2857   -966  -4953       C  
+ATOM  12986  O   ILE D 423     -45.065  50.512 -45.536  1.00118.96           O  
+ANISOU12986  O   ILE D 423    13369  21432  10400   2965   -790  -4654       O  
+ATOM  12987  CB  ILE D 423     -47.862  51.643 -44.284  1.00107.84           C  
+ANISOU12987  CB  ILE D 423    11509  20352   9113   3383  -1402  -4384       C  
+ATOM  12988  CG1 ILE D 423     -48.723  52.676 -45.005  1.00118.09           C  
+ANISOU12988  CG1 ILE D 423    12802  22277   9790   3871  -1717  -4113       C  
+ATOM  12989  CG2 ILE D 423     -46.646  52.355 -43.753  1.00 97.06           C  
+ANISOU12989  CG2 ILE D 423    10592  18381   7906   3400  -1095  -3828       C  
+ATOM  12990  CD1 ILE D 423     -48.929  53.962 -44.242  1.00112.11           C  
+ANISOU12990  CD1 ILE D 423    12278  21210   9109   4201  -1701  -3465       C  
+ATOM  12991  N   ALA D 424     -46.001  48.958 -44.196  1.00105.24           N  
+ANISOU12991  N   ALA D 424    11127  19282   9579   2507   -818  -5289       N  
+ATOM  12992  CA  ALA D 424     -44.762  48.234 -43.957  1.00102.85           C  
+ANISOU12992  CA  ALA D 424    10966  18465   9647   2263   -472  -5367       C  
+ATOM  12993  C   ALA D 424     -44.134  47.868 -45.320  1.00110.64           C  
+ANISOU12993  C   ALA D 424    12030  19833  10175   2258   -381  -5669       C  
+ATOM  12994  O   ALA D 424     -42.929  48.029 -45.506  1.00114.08           O  
+ANISOU12994  O   ALA D 424    12711  20047  10587   2270   -120  -5449       O  
+ATOM  12995  CB  ALA D 424     -45.022  47.004 -43.111  1.00103.10           C  
+ANISOU12995  CB  ALA D 424    10767  18073  10334   1924   -358  -5773       C  
+ATOM  12996  N   LYS D 425     -44.940  47.339 -46.245  1.00102.40           N  
+ANISOU12996  N   LYS D 425    10754  19378   8777   2216   -581  -6210       N  
+ATOM  12997  CA  LYS D 425     -44.494  47.048 -47.621  1.00109.48           C  
+ANISOU12997  CA  LYS D 425    11724  20703   9171   2214   -527  -6485       C  
+ATOM  12998  C   LYS D 425     -44.007  48.279 -48.405  1.00120.35           C  
+ANISOU12998  C   LYS D 425    13430  22421   9875   2567   -549  -5955       C  
+ATOM  12999  O   LYS D 425     -43.017  48.203 -49.142  1.00123.43           O  
+ANISOU12999  O   LYS D 425    14030  22793  10074   2535   -307  -5909       O  
+ATOM  13000  CB  LYS D 425     -45.613  46.375 -48.416  1.00115.12           C  
+ANISOU13000  CB  LYS D 425    12093  21908   9740   2066   -791  -6974       C  
+ATOM  13001  N   ASP D 426     -44.756  49.377 -48.313  1.00124.41           N  
+ANISOU13001  N   ASP D 426    13988  23249  10031   2903   -826  -5557       N  
+ATOM  13002  CA  ASP D 426     -44.367  50.617 -48.979  1.00126.75           C  
+ANISOU13002  CA  ASP D 426    14648  23789   9722   3261   -819  -4972       C  
+ATOM  13003  C   ASP D 426     -42.963  51.034 -48.534  1.00120.94           C  
+ANISOU13003  C   ASP D 426    14258  22440   9253   3193   -410  -4528       C  
+ATOM  13004  O   ASP D 426     -42.114  51.347 -49.362  1.00129.84           O  
+ANISOU13004  O   ASP D 426    15655  23710   9970   3259   -200  -4377       O  
+ATOM  13005  CB  ASP D 426     -45.382  51.727 -48.678  1.00122.40           C  
+ANISOU13005  CB  ASP D 426    14101  23450   8957   3639  -1131  -4518       C  
+ATOM  13006  CG  ASP D 426     -46.709  51.492 -49.359  1.00132.61           C  
+ANISOU13006  CG  ASP D 426    15025  25391   9970   3744  -1535  -4819       C  
+ATOM  13007  OD1 ASP D 426     -46.976  50.317 -49.676  1.00131.40           O  
+ANISOU13007  OD1 ASP D 426    14549  25356  10022   3407  -1566  -5434       O  
+ATOM  13008  OD2 ASP D 426     -47.510  52.443 -49.518  1.00137.25           O  
+ANISOU13008  OD2 ASP D 426    15619  26305  10226   4142  -1797  -4435       O  
+ATOM  13009  N   LEU D 427     -42.714  50.974 -47.226  1.00113.17           N  
+ANISOU13009  N   LEU D 427    13238  20798   8963   3033   -291  -4357       N  
+ATOM  13010  CA  LEU D 427     -41.425  51.379 -46.657  1.00115.83           C  
+ANISOU13010  CA  LEU D 427    13834  20568   9610   2943     55  -3950       C  
+ATOM  13011  C   LEU D 427     -40.309  50.360 -46.889  1.00114.19           C  
+ANISOU13011  C   LEU D 427    13575  20163   9649   2676    371  -4306       C  
+ATOM  13012  O   LEU D 427     -39.136  50.722 -46.965  1.00116.29           O  
+ANISOU13012  O   LEU D 427    14045  20214   9926   2644    669  -4033       O  
+ATOM  13013  CB  LEU D 427     -41.561  51.646 -45.157  1.00106.08           C  
+ANISOU13013  CB  LEU D 427    12563  18756   8986   2869     46  -3668       C  
+ATOM  13014  N   TRP D 428     -40.674  49.083 -46.940  1.00111.28           N  
+ANISOU13014  N   TRP D 428    12921  19831   9528   2477    331  -4919       N  
+ATOM  13015  CA  TRP D 428     -39.736  48.004 -47.255  1.00111.72           C  
+ANISOU13015  CA  TRP D 428    12918  19718   9814   2265    636  -5330       C  
+ATOM  13016  C   TRP D 428     -39.250  48.090 -48.697  1.00113.02           C  
+ANISOU13016  C   TRP D 428    13233  20388   9324   2346    766  -5482       C  
+ATOM  13017  O   TRP D 428     -38.109  47.751 -49.004  1.00123.75           O  
+ANISOU13017  O   TRP D 428    14664  21584  10770   2260   1107  -5546       O  
+ATOM  13018  CB  TRP D 428     -40.393  46.649 -47.013  1.00112.58           C  
+ANISOU13018  CB  TRP D 428    12725  19728  10321   2035    577  -5971       C  
+ATOM  13019  CG  TRP D 428     -39.474  45.474 -47.123  1.00111.76           C  
+ANISOU13019  CG  TRP D 428    12569  19295  10601   1836    919  -6363       C  
+ATOM  13020  CD1 TRP D 428     -38.837  44.854 -46.093  1.00112.26           C  
+ANISOU13020  CD1 TRP D 428    12576  18720  11355   1721   1137  -6322       C  
+ATOM  13021  CD2 TRP D 428     -39.099  44.762 -48.312  1.00105.58           C  
+ANISOU13021  CD2 TRP D 428    11801  18687   9630   1717   1054  -6695       C  
+ATOM  13022  NE1 TRP D 428     -38.086  43.807 -46.558  1.00109.28           N  
+ANISOU13022  NE1 TRP D 428    12173  18140  11207   1587   1418  -6653       N  
+ATOM  13023  CE2 TRP D 428     -38.229  43.728 -47.918  1.00106.27           C  
+ANISOU13023  CE2 TRP D 428    11841  18225  10311   1562   1378  -6882       C  
+ATOM  13024  CE3 TRP D 428     -39.411  44.899 -49.669  1.00110.92           C  
+ANISOU13024  CE3 TRP D 428    12532  19927   9686   1747    936  -6837       C  
+ATOM  13025  CZ2 TRP D 428     -37.667  42.835 -48.827  1.00119.69           C  
+ANISOU13025  CZ2 TRP D 428    13557  19908  12013   1439   1605  -7223       C  
+ATOM  13026  CZ3 TRP D 428     -38.849  44.009 -50.574  1.00115.21           C  
+ANISOU13026  CZ3 TRP D 428    13091  20467  10218   1594   1160  -7198       C  
+ATOM  13027  CH2 TRP D 428     -37.987  42.991 -50.147  1.00121.05           C  
+ANISOU13027  CH2 TRP D 428    13790  20635  11566   1442   1500  -7396       C  
+ATOM  13028  N   ASN D 429     -40.146  48.505 -49.588  1.00108.02           N  
+ANISOU13028  N   ASN D 429    12623  20326   8095   2497    477  -5489       N  
+ATOM  13029  CA  ASN D 429     -39.783  48.716 -50.984  1.00121.50           C  
+ANISOU13029  CA  ASN D 429    14515  22436   9215   2559    549  -5447       C  
+ATOM  13030  C   ASN D 429     -39.023  50.026 -51.131  1.00119.77           C  
+ANISOU13030  C   ASN D 429    14666  22229   8612   2784    739  -4809       C  
+ATOM  13031  O   ASN D 429     -38.160  50.170 -52.001  1.00126.19           O  
+ANISOU13031  O   ASN D 429    15685  23138   9124   2767   1007  -4716       O  
+ATOM  13032  CB  ASN D 429     -41.024  48.715 -51.880  1.00129.74           C  
+ANISOU13032  CB  ASN D 429    15433  24079   9783   2653    155  -5624       C  
+ATOM  13033  CG  ASN D 429     -41.716  47.362 -51.928  1.00133.85           C  
+ANISOU13033  CG  ASN D 429    15587  24621  10649   2362     27  -6307       C  
+ATOM  13034  OD1 ASN D 429     -41.072  46.316 -51.870  1.00137.20           O  
+ANISOU13034  OD1 ASN D 429    15948  24693  11487   2092    298  -6682       O  
+ATOM  13035  ND2 ASN D 429     -43.040  47.381 -52.036  1.00133.05           N  
+ANISOU13035  ND2 ASN D 429    15233  24922  10397   2420   -367  -6458       N  
+ATOM  13036  N   LYS D 430     -39.359  50.981 -50.270  1.00121.13           N  
+ANISOU13036  N   LYS D 430    14935  22274   8814   2979    627  -4367       N  
+ATOM  13037  CA  LYS D 430     -38.666  52.260 -50.227  1.00119.47           C  
+ANISOU13037  CA  LYS D 430    15092  21879   8422   3123    832  -3680       C  
+ATOM  13038  C   LYS D 430     -37.239  52.039 -49.717  1.00117.92           C  
+ANISOU13038  C   LYS D 430    14919  21150   8735   2869   1255  -3608       C  
+ATOM  13039  O   LYS D 430     -36.335  52.825 -50.001  1.00123.26           O  
+ANISOU13039  O   LYS D 430    15869  21745   9221   2883   1553  -3211       O  
+ATOM  13040  CB  LYS D 430     -39.428  53.267 -49.355  1.00110.90           C  
+ANISOU13040  CB  LYS D 430    14090  20580   7466   3315    600  -3180       C  
+ATOM  13041  CG  LYS D 430     -38.792  54.652 -49.304  1.00111.22           C  
+ANISOU13041  CG  LYS D 430    14552  20382   7324   3450    833  -2479       C  
+ATOM  13042  CD  LYS D 430     -39.570  55.617 -48.423  1.00111.40           C  
+ANISOU13042  CD  LYS D 430    14672  20150   7503   3647    634  -2032       C  
+ATOM  13043  CE  LYS D 430     -39.182  57.060 -48.718  1.00119.71           C  
+ANISOU13043  CE  LYS D 430    16211  21088   8185   3855    849  -1360       C  
+ATOM  13044  NZ  LYS D 430     -38.034  57.506 -47.889  1.00119.57           N  
+ANISOU13044  NZ  LYS D 430    16343  20436   8651   3575   1216  -1084       N  
+ATOM  13045  N   VAL D 431     -37.051  50.953 -48.970  1.00112.58           N  
+ANISOU13045  N   VAL D 431    13943  20124   8708   2640   1287  -3996       N  
+ATOM  13046  CA  VAL D 431     -35.755  50.609 -48.388  1.00110.07           C  
+ANISOU13046  CA  VAL D 431    13564  19329   8929   2437   1635  -3962       C  
+ATOM  13047  C   VAL D 431     -34.934  49.721 -49.324  1.00118.03           C  
+ANISOU13047  C   VAL D 431    14503  20523   9820   2341   1939  -4408       C  
+ATOM  13048  O   VAL D 431     -33.721  49.901 -49.450  1.00123.12           O  
+ANISOU13048  O   VAL D 431    15208  21030  10542   2269   2298  -4254       O  
+ATOM  13049  CB  VAL D 431     -35.925  49.896 -47.021  1.00 99.97           C  
+ANISOU13049  CB  VAL D 431    12023  17539   8423   2291   1533  -4085       C  
+ATOM  13050  CG1 VAL D 431     -34.666  49.135 -46.635  1.00 94.43           C  
+ANISOU13050  CG1 VAL D 431    11171  16468   8239   2126   1857  -4224       C  
+ATOM  13051  CG2 VAL D 431     -36.289  50.898 -45.939  1.00 91.37           C  
+ANISOU13051  CG2 VAL D 431    11037  16154   7528   2344   1370  -3569       C  
+ATOM  13052  N   ASN D 432     -35.596  48.771 -49.982  1.00110.34           N  
+ANISOU13052  N   ASN D 432    13387  19874   8664   2325   1814  -4988       N  
+ATOM  13053  CA  ASN D 432     -34.917  47.870 -50.908  1.00112.79           C  
+ANISOU13053  CA  ASN D 432    13662  20220   8972   2182   2063  -5357       C  
+ATOM  13054  C   ASN D 432     -34.285  48.673 -52.036  1.00123.91           C  
+ANISOU13054  C   ASN D 432    15363  21963   9754   2262   2278  -5072       C  
+ATOM  13055  O   ASN D 432     -33.161  48.398 -52.458  1.00127.89           O  
+ANISOU13055  O   ASN D 432    15891  22370  10331   2172   2659  -5134       O  
+ATOM  13056  CB  ASN D 432     -35.893  46.834 -51.468  1.00118.87           C  
+ANISOU13056  CB  ASN D 432    14278  21169   9719   2074   1815  -5891       C  
+ATOM  13057  N   GLU D 433     -35.020  49.667 -52.520  1.00124.52           N  
+ANISOU13057  N   GLU D 433    15666  22418   9228   2448   2045  -4738       N  
+ATOM  13058  CA  GLU D 433     -34.456  50.672 -53.408  1.00127.01           C  
+ANISOU13058  CA  GLU D 433    16331  22970   8958   2550   2265  -4312       C  
+ATOM  13059  C   GLU D 433     -33.689  51.672 -52.548  1.00126.77           C  
+ANISOU13059  C   GLU D 433    16431  22632   9102   2580   2518  -3794       C  
+ATOM  13060  O   GLU D 433     -34.117  51.981 -51.435  1.00117.68           O  
+ANISOU13060  O   GLU D 433    15201  21208   8304   2620   2326  -3605       O  
+ATOM  13061  CB  GLU D 433     -35.548  51.368 -54.221  1.00123.76           C  
+ANISOU13061  CB  GLU D 433    16124  23033   7867   2776   1916  -4094       C  
+ATOM  13062  N   GLU D 434     -32.567  52.171 -53.061  1.00133.04           N  
+ANISOU13062  N   GLU D 434    17423  23410   9714   2512   2947  -3547       N  
+ATOM  13063  CA  GLU D 434     -31.711  53.095 -52.315  1.00121.87           C  
+ANISOU13063  CA  GLU D 434    16110  21661   8534   2449   3235  -3064       C  
+ATOM  13064  C   GLU D 434     -31.351  52.522 -50.945  1.00119.24           C  
+ANISOU13064  C   GLU D 434    15425  20783   9097   2267   3185  -3176       C  
+ATOM  13065  O   GLU D 434     -31.531  53.174 -49.919  1.00113.86           O  
+ANISOU13065  O   GLU D 434    14772  19739   8749   2242   3042  -2808       O  
+ATOM  13066  CB  GLU D 434     -32.388  54.460 -52.159  1.00114.99           C  
+ANISOU13066  CB  GLU D 434    15595  20762   7333   2634   3059  -2449       C  
+ATOM  13067  N   PHE D 435     -30.855  51.290 -50.944  1.00123.61           N  
+ANISOU13067  N   PHE D 435    15665  21285  10016   2159   3312  -3686       N  
+ATOM  13068  CA  PHE D 435     -30.618  50.543 -49.714  1.00115.16           C  
+ANISOU13068  CA  PHE D 435    14258  19742   9755   2047   3235  -3834       C  
+ATOM  13069  C   PHE D 435     -29.354  51.033 -49.011  1.00116.46           C  
+ANISOU13069  C   PHE D 435    14336  19568  10347   1892   3523  -3499       C  
+ATOM  13070  O   PHE D 435     -29.143  50.765 -47.828  1.00101.45           O  
+ANISOU13070  O   PHE D 435    12209  17276   9062   1819   3420  -3446       O  
+ATOM  13071  CB  PHE D 435     -30.526  49.045 -50.025  1.00118.57           C  
+ANISOU13071  CB  PHE D 435    14422  20209  10419   2023   3309  -4487       C  
+ATOM  13072  CG  PHE D 435     -30.352  48.175 -48.812  1.00107.34           C  
+ANISOU13072  CG  PHE D 435    12689  18293   9802   1958   3238  -4631       C  
+ATOM  13073  CD1 PHE D 435     -31.437  47.848 -48.015  1.00102.81           C  
+ANISOU13073  CD1 PHE D 435    12048  17525   9490   1973   2865  -4697       C  
+ATOM  13074  CD2 PHE D 435     -29.108  47.658 -48.487  1.00103.82           C  
+ANISOU13074  CD2 PHE D 435    12012  17599   9838   1901   3557  -4697       C  
+ATOM  13075  CE1 PHE D 435     -31.280  47.039 -46.904  1.00 97.18           C  
+ANISOU13075  CE1 PHE D 435    11095  16349   9481   1926   2826  -4791       C  
+ATOM  13076  CE2 PHE D 435     -28.946  46.848 -47.379  1.00101.86           C  
+ANISOU13076  CE2 PHE D 435    11500  16910  10292   1895   3485  -4783       C  
+ATOM  13077  CZ  PHE D 435     -30.033  46.538 -46.586  1.00 99.80           C  
+ANISOU13077  CZ  PHE D 435    11228  16430  10261   1904   3127  -4817       C  
+ATOM  13078  N   GLU D 436     -28.522  51.759 -49.750  1.00124.83           N  
+ANISOU13078  N   GLU D 436    15571  20807  11052   1832   3889  -3278       N  
+ATOM  13079  CA  GLU D 436     -27.268  52.287 -49.224  1.00119.20           C  
+ANISOU13079  CA  GLU D 436    14748  19851  10691   1639   4204  -2998       C  
+ATOM  13080  C   GLU D 436     -27.491  53.490 -48.299  1.00108.64           C  
+ANISOU13080  C   GLU D 436    13591  18220   9467   1557   4053  -2474       C  
+ATOM  13081  O   GLU D 436     -26.628  53.831 -47.487  1.00103.90           O  
+ANISOU13081  O   GLU D 436    12826  17353   9297   1363   4187  -2292       O  
+ATOM  13082  CB  GLU D 436     -26.345  52.663 -50.393  1.00118.12           C  
+ANISOU13082  CB  GLU D 436    14747  20017  10114   1566   4698  -2964       C  
+ATOM  13083  CG  GLU D 436     -25.076  53.426 -50.029  1.00123.03           C  
+ANISOU13083  CG  GLU D 436    15288  20466  10993   1318   5075  -2650       C  
+ATOM  13084  CD  GLU D 436     -24.044  52.565 -49.323  1.00126.43           C  
+ANISOU13084  CD  GLU D 436    15196  20721  12122   1219   5198  -2909       C  
+ATOM  13085  OE1 GLU D 436     -24.222  51.330 -49.275  1.00130.28           O  
+ANISOU13085  OE1 GLU D 436    15433  21205  12863   1364   5076  -3335       O  
+ATOM  13086  OE2 GLU D 436     -23.051  53.128 -48.816  1.00122.82           O  
+ANISOU13086  OE2 GLU D 436    14573  20131  11963   1000   5423  -2689       O  
+ATOM  13087  N   THR D 437     -28.666  54.106 -48.391  1.00107.50           N  
+ANISOU13087  N   THR D 437    13760  18134   8951   1714   3763  -2261       N  
+ATOM  13088  CA  THR D 437     -28.963  55.301 -47.604  1.00114.32           C  
+ANISOU13088  CA  THR D 437    14856  18704   9877   1670   3655  -1774       C  
+ATOM  13089  C   THR D 437     -29.494  54.938 -46.218  1.00111.80           C  
+ANISOU13089  C   THR D 437    14313  18046  10120   1657   3288  -1823       C  
+ATOM  13090  O   THR D 437     -29.678  55.807 -45.365  1.00112.20           O  
+ANISOU13090  O   THR D 437    14500  17806  10325   1592   3197  -1484       O  
+ATOM  13091  CB  THR D 437     -29.981  56.218 -48.314  1.00122.46           C  
+ANISOU13091  CB  THR D 437    16340  19936  10252   1903   3534  -1466       C  
+ATOM  13092  OG1 THR D 437     -29.850  57.556 -47.818  1.00126.74           O  
+ANISOU13092  OG1 THR D 437    17186  20164  10806   1820   3649   -949       O  
+ATOM  13093  CG2 THR D 437     -31.403  55.731 -48.082  1.00119.16           C  
+ANISOU13093  CG2 THR D 437    15860  19623   9795   2142   3041  -1649       C  
+ATOM  13094  N   TYR D 438     -29.731  53.649 -46.002  1.00108.37           N  
+ANISOU13094  N   TYR D 438    13560  17630   9985   1711   3114  -2252       N  
+ATOM  13095  CA  TYR D 438     -30.304  53.163 -44.751  1.00 96.39           C  
+ANISOU13095  CA  TYR D 438    11847  15810   8967   1714   2787  -2319       C  
+ATOM  13096  C   TYR D 438     -29.319  52.234 -44.053  1.00 97.20           C  
+ANISOU13096  C   TYR D 438    11567  15702   9661   1593   2896  -2525       C  
+ATOM  13097  O   TYR D 438     -29.222  52.221 -42.826  1.00 95.64           O  
+ANISOU13097  O   TYR D 438    11232  15199   9907   1518   2752  -2400       O  
+ATOM  13098  CB  TYR D 438     -31.631  52.446 -45.008  1.00 93.58           C  
+ANISOU13098  CB  TYR D 438    11471  15617   8467   1895   2467  -2622       C  
+ATOM  13099  CG  TYR D 438     -32.713  53.346 -45.563  1.00107.23           C  
+ANISOU13099  CG  TYR D 438    13518  17588   9637   2077   2282  -2399       C  
+ATOM  13100  CD1 TYR D 438     -33.014  54.557 -44.953  1.00109.83           C  
+ANISOU13100  CD1 TYR D 438    14088  17710   9934   2100   2209  -1932       C  
+ATOM  13101  CD2 TYR D 438     -33.430  52.988 -46.698  1.00115.33           C  
+ANISOU13101  CD2 TYR D 438    14600  19061  10157   2243   2182  -2663       C  
+ATOM  13102  CE1 TYR D 438     -34.001  55.385 -45.454  1.00108.11           C  
+ANISOU13102  CE1 TYR D 438    14159  17696   9221   2333   2050  -1695       C  
+ATOM  13103  CE2 TYR D 438     -34.419  53.811 -47.208  1.00115.70           C  
+ANISOU13103  CE2 TYR D 438    14908  19382   9670   2466   1982  -2432       C  
+ATOM  13104  CZ  TYR D 438     -34.699  55.008 -46.581  1.00113.48           C  
+ANISOU13104  CZ  TYR D 438    14863  18860   9392   2535   1922  -1928       C  
+ATOM  13105  OH  TYR D 438     -35.682  55.830 -47.084  1.00118.79           O  
+ANISOU13105  OH  TYR D 438    15796  19789   9549   2822   1733  -1666       O  
+ATOM  13106  N   TYR D 439     -28.592  51.457 -44.847  1.00100.68           N  
+ANISOU13106  N   TYR D 439    11842  16326  10087   1602   3156  -2836       N  
+ATOM  13107  CA  TYR D 439     -27.577  50.548 -44.327  1.00 93.93           C  
+ANISOU13107  CA  TYR D 439    10610  15307   9774   1556   3301  -3027       C  
+ATOM  13108  C   TYR D 439     -26.306  50.631 -45.164  1.00101.90           C  
+ANISOU13108  C   TYR D 439    11516  16529  10671   1481   3738  -3083       C  
+ATOM  13109  O   TYR D 439     -26.085  49.799 -46.045  1.00111.18           O  
+ANISOU13109  O   TYR D 439    12605  17892  11747   1569   3935  -3452       O  
+ATOM  13110  CB  TYR D 439     -28.092  49.106 -44.290  1.00 91.51           C  
+ANISOU13110  CB  TYR D 439    10124  14917   9730   1693   3180  -3471       C  
+ATOM  13111  CG  TYR D 439     -29.257  48.881 -43.351  1.00 96.99           C  
+ANISOU13111  CG  TYR D 439    10853  15369  10629   1733   2797  -3445       C  
+ATOM  13112  CD1 TYR D 439     -29.046  48.433 -42.054  1.00100.91           C  
+ANISOU13112  CD1 TYR D 439    11150  15508  11682   1722   2676  -3356       C  
+ATOM  13113  CD2 TYR D 439     -30.564  49.111 -43.760  1.00 99.87           C  
+ANISOU13113  CD2 TYR D 439    11435  15896  10617   1793   2563  -3505       C  
+ATOM  13114  CE1 TYR D 439     -30.102  48.222 -41.188  1.00103.56           C  
+ANISOU13114  CE1 TYR D 439    11531  15622  12195   1742   2372  -3327       C  
+ATOM  13115  CE2 TYR D 439     -31.629  48.903 -42.899  1.00 92.90           C  
+ANISOU13115  CE2 TYR D 439    10547  14810   9940   1814   2248  -3500       C  
+ATOM  13116  CZ  TYR D 439     -31.391  48.459 -41.615  1.00 95.30           C  
+ANISOU13116  CZ  TYR D 439    10680  14727  10801   1775   2174  -3411       C  
+ATOM  13117  OH  TYR D 439     -32.443  48.249 -40.752  1.00 91.57           O  
+ANISOU13117  OH  TYR D 439    10218  14052  10524   1779   1904  -3400       O  
+ATOM  13118  N   PRO D 440     -25.466  51.643 -44.892  1.00102.92           N  
+ANISOU13118  N   PRO D 440    11653  16632  10820   1293   3919  -2743       N  
+ATOM  13119  CA  PRO D 440     -24.195  51.780 -45.609  1.00107.52           C  
+ANISOU13119  CA  PRO D 440    12095  17421  11339   1177   4373  -2785       C  
+ATOM  13120  C   PRO D 440     -23.282  50.601 -45.304  1.00109.83           C  
+ANISOU13120  C   PRO D 440    11903  17671  12157   1250   4493  -3092       C  
+ATOM  13121  O   PRO D 440     -22.487  50.634 -44.364  1.00104.84           O  
+ANISOU13121  O   PRO D 440    10951  16905  11978   1163   4480  -2971       O  
+ATOM  13122  CB  PRO D 440     -23.616  53.087 -45.057  1.00104.45           C  
+ANISOU13122  CB  PRO D 440    11776  16927  10984    911   4475  -2367       C  
+ATOM  13123  CG  PRO D 440     -24.800  53.838 -44.540  1.00103.26           C  
+ANISOU13123  CG  PRO D 440    11988  16587  10660    937   4133  -2090       C  
+ATOM  13124  CD  PRO D 440     -25.717  52.784 -43.996  1.00 99.59           C  
+ANISOU13124  CD  PRO D 440    11405  16000  10433   1152   3747  -2327       C  
+ATOM  13125  N   GLY D 441     -23.413  49.564 -46.121  1.00117.56           N  
+ANISOU13125  N   GLY D 441    12833  18778  13055   1425   4612  -3499       N  
+ATOM  13126  CA  GLY D 441     -22.682  48.325 -45.949  1.00117.80           C  
+ANISOU13126  CA  GLY D 441    12456  18728  13574   1569   4753  -3826       C  
+ATOM  13127  C   GLY D 441     -23.498  47.234 -46.609  1.00125.41           C  
+ANISOU13127  C   GLY D 441    13532  19699  14418   1753   4709  -4273       C  
+ATOM  13128  O   GLY D 441     -24.598  47.494 -47.098  1.00134.00           O  
+ANISOU13128  O   GLY D 441    14958  20900  15057   1749   4524  -4309       O  
+ATOM  13129  N   ALA D 442     -22.977  46.014 -46.628  1.00117.80           N  
+ANISOU13129  N   ALA D 442    12281  18620  13859   1917   4883  -4629       N  
+ATOM  13130  CA  ALA D 442     -23.680  44.916 -47.279  1.00115.98           C  
+ANISOU13130  CA  ALA D 442    12226  18271  13572   2023   4813  -4997       C  
+ATOM  13131  C   ALA D 442     -23.626  43.646 -46.441  1.00120.70           C  
+ANISOU13131  C   ALA D 442    12617  18416  14826   2190   4704  -5127       C  
+ATOM  13132  O   ALA D 442     -23.335  43.691 -45.245  1.00123.52           O  
+ANISOU13132  O   ALA D 442    12741  18569  15624   2251   4580  -4904       O  
+ATOM  13133  CB  ALA D 442     -23.102  44.665 -48.662  1.00121.05           C  
+ANISOU13133  CB  ALA D 442    12965  19135  13893   2015   5147  -5196       C  
+ATOM  13134  N   ASP D 443     -23.915  42.515 -47.076  1.00129.96           N  
+ANISOU13134  N   ASP D 443    13901  19435  16043   2261   4758  -5476       N  
+ATOM  13135  CA  ASP D 443     -23.909  41.226 -46.396  1.00126.68           C  
+ANISOU13135  CA  ASP D 443    13370  18548  16213   2422   4709  -5597       C  
+ATOM  13136  C   ASP D 443     -22.487  40.757 -46.112  1.00129.73           C  
+ANISOU13136  C   ASP D 443    13435  18813  17045   2617   4958  -5480       C  
+ATOM  13137  O   ASP D 443     -21.778  41.347 -45.296  1.00112.66           O  
+ANISOU13137  O   ASP D 443    11003  16701  15101   2654   4929  -5157       O  
+ATOM  13138  CB  ASP D 443     -24.651  40.180 -47.231  1.00115.24           C  
+ANISOU13138  CB  ASP D 443    12153  16980  14654   2395   4731  -6036       C  
+HETATM13139  N   MSE D 446     -26.877  39.748 -44.720  1.00108.17           N  
+ANISOU13139  N   MSE D 446    11338  15380  14383   2343   4033  -5851       N  
+HETATM13140  CA  MSE D 446     -27.571  40.967 -44.322  1.00105.46           C  
+ANISOU13140  CA  MSE D 446    11046  15291  13733   2234   3771  -5636       C  
+HETATM13141  C   MSE D 446     -28.527  41.437 -45.413  1.00104.12           C  
+ANISOU13141  C   MSE D 446    11105  15528  12930   2074   3666  -5871       C  
+HETATM13142  O   MSE D 446     -29.660  41.830 -45.131  1.00105.33           O  
+ANISOU13142  O   MSE D 446    11358  15757  12904   1990   3387  -5870       O  
+HETATM13143  CB  MSE D 446     -26.566  42.070 -43.983  1.00112.86           C  
+ANISOU13143  CB  MSE D 446    11804  16463  14617   2279   3849  -5268       C  
+HETATM13144  CG  MSE D 446     -27.176  43.456 -43.866  1.00115.98           C  
+ANISOU13144  CG  MSE D 446    12340  17159  14569   2142   3624  -5002       C  
+HETATM13145 SE   MSE D 446     -25.948  44.754 -43.087  1.00190.31          SE  
+ANISOU13145 SE   MSE D 446    21592  26660  24058   2079   3625  -4380      SE  
+HETATM13146  CE  MSE D 446     -25.909  44.069 -41.261  1.00 90.96           C  
+ANISOU13146  CE  MSE D 446     8803  13564  12192   2203   3371  -4141       C  
+ATOM  13147  N   LYS D 447     -28.066  41.397 -46.659  1.00114.60           N  
+ANISOU13147  N   LYS D 447    12503  17137  13903   2052   3883  -6060       N  
+ATOM  13148  CA  LYS D 447     -28.914  41.739 -47.794  1.00116.62           C  
+ANISOU13148  CA  LYS D 447    12977  17813  13519   1932   3779  -6283       C  
+ATOM  13149  C   LYS D 447     -29.979  40.667 -47.992  1.00121.02           C  
+ANISOU13149  C   LYS D 447    13601  18204  14176   1824   3633  -6702       C  
+ATOM  13150  O   LYS D 447     -31.117  40.965 -48.358  1.00119.53           O  
+ANISOU13150  O   LYS D 447    13518  18297  13599   1716   3371  -6837       O  
+ATOM  13151  CB  LYS D 447     -28.078  41.902 -49.065  1.00119.18           C  
+ANISOU13151  CB  LYS D 447    13373  18462  13448   1939   4080  -6369       C  
+ATOM  13152  N   LYS D 448     -29.596  39.418 -47.748  1.00119.87           N  
+ANISOU13152  N   LYS D 448    13380  17609  14554   1857   3811  -6900       N  
+ATOM  13153  CA  LYS D 448     -30.517  38.293 -47.848  1.00114.87           C  
+ANISOU13153  CA  LYS D 448    12803  16735  14109   1717   3740  -7306       C  
+ATOM  13154  C   LYS D 448     -31.575  38.354 -46.751  1.00115.94           C  
+ANISOU13154  C   LYS D 448    12910  16658  14485   1638   3447  -7203       C  
+ATOM  13155  O   LYS D 448     -32.749  38.075 -46.993  1.00121.88           O  
+ANISOU13155  O   LYS D 448    13704  17505  15100   1451   3255  -7496       O  
+ATOM  13156  CB  LYS D 448     -29.755  36.968 -47.772  1.00118.49           C  
+ANISOU13156  CB  LYS D 448    13220  16705  15093   1806   4050  -7479       C  
+ATOM  13157  N   LEU D 449     -31.146  38.714 -45.544  1.00106.46           N  
+ANISOU13157  N   LEU D 449    11615  15191  13643   1775   3417  -6795       N  
+ATOM  13158  CA  LEU D 449     -32.042  38.792 -44.395  1.00102.55           C  
+ANISOU13158  CA  LEU D 449    11101  14457  13406   1722   3175  -6652       C  
+ATOM  13159  C   LEU D 449     -33.085  39.892 -44.571  1.00105.13           C  
+ANISOU13159  C   LEU D 449    11474  15247  13224   1628   2862  -6615       C  
+ATOM  13160  O   LEU D 449     -34.259  39.700 -44.253  1.00100.69           O  
+ANISOU13160  O   LEU D 449    10914  14642  12700   1491   2654  -6763       O  
+ATOM  13161  CB  LEU D 449     -31.244  39.029 -43.111  1.00 99.02           C  
+ANISOU13161  CB  LEU D 449    10541  13687  13393   1911   3208  -6198       C  
+ATOM  13162  N   PHE D 450     -32.647  41.043 -45.072  1.00104.86           N  
+ANISOU13162  N   PHE D 450    11473  15654  12714   1712   2848  -6403       N  
+ATOM  13163  CA  PHE D 450     -33.546  42.161 -45.341  1.00100.23           C  
+ANISOU13163  CA  PHE D 450    10969  15541  11574   1692   2570  -6311       C  
+ATOM  13164  C   PHE D 450     -34.607  41.758 -46.358  1.00105.75           C  
+ANISOU13164  C   PHE D 450    11718  16559  11901   1548   2413  -6731       C  
+ATOM  13165  O   PHE D 450     -35.787  42.069 -46.198  1.00100.61           O  
+ANISOU13165  O   PHE D 450    11052  16104  11073   1493   2117  -6783       O  
+ATOM  13166  CB  PHE D 450     -32.764  43.377 -45.842  1.00 97.88           C  
+ANISOU13166  CB  PHE D 450    10750  15630  10809   1806   2666  -5999       C  
+ATOM  13167  N   GLY D 451     -34.173  41.065 -47.406  1.00116.73           N  
+ANISOU13167  N   GLY D 451    13146  18029  13176   1491   2612  -7040       N  
+ATOM  13168  CA  GLY D 451     -35.076  40.581 -48.434  1.00116.20           C  
+ANISOU13168  CA  GLY D 451    13099  18284  12769   1332   2483  -7484       C  
+ATOM  13169  C   GLY D 451     -36.031  39.533 -47.897  1.00117.17           C  
+ANISOU13169  C   GLY D 451    13106  18076  13336   1133   2386  -7818       C  
+ATOM  13170  O   GLY D 451     -37.122  39.339 -48.433  1.00125.02           O  
+ANISOU13170  O   GLY D 451    14041  19385  14078    973   2169  -8147       O  
+ATOM  13171  N   GLU D 452     -35.615  38.856 -46.831  1.00109.32           N  
+ANISOU13171  N   GLU D 452    12070  16460  13005   1143   2555  -7717       N  
+ATOM  13172  CA  GLU D 452     -36.420  37.801 -46.225  1.00113.89           C  
+ANISOU13172  CA  GLU D 452    12578  16627  14068    945   2542  -7982       C  
+ATOM  13173  C   GLU D 452     -37.541  38.373 -45.362  1.00117.00           C  
+ANISOU13173  C   GLU D 452    12888  17086  14482    889   2237  -7843       C  
+ATOM  13174  O   GLU D 452     -38.366  37.631 -44.829  1.00124.93           O  
+ANISOU13174  O   GLU D 452    13818  17804  15847    692   2212  -8049       O  
+ATOM  13175  CB  GLU D 452     -35.537  36.872 -45.389  1.00109.81           C  
+ANISOU13175  CB  GLU D 452    12088  15409  14225   1024   2849  -7855       C  
+ATOM  13176  N   LEU D 453     -37.567  39.695 -45.227  1.00112.63           N  
+ANISOU13176  N   LEU D 453    12353  16898  13542   1060   2034  -7491       N  
+ATOM  13177  CA  LEU D 453     -38.588  40.363 -44.430  1.00108.02           C  
+ANISOU13177  CA  LEU D 453    11698  16411  12934   1058   1749  -7334       C  
+ATOM  13178  C   LEU D 453     -39.821  40.676 -45.272  1.00106.10           C  
+ANISOU13178  C   LEU D 453    11359  16779  12176    962   1442  -7619       C  
+ATOM  13179  O   LEU D 453     -39.897  40.301 -46.442  1.00112.14           O  
+ANISOU13179  O   LEU D 453    12114  17870  12624    872   1449  -7951       O  
+ATOM  13180  CB  LEU D 453     -38.032  41.647 -43.810  1.00 94.73           C  
+ANISOU13180  CB  LEU D 453    10090  14799  11103   1309   1693  -6804       C  
+ATOM  13181  N   LEU D 458     -43.011  32.441 -45.592  1.00144.36           N  
+ANISOU13181  N   LEU D 458    15698  19655  19496  -1042   2533 -10434       N  
+ATOM  13182  CA  LEU D 458     -42.236  31.915 -44.475  1.00149.67           C  
+ANISOU13182  CA  LEU D 458    16594  19514  20760   -915   2843 -10066       C  
+ATOM  13183  C   LEU D 458     -43.147  31.563 -43.307  1.00136.82           C  
+ANISOU13183  C   LEU D 458    14893  17499  19595  -1129   2892 -10006       C  
+ATOM  13184  O   LEU D 458     -44.325  31.918 -43.307  1.00134.20           O  
+ANISOU13184  O   LEU D 458    14310  17574  19104  -1336   2657 -10204       O  
+ATOM  13185  CB  LEU D 458     -41.184  32.936 -44.034  1.00146.13           C  
+ANISOU13185  CB  LEU D 458    16290  19069  20165   -489   2755  -9481       C  
+ATOM  13186  N   SER D 459     -42.597  30.883 -42.306  1.00128.47           N  
+ANISOU13186  N   SER D 459    14045  15677  19090  -1056   3201  -9710       N  
+ATOM  13187  CA  SER D 459     -43.369  30.501 -41.130  1.00124.73           C  
+ANISOU13187  CA  SER D 459    13558  14768  19066  -1245   3308  -9593       C  
+ATOM  13188  C   SER D 459     -43.343  31.620 -40.097  1.00127.72           C  
+ANISOU13188  C   SER D 459    13948  15197  19383   -997   3077  -9057       C  
+ATOM  13189  O   SER D 459     -42.707  32.650 -40.308  1.00130.89           O  
+ANISOU13189  O   SER D 459    14369  15950  19414   -688   2852  -8789       O  
+ATOM  13190  CB  SER D 459     -42.837  29.197 -40.526  1.00127.90           C  
+ANISOU13190  CB  SER D 459    14213  14316  20067  -1266   3766  -9497       C  
+ATOM  13191  N   ILE D 460     -44.006  31.403 -38.967  1.00123.82           N  
+ANISOU13191  N   ILE D 460    13460  14332  19255  -1137   3168  -8896       N  
+ATOM  13192  CA  ILE D 460     -44.041  32.409 -37.917  1.00121.87           C  
+ANISOU13192  CA  ILE D 460    13236  14095  18974   -925   2977  -8410       C  
+ATOM  13193  C   ILE D 460     -42.710  32.404 -37.178  1.00124.65           C  
+ANISOU13193  C   ILE D 460    13867  13958  19538   -544   3121  -7853       C  
+ATOM  13194  O   ILE D 460     -42.080  33.452 -37.006  1.00118.77           O  
+ANISOU13194  O   ILE D 460    13142  13451  18534   -230   2912  -7498       O  
+ATOM  13195  CB  ILE D 460     -45.191  32.161 -36.924  1.00120.00           C  
+ANISOU13195  CB  ILE D 460    12920  13621  19055  -1206   3057  -8417       C  
+ATOM  13196  N   GLU D 461     -42.281  31.216 -36.763  1.00127.89           N  
+ANISOU13196  N   GLU D 461    14478  13707  20409   -562   3484  -7778       N  
+ATOM  13197  CA  GLU D 461     -40.986  31.040 -36.118  1.00120.43           C  
+ANISOU13197  CA  GLU D 461    13765  12312  19681   -171   3630  -7272       C  
+ATOM  13198  C   GLU D 461     -39.877  31.540 -37.038  1.00117.72           C  
+ANISOU13198  C   GLU D 461    13393  12327  19009    115   3521  -7263       C  
+ATOM  13199  O   GLU D 461     -38.922  32.178 -36.594  1.00120.81           O  
+ANISOU13199  O   GLU D 461    13830  12729  19343    470   3437  -6819       O  
+ATOM  13200  CB  GLU D 461     -40.756  29.574 -35.749  1.00114.57           C  
+ANISOU13200  CB  GLU D 461    13237  10850  19443   -224   4049  -7263       C  
+ATOM  13201  N   GLU D 462     -40.017  31.247 -38.327  1.00118.25           N  
+ANISOU13201  N   GLU D 462    13370  12708  18852    -56   3537  -7766       N  
+ATOM  13202  CA  GLU D 462     -39.005  31.614 -39.307  1.00123.91           C  
+ANISOU13202  CA  GLU D 462    14074  13761  19246    175   3493  -7806       C  
+ATOM  13203  C   GLU D 462     -38.930  33.128 -39.488  1.00118.09           C  
+ANISOU13203  C   GLU D 462    13214  13645  18008    334   3141  -7611       C  
+ATOM  13204  O   GLU D 462     -37.839  33.696 -39.549  1.00116.39           O  
+ANISOU13204  O   GLU D 462    13027  13537  17657    644   3121  -7310       O  
+ATOM  13205  CB  GLU D 462     -39.292  30.940 -40.651  1.00124.86           C  
+ANISOU13205  CB  GLU D 462    14139  14096  19206    -78   3595  -8414       C  
+ATOM  13206  N   LEU D 463     -40.086  33.779 -39.578  1.00115.30           N  
+ANISOU13206  N   LEU D 463    12711  13712  17385    129   2878  -7783       N  
+ATOM  13207  CA  LEU D 463     -40.120  35.227 -39.748  1.00109.04           C  
+ANISOU13207  CA  LEU D 463    11826  13504  16100    292   2551  -7593       C  
+ATOM  13208  C   LEU D 463     -39.599  35.960 -38.511  1.00104.22           C  
+ANISOU13208  C   LEU D 463    11288  12674  15639    557   2497  -7013       C  
+ATOM  13209  O   LEU D 463     -38.775  36.877 -38.629  1.00100.96           O  
+ANISOU13209  O   LEU D 463    10881  12514  14963    814   2402  -6729       O  
+ATOM  13210  CB  LEU D 463     -41.540  35.695 -40.077  1.00102.68           C  
+ANISOU13210  CB  LEU D 463    10825  13198  14989     52   2276  -7904       C  
+ATOM  13211  CG  LEU D 463     -41.679  37.155 -40.516  1.00 98.77           C  
+ANISOU13211  CG  LEU D 463    10249  13386  13894    238   1934  -7767       C  
+ATOM  13212  CD1 LEU D 463     -40.635  37.502 -41.568  1.00101.12           C  
+ANISOU13212  CD1 LEU D 463    10625  13990  13806    434   1960  -7741       C  
+ATOM  13213  CD2 LEU D 463     -43.080  37.437 -41.035  1.00100.85           C  
+ANISOU13213  CD2 LEU D 463    10283  14201  13836     32   1660  -8135       C  
+ATOM  13214  N   ILE D 464     -40.058  35.549 -37.329  1.00101.39           N  
+ANISOU13214  N   ILE D 464    10982  11846  15694    480   2579  -6836       N  
+ATOM  13215  CA  ILE D 464     -39.587  36.176 -36.095  1.00103.84           C  
+ANISOU13215  CA  ILE D 464    11364  11937  16152    721   2530  -6289       C  
+ATOM  13216  C   ILE D 464     -38.078  35.971 -35.937  1.00106.68           C  
+ANISOU13216  C   ILE D 464    11811  12050  16672   1035   2685  -5959       C  
+ATOM  13217  O   ILE D 464     -37.366  36.898 -35.557  1.00106.69           O  
+ANISOU13217  O   ILE D 464    11781  12214  16543   1275   2564  -5594       O  
+ATOM  13218  CB  ILE D 464     -40.346  35.670 -34.830  1.00 98.63           C  
+ANISOU13218  CB  ILE D 464    10779  10789  15906    579   2631  -6143       C  
+ATOM  13219  CG1 ILE D 464     -40.109  34.182 -34.567  1.00114.54           C  
+ANISOU13219  CG1 ILE D 464    12949  12174  18399    502   2978  -6185       C  
+ATOM  13220  CG2 ILE D 464     -41.834  35.965 -34.944  1.00 90.52           C  
+ANISOU13220  CG2 ILE D 464     9601  10063  14728    276   2475  -6471       C  
+ATOM  13221  CD1 ILE D 464     -40.565  33.726 -33.199  1.00119.83           C  
+ANISOU13221  CD1 ILE D 464    13757  12310  19463    442   3123  -5892       C  
+ATOM  13222  N   ASN D 465     -37.594  34.761 -36.211  1.00108.10           N  
+ANISOU13222  N   ASN D 465    12079  11852  17143   1034   2957  -6094       N  
+ATOM  13223  CA  ASN D 465     -36.160  34.490 -36.161  1.00106.84           C  
+ANISOU13223  CA  ASN D 465    11958  11504  17133   1360   3109  -5823       C  
+ATOM  13224  C   ASN D 465     -35.372  35.329 -37.167  1.00111.97           C  
+ANISOU13224  C   ASN D 465    12489  12688  17366   1495   3016  -5876       C  
+ATOM  13225  O   ASN D 465     -34.262  35.769 -36.876  1.00116.58           O  
+ANISOU13225  O   ASN D 465    13015  13314  17967   1773   3019  -5532       O  
+ATOM  13226  CB  ASN D 465     -35.883  33.003 -36.384  1.00101.08           C  
+ANISOU13226  CB  ASN D 465    11354  10283  16770   1342   3435  -6009       C  
+ATOM  13227  CG  ASN D 465     -36.209  32.164 -35.163  1.00102.24           C  
+ANISOU13227  CG  ASN D 465    11663   9802  17381   1337   3593  -5760       C  
+ATOM  13228  OD1 ASN D 465     -36.208  32.662 -34.036  1.00104.67           O  
+ANISOU13228  OD1 ASN D 465    11994  10004  17771   1466   3478  -5329       O  
+ATOM  13229  ND2 ASN D 465     -36.486  30.884 -35.379  1.00110.20           N  
+ANISOU13229  ND2 ASN D 465    12800  10389  18684   1182   3877  -6022       N  
+ATOM  13230  N   THR D 466     -35.941  35.529 -38.352  1.00106.85           N  
+ANISOU13230  N   THR D 466    11793  12468  16336   1291   2944  -6305       N  
+ATOM  13231  CA  THR D 466     -35.335  36.390 -39.366  1.00 97.10           C  
+ANISOU13231  CA  THR D 466    10484  11778  14631   1390   2866  -6353       C  
+ATOM  13232  C   THR D 466     -35.149  37.799 -38.815  1.00 90.63           C  
+ANISOU13232  C   THR D 466     9597  11260  13576   1535   2644  -5960       C  
+ATOM  13233  O   THR D 466     -34.050  38.366 -38.864  1.00 89.54           O  
+ANISOU13233  O   THR D 466     9402  11264  13355   1741   2685  -5705       O  
+ATOM  13234  CB  THR D 466     -36.189  36.450 -40.647  1.00105.62           C  
+ANISOU13234  CB  THR D 466    11537  13321  15273   1146   2769  -6848       C  
+ATOM  13235  OG1 THR D 466     -36.366  35.127 -41.169  1.00124.84           O  
+ANISOU13235  OG1 THR D 466    14021  15475  17937    975   2991  -7252       O  
+ATOM  13236  CG2 THR D 466     -35.517  37.319 -41.700  1.00101.15           C  
+ANISOU13236  CG2 THR D 466    10944  13302  14188   1268   2727  -6848       C  
+ATOM  13237  N   ILE D 467     -36.240  38.348 -38.287  1.00 93.93           N  
+ANISOU13237  N   ILE D 467    10009  11775  13903   1413   2426  -5931       N  
+ATOM  13238  CA  ILE D 467     -36.249  39.692 -37.716  1.00 86.34           C  
+ANISOU13238  CA  ILE D 467     9048  11075  12681   1489   2159  -5457       C  
+ATOM  13239  C   ILE D 467     -35.196  39.817 -36.621  1.00 89.00           C  
+ANISOU13239  C   ILE D 467     9396  11107  13314   1678   2193  -4926       C  
+ATOM  13240  O   ILE D 467     -34.332  40.706 -36.645  1.00 88.84           O  
+ANISOU13240  O   ILE D 467     9346  11323  13085   1791   2120  -4597       O  
+ATOM  13241  CB  ILE D 467     -37.621  40.029 -37.103  1.00 84.15           C  
+ANISOU13241  CB  ILE D 467     8788  10825  12358   1320   1929  -5412       C  
+ATOM  13242  CG1 ILE D 467     -38.716  40.025 -38.171  1.00 89.50           C  
+ANISOU13242  CG1 ILE D 467     9391  11920  12693   1147   1827  -5924       C  
+ATOM  13243  CG2 ILE D 467     -37.557  41.353 -36.348  1.00 80.21           C  
+ANISOU13243  CG2 ILE D 467     8343  10484  11649   1401   1679  -4843       C  
+ATOM  13244  CD1 ILE D 467     -40.121  40.107 -37.601  1.00 86.96           C  
+ANISOU13244  CD1 ILE D 467     9013  11610  12417    967   1652  -5985       C  
+ATOM  13245  N   ILE D 468     -35.293  38.900 -35.664  1.00 93.20           N  
+ANISOU13245  N   ILE D 468     9968  11120  14323   1698   2312  -4857       N  
+ATOM  13246  CA  ILE D 468     -34.431  38.857 -34.495  1.00 90.48           C  
+ANISOU13246  CA  ILE D 468     9629  10479  14269   1894   2317  -4358       C  
+ATOM  13247  C   ILE D 468     -32.963  38.769 -34.879  1.00 93.66           C  
+ANISOU13247  C   ILE D 468     9908  10947  14732   2132   2463  -4274       C  
+ATOM  13248  O   ILE D 468     -32.127  39.429 -34.277  1.00 89.27           O  
+ANISOU13248  O   ILE D 468     9278  10505  14137   2259   2342  -3846       O  
+ATOM  13249  CB  ILE D 468     -34.783  37.664 -33.587  1.00 83.80           C  
+ANISOU13249  CB  ILE D 468     8883   9030  13925   1909   2493  -4348       C  
+ATOM  13250  N   GLU D 469     -32.648  37.937 -35.866  1.00 86.16           N  
+ANISOU13250  N   GLU D 469     8916   9935  13885   2181   2737  -4711       N  
+ATOM  13251  CA  GLU D 469     -31.266  37.767 -36.296  1.00108.99           C  
+ANISOU13251  CA  GLU D 469    11673  12897  16842   2409   2909  -4652       C  
+ATOM  13252  C   GLU D 469     -30.769  38.995 -37.053  1.00105.89           C  
+ANISOU13252  C   GLU D 469    11175  13079  15980   2373   2813  -4606       C  
+ATOM  13253  O   GLU D 469     -29.579  39.312 -37.022  1.00115.19           O  
+ANISOU13253  O   GLU D 469    12189  14396  17182   2534   2870  -4380       O  
+ATOM  13254  CB  GLU D 469     -31.124  36.520 -37.171  1.00 94.56           C  
+ANISOU13254  CB  GLU D 469     9934  10858  15136   2394   3166  -5000       C  
+ATOM  13255  N   PHE D 470     -31.686  39.691 -37.719  1.00 92.74           N  
+ANISOU13255  N   PHE D 470     9609  11756  13871   2155   2660  -4781       N  
+ATOM  13256  CA  PHE D 470     -31.336  40.927 -38.410  1.00 86.31           C  
+ANISOU13256  CA  PHE D 470     8780  11454  12560   2107   2565  -4652       C  
+ATOM  13257  C   PHE D 470     -30.955  42.009 -37.395  1.00 89.53           C  
+ANISOU13257  C   PHE D 470     9172  11920  12924   2112   2345  -4087       C  
+ATOM  13258  O   PHE D 470     -29.899  42.644 -37.506  1.00 85.27           O  
+ANISOU13258  O   PHE D 470     8523  11588  12288   2162   2396  -3871       O  
+ATOM  13259  CB  PHE D 470     -32.502  41.388 -39.291  1.00 84.30           C  
+ANISOU13259  CB  PHE D 470     8654  11544  11832   1927   2429  -4929       C  
+ATOM  13260  CG  PHE D 470     -32.224  42.639 -40.080  1.00 91.09           C  
+ANISOU13260  CG  PHE D 470     9564  12901  12146   1904   2363  -4776       C  
+ATOM  13261  CD1 PHE D 470     -31.584  42.568 -41.307  1.00 93.27           C  
+ANISOU13261  CD1 PHE D 470     9815  13466  12160   1939   2592  -5037       C  
+ATOM  13262  CD2 PHE D 470     -32.623  43.879 -39.610  1.00 89.70           C  
+ANISOU13262  CD2 PHE D 470     9490  12880  11712   1849   2111  -4375       C  
+ATOM  13263  CE1 PHE D 470     -31.332  43.712 -42.043  1.00 94.47           C  
+ANISOU13263  CE1 PHE D 470    10053  14048  11791   1916   2574  -4864       C  
+ATOM  13264  CE2 PHE D 470     -32.374  45.027 -40.342  1.00 96.30           C  
+ANISOU13264  CE2 PHE D 470    10422  14109  12060   1836   2097  -4207       C  
+ATOM  13265  CZ  PHE D 470     -31.728  44.943 -41.559  1.00 95.47           C  
+ANISOU13265  CZ  PHE D 470    10303  14285  11685   1867   2331  -4435       C  
+ATOM  13266  N   VAL D 471     -31.807  42.192 -36.390  1.00 83.36           N  
+ANISOU13266  N   VAL D 471     8492  10956  12226   2036   2124  -3879       N  
+ATOM  13267  CA  VAL D 471     -31.567  43.196 -35.355  1.00 87.83           C  
+ANISOU13267  CA  VAL D 471     9075  11557  12740   2012   1914  -3391       C  
+ATOM  13268  C   VAL D 471     -30.368  42.815 -34.478  1.00 97.78           C  
+ANISOU13268  C   VAL D 471    10164  12630  14358   2179   1968  -3118       C  
+ATOM  13269  O   VAL D 471     -29.625  43.678 -34.006  1.00104.62           O  
+ANISOU13269  O   VAL D 471    10950  13667  15133   2162   1868  -2798       O  
+ATOM  13270  CB  VAL D 471     -32.827  43.397 -34.479  1.00 85.09           C  
+ANISOU13270  CB  VAL D 471     8880  11053  12399   1900   1699  -3273       C  
+ATOM  13271  CG1 VAL D 471     -32.507  44.201 -33.226  1.00 81.62           C  
+ANISOU13271  CG1 VAL D 471     8466  10568  11979   1887   1519  -2802       C  
+ATOM  13272  CG2 VAL D 471     -33.920  44.085 -35.283  1.00 79.93           C  
+ANISOU13272  CG2 VAL D 471     8341  10698  11330   1772   1584  -3453       C  
+ATOM  13273  N   GLU D 472     -30.172  41.517 -34.276  1.00 98.36           N  
+ANISOU13273  N   GLU D 472    10176  12359  14836   2347   2134  -3257       N  
+ATOM  13274  CA  GLU D 472     -29.033  41.028 -33.507  1.00 93.14           C  
+ANISOU13274  CA  GLU D 472     9331  11539  14521   2586   2185  -2998       C  
+ATOM  13275  C   GLU D 472     -27.747  41.309 -34.268  1.00 97.43           C  
+ANISOU13275  C   GLU D 472     9627  12395  14996   2679   2336  -3044       C  
+ATOM  13276  O   GLU D 472     -26.737  41.687 -33.675  1.00 98.13           O  
+ANISOU13276  O   GLU D 472     9504  12625  15157   2772   2262  -2744       O  
+ATOM  13277  CB  GLU D 472     -29.170  39.536 -33.201  1.00 94.37           C  
+ANISOU13277  CB  GLU D 472     9523  11198  15135   2785   2377  -3130       C  
+ATOM  13278  CG  GLU D 472     -29.923  39.250 -31.908  1.00 98.48           C  
+ANISOU13278  CG  GLU D 472    10217  11372  15830   2772   2233  -2861       C  
+ATOM  13279  CD  GLU D 472     -30.271  37.784 -31.739  1.00117.69           C  
+ANISOU13279  CD  GLU D 472    12766  13253  18697   2908   2485  -3029       C  
+ATOM  13280  OE1 GLU D 472     -29.954  36.987 -32.646  1.00115.73           O  
+ANISOU13280  OE1 GLU D 472    12469  12880  18625   3010   2769  -3393       O  
+ATOM  13281  OE2 GLU D 472     -30.866  37.430 -30.698  1.00126.34           O  
+ANISOU13281  OE2 GLU D 472    14025  14019  19958   2904   2431  -2805       O  
+ATOM  13282  N   ILE D 473     -27.786  41.107 -35.583  1.00104.90           N  
+ANISOU13282  N   ILE D 473    10585  13480  15793   2643   2557  -3441       N  
+ATOM  13283  CA  ILE D 473     -26.655  41.455 -36.433  1.00101.81           C  
+ANISOU13283  CA  ILE D 473     9982  13423  15277   2689   2747  -3515       C  
+ATOM  13284  C   ILE D 473     -26.405  42.957 -36.344  1.00100.39           C  
+ANISOU13284  C   ILE D 473     9798  13620  14727   2479   2576  -3224       C  
+ATOM  13285  O   ILE D 473     -25.262  43.410 -36.399  1.00112.27           O  
+ANISOU13285  O   ILE D 473    11061  15362  16234   2498   2659  -3089       O  
+ATOM  13286  CB  ILE D 473     -26.893  41.056 -37.901  1.00 88.47           C  
+ANISOU13286  CB  ILE D 473     8368  11853  13393   2650   3011  -4010       C  
+ATOM  13287  N   LEU D 474     -27.486  43.722 -36.204  1.00100.84           N  
+ANISOU13287  N   LEU D 474    10113  13716  14485   2276   2363  -3141       N  
+ATOM  13288  CA  LEU D 474     -27.382  45.167 -36.017  1.00102.53           C  
+ANISOU13288  CA  LEU D 474    10394  14190  14374   2077   2217  -2849       C  
+ATOM  13289  C   LEU D 474     -26.660  45.520 -34.717  1.00115.25           C  
+ANISOU13289  C   LEU D 474    11839  15758  16194   2079   2055  -2481       C  
+ATOM  13290  O   LEU D 474     -25.878  46.469 -34.670  1.00116.06           O  
+ANISOU13290  O   LEU D 474    11833  16104  16161   1943   2061  -2306       O  
+ATOM  13291  CB  LEU D 474     -28.768  45.813 -36.030  1.00 94.18           C  
+ANISOU13291  CB  LEU D 474     9646  13130  13006   1927   2022  -2828       C  
+ATOM  13292  CG  LEU D 474     -29.380  46.069 -37.405  1.00 99.00           C  
+ANISOU13292  CG  LEU D 474    10422  13988  13208   1872   2117  -3098       C  
+ATOM  13293  CD1 LEU D 474     -30.833  46.491 -37.270  1.00 78.99           C  
+ANISOU13293  CD1 LEU D 474     8125  11440  10449   1796   1887  -3086       C  
+ATOM  13294  CD2 LEU D 474     -28.574  47.117 -38.153  1.00104.76           C  
+ANISOU13294  CD2 LEU D 474    11158  15042  13603   1781   2264  -2975       C  
+ATOM  13295  N   SER D 475     -26.930  44.754 -33.664  1.00119.06           N  
+ANISOU13295  N   SER D 475    12309  15942  16988   2216   1919  -2373       N  
+ATOM  13296  CA  SER D 475     -26.307  44.990 -32.366  1.00111.04           C  
+ANISOU13296  CA  SER D 475    11141  14919  16131   2245   1729  -2029       C  
+ATOM  13297  C   SER D 475     -24.936  44.328 -32.278  1.00113.88           C  
+ANISOU13297  C   SER D 475    11115  15360  16796   2486   1846  -2002       C  
+ATOM  13298  O   SER D 475     -23.931  44.902 -32.698  1.00111.90           O  
+ANISOU13298  O   SER D 475    10619  15430  16467   2414   1942  -2000       O  
+ATOM  13299  CB  SER D 475     -27.209  44.482 -31.240  1.00103.85           C  
+ANISOU13299  CB  SER D 475    10413  13673  15373   2306   1541  -1882       C  
+TER   13300      SER D 475                                                      
+HETATM13301  O   HOH A 501     -16.859  30.799  -6.670  0.81 32.32           O  
+HETATM13302  O   HOH A 502     -23.709   3.649 -17.621  1.00 58.27           O  
+HETATM13303  O   HOH A 503     -33.496  17.961  -0.825  0.99 52.52           O  
+HETATM13304  O   HOH A 504     -56.197  29.448  23.211  0.85 50.00           O  
+HETATM13305  O   HOH A 505     -12.165  25.213  -3.783  0.81 38.68           O  
+HETATM13306  O   HOH A 506     -24.536  16.807 -25.968  1.00 71.02           O  
+HETATM13307  O   HOH A 507     -29.266  12.369   1.832  0.85 36.01           O  
+HETATM13308  O   HOH A 508     -26.971  13.264 -16.755  0.97 40.98           O  
+HETATM13309  O   HOH A 509     -45.487   6.610  -7.775  0.92 61.34           O  
+HETATM13310  O   HOH A 510     -15.126  37.349  -6.947  1.00 42.51           O  
+HETATM13311  O   HOH A 511     -26.774   1.464  -4.575  1.00 61.15           O  
+HETATM13312  O   HOH A 512     -29.046  28.203  10.670  1.00 61.69           O  
+HETATM13313  O   HOH A 513     -13.405   8.827 -17.118  1.00 68.77           O  
+HETATM13314  O   HOH A 514      -2.477  40.036 -20.193  1.00 65.20           O  
+HETATM13315  O   HOH A 515     -64.969  20.266  14.000  1.00 54.07           O  
+HETATM13316  O   HOH B 501     -13.323   3.466  28.027  1.00 67.91           O  
+HETATM13317  O   HOH B 502     -55.492  23.012  27.512  1.00 33.92           O  
+HETATM13318  O   HOH B 503     -11.840  20.191   6.196  0.84 40.82           O  
+HETATM13319  O   HOH B 504     -48.362  16.968  32.837  1.00 63.29           O  
+HETATM13320  O   HOH B 505     -53.377  13.297  37.095  1.00 56.97           O  
+HETATM13321  O   HOH B 506      -7.212   7.772  25.424  1.00 55.40           O  
+HETATM13322  O   HOH B 507       1.583   6.884  32.566  1.00 63.40           O  
+HETATM13323  O   HOH B 508     -22.634  10.876  10.670  1.00 52.27           O  
+HETATM13324  O   HOH B 509     -24.255  -5.043  10.045  0.95 52.46           O  
+HETATM13325  O   HOH C 501     -24.539  37.060   1.744  1.00 60.87           O  
+HETATM13326  O   HOH C 502     -27.129  54.879  -3.449  0.98 53.53           O  
+HETATM13327  O   HOH C 503     -32.097  49.301  16.792  1.00 58.05           O  
+HETATM13328  O   HOH C 504     -20.823  40.624  -5.039  1.00 45.85           O  
+HETATM13329  O   HOH C 505     -13.534  58.180  16.872  1.00 58.87           O  
+HETATM13330  O   HOH C 506     -16.152  53.310  22.240  1.00 60.30           O  
+HETATM13331  O   HOH C 507     -23.573  35.571  -0.918  1.00 57.22           O  
+HETATM13332  O   HOH D 501     -54.936  46.269 -29.834  1.00 49.42           O  
+HETATM13333  O   HOH D 502     -52.053  56.702 -38.638  1.00 77.02           O  
+HETATM13334  O   HOH D 503     -11.889  47.539  -6.605  0.93 49.77           O  
+HETATM13335  O   HOH D 504     -44.818  59.323 -25.987  1.00 57.08           O  
+HETATM13336  O   HOH D 505      -6.753  59.961 -25.171  1.00 58.33           O  
+CONECT    3    6                                                                
+CONECT    6    3    7                                                           
+CONECT    7    6    8   10                                                      
+CONECT    8    7    9   14                                                      
+CONECT    9    8                                                                
+CONECT   10    7   11                                                           
+CONECT   11   10   12                                                           
+CONECT   12   11   13                                                           
+CONECT   13   12                                                                
+CONECT   14    8                                                                
+CONECT  135  140                                                                
+CONECT  140  135  141                                                           
+CONECT  141  140  142  144                                                      
+CONECT  142  141  143  148                                                      
+CONECT  143  142                                                                
+CONECT  144  141  145                                                           
+CONECT  145  144  146                                                           
+CONECT  146  145  147                                                           
+CONECT  147  146                                                                
+CONECT  148  142                                                                
+CONECT  231  235                                                                
+CONECT  235  231  236                                                           
+CONECT  236  235  237  239                                                      
+CONECT  237  236  238  243                                                      
+CONECT  238  237                                                                
+CONECT  239  236  240                                                           
+CONECT  240  239  241                                                           
+CONECT  241  240  242                                                           
+CONECT  242  241                                                                
+CONECT  243  237                                                                
+CONECT 1099 1106                                                                
+CONECT 1106 1099 1107                                                           
+CONECT 1107 1106 1108 1110                                                      
+CONECT 1108 1107 1109 1114                                                      
+CONECT 1109 1108                                                                
+CONECT 1110 1107 1111                                                           
+CONECT 1111 1110 1112                                                           
+CONECT 1112 1111 1113                                                           
+CONECT 1113 1112                                                                
+CONECT 1114 1108                                                                
+CONECT 1291 1298                                                                
+CONECT 1298 1291 1299                                                           
+CONECT 1299 1298 1300 1302                                                      
+CONECT 1300 1299 1301 1306                                                      
+CONECT 1301 1300                                                                
+CONECT 1302 1299 1303                                                           
+CONECT 1303 1302 1304                                                           
+CONECT 1304 1303 1305                                                           
+CONECT 1305 1304                                                                
+CONECT 1306 1300                                                                
+CONECT 2620 2630                                                                
+CONECT 2630 2620 2631                                                           
+CONECT 2631 2630 2632 2634                                                      
+CONECT 2632 2631 2633                                                           
+CONECT 2633 2632                                                                
+CONECT 2634 2631                                                                
+CONECT 2860 2866                                                                
+CONECT 2866 2860 2867                                                           
+CONECT 2867 2866 2868 2870                                                      
+CONECT 2868 2867 2869 2874                                                      
+CONECT 2869 2868                                                                
+CONECT 2870 2867 2871                                                           
+CONECT 2871 2870 2872                                                           
+CONECT 2872 2871 2873                                                           
+CONECT 2873 2872                                                                
+CONECT 2874 2868                                                                
+CONECT 3355 3364                                                                
+CONECT 3364 3355 3365                                                           
+CONECT 3365 3364 3366 3368                                                      
+CONECT 3366 3365 3367 3372                                                      
+CONECT 3367 3366                                                                
+CONECT 3368 3365 3369                                                           
+CONECT 3369 3368 3370                                                           
+CONECT 3370 3369 3371                                                           
+CONECT 3371 3370                                                                
+CONECT 3372 3366                                                                
+CONECT 3560 3563                                                                
+CONECT 3563 3560 3564                                                           
+CONECT 3564 3563 3565 3567                                                      
+CONECT 3565 3564 3566 3571                                                      
+CONECT 3566 3565                                                                
+CONECT 3567 3564 3568                                                           
+CONECT 3568 3567 3569                                                           
+CONECT 3569 3568 3570                                                           
+CONECT 3570 3569                                                                
+CONECT 3571 3565                                                                
+CONECT 3692 3697                                                                
+CONECT 3697 3692 3698                                                           
+CONECT 3698 3697 3699 3701                                                      
+CONECT 3699 3698 3700 3705                                                      
+CONECT 3700 3699                                                                
+CONECT 3701 3698 3702                                                           
+CONECT 3702 3701 3703                                                           
+CONECT 3703 3702 3704                                                           
+CONECT 3704 3703                                                                
+CONECT 3705 3699                                                                
+CONECT 3788 3792                                                                
+CONECT 3792 3788 3793                                                           
+CONECT 3793 3792 3794 3796                                                      
+CONECT 3794 3793 3795 3800                                                      
+CONECT 3795 3794                                                                
+CONECT 3796 3793 3797                                                           
+CONECT 3797 3796 3798                                                           
+CONECT 3798 3797 3799                                                           
+CONECT 3799 3798                                                                
+CONECT 3800 3794                                                                
+CONECT 4364 4371                                                                
+CONECT 4371 4364 4372                                                           
+CONECT 4372 4371 4373 4375                                                      
+CONECT 4373 4372 4374 4379                                                      
+CONECT 4374 4373                                                                
+CONECT 4375 4372 4376                                                           
+CONECT 4376 4375 4377                                                           
+CONECT 4377 4376 4378                                                           
+CONECT 4378 4377                                                                
+CONECT 4379 4373                                                                
+CONECT 4452 4455                                                                
+CONECT 4455 4452 4456                                                           
+CONECT 4456 4455 4457 4459                                                      
+CONECT 4457 4456 4458 4463                                                      
+CONECT 4458 4457                                                                
+CONECT 4459 4456 4460                                                           
+CONECT 4460 4459 4461                                                           
+CONECT 4461 4460 4462                                                           
+CONECT 4462 4461                                                                
+CONECT 4463 4457                                                                
+CONECT 5804 5814                                                                
+CONECT 5814 5804 5815                                                           
+CONECT 5815 5814 5816 5818                                                      
+CONECT 5816 5815 5817 5822                                                      
+CONECT 5817 5816                                                                
+CONECT 5818 5815 5819                                                           
+CONECT 5819 5818 5820                                                           
+CONECT 5820 5819 5821                                                           
+CONECT 5821 5820                                                                
+CONECT 5822 5816                                                                
+CONECT 6039 6045                                                                
+CONECT 6045 6039 6046                                                           
+CONECT 6046 6045 6047 6049                                                      
+CONECT 6047 6046 6048 6053                                                      
+CONECT 6048 6047                                                                
+CONECT 6049 6046 6050                                                           
+CONECT 6050 6049 6051                                                           
+CONECT 6051 6050 6052                                                           
+CONECT 6052 6051                                                                
+CONECT 6053 6047                                                                
+CONECT 6541 6542                                                                
+CONECT 6542 6541 6543 6545                                                      
+CONECT 6543 6542 6544 6549                                                      
+CONECT 6544 6543                                                                
+CONECT 6545 6542 6546                                                           
+CONECT 6546 6545 6547                                                           
+CONECT 6547 6546 6548                                                           
+CONECT 6548 6547                                                                
+CONECT 6549 6543                                                                
+CONECT 6731 6734                                                                
+CONECT 6734 6731 6735                                                           
+CONECT 6735 6734 6736 6738                                                      
+CONECT 6736 6735 6737 6742                                                      
+CONECT 6737 6736                                                                
+CONECT 6738 6735 6739                                                           
+CONECT 6739 6738 6740                                                           
+CONECT 6740 6739 6741                                                           
+CONECT 6741 6740                                                                
+CONECT 6742 6736                                                                
+CONECT 6859 6864                                                                
+CONECT 6864 6859 6865                                                           
+CONECT 6865 6864 6866 6868                                                      
+CONECT 6866 6865 6867 6872                                                      
+CONECT 6867 6866                                                                
+CONECT 6868 6865 6869                                                           
+CONECT 6869 6868 6870                                                           
+CONECT 6870 6869 6871                                                           
+CONECT 6871 6870                                                                
+CONECT 6872 6866                                                                
+CONECT 6955 6959                                                                
+CONECT 6959 6955 6960                                                           
+CONECT 6960 6959 6961 6963                                                      
+CONECT 6961 6960 6962 6967                                                      
+CONECT 6962 6961                                                                
+CONECT 6963 6960 6964                                                           
+CONECT 6964 6963 6965                                                           
+CONECT 6965 6964 6966                                                           
+CONECT 6966 6965                                                                
+CONECT 6967 6961                                                                
+CONECT 7832 7839                                                                
+CONECT 7839 7832 7840                                                           
+CONECT 7840 7839 7841 7843                                                      
+CONECT 7841 7840 7842 7847                                                      
+CONECT 7842 7841                                                                
+CONECT 7843 7840 7844                                                           
+CONECT 7844 7843 7845                                                           
+CONECT 7845 7844 7846                                                           
+CONECT 7846 7845                                                                
+CONECT 7847 7841                                                                
+CONECT 8024 8027                                                                
+CONECT 8027 8024 8028                                                           
+CONECT 8028 8027 8029 8031                                                      
+CONECT 8029 8028 8030 8035                                                      
+CONECT 8030 8029                                                                
+CONECT 8031 8028 8032                                                           
+CONECT 8032 8031 8033                                                           
+CONECT 8033 8032 8034                                                           
+CONECT 8034 8033                                                                
+CONECT 8035 8029                                                                
+CONECT 9352 9362                                                                
+CONECT 9362 9352 9363                                                           
+CONECT 9363 9362 9364 9366                                                      
+CONECT 9364 9363 9365                                                           
+CONECT 9365 9364                                                                
+CONECT 9366 9363                                                                
+CONECT 9585 9591                                                                
+CONECT 9591 9585 9592                                                           
+CONECT 9592 9591 9593 9595                                                      
+CONECT 9593 9592 9594 9599                                                      
+CONECT 9594 9593                                                                
+CONECT 9595 9592 9596                                                           
+CONECT 9596 9595 9597                                                           
+CONECT 9597 9596 9598                                                           
+CONECT 9598 9597                                                                
+CONECT 9599 9593                                                                
+CONECT1007910080                                                                
+CONECT10080100791008110083                                                      
+CONECT10081100801008210087                                                      
+CONECT1008210081                                                                
+CONECT100831008010084                                                           
+CONECT100841008310085                                                           
+CONECT100851008410086                                                           
+CONECT1008610085                                                                
+CONECT1008710081                                                                
+CONECT1026710275                                                                
+CONECT102751026710276                                                           
+CONECT10276102751027710279                                                      
+CONECT10277102761027810283                                                      
+CONECT1027810277                                                                
+CONECT102791027610280                                                           
+CONECT102801027910281                                                           
+CONECT102811028010282                                                           
+CONECT1028210281                                                                
+CONECT1028310277                                                                
+CONECT1040410409                                                                
+CONECT104091040410410                                                           
+CONECT10410104091041110413                                                      
+CONECT10411104101041210417                                                      
+CONECT1041210411                                                                
+CONECT104131041010414                                                           
+CONECT104141041310415                                                           
+CONECT104151041410416                                                           
+CONECT1041610415                                                                
+CONECT1041710411                                                                
+CONECT1050010504                                                                
+CONECT105041050010505                                                           
+CONECT10505105041050610508                                                      
+CONECT10506105051050710512                                                      
+CONECT1050710506                                                                
+CONECT105081050510509                                                           
+CONECT105091050810510                                                           
+CONECT105101050910511                                                           
+CONECT1051110510                                                                
+CONECT1051210506                                                                
+CONECT1107211079                                                                
+CONECT110791107211080                                                           
+CONECT11080110791108111083                                                      
+CONECT11081110801108211087                                                      
+CONECT1108211081                                                                
+CONECT110831108011084                                                           
+CONECT110841108311085                                                           
+CONECT110851108411086                                                           
+CONECT1108611085                                                                
+CONECT1108711081                                                                
+CONECT1113711140                                                                
+CONECT111401113711141                                                           
+CONECT11141111401114211144                                                      
+CONECT11142111411114311148                                                      
+CONECT1114311142                                                                
+CONECT111441114111145                                                           
+CONECT111451114411146                                                           
+CONECT111461114511147                                                           
+CONECT1114711146                                                                
+CONECT1114811142                                                                
+CONECT1263012636                                                                
+CONECT126361263012637                                                           
+CONECT12637126361263812640                                                      
+CONECT12638126371263912644                                                      
+CONECT1263912638                                                                
+CONECT126401263712641                                                           
+CONECT126411264012642                                                           
+CONECT126421264112643                                                           
+CONECT1264312642                                                                
+CONECT1264412638                                                                
+CONECT1313913140                                                                
+CONECT13140131391314113143                                                      
+CONECT13141131401314213147                                                      
+CONECT1314213141                                                                
+CONECT131431314013144                                                           
+CONECT131441314313145                                                           
+CONECT131451314413146                                                           
+CONECT1314613145                                                                
+CONECT1314713141                                                                
+MASTER      897    0   31   84   54    0    0    613332    4  299  148          
+END                                                                             
diff --git a/public/thoeris/6lhy_BcThsB_1mer.pdb b/public/thoeris/6lhy_BcThsB_1mer.pdb
new file mode 100644
index 0000000000000000000000000000000000000000..825f49d5f38771b36db68396f3ef6771d8794c0b
--- /dev/null
+++ b/public/thoeris/6lhy_BcThsB_1mer.pdb
@@ -0,0 +1,6723 @@
+HEADER    UNKNOWN FUNCTION                        10-DEC-19   6LHY              
+TITLE     CRYSTAL STRUCTURE OF THSB                                             
+COMPND    MOL_ID: 1;                                                            
+COMPND   2 MOLECULE: DUF1863 DOMAIN-CONTAINING PROTEIN;                         
+COMPND   3 CHAIN: A, B;                                                         
+COMPND   4 SYNONYM: THSB;                                                       
+COMPND   5 ENGINEERED: YES                                                      
+SOURCE    MOL_ID: 1;                                                            
+SOURCE   2 ORGANISM_SCIENTIFIC: BACILLUS CEREUS MSX-D12;                        
+SOURCE   3 ORGANISM_TAXID: 1053222;                                             
+SOURCE   4 GENE: II9_05449;                                                     
+SOURCE   5 EXPRESSION_SYSTEM: ESCHERICHIA COLI BL21(DE3);                       
+SOURCE   6 EXPRESSION_SYSTEM_TAXID: 469008                                      
+KEYWDS    TIR-LIKE DOMAIN, UNKNOWN FUNCTION                                     
+EXPDTA    X-RAY DIFFRACTION                                                     
+AUTHOR    E.BAE,D.KA,H.OH                                                       
+REVDAT   1   24-JUN-20 6LHY    0                                                
+JRNL        AUTH   D.KA,H.OH,E.PARK,J.H.KIM,E.BAE                               
+JRNL        TITL   STRUCTURAL AND FUNCTIONAL EVIDENCE OF BACTERIAL ANTIPHAGE    
+JRNL        TITL 2 PROTECTION BY THOERIS DEFENSE SYSTEM VIA NAD+DEGRADATION.    
+JRNL        REF    NAT COMMUN                    V.  11  2816 2020              
+JRNL        REFN                   ESSN 2041-1723                               
+JRNL        PMID   32499527                                                     
+JRNL        DOI    10.1038/S41467-020-16703-W                                   
+REMARK   2                                                                      
+REMARK   2 RESOLUTION.    1.80 ANGSTROMS.                                       
+REMARK   3                                                                      
+REMARK   3 REFINEMENT.                                                          
+REMARK   3   PROGRAM     : PHENIX 1.9_1692                                      
+REMARK   3   AUTHORS     : PAUL ADAMS,PAVEL AFONINE,VINCENT CHEN,IAN            
+REMARK   3               : DAVIS,KRESHNA GOPAL,RALF GROSSE-KUNSTLEVE,           
+REMARK   3               : LI-WEI HUNG,ROBERT IMMORMINO,TOM IOERGER,            
+REMARK   3               : AIRLIE MCCOY,ERIK MCKEE,NIGEL MORIARTY,              
+REMARK   3               : REETAL PAI,RANDY READ,JANE RICHARDSON,               
+REMARK   3               : DAVID RICHARDSON,TOD ROMO,JIM SACCHETTINI,           
+REMARK   3               : NICHOLAS SAUTER,JACOB SMITH,LAURENT                  
+REMARK   3               : STORONI,TOM TERWILLIGER,PETER ZWART                  
+REMARK   3                                                                      
+REMARK   3    REFINEMENT TARGET : MLHL                                          
+REMARK   3                                                                      
+REMARK   3  DATA USED IN REFINEMENT.                                            
+REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 1.80                           
+REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 29.56                          
+REMARK   3   MIN(FOBS/SIGMA_FOBS)              : 0.000                          
+REMARK   3   COMPLETENESS FOR RANGE        (%) : 98.4                           
+REMARK   3   NUMBER OF REFLECTIONS             : 38906                          
+REMARK   3                                                                      
+REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
+REMARK   3   R VALUE     (WORKING + TEST SET) : 0.193                           
+REMARK   3   R VALUE            (WORKING SET) : 0.191                           
+REMARK   3   FREE R VALUE                     : 0.226                           
+REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.100                           
+REMARK   3   FREE R VALUE TEST SET COUNT      : 1986                            
+REMARK   3                                                                      
+REMARK   3  FIT TO DATA USED IN REFINEMENT (IN BINS).                           
+REMARK   3   BIN  RESOLUTION RANGE  COMPL.    NWORK NFREE   RWORK  RFREE        
+REMARK   3     1 29.5590 -  4.3235    1.00     2759   146  0.1791 0.1939        
+REMARK   3     2  4.3235 -  3.4334    1.00     2703   145  0.1534 0.2129        
+REMARK   3     3  3.4334 -  2.9999    1.00     2683   142  0.1892 0.2020        
+REMARK   3     4  2.9999 -  2.7258    1.00     2684   149  0.2161 0.2619        
+REMARK   3     5  2.7258 -  2.5305    1.00     2668   138  0.2057 0.2545        
+REMARK   3     6  2.5305 -  2.3814    0.99     2671   147  0.2122 0.2333        
+REMARK   3     7  2.3814 -  2.2622    0.99     2646   139  0.2011 0.2380        
+REMARK   3     8  2.2622 -  2.1637    0.99     2653   135  0.1955 0.2624        
+REMARK   3     9  2.1637 -  2.0805    0.99     2635   153  0.1909 0.2374        
+REMARK   3    10  2.0805 -  2.0087    0.99     2650   148  0.1942 0.2179        
+REMARK   3    11  2.0087 -  1.9459    0.98     2614   136  0.1948 0.2049        
+REMARK   3    12  1.9459 -  1.8903    0.97     2574   130  0.2089 0.2626        
+REMARK   3    13  1.8903 -  1.8405    0.97     2551   156  0.2262 0.2613        
+REMARK   3    14  1.8405 -  1.7960    0.91     2429   122  0.2469 0.2832        
+REMARK   3                                                                      
+REMARK   3  BULK SOLVENT MODELLING.                                             
+REMARK   3   METHOD USED        : FLAT BULK SOLVENT MODEL                       
+REMARK   3   SOLVENT RADIUS     : 1.11                                          
+REMARK   3   SHRINKAGE RADIUS   : 0.90                                          
+REMARK   3   K_SOL              : NULL                                          
+REMARK   3   B_SOL              : NULL                                          
+REMARK   3                                                                      
+REMARK   3  ERROR ESTIMATES.                                                    
+REMARK   3   COORDINATE ERROR (MAXIMUM-LIKELIHOOD BASED)     : 0.210            
+REMARK   3   PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 22.660           
+REMARK   3                                                                      
+REMARK   3  B VALUES.                                                           
+REMARK   3   FROM WILSON PLOT           (A**2) : 21.25                          
+REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 28.64                          
+REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
+REMARK   3    B11 (A**2) : NULL                                                 
+REMARK   3    B22 (A**2) : NULL                                                 
+REMARK   3    B33 (A**2) : NULL                                                 
+REMARK   3    B12 (A**2) : NULL                                                 
+REMARK   3    B13 (A**2) : NULL                                                 
+REMARK   3    B23 (A**2) : NULL                                                 
+REMARK   3                                                                      
+REMARK   3  TWINNING INFORMATION.                                               
+REMARK   3   FRACTION: NULL                                                     
+REMARK   3   OPERATOR: NULL                                                     
+REMARK   3                                                                      
+REMARK   3  DEVIATIONS FROM IDEAL VALUES.                                       
+REMARK   3                 RMSD          COUNT                                  
+REMARK   3   BOND      :  0.007           2930                                  
+REMARK   3   ANGLE     :  0.951           3972                                  
+REMARK   3   CHIRALITY :  0.043            407                                  
+REMARK   3   PLANARITY :  0.004            503                                  
+REMARK   3   DIHEDRAL  : 11.920           1023                                  
+REMARK   3                                                                      
+REMARK   3  TLS DETAILS                                                         
+REMARK   3   NUMBER OF TLS GROUPS  : 18                                         
+REMARK   3   TLS GROUP : 1                                                      
+REMARK   3    SELECTION: CHAIN 'A' AND (RESID 3 THROUGH 18 )                    
+REMARK   3    ORIGIN FOR THE GROUP (A):  24.6680  28.3902  33.1790              
+REMARK   3    T TENSOR                                                          
+REMARK   3      T11:   0.2507 T22:   0.1433                                     
+REMARK   3      T33:   0.2395 T12:  -0.0738                                     
+REMARK   3      T13:   0.0549 T23:   0.0096                                     
+REMARK   3    L TENSOR                                                          
+REMARK   3      L11:   2.0699 L22:   4.2381                                     
+REMARK   3      L33:   6.0506 L12:  -6.6638                                     
+REMARK   3      L13:   3.0592 L23:  -2.3844                                     
+REMARK   3    S TENSOR                                                          
+REMARK   3      S11:   0.1995 S12:   0.4207 S13:   0.4424                       
+REMARK   3      S21:  -0.3064 S22:  -0.1814 S23:  -0.3560                       
+REMARK   3      S31:   0.0299 S32:   0.1132 S33:  -0.0271                       
+REMARK   3   TLS GROUP : 2                                                      
+REMARK   3    SELECTION: CHAIN 'A' AND (RESID 19 THROUGH 27 )                   
+REMARK   3    ORIGIN FOR THE GROUP (A):  29.9186  34.2038  37.0415              
+REMARK   3    T TENSOR                                                          
+REMARK   3      T11:   0.2651 T22:   0.1956                                     
+REMARK   3      T33:   0.2515 T12:  -0.0518                                     
+REMARK   3      T13:   0.0371 T23:  -0.0115                                     
+REMARK   3    L TENSOR                                                          
+REMARK   3      L11:   7.8862 L22:   4.2558                                     
+REMARK   3      L33:   3.7507 L12:  -0.1352                                     
+REMARK   3      L13:   2.5468 L23:  -0.4214                                     
+REMARK   3    S TENSOR                                                          
+REMARK   3      S11:  -0.1997 S12:   0.4848 S13:   0.0928                       
+REMARK   3      S21:  -0.2674 S22:   0.2421 S23:  -0.3963                       
+REMARK   3      S31:  -0.4881 S32:   0.3730 S33:   0.0226                       
+REMARK   3   TLS GROUP : 3                                                      
+REMARK   3    SELECTION: CHAIN 'A' AND (RESID 28 THROUGH 52 )                   
+REMARK   3    ORIGIN FOR THE GROUP (A):  33.9950  30.7638  33.0548              
+REMARK   3    T TENSOR                                                          
+REMARK   3      T11:   0.4012 T22:   0.3613                                     
+REMARK   3      T33:   0.3409 T12:  -0.0842                                     
+REMARK   3      T13:   0.1323 T23:  -0.0411                                     
+REMARK   3    L TENSOR                                                          
+REMARK   3      L11:   2.8203 L22:   4.4519                                     
+REMARK   3      L33:   5.4833 L12:   0.1088                                     
+REMARK   3      L13:   1.8390 L23:   1.2364                                     
+REMARK   3    S TENSOR                                                          
+REMARK   3      S11:  -0.1797 S12:   0.8957 S13:  -0.0703                       
+REMARK   3      S21:  -0.7092 S22:   0.2994 S23:  -0.7678                       
+REMARK   3      S31:  -0.2120 S32:   0.5037 S33:  -0.1189                       
+REMARK   3   TLS GROUP : 4                                                      
+REMARK   3    SELECTION: CHAIN 'A' AND (RESID 53 THROUGH 62 )                   
+REMARK   3    ORIGIN FOR THE GROUP (A):  32.2431  16.6988  25.9025              
+REMARK   3    T TENSOR                                                          
+REMARK   3      T11:   0.6789 T22:   0.3399                                     
+REMARK   3      T33:   0.3912 T12:  -0.1356                                     
+REMARK   3      T13:   0.2240 T23:  -0.0588                                     
+REMARK   3    L TENSOR                                                          
+REMARK   3      L11:   2.0149 L22:   5.8338                                     
+REMARK   3      L33:   4.6173 L12:   0.8888                                     
+REMARK   3      L13:  -4.3023 L23:  -0.6947                                     
+REMARK   3    S TENSOR                                                          
+REMARK   3      S11:  -0.6046 S12:   1.0124 S13:   0.0909                       
+REMARK   3      S21:  -1.8489 S22:   0.8655 S23:  -0.6079                       
+REMARK   3      S31:   0.0615 S32:   0.1548 S33:  -0.1895                       
+REMARK   3   TLS GROUP : 5                                                      
+REMARK   3    SELECTION: CHAIN 'A' AND (RESID 63 THROUGH 126 )                  
+REMARK   3    ORIGIN FOR THE GROUP (A):  22.8437  20.6856  38.2248              
+REMARK   3    T TENSOR                                                          
+REMARK   3      T11:   0.1550 T22:   0.1220                                     
+REMARK   3      T33:   0.1098 T12:  -0.0314                                     
+REMARK   3      T13:   0.0335 T23:  -0.0025                                     
+REMARK   3    L TENSOR                                                          
+REMARK   3      L11:   2.8894 L22:   4.2287                                     
+REMARK   3      L33:   1.8959 L12:  -1.5473                                     
+REMARK   3      L13:  -0.2153 L23:   0.5278                                     
+REMARK   3    S TENSOR                                                          
+REMARK   3      S11:   0.0145 S12:   0.0994 S13:   0.0040                       
+REMARK   3      S21:  -0.2407 S22:   0.0241 S23:  -0.2628                       
+REMARK   3      S31:   0.0165 S32:   0.0815 S33:  -0.0292                       
+REMARK   3   TLS GROUP : 6                                                      
+REMARK   3    SELECTION: CHAIN 'A' AND (RESID 127 THROUGH 145 )                 
+REMARK   3    ORIGIN FOR THE GROUP (A):  21.6378   2.3625  38.4569              
+REMARK   3    T TENSOR                                                          
+REMARK   3      T11:   0.3094 T22:   0.1295                                     
+REMARK   3      T33:   0.2715 T12:  -0.0189                                     
+REMARK   3      T13:   0.0390 T23:  -0.0405                                     
+REMARK   3    L TENSOR                                                          
+REMARK   3      L11:   5.7407 L22:   3.1630                                     
+REMARK   3      L33:   4.9615 L12:  -3.2489                                     
+REMARK   3      L13:   1.6831 L23:  -0.6469                                     
+REMARK   3    S TENSOR                                                          
+REMARK   3      S11:   0.4197 S12:   0.3318 S13:  -0.7677                       
+REMARK   3      S21:  -0.2528 S22:  -0.3290 S23:   0.3299                       
+REMARK   3      S31:   0.8118 S32:   0.0323 S33:  -0.0358                       
+REMARK   3   TLS GROUP : 7                                                      
+REMARK   3    SELECTION: CHAIN 'A' AND (RESID 146 THROUGH 159 )                 
+REMARK   3    ORIGIN FOR THE GROUP (A):  31.1843   3.6167  37.8554              
+REMARK   3    T TENSOR                                                          
+REMARK   3      T11:   0.2608 T22:   0.2356                                     
+REMARK   3      T33:   0.2399 T12:   0.0174                                     
+REMARK   3      T13:   0.0630 T23:   0.0031                                     
+REMARK   3    L TENSOR                                                          
+REMARK   3      L11:   4.3051 L22:   3.9998                                     
+REMARK   3      L33:   7.3920 L12:  -3.0221                                     
+REMARK   3      L13:   1.6660 L23:  -1.6408                                     
+REMARK   3    S TENSOR                                                          
+REMARK   3      S11:   0.2159 S12:   0.3922 S13:  -0.1857                       
+REMARK   3      S21:  -0.1608 S22:  -0.2972 S23:  -0.1218                       
+REMARK   3      S31:   0.5156 S32:   0.9795 S33:   0.0955                       
+REMARK   3   TLS GROUP : 8                                                      
+REMARK   3    SELECTION: CHAIN 'A' AND (RESID 160 THROUGH 182 )                 
+REMARK   3    ORIGIN FOR THE GROUP (A):  25.3601  15.2180  48.3367              
+REMARK   3    T TENSOR                                                          
+REMARK   3      T11:   0.1736 T22:   0.1803                                     
+REMARK   3      T33:   0.0942 T12:   0.0112                                     
+REMARK   3      T13:   0.0094 T23:   0.0104                                     
+REMARK   3    L TENSOR                                                          
+REMARK   3      L11:   2.9780 L22:   8.2759                                     
+REMARK   3      L33:   2.1454 L12:  -2.3573                                     
+REMARK   3      L13:  -0.4803 L23:  -0.5953                                     
+REMARK   3    S TENSOR                                                          
+REMARK   3      S11:  -0.1978 S12:  -0.2554 S13:  -0.2047                       
+REMARK   3      S21:   0.5461 S22:   0.0936 S23:   0.0323                       
+REMARK   3      S31:   0.2202 S32:   0.1630 S33:   0.0772                       
+REMARK   3   TLS GROUP : 9                                                      
+REMARK   3    SELECTION: CHAIN 'A' AND (RESID 183 THROUGH 192 )                 
+REMARK   3    ORIGIN FOR THE GROUP (A):  32.4836  31.3981  47.7198              
+REMARK   3    T TENSOR                                                          
+REMARK   3      T11:   0.3079 T22:   0.3225                                     
+REMARK   3      T33:   0.3242 T12:  -0.0209                                     
+REMARK   3      T13:  -0.0722 T23:   0.0165                                     
+REMARK   3    L TENSOR                                                          
+REMARK   3      L11:   4.7326 L22:   9.8621                                     
+REMARK   3      L33:   2.0534 L12:   3.1342                                     
+REMARK   3      L13:  -3.8634 L23:   1.9172                                     
+REMARK   3    S TENSOR                                                          
+REMARK   3      S11:   0.0035 S12:  -0.1233 S13:   0.0529                       
+REMARK   3      S21:   0.4458 S22:   0.1832 S23:  -0.8204                       
+REMARK   3      S31:  -0.4601 S32:   1.0413 S33:  -0.2282                       
+REMARK   3   TLS GROUP : 10                                                     
+REMARK   3    SELECTION: CHAIN 'B' AND (RESID 2 THROUGH 18 )                    
+REMARK   3    ORIGIN FOR THE GROUP (A):  48.0251 -21.6936  60.3036              
+REMARK   3    T TENSOR                                                          
+REMARK   3      T11:   0.0909 T22:   0.1323                                     
+REMARK   3      T33:   0.1985 T12:  -0.0071                                     
+REMARK   3      T13:   0.0511 T23:  -0.0324                                     
+REMARK   3    L TENSOR                                                          
+REMARK   3      L11:   1.8820 L22:   4.8890                                     
+REMARK   3      L33:   7.7120 L12:   0.2895                                     
+REMARK   3      L13:   1.0247 L23:   0.4791                                     
+REMARK   3    S TENSOR                                                          
+REMARK   3      S11:  -0.0931 S12:   0.1829 S13:  -0.2221                       
+REMARK   3      S21:  -0.0792 S22:   0.2627 S23:  -0.1766                       
+REMARK   3      S31:  -0.0202 S32:   0.1406 S33:  -0.2411                       
+REMARK   3   TLS GROUP : 11                                                     
+REMARK   3    SELECTION: CHAIN 'B' AND (RESID 19 THROUGH 52 )                   
+REMARK   3    ORIGIN FOR THE GROUP (A):  44.9919 -26.4519  53.9646              
+REMARK   3    T TENSOR                                                          
+REMARK   3      T11:   0.2236 T22:   0.3196                                     
+REMARK   3      T33:   0.3307 T12:  -0.0045                                     
+REMARK   3      T13:   0.0613 T23:  -0.0536                                     
+REMARK   3    L TENSOR                                                          
+REMARK   3      L11:   1.7519 L22:   6.6711                                     
+REMARK   3      L33:   4.6708 L12:   0.8900                                     
+REMARK   3      L13:   2.4477 L23:   3.9131                                     
+REMARK   3    S TENSOR                                                          
+REMARK   3      S11:   0.3052 S12:   0.8513 S13:  -0.2163                       
+REMARK   3      S21:  -0.5964 S22:   0.4042 S23:  -0.3142                       
+REMARK   3      S31:  -0.0143 S32:   0.3478 S33:  -0.5777                       
+REMARK   3   TLS GROUP : 12                                                     
+REMARK   3    SELECTION: CHAIN 'B' AND (RESID 53 THROUGH 62 )                   
+REMARK   3    ORIGIN FOR THE GROUP (A):  53.7307  -9.5583  51.3476              
+REMARK   3    T TENSOR                                                          
+REMARK   3      T11:   0.5455 T22:   0.6815                                     
+REMARK   3      T33:   0.5074 T12:  -0.1277                                     
+REMARK   3      T13:   0.2879 T23:  -0.1259                                     
+REMARK   3    L TENSOR                                                          
+REMARK   3      L11:   7.4101 L22:   4.0050                                     
+REMARK   3      L33:   7.0741 L12:   0.8185                                     
+REMARK   3      L13:  -3.1356 L23:  -1.9041                                     
+REMARK   3    S TENSOR                                                          
+REMARK   3      S11:  -0.8014 S12:   1.2250 S13:  -0.1793                       
+REMARK   3      S21:  -0.8608 S22:   0.7919 S23:  -0.8574                       
+REMARK   3      S31:   0.8129 S32:   1.2879 S33:  -0.0223                       
+REMARK   3   TLS GROUP : 13                                                     
+REMARK   3    SELECTION: CHAIN 'B' AND (RESID 63 THROUGH 126 )                  
+REMARK   3    ORIGIN FOR THE GROUP (A):  42.6394 -13.8516  62.0915              
+REMARK   3    T TENSOR                                                          
+REMARK   3      T11:   0.1442 T22:   0.1471                                     
+REMARK   3      T33:   0.1538 T12:  -0.0243                                     
+REMARK   3      T13:   0.0326 T23:  -0.0110                                     
+REMARK   3    L TENSOR                                                          
+REMARK   3      L11:   2.7643 L22:   3.6088                                     
+REMARK   3      L33:   2.3528 L12:  -0.2699                                     
+REMARK   3      L13:   0.2205 L23:  -0.3924                                     
+REMARK   3    S TENSOR                                                          
+REMARK   3      S11:  -0.0754 S12:   0.2980 S13:   0.0833                       
+REMARK   3      S21:  -0.3546 S22:   0.1263 S23:  -0.1632                       
+REMARK   3      S31:  -0.0772 S32:   0.1203 S33:  -0.0349                       
+REMARK   3   TLS GROUP : 14                                                     
+REMARK   3    SELECTION: CHAIN 'B' AND (RESID 127 THROUGH 145 )                 
+REMARK   3    ORIGIN FOR THE GROUP (A):  41.1624   5.2182  62.5006              
+REMARK   3    T TENSOR                                                          
+REMARK   3      T11:   0.3518 T22:   0.1627                                     
+REMARK   3      T33:   0.2686 T12:  -0.0050                                     
+REMARK   3      T13:   0.0102 T23:  -0.0059                                     
+REMARK   3    L TENSOR                                                          
+REMARK   3      L11:   5.2780 L22:   8.5884                                     
+REMARK   3      L33:   2.2084 L12:  -2.9377                                     
+REMARK   3      L13:   3.9101 L23:  -8.9745                                     
+REMARK   3    S TENSOR                                                          
+REMARK   3      S11:  -0.2295 S12:   0.0310 S13:   0.5748                       
+REMARK   3      S21:   0.8016 S22:  -0.2122 S23:  -0.2819                       
+REMARK   3      S31:  -1.3005 S32:   0.2123 S33:   0.5360                       
+REMARK   3   TLS GROUP : 15                                                     
+REMARK   3    SELECTION: CHAIN 'B' AND (RESID 146 THROUGH 159 )                 
+REMARK   3    ORIGIN FOR THE GROUP (A):  42.1034   5.3160  52.3466              
+REMARK   3    T TENSOR                                                          
+REMARK   3      T11:   0.2157 T22:   0.2322                                     
+REMARK   3      T33:   0.2546 T12:  -0.0256                                     
+REMARK   3      T13:   0.0620 T23:   0.0428                                     
+REMARK   3    L TENSOR                                                          
+REMARK   3      L11:   5.8538 L22:   5.8675                                     
+REMARK   3      L33:   1.7253 L12:  -5.7996                                     
+REMARK   3      L13:   2.2249 L23:  -2.6109                                     
+REMARK   3    S TENSOR                                                          
+REMARK   3      S11:   0.3229 S12:   0.7466 S13:   0.3581                       
+REMARK   3      S21:  -0.1317 S22:  -0.6587 S23:  -0.3754                       
+REMARK   3      S31:  -0.0012 S32:   0.3370 S33:   0.4200                       
+REMARK   3   TLS GROUP : 16                                                     
+REMARK   3    SELECTION: CHAIN 'B' AND (RESID 160 THROUGH 171 )                 
+REMARK   3    ORIGIN FOR THE GROUP (A):  31.3539   2.6679  59.5141              
+REMARK   3    T TENSOR                                                          
+REMARK   3      T11:   0.3151 T22:   0.2343                                     
+REMARK   3      T33:   0.2606 T12:   0.0642                                     
+REMARK   3      T13:   0.0382 T23:   0.0437                                     
+REMARK   3    L TENSOR                                                          
+REMARK   3      L11:   1.1530 L22:   2.0257                                     
+REMARK   3      L33:   2.4128 L12:  -3.6023                                     
+REMARK   3      L13:   1.6020 L23:  -4.9301                                     
+REMARK   3    S TENSOR                                                          
+REMARK   3      S11:  -0.1561 S12:  -0.0273 S13:  -0.1003                       
+REMARK   3      S21:   0.2622 S22:   0.3077 S23:   0.5300                       
+REMARK   3      S31:  -0.4418 S32:  -0.4211 S33:  -0.2239                       
+REMARK   3   TLS GROUP : 17                                                     
+REMARK   3    SELECTION: CHAIN 'B' AND (RESID 172 THROUGH 182 )                 
+REMARK   3    ORIGIN FOR THE GROUP (A):  32.8759 -20.6091  61.2337              
+REMARK   3    T TENSOR                                                          
+REMARK   3      T11:   0.1743 T22:   0.2046                                     
+REMARK   3      T33:   0.2625 T12:  -0.0233                                     
+REMARK   3      T13:  -0.0025 T23:   0.0182                                     
+REMARK   3    L TENSOR                                                          
+REMARK   3      L11:   0.8878 L22:   2.0399                                     
+REMARK   3      L33:   2.6620 L12:  -1.1788                                     
+REMARK   3      L13:  -0.0390 L23:  -3.8507                                     
+REMARK   3    S TENSOR                                                          
+REMARK   3      S11:  -0.0273 S12:   0.2783 S13:  -0.1571                       
+REMARK   3      S21:  -0.0251 S22:   0.1758 S23:   0.7929                       
+REMARK   3      S31:   0.1470 S32:  -0.3089 S33:  -0.2162                       
+REMARK   3   TLS GROUP : 18                                                     
+REMARK   3    SELECTION: CHAIN 'B' AND (RESID 183 THROUGH 192 )                 
+REMARK   3    ORIGIN FOR THE GROUP (A):  33.7206 -26.2219  54.4793              
+REMARK   3    T TENSOR                                                          
+REMARK   3      T11:   0.3844 T22:   0.3829                                     
+REMARK   3      T33:   0.3124 T12:  -0.0460                                     
+REMARK   3      T13:  -0.0589 T23:  -0.0635                                     
+REMARK   3    L TENSOR                                                          
+REMARK   3      L11:   2.0464 L22:   2.0616                                     
+REMARK   3      L33:   2.0331 L12:   6.6586                                     
+REMARK   3      L13:  -8.4680 L23:  -6.6903                                     
+REMARK   3    S TENSOR                                                          
+REMARK   3      S11:  -0.3919 S12:   0.9895 S13:  -0.5107                       
+REMARK   3      S21:  -1.0923 S22:   0.5169 S23:  -0.1622                       
+REMARK   3      S31:   0.5752 S32:  -0.8015 S33:  -0.1050                       
+REMARK   3                                                                      
+REMARK   3  NCS DETAILS                                                         
+REMARK   3   NUMBER OF NCS GROUPS : NULL                                        
+REMARK   3                                                                      
+REMARK   3  OTHER REFINEMENT REMARKS: NULL                                      
+REMARK   4                                                                      
+REMARK   4 6LHY COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
+REMARK 100                                                                      
+REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 11-DEC-19.                  
+REMARK 100 THE DEPOSITION ID IS D_1300014782.                                   
+REMARK 200                                                                      
+REMARK 200 EXPERIMENTAL DETAILS                                                 
+REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
+REMARK 200  DATE OF DATA COLLECTION        : 12-MAR-19                          
+REMARK 200  TEMPERATURE           (KELVIN) : 100                                
+REMARK 200  PH                             : NULL                               
+REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
+REMARK 200                                                                      
+REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
+REMARK 200  RADIATION SOURCE               : PAL/PLS                            
+REMARK 200  BEAMLINE                       : 7A (6B, 6C1)                       
+REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
+REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
+REMARK 200  WAVELENGTH OR RANGE        (A) : 0.97910                            
+REMARK 200  MONOCHROMATOR                  : NULL                               
+REMARK 200  OPTICS                         : NULL                               
+REMARK 200                                                                      
+REMARK 200  DETECTOR TYPE                  : CCD                                
+REMARK 200  DETECTOR MANUFACTURER          : ADSC QUANTUM 270                   
+REMARK 200  INTENSITY-INTEGRATION SOFTWARE : HKL-2000                           
+REMARK 200  DATA SCALING SOFTWARE          : HKL-2000                           
+REMARK 200                                                                      
+REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 39424                              
+REMARK 200  RESOLUTION RANGE HIGH      (A) : 1.796                              
+REMARK 200  RESOLUTION RANGE LOW       (A) : 50.000                             
+REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : NULL                               
+REMARK 200                                                                      
+REMARK 200 OVERALL.                                                             
+REMARK 200  COMPLETENESS FOR RANGE     (%) : 99.0                               
+REMARK 200  DATA REDUNDANCY                : 3.800                              
+REMARK 200  R MERGE                    (I) : 0.09200                            
+REMARK 200  R SYM                      (I) : NULL                               
+REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 12.3500                            
+REMARK 200                                                                      
+REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
+REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.80                     
+REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 1.86                     
+REMARK 200  COMPLETENESS FOR SHELL     (%) : NULL                               
+REMARK 200  DATA REDUNDANCY IN SHELL       : NULL                               
+REMARK 200  R MERGE FOR SHELL          (I) : 0.60500                            
+REMARK 200  R SYM FOR SHELL            (I) : NULL                               
+REMARK 200  <I/SIGMA(I)> FOR SHELL         : 2.310                              
+REMARK 200                                                                      
+REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
+REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: SAD                          
+REMARK 200 SOFTWARE USED: AUTOSOL                                               
+REMARK 200 STARTING MODEL: NULL                                                 
+REMARK 200                                                                      
+REMARK 200 REMARK: NULL                                                         
+REMARK 280                                                                      
+REMARK 280 CRYSTAL                                                              
+REMARK 280 SOLVENT CONTENT, VS   (%): 48.07                                     
+REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.37                     
+REMARK 280                                                                      
+REMARK 280 CRYSTALLIZATION CONDITIONS: 3 M NACL, 0.1 M TRIS PH 8.5, VAPOR       
+REMARK 280  DIFFUSION, SITTING DROP, TEMPERATURE 293K                           
+REMARK 290                                                                      
+REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
+REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 1 21 1                         
+REMARK 290                                                                      
+REMARK 290      SYMOP   SYMMETRY                                                
+REMARK 290     NNNMMM   OPERATOR                                                
+REMARK 290       1555   X,Y,Z                                                   
+REMARK 290       2555   -X,Y+1/2,-Z                                             
+REMARK 290                                                                      
+REMARK 290     WHERE NNN -> OPERATOR NUMBER                                     
+REMARK 290           MMM -> TRANSLATION VECTOR                                  
+REMARK 290                                                                      
+REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS                            
+REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM             
+REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY                
+REMARK 290 RELATED MOLECULES.                                                   
+REMARK 290   SMTRY1   1  1.000000  0.000000  0.000000        0.00000            
+REMARK 290   SMTRY2   1  0.000000  1.000000  0.000000        0.00000            
+REMARK 290   SMTRY3   1  0.000000  0.000000  1.000000        0.00000            
+REMARK 290   SMTRY1   2 -1.000000  0.000000  0.000000        0.00000            
+REMARK 290   SMTRY2   2  0.000000  1.000000  0.000000       33.86550            
+REMARK 290   SMTRY3   2  0.000000  0.000000 -1.000000        0.00000            
+REMARK 290                                                                      
+REMARK 290 REMARK: NULL                                                         
+REMARK 300                                                                      
+REMARK 300 BIOMOLECULE: 1, 2                                                    
+REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM                
+REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN                  
+REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON               
+REMARK 300 BURIED SURFACE AREA.                                                 
+REMARK 350                                                                      
+REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN           
+REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE                
+REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS          
+REMARK 350 GIVEN BELOW.  BOTH NON-CRYSTALLOGRAPHIC AND                          
+REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.                               
+REMARK 350                                                                      
+REMARK 350 BIOMOLECULE: 1                                                       
+REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC                         
+REMARK 350 APPLY THE FOLLOWING TO CHAINS: A                                     
+REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
+REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
+REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
+REMARK 350                                                                      
+REMARK 350 BIOMOLECULE: 2                                                       
+REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC                         
+REMARK 350 APPLY THE FOLLOWING TO CHAINS: B                                     
+REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
+REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
+REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
+REMARK 465                                                                      
+REMARK 465 MISSING RESIDUES                                                     
+REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE                       
+REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
+REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)                
+REMARK 465                                                                      
+REMARK 465   M RES C SSSEQI                                                     
+REMARK 465     GLY A    -1                                                      
+REMARK 465     HIS A     0                                                      
+REMARK 465     MSE A     1                                                      
+REMARK 465     ALA A     2                                                      
+REMARK 465     ASP A    39                                                      
+REMARK 465     ALA A    40                                                      
+REMARK 465     SER A    41                                                      
+REMARK 465     LEU A    42                                                      
+REMARK 465     TRP A    43                                                      
+REMARK 465     GLU A    44                                                      
+REMARK 465     ASP A    45                                                      
+REMARK 465     ALA A    46                                                      
+REMARK 465     LYS A    47                                                      
+REMARK 465     LYS A    48                                                      
+REMARK 465     THR A    49                                                      
+REMARK 465     SER A    50                                                      
+REMARK 465     ASP A    51                                                      
+REMARK 465     GLY B    -1                                                      
+REMARK 465     HIS B     0                                                      
+REMARK 465     MSE B     1                                                      
+REMARK 465     LEU B    30                                                      
+REMARK 465     ASN B    31                                                      
+REMARK 465     GLY B    36                                                      
+REMARK 465     VAL B    37                                                      
+REMARK 465     PHE B    38                                                      
+REMARK 465     ASP B    39                                                      
+REMARK 465     ALA B    40                                                      
+REMARK 465     SER B    41                                                      
+REMARK 465     LEU B    42                                                      
+REMARK 465     TRP B    43                                                      
+REMARK 465     GLU B    44                                                      
+REMARK 465     ASP B    45                                                      
+REMARK 465     ALA B    46                                                      
+REMARK 465     LYS B    47                                                      
+REMARK 465     LYS B    48                                                      
+REMARK 465     THR B    49                                                      
+REMARK 465     SER B    50                                                      
+REMARK 465     ASP B    51                                                      
+REMARK 470                                                                      
+REMARK 470 MISSING ATOM                                                         
+REMARK 470 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER;           
+REMARK 470 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;          
+REMARK 470 I=INSERTION CODE):                                                   
+REMARK 470   M RES CSSEQI  ATOMS                                                
+REMARK 470     LYS A  29    CG   CD   CE   NZ                                   
+REMARK 470     ILE A  52    CG1  CG2  CD1                                       
+REMARK 470     ARG A  56    CG   CD   NE   CZ   NH1  NH2                        
+REMARK 470     ASN A  63    CG   OD1  ND2                                       
+REMARK 470     ASN A  64    CG   OD1  ND2                                       
+REMARK 470     LYS A  92    CG   CD   CE   NZ                                   
+REMARK 470     LYS A 131    CG   CD   CE   NZ                                   
+REMARK 470     ARG A 153    CG   CD   NE   CZ   NH1  NH2                        
+REMARK 470     ASN A 155    CG   OD1  ND2                                       
+REMARK 470     LYS A 165    CG   CD   CE   NZ                                   
+REMARK 470     ARG B   4    CG   CD   NE   CZ   NH1  NH2                        
+REMARK 470     LYS B  29    CG   CD   CE   NZ                                   
+REMARK 470     ILE B  52    CG1  CG2  CD1                                       
+REMARK 470     ARG B  56    CG   CD   NE   CZ   NH1  NH2                        
+REMARK 470     ASN B  63    CG   OD1  ND2                                       
+REMARK 470     ASN B  64    CG   OD1  ND2                                       
+REMARK 470     GLU B 160    CG   CD   OE1  OE2                                  
+REMARK 525                                                                      
+REMARK 525 SOLVENT                                                              
+REMARK 525                                                                      
+REMARK 525 THE SOLVENT MOLECULES HAVE CHAIN IDENTIFIERS THAT                    
+REMARK 525 INDICATE THE POLYMER CHAIN WITH WHICH THEY ARE MOST                  
+REMARK 525 CLOSELY ASSOCIATED. THE REMARK LISTS ALL THE SOLVENT                 
+REMARK 525 MOLECULES WHICH ARE MORE THAN 5A AWAY FROM THE                       
+REMARK 525 NEAREST POLYMER CHAIN (M = MODEL NUMBER;                             
+REMARK 525 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE                  
+REMARK 525 NUMBER; I=INSERTION CODE):                                           
+REMARK 525                                                                      
+REMARK 525  M RES CSSEQI                                                        
+REMARK 525    HOH A 373        DISTANCE =  6.83 ANGSTROMS                       
+REMARK 525    HOH B 359        DISTANCE =  6.20 ANGSTROMS                       
+DBREF  6LHY A    1   192  UNP    J8G8J6   J8G8J6_BACCE     1    192             
+DBREF  6LHY B    1   192  UNP    J8G8J6   J8G8J6_BACCE     1    192             
+SEQADV 6LHY GLY A   -1  UNP  J8G8J6              EXPRESSION TAG                 
+SEQADV 6LHY HIS A    0  UNP  J8G8J6              EXPRESSION TAG                 
+SEQADV 6LHY GLY B   -1  UNP  J8G8J6              EXPRESSION TAG                 
+SEQADV 6LHY HIS B    0  UNP  J8G8J6              EXPRESSION TAG                 
+SEQRES   1 A  194  GLY HIS MSE ALA LYS ARG VAL PHE PHE SER PHE HIS TYR          
+SEQRES   2 A  194  GLN ASP VAL ILE ASP PHE ARG VAL ASN VAL VAL ARG ASN          
+SEQRES   3 A  194  HIS TRP VAL THR LYS LEU ASN GLN SER ALA ALA GLY VAL          
+SEQRES   4 A  194  PHE ASP ALA SER LEU TRP GLU ASP ALA LYS LYS THR SER          
+SEQRES   5 A  194  ASP ILE ALA LEU LYS ARG LEU ILE ASN GLY GLY LEU ASN          
+SEQRES   6 A  194  ASN THR SER VAL THR CYS VAL LEU ILE GLY SER GLN THR          
+SEQRES   7 A  194  PHE ASN ARG ARG TRP VAL ARG TYR GLU ILE MSE LYS SER          
+SEQRES   8 A  194  ILE GLU LYS GLY ASN LYS ILE ILE GLY ILE HIS ILE ASN          
+SEQRES   9 A  194  ALA PHE LYS ASP LYS TYR GLY ASN ILE LYS SER LYS GLY          
+SEQRES  10 A  194  PRO ASN PRO PHE ASP TYR LEU GLY TYR GLN TYR SER SER          
+SEQRES  11 A  194  ASP GLY LYS GLN LEU HIS LEU TYR GLU TRP THR GLY GLY          
+SEQRES  12 A  194  LYS TRP GLU GLU TYR LYS ASP LEU ALA PRO TYR ARG VAL          
+SEQRES  13 A  194  ASN GLN ILE ALA PRO GLU SER LEU ARG GLY LYS PHE TYR          
+SEQRES  14 A  194  SER LEU SER SER VAL TYR ARG VAL TYR ASP TRP VAL ALA          
+SEQRES  15 A  194  ASP ASP GLY TYR ASN LYS PHE SER SER TRP VAL ASN              
+SEQRES   1 B  194  GLY HIS MSE ALA LYS ARG VAL PHE PHE SER PHE HIS TYR          
+SEQRES   2 B  194  GLN ASP VAL ILE ASP PHE ARG VAL ASN VAL VAL ARG ASN          
+SEQRES   3 B  194  HIS TRP VAL THR LYS LEU ASN GLN SER ALA ALA GLY VAL          
+SEQRES   4 B  194  PHE ASP ALA SER LEU TRP GLU ASP ALA LYS LYS THR SER          
+SEQRES   5 B  194  ASP ILE ALA LEU LYS ARG LEU ILE ASN GLY GLY LEU ASN          
+SEQRES   6 B  194  ASN THR SER VAL THR CYS VAL LEU ILE GLY SER GLN THR          
+SEQRES   7 B  194  PHE ASN ARG ARG TRP VAL ARG TYR GLU ILE MSE LYS SER          
+SEQRES   8 B  194  ILE GLU LYS GLY ASN LYS ILE ILE GLY ILE HIS ILE ASN          
+SEQRES   9 B  194  ALA PHE LYS ASP LYS TYR GLY ASN ILE LYS SER LYS GLY          
+SEQRES  10 B  194  PRO ASN PRO PHE ASP TYR LEU GLY TYR GLN TYR SER SER          
+SEQRES  11 B  194  ASP GLY LYS GLN LEU HIS LEU TYR GLU TRP THR GLY GLY          
+SEQRES  12 B  194  LYS TRP GLU GLU TYR LYS ASP LEU ALA PRO TYR ARG VAL          
+SEQRES  13 B  194  ASN GLN ILE ALA PRO GLU SER LEU ARG GLY LYS PHE TYR          
+SEQRES  14 B  194  SER LEU SER SER VAL TYR ARG VAL TYR ASP TRP VAL ALA          
+SEQRES  15 B  194  ASP ASP GLY TYR ASN LYS PHE SER SER TRP VAL ASN              
+MODRES 6LHY MSE A   87  MET  MODIFIED RESIDUE                                   
+MODRES 6LHY MSE B   87  MET  MODIFIED RESIDUE                                   
+HET    MSE  A  87       8                                                       
+HET    MSE  B  87       8                                                       
+HETNAM     MSE SELENOMETHIONINE                                                 
+FORMUL   1  MSE    2(C5 H11 N O2 SE)                                            
+FORMUL   3  HOH   *332(H2 O)                                                    
+HELIX    1 AA1 HIS A   10  ASP A   16  1                                   7    
+HELIX    2 AA2 ARG A   18  THR A   28  1                                  11    
+HELIX    3 AA3 ALA A   53  ASN A   63  1                                  11    
+HELIX    4 AA4 GLN A   75  ASN A   78  5                                   4    
+HELIX    5 AA5 ARG A   79  GLY A   93  1                                  15    
+HELIX    6 AA6 ASN A  117  ASP A  120  5                                   4    
+HELIX    7 AA7 PRO A  159  ARG A  163  5                                   5    
+HELIX    8 AA8 SER A  170  VAL A  172  5                                   3    
+HELIX    9 AA9 ASP A  182  VAL A  191  1                                  10    
+HELIX   10 AB1 TYR B   11  ASP B   16  1                                   6    
+HELIX   11 AB2 ARG B   18  THR B   28  1                                  11    
+HELIX   12 AB3 ALA B   53  ASN B   63  1                                  11    
+HELIX   13 AB4 GLN B   75  ASN B   78  5                                   4    
+HELIX   14 AB5 ARG B   79  LYS B   92  1                                  14    
+HELIX   15 AB6 ASN B  117  ASP B  120  5                                   4    
+HELIX   16 AB7 PRO B  159  ARG B  163  5                                   5    
+HELIX   17 AB8 SER B  170  VAL B  172  5                                   3    
+HELIX   18 AB9 ASP B  182  ASN B  192  1                                  11    
+SHEET    1 AA1 5 ALA A  34  ALA A  35  0                                        
+SHEET    2 AA1 5 VAL A   5  SER A   8  1  N  PHE A   7   O  ALA A  35           
+SHEET    3 AA1 5 VAL A  67  ILE A  72  1  O  VAL A  67   N  PHE A   6           
+SHEET    4 AA1 5 LYS A  95  HIS A 100  1  O  LYS A  95   N  THR A  68           
+SHEET    5 AA1 5 ARG A 174  ASP A 177  1  O  TYR A 176   N  GLY A  98           
+SHEET    1 AA2 3 TRP A 143  GLU A 145  0                                        
+SHEET    2 AA2 3 GLN A 132  TRP A 138 -1  N  GLU A 137   O  GLU A 144           
+SHEET    3 AA2 3 TYR A 152  ARG A 153 -1  O  TYR A 152   N  LEU A 133           
+SHEET    1 AA3 4 TRP A 143  GLU A 145  0                                        
+SHEET    2 AA3 4 GLN A 132  TRP A 138 -1  N  GLU A 137   O  GLU A 144           
+SHEET    3 AA3 4 LEU A 122  TYR A 126 -1  N  GLN A 125   O  HIS A 134           
+SHEET    4 AA3 4 PHE A 166  SER A 168 -1  O  TYR A 167   N  TYR A 124           
+SHEET    1 AA4 5 SER B  33  ALA B  35  0                                        
+SHEET    2 AA4 5 ARG B   4  SER B   8  1  N  VAL B   5   O  ALA B  35           
+SHEET    3 AA4 5 VAL B  67  ILE B  72  1  O  CYS B  69   N  PHE B   6           
+SHEET    4 AA4 5 LYS B  95  HIS B 100  1  O  LYS B  95   N  THR B  68           
+SHEET    5 AA4 5 ARG B 174  ASP B 177  1  O  TYR B 176   N  GLY B  98           
+SHEET    1 AA5 3 TRP B 143  GLU B 145  0                                        
+SHEET    2 AA5 3 GLN B 132  TRP B 138 -1  N  GLU B 137   O  GLU B 144           
+SHEET    3 AA5 3 TYR B 152  ARG B 153 -1  O  TYR B 152   N  LEU B 133           
+SHEET    1 AA6 4 TRP B 143  GLU B 145  0                                        
+SHEET    2 AA6 4 GLN B 132  TRP B 138 -1  N  GLU B 137   O  GLU B 144           
+SHEET    3 AA6 4 LEU B 122  TYR B 126 -1  N  GLY B 123   O  TYR B 136           
+SHEET    4 AA6 4 PHE B 166  SER B 168 -1  O  TYR B 167   N  TYR B 124           
+LINK         C   ILE A  86                 N   MSE A  87     1555   1555  1.33  
+LINK         C   MSE A  87                 N   LYS A  88     1555   1555  1.33  
+LINK         C   ILE B  86                 N   MSE B  87     1555   1555  1.33  
+LINK         C   MSE B  87                 N   LYS B  88     1555   1555  1.33  
+CRYST1   53.570   67.731   59.169  90.00  92.38  90.00 P 1 21 1      4          
+ORIGX1      1.000000  0.000000  0.000000        0.00000                         
+ORIGX2      0.000000  1.000000  0.000000        0.00000                         
+ORIGX3      0.000000  0.000000  1.000000        0.00000                         
+SCALE1      0.018667  0.000000  0.000775        0.00000                         
+SCALE2      0.000000  0.014764  0.000000        0.00000                         
+SCALE3      0.000000  0.000000  0.016915        0.00000                         
+ATOM      1  N   LYS A   3      41.391  27.682  41.031  1.00 55.07           N  
+ANISOU    1  N   LYS A   3     4729   6367   9827   -695   -572   -796       N  
+ATOM      2  CA  LYS A   3      40.863  26.500  40.355  1.00 52.59           C  
+ANISOU    2  CA  LYS A   3     4758   6477   8746   -455   -138   -790       C  
+ATOM      3  C   LYS A   3      40.023  26.859  39.128  1.00 50.50           C  
+ANISOU    3  C   LYS A   3     4498   6276   8415   -620     97   -342       C  
+ATOM      4  O   LYS A   3      39.474  27.959  39.034  1.00 55.38           O  
+ANISOU    4  O   LYS A   3     5031   6535   9476   -882    -63   -177       O  
+ATOM      5  CB  LYS A   3      40.033  25.654  41.326  1.00 50.30           C  
+ANISOU    5  CB  LYS A   3     5077   6023   8012   -141   -167  -1374       C  
+ATOM      6  CG  LYS A   3      40.858  24.915  42.373  1.00 52.16           C  
+ANISOU    6  CG  LYS A   3     5427   6330   8063    177   -265  -1849       C  
+ATOM      7  CD  LYS A   3      40.033  23.837  43.061  1.00 52.31           C  
+ANISOU    7  CD  LYS A   3     6071   6409   7394    417   -155  -1884       C  
+ATOM      8  CE  LYS A   3      40.919  22.814  43.756  1.00 54.09           C  
+ANISOU    8  CE  LYS A   3     6485   6848   7219    582   -125  -1799       C  
+ATOM      9  NZ  LYS A   3      40.135  21.631  44.213  1.00 53.68           N  
+ANISOU    9  NZ  LYS A   3     6762   6839   6793    632    -54  -1583       N  
+ATOM     10  N   ARG A   4      39.941  25.924  38.184  1.00 39.22           N  
+ANISOU   10  N   ARG A   4     3214   5295   6393   -410    442   -167       N  
+ATOM     11  CA  ARG A   4      39.153  26.116  36.971  1.00 38.44           C  
+ANISOU   11  CA  ARG A   4     3179   5280   6145   -450    659    205       C  
+ATOM     12  C   ARG A   4      37.821  25.382  37.115  1.00 32.71           C  
+ANISOU   12  C   ARG A   4     3036   4420   4973   -315    669   -143       C  
+ATOM     13  O   ARG A   4      37.792  24.187  37.423  1.00 30.28           O  
+ANISOU   13  O   ARG A   4     3082   4265   4158    -58    707   -448       O  
+ATOM     14  CB  ARG A   4      39.922  25.626  35.741  1.00 43.61           C  
+ANISOU   14  CB  ARG A   4     3625   6501   6444   -214    975    678       C  
+ATOM     15  CG  ARG A   4      39.342  26.110  34.425  1.00 46.24           C  
+ANISOU   15  CG  ARG A   4     3908   6903   6756   -211   1186   1149       C  
+ATOM     16  CD  ARG A   4      40.395  26.157  33.314  1.00 49.41           C  
+ANISOU   16  CD  ARG A   4     3954   7772   7046     10   1433   1740       C  
+ATOM     17  NE  ARG A   4      39.836  26.784  32.118  1.00 57.81           N  
+ANISOU   17  NE  ARG A   4     5100   8752   8113     60   1531   2077       N  
+ATOM     18  CZ  ARG A   4      39.210  26.122  31.148  1.00 58.46           C  
+ANISOU   18  CZ  ARG A   4     5551   9012   7651    453   1654   2122       C  
+ATOM     19  NH1 ARG A   4      38.724  26.777  30.101  1.00 60.26           N  
+ANISOU   19  NH1 ARG A   4     5802   9150   7944    532   1726   2400       N  
+ATOM     20  NH2 ARG A   4      39.071  24.803  31.222  1.00 56.47           N  
+ANISOU   20  NH2 ARG A   4     5705   8977   6774    803   1634   1834       N  
+ATOM     21  N   VAL A   5      36.720  26.095  36.888  1.00 29.33           N  
+ANISOU   21  N   VAL A   5     2698   3709   4736   -492    623    -73       N  
+ATOM     22  CA  VAL A   5      35.398  25.573  37.248  1.00 25.44           C  
+ANISOU   22  CA  VAL A   5     2660   3038   3967   -428    578   -379       C  
+ATOM     23  C   VAL A   5      34.538  25.277  36.029  1.00 25.78           C  
+ANISOU   23  C   VAL A   5     2878   3216   3701   -371    731   -166       C  
+ATOM     24  O   VAL A   5      34.408  26.125  35.150  1.00 28.56           O  
+ANISOU   24  O   VAL A   5     3030   3575   4247   -470    817    177       O  
+ATOM     25  CB  VAL A   5      34.640  26.575  38.157  1.00 22.31           C  
+ANISOU   25  CB  VAL A   5     2293   2211   3974   -590    347   -535       C  
+ATOM     26  CG1 VAL A   5      33.207  26.091  38.420  1.00 23.03           C  
+ANISOU   26  CG1 VAL A   5     2760   2197   3792   -515    353   -720       C  
+ATOM     27  CG2 VAL A   5      35.417  26.817  39.449  1.00 23.01           C  
+ANISOU   27  CG2 VAL A   5     2300   2096   4346   -540    104   -822       C  
+ATOM     28  N   PHE A   6      33.968  24.071  35.969  1.00 23.65           N  
+ANISOU   28  N   PHE A   6     2998   3026   2962   -193    737   -369       N  
+ATOM     29  CA  PHE A   6      33.022  23.727  34.910  1.00 22.64           C  
+ANISOU   29  CA  PHE A   6     3091   2944   2568   -119    769   -241       C  
+ATOM     30  C   PHE A   6      31.618  24.048  35.394  1.00 21.97           C  
+ANISOU   30  C   PHE A   6     3133   2564   2652   -309    658   -378       C  
+ATOM     31  O   PHE A   6      31.203  23.551  36.433  1.00 20.16           O  
+ANISOU   31  O   PHE A   6     3071   2193   2397   -328    569   -642       O  
+ATOM     32  CB  PHE A   6      33.120  22.246  34.516  1.00 21.41           C  
+ANISOU   32  CB  PHE A   6     3317   2978   1838    173    731   -361       C  
+ATOM     33  CG  PHE A   6      32.277  21.883  33.324  1.00 20.77           C  
+ANISOU   33  CG  PHE A   6     3482   2915   1495    316    670   -234       C  
+ATOM     34  CD1 PHE A   6      30.914  21.644  33.458  1.00 20.97           C  
+ANISOU   34  CD1 PHE A   6     3717   2684   1566    157    507   -376       C  
+ATOM     35  CD2 PHE A   6      32.842  21.780  32.065  1.00 25.00           C  
+ANISOU   35  CD2 PHE A   6     4028   3734   1739    665    758     50       C  
+ATOM     36  CE1 PHE A   6      30.130  21.321  32.359  1.00 20.66           C  
+ANISOU   36  CE1 PHE A   6     3898   2623   1330    296    379   -293       C  
+ATOM     37  CE2 PHE A   6      32.061  21.458  30.959  1.00 34.09           C  
+ANISOU   37  CE2 PHE A   6     5380   4823   2750    835    600    117       C  
+ATOM     38  CZ  PHE A   6      30.704  21.230  31.109  1.00 27.89           C  
+ANISOU   38  CZ  PHE A   6     4823   3759   2014    655    406    -72       C  
+ATOM     39  N   PHE A   7      30.891  24.882  34.655  1.00 19.73           N  
+ANISOU   39  N   PHE A   7     2763   2217   2515   -403    687   -175       N  
+ATOM     40  CA  PHE A   7      29.524  25.218  35.059  1.00 18.19           C  
+ANISOU   40  CA  PHE A   7     2664   1817   2432   -542    593   -264       C  
+ATOM     41  C   PHE A   7      28.525  24.406  34.267  1.00 21.84           C  
+ANISOU   41  C   PHE A   7     3365   2318   2615   -476    534   -264       C  
+ATOM     42  O   PHE A   7      28.634  24.298  33.047  1.00 20.59           O  
+ANISOU   42  O   PHE A   7     3256   2285   2281   -320    572   -111       O  
+ATOM     43  CB  PHE A   7      29.239  26.714  34.880  1.00 17.61           C  
+ANISOU   43  CB  PHE A   7     2390   1622   2680   -678    611    -88       C  
+ATOM     44  CG  PHE A   7      29.940  27.596  35.871  1.00 18.32           C  
+ANISOU   44  CG  PHE A   7     2301   1540   3120   -773    518   -132       C  
+ATOM     45  CD1 PHE A   7      29.484  27.704  37.175  1.00 22.88           C  
+ANISOU   45  CD1 PHE A   7     2985   1951   3759   -730    349   -352       C  
+ATOM     46  CD2 PHE A   7      31.030  28.363  35.487  1.00 22.80           C  
+ANISOU   46  CD2 PHE A   7     2590   2114   3959   -854    558     92       C  
+ATOM     47  CE1 PHE A   7      30.122  28.546  38.081  1.00 26.28           C  
+ANISOU   47  CE1 PHE A   7     3332   2260   4393   -686    146   -389       C  
+ATOM     48  CE2 PHE A   7      31.670  29.202  36.390  1.00 27.94           C  
+ANISOU   48  CE2 PHE A   7     3094   2554   4968   -948    355     43       C  
+ATOM     49  CZ  PHE A   7      31.216  29.294  37.683  1.00 30.60           C  
+ANISOU   49  CZ  PHE A   7     3633   2755   5240   -824    122   -230       C  
+ATOM     50  N   SER A   8      27.550  23.840  34.976  1.00 18.03           N  
+ANISOU   50  N   SER A   8     3022   1716   2111   -560    420   -410       N  
+ATOM     51  CA  SER A   8      26.537  22.971  34.397  1.00 19.99           C  
+ANISOU   51  CA  SER A   8     3473   1935   2185   -564    272   -417       C  
+ATOM     52  C   SER A   8      25.175  23.610  34.621  1.00 19.80           C  
+ANISOU   52  C   SER A   8     3336   1832   2355   -720    240   -344       C  
+ATOM     53  O   SER A   8      24.884  24.077  35.714  1.00 21.43           O  
+ANISOU   53  O   SER A   8     3414   2008   2719   -757    281   -351       O  
+ATOM     54  CB  SER A   8      26.610  21.585  35.036  1.00 23.61           C  
+ANISOU   54  CB  SER A   8     4082   2388   2501   -509    146   -528       C  
+ATOM     55  OG  SER A   8      25.702  20.684  34.439  1.00 22.45           O  
+ANISOU   55  OG  SER A   8     4078   2184   2267   -521    -68   -489       O  
+ATOM     56  N   PHE A   9      24.332  23.642  33.598  1.00 20.77           N  
+ANISOU   56  N   PHE A   9     3500   1964   2428   -718    145   -264       N  
+ATOM     57  CA  PHE A   9      23.113  24.435  33.699  1.00 19.78           C  
+ANISOU   57  CA  PHE A   9     3232   1834   2448   -824    145   -175       C  
+ATOM     58  C   PHE A   9      22.138  24.098  32.589  1.00 26.23           C  
+ANISOU   58  C   PHE A   9     4129   2646   3190   -808    -34   -145       C  
+ATOM     59  O   PHE A   9      22.521  23.512  31.569  1.00 21.88           O  
+ANISOU   59  O   PHE A   9     3771   2077   2464   -639   -153   -188       O  
+ATOM     60  CB  PHE A   9      23.454  25.937  33.661  1.00 15.72           C  
+ANISOU   60  CB  PHE A   9     2578   1354   2043   -785    315    -98       C  
+ATOM     61  CG  PHE A   9      24.419  26.300  32.565  1.00 16.59           C  
+ANISOU   61  CG  PHE A   9     2698   1514   2090   -649    422    -23       C  
+ATOM     62  CD1 PHE A   9      23.991  26.396  31.247  1.00 17.63           C  
+ANISOU   62  CD1 PHE A   9     2912   1698   2088   -497    415     44       C  
+ATOM     63  CD2 PHE A   9      25.762  26.470  32.845  1.00 18.54           C  
+ANISOU   63  CD2 PHE A   9     2862   1776   2408   -623    528      4       C  
+ATOM     64  CE1 PHE A   9      24.899  26.687  30.211  1.00 21.56           C  
+ANISOU   64  CE1 PHE A   9     3416   2281   2496   -268    563    185       C  
+ATOM     65  CE2 PHE A   9      26.672  26.781  31.827  1.00 20.88           C  
+ANISOU   65  CE2 PHE A   9     3098   2174   2659   -470    669    179       C  
+ATOM     66  CZ  PHE A   9      26.234  26.886  30.510  1.00 22.84           C  
+ANISOU   66  CZ  PHE A   9     3438   2493   2745   -267    710    291       C  
+ATOM     67  N   HIS A  10      20.873  24.448  32.812  1.00 20.35           N  
+ANISOU   67  N   HIS A  10     3247   1928   2556   -926    -82    -67       N  
+ATOM     68  CA  HIS A  10      19.873  24.494  31.760  1.00 18.94           C  
+ANISOU   68  CA  HIS A  10     3085   1762   2348   -894   -244    -49       C  
+ATOM     69  C   HIS A  10      20.109  25.733  30.896  1.00 25.13           C  
+ANISOU   69  C   HIS A  10     3881   2628   3039   -694    -65    -39       C  
+ATOM     70  O   HIS A  10      20.340  26.825  31.435  1.00 19.15           O  
+ANISOU   70  O   HIS A  10     3019   1927   2332   -707    142     21       O  
+ATOM     71  CB  HIS A  10      18.475  24.537  32.375  1.00 19.67           C  
+ANISOU   71  CB  HIS A  10     2960   1925   2588  -1075   -317     79       C  
+ATOM     72  CG  HIS A  10      17.361  24.500  31.379  1.00 21.46           C  
+ANISOU   72  CG  HIS A  10     3162   2169   2825  -1068   -537     82       C  
+ATOM     73  ND1 HIS A  10      16.066  24.824  31.715  1.00 25.44           N  
+ANISOU   73  ND1 HIS A  10     3413   2825   3430  -1180   -565    237       N  
+ATOM     74  CD2 HIS A  10      17.330  24.138  30.073  1.00 23.95           C  
+ANISOU   74  CD2 HIS A  10     3679   2374   3048   -908   -769    -50       C  
+ATOM     75  CE1 HIS A  10      15.283  24.663  30.662  1.00 24.32           C  
+ANISOU   75  CE1 HIS A  10     3289   2655   3297  -1147   -817    176       C  
+ATOM     76  NE2 HIS A  10      16.028  24.251  29.651  1.00 27.41           N  
+ANISOU   76  NE2 HIS A  10     3981   2862   3571   -959   -960    -17       N  
+ATOM     77  N   TYR A  11      20.032  25.581  29.573  1.00 21.15           N  
+ANISOU   77  N   TYR A  11     3538   2102   2396   -470   -171    -90       N  
+ATOM     78  CA  TYR A  11      20.259  26.722  28.664  1.00 22.50           C  
+ANISOU   78  CA  TYR A  11     3739   2346   2464   -224     41    -46       C  
+ATOM     79  C   TYR A  11      19.343  27.913  28.979  1.00 21.31           C  
+ANISOU   79  C   TYR A  11     3451   2286   2359   -310    157     -4       C  
+ATOM     80  O   TYR A  11      19.728  29.089  28.825  1.00 19.63           O  
+ANISOU   80  O   TYR A  11     3231   2102   2123   -225    387     70       O  
+ATOM     81  CB  TYR A  11      20.073  26.290  27.201  1.00 30.65           C  
+ANISOU   81  CB  TYR A  11     5003   3342   3301    141   -126   -121       C  
+ATOM     82  CG  TYR A  11      18.629  26.154  26.739  1.00 35.57           C  
+ANISOU   82  CG  TYR A  11     5643   3936   3936    147   -398   -233       C  
+ATOM     83  CD1 TYR A  11      17.932  27.241  26.211  1.00 35.74           C  
+ANISOU   83  CD1 TYR A  11     5632   4058   3888    289   -259   -244       C  
+ATOM     84  CD2 TYR A  11      17.974  24.932  26.806  1.00 37.84           C  
+ANISOU   84  CD2 TYR A  11     5981   4083   4314     12   -822   -321       C  
+ATOM     85  CE1 TYR A  11      16.620  27.114  25.788  1.00 40.94           C  
+ANISOU   85  CE1 TYR A  11     6277   4724   4555    312   -520   -357       C  
+ATOM     86  CE2 TYR A  11      16.670  24.794  26.381  1.00 40.73           C  
+ANISOU   86  CE2 TYR A  11     6302   4414   4761    -16  -1120   -397       C  
+ATOM     87  CZ  TYR A  11      15.994  25.883  25.872  1.00 45.58           C  
+ANISOU   87  CZ  TYR A  11     6854   5174   5291    145   -963   -424       C  
+ATOM     88  OH  TYR A  11      14.688  25.730  25.453  1.00 50.46           O  
+ANISOU   88  OH  TYR A  11     7397   5785   5988    129  -1277   -511       O  
+ATOM     89  N   GLN A  12      18.127  27.615  29.421  1.00 20.71           N  
+ANISOU   89  N   GLN A  12     3268   2262   2340   -466    -15    -17       N  
+ATOM     90  CA  GLN A  12      17.156  28.680  29.655  1.00 20.68           C  
+ANISOU   90  CA  GLN A  12     3163   2414   2281   -459     71     34       C  
+ATOM     91  C   GLN A  12      17.617  29.620  30.767  1.00 23.30           C  
+ANISOU   91  C   GLN A  12     3442   2775   2638   -512    258    125       C  
+ATOM     92  O   GLN A  12      17.273  30.810  30.772  1.00 21.29           O  
+ANISOU   92  O   GLN A  12     3231   2601   2259   -401    359    154       O  
+ATOM     93  CB  GLN A  12      15.783  28.103  29.993  1.00 23.02           C  
+ANISOU   93  CB  GLN A  12     3276   2821   2648   -605   -142     84       C  
+ATOM     94  CG  GLN A  12      14.676  29.149  30.086  1.00 26.45           C  
+ANISOU   94  CG  GLN A  12     3613   3500   2938   -512    -66    148       C  
+ATOM     95  CD  GLN A  12      14.363  29.796  28.742  1.00 29.77           C  
+ANISOU   95  CD  GLN A  12     4204   3944   3163   -249    -50     -5       C  
+ATOM     96  OE1 GLN A  12      14.056  29.108  27.766  1.00 26.25           O  
+ANISOU   96  OE1 GLN A  12     3820   3410   2745   -166   -267   -131       O  
+ATOM     97  NE2 GLN A  12      14.445  31.128  28.685  1.00 26.90           N  
+ANISOU   97  NE2 GLN A  12     3962   3669   2590    -70    176     -4       N  
+ATOM     98  N   ASP A  13      18.403  29.090  31.703  1.00 18.06           N  
+ANISOU   98  N   ASP A  13     2732   2020   2109   -639    261    146       N  
+ATOM     99  CA  ASP A  13      18.917  29.910  32.781  1.00 22.87           C  
+ANISOU   99  CA  ASP A  13     3332   2595   2763   -630    349    190       C  
+ATOM    100  C   ASP A  13      20.072  30.795  32.313  1.00 24.01           C  
+ANISOU  100  C   ASP A  13     3563   2601   2958   -582    466    191       C  
+ATOM    101  O   ASP A  13      20.404  31.785  32.969  1.00 18.78           O  
+ANISOU  101  O   ASP A  13     2935   1853   2347   -559    464    223       O  
+ATOM    102  CB  ASP A  13      19.322  29.026  33.956  1.00 19.77           C  
+ANISOU  102  CB  ASP A  13     2871   2148   2494   -721    304    187       C  
+ATOM    103  CG  ASP A  13      18.115  28.488  34.698  1.00 21.34           C  
+ANISOU  103  CG  ASP A  13     2931   2499   2679   -743    238    306       C  
+ATOM    104  OD1 ASP A  13      17.188  29.297  34.933  1.00 21.65           O  
+ANISOU  104  OD1 ASP A  13     2923   2710   2592   -614    253    413       O  
+ATOM    105  OD2 ASP A  13      18.071  27.272  35.015  1.00 19.52           O  
+ANISOU  105  OD2 ASP A  13     2637   2231   2550   -872    173    328       O  
+ATOM    106  N   VAL A  14      20.674  30.465  31.173  1.00 17.44           N  
+ANISOU  106  N   VAL A  14     2771   1740   2115   -529    540    191       N  
+ATOM    107  CA  VAL A  14      21.610  31.409  30.556  1.00 18.28           C  
+ANISOU  107  CA  VAL A  14     2898   1764   2284   -462    703    302       C  
+ATOM    108  C   VAL A  14      20.836  32.570  29.935  1.00 20.34           C  
+ANISOU  108  C   VAL A  14     3265   2057   2407   -333    773    334       C  
+ATOM    109  O   VAL A  14      21.143  33.750  30.174  1.00 19.39           O  
+ANISOU  109  O   VAL A  14     3184   1824   2359   -358    811    422       O  
+ATOM    110  CB  VAL A  14      22.499  30.748  29.469  1.00 23.11           C  
+ANISOU  110  CB  VAL A  14     3517   2401   2863   -316    812    372       C  
+ATOM    111  CG1 VAL A  14      23.334  31.817  28.713  1.00 27.77           C  
+ANISOU  111  CG1 VAL A  14     4066   2950   3535   -213   1043    600       C  
+ATOM    112  CG2 VAL A  14      23.415  29.726  30.083  1.00 23.09           C  
+ANISOU  112  CG2 VAL A  14     3449   2384   2938   -407    755    340       C  
+ATOM    113  N   ILE A  15      19.847  32.219  29.116  1.00 23.01           N  
+ANISOU  113  N   ILE A  15     3674   2523   2545   -181    750    250       N  
+ATOM    114  CA  ILE A  15      18.979  33.190  28.450  1.00 23.81           C  
+ANISOU  114  CA  ILE A  15     3906   2699   2443      2    818    229       C  
+ATOM    115  C   ILE A  15      18.350  34.184  29.428  1.00 23.33           C  
+ANISOU  115  C   ILE A  15     3888   2674   2301    -51    753    236       C  
+ATOM    116  O   ILE A  15      18.223  35.365  29.120  1.00 20.88           O  
+ANISOU  116  O   ILE A  15     3740   2330   1862     69    832    268       O  
+ATOM    117  CB  ILE A  15      17.856  32.455  27.667  1.00 21.21           C  
+ANISOU  117  CB  ILE A  15     3611   2507   1941    158    699     84       C  
+ATOM    118  CG1 ILE A  15      18.470  31.690  26.485  1.00 26.00           C  
+ANISOU  118  CG1 ILE A  15     4305   3048   2527    388    719     64       C  
+ATOM    119  CG2 ILE A  15      16.770  33.427  27.205  1.00 22.43           C  
+ANISOU  119  CG2 ILE A  15     3886   2796   1843    353    743     16       C  
+ATOM    120  CD1 ILE A  15      17.476  30.924  25.632  1.00 32.65           C  
+ANISOU  120  CD1 ILE A  15     5238   3933   3235    595    490   -116       C  
+ATOM    121  N   ASP A  16      17.998  33.707  30.618  1.00 19.20           N  
+ANISOU  121  N   ASP A  16     3258   2214   1824   -172    604    226       N  
+ATOM    122  CA  ASP A  16      17.283  34.534  31.601  1.00 18.16           C  
+ANISOU  122  CA  ASP A  16     3198   2177   1525    -82    510    256       C  
+ATOM    123  C   ASP A  16      18.197  35.365  32.487  1.00 18.41           C  
+ANISOU  123  C   ASP A  16     3341   1971   1682   -100    426    300       C  
+ATOM    124  O   ASP A  16      17.722  36.051  33.403  1.00 24.39           O  
+ANISOU  124  O   ASP A  16     4232   2767   2269     68    280    318       O  
+ATOM    125  CB  ASP A  16      16.405  33.652  32.490  1.00 17.96           C  
+ANISOU  125  CB  ASP A  16     2989   2364   1471   -104    408    298       C  
+ATOM    126  CG  ASP A  16      15.242  33.043  31.740  1.00 24.11           C  
+ANISOU  126  CG  ASP A  16     3643   3373   2147    -94    389    283       C  
+ATOM    127  OD1 ASP A  16      15.079  33.332  30.533  1.00 25.81           O  
+ANISOU  127  OD1 ASP A  16     3964   3584   2258     -1    443    183       O  
+ATOM    128  OD2 ASP A  16      14.487  32.282  32.373  1.00 21.35           O  
+ANISOU  128  OD2 ASP A  16     3078   3195   1839   -160    307    391       O  
+ATOM    129  N   PHE A  17      19.502  35.314  32.201  1.00 19.52           N  
+ANISOU  129  N   PHE A  17     3433   1872   2112   -258    482    333       N  
+ATOM    130  CA  PHE A  17      20.536  35.958  33.013  1.00 19.59           C  
+ANISOU  130  CA  PHE A  17     3483   1597   2362   -338    336    373       C  
+ATOM    131  C   PHE A  17      20.488  35.521  34.480  1.00 22.72           C  
+ANISOU  131  C   PHE A  17     3861   1985   2786   -278    140    301       C  
+ATOM    132  O   PHE A  17      20.551  36.348  35.400  1.00 19.82           O  
+ANISOU  132  O   PHE A  17     3674   1459   2400   -130   -100    283       O  
+ATOM    133  CB  PHE A  17      20.457  37.488  32.937  1.00 22.35           C  
+ANISOU  133  CB  PHE A  17     4091   1770   2631   -245    223    427       C  
+ATOM    134  CG  PHE A  17      21.802  38.148  33.066  1.00 25.92           C  
+ANISOU  134  CG  PHE A  17     4521   1847   3481   -436    108    539       C  
+ATOM    135  CD1 PHE A  17      22.585  38.372  31.945  1.00 24.48           C  
+ANISOU  135  CD1 PHE A  17     4212   1574   3517   -584    333    728       C  
+ATOM    136  CD2 PHE A  17      22.318  38.476  34.311  1.00 26.51           C  
+ANISOU  136  CD2 PHE A  17     4668   1664   3741   -437   -237    483       C  
+ATOM    137  CE1 PHE A  17      23.836  38.939  32.056  1.00 26.99           C  
+ANISOU  137  CE1 PHE A  17     4360   1617   4279   -775    233    894       C  
+ATOM    138  CE2 PHE A  17      23.570  39.059  34.429  1.00 31.11           C  
+ANISOU  138  CE2 PHE A  17     5077   2016   4726   -601   -344    549       C  
+ATOM    139  CZ  PHE A  17      24.331  39.292  33.297  1.00 32.68           C  
+ANISOU  139  CZ  PHE A  17     5098   2183   5137   -789    -77    745       C  
+ATOM    140  N   ARG A  18      20.401  34.211  34.688  1.00 19.96           N  
+ANISOU  140  N   ARG A  18     3334   1781   2471   -343    218    261       N  
+ATOM    141  CA  ARG A  18      20.595  33.657  36.018  1.00 20.06           C  
+ANISOU  141  CA  ARG A  18     3312   1759   2551   -270     98    208       C  
+ATOM    142  C   ARG A  18      21.991  33.063  36.114  1.00 20.87           C  
+ANISOU  142  C   ARG A  18     3302   1675   2951   -449    112    144       C  
+ATOM    143  O   ARG A  18      22.702  33.299  37.082  1.00 21.51           O  
+ANISOU  143  O   ARG A  18     3425   1561   3186   -384    -56     72       O  
+ATOM    144  CB  ARG A  18      19.539  32.589  36.340  1.00 18.26           C  
+ANISOU  144  CB  ARG A  18     2961   1806   2171   -217    170    250       C  
+ATOM    145  CG  ARG A  18      18.109  33.130  36.368  1.00 20.69           C  
+ANISOU  145  CG  ARG A  18     3308   2380   2173     -6    160    363       C  
+ATOM    146  CD  ARG A  18      17.117  32.115  36.957  1.00 20.54           C  
+ANISOU  146  CD  ARG A  18     3085   2630   2090     44    210    505       C  
+ATOM    147  NE  ARG A  18      15.846  32.777  37.222  1.00 19.27           N  
+ANISOU  147  NE  ARG A  18     2934   2775   1612    330    195    671       N  
+ATOM    148  CZ  ARG A  18      15.605  33.541  38.287  1.00 19.79           C  
+ANISOU  148  CZ  ARG A  18     3162   2913   1443    744     98    757       C  
+ATOM    149  NH1 ARG A  18      16.526  33.711  39.233  1.00 19.32           N  
+ANISOU  149  NH1 ARG A  18     3267   2594   1480    912    -27    662       N  
+ATOM    150  NH2 ARG A  18      14.424  34.122  38.409  1.00 20.61           N  
+ANISOU  150  NH2 ARG A  18     3179   3259   1394    915     91    796       N  
+ATOM    151  N   VAL A  19      22.388  32.302  35.094  1.00 17.55           N  
+ANISOU  151  N   VAL A  19     2609   1816   2245    -55    -32    218       N  
+ATOM    152  CA  VAL A  19      23.722  31.702  35.102  1.00 17.36           C  
+ANISOU  152  CA  VAL A  19     2538   1820   2237   -130     58     60       C  
+ATOM    153  C   VAL A  19      24.818  32.761  35.161  1.00 22.40           C  
+ANISOU  153  C   VAL A  19     3275   2461   2774   -209    151     68       C  
+ATOM    154  O   VAL A  19      25.791  32.620  35.912  1.00 20.36           O  
+ANISOU  154  O   VAL A  19     2956   2182   2599   -217    210      2       O  
+ATOM    155  CB  VAL A  19      23.928  30.800  33.879  1.00 18.58           C  
+ANISOU  155  CB  VAL A  19     2656   2067   2336   -200     37   -117       C  
+ATOM    156  CG1 VAL A  19      25.402  30.508  33.653  1.00 20.71           C  
+ANISOU  156  CG1 VAL A  19     2876   2414   2579   -263    165   -300       C  
+ATOM    157  CG2 VAL A  19      23.153  29.511  34.073  1.00 18.70           C  
+ANISOU  157  CG2 VAL A  19     2530   2000   2575   -142    -89   -166       C  
+ATOM    158  N   ASN A  20      24.649  33.843  34.407  1.00 23.55           N  
+ANISOU  158  N   ASN A  20     3562   2617   2771   -278    133    181       N  
+ATOM    159  CA  ASN A  20      25.710  34.853  34.365  1.00 23.95           C  
+ANISOU  159  CA  ASN A  20     3686   2642   2772   -402    196    231       C  
+ATOM    160  C   ASN A  20      25.972  35.533  35.696  1.00 24.71           C  
+ANISOU  160  C   ASN A  20     3804   2570   3014   -332    168    235       C  
+ATOM    161  O   ASN A  20      27.065  36.058  35.900  1.00 20.68           O  
+ANISOU  161  O   ASN A  20     3297   2024   2536   -444    204    221       O  
+ATOM    162  CB  ASN A  20      25.414  35.906  33.310  1.00 23.03           C  
+ANISOU  162  CB  ASN A  20     3715   2535   2501   -511    144    425       C  
+ATOM    163  CG  ASN A  20      25.866  35.474  31.925  1.00 28.82           C  
+ANISOU  163  CG  ASN A  20     4430   3533   2987   -658    228    405       C  
+ATOM    164  OD1 ASN A  20      25.852  34.290  31.604  1.00 27.34           O  
+ANISOU  164  OD1 ASN A  20     4142   3489   2756   -613    268    203       O  
+ATOM    165  ND2 ASN A  20      26.280  36.432  31.107  1.00 27.91           N  
+ANISOU  165  ND2 ASN A  20     4405   3490   2709   -834    247    613       N  
+ATOM    166  N   VAL A  21      24.999  35.529  36.605  1.00 18.91           N  
+ANISOU  166  N   VAL A  21     3066   1765   2355   -152    102    242       N  
+ATOM    167  CA  VAL A  21      25.217  36.161  37.909  1.00 17.87           C  
+ANISOU  167  CA  VAL A  21     2961   1531   2299    -54     72    188       C  
+ATOM    168  C   VAL A  21      26.364  35.461  38.661  1.00 26.63           C  
+ANISOU  168  C   VAL A  21     3961   2706   3452    -97    125     77       C  
+ATOM    169  O   VAL A  21      27.260  36.117  39.202  1.00 23.09           O  
+ANISOU  169  O   VAL A  21     3547   2185   3043   -150     96     16       O  
+ATOM    170  CB  VAL A  21      23.936  36.166  38.771  1.00 21.73           C  
+ANISOU  170  CB  VAL A  21     3421   2031   2804    172     36    198       C  
+ATOM    171  CG1 VAL A  21      24.266  36.462  40.235  1.00 27.56           C  
+ANISOU  171  CG1 VAL A  21     4154   2777   3539    292     32     81       C  
+ATOM    172  CG2 VAL A  21      22.938  37.177  38.230  1.00 21.15           C  
+ANISOU  172  CG2 VAL A  21     3450   1840   2748    250    -55    284       C  
+ATOM    173  N   VAL A  22      26.339  34.133  38.665  1.00 23.08           N  
+ANISOU  173  N   VAL A  22     3371   2365   3034    -79    168     54       N  
+ATOM    174  CA  VAL A  22      27.388  33.334  39.285  1.00 16.13           C  
+ANISOU  174  CA  VAL A  22     2362   1529   2239   -104    187    -25       C  
+ATOM    175  C   VAL A  22      28.648  33.325  38.421  1.00 16.85           C  
+ANISOU  175  C   VAL A  22     2403   1648   2351   -266    256   -108       C  
+ATOM    176  O   VAL A  22      29.759  33.543  38.908  1.00 20.74           O  
+ANISOU  176  O   VAL A  22     2837   2134   2908   -327    253   -163       O  
+ATOM    177  CB  VAL A  22      26.906  31.885  39.529  1.00 15.63           C  
+ANISOU  177  CB  VAL A  22     2150   1511   2275    -31    170      5       C  
+ATOM    178  CG1 VAL A  22      28.013  31.026  40.157  1.00 17.81           C  
+ANISOU  178  CG1 VAL A  22     2282   1795   2690    -43    148    -48       C  
+ATOM    179  CG2 VAL A  22      25.668  31.892  40.414  1.00 20.22           C  
+ANISOU  179  CG2 VAL A  22     2729   2132   2821    105    137    138       C  
+ATOM    180  N   ARG A  23      28.475  33.099  37.125  1.00 18.05           N  
+ANISOU  180  N   ARG A  23     2560   1871   2429   -336    318   -121       N  
+ATOM    181  CA  ARG A  23      29.634  32.988  36.244  1.00 19.74           C  
+ANISOU  181  CA  ARG A  23     2684   2205   2611   -473    431   -212       C  
+ATOM    182  C   ARG A  23      30.434  34.289  36.182  1.00 20.65           C  
+ANISOU  182  C   ARG A  23     2856   2296   2693   -634    457   -117       C  
+ATOM    183  O   ARG A  23      31.671  34.272  36.209  1.00 25.04           O  
+ANISOU  183  O   ARG A  23     3272   2922   3322   -736    527   -176       O  
+ATOM    184  CB  ARG A  23      29.189  32.580  34.851  1.00 21.49           C  
+ANISOU  184  CB  ARG A  23     2922   2570   2674   -505    488   -257       C  
+ATOM    185  CG  ARG A  23      30.335  32.417  33.863  1.00 29.48           C  
+ANISOU  185  CG  ARG A  23     3815   3803   3583   -624    650   -377       C  
+ATOM    186  CD  ARG A  23      29.918  31.443  32.782  1.00 38.26           C  
+ANISOU  186  CD  ARG A  23     4892   5074   4570   -568    677   -562       C  
+ATOM    187  NE  ARG A  23      28.817  31.974  31.981  1.00 40.58           N  
+ANISOU  187  NE  ARG A  23     5367   5417   4633   -607    612   -420       N  
+ATOM    188  CZ  ARG A  23      28.070  31.237  31.162  1.00 44.13           C  
+ANISOU  188  CZ  ARG A  23     5836   5959   4972   -548    549   -556       C  
+ATOM    189  NH1 ARG A  23      28.297  29.929  31.052  1.00 38.95           N  
+ANISOU  189  NH1 ARG A  23     5038   5316   4447   -442    539   -861       N  
+ATOM    190  NH2 ARG A  23      27.090  31.803  30.463  1.00 43.54           N  
+ANISOU  190  NH2 ARG A  23     5917   5937   4687   -589    458   -395       N  
+ATOM    191  N   ASN A  24      29.738  35.424  36.127  1.00 22.30           N  
+ANISOU  191  N   ASN A  24     3247   2383   2843   -659    379     37       N  
+ATOM    192  CA  ASN A  24      30.438  36.707  36.073  1.00 21.81           C  
+ANISOU  192  CA  ASN A  24     3245   2221   2823   -833    350    155       C  
+ATOM    193  C   ASN A  24      31.163  37.010  37.385  1.00 25.42           C  
+ANISOU  193  C   ASN A  24     3658   2541   3457   -813    256     61       C  
+ATOM    194  O   ASN A  24      32.223  37.636  37.381  1.00 24.24           O  
+ANISOU  194  O   ASN A  24     3448   2355   3408   -994    248     95       O  
+ATOM    195  CB  ASN A  24      29.482  37.855  35.718  1.00 22.66           C  
+ANISOU  195  CB  ASN A  24     3559   2158   2894   -840    235    341       C  
+ATOM    196  CG  ASN A  24      28.958  37.768  34.280  1.00 29.14           C  
+ANISOU  196  CG  ASN A  24     4426   3142   3503   -919    294    489       C  
+ATOM    197  OD1 ASN A  24      29.428  36.959  33.476  1.00 28.91           O  
+ANISOU  197  OD1 ASN A  24     4282   3379   3323   -989    443    425       O  
+ATOM    198  ND2 ASN A  24      27.992  38.618  33.951  1.00 25.15           N  
+ANISOU  198  ND2 ASN A  24     4084   2488   2982   -892    162    668       N  
+ATOM    199  N   HIS A  25      30.604  36.554  38.501  1.00 26.02           N  
+ANISOU  199  N   HIS A  25     3751   2575   3562   -609    178    -44       N  
+ATOM    200  CA  HIS A  25      31.256  36.726  39.798  1.00 26.29           C  
+ANISOU  200  CA  HIS A  25     3748   2545   3696   -570     69   -153       C  
+ATOM    201  C   HIS A  25      32.633  36.053  39.789  1.00 21.02           C  
+ANISOU  201  C   HIS A  25     2859   1994   3132   -682    125   -215       C  
+ATOM    202  O   HIS A  25      33.635  36.644  40.197  1.00 23.87           O  
+ANISOU  202  O   HIS A  25     3163   2294   3611   -805     46   -246       O  
+ATOM    203  CB  HIS A  25      30.386  36.156  40.927  1.00 20.51           C  
+ANISOU  203  CB  HIS A  25     3039   1855   2897   -333     13   -212       C  
+ATOM    204  CG  HIS A  25      31.042  36.215  42.273  1.00 25.92           C  
+ANISOU  204  CG  HIS A  25     3689   2553   3606   -282   -109   -322       C  
+ATOM    205  ND1 HIS A  25      31.059  37.361  43.041  1.00 31.50           N  
+ANISOU  205  ND1 HIS A  25     4529   3134   4305   -246   -256   -430       N  
+ATOM    206  CD2 HIS A  25      31.728  35.281  42.975  1.00 26.46           C  
+ANISOU  206  CD2 HIS A  25     3604   2741   3709   -257   -138   -349       C  
+ATOM    207  CE1 HIS A  25      31.708  37.122  44.167  1.00 30.07           C  
+ANISOU  207  CE1 HIS A  25     4287   3036   4102   -205   -365   -533       C  
+ATOM    208  NE2 HIS A  25      32.132  35.871  44.149  1.00 26.37           N  
+ANISOU  208  NE2 HIS A  25     3641   2719   3660   -217   -299   -455       N  
+ATOM    209  N   TRP A  26      32.673  34.819  39.295  1.00 21.37           N  
+ANISOU  209  N   TRP A  26     2763   2189   3168   -634    240   -249       N  
+ATOM    210  CA  TRP A  26      33.906  34.047  39.247  1.00 21.43           C  
+ANISOU  210  CA  TRP A  26     2524   2307   3311   -682    295   -342       C  
+ATOM    211  C   TRP A  26      34.873  34.588  38.195  1.00 23.14           C  
+ANISOU  211  C   TRP A  26     2629   2629   3536   -902    434   -314       C  
+ATOM    212  O   TRP A  26      36.052  34.794  38.485  1.00 24.70           O  
+ANISOU  212  O   TRP A  26     2650   2852   3881  -1013    418   -341       O  
+ATOM    213  CB  TRP A  26      33.579  32.574  38.974  1.00 20.27           C  
+ANISOU  213  CB  TRP A  26     2263   2238   3201   -539    349   -423       C  
+ATOM    214  CG  TRP A  26      34.733  31.616  38.996  1.00 22.42           C  
+ANISOU  214  CG  TRP A  26     2262   2584   3670   -517    375   -554       C  
+ATOM    215  CD1 TRP A  26      35.168  30.831  37.964  1.00 22.67           C  
+ANISOU  215  CD1 TRP A  26     2123   2743   3747   -503    517   -706       C  
+ATOM    216  CD2 TRP A  26      35.574  31.303  40.118  1.00 27.20           C  
+ANISOU  216  CD2 TRP A  26     2722   3151   4463   -474    235   -570       C  
+ATOM    217  NE1 TRP A  26      36.230  30.052  38.372  1.00 23.97           N  
+ANISOU  217  NE1 TRP A  26     2025   2919   4162   -437    480   -824       N  
+ATOM    218  CE2 TRP A  26      36.498  30.326  39.689  1.00 26.20           C  
+ANISOU  218  CE2 TRP A  26     2319   3097   4540   -430    295   -716       C  
+ATOM    219  CE3 TRP A  26      35.645  31.769  41.437  1.00 27.90           C  
+ANISOU  219  CE3 TRP A  26     2881   3171   4549   -457     51   -496       C  
+ATOM    220  CZ2 TRP A  26      37.483  29.808  40.531  1.00 30.25           C  
+ANISOU  220  CZ2 TRP A  26     2613   3584   5295   -375    160   -746       C  
+ATOM    221  CZ3 TRP A  26      36.612  31.245  42.274  1.00 26.97           C  
+ANISOU  221  CZ3 TRP A  26     2569   3063   4615   -420    -88   -521       C  
+ATOM    222  CH2 TRP A  26      37.526  30.285  41.816  1.00 30.73           C  
+ANISOU  222  CH2 TRP A  26     2760   3583   5334   -385    -41   -624       C  
+ATOM    223  N   VAL A  27      34.375  34.834  36.984  1.00 23.60           N  
+ANISOU  223  N   VAL A  27     2768   2776   3421   -975    562   -234       N  
+ATOM    224  CA  VAL A  27      35.252  35.152  35.847  1.00 26.94           C  
+ANISOU  224  CA  VAL A  27     3050   3410   3777  -1184    746   -175       C  
+ATOM    225  C   VAL A  27      35.589  36.648  35.737  1.00 32.10           C  
+ANISOU  225  C   VAL A  27     3783   3950   4462  -1434    691     59       C  
+ATOM    226  O   VAL A  27      36.705  37.021  35.352  1.00 30.66           O  
+ANISOU  226  O   VAL A  27     3404   3898   4348  -1650    791    140       O  
+ATOM    227  CB  VAL A  27      34.614  34.670  34.512  1.00 26.60           C  
+ANISOU  227  CB  VAL A  27     3049   3585   3472  -1160    902   -190       C  
+ATOM    228  CG1 VAL A  27      35.471  35.038  33.331  1.00 30.16           C  
+ANISOU  228  CG1 VAL A  27     3352   4343   3764  -1376   1121   -102       C  
+ATOM    229  CG2 VAL A  27      34.396  33.152  34.545  1.00 25.53           C  
+ANISOU  229  CG2 VAL A  27     2805   3513   3382   -933    922   -455       C  
+ATOM    230  N   THR A  28      34.638  37.511  36.066  1.00 29.35           N  
+ANISOU  230  N   THR A  28     4496   2847   3809  -1162    671    482       N  
+ATOM    231  CA  THR A  28      34.895  38.945  35.955  1.00 31.33           C  
+ANISOU  231  CA  THR A  28     4953   2921   4030  -1336    586    673       C  
+ATOM    232  C   THR A  28      35.334  39.543  37.288  1.00 32.23           C  
+ANISOU  232  C   THR A  28     5032   2813   4399  -1283    378    657       C  
+ATOM    233  O   THR A  28      36.429  40.103  37.392  1.00 32.93           O  
+ANISOU  233  O   THR A  28     5036   2827   4647  -1510    413    684       O  
+ATOM    234  CB  THR A  28      33.658  39.706  35.438  1.00 33.69           C  
+ANISOU  234  CB  THR A  28     5605   3137   4058  -1252    427    840       C  
+ATOM    235  OG1 THR A  28      33.280  39.187  34.155  1.00 38.63           O  
+ANISOU  235  OG1 THR A  28     6289   3964   4424  -1315    593    856       O  
+ATOM    236  CG2 THR A  28      33.956  41.195  35.312  1.00 34.78           C  
+ANISOU  236  CG2 THR A  28     6021   3031   4164  -1433    305   1045       C  
+ATOM    237  N   LYS A  29      34.477  39.422  38.301  1.00 28.62           N  
+ANISOU  237  N   LYS A  29     4637   2269   3970   -998    166    604       N  
+ATOM    238  CA  LYS A  29      34.743  40.042  39.595  1.00 36.21           C  
+ANISOU  238  CA  LYS A  29     5631   3012   5115   -911    -60    582       C  
+ATOM    239  C   LYS A  29      35.999  39.459  40.236  1.00 33.53           C  
+ANISOU  239  C   LYS A  29     4995   2694   5051   -985    -14    440       C  
+ATOM    240  O   LYS A  29      36.819  40.192  40.794  1.00 38.31           O  
+ANISOU  240  O   LYS A  29     5586   3137   5833  -1102   -133    450       O  
+ATOM    241  CB  LYS A  29      33.542  39.879  40.528  1.00 31.90           C  
+ANISOU  241  CB  LYS A  29     5185   2434   4500   -583   -242    528       C  
+ATOM    242  N   LEU A  30      36.161  38.145  40.136  1.00 28.26           N  
+ANISOU  242  N   LEU A  30     4099   2214   4427   -913    130    299       N  
+ATOM    243  CA  LEU A  30      37.309  37.482  40.747  1.00 30.42           C  
+ANISOU  243  CA  LEU A  30     4084   2509   4966   -919    135    139       C  
+ATOM    244  C   LEU A  30      38.389  37.127  39.728  1.00 30.72           C  
+ANISOU  244  C   LEU A  30     3853   2737   5083  -1140    401     73       C  
+ATOM    245  O   LEU A  30      39.448  36.616  40.094  1.00 31.83           O  
+ANISOU  245  O   LEU A  30     3701   2927   5467  -1144    415    -83       O  
+ATOM    246  CB  LEU A  30      36.857  36.231  41.492  1.00 27.57           C  
+ANISOU  246  CB  LEU A  30     3670   2180   4624   -659     69      6       C  
+ATOM    247  CG  LEU A  30      35.902  36.501  42.656  1.00 28.67           C  
+ANISOU  247  CG  LEU A  30     4029   2177   4688   -450   -160     44       C  
+ATOM    248  CD1 LEU A  30      35.619  35.217  43.439  1.00 25.83           C  
+ANISOU  248  CD1 LEU A  30     3625   1842   4345   -260   -211    -68       C  
+ATOM    249  CD2 LEU A  30      36.449  37.581  43.565  1.00 34.04           C  
+ANISOU  249  CD2 LEU A  30     4781   2650   5501   -471   -376     68       C  
+ATOM    250  N   ASN A  31      38.104  37.406  38.458  1.00 31.81           N  
+ANISOU  250  N   ASN A  31     4092   2994   5001  -1307    605    181       N  
+ATOM    251  CA  ASN A  31      39.059  37.231  37.359  1.00 34.96           C  
+ANISOU  251  CA  ASN A  31     4274   3609   5401  -1554    908    137       C  
+ATOM    252  C   ASN A  31      39.624  35.807  37.277  1.00 34.88           C  
+ANISOU  252  C   ASN A  31     3942   3793   5518  -1412   1051   -118       C  
+ATOM    253  O   ASN A  31      40.804  35.607  36.997  1.00 39.74           O  
+ANISOU  253  O   ASN A  31     4232   4563   6302  -1539   1222   -249       O  
+ATOM    254  CB  ASN A  31      40.200  38.259  37.469  1.00 38.46           C  
+ANISOU  254  CB  ASN A  31     4593   3993   6028  -1857    921    201       C  
+ATOM    255  CG  ASN A  31      40.942  38.448  36.158  1.00 48.04           C  
+ANISOU  255  CG  ASN A  31     5678   5439   7137  -2196   1273    239       C  
+ATOM    256  OD1 ASN A  31      40.387  38.240  35.078  1.00 50.32           O  
+ANISOU  256  OD1 ASN A  31     6127   5864   7128  -2233   1462    303       O  
+ATOM    257  ND2 ASN A  31      42.207  38.835  36.248  1.00 56.05           N  
+ANISOU  257  ND2 ASN A  31     6393   6521   8384  -2456   1365    193       N  
+ATOM    258  N   GLN A  32      38.760  34.824  37.510  1.00 31.61           N  
+ANISOU  258  N   GLN A  32     3618   3369   5023  -1152    972   -196       N  
+ATOM    259  CA  GLN A  32      39.130  33.416  37.379  1.00 33.86           C  
+ANISOU  259  CA  GLN A  32     3688   3782   5395   -990   1066   -434       C  
+ATOM    260  C   GLN A  32      38.657  32.859  36.043  1.00 36.68           C  
+ANISOU  260  C   GLN A  32     4123   4330   5482  -1028   1303   -465       C  
+ATOM    261  O   GLN A  32      38.208  33.608  35.182  1.00 42.86           O  
+ANISOU  261  O   GLN A  32     5095   5171   6018  -1205   1410   -298       O  
+ATOM    262  CB  GLN A  32      38.547  32.605  38.531  1.00 30.07           C  
+ANISOU  262  CB  GLN A  32     3290   3136   4999   -715    812   -499       C  
+ATOM    263  CG  GLN A  32      39.051  33.052  39.879  1.00 32.20           C  
+ANISOU  263  CG  GLN A  32     3508   3223   5506   -651    562   -494       C  
+ATOM    264  CD  GLN A  32      40.557  33.032  39.928  1.00 39.55           C  
+ANISOU  264  CD  GLN A  32     4079   4228   6721   -717    612   -650       C  
+ATOM    265  OE1 GLN A  32      41.182  32.042  39.554  1.00 42.33           O  
+ANISOU  265  OE1 GLN A  32     4198   4709   7175   -622    723   -857       O  
+ATOM    266  NE2 GLN A  32      41.155  34.141  40.353  1.00 44.84           N  
+ANISOU  266  NE2 GLN A  32     4687   4823   7527   -881    523   -570       N  
+ATOM    267  N   SER A  33      38.759  31.548  35.860  1.00 35.20           N  
+ANISOU  267  N   SER A  33     3826   4220   5327   -856   1359   -682       N  
+ATOM    268  CA  SER A  33      38.409  30.976  34.567  1.00 39.33           C  
+ANISOU  268  CA  SER A  33     4424   4928   5592   -887   1578   -751       C  
+ATOM    269  C   SER A  33      37.361  29.878  34.684  1.00 38.22           C  
+ANISOU  269  C   SER A  33     4463   4705   5355   -691   1440   -821       C  
+ATOM    270  O   SER A  33      37.328  29.120  35.662  1.00 34.50           O  
+ANISOU  270  O   SER A  33     3962   4078   5068   -505   1249   -913       O  
+ATOM    271  CB  SER A  33      39.654  30.435  33.862  1.00 50.36           C  
+ANISOU  271  CB  SER A  33     5507   6551   7077   -909   1849   -994       C  
+ATOM    272  OG  SER A  33      40.172  29.302  34.530  1.00 59.93           O  
+ANISOU  272  OG  SER A  33     6526   7697   8548   -647   1735  -1246       O  
+ATOM    273  N   ALA A  34      36.510  29.804  33.665  1.00 31.51           N  
+ANISOU  273  N   ALA A  34     3815   3956   4202   -757   1528   -770       N  
+ATOM    274  CA  ALA A  34      35.405  28.863  33.656  1.00 32.01           C  
+ANISOU  274  CA  ALA A  34     4054   3957   4151   -636   1395   -817       C  
+ATOM    275  C   ALA A  34      35.360  28.073  32.354  1.00 33.08           C  
+ANISOU  275  C   ALA A  34     4241   4259   4071   -647   1574   -985       C  
+ATOM    276  O   ALA A  34      35.971  28.456  31.354  1.00 34.81           O  
+ANISOU  276  O   ALA A  34     4411   4670   4147   -770   1820  -1013       O  
+ATOM    277  CB  ALA A  34      34.089  29.595  33.877  1.00 30.92           C  
+ANISOU  277  CB  ALA A  34     4140   3756   3854   -678   1228   -583       C  
+ATOM    278  N   ALA A  35      34.651  26.951  32.391  1.00 31.28           N  
+ANISOU  278  N   ALA A  35     4124   3951   3811   -533   1449  -1101       N  
+ATOM    279  CA  ALA A  35      34.354  26.162  31.202  1.00 33.07           C  
+ANISOU  279  CA  ALA A  35     4466   4294   3803   -534   1551  -1263       C  
+ATOM    280  C   ALA A  35      32.850  25.886  31.205  1.00 33.37           C  
+ANISOU  280  C   ALA A  35     4730   4263   3686   -562   1342  -1163       C  
+ATOM    281  O   ALA A  35      32.217  26.010  32.251  1.00 29.19           O  
+ANISOU  281  O   ALA A  35     4217   3594   3280   -541   1148  -1031       O  
+ATOM    282  CB  ALA A  35      35.152  24.875  31.194  1.00 34.84           C  
+ANISOU  282  CB  ALA A  35     4581   4474   4184   -357   1590  -1578       C  
+ATOM    283  N   GLY A  36      32.277  25.538  30.053  1.00 40.33           N  
+ANISOU  283  N   GLY A  36     5773   5262   4290   -616   1384  -1233       N  
+ATOM    284  CA  GLY A  36      30.837  25.335  29.942  1.00 38.25           C  
+ANISOU  284  CA  GLY A  36     5682   4975   3877   -666   1178  -1151       C  
+ATOM    285  C   GLY A  36      30.359  25.239  28.498  1.00 42.24           C  
+ANISOU  285  C   GLY A  36     6369   5647   4034   -742   1230  -1213       C  
+ATOM    286  O   GLY A  36      31.033  25.719  27.581  1.00 42.30           O  
+ANISOU  286  O   GLY A  36     6405   5813   3854   -791   1446  -1232       O  
+ATOM    287  N   VAL A  37      29.192  24.625  28.292  1.00 41.76           N  
+ANISOU  287  N   VAL A  37     6434   5562   3870   -773   1031  -1243       N  
+ATOM    288  CA  VAL A  37      28.657  24.379  26.942  1.00 45.66           C  
+ANISOU  288  CA  VAL A  37     7125   6195   4028   -835   1019  -1335       C  
+ATOM    289  C   VAL A  37      27.240  24.959  26.802  1.00 46.38           C  
+ANISOU  289  C   VAL A  37     7298   6353   3971   -910    784  -1152       C  
+ATOM    290  O   VAL A  37      26.360  24.633  27.594  1.00 39.40           O  
+ANISOU  290  O   VAL A  37     6339   5388   3244   -925    586  -1109       O  
+ATOM    291  CB  VAL A  37      28.630  22.851  26.610  1.00 43.98           C  
+ANISOU  291  CB  VAL A  37     7002   5889   3820   -794    963  -1632       C  
+ATOM    292  CG1 VAL A  37      27.936  22.582  25.272  1.00 44.86           C  
+ANISOU  292  CG1 VAL A  37     7339   6132   3572   -863    895  -1735       C  
+ATOM    293  CG2 VAL A  37      30.043  22.262  26.602  1.00 42.72           C  
+ANISOU  293  CG2 VAL A  37     6758   5687   3788   -660   1182  -1864       C  
+ATOM    294  N   PHE A  38      27.025  25.820  25.805  1.00 41.58           N  
+ANISOU  294  N   PHE A  38     6842   5900   3058   -958    803  -1045       N  
+ATOM    295  CA  PHE A  38      25.710  26.439  25.589  1.00 44.94           C  
+ANISOU  295  CA  PHE A  38     7341   6398   3337   -983    545   -888       C  
+ATOM    296  C   PHE A  38      25.340  26.452  24.111  1.00 47.16           C  
+ANISOU  296  C   PHE A  38     7879   6825   3213  -1033    495   -941       C  
+ATOM    297  O   PHE A  38      26.102  26.950  23.286  1.00 45.01           O  
+ANISOU  297  O   PHE A  38     7766   6637   2698  -1067    694   -911       O  
+ATOM    298  CB  PHE A  38      25.678  27.871  26.146  1.00 49.52           C  
+ANISOU  298  CB  PHE A  38     7876   6963   3976   -947    521   -618       C  
+ATOM    299  CG  PHE A  38      24.382  28.613  25.880  1.00 48.96           C  
+ANISOU  299  CG  PHE A  38     7879   6969   3755   -914    239   -474       C  
+ATOM    300  CD1 PHE A  38      24.347  29.687  25.004  1.00 50.34           C  
+ANISOU  300  CD1 PHE A  38     8285   7201   3641   -918    201   -314       C  
+ATOM    301  CD2 PHE A  38      23.206  28.237  26.509  1.00 47.26           C  
+ANISOU  301  CD2 PHE A  38     7499   6773   3685   -879      6   -502       C  
+ATOM    302  CE1 PHE A  38      23.163  30.365  24.759  1.00 48.36           C  
+ANISOU  302  CE1 PHE A  38     8106   7005   3264   -838   -104   -200       C  
+ATOM    303  CE2 PHE A  38      22.018  28.910  26.259  1.00 45.51           C  
+ANISOU  303  CE2 PHE A  38     7289   6655   3347   -814   -264   -406       C  
+ATOM    304  CZ  PHE A  38      21.995  29.968  25.383  1.00 40.58           C  
+ANISOU  304  CZ  PHE A  38     6902   6067   2451   -768   -340   -263       C  
+ATOM    305  N   ILE A  52      28.027  10.911  20.714  1.00 68.40           N  
+ANISOU  305  N   ILE A  52    11484   7884   6620   -189   -232  -4296       N  
+ATOM    306  CA  ILE A  52      29.453  10.734  20.966  1.00 71.20           C  
+ANISOU  306  CA  ILE A  52    11709   8215   7127      3     66  -4420       C  
+ATOM    307  C   ILE A  52      30.219  12.018  20.661  1.00 75.80           C  
+ANISOU  307  C   ILE A  52    12406   9004   7391    394    171  -4187       C  
+ATOM    308  O   ILE A  52      31.279  12.267  21.239  1.00 78.02           O  
+ANISOU  308  O   ILE A  52    12743   9162   7738    506    439  -4082       O  
+ATOM    309  CB  ILE A  52      30.041   9.582  20.132  1.00 76.85           C  
+ANISOU  309  CB  ILE A  52    12747   8731   7724    -12    260  -4705       C  
+ATOM    310  N   ALA A  53      29.674  12.830  19.755  1.00 62.45           N  
+ANISOU  310  N   ALA A  53    12215   6858   4654  -3250   2026   -833       N  
+ATOM    311  CA  ALA A  53      30.279  14.113  19.395  1.00 62.95           C  
+ANISOU  311  CA  ALA A  53    12330   6900   4687  -3209   2103   -681       C  
+ATOM    312  C   ALA A  53      30.078  15.172  20.480  1.00 62.90           C  
+ANISOU  312  C   ALA A  53    11997   6975   4928  -2891   1932   -421       C  
+ATOM    313  O   ALA A  53      31.029  15.828  20.907  1.00 60.33           O  
+ANISOU  313  O   ALA A  53    11481   6525   4916  -2695   2229   -468       O  
+ATOM    314  CB  ALA A  53      29.715  14.611  18.072  1.00 64.16           C  
+ANISOU  314  CB  ALA A  53    12859   7178   4341  -3539   1835   -476       C  
+ATOM    315  N   LEU A  54      28.834  15.343  20.916  1.00 65.16           N  
+ANISOU  315  N   LEU A  54    12192   7447   5121  -2858   1450   -123       N  
+ATOM    316  CA  LEU A  54      28.513  16.331  21.938  1.00 56.91           C  
+ANISOU  316  CA  LEU A  54    10760   6395   4467  -2515   1219    186       C  
+ATOM    317  C   LEU A  54      29.118  15.934  23.282  1.00 46.40           C  
+ANISOU  317  C   LEU A  54     8987   4902   3740  -2137   1418    -68       C  
+ATOM    318  O   LEU A  54      29.520  16.793  24.073  1.00 41.19           O  
+ANISOU  318  O   LEU A  54     8027   4154   3470  -1871   1461     26       O  
+ATOM    319  CB  LEU A  54      27.001  16.498  22.060  1.00 55.12           C  
+ANISOU  319  CB  LEU A  54    10422   6361   4159  -2500    610    562       C  
+ATOM    320  CG  LEU A  54      26.500  17.590  23.004  1.00 52.47           C  
+ANISOU  320  CG  LEU A  54     9704   5979   4254  -2137    359    942       C  
+ATOM    321  CD1 LEU A  54      26.883  18.970  22.492  1.00 51.19           C  
+ANISOU  321  CD1 LEU A  54     9674   5786   3990  -2130    477   1223       C  
+ATOM    322  CD2 LEU A  54      24.997  17.477  23.183  1.00 53.01           C  
+ANISOU  322  CD2 LEU A  54     9608   6219   4316  -2107   -193   1268       C  
+ATOM    323  N   LYS A  55      29.178  14.630  23.533  1.00 42.97           N  
+ANISOU  323  N   LYS A  55     8544   4428   3355  -2125   1553   -387       N  
+ATOM    324  CA  LYS A  55      29.835  14.107  24.729  1.00 42.13           C  
+ANISOU  324  CA  LYS A  55     8065   4179   3761  -1750   1776   -635       C  
+ATOM    325  C   LYS A  55      31.321  14.423  24.677  1.00 41.86           C  
+ANISOU  325  C   LYS A  55     7958   4051   3897  -1691   2260   -829       C  
+ATOM    326  O   LYS A  55      31.914  14.818  25.676  1.00 41.44           O  
+ANISOU  326  O   LYS A  55     7511   3948   4285  -1381   2316   -863       O  
+ATOM    327  CB  LYS A  55      29.617  12.594  24.869  1.00 40.19           C  
+ANISOU  327  CB  LYS A  55     7906   3885   3479  -1754   1910   -926       C  
+ATOM    328  CG  LYS A  55      28.209  12.211  25.273  1.00 41.80           C  
+ANISOU  328  CG  LYS A  55     8047   4155   3681  -1737   1462   -791       C  
+ATOM    329  CD  LYS A  55      27.903  10.735  24.984  1.00 47.27           C  
+ANISOU  329  CD  LYS A  55     8992   4808   4159  -1923   1650  -1096       C  
+ATOM    330  CE  LYS A  55      28.568   9.804  25.976  1.00 41.86           C  
+ANISOU  330  CE  LYS A  55     7909   3999   3998  -1478   1914  -1213       C  
+ATOM    331  NZ  LYS A  55      28.156   8.377  25.755  1.00 42.21           N  
+ANISOU  331  NZ  LYS A  55     8002   4040   3995  -1575   2008  -1297       N  
+ATOM    332  N   ARG A  56      31.915  14.240  23.499  1.00 46.62           N  
+ANISOU  332  N   ARG A  56     8945   4628   4139  -2015   2616   -965       N  
+ATOM    333  CA  ARG A  56      33.311  14.589  23.284  1.00 48.89           C  
+ANISOU  333  CA  ARG A  56     9084   4798   4694  -1970   2982  -1098       C  
+ATOM    334  C   ARG A  56      33.554  16.068  23.588  1.00 44.42           C  
+ANISOU  334  C   ARG A  56     8387   4262   4227  -1924   2984   -921       C  
+ATOM    335  O   ARG A  56      34.549  16.415  24.223  1.00 45.58           O  
+ANISOU  335  O   ARG A  56     8162   4363   4794  -1731   3183  -1046       O  
+ATOM    336  CB  ARG A  56      33.736  14.262  21.849  1.00 54.36           C  
+ANISOU  336  CB  ARG A  56    10168   5384   5103  -2303   3178  -1180       C  
+ATOM    337  N   LEU A  57      32.635  16.930  23.155  1.00 45.02           N  
+ANISOU  337  N   LEU A  57     8689   4411   4005  -2074   2662   -581       N  
+ATOM    338  CA  LEU A  57      32.769  18.366  23.407  1.00 50.59           C  
+ANISOU  338  CA  LEU A  57     9268   5089   4866  -2007   2621   -346       C  
+ATOM    339  C   LEU A  57      32.739  18.665  24.902  1.00 44.87           C  
+ANISOU  339  C   LEU A  57     8028   4347   4674  -1650   2440   -324       C  
+ATOM    340  O   LEU A  57      33.561  19.428  25.411  1.00 40.68           O  
+ANISOU  340  O   LEU A  57     7257   3758   4441  -1574   2652   -394       O  
+ATOM    341  CB  LEU A  57      31.666  19.159  22.689  1.00 52.54           C  
+ANISOU  341  CB  LEU A  57     9805   5421   4738  -2134   2242     69       C  
+ATOM    342  CG  LEU A  57      31.816  20.687  22.692  1.00 55.45           C  
+ANISOU  342  CG  LEU A  57    10097   5739   5231  -2036   2245    300       C  
+ATOM    343  CD1 LEU A  57      33.145  21.086  22.077  1.00 49.45           C  
+ANISOU  343  CD1 LEU A  57     9422   4863   4503  -2142   2703     24       C  
+ATOM    344  CD2 LEU A  57      30.669  21.373  21.956  1.00 52.15           C  
+ANISOU  344  CD2 LEU A  57     9888   5442   4484  -2065   1856    733       C  
+ATOM    345  N   ILE A  58      31.779  18.054  25.590  1.00 42.38           N  
+ANISOU  345  N   ILE A  58     7571   4075   4458  -1464   2064   -241       N  
+ATOM    346  CA  ILE A  58      31.620  18.199  27.032  1.00 37.54           C  
+ANISOU  346  CA  ILE A  58     6543   3415   4307  -1124   1878   -218       C  
+ATOM    347  C   ILE A  58      32.819  17.627  27.785  1.00 32.98           C  
+ANISOU  347  C   ILE A  58     5637   2820   4072   -934   2166   -581       C  
+ATOM    348  O   ILE A  58      33.367  18.278  28.677  1.00 31.61           O  
+ANISOU  348  O   ILE A  58     5155   2626   4229   -784   2199   -613       O  
+ATOM    349  CB  ILE A  58      30.329  17.508  27.511  1.00 34.55           C  
+ANISOU  349  CB  ILE A  58     6131   3051   3946   -981   1473    -83       C  
+ATOM    350  CG1 ILE A  58      29.097  18.283  27.023  1.00 32.89           C  
+ANISOU  350  CG1 ILE A  58     6097   2888   3513  -1094   1122    358       C  
+ATOM    351  CG2 ILE A  58      30.323  17.372  29.025  1.00 28.15           C  
+ANISOU  351  CG2 ILE A  58     4948   2146   3601   -616   1369   -146       C  
+ATOM    352  CD1 ILE A  58      27.770  17.616  27.415  1.00 32.81           C  
+ANISOU  352  CD1 ILE A  58     6017   2907   3541   -993    725    498       C  
+ATOM    353  N   ASN A  59      33.234  16.416  27.408  1.00 34.17           N  
+ANISOU  353  N   ASN A  59     5863   2988   4133   -951   2391   -844       N  
+ATOM    354  CA  ASN A  59      34.431  15.812  27.983  1.00 34.19           C  
+ANISOU  354  CA  ASN A  59     5536   3000   4452   -746   2685  -1134       C  
+ATOM    355  C   ASN A  59      35.630  16.750  27.886  1.00 35.94           C  
+ANISOU  355  C   ASN A  59     5556   3251   4849   -843   2911  -1190       C  
+ATOM    356  O   ASN A  59      36.393  16.897  28.841  1.00 37.92           O  
+ANISOU  356  O   ASN A  59     5369   3582   5455   -649   2812  -1235       O  
+ATOM    357  CB  ASN A  59      34.765  14.480  27.294  1.00 36.36           C  
+ANISOU  357  CB  ASN A  59     5925   3286   4606   -812   2806  -1227       C  
+ATOM    358  CG  ASN A  59      33.746  13.385  27.576  1.00 34.81           C  
+ANISOU  358  CG  ASN A  59     5815   3090   4321   -701   2582  -1191       C  
+ATOM    359  OD1 ASN A  59      32.922  13.489  28.486  1.00 31.77           O  
+ANISOU  359  OD1 ASN A  59     5305   2708   4059   -495   2285  -1098       O  
+ATOM    360  ND2 ASN A  59      33.816  12.311  26.793  1.00 37.18           N  
+ANISOU  360  ND2 ASN A  59     6329   3359   4440   -850   2733  -1259       N  
+ATOM    361  N   GLY A  60      35.786  17.393  26.732  1.00 38.73           N  
+ANISOU  361  N   GLY A  60     6249   3553   4911  -1169   3158  -1160       N  
+ATOM    362  CA  GLY A  60      36.879  18.326  26.524  1.00 40.84           C  
+ANISOU  362  CA  GLY A  60     6376   3797   5343  -1290   3364  -1225       C  
+ATOM    363  C   GLY A  60      36.736  19.543  27.417  1.00 39.57           C  
+ANISOU  363  C   GLY A  60     5998   3656   5383  -1237   3257  -1113       C  
+ATOM    364  O   GLY A  60      37.722  20.098  27.896  1.00 42.57           O  
+ANISOU  364  O   GLY A  60     6057   4063   6054  -1221   3314  -1243       O  
+ATOM    365  N   GLY A  61      35.494  19.955  27.643  1.00 36.84           N  
+ANISOU  365  N   GLY A  61     5823   3275   4901  -1205   2940   -815       N  
+ATOM    366  CA  GLY A  61      35.219  21.057  28.544  1.00 41.26           C  
+ANISOU  366  CA  GLY A  61     6218   3787   5673  -1133   2771   -646       C  
+ATOM    367  C   GLY A  61      35.582  20.693  29.969  1.00 40.01           C  
+ANISOU  367  C   GLY A  61     5602   3693   5907   -858   2630   -818       C  
+ATOM    368  O   GLY A  61      36.108  21.522  30.717  1.00 37.64           O  
+ANISOU  368  O   GLY A  61     5065   3396   5842   -878   2685   -877       O  
+ATOM    369  N   LEU A  62      35.313  19.442  30.342  1.00 37.04           N  
+ANISOU  369  N   LEU A  62     5131   3365   5577   -618   2467   -906       N  
+ATOM    370  CA  LEU A  62      35.589  18.974  31.696  1.00 37.37           C  
+ANISOU  370  CA  LEU A  62     4787   3486   5927   -321   2255  -1004       C  
+ATOM    371  C   LEU A  62      37.080  18.742  31.900  1.00 37.29           C  
+ANISOU  371  C   LEU A  62     4441   3665   6065   -331   2319  -1191       C  
+ATOM    372  O   LEU A  62      37.572  18.857  33.022  1.00 33.68           O  
+ANISOU  372  O   LEU A  62     3686   3326   5786   -199   2102  -1221       O  
+ATOM    373  CB  LEU A  62      34.800  17.695  32.003  1.00 32.38           C  
+ANISOU  373  CB  LEU A  62     4202   2891   5211    -88   1948   -914       C  
+ATOM    374  CG  LEU A  62      33.316  17.909  32.318  1.00 33.03           C  
+ANISOU  374  CG  LEU A  62     4479   2823   5247     -2   1672   -675       C  
+ATOM    375  CD1 LEU A  62      32.575  16.584  32.282  1.00 33.59           C  
+ANISOU  375  CD1 LEU A  62     4631   2959   5172    126   1473   -648       C  
+ATOM    376  CD2 LEU A  62      33.123  18.599  33.675  1.00 33.21           C  
+ANISOU  376  CD2 LEU A  62     4284   2910   5423    124   1371   -522       C  
+ATOM    377  N   ASN A  63      37.794  18.418  30.821  1.00 37.31           N  
+ANISOU  377  N   ASN A  63     3937   4433   5806      8   2185   -159       N  
+ATOM    378  CA  ASN A  63      39.248  18.330  30.879  1.00 40.39           C  
+ANISOU  378  CA  ASN A  63     4079   4790   6478     16   2278   -194       C  
+ATOM    379  C   ASN A  63      39.825  19.693  31.244  1.00 40.72           C  
+ANISOU  379  C   ASN A  63     3954   4755   6765   -108   2294   -151       C  
+ATOM    380  O   ASN A  63      39.353  20.725  30.754  1.00 40.83           O  
+ANISOU  380  O   ASN A  63     4098   4732   6684   -170   2371    -52       O  
+ATOM    381  CB  ASN A  63      39.829  17.832  29.548  1.00 44.77           C  
+ANISOU  381  CB  ASN A  63     4718   5362   6931    108   2519   -167       C  
+ATOM    382  N   ASN A  64      40.843  19.682  32.103  1.00 40.84           N  
+ANISOU  382  N   ASN A  64     3685   4737   7097   -131   2203   -235       N  
+ATOM    383  CA  ASN A  64      41.425  20.900  32.673  1.00 40.21           C  
+ANISOU  383  CA  ASN A  64     3418   4569   7291   -247   2159   -242       C  
+ATOM    384  C   ASN A  64      40.422  21.699  33.513  1.00 36.64           C  
+ANISOU  384  C   ASN A  64     3037   4107   6779   -326   1960   -242       C  
+ATOM    385  O   ASN A  64      40.424  22.933  33.488  1.00 37.80           O  
+ANISOU  385  O   ASN A  64     3175   4172   7014   -419   1995   -196       O  
+ATOM    386  CB  ASN A  64      42.017  21.796  31.574  1.00 48.61           C  
+ANISOU  386  CB  ASN A  64     4496   5553   8422   -296   2441   -135       C  
+ATOM    387  N   THR A  65      39.548  20.988  34.228  1.00 33.29           N  
+ANISOU  387  N   THR A  65     2688   3757   6205   -280   1767   -291       N  
+ATOM    388  CA  THR A  65      38.796  21.566  35.342  1.00 30.29           C  
+ANISOU  388  CA  THR A  65     2307   3377   5825   -339   1535   -330       C  
+ATOM    389  C   THR A  65      38.900  20.621  36.533  1.00 33.65           C  
+ANISOU  389  C   THR A  65     2603   3862   6322   -262   1286   -451       C  
+ATOM    390  O   THR A  65      39.232  19.448  36.368  1.00 33.71           O  
+ANISOU  390  O   THR A  65     2586   3910   6312   -156   1308   -481       O  
+ATOM    391  CB  THR A  65      37.293  21.791  35.028  1.00 31.67           C  
+ANISOU  391  CB  THR A  65     2754   3586   5695   -357   1545   -243       C  
+ATOM    392  OG1 THR A  65      36.632  20.522  34.912  1.00 31.61           O  
+ANISOU  392  OG1 THR A  65     2870   3657   5484   -264   1527   -257       O  
+ATOM    393  CG2 THR A  65      37.102  22.605  33.750  1.00 30.09           C  
+ANISOU  393  CG2 THR A  65     2723   3339   5369   -388   1768   -113       C  
+ATOM    394  N   SER A  66      38.597  21.115  37.729  1.00 35.56           N  
+ANISOU  394  N   SER A  66     2781   4106   6626   -294   1039   -521       N  
+ATOM    395  CA  SER A  66      38.707  20.283  38.923  1.00 35.71           C  
+ANISOU  395  CA  SER A  66     2695   4183   6689   -192    769   -629       C  
+ATOM    396  C   SER A  66      37.453  20.390  39.777  1.00 31.74           C  
+ANISOU  396  C   SER A  66     2319   3730   6011   -192    578   -635       C  
+ATOM    397  O   SER A  66      37.256  19.612  40.705  1.00 24.33           O  
+ANISOU  397  O   SER A  66     1442   2845   4958    -75    345   -672       O  
+ATOM    398  CB  SER A  66      39.945  20.664  39.741  1.00 42.38           C  
+ANISOU  398  CB  SER A  66     3304   4991   7807   -185    589   -749       C  
+ATOM    399  OG  SER A  66      39.819  21.957  40.300  1.00 46.58           O  
+ANISOU  399  OG  SER A  66     3819   5469   8411   -283    479   -789       O  
+ATOM    400  N   VAL A  67      36.604  21.357  39.446  1.00 27.57           N  
+ANISOU  400  N   VAL A  67     1937   3172   5365   -301    658   -562       N  
+ATOM    401  CA  VAL A  67      35.342  21.551  40.133  1.00 24.63           C  
+ANISOU  401  CA  VAL A  67     1793   2837   4728   -295    484   -534       C  
+ATOM    402  C   VAL A  67      34.211  21.676  39.123  1.00 23.52           C  
+ANISOU  402  C   VAL A  67     1901   2698   4340   -339    664   -404       C  
+ATOM    403  O   VAL A  67      34.331  22.395  38.126  1.00 24.18           O  
+ANISOU  403  O   VAL A  67     1982   2727   4480   -420    887   -340       O  
+ATOM    404  CB  VAL A  67      35.334  22.822  41.010  1.00 27.35           C  
+ANISOU  404  CB  VAL A  67     2057   3140   5194   -369    322   -612       C  
+ATOM    405  CG1 VAL A  67      34.017  22.911  41.769  1.00 24.68           C  
+ANISOU  405  CG1 VAL A  67     1959   2853   4566   -333    159   -585       C  
+ATOM    406  CG2 VAL A  67      36.493  22.823  41.969  1.00 24.26           C  
+ANISOU  406  CG2 VAL A  67     1404   2745   5068   -324    111   -770       C  
+ATOM    407  N   THR A  68      33.119  20.974  39.385  1.00 19.27           N  
+ANISOU  407  N   THR A  68     1572   2214   3534   -278    566   -365       N  
+ATOM    408  CA  THR A  68      31.909  21.145  38.596  1.00 17.09           C  
+ANISOU  408  CA  THR A  68     1519   1945   3030   -311    666   -269       C  
+ATOM    409  C   THR A  68      30.851  21.795  39.466  1.00 21.34           C  
+ANISOU  409  C   THR A  68     2158   2498   3450   -333    506   -263       C  
+ATOM    410  O   THR A  68      30.563  21.334  40.574  1.00 19.03           O  
+ANISOU  410  O   THR A  68     1889   2246   3096   -271    325   -298       O  
+ATOM    411  CB  THR A  68      31.406  19.819  38.045  1.00 22.11           C  
+ANISOU  411  CB  THR A  68     2299   2616   3487   -236    703   -241       C  
+ATOM    412  OG1 THR A  68      32.361  19.309  37.112  1.00 23.31           O  
+ANISOU  412  OG1 THR A  68     2375   2751   3730   -205    883   -253       O  
+ATOM    413  CG2 THR A  68      30.068  19.999  37.343  1.00 20.88           C  
+ANISOU  413  CG2 THR A  68     2355   2472   3105   -263    744   -172       C  
+ATOM    414  N  ACYS A  69      30.256  22.860  38.945  0.65 20.96           N  
+ANISOU  414  N  ACYS A  69     2186   2415   3362   -405    587   -207       N  
+ATOM    415  N  BCYS A  69      30.300  22.900  38.967  0.35 20.62           N  
+ANISOU  415  N  BCYS A  69     2135   2370   3330   -407    586   -210       N  
+ATOM    416  CA ACYS A  69      29.265  23.619  39.685  0.65 17.34           C  
+ANISOU  416  CA ACYS A  69     1813   1960   2814   -421    460   -206       C  
+ATOM    417  CA BCYS A  69      29.244  23.635  39.655  0.35 18.81           C  
+ANISOU  417  CA BCYS A  69     2002   2146   2998   -422    464   -204       C  
+ATOM    418  C  ACYS A  69      27.925  23.587  38.948  0.65 17.80           C  
+ANISOU  418  C  ACYS A  69     2065   2042   2657   -417    514   -118       C  
+ATOM    419  C  BCYS A  69      27.935  23.517  38.890  0.35 18.03           C  
+ANISOU  419  C  BCYS A  69     2096   2073   2682   -415    521   -116       C  
+ATOM    420  O  ACYS A  69      27.784  24.204  37.889  0.65 17.36           O  
+ANISOU  420  O  ACYS A  69     2071   1948   2579   -452    654    -51       O  
+ATOM    421  O  BCYS A  69      27.815  24.014  37.768  0.35 17.92           O  
+ANISOU  421  O  BCYS A  69     2147   2025   2636   -445    666    -48       O  
+ATOM    422  CB ACYS A  69      29.749  25.053  39.873  0.65 24.94           C  
+ANISOU  422  CB ACYS A  69     2672   2838   3968   -501    471   -240       C  
+ATOM    423  CB BCYS A  69      29.617  25.110  39.813  0.35 23.17           C  
+ANISOU  423  CB BCYS A  69     2467   2613   3724   -503    477   -230       C  
+ATOM    424  SG ACYS A  69      28.627  26.057  40.800  0.65 25.17           S  
+ANISOU  424  SG ACYS A  69     2801   2857   3904   -502    322   -263       S  
+ATOM    425  SG BCYS A  69      30.722  25.454  41.183  0.35 19.13           S  
+ANISOU  425  SG BCYS A  69     1742   2077   3450   -501    283   -389       S  
+ATOM    426  N   VAL A  70      26.958  22.859  39.497  1.00 16.26           N  
+ANISOU  426  N   VAL A  70     1962   1904   2314   -368    407   -116       N  
+ATOM    427  CA  VAL A  70      25.636  22.721  38.873  1.00 19.03           C  
+ANISOU  427  CA  VAL A  70     2458   2278   2496   -362    424    -58       C  
+ATOM    428  C   VAL A  70      24.767  23.900  39.289  1.00 18.77           C  
+ANISOU  428  C   VAL A  70     2465   2232   2435   -381    371    -41       C  
+ATOM    429  O   VAL A  70      24.476  24.042  40.466  1.00 15.79           O  
+ANISOU  429  O   VAL A  70     2069   1874   2058   -360    266    -78       O  
+ATOM    430  CB  VAL A  70      24.935  21.412  39.278  1.00 16.29           C  
+ANISOU  430  CB  VAL A  70     2163   1972   2056   -317    352    -62       C  
+ATOM    431  CG1 VAL A  70      23.592  21.273  38.552  1.00 17.95           C  
+ANISOU  431  CG1 VAL A  70     2483   2196   2142   -321    354    -28       C  
+ATOM    432  CG2 VAL A  70      25.829  20.199  38.960  1.00 16.93           C  
+ANISOU  432  CG2 VAL A  70     2207   2045   2180   -282    394    -88       C  
+ATOM    433  N   LEU A  71      24.371  24.747  38.337  1.00 15.37           N  
+ANISOU  433  N   LEU A  71     2104   1766   1970   -403    448     16       N  
+ATOM    434  CA  LEU A  71      23.558  25.912  38.672  1.00 15.96           C  
+ANISOU  434  CA  LEU A  71     2217   1812   2035   -407    402     32       C  
+ATOM    435  C   LEU A  71      22.088  25.547  38.521  1.00 18.21           C  
+ANISOU  435  C   LEU A  71     2591   2153   2177   -364    341     57       C  
+ATOM    436  O   LEU A  71      21.624  25.291  37.409  1.00 19.67           O  
+ANISOU  436  O   LEU A  71     2857   2351   2266   -344    374     98       O  
+ATOM    437  CB  LEU A  71      23.944  27.116  37.779  1.00 14.67           C  
+ANISOU  437  CB  LEU A  71     2082   1557   1935   -441    520     95       C  
+ATOM    438  CG  LEU A  71      25.442  27.448  37.806  1.00 21.80           C  
+ANISOU  438  CG  LEU A  71     2860   2386   3038   -503    612     71       C  
+ATOM    439  CD1 LEU A  71      25.775  28.609  36.843  1.00 20.26           C  
+ANISOU  439  CD1 LEU A  71     2704   2074   2921   -545    777    167       C  
+ATOM    440  CD2 LEU A  71      25.909  27.766  39.228  1.00 20.81           C  
+ANISOU  440  CD2 LEU A  71     2606   2242   3058   -524    478    -43       C  
+ATOM    441  N   ILE A  72      21.368  25.511  39.643  1.00 15.38           N  
+ANISOU  441  N   ILE A  72     2212   1827   1806   -341    251     24       N  
+ATOM    442  CA  ILE A  72      20.035  24.903  39.675  1.00 17.03           C  
+ANISOU  442  CA  ILE A  72     2452   2087   1930   -311    206     38       C  
+ATOM    443  C   ILE A  72      18.906  25.915  39.514  1.00 15.55           C  
+ANISOU  443  C   ILE A  72     2298   1890   1719   -283    178     61       C  
+ATOM    444  O   ILE A  72      18.684  26.769  40.376  1.00 16.39           O  
+ANISOU  444  O   ILE A  72     2389   1979   1858   -263    155     40       O  
+ATOM    445  CB  ILE A  72      19.810  24.139  40.980  1.00 16.49           C  
+ANISOU  445  CB  ILE A  72     2346   2058   1860   -290    167     14       C  
+ATOM    446  CG1 ILE A  72      20.981  23.186  41.249  1.00 16.83           C  
+ANISOU  446  CG1 ILE A  72     2359   2103   1934   -293    175     -6       C  
+ATOM    447  CG2 ILE A  72      18.463  23.383  40.931  1.00 16.85           C  
+ANISOU  447  CG2 ILE A  72     2394   2135   1873   -281    156     36       C  
+ATOM    448  CD1 ILE A  72      21.023  22.654  42.689  1.00 16.74           C  
+ANISOU  448  CD1 ILE A  72     2338   2121   1900   -243    132    -16       C  
+ATOM    449  N   GLY A  73      18.198  25.797  38.396  1.00 15.96           N  
+ANISOU  449  N   GLY A  73     2401   1953   1710   -264    165     91       N  
+ATOM    450  CA  GLY A  73      17.019  26.588  38.125  1.00 18.30           C  
+ANISOU  450  CA  GLY A  73     2720   2247   1984   -215    113    111       C  
+ATOM    451  C   GLY A  73      15.802  25.672  38.130  1.00 20.60           C  
+ANISOU  451  C   GLY A  73     2960   2596   2270   -201     43     83       C  
+ATOM    452  O   GLY A  73      15.856  24.575  38.698  1.00 19.09           O  
+ANISOU  452  O   GLY A  73     2716   2428   2111   -237     56     57       O  
+ATOM    453  N   SER A  74      14.725  26.099  37.472  1.00 16.77           N  
+ANISOU  453  N   SER A  74     2484   2121   1765   -146    -32     88       N  
+ATOM    454  CA  SER A  74      13.436  25.418  37.600  1.00 11.51           C  
+ANISOU  454  CA  SER A  74     1719   1497   1159   -139   -106     45       C  
+ATOM    455  C   SER A  74      13.431  24.018  36.966  1.00 22.12           C  
+ANISOU  455  C   SER A  74     3052   2854   2499   -180   -148     -4       C  
+ATOM    456  O   SER A  74      12.740  23.104  37.443  1.00 18.35           O  
+ANISOU  456  O   SER A  74     2465   2381   2126   -220   -159    -41       O  
+ATOM    457  CB  SER A  74      12.339  26.288  36.979  1.00 17.69           C  
+ANISOU  457  CB  SER A  74     2498   2285   1937    -53   -207     49       C  
+ATOM    458  OG  SER A  74      12.240  27.523  37.690  1.00 16.95           O  
+ANISOU  458  OG  SER A  74     2404   2160   1874    -11   -164     82       O  
+ATOM    459  N   GLN A  75      14.201  23.859  35.898  1.00 14.99           N  
+ANISOU  459  N   GLN A  75     2264   1946   1487   -166   -154     -6       N  
+ATOM    460  CA  GLN A  75      14.119  22.655  35.065  1.00 15.86           C  
+ANISOU  460  CA  GLN A  75     2393   2063   1571   -177   -219    -80       C  
+ATOM    461  C   GLN A  75      15.453  21.916  34.895  1.00 18.45           C  
+ANISOU  461  C   GLN A  75     2788   2371   1853   -211   -123    -83       C  
+ATOM    462  O   GLN A  75      15.539  20.929  34.152  1.00 18.47           O  
+ANISOU  462  O   GLN A  75     2829   2368   1820   -208   -164   -154       O  
+ATOM    463  CB  GLN A  75      13.548  23.042  33.706  1.00 19.23           C  
+ANISOU  463  CB  GLN A  75     2916   2517   1874    -84   -349   -108       C  
+ATOM    464  CG  GLN A  75      12.038  23.233  33.739  1.00 24.94           C  
+ANISOU  464  CG  GLN A  75     3525   3262   2690    -49   -500   -157       C  
+ATOM    465  CD  GLN A  75      11.305  21.933  34.053  1.00 31.83           C  
+ANISOU  465  CD  GLN A  75     4242   4121   3733   -126   -564   -260       C  
+ATOM    466  OE1 GLN A  75      11.496  20.917  33.373  1.00 40.39           O  
+ANISOU  466  OE1 GLN A  75     5365   5190   4793   -142   -625   -349       O  
+ATOM    467  NE2 GLN A  75      10.479  21.951  35.094  1.00 29.28           N  
+ANISOU  467  NE2 GLN A  75     3745   3788   3592   -171   -533   -249       N  
+ATOM    468  N   THR A  76      16.470  22.363  35.621  1.00 17.08           N  
+ANISOU  468  N   THR A  76     2612   2181   1698   -237     -6    -23       N  
+ATOM    469  CA  THR A  76      17.835  21.844  35.471  1.00 18.22           C  
+ANISOU  469  CA  THR A  76     2793   2306   1823   -256     91    -22       C  
+ATOM    470  C   THR A  76      17.896  20.320  35.694  1.00 20.08           C  
+ANISOU  470  C   THR A  76     2988   2524   2119   -288     77    -83       C  
+ATOM    471  O   THR A  76      18.632  19.585  35.009  1.00 17.75           O  
+ANISOU  471  O   THR A  76     2746   2214   1783   -274    113   -123       O  
+ATOM    472  CB  THR A  76      18.784  22.548  36.465  1.00 20.72           C  
+ANISOU  472  CB  THR A  76     3064   2603   2205   -283    176     26       C  
+ATOM    473  OG1 THR A  76      18.599  23.977  36.395  1.00 18.37           O  
+ANISOU  473  OG1 THR A  76     2794   2291   1893   -263    184     76       O  
+ATOM    474  CG2 THR A  76      20.246  22.183  36.172  1.00 18.73           C  
+ANISOU  474  CG2 THR A  76     2822   2332   1963   -293    275     24       C  
+ATOM    475  N   PHE A  77      17.084  19.860  36.641  1.00 15.42           N  
+ANISOU  475  N   PHE A  77     2305   1922   1632   -323     43    -86       N  
+ATOM    476  CA  PHE A  77      17.057  18.467  37.061  1.00 16.99           C  
+ANISOU  476  CA  PHE A  77     2460   2072   1921   -359     50   -116       C  
+ATOM    477  C   PHE A  77      16.682  17.554  35.911  1.00 19.40           C  
+ANISOU  477  C   PHE A  77     2802   2347   2222   -359    -27   -215       C  
+ATOM    478  O   PHE A  77      16.969  16.353  35.931  1.00 18.64           O  
+ANISOU  478  O   PHE A  77     2702   2186   2192   -380    -14   -258       O  
+ATOM    479  CB  PHE A  77      16.039  18.269  38.196  1.00 15.12           C  
+ANISOU  479  CB  PHE A  77     2126   1821   1799   -394     56    -79       C  
+ATOM    480  CG  PHE A  77      14.615  18.259  37.711  1.00 20.12           C  
+ANISOU  480  CG  PHE A  77     2691   2453   2502   -412    -34   -130       C  
+ATOM    481  CD1 PHE A  77      13.963  19.453  37.428  1.00 14.81           C  
+ANISOU  481  CD1 PHE A  77     2008   1836   1784   -372    -90   -125       C  
+ATOM    482  CD2 PHE A  77      13.941  17.063  37.502  1.00 24.75           C  
+ANISOU  482  CD2 PHE A  77     3212   2969   3222   -464    -74   -192       C  
+ATOM    483  CE1 PHE A  77      12.645  19.453  36.964  1.00 16.33           C  
+ANISOU  483  CE1 PHE A  77     2115   2033   2059   -373   -199   -184       C  
+ATOM    484  CE2 PHE A  77      12.634  17.044  37.030  1.00 23.68           C  
+ANISOU  484  CE2 PHE A  77     2979   2828   3192   -484   -182   -264       C  
+ATOM    485  CZ  PHE A  77      11.978  18.243  36.760  1.00 18.31           C  
+ANISOU  485  CZ  PHE A  77     2275   2221   2459   -433   -252   -261       C  
+ATOM    486  N   ASN A  78      15.989  18.118  34.928  1.00 13.88           N  
+ANISOU  486  N   ASN A  78     2143   1687   1445   -322   -124   -261       N  
+ATOM    487  CA  ASN A  78      15.421  17.328  33.854  1.00 19.80           C  
+ANISOU  487  CA  ASN A  78     2926   2415   2181   -306   -247   -386       C  
+ATOM    488  C   ASN A  78      16.272  17.293  32.578  1.00 24.72           C  
+ANISOU  488  C   ASN A  78     3715   3063   2613   -225   -238   -436       C  
+ATOM    489  O   ASN A  78      15.892  16.675  31.589  1.00 22.43           O  
+ANISOU  489  O   ASN A  78     3491   2766   2267   -184   -354   -562       O  
+ATOM    490  CB  ASN A  78      14.031  17.868  33.525  1.00 21.56           C  
+ANISOU  490  CB  ASN A  78     3090   2671   2431   -288   -397   -427       C  
+ATOM    491  CG  ASN A  78      13.184  16.858  32.799  1.00 27.84           C  
+ANISOU  491  CG  ASN A  78     3848   3423   3308   -300   -561   -586       C  
+ATOM    492  OD1 ASN A  78      13.234  15.674  33.107  1.00 27.95           O  
+ANISOU  492  OD1 ASN A  78     3804   3347   3468   -371   -541   -641       O  
+ATOM    493  ND2 ASN A  78      12.413  17.315  31.821  1.00 33.95           N  
+ANISOU  493  ND2 ASN A  78     4657   4247   3994   -223   -739   -668       N  
+ATOM    494  N   ARG A  79      17.422  17.954  32.605  1.00 19.64           N  
+ANISOU  494  N   ARG A  79     3137   2447   1879   -198    -96   -345       N  
+ATOM    495  CA  ARG A  79      18.188  18.159  31.385  1.00 17.71           C  
+ANISOU  495  CA  ARG A  79     3053   2234   1443   -110    -39   -358       C  
+ATOM    496  C   ARG A  79      19.195  17.035  31.144  1.00 15.51           C  
+ANISOU  496  C   ARG A  79     2806   1914   1172   -100     48   -423       C  
+ATOM    497  O   ARG A  79      20.064  16.782  31.986  1.00 18.00           O  
+ANISOU  497  O   ARG A  79     3039   2198   1604   -144    158   -374       O  
+ATOM    498  CB  ARG A  79      18.907  19.509  31.437  1.00 17.74           C  
+ANISOU  498  CB  ARG A  79     3094   2265   1381    -91     97   -222       C  
+ATOM    499  CG  ARG A  79      17.968  20.700  31.677  1.00 18.19           C  
+ANISOU  499  CG  ARG A  79     3132   2344   1435    -85     20   -155       C  
+ATOM    500  CD  ARG A  79      16.871  20.767  30.615  1.00 20.80           C  
+ANISOU  500  CD  ARG A  79     3561   2714   1629      4   -149   -219       C  
+ATOM    501  NE  ARG A  79      17.412  20.961  29.273  1.00 22.17           N  
+ANISOU  501  NE  ARG A  79     3942   2916   1567    118    -97   -209       N  
+ATOM    502  CZ  ARG A  79      16.682  21.017  28.161  1.00 27.33           C  
+ANISOU  502  CZ  ARG A  79     4736   3614   2034    238   -245   -267       C  
+ATOM    503  NH1 ARG A  79      15.362  20.878  28.212  1.00 31.93           N  
+ANISOU  503  NH1 ARG A  79     5243   4214   2674    248   -476   -358       N  
+ATOM    504  NH2 ARG A  79      17.276  21.204  26.992  1.00 32.48           N  
+ANISOU  504  NH2 ARG A  79     5511   4291   2540    334   -151   -225       N  
+ATOM    505  N   ARG A  80      19.072  16.393  29.987  1.00 18.95           N  
+ANISOU  505  N   ARG A  80     3369   2354   1479    -24    -14   -544       N  
+ATOM    506  CA  ARG A  80      19.928  15.260  29.628  1.00 21.74           C  
+ANISOU  506  CA  ARG A  80     3767   2659   1832      7     59   -634       C  
+ATOM    507  C   ARG A  80      21.417  15.559  29.811  1.00 23.38           C  
+ANISOU  507  C   ARG A  80     3966   2877   2041     24    285   -537       C  
+ATOM    508  O   ARG A  80      22.155  14.760  30.392  1.00 22.37           O  
+ANISOU  508  O   ARG A  80     3756   2692   2050     -1    352   -552       O  
+ATOM    509  CB  ARG A  80      19.663  14.835  28.185  1.00 20.02           C  
+ANISOU  509  CB  ARG A  80     3735   2466   1405    124    -28   -781       C  
+ATOM    510  CG  ARG A  80      20.532  13.665  27.718  1.00 21.13           C  
+ANISOU  510  CG  ARG A  80     3943   2553   1531    179     53   -897       C  
+ATOM    511  CD  ARG A  80      20.225  13.298  26.296  1.00 26.22           C  
+ANISOU  511  CD  ARG A  80     4694   3250   2019    286    -39  -1012       C  
+ATOM    512  NE  ARG A  80      20.942  12.080  25.923  1.00 30.31           N  
+ANISOU  512  NE  ARG A  80     5238   3709   2568    328     21  -1134       N  
+ATOM    513  CZ  ARG A  80      21.062  11.622  24.685  1.00 32.52           C  
+ANISOU  513  CZ  ARG A  80     5626   4026   2705    428      6  -1234       C  
+ATOM    514  NH1 ARG A  80      20.528  12.284  23.664  1.00 37.52           N  
+ANISOU  514  NH1 ARG A  80     6364   4753   3139    506    -71  -1217       N  
+ATOM    515  NH2 ARG A  80      21.740  10.504  24.466  1.00 34.06           N  
+ANISOU  515  NH2 ARG A  80     5835   4154   2951    462     70  -1349       N  
+ATOM    516  N   TRP A  81      21.880  16.703  29.318  1.00 19.11           N  
+ANISOU  516  N   TRP A  81     3499   2395   1369     68    405   -434       N  
+ATOM    517  CA  TRP A  81      23.318  16.898  29.323  1.00 22.65           C  
+ANISOU  517  CA  TRP A  81     3917   2838   1850     82    630   -366       C  
+ATOM    518  C   TRP A  81      23.815  17.470  30.641  1.00 19.64           C  
+ANISOU  518  C   TRP A  81     3350   2435   1678    -16    676   -266       C  
+ATOM    519  O   TRP A  81      25.003  17.375  30.942  1.00 20.92           O  
+ANISOU  519  O   TRP A  81     3421   2578   1951    -22    814   -242       O  
+ATOM    520  CB  TRP A  81      23.737  17.743  28.111  1.00 26.88           C  
+ANISOU  520  CB  TRP A  81     4589   3424   2200    173    767   -291       C  
+ATOM    521  CG  TRP A  81      23.408  16.989  26.865  1.00 25.11           C  
+ANISOU  521  CG  TRP A  81     4499   3233   1810    283    687   -402       C  
+ATOM    522  CD1 TRP A  81      22.455  17.295  25.943  1.00 25.30           C  
+ANISOU  522  CD1 TRP A  81     4641   3306   1666    354    544   -422       C  
+ATOM    523  CD2 TRP A  81      23.962  15.731  26.466  1.00 25.82           C  
+ANISOU  523  CD2 TRP A  81     4609   3300   1901    336    720   -530       C  
+ATOM    524  NE1 TRP A  81      22.420  16.330  24.958  1.00 29.48           N  
+ANISOU  524  NE1 TRP A  81     5265   3853   2084    443    489   -558       N  
+ATOM    525  CE2 TRP A  81      23.327  15.352  25.268  1.00 33.32           C  
+ANISOU  525  CE2 TRP A  81     5694   4292   2672    431    597   -628       C  
+ATOM    526  CE3 TRP A  81      24.949  14.894  26.998  1.00 26.66           C  
+ANISOU  526  CE3 TRP A  81     4627   3351   2152    322    838   -575       C  
+ATOM    527  CZ2 TRP A  81      23.653  14.175  24.587  1.00 33.57           C  
+ANISOU  527  CZ2 TRP A  81     5782   4310   2662    504    594   -776       C  
+ATOM    528  CZ3 TRP A  81      25.264  13.724  26.325  1.00 25.77           C  
+ANISOU  528  CZ3 TRP A  81     4568   3219   2003    404    837   -712       C  
+ATOM    529  CH2 TRP A  81      24.620  13.379  25.132  1.00 32.48           C  
+ANISOU  529  CH2 TRP A  81     5559   4112   2671    489    718   -815       C  
+ATOM    530  N   VAL A  82      22.913  18.032  31.447  1.00 18.10           N  
+ANISOU  530  N   VAL A  82     3092   2243   1543    -82    550   -223       N  
+ATOM    531  CA  VAL A  82      23.264  18.329  32.819  1.00 16.51           C  
+ANISOU  531  CA  VAL A  82     2731   2021   1520   -156    550   -168       C  
+ATOM    532  C   VAL A  82      23.537  17.013  33.547  1.00 19.41           C  
+ANISOU  532  C   VAL A  82     3021   2346   2009   -166    510   -228       C  
+ATOM    533  O   VAL A  82      24.529  16.871  34.259  1.00 16.30           O  
+ANISOU  533  O   VAL A  82     2525   1934   1733   -171    566   -209       O  
+ATOM    534  CB  VAL A  82      22.151  19.102  33.548  1.00 16.30           C  
+ANISOU  534  CB  VAL A  82     2670   2008   1516   -204    433   -124       C  
+ATOM    535  CG1 VAL A  82      22.454  19.149  35.045  1.00 15.43           C  
+ANISOU  535  CG1 VAL A  82     2424   1880   1557   -255    414    -95       C  
+ATOM    536  CG2 VAL A  82      22.050  20.529  32.978  1.00 20.86           C  
+ANISOU  536  CG2 VAL A  82     3317   2604   2007   -187    484    -44       C  
+ATOM    537  N   ARG A  83      22.650  16.045  33.348  1.00 17.30           N  
+ANISOU  537  N   ARG A  83     2798   2048   1725   -163    404   -305       N  
+ATOM    538  CA  ARG A  83      22.822  14.731  33.967  1.00 17.88           C  
+ANISOU  538  CA  ARG A  83     2822   2050   1923   -168    377   -349       C  
+ATOM    539  C   ARG A  83      24.142  14.104  33.548  1.00 19.89           C  
+ANISOU  539  C   ARG A  83     3081   2281   2197   -102    491   -390       C  
+ATOM    540  O   ARG A  83      24.858  13.559  34.386  1.00 19.69           O  
+ANISOU  540  O   ARG A  83     2970   2215   2297    -91    511   -370       O  
+ATOM    541  CB  ARG A  83      21.654  13.828  33.612  1.00 14.37           C  
+ANISOU  541  CB  ARG A  83     2421   1549   1488   -186    257   -440       C  
+ATOM    542  CG  ARG A  83      20.359  14.326  34.278  1.00 13.66           C  
+ANISOU  542  CG  ARG A  83     2272   1472   1445   -255    160   -393       C  
+ATOM    543  CD  ARG A  83      19.229  13.328  34.139  1.00 14.53           C  
+ANISOU  543  CD  ARG A  83     2367   1501   1651   -297     49   -483       C  
+ATOM    544  NE  ARG A  83      18.029  13.808  34.848  1.00 18.04           N  
+ANISOU  544  NE  ARG A  83     2721   1958   2175   -362    -11   -430       N  
+ATOM    545  CZ  ARG A  83      16.911  13.100  34.987  1.00 19.66           C  
+ANISOU  545  CZ  ARG A  83     2856   2086   2528   -424    -89   -482       C  
+ATOM    546  NH1 ARG A  83      16.828  11.866  34.489  1.00 19.79           N  
+ANISOU  546  NH1 ARG A  83     2890   1992   2636   -438   -136   -599       N  
+ATOM    547  NH2 ARG A  83      15.875  13.626  35.643  1.00 19.35           N  
+ANISOU  547  NH2 ARG A  83     2715   2067   2569   -473   -111   -425       N  
+ATOM    548  N   TYR A  84      24.474  14.221  32.266  1.00 19.04           N  
+ANISOU  548  N   TYR A  84     3078   2203   1955    -40    571   -442       N  
+ATOM    549  CA  TYR A  84      25.732  13.680  31.777  1.00 16.91           C  
+ANISOU  549  CA  TYR A  84     2806   1916   1701     37    714   -484       C  
+ATOM    550  C   TYR A  84      26.906  14.418  32.415  1.00 24.42           C  
+ANISOU  550  C   TYR A  84     3613   2892   2773     22    831   -394       C  
+ATOM    551  O   TYR A  84      27.861  13.792  32.870  1.00 21.23           O  
+ANISOU  551  O   TYR A  84     3106   2453   2506     57    875   -412       O  
+ATOM    552  CB  TYR A  84      25.828  13.753  30.252  1.00 21.25           C  
+ANISOU  552  CB  TYR A  84     3521   2504   2047    125    806   -548       C  
+ATOM    553  CG  TYR A  84      27.169  13.240  29.772  1.00 21.41           C  
+ANISOU  553  CG  TYR A  84     3528   2512   2096    213    994   -586       C  
+ATOM    554  CD1 TYR A  84      27.417  11.874  29.680  1.00 20.80           C  
+ANISOU  554  CD1 TYR A  84     3466   2359   2078    275    972   -708       C  
+ATOM    555  CD2 TYR A  84      28.207  14.116  29.483  1.00 20.59           C  
+ANISOU  555  CD2 TYR A  84     3372   2453   1999    231   1205   -499       C  
+ATOM    556  CE1 TYR A  84      28.646  11.409  29.277  1.00 25.73           C  
+ANISOU  556  CE1 TYR A  84     4061   2971   2745    370   1151   -748       C  
+ATOM    557  CE2 TYR A  84      29.438  13.662  29.089  1.00 22.14           C  
+ANISOU  557  CE2 TYR A  84     3516   2638   2257    311   1394   -532       C  
+ATOM    558  CZ  TYR A  84      29.652  12.310  28.985  1.00 25.98           C  
+ANISOU  558  CZ  TYR A  84     4024   3065   2781    389   1367   -660       C  
+ATOM    559  OH  TYR A  84      30.874  11.857  28.595  1.00 26.63           O  
+ANISOU  559  OH  TYR A  84     4023   3148   2949    471   1512   -680       O  
+ATOM    560  N   GLU A  85      26.849  15.751  32.428  1.00 18.26           N  
+ANISOU  560  N   GLU A  85     2816   2162   1961    -25    872   -306       N  
+ATOM    561  CA  GLU A  85      27.959  16.515  32.981  1.00 16.41           C  
+ANISOU  561  CA  GLU A  85     2427   1933   1877    -53    971   -244       C  
+ATOM    562  C   GLU A  85      28.230  16.129  34.442  1.00 15.33           C  
+ANISOU  562  C   GLU A  85     2143   1771   1910    -74    848   -247       C  
+ATOM    563  O   GLU A  85      29.379  16.028  34.859  1.00 21.85           O  
+ANISOU  563  O   GLU A  85     2827   2586   2891    -51    896   -258       O  
+ATOM    564  CB  GLU A  85      27.687  18.008  32.843  1.00 19.54           C  
+ANISOU  564  CB  GLU A  85     2838   2353   2233   -110   1012   -154       C  
+ATOM    565  CG  GLU A  85      27.856  18.473  31.402  1.00 26.55           C  
+ANISOU  565  CG  GLU A  85     3864   3258   2965    -61   1193   -119       C  
+ATOM    566  CD  GLU A  85      27.197  19.805  31.123  1.00 29.36           C  
+ANISOU  566  CD  GLU A  85     4304   3622   3229    -94   1199    -21       C  
+ATOM    567  OE1 GLU A  85      26.523  20.349  32.026  1.00 24.75           O  
+ANISOU  567  OE1 GLU A  85     3668   3033   2705   -158   1053      1       O  
+ATOM    568  OE2 GLU A  85      27.360  20.302  29.990  1.00 30.14           O  
+ANISOU  568  OE2 GLU A  85     4510   3729   3214    -39   1307     38       O  
+ATOM    569  N   ILE A  86      27.168  15.873  35.195  1.00 17.09           N  
+ANISOU  569  N   ILE A  86     2405   1987   2103   -105    693   -237       N  
+ATOM    570  CA  ILE A  86      27.306  15.446  36.573  1.00 14.57           C  
+ANISOU  570  CA  ILE A  86     1998   1647   1890    -99    584   -222       C  
+ATOM    571  C   ILE A  86      27.927  14.047  36.659  1.00 18.86           C  
+ANISOU  571  C   ILE A  86     2525   2132   2509    -20    587   -268       C  
+ATOM    572  O   ILE A  86      28.883  13.809  37.413  1.00 17.50           O  
+ANISOU  572  O   ILE A  86     2242   1951   2457     32    563   -268       O  
+ATOM    573  CB  ILE A  86      25.945  15.445  37.290  1.00 13.88           C  
+ANISOU  573  CB  ILE A  86     1971   1558   1745   -142    466   -184       C  
+ATOM    574  CG1 ILE A  86      25.471  16.891  37.501  1.00 15.67           C  
+ANISOU  574  CG1 ILE A  86     2188   1836   1929   -198    448   -139       C  
+ATOM    575  CG2 ILE A  86      26.061  14.737  38.633  1.00 19.56           C  
+ANISOU  575  CG2 ILE A  86     2651   2247   2535   -104    383   -153       C  
+ATOM    576  CD1 ILE A  86      23.990  17.001  37.904  1.00 15.96           C  
+ANISOU  576  CD1 ILE A  86     2282   1880   1902   -235    365   -110       C  
+HETATM  577  N   MSE A  87      27.387  13.114  35.889  1.00 15.88           N  
+ANISOU  577  N   MSE A  87     2257   1706   2072     -1    599   -321       N  
+HETATM  578  CA  MSE A  87      27.882  11.736  35.981  1.00 18.17           C  
+ANISOU  578  CA  MSE A  87     2546   1911   2447     77    598   -369       C  
+HETATM  579  C   MSE A  87      29.328  11.647  35.519  1.00 18.99           C  
+ANISOU  579  C   MSE A  87     2560   2025   2630    158    718   -413       C  
+HETATM  580  O   MSE A  87      30.133  10.931  36.125  1.00 21.78           O  
+ANISOU  580  O   MSE A  87     2830   2333   3111    236    696   -420       O  
+HETATM  581  CB  MSE A  87      27.007  10.793  35.170  1.00 16.38           C  
+ANISOU  581  CB  MSE A  87     2452   1610   2162     76    578   -447       C  
+HETATM  582  CG  MSE A  87      25.596  10.654  35.758  1.00 18.15           C  
+ANISOU  582  CG  MSE A  87     2718   1795   2382     -6    463   -408       C  
+HETATM  583 SE   MSE A  87      25.684   9.802  37.546  1.00 26.29          SE  
+ANISOU  583 SE   MSE A  87     3697   2734   3559     21    403   -293      SE  
+HETATM  584  CE  MSE A  87      24.166   8.556  37.360  1.00 21.50           C  
+ANISOU  584  CE  MSE A  87     3179   1964   3028    -51    354   -329       C  
+ATOM    585  N   LYS A  88      29.656  12.360  34.442  1.00 23.23           N  
+ANISOU  585  N   LYS A  88     3112   2618   3096    151    855   -435       N  
+ATOM    586  CA  LYS A  88      31.022  12.350  33.919  1.00 22.85           C  
+ANISOU  586  CA  LYS A  88     2960   2581   3142    222   1019   -469       C  
+ATOM    587  C   LYS A  88      31.964  13.003  34.922  1.00 20.27           C  
+ANISOU  587  C   LYS A  88     2420   2279   3002    207    993   -425       C  
+ATOM    588  O   LYS A  88      33.112  12.591  35.056  1.00 22.20           O  
+ANISOU  588  O   LYS A  88     2519   2508   3410    284   1044   -463       O  
+ATOM    589  CB  LYS A  88      31.102  13.068  32.570  1.00 19.96           C  
+ANISOU  589  CB  LYS A  88     2678   2265   2641    220   1206   -471       C  
+ATOM    590  CG  LYS A  88      32.504  13.095  31.963  1.00 24.91           C  
+ANISOU  590  CG  LYS A  88     3189   2901   3375    292   1433   -494       C  
+ATOM    591  CD  LYS A  88      33.017  11.700  31.592  1.00 28.38           C  
+ANISOU  591  CD  LYS A  88     3649   3285   3849    420   1478   -601       C  
+ATOM    592  CE  LYS A  88      34.453  11.776  31.101  1.00 37.36           C  
+ANISOU  592  CE  LYS A  88     4630   4439   5127    492   1702   -614       C  
+ATOM    593  NZ  LYS A  88      35.065  10.428  30.942  1.00 41.55           N  
+ANISOU  593  NZ  LYS A  88     5143   4914   5728    623   1705   -711       N  
+ATOM    594  N   SER A  89      31.470  14.025  35.621  1.00 20.02           N  
+ANISOU  594  N   SER A  89     2365   2285   2956    118    900   -362       N  
+ATOM    595  CA  SER A  89      32.255  14.689  36.662  1.00 22.91           C  
+ANISOU  595  CA  SER A  89     2541   2672   3494    104    825   -350       C  
+ATOM    596  C   SER A  89      32.640  13.731  37.788  1.00 22.63           C  
+ANISOU  596  C   SER A  89     2442   2607   3549    198    665   -369       C  
+ATOM    597  O   SER A  89      33.749  13.804  38.305  1.00 23.93           O  
+ANISOU  597  O   SER A  89     2422   2779   3893    251    628   -405       O  
+ATOM    598  CB  SER A  89      31.493  15.889  37.232  1.00 22.68           C  
+ANISOU  598  CB  SER A  89     2537   2675   3404      5    736   -297       C  
+ATOM    599  OG  SER A  89      31.523  16.969  36.312  1.00 23.30           O  
+ANISOU  599  OG  SER A  89     2623   2766   3463    -67    891   -268       O  
+ATOM    600  N   ILE A  90      31.728  12.837  38.169  1.00 22.76           N  
+ANISOU  600  N   ILE A  90     2608   2583   3456    225    571   -341       N  
+ATOM    601  CA  ILE A  90      32.055  11.836  39.182  1.00 19.42           C  
+ANISOU  601  CA  ILE A  90     2167   2114   3099    335    443   -330       C  
+ATOM    602  C   ILE A  90      33.155  10.891  38.678  1.00 22.75           C  
+ANISOU  602  C   ILE A  90     2504   2484   3655    451    518   -396       C  
+ATOM    603  O   ILE A  90      34.148  10.647  39.377  1.00 24.53           O  
+ANISOU  603  O   ILE A  90     2587   2708   4023    554    435   -415       O  
+ATOM    604  CB  ILE A  90      30.811  11.007  39.601  1.00 17.44           C  
+ANISOU  604  CB  ILE A  90     2099   1797   2730    330    376   -267       C  
+ATOM    605  CG1 ILE A  90      29.738  11.915  40.207  1.00 22.66           C  
+ANISOU  605  CG1 ILE A  90     2823   2512   3275    236    312   -203       C  
+ATOM    606  CG2 ILE A  90      31.206   9.921  40.590  1.00 22.82           C  
+ANISOU  606  CG2 ILE A  90     2789   2407   3474    462    275   -228       C  
+ATOM    607  CD1 ILE A  90      28.452  11.174  40.583  1.00 24.77           C  
+ANISOU  607  CD1 ILE A  90     3239   2711   3463    212    283   -134       C  
+ATOM    608  N   GLU A  91      32.987  10.360  37.472  1.00 20.23           N  
+ANISOU  608  N   GLU A  91     2271   2124   3290    451    663   -444       N  
+ATOM    609  CA  GLU A  91      34.002   9.458  36.909  1.00 22.01           C  
+ANISOU  609  CA  GLU A  91     2428   2298   3638    574    761   -520       C  
+ATOM    610  C   GLU A  91      35.393  10.100  36.874  1.00 23.35           C  
+ANISOU  610  C   GLU A  91     2349   2528   3997    610    837   -558       C  
+ATOM    611  O   GLU A  91      36.398   9.424  37.122  1.00 25.46           O  
+ANISOU  611  O   GLU A  91     2480   2760   4433    739    823   -603       O  
+ATOM    612  CB  GLU A  91      33.626   8.995  35.499  1.00 24.36           C  
+ANISOU  612  CB  GLU A  91     2870   2561   3823    574    920   -591       C  
+ATOM    613  CG  GLU A  91      34.582   7.905  34.975  1.00 30.09           C  
+ANISOU  613  CG  GLU A  91     3553   3215   4664    724   1020   -682       C  
+ATOM    614  CD  GLU A  91      34.230   7.385  33.584  1.00 42.29           C  
+ANISOU  614  CD  GLU A  91     5269   4726   6075    751   1165   -781       C  
+ATOM    615  OE1 GLU A  91      33.379   8.001  32.907  1.00 46.05           O  
+ANISOU  615  OE1 GLU A  91     5879   5253   6365    659   1199   -777       O  
+ATOM    616  OE2 GLU A  91      34.807   6.347  33.168  1.00 46.58           O  
+ANISOU  616  OE2 GLU A  91     5820   5187   6690    883   1233   -872       O  
+ATOM    617  N   LYS A  92      35.453  11.401  36.578  1.00 24.97           N  
+ANISOU  617  N   LYS A  92     2482   2807   4200    498    918   -539       N  
+ATOM    618  CA  LYS A  92      36.736  12.111  36.474  1.00 26.23           C  
+ANISOU  618  CA  LYS A  92     2378   3002   4586    499   1019   -575       C  
+ATOM    619  C   LYS A  92      37.316  12.545  37.830  1.00 27.05           C  
+ANISOU  619  C   LYS A  92     2284   3129   4864    513    798   -586       C  
+ATOM    620  O   LYS A  92      38.489  12.935  37.921  1.00 28.34           O  
+ANISOU  620  O   LYS A  92     2182   3305   5282    533    829   -643       O  
+ATOM    621  CB  LYS A  92      36.592  13.348  35.574  1.00 24.52           C  
+ANISOU  621  CB  LYS A  92     2170   2825   4322    370   1217   -539       C  
+ATOM    622  N   GLY A  93      36.499  12.488  38.876  1.00 26.24           N  
+ANISOU  622  N   GLY A  93     2307   3032   4630    510    578   -539       N  
+ATOM    623  CA  GLY A  93      36.945  12.861  40.205  1.00 29.22           C  
+ANISOU  623  CA  GLY A  93     2552   3442   5110    553    340   -560       C  
+ATOM    624  C   GLY A  93      36.895  14.356  40.491  1.00 24.77           C  
+ANISOU  624  C   GLY A  93     1896   2924   4591    419    304   -574       C  
+ATOM    625  O   GLY A  93      37.633  14.855  41.351  1.00 27.93           O  
+ANISOU  625  O   GLY A  93     2107   3348   5155    448    133   -643       O  
+ATOM    626  N   ASN A  94      36.036  15.082  39.780  1.00 22.13           N  
+ANISOU  626  N   ASN A  94     1692   2595   4121    284    445   -520       N  
+ATOM    627  CA  ASN A  94      35.845  16.506  40.084  1.00 21.73           C  
+ANISOU  627  CA  ASN A  94     1588   2564   4103    161    407   -523       C  
+ATOM    628  C   ASN A  94      35.129  16.680  41.407  1.00 23.18           C  
+ANISOU  628  C   ASN A  94     1878   2780   4149    187    156   -514       C  
+ATOM    629  O   ASN A  94      34.273  15.865  41.763  1.00 23.62           O  
+ANISOU  629  O   ASN A  94     2129   2839   4006    247     94   -451       O  
+ATOM    630  CB  ASN A  94      35.016  17.210  39.011  1.00 20.61           C  
+ANISOU  630  CB  ASN A  94     1591   2413   3825     37    608   -451       C  
+ATOM    631  CG  ASN A  94      35.861  17.800  37.900  1.00 23.94           C  
+ANISOU  631  CG  ASN A  94     1871   2806   4420    -25    865   -454       C  
+ATOM    632  OD1 ASN A  94      37.012  17.400  37.678  1.00 28.79           O  
+ANISOU  632  OD1 ASN A  94     2288   3406   5247     30    949   -509       O  
+ATOM    633  ND2 ASN A  94      35.282  18.754  37.185  1.00 21.74           N  
+ANISOU  633  ND2 ASN A  94     1695   2513   4052   -130   1008   -384       N  
+ATOM    634  N   LYS A  95      35.459  17.755  42.117  1.00 22.43           N  
+ANISOU  634  N   LYS A  95     1659   2698   4165    142     27   -580       N  
+ATOM    635  CA  LYS A  95      34.592  18.244  43.177  1.00 23.16           C  
+ANISOU  635  CA  LYS A  95     1890   2824   4084    146   -156   -571       C  
+ATOM    636  C   LYS A  95      33.270  18.677  42.542  1.00 25.64           C  
+ANISOU  636  C   LYS A  95     2405   3133   4204     39    -13   -474       C  
+ATOM    637  O   LYS A  95      33.264  19.271  41.464  1.00 28.66           O  
+ANISOU  637  O   LYS A  95     2762   3483   4644    -66    176   -450       O  
+ATOM    638  CB  LYS A  95      35.261  19.405  43.908  1.00 21.73           C  
+ANISOU  638  CB  LYS A  95     1529   2644   4085    112   -315   -694       C  
+ATOM    639  CG  LYS A  95      34.437  20.025  45.016  1.00 25.71           C  
+ANISOU  639  CG  LYS A  95     2178   3183   4406    132   -500   -711       C  
+ATOM    640  CD  LYS A  95      35.236  21.117  45.688  1.00 32.29           C  
+ANISOU  640  CD  LYS A  95     2816   4000   5452    107   -680   -874       C  
+ATOM    641  CE  LYS A  95      34.546  21.608  46.941  1.00 31.43           C  
+ANISOU  641  CE  LYS A  95     2864   3938   5139    176   -898   -923       C  
+ATOM    642  NZ  LYS A  95      35.521  22.437  47.708  1.00 36.60           N  
+ANISOU  642  NZ  LYS A  95     3313   4576   6016    192  -1140  -1126       N  
+ATOM    643  N   ILE A  96      32.148  18.373  43.185  1.00 17.21           N  
+ANISOU  643  N   ILE A  96     1535   2094   2911     76    -94   -412       N  
+ATOM    644  CA  ILE A  96      30.861  18.702  42.590  1.00 15.57           C  
+ANISOU  644  CA  ILE A  96     1491   1882   2543    -11     20   -332       C  
+ATOM    645  C   ILE A  96      29.960  19.374  43.617  1.00 20.49           C  
+ANISOU  645  C   ILE A  96     2215   2538   3031     -8   -100   -324       C  
+ATOM    646  O   ILE A  96      29.741  18.826  44.706  1.00 19.08           O  
+ANISOU  646  O   ILE A  96     2112   2390   2746     96   -227   -310       O  
+ATOM    647  CB  ILE A  96      30.130  17.447  42.038  1.00 16.46           C  
+ANISOU  647  CB  ILE A  96     1748   1978   2527     18    106   -256       C  
+ATOM    648  CG1 ILE A  96      30.991  16.700  41.026  1.00 18.45           C  
+ANISOU  648  CG1 ILE A  96     1927   2197   2888     40    229   -280       C  
+ATOM    649  CG2 ILE A  96      28.813  17.857  41.406  1.00 19.63           C  
+ANISOU  649  CG2 ILE A  96     2286   2381   2793    -69    190   -199       C  
+ATOM    650  CD1 ILE A  96      30.523  15.279  40.750  1.00 22.19           C  
+ANISOU  650  CD1 ILE A  96     2523   2632   3278    100    259   -244       C  
+ATOM    651  N   ILE A  97      29.449  20.561  43.281  1.00 17.38           N  
+ANISOU  651  N   ILE A  97     1836   2132   2637   -105    -49   -325       N  
+ATOM    652  CA  ILE A  97      28.460  21.217  44.118  1.00 15.54           C  
+ANISOU  652  CA  ILE A  97     1709   1925   2269    -97   -130   -318       C  
+ATOM    653  C   ILE A  97      27.271  21.697  43.293  1.00 16.15           C  
+ANISOU  653  C   ILE A  97     1889   1989   2259   -179     -7   -245       C  
+ATOM    654  O   ILE A  97      27.351  21.828  42.065  1.00 18.92           O  
+ANISOU  654  O   ILE A  97     2226   2307   2656   -246    124   -214       O  
+ATOM    655  CB  ILE A  97      29.041  22.419  44.894  1.00 19.12           C  
+ANISOU  655  CB  ILE A  97     2069   2369   2827   -103   -262   -433       C  
+ATOM    656  CG1 ILE A  97      29.506  23.530  43.930  1.00 17.40           C  
+ANISOU  656  CG1 ILE A  97     1736   2072   2802   -231   -150   -459       C  
+ATOM    657  CG2 ILE A  97      30.164  21.970  45.810  1.00 20.79           C  
+ANISOU  657  CG2 ILE A  97     2176   2606   3116      2   -438   -528       C  
+ATOM    658  CD1 ILE A  97      29.986  24.787  44.640  1.00 19.39           C  
+ANISOU  658  CD1 ILE A  97     1890   2278   3200   -259   -277   -586       C  
+ATOM    659  N   GLY A  98      26.163  21.949  43.978  1.00 16.90           N  
+ANISOU  659  N   GLY A  98     2090   2113   2217   -155    -50   -218       N  
+ATOM    660  CA  GLY A  98      25.014  22.575  43.340  1.00 17.13           C  
+ANISOU  660  CA  GLY A  98     2191   2131   2185   -214     30   -168       C  
+ATOM    661  C   GLY A  98      24.758  23.943  43.958  1.00 15.90           C  
+ANISOU  661  C   GLY A  98     2038   1964   2041   -220    -30   -220       C  
+ATOM    662  O   GLY A  98      25.020  24.150  45.146  1.00 17.29           O  
+ANISOU  662  O   GLY A  98     2212   2165   2194   -154   -146   -289       O  
+ATOM    663  N   ILE A  99      24.252  24.882  43.157  1.00 15.87           N  
+ANISOU  663  N   ILE A  99     2053   1917   2062   -283     41   -193       N  
+ATOM    664  CA  ILE A  99      23.892  26.227  43.659  1.00 16.53           C  
+ANISOU  664  CA  ILE A  99     2150   1963   2169   -285     -4   -242       C  
+ATOM    665  C   ILE A  99      22.549  26.612  43.056  1.00 16.68           C  
+ANISOU  665  C   ILE A  99     2253   1980   2104   -292     60   -167       C  
+ATOM    666  O   ILE A  99      22.442  26.743  41.841  1.00 15.95           O  
+ANISOU  666  O   ILE A  99     2178   1854   2028   -336    144   -103       O  
+ATOM    667  CB  ILE A  99      24.942  27.317  43.283  1.00 15.85           C  
+ANISOU  667  CB  ILE A  99     1968   1774   2280   -358      9   -298       C  
+ATOM    668  CG1 ILE A  99      26.328  26.971  43.840  1.00 18.99           C  
+ANISOU  668  CG1 ILE A  99     2235   2170   2809   -353    -75   -395       C  
+ATOM    669  CG2 ILE A  99      24.533  28.671  43.853  1.00 16.30           C  
+ANISOU  669  CG2 ILE A  99     2050   1768   2376   -356    -49   -363       C  
+ATOM    670  CD1 ILE A  99      27.428  27.940  43.404  1.00 22.03           C  
+ANISOU  670  CD1 ILE A  99     2480   2438   3454   -447    -37   -452       C  
+ATOM    671  N   HIS A 100      21.525  26.788  43.895  1.00 12.98           N  
+ANISOU  671  N   HIS A 100     1839   1552   1542   -231     21   -176       N  
+ATOM    672  CA  HIS A 100      20.247  27.291  43.422  1.00 17.52           C  
+ANISOU  672  CA  HIS A 100     2461   2122   2075   -224     62   -124       C  
+ATOM    673  C   HIS A 100      20.433  28.733  42.965  1.00 16.69           C  
+ANISOU  673  C   HIS A 100     2360   1918   2064   -252     70   -141       C  
+ATOM    674  O   HIS A 100      21.074  29.534  43.654  1.00 16.10           O  
+ANISOU  674  O   HIS A 100     2261   1787   2070   -253     17   -229       O  
+ATOM    675  CB  HIS A 100      19.173  27.192  44.518  1.00 13.76           C  
+ANISOU  675  CB  HIS A 100     2019   1705   1503   -145     47   -134       C  
+ATOM    676  CG  HIS A 100      18.742  25.786  44.812  1.00 17.02           C  
+ANISOU  676  CG  HIS A 100     2436   2186   1845   -127     81    -78       C  
+ATOM    677  ND1 HIS A 100      17.880  25.088  43.996  1.00 15.10           N  
+ANISOU  677  ND1 HIS A 100     2177   1954   1608   -160    130    -13       N  
+ATOM    678  CD2 HIS A 100      19.062  24.948  45.831  1.00 18.45           C  
+ANISOU  678  CD2 HIS A 100     2641   2412   1958    -74     71    -78       C  
+ATOM    679  CE1 HIS A 100      17.681  23.879  44.500  1.00 18.99           C  
+ANISOU  679  CE1 HIS A 100     2669   2477   2069   -148    163     26       C  
+ATOM    680  NE2 HIS A 100      18.388  23.769  45.612  1.00 16.85           N  
+ANISOU  680  NE2 HIS A 100     2435   2227   1742    -89    139      3       N  
+ATOM    681  N   ILE A 101      19.882  29.056  41.798  1.00 15.19           N  
+ANISOU  681  N   ILE A 101     2208   1695   1868   -268    126    -61       N  
+ATOM    682  CA  ILE A 101      20.014  30.399  41.244  1.00 15.78           C  
+ANISOU  682  CA  ILE A 101     2312   1654   2030   -286    157    -41       C  
+ATOM    683  C   ILE A 101      18.655  31.038  40.949  1.00 18.62           C  
+ANISOU  683  C   ILE A 101     2733   2006   2337   -220    145      4       C  
+ATOM    684  O   ILE A 101      18.547  31.868  40.048  1.00 17.00           O  
+ANISOU  684  O   ILE A 101     2586   1714   2159   -215    184     74       O  
+ATOM    685  CB  ILE A 101      20.849  30.384  39.936  1.00 16.93           C  
+ANISOU  685  CB  ILE A 101     2471   1742   2218   -345    259     40       C  
+ATOM    686  CG1 ILE A 101      20.274  29.339  38.967  1.00 19.53           C  
+ANISOU  686  CG1 ILE A 101     2855   2160   2407   -319    281    109       C  
+ATOM    687  CG2 ILE A 101      22.313  30.137  40.255  1.00 18.33           C  
+ANISOU  687  CG2 ILE A 101     2550   1889   2523   -412    281    -18       C  
+ATOM    688  CD1 ILE A 101      20.957  29.325  37.618  1.00 24.80           C  
+ANISOU  688  CD1 ILE A 101     3578   2787   3060   -342    397    191       C  
+ATOM    689  N   ASN A 102      17.626  30.664  41.714  1.00 16.51           N  
+ANISOU  689  N   ASN A 102     2450   1822   2000   -159    100    -28       N  
+ATOM    690  CA  ASN A 102      16.280  31.190  41.461  1.00 18.76           C  
+ANISOU  690  CA  ASN A 102     2756   2110   2263    -85     83      3       C  
+ATOM    691  C   ASN A 102      15.832  32.300  42.419  1.00 16.47           C  
+ANISOU  691  C   ASN A 102     2473   1769   2017    -18     63    -66       C  
+ATOM    692  O   ASN A 102      14.782  32.917  42.198  1.00 18.80           O  
+ANISOU  692  O   ASN A 102     2777   2046   2320     56     51    -44       O  
+ATOM    693  CB  ASN A 102      15.249  30.054  41.492  1.00 16.18           C  
+ANISOU  693  CB  ASN A 102     2379   1897   1870    -62     72     20       C  
+ATOM    694  CG  ASN A 102      15.049  29.400  40.117  1.00 16.37           C  
+ANISOU  694  CG  ASN A 102     2421   1945   1854    -82     55     81       C  
+ATOM    695  OD1 ASN A 102      15.747  29.725  39.152  1.00 16.98           O  
+ANISOU  695  OD1 ASN A 102     2569   1969   1915   -103     74    127       O  
+ATOM    696  ND2 ASN A 102      14.101  28.467  40.032  1.00 16.10           N  
+ANISOU  696  ND2 ASN A 102     2325   1984   1808    -73     25     77       N  
+ATOM    697  N   ALA A 103      16.629  32.566  43.455  1.00 14.60           N  
+ANISOU  697  N   ALA A 103     2232   1505   1810    -29     44   -162       N  
+ATOM    698  CA  ALA A 103      16.211  33.441  44.551  1.00 15.55           C  
+ANISOU  698  CA  ALA A 103     2373   1596   1940     53     15   -264       C  
+ATOM    699  C   ALA A 103      16.498  34.911  44.308  1.00 18.23           C  
+ANISOU  699  C   ALA A 103     2751   1763   2412     53     -2   -299       C  
+ATOM    700  O   ALA A 103      16.080  35.759  45.097  1.00 21.05           O  
+ANISOU  700  O   ALA A 103     3137   2072   2790    133    -29   -394       O  
+ATOM    701  CB  ALA A 103      16.873  33.006  45.850  1.00 15.56           C  
+ANISOU  701  CB  ALA A 103     2374   1656   1882     71    -26   -373       C  
+ATOM    702  N   PHE A 104      17.232  35.210  43.241  1.00 21.62           N  
+ANISOU  702  N   PHE A 104     3190   2090   2935    -32     30   -221       N  
+ATOM    703  CA  PHE A 104      17.480  36.598  42.861  1.00 20.45           C  
+ANISOU  703  CA  PHE A 104     3086   1745   2938    -42     46   -216       C  
+ATOM    704  C   PHE A 104      16.717  36.900  41.574  1.00 20.28           C  
+ANISOU  704  C   PHE A 104     3132   1687   2888      2     96    -56       C  
+ATOM    705  O   PHE A 104      16.188  35.998  40.943  1.00 19.50           O  
+ANISOU  705  O   PHE A 104     3031   1716   2664     21    100     26       O  
+ATOM    706  CB  PHE A 104      18.985  36.865  42.698  1.00 18.19           C  
+ANISOU  706  CB  PHE A 104     2759   1336   2815   -168     70   -244       C  
+ATOM    707  CG  PHE A 104      19.683  35.931  41.728  1.00 19.26           C  
+ANISOU  707  CG  PHE A 104     2867   1531   2920   -250    149   -131       C  
+ATOM    708  CD1 PHE A 104      19.662  36.176  40.365  1.00 25.13           C  
+ANISOU  708  CD1 PHE A 104     3679   2205   3665   -266    256     33       C  
+ATOM    709  CD2 PHE A 104      20.404  34.838  42.188  1.00 21.94           C  
+ANISOU  709  CD2 PHE A 104     3127   1987   3221   -294    118   -191       C  
+ATOM    710  CE1 PHE A 104      20.310  35.332  39.484  1.00 22.74           C  
+ANISOU  710  CE1 PHE A 104     3367   1959   3314   -322    342    122       C  
+ATOM    711  CE2 PHE A 104      21.061  33.986  41.301  1.00 21.37           C  
+ANISOU  711  CE2 PHE A 104     3030   1961   3131   -357    198   -101       C  
+ATOM    712  CZ  PHE A 104      21.008  34.236  39.948  1.00 18.52           C  
+ANISOU  712  CZ  PHE A 104     2738   1538   2761   -371    316     49       C  
+ATOM    713  N   LYS A 105      16.652  38.170  41.183  1.00 21.54           N  
+ANISOU  713  N   LYS A 105     3358   1661   3164     28    120    -16       N  
+ATOM    714  CA  LYS A 105      15.865  38.540  40.009  1.00 20.18           C  
+ANISOU  714  CA  LYS A 105     3276   1452   2941    109    145    141       C  
+ATOM    715  C   LYS A 105      16.525  38.110  38.699  1.00 23.40           C  
+ANISOU  715  C   LYS A 105     3742   1856   3294     48    231    295       C  
+ATOM    716  O   LYS A 105      17.724  38.286  38.523  1.00 25.47           O  
+ANISOU  716  O   LYS A 105     3996   2014   3667    -63    323    314       O  
+ATOM    717  CB  LYS A 105      15.624  40.058  39.990  1.00 21.06           C  
+ANISOU  717  CB  LYS A 105     3464   1342   3196    173    155    155       C  
+ATOM    718  CG  LYS A 105      14.686  40.542  41.087  1.00 24.24           C  
+ANISOU  718  CG  LYS A 105     3836   1756   3619    285     76     16       C  
+ATOM    719  CD  LYS A 105      14.463  42.059  40.992  1.00 30.52           C  
+ANISOU  719  CD  LYS A 105     4718   2305   4573    357     86     29       C  
+ATOM    720  CE  LYS A 105      13.222  42.498  41.770  1.00 37.13           C  
+ANISOU  720  CE  LYS A 105     5537   3174   5397    520     20    -75       C  
+ATOM    721  NZ  LYS A 105      12.998  43.973  41.655  1.00 44.87           N  
+ANISOU  721  NZ  LYS A 105     6609   3895   6543    606     26    -65       N  
+ATOM    722  N   ASP A 106      15.743  37.533  37.786  1.00 21.91           N  
+ANISOU  722  N   ASP A 106     3605   1781   2940    127    202    393       N  
+ATOM    723  CA  ASP A 106      16.236  37.288  36.436  1.00 24.66           C  
+ANISOU  723  CA  ASP A 106     4059   2116   3195    115    286    544       C  
+ATOM    724  C   ASP A 106      16.110  38.566  35.622  1.00 28.54           C  
+ANISOU  724  C   ASP A 106     4703   2418   3723    194    347    693       C  
+ATOM    725  O   ASP A 106      15.791  39.637  36.173  1.00 23.35           O  
+ANISOU  725  O   ASP A 106     4051   1618   3204    234    326    664       O  
+ATOM    726  CB  ASP A 106      15.484  36.133  35.757  1.00 18.17           C  
+ANISOU  726  CB  ASP A 106     3248   1487   2171    181    202    562       C  
+ATOM    727  CG  ASP A 106      13.971  36.320  35.763  1.00 25.12           C  
+ANISOU  727  CG  ASP A 106     4117   2427   3001    325     57    545       C  
+ATOM    728  OD1 ASP A 106      13.495  37.478  35.763  1.00 22.37           O  
+ANISOU  728  OD1 ASP A 106     3826   1955   2718    416     42    588       O  
+ATOM    729  OD2 ASP A 106      13.258  35.289  35.734  1.00 27.09           O  
+ANISOU  729  OD2 ASP A 106     4290   2837   3166    347    -39    486       O  
+ATOM    730  N   LYS A 107      16.344  38.474  34.314  1.00 22.04           N  
+ANISOU  730  N   LYS A 107     4024   1583   2766    234    428    857       N  
+ATOM    731  CA  LYS A 107      16.373  39.686  33.504  1.00 24.38           C  
+ANISOU  731  CA  LYS A 107     4451   1722   3092    300    503   1007       C  
+ATOM    732  C   LYS A 107      14.977  40.287  33.309  1.00 25.28           C  
+ANISOU  732  C   LYS A 107     4645   1827   3135    490    357   1044       C  
+ATOM    733  O   LYS A 107      14.854  41.440  32.881  1.00 27.35           O  
+ANISOU  733  O   LYS A 107     4976   1958   3457    547    385   1134       O  
+ATOM    734  CB  LYS A 107      17.031  39.421  32.139  1.00 28.10           C  
+ANISOU  734  CB  LYS A 107     4997   2261   3417    295    614   1125       C  
+ATOM    735  CG  LYS A 107      16.197  38.600  31.168  1.00 31.03           C  
+ANISOU  735  CG  LYS A 107     5468   2816   3507    435    502   1157       C  
+ATOM    736  CD  LYS A 107      16.998  38.296  29.894  1.00 33.92           C  
+ANISOU  736  CD  LYS A 107     5916   3238   3735    431    634   1241       C  
+ATOM    737  CE  LYS A 107      16.123  37.714  28.793  1.00 34.47           C  
+ANISOU  737  CE  LYS A 107     6109   3461   3527    594    502   1259       C  
+ATOM    738  NZ  LYS A 107      16.907  37.317  27.581  1.00 32.03           N  
+ANISOU  738  NZ  LYS A 107     5896   3206   3067    607    635   1317       N  
+ATOM    739  N   TYR A 108      13.940  39.509  33.611  1.00 29.67           N  
+ANISOU  739  N   TYR A 108     5146   2543   3584    577    190    955       N  
+ATOM    740  CA  TYR A 108      12.563  39.991  33.556  1.00 33.30           C  
+ANISOU  740  CA  TYR A 108     5617   3018   4016    760     28    953       C  
+ATOM    741  C   TYR A 108      12.145  40.622  34.891  1.00 35.49           C  
+ANISOU  741  C   TYR A 108     5759   3228   4498    752     -5    813       C  
+ATOM    742  O   TYR A 108      11.027  41.118  35.032  1.00 32.50           O  
+ANISOU  742  O   TYR A 108     5358   2845   4145    902   -118    791       O  
+ATOM    743  CB  TYR A 108      11.599  38.858  33.200  1.00 30.82           C  
+ANISOU  743  CB  TYR A 108     5232   2940   3540    837   -148    885       C  
+ATOM    744  CG  TYR A 108      12.135  37.842  32.207  1.00 35.93           C  
+ANISOU  744  CG  TYR A 108     5966   3701   3986    805   -126    935       C  
+ATOM    745  CD1 TYR A 108      12.281  38.166  30.862  1.00 37.49           C  
+ANISOU  745  CD1 TYR A 108     6325   3892   4029    884    -98   1061       C  
+ATOM    746  CD2 TYR A 108      12.472  36.549  32.616  1.00 32.27           C  
+ANISOU  746  CD2 TYR A 108     5366   3386   3510    672   -126    811       C  
+ATOM    747  CE1 TYR A 108      12.761  37.242  29.949  1.00 35.92           C  
+ANISOU  747  CE1 TYR A 108     6179   3816   3653    856    -70   1063       C  
+ATOM    748  CE2 TYR A 108      12.955  35.609  31.709  1.00 30.79           C  
+ANISOU  748  CE2 TYR A 108     5262   3293   3145    655   -106    838       C  
+ATOM    749  CZ  TYR A 108      13.095  35.967  30.374  1.00 38.00           C  
+ANISOU  749  CZ  TYR A 108     6359   4189   3892    755    -77    961       C  
+ATOM    750  OH  TYR A 108      13.570  35.049  29.465  1.00 35.36           O  
+ANISOU  750  OH  TYR A 108     6075   3964   3397    737    -49    944       O  
+ATOM    751  N   GLY A 109      13.043  40.595  35.871  1.00 29.19           N  
+ANISOU  751  N   GLY A 109     4869   2382   3838    592     86    706       N  
+ATOM    752  CA  GLY A 109      12.762  41.161  37.180  1.00 30.68           C  
+ANISOU  752  CA  GLY A 109     4956   2512   4187    593     57    552       C  
+ATOM    753  C   GLY A 109      12.000  40.232  38.115  1.00 27.47           C  
+ANISOU  753  C   GLY A 109     4384   2320   3734    605    -30    396       C  
+ATOM    754  O   GLY A 109      11.363  40.691  39.070  1.00 28.87           O  
+ANISOU  754  O   GLY A 109     4494   2484   3993    673    -62    282       O  
+ATOM    755  N   ASN A 110      12.069  38.929  37.855  1.00 23.29           N  
+ANISOU  755  N   ASN A 110     3794   1976   3079    542    -49    392       N  
+ATOM    756  CA  ASN A 110      11.315  37.957  38.644  1.00 24.21           C  
+ANISOU  756  CA  ASN A 110     3756   2279   3164    547   -105    276       C  
+ATOM    757  C   ASN A 110      12.193  37.076  39.516  1.00 27.35           C  
+ANISOU  757  C   ASN A 110     4083   2755   3555    405    -47    185       C  
+ATOM    758  O   ASN A 110      13.326  36.735  39.149  1.00 26.22           O  
+ANISOU  758  O   ASN A 110     3982   2588   3392    295      8    222       O  
+ATOM    759  CB  ASN A 110      10.484  37.041  37.745  1.00 26.02           C  
+ANISOU  759  CB  ASN A 110     3948   2656   3282    601   -199    322       C  
+ATOM    760  CG  ASN A 110       9.394  37.774  37.012  1.00 32.04           C  
+ANISOU  760  CG  ASN A 110     4748   3381   4044    777   -306    385       C  
+ATOM    761  OD1 ASN A 110       8.858  38.778  37.498  1.00 29.50           O  
+ANISOU  761  OD1 ASN A 110     4416   2965   3826    876   -313    361       O  
+ATOM    762  ND2 ASN A 110       9.051  37.276  35.827  1.00 34.88           N  
+ANISOU  762  ND2 ASN A 110     5157   3813   4281    835   -407    454       N  
+ATOM    763  N   ILE A 111      11.632  36.706  40.663  1.00 19.29           N  
+ANISOU  763  N   ILE A 111     2955   1829   2546    426    -52     74       N  
+ATOM    764  CA  ILE A 111      12.201  35.721  41.574  1.00 17.70           C  
+ANISOU  764  CA  ILE A 111     2692   1729   2304    334    -13     -3       C  
+ATOM    765  C   ILE A 111      11.322  34.482  41.476  1.00 17.28           C  
+ANISOU  765  C   ILE A 111     2536   1838   2194    341    -30     10       C  
+ATOM    766  O   ILE A 111      10.109  34.602  41.257  1.00 23.02           O  
+ANISOU  766  O   ILE A 111     3195   2599   2951    434    -69     19       O  
+ATOM    767  CB  ILE A 111      12.249  36.269  43.029  1.00 23.81           C  
+ANISOU  767  CB  ILE A 111     3456   2477   3115    374     11   -134       C  
+ATOM    768  CG1 ILE A 111      13.269  37.409  43.113  1.00 24.79           C  
+ANISOU  768  CG1 ILE A 111     3664   2417   3337    338      7   -175       C  
+ATOM    769  CG2 ILE A 111      12.585  35.167  44.033  1.00 26.44           C  
+ANISOU  769  CG2 ILE A 111     3740   2940   3365    327     42   -197       C  
+ATOM    770  CD1 ILE A 111      13.057  38.350  44.283  1.00 28.50           C  
+ANISOU  770  CD1 ILE A 111     4154   2814   3859    423     -4   -319       C  
+ATOM    771  N   LYS A 112      11.923  33.298  41.600  1.00 16.48           N  
+ANISOU  771  N   LYS A 112     2408   1819   2037    243     -5      8       N  
+ATOM    772  CA  LYS A 112      11.169  32.063  41.437  1.00 17.55           C  
+ANISOU  772  CA  LYS A 112     2444   2073   2153    228    -15     21       C  
+ATOM    773  C   LYS A 112      11.408  31.138  42.606  1.00 17.74           C  
+ANISOU  773  C   LYS A 112     2421   2170   2151    182     60    -21       C  
+ATOM    774  O   LYS A 112      12.375  31.297  43.347  1.00 18.88           O  
+ANISOU  774  O   LYS A 112     2624   2291   2260    157     89    -59       O  
+ATOM    775  CB  LYS A 112      11.548  31.365  40.122  1.00 20.92           C  
+ANISOU  775  CB  LYS A 112     2909   2514   2527    171    -66     79       C  
+ATOM    776  CG  LYS A 112      11.235  32.201  38.868  1.00 20.70           C  
+ANISOU  776  CG  LYS A 112     2963   2426   2478    247   -142    142       C  
+ATOM    777  CD  LYS A 112      11.187  31.363  37.597  1.00 25.09           C  
+ANISOU  777  CD  LYS A 112     3551   3033   2948    237   -215    176       C  
+ATOM    778  CE  LYS A 112      12.513  30.700  37.300  1.00 27.76           C  
+ANISOU  778  CE  LYS A 112     3962   3366   3218    136   -144    195       C  
+ATOM    779  NZ  LYS A 112      12.511  30.103  35.927  1.00 21.78           N  
+ANISOU  779  NZ  LYS A 112     3283   2645   2346    158   -208    224       N  
+ATOM    780  N   SER A 113      10.509  30.175  42.786  1.00 19.82           N  
+ANISOU  780  N   SER A 113     2575   2513   2443    179     87    -13       N  
+ATOM    781  CA  SER A 113      10.748  29.134  43.774  1.00 13.80           C  
+ANISOU  781  CA  SER A 113     1790   1808   1646    137    177    -15       C  
+ATOM    782  C   SER A 113      11.862  28.209  43.278  1.00 17.24           C  
+ANISOU  782  C   SER A 113     2276   2242   2034     40    152      9       C  
+ATOM    783  O   SER A 113      12.062  28.069  42.073  1.00 16.58           O  
+ANISOU  783  O   SER A 113     2208   2137   1956      1     82     29       O  
+ATOM    784  CB  SER A 113       9.468  28.341  44.036  1.00 16.70           C  
+ANISOU  784  CB  SER A 113     2013   2232   2102    145    243      4       C  
+ATOM    785  OG  SER A 113       8.931  27.837  42.821  1.00 21.46           O  
+ANISOU  785  OG  SER A 113     2533   2834   2786    102    148     14       O  
+ATOM    786  N   LYS A 114      12.586  27.595  44.214  1.00 19.32           N  
+ANISOU  786  N   LYS A 114     2576   2528   2238     21    207      5       N  
+ATOM    787  CA  LYS A 114      13.650  26.646  43.872  1.00 24.51           C  
+ANISOU  787  CA  LYS A 114     3266   3181   2865    -54    190     23       C  
+ATOM    788  C   LYS A 114      13.158  25.508  42.993  1.00 20.43           C  
+ANISOU  788  C   LYS A 114     2688   2674   2402   -115    181     56       C  
+ATOM    789  O   LYS A 114      12.078  24.985  43.225  1.00 18.15           O  
+ANISOU  789  O   LYS A 114     2310   2405   2181   -113    223     72       O  
+ATOM    790  CB  LYS A 114      14.264  26.049  45.137  1.00 24.57           C  
+ANISOU  790  CB  LYS A 114     3316   3219   2801    -32    241     22       C  
+ATOM    791  CG  LYS A 114      15.243  26.945  45.814  1.00 22.56           C  
+ANISOU  791  CG  LYS A 114     3133   2947   2491     11    194    -47       C  
+ATOM    792  CD  LYS A 114      15.795  26.292  47.044  1.00 18.95           C  
+ANISOU  792  CD  LYS A 114     2731   2534   1933     64    211    -53       C  
+ATOM    793  CE  LYS A 114      16.560  27.296  47.858  1.00 22.52           C  
+ANISOU  793  CE  LYS A 114     3247   2974   2334    129    132   -160       C  
+ATOM    794  NZ  LYS A 114      16.844  26.762  49.207  1.00 23.19           N  
+ANISOU  794  NZ  LYS A 114     3416   3124   2273    231    136   -173       N  
+ATOM    795  N   GLY A 115      13.958  25.129  42.000  1.00 18.66           N  
+ANISOU  795  N   GLY A 115     2503   2426   2160   -166    132     56       N  
+ATOM    796  CA  GLY A 115      13.688  23.942  41.215  1.00 16.96           C  
+ANISOU  796  CA  GLY A 115     2252   2210   1982   -217    109     57       C  
+ATOM    797  C   GLY A 115      14.097  22.698  41.999  1.00 15.94           C  
+ANISOU  797  C   GLY A 115     2115   2076   1865   -250    177     80       C  
+ATOM    798  O   GLY A 115      14.773  22.793  43.030  1.00 15.08           O  
+ANISOU  798  O   GLY A 115     2049   1977   1703   -221    223     96       O  
+ATOM    799  N   PRO A 116      13.695  21.522  41.510  1.00 15.45           N  
+ANISOU  799  N   PRO A 116     2007   1988   1875   -301    170     75       N  
+ATOM    800  CA  PRO A 116      14.157  20.268  42.106  1.00 15.58           C  
+ANISOU  800  CA  PRO A 116     2034   1971   1916   -329    236    109       C  
+ATOM    801  C   PRO A 116      15.684  20.157  42.143  1.00 17.21           C  
+ANISOU  801  C   PRO A 116     2329   2174   2037   -313    227    107       C  
+ATOM    802  O   PRO A 116      16.388  20.703  41.273  1.00 17.13           O  
+ANISOU  802  O   PRO A 116     2356   2170   1984   -315    177     69       O  
+ATOM    803  CB  PRO A 116      13.568  19.199  41.178  1.00 14.08           C  
+ANISOU  803  CB  PRO A 116     1785   1727   1838   -394    193     69       C  
+ATOM    804  CG  PRO A 116      12.337  19.846  40.596  1.00 17.82           C  
+ANISOU  804  CG  PRO A 116     2170   2225   2375   -391    122     25       C  
+ATOM    805  CD  PRO A 116      12.716  21.305  40.430  1.00 17.57           C  
+ANISOU  805  CD  PRO A 116     2208   2248   2221   -326     86     27       C  
+ATOM    806  N   ASN A 117      16.183  19.468  43.164  1.00 13.48           N  
+ANISOU  806  N   ASN A 117     1886   1689   1548   -288    284    154       N  
+ATOM    807  CA  ASN A 117      17.601  19.160  43.279  1.00 15.66           C  
+ANISOU  807  CA  ASN A 117     2215   1958   1778   -262    261    145       C  
+ATOM    808  C   ASN A 117      17.979  18.125  42.218  1.00 15.60           C  
+ANISOU  808  C   ASN A 117     2206   1895   1828   -306    247    116       C  
+ATOM    809  O   ASN A 117      17.512  17.001  42.305  1.00 14.32           O  
+ANISOU  809  O   ASN A 117     2032   1672   1737   -330    281    142       O  
+ATOM    810  CB  ASN A 117      17.883  18.618  44.690  1.00 16.77           C  
+ANISOU  810  CB  ASN A 117     2402   2100   1868   -193    306    211       C  
+ATOM    811  CG  ASN A 117      19.349  18.343  44.940  1.00 14.03           C  
+ANISOU  811  CG  ASN A 117     2091   1753   1485   -141    252    192       C  
+ATOM    812  OD1 ASN A 117      20.180  18.431  44.036  1.00 17.93           O  
+ANISOU  812  OD1 ASN A 117     2557   2237   2019   -171    210    134       O  
+ATOM    813  ND2 ASN A 117      19.671  17.984  46.189  1.00 17.52           N  
+ANISOU  813  ND2 ASN A 117     2598   2210   1850    -48    257    244       N  
+ATOM    814  N   PRO A 118      18.817  18.487  41.224  1.00 16.42           N  
+ANISOU  814  N   PRO A 118     2324   2007   1908   -313    212     62       N  
+ATOM    815  CA  PRO A 118      19.213  17.495  40.211  1.00 14.59           C  
+ANISOU  815  CA  PRO A 118     2110   1728   1707   -331    210     19       C  
+ATOM    816  C   PRO A 118      19.854  16.224  40.790  1.00 15.47           C  
+ANISOU  816  C   PRO A 118     2230   1779   1867   -305    238     42       C  
+ATOM    817  O   PRO A 118      19.732  15.129  40.224  1.00 15.45           O  
+ANISOU  817  O   PRO A 118     2241   1706   1925   -324    242     11       O  
+ATOM    818  CB  PRO A 118      20.238  18.264  39.355  1.00 14.01           C  
+ANISOU  818  CB  PRO A 118     2057   1683   1583   -318    216    -17       C  
+ATOM    819  CG  PRO A 118      19.792  19.707  39.460  1.00 15.22           C  
+ANISOU  819  CG  PRO A 118     2206   1878   1698   -322    201      2       C  
+ATOM    820  CD  PRO A 118      19.355  19.830  40.917  1.00 15.43           C  
+ANISOU  820  CD  PRO A 118     2205   1921   1739   -304    194     39       C  
+ATOM    821  N   PHE A 119      20.567  16.375  41.893  1.00 12.94           N  
+ANISOU  821  N   PHE A 119     1914   1481   1521   -249    241     86       N  
+ATOM    822  CA  PHE A 119      21.143  15.211  42.556  1.00 17.33           C  
+ANISOU  822  CA  PHE A 119     2495   1980   2109   -195    256    128       C  
+ATOM    823  C   PHE A 119      20.112  14.183  43.083  1.00 20.70           C  
+ANISOU  823  C   PHE A 119     2948   2326   2592   -213    313    205       C  
+ATOM    824  O   PHE A 119      20.477  13.035  43.337  1.00 16.24           O  
+ANISOU  824  O   PHE A 119     2417   1674   2079   -178    338    245       O  
+ATOM    825  CB  PHE A 119      22.060  15.679  43.695  1.00 13.80           C  
+ANISOU  825  CB  PHE A 119     2055   1587   1602   -106    212    150       C  
+ATOM    826  CG  PHE A 119      23.165  16.601  43.233  1.00 22.61           C  
+ANISOU  826  CG  PHE A 119     3110   2751   2729   -104    166     70       C  
+ATOM    827  CD1 PHE A 119      23.984  16.250  42.167  1.00 17.18           C  
+ANISOU  827  CD1 PHE A 119     2385   2036   2108   -119    190     16       C  
+ATOM    828  CD2 PHE A 119      23.373  17.824  43.863  1.00 20.58           C  
+ANISOU  828  CD2 PHE A 119     2831   2555   2433    -88    113     44       C  
+ATOM    829  CE1 PHE A 119      24.995  17.107  41.726  1.00 18.28           C  
+ANISOU  829  CE1 PHE A 119     2449   2205   2290   -128    190    -41       C  
+ATOM    830  CE2 PHE A 119      24.378  18.695  43.431  1.00 15.71           C  
+ANISOU  830  CE2 PHE A 119     2137   1954   1880   -107     86    -29       C  
+ATOM    831  CZ  PHE A 119      25.189  18.344  42.367  1.00 16.19           C  
+ANISOU  831  CZ  PHE A 119     2145   1984   2022   -132    137    -60       C  
+ATOM    832  N   ASP A 120      18.839  14.566  43.224  1.00 16.36           N  
+ANISOU  832  N   ASP A 120     2370   1787   2057   -266    347    231       N  
+ATOM    833  CA  ASP A 120      17.807  13.604  43.643  1.00 19.85           C  
+ANISOU  833  CA  ASP A 120     2802   2134   2606   -305    432    305       C  
+ATOM    834  C   ASP A 120      17.405  12.657  42.509  1.00 17.26           C  
+ANISOU  834  C   ASP A 120     2434   1697   2425   -388    410    228       C  
+ATOM    835  O   ASP A 120      16.719  11.655  42.744  1.00 20.38           O  
+ANISOU  835  O   ASP A 120     2808   1969   2966   -436    478    275       O  
+ATOM    836  CB  ASP A 120      16.545  14.325  44.144  1.00 16.73           C  
+ANISOU  836  CB  ASP A 120     2355   1784   2215   -333    489    346       C  
+ATOM    837  CG  ASP A 120      16.672  14.826  45.571  1.00 18.12           C  
+ANISOU  837  CG  ASP A 120     2600   2026   2258   -235    552    443       C  
+ATOM    838  OD1 ASP A 120      17.229  14.098  46.421  1.00 19.78           O  
+ANISOU  838  OD1 ASP A 120     2898   2198   2419   -158    597    533       O  
+ATOM    839  OD2 ASP A 120      16.162  15.934  45.850  1.00 18.77           O  
+ANISOU  839  OD2 ASP A 120     2660   2195   2278   -220    554    426       O  
+ATOM    840  N   TYR A 121      17.841  12.978  41.287  1.00 13.76           N  
+ANISOU  840  N   TYR A 121     1989   1291   1949   -401    323    108       N  
+ATOM    841  CA  TYR A 121      17.367  12.281  40.086  1.00 16.91           C  
+ANISOU  841  CA  TYR A 121     2366   1611   2446   -462    267     -5       C  
+ATOM    842  C   TYR A 121      18.435  11.372  39.498  1.00 17.47           C  
+ANISOU  842  C   TYR A 121     2500   1613   2524   -422    256    -67       C  
+ATOM    843  O   TYR A 121      18.249  10.785  38.434  1.00 18.13           O  
+ANISOU  843  O   TYR A 121     2596   1636   2658   -448    200   -188       O  
+ATOM    844  CB  TYR A 121      16.903  13.297  39.032  1.00 17.93           C  
+ANISOU  844  CB  TYR A 121     2477   1835   2500   -478    176    -99       C  
+ATOM    845  CG  TYR A 121      15.636  13.981  39.464  1.00 22.17           C  
+ANISOU  845  CG  TYR A 121     2928   2412   3085   -518    175    -64       C  
+ATOM    846  CD1 TYR A 121      15.673  15.031  40.387  1.00 20.23           C  
+ANISOU  846  CD1 TYR A 121     2681   2254   2753   -479    226     25       C  
+ATOM    847  CD2 TYR A 121      14.396  13.553  38.991  1.00 18.18           C  
+ANISOU  847  CD2 TYR A 121     2329   1846   2731   -587    118   -133       C  
+ATOM    848  CE1 TYR A 121      14.507  15.646  40.822  1.00 16.48           C  
+ANISOU  848  CE1 TYR A 121     2123   1811   2327   -499    244     55       C  
+ATOM    849  CE2 TYR A 121      13.218  14.169  39.418  1.00 17.29           C  
+ANISOU  849  CE2 TYR A 121     2107   1769   2695   -616    129   -101       C  
+ATOM    850  CZ  TYR A 121      13.287  15.208  40.330  1.00 14.70           C  
+ANISOU  850  CZ  TYR A 121     1789   1533   2264   -566    204     -2       C  
+ATOM    851  OH  TYR A 121      12.130  15.823  40.765  1.00 16.42           O  
+ANISOU  851  OH  TYR A 121     1896   1783   2558   -577    232     24       O  
+ATOM    852  N   LEU A 122      19.541  11.259  40.227  1.00 17.05           N  
+ANISOU  852  N   LEU A 122     2486   1571   2422   -345    300      5       N  
+ATOM    853  CA  LEU A 122      20.711  10.497  39.812  1.00 20.57           C  
+ANISOU  853  CA  LEU A 122     2973   1962   2879   -281    301    -43       C  
+ATOM    854  C   LEU A 122      21.191   9.671  40.989  1.00 20.68           C  
+ANISOU  854  C   LEU A 122     3018   1894   2945   -214    348     73       C  
+ATOM    855  O   LEU A 122      21.022  10.076  42.142  1.00 16.39           O  
+ANISOU  855  O   LEU A 122     2482   1396   2350   -185    373    189       O  
+ATOM    856  CB  LEU A 122      21.830  11.436  39.346  1.00 15.91           C  
+ANISOU  856  CB  LEU A 122     2379   1494   2172   -226    290    -87       C  
+ATOM    857  CG  LEU A 122      21.532  12.299  38.122  1.00 15.72           C  
+ANISOU  857  CG  LEU A 122     2363   1549   2062   -262    265   -175       C  
+ATOM    858  CD1 LEU A 122      22.577  13.411  38.007  1.00 17.87           C  
+ANISOU  858  CD1 LEU A 122     2614   1924   2251   -223    296   -164       C  
+ATOM    859  CD2 LEU A 122      21.474  11.455  36.850  1.00 17.91           C  
+ANISOU  859  CD2 LEU A 122     2694   1759   2352   -258    247   -301       C  
+ATOM    860  N   GLY A 123      21.808   8.531  40.706  1.00 19.82           N  
+ANISOU  860  N   GLY A 123     2945   1665   2922   -168    358     41       N  
+ATOM    861  CA  GLY A 123      22.251   7.649  41.772  1.00 21.55           C  
+ANISOU  861  CA  GLY A 123     3213   1784   3192    -82    396    164       C  
+ATOM    862  C   GLY A 123      23.237   6.600  41.320  1.00 22.60           C  
+ANISOU  862  C   GLY A 123     3376   1806   3405      1    390    105       C  
+ATOM    863  O   GLY A 123      23.464   6.420  40.120  1.00 18.45           O  
+ANISOU  863  O   GLY A 123     2839   1265   2905    -18    374    -43       O  
+ATOM    864  N   TYR A 124      23.836   5.903  42.277  1.00 18.92           N  
+ANISOU  864  N   TYR A 124     2961   1263   2965    114    404    221       N  
+ATOM    865  CA  TYR A 124      24.706   4.799  41.911  1.00 20.21           C  
+ANISOU  865  CA  TYR A 124     3153   1294   3233    208    403    173       C  
+ATOM    866  C   TYR A 124      24.672   3.668  42.922  1.00 26.48           C  
+ANISOU  866  C   TYR A 124     4041   1907   4113    292    445    334       C  
+ATOM    867  O   TYR A 124      24.110   3.800  44.011  1.00 22.91           O  
+ANISOU  867  O   TYR A 124     3641   1457   3606    297    485    501       O  
+ATOM    868  CB  TYR A 124      26.157   5.272  41.704  1.00 19.89           C  
+ANISOU  868  CB  TYR A 124     3047   1379   3131    327    350    102       C  
+ATOM    869  CG  TYR A 124      26.844   6.040  42.837  1.00 20.13           C  
+ANISOU  869  CG  TYR A 124     3047   1547   3055    427    283    194       C  
+ATOM    870  CD1 TYR A 124      26.966   5.500  44.122  1.00 22.18           C  
+ANISOU  870  CD1 TYR A 124     3389   1748   3291    547    257    349       C  
+ATOM    871  CD2 TYR A 124      27.461   7.264  42.584  1.00 19.53           C  
+ANISOU  871  CD2 TYR A 124     2865   1648   2909    416    240    115       C  
+ATOM    872  CE1 TYR A 124      27.626   6.195  45.134  1.00 24.97           C  
+ANISOU  872  CE1 TYR A 124     3725   2234   3527    662    157    400       C  
+ATOM    873  CE2 TYR A 124      28.130   7.966  43.586  1.00 19.12           C  
+ANISOU  873  CE2 TYR A 124     2770   1709   2787    506    148    158       C  
+ATOM    874  CZ  TYR A 124      28.208   7.430  44.854  1.00 19.72           C  
+ANISOU  874  CZ  TYR A 124     2933   1742   2818    634     91    287       C  
+ATOM    875  OH  TYR A 124      28.878   8.113  45.843  1.00 22.78           O  
+ANISOU  875  OH  TYR A 124     3290   2248   3118    744    -36    303       O  
+ATOM    876  N   GLN A 125      25.277   2.552  42.531  1.00 23.38           N  
+ANISOU  876  N   GLN A 125     3682   1351   3850    369    450    288       N  
+ATOM    877  CA  GLN A 125      25.380   1.373  43.376  1.00 25.41           C  
+ANISOU  877  CA  GLN A 125     4045   1402   4207    471    493    444       C  
+ATOM    878  C   GLN A 125      26.701   0.666  43.088  1.00 29.64           C  
+ANISOU  878  C   GLN A 125     4582   1872   4807    642    445    377       C  
+ATOM    879  O   GLN A 125      27.006   0.375  41.933  1.00 26.63           O  
+ANISOU  879  O   GLN A 125     4158   1451   4508    621    442    192       O  
+ATOM    880  CB  GLN A 125      24.197   0.430  43.135  1.00 26.70           C  
+ANISOU  880  CB  GLN A 125     4242   1353   4549    329    571    456       C  
+ATOM    881  CG  GLN A 125      24.183  -0.785  44.053  1.00 30.83           C  
+ANISOU  881  CG  GLN A 125     4850   1733   5129    396    602    620       C  
+ATOM    882  CD  GLN A 125      22.864  -1.523  44.024  1.00 39.07           C  
+ANISOU  882  CD  GLN A 125     5881   2649   6316    226    671    643       C  
+ATOM    883  OE1 GLN A 125      21.801  -0.927  44.192  1.00 42.48           O  
+ANISOU  883  OE1 GLN A 125     6256   3156   6730     94    721    673       O  
+ATOM    884  NE2 GLN A 125      22.926  -2.828  43.824  1.00 39.02           N  
+ANISOU  884  NE2 GLN A 125     5918   2445   6465    235    676    625       N  
+ATOM    885  N   TYR A 126      27.494   0.410  44.125  1.00 27.63           N  
+ANISOU  885  N   TYR A 126     4379   1615   4503    829    400    518       N  
+ATOM    886  CA  TYR A 126      28.730  -0.348  43.951  1.00 31.88           C  
+ANISOU  886  CA  TYR A 126     4906   2073   5132   1015    349    468       C  
+ATOM    887  C   TYR A 126      28.427  -1.831  43.783  1.00 35.17           C  
+ANISOU  887  C   TYR A 126     5405   2250   5706    999    387    482       C  
+ATOM    888  O   TYR A 126      27.549  -2.376  44.457  1.00 33.07           O  
+ANISOU  888  O   TYR A 126     5224   1890   5448    923    432    628       O  
+ATOM    889  CB  TYR A 126      29.682  -0.149  45.136  1.00 32.55           C  
+ANISOU  889  CB  TYR A 126     5005   2257   5105   1232    238    596       C  
+ATOM    890  CG  TYR A 126      30.390   1.184  45.147  1.00 28.42           C  
+ANISOU  890  CG  TYR A 126     4329   2014   4456   1245    130    496       C  
+ATOM    891  CD1 TYR A 126      31.637   1.338  44.547  1.00 31.70           C  
+ANISOU  891  CD1 TYR A 126     4586   2508   4949   1338     68    340       C  
+ATOM    892  CD2 TYR A 126      29.813   2.293  45.750  1.00 27.01           C  
+ANISOU  892  CD2 TYR A 126     4152   2005   4106   1163    105    551       C  
+ATOM    893  CE1 TYR A 126      32.288   2.568  44.549  1.00 27.75           C  
+ANISOU  893  CE1 TYR A 126     3924   2236   4385   1330    -15    248       C  
+ATOM    894  CE2 TYR A 126      30.456   3.518  45.763  1.00 25.88           C  
+ANISOU  894  CE2 TYR A 126     3866   2085   3880   1165      4    449       C  
+ATOM    895  CZ  TYR A 126      31.692   3.650  45.163  1.00 27.97           C  
+ANISOU  895  CZ  TYR A 126     3966   2411   4251   1240    -55    301       C  
+ATOM    896  OH  TYR A 126      32.322   4.872  45.172  1.00 30.01           O  
+ANISOU  896  OH  TYR A 126     4063   2865   4476   1221   -139    202       O  
+ATOM    897  N   SER A 127      29.159  -2.481  42.885  1.00 25.37           N  
+ANISOU  897  N   SER A 127     4535   1723   3382    894    388    190       N  
+ATOM    898  CA  SER A 127      28.980  -3.908  42.643  1.00 28.18           C  
+ANISOU  898  CA  SER A 127     5161   1699   3846   1013    249    123       C  
+ATOM    899  C   SER A 127      29.365  -4.733  43.863  1.00 33.96           C  
+ANISOU  899  C   SER A 127     6011   2279   4612   1065    233    320       C  
+ATOM    900  O   SER A 127      30.054  -4.244  44.761  1.00 31.05           O  
+ANISOU  900  O   SER A 127     5544   2136   4117   1132    322    464       O  
+ATOM    901  CB  SER A 127      29.808  -4.350  41.436  1.00 34.67           C  
+ANISOU  901  CB  SER A 127     6038   2592   4545   1376    163    -96       C  
+ATOM    902  OG  SER A 127      31.202  -4.262  41.701  1.00 33.95           O  
+ANISOU  902  OG  SER A 127     5856   2766   4275   1670    222    -32       O  
+ATOM    903  N   SER A 128      28.932  -5.990  43.894  1.00 36.53           N  
+ANISOU  903  N   SER A 128     6466   2295   5119   1008     96    317       N  
+ATOM    904  CA  SER A 128      29.146  -6.823  45.071  1.00 38.22           C  
+ANISOU  904  CA  SER A 128     6759   2372   5388   1019     86    543       C  
+ATOM    905  C   SER A 128      30.631  -7.093  45.327  1.00 41.78           C  
+ANISOU  905  C   SER A 128     7256   2986   5633   1395     79    541       C  
+ATOM    906  O   SER A 128      31.043  -7.308  46.471  1.00 36.65           O  
+ANISOU  906  O   SER A 128     6626   2382   4917   1458    120    746       O  
+ATOM    907  CB  SER A 128      28.386  -8.147  44.937  1.00 52.00           C  
+ANISOU  907  CB  SER A 128     8609   3708   7441    884    -54    557       C  
+ATOM    908  OG  SER A 128      28.755  -8.835  43.755  1.00 58.15           O  
+ANISOU  908  OG  SER A 128     9492   4361   8243   1090   -195    278       O  
+ATOM    909  N   ASP A 129      31.439  -7.089  44.270  1.00 36.01           N  
+ANISOU  909  N   ASP A 129     6512   2395   4775   1667     28    316       N  
+ATOM    910  CA  ASP A 129      32.866  -7.298  44.455  1.00 38.37           C  
+ANISOU  910  CA  ASP A 129     6784   2927   4869   2026     26    312       C  
+ATOM    911  C   ASP A 129      33.598  -5.970  44.630  1.00 39.24           C  
+ANISOU  911  C   ASP A 129     6648   3468   4794   2115    162    358       C  
+ATOM    912  O   ASP A 129      34.818  -5.945  44.799  1.00 38.78           O  
+ANISOU  912  O   ASP A 129     6471   3690   4572   2386    169    366       O  
+ATOM    913  CB  ASP A 129      33.468  -8.103  43.295  1.00 42.90           C  
+ANISOU  913  CB  ASP A 129     7430   3495   5374   2307    -96     77       C  
+ATOM    914  CG  ASP A 129      33.274  -7.451  41.934  1.00 44.54           C  
+ANISOU  914  CG  ASP A 129     7529   3887   5505   2332    -82   -128       C  
+ATOM    915  OD1 ASP A 129      32.839  -6.282  41.841  1.00 35.39           O  
+ANISOU  915  OD1 ASP A 129     6219   2887   4342   2161     37    -91       O  
+ATOM    916  OD2 ASP A 129      33.585  -8.129  40.932  1.00 48.39           O  
+ANISOU  916  OD2 ASP A 129     8090   4380   5916   2552   -193   -326       O  
+ATOM    917  N   GLY A 130      32.845  -4.874  44.575  1.00 36.31           N  
+ANISOU  917  N   GLY A 130     6172   3151   4474   1874    261    389       N  
+ATOM    918  CA  GLY A 130      33.368  -3.548  44.856  1.00 37.00           C  
+ANISOU  918  CA  GLY A 130     5930   3663   4464   1781    358    432       C  
+ATOM    919  C   GLY A 130      34.259  -2.961  43.776  1.00 38.31           C  
+ANISOU  919  C   GLY A 130     5860   4172   4526   1952    399    324       C  
+ATOM    920  O   GLY A 130      34.923  -1.951  43.992  1.00 40.79           O  
+ANISOU  920  O   GLY A 130     5877   4819   4800   1896    455    383       O  
+ATOM    921  N   LYS A 131      34.253  -3.576  42.604  1.00 37.09           N  
+ANISOU  921  N   LYS A 131     5823   3937   4332   2163    362    173       N  
+ATOM    922  CA  LYS A 131      35.186  -3.211  41.546  1.00 35.97           C  
+ANISOU  922  CA  LYS A 131     5463   4170   4034   2423    425    111       C  
+ATOM    923  C   LYS A 131      34.560  -2.281  40.519  1.00 40.37           C  
+ANISOU  923  C   LYS A 131     5886   4855   4598   2246    511     64       C  
+ATOM    924  O   LYS A 131      35.264  -1.651  39.731  1.00 43.20           O  
+ANISOU  924  O   LYS A 131     5987   5587   4839   2380    615    103       O  
+ATOM    925  CB  LYS A 131      35.700  -4.471  40.850  1.00 34.70           C  
+ANISOU  925  CB  LYS A 131     5466   3969   3749   2707    305    -35       C  
+ATOM    926  N   GLN A 132      33.231  -2.218  40.525  1.00 34.66           N  
+ANISOU  926  N   GLN A 132     5322   3838   4010   1958    472      9       N  
+ATOM    927  CA  GLN A 132      32.492  -1.467  39.524  1.00 37.00           C  
+ANISOU  927  CA  GLN A 132     5542   4215   4300   1827    524    -57       C  
+ATOM    928  C   GLN A 132      31.430  -0.589  40.158  1.00 28.75           C  
+ANISOU  928  C   GLN A 132     4448   3064   3410   1399    558     23       C  
+ATOM    929  O   GLN A 132      30.894  -0.903  41.215  1.00 29.60           O  
+ANISOU  929  O   GLN A 132     4671   2941   3634   1216    514     79       O  
+ATOM    930  CB  GLN A 132      31.828  -2.411  38.526  1.00 38.92           C  
+ANISOU  930  CB  GLN A 132     6045   4225   4519   2005    393   -295       C  
+ATOM    931  CG  GLN A 132      32.791  -3.299  37.769  1.00 43.64           C  
+ANISOU  931  CG  GLN A 132     6667   4979   4934   2354    307   -397       C  
+ATOM    932  CD  GLN A 132      32.069  -4.371  37.001  1.00 49.80           C  
+ANISOU  932  CD  GLN A 132     7684   5489   5747   2397     95   -634       C  
+ATOM    933  OE1 GLN A 132      30.840  -4.446  37.033  1.00 57.19           O  
+ANISOU  933  OE1 GLN A 132     8735   6127   6867   2147     13   -716       O  
+ATOM    934  NE2 GLN A 132      32.823  -5.209  36.300  1.00 48.42           N  
+ANISOU  934  NE2 GLN A 132     7569   5430   5400   2713     -7   -745       N  
+ATOM    935  N   LEU A 133      31.118   0.501  39.475  1.00 26.03           N  
+ANISOU  935  N   LEU A 133     3934   2909   3047   1280    643     42       N  
+ATOM    936  CA  LEU A 133      30.085   1.413  39.924  1.00 23.05           C  
+ANISOU  936  CA  LEU A 133     3510   2457   2789    932    668     89       C  
+ATOM    937  C   LEU A 133      28.968   1.455  38.895  1.00 23.94           C  
+ANISOU  937  C   LEU A 133     3708   2491   2897    891    639    -48       C  
+ATOM    938  O   LEU A 133      29.193   1.857  37.754  1.00 26.17           O  
+ANISOU  938  O   LEU A 133     3905   2983   3055   1051    691    -75       O  
+ATOM    939  CB  LEU A 133      30.673   2.805  40.145  1.00 22.51           C  
+ANISOU  939  CB  LEU A 133     3169   2644   2741    810    762    239       C  
+ATOM    940  CG  LEU A 133      29.765   3.828  40.827  1.00 22.62           C  
+ANISOU  940  CG  LEU A 133     3142   2583   2869    500    761    275       C  
+ATOM    941  CD1 LEU A 133      29.317   3.283  42.172  1.00 23.73           C  
+ANISOU  941  CD1 LEU A 133     3416   2542   3058    399    697    275       C  
+ATOM    942  CD2 LEU A 133      30.468   5.167  41.002  1.00 24.81           C  
+ANISOU  942  CD2 LEU A 133     3169   3046   3211    396    799    399       C  
+ATOM    943  N   HIS A 134      27.773   1.026  39.294  1.00 22.90           N  
+ANISOU  943  N   HIS A 134     3721   2088   2892    693    558   -115       N  
+ATOM    944  CA  HIS A 134      26.594   1.073  38.422  1.00 21.24           C  
+ANISOU  944  CA  HIS A 134     3564   1803   2705    622    497   -262       C  
+ATOM    945  C   HIS A 134      25.836   2.383  38.580  1.00 22.17           C  
+ANISOU  945  C   HIS A 134     3531   2042   2851    387    579   -183       C  
+ATOM    946  O   HIS A 134      25.742   2.910  39.683  1.00 22.24           O  
+ANISOU  946  O   HIS A 134     3473   2049   2929    203    629    -56       O  
+ATOM    947  CB  HIS A 134      25.679  -0.105  38.729  1.00 22.06           C  
+ANISOU  947  CB  HIS A 134     3860   1546   2978    508    348   -362       C  
+ATOM    948  CG  HIS A 134      26.331  -1.427  38.480  1.00 25.44           C  
+ANISOU  948  CG  HIS A 134     4485   1779   3404    762    222   -474       C  
+ATOM    949  ND1 HIS A 134      26.227  -2.090  37.277  1.00 35.84           N  
+ANISOU  949  ND1 HIS A 134     5933   3021   4665   1000     66   -732       N  
+ATOM    950  CD2 HIS A 134      27.121  -2.195  39.267  1.00 32.74           C  
+ANISOU  950  CD2 HIS A 134     5511   2574   4355    864    209   -381       C  
+ATOM    951  CE1 HIS A 134      26.913  -3.220  37.341  1.00 39.76           C  
+ANISOU  951  CE1 HIS A 134     6560   3372   5173   1195    -41   -782       C  
+ATOM    952  NE2 HIS A 134      27.471  -3.304  38.536  1.00 33.98           N  
+ANISOU  952  NE2 HIS A 134     5854   2566   4490   1146     47   -576       N  
+ATOM    953  N   LEU A 135      25.288   2.892  37.478  1.00 22.04           N  
+ANISOU  953  N   LEU A 135     3477   2139   2759    438    576   -274       N  
+ATOM    954  CA  LEU A 135      24.722   4.236  37.441  1.00 20.17           C  
+ANISOU  954  CA  LEU A 135     3105   2038   2522    289    654   -192       C  
+ATOM    955  C   LEU A 135      23.236   4.216  37.095  1.00 20.52           C  
+ANISOU  955  C   LEU A 135     3184   1999   2613    170    569   -328       C  
+ATOM    956  O   LEU A 135      22.801   3.457  36.215  1.00 19.56           O  
+ANISOU  956  O   LEU A 135     3153   1817   2462    285    450   -516       O  
+ATOM    957  CB  LEU A 135      25.468   5.103  36.413  1.00 19.27           C  
+ANISOU  957  CB  LEU A 135     2870   2190   2261    474    757   -103       C  
+ATOM    958  CG  LEU A 135      26.999   5.159  36.462  1.00 23.51           C  
+ANISOU  958  CG  LEU A 135     3299   2887   2746    621    849     49       C  
+ATOM    959  CD1 LEU A 135      27.555   5.958  35.278  1.00 24.07           C  
+ANISOU  959  CD1 LEU A 135     3223   3248   2675    801    974    187       C  
+ATOM    960  CD2 LEU A 135      27.453   5.746  37.787  1.00 22.18           C  
+ANISOU  960  CD2 LEU A 135     3034   2667   2725    406    871    188       C  
+ATOM    961  N   TYR A 136      22.478   5.087  37.761  1.00 18.91           N  
+ANISOU  961  N   TYR A 136     2897   1815   2475    -33    611   -254       N  
+ATOM    962  CA  TYR A 136      21.029   5.145  37.612  1.00 17.80           C  
+ANISOU  962  CA  TYR A 136     2737   1641   2387   -161    544   -355       C  
+ATOM    963  C   TYR A 136      20.497   6.578  37.516  1.00 19.64           C  
+ANISOU  963  C   TYR A 136     2864   2034   2564   -193    608   -298       C  
+ATOM    964  O   TYR A 136      21.089   7.512  38.048  1.00 17.88           O  
+ANISOU  964  O   TYR A 136     2591   1867   2335   -210    689   -164       O  
+ATOM    965  CB  TYR A 136      20.351   4.432  38.784  1.00 16.95           C  
+ANISOU  965  CB  TYR A 136     2638   1364   2438   -380    517   -313       C  
+ATOM    966  CG  TYR A 136      20.773   2.983  38.911  1.00 18.82           C  
+ANISOU  966  CG  TYR A 136     3007   1371   2771   -362    433   -347       C  
+ATOM    967  CD1 TYR A 136      20.155   1.994  38.162  1.00 24.35           C  
+ANISOU  967  CD1 TYR A 136     3782   1896   3573   -366    267   -527       C  
+ATOM    968  CD2 TYR A 136      21.811   2.615  39.753  1.00 21.27           C  
+ANISOU  968  CD2 TYR A 136     3378   1625   3081   -318    489   -218       C  
+ATOM    969  CE1 TYR A 136      20.556   0.672  38.251  1.00 27.22           C  
+ANISOU  969  CE1 TYR A 136     4301   1987   4055   -332    156   -573       C  
+ATOM    970  CE2 TYR A 136      22.215   1.294  39.846  1.00 24.29           C  
+ANISOU  970  CE2 TYR A 136     3907   1773   3548   -264    402   -242       C  
+ATOM    971  CZ  TYR A 136      21.582   0.333  39.099  1.00 29.12           C  
+ANISOU  971  CZ  TYR A 136     4615   2168   4281   -274    235   -416       C  
+ATOM    972  OH  TYR A 136      21.982  -0.980  39.201  1.00 35.01           O  
+ANISOU  972  OH  TYR A 136     5539   2620   5144   -209    117   -450       O  
+ATOM    973  N   GLU A 137      19.378   6.741  36.816  1.00 18.47           N  
+ANISOU  973  N   GLU A 137     2685   1945   2390   -188    542   -418       N  
+ATOM    974  CA  GLU A 137      18.673   8.010  36.815  1.00 21.46           C  
+ANISOU  974  CA  GLU A 137     2980   2451   2724   -204    582   -376       C  
+ATOM    975  C   GLU A 137      17.169   7.753  36.986  1.00 21.64           C  
+ANISOU  975  C   GLU A 137     2926   2487   2809   -329    502   -487       C  
+ATOM    976  O   GLU A 137      16.671   6.694  36.641  1.00 17.78           O  
+ANISOU  976  O   GLU A 137     2442   1918   2397   -380    389   -618       O  
+ATOM    977  CB  GLU A 137      18.936   8.789  35.532  1.00 21.23           C  
+ANISOU  977  CB  GLU A 137     2953   2571   2542      9    607   -362       C  
+ATOM    978  CG  GLU A 137      18.358   8.111  34.314  1.00 16.64           C  
+ANISOU  978  CG  GLU A 137     2402   2061   1861    161    491   -558       C  
+ATOM    979  CD  GLU A 137      18.564   8.902  33.041  1.00 24.46           C  
+ANISOU  979  CD  GLU A 137     3393   3257   2643    426    535   -510       C  
+ATOM    980  OE1 GLU A 137      18.647  10.146  33.100  1.00 19.97           O  
+ANISOU  980  OE1 GLU A 137     2784   2749   2054    434    636   -328       O  
+ATOM    981  OE2 GLU A 137      18.638   8.265  31.979  1.00 21.10           O  
+ANISOU  981  OE2 GLU A 137     3019   2928   2070    647    458   -653       O  
+ATOM    982  N   TRP A 138      16.473   8.747  37.522  1.00 17.40           N  
+ANISOU  982  N   TRP A 138     2306   2052   2254   -368    545   -436       N  
+ATOM    983  CA  TRP A 138      15.033   8.687  37.693  1.00 18.60           C  
+ANISOU  983  CA  TRP A 138     2330   2296   2443   -459    494   -510       C  
+ATOM    984  C   TRP A 138      14.403   9.139  36.388  1.00 23.96           C  
+ANISOU  984  C   TRP A 138     2981   3110   3014   -300    411   -642       C  
+ATOM    985  O   TRP A 138      14.668  10.252  35.916  1.00 22.46           O  
+ANISOU  985  O   TRP A 138     2834   3003   2699   -132    456   -590       O  
+ATOM    986  CB  TRP A 138      14.592   9.576  38.862  1.00 19.00           C  
+ANISOU  986  CB  TRP A 138     2307   2444   2469   -491    577   -412       C  
+ATOM    987  CG  TRP A 138      13.108   9.598  39.067  1.00 21.97           C  
+ANISOU  987  CG  TRP A 138     2504   2989   2855   -549    553   -458       C  
+ATOM    988  CD1 TRP A 138      12.223  10.567  38.651  1.00 18.40           C  
+ANISOU  988  CD1 TRP A 138     1972   2721   2299   -415    525   -527       C  
+ATOM    989  CD2 TRP A 138      12.326   8.595  39.718  1.00 20.77           C  
+ANISOU  989  CD2 TRP A 138     2202   2854   2835   -752    557   -411       C  
+ATOM    990  NE1 TRP A 138      10.946  10.218  39.008  1.00 21.65           N  
+ANISOU  990  NE1 TRP A 138     2169   3300   2756   -514    512   -544       N  
+ATOM    991  CE2 TRP A 138      10.981   9.016  39.667  1.00 22.23           C  
+ANISOU  991  CE2 TRP A 138     2182   3274   2990   -742    539   -454       C  
+ATOM    992  CE3 TRP A 138      12.635   7.385  40.351  1.00 24.98           C  
+ANISOU  992  CE3 TRP A 138     2745   3225   3521   -939    579   -305       C  
+ATOM    993  CZ2 TRP A 138       9.946   8.271  40.226  1.00 23.86           C  
+ANISOU  993  CZ2 TRP A 138     2153   3582   3329   -941    555   -376       C  
+ATOM    994  CZ3 TRP A 138      11.605   6.646  40.901  1.00 28.65           C  
+ANISOU  994  CZ3 TRP A 138     3010   3745   4132  -1144    593   -210       C  
+ATOM    995  CH2 TRP A 138      10.278   7.092  40.838  1.00 26.65           C  
+ANISOU  995  CH2 TRP A 138     2514   3751   3860  -1157    587   -236       C  
+ATOM    996  N   THR A 139      13.585   8.282  35.792  1.00 23.09           N  
+ANISOU  996  N   THR A 139     2801   3010   2963   -348    272   -808       N  
+ATOM    997  CA  THR A 139      13.040   8.581  34.478  1.00 24.17           C  
+ANISOU  997  CA  THR A 139     2919   3298   2966   -152    157   -971       C  
+ATOM    998  C   THR A 139      11.567   8.997  34.542  1.00 30.98           C  
+ANISOU  998  C   THR A 139     3587   4348   3838   -191     94  -1043       C  
+ATOM    999  O   THR A 139      10.899   9.083  33.515  1.00 32.57           O  
+ANISOU  999  O   THR A 139     3735   4694   3945    -45    -42  -1212       O  
+ATOM   1000  CB  THR A 139      13.210   7.374  33.525  1.00 28.79           C  
+ANISOU 1000  CB  THR A 139     3572   3790   3577    -97    -21  -1182       C  
+ATOM   1001  OG1 THR A 139      12.533   6.234  34.063  1.00 31.76           O  
+ANISOU 1001  OG1 THR A 139     3853   4004   4212   -369   -145  -1265       O  
+ATOM   1002  CG2 THR A 139      14.693   7.040  33.339  1.00 26.75           C  
+ANISOU 1002  CG2 THR A 139     3495   3418   3252     26     52  -1114       C  
+ATOM   1003  N   GLY A 140      11.065   9.270  35.746  1.00 27.98           N  
+ANISOU 1003  N   GLY A 140     3086   4005   3539   -348    191   -919       N  
+ATOM   1004  CA  GLY A 140       9.731   9.831  35.894  1.00 30.26           C  
+ANISOU 1004  CA  GLY A 140     3166   4534   3798   -333    167   -956       C  
+ATOM   1005  C   GLY A 140       8.825   9.003  36.782  1.00 31.83           C  
+ANISOU 1005  C   GLY A 140     3127   4771   4197   -609    164   -909       C  
+ATOM   1006  O   GLY A 140       8.047   9.540  37.571  1.00 32.26           O  
+ANISOU 1006  O   GLY A 140     3009   5035   4216   -614    253   -818       O  
+ATOM   1007  N   GLY A 141       8.925   7.684  36.651  1.00 27.63           N  
+ANISOU 1007  N   GLY A 141     2580   4038   3880   -824     61   -956       N  
+ATOM   1008  CA  GLY A 141       8.149   6.781  37.475  1.00 26.59           C  
+ANISOU 1008  CA  GLY A 141     2216   3887   3999  -1135     64   -845       C  
+ATOM   1009  C   GLY A 141       8.960   5.646  38.082  1.00 33.61           C  
+ANISOU 1009  C   GLY A 141     3232   4454   5084  -1340     94   -715       C  
+ATOM   1010  O   GLY A 141       8.437   4.842  38.859  1.00 33.78           O  
+ANISOU 1010  O   GLY A 141     3081   4417   5336  -1614    126   -547       O  
+ATOM   1011  N   LYS A 142      10.240   5.574  37.728  1.00 27.74           N  
+ANISOU 1011  N   LYS A 142     2776   3514   4250  -1197     93   -764       N  
+ATOM   1012  CA  LYS A 142      11.117   4.552  38.291  1.00 28.12           C  
+ANISOU 1012  CA  LYS A 142     2972   3263   4447  -1328    119   -649       C  
+ATOM   1013  C   LYS A 142      12.585   4.911  38.099  1.00 25.04           C  
+ANISOU 1013  C   LYS A 142     2850   2793   3872  -1101    187   -655       C  
+ATOM   1014  O   LYS A 142      12.924   5.816  37.328  1.00 27.03           O  
+ANISOU 1014  O   LYS A 142     3173   3177   3919   -868    190   -753       O  
+ATOM   1015  CB  LYS A 142      10.822   3.189  37.657  1.00 30.38           C  
+ANISOU 1015  CB  LYS A 142     3259   3270   5015  -1501   -123   -804       C  
+ATOM   1016  CG  LYS A 142      11.134   3.127  36.187  1.00 31.62           C  
+ANISOU 1016  CG  LYS A 142     3562   3385   5066  -1269   -336  -1132       C  
+ATOM   1017  CD  LYS A 142      10.858   1.742  35.635  1.00 39.48           C  
+ANISOU 1017  CD  LYS A 142     4613   4093   6294  -1379   -613  -1280       C  
+ATOM   1018  CE  LYS A 142      11.076   1.697  34.137  1.00 43.40           C  
+ANISOU 1018  CE  LYS A 142     5244   4614   6633  -1083   -837  -1637       C  
+ATOM   1019  NZ  LYS A 142      10.703   0.369  33.572  1.00 47.81           N  
+ANISOU 1019  NZ  LYS A 142     5871   4934   7359  -1147  -1097  -1767       N  
+ATOM   1020  N   TRP A 143      13.457   4.199  38.809  1.00 26.56           N  
+ANISOU 1020  N   TRP A 143     3170   2777   4144  -1168    246   -520       N  
+ATOM   1021  CA  TRP A 143      14.892   4.274  38.560  1.00 24.89           C  
+ANISOU 1021  CA  TRP A 143     3176   2478   3804   -972    280   -535       C  
+ATOM   1022  C   TRP A 143      15.275   3.325  37.435  1.00 23.48           C  
+ANISOU 1022  C   TRP A 143     3135   2108   3678   -878     90   -750       C  
+ATOM   1023  O   TRP A 143      14.844   2.172  37.420  1.00 24.35           O  
+ANISOU 1023  O   TRP A 143     3251   1982   4020  -1037    -59   -814       O  
+ATOM   1024  CB  TRP A 143      15.695   3.927  39.822  1.00 23.47           C  
+ANISOU 1024  CB  TRP A 143     3069   2195   3655  -1033    408   -314       C  
+ATOM   1025  CG  TRP A 143      15.633   4.980  40.886  1.00 24.30           C  
+ANISOU 1025  CG  TRP A 143     3091   2511   3629  -1015    571   -155       C  
+ATOM   1026  CD1 TRP A 143      14.787   5.016  41.964  1.00 25.31           C  
+ANISOU 1026  CD1 TRP A 143     3072   2767   3776  -1121    650     11       C  
+ATOM   1027  CD2 TRP A 143      16.446   6.149  40.971  1.00 21.19           C  
+ANISOU 1027  CD2 TRP A 143     2754   2237   3059   -841    639   -150       C  
+ATOM   1028  NE1 TRP A 143      15.027   6.149  42.716  1.00 26.35           N  
+ANISOU 1028  NE1 TRP A 143     3194   3090   3727   -995    757     65       N  
+ATOM   1029  CE2 TRP A 143      16.044   6.858  42.129  1.00 24.36           C  
+ANISOU 1029  CE2 TRP A 143     3070   2799   3385   -848    735    -39       C  
+ATOM   1030  CE3 TRP A 143      17.486   6.665  40.191  1.00 19.04           C  
+ANISOU 1030  CE3 TRP A 143     2581   1955   2698   -676    625   -214       C  
+ATOM   1031  CZ2 TRP A 143      16.646   8.051  42.517  1.00 25.68           C  
+ANISOU 1031  CZ2 TRP A 143     3278   3056   3424   -709    767    -39       C  
+ATOM   1032  CZ3 TRP A 143      18.078   7.854  40.576  1.00 18.54           C  
+ANISOU 1032  CZ3 TRP A 143     2521   1982   2541   -587    685   -156       C  
+ATOM   1033  CH2 TRP A 143      17.659   8.533  41.728  1.00 23.37           C  
+ANISOU 1033  CH2 TRP A 143     3076   2692   3113   -609    731    -94       C  
+ATOM   1034  N   GLU A 144      16.075   3.814  36.491  1.00 21.92           N  
+ANISOU 1034  N   GLU A 144     3044   2013   3272   -605     88   -855       N  
+ATOM   1035  CA  GLU A 144      16.547   2.975  35.401  1.00 27.55           C  
+ANISOU 1035  CA  GLU A 144     3902   2610   3955   -415    -84  -1077       C  
+ATOM   1036  C   GLU A 144      18.046   3.129  35.284  1.00 22.08           C  
+ANISOU 1036  C   GLU A 144     3338   1961   3089   -182     33   -995       C  
+ATOM   1037  O   GLU A 144      18.604   4.155  35.662  1.00 24.03           O  
+ANISOU 1037  O   GLU A 144     3536   2372   3221   -147    217   -808       O  
+ATOM   1038  CB  GLU A 144      15.879   3.338  34.072  1.00 28.88           C  
+ANISOU 1038  CB  GLU A 144     4030   2959   3984   -234   -225  -1315       C  
+ATOM   1039  CG  GLU A 144      14.361   3.308  34.093  1.00 29.67           C  
+ANISOU 1039  CG  GLU A 144     3947   3081   4245   -447   -354  -1411       C  
+ATOM   1040  CD  GLU A 144      13.762   3.264  32.706  1.00 35.68           C  
+ANISOU 1040  CD  GLU A 144     4698   3964   4893   -240   -584  -1723       C  
+ATOM   1041  OE1 GLU A 144      14.093   2.327  31.955  1.00 38.42           O  
+ANISOU 1041  OE1 GLU A 144     5187   4165   5246    -90   -790  -1955       O  
+ATOM   1042  OE2 GLU A 144      12.956   4.154  32.369  1.00 36.57           O  
+ANISOU 1042  OE2 GLU A 144     4671   4332   4894   -192   -571  -1742       O  
+ATOM   1043  N   GLU A 145      18.697   2.090  34.776  1.00 23.17           N  
+ANISOU 1043  N   GLU A 145     3632   1944   3227    -18    -92  -1140       N  
+ATOM   1044  CA  GLU A 145      20.120   2.184  34.482  1.00 23.25           C  
+ANISOU 1044  CA  GLU A 145     3728   2064   3043    260     12  -1078       C  
+ATOM   1045  C   GLU A 145      20.400   3.402  33.597  1.00 21.73           C  
+ANISOU 1045  C   GLU A 145     3452   2218   2587    480    137  -1023       C  
+ATOM   1046  O   GLU A 145      19.679   3.666  32.638  1.00 25.24           O  
+ANISOU 1046  O   GLU A 145     3874   2794   2922    599     46  -1177       O  
+ATOM   1047  CB  GLU A 145      20.610   0.903  33.804  1.00 27.10           C  
+ANISOU 1047  CB  GLU A 145     4400   2381   3516    498   -181  -1313       C  
+ATOM   1048  CG  GLU A 145      22.095   0.927  33.490  1.00 41.66           C  
+ANISOU 1048  CG  GLU A 145     6299   4395   5135    828    -62  -1240       C  
+ATOM   1049  CD  GLU A 145      22.583  -0.341  32.816  1.00 52.91           C  
+ANISOU 1049  CD  GLU A 145     7858   5723   6521   1073   -242  -1427       C  
+ATOM   1050  OE1 GLU A 145      22.059  -0.695  31.733  1.00 56.24           O  
+ANISOU 1050  OE1 GLU A 145     8287   6213   6869   1199   -415  -1618       O  
+ATOM   1051  OE2 GLU A 145      23.515  -0.968  33.364  1.00 60.11           O  
+ANISOU 1051  OE2 GLU A 145     8847   6527   7465   1142   -214  -1351       O  
+ATOM   1052  N   TYR A 146      21.441   4.144  33.942  1.00 22.91           N  
+ANISOU 1052  N   TYR A 146     3329   1936   3441   -387     31   -579       N  
+ATOM   1053  CA  TYR A 146      21.797   5.358  33.208  1.00 18.72           C  
+ANISOU 1053  CA  TYR A 146     2806   1607   2700   -244    116   -559       C  
+ATOM   1054  C   TYR A 146      22.414   4.981  31.860  1.00 27.45           C  
+ANISOU 1054  C   TYR A 146     4032   2783   3615    -15     28   -703       C  
+ATOM   1055  O   TYR A 146      23.236   4.060  31.781  1.00 31.81           O  
+ANISOU 1055  O   TYR A 146     4684   3275   4128     91      0   -772       O  
+ATOM   1056  CB  TYR A 146      22.750   6.200  34.057  1.00 17.02           C  
+ANISOU 1056  CB  TYR A 146     2584   1458   2426   -273    310   -394       C  
+ATOM   1057  CG  TYR A 146      23.067   7.547  33.463  1.00 18.13           C  
+ANISOU 1057  CG  TYR A 146     2743   1742   2403   -205    393   -313       C  
+ATOM   1058  CD1 TYR A 146      22.096   8.550  33.404  1.00 16.58           C  
+ANISOU 1058  CD1 TYR A 146     2540   1567   2193   -210    395   -275       C  
+ATOM   1059  CD2 TYR A 146      24.338   7.829  32.991  1.00 20.29           C  
+ANISOU 1059  CD2 TYR A 146     3035   2138   2538   -130    477   -241       C  
+ATOM   1060  CE1 TYR A 146      22.391   9.783  32.853  1.00 17.52           C  
+ANISOU 1060  CE1 TYR A 146     2731   1757   2168   -148    460   -179       C  
+ATOM   1061  CE2 TYR A 146      24.639   9.056  32.446  1.00 19.22           C  
+ANISOU 1061  CE2 TYR A 146     2918   2104   2280   -116    556   -111       C  
+ATOM   1062  CZ  TYR A 146      23.664  10.033  32.391  1.00 19.23           C  
+ANISOU 1062  CZ  TYR A 146     2974   2055   2278   -132    540    -85       C  
+ATOM   1063  OH  TYR A 146      23.976  11.256  31.840  1.00 20.80           O  
+ANISOU 1063  OH  TYR A 146     3244   2298   2361   -119    609     66       O  
+ATOM   1064  N   LYS A 147      21.993   5.645  30.787  1.00 24.82           N  
+ANISOU 1064  N   LYS A 147     3710   2591   3129    115    -17   -749       N  
+ATOM   1065  CA  LYS A 147      22.381   5.173  29.461  1.00 25.37           C  
+ANISOU 1065  CA  LYS A 147     3913   2746   2980    389   -126   -908       C  
+ATOM   1066  C   LYS A 147      23.479   6.005  28.796  1.00 22.74           C  
+ANISOU 1066  C   LYS A 147     3598   2666   2376    595     74   -764       C  
+ATOM   1067  O   LYS A 147      24.184   5.501  27.935  1.00 24.50           O  
+ANISOU 1067  O   LYS A 147     3918   3010   2380    872     63   -841       O  
+ATOM   1068  CB  LYS A 147      21.146   5.100  28.563  1.00 33.15           C  
+ANISOU 1068  CB  LYS A 147     4913   3737   3946    443   -366  -1082       C  
+ATOM   1069  CG  LYS A 147      20.207   3.957  28.955  1.00 39.36           C  
+ANISOU 1069  CG  LYS A 147     5676   4274   5004    235   -625  -1236       C  
+ATOM   1070  CD  LYS A 147      19.094   3.732  27.938  1.00 47.58           C  
+ANISOU 1070  CD  LYS A 147     6720   5334   6023    286   -939  -1447       C  
+ATOM   1071  CE  LYS A 147      17.994   2.836  28.518  1.00 46.68           C  
+ANISOU 1071  CE  LYS A 147     6479   4994   6264    -51  -1182  -1504       C  
+ATOM   1072  NZ  LYS A 147      17.099   3.641  29.415  1.00 54.25           N  
+ANISOU 1072  NZ  LYS A 147     7133   6081   7400   -273  -1030  -1274       N  
+ATOM   1073  N   ASP A 148      23.660   7.258  29.230  1.00 21.28           N  
+ANISOU 1073  N   ASP A 148     3327   2556   2203    465    256   -538       N  
+ATOM   1074  CA  ASP A 148      24.596   8.153  28.536  1.00 25.16           C  
+ANISOU 1074  CA  ASP A 148     3813   3272   2474    591    436   -342       C  
+ATOM   1075  C   ASP A 148      26.037   8.040  29.038  1.00 21.89           C  
+ANISOU 1075  C   ASP A 148     3304   2959   2054    548    597   -182       C  
+ATOM   1076  O   ASP A 148      26.959   8.572  28.416  1.00 24.05           O  
+ANISOU 1076  O   ASP A 148     3517   3469   2153    647    753     14       O  
+ATOM   1077  CB  ASP A 148      24.129   9.611  28.653  1.00 24.12           C  
+ANISOU 1077  CB  ASP A 148     3682   3123   2357    466    514   -163       C  
+ATOM   1078  CG  ASP A 148      23.009   9.947  27.690  1.00 26.53           C  
+ANISOU 1078  CG  ASP A 148     4066   3478   2537    641    401   -255       C  
+ATOM   1079  OD1 ASP A 148      22.969   9.351  26.589  1.00 24.95           O  
+ANISOU 1079  OD1 ASP A 148     3927   3412   2142    902    309   -391       O  
+ATOM   1080  OD2 ASP A 148      22.177  10.823  28.019  1.00 24.01           O  
+ANISOU 1080  OD2 ASP A 148     3762   3079   2283    562    390   -200       O  
+ATOM   1081  N   LEU A 149      26.238   7.350  30.152  1.00 21.64           N  
+ANISOU 1081  N   LEU A 149     3236   2780   2207    406    565   -235       N  
+ATOM   1082  CA  LEU A 149      27.588   7.072  30.631  1.00 25.39           C  
+ANISOU 1082  CA  LEU A 149     3602   3383   2663    410    679   -115       C  
+ATOM   1083  C   LEU A 149      27.660   5.641  31.153  1.00 21.09           C  
+ANISOU 1083  C   LEU A 149     3123   2697   2192    498    573   -294       C  
+ATOM   1084  O   LEU A 149      26.782   5.197  31.893  1.00 23.10           O  
+ANISOU 1084  O   LEU A 149     3443   2693   2640    347    459   -402       O  
+ATOM   1085  CB  LEU A 149      28.010   8.056  31.727  1.00 19.77           C  
+ANISOU 1085  CB  LEU A 149     2782   2632   2098    106    759     83       C  
+ATOM   1086  CG  LEU A 149      29.498   7.983  32.114  1.00 28.18           C  
+ANISOU 1086  CG  LEU A 149     3666   3905   3136     84    860    249       C  
+ATOM   1087  CD1 LEU A 149      30.392   8.584  31.035  1.00 35.76           C  
+ANISOU 1087  CD1 LEU A 149     4485   5193   3908    182   1010    475       C  
+ATOM   1088  CD2 LEU A 149      29.771   8.633  33.466  1.00 24.14           C  
+ANISOU 1088  CD2 LEU A 149     3097   3272   2802   -223    836    344       C  
+ATOM   1089  N   ALA A 150      28.694   4.920  30.738  1.00 25.59           N  
+ANISOU 1089  N   ALA A 150     3681   3449   2593    768    619   -302       N  
+ATOM   1090  CA  ALA A 150      28.835   3.517  31.108  1.00 31.16           C  
+ANISOU 1090  CA  ALA A 150     4519   3989   3330    922    505   -476       C  
+ATOM   1091  C   ALA A 150      29.255   3.359  32.565  1.00 26.24           C  
+ANISOU 1091  C   ALA A 150     3809   3269   2891    721    543   -377       C  
+ATOM   1092  O   ALA A 150      29.944   4.228  33.107  1.00 25.67           O  
+ANISOU 1092  O   ALA A 150     3540   3374   2839    564    667   -176       O  
+ATOM   1093  CB  ALA A 150      29.837   2.841  30.199  1.00 30.38           C  
+ANISOU 1093  CB  ALA A 150     4460   4145   2937   1366    548   -518       C  
+ATOM   1094  N   PRO A 151      28.853   2.243  33.201  1.00 29.75           N  
+ANISOU 1094  N   PRO A 151     4416   3421   3468    721    415   -508       N  
+ATOM   1095  CA  PRO A 151      29.447   1.910  34.496  1.00 28.35           C  
+ANISOU 1095  CA  PRO A 151     4185   3200   3387    647    459   -408       C  
+ATOM   1096  C   PRO A 151      30.961   1.813  34.357  1.00 27.55           C  
+ANISOU 1096  C   PRO A 151     3942   3440   3085    907    570   -309       C  
+ATOM   1097  O   PRO A 151      31.461   1.516  33.267  1.00 28.08           O  
+ANISOU 1097  O   PRO A 151     4032   3706   2932   1231    593   -361       O  
+ATOM   1098  CB  PRO A 151      28.836   0.549  34.826  1.00 31.72           C  
+ANISOU 1098  CB  PRO A 151     4861   3255   3936    692    300   -556       C  
+ATOM   1099  CG  PRO A 151      28.472  -0.030  33.497  1.00 34.99           C  
+ANISOU 1099  CG  PRO A 151     5468   3590   4236    917    153   -770       C  
+ATOM   1100  CD  PRO A 151      27.989   1.156  32.709  1.00 33.56           C  
+ANISOU 1100  CD  PRO A 151     5150   3603   3997    817    205   -742       C  
+ATOM   1101  N   TYR A 152      31.693   2.068  35.431  1.00 24.66           N  
+ANISOU 1101  N   TYR A 152     3414   3185   2770    799    632   -161       N  
+ATOM   1102  CA  TYR A 152      33.138   2.073  35.315  1.00 27.76           C  
+ANISOU 1102  CA  TYR A 152     3583   3976   2988   1013    730    -30       C  
+ATOM   1103  C   TYR A 152      33.827   1.396  36.476  1.00 29.18           C  
+ANISOU 1103  C   TYR A 152     3740   4158   3188   1098    702      7       C  
+ATOM   1104  O   TYR A 152      33.238   1.199  37.535  1.00 28.02           O  
+ANISOU 1104  O   TYR A 152     3722   3725   3200    921    634    -18       O  
+ATOM   1105  CB  TYR A 152      33.668   3.502  35.167  1.00 27.05           C  
+ANISOU 1105  CB  TYR A 152     3188   4192   2900    766    834    187       C  
+ATOM   1106  CG  TYR A 152      33.079   4.517  36.117  1.00 28.11           C  
+ANISOU 1106  CG  TYR A 152     3314   4127   3238    344    783    239       C  
+ATOM   1107  CD1 TYR A 152      31.949   5.236  35.769  1.00 26.82           C  
+ANISOU 1107  CD1 TYR A 152     3277   3755   3157    156    765    193       C  
+ATOM   1108  CD2 TYR A 152      33.683   4.791  37.340  1.00 27.80           C  
+ANISOU 1108  CD2 TYR A 152     3151   4136   3275    184    738    325       C  
+ATOM   1109  CE1 TYR A 152      31.420   6.187  36.614  1.00 27.43           C  
+ANISOU 1109  CE1 TYR A 152     3383   3664   3374   -147    720    230       C  
+ATOM   1110  CE2 TYR A 152      33.162   5.745  38.198  1.00 24.61           C  
+ANISOU 1110  CE2 TYR A 152     2795   3547   3009   -136    669    343       C  
+ATOM   1111  CZ  TYR A 152      32.029   6.433  37.829  1.00 26.77           C  
+ANISOU 1111  CZ  TYR A 152     3220   3604   3349   -283    669    295       C  
+ATOM   1112  OH  TYR A 152      31.496   7.381  38.667  1.00 30.87           O  
+ANISOU 1112  OH  TYR A 152     3826   3943   3961   -520    601    299       O  
+ATOM   1113  N   ARG A 153      35.081   1.019  36.241  1.00 32.46           N  
+ANISOU 1113  N   ARG A 153     3982   4940   3412   1418    767     85       N  
+ATOM   1114  CA  ARG A 153      35.895   0.402  37.273  1.00 36.23           C  
+ANISOU 1114  CA  ARG A 153     4400   5504   3861   1567    738    138       C  
+ATOM   1115  C   ARG A 153      36.321   1.450  38.290  1.00 35.88           C  
+ANISOU 1115  C   ARG A 153     4071   5626   3936   1204    727    303       C  
+ATOM   1116  O   ARG A 153      36.755   2.544  37.927  1.00 37.00           O  
+ANISOU 1116  O   ARG A 153     3923   6047   4090    985    779    450       O  
+ATOM   1117  CB  ARG A 153      37.127  -0.285  36.667  1.00 42.89           C  
+ANISOU 1117  CB  ARG A 153     5107   6759   4431   2076    812    181       C  
+ATOM   1118  N   VAL A 154      36.161   1.122  39.565  1.00 33.16           N  
+ANISOU 1118  N   VAL A 154     3842   5081   3676   1138    641    283       N  
+ATOM   1119  CA  VAL A 154      36.746   1.928  40.626  1.00 40.59           C  
+ANISOU 1119  CA  VAL A 154     4550   6202   4669    896    575    399       C  
+ATOM   1120  C   VAL A 154      38.050   1.211  41.017  1.00 41.09           C  
+ANISOU 1120  C   VAL A 154     4418   6621   4572   1237    558    474       C  
+ATOM   1121  O   VAL A 154      38.063   0.004  41.276  1.00 45.77           O  
+ANISOU 1121  O   VAL A 154     5238   7079   5075   1591    550    405       O  
+ATOM   1122  CB  VAL A 154      35.769   2.137  41.846  1.00 36.36           C  
+ANISOU 1122  CB  VAL A 154     4253   5292   4269    660    493    341       C  
+ATOM   1123  CG1 VAL A 154      34.379   2.542  41.362  1.00 40.21           C  
+ANISOU 1123  CG1 VAL A 154     4945   5448   4884    447    529    262       C  
+ATOM   1124  CG2 VAL A 154      35.664   0.919  42.739  1.00 38.68           C  
+ANISOU 1124  CG2 VAL A 154     4779   5398   4519    916    467    311       C  
+ATOM   1125  N   ASN A 155      39.160   1.938  40.984  1.00 38.18           N  
+ANISOU 1125  N   ASN A 155     3620   6717   4168   1139    545    633       N  
+ATOM   1126  CA  ASN A 155      40.444   1.357  41.360  1.00 47.58           C  
+ANISOU 1126  CA  ASN A 155     4537   8339   5200   1461    518    729       C  
+ATOM   1127  C   ASN A 155      40.594   1.390  42.878  1.00 48.84           C  
+ANISOU 1127  C   ASN A 155     4730   8427   5398   1363    341    711       C  
+ATOM   1128  O   ASN A 155      41.460   0.731  43.457  1.00 56.20           O  
+ANISOU 1128  O   ASN A 155     5539   9625   6191   1677    285    753       O  
+ATOM   1129  CB  ASN A 155      41.592   2.108  40.686  1.00 55.20           C  
+ANISOU 1129  CB  ASN A 155     4952   9897   6125   1374    574    953       C  
+ATOM   1130  N   GLN A 156      39.712   2.165  43.499  1.00 37.82           N  
+ANISOU 1130  N   GLN A 156     3524   6684   4160    974    255    643       N  
+ATOM   1131  CA  GLN A 156      39.760   2.495  44.915  1.00 43.55           C  
+ANISOU 1131  CA  GLN A 156     4299   7346   4901    838     71    615       C  
+ATOM   1132  C   GLN A 156      39.225   1.374  45.799  1.00 41.20           C  
+ANISOU 1132  C   GLN A 156     4377   6760   4516   1147     84    543       C  
+ATOM   1133  O   GLN A 156      38.455   0.517  45.356  1.00 35.38           O  
+ANISOU 1133  O   GLN A 156     3939   5715   3790   1321    215    495       O  
+ATOM   1134  CB  GLN A 156      38.951   3.776  45.174  1.00 44.81           C  
+ANISOU 1134  CB  GLN A 156     4574   7234   5218    377    -14    561       C  
+ATOM   1135  CG  GLN A 156      37.487   3.654  44.737  1.00 46.59           C  
+ANISOU 1135  CG  GLN A 156     5165   7015   5524    334    129    470       C  
+ATOM   1136  CD  GLN A 156      36.614   4.822  45.165  1.00 48.66           C  
+ANISOU 1136  CD  GLN A 156     5590   7011   5889     -7     50    408       C  
+ATOM   1137  OE1 GLN A 156      36.904   5.975  44.855  1.00 51.31           O  
+ANISOU 1137  OE1 GLN A 156     5772   7421   6304   -310    -38    444       O  
+ATOM   1138  NE2 GLN A 156      35.525   4.522  45.874  1.00 46.52           N  
+ANISOU 1138  NE2 GLN A 156     5640   6427   5608     58     88    338       N  
+ATOM   1139  N   ILE A 157      39.630   1.405  47.062  1.00 38.44           N  
+ANISOU 1139  N   ILE A 157     4020   6503   4082   1197    -72    549       N  
+ATOM   1140  CA  ILE A 157      39.110   0.487  48.065  1.00 38.13           C  
+ANISOU 1140  CA  ILE A 157     4341   6200   3948   1460    -56    533       C  
+ATOM   1141  C   ILE A 157      37.592   0.625  48.108  1.00 35.85           C  
+ANISOU 1141  C   ILE A 157     4401   5434   3785   1259     54    487       C  
+ATOM   1142  O   ILE A 157      37.052   1.732  48.014  1.00 31.45           O  
+ANISOU 1142  O   ILE A 157     3822   4794   3332    918     22    437       O  
+ATOM   1143  CB  ILE A 157      39.708   0.777  49.454  1.00 47.25           C  
+ANISOU 1143  CB  ILE A 157     5434   7554   4966   1510   -266    537       C  
+ATOM   1144  CG1 ILE A 157      39.055  -0.087  50.526  1.00 45.94           C  
+ANISOU 1144  CG1 ILE A 157     5667   7109   4680   1778   -213    567       C  
+ATOM   1145  CG2 ILE A 157      39.516   2.239  49.821  1.00 46.06           C  
+ANISOU 1145  CG2 ILE A 157     5206   7395   4902   1082   -438    462       C  
+ATOM   1146  CD1 ILE A 157      40.015  -0.531  51.599  1.00 52.40           C  
+ANISOU 1146  CD1 ILE A 157     6425   8218   5268   2115   -370    610       C  
+ATOM   1147  N   ALA A 158      36.895  -0.499  48.218  1.00 32.63           N  
+ANISOU 1147  N   ALA A 158     4310   4712   3375   1469    176    520       N  
+ATOM   1148  CA  ALA A 158      35.442  -0.456  48.335  1.00 34.48           C  
+ANISOU 1148  CA  ALA A 158     4813   4548   3739   1277    283    524       C  
+ATOM   1149  C   ALA A 158      34.995  -1.378  49.458  1.00 31.15           C  
+ANISOU 1149  C   ALA A 158     4680   3916   3241   1484    336    645       C  
+ATOM   1150  O   ALA A 158      34.806  -2.575  49.239  1.00 31.56           O  
+ANISOU 1150  O   ALA A 158     4939   3730   3322   1673    408    712       O  
+ATOM   1151  CB  ALA A 158      34.797  -0.851  47.033  1.00 35.54           C  
+ANISOU 1151  CB  ALA A 158     5022   4456   4026   1206    384    477       C  
+ATOM   1152  N   PRO A 159      34.852  -0.830  50.671  1.00 29.92           N  
+ANISOU 1152  N   PRO A 159     4566   3835   2966   1472    289    683       N  
+ATOM   1153  CA  PRO A 159      34.534  -1.653  51.841  1.00 31.66           C  
+ANISOU 1153  CA  PRO A 159     5043   3929   3059   1714    358    846       C  
+ATOM   1154  C   PRO A 159      33.129  -2.232  51.743  1.00 31.04           C  
+ANISOU 1154  C   PRO A 159     5189   3460   3146   1590    554    987       C  
+ATOM   1155  O   PRO A 159      32.307  -1.713  50.997  1.00 29.02           O  
+ANISOU 1155  O   PRO A 159     4873   3084   3070   1305    608    925       O  
+ATOM   1156  CB  PRO A 159      34.656  -0.674  53.013  1.00 32.24           C  
+ANISOU 1156  CB  PRO A 159     5093   4218   2939   1720    243    811       C  
+ATOM   1157  CG  PRO A 159      34.447   0.668  52.416  1.00 32.97           C  
+ANISOU 1157  CG  PRO A 159     5020   4365   3145   1381    163    646       C  
+ATOM   1158  CD  PRO A 159      34.930   0.605  50.995  1.00 29.16           C  
+ANISOU 1158  CD  PRO A 159     4325   3918   2836   1246    160    577       C  
+ATOM   1159  N   GLU A 160      32.870  -3.315  52.476  1.00 40.07           N  
+ANISOU 1159  N   GLU A 160     6444   3759   5020   1928    806   1606       N  
+ATOM   1160  CA  GLU A 160      31.581  -4.003  52.386  1.00 43.88           C  
+ANISOU 1160  CA  GLU A 160     7047   4043   5584   1788   1091   1607       C  
+ATOM   1161  C   GLU A 160      30.408  -3.092  52.735  1.00 45.23           C  
+ANISOU 1161  C   GLU A 160     7257   4273   5657   1638   1159   1577       C  
+ATOM   1162  O   GLU A 160      29.313  -3.242  52.195  1.00 50.06           O  
+ANISOU 1162  O   GLU A 160     7840   4744   6437   1456   1339   1509       O  
+ATOM   1163  CB  GLU A 160      31.577  -5.234  53.288  1.00 45.10           C  
+ANISOU 1163  CB  GLU A 160     7372   4046   5719   1905   1221   1766       C  
+ATOM   1164  CG  GLU A 160      32.548  -6.318  52.845  1.00 46.03           C  
+ANISOU 1164  CG  GLU A 160     7455   4048   5986   2034   1211   1794       C  
+ATOM   1165  CD  GLU A 160      32.021  -7.126  51.676  1.00 53.92           C  
+ANISOU 1165  CD  GLU A 160     8419   4824   7245   1897   1405   1676       C  
+ATOM   1166  OE1 GLU A 160      30.848  -6.927  51.294  1.00 57.61           O  
+ANISOU 1166  OE1 GLU A 160     8881   5204   7803   1694   1525   1584       O  
+ATOM   1167  OE2 GLU A 160      32.779  -7.960  51.138  1.00 60.52           O  
+ANISOU 1167  OE2 GLU A 160     9231   5556   8206   1993   1417   1662       O  
+ATOM   1168  N   SER A 161      30.652  -2.126  53.612  1.00 45.84           N  
+ANISOU 1168  N   SER A 161     7384   4547   5485   1709    990   1610       N  
+ATOM   1169  CA  SER A 161      29.616  -1.191  54.029  1.00 48.18           C  
+ANISOU 1169  CA  SER A 161     7729   4911   5666   1595   1060   1580       C  
+ATOM   1170  C   SER A 161      29.172  -0.255  52.897  1.00 42.97           C  
+ANISOU 1170  C   SER A 161     6897   4305   5125   1414   1032   1433       C  
+ATOM   1171  O   SER A 161      28.171   0.447  53.027  1.00 44.49           O  
+ANISOU 1171  O   SER A 161     7091   4518   5296   1288   1124   1399       O  
+ATOM   1172  CB  SER A 161      30.109  -0.363  55.214  1.00 51.16           C  
+ANISOU 1172  CB  SER A 161     8234   5476   5729   1730    844   1610       C  
+ATOM   1173  OG  SER A 161      30.997   0.653  54.779  1.00 46.56           O  
+ANISOU 1173  OG  SER A 161     7493   5080   5117   1735    532   1512       O  
+ATOM   1174  N   LEU A 162      29.920  -0.244  51.797  1.00 38.68           N  
+ANISOU 1174  N   LEU A 162     6209   3776   4712   1421    921   1349       N  
+ATOM   1175  CA  LEU A 162      29.613   0.611  50.654  1.00 37.29           C  
+ANISOU 1175  CA  LEU A 162     5900   3640   4629   1285    891   1206       C  
+ATOM   1176  C   LEU A 162      29.009  -0.189  49.487  1.00 36.13           C  
+ANISOU 1176  C   LEU A 162     5714   3279   4737   1145   1035   1076       C  
+ATOM   1177  O   LEU A 162      28.434   0.391  48.565  1.00 37.38           O  
+ANISOU 1177  O   LEU A 162     5761   3479   4961    966    995    888       O  
+ATOM   1178  CB  LEU A 162      30.887   1.353  50.201  1.00 34.17           C  
+ANISOU 1178  CB  LEU A 162     5323   3461   4200   1359    654   1127       C  
+ATOM   1179  CG  LEU A 162      30.909   2.431  49.112  1.00 38.68           C  
+ANISOU 1179  CG  LEU A 162     5694   4188   4813   1203    574    931       C  
+ATOM   1180  CD1 LEU A 162      30.118   3.677  49.493  1.00 35.08           C  
+ANISOU 1180  CD1 LEU A 162     5223   3877   4227   1060    507    872       C  
+ATOM   1181  CD2 LEU A 162      32.351   2.809  48.765  1.00 36.01           C  
+ANISOU 1181  CD2 LEU A 162     5169   3975   4538   1326    429    928       C  
+ATOM   1182  N   ARG A 163      29.124  -1.515  49.539  1.00 34.66           N  
+ANISOU 1182  N   ARG A 163     5609   2889   4673   1206   1156   1135       N  
+ATOM   1183  CA  ARG A 163      28.746  -2.378  48.413  1.00 40.61           C  
+ANISOU 1183  CA  ARG A 163     6361   3411   5659   1106   1236    986       C  
+ATOM   1184  C   ARG A 163      27.297  -2.844  48.420  1.00 41.67           C  
+ANISOU 1184  C   ARG A 163     6494   3331   6009    896   1360    942       C  
+ATOM   1185  O   ARG A 163      26.753  -3.200  49.465  1.00 42.11           O  
+ANISOU 1185  O   ARG A 163     6579   3344   6077    884   1498   1091       O  
+ATOM   1186  CB  ARG A 163      29.633  -3.625  48.369  1.00 38.19           C  
+ANISOU 1186  CB  ARG A 163     6108   3000   5403   1255   1278   1036       C  
+ATOM   1187  CG  ARG A 163      31.104  -3.356  48.205  1.00 35.70           C  
+ANISOU 1187  CG  ARG A 163     5720   2855   4988   1453   1165   1066       C  
+ATOM   1188  CD  ARG A 163      31.858  -4.657  48.041  1.00 41.18           C  
+ANISOU 1188  CD  ARG A 163     6457   3409   5780   1582   1236   1102       C  
+ATOM   1189  NE  ARG A 163      33.238  -4.544  48.494  1.00 40.47           N  
+ANISOU 1189  NE  ARG A 163     6268   3475   5634   1788   1124   1219       N  
+ATOM   1190  CZ  ARG A 163      34.111  -5.540  48.468  1.00 41.68           C  
+ANISOU 1190  CZ  ARG A 163     6421   3539   5875   1937   1162   1279       C  
+ATOM   1191  NH1 ARG A 163      33.746  -6.733  48.009  1.00 41.51           N  
+ANISOU 1191  NH1 ARG A 163     6525   3279   5969   1908   1321   1231       N  
+ATOM   1192  NH2 ARG A 163      35.348  -5.347  48.906  1.00 47.76           N  
+ANISOU 1192  NH2 ARG A 163     7054   4443   6648   2110   1018   1381       N  
+ATOM   1193  N   GLY A 164      26.696  -2.880  47.234  1.00 39.29           N  
+ANISOU 1193  N   GLY A 164     6152   2888   5887    742   1300    722       N  
+ATOM   1194  CA  GLY A 164      25.360  -3.423  47.065  1.00 37.66           C  
+ANISOU 1194  CA  GLY A 164     5878   2455   5975    526   1341    639       C  
+ATOM   1195  C   GLY A 164      24.280  -2.572  47.698  1.00 36.75           C  
+ANISOU 1195  C   GLY A 164     5634   2407   5922    385   1399    701       C  
+ATOM   1196  O   GLY A 164      23.229  -3.077  48.087  1.00 40.27           O  
+ANISOU 1196  O   GLY A 164     5980   2704   6616    256   1513    741       O  
+ATOM   1197  N   LYS A 165      24.549  -1.275  47.806  1.00 29.59           N  
+ANISOU 1197  N   LYS A 165     4716   1724   4802    423   1334    716       N  
+ATOM   1198  CA  LYS A 165      23.601  -0.339  48.388  1.00 40.37           C  
+ANISOU 1198  CA  LYS A 165     5971   3179   6191    312   1394    770       C  
+ATOM   1199  C   LYS A 165      23.398   0.804  47.413  1.00 26.64           C  
+ANISOU 1199  C   LYS A 165     4095   1647   4381    199   1147    542       C  
+ATOM   1200  O   LYS A 165      24.359   1.333  46.864  1.00 26.67           O  
+ANISOU 1200  O   LYS A 165     4131   1865   4138    286    986    454       O  
+ATOM   1201  CB  LYS A 165      24.095   0.188  49.740  1.00 53.40           C  
+ANISOU 1201  CB  LYS A 165     7731   5040   7519    482   1493    987       C  
+ATOM   1202  N   PHE A 166      22.148   1.172  47.181  1.00 27.01           N  
+ANISOU 1202  N   PHE A 166     3977   1608   4679     14   1131    462       N  
+ATOM   1203  CA  PHE A 166      21.863   2.284  46.287  1.00 25.20           C  
+ANISOU 1203  CA  PHE A 166     3635   1560   4381    -76    889    265       C  
+ATOM   1204  C   PHE A 166      22.015   3.626  47.003  1.00 25.17           C  
+ANISOU 1204  C   PHE A 166     3601   1846   4115    -26    919    358       C  
+ATOM   1205  O   PHE A 166      21.512   3.804  48.110  1.00 23.90           O  
+ANISOU 1205  O   PHE A 166     3432   1664   3987    -14   1131    530       O  
+ATOM   1206  CB  PHE A 166      20.449   2.149  45.718  1.00 26.96           C  
+ANISOU 1206  CB  PHE A 166     3665   1558   5021   -281    799    131       C  
+ATOM   1207  CG  PHE A 166      20.087   3.237  44.772  1.00 26.44           C  
+ANISOU 1207  CG  PHE A 166     3507   1654   4884   -349    523    -63       C  
+ATOM   1208  CD1 PHE A 166      20.351   3.106  43.418  1.00 27.36           C  
+ANISOU 1208  CD1 PHE A 166     3730   1751   4915   -340    238   -302       C  
+ATOM   1209  CD2 PHE A 166      19.515   4.418  45.232  1.00 24.38           C  
+ANISOU 1209  CD2 PHE A 166     3101   1558   4605   -388    561     -1       C  
+ATOM   1210  CE1 PHE A 166      20.039   4.136  42.537  1.00 27.26           C  
+ANISOU 1210  CE1 PHE A 166     3686   1883   4788   -366    -14   -459       C  
+ATOM   1211  CE2 PHE A 166      19.204   5.444  44.355  1.00 23.29           C  
+ANISOU 1211  CE2 PHE A 166     2893   1561   4396   -430    306   -162       C  
+ATOM   1212  CZ  PHE A 166      19.468   5.301  43.008  1.00 28.08           C  
+ANISOU 1212  CZ  PHE A 166     3614   2151   4905   -415     15   -383       C  
+ATOM   1213  N   TYR A 167      22.676   4.578  46.354  1.00 21.09           N  
+ANISOU 1213  N   TYR A 167     3091   1572   3351     12    727    244       N  
+ATOM   1214  CA  TYR A 167      22.761   5.938  46.871  1.00 19.39           C  
+ANISOU 1214  CA  TYR A 167     2836   1599   2932     33    711    287       C  
+ATOM   1215  C   TYR A 167      22.294   6.947  45.837  1.00 19.63           C  
+ANISOU 1215  C   TYR A 167     2758   1729   2972    -62    520    115       C  
+ATOM   1216  O   TYR A 167      22.791   6.949  44.720  1.00 18.84           O  
+ANISOU 1216  O   TYR A 167     2706   1662   2792    -41    367    -18       O  
+ATOM   1217  CB  TYR A 167      24.190   6.294  47.281  1.00 18.81           C  
+ANISOU 1217  CB  TYR A 167     2862   1724   2559    191    669    355       C  
+ATOM   1218  CG  TYR A 167      24.775   5.413  48.358  1.00 19.76           C  
+ANISOU 1218  CG  TYR A 167     3121   1774   2612    333    799    535       C  
+ATOM   1219  CD1 TYR A 167      24.515   5.669  49.694  1.00 23.04           C  
+ANISOU 1219  CD1 TYR A 167     3638   2208   2908    402    926    692       C  
+ATOM   1220  CD2 TYR A 167      25.598   4.346  48.035  1.00 24.23           C  
+ANISOU 1220  CD2 TYR A 167     3755   2245   3207    428    798    553       C  
+ATOM   1221  CE1 TYR A 167      25.044   4.873  50.684  1.00 26.92           C  
+ANISOU 1221  CE1 TYR A 167     4313   2627   3289    569   1026    870       C  
+ATOM   1222  CE2 TYR A 167      26.143   3.539  49.021  1.00 25.97           C  
+ANISOU 1222  CE2 TYR A 167     4112   2392   3362    583    899    734       C  
+ATOM   1223  CZ  TYR A 167      25.860   3.815  50.342  1.00 25.26           C  
+ANISOU 1223  CZ  TYR A 167     4138   2327   3130    656    998    894       C  
+ATOM   1224  OH  TYR A 167      26.394   3.036  51.334  1.00 30.02           O  
+ANISOU 1224  OH  TYR A 167     4933   2853   3619    846   1078   1086       O  
+ATOM   1225  N   SER A 168      21.349   7.806  46.211  1.00 19.35           N  
+ANISOU 1225  N   SER A 168     2603   1729   3020   -140    553    133       N  
+ATOM   1226  CA  SER A 168      21.061   8.998  45.413  1.00 16.74           C  
+ANISOU 1226  CA  SER A 168     2191   1533   2636   -188    375      8       C  
+ATOM   1227  C   SER A 168      22.211   9.981  45.553  1.00 16.83           C  
+ANISOU 1227  C   SER A 168     2281   1782   2333    -91    339     31       C  
+ATOM   1228  O   SER A 168      22.811  10.073  46.616  1.00 17.20           O  
+ANISOU 1228  O   SER A 168     2395   1899   2242    -12    439    148       O  
+ATOM   1229  CB  SER A 168      19.759   9.667  45.857  1.00 20.62           C  
+ANISOU 1229  CB  SER A 168     2515   1983   3337   -276    446     39       C  
+ATOM   1230  OG  SER A 168      18.660   8.806  45.655  1.00 26.49           O  
+ANISOU 1230  OG  SER A 168     3111   2475   4478   -386    461     15       O  
+ATOM   1231  N   LEU A 169      22.497  10.742  44.502  1.00 14.47           N  
+ANISOU 1231  N   LEU A 169     1979   1584   1933    -89    187    -77       N  
+ATOM   1232  CA  LEU A 169      23.596  11.700  44.564  1.00 16.85           C  
+ANISOU 1232  CA  LEU A 169     2308   2068   2026    -17    170    -49       C  
+ATOM   1233  C   LEU A 169      23.330  12.811  45.588  1.00 16.31           C  
+ANISOU 1233  C   LEU A 169     2193   2098   1907    -35    210     10       C  
+ATOM   1234  O   LEU A 169      24.267  13.428  46.099  1.00 16.97           O  
+ANISOU 1234  O   LEU A 169     2298   2291   1859     20    190     47       O  
+ATOM   1235  CB  LEU A 169      23.868  12.313  43.179  1.00 15.22           C  
+ANISOU 1235  CB  LEU A 169     2133   1914   1738      2     63   -147       C  
+ATOM   1236  CG  LEU A 169      24.416  11.393  42.079  1.00 16.07           C  
+ANISOU 1236  CG  LEU A 169     2372   1935   1798     78     44   -214       C  
+ATOM   1237  CD1 LEU A 169      24.952  12.255  40.939  1.00 15.60           C  
+ANISOU 1237  CD1 LEU A 169     2393   1950   1583    152     24   -251       C  
+ATOM   1238  CD2 LEU A 169      25.498  10.451  42.606  1.00 22.79           C  
+ANISOU 1238  CD2 LEU A 169     3253   2763   2645    163    158   -129       C  
+ATOM   1239  N   SER A 170      22.066  13.028  45.937  1.00 17.52           N  
+ANISOU 1239  N   SER A 170     2279   2184   2192   -102    266     15       N  
+ATOM   1240  CA  SER A 170      21.743  14.045  46.944  1.00 17.16           C  
+ANISOU 1240  CA  SER A 170     2236   2202   2081    -90    348     66       C  
+ATOM   1241  C   SER A 170      22.211  13.635  48.350  1.00 22.63           C  
+ANISOU 1241  C   SER A 170     3076   2889   2634      4    473    180       C  
+ATOM   1242  O   SER A 170      22.209  14.446  49.283  1.00 22.52           O  
+ANISOU 1242  O   SER A 170     3153   2926   2477     58    517    209       O  
+ATOM   1243  CB  SER A 170      20.244  14.332  46.946  1.00 14.03           C  
+ANISOU 1243  CB  SER A 170     1711   1712   1909   -160    425     63       C  
+ATOM   1244  OG  SER A 170      19.477  13.155  47.061  1.00 18.38           O  
+ANISOU 1244  OG  SER A 170     2195   2083   2706   -205    532    107       O  
+ATOM   1245  N   SER A 171      22.612  12.373  48.497  1.00 15.26           N  
+ANISOU 1245  N   SER A 171     2203   1876   1719     46    518    241       N  
+ATOM   1246  CA  SER A 171      23.244  11.912  49.720  1.00 17.09           C  
+ANISOU 1246  CA  SER A 171     2617   2104   1774    175    587    357       C  
+ATOM   1247  C   SER A 171      24.759  12.103  49.672  1.00 16.62           C  
+ANISOU 1247  C   SER A 171     2587   2168   1560    254    384    331       C  
+ATOM   1248  O   SER A 171      25.465  11.697  50.602  1.00 23.58           O  
+ANISOU 1248  O   SER A 171     3614   3053   2294    382    352    413       O  
+ATOM   1249  CB  SER A 171      22.919  10.421  49.974  1.00 17.78           C  
+ANISOU 1249  CB  SER A 171     2756   2011   1989    200    758    465       C  
+ATOM   1250  OG  SER A 171      21.546  10.249  50.291  1.00 23.78           O  
+ANISOU 1250  OG  SER A 171     3463   2618   2953    138    990    529       O  
+ATOM   1251  N   VAL A 172      25.265  12.700  48.594  1.00 15.67           N  
+ANISOU 1251  N   VAL A 172     2329   2131   1494    193    251    231       N  
+ATOM   1252  CA  VAL A 172      26.710  12.755  48.381  1.00 16.66           C  
+ANISOU 1252  CA  VAL A 172     2408   2331   1590    258    109    227       C  
+ATOM   1253  C   VAL A 172      27.221  14.184  48.156  1.00 16.07           C  
+ANISOU 1253  C   VAL A 172     2236   2361   1510    217    -18    157       C  
+ATOM   1254  O   VAL A 172      28.220  14.587  48.750  1.00 18.52           O  
+ANISOU 1254  O   VAL A 172     2525   2717   1795    272   -167    164       O  
+ATOM   1255  CB  VAL A 172      27.115  11.869  47.185  1.00 17.51           C  
+ANISOU 1255  CB  VAL A 172     2454   2386   1815    262    147    209       C  
+ATOM   1256  CG1 VAL A 172      28.647  11.772  47.058  1.00 21.89           C  
+ANISOU 1256  CG1 VAL A 172     2927   2985   2404    358     67    245       C  
+ATOM   1257  CG2 VAL A 172      26.514  10.472  47.351  1.00 17.25           C  
+ANISOU 1257  CG2 VAL A 172     2511   2205   1837    279    266    259       C  
+ATOM   1258  N   TYR A 173      26.548  14.942  47.303  1.00 16.44           N  
+ANISOU 1258  N   TYR A 173     2217   2422   1608    125     19     91       N  
+ATOM   1259  CA  TYR A 173      27.079  16.253  46.923  1.00 17.23           C  
+ANISOU 1259  CA  TYR A 173     2221   2587   1740     86    -63     44       C  
+ATOM   1260  C   TYR A 173      26.264  17.369  47.550  1.00 17.86           C  
+ANISOU 1260  C   TYR A 173     2349   2681   1757     41    -77      1       C  
+ATOM   1261  O   TYR A 173      25.060  17.243  47.716  1.00 18.73           O  
+ANISOU 1261  O   TYR A 173     2512   2754   1850     20     23      2       O  
+ATOM   1262  CB  TYR A 173      27.142  16.381  45.397  1.00 16.50           C  
+ANISOU 1262  CB  TYR A 173     2061   2487   1721     61      1     22       C  
+ATOM   1263  CG  TYR A 173      28.054  15.309  44.857  1.00 17.31           C  
+ANISOU 1263  CG  TYR A 173     2150   2556   1872    139     51     64       C  
+ATOM   1264  CD1 TYR A 173      29.423  15.364  45.103  1.00 17.46           C  
+ANISOU 1264  CD1 TYR A 173     2051   2591   1991    195     14    117       C  
+ATOM   1265  CD2 TYR A 173      27.545  14.201  44.197  1.00 17.39           C  
+ANISOU 1265  CD2 TYR A 173     2253   2493   1862    162    119     44       C  
+ATOM   1266  CE1 TYR A 173      30.269  14.358  44.663  1.00 18.58           C  
+ANISOU 1266  CE1 TYR A 173     2164   2688   2207    291     91    171       C  
+ATOM   1267  CE2 TYR A 173      28.384  13.200  43.736  1.00 14.36           C  
+ANISOU 1267  CE2 TYR A 173     1888   2056   1512    255    187     77       C  
+ATOM   1268  CZ  TYR A 173      29.744  13.286  43.972  1.00 18.93           C  
+ANISOU 1268  CZ  TYR A 173     2345   2663   2185    328    196    151       C  
+ATOM   1269  OH  TYR A 173      30.582  12.288  43.542  1.00 20.98           O  
+ANISOU 1269  OH  TYR A 173     2606   2858   2510    442    294    197       O  
+ATOM   1270  N   ARG A 174      26.954  18.451  47.893  1.00 16.83           N  
+ANISOU 1270  N   ARG A 174     2180   2580   1635     30   -197    -38       N  
+ATOM   1271  CA  ARG A 174      26.391  19.541  48.683  1.00 20.53           C  
+ANISOU 1271  CA  ARG A 174     2740   3041   2021     15   -231    -95       C  
+ATOM   1272  C   ARG A 174      25.691  20.567  47.788  1.00 17.95           C  
+ANISOU 1272  C   ARG A 174     2336   2708   1775    -60   -159   -128       C  
+ATOM   1273  O   ARG A 174      26.154  20.845  46.687  1.00 17.82           O  
+ANISOU 1273  O   ARG A 174     2203   2698   1870    -95   -150   -116       O  
+ATOM   1274  CB  ARG A 174      27.498  20.218  49.498  1.00 19.97           C  
+ANISOU 1274  CB  ARG A 174     2679   2966   1944     38   -454   -151       C  
+ATOM   1275  CG  ARG A 174      26.986  21.306  50.420  1.00 32.31           C  
+ANISOU 1275  CG  ARG A 174     4407   4492   3378     49   -511   -239       C  
+ATOM   1276  CD  ARG A 174      28.020  21.704  51.434  1.00 38.67           C  
+ANISOU 1276  CD  ARG A 174     5295   5266   4134     99   -806   -323       C  
+ATOM   1277  NE  ARG A 174      27.565  22.831  52.246  1.00 39.89           N  
+ANISOU 1277  NE  ARG A 174     5639   5355   4162    115   -855   -431       N  
+ATOM   1278  CZ  ARG A 174      28.250  23.326  53.268  1.00 38.73           C  
+ANISOU 1278  CZ  ARG A 174     5585   5141   3991    152  -1056   -505       C  
+ATOM   1279  NH1 ARG A 174      29.413  22.786  53.604  1.00 41.42           N  
+ANISOU 1279  NH1 ARG A 174     5849   5478   4410    183  -1270   -494       N  
+ATOM   1280  NH2 ARG A 174      27.775  24.359  53.955  1.00 48.96           N  
+ANISOU 1280  NH2 ARG A 174     7055   6359   5188    174  -1052   -595       N  
+ATOM   1281  N   VAL A 175      24.584  21.125  48.274  1.00 16.79           N  
+ANISOU 1281  N   VAL A 175     2273   2534   1571    -58    -83   -152       N  
+ATOM   1282  CA  VAL A 175      23.840  22.137  47.525  1.00 16.78           C  
+ANISOU 1282  CA  VAL A 175     2206   2517   1654   -105    -33   -175       C  
+ATOM   1283  C   VAL A 175      23.715  23.428  48.344  1.00 18.60           C  
+ANISOU 1283  C   VAL A 175     2525   2706   1838    -96    -59   -241       C  
+ATOM   1284  O   VAL A 175      23.377  23.394  49.537  1.00 18.13           O  
+ANISOU 1284  O   VAL A 175     2633   2617   1640    -29    -25   -262       O  
+ATOM   1285  CB  VAL A 175      22.433  21.617  47.142  1.00 23.38           C  
+ANISOU 1285  CB  VAL A 175     3007   3324   2551   -106     89   -142       C  
+ATOM   1286  CG1 VAL A 175      21.548  22.735  46.629  1.00 21.08           C  
+ANISOU 1286  CG1 VAL A 175     2660   3005   2346   -120    114   -161       C  
+ATOM   1287  CG2 VAL A 175      22.534  20.490  46.108  1.00 18.62           C  
+ANISOU 1287  CG2 VAL A 175     2340   2729   2006   -121     66   -118       C  
+ATOM   1288  N   TYR A 176      23.999  24.558  47.703  1.00 15.94           N  
+ANISOU 1288  N   TYR A 176     2112   2343   1601   -145   -101   -268       N  
+ATOM   1289  CA  TYR A 176      23.884  25.883  48.325  1.00 19.05           C  
+ANISOU 1289  CA  TYR A 176     2587   2663   1988   -146   -133   -347       C  
+ATOM   1290  C   TYR A 176      22.786  26.678  47.648  1.00 16.56           C  
+ANISOU 1290  C   TYR A 176     2229   2311   1750   -143    -12   -322       C  
+ATOM   1291  O   TYR A 176      22.282  26.279  46.593  1.00 17.40           O  
+ANISOU 1291  O   TYR A 176     2236   2454   1922   -147     38   -254       O  
+ATOM   1292  CB  TYR A 176      25.186  26.682  48.201  1.00 21.24           C  
+ANISOU 1292  CB  TYR A 176     2789   2888   2395   -212   -289   -395       C  
+ATOM   1293  CG  TYR A 176      26.436  26.050  48.764  1.00 18.82           C  
+ANISOU 1293  CG  TYR A 176     2456   2596   2100   -215   -472   -422       C  
+ATOM   1294  CD1 TYR A 176      26.884  26.377  50.033  1.00 21.83           C  
+ANISOU 1294  CD1 TYR A 176     2986   2920   2389   -183   -680   -541       C  
+ATOM   1295  CD2 TYR A 176      27.187  25.152  48.013  1.00 18.87           C  
+ANISOU 1295  CD2 TYR A 176     2304   2657   2209   -229   -457   -334       C  
+ATOM   1296  CE1 TYR A 176      28.036  25.831  50.547  1.00 28.99           C  
+ANISOU 1296  CE1 TYR A 176     3854   3829   3331   -170   -913   -569       C  
+ATOM   1297  CE2 TYR A 176      28.346  24.593  48.520  1.00 18.75           C  
+ANISOU 1297  CE2 TYR A 176     2225   2643   2256   -217   -633   -346       C  
+ATOM   1298  CZ  TYR A 176      28.764  24.939  49.783  1.00 24.98           C  
+ANISOU 1298  CZ  TYR A 176     3132   3381   2980   -191   -882   -462       C  
+ATOM   1299  OH  TYR A 176      29.910  24.399  50.309  1.00 25.48           O  
+ANISOU 1299  OH  TYR A 176     3122   3436   3122   -162  -1122   -479       O  
+ATOM   1300  N   ASP A 177      22.440  27.818  48.241  1.00 17.39           N  
+ANISOU 1300  N   ASP A 177     2429   2331   1848   -122      8   -388       N  
+ATOM   1301  CA  ASP A 177      21.617  28.809  47.560  1.00 14.27           C  
+ANISOU 1301  CA  ASP A 177     1980   1879   1564   -111     94   -362       C  
+ATOM   1302  C   ASP A 177      22.400  30.117  47.475  1.00 13.14           C  
+ANISOU 1302  C   ASP A 177     1849   1629   1512   -162     18   -418       C  
+ATOM   1303  O   ASP A 177      22.975  30.550  48.467  1.00 18.21           O  
+ANISOU 1303  O   ASP A 177     2611   2200   2109   -172    -83   -531       O  
+ATOM   1304  CB  ASP A 177      20.294  29.046  48.292  1.00 15.07           C  
+ANISOU 1304  CB  ASP A 177     2162   1929   1636    -20    253   -370       C  
+ATOM   1305  CG  ASP A 177      19.425  30.051  47.577  1.00 16.85           C  
+ANISOU 1305  CG  ASP A 177     2304   2087   2010     11    322   -333       C  
+ATOM   1306  OD1 ASP A 177      18.800  29.672  46.550  1.00 19.50           O  
+ANISOU 1306  OD1 ASP A 177     2489   2467   2454     17    314   -249       O  
+ATOM   1307  OD2 ASP A 177      19.375  31.217  48.033  1.00 20.29           O  
+ANISOU 1307  OD2 ASP A 177     2843   2412   2453     42    356   -395       O  
+ATOM   1308  N   TRP A 178      22.436  30.719  46.285  1.00 17.18           N  
+ANISOU 1308  N   TRP A 178     2260   2110   2157   -184     54   -338       N  
+ATOM   1309  CA  TRP A 178      23.257  31.904  46.044  1.00 17.75           C  
+ANISOU 1309  CA  TRP A 178     2309   2049   2386   -246     25   -354       C  
+ATOM   1310  C   TRP A 178      22.908  33.033  47.013  1.00 18.96           C  
+ANISOU 1310  C   TRP A 178     2596   2059   2549   -230     12   -477       C  
+ATOM   1311  O   TRP A 178      23.784  33.749  47.505  1.00 18.78           O  
+ANISOU 1311  O   TRP A 178     2598   1905   2633   -302   -105   -577       O  
+ATOM   1312  CB  TRP A 178      23.084  32.384  44.602  1.00 18.28           C  
+ANISOU 1312  CB  TRP A 178     2311   2087   2545   -220    132   -212       C  
+ATOM   1313  CG  TRP A 178      23.977  33.522  44.272  1.00 19.05           C  
+ANISOU 1313  CG  TRP A 178     2369   2019   2852   -286    166   -185       C  
+ATOM   1314  CD1 TRP A 178      23.628  34.847  44.152  1.00 21.22           C  
+ANISOU 1314  CD1 TRP A 178     2690   2130   3241   -271    233   -175       C  
+ATOM   1315  CD2 TRP A 178      25.381  33.449  44.024  1.00 20.81           C  
+ANISOU 1315  CD2 TRP A 178     2466   2185   3257   -379    158   -149       C  
+ATOM   1316  NE1 TRP A 178      24.741  35.593  43.843  1.00 22.22           N  
+ANISOU 1316  NE1 TRP A 178     2733   2090   3617   -364    270   -136       N  
+ATOM   1317  CE2 TRP A 178      25.828  34.762  43.759  1.00 23.56           C  
+ANISOU 1317  CE2 TRP A 178     2775   2321   3856   -433    231   -116       C  
+ATOM   1318  CE3 TRP A 178      26.309  32.403  44.003  1.00 21.66           C  
+ANISOU 1318  CE3 TRP A 178     2467   2379   3384   -416    114   -132       C  
+ATOM   1319  CZ2 TRP A 178      27.164  35.049  43.471  1.00 28.38           C  
+ANISOU 1319  CZ2 TRP A 178     3212   2793   4779   -537    273    -59       C  
+ATOM   1320  CZ3 TRP A 178      27.631  32.692  43.719  1.00 23.50           C  
+ANISOU 1320  CZ3 TRP A 178     2527   2491   3912   -502    148    -77       C  
+ATOM   1321  CH2 TRP A 178      28.046  34.002  43.462  1.00 25.35           C  
+ANISOU 1321  CH2 TRP A 178     2694   2504   4435   -568    232    -38       C  
+ATOM   1322  N   VAL A 179      21.620  33.181  47.286  1.00 22.56           N  
+ANISOU 1322  N   VAL A 179     3131   2517   2923   -129    127   -475       N  
+ATOM   1323  CA  VAL A 179      21.169  34.258  48.145  1.00 23.93           C  
+ANISOU 1323  CA  VAL A 179     3467   2539   3088    -75    169   -583       C  
+ATOM   1324  C   VAL A 179      21.241  33.855  49.615  1.00 21.16           C  
+ANISOU 1324  C   VAL A 179     3334   2182   2522    -23    120   -724       C  
+ATOM   1325  O   VAL A 179      21.817  34.566  50.434  1.00 21.41           O  
+ANISOU 1325  O   VAL A 179     3542   2077   2516    -34     -9   -882       O  
+ATOM   1326  CB  VAL A 179      19.734  34.693  47.789  1.00 17.68           C  
+ANISOU 1326  CB  VAL A 179     2650   1721   2347     42    352   -502       C  
+ATOM   1327  CG1 VAL A 179      19.241  35.739  48.767  1.00 21.31           C  
+ANISOU 1327  CG1 VAL A 179     3306   2008   2782    129    444   -616       C  
+ATOM   1328  CG2 VAL A 179      19.689  35.217  46.356  1.00 18.71           C  
+ANISOU 1328  CG2 VAL A 179     2641   1832   2637     31    361   -366       C  
+ATOM   1329  N   ALA A 180      20.671  32.708  49.949  1.00 22.95           N  
+ANISOU 1329  N   ALA A 180     3577   2536   2608     43    212   -668       N  
+ATOM   1330  CA  ALA A 180      20.580  32.302  51.350  1.00 23.81           C  
+ANISOU 1330  CA  ALA A 180     3957   2626   2463    145    234   -762       C  
+ATOM   1331  C   ALA A 180      21.972  32.108  51.973  1.00 22.70           C  
+ANISOU 1331  C   ALA A 180     3935   2477   2213     88    -63   -889       C  
+ATOM   1332  O   ALA A 180      22.196  32.430  53.139  1.00 23.43           O  
+ANISOU 1332  O   ALA A 180     4326   2476   2102    171   -162  -1035       O  
+ATOM   1333  CB  ALA A 180      19.757  31.018  51.474  1.00 24.47           C  
+ANISOU 1333  CB  ALA A 180     3995   2823   2477    215    425   -636       C  
+ATOM   1334  N   ASP A 181      22.896  31.589  51.173  1.00 19.00           N  
+ANISOU 1334  N   ASP A 181     3229   2096   1893    -38   -211   -830       N  
+ATOM   1335  CA  ASP A 181      24.231  31.230  51.652  1.00 19.27           C  
+ANISOU 1335  CA  ASP A 181     3282   2132   1909    -92   -503   -919       C  
+ATOM   1336  C   ASP A 181      25.300  32.248  51.240  1.00 28.88           C  
+ANISOU 1336  C   ASP A 181     4343   3210   3418   -232   -707   -997       C  
+ATOM   1337  O   ASP A 181      26.496  32.017  51.447  1.00 29.56           O  
+ANISOU 1337  O   ASP A 181     4337   3276   3619   -302   -966  -1054       O  
+ATOM   1338  CB  ASP A 181      24.604  29.829  51.139  1.00 23.16           C  
+ANISOU 1338  CB  ASP A 181     3599   2789   2409   -118   -497   -788       C  
+ATOM   1339  CG  ASP A 181      23.735  28.743  51.736  1.00 25.88           C  
+ANISOU 1339  CG  ASP A 181     4102   3224   2508      7   -329   -721       C  
+ATOM   1340  OD1 ASP A 181      23.524  28.751  52.972  1.00 28.42           O  
+ANISOU 1340  OD1 ASP A 181     4723   3494   2582    131   -338   -797       O  
+ATOM   1341  OD2 ASP A 181      23.263  27.884  50.978  1.00 22.52           O  
+ANISOU 1341  OD2 ASP A 181     3513   2897   2147    -10   -177   -587       O  
+ATOM   1342  N   ASP A 182      24.858  33.381  50.690  1.00 26.36           N  
+ANISOU 1342  N   ASP A 182     3982   2775   3260   -265   -581   -988       N  
+ATOM   1343  CA  ASP A 182      25.721  34.549  50.460  1.00 23.67           C  
+ANISOU 1343  CA  ASP A 182     3535   2232   3225   -391   -728  -1069       C  
+ATOM   1344  C   ASP A 182      26.898  34.194  49.546  1.00 26.89           C  
+ANISOU 1344  C   ASP A 182     3611   2663   3944   -524   -784   -956       C  
+ATOM   1345  O   ASP A 182      28.064  34.342  49.921  1.00 24.30           O  
+ANISOU 1345  O   ASP A 182     3175   2249   3809   -608  -1016  -1027       O  
+ATOM   1346  CB  ASP A 182      26.224  35.130  51.794  1.00 25.43           C  
+ANISOU 1346  CB  ASP A 182     3970   2332   3360   -372   -977  -1269       C  
+ATOM   1347  CG  ASP A 182      26.797  36.541  51.651  1.00 37.21           C  
+ANISOU 1347  CG  ASP A 182     5377   3602   5160   -485  -1052  -1334       C  
+ATOM   1348  OD1 ASP A 182      26.730  37.125  50.541  1.00 32.28           O  
+ANISOU 1348  OD1 ASP A 182     4567   2871   4825   -571   -904  -1239       O  
+ATOM   1349  OD2 ASP A 182      27.315  37.070  52.662  1.00 38.05           O  
+ANISOU 1349  OD2 ASP A 182     5607   3625   5224   -476  -1254  -1470       O  
+ATOM   1350  N   GLY A 183      26.571  33.739  48.340  1.00 24.34           N  
+ANISOU 1350  N   GLY A 183     4061   1721   3466    -96   -165    393       N  
+ATOM   1351  CA  GLY A 183      27.571  33.378  47.347  1.00 20.62           C  
+ANISOU 1351  CA  GLY A 183     3376   1619   2839   -107   -293    444       C  
+ATOM   1352  C   GLY A 183      28.480  34.537  46.992  1.00 22.39           C  
+ANISOU 1352  C   GLY A 183     3574   1915   3017   -364   -269    477       C  
+ATOM   1353  O   GLY A 183      29.641  34.328  46.632  1.00 25.95           O  
+ANISOU 1353  O   GLY A 183     3860   2639   3361   -451   -318    422       O  
+ATOM   1354  N   TYR A 184      27.962  35.755  47.087  1.00 25.60           N  
+ANISOU 1354  N   TYR A 184     4123   2035   3571   -489   -139    548       N  
+ATOM   1355  CA  TYR A 184      28.786  36.929  46.843  1.00 26.31           C  
+ANISOU 1355  CA  TYR A 184     4219   2133   3644   -748    -28    554       C  
+ATOM   1356  C   TYR A 184      30.029  36.916  47.727  1.00 27.82           C  
+ANISOU 1356  C   TYR A 184     4331   2545   3694   -930    -68    328       C  
+ATOM   1357  O   TYR A 184      31.132  37.216  47.268  1.00 30.65           O  
+ANISOU 1357  O   TYR A 184     4543   3095   4006  -1090    -50    257       O  
+ATOM   1358  CB  TYR A 184      28.016  38.223  47.079  1.00 27.30           C  
+ANISOU 1358  CB  TYR A 184     4507   1849   4018   -856    187    645       C  
+ATOM   1359  CG  TYR A 184      28.932  39.419  46.923  1.00 38.18           C  
+ANISOU 1359  CG  TYR A 184     5903   3218   5387  -1143    380    610       C  
+ATOM   1360  CD1 TYR A 184      29.416  39.781  45.669  1.00 38.96           C  
+ANISOU 1360  CD1 TYR A 184     5984   3401   5416  -1191    413    757       C  
+ATOM   1361  CD2 TYR A 184      29.341  40.165  48.025  1.00 45.82           C  
+ANISOU 1361  CD2 TYR A 184     6937   4086   6385  -1406    568    395       C  
+ATOM   1362  CE1 TYR A 184      30.270  40.861  45.510  1.00 41.63           C  
+ANISOU 1362  CE1 TYR A 184     6356   3692   5771  -1461    666    691       C  
+ATOM   1363  CE2 TYR A 184      30.194  41.256  47.879  1.00 45.84           C  
+ANISOU 1363  CE2 TYR A 184     6904   4107   6405  -1660    780    306       C  
+ATOM   1364  CZ  TYR A 184      30.655  41.594  46.616  1.00 46.44           C  
+ANISOU 1364  CZ  TYR A 184     6968   4209   6468  -1698    862    455       C  
+ATOM   1365  OH  TYR A 184      31.500  42.666  46.457  1.00 53.11           O  
+ANISOU 1365  OH  TYR A 184     7769   5064   7345  -1907   1109    334       O  
+ATOM   1366  N   ASN A 185      29.854  36.573  49.000  1.00 26.31           N  
+ANISOU 1366  N   ASN A 185     4249   2312   3438   -926   -128    204       N  
+ATOM   1367  CA  ASN A 185      31.000  36.511  49.904  1.00 28.16           C  
+ANISOU 1367  CA  ASN A 185     4416   2786   3499  -1099   -282     15       C  
+ATOM   1368  C   ASN A 185      31.687  35.145  49.908  1.00 30.87           C  
+ANISOU 1368  C   ASN A 185     4540   3445   3745   -891   -570     12       C  
+ATOM   1369  O   ASN A 185      32.896  35.057  50.153  1.00 29.97           O  
+ANISOU 1369  O   ASN A 185     4203   3589   3596   -996   -759   -100       O  
+ATOM   1370  CB  ASN A 185      30.583  36.855  51.340  1.00 29.32           C  
+ANISOU 1370  CB  ASN A 185     4868   2740   3534  -1268   -226   -113       C  
+ATOM   1371  CG  ASN A 185      30.484  38.353  51.583  1.00 35.57           C  
+ANISOU 1371  CG  ASN A 185     5793   3282   4439  -1608     88   -212       C  
+ATOM   1372  OD1 ASN A 185      31.490  39.075  51.564  1.00 38.10           O  
+ANISOU 1372  OD1 ASN A 185     5984   3764   4730  -1867    106   -349       O  
+ATOM   1373  ND2 ASN A 185      29.267  38.824  51.840  1.00 35.13           N  
+ANISOU 1373  ND2 ASN A 185     5973   2793   4582  -1622    385   -172       N  
+ATOM   1374  N   LYS A 186      30.926  34.090  49.622  1.00 25.64           N  
+ANISOU 1374  N   LYS A 186     3901   2738   3103   -599   -585    123       N  
+ATOM   1375  CA  LYS A 186      31.364  32.734  49.959  1.00 25.64           C  
+ANISOU 1375  CA  LYS A 186     3769   2936   3038   -380   -795    131       C  
+ATOM   1376  C   LYS A 186      31.649  31.787  48.791  1.00 24.59           C  
+ANISOU 1376  C   LYS A 186     3338   2967   3039   -198   -766    186       C  
+ATOM   1377  O   LYS A 186      32.150  30.689  49.024  1.00 25.13           O  
+ANISOU 1377  O   LYS A 186     3233   3175   3139    -22   -894    195       O  
+ATOM   1378  CB  LYS A 186      30.320  32.055  50.862  1.00 24.59           C  
+ANISOU 1378  CB  LYS A 186     3949   2585   2808   -206   -761    156       C  
+ATOM   1379  CG  LYS A 186      30.007  32.807  52.157  1.00 28.10           C  
+ANISOU 1379  CG  LYS A 186     4771   2824   3082   -431   -725     64       C  
+ATOM   1380  CD  LYS A 186      31.264  33.225  52.912  1.00 30.88           C  
+ANISOU 1380  CD  LYS A 186     5073   3427   3234   -673  -1002    -23       C  
+ATOM   1381  CE  LYS A 186      31.981  32.057  53.569  1.00 34.39           C  
+ANISOU 1381  CE  LYS A 186     5459   4098   3509   -492  -1370     48       C  
+ATOM   1382  NZ  LYS A 186      33.143  32.539  54.379  1.00 40.41           N  
+ANISOU 1382  NZ  LYS A 186     6162   5109   4081   -752  -1728    -43       N  
+ATOM   1383  N   PHE A 187      31.315  32.177  47.564  1.00 23.71           N  
+ANISOU 1383  N   PHE A 187     3195   2816   2998   -254   -587    231       N  
+ATOM   1384  CA  PHE A 187      31.444  31.257  46.429  1.00 24.15           C  
+ANISOU 1384  CA  PHE A 187     3052   3003   3120   -152   -498    249       C  
+ATOM   1385  C   PHE A 187      32.860  30.688  46.298  1.00 26.80           C  
+ANISOU 1385  C   PHE A 187     3034   3556   3591   -187   -541    152       C  
+ATOM   1386  O   PHE A 187      33.041  29.481  46.083  1.00 27.92           O  
+ANISOU 1386  O   PHE A 187     2983   3776   3848    -18   -500    142       O  
+ATOM   1387  CB  PHE A 187      31.033  31.939  45.116  1.00 22.86           C  
+ANISOU 1387  CB  PHE A 187     2982   2786   2919   -294   -346    324       C  
+ATOM   1388  CG  PHE A 187      31.267  31.086  43.899  1.00 22.98           C  
+ANISOU 1388  CG  PHE A 187     2859   2948   2926   -303   -215    299       C  
+ATOM   1389  CD1 PHE A 187      30.377  30.079  43.558  1.00 25.87           C  
+ANISOU 1389  CD1 PHE A 187     3239   3317   3272   -127   -180    314       C  
+ATOM   1390  CD2 PHE A 187      32.384  31.288  43.102  1.00 24.99           C  
+ANISOU 1390  CD2 PHE A 187     2977   3308   3211   -533    -65    213       C  
+ATOM   1391  CE1 PHE A 187      30.594  29.279  42.433  1.00 25.18           C  
+ANISOU 1391  CE1 PHE A 187     3048   3366   3152   -203     -5    247       C  
+ATOM   1392  CE2 PHE A 187      32.607  30.504  41.979  1.00 25.62           C  
+ANISOU 1392  CE2 PHE A 187     2977   3481   3275   -615    140    150       C  
+ATOM   1393  CZ  PHE A 187      31.710  29.495  41.642  1.00 25.86           C  
+ANISOU 1393  CZ  PHE A 187     3040   3545   3242   -462    166    169       C  
+ATOM   1394  N   SER A 188      33.866  31.535  46.464  1.00 27.15           N  
+ANISOU 1394  N   SER A 188     2955   3667   3694   -409   -593     57       N  
+ATOM   1395  CA  SER A 188      35.226  31.076  46.246  1.00 29.65           C  
+ANISOU 1395  CA  SER A 188     2858   4142   4265   -461   -613    -71       C  
+ATOM   1396  C   SER A 188      35.609  30.033  47.296  1.00 30.77           C  
+ANISOU 1396  C   SER A 188     2804   4375   4513   -215   -907    -31       C  
+ATOM   1397  O   SER A 188      36.430  29.159  47.027  1.00 35.13           O  
+ANISOU 1397  O   SER A 188     2972   5002   5372   -124   -900    -71       O  
+ATOM   1398  CB  SER A 188      36.220  32.250  46.246  1.00 32.31           C  
+ANISOU 1398  CB  SER A 188     3071   4509   4696   -768   -593   -234       C  
+ATOM   1399  OG  SER A 188      36.318  32.836  47.522  1.00 42.28           O  
+ANISOU 1399  OG  SER A 188     4414   5802   5850   -820   -868   -266       O  
+ATOM   1400  N   SER A 189      35.002  30.111  48.478  1.00 30.30           N  
+ANISOU 1400  N   SER A 189     3029   4266   4215   -116  -1135     56       N  
+ATOM   1401  CA  SER A 189      35.212  29.084  49.496  1.00 31.74           C  
+ANISOU 1401  CA  SER A 189     3160   4499   4401    134  -1424    159       C  
+ATOM   1402  C   SER A 189      34.509  27.774  49.113  1.00 29.64           C  
+ANISOU 1402  C   SER A 189     2913   4141   4208    434  -1220    261       C  
+ATOM   1403  O   SER A 189      35.008  26.693  49.423  1.00 36.64           O  
+ANISOU 1403  O   SER A 189     3574   5066   5282    663  -1333    347       O  
+ATOM   1404  CB  SER A 189      34.726  29.557  50.869  1.00 34.11           C  
+ANISOU 1404  CB  SER A 189     3879   4735   4347     85  -1660    201       C  
+ATOM   1405  OG  SER A 189      33.303  29.572  50.922  1.00 40.10           O  
+ANISOU 1405  OG  SER A 189     5061   5255   4920    153  -1409    245       O  
+ATOM   1406  N   TRP A 190      33.368  27.860  48.436  1.00 26.43           N  
+ANISOU 1406  N   TRP A 190     2745   3605   3693    433   -925    252       N  
+ATOM   1407  CA  TRP A 190      32.638  26.644  48.074  1.00 24.67           C  
+ANISOU 1407  CA  TRP A 190     2535   3300   3538    677   -698    287       C  
+ATOM   1408  C   TRP A 190      33.409  25.789  47.061  1.00 31.46           C  
+ANISOU 1408  C   TRP A 190     2975   4264   4715    697   -492    229       C  
+ATOM   1409  O   TRP A 190      33.309  24.564  47.076  1.00 30.93           O  
+ANISOU 1409  O   TRP A 190     2790   4151   4809    923   -346    259       O  
+ATOM   1410  CB  TRP A 190      31.266  26.979  47.515  1.00 21.78           C  
+ANISOU 1410  CB  TRP A 190     2450   2789   3035    642   -482    258       C  
+ATOM   1411  CG  TRP A 190      30.404  27.777  48.443  1.00 21.03           C  
+ANISOU 1411  CG  TRP A 190     2738   2500   2755    608   -565    280       C  
+ATOM   1412  CD1 TRP A 190      30.581  27.972  49.787  1.00 23.58           C  
+ANISOU 1412  CD1 TRP A 190     3276   2755   2928    610   -757    309       C  
+ATOM   1413  CD2 TRP A 190      29.238  28.506  48.078  1.00 19.36           C  
+ANISOU 1413  CD2 TRP A 190     2738   2101   2517    534   -438    265       C  
+ATOM   1414  NE1 TRP A 190      29.577  28.782  50.279  1.00 23.10           N  
+ANISOU 1414  NE1 TRP A 190     3569   2445   2763    505   -664    272       N  
+ATOM   1415  CE2 TRP A 190      28.745  29.127  49.245  1.00 21.92           C  
+ANISOU 1415  CE2 TRP A 190     3380   2204   2747    484   -476    255       C  
+ATOM   1416  CE3 TRP A 190      28.561  28.705  46.867  1.00 19.27           C  
+ANISOU 1416  CE3 TRP A 190     2682   2076   2562    488   -315    269       C  
+ATOM   1417  CZ2 TRP A 190      27.602  29.923  49.237  1.00 19.98           C  
+ANISOU 1417  CZ2 TRP A 190     3339   1676   2578    415   -339    235       C  
+ATOM   1418  CZ3 TRP A 190      27.426  29.497  46.861  1.00 22.36           C  
+ANISOU 1418  CZ3 TRP A 190     3270   2227   3000    455   -284    296       C  
+ATOM   1419  CH2 TRP A 190      26.958  30.094  48.038  1.00 22.36           C  
+ANISOU 1419  CH2 TRP A 190     3517   1960   3019    430   -270    273       C  
+ATOM   1420  N   VAL A 191      34.189  26.431  46.193  1.00 27.78           N  
+ANISOU 1420  N   VAL A 191     2300   3890   4364    435   -409    124       N  
+ATOM   1421  CA  VAL A 191      34.896  25.699  45.149  1.00 28.17           C  
+ANISOU 1421  CA  VAL A 191     1994   3977   4733    367   -102     13       C  
+ATOM   1422  C   VAL A 191      36.344  25.445  45.550  1.00 38.31           C  
+ANISOU 1422  C   VAL A 191     2806   5308   6444    393   -251    -19       C  
+ATOM   1423  O   VAL A 191      37.125  24.893  44.778  1.00 46.73           O  
+ANISOU 1423  O   VAL A 191     3501   6347   7908    310     37   -144       O  
+ATOM   1424  CB  VAL A 191      34.852  26.445  43.796  1.00 27.88           C  
+ANISOU 1424  CB  VAL A 191     2062   3955   4575     21    176   -109       C  
+ATOM   1425  CG1 VAL A 191      33.424  26.533  43.274  1.00 25.10           C  
+ANISOU 1425  CG1 VAL A 191     2095   3568   3876     21    264    -53       C  
+ATOM   1426  CG2 VAL A 191      35.478  27.837  43.901  1.00 29.23           C  
+ANISOU 1426  CG2 VAL A 191     2271   4146   4689   -222     34   -149       C  
+ATOM   1427  N   ASN A 192      36.697  25.858  46.764  1.00 44.50           N  
+ANISOU 1427  N   ASN A 192     3597   6144   7166    481   -700     77       N  
+ATOM   1428  CA  ASN A 192      38.039  25.653  47.301  1.00 45.01           C  
+ANISOU 1428  CA  ASN A 192     3181   6274   7645    532   -990     72       C  
+ATOM   1429  C   ASN A 192      37.990  24.828  48.584  1.00 50.27           C  
+ANISOU 1429  C   ASN A 192     3879   6939   8284    884  -1393    319       C  
+ATOM   1430  O   ASN A 192      36.969  24.227  48.919  1.00 50.03           O  
+ANISOU 1430  O   ASN A 192     4211   6813   7986   1092  -1307    455       O  
+ATOM   1431  CB  ASN A 192      38.727  26.995  47.573  1.00 53.30           C  
+ANISOU 1431  CB  ASN A 192     4181   7428   8641    244  -1231    -64       C  
+ATOM   1432  CG  ASN A 192      39.462  27.540  46.355  1.00 55.78           C  
+ANISOU 1432  CG  ASN A 192     4230   7706   9256    -78   -843   -324       C  
+ATOM   1433  OD1 ASN A 192      40.532  27.046  45.990  1.00 63.85           O  
+ANISOU 1433  OD1 ASN A 192     4724   8690  10847    -98   -736   -453       O  
+ATOM   1434  ND2 ASN A 192      38.893  28.572  45.728  1.00 46.96           N  
+ANISOU 1434  ND2 ASN A 192     3493   6557   7794   -338   -603   -399       N  
+ATOM   1435  OXT ASN A 192      38.968  24.745  49.324  1.00 62.46           O  
+ANISOU 1435  OXT ASN A 192     5215   8570   9948    931  -1739    375       O  
+TER    1436      ASN A 192                                                      
+ATOM   1437  N   ALA B   2      42.314 -24.500  40.477  1.00 42.78           N  
+ANISOU 1437  N   ALA B   2     7796   5278   3181  -1493   -584   -889       N  
+ATOM   1438  CA  ALA B   2      42.356 -24.739  41.918  1.00 48.18           C  
+ANISOU 1438  CA  ALA B   2     8164   5991   4153  -1460   -533   -902       C  
+ATOM   1439  C   ALA B   2      41.926 -23.504  42.710  1.00 46.57           C  
+ANISOU 1439  C   ALA B   2     7740   5889   4066  -1374   -619   -712       C  
+ATOM   1440  O   ALA B   2      42.394 -22.395  42.450  1.00 48.85           O  
+ANISOU 1440  O   ALA B   2     8170   6182   4211  -1331   -508   -631       O  
+ATOM   1441  CB  ALA B   2      43.759 -25.179  42.349  1.00 48.08           C  
+ANISOU 1441  CB  ALA B   2     8103   5932   4231  -1377   -137  -1048       C  
+ATOM   1442  N   LYS B   3      41.033 -23.705  43.675  1.00 44.27           N  
+ANISOU 1442  N   LYS B   3     7092   5671   4058  -1330   -794   -622       N  
+ATOM   1443  CA  LYS B   3      40.596 -22.626  44.557  1.00 39.64           C  
+ANISOU 1443  CA  LYS B   3     6237   5180   3643  -1164   -841   -444       C  
+ATOM   1444  C   LYS B   3      41.698 -22.343  45.568  1.00 38.22           C  
+ANISOU 1444  C   LYS B   3     5929   4957   3638  -1070   -506   -457       C  
+ATOM   1445  O   LYS B   3      42.083 -23.228  46.335  1.00 38.68           O  
+ANISOU 1445  O   LYS B   3     5817   4986   3894  -1078   -372   -539       O  
+ATOM   1446  CB  LYS B   3      39.288 -22.994  45.265  1.00 40.05           C  
+ANISOU 1446  CB  LYS B   3     5917   5374   3924  -1156  -1092   -362       C  
+ATOM   1447  CG  LYS B   3      38.654 -21.851  46.042  1.00 40.91           C  
+ANISOU 1447  CG  LYS B   3     5767   5610   4166   -932  -1167   -194       C  
+ATOM   1448  CD  LYS B   3      38.187 -20.758  45.107  1.00 45.74           C  
+ANISOU 1448  CD  LYS B   3     6604   6241   4535   -816  -1399    -98       C  
+ATOM   1449  CE  LYS B   3      37.474 -19.649  45.865  1.00 42.52           C  
+ANISOU 1449  CE  LYS B   3     5966   5941   4250   -527  -1502     51       C  
+ATOM   1450  NZ  LYS B   3      36.823 -18.686  44.934  1.00 46.34           N1+
+ANISOU 1450  NZ  LYS B   3     6675   6436   4495   -369  -1812    150       N1+
+ATOM   1451  N   ARG B   4      42.211 -21.115  45.564  1.00 34.00           N  
+ANISOU 1451  N   ARG B   4     5507   4401   3011   -994   -397   -374       N  
+ATOM   1452  CA  ARG B   4      43.387 -20.787  46.365  1.00 31.79           C  
+ANISOU 1452  CA  ARG B   4     5140   4090   2850   -960    -94   -401       C  
+ATOM   1453  C   ARG B   4      43.038 -19.912  47.572  1.00 33.82           C  
+ANISOU 1453  C   ARG B   4     5186   4365   3301   -800   -130   -262       C  
+ATOM   1454  O   ARG B   4      42.502 -18.803  47.427  1.00 29.16           O  
+ANISOU 1454  O   ARG B   4     4717   3755   2608   -705   -271   -133       O  
+ATOM   1455  CB  ARG B   4      44.443 -20.099  45.489  1.00 31.57           C  
+ANISOU 1455  CB  ARG B   4     5424   4018   2553  -1073    112   -431       C  
+ATOM   1456  N   VAL B   5      43.357 -20.422  48.761  1.00 32.25           N  
+ANISOU 1456  N   VAL B   5     4715   4183   3356   -748    -10   -297       N  
+ATOM   1457  CA  VAL B   5      43.058 -19.737  50.014  1.00 23.34           C  
+ANISOU 1457  CA  VAL B   5     3398   3069   2399   -594    -20   -192       C  
+ATOM   1458  C   VAL B   5      44.321 -19.233  50.711  1.00 21.92           C  
+ANISOU 1458  C   VAL B   5     3225   2833   2272   -603    206   -220       C  
+ATOM   1459  O   VAL B   5      45.315 -19.952  50.808  1.00 29.58           O  
+ANISOU 1459  O   VAL B   5     4130   3808   3301   -676    375   -340       O  
+ATOM   1460  CB  VAL B   5      42.290 -20.680  50.986  1.00 24.38           C  
+ANISOU 1460  CB  VAL B   5     3223   3277   2763   -546    -84   -185       C  
+ATOM   1461  CG1 VAL B   5      42.162 -20.051  52.369  1.00 24.33           C  
+ANISOU 1461  CG1 VAL B   5     3047   3288   2909   -385    -30   -101       C  
+ATOM   1462  CG2 VAL B   5      40.927 -21.030  50.411  1.00 23.64           C  
+ANISOU 1462  CG2 VAL B   5     3054   3292   2636   -570   -333   -140       C  
+ATOM   1463  N   PHE B   6      44.291 -17.995  51.195  1.00 24.16           N  
+ANISOU 1463  N   PHE B   6     3592   3061   2528   -518    190   -118       N  
+ATOM   1464  CA  PHE B   6      45.375 -17.505  52.039  1.00 23.33           C  
+ANISOU 1464  CA  PHE B   6     3466   2909   2490   -553    357   -138       C  
+ATOM   1465  C   PHE B   6      45.018 -17.747  53.499  1.00 24.16           C  
+ANISOU 1465  C   PHE B   6     3333   3034   2812   -396    337   -113       C  
+ATOM   1466  O   PHE B   6      44.004 -17.248  53.992  1.00 22.98           O  
+ANISOU 1466  O   PHE B   6     3161   2885   2685   -223    219    -20       O  
+ATOM   1467  CB  PHE B   6      45.646 -16.016  51.796  1.00 20.67           C  
+ANISOU 1467  CB  PHE B   6     3438   2448   1969   -598    352    -49       C  
+ATOM   1468  CG  PHE B   6      46.859 -15.484  52.535  1.00 26.71           C  
+ANISOU 1468  CG  PHE B   6     4202   3172   2775   -722    509    -79       C  
+ATOM   1469  CD1 PHE B   6      46.787 -15.164  53.884  1.00 25.29           C  
+ANISOU 1469  CD1 PHE B   6     3924   2948   2738   -591    478    -51       C  
+ATOM   1470  CD2 PHE B   6      48.068 -15.285  51.871  1.00 31.73           C  
+ANISOU 1470  CD2 PHE B   6     4932   3836   3289   -990    687   -139       C  
+ATOM   1471  CE1 PHE B   6      47.896 -14.680  54.568  1.00 26.08           C  
+ANISOU 1471  CE1 PHE B   6     4028   3015   2865   -731    578    -84       C  
+ATOM   1472  CE2 PHE B   6      49.181 -14.792  52.545  1.00 30.16           C  
+ANISOU 1472  CE2 PHE B   6     4680   3643   3136  -1147    807   -170       C  
+ATOM   1473  CZ  PHE B   6      49.092 -14.483  53.896  1.00 25.73           C  
+ANISOU 1473  CZ  PHE B   6     4035   3019   2723  -1021    729   -141       C  
+ATOM   1474  N   PHE B   7      45.855 -18.504  54.200  1.00 21.32           N  
+ANISOU 1474  N   PHE B   7     2803   2700   2597   -432    455   -200       N  
+ATOM   1475  CA  PHE B   7      45.617 -18.747  55.620  1.00 20.02           C  
+ANISOU 1475  CA  PHE B   7     2472   2537   2598   -305    444   -171       C  
+ATOM   1476  C   PHE B   7      46.411 -17.766  56.476  1.00 21.49           C  
+ANISOU 1476  C   PHE B   7     2729   2656   2781   -301    496   -157       C  
+ATOM   1477  O   PHE B   7      47.620 -17.617  56.308  1.00 20.41           O  
+ANISOU 1477  O   PHE B   7     2605   2524   2625   -441    590   -229       O  
+ATOM   1478  CB  PHE B   7      45.978 -20.189  55.990  1.00 21.51           C  
+ANISOU 1478  CB  PHE B   7     2493   2752   2927   -320    487   -260       C  
+ATOM   1479  CG  PHE B   7      45.020 -21.201  55.439  1.00 22.12           C  
+ANISOU 1479  CG  PHE B   7     2529   2859   3016   -347    403   -261       C  
+ATOM   1480  CD1 PHE B   7      43.796 -21.409  56.049  1.00 24.14           C  
+ANISOU 1480  CD1 PHE B   7     2670   3164   3337   -292    316   -168       C  
+ATOM   1481  CD2 PHE B   7      45.336 -21.932  54.302  1.00 24.50           C  
+ANISOU 1481  CD2 PHE B   7     2910   3152   3247   -447    417   -364       C  
+ATOM   1482  CE1 PHE B   7      42.899 -22.343  55.546  1.00 27.74           C  
+ANISOU 1482  CE1 PHE B   7     3070   3666   3803   -385    221   -167       C  
+ATOM   1483  CE2 PHE B   7      44.443 -22.856  53.789  1.00 26.83           C  
+ANISOU 1483  CE2 PHE B   7     3211   3450   3534   -512    308   -372       C  
+ATOM   1484  CZ  PHE B   7      43.224 -23.064  54.412  1.00 29.85           C  
+ANISOU 1484  CZ  PHE B   7     3459   3886   3996   -505    197   -268       C  
+ATOM   1485  N   SER B   8      45.707 -17.094  57.382  1.00 19.35           N  
+ANISOU 1485  N   SER B   8     2497   2339   2516   -146    436    -74       N  
+ATOM   1486  CA  SER B   8      46.315 -16.120  58.284  1.00 19.70           C  
+ANISOU 1486  CA  SER B   8     2673   2283   2531   -137    451    -62       C  
+ATOM   1487  C   SER B   8      46.209 -16.619  59.725  1.00 24.63           C  
+ANISOU 1487  C   SER B   8     3160   2924   3273    -16    459    -63       C  
+ATOM   1488  O   SER B   8      45.128 -16.977  60.173  1.00 22.02           O  
+ANISOU 1488  O   SER B   8     2736   2649   2983    135    442    -11       O  
+ATOM   1489  CB  SER B   8      45.634 -14.756  58.132  1.00 22.41           C  
+ANISOU 1489  CB  SER B   8     3292   2502   2719    -21    372     24       C  
+ATOM   1490  OG  SER B   8      46.189 -13.809  59.037  1.00 21.76           O  
+ANISOU 1490  OG  SER B   8     3405   2278   2584    -26    371     26       O  
+ATOM   1491  N   PHE B   9      47.331 -16.642  60.448  1.00 18.62           N  
+ANISOU 1491  N   PHE B   9     2384   2137   2555    -99    481   -121       N  
+ATOM   1492  CA  PHE B   9      47.376 -17.272  61.766  1.00 19.76           C  
+ANISOU 1492  CA  PHE B   9     2434   2287   2787     -2    470   -125       C  
+ATOM   1493  C   PHE B   9      48.574 -16.790  62.574  1.00 19.43           C  
+ANISOU 1493  C   PHE B   9     2451   2194   2737    -83    434   -176       C  
+ATOM   1494  O   PHE B   9      49.515 -16.227  62.023  1.00 19.77           O  
+ANISOU 1494  O   PHE B   9     2522   2242   2746   -264    440   -225       O  
+ATOM   1495  CB  PHE B   9      47.454 -18.796  61.616  1.00 17.87           C  
+ANISOU 1495  CB  PHE B   9     1995   2123   2671    -10    487   -166       C  
+ATOM   1496  CG  PHE B   9      48.497 -19.229  60.626  1.00 21.46           C  
+ANISOU 1496  CG  PHE B   9     2362   2632   3161   -138    521   -270       C  
+ATOM   1497  CD1 PHE B   9      49.836 -19.300  60.988  1.00 18.01           C  
+ANISOU 1497  CD1 PHE B   9     1836   2231   2776   -189    518   -357       C  
+ATOM   1498  CD2 PHE B   9      48.146 -19.508  59.318  1.00 20.86           C  
+ANISOU 1498  CD2 PHE B   9     2283   2596   3048   -200    557   -289       C  
+ATOM   1499  CE1 PHE B   9      50.796 -19.651  60.064  1.00 24.87           C  
+ANISOU 1499  CE1 PHE B   9     2575   3203   3670   -281    588   -468       C  
+ATOM   1500  CE2 PHE B   9      49.111 -19.885  58.390  1.00 21.86           C  
+ANISOU 1500  CE2 PHE B   9     2345   2788   3173   -301    629   -400       C  
+ATOM   1501  CZ  PHE B   9      50.428 -19.956  58.761  1.00 20.28           C  
+ANISOU 1501  CZ  PHE B   9     2018   2651   3034   -332    664   -493       C  
+ATOM   1502  N   HIS B  10      48.517 -17.050  63.869  1.00 18.89           N  
+ANISOU 1502  N   HIS B  10     2398   2094   2686     24    394   -161       N  
+ATOM   1503  CA  HIS B  10      49.634 -16.908  64.797  1.00 17.97           C  
+ANISOU 1503  CA  HIS B  10     2300   1952   2575    -36    309   -215       C  
+ATOM   1504  C   HIS B  10      50.518 -18.146  64.698  1.00 17.87           C  
+ANISOU 1504  C   HIS B  10     2041   2044   2704    -54    281   -290       C  
+ATOM   1505  O   HIS B  10      50.014 -19.268  64.802  1.00 16.80           O  
+ANISOU 1505  O   HIS B  10     1837   1914   2631     58    297   -268       O  
+ATOM   1506  CB  HIS B  10      49.080 -16.730  66.210  1.00 17.03           C  
+ANISOU 1506  CB  HIS B  10     2353   1744   2373    117    273   -164       C  
+ATOM   1507  CG  HIS B  10      50.119 -16.567  67.268  1.00 16.34           C  
+ANISOU 1507  CG  HIS B  10     2333   1615   2258     66    141   -213       C  
+ATOM   1508  ND1 HIS B  10      49.846 -16.772  68.604  1.00 21.48           N  
+ANISOU 1508  ND1 HIS B  10     3131   2201   2829    196     94   -180       N  
+ATOM   1509  CD2 HIS B  10      51.420 -16.204  67.199  1.00 20.01           C  
+ANISOU 1509  CD2 HIS B  10     2734   2117   2751   -117     36   -293       C  
+ATOM   1510  CE1 HIS B  10      50.937 -16.545  69.310  1.00 24.96           C  
+ANISOU 1510  CE1 HIS B  10     3620   2619   3245    111    -69   -239       C  
+ATOM   1511  NE2 HIS B  10      51.910 -16.207  68.480  1.00 22.70           N  
+ANISOU 1511  NE2 HIS B  10     3174   2411   3039    -85   -111   -310       N  
+ATOM   1512  N   TYR B  11      51.822 -17.961  64.504  1.00 19.10           N  
+ANISOU 1512  N   TYR B  11     2069   2286   2904   -191    237   -381       N  
+ATOM   1513  CA  TYR B  11      52.664 -19.117  64.197  1.00 23.12           C  
+ANISOU 1513  CA  TYR B  11     2314   2923   3550   -145    226   -477       C  
+ATOM   1514  C   TYR B  11      52.672 -20.117  65.350  1.00 24.29           C  
+ANISOU 1514  C   TYR B  11     2471   3011   3748     52    101   -462       C  
+ATOM   1515  O   TYR B  11      52.906 -21.294  65.125  1.00 22.58           O  
+ANISOU 1515  O   TYR B  11     2139   2817   3623    175     89   -512       O  
+ATOM   1516  CB  TYR B  11      54.102 -18.710  63.850  1.00 27.91           C  
+ANISOU 1516  CB  TYR B  11     2701   3703   4200   -318    212   -589       C  
+ATOM   1517  CG  TYR B  11      54.817 -19.842  63.143  1.00 32.53           C  
+ANISOU 1517  CG  TYR B  11     2997   4452   4912   -222    267   -709       C  
+ATOM   1518  CD1 TYR B  11      54.475 -20.187  61.844  1.00 33.47           C  
+ANISOU 1518  CD1 TYR B  11     3112   4599   5006   -240    428   -729       C  
+ATOM   1519  CD2 TYR B  11      55.784 -20.609  63.792  1.00 35.47           C  
+ANISOU 1519  CD2 TYR B  11     3150   4928   5399    -65    134   -799       C  
+ATOM   1520  CE1 TYR B  11      55.100 -21.244  61.191  1.00 33.22           C  
+ANISOU 1520  CE1 TYR B  11     2983   4647   4992   -109    449   -799       C  
+ATOM   1521  CE2 TYR B  11      56.419 -21.673  63.138  1.00 32.85           C  
+ANISOU 1521  CE2 TYR B  11     2691   4686   5102     90    171   -870       C  
+ATOM   1522  CZ  TYR B  11      56.061 -21.982  61.843  1.00 33.58           C  
+ANISOU 1522  CZ  TYR B  11     2861   4770   5128     61    336   -869       C  
+ATOM   1523  OH  TYR B  11      56.677 -23.021  61.172  1.00 40.10           O  
+ANISOU 1523  OH  TYR B  11     3603   5664   5969    214    373   -947       O  
+ATOM   1524  N   GLN B  12      52.377 -19.657  66.570  1.00 20.23           N  
+ANISOU 1524  N   GLN B  12     2152   2393   3142     90     10   -394       N  
+ATOM   1525  CA  GLN B  12      52.280 -20.564  67.716  1.00 23.39           C  
+ANISOU 1525  CA  GLN B  12     2644   2709   3536    258   -103   -353       C  
+ATOM   1526  C   GLN B  12      51.234 -21.664  67.471  1.00 20.17           C  
+ANISOU 1526  C   GLN B  12     2289   2229   3147    349     -8   -283       C  
+ATOM   1527  O   GLN B  12      51.374 -22.806  67.933  1.00 19.58           O  
+ANISOU 1527  O   GLN B  12     2256   2082   3102    465    -90   -273       O  
+ATOM   1528  CB  GLN B  12      51.931 -19.794  68.995  1.00 24.31           C  
+ANISOU 1528  CB  GLN B  12     3024   2719   3493    269   -169   -285       C  
+ATOM   1529  CG  GLN B  12      51.930 -20.675  70.241  1.00 24.43           C  
+ANISOU 1529  CG  GLN B  12     3188   2643   3453    415   -294   -235       C  
+ATOM   1530  CD  GLN B  12      53.321 -21.104  70.651  1.00 22.04           C  
+ANISOU 1530  CD  GLN B  12     2755   2395   3222    470   -534   -322       C  
+ATOM   1531  OE1 GLN B  12      54.179 -20.266  70.904  1.00 24.03           O  
+ANISOU 1531  OE1 GLN B  12     2950   2720   3460    368   -664   -389       O  
+ATOM   1532  NE2 GLN B  12      53.554 -22.418  70.728  1.00 23.25           N  
+ANISOU 1532  NE2 GLN B  12     2872   2512   3450    634   -616   -323       N  
+ATOM   1533  N   ASP B  13      50.183 -21.323  66.736  1.00 18.81           N  
+ANISOU 1533  N   ASP B  13     2135   2066   2946    284    143   -231       N  
+ATOM   1534  CA  ASP B  13      49.157 -22.312  66.431  1.00 19.53           C  
+ANISOU 1534  CA  ASP B  13     2245   2119   3055    302    220   -168       C  
+ATOM   1535  C   ASP B  13      49.582 -23.309  65.353  1.00 18.87           C  
+ANISOU 1535  C   ASP B  13     2041   2048   3079    299    219   -255       C  
+ATOM   1536  O   ASP B  13      48.948 -24.352  65.183  1.00 16.54           O  
+ANISOU 1536  O   ASP B  13     1807   1678   2798    297    234   -220       O  
+ATOM   1537  CB  ASP B  13      47.871 -21.607  66.039  1.00 18.21           C  
+ANISOU 1537  CB  ASP B  13     2095   1999   2824    255    347    -91       C  
+ATOM   1538  CG  ASP B  13      47.165 -21.021  67.244  1.00 18.43           C  
+ANISOU 1538  CG  ASP B  13     2270   2002   2728    324    385     -4       C  
+ATOM   1539  OD1 ASP B  13      47.077 -21.713  68.288  1.00 18.05           O  
+ANISOU 1539  OD1 ASP B  13     2332   1893   2634    361    364     49       O  
+ATOM   1540  OD2 ASP B  13      46.714 -19.866  67.147  1.00 18.92           O1-
+ANISOU 1540  OD2 ASP B  13     2379   2093   2718    355    437      9       O1-
+ATOM   1541  N   VAL B  14      50.660 -22.998  64.636  1.00 19.49           N  
+ANISOU 1541  N   VAL B  14     1965   2223   3216    284    211   -375       N  
+ATOM   1542  CA  VAL B  14      51.299 -23.996  63.780  1.00 22.45           C  
+ANISOU 1542  CA  VAL B  14     2233   2620   3677    348    214   -493       C  
+ATOM   1543  C   VAL B  14      52.111 -24.952  64.632  1.00 17.74           C  
+ANISOU 1543  C   VAL B  14     1651   1951   3138    542     62   -538       C  
+ATOM   1544  O   VAL B  14      51.975 -26.174  64.495  1.00 20.55           O  
+ANISOU 1544  O   VAL B  14     2113   2176   3518    651     25   -558       O  
+ATOM   1545  CB  VAL B  14      52.193 -23.364  62.722  1.00 19.55           C  
+ANISOU 1545  CB  VAL B  14     1670   2426   3333    266    299   -613       C  
+ATOM   1546  CG1 VAL B  14      52.914 -24.452  61.902  1.00 21.61           C  
+ANISOU 1546  CG1 VAL B  14     1863   2727   3620    368    310   -729       C  
+ATOM   1547  CG2 VAL B  14      51.349 -22.476  61.815  1.00 23.60           C  
+ANISOU 1547  CG2 VAL B  14     2247   2963   3756     93    418   -554       C  
+ATOM   1548  N   ILE B  15      52.948 -24.404  65.520  1.00 17.11           N  
+ANISOU 1548  N   ILE B  15     1503   1934   3063    585    -55   -553       N  
+ATOM   1549  CA  ILE B  15      53.725 -25.225  66.438  1.00 23.51           C  
+ANISOU 1549  CA  ILE B  15     2342   2681   3911    800   -255   -584       C  
+ATOM   1550  C   ILE B  15      52.806 -26.198  67.190  1.00 17.91           C  
+ANISOU 1550  C   ILE B  15     1961   1721   3124    866   -308   -455       C  
+ATOM   1551  O   ILE B  15      53.165 -27.360  67.415  1.00 21.14           O  
+ANISOU 1551  O   ILE B  15     2487   1997   3548   1048   -430   -478       O  
+ATOM   1552  CB  ILE B  15      54.525 -24.365  67.476  1.00 20.18           C  
+ANISOU 1552  CB  ILE B  15     1853   2351   3464    788   -415   -587       C  
+ATOM   1553  CG1 ILE B  15      55.472 -23.371  66.777  1.00 19.46           C  
+ANISOU 1553  CG1 ILE B  15     1441   2517   3438    639   -363   -704       C  
+ATOM   1554  CG2 ILE B  15      55.309 -25.248  68.429  1.00 21.90           C  
+ANISOU 1554  CG2 ILE B  15     2112   2505   3706   1041   -671   -613       C  
+ATOM   1555  CD1 ILE B  15      56.563 -24.019  65.936  1.00 26.11           C  
+ANISOU 1555  CD1 ILE B  15     1999   3542   4380    745   -339   -848       C  
+ATOM   1556  N   ASP B  16      51.615 -25.727  67.566  1.00 21.37           N  
+ANISOU 1556  N   ASP B  16     2560   2104   3456    707   -203   -315       N  
+ATOM   1557  CA  ASP B  16      50.732 -26.526  68.420  1.00 24.18           C  
+ANISOU 1557  CA  ASP B  16     3212   2267   3709    701   -220   -175       C  
+ATOM   1558  C   ASP B  16      49.892 -27.540  67.648  1.00 21.72           C  
+ANISOU 1558  C   ASP B  16     2992   1846   3415    617   -132   -148       C  
+ATOM   1559  O   ASP B  16      49.104 -28.273  68.243  1.00 23.03           O  
+ANISOU 1559  O   ASP B  16     3403   1856   3491    540   -126    -25       O  
+ATOM   1560  CB  ASP B  16      49.807 -25.609  69.231  1.00 20.69           C  
+ANISOU 1560  CB  ASP B  16     2870   1858   3132    581   -118    -49       C  
+ATOM   1561  CG  ASP B  16      50.561 -24.763  70.247  1.00 25.30           C  
+ANISOU 1561  CG  ASP B  16     3496   2473   3643    650   -245    -64       C  
+ATOM   1562  OD1 ASP B  16      51.805 -24.913  70.358  1.00 25.50           O  
+ANISOU 1562  OD1 ASP B  16     3430   2522   3739    770   -434   -162       O  
+ATOM   1563  OD2 ASP B  16      49.904 -23.966  70.953  1.00 23.27           O1-
+ANISOU 1563  OD2 ASP B  16     3363   2227   3250    594   -163     12       O1-
+ATOM   1564  N   PHE B  17      50.070 -27.570  66.329  1.00 20.27           N  
+ANISOU 1564  N   PHE B  17     2633   1744   3325    598    -65   -262       N  
+ATOM   1565  CA  PHE B  17      49.261 -28.384  65.407  1.00 21.68           C  
+ANISOU 1565  CA  PHE B  17     2893   1836   3507    480      5   -260       C  
+ATOM   1566  C   PHE B  17      47.765 -28.087  65.530  1.00 22.84           C  
+ANISOU 1566  C   PHE B  17     3069   2028   3582    242    126   -111       C  
+ATOM   1567  O   PHE B  17      46.934 -29.002  65.711  1.00 20.07           O  
+ANISOU 1567  O   PHE B  17     2900   1543   3181    103    129    -21       O  
+ATOM   1568  CB  PHE B  17      49.492 -29.887  65.600  1.00 21.14           C  
+ANISOU 1568  CB  PHE B  17     3106   1498   3428    587   -123   -276       C  
+ATOM   1569  CG  PHE B  17      49.261 -30.685  64.344  1.00 24.26           C  
+ANISOU 1569  CG  PHE B  17     3565   1806   3846    537    -92   -372       C  
+ATOM   1570  CD1 PHE B  17      50.284 -30.878  63.436  1.00 24.04           C  
+ANISOU 1570  CD1 PHE B  17     3425   1821   3888    740   -101   -567       C  
+ATOM   1571  CD2 PHE B  17      48.011 -31.190  64.042  1.00 25.95           C  
+ANISOU 1571  CD2 PHE B  17     3933   1927   4000    268    -43   -277       C  
+ATOM   1572  CE1 PHE B  17      50.075 -31.593  62.272  1.00 28.69           C  
+ANISOU 1572  CE1 PHE B  17     4125   2316   4462    705    -66   -673       C  
+ATOM   1573  CE2 PHE B  17      47.790 -31.901  62.874  1.00 30.90           C  
+ANISOU 1573  CE2 PHE B  17     4658   2459   4625    195    -44   -375       C  
+ATOM   1574  CZ  PHE B  17      48.829 -32.102  61.986  1.00 32.68           C  
+ANISOU 1574  CZ  PHE B  17     4836   2686   4895    427    -55   -577       C  
+ATOM   1575  N   ARG B  18      47.433 -26.807  65.432  1.00 20.18           N  
+ANISOU 1575  N   ARG B  18     2552   1883   3233    195    221    -87       N  
+ATOM   1576  CA  ARG B  18      46.049 -26.382  65.292  1.00 21.14           C  
+ANISOU 1576  CA  ARG B  18     2607   2117   3308     34    338     17       C  
+ATOM   1577  C   ARG B  18      45.813 -25.906  63.851  1.00 17.81           C  
+ANISOU 1577  C   ARG B  18     2022   1817   2926    -27    377    -54       C  
+ATOM   1578  O   ARG B  18      44.836 -26.295  63.200  1.00 21.29           O  
+ANISOU 1578  O   ARG B  18     2429   2297   3363   -174    397    -19       O  
+ATOM   1579  CB  ARG B  18      45.709 -25.280  66.310  1.00 19.26           C  
+ANISOU 1579  CB  ARG B  18     2352   1977   2991     84    406     98       C  
+ATOM   1580  CG  ARG B  18      45.782 -25.742  67.781  1.00 19.00           C  
+ANISOU 1580  CG  ARG B  18     2530   1828   2863    119    380    185       C  
+ATOM   1581  CD  ARG B  18      45.275 -24.648  68.776  1.00 17.97           C  
+ANISOU 1581  CD  ARG B  18     2419   1799   2610    171    482    255       C  
+ATOM   1582  NE  ARG B  18      45.162 -25.233  70.114  1.00 17.17           N  
+ANISOU 1582  NE  ARG B  18     2558   1591   2375    163    485    353       N  
+ATOM   1583  CZ  ARG B  18      44.196 -26.068  70.481  1.00 17.82           C  
+ANISOU 1583  CZ  ARG B  18     2719   1666   2387      1    592    471       C  
+ATOM   1584  NH1 ARG B  18      43.229 -26.385  69.619  1.00 20.65           N1+
+ANISOU 1584  NH1 ARG B  18     2889   2143   2816   -167    686    497       N1+
+ATOM   1585  NH2 ARG B  18      44.190 -26.594  71.704  1.00 19.59           N  
+ANISOU 1585  NH2 ARG B  18     3223   1770   2452    -23    595    570       N  
+ATOM   1586  N   VAL B  19      46.721 -25.086  63.344  1.00 19.45           N  
+ANISOU 1586  N   VAL B  19     2215   1343   3830     44    235   -347       N  
+ATOM   1587  CA  VAL B  19      46.593 -24.597  61.979  1.00 22.94           C  
+ANISOU 1587  CA  VAL B  19     2425   2045   4246     25    458   -322       C  
+ATOM   1588  C   VAL B  19      46.544 -25.760  60.994  1.00 21.40           C  
+ANISOU 1588  C   VAL B  19     2191   1950   3991     48    313   -486       C  
+ATOM   1589  O   VAL B  19      45.715 -25.762  60.084  1.00 18.65           O  
+ANISOU 1589  O   VAL B  19     1800   1774   3513     -7    399   -356       O  
+ATOM   1590  CB  VAL B  19      47.733 -23.645  61.618  1.00 21.07           C  
+ANISOU 1590  CB  VAL B  19     1997   1911   4099     52    641   -453       C  
+ATOM   1591  CG1 VAL B  19      47.845 -23.468  60.100  1.00 21.36           C  
+ANISOU 1591  CG1 VAL B  19     1879   2224   4011     -5    831   -499       C  
+ATOM   1592  CG2 VAL B  19      47.483 -22.298  62.308  1.00 21.79           C  
+ANISOU 1592  CG2 VAL B  19     2129   1944   4205     11    817   -213       C  
+ATOM   1593  N   ASN B  20      47.389 -26.763  61.206  1.00 20.71           N  
+ANISOU 1593  N   ASN B  20     2137   1727   4005    152     42   -790       N  
+ATOM   1594  CA  ASN B  20      47.468 -27.882  60.256  1.00 24.42           C  
+ANISOU 1594  CA  ASN B  20     2560   2285   4434    206   -126  -1001       C  
+ATOM   1595  C   ASN B  20      46.197 -28.716  60.150  1.00 22.58           C  
+ANISOU 1595  C   ASN B  20     2507   2003   4068    116   -262   -816       C  
+ATOM   1596  O   ASN B  20      45.938 -29.322  59.114  1.00 22.44           O  
+ANISOU 1596  O   ASN B  20     2425   2129   3971    131   -312   -891       O  
+ATOM   1597  CB  ASN B  20      48.631 -28.798  60.606  1.00 28.44           C  
+ANISOU 1597  CB  ASN B  20     3073   2710   5024    346   -446  -1312       C  
+ATOM   1598  CG  ASN B  20      49.945 -28.283  60.072  1.00 34.22           C  
+ANISOU 1598  CG  ASN B  20     3490   3653   5858    389   -308  -1576       C  
+ATOM   1599  OD1 ASN B  20      50.193 -27.081  60.084  1.00 35.77           O  
+ANISOU 1599  OD1 ASN B  20     3572   3920   6098    313    -16  -1516       O  
+ATOM   1600  ND2 ASN B  20      50.791 -29.187  59.584  1.00 31.05           N  
+ANISOU 1600  ND2 ASN B  20     2944   3362   5494    481   -509  -1856       N  
+ATOM   1601  N   VAL B  21      45.402 -28.762  61.210  1.00 21.69           N  
+ANISOU 1601  N   VAL B  21     2621   1693   3926      1   -307   -597       N  
+ATOM   1602  CA  VAL B  21      44.151 -29.507  61.143  1.00 22.99           C  
+ANISOU 1602  CA  VAL B  21     2921   1828   3988   -145   -385   -444       C  
+ATOM   1603  C   VAL B  21      43.233 -28.922  60.061  1.00 22.92           C  
+ANISOU 1603  C   VAL B  21     2692   2109   3909   -188   -158   -284       C  
+ATOM   1604  O   VAL B  21      42.661 -29.659  59.254  1.00 23.63           O  
+ANISOU 1604  O   VAL B  21     2762   2275   3942   -208   -270   -312       O  
+ATOM   1605  CB  VAL B  21      43.430 -29.532  62.503  1.00 27.49           C  
+ANISOU 1605  CB  VAL B  21     3761   2166   4517   -328   -377   -257       C  
+ATOM   1606  CG1 VAL B  21      42.015 -30.103  62.355  1.00 25.55           C  
+ANISOU 1606  CG1 VAL B  21     3563   1956   4190   -542   -349   -112       C  
+ATOM   1607  CG2 VAL B  21      44.255 -30.349  63.512  1.00 20.13           C  
+ANISOU 1607  CG2 VAL B  21     3110   1090   3450   -259   -594   -365       C  
+ATOM   1608  N   VAL B  22      43.121 -27.601  60.018  1.00 20.49           N  
+ANISOU 1608  N   VAL B  22     2248   1932   3604   -183    110   -134       N  
+ATOM   1609  CA  VAL B  22      42.305 -26.947  58.998  1.00 25.07           C  
+ANISOU 1609  CA  VAL B  22     2682   2732   4110   -188    252      3       C  
+ATOM   1610  C   VAL B  22      43.019 -26.885  57.639  1.00 24.46           C  
+ANISOU 1610  C   VAL B  22     2521   2837   3936    -97    282   -129       C  
+ATOM   1611  O   VAL B  22      42.433 -27.180  56.594  1.00 23.44           O  
+ANISOU 1611  O   VAL B  22     2374   2830   3703    -88    224   -120       O  
+ATOM   1612  CB  VAL B  22      41.926 -25.520  59.433  1.00 27.64           C  
+ANISOU 1612  CB  VAL B  22     2951   3091   4462   -201    473    199       C  
+ATOM   1613  CG1 VAL B  22      41.092 -24.830  58.350  1.00 29.98           C  
+ANISOU 1613  CG1 VAL B  22     3154   3557   4679   -171    526    316       C  
+ATOM   1614  CG2 VAL B  22      41.198 -25.566  60.760  1.00 26.06           C  
+ANISOU 1614  CG2 VAL B  22     2825   2745   4333   -311    497    291       C  
+ATOM   1615  N   ARG B  23      44.285 -26.499  57.656  1.00 21.71           N  
+ANISOU 1615  N   ARG B  23     2124   2507   3619    -46    382   -278       N  
+ATOM   1616  CA  ARG B  23      45.038 -26.379  56.422  1.00 23.07           C  
+ANISOU 1616  CA  ARG B  23     2215   2873   3679    -21    494   -442       C  
+ATOM   1617  C   ARG B  23      45.156 -27.720  55.686  1.00 26.24           C  
+ANISOU 1617  C   ARG B  23     2611   3321   4036     44    285   -681       C  
+ATOM   1618  O   ARG B  23      44.983 -27.779  54.467  1.00 27.50           O  
+ANISOU 1618  O   ARG B  23     2776   3652   4021     39    335   -709       O  
+ATOM   1619  CB  ARG B  23      46.421 -25.798  56.707  1.00 21.65           C  
+ANISOU 1619  CB  ARG B  23     1925   2706   3594    -14    661   -629       C  
+ATOM   1620  CG  ARG B  23      47.152 -25.336  55.462  1.00 27.64           C  
+ANISOU 1620  CG  ARG B  23     2606   3696   4201    -81    912   -771       C  
+ATOM   1621  CD  ARG B  23      48.327 -24.452  55.815  1.00 41.45           C  
+ANISOU 1621  CD  ARG B  23     4226   5462   6060   -145   1147   -903       C  
+ATOM   1622  NE  ARG B  23      49.220 -25.080  56.787  1.00 39.55           N  
+ANISOU 1622  NE  ARG B  23     3844   5082   6102    -23    965  -1205       N  
+ATOM   1623  CZ  ARG B  23      50.261 -24.470  57.342  1.00 40.15           C  
+ANISOU 1623  CZ  ARG B  23     3878   5096   6279    -59    987  -1292       C  
+ATOM   1624  NH1 ARG B  23      50.548 -23.210  57.016  1.00 37.00           N1+
+ANISOU 1624  NH1 ARG B  23     3535   4772   5750   -209   1226  -1126       N1+
+ATOM   1625  NH2 ARG B  23      51.019 -25.119  58.217  1.00 37.63           N  
+ANISOU 1625  NH2 ARG B  23     3500   4621   6179     52    712  -1539       N  
+ATOM   1626  N   ASN B  24      45.419 -28.799  56.417  1.00 26.81           N  
+ANISOU 1626  N   ASN B  24     2727   3213   4245    107     18   -851       N  
+ATOM   1627  CA  ASN B  24      45.508 -30.106  55.767  1.00 24.12           C  
+ANISOU 1627  CA  ASN B  24     2406   2880   3877    187   -238  -1091       C  
+ATOM   1628  C   ASN B  24      44.167 -30.497  55.159  1.00 23.81           C  
+ANISOU 1628  C   ASN B  24     2453   2881   3714    124   -330   -892       C  
+ATOM   1629  O   ASN B  24      44.115 -31.059  54.064  1.00 27.62           O  
+ANISOU 1629  O   ASN B  24     2922   3489   4083    177   -409  -1023       O  
+ATOM   1630  CB  ASN B  24      45.949 -31.203  56.736  1.00 24.00           C  
+ANISOU 1630  CB  ASN B  24     2512   2588   4020    267   -593  -1291       C  
+ATOM   1631  CG  ASN B  24      47.385 -31.062  57.174  1.00 29.70           C  
+ANISOU 1631  CG  ASN B  24     3113   3258   4911    395   -616  -1616       C  
+ATOM   1632  OD1 ASN B  24      48.144 -30.247  56.641  1.00 33.68           O  
+ANISOU 1632  OD1 ASN B  24     3394   3978   5424    400   -326  -1742       O  
+ATOM   1633  ND2 ASN B  24      47.775 -31.871  58.153  1.00 30.15           N  
+ANISOU 1633  ND2 ASN B  24     3329   3071   5056    474   -947  -1677       N  
+ATOM   1634  N   HIS B  25      43.082 -30.211  55.872  1.00 24.51           N  
+ANISOU 1634  N   HIS B  25     2611   2867   3837     12   -321   -613       N  
+ATOM   1635  CA  HIS B  25      41.762 -30.535  55.350  1.00 25.12           C  
+ANISOU 1635  CA  HIS B  25     2705   2984   3857    -53   -413   -470       C  
+ATOM   1636  C   HIS B  25      41.555 -29.884  53.987  1.00 24.73           C  
+ANISOU 1636  C   HIS B  25     2598   3155   3643      3   -299   -430       C  
+ATOM   1637  O   HIS B  25      40.999 -30.497  53.076  1.00 31.60           O  
+ANISOU 1637  O   HIS B  25     3495   4084   4429     33   -462   -474       O  
+ATOM   1638  CB  HIS B  25      40.649 -30.096  56.305  1.00 23.40           C  
+ANISOU 1638  CB  HIS B  25     2487   2675   3727   -197   -339   -234       C  
+ATOM   1639  CG  HIS B  25      39.288 -30.477  55.824  1.00 27.50           C  
+ANISOU 1639  CG  HIS B  25     2956   3238   4256   -272   -447   -161       C  
+ATOM   1640  ND1 HIS B  25      38.769 -31.740  56.001  1.00 36.30           N  
+ANISOU 1640  ND1 HIS B  25     4154   4226   5411   -384   -671   -228       N  
+ATOM   1641  CD2 HIS B  25      38.365 -29.786  55.115  1.00 28.32           C  
+ANISOU 1641  CD2 HIS B  25     2939   3477   4346   -243   -405    -59       C  
+ATOM   1642  CE1 HIS B  25      37.568 -31.801  55.452  1.00 35.50           C  
+ANISOU 1642  CE1 HIS B  25     3935   4206   5347   -438   -725   -180       C  
+ATOM   1643  NE2 HIS B  25      37.304 -30.630  54.902  1.00 31.60           N  
+ANISOU 1643  NE2 HIS B  25     3310   3867   4830   -330   -590    -91       N  
+ATOM   1644  N   TRP B  26      42.024 -28.651  53.852  1.00 22.97           N  
+ANISOU 1644  N   TRP B  26     2349   3026   3354      7    -43   -347       N  
+ATOM   1645  CA  TRP B  26      41.876 -27.903  52.608  1.00 25.49           C  
+ANISOU 1645  CA  TRP B  26     2728   3502   3456     23     64   -278       C  
+ATOM   1646  C   TRP B  26      42.798 -28.441  51.510  1.00 27.90           C  
+ANISOU 1646  C   TRP B  26     3070   3949   3582     61     94   -534       C  
+ATOM   1647  O   TRP B  26      42.347 -28.753  50.418  1.00 28.25           O  
+ANISOU 1647  O   TRP B  26     3217   4072   3446     92    -10   -554       O  
+ATOM   1648  CB  TRP B  26      42.156 -26.406  52.831  1.00 23.53           C  
+ANISOU 1648  CB  TRP B  26     2508   3270   3165    -24    321   -109       C  
+ATOM   1649  CG  TRP B  26      41.946 -25.587  51.589  1.00 29.38           C  
+ANISOU 1649  CG  TRP B  26     3427   4104   3633    -38    390     -5       C  
+ATOM   1650  CD1 TRP B  26      42.912 -25.047  50.776  1.00 29.87           C  
+ANISOU 1650  CD1 TRP B  26     3616   4276   3455   -120    624    -75       C  
+ATOM   1651  CD2 TRP B  26      40.688 -25.251  50.994  1.00 28.90           C  
+ANISOU 1651  CD2 TRP B  26     3479   4009   3490     17    199    161       C  
+ATOM   1652  NE1 TRP B  26      42.324 -24.377  49.726  1.00 30.09           N  
+ANISOU 1652  NE1 TRP B  26     3915   4310   3206   -138    584     82       N  
+ATOM   1653  CE2 TRP B  26      40.961 -24.494  49.833  1.00 28.52           C  
+ANISOU 1653  CE2 TRP B  26     3706   4014   3117    -21    284    218       C  
+ATOM   1654  CE3 TRP B  26      39.354 -25.497  51.342  1.00 33.32           C  
+ANISOU 1654  CE3 TRP B  26     3935   4494   4232     82    -39    237       C  
+ATOM   1655  CZ2 TRP B  26      39.948 -23.996  49.011  1.00 34.09           C  
+ANISOU 1655  CZ2 TRP B  26     4633   4655   3664     50     62    359       C  
+ATOM   1656  CZ3 TRP B  26      38.351 -25.001  50.525  1.00 38.24           C  
+ANISOU 1656  CZ3 TRP B  26     4679   5092   4759    164   -241    332       C  
+ATOM   1657  CH2 TRP B  26      38.655 -24.255  49.375  1.00 42.35           C  
+ANISOU 1657  CH2 TRP B  26     5523   5623   4947    171   -226    399       C  
+ATOM   1658  N   VAL B  27      44.086 -28.562  51.809  1.00 27.93           N  
+ANISOU 1658  N   VAL B  27     2976   3986   3649     66    226   -769       N  
+ATOM   1659  CA  VAL B  27      45.080 -28.785  50.756  1.00 29.96           C  
+ANISOU 1659  CA  VAL B  27     3214   4433   3737     69    368  -1063       C  
+ATOM   1660  C   VAL B  27      45.186 -30.230  50.292  1.00 32.31           C  
+ANISOU 1660  C   VAL B  27     3482   4748   4049    190    103  -1355       C  
+ATOM   1661  O   VAL B  27      45.661 -30.490  49.185  1.00 42.16           O  
+ANISOU 1661  O   VAL B  27     4748   6174   5097    198    194  -1584       O  
+ATOM   1662  CB  VAL B  27      46.479 -28.307  51.201  1.00 31.09           C  
+ANISOU 1662  CB  VAL B  27     3187   4634   3992     24    630  -1290       C  
+ATOM   1663  CG1 VAL B  27      46.398 -26.889  51.730  1.00 31.91           C  
+ANISOU 1663  CG1 VAL B  27     3337   4689   4096    -95    863  -1000       C  
+ATOM   1664  CG2 VAL B  27      47.050 -29.221  52.275  1.00 30.31           C  
+ANISOU 1664  CG2 VAL B  27     2933   4379   4204    156    388  -1539       C  
+ATOM   1665  N   THR B  28      44.758 -31.172  51.122  1.00 31.19           N  
+ANISOU 1665  N   THR B  28     3329   4409   4115    264   -221  -1361       N  
+ATOM   1666  CA  THR B  28      44.767 -32.568  50.698  1.00 37.33           C  
+ANISOU 1666  CA  THR B  28     4125   5153   4904    380   -537  -1619       C  
+ATOM   1667  C   THR B  28      43.529 -32.921  49.858  1.00 41.83           C  
+ANISOU 1667  C   THR B  28     4834   5739   5321    370   -709  -1448       C  
+ATOM   1668  O   THR B  28      43.331 -34.082  49.507  1.00 44.06           O  
+ANISOU 1668  O   THR B  28     5162   5968   5613    453  -1008  -1615       O  
+ATOM   1669  CB  THR B  28      44.858 -33.521  51.901  1.00 38.57           C  
+ANISOU 1669  CB  THR B  28     4305   5036   5313    436   -867  -1708       C  
+ATOM   1670  OG1 THR B  28      43.730 -33.304  52.755  1.00 40.43           O  
+ANISOU 1670  OG1 THR B  28     4646   5102   5614    307   -921  -1349       O  
+ATOM   1671  CG2 THR B  28      46.173 -33.323  52.677  1.00 32.86           C  
+ANISOU 1671  CG2 THR B  28     3454   4262   4769    506   -804  -1963       C  
+ATOM   1672  N   LYS B  29      42.702 -31.920  49.544  1.00 38.54           N  
+ANISOU 1672  N   LYS B  29     4489   5373   4781    286   -565  -1141       N  
+ATOM   1673  CA  LYS B  29      41.537 -32.115  48.675  1.00 41.54           C  
+ANISOU 1673  CA  LYS B  29     4988   5763   5032    303   -755  -1012       C  
+ATOM   1674  C   LYS B  29      41.774 -31.560  47.272  1.00 45.25           C  
+ANISOU 1674  C   LYS B  29     5625   6413   5155    314   -603  -1047       C  
+ATOM   1675  O   LYS B  29      42.777 -30.889  47.016  1.00 39.96           O  
+ANISOU 1675  O   LYS B  29     4972   5875   4336    253   -281  -1135       O  
+ATOM   1676  CB  LYS B  29      40.282 -31.470  49.281  1.00 53.52           C  
+ANISOU 1676  CB  LYS B  29     6483   7172   6680    233   -799   -697       C  
+ATOM   1677  N   GLN B  32      42.125 -27.712  45.311  1.00 41.59           N  
+ANISOU 1677  N   GLN B  32     5875   6125   3803     12    123   -555       N  
+ATOM   1678  CA  GLN B  32      42.280 -26.870  46.495  1.00 39.51           C  
+ANISOU 1678  CA  GLN B  32     5447   5782   3782    -44    276   -394       C  
+ATOM   1679  C   GLN B  32      43.735 -26.739  46.949  1.00 39.37           C  
+ANISOU 1679  C   GLN B  32     5251   5884   3824   -164    646   -602       C  
+ATOM   1680  O   GLN B  32      44.404 -27.737  47.227  1.00 37.81           O  
+ANISOU 1680  O   GLN B  32     4814   5757   3794   -104    634   -901       O  
+ATOM   1681  CB  GLN B  32      41.432 -27.418  47.646  1.00 37.63           C  
+ANISOU 1681  CB  GLN B  32     4939   5413   3947     70     12   -323       C  
+ATOM   1682  CG  GLN B  32      39.940 -27.400  47.384  1.00 41.51           C  
+ANISOU 1682  CG  GLN B  32     5501   5792   4478    169   -328   -155       C  
+ATOM   1683  CD  GLN B  32      39.116 -27.652  48.637  1.00 45.01           C  
+ANISOU 1683  CD  GLN B  32     5668   6125   5309    194   -464    -82       C  
+ATOM   1684  OE1 GLN B  32      39.654 -27.956  49.701  1.00 50.31           O  
+ANISOU 1684  OE1 GLN B  32     6162   6774   6180    142   -341   -135       O  
+ATOM   1685  NE2 GLN B  32      37.801 -27.530  48.513  1.00 46.61           N  
+ANISOU 1685  NE2 GLN B  32     5845   6251   5613    265   -724     12       N  
+ATOM   1686  N   SER B  33      44.212 -25.499  47.030  1.00 37.47           N  
+ANISOU 1686  N   SER B  33     5128   5642   3467   -325    938   -467       N  
+ATOM   1687  CA  SER B  33      45.562 -25.231  47.515  1.00 38.93           C  
+ANISOU 1687  CA  SER B  33     5106   5930   3756   -457   1293   -676       C  
+ATOM   1688  C   SER B  33      45.616 -23.953  48.351  1.00 38.66           C  
+ANISOU 1688  C   SER B  33     5089   5773   3828   -549   1434   -425       C  
+ATOM   1689  O   SER B  33      44.672 -23.160  48.363  1.00 33.43           O  
+ANISOU 1689  O   SER B  33     4650   4964   3089   -527   1291   -102       O  
+ATOM   1690  CB  SER B  33      46.547 -25.137  46.349  1.00 42.48           C  
+ANISOU 1690  CB  SER B  33     5696   6594   3852   -662   1651   -922       C  
+ATOM   1691  OG  SER B  33      46.332 -23.961  45.597  1.00 51.11           O  
+ANISOU 1691  OG  SER B  33     7229   7642   4549   -870   1818   -658       O  
+ATOM   1692  N   ALA B  34      46.735 -23.759  49.037  1.00 36.92           N  
+ANISOU 1692  N   ALA B  34     4621   5605   3802   -632   1682   -614       N  
+ATOM   1693  CA  ALA B  34      46.852 -22.688  50.020  1.00 34.03           C  
+ANISOU 1693  CA  ALA B  34     4219   5106   3606   -686   1777   -417       C  
+ATOM   1694  C   ALA B  34      48.056 -21.781  49.792  1.00 40.73           C  
+ANISOU 1694  C   ALA B  34     5082   6033   4361   -935   2158   -518       C  
+ATOM   1695  O   ALA B  34      48.989 -22.125  49.060  1.00 46.06           O  
+ANISOU 1695  O   ALA B  34     5692   6850   4960  -1021   2290   -791       O  
+ATOM   1696  CB  ALA B  34      46.922 -23.280  51.413  1.00 38.01           C  
+ANISOU 1696  CB  ALA B  34     4407   5505   4531   -510   1592   -505       C  
+ATOM   1697  N   ALA B  35      48.014 -20.618  50.433  1.00 43.04           N  
+ANISOU 1697  N   ALA B  35     5452   6162   4740   -966   2141   -261       N  
+ATOM   1698  CA  ALA B  35      49.137 -19.689  50.501  1.00 36.83           C  
+ANISOU 1698  CA  ALA B  35     4638   5352   4002  -1103   2269   -308       C  
+ATOM   1699  C   ALA B  35      49.351 -19.262  51.955  1.00 38.44           C  
+ANISOU 1699  C   ALA B  35     4641   5414   4550   -983   2141   -256       C  
+ATOM   1700  O   ALA B  35      48.528 -19.568  52.830  1.00 32.19           O  
+ANISOU 1700  O   ALA B  35     3781   4525   3924   -814   1963   -137       O  
+ATOM   1701  CB  ALA B  35      48.890 -18.479  49.618  1.00 38.73           C  
+ANISOU 1701  CB  ALA B  35     5294   5525   3897  -1296   2356    -49       C  
+ATOM   1702  N   ILE B  52      58.235  -3.582  55.788  1.00 64.89           N  
+ANISOU 1702  N   ILE B  52     8812   7515   8329  -3149   3230    194       N  
+ATOM   1703  CA  ILE B  52      58.356  -2.967  54.465  1.00 69.39           C  
+ANISOU 1703  CA  ILE B  52     9780   8064   8522  -3533   3460    266       C  
+ATOM   1704  C   ILE B  52      58.636  -4.013  53.396  1.00 71.97           C  
+ANISOU 1704  C   ILE B  52    10056   8603   8685  -3670   3711     10       C  
+ATOM   1705  O   ILE B  52      57.900  -4.144  52.413  1.00 72.00           O  
+ANISOU 1705  O   ILE B  52    10401   8596   8361  -3723   3695    173       O  
+ATOM   1706  CB  ILE B  52      59.476  -1.911  54.426  1.00 77.32           C  
+ANISOU 1706  CB  ILE B  52    10844   9005   9530  -3926   3712    152       C  
+ATOM   1707  N   ALA B  53      59.719  -4.752  53.589  1.00 60.61           N  
+ANISOU 1707  N   ALA B  53     4896  10149   7986  -1588   2521  -1165       N  
+ATOM   1708  CA  ALA B  53      60.067  -5.832  52.681  1.00 61.51           C  
+ANISOU 1708  CA  ALA B  53     5061  10417   7894  -1333   2792  -1244       C  
+ATOM   1709  C   ALA B  53      59.159  -7.020  52.947  1.00 62.52           C  
+ANISOU 1709  C   ALA B  53     5545  10274   7937   -968   2847  -1356       C  
+ATOM   1710  O   ALA B  53      58.742  -7.721  52.025  1.00 65.64           O  
+ANISOU 1710  O   ALA B  53     6256  10565   8117   -948   3029  -1386       O  
+ATOM   1711  CB  ALA B  53      61.518  -6.221  52.849  1.00 62.36           C  
+ANISOU 1711  CB  ALA B  53     4708  10928   8059  -1050   2893  -1354       C  
+ATOM   1712  N   LEU B  54      58.848  -7.226  54.223  1.00 58.34           N  
+ANISOU 1712  N   LEU B  54     4982   9617   7568   -692   2674  -1424       N  
+ATOM   1713  CA  LEU B  54      58.036  -8.355  54.655  1.00 57.11           C  
+ANISOU 1713  CA  LEU B  54     5195   9119   7385   -277   2680  -1483       C  
+ATOM   1714  C   LEU B  54      56.606  -8.246  54.129  1.00 50.57           C  
+ANISOU 1714  C   LEU B  54     4886   7889   6439   -573   2615  -1335       C  
+ATOM   1715  O   LEU B  54      55.957  -9.255  53.835  1.00 48.85           O  
+ANISOU 1715  O   LEU B  54     5030   7427   6103   -407   2729  -1402       O  
+ATOM   1716  CB  LEU B  54      58.035  -8.442  56.181  1.00 55.83           C  
+ANISOU 1716  CB  LEU B  54     4935   8881   7397     93   2388  -1466       C  
+ATOM   1717  CG  LEU B  54      57.315  -9.635  56.802  1.00 53.40           C  
+ANISOU 1717  CG  LEU B  54     4986   8205   7100    587   2374  -1459       C  
+ATOM   1718  CD1 LEU B  54      57.812 -10.927  56.185  1.00 60.31           C  
+ANISOU 1718  CD1 LEU B  54     5945   9075   7897    962   2693  -1551       C  
+ATOM   1719  CD2 LEU B  54      57.529  -9.634  58.307  1.00 55.12           C  
+ANISOU 1719  CD2 LEU B  54     5012   8497   7435    951   2096  -1412       C  
+ATOM   1720  N   LYS B  55      56.132  -7.009  54.017  1.00 45.31           N  
+ANISOU 1720  N   LYS B  55     4236   7161   5820  -1019   2445  -1121       N  
+ATOM   1721  CA  LYS B  55      54.825  -6.714  53.453  1.00 44.09           C  
+ANISOU 1721  CA  LYS B  55     4466   6729   5558  -1325   2371   -887       C  
+ATOM   1722  C   LYS B  55      54.777  -7.127  51.993  1.00 48.11           C  
+ANISOU 1722  C   LYS B  55     5099   7432   5747  -1571   2633   -914       C  
+ATOM   1723  O   LYS B  55      53.814  -7.748  51.554  1.00 47.16           O  
+ANISOU 1723  O   LYS B  55     5334   7145   5439  -1622   2635   -887       O  
+ATOM   1724  CB  LYS B  55      54.499  -5.225  53.604  1.00 41.93           C  
+ANISOU 1724  CB  LYS B  55     4128   6356   5448  -1703   2206   -612       C  
+ATOM   1725  CG  LYS B  55      54.243  -4.787  55.044  1.00 43.28           C  
+ANISOU 1725  CG  LYS B  55     4301   6263   5882  -1515   1951   -609       C  
+ATOM   1726  CD  LYS B  55      54.215  -3.261  55.176  1.00 44.79           C  
+ANISOU 1726  CD  LYS B  55     4402   6338   6279  -1903   1886   -427       C  
+ATOM   1727  CE  LYS B  55      53.193  -2.625  54.238  1.00 41.69           C  
+ANISOU 1727  CE  LYS B  55     4292   5731   5816  -2094   1814     -7       C  
+ATOM   1728  NZ  LYS B  55      53.279  -1.138  54.243  1.00 43.03           N1+
+ANISOU 1728  NZ  LYS B  55     4426   5733   6191  -2260   1697    230       N1+
+ATOM   1729  N   ARG B  56      55.825  -6.784  51.248  1.00 51.66           N  
+ANISOU 1729  N   ARG B  56     5294   8209   6126  -1686   2749   -941       N  
+ATOM   1730  CA  ARG B  56      55.934  -7.176  49.849  1.00 54.42           C  
+ANISOU 1730  CA  ARG B  56     5782   8738   6159  -1830   2912   -966       C  
+ATOM   1731  C   ARG B  56      55.778  -8.692  49.705  1.00 54.94           C  
+ANISOU 1731  C   ARG B  56     6108   8702   6067  -1536   3111  -1279       C  
+ATOM   1732  O   ARG B  56      55.044  -9.170  48.841  1.00 53.23           O  
+ANISOU 1732  O   ARG B  56     6218   8434   5574  -1725   3142  -1305       O  
+ATOM   1733  CB  ARG B  56      57.272  -6.711  49.262  1.00 55.80           C  
+ANISOU 1733  CB  ARG B  56     5604   9264   6332  -1888   3053   -977       C  
+ATOM   1734  N   LEU B  57      56.447  -9.441  50.575  1.00 52.97           N  
+ANISOU 1734  N   LEU B  57     5722   8394   6011  -1053   3206  -1490       N  
+ATOM   1735  CA  LEU B  57      56.334 -10.894  50.585  1.00 54.30           C  
+ANISOU 1735  CA  LEU B  57     6177   8324   6131   -671   3362  -1724       C  
+ATOM   1736  C   LEU B  57      54.905 -11.377  50.850  1.00 55.60           C  
+ANISOU 1736  C   LEU B  57     6787   8085   6254   -752   3244  -1712       C  
+ATOM   1737  O   LEU B  57      54.412 -12.290  50.187  1.00 52.82           O  
+ANISOU 1737  O   LEU B  57     6785   7565   5719   -809   3347  -1863       O  
+ATOM   1738  CB  LEU B  57      57.276 -11.483  51.631  1.00 59.75           C  
+ANISOU 1738  CB  LEU B  57     6612   9010   7081    -64   3393  -1796       C  
+ATOM   1739  CG  LEU B  57      57.272 -13.009  51.701  1.00 62.34           C  
+ANISOU 1739  CG  LEU B  57     7230   9047   7410    406   3535  -1948       C  
+ATOM   1740  CD1 LEU B  57      57.623 -13.597  50.343  1.00 62.39           C  
+ANISOU 1740  CD1 LEU B  57     7392   9146   7168    295   3825  -2130       C  
+ATOM   1741  CD2 LEU B  57      58.233 -13.500  52.769  1.00 64.18           C  
+ANISOU 1741  CD2 LEU B  57     7160   9365   7861   1038   3516  -1893       C  
+ATOM   1742  N   ILE B  58      54.244 -10.765  51.826  1.00 50.07           N  
+ANISOU 1742  N   ILE B  58     6066   7230   5730   -776   3040  -1537       N  
+ATOM   1743  CA  ILE B  58      52.873 -11.133  52.160  1.00 48.92           C  
+ANISOU 1743  CA  ILE B  58     6308   6703   5578   -834   2872  -1435       C  
+ATOM   1744  C   ILE B  58      51.922 -10.765  51.024  1.00 50.78           C  
+ANISOU 1744  C   ILE B  58     6755   7047   5493  -1407   2821  -1290       C  
+ATOM   1745  O   ILE B  58      50.988 -11.509  50.713  1.00 44.44           O  
+ANISOU 1745  O   ILE B  58     6301   6057   4527  -1543   2825  -1353       O  
+ATOM   1746  CB  ILE B  58      52.417 -10.460  53.463  1.00 42.96           C  
+ANISOU 1746  CB  ILE B  58     5466   5745   5112   -675   2522  -1172       C  
+ATOM   1747  CG1 ILE B  58      53.245 -10.985  54.638  1.00 43.99           C  
+ANISOU 1747  CG1 ILE B  58     5409   5824   5479    -98   2538  -1298       C  
+ATOM   1748  CG2 ILE B  58      50.937 -10.705  53.707  1.00 37.57           C  
+ANISOU 1748  CG2 ILE B  58     5137   4718   4419   -778   2336   -990       C  
+ATOM   1749  CD1 ILE B  58      52.930 -10.321  55.961  1.00 40.54           C  
+ANISOU 1749  CD1 ILE B  58     4877   5265   5260     52   2214  -1101       C  
+ATOM   1750  N   ASN B  59      52.177  -9.623  50.392  1.00 47.42           N  
+ANISOU 1750  N   ASN B  59     6098   6944   4975  -1754   2762  -1071       N  
+ATOM   1751  CA  ASN B  59      51.368  -9.186  49.263  1.00 45.79           C  
+ANISOU 1751  CA  ASN B  59     6020   6890   4489  -2191   2586   -827       C  
+ATOM   1752  C   ASN B  59      51.425 -10.211  48.138  1.00 49.73           C  
+ANISOU 1752  C   ASN B  59     6741   7518   4636  -2322   2778  -1139       C  
+ATOM   1753  O   ASN B  59      50.409 -10.513  47.517  1.00 53.57           O  
+ANISOU 1753  O   ASN B  59     7467   8017   4872  -2619   2654  -1094       O  
+ATOM   1754  CB  ASN B  59      51.830  -7.820  48.751  1.00 46.74           C  
+ANISOU 1754  CB  ASN B  59     5856   7252   4651  -2367   2451   -516       C  
+ATOM   1755  CG  ASN B  59      51.657  -6.718  49.782  1.00 44.12           C  
+ANISOU 1755  CG  ASN B  59     5363   6710   4690  -2276   2232   -215       C  
+ATOM   1756  OD1 ASN B  59      50.860  -6.843  50.720  1.00 43.93           O  
+ANISOU 1756  OD1 ASN B  59     5464   6392   4837  -2151   2100   -137       O  
+ATOM   1757  ND2 ASN B  59      52.406  -5.628  49.613  1.00 46.49           N  
+ANISOU 1757  ND2 ASN B  59     5407   7128   5129  -2342   2208    -58       N  
+ATOM   1758  N   GLY B  60      52.618 -10.746  47.890  1.00 52.83           N  
+ANISOU 1758  N   GLY B  60     7032   8011   5031  -2089   3060  -1449       N  
+ATOM   1759  CA  GLY B  60      52.807 -11.771  46.878  1.00 57.37           C  
+ANISOU 1759  CA  GLY B  60     7825   8637   5335  -2149   3279  -1777       C  
+ATOM   1760  C   GLY B  60      52.044 -13.041  47.207  1.00 57.90           C  
+ANISOU 1760  C   GLY B  60     8276   8295   5426  -2050   3328  -2021       C  
+ATOM   1761  O   GLY B  60      51.510 -13.704  46.318  1.00 60.51           O  
+ANISOU 1761  O   GLY B  60     8882   8632   5479  -2350   3380  -2204       O  
+ATOM   1762  N   GLY B  61      51.993 -13.381  48.491  1.00 55.80           N  
+ANISOU 1762  N   GLY B  61     8023   7671   5505  -1639   3302  -2013       N  
+ATOM   1763  CA  GLY B  61      51.226 -14.527  48.945  1.00 55.24           C  
+ANISOU 1763  CA  GLY B  61     8308   7146   5536  -1516   3319  -2157       C  
+ATOM   1764  C   GLY B  61      49.744 -14.291  48.741  1.00 53.33           C  
+ANISOU 1764  C   GLY B  61     8297   6887   5079  -2019   3107  -2002       C  
+ATOM   1765  O   GLY B  61      49.025 -15.174  48.270  1.00 56.17           O  
+ANISOU 1765  O   GLY B  61     8970   7084   5288  -2268   3146  -2181       O  
+ATOM   1766  N   LEU B  62      49.294 -13.089  49.092  1.00 48.77           N  
+ANISOU 1766  N   LEU B  62     7534   6495   4503  -2180   2874  -1625       N  
+ATOM   1767  CA  LEU B  62      47.896 -12.701  48.939  1.00 47.03           C  
+ANISOU 1767  CA  LEU B  62     7422   6334   4114  -2602   2591  -1311       C  
+ATOM   1768  C   LEU B  62      47.468 -12.635  47.478  1.00 57.05           C  
+ANISOU 1768  C   LEU B  62     8724   7990   4961  -3122   2475  -1311       C  
+ATOM   1769  O   LEU B  62      46.300 -12.867  47.152  1.00 51.52           O  
+ANISOU 1769  O   LEU B  62     8171   7338   4066  -3478   2274  -1213       O  
+ATOM   1770  CB  LEU B  62      47.649 -11.353  49.609  1.00 44.20           C  
+ANISOU 1770  CB  LEU B  62     6765   6025   4002  -2530   2294   -800       C  
+ATOM   1771  CG  LEU B  62      47.508 -11.418  51.129  1.00 39.27           C  
+ANISOU 1771  CG  LEU B  62     6129   4972   3821  -2064   2190   -706       C  
+ATOM   1772  CD1 LEU B  62      47.580 -10.023  51.727  1.00 36.46           C  
+ANISOU 1772  CD1 LEU B  62     5478   4662   3715  -1987   1977   -317       C  
+ATOM   1773  CD2 LEU B  62      46.209 -12.118  51.508  1.00 38.31           C  
+ANISOU 1773  CD2 LEU B  62     6271   4562   3726  -2129   2052   -624       C  
+ATOM   1774  N   ASN B  63      48.412 -12.308  46.601  1.00 48.61           N  
+ANISOU 1774  N   ASN B  63     7247   7152   4070   -536   1830    337       N  
+ATOM   1775  CA  ASN B  63      48.132 -12.303  45.173  1.00 48.87           C  
+ANISOU 1775  CA  ASN B  63     7489   7308   3769   -511   1843    380       C  
+ATOM   1776  C   ASN B  63      47.845 -13.728  44.711  1.00 43.67           C  
+ANISOU 1776  C   ASN B  63     6949   6702   2942   -415   1801    137       C  
+ATOM   1777  O   ASN B  63      48.418 -14.686  45.239  1.00 41.64           O  
+ANISOU 1777  O   ASN B  63     6576   6417   2828   -354   1878    -41       O  
+ATOM   1778  CB  ASN B  63      49.295 -11.693  44.385  1.00 50.12           C  
+ANISOU 1778  CB  ASN B  63     7588   7580   3875   -533   2093    517       C  
+ATOM   1779  N   ASN B  64      46.947 -13.851  43.738  1.00 42.87           N  
+ANISOU 1779  N   ASN B  64     7073   6665   2550   -401   1659    132       N  
+ATOM   1780  CA  ASN B  64      46.497 -15.144  43.221  1.00 45.37           C  
+ANISOU 1780  CA  ASN B  64     7528   7015   2694   -327   1567   -102       C  
+ATOM   1781  C   ASN B  64      45.810 -16.010  44.284  1.00 42.49           C  
+ANISOU 1781  C   ASN B  64     7112   6515   2518   -321   1385   -269       C  
+ATOM   1782  O   ASN B  64      45.766 -17.233  44.160  1.00 45.12           O  
+ANISOU 1782  O   ASN B  64     7489   6833   2820   -256   1357   -489       O  
+ATOM   1783  CB  ASN B  64      47.665 -15.917  42.590  1.00 53.42           C  
+ANISOU 1783  CB  ASN B  64     8524   8138   3636   -241   1819   -240       C  
+ATOM   1784  N   THR B  65      45.284 -15.374  45.327  1.00 37.32           N  
+ANISOU 1784  N   THR B  65     6363   5756   2061   -388   1264   -162       N  
+ATOM   1785  CA  THR B  65      44.304 -16.031  46.195  1.00 38.68           C  
+ANISOU 1785  CA  THR B  65     6523   5821   2353   -403   1042   -278       C  
+ATOM   1786  C   THR B  65      43.009 -15.231  46.129  1.00 44.77           C  
+ANISOU 1786  C   THR B  65     7383   6577   3051   -469    786   -126       C  
+ATOM   1787  O   THR B  65      43.016 -14.075  45.711  1.00 41.56           O  
+ANISOU 1787  O   THR B  65     7008   6207   2575   -499    805     82       O  
+ATOM   1788  CB  THR B  65      44.770 -16.157  47.662  1.00 39.39           C  
+ANISOU 1788  CB  THR B  65     6400   5806   2761   -411   1112   -313       C  
+ATOM   1789  OG1 THR B  65      44.808 -14.866  48.289  1.00 33.34           O  
+ANISOU 1789  OG1 THR B  65     5537   5007   2124   -482   1126   -109       O  
+ATOM   1790  CG2 THR B  65      46.137 -16.828  47.739  1.00 32.67           C  
+ANISOU 1790  CG2 THR B  65     5423   4969   2020   -331   1355   -428       C  
+ATOM   1791  N   SER B  66      41.895 -15.843  46.524  1.00 39.97           N  
+ANISOU 1791  N   SER B  66     6799   5909   2479   -487    538   -218       N  
+ATOM   1792  CA  SER B  66      40.605 -15.177  46.396  1.00 37.81           C  
+ANISOU 1792  CA  SER B  66     6581   5631   2155   -531    266    -78       C  
+ATOM   1793  C   SER B  66      39.893 -15.097  47.734  1.00 30.37           C  
+ANISOU 1793  C   SER B  66     5503   4586   1450   -574    117    -53       C  
+ATOM   1794  O   SER B  66      38.960 -14.318  47.907  1.00 30.75           O  
+ANISOU 1794  O   SER B  66     5510   4609   1564   -588    -77    104       O  
+ATOM   1795  CB  SER B  66      39.727 -15.897  45.362  1.00 39.57           C  
+ANISOU 1795  CB  SER B  66     6952   5908   2176   -517     51   -184       C  
+ATOM   1796  OG  SER B  66      39.547 -17.265  45.706  1.00 43.81           O  
+ANISOU 1796  OG  SER B  66     7467   6383   2795   -510    -10   -421       O  
+ATOM   1797  N   VAL B  67      40.351 -15.901  48.685  1.00 28.54           N  
+ANISOU 1797  N   VAL B  67     5118   4279   1448   -545    207   -198       N  
+ATOM   1798  CA  VAL B  67      39.732 -15.992  49.995  1.00 26.03           C  
+ANISOU 1798  CA  VAL B  67     4585   3853   1452   -533     82   -188       C  
+ATOM   1799  C   VAL B  67      40.830 -16.002  51.046  1.00 27.60           C  
+ANISOU 1799  C   VAL B  67     4610   3995   1881   -498    291   -215       C  
+ATOM   1800  O   VAL B  67      41.818 -16.726  50.902  1.00 29.11           O  
+ANISOU 1800  O   VAL B  67     4817   4202   2043   -469    471   -348       O  
+ATOM   1801  CB  VAL B  67      38.876 -17.273  50.142  1.00 26.00           C  
+ANISOU 1801  CB  VAL B  67     4580   3800   1499   -542   -103   -354       C  
+ATOM   1802  CG1 VAL B  67      38.279 -17.375  51.553  1.00 23.84           C  
+ANISOU 1802  CG1 VAL B  67     4079   3423   1555   -530   -191   -323       C  
+ATOM   1803  CG2 VAL B  67      37.797 -17.355  49.048  1.00 30.13           C  
+ANISOU 1803  CG2 VAL B  67     5272   4383   1791   -590   -347   -350       C  
+ATOM   1804  N   THR B  68      40.671 -15.178  52.076  1.00 22.42           N  
+ANISOU 1804  N   THR B  68     3793   3276   1449   -492    263    -94       N  
+ATOM   1805  CA  THR B  68      41.550 -15.224  53.240  1.00 21.65           C  
+ANISOU 1805  CA  THR B  68     3522   3119   1584   -461    398   -127       C  
+ATOM   1806  C   THR B  68      40.829 -15.876  54.412  1.00 23.68           C  
+ANISOU 1806  C   THR B  68     3652   3294   2051   -430    269   -184       C  
+ATOM   1807  O   THR B  68      39.722 -15.473  54.789  1.00 26.39           O  
+ANISOU 1807  O   THR B  68     3953   3607   2466   -434    109   -102       O  
+ATOM   1808  CB  THR B  68      42.043 -13.823  53.654  1.00 22.47           C  
+ANISOU 1808  CB  THR B  68     3550   3200   1789   -480    474     31       C  
+ATOM   1809  OG1 THR B  68      42.781 -13.245  52.575  1.00 26.91           O  
+ANISOU 1809  OG1 THR B  68     4222   3833   2168   -521    623    105       O  
+ATOM   1810  CG2 THR B  68      42.949 -13.917  54.883  1.00 20.23           C  
+ANISOU 1810  CG2 THR B  68     3089   2860   1739   -453    575    -20       C  
+ATOM   1811  N  ACYS B  69      41.497 -16.844  55.017  0.39 22.64           N  
+ANISOU 1811  N  ACYS B  69     3449   3126   2028   -392    353   -309       N  
+ATOM   1812  N  BCYS B  69      41.432 -16.930  54.961  0.61 22.59           N  
+ANISOU 1812  N  BCYS B  69     3451   3119   2012   -393    344   -317       N  
+ATOM   1813  CA ACYS B  69      40.919 -17.593  56.110  0.39 19.95           C  
+ANISOU 1813  CA ACYS B  69     3006   2707   1869   -366    258   -354       C  
+ATOM   1814  CA BCYS B  69      40.887 -17.615  56.139  0.61 19.59           C  
+ANISOU 1814  CA BCYS B  69     2958   2659   1828   -365    253   -354       C  
+ATOM   1815  C  ACYS B  69      41.716 -17.385  57.396  0.39 18.74           C  
+ANISOU 1815  C  ACYS B  69     2703   2510   1906   -321    344   -337       C  
+ATOM   1816  C  BCYS B  69      41.736 -17.332  57.370  0.61 19.17           C  
+ANISOU 1816  C  BCYS B  69     2759   2568   1957   -322    347   -334       C  
+ATOM   1817  O  ACYS B  69      42.807 -17.937  57.547  0.39 19.90           O  
+ANISOU 1817  O  ACYS B  69     2813   2653   2096   -284    466   -418       O  
+ATOM   1818  O  BCYS B  69      42.878 -17.790  57.460  0.61 19.03           O  
+ANISOU 1818  O  BCYS B  69     2706   2552   1973   -288    478   -408       O  
+ATOM   1819  CB ACYS B  69      40.873 -19.065  55.733  0.39 20.25           C  
+ANISOU 1819  CB ACYS B  69     3112   2711   1869   -357    240   -513       C  
+ATOM   1820  CB BCYS B  69      40.816 -19.127  55.918  0.61 20.24           C  
+ANISOU 1820  CB BCYS B  69     3092   2698   1899   -354    231   -512       C  
+ATOM   1821  SG ACYS B  69      39.977 -20.042  56.886  0.39 22.88           S  
+ANISOU 1821  SG ACYS B  69     3346   2938   2410   -351    112   -537       S  
+ATOM   1822  SG BCYS B  69      39.570 -19.687  54.760  0.61 24.51           S  
+ANISOU 1822  SG BCYS B  69     3788   3253   2271   -419     43   -568       S  
+ATOM   1823  N   VAL B  70      41.181 -16.577  58.312  1.00 19.45           N  
+ANISOU 1823  N   VAL B  70     2711   2571   2108   -315    276   -238       N  
+ATOM   1824  CA  VAL B  70      41.881 -16.276  59.566  1.00 15.83           C  
+ANISOU 1824  CA  VAL B  70     2135   2077   1802   -277    329   -227       C  
+ATOM   1825  C   VAL B  70      41.632 -17.417  60.541  1.00 17.83           C  
+ANISOU 1825  C   VAL B  70     2331   2278   2164   -231    289   -286       C  
+ATOM   1826  O   VAL B  70      40.497 -17.691  60.893  1.00 17.76           O  
+ANISOU 1826  O   VAL B  70     2316   2244   2189   -233    192   -256       O  
+ATOM   1827  CB  VAL B  70      41.411 -14.957  60.214  1.00 16.46           C  
+ANISOU 1827  CB  VAL B  70     2178   2133   1945   -277    279   -119       C  
+ATOM   1828  CG1 VAL B  70      42.226 -14.672  61.484  1.00 17.41           C  
+ANISOU 1828  CG1 VAL B  70     2202   2218   2195   -243    317   -135       C  
+ATOM   1829  CG2 VAL B  70      41.545 -13.800  59.234  1.00 16.26           C  
+ANISOU 1829  CG2 VAL B  70     2221   2131   1825   -326    305    -32       C  
+ATOM   1830  N   LEU B  71      42.690 -18.083  60.977  1.00 17.19           N  
+ANISOU 1830  N   LEU B  71     2200   2181   2149   -188    364   -356       N  
+ATOM   1831  CA  LEU B  71      42.515 -19.212  61.897  1.00 16.58           C  
+ANISOU 1831  CA  LEU B  71     2085   2041   2173   -139    326   -391       C  
+ATOM   1832  C   LEU B  71      42.750 -18.739  63.309  1.00 17.82           C  
+ANISOU 1832  C   LEU B  71     2158   2187   2427    -98    307   -336       C  
+ATOM   1833  O   LEU B  71      43.876 -18.404  63.681  1.00 15.29           O  
+ANISOU 1833  O   LEU B  71     1775   1881   2152    -73    354   -351       O  
+ATOM   1834  CB  LEU B  71      43.468 -20.353  61.521  1.00 19.81           C  
+ANISOU 1834  CB  LEU B  71     2502   2423   2600    -95    402   -499       C  
+ATOM   1835  CG  LEU B  71      43.418 -20.746  60.053  1.00 20.56           C  
+ANISOU 1835  CG  LEU B  71     2711   2540   2562   -127    442   -583       C  
+ATOM   1836  CD1 LEU B  71      44.433 -21.846  59.761  1.00 18.34           C  
+ANISOU 1836  CD1 LEU B  71     2435   2220   2315    -56    543   -707       C  
+ATOM   1837  CD2 LEU B  71      42.026 -21.177  59.638  1.00 17.33           C  
+ANISOU 1837  CD2 LEU B  71     2388   2098   2099   -184    317   -586       C  
+ATOM   1838  N   ILE B  72      41.679 -18.723  64.105  1.00 15.96           N  
+ANISOU 1838  N   ILE B  72     1915   1927   2221    -91    238   -275       N  
+ATOM   1839  CA  ILE B  72      41.689 -17.993  65.370  1.00 16.52           C  
+ANISOU 1839  CA  ILE B  72     1942   2000   2333    -52    221   -223       C  
+ATOM   1840  C   ILE B  72      42.039 -18.889  66.552  1.00 12.39           C  
+ANISOU 1840  C   ILE B  72     1392   1446   1871     11    211   -225       C  
+ATOM   1841  O   ILE B  72      41.269 -19.782  66.903  1.00 16.75           O  
+ANISOU 1841  O   ILE B  72     1956   1961   2449     19    192   -193       O  
+ATOM   1842  CB  ILE B  72      40.314 -17.331  65.646  1.00 19.32           C  
+ANISOU 1842  CB  ILE B  72     2303   2359   2678    -59    179   -148       C  
+ATOM   1843  CG1 ILE B  72      39.849 -16.523  64.429  1.00 22.35           C  
+ANISOU 1843  CG1 ILE B  72     2722   2766   3004   -112    161   -125       C  
+ATOM   1844  CG2 ILE B  72      40.403 -16.431  66.884  1.00 14.31           C  
+ANISOU 1844  CG2 ILE B  72     1653   1725   2059     -8    179   -122       C  
+ATOM   1845  CD1 ILE B  72      38.364 -16.169  64.467  1.00 23.59           C  
+ANISOU 1845  CD1 ILE B  72     2861   2925   3177   -111    105    -50       C  
+ATOM   1846  N   GLY B  73      43.206 -18.639  67.142  1.00 16.75           N  
+ANISOU 1846  N   GLY B  73     1902   2010   2451     49    214   -250       N  
+ATOM   1847  CA  GLY B  73      43.622 -19.275  68.375  1.00 16.61           C  
+ANISOU 1847  CA  GLY B  73     1866   1974   2470    120    178   -235       C  
+ATOM   1848  C   GLY B  73      43.580 -18.275  69.519  1.00 21.28           C  
+ANISOU 1848  C   GLY B  73     2466   2594   3025    144    134   -208       C  
+ATOM   1849  O   GLY B  73      42.913 -17.247  69.427  1.00 17.23           O  
+ANISOU 1849  O   GLY B  73     1980   2093   2474    115    140   -194       O  
+ATOM   1850  N   SER B  74      44.344 -18.542  70.574  1.00 13.79           N  
+ANISOU 1850  N   SER B  74     1502   1651   2086    204     79   -209       N  
+ATOM   1851  CA  SER B  74      44.230 -17.765  71.809  1.00 14.82           C  
+ANISOU 1851  CA  SER B  74     1677   1806   2148    239     23   -198       C  
+ATOM   1852  C   SER B  74      44.768 -16.330  71.681  1.00 18.97           C  
+ANISOU 1852  C   SER B  74     2185   2341   2679    192     -7   -259       C  
+ATOM   1853  O   SER B  74      44.268 -15.416  72.360  1.00 16.46           O  
+ANISOU 1853  O   SER B  74     1934   2023   2298    204    -28   -268       O  
+ATOM   1854  CB  SER B  74      44.959 -18.504  72.945  1.00 18.87           C  
+ANISOU 1854  CB  SER B  74     2193   2327   2649    316    -56   -178       C  
+ATOM   1855  OG  SER B  74      44.366 -19.788  73.170  1.00 19.91           O  
+ANISOU 1855  OG  SER B  74     2360   2425   2781    356    -25    -99       O  
+ATOM   1856  N   GLN B  75      45.769 -16.137  70.820  1.00 18.61           N  
+ANISOU 1856  N   GLN B  75     2056   2298   2718    138      2   -301       N  
+ATOM   1857  CA  GLN B  75      46.466 -14.848  70.712  1.00 18.83           C  
+ANISOU 1857  CA  GLN B  75     2049   2319   2788     74    -30   -346       C  
+ATOM   1858  C   GLN B  75      46.486 -14.257  69.294  1.00 17.18           C  
+ANISOU 1858  C   GLN B  75     1814   2099   2617    -14     60   -337       C  
+ATOM   1859  O   GLN B  75      47.122 -13.233  69.058  1.00 19.77           O  
+ANISOU 1859  O   GLN B  75     2104   2407   3002    -85     52   -354       O  
+ATOM   1860  CB  GLN B  75      47.908 -14.984  71.205  1.00 22.75           C  
+ANISOU 1860  CB  GLN B  75     2438   2836   3369     78   -116   -388       C  
+ATOM   1861  CG  GLN B  75      48.036 -15.197  72.701  1.00 26.41           C  
+ANISOU 1861  CG  GLN B  75     2950   3315   3771    153   -247   -398       C  
+ATOM   1862  CD  GLN B  75      47.561 -13.985  73.483  1.00 31.75           C  
+ANISOU 1862  CD  GLN B  75     3735   3967   4363    138   -308   -440       C  
+ATOM   1863  OE1 GLN B  75      47.910 -12.851  73.157  1.00 38.20           O  
+ANISOU 1863  OE1 GLN B  75     4530   4744   5241     56   -324   -487       O  
+ATOM   1864  NE2 GLN B  75      46.767 -14.221  74.520  1.00 32.09           N  
+ANISOU 1864  NE2 GLN B  75     3901   4025   4268    221   -329   -422       N  
+ATOM   1865  N   THR B  76      45.769 -14.888  68.368  1.00 16.57           N  
+ANISOU 1865  N   THR B  76     1766   2029   2502    -14    138   -304       N  
+ATOM   1866  CA  THR B  76      45.689 -14.425  66.988  1.00 16.87           C  
+ANISOU 1866  CA  THR B  76     1811   2070   2528    -87    218   -284       C  
+ATOM   1867  C   THR B  76      45.307 -12.934  66.835  1.00 18.96           C  
+ANISOU 1867  C   THR B  76     2124   2294   2786   -142    206   -251       C  
+ATOM   1868  O   THR B  76      45.905 -12.206  66.028  1.00 19.15           O  
+ANISOU 1868  O   THR B  76     2125   2309   2841   -219    254   -232       O  
+ATOM   1869  CB  THR B  76      44.694 -15.296  66.215  1.00 15.43           C  
+ANISOU 1869  CB  THR B  76     1687   1897   2279    -74    256   -263       C  
+ATOM   1870  OG1 THR B  76      44.991 -16.685  66.484  1.00 18.09           O  
+ANISOU 1870  OG1 THR B  76     1996   2235   2641    -17    258   -296       O  
+ATOM   1871  CG2 THR B  76      44.825 -15.044  64.716  1.00 15.44           C  
+ANISOU 1871  CG2 THR B  76     1710   1921   2235   -139    333   -252       C  
+ATOM   1872  N   PHE B  77      44.315 -12.497  67.609  1.00 17.84           N  
+ANISOU 1872  N   PHE B  77     2049   2119   2611    -97    155   -238       N  
+ATOM   1873  CA  PHE B  77      43.849 -11.100  67.615  1.00 19.32           C  
+ANISOU 1873  CA  PHE B  77     2294   2241   2808   -119    137   -214       C  
+ATOM   1874  C   PHE B  77      44.957 -10.073  67.842  1.00 18.81           C  
+ANISOU 1874  C   PHE B  77     2202   2121   2826   -188    105   -251       C  
+ATOM   1875  O   PHE B  77      44.840  -8.911  67.419  1.00 21.21           O  
+ANISOU 1875  O   PHE B  77     2546   2348   3164   -239    110   -217       O  
+ATOM   1876  CB  PHE B  77      42.792 -10.913  68.711  1.00 15.18           C  
+ANISOU 1876  CB  PHE B  77     1829   1694   2243    -29    101   -223       C  
+ATOM   1877  CG  PHE B  77      43.383 -10.782  70.089  1.00 15.93           C  
+ANISOU 1877  CG  PHE B  77     1939   1780   2334     10     37   -299       C  
+ATOM   1878  CD1 PHE B  77      43.795 -11.918  70.788  1.00 18.55           C  
+ANISOU 1878  CD1 PHE B  77     2241   2173   2635     53     12   -319       C  
+ATOM   1879  CD2 PHE B  77      43.533  -9.534  70.689  1.00 15.70           C  
+ANISOU 1879  CD2 PHE B  77     1969   1672   2326      6    -14   -354       C  
+ATOM   1880  CE1 PHE B  77      44.350 -11.807  72.039  1.00 16.14           C  
+ANISOU 1880  CE1 PHE B  77     1962   1870   2298     91    -71   -381       C  
+ATOM   1881  CE2 PHE B  77      44.093  -9.412  71.955  1.00 17.13           C  
+ANISOU 1881  CE2 PHE B  77     2183   1848   2477     38    -98   -441       C  
+ATOM   1882  CZ  PHE B  77      44.502 -10.543  72.632  1.00 17.19           C  
+ANISOU 1882  CZ  PHE B  77     2161   1938   2432     81   -132   -451       C  
+ATOM   1883  N   ASN B  78      46.020 -10.494  68.524  1.00 16.56           N  
+ANISOU 1883  N   ASN B  78     1842   1863   2586   -191     60   -312       N  
+ATOM   1884  CA  ASN B  78      47.105  -9.594  68.929  1.00 23.72           C  
+ANISOU 1884  CA  ASN B  78     2699   2718   3595   -266     -5   -360       C  
+ATOM   1885  C   ASN B  78      48.328  -9.582  68.001  1.00 20.27           C  
+ANISOU 1885  C   ASN B  78     2131   2306   3266   -369     60   -335       C  
+ATOM   1886  O   ASN B  78      49.326  -8.903  68.290  1.00 19.55           O  
+ANISOU 1886  O   ASN B  78     1958   2174   3294   -453      5   -367       O  
+ATOM   1887  CB  ASN B  78      47.570  -9.968  70.341  1.00 22.13           C  
+ANISOU 1887  CB  ASN B  78     2485   2540   3385   -208   -127   -442       C  
+ATOM   1888  CG  ASN B  78      48.255  -8.833  71.052  1.00 29.41           C  
+ANISOU 1888  CG  ASN B  78     3411   3381   4381   -274   -244   -517       C  
+ATOM   1889  OD1 ASN B  78      47.859  -7.681  70.924  1.00 27.95           O  
+ANISOU 1889  OD1 ASN B  78     3307   3093   4219   -317   -245   -522       O  
+ATOM   1890  ND2 ASN B  78      49.311  -9.151  71.798  1.00 36.70           N  
+ANISOU 1890  ND2 ASN B  78     4245   4342   5357   -283   -359   -576       N  
+ATOM   1891  N   ARG B  79      48.275 -10.333  66.906  1.00 17.02           N  
+ANISOU 1891  N   ARG B  79     1691   1960   2814   -367    179   -285       N  
+ATOM   1892  CA  ARG B  79      49.454 -10.486  66.047  1.00 15.42           C  
+ANISOU 1892  CA  ARG B  79     1358   1804   2697   -441    278   -267       C  
+ATOM   1893  C   ARG B  79      49.497  -9.433  64.934  1.00 16.05           C  
+ANISOU 1893  C   ARG B  79     1468   1842   2788   -553    377   -179       C  
+ATOM   1894  O   ARG B  79      48.538  -9.294  64.157  1.00 21.05           O  
+ANISOU 1894  O   ARG B  79     2224   2469   3305   -542    425   -115       O  
+ATOM   1895  CB  ARG B  79      49.496 -11.898  65.451  1.00 17.00           C  
+ANISOU 1895  CB  ARG B  79     1528   2093   2839   -368    369   -279       C  
+ATOM   1896  CG  ARG B  79      49.415 -12.998  66.498  1.00 16.78           C  
+ANISOU 1896  CG  ARG B  79     1483   2086   2805   -255    278   -337       C  
+ATOM   1897  CD  ARG B  79      50.519 -12.835  67.548  1.00 17.03           C  
+ANISOU 1897  CD  ARG B  79     1387   2118   2966   -259    167   -383       C  
+ATOM   1898  NE  ARG B  79      51.860 -12.942  66.984  1.00 23.81           N  
+ANISOU 1898  NE  ARG B  79     2061   3020   3966   -305    243   -387       N  
+ATOM   1899  CZ  ARG B  79      52.976 -12.827  67.698  1.00 28.60           C  
+ANISOU 1899  CZ  ARG B  79     2507   3639   4722   -321    147   -419       C  
+ATOM   1900  NH1 ARG B  79      52.908 -12.592  68.998  1.00 32.65           N1+
+ANISOU 1900  NH1 ARG B  79     3054   4122   5230   -297    -44   -460       N1+
+ATOM   1901  NH2 ARG B  79      54.158 -12.933  67.111  1.00 29.58           N  
+ANISOU 1901  NH2 ARG B  79     2432   3810   4996   -361    240   -412       N  
+ATOM   1902  N   ARG B  80      50.625  -8.724  64.860  1.00 18.94           N  
+ANISOU 1902  N   ARG B  80     1714   2180   3302   -664    398   -165       N  
+ATOM   1903  CA  ARG B  80      50.821  -7.643  63.902  1.00 25.77           C  
+ANISOU 1903  CA  ARG B  80     2599   2989   4204   -791    496    -59       C  
+ATOM   1904  C   ARG B  80      50.570  -8.089  62.465  1.00 25.17           C  
+ANISOU 1904  C   ARG B  80     2579   2996   3987   -787    670     24       C  
+ATOM   1905  O   ARG B  80      49.846  -7.420  61.713  1.00 19.39           O  
+ANISOU 1905  O   ARG B  80     1985   2221   3162   -818    704    123       O  
+ATOM   1906  CB  ARG B  80      52.232  -7.071  64.022  1.00 26.91           C  
+ANISOU 1906  CB  ARG B  80     2558   3109   4558   -923    513    -54       C  
+ATOM   1907  CG  ARG B  80      52.512  -5.956  63.034  1.00 27.50           C  
+ANISOU 1907  CG  ARG B  80     2653   3119   4676  -1065    626     81       C  
+ATOM   1908  CD  ARG B  80      53.973  -5.558  63.013  1.00 32.47           C  
+ANISOU 1908  CD  ARG B  80     3113   3778   5446  -1158    637    104       C  
+ATOM   1909  NE  ARG B  80      54.186  -4.415  62.128  1.00 30.85           N  
+ANISOU 1909  NE  ARG B  80     2960   3510   5250  -1287    721    246       N  
+ATOM   1910  CZ  ARG B  80      55.349  -3.794  61.978  1.00 38.16           C  
+ANISOU 1910  CZ  ARG B  80     3761   4438   6302  -1406    745    294       C  
+ATOM   1911  NH1 ARG B  80      56.406  -4.201  62.662  1.00 37.78           N1+
+ANISOU 1911  NH1 ARG B  80     3518   4451   6384  -1407    680    211       N1+
+ATOM   1912  NH2 ARG B  80      55.449  -2.763  61.150  1.00 39.94           N  
+ANISOU 1912  NH2 ARG B  80     4052   4599   6524  -1526    827    432       N  
+ATOM   1913  N   TRP B  81      51.157  -9.221  62.077  1.00 21.53           N  
+ANISOU 1913  N   TRP B  81     2024   2652   3503   -738    774    -19       N  
+ATOM   1914  CA  TRP B  81      51.091  -9.598  60.677  1.00 24.06           C  
+ANISOU 1914  CA  TRP B  81     2408   3057   3679   -741    953     40       C  
+ATOM   1915  C   TRP B  81      49.766 -10.261  60.328  1.00 23.14           C  
+ANISOU 1915  C   TRP B  81     2470   2963   3359   -646    906     23       C  
+ATOM   1916  O   TRP B  81      49.334 -10.192  59.178  1.00 21.80           O  
+ANISOU 1916  O   TRP B  81     2422   2831   3029   -665    993     91       O  
+ATOM   1917  CB  TRP B  81      52.319 -10.450  60.306  1.00 23.03           C  
+ANISOU 1917  CB  TRP B  81     2104   3030   3615   -724   1109     -7       C  
+ATOM   1918  CG  TRP B  81      53.537  -9.587  60.466  1.00 26.64           C  
+ANISOU 1918  CG  TRP B  81     2403   3470   4250   -822   1116     49       C  
+ATOM   1919  CD1 TRP B  81      54.572  -9.768  61.337  1.00 32.66           C  
+ANISOU 1919  CD1 TRP B  81     2974   4241   5193   -811   1032     -9       C  
+ATOM   1920  CD2 TRP B  81      53.789  -8.336  59.802  1.00 31.16           C  
+ANISOU 1920  CD2 TRP B  81     3008   4000   4829   -952   1173    185       C  
+ATOM   1921  NE1 TRP B  81      55.470  -8.731  61.227  1.00 37.10           N  
+ANISOU 1921  NE1 TRP B  81     3441   4778   5876   -935   1039     71       N  
+ATOM   1922  CE2 TRP B  81      55.011  -7.841  60.293  1.00 34.34           C  
+ANISOU 1922  CE2 TRP B  81     3226   4393   5428  -1025   1131    191       C  
+ATOM   1923  CE3 TRP B  81      53.108  -7.603  58.822  1.00 31.38           C  
+ANISOU 1923  CE3 TRP B  81     3210   4001   4714  -1012   1246    311       C  
+ATOM   1924  CZ2 TRP B  81      55.566  -6.646  59.841  1.00 34.74           C  
+ANISOU 1924  CZ2 TRP B  81     3255   4400   5543  -1168   1171    312       C  
+ATOM   1925  CZ3 TRP B  81      53.661  -6.419  58.374  1.00 36.16           C  
+ANISOU 1925  CZ3 TRP B  81     3798   4560   5380  -1140   1284    443       C  
+ATOM   1926  CH2 TRP B  81      54.879  -5.951  58.884  1.00 36.20           C  
+ANISOU 1926  CH2 TRP B  81     3614   4550   5590  -1224   1252    439       C  
+ATOM   1927  N   VAL B  82      49.073 -10.832  61.318  1.00 19.48           N  
+ANISOU 1927  N   VAL B  82     2028   2473   2899   -554    761    -55       N  
+ATOM   1928  CA  VAL B  82      47.690 -11.249  61.095  1.00 15.62           C  
+ANISOU 1928  CA  VAL B  82     1689   1985   2260   -490    693    -51       C  
+ATOM   1929  C   VAL B  82      46.822 -10.029  60.766  1.00 21.13           C  
+ANISOU 1929  C   VAL B  82     2503   2614   2911   -536    643     57       C  
+ATOM   1930  O   VAL B  82      46.012 -10.052  59.818  1.00 18.29           O  
+ANISOU 1930  O   VAL B  82     2262   2281   2405   -532    650    117       O  
+ATOM   1931  CB  VAL B  82      47.096 -11.998  62.321  1.00 17.00           C  
+ANISOU 1931  CB  VAL B  82     1852   2138   2469   -394    564   -130       C  
+ATOM   1932  CG1 VAL B  82      45.599 -12.251  62.136  1.00 18.65           C  
+ANISOU 1932  CG1 VAL B  82     2184   2339   2565   -349    492   -106       C  
+ATOM   1933  CG2 VAL B  82      47.833 -13.328  62.526  1.00 19.50           C  
+ANISOU 1933  CG2 VAL B  82     2078   2507   2824   -330    605   -220       C  
+ATOM   1934  N   ARG B  83      46.987  -8.968  61.552  1.00 18.41           N  
+ANISOU 1934  N   ARG B  83     2129   2172   2692   -574    576     78       N  
+ATOM   1935  CA  ARG B  83      46.219  -7.752  61.322  1.00 19.34           C  
+ANISOU 1935  CA  ARG B  83     2355   2193   2801   -602    527    179       C  
+ATOM   1936  C   ARG B  83      46.499  -7.217  59.931  1.00 17.80           C  
+ANISOU 1936  C   ARG B  83     2221   2015   2527   -689    641    309       C  
+ATOM   1937  O   ARG B  83      45.579  -6.807  59.224  1.00 20.04           O  
+ANISOU 1937  O   ARG B  83     2630   2281   2703   -676    611    408       O  
+ATOM   1938  CB  ARG B  83      46.537  -6.699  62.385  1.00 18.88           C  
+ANISOU 1938  CB  ARG B  83     2264   2005   2905   -635    446    155       C  
+ATOM   1939  CG  ARG B  83      46.130  -7.162  63.805  1.00 17.78           C  
+ANISOU 1939  CG  ARG B  83     2105   1857   2795   -534    332     34       C  
+ATOM   1940  CD  ARG B  83      46.361  -6.068  64.865  1.00 19.71           C  
+ANISOU 1940  CD  ARG B  83     2357   1967   3165   -558    238    -15       C  
+ATOM   1941  NE  ARG B  83      45.757  -6.483  66.141  1.00 19.03           N  
+ANISOU 1941  NE  ARG B  83     2295   1887   3047   -443    145   -117       N  
+ATOM   1942  CZ  ARG B  83      45.565  -5.684  67.187  1.00 16.36           C  
+ANISOU 1942  CZ  ARG B  83     2015   1444   2758   -414     56   -186       C  
+ATOM   1943  NH1 ARG B  83      45.912  -4.398  67.128  1.00 17.45           N1+
+ANISOU 1943  NH1 ARG B  83     2190   1436   3004   -496     27   -174       N1+
+ATOM   1944  NH2 ARG B  83      44.998  -6.168  68.297  1.00 19.93           N  
+ANISOU 1944  NH2 ARG B  83     2500   1928   3143   -301      1   -269       N  
+ATOM   1945  N   TYR B  84      47.767  -7.246  59.528  1.00 19.03           N  
+ANISOU 1945  N   TYR B  84     2282   2214   2734   -774    777    320       N  
+ATOM   1946  CA  TYR B  84      48.131  -6.785  58.199  1.00 20.86           C  
+ANISOU 1946  CA  TYR B  84     2573   2479   2872   -861    924    455       C  
+ATOM   1947  C   TYR B  84      47.491  -7.641  57.103  1.00 23.31           C  
+ANISOU 1947  C   TYR B  84     3010   2911   2935   -801    972    464       C  
+ATOM   1948  O   TYR B  84      46.986  -7.116  56.106  1.00 22.92           O  
+ANISOU 1948  O   TYR B  84     3105   2866   2737   -830    991    596       O  
+ATOM   1949  CB  TYR B  84      49.652  -6.769  58.018  1.00 22.84           C  
+ANISOU 1949  CB  TYR B  84     2663   2773   3241   -957   1091    459       C  
+ATOM   1950  CG  TYR B  84      50.024  -6.366  56.614  1.00 27.34           C  
+ANISOU 1950  CG  TYR B  84     3303   3399   3686  -1039   1276    610       C  
+ATOM   1951  CD1 TYR B  84      50.001  -5.030  56.225  1.00 26.89           C  
+ANISOU 1951  CD1 TYR B  84     3313   3241   3663  -1129   1258    777       C  
+ATOM   1952  CD2 TYR B  84      50.370  -7.328  55.657  1.00 25.40           C  
+ANISOU 1952  CD2 TYR B  84     3071   3315   3264   -985   1417    579       C  
+ATOM   1953  CE1 TYR B  84      50.317  -4.663  54.935  1.00 29.14           C  
+ANISOU 1953  CE1 TYR B  84     3666   3601   3806  -1174   1380    927       C  
+ATOM   1954  CE2 TYR B  84      50.686  -6.964  54.366  1.00 28.79           C  
+ANISOU 1954  CE2 TYR B  84     3576   3821   3541  -1020   1543    711       C  
+ATOM   1955  CZ  TYR B  84      50.661  -5.635  54.014  1.00 30.88           C  
+ANISOU 1955  CZ  TYR B  84     3895   3999   3837  -1118   1526    893       C  
+ATOM   1956  OH  TYR B  84      50.975  -5.272  52.731  1.00 32.86           O  
+ANISOU 1956  OH  TYR B  84     4221   4336   3929  -1154   1652   1039       O  
+ATOM   1957  N   GLU B  85      47.521  -8.955  57.298  1.00 23.49           N  
+ANISOU 1957  N   GLU B  85     2988   3023   2914   -720    976    325       N  
+ATOM   1958  CA  GLU B  85      46.960  -9.881  56.334  1.00 21.66           C  
+ANISOU 1958  CA  GLU B  85     2879   2892   2460   -668   1002    293       C  
+ATOM   1959  C   GLU B  85      45.463  -9.626  56.154  1.00 24.56           C  
+ANISOU 1959  C   GLU B  85     3387   3224   2720   -632    831    351       C  
+ATOM   1960  O   GLU B  85      44.938  -9.670  55.038  1.00 25.12           O  
+ANISOU 1960  O   GLU B  85     3604   3354   2586   -638    831    413       O  
+ATOM   1961  CB  GLU B  85      47.257 -11.323  56.782  1.00 23.13           C  
+ANISOU 1961  CB  GLU B  85     2982   3132   2673   -585   1015    122       C  
+ATOM   1962  CG  GLU B  85      48.715 -11.677  56.483  1.00 25.99           C  
+ANISOU 1962  CG  GLU B  85     3222   3561   3091   -604   1218     80       C  
+ATOM   1963  CD  GLU B  85      49.288 -12.859  57.260  1.00 32.29           C  
+ANISOU 1963  CD  GLU B  85     3882   4372   4014   -516   1220    -70       C  
+ATOM   1964  OE1 GLU B  85      48.552 -13.526  58.016  1.00 27.46           O  
+ANISOU 1964  OE1 GLU B  85     3289   3719   3426   -445   1070   -143       O  
+ATOM   1965  OE2 GLU B  85      50.512 -13.108  57.105  1.00 33.15           O1-
+ANISOU 1965  OE2 GLU B  85     3854   4533   4210   -517   1380   -101       O1-
+ATOM   1966  N   ILE B  86      44.782  -9.325  57.249  1.00 22.09           N  
+ANISOU 1966  N   ILE B  86     3029   2822   2544   -590    684    334       N  
+ATOM   1967  CA  ILE B  86      43.350  -9.049  57.189  1.00 20.91           C  
+ANISOU 1967  CA  ILE B  86     2967   2637   2339   -542    527    393       C  
+ATOM   1968  C   ILE B  86      43.091  -7.721  56.467  1.00 21.96           C  
+ANISOU 1968  C   ILE B  86     3203   2711   2430   -589    516    571       C  
+ATOM   1969  O   ILE B  86      42.276  -7.657  55.536  1.00 20.90           O  
+ANISOU 1969  O   ILE B  86     3189   2615   2136   -577    448    657       O  
+ATOM   1970  CB  ILE B  86      42.737  -9.014  58.590  1.00 17.30           C  
+ANISOU 1970  CB  ILE B  86     2428   2104   2043   -473    413    333       C  
+ATOM   1971  CG1 ILE B  86      42.780 -10.412  59.224  1.00 20.14           C  
+ANISOU 1971  CG1 ILE B  86     2715   2519   2420   -421    406    190       C  
+ATOM   1972  CG2 ILE B  86      41.299  -8.489  58.548  1.00 18.06           C  
+ANISOU 1972  CG2 ILE B  86     2583   2154   2126   -419    274    415       C  
+ATOM   1973  CD1 ILE B  86      42.431 -10.426  60.690  1.00 18.09           C  
+ANISOU 1973  CD1 ILE B  86     2376   2199   2298   -358    332    134       C  
+HETATM 1974  N   MSE B  87      43.809  -6.677  56.875  1.00 20.76           N  
+ANISOU 1974  N   MSE B  87     3007   2458   2423   -648    570    630       N  
+HETATM 1975  CA  MSE B  87      43.626  -5.354  56.273  1.00 24.14           C  
+ANISOU 1975  CA  MSE B  87     3535   2790   2846   -698    562    814       C  
+HETATM 1976  C   MSE B  87      43.965  -5.344  54.780  1.00 24.03           C  
+ANISOU 1976  C   MSE B  87     3642   2871   2617   -764    676    939       C  
+HETATM 1977  O   MSE B  87      43.221  -4.773  53.978  1.00 28.41           O  
+ANISOU 1977  O   MSE B  87     4336   3409   3048   -754    605   1090       O  
+HETATM 1978  CB  MSE B  87      44.469  -4.296  57.001  1.00 22.79           C  
+ANISOU 1978  CB  MSE B  87     3293   2472   2895   -773    604    837       C  
+HETATM 1979  CG  MSE B  87      44.042  -3.985  58.431  1.00 21.52           C  
+ANISOU 1979  CG  MSE B  87     3067   2192   2917   -704    479    733       C  
+HETATM 1980 SE   MSE B  87      42.111  -3.521  58.588  1.00 27.80          SE  
+ANISOU 1980 SE   MSE B  87     3960   2909   3693   -553    293    794      SE  
+HETATM 1981  CE  MSE B  87      42.245  -1.975  59.775  1.00 20.62           C  
+ANISOU 1981  CE  MSE B  87     3053   1740   3043   -550    240    781       C  
+ATOM   1982  N   LYS B  88      45.088  -5.955  54.404  1.00 23.76           N  
+ANISOU 1982  N   LYS B  88     3558   2939   2530   -820    855    883       N  
+ATOM   1983  CA  LYS B  88      45.493  -5.997  52.999  1.00 30.29           C  
+ANISOU 1983  CA  LYS B  88     4509   3875   3124   -876   1004    990       C  
+ATOM   1984  C   LYS B  88      44.498  -6.815  52.165  1.00 31.02           C  
+ANISOU 1984  C   LYS B  88     4754   4084   2948   -803    905    959       C  
+ATOM   1985  O   LYS B  88      44.231  -6.491  51.013  1.00 30.52           O  
+ANISOU 1985  O   LYS B  88     4864   4076   2656   -825    919   1097       O  
+ATOM   1986  CB  LYS B  88      46.900  -6.576  52.869  1.00 28.96           C  
+ANISOU 1986  CB  LYS B  88     4224   3799   2979   -928   1236    910       C  
+ATOM   1987  CG  LYS B  88      47.530  -6.391  51.493  1.00 29.45           C  
+ANISOU 1987  CG  LYS B  88     4351   3974   2866   -949   1390   1022       C  
+ATOM   1988  CD  LYS B  88      47.683  -4.918  51.141  1.00 36.09           C  
+ANISOU 1988  CD  LYS B  88     5215   4718   3781  -1024   1391   1248       C  
+ATOM   1989  CE  LYS B  88      48.470  -4.764  49.847  1.00 40.82           C  
+ANISOU 1989  CE  LYS B  88     5840   5448   4222  -1052   1567   1364       C  
+ATOM   1990  NZ  LYS B  88      48.968  -3.372  49.628  1.00 36.48           N1+
+ANISOU 1990  NZ  LYS B  88     5253   4807   3802  -1159   1603   1582       N1+
+ATOM   1991  N   SER B  89      43.940  -7.867  52.760  1.00 28.51           N  
+ANISOU 1991  N   SER B  89     4378   3797   2659   -722    793    784       N  
+ATOM   1992  CA  SER B  89      42.950  -8.701  52.074  1.00 30.63           C  
+ANISOU 1992  CA  SER B  89     4770   4155   2712   -668    666    732       C  
+ATOM   1993  C   SER B  89      41.728  -7.890  51.633  1.00 32.56           C  
+ANISOU 1993  C   SER B  89     5130   4359   2883   -648    471    895       C  
+ATOM   1994  O   SER B  89      41.158  -8.143  50.569  1.00 36.47           O  
+ANISOU 1994  O   SER B  89     5783   4944   3130   -643    393    937       O  
+ATOM   1995  CB  SER B  89      42.510  -9.865  52.974  1.00 30.15           C  
+ANISOU 1995  CB  SER B  89     4600   4093   2761   -599    568    539       C  
+ATOM   1996  OG  SER B  89      43.553 -10.810  53.140  1.00 28.24           O  
+ANISOU 1996  OG  SER B  89     4285   3904   2542   -597    728    389       O  
+ATOM   1997  N   ILE B  90      41.332  -6.915  52.448  1.00 28.27           N  
+ANISOU 1997  N   ILE B  90     4510   3678   2555   -629    385    980       N  
+ATOM   1998  CA  ILE B  90      40.240  -6.007  52.089  1.00 33.82           C  
+ANISOU 1998  CA  ILE B  90     5299   4316   3234   -591    211   1153       C  
+ATOM   1999  C   ILE B  90      40.571  -5.205  50.832  1.00 39.37           C  
+ANISOU 1999  C   ILE B  90     6182   5039   3736   -654    277   1361       C  
+ATOM   2000  O   ILE B  90      39.775  -5.133  49.888  1.00 33.58           O  
+ANISOU 2000  O   ILE B  90     5595   4366   2797   -629    141   1470       O  
+ATOM   2001  CB  ILE B  90      39.925  -5.006  53.213  1.00 34.95           C  
+ANISOU 2001  CB  ILE B  90     5337   4283   3659   -549    149   1197       C  
+ATOM   2002  CG1 ILE B  90      39.535  -5.728  54.503  1.00 39.63           C  
+ANISOU 2002  CG1 ILE B  90     5769   4862   4427   -480     93   1013       C  
+ATOM   2003  CG2 ILE B  90      38.824  -4.054  52.785  1.00 29.21           C  
+ANISOU 2003  CG2 ILE B  90     4694   3478   2926   -489    -22   1384       C  
+ATOM   2004  CD1 ILE B  90      39.220  -4.772  55.646  1.00 40.43           C  
+ANISOU 2004  CD1 ILE B  90     5788   4798   4775   -423     47   1029       C  
+ATOM   2005  N   GLU B  91      41.744  -4.581  50.857  1.00 36.38           N  
+ANISOU 2005  N   GLU B  91     5788   4608   3427   -739    478   1427       N  
+ATOM   2006  CA  GLU B  91      42.269  -3.836  49.726  1.00 38.56           C  
+ANISOU 2006  CA  GLU B  91     6164   4906   3580   -771    592   1596       C  
+ATOM   2007  C   GLU B  91      42.271  -4.684  48.452  1.00 36.84           C  
+ANISOU 2007  C   GLU B  91     6071   4888   3039   -746    629   1558       C  
+ATOM   2008  O   GLU B  91      41.790  -4.253  47.399  1.00 36.15           O  
+ANISOU 2008  O   GLU B  91     6118   4844   2773   -707    559   1696       O  
+ATOM   2009  CB  GLU B  91      43.686  -3.355  50.052  1.00 34.05           C  
+ANISOU 2009  CB  GLU B  91     5471   4280   3186   -861    820   1609       C  
+ATOM   2010  CG  GLU B  91      44.428  -2.703  48.902  1.00 39.64           C  
+ANISOU 2010  CG  GLU B  91     6232   5036   3792   -898    977   1780       C  
+ATOM   2011  CD  GLU B  91      45.848  -2.334  49.282  1.00 45.00           C  
+ANISOU 2011  CD  GLU B  91     6739   5680   4679  -1002   1176   1788       C  
+ATOM   2012  OE1 GLU B  91      46.032  -1.667  50.321  1.00 45.35           O  
+ANISOU 2012  OE1 GLU B  91     6674   5552   5005  -1049   1136   1784       O  
+ATOM   2013  OE2 GLU B  91      46.783  -2.721  48.551  1.00 54.31           O1-
+ANISOU 2013  OE2 GLU B  91     7883   7009   5744  -1038   1358   1790       O1-
+ATOM   2014  N   LYS B  92      42.792  -5.902  48.564  1.00 37.40           N  
+ANISOU 2014  N   LYS B  92     6101   5072   3039   -757    730   1360       N  
+ATOM   2015  CA  LYS B  92      43.014  -6.751  47.391  1.00 40.54           C  
+ANISOU 2015  CA  LYS B  92     6611   5645   3149   -729    802   1285       C  
+ATOM   2016  C   LYS B  92      41.749  -7.495  46.963  1.00 36.55           C  
+ANISOU 2016  C   LYS B  92     6229   5207   2450   -670    560   1206       C  
+ATOM   2017  O   LYS B  92      41.755  -8.234  45.979  1.00 37.02           O  
+ANISOU 2017  O   LYS B  92     6404   5401   2263   -640    572   1122       O  
+ATOM   2018  CB  LYS B  92      44.157  -7.732  47.668  1.00 41.37           C  
+ANISOU 2018  CB  LYS B  92     6606   5821   3291   -743   1018   1094       C  
+ATOM   2019  CG  LYS B  92      45.497  -7.023  47.906  1.00 43.97           C  
+ANISOU 2019  CG  LYS B  92     6783   6112   3809   -806   1247   1177       C  
+ATOM   2020  CD  LYS B  92      46.650  -7.990  48.153  1.00 46.35           C  
+ANISOU 2020  CD  LYS B  92     6943   6492   4177   -797   1444    996       C  
+ATOM   2021  CE  LYS B  92      47.116  -8.645  46.867  1.00 48.95           C  
+ANISOU 2021  CE  LYS B  92     7368   6990   4240   -749   1582    951       C  
+ATOM   2022  NZ  LYS B  92      47.476  -7.630  45.829  1.00 53.43           N1+
+ANISOU 2022  NZ  LYS B  92     8002   7611   4686   -790   1680   1178       N1+
+ATOM   2023  N   GLY B  93      40.664  -7.286  47.699  1.00 37.90           N  
+ANISOU 2023  N   GLY B  93     6363   5285   2752   -651    332   1233       N  
+ATOM   2024  CA  GLY B  93      39.361  -7.779  47.290  1.00 36.67           C  
+ANISOU 2024  CA  GLY B  93     6283   5182   2468   -600     63   1200       C  
+ATOM   2025  C   GLY B  93      39.039  -9.214  47.670  1.00 33.03           C  
+ANISOU 2025  C   GLY B  93     5795   4776   1978   -602    -14    966       C  
+ATOM   2026  O   GLY B  93      38.098  -9.801  47.136  1.00 39.49           O  
+ANISOU 2026  O   GLY B  93     6675   5655   2674   -575   -224    905       O  
+ATOM   2027  N   ASN B  94      39.811  -9.781  48.588  1.00 29.52           N  
+ANISOU 2027  N   ASN B  94     5215   4298   1704   -616    146    819       N  
+ATOM   2028  CA  ASN B  94      39.541 -11.140  49.055  1.00 28.17           C  
+ANISOU 2028  CA  ASN B  94     4965   4143   1594   -589     84    586       C  
+ATOM   2029  C   ASN B  94      38.276 -11.226  49.887  1.00 33.88           C  
+ANISOU 2029  C   ASN B  94     5550   4793   2530   -549   -158    580       C  
+ATOM   2030  O   ASN B  94      37.949 -10.309  50.647  1.00 31.11           O  
+ANISOU 2030  O   ASN B  94     5083   4349   2390   -521   -199    698       O  
+ATOM   2031  CB  ASN B  94      40.711 -11.678  49.885  1.00 26.57           C  
+ANISOU 2031  CB  ASN B  94     4620   3909   1565   -586    310    446       C  
+ATOM   2032  CG  ASN B  94      41.785 -12.313  49.030  1.00 30.28           C  
+ANISOU 2032  CG  ASN B  94     5204   4481   1820   -601    533    346       C  
+ATOM   2033  OD1 ASN B  94      41.859 -12.059  47.831  1.00 31.56           O  
+ANISOU 2033  OD1 ASN B  94     5540   4730   1720   -611    567    417       O  
+ATOM   2034  ND2 ASN B  94      42.620 -13.152  49.644  1.00 30.26           N  
+ANISOU 2034  ND2 ASN B  94     5081   4463   1954   -574    681    181       N  
+ATOM   2035  N   LYS B  95      37.566 -12.337  49.734  1.00 26.78           N  
+ANISOU 2035  N   LYS B  95     4663   3930   1582   -548   -308    437       N  
+ATOM   2036  CA  LYS B  95      36.577 -12.741  50.727  1.00 25.17           C  
+ANISOU 2036  CA  LYS B  95     4277   3657   1628   -521   -470    389       C  
+ATOM   2037  C   LYS B  95      37.322 -13.105  52.009  1.00 24.47           C  
+ANISOU 2037  C   LYS B  95     4025   3494   1777   -499   -298    290       C  
+ATOM   2038  O   LYS B  95      38.373 -13.743  51.958  1.00 29.22           O  
+ANISOU 2038  O   LYS B  95     4658   4115   2329   -509   -124    170       O  
+ATOM   2039  CB  LYS B  95      35.755 -13.919  50.195  1.00 31.93           C  
+ANISOU 2039  CB  LYS B  95     5189   4559   2383   -552   -662    255       C  
+ATOM   2040  CG  LYS B  95      34.878 -14.641  51.203  1.00 30.60           C  
+ANISOU 2040  CG  LYS B  95     4826   4323   2479   -547   -784    181       C  
+ATOM   2041  CD  LYS B  95      34.100 -15.744  50.480  1.00 38.26           C  
+ANISOU 2041  CD  LYS B  95     5871   5327   3337   -605   -993     56       C  
+ATOM   2042  CE  LYS B  95      33.187 -16.520  51.409  1.00 37.46           C  
+ANISOU 2042  CE  LYS B  95     5570   5155   3509   -624  -1111     -1       C  
+ATOM   2043  NZ  LYS B  95      32.311 -17.422  50.610  1.00 40.90           N1+
+ANISOU 2043  NZ  LYS B  95     6073   5614   3853   -703  -1361   -100       N1+
+ATOM   2044  N   ILE B  96      36.800 -12.680  53.156  1.00 21.21           N  
+ANISOU 2044  N   ILE B  96     3442   3002   1614   -458   -343    343       N  
+ATOM   2045  CA  ILE B  96      37.475 -12.920  54.424  1.00 19.31           C  
+ANISOU 2045  CA  ILE B  96     3064   2697   1576   -432   -203    266       C  
+ATOM   2046  C   ILE B  96      36.558 -13.637  55.397  1.00 25.36           C  
+ANISOU 2046  C   ILE B  96     3688   3422   2525   -404   -305    208       C  
+ATOM   2047  O   ILE B  96      35.425 -13.205  55.622  1.00 23.43           O  
+ANISOU 2047  O   ILE B  96     3370   3161   2370   -378   -443    297       O  
+ATOM   2048  CB  ILE B  96      37.960 -11.607  55.080  1.00 20.13           C  
+ANISOU 2048  CB  ILE B  96     3111   2732   1804   -408   -112    378       C  
+ATOM   2049  CG1 ILE B  96      38.791 -10.777  54.091  1.00 23.96           C  
+ANISOU 2049  CG1 ILE B  96     3727   3245   2130   -453     -8    477       C  
+ATOM   2050  CG2 ILE B  96      38.770 -11.917  56.342  1.00 22.92           C  
+ANISOU 2050  CG2 ILE B  96     3343   3036   2331   -387     13    282       C  
+ATOM   2051  CD1 ILE B  96      39.055  -9.358  54.557  1.00 23.23           C  
+ANISOU 2051  CD1 ILE B  96     3602   3057   2168   -447     36    611       C  
+ATOM   2052  N   ILE B  97      37.040 -14.734  55.977  1.00 23.69           N  
+ANISOU 2052  N   ILE B  97     3431   3192   2379   -406   -230     73       N  
+ATOM   2053  CA  ILE B  97      36.293 -15.409  57.038  1.00 18.93           C  
+ANISOU 2053  CA  ILE B  97     2692   2541   1960   -385   -288     41       C  
+ATOM   2054  C   ILE B  97      37.236 -15.759  58.186  1.00 19.32           C  
+ANISOU 2054  C   ILE B  97     2670   2544   2127   -349   -142    -24       C  
+ATOM   2055  O   ILE B  97      38.451 -15.813  57.995  1.00 20.86           O  
+ANISOU 2055  O   ILE B  97     2912   2750   2265   -349    -16    -78       O  
+ATOM   2056  CB  ILE B  97      35.593 -16.698  56.535  1.00 18.85           C  
+ANISOU 2056  CB  ILE B  97     2708   2536   1920   -438   -412    -52       C  
+ATOM   2057  CG1 ILE B  97      36.621 -17.690  55.977  1.00 18.81           C  
+ANISOU 2057  CG1 ILE B  97     2820   2531   1795   -459   -317   -204       C  
+ATOM   2058  CG2 ILE B  97      34.541 -16.372  55.481  1.00 21.08           C  
+ANISOU 2058  CG2 ILE B  97     3044   2870   2097   -477   -607     13       C  
+ATOM   2059  CD1 ILE B  97      36.079 -19.105  55.852  1.00 25.75           C  
+ANISOU 2059  CD1 ILE B  97     3713   3362   2709   -506   -416   -325       C  
+ATOM   2060  N   GLY B  98      36.674 -15.975  59.371  1.00 16.89           N  
+ANISOU 2060  N   GLY B  98     2244   2194   1981   -314   -158     -8       N  
+ATOM   2061  CA  GLY B  98      37.431 -16.470  60.507  1.00 18.10           C  
+ANISOU 2061  CA  GLY B  98     2341   2308   2230   -276    -55    -62       C  
+ATOM   2062  C   GLY B  98      36.972 -17.865  60.908  1.00 18.12           C  
+ANISOU 2062  C   GLY B  98     2306   2272   2307   -290    -89   -118       C  
+ATOM   2063  O   GLY B  98      35.810 -18.214  60.725  1.00 21.53           O  
+ANISOU 2063  O   GLY B  98     2700   2699   2779   -326   -195    -88       O  
+ATOM   2064  N   ILE B  99      37.889 -18.660  61.455  1.00 15.22           N  
+ANISOU 2064  N   ILE B  99     1938   1868   1977   -265     -8   -190       N  
+ATOM   2065  CA  ILE B  99      37.573 -20.017  61.923  1.00 12.51           C  
+ANISOU 2065  CA  ILE B  99     1572   1459   1723   -275    -29   -230       C  
+ATOM   2066  C   ILE B  99      38.300 -20.246  63.243  1.00 19.25           C  
+ANISOU 2066  C   ILE B  99     2375   2280   2660   -206     53   -218       C  
+ATOM   2067  O   ILE B  99      39.514 -20.282  63.247  1.00 16.01           O  
+ANISOU 2067  O   ILE B  99     1985   1872   2227   -168    121   -274       O  
+ATOM   2068  CB  ILE B  99      38.013 -21.102  60.904  1.00 20.60           C  
+ANISOU 2068  CB  ILE B  99     2696   2447   2686   -310    -38   -356       C  
+ATOM   2069  CG1 ILE B  99      37.316 -20.915  59.552  1.00 21.92           C  
+ANISOU 2069  CG1 ILE B  99     2943   2656   2728   -380   -143   -379       C  
+ATOM   2070  CG2 ILE B  99      37.730 -22.512  61.452  1.00 20.06           C  
+ANISOU 2070  CG2 ILE B  99     2610   2271   2740   -322    -63   -391       C  
+ATOM   2071  CD1 ILE B  99      37.739 -21.950  58.516  1.00 22.48           C  
+ANISOU 2071  CD1 ILE B  99     3146   2693   2704   -408   -148   -531       C  
+ATOM   2072  N   HIS B 100      37.576 -20.360  64.356  1.00 16.62           N  
+ANISOU 2072  N   HIS B 100     1973   1927   2415   -186     46   -139       N  
+ATOM   2073  CA  HIS B 100      38.202 -20.691  65.639  1.00 18.76           C  
+ANISOU 2073  CA  HIS B 100     2223   2172   2735   -119    105   -119       C  
+ATOM   2074  C   HIS B 100      38.783 -22.092  65.564  1.00 18.62           C  
+ANISOU 2074  C   HIS B 100     2239   2072   2764   -116    111   -179       C  
+ATOM   2075  O   HIS B 100      38.132 -23.000  65.042  1.00 19.08           O  
+ANISOU 2075  O   HIS B 100     2317   2067   2867   -177     65   -199       O  
+ATOM   2076  CB  HIS B 100      37.191 -20.591  66.786  1.00 14.46           C  
+ANISOU 2076  CB  HIS B 100     1616   1632   2246    -98    117    -13       C  
+ATOM   2077  CG  HIS B 100      36.804 -19.183  67.121  1.00 17.29           C  
+ANISOU 2077  CG  HIS B 100     1947   2053   2569    -60    133     31       C  
+ATOM   2078  ND1 HIS B 100      37.613 -18.358  67.871  1.00 17.32           N  
+ANISOU 2078  ND1 HIS B 100     1975   2080   2526      6    170     15       N  
+ATOM   2079  CD2 HIS B 100      35.700 -18.460  66.816  1.00 16.13           C  
+ANISOU 2079  CD2 HIS B 100     1750   1937   2441    -72    108     85       C  
+ATOM   2080  CE1 HIS B 100      37.020 -17.180  68.016  1.00 16.25           C  
+ANISOU 2080  CE1 HIS B 100     1824   1972   2379     33    176     48       C  
+ATOM   2081  NE2 HIS B 100      35.859 -17.216  67.382  1.00 18.06           N  
+ANISOU 2081  NE2 HIS B 100     2001   2208   2651     -4    144     97       N  
+ATOM   2082  N   ILE B 101      39.988 -22.285  66.100  1.00 17.01           N  
+ANISOU 2082  N   ILE B 101     2038   1857   2568    -46    154   -208       N  
+ATOM   2083  CA  ILE B 101      40.660 -23.584  66.013  1.00 17.49           C  
+ANISOU 2083  CA  ILE B 101     2128   1826   2692    -15    164   -267       C  
+ATOM   2084  C   ILE B 101      41.090 -24.075  67.392  1.00 18.04           C  
+ANISOU 2084  C   ILE B 101     2176   1857   2822     63    169   -195       C  
+ATOM   2085  O   ILE B 101      42.071 -24.817  67.525  1.00 17.78           O  
+ANISOU 2085  O   ILE B 101     2147   1766   2842    130    178   -233       O  
+ATOM   2086  CB  ILE B 101      41.885 -23.505  65.068  1.00 14.38           C  
+ANISOU 2086  CB  ILE B 101     1752   1453   2259     13    213   -383       C  
+ATOM   2087  CG1 ILE B 101      42.845 -22.413  65.538  1.00 17.04           C  
+ANISOU 2087  CG1 ILE B 101     2027   1877   2572     57    247   -365       C  
+ATOM   2088  CG2 ILE B 101      41.401 -23.251  63.636  1.00 17.80           C  
+ANISOU 2088  CG2 ILE B 101     2247   1917   2599    -63    206   -450       C  
+ATOM   2089  CD1 ILE B 101      44.184 -22.375  64.838  1.00 22.48           C  
+ANISOU 2089  CD1 ILE B 101     2688   2593   3262     92    320   -454       C  
+ATOM   2090  N   ASN B 102      40.337 -23.683  68.423  1.00 17.82           N  
+ANISOU 2090  N   ASN B 102     2128   1861   2781     64    165    -85       N  
+ATOM   2091  CA  ASN B 102      40.712 -24.055  69.788  1.00 16.60           C  
+ANISOU 2091  CA  ASN B 102     1979   1690   2636    141    166     -2       C  
+ATOM   2092  C   ASN B 102      39.882 -25.199  70.383  1.00 18.44           C  
+ANISOU 2092  C   ASN B 102     2235   1828   2942    121    173    105       C  
+ATOM   2093  O   ASN B 102      40.193 -25.690  71.468  1.00 19.95           O  
+ANISOU 2093  O   ASN B 102     2454   1993   3133    187    173    193       O  
+ATOM   2094  CB  ASN B 102      40.633 -22.814  70.703  1.00 16.87           C  
+ANISOU 2094  CB  ASN B 102     2003   1830   2575    177    173     41       C  
+ATOM   2095  CG  ASN B 102      41.950 -22.035  70.739  1.00 17.55           C  
+ANISOU 2095  CG  ASN B 102     2071   1971   2626    224    144    -35       C  
+ATOM   2096  OD1 ASN B 102      42.901 -22.386  70.044  1.00 17.46           O  
+ANISOU 2096  OD1 ASN B 102     2033   1935   2665    233    139   -110       O  
+ATOM   2097  ND2 ASN B 102      42.009 -20.987  71.560  1.00 13.20           N  
+ANISOU 2097  ND2 ASN B 102     1529   1488   1997    252    130    -22       N  
+ATOM   2098  N   ALA B 103      38.848 -25.647  69.671  1.00 17.68           N  
+ANISOU 2098  N   ALA B 103     2129   1677   2911     24    169    107       N  
+ATOM   2099  CA  ALA B 103      37.891 -26.593  70.260  1.00 20.78           C  
+ANISOU 2099  CA  ALA B 103     2520   1982   3395    -26    185    231       C  
+ATOM   2100  C   ALA B 103      38.250 -28.075  70.074  1.00 19.29           C  
+ANISOU 2100  C   ALA B 103     2387   1615   3329    -33    156    219       C  
+ATOM   2101  O   ALA B 103      37.528 -28.958  70.551  1.00 22.02           O  
+ANISOU 2101  O   ALA B 103     2736   1856   3774    -87    168    334       O  
+ATOM   2102  CB  ALA B 103      36.493 -26.317  69.696  1.00 20.46           C  
+ANISOU 2102  CB  ALA B 103     2410   1965   3398   -140    178    254       C  
+ATOM   2103  N   PHE B 104      39.356 -28.352  69.384  1.00 19.30           N  
+ANISOU 2103  N   PHE B 104     2427   1571   3336     23    129     86       N  
+ATOM   2104  CA  PHE B 104      39.842 -29.713  69.235  1.00 22.87           C  
+ANISOU 2104  CA  PHE B 104     2939   1839   3910     51    108     57       C  
+ATOM   2105  C   PHE B 104      41.203 -29.815  69.917  1.00 20.37           C  
+ANISOU 2105  C   PHE B 104     2629   1527   3582    203    110     69       C  
+ATOM   2106  O   PHE B 104      41.781 -28.796  70.305  1.00 20.27           O  
+ANISOU 2106  O   PHE B 104     2572   1664   3464    261    116     68       O  
+ATOM   2107  CB  PHE B 104      39.924 -30.120  67.750  1.00 21.90           C  
+ANISOU 2107  CB  PHE B 104     2861   1640   3821      1     81   -128       C  
+ATOM   2108  CG  PHE B 104      40.748 -29.181  66.903  1.00 25.37           C  
+ANISOU 2108  CG  PHE B 104     3285   2214   4140     47    106   -267       C  
+ATOM   2109  CD1 PHE B 104      42.136 -29.315  66.833  1.00 28.25           C  
+ANISOU 2109  CD1 PHE B 104     3647   2574   4511    172    143   -343       C  
+ATOM   2110  CD2 PHE B 104      40.139 -28.176  66.169  1.00 20.62           C  
+ANISOU 2110  CD2 PHE B 104     2664   1739   3433    -35     96   -306       C  
+ATOM   2111  CE1 PHE B 104      42.894 -28.447  66.052  1.00 25.56           C  
+ANISOU 2111  CE1 PHE B 104     3278   2360   4075    199    189   -451       C  
+ATOM   2112  CE2 PHE B 104      40.894 -27.303  65.370  1.00 18.59           C  
+ANISOU 2112  CE2 PHE B 104     2403   1597   3063     -4    132   -408       C  
+ATOM   2113  CZ  PHE B 104      42.261 -27.431  65.320  1.00 18.73           C  
+ANISOU 2113  CZ  PHE B 104     2413   1615   3089    105    188   -478       C  
+ATOM   2114  N   LYS B 105      41.720 -31.030  70.083  1.00 21.20           N  
+ANISOU 2114  N   LYS B 105     2784   1460   3811    268     92     82       N  
+ATOM   2115  CA  LYS B 105      42.966 -31.178  70.839  1.00 23.58           C  
+ANISOU 2115  CA  LYS B 105     3072   1766   4122    423     70    121       C  
+ATOM   2116  C   LYS B 105      44.191 -30.710  70.045  1.00 21.48           C  
+ANISOU 2116  C   LYS B 105     2745   1572   3843    505     83    -47       C  
+ATOM   2117  O   LYS B 105      44.348 -31.067  68.880  1.00 21.26           O  
+ANISOU 2117  O   LYS B 105     2737   1478   3862    491    117   -199       O  
+ATOM   2118  CB  LYS B 105      43.164 -32.632  71.282  1.00 26.47           C  
+ANISOU 2118  CB  LYS B 105     3507   1909   4643    487     41    206       C  
+ATOM   2119  CG  LYS B 105      42.236 -33.066  72.412  1.00 25.17           C  
+ANISOU 2119  CG  LYS B 105     3394   1688   4483    433     41    431       C  
+ATOM   2120  CD  LYS B 105      42.470 -34.536  72.753  1.00 25.10           C  
+ANISOU 2120  CD  LYS B 105     3465   1447   4623    487      9    517       C  
+ATOM   2121  CE  LYS B 105      41.612 -35.002  73.917  1.00 32.09           C  
+ANISOU 2121  CE  LYS B 105     4409   2300   5484    427     26    758       C  
+ATOM   2122  NZ  LYS B 105      41.749 -36.489  74.121  1.00 39.83           N1+
+ANISOU 2122  NZ  LYS B 105     5483   3084   6567    445     -7    814       N1+
+ATOM   2123  N   ASP B 106      45.057 -29.922  70.682  1.00 20.45           N  
+ANISOU 2123  N   ASP B 106     2543   1580   3648    586     58    -20       N  
+ATOM   2124  CA  ASP B 106      46.370 -29.644  70.100  1.00 24.30           C  
+ANISOU 2124  CA  ASP B 106     2941   2120   4173    675     75   -146       C  
+ATOM   2125  C   ASP B 106      47.326 -30.834  70.292  1.00 25.69           C  
+ANISOU 2125  C   ASP B 106     3103   2148   4511    826     49   -144       C  
+ATOM   2126  O   ASP B 106      46.924 -31.917  70.750  1.00 24.56           O  
+ANISOU 2126  O   ASP B 106     3045   1836   4451    851     16    -52       O  
+ATOM   2127  CB  ASP B 106      46.973 -28.352  70.688  1.00 19.13           C  
+ANISOU 2127  CB  ASP B 106     2194   1652   3422    689     38   -124       C  
+ATOM   2128  CG  ASP B 106      47.032 -28.354  72.218  1.00 20.84           C  
+ANISOU 2128  CG  ASP B 106     2431   1894   3594    748    -62     33       C  
+ATOM   2129  OD1 ASP B 106      47.263 -29.417  72.830  1.00 20.38           O  
+ANISOU 2129  OD1 ASP B 106     2409   1717   3616    839   -112    125       O  
+ATOM   2130  OD2 ASP B 106      46.858 -27.268  72.809  1.00 21.81           O1-
+ANISOU 2130  OD2 ASP B 106     2546   2151   3590    709    -93     62       O1-
+ATOM   2131  N   LYS B 107      48.595 -30.643  69.943  1.00 21.77           N  
+ANISOU 2131  N   LYS B 107     2495   1716   4060    921     67   -232       N  
+ATOM   2132  CA  LYS B 107      49.534 -31.753  70.001  1.00 23.12           C  
+ANISOU 2132  CA  LYS B 107     2659   1804   4324   1045     53   -231       C  
+ATOM   2133  C   LYS B 107      49.898 -32.097  71.446  1.00 26.39           C  
+ANISOU 2133  C   LYS B 107     3065   2202   4761   1141    -74    -57       C  
+ATOM   2134  O   LYS B 107      50.486 -33.136  71.697  1.00 25.98           O  
+ANISOU 2134  O   LYS B 107     3031   2052   4789   1248   -105    -18       O  
+ATOM   2135  CB  LYS B 107      50.797 -31.461  69.175  1.00 27.02           C  
+ANISOU 2135  CB  LYS B 107     3027   2401   4840   1106    128   -357       C  
+ATOM   2136  CG  LYS B 107      51.766 -30.427  69.766  1.00 26.52           C  
+ANISOU 2136  CG  LYS B 107     2795   2510   4772   1136     74   -319       C  
+ATOM   2137  CD  LYS B 107      52.950 -30.234  68.795  1.00 29.00           C  
+ANISOU 2137  CD  LYS B 107     2980   2910   5129   1176    181   -432       C  
+ATOM   2138  CE  LYS B 107      54.099 -29.452  69.428  1.00 30.94           C  
+ANISOU 2138  CE  LYS B 107     3036   3299   5422   1210    109   -385       C  
+ATOM   2139  NZ  LYS B 107      55.192 -29.179  68.434  1.00 28.75           N1+
+ANISOU 2139  NZ  LYS B 107     2618   3109   5195   1228    237   -479       N1+
+ATOM   2140  N   TYR B 108      49.532 -31.244  72.398  1.00 24.40           N  
+ANISOU 2140  N   TYR B 108     2802   2043   4425   1109   -153     49       N  
+ATOM   2141  CA  TYR B 108      49.757 -31.566  73.810  1.00 28.71           C  
+ANISOU 2141  CA  TYR B 108     3381   2584   4943   1194   -283    227       C  
+ATOM   2142  C   TYR B 108      48.557 -32.303  74.418  1.00 30.35           C  
+ANISOU 2142  C   TYR B 108     3753   2657   5122   1147   -284    382       C  
+ATOM   2143  O   TYR B 108      48.599 -32.744  75.568  1.00 35.64           O  
+ANISOU 2143  O   TYR B 108     4493   3305   5743   1210   -371    551       O  
+ATOM   2144  CB  TYR B 108      50.053 -30.297  74.605  1.00 30.48           C  
+ANISOU 2144  CB  TYR B 108     3532   2985   5064   1192   -384    262       C  
+ATOM   2145  CG  TYR B 108      50.911 -29.312  73.848  1.00 31.45           C  
+ANISOU 2145  CG  TYR B 108     3491   3244   5214   1168   -352    105       C  
+ATOM   2146  CD1 TYR B 108      52.242 -29.603  73.563  1.00 29.63           C  
+ANISOU 2146  CD1 TYR B 108     3128   3046   5083   1249   -357     51       C  
+ATOM   2147  CD2 TYR B 108      50.390 -28.096  73.409  1.00 30.40           C  
+ANISOU 2147  CD2 TYR B 108     3351   3228   4970   1034   -292     27       C  
+ATOM   2148  CE1 TYR B 108      53.034 -28.711  72.870  1.00 30.35           C  
+ANISOU 2148  CE1 TYR B 108     3064   3260   5207   1208   -308    -66       C  
+ATOM   2149  CE2 TYR B 108      51.180 -27.192  72.711  1.00 27.77           C  
+ANISOU 2149  CE2 TYR B 108     2872   3003   4677   1002   -255    -94       C  
+ATOM   2150  CZ  TYR B 108      52.500 -27.515  72.440  1.00 31.21           C  
+ANISOU 2150  CZ  TYR B 108     3160   3454   5244   1087   -259   -136       C  
+ATOM   2151  OH  TYR B 108      53.299 -26.627  71.748  1.00 26.11           O  
+ANISOU 2151  OH  TYR B 108     2366   2920   4633   1033   -199   -232       O  
+ATOM   2152  N   GLY B 109      47.494 -32.440  73.634  1.00 28.41           N  
+ANISOU 2152  N   GLY B 109     3568   2326   4899   1026   -184    329       N  
+ATOM   2153  CA  GLY B 109      46.307 -33.161  74.058  1.00 30.67           C  
+ANISOU 2153  CA  GLY B 109     3984   2484   5186    946   -162    471       C  
+ATOM   2154  C   GLY B 109      45.291 -32.272  74.755  1.00 30.25           C  
+ANISOU 2154  C   GLY B 109     3965   2571   4957    839   -138    578       C  
+ATOM   2155  O   GLY B 109      44.371 -32.759  75.411  1.00 26.61           O  
+ANISOU 2155  O   GLY B 109     3593   2042   4475    784   -113    742       O  
+ATOM   2156  N   ASN B 110      45.451 -30.961  74.613  1.00 21.13           N  
+ANISOU 2156  N   ASN B 110     2740   1616   3673    807   -133    483       N  
+ATOM   2157  CA  ASN B 110      44.553 -30.018  75.287  1.00 23.88           C  
+ANISOU 2157  CA  ASN B 110     3123   2110   3840    727   -103    557       C  
+ATOM   2158  C   ASN B 110      43.544 -29.350  74.369  1.00 29.43           C  
+ANISOU 2158  C   ASN B 110     3800   2864   4519    586    -11    462       C  
+ATOM   2159  O   ASN B 110      43.827 -29.100  73.195  1.00 25.50           O  
+ANISOU 2159  O   ASN B 110     3245   2368   4077    554      8    303       O  
+ATOM   2160  CB  ASN B 110      45.367 -28.937  75.991  1.00 27.41           C  
+ANISOU 2160  CB  ASN B 110     3533   2734   4150    794   -184    534       C  
+ATOM   2161  CG  ASN B 110      46.303 -29.508  77.026  1.00 31.61           C  
+ANISOU 2161  CG  ASN B 110     4091   3242   4678    935   -311    646       C  
+ATOM   2162  OD1 ASN B 110      46.000 -30.523  77.667  1.00 33.97           O  
+ANISOU 2162  OD1 ASN B 110     4484   3427   4998    975   -320    811       O  
+ATOM   2163  ND2 ASN B 110      47.455 -28.871  77.193  1.00 36.09           N  
+ANISOU 2163  ND2 ASN B 110     4569   3911   5231   1006   -420    569       N  
+ATOM   2164  N   ILE B 111      42.370 -29.060  74.931  1.00 22.86           N  
+ANISOU 2164  N   ILE B 111     3008   2080   3598    512     47    570       N  
+ATOM   2165  CA  ILE B 111      41.354 -28.216  74.304  1.00 22.36           C  
+ANISOU 2165  CA  ILE B 111     2904   2098   3495    398    116    509       C  
+ATOM   2166  C   ILE B 111      41.353 -26.873  75.056  1.00 21.72           C  
+ANISOU 2166  C   ILE B 111     2823   2195   3236    429    121    512       C  
+ATOM   2167  O   ILE B 111      41.640 -26.836  76.260  1.00 19.67           O  
+ANISOU 2167  O   ILE B 111     2624   1982   2866    508     95    610       O  
+ATOM   2168  CB  ILE B 111      39.965 -28.911  74.340  1.00 24.34           C  
+ANISOU 2168  CB  ILE B 111     3170   2259   3818    291    188    627       C  
+ATOM   2169  CG1 ILE B 111      40.039 -30.244  73.580  1.00 28.44           C  
+ANISOU 2169  CG1 ILE B 111     3709   2571   4525    253    160    597       C  
+ATOM   2170  CG2 ILE B 111      38.880 -28.032  73.753  1.00 24.08           C  
+ANISOU 2170  CG2 ILE B 111     3070   2318   3760    188    241    580       C  
+ATOM   2171  CD1 ILE B 111      38.803 -31.121  73.734  1.00 30.70           C  
+ANISOU 2171  CD1 ILE B 111     4008   2731   4925    137    208    733       C  
+ATOM   2172  N   LYS B 112      41.091 -25.773  74.354  1.00 17.97           N  
+ANISOU 2172  N   LYS B 112     2294   1809   2726    376    143    401       N  
+ATOM   2173  CA  LYS B 112      41.147 -24.447  74.984  1.00 14.51           C  
+ANISOU 2173  CA  LYS B 112     1866   1509   2140    409    141    377       C  
+ATOM   2174  C   LYS B 112      39.872 -23.637  74.770  1.00 18.04           C  
+ANISOU 2174  C   LYS B 112     2288   2014   2553    343    227    383       C  
+ATOM   2175  O   LYS B 112      39.098 -23.892  73.847  1.00 18.31           O  
+ANISOU 2175  O   LYS B 112     2270   2004   2684    259    260    373       O  
+ATOM   2176  CB  LYS B 112      42.361 -23.661  74.459  1.00 19.54           C  
+ANISOU 2176  CB  LYS B 112     2454   2192   2779    431     68    235       C  
+ATOM   2177  CG  LYS B 112      43.681 -24.401  74.647  1.00 24.23           C  
+ANISOU 2177  CG  LYS B 112     3032   2741   3436    511    -18    225       C  
+ATOM   2178  CD  LYS B 112      44.907 -23.492  74.503  1.00 27.98           C  
+ANISOU 2178  CD  LYS B 112     3437   3289   3907    536    -93    113       C  
+ATOM   2179  CE  LYS B 112      45.014 -22.905  73.113  1.00 25.01           C  
+ANISOU 2179  CE  LYS B 112     2986   2921   3595    459    -37     -4       C  
+ATOM   2180  NZ  LYS B 112      46.371 -22.322  72.875  1.00 20.15           N1+
+ANISOU 2180  NZ  LYS B 112     2274   2352   3030    477    -91    -92       N1+
+ATOM   2181  N   SER B 113      39.659 -22.642  75.623  1.00 16.56           N  
+ANISOU 2181  N   SER B 113     2138   1924   2230    390    252    391       N  
+ATOM   2182  CA  SER B 113      38.603 -21.678  75.375  1.00 18.05           C  
+ANISOU 2182  CA  SER B 113     2290   2167   2400    357    327    374       C  
+ATOM   2183  C   SER B 113      38.948 -20.862  74.126  1.00 20.53           C  
+ANISOU 2183  C   SER B 113     2548   2483   2771    308    279    245       C  
+ATOM   2184  O   SER B 113      40.122 -20.690  73.800  1.00 16.03           O  
+ANISOU 2184  O   SER B 113     1978   1906   2207    318    204    159       O  
+ATOM   2185  CB  SER B 113      38.410 -20.760  76.591  1.00 18.56           C  
+ANISOU 2185  CB  SER B 113     2431   2322   2298    440    370    385       C  
+ATOM   2186  OG  SER B 113      39.662 -20.251  77.042  1.00 20.35           O  
+ANISOU 2186  OG  SER B 113     2721   2576   2436    495    261    297       O  
+ATOM   2187  N   LYS B 114      37.930 -20.372  73.425  1.00 17.90           N  
+ANISOU 2187  N   LYS B 114     2156   2160   2485    257    322    245       N  
+ATOM   2188  CA  LYS B 114      38.160 -19.525  72.252  1.00 19.67           C  
+ANISOU 2188  CA  LYS B 114     2347   2388   2739    213    279    149       C  
+ATOM   2189  C   LYS B 114      38.950 -18.257  72.562  1.00 20.67           C  
+ANISOU 2189  C   LYS B 114     2512   2551   2790    257    248     70       C  
+ATOM   2190  O   LYS B 114      38.709 -17.594  73.577  1.00 17.06           O  
+ANISOU 2190  O   LYS B 114     2102   2129   2252    322    276     77       O  
+ATOM   2191  CB  LYS B 114      36.829 -19.114  71.615  1.00 19.87           C  
+ANISOU 2191  CB  LYS B 114     2306   2426   2818    169    312    186       C  
+ATOM   2192  CG  LYS B 114      36.089 -20.226  70.928  1.00 23.81           C  
+ANISOU 2192  CG  LYS B 114     2749   2877   3420     87    302    234       C  
+ATOM   2193  CD  LYS B 114      34.786 -19.727  70.329  1.00 22.06           C  
+ANISOU 2193  CD  LYS B 114     2439   2682   3261     47    303    273       C  
+ATOM   2194  CE  LYS B 114      34.007 -20.876  69.721  1.00 25.13           C  
+ANISOU 2194  CE  LYS B 114     2764   3018   3767    -54    267    316       C  
+ATOM   2195  NZ  LYS B 114      32.648 -20.453  69.291  1.00 23.57           N1+
+ANISOU 2195  NZ  LYS B 114     2446   2856   3654    -92    253    374       N1+
+ATOM   2196  N   GLY B 115      39.861 -17.890  71.662  1.00 18.20           N  
+ANISOU 2196  N   GLY B 115     2184   2226   2507    217    199    -10       N  
+ATOM   2197  CA  GLY B 115      40.507 -16.590  71.753  1.00 17.31           C  
+ANISOU 2197  CA  GLY B 115     2091   2125   2362    226    167    -78       C  
+ATOM   2198  C   GLY B 115      39.592 -15.458  71.298  1.00 18.57           C  
+ANISOU 2198  C   GLY B 115     2250   2279   2525    215    195    -71       C  
+ATOM   2199  O   GLY B 115      38.523 -15.700  70.743  1.00 16.52           O  
+ANISOU 2199  O   GLY B 115     1954   2021   2301    195    226    -16       O  
+ATOM   2200  N   PRO B 116      40.005 -14.200  71.544  1.00 14.07           N  
+ANISOU 2200  N   PRO B 116     1718   1693   1937    227    171   -127       N  
+ATOM   2201  CA  PRO B 116      39.228 -13.053  71.051  1.00 14.71           C  
+ANISOU 2201  CA  PRO B 116     1805   1742   2042    229    189   -117       C  
+ATOM   2202  C   PRO B 116      39.071 -13.067  69.530  1.00 15.09           C  
+ANISOU 2202  C   PRO B 116     1811   1782   2140    152    180    -81       C  
+ATOM   2203  O   PRO B 116      39.926 -13.607  68.813  1.00 16.61           O  
+ANISOU 2203  O   PRO B 116     1987   1985   2340     90    166   -102       O  
+ATOM   2204  CB  PRO B 116      40.059 -11.839  71.507  1.00 15.54           C  
+ANISOU 2204  CB  PRO B 116     1969   1799   2138    233    145   -198       C  
+ATOM   2205  CG  PRO B 116      40.871 -12.339  72.659  1.00 18.11           C  
+ANISOU 2205  CG  PRO B 116     2327   2155   2400    266    103   -248       C  
+ATOM   2206  CD  PRO B 116      41.173 -13.791  72.342  1.00 17.59           C  
+ANISOU 2206  CD  PRO B 116     2201   2133   2349    242    108   -201       C  
+ATOM   2207  N   ASN B 117      37.971 -12.498  69.050  1.00 16.82           N  
+ANISOU 2207  N   ASN B 117     2015   1989   2386    167    189    -27       N  
+ATOM   2208  CA  ASN B 117      37.726 -12.367  67.624  1.00 16.96           C  
+ANISOU 2208  CA  ASN B 117     2018   2006   2422    103    157     16       C  
+ATOM   2209  C   ASN B 117      38.661 -11.300  67.056  1.00 15.54           C  
+ANISOU 2209  C   ASN B 117     1887   1778   2240     57    142     -5       C  
+ATOM   2210  O   ASN B 117      38.520 -10.134  67.416  1.00 16.10           O  
+ANISOU 2210  O   ASN B 117     1992   1785   2340     95    137     -6       O  
+ATOM   2211  CB  ASN B 117      36.255 -11.985  67.402  1.00 16.13           C  
+ANISOU 2211  CB  ASN B 117     1868   1900   2361    147    148     92       C  
+ATOM   2212  CG  ASN B 117      35.891 -11.854  65.944  1.00 18.20           C  
+ANISOU 2212  CG  ASN B 117     2126   2170   2620     87     83    148       C  
+ATOM   2213  OD1 ASN B 117      36.757 -11.877  65.069  1.00 15.60           O  
+ANISOU 2213  OD1 ASN B 117     1848   1842   2236     15     68    130       O  
+ATOM   2214  ND2 ASN B 117      34.597 -11.707  65.670  1.00 21.02           N  
+ANISOU 2214  ND2 ASN B 117     2416   2539   3031    120     45    223       N  
+ATOM   2215  N   PRO B 118      39.620 -11.677  66.189  1.00 16.38           N  
+ANISOU 2215  N   PRO B 118     1997   1905   2322    -22    147    -22       N  
+ATOM   2216  CA  PRO B 118      40.525 -10.653  65.641  1.00 14.20           C  
+ANISOU 2216  CA  PRO B 118     1751   1585   2058    -81    155    -19       C  
+ATOM   2217  C   PRO B 118      39.803  -9.517  64.966  1.00 15.81           C  
+ANISOU 2217  C   PRO B 118     2001   1734   2272    -81    132     64       C  
+ATOM   2218  O   PRO B 118      40.296  -8.378  64.987  1.00 17.69           O  
+ANISOU 2218  O   PRO B 118     2276   1890   2555   -106    132     75       O  
+ATOM   2219  CB  PRO B 118      41.366 -11.431  64.611  1.00 15.10           C  
+ANISOU 2219  CB  PRO B 118     1853   1756   2129   -152    195    -30       C  
+ATOM   2220  CG  PRO B 118      41.347 -12.832  65.098  1.00 17.99           C  
+ANISOU 2220  CG  PRO B 118     2181   2167   2488   -117    197    -83       C  
+ATOM   2221  CD  PRO B 118      39.939 -13.018  65.660  1.00 17.47           C  
+ANISOU 2221  CD  PRO B 118     2112   2096   2428    -58    160    -45       C  
+ATOM   2222  N   PHE B 119      38.649  -9.809  64.373  1.00 15.63           N  
+ANISOU 2222  N   PHE B 119     1972   1744   2221    -56     98    128       N  
+ATOM   2223  CA  PHE B 119      37.894  -8.780  63.675  1.00 16.61           C  
+ANISOU 2223  CA  PHE B 119     2133   1819   2359    -40     53    227       C  
+ATOM   2224  C   PHE B 119      37.367  -7.691  64.629  1.00 17.61           C  
+ANISOU 2224  C   PHE B 119     2264   1847   2579     53     49    227       C  
+ATOM   2225  O   PHE B 119      37.047  -6.591  64.187  1.00 18.78           O  
+ANISOU 2225  O   PHE B 119     2456   1911   2767     73     19    302       O  
+ATOM   2226  CB  PHE B 119      36.733  -9.404  62.885  1.00 18.57           C  
+ANISOU 2226  CB  PHE B 119     2352   2134   2569    -32    -14    290       C  
+ATOM   2227  CG  PHE B 119      37.175 -10.405  61.841  1.00 19.41           C  
+ANISOU 2227  CG  PHE B 119     2490   2320   2564   -117    -19    271       C  
+ATOM   2228  CD1 PHE B 119      38.234 -10.125  60.989  1.00 22.14           C  
+ANISOU 2228  CD1 PHE B 119     2912   2673   2828   -190     29    279       C  
+ATOM   2229  CD2 PHE B 119      36.538 -11.629  61.729  1.00 22.23           C  
+ANISOU 2229  CD2 PHE B 119     2804   2739   2905   -126    -61    240       C  
+ATOM   2230  CE1 PHE B 119      38.637 -11.048  60.031  1.00 25.12           C  
+ANISOU 2230  CE1 PHE B 119     3331   3126   3085   -250     47    243       C  
+ATOM   2231  CE2 PHE B 119      36.931 -12.551  60.776  1.00 18.23           C  
+ANISOU 2231  CE2 PHE B 119     2347   2287   2291   -195    -69    195       C  
+ATOM   2232  CZ  PHE B 119      37.989 -12.261  59.932  1.00 21.62           C  
+ANISOU 2232  CZ  PHE B 119     2865   2733   2617   -247     -7    189       C  
+ATOM   2233  N   ASP B 120      37.306  -7.985  65.928  1.00 16.74           N  
+ANISOU 2233  N   ASP B 120     2126   1742   2494    117     82    144       N  
+ATOM   2234  CA  ASP B 120      36.888  -6.976  66.917  1.00 18.17           C  
+ANISOU 2234  CA  ASP B 120     2335   1829   2738    218     97    111       C  
+ATOM   2235  C   ASP B 120      37.964  -5.905  67.151  1.00 19.76           C  
+ANISOU 2235  C   ASP B 120     2621   1913   2975    174     88     56       C  
+ATOM   2236  O   ASP B 120      37.668  -4.864  67.730  1.00 18.81           O  
+ANISOU 2236  O   ASP B 120     2556   1678   2915    248     85     25       O  
+ATOM   2237  CB  ASP B 120      36.536  -7.633  68.263  1.00 14.42           C  
+ANISOU 2237  CB  ASP B 120     1830   1408   2240    301    148     39       C  
+ATOM   2238  CG  ASP B 120      35.148  -8.247  68.280  1.00 15.23           C  
+ANISOU 2238  CG  ASP B 120     1837   1581   2368    370    172    108       C  
+ATOM   2239  OD1 ASP B 120      34.215  -7.650  67.704  1.00 17.05           O  
+ANISOU 2239  OD1 ASP B 120     2030   1781   2667    419    146    187       O  
+ATOM   2240  OD2 ASP B 120      35.003  -9.331  68.880  1.00 19.47           O1-
+ANISOU 2240  OD2 ASP B 120     2330   2200   2870    372    213     93       O1-
+ATOM   2241  N   TYR B 121      39.192  -6.146  66.667  1.00 17.32           N  
+ANISOU 2241  N   TYR B 121     2314   1624   2644     53     86     43       N  
+ATOM   2242  CA  TYR B 121      40.337  -5.300  67.003  1.00 15.71           C  
+ANISOU 2242  CA  TYR B 121     2153   1319   2496    -15     71    -17       C  
+ATOM   2243  C   TYR B 121      40.756  -4.412  65.822  1.00 17.30           C  
+ANISOU 2243  C   TYR B 121     2391   1436   2746   -113     73     86       C  
+ATOM   2244  O   TYR B 121      41.762  -3.700  65.869  1.00 17.97           O  
+ANISOU 2244  O   TYR B 121     2493   1430   2903   -206     67     65       O  
+ATOM   2245  CB  TYR B 121      41.503  -6.174  67.485  1.00 15.62           C  
+ANISOU 2245  CB  TYR B 121     2087   1389   2457    -77     73   -102       C  
+ATOM   2246  CG  TYR B 121      41.190  -6.805  68.834  1.00 16.77           C  
+ANISOU 2246  CG  TYR B 121     2233   1586   2551     21     61   -193       C  
+ATOM   2247  CD1 TYR B 121      40.346  -7.910  68.931  1.00 17.70           C  
+ANISOU 2247  CD1 TYR B 121     2312   1808   2605     87     95   -162       C  
+ATOM   2248  CD2 TYR B 121      41.723  -6.283  70.004  1.00 19.38           C  
+ANISOU 2248  CD2 TYR B 121     2613   1857   2891     40     12   -305       C  
+ATOM   2249  CE1 TYR B 121      40.046  -8.471  70.177  1.00 19.67           C  
+ANISOU 2249  CE1 TYR B 121     2572   2104   2798    172    104   -218       C  
+ATOM   2250  CE2 TYR B 121      41.416  -6.825  71.250  1.00 20.12           C  
+ANISOU 2250  CE2 TYR B 121     2737   2009   2900    136      7   -377       C  
+ATOM   2251  CZ  TYR B 121      40.583  -7.915  71.328  1.00 20.58           C  
+ANISOU 2251  CZ  TYR B 121     2756   2174   2892    203     65   -321       C  
+ATOM   2252  OH  TYR B 121      40.293  -8.449  72.564  1.00 17.05           O  
+ANISOU 2252  OH  TYR B 121     2345   1783   2350    293     79   -367       O  
+ATOM   2253  N   LEU B 122      39.941  -4.442  64.778  1.00 19.25           N  
+ANISOU 2253  N   LEU B 122     2649   1713   2954    -96     72    208       N  
+ATOM   2254  CA  LEU B 122      40.241  -3.758  63.533  1.00 21.66           C  
+ANISOU 2254  CA  LEU B 122     3005   1966   3258   -182     80    339       C  
+ATOM   2255  C   LEU B 122      38.989  -3.036  63.059  1.00 21.16           C  
+ANISOU 2255  C   LEU B 122     2993   1831   3217    -91     25    455       C  
+ATOM   2256  O   LEU B 122      37.874  -3.499  63.307  1.00 17.16           O  
+ANISOU 2256  O   LEU B 122     2441   1384   2695     17     -7    451       O  
+ATOM   2257  CB  LEU B 122      40.711  -4.773  62.482  1.00 20.73           C  
+ANISOU 2257  CB  LEU B 122     2860   1999   3019   -265    128    379       C  
+ATOM   2258  CG  LEU B 122      42.014  -5.520  62.782  1.00 20.35           C  
+ANISOU 2258  CG  LEU B 122     2741   2024   2968   -343    192    281       C  
+ATOM   2259  CD1 LEU B 122      42.188  -6.699  61.829  1.00 18.29           C  
+ANISOU 2259  CD1 LEU B 122     2460   1911   2577   -374    245    293       C  
+ATOM   2260  CD2 LEU B 122      43.205  -4.557  62.683  1.00 23.61           C  
+ANISOU 2260  CD2 LEU B 122     3155   2338   3480   -459    232    304       C  
+ATOM   2261  N   GLY B 123      39.164  -1.918  62.368  1.00 22.17           N  
+ANISOU 2261  N   GLY B 123     3202   1828   3394   -136     14    574       N  
+ATOM   2262  CA  GLY B 123      38.024  -1.209  61.830  1.00 22.00           C  
+ANISOU 2262  CA  GLY B 123     3228   1730   3401    -40    -54    707       C  
+ATOM   2263  C   GLY B 123      38.423  -0.119  60.863  1.00 23.07           C  
+ANISOU 2263  C   GLY B 123     3470   1733   3563   -119    -59    873       C  
+ATOM   2264  O   GLY B 123      39.609   0.094  60.617  1.00 22.07           O  
+ANISOU 2264  O   GLY B 123     3369   1575   3440   -261      9    882       O  
+ATOM   2265  N   TYR B 124      37.426   0.563  60.312  1.00 23.01           N  
+ANISOU 2265  N   TYR B 124     3513   1646   3585    -25   -138   1017       N  
+ATOM   2266  CA  TYR B 124      37.680   1.680  59.410  1.00 25.12           C  
+ANISOU 2266  CA  TYR B 124     3901   1761   3882    -82   -153   1207       C  
+ATOM   2267  C   TYR B 124      36.620   2.754  59.581  1.00 31.00           C  
+ANISOU 2267  C   TYR B 124     4689   2315   4776     77   -243   1291       C  
+ATOM   2268  O   TYR B 124      35.526   2.490  60.095  1.00 26.62           O  
+ANISOU 2268  O   TYR B 124     4051   1799   4264    237   -297   1234       O  
+ATOM   2269  CB  TYR B 124      37.715   1.211  57.952  1.00 25.69           C  
+ANISOU 2269  CB  TYR B 124     4026   1986   3751   -159   -162   1373       C  
+ATOM   2270  CG  TYR B 124      36.506   0.403  57.507  1.00 29.75           C  
+ANISOU 2270  CG  TYR B 124     4490   2665   4149    -54   -271   1401       C  
+ATOM   2271  CD1 TYR B 124      35.324   1.026  57.095  1.00 33.47           C  
+ANISOU 2271  CD1 TYR B 124     4984   3067   4666     75   -407   1549       C  
+ATOM   2272  CD2 TYR B 124      36.560  -0.983  57.470  1.00 35.62           C  
+ANISOU 2272  CD2 TYR B 124     5158   3621   4755    -89   -251   1284       C  
+ATOM   2273  CE1 TYR B 124      34.216   0.263  56.684  1.00 30.95           C  
+ANISOU 2273  CE1 TYR B 124     4591   2906   4263    155   -531   1573       C  
+ATOM   2274  CE2 TYR B 124      35.476  -1.738  57.061  1.00 39.41           C  
+ANISOU 2274  CE2 TYR B 124     5587   4238   5151    -19   -367   1301       C  
+ATOM   2275  CZ  TYR B 124      34.311  -1.119  56.671  1.00 39.12           C  
+ANISOU 2275  CZ  TYR B 124     5553   4147   5165     95   -511   1444       C  
+ATOM   2276  OH  TYR B 124      33.245  -1.906  56.270  1.00 47.15           O  
+ANISOU 2276  OH  TYR B 124     6493   5306   6117    148   -646   1457       O  
+ATOM   2277  N   GLN B 125      36.941   3.957  59.115  1.00 28.82           N  
+ANISOU 2277  N   GLN B 125     4527   1888   4537     40   -229   1379       N  
+ATOM   2278  CA  GLN B 125      36.027   5.072  59.176  1.00 30.79           C  
+ANISOU 2278  CA  GLN B 125     4828   1985   4885    194   -289   1421       C  
+ATOM   2279  C   GLN B 125      36.381   6.063  58.081  1.00 33.66           C  
+ANISOU 2279  C   GLN B 125     5329   2248   5211    121   -280   1605       C  
+ATOM   2280  O   GLN B 125      37.523   6.511  57.993  1.00 33.91           O  
+ANISOU 2280  O   GLN B 125     5426   2194   5265    -35   -195   1609       O  
+ATOM   2281  CB  GLN B 125      36.102   5.727  60.549  1.00 33.06           C  
+ANISOU 2281  CB  GLN B 125     5121   2097   5343    263   -259   1231       C  
+ATOM   2282  CG  GLN B 125      35.212   6.917  60.753  1.00 37.67           C  
+ANISOU 2282  CG  GLN B 125     5768   2506   6037    432   -299   1247       C  
+ATOM   2283  CD  GLN B 125      35.369   7.510  62.138  1.00 38.29           C  
+ANISOU 2283  CD  GLN B 125     5880   2425   6243    494   -258   1034       C  
+ATOM   2284  OE1 GLN B 125      35.052   6.870  63.137  1.00 46.60           O  
+ANISOU 2284  OE1 GLN B 125     6850   3555   7299    578   -236    870       O  
+ATOM   2285  NE2 GLN B 125      35.871   8.735  62.205  1.00 40.59           N  
+ANISOU 2285  NE2 GLN B 125     6302   2493   6626    449   -242   1033       N  
+ATOM   2286  N   TYR B 126      35.406   6.393  57.242  1.00 34.86           N  
+ANISOU 2286  N   TYR B 126     5516   2420   5310    234   -367   1758       N  
+ATOM   2287  CA  TYR B 126      35.589   7.459  56.260  1.00 37.69           C  
+ANISOU 2287  CA  TYR B 126     6019   2657   5642    201   -363   1944       C  
+ATOM   2288  C   TYR B 126      35.741   8.809  56.949  1.00 39.50           C  
+ANISOU 2288  C   TYR B 126     6330   2606   6072    239   -337   1894       C  
+ATOM   2289  O   TYR B 126      35.146   9.055  57.994  1.00 39.22           O  
+ANISOU 2289  O   TYR B 126     6247   2482   6174    377   -364   1749       O  
+ATOM   2290  CB  TYR B 126      34.413   7.520  55.285  1.00 39.27           C  
+ANISOU 2290  CB  TYR B 126     6235   2939   5747    337   -489   2110       C  
+ATOM   2291  CG  TYR B 126      34.453   6.496  54.178  1.00 38.75           C  
+ANISOU 2291  CG  TYR B 126     6168   3120   5436    262   -519   2211       C  
+ATOM   2292  CD1 TYR B 126      35.222   6.704  53.040  1.00 40.32           C  
+ANISOU 2292  CD1 TYR B 126     6503   3348   5470    135   -450   2367       C  
+ATOM   2293  CD2 TYR B 126      33.722   5.312  54.271  1.00 36.97           C  
+ANISOU 2293  CD2 TYR B 126     5812   3099   5135    317   -609   2141       C  
+ATOM   2294  CE1 TYR B 126      35.255   5.773  52.018  1.00 40.18           C  
+ANISOU 2294  CE1 TYR B 126     6506   3564   5198     80   -470   2439       C  
+ATOM   2295  CE2 TYR B 126      33.752   4.373  53.254  1.00 41.27           C  
+ANISOU 2295  CE2 TYR B 126     6377   3864   5439    245   -650   2210       C  
+ATOM   2296  CZ  TYR B 126      34.519   4.609  52.130  1.00 41.89           C  
+ANISOU 2296  CZ  TYR B 126     6606   3974   5335    133   -580   2350       C  
+ATOM   2297  OH  TYR B 126      34.550   3.679  51.114  1.00 38.53           O  
+ANISOU 2297  OH  TYR B 126     6222   3773   4644     74   -612   2395       O  
+ATOM   2298  N   SER B 127      36.530   9.690  56.344  1.00 22.40           N  
+ANISOU 2298  N   SER B 127     3446   1425   3639    188    358    582       N  
+ATOM   2299  CA  SER B 127      36.723  11.036  56.877  1.00 24.76           C  
+ANISOU 2299  CA  SER B 127     3897   1451   4059    110    261    564       C  
+ATOM   2300  C   SER B 127      35.418  11.810  56.826  1.00 26.97           C  
+ANISOU 2300  C   SER B 127     4219   1522   4506    189    381    626       C  
+ATOM   2301  O   SER B 127      34.500  11.433  56.097  1.00 32.69           O  
+ANISOU 2301  O   SER B 127     4745   2421   5255    190    451    745       O  
+ATOM   2302  CB  SER B 127      37.801  11.777  56.093  1.00 31.34           C  
+ANISOU 2302  CB  SER B 127     4504   2406   4999   -123     23    765       C  
+ATOM   2303  OG  SER B 127      37.442  11.877  54.728  1.00 32.14           O  
+ANISOU 2303  OG  SER B 127     4315   2711   5187   -175     81    989       O  
+ATOM   2304  N   SER B 128      35.343  12.903  57.581  1.00 30.42           N  
+ANISOU 2304  N   SER B 128     4899   1692   4969    233    296    518       N  
+ATOM   2305  CA  SER B 128      34.116  13.685  57.671  1.00 33.97           C  
+ANISOU 2305  CA  SER B 128     5350   2071   5485    340    400    558       C  
+ATOM   2306  C   SER B 128      33.682  14.269  56.321  1.00 30.70           C  
+ANISOU 2306  C   SER B 128     4619   1790   5254    118    387    775       C  
+ATOM   2307  O   SER B 128      32.495  14.497  56.107  1.00 33.26           O  
+ANISOU 2307  O   SER B 128     4821   2180   5636    164    528    878       O  
+ATOM   2308  CB  SER B 128      34.280  14.817  58.687  1.00 43.24           C  
+ANISOU 2308  CB  SER B 128     6868   2884   6677    465    268    374       C  
+ATOM   2309  OG  SER B 128      35.137  15.829  58.185  1.00 52.64           O  
+ANISOU 2309  OG  SER B 128     8079   3878   8045    211    -88    418       O  
+ATOM   2310  N   ASP B 129      34.634  14.506  55.419  1.00 29.67           N  
+ANISOU 2310  N   ASP B 129     4271   1764   5239   -116    225    883       N  
+ATOM   2311  CA  ASP B 129      34.309  15.008  54.078  1.00 33.77           C  
+ANISOU 2311  CA  ASP B 129     4406   2519   5906   -292    198   1077       C  
+ATOM   2312  C   ASP B 129      34.157  13.879  53.039  1.00 33.96           C  
+ANISOU 2312  C   ASP B 129     4250   2839   5813   -309    237   1179       C  
+ATOM   2313  O   ASP B 129      33.783  14.123  51.892  1.00 30.32           O  
+ANISOU 2313  O   ASP B 129     3563   2565   5391   -401    193   1303       O  
+ATOM   2314  CB  ASP B 129      35.367  16.019  53.603  1.00 41.03           C  
+ANISOU 2314  CB  ASP B 129     5075   3473   7042   -479    -69   1220       C  
+ATOM   2315  CG  ASP B 129      36.797  15.473  53.669  1.00 43.34           C  
+ANISOU 2315  CG  ASP B 129     5304   3856   7306   -535   -258   1334       C  
+ATOM   2316  OD1 ASP B 129      36.994  14.247  53.776  1.00 33.23           O  
+ANISOU 2316  OD1 ASP B 129     4127   2663   5835   -445   -127   1308       O  
+ATOM   2317  OD2 ASP B 129      37.742  16.283  53.594  1.00 45.84           O1-
+ANISOU 2317  OD2 ASP B 129     5424   4183   7811   -662   -571   1508       O1-
+ATOM   2318  N   GLY B 130      34.462  12.650  53.446  1.00 28.62           N  
+ANISOU 2318  N   GLY B 130     3725   2169   4979   -195    283   1111       N  
+ATOM   2319  CA  GLY B 130      34.243  11.489  52.599  1.00 29.95           C  
+ANISOU 2319  CA  GLY B 130     3861   2503   5017   -164    264   1183       C  
+ATOM   2320  C   GLY B 130      35.338  11.221  51.575  1.00 26.19           C  
+ANISOU 2320  C   GLY B 130     3260   2240   4452   -200    200   1401       C  
+ATOM   2321  O   GLY B 130      35.246  10.280  50.781  1.00 27.41           O  
+ANISOU 2321  O   GLY B 130     3505   2554   4357   -101    144   1402       O  
+ATOM   2322  N   LYS B 131      36.389  12.023  51.616  1.00 24.94           N  
+ANISOU 2322  N   LYS B 131     2923   2212   4341   -275    149   1487       N  
+ATOM   2323  CA  LYS B 131      37.489  11.901  50.653  1.00 26.25           C  
+ANISOU 2323  CA  LYS B 131     2881   2795   4297   -211    126   1707       C  
+ATOM   2324  C   LYS B 131      38.524  10.833  51.032  1.00 26.22           C  
+ANISOU 2324  C   LYS B 131     2990   2997   3977    -11    192   1599       C  
+ATOM   2325  O   LYS B 131      39.342  10.432  50.203  1.00 27.72           O  
+ANISOU 2325  O   LYS B 131     3078   3546   3907    175    275   1803       O  
+ATOM   2326  CB  LYS B 131      38.181  13.261  50.468  1.00 34.23           C  
+ANISOU 2326  CB  LYS B 131     3518   3854   5634   -384    -18   2044       C  
+ATOM   2327  CG  LYS B 131      37.231  14.459  50.384  1.00 38.15           C  
+ANISOU 2327  CG  LYS B 131     3909   4147   6439   -544   -117   1965       C  
+ATOM   2328  CD  LYS B 131      37.996  15.794  50.418  1.00 46.18           C  
+ANISOU 2328  CD  LYS B 131     4600   5188   7758   -638   -391   2162       C  
+ATOM   2329  CE  LYS B 131      37.171  16.946  49.837  1.00 47.85           C  
+ANISOU 2329  CE  LYS B 131     4651   5379   8150   -668   -476   2147       C  
+ATOM   2330  NZ  LYS B 131      37.071  18.125  50.757  1.00 52.32           N1+
+ANISOU 2330  NZ  LYS B 131     5271   5613   8995   -741   -680   2024       N1+
+ATOM   2331  N   GLN B 132      38.497  10.360  52.274  1.00 27.70           N  
+ANISOU 2331  N   GLN B 132     3381   2971   4172    -10    193   1323       N  
+ATOM   2332  CA  GLN B 132      39.514   9.409  52.714  1.00 24.85           C  
+ANISOU 2332  CA  GLN B 132     3064   2785   3594    114    248   1264       C  
+ATOM   2333  C   GLN B 132      38.939   8.305  53.586  1.00 22.92           C  
+ANISOU 2333  C   GLN B 132     3064   2398   3246    201    292    917       C  
+ATOM   2334  O   GLN B 132      38.050   8.546  54.401  1.00 23.61           O  
+ANISOU 2334  O   GLN B 132     3278   2202   3492    155    279    766       O  
+ATOM   2335  CB  GLN B 132      40.645  10.137  53.463  1.00 26.20           C  
+ANISOU 2335  CB  GLN B 132     3091   2891   3972    -51    100   1465       C  
+ATOM   2336  CG  GLN B 132      41.430  11.122  52.570  1.00 28.74           C  
+ANISOU 2336  CG  GLN B 132     3029   3404   4487   -113     -2   1987       C  
+ATOM   2337  CD  GLN B 132      42.346  12.056  53.330  1.00 40.37           C  
+ANISOU 2337  CD  GLN B 132     4360   4652   6325   -352   -346   2273       C  
+ATOM   2338  OE1 GLN B 132      42.954  12.948  52.737  1.00 46.76           O  
+ANISOU 2338  OE1 GLN B 132     4783   5589   7394   -422   -521   2696       O  
+ATOM   2339  NE2 GLN B 132      42.462  11.858  54.639  1.00 34.67           N  
+ANISOU 2339  NE2 GLN B 132     3948   3613   5610   -462   -497   1994       N  
+ATOM   2340  N   LEU B 133      39.463   7.094  53.404  1.00 22.72           N  
+ANISOU 2340  N   LEU B 133     3080   2581   2970    375    361    847       N  
+ATOM   2341  CA  LEU B 133      39.091   5.961  54.251  1.00 21.69           C  
+ANISOU 2341  CA  LEU B 133     3076   2359   2805    447    354    581       C  
+ATOM   2342  C   LEU B 133      40.256   5.702  55.192  1.00 22.52           C  
+ANISOU 2342  C   LEU B 133     3099   2546   2912    374    400    588       C  
+ATOM   2343  O   LEU B 133      41.391   5.473  54.752  1.00 25.26           O  
+ANISOU 2343  O   LEU B 133     3319   3126   3153    427    483    795       O  
+ATOM   2344  CB  LEU B 133      38.769   4.719  53.422  1.00 25.04           C  
+ANISOU 2344  CB  LEU B 133     3636   2873   3004    674    298    479       C  
+ATOM   2345  CG  LEU B 133      38.353   3.484  54.228  1.00 24.62           C  
+ANISOU 2345  CG  LEU B 133     3621   2719   3013    742    200    276       C  
+ATOM   2346  CD1 LEU B 133      37.083   3.767  55.013  1.00 25.30           C  
+ANISOU 2346  CD1 LEU B 133     3677   2530   3406    664    128    296       C  
+ATOM   2347  CD2 LEU B 133      38.189   2.261  53.324  1.00 28.55           C  
+ANISOU 2347  CD2 LEU B 133     4319   3235   3294    979     15    172       C  
+ATOM   2348  N   HIS B 134      39.985   5.796  56.485  1.00 20.32           N  
+ANISOU 2348  N   HIS B 134     2897   2068   2756    271    356    436       N  
+ATOM   2349  CA  HIS B 134      41.031   5.632  57.475  1.00 21.17           C  
+ANISOU 2349  CA  HIS B 134     2974   2188   2884    133    320    460       C  
+ATOM   2350  C   HIS B 134      40.864   4.284  58.149  1.00 24.61           C  
+ANISOU 2350  C   HIS B 134     3378   2705   3269    220    379    267       C  
+ATOM   2351  O   HIS B 134      39.743   3.864  58.418  1.00 27.51           O  
+ANISOU 2351  O   HIS B 134     3792   2990   3671    354    385    118       O  
+ATOM   2352  CB  HIS B 134      40.982   6.768  58.495  1.00 21.34           C  
+ANISOU 2352  CB  HIS B 134     3197   1898   3014    -27    159    422       C  
+ATOM   2353  CG  HIS B 134      41.394   8.096  57.931  1.00 24.10           C  
+ANISOU 2353  CG  HIS B 134     3509   2136   3513   -168    -14    672       C  
+ATOM   2354  ND1 HIS B 134      42.631   8.651  58.172  1.00 31.12           N  
+ANISOU 2354  ND1 HIS B 134     4321   2949   4554   -393   -271    976       N  
+ATOM   2355  CD2 HIS B 134      40.747   8.956  57.110  1.00 29.15           C  
+ANISOU 2355  CD2 HIS B 134     4109   2719   4246   -141    -14    745       C  
+ATOM   2356  CE1 HIS B 134      42.722   9.810  57.541  1.00 33.34           C  
+ANISOU 2356  CE1 HIS B 134     4498   3136   5035   -477   -450   1229       C  
+ATOM   2357  NE2 HIS B 134      41.590  10.020  56.893  1.00 32.00           N  
+ANISOU 2357  NE2 HIS B 134     4347   2996   4816   -329   -271   1062       N  
+ATOM   2358  N   LEU B 135      41.982   3.621  58.420  1.00 24.49           N  
+ANISOU 2358  N   LEU B 135     3220   2844   3241    138    410    363       N  
+ATOM   2359  CA  LEU B 135      41.980   2.317  59.063  1.00 22.50           C  
+ANISOU 2359  CA  LEU B 135     2856   2692   3000    179    446    218       C  
+ATOM   2360  C   LEU B 135      42.404   2.448  60.525  1.00 19.50           C  
+ANISOU 2360  C   LEU B 135     2502   2213   2695    -45    368    201       C  
+ATOM   2361  O   LEU B 135      43.265   3.272  60.858  1.00 19.41           O  
+ANISOU 2361  O   LEU B 135     2568   2079   2728   -276    246    387       O  
+ATOM   2362  CB  LEU B 135      42.917   1.348  58.331  1.00 25.40           C  
+ANISOU 2362  CB  LEU B 135     3052   3297   3301    276    570    348       C  
+ATOM   2363  CG  LEU B 135      42.659   1.068  56.848  1.00 31.65           C  
+ANISOU 2363  CG  LEU B 135     3948   4191   3886    585    633    342       C  
+ATOM   2364  CD1 LEU B 135      43.641   0.037  56.331  1.00 36.96           C  
+ANISOU 2364  CD1 LEU B 135     4541   5072   4430    787    811    453       C  
+ATOM   2365  CD2 LEU B 135      41.233   0.632  56.599  1.00 32.51           C  
+ANISOU 2365  CD2 LEU B 135     4206   4155   3993    734    447     81       C  
+ATOM   2366  N   TYR B 136      41.811   1.619  61.384  1.00 18.57           N  
+ANISOU 2366  N   TYR B 136     2315   2131   2609     27    381     33       N  
+ATOM   2367  CA  TYR B 136      42.042   1.701  62.822  1.00 19.88           C  
+ANISOU 2367  CA  TYR B 136     2569   2223   2764   -118    316    -10       C  
+ATOM   2368  C   TYR B 136      42.264   0.318  63.426  1.00 19.68           C  
+ANISOU 2368  C   TYR B 136     2208   2416   2852   -153    352    -20       C  
+ATOM   2369  O   TYR B 136      41.777  -0.691  62.895  1.00 22.36           O  
+ANISOU 2369  O   TYR B 136     2292   2903   3302     22    387    -58       O  
+ATOM   2370  CB  TYR B 136      40.861   2.374  63.532  1.00 17.94           C  
+ANISOU 2370  CB  TYR B 136     2613   1795   2409    104    342   -150       C  
+ATOM   2371  CG  TYR B 136      40.705   3.829  63.148  1.00 20.92           C  
+ANISOU 2371  CG  TYR B 136     3342   1900   2708    104    273   -153       C  
+ATOM   2372  CD1 TYR B 136      41.380   4.824  63.835  1.00 21.09           C  
+ANISOU 2372  CD1 TYR B 136     3731   1651   2630    -78     50   -164       C  
+ATOM   2373  CD2 TYR B 136      39.925   4.192  62.062  1.00 20.65           C  
+ANISOU 2373  CD2 TYR B 136     3267   1842   2739    251    352   -117       C  
+ATOM   2374  CE1 TYR B 136      41.254   6.159  63.467  1.00 25.73           C  
+ANISOU 2374  CE1 TYR B 136     4611   1952   3215    -86    -92   -155       C  
+ATOM   2375  CE2 TYR B 136      39.794   5.513  61.691  1.00 20.04           C  
+ANISOU 2375  CE2 TYR B 136     3430   1532   2654    223    282    -92       C  
+ATOM   2376  CZ  TYR B 136      40.460   6.482  62.391  1.00 25.47           C  
+ANISOU 2376  CZ  TYR B 136     4445   1959   3274     65     63   -117       C  
+ATOM   2377  OH  TYR B 136      40.317   7.783  62.004  1.00 30.92           O  
+ANISOU 2377  OH  TYR B 136     5342   2386   4020     36    -74    -81       O  
+ATOM   2378  N   GLU B 137      43.024   0.283  64.520  1.00 19.29           N  
+ANISOU 2378  N   GLU B 137     2175   2349   2803   -407    273     36       N  
+ATOM   2379  CA  GLU B 137      43.198  -0.941  65.310  1.00 19.82           C  
+ANISOU 2379  CA  GLU B 137     1889   2632   3010   -483    297     49       C  
+ATOM   2380  C   GLU B 137      43.165  -0.629  66.811  1.00 21.94           C  
+ANISOU 2380  C   GLU B 137     2382   2823   3129   -566    208      4       C  
+ATOM   2381  O   GLU B 137      43.525   0.467  67.242  1.00 20.97           O  
+ANISOU 2381  O   GLU B 137     2734   2421   2811   -694     42    -10       O  
+ATOM   2382  CB  GLU B 137      44.511  -1.644  64.954  1.00 17.65           C  
+ANISOU 2382  CB  GLU B 137     1558   2465   2683   -619    271    109       C  
+ATOM   2383  CG  GLU B 137      45.762  -0.905  65.458  1.00 22.81           C  
+ANISOU 2383  CG  GLU B 137     2356   2894   3418   -834    200    277       C  
+ATOM   2384  CD  GLU B 137      47.077  -1.563  65.043  1.00 31.76           C  
+ANISOU 2384  CD  GLU B 137     3387   4105   4575   -808    185    468       C  
+ATOM   2385  OE1 GLU B 137      47.173  -2.814  65.012  1.00 26.06           O  
+ANISOU 2385  OE1 GLU B 137     2541   3497   3864   -684    216    436       O  
+ATOM   2386  OE2 GLU B 137      48.027  -0.816  64.741  1.00 26.94           O1-
+ANISOU 2386  OE2 GLU B 137     2808   3414   4014   -904     88    739       O1-
+ATOM   2387  N   TRP B 138      42.748  -1.617  67.597  1.00 19.27           N  
+ANISOU 2387  N   TRP B 138     1719   2720   2882   -472    271      1       N  
+ATOM   2388  CA  TRP B 138      42.738  -1.523  69.044  1.00 24.11           C  
+ANISOU 2388  CA  TRP B 138     2513   3344   3305   -491    224    -14       C  
+ATOM   2389  C   TRP B 138      44.124  -1.842  69.573  1.00 27.32           C  
+ANISOU 2389  C   TRP B 138     2867   3692   3823   -906     47    116       C  
+ATOM   2390  O   TRP B 138      44.647  -2.946  69.355  1.00 25.19           O  
+ANISOU 2390  O   TRP B 138     2453   3398   3719   -684    115     76       O  
+ATOM   2391  CB  TRP B 138      41.712  -2.488  69.640  1.00 23.39           C  
+ANISOU 2391  CB  TRP B 138     1991   3568   3330   -146    375     53       C  
+ATOM   2392  CG  TRP B 138      41.585  -2.365  71.120  1.00 26.58           C  
+ANISOU 2392  CG  TRP B 138     2611   4042   3445    -30    400     68       C  
+ATOM   2393  CD1 TRP B 138      42.130  -3.187  72.074  1.00 27.17           C  
+ANISOU 2393  CD1 TRP B 138     2359   4354   3612   -265    339    184       C  
+ATOM   2394  CD2 TRP B 138      40.878  -1.340  71.830  1.00 22.17           C  
+ANISOU 2394  CD2 TRP B 138     2711   3307   2407    396    505    -31       C  
+ATOM   2395  NE1 TRP B 138      41.796  -2.736  73.332  1.00 23.48           N  
+ANISOU 2395  NE1 TRP B 138     2331   3892   2699      4    388    158       N  
+ATOM   2396  CE2 TRP B 138      41.031  -1.601  73.206  1.00 22.85           C  
+ANISOU 2396  CE2 TRP B 138     2904   3544   2235    453    504     12       C  
+ATOM   2397  CE3 TRP B 138      40.134  -0.222  71.433  1.00 22.71           C  
+ANISOU 2397  CE3 TRP B 138     3308   3094   2228    761    614   -143       C  
+ATOM   2398  CZ2 TRP B 138      40.460  -0.791  74.185  1.00 26.39           C  
+ANISOU 2398  CZ2 TRP B 138     4058   3866   2103    949    627    -78       C  
+ATOM   2399  CZ3 TRP B 138      39.562   0.579  72.413  1.00 26.07           C  
+ANISOU 2399  CZ3 TRP B 138     4386   3376   2143   1230    749   -221       C  
+ATOM   2400  CH2 TRP B 138      39.734   0.292  73.769  1.00 28.92           C  
+ANISOU 2400  CH2 TRP B 138     4931   3884   2172   1359    761   -203       C  
+ATOM   2401  N   THR B 139      44.715  -0.895  70.290  1.00 23.53           N  
+ANISOU 2401  N   THR B 139     2899   2949   3093  -1241   -211    136       N  
+ATOM   2402  CA  THR B 139      46.101  -1.058  70.706  1.00 28.04           C  
+ANISOU 2402  CA  THR B 139     3434   3442   3776  -1296   -334    285       C  
+ATOM   2403  C   THR B 139      46.231  -1.379  72.189  1.00 29.31           C  
+ANISOU 2403  C   THR B 139     3711   3652   3776  -1441   -470    311       C  
+ATOM   2404  O   THR B 139      47.336  -1.411  72.727  1.00 28.90           O  
+ANISOU 2404  O   THR B 139     3707   3527   3748  -1509   -601    443       O  
+ATOM   2405  CB  THR B 139      46.930   0.197  70.383  1.00 33.01           C  
+ANISOU 2405  CB  THR B 139     4446   3765   4333  -1483   -622    428       C  
+ATOM   2406  OG1 THR B 139      46.384   1.331  71.072  1.00 34.53           O  
+ANISOU 2406  OG1 THR B 139     5406   3554   4158  -1628   -967    289       O  
+ATOM   2407  CG2 THR B 139      46.923   0.460  68.874  1.00 31.92           C  
+ANISOU 2407  CG2 THR B 139     4130   3642   4357  -1359   -464    466       C  
+ATOM   2408  N   GLY B 140      45.104  -1.614  72.854  1.00 29.12           N  
+ANISOU 2408  N   GLY B 140     3717   3816   3531  -1478   -412    191       N  
+ATOM   2409  CA  GLY B 140      45.135  -2.017  74.251  1.00 34.67           C  
+ANISOU 2409  CA  GLY B 140     4491   4662   4019  -1508   -482    215       C  
+ATOM   2410  C   GLY B 140      44.199  -1.219  75.135  1.00 37.84           C  
+ANISOU 2410  C   GLY B 140     5659   4950   3770   -920   -425    -31       C  
+ATOM   2411  O   GLY B 140      43.472  -1.778  75.957  1.00 35.60           O  
+ANISOU 2411  O   GLY B 140     5191   5025   3311   -516   -175      6       O  
+ATOM   2412  N   GLY B 141      44.217   0.099  74.973  1.00 31.68           N  
+ANISOU 2412  N   GLY B 141     5732   3667   2637   -821   -649   -235       N  
+ATOM   2413  CA  GLY B 141      43.363   0.962  75.763  1.00 35.46           C  
+ANISOU 2413  CA  GLY B 141     7077   3955   2442   -185   -578   -494       C  
+ATOM   2414  C   GLY B 141      42.577   1.936  74.910  1.00 35.36           C  
+ANISOU 2414  C   GLY B 141     7402   3697   2337    232   -418   -663       C  
+ATOM   2415  O   GLY B 141      41.792   2.727  75.430  1.00 43.29           O  
+ANISOU 2415  O   GLY B 141     8951   4529   2967    804   -275   -790       O  
+ATOM   2416  N   LYS B 142      42.782   1.880  73.596  1.00 33.01           N  
+ANISOU 2416  N   LYS B 142     6591   3409   2540    -55   -403   -563       N  
+ATOM   2417  CA  LYS B 142      42.094   2.796  72.692  1.00 35.17           C  
+ANISOU 2417  CA  LYS B 142     7105   3463   2796    250   -281   -679       C  
+ATOM   2418  C   LYS B 142      42.251   2.410  71.234  1.00 30.00           C  
+ANISOU 2418  C   LYS B 142     5744   2971   2682    -15   -190   -521       C  
+ATOM   2419  O   LYS B 142      43.126   1.625  70.873  1.00 31.64           O  
+ANISOU 2419  O   LYS B 142     5416   3355   3252   -470   -285   -336       O  
+ATOM   2420  CB  LYS B 142      42.600   4.233  72.893  1.00 39.69           C  
+ANISOU 2420  CB  LYS B 142     8493   3448   3138    138   -738   -803       C  
+ATOM   2421  CG  LYS B 142      44.054   4.443  72.515  1.00 36.96           C  
+ANISOU 2421  CG  LYS B 142     8044   2863   3137   -574  -1265   -578       C  
+ATOM   2422  CD  LYS B 142      44.428   5.927  72.604  1.00 48.58           C  
+ANISOU 2422  CD  LYS B 142    10065   3876   4517   -573  -1700   -520       C  
+ATOM   2423  CE  LYS B 142      45.885   6.169  72.232  1.00 53.39           C  
+ANISOU 2423  CE  LYS B 142    10421   4373   5491  -1143  -2193   -111       C  
+ATOM   2424  NZ  LYS B 142      46.231   7.627  72.198  1.00 58.71           N1+
+ANISOU 2424  NZ  LYS B 142    11574   4639   6096  -1131  -2706    -21       N1+
+ATOM   2425  N   TRP B 143      41.378   2.958  70.397  1.00 28.25           N  
+ANISOU 2425  N   TRP B 143     5556   2685   2493    311     16   -572       N  
+ATOM   2426  CA  TRP B 143      41.545   2.834  68.964  1.00 23.84           C  
+ANISOU 2426  CA  TRP B 143     4533   2199   2324    100     41   -458       C  
+ATOM   2427  C   TRP B 143      42.594   3.832  68.509  1.00 28.39           C  
+ANISOU 2427  C   TRP B 143     5425   2411   2951   -303   -350   -417       C  
+ATOM   2428  O   TRP B 143      42.586   5.001  68.929  1.00 30.24           O  
+ANISOU 2428  O   TRP B 143     6327   2227   2934   -241   -607   -550       O  
+ATOM   2429  CB  TRP B 143      40.221   3.061  68.224  1.00 26.11           C  
+ANISOU 2429  CB  TRP B 143     4725   2529   2667    541    346   -457       C  
+ATOM   2430  CG  TRP B 143      39.235   1.956  68.458  1.00 24.26           C  
+ANISOU 2430  CG  TRP B 143     3996   2644   2577    884    637   -303       C  
+ATOM   2431  CD1 TRP B 143      38.261   1.912  69.422  1.00 35.33           C  
+ANISOU 2431  CD1 TRP B 143     5511   4125   3787   1393    893   -210       C  
+ATOM   2432  CD2 TRP B 143      39.127   0.734  67.721  1.00 24.97           C  
+ANISOU 2432  CD2 TRP B 143     3397   3025   3066    788    654   -146       C  
+ATOM   2433  NE1 TRP B 143      37.555   0.731  69.325  1.00 27.12           N  
+ANISOU 2433  NE1 TRP B 143     3766   3424   3114   1434    939     94       N  
+ATOM   2434  CE2 TRP B 143      38.070  -0.011  68.294  1.00 28.07           C  
+ANISOU 2434  CE2 TRP B 143     3449   3634   3581   1122    791     77       C  
+ATOM   2435  CE3 TRP B 143      39.824   0.192  66.637  1.00 19.25           C  
+ANISOU 2435  CE3 TRP B 143     2348   2376   2592    464    521   -141       C  
+ATOM   2436  CZ2 TRP B 143      37.697  -1.263  67.815  1.00 23.63           C  
+ANISOU 2436  CZ2 TRP B 143     2416   3219   3343    860    543    182       C  
+ATOM   2437  CZ3 TRP B 143      39.448  -1.054  66.157  1.00 23.67           C  
+ANISOU 2437  CZ3 TRP B 143     2366   3157   3472    528    504    -22       C  
+ATOM   2438  CH2 TRP B 143      38.396  -1.769  66.744  1.00 19.43           C  
+ANISOU 2438  CH2 TRP B 143     1740   2704   2938    606    372     52       C  
+ATOM   2439  N   GLU B 144      43.513   3.354  67.676  1.00 24.49           N  
+ANISOU 2439  N   GLU B 144     4449   2056   2798   -677   -416   -175       N  
+ATOM   2440  CA  GLU B 144      44.496   4.217  67.033  1.00 25.16           C  
+ANISOU 2440  CA  GLU B 144     4628   1870   3060  -1017   -745     63       C  
+ATOM   2441  C   GLU B 144      44.490   3.997  65.524  1.00 22.87           C  
+ANISOU 2441  C   GLU B 144     3857   1823   3009   -961   -506    234       C  
+ATOM   2442  O   GLU B 144      44.117   2.938  65.045  1.00 26.08           O  
+ANISOU 2442  O   GLU B 144     3854   2574   3482   -800   -191    195       O  
+ATOM   2443  CB  GLU B 144      45.887   3.964  67.602  1.00 27.45           C  
+ANISOU 2443  CB  GLU B 144     4750   2179   3501  -1396  -1024    368       C  
+ATOM   2444  CG  GLU B 144      46.034   4.407  69.042  1.00 40.16           C  
+ANISOU 2444  CG  GLU B 144     6908   3537   4813  -1431  -1360    248       C  
+ATOM   2445  CD  GLU B 144      47.471   4.393  69.520  1.00 46.96           C  
+ANISOU 2445  CD  GLU B 144     7568   4464   5811  -1686  -1666    604       C  
+ATOM   2446  OE1 GLU B 144      48.268   5.240  69.060  1.00 54.03           O  
+ANISOU 2446  OE1 GLU B 144     8422   5252   6853  -1781  -1975    865       O  
+ATOM   2447  OE2 GLU B 144      47.801   3.532  70.360  1.00 41.39           O1-
+ANISOU 2447  OE2 GLU B 144     6722   3927   5077  -1765  -1609    636       O1-
+ATOM   2448  N   GLU B 145      44.890   5.015  64.774  1.00 24.71           N  
+ANISOU 2448  N   GLU B 145     4172   1854   3363  -1067   -704    440       N  
+ATOM   2449  CA  GLU B 145      45.011   4.837  63.341  1.00 29.27           C  
+ANISOU 2449  CA  GLU B 145     4332   2687   4101   -983   -476    657       C  
+ATOM   2450  C   GLU B 145      45.992   3.684  63.059  1.00 22.11           C  
+ANISOU 2450  C   GLU B 145     2955   2077   3369  -1119   -309    967       C  
+ATOM   2451  O   GLU B 145      47.041   3.559  63.706  1.00 23.40           O  
+ANISOU 2451  O   GLU B 145     3032   2278   3581  -1217   -444   1073       O  
+ATOM   2452  CB  GLU B 145      45.462   6.142  62.674  1.00 33.32           C  
+ANISOU 2452  CB  GLU B 145     4916   2966   4778  -1104   -756    963       C  
+ATOM   2453  CG  GLU B 145      45.182   6.176  61.191  1.00 37.24           C  
+ANISOU 2453  CG  GLU B 145     5102   3734   5313   -883   -475   1091       C  
+ATOM   2454  CD  GLU B 145      44.899   7.572  60.663  1.00 37.88           C  
+ANISOU 2454  CD  GLU B 145     5314   3588   5490   -884   -694   1182       C  
+ATOM   2455  OE1 GLU B 145      45.144   8.570  61.382  1.00 38.71           O  
+ANISOU 2455  OE1 GLU B 145     5721   3312   5676  -1061  -1123   1194       O  
+ATOM   2456  OE2 GLU B 145      44.426   7.664  59.517  1.00 36.22           O1-
+ANISOU 2456  OE2 GLU B 145     4911   3591   5258   -685   -463   1217       O1-
+ATOM   2457  N   TYR B 146      45.615   2.821  62.129  1.00 20.05           N  
+ANISOU 2457  N   TYR B 146     3178   1608   2833   -488    -90    -32       N  
+ATOM   2458  CA  TYR B 146      46.398   1.630  61.796  1.00 18.42           C  
+ANISOU 2458  CA  TYR B 146     2834   1504   2661   -557     32     46       C  
+ATOM   2459  C   TYR B 146      47.751   2.037  61.187  1.00 26.77           C  
+ANISOU 2459  C   TYR B 146     3701   2527   3944   -694   -128    191       C  
+ATOM   2460  O   TYR B 146      47.795   2.932  60.361  1.00 26.72           O  
+ANISOU 2460  O   TYR B 146     3560   2500   4094   -776   -177    305       O  
+ATOM   2461  CB  TYR B 146      45.595   0.756  60.837  1.00 19.53           C  
+ANISOU 2461  CB  TYR B 146     2862   1783   2775   -584    294     65       C  
+ATOM   2462  CG  TYR B 146      46.258  -0.543  60.488  1.00 23.32           C  
+ANISOU 2462  CG  TYR B 146     3237   2354   3269   -601    394    102       C  
+ATOM   2463  CD1 TYR B 146      46.465  -1.528  61.454  1.00 22.66           C  
+ANISOU 2463  CD1 TYR B 146     3224   2254   3134   -531    450     83       C  
+ATOM   2464  CD2 TYR B 146      46.676  -0.795  59.189  1.00 24.21           C  
+ANISOU 2464  CD2 TYR B 146     3195   2585   3421   -628    439    167       C  
+ATOM   2465  CE1 TYR B 146      47.081  -2.723  61.128  1.00 23.92           C  
+ANISOU 2465  CE1 TYR B 146     3291   2478   3321   -542    523    108       C  
+ATOM   2466  CE2 TYR B 146      47.294  -1.980  58.859  1.00 22.16           C  
+ANISOU 2466  CE2 TYR B 146     2870   2409   3141   -586    505    179       C  
+ATOM   2467  CZ  TYR B 146      47.490  -2.943  59.834  1.00 23.24           C  
+ANISOU 2467  CZ  TYR B 146     3069   2493   3266   -570    535    138       C  
+ATOM   2468  OH  TYR B 146      48.106  -4.122  59.497  1.00 20.94           O  
+ANISOU 2468  OH  TYR B 146     2718   2269   2969   -525    583    141       O  
+ATOM   2469  N   LYS B 147      48.845   1.405  61.608  1.00 23.44           N  
+ANISOU 2469  N   LYS B 147     3241   2098   3568   -702   -193    235       N  
+ATOM   2470  CA  LYS B 147      50.174   1.860  61.183  1.00 30.49           C  
+ANISOU 2470  CA  LYS B 147     3910   2925   4751   -816   -360    440       C  
+ATOM   2471  C   LYS B 147      50.739   1.189  59.930  1.00 24.87           C  
+ANISOU 2471  C   LYS B 147     2956   2422   4070   -844   -118    668       C  
+ATOM   2472  O   LYS B 147      51.573   1.777  59.243  1.00 25.53           O  
+ANISOU 2472  O   LYS B 147     2791   2498   4412   -900   -161    947       O  
+ATOM   2473  CB  LYS B 147      51.178   1.687  62.328  1.00 35.19           C  
+ANISOU 2473  CB  LYS B 147     4572   3372   5427   -787   -623    384       C  
+ATOM   2474  CG  LYS B 147      51.134   2.799  63.372  1.00 38.83           C  
+ANISOU 2474  CG  LYS B 147     5213   3558   5982   -712  -1041    209       C  
+ATOM   2475  CD  LYS B 147      52.173   2.590  64.468  1.00 41.95           C  
+ANISOU 2475  CD  LYS B 147     5690   3798   6452   -629  -1366    116       C  
+ATOM   2476  CE  LYS B 147      51.775   3.309  65.758  1.00 48.72           C  
+ANISOU 2476  CE  LYS B 147     6893   4451   7166   -372  -1747   -192       C  
+ATOM   2477  NZ  LYS B 147      50.604   2.660  66.435  1.00 48.75           N1+
+ANISOU 2477  NZ  LYS B 147     7207   4657   6658    -96  -1449   -350       N1+
+ATOM   2478  N   ASP B 148      50.301  -0.027  59.611  1.00 22.42           N  
+ANISOU 2478  N   ASP B 148     2706   2290   3524   -762    121    578       N  
+ATOM   2479  CA  ASP B 148      50.981  -0.760  58.536  1.00 25.69           C  
+ANISOU 2479  CA  ASP B 148     2949   2905   3910   -693    293    751       C  
+ATOM   2480  C   ASP B 148      50.351  -0.637  57.146  1.00 23.63           C  
+ANISOU 2480  C   ASP B 148     2621   2817   3540   -573    456    802       C  
+ATOM   2481  O   ASP B 148      50.862  -1.209  56.176  1.00 26.02           O  
+ANISOU 2481  O   ASP B 148     2822   3320   3745   -407    593    934       O  
+ATOM   2482  CB  ASP B 148      51.093  -2.235  58.918  1.00 23.24           C  
+ANISOU 2482  CB  ASP B 148     2731   2659   3441   -626    387    618       C  
+ATOM   2483  CG  ASP B 148      52.101  -2.461  60.022  1.00 26.63           C  
+ANISOU 2483  CG  ASP B 148     3176   2987   3955   -681    256    647       C  
+ATOM   2484  OD1 ASP B 148      53.137  -1.772  60.007  1.00 31.09           O  
+ANISOU 2484  OD1 ASP B 148     3579   3493   4743   -746    118    854       O  
+ATOM   2485  OD2 ASP B 148      51.853  -3.309  60.906  1.00 23.45           O1-
+ANISOU 2485  OD2 ASP B 148     2923   2550   3437   -645    280    490       O1-
+ATOM   2486  N   LEU B 149      49.247   0.095  57.057  1.00 22.00           N  
+ANISOU 2486  N   LEU B 149     2493   2549   3316   -604    432    690       N  
+ATOM   2487  CA  LEU B 149      48.717   0.529  55.771  1.00 25.46           C  
+ANISOU 2487  CA  LEU B 149     2860   3133   3679   -480    540    764       C  
+ATOM   2488  C   LEU B 149      48.298   1.982  55.847  1.00 29.16           C  
+ANISOU 2488  C   LEU B 149     3297   3476   4306   -587    448    840       C  
+ATOM   2489  O   LEU B 149      47.767   2.423  56.861  1.00 29.27           O  
+ANISOU 2489  O   LEU B 149     3450   3299   4372   -706    308    677       O  
+ATOM   2490  CB  LEU B 149      47.533  -0.317  55.338  1.00 22.64           C  
+ANISOU 2490  CB  LEU B 149     2637   2838   3127   -363    597    490       C  
+ATOM   2491  CG  LEU B 149      47.857  -1.714  54.830  1.00 26.46           C  
+ANISOU 2491  CG  LEU B 149     3137   3447   3470   -180    645    403       C  
+ATOM   2492  CD1 LEU B 149      46.536  -2.459  54.638  1.00 26.95           C  
+ANISOU 2492  CD1 LEU B 149     3307   3436   3497   -120    587    102       C  
+ATOM   2493  CD2 LEU B 149      48.643  -1.637  53.526  1.00 36.62           C  
+ANISOU 2493  CD2 LEU B 149     4309   4990   4614     96    750    625       C  
+ATOM   2494  N   ALA B 150      48.525   2.708  54.760  1.00 26.08           N  
+ANISOU 2494  N   ALA B 150     2730   3205   3973   -492    537   1105       N  
+ATOM   2495  CA  ALA B 150      48.188   4.130  54.674  1.00 23.51           C  
+ANISOU 2495  CA  ALA B 150     2332   2753   3849   -584    454   1229       C  
+ATOM   2496  C   ALA B 150      46.690   4.327  54.522  1.00 26.75           C  
+ANISOU 2496  C   ALA B 150     2926   3168   4071   -558    474    958       C  
+ATOM   2497  O   ALA B 150      46.001   3.419  54.062  1.00 25.51           O  
+ANISOU 2497  O   ALA B 150     2873   3151   3670   -424    574    761       O  
+ATOM   2498  CB  ALA B 150      48.918   4.754  53.506  1.00 24.14           C  
+ANISOU 2498  CB  ALA B 150     2157   2988   4025   -411    563   1601       C  
+ATOM   2499  N   PRO B 151      46.179   5.521  54.892  1.00 28.09           N  
+ANISOU 2499  N   PRO B 151     3123   3159   4392   -674    345    948       N  
+ATOM   2500  CA  PRO B 151      44.794   5.865  54.535  1.00 25.17           C  
+ANISOU 2500  CA  PRO B 151     2873   2823   3865   -626    397    772       C  
+ATOM   2501  C   PRO B 151      44.587   5.805  53.026  1.00 25.22           C  
+ANISOU 2501  C   PRO B 151     2772   3087   3722   -411    584    902       C  
+ATOM   2502  O   PRO B 151      45.555   5.900  52.260  1.00 25.63           O  
+ANISOU 2502  O   PRO B 151     2627   3283   3827   -285    692   1223       O  
+ATOM   2503  CB  PRO B 151      44.626   7.303  55.031  1.00 28.39           C  
+ANISOU 2503  CB  PRO B 151     3282   3003   4500   -750    216    827       C  
+ATOM   2504  CG  PRO B 151      45.815   7.606  55.872  1.00 29.13           C  
+ANISOU 2504  CG  PRO B 151     3305   2893   4869   -859    -10    930       C  
+ATOM   2505  CD  PRO B 151      46.899   6.649  55.514  1.00 30.11           C  
+ANISOU 2505  CD  PRO B 151     3284   3175   4982   -805    108   1090       C  
+ATOM   2506  N   TYR B 152      43.343   5.640  52.598  1.00 20.77           N  
+ANISOU 2506  N   TYR B 152     2329   2588   2973   -321    620    677       N  
+ATOM   2507  CA  TYR B 152      43.044   5.615  51.175  1.00 25.59           C  
+ANISOU 2507  CA  TYR B 152     2890   3442   3393    -44    741    738       C  
+ATOM   2508  C   TYR B 152      42.397   6.919  50.756  1.00 26.74           C  
+ANISOU 2508  C   TYR B 152     2995   3569   3595    -49    760    845       C  
+ATOM   2509  O   TYR B 152      41.416   7.340  51.351  1.00 31.68           O  
+ANISOU 2509  O   TYR B 152     3735   4037   4266   -199    672    653       O  
+ATOM   2510  CB  TYR B 152      42.120   4.453  50.828  1.00 27.80           C  
+ANISOU 2510  CB  TYR B 152     3311   3781   3472    105    694    390       C  
+ATOM   2511  CG  TYR B 152      42.718   3.106  51.114  1.00 25.27           C  
+ANISOU 2511  CG  TYR B 152     3023   3469   3110    143    663    282       C  
+ATOM   2512  CD1 TYR B 152      42.577   2.519  52.367  1.00 26.56           C  
+ANISOU 2512  CD1 TYR B 152     3251   3429   3411    -89    594    138       C  
+ATOM   2513  CD2 TYR B 152      43.420   2.415  50.137  1.00 28.51           C  
+ANISOU 2513  CD2 TYR B 152     3408   4106   3319    466    714    341       C  
+ATOM   2514  CE1 TYR B 152      43.129   1.279  52.636  1.00 27.95           C  
+ANISOU 2514  CE1 TYR B 152     3443   3603   3572    -55    572     58       C  
+ATOM   2515  CE2 TYR B 152      43.972   1.173  50.399  1.00 32.89           C  
+ANISOU 2515  CE2 TYR B 152     4001   4655   3838    512    668    230       C  
+ATOM   2516  CZ  TYR B 152      43.821   0.612  51.656  1.00 29.59           C  
+ANISOU 2516  CZ  TYR B 152     3626   4008   3608    221    593     88       C  
+ATOM   2517  OH  TYR B 152      44.368  -0.624  51.924  1.00 33.15           O  
+ANISOU 2517  OH  TYR B 152     4104   4444   4048    264    554     -5       O  
+ATOM   2518  N   ARG B 153      42.941   7.565  49.732  1.00 26.77           N  
+ANISOU 2518  N   ARG B 153     2825   3749   3598    148    899   1192       N  
+ATOM   2519  CA  ARG B 153      42.272   8.742  49.200  1.00 27.65           C  
+ANISOU 2519  CA  ARG B 153     2891   3868   3748    185    938   1306       C  
+ATOM   2520  C   ARG B 153      41.462   8.279  48.000  1.00 32.60           C  
+ANISOU 2520  C   ARG B 153     3617   4761   4010    549   1017   1145       C  
+ATOM   2521  O   ARG B 153      42.019   7.907  46.967  1.00 37.11           O  
+ANISOU 2521  O   ARG B 153     4126   5614   4361    928   1159   1326       O  
+ATOM   2522  CB  ARG B 153      43.279   9.841  48.826  1.00 30.68           C  
+ANISOU 2522  CB  ARG B 153     2982   4248   4429    197   1042   1846       C  
+ATOM   2523  CG  ARG B 153      42.638  11.195  48.490  1.00 30.94           C  
+ANISOU 2523  CG  ARG B 153     2961   4199   4595    177   1019   1947       C  
+ATOM   2524  CD  ARG B 153      43.666  12.318  48.461  1.00 43.99           C  
+ANISOU 2524  CD  ARG B 153     4345   5697   6671    140    914   2282       C  
+ATOM   2525  NE  ARG B 153      43.917  12.888  49.785  1.00 42.31           N  
+ANISOU 2525  NE  ARG B 153     4154   5117   6806   -202    613   2148       N  
+ATOM   2526  CZ  ARG B 153      44.948  13.680  50.074  1.00 47.21           C  
+ANISOU 2526  CZ  ARG B 153     4535   5555   7846   -262    431   2364       C  
+ATOM   2527  NH1 ARG B 153      45.839  13.988  49.140  1.00 50.24           N1+
+ANISOU 2527  NH1 ARG B 153     4595   6080   8413    -35    561   2783       N1+
+ATOM   2528  NH2 ARG B 153      45.098  14.162  51.302  1.00 48.09           N  
+ANISOU 2528  NH2 ARG B 153     4720   5348   8203   -496    103   2171       N  
+ATOM   2529  N   VAL B 154      40.142   8.297  48.134  1.00 27.51           N  
+ANISOU 2529  N   VAL B 154     3129   4027   3295    484    905    808       N  
+ATOM   2530  CA  VAL B 154      39.289   7.670  47.132  1.00 28.22           C  
+ANISOU 2530  CA  VAL B 154     3334   4294   3095    815    861    550       C  
+ATOM   2531  C   VAL B 154      38.956   8.632  45.995  1.00 32.67           C  
+ANISOU 2531  C   VAL B 154     3847   5061   3506   1104    980    741       C  
+ATOM   2532  O   VAL B 154      39.027   9.851  46.151  1.00 37.10           O  
+ANISOU 2532  O   VAL B 154     4292   5552   4254    949   1072   1017       O  
+ATOM   2533  CB  VAL B 154      37.995   7.135  47.773  1.00 33.73           C  
+ANISOU 2533  CB  VAL B 154     4166   4777   3871    625    669    138       C  
+ATOM   2534  CG1 VAL B 154      38.324   5.986  48.712  1.00 37.70           C  
+ANISOU 2534  CG1 VAL B 154     4704   5130   4489    449    584    -16       C  
+ATOM   2535  CG2 VAL B 154      37.287   8.226  48.524  1.00 30.68           C  
+ANISOU 2535  CG2 VAL B 154     3782   4205   3669    339    675    173       C  
+ATOM   2536  N   ASN B 155      38.605   8.074  44.847  1.00 27.56           N  
+ANISOU 2536  N   ASN B 155     3296   4654   2523   1563    946    586       N  
+ATOM   2537  CA  ASN B 155      38.340   8.874  43.663  1.00 37.01           C  
+ANISOU 2537  CA  ASN B 155     4467   6106   3490   1956   1077    777       C  
+ATOM   2538  C   ASN B 155      36.899   9.371  43.623  1.00 38.09           C  
+ANISOU 2538  C   ASN B 155     4697   6121   3656   1856    933    499       C  
+ATOM   2539  O   ASN B 155      36.612  10.414  43.047  1.00 43.85           O  
+ANISOU 2539  O   ASN B 155     5368   6962   4331   1986   1063    714       O  
+ATOM   2540  CB  ASN B 155      38.685   8.057  42.422  1.00 42.72           C  
+ANISOU 2540  CB  ASN B 155     5320   7052   3858   2466    949    735       C  
+ATOM   2541  CG  ASN B 155      40.071   7.434  42.522  1.00 51.88           C  
+ANISOU 2541  CG  ASN B 155     6412   8289   5011   2540   1041    983       C  
+ATOM   2542  OD1 ASN B 155      40.971   8.005  43.147  1.00 50.03           O  
+ANISOU 2542  OD1 ASN B 155     5966   7982   5059   2284   1238   1363       O  
+ATOM   2543  ND2 ASN B 155      40.241   6.247  41.939  1.00 51.76           N  
+ANISOU 2543  ND2 ASN B 155     6569   8384   4715   2873    849    759       N  
+ATOM   2544  N   GLN B 156      36.002   8.623  44.259  1.00 30.96           N  
+ANISOU 2544  N   GLN B 156     3904   4979   2881   1624    679     70       N  
+ATOM   2545  CA  GLN B 156      34.607   9.028  44.407  1.00 29.22           C  
+ANISOU 2545  CA  GLN B 156     3731   4600   2772   1475    544   -161       C  
+ATOM   2546  C   GLN B 156      34.307   9.201  45.892  1.00 26.34           C  
+ANISOU 2546  C   GLN B 156     3335   3922   2750    948    537   -180       C  
+ATOM   2547  O   GLN B 156      34.419   8.245  46.649  1.00 31.23           O  
+ANISOU 2547  O   GLN B 156     3970   4389   3508    780    443   -327       O  
+ATOM   2548  CB  GLN B 156      33.664   7.983  43.794  1.00 30.61           C  
+ANISOU 2548  CB  GLN B 156     4019   4745   2865   1736    224   -610       C  
+ATOM   2549  CG  GLN B 156      33.695   7.895  42.274  1.00 34.65           C  
+ANISOU 2549  CG  GLN B 156     4630   5547   2988   2321    132   -655       C  
+ATOM   2550  CD  GLN B 156      34.961   7.253  41.729  1.00 43.57           C  
+ANISOU 2550  CD  GLN B 156     5795   6876   3883   2596    165   -475       C  
+ATOM   2551  OE1 GLN B 156      35.438   6.251  42.260  1.00 42.38           O  
+ANISOU 2551  OE1 GLN B 156     5658   6626   3820   2514     82   -617       O  
+ATOM   2552  NE2 GLN B 156      35.519   7.841  40.667  1.00 50.69           N  
+ANISOU 2552  NE2 GLN B 156     6709   8059   4493   2942    291   -129       N  
+ATOM   2553  N   ILE B 157      33.936  10.401  46.326  1.00 21.82           N  
+ANISOU 2553  N   ILE B 157     2733   3261   2298    738    632    -25       N  
+ATOM   2554  CA  ILE B 157      33.739  10.613  47.763  1.00 21.60           C  
+ANISOU 2554  CA  ILE B 157     2723   2972   2514    354    622    -36       C  
+ATOM   2555  C   ILE B 157      32.623   9.746  48.343  1.00 22.82           C  
+ANISOU 2555  C   ILE B 157     2915   2959   2795    253    490   -314       C  
+ATOM   2556  O   ILE B 157      31.644   9.419  47.661  1.00 24.64           O  
+ANISOU 2556  O   ILE B 157     3139   3205   3017    401    368   -504       O  
+ATOM   2557  CB  ILE B 157      33.428  12.079  48.094  1.00 26.10           C  
+ANISOU 2557  CB  ILE B 157     3290   3457   3171    216    689    131       C  
+ATOM   2558  CG1 ILE B 157      32.214  12.544  47.307  1.00 25.59           C  
+ANISOU 2558  CG1 ILE B 157     3244   3467   3011    365    674     30       C  
+ATOM   2559  CG2 ILE B 157      34.617  12.969  47.770  1.00 30.16           C  
+ANISOU 2559  CG2 ILE B 157     3690   4033   3738    241    796    488       C  
+ATOM   2560  CD1 ILE B 157      31.547  13.691  47.962  1.00 31.44           C  
+ANISOU 2560  CD1 ILE B 157     4024   4059   3863    192    695     85       C  
+ATOM   2561  N   ALA B 158      32.781   9.365  49.606  1.00 22.83           N  
+ANISOU 2561  N   ALA B 158     2935   2791   2949     30    505   -310       N  
+ATOM   2562  CA  ALA B 158      31.798   8.496  50.255  1.00 20.43           C  
+ANISOU 2562  CA  ALA B 158     2602   2322   2836    -50    437   -456       C  
+ATOM   2563  C   ALA B 158      30.493   9.237  50.491  1.00 21.48           C  
+ANISOU 2563  C   ALA B 158     2732   2380   3051    -87    467   -448       C  
+ATOM   2564  O   ALA B 158      30.497  10.448  50.751  1.00 20.64           O  
+ANISOU 2564  O   ALA B 158     2700   2289   2853   -127    555   -332       O  
+ATOM   2565  CB  ALA B 158      32.347   7.963  51.573  1.00 24.31           C  
+ANISOU 2565  CB  ALA B 158     3118   2695   3422   -205    500   -387       C  
+ATOM   2566  N   PRO B 159      29.367   8.512  50.396  1.00 19.34           N  
+ANISOU 2566  N   PRO B 159     2351   1997   3001    -66    368   -558       N  
+ATOM   2567  CA  PRO B 159      28.068   9.094  50.771  1.00 22.14           C  
+ANISOU 2567  CA  PRO B 159     2660   2266   3486    -99    427   -495       C  
+ATOM   2568  C   PRO B 159      28.036   9.570  52.234  1.00 21.57           C  
+ANISOU 2568  C   PRO B 159     2668   2132   3396   -185    628   -304       C  
+ATOM   2569  O   PRO B 159      28.789   9.045  53.065  1.00 23.19           O  
+ANISOU 2569  O   PRO B 159     2914   2304   3594   -231    683   -248       O  
+ATOM   2570  CB  PRO B 159      27.087   7.944  50.527  1.00 21.46           C  
+ANISOU 2570  CB  PRO B 159     2368   2011   3773    -80    251   -594       C  
+ATOM   2571  CG  PRO B 159      27.770   7.050  49.534  1.00 24.18           C  
+ANISOU 2571  CG  PRO B 159     2715   2392   4081     44     14   -818       C  
+ATOM   2572  CD  PRO B 159      29.238   7.152  49.843  1.00 22.56           C  
+ANISOU 2572  CD  PRO B 159     2651   2328   3595     15    155   -740       C  
+ATOM   2573  N   GLU B 160      27.200  10.576  52.510  1.00 22.20           N  
+ANISOU 2573  N   GLU B 160     2828   2902   2703   1049    535    584       N  
+ATOM   2574  CA  GLU B 160      27.094  11.209  53.829  1.00 37.36           C  
+ANISOU 2574  CA  GLU B 160     5019   4719   4458   1160    618    638       C  
+ATOM   2575  C   GLU B 160      26.912  10.220  54.979  1.00 33.13           C  
+ANISOU 2575  C   GLU B 160     4568   4123   3899   1175    637    710       C  
+ATOM   2576  O   GLU B 160      27.549  10.351  56.024  1.00 26.59           O  
+ANISOU 2576  O   GLU B 160     3986   3155   2962   1236    591    668       O  
+ATOM   2577  CB  GLU B 160      25.934  12.208  53.832  1.00 47.78           C  
+ANISOU 2577  CB  GLU B 160     6361   6133   5660   1308    834    768       C  
+ATOM   2578  N   SER B 161      26.059   9.221  54.782  1.00 31.54           N  
+ANISOU 2578  N   SER B 161     4151   4016   3818   1122    679    833       N  
+ATOM   2579  CA  SER B 161      25.780   8.249  55.837  1.00 33.63           C  
+ANISOU 2579  CA  SER B 161     4419   4250   4108   1154    707    955       C  
+ATOM   2580  C   SER B 161      27.054   7.546  56.330  1.00 29.55           C  
+ANISOU 2580  C   SER B 161     4014   3613   3599   1059    566    783       C  
+ATOM   2581  O   SER B 161      27.111   7.095  57.469  1.00 31.58           O  
+ANISOU 2581  O   SER B 161     4358   3823   3817   1138    616    836       O  
+ATOM   2582  CB  SER B 161      24.761   7.213  55.356  1.00 36.81           C  
+ANISOU 2582  CB  SER B 161     4526   4749   4713   1054    683   1143       C  
+ATOM   2583  OG  SER B 161      25.329   6.306  54.422  1.00 29.79           O  
+ANISOU 2583  OG  SER B 161     3531   3822   3967    856    463    980       O  
+ATOM   2584  N   LEU B 162      28.084   7.465  55.487  1.00 26.98           N  
+ANISOU 2584  N   LEU B 162     3678   3259   3312    922    410    613       N  
+ATOM   2585  CA  LEU B 162      29.321   6.784  55.877  1.00 23.24           C  
+ANISOU 2585  CA  LEU B 162     3299   2702   2829    830    297    510       C  
+ATOM   2586  C   LEU B 162      30.380   7.713  56.495  1.00 22.38           C  
+ANISOU 2586  C   LEU B 162     3439   2468   2597    861    242    450       C  
+ATOM   2587  O   LEU B 162      31.359   7.243  57.074  1.00 23.46           O  
+ANISOU 2587  O   LEU B 162     3677   2529   2708    791    173    412       O  
+ATOM   2588  CB  LEU B 162      29.937   6.063  54.670  1.00 26.28           C  
+ANISOU 2588  CB  LEU B 162     3563   3131   3292    718    150    439       C  
+ATOM   2589  CG  LEU B 162      29.030   5.065  53.948  1.00 30.25           C  
+ANISOU 2589  CG  LEU B 162     3882   3691   3921    668     94    473       C  
+ATOM   2590  CD1 LEU B 162      29.849   4.270  52.964  1.00 33.53           C  
+ANISOU 2590  CD1 LEU B 162     4301   4107   4333    635    -78    386       C  
+ATOM   2591  CD2 LEU B 162      28.379   4.150  54.952  1.00 38.37           C  
+ANISOU 2591  CD2 LEU B 162     4858   4697   5024    635    141    575       C  
+ATOM   2592  N   ARG B 163      30.212   9.024  56.363  1.00 24.09           N  
+ANISOU 2592  N   ARG B 163     3758   2649   2744    953    247    458       N  
+ATOM   2593  CA  ARG B 163      31.263   9.925  56.842  1.00 23.07           C  
+ANISOU 2593  CA  ARG B 163     3874   2354   2539    951     98    425       C  
+ATOM   2594  C   ARG B 163      31.280   9.982  58.369  1.00 26.58           C  
+ANISOU 2594  C   ARG B 163     4620   2643   2836   1069    112    414       C  
+ATOM   2595  O   ARG B 163      30.253  10.227  59.012  1.00 28.51           O  
+ANISOU 2595  O   ARG B 163     4971   2897   2964   1279    265    465       O  
+ATOM   2596  CB  ARG B 163      31.089  11.324  56.253  1.00 23.43           C  
+ANISOU 2596  CB  ARG B 163     3956   2380   2565   1018     59    440       C  
+ATOM   2597  CG  ARG B 163      31.245  11.358  54.743  1.00 23.13           C  
+ANISOU 2597  CG  ARG B 163     3614   2498   2676    950     37    456       C  
+ATOM   2598  CD  ARG B 163      30.823  12.702  54.157  1.00 26.49           C  
+ANISOU 2598  CD  ARG B 163     4016   2951   3097   1036     64    474       C  
+ATOM   2599  NE  ARG B 163      30.503  12.527  52.749  1.00 24.83           N  
+ANISOU 2599  NE  ARG B 163     3478   2945   3012   1037    136    481       N  
+ATOM   2600  CZ  ARG B 163      29.950  13.445  51.971  1.00 25.90           C  
+ANISOU 2600  CZ  ARG B 163     3482   3185   3173   1112    227    491       C  
+ATOM   2601  NH1 ARG B 163      29.649  14.648  52.442  1.00 27.15           N1+
+ANISOU 2601  NH1 ARG B 163     3825   3260   3231   1186    258    502       N1+
+ATOM   2602  NH2 ARG B 163      29.698  13.150  50.710  1.00 21.39           N  
+ANISOU 2602  NH2 ARG B 163     2619   2796   2711   1136    283    487       N  
+ATOM   2603  N   GLY B 164      32.450   9.730  58.946  1.00 29.91           N  
+ANISOU 2603  N   GLY B 164     5179   2935   3251    967    -38    382       N  
+ATOM   2604  CA  GLY B 164      32.600   9.721  60.389  1.00 33.39           C  
+ANISOU 2604  CA  GLY B 164     5919   3216   3550   1093    -49    351       C  
+ATOM   2605  C   GLY B 164      31.974   8.518  61.077  1.00 34.67           C  
+ANISOU 2605  C   GLY B 164     5964   3495   3715   1181    166    368       C  
+ATOM   2606  O   GLY B 164      31.942   8.453  62.302  1.00 34.88           O  
+ANISOU 2606  O   GLY B 164     6206   3426   3618   1362    207    358       O  
+ATOM   2607  N   LYS B 165      31.491   7.556  60.296  1.00 33.28           N  
+ANISOU 2607  N   LYS B 165     5449   3509   3686   1073    275    405       N  
+ATOM   2608  CA  LYS B 165      30.860   6.358  60.861  1.00 28.64           C  
+ANISOU 2608  CA  LYS B 165     4689   3028   3163   1128    437    467       C  
+ATOM   2609  C   LYS B 165      31.859   5.224  61.032  1.00 22.79           C  
+ANISOU 2609  C   LYS B 165     3874   2297   2487    937    399    399       C  
+ATOM   2610  O   LYS B 165      32.388   4.711  60.049  1.00 23.71           O  
+ANISOU 2610  O   LYS B 165     3853   2472   2683    740    315    370       O  
+ATOM   2611  CB  LYS B 165      29.707   5.878  59.981  1.00 31.03           C  
+ANISOU 2611  CB  LYS B 165     4687   3494   3611   1103    516    580       C  
+ATOM   2612  CG  LYS B 165      29.085   4.574  60.467  1.00 35.71           C  
+ANISOU 2612  CG  LYS B 165     5050   4178   4339   1117    613    700       C  
+ATOM   2613  CD  LYS B 165      27.761   4.278  59.774  1.00 37.99           C  
+ANISOU 2613  CD  LYS B 165     5064   4586   4785   1118    645    896       C  
+ATOM   2614  CE  LYS B 165      27.182   2.953  60.262  1.00 41.52           C  
+ANISOU 2614  CE  LYS B 165     5251   5100   5426   1108    676   1072       C  
+ATOM   2615  NZ  LYS B 165      26.913   2.965  61.728  1.00 46.35           N1+
+ANISOU 2615  NZ  LYS B 165     5908   5733   5968   1400    863   1226       N1+
+ATOM   2616  N   PHE B 166      32.106   4.818  62.271  1.00 24.45           N  
+ANISOU 2616  N   PHE B 166     4187   2462   2640   1035    476    388       N  
+ATOM   2617  CA  PHE B 166      33.108   3.779  62.514  1.00 21.81           C  
+ANISOU 2617  CA  PHE B 166     3795   2150   2342    853    474    330       C  
+ATOM   2618  C   PHE B 166      32.519   2.379  62.350  1.00 23.14           C  
+ANISOU 2618  C   PHE B 166     3657   2469   2667    798    585    380       C  
+ATOM   2619  O   PHE B 166      31.425   2.099  62.839  1.00 23.21           O  
+ANISOU 2619  O   PHE B 166     3523   2542   2755    973    705    496       O  
+ATOM   2620  CB  PHE B 166      33.704   3.931  63.911  1.00 23.43           C  
+ANISOU 2620  CB  PHE B 166     4239   2239   2424    972    503    284       C  
+ATOM   2621  CG  PHE B 166      34.769   2.917  64.226  1.00 26.61           C  
+ANISOU 2621  CG  PHE B 166     4583   2682   2846    780    536    243       C  
+ATOM   2622  CD1 PHE B 166      36.092   3.158  63.881  1.00 28.26           C  
+ANISOU 2622  CD1 PHE B 166     4912   2820   3004    558    382    245       C  
+ATOM   2623  CD2 PHE B 166      34.448   1.721  64.863  1.00 30.46           C  
+ANISOU 2623  CD2 PHE B 166     4870   3293   3410    829    729    253       C  
+ATOM   2624  CE1 PHE B 166      37.079   2.218  64.161  1.00 26.98           C  
+ANISOU 2624  CE1 PHE B 166     4699   2723   2829    390    447    257       C  
+ATOM   2625  CE2 PHE B 166      35.430   0.780  65.150  1.00 25.92           C  
+ANISOU 2625  CE2 PHE B 166     4244   2773   2830    653    792    215       C  
+ATOM   2626  CZ  PHE B 166      36.745   1.032  64.798  1.00 26.24           C  
+ANISOU 2626  CZ  PHE B 166     4435   2755   2781    435    664    216       C  
+ATOM   2627  N   TYR B 167      33.253   1.519  61.659  1.00 21.99           N  
+ANISOU 2627  N   TYR B 167     3421   2374   2561    578    523    335       N  
+ATOM   2628  CA  TYR B 167      32.885   0.120  61.491  1.00 21.73           C  
+ANISOU 2628  CA  TYR B 167     3158   2437   2662    498    561    362       C  
+ATOM   2629  C   TYR B 167      33.956  -0.776  62.067  1.00 23.60           C  
+ANISOU 2629  C   TYR B 167     3425   2701   2840    390    634    306       C  
+ATOM   2630  O   TYR B 167      35.115  -0.665  61.672  1.00 25.22           O  
+ANISOU 2630  O   TYR B 167     3770   2892   2919    268    575    277       O  
+ATOM   2631  CB  TYR B 167      32.713  -0.242  60.013  1.00 22.09           C  
+ANISOU 2631  CB  TYR B 167     3121   2508   2763    378    398    357       C  
+ATOM   2632  CG  TYR B 167      31.491   0.316  59.345  1.00 24.97           C  
+ANISOU 2632  CG  TYR B 167     3381   2877   3230    450    336    432       C  
+ATOM   2633  CD1 TYR B 167      31.497   1.595  58.805  1.00 26.47           C  
+ANISOU 2633  CD1 TYR B 167     3677   3040   3340    507    300    416       C  
+ATOM   2634  CD2 TYR B 167      30.330  -0.441  59.236  1.00 32.86           C  
+ANISOU 2634  CD2 TYR B 167     4154   3907   4425    447    300    554       C  
+ATOM   2635  CE1 TYR B 167      30.379   2.114  58.184  1.00 32.45           C  
+ANISOU 2635  CE1 TYR B 167     4330   3824   4175    569    279    495       C  
+ATOM   2636  CE2 TYR B 167      29.205   0.070  58.612  1.00 36.32           C  
+ANISOU 2636  CE2 TYR B 167     4483   4358   4959    494    245    673       C  
+ATOM   2637  CZ  TYR B 167      29.238   1.348  58.088  1.00 35.28           C  
+ANISOU 2637  CZ  TYR B 167     4472   4223   4711    558    258    629       C  
+ATOM   2638  OH  TYR B 167      28.130   1.871  57.470  1.00 40.23           O  
+ANISOU 2638  OH  TYR B 167     4983   4887   5416    603    241    754       O  
+ATOM   2639  N   SER B 168      33.577  -1.673  62.971  1.00 18.70           N  
+ANISOU 2639  N   SER B 168     2647   2139   2319    445    774    336       N  
+ATOM   2640  CA  SER B 168      34.451  -2.761  63.380  1.00 16.56           C  
+ANISOU 2640  CA  SER B 168     2346   1931   2017    323    867    287       C  
+ATOM   2641  C   SER B 168      34.366  -3.834  62.294  1.00 20.01           C  
+ANISOU 2641  C   SER B 168     2683   2403   2516    172    741    288       C  
+ATOM   2642  O   SER B 168      33.296  -4.046  61.723  1.00 23.47           O  
+ANISOU 2642  O   SER B 168     2976   2824   3119    190    615    350       O  
+ATOM   2643  CB  SER B 168      34.037  -3.353  64.736  1.00 20.98           C  
+ANISOU 2643  CB  SER B 168     2735   2554   2681    470   1071    328       C  
+ATOM   2644  OG  SER B 168      34.216  -2.431  65.802  1.00 32.60           O  
+ANISOU 2644  OG  SER B 168     4376   3969   4040    670   1170    309       O  
+ATOM   2645  N   LEU B 169      35.475  -4.496  61.992  1.00 19.46           N  
+ANISOU 2645  N   LEU B 169     2721   2374   2298     43    753    245       N  
+ATOM   2646  CA  LEU B 169      35.431  -5.584  61.011  1.00 19.56           C  
+ANISOU 2646  CA  LEU B 169     2726   2396   2311    -38    611    238       C  
+ATOM   2647  C   LEU B 169      34.524  -6.731  61.479  1.00 17.90           C  
+ANISOU 2647  C   LEU B 169     2271   2193   2338    -56    607    264       C  
+ATOM   2648  O   LEU B 169      34.007  -7.494  60.658  1.00 21.85           O  
+ANISOU 2648  O   LEU B 169     2747   2631   2926   -106    384    275       O  
+ATOM   2649  CB  LEU B 169      36.834  -6.115  60.725  1.00 20.91           C  
+ANISOU 2649  CB  LEU B 169     3088   2634   2224   -110    672    241       C  
+ATOM   2650  CG  LEU B 169      37.890  -5.150  60.170  1.00 21.89           C  
+ANISOU 2650  CG  LEU B 169     3412   2770   2136    -92    649    325       C  
+ATOM   2651  CD1 LEU B 169      39.026  -5.951  59.511  1.00 26.09           C  
+ANISOU 2651  CD1 LEU B 169     3887   3419   2607    -85    499    341       C  
+ATOM   2652  CD2 LEU B 169      37.293  -4.146  59.208  1.00 23.43           C  
+ANISOU 2652  CD2 LEU B 169     3624   2892   2386     -5    457    333       C  
+ATOM   2653  N   SER B 170      34.298  -6.844  62.783  1.00 19.09           N  
+ANISOU 2653  N   SER B 170     2238   2407   2609      7    818    301       N  
+ATOM   2654  CA  SER B 170      33.474  -7.953  63.271  1.00 20.24           C  
+ANISOU 2654  CA  SER B 170     2085   2582   3025      8    817    394       C  
+ATOM   2655  C   SER B 170      32.014  -7.777  62.890  1.00 20.10           C  
+ANISOU 2655  C   SER B 170     1859   2496   3281     67    617    565       C  
+ATOM   2656  O   SER B 170      31.221  -8.699  63.043  1.00 23.02           O  
+ANISOU 2656  O   SER B 170     1958   2859   3930     39    513    717       O  
+ATOM   2657  CB  SER B 170      33.597  -8.108  64.782  1.00 24.47           C  
+ANISOU 2657  CB  SER B 170     2526   3212   3557    115    975    373       C  
+ATOM   2658  OG  SER B 170      33.445  -6.854  65.425  1.00 25.58           O  
+ANISOU 2658  OG  SER B 170     2752   3333   3633    282   1044    386       O  
+ATOM   2659  N   SER B 171      31.658  -6.583  62.424  1.00 28.08           N  
+ANISOU 2659  N   SER B 171     2979   3463   4228    143    559    580       N  
+ATOM   2660  CA  SER B 171      30.307  -6.322  61.946  1.00 30.00           C  
+ANISOU 2660  CA  SER B 171     3045   3657   4695    186    382    774       C  
+ATOM   2661  C   SER B 171      30.146  -6.754  60.489  1.00 28.30           C  
+ANISOU 2661  C   SER B 171     2936   3321   4496     21     39    719       C  
+ATOM   2662  O   SER B 171      29.030  -6.813  59.971  1.00 31.17           O  
+ANISOU 2662  O   SER B 171     3143   3620   5081     -3   -177    892       O  
+ATOM   2663  CB  SER B 171      29.971  -4.832  62.087  1.00 33.94           C  
+ANISOU 2663  CB  SER B 171     3634   4172   5090    362    493    815       C  
+ATOM   2664  OG  SER B 171      29.961  -4.444  63.451  1.00 32.92           O  
+ANISOU 2664  OG  SER B 171     3454   4121   4933    589    761    888       O  
+ATOM   2665  N   VAL B 172      31.270  -7.055  59.843  1.00 23.25           N  
+ANISOU 2665  N   VAL B 172     2669   2931   3233    566    393    969       N  
+ATOM   2666  CA  VAL B 172      31.337  -7.229  58.402  1.00 22.78           C  
+ANISOU 2666  CA  VAL B 172     2281   3116   3256    497    231    959       C  
+ATOM   2667  C   VAL B 172      31.693  -8.654  57.959  1.00 27.22           C  
+ANISOU 2667  C   VAL B 172     2717   3784   3842    377     69    850       C  
+ATOM   2668  O   VAL B 172      31.133  -9.165  56.981  1.00 34.78           O  
+ANISOU 2668  O   VAL B 172     3412   4908   4896    334     -1    863       O  
+ATOM   2669  CB  VAL B 172      32.370  -6.248  57.802  1.00 28.46           C  
+ANISOU 2669  CB  VAL B 172     3037   3879   3896    493     77    945       C  
+ATOM   2670  CG1 VAL B 172      32.621  -6.551  56.349  1.00 36.13           C  
+ANISOU 2670  CG1 VAL B 172     3696   5105   4926    453   -101    928       C  
+ATOM   2671  CG2 VAL B 172      31.909  -4.826  57.986  1.00 27.19           C  
+ANISOU 2671  CG2 VAL B 172     2973   3631   3726    609    228   1055       C  
+ATOM   2672  N   TYR B 173      32.601  -9.306  58.681  1.00 24.31           N  
+ANISOU 2672  N   TYR B 173     2553   3310   3373    322     10    754       N  
+ATOM   2673  CA  TYR B 173      33.091 -10.623  58.267  1.00 21.89           C  
+ANISOU 2673  CA  TYR B 173     2177   3087   3055    231   -127    657       C  
+ATOM   2674  C   TYR B 173      32.599 -11.745  59.159  1.00 24.31           C  
+ANISOU 2674  C   TYR B 173     2538   3289   3410    195    -26    621       C  
+ATOM   2675  O   TYR B 173      32.415 -11.556  60.355  1.00 27.27           O  
+ANISOU 2675  O   TYR B 173     3088   3504   3768    245    127    647       O  
+ATOM   2676  CB  TYR B 173      34.615 -10.617  58.215  1.00 18.55           C  
+ANISOU 2676  CB  TYR B 173     1890   2675   2484    200   -275    620       C  
+ATOM   2677  CG  TYR B 173      35.074  -9.588  57.226  1.00 22.38           C  
+ANISOU 2677  CG  TYR B 173     2268   3285   2951    245   -393    688       C  
+ATOM   2678  CD1 TYR B 173      34.795  -9.749  55.871  1.00 28.98           C  
+ANISOU 2678  CD1 TYR B 173     2909   4273   3830    256   -455    641       C  
+ATOM   2679  CD2 TYR B 173      35.727  -8.435  57.636  1.00 29.11           C  
+ANISOU 2679  CD2 TYR B 173     3271   4053   3735    259   -422    760       C  
+ATOM   2680  CE1 TYR B 173      35.178  -8.795  54.944  1.00 24.95           C  
+ANISOU 2680  CE1 TYR B 173     2423   3760   3295    271   -461    583       C  
+ATOM   2681  CE2 TYR B 173      36.124  -7.476  56.713  1.00 24.61           C  
+ANISOU 2681  CE2 TYR B 173     2622   3559   3170    279   -488    768       C  
+ATOM   2682  CZ  TYR B 173      35.838  -7.661  55.373  1.00 27.81           C  
+ANISOU 2682  CZ  TYR B 173     2885   4061   3620    282   -469    647       C  
+ATOM   2683  OH  TYR B 173      36.220  -6.714  54.441  1.00 28.63           O  
+ANISOU 2683  OH  TYR B 173     2991   4161   3725    291   -471    592       O  
+ATOM   2684  N   ARG B 174      32.386 -12.912  58.555  1.00 20.72           N  
+ANISOU 2684  N   ARG B 174     1948   2916   3008    118   -118    565       N  
+ATOM   2685  CA  ARG B 174      31.792 -14.047  59.261  1.00 24.30           C  
+ANISOU 2685  CA  ARG B 174     2402   3283   3546     71    -42    550       C  
+ATOM   2686  C   ARG B 174      32.832 -14.905  59.981  1.00 23.96           C  
+ANISOU 2686  C   ARG B 174     2551   3160   3394     37    -46    447       C  
+ATOM   2687  O   ARG B 174      33.929 -15.117  59.471  1.00 21.35           O  
+ANISOU 2687  O   ARG B 174     2286   2893   2935     15   -166    386       O  
+ATOM   2688  CB  ARG B 174      30.993 -14.911  58.286  1.00 25.86           C  
+ANISOU 2688  CB  ARG B 174     2390   3579   3857    -24   -166    553       C  
+ATOM   2689  CG  ARG B 174      30.249 -16.082  58.953  1.00 32.00           C  
+ANISOU 2689  CG  ARG B 174     3132   4267   4761    -91   -115    577       C  
+ATOM   2690  CD  ARG B 174      29.260 -16.744  58.007  1.00 39.26           C  
+ANISOU 2690  CD  ARG B 174     3842   5262   5811   -217   -268    633       C  
+ATOM   2691  NE  ARG B 174      28.580 -17.859  58.664  1.00 45.58           N  
+ANISOU 2691  NE  ARG B 174     4599   5967   6751   -295   -245    686       N  
+ATOM   2692  CZ  ARG B 174      27.582 -18.555  58.129  1.00 45.31           C  
+ANISOU 2692  CZ  ARG B 174     4391   5957   6867   -438   -386    785       C  
+ATOM   2693  NH1 ARG B 174      27.134 -18.253  56.917  1.00 45.52           N1+
+ANISOU 2693  NH1 ARG B 174     4281   6107   6907   -519   -556    830       N1+
+ATOM   2694  NH2 ARG B 174      27.031 -19.553  58.809  1.00 46.80           N  
+ANISOU 2694  NH2 ARG B 174     4536   6049   7197   -507   -371    856       N  
+ATOM   2695  N   VAL B 175      32.471 -15.398  61.166  1.00 20.73           N  
+ANISOU 2695  N   VAL B 175     2215   2625   3038     52    103    460       N  
+ATOM   2696  CA  VAL B 175      33.346 -16.257  61.952  1.00 17.92           C  
+ANISOU 2696  CA  VAL B 175     2014   2199   2594     20    133    380       C  
+ATOM   2697  C   VAL B 175      32.657 -17.611  62.199  1.00 18.31           C  
+ANISOU 2697  C   VAL B 175     1963   2215   2777    -32    170    360       C  
+ATOM   2698  O   VAL B 175      31.468 -17.665  62.566  1.00 19.73           O  
+ANISOU 2698  O   VAL B 175     2018   2354   3124     -2    262    462       O  
+ATOM   2699  CB  VAL B 175      33.726 -15.601  63.307  1.00 24.91           C  
+ANISOU 2699  CB  VAL B 175     3120   2949   3396     91    276    408       C  
+ATOM   2700  CG1 VAL B 175      34.357 -16.620  64.241  1.00 25.43           C  
+ANISOU 2700  CG1 VAL B 175     3296   2955   3413     57    344    351       C  
+ATOM   2701  CG2 VAL B 175      34.677 -14.419  63.082  1.00 21.01           C  
+ANISOU 2701  CG2 VAL B 175     2768   2467   2749     94    181    426       C  
+ATOM   2702  N   TYR B 176      33.400 -18.689  61.956  1.00 15.85           N  
+ANISOU 2702  N   TYR B 176     1704   1923   2394   -102     99    264       N  
+ATOM   2703  CA  TYR B 176      32.954 -20.054  62.214  1.00 20.12           C  
+ANISOU 2703  CA  TYR B 176     2194   2412   3041   -164    119    230       C  
+ATOM   2704  C   TYR B 176      33.773 -20.674  63.343  1.00 21.27           C  
+ANISOU 2704  C   TYR B 176     2479   2490   3112   -145    258    189       C  
+ATOM   2705  O   TYR B 176      34.839 -20.158  63.679  1.00 17.18           O  
+ANISOU 2705  O   TYR B 176     2107   1990   2432   -114    287    185       O  
+ATOM   2706  CB  TYR B 176      33.125 -20.938  60.976  1.00 20.74           C  
+ANISOU 2706  CB  TYR B 176     2264   2544   3073   -252    -66    146       C  
+ATOM   2707  CG  TYR B 176      32.381 -20.539  59.737  1.00 17.84           C  
+ANISOU 2707  CG  TYR B 176     1764   2253   2760   -296   -237    173       C  
+ATOM   2708  CD1 TYR B 176      31.132 -21.083  59.452  1.00 21.21           C  
+ANISOU 2708  CD1 TYR B 176     2036   2653   3371   -399   -322    231       C  
+ATOM   2709  CD2 TYR B 176      32.947 -19.645  58.809  1.00 19.71           C  
+ANISOU 2709  CD2 TYR B 176     2017   2603   2869   -243   -331    166       C  
+ATOM   2710  CE1 TYR B 176      30.454 -20.734  58.301  1.00 29.09           C  
+ANISOU 2710  CE1 TYR B 176     2908   3735   4412   -461   -493    275       C  
+ATOM   2711  CE2 TYR B 176      32.278 -19.303  57.654  1.00 23.00           C  
+ANISOU 2711  CE2 TYR B 176     2301   3107   3330   -277   -483    191       C  
+ATOM   2712  CZ  TYR B 176      31.033 -19.846  57.404  1.00 27.90           C  
+ANISOU 2712  CZ  TYR B 176     2779   3700   4121   -393   -564    241       C  
+ATOM   2713  OH  TYR B 176      30.350 -19.508  56.256  1.00 31.78           O  
+ANISOU 2713  OH  TYR B 176     3132   4290   4653   -450   -728    287       O  
+ATOM   2714  N   ASP B 177      33.296 -21.796  63.895  1.00 18.92           N  
+ANISOU 2714  N   ASP B 177     2124   2126   2938   -175    330    181       N  
+ATOM   2715  CA  ASP B 177      34.132 -22.641  64.752  1.00 16.85           C  
+ANISOU 2715  CA  ASP B 177     1971   1828   2603   -172    453    131       C  
+ATOM   2716  C   ASP B 177      34.340 -23.988  64.068  1.00 18.06           C  
+ANISOU 2716  C   ASP B 177     2138   1981   2742   -256    370     50       C  
+ATOM   2717  O   ASP B 177      33.373 -24.588  63.615  1.00 17.83           O  
+ANISOU 2717  O   ASP B 177     1998   1910   2867   -327    274     51       O  
+ATOM   2718  CB  ASP B 177      33.503 -22.855  66.131  1.00 18.38           C  
+ANISOU 2718  CB  ASP B 177     2108   1933   2942   -102    645    196       C  
+ATOM   2719  CG  ASP B 177      34.356 -23.745  67.013  1.00 20.32           C  
+ANISOU 2719  CG  ASP B 177     2440   2160   3119   -100    782    149       C  
+ATOM   2720  OD1 ASP B 177      35.377 -23.247  67.540  1.00 21.98           O  
+ANISOU 2720  OD1 ASP B 177     2804   2393   3155    -75    842    148       O  
+ATOM   2721  OD2 ASP B 177      34.023 -24.948  67.164  1.00 21.03           O1-
+ANISOU 2721  OD2 ASP B 177     2444   2217   3332   -138    819    131       O1-
+ATOM   2722  N   TRP B 178      35.585 -24.452  63.973  1.00 16.02           N  
+ANISOU 2722  N   TRP B 178     2030   1764   2291   -248    400      7       N  
+ATOM   2723  CA  TRP B 178      35.874 -25.707  63.257  1.00 16.21           C  
+ANISOU 2723  CA  TRP B 178     2139   1770   2249   -291    342    -66       C  
+ATOM   2724  C   TRP B 178      35.026 -26.876  63.768  1.00 18.74           C  
+ANISOU 2724  C   TRP B 178     2380   1976   2764   -356    388    -95       C  
+ATOM   2725  O   TRP B 178      34.468 -27.657  62.988  1.00 21.11           O  
+ANISOU 2725  O   TRP B 178     2696   2209   3115   -439    240   -147       O  
+ATOM   2726  CB  TRP B 178      37.364 -26.060  63.371  1.00 13.80           C  
+ANISOU 2726  CB  TRP B 178     2000   1533   1712   -233    447    -42       C  
+ATOM   2727  CG  TRP B 178      37.722 -27.224  62.533  1.00 17.26           C  
+ANISOU 2727  CG  TRP B 178     2584   1944   2030   -226    409    -98       C  
+ATOM   2728  CD1 TRP B 178      37.987 -28.491  62.961  1.00 23.63           C  
+ANISOU 2728  CD1 TRP B 178     3472   2686   2821   -230    543   -126       C  
+ATOM   2729  CD2 TRP B 178      37.800 -27.253  61.111  1.00 19.25           C  
+ANISOU 2729  CD2 TRP B 178     2951   2212   2150   -197    228   -134       C  
+ATOM   2730  NE1 TRP B 178      38.260 -29.298  61.888  1.00 20.44           N  
+ANISOU 2730  NE1 TRP B 178     3266   2240   2261   -200    461   -178       N  
+ATOM   2731  CE2 TRP B 178      38.151 -28.564  60.741  1.00 18.99           C  
+ANISOU 2731  CE2 TRP B 178     3115   2104   1997   -173    263   -186       C  
+ATOM   2732  CE3 TRP B 178      37.635 -26.291  60.110  1.00 22.37           C  
+ANISOU 2732  CE3 TRP B 178     3315   2679   2504   -172     51   -123       C  
+ATOM   2733  CZ2 TRP B 178      38.332 -28.938  59.416  1.00 22.34           C  
+ANISOU 2733  CZ2 TRP B 178     3745   2503   2238   -112    119   -232       C  
+ATOM   2734  CZ3 TRP B 178      37.814 -26.667  58.793  1.00 21.94           C  
+ANISOU 2734  CZ3 TRP B 178     3420   2625   2290   -116    -93   -165       C  
+ATOM   2735  CH2 TRP B 178      38.150 -27.984  58.460  1.00 22.39           C  
+ANISOU 2735  CH2 TRP B 178     3711   2587   2207    -82    -62   -222       C  
+ATOM   2736  N   VAL B 179      34.907 -26.991  65.082  1.00 16.32           N  
+ANISOU 2736  N   VAL B 179     1994   1640   2566   -319    577    -49       N  
+ATOM   2737  CA  VAL B 179      34.138 -28.095  65.660  1.00 22.75           C  
+ANISOU 2737  CA  VAL B 179     2697   2358   3590   -362    636    -42       C  
+ATOM   2738  C   VAL B 179      32.622 -27.872  65.598  1.00 23.81           C  
+ANISOU 2738  C   VAL B 179     2618   2439   3988   -407    529     54       C  
+ATOM   2739  O   VAL B 179      31.889 -28.707  65.065  1.00 22.36           O  
+ANISOU 2739  O   VAL B 179     2375   2183   3939   -523    378     58       O  
+ATOM   2740  CB  VAL B 179      34.548 -28.344  67.114  1.00 21.70           C  
+ANISOU 2740  CB  VAL B 179     2534   2226   3486   -280    893     -5       C  
+ATOM   2741  CG1 VAL B 179      33.593 -29.329  67.779  1.00 25.33           C  
+ANISOU 2741  CG1 VAL B 179     2819   2596   4211   -297    957     42       C  
+ATOM   2742  CG2 VAL B 179      35.976 -28.834  67.161  1.00 21.41           C  
+ANISOU 2742  CG2 VAL B 179     2671   2249   3213   -264   1002    -48       C  
+ATOM   2743  N   ALA B 180      32.153 -26.746  66.128  1.00 23.78           N  
+ANISOU 2743  N   ALA B 180     2516   2469   4050   -314    601    159       N  
+ATOM   2744  CA  ALA B 180      30.716 -26.496  66.225  1.00 22.01           C  
+ANISOU 2744  CA  ALA B 180     2067   2216   4079   -313    559    327       C  
+ATOM   2745  C   ALA B 180      30.028 -26.404  64.855  1.00 20.95           C  
+ANISOU 2745  C   ALA B 180     1870   2100   3991   -454    291    348       C  
+ATOM   2746  O   ALA B 180      28.860 -26.780  64.713  1.00 23.85           O  
+ANISOU 2746  O   ALA B 180     2041   2433   4588   -537    186    500       O  
+ATOM   2747  CB  ALA B 180      30.462 -25.221  67.026  1.00 23.74           C  
+ANISOU 2747  CB  ALA B 180     2262   2458   4299   -141    723    443       C  
+ATOM   2748  N   ASP B 181      30.746 -25.899  63.853  1.00 23.18           N  
+ANISOU 2748  N   ASP B 181     2305   2445   4059   -480    171    227       N  
+ATOM   2749  CA  ASP B 181      30.137 -25.670  62.545  1.00 21.61           C  
+ANISOU 2749  CA  ASP B 181     2054   2279   3876   -593    -77    245       C  
+ATOM   2750  C   ASP B 181      30.524 -26.769  61.540  1.00 26.06           C  
+ANISOU 2750  C   ASP B 181     2791   2786   4326   -723   -278     96       C  
+ATOM   2751  O   ASP B 181      30.232 -26.661  60.347  1.00 26.99           O  
+ANISOU 2751  O   ASP B 181     2937   2925   4394   -814   -505     71       O  
+ATOM   2752  CB  ASP B 181      30.509 -24.278  62.027  1.00 21.98           C  
+ANISOU 2752  CB  ASP B 181     2135   2436   3781   -509    -82    239       C  
+ATOM   2753  CG  ASP B 181      29.889 -23.174  62.867  1.00 27.10           C  
+ANISOU 2753  CG  ASP B 181     2650   3106   4539   -385     89    404       C  
+ATOM   2754  OD1 ASP B 181      28.674 -23.271  63.151  1.00 27.43           O  
+ANISOU 2754  OD1 ASP B 181     2487   3127   4807   -399    103    592       O  
+ATOM   2755  OD2 ASP B 181      30.613 -22.239  63.264  1.00 22.41           O1-
+ANISOU 2755  OD2 ASP B 181     2174   2540   3802   -268    209    372       O1-
+ATOM   2756  N   ASP B 182      31.136 -27.836  62.056  1.00 22.90           N  
+ANISOU 2756  N   ASP B 182     2519   2304   3877   -720   -183      8       N  
+ATOM   2757  CA  ASP B 182      31.406 -29.057  61.291  1.00 23.03           C  
+ANISOU 2757  CA  ASP B 182     2743   2217   3791   -824   -338   -118       C  
+ATOM   2758  C   ASP B 182      32.284 -28.779  60.059  1.00 24.78           C  
+ANISOU 2758  C   ASP B 182     3208   2491   3715   -774   -451   -238       C  
+ATOM   2759  O   ASP B 182      31.934 -29.150  58.937  1.00 26.29           O  
+ANISOU 2759  O   ASP B 182     3518   2625   3847   -873   -698   -294       O  
+ATOM   2760  CB  ASP B 182      30.094 -29.720  60.871  1.00 27.95           C  
+ANISOU 2760  CB  ASP B 182     3252   2732   4636  -1026   -586    -37       C  
+ATOM   2761  CG  ASP B 182      30.291 -31.155  60.407  1.00 37.02           C  
+ANISOU 2761  CG  ASP B 182     4650   3710   5705  -1142   -726   -162       C  
+ATOM   2762  OD1 ASP B 182      31.379 -31.717  60.663  1.00 39.84           O  
+ANISOU 2762  OD1 ASP B 182     5226   4039   5872  -1035   -554   -284       O  
+ATOM   2763  OD2 ASP B 182      29.362 -31.713  59.781  1.00 41.21           O1-
+ANISOU 2763  OD2 ASP B 182     5174   4130   6354  -1344  -1009   -120       O1-
+ATOM   2764  N   GLY B 183      33.421 -28.127  60.285  1.00 23.10           N  
+ANISOU 2764  N   GLY B 183     2298   2531   3948   -202   -853   -392       N  
+ATOM   2765  CA  GLY B 183      34.356 -27.802  59.215  1.00 23.06           C  
+ANISOU 2765  CA  GLY B 183     2454   2560   3747   -183   -614   -415       C  
+ATOM   2766  C   GLY B 183      34.816 -29.014  58.416  1.00 26.03           C  
+ANISOU 2766  C   GLY B 183     2912   2801   4175   -216   -348   -629       C  
+ATOM   2767  O   GLY B 183      35.082 -28.911  57.217  1.00 28.38           O  
+ANISOU 2767  O   GLY B 183     3469   3090   4222   -281   -193   -754       O  
+ATOM   2768  N   TYR B 184      34.899 -30.167  59.076  1.00 23.63           N  
+ANISOU 2768  N   TYR B 184     2402   2361   4217   -207   -216   -667       N  
+ATOM   2769  CA  TYR B 184      35.339 -31.403  58.417  1.00 26.15           C  
+ANISOU 2769  CA  TYR B 184     2814   2458   4663   -264    259   -834       C  
+ATOM   2770  C   TYR B 184      34.427 -31.811  57.263  1.00 28.56           C  
+ANISOU 2770  C   TYR B 184     3513   2823   4518   -501    286  -1182       C  
+ATOM   2771  O   TYR B 184      34.837 -32.549  56.365  1.00 31.69           O  
+ANISOU 2771  O   TYR B 184     4179   3004   4859   -698    787  -1360       O  
+ATOM   2772  CB  TYR B 184      35.403 -32.560  59.423  1.00 31.31           C  
+ANISOU 2772  CB  TYR B 184     3103   2997   5796   -185    453   -780       C  
+ATOM   2773  CG  TYR B 184      36.661 -32.601  60.261  1.00 37.80           C  
+ANISOU 2773  CG  TYR B 184     3492   3762   7109    -97    682   -316       C  
+ATOM   2774  CD1 TYR B 184      37.914 -32.494  59.676  1.00 44.13           C  
+ANISOU 2774  CD1 TYR B 184     4338   4395   8034    -81   1108    -43       C  
+ATOM   2775  CD2 TYR B 184      36.592 -32.734  61.643  1.00 41.81           C  
+ANISOU 2775  CD2 TYR B 184     3796   4411   7679    -64    404    -79       C  
+ATOM   2776  CE1 TYR B 184      39.065 -32.528  60.445  1.00 46.08           C  
+ANISOU 2776  CE1 TYR B 184     4328   4683   8497    -11   1185    501       C  
+ATOM   2777  CE2 TYR B 184      37.736 -32.770  62.415  1.00 39.55           C  
+ANISOU 2777  CE2 TYR B 184     3497   4203   7326    -52    463    372       C  
+ATOM   2778  CZ  TYR B 184      38.968 -32.662  61.813  1.00 41.06           C  
+ANISOU 2778  CZ  TYR B 184     3635   4288   7678    -12    789    671       C  
+ATOM   2779  OH  TYR B 184      40.110 -32.707  62.581  1.00 49.72           O  
+ANISOU 2779  OH  TYR B 184     4690   5505   8696     20    752   1101       O  
+ATOM   2780  N   ASN B 185      33.180 -31.357  57.307  1.00 27.52           N  
+ANISOU 2780  N   ASN B 185     3418   2977   4062   -558   -194  -1215       N  
+ATOM   2781  CA  ASN B 185      32.213 -31.727  56.284  1.00 30.19           C  
+ANISOU 2781  CA  ASN B 185     4064   3522   3886   -901   -242  -1417       C  
+ATOM   2782  C   ASN B 185      31.712 -30.527  55.497  1.00 35.67           C  
+ANISOU 2782  C   ASN B 185     4849   4552   4153  -1023   -574  -1217       C  
+ATOM   2783  O   ASN B 185      31.002 -30.692  54.507  1.00 41.39           O  
+ANISOU 2783  O   ASN B 185     5786   5559   4382  -1425   -634  -1263       O  
+ATOM   2784  CB  ASN B 185      31.023 -32.464  56.917  1.00 31.72           C  
+ANISOU 2784  CB  ASN B 185     4177   3836   4040   -916   -487  -1518       C  
+ATOM   2785  CG  ASN B 185      31.409 -33.818  57.471  1.00 37.72           C  
+ANISOU 2785  CG  ASN B 185     4853   4312   5165   -843    -47  -1764       C  
+ATOM   2786  OD1 ASN B 185      31.978 -34.642  56.763  1.00 39.81           O  
+ANISOU 2786  OD1 ASN B 185     5354   4377   5394  -1070    571  -1968       O  
+ATOM   2787  ND2 ASN B 185      31.115 -34.050  58.750  1.00 41.50           N  
+ANISOU 2787  ND2 ASN B 185     4993   4744   6029   -538   -280  -1694       N  
+ATOM   2788  N   LYS B 186      32.093 -29.323  55.921  1.00 28.84           N  
+ANISOU 2788  N   LYS B 186     3807   3695   3456   -739   -726   -955       N  
+ATOM   2789  CA  LYS B 186      31.478 -28.117  55.377  1.00 33.40           C  
+ANISOU 2789  CA  LYS B 186     4358   4597   3734   -766   -969   -668       C  
+ATOM   2790  C   LYS B 186      32.453 -27.057  54.875  1.00 29.10           C  
+ANISOU 2790  C   LYS B 186     3852   4032   3172   -633   -810   -604       C  
+ATOM   2791  O   LYS B 186      32.025 -26.073  54.280  1.00 29.81           O  
+ANISOU 2791  O   LYS B 186     3889   4408   3030   -647   -910   -365       O  
+ATOM   2792  CB  LYS B 186      30.567 -27.480  56.433  1.00 26.77           C  
+ANISOU 2792  CB  LYS B 186     3285   3804   3081   -556  -1238   -334       C  
+ATOM   2793  CG  LYS B 186      29.306 -28.281  56.721  1.00 28.96           C  
+ANISOU 2793  CG  LYS B 186     3532   4192   3281   -673  -1505   -305       C  
+ATOM   2794  CD  LYS B 186      28.434 -28.443  55.481  1.00 34.96           C  
+ANISOU 2794  CD  LYS B 186     4391   5406   3488  -1071  -1645   -164       C  
+ATOM   2795  CE  LYS B 186      27.120 -29.124  55.835  1.00 41.26           C  
+ANISOU 2795  CE  LYS B 186     5149   6241   4288  -1012  -1725    -69       C  
+ATOM   2796  NZ  LYS B 186      26.255 -29.377  54.650  1.00 44.74           N1+
+ANISOU 2796  NZ  LYS B 186     5677   7061   4261  -1406  -1724    135       N1+
+ATOM   2797  N   PHE B 187      33.745 -27.253  55.111  1.00 29.49           N  
+ANISOU 2797  N   PHE B 187     3955   3770   3479   -493   -539   -754       N  
+ATOM   2798  CA  PHE B 187      34.751 -26.227  54.812  1.00 30.53           C  
+ANISOU 2798  CA  PHE B 187     4133   3865   3604   -314   -403   -693       C  
+ATOM   2799  C   PHE B 187      34.669 -25.699  53.371  1.00 31.62           C  
+ANISOU 2799  C   PHE B 187     4444   4203   3368   -459   -409   -762       C  
+ATOM   2800  O   PHE B 187      34.757 -24.487  53.155  1.00 31.30           O  
+ANISOU 2800  O   PHE B 187     4332   4339   3222   -283   -431   -607       O  
+ATOM   2801  CB  PHE B 187      36.152 -26.778  55.100  1.00 31.10           C  
+ANISOU 2801  CB  PHE B 187     4243   3585   3988   -217    -98   -760       C  
+ATOM   2802  CG  PHE B 187      37.237 -25.734  55.130  1.00 30.96           C  
+ANISOU 2802  CG  PHE B 187     4243   3546   3973    -10      4   -634       C  
+ATOM   2803  CD1 PHE B 187      36.940 -24.389  55.229  1.00 35.22           C  
+ANISOU 2803  CD1 PHE B 187     4745   4337   4301    106   -102   -513       C  
+ATOM   2804  CD2 PHE B 187      38.563 -26.109  55.054  1.00 41.01           C  
+ANISOU 2804  CD2 PHE B 187     5575   4535   5471     64    286   -587       C  
+ATOM   2805  CE1 PHE B 187      37.951 -23.436  55.251  1.00 32.26           C  
+ANISOU 2805  CE1 PHE B 187     4435   3967   3855    269     49   -445       C  
+ATOM   2806  CE2 PHE B 187      39.571 -25.159  55.079  1.00 41.60           C  
+ANISOU 2806  CE2 PHE B 187     5688   4631   5486    237    354   -449       C  
+ATOM   2807  CZ  PHE B 187      39.259 -23.820  55.171  1.00 31.61           C  
+ANISOU 2807  CZ  PHE B 187     4430   3657   3924    328    223   -430       C  
+ATOM   2808  N   SER B 188      34.478 -26.590  52.397  1.00 32.47           N  
+ANISOU 2808  N   SER B 188     4781   4296   3258   -840   -333   -987       N  
+ATOM   2809  CA  SER B 188      34.378 -26.183  50.995  1.00 34.93           C  
+ANISOU 2809  CA  SER B 188     5259   4833   3179  -1138   -355  -1050       C  
+ATOM   2810  C   SER B 188      33.256 -25.172  50.777  1.00 40.38           C  
+ANISOU 2810  C   SER B 188     5650   6084   3609  -1157   -672   -655       C  
+ATOM   2811  O   SER B 188      33.387 -24.245  49.966  1.00 35.39           O  
+ANISOU 2811  O   SER B 188     4956   5687   2804  -1143   -693   -553       O  
+ATOM   2812  CB  SER B 188      34.161 -27.401  50.091  1.00 38.76           C  
+ANISOU 2812  CB  SER B 188     6094   5243   3390  -1759   -162  -1333       C  
+ATOM   2813  OG  SER B 188      35.368 -28.125  49.926  1.00 40.08           O  
+ANISOU 2813  OG  SER B 188     6580   4813   3836  -1755    323  -1624       O  
+ATOM   2814  N   SER B 189      32.162 -25.355  51.513  1.00 40.18           N  
+ANISOU 2814  N   SER B 189     5408   6250   3608  -1164   -876   -381       N  
+ATOM   2815  CA  SER B 189      31.012 -24.457  51.448  1.00 40.72           C  
+ANISOU 2815  CA  SER B 189     5135   6791   3546  -1152  -1084    176       C  
+ATOM   2816  C   SER B 189      31.306 -23.069  52.012  1.00 37.48           C  
+ANISOU 2816  C   SER B 189     4513   6317   3411   -650   -910    445       C  
+ATOM   2817  O   SER B 189      30.790 -22.078  51.506  1.00 33.98           O  
+ANISOU 2817  O   SER B 189     3805   6234   2873   -610   -870    886       O  
+ATOM   2818  CB  SER B 189      29.820 -25.068  52.193  1.00 40.86           C  
+ANISOU 2818  CB  SER B 189     5027   6906   3593  -1245  -1305    421       C  
+ATOM   2819  OG  SER B 189      29.212 -26.074  51.411  1.00 47.80           O  
+ANISOU 2819  OG  SER B 189     6055   8079   4027  -1836  -1450    337       O  
+ATOM   2820  N   TRP B 190      32.124 -22.998  53.056  1.00 30.91           N  
+ANISOU 2820  N   TRP B 190     3780   5064   2899   -332   -737    234       N  
+ATOM   2821  CA  TRP B 190      32.453 -21.703  53.660  1.00 28.15           C  
+ANISOU 2821  CA  TRP B 190     3334   4640   2722     11   -455    439       C  
+ATOM   2822  C   TRP B 190      33.304 -20.830  52.746  1.00 29.51           C  
+ANISOU 2822  C   TRP B 190     3560   4921   2732    157   -268    323       C  
+ATOM   2823  O   TRP B 190      33.222 -19.604  52.790  1.00 30.55           O  
+ANISOU 2823  O   TRP B 190     3551   5174   2883    381     21    591       O  
+ATOM   2824  CB  TRP B 190      33.219 -21.870  54.970  1.00 27.23           C  
+ANISOU 2824  CB  TRP B 190     3335   4136   2874    134   -323    260       C  
+ATOM   2825  CG  TRP B 190      32.566 -22.729  56.014  1.00 25.75           C  
+ANISOU 2825  CG  TRP B 190     3093   3781   2911     31   -498    296       C  
+ATOM   2826  CD1 TRP B 190      31.278 -23.182  56.038  1.00 26.30           C  
+ANISOU 2826  CD1 TRP B 190     3044   3969   2979    -81   -730    509       C  
+ATOM   2827  CD2 TRP B 190      33.200 -23.244  57.182  1.00 24.44           C  
+ANISOU 2827  CD2 TRP B 190     2958   3330   2997     15   -471    145       C  
+ATOM   2828  NE1 TRP B 190      31.073 -23.952  57.163  1.00 26.03           N  
+ANISOU 2828  NE1 TRP B 190     3005   3680   3204   -104   -851    409       N  
+ATOM   2829  CE2 TRP B 190      32.240 -24.002  57.881  1.00 24.79           C  
+ANISOU 2829  CE2 TRP B 190     2909   3292   3220    -65   -692    198       C  
+ATOM   2830  CE3 TRP B 190      34.489 -23.134  57.709  1.00 24.14           C  
+ANISOU 2830  CE3 TRP B 190     2980   3152   3040     27   -293     39       C  
+ATOM   2831  CZ2 TRP B 190      32.529 -24.642  59.077  1.00 22.25           C  
+ANISOU 2831  CZ2 TRP B 190     2527   2742   3185   -122   -735    102       C  
+ATOM   2832  CZ3 TRP B 190      34.773 -23.774  58.900  1.00 24.17           C  
+ANISOU 2832  CZ3 TRP B 190     2886   2995   3305    -97   -335     47       C  
+ATOM   2833  CH2 TRP B 190      33.795 -24.522  59.569  1.00 22.46           C  
+ANISOU 2833  CH2 TRP B 190     2552   2688   3295   -165   -553     55       C  
+ATOM   2834  N   VAL B 191      34.161 -21.470  51.959  1.00 29.43           N  
+ANISOU 2834  N   VAL B 191     3783   4801   2599     39   -351    -86       N  
+ATOM   2835  CA  VAL B 191      35.143 -20.737  51.171  1.00 31.81           C  
+ANISOU 2835  CA  VAL B 191     4200   5093   2791    219   -201   -284       C  
+ATOM   2836  C   VAL B 191      34.548 -20.325  49.839  1.00 38.36           C  
+ANISOU 2836  C   VAL B 191     4873   6350   3352     29   -307   -142       C  
+ATOM   2837  O   VAL B 191      34.743 -19.202  49.379  1.00 47.37           O  
+ANISOU 2837  O   VAL B 191     5872   7689   4437    273   -145    -38       O  
+ATOM   2838  CB  VAL B 191      36.408 -21.577  50.956  1.00 36.95           C  
+ANISOU 2838  CB  VAL B 191     5196   5325   3519    186   -163   -713       C  
+ATOM   2839  CG1 VAL B 191      37.328 -20.936  49.918  1.00 39.21           C  
+ANISOU 2839  CG1 VAL B 191     5653   5567   3679    335    -71   -943       C  
+ATOM   2840  CG2 VAL B 191      37.128 -21.763  52.282  1.00 31.54           C  
+ANISOU 2840  CG2 VAL B 191     4538   4348   3100    370    -33   -688       C  
+ATOM   2841  N   ASN B 192      33.796 -21.233  49.234  1.00 37.30           N  
+ANISOU 2841  N   ASN B 192     4742   6411   3018   -464   -552   -104       N  
+ATOM   2842  CA  ASN B 192      33.203 -20.983  47.929  1.00 44.27           C  
+ANISOU 2842  CA  ASN B 192     5452   7803   3565   -856   -700    102       C  
+ATOM   2843  C   ASN B 192      31.888 -20.206  47.998  1.00 48.56           C  
+ANISOU 2843  C   ASN B 192     5448   8918   4084   -851   -742    869       C  
+ATOM   2844  O   ASN B 192      31.222 -20.132  49.033  1.00 46.73           O  
+ANISOU 2844  O   ASN B 192     5053   8627   4076   -652   -686   1214       O  
+ATOM   2845  CB  ASN B 192      33.000 -22.310  47.198  1.00 50.07           C  
+ANISOU 2845  CB  ASN B 192     6492   8541   3990  -1571   -860   -160       C  
+ATOM   2846  CG  ASN B 192      34.316 -22.937  46.762  1.00 53.45           C  
+ANISOU 2846  CG  ASN B 192     7450   8380   4478  -1638   -656   -800       C  
+ATOM   2847  OD1 ASN B 192      35.014 -22.411  45.885  1.00 53.66           O  
+ANISOU 2847  OD1 ASN B 192     7591   8346   4452  -1609   -593   -996       O  
+ATOM   2848  ND2 ASN B 192      34.674 -24.053  47.390  1.00 51.54           N  
+ANISOU 2848  ND2 ASN B 192     7505   7658   4418  -1684   -497  -1075       N  
+ATOM   2849  OXT ASN B 192      31.468 -19.613  47.001  1.00 54.13           O1-
+ANISOU 2849  OXT ASN B 192     5833  10149   4584  -1059   -792   1229       O1-
+TER    2850      ASN B 192                                                      
+HETATM 2851  O   HOH A 201      37.468  -1.508  44.497  1.00 42.67           O  
+HETATM 2852  O   HOH A 202      30.030  -8.325  41.768  1.00 39.61           O  
+HETATM 2853  O   HOH A 203      26.760   0.643  46.827  1.00 28.07           O  
+HETATM 2854  O   HOH A 204      21.614  28.868  54.471  1.00 29.95           O  
+HETATM 2855  O   HOH A 205      25.125  22.211  31.063  1.00 27.66           O  
+HETATM 2856  O   HOH A 206      37.086   7.090  37.813  1.00 41.71           O  
+HETATM 2857  O   HOH A 207      33.090  12.263  43.948  1.00 27.97           O  
+HETATM 2858  O   HOH A 208       8.802   8.285  32.293  1.00 47.38           O  
+HETATM 2859  O   HOH A 209      12.750  13.177  32.732  1.00 39.48           O  
+HETATM 2860  O   HOH A 210       8.779  20.333  36.162  1.00 44.27           O  
+HETATM 2861  O   HOH A 211      20.227  25.820  35.302  1.00 18.09           O  
+HETATM 2862  O   HOH A 212      29.241  34.519  31.817  1.00 43.40           O  
+HETATM 2863  O   HOH A 213      34.823  32.815  49.635  1.00 30.97           O  
+HETATM 2864  O   HOH A 214      28.571  35.562  54.377  1.00 35.11           O  
+HETATM 2865  O   HOH A 215       9.442  25.353  42.195  1.00 21.31           O  
+HETATM 2866  O   HOH A 216      25.383   3.132  32.948  1.00 24.37           O  
+HETATM 2867  O   HOH A 217       7.598  39.425  39.699  1.00 40.29           O  
+HETATM 2868  O   HOH A 218      21.937  12.123  30.439  1.00 20.80           O  
+HETATM 2869  O   HOH A 219      26.865  -4.183  52.082  1.00 51.08           O  
+HETATM 2870  O   HOH A 220      25.541  21.248  28.350  1.00 32.43           O  
+HETATM 2871  O   HOH A 221      12.436  16.282  43.332  1.00 16.25           O  
+HETATM 2872  O   HOH A 222      34.376  11.650  41.810  1.00 32.88           O  
+HETATM 2873  O   HOH A 223      31.295   6.528  46.966  1.00 25.94           O  
+HETATM 2874  O   HOH A 224      19.230  11.599  30.961  1.00 20.27           O  
+HETATM 2875  O   HOH A 225      10.010  17.022  39.713  1.00 26.27           O  
+HETATM 2876  O   HOH A 226      30.802   9.769  45.029  1.00 17.46           O  
+HETATM 2877  O   HOH A 227      31.870  23.202  48.947  1.00 21.32           O  
+HETATM 2878  O   HOH A 228      27.615  38.755  39.480  1.00 23.14           O  
+HETATM 2879  O   HOH A 229      21.358  26.094  51.553  1.00 43.46           O  
+HETATM 2880  O   HOH A 230      32.505  28.141  53.039  1.00 43.29           O  
+HETATM 2881  O   HOH A 231      18.699  39.223  27.012  1.00 26.98           O  
+HETATM 2882  O   HOH A 232      16.144  21.760  38.819  1.00 18.09           O  
+HETATM 2883  O   HOH A 233      15.131  28.839  36.688  1.00 17.97           O  
+HETATM 2884  O   HOH A 234      14.003  24.054  27.452  1.00 47.17           O  
+HETATM 2885  O   HOH A 235      22.995  34.063  32.114  1.00 22.85           O  
+HETATM 2886  O   HOH A 236      31.193  25.274  52.519  1.00 42.40           O  
+HETATM 2887  O   HOH A 237      19.373  11.630  49.461  1.00 24.94           O  
+HETATM 2888  O   HOH A 238      27.283  30.928  53.799  1.00 38.99           O  
+HETATM 2889  O   HOH A 239      10.376  28.787  34.890  1.00 31.27           O  
+HETATM 2890  O   HOH A 240      25.136  29.699  54.949  1.00 32.10           O  
+HETATM 2891  O   HOH A 241      17.939   5.643  31.757  1.00 27.03           O  
+HETATM 2892  O   HOH A 242      13.363  12.664  35.211  1.00 24.17           O  
+HETATM 2893  O   HOH A 243      39.334  16.385  38.683  1.00 43.50           O  
+HETATM 2894  O   HOH A 244      17.168  17.244  48.023  1.00 25.30           O  
+HETATM 2895  O   HOH A 245      13.295  21.065  31.322  1.00 44.71           O  
+HETATM 2896  O   HOH A 246      16.900  31.695  49.098  1.00 22.06           O  
+HETATM 2897  O   HOH A 247      19.457  38.750  36.455  1.00 23.75           O  
+HETATM 2898  O   HOH A 248      38.067  16.679  35.254  1.00 33.50           O  
+HETATM 2899  O   HOH A 249      14.784  29.829  33.566  1.00 26.35           O  
+HETATM 2900  O   HOH A 250      11.343  27.577  46.661  1.00 22.86           O  
+HETATM 2901  O   HOH A 251      38.759  35.932  33.827  1.00 49.64           O  
+HETATM 2902  O   HOH A 252      14.068  32.750  35.066  1.00 16.77           O  
+HETATM 2903  O   HOH A 253      41.182  17.555  33.809  1.00 31.88           O  
+HETATM 2904  O   HOH A 254       6.386   3.989  40.477  1.00 32.29           O  
+HETATM 2905  O   HOH A 255      20.612   7.926  30.078  1.00 29.36           O  
+HETATM 2906  O   HOH A 256      29.271   8.652  37.437  1.00 26.59           O  
+HETATM 2907  O   HOH A 257      17.010  29.683  44.435  1.00 18.43           O  
+HETATM 2908  O   HOH A 258      34.185  14.790  44.319  1.00 30.83           O  
+HETATM 2909  O   HOH A 259      25.058   8.535  24.954  1.00 26.75           O  
+HETATM 2910  O   HOH A 260      10.599  34.697  35.198  1.00 24.00           O  
+HETATM 2911  O   HOH A 261      25.115   1.526  35.064  1.00 28.47           O  
+HETATM 2912  O   HOH A 262       7.903  34.120  39.629  1.00 35.74           O  
+HETATM 2913  O   HOH A 263      29.753  18.548  47.480  1.00 21.33           O  
+HETATM 2914  O   HOH A 264      16.434  26.566  42.022  1.00 15.78           O  
+HETATM 2915  O   HOH A 265       9.743   6.373  34.189  1.00 29.21           O  
+HETATM 2916  O   HOH A 266      11.968  31.739  31.272  1.00 25.33           O  
+HETATM 2917  O   HOH A 267      22.264  17.329  47.475  1.00 20.64           O  
+HETATM 2918  O   HOH A 268      24.920  36.313  47.336  1.00 25.99           O  
+HETATM 2919  O   HOH A 269      13.485   0.428  39.154  1.00 43.39           O  
+HETATM 2920  O   HOH A 270      19.556  31.731  44.791  1.00 16.88           O  
+HETATM 2921  O   HOH A 271      16.645   9.054  30.158  1.00 42.88           O  
+HETATM 2922  O   HOH A 272      35.276  39.123  32.169  1.00 41.57           O  
+HETATM 2923  O   HOH A 273      16.413  10.700  45.378  1.00 22.75           O  
+HETATM 2924  O   HOH A 274      14.433  35.664  47.383  1.00 28.24           O  
+HETATM 2925  O   HOH A 275      20.762   7.800  49.132  1.00 24.88           O  
+HETATM 2926  O   HOH A 276      13.558   7.454  44.751  1.00 33.98           O  
+HETATM 2927  O   HOH A 277      14.258  17.667  44.667  1.00 17.73           O  
+HETATM 2928  O   HOH A 278      10.400  23.595  38.971  1.00 30.84           O  
+HETATM 2929  O   HOH A 279      24.895  23.787  52.027  1.00 39.52           O  
+HETATM 2930  O   HOH A 280      10.393  27.417  39.852  1.00 25.80           O  
+HETATM 2931  O   HOH A 281      15.667  25.871  34.399  1.00 21.49           O  
+HETATM 2932  O   HOH A 282      14.480  30.430  45.062  1.00 16.86           O  
+HETATM 2933  O   HOH A 283      40.827  11.304  37.903  1.00 50.15           O  
+HETATM 2934  O   HOH A 284       5.242   9.430  38.070  1.00 38.61           O  
+HETATM 2935  O   HOH A 285      39.220   9.812  36.960  1.00 50.14           O  
+HETATM 2936  O   HOH A 286       8.860  41.606  36.823  1.00 47.00           O  
+HETATM 2937  O   HOH A 287      13.939  11.298  42.183  1.00 24.19           O  
+HETATM 2938  O   HOH A 288      22.983  21.494  29.595  1.00 49.41           O  
+HETATM 2939  O   HOH A 289      12.924  26.512  28.187  1.00 33.31           O  
+HETATM 2940  O   HOH A 290      32.291   9.411  28.110  1.00 27.42           O  
+HETATM 2941  O   HOH A 291      25.105   3.499  53.856  1.00 36.08           O  
+HETATM 2942  O   HOH A 292      33.428  34.723  46.443  1.00 24.35           O  
+HETATM 2943  O   HOH A 293      16.696  29.294  50.570  1.00 28.57           O  
+HETATM 2944  O   HOH A 294      39.074  17.944  42.191  1.00 48.73           O  
+HETATM 2945  O   HOH A 295      16.905  38.261  46.278  1.00 34.90           O  
+HETATM 2946  O   HOH A 296      19.518  15.860  37.433  1.00 33.35           O  
+HETATM 2947  O   HOH A 297      33.460   9.648  25.719  1.00 39.04           O  
+HETATM 2948  O   HOH A 298      14.156  22.043  45.757  1.00 22.29           O  
+HETATM 2949  O   HOH A 299      40.397  20.512  26.850  1.00 44.04           O  
+HETATM 2950  O   HOH A 300      33.694   8.055  29.987  1.00 36.55           O  
+HETATM 2951  O   HOH A 301      27.724  23.261  30.405  1.00 30.16           O  
+HETATM 2952  O   HOH A 302       9.062  12.379  38.496  1.00 30.30           O  
+HETATM 2953  O   HOH A 303      38.113  -3.120  47.740  1.00 40.19           O  
+HETATM 2954  O   HOH A 304      28.023  16.598  50.894  1.00 31.17           O  
+HETATM 2955  O   HOH A 305      21.319  35.951  52.997  1.00 37.26           O  
+HETATM 2956  O   HOH A 306      24.295  25.994  53.711  1.00 33.26           O  
+HETATM 2957  O   HOH A 307      23.080  37.152  49.737  1.00 38.69           O  
+HETATM 2958  O   HOH A 308      33.981  38.099  47.251  1.00 44.04           O  
+HETATM 2959  O   HOH A 309      30.643   7.348  27.042  1.00 28.42           O  
+HETATM 2960  O   HOH A 310      30.931   5.985  29.047  1.00 30.95           O  
+HETATM 2961  O   HOH A 311      20.157  18.849  28.103  1.00 26.73           O  
+HETATM 2962  O   HOH A 312      19.511  25.370  49.308  1.00 18.64           O  
+HETATM 2963  O   HOH A 313      17.058  -0.410  34.366  1.00 31.90           O  
+HETATM 2964  O   HOH A 314      24.602   1.493  30.939  1.00 38.38           O  
+HETATM 2965  O   HOH A 315      19.878   8.902  27.541  1.00 42.16           O  
+HETATM 2966  O   HOH A 316      31.520  44.052  43.726  1.00 38.50           O  
+HETATM 2967  O   HOH A 317      39.380  32.918  47.682  1.00 43.85           O  
+HETATM 2968  O   HOH A 318       8.524  30.148  40.429  1.00 26.19           O  
+HETATM 2969  O   HOH A 319      30.712  16.416  48.727  1.00 38.74           O  
+HETATM 2970  O   HOH A 320      34.302  29.778  55.152  1.00 44.34           O  
+HETATM 2971  O   HOH A 321      17.840  40.523  42.841  1.00 29.64           O  
+HETATM 2972  O   HOH A 322      16.939  17.478  27.981  1.00 18.40           O  
+HETATM 2973  O   HOH A 323      29.417  28.968  53.395  1.00 29.07           O  
+HETATM 2974  O   HOH A 324      27.021  29.881  27.988  1.00 25.98           O  
+HETATM 2975  O   HOH A 325       6.281  12.130  37.552  1.00 41.69           O  
+HETATM 2976  O   HOH A 326      17.759   6.854  47.938  1.00 29.23           O  
+HETATM 2977  O   HOH A 327      36.360   2.216  33.625  1.00 24.90           O  
+HETATM 2978  O   HOH A 328      40.149  14.972  36.181  1.00 41.82           O  
+HETATM 2979  O   HOH A 329      39.596  29.752  30.747  1.00 38.79           O  
+HETATM 2980  O   HOH A 330      23.320  19.927  50.928  1.00 18.92           O  
+HETATM 2981  O   HOH A 331      26.978  40.591  36.228  1.00 31.15           O  
+HETATM 2982  O   HOH A 332      11.064  31.727  46.214  1.00 29.21           O  
+HETATM 2983  O   HOH A 333      32.698  16.903  45.971  1.00 18.28           O  
+HETATM 2984  O   HOH A 334      20.189  22.475  28.531  1.00 14.63           O  
+HETATM 2985  O   HOH A 335      12.125   2.441  41.202  1.00 15.94           O  
+HETATM 2986  O   HOH A 336       6.809  26.887  40.509  1.00 37.08           O  
+HETATM 2987  O   HOH A 337      19.880  15.483  23.006  1.00 39.65           O  
+HETATM 2988  O   HOH A 338      25.776  38.776  43.411  1.00 27.92           O  
+HETATM 2989  O   HOH A 339      28.143  39.010  42.290  1.00 45.44           O  
+HETATM 2990  O   HOH A 340       9.309  18.282  33.885  1.00 46.56           O  
+HETATM 2991  O   HOH A 341      17.574  14.123  23.821  1.00 39.31           O  
+HETATM 2992  O   HOH A 342       9.122   2.080  40.996  1.00 40.17           O  
+HETATM 2993  O   HOH A 343      18.880  15.696  49.699  1.00 40.52           O  
+HETATM 2994  O   HOH A 344      24.564  38.567  45.838  1.00 44.52           O  
+HETATM 2995  O   HOH A 345       8.637  33.825  36.801  1.00 32.75           O  
+HETATM 2996  O   HOH A 346      10.773  32.681  29.102  1.00 50.94           O  
+HETATM 2997  O   HOH A 347       5.579  26.302  42.684  1.00 38.77           O  
+HETATM 2998  O   HOH A 348      11.157  26.857  25.665  1.00 60.81           O  
+HETATM 2999  O   HOH A 349      25.624  23.554  21.788  1.00 53.01           O  
+HETATM 3000  O   HOH A 350      38.484  34.096  31.471  1.00 50.71           O  
+HETATM 3001  O   HOH A 351      19.319  40.810  34.774  1.00 29.96           O  
+HETATM 3002  O   HOH A 352      22.029  38.083  44.882  1.00 26.43           O  
+HETATM 3003  O   HOH A 353      13.676  27.348  33.512  1.00 29.75           O  
+HETATM 3004  O   HOH A 354      14.672  10.372  31.663  1.00 39.89           O  
+HETATM 3005  O   HOH A 355      21.216  18.196  49.761  1.00 34.58           O  
+HETATM 3006  O   HOH A 356      13.507   2.636  44.322  1.00 31.54           O  
+HETATM 3007  O   HOH A 357      10.593  13.628  36.575  1.00 15.63           O  
+HETATM 3008  O   HOH A 358      19.355  20.373  49.688  1.00 26.39           O  
+HETATM 3009  O   HOH A 359      15.801   4.398  46.566  1.00 41.14           O  
+HETATM 3010  O   HOH A 360      16.326   2.326  44.356  1.00 44.12           O  
+HETATM 3011  O   HOH A 361       9.336  26.176  34.456  1.00 42.89           O  
+HETATM 3012  O   HOH A 362      14.296   9.563  46.257  1.00 26.41           O  
+HETATM 3013  O   HOH A 363      11.924  26.502  31.454  1.00 42.53           O  
+HETATM 3014  O   HOH A 364      11.203  29.121  31.274  1.00 43.08           O  
+HETATM 3015  O   HOH A 365      14.897   0.062  41.500  1.00 48.67           O  
+HETATM 3016  O   HOH A 366      31.569  20.344  48.907  1.00 23.13           O  
+HETATM 3017  O   HOH A 367       9.158  19.879  39.042  1.00 32.80           O  
+HETATM 3018  O   HOH A 368      25.279  40.398  38.290  1.00 30.62           O  
+HETATM 3019  O   HOH A 369      16.745   2.267  47.784  1.00 36.43           O  
+HETATM 3020  O   HOH A 370      27.204  23.251  20.034  1.00 43.44           O  
+HETATM 3021  O   HOH A 371       9.226  -0.174  39.002  1.00 53.98           O  
+HETATM 3022  O   HOH A 372      33.654  29.652  25.206  1.00 43.46           O  
+HETATM 3023  O   HOH A 373      16.649  -4.403  36.655  1.00 46.00           O  
+HETATM 3024  O   HOH B 201      34.020   6.106  47.772  1.00 42.40           O  
+HETATM 3025  O   HOH B 202      46.837   4.169  58.452  1.00 27.65           O  
+HETATM 3026  O   HOH B 203      43.373 -26.217  77.946  1.00 30.63           O  
+HETATM 3027  O   HOH B 204      29.544  -9.904  64.446  1.00 46.27           O  
+HETATM 3028  O   HOH B 205      34.901  18.072  57.070  1.00 45.82           O  
+HETATM 3029  O   HOH B 206      35.910   4.026  49.019  1.00 34.32           O  
+HETATM 3030  O   HOH B 207      33.469   7.721  64.913  1.00 40.28           O  
+HETATM 3031  O   HOH B 208      33.062 -10.853  68.251  1.00 22.14           O  
+HETATM 3032  O   HOH B 209      37.771 -13.134  45.959  1.00 40.04           O  
+HETATM 3033  O   HOH B 210      46.215 -31.338  67.132  1.00 25.19           O  
+HETATM 3034  O   HOH B 211      33.103 -25.216  69.560  1.00 20.82           O  
+HETATM 3035  O   HOH B 212      55.721 -31.165  66.867  1.00 27.69           O  
+HETATM 3036  O   HOH B 213      42.666  -2.296  52.951  1.00 35.05           O  
+HETATM 3037  O   HOH B 214      49.619  -4.800  61.498  1.00 22.78           O  
+HETATM 3038  O   HOH B 215      46.198 -18.375  64.854  1.00 17.94           O  
+HETATM 3039  O   HOH B 216      34.783 -17.902  47.121  1.00 42.43           O  
+HETATM 3040  O   HOH B 217      44.233   5.366  58.283  1.00 28.77           O  
+HETATM 3041  O   HOH B 218      37.757  -9.077  72.412  1.00 21.67           O  
+HETATM 3042  O   HOH B 219      27.333 -27.884  66.535  1.00 31.95           O  
+HETATM 3043  O   HOH B 220      48.241   1.913  65.580  1.00 26.71           O  
+HETATM 3044  O   HOH B 221      39.892 -17.780  76.184  1.00 19.59           O  
+HETATM 3045  O   HOH B 222      53.544 -17.889  71.835  1.00 36.84           O  
+HETATM 3046  O   HOH B 223      45.644 -12.351  76.012  1.00 49.40           O  
+HETATM 3047  O   HOH B 224      49.363  -4.094  64.259  1.00 23.81           O  
+HETATM 3048  O   HOH B 225      42.441 -19.647  74.980  1.00 22.46           O  
+HETATM 3049  O   HOH B 226      48.536 -21.725  70.620  1.00 18.96           O  
+HETATM 3050  O   HOH B 227      49.379 -27.683  56.335  1.00 27.25           O  
+HETATM 3051  O   HOH B 228      42.791 -32.289  58.927  1.00 29.39           O  
+HETATM 3052  O   HOH B 229      55.928 -26.343  71.973  1.00 21.79           O  
+HETATM 3053  O   HOH B 230      32.793   4.995  57.435  1.00 23.96           O  
+HETATM 3054  O   HOH B 231      49.825 -26.772  62.707  1.00 24.75           O  
+HETATM 3055  O   HOH B 232      45.296 -21.222  70.295  1.00 15.76           O  
+HETATM 3056  O   HOH B 233      50.205   2.429  70.807  1.00 44.47           O  
+HETATM 3057  O   HOH B 234      29.132 -18.406  61.445  1.00 42.74           O  
+HETATM 3058  O   HOH B 235      54.272 -15.617  69.641  1.00 35.61           O  
+HETATM 3059  O   HOH B 236      41.054 -11.241  45.376  1.00 35.89           O  
+HETATM 3060  O   HOH B 237      37.565 -22.804  69.092  1.00 15.82           O  
+HETATM 3061  O   HOH B 238      42.911 -15.726  74.702  1.00 27.74           O  
+HETATM 3062  O   HOH B 239      34.772 -30.237  62.164  1.00 25.92           O  
+HETATM 3063  O   HOH B 240      31.575 -17.996  54.256  1.00 29.92           O  
+HETATM 3064  O   HOH B 241      41.415  -9.435  74.850  1.00 33.86           O  
+HETATM 3065  O   HOH B 242      51.383  -2.858  51.515  1.00 34.05           O  
+HETATM 3066  O   HOH B 243      36.669 -31.490  69.982  1.00 28.12           O  
+HETATM 3067  O   HOH B 244      47.390 -24.773  71.807  1.00 19.82           O  
+HETATM 3068  O   HOH B 245      47.679 -26.361  75.267  1.00 26.42           O  
+HETATM 3069  O   HOH B 246      30.659  -5.655  65.815  1.00 39.83           O  
+HETATM 3070  O   HOH B 247      46.341   1.444  73.852  1.00 37.02           O  
+HETATM 3071  O   HOH B 248      46.359   9.532  63.659  1.00 37.54           O  
+HETATM 3072  O   HOH B 249      49.693 -21.366  54.567  1.00 34.02           O  
+HETATM 3073  O   HOH B 250      30.038 -20.782  65.538  1.00 36.81           O  
+HETATM 3074  O   HOH B 251      47.916   0.355  50.269  1.00 31.26           O  
+HETATM 3075  O   HOH B 252      32.655 -13.072  55.691  1.00 25.95           O  
+HETATM 3076  O   HOH B 253      36.425 -10.721  70.819  1.00 16.61           O  
+HETATM 3077  O   HOH B 254      51.046 -23.279  73.390  1.00 23.19           O  
+HETATM 3078  O   HOH B 255      31.546 -22.990  69.593  1.00 29.90           O  
+HETATM 3079  O   HOH B 256      35.058  -3.932  68.017  1.00 23.05           O  
+HETATM 3080  O   HOH B 257      37.166 -23.510  71.874  1.00 19.30           O  
+HETATM 3081  O   HOH B 258      42.590 -14.427  68.990  1.00 15.95           O  
+HETATM 3082  O   HOH B 259      30.675  -1.750  63.655  1.00 23.67           O  
+HETATM 3083  O   HOH B 260      35.415 -28.856  72.380  1.00 25.61           O  
+HETATM 3084  O   HOH B 261      39.776   4.021  76.882  1.00 33.51           O  
+HETATM 3085  O   HOH B 262      54.638  -1.029  57.754  1.00 34.10           O  
+HETATM 3086  O   HOH B 263      35.127  -4.105  54.446  1.00 28.00           O  
+HETATM 3087  O   HOH B 264      39.773 -19.533  69.294  1.00 16.83           O  
+HETATM 3088  O   HOH B 265      28.684 -25.016  58.638  1.00 30.47           O  
+HETATM 3089  O   HOH B 266      29.682 -30.191  66.042  1.00 36.93           O  
+HETATM 3090  O   HOH B 267      32.443 -31.324  64.104  1.00 41.98           O  
+HETATM 3091  O   HOH B 268      37.357 -25.171  66.838  1.00 21.21           O  
+HETATM 3092  O   HOH B 269      24.641   2.150  63.261  1.00 36.64           O  
+HETATM 3093  O   HOH B 270      36.518 -26.301  46.267  1.00 48.68           O  
+HETATM 3094  O   HOH B 271      47.291 -18.029  69.272  1.00 18.08           O  
+HETATM 3095  O   HOH B 272      27.681  11.656  58.585  1.00 46.68           O  
+HETATM 3096  O   HOH B 273      49.759 -29.627  78.745  1.00 47.50           O  
+HETATM 3097  O   HOH B 274      27.669 -20.646  62.518  1.00 46.80           O  
+HETATM 3098  O   HOH B 275      45.367  -5.214  70.991  1.00 35.95           O  
+HETATM 3099  O   HOH B 276      41.304 -18.948  43.869  1.00 28.08           O  
+HETATM 3100  O   HOH B 277      37.561  -7.010  49.981  1.00 34.84           O  
+HETATM 3101  O   HOH B 278      49.115  -6.008  68.404  1.00 40.62           O  
+HETATM 3102  O   HOH B 279      35.264 -20.502  74.572  1.00 18.18           O  
+HETATM 3103  O   HOH B 280      52.053  -0.105  51.805  1.00 37.65           O  
+HETATM 3104  O   HOH B 281      33.076 -11.226  63.215  1.00 22.82           O  
+HETATM 3105  O   HOH B 282      47.257 -20.526  75.024  1.00 36.16           O  
+HETATM 3106  O   HOH B 283      43.159   9.305  44.648  1.00 42.93           O  
+HETATM 3107  O   HOH B 284      35.747 -14.975  71.384  1.00 20.10           O  
+HETATM 3108  O   HOH B 285      27.165 -28.581  63.110  1.00 38.74           O  
+HETATM 3109  O   HOH B 286      38.200   8.714  60.154  1.00 41.68           O  
+HETATM 3110  O   HOH B 287      29.663 -10.480  61.243  1.00 37.58           O  
+HETATM 3111  O   HOH B 288      51.631 -14.277  61.269  1.00 49.72           O  
+HETATM 3112  O   HOH B 289      42.405  -4.718  75.467  1.00 34.18           O  
+HETATM 3113  O   HOH B 290      35.418  -0.478  71.020  1.00 28.45           O  
+HETATM 3114  O   HOH B 291      37.631  13.537  59.400  1.00 37.53           O  
+HETATM 3115  O   HOH B 292      31.999  -0.590  66.619  1.00 23.51           O  
+HETATM 3116  O   HOH B 293      47.312   8.358  59.063  1.00 39.20           O  
+HETATM 3117  O   HOH B 294      37.765  15.239  56.856  1.00 42.18           O  
+HETATM 3118  O   HOH B 295      38.381  -4.277  70.590  1.00 29.42           O  
+HETATM 3119  O   HOH B 296      34.627 -29.572  52.751  1.00 33.02           O  
+HETATM 3120  O   HOH B 297      41.937 -18.990  78.571  1.00 33.95           O  
+HETATM 3121  O   HOH B 298      49.781   1.496  52.291  1.00 28.35           O  
+HETATM 3122  O   HOH B 299      31.637 -10.920  54.562  1.00 43.06           O  
+HETATM 3123  O   HOH B 300      32.192 -19.183  66.570  1.00 20.54           O  
+HETATM 3124  O   HOH B 301      34.007 -15.010  68.351  1.00 19.70           O  
+HETATM 3125  O   HOH B 302      52.750 -11.092  63.878  1.00 26.69           O  
+HETATM 3126  O   HOH B 303      27.402 -24.629  49.424  1.00 44.79           O  
+HETATM 3127  O   HOH B 304      50.637  -4.002  47.147  1.00 40.86           O  
+HETATM 3128  O   HOH B 305      45.587   7.680  66.110  1.00 35.78           O  
+HETATM 3129  O   HOH B 306      53.949  -5.032  47.032  1.00 40.79           O  
+HETATM 3130  O   HOH B 307      30.617   5.962  64.709  1.00 26.13           O  
+HETATM 3131  O   HOH B 308      53.059  -9.256  66.669  1.00 21.92           O  
+HETATM 3132  O   HOH B 309      29.938  15.993  55.237  1.00 42.52           O  
+HETATM 3133  O   HOH B 310      23.763   8.162  52.505  1.00 16.77           O  
+HETATM 3134  O   HOH B 311      36.383 -24.712  75.083  1.00 24.56           O  
+HETATM 3135  O   HOH B 312      30.784 -16.932  65.500  1.00 41.00           O  
+HETATM 3136  O   HOH B 313      43.498 -32.153  78.510  1.00 41.06           O  
+HETATM 3137  O   HOH B 314      48.239  -4.702  70.138  1.00 43.37           O  
+HETATM 3138  O   HOH B 315      55.806  -2.229  51.141  1.00 40.20           O  
+HETATM 3139  O   HOH B 316      47.302  16.351  50.931  1.00 24.58           O  
+HETATM 3140  O   HOH B 317      45.401 -33.508  59.391  1.00 30.28           O  
+HETATM 3141  O   HOH B 318      29.779 -14.313  62.425  1.00 17.43           O  
+HETATM 3142  O   HOH B 319      50.590 -12.244  71.151  1.00 19.77           O  
+HETATM 3143  O   HOH B 320      28.048 -21.432  55.109  1.00 42.72           O  
+HETATM 3144  O   HOH B 321      33.847 -11.504  52.576  1.00 22.72           O  
+HETATM 3145  O   HOH B 322      28.083 -16.198  54.589  1.00 54.32           O  
+HETATM 3146  O   HOH B 323      47.393 -10.318  75.171  1.00 47.43           O  
+HETATM 3147  O   HOH B 324      42.710 -16.589  42.944  1.00 47.03           O  
+HETATM 3148  O   HOH B 325      52.670 -28.086  57.002  1.00 34.48           O  
+HETATM 3149  O   HOH B 326      26.064  -5.731  61.175  1.00 45.42           O  
+HETATM 3150  O   HOH B 327      53.782 -27.608  59.364  1.00 40.62           O  
+HETATM 3151  O   HOH B 328      27.840  -8.489  63.788  1.00 49.16           O  
+HETATM 3152  O   HOH B 329      53.715 -23.978  74.020  1.00 36.27           O  
+HETATM 3153  O   HOH B 330      39.722 -18.416  80.190  1.00 36.67           O  
+HETATM 3154  O   HOH B 331      35.719   3.605  67.852  1.00 43.64           O  
+HETATM 3155  O   HOH B 332      42.616   2.584  79.052  1.00 45.59           O  
+HETATM 3156  O   HOH B 333      45.960 -25.450  77.526  1.00 26.63           O  
+HETATM 3157  O   HOH B 334      47.998 -33.472  67.477  1.00 45.99           O  
+HETATM 3158  O   HOH B 335      44.267 -28.036  79.950  1.00 41.38           O  
+HETATM 3159  O   HOH B 336      30.975 -12.543  64.661  1.00 35.92           O  
+HETATM 3160  O   HOH B 337      47.482 -17.869  75.663  1.00 46.85           O  
+HETATM 3161  O   HOH B 338      48.348 -19.247  71.438  1.00 20.88           O  
+HETATM 3162  O   HOH B 339      44.398  -5.787  73.664  1.00 15.48           O  
+HETATM 3163  O   HOH B 340      27.834 -24.256  54.776  1.00 43.94           O  
+HETATM 3164  O   HOH B 341      50.541  -5.052  66.534  1.00 36.03           O  
+HETATM 3165  O   HOH B 342      28.049 -34.504  55.744  1.00 32.01           O  
+HETATM 3166  O   HOH B 343      27.657  12.298  61.405  1.00 51.50           O  
+HETATM 3167  O   HOH B 344      35.381  17.103  47.136  1.00 50.71           O  
+HETATM 3168  O   HOH B 345      33.656   1.752  68.443  1.00 39.79           O  
+HETATM 3169  O   HOH B 346      49.788 -16.889  75.453  1.00 46.03           O  
+HETATM 3170  O   HOH B 347      45.956   3.908  75.524  1.00 34.58           O  
+HETATM 3171  O   HOH B 348      31.275 -14.429  66.373  1.00 29.00           O  
+HETATM 3172  O   HOH B 349      35.265   4.405  70.061  1.00 41.32           O  
+HETATM 3173  O   HOH B 350      49.516 -24.645  75.306  1.00 42.00           O  
+HETATM 3174  O   HOH B 351      31.123 -15.338  54.359  1.00 27.47           O  
+HETATM 3175  O   HOH B 352      51.275 -20.524  74.267  1.00 35.95           O  
+HETATM 3176  O   HOH B 353      34.123  -2.806  70.362  1.00 27.10           O  
+HETATM 3177  O   HOH B 354      53.066  -4.129  66.620  1.00 38.60           O  
+HETATM 3178  O   HOH B 355      50.484 -18.141  73.020  1.00 34.33           O  
+HETATM 3179  O   HOH B 356      30.950   4.268  67.028  1.00 41.24           O  
+HETATM 3180  O   HOH B 357      42.555 -11.967  75.766  1.00 40.48           O  
+HETATM 3181  O   HOH B 358      42.330 -15.750  78.071  1.00 36.67           O  
+HETATM 3182  O   HOH B 359      41.318 -13.217  77.518  1.00 42.08           O  
+CONECT  571  577                                                                
+CONECT  577  571  578                                                           
+CONECT  578  577  579  581                                                      
+CONECT  579  578  580  585                                                      
+CONECT  580  579                                                                
+CONECT  581  578  582                                                           
+CONECT  582  581  583                                                           
+CONECT  583  582  584                                                           
+CONECT  584  583                                                                
+CONECT  585  579                                                                
+CONECT 1968 1974                                                                
+CONECT 1974 1968 1975                                                           
+CONECT 1975 1974 1976 1978                                                      
+CONECT 1976 1975 1977 1982                                                      
+CONECT 1977 1976                                                                
+CONECT 1978 1975 1979                                                           
+CONECT 1979 1978 1980                                                           
+CONECT 1980 1979 1981                                                           
+CONECT 1981 1980                                                                
+CONECT 1982 1976                                                                
+MASTER      551    0    2   18   24    0    0    6 3168    2   20   30          
+END                                                                             
diff --git a/public/thoeris/7uxs_BcThsA_2mer_cdpr.pdb b/public/thoeris/7uxs_BcThsA_2mer_cdpr.pdb
new file mode 100644
index 0000000000000000000000000000000000000000..ebded12045158df29e2772eb7f5ae44e5b8108a7
--- /dev/null
+++ b/public/thoeris/7uxs_BcThsA_2mer_cdpr.pdb
@@ -0,0 +1,7264 @@
+HEADER    HYDROLASE                               06-MAY-22   7UXS              
+TITLE     CRYSTAL STRUCTURE OF THE BCTHSA SLOG DOMAIN IN COMPLEX WITH 3'CADPR   
+COMPND    MOL_ID: 1;                                                            
+COMPND   2 MOLECULE: BCTHSA;                                                    
+COMPND   3 CHAIN: B, A;                                                         
+COMPND   4 FRAGMENT: SLOG DOMAIN;                                               
+COMPND   5 ENGINEERED: YES                                                      
+SOURCE    MOL_ID: 1;                                                            
+SOURCE   2 ORGANISM_SCIENTIFIC: BACILLUS SUBTILIS;                              
+SOURCE   3 ORGANISM_TAXID: 1423;                                                
+SOURCE   4 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
+SOURCE   5 EXPRESSION_SYSTEM_TAXID: 562                                         
+KEYWDS    CADPR ISOMER, BACTERIAL TIR, THOERIS DEFENSE SYSTEM, THSA, THSB,      
+KEYWDS   2 ANTIPHAGE DEFENSE, NAD+, HYDROLASE                                   
+EXPDTA    X-RAY DIFFRACTION                                                     
+AUTHOR    Y.SHI,V.MASIC,T.MOSAIAB,T.VE                                          
+REVDAT   4   18-OCT-23 7UXS    1       REMARK                                   
+REVDAT   3   12-OCT-22 7UXS    1       JRNL                                     
+REVDAT   2   14-SEP-22 7UXS    1       JRNL                                     
+REVDAT   1   07-SEP-22 7UXS    0                                                
+JRNL        AUTH   M.K.MANIK,Y.SHI,S.LI,M.A.ZAYDMAN,N.DAMARAJU,S.EASTMAN,       
+JRNL        AUTH 2 T.G.SMITH,W.GU,V.MASIC,T.MOSAIAB,J.S.WEAGLEY,S.J.HANCOCK,    
+JRNL        AUTH 3 E.VASQUEZ,L.HARTLEY-TASSELL,N.KARGIOS,N.MARUTA,B.Y.J.LIM,    
+JRNL        AUTH 4 H.BURDETT,M.J.LANDSBERG,M.A.SCHEMBRI,I.PROKES,L.SONG,        
+JRNL        AUTH 5 M.GRANT,A.DIANTONIO,J.D.NANSON,M.GUO,J.MILBRANDT,T.VE,B.KOBE 
+JRNL        TITL   CYCLIC ADP RIBOSE ISOMERS: PRODUCTION, CHEMICAL STRUCTURES,  
+JRNL        TITL 2 AND IMMUNE SIGNALING.                                        
+JRNL        REF    SCIENCE                       V. 377 C8969 2022              
+JRNL        REFN                   ESSN 1095-9203                               
+JRNL        PMID   36048923                                                     
+JRNL        DOI    10.1126/SCIENCE.ADC8969                                      
+REMARK   2                                                                      
+REMARK   2 RESOLUTION.    1.57 ANGSTROMS.                                       
+REMARK   3                                                                      
+REMARK   3 REFINEMENT.                                                          
+REMARK   3   PROGRAM     : PHENIX 1.20.1_4487                                   
+REMARK   3   AUTHORS     : PAUL ADAMS,PAVEL AFONINE,VINCENT CHEN,IAN            
+REMARK   3               : DAVIS,KRESHNA GOPAL,RALF GROSSE-KUNSTLEVE,           
+REMARK   3               : LI-WEI HUNG,ROBERT IMMORMINO,TOM IOERGER,            
+REMARK   3               : AIRLIE MCCOY,ERIK MCKEE,NIGEL MORIARTY,              
+REMARK   3               : REETAL PAI,RANDY READ,JANE RICHARDSON,               
+REMARK   3               : DAVID RICHARDSON,TOD ROMO,JIM SACCHETTINI,           
+REMARK   3               : NICHOLAS SAUTER,JACOB SMITH,LAURENT                  
+REMARK   3               : STORONI,TOM TERWILLIGER,PETER ZWART                  
+REMARK   3                                                                      
+REMARK   3    REFINEMENT TARGET : GEOSTD + MONOMER LIBRARY + CDL V1.2           
+REMARK   3                                                                      
+REMARK   3  DATA USED IN REFINEMENT.                                            
+REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 1.57                           
+REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 36.87                          
+REMARK   3   MIN(FOBS/SIGMA_FOBS)              : 1.390                          
+REMARK   3   COMPLETENESS FOR RANGE        (%) : 99.7                           
+REMARK   3   NUMBER OF REFLECTIONS             : 56645                          
+REMARK   3                                                                      
+REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
+REMARK   3   R VALUE     (WORKING + TEST SET) : 0.150                           
+REMARK   3   R VALUE            (WORKING SET) : 0.149                           
+REMARK   3   FREE R VALUE                     : 0.176                           
+REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 3.530                           
+REMARK   3   FREE R VALUE TEST SET COUNT      : 2000                            
+REMARK   3                                                                      
+REMARK   3  FIT TO DATA USED IN REFINEMENT (IN BINS).                           
+REMARK   3   BIN  RESOLUTION RANGE  COMPL.    NWORK NFREE   RWORK  RFREE        
+REMARK   3     1 36.8700 -  3.7800    1.00     4176   153  0.1557 0.1911        
+REMARK   3     2  3.7800 -  3.0000    1.00     3985   145  0.1479 0.1658        
+REMARK   3     3  3.0000 -  2.6200    1.00     3949   146  0.1497 0.1714        
+REMARK   3     4  2.6200 -  2.3800    1.00     3932   144  0.1497 0.1732        
+REMARK   3     5  2.3800 -  2.2100    1.00     3887   141  0.1421 0.1768        
+REMARK   3     6  2.2100 -  2.0800    1.00     3901   143  0.1390 0.1800        
+REMARK   3     7  2.0800 -  1.9800    1.00     3890   142  0.1409 0.1612        
+REMARK   3     8  1.9800 -  1.8900    1.00     3892   143  0.1495 0.1622        
+REMARK   3     9  1.8900 -  1.8200    1.00     3860   141  0.1445 0.1704        
+REMARK   3    10  1.8200 -  1.7500    1.00     3889   143  0.1415 0.1851        
+REMARK   3    11  1.7500 -  1.7000    1.00     3856   140  0.1456 0.1662        
+REMARK   3    12  1.7000 -  1.6500    1.00     3827   140  0.1485 0.1883        
+REMARK   3    13  1.6500 -  1.6100    1.00     3881   143  0.1532 0.1897        
+REMARK   3    14  1.6100 -  1.5700    0.97     3720   136  0.1771 0.2062        
+REMARK   3                                                                      
+REMARK   3  BULK SOLVENT MODELLING.                                             
+REMARK   3   METHOD USED        : FLAT BULK SOLVENT MODEL                       
+REMARK   3   SOLVENT RADIUS     : 1.11                                          
+REMARK   3   SHRINKAGE RADIUS   : 0.90                                          
+REMARK   3   K_SOL              : NULL                                          
+REMARK   3   B_SOL              : NULL                                          
+REMARK   3                                                                      
+REMARK   3  ERROR ESTIMATES.                                                    
+REMARK   3   COORDINATE ERROR (MAXIMUM-LIKELIHOOD BASED)     : 0.144            
+REMARK   3   PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 15.241           
+REMARK   3                                                                      
+REMARK   3  B VALUES.                                                           
+REMARK   3   FROM WILSON PLOT           (A**2) : 15.42                          
+REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 17.84                          
+REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
+REMARK   3    B11 (A**2) : NULL                                                 
+REMARK   3    B22 (A**2) : NULL                                                 
+REMARK   3    B33 (A**2) : NULL                                                 
+REMARK   3    B12 (A**2) : NULL                                                 
+REMARK   3    B13 (A**2) : NULL                                                 
+REMARK   3    B23 (A**2) : NULL                                                 
+REMARK   3                                                                      
+REMARK   3  TWINNING INFORMATION.                                               
+REMARK   3   FRACTION: NULL                                                     
+REMARK   3   OPERATOR: NULL                                                     
+REMARK   3                                                                      
+REMARK   3  DEVIATIONS FROM IDEAL VALUES.                                       
+REMARK   3                 RMSD          COUNT                                  
+REMARK   3   BOND      :  0.008           3312                                  
+REMARK   3   ANGLE     :  0.945           4487                                  
+REMARK   3   CHIRALITY :  0.055            481                                  
+REMARK   3   PLANARITY :  0.010            600                                  
+REMARK   3   DIHEDRAL  : 13.728           1249                                  
+REMARK   3                                                                      
+REMARK   3  TLS DETAILS                                                         
+REMARK   3   NUMBER OF TLS GROUPS  : NULL                                       
+REMARK   3                                                                      
+REMARK   3  NCS DETAILS                                                         
+REMARK   3   NUMBER OF NCS GROUPS : NULL                                        
+REMARK   3                                                                      
+REMARK   3  OTHER REFINEMENT REMARKS: NULL                                      
+REMARK   4                                                                      
+REMARK   4 7UXS COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
+REMARK 100                                                                      
+REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 06-MAY-22.                  
+REMARK 100 THE DEPOSITION ID IS D_1000265058.                                   
+REMARK 200                                                                      
+REMARK 200 EXPERIMENTAL DETAILS                                                 
+REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
+REMARK 200  DATE OF DATA COLLECTION        : 17-FEB-22                          
+REMARK 200  TEMPERATURE           (KELVIN) : 100                                
+REMARK 200  PH                             : NULL                               
+REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
+REMARK 200                                                                      
+REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
+REMARK 200  RADIATION SOURCE               : AUSTRALIAN SYNCHROTRON             
+REMARK 200  BEAMLINE                       : MX2                                
+REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
+REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
+REMARK 200  WAVELENGTH OR RANGE        (A) : 0.9537                             
+REMARK 200  MONOCHROMATOR                  : NULL                               
+REMARK 200  OPTICS                         : NULL                               
+REMARK 200                                                                      
+REMARK 200  DETECTOR TYPE                  : PIXEL                              
+REMARK 200  DETECTOR MANUFACTURER          : DECTRIS EIGER X 16M                
+REMARK 200  INTENSITY-INTEGRATION SOFTWARE : XDS                                
+REMARK 200  DATA SCALING SOFTWARE          : AIMLESS                            
+REMARK 200                                                                      
+REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 56724                              
+REMARK 200  RESOLUTION RANGE HIGH      (A) : 1.570                              
+REMARK 200  RESOLUTION RANGE LOW       (A) : 46.160                             
+REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : NULL                               
+REMARK 200                                                                      
+REMARK 200 OVERALL.                                                             
+REMARK 200  COMPLETENESS FOR RANGE     (%) : 99.7                               
+REMARK 200  DATA REDUNDANCY                : 6.600                              
+REMARK 200  R MERGE                    (I) : 0.03800                            
+REMARK 200  R SYM                      (I) : NULL                               
+REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 20.2000                            
+REMARK 200                                                                      
+REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
+REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.57                     
+REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 1.59                     
+REMARK 200  COMPLETENESS FOR SHELL     (%) : 95.2                               
+REMARK 200  DATA REDUNDANCY IN SHELL       : 6.40                               
+REMARK 200  R MERGE FOR SHELL          (I) : 0.24200                            
+REMARK 200  R SYM FOR SHELL            (I) : NULL                               
+REMARK 200  <I/SIGMA(I)> FOR SHELL         : 4.600                              
+REMARK 200                                                                      
+REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
+REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT        
+REMARK 200 SOFTWARE USED: PHASER                                                
+REMARK 200 STARTING MODEL: PDB ENTRY 6LHX                                       
+REMARK 200                                                                      
+REMARK 200 REMARK: NULL                                                         
+REMARK 280                                                                      
+REMARK 280 CRYSTAL                                                              
+REMARK 280 SOLVENT CONTENT, VS   (%): 44.52                                     
+REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.22                     
+REMARK 280                                                                      
+REMARK 280 CRYSTALLIZATION CONDITIONS: 0.1 M BIS-TRIS, PH 5.5, 0.1 M AMMONIUM   
+REMARK 280  SULFATE, 25-29% PEG3350, VAPOR DIFFUSION, HANGING DROP,             
+REMARK 280  TEMPERATURE 293K                                                    
+REMARK 290                                                                      
+REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
+REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 21 21 21                       
+REMARK 290                                                                      
+REMARK 290      SYMOP   SYMMETRY                                                
+REMARK 290     NNNMMM   OPERATOR                                                
+REMARK 290       1555   X,Y,Z                                                   
+REMARK 290       2555   -X+1/2,-Y,Z+1/2                                         
+REMARK 290       3555   -X,Y+1/2,-Z+1/2                                         
+REMARK 290       4555   X+1/2,-Y+1/2,-Z                                         
+REMARK 290                                                                      
+REMARK 290     WHERE NNN -> OPERATOR NUMBER                                     
+REMARK 290           MMM -> TRANSLATION VECTOR                                  
+REMARK 290                                                                      
+REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS                            
+REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM             
+REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY                
+REMARK 290 RELATED MOLECULES.                                                   
+REMARK 290   SMTRY1   1  1.000000  0.000000  0.000000        0.00000            
+REMARK 290   SMTRY2   1  0.000000  1.000000  0.000000        0.00000            
+REMARK 290   SMTRY3   1  0.000000  0.000000  1.000000        0.00000            
+REMARK 290   SMTRY1   2 -1.000000  0.000000  0.000000       23.09700            
+REMARK 290   SMTRY2   2  0.000000 -1.000000  0.000000        0.00000            
+REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000       60.87000            
+REMARK 290   SMTRY1   3 -1.000000  0.000000  0.000000        0.00000            
+REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000       35.40050            
+REMARK 290   SMTRY3   3  0.000000  0.000000 -1.000000       60.87000            
+REMARK 290   SMTRY1   4  1.000000  0.000000  0.000000       23.09700            
+REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000       35.40050            
+REMARK 290   SMTRY3   4  0.000000  0.000000 -1.000000        0.00000            
+REMARK 290                                                                      
+REMARK 290 REMARK: NULL                                                         
+REMARK 300                                                                      
+REMARK 300 BIOMOLECULE: 1                                                       
+REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM                
+REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN                  
+REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON               
+REMARK 300 BURIED SURFACE AREA.                                                 
+REMARK 350                                                                      
+REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN           
+REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE                
+REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS          
+REMARK 350 GIVEN BELOW.  BOTH NON-CRYSTALLOGRAPHIC AND                          
+REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.                               
+REMARK 350                                                                      
+REMARK 350 BIOMOLECULE: 1                                                       
+REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC                           
+REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC                    
+REMARK 350 SOFTWARE USED: PISA                                                  
+REMARK 350 TOTAL BURIED SURFACE AREA: 3120 ANGSTROM**2                          
+REMARK 350 SURFACE AREA OF THE COMPLEX: 16350 ANGSTROM**2                       
+REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -20.0 KCAL/MOL                        
+REMARK 350 APPLY THE FOLLOWING TO CHAINS: B, A                                  
+REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
+REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
+REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
+REMARK 465                                                                      
+REMARK 465 MISSING RESIDUES                                                     
+REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE                       
+REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
+REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)                
+REMARK 465                                                                      
+REMARK 465   M RES C SSSEQI                                                     
+REMARK 465     SER B   281                                                      
+REMARK 465     ASN B   282                                                      
+REMARK 500                                                                      
+REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
+REMARK 500 SUBTOPIC: TORSION ANGLES                                             
+REMARK 500                                                                      
+REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:            
+REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
+REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                             
+REMARK 500                                                                      
+REMARK 500 STANDARD TABLE:                                                      
+REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)                    
+REMARK 500                                                                      
+REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-           
+REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400            
+REMARK 500                                                                      
+REMARK 500  M RES CSSEQI        PSI       PHI                                   
+REMARK 500    ASN B 295     -125.60     64.19                                   
+REMARK 500    ASP B 317       30.57     75.86                                   
+REMARK 500    VAL B 328      -53.23   -136.43                                   
+REMARK 500    TYR B 385     -124.02     53.61                                   
+REMARK 500    TYR B 422     -137.44     55.76                                   
+REMARK 500    ALA A 283     -124.91   -131.14                                   
+REMARK 500    ASN A 295     -112.71     66.16                                   
+REMARK 500    VAL A 328      -51.66   -134.87                                   
+REMARK 500    TYR A 385     -126.89     56.56                                   
+REMARK 500    TYR A 422     -138.14     57.81                                   
+REMARK 500                                                                      
+REMARK 500 REMARK: NULL                                                         
+REMARK 525                                                                      
+REMARK 525 SOLVENT                                                              
+REMARK 525                                                                      
+REMARK 525 THE SOLVENT MOLECULES HAVE CHAIN IDENTIFIERS THAT                    
+REMARK 525 INDICATE THE POLYMER CHAIN WITH WHICH THEY ARE MOST                  
+REMARK 525 CLOSELY ASSOCIATED. THE REMARK LISTS ALL THE SOLVENT                 
+REMARK 525 MOLECULES WHICH ARE MORE THAN 5A AWAY FROM THE                       
+REMARK 525 NEAREST POLYMER CHAIN (M = MODEL NUMBER;                             
+REMARK 525 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE                  
+REMARK 525 NUMBER; I=INSERTION CODE):                                           
+REMARK 525                                                                      
+REMARK 525  M RES CSSEQI                                                        
+REMARK 525    HOH A 787        DISTANCE =  5.95 ANGSTROMS                       
+DBREF  7UXS B  281   476  PDB    7UXS     7UXS           281    476             
+DBREF  7UXS A  281   476  PDB    7UXS     7UXS           281    476             
+SEQRES   1 B  196  SER ASN ALA THR VAL PHE LEU SER GLY SER ALA VAL GLU          
+SEQRES   2 B  196  TYR ASN HIS TRP GLU THR GLU HIS ALA GLU GLN PHE ILE          
+SEQRES   3 B  196  HIS GLN LEU SER LYS GLU LEU ILE ARG LYS ASP PHE ASN          
+SEQRES   4 B  196  ILE VAL SER GLY PHE GLY LEU GLY VAL GLY SER PHE VAL          
+SEQRES   5 B  196  ILE ASN GLY VAL LEU GLU GLU LEU TYR MET ASN GLN GLY          
+SEQRES   6 B  196  THR ILE ASP ASP ASP ARG LEU ILE LEU ARG PRO PHE PRO          
+SEQRES   7 B  196  GLN GLY LYS LYS GLY GLU GLU GLN TRP ASP LYS TYR ARG          
+SEQRES   8 B  196  ARG ASP MET ILE THR ARG THR GLY VAL SER ILE PHE LEU          
+SEQRES   9 B  196  TYR GLY ASN LYS ILE ASP LYS GLY GLN VAL VAL LYS ALA          
+SEQRES  10 B  196  LYS GLY VAL GLN SER GLU PHE ASN ILE SER PHE GLU GLN          
+SEQRES  11 B  196  ASN ASN TYR VAL VAL PRO VAL GLY ALA THR GLY TYR ILE          
+SEQRES  12 B  196  ALA LYS ASP LEU TRP ASN LYS VAL ASN GLU GLU PHE GLU          
+SEQRES  13 B  196  THR TYR TYR PRO GLY ALA ASP ALA ARG MET LYS LYS LEU          
+SEQRES  14 B  196  PHE GLY GLU LEU ASN ASN GLU ALA LEU SER ILE GLU GLU          
+SEQRES  15 B  196  LEU ILE ASN THR ILE ILE GLU PHE VAL GLU ILE LEU SER          
+SEQRES  16 B  196  ASN                                                          
+SEQRES   1 A  196  SER ASN ALA THR VAL PHE LEU SER GLY SER ALA VAL GLU          
+SEQRES   2 A  196  TYR ASN HIS TRP GLU THR GLU HIS ALA GLU GLN PHE ILE          
+SEQRES   3 A  196  HIS GLN LEU SER LYS GLU LEU ILE ARG LYS ASP PHE ASN          
+SEQRES   4 A  196  ILE VAL SER GLY PHE GLY LEU GLY VAL GLY SER PHE VAL          
+SEQRES   5 A  196  ILE ASN GLY VAL LEU GLU GLU LEU TYR MET ASN GLN GLY          
+SEQRES   6 A  196  THR ILE ASP ASP ASP ARG LEU ILE LEU ARG PRO PHE PRO          
+SEQRES   7 A  196  GLN GLY LYS LYS GLY GLU GLU GLN TRP ASP LYS TYR ARG          
+SEQRES   8 A  196  ARG ASP MET ILE THR ARG THR GLY VAL SER ILE PHE LEU          
+SEQRES   9 A  196  TYR GLY ASN LYS ILE ASP LYS GLY GLN VAL VAL LYS ALA          
+SEQRES  10 A  196  LYS GLY VAL GLN SER GLU PHE ASN ILE SER PHE GLU GLN          
+SEQRES  11 A  196  ASN ASN TYR VAL VAL PRO VAL GLY ALA THR GLY TYR ILE          
+SEQRES  12 A  196  ALA LYS ASP LEU TRP ASN LYS VAL ASN GLU GLU PHE GLU          
+SEQRES  13 A  196  THR TYR TYR PRO GLY ALA ASP ALA ARG MET LYS LYS LEU          
+SEQRES  14 A  196  PHE GLY GLU LEU ASN ASN GLU ALA LEU SER ILE GLU GLU          
+SEQRES  15 A  196  LEU ILE ASN THR ILE ILE GLU PHE VAL GLU ILE LEU SER          
+SEQRES  16 A  196  ASN                                                          
+HET    OJC  B 501      56                                                       
+HET    GOL  B 502      14                                                       
+HET    SO4  B 503       5                                                       
+HET    OJC  A 501      56                                                       
+HET    GOL  A 502      13                                                       
+HETNAM     OJC (2R,3R,3AS,5S,6R,7S,8R,11R,13S,15AR)-2-(6-AMINO-9H-              
+HETNAM   2 OJC  PURIN-9-YL)-3,6,7,11,13-PENTAHYDROXYOCTAHYDRO-2H,5H,            
+HETNAM   3 OJC  11H,13H-5,8-EPOXY-11LAMBDA~5~,13LAMBDA~5~-FURO[2,3-             
+HETNAM   4 OJC  G][1,3,5,9,2,4]TETRAOXADIPHOSPHACYCLOTETRADECINE-11,            
+HETNAM   5 OJC  13-DIONE                                                        
+HETNAM     GOL GLYCEROL                                                         
+HETNAM     SO4 SULFATE ION                                                      
+HETSYN     GOL GLYCERIN; PROPANE-1,2,3-TRIOL                                    
+FORMUL   3  OJC    2(C15 H21 N5 O13 P2)                                         
+FORMUL   4  GOL    2(C3 H8 O3)                                                  
+FORMUL   5  SO4    O4 S 2-                                                      
+FORMUL   8  HOH   *365(H2 O)                                                    
+HELIX    1 AA1 GLU B  298  LYS B  316  1                                  19    
+HELIX    2 AA2 VAL B  328  MET B  342  1                                  15    
+HELIX    3 AA3 THR B  346  ASP B  350  5                                   5    
+HELIX    4 AA4 GLY B  360  GLN B  366  1                                   7    
+HELIX    5 AA5 GLN B  366  THR B  376  1                                  11    
+HELIX    6 AA6 ALA B  397  GLN B  410  1                                  14    
+HELIX    7 AA7 GLY B  418  THR B  420  5                                   3    
+HELIX    8 AA8 GLY B  421  GLU B  434  1                                  14    
+HELIX    9 AA9 GLU B  434  TYR B  439  1                                   6    
+HELIX   10 AB1 ASP B  443  LEU B  453  1                                  11    
+HELIX   11 AB2 SER B  459  SER B  475  1                                  17    
+HELIX   12 AB3 GLU A  298  LYS A  316  1                                  19    
+HELIX   13 AB4 VAL A  328  ASN A  343  1                                  16    
+HELIX   14 AB5 THR A  346  ASP A  350  5                                   5    
+HELIX   15 AB6 GLY A  360  GLN A  366  1                                   7    
+HELIX   16 AB7 GLN A  366  THR A  376  1                                  11    
+HELIX   17 AB8 ALA A  397  GLN A  410  1                                  14    
+HELIX   18 AB9 GLY A  418  THR A  420  5                                   3    
+HELIX   19 AC1 GLY A  421  GLU A  434  1                                  14    
+HELIX   20 AC2 GLU A  434  TYR A  439  1                                   6    
+HELIX   21 AC3 ASP A  443  LEU A  453  1                                  11    
+HELIX   22 AC4 SER A  459  ASN A  476  1                                  18    
+SHEET    1 AA1 5 LEU B 352  LEU B 354  0                                        
+SHEET    2 AA1 5 ASN B 319  SER B 322  1  N  ILE B 320   O  ILE B 353           
+SHEET    3 AA1 5 THR B 284  SER B 290  1  N  VAL B 285   O  ASN B 319           
+SHEET    4 AA1 5 VAL B 380  TYR B 385  1  O  ILE B 382   N  SER B 288           
+SHEET    5 AA1 5 TYR B 413  PRO B 416  1  O  TYR B 413   N  SER B 381           
+SHEET    1 AA2 2 ASN B 387  ASP B 390  0                                        
+SHEET    2 AA2 2 GLN B 393  LYS B 396 -1  O  VAL B 395   N  LYS B 388           
+SHEET    1 AA3 5 LEU A 352  LEU A 354  0                                        
+SHEET    2 AA3 5 ASN A 319  SER A 322  1  N  ILE A 320   O  ILE A 353           
+SHEET    3 AA3 5 THR A 284  SER A 290  1  N  VAL A 285   O  ASN A 319           
+SHEET    4 AA3 5 VAL A 380  TYR A 385  1  O  ILE A 382   N  SER A 288           
+SHEET    5 AA3 5 TYR A 413  PRO A 416  1  O  TYR A 413   N  SER A 381           
+SHEET    1 AA4 2 ASN A 387  ASP A 390  0                                        
+SHEET    2 AA4 2 GLN A 393  LYS A 396 -1  O  VAL A 395   N  LYS A 388           
+CRYST1   46.194   70.801  121.740  90.00  90.00  90.00 P 21 21 21    8          
+ORIGX1      1.000000  0.000000  0.000000        0.00000                         
+ORIGX2      0.000000  1.000000  0.000000        0.00000                         
+ORIGX3      0.000000  0.000000  1.000000        0.00000                         
+SCALE1      0.021648  0.000000  0.000000        0.00000                         
+SCALE2      0.000000  0.014124  0.000000        0.00000                         
+SCALE3      0.000000  0.000000  0.008214        0.00000                         
+ATOM      1  N   ALA B 283      -5.606   2.358  -8.513  1.00 24.01           N  
+ATOM      2  CA  ALA B 283      -5.679   2.270  -9.973  1.00 18.71           C  
+ATOM      3  C   ALA B 283      -6.254   3.579 -10.527  1.00 18.96           C  
+ATOM      4  O   ALA B 283      -7.175   4.143  -9.951  1.00 15.58           O  
+ATOM      5  CB  ALA B 283      -6.523   1.107 -10.395  1.00 29.55           C  
+ATOM      6  HA  ALA B 283      -4.792   2.126 -10.339  1.00 22.45           H  
+ATOM      7  HB1 ALA B 283      -6.553   1.074 -11.364  1.00 35.47           H  
+ATOM      8  HB2 ALA B 283      -6.130   0.290 -10.049  1.00 35.47           H  
+ATOM      9  HB3 ALA B 283      -7.418   1.220 -10.040  1.00 35.47           H  
+ATOM     10  N   THR B 284      -5.712   4.057 -11.643  1.00 12.85           N  
+ATOM     11  CA  THR B 284      -6.043   5.372 -12.171  1.00 10.57           C  
+ATOM     12  C   THR B 284      -6.695   5.201 -13.536  1.00 12.81           C  
+ATOM     13  O   THR B 284      -6.152   4.526 -14.417  1.00 13.61           O  
+ATOM     14  CB  THR B 284      -4.798   6.253 -12.262  1.00 14.55           C  
+ATOM     15  OG1 THR B 284      -4.210   6.403 -10.963  1.00 14.09           O  
+ATOM     16  CG2 THR B 284      -5.111   7.640 -12.792  1.00 14.22           C  
+ATOM     17  H   THR B 284      -5.139   3.627 -12.120  1.00 15.42           H  
+ATOM     18  HA  THR B 284      -6.678   5.817 -11.588  1.00 12.68           H  
+ATOM     19  HB  THR B 284      -4.181   5.824 -12.875  1.00 17.46           H  
+ATOM     20  HG1 THR B 284      -3.543   6.910 -11.007  1.00 16.91           H  
+ATOM     21 HG21 THR B 284      -4.290   8.144 -12.906  1.00 17.06           H  
+ATOM     22 HG22 THR B 284      -5.562   7.575 -13.648  1.00 17.06           H  
+ATOM     23 HG23 THR B 284      -5.685   8.112 -12.169  1.00 17.06           H  
+ATOM     24  N   VAL B 285      -7.868   5.800 -13.702  1.00 11.66           N  
+ATOM     25  CA  VAL B 285      -8.638   5.716 -14.933  1.00 10.99           C  
+ATOM     26  C   VAL B 285      -8.611   7.059 -15.644  1.00 10.27           C  
+ATOM     27  O   VAL B 285      -8.591   8.116 -15.004  1.00 12.83           O  
+ATOM     28  CB  VAL B 285     -10.091   5.279 -14.665  1.00 13.02           C  
+ATOM     29  CG1 VAL B 285     -10.099   3.960 -13.881  1.00 17.83           C  
+ATOM     30  CG2 VAL B 285     -10.863   6.349 -13.966  1.00 14.63           C  
+ATOM     31  H   VAL B 285      -8.249   6.276 -13.096  1.00 13.99           H  
+ATOM     32  HA  VAL B 285      -8.216   5.061 -15.511  1.00 13.19           H  
+ATOM     33  HB  VAL B 285     -10.540   5.128 -15.511  1.00 15.62           H  
+ATOM     34 HG11 VAL B 285     -11.013   3.645 -13.803  1.00 21.39           H  
+ATOM     35 HG12 VAL B 285      -9.564   3.306 -14.357  1.00 21.39           H  
+ATOM     36 HG13 VAL B 285      -9.726   4.115 -12.999  1.00 21.39           H  
+ATOM     37 HG21 VAL B 285     -11.671   5.963 -13.592  1.00 17.55           H  
+ATOM     38 HG22 VAL B 285     -10.316   6.722 -13.257  1.00 17.55           H  
+ATOM     39 HG23 VAL B 285     -11.093   7.041 -14.605  1.00 17.55           H  
+ATOM     40  N   PHE B 286      -8.580   7.012 -16.964  1.00  8.97           N  
+ATOM     41  CA  PHE B 286      -8.824   8.188 -17.780  1.00  8.87           C  
+ATOM     42  C   PHE B 286     -10.298   8.220 -18.147  1.00  9.90           C  
+ATOM     43  O   PHE B 286     -10.828   7.232 -18.665  1.00 11.30           O  
+ATOM     44  CB  PHE B 286      -7.979   8.192 -19.057  1.00 10.95           C  
+ATOM     45  CG  PHE B 286      -8.148   9.453 -19.867  1.00 10.28           C  
+ATOM     46  CD1 PHE B 286      -7.621  10.656 -19.418  1.00 11.11           C  
+ATOM     47  CD2 PHE B 286      -8.813   9.441 -21.076  1.00 10.22           C  
+ATOM     48  CE1 PHE B 286      -7.775  11.801 -20.136  1.00 11.20           C  
+ATOM     49  CE2 PHE B 286      -8.972  10.605 -21.804  1.00 11.18           C  
+ATOM     50  CZ  PHE B 286      -8.453  11.783 -21.339  1.00  9.15           C  
+ATOM     51  H   PHE B 286      -8.417   6.300 -17.418  1.00 10.77           H  
+ATOM     52  HA  PHE B 286      -8.583   8.980 -17.274  1.00 10.65           H  
+ATOM     53  HB2 PHE B 286      -7.043   8.113 -18.816  1.00 13.14           H  
+ATOM     54  HB3 PHE B 286      -8.244   7.441 -19.612  1.00 13.14           H  
+ATOM     55  HD1 PHE B 286      -7.155  10.680 -18.613  1.00 13.33           H  
+ATOM     56  HD2 PHE B 286      -9.158   8.642 -21.404  1.00 12.26           H  
+ATOM     57  HE1 PHE B 286      -7.422  12.599 -19.815  1.00 13.44           H  
+ATOM     58  HE2 PHE B 286      -9.433  10.588 -22.611  1.00 13.41           H  
+ATOM     59  HZ  PHE B 286      -8.556  12.566 -21.830  1.00 10.98           H  
+ATOM     60  N   LEU B 287     -10.968   9.324 -17.856  1.00  8.99           N  
+ATOM     61  CA  LEU B 287     -12.375   9.507 -18.184  1.00 10.02           C  
+ATOM     62  C   LEU B 287     -12.460  10.438 -19.381  1.00  9.17           C  
+ATOM     63  O   LEU B 287     -12.138  11.632 -19.277  1.00 10.48           O  
+ATOM     64  CB  LEU B 287     -13.134  10.072 -16.992  1.00 12.93           C  
+ATOM     65  CG  LEU B 287     -14.640  10.037 -17.035  1.00 16.19           C  
+ATOM     66  CD1 LEU B 287     -15.169   8.716 -17.494  1.00 20.22           C  
+ATOM     67  CD2 LEU B 287     -15.115  10.308 -15.596  1.00 16.25           C  
+ATOM     68  H   LEU B 287     -10.620  10.001 -17.457  1.00 10.79           H  
+ATOM     69  HA  LEU B 287     -12.773   8.655 -18.423  1.00 12.03           H  
+ATOM     70  HB2 LEU B 287     -12.865   9.571 -16.207  1.00 15.52           H  
+ATOM     71  HB3 LEU B 287     -12.879  11.003 -16.895  1.00 15.52           H  
+ATOM     72  HG  LEU B 287     -14.975  10.694 -17.665  1.00 19.43           H  
+ATOM     73 HD11 LEU B 287     -16.122   8.679 -17.319  1.00 24.26           H  
+ATOM     74 HD12 LEU B 287     -15.004   8.624 -18.446  1.00 24.26           H  
+ATOM     75 HD13 LEU B 287     -14.716   8.009 -17.010  1.00 24.26           H  
+ATOM     76 HD21 LEU B 287     -16.083  10.363 -15.588  1.00 19.50           H  
+ATOM     77 HD22 LEU B 287     -14.820   9.583 -15.024  1.00 19.50           H  
+ATOM     78 HD23 LEU B 287     -14.734  11.146 -15.291  1.00 19.50           H  
+ATOM     79  N   SER B 288     -12.852   9.864 -20.512  1.00  9.19           N  
+ATOM     80  CA  SER B 288     -12.938  10.526 -21.809  1.00 10.58           C  
+ATOM     81  C   SER B 288     -14.400  10.810 -22.120  1.00 10.80           C  
+ATOM     82  O   SER B 288     -15.250   9.934 -21.951  1.00 11.14           O  
+ATOM     83  CB  SER B 288     -12.343   9.595 -22.863  1.00  9.23           C  
+ATOM     84  OG  SER B 288     -12.485  10.130 -24.161  1.00 10.20           O  
+ATOM     85  H   SER B 288     -13.089   9.038 -20.557  1.00 11.02           H  
+ATOM     86  HA  SER B 288     -12.461  11.370 -21.812  1.00 12.70           H  
+ATOM     87  HB2 SER B 288     -11.400   9.472 -22.675  1.00 11.07           H  
+ATOM     88  HB3 SER B 288     -12.803   8.742 -22.823  1.00 11.07           H  
+ATOM     89  HG  SER B 288     -12.057  10.850 -24.224  1.00 12.24           H  
+ATOM     90  N   GLY B 289     -14.686  12.022 -22.562  1.00  9.59           N  
+ATOM     91  CA  GLY B 289     -16.036  12.338 -22.997  1.00 10.63           C  
+ATOM     92  C   GLY B 289     -16.290  13.813 -23.193  1.00 10.07           C  
+ATOM     93  O   GLY B 289     -15.666  14.670 -22.568  1.00 10.05           O  
+ATOM     94  H   GLY B 289     -14.124  12.671 -22.621  1.00 11.51           H  
+ATOM     95  HA2 GLY B 289     -16.208  11.890 -23.840  1.00 12.75           H  
+ATOM     96  HA3 GLY B 289     -16.664  12.012 -22.333  1.00 12.75           H  
+ATOM     97  N   SER B 290     -17.223  14.114 -24.077  1.00  8.59           N  
+ATOM     98  CA  SER B 290     -17.719  15.460 -24.301  1.00 10.19           C  
+ATOM     99  C   SER B 290     -19.153  15.344 -24.792  1.00  9.09           C  
+ATOM    100  O   SER B 290     -19.548  14.321 -25.364  1.00  9.59           O  
+ATOM    101  CB  SER B 290     -16.884  16.218 -25.322  1.00 10.61           C  
+ATOM    102  OG  SER B 290     -16.847  15.489 -26.538  1.00 10.65           O  
+ATOM    103  H   SER B 290     -17.603  13.531 -24.583  1.00 10.31           H  
+ATOM    104  HA  SER B 290     -17.694  15.958 -23.469  1.00 12.23           H  
+ATOM    105  HB2 SER B 290     -17.283  17.087 -25.481  1.00 12.73           H  
+ATOM    106  HB3 SER B 290     -15.981  16.324 -24.984  1.00 12.73           H  
+ATOM    107  HG  SER B 290     -17.618  15.439 -26.867  1.00 12.78           H  
+ATOM    108  N   ALA B 291     -19.930  16.403 -24.565  1.00  9.45           N  
+ATOM    109  CA  ALA B 291     -21.325  16.367 -24.986  1.00  9.23           C  
+ATOM    110  C   ALA B 291     -21.934  17.759 -25.006  1.00 11.39           C  
+ATOM    111  O   ALA B 291     -21.731  18.549 -24.087  1.00 12.17           O  
+ATOM    112  CB  ALA B 291     -22.167  15.493 -24.047  1.00 12.49           C  
+ATOM    113  H   ALA B 291     -19.678  17.131 -24.182  1.00 11.34           H  
+ATOM    114  HA  ALA B 291     -21.342  16.016 -25.890  1.00 11.07           H  
+ATOM    115  HB1 ALA B 291     -23.085  15.487 -24.360  1.00 14.99           H  
+ATOM    116  HB2 ALA B 291     -21.810  14.592 -24.050  1.00 14.99           H  
+ATOM    117  HB3 ALA B 291     -22.126  15.862 -23.151  1.00 14.99           H  
+ATOM    118  N   VAL B 292     -22.722  18.028 -26.039  1.00 13.40           N  
+ATOM    119  CA  VAL B 292     -23.718  19.087 -25.977  1.00 14.98           C  
+ATOM    120  C   VAL B 292     -25.138  18.539 -25.932  1.00 17.46           C  
+ATOM    121  O   VAL B 292     -26.061  19.304 -25.607  1.00 22.06           O  
+ATOM    122  CB  VAL B 292     -23.551  20.092 -27.133  1.00 19.57           C  
+ATOM    123  CG1 VAL B 292     -22.246  20.835 -26.993  1.00 21.68           C  
+ATOM    124  CG2 VAL B 292     -23.618  19.402 -28.473  1.00 21.10           C  
+ATOM    125  H   VAL B 292     -22.699  17.609 -26.790  1.00 16.08           H  
+ATOM    126  HA  VAL B 292     -23.582  19.589 -25.159  1.00 17.97           H  
+ATOM    127  HB  VAL B 292     -24.282  20.729 -27.091  1.00 23.49           H  
+ATOM    128 HG11 VAL B 292     -22.165  21.472 -27.721  1.00 26.01           H  
+ATOM    129 HG12 VAL B 292     -22.237  21.302 -26.143  1.00 26.01           H  
+ATOM    130 HG13 VAL B 292     -21.514  20.199 -27.029  1.00 26.01           H  
+ATOM    131 HG21 VAL B 292     -23.555  20.069 -29.175  1.00 25.32           H  
+ATOM    132 HG22 VAL B 292     -22.879  18.777 -28.544  1.00 25.32           H  
+ATOM    133 HG23 VAL B 292     -24.461  18.927 -28.542  1.00 25.32           H  
+ATOM    134  N   GLU B 293     -25.345  17.253 -26.223  1.00 15.69           N  
+ATOM    135  CA  GLU B 293     -26.615  16.562 -25.975  1.00 21.72           C  
+ATOM    136  C   GLU B 293     -26.328  15.141 -25.494  1.00 17.02           C  
+ATOM    137  O   GLU B 293     -25.209  14.644 -25.633  1.00 15.07           O  
+ATOM    138  CB  GLU B 293     -27.496  16.550 -27.229  1.00 28.01           C  
+ATOM    139  CG  GLU B 293     -26.825  15.921 -28.397  1.00 25.35           C  
+ATOM    140  CD  GLU B 293     -27.762  15.742 -29.598  1.00 28.81           C  
+ATOM    141  OE1 GLU B 293     -28.375  16.744 -30.042  1.00 26.35           O  
+ATOM    142  OE2 GLU B 293     -27.887  14.588 -30.084  1.00 28.75           O  
+ATOM    143  H   GLU B 293     -24.749  16.743 -26.575  1.00 18.83           H  
+ATOM    144  HA  GLU B 293     -27.105  17.015 -25.271  1.00 26.07           H  
+ATOM    145  HB2 GLU B 293     -28.305  16.049 -27.042  1.00 33.61           H  
+ATOM    146  HB3 GLU B 293     -27.720  17.463 -27.467  1.00 33.61           H  
+ATOM    147  HG2 GLU B 293     -26.085  16.483 -28.676  1.00 30.42           H  
+ATOM    148  HG3 GLU B 293     -26.498  15.045 -28.139  1.00 30.42           H  
+ATOM    149  N   TYR B 294     -27.342  14.480 -24.922  1.00 15.59           N  
+ATOM    150  CA  TYR B 294     -27.113  13.314 -24.078  1.00 17.68           C  
+ATOM    151  C   TYR B 294     -28.004  12.129 -24.434  1.00 23.10           C  
+ATOM    152  O   TYR B 294     -28.546  11.445 -23.559  1.00 21.10           O  
+ATOM    153  CB  TYR B 294     -27.339  13.680 -22.615  1.00 16.11           C  
+ATOM    154  CG  TYR B 294     -26.374  14.710 -22.081  1.00 15.23           C  
+ATOM    155  CD1 TYR B 294     -25.121  14.329 -21.640  1.00 14.94           C  
+ATOM    156  CD2 TYR B 294     -26.712  16.048 -22.023  1.00 16.21           C  
+ATOM    157  CE1 TYR B 294     -24.222  15.257 -21.152  1.00 12.43           C  
+ATOM    158  CE2 TYR B 294     -25.826  16.980 -21.515  1.00 16.62           C  
+ATOM    159  CZ  TYR B 294     -24.581  16.568 -21.081  1.00 12.08           C  
+ATOM    160  OH  TYR B 294     -23.726  17.519 -20.582  1.00 15.25           O  
+ATOM    161  H   TYR B 294     -28.170  14.694 -25.013  1.00 18.71           H  
+ATOM    162  HA  TYR B 294     -26.199  13.034 -24.237  1.00 21.22           H  
+ATOM    163  HB2 TYR B 294     -28.236  14.038 -22.520  1.00 19.34           H  
+ATOM    164  HB3 TYR B 294     -27.243  12.879 -22.077  1.00 19.34           H  
+ATOM    165  HD1 TYR B 294     -24.878  13.432 -21.673  1.00 17.93           H  
+ATOM    166  HD2 TYR B 294     -27.546  16.325 -22.328  1.00 19.45           H  
+ATOM    167  HE1 TYR B 294     -23.376  14.988 -20.873  1.00 14.92           H  
+ATOM    168  HE2 TYR B 294     -26.066  17.877 -21.466  1.00 19.94           H  
+ATOM    169  HH  TYR B 294     -22.999  17.162 -20.358  1.00 18.30           H  
+ATOM    170  N   ASN B 295     -28.111  11.835 -25.724  1.00 23.62           N  
+ATOM    171  CA  ASN B 295     -28.775  10.620 -26.214  1.00 27.66           C  
+ATOM    172  C   ASN B 295     -30.242  10.743 -25.808  1.00 27.39           C  
+ATOM    173  O   ASN B 295     -30.877  11.762 -26.115  1.00 26.99           O  
+ATOM    174  CB  ASN B 295     -28.030   9.388 -25.702  1.00 26.89           C  
+ATOM    175  CG  ASN B 295     -28.291   8.149 -26.554  1.00 30.51           C  
+ATOM    176  OD1 ASN B 295     -28.724   8.252 -27.698  1.00 35.33           O  
+ATOM    177  ND2 ASN B 295     -28.027   6.975 -25.992  1.00 29.56           N  
+ATOM    178  H   ASN B 295     -27.801  12.332 -26.354  1.00 28.34           H  
+ATOM    179  HA  ASN B 295     -28.742  10.593 -27.183  1.00 33.19           H  
+ATOM    180  HB2 ASN B 295     -27.077   9.567 -25.714  1.00 32.26           H  
+ATOM    181  HB3 ASN B 295     -28.320   9.197 -24.796  1.00 32.26           H  
+ATOM    182 HD21 ASN B 295     -28.158   6.248 -26.434  1.00 35.47           H  
+ATOM    183 HD22 ASN B 295     -27.725   6.941 -25.188  1.00 35.47           H  
+ATOM    184  N   HIS B 296     -30.818   9.782 -25.111  1.00 35.70           N  
+ATOM    185  CA  HIS B 296     -32.237   9.873 -24.786  1.00 39.76           C  
+ATOM    186  C   HIS B 296     -32.512  10.569 -23.460  1.00 37.93           C  
+ATOM    187  O   HIS B 296     -33.677  10.856 -23.153  1.00 30.45           O  
+ATOM    188  CB  HIS B 296     -32.841   8.468 -24.774  1.00 40.87           C  
+ATOM    189  CG  HIS B 296     -32.352   7.605 -25.895  1.00 47.36           C  
+ATOM    190  ND1 HIS B 296     -32.725   7.809 -27.206  1.00 52.53           N  
+ATOM    191  CD2 HIS B 296     -31.499   6.554 -25.906  1.00 51.57           C  
+ATOM    192  CE1 HIS B 296     -32.133   6.912 -27.975  1.00 55.86           C  
+ATOM    193  NE2 HIS B 296     -31.386   6.137 -27.210  1.00 52.80           N  
+ATOM    194  H   HIS B 296     -30.420   9.078 -24.818  1.00 42.84           H  
+ATOM    195  HA  HIS B 296     -32.688  10.392 -25.471  1.00 47.71           H  
+ATOM    196  HB2 HIS B 296     -32.608   8.033 -23.939  1.00 49.05           H  
+ATOM    197  HB3 HIS B 296     -33.805   8.541 -24.852  1.00 49.05           H  
+ATOM    198  HD2 HIS B 296     -31.070   6.183 -25.169  1.00 61.89           H  
+ATOM    199  HE1 HIS B 296     -32.227   6.839 -28.897  1.00 67.03           H  
+ATOM    200  HE2 HIS B 296     -30.906   5.478 -27.484  1.00 63.36           H  
+ATOM    201  N   TRP B 297     -31.483  10.883 -22.683  1.00 27.53           N  
+ATOM    202  CA  TRP B 297     -31.686  11.227 -21.291  1.00 19.83           C  
+ATOM    203  C   TRP B 297     -31.911  12.721 -21.091  1.00 15.67           C  
+ATOM    204  O   TRP B 297     -31.395  13.569 -21.827  1.00 17.27           O  
+ATOM    205  CB  TRP B 297     -30.492  10.792 -20.434  1.00 29.53           C  
+ATOM    206  CG  TRP B 297     -30.591   9.406 -19.831  1.00 33.26           C  
+ATOM    207  CD1 TRP B 297     -31.667   8.551 -19.855  1.00 33.86           C  
+ATOM    208  CD2 TRP B 297     -29.558   8.723 -19.114  1.00 35.69           C  
+ATOM    209  NE1 TRP B 297     -31.360   7.382 -19.197  1.00 40.11           N  
+ATOM    210  CE2 TRP B 297     -30.072   7.460 -18.735  1.00 39.25           C  
+ATOM    211  CE3 TRP B 297     -28.249   9.062 -18.745  1.00 20.78           C  
+ATOM    212  CZ2 TRP B 297     -29.320   6.536 -18.019  1.00 36.11           C  
+ATOM    213  CZ3 TRP B 297     -27.513   8.150 -18.052  1.00 22.03           C  
+ATOM    214  CH2 TRP B 297     -28.042   6.899 -17.683  1.00 31.35           C  
+ATOM    215  H   TRP B 297     -30.663  10.903 -22.942  1.00 33.03           H  
+ATOM    216  HA  TRP B 297     -32.482  10.761 -20.992  1.00 23.80           H  
+ATOM    217  HB2 TRP B 297     -29.696  10.810 -20.988  1.00 35.43           H  
+ATOM    218  HB3 TRP B 297     -30.399  11.420 -19.700  1.00 35.43           H  
+ATOM    219  HD1 TRP B 297     -32.484   8.735 -20.258  1.00 40.63           H  
+ATOM    220  HE1 TRP B 297     -31.889   6.713 -19.092  1.00 48.13           H  
+ATOM    221  HE3 TRP B 297     -27.892   9.890 -18.969  1.00 24.94           H  
+ATOM    222  HZ2 TRP B 297     -29.668   5.708 -17.779  1.00 43.33           H  
+ATOM    223  HZ3 TRP B 297     -26.638   8.360 -17.816  1.00 26.43           H  
+ATOM    224  HH2 TRP B 297     -27.513   6.306 -17.200  1.00 37.63           H  
+ATOM    225  N   GLU B 298     -32.716  13.030 -20.081  1.00 14.56           N  
+ATOM    226  CA  GLU B 298     -32.881  14.400 -19.629  1.00 14.36           C  
+ATOM    227  C   GLU B 298     -31.526  14.951 -19.218  1.00 16.18           C  
+ATOM    228  O   GLU B 298     -30.699  14.238 -18.648  1.00 14.17           O  
+ATOM    229  CB  GLU B 298     -33.877  14.434 -18.453  1.00 19.20           C  
+ATOM    230  CG  GLU B 298     -33.888  15.722 -17.655  1.00 25.22           C  
+ATOM    231  CD  GLU B 298     -34.895  15.702 -16.512  1.00 35.40           C  
+ATOM    232  OE1 GLU B 298     -35.973  15.087 -16.682  1.00 32.70           O  
+ATOM    233  OE2 GLU B 298     -34.610  16.311 -15.454  1.00 37.50           O  
+ATOM    234  H   GLU B 298     -33.181  12.459 -19.637  1.00 17.47           H  
+ATOM    235  HA  GLU B 298     -33.239  14.963 -20.333  1.00 17.23           H  
+ATOM    236  HB2 GLU B 298     -34.771  14.304 -18.806  1.00 23.04           H  
+ATOM    237  HB3 GLU B 298     -33.654  13.716 -17.841  1.00 23.04           H  
+ATOM    238  HG2 GLU B 298     -33.007  15.866 -17.276  1.00 30.27           H  
+ATOM    239  HG3 GLU B 298     -34.120  16.457 -18.245  1.00 30.27           H  
+ATOM    240  N   THR B 299     -31.286  16.216 -19.545  1.00 13.91           N  
+ATOM    241  CA  THR B 299     -29.973  16.819 -19.306  1.00 14.37           C  
+ATOM    242  C   THR B 299     -29.510  16.636 -17.871  1.00 14.98           C  
+ATOM    243  O   THR B 299     -28.383  16.177 -17.624  1.00 14.68           O  
+ATOM    244  CB  THR B 299     -30.021  18.297 -19.665  1.00 13.25           C  
+ATOM    245  OG1 THR B 299     -30.362  18.427 -21.037  1.00 16.27           O  
+ATOM    246  CG2 THR B 299     -28.657  18.961 -19.395  1.00 16.99           C  
+ATOM    247  H   THR B 299     -31.860  16.746 -19.904  1.00 16.69           H  
+ATOM    248  HA  THR B 299     -29.324  16.377 -19.877  1.00 17.25           H  
+ATOM    249  HB  THR B 299     -30.685  18.751 -19.123  1.00 15.90           H  
+ATOM    250  HG1 THR B 299     -30.425  19.239 -21.241  1.00 19.53           H  
+ATOM    251 HG21 THR B 299     -28.619  19.829 -19.827  1.00 20.39           H  
+ATOM    252 HG22 THR B 299     -28.528  19.078 -18.441  1.00 20.39           H  
+ATOM    253 HG23 THR B 299     -27.942  18.404 -19.743  1.00 20.39           H  
+ATOM    254  N   GLU B 300     -30.362  16.976 -16.898  1.00 13.85           N  
+ATOM    255  CA  GLU B 300     -29.914  16.875 -15.511  1.00 16.28           C  
+ATOM    256  C   GLU B 300     -29.644  15.430 -15.117  1.00 14.26           C  
+ATOM    257  O   GLU B 300     -28.742  15.168 -14.310  1.00 14.99           O  
+ATOM    258  CB  GLU B 300     -30.945  17.495 -14.560  1.00 20.66           C  
+ATOM    259  CG  GLU B 300     -30.560  17.332 -13.096  1.00 29.72           C  
+ATOM    260  CD  GLU B 300     -31.371  18.200 -12.152  1.00 47.94           C  
+ATOM    261  OE1 GLU B 300     -32.601  18.312 -12.340  1.00 57.36           O  
+ATOM    262  OE2 GLU B 300     -30.766  18.770 -11.220  1.00 51.96           O  
+ATOM    263  H   GLU B 300     -31.168  17.254 -17.011  1.00 16.62           H  
+ATOM    264  HA  GLU B 300     -29.089  17.378 -15.419  1.00 19.54           H  
+ATOM    265  HB2 GLU B 300     -31.019  18.444 -14.749  1.00 24.80           H  
+ATOM    266  HB3 GLU B 300     -31.802  17.062 -14.697  1.00 24.80           H  
+ATOM    267  HG2 GLU B 300     -30.697  16.407 -12.838  1.00 35.67           H  
+ATOM    268  HG3 GLU B 300     -29.626  17.572 -12.989  1.00 35.67           H  
+ATOM    269  N  AHIS B 301     -30.419  14.494 -15.666  0.44 15.38           N  
+ATOM    270  N  BHIS B 301     -30.408  14.478 -15.655  0.56 15.31           N  
+ATOM    271  CA AHIS B 301     -30.205  13.073 -15.418  0.44 14.58           C  
+ATOM    272  CA BHIS B 301     -30.151  13.076 -15.345  0.56 14.44           C  
+ATOM    273  C  AHIS B 301     -28.842  12.618 -15.925  0.44 14.63           C  
+ATOM    274  C  BHIS B 301     -28.811  12.614 -15.914  0.56 14.61           C  
+ATOM    275  O  AHIS B 301     -28.149  11.845 -15.254  0.44 14.49           O  
+ATOM    276  O  BHIS B 301     -28.111  11.813 -15.283  0.56 14.46           O  
+ATOM    277  CB AHIS B 301     -31.326  12.287 -16.101  0.44 18.97           C  
+ATOM    278  CB BHIS B 301     -31.277  12.190 -15.882  0.56 18.72           C  
+ATOM    279  CG AHIS B 301     -31.605  10.946 -15.499  0.44 19.17           C  
+ATOM    280  CG BHIS B 301     -32.587  12.369 -15.180  0.56 20.64           C  
+ATOM    281  ND1AHIS B 301     -31.499   9.775 -16.218  0.44 23.72           N  
+ATOM    282  ND1BHIS B 301     -33.620  11.464 -15.298  0.56 30.78           N  
+ATOM    283  CD2AHIS B 301     -32.023  10.590 -14.261  0.44 18.39           C  
+ATOM    284  CD2BHIS B 301     -33.039  13.350 -14.365  0.56 24.10           C  
+ATOM    285  CE1AHIS B 301     -31.832   8.755 -15.449  0.44 18.38           C  
+ATOM    286  CE1BHIS B 301     -34.648  11.876 -14.578  0.56 26.57           C  
+ATOM    287  NE2AHIS B 301     -32.146   9.220 -14.254  0.44 19.93           N  
+ATOM    288  NE2BHIS B 301     -34.321  13.017 -14.002  0.56 27.47           N  
+ATOM    289  H  AHIS B 301     -31.082  14.658 -16.190  0.44 18.45           H  
+ATOM    290  H  BHIS B 301     -31.067  14.616 -16.190  0.56 18.37           H  
+ATOM    291  HA AHIS B 301     -30.229  12.899 -14.464  0.44 17.50           H  
+ATOM    292  HA BHIS B 301     -30.125  12.982 -14.380  0.56 17.33           H  
+ATOM    293  HB2AHIS B 301     -32.143  12.807 -16.048  0.44 22.76           H  
+ATOM    294  HB2BHIS B 301     -31.415  12.398 -16.820  0.56 22.47           H  
+ATOM    295  HB3AHIS B 301     -31.082  12.145 -17.029  0.44 22.76           H  
+ATOM    296  HB3BHIS B 301     -31.015  11.261 -15.784  0.56 22.47           H  
+ATOM    297  HD1AHIS B 301     -31.253   9.718 -17.040  0.44 28.47           H  
+ATOM    298  HD2AHIS B 301     -32.195  11.164 -13.549  0.44 22.07           H  
+ATOM    299  HD2BHIS B 301     -32.569  14.107 -14.101  0.56 28.91           H  
+ATOM    300  HE1AHIS B 301     -31.844   7.861 -15.706  0.44 22.05           H  
+ATOM    301  HE1BHIS B 301     -35.463  11.436 -14.492  0.56 31.89           H  
+ATOM    302  HE2BHIS B 301     -34.829  13.479 -13.483  0.56 32.97           H  
+ATOM    303  N   ALA B 302     -28.448  13.071 -17.120  1.00 13.51           N  
+ATOM    304  CA  ALA B 302     -27.150  12.677 -17.681  1.00 12.96           C  
+ATOM    305  C   ALA B 302     -26.018  13.290 -16.879  1.00 12.72           C  
+ATOM    306  O   ALA B 302     -24.996  12.638 -16.619  1.00 12.71           O  
+ATOM    307  CB  ALA B 302     -27.049  13.108 -19.144  1.00 14.63           C  
+ATOM    308  H  AALA B 302     -28.905  13.600 -17.620  0.44 16.22           H  
+ATOM    309  H  BALA B 302     -28.918  13.592 -17.616  0.56 16.22           H  
+ATOM    310  HA  ALA B 302     -27.074  11.711 -17.650  1.00 15.55           H  
+ATOM    311  HB1 ALA B 302     -26.185  12.838 -19.494  1.00 17.55           H  
+ATOM    312  HB2 ALA B 302     -27.758  12.680 -19.649  1.00 17.55           H  
+ATOM    313  HB3 ALA B 302     -27.141  14.072 -19.197  1.00 17.55           H  
+ATOM    314  N   GLU B 303     -26.186  14.551 -16.487  1.00 12.69           N  
+ATOM    315  CA  GLU B 303     -25.208  15.199 -15.615  1.00 12.38           C  
+ATOM    316  C   GLU B 303     -25.071  14.458 -14.302  1.00 12.10           C  
+ATOM    317  O   GLU B 303     -23.953  14.282 -13.804  1.00 12.40           O  
+ATOM    318  CB  GLU B 303     -25.635  16.648 -15.360  1.00 12.87           C  
+ATOM    319  CG  GLU B 303     -25.617  17.518 -16.576  1.00 14.32           C  
+ATOM    320  CD  GLU B 303     -26.177  18.927 -16.305  1.00 17.16           C  
+ATOM    321  OE1 GLU B 303     -26.719  19.152 -15.209  1.00 21.73           O  
+ATOM    322  OE2 GLU B 303     -26.058  19.796 -17.187  1.00 21.16           O  
+ATOM    323  H   GLU B 303     -26.850  15.050 -16.709  1.00 15.23           H  
+ATOM    324  HA  GLU B 303     -24.344  15.202 -16.054  1.00 14.86           H  
+ATOM    325  HB2 GLU B 303     -26.540  16.647 -15.012  1.00 15.44           H  
+ATOM    326  HB3 GLU B 303     -25.030  17.038 -14.710  1.00 15.44           H  
+ATOM    327  HG2 GLU B 303     -24.702  17.613 -16.884  1.00 17.19           H  
+ATOM    328  HG3 GLU B 303     -26.159  17.108 -17.267  1.00 17.19           H  
+ATOM    329  N   GLN B 304     -26.202  14.029 -13.715  1.00 13.48           N  
+ATOM    330  CA  GLN B 304     -26.161  13.263 -12.476  1.00 14.43           C  
+ATOM    331  C   GLN B 304     -25.454  11.922 -12.677  1.00 12.83           C  
+ATOM    332  O   GLN B 304     -24.710  11.465 -11.802  1.00 13.40           O  
+ATOM    333  CB  GLN B 304     -27.581  13.044 -11.938  1.00 17.70           C  
+ATOM    334  CG  GLN B 304     -27.617  12.411 -10.550  1.00 26.04           C  
+ATOM    335  CD  GLN B 304     -27.004  13.309  -9.473  1.00 37.45           C  
+ATOM    336  OE1 GLN B 304     -26.954  14.537  -9.614  1.00 38.90           O  
+ATOM    337  NE2 GLN B 304     -26.529  12.695  -8.392  1.00 40.52           N  
+ATOM    338  H   GLN B 304     -26.994  14.171 -14.017  1.00 16.18           H  
+ATOM    339  HA  GLN B 304     -25.665  13.771 -11.815  1.00 17.31           H  
+ATOM    340  HB2 GLN B 304     -28.031  13.902 -11.885  1.00 21.24           H  
+ATOM    341  HB3 GLN B 304     -28.058  12.456 -12.545  1.00 21.24           H  
+ATOM    342  HG2 GLN B 304     -28.540  12.238 -10.305  1.00 31.25           H  
+ATOM    343  HG3 GLN B 304     -27.117  11.581 -10.568  1.00 31.25           H  
+ATOM    344 HE21 GLN B 304     -26.577  11.839  -8.329  1.00 48.63           H  
+ATOM    345 HE22 GLN B 304     -26.174  13.154  -7.758  1.00 48.63           H  
+ATOM    346  N   PHE B 305     -25.671  11.276 -13.826  1.00 11.91           N  
+ATOM    347  CA  PHE B 305     -24.958  10.034 -14.122  1.00 10.92           C  
+ATOM    348  C   PHE B 305     -23.447  10.251 -14.094  1.00 11.31           C  
+ATOM    349  O   PHE B 305     -22.706   9.476 -13.482  1.00 10.19           O  
+ATOM    350  CB  PHE B 305     -25.414   9.486 -15.481  1.00 11.52           C  
+ATOM    351  CG  PHE B 305     -24.454   8.503 -16.102  1.00 10.53           C  
+ATOM    352  CD1 PHE B 305     -24.231   7.264 -15.543  1.00 11.47           C  
+ATOM    353  CD2 PHE B 305     -23.748   8.845 -17.238  1.00 11.66           C  
+ATOM    354  CE1 PHE B 305     -23.338   6.373 -16.119  1.00 11.92           C  
+ATOM    355  CE2 PHE B 305     -22.837   7.969 -17.802  1.00 13.53           C  
+ATOM    356  CZ  PHE B 305     -22.644   6.739 -17.266  1.00 11.46           C  
+ATOM    357  H   PHE B 305     -26.216  11.532 -14.440  1.00 14.29           H  
+ATOM    358  HA  PHE B 305     -25.175   9.373 -13.446  1.00 13.10           H  
+ATOM    359  HB2 PHE B 305     -26.264   9.033 -15.364  1.00 13.82           H  
+ATOM    360  HB3 PHE B 305     -25.515  10.228 -16.097  1.00 13.82           H  
+ATOM    361  HD1 PHE B 305     -24.687   7.021 -14.769  1.00 13.76           H  
+ATOM    362  HD2 PHE B 305     -23.886   9.677 -17.631  1.00 14.00           H  
+ATOM    363  HE1 PHE B 305     -23.203   5.535 -15.739  1.00 14.30           H  
+ATOM    364  HE2 PHE B 305     -22.354   8.225 -18.554  1.00 16.24           H  
+ATOM    365  HZ  PHE B 305     -22.051   6.143 -17.664  1.00 13.75           H  
+ATOM    366  N   ILE B 306     -22.978  11.310 -14.746  1.00 10.65           N  
+ATOM    367  CA  ILE B 306     -21.539  11.572 -14.797  1.00  9.83           C  
+ATOM    368  C   ILE B 306     -21.006  11.862 -13.403  1.00  9.96           C  
+ATOM    369  O   ILE B 306     -19.962  11.344 -12.982  1.00 10.18           O  
+ATOM    370  CB  ILE B 306     -21.258  12.735 -15.763  1.00 10.35           C  
+ATOM    371  CG1 ILE B 306     -21.673  12.357 -17.181  1.00 10.99           C  
+ATOM    372  CG2 ILE B 306     -19.782  13.125 -15.725  1.00 12.49           C  
+ATOM    373  CD1 ILE B 306     -21.723  13.507 -18.124  1.00 12.61           C  
+ATOM    374  H   ILE B 306     -23.462  11.886 -15.163  1.00 12.79           H  
+ATOM    375  HA  ILE B 306     -21.084  10.781 -15.127  1.00 11.79           H  
+ATOM    376  HB  ILE B 306     -21.783  13.499 -15.479  1.00 12.42           H  
+ATOM    377 HG12 ILE B 306     -21.035  11.716 -17.531  1.00 13.19           H  
+ATOM    378 HG13 ILE B 306     -22.558  11.962 -17.151  1.00 13.19           H  
+ATOM    379 HG21 ILE B 306     -19.591  13.713 -16.472  1.00 14.98           H  
+ATOM    380 HG22 ILE B 306     -19.597  13.582 -14.889  1.00 14.98           H  
+ATOM    381 HG23 ILE B 306     -19.241  12.322 -15.789  1.00 14.98           H  
+ATOM    382 HD11 ILE B 306     -22.182  13.232 -18.933  1.00 15.14           H  
+ATOM    383 HD12 ILE B 306     -22.201  14.239 -17.704  1.00 15.14           H  
+ATOM    384 HD13 ILE B 306     -20.817  13.781 -18.335  1.00 15.14           H  
+ATOM    385  N   HIS B 307     -21.734  12.699 -12.673  1.00 11.49           N  
+ATOM    386  CA  HIS B 307     -21.437  13.037 -11.284  1.00 10.82           C  
+ATOM    387  C   HIS B 307     -21.345  11.796 -10.408  1.00 11.60           C  
+ATOM    388  O   HIS B 307     -20.369  11.610  -9.658  1.00 11.49           O  
+ATOM    389  CB  HIS B 307     -22.554  13.979 -10.833  1.00 11.55           C  
+ATOM    390  CG  HIS B 307     -22.548  14.349  -9.391  1.00 11.87           C  
+ATOM    391  ND1 HIS B 307     -22.388  15.653  -8.978  1.00 14.12           N  
+ATOM    392  CD2 HIS B 307     -22.775  13.623  -8.274  1.00 16.54           C  
+ATOM    393  CE1 HIS B 307     -22.464  15.705  -7.659  1.00 15.47           C  
+ATOM    394  NE2 HIS B 307     -22.700  14.488  -7.208  1.00 17.61           N  
+ATOM    395  H   HIS B 307     -22.433  13.103 -12.968  1.00 13.79           H  
+ATOM    396  HA  HIS B 307     -20.577  13.476 -11.199  1.00 12.98           H  
+ATOM    397  HB2 HIS B 307     -22.481  14.802 -11.341  1.00 13.86           H  
+ATOM    398  HB3 HIS B 307     -23.405  13.551 -11.015  1.00 13.86           H  
+ATOM    399  HD2 HIS B 307     -22.948  12.710  -8.234  1.00 19.85           H  
+ATOM    400  HE1 HIS B 307     -22.367  16.469  -7.138  1.00 18.56           H  
+ATOM    401  HE2 HIS B 307     -22.792  14.271  -6.381  1.00 21.13           H  
+ATOM    402  N   GLN B 308     -22.375  10.943 -10.464  1.00 10.59           N  
+ATOM    403  CA  GLN B 308     -22.422   9.762  -9.611  1.00 11.45           C  
+ATOM    404  C   GLN B 308     -21.378   8.725 -10.004  1.00 10.37           C  
+ATOM    405  O   GLN B 308     -20.837   8.030  -9.126  1.00 12.00           O  
+ATOM    406  CB  GLN B 308     -23.829   9.152  -9.649  1.00 13.98           C  
+ATOM    407  CG  GLN B 308     -24.826   9.795  -8.736  1.00 28.64           C  
+ATOM    408  CD  GLN B 308     -24.421   9.709  -7.278  1.00 13.75           C  
+ATOM    409  OE1 GLN B 308     -24.321  10.722  -6.624  1.00 31.12           O  
+ATOM    410  NE2 GLN B 308     -24.138   8.504  -6.798  1.00 22.30           N  
+ATOM    411  H   GLN B 308     -23.053  11.029 -10.985  1.00 12.70           H  
+ATOM    412  HA  GLN B 308     -22.227  10.035  -8.701  1.00 13.74           H  
+ATOM    413  HB2 GLN B 308     -24.172   9.229 -10.553  1.00 16.77           H  
+ATOM    414  HB3 GLN B 308     -23.765   8.218  -9.397  1.00 16.77           H  
+ATOM    415  HG2 GLN B 308     -24.910  10.733  -8.970  1.00 34.36           H  
+ATOM    416  HG3 GLN B 308     -25.681   9.350  -8.837  1.00 34.36           H  
+ATOM    417 HE21 GLN B 308     -24.189   7.814  -7.309  1.00 26.76           H  
+ATOM    418 HE22 GLN B 308     -23.904   8.413  -5.975  1.00 26.76           H  
+ATOM    419  N   LEU B 309     -21.109   8.575 -11.302  1.00 10.16           N  
+ATOM    420  CA  LEU B 309     -20.038   7.679 -11.743  1.00  8.69           C  
+ATOM    421  C   LEU B 309     -18.719   8.105 -11.121  1.00  9.65           C  
+ATOM    422  O   LEU B 309     -17.941   7.279 -10.639  1.00 10.81           O  
+ATOM    423  CB  LEU B 309     -19.936   7.685 -13.268  1.00 10.36           C  
+ATOM    424  CG  LEU B 309     -18.733   6.942 -13.860  1.00 11.26           C  
+ATOM    425  CD1 LEU B 309     -18.730   5.464 -13.494  1.00 12.30           C  
+ATOM    426  CD2 LEU B 309     -18.691   7.148 -15.370  1.00 12.22           C  
+ATOM    427  H   LEU B 309     -21.525   8.975 -11.940  1.00 12.20           H  
+ATOM    428  HA  LEU B 309     -20.243   6.773 -11.466  1.00 10.42           H  
+ATOM    429  HB2 LEU B 309     -20.735   7.269 -13.626  1.00 12.43           H  
+ATOM    430  HB3 LEU B 309     -19.880   8.607 -13.564  1.00 12.43           H  
+ATOM    431  HG  LEU B 309     -17.920   7.311 -13.479  1.00 13.51           H  
+ATOM    432 HD11 LEU B 309     -17.969   5.035 -13.916  1.00 14.76           H  
+ATOM    433 HD12 LEU B 309     -18.666   5.378 -12.530  1.00 14.76           H  
+ATOM    434 HD13 LEU B 309     -19.554   5.059 -13.808  1.00 14.76           H  
+ATOM    435 HD21 LEU B 309     -17.925   6.676 -15.732  1.00 14.66           H  
+ATOM    436 HD22 LEU B 309     -19.508   6.798 -15.758  1.00 14.66           H  
+ATOM    437 HD23 LEU B 309     -18.615   8.096 -15.558  1.00 14.66           H  
+ATOM    438  N   SER B 310     -18.444   9.398 -11.162  1.00 10.44           N  
+ATOM    439  CA  SER B 310     -17.180   9.917 -10.663  1.00 10.94           C  
+ATOM    440  C   SER B 310     -17.096   9.736  -9.158  1.00 12.97           C  
+ATOM    441  O   SER B 310     -16.069   9.294  -8.625  1.00 10.76           O  
+ATOM    442  CB  SER B 310     -17.041  11.380 -11.077  1.00 11.00           C  
+ATOM    443  OG  SER B 310     -17.112  11.522 -12.501  1.00 12.22           O  
+ATOM    444  H   SER B 310     -18.973  10.001 -11.474  1.00 12.53           H  
+ATOM    445  HA  SER B 310     -16.434   9.436 -11.054  1.00 13.13           H  
+ATOM    446  HB2 SER B 310     -17.760  11.891 -10.673  1.00 13.20           H  
+ATOM    447  HB3 SER B 310     -16.184  11.714 -10.769  1.00 13.20           H  
+ATOM    448  HG  SER B 310     -17.853  11.243 -12.781  1.00 14.66           H  
+ATOM    449  N   LYS B 311     -18.193  10.013  -8.462  1.00 11.53           N  
+ATOM    450  CA  LYS B 311     -18.236   9.825  -7.015  1.00 12.76           C  
+ATOM    451  C   LYS B 311     -18.000   8.369  -6.631  1.00 12.26           C  
+ATOM    452  O   LYS B 311     -17.241   8.075  -5.699  1.00 13.41           O  
+ATOM    453  CB  LYS B 311     -19.576  10.326  -6.482  1.00 13.64           C  
+ATOM    454  CG  LYS B 311     -19.706  10.205  -4.980  1.00 17.86           C  
+ATOM    455  CD  LYS B 311     -20.842  11.081  -4.473  1.00 24.44           C  
+ATOM    456  CE  LYS B 311     -22.149  10.352  -4.477  1.00 27.62           C  
+ATOM    457  NZ  LYS B 311     -23.208  11.276  -3.955  1.00 32.49           N  
+ATOM    458  H   LYS B 311     -18.925  10.311  -8.801  1.00 13.83           H  
+ATOM    459  HA  LYS B 311     -17.529  10.346  -6.606  1.00 15.31           H  
+ATOM    460  HB2 LYS B 311     -19.675  11.263  -6.715  1.00 16.36           H  
+ATOM    461  HB3 LYS B 311     -20.288   9.807  -6.886  1.00 16.36           H  
+ATOM    462  HG2 LYS B 311     -19.897   9.284  -4.743  1.00 21.43           H  
+ATOM    463  HG3 LYS B 311     -18.882  10.492  -4.557  1.00 21.43           H  
+ATOM    464  HD2 LYS B 311     -20.651  11.358  -3.564  1.00 29.33           H  
+ATOM    465  HD3 LYS B 311     -20.926  11.859  -5.047  1.00 29.33           H  
+ATOM    466  HE2 LYS B 311     -22.378  10.084  -5.381  1.00 33.14           H  
+ATOM    467  HE3 LYS B 311     -22.097   9.572  -3.903  1.00 33.14           H  
+ATOM    468  HZ1 LYS B 311     -23.007  11.532  -3.127  1.00 38.99           H  
+ATOM    469  HZ2 LYS B 311     -23.266  11.996  -4.475  1.00 38.99           H  
+ATOM    470  HZ3 LYS B 311     -23.996  10.862  -3.947  1.00 38.99           H  
+ATOM    471  N   GLU B 312     -18.662   7.433  -7.312  1.00 11.27           N  
+ATOM    472  CA  GLU B 312     -18.527   6.029  -6.957  1.00 10.53           C  
+ATOM    473  C   GLU B 312     -17.156   5.492  -7.352  1.00 10.56           C  
+ATOM    474  O   GLU B 312     -16.640   4.596  -6.685  1.00 11.40           O  
+ATOM    475  CB  GLU B 312     -19.677   5.228  -7.580  1.00 13.15           C  
+ATOM    476  CG  GLU B 312     -21.029   5.586  -6.909  1.00 13.39           C  
+ATOM    477  CD  GLU B 312     -22.229   4.753  -7.353  1.00 15.92           C  
+ATOM    478  OE1 GLU B 312     -22.082   3.553  -7.602  1.00 15.25           O  
+ATOM    479  OE2 GLU B 312     -23.334   5.339  -7.427  1.00 21.20           O  
+ATOM    480  H   GLU B 312     -19.187   7.587  -7.975  1.00 13.53           H  
+ATOM    481  HA  GLU B 312     -18.603   5.916  -5.997  1.00 12.64           H  
+ATOM    482  HB2 GLU B 312     -19.738   5.433  -8.526  1.00 15.77           H  
+ATOM    483  HB3 GLU B 312     -19.513   4.280  -7.457  1.00 15.77           H  
+ATOM    484  HG2 GLU B 312     -20.935   5.468  -5.951  1.00 16.07           H  
+ATOM    485  HG3 GLU B 312     -21.233   6.513  -7.110  1.00 16.07           H  
+ATOM    486  N   LEU B 313     -16.537   6.021  -8.409  1.00 10.87           N  
+ATOM    487  CA  LEU B 313     -15.154   5.641  -8.690  1.00 10.50           C  
+ATOM    488  C   LEU B 313     -14.253   6.000  -7.517  1.00 10.29           C  
+ATOM    489  O   LEU B 313     -13.405   5.197  -7.105  1.00 10.61           O  
+ATOM    490  CB  LEU B 313     -14.662   6.311  -9.972  1.00 10.59           C  
+ATOM    491  CG  LEU B 313     -15.103   5.618 -11.256  1.00  9.67           C  
+ATOM    492  CD1 LEU B 313     -14.946   6.571 -12.454  1.00 12.40           C  
+ATOM    493  CD2 LEU B 313     -14.312   4.338 -11.517  1.00 11.56           C  
+ATOM    494  H   LEU B 313     -16.883   6.583  -8.960  1.00 13.04           H  
+ATOM    495  HA  LEU B 313     -15.116   4.682  -8.830  1.00 12.61           H  
+ATOM    496  HB2 LEU B 313     -15.003   7.219  -9.996  1.00 12.71           H  
+ATOM    497  HB3 LEU B 313     -13.692   6.322  -9.962  1.00 12.71           H  
+ATOM    498  HG  LEU B 313     -16.036   5.373 -11.156  1.00 11.60           H  
+ATOM    499 HD11 LEU B 313     -15.237   6.116 -13.260  1.00 14.88           H  
+ATOM    500 HD12 LEU B 313     -15.490   7.359 -12.304  1.00 14.88           H  
+ATOM    501 HD13 LEU B 313     -14.013   6.824 -12.536  1.00 14.88           H  
+ATOM    502 HD21 LEU B 313     -14.611   3.947 -12.353  1.00 13.87           H  
+ATOM    503 HD22 LEU B 313     -13.368   4.556 -11.572  1.00 13.87           H  
+ATOM    504 HD23 LEU B 313     -14.466   3.718 -10.788  1.00 13.87           H  
+ATOM    505  N   ILE B 314     -14.426   7.212  -6.973  1.00 10.85           N  
+ATOM    506  CA  ILE B 314     -13.673   7.637  -5.795  1.00 11.15           C  
+ATOM    507  C   ILE B 314     -13.970   6.718  -4.616  1.00 11.31           C  
+ATOM    508  O   ILE B 314     -13.059   6.289  -3.895  1.00 11.65           O  
+ATOM    509  CB  ILE B 314     -13.996   9.097  -5.448  1.00 10.95           C  
+ATOM    510  CG1 ILE B 314     -13.546  10.040  -6.541  1.00 15.96           C  
+ATOM    511  CG2 ILE B 314     -13.346   9.468  -4.101  1.00 14.32           C  
+ATOM    512  CD1 ILE B 314     -12.094   9.906  -6.893  1.00 15.51           C  
+ATOM    513  H   ILE B 314     -14.975   7.804  -7.269  1.00 13.02           H  
+ATOM    514  HA  ILE B 314     -12.727   7.575  -6.001  1.00 13.38           H  
+ATOM    515  HB  ILE B 314     -14.959   9.183  -5.372  1.00 13.14           H  
+ATOM    516 HG12 ILE B 314     -14.063   9.859  -7.342  1.00 19.15           H  
+ATOM    517 HG13 ILE B 314     -13.697  10.952  -6.248  1.00 19.15           H  
+ATOM    518 HG21 ILE B 314     -13.292  10.434  -4.032  1.00 17.18           H  
+ATOM    519 HG22 ILE B 314     -13.890   9.115  -3.380  1.00 17.18           H  
+ATOM    520 HG23 ILE B 314     -12.456   9.083  -4.063  1.00 17.18           H  
+ATOM    521 HD11 ILE B 314     -11.813  10.696  -7.382  1.00 18.61           H  
+ATOM    522 HD12 ILE B 314     -11.577   9.821  -6.077  1.00 18.61           H  
+ATOM    523 HD13 ILE B 314     -11.974   9.117  -7.444  1.00 18.61           H  
+ATOM    524  N   ARG B 315     -15.251   6.414  -4.390  1.00 10.39           N  
+ATOM    525  CA  ARG B 315     -15.610   5.529  -3.282  1.00 12.35           C  
+ATOM    526  C   ARG B 315     -14.948   4.169  -3.381  1.00 14.63           C  
+ATOM    527  O   ARG B 315     -14.559   3.583  -2.358  1.00 15.14           O  
+ATOM    528  CB  ARG B 315     -17.120   5.309  -3.230  1.00 15.86           C  
+ATOM    529  CG  ARG B 315     -17.824   6.431  -2.626  1.00 17.24           C  
+ATOM    530  CD  ARG B 315     -19.318   6.184  -2.592  1.00 15.87           C  
+ATOM    531  NE  ARG B 315     -19.930   7.323  -1.948  1.00 16.76           N  
+ATOM    532  CZ  ARG B 315     -21.218   7.604  -2.008  1.00 15.62           C  
+ATOM    533  NH1 ARG B 315     -22.062   6.821  -2.657  1.00 16.25           N  
+ATOM    534  NH2 ARG B 315     -21.666   8.698  -1.404  1.00 17.69           N  
+ATOM    535  H   ARG B 315     -15.916   6.701  -4.853  1.00 12.47           H  
+ATOM    536  HA  ARG B 315     -15.311   5.971  -2.472  1.00 14.82           H  
+ATOM    537  HB2 ARG B 315     -17.455   5.194  -4.133  1.00 19.03           H  
+ATOM    538  HB3 ARG B 315     -17.308   4.517  -2.704  1.00 19.03           H  
+ATOM    539  HG2 ARG B 315     -17.514   6.555  -1.716  1.00 20.68           H  
+ATOM    540  HG3 ARG B 315     -17.659   7.234  -3.145  1.00 20.68           H  
+ATOM    541  HD2 ARG B 315     -19.665   6.098  -3.493  1.00 19.05           H  
+ATOM    542  HD3 ARG B 315     -19.515   5.382  -2.083  1.00 19.05           H  
+ATOM    543  HE  ARG B 315     -19.423   7.852  -1.497  1.00 20.11           H  
+ATOM    544 HH11 ARG B 315     -21.774   6.112  -3.051  1.00 19.51           H  
+ATOM    545 HH12 ARG B 315     -22.898   7.019  -2.686  1.00 19.51           H  
+ATOM    546 HH21 ARG B 315     -21.119   9.211  -0.983  1.00 21.23           H  
+ATOM    547 HH22 ARG B 315     -22.502   8.895  -1.434  1.00 21.23           H  
+ATOM    548  N   LYS B 316     -14.866   3.617  -4.586  1.00 13.26           N  
+ATOM    549  CA  LYS B 316     -14.281   2.306  -4.827  1.00 12.14           C  
+ATOM    550  C   LYS B 316     -12.772   2.380  -5.057  1.00 12.06           C  
+ATOM    551  O   LYS B 316     -12.172   1.423  -5.575  1.00 15.38           O  
+ATOM    552  CB  LYS B 316     -14.988   1.636  -6.004  1.00 17.87           C  
+ATOM    553  CG  LYS B 316     -16.517   1.517  -5.881  1.00 26.40           C  
+ATOM    554  CD  LYS B 316     -16.940   0.526  -4.843  1.00 29.69           C  
+ATOM    555  CE  LYS B 316     -18.377   0.016  -5.060  1.00 22.84           C  
+ATOM    556  NZ  LYS B 316     -19.403   1.066  -4.811  1.00 31.84           N  
+ATOM    557  H   LYS B 316     -15.153   3.996  -5.303  1.00 15.91           H  
+ATOM    558  HA  LYS B 316     -14.423   1.744  -4.049  1.00 14.57           H  
+ATOM    559  HB2 LYS B 316     -14.803   2.152  -6.804  1.00 21.44           H  
+ATOM    560  HB3 LYS B 316     -14.636   0.737  -6.099  1.00 21.44           H  
+ATOM    561  HG2 LYS B 316     -16.883   2.381  -5.636  1.00 31.68           H  
+ATOM    562  HG3 LYS B 316     -16.882   1.232  -6.733  1.00 31.68           H  
+ATOM    563  HD2 LYS B 316     -16.343  -0.238  -4.872  1.00 35.63           H  
+ATOM    564  HD3 LYS B 316     -16.899   0.945  -3.969  1.00 35.63           H  
+ATOM    565  HE2 LYS B 316     -18.472  -0.284  -5.977  1.00 27.40           H  
+ATOM    566  HE3 LYS B 316     -18.547  -0.720  -4.451  1.00 27.40           H  
+ATOM    567  HZ1 LYS B 316     -19.348   1.353  -3.970  1.00 38.21           H  
+ATOM    568  HZ2 LYS B 316     -19.274   1.754  -5.360  1.00 38.21           H  
+ATOM    569  HZ3 LYS B 316     -20.218   0.735  -4.950  1.00 38.21           H  
+ATOM    570  N   ASP B 317     -12.158   3.498  -4.648  1.00 12.83           N  
+ATOM    571  CA  ASP B 317     -10.721   3.649  -4.464  1.00 13.24           C  
+ATOM    572  C   ASP B 317      -9.972   3.789  -5.784  1.00 15.03           C  
+ATOM    573  O   ASP B 317      -8.809   3.392  -5.884  1.00 17.50           O  
+ATOM    574  CB  ASP B 317     -10.130   2.496  -3.649  1.00 18.81           C  
+ATOM    575  CG  ASP B 317      -8.956   2.933  -2.805  1.00 23.57           C  
+ATOM    576  OD1 ASP B 317      -8.910   4.116  -2.402  1.00 26.21           O  
+ATOM    577  OD2 ASP B 317      -8.069   2.093  -2.559  1.00 28.79           O  
+ATOM    578  H   ASP B 317     -12.583   4.222  -4.463  1.00 15.40           H  
+ATOM    579  HA  ASP B 317     -10.581   4.470  -3.966  1.00 15.89           H  
+ATOM    580  HB2 ASP B 317     -10.813   2.143  -3.057  1.00 22.58           H  
+ATOM    581  HB3 ASP B 317      -9.825   1.803  -4.255  1.00 22.58           H  
+ATOM    582  N   PHE B 318     -10.614   4.366  -6.793  1.00 12.19           N  
+ATOM    583  CA  PHE B 318      -9.941   4.696  -8.033  1.00 11.60           C  
+ATOM    584  C   PHE B 318      -9.532   6.158  -8.026  1.00 12.31           C  
+ATOM    585  O   PHE B 318     -10.110   6.981  -7.312  1.00 12.28           O  
+ATOM    586  CB  PHE B 318     -10.841   4.428  -9.247  1.00 10.79           C  
+ATOM    587  CG  PHE B 318     -11.103   2.985  -9.471  1.00 13.21           C  
+ATOM    588  CD1 PHE B 318     -10.193   2.226 -10.185  1.00 13.58           C  
+ATOM    589  CD2 PHE B 318     -12.233   2.364  -8.946  1.00 11.98           C  
+ATOM    590  CE1 PHE B 318     -10.411   0.878 -10.385  1.00 16.83           C  
+ATOM    591  CE2 PHE B 318     -12.451   1.011  -9.155  1.00 12.39           C  
+ATOM    592  CZ  PHE B 318     -11.530   0.274  -9.861  1.00 15.84           C  
+ATOM    593  H   PHE B 318     -11.448   4.575  -6.779  1.00 14.63           H  
+ATOM    594  HA  PHE B 318      -9.149   4.142  -8.118  1.00 13.92           H  
+ATOM    595  HB2 PHE B 318     -11.693   4.869  -9.109  1.00 12.95           H  
+ATOM    596  HB3 PHE B 318     -10.409   4.780 -10.041  1.00 12.95           H  
+ATOM    597  HD1 PHE B 318      -9.429   2.627 -10.532  1.00 16.29           H  
+ATOM    598  HD2 PHE B 318     -12.846   2.860  -8.453  1.00 14.37           H  
+ATOM    599  HE1 PHE B 318      -9.800   0.376 -10.875  1.00 20.20           H  
+ATOM    600  HE2 PHE B 318     -13.217   0.604  -8.819  1.00 14.87           H  
+ATOM    601  HZ  PHE B 318     -11.664  -0.637  -9.985  1.00 19.00           H  
+ATOM    602  N   ASN B 319      -8.542   6.482  -8.855  1.00 11.18           N  
+ATOM    603  CA  ASN B 319      -8.220   7.859  -9.183  1.00 10.08           C  
+ATOM    604  C   ASN B 319      -8.655   8.137 -10.616  1.00 10.22           C  
+ATOM    605  O   ASN B 319      -8.755   7.217 -11.440  1.00 10.40           O  
+ATOM    606  CB  ASN B 319      -6.727   8.156  -9.069  1.00 11.14           C  
+ATOM    607  CG  ASN B 319      -6.133   7.631  -7.808  1.00 13.10           C  
+ATOM    608  OD1 ASN B 319      -6.647   7.865  -6.711  1.00 14.66           O  
+ATOM    609  ND2 ASN B 319      -5.037   6.894  -7.947  1.00 19.79           N  
+ATOM    610  H   ASN B 319      -8.035   5.906  -9.245  1.00 13.42           H  
+ATOM    611  HA  ASN B 319      -8.685   8.444  -8.564  1.00 12.10           H  
+ATOM    612  HB2 ASN B 319      -6.264   7.742  -9.815  1.00 13.36           H  
+ATOM    613  HB3 ASN B 319      -6.592   9.117  -9.088  1.00 13.36           H  
+ATOM    614 HD21 ASN B 319      -4.650   6.564  -7.253  1.00 23.74           H  
+ATOM    615 HD22 ASN B 319      -4.714   6.747  -8.730  1.00 23.74           H  
+ATOM    616  N   ILE B 320      -8.950   9.398 -10.890  1.00  9.48           N  
+ATOM    617  CA  ILE B 320      -9.495   9.817 -12.179  1.00  9.28           C  
+ATOM    618  C   ILE B 320      -8.589  10.880 -12.779  1.00  9.49           C  
+ATOM    619  O   ILE B 320      -8.279  11.878 -12.116  1.00 11.52           O  
+ATOM    620  CB  ILE B 320     -10.913  10.395 -12.039  1.00 10.34           C  
+ATOM    621  CG1 ILE B 320     -11.881   9.353 -11.491  1.00 13.61           C  
+ATOM    622  CG2 ILE B 320     -11.418  10.948 -13.378  1.00 12.69           C  
+ATOM    623  CD1 ILE B 320     -13.195   9.977 -10.997  1.00 14.23           C  
+ATOM    624  H   ILE B 320      -8.842  10.046 -10.335  1.00 11.37           H  
+ATOM    625  HA  ILE B 320      -9.512   9.042 -12.762  1.00 11.13           H  
+ATOM    626  HB  ILE B 320     -10.866  11.128 -11.405  1.00 12.40           H  
+ATOM    627 HG12 ILE B 320     -12.093   8.718 -12.192  1.00 16.33           H  
+ATOM    628 HG13 ILE B 320     -11.464   8.895 -10.744  1.00 16.33           H  
+ATOM    629 HG21 ILE B 320     -12.375  11.090 -13.320  1.00 15.23           H  
+ATOM    630 HG22 ILE B 320     -10.969  11.789 -13.561  1.00 15.23           H  
+ATOM    631 HG23 ILE B 320     -11.220  10.308 -14.079  1.00 15.23           H  
+ATOM    632 HD11 ILE B 320     -13.682   9.319 -10.477  1.00 17.08           H  
+ATOM    633 HD12 ILE B 320     -12.990  10.749 -10.445  1.00 17.08           H  
+ATOM    634 HD13 ILE B 320     -13.723  10.250 -11.764  1.00 17.08           H  
+ATOM    635  N   VAL B 321      -8.232  10.715 -14.053  1.00  9.70           N  
+ATOM    636  CA  VAL B 321      -7.692  11.796 -14.875  1.00  8.68           C  
+ATOM    637  C   VAL B 321      -8.790  12.258 -15.829  1.00  8.54           C  
+ATOM    638  O   VAL B 321      -9.428  11.431 -16.487  1.00  9.41           O  
+ATOM    639  CB  VAL B 321      -6.446  11.335 -15.657  1.00  8.73           C  
+ATOM    640  CG1 VAL B 321      -5.930  12.443 -16.567  1.00 10.66           C  
+ATOM    641  CG2 VAL B 321      -5.319  10.903 -14.681  1.00 10.92           C  
+ATOM    642  H   VAL B 321      -8.296   9.967 -14.473  1.00 11.64           H  
+ATOM    643  HA  VAL B 321      -7.436  12.539 -14.307  1.00 10.41           H  
+ATOM    644  HB  VAL B 321      -6.700  10.576 -16.205  1.00 10.48           H  
+ATOM    645 HG11 VAL B 321      -5.065  12.184 -16.921  1.00 12.79           H  
+ATOM    646 HG12 VAL B 321      -6.560  12.573 -17.294  1.00 12.79           H  
+ATOM    647 HG13 VAL B 321      -5.845  13.261 -16.052  1.00 12.79           H  
+ATOM    648 HG21 VAL B 321      -4.595  10.506 -15.191  1.00 13.11           H  
+ATOM    649 HG22 VAL B 321      -4.998  11.684 -14.204  1.00 13.11           H  
+ATOM    650 HG23 VAL B 321      -5.675  10.255 -14.054  1.00 13.11           H  
+ATOM    651  N   SER B 322      -9.022  13.573 -15.881  1.00  9.27           N  
+ATOM    652  CA  SER B 322     -10.040  14.165 -16.745  1.00  8.55           C  
+ATOM    653  C   SER B 322      -9.469  15.347 -17.510  1.00  8.51           C  
+ATOM    654  O   SER B 322      -8.796  16.212 -16.935  1.00 10.71           O  
+ATOM    655  CB  SER B 322     -11.249  14.647 -15.932  1.00 10.83           C  
+ATOM    656  OG  SER B 322     -12.139  15.415 -16.717  1.00 12.16           O  
+ATOM    657  H   SER B 322      -8.592  14.153 -15.413  1.00 11.12           H  
+ATOM    658  HA  SER B 322     -10.327  13.495 -17.385  1.00 10.26           H  
+ATOM    659  HB2 SER B 322     -11.723  13.873 -15.590  1.00 12.99           H  
+ATOM    660  HB3 SER B 322     -10.932  15.193 -15.196  1.00 12.99           H  
+ATOM    661  HG  SER B 322     -12.417  14.959 -17.366  1.00 14.59           H  
+ATOM    662  N   GLY B 323      -9.784  15.399 -18.800  1.00  9.08           N  
+ATOM    663  CA  GLY B 323      -9.489  16.522 -19.654  1.00  8.79           C  
+ATOM    664  C   GLY B 323     -10.549  17.603 -19.669  1.00  9.27           C  
+ATOM    665  O   GLY B 323     -10.494  18.471 -20.544  1.00  9.51           O  
+ATOM    666  H   GLY B 323     -10.187  14.762 -19.214  1.00 10.89           H  
+ATOM    667  HA2 GLY B 323      -8.658  16.926 -19.360  1.00 10.55           H  
+ATOM    668  HA3 GLY B 323      -9.380  16.201 -20.563  1.00 10.55           H  
+ATOM    669  N   PHE B 324     -11.509  17.577 -18.745  1.00 10.31           N  
+ATOM    670  CA  PHE B 324     -12.444  18.686 -18.565  1.00  9.31           C  
+ATOM    671  C   PHE B 324     -13.235  18.950 -19.851  1.00 10.03           C  
+ATOM    672  O   PHE B 324     -13.401  20.083 -20.278  1.00 10.88           O  
+ATOM    673  CB  PHE B 324     -11.693  19.953 -18.078  1.00  8.43           C  
+ATOM    674  CG  PHE B 324     -12.587  21.082 -17.618  1.00  9.26           C  
+ATOM    675  CD1 PHE B 324     -13.430  20.932 -16.518  1.00  9.86           C  
+ATOM    676  CD2 PHE B 324     -12.564  22.303 -18.274  1.00  9.87           C  
+ATOM    677  CE1 PHE B 324     -14.250  21.993 -16.105  1.00 10.35           C  
+ATOM    678  CE2 PHE B 324     -13.357  23.355 -17.860  1.00  9.59           C  
+ATOM    679  CZ  PHE B 324     -14.208  23.186 -16.777  1.00 10.72           C  
+ATOM    680  H   PHE B 324     -11.640  16.920 -18.204  1.00 12.37           H  
+ATOM    681  HA  PHE B 324     -13.093  18.448 -17.884  1.00 11.17           H  
+ATOM    682  HB2 PHE B 324     -11.126  19.706 -17.330  1.00 10.12           H  
+ATOM    683  HB3 PHE B 324     -11.151  20.289 -18.808  1.00 10.12           H  
+ATOM    684  HD1 PHE B 324     -13.450  20.125 -16.057  1.00 11.84           H  
+ATOM    685  HD2 PHE B 324     -12.004  22.416 -19.007  1.00 11.85           H  
+ATOM    686  HE1 PHE B 324     -14.820  21.888 -15.377  1.00 12.42           H  
+ATOM    687  HE2 PHE B 324     -13.320  24.172 -18.304  1.00 11.51           H  
+ATOM    688  HZ  PHE B 324     -14.755  23.888 -16.506  1.00 12.87           H  
+ATOM    689  N   GLY B 325     -13.752  17.876 -20.453  1.00 10.06           N  
+ATOM    690  CA  GLY B 325     -14.489  18.013 -21.696  1.00  9.44           C  
+ATOM    691  C   GLY B 325     -15.800  18.747 -21.511  1.00  9.71           C  
+ATOM    692  O   GLY B 325     -16.481  18.633 -20.484  1.00  8.77           O  
+ATOM    693  H   GLY B 325     -13.688  17.070 -20.162  1.00 12.07           H  
+ATOM    694  HA2 GLY B 325     -13.951  18.506 -22.336  1.00 11.32           H  
+ATOM    695  HA3 GLY B 325     -14.679  17.133 -22.055  1.00 11.32           H  
+ATOM    696  N   LEU B 326     -16.194  19.499 -22.545  1.00  8.33           N  
+ATOM    697  CA  LEU B 326     -17.472  20.185 -22.498  1.00  8.86           C  
+ATOM    698  C   LEU B 326     -18.578  19.187 -22.219  1.00 11.30           C  
+ATOM    699  O   LEU B 326     -18.605  18.095 -22.790  1.00 10.08           O  
+ATOM    700  CB  LEU B 326     -17.761  20.891 -23.827  1.00 11.04           C  
+ATOM    701  CG  LEU B 326     -16.884  22.031 -24.276  1.00 14.48           C  
+ATOM    702  CD1 LEU B 326     -17.366  22.550 -25.628  1.00 15.59           C  
+ATOM    703  CD2 LEU B 326     -16.922  23.124 -23.254  1.00 14.28           C  
+ATOM    704  H   LEU B 326     -15.743  19.620 -23.267  1.00 10.00           H  
+ATOM    705  HA  LEU B 326     -17.445  20.855 -21.797  1.00 10.63           H  
+ATOM    706  HB2 LEU B 326     -17.712  20.220 -24.525  1.00 13.25           H  
+ATOM    707  HB3 LEU B 326     -18.662  21.248 -23.772  1.00 13.25           H  
+ATOM    708  HG  LEU B 326     -15.968  21.729 -24.374  1.00 17.38           H  
+ATOM    709 HD11 LEU B 326     -16.805  23.294 -25.899  1.00 18.70           H  
+ATOM    710 HD12 LEU B 326     -17.306  21.835 -26.281  1.00 18.70           H  
+ATOM    711 HD13 LEU B 326     -18.287  22.844 -25.544  1.00 18.70           H  
+ATOM    712 HD21 LEU B 326     -16.450  23.898 -23.601  1.00 17.14           H  
+ATOM    713 HD22 LEU B 326     -17.847  23.355 -23.073  1.00 17.14           H  
+ATOM    714 HD23 LEU B 326     -16.494  22.812 -22.442  1.00 17.14           H  
+ATOM    715  N   GLY B 327     -19.499  19.565 -21.351  1.00  9.88           N  
+ATOM    716  CA  GLY B 327     -20.631  18.727 -21.042  1.00 10.21           C  
+ATOM    717  C   GLY B 327     -20.351  17.563 -20.128  1.00 10.75           C  
+ATOM    718  O   GLY B 327     -21.287  16.815 -19.808  1.00 11.65           O  
+ATOM    719  H   GLY B 327     -19.487  20.312 -20.925  1.00 11.86           H  
+ATOM    720  HA2 GLY B 327     -21.311  19.274 -20.618  1.00 12.25           H  
+ATOM    721  HA3 GLY B 327     -20.984  18.370 -21.871  1.00 12.25           H  
+ATOM    722  N   VAL B 328     -19.107  17.392 -19.680  1.00 10.41           N  
+ATOM    723  CA  VAL B 328     -18.719  16.220 -18.908  1.00 10.85           C  
+ATOM    724  C   VAL B 328     -17.849  16.644 -17.732  1.00 10.52           C  
+ATOM    725  O   VAL B 328     -18.135  16.289 -16.587  1.00 10.47           O  
+ATOM    726  CB  VAL B 328     -17.992  15.201 -19.812  1.00 11.06           C  
+ATOM    727  CG1 VAL B 328     -17.409  14.050 -18.992  1.00 12.56           C  
+ATOM    728  CG2 VAL B 328     -18.964  14.673 -20.907  1.00 11.88           C  
+ATOM    729  H   VAL B 328     -18.465  17.949 -19.812  1.00 12.50           H  
+ATOM    730  HA  VAL B 328     -19.513  15.799 -18.543  1.00 13.02           H  
+ATOM    731  HB  VAL B 328     -17.248  15.645 -20.249  1.00 13.27           H  
+ATOM    732 HG11 VAL B 328     -17.147  13.335 -19.593  1.00 15.07           H  
+ATOM    733 HG12 VAL B 328     -16.635  14.370 -18.503  1.00 15.07           H  
+ATOM    734 HG13 VAL B 328     -18.083  13.730 -18.372  1.00 15.07           H  
+ATOM    735 HG21 VAL B 328     -18.509  13.996 -21.432  1.00 14.26           H  
+ATOM    736 HG22 VAL B 328     -19.744  14.289 -20.478  1.00 14.26           H  
+ATOM    737 HG23 VAL B 328     -19.229  15.411 -21.477  1.00 14.26           H  
+ATOM    738  N   GLY B 329     -16.782  17.393 -18.010  1.00 10.40           N  
+ATOM    739  CA  GLY B 329     -15.780  17.684 -16.990  1.00 11.08           C  
+ATOM    740  C   GLY B 329     -16.330  18.337 -15.736  1.00 11.03           C  
+ATOM    741  O   GLY B 329     -15.918  17.990 -14.625  1.00 10.57           O  
+ATOM    742  H   GLY B 329     -16.616  17.743 -18.778  1.00 12.48           H  
+ATOM    743  HA2 GLY B 329     -15.349  16.855 -16.729  1.00 13.29           H  
+ATOM    744  HA3 GLY B 329     -15.114  18.281 -17.367  1.00 13.29           H  
+ATOM    745  N   SER B 330     -17.239  19.307 -15.887  1.00 10.84           N  
+ATOM    746  CA  SER B 330     -17.787  19.973 -14.712  1.00  9.07           C  
+ATOM    747  C   SER B 330     -18.471  18.989 -13.773  1.00 10.40           C  
+ATOM    748  O   SER B 330     -18.436  19.156 -12.546  1.00 10.56           O  
+ATOM    749  CB  SER B 330     -18.772  21.073 -15.117  1.00 10.29           C  
+ATOM    750  OG  SER B 330     -18.083  22.178 -15.643  1.00 12.05           O  
+ATOM    751  H   SER B 330     -17.545  19.588 -16.640  1.00 13.01           H  
+ATOM    752  HA  SER B 330     -17.048  20.388 -14.239  1.00 10.89           H  
+ATOM    753  HB2 SER B 330     -19.376  20.725 -15.792  1.00 12.34           H  
+ATOM    754  HB3 SER B 330     -19.273  21.354 -14.336  1.00 12.34           H  
+ATOM    755  HG  SER B 330     -17.647  21.948 -16.324  1.00 14.46           H  
+ATOM    756  N   PHE B 331     -19.137  17.990 -14.327  1.00  9.57           N  
+ATOM    757  CA  PHE B 331     -19.888  17.037 -13.507  1.00  8.47           C  
+ATOM    758  C   PHE B 331     -18.984  15.997 -12.869  1.00 10.31           C  
+ATOM    759  O   PHE B 331     -19.268  15.561 -11.754  1.00 10.82           O  
+ATOM    760  CB  PHE B 331     -21.014  16.468 -14.371  1.00 11.10           C  
+ATOM    761  CG  PHE B 331     -21.736  17.569 -15.087  1.00 11.38           C  
+ATOM    762  CD1 PHE B 331     -22.436  18.511 -14.369  1.00 11.28           C  
+ATOM    763  CD2 PHE B 331     -21.595  17.753 -16.446  1.00 10.52           C  
+ATOM    764  CE1 PHE B 331     -23.043  19.592 -14.992  1.00 13.03           C  
+ATOM    765  CE2 PHE B 331     -22.192  18.836 -17.082  1.00 13.18           C  
+ATOM    766  CZ  PHE B 331     -22.906  19.762 -16.348  1.00 14.12           C  
+ATOM    767  H   PHE B 331     -19.174  17.836 -15.172  1.00 11.49           H  
+ATOM    768  HA  PHE B 331     -20.317  17.463 -12.748  1.00 10.16           H  
+ATOM    769  HB2 PHE B 331     -20.642  15.862 -15.031  1.00 13.32           H  
+ATOM    770  HB3 PHE B 331     -21.648  15.996 -13.809  1.00 13.32           H  
+ATOM    771  HD1 PHE B 331     -22.503  18.422 -13.446  1.00 13.53           H  
+ATOM    772  HD2 PHE B 331     -21.096  17.146 -16.943  1.00 12.62           H  
+ATOM    773  HE1 PHE B 331     -23.541  20.198 -14.494  1.00 15.64           H  
+ATOM    774  HE2 PHE B 331     -22.110  18.936 -18.003  1.00 15.81           H  
+ATOM    775  HZ  PHE B 331     -23.291  20.496 -16.769  1.00 16.94           H  
+ATOM    776  N   VAL B 332     -17.896  15.615 -13.537  1.00  8.56           N  
+ATOM    777  CA  VAL B 332     -16.848  14.827 -12.895  1.00  9.28           C  
+ATOM    778  C   VAL B 332     -16.348  15.551 -11.654  1.00 10.21           C  
+ATOM    779  O   VAL B 332     -16.296  14.975 -10.561  1.00 10.17           O  
+ATOM    780  CB  VAL B 332     -15.700  14.551 -13.892  1.00  9.17           C  
+ATOM    781  CG1 VAL B 332     -14.530  13.828 -13.202  1.00 10.96           C  
+ATOM    782  CG2 VAL B 332     -16.210  13.769 -15.111  1.00 10.01           C  
+ATOM    783  H   VAL B 332     -17.741  15.799 -14.363  1.00 10.27           H  
+ATOM    784  HA  VAL B 332     -17.218  13.973 -12.622  1.00 11.14           H  
+ATOM    785  HB  VAL B 332     -15.360  15.400 -14.214  1.00 11.01           H  
+ATOM    786 HG11 VAL B 332     -13.921  13.494 -13.880  1.00 13.15           H  
+ATOM    787 HG12 VAL B 332     -14.068  14.454 -12.623  1.00 13.15           H  
+ATOM    788 HG13 VAL B 332     -14.879  13.090 -12.679  1.00 13.15           H  
+ATOM    789 HG21 VAL B 332     -15.460  13.567 -15.693  1.00 12.01           H  
+ATOM    790 HG22 VAL B 332     -16.625  12.947 -14.808  1.00 12.01           H  
+ATOM    791 HG23 VAL B 332     -16.859  14.312 -15.586  1.00 12.01           H  
+ATOM    792  N   ILE B 333     -16.003  16.840 -11.801  1.00 10.13           N  
+ATOM    793  CA  ILE B 333     -15.520  17.624 -10.671  1.00  9.78           C  
+ATOM    794  C   ILE B 333     -16.576  17.678  -9.582  1.00 11.58           C  
+ATOM    795  O   ILE B 333     -16.285  17.465  -8.397  1.00 11.28           O  
+ATOM    796  CB  ILE B 333     -15.119  19.041 -11.121  1.00 11.15           C  
+ATOM    797  CG1 ILE B 333     -13.921  18.980 -12.059  1.00 10.26           C  
+ATOM    798  CG2 ILE B 333     -14.794  19.892  -9.913  1.00 10.83           C  
+ATOM    799  CD1 ILE B 333     -13.590  20.251 -12.792  1.00 11.04           C  
+ATOM    800  H   ILE B 333     -16.040  17.275 -12.542  1.00 12.15           H  
+ATOM    801  HA  ILE B 333     -14.731  17.187 -10.315  1.00 11.74           H  
+ATOM    802  HB  ILE B 333     -15.866  19.437 -11.597  1.00 13.38           H  
+ATOM    803 HG12 ILE B 333     -13.139  18.740 -11.537  1.00 12.31           H  
+ATOM    804 HG13 ILE B 333     -14.094  18.301 -12.729  1.00 12.31           H  
+ATOM    805 HG21 ILE B 333     -14.311  20.681 -10.204  1.00 13.00           H  
+ATOM    806 HG22 ILE B 333     -15.621  20.152  -9.478  1.00 13.00           H  
+ATOM    807 HG23 ILE B 333     -14.247  19.375  -9.301  1.00 13.00           H  
+ATOM    808 HD11 ILE B 333     -12.914  20.063 -13.461  1.00 13.25           H  
+ATOM    809 HD12 ILE B 333     -14.393  20.587 -13.219  1.00 13.25           H  
+ATOM    810 HD13 ILE B 333     -13.255  20.904 -12.157  1.00 13.25           H  
+ATOM    811  N   ASN B 334     -17.828  17.955  -9.959  1.00  9.98           N  
+ATOM    812  CA  ASN B 334     -18.875  18.051  -8.948  1.00 10.10           C  
+ATOM    813  C   ASN B 334     -18.970  16.782  -8.121  1.00 12.13           C  
+ATOM    814  O   ASN B 334     -19.098  16.834  -6.892  1.00 11.92           O  
+ATOM    815  CB  ASN B 334     -20.228  18.324  -9.583  1.00 10.75           C  
+ATOM    816  CG  ASN B 334     -20.361  19.699 -10.129  1.00 11.87           C  
+ATOM    817  OD1 ASN B 334     -19.609  20.603  -9.780  1.00 14.70           O  
+ATOM    818  ND2 ASN B 334     -21.392  19.892 -10.950  1.00 14.04           N  
+ATOM    819  H   ASN B 334     -18.086  18.087 -10.769  1.00 11.98           H  
+ATOM    820  HA  ASN B 334     -18.646  18.797  -8.372  1.00 12.12           H  
+ATOM    821  HB2 ASN B 334     -20.362  17.701 -10.315  1.00 12.90           H  
+ATOM    822  HB3 ASN B 334     -20.919  18.202  -8.913  1.00 12.90           H  
+ATOM    823 HD21 ASN B 334     -21.525  20.666 -11.300  1.00 16.85           H  
+ATOM    824 HD22 ASN B 334     -21.925  19.241 -11.131  1.00 16.85           H  
+ATOM    825  N   GLY B 335     -18.939  15.625  -8.781  1.00  9.95           N  
+ATOM    826  CA  GLY B 335     -19.079  14.376  -8.064  1.00 11.19           C  
+ATOM    827  C   GLY B 335     -17.903  14.113  -7.145  1.00 12.26           C  
+ATOM    828  O   GLY B 335     -18.079  13.642  -6.014  1.00 12.47           O  
+ATOM    829  H   GLY B 335     -18.838  15.543  -9.631  1.00 11.94           H  
+ATOM    830  HA2 GLY B 335     -19.888  14.400  -7.530  1.00 13.43           H  
+ATOM    831  HA3 GLY B 335     -19.142  13.645  -8.699  1.00 13.43           H  
+ATOM    832  N   VAL B 336     -16.693  14.432  -7.600  1.00 11.66           N  
+ATOM    833  CA  VAL B 336     -15.529  14.191  -6.755  1.00 11.42           C  
+ATOM    834  C   VAL B 336     -15.512  15.154  -5.576  1.00 12.59           C  
+ATOM    835  O   VAL B 336     -15.252  14.749  -4.431  1.00 11.63           O  
+ATOM    836  CB  VAL B 336     -14.234  14.292  -7.579  1.00 10.80           C  
+ATOM    837  CG1 VAL B 336     -13.014  14.203  -6.642  1.00 12.27           C  
+ATOM    838  CG2 VAL B 336     -14.200  13.173  -8.611  1.00 13.30           C  
+ATOM    839  H   VAL B 336     -16.526  14.778  -8.369  1.00 13.99           H  
+ATOM    840  HA  VAL B 336     -15.592  13.289  -6.404  1.00 13.70           H  
+ATOM    841  HB  VAL B 336     -14.200  15.143  -8.044  1.00 12.96           H  
+ATOM    842 HG11 VAL B 336     -12.228  13.986  -7.166  1.00 14.72           H  
+ATOM    843 HG12 VAL B 336     -12.891  15.058  -6.200  1.00 14.72           H  
+ATOM    844 HG13 VAL B 336     -13.173  13.510  -5.981  1.00 14.72           H  
+ATOM    845 HG21 VAL B 336     -13.376  13.237  -9.119  1.00 15.96           H  
+ATOM    846 HG22 VAL B 336     -14.241  12.319  -8.153  1.00 15.96           H  
+ATOM    847 HG23 VAL B 336     -14.962  13.268  -9.204  1.00 15.96           H  
+ATOM    848  N   LEU B 337     -15.765  16.445  -5.833  1.00 10.86           N  
+ATOM    849  CA  LEU B 337     -15.749  17.419  -4.739  1.00 10.93           C  
+ATOM    850  C   LEU B 337     -16.804  17.082  -3.698  1.00 11.84           C  
+ATOM    851  O   LEU B 337     -16.600  17.303  -2.490  1.00 13.48           O  
+ATOM    852  CB  LEU B 337     -15.950  18.830  -5.263  1.00 12.70           C  
+ATOM    853  CG  LEU B 337     -14.847  19.378  -6.167  1.00 13.69           C  
+ATOM    854  CD1 LEU B 337     -15.148  20.828  -6.478  1.00 13.81           C  
+ATOM    855  CD2 LEU B 337     -13.483  19.215  -5.528  1.00 14.51           C  
+ATOM    856  H   LEU B 337     -15.943  16.770  -6.609  1.00 13.03           H  
+ATOM    857  HA  LEU B 337     -14.876  17.390  -4.318  1.00 13.11           H  
+ATOM    858  HB2 LEU B 337     -16.774  18.847  -5.774  1.00 15.24           H  
+ATOM    859  HB3 LEU B 337     -16.019  19.427  -4.502  1.00 15.24           H  
+ATOM    860  HG  LEU B 337     -14.819  18.880  -6.999  1.00 16.42           H  
+ATOM    861 HD11 LEU B 337     -14.442  21.183  -7.041  1.00 16.57           H  
+ATOM    862 HD12 LEU B 337     -15.999  20.881  -6.941  1.00 16.57           H  
+ATOM    863 HD13 LEU B 337     -15.192  21.326  -5.648  1.00 16.57           H  
+ATOM    864 HD21 LEU B 337     -12.835  19.737  -6.027  1.00 17.42           H  
+ATOM    865 HD22 LEU B 337     -13.524  19.530  -4.611  1.00 17.42           H  
+ATOM    866 HD23 LEU B 337     -13.236  18.277  -5.545  1.00 17.42           H  
+ATOM    867  N   GLU B 338     -17.958  16.579  -4.133  1.00 12.61           N  
+ATOM    868  CA  GLU B 338     -18.998  16.238  -3.170  1.00 14.65           C  
+ATOM    869  C   GLU B 338     -18.480  15.209  -2.183  1.00 14.99           C  
+ATOM    870  O   GLU B 338     -18.657  15.350  -0.964  1.00 16.40           O  
+ATOM    871  CB  GLU B 338     -20.222  15.717  -3.902  1.00 14.95           C  
+ATOM    872  CG  GLU B 338     -21.464  15.563  -3.064  1.00 20.67           C  
+ATOM    873  CD  GLU B 338     -22.672  15.435  -3.971  1.00 24.04           C  
+ATOM    874  OE1 GLU B 338     -23.242  16.478  -4.337  1.00 27.76           O  
+ATOM    875  OE2 GLU B 338     -22.984  14.296  -4.361  1.00 28.12           O  
+ATOM    876  H   GLU B 338     -18.156  16.430  -4.957  1.00 15.14           H  
+ATOM    877  HA  GLU B 338     -19.261  17.032  -2.678  1.00 17.58           H  
+ATOM    878  HB2 GLU B 338     -20.433  16.333  -4.620  1.00 17.93           H  
+ATOM    879  HB3 GLU B 338     -20.010  14.843  -4.266  1.00 17.93           H  
+ATOM    880  HG2 GLU B 338     -21.395  14.764  -2.519  1.00 24.81           H  
+ATOM    881  HG3 GLU B 338     -21.577  16.343  -2.499  1.00 24.81           H  
+ATOM    882  N   GLU B 339     -17.824  14.167  -2.692  1.00 11.23           N  
+ATOM    883  CA  GLU B 339     -17.280  13.131  -1.824  1.00 13.65           C  
+ATOM    884  C   GLU B 339     -16.111  13.664  -0.997  1.00 16.99           C  
+ATOM    885  O   GLU B 339     -16.061  13.455   0.219  1.00 15.62           O  
+ATOM    886  CB  GLU B 339     -16.878  11.920  -2.666  1.00 16.19           C  
+ATOM    887  CG  GLU B 339     -16.610  10.644  -1.864  1.00 19.15           C  
+ATOM    888  CD  GLU B 339     -17.838   9.989  -1.221  1.00 18.63           C  
+ATOM    889  OE1 GLU B 339     -18.988  10.490  -1.337  1.00 21.22           O  
+ATOM    890  OE2 GLU B 339     -17.630   8.957  -0.557  1.00 23.27           O  
+ATOM    891  H   GLU B 339     -17.683  14.039  -3.530  1.00 13.47           H  
+ATOM    892  HA  GLU B 339     -17.961  12.840  -1.198  1.00 16.38           H  
+ATOM    893  HB2 GLU B 339     -17.595  11.728  -3.290  1.00 19.43           H  
+ATOM    894  HB3 GLU B 339     -16.066  12.137  -3.150  1.00 19.43           H  
+ATOM    895  HG2 GLU B 339     -16.214   9.988  -2.459  1.00 22.98           H  
+ATOM    896  HG3 GLU B 339     -15.991  10.858  -1.149  1.00 22.98           H  
+ATOM    897  N   LEU B 340     -15.179  14.396  -1.623  1.00 11.50           N  
+ATOM    898  CA  LEU B 340     -14.016  14.885  -0.882  1.00 14.15           C  
+ATOM    899  C   LEU B 340     -14.429  15.805   0.252  1.00 13.51           C  
+ATOM    900  O   LEU B 340     -13.948  15.675   1.392  1.00 14.52           O  
+ATOM    901  CB  LEU B 340     -13.047  15.643  -1.805  1.00 13.38           C  
+ATOM    902  CG  LEU B 340     -12.189  14.859  -2.778  1.00 19.06           C  
+ATOM    903  CD1 LEU B 340     -11.452  15.884  -3.639  1.00 19.79           C  
+ATOM    904  CD2 LEU B 340     -11.214  13.975  -2.099  1.00 26.63           C  
+ATOM    905  H   LEU B 340     -15.199  14.617  -2.454  1.00 13.80           H  
+ATOM    906  HA  LEU B 340     -13.561  14.107  -0.523  1.00 16.98           H  
+ATOM    907  HB2 LEU B 340     -13.575  16.257  -2.338  1.00 16.06           H  
+ATOM    908  HB3 LEU B 340     -12.435  16.138  -1.238  1.00 16.06           H  
+ATOM    909  HG  LEU B 340     -12.748  14.273  -3.312  1.00 22.87           H  
+ATOM    910 HD11 LEU B 340     -10.879  15.417  -4.266  1.00 23.75           H  
+ATOM    911 HD12 LEU B 340     -12.103  16.418  -4.121  1.00 23.75           H  
+ATOM    912 HD13 LEU B 340     -10.918  16.454  -3.063  1.00 23.75           H  
+ATOM    913 HD21 LEU B 340     -10.650  13.554  -2.767  1.00 31.96           H  
+ATOM    914 HD22 LEU B 340     -10.671  14.507  -1.496  1.00 31.96           H  
+ATOM    915 HD23 LEU B 340     -11.696  13.298  -1.598  1.00 31.96           H  
+ATOM    916  N   TYR B 341     -15.306  16.757  -0.031  1.00 12.68           N  
+ATOM    917  CA  TYR B 341     -15.593  17.816   0.927  1.00 14.03           C  
+ATOM    918  C   TYR B 341     -16.624  17.405   1.968  1.00 18.44           C  
+ATOM    919  O   TYR B 341     -16.908  18.193   2.886  1.00 21.48           O  
+ATOM    920  CB  TYR B 341     -16.029  19.089   0.214  1.00 14.10           C  
+ATOM    921  CG  TYR B 341     -14.926  19.741  -0.611  1.00 13.58           C  
+ATOM    922  CD1 TYR B 341     -13.590  19.393  -0.453  1.00 14.52           C  
+ATOM    923  CD2 TYR B 341     -15.231  20.701  -1.549  1.00 13.48           C  
+ATOM    924  CE1 TYR B 341     -12.604  19.971  -1.221  1.00 13.70           C  
+ATOM    925  CE2 TYR B 341     -14.246  21.301  -2.319  1.00 12.29           C  
+ATOM    926  CZ  TYR B 341     -12.940  20.941  -2.142  1.00 12.72           C  
+ATOM    927  OH  TYR B 341     -11.966  21.540  -2.911  1.00 11.74           O  
+ATOM    928  H   TYR B 341     -15.747  16.812  -0.767  1.00 15.21           H  
+ATOM    929  HA  TYR B 341     -14.774  18.032   1.400  1.00 16.83           H  
+ATOM    930  HB2 TYR B 341     -16.760  18.876  -0.386  1.00 16.92           H  
+ATOM    931  HB3 TYR B 341     -16.321  19.733   0.878  1.00 16.92           H  
+ATOM    932  HD1 TYR B 341     -13.358  18.757   0.185  1.00 17.43           H  
+ATOM    933  HD2 TYR B 341     -16.118  20.953  -1.670  1.00 16.18           H  
+ATOM    934  HE1 TYR B 341     -11.717  19.709  -1.120  1.00 16.43           H  
+ATOM    935  HE2 TYR B 341     -14.473  21.944  -2.951  1.00 14.75           H  
+ATOM    936  HH  TYR B 341     -11.216  21.204  -2.737  1.00 14.08           H  
+ATOM    937  N   MET B 342     -17.174  16.202   1.868  1.00 12.97           N  
+ATOM    938  CA  MET B 342     -17.928  15.624   2.973  1.00 14.15           C  
+ATOM    939  C   MET B 342     -17.096  14.633   3.773  1.00 15.88           C  
+ATOM    940  O   MET B 342     -17.588  14.071   4.762  1.00 17.62           O  
+ATOM    941  CB  MET B 342     -19.195  14.949   2.457  1.00 16.10           C  
+ATOM    942  CG  MET B 342     -20.314  15.918   2.249  1.00 22.83           C  
+ATOM    943  SD  MET B 342     -21.811  15.034   1.759  1.00 34.75           S  
+ATOM    944  CE  MET B 342     -21.989  15.698   0.140  1.00 31.40           C  
+ATOM    945  H   MET B 342     -17.123  15.701   1.171  1.00 15.56           H  
+ATOM    946  HA  MET B 342     -18.215  16.339   3.563  1.00 16.97           H  
+ATOM    947  HB2 MET B 342     -19.003  14.523   1.607  1.00 19.32           H  
+ATOM    948  HB3 MET B 342     -19.486  14.286   3.102  1.00 19.32           H  
+ATOM    949  HG2 MET B 342     -20.490  16.396   3.074  1.00 27.39           H  
+ATOM    950  HG3 MET B 342     -20.078  16.544   1.547  1.00 27.39           H  
+ATOM    951  HE1 MET B 342     -22.702  15.226  -0.318  1.00 37.69           H  
+ATOM    952  HE2 MET B 342     -22.205  16.641   0.208  1.00 37.69           H  
+ATOM    953  HE3 MET B 342     -21.154  15.584  -0.341  1.00 37.69           H  
+ATOM    954  N   ASN B 343     -15.843  14.409   3.382  1.00 14.76           N  
+ATOM    955  CA  ASN B 343     -14.983  13.427   4.033  1.00 15.11           C  
+ATOM    956  C   ASN B 343     -13.605  14.008   4.320  1.00 14.05           C  
+ATOM    957  O   ASN B 343     -12.595  13.282   4.345  1.00 15.30           O  
+ATOM    958  CB  ASN B 343     -14.906  12.157   3.202  1.00 14.70           C  
+ATOM    959  CG  ASN B 343     -16.198  11.389   3.232  1.00 15.53           C  
+ATOM    960  OD1 ASN B 343     -16.492  10.716   4.210  1.00 14.72           O  
+ATOM    961  ND2 ASN B 343     -17.003  11.521   2.172  1.00 16.30           N  
+ATOM    962  H   ASN B 343     -15.462  14.821   2.730  1.00 17.72           H  
+ATOM    963  HA  ASN B 343     -15.363  13.184   4.892  1.00 18.14           H  
+ATOM    964  HB2 ASN B 343     -14.712  12.390   2.280  1.00 17.64           H  
+ATOM    965  HB3 ASN B 343     -14.205  11.586   3.554  1.00 17.64           H  
+ATOM    966 HD21 ASN B 343     -17.753  11.100   2.146  1.00 19.57           H  
+ATOM    967 HD22 ASN B 343     -16.771  12.027   1.516  1.00 19.57           H  
+ATOM    968  N   GLN B 344     -13.570  15.306   4.560  1.00 14.56           N  
+ATOM    969  CA  GLN B 344     -12.387  15.996   5.060  1.00 16.06           C  
+ATOM    970  C   GLN B 344     -11.215  15.854   4.102  1.00 17.61           C  
+ATOM    971  O   GLN B 344     -10.055  15.826   4.518  1.00 19.42           O  
+ATOM    972  CB  GLN B 344     -12.022  15.488   6.455  1.00 21.91           C  
+ATOM    973  CG  GLN B 344     -13.077  15.779   7.523  1.00 23.99           C  
+ATOM    974  CD  GLN B 344     -14.302  14.841   7.503  1.00 19.98           C  
+ATOM    975  OE1 GLN B 344     -14.233  13.685   7.089  1.00 21.54           O  
+ATOM    976  NE2 GLN B 344     -15.428  15.359   7.974  1.00 30.41           N  
+ATOM    977  H   GLN B 344     -14.240  15.831   4.438  1.00 17.47           H  
+ATOM    978  HA  GLN B 344     -12.579  16.944   5.130  1.00 19.27           H  
+ATOM    979  HB2 GLN B 344     -11.903  14.526   6.414  1.00 26.30           H  
+ATOM    980  HB3 GLN B 344     -11.196  15.913   6.734  1.00 26.30           H  
+ATOM    981  HG2 GLN B 344     -12.662  15.697   8.396  1.00 28.78           H  
+ATOM    982  HG3 GLN B 344     -13.403  16.684   7.395  1.00 28.78           H  
+ATOM    983 HE21 GLN B 344     -15.441  16.169   8.264  1.00 36.49           H  
+ATOM    984 HE22 GLN B 344     -16.146  14.886   7.989  1.00 36.49           H  
+ATOM    985  N   GLY B 345     -11.523  15.787   2.796  1.00 13.96           N  
+ATOM    986  CA  GLY B 345     -10.515  15.591   1.783  1.00 13.22           C  
+ATOM    987  C   GLY B 345     -10.080  16.893   1.124  1.00 11.85           C  
+ATOM    988  O   GLY B 345     -10.637  17.958   1.344  1.00 14.88           O  
+ATOM    989  H   GLY B 345     -12.321  15.855   2.484  1.00 16.75           H  
+ATOM    990  HA2 GLY B 345      -9.735  15.178   2.185  1.00 15.86           H  
+ATOM    991  HA3 GLY B 345     -10.864  15.004   1.095  1.00 15.86           H  
+ATOM    992  N   THR B 346      -9.059  16.767   0.275  1.00 12.25           N  
+ATOM    993  CA  THR B 346      -8.505  17.903  -0.449  1.00 12.49           C  
+ATOM    994  C   THR B 346      -8.231  17.504  -1.894  1.00 11.74           C  
+ATOM    995  O   THR B 346      -7.858  16.359  -2.183  1.00 12.10           O  
+ATOM    996  CB  THR B 346      -7.197  18.423   0.197  1.00 12.45           C  
+ATOM    997  OG1 THR B 346      -6.538  19.347  -0.681  1.00 14.11           O  
+ATOM    998  CG2 THR B 346      -6.266  17.311   0.487  1.00 14.77           C  
+ATOM    999  H   THR B 346      -8.667  16.022   0.100  1.00 14.70           H  
+ATOM   1000  HA  THR B 346      -9.155  18.624  -0.444  1.00 14.99           H  
+ATOM   1001  HB  THR B 346      -7.425  18.867   1.029  1.00 14.94           H  
+ATOM   1002  HG1 THR B 346      -7.024  20.020  -0.808  1.00 16.93           H  
+ATOM   1003 HG21 THR B 346      -5.421  17.661   0.810  1.00 17.73           H  
+ATOM   1004 HG22 THR B 346      -6.645  16.729   1.165  1.00 17.73           H  
+ATOM   1005 HG23 THR B 346      -6.106  16.793  -0.317  1.00 17.73           H  
+ATOM   1006  N   ILE B 347      -8.399  18.485  -2.795  1.00 11.62           N  
+ATOM   1007  CA  ILE B 347      -8.034  18.308  -4.196  1.00 11.37           C  
+ATOM   1008  C   ILE B 347      -6.560  17.934  -4.357  1.00 11.74           C  
+ATOM   1009  O   ILE B 347      -6.194  17.237  -5.316  1.00 12.45           O  
+ATOM   1010  CB  ILE B 347      -8.415  19.574  -4.993  1.00 12.56           C  
+ATOM   1011  CG1 ILE B 347      -8.414  19.294  -6.517  1.00 12.85           C  
+ATOM   1012  CG2 ILE B 347      -7.526  20.755  -4.656  1.00 13.90           C  
+ATOM   1013  CD1 ILE B 347      -9.579  18.431  -6.974  1.00 15.00           C  
+ATOM   1014  H   ILE B 347      -8.724  19.261  -2.615  1.00 13.94           H  
+ATOM   1015  HA  ILE B 347      -8.539  17.562  -4.556  1.00 13.65           H  
+ATOM   1016  HB  ILE B 347      -9.317  19.811  -4.726  1.00 15.07           H  
+ATOM   1017 HG12 ILE B 347      -8.465  20.139  -6.990  1.00 15.42           H  
+ATOM   1018 HG13 ILE B 347      -7.593  18.833  -6.749  1.00 15.42           H  
+ATOM   1019 HG21 ILE B 347      -7.888  21.552  -5.073  1.00 16.68           H  
+ATOM   1020 HG22 ILE B 347      -7.501  20.868  -3.693  1.00 16.68           H  
+ATOM   1021 HG23 ILE B 347      -6.632  20.583  -4.992  1.00 16.68           H  
+ATOM   1022 HD11 ILE B 347      -9.590  18.404  -7.944  1.00 18.01           H  
+ATOM   1023 HD12 ILE B 347      -9.467  17.536  -6.620  1.00 18.01           H  
+ATOM   1024 HD13 ILE B 347     -10.406  18.817  -6.645  1.00 18.01           H  
+ATOM   1025  N   ASP B 348      -5.713  18.310  -3.392  1.00 12.39           N  
+ATOM   1026  CA  ASP B 348      -4.287  18.018  -3.501  1.00 12.81           C  
+ATOM   1027  C   ASP B 348      -3.953  16.545  -3.272  1.00 13.75           C  
+ATOM   1028  O   ASP B 348      -2.808  16.154  -3.507  1.00 16.18           O  
+ATOM   1029  CB  ASP B 348      -3.491  18.871  -2.523  1.00 12.11           C  
+ATOM   1030  CG  ASP B 348      -3.409  20.332  -2.929  1.00 12.94           C  
+ATOM   1031  OD1 ASP B 348      -3.622  20.682  -4.113  1.00 13.57           O  
+ATOM   1032  OD2 ASP B 348      -3.134  21.139  -2.019  1.00 15.69           O  
+ATOM   1033  H   ASP B 348      -5.940  18.729  -2.676  1.00 14.87           H  
+ATOM   1034  HA  ASP B 348      -4.006  18.250  -4.400  1.00 15.37           H  
+ATOM   1035  HB2 ASP B 348      -3.914  18.828  -1.651  1.00 14.54           H  
+ATOM   1036  HB3 ASP B 348      -2.585  18.526  -2.470  1.00 14.54           H  
+ATOM   1037  N   ASP B 349      -4.901  15.722  -2.849  1.00 13.44           N  
+ATOM   1038  CA  ASP B 349      -4.625  14.294  -2.722  1.00 15.55           C  
+ATOM   1039  C   ASP B 349      -4.601  13.577  -4.066  1.00 16.24           C  
+ATOM   1040  O   ASP B 349      -4.283  12.382  -4.107  1.00 17.52           O  
+ATOM   1041  CB  ASP B 349      -5.647  13.645  -1.793  1.00 18.83           C  
+ATOM   1042  CG  ASP B 349      -5.427  14.016  -0.340  1.00 32.72           C  
+ATOM   1043  OD1 ASP B 349      -4.258  14.247   0.037  1.00 27.67           O  
+ATOM   1044  OD2 ASP B 349      -6.428  14.083   0.405  1.00 40.55           O  
+ATOM   1045  H   ASP B 349      -5.699  15.960  -2.632  1.00 16.12           H  
+ATOM   1046  HA  ASP B 349      -3.751  14.178  -2.317  1.00 18.67           H  
+ATOM   1047  HB2 ASP B 349      -6.537  13.936  -2.047  1.00 22.60           H  
+ATOM   1048  HB3 ASP B 349      -5.580  12.680  -1.871  1.00 22.60           H  
+ATOM   1049  N   ASP B 350      -4.915  14.284  -5.156  1.00 13.74           N  
+ATOM   1050  CA  ASP B 350      -4.749  13.787  -6.523  1.00 17.43           C  
+ATOM   1051  C   ASP B 350      -5.590  12.548  -6.803  1.00 14.95           C  
+ATOM   1052  O   ASP B 350      -5.262  11.730  -7.665  1.00 18.20           O  
+ATOM   1053  CB  ASP B 350      -3.270  13.552  -6.835  1.00 18.26           C  
+ATOM   1054  CG  ASP B 350      -2.497  14.856  -6.965  1.00 25.92           C  
+ATOM   1055  OD1 ASP B 350      -3.144  15.926  -7.067  1.00 23.64           O  
+ATOM   1056  OD2 ASP B 350      -1.244  14.820  -6.948  1.00 31.74           O  
+ATOM   1057  H   ASP B 350      -5.237  15.081  -5.127  1.00 16.49           H  
+ATOM   1058  HA  ASP B 350      -5.076  14.464  -7.136  1.00 20.92           H  
+ATOM   1059  HB2 ASP B 350      -2.872  13.035  -6.117  1.00 21.91           H  
+ATOM   1060  HB3 ASP B 350      -3.194  13.070  -7.673  1.00 21.91           H  
+ATOM   1061  N   ARG B 351      -6.727  12.430  -6.114  1.00 13.11           N  
+ATOM   1062  CA  ARG B 351      -7.731  11.469  -6.533  1.00 12.11           C  
+ATOM   1063  C   ARG B 351      -8.363  11.881  -7.852  1.00 11.41           C  
+ATOM   1064  O   ARG B 351      -8.882  11.027  -8.583  1.00 13.23           O  
+ATOM   1065  CB  ARG B 351      -8.815  11.346  -5.482  1.00 13.06           C  
+ATOM   1066  CG  ARG B 351      -8.296  10.950  -4.105  1.00 14.98           C  
+ATOM   1067  CD  ARG B 351      -7.665   9.578  -4.096  1.00 13.85           C  
+ATOM   1068  NE  ARG B 351      -8.565   8.552  -4.605  1.00 13.93           N  
+ATOM   1069  CZ  ARG B 351      -9.576   8.024  -3.925  1.00 13.62           C  
+ATOM   1070  NH1 ARG B 351      -9.820   8.361  -2.671  1.00 14.29           N  
+ATOM   1071  NH2 ARG B 351     -10.353   7.125  -4.523  1.00 11.74           N  
+ATOM   1072  H   ARG B 351      -6.932  12.887  -5.416  1.00 15.74           H  
+ATOM   1073  HA  ARG B 351      -7.306  10.604  -6.637  1.00 14.54           H  
+ATOM   1074  HB2 ARG B 351      -9.262  12.202  -5.395  1.00 15.67           H  
+ATOM   1075  HB3 ARG B 351      -9.448  10.668  -5.765  1.00 15.67           H  
+ATOM   1076  HG2 ARG B 351      -7.625  11.591  -3.822  1.00 17.97           H  
+ATOM   1077  HG3 ARG B 351      -9.035  10.945  -3.476  1.00 17.97           H  
+ATOM   1078  HD2 ARG B 351      -6.873   9.589  -4.657  1.00 16.62           H  
+ATOM   1079  HD3 ARG B 351      -7.424   9.344  -3.186  1.00 16.62           H  
+ATOM   1080  HE  ARG B 351      -8.432   8.266  -5.405  1.00 16.72           H  
+ATOM   1081 HH11 ARG B 351      -9.318   8.936  -2.274  1.00 17.15           H  
+ATOM   1082 HH12 ARG B 351     -10.481   8.005  -2.251  1.00 17.15           H  
+ATOM   1083 HH21 ARG B 351     -10.196   6.895  -5.337  1.00 14.09           H  
+ATOM   1084 HH22 ARG B 351     -11.012   6.774  -4.096  1.00 14.09           H  
+ATOM   1085  N   LEU B 352      -8.390  13.187  -8.127  1.00 12.32           N  
+ATOM   1086  CA  LEU B 352      -8.884  13.736  -9.387  1.00 10.46           C  
+ATOM   1087  C   LEU B 352      -7.783  14.625  -9.937  1.00  9.92           C  
+ATOM   1088  O   LEU B 352      -7.352  15.581  -9.276  1.00 12.74           O  
+ATOM   1089  CB  LEU B 352     -10.173  14.527  -9.202  1.00 11.16           C  
+ATOM   1090  CG  LEU B 352     -10.685  15.294 -10.420  1.00 12.40           C  
+ATOM   1091  CD1 LEU B 352     -10.949  14.343 -11.566  1.00 11.15           C  
+ATOM   1092  CD2 LEU B 352     -11.942  16.123 -10.091  1.00 13.37           C  
+ATOM   1093  H   LEU B 352      -8.118  13.793  -7.581  1.00 14.78           H  
+ATOM   1094  HA  LEU B 352      -9.077  13.020 -10.012  1.00 12.55           H  
+ATOM   1095  HB2 LEU B 352     -10.872  13.906  -8.942  1.00 13.39           H  
+ATOM   1096  HB3 LEU B 352     -10.028  15.176  -8.496  1.00 13.39           H  
+ATOM   1097  HG  LEU B 352      -9.999  15.924 -10.694  1.00 14.88           H  
+ATOM   1098 HD11 LEU B 352     -11.366  14.832 -12.292  1.00 13.39           H  
+ATOM   1099 HD12 LEU B 352     -10.106  13.965 -11.863  1.00 13.39           H  
+ATOM   1100 HD13 LEU B 352     -11.539  13.637 -11.260  1.00 13.39           H  
+ATOM   1101 HD21 LEU B 352     -12.227  16.594 -10.889  1.00 16.04           H  
+ATOM   1102 HD22 LEU B 352     -12.645  15.525  -9.791  1.00 16.04           H  
+ATOM   1103 HD23 LEU B 352     -11.728  16.758  -9.390  1.00 16.04           H  
+ATOM   1104  N   ILE B 353      -7.305  14.274 -11.122  1.00  9.15           N  
+ATOM   1105  CA  ILE B 353      -6.198  14.927 -11.794  1.00  8.98           C  
+ATOM   1106  C   ILE B 353      -6.763  15.608 -13.019  1.00 10.49           C  
+ATOM   1107  O   ILE B 353      -7.298  14.938 -13.906  1.00 12.31           O  
+ATOM   1108  CB  ILE B 353      -5.108  13.907 -12.145  1.00  9.77           C  
+ATOM   1109  CG1 ILE B 353      -4.505  13.365 -10.843  1.00 15.61           C  
+ATOM   1110  CG2 ILE B 353      -4.056  14.508 -13.046  1.00 12.75           C  
+ATOM   1111  CD1 ILE B 353      -3.861  12.026 -11.006  1.00 26.79           C  
+ATOM   1112  H   ILE B 353      -7.626  13.621 -11.581  1.00 10.98           H  
+ATOM   1113  HA  ILE B 353      -5.802  15.610 -11.232  1.00 10.77           H  
+ATOM   1114  HB  ILE B 353      -5.504  13.174 -12.642  1.00 11.72           H  
+ATOM   1115 HG12 ILE B 353      -3.829  13.985 -10.528  1.00 18.73           H  
+ATOM   1116 HG13 ILE B 353      -5.210  13.278 -10.183  1.00 18.73           H  
+ATOM   1117 HG21 ILE B 353      -3.287  13.917 -13.071  1.00 15.30           H  
+ATOM   1118 HG22 ILE B 353      -4.424  14.609 -13.938  1.00 15.30           H  
+ATOM   1119 HG23 ILE B 353      -3.796  15.374 -12.695  1.00 15.30           H  
+ATOM   1120 HD11 ILE B 353      -3.526  11.730 -10.146  1.00 32.15           H  
+ATOM   1121 HD12 ILE B 353      -4.520  11.397 -11.339  1.00 32.15           H  
+ATOM   1122 HD13 ILE B 353      -3.129  12.102 -11.638  1.00 32.15           H  
+ATOM   1123  N   LEU B 354      -6.663  16.933 -13.071  1.00  9.72           N  
+ATOM   1124  CA  LEU B 354      -7.373  17.723 -14.074  1.00  9.49           C  
+ATOM   1125  C   LEU B 354      -6.410  18.278 -15.117  1.00  8.29           C  
+ATOM   1126  O   LEU B 354      -5.375  18.853 -14.763  1.00  9.36           O  
+ATOM   1127  CB  LEU B 354      -8.141  18.863 -13.399  1.00  9.56           C  
+ATOM   1128  CG  LEU B 354      -9.274  18.349 -12.498  1.00 11.19           C  
+ATOM   1129  CD1 LEU B 354      -9.718  19.392 -11.488  1.00 14.14           C  
+ATOM   1130  CD2 LEU B 354     -10.452  17.897 -13.382  1.00 13.41           C  
+ATOM   1131  H   LEU B 354      -6.186  17.402 -12.531  1.00 11.66           H  
+ATOM   1132  HA  LEU B 354      -7.996  17.148 -14.545  1.00 11.39           H  
+ATOM   1133  HB2 LEU B 354      -7.528  19.378 -12.851  1.00 11.47           H  
+ATOM   1134  HB3 LEU B 354      -8.531  19.431 -14.082  1.00 11.47           H  
+ATOM   1135  HG  LEU B 354      -8.953  17.595 -11.981  1.00 13.42           H  
+ATOM   1136 HD11 LEU B 354     -10.373  18.996 -10.893  1.00 16.97           H  
+ATOM   1137 HD12 LEU B 354      -8.946  19.688 -10.981  1.00 16.97           H  
+ATOM   1138 HD13 LEU B 354     -10.111  20.143 -11.961  1.00 16.97           H  
+ATOM   1139 HD21 LEU B 354     -11.192  17.636 -12.813  1.00 16.09           H  
+ATOM   1140 HD22 LEU B 354     -10.718  18.633 -13.955  1.00 16.09           H  
+ATOM   1141 HD23 LEU B 354     -10.169  17.142 -13.923  1.00 16.09           H  
+ATOM   1142  N   ARG B 355      -6.751  18.102 -16.392  1.00  9.48           N  
+ATOM   1143  CA  ARG B 355      -5.948  18.615 -17.502  1.00 10.02           C  
+ATOM   1144  C   ARG B 355      -6.875  19.333 -18.482  1.00  8.74           C  
+ATOM   1145  O   ARG B 355      -7.110  18.875 -19.612  1.00  9.60           O  
+ATOM   1146  CB  ARG B 355      -5.152  17.504 -18.199  1.00 12.80           C  
+ATOM   1147  CG  ARG B 355      -3.824  17.134 -17.487  1.00 13.08           C  
+ATOM   1148  CD  ARG B 355      -4.047  16.098 -16.461  1.00 12.71           C  
+ATOM   1149  NE  ARG B 355      -2.789  15.708 -15.834  1.00 11.07           N  
+ATOM   1150  CZ  ARG B 355      -2.181  16.423 -14.902  1.00 11.59           C  
+ATOM   1151  NH1 ARG B 355      -2.647  17.602 -14.526  1.00 13.54           N  
+ATOM   1152  NH2 ARG B 355      -1.075  15.949 -14.336  1.00 12.79           N  
+ATOM   1153  H   ARG B 355      -7.457  17.681 -16.644  1.00 11.37           H  
+ATOM   1154  HA  ARG B 355      -5.306  19.254 -17.154  1.00 12.02           H  
+ATOM   1155  HB2 ARG B 355      -5.700  16.704 -18.233  1.00 15.36           H  
+ATOM   1156  HB3 ARG B 355      -4.934  17.795 -19.098  1.00 15.36           H  
+ATOM   1157  HG2 ARG B 355      -3.193  16.791 -18.139  1.00 15.70           H  
+ATOM   1158  HG3 ARG B 355      -3.459  17.922 -17.054  1.00 15.70           H  
+ATOM   1159  HD2 ARG B 355      -4.638  16.444 -15.775  1.00 15.25           H  
+ATOM   1160  HD3 ARG B 355      -4.441  15.313 -16.874  1.00 15.25           H  
+ATOM   1161  HE  ARG B 355      -2.423  14.971 -16.084  1.00 13.28           H  
+ATOM   1162 HH11 ARG B 355      -3.360  17.918 -14.889  1.00 16.25           H  
+ATOM   1163 HH12 ARG B 355      -2.238  18.052 -13.918  1.00 16.25           H  
+ATOM   1164 HH21 ARG B 355      -0.762  15.185 -14.578  1.00 15.34           H  
+ATOM   1165 HH22 ARG B 355      -0.672  16.406 -13.730  1.00 15.34           H  
+ATOM   1166  N   PRO B 356      -7.408  20.492 -18.090  1.00  9.62           N  
+ATOM   1167  CA  PRO B 356      -8.173  21.281 -19.057  1.00  9.08           C  
+ATOM   1168  C   PRO B 356      -7.330  21.638 -20.272  1.00 10.13           C  
+ATOM   1169  O   PRO B 356      -6.116  21.833 -20.179  1.00 10.25           O  
+ATOM   1170  CB  PRO B 356      -8.572  22.532 -18.266  1.00  9.84           C  
+ATOM   1171  CG  PRO B 356      -7.518  22.651 -17.226  1.00  9.27           C  
+ATOM   1172  CD  PRO B 356      -7.191  21.225 -16.839  1.00  9.69           C  
+ATOM   1173  HA  PRO B 356      -8.970  20.804 -19.338  1.00 10.89           H  
+ATOM   1174  HB2 PRO B 356      -8.579  23.308 -18.848  1.00 11.81           H  
+ATOM   1175  HB3 PRO B 356      -9.447  22.409 -17.866  1.00 11.81           H  
+ATOM   1176  HG2 PRO B 356      -6.740  23.099 -17.593  1.00 11.13           H  
+ATOM   1177  HG3 PRO B 356      -7.858  23.148 -16.465  1.00 11.13           H  
+ATOM   1178  HD2 PRO B 356      -6.270  21.148 -16.547  1.00 11.63           H  
+ATOM   1179  HD3 PRO B 356      -7.788  20.909 -16.144  1.00 11.63           H  
+ATOM   1180  N   PHE B 357      -7.991  21.701 -21.426  1.00  9.45           N  
+ATOM   1181  CA  PHE B 357      -7.259  21.900 -22.679  1.00 11.09           C  
+ATOM   1182  C   PHE B 357      -7.108  23.385 -22.989  1.00 11.60           C  
+ATOM   1183  O   PHE B 357      -8.092  24.135 -22.923  1.00 11.21           O  
+ATOM   1184  CB  PHE B 357      -7.987  21.219 -23.845  1.00  9.67           C  
+ATOM   1185  CG  PHE B 357      -7.721  19.746 -23.952  1.00  9.94           C  
+ATOM   1186  CD1 PHE B 357      -8.012  18.889 -22.914  1.00 10.46           C  
+ATOM   1187  CD2 PHE B 357      -7.233  19.212 -25.134  1.00 10.22           C  
+ATOM   1188  CE1 PHE B 357      -7.767  17.527 -23.025  1.00 10.36           C  
+ATOM   1189  CE2 PHE B 357      -7.005  17.847 -25.259  1.00 10.88           C  
+ATOM   1190  CZ  PHE B 357      -7.254  17.010 -24.193  1.00 10.36           C  
+ATOM   1191  H   PHE B 357      -8.845  21.634 -21.510  1.00 11.34           H  
+ATOM   1192  HA  PHE B 357      -6.373  21.516 -22.589  1.00 13.31           H  
+ATOM   1193  HB2 PHE B 357      -8.942  21.339 -23.727  1.00 11.60           H  
+ATOM   1194  HB3 PHE B 357      -7.700  21.632 -24.674  1.00 11.60           H  
+ATOM   1195  HD1 PHE B 357      -8.377  19.227 -22.128  1.00 12.55           H  
+ATOM   1196  HD2 PHE B 357      -7.057  19.775 -25.853  1.00 12.26           H  
+ATOM   1197  HE1 PHE B 357      -7.950  16.963 -22.308  1.00 12.43           H  
+ATOM   1198  HE2 PHE B 357      -6.685  17.499 -26.060  1.00 13.06           H  
+ATOM   1199  HZ  PHE B 357      -7.076  16.100 -24.262  1.00 12.43           H  
+ATOM   1200  N   PRO B 358      -5.909  23.830 -23.350  1.00 10.40           N  
+ATOM   1201  CA  PRO B 358      -5.743  25.225 -23.764  1.00 10.72           C  
+ATOM   1202  C   PRO B 358      -6.473  25.481 -25.077  1.00 10.23           C  
+ATOM   1203  O   PRO B 358      -6.303  24.745 -26.051  1.00 11.68           O  
+ATOM   1204  CB  PRO B 358      -4.219  25.360 -23.928  1.00 11.68           C  
+ATOM   1205  CG  PRO B 358      -3.752  23.965 -24.311  1.00 10.00           C  
+ATOM   1206  CD  PRO B 358      -4.663  23.043 -23.504  1.00  9.95           C  
+ATOM   1207  HA  PRO B 358      -6.058  25.839 -23.083  1.00 12.87           H  
+ATOM   1208  HB2 PRO B 358      -4.015  26.001 -24.627  1.00 14.01           H  
+ATOM   1209  HB3 PRO B 358      -3.819  25.644 -23.091  1.00 14.01           H  
+ATOM   1210  HG2 PRO B 358      -3.865  23.824 -25.264  1.00 11.99           H  
+ATOM   1211  HG3 PRO B 358      -2.822  23.843 -24.065  1.00 11.99           H  
+ATOM   1212  HD2 PRO B 358      -4.834  22.219 -23.987  1.00 11.94           H  
+ATOM   1213  HD3 PRO B 358      -4.272  22.845 -22.638  1.00 11.94           H  
+ATOM   1214  N   GLN B 359      -7.301  26.513 -25.088  1.00 11.90           N  
+ATOM   1215  CA  GLN B 359      -8.123  26.849 -26.241  1.00 12.17           C  
+ATOM   1216  C   GLN B 359      -7.430  27.896 -27.095  1.00 13.74           C  
+ATOM   1217  O   GLN B 359      -6.756  28.796 -26.583  1.00 14.27           O  
+ATOM   1218  CB  GLN B 359      -9.485  27.356 -25.767  1.00 11.84           C  
+ATOM   1219  CG  GLN B 359     -10.213  26.400 -24.855  1.00 11.40           C  
+ATOM   1220  CD  GLN B 359     -10.564  25.125 -25.546  1.00 14.24           C  
+ATOM   1221  OE1 GLN B 359     -11.171  25.138 -26.625  1.00 17.53           O  
+ATOM   1222  NE2 GLN B 359     -10.133  23.994 -24.980  1.00 12.95           N  
+ATOM   1223  H   GLN B 359      -7.407  27.048 -24.424  1.00 14.28           H  
+ATOM   1224  HA  GLN B 359      -8.261  26.067 -26.799  1.00 14.61           H  
+ATOM   1225  HB2 GLN B 359      -9.357  28.186 -25.282  1.00 14.20           H  
+ATOM   1226  HB3 GLN B 359     -10.047  27.509 -26.543  1.00 14.20           H  
+ATOM   1227  HG2 GLN B 359      -9.646  26.187 -24.098  1.00 13.68           H  
+ATOM   1228  HG3 GLN B 359     -11.034  26.815 -24.548  1.00 13.68           H  
+ATOM   1229 HE21 GLN B 359      -9.676  24.024 -24.252  1.00 15.54           H  
+ATOM   1230 HE22 GLN B 359     -10.312  23.235 -25.344  1.00 15.54           H  
+ATOM   1231  N   GLY B 360      -7.638  27.785 -28.399  1.00 13.22           N  
+ATOM   1232  CA  GLY B 360      -7.012  28.654 -29.382  1.00 16.07           C  
+ATOM   1233  C   GLY B 360      -5.998  27.901 -30.230  1.00 15.92           C  
+ATOM   1234  O   GLY B 360      -5.676  26.734 -29.992  1.00 16.21           O  
+ATOM   1235  H   GLY B 360      -8.155  27.195 -28.750  1.00 15.87           H  
+ATOM   1236  HA2 GLY B 360      -7.692  29.023 -29.967  1.00 19.29           H  
+ATOM   1237  HA3 GLY B 360      -6.557  29.381 -28.929  1.00 19.29           H  
+ATOM   1238  N   LYS B 361      -5.467  28.623 -31.220  1.00 18.39           N  
+ATOM   1239  CA  LYS B 361      -4.601  27.994 -32.211  1.00 19.67           C  
+ATOM   1240  C   LYS B 361      -3.327  27.441 -31.587  1.00 16.26           C  
+ATOM   1241  O   LYS B 361      -2.927  26.313 -31.896  1.00 18.88           O  
+ATOM   1242  CB  LYS B 361      -4.272  28.994 -33.316  1.00 25.95           C  
+ATOM   1243  CG  LYS B 361      -3.376  28.422 -34.415  1.00 34.02           C  
+ATOM   1244  CD  LYS B 361      -3.128  29.440 -35.524  1.00 53.14           C  
+ATOM   1245  CE  LYS B 361      -2.336  28.834 -36.676  1.00 57.64           C  
+ATOM   1246  NZ  LYS B 361      -2.166  29.816 -37.779  1.00 60.08           N  
+ATOM   1247  H   LYS B 361      -5.592  29.465 -31.337  1.00 22.07           H  
+ATOM   1248  HA  LYS B 361      -5.075  27.246 -32.606  1.00 23.60           H  
+ATOM   1249  HB2 LYS B 361      -5.100  29.285 -33.730  1.00 31.14           H  
+ATOM   1250  HB3 LYS B 361      -3.813  29.754 -32.924  1.00 31.14           H  
+ATOM   1251  HG2 LYS B 361      -2.519  28.173 -34.033  1.00 40.83           H  
+ATOM   1252  HG3 LYS B 361      -3.803  27.644 -34.806  1.00 40.83           H  
+ATOM   1253  HD2 LYS B 361      -3.979  29.751 -35.870  1.00 63.76           H  
+ATOM   1254  HD3 LYS B 361      -2.622  30.186 -35.167  1.00 63.76           H  
+ATOM   1255  HE2 LYS B 361      -1.457  28.570 -36.361  1.00 69.17           H  
+ATOM   1256  HE3 LYS B 361      -2.809  28.061 -37.023  1.00 69.17           H  
+ATOM   1257  HZ1 LYS B 361      -1.698  29.451 -38.442  1.00 72.10           H  
+ATOM   1258  HZ2 LYS B 361      -2.962  30.065 -38.090  1.00 72.10           H  
+ATOM   1259  HZ3 LYS B 361      -1.733  30.535 -37.482  1.00 72.10           H  
+ATOM   1260  N   LYS B 362      -2.684  28.202 -30.695  1.00 17.10           N  
+ATOM   1261  CA  LYS B 362      -1.467  27.710 -30.061  1.00 17.34           C  
+ATOM   1262  C   LYS B 362      -1.765  26.494 -29.195  1.00 13.86           C  
+ATOM   1263  O   LYS B 362      -1.008  25.513 -29.190  1.00 16.71           O  
+ATOM   1264  CB  LYS B 362      -0.823  28.820 -29.227  1.00 20.77           C  
+ATOM   1265  CG  LYS B 362      -0.484  30.089 -30.006  1.00 36.53           C  
+ATOM   1266  CD  LYS B 362       0.549  29.832 -31.100  1.00 41.46           C  
+ATOM   1267  CE  LYS B 362       1.110  31.142 -31.660  1.00 43.59           C  
+ATOM   1268  NZ  LYS B 362       2.238  30.881 -32.595  1.00 40.39           N  
+ATOM   1269  H   LYS B 362      -2.929  28.988 -30.447  1.00 20.52           H  
+ATOM   1270  HA  LYS B 362      -0.834  27.448 -30.748  1.00 20.81           H  
+ATOM   1271  HB2 LYS B 362      -1.437  29.068 -28.518  1.00 24.92           H  
+ATOM   1272  HB3 LYS B 362       0.002  28.481 -28.847  1.00 24.92           H  
+ATOM   1273  HG2 LYS B 362      -1.290  30.431 -30.425  1.00 43.84           H  
+ATOM   1274  HG3 LYS B 362      -0.121  30.750 -29.396  1.00 43.84           H  
+ATOM   1275  HD2 LYS B 362       1.285  29.317 -30.733  1.00 49.75           H  
+ATOM   1276  HD3 LYS B 362       0.133  29.343 -31.827  1.00 49.75           H  
+ATOM   1277  HE2 LYS B 362       0.413  31.612 -32.143  1.00 52.31           H  
+ATOM   1278  HE3 LYS B 362       1.437  31.692 -30.931  1.00 52.31           H  
+ATOM   1279  HZ1 LYS B 362       2.561  31.651 -32.904  1.00 48.46           H  
+ATOM   1280  HZ2 LYS B 362       2.888  30.444 -32.174  1.00 48.46           H  
+ATOM   1281  HZ3 LYS B 362       1.957  30.390 -33.282  1.00 48.46           H  
+ATOM   1282  N   GLY B 363      -2.871  26.526 -28.468  1.00 14.73           N  
+ATOM   1283  CA  GLY B 363      -3.202  25.373 -27.645  1.00 13.79           C  
+ATOM   1284  C   GLY B 363      -3.453  24.134 -28.474  1.00 13.44           C  
+ATOM   1285  O   GLY B 363      -2.976  23.045 -28.141  1.00 14.40           O  
+ATOM   1286  H   GLY B 363      -3.429  27.179 -28.433  1.00 17.67           H  
+ATOM   1287  HA2 GLY B 363      -2.469  25.191 -27.036  1.00 16.55           H  
+ATOM   1288  HA3 GLY B 363      -4.001  25.564 -27.129  1.00 16.55           H  
+ATOM   1289  N   GLU B 364      -4.202  24.281 -29.571  1.00 13.04           N  
+ATOM   1290  CA  GLU B 364      -4.514  23.135 -30.420  1.00 11.82           C  
+ATOM   1291  C   GLU B 364      -3.255  22.440 -30.935  1.00 14.64           C  
+ATOM   1292  O   GLU B 364      -3.262  21.217 -31.133  1.00 14.11           O  
+ATOM   1293  CB  GLU B 364      -5.405  23.568 -31.600  1.00 13.37           C  
+ATOM   1294  CG  GLU B 364      -6.801  23.882 -31.187  1.00 15.82           C  
+ATOM   1295  CD  GLU B 364      -7.689  24.394 -32.301  1.00 22.94           C  
+ATOM   1296  OE1 GLU B 364      -7.393  24.131 -33.485  1.00 32.10           O  
+ATOM   1297  OE2 GLU B 364      -8.699  25.059 -31.980  1.00 21.99           O  
+ATOM   1298  H   GLU B 364      -4.537  25.026 -29.842  1.00 15.64           H  
+ATOM   1299  HA  GLU B 364      -5.010  22.492 -29.888  1.00 14.18           H  
+ATOM   1300  HB2 GLU B 364      -5.027  24.363 -32.006  1.00 16.04           H  
+ATOM   1301  HB3 GLU B 364      -5.440  22.848 -32.250  1.00 16.04           H  
+ATOM   1302  HG2 GLU B 364      -7.208  23.074 -30.836  1.00 18.98           H  
+ATOM   1303  HG3 GLU B 364      -6.773  24.565 -30.498  1.00 18.98           H  
+ATOM   1304  N   GLU B 365      -2.175  23.190 -31.170  1.00 13.12           N  
+ATOM   1305  CA  GLU B 365      -0.930  22.591 -31.627  1.00 16.12           C  
+ATOM   1306  C   GLU B 365      -0.352  21.597 -30.630  1.00 17.16           C  
+ATOM   1307  O   GLU B 365       0.403  20.707 -31.035  1.00 18.32           O  
+ATOM   1308  CB  GLU B 365       0.098  23.692 -31.917  1.00 18.93           C  
+ATOM   1309  CG  GLU B 365      -0.245  24.476 -33.185  1.00 20.10           C  
+ATOM   1310  CD  GLU B 365       0.550  25.755 -33.350  1.00 29.36           C  
+ATOM   1311  OE1 GLU B 365       1.479  25.991 -32.552  1.00 31.88           O  
+ATOM   1312  OE2 GLU B 365       0.232  26.528 -34.282  1.00 35.97           O  
+ATOM   1313  H   GLU B 365      -2.141  24.044 -31.072  1.00 15.75           H  
+ATOM   1314  HA  GLU B 365      -1.107  22.109 -32.450  1.00 19.34           H  
+ATOM   1315  HB2 GLU B 365       0.119  24.313 -31.173  1.00 22.72           H  
+ATOM   1316  HB3 GLU B 365       0.972  23.288 -32.037  1.00 22.72           H  
+ATOM   1317  HG2 GLU B 365      -0.065  23.915 -33.956  1.00 24.12           H  
+ATOM   1318  HG3 GLU B 365      -1.185  24.714 -33.160  1.00 24.12           H  
+ATOM   1319  N   GLN B 366      -0.690  21.714 -29.347  1.00 14.72           N  
+ATOM   1320  CA  GLN B 366      -0.148  20.829 -28.326  1.00 13.60           C  
+ATOM   1321  C   GLN B 366      -1.137  19.763 -27.869  1.00 12.86           C  
+ATOM   1322  O   GLN B 366      -0.786  18.950 -27.010  1.00 12.94           O  
+ATOM   1323  CB  GLN B 366       0.316  21.631 -27.108  1.00 17.13           C  
+ATOM   1324  CG  GLN B 366       1.431  22.656 -27.365  1.00 23.17           C  
+ATOM   1325  CD  GLN B 366       2.831  22.046 -27.356  1.00 28.89           C  
+ATOM   1326  OE1 GLN B 366       3.053  20.917 -27.821  1.00 27.38           O  
+ATOM   1327  NE2 GLN B 366       3.788  22.797 -26.819  1.00 32.19           N  
+ATOM   1328  H   GLN B 366      -1.236  22.304 -29.044  1.00 17.67           H  
+ATOM   1329  HA  GLN B 366       0.625  20.382 -28.703  1.00 16.31           H  
+ATOM   1330  HB2 GLN B 366      -0.446  22.118 -26.757  1.00 20.56           H  
+ATOM   1331  HB3 GLN B 366       0.647  21.007 -26.443  1.00 20.56           H  
+ATOM   1332  HG2 GLN B 366       1.289  23.062 -28.234  1.00 27.80           H  
+ATOM   1333  HG3 GLN B 366       1.398  23.334 -26.672  1.00 27.80           H  
+ATOM   1334 HE21 GLN B 366       3.598  23.574 -26.503  1.00 38.62           H  
+ATOM   1335 HE22 GLN B 366       4.596  22.505 -26.786  1.00 38.62           H  
+ATOM   1336  N   TRP B 367      -2.345  19.697 -28.445  1.00 13.21           N  
+ATOM   1337  CA  TRP B 367      -3.366  18.822 -27.863  1.00 10.36           C  
+ATOM   1338  C   TRP B 367      -2.986  17.344 -27.923  1.00 11.91           C  
+ATOM   1339  O   TRP B 367      -3.269  16.594 -26.985  1.00 12.33           O  
+ATOM   1340  CB  TRP B 367      -4.717  19.009 -28.552  1.00 12.21           C  
+ATOM   1341  CG  TRP B 367      -5.445  20.244 -28.137  1.00 10.64           C  
+ATOM   1342  CD1 TRP B 367      -5.045  21.172 -27.223  1.00 10.94           C  
+ATOM   1343  CD2 TRP B 367      -6.712  20.684 -28.631  1.00  9.15           C  
+ATOM   1344  NE1 TRP B 367      -5.992  22.159 -27.106  1.00 10.05           N  
+ATOM   1345  CE2 TRP B 367      -7.021  21.883 -27.972  1.00  9.90           C  
+ATOM   1346  CE3 TRP B 367      -7.610  20.184 -29.577  1.00 11.56           C  
+ATOM   1347  CZ2 TRP B 367      -8.196  22.590 -28.227  1.00 11.86           C  
+ATOM   1348  CZ3 TRP B 367      -8.760  20.890 -29.834  1.00 11.37           C  
+ATOM   1349  CH2 TRP B 367      -9.040  22.082 -29.180  1.00 11.86           C  
+ATOM   1350  H   TRP B 367      -2.588  20.131 -29.146  1.00 15.86           H  
+ATOM   1351  HA  TRP B 367      -3.447  19.085 -26.932  1.00 12.44           H  
+ATOM   1352  HB2 TRP B 367      -4.572  19.060 -29.510  1.00 14.65           H  
+ATOM   1353  HB3 TRP B 367      -5.281  18.249 -28.341  1.00 14.65           H  
+ATOM   1354  HD1 TRP B 367      -4.247  21.140 -26.746  1.00 13.12           H  
+ATOM   1355  HE1 TRP B 367      -5.947  22.837 -26.580  1.00 12.06           H  
+ATOM   1356  HE3 TRP B 367      -7.432  19.389 -30.025  1.00 13.87           H  
+ATOM   1357  HZ2 TRP B 367      -8.398  23.374 -27.769  1.00 14.23           H  
+ATOM   1358  HZ3 TRP B 367      -9.365  20.562 -30.460  1.00 13.65           H  
+ATOM   1359  HH2 TRP B 367      -9.818  22.545 -29.393  1.00 14.23           H  
+ATOM   1360  N   ASP B 368      -2.398  16.886 -29.030  1.00 12.17           N  
+ATOM   1361  CA  ASP B 368      -2.099  15.460 -29.093  1.00 12.22           C  
+ATOM   1362  C   ASP B 368      -1.007  15.092 -28.098  1.00 13.09           C  
+ATOM   1363  O   ASP B 368      -1.097  14.067 -27.413  1.00 12.91           O  
+ATOM   1364  CB  ASP B 368      -1.685  15.029 -30.492  1.00 14.42           C  
+ATOM   1365  CG  ASP B 368      -1.700  13.523 -30.614  1.00 15.59           C  
+ATOM   1366  OD1 ASP B 368      -2.806  12.936 -30.479  1.00 17.52           O  
+ATOM   1367  OD2 ASP B 368      -0.624  12.919 -30.734  1.00 19.61           O  
+ATOM   1368  H   ASP B 368      -2.175  17.354 -29.717  1.00 14.61           H  
+ATOM   1369  HA  ASP B 368      -2.913  14.980 -28.875  1.00 14.66           H  
+ATOM   1370  HB2 ASP B 368      -2.305  15.397 -31.141  1.00 17.30           H  
+ATOM   1371  HB3 ASP B 368      -0.787  15.345 -30.676  1.00 17.30           H  
+ATOM   1372  N   LYS B 369       0.023  15.934 -27.980  1.00 12.94           N  
+ATOM   1373  CA  LYS B 369       1.077  15.653 -27.018  1.00 11.36           C  
+ATOM   1374  C   LYS B 369       0.533  15.720 -25.593  1.00 10.78           C  
+ATOM   1375  O   LYS B 369       0.885  14.887 -24.748  1.00 12.85           O  
+ATOM   1376  CB  LYS B 369       2.231  16.629 -27.212  1.00 15.82           C  
+ATOM   1377  CG  LYS B 369       3.441  16.337 -26.380  1.00 23.07           C  
+ATOM   1378  CD  LYS B 369       4.613  17.242 -26.786  1.00 27.95           C  
+ATOM   1379  CE  LYS B 369       5.265  16.799 -28.086  1.00 38.41           C  
+ATOM   1380  NZ  LYS B 369       6.602  17.446 -28.270  1.00 41.42           N  
+ATOM   1381  H   LYS B 369       0.129  16.655 -28.437  1.00 15.53           H  
+ATOM   1382  HA  LYS B 369       1.422  14.759 -27.166  1.00 13.63           H  
+ATOM   1383  HB2 LYS B 369       2.502  16.604 -28.143  1.00 18.98           H  
+ATOM   1384  HB3 LYS B 369       1.924  17.519 -26.980  1.00 18.98           H  
+ATOM   1385  HG2 LYS B 369       3.238  16.497 -25.446  1.00 27.68           H  
+ATOM   1386  HG3 LYS B 369       3.708  15.413 -26.509  1.00 27.68           H  
+ATOM   1387  HD2 LYS B 369       4.289  18.149 -26.906  1.00 33.54           H  
+ATOM   1388  HD3 LYS B 369       5.287  17.221 -26.089  1.00 33.54           H  
+ATOM   1389  HE2 LYS B 369       5.390  15.837 -28.072  1.00 46.10           H  
+ATOM   1390  HE3 LYS B 369       4.698  17.049 -28.832  1.00 46.10           H  
+ATOM   1391  HZ1 LYS B 369       7.143  17.225 -27.599  1.00 49.71           H  
+ATOM   1392  HZ2 LYS B 369       6.967  17.177 -29.036  1.00 49.71           H  
+ATOM   1393  HZ3 LYS B 369       6.512  18.331 -28.288  1.00 49.71           H  
+ATOM   1394  N   TYR B 370      -0.352  16.685 -25.323  1.00 11.79           N  
+ATOM   1395  CA  TYR B 370      -0.975  16.806 -24.014  1.00 11.48           C  
+ATOM   1396  C   TYR B 370      -1.804  15.575 -23.673  1.00 10.45           C  
+ATOM   1397  O   TYR B 370      -1.755  15.091 -22.542  1.00 10.44           O  
+ATOM   1398  CB  TYR B 370      -1.825  18.068 -24.024  1.00 11.48           C  
+ATOM   1399  CG  TYR B 370      -2.387  18.622 -22.741  1.00 10.38           C  
+ATOM   1400  CD1 TYR B 370      -1.603  18.809 -21.619  1.00  9.42           C  
+ATOM   1401  CD2 TYR B 370      -3.707  19.023 -22.688  1.00  9.19           C  
+ATOM   1402  CE1 TYR B 370      -2.118  19.394 -20.480  1.00 11.43           C  
+ATOM   1403  CE2 TYR B 370      -4.239  19.584 -21.559  1.00 10.47           C  
+ATOM   1404  CZ  TYR B 370      -3.444  19.778 -20.463  1.00 11.27           C  
+ATOM   1405  OH  TYR B 370      -3.959  20.363 -19.337  1.00 11.11           O  
+ATOM   1406  H   TYR B 370      -0.608  17.283 -25.887  1.00 14.15           H  
+ATOM   1407  HA  TYR B 370      -0.300  16.882 -23.321  1.00 13.78           H  
+ATOM   1408  HB2 TYR B 370      -1.281  18.776 -24.404  1.00 13.78           H  
+ATOM   1409  HB3 TYR B 370      -2.588  17.893 -24.596  1.00 13.78           H  
+ATOM   1410  HD1 TYR B 370      -0.714  18.537 -21.632  1.00 11.30           H  
+ATOM   1411  HD2 TYR B 370      -4.247  18.909 -23.437  1.00 11.03           H  
+ATOM   1412  HE1 TYR B 370      -1.579  19.527 -19.734  1.00 13.72           H  
+ATOM   1413  HE2 TYR B 370      -5.135  19.831 -21.537  1.00 12.56           H  
+ATOM   1414  HH  TYR B 370      -4.744  20.623 -19.482  1.00 13.33           H  
+ATOM   1415  N   ARG B 371      -2.574  15.066 -24.635  1.00 10.40           N  
+ATOM   1416  CA  ARG B 371      -3.355  13.852 -24.422  1.00 11.13           C  
+ATOM   1417  C   ARG B 371      -2.464  12.654 -24.136  1.00 10.83           C  
+ATOM   1418  O   ARG B 371      -2.717  11.874 -23.208  1.00 11.67           O  
+ATOM   1419  CB  ARG B 371      -4.211  13.545 -25.653  1.00 12.80           C  
+ATOM   1420  CG  ARG B 371      -5.426  14.376 -25.762  1.00 12.35           C  
+ATOM   1421  CD  ARG B 371      -6.183  14.057 -27.040  1.00 12.27           C  
+ATOM   1422  NE  ARG B 371      -7.503  14.668 -26.982  1.00 11.32           N  
+ATOM   1423  CZ  ARG B 371      -8.062  15.432 -27.909  1.00  9.62           C  
+ATOM   1424  NH1 ARG B 371      -7.460  15.687 -29.064  1.00 12.12           N  
+ATOM   1425  NH2 ARG B 371      -9.262  15.953 -27.674  1.00 10.51           N  
+ATOM   1426  H   ARG B 371      -2.660  15.406 -25.421  1.00 12.48           H  
+ATOM   1427  HA  ARG B 371      -3.933  14.007 -23.659  1.00 13.35           H  
+ATOM   1428  HB2 ARG B 371      -3.677  13.697 -26.448  1.00 15.36           H  
+ATOM   1429  HB3 ARG B 371      -4.491  12.617 -25.614  1.00 15.36           H  
+ATOM   1430  HG2 ARG B 371      -6.009  14.200 -25.007  1.00 14.82           H  
+ATOM   1431  HG3 ARG B 371      -5.177  15.314 -25.777  1.00 14.82           H  
+ATOM   1432  HD2 ARG B 371      -5.704  14.415 -27.804  1.00 14.72           H  
+ATOM   1433  HD3 ARG B 371      -6.284  13.097 -27.132  1.00 14.72           H  
+ATOM   1434  HE  ARG B 371      -7.968  14.517 -26.274  1.00 13.58           H  
+ATOM   1435 HH11 ARG B 371      -6.685  15.352 -29.228  1.00 14.54           H  
+ATOM   1436 HH12 ARG B 371      -7.845  16.186 -29.649  1.00 14.54           H  
+ATOM   1437 HH21 ARG B 371      -9.663  15.792 -26.930  1.00 12.61           H  
+ATOM   1438 HH22 ARG B 371      -9.638  16.451 -28.265  1.00 12.61           H  
+ATOM   1439  N   ARG B 372      -1.437  12.455 -24.961  1.00 11.11           N  
+ATOM   1440  CA  ARG B 372      -0.559  11.315 -24.742  1.00 10.30           C  
+ATOM   1441  C   ARG B 372       0.126  11.431 -23.389  1.00 11.09           C  
+ATOM   1442  O   ARG B 372       0.270  10.441 -22.658  1.00 13.35           O  
+ATOM   1443  CB  ARG B 372       0.450  11.218 -25.881  1.00 10.76           C  
+ATOM   1444  CG  ARG B 372      -0.221  10.820 -27.177  1.00 13.26           C  
+ATOM   1445  CD  ARG B 372       0.752  10.722 -28.296  1.00 14.15           C  
+ATOM   1446  NE  ARG B 372       0.042  10.348 -29.514  1.00 14.27           N  
+ATOM   1447  CZ  ARG B 372      -0.282   9.098 -29.848  1.00 13.25           C  
+ATOM   1448  NH1 ARG B 372       0.107   8.059 -29.124  1.00 13.85           N  
+ATOM   1449  NH2 ARG B 372      -1.049   8.896 -30.911  1.00 13.69           N  
+ATOM   1450  H   ARG B 372      -1.234  12.952 -25.633  1.00 13.33           H  
+ATOM   1451  HA  ARG B 372      -1.072  10.492 -24.744  1.00 12.36           H  
+ATOM   1452  HB2 ARG B 372       0.875  12.080 -26.007  1.00 12.91           H  
+ATOM   1453  HB3 ARG B 372       1.117  10.548 -25.663  1.00 12.91           H  
+ATOM   1454  HG2 ARG B 372      -0.645   9.955 -27.066  1.00 15.91           H  
+ATOM   1455  HG3 ARG B 372      -0.886  11.487 -27.411  1.00 15.91           H  
+ATOM   1456  HD2 ARG B 372       1.185  11.579 -28.434  1.00 16.98           H  
+ATOM   1457  HD3 ARG B 372       1.416  10.043 -28.097  1.00 16.98           H  
+ATOM   1458  HE  ARG B 372      -0.183  10.977 -30.055  1.00 17.12           H  
+ATOM   1459 HH11 ARG B 372       0.581   8.182 -28.417  1.00 16.62           H  
+ATOM   1460 HH12 ARG B 372      -0.116   7.263 -29.360  1.00 16.62           H  
+ATOM   1461 HH21 ARG B 372      -1.330   9.565 -31.373  1.00 16.43           H  
+ATOM   1462 HH22 ARG B 372      -1.267   8.095 -31.138  1.00 16.43           H  
+ATOM   1463  N   ASP B 373       0.489  12.656 -23.009  1.00 10.03           N  
+ATOM   1464  CA  ASP B 373       1.074  12.891 -21.697  1.00 10.01           C  
+ATOM   1465  C   ASP B 373       0.102  12.517 -20.580  1.00 12.76           C  
+ATOM   1466  O   ASP B 373       0.432  11.703 -19.712  1.00 12.36           O  
+ATOM   1467  CB  ASP B 373       1.496  14.359 -21.642  1.00 11.60           C  
+ATOM   1468  CG  ASP B 373       2.275  14.721 -20.413  1.00 12.87           C  
+ATOM   1469  OD1 ASP B 373       2.649  13.803 -19.653  1.00 15.69           O  
+ATOM   1470  OD2 ASP B 373       2.488  15.951 -20.206  1.00 13.09           O  
+ATOM   1471  H   ASP B 373       0.406  13.364 -23.491  1.00 12.03           H  
+ATOM   1472  HA  ASP B 373       1.859  12.337 -21.560  1.00 12.01           H  
+ATOM   1473  HB2 ASP B 373       2.052  14.553 -22.412  1.00 13.91           H  
+ATOM   1474  HB3 ASP B 373       0.699  14.913 -21.660  1.00 13.91           H  
+ATOM   1475  N   MET B 374      -1.117  13.076 -20.604  1.00 11.73           N  
+ATOM   1476  CA  MET B 374      -2.018  12.925 -19.465  1.00 10.58           C  
+ATOM   1477  C   MET B 374      -2.549  11.505 -19.319  1.00 10.15           C  
+ATOM   1478  O   MET B 374      -2.928  11.116 -18.213  1.00 11.55           O  
+ATOM   1479  CB  MET B 374      -3.196  13.909 -19.561  1.00 11.34           C  
+ATOM   1480  CG  MET B 374      -4.264  13.539 -20.585  1.00 11.13           C  
+ATOM   1481  SD  MET B 374      -5.652  14.719 -20.651  1.00 12.17           S  
+ATOM   1482  CE  MET B 374      -4.857  16.115 -21.468  1.00 12.79           C  
+ATOM   1483  H   MET B 374      -1.435  13.537 -21.257  1.00 14.08           H  
+ATOM   1484  HA  MET B 374      -1.516  13.153 -18.667  1.00 12.69           H  
+ATOM   1485  HB2 MET B 374      -3.629  13.955 -18.694  1.00 13.60           H  
+ATOM   1486  HB3 MET B 374      -2.849  14.781 -19.805  1.00 13.60           H  
+ATOM   1487  HG2 MET B 374      -3.857  13.511 -21.465  1.00 13.36           H  
+ATOM   1488  HG3 MET B 374      -4.626  12.668 -20.359  1.00 13.36           H  
+ATOM   1489  HE1 MET B 374      -5.487  16.850 -21.522  1.00 15.35           H  
+ATOM   1490  HE2 MET B 374      -4.080  16.382 -20.952  1.00 15.35           H  
+ATOM   1491  HE3 MET B 374      -4.585  15.846 -22.359  1.00 15.35           H  
+ATOM   1492  N   ILE B 375      -2.585  10.727 -20.402  1.00 10.56           N  
+ATOM   1493  CA  ILE B 375      -3.081   9.350 -20.331  1.00  9.78           C  
+ATOM   1494  C   ILE B 375      -2.012   8.394 -19.830  1.00  9.85           C  
+ATOM   1495  O   ILE B 375      -2.346   7.299 -19.366  1.00 10.48           O  
+ATOM   1496  CB  ILE B 375      -3.642   8.965 -21.712  1.00 10.22           C  
+ATOM   1497  CG1 ILE B 375      -4.867   9.832 -22.023  1.00  9.74           C  
+ATOM   1498  CG2 ILE B 375      -4.019   7.494 -21.779  1.00 10.53           C  
+ATOM   1499  CD1 ILE B 375      -5.393   9.707 -23.462  1.00 11.90           C  
+ATOM   1500  H   ILE B 375      -2.330  10.969 -21.186  1.00 12.67           H  
+ATOM   1501  HA  ILE B 375      -3.806   9.271 -19.691  1.00 11.74           H  
+ATOM   1502  HB  ILE B 375      -2.947   9.123 -22.370  1.00 12.27           H  
+ATOM   1503 HG12 ILE B 375      -5.587   9.574 -21.426  1.00 11.69           H  
+ATOM   1504 HG13 ILE B 375      -4.633  10.762 -21.878  1.00 11.69           H  
+ATOM   1505 HG21 ILE B 375      -4.482   7.325 -22.614  1.00 12.63           H  
+ATOM   1506 HG22 ILE B 375      -3.211   6.959 -21.734  1.00 12.63           H  
+ATOM   1507 HG23 ILE B 375      -4.598   7.282 -21.030  1.00 12.63           H  
+ATOM   1508 HD11 ILE B 375      -6.044  10.408 -23.622  1.00 14.28           H  
+ATOM   1509 HD12 ILE B 375      -4.649   9.799 -24.078  1.00 14.28           H  
+ATOM   1510 HD13 ILE B 375      -5.808   8.838 -23.572  1.00 14.28           H  
+ATOM   1511  N   THR B 376      -0.746   8.807 -19.846  1.00 11.81           N  
+ATOM   1512  CA  THR B 376       0.348   7.897 -19.502  1.00 13.06           C  
+ATOM   1513  C   THR B 376       0.154   7.225 -18.139  1.00 12.02           C  
+ATOM   1514  O   THR B 376       0.348   6.006 -18.013  1.00 13.08           O  
+ATOM   1515  CB  THR B 376       1.684   8.651 -19.539  1.00 13.11           C  
+ATOM   1516  OG1 THR B 376       1.981   9.055 -20.884  1.00 14.52           O  
+ATOM   1517  CG2 THR B 376       2.797   7.756 -19.038  1.00 13.71           C  
+ATOM   1518  H   THR B 376      -0.493   9.603 -20.051  1.00 14.17           H  
+ATOM   1519  HA  THR B 376       0.366   7.192 -20.168  1.00 15.67           H  
+ATOM   1520  HB  THR B 376       1.627   9.437 -18.973  1.00 15.73           H  
+ATOM   1521  HG1 THR B 376       1.383   9.572 -21.167  1.00 17.42           H  
+ATOM   1522 HG21 THR B 376       3.655   8.096 -19.336  1.00 16.46           H  
+ATOM   1523 HG22 THR B 376       2.789   7.728 -18.068  1.00 16.46           H  
+ATOM   1524 HG23 THR B 376       2.679   6.856 -19.380  1.00 16.46           H  
+ATOM   1525  N   ARG B 377      -0.192   7.996 -17.096  1.00 10.71           N  
+ATOM   1526  CA  ARG B 377      -0.293   7.441 -15.751  1.00 12.39           C  
+ATOM   1527  C   ARG B 377      -1.517   6.560 -15.536  1.00 13.26           C  
+ATOM   1528  O   ARG B 377      -1.630   5.936 -14.469  1.00 14.47           O  
+ATOM   1529  CB  ARG B 377      -0.290   8.580 -14.732  1.00 13.06           C  
+ATOM   1530  CG  ARG B 377      -1.583   9.358 -14.648  1.00 11.72           C  
+ATOM   1531  CD  ARG B 377      -1.539  10.602 -13.759  1.00 15.30           C  
+ATOM   1532  NE  ARG B 377      -0.763  10.459 -12.531  1.00 28.57           N  
+ATOM   1533  CZ  ARG B 377      -1.174   9.970 -11.371  1.00 46.57           C  
+ATOM   1534  NH1 ARG B 377      -2.331   9.334 -11.248  1.00 52.32           N  
+ATOM   1535  NH2 ARG B 377      -0.395  10.118 -10.299  1.00 36.68           N  
+ATOM   1536  H   ARG B 377      -0.370   8.835 -17.146  1.00 12.85           H  
+ATOM   1537  HA  ARG B 377       0.483   6.880 -15.594  1.00 14.87           H  
+ATOM   1538  HB2 ARG B 377      -0.117   8.207 -13.853  1.00 15.68           H  
+ATOM   1539  HB3 ARG B 377       0.412   9.205 -14.971  1.00 15.68           H  
+ATOM   1540  HG2 ARG B 377      -1.824   9.650 -15.541  1.00 14.06           H  
+ATOM   1541  HG3 ARG B 377      -2.270   8.773 -14.293  1.00 14.06           H  
+ATOM   1542  HD2 ARG B 377      -1.146  11.328 -14.267  1.00 18.36           H  
+ATOM   1543  HD3 ARG B 377      -2.446  10.828 -13.503  1.00 18.36           H  
+ATOM   1544  HE  ARG B 377       0.055  10.722 -12.564  1.00 34.28           H  
+ATOM   1545 HH11 ARG B 377      -2.838   9.228 -11.934  1.00 62.79           H  
+ATOM   1546 HH12 ARG B 377      -2.573   9.026 -10.482  1.00 62.79           H  
+ATOM   1547 HH21 ARG B 377       0.359  10.525 -10.368  1.00 44.02           H  
+ATOM   1548 HH22 ARG B 377      -0.647   9.807  -9.538  1.00 44.02           H  
+ATOM   1549  N   THR B 378      -2.436   6.508 -16.485  1.00 10.11           N  
+ATOM   1550  CA  THR B 378      -3.649   5.723 -16.359  1.00 11.07           C  
+ATOM   1551  C   THR B 378      -3.458   4.320 -16.922  1.00 11.26           C  
+ATOM   1552  O   THR B 378      -2.558   4.054 -17.716  1.00 13.65           O  
+ATOM   1553  CB  THR B 378      -4.831   6.396 -17.063  1.00 10.90           C  
+ATOM   1554  OG1 THR B 378      -4.697   6.290 -18.494  1.00 11.35           O  
+ATOM   1555  CG2 THR B 378      -4.887   7.851 -16.692  1.00 11.12           C  
+ATOM   1556  H   THR B 378      -2.377   6.930 -17.232  1.00 12.13           H  
+ATOM   1557  HA  THR B 378      -3.860   5.650 -15.415  1.00 13.29           H  
+ATOM   1558  HB  THR B 378      -5.653   5.959 -16.789  1.00 13.08           H  
+ATOM   1559  HG1 THR B 378      -3.991   6.671 -18.745  1.00 13.62           H  
+ATOM   1560 HG21 THR B 378      -5.747   8.224 -16.941  1.00 13.35           H  
+ATOM   1561 HG22 THR B 378      -4.764   7.954 -15.735  1.00 13.35           H  
+ATOM   1562 HG23 THR B 378      -4.186   8.338 -17.153  1.00 13.35           H  
+ATOM   1563  N   GLY B 379      -4.335   3.414 -16.497  1.00 11.00           N  
+ATOM   1564  CA  GLY B 379      -4.271   2.037 -16.940  1.00 11.74           C  
+ATOM   1565  C   GLY B 379      -5.532   1.540 -17.609  1.00 10.33           C  
+ATOM   1566  O   GLY B 379      -5.521   0.527 -18.303  1.00 13.17           O  
+ATOM   1567  H   GLY B 379      -4.978   3.578 -15.949  1.00 13.20           H  
+ATOM   1568  HA2 GLY B 379      -3.542   1.945 -17.574  1.00 14.09           H  
+ATOM   1569  HA3 GLY B 379      -4.096   1.469 -16.174  1.00 14.09           H  
+ATOM   1570  N   VAL B 380      -6.621   2.264 -17.402  1.00 11.10           N  
+ATOM   1571  CA  VAL B 380      -7.931   1.945 -17.953  1.00 10.04           C  
+ATOM   1572  C   VAL B 380      -8.544   3.256 -18.400  1.00 10.93           C  
+ATOM   1573  O   VAL B 380      -8.411   4.266 -17.700  1.00 11.30           O  
+ATOM   1574  CB  VAL B 380      -8.846   1.276 -16.914  1.00 13.00           C  
+ATOM   1575  CG1 VAL B 380     -10.231   1.009 -17.506  1.00 13.19           C  
+ATOM   1576  CG2 VAL B 380      -8.229  -0.017 -16.372  1.00 15.49           C  
+ATOM   1577  H   VAL B 380      -6.628   2.979 -16.924  1.00 13.32           H  
+ATOM   1578  HA  VAL B 380      -7.833   1.340 -18.704  1.00 12.05           H  
+ATOM   1579  HB  VAL B 380      -8.947   1.885 -16.165  1.00 15.59           H  
+ATOM   1580 HG11 VAL B 380     -10.722   0.423 -16.908  1.00 15.82           H  
+ATOM   1581 HG12 VAL B 380     -10.701   1.852 -17.603  1.00 15.82           H  
+ATOM   1582 HG13 VAL B 380     -10.128   0.586 -18.372  1.00 15.82           H  
+ATOM   1583 HG21 VAL B 380      -8.845  -0.421 -15.741  1.00 18.59           H  
+ATOM   1584 HG22 VAL B 380      -8.067  -0.624 -17.112  1.00 18.59           H  
+ATOM   1585 HG23 VAL B 380      -7.392   0.193 -15.929  1.00 18.59           H  
+ATOM   1586  N   SER B 381      -9.192   3.260 -19.563  1.00  9.12           N  
+ATOM   1587  CA  SER B 381      -9.886   4.436 -20.068  1.00  9.33           C  
+ATOM   1588  C   SER B 381     -11.364   4.137 -20.254  1.00 11.04           C  
+ATOM   1589  O   SER B 381     -11.724   3.095 -20.817  1.00 10.97           O  
+ATOM   1590  CB  SER B 381      -9.288   4.884 -21.402  1.00 11.37           C  
+ATOM   1591  OG  SER B 381      -7.916   5.206 -21.214  1.00 10.37           O  
+ATOM   1592  H   SER B 381      -9.243   2.578 -20.085  1.00 10.94           H  
+ATOM   1593  HA  SER B 381      -9.801   5.151 -19.417  1.00 11.19           H  
+ATOM   1594  HB2 SER B 381      -9.365   4.164 -22.048  1.00 13.64           H  
+ATOM   1595  HB3 SER B 381      -9.763   5.667 -21.721  1.00 13.64           H  
+ATOM   1596  HG  SER B 381      -7.589   5.501 -21.930  1.00 12.45           H  
+ATOM   1597  N   ILE B 382     -12.212   5.061 -19.792  1.00  9.37           N  
+ATOM   1598  CA  ILE B 382     -13.662   4.962 -19.904  1.00  9.53           C  
+ATOM   1599  C   ILE B 382     -14.118   6.037 -20.888  1.00  9.34           C  
+ATOM   1600  O   ILE B 382     -13.651   7.176 -20.813  1.00 10.32           O  
+ATOM   1601  CB  ILE B 382     -14.328   5.167 -18.535  1.00  9.40           C  
+ATOM   1602  CG1 ILE B 382     -13.831   4.124 -17.518  1.00 10.52           C  
+ATOM   1603  CG2 ILE B 382     -15.814   5.145 -18.657  1.00 11.53           C  
+ATOM   1604  CD1 ILE B 382     -14.223   4.470 -16.083  1.00 13.40           C  
+ATOM   1605  H   ILE B 382     -11.956   5.781 -19.396  1.00 11.24           H  
+ATOM   1606  HA  ILE B 382     -13.916   4.090 -20.242  1.00 11.44           H  
+ATOM   1607  HB  ILE B 382     -14.072   6.043 -18.206  1.00 11.28           H  
+ATOM   1608 HG12 ILE B 382     -14.216   3.261 -17.735  1.00 12.62           H  
+ATOM   1609 HG13 ILE B 382     -12.863   4.076 -17.561  1.00 12.62           H  
+ATOM   1610 HG21 ILE B 382     -16.204   5.155 -17.768  1.00 13.84           H  
+ATOM   1611 HG22 ILE B 382     -16.102   5.927 -19.153  1.00 13.84           H  
+ATOM   1612 HG23 ILE B 382     -16.081   4.339 -19.126  1.00 13.84           H  
+ATOM   1613 HD11 ILE B 382     -13.714   3.913 -15.474  1.00 16.08           H  
+ATOM   1614 HD12 ILE B 382     -14.027   5.405 -15.919  1.00 16.08           H  
+ATOM   1615 HD13 ILE B 382     -15.172   4.305 -15.967  1.00 16.08           H  
+ATOM   1616  N   PHE B 383     -15.051   5.691 -21.777  1.00  9.27           N  
+ATOM   1617  CA  PHE B 383     -15.534   6.605 -22.818  1.00  9.46           C  
+ATOM   1618  C   PHE B 383     -17.032   6.815 -22.697  1.00  9.25           C  
+ATOM   1619  O   PHE B 383     -17.807   5.853 -22.731  1.00  9.88           O  
+ATOM   1620  CB  PHE B 383     -15.158   6.080 -24.221  1.00  9.41           C  
+ATOM   1621  CG  PHE B 383     -13.704   5.858 -24.365  1.00  8.98           C  
+ATOM   1622  CD1 PHE B 383     -13.133   4.657 -23.951  1.00  9.82           C  
+ATOM   1623  CD2 PHE B 383     -12.875   6.881 -24.784  1.00  8.93           C  
+ATOM   1624  CE1 PHE B 383     -11.785   4.488 -23.997  1.00 10.36           C  
+ATOM   1625  CE2 PHE B 383     -11.511   6.715 -24.822  1.00 11.89           C  
+ATOM   1626  CZ  PHE B 383     -10.978   5.512 -24.441  1.00 11.43           C  
+ATOM   1627  H   PHE B 383     -15.427   4.918 -21.798  1.00 11.12           H  
+ATOM   1628  HA  PHE B 383     -15.122   7.473 -22.683  1.00 11.36           H  
+ATOM   1629  HB2 PHE B 383     -15.609   5.235 -24.376  1.00 11.29           H  
+ATOM   1630  HB3 PHE B 383     -15.432   6.729 -24.887  1.00 11.29           H  
+ATOM   1631  HD1 PHE B 383     -13.676   3.967 -23.642  1.00 11.79           H  
+ATOM   1632  HD2 PHE B 383     -13.245   7.694 -25.044  1.00 10.72           H  
+ATOM   1633  HE1 PHE B 383     -11.407   3.681 -23.730  1.00 12.44           H  
+ATOM   1634  HE2 PHE B 383     -10.959   7.409 -25.102  1.00 14.27           H  
+ATOM   1635  HZ  PHE B 383     -10.058   5.386 -24.482  1.00 13.71           H  
+ATOM   1636  N   LEU B 384     -17.425   8.089 -22.593  1.00  9.16           N  
+ATOM   1637  CA  LEU B 384     -18.807   8.522 -22.442  1.00  9.50           C  
+ATOM   1638  C   LEU B 384     -19.196   9.488 -23.545  1.00 10.55           C  
+ATOM   1639  O   LEU B 384     -18.463  10.447 -23.814  1.00 10.72           O  
+ATOM   1640  CB  LEU B 384     -19.042   9.254 -21.118  1.00 11.19           C  
+ATOM   1641  CG  LEU B 384     -18.555   8.614 -19.815  1.00 11.73           C  
+ATOM   1642  CD1 LEU B 384     -18.887   9.532 -18.636  1.00 13.06           C  
+ATOM   1643  CD2 LEU B 384     -19.187   7.251 -19.632  1.00 11.93           C  
+ATOM   1644  H   LEU B 384     -16.875   8.751 -22.610  1.00 10.99           H  
+ATOM   1645  HA  LEU B 384     -19.357   7.724 -22.488  1.00 11.40           H  
+ATOM   1646  HB2 LEU B 384     -18.601  10.116 -21.181  1.00 13.43           H  
+ATOM   1647  HB3 LEU B 384     -19.999   9.378 -21.021  1.00 13.43           H  
+ATOM   1648  HG  LEU B 384     -17.593   8.492 -19.846  1.00 14.07           H  
+ATOM   1649 HD11 LEU B 384     -18.570   9.121 -17.816  1.00 15.67           H  
+ATOM   1650 HD12 LEU B 384     -18.449  10.387 -18.768  1.00 15.67           H  
+ATOM   1651 HD13 LEU B 384     -19.848   9.656 -18.593  1.00 15.67           H  
+ATOM   1652 HD21 LEU B 384     -18.894   6.877 -18.786  1.00 14.31           H  
+ATOM   1653 HD22 LEU B 384     -20.152   7.347 -19.635  1.00 14.31           H  
+ATOM   1654 HD23 LEU B 384     -18.910   6.674 -20.362  1.00 14.31           H  
+ATOM   1655  N   TYR B 385     -20.409   9.297 -24.095  1.00 10.62           N  
+ATOM   1656  CA  TYR B 385     -21.024  10.253 -25.027  1.00  9.59           C  
+ATOM   1657  C   TYR B 385     -20.055  10.532 -26.175  1.00 11.26           C  
+ATOM   1658  O   TYR B 385     -19.628   9.603 -26.871  1.00 11.43           O  
+ATOM   1659  CB  TYR B 385     -21.473  11.540 -24.300  1.00 10.84           C  
+ATOM   1660  CG  TYR B 385     -22.520  11.252 -23.243  1.00  9.42           C  
+ATOM   1661  CD1 TYR B 385     -23.818  10.904 -23.594  1.00 12.87           C  
+ATOM   1662  CD2 TYR B 385     -22.198  11.261 -21.883  1.00 10.01           C  
+ATOM   1663  CE1 TYR B 385     -24.767  10.587 -22.620  1.00 12.71           C  
+ATOM   1664  CE2 TYR B 385     -23.128  10.958 -20.920  1.00 11.71           C  
+ATOM   1665  CZ  TYR B 385     -24.414  10.595 -21.292  1.00 13.06           C  
+ATOM   1666  OH  TYR B 385     -25.333  10.298 -20.316  1.00 15.91           O  
+ATOM   1667  H   TYR B 385     -20.902   8.610 -23.941  1.00 12.74           H  
+ATOM   1668  HA  TYR B 385     -21.834   9.879 -25.407  1.00 11.51           H  
+ATOM   1669  HB2 TYR B 385     -20.706  11.947 -23.867  1.00 13.01           H  
+ATOM   1670  HB3 TYR B 385     -21.854  12.156 -24.946  1.00 13.01           H  
+ATOM   1671  HD1 TYR B 385     -24.059  10.883 -24.492  1.00 15.44           H  
+ATOM   1672  HD2 TYR B 385     -21.331  11.478 -21.624  1.00 12.02           H  
+ATOM   1673  HE1 TYR B 385     -25.637  10.370 -22.869  1.00 15.25           H  
+ATOM   1674  HE2 TYR B 385     -22.897  10.996 -20.020  1.00 14.05           H  
+ATOM   1675  HH  TYR B 385     -24.988  10.399 -19.557  1.00 19.09           H  
+ATOM   1676  N   GLY B 386     -19.716  11.801 -26.402  1.00 10.12           N  
+ATOM   1677  CA  GLY B 386     -18.759  12.176 -27.416  1.00  9.60           C  
+ATOM   1678  C   GLY B 386     -19.412  12.863 -28.593  1.00 10.95           C  
+ATOM   1679  O   GLY B 386     -19.541  12.295 -29.683  1.00 10.73           O  
+ATOM   1680  H   GLY B 386     -20.038  12.470 -25.969  1.00 12.15           H  
+ATOM   1681  HA2 GLY B 386     -18.104  12.780 -27.032  1.00 11.52           H  
+ATOM   1682  HA3 GLY B 386     -18.304  11.382 -27.738  1.00 11.52           H  
+ATOM   1683  N   ASN B 387     -19.859  14.092 -28.367  1.00 10.38           N  
+ATOM   1684  CA  ASN B 387     -20.443  14.902 -29.426  1.00 12.47           C  
+ATOM   1685  C   ASN B 387     -20.149  16.365 -29.125  1.00 11.63           C  
+ATOM   1686  O   ASN B 387     -19.913  16.751 -27.973  1.00 11.09           O  
+ATOM   1687  CB  ASN B 387     -21.943  14.634 -29.581  1.00 12.05           C  
+ATOM   1688  CG  ASN B 387     -22.745  15.041 -28.369  1.00 12.81           C  
+ATOM   1689  OD1 ASN B 387     -23.012  16.218 -28.180  1.00 13.57           O  
+ATOM   1690  ND2 ASN B 387     -23.135  14.075 -27.560  1.00 13.12           N  
+ATOM   1691  H   ASN B 387     -19.835  14.482 -27.601  1.00 12.45           H  
+ATOM   1692  HA  ASN B 387     -20.032  14.691 -30.278  1.00 14.96           H  
+ATOM   1693  HB2 ASN B 387     -22.276  15.136 -30.341  1.00 14.46           H  
+ATOM   1694  HB3 ASN B 387     -22.080  13.684 -29.724  1.00 14.46           H  
+ATOM   1695 HD21 ASN B 387     -23.595  14.262 -26.857  1.00 15.74           H  
+ATOM   1696 HD22 ASN B 387     -22.930  13.258 -27.735  1.00 15.74           H  
+ATOM   1697  N   LYS B 388     -20.150  17.161 -30.193  1.00 11.77           N  
+ATOM   1698  CA  LYS B 388     -19.735  18.556 -30.133  1.00 11.89           C  
+ATOM   1699  C   LYS B 388     -20.374  19.290 -31.303  1.00 14.02           C  
+ATOM   1700  O   LYS B 388     -20.907  18.680 -32.230  1.00 12.97           O  
+ATOM   1701  CB  LYS B 388     -18.218  18.703 -30.196  1.00 14.08           C  
+ATOM   1702  CG  LYS B 388     -17.695  18.348 -31.573  1.00 14.49           C  
+ATOM   1703  CD  LYS B 388     -16.215  18.126 -31.603  1.00 23.30           C  
+ATOM   1704  CE  LYS B 388     -15.445  19.397 -31.548  1.00 29.05           C  
+ATOM   1705  NZ  LYS B 388     -14.100  19.162 -32.174  1.00 33.53           N  
+ATOM   1706  H   LYS B 388     -20.391  16.909 -30.979  1.00 14.13           H  
+ATOM   1707  HA  LYS B 388     -20.049  18.938 -29.299  1.00 14.27           H  
+ATOM   1708  HB2 LYS B 388     -17.975  19.621 -30.001  1.00 16.89           H  
+ATOM   1709  HB3 LYS B 388     -17.810  18.107 -29.549  1.00 16.89           H  
+ATOM   1710  HG2 LYS B 388     -18.125  17.532 -31.873  1.00 17.38           H  
+ATOM   1711  HG3 LYS B 388     -17.899  19.074 -32.184  1.00 17.38           H  
+ATOM   1712  HD2 LYS B 388     -15.960  17.587 -30.837  1.00 27.96           H  
+ATOM   1713  HD3 LYS B 388     -15.980  17.667 -32.424  1.00 27.96           H  
+ATOM   1714  HE2 LYS B 388     -15.910  20.089 -32.043  1.00 34.86           H  
+ATOM   1715  HE3 LYS B 388     -15.324  19.673 -30.626  1.00 34.86           H  
+ATOM   1716  HZ1 LYS B 388     -13.674  18.509 -31.745  1.00 40.23           H  
+ATOM   1717  HZ2 LYS B 388     -14.197  18.932 -33.028  1.00 40.23           H  
+ATOM   1718  HZ3 LYS B 388     -13.610  19.904 -32.128  1.00 40.23           H  
+ATOM   1719  N   ILE B 389     -20.311  20.615 -31.242  1.00 13.90           N  
+ATOM   1720  CA  ILE B 389     -20.753  21.428 -32.372  1.00 14.67           C  
+ATOM   1721  C   ILE B 389     -19.621  21.573 -33.373  1.00 18.39           C  
+ATOM   1722  O   ILE B 389     -18.489  21.935 -33.026  1.00 19.88           O  
+ATOM   1723  CB  ILE B 389     -21.232  22.812 -31.902  1.00 17.89           C  
+ATOM   1724  CG1 ILE B 389     -22.419  22.706 -30.956  1.00 20.00           C  
+ATOM   1725  CG2 ILE B 389     -21.565  23.696 -33.138  1.00 16.78           C  
+ATOM   1726  CD1 ILE B 389     -23.610  21.969 -31.502  1.00 23.67           C  
+ATOM   1727  H   ILE B 389     -20.021  21.063 -30.568  1.00 16.68           H  
+ATOM   1728  HA  ILE B 389     -21.491  20.970 -32.804  1.00 17.60           H  
+ATOM   1729  HB  ILE B 389     -20.515  23.230 -31.400  1.00 21.47           H  
+ATOM   1730 HG12 ILE B 389     -22.132  22.240 -30.155  1.00 24.00           H  
+ATOM   1731 HG13 ILE B 389     -22.712  23.603 -30.731  1.00 24.00           H  
+ATOM   1732 HG21 ILE B 389     -22.103  24.451 -32.851  1.00 20.14           H  
+ATOM   1733 HG22 ILE B 389     -20.738  24.011 -33.533  1.00 20.14           H  
+ATOM   1734 HG23 ILE B 389     -22.058  23.165 -33.783  1.00 20.14           H  
+ATOM   1735 HD11 ILE B 389     -24.361  22.090 -30.900  1.00 28.40           H  
+ATOM   1736 HD12 ILE B 389     -23.828  22.325 -32.378  1.00 28.40           H  
+ATOM   1737 HD13 ILE B 389     -23.393  21.026 -31.574  1.00 28.40           H  
+ATOM   1738  N   ASP B 390     -19.928  21.307 -34.632  1.00 16.19           N  
+ATOM   1739  CA  ASP B 390     -19.017  21.604 -35.726  1.00 17.74           C  
+ATOM   1740  C   ASP B 390     -19.868  22.044 -36.905  1.00 17.99           C  
+ATOM   1741  O   ASP B 390     -20.840  21.371 -37.253  1.00 17.18           O  
+ATOM   1742  CB  ASP B 390     -18.153  20.400 -36.086  1.00 19.65           C  
+ATOM   1743  CG  ASP B 390     -17.101  20.743 -37.125  1.00 29.26           C  
+ATOM   1744  OD1 ASP B 390     -16.383  21.741 -36.911  1.00 31.81           O  
+ATOM   1745  OD2 ASP B 390     -17.011  20.029 -38.147  1.00 35.73           O  
+ATOM   1746  H   ASP B 390     -20.669  20.950 -34.884  1.00 19.43           H  
+ATOM   1747  HA  ASP B 390     -18.408  22.319 -35.485  1.00 21.29           H  
+ATOM   1748  HB2 ASP B 390     -17.699  20.083 -35.289  1.00 23.58           H  
+ATOM   1749  HB3 ASP B 390     -18.718  19.699 -36.447  1.00 23.58           H  
+ATOM   1750  N   LYS B 391     -19.508  23.179 -37.498  1.00 19.08           N  
+ATOM   1751  CA  LYS B 391     -20.238  23.705 -38.657  1.00 22.16           C  
+ATOM   1752  C   LYS B 391     -21.737  23.778 -38.369  1.00 17.56           C  
+ATOM   1753  O   LYS B 391     -22.577  23.390 -39.182  1.00 17.20           O  
+ATOM   1754  CB  LYS B 391     -19.957  22.867 -39.901  1.00 26.06           C  
+ATOM   1755  CG  LYS B 391     -18.509  22.893 -40.334  1.00 31.30           C  
+ATOM   1756  CD  LYS B 391     -18.264  22.007 -41.545  1.00 41.02           C  
+ATOM   1757  CE  LYS B 391     -16.894  22.278 -42.159  1.00 53.61           C  
+ATOM   1758  NZ  LYS B 391     -16.336  21.089 -42.871  1.00 62.52           N  
+ATOM   1759  H   LYS B 391     -18.844  23.667 -37.250  1.00 22.90           H  
+ATOM   1760  HA  LYS B 391     -19.931  24.608 -38.833  1.00 26.59           H  
+ATOM   1761  HB2 LYS B 391     -20.195  21.945 -39.718  1.00 31.28           H  
+ATOM   1762  HB3 LYS B 391     -20.492  23.209 -40.635  1.00 31.28           H  
+ATOM   1763  HG2 LYS B 391     -18.261  23.801 -40.567  1.00 37.56           H  
+ATOM   1764  HG3 LYS B 391     -17.952  22.574 -39.606  1.00 37.56           H  
+ATOM   1765  HD2 LYS B 391     -18.300  21.075 -41.276  1.00 49.22           H  
+ATOM   1766  HD3 LYS B 391     -18.941  22.184 -42.217  1.00 49.22           H  
+ATOM   1767  HE2 LYS B 391     -16.972  23.002 -42.800  1.00 64.33           H  
+ATOM   1768  HE3 LYS B 391     -16.274  22.523 -41.455  1.00 64.33           H  
+ATOM   1769  HZ1 LYS B 391     -15.541  21.287 -43.217  1.00 75.03           H  
+ATOM   1770  HZ2 LYS B 391     -16.244  20.410 -42.303  1.00 75.03           H  
+ATOM   1771  HZ3 LYS B 391     -16.884  20.843 -43.528  1.00 75.03           H  
+ATOM   1772  N   GLY B 392     -22.066  24.264 -37.177  1.00 15.21           N  
+ATOM   1773  CA  GLY B 392     -23.436  24.512 -36.788  1.00 16.42           C  
+ATOM   1774  C   GLY B 392     -24.232  23.279 -36.443  1.00 14.61           C  
+ATOM   1775  O   GLY B 392     -25.426  23.390 -36.176  1.00 15.00           O  
+ATOM   1776  H   GLY B 392     -21.495  24.461 -36.564  1.00 18.26           H  
+ATOM   1777  HA2 GLY B 392     -23.437  25.092 -36.010  1.00 19.70           H  
+ATOM   1778  HA3 GLY B 392     -23.889  24.962 -37.518  1.00 19.70           H  
+ATOM   1779  N   GLN B 393     -23.601  22.105 -36.399  1.00 13.42           N  
+ATOM   1780  CA  GLN B 393     -24.322  20.856 -36.241  1.00 14.99           C  
+ATOM   1781  C   GLN B 393     -23.735  20.064 -35.088  1.00 12.88           C  
+ATOM   1782  O   GLN B 393     -22.545  20.191 -34.784  1.00 15.61           O  
+ATOM   1783  CB  GLN B 393     -24.246  19.982 -37.495  1.00 17.64           C  
+ATOM   1784  CG  GLN B 393     -24.701  20.701 -38.757  1.00 22.07           C  
+ATOM   1785  CD  GLN B 393     -24.040  20.178 -40.013  1.00 33.32           C  
+ATOM   1786  OE1 GLN B 393     -24.250  19.029 -40.413  1.00 37.21           O  
+ATOM   1787  NE2 GLN B 393     -23.219  21.017 -40.636  1.00 29.50           N  
+ATOM   1788  H   GLN B 393     -22.748  22.012 -36.461  1.00 16.10           H  
+ATOM   1789  HA  GLN B 393     -25.250  21.064 -36.054  1.00 17.98           H  
+ATOM   1790  HB2 GLN B 393     -23.326  19.702 -37.626  1.00 21.17           H  
+ATOM   1791  HB3 GLN B 393     -24.815  19.207 -37.371  1.00 21.17           H  
+ATOM   1792  HG2 GLN B 393     -25.659  20.587 -38.855  1.00 26.49           H  
+ATOM   1793  HG3 GLN B 393     -24.486  21.643 -38.677  1.00 26.49           H  
+ATOM   1794 HE21 GLN B 393     -22.817  20.770 -41.355  1.00 35.40           H  
+ATOM   1795 HE22 GLN B 393     -23.090  21.806 -40.321  1.00 35.40           H  
+ATOM   1796  N   VAL B 394     -24.568  19.214 -34.493  1.00 13.57           N  
+ATOM   1797  CA  VAL B 394     -24.079  18.267 -33.487  1.00 12.46           C  
+ATOM   1798  C   VAL B 394     -23.472  17.085 -34.230  1.00 14.00           C  
+ATOM   1799  O   VAL B 394     -24.135  16.456 -35.070  1.00 16.97           O  
+ATOM   1800  CB  VAL B 394     -25.197  17.814 -32.548  1.00 15.01           C  
+ATOM   1801  CG1 VAL B 394     -24.674  16.717 -31.586  1.00 16.38           C  
+ATOM   1802  CG2 VAL B 394     -25.747  18.976 -31.748  1.00 17.90           C  
+ATOM   1803  H   VAL B 394     -25.411  19.164 -34.652  1.00 16.29           H  
+ATOM   1804  HA  VAL B 394     -23.397  18.692 -32.943  1.00 14.95           H  
+ATOM   1805  HB  VAL B 394     -25.918  17.450 -33.086  1.00 18.02           H  
+ATOM   1806 HG11 VAL B 394     -25.320  16.586 -30.874  1.00 19.66           H  
+ATOM   1807 HG12 VAL B 394     -24.557  15.891 -32.082  1.00 19.66           H  
+ATOM   1808 HG13 VAL B 394     -23.824  17.002 -31.214  1.00 19.66           H  
+ATOM   1809 HG21 VAL B 394     -26.452  18.653 -31.165  1.00 21.48           H  
+ATOM   1810 HG22 VAL B 394     -25.031  19.363 -31.220  1.00 21.48           H  
+ATOM   1811 HG23 VAL B 394     -26.103  19.640 -32.360  1.00 21.48           H  
+ATOM   1812  N   VAL B 395     -22.188  16.819 -33.969  1.00 12.72           N  
+ATOM   1813  CA  VAL B 395     -21.438  15.787 -34.666  1.00 12.88           C  
+ATOM   1814  C   VAL B 395     -20.726  14.922 -33.632  1.00 10.15           C  
+ATOM   1815  O   VAL B 395     -20.537  15.321 -32.484  1.00 11.98           O  
+ATOM   1816  CB  VAL B 395     -20.405  16.360 -35.651  1.00 13.64           C  
+ATOM   1817  CG1 VAL B 395     -21.124  17.242 -36.668  1.00 16.04           C  
+ATOM   1818  CG2 VAL B 395     -19.321  17.148 -34.928  1.00 15.89           C  
+ATOM   1819  H   VAL B 395     -21.725  17.236 -33.377  1.00 15.26           H  
+ATOM   1820  HA  VAL B 395     -22.063  15.238 -35.166  1.00 15.45           H  
+ATOM   1821  HB  VAL B 395     -19.963  15.629 -36.110  1.00 16.37           H  
+ATOM   1822 HG11 VAL B 395     -20.484  17.549 -37.329  1.00 19.25           H  
+ATOM   1823 HG12 VAL B 395     -21.821  16.722 -37.099  1.00 19.25           H  
+ATOM   1824 HG13 VAL B 395     -21.515  18.001 -36.208  1.00 19.25           H  
+ATOM   1825 HG21 VAL B 395     -18.786  17.623 -35.584  1.00 19.07           H  
+ATOM   1826 HG22 VAL B 395     -19.740  17.780 -34.323  1.00 19.07           H  
+ATOM   1827 HG23 VAL B 395     -18.762  16.532 -34.429  1.00 19.07           H  
+ATOM   1828  N   LYS B 396     -20.306  13.734 -34.061  1.00 12.61           N  
+ATOM   1829  CA  LYS B 396     -19.526  12.883 -33.169  1.00 13.78           C  
+ATOM   1830  C   LYS B 396     -18.160  13.511 -32.922  1.00 13.51           C  
+ATOM   1831  O   LYS B 396     -17.563  14.128 -33.807  1.00 16.29           O  
+ATOM   1832  CB  LYS B 396     -19.407  11.480 -33.741  1.00 15.62           C  
+ATOM   1833  CG  LYS B 396     -20.692  10.719 -33.590  1.00 16.70           C  
+ATOM   1834  CD  LYS B 396     -20.568   9.332 -34.198  1.00 29.48           C  
+ATOM   1835  CE  LYS B 396     -21.826   8.915 -34.921  1.00 31.47           C  
+ATOM   1836  NZ  LYS B 396     -21.601   7.637 -35.633  1.00 27.85           N  
+ATOM   1837  H   LYS B 396     -20.456  13.407 -34.842  1.00 15.13           H  
+ATOM   1838  HA  LYS B 396     -19.969  12.794 -32.311  1.00 16.53           H  
+ATOM   1839  HB2 LYS B 396     -19.192  11.535 -34.685  1.00 18.75           H  
+ATOM   1840  HB3 LYS B 396     -18.709  10.999 -33.270  1.00 18.75           H  
+ATOM   1841  HG2 LYS B 396     -20.905  10.625 -32.648  1.00 20.04           H  
+ATOM   1842  HG3 LYS B 396     -21.405  11.193 -34.046  1.00 20.04           H  
+ATOM   1843  HD2 LYS B 396     -19.837   9.327 -34.835  1.00 35.38           H  
+ATOM   1844  HD3 LYS B 396     -20.398   8.688 -33.493  1.00 35.38           H  
+ATOM   1845  HE2 LYS B 396     -22.545   8.793 -34.282  1.00 37.77           H  
+ATOM   1846  HE3 LYS B 396     -22.070   9.594 -35.569  1.00 37.77           H  
+ATOM   1847  HZ1 LYS B 396     -20.928   7.724 -36.209  1.00 33.42           H  
+ATOM   1848  HZ2 LYS B 396     -21.401   6.995 -35.050  1.00 33.42           H  
+ATOM   1849  HZ3 LYS B 396     -22.335   7.404 -36.080  1.00 33.42           H  
+ATOM   1850  N   ALA B 397     -17.660  13.353 -31.704  1.00 10.90           N  
+ATOM   1851  CA  ALA B 397     -16.481  14.077 -31.239  1.00 12.46           C  
+ATOM   1852  C   ALA B 397     -15.195  13.305 -31.534  1.00 12.97           C  
+ATOM   1853  O   ALA B 397     -14.867  12.323 -30.843  1.00 12.96           O  
+ATOM   1854  CB  ALA B 397     -16.612  14.345 -29.736  1.00 15.14           C  
+ATOM   1855  H   ALA B 397     -17.991  12.822 -31.115  1.00 13.08           H  
+ATOM   1856  HA  ALA B 397     -16.422  14.910 -31.733  1.00 14.95           H  
+ATOM   1857  HB1 ALA B 397     -15.821  14.814 -29.429  1.00 18.16           H  
+ATOM   1858  HB2 ALA B 397     -17.401  14.888 -29.580  1.00 18.16           H  
+ATOM   1859  HB3 ALA B 397     -16.696  13.498 -29.271  1.00 18.16           H  
+ATOM   1860  N   LYS B 398     -14.439  13.801 -32.507  1.00 11.48           N  
+ATOM   1861  CA  LYS B 398     -13.236  13.091 -32.949  1.00 13.73           C  
+ATOM   1862  C   LYS B 398     -12.169  13.036 -31.870  1.00 13.81           C  
+ATOM   1863  O   LYS B 398     -11.333  12.123 -31.876  1.00 12.51           O  
+ATOM   1864  CB  LYS B 398     -12.664  13.751 -34.201  1.00 20.97           C  
+ATOM   1865  CG  LYS B 398     -13.581  13.657 -35.416  1.00 33.50           C  
+ATOM   1866  CD  LYS B 398     -13.964  12.221 -35.768  1.00 40.81           C  
+ATOM   1867  CE  LYS B 398     -14.912  12.192 -36.977  1.00 54.13           C  
+ATOM   1868  NZ  LYS B 398     -15.368  10.816 -37.330  1.00 53.66           N  
+ATOM   1869  H   LYS B 398     -14.594  14.536 -32.925  1.00 13.78           H  
+ATOM   1870  HA  LYS B 398     -13.490  12.180 -33.167  1.00 16.47           H  
+ATOM   1871  HB2 LYS B 398     -12.512  14.691 -34.016  1.00 25.17           H  
+ATOM   1872  HB3 LYS B 398     -11.826  13.318 -34.427  1.00 25.17           H  
+ATOM   1873  HG2 LYS B 398     -14.398  14.147 -35.234  1.00 40.20           H  
+ATOM   1874  HG3 LYS B 398     -13.129  14.041 -36.183  1.00 40.20           H  
+ATOM   1875  HD2 LYS B 398     -13.165  11.717 -35.991  1.00 48.97           H  
+ATOM   1876  HD3 LYS B 398     -14.415  11.811 -35.014  1.00 48.97           H  
+ATOM   1877  HE2 LYS B 398     -15.697  12.725 -36.775  1.00 64.95           H  
+ATOM   1878  HE3 LYS B 398     -14.451  12.561 -37.747  1.00 64.95           H  
+ATOM   1879  HZ1 LYS B 398     -15.925  10.849 -38.024  1.00 64.39           H  
+ATOM   1880  HZ2 LYS B 398     -14.669  10.309 -37.544  1.00 64.39           H  
+ATOM   1881  HZ3 LYS B 398     -15.791  10.449 -36.639  1.00 64.39           H  
+ATOM   1882  N   GLY B 399     -12.173  13.991 -30.938  1.00 12.22           N  
+ATOM   1883  CA  GLY B 399     -11.211  13.976 -29.840  1.00 10.20           C  
+ATOM   1884  C   GLY B 399     -11.355  12.773 -28.938  1.00 11.44           C  
+ATOM   1885  O   GLY B 399     -10.365  12.277 -28.401  1.00 11.60           O  
+ATOM   1886  H   GLY B 399     -12.719  14.655 -30.919  1.00 14.66           H  
+ATOM   1887  HA2 GLY B 399     -10.312  13.973 -30.206  1.00 12.24           H  
+ATOM   1888  HA3 GLY B 399     -11.331  14.774 -29.302  1.00 12.24           H  
+ATOM   1889  N   VAL B 400     -12.586  12.294 -28.742  1.00 10.65           N  
+ATOM   1890  CA  VAL B 400     -12.803  11.074 -27.962  1.00 10.33           C  
+ATOM   1891  C   VAL B 400     -12.243   9.865 -28.703  1.00 10.26           C  
+ATOM   1892  O   VAL B 400     -11.623   8.988 -28.088  1.00 11.34           O  
+ATOM   1893  CB  VAL B 400     -14.297  10.924 -27.639  1.00 10.01           C  
+ATOM   1894  CG1 VAL B 400     -14.590   9.644 -26.914  1.00 10.29           C  
+ATOM   1895  CG2 VAL B 400     -14.745  12.134 -26.822  1.00 12.11           C  
+ATOM   1896  H   VAL B 400     -13.306  12.653 -29.046  1.00 12.77           H  
+ATOM   1897  HA  VAL B 400     -12.325  11.142 -27.121  1.00 12.40           H  
+ATOM   1898  HB  VAL B 400     -14.801  10.887 -28.467  1.00 12.01           H  
+ATOM   1899 HG11 VAL B 400     -15.509   9.660 -26.602  1.00 12.34           H  
+ATOM   1900 HG12 VAL B 400     -14.460   8.899 -27.522  1.00 12.34           H  
+ATOM   1901 HG13 VAL B 400     -13.986   9.563 -26.159  1.00 12.34           H  
+ATOM   1902 HG21 VAL B 400     -15.662  11.998 -26.534  1.00 14.54           H  
+ATOM   1903 HG22 VAL B 400     -14.166  12.225 -26.049  1.00 14.54           H  
+ATOM   1904 HG23 VAL B 400     -14.686  12.928 -27.375  1.00 14.54           H  
+ATOM   1905  N   GLN B 401     -12.451   9.801 -30.024  1.00 11.93           N  
+ATOM   1906  CA  GLN B 401     -11.818   8.766 -30.844  1.00 12.70           C  
+ATOM   1907  C   GLN B 401     -10.295   8.815 -30.722  1.00 11.39           C  
+ATOM   1908  O   GLN B 401      -9.645   7.776 -30.588  1.00 11.27           O  
+ATOM   1909  CB  GLN B 401     -12.270   8.943 -32.298  1.00 13.47           C  
+ATOM   1910  CG  GLN B 401     -11.557   8.077 -33.316  1.00 19.39           C  
+ATOM   1911  CD  GLN B 401     -12.253   6.787 -33.550  1.00 38.62           C  
+ATOM   1912  OE1 GLN B 401     -11.815   5.742 -33.061  1.00 46.02           O  
+ATOM   1913  NE2 GLN B 401     -13.347   6.831 -34.305  1.00 41.52           N  
+ATOM   1914  H   GLN B 401     -12.951  10.342 -30.466  1.00 14.32           H  
+ATOM   1915  HA  GLN B 401     -12.097   7.888 -30.542  1.00 15.24           H  
+ATOM   1916  HB2 GLN B 401     -13.215   8.730 -32.350  1.00 16.16           H  
+ATOM   1917  HB3 GLN B 401     -12.123   9.867 -32.552  1.00 16.16           H  
+ATOM   1918  HG2 GLN B 401     -11.512   8.553 -34.161  1.00 23.26           H  
+ATOM   1919  HG3 GLN B 401     -10.662   7.883 -32.997  1.00 23.26           H  
+ATOM   1920 HE21 GLN B 401     -13.616   7.581 -34.629  1.00 49.82           H  
+ATOM   1921 HE22 GLN B 401     -13.786   6.110 -34.469  1.00 49.82           H  
+ATOM   1922  N   SER B 402      -9.711  10.015 -30.778  1.00 10.75           N  
+ATOM   1923  CA  SER B 402      -8.265  10.138 -30.626  1.00  9.90           C  
+ATOM   1924  C   SER B 402      -7.815   9.620 -29.263  1.00 10.87           C  
+ATOM   1925  O   SER B 402      -6.783   8.944 -29.148  1.00 12.57           O  
+ATOM   1926  CB  SER B 402      -7.831  11.583 -30.787  1.00 12.28           C  
+ATOM   1927  OG  SER B 402      -8.186  12.121 -32.051  1.00 16.50           O  
+ATOM   1928  H   SER B 402     -10.124  10.759 -30.901  1.00 12.91           H  
+ATOM   1929  HA  SER B 402      -7.840   9.613 -31.322  1.00 11.88           H  
+ATOM   1930  HB2 SER B 402      -8.259  12.113 -30.095  1.00 14.74           H  
+ATOM   1931  HB3 SER B 402      -6.867  11.629 -30.691  1.00 14.74           H  
+ATOM   1932  HG  SER B 402      -7.828  11.672 -32.665  1.00 19.80           H  
+ATOM   1933  N   GLU B 403      -8.576   9.930 -28.209  1.00  9.95           N  
+ATOM   1934  CA  GLU B 403      -8.215   9.451 -26.879  1.00 10.56           C  
+ATOM   1935  C   GLU B 403      -8.368   7.937 -26.754  1.00  9.14           C  
+ATOM   1936  O   GLU B 403      -7.584   7.305 -26.034  1.00 10.27           O  
+ATOM   1937  CB  GLU B 403      -9.048  10.181 -25.815  1.00 11.25           C  
+ATOM   1938  CG  GLU B 403      -8.627  11.644 -25.726  1.00 11.73           C  
+ATOM   1939  CD  GLU B 403      -9.557  12.553 -24.959  1.00  9.82           C  
+ATOM   1940  OE1 GLU B 403     -10.614  12.105 -24.443  1.00  9.99           O  
+ATOM   1941  OE2 GLU B 403      -9.194  13.753 -24.871  1.00 11.00           O  
+ATOM   1942  H   GLU B 403      -9.290  10.407 -28.238  1.00 11.94           H  
+ATOM   1943  HA  GLU B 403      -7.281   9.656 -26.714  1.00 12.67           H  
+ATOM   1944  HB2 GLU B 403      -9.987  10.143 -26.054  1.00 13.50           H  
+ATOM   1945  HB3 GLU B 403      -8.909   9.765 -24.950  1.00 13.50           H  
+ATOM   1946  HG2 GLU B 403      -7.762  11.685 -25.289  1.00 14.08           H  
+ATOM   1947  HG3 GLU B 403      -8.561  11.997 -26.627  1.00 14.08           H  
+ATOM   1948  N   PHE B 404      -9.339   7.340 -27.455  1.00 10.77           N  
+ATOM   1949  CA  PHE B 404      -9.411   5.883 -27.541  1.00 10.22           C  
+ATOM   1950  C   PHE B 404      -8.158   5.298 -28.192  1.00 10.92           C  
+ATOM   1951  O   PHE B 404      -7.563   4.338 -27.684  1.00 11.59           O  
+ATOM   1952  CB  PHE B 404     -10.669   5.491 -28.314  1.00 11.41           C  
+ATOM   1953  CG  PHE B 404     -10.866   4.010 -28.497  1.00 11.40           C  
+ATOM   1954  CD1 PHE B 404     -11.595   3.291 -27.575  1.00 13.61           C  
+ATOM   1955  CD2 PHE B 404     -10.361   3.369 -29.611  1.00 15.17           C  
+ATOM   1956  CE1 PHE B 404     -11.822   1.937 -27.757  1.00 15.17           C  
+ATOM   1957  CE2 PHE B 404     -10.556   1.998 -29.778  1.00 16.74           C  
+ATOM   1958  CZ  PHE B 404     -11.292   1.294 -28.848  1.00 18.00           C  
+ATOM   1959  H   PHE B 404      -9.960   7.753 -27.883  1.00 12.93           H  
+ATOM   1960  HA  PHE B 404      -9.468   5.509 -26.648  1.00 12.27           H  
+ATOM   1961  HB2 PHE B 404     -11.442   5.831 -27.835  1.00 13.69           H  
+ATOM   1962  HB3 PHE B 404     -10.625   5.891 -29.197  1.00 13.69           H  
+ATOM   1963  HD1 PHE B 404     -11.937   3.718 -26.824  1.00 16.33           H  
+ATOM   1964  HD2 PHE B 404      -9.890   3.852 -30.251  1.00 18.20           H  
+ATOM   1965  HE1 PHE B 404     -12.333   1.464 -27.141  1.00 18.20           H  
+ATOM   1966  HE2 PHE B 404     -10.192   1.560 -30.513  1.00 20.09           H  
+ATOM   1967  HZ  PHE B 404     -11.429   0.381 -28.960  1.00 21.60           H  
+ATOM   1968  N   ASN B 405      -7.743   5.862 -29.315  1.00 11.75           N  
+ATOM   1969  CA  ASN B 405      -6.576   5.322 -30.002  1.00 11.10           C  
+ATOM   1970  C   ASN B 405      -5.319   5.469 -29.164  1.00 11.23           C  
+ATOM   1971  O   ASN B 405      -4.504   4.538 -29.087  1.00 11.71           O  
+ATOM   1972  CB  ASN B 405      -6.439   6.009 -31.350  1.00 12.79           C  
+ATOM   1973  CG  ASN B 405      -7.388   5.450 -32.359  1.00 17.43           C  
+ATOM   1974  OD1 ASN B 405      -7.822   4.292 -32.243  1.00 18.18           O  
+ATOM   1975  ND2 ASN B 405      -7.731   6.261 -33.357  1.00 17.77           N  
+ATOM   1976  H   ASN B 405      -8.109   6.542 -29.694  1.00 14.10           H  
+ATOM   1977  HA  ASN B 405      -6.695   4.372 -30.158  1.00 13.32           H  
+ATOM   1978  HB2 ASN B 405      -6.628   6.955 -31.248  1.00 15.35           H  
+ATOM   1979  HB3 ASN B 405      -5.536   5.886 -31.682  1.00 15.35           H  
+ATOM   1980 HD21 ASN B 405      -8.275   5.989 -33.965  1.00 21.32           H  
+ATOM   1981 HD22 ASN B 405      -7.409   7.058 -33.394  1.00 21.32           H  
+ATOM   1982  N   ILE B 406      -5.152   6.613 -28.503  1.00 11.13           N  
+ATOM   1983  CA  ILE B 406      -3.991   6.790 -27.633  1.00 11.33           C  
+ATOM   1984  C   ILE B 406      -4.032   5.771 -26.509  1.00 12.69           C  
+ATOM   1985  O   ILE B 406      -3.012   5.166 -26.159  1.00 12.08           O  
+ATOM   1986  CB  ILE B 406      -3.945   8.232 -27.088  1.00 10.76           C  
+ATOM   1987  CG1 ILE B 406      -3.612   9.210 -28.224  1.00 12.32           C  
+ATOM   1988  CG2 ILE B 406      -2.932   8.358 -25.966  1.00 11.05           C  
+ATOM   1989  CD1 ILE B 406      -3.918  10.676 -27.953  1.00 10.77           C  
+ATOM   1990  H   ILE B 406      -5.684   7.287 -28.539  1.00 13.35           H  
+ATOM   1991  HA  ILE B 406      -3.185   6.644 -28.152  1.00 13.60           H  
+ATOM   1992  HB  ILE B 406      -4.819   8.450 -26.728  1.00 12.91           H  
+ATOM   1993 HG12 ILE B 406      -2.662   9.145 -28.411  1.00 14.78           H  
+ATOM   1994 HG13 ILE B 406      -4.123   8.951 -29.007  1.00 14.78           H  
+ATOM   1995 HG21 ILE B 406      -2.752   9.298 -25.807  1.00 13.27           H  
+ATOM   1996 HG22 ILE B 406      -3.296   7.950 -25.165  1.00 13.27           H  
+ATOM   1997 HG23 ILE B 406      -2.115   7.904 -26.226  1.00 13.27           H  
+ATOM   1998 HD11 ILE B 406      -3.713  11.193 -28.747  1.00 12.93           H  
+ATOM   1999 HD12 ILE B 406      -4.858  10.766 -27.732  1.00 12.93           H  
+ATOM   2000 HD13 ILE B 406      -3.373  10.980 -27.210  1.00 12.93           H  
+ATOM   2001  N   SER B 407      -5.219   5.563 -25.927  1.00 10.39           N  
+ATOM   2002  CA  SER B 407      -5.350   4.600 -24.839  1.00 10.93           C  
+ATOM   2003  C   SER B 407      -4.922   3.211 -25.292  1.00  9.99           C  
+ATOM   2004  O   SER B 407      -4.164   2.528 -24.596  1.00 11.31           O  
+ATOM   2005  CB  SER B 407      -6.791   4.566 -24.330  1.00  9.99           C  
+ATOM   2006  OG  SER B 407      -7.137   5.806 -23.732  1.00 11.83           O  
+ATOM   2007  H   SER B 407      -5.950   5.961 -26.142  1.00 12.47           H  
+ATOM   2008  HA  SER B 407      -4.778   4.881 -24.108  1.00 13.12           H  
+ATOM   2009  HB2 SER B 407      -7.387   4.396 -25.076  1.00 11.99           H  
+ATOM   2010  HB3 SER B 407      -6.876   3.861 -23.669  1.00 11.99           H  
+ATOM   2011  HG  SER B 407      -7.060   6.426 -24.293  1.00 14.20           H  
+ATOM   2012  N   PHE B 408      -5.397   2.793 -26.467  1.00 12.43           N  
+ATOM   2013  CA  PHE B 408      -5.033   1.482 -26.988  1.00 12.34           C  
+ATOM   2014  C   PHE B 408      -3.537   1.396 -27.259  1.00 11.72           C  
+ATOM   2015  O   PHE B 408      -2.886   0.389 -26.924  1.00 12.23           O  
+ATOM   2016  CB  PHE B 408      -5.815   1.198 -28.267  1.00 14.31           C  
+ATOM   2017  CG  PHE B 408      -5.555  -0.161 -28.835  1.00 19.68           C  
+ATOM   2018  CD1 PHE B 408      -6.218  -1.272 -28.334  1.00 23.92           C  
+ATOM   2019  CD2 PHE B 408      -4.628  -0.328 -29.840  1.00 21.92           C  
+ATOM   2020  CE1 PHE B 408      -5.986  -2.532 -28.859  1.00 26.55           C  
+ATOM   2021  CE2 PHE B 408      -4.388  -1.599 -30.367  1.00 25.22           C  
+ATOM   2022  CZ  PHE B 408      -5.072  -2.689 -29.871  1.00 28.26           C  
+ATOM   2023  H   PHE B 408      -5.925   3.245 -26.974  1.00 14.91           H  
+ATOM   2024  HA  PHE B 408      -5.264   0.807 -26.331  1.00 14.80           H  
+ATOM   2025  HB2 PHE B 408      -6.764   1.264 -28.074  1.00 17.18           H  
+ATOM   2026  HB3 PHE B 408      -5.566   1.853 -28.937  1.00 17.18           H  
+ATOM   2027  HD1 PHE B 408      -6.826  -1.170 -27.638  1.00 28.71           H  
+ATOM   2028  HD2 PHE B 408      -4.161   0.406 -30.168  1.00 26.31           H  
+ATOM   2029  HE1 PHE B 408      -6.447  -3.269 -28.527  1.00 31.86           H  
+ATOM   2030  HE2 PHE B 408      -3.768  -1.710 -31.052  1.00 30.26           H  
+ATOM   2031  HZ  PHE B 408      -4.913  -3.535 -30.223  1.00 33.92           H  
+ATOM   2032  N   GLU B 409      -2.968   2.458 -27.813  1.00 11.57           N  
+ATOM   2033  CA  GLU B 409      -1.552   2.477 -28.152  1.00 11.08           C  
+ATOM   2034  C   GLU B 409      -0.680   2.384 -26.914  1.00 14.53           C  
+ATOM   2035  O   GLU B 409       0.428   1.846 -26.985  1.00 15.59           O  
+ATOM   2036  CB  GLU B 409      -1.233   3.741 -28.947  1.00 12.66           C  
+ATOM   2037  CG  GLU B 409      -1.808   3.677 -30.347  1.00 14.04           C  
+ATOM   2038  CD  GLU B 409      -1.964   5.001 -31.042  1.00 14.46           C  
+ATOM   2039  OE1 GLU B 409      -1.356   6.006 -30.630  1.00 14.59           O  
+ATOM   2040  OE2 GLU B 409      -2.721   5.034 -32.033  1.00 15.03           O  
+ATOM   2041  H   GLU B 409      -3.382   3.187 -28.005  1.00 13.88           H  
+ATOM   2042  HA  GLU B 409      -1.346   1.712 -28.711  1.00 13.29           H  
+ATOM   2043  HB2 GLU B 409      -1.614   4.510 -28.495  1.00 15.19           H  
+ATOM   2044  HB3 GLU B 409      -0.270   3.841 -29.017  1.00 15.19           H  
+ATOM   2045  HG2 GLU B 409      -1.222   3.131 -30.894  1.00 16.85           H  
+ATOM   2046  HG3 GLU B 409      -2.688   3.272 -30.297  1.00 16.85           H  
+ATOM   2047  N   GLN B 410      -1.165   2.880 -25.782  1.00 11.20           N  
+ATOM   2048  CA  GLN B 410      -0.442   2.806 -24.517  1.00 12.15           C  
+ATOM   2049  C   GLN B 410      -0.775   1.549 -23.726  1.00 12.17           C  
+ATOM   2050  O   GLN B 410      -0.358   1.422 -22.562  1.00 13.41           O  
+ATOM   2051  CB  GLN B 410      -0.738   4.057 -23.678  1.00 11.87           C  
+ATOM   2052  CG  GLN B 410      -0.213   5.330 -24.277  1.00 12.16           C  
+ATOM   2053  CD  GLN B 410      -0.341   6.536 -23.360  1.00 13.27           C  
+ATOM   2054  OE1 GLN B 410      -0.760   6.420 -22.205  1.00 13.04           O  
+ATOM   2055  NE2 GLN B 410       0.023   7.704 -23.875  1.00 14.02           N  
+ATOM   2056  H   GLN B 410      -1.927   3.273 -25.720  1.00 13.44           H  
+ATOM   2057  HA  GLN B 410       0.511   2.791 -24.699  1.00 14.58           H  
+ATOM   2058  HB2 GLN B 410      -1.699   4.149 -23.585  1.00 14.24           H  
+ATOM   2059  HB3 GLN B 410      -0.329   3.950 -22.805  1.00 14.24           H  
+ATOM   2060  HG2 GLN B 410       0.728   5.214 -24.483  1.00 14.60           H  
+ATOM   2061  HG3 GLN B 410      -0.708   5.522 -25.089  1.00 14.60           H  
+ATOM   2062 HE21 GLN B 410       0.312   7.747 -24.684  1.00 16.82           H  
+ATOM   2063 HE22 GLN B 410      -0.029   8.419 -23.399  1.00 16.82           H  
+ATOM   2064  N   ASN B 411      -1.545   0.643 -24.325  1.00 12.55           N  
+ATOM   2065  CA  ASN B 411      -1.924  -0.644 -23.755  1.00 11.55           C  
+ATOM   2066  C   ASN B 411      -2.873  -0.505 -22.568  1.00 13.13           C  
+ATOM   2067  O   ASN B 411      -2.968  -1.420 -21.728  1.00 13.58           O  
+ATOM   2068  CB  ASN B 411      -0.695  -1.461 -23.372  1.00 12.75           C  
+ATOM   2069  CG  ASN B 411       0.128  -1.856 -24.580  1.00 18.72           C  
+ATOM   2070  OD1 ASN B 411      -0.395  -2.385 -25.562  1.00 22.95           O  
+ATOM   2071  ND2 ASN B 411       1.418  -1.578 -24.520  1.00 28.71           N  
+ATOM   2072  H   ASN B 411      -1.879   0.761 -25.109  1.00 15.06           H  
+ATOM   2073  HA  ASN B 411      -2.404  -1.146 -24.432  1.00 13.86           H  
+ATOM   2074  HB2 ASN B 411      -0.134  -0.935 -22.783  1.00 15.31           H  
+ATOM   2075  HB3 ASN B 411      -0.980  -2.272 -22.923  1.00 15.31           H  
+ATOM   2076 HD21 ASN B 411       1.933  -1.780 -25.178  1.00 34.46           H  
+ATOM   2077 HD22 ASN B 411       1.743  -1.195 -23.822  1.00 34.46           H  
+ATOM   2078  N   ASN B 412      -3.621   0.593 -22.497  1.00 12.64           N  
+ATOM   2079  CA  ASN B 412      -4.735   0.653 -21.556  1.00 12.19           C  
+ATOM   2080  C   ASN B 412      -5.827  -0.327 -21.971  1.00 11.58           C  
+ATOM   2081  O   ASN B 412      -6.069  -0.555 -23.164  1.00 14.39           O  
+ATOM   2082  CB  ASN B 412      -5.374   2.045 -21.513  1.00 10.22           C  
+ATOM   2083  CG  ASN B 412      -4.610   3.037 -20.687  1.00 11.87           C  
+ATOM   2084  OD1 ASN B 412      -3.419   2.883 -20.437  1.00 13.62           O  
+ATOM   2085  ND2 ASN B 412      -5.321   4.085 -20.251  1.00 12.01           N  
+ATOM   2086  H   ASN B 412      -3.507   1.300 -22.972  1.00 15.16           H  
+ATOM   2087  HA  ASN B 412      -4.389   0.439 -20.675  1.00 14.63           H  
+ATOM   2088  HB2 ASN B 412      -5.427   2.392 -22.417  1.00 12.26           H  
+ATOM   2089  HB3 ASN B 412      -6.264   1.968 -21.135  1.00 12.26           H  
+ATOM   2090 HD21 ASN B 412      -4.944   4.691 -19.772  1.00 14.42           H  
+ATOM   2091 HD22 ASN B 412      -6.155   4.152 -20.451  1.00 14.42           H  
+ATOM   2092  N   TYR B 413      -6.533  -0.855 -20.980  1.00 12.14           N  
+ATOM   2093  CA  TYR B 413      -7.846  -1.410 -21.238  1.00 11.89           C  
+ATOM   2094  C   TYR B 413      -8.837  -0.288 -21.520  1.00 13.73           C  
+ATOM   2095  O   TYR B 413      -8.708   0.821 -20.985  1.00 12.90           O  
+ATOM   2096  CB  TYR B 413      -8.328  -2.220 -20.041  1.00 13.74           C  
+ATOM   2097  CG  TYR B 413      -7.546  -3.486 -19.823  1.00 18.91           C  
+ATOM   2098  CD1 TYR B 413      -7.673  -4.551 -20.694  1.00 21.74           C  
+ATOM   2099  CD2 TYR B 413      -6.688  -3.606 -18.748  1.00 28.37           C  
+ATOM   2100  CE1 TYR B 413      -6.962  -5.719 -20.499  1.00 28.54           C  
+ATOM   2101  CE2 TYR B 413      -5.975  -4.769 -18.535  1.00 30.03           C  
+ATOM   2102  CZ  TYR B 413      -6.110  -5.818 -19.413  1.00 32.34           C  
+ATOM   2103  OH  TYR B 413      -5.390  -6.974 -19.210  1.00 39.00           O  
+ATOM   2104  H   TYR B 413      -6.275  -0.902 -20.161  1.00 14.56           H  
+ATOM   2105  HA  TYR B 413      -7.806  -2.000 -22.007  1.00 14.27           H  
+ATOM   2106  HB2 TYR B 413      -8.244  -1.677 -19.241  1.00 16.49           H  
+ATOM   2107  HB3 TYR B 413      -9.256  -2.464 -20.180  1.00 16.49           H  
+ATOM   2108  HD1 TYR B 413      -8.246  -4.480 -21.424  1.00 26.08           H  
+ATOM   2109  HD2 TYR B 413      -6.589  -2.894 -18.158  1.00 34.04           H  
+ATOM   2110  HE1 TYR B 413      -7.055  -6.430 -21.091  1.00 34.25           H  
+ATOM   2111  HE2 TYR B 413      -5.406  -4.842 -17.803  1.00 36.04           H  
+ATOM   2112  HH  TYR B 413      -5.558  -7.528 -19.818  1.00 46.80           H  
+ATOM   2113  N   VAL B 414      -9.848  -0.592 -22.339  1.00 12.86           N  
+ATOM   2114  CA  VAL B 414     -10.844   0.395 -22.747  1.00 11.56           C  
+ATOM   2115  C   VAL B 414     -12.223  -0.038 -22.275  1.00 16.45           C  
+ATOM   2116  O   VAL B 414     -12.544  -1.235 -22.231  1.00 15.98           O  
+ATOM   2117  CB  VAL B 414     -10.839   0.654 -24.270  1.00 12.06           C  
+ATOM   2118  CG1 VAL B 414      -9.515   1.257 -24.694  1.00 15.07           C  
+ATOM   2119  CG2 VAL B 414     -11.169  -0.627 -25.062  1.00 16.31           C  
+ATOM   2120  H   VAL B 414      -9.976  -1.373 -22.674  1.00 15.43           H  
+ATOM   2121  HA  VAL B 414     -10.628   1.231 -22.304  1.00 13.88           H  
+ATOM   2122  HB  VAL B 414     -11.537   1.294 -24.481  1.00 14.48           H  
+ATOM   2123 HG11 VAL B 414      -9.537   1.427 -25.649  1.00 18.08           H  
+ATOM   2124 HG12 VAL B 414      -9.378   2.089 -24.213  1.00 18.08           H  
+ATOM   2125 HG13 VAL B 414      -8.803   0.633 -24.485  1.00 18.08           H  
+ATOM   2126 HG21 VAL B 414     -11.077  -0.445 -26.010  1.00 19.57           H  
+ATOM   2127 HG22 VAL B 414     -10.552  -1.329 -24.799  1.00 19.57           H  
+ATOM   2128 HG23 VAL B 414     -12.079  -0.896 -24.864  1.00 19.57           H  
+ATOM   2129  N   VAL B 415     -13.031   0.947 -21.899  1.00 11.39           N  
+ATOM   2130  CA  VAL B 415     -14.387   0.704 -21.403  1.00 11.90           C  
+ATOM   2131  C   VAL B 415     -15.323   1.666 -22.122  1.00 11.13           C  
+ATOM   2132  O   VAL B 415     -15.601   2.767 -21.633  1.00 11.14           O  
+ATOM   2133  CB  VAL B 415     -14.468   0.872 -19.876  1.00 12.20           C  
+ATOM   2134  CG1 VAL B 415     -15.873   0.604 -19.393  1.00 13.59           C  
+ATOM   2135  CG2 VAL B 415     -13.472  -0.054 -19.206  1.00 15.20           C  
+ATOM   2136  H   VAL B 415     -12.816   1.780 -21.922  1.00 13.67           H  
+ATOM   2137  HA  VAL B 415     -14.653  -0.206 -21.608  1.00 14.28           H  
+ATOM   2138  HB  VAL B 415     -14.244   1.784 -19.635  1.00 14.64           H  
+ATOM   2139 HG11 VAL B 415     -15.872   0.567 -18.424  1.00 16.31           H  
+ATOM   2140 HG12 VAL B 415     -16.453   1.321 -19.695  1.00 16.31           H  
+ATOM   2141 HG13 VAL B 415     -16.176  -0.242 -19.756  1.00 16.31           H  
+ATOM   2142 HG21 VAL B 415     -13.595  -0.007 -18.245  1.00 18.24           H  
+ATOM   2143 HG22 VAL B 415     -13.626  -0.961 -19.515  1.00 18.24           H  
+ATOM   2144 HG23 VAL B 415     -12.573   0.226 -19.439  1.00 18.24           H  
+ATOM   2145  N   PRO B 416     -15.790   1.322 -23.322  1.00  9.56           N  
+ATOM   2146  CA  PRO B 416     -16.683   2.211 -24.067  1.00  9.50           C  
+ATOM   2147  C   PRO B 416     -18.119   2.015 -23.599  1.00 11.03           C  
+ATOM   2148  O   PRO B 416     -18.679   0.926 -23.725  1.00 10.98           O  
+ATOM   2149  CB  PRO B 416     -16.487   1.759 -25.525  1.00 13.38           C  
+ATOM   2150  CG  PRO B 416     -16.154   0.284 -25.395  1.00 13.69           C  
+ATOM   2151  CD  PRO B 416     -15.381   0.131 -24.094  1.00 13.49           C  
+ATOM   2152  HA  PRO B 416     -16.427   3.142 -23.972  1.00 11.40           H  
+ATOM   2153  HB2 PRO B 416     -17.303   1.893 -26.032  1.00 16.06           H  
+ATOM   2154  HB3 PRO B 416     -15.758   2.250 -25.935  1.00 16.06           H  
+ATOM   2155  HG2 PRO B 416     -16.974  -0.233 -25.368  1.00 16.43           H  
+ATOM   2156  HG3 PRO B 416     -15.611   0.006 -26.150  1.00 16.43           H  
+ATOM   2157  HD2 PRO B 416     -15.636  -0.684 -23.634  1.00 16.18           H  
+ATOM   2158  HD3 PRO B 416     -14.425   0.135 -24.256  1.00 16.18           H  
+ATOM   2159  N   VAL B 417     -18.728   3.070 -23.069  1.00 11.32           N  
+ATOM   2160  CA  VAL B 417     -20.062   2.948 -22.471  1.00 10.39           C  
+ATOM   2161  C   VAL B 417     -21.068   3.176 -23.597  1.00 10.11           C  
+ATOM   2162  O   VAL B 417     -21.572   4.275 -23.811  1.00 11.40           O  
+ATOM   2163  CB  VAL B 417     -20.259   3.887 -21.285  1.00  9.88           C  
+ATOM   2164  CG1 VAL B 417     -21.591   3.581 -20.617  1.00 11.21           C  
+ATOM   2165  CG2 VAL B 417     -19.116   3.690 -20.303  1.00 11.14           C  
+ATOM   2166  H   VAL B 417     -18.395   3.863 -23.041  1.00 13.58           H  
+ATOM   2167  HA  VAL B 417     -20.181   2.041 -22.148  1.00 12.47           H  
+ATOM   2168  HB  VAL B 417     -20.266   4.811 -21.580  1.00 11.85           H  
+ATOM   2169 HG11 VAL B 417     -21.680   4.132 -19.823  1.00 13.45           H  
+ATOM   2170 HG12 VAL B 417     -22.309   3.778 -21.239  1.00 13.45           H  
+ATOM   2171 HG13 VAL B 417     -21.613   2.643 -20.373  1.00 13.45           H  
+ATOM   2172 HG21 VAL B 417     -19.301   4.198 -19.497  1.00 13.37           H  
+ATOM   2173 HG22 VAL B 417     -19.043   2.747 -20.089  1.00 13.37           H  
+ATOM   2174 HG23 VAL B 417     -18.293   4.003 -20.709  1.00 13.37           H  
+ATOM   2175  N   GLY B 418     -21.389   2.093 -24.305  1.00 10.68           N  
+ATOM   2176  CA  GLY B 418     -22.220   2.202 -25.490  1.00 12.97           C  
+ATOM   2177  C   GLY B 418     -23.598   2.774 -25.236  1.00 11.24           C  
+ATOM   2178  O   GLY B 418     -24.179   3.409 -26.121  1.00 12.34           O  
+ATOM   2179  H   GLY B 418     -21.138   1.292 -24.118  1.00 12.81           H  
+ATOM   2180  HA2 GLY B 418     -21.774   2.774 -26.134  1.00 15.56           H  
+ATOM   2181  HA3 GLY B 418     -22.331   1.319 -25.877  1.00 15.56           H  
+ATOM   2182  N   ALA B 419     -24.151   2.544 -24.045  1.00 10.60           N  
+ATOM   2183  CA  ALA B 419     -25.462   3.068 -23.698  1.00 11.26           C  
+ATOM   2184  C   ALA B 419     -25.518   4.588 -23.746  1.00 15.48           C  
+ATOM   2185  O   ALA B 419     -26.616   5.149 -23.791  1.00 18.64           O  
+ATOM   2186  CB  ALA B 419     -25.864   2.582 -22.308  1.00 14.51           C  
+ATOM   2187  H   ALA B 419     -23.783   2.084 -23.418  1.00 12.73           H  
+ATOM   2188  HA  ALA B 419     -26.107   2.730 -24.339  1.00 13.51           H  
+ATOM   2189  HB1 ALA B 419     -26.736   2.943 -22.087  1.00 17.41           H  
+ATOM   2190  HB2 ALA B 419     -25.897   1.612 -22.310  1.00 17.41           H  
+ATOM   2191  HB3 ALA B 419     -25.206   2.888 -21.664  1.00 17.41           H  
+ATOM   2192  N   THR B 420     -24.371   5.275 -23.759  1.00 11.28           N  
+ATOM   2193  CA  THR B 420     -24.392   6.729 -23.823  1.00 10.76           C  
+ATOM   2194  C   THR B 420     -24.408   7.268 -25.247  1.00 12.44           C  
+ATOM   2195  O   THR B 420     -24.493   8.490 -25.420  1.00 12.64           O  
+ATOM   2196  CB  THR B 420     -23.216   7.357 -23.040  1.00 10.05           C  
+ATOM   2197  OG1 THR B 420     -21.944   7.032 -23.618  1.00 12.08           O  
+ATOM   2198  CG2 THR B 420     -23.249   6.954 -21.562  1.00 12.69           C  
+ATOM   2199  H   THR B 420     -23.587   4.923 -23.733  1.00 13.54           H  
+ATOM   2200  HA  THR B 420     -25.205   7.022 -23.382  1.00 12.91           H  
+ATOM   2201  HB  THR B 420     -23.316   8.321 -23.089  1.00 12.06           H  
+ATOM   2202  HG1 THR B 420     -21.816   6.203 -23.582  1.00 14.50           H  
+ATOM   2203 HG21 THR B 420     -22.510   7.368 -21.088  1.00 15.22           H  
+ATOM   2204 HG22 THR B 420     -24.082   7.241 -21.158  1.00 15.22           H  
+ATOM   2205 HG23 THR B 420     -23.174   5.990 -21.479  1.00 15.22           H  
+ATOM   2206  N   GLY B 421     -24.382   6.410 -26.264  1.00 11.54           N  
+ATOM   2207  CA  GLY B 421     -24.535   6.888 -27.622  1.00 11.55           C  
+ATOM   2208  C   GLY B 421     -23.269   7.486 -28.225  1.00 10.36           C  
+ATOM   2209  O   GLY B 421     -22.175   7.390 -27.686  1.00 11.60           O  
+ATOM   2210  H   GLY B 421     -24.278   5.559 -26.189  1.00 13.84           H  
+ATOM   2211  HA2 GLY B 421     -24.812   6.149 -28.185  1.00 13.86           H  
+ATOM   2212  HA3 GLY B 421     -25.223   7.572 -27.638  1.00 13.86           H  
+ATOM   2213  N   TYR B 422     -23.447   8.094 -29.394  1.00 12.06           N  
+ATOM   2214  CA  TYR B 422     -22.429   8.923 -30.065  1.00 12.43           C  
+ATOM   2215  C   TYR B 422     -21.145   8.099 -30.247  1.00 11.55           C  
+ATOM   2216  O   TYR B 422     -21.215   6.937 -30.684  1.00 12.96           O  
+ATOM   2217  CB  TYR B 422     -22.236  10.234 -29.311  1.00 11.07           C  
+ATOM   2218  CG  TYR B 422     -23.515  10.937 -29.014  1.00 12.67           C  
+ATOM   2219  CD1 TYR B 422     -24.118  11.736 -29.967  1.00 13.88           C  
+ATOM   2220  CD2 TYR B 422     -24.120  10.814 -27.774  1.00 13.29           C  
+ATOM   2221  CE1 TYR B 422     -25.283  12.383 -29.696  1.00 13.00           C  
+ATOM   2222  CE2 TYR B 422     -25.295  11.461 -27.485  1.00 15.58           C  
+ATOM   2223  CZ  TYR B 422     -25.872  12.251 -28.458  1.00 16.79           C  
+ATOM   2224  OH  TYR B 422     -27.054  12.892 -28.188  1.00 19.40           O  
+ATOM   2225  H   TYR B 422     -24.178   8.043 -29.845  1.00 14.47           H  
+ATOM   2226  HA  TYR B 422     -22.768   9.115 -30.953  1.00 14.92           H  
+ATOM   2227  HB2 TYR B 422     -21.795  10.048 -28.467  1.00 13.28           H  
+ATOM   2228  HB3 TYR B 422     -21.687  10.827 -29.849  1.00 13.28           H  
+ATOM   2229  HD1 TYR B 422     -23.722  11.833 -30.804  1.00 16.65           H  
+ATOM   2230  HD2 TYR B 422     -23.722  10.281 -27.124  1.00 15.95           H  
+ATOM   2231  HE1 TYR B 422     -25.682  12.915 -30.346  1.00 15.61           H  
+ATOM   2232  HE2 TYR B 422     -25.695  11.369 -26.650  1.00 18.69           H  
+ATOM   2233  HH  TYR B 422     -27.338  13.274 -28.880  1.00 23.28           H  
+ATOM   2234  N   ILE B 423     -19.979   8.701 -29.992  1.00 12.77           N  
+ATOM   2235  CA  ILE B 423     -18.698   8.020 -30.197  1.00 12.40           C  
+ATOM   2236  C   ILE B 423     -18.614   6.786 -29.325  1.00 12.20           C  
+ATOM   2237  O   ILE B 423     -18.081   5.747 -29.734  1.00 12.69           O  
+ATOM   2238  CB  ILE B 423     -17.520   8.978 -29.907  1.00 16.22           C  
+ATOM   2239  CG1 ILE B 423     -17.375   9.949 -31.078  1.00 18.82           C  
+ATOM   2240  CG2 ILE B 423     -16.198   8.199 -29.664  1.00 16.95           C  
+ATOM   2241  CD1 ILE B 423     -16.664   9.323 -32.287  1.00 21.10           C  
+ATOM   2242  H   ILE B 423     -19.901   9.506 -29.699  1.00 15.32           H  
+ATOM   2243  HA  ILE B 423     -18.647   7.747 -31.127  1.00 14.88           H  
+ATOM   2244  HB  ILE B 423     -17.710   9.472 -29.094  1.00 19.46           H  
+ATOM   2245 HG12 ILE B 423     -18.258  10.233 -31.363  1.00 22.58           H  
+ATOM   2246 HG13 ILE B 423     -16.857  10.716 -30.789  1.00 22.58           H  
+ATOM   2247 HG21 ILE B 423     -15.451   8.812 -29.744  1.00 20.34           H  
+ATOM   2248 HG22 ILE B 423     -16.217   7.815 -28.773  1.00 20.34           H  
+ATOM   2249 HG23 ILE B 423     -16.121   7.494 -30.326  1.00 20.34           H  
+ATOM   2250 HD11 ILE B 423     -16.790   9.897 -33.059  1.00 25.32           H  
+ATOM   2251 HD12 ILE B 423     -15.718   9.240 -32.089  1.00 25.32           H  
+ATOM   2252 HD13 ILE B 423     -17.044   8.448 -32.459  1.00 25.32           H  
+ATOM   2253  N   ALA B 424     -19.089   6.894 -28.079  1.00 12.43           N  
+ATOM   2254  CA  ALA B 424     -18.959   5.773 -27.158  1.00 11.42           C  
+ATOM   2255  C   ALA B 424     -19.677   4.538 -27.693  1.00 10.35           C  
+ATOM   2256  O   ALA B 424     -19.207   3.412 -27.507  1.00 10.91           O  
+ATOM   2257  CB  ALA B 424     -19.496   6.154 -25.780  1.00 11.32           C  
+ATOM   2258  H   ALA B 424     -19.481   7.588 -27.756  1.00 14.91           H  
+ATOM   2259  HA  ALA B 424     -18.018   5.557 -27.059  1.00 13.71           H  
+ATOM   2260  HB1 ALA B 424     -19.408   5.393 -25.185  1.00 13.59           H  
+ATOM   2261  HB2 ALA B 424     -18.983   6.903 -25.437  1.00 13.59           H  
+ATOM   2262  HB3 ALA B 424     -20.430   6.404 -25.863  1.00 13.59           H  
+ATOM   2263  N   LYS B 425     -20.807   4.732 -28.369  1.00 11.23           N  
+ATOM   2264  CA  LYS B 425     -21.499   3.603 -28.980  1.00 12.12           C  
+ATOM   2265  C   LYS B 425     -20.721   3.060 -30.170  1.00 12.93           C  
+ATOM   2266  O   LYS B 425     -20.612   1.839 -30.332  1.00 11.96           O  
+ATOM   2267  CB  LYS B 425     -22.905   4.031 -29.382  1.00 14.61           C  
+ATOM   2268  CG  LYS B 425     -23.614   3.043 -30.277  1.00 20.87           C  
+ATOM   2269  CD  LYS B 425     -24.370   2.093 -29.453  1.00 22.18           C  
+ATOM   2270  CE  LYS B 425     -25.698   2.697 -29.015  1.00 23.06           C  
+ATOM   2271  NZ  LYS B 425     -26.398   1.745 -28.092  1.00 23.85           N  
+ATOM   2272  H   LYS B 425     -21.187   5.494 -28.487  1.00 13.47           H  
+ATOM   2273  HA  LYS B 425     -21.578   2.883 -28.336  1.00 14.54           H  
+ATOM   2274  HB2 LYS B 425     -23.439   4.139 -28.580  1.00 17.54           H  
+ATOM   2275  HB3 LYS B 425     -22.849   4.874 -29.859  1.00 17.54           H  
+ATOM   2276  HG2 LYS B 425     -24.232   3.512 -30.860  1.00 25.04           H  
+ATOM   2277  HG3 LYS B 425     -22.965   2.553 -30.805  1.00 25.04           H  
+ATOM   2278  HD2 LYS B 425     -24.551   1.290 -29.966  1.00 26.61           H  
+ATOM   2279  HD3 LYS B 425     -23.856   1.871 -28.660  1.00 26.61           H  
+ATOM   2280  HE2 LYS B 425     -25.541   3.531 -28.545  1.00 27.67           H  
+ATOM   2281  HE3 LYS B 425     -26.260   2.853 -29.790  1.00 27.67           H  
+ATOM   2282  HZ1 LYS B 425     -27.172   2.093 -27.827  1.00 28.63           H  
+ATOM   2283  HZ2 LYS B 425     -26.555   0.976 -28.511  1.00 28.63           H  
+ATOM   2284  HZ3 LYS B 425     -25.892   1.587 -27.377  1.00 28.63           H  
+ATOM   2285  N   ASP B 426     -20.161   3.936 -31.004  1.00 13.97           N  
+ATOM   2286  CA  ASP B 426     -19.323   3.463 -32.104  1.00 14.36           C  
+ATOM   2287  C   ASP B 426     -18.138   2.669 -31.571  1.00 13.32           C  
+ATOM   2288  O   ASP B 426     -17.766   1.628 -32.124  1.00 14.32           O  
+ATOM   2289  CB  ASP B 426     -18.825   4.632 -32.950  1.00 14.96           C  
+ATOM   2290  CG  ASP B 426     -19.921   5.271 -33.794  1.00 21.88           C  
+ATOM   2291  OD1 ASP B 426     -21.027   4.698 -33.955  1.00 19.26           O  
+ATOM   2292  OD2 ASP B 426     -19.647   6.386 -34.288  1.00 24.75           O  
+ATOM   2293  H   ASP B 426     -20.248   4.791 -30.956  1.00 16.76           H  
+ATOM   2294  HA  ASP B 426     -19.861   2.892 -32.675  1.00 17.23           H  
+ATOM   2295  HB2 ASP B 426     -18.465   5.314 -32.362  1.00 17.95           H  
+ATOM   2296  HB3 ASP B 426     -18.134   4.313 -33.551  1.00 17.95           H  
+ATOM   2297  N   LEU B 427     -17.520   3.155 -30.498  1.00 12.27           N  
+ATOM   2298  CA  LEU B 427     -16.396   2.435 -29.915  1.00 12.48           C  
+ATOM   2299  C   LEU B 427     -16.850   1.118 -29.285  1.00 11.77           C  
+ATOM   2300  O   LEU B 427     -16.121   0.124 -29.346  1.00 12.10           O  
+ATOM   2301  CB  LEU B 427     -15.686   3.314 -28.895  1.00 13.49           C  
+ATOM   2302  CG  LEU B 427     -15.020   4.582 -29.436  1.00 12.92           C  
+ATOM   2303  CD1 LEU B 427     -14.506   5.434 -28.279  1.00 14.36           C  
+ATOM   2304  CD2 LEU B 427     -13.899   4.255 -30.423  1.00 12.94           C  
+ATOM   2305  H   LEU B 427     -17.728   3.887 -30.096  1.00 14.72           H  
+ATOM   2306  HA  LEU B 427     -15.759   2.223 -30.615  1.00 14.98           H  
+ATOM   2307  HB2 LEU B 427     -16.337   3.594 -28.233  1.00 16.19           H  
+ATOM   2308  HB3 LEU B 427     -14.991   2.785 -28.473  1.00 16.19           H  
+ATOM   2309  HG  LEU B 427     -15.679   5.097 -29.927  1.00 15.50           H  
+ATOM   2310 HD11 LEU B 427     -14.056   6.215 -28.637  1.00 17.23           H  
+ATOM   2311 HD12 LEU B 427     -15.257   5.708 -27.730  1.00 17.23           H  
+ATOM   2312 HD13 LEU B 427     -13.885   4.907 -27.751  1.00 17.23           H  
+ATOM   2313 HD21 LEU B 427     -13.436   5.074 -30.658  1.00 15.53           H  
+ATOM   2314 HD22 LEU B 427     -13.281   3.635 -30.005  1.00 15.53           H  
+ATOM   2315 HD23 LEU B 427     -14.285   3.853 -31.217  1.00 15.53           H  
+ATOM   2316  N   TRP B 428     -18.025   1.100 -28.642  1.00 11.12           N  
+ATOM   2317  CA  TRP B 428     -18.542  -0.158 -28.119  1.00 10.13           C  
+ATOM   2318  C   TRP B 428     -18.728  -1.167 -29.237  1.00 12.71           C  
+ATOM   2319  O   TRP B 428     -18.333  -2.328 -29.099  1.00 12.88           O  
+ATOM   2320  CB  TRP B 428     -19.848   0.055 -27.346  1.00 11.62           C  
+ATOM   2321  CG  TRP B 428     -20.295  -1.212 -26.669  1.00 11.36           C  
+ATOM   2322  CD1 TRP B 428     -20.044  -1.601 -25.378  1.00 11.73           C  
+ATOM   2323  CD2 TRP B 428     -21.027  -2.293 -27.268  1.00 13.07           C  
+ATOM   2324  NE1 TRP B 428     -20.590  -2.839 -25.143  1.00 11.61           N  
+ATOM   2325  CE2 TRP B 428     -21.199  -3.284 -26.287  1.00 12.96           C  
+ATOM   2326  CE3 TRP B 428     -21.574  -2.497 -28.531  1.00 15.07           C  
+ATOM   2327  CZ2 TRP B 428     -21.899  -4.471 -26.536  1.00 13.20           C  
+ATOM   2328  CZ3 TRP B 428     -22.249  -3.674 -28.787  1.00 16.50           C  
+ATOM   2329  CH2 TRP B 428     -22.407  -4.651 -27.797  1.00 17.94           C  
+ATOM   2330  H   TRP B 428     -18.525   1.786 -28.502  1.00 13.34           H  
+ATOM   2331  HA  TRP B 428     -17.900  -0.515 -27.485  1.00 12.16           H  
+ATOM   2332  HB2 TRP B 428     -19.712   0.734 -26.666  1.00 13.94           H  
+ATOM   2333  HB3 TRP B 428     -20.543   0.336 -27.961  1.00 13.94           H  
+ATOM   2334  HD1 TRP B 428     -19.573  -1.100 -24.753  1.00 14.08           H  
+ATOM   2335  HE1 TRP B 428     -20.555  -3.266 -24.398  1.00 13.93           H  
+ATOM   2336  HE3 TRP B 428     -21.487  -1.851 -29.193  1.00 18.08           H  
+ATOM   2337  HZ2 TRP B 428     -22.013  -5.113 -25.873  1.00 15.84           H  
+ATOM   2338  HZ3 TRP B 428     -22.605  -3.820 -29.634  1.00 19.80           H  
+ATOM   2339  HH2 TRP B 428     -22.865  -5.435 -27.998  1.00 21.53           H  
+ATOM   2340  N   ASN B 429     -19.268  -0.728 -30.379  1.00 11.78           N  
+ATOM   2341  CA  ASN B 429     -19.479  -1.658 -31.484  1.00 13.03           C  
+ATOM   2342  C   ASN B 429     -18.164  -2.173 -32.026  1.00 14.36           C  
+ATOM   2343  O   ASN B 429     -18.036  -3.370 -32.316  1.00 17.62           O  
+ATOM   2344  CB  ASN B 429     -20.282  -0.989 -32.597  1.00 14.55           C  
+ATOM   2345  CG  ASN B 429     -21.737  -0.944 -32.294  1.00 15.61           C  
+ATOM   2346  OD1 ASN B 429     -22.313  -1.909 -31.797  1.00 20.60           O  
+ATOM   2347  ND2 ASN B 429     -22.372   0.164 -32.655  1.00 23.97           N  
+ATOM   2348  H   ASN B 429     -19.514   0.081 -30.533  1.00 14.13           H  
+ATOM   2349  HA  ASN B 429     -19.991  -2.414 -31.155  1.00 15.63           H  
+ATOM   2350  HB2 ASN B 429     -19.969  -0.078 -32.711  1.00 17.45           H  
+ATOM   2351  HB3 ASN B 429     -20.160  -1.487 -33.420  1.00 17.45           H  
+ATOM   2352 HD21 ASN B 429     -23.215   0.244 -32.504  1.00 28.77           H  
+ATOM   2353 HD22 ASN B 429     -21.941   0.801 -33.039  1.00 28.77           H  
+ATOM   2354  N   LYS B 430     -17.179  -1.288 -32.149  1.00 12.56           N  
+ATOM   2355  CA  LYS B 430     -15.861  -1.681 -32.628  1.00 17.87           C  
+ATOM   2356  C   LYS B 430     -15.250  -2.747 -31.726  1.00 17.93           C  
+ATOM   2357  O   LYS B 430     -14.774  -3.783 -32.198  1.00 19.12           O  
+ATOM   2358  CB  LYS B 430     -14.953  -0.463 -32.700  1.00 17.55           C  
+ATOM   2359  CG  LYS B 430     -13.503  -0.767 -33.078  1.00 24.57           C  
+ATOM   2360  CD  LYS B 430     -12.541   0.409 -32.797  1.00 30.69           C  
+ATOM   2361  CE  LYS B 430     -12.751   1.596 -33.749  1.00 49.07           C  
+ATOM   2362  NZ  LYS B 430     -11.801   2.747 -33.521  1.00 48.36           N  
+ATOM   2363  H   LYS B 430     -17.249  -0.452 -31.962  1.00 15.07           H  
+ATOM   2364  HA  LYS B 430     -15.947  -2.050 -33.521  1.00 21.45           H  
+ATOM   2365  HB2 LYS B 430     -15.307   0.146 -33.367  1.00 21.06           H  
+ATOM   2366  HB3 LYS B 430     -14.944  -0.033 -31.831  1.00 21.06           H  
+ATOM   2367  HG2 LYS B 430     -13.197  -1.531 -32.564  1.00 29.48           H  
+ATOM   2368  HG3 LYS B 430     -13.459  -0.966 -34.026  1.00 29.48           H  
+ATOM   2369  HD2 LYS B 430     -12.684   0.724 -31.891  1.00 36.83           H  
+ATOM   2370  HD3 LYS B 430     -11.627   0.101 -32.900  1.00 36.83           H  
+ATOM   2371  HE2 LYS B 430     -12.626   1.289 -34.661  1.00 58.88           H  
+ATOM   2372  HE3 LYS B 430     -13.653   1.932 -33.633  1.00 58.88           H  
+ATOM   2373  HZ1 LYS B 430     -11.891   3.056 -32.690  1.00 58.03           H  
+ATOM   2374  HZ2 LYS B 430     -10.961   2.478 -33.639  1.00 58.03           H  
+ATOM   2375  HZ3 LYS B 430     -11.976   3.405 -34.093  1.00 58.03           H  
+ATOM   2376  N   VAL B 431     -15.252  -2.503 -30.418  1.00 12.93           N  
+ATOM   2377  CA  VAL B 431     -14.652  -3.443 -29.481  1.00 12.83           C  
+ATOM   2378  C   VAL B 431     -15.417  -4.762 -29.500  1.00 16.41           C  
+ATOM   2379  O   VAL B 431     -14.821  -5.852 -29.488  1.00 16.99           O  
+ATOM   2380  CB  VAL B 431     -14.621  -2.811 -28.071  1.00 12.74           C  
+ATOM   2381  CG1 VAL B 431     -14.294  -3.853 -27.029  1.00 12.66           C  
+ATOM   2382  CG2 VAL B 431     -13.630  -1.642 -28.032  1.00 14.22           C  
+ATOM   2383  H   VAL B 431     -15.592  -1.804 -30.050  1.00 15.51           H  
+ATOM   2384  HA  VAL B 431     -13.739  -3.631 -29.749  1.00 15.40           H  
+ATOM   2385  HB  VAL B 431     -15.499  -2.457 -27.860  1.00 15.29           H  
+ATOM   2386 HG11 VAL B 431     -14.053  -3.408 -26.202  1.00 15.19           H  
+ATOM   2387 HG12 VAL B 431     -15.073  -4.414 -26.888  1.00 15.19           H  
+ATOM   2388 HG13 VAL B 431     -13.551  -4.392 -27.343  1.00 15.19           H  
+ATOM   2389 HG21 VAL B 431     -13.620  -1.266 -27.138  1.00 17.07           H  
+ATOM   2390 HG22 VAL B 431     -12.746  -1.969 -28.264  1.00 17.07           H  
+ATOM   2391 HG23 VAL B 431     -13.911  -0.968 -28.671  1.00 17.07           H  
+ATOM   2392  N   ASN B 432     -16.746  -4.681 -29.533  1.00 14.31           N  
+ATOM   2393  CA  ASN B 432     -17.589  -5.872 -29.581  1.00 13.35           C  
+ATOM   2394  C   ASN B 432     -17.244  -6.742 -30.779  1.00 17.82           C  
+ATOM   2395  O   ASN B 432     -17.208  -7.973 -30.671  1.00 20.12           O  
+ATOM   2396  CB  ASN B 432     -19.056  -5.452 -29.627  1.00 14.83           C  
+ATOM   2397  CG  ASN B 432     -20.009  -6.623 -29.538  1.00 16.45           C  
+ATOM   2398  OD1 ASN B 432     -20.946  -6.760 -30.356  1.00 25.12           O  
+ATOM   2399  ND2 ASN B 432     -19.802  -7.471 -28.552  1.00 13.85           N  
+ATOM   2400  H   ASN B 432     -17.188  -3.943 -29.529  1.00 17.17           H  
+ATOM   2401  HA  ASN B 432     -17.445  -6.400 -28.781  1.00 16.02           H  
+ATOM   2402  HB2 ASN B 432     -19.238  -4.861 -28.879  1.00 17.80           H  
+ATOM   2403  HB3 ASN B 432     -19.226  -4.991 -30.463  1.00 17.80           H  
+ATOM   2404 HD21 ASN B 432     -20.316  -8.154 -28.457  1.00 16.62           H  
+ATOM   2405 HD22 ASN B 432     -19.152  -7.342 -28.003  1.00 16.62           H  
+ATOM   2406  N   GLU B 433     -16.991  -6.117 -31.924  1.00 16.44           N  
+ATOM   2407  CA  GLU B 433     -16.683  -6.877 -33.132  1.00 19.33           C  
+ATOM   2408  C   GLU B 433     -15.297  -7.502 -33.084  1.00 25.06           C  
+ATOM   2409  O   GLU B 433     -15.045  -8.478 -33.802  1.00 27.62           O  
+ATOM   2410  CB  GLU B 433     -16.803  -5.964 -34.353  1.00 24.17           C  
+ATOM   2411  CG  GLU B 433     -16.041  -6.470 -35.566  1.00 55.38           C  
+ATOM   2412  CD  GLU B 433     -16.521  -5.853 -36.864  1.00 69.33           C  
+ATOM   2413  OE1 GLU B 433     -16.733  -4.619 -36.901  1.00 71.51           O  
+ATOM   2414  OE2 GLU B 433     -16.692  -6.614 -37.844  1.00 64.32           O  
+ATOM   2415  H   GLU B 433     -16.991  -5.264 -32.028  1.00 19.73           H  
+ATOM   2416  HA  GLU B 433     -17.326  -7.597 -33.227  1.00 23.20           H  
+ATOM   2417  HB2 GLU B 433     -17.739  -5.892 -34.598  1.00 29.01           H  
+ATOM   2418  HB3 GLU B 433     -16.451  -5.089 -34.125  1.00 29.01           H  
+ATOM   2419  HG2 GLU B 433     -15.101  -6.254 -35.461  1.00 66.46           H  
+ATOM   2420  HG3 GLU B 433     -16.155  -7.431 -35.631  1.00 66.46           H  
+ATOM   2421  N   GLU B 434     -14.391  -6.961 -32.280  1.00 19.34           N  
+ATOM   2422  CA  GLU B 434     -13.031  -7.469 -32.146  1.00 21.27           C  
+ATOM   2423  C   GLU B 434     -12.738  -7.809 -30.693  1.00 13.83           C  
+ATOM   2424  O   GLU B 434     -11.668  -7.503 -30.161  1.00 17.70           O  
+ATOM   2425  CB  GLU B 434     -12.022  -6.457 -32.681  1.00 26.19           C  
+ATOM   2426  CG  GLU B 434     -12.430  -5.896 -34.020  1.00 35.24           C  
+ATOM   2427  CD  GLU B 434     -11.250  -5.519 -34.858  1.00 49.03           C  
+ATOM   2428  OE1 GLU B 434     -10.751  -4.385 -34.704  1.00 48.58           O  
+ATOM   2429  OE2 GLU B 434     -10.808  -6.374 -35.657  1.00 50.64           O  
+ATOM   2430  H   GLU B 434     -14.546  -6.275 -31.784  1.00 23.21           H  
+ATOM   2431  HA  GLU B 434     -12.942  -8.281 -32.671  1.00 25.52           H  
+ATOM   2432  HB2 GLU B 434     -11.949  -5.720 -32.054  1.00 31.42           H  
+ATOM   2433  HB3 GLU B 434     -11.161  -6.891 -32.785  1.00 31.42           H  
+ATOM   2434  HG2 GLU B 434     -12.942  -6.564 -34.502  1.00 42.29           H  
+ATOM   2435  HG3 GLU B 434     -12.968  -5.101 -33.881  1.00 42.29           H  
+ATOM   2436  N   PHE B 435     -13.698  -8.467 -30.049  1.00 16.77           N  
+ATOM   2437  CA  PHE B 435     -13.692  -8.556 -28.593  1.00 17.39           C  
+ATOM   2438  C   PHE B 435     -12.407  -9.182 -28.066  1.00 17.92           C  
+ATOM   2439  O   PHE B 435     -11.856  -8.722 -27.055  1.00 19.15           O  
+ATOM   2440  CB  PHE B 435     -14.918  -9.341 -28.136  1.00 19.99           C  
+ATOM   2441  CG  PHE B 435     -15.057  -9.453 -26.645  1.00 18.79           C  
+ATOM   2442  CD1 PHE B 435     -14.408 -10.463 -25.951  1.00 20.98           C  
+ATOM   2443  CD2 PHE B 435     -15.858  -8.574 -25.934  1.00 20.14           C  
+ATOM   2444  CE1 PHE B 435     -14.543 -10.571 -24.581  1.00 20.77           C  
+ATOM   2445  CE2 PHE B 435     -15.999  -8.687 -24.557  1.00 25.19           C  
+ATOM   2446  CZ  PHE B 435     -15.343  -9.687 -23.885  1.00 21.56           C  
+ATOM   2447  H   PHE B 435     -14.358  -8.867 -30.428  1.00 20.12           H  
+ATOM   2448  HA  PHE B 435     -13.742  -7.663 -28.218  1.00 20.86           H  
+ATOM   2449  HB2 PHE B 435     -15.712  -8.899 -28.473  1.00 23.99           H  
+ATOM   2450  HB3 PHE B 435     -14.861 -10.241 -28.494  1.00 23.99           H  
+ATOM   2451  HD1 PHE B 435     -13.879 -11.073 -26.412  1.00 25.18           H  
+ATOM   2452  HD2 PHE B 435     -16.309  -7.898 -26.387  1.00 24.17           H  
+ATOM   2453  HE1 PHE B 435     -14.092 -11.243 -24.124  1.00 24.93           H  
+ATOM   2454  HE2 PHE B 435     -16.537  -8.087 -24.092  1.00 30.23           H  
+ATOM   2455  HZ  PHE B 435     -15.436  -9.769 -22.964  1.00 25.87           H  
+ATOM   2456  N   GLU B 436     -11.913 -10.234 -28.725  1.00 20.10           N  
+ATOM   2457  CA  GLU B 436     -10.762 -10.951 -28.193  1.00 23.69           C  
+ATOM   2458  C   GLU B 436      -9.477 -10.153 -28.299  1.00 22.93           C  
+ATOM   2459  O   GLU B 436      -8.537 -10.417 -27.536  1.00 25.93           O  
+ATOM   2460  CB  GLU B 436     -10.631 -12.303 -28.899  1.00 24.75           C  
+ATOM   2461  CG  GLU B 436     -11.511 -13.352 -28.262  1.00 27.56           C  
+ATOM   2462  CD  GLU B 436     -11.092 -13.646 -26.827  1.00 36.59           C  
+ATOM   2463  OE1 GLU B 436      -9.919 -14.046 -26.628  1.00 45.01           O  
+ATOM   2464  OE2 GLU B 436     -11.916 -13.451 -25.898  1.00 45.11           O  
+ATOM   2465  H   GLU B 436     -12.222 -10.543 -29.466  1.00 24.12           H  
+ATOM   2466  HA  GLU B 436     -10.903 -11.126 -27.249  1.00 28.43           H  
+ATOM   2467  HB2 GLU B 436     -10.895 -12.206 -29.828  1.00 29.70           H  
+ATOM   2468  HB3 GLU B 436      -9.710 -12.604 -28.846  1.00 29.70           H  
+ATOM   2469  HG2 GLU B 436     -12.428 -13.037 -28.252  1.00 33.07           H  
+ATOM   2470  HG3 GLU B 436     -11.448 -14.175 -28.771  1.00 33.07           H  
+ATOM   2471  N   THR B 437      -9.420  -9.179 -29.206  1.00 19.11           N  
+ATOM   2472  CA  THR B 437      -8.295  -8.257 -29.254  1.00 21.37           C  
+ATOM   2473  C   THR B 437      -8.250  -7.398 -27.995  1.00 25.99           C  
+ATOM   2474  O   THR B 437      -7.190  -7.223 -27.387  1.00 26.69           O  
+ATOM   2475  CB  THR B 437      -8.395  -7.383 -30.498  1.00 25.68           C  
+ATOM   2476  OG1 THR B 437      -8.259  -8.190 -31.681  1.00 28.27           O  
+ATOM   2477  CG2 THR B 437      -7.316  -6.307 -30.498  1.00 34.21           C  
+ATOM   2478  H   THR B 437     -10.021  -9.032 -29.804  1.00 22.94           H  
+ATOM   2479  HA  THR B 437      -7.468  -8.761 -29.308  1.00 25.64           H  
+ATOM   2480  HB  THR B 437      -9.261  -6.946 -30.505  1.00 30.81           H  
+ATOM   2481  HG1 THR B 437      -7.523  -8.594 -31.670  1.00 33.92           H  
+ATOM   2482 HG21 THR B 437      -6.471  -6.684 -30.207  1.00 41.05           H  
+ATOM   2483 HG22 THR B 437      -7.209  -5.945 -31.392  1.00 41.05           H  
+ATOM   2484 HG23 THR B 437      -7.565  -5.588 -29.896  1.00 41.05           H  
+ATOM   2485  N   TYR B 438      -9.398  -6.901 -27.559  1.00 19.05           N  
+ATOM   2486  CA  TYR B 438      -9.415  -5.984 -26.427  1.00 19.86           C  
+ATOM   2487  C   TYR B 438      -9.443  -6.672 -25.075  1.00 19.15           C  
+ATOM   2488  O   TYR B 438      -8.902  -6.121 -24.105  1.00 18.42           O  
+ATOM   2489  CB  TYR B 438     -10.614  -5.049 -26.561  1.00 19.23           C  
+ATOM   2490  CG  TYR B 438     -10.454  -4.115 -27.712  1.00 15.63           C  
+ATOM   2491  CD1 TYR B 438      -9.732  -2.929 -27.571  1.00 17.23           C  
+ATOM   2492  CD2 TYR B 438     -10.964  -4.417 -28.961  1.00 19.98           C  
+ATOM   2493  CE1 TYR B 438      -9.556  -2.068 -28.612  1.00 21.18           C  
+ATOM   2494  CE2 TYR B 438     -10.784  -3.554 -30.024  1.00 17.29           C  
+ATOM   2495  CZ  TYR B 438     -10.065  -2.385 -29.848  1.00 20.58           C  
+ATOM   2496  OH  TYR B 438      -9.868  -1.491 -30.870  1.00 24.50           O  
+ATOM   2497  H   TYR B 438     -10.170  -7.076 -27.896  1.00 22.86           H  
+ATOM   2498  HA  TYR B 438      -8.603  -5.454 -26.443  1.00 23.84           H  
+ATOM   2499  HB2 TYR B 438     -11.417  -5.575 -26.704  1.00 23.07           H  
+ATOM   2500  HB3 TYR B 438     -10.703  -4.523 -25.751  1.00 23.07           H  
+ATOM   2501  HD1 TYR B 438      -9.360  -2.721 -26.744  1.00 20.67           H  
+ATOM   2502  HD2 TYR B 438     -11.433  -5.210 -29.087  1.00 23.98           H  
+ATOM   2503  HE1 TYR B 438      -9.094  -1.270 -28.487  1.00 25.42           H  
+ATOM   2504  HE2 TYR B 438     -11.145  -3.758 -30.856  1.00 20.74           H  
+ATOM   2505  HH  TYR B 438     -10.245  -1.766 -31.569  1.00 29.40           H  
+ATOM   2506  N   TYR B 439     -10.050  -7.857 -24.970  1.00 18.41           N  
+ATOM   2507  CA  TYR B 439     -10.167  -8.558 -23.692  1.00 20.64           C  
+ATOM   2508  C   TYR B 439      -9.851 -10.039 -23.888  1.00 22.41           C  
+ATOM   2509  O   TYR B 439     -10.696 -10.911 -23.656  1.00 21.33           O  
+ATOM   2510  CB  TYR B 439     -11.557  -8.389 -23.089  1.00 19.53           C  
+ATOM   2511  CG  TYR B 439     -12.126  -6.991 -23.173  1.00 18.73           C  
+ATOM   2512  CD1 TYR B 439     -11.589  -5.956 -22.439  1.00 19.66           C  
+ATOM   2513  CD2 TYR B 439     -13.224  -6.733 -23.979  1.00 16.92           C  
+ATOM   2514  CE1 TYR B 439     -12.121  -4.669 -22.517  1.00 13.36           C  
+ATOM   2515  CE2 TYR B 439     -13.764  -5.484 -24.055  1.00 17.00           C  
+ATOM   2516  CZ  TYR B 439     -13.214  -4.457 -23.321  1.00 12.87           C  
+ATOM   2517  OH  TYR B 439     -13.805  -3.208 -23.444  1.00 15.90           O  
+ATOM   2518  H   TYR B 439     -10.404  -8.277 -25.631  1.00 22.10           H  
+ATOM   2519  HA  TYR B 439      -9.518  -8.177 -23.081  1.00 24.77           H  
+ATOM   2520  HB2 TYR B 439     -12.168  -8.980 -23.556  1.00 23.44           H  
+ATOM   2521  HB3 TYR B 439     -11.516  -8.630 -22.150  1.00 23.44           H  
+ATOM   2522  HD1 TYR B 439     -10.861  -6.118 -21.883  1.00 23.59           H  
+ATOM   2523  HD2 TYR B 439     -13.599  -7.424 -24.477  1.00 20.30           H  
+ATOM   2524  HE1 TYR B 439     -11.744  -3.969 -22.035  1.00 16.03           H  
+ATOM   2525  HE2 TYR B 439     -14.501  -5.325 -24.600  1.00 20.40           H  
+ATOM   2526  HH  TYR B 439     -13.397  -2.649 -22.967  1.00 19.08           H  
+ATOM   2527  N   PRO B 440      -8.623 -10.350 -24.288  1.00 24.94           N  
+ATOM   2528  CA  PRO B 440      -8.234 -11.753 -24.478  1.00 28.36           C  
+ATOM   2529  C   PRO B 440      -8.465 -12.584 -23.224  1.00 28.02           C  
+ATOM   2530  O   PRO B 440      -8.170 -12.162 -22.106  1.00 29.25           O  
+ATOM   2531  CB  PRO B 440      -6.742 -11.659 -24.833  1.00 28.07           C  
+ATOM   2532  CG  PRO B 440      -6.306 -10.292 -24.349  1.00 28.73           C  
+ATOM   2533  CD  PRO B 440      -7.510  -9.425 -24.560  1.00 22.97           C  
+ATOM   2534  HA  PRO B 440      -8.727 -12.145 -25.216  1.00 34.03           H  
+ATOM   2535  HB2 PRO B 440      -6.251 -12.361 -24.379  1.00 33.69           H  
+ATOM   2536  HB3 PRO B 440      -6.626 -11.740 -25.793  1.00 33.69           H  
+ATOM   2537  HG2 PRO B 440      -6.065 -10.332 -23.410  1.00 34.48           H  
+ATOM   2538  HG3 PRO B 440      -5.552  -9.977 -24.872  1.00 34.48           H  
+ATOM   2539  HD2 PRO B 440      -7.516  -8.680 -23.939  1.00 27.57           H  
+ATOM   2540  HD3 PRO B 440      -7.546  -9.096 -25.472  1.00 27.57           H  
+ATOM   2541  N   GLY B 441      -9.034 -13.771 -23.423  1.00 27.22           N  
+ATOM   2542  CA  GLY B 441      -9.243 -14.671 -22.307  1.00 32.90           C  
+ATOM   2543  C   GLY B 441     -10.307 -14.260 -21.317  1.00 29.44           C  
+ATOM   2544  O   GLY B 441     -10.319 -14.765 -20.195  1.00 35.23           O  
+ATOM   2545  H   GLY B 441      -9.301 -14.069 -24.184  1.00 32.67           H  
+ATOM   2546  HA2 GLY B 441      -9.491 -15.540 -22.657  1.00 39.48           H  
+ATOM   2547  HA3 GLY B 441      -8.408 -14.753 -21.820  1.00 39.48           H  
+ATOM   2548  N   ALA B 442     -11.218 -13.369 -21.706  1.00 27.33           N  
+ATOM   2549  CA  ALA B 442     -12.295 -12.953 -20.822  1.00 24.51           C  
+ATOM   2550  C   ALA B 442     -13.205 -14.118 -20.454  1.00 24.19           C  
+ATOM   2551  O   ALA B 442     -13.468 -15.003 -21.272  1.00 28.64           O  
+ATOM   2552  CB  ALA B 442     -13.121 -11.857 -21.502  1.00 21.09           C  
+ATOM   2553  H   ALA B 442     -11.233 -12.992 -22.479  1.00 32.79           H  
+ATOM   2554  HA  ALA B 442     -11.911 -12.608 -20.000  1.00 29.41           H  
+ATOM   2555  HB1 ALA B 442     -13.831 -11.578 -20.902  1.00 25.31           H  
+ATOM   2556  HB2 ALA B 442     -12.543 -11.104 -21.703  1.00 25.31           H  
+ATOM   2557  HB3 ALA B 442     -13.501 -12.210 -22.321  1.00 25.31           H  
+ATOM   2558  N   ASP B 443     -13.713 -14.103 -19.218  1.00 26.19           N  
+ATOM   2559  CA  ASP B 443     -14.659 -15.123 -18.787  1.00 25.75           C  
+ATOM   2560  C   ASP B 443     -16.095 -14.648 -18.992  1.00 23.98           C  
+ATOM   2561  O   ASP B 443     -16.357 -13.544 -19.493  1.00 19.88           O  
+ATOM   2562  CB  ASP B 443     -14.406 -15.545 -17.330  1.00 26.32           C  
+ATOM   2563  CG  ASP B 443     -14.668 -14.437 -16.309  1.00 30.11           C  
+ATOM   2564  OD1 ASP B 443     -15.169 -13.356 -16.671  1.00 30.68           O  
+ATOM   2565  OD2 ASP B 443     -14.365 -14.657 -15.108  1.00 33.68           O  
+ATOM   2566  H   ASP B 443     -13.523 -13.515 -18.620  1.00 31.43           H  
+ATOM   2567  HA  ASP B 443     -14.520 -15.906 -19.342  1.00 30.90           H  
+ATOM   2568  HB2 ASP B 443     -14.992 -16.289 -17.115  1.00 31.58           H  
+ATOM   2569  HB3 ASP B 443     -13.480 -15.817 -17.240  1.00 31.58           H  
+ATOM   2570  N   ALA B 444     -17.050 -15.502 -18.616  1.00 21.49           N  
+ATOM   2571  CA  ALA B 444     -18.457 -15.201 -18.850  1.00 21.12           C  
+ATOM   2572  C   ALA B 444     -18.876 -13.931 -18.132  1.00 19.06           C  
+ATOM   2573  O   ALA B 444     -19.715 -13.170 -18.628  1.00 19.07           O  
+ATOM   2574  CB  ALA B 444     -19.343 -16.365 -18.395  1.00 25.16           C  
+ATOM   2575  H   ALA B 444     -16.908 -16.256 -18.226  1.00 25.79           H  
+ATOM   2576  HA  ALA B 444     -18.582 -15.079 -19.804  1.00 25.34           H  
+ATOM   2577  HB1 ALA B 444     -20.270 -16.145 -18.576  1.00 30.19           H  
+ATOM   2578  HB2 ALA B 444     -19.091 -17.164 -18.883  1.00 30.19           H  
+ATOM   2579  HB3 ALA B 444     -19.216 -16.505 -17.443  1.00 30.19           H  
+ATOM   2580  N   ARG B 445     -18.339 -13.707 -16.930  1.00 19.85           N  
+ATOM   2581  CA  ARG B 445     -18.739 -12.526 -16.184  1.00 21.01           C  
+ATOM   2582  C   ARG B 445     -18.272 -11.254 -16.881  1.00 17.95           C  
+ATOM   2583  O   ARG B 445     -19.030 -10.273 -16.964  1.00 17.07           O  
+ATOM   2584  CB  ARG B 445     -18.187 -12.604 -14.768  1.00 21.38           C  
+ATOM   2585  CG  ARG B 445     -18.547 -11.397 -13.976  1.00 23.90           C  
+ATOM   2586  CD  ARG B 445     -18.611 -11.677 -12.499  1.00 33.34           C  
+ATOM   2587  NE  ARG B 445     -18.945 -10.431 -11.833  1.00 46.54           N  
+ATOM   2588  CZ  ARG B 445     -18.053  -9.523 -11.465  1.00 27.41           C  
+ATOM   2589  NH1 ARG B 445     -16.753  -9.772 -11.517  1.00 31.62           N  
+ATOM   2590  NH2 ARG B 445     -18.478  -8.343 -11.041  1.00 29.26           N  
+ATOM   2591  H   ARG B 445     -17.761 -14.211 -16.541  1.00 23.82           H  
+ATOM   2592  HA  ARG B 445     -19.707 -12.494 -16.127  1.00 25.21           H  
+ATOM   2593  HB2 ARG B 445     -18.555 -13.383 -14.323  1.00 25.66           H  
+ATOM   2594  HB3 ARG B 445     -17.220 -12.669 -14.804  1.00 25.66           H  
+ATOM   2595  HG2 ARG B 445     -17.879 -10.709 -14.123  1.00 28.68           H  
+ATOM   2596  HG3 ARG B 445     -19.419 -11.079 -14.259  1.00 28.68           H  
+ATOM   2597  HD2 ARG B 445     -19.297 -12.337 -12.312  1.00 40.00           H  
+ATOM   2598  HD3 ARG B 445     -17.751 -11.993 -12.180  1.00 40.00           H  
+ATOM   2599  HE  ARG B 445     -19.773 -10.273 -11.666  1.00 55.85           H  
+ATOM   2600 HH11 ARG B 445     -16.472 -10.537 -11.794  1.00 37.95           H  
+ATOM   2601 HH12 ARG B 445     -16.189  -9.169 -11.274  1.00 37.95           H  
+ATOM   2602 HH21 ARG B 445     -19.321  -8.176 -11.008  1.00 35.11           H  
+ATOM   2603 HH22 ARG B 445     -17.911  -7.743 -10.799  1.00 35.11           H  
+ATOM   2604  N   MET B 446     -17.030 -11.253 -17.367  1.00 18.90           N  
+ATOM   2605  CA  MET B 446     -16.519 -10.102 -18.105  1.00 16.34           C  
+ATOM   2606  C   MET B 446     -17.357  -9.843 -19.343  1.00 16.92           C  
+ATOM   2607  O   MET B 446     -17.663  -8.689 -19.672  1.00 15.78           O  
+ATOM   2608  CB  MET B 446     -15.071 -10.316 -18.522  1.00 18.19           C  
+ATOM   2609  CG  MET B 446     -14.040 -10.202 -17.431  1.00 29.18           C  
+ATOM   2610  SD  MET B 446     -12.387 -10.385 -18.160  1.00 33.44           S  
+ATOM   2611  CE  MET B 446     -12.318  -8.892 -19.137  1.00 32.33           C  
+ATOM   2612  H   MET B 446     -16.469 -11.899 -17.283  1.00 22.68           H  
+ATOM   2613  HA  MET B 446     -16.548  -9.335 -17.511  1.00 19.61           H  
+ATOM   2614  HB2 MET B 446     -14.993 -11.208 -18.896  1.00 21.83           H  
+ATOM   2615  HB3 MET B 446     -14.848  -9.654 -19.195  1.00 21.83           H  
+ATOM   2616  HG2 MET B 446     -14.103  -9.333 -17.006  1.00 35.02           H  
+ATOM   2617  HG3 MET B 446     -14.175 -10.903 -16.775  1.00 35.02           H  
+ATOM   2618  HE1 MET B 446     -11.402  -8.741 -19.418  1.00 38.79           H  
+ATOM   2619  HE2 MET B 446     -12.889  -8.997 -19.914  1.00 38.79           H  
+ATOM   2620  HE3 MET B 446     -12.626  -8.147 -18.598  1.00 38.79           H  
+ATOM   2621  N   LYS B 447     -17.698 -10.910 -20.074  1.00 17.40           N  
+ATOM   2622  CA  LYS B 447     -18.495 -10.752 -21.287  1.00 15.28           C  
+ATOM   2623  C   LYS B 447     -19.885 -10.221 -20.966  1.00 14.08           C  
+ATOM   2624  O   LYS B 447     -20.427  -9.385 -21.704  1.00 13.00           O  
+ATOM   2625  CB  LYS B 447     -18.586 -12.094 -22.017  1.00 13.05           C  
+ATOM   2626  CG  LYS B 447     -17.274 -12.526 -22.613  1.00 16.37           C  
+ATOM   2627  CD  LYS B 447     -17.334 -13.956 -23.139  1.00 20.50           C  
+ATOM   2628  CE  LYS B 447     -16.007 -14.359 -23.709  1.00 25.56           C  
+ATOM   2629  NZ  LYS B 447     -16.156 -15.675 -24.389  1.00 32.35           N  
+ATOM   2630  H   LYS B 447     -17.484 -11.723 -19.890  1.00 20.88           H  
+ATOM   2631  HA  LYS B 447     -18.062 -10.114 -21.874  1.00 18.34           H  
+ATOM   2632  HB2 LYS B 447     -18.869 -12.776 -21.388  1.00 15.66           H  
+ATOM   2633  HB3 LYS B 447     -19.232 -12.018 -22.737  1.00 15.66           H  
+ATOM   2634  HG2 LYS B 447     -17.050 -11.939 -23.353  1.00 19.65           H  
+ATOM   2635  HG3 LYS B 447     -16.583 -12.481 -21.934  1.00 19.65           H  
+ATOM   2636  HD2 LYS B 447     -17.556 -14.561 -22.414  1.00 24.60           H  
+ATOM   2637  HD3 LYS B 447     -18.003 -14.018 -23.839  1.00 24.60           H  
+ATOM   2638  HE2 LYS B 447     -15.710 -13.701 -24.357  1.00 30.67           H  
+ATOM   2639  HE3 LYS B 447     -15.352 -14.443 -22.998  1.00 30.67           H  
+ATOM   2640  HZ1 LYS B 447     -15.376 -15.929 -24.735  1.00 38.82           H  
+ATOM   2641  HZ2 LYS B 447     -16.426 -16.290 -23.805  1.00 38.82           H  
+ATOM   2642  HZ3 LYS B 447     -16.756 -15.614 -25.043  1.00 38.82           H  
+ATOM   2643  N   LYS B 448     -20.490 -10.704 -19.879  1.00 14.45           N  
+ATOM   2644  CA  LYS B 448     -21.793 -10.199 -19.480  1.00 12.67           C  
+ATOM   2645  C   LYS B 448     -21.723  -8.713 -19.172  1.00 12.54           C  
+ATOM   2646  O   LYS B 448     -22.548  -7.925 -19.653  1.00 13.91           O  
+ATOM   2647  CB  LYS B 448     -22.316 -10.982 -18.270  1.00 15.78           C  
+ATOM   2648  CG  LYS B 448     -23.652 -10.503 -17.819  1.00 18.93           C  
+ATOM   2649  CD  LYS B 448     -24.356 -11.512 -16.928  1.00 28.13           C  
+ATOM   2650  CE  LYS B 448     -25.450 -10.834 -16.125  1.00 41.36           C  
+ATOM   2651  NZ  LYS B 448     -26.482 -11.808 -15.685  1.00 53.21           N  
+ATOM   2652  H   LYS B 448     -20.168 -11.315 -19.366  1.00 17.34           H  
+ATOM   2653  HA  LYS B 448     -22.418 -10.331 -20.210  1.00 15.21           H  
+ATOM   2654  HB2 LYS B 448     -22.395 -11.919 -18.508  1.00 18.94           H  
+ATOM   2655  HB3 LYS B 448     -21.694 -10.878 -17.532  1.00 18.94           H  
+ATOM   2656  HG2 LYS B 448     -23.543  -9.681 -17.316  1.00 22.72           H  
+ATOM   2657  HG3 LYS B 448     -24.211 -10.345 -18.596  1.00 22.72           H  
+ATOM   2658  HD2 LYS B 448     -24.758 -12.205 -17.475  1.00 33.76           H  
+ATOM   2659  HD3 LYS B 448     -23.717 -11.904 -16.312  1.00 33.76           H  
+ATOM   2660  HE2 LYS B 448     -25.062 -10.423 -15.337  1.00 49.63           H  
+ATOM   2661  HE3 LYS B 448     -25.880 -10.160 -16.673  1.00 49.63           H  
+ATOM   2662  HZ1 LYS B 448     -27.105 -11.395 -15.202  1.00 63.85           H  
+ATOM   2663  HZ2 LYS B 448     -26.868 -12.184 -16.394  1.00 63.85           H  
+ATOM   2664  HZ3 LYS B 448     -26.108 -12.445 -15.189  1.00 63.85           H  
+ATOM   2665  N   LEU B 449     -20.739  -8.309 -18.365  1.00 13.86           N  
+ATOM   2666  CA  LEU B 449     -20.620  -6.896 -18.031  1.00 13.23           C  
+ATOM   2667  C   LEU B 449     -20.380  -6.042 -19.268  1.00 12.98           C  
+ATOM   2668  O   LEU B 449     -20.981  -4.969 -19.410  1.00 12.47           O  
+ATOM   2669  CB  LEU B 449     -19.502  -6.682 -17.012  1.00 12.40           C  
+ATOM   2670  CG  LEU B 449     -19.785  -7.181 -15.587  1.00 14.51           C  
+ATOM   2671  CD1 LEU B 449     -18.480  -7.248 -14.817  1.00 13.37           C  
+ATOM   2672  CD2 LEU B 449     -20.801  -6.265 -14.939  1.00 14.84           C  
+ATOM   2673  H   LEU B 449     -20.146  -8.821 -18.010  1.00 16.63           H  
+ATOM   2674  HA  LEU B 449     -21.454  -6.610 -17.629  1.00 15.87           H  
+ATOM   2675  HB2 LEU B 449     -18.712  -7.148 -17.327  1.00 14.88           H  
+ATOM   2676  HB3 LEU B 449     -19.325  -5.730 -16.953  1.00 14.88           H  
+ATOM   2677  HG  LEU B 449     -20.163  -8.075 -15.584  1.00 17.41           H  
+ATOM   2678 HD11 LEU B 449     -18.662  -7.540 -13.910  1.00 16.04           H  
+ATOM   2679 HD12 LEU B 449     -17.887  -7.879 -15.255  1.00 16.04           H  
+ATOM   2680 HD13 LEU B 449     -18.075  -6.367 -14.806  1.00 16.04           H  
+ATOM   2681 HD21 LEU B 449     -20.914  -6.524 -14.011  1.00 17.81           H  
+ATOM   2682 HD22 LEU B 449     -20.480  -5.351 -14.991  1.00 17.81           H  
+ATOM   2683 HD23 LEU B 449     -21.645  -6.346 -15.410  1.00 17.81           H  
+ATOM   2684  N   PHE B 450     -19.508  -6.495 -20.174  1.00 11.47           N  
+ATOM   2685  CA  PHE B 450     -19.245  -5.714 -21.379  1.00 11.34           C  
+ATOM   2686  C   PHE B 450     -20.529  -5.518 -22.178  1.00 12.82           C  
+ATOM   2687  O   PHE B 450     -20.799  -4.427 -22.695  1.00 11.99           O  
+ATOM   2688  CB  PHE B 450     -18.165  -6.369 -22.254  1.00 11.98           C  
+ATOM   2689  CG  PHE B 450     -17.972  -5.650 -23.558  1.00 13.09           C  
+ATOM   2690  CD1 PHE B 450     -17.204  -4.504 -23.612  1.00 13.13           C  
+ATOM   2691  CD2 PHE B 450     -18.594  -6.088 -24.713  1.00 13.85           C  
+ATOM   2692  CE1 PHE B 450     -17.057  -3.804 -24.793  1.00 13.42           C  
+ATOM   2693  CE2 PHE B 450     -18.449  -5.410 -25.905  1.00 12.98           C  
+ATOM   2694  CZ  PHE B 450     -17.670  -4.252 -25.938  1.00 12.87           C  
+ATOM   2695  H   PHE B 450     -19.068  -7.232 -20.115  1.00 13.77           H  
+ATOM   2696  HA  PHE B 450     -18.900  -4.849 -21.109  1.00 13.60           H  
+ATOM   2697  HB2 PHE B 450     -17.321  -6.360 -21.777  1.00 14.37           H  
+ATOM   2698  HB3 PHE B 450     -18.426  -7.283 -22.450  1.00 14.37           H  
+ATOM   2699  HD1 PHE B 450     -16.778  -4.200 -22.843  1.00 15.75           H  
+ATOM   2700  HD2 PHE B 450     -19.120  -6.855 -24.685  1.00 16.62           H  
+ATOM   2701  HE1 PHE B 450     -16.544  -3.028 -24.813  1.00 16.10           H  
+ATOM   2702  HE2 PHE B 450     -18.865  -5.720 -26.677  1.00 15.57           H  
+ATOM   2703  HZ  PHE B 450     -17.566  -3.784 -26.735  1.00 15.44           H  
+ATOM   2704  N   GLY B 451     -21.346  -6.568 -22.282  1.00 12.80           N  
+ATOM   2705  CA  GLY B 451     -22.624  -6.428 -22.952  1.00 12.53           C  
+ATOM   2706  C   GLY B 451     -23.531  -5.405 -22.294  1.00 13.55           C  
+ATOM   2707  O   GLY B 451     -24.238  -4.660 -22.977  1.00 12.60           O  
+ATOM   2708  H   GLY B 451     -21.183  -7.355 -21.976  1.00 15.35           H  
+ATOM   2709  HA2 GLY B 451     -22.474  -6.153 -23.870  1.00 15.04           H  
+ATOM   2710  HA3 GLY B 451     -23.081  -7.284 -22.950  1.00 15.04           H  
+ATOM   2711  N   GLU B 452     -23.527  -5.361 -20.957  1.00 13.88           N  
+ATOM   2712  CA  GLU B 452     -24.393  -4.449 -20.235  1.00 11.61           C  
+ATOM   2713  C   GLU B 452     -23.976  -2.989 -20.373  1.00 10.67           C  
+ATOM   2714  O   GLU B 452     -24.805  -2.107 -20.145  1.00 12.75           O  
+ATOM   2715  CB  GLU B 452     -24.434  -4.835 -18.749  1.00 16.10           C  
+ATOM   2716  CG  GLU B 452     -25.187  -6.129 -18.471  1.00 16.84           C  
+ATOM   2717  CD  GLU B 452     -26.680  -5.939 -18.305  1.00 24.61           C  
+ATOM   2718  OE1 GLU B 452     -27.315  -5.313 -19.165  1.00 29.46           O  
+ATOM   2719  OE2 GLU B 452     -27.225  -6.413 -17.287  1.00 41.61           O  
+ATOM   2720  H   GLU B 452     -23.030  -5.850 -20.454  1.00 16.66           H  
+ATOM   2721  HA  GLU B 452     -25.288  -4.530 -20.600  1.00 13.93           H  
+ATOM   2722  HB2 GLU B 452     -23.524  -4.948 -18.432  1.00 19.32           H  
+ATOM   2723  HB3 GLU B 452     -24.872  -4.125 -18.255  1.00 19.32           H  
+ATOM   2724  HG2 GLU B 452     -25.046  -6.738 -19.212  1.00 20.21           H  
+ATOM   2725  HG3 GLU B 452     -24.845  -6.519 -17.651  1.00 20.21           H  
+ATOM   2726  N   LEU B 453     -22.726  -2.715 -20.756  1.00 11.65           N  
+ATOM   2727  CA  LEU B 453     -22.308  -1.348 -21.047  1.00 10.60           C  
+ATOM   2728  C   LEU B 453     -23.132  -0.709 -22.154  1.00 11.63           C  
+ATOM   2729  O   LEU B 453     -23.190   0.524 -22.242  1.00 12.53           O  
+ATOM   2730  CB  LEU B 453     -20.843  -1.311 -21.465  1.00 11.12           C  
+ATOM   2731  CG  LEU B 453     -19.788  -1.739 -20.447  1.00 12.50           C  
+ATOM   2732  CD1 LEU B 453     -18.453  -1.817 -21.121  1.00 13.88           C  
+ATOM   2733  CD2 LEU B 453     -19.775  -0.748 -19.279  1.00 13.88           C  
+ATOM   2734  H   LEU B 453     -22.105  -3.302 -20.855  1.00 13.98           H  
+ATOM   2735  HA  LEU B 453     -22.416  -0.833 -20.232  1.00 12.72           H  
+ATOM   2736  HB2 LEU B 453     -20.742  -1.897 -22.232  1.00 13.34           H  
+ATOM   2737  HB3 LEU B 453     -20.633  -0.398 -21.716  1.00 13.34           H  
+ATOM   2738  HG  LEU B 453     -19.990  -2.616 -20.086  1.00 15.00           H  
+ATOM   2739 HD11 LEU B 453     -17.783  -2.071 -20.466  1.00 16.66           H  
+ATOM   2740 HD12 LEU B 453     -18.494  -2.481 -21.827  1.00 16.66           H  
+ATOM   2741 HD13 LEU B 453     -18.236  -0.949 -21.495  1.00 16.66           H  
+ATOM   2742 HD21 LEU B 453     -19.048  -0.976 -18.679  1.00 16.66           H  
+ATOM   2743 HD22 LEU B 453     -19.648   0.149 -19.626  1.00 16.66           H  
+ATOM   2744 HD23 LEU B 453     -20.622  -0.803 -18.808  1.00 16.66           H  
+ATOM   2745  N   ASN B 454     -23.755  -1.526 -22.996  1.00 12.86           N  
+ATOM   2746  CA  ASN B 454     -24.567  -1.052 -24.101  1.00 11.33           C  
+ATOM   2747  C   ASN B 454     -26.061  -1.237 -23.849  1.00 15.10           C  
+ATOM   2748  O   ASN B 454     -26.861  -1.121 -24.781  1.00 17.60           O  
+ATOM   2749  CB  ASN B 454     -24.138  -1.779 -25.374  1.00 14.90           C  
+ATOM   2750  CG  ASN B 454     -24.531  -1.039 -26.626  1.00 17.34           C  
+ATOM   2751  OD1 ASN B 454     -24.494   0.179 -26.681  1.00 16.19           O  
+ATOM   2752  ND2 ASN B 454     -24.918  -1.788 -27.651  1.00 19.35           N  
+ATOM   2753  H   ASN B 454     -23.719  -2.384 -22.943  1.00 15.43           H  
+ATOM   2754  HA  ASN B 454     -24.422  -0.100 -24.221  1.00 13.59           H  
+ATOM   2755  HB2 ASN B 454     -23.172  -1.875 -25.374  1.00 17.88           H  
+ATOM   2756  HB3 ASN B 454     -24.558  -2.652 -25.397  1.00 17.88           H  
+ATOM   2757 HD21 ASN B 454     -25.154  -1.418 -28.390  1.00 23.22           H  
+ATOM   2758 HD22 ASN B 454     -24.933  -2.645 -27.575  1.00 23.22           H  
+ATOM   2759  N   ASN B 455     -26.466  -1.492 -22.605  1.00 14.69           N  
+ATOM   2760  CA  ASN B 455     -27.872  -1.746 -22.291  1.00 12.93           C  
+ATOM   2761  C   ASN B 455     -28.517  -0.423 -21.891  1.00 16.83           C  
+ATOM   2762  O   ASN B 455     -28.316   0.070 -20.778  1.00 16.40           O  
+ATOM   2763  CB  ASN B 455     -28.013  -2.799 -21.194  1.00 15.74           C  
+ATOM   2764  CG  ASN B 455     -29.458  -3.131 -20.892  1.00 16.20           C  
+ATOM   2765  OD1 ASN B 455     -30.378  -2.470 -21.391  1.00 18.92           O  
+ATOM   2766  ND2 ASN B 455     -29.671  -4.139 -20.052  1.00 18.98           N  
+ATOM   2767  H   ASN B 455     -25.943  -1.524 -21.923  1.00 17.63           H  
+ATOM   2768  HA  ASN B 455     -28.320  -2.080 -23.084  1.00 15.51           H  
+ATOM   2769  HB2 ASN B 455     -27.569  -3.613 -21.477  1.00 18.89           H  
+ATOM   2770  HB3 ASN B 455     -27.604  -2.465 -20.380  1.00 18.89           H  
+ATOM   2771 HD21 ASN B 455     -30.475  -4.367 -19.849  1.00 22.78           H  
+ATOM   2772 HD22 ASN B 455     -29.004  -4.564 -19.712  1.00 22.78           H  
+ATOM   2773  N   GLU B 456     -29.305   0.155 -22.799  1.00 18.97           N  
+ATOM   2774  CA  GLU B 456     -29.940   1.445 -22.561  1.00 15.57           C  
+ATOM   2775  C   GLU B 456     -31.142   1.378 -21.633  1.00 16.14           C  
+ATOM   2776  O   GLU B 456     -31.673   2.435 -21.285  1.00 21.18           O  
+ATOM   2777  CB  GLU B 456     -30.336   2.085 -23.911  1.00 21.58           C  
+ATOM   2778  CG  GLU B 456     -29.105   2.447 -24.757  1.00 22.96           C  
+ATOM   2779  CD  GLU B 456     -29.423   3.051 -26.110  1.00 35.31           C  
+ATOM   2780  OE1 GLU B 456     -30.613   3.268 -26.405  1.00 32.88           O  
+ATOM   2781  OE2 GLU B 456     -28.461   3.311 -26.874  1.00 27.84           O  
+ATOM   2782  H   GLU B 456     -29.486  -0.186 -23.568  1.00 22.77           H  
+ATOM   2783  HA  GLU B 456     -29.297   2.029 -22.130  1.00 18.68           H  
+ATOM   2784  HB2 GLU B 456     -30.877   1.457 -24.415  1.00 25.89           H  
+ATOM   2785  HB3 GLU B 456     -30.839   2.897 -23.744  1.00 25.89           H  
+ATOM   2786  HG2 GLU B 456     -28.573   3.093 -24.267  1.00 27.55           H  
+ATOM   2787  HG3 GLU B 456     -28.588   1.640 -24.911  1.00 27.55           H  
+ATOM   2788  N   ALA B 457     -31.544   0.192 -21.197  1.00 17.27           N  
+ATOM   2789  CA  ALA B 457     -32.611   0.021 -20.221  1.00 18.96           C  
+ATOM   2790  C   ALA B 457     -32.132   0.112 -18.784  1.00 21.42           C  
+ATOM   2791  O   ALA B 457     -32.963   0.198 -17.875  1.00 21.02           O  
+ATOM   2792  CB  ALA B 457     -33.300  -1.329 -20.410  1.00 19.88           C  
+ATOM   2793  H   ALA B 457     -31.204  -0.553 -21.459  1.00 20.72           H  
+ATOM   2794  HA  ALA B 457     -33.263   0.723 -20.373  1.00 22.75           H  
+ATOM   2795  HB1 ALA B 457     -34.004  -1.419 -19.749  1.00 23.86           H  
+ATOM   2796  HB2 ALA B 457     -33.677  -1.369 -21.302  1.00 23.86           H  
+ATOM   2797  HB3 ALA B 457     -32.646  -2.036 -20.295  1.00 23.86           H  
+ATOM   2798  N   LEU B 458     -30.823   0.053 -18.557  1.00 17.06           N  
+ATOM   2799  CA  LEU B 458     -30.328   0.110 -17.187  1.00 15.73           C  
+ATOM   2800  C   LEU B 458     -30.547   1.491 -16.597  1.00 15.39           C  
+ATOM   2801  O   LEU B 458     -30.442   2.514 -17.275  1.00 17.67           O  
+ATOM   2802  CB  LEU B 458     -28.841  -0.222 -17.132  1.00 15.07           C  
+ATOM   2803  CG  LEU B 458     -28.438  -1.619 -17.548  1.00 13.40           C  
+ATOM   2804  CD1 LEU B 458     -26.917  -1.799 -17.409  1.00 17.38           C  
+ATOM   2805  CD2 LEU B 458     -29.180  -2.692 -16.786  1.00 17.04           C  
+ATOM   2806  H   LEU B 458     -30.217  -0.018 -19.163  1.00 20.47           H  
+ATOM   2807  HA  LEU B 458     -30.809  -0.542 -16.655  1.00 18.88           H  
+ATOM   2808  HB2 LEU B 458     -28.375   0.394 -17.718  1.00 18.08           H  
+ATOM   2809  HB3 LEU B 458     -28.542  -0.101 -16.217  1.00 18.08           H  
+ATOM   2810  HG  LEU B 458     -28.682  -1.732 -18.480  1.00 16.08           H  
+ATOM   2811 HD11 LEU B 458     -26.681  -2.701 -17.675  1.00 20.86           H  
+ATOM   2812 HD12 LEU B 458     -26.469  -1.157 -17.982  1.00 20.86           H  
+ATOM   2813 HD13 LEU B 458     -26.665  -1.650 -16.485  1.00 20.86           H  
+ATOM   2814 HD21 LEU B 458     -28.792  -3.555 -16.997  1.00 20.45           H  
+ATOM   2815 HD22 LEU B 458     -29.100  -2.516 -15.835  1.00 20.45           H  
+ATOM   2816 HD23 LEU B 458     -30.114  -2.676 -17.048  1.00 20.45           H  
+ATOM   2817  N   SER B 459     -30.827   1.510 -15.293  1.00 16.44           N  
+ATOM   2818  CA  SER B 459     -30.882   2.758 -14.559  1.00 12.44           C  
+ATOM   2819  C   SER B 459     -29.488   3.358 -14.435  1.00 12.58           C  
+ATOM   2820  O   SER B 459     -28.482   2.699 -14.728  1.00 14.37           O  
+ATOM   2821  CB  SER B 459     -31.430   2.526 -13.154  1.00 15.20           C  
+ATOM   2822  OG  SER B 459     -30.500   1.780 -12.403  1.00 17.81           O  
+ATOM   2823  H   SER B 459     -30.987   0.812 -14.818  1.00 19.72           H  
+ATOM   2824  HA  SER B 459     -31.462   3.372 -15.035  1.00 14.93           H  
+ATOM   2825  HB2 SER B 459     -31.579   3.381 -12.722  1.00 18.24           H  
+ATOM   2826  HB3 SER B 459     -32.264   2.034 -13.212  1.00 18.24           H  
+ATOM   2827  HG  SER B 459     -30.802   1.636 -11.632  1.00 21.37           H  
+ATOM   2828  N   ILE B 460     -29.442   4.607 -13.962  1.00 15.19           N  
+ATOM   2829  CA  ILE B 460     -28.163   5.261 -13.710  1.00 12.32           C  
+ATOM   2830  C   ILE B 460     -27.292   4.396 -12.806  1.00 11.53           C  
+ATOM   2831  O   ILE B 460     -26.120   4.137 -13.107  1.00 12.75           O  
+ATOM   2832  CB  ILE B 460     -28.373   6.660 -13.103  1.00 16.38           C  
+ATOM   2833  CG1 ILE B 460     -28.841   7.629 -14.192  1.00 22.88           C  
+ATOM   2834  CG2 ILE B 460     -27.102   7.153 -12.426  1.00 18.49           C  
+ATOM   2835  CD1 ILE B 460     -29.121   9.026 -13.669  1.00 25.77           C  
+ATOM   2836  H   ILE B 460     -30.131   5.090 -13.782  1.00 18.23           H  
+ATOM   2837  HA  ILE B 460     -27.708   5.368 -14.560  1.00 14.78           H  
+ATOM   2838  HB  ILE B 460     -29.061   6.607 -12.422  1.00 19.66           H  
+ATOM   2839 HG12 ILE B 460     -28.150   7.697 -14.869  1.00 27.45           H  
+ATOM   2840 HG13 ILE B 460     -29.659   7.288 -14.585  1.00 27.45           H  
+ATOM   2841 HG21 ILE B 460     -27.220   8.081 -12.169  1.00 22.19           H  
+ATOM   2842 HG22 ILE B 460     -26.932   6.612 -11.639  1.00 22.19           H  
+ATOM   2843 HG23 ILE B 460     -26.361   7.074 -13.048  1.00 22.19           H  
+ATOM   2844 HD11 ILE B 460     -29.503   9.560 -14.384  1.00 30.93           H  
+ATOM   2845 HD12 ILE B 460     -29.747   8.967 -12.930  1.00 30.93           H  
+ATOM   2846 HD13 ILE B 460     -28.290   9.424 -13.368  1.00 30.93           H  
+ATOM   2847  N   GLU B 461     -27.832   3.970 -11.663  1.00 13.17           N  
+ATOM   2848  CA  GLU B 461     -26.991   3.230 -10.731  1.00 13.99           C  
+ATOM   2849  C   GLU B 461     -26.597   1.857 -11.259  1.00 11.26           C  
+ATOM   2850  O   GLU B 461     -25.492   1.390 -10.960  1.00 11.41           O  
+ATOM   2851  CB  GLU B 461     -27.677   3.081  -9.379  1.00 13.04           C  
+ATOM   2852  CG  GLU B 461     -27.793   4.403  -8.613  1.00 15.74           C  
+ATOM   2853  CD  GLU B 461     -26.449   4.952  -8.124  1.00 19.62           C  
+ATOM   2854  OE1 GLU B 461     -25.423   4.263  -8.244  1.00 18.70           O  
+ATOM   2855  OE2 GLU B 461     -26.430   6.079  -7.610  1.00 24.12           O  
+ATOM   2856  H   GLU B 461     -28.647   4.093 -11.417  1.00 15.80           H  
+ATOM   2857  HA  GLU B 461     -26.181   3.748 -10.603  1.00 16.79           H  
+ATOM   2858  HB2 GLU B 461     -28.573   2.737  -9.518  1.00 15.64           H  
+ATOM   2859  HB3 GLU B 461     -27.165   2.464  -8.833  1.00 15.64           H  
+ATOM   2860  HG2 GLU B 461     -28.190   5.069  -9.196  1.00 18.89           H  
+ATOM   2861  HG3 GLU B 461     -28.356   4.265  -7.835  1.00 18.89           H  
+ATOM   2862  N   GLU B 462     -27.465   1.192 -12.035  1.00 11.67           N  
+ATOM   2863  CA  GLU B 462     -27.089  -0.085 -12.631  1.00 10.97           C  
+ATOM   2864  C   GLU B 462     -25.992   0.080 -13.688  1.00 11.12           C  
+ATOM   2865  O   GLU B 462     -25.063  -0.738 -13.768  1.00 11.08           O  
+ATOM   2866  CB  GLU B 462     -28.325  -0.754 -13.258  1.00 13.37           C  
+ATOM   2867  CG  GLU B 462     -29.350  -1.221 -12.238  1.00 13.13           C  
+ATOM   2868  CD  GLU B 462     -30.683  -1.625 -12.860  1.00 21.29           C  
+ATOM   2869  OE1 GLU B 462     -31.057  -1.103 -13.931  1.00 19.90           O  
+ATOM   2870  OE2 GLU B 462     -31.377  -2.465 -12.257  1.00 27.31           O  
+ATOM   2871  H   GLU B 462     -28.261   1.457 -12.225  1.00 14.00           H  
+ATOM   2872  HA  GLU B 462     -26.744  -0.658 -11.929  1.00 13.16           H  
+ATOM   2873  HB2 GLU B 462     -28.761  -0.117 -13.845  1.00 16.05           H  
+ATOM   2874  HB3 GLU B 462     -28.037  -1.529 -13.765  1.00 16.05           H  
+ATOM   2875  HG2 GLU B 462     -28.996  -1.992 -11.767  1.00 15.76           H  
+ATOM   2876  HG3 GLU B 462     -29.521  -0.500 -11.612  1.00 15.76           H  
+ATOM   2877  N   LEU B 463     -26.090   1.121 -14.519  1.00 10.60           N  
+ATOM   2878  CA  LEU B 463     -25.040   1.374 -15.499  1.00 11.14           C  
+ATOM   2879  C   LEU B 463     -23.722   1.705 -14.807  1.00  9.70           C  
+ATOM   2880  O   LEU B 463     -22.665   1.188 -15.193  1.00 10.30           O  
+ATOM   2881  CB  LEU B 463     -25.466   2.493 -16.440  1.00 11.33           C  
+ATOM   2882  CG  LEU B 463     -24.531   2.752 -17.620  1.00 10.39           C  
+ATOM   2883  CD1 LEU B 463     -24.370   1.490 -18.481  1.00 14.06           C  
+ATOM   2884  CD2 LEU B 463     -25.061   3.949 -18.432  1.00 13.03           C  
+ATOM   2885  H   LEU B 463     -26.741   1.683 -14.533  1.00 12.71           H  
+ATOM   2886  HA  LEU B 463     -24.902   0.578 -16.036  1.00 13.36           H  
+ATOM   2887  HB2 LEU B 463     -26.337   2.269 -16.805  1.00 13.59           H  
+ATOM   2888  HB3 LEU B 463     -25.522   3.315 -15.930  1.00 13.59           H  
+ATOM   2889  HG  LEU B 463     -23.643   2.975 -17.302  1.00 12.47           H  
+ATOM   2890 HD11 LEU B 463     -23.934   1.729 -19.314  1.00 16.87           H  
+ATOM   2891 HD12 LEU B 463     -23.831   0.845 -17.998  1.00 16.87           H  
+ATOM   2892 HD13 LEU B 463     -25.248   1.118 -18.663  1.00 16.87           H  
+ATOM   2893 HD21 LEU B 463     -24.461   4.116 -19.176  1.00 15.64           H  
+ATOM   2894 HD22 LEU B 463     -25.948   3.738 -18.764  1.00 15.64           H  
+ATOM   2895 HD23 LEU B 463     -25.100   4.729 -17.857  1.00 15.64           H  
+ATOM   2896  N   ILE B 464     -23.770   2.531 -13.753  1.00 10.17           N  
+ATOM   2897  CA  ILE B 464     -22.553   2.838 -13.008  1.00 10.71           C  
+ATOM   2898  C   ILE B 464     -21.951   1.570 -12.421  1.00  9.85           C  
+ATOM   2899  O   ILE B 464     -20.737   1.348 -12.501  1.00 11.85           O  
+ATOM   2900  CB  ILE B 464     -22.829   3.886 -11.911  1.00 11.88           C  
+ATOM   2901  CG1 ILE B 464     -23.142   5.231 -12.559  1.00 11.57           C  
+ATOM   2902  CG2 ILE B 464     -21.643   3.952 -10.922  1.00 12.01           C  
+ATOM   2903  CD1 ILE B 464     -23.660   6.270 -11.578  1.00 12.48           C  
+ATOM   2904  H   ILE B 464     -24.481   2.915 -13.459  1.00 12.20           H  
+ATOM   2905  HA  ILE B 464     -21.912   3.218 -13.628  1.00 12.85           H  
+ATOM   2906  HB  ILE B 464     -23.607   3.627 -11.393  1.00 14.25           H  
+ATOM   2907 HG12 ILE B 464     -22.332   5.580 -12.962  1.00 13.89           H  
+ATOM   2908 HG13 ILE B 464     -23.821   5.100 -13.239  1.00 13.89           H  
+ATOM   2909 HG21 ILE B 464     -21.704   4.774 -10.411  1.00 14.41           H  
+ATOM   2910 HG22 ILE B 464     -21.686   3.188 -10.326  1.00 14.41           H  
+ATOM   2911 HG23 ILE B 464     -20.813   3.934 -11.423  1.00 14.41           H  
+ATOM   2912 HD11 ILE B 464     -23.976   7.042 -12.074  1.00 14.98           H  
+ATOM   2913 HD12 ILE B 464     -24.388   5.886 -11.066  1.00 14.98           H  
+ATOM   2914 HD13 ILE B 464     -22.939   6.531 -10.984  1.00 14.98           H  
+ATOM   2915  N   ASN B 465     -22.784   0.726 -11.808  1.00 10.48           N  
+ATOM   2916  CA  ASN B 465     -22.257  -0.493 -11.202  1.00 11.38           C  
+ATOM   2917  C   ASN B 465     -21.615  -1.388 -12.252  1.00 11.90           C  
+ATOM   2918  O   ASN B 465     -20.584  -2.020 -11.995  1.00 12.53           O  
+ATOM   2919  CB  ASN B 465     -23.346  -1.269 -10.463  1.00 10.64           C  
+ATOM   2920  CG  ASN B 465     -22.787  -2.164  -9.356  1.00 14.00           C  
+ATOM   2921  OD1 ASN B 465     -21.940  -1.746  -8.595  1.00 15.98           O  
+ATOM   2922  ND2 ASN B 465     -23.259  -3.383  -9.296  1.00 21.25           N  
+ATOM   2923  H   ASN B 465     -23.634   0.833 -11.733  1.00 12.57           H  
+ATOM   2924  HA  ASN B 465     -21.589  -0.232 -10.548  1.00 13.65           H  
+ATOM   2925  HB2 ASN B 465     -23.963  -0.640 -10.058  1.00 12.77           H  
+ATOM   2926  HB3 ASN B 465     -23.816  -1.834 -11.097  1.00 12.77           H  
+ATOM   2927 HD21 ASN B 465     -22.976  -3.924  -8.691  1.00 25.51           H  
+ATOM   2928 HD22 ASN B 465     -23.852  -3.643  -9.862  1.00 25.51           H  
+ATOM   2929  N   THR B 466     -22.219  -1.455 -13.447  1.00 10.04           N  
+ATOM   2930  CA  THR B 466     -21.638  -2.227 -14.538  1.00 11.32           C  
+ATOM   2931  C   THR B 466     -20.262  -1.696 -14.912  1.00 10.45           C  
+ATOM   2932  O   THR B 466     -19.298  -2.462 -15.031  1.00 11.24           O  
+ATOM   2933  CB  THR B 466     -22.566  -2.177 -15.755  1.00 11.05           C  
+ATOM   2934  OG1 THR B 466     -23.856  -2.679 -15.416  1.00 13.75           O  
+ATOM   2935  CG2 THR B 466     -21.989  -2.978 -16.902  1.00 12.48           C  
+ATOM   2936  H   THR B 466     -22.958  -1.063 -13.644  1.00 12.05           H  
+ATOM   2937  HA  THR B 466     -21.544  -3.150 -14.253  1.00 13.58           H  
+ATOM   2938  HB  THR B 466     -22.658  -1.256 -16.045  1.00 13.27           H  
+ATOM   2939  HG1 THR B 466     -24.203  -2.200 -14.819  1.00 16.50           H  
+ATOM   2940 HG21 THR B 466     -22.634  -3.035 -17.624  1.00 14.97           H  
+ATOM   2941 HG22 THR B 466     -21.183  -2.551 -17.232  1.00 14.97           H  
+ATOM   2942 HG23 THR B 466     -21.771  -3.875 -16.603  1.00 14.97           H  
+ATOM   2943  N   ILE B 467     -20.158  -0.379 -15.092  1.00 10.26           N  
+ATOM   2944  CA  ILE B 467     -18.883   0.236 -15.440  1.00 10.19           C  
+ATOM   2945  C   ILE B 467     -17.826  -0.067 -14.384  1.00 10.34           C  
+ATOM   2946  O   ILE B 467     -16.714  -0.507 -14.697  1.00 12.24           O  
+ATOM   2947  CB  ILE B 467     -19.062   1.752 -15.634  1.00 10.83           C  
+ATOM   2948  CG1 ILE B 467     -19.995   2.052 -16.810  1.00 11.62           C  
+ATOM   2949  CG2 ILE B 467     -17.693   2.413 -15.804  1.00 10.95           C  
+ATOM   2950  CD1 ILE B 467     -20.509   3.472 -16.820  1.00 11.91           C  
+ATOM   2951  H   ILE B 467     -20.810   0.177 -15.018  1.00 12.31           H  
+ATOM   2952  HA  ILE B 467     -18.579  -0.149 -16.277  1.00 12.22           H  
+ATOM   2953  HB  ILE B 467     -19.485   2.124 -14.844  1.00 12.99           H  
+ATOM   2954 HG12 ILE B 467     -19.512   1.905 -17.639  1.00 13.94           H  
+ATOM   2955 HG13 ILE B 467     -20.760   1.458 -16.763  1.00 13.94           H  
+ATOM   2956 HG21 ILE B 467     -17.813   3.293 -16.194  1.00 13.14           H  
+ATOM   2957 HG22 ILE B 467     -17.271   2.492 -14.934  1.00 13.14           H  
+ATOM   2958 HG23 ILE B 467     -17.148   1.864 -16.388  1.00 13.14           H  
+ATOM   2959 HD11 ILE B 467     -21.169   3.564 -17.525  1.00 14.29           H  
+ATOM   2960 HD12 ILE B 467     -20.914   3.668 -15.961  1.00 14.29           H  
+ATOM   2961 HD13 ILE B 467     -19.767   4.076 -16.982  1.00 14.29           H  
+ATOM   2962  N   ILE B 468     -18.152   0.174 -13.116  1.00 10.51           N  
+ATOM   2963  CA  ILE B 468     -17.130   0.050 -12.088  1.00 11.40           C  
+ATOM   2964  C   ILE B 468     -16.772  -1.419 -11.849  1.00 11.89           C  
+ATOM   2965  O   ILE B 468     -15.600  -1.746 -11.661  1.00 11.59           O  
+ATOM   2966  CB  ILE B 468     -17.579   0.786 -10.809  1.00 10.79           C  
+ATOM   2967  CG1 ILE B 468     -17.690   2.303 -11.096  1.00 12.80           C  
+ATOM   2968  CG2 ILE B 468     -16.601   0.482  -9.679  1.00 13.13           C  
+ATOM   2969  CD1 ILE B 468     -18.212   3.156  -9.969  1.00 14.73           C  
+ATOM   2970  H   ILE B 468     -18.932   0.403 -12.837  1.00 12.61           H  
+ATOM   2971  HA  ILE B 468     -16.317   0.481 -12.394  1.00 13.69           H  
+ATOM   2972  HB  ILE B 468     -18.456   0.475 -10.534  1.00 12.95           H  
+ATOM   2973 HG12 ILE B 468     -16.806   2.634 -11.318  1.00 15.35           H  
+ATOM   2974 HG13 ILE B 468     -18.289   2.425 -11.848  1.00 15.35           H  
+ATOM   2975 HG21 ILE B 468     -16.748   1.112  -8.957  1.00 15.76           H  
+ATOM   2976 HG22 ILE B 468     -16.752  -0.423  -9.365  1.00 15.76           H  
+ATOM   2977 HG23 ILE B 468     -15.695   0.569 -10.014  1.00 15.76           H  
+ATOM   2978 HD11 ILE B 468     -18.387   4.049 -10.304  1.00 17.67           H  
+ATOM   2979 HD12 ILE B 468     -19.032   2.764  -9.629  1.00 17.67           H  
+ATOM   2980 HD13 ILE B 468     -17.546   3.192  -9.265  1.00 17.67           H  
+ATOM   2981  N   GLU B 469     -17.747  -2.335 -11.883  1.00 10.55           N  
+ATOM   2982  CA  GLU B 469     -17.387  -3.745 -11.726  1.00 10.48           C  
+ATOM   2983  C   GLU B 469     -16.502  -4.218 -12.874  1.00 12.70           C  
+ATOM   2984  O   GLU B 469     -15.573  -5.000 -12.660  1.00 13.11           O  
+ATOM   2985  CB  GLU B 469     -18.642  -4.611 -11.605  1.00 10.96           C  
+ATOM   2986  CG  GLU B 469     -19.344  -4.438 -10.251  1.00 14.29           C  
+ATOM   2987  CD  GLU B 469     -20.483  -5.389 -10.032  1.00 20.00           C  
+ATOM   2988  OE1 GLU B 469     -20.926  -6.061 -10.999  1.00 22.34           O  
+ATOM   2989  OE2 GLU B 469     -20.955  -5.470  -8.874  1.00 18.35           O  
+ATOM   2990  H   GLU B 469     -18.585  -2.172 -11.991  1.00 12.66           H  
+ATOM   2991  HA  GLU B 469     -16.890  -3.852 -10.900  1.00 12.58           H  
+ATOM   2992  HB2 GLU B 469     -19.267  -4.363 -12.303  1.00 13.15           H  
+ATOM   2993  HB3 GLU B 469     -18.393  -5.544 -11.699  1.00 13.15           H  
+ATOM   2994  HG2 GLU B 469     -18.697  -4.585  -9.544  1.00 17.15           H  
+ATOM   2995  HG3 GLU B 469     -19.697  -3.537 -10.196  1.00 17.15           H  
+ATOM   2996  N   PHE B 470     -16.732  -3.710 -14.079  1.00 11.64           N  
+ATOM   2997  CA  PHE B 470     -15.880  -4.059 -15.213  1.00 11.91           C  
+ATOM   2998  C   PHE B 470     -14.479  -3.477 -15.042  1.00 11.62           C  
+ATOM   2999  O   PHE B 470     -13.476  -4.176 -15.220  1.00 13.60           O  
+ATOM   3000  CB  PHE B 470     -16.558  -3.571 -16.498  1.00 12.40           C  
+ATOM   3001  CG  PHE B 470     -15.979  -4.134 -17.771  1.00 13.85           C  
+ATOM   3002  CD1 PHE B 470     -16.100  -5.478 -18.066  1.00 15.71           C  
+ATOM   3003  CD2 PHE B 470     -15.371  -3.302 -18.689  1.00 17.21           C  
+ATOM   3004  CE1 PHE B 470     -15.593  -5.986 -19.240  1.00 17.34           C  
+ATOM   3005  CE2 PHE B 470     -14.883  -3.802 -19.875  1.00 16.05           C  
+ATOM   3006  CZ  PHE B 470     -14.985  -5.144 -20.144  1.00 13.75           C  
+ATOM   3007  H   PHE B 470     -17.370  -3.165 -14.268  1.00 13.97           H  
+ATOM   3008  HA  PHE B 470     -15.773  -5.022 -15.276  1.00 14.29           H  
+ATOM   3009  HB2 PHE B 470     -17.494  -3.824 -16.467  1.00 14.88           H  
+ATOM   3010  HB3 PHE B 470     -16.476  -2.606 -16.542  1.00 14.88           H  
+ATOM   3011  HD1 PHE B 470     -16.529  -6.044 -17.466  1.00 18.86           H  
+ATOM   3012  HD2 PHE B 470     -15.290  -2.394 -18.505  1.00 20.66           H  
+ATOM   3013  HE1 PHE B 470     -15.660  -6.896 -19.422  1.00 20.81           H  
+ATOM   3014  HE2 PHE B 470     -14.486  -3.232 -20.492  1.00 19.26           H  
+ATOM   3015  HZ  PHE B 470     -14.642  -5.485 -20.938  1.00 16.51           H  
+ATOM   3016  N   VAL B 471     -14.388  -2.207 -14.651  1.00 11.96           N  
+ATOM   3017  CA  VAL B 471     -13.085  -1.609 -14.377  1.00 12.44           C  
+ATOM   3018  C   VAL B 471     -12.349  -2.373 -13.284  1.00 15.14           C  
+ATOM   3019  O   VAL B 471     -11.119  -2.532 -13.337  1.00 16.16           O  
+ATOM   3020  CB  VAL B 471     -13.266  -0.130 -14.005  1.00 13.62           C  
+ATOM   3021  CG1 VAL B 471     -11.992   0.444 -13.443  1.00 13.74           C  
+ATOM   3022  CG2 VAL B 471     -13.724   0.659 -15.239  1.00 14.88           C  
+ATOM   3023  H   VAL B 471     -15.056  -1.678 -14.539  1.00 14.36           H  
+ATOM   3024  HA  VAL B 471     -12.545  -1.666 -15.181  1.00 14.93           H  
+ATOM   3025  HB  VAL B 471     -13.945  -0.054 -13.317  1.00 16.35           H  
+ATOM   3026 HG11 VAL B 471     -12.065   1.411 -13.419  1.00 16.49           H  
+ATOM   3027 HG12 VAL B 471     -11.859   0.099 -12.546  1.00 16.49           H  
+ATOM   3028 HG13 VAL B 471     -11.250   0.182 -14.011  1.00 16.49           H  
+ATOM   3029 HG21 VAL B 471     -13.868   1.585 -14.986  1.00 17.85           H  
+ATOM   3030 HG22 VAL B 471     -13.037   0.605 -15.922  1.00 17.85           H  
+ATOM   3031 HG23 VAL B 471     -14.551   0.275 -15.570  1.00 17.85           H  
+ATOM   3032  N   GLU B 472     -13.073  -2.830 -12.262  1.00 12.56           N  
+ATOM   3033  CA  GLU B 472     -12.437  -3.573 -11.175  1.00 13.31           C  
+ATOM   3034  C   GLU B 472     -11.791  -4.853 -11.675  1.00 17.63           C  
+ATOM   3035  O   GLU B 472     -10.699  -5.216 -11.227  1.00 20.90           O  
+ATOM   3036  CB  GLU B 472     -13.461  -3.867 -10.077  1.00 13.82           C  
+ATOM   3037  CG  GLU B 472     -13.744  -2.667  -9.224  1.00 14.18           C  
+ATOM   3038  CD  GLU B 472     -14.846  -2.897  -8.246  1.00 24.07           C  
+ATOM   3039  OE1 GLU B 472     -15.684  -3.794  -8.478  1.00 26.46           O  
+ATOM   3040  OE2 GLU B 472     -14.876  -2.166  -7.239  1.00 25.67           O  
+ATOM   3041  H   GLU B 472     -13.922  -2.726 -12.175  1.00 15.08           H  
+ATOM   3042  HA  GLU B 472     -11.735  -3.025 -10.791  1.00 15.97           H  
+ATOM   3043  HB2 GLU B 472     -14.293  -4.150 -10.487  1.00 16.59           H  
+ATOM   3044  HB3 GLU B 472     -13.118  -4.571  -9.504  1.00 16.59           H  
+ATOM   3045  HG2 GLU B 472     -12.944  -2.439  -8.725  1.00 17.01           H  
+ATOM   3046  HG3 GLU B 472     -14.001  -1.927  -9.796  1.00 17.01           H  
+ATOM   3047  N   ILE B 473     -12.445  -5.555 -12.593  1.00 15.29           N  
+ATOM   3048  CA  ILE B 473     -11.801  -6.711 -13.215  1.00 19.91           C  
+ATOM   3049  C   ILE B 473     -10.549  -6.283 -13.971  1.00 22.00           C  
+ATOM   3050  O   ILE B 473      -9.493  -6.923 -13.877  1.00 24.77           O  
+ATOM   3051  CB  ILE B 473     -12.788  -7.423 -14.151  1.00 19.91           C  
+ATOM   3052  CG1 ILE B 473     -13.911  -8.055 -13.355  1.00 18.50           C  
+ATOM   3053  CG2 ILE B 473     -12.044  -8.453 -14.978  1.00 22.72           C  
+ATOM   3054  CD1 ILE B 473     -15.133  -8.301 -14.165  1.00 24.71           C  
+ATOM   3055  H   ILE B 473     -13.242  -5.389 -12.870  1.00 18.35           H  
+ATOM   3056  HA  ILE B 473     -11.536  -7.328 -12.515  1.00 23.89           H  
+ATOM   3057  HB  ILE B 473     -13.187  -6.774 -14.752  1.00 23.89           H  
+ATOM   3058 HG12 ILE B 473     -13.607  -8.907 -13.005  1.00 22.20           H  
+ATOM   3059 HG13 ILE B 473     -14.150  -7.463 -12.625  1.00 22.20           H  
+ATOM   3060 HG21 ILE B 473     -12.671  -9.130 -15.277  1.00 27.26           H  
+ATOM   3061 HG22 ILE B 473     -11.641  -8.014 -15.743  1.00 27.26           H  
+ATOM   3062 HG23 ILE B 473     -11.355  -8.860 -14.429  1.00 27.26           H  
+ATOM   3063 HD11 ILE B 473     -15.843  -8.608 -13.580  1.00 29.65           H  
+ATOM   3064 HD12 ILE B 473     -15.396  -7.474 -14.599  1.00 29.65           H  
+ATOM   3065 HD13 ILE B 473     -14.938  -8.978 -14.832  1.00 29.65           H  
+ATOM   3066  N   LEU B 474     -10.661  -5.224 -14.777  1.00 20.42           N  
+ATOM   3067  CA  LEU B 474      -9.551  -4.821 -15.634  1.00 21.08           C  
+ATOM   3068  C   LEU B 474      -8.365  -4.288 -14.846  1.00 30.15           C  
+ATOM   3069  O   LEU B 474      -7.253  -4.216 -15.390  1.00 29.30           O  
+ATOM   3070  CB  LEU B 474     -10.014  -3.748 -16.618  1.00 21.88           C  
+ATOM   3071  CG  LEU B 474     -11.100  -4.200 -17.591  1.00 24.07           C  
+ATOM   3072  CD1 LEU B 474     -11.660  -3.020 -18.349  1.00 23.27           C  
+ATOM   3073  CD2 LEU B 474     -10.526  -5.234 -18.526  1.00 25.73           C  
+ATOM   3074  H   LEU B 474     -11.362  -4.730 -14.845  1.00 24.50           H  
+ATOM   3075  HA  LEU B 474      -9.258  -5.599 -16.134  1.00 25.29           H  
+ATOM   3076  HB2 LEU B 474     -10.367  -2.999 -16.112  1.00 26.26           H  
+ATOM   3077  HB3 LEU B 474      -9.250  -3.463 -17.143  1.00 26.26           H  
+ATOM   3078  HG  LEU B 474     -11.839  -4.599 -17.106  1.00 28.88           H  
+ATOM   3079 HD11 LEU B 474     -12.219  -3.346 -19.071  1.00 27.92           H  
+ATOM   3080 HD12 LEU B 474     -12.186  -2.476 -17.743  1.00 27.92           H  
+ATOM   3081 HD13 LEU B 474     -10.925  -2.499 -18.710  1.00 27.92           H  
+ATOM   3082 HD21 LEU B 474     -11.122  -5.340 -19.284  1.00 30.88           H  
+ATOM   3083 HD22 LEU B 474      -9.654  -4.936 -18.830  1.00 30.88           H  
+ATOM   3084 HD23 LEU B 474     -10.441  -6.076 -18.052  1.00 30.88           H  
+ATOM   3085  N   SER B 475      -8.588  -3.900 -13.598  1.00 26.15           N  
+ATOM   3086  CA  SER B 475      -7.588  -3.281 -12.745  1.00 35.06           C  
+ATOM   3087  C   SER B 475      -6.860  -4.280 -11.863  1.00 33.04           C  
+ATOM   3088  O   SER B 475      -6.043  -3.862 -11.035  1.00 46.78           O  
+ATOM   3089  CB  SER B 475      -8.263  -2.216 -11.865  1.00 28.12           C  
+ATOM   3090  OG  SER B 475      -8.630  -1.121 -12.665  1.00 33.56           O  
+ATOM   3091  H   SER B 475      -9.348  -3.990 -13.205  1.00 31.38           H  
+ATOM   3092  HA  SER B 475      -6.922  -2.846 -13.301  1.00 42.07           H  
+ATOM   3093  HB2 SER B 475      -9.056  -2.594 -11.453  1.00 33.75           H  
+ATOM   3094  HB3 SER B 475      -7.642  -1.922 -11.181  1.00 33.75           H  
+ATOM   3095  HG  SER B 475      -9.159  -1.371 -13.269  1.00 40.28           H  
+ATOM   3096  N   ASN B 476      -7.148  -5.569 -12.006  1.00 40.66           N  
+ATOM   3097  CA  ASN B 476      -6.507  -6.645 -11.239  1.00 49.09           C  
+ATOM   3098  C   ASN B 476      -7.244  -6.880  -9.922  1.00 47.73           C  
+ATOM   3099  O   ASN B 476      -6.915  -7.803  -9.175  1.00 51.93           O  
+ATOM   3100  CB  ASN B 476      -5.031  -6.344 -10.953  1.00 54.16           C  
+ATOM   3101  CG  ASN B 476      -4.278  -5.876 -12.183  1.00 57.80           C  
+ATOM   3102  OD1 ASN B 476      -4.626  -6.229 -13.312  1.00 52.02           O  
+ATOM   3103  ND2 ASN B 476      -3.247  -5.063 -11.971  1.00 64.34           N  
+ATOM   3104  OXT ASN B 476      -8.173  -6.150  -9.572  1.00 48.23           O  
+ATOM   3105  H   ASN B 476      -7.734  -5.864 -12.563  1.00 48.79           H  
+ATOM   3106  HA  ASN B 476      -6.539  -7.455 -11.771  1.00 58.91           H  
+ATOM   3107  HB2 ASN B 476      -4.976  -5.644 -10.284  1.00 64.99           H  
+ATOM   3108  HB3 ASN B 476      -4.602  -7.150 -10.627  1.00 64.99           H  
+ATOM   3109 HD21 ASN B 476      -2.787  -4.770 -12.635  1.00 77.20           H  
+ATOM   3110 HD22 ASN B 476      -3.040  -4.831 -11.169  1.00 77.20           H  
+TER    3111      ASN B 476                                                      
+ATOM   3112  N   SER A 281      12.680  30.005  -0.185  1.00 21.90           N  
+ATOM   3113  CA  SER A 281      13.110  29.700  -1.547  1.00 22.63           C  
+ATOM   3114  C   SER A 281      11.897  29.679  -2.468  1.00 22.99           C  
+ATOM   3115  O   SER A 281      10.751  29.613  -1.993  1.00 21.78           O  
+ATOM   3116  CB  SER A 281      13.860  28.371  -1.610  1.00 28.89           C  
+ATOM   3117  OG  SER A 281      13.104  27.314  -1.068  1.00 28.31           O  
+ATOM   3118  HA  SER A 281      13.729  30.380  -1.855  1.00 27.15           H  
+ATOM   3119  HB2 SER A 281      14.057  28.168  -2.538  1.00 34.67           H  
+ATOM   3120  HB3 SER A 281      14.684  28.454  -1.106  1.00 34.67           H  
+ATOM   3121  HG  SER A 281      12.948  27.459  -0.255  1.00 33.97           H  
+ATOM   3122  N   ASN A 282      12.150  29.755  -3.776  1.00 20.38           N  
+ATOM   3123  CA  ASN A 282      11.069  29.805  -4.748  1.00 19.84           C  
+ATOM   3124  C   ASN A 282      10.199  28.565  -4.617  1.00 20.83           C  
+ATOM   3125  O   ASN A 282      10.700  27.437  -4.665  1.00 24.15           O  
+ATOM   3126  CB  ASN A 282      11.631  29.905  -6.170  1.00 19.89           C  
+ATOM   3127  CG  ASN A 282      12.398  31.194  -6.408  1.00 22.39           C  
+ATOM   3128  OD1 ASN A 282      12.358  32.121  -5.592  1.00 20.51           O  
+ATOM   3129  ND2 ASN A 282      13.063  31.277  -7.548  1.00 23.10           N  
+ATOM   3130  H   ASN A 282      12.938  29.778  -4.121  1.00 24.46           H  
+ATOM   3131  HA  ASN A 282      10.525  30.592  -4.586  1.00 23.81           H  
+ATOM   3132  HB2 ASN A 282      12.237  29.163  -6.323  1.00 23.87           H  
+ATOM   3133  HB3 ASN A 282      10.898  29.871  -6.804  1.00 23.87           H  
+ATOM   3134 HD21 ASN A 282      13.514  31.986  -7.733  1.00 27.73           H  
+ATOM   3135 HD22 ASN A 282      13.045  30.622  -8.105  1.00 27.73           H  
+ATOM   3136  N   ALA A 283       8.890  28.777  -4.476  1.00 15.64           N  
+ATOM   3137  CA  ALA A 283       7.971  27.677  -4.250  1.00 14.67           C  
+ATOM   3138  C   ALA A 283       6.798  27.789  -5.207  1.00 13.02           C  
+ATOM   3139  O   ALA A 283       7.007  27.854  -6.421  1.00 13.63           O  
+ATOM   3140  CB  ALA A 283       7.511  27.650  -2.791  1.00 19.99           C  
+ATOM   3141  H   ALA A 283       8.515  29.551  -4.509  1.00 18.77           H  
+ATOM   3142  HA  ALA A 283       8.416  26.831  -4.416  1.00 17.61           H  
+ATOM   3143  HB1 ALA A 283       6.917  26.894  -2.661  1.00 23.99           H  
+ATOM   3144  HB2 ALA A 283       8.287  27.564  -2.216  1.00 23.99           H  
+ATOM   3145  HB3 ALA A 283       7.043  28.476  -2.592  1.00 23.99           H  
+ATOM   3146  N   THR A 284       5.567  27.807  -4.691  1.00 12.47           N  
+ATOM   3147  CA  THR A 284       4.379  27.699  -5.537  1.00 11.36           C  
+ATOM   3148  C   THR A 284       3.556  28.973  -5.447  1.00 11.46           C  
+ATOM   3149  O   THR A 284       3.217  29.428  -4.352  1.00 13.67           O  
+ATOM   3150  CB  THR A 284       3.541  26.483  -5.142  1.00 11.76           C  
+ATOM   3151  OG1 THR A 284       4.348  25.296  -5.262  1.00 11.95           O  
+ATOM   3152  CG2 THR A 284       2.302  26.345  -5.998  1.00 11.90           C  
+ATOM   3153  H   THR A 284       5.396  27.882  -3.852  1.00 14.96           H  
+ATOM   3154  HA  THR A 284       4.652  27.597  -6.462  1.00 13.63           H  
+ATOM   3155  HB  THR A 284       3.240  26.591  -4.226  1.00 14.11           H  
+ATOM   3156  HG1 THR A 284       3.882  24.614  -5.112  1.00 14.34           H  
+ATOM   3157 HG21 THR A 284       1.831  25.528  -5.771  1.00 14.27           H  
+ATOM   3158 HG22 THR A 284       1.711  27.100  -5.852  1.00 14.27           H  
+ATOM   3159 HG23 THR A 284       2.548  26.315  -6.936  1.00 14.27           H  
+ATOM   3160  N   VAL A 285       3.207  29.526  -6.603  1.00  9.89           N  
+ATOM   3161  CA  VAL A 285       2.410  30.743  -6.690  1.00 10.12           C  
+ATOM   3162  C   VAL A 285       1.009  30.399  -7.161  1.00 12.05           C  
+ATOM   3163  O   VAL A 285       0.810  29.458  -7.928  1.00 13.01           O  
+ATOM   3164  CB  VAL A 285       3.045  31.775  -7.637  1.00 10.49           C  
+ATOM   3165  CG1 VAL A 285       4.490  32.068  -7.192  1.00 12.99           C  
+ATOM   3166  CG2 VAL A 285       2.973  31.342  -9.098  1.00 14.88           C  
+ATOM   3167  H   VAL A 285       3.426  29.206  -7.371  1.00 11.87           H  
+ATOM   3168  HA  VAL A 285       2.347  31.128  -5.801  1.00 12.15           H  
+ATOM   3169  HB  VAL A 285       2.535  32.599  -7.586  1.00 12.59           H  
+ATOM   3170 HG11 VAL A 285       4.851  32.781  -7.742  1.00 15.58           H  
+ATOM   3171 HG12 VAL A 285       4.484  32.340  -6.261  1.00 15.58           H  
+ATOM   3172 HG13 VAL A 285       5.022  31.265  -7.299  1.00 15.58           H  
+ATOM   3173 HG21 VAL A 285       3.578  31.891  -9.621  1.00 17.85           H  
+ATOM   3174 HG22 VAL A 285       3.233  30.410  -9.164  1.00 17.85           H  
+ATOM   3175 HG23 VAL A 285       2.064  31.456  -9.417  1.00 17.85           H  
+ATOM   3176  N   PHE A 286       0.035  31.172  -6.701  1.00 10.43           N  
+ATOM   3177  CA  PHE A 286      -1.306  31.150  -7.271  1.00  9.49           C  
+ATOM   3178  C   PHE A 286      -1.416  32.254  -8.312  1.00 11.18           C  
+ATOM   3179  O   PHE A 286      -1.140  33.422  -8.021  1.00 10.75           O  
+ATOM   3180  CB  PHE A 286      -2.387  31.337  -6.210  1.00 10.24           C  
+ATOM   3181  CG  PHE A 286      -3.772  31.180  -6.757  1.00  9.97           C  
+ATOM   3182  CD1 PHE A 286      -4.249  29.919  -7.057  1.00 10.66           C  
+ATOM   3183  CD2 PHE A 286      -4.591  32.271  -6.992  1.00 11.72           C  
+ATOM   3184  CE1 PHE A 286      -5.495  29.736  -7.593  1.00 11.98           C  
+ATOM   3185  CE2 PHE A 286      -5.868  32.083  -7.526  1.00 11.38           C  
+ATOM   3186  CZ  PHE A 286      -6.308  30.812  -7.821  1.00 12.15           C  
+ATOM   3187  H   PHE A 286       0.128  31.727  -6.050  1.00 12.52           H  
+ATOM   3188  HA  PHE A 286      -1.453  30.288  -7.690  1.00 11.39           H  
+ATOM   3189  HB2 PHE A 286      -2.263  30.673  -5.514  1.00 12.28           H  
+ATOM   3190  HB3 PHE A 286      -2.311  32.228  -5.836  1.00 12.28           H  
+ATOM   3191  HD1 PHE A 286      -3.712  29.178  -6.892  1.00 12.79           H  
+ATOM   3192  HD2 PHE A 286      -4.291  33.129  -6.795  1.00 14.06           H  
+ATOM   3193  HE1 PHE A 286      -5.789  28.879  -7.802  1.00 14.38           H  
+ATOM   3194  HE2 PHE A 286      -6.421  32.815  -7.682  1.00 13.66           H  
+ATOM   3195  HZ  PHE A 286      -7.158  30.685  -8.175  1.00 14.58           H  
+ATOM   3196  N   LEU A 287      -1.825  31.893  -9.513  1.00  9.98           N  
+ATOM   3197  CA  LEU A 287      -1.937  32.854 -10.601  1.00 10.11           C  
+ATOM   3198  C   LEU A 287      -3.423  33.104 -10.848  1.00 10.97           C  
+ATOM   3199  O   LEU A 287      -4.140  32.218 -11.344  1.00 11.14           O  
+ATOM   3200  CB  LEU A 287      -1.215  32.367 -11.852  1.00 11.53           C  
+ATOM   3201  CG  LEU A 287      -1.111  33.378 -12.977  1.00 14.93           C  
+ATOM   3202  CD1 LEU A 287      -0.587  34.731 -12.545  1.00 13.68           C  
+ATOM   3203  CD2 LEU A 287      -0.174  32.750 -14.048  1.00 18.44           C  
+ATOM   3204  H   LEU A 287      -2.046  31.090  -9.728  1.00 11.97           H  
+ATOM   3205  HA  LEU A 287      -1.526  33.694 -10.344  1.00 12.13           H  
+ATOM   3206  HB2 LEU A 287      -0.312  32.115 -11.604  1.00 13.84           H  
+ATOM   3207  HB3 LEU A 287      -1.691  31.596 -12.198  1.00 13.84           H  
+ATOM   3208  HG  LEU A 287      -1.997  33.563 -13.326  1.00 17.92           H  
+ATOM   3209 HD11 LEU A 287      -0.390  35.261 -13.333  1.00 16.41           H  
+ATOM   3210 HD12 LEU A 287      -1.262  35.175 -12.008  1.00 16.41           H  
+ATOM   3211 HD13 LEU A 287       0.221  34.604 -12.022  1.00 16.41           H  
+ATOM   3212 HD21 LEU A 287      -0.097  33.361 -14.798  1.00 22.13           H  
+ATOM   3213 HD22 LEU A 287       0.699  32.599 -13.654  1.00 22.13           H  
+ATOM   3214 HD23 LEU A 287      -0.553  31.909 -14.345  1.00 22.13           H  
+ATOM   3215  N   SER A 288      -3.879  34.286 -10.427  1.00 10.68           N  
+ATOM   3216  CA  SER A 288      -5.273  34.688 -10.444  1.00 11.04           C  
+ATOM   3217  C   SER A 288      -5.510  35.644 -11.603  1.00 10.43           C  
+ATOM   3218  O   SER A 288      -4.715  36.570 -11.817  1.00 11.51           O  
+ATOM   3219  CB  SER A 288      -5.644  35.371  -9.124  1.00 11.14           C  
+ATOM   3220  OG  SER A 288      -6.974  35.861  -9.108  1.00 12.14           O  
+ATOM   3221  H   SER A 288      -3.366  34.900 -10.111  1.00 12.81           H  
+ATOM   3222  HA  SER A 288      -5.839  33.909 -10.565  1.00 13.25           H  
+ATOM   3223  HB2 SER A 288      -5.546  34.727  -8.407  1.00 13.37           H  
+ATOM   3224  HB3 SER A 288      -5.040  36.118  -8.985  1.00 13.37           H  
+ATOM   3225  HG  SER A 288      -7.515  35.228  -9.218  1.00 14.56           H  
+ATOM   3226  N   GLY A 289      -6.573  35.410 -12.351  1.00  9.72           N  
+ATOM   3227  CA  GLY A 289      -6.951  36.351 -13.375  1.00  9.48           C  
+ATOM   3228  C   GLY A 289      -7.981  35.821 -14.346  1.00  8.72           C  
+ATOM   3229  O   GLY A 289      -8.109  34.617 -14.563  1.00 10.53           O  
+ATOM   3230  H   GLY A 289      -7.083  34.721 -12.282  1.00 11.67           H  
+ATOM   3231  HA2 GLY A 289      -7.318  37.144 -12.954  1.00 11.37           H  
+ATOM   3232  HA3 GLY A 289      -6.162  36.599 -13.882  1.00 11.37           H  
+ATOM   3233  N   SER A 290      -8.734  36.746 -14.935  1.00 10.10           N  
+ATOM   3234  CA  SER A 290      -9.688  36.438 -15.995  1.00 10.08           C  
+ATOM   3235  C   SER A 290      -9.825  37.698 -16.831  1.00  9.26           C  
+ATOM   3236  O   SER A 290      -9.612  38.804 -16.324  1.00 11.32           O  
+ATOM   3237  CB  SER A 290     -11.039  36.004 -15.472  1.00  9.82           C  
+ATOM   3238  OG  SER A 290     -11.593  37.008 -14.657  1.00 12.24           O  
+ATOM   3239  H   SER A 290      -8.711  37.581 -14.733  1.00 12.12           H  
+ATOM   3240  HA  SER A 290      -9.358  35.705 -16.537  1.00 12.10           H  
+ATOM   3241  HB2 SER A 290     -11.633  35.840 -16.221  1.00 11.78           H  
+ATOM   3242  HB3 SER A 290     -10.933  35.194 -14.949  1.00 11.78           H  
+ATOM   3243  HG  SER A 290     -11.726  37.704 -15.109  1.00 14.69           H  
+ATOM   3244  N   ALA A 291     -10.168  37.528 -18.111  1.00 10.28           N  
+ATOM   3245  CA  ALA A 291     -10.258  38.694 -18.982  1.00 10.32           C  
+ATOM   3246  C   ALA A 291     -10.995  38.385 -20.270  1.00 11.72           C  
+ATOM   3247  O   ALA A 291     -10.842  37.299 -20.844  1.00 13.03           O  
+ATOM   3248  CB  ALA A 291      -8.859  39.218 -19.346  1.00 11.73           C  
+ATOM   3249  H   ALA A 291     -10.347  36.773 -18.482  1.00 12.33           H  
+ATOM   3250  HA  ALA A 291     -10.770  39.365 -18.504  1.00 12.38           H  
+ATOM   3251  HB1 ALA A 291      -8.952  40.002 -19.910  1.00 14.07           H  
+ATOM   3252  HB2 ALA A 291      -8.387  39.451 -18.531  1.00 14.07           H  
+ATOM   3253  HB3 ALA A 291      -8.376  38.524 -19.821  1.00 14.07           H  
+ATOM   3254  N   VAL A 292     -11.762  39.370 -20.740  1.00 12.14           N  
+ATOM   3255  CA  VAL A 292     -12.161  39.452 -22.142  1.00 11.77           C  
+ATOM   3256  C   VAL A 292     -11.537  40.653 -22.831  1.00 16.36           C  
+ATOM   3257  O   VAL A 292     -11.553  40.715 -24.075  1.00 17.54           O  
+ATOM   3258  CB  VAL A 292     -13.693  39.482 -22.318  1.00 15.74           C  
+ATOM   3259  CG1 VAL A 292     -14.323  38.181 -21.834  1.00 19.75           C  
+ATOM   3260  CG2 VAL A 292     -14.315  40.679 -21.603  1.00 18.48           C  
+ATOM   3261  H   VAL A 292     -12.068  40.013 -20.256  1.00 14.57           H  
+ATOM   3262  HA  VAL A 292     -11.854  38.647 -22.588  1.00 14.12           H  
+ATOM   3263  HB  VAL A 292     -13.881  39.577 -23.264  1.00 18.89           H  
+ATOM   3264 HG11 VAL A 292     -15.264  38.178 -22.073  1.00 23.70           H  
+ATOM   3265 HG12 VAL A 292     -13.872  37.434 -22.259  1.00 23.70           H  
+ATOM   3266 HG13 VAL A 292     -14.226  38.121 -20.871  1.00 23.70           H  
+ATOM   3267 HG21 VAL A 292     -15.280  40.634 -21.693  1.00 22.18           H  
+ATOM   3268 HG22 VAL A 292     -14.069  40.650 -20.665  1.00 22.18           H  
+ATOM   3269 HG23 VAL A 292     -13.984  41.496 -22.007  1.00 22.18           H  
+ATOM   3270  N   GLU A 293     -10.989  41.599 -22.076  1.00 13.91           N  
+ATOM   3271  CA  GLU A 293     -10.189  42.688 -22.623  1.00 14.27           C  
+ATOM   3272  C   GLU A 293      -9.012  42.925 -21.690  1.00 14.64           C  
+ATOM   3273  O   GLU A 293      -9.013  42.480 -20.531  1.00 13.74           O  
+ATOM   3274  CB  GLU A 293     -11.022  43.959 -22.819  1.00 19.38           C  
+ATOM   3275  CG  GLU A 293     -11.824  44.331 -21.622  1.00 17.45           C  
+ATOM   3276  CD  GLU A 293     -12.467  45.706 -21.753  1.00 18.75           C  
+ATOM   3277  OE1 GLU A 293     -13.515  45.778 -22.424  1.00 23.87           O  
+ATOM   3278  OE2 GLU A 293     -11.931  46.701 -21.199  1.00 20.07           O  
+ATOM   3279  H   GLU A 293     -11.068  41.632 -21.220  1.00 16.69           H  
+ATOM   3280  HA  GLU A 293      -9.834  42.449 -23.493  1.00 17.13           H  
+ATOM   3281  HB2 GLU A 293     -10.426  44.697 -23.019  1.00 23.26           H  
+ATOM   3282  HB3 GLU A 293     -11.636  43.819 -23.557  1.00 23.26           H  
+ATOM   3283  HG2 GLU A 293     -12.531  43.678 -21.500  1.00 20.94           H  
+ATOM   3284  HG3 GLU A 293     -11.245  44.342 -20.844  1.00 20.94           H  
+ATOM   3285  N   TYR A 294      -7.991  43.612 -22.209  1.00 13.17           N  
+ATOM   3286  CA  TYR A 294      -6.677  43.604 -21.581  1.00 12.09           C  
+ATOM   3287  C   TYR A 294      -6.100  45.014 -21.436  1.00 13.72           C  
+ATOM   3288  O   TYR A 294      -4.894  45.240 -21.595  1.00 14.49           O  
+ATOM   3289  CB  TYR A 294      -5.745  42.677 -22.361  1.00 12.15           C  
+ATOM   3290  CG  TYR A 294      -6.218  41.224 -22.479  1.00 13.14           C  
+ATOM   3291  CD1 TYR A 294      -5.855  40.284 -21.522  1.00 13.23           C  
+ATOM   3292  CD2 TYR A 294      -7.001  40.800 -23.540  1.00 13.16           C  
+ATOM   3293  CE1 TYR A 294      -6.245  38.973 -21.629  1.00 12.41           C  
+ATOM   3294  CE2 TYR A 294      -7.404  39.491 -23.656  1.00 12.15           C  
+ATOM   3295  CZ  TYR A 294      -7.020  38.572 -22.689  1.00 12.00           C  
+ATOM   3296  OH  TYR A 294      -7.409  37.252 -22.827  1.00 13.25           O  
+ATOM   3297  H   TYR A 294      -8.041  44.088 -22.924  1.00 15.80           H  
+ATOM   3298  HA  TYR A 294      -6.762  43.269 -20.674  1.00 14.50           H  
+ATOM   3299  HB2 TYR A 294      -5.651  43.025 -23.261  1.00 14.58           H  
+ATOM   3300  HB3 TYR A 294      -4.883  42.666 -21.917  1.00 14.58           H  
+ATOM   3301  HD1 TYR A 294      -5.339  40.548 -20.795  1.00 15.88           H  
+ATOM   3302  HD2 TYR A 294      -7.260  41.414 -24.188  1.00 15.79           H  
+ATOM   3303  HE1 TYR A 294      -5.985  38.356 -20.984  1.00 14.90           H  
+ATOM   3304  HE2 TYR A 294      -7.929  39.224 -24.375  1.00 14.58           H  
+ATOM   3305  HH  TYR A 294      -7.117  36.797 -22.184  1.00 15.90           H  
+ATOM   3306  N   ASN A 295      -6.949  45.974 -21.073  1.00 15.06           N  
+ATOM   3307  CA  ASN A 295      -6.548  47.343 -20.732  1.00 13.99           C  
+ATOM   3308  C   ASN A 295      -5.998  48.006 -21.988  1.00 17.76           C  
+ATOM   3309  O   ASN A 295      -6.767  48.224 -22.925  1.00 20.49           O  
+ATOM   3310  CB  ASN A 295      -5.566  47.400 -19.562  1.00 16.29           C  
+ATOM   3311  CG  ASN A 295      -5.516  48.785 -18.920  1.00 18.85           C  
+ATOM   3312  OD1 ASN A 295      -6.319  49.660 -19.256  1.00 20.34           O  
+ATOM   3313  ND2 ASN A 295      -4.581  48.989 -17.988  1.00 19.96           N  
+ATOM   3314  H   ASN A 295      -7.799  45.855 -21.012  1.00 18.08           H  
+ATOM   3315  HA  ASN A 295      -7.316  47.845 -20.417  1.00 16.79           H  
+ATOM   3316  HB2 ASN A 295      -5.841  46.762 -18.884  1.00 19.54           H  
+ATOM   3317  HB3 ASN A 295      -4.677  47.181 -19.881  1.00 19.54           H  
+ATOM   3318 HD21 ASN A 295      -4.519  49.755 -17.602  1.00 23.95           H  
+ATOM   3319 HD22 ASN A 295      -4.042  48.354 -17.774  1.00 23.95           H  
+ATOM   3320  N   HIS A 296      -4.706  48.317 -22.046  1.00 17.47           N  
+ATOM   3321  CA  HIS A 296      -4.156  49.011 -23.209  1.00 18.69           C  
+ATOM   3322  C   HIS A 296      -3.581  48.078 -24.260  1.00 21.60           C  
+ATOM   3323  O   HIS A 296      -3.074  48.553 -25.282  1.00 22.66           O  
+ATOM   3324  CB  HIS A 296      -3.082  50.001 -22.755  1.00 20.23           C  
+ATOM   3325  CG  HIS A 296      -3.592  51.001 -21.775  1.00 22.80           C  
+ATOM   3326  ND1 HIS A 296      -4.678  51.810 -22.042  1.00 29.47           N  
+ATOM   3327  CD2 HIS A 296      -3.188  51.311 -20.520  1.00 24.77           C  
+ATOM   3328  CE1 HIS A 296      -4.916  52.577 -20.992  1.00 33.31           C  
+ATOM   3329  NE2 HIS A 296      -4.022  52.298 -20.059  1.00 28.81           N  
+ATOM   3330  H   HIS A 296      -4.133  48.138 -21.431  1.00 20.96           H  
+ATOM   3331  HA  HIS A 296      -4.872  49.509 -23.633  1.00 22.43           H  
+ATOM   3332  HB2 HIS A 296      -2.359  49.510 -22.334  1.00 24.28           H  
+ATOM   3333  HB3 HIS A 296      -2.749  50.482 -23.529  1.00 24.28           H  
+ATOM   3334  HD2 HIS A 296      -2.479  50.927 -20.057  1.00 29.72           H  
+ATOM   3335  HE1 HIS A 296      -5.596  53.207 -20.922  1.00 39.98           H  
+ATOM   3336  HE2 HIS A 296      -3.972  52.674 -19.288  1.00 34.58           H  
+ATOM   3337  N   TRP A 297      -3.671  46.772 -24.065  1.00 16.91           N  
+ATOM   3338  CA  TRP A 297      -3.037  45.819 -24.958  1.00 14.19           C  
+ATOM   3339  C   TRP A 297      -4.073  45.068 -25.773  1.00 15.66           C  
+ATOM   3340  O   TRP A 297      -5.154  44.747 -25.274  1.00 18.98           O  
+ATOM   3341  CB  TRP A 297      -2.205  44.816 -24.163  1.00 13.98           C  
+ATOM   3342  CG  TRP A 297      -0.937  45.348 -23.633  1.00 14.89           C  
+ATOM   3343  CD1 TRP A 297      -0.340  46.535 -23.947  1.00 15.48           C  
+ATOM   3344  CD2 TRP A 297      -0.067  44.697 -22.715  1.00 13.79           C  
+ATOM   3345  NE1 TRP A 297       0.843  46.662 -23.284  1.00 15.73           N  
+ATOM   3346  CE2 TRP A 297       1.036  45.547 -22.510  1.00 15.91           C  
+ATOM   3347  CE3 TRP A 297      -0.117  43.475 -22.027  1.00 16.29           C  
+ATOM   3348  CZ2 TRP A 297       2.080  45.222 -21.655  1.00 17.48           C  
+ATOM   3349  CZ3 TRP A 297       0.921  43.163 -21.171  1.00 15.35           C  
+ATOM   3350  CH2 TRP A 297       2.000  44.023 -20.989  1.00 18.81           C  
+ATOM   3351  H   TRP A 297      -4.100  46.410 -23.414  1.00 20.29           H  
+ATOM   3352  HA  TRP A 297      -2.463  46.301 -25.575  1.00 17.03           H  
+ATOM   3353  HB2 TRP A 297      -2.731  44.510 -23.408  1.00 16.78           H  
+ATOM   3354  HB3 TRP A 297      -1.988  44.069 -24.742  1.00 16.78           H  
+ATOM   3355  HD1 TRP A 297      -0.692  47.168 -24.530  1.00 18.58           H  
+ATOM   3356  HE1 TRP A 297       1.381  47.331 -23.341  1.00 18.87           H  
+ATOM   3357  HE3 TRP A 297      -0.831  42.890 -22.144  1.00 19.55           H  
+ATOM   3358  HZ2 TRP A 297       2.804  45.792 -21.537  1.00 20.97           H  
+ATOM   3359  HZ3 TRP A 297       0.899  42.358 -20.705  1.00 18.42           H  
+ATOM   3360  HH2 TRP A 297       2.682  43.781 -20.405  1.00 22.57           H  
+ATOM   3361  N   GLU A 298      -3.725  44.780 -27.029  1.00 17.94           N  
+ATOM   3362  CA  GLU A 298      -4.515  43.880 -27.847  1.00 20.56           C  
+ATOM   3363  C   GLU A 298      -4.461  42.463 -27.290  1.00 14.96           C  
+ATOM   3364  O   GLU A 298      -3.491  42.057 -26.647  1.00 15.36           O  
+ATOM   3365  CB  GLU A 298      -3.996  43.874 -29.288  1.00 18.89           C  
+ATOM   3366  CG  GLU A 298      -3.917  45.264 -29.878  1.00 26.28           C  
+ATOM   3367  CD  GLU A 298      -4.197  45.272 -31.354  1.00 37.87           C  
+ATOM   3368  OE1 GLU A 298      -3.938  44.238 -32.007  1.00 46.04           O  
+ATOM   3369  OE2 GLU A 298      -4.690  46.305 -31.859  1.00 43.98           O  
+ATOM   3370  H   GLU A 298      -3.032  45.097 -27.427  1.00 21.53           H  
+ATOM   3371  HA  GLU A 298      -5.437  44.180 -27.851  1.00 24.67           H  
+ATOM   3372  HB2 GLU A 298      -3.106  43.489 -29.303  1.00 22.67           H  
+ATOM   3373  HB3 GLU A 298      -4.595  43.346 -29.839  1.00 22.67           H  
+ATOM   3374  HG2 GLU A 298      -4.573  45.831 -29.443  1.00 31.54           H  
+ATOM   3375  HG3 GLU A 298      -3.026  45.619 -29.738  1.00 31.54           H  
+ATOM   3376  N   THR A 299      -5.515  41.699 -27.568  1.00 16.73           N  
+ATOM   3377  CA  THR A 299      -5.620  40.332 -27.062  1.00 13.75           C  
+ATOM   3378  C   THR A 299      -4.364  39.516 -27.340  1.00 15.97           C  
+ATOM   3379  O   THR A 299      -3.822  38.873 -26.434  1.00 14.99           O  
+ATOM   3380  CB  THR A 299      -6.856  39.658 -27.670  1.00 19.19           C  
+ATOM   3381  OG1 THR A 299      -8.037  40.366 -27.254  1.00 23.07           O  
+ATOM   3382  CG2 THR A 299      -6.938  38.203 -27.263  1.00 23.03           C  
+ATOM   3383  H   THR A 299      -6.184  41.948 -28.047  1.00 20.07           H  
+ATOM   3384  HA  THR A 299      -5.727  40.366 -26.099  1.00 16.50           H  
+ATOM   3385  HB  THR A 299      -6.798  39.680 -28.638  1.00 23.02           H  
+ATOM   3386  HG1 THR A 299      -8.086  40.376 -26.415  1.00 27.69           H  
+ATOM   3387 HG21 THR A 299      -7.827  37.858 -27.445  1.00 27.64           H  
+ATOM   3388 HG22 THR A 299      -6.290  37.682 -27.762  1.00 27.64           H  
+ATOM   3389 HG23 THR A 299      -6.753  38.112 -26.315  1.00 27.64           H  
+ATOM   3390  N   GLU A 300      -3.880  39.509 -28.599  1.00 15.65           N  
+ATOM   3391  CA  GLU A 300      -2.735  38.660 -28.909  1.00 15.11           C  
+ATOM   3392  C   GLU A 300      -1.492  39.089 -28.145  1.00 13.27           C  
+ATOM   3393  O   GLU A 300      -0.626  38.257 -27.853  1.00 13.50           O  
+ATOM   3394  CB  GLU A 300      -2.433  38.668 -30.410  1.00 16.33           C  
+ATOM   3395  CG  GLU A 300      -3.468  37.969 -31.260  1.00 26.21           C  
+ATOM   3396  CD  GLU A 300      -4.679  38.836 -31.515  1.00 29.96           C  
+ATOM   3397  OE1 GLU A 300      -4.610  40.061 -31.248  1.00 29.40           O  
+ATOM   3398  OE2 GLU A 300      -5.705  38.284 -31.967  1.00 38.87           O  
+ATOM   3399  H   GLU A 300      -4.189  39.969 -29.256  1.00 18.78           H  
+ATOM   3400  HA  GLU A 300      -2.966  37.753 -28.652  1.00 18.13           H  
+ATOM   3401  HB2 GLU A 300      -2.380  39.589 -30.710  1.00 19.59           H  
+ATOM   3402  HB3 GLU A 300      -1.583  38.223 -30.557  1.00 19.59           H  
+ATOM   3403  HG2 GLU A 300      -3.075  37.741 -32.117  1.00 31.45           H  
+ATOM   3404  HG3 GLU A 300      -3.763  37.165 -30.805  1.00 31.45           H  
+ATOM   3405  N   HIS A 301      -1.382  40.376 -27.814  1.00 12.62           N  
+ATOM   3406  CA  HIS A 301      -0.234  40.861 -27.067  1.00 12.38           C  
+ATOM   3407  C   HIS A 301      -0.328  40.459 -25.610  1.00 12.41           C  
+ATOM   3408  O   HIS A 301       0.663  40.020 -25.017  1.00 11.94           O  
+ATOM   3409  CB  HIS A 301      -0.148  42.371 -27.207  1.00 12.70           C  
+ATOM   3410  CG  HIS A 301       1.184  42.937 -26.857  1.00 13.58           C  
+ATOM   3411  ND1 HIS A 301       1.344  43.946 -25.942  1.00 18.06           N  
+ATOM   3412  CD2 HIS A 301       2.419  42.658 -27.328  1.00 10.19           C  
+ATOM   3413  CE1 HIS A 301       2.622  44.273 -25.867  1.00 11.84           C  
+ATOM   3414  NE2 HIS A 301       3.300  43.489 -26.680  1.00 19.07           N  
+ATOM   3415  H   HIS A 301      -1.959  40.983 -28.010  1.00 15.15           H  
+ATOM   3416  HA  HIS A 301       0.581  40.479 -27.429  1.00 14.85           H  
+ATOM   3417  HB2 HIS A 301      -0.337  42.609 -28.128  1.00 15.24           H  
+ATOM   3418  HB3 HIS A 301      -0.804  42.775 -26.618  1.00 15.24           H  
+ATOM   3419  HD1 HIS A 301       0.711  44.310 -25.487  1.00 21.68           H  
+ATOM   3420  HD2 HIS A 301       2.634  42.021 -27.972  1.00 12.23           H  
+ATOM   3421  HE1 HIS A 301       2.981  44.942 -25.331  1.00 14.21           H  
+ATOM   3422  N   ALA A 302      -1.513  40.597 -25.022  1.00 11.79           N  
+ATOM   3423  CA  ALA A 302      -1.702  40.157 -23.643  1.00 12.06           C  
+ATOM   3424  C   ALA A 302      -1.500  38.648 -23.530  1.00 12.15           C  
+ATOM   3425  O   ALA A 302      -0.958  38.162 -22.526  1.00 12.22           O  
+ATOM   3426  CB  ALA A 302      -3.076  40.579 -23.148  1.00 10.96           C  
+ATOM   3427  H   ALA A 302      -2.211  40.935 -25.392  1.00 14.15           H  
+ATOM   3428  HA  ALA A 302      -1.047  40.586 -23.070  1.00 14.47           H  
+ATOM   3429  HB1 ALA A 302      -3.185  40.283 -22.230  1.00 13.15           H  
+ATOM   3430  HB2 ALA A 302      -3.146  41.545 -23.195  1.00 13.15           H  
+ATOM   3431  HB3 ALA A 302      -3.753  40.170 -23.709  1.00 13.15           H  
+ATOM   3432  N   GLU A 303      -1.934  37.885 -24.542  1.00 12.15           N  
+ATOM   3433  CA  GLU A 303      -1.697  36.446 -24.521  1.00 14.73           C  
+ATOM   3434  C   GLU A 303      -0.205  36.144 -24.475  1.00 14.60           C  
+ATOM   3435  O   GLU A 303       0.235  35.256 -23.735  1.00 14.41           O  
+ATOM   3436  CB  GLU A 303      -2.356  35.793 -25.745  1.00 15.37           C  
+ATOM   3437  CG  GLU A 303      -3.891  35.811 -25.680  1.00 16.79           C  
+ATOM   3438  CD  GLU A 303      -4.570  35.340 -26.972  1.00 22.90           C  
+ATOM   3439  OE1 GLU A 303      -3.860  35.012 -27.948  1.00 25.16           O  
+ATOM   3440  OE2 GLU A 303      -5.831  35.318 -26.997  1.00 24.59           O  
+ATOM   3441  H   GLU A 303      -2.357  38.173 -25.233  1.00 14.58           H  
+ATOM   3442  HA  GLU A 303      -2.103  36.062 -23.728  1.00 17.68           H  
+ATOM   3443  HB2 GLU A 303      -2.085  36.274 -26.543  1.00 18.45           H  
+ATOM   3444  HB3 GLU A 303      -2.069  34.868 -25.802  1.00 18.45           H  
+ATOM   3445  HG2 GLU A 303      -4.180  35.224 -24.963  1.00 20.14           H  
+ATOM   3446  HG3 GLU A 303      -4.186  36.718 -25.505  1.00 20.14           H  
+ATOM   3447  N   GLN A 304       0.599  36.866 -25.264  1.00 12.69           N  
+ATOM   3448  CA  GLN A 304       2.042  36.664 -25.210  1.00 13.40           C  
+ATOM   3449  C   GLN A 304       2.603  36.992 -23.830  1.00 12.08           C  
+ATOM   3450  O   GLN A 304       3.484  36.287 -23.326  1.00 12.42           O  
+ATOM   3451  CB  GLN A 304       2.750  37.515 -26.265  1.00 19.87           C  
+ATOM   3452  CG  GLN A 304       2.904  36.865 -27.627  1.00 32.53           C  
+ATOM   3453  CD  GLN A 304       3.301  35.397 -27.549  1.00 39.07           C  
+ATOM   3454  OE1 GLN A 304       2.592  34.528 -28.067  1.00 46.09           O  
+ATOM   3455  NE2 GLN A 304       4.415  35.111 -26.879  1.00 38.11           N  
+ATOM   3456  H   GLN A 304       0.337  37.463 -25.824  1.00 15.22           H  
+ATOM   3457  HA  GLN A 304       2.216  35.730 -25.405  1.00 16.08           H  
+ATOM   3458  HB2 GLN A 304       2.243  38.332 -26.391  1.00 23.85           H  
+ATOM   3459  HB3 GLN A 304       3.641  37.724 -25.942  1.00 23.85           H  
+ATOM   3460  HG2 GLN A 304       2.059  36.920 -28.099  1.00 39.03           H  
+ATOM   3461  HG3 GLN A 304       3.593  37.334 -28.123  1.00 39.03           H  
+ATOM   3462 HE21 GLN A 304       4.872  35.742 -26.515  1.00 45.73           H  
+ATOM   3463 HE22 GLN A 304       4.677  34.295 -26.810  1.00 45.73           H  
+ATOM   3464  N   PHE A 305       2.105  38.066 -23.201  1.00 11.60           N  
+ATOM   3465  CA  PHE A 305       2.533  38.417 -21.849  1.00 11.78           C  
+ATOM   3466  C   PHE A 305       2.261  37.280 -20.867  1.00 10.91           C  
+ATOM   3467  O   PHE A 305       3.144  36.873 -20.108  1.00 12.09           O  
+ATOM   3468  CB  PHE A 305       1.818  39.691 -21.403  1.00 11.23           C  
+ATOM   3469  CG  PHE A 305       1.858  39.937 -19.913  1.00 12.28           C  
+ATOM   3470  CD1 PHE A 305       3.055  40.213 -19.266  1.00 13.30           C  
+ATOM   3471  CD2 PHE A 305       0.701  39.912 -19.180  1.00 14.07           C  
+ATOM   3472  CE1 PHE A 305       3.067  40.452 -17.906  1.00 14.56           C  
+ATOM   3473  CE2 PHE A 305       0.717  40.155 -17.822  1.00 14.63           C  
+ATOM   3474  CZ  PHE A 305       1.899  40.422 -17.193  1.00 13.27           C  
+ATOM   3475  H   PHE A 305       1.522  38.603 -23.536  1.00 13.92           H  
+ATOM   3476  HA  PHE A 305       3.489  38.582 -21.855  1.00 14.14           H  
+ATOM   3477  HB2 PHE A 305       2.238  40.450 -21.838  1.00 13.47           H  
+ATOM   3478  HB3 PHE A 305       0.886  39.632 -21.666  1.00 13.47           H  
+ATOM   3479  HD1 PHE A 305       3.849  40.237 -19.749  1.00 15.96           H  
+ATOM   3480  HD2 PHE A 305      -0.107  39.729 -19.604  1.00 16.88           H  
+ATOM   3481  HE1 PHE A 305       3.870  40.634 -17.474  1.00 17.47           H  
+ATOM   3482  HE2 PHE A 305      -0.075  40.137 -17.336  1.00 17.55           H  
+ATOM   3483  HZ  PHE A 305       1.911  40.583 -16.277  1.00 15.92           H  
+ATOM   3484  N   ILE A 306       1.044  36.743 -20.887  1.00 10.41           N  
+ATOM   3485  CA  ILE A 306       0.688  35.696 -19.928  1.00 10.22           C  
+ATOM   3486  C   ILE A 306       1.487  34.430 -20.204  1.00 10.13           C  
+ATOM   3487  O   ILE A 306       2.011  33.790 -19.281  1.00 11.71           O  
+ATOM   3488  CB  ILE A 306      -0.828  35.440 -19.995  1.00 10.59           C  
+ATOM   3489  CG1 ILE A 306      -1.610  36.686 -19.574  1.00 12.12           C  
+ATOM   3490  CG2 ILE A 306      -1.201  34.227 -19.125  1.00 11.24           C  
+ATOM   3491  CD1 ILE A 306      -3.090  36.654 -19.988  1.00 13.43           C  
+ATOM   3492  H   ILE A 306       0.416  36.961 -21.433  1.00 12.50           H  
+ATOM   3493  HA  ILE A 306       0.911  35.992 -19.032  1.00 12.27           H  
+ATOM   3494  HB  ILE A 306      -1.067  35.242 -20.914  1.00 12.71           H  
+ATOM   3495 HG12 ILE A 306      -1.573  36.766 -18.608  1.00 14.54           H  
+ATOM   3496 HG13 ILE A 306      -1.203  37.464 -19.987  1.00 14.54           H  
+ATOM   3497 HG21 ILE A 306      -2.162  34.212 -18.999  1.00 13.49           H  
+ATOM   3498 HG22 ILE A 306      -0.913  33.417 -19.575  1.00 13.49           H  
+ATOM   3499 HG23 ILE A 306      -0.755  34.305 -18.267  1.00 13.49           H  
+ATOM   3500 HD11 ILE A 306      -3.498  37.505 -19.766  1.00 16.12           H  
+ATOM   3501 HD12 ILE A 306      -3.147  36.499 -20.944  1.00 16.12           H  
+ATOM   3502 HD13 ILE A 306      -3.536  35.938 -19.510  1.00 16.12           H  
+ATOM   3503  N   HIS A 307       1.617  34.073 -21.484  1.00 11.00           N  
+ATOM   3504  CA  HIS A 307       2.436  32.934 -21.883  1.00 10.61           C  
+ATOM   3505  C   HIS A 307       3.869  33.080 -21.407  1.00 12.41           C  
+ATOM   3506  O   HIS A 307       4.436  32.152 -20.813  1.00 12.30           O  
+ATOM   3507  CB  HIS A 307       2.363  32.819 -23.407  1.00 11.15           C  
+ATOM   3508  CG  HIS A 307       3.170  31.711 -23.996  1.00 11.60           C  
+ATOM   3509  ND1 HIS A 307       2.592  30.707 -24.744  1.00 13.18           N  
+ATOM   3510  CD2 HIS A 307       4.505  31.487 -24.034  1.00 14.94           C  
+ATOM   3511  CE1 HIS A 307       3.529  29.886 -25.174  1.00 14.68           C  
+ATOM   3512  NE2 HIS A 307       4.700  30.331 -24.753  1.00 15.47           N  
+ATOM   3513  H   HIS A 307       1.239  34.477 -22.142  1.00 13.20           H  
+ATOM   3514  HA  HIS A 307       2.094  32.119 -21.483  1.00 12.73           H  
+ATOM   3515  HB2 HIS A 307       1.438  32.671 -23.660  1.00 13.38           H  
+ATOM   3516  HB3 HIS A 307       2.684  33.649 -23.793  1.00 13.38           H  
+ATOM   3517  HD2 HIS A 307       5.165  32.015 -23.647  1.00 17.93           H  
+ATOM   3518  HE1 HIS A 307       3.390  29.123 -25.688  1.00 17.62           H  
+ATOM   3519  HE2 HIS A 307       5.460  29.959 -24.904  1.00 18.56           H  
+ATOM   3520  N   GLN A 308       4.479  34.244 -21.666  1.00 11.49           N  
+ATOM   3521  CA  GLN A 308       5.886  34.425 -21.312  1.00 12.00           C  
+ATOM   3522  C   GLN A 308       6.069  34.566 -19.800  1.00 11.29           C  
+ATOM   3523  O   GLN A 308       7.083  34.115 -19.264  1.00 11.95           O  
+ATOM   3524  CB  GLN A 308       6.476  35.625 -22.065  1.00 11.95           C  
+ATOM   3525  CG  GLN A 308       6.641  35.389 -23.555  1.00 15.62           C  
+ATOM   3526  CD  GLN A 308       7.242  36.589 -24.271  1.00 25.98           C  
+ATOM   3527  OE1 GLN A 308       7.784  37.508 -23.641  1.00 26.10           O  
+ATOM   3528  NE2 GLN A 308       7.135  36.595 -25.588  1.00 34.00           N  
+ATOM   3529  H   GLN A 308       4.107  34.926 -22.036  1.00 13.79           H  
+ATOM   3530  HA  GLN A 308       6.387  33.643 -21.593  1.00 14.40           H  
+ATOM   3531  HB2 GLN A 308       5.886  36.387 -21.949  1.00 14.34           H  
+ATOM   3532  HB3 GLN A 308       7.351  35.824 -21.698  1.00 14.34           H  
+ATOM   3533  HG2 GLN A 308       7.229  34.631 -23.693  1.00 18.74           H  
+ATOM   3534  HG3 GLN A 308       5.771  35.210 -23.946  1.00 18.74           H  
+ATOM   3535 HE21 GLN A 308       6.743  35.944 -25.990  1.00 40.80           H  
+ATOM   3536 HE22 GLN A 308       7.458  37.250 -26.042  1.00 40.80           H  
+ATOM   3537  N   LEU A 309       5.115  35.179 -19.103  1.00 11.34           N  
+ATOM   3538  CA  LEU A 309       5.193  35.232 -17.644  1.00 11.45           C  
+ATOM   3539  C   LEU A 309       5.184  33.821 -17.060  1.00 11.70           C  
+ATOM   3540  O   LEU A 309       5.972  33.499 -16.162  1.00 11.26           O  
+ATOM   3541  CB  LEU A 309       4.044  36.058 -17.071  1.00 10.80           C  
+ATOM   3542  CG  LEU A 309       3.901  36.073 -15.551  1.00 11.76           C  
+ATOM   3543  CD1 LEU A 309       5.134  36.677 -14.892  1.00 12.79           C  
+ATOM   3544  CD2 LEU A 309       2.629  36.822 -15.133  1.00 12.09           C  
+ATOM   3545  H   LEU A 309       4.425  35.564 -19.443  1.00 13.60           H  
+ATOM   3546  HA  LEU A 309       6.020  35.672 -17.391  1.00 13.74           H  
+ATOM   3547  HB2 LEU A 309       4.166  36.978 -17.355  1.00 12.96           H  
+ATOM   3548  HB3 LEU A 309       3.214  35.707 -17.431  1.00 12.96           H  
+ATOM   3549  HG  LEU A 309       3.823  35.159 -15.236  1.00 14.11           H  
+ATOM   3550 HD11 LEU A 309       4.989  36.724 -13.934  1.00 15.35           H  
+ATOM   3551 HD12 LEU A 309       5.902  36.116 -15.083  1.00 15.35           H  
+ATOM   3552 HD13 LEU A 309       5.279  37.567 -15.249  1.00 15.35           H  
+ATOM   3553 HD21 LEU A 309       2.567  36.823 -14.165  1.00 14.51           H  
+ATOM   3554 HD22 LEU A 309       2.676  37.733 -15.462  1.00 14.51           H  
+ATOM   3555 HD23 LEU A 309       1.859  36.372 -15.513  1.00 14.51           H  
+ATOM   3556  N   SER A 310       4.273  32.972 -17.549  1.00 12.03           N  
+ATOM   3557  CA  SER A 310       4.160  31.614 -17.020  1.00 11.49           C  
+ATOM   3558  C   SER A 310       5.417  30.816 -17.312  1.00 12.00           C  
+ATOM   3559  O   SER A 310       5.958  30.153 -16.418  1.00 11.22           O  
+ATOM   3560  CB  SER A 310       2.925  30.941 -17.622  1.00 12.58           C  
+ATOM   3561  OG  SER A 310       1.770  31.693 -17.313  1.00 14.21           O  
+ATOM   3562  H   SER A 310       3.717  33.157 -18.178  1.00 14.43           H  
+ATOM   3563  HA  SER A 310       4.047  31.642 -16.057  1.00 13.79           H  
+ATOM   3564  HB2 SER A 310       3.026  30.893 -18.586  1.00 15.09           H  
+ATOM   3565  HB3 SER A 310       2.835  30.049 -17.253  1.00 15.09           H  
+ATOM   3566  HG  SER A 310       1.835  32.466 -17.635  1.00 17.05           H  
+ATOM   3567  N   LYS A 311       5.925  30.920 -18.541  1.00 11.80           N  
+ATOM   3568  CA  LYS A 311       7.172  30.260 -18.902  1.00 12.87           C  
+ATOM   3569  C   LYS A 311       8.313  30.702 -17.988  1.00 11.64           C  
+ATOM   3570  O   LYS A 311       9.094  29.867 -17.512  1.00 13.85           O  
+ATOM   3571  CB  LYS A 311       7.497  30.545 -20.372  1.00 15.34           C  
+ATOM   3572  CG  LYS A 311       8.875  30.086 -20.771  1.00 24.10           C  
+ATOM   3573  CD  LYS A 311       9.105  30.217 -22.272  1.00 30.63           C  
+ATOM   3574  CE  LYS A 311      10.601  30.290 -22.562  1.00 50.05           C  
+ATOM   3575  NZ  LYS A 311      10.963  31.484 -23.383  1.00 53.36           N  
+ATOM   3576  H   LYS A 311       5.565  31.368 -19.182  1.00 14.16           H  
+ATOM   3577  HA  LYS A 311       7.068  29.301 -18.798  1.00 15.44           H  
+ATOM   3578  HB2 LYS A 311       6.854  30.083 -20.931  1.00 18.40           H  
+ATOM   3579  HB3 LYS A 311       7.444  31.501 -20.526  1.00 18.40           H  
+ATOM   3580  HG2 LYS A 311       9.538  30.627 -20.314  1.00 28.92           H  
+ATOM   3581  HG3 LYS A 311       8.985  29.153 -20.528  1.00 28.92           H  
+ATOM   3582  HD2 LYS A 311       8.736  29.445 -22.729  1.00 36.75           H  
+ATOM   3583  HD3 LYS A 311       8.684  31.028 -22.598  1.00 36.75           H  
+ATOM   3584  HE2 LYS A 311      11.085  30.343 -21.723  1.00 60.06           H  
+ATOM   3585  HE3 LYS A 311      10.869  29.496 -23.050  1.00 60.06           H  
+ATOM   3586  HZ1 LYS A 311      11.829  31.461 -23.589  1.00 64.04           H  
+ATOM   3587  HZ2 LYS A 311      10.487  31.491 -24.135  1.00 64.04           H  
+ATOM   3588  HZ3 LYS A 311      10.794  32.229 -22.927  1.00 64.04           H  
+ATOM   3589  N   GLU A 312       8.437  32.012 -17.749  1.00 12.86           N  
+ATOM   3590  CA  GLU A 312       9.534  32.525 -16.946  1.00 13.30           C  
+ATOM   3591  C   GLU A 312       9.409  32.088 -15.490  1.00 14.60           C  
+ATOM   3592  O   GLU A 312      10.418  31.800 -14.832  1.00 16.17           O  
+ATOM   3593  CB  GLU A 312       9.609  34.048 -17.040  1.00 18.78           C  
+ATOM   3594  CG  GLU A 312      10.853  34.637 -16.401  1.00 21.18           C  
+ATOM   3595  CD  GLU A 312      12.154  34.309 -17.144  1.00 29.11           C  
+ATOM   3596  OE1 GLU A 312      12.134  33.506 -18.099  1.00 29.64           O  
+ATOM   3597  OE2 GLU A 312      13.198  34.875 -16.762  1.00 35.72           O  
+ATOM   3598  H   GLU A 312       7.900  32.616 -18.042  1.00 15.43           H  
+ATOM   3599  HA  GLU A 312      10.363  32.167 -17.301  1.00 15.96           H  
+ATOM   3600  HB2 GLU A 312       9.607  34.303 -17.976  1.00 22.53           H  
+ATOM   3601  HB3 GLU A 312       8.837  34.427 -16.592  1.00 22.53           H  
+ATOM   3602  HG2 GLU A 312      10.763  35.603 -16.377  1.00 25.42           H  
+ATOM   3603  HG3 GLU A 312      10.934  34.290 -15.499  1.00 25.42           H  
+ATOM   3604  N   LEU A 313       8.183  32.019 -14.961  1.00 13.81           N  
+ATOM   3605  CA  LEU A 313       7.996  31.460 -13.624  1.00 13.51           C  
+ATOM   3606  C   LEU A 313       8.545  30.037 -13.554  1.00 11.89           C  
+ATOM   3607  O   LEU A 313       9.253  29.673 -12.605  1.00 12.80           O  
+ATOM   3608  CB  LEU A 313       6.511  31.493 -13.242  1.00 12.87           C  
+ATOM   3609  CG  LEU A 313       5.997  32.848 -12.790  1.00 11.86           C  
+ATOM   3610  CD1 LEU A 313       4.460  32.859 -12.793  1.00 13.51           C  
+ATOM   3611  CD2 LEU A 313       6.531  33.228 -11.411  1.00 14.95           C  
+ATOM   3612  H   LEU A 313       7.462  32.283 -15.348  1.00 16.57           H  
+ATOM   3613  HA  LEU A 313       8.479  32.004 -12.982  1.00 16.22           H  
+ATOM   3614  HB2 LEU A 313       5.989  31.226 -14.014  1.00 15.44           H  
+ATOM   3615  HB3 LEU A 313       6.368  30.869 -12.513  1.00 15.44           H  
+ATOM   3616  HG  LEU A 313       6.318  33.519 -13.414  1.00 14.23           H  
+ATOM   3617 HD11 LEU A 313       4.150  33.730 -12.501  1.00 16.22           H  
+ATOM   3618 HD12 LEU A 313       4.145  32.681 -13.693  1.00 16.22           H  
+ATOM   3619 HD13 LEU A 313       4.138  32.173 -12.188  1.00 16.22           H  
+ATOM   3620 HD21 LEU A 313       6.125  34.063 -11.133  1.00 17.93           H  
+ATOM   3621 HD22 LEU A 313       6.306  32.525 -10.781  1.00 17.93           H  
+ATOM   3622 HD23 LEU A 313       7.495  33.329 -11.462  1.00 17.93           H  
+ATOM   3623  N   ILE A 314       8.234  29.212 -14.553  1.00 12.64           N  
+ATOM   3624  CA  ILE A 314       8.740  27.847 -14.554  1.00 12.03           C  
+ATOM   3625  C   ILE A 314      10.257  27.855 -14.631  1.00 12.23           C  
+ATOM   3626  O   ILE A 314      10.926  27.099 -13.921  1.00 12.80           O  
+ATOM   3627  CB  ILE A 314       8.128  27.044 -15.715  1.00 15.41           C  
+ATOM   3628  CG1 ILE A 314       6.601  26.941 -15.563  1.00 15.94           C  
+ATOM   3629  CG2 ILE A 314       8.728  25.663 -15.804  1.00 14.89           C  
+ATOM   3630  CD1 ILE A 314       6.118  26.400 -14.226  1.00 14.69           C  
+ATOM   3631  H   ILE A 314       7.741  29.416 -15.227  1.00 15.17           H  
+ATOM   3632  HA  ILE A 314       8.475  27.420 -13.724  1.00 14.44           H  
+ATOM   3633  HB  ILE A 314       8.332  27.522 -16.534  1.00 18.49           H  
+ATOM   3634 HG12 ILE A 314       6.223  27.827 -15.671  1.00 19.13           H  
+ATOM   3635 HG13 ILE A 314       6.264  26.349 -16.254  1.00 19.13           H  
+ATOM   3636 HG21 ILE A 314       8.179  25.118 -16.389  1.00 17.86           H  
+ATOM   3637 HG22 ILE A 314       9.627  25.732 -16.163  1.00 17.86           H  
+ATOM   3638 HG23 ILE A 314       8.755  25.273 -14.917  1.00 17.86           H  
+ATOM   3639 HD11 ILE A 314       5.173  26.189 -14.294  1.00 17.63           H  
+ATOM   3640 HD12 ILE A 314       6.621  25.600 -14.008  1.00 17.63           H  
+ATOM   3641 HD13 ILE A 314       6.257  27.075 -13.543  1.00 17.63           H  
+ATOM   3642  N   ARG A 315      10.817  28.695 -15.502  1.00 14.55           N  
+ATOM   3643  CA  ARG A 315      12.266  28.677 -15.697  1.00 15.42           C  
+ATOM   3644  C   ARG A 315      13.013  29.101 -14.445  1.00 17.39           C  
+ATOM   3645  O   ARG A 315      14.168  28.691 -14.253  1.00 19.02           O  
+ATOM   3646  CB  ARG A 315      12.638  29.559 -16.878  1.00 17.59           C  
+ATOM   3647  CG  ARG A 315      12.234  28.901 -18.171  1.00 23.31           C  
+ATOM   3648  CD  ARG A 315      12.462  29.789 -19.368  1.00 35.04           C  
+ATOM   3649  NE  ARG A 315      13.876  29.913 -19.690  1.00 48.01           N  
+ATOM   3650  CZ  ARG A 315      14.519  29.147 -20.563  1.00 56.56           C  
+ATOM   3651  NH1 ARG A 315      13.903  28.177 -21.223  1.00 53.58           N  
+ATOM   3652  NH2 ARG A 315      15.814  29.359 -20.779  1.00 65.22           N  
+ATOM   3653  H   ARG A 315      10.392  29.270 -15.980  1.00 17.46           H  
+ATOM   3654  HA  ARG A 315      12.543  27.770 -15.902  1.00 18.50           H  
+ATOM   3655  HB2 ARG A 315      12.178  30.410 -16.805  1.00 21.11           H  
+ATOM   3656  HB3 ARG A 315      13.598  29.700 -16.888  1.00 21.11           H  
+ATOM   3657  HG2 ARG A 315      12.757  28.093 -18.292  1.00 27.98           H  
+ATOM   3658  HG3 ARG A 315      11.290  28.683 -18.134  1.00 27.98           H  
+ATOM   3659  HD2 ARG A 315      12.007  29.411 -20.137  1.00 42.04           H  
+ATOM   3660  HD3 ARG A 315      12.114  30.675 -19.180  1.00 42.04           H  
+ATOM   3661  HE  ARG A 315      14.326  30.525 -19.287  1.00 57.61           H  
+ATOM   3662 HH11 ARG A 315      13.066  28.031 -21.091  1.00 64.30           H  
+ATOM   3663 HH12 ARG A 315      14.340  27.693 -21.784  1.00 64.30           H  
+ATOM   3664 HH21 ARG A 315      16.223  29.986 -20.355  1.00 78.27           H  
+ATOM   3665 HH22 ARG A 315      16.242  28.870 -21.342  1.00 78.27           H  
+ATOM   3666  N   LYS A 316      12.375  29.900 -13.591  1.00 17.11           N  
+ATOM   3667  CA  LYS A 316      12.927  30.339 -12.318  1.00 14.63           C  
+ATOM   3668  C   LYS A 316      12.565  29.418 -11.159  1.00 16.72           C  
+ATOM   3669  O   LYS A 316      12.759  29.793  -9.997  1.00 20.11           O  
+ATOM   3670  CB  LYS A 316      12.446  31.763 -12.017  1.00 18.30           C  
+ATOM   3671  CG  LYS A 316      12.919  32.800 -13.029  1.00 25.46           C  
+ATOM   3672  CD  LYS A 316      14.407  33.040 -12.894  1.00 30.65           C  
+ATOM   3673  CE  LYS A 316      14.736  34.513 -13.041  1.00 40.14           C  
+ATOM   3674  NZ  LYS A 316      14.247  35.067 -14.340  1.00 49.31           N  
+ATOM   3675  H   LYS A 316      11.587  30.213 -13.736  1.00 20.53           H  
+ATOM   3676  HA  LYS A 316      13.895  30.348 -12.388  1.00 17.55           H  
+ATOM   3677  HB2 LYS A 316      11.476  31.771 -12.017  1.00 21.96           H  
+ATOM   3678  HB3 LYS A 316      12.780  32.027 -11.145  1.00 21.96           H  
+ATOM   3679  HG2 LYS A 316      12.738  32.483 -13.927  1.00 30.55           H  
+ATOM   3680  HG3 LYS A 316      12.457  33.639 -12.874  1.00 30.55           H  
+ATOM   3681  HD2 LYS A 316      14.704  32.745 -12.019  1.00 36.78           H  
+ATOM   3682  HD3 LYS A 316      14.878  32.550 -13.587  1.00 36.78           H  
+ATOM   3683  HE2 LYS A 316      14.313  35.008 -12.322  1.00 48.16           H  
+ATOM   3684  HE3 LYS A 316      15.698  34.631 -13.004  1.00 48.16           H  
+ATOM   3685  HZ1 LYS A 316      13.363  34.981 -14.394  1.00 59.17           H  
+ATOM   3686  HZ2 LYS A 316      14.622  34.629 -15.018  1.00 59.17           H  
+ATOM   3687  HZ3 LYS A 316      14.458  35.929 -14.401  1.00 59.17           H  
+ATOM   3688  N   ASP A 317      12.069  28.215 -11.448  1.00 13.31           N  
+ATOM   3689  CA  ASP A 317      11.843  27.148 -10.477  1.00 14.46           C  
+ATOM   3690  C   ASP A 317      10.676  27.428  -9.550  1.00 19.43           C  
+ATOM   3691  O   ASP A 317      10.646  26.948  -8.418  1.00 23.16           O  
+ATOM   3692  CB  ASP A 317      13.121  26.852  -9.688  1.00 19.95           C  
+ATOM   3693  CG  ASP A 317      14.190  26.251 -10.577  1.00 30.38           C  
+ATOM   3694  OD1 ASP A 317      13.905  25.220 -11.218  1.00 36.96           O  
+ATOM   3695  OD2 ASP A 317      15.279  26.844 -10.687  1.00 39.19           O  
+ATOM   3696  H   ASP A 317      11.844  27.981 -12.244  1.00 15.98           H  
+ATOM   3697  HA  ASP A 317      11.601  26.345 -10.963  1.00 17.35           H  
+ATOM   3698  HB2 ASP A 317      13.465  27.677  -9.311  1.00 23.95           H  
+ATOM   3699  HB3 ASP A 317      12.922  26.221  -8.979  1.00 23.95           H  
+ATOM   3700  N   PHE A 318       9.691  28.168 -10.040  1.00 13.12           N  
+ATOM   3701  CA  PHE A 318       8.411  28.256  -9.366  1.00 14.19           C  
+ATOM   3702  C   PHE A 318       7.479  27.180  -9.905  1.00 12.89           C  
+ATOM   3703  O   PHE A 318       7.625  26.698 -11.036  1.00 14.14           O  
+ATOM   3704  CB  PHE A 318       7.767  29.615  -9.570  1.00 10.75           C  
+ATOM   3705  CG  PHE A 318       8.500  30.743  -8.927  1.00 14.65           C  
+ATOM   3706  CD1 PHE A 318       8.249  31.078  -7.613  1.00 16.17           C  
+ATOM   3707  CD2 PHE A 318       9.444  31.471  -9.623  1.00 13.56           C  
+ATOM   3708  CE1 PHE A 318       8.928  32.126  -7.019  1.00 15.41           C  
+ATOM   3709  CE2 PHE A 318      10.109  32.508  -9.049  1.00 14.60           C  
+ATOM   3710  CZ  PHE A 318       9.866  32.840  -7.741  1.00 14.76           C  
+ATOM   3711  H   PHE A 318       9.743  28.628 -10.764  1.00 15.74           H  
+ATOM   3712  HA  PHE A 318       8.546  28.132  -8.414  1.00 17.03           H  
+ATOM   3713  HB2 PHE A 318       7.722  29.797 -10.521  1.00 12.90           H  
+ATOM   3714  HB3 PHE A 318       6.873  29.593  -9.194  1.00 12.90           H  
+ATOM   3715  HD1 PHE A 318       7.620  30.598  -7.125  1.00 19.41           H  
+ATOM   3716  HD2 PHE A 318       9.630  31.246 -10.506  1.00 16.27           H  
+ATOM   3717  HE1 PHE A 318       8.753  32.350  -6.134  1.00 18.49           H  
+ATOM   3718  HE2 PHE A 318      10.729  32.993  -9.544  1.00 17.53           H  
+ATOM   3719  HZ  PHE A 318      10.330  33.541  -7.342  1.00 17.72           H  
+ATOM   3720  N   ASN A 319       6.507  26.816  -9.081  1.00 11.20           N  
+ATOM   3721  CA  ASN A 319       5.347  26.054  -9.501  1.00  9.99           C  
+ATOM   3722  C   ASN A 319       4.159  26.998  -9.541  1.00  9.57           C  
+ATOM   3723  O   ASN A 319       4.167  28.037  -8.866  1.00 10.72           O  
+ATOM   3724  CB  ASN A 319       5.062  24.877  -8.565  1.00 11.80           C  
+ATOM   3725  CG  ASN A 319       6.260  23.963  -8.421  1.00 15.78           C  
+ATOM   3726  OD1 ASN A 319       6.976  23.708  -9.376  1.00 12.80           O  
+ATOM   3727  ND2 ASN A 319       6.475  23.454  -7.212  1.00 17.23           N  
+ATOM   3728  H   ASN A 319       6.499  27.008  -8.242  1.00 13.44           H  
+ATOM   3729  HA  ASN A 319       5.492  25.673 -10.381  1.00 11.99           H  
+ATOM   3730  HB2 ASN A 319       4.832  25.217  -7.686  1.00 14.16           H  
+ATOM   3731  HB3 ASN A 319       4.325  24.357  -8.922  1.00 14.16           H  
+ATOM   3732 HD21 ASN A 319       7.143  22.928  -7.079  1.00 20.67           H  
+ATOM   3733 HD22 ASN A 319       5.947  23.649  -6.562  1.00 20.67           H  
+ATOM   3734  N   ILE A 320       3.165  26.669 -10.364  1.00 10.10           N  
+ATOM   3735  CA  ILE A 320       1.990  27.512 -10.576  1.00  8.79           C  
+ATOM   3736  C   ILE A 320       0.723  26.728 -10.290  1.00  9.52           C  
+ATOM   3737  O   ILE A 320       0.554  25.624 -10.812  1.00 10.39           O  
+ATOM   3738  CB  ILE A 320       1.942  28.040 -12.021  1.00  8.47           C  
+ATOM   3739  CG1 ILE A 320       3.148  28.905 -12.342  1.00 11.37           C  
+ATOM   3740  CG2 ILE A 320       0.628  28.785 -12.230  1.00 11.98           C  
+ATOM   3741  CD1 ILE A 320       3.297  29.166 -13.843  1.00 11.29           C  
+ATOM   3742  H   ILE A 320       3.149  25.942 -10.824  1.00 12.12           H  
+ATOM   3743  HA  ILE A 320       2.035  28.248  -9.946  1.00 10.54           H  
+ATOM   3744  HB  ILE A 320       1.982  27.292 -12.637  1.00 10.17           H  
+ATOM   3745 HG12 ILE A 320       3.053  29.761 -11.895  1.00 13.65           H  
+ATOM   3746 HG13 ILE A 320       3.951  28.458 -12.032  1.00 13.65           H  
+ATOM   3747 HG21 ILE A 320       0.723  29.390 -12.981  1.00 14.37           H  
+ATOM   3748 HG22 ILE A 320      -0.075  28.141 -12.411  1.00 14.37           H  
+ATOM   3749 HG23 ILE A 320       0.418  29.286 -11.426  1.00 14.37           H  
+ATOM   3750 HD11 ILE A 320       4.164  29.569 -14.009  1.00 13.55           H  
+ATOM   3751 HD12 ILE A 320       3.228  28.324 -14.318  1.00 13.55           H  
+ATOM   3752 HD13 ILE A 320       2.593  29.768 -14.130  1.00 13.55           H  
+ATOM   3753  N   VAL A 321      -0.189  27.318  -9.490  1.00  9.66           N  
+ATOM   3754  CA  VAL A 321      -1.577  26.854  -9.401  1.00  8.98           C  
+ATOM   3755  C   VAL A 321      -2.432  27.827 -10.209  1.00  8.15           C  
+ATOM   3756  O   VAL A 321      -2.318  29.052 -10.046  1.00  9.96           O  
+ATOM   3757  CB  VAL A 321      -2.072  26.782  -7.947  1.00  8.09           C  
+ATOM   3758  CG1 VAL A 321      -3.522  26.329  -7.889  1.00  8.43           C  
+ATOM   3759  CG2 VAL A 321      -1.201  25.850  -7.122  1.00 10.82           C  
+ATOM   3760  H   VAL A 321      -0.018  27.994  -8.987  1.00 11.60           H  
+ATOM   3761  HA  VAL A 321      -1.642  25.963  -9.778  1.00 10.78           H  
+ATOM   3762  HB  VAL A 321      -2.013  27.672  -7.566  1.00  9.71           H  
+ATOM   3763 HG11 VAL A 321      -3.760  26.149  -6.966  1.00 10.11           H  
+ATOM   3764 HG12 VAL A 321      -4.087  27.032  -8.245  1.00 10.11           H  
+ATOM   3765 HG13 VAL A 321      -3.623  25.522  -8.419  1.00 10.11           H  
+ATOM   3766 HG21 VAL A 321      -1.483  25.893  -6.194  1.00 12.99           H  
+ATOM   3767 HG22 VAL A 321      -1.302  24.945  -7.456  1.00 12.99           H  
+ATOM   3768 HG23 VAL A 321      -0.276  26.131  -7.199  1.00 12.99           H  
+ATOM   3769  N   SER A 322      -3.275  27.291 -11.081  1.00  8.42           N  
+ATOM   3770  CA  SER A 322      -4.137  28.095 -11.930  1.00  9.18           C  
+ATOM   3771  C   SER A 322      -5.542  27.528 -11.914  1.00  8.50           C  
+ATOM   3772  O   SER A 322      -5.729  26.310 -12.079  1.00 10.29           O  
+ATOM   3773  CB  SER A 322      -3.611  28.118 -13.375  1.00  9.98           C  
+ATOM   3774  OG  SER A 322      -4.567  28.672 -14.272  1.00 11.22           O  
+ATOM   3775  H   SER A 322      -3.367  26.444 -11.201  1.00 10.10           H  
+ATOM   3776  HA  SER A 322      -4.168  29.001 -11.585  1.00 11.02           H  
+ATOM   3777  HB2 SER A 322      -2.805  28.657 -13.405  1.00 11.98           H  
+ATOM   3778  HB3 SER A 322      -3.414  27.209 -13.650  1.00 11.98           H  
+ATOM   3779  HG  SER A 322      -4.746  29.462 -14.050  1.00 13.47           H  
+ATOM   3780  N   GLY A 323      -6.522  28.412 -11.757  1.00  8.46           N  
+ATOM   3781  CA  GLY A 323      -7.915  28.036 -11.878  1.00  8.94           C  
+ATOM   3782  C   GLY A 323      -8.485  28.169 -13.279  1.00 10.18           C  
+ATOM   3783  O   GLY A 323      -9.708  28.152 -13.440  1.00  9.47           O  
+ATOM   3784  H   GLY A 323      -6.400  29.244 -11.578  1.00 10.15           H  
+ATOM   3785  HA2 GLY A 323      -8.014  27.111 -11.603  1.00 10.73           H  
+ATOM   3786  HA3 GLY A 323      -8.443  28.598 -11.288  1.00 10.73           H  
+ATOM   3787  N   PHE A 324      -7.629  28.267 -14.304  1.00  9.80           N  
+ATOM   3788  CA  PHE A 324      -8.079  28.163 -15.698  1.00  9.53           C  
+ATOM   3789  C   PHE A 324      -9.116  29.254 -16.010  1.00  9.08           C  
+ATOM   3790  O   PHE A 324     -10.174  29.009 -16.597  1.00 10.86           O  
+ATOM   3791  CB  PHE A 324      -8.629  26.742 -15.976  1.00  8.92           C  
+ATOM   3792  CG  PHE A 324      -8.875  26.429 -17.440  1.00 10.39           C  
+ATOM   3793  CD1 PHE A 324      -7.844  26.431 -18.375  1.00  8.57           C  
+ATOM   3794  CD2 PHE A 324     -10.146  26.107 -17.869  1.00 10.20           C  
+ATOM   3795  CE1 PHE A 324      -8.083  26.127 -19.715  1.00 11.26           C  
+ATOM   3796  CE2 PHE A 324     -10.390  25.823 -19.218  1.00 10.53           C  
+ATOM   3797  CZ  PHE A 324      -9.370  25.818 -20.125  1.00 10.93           C  
+ATOM   3798  H   PHE A 324      -6.783  28.394 -14.217  1.00 11.76           H  
+ATOM   3799  HA  PHE A 324      -7.330  28.308 -16.297  1.00 11.44           H  
+ATOM   3800  HB2 PHE A 324      -7.990  26.094 -15.642  1.00 10.70           H  
+ATOM   3801  HB3 PHE A 324      -9.475  26.644 -15.511  1.00 10.70           H  
+ATOM   3802  HD1 PHE A 324      -6.980  26.639 -18.101  1.00 10.29           H  
+ATOM   3803  HD2 PHE A 324     -10.846  26.078 -17.258  1.00 12.24           H  
+ATOM   3804  HE1 PHE A 324      -7.384  26.131 -20.329  1.00 13.51           H  
+ATOM   3805  HE2 PHE A 324     -11.256  25.636 -19.499  1.00 12.63           H  
+ATOM   3806  HZ  PHE A 324      -9.539  25.608 -21.015  1.00 13.12           H  
+ATOM   3807  N   GLY A 325      -8.800  30.488 -15.611  1.00  9.18           N  
+ATOM   3808  CA  GLY A 325      -9.722  31.582 -15.825  1.00 10.10           C  
+ATOM   3809  C   GLY A 325      -9.859  31.934 -17.287  1.00 10.47           C  
+ATOM   3810  O   GLY A 325      -8.908  31.852 -18.072  1.00 10.77           O  
+ATOM   3811  H   GLY A 325      -8.066  30.708 -15.221  1.00 11.02           H  
+ATOM   3812  HA2 GLY A 325     -10.597  31.336 -15.486  1.00 12.13           H  
+ATOM   3813  HA3 GLY A 325      -9.408  32.366 -15.349  1.00 12.13           H  
+ATOM   3814  N   LEU A 326     -11.068  32.325 -17.681  1.00  9.75           N  
+ATOM   3815  CA  LEU A 326     -11.279  32.745 -19.072  1.00 11.01           C  
+ATOM   3816  C   LEU A 326     -10.294  33.841 -19.449  1.00  9.96           C  
+ATOM   3817  O   LEU A 326     -10.062  34.789 -18.678  1.00 11.26           O  
+ATOM   3818  CB  LEU A 326     -12.692  33.271 -19.289  1.00 12.07           C  
+ATOM   3819  CG  LEU A 326     -13.843  32.312 -19.139  1.00 13.33           C  
+ATOM   3820  CD1 LEU A 326     -15.134  33.072 -19.380  1.00 13.72           C  
+ATOM   3821  CD2 LEU A 326     -13.697  31.171 -20.106  1.00 15.11           C  
+ATOM   3822  H   LEU A 326     -11.766  32.357 -17.180  1.00 11.70           H  
+ATOM   3823  HA  LEU A 326     -11.150  31.969 -19.641  1.00 13.21           H  
+ATOM   3824  HB2 LEU A 326     -12.840  33.985 -18.649  1.00 14.48           H  
+ATOM   3825  HB3 LEU A 326     -12.739  33.621 -20.193  1.00 14.48           H  
+ATOM   3826  HG  LEU A 326     -13.861  31.932 -18.246  1.00 16.00           H  
+ATOM   3827 HD11 LEU A 326     -15.882  32.461 -19.284  1.00 16.46           H  
+ATOM   3828 HD12 LEU A 326     -15.205  33.788 -18.730  1.00 16.46           H  
+ATOM   3829 HD13 LEU A 326     -15.120  33.440 -20.277  1.00 16.46           H  
+ATOM   3830 HD21 LEU A 326     -14.512  30.645 -20.099  1.00 18.13           H  
+ATOM   3831 HD22 LEU A 326     -13.541  31.528 -20.994  1.00 18.13           H  
+ATOM   3832 HD23 LEU A 326     -12.946  30.620 -19.834  1.00 18.13           H  
+ATOM   3833  N   GLY A 327      -9.716  33.714 -20.645  1.00 10.25           N  
+ATOM   3834  CA  GLY A 327      -8.813  34.720 -21.159  1.00 12.36           C  
+ATOM   3835  C   GLY A 327      -7.429  34.701 -20.574  1.00 12.01           C  
+ATOM   3836  O   GLY A 327      -6.605  35.537 -20.958  1.00 11.85           O  
+ATOM   3837  H   GLY A 327      -9.836  33.047 -21.174  1.00 12.30           H  
+ATOM   3838  HA2 GLY A 327      -8.729  34.597 -22.118  1.00 14.84           H  
+ATOM   3839  HA3 GLY A 327      -9.194  35.595 -20.985  1.00 14.84           H  
+ATOM   3840  N   VAL A 328      -7.147  33.769 -19.658  1.00 10.54           N  
+ATOM   3841  CA  VAL A 328      -5.872  33.721 -18.950  1.00 10.49           C  
+ATOM   3842  C   VAL A 328      -5.336  32.297 -18.907  1.00 10.70           C  
+ATOM   3843  O   VAL A 328      -4.189  32.044 -19.297  1.00 10.10           O  
+ATOM   3844  CB  VAL A 328      -6.027  34.300 -17.536  1.00 10.25           C  
+ATOM   3845  CG1 VAL A 328      -4.754  34.113 -16.722  1.00 12.79           C  
+ATOM   3846  CG2 VAL A 328      -6.437  35.769 -17.620  1.00 11.32           C  
+ATOM   3847  H   VAL A 328      -7.690  33.144 -19.427  1.00 12.64           H  
+ATOM   3848  HA  VAL A 328      -5.223  34.249 -19.441  1.00 12.59           H  
+ATOM   3849  HB  VAL A 328      -6.728  33.820 -17.067  1.00 12.30           H  
+ATOM   3850 HG11 VAL A 328      -4.796  34.678 -15.935  1.00 15.35           H  
+ATOM   3851 HG12 VAL A 328      -4.681  33.182 -16.458  1.00 15.35           H  
+ATOM   3852 HG13 VAL A 328      -3.991  34.362 -17.267  1.00 15.35           H  
+ATOM   3853 HG21 VAL A 328      -6.437  36.149 -16.727  1.00 13.58           H  
+ATOM   3854 HG22 VAL A 328      -5.802  36.243 -18.181  1.00 13.58           H  
+ATOM   3855 HG23 VAL A 328      -7.326  35.828 -18.004  1.00 13.58           H  
+ATOM   3856  N   GLY A 329      -6.171  31.354 -18.459  1.00 10.74           N  
+ATOM   3857  CA  GLY A 329      -5.669  30.024 -18.138  1.00 11.14           C  
+ATOM   3858  C   GLY A 329      -5.063  29.285 -19.320  1.00  8.99           C  
+ATOM   3859  O   GLY A 329      -4.068  28.570 -19.171  1.00 10.48           O  
+ATOM   3860  H   GLY A 329      -7.015  31.459 -18.336  1.00 12.89           H  
+ATOM   3861  HA2 GLY A 329      -4.985  30.103 -17.454  1.00 13.36           H  
+ATOM   3862  HA3 GLY A 329      -6.399  29.487 -17.794  1.00 13.36           H  
+ATOM   3863  N   SER A 330      -5.680  29.404 -20.497  1.00  9.82           N  
+ATOM   3864  CA  SER A 330      -5.164  28.719 -21.670  1.00 10.20           C  
+ATOM   3865  C   SER A 330      -3.738  29.163 -21.966  1.00  9.90           C  
+ATOM   3866  O   SER A 330      -2.903  28.365 -22.407  1.00 10.63           O  
+ATOM   3867  CB  SER A 330      -6.059  28.996 -22.878  1.00 11.04           C  
+ATOM   3868  OG  SER A 330      -7.249  28.239 -22.815  1.00 11.26           O  
+ATOM   3869  H   SER A 330      -6.390  29.869 -20.636  1.00 11.79           H  
+ATOM   3870  HA  SER A 330      -5.167  27.764 -21.503  1.00 12.24           H  
+ATOM   3871  HB2 SER A 330      -6.287  29.939 -22.892  1.00 13.25           H  
+ATOM   3872  HB3 SER A 330      -5.578  28.760 -23.687  1.00 13.25           H  
+ATOM   3873  HG  SER A 330      -7.677  28.433 -22.119  1.00 13.51           H  
+ATOM   3874  N   PHE A 331      -3.436  30.440 -21.725  1.00 10.75           N  
+ATOM   3875  CA  PHE A 331      -2.118  30.979 -22.078  1.00 11.16           C  
+ATOM   3876  C   PHE A 331      -1.085  30.640 -21.018  1.00 11.09           C  
+ATOM   3877  O   PHE A 331       0.100  30.481 -21.347  1.00 11.39           O  
+ATOM   3878  CB  PHE A 331      -2.274  32.477 -22.351  1.00 11.21           C  
+ATOM   3879  CG  PHE A 331      -3.426  32.724 -23.251  1.00 10.64           C  
+ATOM   3880  CD1 PHE A 331      -3.401  32.227 -24.539  1.00 12.64           C  
+ATOM   3881  CD2 PHE A 331      -4.591  33.289 -22.777  1.00 14.46           C  
+ATOM   3882  CE1 PHE A 331      -4.493  32.355 -25.373  1.00 15.87           C  
+ATOM   3883  CE2 PHE A 331      -5.701  33.406 -23.607  1.00 15.21           C  
+ATOM   3884  CZ  PHE A 331      -5.637  32.938 -24.912  1.00 16.83           C  
+ATOM   3885  H   PHE A 331      -3.969  31.009 -21.362  1.00 12.90           H  
+ATOM   3886  HA  PHE A 331      -1.769  30.592 -22.897  1.00 13.39           H  
+ATOM   3887  HB2 PHE A 331      -2.429  32.944 -21.515  1.00 13.45           H  
+ATOM   3888  HB3 PHE A 331      -1.471  32.815 -22.776  1.00 13.45           H  
+ATOM   3889  HD1 PHE A 331      -2.636  31.799 -24.849  1.00 15.17           H  
+ATOM   3890  HD2 PHE A 331      -4.635  33.593 -21.900  1.00 17.35           H  
+ATOM   3891  HE1 PHE A 331      -4.450  32.044 -26.248  1.00 19.05           H  
+ATOM   3892  HE2 PHE A 331      -6.483  33.796 -23.289  1.00 18.25           H  
+ATOM   3893  HZ  PHE A 331      -6.375  33.022 -25.473  1.00 20.20           H  
+ATOM   3894  N   VAL A 332      -1.515  30.496 -19.766  1.00  9.82           N  
+ATOM   3895  CA  VAL A 332      -0.654  29.902 -18.738  1.00  9.56           C  
+ATOM   3896  C   VAL A 332      -0.226  28.497 -19.157  1.00 11.21           C  
+ATOM   3897  O   VAL A 332       0.960  28.139 -19.108  1.00 10.27           O  
+ATOM   3898  CB  VAL A 332      -1.395  29.896 -17.382  1.00  9.46           C  
+ATOM   3899  CG1 VAL A 332      -0.568  29.192 -16.304  1.00 10.24           C  
+ATOM   3900  CG2 VAL A 332      -1.751  31.323 -16.950  1.00 10.66           C  
+ATOM   3901  H   VAL A 332      -2.293  30.730 -19.484  1.00 11.78           H  
+ATOM   3902  HA  VAL A 332       0.150  30.437 -18.643  1.00 11.47           H  
+ATOM   3903  HB  VAL A 332      -2.222  29.400 -17.490  1.00 11.36           H  
+ATOM   3904 HG11 VAL A 332      -0.987  29.335 -15.441  1.00 12.28           H  
+ATOM   3905 HG12 VAL A 332      -0.532  28.244 -16.502  1.00 12.28           H  
+ATOM   3906 HG13 VAL A 332       0.329  29.564 -16.301  1.00 12.28           H  
+ATOM   3907 HG21 VAL A 332      -2.175  31.293 -16.078  1.00 12.79           H  
+ATOM   3908 HG22 VAL A 332      -0.938  31.851 -16.904  1.00 12.79           H  
+ATOM   3909 HG23 VAL A 332      -2.359  31.708 -17.600  1.00 12.79           H  
+ATOM   3910  N   ILE A 333      -1.208  27.663 -19.536  1.00 10.14           N  
+ATOM   3911  CA  ILE A 333      -0.918  26.301 -19.979  1.00  8.56           C  
+ATOM   3912  C   ILE A 333       0.036  26.324 -21.164  1.00 10.58           C  
+ATOM   3913  O   ILE A 333       1.038  25.593 -21.194  1.00 11.59           O  
+ATOM   3914  CB  ILE A 333      -2.221  25.554 -20.317  1.00  9.05           C  
+ATOM   3915  CG1 ILE A 333      -3.058  25.330 -19.053  1.00  9.93           C  
+ATOM   3916  CG2 ILE A 333      -1.913  24.219 -20.990  1.00  9.59           C  
+ATOM   3917  CD1 ILE A 333      -4.474  24.903 -19.334  1.00 10.93           C  
+ATOM   3918  H   ILE A 333      -2.044  27.865 -19.545  1.00 12.16           H  
+ATOM   3919  HA  ILE A 333      -0.484  25.826 -19.253  1.00 10.27           H  
+ATOM   3920  HB  ILE A 333      -2.733  26.104 -20.932  1.00 10.86           H  
+ATOM   3921 HG12 ILE A 333      -2.639  24.636 -18.521  1.00 11.92           H  
+ATOM   3922 HG13 ILE A 333      -3.093  26.159 -18.551  1.00 11.92           H  
+ATOM   3923 HG21 ILE A 333      -2.712  23.669 -20.982  1.00 11.51           H  
+ATOM   3924 HG22 ILE A 333      -1.634  24.384 -21.905  1.00 11.51           H  
+ATOM   3925 HG23 ILE A 333      -1.201  23.777 -20.502  1.00 11.51           H  
+ATOM   3926 HD11 ILE A 333      -4.995  24.982 -18.519  1.00 13.11           H  
+ATOM   3927 HD12 ILE A 333      -4.847  25.476 -20.022  1.00 13.11           H  
+ATOM   3928 HD13 ILE A 333      -4.472  23.981 -19.636  1.00 13.11           H  
+ATOM   3929  N   ASN A 334      -0.234  27.188 -22.145  1.00 10.49           N  
+ATOM   3930  CA  ASN A 334       0.610  27.232 -23.335  1.00 10.89           C  
+ATOM   3931  C   ASN A 334       2.065  27.513 -22.969  1.00 11.22           C  
+ATOM   3932  O   ASN A 334       2.985  26.870 -23.481  1.00 12.47           O  
+ATOM   3933  CB  ASN A 334       0.116  28.287 -24.318  1.00 10.37           C  
+ATOM   3934  CG  ASN A 334      -1.172  27.890 -25.034  1.00 12.29           C  
+ATOM   3935  OD1 ASN A 334      -1.552  26.711 -25.096  1.00 12.77           O  
+ATOM   3936  ND2 ASN A 334      -1.832  28.885 -25.610  1.00 12.79           N  
+ATOM   3937  H   ASN A 334      -0.887  27.748 -22.145  1.00 12.58           H  
+ATOM   3938  HA  ASN A 334       0.554  26.365 -23.768  1.00 13.07           H  
+ATOM   3939  HB2 ASN A 334      -0.054  29.111 -23.835  1.00 12.44           H  
+ATOM   3940  HB3 ASN A 334       0.798  28.433 -24.992  1.00 12.44           H  
+ATOM   3941 HD21 ASN A 334      -2.566  28.728 -26.030  1.00 15.35           H  
+ATOM   3942 HD22 ASN A 334      -1.527  29.688 -25.564  1.00 15.35           H  
+ATOM   3943  N   GLY A 335       2.293  28.487 -22.088  1.00  9.81           N  
+ATOM   3944  CA  GLY A 335       3.650  28.816 -21.699  1.00 10.45           C  
+ATOM   3945  C   GLY A 335       4.329  27.698 -20.947  1.00 12.71           C  
+ATOM   3946  O   GLY A 335       5.509  27.410 -21.166  1.00 13.92           O  
+ATOM   3947  H   GLY A 335       1.684  28.962 -21.708  1.00 11.77           H  
+ATOM   3948  HA2 GLY A 335       4.172  29.008 -22.494  1.00 12.54           H  
+ATOM   3949  HA3 GLY A 335       3.639  29.602 -21.131  1.00 12.54           H  
+ATOM   3950  N   VAL A 336       3.596  27.037 -20.053  1.00 10.75           N  
+ATOM   3951  CA  VAL A 336       4.200  25.951 -19.306  1.00 10.71           C  
+ATOM   3952  C   VAL A 336       4.494  24.774 -20.223  1.00 11.57           C  
+ATOM   3953  O   VAL A 336       5.576  24.193 -20.168  1.00 12.34           O  
+ATOM   3954  CB  VAL A 336       3.309  25.539 -18.124  1.00 11.31           C  
+ATOM   3955  CG1 VAL A 336       3.862  24.270 -17.464  1.00 11.39           C  
+ATOM   3956  CG2 VAL A 336       3.229  26.667 -17.124  1.00 12.73           C  
+ATOM   3957  H   VAL A 336       2.772  27.197 -19.869  1.00 12.90           H  
+ATOM   3958  HA  VAL A 336       5.043  26.266 -18.942  1.00 12.85           H  
+ATOM   3959  HB  VAL A 336       2.413  25.348 -18.443  1.00 13.57           H  
+ATOM   3960 HG11 VAL A 336       3.492  24.191 -16.571  1.00 13.66           H  
+ATOM   3961 HG12 VAL A 336       3.607  23.500 -17.997  1.00 13.66           H  
+ATOM   3962 HG13 VAL A 336       4.829  24.334 -17.417  1.00 13.66           H  
+ATOM   3963 HG21 VAL A 336       2.700  26.378 -16.363  1.00 15.27           H  
+ATOM   3964 HG22 VAL A 336       4.126  26.896 -16.835  1.00 15.27           H  
+ATOM   3965 HG23 VAL A 336       2.811  27.434 -17.545  1.00 15.27           H  
+ATOM   3966  N   LEU A 337       3.538  24.396 -21.079  1.00 10.44           N  
+ATOM   3967  CA  LEU A 337       3.754  23.246 -21.964  1.00 10.91           C  
+ATOM   3968  C   LEU A 337       4.931  23.495 -22.901  1.00 12.76           C  
+ATOM   3969  O   LEU A 337       5.684  22.568 -23.209  1.00 13.20           O  
+ATOM   3970  CB  LEU A 337       2.493  22.914 -22.761  1.00 13.91           C  
+ATOM   3971  CG  LEU A 337       1.275  22.412 -21.974  1.00 12.00           C  
+ATOM   3972  CD1 LEU A 337       0.170  22.021 -22.958  1.00 15.46           C  
+ATOM   3973  CD2 LEU A 337       1.625  21.254 -21.051  1.00 14.52           C  
+ATOM   3974  H   LEU A 337       2.773  24.780 -21.166  1.00 12.53           H  
+ATOM   3975  HA  LEU A 337       3.953  22.473 -21.413  1.00 13.09           H  
+ATOM   3976  HB2 LEU A 337       2.215  23.719 -23.227  1.00 16.70           H  
+ATOM   3977  HB3 LEU A 337       2.719  22.222 -23.402  1.00 16.70           H  
+ATOM   3978  HG  LEU A 337       0.954  23.124 -21.398  1.00 14.40           H  
+ATOM   3979 HD11 LEU A 337      -0.598  21.702 -22.460  1.00 18.55           H  
+ATOM   3980 HD12 LEU A 337      -0.076  22.800 -23.482  1.00 18.55           H  
+ATOM   3981 HD13 LEU A 337       0.501  21.321 -23.542  1.00 18.55           H  
+ATOM   3982 HD21 LEU A 337       0.806  20.877 -20.692  1.00 17.43           H  
+ATOM   3983 HD22 LEU A 337       2.105  20.581 -21.558  1.00 17.43           H  
+ATOM   3984 HD23 LEU A 337       2.182  21.583 -20.328  1.00 17.43           H  
+ATOM   3985  N   GLU A 338       5.119  24.734 -23.356  1.00 12.78           N  
+ATOM   3986  CA  GLU A 338       6.285  25.002 -24.193  1.00 15.39           C  
+ATOM   3987  C   GLU A 338       7.563  24.614 -23.459  1.00 15.26           C  
+ATOM   3988  O   GLU A 338       8.424  23.921 -24.011  1.00 19.05           O  
+ATOM   3989  CB  GLU A 338       6.329  26.480 -24.600  1.00 16.90           C  
+ATOM   3990  CG  GLU A 338       7.431  26.766 -25.652  1.00 21.79           C  
+ATOM   3991  CD  GLU A 338       7.557  28.227 -26.067  1.00 37.55           C  
+ATOM   3992  OE1 GLU A 338       7.222  29.129 -25.281  1.00 21.13           O  
+ATOM   3993  OE2 GLU A 338       8.018  28.483 -27.205  1.00 40.33           O  
+ATOM   3994  H   GLU A 338       4.608  25.408 -23.202  1.00 15.34           H  
+ATOM   3995  HA  GLU A 338       6.215  24.476 -25.005  1.00 18.47           H  
+ATOM   3996  HB2 GLU A 338       5.473  26.729 -24.983  1.00 20.28           H  
+ATOM   3997  HB3 GLU A 338       6.512  27.020 -23.816  1.00 20.28           H  
+ATOM   3998  HG2 GLU A 338       8.286  26.493 -25.284  1.00 26.15           H  
+ATOM   3999  HG3 GLU A 338       7.234  26.252 -26.451  1.00 26.15           H  
+ATOM   4000  N   GLU A 339       7.690  25.044 -22.208  1.00 15.92           N  
+ATOM   4001  CA  GLU A 339       8.895  24.777 -21.430  1.00 18.21           C  
+ATOM   4002  C   GLU A 339       9.016  23.296 -21.098  1.00 18.66           C  
+ATOM   4003  O   GLU A 339      10.094  22.705 -21.260  1.00 19.46           O  
+ATOM   4004  CB  GLU A 339       8.878  25.640 -20.170  1.00 19.90           C  
+ATOM   4005  CG  GLU A 339      10.082  25.493 -19.264  1.00 24.31           C  
+ATOM   4006  CD  GLU A 339      11.376  25.969 -19.899  1.00 33.66           C  
+ATOM   4007  OE1 GLU A 339      11.329  26.746 -20.882  1.00 30.70           O  
+ATOM   4008  OE2 GLU A 339      12.439  25.559 -19.393  1.00 34.87           O  
+ATOM   4009  H   GLU A 339       7.092  25.495 -21.785  1.00 19.11           H  
+ATOM   4010  HA  GLU A 339       9.681  25.017 -21.945  1.00 21.85           H  
+ATOM   4011  HB2 GLU A 339       8.830  26.571 -20.438  1.00 23.87           H  
+ATOM   4012  HB3 GLU A 339       8.094  25.405 -19.649  1.00 23.87           H  
+ATOM   4013  HG2 GLU A 339       9.936  26.016 -18.460  1.00 29.17           H  
+ATOM   4014  HG3 GLU A 339      10.190  24.557 -19.035  1.00 29.17           H  
+ATOM   4015  N   LEU A 340       7.921  22.660 -20.678  1.00 13.34           N  
+ATOM   4016  CA  LEU A 340       7.994  21.246 -20.343  1.00 14.08           C  
+ATOM   4017  C   LEU A 340       8.361  20.405 -21.555  1.00 14.58           C  
+ATOM   4018  O   LEU A 340       9.245  19.544 -21.488  1.00 16.36           O  
+ATOM   4019  CB  LEU A 340       6.660  20.752 -19.775  1.00 16.96           C  
+ATOM   4020  CG  LEU A 340       6.205  21.326 -18.444  1.00 20.63           C  
+ATOM   4021  CD1 LEU A 340       4.915  20.622 -18.073  1.00 17.59           C  
+ATOM   4022  CD2 LEU A 340       7.237  21.153 -17.348  1.00 24.65           C  
+ATOM   4023  H   LEU A 340       7.146  23.019 -20.581  1.00 16.00           H  
+ATOM   4024  HA  LEU A 340       8.680  21.142 -19.665  1.00 16.89           H  
+ATOM   4025  HB2 LEU A 340       5.968  20.961 -20.422  1.00 20.35           H  
+ATOM   4026  HB3 LEU A 340       6.726  19.791 -19.658  1.00 20.35           H  
+ATOM   4027  HG  LEU A 340       6.073  22.283 -18.528  1.00 24.75           H  
+ATOM   4028 HD11 LEU A 340       4.601  20.965 -17.222  1.00 21.10           H  
+ATOM   4029 HD12 LEU A 340       4.253  20.791 -18.762  1.00 21.10           H  
+ATOM   4030 HD13 LEU A 340       5.084  19.669 -18.003  1.00 21.10           H  
+ATOM   4031 HD21 LEU A 340       6.854  21.442 -16.505  1.00 29.59           H  
+ATOM   4032 HD22 LEU A 340       7.486  20.217 -17.293  1.00 29.59           H  
+ATOM   4033 HD23 LEU A 340       8.016  21.691 -17.559  1.00 29.59           H  
+ATOM   4034  N   TYR A 341       7.681  20.624 -22.668  1.00 13.80           N  
+ATOM   4035  CA  TYR A 341       7.800  19.696 -23.779  1.00 12.69           C  
+ATOM   4036  C   TYR A 341       9.085  19.916 -24.564  1.00 16.06           C  
+ATOM   4037  O   TYR A 341       9.613  18.953 -25.138  1.00 17.28           O  
+ATOM   4038  CB  TYR A 341       6.558  19.757 -24.663  1.00 13.03           C  
+ATOM   4039  CG  TYR A 341       5.298  19.210 -23.993  1.00 13.39           C  
+ATOM   4040  CD1 TYR A 341       5.364  18.408 -22.859  1.00 15.11           C  
+ATOM   4041  CD2 TYR A 341       4.027  19.478 -24.514  1.00 14.31           C  
+ATOM   4042  CE1 TYR A 341       4.210  17.911 -22.246  1.00 14.91           C  
+ATOM   4043  CE2 TYR A 341       2.880  18.980 -23.915  1.00 14.64           C  
+ATOM   4044  CZ  TYR A 341       2.962  18.196 -22.795  1.00 13.65           C  
+ATOM   4045  OH  TYR A 341       1.830  17.696 -22.175  1.00 13.27           O  
+ATOM   4046  H   TYR A 341       7.154  21.289 -22.804  1.00 16.55           H  
+ATOM   4047  HA  TYR A 341       7.837  18.788 -23.439  1.00 15.22           H  
+ATOM   4048  HB2 TYR A 341       6.389  20.682 -24.901  1.00 15.64           H  
+ATOM   4049  HB3 TYR A 341       6.719  19.233 -25.464  1.00 15.64           H  
+ATOM   4050  HD1 TYR A 341       6.195  18.198 -22.499  1.00 18.13           H  
+ATOM   4051  HD2 TYR A 341       3.950  20.002 -25.279  1.00 17.17           H  
+ATOM   4052  HE1 TYR A 341       4.276  17.392 -21.476  1.00 17.89           H  
+ATOM   4053  HE2 TYR A 341       2.047  19.180 -24.278  1.00 17.57           H  
+ATOM   4054  HH  TYR A 341       2.047  17.252 -21.496  1.00 15.92           H  
+ATOM   4055  N   MET A 342       9.649  21.127 -24.544  1.00 15.09           N  
+ATOM   4056  CA  MET A 342      10.979  21.283 -25.141  1.00 19.28           C  
+ATOM   4057  C   MET A 342      12.016  20.476 -24.370  1.00 19.22           C  
+ATOM   4058  O   MET A 342      13.086  20.173 -24.917  1.00 19.67           O  
+ATOM   4059  CB  MET A 342      11.366  22.762 -25.222  1.00 21.51           C  
+ATOM   4060  CG  MET A 342      12.191  23.306 -24.099  1.00 31.66           C  
+ATOM   4061  SD  MET A 342      12.838  24.952 -24.514  1.00 60.20           S  
+ATOM   4062  CE  MET A 342      11.377  25.964 -24.289  1.00 40.54           C  
+ATOM   4063  H   MET A 342       9.302  21.838 -24.208  1.00 18.11           H  
+ATOM   4064  HA  MET A 342      10.960  20.968 -26.058  1.00 23.14           H  
+ATOM   4065  HB2 MET A 342      11.875  22.894 -26.037  1.00 25.82           H  
+ATOM   4066  HB3 MET A 342      10.550  23.284 -25.252  1.00 25.82           H  
+ATOM   4067  HG2 MET A 342      11.644  23.381 -23.302  1.00 37.99           H  
+ATOM   4068  HG3 MET A 342      12.941  22.713 -23.932  1.00 37.99           H  
+ATOM   4069  HE1 MET A 342      11.560  26.859 -24.615  1.00 48.65           H  
+ATOM   4070  HE2 MET A 342      10.643  25.574 -24.789  1.00 48.65           H  
+ATOM   4071  HE3 MET A 342      11.156  25.994 -23.345  1.00 48.65           H  
+ATOM   4072  N   ASN A 343      11.707  20.093 -23.131  1.00 15.45           N  
+ATOM   4073  CA  ASN A 343      12.601  19.296 -22.296  1.00 14.50           C  
+ATOM   4074  C   ASN A 343      12.120  17.859 -22.105  1.00 16.28           C  
+ATOM   4075  O   ASN A 343      12.560  17.184 -21.165  1.00 14.71           O  
+ATOM   4076  CB  ASN A 343      12.777  19.976 -20.940  1.00 15.41           C  
+ATOM   4077  CG  ASN A 343      13.676  21.185 -21.030  1.00 21.22           C  
+ATOM   4078  OD1 ASN A 343      14.901  21.055 -21.118  1.00 20.11           O  
+ATOM   4079  ND2 ASN A 343      13.078  22.366 -21.057  1.00 20.03           N  
+ATOM   4080  H   ASN A 343      10.965  20.290 -22.742  1.00 18.54           H  
+ATOM   4081  HA  ASN A 343      13.464  19.247 -22.736  1.00 17.40           H  
+ATOM   4082  HB2 ASN A 343      11.911  20.265 -20.613  1.00 18.49           H  
+ATOM   4083  HB3 ASN A 343      13.174  19.348 -20.317  1.00 18.49           H  
+ATOM   4084 HD21 ASN A 343      13.548  23.084 -21.107  1.00 24.04           H  
+ATOM   4085 HD22 ASN A 343      12.220  22.414 -21.023  1.00 24.04           H  
+ATOM   4086  N   GLN A 344      11.225  17.374 -22.976  1.00 17.15           N  
+ATOM   4087  CA  GLN A 344      10.677  16.016 -22.907  1.00 15.70           C  
+ATOM   4088  C   GLN A 344      10.038  15.733 -21.553  1.00 14.20           C  
+ATOM   4089  O   GLN A 344      10.042  14.596 -21.066  1.00 16.19           O  
+ATOM   4090  CB  GLN A 344      11.745  14.954 -23.213  1.00 18.34           C  
+ATOM   4091  CG  GLN A 344      12.507  15.175 -24.502  1.00 26.72           C  
+ATOM   4092  CD  GLN A 344      11.597  15.322 -25.685  1.00 37.72           C  
+ATOM   4093  OE1 GLN A 344      10.735  14.475 -25.931  1.00 38.99           O  
+ATOM   4094  NE2 GLN A 344      11.767  16.415 -26.424  1.00 37.38           N  
+ATOM   4095  H   GLN A 344      10.911  17.827 -23.636  1.00 20.57           H  
+ATOM   4096  HA  GLN A 344       9.986  15.947 -23.583  1.00 18.84           H  
+ATOM   4097  HB2 GLN A 344      12.391  14.948 -22.489  1.00 22.01           H  
+ATOM   4098  HB3 GLN A 344      11.310  14.089 -23.275  1.00 22.01           H  
+ATOM   4099  HG2 GLN A 344      13.033  15.986 -24.424  1.00 32.07           H  
+ATOM   4100  HG3 GLN A 344      13.089  14.416 -24.661  1.00 32.07           H  
+ATOM   4101 HE21 GLN A 344      12.372  16.988 -26.212  1.00 44.86           H  
+ATOM   4102 HE22 GLN A 344      11.272  16.548 -27.115  1.00 44.86           H  
+ATOM   4103  N   GLY A 345       9.452  16.764 -20.952  1.00 13.78           N  
+ATOM   4104  CA  GLY A 345       8.859  16.670 -19.637  1.00 15.09           C  
+ATOM   4105  C   GLY A 345       7.386  16.309 -19.674  1.00 14.78           C  
+ATOM   4106  O   GLY A 345       6.817  15.958 -20.711  1.00 15.09           O  
+ATOM   4107  H   GLY A 345       9.387  17.547 -21.301  1.00 16.53           H  
+ATOM   4108  HA2 GLY A 345       9.324  15.991 -19.125  1.00 18.11           H  
+ATOM   4109  HA3 GLY A 345       8.950  17.524 -19.185  1.00 18.11           H  
+ATOM   4110  N   THR A 346       6.767  16.387 -18.491  1.00 14.86           N  
+ATOM   4111  CA  THR A 346       5.409  15.899 -18.310  1.00 13.88           C  
+ATOM   4112  C   THR A 346       4.620  16.804 -17.384  1.00 11.16           C  
+ATOM   4113  O   THR A 346       5.128  17.302 -16.377  1.00 12.42           O  
+ATOM   4114  CB  THR A 346       5.382  14.455 -17.746  1.00 14.68           C  
+ATOM   4115  OG1 THR A 346       4.031  14.092 -17.403  1.00 14.59           O  
+ATOM   4116  CG2 THR A 346       6.262  14.286 -16.514  1.00 17.34           C  
+ATOM   4117  H   THR A 346       7.120  16.720 -17.781  1.00 17.83           H  
+ATOM   4118  HA  THR A 346       4.976  15.911 -19.178  1.00 16.66           H  
+ATOM   4119  HB  THR A 346       5.731  13.864 -18.431  1.00 17.62           H  
+ATOM   4120  HG1 THR A 346       3.544  14.119 -18.087  1.00 17.51           H  
+ATOM   4121 HG21 THR A 346       6.198  13.377 -16.183  1.00 20.80           H  
+ATOM   4122 HG22 THR A 346       7.187  14.475 -16.739  1.00 20.80           H  
+ATOM   4123 HG23 THR A 346       5.977  14.897 -15.816  1.00 20.80           H  
+ATOM   4124  N   ILE A 347       3.339  16.966 -17.717  1.00 11.36           N  
+ATOM   4125  CA  ILE A 347       2.411  17.645 -16.832  1.00 12.19           C  
+ATOM   4126  C   ILE A 347       2.343  16.979 -15.465  1.00 12.73           C  
+ATOM   4127  O   ILE A 347       1.948  17.630 -14.492  1.00 14.44           O  
+ATOM   4128  CB  ILE A 347       1.031  17.714 -17.549  1.00 12.26           C  
+ATOM   4129  CG1 ILE A 347       0.104  18.722 -16.873  1.00 13.19           C  
+ATOM   4130  CG2 ILE A 347       0.392  16.312 -17.661  1.00 15.60           C  
+ATOM   4131  CD1 ILE A 347       0.512  20.172 -17.124  1.00 16.78           C  
+ATOM   4132  H   ILE A 347       2.987  16.690 -18.452  1.00 13.64           H  
+ATOM   4133  HA  ILE A 347       2.708  18.552 -16.658  1.00 14.63           H  
+ATOM   4134  HB  ILE A 347       1.179  18.034 -18.453  1.00 14.72           H  
+ATOM   4135 HG12 ILE A 347      -0.795  18.601 -17.215  1.00 15.83           H  
+ATOM   4136 HG13 ILE A 347       0.119  18.569 -15.916  1.00 15.83           H  
+ATOM   4137 HG21 ILE A 347      -0.400  16.369 -18.217  1.00 18.71           H  
+ATOM   4138 HG22 ILE A 347       1.033  15.704 -18.059  1.00 18.71           H  
+ATOM   4139 HG23 ILE A 347       0.151  16.004 -16.773  1.00 18.71           H  
+ATOM   4140 HD11 ILE A 347      -0.162  20.759 -16.746  1.00 20.14           H  
+ATOM   4141 HD12 ILE A 347       1.369  20.337 -16.702  1.00 20.14           H  
+ATOM   4142 HD13 ILE A 347       0.580  20.320 -18.080  1.00 20.14           H  
+ATOM   4143  N   ASP A 348       2.708  15.694 -15.357  1.00 14.03           N  
+ATOM   4144  CA  ASP A 348       2.679  15.003 -14.071  1.00 14.09           C  
+ATOM   4145  C   ASP A 348       3.774  15.461 -13.110  1.00 15.25           C  
+ATOM   4146  O   ASP A 348       3.730  15.068 -11.934  1.00 19.79           O  
+ATOM   4147  CB  ASP A 348       2.782  13.493 -14.279  1.00 13.09           C  
+ATOM   4148  CG  ASP A 348       1.512  12.881 -14.863  1.00 14.92           C  
+ATOM   4149  OD1 ASP A 348       0.441  13.540 -14.888  1.00 14.67           O  
+ATOM   4150  OD2 ASP A 348       1.593  11.713 -15.302  1.00 17.09           O  
+ATOM   4151  H   ASP A 348       2.975  15.206 -16.013  1.00 16.83           H  
+ATOM   4152  HA  ASP A 348       1.825  15.193 -13.651  1.00 16.90           H  
+ATOM   4153  HB2 ASP A 348       3.511  13.309 -14.892  1.00 15.71           H  
+ATOM   4154  HB3 ASP A 348       2.952  13.068 -13.423  1.00 15.71           H  
+ATOM   4155  N   ASP A 349       4.724  16.288 -13.561  1.00 15.52           N  
+ATOM   4156  CA  ASP A 349       5.780  16.789 -12.680  1.00 17.50           C  
+ATOM   4157  C   ASP A 349       5.273  17.851 -11.705  1.00 18.11           C  
+ATOM   4158  O   ASP A 349       6.044  18.284 -10.839  1.00 21.09           O  
+ATOM   4159  CB  ASP A 349       6.942  17.369 -13.504  1.00 17.37           C  
+ATOM   4160  CG  ASP A 349       7.834  16.302 -14.143  1.00 29.31           C  
+ATOM   4161  OD1 ASP A 349       7.971  15.202 -13.560  1.00 28.42           O  
+ATOM   4162  OD2 ASP A 349       8.407  16.579 -15.236  1.00 36.78           O  
+ATOM   4163  H   ASP A 349       4.778  16.572 -14.371  1.00 18.63           H  
+ATOM   4164  HA  ASP A 349       6.127  16.042 -12.167  1.00 21.00           H  
+ATOM   4165  HB2 ASP A 349       6.577  17.916 -14.217  1.00 20.84           H  
+ATOM   4166  HB3 ASP A 349       7.498  17.910 -12.922  1.00 20.84           H  
+ATOM   4167  N   ASP A 350       4.014  18.276 -11.832  1.00 16.59           N  
+ATOM   4168  CA  ASP A 350       3.353  19.190 -10.901  1.00 19.35           C  
+ATOM   4169  C   ASP A 350       4.069  20.533 -10.798  1.00 16.48           C  
+ATOM   4170  O   ASP A 350       4.063  21.194  -9.756  1.00 20.14           O  
+ATOM   4171  CB  ASP A 350       3.178  18.528  -9.540  1.00 23.97           C  
+ATOM   4172  CG  ASP A 350       2.080  17.464  -9.555  1.00 34.73           C  
+ATOM   4173  OD1 ASP A 350       1.360  17.357 -10.586  1.00 28.95           O  
+ATOM   4174  OD2 ASP A 350       1.939  16.735  -8.551  1.00 39.07           O  
+ATOM   4175  H   ASP A 350       3.500  18.038 -12.479  1.00 19.91           H  
+ATOM   4176  HA  ASP A 350       2.468  19.397 -11.240  1.00 23.22           H  
+ATOM   4177  HB2 ASP A 350       4.010  18.100  -9.284  1.00 28.77           H  
+ATOM   4178  HB3 ASP A 350       2.937  19.202  -8.886  1.00 28.77           H  
+ATOM   4179  N   ARG A 351       4.637  20.970 -11.907  1.00 13.15           N  
+ATOM   4180  CA  ARG A 351       5.050  22.354 -12.038  1.00 12.73           C  
+ATOM   4181  C   ARG A 351       3.850  23.264 -12.265  1.00 11.31           C  
+ATOM   4182  O   ARG A 351       3.902  24.449 -11.928  1.00 13.69           O  
+ATOM   4183  CB  ARG A 351       6.026  22.518 -13.200  1.00 14.05           C  
+ATOM   4184  CG  ARG A 351       7.270  21.619 -13.129  1.00 18.41           C  
+ATOM   4185  CD  ARG A 351       8.089  21.893 -11.881  1.00 16.57           C  
+ATOM   4186  NE  ARG A 351       8.461  23.296 -11.783  1.00 15.58           N  
+ATOM   4187  CZ  ARG A 351       9.457  23.868 -12.447  1.00 15.20           C  
+ATOM   4188  NH1 ARG A 351      10.254  23.165 -13.240  1.00 17.08           N  
+ATOM   4189  NH2 ARG A 351       9.661  25.166 -12.303  1.00 14.52           N  
+ATOM   4190  H   ARG A 351       4.796  20.486 -12.600  1.00 15.78           H  
+ATOM   4191  HA  ARG A 351       5.508  22.619 -11.225  1.00 15.28           H  
+ATOM   4192  HB2 ARG A 351       5.561  22.307 -14.025  1.00 16.85           H  
+ATOM   4193  HB3 ARG A 351       6.332  23.438 -13.218  1.00 16.85           H  
+ATOM   4194  HG2 ARG A 351       6.993  20.689 -13.112  1.00 22.09           H  
+ATOM   4195  HG3 ARG A 351       7.830  21.785 -13.903  1.00 22.09           H  
+ATOM   4196  HD2 ARG A 351       7.567  21.661 -11.098  1.00 19.88           H  
+ATOM   4197  HD3 ARG A 351       8.901  21.364 -11.908  1.00 19.88           H  
+ATOM   4198  HE  ARG A 351       8.000  23.792 -11.253  1.00 18.69           H  
+ATOM   4199 HH11 ARG A 351      10.131  22.319 -13.334  1.00 20.50           H  
+ATOM   4200 HH12 ARG A 351      10.894  23.555 -13.662  1.00 20.50           H  
+ATOM   4201 HH21 ARG A 351       9.152  25.627 -11.785  1.00 17.43           H  
+ATOM   4202 HH22 ARG A 351      10.303  25.550 -12.727  1.00 17.43           H  
+ATOM   4203  N   LEU A 352       2.798  22.733 -12.888  1.00 11.33           N  
+ATOM   4204  CA  LEU A 352       1.563  23.450 -13.151  1.00 11.15           C  
+ATOM   4205  C   LEU A 352       0.421  22.605 -12.594  1.00  9.85           C  
+ATOM   4206  O   LEU A 352       0.201  21.459 -13.022  1.00 11.54           O  
+ATOM   4207  CB  LEU A 352       1.381  23.722 -14.655  1.00 10.37           C  
+ATOM   4208  CG  LEU A 352       0.039  24.351 -15.015  1.00 10.95           C  
+ATOM   4209  CD1 LEU A 352      -0.182  25.715 -14.393  1.00 11.38           C  
+ATOM   4210  CD2 LEU A 352      -0.087  24.426 -16.553  1.00 11.71           C  
+ATOM   4211  H   LEU A 352       2.780  21.923 -13.177  1.00 13.59           H  
+ATOM   4212  HA  LEU A 352       1.565  24.310 -12.702  1.00 13.37           H  
+ATOM   4213  HB2 LEU A 352       2.080  24.328 -14.947  1.00 12.44           H  
+ATOM   4214  HB3 LEU A 352       1.451  22.880 -15.133  1.00 12.44           H  
+ATOM   4215  HG  LEU A 352      -0.661  23.789 -14.647  1.00 13.14           H  
+ATOM   4216 HD11 LEU A 352      -1.025  26.074 -14.711  1.00 13.65           H  
+ATOM   4217 HD12 LEU A 352      -0.205  25.622 -13.428  1.00 13.65           H  
+ATOM   4218 HD13 LEU A 352       0.546  26.301 -14.652  1.00 13.65           H  
+ATOM   4219 HD21 LEU A 352      -0.932  24.843 -16.781  1.00 14.05           H  
+ATOM   4220 HD22 LEU A 352       0.647  24.954 -16.905  1.00 14.05           H  
+ATOM   4221 HD23 LEU A 352      -0.052  23.528 -16.917  1.00 14.05           H  
+ATOM   4222  N   ILE A 353      -0.298  23.167 -11.635  1.00  9.16           N  
+ATOM   4223  CA  ILE A 353      -1.380  22.517 -10.914  1.00  8.07           C  
+ATOM   4224  C   ILE A 353      -2.671  23.159 -11.377  1.00  9.87           C  
+ATOM   4225  O   ILE A 353      -2.893  24.348 -11.122  1.00 11.87           O  
+ATOM   4226  CB  ILE A 353      -1.209  22.664  -9.396  1.00 10.90           C  
+ATOM   4227  CG1 ILE A 353       0.148  22.120  -8.921  1.00 15.49           C  
+ATOM   4228  CG2 ILE A 353      -2.406  22.026  -8.649  1.00 13.90           C  
+ATOM   4229  CD1 ILE A 353       0.358  20.702  -9.203  1.00 21.80           C  
+ATOM   4230  H   ILE A 353      -0.170  23.975 -11.368  1.00 10.99           H  
+ATOM   4231  HA  ILE A 353      -1.402  21.573 -11.136  1.00  9.69           H  
+ATOM   4232  HB  ILE A 353      -1.207  23.610  -9.183  1.00 13.07           H  
+ATOM   4233 HG12 ILE A 353       0.854  22.616  -9.364  1.00 18.59           H  
+ATOM   4234 HG13 ILE A 353       0.211  22.241  -7.960  1.00 18.59           H  
+ATOM   4235 HG21 ILE A 353      -2.192  21.965  -7.704  1.00 16.68           H  
+ATOM   4236 HG22 ILE A 353      -3.190  22.583  -8.775  1.00 16.68           H  
+ATOM   4237 HG23 ILE A 353      -2.567  21.140  -9.009  1.00 16.68           H  
+ATOM   4238 HD11 ILE A 353       1.132  20.392  -8.708  1.00 26.17           H  
+ATOM   4239 HD12 ILE A 353      -0.429  20.206  -8.931  1.00 26.17           H  
+ATOM   4240 HD13 ILE A 353       0.508  20.588 -10.155  1.00 26.17           H  
+ATOM   4241  N   LEU A 354      -3.514  22.395 -12.069  1.00  9.68           N  
+ATOM   4242  CA  LEU A 354      -4.687  22.946 -12.736  1.00  9.78           C  
+ATOM   4243  C   LEU A 354      -5.955  22.627 -11.967  1.00  8.86           C  
+ATOM   4244  O   LEU A 354      -6.179  21.477 -11.561  1.00 10.41           O  
+ATOM   4245  CB  LEU A 354      -4.786  22.394 -14.164  1.00 10.76           C  
+ATOM   4246  CG  LEU A 354      -3.637  22.857 -15.042  1.00 11.01           C  
+ATOM   4247  CD1 LEU A 354      -3.579  22.011 -16.313  1.00 12.23           C  
+ATOM   4248  CD2 LEU A 354      -3.780  24.334 -15.405  1.00 13.24           C  
+ATOM   4249  H   LEU A 354      -3.425  21.545 -12.166  1.00 11.62           H  
+ATOM   4250  HA  LEU A 354      -4.606  23.912 -12.766  1.00 11.73           H  
+ATOM   4251  HB2 LEU A 354      -4.770  21.424 -14.131  1.00 12.91           H  
+ATOM   4252  HB3 LEU A 354      -5.615  22.698 -14.565  1.00 12.91           H  
+ATOM   4253  HG  LEU A 354      -2.807  22.750 -14.552  1.00 13.21           H  
+ATOM   4254 HD11 LEU A 354      -2.749  22.197 -16.778  1.00 14.67           H  
+ATOM   4255 HD12 LEU A 354      -3.621  21.073 -16.070  1.00 14.67           H  
+ATOM   4256 HD13 LEU A 354      -4.333  22.240 -16.879  1.00 14.67           H  
+ATOM   4257 HD21 LEU A 354      -3.110  24.563 -16.067  1.00 15.89           H  
+ATOM   4258 HD22 LEU A 354      -4.667  24.486 -15.766  1.00 15.89           H  
+ATOM   4259 HD23 LEU A 354      -3.652  24.869 -14.606  1.00 15.89           H  
+ATOM   4260  N   ARG A 355      -6.766  23.655 -11.745  1.00  9.36           N  
+ATOM   4261  CA  ARG A 355      -8.013  23.537 -10.992  1.00 10.74           C  
+ATOM   4262  C   ARG A 355      -9.115  24.278 -11.748  1.00  9.35           C  
+ATOM   4263  O   ARG A 355      -9.641  25.298 -11.286  1.00  9.96           O  
+ATOM   4264  CB  ARG A 355      -7.882  24.084  -9.568  1.00 12.76           C  
+ATOM   4265  CG  ARG A 355      -7.495  23.031  -8.504  1.00 20.17           C  
+ATOM   4266  CD  ARG A 355      -6.048  22.968  -8.473  1.00 18.73           C  
+ATOM   4267  NE  ARG A 355      -5.562  22.002  -7.495  1.00 12.12           N  
+ATOM   4268  CZ  ARG A 355      -5.297  20.735  -7.773  1.00 11.91           C  
+ATOM   4269  NH1 ARG A 355      -5.667  20.185  -8.917  1.00 12.38           N  
+ATOM   4270  NH2 ARG A 355      -4.627  20.005  -6.890  1.00 12.01           N  
+ATOM   4271  H   ARG A 355      -6.612  24.452 -12.028  1.00 11.23           H  
+ATOM   4272  HA  ARG A 355      -8.243  22.597 -10.930  1.00 12.88           H  
+ATOM   4273  HB2 ARG A 355      -7.196  24.770  -9.563  1.00 15.31           H  
+ATOM   4274  HB3 ARG A 355      -8.734  24.465  -9.305  1.00 15.31           H  
+ATOM   4275  HG2 ARG A 355      -7.825  23.296  -7.631  1.00 24.20           H  
+ATOM   4276  HG3 ARG A 355      -7.851  22.162  -8.744  1.00 24.20           H  
+ATOM   4277  HD2 ARG A 355      -5.722  22.703  -9.347  1.00 22.48           H  
+ATOM   4278  HD3 ARG A 355      -5.695  23.840  -8.237  1.00 22.48           H  
+ATOM   4279  HE  ARG A 355      -5.440  22.272  -6.688  1.00 14.55           H  
+ATOM   4280 HH11 ARG A 355      -6.091  20.653  -9.501  1.00 14.86           H  
+ATOM   4281 HH12 ARG A 355      -5.485  19.360  -9.076  1.00 14.86           H  
+ATOM   4282 HH21 ARG A 355      -4.371  20.356  -6.148  1.00 14.41           H  
+ATOM   4283 HH22 ARG A 355      -4.450  19.181  -7.060  1.00 14.41           H  
+ATOM   4284  N   PRO A 356      -9.489  23.787 -12.931  1.00  8.20           N  
+ATOM   4285  CA  PRO A 356     -10.641  24.365 -13.631  1.00 10.04           C  
+ATOM   4286  C   PRO A 356     -11.895  24.296 -12.775  1.00  9.50           C  
+ATOM   4287  O   PRO A 356     -12.089  23.362 -11.978  1.00  9.62           O  
+ATOM   4288  CB  PRO A 356     -10.762  23.497 -14.886  1.00 10.73           C  
+ATOM   4289  CG  PRO A 356     -10.184  22.147 -14.449  1.00  8.93           C  
+ATOM   4290  CD  PRO A 356      -9.028  22.531 -13.541  1.00  9.13           C  
+ATOM   4291  HA  PRO A 356     -10.472  25.286 -13.887  1.00 12.05           H  
+ATOM   4292  HB2 PRO A 356     -11.692  23.414 -15.147  1.00 12.88           H  
+ATOM   4293  HB3 PRO A 356     -10.247  23.883 -15.611  1.00 12.88           H  
+ATOM   4294  HG2 PRO A 356     -10.853  21.634 -13.969  1.00 10.71           H  
+ATOM   4295  HG3 PRO A 356      -9.875  21.649 -15.221  1.00 10.71           H  
+ATOM   4296  HD2 PRO A 356      -8.879  21.852 -12.864  1.00 10.96           H  
+ATOM   4297  HD3 PRO A 356      -8.217  22.672 -14.053  1.00 10.96           H  
+ATOM   4298  N   PHE A 357     -12.752  25.311 -12.935  1.00  9.07           N  
+ATOM   4299  CA  PHE A 357     -13.932  25.448 -12.088  1.00  9.86           C  
+ATOM   4300  C   PHE A 357     -15.127  24.735 -12.717  1.00 10.56           C  
+ATOM   4301  O   PHE A 357     -15.387  24.907 -13.920  1.00 11.15           O  
+ATOM   4302  CB  PHE A 357     -14.278  26.916 -11.880  1.00 10.51           C  
+ATOM   4303  CG  PHE A 357     -13.456  27.585 -10.823  1.00  9.50           C  
+ATOM   4304  CD1 PHE A 357     -12.084  27.708 -10.954  1.00  8.56           C  
+ATOM   4305  CD2 PHE A 357     -14.067  28.137  -9.725  1.00 10.74           C  
+ATOM   4306  CE1 PHE A 357     -11.333  28.342  -9.970  1.00  9.91           C  
+ATOM   4307  CE2 PHE A 357     -13.314  28.772  -8.740  1.00  9.38           C  
+ATOM   4308  CZ  PHE A 357     -11.952  28.867  -8.874  1.00  9.81           C  
+ATOM   4309  H   PHE A 357     -12.670  25.929 -13.528  1.00 10.89           H  
+ATOM   4310  HA  PHE A 357     -13.753  25.045 -11.224  1.00 11.83           H  
+ATOM   4311  HB2 PHE A 357     -14.133  27.391 -12.713  1.00 12.61           H  
+ATOM   4312  HB3 PHE A 357     -15.209  26.982 -11.618  1.00 12.61           H  
+ATOM   4313  HD1 PHE A 357     -11.660  27.363 -11.707  1.00 10.27           H  
+ATOM   4314  HD2 PHE A 357     -14.992  28.087  -9.638  1.00 12.89           H  
+ATOM   4315  HE1 PHE A 357     -10.410  28.408 -10.059  1.00 11.89           H  
+ATOM   4316  HE2 PHE A 357     -13.734  29.132  -7.993  1.00 11.26           H  
+ATOM   4317  HZ  PHE A 357     -11.450  29.290  -8.215  1.00 11.78           H  
+ATOM   4318  N   PRO A 358     -15.862  23.947 -11.940  1.00 10.47           N  
+ATOM   4319  CA  PRO A 358     -17.083  23.320 -12.461  1.00 11.01           C  
+ATOM   4320  C   PRO A 358     -18.149  24.377 -12.708  1.00 10.39           C  
+ATOM   4321  O   PRO A 358     -18.411  25.231 -11.859  1.00 12.23           O  
+ATOM   4322  CB  PRO A 358     -17.478  22.345 -11.353  1.00 10.88           C  
+ATOM   4323  CG  PRO A 358     -16.984  23.011 -10.102  1.00 10.89           C  
+ATOM   4324  CD  PRO A 358     -15.689  23.706 -10.493  1.00 10.64           C  
+ATOM   4325  HA  PRO A 358     -16.915  22.824 -13.277  1.00 13.21           H  
+ATOM   4326  HB2 PRO A 358     -18.441  22.231 -11.334  1.00 13.06           H  
+ATOM   4327  HB3 PRO A 358     -17.045  21.488 -11.490  1.00 13.06           H  
+ATOM   4328  HG2 PRO A 358     -17.640  23.655  -9.792  1.00 13.07           H  
+ATOM   4329  HG3 PRO A 358     -16.824  22.344  -9.417  1.00 13.07           H  
+ATOM   4330  HD2 PRO A 358     -15.586  24.542 -10.012  1.00 12.77           H  
+ATOM   4331  HD3 PRO A 358     -14.925  23.132 -10.327  1.00 12.77           H  
+ATOM   4332  N   GLN A 359     -18.725  24.333 -13.901  1.00 11.27           N  
+ATOM   4333  CA  GLN A 359     -19.681  25.338 -14.340  1.00 13.48           C  
+ATOM   4334  C   GLN A 359     -21.106  24.859 -14.106  1.00 14.24           C  
+ATOM   4335  O   GLN A 359     -21.412  23.674 -14.242  1.00 16.47           O  
+ATOM   4336  CB  GLN A 359     -19.464  25.658 -15.816  1.00 13.05           C  
+ATOM   4337  CG  GLN A 359     -18.056  26.126 -16.127  1.00 13.90           C  
+ATOM   4338  CD  GLN A 359     -17.724  27.448 -15.452  1.00 15.92           C  
+ATOM   4339  OE1 GLN A 359     -18.486  28.410 -15.544  1.00 20.69           O  
+ATOM   4340  NE2 GLN A 359     -16.603  27.490 -14.731  1.00 13.58           N  
+ATOM   4341  H   GLN A 359     -18.576  23.720 -14.485  1.00 13.53           H  
+ATOM   4342  HA  GLN A 359     -19.560  26.153 -13.828  1.00 16.17           H  
+ATOM   4343  HB2 GLN A 359     -19.636  24.859 -16.338  1.00 15.65           H  
+ATOM   4344  HB3 GLN A 359     -20.078  26.363 -16.077  1.00 15.65           H  
+ATOM   4345  HG2 GLN A 359     -17.423  25.460 -15.814  1.00 16.67           H  
+ATOM   4346  HG3 GLN A 359     -17.965  26.245 -17.086  1.00 16.67           H  
+ATOM   4347 HE21 GLN A 359     -16.107  26.790 -14.666  1.00 16.30           H  
+ATOM   4348 HE22 GLN A 359     -16.375  28.216 -14.331  1.00 16.30           H  
+ATOM   4349  N   GLY A 360     -21.986  25.804 -13.769  1.00 15.81           N  
+ATOM   4350  CA  GLY A 360     -23.374  25.505 -13.454  1.00 16.48           C  
+ATOM   4351  C   GLY A 360     -23.655  25.688 -11.971  1.00 19.70           C  
+ATOM   4352  O   GLY A 360     -22.760  25.923 -11.163  1.00 16.97           O  
+ATOM   4353  H   GLY A 360     -21.793  26.640 -13.715  1.00 18.98           H  
+ATOM   4354  HA2 GLY A 360     -23.956  26.098 -13.955  1.00 19.78           H  
+ATOM   4355  HA3 GLY A 360     -23.573  24.588 -13.697  1.00 19.78           H  
+ATOM   4356  N   LYS A 361     -24.934  25.535 -11.611  1.00 20.53           N  
+ATOM   4357  CA  LYS A 361     -25.351  25.888 -10.254  1.00 22.28           C  
+ATOM   4358  C   LYS A 361     -24.686  25.000  -9.206  1.00 18.74           C  
+ATOM   4359  O   LYS A 361     -24.199  25.496  -8.183  1.00 20.00           O  
+ATOM   4360  CB  LYS A 361     -26.877  25.817 -10.112  1.00 31.88           C  
+ATOM   4361  CG  LYS A 361     -27.375  26.296  -8.730  1.00 40.49           C  
+ATOM   4362  CD  LYS A 361     -28.898  26.164  -8.565  1.00 51.60           C  
+ATOM   4363  CE  LYS A 361     -29.411  26.741  -7.229  1.00 57.27           C  
+ATOM   4364  NZ  LYS A 361     -29.265  28.228  -7.086  1.00 53.45           N  
+ATOM   4365  H   LYS A 361     -25.560  25.238 -12.120  1.00 24.63           H  
+ATOM   4366  HA  LYS A 361     -25.076  26.804 -10.095  1.00 26.74           H  
+ATOM   4367  HB2 LYS A 361     -27.283  26.381 -10.789  1.00 38.26           H  
+ATOM   4368  HB3 LYS A 361     -27.163  24.898 -10.232  1.00 38.26           H  
+ATOM   4369  HG2 LYS A 361     -26.952  25.763  -8.039  1.00 48.59           H  
+ATOM   4370  HG3 LYS A 361     -27.142  27.231  -8.616  1.00 48.59           H  
+ATOM   4371  HD2 LYS A 361     -29.336  26.644  -9.285  1.00 61.92           H  
+ATOM   4372  HD3 LYS A 361     -29.138  25.225  -8.597  1.00 61.92           H  
+ATOM   4373  HE2 LYS A 361     -30.355  26.533  -7.146  1.00 68.73           H  
+ATOM   4374  HE3 LYS A 361     -28.915  26.329  -6.504  1.00 68.73           H  
+ATOM   4375  HZ1 LYS A 361     -28.464  28.484  -7.379  1.00 64.13           H  
+ATOM   4376  HZ2 LYS A 361     -29.349  28.461  -6.232  1.00 64.13           H  
+ATOM   4377  HZ3 LYS A 361     -29.892  28.642  -7.562  1.00 64.13           H  
+ATOM   4378  N   LYS A 362     -24.677  23.679  -9.434  1.00 17.74           N  
+ATOM   4379  CA  LYS A 362     -24.045  22.768  -8.485  1.00 20.14           C  
+ATOM   4380  C   LYS A 362     -22.568  23.098  -8.333  1.00 18.12           C  
+ATOM   4381  O   LYS A 362     -22.033  23.117  -7.218  1.00 16.39           O  
+ATOM   4382  CB  LYS A 362     -24.220  21.320  -8.940  1.00 19.76           C  
+ATOM   4383  CG  LYS A 362     -23.592  20.289  -8.006  1.00 28.61           C  
+ATOM   4384  CD  LYS A 362     -24.326  20.186  -6.663  1.00 31.79           C  
+ATOM   4385  CE  LYS A 362     -23.360  19.834  -5.526  1.00 50.27           C  
+ATOM   4386  NZ  LYS A 362     -24.040  19.630  -4.207  1.00 54.93           N  
+ATOM   4387  H   LYS A 362     -25.026  23.296 -10.120  1.00 21.29           H  
+ATOM   4388  HA  LYS A 362     -24.478  22.861  -7.622  1.00 24.16           H  
+ATOM   4389  HB2 LYS A 362     -25.169  21.125  -8.996  1.00 23.71           H  
+ATOM   4390  HB3 LYS A 362     -23.808  21.216  -9.812  1.00 23.71           H  
+ATOM   4391  HG2 LYS A 362     -23.620  19.418  -8.431  1.00 34.33           H  
+ATOM   4392  HG3 LYS A 362     -22.673  20.542  -7.828  1.00 34.33           H  
+ATOM   4393  HD2 LYS A 362     -24.742  21.037  -6.458  1.00 38.14           H  
+ATOM   4394  HD3 LYS A 362     -25.000  19.491  -6.718  1.00 38.14           H  
+ATOM   4395  HE2 LYS A 362     -22.897  19.012  -5.751  1.00 60.32           H  
+ATOM   4396  HE3 LYS A 362     -22.722  20.557  -5.422  1.00 60.32           H  
+ATOM   4397  HZ1 LYS A 362     -24.476  20.370  -3.972  1.00 65.92           H  
+ATOM   4398  HZ2 LYS A 362     -24.621  18.959  -4.265  1.00 65.92           H  
+ATOM   4399  HZ3 LYS A 362     -23.438  19.439  -3.581  1.00 65.92           H  
+ATOM   4400  N   GLY A 363     -21.899  23.357  -9.452  1.00 15.56           N  
+ATOM   4401  CA  GLY A 363     -20.497  23.731  -9.381  1.00 14.74           C  
+ATOM   4402  C   GLY A 363     -20.276  24.974  -8.543  1.00 14.08           C  
+ATOM   4403  O   GLY A 363     -19.376  25.023  -7.696  1.00 13.71           O  
+ATOM   4404  H   GLY A 363     -22.227  23.323 -10.246  1.00 18.67           H  
+ATOM   4405  HA2 GLY A 363     -19.989  23.004  -8.989  1.00 17.68           H  
+ATOM   4406  HA3 GLY A 363     -20.164  23.903 -10.276  1.00 17.68           H  
+ATOM   4407  N   GLU A 364     -21.100  25.998  -8.765  1.00 14.58           N  
+ATOM   4408  CA  GLU A 364     -20.911  27.273  -8.087  1.00 14.50           C  
+ATOM   4409  C   GLU A 364     -21.039  27.125  -6.580  1.00 13.00           C  
+ATOM   4410  O   GLU A 364     -20.417  27.893  -5.835  1.00 14.32           O  
+ATOM   4411  CB  GLU A 364     -21.919  28.300  -8.609  1.00 16.82           C  
+ATOM   4412  CG  GLU A 364     -21.621  28.768  -9.996  1.00 16.51           C  
+ATOM   4413  CD  GLU A 364     -22.640  29.744 -10.537  1.00 26.05           C  
+ATOM   4414  OE1 GLU A 364     -23.311  30.410  -9.726  1.00 29.75           O  
+ATOM   4415  OE2 GLU A 364     -22.768  29.835 -11.781  1.00 24.91           O  
+ATOM   4416  H   GLU A 364     -21.772  25.980  -9.301  1.00 17.50           H  
+ATOM   4417  HA  GLU A 364     -20.019  27.602  -8.282  1.00 17.40           H  
+ATOM   4418  HB2 GLU A 364     -22.802  27.899  -8.613  1.00 20.18           H  
+ATOM   4419  HB3 GLU A 364     -21.908  29.075  -8.024  1.00 20.18           H  
+ATOM   4420  HG2 GLU A 364     -20.757  29.210  -9.998  1.00 19.81           H  
+ATOM   4421  HG3 GLU A 364     -21.602  28.000 -10.588  1.00 19.81           H  
+ATOM   4422  N   GLU A 365     -21.819  26.136  -6.121  1.00 15.17           N  
+ATOM   4423  CA  GLU A 365     -21.980  25.901  -4.689  1.00 18.08           C  
+ATOM   4424  C   GLU A 365     -20.664  25.545  -4.008  1.00 15.07           C  
+ATOM   4425  O   GLU A 365     -20.507  25.771  -2.806  1.00 17.47           O  
+ATOM   4426  CB  GLU A 365     -22.986  24.772  -4.444  1.00 19.53           C  
+ATOM   4427  CG  GLU A 365     -24.409  25.132  -4.787  1.00 22.85           C  
+ATOM   4428  CD  GLU A 365     -25.354  23.934  -4.718  1.00 34.24           C  
+ATOM   4429  OE1 GLU A 365     -24.959  22.873  -4.181  1.00 36.28           O  
+ATOM   4430  OE2 GLU A 365     -26.494  24.058  -5.212  1.00 40.49           O  
+ATOM   4431  H   GLU A 365     -22.262  25.592  -6.618  1.00 18.20           H  
+ATOM   4432  HA  GLU A 365     -22.320  26.719  -4.294  1.00 21.69           H  
+ATOM   4433  HB2 GLU A 365     -22.736  24.009  -4.989  1.00 23.44           H  
+ATOM   4434  HB3 GLU A 365     -22.961  24.531  -3.505  1.00 23.44           H  
+ATOM   4435  HG2 GLU A 365     -24.726  25.800  -4.159  1.00 27.42           H  
+ATOM   4436  HG3 GLU A 365     -24.438  25.485  -5.690  1.00 27.42           H  
+ATOM   4437  N   GLN A 366     -19.711  24.984  -4.754  1.00 15.89           N  
+ATOM   4438  CA  GLN A 366     -18.429  24.567  -4.206  1.00 15.09           C  
+ATOM   4439  C   GLN A 366     -17.295  25.551  -4.476  1.00 12.77           C  
+ATOM   4440  O   GLN A 366     -16.173  25.292  -4.053  1.00 12.44           O  
+ATOM   4441  CB  GLN A 366     -18.041  23.200  -4.778  1.00 16.57           C  
+ATOM   4442  CG  GLN A 366     -18.988  22.060  -4.379  1.00 23.28           C  
+ATOM   4443  CD  GLN A 366     -18.734  21.511  -2.981  1.00 21.75           C  
+ATOM   4444  OE1 GLN A 366     -18.429  22.256  -2.039  1.00 23.36           O  
+ATOM   4445  NE2 GLN A 366     -18.862  20.194  -2.839  1.00 25.31           N  
+ATOM   4446  H   GLN A 366     -19.789  24.833  -5.597  1.00 19.06           H  
+ATOM   4447  HA  GLN A 366     -18.529  24.491  -3.244  1.00 18.11           H  
+ATOM   4448  HB2 GLN A 366     -18.041  23.257  -5.746  1.00 19.89           H  
+ATOM   4449  HB3 GLN A 366     -17.154  22.971  -4.459  1.00 19.89           H  
+ATOM   4450  HG2 GLN A 366     -19.901  22.388  -4.406  1.00 27.94           H  
+ATOM   4451  HG3 GLN A 366     -18.879  21.329  -5.007  1.00 27.94           H  
+ATOM   4452 HE21 GLN A 366     -19.076  19.708  -3.515  1.00 30.38           H  
+ATOM   4453 HE22 GLN A 366     -18.730  19.829  -2.072  1.00 30.38           H  
+ATOM   4454  N   TRP A 367     -17.537  26.648  -5.192  1.00 11.72           N  
+ATOM   4455  CA  TRP A 367     -16.418  27.479  -5.639  1.00 12.66           C  
+ATOM   4456  C   TRP A 367     -15.620  28.069  -4.468  1.00 13.32           C  
+ATOM   4457  O   TRP A 367     -14.388  28.160  -4.538  1.00 12.14           O  
+ATOM   4458  CB  TRP A 367     -16.901  28.603  -6.555  1.00 11.68           C  
+ATOM   4459  CG  TRP A 367     -17.242  28.172  -7.926  1.00 11.74           C  
+ATOM   4460  CD1 TRP A 367     -17.168  26.914  -8.456  1.00 12.43           C  
+ATOM   4461  CD2 TRP A 367     -17.726  29.015  -8.964  1.00 12.64           C  
+ATOM   4462  NE1 TRP A 367     -17.571  26.929  -9.759  1.00 11.20           N  
+ATOM   4463  CE2 TRP A 367     -17.925  28.214 -10.097  1.00 11.54           C  
+ATOM   4464  CE3 TRP A 367     -18.016  30.388  -9.044  1.00 10.83           C  
+ATOM   4465  CZ2 TRP A 367     -18.399  28.737 -11.297  1.00 11.77           C  
+ATOM   4466  CZ3 TRP A 367     -18.475  30.907 -10.240  1.00 12.69           C  
+ATOM   4467  CH2 TRP A 367     -18.678  30.082 -11.345  1.00 11.49           C  
+ATOM   4468  H   TRP A 367     -18.316  26.927  -5.427  1.00 14.07           H  
+ATOM   4469  HA  TRP A 367     -15.824  26.904  -6.146  1.00 15.19           H  
+ATOM   4470  HB2 TRP A 367     -17.698  28.997  -6.166  1.00 14.01           H  
+ATOM   4471  HB3 TRP A 367     -16.200  29.269  -6.623  1.00 14.01           H  
+ATOM   4472  HD1 TRP A 367     -16.884  26.158  -7.995  1.00 14.92           H  
+ATOM   4473  HE1 TRP A 367     -17.598  26.248 -10.283  1.00 13.45           H  
+ATOM   4474  HE3 TRP A 367     -17.900  30.939  -8.303  1.00 13.00           H  
+ATOM   4475  HZ2 TRP A 367     -18.524  28.194 -12.042  1.00 14.13           H  
+ATOM   4476  HZ3 TRP A 367     -18.651  31.818 -10.308  1.00 15.22           H  
+ATOM   4477  HH2 TRP A 367     -19.008  30.450 -12.133  1.00 13.79           H  
+ATOM   4478  N   ASP A 368     -16.292  28.515  -3.406  1.00 12.67           N  
+ATOM   4479  CA  ASP A 368     -15.553  29.088  -2.279  1.00 14.00           C  
+ATOM   4480  C   ASP A 368     -14.661  28.039  -1.607  1.00 12.90           C  
+ATOM   4481  O   ASP A 368     -13.482  28.299  -1.326  1.00 12.54           O  
+ATOM   4482  CB  ASP A 368     -16.524  29.711  -1.270  1.00 15.18           C  
+ATOM   4483  CG  ASP A 368     -15.830  30.205   0.000  1.00 21.43           C  
+ATOM   4484  OD1 ASP A 368     -15.193  31.258  -0.052  1.00 28.65           O  
+ATOM   4485  OD2 ASP A 368     -15.949  29.534   1.053  1.00 29.24           O  
+ATOM   4486  H   ASP A 368     -17.146  28.500  -3.315  1.00 15.21           H  
+ATOM   4487  HA  ASP A 368     -14.979  29.795  -2.613  1.00 16.80           H  
+ATOM   4488  HB2 ASP A 368     -16.966  30.469  -1.684  1.00 18.22           H  
+ATOM   4489  HB3 ASP A 368     -17.181  29.045  -1.012  1.00 18.22           H  
+ATOM   4490  N   LYS A 369     -15.212  26.855  -1.323  1.00 11.00           N  
+ATOM   4491  CA  LYS A 369     -14.420  25.792  -0.722  1.00 12.07           C  
+ATOM   4492  C   LYS A 369     -13.288  25.377  -1.644  1.00 12.10           C  
+ATOM   4493  O   LYS A 369     -12.171  25.104  -1.190  1.00 12.28           O  
+ATOM   4494  CB  LYS A 369     -15.301  24.596  -0.395  1.00 14.76           C  
+ATOM   4495  CG  LYS A 369     -16.126  24.760   0.853  1.00 21.99           C  
+ATOM   4496  CD  LYS A 369     -16.861  23.448   1.163  1.00 31.24           C  
+ATOM   4497  CE  LYS A 369     -17.934  23.647   2.216  1.00 39.74           C  
+ATOM   4498  NZ  LYS A 369     -18.963  22.570   2.140  1.00 48.12           N  
+ATOM   4499  H   LYS A 369     -16.034  26.648  -1.468  1.00 13.20           H  
+ATOM   4500  HA  LYS A 369     -14.039  26.117   0.109  1.00 14.48           H  
+ATOM   4501  HB2 LYS A 369     -15.911  24.449  -1.134  1.00 17.71           H  
+ATOM   4502  HB3 LYS A 369     -14.735  23.818  -0.273  1.00 17.71           H  
+ATOM   4503  HG2 LYS A 369     -15.550  24.979   1.602  1.00 26.39           H  
+ATOM   4504  HG3 LYS A 369     -16.783  25.462   0.723  1.00 26.39           H  
+ATOM   4505  HD2 LYS A 369     -17.284  23.118   0.355  1.00 37.48           H  
+ATOM   4506  HD3 LYS A 369     -16.225  22.795   1.496  1.00 37.48           H  
+ATOM   4507  HE2 LYS A 369     -17.530  23.625   3.098  1.00 47.69           H  
+ATOM   4508  HE3 LYS A 369     -18.371  24.501   2.074  1.00 47.69           H  
+ATOM   4509  HZ1 LYS A 369     -19.339  22.566   1.333  1.00 57.75           H  
+ATOM   4510  HZ2 LYS A 369     -18.585  21.778   2.287  1.00 57.75           H  
+ATOM   4511  HZ3 LYS A 369     -19.594  22.708   2.752  1.00 57.75           H  
+ATOM   4512  N   TYR A 370     -13.580  25.286  -2.945  1.00 11.02           N  
+ATOM   4513  CA  TYR A 370     -12.570  24.890  -3.930  1.00 10.93           C  
+ATOM   4514  C   TYR A 370     -11.422  25.886  -3.981  1.00 10.83           C  
+ATOM   4515  O   TYR A 370     -10.249  25.492  -4.042  1.00 10.74           O  
+ATOM   4516  CB  TYR A 370     -13.258  24.762  -5.285  1.00  9.38           C  
+ATOM   4517  CG  TYR A 370     -12.527  24.136  -6.454  1.00  9.33           C  
+ATOM   4518  CD1 TYR A 370     -11.850  22.943  -6.341  1.00 10.55           C  
+ATOM   4519  CD2 TYR A 370     -12.616  24.706  -7.727  1.00  9.13           C  
+ATOM   4520  CE1 TYR A 370     -11.240  22.348  -7.454  1.00 10.07           C  
+ATOM   4521  CE2 TYR A 370     -12.038  24.136  -8.811  1.00  9.97           C  
+ATOM   4522  CZ  TYR A 370     -11.331  22.962  -8.687  1.00 10.60           C  
+ATOM   4523  OH  TYR A 370     -10.750  22.336  -9.776  1.00 10.90           O  
+ATOM   4524  H   TYR A 370     -14.354  25.448  -3.283  1.00 13.23           H  
+ATOM   4525  HA  TYR A 370     -12.184  24.034  -3.690  1.00 13.12           H  
+ATOM   4526  HB2 TYR A 370     -14.057  24.228  -5.151  1.00 11.26           H  
+ATOM   4527  HB3 TYR A 370     -13.501  25.657  -5.568  1.00 11.26           H  
+ATOM   4528  HD1 TYR A 370     -11.796  22.524  -5.512  1.00 12.66           H  
+ATOM   4529  HD2 TYR A 370     -13.086  25.502  -7.832  1.00 10.95           H  
+ATOM   4530  HE1 TYR A 370     -10.777  21.546  -7.362  1.00 12.09           H  
+ATOM   4531  HE2 TYR A 370     -12.120  24.540  -9.645  1.00 11.97           H  
+ATOM   4532  HH  TYR A 370     -10.944  22.748 -10.482  1.00 13.08           H  
+ATOM   4533  N   ARG A 371     -11.744  27.180  -3.976  1.00 10.52           N  
+ATOM   4534  CA  ARG A 371     -10.699  28.202  -3.944  1.00 10.03           C  
+ATOM   4535  C   ARG A 371      -9.853  28.097  -2.685  1.00 11.20           C  
+ATOM   4536  O   ARG A 371      -8.625  28.143  -2.745  1.00 11.83           O  
+ATOM   4537  CB  ARG A 371     -11.321  29.599  -4.032  1.00 12.34           C  
+ATOM   4538  CG  ARG A 371     -11.731  29.978  -5.414  1.00 12.76           C  
+ATOM   4539  CD  ARG A 371     -12.409  31.327  -5.442  1.00 12.87           C  
+ATOM   4540  NE  ARG A 371     -12.544  31.765  -6.817  1.00 11.53           N  
+ATOM   4541  CZ  ARG A 371     -13.653  32.197  -7.396  1.00 12.39           C  
+ATOM   4542  NH1 ARG A 371     -14.786  32.331  -6.726  1.00 14.13           N  
+ATOM   4543  NH2 ARG A 371     -13.617  32.532  -8.683  1.00 12.67           N  
+ATOM   4544  H   ARG A 371     -12.546  27.488  -3.990  1.00 12.62           H  
+ATOM   4545  HA  ARG A 371     -10.125  28.066  -4.714  1.00 12.03           H  
+ATOM   4546  HB2 ARG A 371     -12.110  29.626  -3.469  1.00 14.81           H  
+ATOM   4547  HB3 ARG A 371     -10.672  30.251  -3.725  1.00 14.81           H  
+ATOM   4548  HG2 ARG A 371     -10.946  30.020  -5.982  1.00 15.31           H  
+ATOM   4549  HG3 ARG A 371     -12.353  29.317  -5.757  1.00 15.31           H  
+ATOM   4550  HD2 ARG A 371     -13.291  31.261  -5.045  1.00 15.44           H  
+ATOM   4551  HD3 ARG A 371     -11.874  31.975  -4.957  1.00 15.44           H  
+ATOM   4552  HE  ARG A 371     -11.836  31.741  -7.304  1.00 13.83           H  
+ATOM   4553 HH11 ARG A 371     -14.816  32.136  -5.889  1.00 16.95           H  
+ATOM   4554 HH12 ARG A 371     -15.492  32.614  -7.127  1.00 16.95           H  
+ATOM   4555 HH21 ARG A 371     -12.882  32.466  -9.125  1.00 15.21           H  
+ATOM   4556 HH22 ARG A 371     -14.329  32.814  -9.074  1.00 15.21           H  
+ATOM   4557  N   ARG A 372     -10.492  27.996  -1.518  1.00 11.36           N  
+ATOM   4558  CA  ARG A 372      -9.725  27.903  -0.279  1.00 11.01           C  
+ATOM   4559  C   ARG A 372      -8.828  26.674  -0.296  1.00 13.02           C  
+ATOM   4560  O   ARG A 372      -7.668  26.731   0.133  1.00 13.93           O  
+ATOM   4561  CB  ARG A 372     -10.677  27.904   0.923  1.00 13.47           C  
+ATOM   4562  CG  ARG A 372     -11.382  29.244   1.070  1.00 15.12           C  
+ATOM   4563  CD  ARG A 372     -12.430  29.280   2.195  1.00 17.69           C  
+ATOM   4564  NE  ARG A 372     -13.075  30.586   2.240  1.00 20.31           N  
+ATOM   4565  CZ  ARG A 372     -12.518  31.673   2.766  1.00 22.46           C  
+ATOM   4566  NH1 ARG A 372     -11.344  31.623   3.375  1.00 22.60           N  
+ATOM   4567  NH2 ARG A 372     -13.133  32.847   2.640  1.00 31.03           N  
+ATOM   4568  H   ARG A 372     -11.347  27.980  -1.420  1.00 13.63           H  
+ATOM   4569  HA  ARG A 372      -9.150  28.679  -0.186  1.00 13.22           H  
+ATOM   4570  HB2 ARG A 372     -11.349  27.215   0.801  1.00 16.16           H  
+ATOM   4571  HB3 ARG A 372     -10.171  27.734   1.733  1.00 16.16           H  
+ATOM   4572  HG2 ARG A 372     -10.720  29.925   1.262  1.00 18.14           H  
+ATOM   4573  HG3 ARG A 372     -11.837  29.449   0.238  1.00 18.14           H  
+ATOM   4574  HD2 ARG A 372     -13.107  28.604   2.033  1.00 21.23           H  
+ATOM   4575  HD3 ARG A 372     -11.998  29.117   3.048  1.00 21.23           H  
+ATOM   4576  HE  ARG A 372     -13.865  30.658   1.905  1.00 24.37           H  
+ATOM   4577 HH11 ARG A 372     -10.924  30.875   3.437  1.00 27.12           H  
+ATOM   4578 HH12 ARG A 372     -11.002  32.338   3.708  1.00 27.12           H  
+ATOM   4579 HH21 ARG A 372     -13.883  32.896   2.222  1.00 37.24           H  
+ATOM   4580 HH22 ARG A 372     -12.781  33.555   2.977  1.00 37.24           H  
+ATOM   4581  N   ASP A 373      -9.330  25.571  -0.846  1.00  9.55           N  
+ATOM   4582  CA  ASP A 373      -8.544  24.349  -0.970  1.00 11.14           C  
+ATOM   4583  C   ASP A 373      -7.348  24.548  -1.897  1.00 10.60           C  
+ATOM   4584  O   ASP A 373      -6.203  24.280  -1.520  1.00 12.12           O  
+ATOM   4585  CB  ASP A 373      -9.479  23.244  -1.478  1.00 10.44           C  
+ATOM   4586  CG  ASP A 373      -8.903  21.854  -1.390  1.00 10.68           C  
+ATOM   4587  OD1 ASP A 373      -7.859  21.620  -0.735  1.00 13.17           O  
+ATOM   4588  OD2 ASP A 373      -9.550  20.949  -1.970  1.00 11.51           O  
+ATOM   4589  H   ASP A 373     -10.129  25.504  -1.158  1.00 11.46           H  
+ATOM   4590  HA  ASP A 373      -8.182  24.087  -0.110  1.00 13.37           H  
+ATOM   4591  HB2 ASP A 373     -10.292  23.258  -0.949  1.00 12.52           H  
+ATOM   4592  HB3 ASP A 373      -9.686  23.417  -2.410  1.00 12.52           H  
+ATOM   4593  N   MET A 374      -7.595  25.040  -3.111  1.00 10.07           N  
+ATOM   4594  CA  MET A 374      -6.537  25.096  -4.115  1.00  9.98           C  
+ATOM   4595  C   MET A 374      -5.455  26.113  -3.781  1.00 10.79           C  
+ATOM   4596  O   MET A 374      -4.327  25.964  -4.268  1.00 10.03           O  
+ATOM   4597  CB  MET A 374      -7.100  25.381  -5.513  1.00 10.87           C  
+ATOM   4598  CG  MET A 374      -7.463  26.812  -5.783  1.00  9.73           C  
+ATOM   4599  SD  MET A 374      -8.118  27.162  -7.429  1.00 11.66           S  
+ATOM   4600  CE  MET A 374      -9.701  26.290  -7.367  1.00 11.44           C  
+ATOM   4601  H   MET A 374      -8.356  25.342  -3.374  1.00 12.09           H  
+ATOM   4602  HA  MET A 374      -6.135  24.214  -4.147  1.00 11.98           H  
+ATOM   4603  HB2 MET A 374      -6.434  25.122  -6.169  1.00 13.04           H  
+ATOM   4604  HB3 MET A 374      -7.905  24.852  -5.631  1.00 13.04           H  
+ATOM   4605  HG2 MET A 374      -8.139  27.080  -5.142  1.00 11.68           H  
+ATOM   4606  HG3 MET A 374      -6.666  27.354  -5.670  1.00 11.68           H  
+ATOM   4607  HE1 MET A 374     -10.158  26.403  -8.215  1.00 13.73           H  
+ATOM   4608  HE2 MET A 374      -9.537  25.348  -7.202  1.00 13.73           H  
+ATOM   4609  HE3 MET A 374     -10.239  26.662  -6.650  1.00 13.73           H  
+ATOM   4610  N   ILE A 375      -5.774  27.148  -2.997  1.00 10.02           N  
+ATOM   4611  CA  ILE A 375      -4.787  28.178  -2.640  1.00  9.93           C  
+ATOM   4612  C   ILE A 375      -3.910  27.713  -1.486  1.00  9.82           C  
+ATOM   4613  O   ILE A 375      -2.790  28.224  -1.319  1.00 10.26           O  
+ATOM   4614  CB  ILE A 375      -5.540  29.503  -2.365  1.00 10.15           C  
+ATOM   4615  CG1 ILE A 375      -6.075  30.068  -3.703  1.00  9.99           C  
+ATOM   4616  CG2 ILE A 375      -4.661  30.503  -1.677  1.00 12.35           C  
+ATOM   4617  CD1 ILE A 375      -7.047  31.252  -3.591  1.00 11.27           C  
+ATOM   4618  H   ILE A 375      -6.553  27.280  -2.659  1.00 12.03           H  
+ATOM   4619  HA  ILE A 375      -4.170  28.356  -3.367  1.00 11.91           H  
+ATOM   4620  HB  ILE A 375      -6.284  29.318  -1.770  1.00 12.18           H  
+ATOM   4621 HG12 ILE A 375      -5.318  30.368  -4.230  1.00 11.99           H  
+ATOM   4622 HG13 ILE A 375      -6.542  29.357  -4.168  1.00 11.99           H  
+ATOM   4623 HG21 ILE A 375      -5.111  31.362  -1.662  1.00 14.82           H  
+ATOM   4624 HG22 ILE A 375      -4.491  30.204  -0.770  1.00 14.82           H  
+ATOM   4625 HG23 ILE A 375      -3.825  30.576  -2.163  1.00 14.82           H  
+ATOM   4626 HD11 ILE A 375      -7.421  31.437  -4.467  1.00 13.52           H  
+ATOM   4627 HD12 ILE A 375      -7.756  31.021  -2.971  1.00 13.52           H  
+ATOM   4628 HD13 ILE A 375      -6.563  32.028  -3.268  1.00 13.52           H  
+ATOM   4629  N   THR A 376      -4.331  26.690  -0.743  1.00 10.05           N  
+ATOM   4630  CA  THR A 376      -3.575  26.259   0.434  1.00  9.31           C  
+ATOM   4631  C   THR A 376      -2.098  26.009   0.144  1.00 11.55           C  
+ATOM   4632  O   THR A 376      -1.225  26.442   0.926  1.00 12.13           O  
+ATOM   4633  CB  THR A 376      -4.224  25.010   1.027  1.00 14.80           C  
+ATOM   4634  OG1 THR A 376      -5.521  25.368   1.533  1.00 15.88           O  
+ATOM   4635  CG2 THR A 376      -3.391  24.430   2.158  1.00 16.15           C  
+ATOM   4636  H   THR A 376      -5.043  26.233  -0.895  1.00 12.07           H  
+ATOM   4637  HA  THR A 376      -3.609  26.975   1.088  1.00 11.17           H  
+ATOM   4638  HB  THR A 376      -4.299  24.327   0.342  1.00 17.76           H  
+ATOM   4639  HG1 THR A 376      -6.001  25.663   0.910  1.00 19.05           H  
+ATOM   4640 HG21 THR A 376      -3.926  23.814   2.683  1.00 19.38           H  
+ATOM   4641 HG22 THR A 376      -2.626  23.954   1.797  1.00 19.38           H  
+ATOM   4642 HG23 THR A 376      -3.074  25.142   2.736  1.00 19.38           H  
+ATOM   4643  N   ARG A 377      -1.784  25.349  -0.977  1.00  9.94           N  
+ATOM   4644  CA  ARG A 377      -0.397  24.990  -1.269  1.00 10.63           C  
+ATOM   4645  C   ARG A 377       0.460  26.147  -1.769  1.00 12.34           C  
+ATOM   4646  O   ARG A 377       1.669  25.951  -1.977  1.00 13.23           O  
+ATOM   4647  CB  ARG A 377      -0.344  23.838  -2.273  1.00 10.87           C  
+ATOM   4648  CG  ARG A 377      -0.745  24.227  -3.689  1.00 11.39           C  
+ATOM   4649  CD  ARG A 377      -1.026  22.981  -4.487  1.00 14.21           C  
+ATOM   4650  NE  ARG A 377       0.183  22.259  -4.819  1.00 14.20           N  
+ATOM   4651  CZ  ARG A 377       0.203  21.004  -5.244  1.00 15.69           C  
+ATOM   4652  NH1 ARG A 377      -0.908  20.283  -5.338  1.00 16.52           N  
+ATOM   4653  NH2 ARG A 377       1.361  20.460  -5.598  1.00 17.07           N  
+ATOM   4654  H   ARG A 377      -2.351  25.102  -1.574  1.00 11.93           H  
+ATOM   4655  HA  ARG A 377       0.002  24.683  -0.440  1.00 12.75           H  
+ATOM   4656  HB2 ARG A 377       0.564  23.497  -2.307  1.00 13.05           H  
+ATOM   4657  HB3 ARG A 377      -0.949  23.140  -1.977  1.00 13.05           H  
+ATOM   4658  HG2 ARG A 377      -1.547  24.773  -3.666  1.00 13.67           H  
+ATOM   4659  HG3 ARG A 377      -0.023  24.716  -4.114  1.00 13.67           H  
+ATOM   4660  HD2 ARG A 377      -1.596  22.393  -3.967  1.00 17.05           H  
+ATOM   4661  HD3 ARG A 377      -1.468  23.226  -5.314  1.00 17.05           H  
+ATOM   4662  HE  ARG A 377       0.934  22.670  -4.736  1.00 17.04           H  
+ATOM   4663 HH11 ARG A 377      -1.665  20.629  -5.120  1.00 19.82           H  
+ATOM   4664 HH12 ARG A 377      -0.871  19.470  -5.616  1.00 19.82           H  
+ATOM   4665 HH21 ARG A 377       2.085  20.921  -5.551  1.00 20.48           H  
+ATOM   4666 HH22 ARG A 377       1.386  19.646  -5.875  1.00 20.48           H  
+ATOM   4667  N   THR A 378      -0.115  27.322  -1.989  1.00  9.99           N  
+ATOM   4668  CA  THR A 378       0.613  28.473  -2.499  1.00 10.03           C  
+ATOM   4669  C   THR A 378       1.012  29.407  -1.370  1.00 10.11           C  
+ATOM   4670  O   THR A 378       0.388  29.437  -0.313  1.00 11.09           O  
+ATOM   4671  CB  THR A 378      -0.233  29.236  -3.542  1.00 10.41           C  
+ATOM   4672  OG1 THR A 378      -1.300  29.946  -2.882  1.00  9.89           O  
+ATOM   4673  CG2 THR A 378      -0.824  28.271  -4.559  1.00 11.79           C  
+ATOM   4674  H   THR A 378      -0.948  27.481  -1.845  1.00 11.99           H  
+ATOM   4675  HA  THR A 378       1.427  28.167  -2.930  1.00 12.03           H  
+ATOM   4676  HB  THR A 378       0.333  29.870  -4.010  1.00 12.49           H  
+ATOM   4677  HG1 THR A 378      -1.780  29.407  -2.452  1.00 11.86           H  
+ATOM   4678 HG21 THR A 378      -1.083  28.752  -5.361  1.00 14.15           H  
+ATOM   4679 HG22 THR A 378      -0.170  27.595  -4.795  1.00 14.15           H  
+ATOM   4680 HG23 THR A 378      -1.607  27.836  -4.187  1.00 14.15           H  
+ATOM   4681  N   GLY A 379       2.077  30.168  -1.603  1.00 12.14           N  
+ATOM   4682  CA  GLY A 379       2.536  31.135  -0.613  1.00 11.58           C  
+ATOM   4683  C   GLY A 379       2.583  32.565  -1.114  1.00 11.12           C  
+ATOM   4684  O   GLY A 379       2.680  33.511  -0.320  1.00 11.53           O  
+ATOM   4685  H   GLY A 379       2.548  30.144  -2.322  1.00 14.57           H  
+ATOM   4686  HA2 GLY A 379       1.941  31.107   0.152  1.00 13.89           H  
+ATOM   4687  HA3 GLY A 379       3.430  30.890  -0.327  1.00 13.89           H  
+ATOM   4688  N   VAL A 380       2.500  32.734  -2.432  1.00 10.90           N  
+ATOM   4689  CA  VAL A 380       2.492  34.032  -3.088  1.00 11.38           C  
+ATOM   4690  C   VAL A 380       1.400  33.968  -4.143  1.00 10.35           C  
+ATOM   4691  O   VAL A 380       1.258  32.948  -4.829  1.00 11.62           O  
+ATOM   4692  CB  VAL A 380       3.854  34.366  -3.729  1.00 11.66           C  
+ATOM   4693  CG1 VAL A 380       3.787  35.726  -4.403  1.00 13.86           C  
+ATOM   4694  CG2 VAL A 380       4.961  34.320  -2.705  1.00 13.08           C  
+ATOM   4695  H   VAL A 380       2.445  32.080  -2.988  1.00 13.08           H  
+ATOM   4696  HA  VAL A 380       2.296  34.734  -2.447  1.00 13.65           H  
+ATOM   4697  HB  VAL A 380       4.059  33.699  -4.402  1.00 13.99           H  
+ATOM   4698 HG11 VAL A 380       4.683  35.996  -4.660  1.00 16.63           H  
+ATOM   4699 HG12 VAL A 380       3.223  35.661  -5.190  1.00 16.63           H  
+ATOM   4700 HG13 VAL A 380       3.413  36.369  -3.781  1.00 16.63           H  
+ATOM   4701 HG21 VAL A 380       5.794  34.580  -3.128  1.00 15.70           H  
+ATOM   4702 HG22 VAL A 380       4.750  34.935  -1.984  1.00 15.70           H  
+ATOM   4703 HG23 VAL A 380       5.033  33.417  -2.358  1.00 15.70           H  
+ATOM   4704  N   SER A 381       0.598  35.020  -4.242  1.00  9.47           N  
+ATOM   4705  CA  SER A 381      -0.478  35.097  -5.223  1.00  8.73           C  
+ATOM   4706  C   SER A 381      -0.282  36.304  -6.119  1.00 10.82           C  
+ATOM   4707  O   SER A 381      -0.034  37.411  -5.633  1.00 11.53           O  
+ATOM   4708  CB  SER A 381      -1.844  35.169  -4.538  1.00 10.74           C  
+ATOM   4709  OG  SER A 381      -2.027  33.996  -3.751  1.00 10.47           O  
+ATOM   4710  H   SER A 381       0.658  35.717  -3.742  1.00 11.37           H  
+ATOM   4711  HA  SER A 381      -0.451  34.304  -5.781  1.00 10.48           H  
+ATOM   4712  HB2 SER A 381      -1.878  35.952  -3.966  1.00 12.89           H  
+ATOM   4713  HB3 SER A 381      -2.541  35.220  -5.211  1.00 12.89           H  
+ATOM   4714  HG  SER A 381      -2.798  33.991  -3.417  1.00 12.56           H  
+ATOM   4715  N   ILE A 382      -0.429  36.084  -7.425  1.00  9.31           N  
+ATOM   4716  CA  ILE A 382      -0.271  37.114  -8.451  1.00 10.10           C  
+ATOM   4717  C   ILE A 382      -1.644  37.355  -9.065  1.00 10.11           C  
+ATOM   4718  O   ILE A 382      -2.344  36.393  -9.399  1.00 10.86           O  
+ATOM   4719  CB  ILE A 382       0.731  36.666  -9.527  1.00  9.61           C  
+ATOM   4720  CG1 ILE A 382       2.090  36.369  -8.902  1.00 11.77           C  
+ATOM   4721  CG2 ILE A 382       0.807  37.702 -10.637  1.00 11.54           C  
+ATOM   4722  CD1 ILE A 382       3.045  35.630  -9.870  1.00 15.75           C  
+ATOM   4723  H   ILE A 382      -0.629  35.315  -7.753  1.00 11.17           H  
+ATOM   4724  HA  ILE A 382       0.049  37.938  -8.052  1.00 12.12           H  
+ATOM   4725  HB  ILE A 382       0.422  35.839  -9.929  1.00 11.53           H  
+ATOM   4726 HG12 ILE A 382       2.509  37.206  -8.646  1.00 14.12           H  
+ATOM   4727 HG13 ILE A 382       1.962  35.810  -8.120  1.00 14.12           H  
+ATOM   4728 HG21 ILE A 382       1.577  37.512 -11.194  1.00 13.85           H  
+ATOM   4729 HG22 ILE A 382      -0.004  37.658 -11.166  1.00 13.85           H  
+ATOM   4730 HG23 ILE A 382       0.896  38.583 -10.240  1.00 13.85           H  
+ATOM   4731 HD11 ILE A 382       3.830  35.341  -9.379  1.00 18.89           H  
+ATOM   4732 HD12 ILE A 382       2.585  34.861 -10.241  1.00 18.89           H  
+ATOM   4733 HD13 ILE A 382       3.304  36.236 -10.581  1.00 18.89           H  
+ATOM   4734  N   PHE A 383      -2.014  38.628  -9.257  1.00 10.76           N  
+ATOM   4735  CA  PHE A 383      -3.330  39.009  -9.783  1.00  9.63           C  
+ATOM   4736  C   PHE A 383      -3.191  39.794 -11.077  1.00  9.90           C  
+ATOM   4737  O   PHE A 383      -2.496  40.819 -11.117  1.00 11.69           O  
+ATOM   4738  CB  PHE A 383      -4.101  39.812  -8.722  1.00 10.79           C  
+ATOM   4739  CG  PHE A 383      -4.236  39.049  -7.441  1.00 10.11           C  
+ATOM   4740  CD1 PHE A 383      -3.254  39.114  -6.488  1.00 11.04           C  
+ATOM   4741  CD2 PHE A 383      -5.277  38.169  -7.245  1.00 10.35           C  
+ATOM   4742  CE1 PHE A 383      -3.322  38.343  -5.350  1.00 10.82           C  
+ATOM   4743  CE2 PHE A 383      -5.351  37.400  -6.107  1.00 11.19           C  
+ATOM   4744  CZ  PHE A 383      -4.354  37.490  -5.150  1.00 11.14           C  
+ATOM   4745  H   PHE A 383      -1.508  39.302  -9.086  1.00 12.92           H  
+ATOM   4746  HA  PHE A 383      -3.829  38.209 -10.009  1.00 11.55           H  
+ATOM   4747  HB2 PHE A 383      -3.624  40.637  -8.537  1.00 12.95           H  
+ATOM   4748  HB3 PHE A 383      -4.990  40.010  -9.054  1.00 12.95           H  
+ATOM   4749  HD1 PHE A 383      -2.532  39.686  -6.611  1.00 13.25           H  
+ATOM   4750  HD2 PHE A 383      -5.941  38.094  -7.892  1.00 12.42           H  
+ATOM   4751  HE1 PHE A 383      -2.650  38.408  -4.710  1.00 12.98           H  
+ATOM   4752  HE2 PHE A 383      -6.068  36.821  -5.981  1.00 13.43           H  
+ATOM   4753  HZ  PHE A 383      -4.393  36.972  -4.379  1.00 13.37           H  
+ATOM   4754  N   LEU A 384      -3.856  39.304 -12.125  1.00 10.36           N  
+ATOM   4755  CA  LEU A 384      -3.849  39.894 -13.451  1.00  9.83           C  
+ATOM   4756  C   LEU A 384      -5.262  40.198 -13.923  1.00 10.32           C  
+ATOM   4757  O   LEU A 384      -6.143  39.343 -13.845  1.00 10.85           O  
+ATOM   4758  CB  LEU A 384      -3.216  38.948 -14.514  1.00 10.83           C  
+ATOM   4759  CG  LEU A 384      -1.860  38.354 -14.159  1.00 10.06           C  
+ATOM   4760  CD1 LEU A 384      -1.434  37.409 -15.248  1.00 12.05           C  
+ATOM   4761  CD2 LEU A 384      -0.813  39.432 -13.945  1.00 12.54           C  
+ATOM   4762  H   LEU A 384      -4.340  38.594 -12.084  1.00 12.43           H  
+ATOM   4763  HA  LEU A 384      -3.337  40.716 -13.387  1.00 11.80           H  
+ATOM   4764  HB2 LEU A 384      -3.825  38.206 -14.659  1.00 12.99           H  
+ATOM   4765  HB3 LEU A 384      -3.103  39.450 -15.336  1.00 12.99           H  
+ATOM   4766  HG  LEU A 384      -1.934  37.868 -13.322  1.00 12.07           H  
+ATOM   4767 HD11 LEU A 384      -0.574  37.025 -15.016  1.00 14.46           H  
+ATOM   4768 HD12 LEU A 384      -2.098  36.706 -15.334  1.00 14.46           H  
+ATOM   4769 HD13 LEU A 384      -1.363  37.899 -16.082  1.00 14.46           H  
+ATOM   4770 HD21 LEU A 384       0.038  39.011 -13.748  1.00 15.05           H  
+ATOM   4771 HD22 LEU A 384      -0.740  39.966 -14.751  1.00 15.05           H  
+ATOM   4772 HD23 LEU A 384      -1.085  39.992 -13.201  1.00 15.05           H  
+ATOM   4773  N   TYR A 385      -5.456  41.382 -14.508  1.00 10.77           N  
+ATOM   4774  CA  TYR A 385      -6.714  41.733 -15.212  1.00 11.79           C  
+ATOM   4775  C   TYR A 385      -7.881  41.564 -14.240  1.00 12.44           C  
+ATOM   4776  O   TYR A 385      -7.859  42.174 -13.160  1.00 12.49           O  
+ATOM   4777  CB  TYR A 385      -6.825  40.928 -16.525  1.00 10.71           C  
+ATOM   4778  CG  TYR A 385      -5.669  41.228 -17.438  1.00 10.45           C  
+ATOM   4779  CD1 TYR A 385      -5.576  42.455 -18.093  1.00 13.11           C  
+ATOM   4780  CD2 TYR A 385      -4.642  40.312 -17.619  1.00 10.66           C  
+ATOM   4781  CE1 TYR A 385      -4.501  42.756 -18.894  1.00 12.83           C  
+ATOM   4782  CE2 TYR A 385      -3.551  40.600 -18.438  1.00 11.12           C  
+ATOM   4783  CZ  TYR A 385      -3.489  41.832 -19.067  1.00 13.35           C  
+ATOM   4784  OH  TYR A 385      -2.400  42.131 -19.847  1.00 14.19           O  
+ATOM   4785  H   TYR A 385      -4.872  42.012 -14.516  1.00 12.92           H  
+ATOM   4786  HA  TYR A 385      -6.669  42.677 -15.432  1.00 14.15           H  
+ATOM   4787  HB2 TYR A 385      -6.820  39.979 -16.324  1.00 12.85           H  
+ATOM   4788  HB3 TYR A 385      -7.648  41.166 -16.981  1.00 12.85           H  
+ATOM   4789  HD1 TYR A 385      -6.255  43.082 -17.986  1.00 15.74           H  
+ATOM   4790  HD2 TYR A 385      -4.683  39.490 -17.186  1.00 12.79           H  
+ATOM   4791  HE1 TYR A 385      -4.455  43.582 -19.320  1.00 15.40           H  
+ATOM   4792  HE2 TYR A 385      -2.874  39.974 -18.560  1.00 13.35           H  
+ATOM   4793  HH  TYR A 385      -2.464  42.915 -20.142  1.00 17.02           H  
+ATOM   4794  N   GLY A 386      -8.912  40.813 -14.594  1.00 11.10           N  
+ATOM   4795  CA  GLY A 386     -10.062  40.626 -13.737  1.00 11.82           C  
+ATOM   4796  C   GLY A 386     -11.298  41.287 -14.294  1.00 12.15           C  
+ATOM   4797  O   GLY A 386     -11.813  42.251 -13.716  1.00 12.68           O  
+ATOM   4798  H   GLY A 386      -8.969  40.393 -15.342  1.00 13.32           H  
+ATOM   4799  HA2 GLY A 386     -10.239  39.677 -13.638  1.00 14.19           H  
+ATOM   4800  HA3 GLY A 386      -9.877  41.005 -12.863  1.00 14.19           H  
+ATOM   4801  N   ASN A 387     -11.751  40.804 -15.445  1.00 10.69           N  
+ATOM   4802  CA  ASN A 387     -12.969  41.314 -16.065  1.00 12.26           C  
+ATOM   4803  C   ASN A 387     -13.638  40.170 -16.815  1.00 12.30           C  
+ATOM   4804  O   ASN A 387     -12.979  39.193 -17.209  1.00 12.37           O  
+ATOM   4805  CB  ASN A 387     -12.683  42.522 -16.974  1.00 12.75           C  
+ATOM   4806  CG  ASN A 387     -11.819  42.175 -18.180  1.00 12.99           C  
+ATOM   4807  OD1 ASN A 387     -12.319  41.650 -19.168  1.00 11.92           O  
+ATOM   4808  ND2 ASN A 387     -10.536  42.483 -18.103  1.00 12.45           N  
+ATOM   4809  H   ASN A 387     -11.368  40.176 -15.891  1.00 12.82           H  
+ATOM   4810  HA  ASN A 387     -13.594  41.621 -15.390  1.00 14.71           H  
+ATOM   4811  HB2 ASN A 387     -13.525  42.875 -17.302  1.00 15.30           H  
+ATOM   4812  HB3 ASN A 387     -12.217  43.200 -16.459  1.00 15.30           H  
+ATOM   4813 HD21 ASN A 387     -10.011  42.305 -18.761  1.00 14.94           H  
+ATOM   4814 HD22 ASN A 387     -10.226  42.862 -17.396  1.00 14.94           H  
+ATOM   4815  N   LYS A 388     -14.955  40.270 -16.970  1.00 11.73           N  
+ATOM   4816  CA  LYS A 388     -15.732  39.206 -17.571  1.00 12.11           C  
+ATOM   4817  C   LYS A 388     -17.003  39.783 -18.169  1.00 15.58           C  
+ATOM   4818  O   LYS A 388     -17.400  40.912 -17.862  1.00 14.48           O  
+ATOM   4819  CB  LYS A 388     -16.098  38.133 -16.530  1.00 13.94           C  
+ATOM   4820  CG  LYS A 388     -17.016  38.633 -15.442  1.00 14.97           C  
+ATOM   4821  CD  LYS A 388     -17.285  37.510 -14.435  1.00 19.43           C  
+ATOM   4822  CE  LYS A 388     -17.879  38.035 -13.124  1.00 25.24           C  
+ATOM   4823  NZ  LYS A 388     -17.895  37.020 -11.990  1.00 26.27           N  
+ATOM   4824  H   LYS A 388     -15.420  40.953 -16.731  1.00 14.07           H  
+ATOM   4825  HA  LYS A 388     -15.214  38.802 -18.284  1.00 14.53           H  
+ATOM   4826  HB2 LYS A 388     -16.544  37.399 -16.981  1.00 16.72           H  
+ATOM   4827  HB3 LYS A 388     -15.283  37.816 -16.109  1.00 16.72           H  
+ATOM   4828  HG2 LYS A 388     -16.599  39.376 -14.978  1.00 17.97           H  
+ATOM   4829  HG3 LYS A 388     -17.860  38.915 -15.829  1.00 17.97           H  
+ATOM   4830  HD2 LYS A 388     -17.914  36.880 -14.820  1.00 23.31           H  
+ATOM   4831  HD3 LYS A 388     -16.450  37.060 -14.229  1.00 23.31           H  
+ATOM   4832  HE2 LYS A 388     -17.354  38.796 -12.829  1.00 30.28           H  
+ATOM   4833  HE3 LYS A 388     -18.795  38.307 -13.287  1.00 30.28           H  
+ATOM   4834  HZ1 LYS A 388     -18.384  36.314 -12.220  1.00 31.53           H  
+ATOM   4835  HZ2 LYS A 388     -17.065  36.751 -11.811  1.00 31.53           H  
+ATOM   4836  HZ3 LYS A 388     -18.243  37.387 -11.258  1.00 31.53           H  
+ATOM   4837  N   ILE A 389     -17.635  38.999 -19.040  1.00 15.31           N  
+ATOM   4838  CA  ILE A 389     -18.960  39.343 -19.546  1.00 18.56           C  
+ATOM   4839  C   ILE A 389     -20.007  38.893 -18.537  1.00 18.95           C  
+ATOM   4840  O   ILE A 389     -20.013  37.734 -18.091  1.00 21.24           O  
+ATOM   4841  CB  ILE A 389     -19.222  38.701 -20.916  1.00 18.76           C  
+ATOM   4842  CG1 ILE A 389     -18.199  39.173 -21.944  1.00 20.47           C  
+ATOM   4843  CG2 ILE A 389     -20.655  39.026 -21.389  1.00 23.53           C  
+ATOM   4844  CD1 ILE A 389     -18.230  40.654 -22.218  1.00 25.71           C  
+ATOM   4845  H   ILE A 389     -17.317  38.263 -19.352  1.00 18.37           H  
+ATOM   4846  HA  ILE A 389     -19.011  40.306 -19.648  1.00 22.27           H  
+ATOM   4847  HB  ILE A 389     -19.131  37.739 -20.822  1.00 22.51           H  
+ATOM   4848 HG12 ILE A 389     -17.311  38.953 -21.621  1.00 24.57           H  
+ATOM   4849 HG13 ILE A 389     -18.369  38.715 -22.783  1.00 24.57           H  
+ATOM   4850 HG21 ILE A 389     -20.727  38.827 -22.335  1.00 28.23           H  
+ATOM   4851 HG22 ILE A 389     -21.283  38.483 -20.888  1.00 28.23           H  
+ATOM   4852 HG23 ILE A 389     -20.832  39.967 -21.234  1.00 28.23           H  
+ATOM   4853 HD11 ILE A 389     -17.591  40.860 -22.918  1.00 30.85           H  
+ATOM   4854 HD12 ILE A 389     -19.124  40.904 -22.503  1.00 30.85           H  
+ATOM   4855 HD13 ILE A 389     -17.997  41.131 -21.406  1.00 30.85           H  
+ATOM   4856  N   ASP A 390     -20.893  39.807 -18.168  1.00 19.02           N  
+ATOM   4857  CA  ASP A 390     -22.060  39.476 -17.367  1.00 23.96           C  
+ATOM   4858  C   ASP A 390     -23.230  40.240 -17.960  1.00 24.94           C  
+ATOM   4859  O   ASP A 390     -23.168  41.468 -18.081  1.00 23.52           O  
+ATOM   4860  CB  ASP A 390     -21.857  39.840 -15.899  1.00 25.29           C  
+ATOM   4861  CG  ASP A 390     -23.034  39.427 -15.042  1.00 37.28           C  
+ATOM   4862  OD1 ASP A 390     -23.559  38.314 -15.260  1.00 41.72           O  
+ATOM   4863  OD2 ASP A 390     -23.428  40.210 -14.153  1.00 38.81           O  
+ATOM   4864  H   ASP A 390     -20.838  40.641 -18.373  1.00 22.82           H  
+ATOM   4865  HA  ASP A 390     -22.241  38.523 -17.405  1.00 28.76           H  
+ATOM   4866  HB2 ASP A 390     -21.066  39.389 -15.565  1.00 30.35           H  
+ATOM   4867  HB3 ASP A 390     -21.748  40.801 -15.822  1.00 30.35           H  
+ATOM   4868  N   LYS A 391     -24.274  39.519 -18.361  1.00 29.85           N  
+ATOM   4869  CA  LYS A 391     -25.458  40.156 -18.931  1.00 35.32           C  
+ATOM   4870  C   LYS A 391     -25.074  41.031 -20.122  1.00 26.72           C  
+ATOM   4871  O   LYS A 391     -25.567  42.149 -20.281  1.00 30.16           O  
+ATOM   4872  CB  LYS A 391     -26.197  40.970 -17.866  1.00 37.47           C  
+ATOM   4873  CG  LYS A 391     -26.611  40.156 -16.642  1.00 39.47           C  
+ATOM   4874  CD  LYS A 391     -27.248  41.038 -15.573  1.00 52.26           C  
+ATOM   4875  CE  LYS A 391     -27.873  40.209 -14.459  1.00 62.75           C  
+ATOM   4876  NZ  LYS A 391     -28.660  41.050 -13.507  1.00 76.42           N  
+ATOM   4877  H   LYS A 391     -24.320  38.662 -18.313  1.00 35.83           H  
+ATOM   4878  HA  LYS A 391     -26.063  39.471 -19.255  1.00 42.38           H  
+ATOM   4879  HB2 LYS A 391     -25.616  41.685 -17.563  1.00 44.97           H  
+ATOM   4880  HB3 LYS A 391     -27.001  41.340 -18.261  1.00 44.97           H  
+ATOM   4881  HG2 LYS A 391     -27.258  39.483 -16.907  1.00 47.37           H  
+ATOM   4882  HG3 LYS A 391     -25.828  39.730 -16.259  1.00 47.37           H  
+ATOM   4883  HD2 LYS A 391     -26.568  41.609 -15.183  1.00 62.71           H  
+ATOM   4884  HD3 LYS A 391     -27.944  41.579 -15.977  1.00 62.71           H  
+ATOM   4885  HE2 LYS A 391     -28.471  39.551 -14.848  1.00 75.30           H  
+ATOM   4886  HE3 LYS A 391     -27.171  39.764 -13.959  1.00 75.30           H  
+ATOM   4887  HZ1 LYS A 391     -29.015  40.539 -12.871  1.00 91.71           H  
+ATOM   4888  HZ2 LYS A 391     -28.131  41.657 -13.129  1.00 91.71           H  
+ATOM   4889  HZ3 LYS A 391     -29.316  41.467 -13.941  1.00 91.71           H  
+ATOM   4890  N   GLY A 392     -24.165  40.525 -20.952  1.00 27.77           N  
+ATOM   4891  CA  GLY A 392     -23.785  41.219 -22.164  1.00 29.04           C  
+ATOM   4892  C   GLY A 392     -22.905  42.434 -21.978  1.00 29.90           C  
+ATOM   4893  O   GLY A 392     -22.642  43.138 -22.958  1.00 29.61           O  
+ATOM   4894  H   GLY A 392     -23.755  39.778 -20.830  1.00 33.33           H  
+ATOM   4895  HA2 GLY A 392     -23.307  40.598 -22.736  1.00 34.84           H  
+ATOM   4896  HA3 GLY A 392     -24.592  41.509 -22.617  1.00 34.84           H  
+ATOM   4897  N   GLN A 393     -22.437  42.702 -20.758  1.00 21.63           N  
+ATOM   4898  CA  GLN A 393     -21.595  43.840 -20.456  1.00 21.71           C  
+ATOM   4899  C   GLN A 393     -20.283  43.371 -19.842  1.00 17.70           C  
+ATOM   4900  O   GLN A 393     -20.238  42.347 -19.156  1.00 20.31           O  
+ATOM   4901  CB  GLN A 393     -22.284  44.793 -19.486  1.00 26.18           C  
+ATOM   4902  CG  GLN A 393     -23.599  45.336 -20.003  1.00 27.99           C  
+ATOM   4903  CD  GLN A 393     -23.401  46.248 -21.199  1.00 30.91           C  
+ATOM   4904  OE1 GLN A 393     -22.521  47.111 -21.198  1.00 39.65           O  
+ATOM   4905  NE2 GLN A 393     -24.211  46.053 -22.233  1.00 39.22           N  
+ATOM   4906  H   GLN A 393     -22.604  42.215 -20.069  1.00 25.95           H  
+ATOM   4907  HA  GLN A 393     -21.398  44.317 -21.277  1.00 26.05           H  
+ATOM   4908  HB2 GLN A 393     -22.462  44.321 -18.657  1.00 31.41           H  
+ATOM   4909  HB3 GLN A 393     -21.697  45.547 -19.317  1.00 31.41           H  
+ATOM   4910  HG2 GLN A 393     -24.166  44.597 -20.274  1.00 33.59           H  
+ATOM   4911  HG3 GLN A 393     -24.033  45.846 -19.300  1.00 33.59           H  
+ATOM   4912 HE21 GLN A 393     -24.808  45.435 -22.200  1.00 47.06           H  
+ATOM   4913 HE22 GLN A 393     -24.138  46.544 -22.935  1.00 47.06           H  
+ATOM   4914  N   VAL A 394     -19.209  44.115 -20.106  1.00 17.67           N  
+ATOM   4915  CA  VAL A 394     -17.932  43.856 -19.445  1.00 16.92           C  
+ATOM   4916  C   VAL A 394     -17.992  44.423 -18.034  1.00 19.46           C  
+ATOM   4917  O   VAL A 394     -18.244  45.619 -17.847  1.00 20.87           O  
+ATOM   4918  CB  VAL A 394     -16.769  44.470 -20.224  1.00 18.80           C  
+ATOM   4919  CG1 VAL A 394     -15.448  44.217 -19.497  1.00 18.45           C  
+ATOM   4920  CG2 VAL A 394     -16.719  43.906 -21.643  1.00 20.43           C  
+ATOM   4921  H   VAL A 394     -19.195  44.771 -20.662  1.00 21.20           H  
+ATOM   4922  HA  VAL A 394     -17.793  42.898 -19.390  1.00 20.31           H  
+ATOM   4923  HB  VAL A 394     -16.902  45.429 -20.286  1.00 22.56           H  
+ATOM   4924 HG11 VAL A 394     -14.713  44.423 -20.096  1.00 22.14           H  
+ATOM   4925 HG12 VAL A 394     -15.405  44.788 -18.713  1.00 22.14           H  
+ATOM   4926 HG13 VAL A 394     -15.408  43.286 -19.230  1.00 22.14           H  
+ATOM   4927 HG21 VAL A 394     -15.959  44.288 -22.109  1.00 24.52           H  
+ATOM   4928 HG22 VAL A 394     -16.628  42.941 -21.596  1.00 24.52           H  
+ATOM   4929 HG23 VAL A 394     -17.540  44.138 -22.104  1.00 24.52           H  
+ATOM   4930  N   VAL A 395     -17.736  43.571 -17.036  1.00 16.56           N  
+ATOM   4931  CA  VAL A 395     -17.762  43.962 -15.635  1.00 17.42           C  
+ATOM   4932  C   VAL A 395     -16.498  43.440 -14.963  1.00 16.23           C  
+ATOM   4933  O   VAL A 395     -15.803  42.571 -15.490  1.00 15.89           O  
+ATOM   4934  CB  VAL A 395     -19.010  43.433 -14.901  1.00 17.34           C  
+ATOM   4935  CG1 VAL A 395     -20.270  43.917 -15.606  1.00 21.20           C  
+ATOM   4936  CG2 VAL A 395     -18.978  41.916 -14.783  1.00 19.14           C  
+ATOM   4937  H   VAL A 395     -17.540  42.742 -17.154  1.00 19.87           H  
+ATOM   4938  HA  VAL A 395     -17.766  44.931 -15.577  1.00 20.91           H  
+ATOM   4939  HB  VAL A 395     -19.018  43.782 -13.996  1.00 20.80           H  
+ATOM   4940 HG11 VAL A 395     -21.046  43.628 -15.100  1.00 25.45           H  
+ATOM   4941 HG12 VAL A 395     -20.251  44.886 -15.658  1.00 25.45           H  
+ATOM   4942 HG13 VAL A 395     -20.298  43.539 -16.499  1.00 25.45           H  
+ATOM   4943 HG21 VAL A 395     -19.861  41.601 -14.533  1.00 22.97           H  
+ATOM   4944 HG22 VAL A 395     -18.721  41.538 -15.638  1.00 22.97           H  
+ATOM   4945 HG23 VAL A 395     -18.333  41.666 -14.103  1.00 22.97           H  
+ATOM   4946  N   LYS A 396     -16.194  44.003 -13.793  1.00 17.98           N  
+ATOM   4947  CA  LYS A 396     -15.082  43.514 -12.990  1.00 16.45           C  
+ATOM   4948  C   LYS A 396     -15.368  42.107 -12.472  1.00 16.86           C  
+ATOM   4949  O   LYS A 396     -16.516  41.715 -12.235  1.00 19.35           O  
+ATOM   4950  CB  LYS A 396     -14.815  44.475 -11.833  1.00 21.16           C  
+ATOM   4951  CG  LYS A 396     -14.168  45.753 -12.313  1.00 27.70           C  
+ATOM   4952  CD  LYS A 396     -14.079  46.799 -11.212  1.00 28.61           C  
+ATOM   4953  CE  LYS A 396     -13.332  48.018 -11.704  1.00 32.28           C  
+ATOM   4954  NZ  LYS A 396     -13.173  48.994 -10.607  1.00 29.14           N  
+ATOM   4955  H   LYS A 396     -16.616  44.667 -13.446  1.00 21.58           H  
+ATOM   4956  HA  LYS A 396     -14.278  43.466 -13.531  1.00 19.74           H  
+ATOM   4957  HB2 LYS A 396     -15.655  44.700 -11.403  1.00 25.39           H  
+ATOM   4958  HB3 LYS A 396     -14.219  44.051 -11.195  1.00 25.39           H  
+ATOM   4959  HG2 LYS A 396     -13.269  45.560 -12.620  1.00 33.24           H  
+ATOM   4960  HG3 LYS A 396     -14.694  46.123 -13.039  1.00 33.24           H  
+ATOM   4961  HD2 LYS A 396     -14.972  47.069 -10.946  1.00 34.34           H  
+ATOM   4962  HD3 LYS A 396     -13.604  46.430 -10.451  1.00 34.34           H  
+ATOM   4963  HE2 LYS A 396     -12.452  47.757 -12.017  1.00 38.74           H  
+ATOM   4964  HE3 LYS A 396     -13.829  48.437 -12.423  1.00 38.74           H  
+ATOM   4965  HZ1 LYS A 396     -13.971  49.277 -10.334  1.00 34.97           H  
+ATOM   4966  HZ2 LYS A 396     -12.751  48.615  -9.921  1.00 34.97           H  
+ATOM   4967  HZ3 LYS A 396     -12.698  49.692 -10.887  1.00 34.97           H  
+ATOM   4968  N   ALA A 397     -14.297  41.336 -12.311  1.00 13.25           N  
+ATOM   4969  CA  ALA A 397     -14.375  39.922 -11.950  1.00 13.37           C  
+ATOM   4970  C   ALA A 397     -14.275  39.727 -10.441  1.00 14.75           C  
+ATOM   4971  O   ALA A 397     -13.179  39.667  -9.886  1.00 13.94           O  
+ATOM   4972  CB  ALA A 397     -13.257  39.149 -12.640  1.00 15.08           C  
+ATOM   4973  H   ALA A 397     -13.489  41.616 -12.408  1.00 15.90           H  
+ATOM   4974  HA  ALA A 397     -15.249  39.604 -12.227  1.00 16.04           H  
+ATOM   4975  HB1 ALA A 397     -13.302  38.219 -12.369  1.00 18.10           H  
+ATOM   4976  HB2 ALA A 397     -13.371  39.220 -13.601  1.00 18.10           H  
+ATOM   4977  HB3 ALA A 397     -12.404  39.529 -12.380  1.00 18.10           H  
+ATOM   4978  N   LYS A 398     -15.423  39.555  -9.786  1.00 14.84           N  
+ATOM   4979  CA  LYS A 398     -15.428  39.392  -8.337  1.00 13.99           C  
+ATOM   4980  C   LYS A 398     -14.649  38.165  -7.895  1.00 11.42           C  
+ATOM   4981  O   LYS A 398     -14.164  38.127  -6.759  1.00 13.02           O  
+ATOM   4982  CB  LYS A 398     -16.862  39.320  -7.817  1.00 17.69           C  
+ATOM   4983  CG  LYS A 398     -17.618  40.629  -7.955  1.00 32.09           C  
+ATOM   4984  CD  LYS A 398     -19.029  40.505  -7.396  1.00 44.39           C  
+ATOM   4985  CE  LYS A 398     -19.800  41.810  -7.512  1.00 44.19           C  
+ATOM   4986  NZ  LYS A 398     -21.222  41.621  -7.112  1.00 56.00           N  
+ATOM   4987  H   LYS A 398     -16.200  39.529 -10.153  1.00 17.81           H  
+ATOM   4988  HA  LYS A 398     -15.003  40.171  -7.945  1.00 16.78           H  
+ATOM   4989  HB2 LYS A 398     -17.344  38.643  -8.318  1.00 21.23           H  
+ATOM   4990  HB3 LYS A 398     -16.843  39.084  -6.876  1.00 21.23           H  
+ATOM   4991  HG2 LYS A 398     -17.153  41.324  -7.463  1.00 38.50           H  
+ATOM   4992  HG3 LYS A 398     -17.679  40.870  -8.892  1.00 38.50           H  
+ATOM   4993  HD2 LYS A 398     -19.510  39.823  -7.891  1.00 53.27           H  
+ATOM   4994  HD3 LYS A 398     -18.982  40.263  -6.458  1.00 53.27           H  
+ATOM   4995  HE2 LYS A 398     -19.401  42.475  -6.929  1.00 53.03           H  
+ATOM   4996  HE3 LYS A 398     -19.777  42.119  -8.432  1.00 53.03           H  
+ATOM   4997  HZ1 LYS A 398     -21.664  42.390  -7.185  1.00 67.20           H  
+ATOM   4998  HZ2 LYS A 398     -21.608  41.015  -7.637  1.00 67.20           H  
+ATOM   4999  HZ3 LYS A 398     -21.266  41.341  -6.268  1.00 67.20           H  
+ATOM   5000  N   GLY A 399     -14.529  37.144  -8.747  1.00 10.73           N  
+ATOM   5001  CA  GLY A 399     -13.779  35.957  -8.343  1.00 11.97           C  
+ATOM   5002  C   GLY A 399     -12.314  36.238  -8.082  1.00 12.41           C  
+ATOM   5003  O   GLY A 399     -11.694  35.577  -7.239  1.00 12.76           O  
+ATOM   5004  H   GLY A 399     -14.862  37.115  -9.539  1.00 12.88           H  
+ATOM   5005  HA2 GLY A 399     -14.167  35.596  -7.531  1.00 14.36           H  
+ATOM   5006  HA3 GLY A 399     -13.838  35.290  -9.045  1.00 14.36           H  
+ATOM   5007  N   VAL A 400     -11.734  37.208  -8.802  1.00 10.88           N  
+ATOM   5008  CA  VAL A 400     -10.346  37.589  -8.560  1.00 10.72           C  
+ATOM   5009  C   VAL A 400     -10.229  38.265  -7.203  1.00 10.75           C  
+ATOM   5010  O   VAL A 400      -9.272  38.043  -6.466  1.00 12.21           O  
+ATOM   5011  CB  VAL A 400      -9.827  38.490  -9.696  1.00 10.94           C  
+ATOM   5012  CG1 VAL A 400      -8.414  38.970  -9.405  1.00 10.72           C  
+ATOM   5013  CG2 VAL A 400      -9.870  37.716 -11.008  1.00 10.73           C  
+ATOM   5014  H   VAL A 400     -12.121  37.653  -9.428  1.00 13.06           H  
+ATOM   5015  HA  VAL A 400      -9.798  36.789  -8.551  1.00 12.86           H  
+ATOM   5016  HB  VAL A 400     -10.391  39.275  -9.769  1.00 13.12           H  
+ATOM   5017 HG11 VAL A 400      -8.043  39.365 -10.209  1.00 12.86           H  
+ATOM   5018 HG12 VAL A 400      -8.446  39.632  -8.696  1.00 12.86           H  
+ATOM   5019 HG13 VAL A 400      -7.874  38.214  -9.127  1.00 12.86           H  
+ATOM   5020 HG21 VAL A 400      -9.489  38.265 -11.711  1.00 12.87           H  
+ATOM   5021 HG22 VAL A 400      -9.355  36.900 -10.910  1.00 12.87           H  
+ATOM   5022 HG23 VAL A 400     -10.792  37.503 -11.218  1.00 12.87           H  
+ATOM   5023  N   GLN A 401     -11.216  39.084  -6.852  1.00 12.32           N  
+ATOM   5024  CA  GLN A 401     -11.239  39.686  -5.523  1.00 13.75           C  
+ATOM   5025  C   GLN A 401     -11.349  38.619  -4.446  1.00 11.48           C  
+ATOM   5026  O   GLN A 401     -10.650  38.680  -3.422  1.00 11.86           O  
+ATOM   5027  CB  GLN A 401     -12.404  40.677  -5.431  1.00 15.04           C  
+ATOM   5028  CG  GLN A 401     -12.604  41.307  -4.043  1.00 17.91           C  
+ATOM   5029  CD  GLN A 401     -11.555  42.305  -3.702  1.00 25.25           C  
+ATOM   5030  OE1 GLN A 401     -10.824  42.151  -2.709  1.00 27.20           O  
+ATOM   5031  NE2 GLN A 401     -11.466  43.358  -4.503  1.00 23.41           N  
+ATOM   5032  H   GLN A 401     -11.876  39.306  -7.357  1.00 14.78           H  
+ATOM   5033  HA  GLN A 401     -10.414  40.176  -5.375  1.00 16.50           H  
+ATOM   5034  HB2 GLN A 401     -12.246  41.398  -6.059  1.00 18.05           H  
+ATOM   5035  HB3 GLN A 401     -13.223  40.210  -5.661  1.00 18.05           H  
+ATOM   5036  HG2 GLN A 401     -13.463  41.756  -4.021  1.00 21.49           H  
+ATOM   5037  HG3 GLN A 401     -12.579  40.606  -3.372  1.00 21.49           H  
+ATOM   5038 HE21 GLN A 401     -11.997  43.434  -5.174  1.00 28.09           H  
+ATOM   5039 HE22 GLN A 401     -10.876  43.965  -4.351  1.00 28.09           H  
+ATOM   5040  N   SER A 402     -12.212  37.620  -4.662  1.00 12.81           N  
+ATOM   5041  CA  SER A 402     -12.346  36.545  -3.682  1.00 13.10           C  
+ATOM   5042  C   SER A 402     -11.025  35.807  -3.503  1.00 12.48           C  
+ATOM   5043  O   SER A 402     -10.633  35.462  -2.372  1.00 11.77           O  
+ATOM   5044  CB  SER A 402     -13.428  35.562  -4.110  1.00 14.79           C  
+ATOM   5045  OG  SER A 402     -14.708  36.178  -4.109  1.00 17.55           O  
+ATOM   5046  H   SER A 402     -12.719  37.545  -5.352  1.00 15.37           H  
+ATOM   5047  HA  SER A 402     -12.609  36.934  -2.833  1.00 15.72           H  
+ATOM   5048  HB2 SER A 402     -13.231  35.248  -5.006  1.00 17.75           H  
+ATOM   5049  HB3 SER A 402     -13.438  34.816  -3.491  1.00 17.75           H  
+ATOM   5050  HG  SER A 402     -14.704  36.851  -4.612  1.00 21.07           H  
+ATOM   5051  N   GLU A 403     -10.327  35.547  -4.612  1.00 10.92           N  
+ATOM   5052  CA  GLU A 403      -9.026  34.878  -4.523  1.00 10.60           C  
+ATOM   5053  C   GLU A 403      -7.998  35.739  -3.796  1.00 10.38           C  
+ATOM   5054  O   GLU A 403      -7.136  35.196  -3.090  1.00 11.17           O  
+ATOM   5055  CB  GLU A 403      -8.558  34.483  -5.925  1.00 10.08           C  
+ATOM   5056  CG  GLU A 403      -9.419  33.319  -6.452  1.00 11.36           C  
+ATOM   5057  CD  GLU A 403      -9.401  33.074  -7.961  1.00 11.42           C  
+ATOM   5058  OE1 GLU A 403      -8.644  33.751  -8.689  1.00 11.76           O  
+ATOM   5059  OE2 GLU A 403     -10.166  32.173  -8.391  1.00  9.90           O  
+ATOM   5060  H   GLU A 403     -10.579  35.742  -5.411  1.00 13.11           H  
+ATOM   5061  HA  GLU A 403      -9.112  34.060  -4.009  1.00 12.72           H  
+ATOM   5062  HB2 GLU A 403      -8.651  35.239  -6.526  1.00 12.09           H  
+ATOM   5063  HB3 GLU A 403      -7.631  34.198  -5.893  1.00 12.09           H  
+ATOM   5064  HG2 GLU A 403      -9.110  32.502  -6.029  1.00 13.64           H  
+ATOM   5065  HG3 GLU A 403     -10.341  33.492  -6.205  1.00 13.64           H  
+ATOM   5066  N   PHE A 404      -8.058  37.068  -3.955  1.00 10.33           N  
+ATOM   5067  CA  PHE A 404      -7.191  37.951  -3.183  1.00 10.23           C  
+ATOM   5068  C   PHE A 404      -7.484  37.835  -1.693  1.00 11.91           C  
+ATOM   5069  O   PHE A 404      -6.569  37.685  -0.881  1.00 11.07           O  
+ATOM   5070  CB  PHE A 404      -7.376  39.398  -3.664  1.00 12.04           C  
+ATOM   5071  CG  PHE A 404      -6.572  40.413  -2.903  1.00 11.84           C  
+ATOM   5072  CD1 PHE A 404      -7.099  41.022  -1.785  1.00 14.26           C  
+ATOM   5073  CD2 PHE A 404      -5.323  40.804  -3.344  1.00 11.21           C  
+ATOM   5074  CE1 PHE A 404      -6.371  41.988  -1.095  1.00 14.34           C  
+ATOM   5075  CE2 PHE A 404      -4.600  41.772  -2.665  1.00 14.38           C  
+ATOM   5076  CZ  PHE A 404      -5.127  42.348  -1.523  1.00 14.73           C  
+ATOM   5077  H   PHE A 404      -8.587  37.474  -4.498  1.00 12.39           H  
+ATOM   5078  HA  PHE A 404      -6.265  37.698  -3.326  1.00 12.27           H  
+ATOM   5079  HB2 PHE A 404      -7.109  39.451  -4.595  1.00 14.44           H  
+ATOM   5080  HB3 PHE A 404      -8.311  39.637  -3.573  1.00 14.44           H  
+ATOM   5081  HD1 PHE A 404      -7.948  40.786  -1.488  1.00 17.11           H  
+ATOM   5082  HD2 PHE A 404      -4.962  40.412  -4.106  1.00 13.45           H  
+ATOM   5083  HE1 PHE A 404      -6.735  42.390  -0.339  1.00 17.21           H  
+ATOM   5084  HE2 PHE A 404      -3.764  42.034  -2.977  1.00 17.25           H  
+ATOM   5085  HZ  PHE A 404      -4.634  42.978  -1.049  1.00 17.67           H  
+ATOM   5086  N   ASN A 405      -8.762  37.896  -1.323  1.00 12.24           N  
+ATOM   5087  CA  ASN A 405      -9.139  37.814   0.089  1.00 11.16           C  
+ATOM   5088  C   ASN A 405      -8.677  36.499   0.696  1.00 13.16           C  
+ATOM   5089  O   ASN A 405      -8.092  36.477   1.777  1.00 12.08           O  
+ATOM   5090  CB  ASN A 405     -10.651  37.960   0.224  1.00 14.46           C  
+ATOM   5091  CG  ASN A 405     -11.145  39.332  -0.184  1.00 14.53           C  
+ATOM   5092  OD1 ASN A 405     -10.369  40.288  -0.260  1.00 17.72           O  
+ATOM   5093  ND2 ASN A 405     -12.434  39.431  -0.465  1.00 20.24           N  
+ATOM   5094  H   ASN A 405      -9.425  37.983  -1.863  1.00 14.69           H  
+ATOM   5095  HA  ASN A 405      -8.716  38.539   0.575  1.00 13.39           H  
+ATOM   5096  HB2 ASN A 405     -11.084  37.304  -0.344  1.00 17.35           H  
+ATOM   5097  HB3 ASN A 405     -10.901  37.814   1.150  1.00 17.35           H  
+ATOM   5098 HD21 ASN A 405     -12.765  40.188  -0.702  1.00 24.28           H  
+ATOM   5099 HD22 ASN A 405     -12.940  38.738  -0.410  1.00 24.28           H  
+ATOM   5100  N   ILE A 406      -8.916  35.390  -0.009  1.00 11.14           N  
+ATOM   5101  CA  ILE A 406      -8.533  34.074   0.495  1.00 10.70           C  
+ATOM   5102  C   ILE A 406      -7.024  33.974   0.620  1.00 10.99           C  
+ATOM   5103  O   ILE A 406      -6.503  33.414   1.592  1.00 12.00           O  
+ATOM   5104  CB  ILE A 406      -9.103  32.975  -0.423  1.00 10.85           C  
+ATOM   5105  CG1 ILE A 406     -10.627  32.928  -0.290  1.00 12.56           C  
+ATOM   5106  CG2 ILE A 406      -8.461  31.609  -0.133  1.00 11.96           C  
+ATOM   5107  CD1 ILE A 406     -11.314  32.162  -1.385  1.00 13.08           C  
+ATOM   5108  H   ILE A 406      -9.297  35.374  -0.779  1.00 13.36           H  
+ATOM   5109  HA  ILE A 406      -8.912  33.955   1.380  1.00 12.83           H  
+ATOM   5110  HB  ILE A 406      -8.882  33.196  -1.342  1.00 13.02           H  
+ATOM   5111 HG12 ILE A 406     -10.853  32.503   0.553  1.00 15.07           H  
+ATOM   5112 HG13 ILE A 406     -10.969  33.836  -0.306  1.00 15.07           H  
+ATOM   5113 HG21 ILE A 406      -8.983  30.916  -0.567  1.00 14.35           H  
+ATOM   5114 HG22 ILE A 406      -7.555  31.605  -0.480  1.00 14.35           H  
+ATOM   5115 HG23 ILE A 406      -8.448  31.463   0.826  1.00 14.35           H  
+ATOM   5116 HD11 ILE A 406     -12.274  32.268  -1.290  1.00 15.69           H  
+ATOM   5117 HD12 ILE A 406     -11.026  32.511  -2.243  1.00 15.69           H  
+ATOM   5118 HD13 ILE A 406     -11.076  31.225  -1.312  1.00 15.69           H  
+ATOM   5119  N   SER A 407      -6.301  34.490  -0.370  1.00 10.21           N  
+ATOM   5120  CA  SER A 407      -4.847  34.491  -0.306  1.00 11.18           C  
+ATOM   5121  C   SER A 407      -4.348  35.245   0.923  1.00 11.02           C  
+ATOM   5122  O   SER A 407      -3.473  34.762   1.667  1.00 11.38           O  
+ATOM   5123  CB  SER A 407      -4.293  35.132  -1.576  1.00 12.61           C  
+ATOM   5124  OG  SER A 407      -4.525  34.333  -2.716  1.00 12.13           O  
+ATOM   5125  H   SER A 407      -6.627  34.841  -1.084  1.00 12.25           H  
+ATOM   5126  HA  SER A 407      -4.531  33.576  -0.246  1.00 13.41           H  
+ATOM   5127  HB2 SER A 407      -4.724  35.991  -1.705  1.00 15.13           H  
+ATOM   5128  HB3 SER A 407      -3.336  35.254  -1.470  1.00 15.13           H  
+ATOM   5129  HG  SER A 407      -5.351  34.247  -2.844  1.00 14.56           H  
+ATOM   5130  N   PHE A 408      -4.878  36.453   1.130  1.00 11.49           N  
+ATOM   5131  CA  PHE A 408      -4.446  37.254   2.273  1.00 12.49           C  
+ATOM   5132  C   PHE A 408      -4.826  36.596   3.592  1.00 12.06           C  
+ATOM   5133  O   PHE A 408      -4.063  36.669   4.562  1.00 11.15           O  
+ATOM   5134  CB  PHE A 408      -5.048  38.649   2.166  1.00 13.21           C  
+ATOM   5135  CG  PHE A 408      -4.600  39.580   3.224  1.00 16.27           C  
+ATOM   5136  CD1 PHE A 408      -3.316  40.062   3.230  1.00 17.64           C  
+ATOM   5137  CD2 PHE A 408      -5.467  39.961   4.232  1.00 23.15           C  
+ATOM   5138  CE1 PHE A 408      -2.908  40.933   4.223  1.00 21.63           C  
+ATOM   5139  CE2 PHE A 408      -5.052  40.835   5.236  1.00 18.82           C  
+ATOM   5140  CZ  PHE A 408      -3.779  41.305   5.223  1.00 18.56           C  
+ATOM   5141  H   PHE A 408      -5.476  36.823   0.635  1.00 13.78           H  
+ATOM   5142  HA  PHE A 408      -3.480  37.337   2.259  1.00 14.98           H  
+ATOM   5143  HB2 PHE A 408      -4.797  39.032   1.311  1.00 15.85           H  
+ATOM   5144  HB3 PHE A 408      -6.014  38.577   2.227  1.00 15.85           H  
+ATOM   5145  HD1 PHE A 408      -2.720  39.802   2.565  1.00 21.16           H  
+ATOM   5146  HD2 PHE A 408      -6.337  39.631   4.241  1.00 27.79           H  
+ATOM   5147  HE1 PHE A 408      -2.040  41.269   4.215  1.00 25.95           H  
+ATOM   5148  HE2 PHE A 408      -5.642  41.092   5.908  1.00 22.59           H  
+ATOM   5149  HZ  PHE A 408      -3.494  41.883   5.893  1.00 22.27           H  
+ATOM   5150  N   GLU A 409      -5.982  35.931   3.641  1.00 12.95           N  
+ATOM   5151  CA  GLU A 409      -6.423  35.275   4.870  1.00 12.57           C  
+ATOM   5152  C   GLU A 409      -5.493  34.149   5.297  1.00 12.57           C  
+ATOM   5153  O   GLU A 409      -5.405  33.850   6.489  1.00 14.80           O  
+ATOM   5154  CB  GLU A 409      -7.855  34.770   4.703  1.00 16.33           C  
+ATOM   5155  CG  GLU A 409      -8.865  35.891   4.755  1.00 20.60           C  
+ATOM   5156  CD  GLU A 409     -10.201  35.522   4.142  1.00 31.01           C  
+ATOM   5157  OE1 GLU A 409     -10.536  34.316   4.133  1.00 30.80           O  
+ATOM   5158  OE2 GLU A 409     -10.898  36.453   3.665  1.00 27.09           O  
+ATOM   5159  H   GLU A 409      -6.526  35.845   2.980  1.00 15.54           H  
+ATOM   5160  HA  GLU A 409      -6.416  35.929   5.587  1.00 15.08           H  
+ATOM   5161  HB2 GLU A 409      -7.937  34.328   3.843  1.00 19.60           H  
+ATOM   5162  HB3 GLU A 409      -8.058  34.146   5.417  1.00 19.60           H  
+ATOM   5163  HG2 GLU A 409      -9.019  36.132   5.682  1.00 24.72           H  
+ATOM   5164  HG3 GLU A 409      -8.514  36.653   4.268  1.00 24.72           H  
+ATOM   5165  N   GLN A 410      -4.769  33.521   4.370  1.00 11.96           N  
+ATOM   5166  CA  GLN A 410      -3.780  32.525   4.759  1.00 11.41           C  
+ATOM   5167  C   GLN A 410      -2.362  33.095   4.764  1.00 11.40           C  
+ATOM   5168  O   GLN A 410      -1.379  32.339   4.764  1.00 12.66           O  
+ATOM   5169  CB  GLN A 410      -3.856  31.278   3.887  1.00 16.92           C  
+ATOM   5170  CG  GLN A 410      -3.406  31.419   2.469  1.00 13.69           C  
+ATOM   5171  CD  GLN A 410      -3.228  30.050   1.819  1.00 15.33           C  
+ATOM   5172  OE1 GLN A 410      -4.117  29.191   1.900  1.00 17.36           O  
+ATOM   5173  NE2 GLN A 410      -2.080  29.829   1.175  1.00 11.64           N  
+ATOM   5174  H   GLN A 410      -4.834  33.655   3.523  1.00 14.35           H  
+ATOM   5175  HA  GLN A 410      -3.994  32.236   5.660  1.00 13.69           H  
+ATOM   5176  HB2 GLN A 410      -3.301  30.594   4.293  1.00 20.30           H  
+ATOM   5177  HB3 GLN A 410      -4.780  30.984   3.863  1.00 20.30           H  
+ATOM   5178  HG2 GLN A 410      -4.072  31.914   1.966  1.00 16.43           H  
+ATOM   5179  HG3 GLN A 410      -2.556  31.885   2.443  1.00 16.43           H  
+ATOM   5180 HE21 GLN A 410      -1.481  30.446   1.141  1.00 13.97           H  
+ATOM   5181 HE22 GLN A 410      -1.939  29.071   0.795  1.00 13.97           H  
+ATOM   5182  N   ASN A 411      -2.240  34.418   4.804  1.00 10.40           N  
+ATOM   5183  CA  ASN A 411      -0.982  35.128   4.938  1.00  9.88           C  
+ATOM   5184  C   ASN A 411      -0.073  34.972   3.727  1.00 11.33           C  
+ATOM   5185  O   ASN A 411       1.143  35.155   3.835  1.00 11.49           O  
+ATOM   5186  CB  ASN A 411      -0.250  34.712   6.209  1.00 10.38           C  
+ATOM   5187  CG  ASN A 411      -1.119  34.830   7.435  1.00 11.03           C  
+ATOM   5188  OD1 ASN A 411      -1.859  35.802   7.596  1.00 11.99           O  
+ATOM   5189  ND2 ASN A 411      -1.063  33.824   8.296  1.00 11.67           N  
+ATOM   5190  H   ASN A 411      -2.912  34.952   4.751  1.00 12.49           H  
+ATOM   5191  HA  ASN A 411      -1.182  36.075   5.007  1.00 11.86           H  
+ATOM   5192  HB2 ASN A 411       0.030  33.787   6.126  1.00 12.46           H  
+ATOM   5193  HB3 ASN A 411       0.524  35.283   6.332  1.00 12.46           H  
+ATOM   5194 HD21 ASN A 411      -1.540  33.844   9.012  1.00 14.00           H  
+ATOM   5195 HD22 ASN A 411      -0.550  33.152   8.140  1.00 14.00           H  
+ATOM   5196  N   ASN A 412      -0.631  34.705   2.551  1.00 10.90           N  
+ATOM   5197  CA  ASN A 412       0.168  34.831   1.346  1.00 11.47           C  
+ATOM   5198  C   ASN A 412       0.615  36.275   1.133  1.00  9.70           C  
+ATOM   5199  O   ASN A 412      -0.110  37.224   1.430  1.00 12.18           O  
+ATOM   5200  CB  ASN A 412      -0.626  34.420   0.104  1.00  9.20           C  
+ATOM   5201  CG  ASN A 412      -0.691  32.923  -0.098  1.00 12.11           C  
+ATOM   5202  OD1 ASN A 412      -0.470  32.151   0.823  1.00 11.31           O  
+ATOM   5203  ND2 ASN A 412      -0.995  32.507  -1.326  1.00 11.89           N  
+ATOM   5204  H   ASN A 412      -1.446  34.457   2.431  1.00 13.08           H  
+ATOM   5205  HA  ASN A 412       0.939  34.250   1.449  1.00 13.77           H  
+ATOM   5206  HB2 ASN A 412      -1.535  34.748   0.190  1.00 11.05           H  
+ATOM   5207  HB3 ASN A 412      -0.206  34.808  -0.679  1.00 11.05           H  
+ATOM   5208 HD21 ASN A 412      -1.045  31.665  -1.495  1.00 14.27           H  
+ATOM   5209 HD22 ASN A 412      -1.141  33.080  -1.951  1.00 14.27           H  
+ATOM   5210  N   TYR A 413       1.795  36.433   0.556  1.00 10.43           N  
+ATOM   5211  CA  TYR A 413       2.114  37.698  -0.085  1.00 11.59           C  
+ATOM   5212  C   TYR A 413       1.262  37.824  -1.351  1.00 14.18           C  
+ATOM   5213  O   TYR A 413       1.049  36.845  -2.085  1.00 12.57           O  
+ATOM   5214  CB  TYR A 413       3.601  37.793  -0.411  1.00 11.59           C  
+ATOM   5215  CG  TYR A 413       4.505  37.922   0.797  1.00 12.43           C  
+ATOM   5216  CD1 TYR A 413       4.400  39.000   1.642  1.00 12.67           C  
+ATOM   5217  CD2 TYR A 413       5.448  36.953   1.072  1.00 15.38           C  
+ATOM   5218  CE1 TYR A 413       5.223  39.120   2.759  1.00 17.15           C  
+ATOM   5219  CE2 TYR A 413       6.275  37.061   2.178  1.00 15.54           C  
+ATOM   5220  CZ  TYR A 413       6.151  38.139   3.014  1.00 18.04           C  
+ATOM   5221  OH  TYR A 413       6.968  38.240   4.128  1.00 20.48           O  
+ATOM   5222  H   TYR A 413       2.415  35.838   0.522  1.00 12.51           H  
+ATOM   5223  HA  TYR A 413       1.922  38.441   0.509  1.00 13.91           H  
+ATOM   5224  HB2 TYR A 413       3.864  36.990  -0.888  1.00 13.91           H  
+ATOM   5225  HB3 TYR A 413       3.746  38.573  -0.969  1.00 13.91           H  
+ATOM   5226  HD1 TYR A 413       3.769  39.660   1.465  1.00 15.20           H  
+ATOM   5227  HD2 TYR A 413       5.530  36.219   0.508  1.00 18.45           H  
+ATOM   5228  HE1 TYR A 413       5.146  39.854   3.324  1.00 20.58           H  
+ATOM   5229  HE2 TYR A 413       6.911  36.406   2.352  1.00 18.65           H  
+ATOM   5230  HH  TYR A 413       6.780  38.935   4.560  1.00 24.57           H  
+ATOM   5231  N   VAL A 414       0.734  39.018  -1.578  1.00 12.29           N  
+ATOM   5232  CA  VAL A 414      -0.098  39.306  -2.738  1.00 10.66           C  
+ATOM   5233  C   VAL A 414       0.679  40.210  -3.682  1.00 15.96           C  
+ATOM   5234  O   VAL A 414       1.442  41.084  -3.250  1.00 17.45           O  
+ATOM   5235  CB  VAL A 414      -1.447  39.933  -2.348  1.00 12.93           C  
+ATOM   5236  CG1 VAL A 414      -2.271  38.930  -1.595  1.00 14.10           C  
+ATOM   5237  CG2 VAL A 414      -1.233  41.232  -1.550  1.00 17.20           C  
+ATOM   5238  H   VAL A 414       0.847  39.695  -1.061  1.00 14.74           H  
+ATOM   5239  HA  VAL A 414      -0.288  38.474  -3.199  1.00 12.80           H  
+ATOM   5240  HB  VAL A 414      -1.941  40.178  -3.146  1.00 15.52           H  
+ATOM   5241 HG11 VAL A 414      -3.116  39.337  -1.349  1.00 16.92           H  
+ATOM   5242 HG12 VAL A 414      -2.427  38.160  -2.163  1.00 16.92           H  
+ATOM   5243 HG13 VAL A 414      -1.788  38.661  -0.798  1.00 16.92           H  
+ATOM   5244 HG21 VAL A 414      -2.097  41.612  -1.328  1.00 20.65           H  
+ATOM   5245 HG22 VAL A 414      -0.742  41.026  -0.739  1.00 20.65           H  
+ATOM   5246 HG23 VAL A 414      -0.727  41.856  -2.094  1.00 20.65           H  
+ATOM   5247  N   VAL A 415       0.492  39.989  -4.977  1.00 11.64           N  
+ATOM   5248  CA  VAL A 415       1.213  40.730  -6.004  1.00 12.03           C  
+ATOM   5249  C   VAL A 415       0.203  41.198  -7.047  1.00 11.28           C  
+ATOM   5250  O   VAL A 415      -0.015  40.510  -8.059  1.00 11.33           O  
+ATOM   5251  CB  VAL A 415       2.323  39.879  -6.639  1.00 11.38           C  
+ATOM   5252  CG1 VAL A 415       3.085  40.674  -7.680  1.00 12.96           C  
+ATOM   5253  CG2 VAL A 415       3.267  39.348  -5.558  1.00 15.81           C  
+ATOM   5254  H   VAL A 415      -0.056  39.406  -5.292  1.00 13.96           H  
+ATOM   5255  HA  VAL A 415       1.633  41.508  -5.605  1.00 14.43           H  
+ATOM   5256  HB  VAL A 415       1.917  39.120  -7.088  1.00 13.65           H  
+ATOM   5257 HG11 VAL A 415       3.864  40.166  -7.957  1.00 15.55           H  
+ATOM   5258 HG12 VAL A 415       2.506  40.834  -8.441  1.00 15.55           H  
+ATOM   5259 HG13 VAL A 415       3.363  41.518  -7.291  1.00 15.55           H  
+ATOM   5260 HG21 VAL A 415       3.999  38.874  -5.983  1.00 18.97           H  
+ATOM   5261 HG22 VAL A 415       3.611  40.095  -5.044  1.00 18.97           H  
+ATOM   5262 HG23 VAL A 415       2.776  38.746  -4.977  1.00 18.97           H  
+ATOM   5263  N   PRO A 416      -0.438  42.342  -6.832  1.00 11.08           N  
+ATOM   5264  CA  PRO A 416      -1.447  42.835  -7.778  1.00 10.62           C  
+ATOM   5265  C   PRO A 416      -0.799  43.615  -8.890  1.00 11.55           C  
+ATOM   5266  O   PRO A 416      -0.125  44.620  -8.635  1.00 13.12           O  
+ATOM   5267  CB  PRO A 416      -2.344  43.722  -6.903  1.00 15.18           C  
+ATOM   5268  CG  PRO A 416      -1.389  44.266  -5.852  1.00 15.07           C  
+ATOM   5269  CD  PRO A 416      -0.346  43.184  -5.620  1.00 13.62           C  
+ATOM   5270  HA  PRO A 416      -1.982  42.113  -8.141  1.00 12.75           H  
+ATOM   5271  HB2 PRO A 416      -2.729  44.437  -7.434  1.00 18.22           H  
+ATOM   5272  HB3 PRO A 416      -3.049  43.193  -6.499  1.00 18.22           H  
+ATOM   5273  HG2 PRO A 416      -0.971  45.078  -6.181  1.00 18.08           H  
+ATOM   5274  HG3 PRO A 416      -1.876  44.452  -5.034  1.00 18.08           H  
+ATOM   5275  HD2 PRO A 416       0.540  43.572  -5.537  1.00 16.35           H  
+ATOM   5276  HD3 PRO A 416      -0.557  42.668  -4.826  1.00 16.35           H  
+ATOM   5277  N   VAL A 417      -0.940  43.163 -10.134  1.00 10.71           N  
+ATOM   5278  CA  VAL A 417      -0.233  43.779 -11.248  1.00 10.69           C  
+ATOM   5279  C   VAL A 417      -1.137  44.893 -11.762  1.00 12.63           C  
+ATOM   5280  O   VAL A 417      -1.890  44.724 -12.707  1.00 11.82           O  
+ATOM   5281  CB  VAL A 417       0.154  42.767 -12.311  1.00 11.19           C  
+ATOM   5282  CG1 VAL A 417       1.043  43.420 -13.370  1.00 13.32           C  
+ATOM   5283  CG2 VAL A 417       0.874  41.605 -11.686  1.00 11.88           C  
+ATOM   5284  H   VAL A 417      -1.441  42.500 -10.355  1.00 12.85           H  
+ATOM   5285  HA  VAL A 417       0.586  44.188 -10.928  1.00 12.82           H  
+ATOM   5286  HB  VAL A 417      -0.652  42.441 -12.741  1.00 13.43           H  
+ATOM   5287 HG11 VAL A 417       1.306  42.748 -14.019  1.00 15.98           H  
+ATOM   5288 HG12 VAL A 417       0.545  44.127 -13.808  1.00 15.98           H  
+ATOM   5289 HG13 VAL A 417       1.830  43.788 -12.938  1.00 15.98           H  
+ATOM   5290 HG21 VAL A 417       1.224  41.035 -12.389  1.00 14.25           H  
+ATOM   5291 HG22 VAL A 417       1.602  41.941 -11.140  1.00 14.25           H  
+ATOM   5292 HG23 VAL A 417       0.250  41.106 -11.135  1.00 14.25           H  
+ATOM   5293  N   GLY A 418      -1.015  46.065 -11.122  1.00 12.70           N  
+ATOM   5294  CA  GLY A 418      -1.955  47.136 -11.374  1.00 13.61           C  
+ATOM   5295  C   GLY A 418      -1.974  47.610 -12.815  1.00 13.90           C  
+ATOM   5296  O   GLY A 418      -3.003  48.090 -13.296  1.00 12.67           O  
+ATOM   5297  H   GLY A 418      -0.403  46.253 -10.548  1.00 15.24           H  
+ATOM   5298  HA2 GLY A 418      -2.848  46.831 -11.146  1.00 16.33           H  
+ATOM   5299  HA3 GLY A 418      -1.727  47.893 -10.812  1.00 16.33           H  
+ATOM   5300  N   ALA A 419      -0.856  47.456 -13.530  1.00 13.62           N  
+ATOM   5301  CA  ALA A 419      -0.788  47.895 -14.918  1.00 12.88           C  
+ATOM   5302  C   ALA A 419      -1.773  47.151 -15.810  1.00 13.85           C  
+ATOM   5303  O   ALA A 419      -2.126  47.651 -16.887  1.00 15.06           O  
+ATOM   5304  CB  ALA A 419       0.631  47.716 -15.451  1.00 12.88           C  
+ATOM   5305  H   ALA A 419      -0.130  47.102 -13.234  1.00 16.34           H  
+ATOM   5306  HA  ALA A 419      -1.009  48.839 -14.955  1.00 15.45           H  
+ATOM   5307  HB1 ALA A 419       0.662  48.016 -16.373  1.00 15.46           H  
+ATOM   5308  HB2 ALA A 419       1.240  48.242 -14.910  1.00 15.46           H  
+ATOM   5309  HB3 ALA A 419       0.871  46.777 -15.401  1.00 15.46           H  
+ATOM   5310  N   THR A 420      -2.254  45.991 -15.381  1.00 12.96           N  
+ATOM   5311  CA  THR A 420      -3.205  45.243 -16.188  1.00 12.03           C  
+ATOM   5312  C   THR A 420      -4.648  45.707 -16.008  1.00 11.94           C  
+ATOM   5313  O   THR A 420      -5.531  45.211 -16.716  1.00 12.66           O  
+ATOM   5314  CB  THR A 420      -3.103  43.729 -15.913  1.00 10.83           C  
+ATOM   5315  OG1 THR A 420      -3.479  43.413 -14.561  1.00 12.05           O  
+ATOM   5316  CG2 THR A 420      -1.690  43.245 -16.188  1.00 13.83           C  
+ATOM   5317  H   THR A 420      -2.046  45.620 -14.633  1.00 15.55           H  
+ATOM   5318  HA  THR A 420      -2.967  45.378 -17.119  1.00 14.44           H  
+ATOM   5319  HB  THR A 420      -3.715  43.261 -16.503  1.00 12.99           H  
+ATOM   5320  HG1 THR A 420      -2.948  43.778 -14.023  1.00 14.46           H  
+ATOM   5321 HG21 THR A 420      -1.643  42.282 -16.083  1.00 16.60           H  
+ATOM   5322 HG22 THR A 420      -1.431  43.476 -17.094  1.00 16.60           H  
+ATOM   5323 HG23 THR A 420      -1.071  43.660 -15.568  1.00 16.60           H  
+ATOM   5324  N   GLY A 421      -4.914  46.665 -15.124  1.00 12.62           N  
+ATOM   5325  CA  GLY A 421      -6.236  47.243 -15.024  1.00 12.20           C  
+ATOM   5326  C   GLY A 421      -7.228  46.433 -14.204  1.00 12.28           C  
+ATOM   5327  O   GLY A 421      -6.899  45.449 -13.550  1.00 12.34           O  
+ATOM   5328  H   GLY A 421      -4.341  46.993 -14.573  1.00 15.14           H  
+ATOM   5329  HA2 GLY A 421      -6.162  48.120 -14.617  1.00 14.64           H  
+ATOM   5330  HA3 GLY A 421      -6.602  47.339 -15.918  1.00 14.64           H  
+ATOM   5331  N   TYR A 422      -8.475  46.882 -14.238  1.00 11.90           N  
+ATOM   5332  CA  TYR A 422      -9.628  46.127 -13.713  1.00 11.14           C  
+ATOM   5333  C   TYR A 422      -9.410  45.807 -12.236  1.00 12.76           C  
+ATOM   5334  O   TYR A 422      -8.963  46.674 -11.468  1.00 12.78           O  
+ATOM   5335  CB  TYR A 422      -9.881  44.890 -14.615  1.00 13.39           C  
+ATOM   5336  CG  TYR A 422      -9.860  45.216 -16.084  1.00 13.90           C  
+ATOM   5337  CD1 TYR A 422     -10.985  45.718 -16.727  1.00 12.03           C  
+ATOM   5338  CD2 TYR A 422      -8.703  45.027 -16.830  1.00 13.35           C  
+ATOM   5339  CE1 TYR A 422     -10.941  46.027 -18.070  1.00 13.32           C  
+ATOM   5340  CE2 TYR A 422      -8.641  45.344 -18.161  1.00 12.54           C  
+ATOM   5341  CZ  TYR A 422      -9.762  45.836 -18.787  1.00 13.68           C  
+ATOM   5342  OH  TYR A 422      -9.674  46.137 -20.136  1.00 13.85           O  
+ATOM   5343  H   TYR A 422      -8.696  47.645 -14.568  1.00 14.28           H  
+ATOM   5344  HA  TYR A 422     -10.395  46.719 -13.745  1.00 13.37           H  
+ATOM   5345  HB2 TYR A 422      -9.190  44.231 -14.445  1.00 16.07           H  
+ATOM   5346  HB3 TYR A 422     -10.752  44.520 -14.404  1.00 16.07           H  
+ATOM   5347  HD1 TYR A 422     -11.772  45.846 -16.249  1.00 14.44           H  
+ATOM   5348  HD2 TYR A 422      -7.949  44.675 -16.413  1.00 16.01           H  
+ATOM   5349  HE1 TYR A 422     -11.697  46.362 -18.497  1.00 15.98           H  
+ATOM   5350  HE2 TYR A 422      -7.850  45.227 -18.636  1.00 15.04           H  
+ATOM   5351  HH  TYR A 422     -10.382  46.508 -20.395  1.00 16.62           H  
+ATOM   5352  N   ILE A 423      -9.741  44.593 -11.796  1.00 11.80           N  
+ATOM   5353  CA  ILE A 423      -9.585  44.242 -10.381  1.00 12.38           C  
+ATOM   5354  C   ILE A 423      -8.122  44.334  -9.959  1.00 12.76           C  
+ATOM   5355  O   ILE A 423      -7.807  44.740  -8.833  1.00 12.06           O  
+ATOM   5356  CB  ILE A 423     -10.141  42.836 -10.102  1.00 12.33           C  
+ATOM   5357  CG1 ILE A 423     -11.672  42.792 -10.202  1.00 15.74           C  
+ATOM   5358  CG2 ILE A 423      -9.672  42.340  -8.722  1.00 12.82           C  
+ATOM   5359  CD1 ILE A 423     -12.409  43.494  -9.106  1.00 18.04           C  
+ATOM   5360  H   ILE A 423     -10.054  43.960 -12.287  1.00 14.16           H  
+ATOM   5361  HA  ILE A 423     -10.098  44.883  -9.863  1.00 14.86           H  
+ATOM   5362  HB  ILE A 423      -9.791  42.245 -10.787  1.00 14.80           H  
+ATOM   5363 HG12 ILE A 423     -11.935  43.208 -11.038  1.00 18.89           H  
+ATOM   5364 HG13 ILE A 423     -11.952  41.864 -10.190  1.00 18.89           H  
+ATOM   5365 HG21 ILE A 423     -10.256  41.623  -8.429  1.00 15.38           H  
+ATOM   5366 HG22 ILE A 423      -8.761  42.016  -8.795  1.00 15.38           H  
+ATOM   5367 HG23 ILE A 423      -9.712  43.076  -8.092  1.00 15.38           H  
+ATOM   5368 HD11 ILE A 423     -13.362  43.376  -9.240  1.00 21.65           H  
+ATOM   5369 HD12 ILE A 423     -12.146  43.112  -8.254  1.00 21.65           H  
+ATOM   5370 HD13 ILE A 423     -12.186  44.437  -9.128  1.00 21.65           H  
+ATOM   5371  N   ALA A 424      -7.195  43.929 -10.830  1.00 12.21           N  
+ATOM   5372  CA  ALA A 424      -5.796  43.973 -10.448  1.00 11.66           C  
+ATOM   5373  C   ALA A 424      -5.371  45.393 -10.107  1.00 11.83           C  
+ATOM   5374  O   ALA A 424      -4.578  45.599  -9.186  1.00 12.26           O  
+ATOM   5375  CB  ALA A 424      -4.910  43.385 -11.550  1.00 12.69           C  
+ATOM   5376  H   ALA A 424      -7.351  43.635 -11.623  1.00 14.65           H  
+ATOM   5377  HA  ALA A 424      -5.673  43.421  -9.660  1.00 13.99           H  
+ATOM   5378  HB1 ALA A 424      -3.984  43.417 -11.261  1.00 15.23           H  
+ATOM   5379  HB2 ALA A 424      -5.174  42.465 -11.710  1.00 15.23           H  
+ATOM   5380  HB3 ALA A 424      -5.023  43.908 -12.359  1.00 15.23           H  
+ATOM   5381  N   LYS A 425      -5.909  46.382 -10.829  1.00 13.11           N  
+ATOM   5382  CA  LYS A 425      -5.652  47.784 -10.515  1.00 14.04           C  
+ATOM   5383  C   LYS A 425      -6.282  48.190  -9.188  1.00 13.64           C  
+ATOM   5384  O   LYS A 425      -5.632  48.860  -8.373  1.00 13.30           O  
+ATOM   5385  CB  LYS A 425      -6.180  48.650 -11.663  1.00 13.26           C  
+ATOM   5386  CG  LYS A 425      -6.163  50.136 -11.389  1.00 18.60           C  
+ATOM   5387  CD  LYS A 425      -4.807  50.694 -11.601  1.00 19.91           C  
+ATOM   5388  CE  LYS A 425      -4.536  50.963 -13.072  1.00 20.96           C  
+ATOM   5389  NZ  LYS A 425      -3.193  51.568 -13.208  1.00 21.55           N  
+ATOM   5390  H   LYS A 425      -6.427  46.265 -11.506  1.00 15.73           H  
+ATOM   5391  HA  LYS A 425      -4.697  47.927 -10.428  1.00 16.85           H  
+ATOM   5392  HB2 LYS A 425      -5.632  48.491 -12.447  1.00 15.92           H  
+ATOM   5393  HB3 LYS A 425      -7.099  48.396 -11.844  1.00 15.92           H  
+ATOM   5394  HG2 LYS A 425      -6.778  50.583 -11.992  1.00 22.32           H  
+ATOM   5395  HG3 LYS A 425      -6.423  50.299 -10.469  1.00 22.32           H  
+ATOM   5396  HD2 LYS A 425      -4.726  51.532 -11.118  1.00 23.89           H  
+ATOM   5397  HD3 LYS A 425      -4.146  50.061 -11.280  1.00 23.89           H  
+ATOM   5398  HE2 LYS A 425      -4.560  50.132 -13.570  1.00 25.15           H  
+ATOM   5399  HE3 LYS A 425      -5.197  51.580 -13.423  1.00 25.15           H  
+ATOM   5400  HZ1 LYS A 425      -3.157  52.335 -12.757  1.00 25.86           H  
+ATOM   5401  HZ2 LYS A 425      -2.576  51.014 -12.886  1.00 25.86           H  
+ATOM   5402  HZ3 LYS A 425      -3.018  51.729 -14.065  1.00 25.86           H  
+ATOM   5403  N   ASP A 426      -7.539  47.794  -8.951  1.00 13.44           N  
+ATOM   5404  CA  ASP A 426      -8.179  48.078  -7.667  1.00 13.18           C  
+ATOM   5405  C   ASP A 426      -7.375  47.476  -6.522  1.00 15.77           C  
+ATOM   5406  O   ASP A 426      -7.178  48.113  -5.475  1.00 15.68           O  
+ATOM   5407  CB  ASP A 426      -9.602  47.531  -7.648  1.00 12.72           C  
+ATOM   5408  CG  ASP A 426     -10.525  48.248  -8.598  1.00 18.11           C  
+ATOM   5409  OD1 ASP A 426     -10.202  49.377  -9.024  1.00 19.66           O  
+ATOM   5410  OD2 ASP A 426     -11.588  47.679  -8.905  1.00 20.49           O  
+ATOM   5411  H   ASP A 426      -8.033  47.365  -9.509  1.00 16.13           H  
+ATOM   5412  HA  ASP A 426      -8.225  49.040  -7.550  1.00 15.82           H  
+ATOM   5413  HB2 ASP A 426      -9.582  46.595  -7.900  1.00 15.26           H  
+ATOM   5414  HB3 ASP A 426      -9.963  47.626  -6.753  1.00 15.26           H  
+ATOM   5415  N   LEU A 427      -6.882  46.252  -6.711  1.00 13.79           N  
+ATOM   5416  CA  LEU A 427      -6.119  45.604  -5.654  1.00 12.13           C  
+ATOM   5417  C   LEU A 427      -4.776  46.292  -5.452  1.00 12.85           C  
+ATOM   5418  O   LEU A 427      -4.305  46.422  -4.321  1.00 12.88           O  
+ATOM   5419  CB  LEU A 427      -5.920  44.122  -5.982  1.00 11.18           C  
+ATOM   5420  CG  LEU A 427      -7.195  43.302  -6.023  1.00 11.97           C  
+ATOM   5421  CD1 LEU A 427      -6.899  41.894  -6.548  1.00 14.83           C  
+ATOM   5422  CD2 LEU A 427      -7.884  43.265  -4.661  1.00 14.30           C  
+ATOM   5423  H   LEU A 427      -6.974  45.787  -7.429  1.00 16.55           H  
+ATOM   5424  HA  LEU A 427      -6.618  45.661  -4.824  1.00 14.55           H  
+ATOM   5425  HB2 LEU A 427      -5.501  44.055  -6.854  1.00 13.41           H  
+ATOM   5426  HB3 LEU A 427      -5.344  43.733  -5.305  1.00 13.41           H  
+ATOM   5427  HG  LEU A 427      -7.820  43.723  -6.634  1.00 14.37           H  
+ATOM   5428 HD11 LEU A 427      -7.720  41.377  -6.548  1.00 17.79           H  
+ATOM   5429 HD12 LEU A 427      -6.550  41.960  -7.451  1.00 17.79           H  
+ATOM   5430 HD13 LEU A 427      -6.243  41.473  -5.970  1.00 17.79           H  
+ATOM   5431 HD21 LEU A 427      -8.602  42.613  -4.687  1.00 17.15           H  
+ATOM   5432 HD22 LEU A 427      -7.235  43.016  -3.985  1.00 17.15           H  
+ATOM   5433 HD23 LEU A 427      -8.244  44.145  -4.465  1.00 17.15           H  
+ATOM   5434  N   TRP A 428      -4.143  46.743  -6.541  1.00 11.96           N  
+ATOM   5435  CA  TRP A 428      -2.893  47.471  -6.407  1.00 10.66           C  
+ATOM   5436  C   TRP A 428      -3.107  48.745  -5.594  1.00 12.39           C  
+ATOM   5437  O   TRP A 428      -2.324  49.046  -4.692  1.00 13.63           O  
+ATOM   5438  CB  TRP A 428      -2.284  47.777  -7.789  1.00 12.83           C  
+ATOM   5439  CG  TRP A 428      -0.934  48.421  -7.671  1.00 11.86           C  
+ATOM   5440  CD1 TRP A 428       0.282  47.808  -7.717  1.00 12.67           C  
+ATOM   5441  CD2 TRP A 428      -0.674  49.813  -7.433  1.00 12.55           C  
+ATOM   5442  NE1 TRP A 428       1.288  48.735  -7.538  1.00 14.65           N  
+ATOM   5443  CE2 TRP A 428       0.723  49.970  -7.361  1.00 15.21           C  
+ATOM   5444  CE3 TRP A 428      -1.494  50.941  -7.298  1.00 14.21           C  
+ATOM   5445  CZ2 TRP A 428       1.330  51.210  -7.130  1.00 15.63           C  
+ATOM   5446  CZ3 TRP A 428      -0.888  52.177  -7.068  1.00 16.40           C  
+ATOM   5447  CH2 TRP A 428       0.508  52.297  -7.004  1.00 15.33           C  
+ATOM   5448  H   TRP A 428      -4.417  46.641  -7.350  1.00 14.35           H  
+ATOM   5449  HA  TRP A 428      -2.249  46.917  -5.941  1.00 12.79           H  
+ATOM   5450  HB2 TRP A 428      -2.183  46.949  -8.285  1.00 15.39           H  
+ATOM   5451  HB3 TRP A 428      -2.869  48.382  -8.271  1.00 15.39           H  
+ATOM   5452  HD1 TRP A 428       0.414  46.897  -7.849  1.00 15.21           H  
+ATOM   5453  HE1 TRP A 428       2.131  48.565  -7.539  1.00 17.58           H  
+ATOM   5454  HE3 TRP A 428      -2.419  50.868  -7.360  1.00 17.05           H  
+ATOM   5455  HZ2 TRP A 428       2.254  51.292  -7.066  1.00 18.75           H  
+ATOM   5456  HZ3 TRP A 428      -1.418  52.933  -6.955  1.00 19.68           H  
+ATOM   5457  HH2 TRP A 428       0.885  53.137  -6.871  1.00 18.39           H  
+ATOM   5458  N   ASN A 429      -4.193  49.468  -5.868  1.00 13.29           N  
+ATOM   5459  CA  ASN A 429      -4.458  50.691  -5.108  1.00 14.64           C  
+ATOM   5460  C   ASN A 429      -4.714  50.383  -3.636  1.00 16.58           C  
+ATOM   5461  O   ASN A 429      -4.208  51.087  -2.750  1.00 15.94           O  
+ATOM   5462  CB  ASN A 429      -5.635  51.439  -5.726  1.00 14.28           C  
+ATOM   5463  CG  ASN A 429      -5.259  52.179  -6.995  1.00 16.33           C  
+ATOM   5464  OD1 ASN A 429      -4.168  52.737  -7.104  1.00 24.50           O  
+ATOM   5465  ND2 ASN A 429      -6.154  52.176  -7.960  1.00 22.71           N  
+ATOM   5466  H   ASN A 429      -4.775  49.280  -6.472  1.00 15.95           H  
+ATOM   5467  HA  ASN A 429      -3.681  51.269  -5.155  1.00 17.57           H  
+ATOM   5468  HB2 ASN A 429      -6.334  50.803  -5.945  1.00 17.13           H  
+ATOM   5469  HB3 ASN A 429      -5.967  52.089  -5.087  1.00 17.13           H  
+ATOM   5470 HD21 ASN A 429      -5.990  52.581  -8.700  1.00 27.25           H  
+ATOM   5471 HD22 ASN A 429      -6.903  51.768  -7.850  1.00 27.25           H  
+ATOM   5472  N   LYS A 430      -5.497  49.339  -3.356  1.00 13.80           N  
+ATOM   5473  CA  LYS A 430      -5.746  48.925  -1.972  1.00 13.87           C  
+ATOM   5474  C   LYS A 430      -4.443  48.627  -1.240  1.00 17.20           C  
+ATOM   5475  O   LYS A 430      -4.237  49.062  -0.097  1.00 16.61           O  
+ATOM   5476  CB  LYS A 430      -6.669  47.702  -1.972  1.00 16.65           C  
+ATOM   5477  CG  LYS A 430      -6.948  47.071  -0.619  1.00 19.47           C  
+ATOM   5478  CD  LYS A 430      -7.814  45.826  -0.800  1.00 25.40           C  
+ATOM   5479  CE  LYS A 430      -8.309  45.259   0.518  1.00 31.89           C  
+ATOM   5480  NZ  LYS A 430      -8.989  46.295   1.346  1.00 37.79           N  
+ATOM   5481  H   LYS A 430      -5.895  48.855  -3.945  1.00 16.56           H  
+ATOM   5482  HA  LYS A 430      -6.188  49.646  -1.496  1.00 16.64           H  
+ATOM   5483  HB2 LYS A 430      -7.524  47.969  -2.344  1.00 19.98           H  
+ATOM   5484  HB3 LYS A 430      -6.264  47.019  -2.529  1.00 19.98           H  
+ATOM   5485  HG2 LYS A 430      -6.112  46.811  -0.200  1.00 23.37           H  
+ATOM   5486  HG3 LYS A 430      -7.421  47.701  -0.054  1.00 23.37           H  
+ATOM   5487  HD2 LYS A 430      -8.589  46.055  -1.337  1.00 30.48           H  
+ATOM   5488  HD3 LYS A 430      -7.293  45.140  -1.245  1.00 30.48           H  
+ATOM   5489  HE2 LYS A 430      -8.943  44.546   0.342  1.00 38.27           H  
+ATOM   5490  HE3 LYS A 430      -7.554  44.915   1.022  1.00 38.27           H  
+ATOM   5491  HZ1 LYS A 430      -9.380  45.914   2.049  1.00 45.35           H  
+ATOM   5492  HZ2 LYS A 430      -8.395  46.892   1.634  1.00 45.35           H  
+ATOM   5493  HZ3 LYS A 430      -9.608  46.713   0.862  1.00 45.35           H  
+ATOM   5494  N   VAL A 431      -3.550  47.861  -1.869  1.00 13.53           N  
+ATOM   5495  CA  VAL A 431      -2.286  47.537  -1.236  1.00 11.41           C  
+ATOM   5496  C   VAL A 431      -1.431  48.794  -1.081  1.00 16.07           C  
+ATOM   5497  O   VAL A 431      -0.819  49.020  -0.031  1.00 15.50           O  
+ATOM   5498  CB  VAL A 431      -1.576  46.423  -2.030  1.00 13.37           C  
+ATOM   5499  CG1 VAL A 431      -0.176  46.201  -1.516  1.00 13.84           C  
+ATOM   5500  CG2 VAL A 431      -2.397  45.120  -1.970  1.00 13.45           C  
+ATOM   5501  H   VAL A 431      -3.656  47.523  -2.653  1.00 16.24           H  
+ATOM   5502  HA  VAL A 431      -2.452  47.197  -0.342  1.00 13.69           H  
+ATOM   5503  HB  VAL A 431      -1.506  46.698  -2.957  1.00 16.04           H  
+ATOM   5504 HG11 VAL A 431       0.160  45.361  -1.867  1.00 16.61           H  
+ATOM   5505 HG12 VAL A 431       0.389  46.932  -1.811  1.00 16.61           H  
+ATOM   5506 HG13 VAL A 431      -0.197  46.170  -0.546  1.00 16.61           H  
+ATOM   5507 HG21 VAL A 431      -1.939  44.435  -2.483  1.00 16.14           H  
+ATOM   5508 HG22 VAL A 431      -2.479  44.841  -1.045  1.00 16.14           H  
+ATOM   5509 HG23 VAL A 431      -3.276  45.283  -2.346  1.00 16.14           H  
+ATOM   5510  N   ASN A 432      -1.401  49.643  -2.108  1.00 16.30           N  
+ATOM   5511  CA  ASN A 432      -0.605  50.862  -2.042  1.00 15.30           C  
+ATOM   5512  C   ASN A 432      -1.046  51.744  -0.883  1.00 17.64           C  
+ATOM   5513  O   ASN A 432      -0.210  52.413  -0.256  1.00 19.72           O  
+ATOM   5514  CB  ASN A 432      -0.727  51.619  -3.363  1.00 16.77           C  
+ATOM   5515  CG  ASN A 432       0.252  52.770  -3.465  1.00 16.71           C  
+ATOM   5516  OD1 ASN A 432       1.438  52.616  -3.181  1.00 18.05           O  
+ATOM   5517  ND2 ASN A 432      -0.240  53.915  -3.893  1.00 22.85           N  
+ATOM   5518  H   ASN A 432      -1.829  49.537  -2.846  1.00 19.56           H  
+ATOM   5519  HA  ASN A 432       0.328  50.633  -1.906  1.00 18.36           H  
+ATOM   5520  HB2 ASN A 432      -0.550  51.008  -4.095  1.00 20.12           H  
+ATOM   5521  HB3 ASN A 432      -1.624  51.980  -3.440  1.00 20.12           H  
+ATOM   5522 HD21 ASN A 432       0.272  54.601  -3.969  1.00 27.42           H  
+ATOM   5523 HD22 ASN A 432      -1.074  53.976  -4.095  1.00 27.42           H  
+ATOM   5524  N   GLU A 433      -2.342  51.729  -0.576  1.00 16.26           N  
+ATOM   5525  CA  GLU A 433      -2.914  52.567   0.480  1.00 18.25           C  
+ATOM   5526  C   GLU A 433      -2.544  52.076   1.875  1.00 22.60           C  
+ATOM   5527  O   GLU A 433      -2.534  52.878   2.817  1.00 23.07           O  
+ATOM   5528  CB  GLU A 433      -4.429  52.630   0.312  1.00 19.10           C  
+ATOM   5529  CG  GLU A 433      -4.853  53.529  -0.830  1.00 22.03           C  
+ATOM   5530  CD  GLU A 433      -6.222  53.207  -1.393  1.00 22.88           C  
+ATOM   5531  OE1 GLU A 433      -6.918  52.339  -0.829  1.00 24.78           O  
+ATOM   5532  OE2 GLU A 433      -6.586  53.820  -2.425  1.00 30.34           O  
+ATOM   5533  H   GLU A 433      -2.925  51.234  -0.970  1.00 19.52           H  
+ATOM   5534  HA  GLU A 433      -2.568  53.469   0.398  1.00 21.90           H  
+ATOM   5535  HB2 GLU A 433      -4.764  51.737   0.133  1.00 22.92           H  
+ATOM   5536  HB3 GLU A 433      -4.823  52.975   1.129  1.00 22.92           H  
+ATOM   5537  HG2 GLU A 433      -4.873  54.446  -0.514  1.00 26.44           H  
+ATOM   5538  HG3 GLU A 433      -4.210  53.441  -1.551  1.00 26.44           H  
+ATOM   5539  N   GLU A 434      -2.215  50.794   2.029  1.00 18.33           N  
+ATOM   5540  CA  GLU A 434      -1.872  50.208   3.328  1.00 19.65           C  
+ATOM   5541  C   GLU A 434      -0.657  49.304   3.165  1.00 16.84           C  
+ATOM   5542  O   GLU A 434      -0.639  48.140   3.575  1.00 17.39           O  
+ATOM   5543  CB  GLU A 434      -3.073  49.466   3.906  1.00 27.81           C  
+ATOM   5544  CG  GLU A 434      -4.223  50.394   4.264  1.00 33.45           C  
+ATOM   5545  CD  GLU A 434      -5.436  49.663   4.812  1.00 62.71           C  
+ATOM   5546  OE1 GLU A 434      -5.398  48.416   4.910  1.00 63.91           O  
+ATOM   5547  OE2 GLU A 434      -6.431  50.343   5.147  1.00 75.34           O  
+ATOM   5548  H   GLU A 434      -2.183  50.229   1.381  1.00 22.00           H  
+ATOM   5549  HA  GLU A 434      -1.628  50.908   3.954  1.00 23.58           H  
+ATOM   5550  HB2 GLU A 434      -3.395  48.828   3.251  1.00 33.38           H  
+ATOM   5551  HB3 GLU A 434      -2.800  49.003   4.713  1.00 33.38           H  
+ATOM   5552  HG2 GLU A 434      -3.922  51.021   4.940  1.00 40.14           H  
+ATOM   5553  HG3 GLU A 434      -4.500  50.873   3.467  1.00 40.14           H  
+ATOM   5554  N   PHE A 435       0.398  49.870   2.586  1.00 19.36           N  
+ATOM   5555  CA  PHE A 435       1.516  49.076   2.098  1.00 17.90           C  
+ATOM   5556  C   PHE A 435       2.137  48.229   3.201  1.00 18.66           C  
+ATOM   5557  O   PHE A 435       2.489  47.062   2.970  1.00 19.16           O  
+ATOM   5558  CB  PHE A 435       2.543  50.013   1.470  1.00 17.99           C  
+ATOM   5559  CG  PHE A 435       3.694  49.325   0.841  1.00 19.09           C  
+ATOM   5560  CD1 PHE A 435       3.644  48.924  -0.486  1.00 17.98           C  
+ATOM   5561  CD2 PHE A 435       4.849  49.095   1.558  1.00 20.47           C  
+ATOM   5562  CE1 PHE A 435       4.731  48.301  -1.066  1.00 21.13           C  
+ATOM   5563  CE2 PHE A 435       5.922  48.475   0.985  1.00 20.00           C  
+ATOM   5564  CZ  PHE A 435       5.865  48.065  -0.331  1.00 21.12           C  
+ATOM   5565  H   PHE A 435       0.490  50.716   2.463  1.00 23.23           H  
+ATOM   5566  HA  PHE A 435       1.204  48.456   1.420  1.00 21.49           H  
+ATOM   5567  HB2 PHE A 435       2.103  50.537   0.782  1.00 21.59           H  
+ATOM   5568  HB3 PHE A 435       2.891  50.598   2.160  1.00 21.59           H  
+ATOM   5569  HD1 PHE A 435       2.875  49.076  -0.987  1.00 21.58           H  
+ATOM   5570  HD2 PHE A 435       4.898  49.368   2.446  1.00 24.56           H  
+ATOM   5571  HE1 PHE A 435       4.695  48.040  -1.958  1.00 25.36           H  
+ATOM   5572  HE2 PHE A 435       6.693  48.328   1.484  1.00 24.00           H  
+ATOM   5573  HZ  PHE A 435       6.591  47.632  -0.718  1.00 25.34           H  
+ATOM   5574  N   GLU A 436       2.283  48.789   4.405  1.00 21.60           N  
+ATOM   5575  CA  GLU A 436       2.955  48.071   5.482  1.00 21.96           C  
+ATOM   5576  C   GLU A 436       2.134  46.904   6.017  1.00 21.89           C  
+ATOM   5577  O   GLU A 436       2.701  46.021   6.681  1.00 22.48           O  
+ATOM   5578  CB  GLU A 436       3.301  49.052   6.612  1.00 27.43           C  
+ATOM   5579  CG  GLU A 436       4.024  48.405   7.791  1.00 50.91           C  
+ATOM   5580  CD  GLU A 436       4.579  49.409   8.797  1.00 70.43           C  
+ATOM   5581  OE1 GLU A 436       4.453  50.634   8.570  1.00 77.60           O  
+ATOM   5582  OE2 GLU A 436       5.148  48.961   9.818  1.00 63.05           O  
+ATOM   5583  H   GLU A 436       2.005  49.574   4.618  1.00 25.92           H  
+ATOM   5584  HA  GLU A 436       3.784  47.697   5.143  1.00 26.35           H  
+ATOM   5585  HB2 GLU A 436       3.877  49.746   6.256  1.00 32.91           H  
+ATOM   5586  HB3 GLU A 436       2.479  49.442   6.947  1.00 32.91           H  
+ATOM   5587  HG2 GLU A 436       3.402  47.829   8.262  1.00 61.10           H  
+ATOM   5588  HG3 GLU A 436       4.769  47.883   7.453  1.00 61.10           H  
+ATOM   5589  N   THR A 437       0.824  46.871   5.742  1.00 17.10           N  
+ATOM   5590  CA  THR A 437       0.002  45.723   6.112  1.00 17.40           C  
+ATOM   5591  C   THR A 437       0.350  44.523   5.249  1.00 19.71           C  
+ATOM   5592  O   THR A 437       0.336  43.375   5.711  1.00 19.77           O  
+ATOM   5593  CB  THR A 437      -1.484  46.042   5.949  1.00 22.12           C  
+ATOM   5594  OG1 THR A 437      -1.892  47.013   6.925  1.00 25.44           O  
+ATOM   5595  CG2 THR A 437      -2.364  44.774   6.088  1.00 22.23           C  
+ATOM   5596  H   THR A 437       0.392  47.498   5.343  1.00 20.52           H  
+ATOM   5597  HA  THR A 437       0.167  45.517   7.046  1.00 20.88           H  
+ATOM   5598  HB  THR A 437      -1.621  46.401   5.058  1.00 26.54           H  
+ATOM   5599  HG1 THR A 437      -2.706  47.195   6.826  1.00 30.53           H  
+ATOM   5600 HG21 THR A 437      -3.286  45.026   6.251  1.00 26.67           H  
+ATOM   5601 HG22 THR A 437      -2.320  44.249   5.274  1.00 26.67           H  
+ATOM   5602 HG23 THR A 437      -2.050  44.232   6.829  1.00 26.67           H  
+ATOM   5603  N   TYR A 438       0.636  44.774   3.982  1.00 15.48           N  
+ATOM   5604  CA  TYR A 438       0.889  43.704   3.032  1.00 13.75           C  
+ATOM   5605  C   TYR A 438       2.354  43.319   2.952  1.00 15.73           C  
+ATOM   5606  O   TYR A 438       2.663  42.141   2.719  1.00 15.41           O  
+ATOM   5607  CB  TYR A 438       0.352  44.124   1.649  1.00 12.42           C  
+ATOM   5608  CG  TYR A 438      -1.135  44.247   1.687  1.00 12.08           C  
+ATOM   5609  CD1 TYR A 438      -1.951  43.134   1.557  1.00 14.78           C  
+ATOM   5610  CD2 TYR A 438      -1.753  45.475   1.928  1.00 14.70           C  
+ATOM   5611  CE1 TYR A 438      -3.332  43.238   1.630  1.00 16.32           C  
+ATOM   5612  CE2 TYR A 438      -3.128  45.589   2.008  1.00 14.13           C  
+ATOM   5613  CZ  TYR A 438      -3.916  44.465   1.860  1.00 17.42           C  
+ATOM   5614  OH  TYR A 438      -5.283  44.574   1.934  1.00 22.05           O  
+ATOM   5615  H   TYR A 438       0.691  45.563   3.643  1.00 18.57           H  
+ATOM   5616  HA  TYR A 438       0.413  42.903   3.302  1.00 16.50           H  
+ATOM   5617  HB2 TYR A 438       0.729  44.983   1.401  1.00 14.90           H  
+ATOM   5618  HB3 TYR A 438       0.592  43.454   0.990  1.00 14.90           H  
+ATOM   5619  HD1 TYR A 438      -1.564  42.300   1.418  1.00 17.74           H  
+ATOM   5620  HD2 TYR A 438      -1.227  46.235   2.037  1.00 17.64           H  
+ATOM   5621  HE1 TYR A 438      -3.863  42.482   1.523  1.00 19.59           H  
+ATOM   5622  HE2 TYR A 438      -3.520  46.418   2.160  1.00 16.96           H  
+ATOM   5623  HH  TYR A 438      -5.637  43.821   1.822  1.00 26.46           H  
+ATOM   5624  N   TYR A 439       3.269  44.266   3.156  1.00 15.87           N  
+ATOM   5625  CA  TYR A 439       4.702  44.011   3.054  1.00 16.18           C  
+ATOM   5626  C   TYR A 439       5.424  44.669   4.225  1.00 19.43           C  
+ATOM   5627  O   TYR A 439       6.223  45.595   4.047  1.00 16.13           O  
+ATOM   5628  CB  TYR A 439       5.273  44.533   1.730  1.00 15.84           C  
+ATOM   5629  CG  TYR A 439       4.456  44.236   0.489  1.00 16.37           C  
+ATOM   5630  CD1 TYR A 439       4.344  42.955  -0.016  1.00 19.35           C  
+ATOM   5631  CD2 TYR A 439       3.855  45.275  -0.207  1.00 18.65           C  
+ATOM   5632  CE1 TYR A 439       3.591  42.716  -1.152  1.00 14.89           C  
+ATOM   5633  CE2 TYR A 439       3.130  45.052  -1.348  1.00 18.12           C  
+ATOM   5634  CZ  TYR A 439       2.999  43.772  -1.821  1.00 17.12           C  
+ATOM   5635  OH  TYR A 439       2.252  43.574  -2.970  1.00 16.24           O  
+ATOM   5636  H   TYR A 439       3.078  45.080   3.359  1.00 19.04           H  
+ATOM   5637  HA  TYR A 439       4.836  43.051   3.101  1.00 19.42           H  
+ATOM   5638  HB2 TYR A 439       5.354  45.498   1.795  1.00 19.01           H  
+ATOM   5639  HB3 TYR A 439       6.148  44.135   1.599  1.00 19.01           H  
+ATOM   5640  HD1 TYR A 439       4.777  42.251   0.409  1.00 23.22           H  
+ATOM   5641  HD2 TYR A 439       3.947  46.145   0.108  1.00 22.38           H  
+ATOM   5642  HE1 TYR A 439       3.483  41.847  -1.464  1.00 17.86           H  
+ATOM   5643  HE2 TYR A 439       2.731  45.761  -1.797  1.00 21.74           H  
+ATOM   5644  HH  TYR A 439       2.248  42.759  -3.173  1.00 19.49           H  
+ATOM   5645  N   PRO A 440       5.167  44.216   5.445  1.00 19.05           N  
+ATOM   5646  CA  PRO A 440       5.816  44.853   6.597  1.00 19.74           C  
+ATOM   5647  C   PRO A 440       7.327  44.732   6.499  1.00 17.54           C  
+ATOM   5648  O   PRO A 440       7.870  43.685   6.140  1.00 19.92           O  
+ATOM   5649  CB  PRO A 440       5.250  44.085   7.797  1.00 23.59           C  
+ATOM   5650  CG  PRO A 440       4.770  42.795   7.254  1.00 22.17           C  
+ATOM   5651  CD  PRO A 440       4.334  43.066   5.836  1.00 20.96           C  
+ATOM   5652  HA  PRO A 440       5.567  45.788   6.671  1.00 23.68           H  
+ATOM   5653  HB2 PRO A 440       5.949  43.943   8.454  1.00 28.30           H  
+ATOM   5654  HB3 PRO A 440       4.519  44.586   8.191  1.00 28.30           H  
+ATOM   5655  HG2 PRO A 440       5.490  42.146   7.272  1.00 26.61           H  
+ATOM   5656  HG3 PRO A 440       4.023  42.476   7.786  1.00 26.61           H  
+ATOM   5657  HD2 PRO A 440       4.512  42.300   5.267  1.00 25.15           H  
+ATOM   5658  HD3 PRO A 440       3.392  43.293   5.801  1.00 25.15           H  
+ATOM   5659  N   GLY A 441       8.015  45.836   6.798  1.00 22.96           N  
+ATOM   5660  CA  GLY A 441       9.461  45.813   6.746  1.00 21.22           C  
+ATOM   5661  C   GLY A 441      10.060  45.783   5.360  1.00 22.65           C  
+ATOM   5662  O   GLY A 441      11.227  45.417   5.209  1.00 24.19           O  
+ATOM   5663  H   GLY A 441       7.668  46.589   7.028  1.00 27.55           H  
+ATOM   5664  HA2 GLY A 441       9.798  46.604   7.194  1.00 25.47           H  
+ATOM   5665  HA3 GLY A 441       9.773  45.025   7.217  1.00 25.47           H  
+ATOM   5666  N   ALA A 442       9.297  46.150   4.339  1.00 19.33           N  
+ATOM   5667  CA  ALA A 442       9.817  46.100   2.980  1.00 20.10           C  
+ATOM   5668  C   ALA A 442      11.006  47.040   2.820  1.00 22.15           C  
+ATOM   5669  O   ALA A 442      11.082  48.089   3.466  1.00 23.20           O  
+ATOM   5670  CB  ALA A 442       8.726  46.485   1.986  1.00 19.27           C  
+ATOM   5671  H   ALA A 442       8.486  46.428   4.404  1.00 23.19           H  
+ATOM   5672  HA  ALA A 442      10.113  45.197   2.785  1.00 24.12           H  
+ATOM   5673  HB1 ALA A 442       9.088  46.440   1.087  1.00 23.13           H  
+ATOM   5674  HB2 ALA A 442       7.985  45.866   2.075  1.00 23.13           H  
+ATOM   5675  HB3 ALA A 442       8.428  47.388   2.178  1.00 23.13           H  
+ATOM   5676  N   ASP A 443      11.933  46.659   1.935  1.00 20.33           N  
+ATOM   5677  CA  ASP A 443      13.093  47.485   1.632  1.00 20.85           C  
+ATOM   5678  C   ASP A 443      12.842  48.360   0.396  1.00 21.32           C  
+ATOM   5679  O   ASP A 443      11.776  48.333  -0.226  1.00 19.80           O  
+ATOM   5680  CB  ASP A 443      14.347  46.621   1.485  1.00 22.06           C  
+ATOM   5681  CG  ASP A 443      14.329  45.709   0.268  1.00 26.11           C  
+ATOM   5682  OD1 ASP A 443      13.463  45.863  -0.618  1.00 24.36           O  
+ATOM   5683  OD2 ASP A 443      15.220  44.833   0.196  1.00 33.29           O  
+ATOM   5684  H   ASP A 443      11.907  45.920   1.496  1.00 24.39           H  
+ATOM   5685  HA  ASP A 443      13.238  48.087   2.378  1.00 25.02           H  
+ATOM   5686  HB2 ASP A 443      15.119  47.203   1.406  1.00 26.47           H  
+ATOM   5687  HB3 ASP A 443      14.433  46.060   2.271  1.00 26.47           H  
+ATOM   5688  N   ALA A 444      13.825  49.207   0.083  1.00 19.94           N  
+ATOM   5689  CA  ALA A 444      13.642  50.186  -0.983  1.00 18.51           C  
+ATOM   5690  C   ALA A 444      13.412  49.504  -2.320  1.00 17.68           C  
+ATOM   5691  O   ALA A 444      12.613  49.977  -3.135  1.00 18.86           O  
+ATOM   5692  CB  ALA A 444      14.860  51.111  -1.078  1.00 20.97           C  
+ATOM   5693  H   ALA A 444      14.595  49.234   0.467  1.00 23.93           H  
+ATOM   5694  HA  ALA A 444      12.864  50.725  -0.769  1.00 22.22           H  
+ATOM   5695  HB1 ALA A 444      14.711  51.758  -1.785  1.00 25.17           H  
+ATOM   5696  HB2 ALA A 444      14.977  51.568  -0.230  1.00 25.17           H  
+ATOM   5697  HB3 ALA A 444      15.646  50.578  -1.277  1.00 25.17           H  
+ATOM   5698  N   ARG A 445      14.125  48.407  -2.578  1.00 18.56           N  
+ATOM   5699  CA  ARG A 445      13.949  47.726  -3.860  1.00 19.28           C  
+ATOM   5700  C   ARG A 445      12.531  47.198  -3.986  1.00 17.60           C  
+ATOM   5701  O   ARG A 445      11.911  47.304  -5.050  1.00 16.93           O  
+ATOM   5702  CB  ARG A 445      14.954  46.596  -4.019  1.00 19.45           C  
+ATOM   5703  CG  ARG A 445      14.889  45.888  -5.367  1.00 20.30           C  
+ATOM   5704  CD  ARG A 445      15.092  46.853  -6.539  1.00 23.45           C  
+ATOM   5705  NE  ARG A 445      15.088  46.143  -7.816  1.00 24.77           N  
+ATOM   5706  CZ  ARG A 445      15.141  46.731  -9.003  1.00 30.94           C  
+ATOM   5707  NH1 ARG A 445      15.200  48.048  -9.119  1.00 31.61           N  
+ATOM   5708  NH2 ARG A 445      15.131  45.980 -10.102  1.00 26.43           N  
+ATOM   5709  H   ARG A 445      14.698  48.049  -2.046  1.00 22.27           H  
+ATOM   5710  HA  ARG A 445      14.116  48.359  -4.575  1.00 23.13           H  
+ATOM   5711  HB2 ARG A 445      15.847  46.959  -3.920  1.00 23.35           H  
+ATOM   5712  HB3 ARG A 445      14.787  45.933  -3.330  1.00 23.35           H  
+ATOM   5713  HG2 ARG A 445      15.585  45.214  -5.407  1.00 24.36           H  
+ATOM   5714  HG3 ARG A 445      14.018  45.471  -5.467  1.00 24.36           H  
+ATOM   5715  HD2 ARG A 445      14.372  47.504  -6.548  1.00 28.14           H  
+ATOM   5716  HD3 ARG A 445      15.945  47.303  -6.441  1.00 28.14           H  
+ATOM   5717  HE  ARG A 445      15.049  45.284  -7.796  1.00 29.73           H  
+ATOM   5718 HH11 ARG A 445      15.205  48.542  -8.415  1.00 37.93           H  
+ATOM   5719 HH12 ARG A 445      15.234  48.410  -9.898  1.00 37.93           H  
+ATOM   5720 HH21 ARG A 445      15.091  45.123 -10.037  1.00 31.71           H  
+ATOM   5721 HH22 ARG A 445      15.165  46.352 -10.877  1.00 31.71           H  
+ATOM   5722  N   MET A 446      11.998  46.614  -2.907  1.00 16.74           N  
+ATOM   5723  CA  MET A 446      10.619  46.134  -2.931  1.00 15.71           C  
+ATOM   5724  C   MET A 446       9.647  47.262  -3.230  1.00 18.09           C  
+ATOM   5725  O   MET A 446       8.677  47.081  -3.975  1.00 15.12           O  
+ATOM   5726  CB  MET A 446      10.271  45.479  -1.594  1.00 16.57           C  
+ATOM   5727  CG  MET A 446      10.963  44.182  -1.411  1.00 17.80           C  
+ATOM   5728  SD  MET A 446      10.683  43.514   0.230  1.00 21.51           S  
+ATOM   5729  CE  MET A 446       8.905  43.334   0.231  1.00 23.26           C  
+ATOM   5730  H   MET A 446      12.409  46.486  -2.162  1.00 20.09           H  
+ATOM   5731  HA  MET A 446      10.541  45.462  -3.626  1.00 18.85           H  
+ATOM   5732  HB2 MET A 446      10.537  46.069  -0.872  1.00 19.88           H  
+ATOM   5733  HB3 MET A 446       9.315  45.320  -1.557  1.00 19.88           H  
+ATOM   5734  HG2 MET A 446      10.628  43.545  -2.061  1.00 21.36           H  
+ATOM   5735  HG3 MET A 446      11.917  44.308  -1.531  1.00 21.36           H  
+ATOM   5736  HE1 MET A 446       8.636  42.854   1.030  1.00 27.91           H  
+ATOM   5737  HE2 MET A 446       8.498  44.214   0.222  1.00 27.91           H  
+ATOM   5738  HE3 MET A 446       8.637  42.838  -0.559  1.00 27.91           H  
+ATOM   5739  N   LYS A 447       9.873  48.436  -2.636  1.00 16.33           N  
+ATOM   5740  CA  LYS A 447       8.977  49.557  -2.863  1.00 14.94           C  
+ATOM   5741  C   LYS A 447       9.031  50.031  -4.312  1.00 14.87           C  
+ATOM   5742  O   LYS A 447       7.992  50.339  -4.905  1.00 16.50           O  
+ATOM   5743  CB  LYS A 447       9.334  50.687  -1.898  1.00 17.76           C  
+ATOM   5744  CG  LYS A 447       9.065  50.344  -0.439  1.00 18.52           C  
+ATOM   5745  CD  LYS A 447       9.542  51.454   0.503  1.00 21.38           C  
+ATOM   5746  CE  LYS A 447       9.160  51.122   1.937  1.00 27.80           C  
+ATOM   5747  NZ  LYS A 447       9.862  51.997   2.925  1.00 36.74           N  
+ATOM   5748  H   LYS A 447      10.530  48.601  -2.105  1.00 19.60           H  
+ATOM   5749  HA  LYS A 447       8.064  49.283  -2.686  1.00 17.93           H  
+ATOM   5750  HB2 LYS A 447      10.278  50.889  -1.987  1.00 21.31           H  
+ATOM   5751  HB3 LYS A 447       8.805  51.469  -2.122  1.00 21.31           H  
+ATOM   5752  HG2 LYS A 447       8.111  50.224  -0.309  1.00 22.22           H  
+ATOM   5753  HG3 LYS A 447       9.537  49.528  -0.210  1.00 22.22           H  
+ATOM   5754  HD2 LYS A 447      10.507  51.535   0.450  1.00 25.65           H  
+ATOM   5755  HD3 LYS A 447       9.124  52.294   0.257  1.00 25.65           H  
+ATOM   5756  HE2 LYS A 447       8.204  51.247   2.049  1.00 33.36           H  
+ATOM   5757  HE3 LYS A 447       9.399  50.201   2.125  1.00 33.36           H  
+ATOM   5758  HZ1 LYS A 447       9.611  51.784   3.752  1.00 44.08           H  
+ATOM   5759  HZ2 LYS A 447      10.743  51.890   2.854  1.00 44.08           H  
+ATOM   5760  HZ3 LYS A 447       9.661  52.850   2.773  1.00 44.08           H  
+ATOM   5761  N   LYS A 448      10.220  50.081  -4.899  1.00 15.96           N  
+ATOM   5762  CA  LYS A 448      10.322  50.480  -6.298  1.00 16.72           C  
+ATOM   5763  C   LYS A 448       9.638  49.463  -7.202  1.00 16.36           C  
+ATOM   5764  O   LYS A 448       8.853  49.834  -8.082  1.00 17.72           O  
+ATOM   5765  CB  LYS A 448      11.780  50.664  -6.707  1.00 17.67           C  
+ATOM   5766  CG  LYS A 448      11.941  50.992  -8.190  1.00 25.72           C  
+ATOM   5767  CD  LYS A 448      13.357  51.352  -8.553  1.00 39.56           C  
+ATOM   5768  CE  LYS A 448      13.419  51.847 -10.000  1.00 49.57           C  
+ATOM   5769  NZ  LYS A 448      14.820  52.029 -10.468  1.00 65.85           N  
+ATOM   5770  H   LYS A 448      10.968  49.893  -4.519  1.00 19.15           H  
+ATOM   5771  HA  LYS A 448       9.881  51.338  -6.405  1.00 20.07           H  
+ATOM   5772  HB2 LYS A 448      12.161  51.394  -6.194  1.00 21.20           H  
+ATOM   5773  HB3 LYS A 448      12.264  49.844  -6.526  1.00 21.20           H  
+ATOM   5774  HG2 LYS A 448      11.684  50.218  -8.715  1.00 30.87           H  
+ATOM   5775  HG3 LYS A 448      11.373  51.747  -8.411  1.00 30.87           H  
+ATOM   5776  HD2 LYS A 448      13.675  52.058  -7.969  1.00 47.47           H  
+ATOM   5777  HD3 LYS A 448      13.925  50.570  -8.468  1.00 47.47           H  
+ATOM   5778  HE2 LYS A 448      12.988  51.199 -10.578  1.00 59.49           H  
+ATOM   5779  HE3 LYS A 448      12.965  52.702 -10.064  1.00 59.49           H  
+ATOM   5780  HZ1 LYS A 448      14.825  52.317 -11.310  1.00 79.03           H  
+ATOM   5781  HZ2 LYS A 448      15.237  52.625  -9.956  1.00 79.03           H  
+ATOM   5782  HZ3 LYS A 448      15.258  51.255 -10.426  1.00 79.03           H  
+ATOM   5783  N   LEU A 449       9.912  48.173  -6.981  1.00 15.02           N  
+ATOM   5784  CA  LEU A 449       9.280  47.138  -7.806  1.00 15.01           C  
+ATOM   5785  C   LEU A 449       7.768  47.179  -7.679  1.00 14.23           C  
+ATOM   5786  O   LEU A 449       7.042  47.005  -8.669  1.00 13.71           O  
+ATOM   5787  CB  LEU A 449       9.809  45.760  -7.422  1.00 14.45           C  
+ATOM   5788  CG  LEU A 449      11.248  45.461  -7.817  1.00 15.79           C  
+ATOM   5789  CD1 LEU A 449      11.699  44.189  -7.110  1.00 16.99           C  
+ATOM   5790  CD2 LEU A 449      11.423  45.287  -9.323  1.00 18.76           C  
+ATOM   5791  H   LEU A 449      10.447  47.878  -6.376  1.00 18.02           H  
+ATOM   5792  HA  LEU A 449       9.511  47.299  -8.734  1.00 18.01           H  
+ATOM   5793  HB2 LEU A 449       9.752  45.673  -6.457  1.00 17.34           H  
+ATOM   5794  HB3 LEU A 449       9.250  45.092  -7.849  1.00 17.34           H  
+ATOM   5795  HG  LEU A 449      11.797  46.216  -7.554  1.00 18.95           H  
+ATOM   5796 HD11 LEU A 449      12.614  43.993  -7.365  1.00 20.39           H  
+ATOM   5797 HD12 LEU A 449      11.645  44.325  -6.151  1.00 20.39           H  
+ATOM   5798 HD13 LEU A 449      11.118  43.458  -7.374  1.00 20.39           H  
+ATOM   5799 HD21 LEU A 449      12.347  45.061  -9.510  1.00 22.51           H  
+ATOM   5800 HD22 LEU A 449      10.840  44.575  -9.628  1.00 22.51           H  
+ATOM   5801 HD23 LEU A 449      11.189  46.118  -9.766  1.00 22.51           H  
+ATOM   5802  N   PHE A 450       7.264  47.380  -6.467  1.00 14.32           N  
+ATOM   5803  CA  PHE A 450       5.826  47.441  -6.297  1.00 12.20           C  
+ATOM   5804  C   PHE A 450       5.235  48.581  -7.124  1.00 13.67           C  
+ATOM   5805  O   PHE A 450       4.201  48.423  -7.782  1.00 13.75           O  
+ATOM   5806  CB  PHE A 450       5.461  47.603  -4.823  1.00 14.66           C  
+ATOM   5807  CG  PHE A 450       3.986  47.754  -4.611  1.00 13.28           C  
+ATOM   5808  CD1 PHE A 450       3.142  46.647  -4.654  1.00 14.30           C  
+ATOM   5809  CD2 PHE A 450       3.431  49.007  -4.434  1.00 14.87           C  
+ATOM   5810  CE1 PHE A 450       1.776  46.804  -4.489  1.00 14.82           C  
+ATOM   5811  CE2 PHE A 450       2.079  49.157  -4.278  1.00 13.15           C  
+ATOM   5812  CZ  PHE A 450       1.249  48.069  -4.320  1.00 15.53           C  
+ATOM   5813  H   PHE A 450       7.724  47.482  -5.747  1.00 17.18           H  
+ATOM   5814  HA  PHE A 450       5.441  46.604  -6.601  1.00 14.64           H  
+ATOM   5815  HB2 PHE A 450       5.756  46.818  -4.335  1.00 17.59           H  
+ATOM   5816  HB3 PHE A 450       5.899  48.394  -4.473  1.00 17.59           H  
+ATOM   5817  HD1 PHE A 450       3.497  45.799  -4.794  1.00 17.16           H  
+ATOM   5818  HD2 PHE A 450       3.982  49.756  -4.420  1.00 17.84           H  
+ATOM   5819  HE1 PHE A 450       1.217  46.061  -4.492  1.00 17.78           H  
+ATOM   5820  HE2 PHE A 450       1.722  50.005  -4.142  1.00 15.78           H  
+ATOM   5821  HZ  PHE A 450       0.330  48.182  -4.235  1.00 18.63           H  
+ATOM   5822  N   GLY A 451       5.877  49.748  -7.102  1.00 14.60           N  
+ATOM   5823  CA  GLY A 451       5.401  50.838  -7.935  1.00 17.62           C  
+ATOM   5824  C   GLY A 451       5.389  50.480  -9.411  1.00 15.69           C  
+ATOM   5825  O   GLY A 451       4.442  50.806 -10.138  1.00 16.44           O  
+ATOM   5826  H   GLY A 451       6.571  49.926  -6.626  1.00 17.52           H  
+ATOM   5827  HA2 GLY A 451       4.498  51.073  -7.671  1.00 21.15           H  
+ATOM   5828  HA3 GLY A 451       5.977  51.610  -7.813  1.00 21.15           H  
+ATOM   5829  N   GLU A 452       6.439  49.813  -9.871  1.00 15.34           N  
+ATOM   5830  CA  GLU A 452       6.542  49.442 -11.279  1.00 14.54           C  
+ATOM   5831  C   GLU A 452       5.479  48.442 -11.697  1.00 17.11           C  
+ATOM   5832  O   GLU A 452       5.149  48.390 -12.882  1.00 15.63           O  
+ATOM   5833  CB  GLU A 452       7.943  48.909 -11.561  1.00 16.59           C  
+ATOM   5834  CG  GLU A 452       9.005  50.008 -11.467  1.00 17.12           C  
+ATOM   5835  CD  GLU A 452       8.726  51.170 -12.417  1.00 31.94           C  
+ATOM   5836  OE1 GLU A 452       8.824  50.968 -13.637  1.00 31.61           O  
+ATOM   5837  OE2 GLU A 452       8.372  52.273 -11.947  1.00 40.68           O  
+ATOM   5838  H   GLU A 452       7.107  49.562  -9.391  1.00 18.41           H  
+ATOM   5839  HA  GLU A 452       6.410  50.229 -11.831  1.00 17.45           H  
+ATOM   5840  HB2 GLU A 452       8.159  48.222 -10.911  1.00 19.90           H  
+ATOM   5841  HB3 GLU A 452       7.969  48.538 -12.457  1.00 19.90           H  
+ATOM   5842  HG2 GLU A 452       9.022  50.357 -10.561  1.00 20.55           H  
+ATOM   5843  HG3 GLU A 452       9.871  49.634 -11.694  1.00 20.55           H  
+ATOM   5844  N   LEU A 453       4.895  47.687 -10.759  1.00 14.30           N  
+ATOM   5845  CA  LEU A 453       3.782  46.815 -11.128  1.00 14.59           C  
+ATOM   5846  C   LEU A 453       2.615  47.585 -11.711  1.00 15.80           C  
+ATOM   5847  O   LEU A 453       1.779  46.993 -12.405  1.00 13.52           O  
+ATOM   5848  CB  LEU A 453       3.262  46.030  -9.919  1.00 11.61           C  
+ATOM   5849  CG  LEU A 453       4.229  45.057  -9.283  1.00 13.25           C  
+ATOM   5850  CD1 LEU A 453       3.628  44.542  -7.962  1.00 16.93           C  
+ATOM   5851  CD2 LEU A 453       4.547  43.899 -10.220  1.00 16.53           C  
+ATOM   5852  H   LEU A 453       5.118  47.664  -9.929  1.00 17.16           H  
+ATOM   5853  HA  LEU A 453       4.123  46.188 -11.784  1.00 17.51           H  
+ATOM   5854  HB2 LEU A 453       3.006  46.667  -9.234  1.00 13.93           H  
+ATOM   5855  HB3 LEU A 453       2.488  45.519 -10.203  1.00 13.93           H  
+ATOM   5856  HG  LEU A 453       5.068  45.507  -9.099  1.00 15.90           H  
+ATOM   5857 HD11 LEU A 453       4.253  43.927  -7.548  1.00 20.32           H  
+ATOM   5858 HD12 LEU A 453       3.467  45.296  -7.373  1.00 20.32           H  
+ATOM   5859 HD13 LEU A 453       2.792  44.087  -8.151  1.00 20.32           H  
+ATOM   5860 HD21 LEU A 453       5.117  43.265  -9.756  1.00 19.84           H  
+ATOM   5861 HD22 LEU A 453       3.719  43.468 -10.482  1.00 19.84           H  
+ATOM   5862 HD23 LEU A 453       5.004  44.243 -11.003  1.00 19.84           H  
+ATOM   5863  N   ASN A 454       2.519  48.883 -11.403  1.00 15.23           N  
+ATOM   5864  CA  ASN A 454       1.453  49.742 -11.875  1.00 13.40           C  
+ATOM   5865  C   ASN A 454       1.896  50.668 -13.001  1.00 13.81           C  
+ATOM   5866  O   ASN A 454       1.161  51.597 -13.338  1.00 18.83           O  
+ATOM   5867  CB  ASN A 454       0.916  50.569 -10.724  1.00 12.66           C  
+ATOM   5868  CG  ASN A 454      -0.477  51.072 -10.966  1.00 17.29           C  
+ATOM   5869  OD1 ASN A 454      -1.305  50.389 -11.560  1.00 17.23           O  
+ATOM   5870  ND2 ASN A 454      -0.748  52.299 -10.502  1.00 19.11           N  
+ATOM   5871  H   ASN A 454       3.084  49.295 -10.903  1.00 18.27           H  
+ATOM   5872  HA  ASN A 454       0.738  49.182 -12.216  1.00 16.08           H  
+ATOM   5873  HB2 ASN A 454       0.902  50.023  -9.923  1.00 15.20           H  
+ATOM   5874  HB3 ASN A 454       1.493  51.338 -10.592  1.00 15.20           H  
+ATOM   5875 HD21 ASN A 454      -1.531  52.637 -10.613  1.00 22.93           H  
+ATOM   5876 HD22 ASN A 454      -0.139  52.748 -10.094  1.00 22.93           H  
+ATOM   5877  N   ASN A 455       3.068  50.435 -13.580  1.00 14.59           N  
+ATOM   5878  CA  ASN A 455       3.603  51.272 -14.661  1.00 14.17           C  
+ATOM   5879  C   ASN A 455       3.125  50.732 -16.006  1.00 13.61           C  
+ATOM   5880  O   ASN A 455       3.671  49.754 -16.530  1.00 15.86           O  
+ATOM   5881  CB  ASN A 455       5.123  51.312 -14.598  1.00 16.40           C  
+ATOM   5882  CG  ASN A 455       5.726  52.302 -15.579  1.00 18.95           C  
+ATOM   5883  OD1 ASN A 455       5.038  52.837 -16.450  1.00 19.64           O  
+ATOM   5884  ND2 ASN A 455       7.021  52.537 -15.443  1.00 19.09           N  
+ATOM   5885  H   ASN A 455       3.588  49.785 -13.363  1.00 17.50           H  
+ATOM   5886  HA  ASN A 455       3.253  52.171 -14.559  1.00 17.00           H  
+ATOM   5887  HB2 ASN A 455       5.395  51.572 -13.704  1.00 19.69           H  
+ATOM   5888  HB3 ASN A 455       5.471  50.431 -14.808  1.00 19.69           H  
+ATOM   5889 HD21 ASN A 455       7.415  53.089 -15.972  1.00 22.90           H  
+ATOM   5890 HD22 ASN A 455       7.468  52.138 -14.826  1.00 22.90           H  
+ATOM   5891  N   GLU A 456       2.134  51.414 -16.587  1.00 16.27           N  
+ATOM   5892  CA  GLU A 456       1.522  50.990 -17.836  1.00 16.76           C  
+ATOM   5893  C   GLU A 456       2.413  51.257 -19.036  1.00 17.56           C  
+ATOM   5894  O   GLU A 456       2.080  50.811 -20.137  1.00 18.21           O  
+ATOM   5895  CB  GLU A 456       0.156  51.678 -17.985  1.00 17.18           C  
+ATOM   5896  CG  GLU A 456      -0.814  51.215 -16.907  1.00 18.57           C  
+ATOM   5897  CD  GLU A 456      -2.181  51.856 -16.956  1.00 23.26           C  
+ATOM   5898  OE1 GLU A 456      -2.410  52.769 -17.779  1.00 26.06           O  
+ATOM   5899  OE2 GLU A 456      -3.039  51.432 -16.161  1.00 25.73           O  
+ATOM   5900  H   GLU A 456       1.796  52.137 -16.268  1.00 19.52           H  
+ATOM   5901  HA  GLU A 456       1.361  50.034 -17.820  1.00 20.11           H  
+ATOM   5902  HB2 GLU A 456       0.269  52.638 -17.904  1.00 20.61           H  
+ATOM   5903  HB3 GLU A 456      -0.221  51.461 -18.852  1.00 20.61           H  
+ATOM   5904  HG2 GLU A 456      -0.939  50.258 -16.999  1.00 22.29           H  
+ATOM   5905  HG3 GLU A 456      -0.430  51.418 -16.040  1.00 22.29           H  
+ATOM   5906  N   ALA A 457       3.543  51.923 -18.852  1.00 17.21           N  
+ATOM   5907  CA  ALA A 457       4.490  52.151 -19.935  1.00 18.70           C  
+ATOM   5908  C   ALA A 457       5.462  51.001 -20.146  1.00 17.72           C  
+ATOM   5909  O   ALA A 457       6.126  50.944 -21.197  1.00 19.92           O  
+ATOM   5910  CB  ALA A 457       5.288  53.436 -19.667  1.00 19.83           C  
+ATOM   5911  H   ALA A 457       3.788  52.258 -18.099  1.00 20.66           H  
+ATOM   5912  HA  ALA A 457       3.990  52.265 -20.758  1.00 22.44           H  
+ATOM   5913  HB1 ALA A 457       5.916  53.574 -20.393  1.00 23.80           H  
+ATOM   5914  HB2 ALA A 457       4.673  54.184 -19.615  1.00 23.80           H  
+ATOM   5915  HB3 ALA A 457       5.766  53.342 -18.829  1.00 23.80           H  
+ATOM   5916  N   LEU A 458       5.556  50.071 -19.198  1.00 16.60           N  
+ATOM   5917  CA  LEU A 458       6.513  48.990 -19.341  1.00 16.71           C  
+ATOM   5918  C   LEU A 458       6.117  48.052 -20.470  1.00 12.95           C  
+ATOM   5919  O   LEU A 458       4.934  47.758 -20.681  1.00 15.35           O  
+ATOM   5920  CB  LEU A 458       6.628  48.203 -18.036  1.00 16.00           C  
+ATOM   5921  CG  LEU A 458       7.127  49.006 -16.843  1.00 16.67           C  
+ATOM   5922  CD1 LEU A 458       7.224  48.108 -15.622  1.00 17.32           C  
+ATOM   5923  CD2 LEU A 458       8.450  49.660 -17.125  1.00 18.89           C  
+ATOM   5924  H   LEU A 458       5.085  50.047 -18.480  1.00 19.92           H  
+ATOM   5925  HA  LEU A 458       7.380  49.369 -19.552  1.00 20.05           H  
+ATOM   5926  HB2 LEU A 458       5.751  47.857 -17.809  1.00 19.20           H  
+ATOM   5927  HB3 LEU A 458       7.248  47.470 -18.174  1.00 19.20           H  
+ATOM   5928  HG  LEU A 458       6.493  49.718 -16.662  1.00 20.01           H  
+ATOM   5929 HD11 LEU A 458       7.534  48.633 -14.868  1.00 20.78           H  
+ATOM   5930 HD12 LEU A 458       6.348  47.739 -15.431  1.00 20.78           H  
+ATOM   5931 HD13 LEU A 458       7.852  47.392 -15.807  1.00 20.78           H  
+ATOM   5932 HD21 LEU A 458       8.817  50.000 -16.294  1.00 22.67           H  
+ATOM   5933 HD22 LEU A 458       9.051  49.002 -17.508  1.00 22.67           H  
+ATOM   5934 HD23 LEU A 458       8.315  50.389 -17.750  1.00 22.67           H  
+ATOM   5935  N   SER A 459       7.131  47.560 -21.167  1.00 14.85           N  
+ATOM   5936  CA  SER A 459       6.998  46.501 -22.151  1.00 15.08           C  
+ATOM   5937  C   SER A 459       6.647  45.176 -21.468  1.00 15.04           C  
+ATOM   5938  O   SER A 459       6.753  45.023 -20.246  1.00 15.92           O  
+ATOM   5939  CB  SER A 459       8.296  46.323 -22.923  1.00 18.27           C  
+ATOM   5940  OG  SER A 459       9.331  45.839 -22.083  1.00 17.50           O  
+ATOM   5941  H   SER A 459       7.942  47.835 -21.084  1.00 17.82           H  
+ATOM   5942  HA  SER A 459       6.289  46.741 -22.768  1.00 18.10           H  
+ATOM   5943  HB2 SER A 459       8.150  45.687 -23.641  1.00 21.92           H  
+ATOM   5944  HB3 SER A 459       8.564  47.181 -23.290  1.00 21.92           H  
+ATOM   5945  HG  SER A 459      10.040  45.749 -22.524  1.00 21.00           H  
+ATOM   5946  N   ILE A 460       6.269  44.198 -22.294  1.00 14.04           N  
+ATOM   5947  CA  ILE A 460       6.054  42.846 -21.775  1.00 15.41           C  
+ATOM   5948  C   ILE A 460       7.270  42.365 -20.989  1.00 17.28           C  
+ATOM   5949  O   ILE A 460       7.145  41.860 -19.862  1.00 13.92           O  
+ATOM   5950  CB  ILE A 460       5.712  41.870 -22.913  1.00 15.77           C  
+ATOM   5951  CG1 ILE A 460       4.285  42.109 -23.379  1.00 16.97           C  
+ATOM   5952  CG2 ILE A 460       5.938  40.433 -22.428  1.00 20.28           C  
+ATOM   5953  CD1 ILE A 460       3.893  41.207 -24.532  1.00 22.40           C  
+ATOM   5954  H   ILE A 460       6.134  44.288 -23.138  1.00 16.85           H  
+ATOM   5955  HA  ILE A 460       5.298  42.881 -21.168  1.00 18.49           H  
+ATOM   5956  HB  ILE A 460       6.292  42.020 -23.675  1.00 18.93           H  
+ATOM   5957 HG12 ILE A 460       3.678  41.939 -22.643  1.00 20.37           H  
+ATOM   5958 HG13 ILE A 460       4.199  43.029 -23.674  1.00 20.37           H  
+ATOM   5959 HG21 ILE A 460       5.507  39.820 -23.044  1.00 24.33           H  
+ATOM   5960 HG22 ILE A 460       6.892  40.256 -22.399  1.00 24.33           H  
+ATOM   5961 HG23 ILE A 460       5.557  40.335 -21.542  1.00 24.33           H  
+ATOM   5962 HD11 ILE A 460       3.068  41.534 -24.923  1.00 26.87           H  
+ATOM   5963 HD12 ILE A 460       4.600  41.217 -25.196  1.00 26.87           H  
+ATOM   5964 HD13 ILE A 460       3.766  40.305 -24.198  1.00 26.87           H  
+ATOM   5965  N   GLU A 461       8.466  42.500 -21.570  1.00 15.29           N  
+ATOM   5966  CA  GLU A 461       9.658  41.988 -20.896  1.00 13.60           C  
+ATOM   5967  C   GLU A 461       9.912  42.728 -19.589  1.00 14.02           C  
+ATOM   5968  O   GLU A 461      10.282  42.116 -18.576  1.00 14.72           O  
+ATOM   5969  CB  GLU A 461      10.882  42.082 -21.814  1.00 17.00           C  
+ATOM   5970  CG  GLU A 461      12.120  41.412 -21.254  1.00 23.48           C  
+ATOM   5971  CD  GLU A 461      13.384  41.733 -22.047  1.00 38.53           C  
+ATOM   5972  OE1 GLU A 461      13.385  42.719 -22.816  1.00 40.18           O  
+ATOM   5973  OE2 GLU A 461      14.379  40.998 -21.885  1.00 47.82           O  
+ATOM   5974  H   GLU A 461       8.610  42.872 -22.332  1.00 18.35           H  
+ATOM   5975  HA  GLU A 461       9.515  41.051 -20.693  1.00 16.31           H  
+ATOM   5976  HB2 GLU A 461      10.671  41.655 -22.659  1.00 20.40           H  
+ATOM   5977  HB3 GLU A 461      11.091  43.018 -21.959  1.00 20.40           H  
+ATOM   5978  HG2 GLU A 461      12.256  41.713 -20.342  1.00 28.18           H  
+ATOM   5979  HG3 GLU A 461      11.993  40.451 -21.272  1.00 28.18           H  
+ATOM   5980  N   GLU A 462       9.736  44.044 -19.595  1.00 13.38           N  
+ATOM   5981  CA  GLU A 462       9.995  44.827 -18.395  1.00 13.11           C  
+ATOM   5982  C   GLU A 462       8.991  44.499 -17.304  1.00 13.48           C  
+ATOM   5983  O   GLU A 462       9.360  44.408 -16.125  1.00 14.84           O  
+ATOM   5984  CB  GLU A 462       9.960  46.315 -18.732  1.00 17.57           C  
+ATOM   5985  CG  GLU A 462      11.147  46.769 -19.570  1.00 18.06           C  
+ATOM   5986  CD  GLU A 462      10.934  48.121 -20.240  1.00 21.64           C  
+ATOM   5987  OE1 GLU A 462       9.794  48.640 -20.275  1.00 19.14           O  
+ATOM   5988  OE2 GLU A 462      11.933  48.676 -20.751  1.00 28.92           O  
+ATOM   5989  H   GLU A 462       9.471  44.503 -20.272  1.00 16.05           H  
+ATOM   5990  HA  GLU A 462      10.880  44.615 -18.060  1.00 15.73           H  
+ATOM   5991  HB2 GLU A 462       9.151  46.504 -19.233  1.00 21.08           H  
+ATOM   5992  HB3 GLU A 462       9.966  46.824 -17.906  1.00 21.08           H  
+ATOM   5993  HG2 GLU A 462      11.926  46.842 -18.997  1.00 21.67           H  
+ATOM   5994  HG3 GLU A 462      11.307  46.114 -20.267  1.00 21.67           H  
+ATOM   5995  N   LEU A 463       7.716  44.339 -17.671  1.00 14.10           N  
+ATOM   5996  CA  LEU A 463       6.698  44.019 -16.672  1.00 12.50           C  
+ATOM   5997  C   LEU A 463       6.915  42.615 -16.123  1.00 12.30           C  
+ATOM   5998  O   LEU A 463       6.791  42.396 -14.918  1.00 12.40           O  
+ATOM   5999  CB  LEU A 463       5.296  44.162 -17.276  1.00 13.46           C  
+ATOM   6000  CG  LEU A 463       4.128  44.011 -16.301  1.00 12.46           C  
+ATOM   6001  CD1 LEU A 463       4.228  45.018 -15.184  1.00 14.02           C  
+ATOM   6002  CD2 LEU A 463       2.815  44.160 -17.045  1.00 13.14           C  
+ATOM   6003  H   LEU A 463       7.422  44.410 -18.476  1.00 16.92           H  
+ATOM   6004  HA  LEU A 463       6.761  44.649 -15.937  1.00 15.00           H  
+ATOM   6005  HB2 LEU A 463       5.226  45.044 -17.673  1.00 16.16           H  
+ATOM   6006  HB3 LEU A 463       5.189  43.481 -17.959  1.00 16.16           H  
+ATOM   6007  HG  LEU A 463       4.156  43.128 -15.900  1.00 14.96           H  
+ATOM   6008 HD11 LEU A 463       3.398  45.015 -14.681  1.00 16.83           H  
+ATOM   6009 HD12 LEU A 463       4.966  44.774 -14.604  1.00 16.83           H  
+ATOM   6010 HD13 LEU A 463       4.381  45.897 -15.563  1.00 16.83           H  
+ATOM   6011 HD21 LEU A 463       2.083  44.059 -16.417  1.00 15.77           H  
+ATOM   6012 HD22 LEU A 463       2.782  45.039 -17.453  1.00 15.77           H  
+ATOM   6013 HD23 LEU A 463       2.761  43.475 -17.730  1.00 15.77           H  
+ATOM   6014  N   ILE A 464       7.256  41.653 -16.979  1.00 13.19           N  
+ATOM   6015  CA  ILE A 464       7.536  40.304 -16.485  1.00 13.37           C  
+ATOM   6016  C   ILE A 464       8.711  40.325 -15.517  1.00 14.87           C  
+ATOM   6017  O   ILE A 464       8.665  39.713 -14.438  1.00 13.73           O  
+ATOM   6018  CB  ILE A 464       7.792  39.336 -17.653  1.00 12.84           C  
+ATOM   6019  CG1 ILE A 464       6.485  39.014 -18.370  1.00 12.10           C  
+ATOM   6020  CG2 ILE A 464       8.435  38.049 -17.155  1.00 11.83           C  
+ATOM   6021  CD1 ILE A 464       6.655  38.279 -19.678  1.00 13.84           C  
+ATOM   6022  H   ILE A 464       7.331  41.751 -17.830  1.00 15.83           H  
+ATOM   6023  HA  ILE A 464       6.754  39.992 -16.005  1.00 16.05           H  
+ATOM   6024  HB  ILE A 464       8.398  39.770 -18.274  1.00 15.40           H  
+ATOM   6025 HG12 ILE A 464       5.943  38.458 -17.789  1.00 14.52           H  
+ATOM   6026 HG13 ILE A 464       6.023  39.846 -18.559  1.00 14.52           H  
+ATOM   6027 HG21 ILE A 464       8.373  37.375 -17.850  1.00 14.20           H  
+ATOM   6028 HG22 ILE A 464       9.366  38.222 -16.944  1.00 14.20           H  
+ATOM   6029 HG23 ILE A 464       7.966  37.749 -16.361  1.00 14.20           H  
+ATOM   6030 HD11 ILE A 464       5.824  38.327 -20.177  1.00 16.61           H  
+ATOM   6031 HD12 ILE A 464       7.369  38.696 -20.184  1.00 16.61           H  
+ATOM   6032 HD13 ILE A 464       6.877  37.353 -19.493  1.00 16.61           H  
+ATOM   6033  N   ASN A 465       9.786  41.034 -15.882  1.00 11.94           N  
+ATOM   6034  CA  ASN A 465      10.965  41.038 -15.024  1.00 13.73           C  
+ATOM   6035  C   ASN A 465      10.668  41.698 -13.687  1.00 15.11           C  
+ATOM   6036  O   ASN A 465      11.199  41.261 -12.656  1.00 15.41           O  
+ATOM   6037  CB  ASN A 465      12.132  41.713 -15.755  1.00 15.23           C  
+ATOM   6038  CG  ASN A 465      12.721  40.830 -16.851  1.00 18.21           C  
+ATOM   6039  OD1 ASN A 465      12.559  39.609 -16.844  1.00 23.13           O  
+ATOM   6040  ND2 ASN A 465      13.421  41.447 -17.792  1.00 23.14           N  
+ATOM   6041  H   ASN A 465       9.852  41.504 -16.599  1.00 14.33           H  
+ATOM   6042  HA  ASN A 465      11.241  40.128 -14.834  1.00 16.48           H  
+ATOM   6043  HB2 ASN A 465      11.817  42.534 -16.166  1.00 18.28           H  
+ATOM   6044  HB3 ASN A 465      12.836  41.911 -15.117  1.00 18.28           H  
+ATOM   6045 HD21 ASN A 465      13.774  40.994 -18.433  1.00 27.77           H  
+ATOM   6046 HD22 ASN A 465      13.522  42.301 -17.762  1.00 27.77           H  
+ATOM   6047  N   THR A 466       9.796  42.709 -13.676  1.00 12.80           N  
+ATOM   6048  CA  THR A 466       9.359  43.335 -12.424  1.00 12.78           C  
+ATOM   6049  C   THR A 466       8.635  42.326 -11.545  1.00 13.39           C  
+ATOM   6050  O   THR A 466       8.966  42.158 -10.362  1.00 13.75           O  
+ATOM   6051  CB  THR A 466       8.447  44.532 -12.731  1.00 13.85           C  
+ATOM   6052  OG1 THR A 466       9.159  45.505 -13.523  1.00 15.69           O  
+ATOM   6053  CG2 THR A 466       7.952  45.217 -11.468  1.00 14.43           C  
+ATOM   6054  H   THR A 466       9.442  43.054 -14.380  1.00 15.36           H  
+ATOM   6055  HA  THR A 466      10.135  43.661 -11.942  1.00 15.33           H  
+ATOM   6056  HB  THR A 466       7.676  44.199 -13.216  1.00 16.62           H  
+ATOM   6057  HG1 THR A 466       9.424  45.154 -14.239  1.00 18.83           H  
+ATOM   6058 HG21 THR A 466       7.501  46.045 -11.695  1.00 17.31           H  
+ATOM   6059 HG22 THR A 466       7.332  44.639 -10.998  1.00 17.31           H  
+ATOM   6060 HG23 THR A 466       8.701  45.417 -10.884  1.00 17.31           H  
+ATOM   6061  N   ILE A 467       7.641  41.643 -12.114  1.00 12.31           N  
+ATOM   6062  CA  ILE A 467       6.885  40.639 -11.368  1.00 11.82           C  
+ATOM   6063  C   ILE A 467       7.813  39.556 -10.838  1.00 12.12           C  
+ATOM   6064  O   ILE A 467       7.744  39.191  -9.659  1.00 12.07           O  
+ATOM   6065  CB  ILE A 467       5.782  40.034 -12.252  1.00 11.43           C  
+ATOM   6066  CG1 ILE A 467       4.730  41.065 -12.663  1.00 11.67           C  
+ATOM   6067  CG2 ILE A 467       5.106  38.855 -11.538  1.00 10.47           C  
+ATOM   6068  CD1 ILE A 467       3.881  40.622 -13.885  1.00 13.87           C  
+ATOM   6069  H   ILE A 467       7.385  41.741 -12.929  1.00 14.78           H  
+ATOM   6070  HA  ILE A 467       6.467  41.076 -10.610  1.00 14.18           H  
+ATOM   6071  HB  ILE A 467       6.215  39.721 -13.061  1.00 13.71           H  
+ATOM   6072 HG12 ILE A 467       4.127  41.212 -11.918  1.00 14.00           H  
+ATOM   6073 HG13 ILE A 467       5.178  41.894 -12.896  1.00 14.00           H  
+ATOM   6074 HG21 ILE A 467       4.266  38.656 -11.981  1.00 12.56           H  
+ATOM   6075 HG22 ILE A 467       5.692  38.084 -11.578  1.00 12.56           H  
+ATOM   6076 HG23 ILE A 467       4.941  39.099 -10.613  1.00 12.56           H  
+ATOM   6077 HD11 ILE A 467       3.310  41.359 -14.157  1.00 16.65           H  
+ATOM   6078 HD12 ILE A 467       4.476  40.379 -14.612  1.00 16.65           H  
+ATOM   6079 HD13 ILE A 467       3.338  39.859 -13.633  1.00 16.65           H  
+ATOM   6080  N   ILE A 468       8.687  39.017 -11.693  1.00 13.71           N  
+ATOM   6081  CA  ILE A 468       9.521  37.886 -11.295  1.00 12.68           C  
+ATOM   6082  C   ILE A 468      10.458  38.299 -10.170  1.00 15.53           C  
+ATOM   6083  O   ILE A 468      10.596  37.589  -9.168  1.00 14.87           O  
+ATOM   6084  CB  ILE A 468      10.304  37.326 -12.500  1.00 15.49           C  
+ATOM   6085  CG1 ILE A 468       9.345  36.734 -13.533  1.00 20.85           C  
+ATOM   6086  CG2 ILE A 468      11.321  36.302 -12.025  1.00 19.39           C  
+ATOM   6087  CD1 ILE A 468       8.696  35.434 -13.125  1.00 22.99           C  
+ATOM   6088  H   ILE A 468       8.814  39.286 -12.500  1.00 16.45           H  
+ATOM   6089  HA  ILE A 468       8.940  37.181 -10.968  1.00 15.21           H  
+ATOM   6090  HB  ILE A 468      10.784  38.051 -12.931  1.00 18.59           H  
+ATOM   6091 HG12 ILE A 468       8.635  37.375 -13.697  1.00 25.02           H  
+ATOM   6092 HG13 ILE A 468       9.838  36.569 -14.352  1.00 25.02           H  
+ATOM   6093 HG21 ILE A 468      11.610  35.769 -12.782  1.00 23.27           H  
+ATOM   6094 HG22 ILE A 468      12.080  36.766 -11.638  1.00 23.27           H  
+ATOM   6095 HG23 ILE A 468      10.907  35.731 -11.358  1.00 23.27           H  
+ATOM   6096 HD11 ILE A 468       8.034  35.189 -13.790  1.00 27.59           H  
+ATOM   6097 HD12 ILE A 468       9.377  34.746 -13.065  1.00 27.59           H  
+ATOM   6098 HD13 ILE A 468       8.269  35.552 -12.262  1.00 27.59           H  
+ATOM   6099  N   GLU A 469      11.103  39.463 -10.304  1.00 12.24           N  
+ATOM   6100  CA  GLU A 469      12.043  39.873  -9.266  1.00 14.21           C  
+ATOM   6101  C   GLU A 469      11.316  40.090  -7.939  1.00 14.82           C  
+ATOM   6102  O   GLU A 469      11.836  39.733  -6.868  1.00 14.83           O  
+ATOM   6103  CB  GLU A 469      12.795  41.140  -9.676  1.00 14.38           C  
+ATOM   6104  CG  GLU A 469      13.873  41.508  -8.666  1.00 16.83           C  
+ATOM   6105  CD  GLU A 469      14.608  42.789  -8.979  1.00 23.76           C  
+ATOM   6106  OE1 GLU A 469      14.473  43.321 -10.107  1.00 20.63           O  
+ATOM   6107  OE2 GLU A 469      15.333  43.264  -8.079  1.00 22.69           O  
+ATOM   6108  H   GLU A 469      11.016  40.011 -10.961  1.00 14.69           H  
+ATOM   6109  HA  GLU A 469      12.703  39.171  -9.153  1.00 17.05           H  
+ATOM   6110  HB2 GLU A 469      13.220  40.995 -10.536  1.00 17.26           H  
+ATOM   6111  HB3 GLU A 469      12.169  41.878  -9.736  1.00 17.26           H  
+ATOM   6112  HG2 GLU A 469      13.459  41.613  -7.795  1.00 20.20           H  
+ATOM   6113  HG3 GLU A 469      14.528  40.793  -8.638  1.00 20.20           H  
+ATOM   6114  N   PHE A 470      10.134  40.706  -7.984  1.00 13.38           N  
+ATOM   6115  CA  PHE A 470       9.361  40.937  -6.763  1.00 13.16           C  
+ATOM   6116  C   PHE A 470       8.968  39.621  -6.104  1.00 14.74           C  
+ATOM   6117  O   PHE A 470       9.126  39.457  -4.889  1.00 14.58           O  
+ATOM   6118  CB  PHE A 470       8.132  41.777  -7.105  1.00 11.56           C  
+ATOM   6119  CG  PHE A 470       7.447  42.402  -5.923  1.00 13.29           C  
+ATOM   6120  CD1 PHE A 470       8.135  43.210  -5.023  1.00 17.13           C  
+ATOM   6121  CD2 PHE A 470       6.088  42.211  -5.733  1.00 14.65           C  
+ATOM   6122  CE1 PHE A 470       7.468  43.794  -3.946  1.00 18.13           C  
+ATOM   6123  CE2 PHE A 470       5.424  42.792  -4.665  1.00 17.38           C  
+ATOM   6124  CZ  PHE A 470       6.115  43.585  -3.774  1.00 16.46           C  
+ATOM   6125  H   PHE A 470       9.760  40.998  -8.702  1.00 16.06           H  
+ATOM   6126  HA  PHE A 470       9.898  41.428  -6.123  1.00 15.79           H  
+ATOM   6127  HB2 PHE A 470       8.405  42.495  -7.697  1.00 13.87           H  
+ATOM   6128  HB3 PHE A 470       7.484  41.209  -7.550  1.00 13.87           H  
+ATOM   6129  HD1 PHE A 470       9.045  43.360  -5.140  1.00 20.55           H  
+ATOM   6130  HD2 PHE A 470       5.612  41.684  -6.334  1.00 17.58           H  
+ATOM   6131  HE1 PHE A 470       7.936  44.326  -3.344  1.00 21.76           H  
+ATOM   6132  HE2 PHE A 470       4.512  42.648  -4.549  1.00 20.85           H  
+ATOM   6133  HZ  PHE A 470       5.670  43.978  -3.058  1.00 19.75           H  
+ATOM   6134  N   VAL A 471       8.483  38.661  -6.893  1.00 14.08           N  
+ATOM   6135  CA  VAL A 471       8.069  37.370  -6.342  1.00 13.03           C  
+ATOM   6136  C   VAL A 471       9.269  36.600  -5.799  1.00 15.75           C  
+ATOM   6137  O   VAL A 471       9.168  35.909  -4.773  1.00 15.38           O  
+ATOM   6138  CB  VAL A 471       7.304  36.571  -7.418  1.00 12.86           C  
+ATOM   6139  CG1 VAL A 471       7.057  35.132  -6.975  1.00 17.72           C  
+ATOM   6140  CG2 VAL A 471       5.994  37.289  -7.742  1.00 14.95           C  
+ATOM   6141  H   VAL A 471       8.383  38.730  -7.744  1.00 16.90           H  
+ATOM   6142  HA  VAL A 471       7.470  37.524  -5.594  1.00 15.64           H  
+ATOM   6143  HB  VAL A 471       7.842  36.523  -8.224  1.00 15.44           H  
+ATOM   6144 HG11 VAL A 471       6.414  34.723  -7.575  1.00 21.26           H  
+ATOM   6145 HG12 VAL A 471       7.894  34.644  -7.005  1.00 21.26           H  
+ATOM   6146 HG13 VAL A 471       6.708  35.136  -6.070  1.00 21.26           H  
+ATOM   6147 HG21 VAL A 471       5.527  36.796  -8.435  1.00 17.94           H  
+ATOM   6148 HG22 VAL A 471       5.449  37.329  -6.941  1.00 17.94           H  
+ATOM   6149 HG23 VAL A 471       6.194  38.186  -8.052  1.00 17.94           H  
+ATOM   6150  N   GLU A 472      10.428  36.711  -6.455  1.00 13.64           N  
+ATOM   6151  CA  GLU A 472      11.640  36.088  -5.922  1.00 16.80           C  
+ATOM   6152  C   GLU A 472      12.005  36.687  -4.562  1.00 15.07           C  
+ATOM   6153  O   GLU A 472      12.295  35.957  -3.609  1.00 17.07           O  
+ATOM   6154  CB  GLU A 472      12.786  36.233  -6.928  1.00 18.91           C  
+ATOM   6155  CG  GLU A 472      12.698  35.253  -8.108  1.00 21.23           C  
+ATOM   6156  CD  GLU A 472      13.854  35.362  -9.101  1.00 31.91           C  
+ATOM   6157  OE1 GLU A 472      14.449  36.451  -9.223  1.00 31.88           O  
+ATOM   6158  OE2 GLU A 472      14.155  34.353  -9.773  1.00 40.88           O  
+ATOM   6159  H   GLU A 472      10.537  37.134  -7.197  1.00 16.36           H  
+ATOM   6160  HA  GLU A 472      11.485  35.140  -5.792  1.00 20.16           H  
+ATOM   6161  HB2 GLU A 472      12.772  37.134  -7.289  1.00 22.69           H  
+ATOM   6162  HB3 GLU A 472      13.626  36.072  -6.470  1.00 22.69           H  
+ATOM   6163  HG2 GLU A 472      12.695  34.348  -7.759  1.00 25.48           H  
+ATOM   6164  HG3 GLU A 472      11.876  35.425  -8.593  1.00 25.48           H  
+ATOM   6165  N   ILE A 473      11.974  38.016  -4.441  1.00 14.29           N  
+ATOM   6166  CA  ILE A 473      12.273  38.621  -3.145  1.00 15.34           C  
+ATOM   6167  C   ILE A 473      11.307  38.104  -2.076  1.00 14.99           C  
+ATOM   6168  O   ILE A 473      11.717  37.752  -0.957  1.00 17.37           O  
+ATOM   6169  CB  ILE A 473      12.221  40.152  -3.259  1.00 13.70           C  
+ATOM   6170  CG1 ILE A 473      13.361  40.663  -4.126  1.00 17.01           C  
+ATOM   6171  CG2 ILE A 473      12.286  40.797  -1.866  1.00 15.89           C  
+ATOM   6172  CD1 ILE A 473      13.208  42.114  -4.518  1.00 17.38           C  
+ATOM   6173  H   ILE A 473      11.789  38.569  -5.073  1.00 17.15           H  
+ATOM   6174  HA  ILE A 473      13.170  38.364  -2.882  1.00 18.41           H  
+ATOM   6175  HB  ILE A 473      11.380  40.395  -3.678  1.00 16.43           H  
+ATOM   6176 HG12 ILE A 473      14.193  40.572  -3.635  1.00 20.41           H  
+ATOM   6177 HG13 ILE A 473      13.397  40.136  -4.940  1.00 20.41           H  
+ATOM   6178 HG21 ILE A 473      12.475  41.743  -1.964  1.00 19.07           H  
+ATOM   6179 HG22 ILE A 473      11.432  40.675  -1.421  1.00 19.07           H  
+ATOM   6180 HG23 ILE A 473      12.990  40.370  -1.353  1.00 19.07           H  
+ATOM   6181 HD11 ILE A 473      13.827  42.314  -5.238  1.00 20.86           H  
+ATOM   6182 HD12 ILE A 473      12.297  42.267  -4.813  1.00 20.86           H  
+ATOM   6183 HD13 ILE A 473      13.405  42.672  -3.749  1.00 20.86           H  
+ATOM   6184  N   LEU A 474      10.019  38.042  -2.398  1.00 13.55           N  
+ATOM   6185  CA  LEU A 474       9.007  37.635  -1.432  1.00 13.90           C  
+ATOM   6186  C   LEU A 474       9.118  36.170  -1.066  1.00 17.23           C  
+ATOM   6187  O   LEU A 474       8.568  35.751  -0.034  1.00 18.58           O  
+ATOM   6188  CB  LEU A 474       7.617  37.901  -1.985  1.00 15.42           C  
+ATOM   6189  CG  LEU A 474       7.245  39.357  -2.194  1.00 14.00           C  
+ATOM   6190  CD1 LEU A 474       5.931  39.470  -2.920  1.00 20.02           C  
+ATOM   6191  CD2 LEU A 474       7.191  40.082  -0.857  1.00 17.59           C  
+ATOM   6192  H   LEU A 474       9.703  38.232  -3.175  1.00 16.26           H  
+ATOM   6193  HA  LEU A 474       9.127  38.163  -0.628  1.00 16.67           H  
+ATOM   6194  HB2 LEU A 474       7.546  37.461  -2.847  1.00 18.50           H  
+ATOM   6195  HB3 LEU A 474       6.970  37.526  -1.367  1.00 18.50           H  
+ATOM   6196  HG  LEU A 474       7.921  39.785  -2.742  1.00 16.79           H  
+ATOM   6197 HD11 LEU A 474       5.616  40.386  -2.863  1.00 24.03           H  
+ATOM   6198 HD12 LEU A 474       6.061  39.223  -3.849  1.00 24.03           H  
+ATOM   6199 HD13 LEU A 474       5.288  38.873  -2.506  1.00 24.03           H  
+ATOM   6200 HD21 LEU A 474       6.818  40.967  -0.992  1.00 21.11           H  
+ATOM   6201 HD22 LEU A 474       6.632  39.577  -0.246  1.00 21.11           H  
+ATOM   6202 HD23 LEU A 474       8.091  40.153  -0.500  1.00 21.11           H  
+ATOM   6203  N   SER A 475       9.798  35.386  -1.884  1.00 16.44           N  
+ATOM   6204  CA  SER A 475       9.963  33.957  -1.655  1.00 15.85           C  
+ATOM   6205  C   SER A 475      11.260  33.656  -0.924  1.00 22.46           C  
+ATOM   6206  O   SER A 475      11.493  32.496  -0.562  1.00 21.88           O  
+ATOM   6207  CB  SER A 475       9.906  33.210  -2.989  1.00 16.17           C  
+ATOM   6208  OG  SER A 475       8.649  33.448  -3.608  1.00 16.83           O  
+ATOM   6209  H   SER A 475      10.185  35.664  -2.600  1.00 19.73           H  
+ATOM   6210  HA  SER A 475       9.233  33.618  -1.114  1.00 19.02           H  
+ATOM   6211  HB2 SER A 475      10.615  33.530  -3.567  1.00 19.41           H  
+ATOM   6212  HB3 SER A 475      10.011  32.259  -2.829  1.00 19.41           H  
+ATOM   6213  HG  SER A 475       8.537  34.273  -3.723  1.00 20.20           H  
+ATOM   6214  N   ASN A 476      12.066  34.683  -0.655  1.00 20.25           N  
+ATOM   6215  CA  ASN A 476      13.407  34.542  -0.105  1.00 22.34           C  
+ATOM   6216  C   ASN A 476      13.644  35.658   0.909  1.00 22.32           C  
+ATOM   6217  O   ASN A 476      14.659  36.361   0.848  1.00 31.65           O  
+ATOM   6218  CB  ASN A 476      14.452  34.579  -1.211  1.00 22.46           C  
+ATOM   6219  CG  ASN A 476      14.379  33.370  -2.108  1.00 23.30           C  
+ATOM   6220  OD1 ASN A 476      14.912  32.308  -1.771  1.00 24.20           O  
+ATOM   6221  ND2 ASN A 476      13.703  33.507  -3.250  1.00 22.74           N  
+ATOM   6222  OXT ASN A 476      12.804  35.906   1.787  1.00 23.68           O  
+ATOM   6223  H   ASN A 476      11.848  35.504  -0.789  1.00 24.30           H  
+ATOM   6224  HA  ASN A 476      13.505  33.685   0.339  1.00 26.80           H  
+ATOM   6225  HB2 ASN A 476      14.311  35.369  -1.756  1.00 26.96           H  
+ATOM   6226  HB3 ASN A 476      15.336  34.606  -0.812  1.00 26.96           H  
+ATOM   6227 HD21 ASN A 476      13.635  32.843  -3.792  1.00 27.28           H  
+ATOM   6228 HD22 ASN A 476      13.335  34.260  -3.445  1.00 27.28           H  
+TER    6229      ASN A 476                                                      
+HETATM 6230  N   OJC B 501     -13.158  25.397 -22.403  1.00 13.75           N  
+HETATM 6231  C   OJC B 501     -12.670  24.235 -21.954  1.00 12.77           C  
+HETATM 6232  O   OJC B 501     -11.281  20.931 -25.250  1.00 11.35           O  
+HETATM 6233  C1  OJC B 501     -13.683  25.446 -23.646  1.00 13.78           C  
+HETATM 6234  C2  OJC B 501     -13.684  24.261 -24.401  1.00 12.23           C  
+HETATM 6235  C3  OJC B 501     -13.129  23.139 -23.805  1.00 10.16           C  
+HETATM 6236  C10 OJC B 501     -13.429  15.620 -26.318  1.00  9.20           C  
+HETATM 6237  C11 OJC B 501     -12.240  15.191 -25.487  1.00  9.17           C  
+HETATM 6238  C12 OJC B 501     -12.599  15.043 -24.004  1.00  8.47           C  
+HETATM 6239  C13 OJC B 501     -11.516  15.842 -23.281  1.00  8.72           C  
+HETATM 6240  C14 OJC B 501     -11.117  16.872 -24.333  1.00  9.48           C  
+HETATM 6241  C4  OJC B 501     -13.764  22.719 -25.856  1.00 12.49           C  
+HETATM 6242  C5  OJC B 501     -12.569  20.838 -24.672  1.00  8.55           C  
+HETATM 6243  C6  OJC B 501     -13.258  19.733 -25.469  1.00  9.97           C  
+HETATM 6244  C7  OJC B 501     -12.116  18.710 -25.511  1.00  7.88           C  
+HETATM 6245  C8  OJC B 501     -10.874  19.599 -25.641  1.00  9.42           C  
+HETATM 6246  C9  OJC B 501     -10.286  19.647 -27.025  1.00  9.66           C  
+HETATM 6247  N1  OJC B 501     -12.607  23.061 -22.580  1.00 11.31           N  
+HETATM 6248  N2  OJC B 501     -13.177  22.153 -24.753  1.00 10.26           N  
+HETATM 6249  N3  OJC B 501     -14.094  23.978 -25.694  1.00 14.41           N  
+HETATM 6250  N4  OJC B 501     -14.141  26.617 -24.112  1.00 15.72           N  
+HETATM 6251  O1  OJC B 501     -11.353  19.857 -27.985  1.00 11.22           O  
+HETATM 6252  O10 OJC B 501     -10.375  15.091 -22.879  1.00  9.35           O  
+HETATM 6253  O11 OJC B 501     -12.625  13.687 -23.595  1.00 10.60           O  
+HETATM 6254  O12 OJC B 501     -14.464  19.276 -24.881  1.00  9.38           O  
+HETATM 6255  O2  OJC B 501     -10.728  17.775 -29.311  1.00 11.56           O  
+HETATM 6256  O3  OJC B 501     -12.239  19.571 -30.350  1.00 12.96           O  
+HETATM 6257  O4  OJC B 501     -13.048  18.142 -28.475  1.00 10.24           O  
+HETATM 6258  O5  OJC B 501     -13.567  16.303 -30.091  1.00 11.09           O  
+HETATM 6259  O6  OJC B 501     -15.184  16.959 -28.211  1.00 10.48           O  
+HETATM 6260  O7  OJC B 501     -13.047  15.755 -27.700  1.00 10.88           O  
+HETATM 6261  O8  OJC B 501     -11.182  16.175 -25.563  1.00  9.10           O  
+HETATM 6262  O9  OJC B 501     -12.051  17.930 -24.304  1.00  9.33           O  
+HETATM 6263  P   OJC B 501     -11.750  18.816 -29.123  1.00 10.55           P  
+HETATM 6264  P1  OJC B 501     -13.793  16.754 -28.688  1.00 10.03           P  
+HETATM 6265  H8  OJC B 501     -12.275  24.265 -20.940  1.00 15.33           H  
+HETATM 6266  H14 OJC B 501     -14.236  14.891 -26.253  1.00 11.03           H  
+HETATM 6267  H15 OJC B 501     -13.823  16.574 -25.974  1.00 11.03           H  
+HETATM 6268  H4  OJC B 501     -11.791  14.294 -25.911  1.00 11.00           H  
+HETATM 6269  H5  OJC B 501     -13.578  15.478 -23.809  1.00 10.17           H  
+HETATM 6270  H6  OJC B 501     -11.851  16.223 -22.317  1.00 10.47           H  
+HETATM 6271  H7  OJC B 501     -10.153  17.366 -24.227  1.00 11.38           H  
+HETATM 6272  H9  OJC B 501     -13.938  22.168 -26.780  1.00 14.99           H  
+HETATM 6273  H   OJC B 501     -12.502  20.592 -23.613  1.00 10.25           H  
+HETATM 6274  H1  OJC B 501     -13.514  20.024 -26.486  1.00 11.96           H  
+HETATM 6275  H2  OJC B 501     -12.199  18.056 -26.379  1.00  9.45           H  
+HETATM 6276  H3  OJC B 501     -10.116  19.341 -24.902  1.00 11.31           H  
+HETATM 6277  H10 OJC B 501      -9.774  18.715 -27.260  1.00 11.60           H  
+HETATM 6278  H11 OJC B 501      -9.565  20.459 -27.111  1.00 11.60           H  
+HETATM 6279  H20 OJC B 501     -14.128  27.458 -23.545  1.00 18.87           H  
+HETATM 6280  H19 OJC B 501     -14.517  26.706 -25.051  1.00 18.87           H  
+HETATM 6281  H16 OJC B 501     -10.621  14.129 -22.844  1.00 11.23           H  
+HETATM 6282  H17 OJC B 501     -13.044  13.165 -24.329  1.00 12.73           H  
+HETATM 6283  H18 OJC B 501     -14.889  18.684 -25.555  1.00 11.26           H  
+HETATM 6284  H12 OJC B 501     -12.228  20.563 -30.410  1.00 15.55           H  
+HETATM 6285  H13 OJC B 501     -15.657  16.228 -27.734  1.00 12.57           H  
+HETATM 6286  C1  GOL B 502     -20.650  -4.302  -5.482  1.00 25.21           C  
+HETATM 6287  O1  GOL B 502     -19.999  -3.811  -6.610  1.00 27.65           O  
+HETATM 6288  C2  GOL B 502     -21.912  -3.454  -5.328  1.00 27.90           C  
+HETATM 6289  O2  GOL B 502     -22.862  -3.798  -6.294  1.00 24.00           O  
+HETATM 6290  C3  GOL B 502     -22.362  -3.687  -3.899  1.00 26.02           C  
+HETATM 6291  O3  GOL B 502     -23.573  -3.065  -3.789  1.00 28.07           O  
+HETATM 6292  H11 GOL B 502     -20.112  -4.237  -4.677  1.00 30.25           H  
+HETATM 6293  H12 GOL B 502     -20.893  -5.238  -5.564  1.00 30.25           H  
+HETATM 6294  HO1 GOL B 502     -20.268  -4.271  -7.272  1.00 33.18           H  
+HETATM 6295  H2  GOL B 502     -21.739  -2.509  -5.461  1.00 33.48           H  
+HETATM 6296  HO2 GOL B 502     -23.630  -3.622  -5.975  1.00 28.80           H  
+HETATM 6297  H31 GOL B 502     -21.690  -3.341  -3.291  1.00 31.22           H  
+HETATM 6298  H32 GOL B 502     -22.397  -4.641  -3.726  1.00 31.22           H  
+HETATM 6299  HO3 GOL B 502     -23.833  -3.189  -2.988  1.00 33.69           H  
+HETATM 6300  S   SO4 B 503      -6.823   9.606 -34.448  1.00 17.99           S  
+HETATM 6301  O1  SO4 B 503      -6.080   9.486 -35.741  1.00 18.90           O  
+HETATM 6302  O2  SO4 B 503      -8.214   9.245 -34.606  1.00 18.01           O  
+HETATM 6303  O3  SO4 B 503      -6.244   8.704 -33.458  1.00 18.44           O  
+HETATM 6304  O4  SO4 B 503      -6.680  10.993 -33.993  1.00 20.37           O  
+HETATM 6305  N   OJC A 501     -15.106  27.089 -18.720  1.00 14.54           N  
+HETATM 6306  C   OJC A 501     -14.126  27.140 -17.809  1.00 14.63           C  
+HETATM 6307  O   OJC A 501     -14.687  29.872 -13.874  1.00 10.50           O  
+HETATM 6308  C1  OJC A 501     -16.019  28.082 -18.749  1.00 12.99           C  
+HETATM 6309  C2  OJC A 501     -15.866  29.136 -17.827  1.00 10.06           C  
+HETATM 6310  C3  OJC A 501     -14.792  29.055 -16.964  1.00 10.00           C  
+HETATM 6311  C10 OJC A 501     -11.915  34.702 -12.145  1.00 10.37           C  
+HETATM 6312  C11 OJC A 501     -11.154  33.724 -11.283  1.00 10.53           C  
+HETATM 6313  C12 OJC A 501      -9.886  33.239 -11.993  1.00 10.06           C  
+HETATM 6314  C13 OJC A 501      -9.962  31.717 -11.869  1.00  8.52           C  
+HETATM 6315  C14 OJC A 501     -11.468  31.487 -11.802  1.00 11.00           C  
+HETATM 6316  C4  OJC A 501     -15.982  30.851 -16.587  1.00 12.25           C  
+HETATM 6317  C5  OJC A 501     -14.056  30.451 -14.998  1.00 10.44           C  
+HETATM 6318  C6  OJC A 501     -13.902  31.930 -14.629  1.00  9.12           C  
+HETATM 6319  C7  OJC A 501     -13.420  31.774 -13.184  1.00 10.20           C  
+HETATM 6320  C8  OJC A 501     -14.201  30.554 -12.692  1.00  9.81           C  
+HETATM 6321  C9  OJC A 501     -15.374  30.869 -11.798  1.00 10.89           C  
+HETATM 6322  N1  OJC A 501     -13.883  28.080 -16.896  1.00 11.45           N  
+HETATM 6323  N2  OJC A 501     -14.877  30.167 -16.152  1.00 10.74           N  
+HETATM 6324  N3  OJC A 501     -16.616  30.275 -17.582  1.00 14.99           N  
+HETATM 6325  N4  OJC A 501     -17.037  28.002 -19.629  1.00 18.22           N  
+HETATM 6326  O1  OJC A 501     -16.121  31.983 -12.361  1.00 10.58           O  
+HETATM 6327  O10 OJC A 501      -9.331  31.182 -10.709  1.00  9.83           O  
+HETATM 6328  O11 OJC A 501      -8.707  33.768 -11.397  1.00  9.90           O  
+HETATM 6329  O12 OJC A 501     -12.980  32.579 -15.481  1.00 10.67           O  
+HETATM 6330  O2  OJC A 501     -15.765  33.436 -10.275  1.00 11.29           O  
+HETATM 6331  O3  OJC A 501     -17.619  33.947 -11.970  1.00 15.03           O  
+HETATM 6332  O4  OJC A 501     -15.209  34.296 -12.565  1.00 10.98           O  
+HETATM 6333  O5  OJC A 501     -15.185  36.530 -11.384  1.00 11.06           O  
+HETATM 6334  O6  OJC A 501     -13.988  36.124 -13.617  1.00 12.60           O  
+HETATM 6335  O7  OJC A 501     -13.126  35.152 -11.506  1.00 10.21           O  
+HETATM 6336  O8  OJC A 501     -11.948  32.555 -11.004  1.00 10.30           O  
+HETATM 6337  O9  OJC A 501     -12.003  31.532 -13.117  1.00 10.20           O  
+HETATM 6338  P   OJC A 501     -16.211  33.437 -11.676  1.00 11.51           P  
+HETATM 6339  P1  OJC A 501     -14.404  35.642 -12.283  1.00 10.98           P  
+HETATM 6340  H8  OJC A 501     -13.441  26.293 -17.827  1.00 17.55           H  
+HETATM 6341  H14 OJC A 501     -11.305  35.577 -12.364  1.00 12.44           H  
+HETATM 6342  H15 OJC A 501     -12.185  34.247 -13.096  1.00 12.44           H  
+HETATM 6343  H4  OJC A 501     -10.973  34.143 -10.294  1.00 12.64           H  
+HETATM 6344  H5  OJC A 501      -9.899  33.531 -13.042  1.00 12.07           H  
+HETATM 6345  H6  OJC A 501      -9.418  31.193 -12.653  1.00 10.23           H  
+HETATM 6346  H7  OJC A 501     -11.829  30.533 -11.422  1.00 13.20           H  
+HETATM 6347  H9  OJC A 501     -16.303  31.792 -16.143  1.00 14.70           H  
+HETATM 6348  H   OJC A 501     -13.092  29.979 -15.180  1.00 12.53           H  
+HETATM 6349  H1  OJC A 501     -14.831  32.499 -14.642  1.00 10.94           H  
+HETATM 6350  H2  OJC A 501     -13.683  32.642 -12.581  1.00 12.24           H  
+HETATM 6351  H3  OJC A 501     -13.539  29.825 -12.226  1.00 11.77           H  
+HETATM 6352  H10 OJC A 501     -15.034  31.139 -10.799  1.00 13.06           H  
+HETATM 6353  H11 OJC A 501     -16.033  30.007 -11.709  1.00 13.06           H  
+HETATM 6354  H20 OJC A 501     -17.118  27.228 -20.281  1.00 21.87           H  
+HETATM 6355  H19 OJC A 501     -17.761  28.712 -19.674  1.00 21.87           H  
+HETATM 6356  H16 OJC A 501      -8.500  31.696 -10.532  1.00 11.80           H  
+HETATM 6357  H17 OJC A 501      -8.899  34.710 -11.148  1.00 11.88           H  
+HETATM 6358  H18 OJC A 501     -13.187  33.548 -15.421  1.00 12.80           H  
+HETATM 6359  H12 OJC A 501     -18.261  33.450 -12.542  1.00 18.03           H  
+HETATM 6360  H13 OJC A 501     -13.078  36.500 -13.746  1.00 15.12           H  
+HETATM 6361  C1  GOL A 502      -1.152  45.702 -19.625  1.00 15.92           C  
+HETATM 6362  O1  GOL A 502      -2.322  44.961 -19.934  1.00 16.36           O  
+HETATM 6363  C2  GOL A 502      -1.246  47.051 -20.340  1.00 21.77           C  
+HETATM 6364  O2  GOL A 502      -2.440  47.631 -20.110  1.00 29.59           O  
+HETATM 6365  C3  GOL A 502      -0.085  47.919 -19.825  1.00 21.46           C  
+HETATM 6366  O3  GOL A 502      -0.331  49.229 -20.324  1.00 30.72           O  
+HETATM 6367  H11 GOL A 502      -0.342  45.250 -19.909  1.00 19.10           H  
+HETATM 6368  H12 GOL A 502      -1.051  45.855 -18.673  1.00 19.10           H  
+HETATM 6369  HO1 GOL A 502      -2.975  45.381 -19.609  1.00 19.63           H  
+HETATM 6370  H2  GOL A 502      -1.155  46.921 -21.297  1.00 26.12           H  
+HETATM 6371  H31 GOL A 502       0.756  47.540 -20.127  1.00 25.75           H  
+HETATM 6372  H32 GOL A 502      -0.055  47.871 -18.857  1.00 25.75           H  
+HETATM 6373  HO3 GOL A 502       0.416  49.640 -20.308  1.00 36.87           H  
+HETATM 6374  O   HOH B 601     -19.721   3.179  -4.091  1.00 26.11           O  
+HETATM 6375  O   HOH B 602     -28.806  18.945 -29.560  1.00 27.20           O  
+HETATM 6376  O   HOH B 603     -18.446  18.405 -39.169  1.00 39.30           O  
+HETATM 6377  O   HOH B 604     -17.127  23.548 -31.821  1.00 34.50           O  
+HETATM 6378  O   HOH B 605      -2.268  18.200  -7.799  1.00 27.53           O  
+HETATM 6379  O   HOH B 606      -4.035  10.945 -36.181  1.00 21.59           O  
+HETATM 6380  O   HOH B 607      -5.326  -8.762 -21.031  1.00 38.22           O  
+HETATM 6381  O   HOH B 608      -2.910  10.787 -31.855  1.00 20.19           O  
+HETATM 6382  O   HOH B 609      -4.955   9.390 -31.341  1.00 23.14           O  
+HETATM 6383  O   HOH B 610       2.756  32.989 -33.995  1.00 30.61           O  
+HETATM 6384  O   HOH B 611      -3.687  23.669  -2.331  1.00 11.80           O  
+HETATM 6385  O   HOH B 612     -36.593  12.611 -17.228  1.00 38.60           O  
+HETATM 6386  O   HOH B 613      -6.531   2.832  -0.578  1.00 34.81           O  
+HETATM 6387  O   HOH B 614      -2.303   4.705 -10.398  1.00 37.15           O  
+HETATM 6388  O   HOH B 615       1.818  13.857 -30.621  1.00 33.77           O  
+HETATM 6389  O   HOH B 616     -12.638  -1.203  -6.247  1.00 24.19           O  
+HETATM 6390  O   HOH B 617     -23.009  -6.995  -8.232  1.00 21.42           O  
+HETATM 6391  O   HOH B 618     -20.959  -8.673 -11.871  1.00 35.77           O  
+HETATM 6392  O   HOH B 619     -17.379  -3.985  -6.364  1.00 29.82           O  
+HETATM 6393  O   HOH B 620     -15.240   7.838  -0.707  1.00 22.57           O  
+HETATM 6394  O   HOH B 621     -17.102 -10.576 -31.171  1.00 32.70           O  
+HETATM 6395  O   HOH B 622      -6.974  -2.348 -24.901  1.00 28.25           O  
+HETATM 6396  O   HOH B 623     -13.680  13.633 -17.947  1.00 12.14           O  
+HETATM 6397  O   HOH B 624     -16.015  19.223 -27.042  1.00 10.57           O  
+HETATM 6398  O   HOH B 625      -7.877   0.085 -31.670  1.00 33.70           O  
+HETATM 6399  O   HOH B 626     -13.199  22.041 -29.969  1.00 24.79           O  
+HETATM 6400  O   HOH B 627     -12.230  19.184   3.116  1.00 25.53           O  
+HETATM 6401  O   HOH B 628      -6.663  13.163 -35.572  1.00 29.23           O  
+HETATM 6402  O   HOH B 629     -19.798  21.205  -7.171  1.00 23.67           O  
+HETATM 6403  O   HOH B 630     -11.987  24.217 -29.013  1.00 24.45           O  
+HETATM 6404  O   HOH B 631      -9.506  25.923 -29.565  1.00 16.58           O  
+HETATM 6405  O   HOH B 632      -0.897  17.313  -5.022  1.00 35.43           O  
+HETATM 6406  O   HOH B 633     -18.763   8.445   1.841  1.00 21.45           O  
+HETATM 6407  O   HOH B 634     -31.246   1.104  -9.894  1.00 23.38           O  
+HETATM 6408  O   HOH B 635     -18.121   1.296 -34.786  1.00 29.27           O  
+HETATM 6409  O   HOH B 636     -11.378  13.872 -20.594  1.00 10.59           O  
+HETATM 6410  O   HOH B 637      -8.907  17.057 -31.189  1.00 14.96           O  
+HETATM 6411  O   HOH B 638      -4.274   9.933  -2.916  1.00 33.28           O  
+HETATM 6412  O   HOH B 639     -12.555 -15.478 -23.796  1.00 39.68           O  
+HETATM 6413  O   HOH B 640     -24.656  19.869 -19.527  1.00 21.62           O  
+HETATM 6414  O   HOH B 641     -18.966  14.825   6.999  1.00 28.54           O  
+HETATM 6415  O   HOH B 642      -9.287   7.620 -36.527  1.00 18.18           O  
+HETATM 6416  O   HOH B 643     -15.555  25.247 -27.633  1.00 32.52           O  
+HETATM 6417  O   HOH B 644      -5.166  17.158  -8.750  1.00 20.93           O  
+HETATM 6418  O   HOH B 645       0.288   3.770 -16.406  1.00 31.19           O  
+HETATM 6419  O   HOH B 646       3.813  11.307 -19.703  1.00 22.81           O  
+HETATM 6420  O   HOH B 647       5.748  20.421 -28.111  1.00 43.26           O  
+HETATM 6421  O   HOH B 648      -3.216   9.884  -7.714  1.00 30.90           O  
+HETATM 6422  O   HOH B 649      -5.215  14.303 -30.436  1.00 16.80           O  
+HETATM 6423  O   HOH B 650     -20.054  19.014  -5.472  1.00 20.10           O  
+HETATM 6424  O   HOH B 651     -14.214  -3.749 -36.131  1.00 50.93           O  
+HETATM 6425  O   HOH B 652      -3.484  25.215 -34.383  1.00 29.21           O  
+HETATM 6426  O   HOH B 653      -2.115  13.026 -16.077  1.00 11.62           O  
+HETATM 6427  O   HOH B 654     -10.203  11.178 -34.461  1.00 19.22           O  
+HETATM 6428  O   HOH B 655     -22.406  21.016 -23.004  1.00 19.67           O  
+HETATM 6429  O   HOH B 656      -7.497  16.676   3.829  1.00 33.83           O  
+HETATM 6430  O   HOH B 657     -25.465  -2.814  -6.293  1.00 14.98           O  
+HETATM 6431  O   HOH B 658     -17.065   6.917 -35.183  1.00 37.29           O  
+HETATM 6432  O   HOH B 659     -32.231  -3.850 -22.955  1.00 32.02           O  
+HETATM 6433  O   HOH B 660     -16.124  -6.904 -10.600  1.00 17.86           O  
+HETATM 6434  O   HOH B 661     -17.821  13.594 -36.540  1.00 30.63           O  
+HETATM 6435  O   HOH B 662      -4.107  28.995 -27.474  1.00 15.42           O  
+HETATM 6436  O   HOH B 663     -24.524  -5.333 -14.799  1.00 31.31           O  
+HETATM 6437  O   HOH B 664      -3.674  -1.497 -17.703  1.00 31.39           O  
+HETATM 6438  O   HOH B 665     -12.879  27.268 -27.279  1.00 24.80           O  
+HETATM 6439  O   HOH B 666       3.311  13.473 -24.886  1.00 28.83           O  
+HETATM 6440  O   HOH B 667     -26.424  26.008 -36.407  1.00 14.44           O  
+HETATM 6441  O   HOH B 668     -28.244  -0.469 -27.140  1.00 34.80           O  
+HETATM 6442  O   HOH B 669     -10.740  21.121 -21.541  1.00 10.37           O  
+HETATM 6443  O   HOH B 670     -10.994  11.955   2.451  1.00 26.81           O  
+HETATM 6444  O   HOH B 671       0.966  -0.003 -29.037  1.00 27.94           O  
+HETATM 6445  O   HOH B 672     -13.887  14.943 -20.404  1.00 10.89           O  
+HETATM 6446  O   HOH B 673      -1.148   4.539 -20.147  1.00 15.46           O  
+HETATM 6447  O   HOH B 674      -9.105  14.701 -32.705  1.00 23.39           O  
+HETATM 6448  O   HOH B 675     -25.315  -5.483 -25.447  1.00 25.74           O  
+HETATM 6449  O   HOH B 676     -21.112   2.040 -34.904  1.00 28.54           O  
+HETATM 6450  O   HOH B 677      -8.117  31.245 -26.937  1.00 24.32           O  
+HETATM 6451  O   HOH B 678     -15.566  21.908 -34.207  1.00 40.90           O  
+HETATM 6452  O   HOH B 679      -0.474   6.150 -11.893  1.00 35.83           O  
+HETATM 6453  O   HOH B 680       1.124   3.004 -20.733  1.00 23.51           O  
+HETATM 6454  O   HOH B 681     -31.960   5.903 -13.782  1.00 25.07           O  
+HETATM 6455  O   HOH B 682     -17.665  20.983 -18.184  1.00 13.80           O  
+HETATM 6456  O   HOH B 683      -8.228  -9.557 -20.973  1.00 34.14           O  
+HETATM 6457  O   HOH B 684     -24.224   7.174 -34.639  1.00 41.92           O  
+HETATM 6458  O   HOH B 685     -15.373  17.403   5.227  1.00 24.40           O  
+HETATM 6459  O   HOH B 686     -20.346  25.966 -35.661  1.00 19.69           O  
+HETATM 6460  O   HOH B 687     -24.966  -8.855 -20.865  1.00 19.75           O  
+HETATM 6461  O   HOH B 688     -23.386   6.179 -32.387  1.00 26.57           O  
+HETATM 6462  O   HOH B 689      -1.443   0.930 -19.739  1.00 23.22           O  
+HETATM 6463  O   HOH B 690     -25.967  -4.452 -27.535  1.00 29.27           O  
+HETATM 6464  O   HOH B 691     -23.028  12.484  -1.360  1.00 28.05           O  
+HETATM 6465  O   HOH B 692       1.364   7.716 -26.568  1.00 17.86           O  
+HETATM 6466  O   HOH B 693       0.276  29.400 -34.432  1.00 47.92           O  
+HETATM 6467  O   HOH B 694     -25.311  21.518 -23.921  1.00 39.56           O  
+HETATM 6468  O   HOH B 695     -18.799  19.186 -26.904  1.00 12.96           O  
+HETATM 6469  O   HOH B 696     -28.490   2.637 -19.473  1.00 18.01           O  
+HETATM 6470  O   HOH B 697     -12.494  27.946 -21.226  1.00 15.74           O  
+HETATM 6471  O   HOH B 698     -17.188  24.793 -36.885  1.00 33.97           O  
+HETATM 6472  O   HOH B 699     -21.402  -7.923 -26.186  1.00 16.88           O  
+HETATM 6473  O   HOH B 700     -25.063  -1.324 -30.506  1.00 29.99           O  
+HETATM 6474  O   HOH B 701     -19.880  21.913 -19.693  1.00 15.80           O  
+HETATM 6475  O   HOH B 702       0.587  17.942 -30.181  1.00 17.24           O  
+HETATM 6476  O   HOH B 703       3.326   7.047 -22.498  1.00 35.64           O  
+HETATM 6477  O   HOH B 704     -15.729  21.794 -19.920  1.00 12.24           O  
+HETATM 6478  O   HOH B 705     -32.221  -4.905 -18.874  1.00 30.98           O  
+HETATM 6479  O   HOH B 706     -22.191  -9.403 -30.306  1.00 35.32           O  
+HETATM 6480  O   HOH B 707     -16.524 -18.206 -17.598  1.00 32.61           O  
+HETATM 6481  O   HOH B 708     -28.869   7.003  -6.261  1.00 36.93           O  
+HETATM 6482  O   HOH B 709      -2.240  18.490 -31.533  1.00 19.42           O  
+HETATM 6483  O   HOH B 710     -33.960  10.887 -18.489  1.00 32.26           O  
+HETATM 6484  O   HOH B 711     -15.250  16.014 -34.275  1.00 22.17           O  
+HETATM 6485  O   HOH B 712      -6.978   6.048  -1.290  1.00 42.44           O  
+HETATM 6486  O   HOH B 713       1.202  20.217 -33.843  1.00 38.45           O  
+HETATM 6487  O   HOH B 714     -25.063   1.217 -33.306  1.00 36.41           O  
+HETATM 6488  O   HOH B 715     -14.959  28.816 -22.291  1.00 20.70           O  
+HETATM 6489  O   HOH B 716      -9.190  -3.186 -23.745  1.00 15.73           O  
+HETATM 6490  O   HOH B 717     -12.866  11.458   8.527  1.00 32.80           O  
+HETATM 6491  O   HOH B 718     -19.393  21.584 -28.569  1.00 16.01           O  
+HETATM 6492  O   HOH B 719     -21.602  -4.734 -32.471  1.00 25.07           O  
+HETATM 6493  O   HOH B 720     -30.155  -1.463 -25.172  1.00 23.96           O  
+HETATM 6494  O   HOH B 721     -30.521   4.824 -10.628  1.00 18.92           O  
+HETATM 6495  O   HOH B 722     -10.975  23.287 -32.869  1.00 39.47           O  
+HETATM 6496  O   HOH B 723      -0.523   1.855 -17.232  1.00 37.26           O  
+HETATM 6497  O   HOH B 724      -6.242  31.560 -31.397  1.00 35.97           O  
+HETATM 6498  O   HOH B 725     -26.298   8.598 -30.356  1.00 27.16           O  
+HETATM 6499  O   HOH B 726     -17.411 -15.971 -15.099  1.00 28.44           O  
+HETATM 6500  O   HOH B 727     -23.817  14.854 -37.657  1.00 40.97           O  
+HETATM 6501  O   HOH B 728     -29.867  16.228 -25.196  1.00 28.88           O  
+HETATM 6502  O   HOH B 729     -10.548  19.626 -32.949  1.00 41.28           O  
+HETATM 6503  O   HOH B 730      -3.576  30.886 -29.389  1.00 21.16           O  
+HETATM 6504  O   HOH B 731     -28.254   8.352  -8.810  1.00 35.83           O  
+HETATM 6505  O   HOH B 732     -19.468  18.331  -0.320  1.00 25.60           O  
+HETATM 6506  O   HOH B 733      -9.602  27.427 -33.861  1.00 42.08           O  
+HETATM 6507  O   HOH B 734      -4.815  -2.200 -15.445  1.00 40.08           O  
+HETATM 6508  O   HOH B 735       2.937   4.123 -18.039  1.00 39.19           O  
+HETATM 6509  O   HOH B 736     -13.765  22.463 -32.566  1.00 43.85           O  
+HETATM 6510  O   HOH B 737     -26.676  -9.374 -18.805  1.00 31.69           O  
+HETATM 6511  O   HOH B 738      -3.749   8.160  -4.954  1.00 40.15           O  
+HETATM 6512  O   HOH B 739     -28.977   4.798 -21.344  1.00 34.66           O  
+HETATM 6513  O   HOH B 740     -23.893  -5.019 -12.395  1.00 41.95           O  
+HETATM 6514  O   HOH B 741     -10.793  28.220 -29.769  1.00 32.24           O  
+HETATM 6515  O   HOH B 742     -33.543  -3.121 -17.040  1.00 39.08           O  
+HETATM 6516  O   HOH B 743     -19.903  18.819   4.532  1.00 42.17           O  
+HETATM 6517  O   HOH B 744     -20.462  22.781 -22.394  1.00 30.18           O  
+HETATM 6518  O   HOH B 745     -15.118  17.695 -36.273  1.00 37.42           O  
+HETATM 6519  O   HOH B 746      -9.295  12.441  -0.913  1.00 33.65           O  
+HETATM 6520  O   HOH B 747      -2.751  12.237 -33.971  1.00 30.69           O  
+HETATM 6521  O   HOH B 748     -25.477  22.914 -15.550  1.00 37.09           O  
+HETATM 6522  O   HOH B 749     -19.493  -9.921 -32.602  1.00 41.55           O  
+HETATM 6523  O   HOH B 750     -18.212  17.241   6.283  1.00 35.23           O  
+HETATM 6524  O   HOH B 751      -8.416  12.386   2.931  1.00 38.23           O  
+HETATM 6525  O   HOH B 752      -4.174  -7.457 -25.344  1.00 43.09           O  
+HETATM 6526  O   HOH B 753      -3.007  22.404 -34.677  1.00 37.62           O  
+HETATM 6527  O   HOH B 754       3.132   7.722 -15.344  1.00 27.85           O  
+HETATM 6528  O   HOH B 755     -16.805   4.260   0.591  1.00 27.95           O  
+HETATM 6529  O   HOH B 756     -12.627  29.564 -25.976  1.00 34.00           O  
+HETATM 6530  O   HOH B 757     -10.095  30.688 -28.294  1.00 35.39           O  
+HETATM 6531  O   HOH B 758     -15.182  21.347 -28.682  1.00 17.96           O  
+HETATM 6532  O   HOH B 759     -17.961  25.436 -34.564  1.00 40.62           O  
+HETATM 6533  O   HOH B 760     -24.503  -7.979 -29.245  1.00 29.78           O  
+HETATM 6534  O   HOH B 761     -26.482   5.897 -30.574  1.00 32.36           O  
+HETATM 6535  O   HOH B 762     -24.596   9.462 -32.924  1.00 28.74           O  
+HETATM 6536  O   HOH B 763      -5.817  10.190  -0.538  1.00 32.13           O  
+HETATM 6537  O   HOH B 764      -5.223  16.573 -32.348  1.00 37.96           O  
+HETATM 6538  O   HOH B 765     -23.956  -7.763 -15.257  1.00 34.67           O  
+HETATM 6539  O   HOH B 766     -17.101  22.823 -29.266  1.00 33.92           O  
+HETATM 6540  O   HOH B 767       1.932  16.234 -31.697  1.00 32.16           O  
+HETATM 6541  O   HOH B 768     -18.360  26.453 -24.119  1.00 31.63           O  
+HETATM 6542  O   HOH B 769       3.000   4.501 -21.972  1.00 40.13           O  
+HETATM 6543  O   HOH B 770     -24.890  12.530 -33.631  1.00 40.49           O  
+HETATM 6544  O   HOH B 771     -25.769  -5.507 -29.874  1.00 35.82           O  
+HETATM 6545  O   HOH B 772     -26.300  21.139 -21.584  1.00 37.43           O  
+HETATM 6546  O   HOH B 773     -22.168  27.630 -34.291  1.00 20.91           O  
+HETATM 6547  O   HOH B 774     -22.612  21.980 -19.093  1.00 22.68           O  
+HETATM 6548  O   HOH B 775      -1.333  -0.078 -15.849  1.00 41.69           O  
+HETATM 6549  O   HOH B 776     -22.847 -10.617 -32.623  1.00 39.33           O  
+HETATM 6550  O   HOH B 777     -38.315  10.767 -16.350  1.00 45.33           O  
+HETATM 6551  O   HOH B 778     -20.709  23.822 -27.393  1.00 24.95           O  
+HETATM 6552  O   HOH A 601      -4.362  48.008   6.850  1.00 40.67           O  
+HETATM 6553  O   HOH A 602      11.543  32.692 -20.127  1.00 39.62           O  
+HETATM 6554  O   HOH A 603      -3.783  47.802 -33.360  1.00 38.88           O  
+HETATM 6555  O   HOH A 604     -15.114  33.008  -1.605  1.00 31.58           O  
+HETATM 6556  O   HOH A 605       1.380  17.645  -6.464  1.00 36.87           O  
+HETATM 6557  O   HOH A 606     -13.499  44.071  -5.437  1.00 30.74           O  
+HETATM 6558  O   HOH A 607      15.045  37.998  -0.825  1.00 33.14           O  
+HETATM 6559  O   HOH A 608     -30.277  29.216  -9.015  1.00 39.67           O  
+HETATM 6560  O   HOH A 609      -5.363  51.994 -16.674  1.00 32.72           O  
+HETATM 6561  O   HOH A 610      12.671  37.542 -15.380  1.00 31.84           O  
+HETATM 6562  O   HOH A 611       0.589  33.134 -27.380  1.00 42.85           O  
+HETATM 6563  O   HOH A 612      15.490  43.138  -1.677  1.00 36.46           O  
+HETATM 6564  O   HOH A 613       8.362  17.609  -9.996  1.00 36.00           O  
+HETATM 6565  O   HOH A 614       3.309  23.983  -1.976  1.00 27.25           O  
+HETATM 6566  O   HOH A 615     -19.508  30.675 -14.867  1.00 24.83           O  
+HETATM 6567  O   HOH A 616      13.303  43.388 -12.404  1.00 26.98           O  
+HETATM 6568  O   HOH A 617     -15.169  47.732 -22.792  1.00 38.71           O  
+HETATM 6569  O   HOH A 618     -26.931  26.601  -5.441  1.00 46.12           O  
+HETATM 6570  O   HOH A 619     -13.349  36.156   2.870  1.00 41.24           O  
+HETATM 6571  O   HOH A 620       2.384  20.183 -14.273  1.00 22.19           O  
+HETATM 6572  O   HOH A 621      -9.544  29.814   3.907  1.00 36.68           O  
+HETATM 6573  O   HOH A 622       0.015  25.010 -26.322  1.00 24.55           O  
+HETATM 6574  O   HOH A 623      -0.046  10.824 -17.165  1.00 12.76           O  
+HETATM 6575  O   HOH A 624      -7.291  51.636   1.694  1.00 29.49           O  
+HETATM 6576  O   HOH A 625      -6.380  46.814   3.046  1.00 27.02           O  
+HETATM 6577  O   HOH A 626      -9.059  47.123 -23.674  1.00 35.06           O  
+HETATM 6578  O   HOH A 627      -8.271  53.764  -4.476  1.00 39.41           O  
+HETATM 6579  O   HOH A 628      16.547  41.922  -6.123  1.00 32.21           O  
+HETATM 6580  O   HOH A 629       3.364  48.391 -22.740  1.00 25.59           O  
+HETATM 6581  O   HOH A 630       5.042  55.479 -16.870  1.00 33.49           O  
+HETATM 6582  O   HOH A 631      11.061  26.007  -2.432  1.00 27.41           O  
+HETATM 6583  O   HOH A 632     -24.157  43.427 -16.547  1.00 39.66           O  
+HETATM 6584  O   HOH A 633       2.987  23.038  -4.798  1.00 26.40           O  
+HETATM 6585  O   HOH A 634     -19.877  34.383 -10.596  1.00 29.38           O  
+HETATM 6586  O   HOH A 635      -9.139  51.438  -7.680  1.00 31.81           O  
+HETATM 6587  O   HOH A 636     -18.757  33.264 -14.302  1.00 20.96           O  
+HETATM 6588  O   HOH A 637     -21.321  28.668 -13.719  1.00 20.25           O  
+HETATM 6589  O   HOH A 638     -14.385  34.856 -15.951  1.00 11.10           O  
+HETATM 6590  O   HOH A 639     -17.085  33.736  -7.952  1.00 15.02           O  
+HETATM 6591  O   HOH A 640      -6.791  28.963   1.689  1.00 17.79           O  
+HETATM 6592  O   HOH A 641      -4.181  31.333 -14.020  1.00 12.60           O  
+HETATM 6593  O   HOH A 642     -11.464  42.549 -26.077  1.00 35.93           O  
+HETATM 6594  O   HOH A 643      -6.658  31.193 -11.543  1.00 10.76           O  
+HETATM 6595  O   HOH A 644      -7.904  35.787 -25.074  1.00 25.02           O  
+HETATM 6596  O   HOH A 645       7.096  33.632   0.864  1.00 17.71           O  
+HETATM 6597  O   HOH A 646      -6.441  22.413   1.462  1.00 25.40           O  
+HETATM 6598  O   HOH A 647     -11.865  24.317   1.414  1.00 23.22           O  
+HETATM 6599  O   HOH A 648      -6.224  35.507   8.519  1.00 16.02           O  
+HETATM 6600  O   HOH A 649     -18.845  31.166 -18.917  1.00 32.78           O  
+HETATM 6601  O   HOH A 650      -9.067  49.868  -4.516  1.00 28.04           O  
+HETATM 6602  O   HOH A 651     -25.316  27.735  -7.035  1.00 32.17           O  
+HETATM 6603  O   HOH A 652      11.458  45.683 -23.830  1.00 31.65           O  
+HETATM 6604  O   HOH A 653     -20.109  28.695 -17.758  1.00 29.81           O  
+HETATM 6605  O   HOH A 654      11.149  28.247   1.297  1.00 18.73           O  
+HETATM 6606  O   HOH A 655      -7.876  44.346 -25.001  1.00 20.18           O  
+HETATM 6607  O   HOH A 656      -7.154  42.801   2.934  1.00 36.26           O  
+HETATM 6608  O   HOH A 657      -3.636  44.772 -34.706  1.00 34.80           O  
+HETATM 6609  O   HOH A 658       2.754  25.629 -25.944  1.00 18.41           O  
+HETATM 6610  O   HOH A 659      -0.867  53.396 -13.900  1.00 31.59           O  
+HETATM 6611  O   HOH A 660     -13.069  46.493  -6.883  1.00 25.19           O  
+HETATM 6612  O   HOH A 661      -3.804  36.625   9.404  1.00 14.53           O  
+HETATM 6613  O   HOH A 662      14.786  30.058  -4.606  1.00 29.53           O  
+HETATM 6614  O   HOH A 663      14.418  25.106 -21.293  1.00 43.80           O  
+HETATM 6615  O   HOH A 664     -16.759  35.387  -5.813  1.00 28.33           O  
+HETATM 6616  O   HOH A 665       7.259  15.200 -23.354  1.00 27.85           O  
+HETATM 6617  O   HOH A 666       4.470  33.320   1.811  1.00 14.77           O  
+HETATM 6618  O   HOH A 667       8.388  13.052 -19.425  1.00 31.88           O  
+HETATM 6619  O   HOH A 668       0.865  31.434   3.177  1.00 14.60           O  
+HETATM 6620  O   HOH A 669     -18.291  43.379 -10.849  1.00 39.27           O  
+HETATM 6621  O   HOH A 670       9.548  37.218   3.733  1.00 36.81           O  
+HETATM 6622  O   HOH A 671      -6.889  32.127 -14.150  1.00 10.60           O  
+HETATM 6623  O   HOH A 672       8.714  30.252  -0.176  1.00 19.72           O  
+HETATM 6624  O   HOH A 673     -22.684  22.394 -12.091  1.00 14.46           O  
+HETATM 6625  O   HOH A 674       5.511  52.421 -23.505  1.00 35.40           O  
+HETATM 6626  O   HOH A 675     -22.470  27.025  -1.235  1.00 37.28           O  
+HETATM 6627  O   HOH A 676       0.135  35.880 -29.147  1.00 22.82           O  
+HETATM 6628  O   HOH A 677       1.185  40.772   0.758  1.00 20.75           O  
+HETATM 6629  O   HOH A 678      -4.171  23.263  -5.399  1.00 12.12           O  
+HETATM 6630  O   HOH A 679      -1.575  27.083   3.646  1.00 20.16           O  
+HETATM 6631  O   HOH A 680       7.252  31.040  -4.044  1.00 23.48           O  
+HETATM 6632  O   HOH A 681      12.315  52.760  -3.541  1.00 27.77           O  
+HETATM 6633  O   HOH A 682     -12.137  27.408 -14.737  1.00 11.02           O  
+HETATM 6634  O   HOH A 683     -10.364  45.791  -3.549  1.00 36.92           O  
+HETATM 6635  O   HOH A 684      -8.452  30.074 -21.012  1.00 14.03           O  
+HETATM 6636  O   HOH A 685      -3.249  53.631  -9.642  1.00 27.45           O  
+HETATM 6637  O   HOH A 686       8.416  52.575  -8.707  1.00 31.21           O  
+HETATM 6638  O   HOH A 687      -1.141  45.715 -27.768  1.00 19.92           O  
+HETATM 6639  O   HOH A 688      10.068  35.331   2.349  1.00 22.29           O  
+HETATM 6640  O   HOH A 689     -15.504  32.231  -3.970  1.00 19.80           O  
+HETATM 6641  O   HOH A 690      -6.242  51.734 -24.424  1.00 42.15           O  
+HETATM 6642  O   HOH A 691     -25.919  43.772 -22.599  1.00 35.79           O  
+HETATM 6643  O   HOH A 692       2.893  53.039  -0.766  1.00 33.14           O  
+HETATM 6644  O   HOH A 693     -24.563  36.712 -17.943  1.00 38.64           O  
+HETATM 6645  O   HOH A 694      -9.940  49.303 -12.018  1.00 25.77           O  
+HETATM 6646  O   HOH A 695      11.227  49.516 -14.197  1.00 34.69           O  
+HETATM 6647  O   HOH A 696     -23.003  23.365 -16.608  1.00 22.67           O  
+HETATM 6648  O   HOH A 697     -19.242  28.824  -3.385  1.00 17.77           O  
+HETATM 6649  O   HOH A 698     -14.256  44.140 -24.664  1.00 32.23           O  
+HETATM 6650  O   HOH A 699     -18.176  26.601  -1.335  1.00 16.25           O  
+HETATM 6651  O   HOH A 700       2.994  47.720 -18.454  1.00 17.65           O  
+HETATM 6652  O   HOH A 701       5.863  51.710  -3.529  1.00 31.65           O  
+HETATM 6653  O   HOH A 702     -15.314  38.912  -3.407  1.00 32.70           O  
+HETATM 6654  O   HOH A 703       5.848  14.477 -10.063  1.00 42.23           O  
+HETATM 6655  O   HOH A 704      -0.082  31.294 -25.664  1.00 16.14           O  
+HETATM 6656  O   HOH A 705     -15.934  24.673 -20.075  1.00 15.91           O  
+HETATM 6657  O   HOH A 706      -7.530  42.904 -29.258  1.00 29.85           O  
+HETATM 6658  O   HOH A 707      -3.289  55.649   2.474  1.00 35.30           O  
+HETATM 6659  O   HOH A 708       1.350  54.037 -15.646  1.00 23.17           O  
+HETATM 6660  O   HOH A 709     -11.573  35.618 -23.090  1.00 20.07           O  
+HETATM 6661  O   HOH A 710       0.548  52.924   2.499  1.00 33.38           O  
+HETATM 6662  O   HOH A 711     -10.575  29.265 -19.462  1.00 12.59           O  
+HETATM 6663  O   HOH A 712     -23.800  37.649 -21.138  1.00 31.13           O  
+HETATM 6664  O   HOH A 713       3.701  52.611  -5.010  1.00 27.03           O  
+HETATM 6665  O   HOH A 714      14.690  25.523   0.591  1.00 20.39           O  
+HETATM 6666  O   HOH A 715     -13.728  36.545 -18.165  1.00 12.05           O  
+HETATM 6667  O   HOH A 716      -7.011  56.673  -1.993  1.00 25.51           O  
+HETATM 6668  O   HOH A 717     -19.932  19.819   1.995  1.00 37.90           O  
+HETATM 6669  O   HOH A 718       9.563  34.062 -20.805  1.00 29.21           O  
+HETATM 6670  O   HOH A 719       4.818  19.738 -14.786  1.00 23.68           O  
+HETATM 6671  O   HOH A 720     -16.952  26.391 -22.070  1.00 22.52           O  
+HETATM 6672  O   HOH A 721       8.156  16.510 -25.828  1.00 32.78           O  
+HETATM 6673  O   HOH A 722      -4.444  27.452   4.237  1.00 36.84           O  
+HETATM 6674  O   HOH A 723      -7.454  31.138   3.180  1.00 20.25           O  
+HETATM 6675  O   HOH A 724       5.112  30.255  -2.266  1.00 25.52           O  
+HETATM 6676  O   HOH A 725      12.462  24.612 -14.530  1.00 32.43           O  
+HETATM 6677  O   HOH A 726      13.323  20.305 -27.847  1.00 45.76           O  
+HETATM 6678  O   HOH A 727     -19.498  46.491 -21.835  1.00 29.85           O  
+HETATM 6679  O   HOH A 728       9.153  49.552   5.159  1.00 33.05           O  
+HETATM 6680  O   HOH A 729     -18.245  35.387 -18.488  1.00 21.18           O  
+HETATM 6681  O   HOH A 730      13.733  44.397 -17.663  1.00 33.69           O  
+HETATM 6682  O   HOH A 731     -16.156  36.489 -19.622  1.00 16.99           O  
+HETATM 6683  O   HOH A 732      13.516  32.500 -22.254  1.00 52.81           O  
+HETATM 6684  O   HOH A 733     -17.610  46.416 -12.783  1.00 29.23           O  
+HETATM 6685  O   HOH A 734      16.705  47.719  -1.253  1.00 32.94           O  
+HETATM 6686  O   HOH A 735      10.340  20.284 -14.001  1.00 27.48           O  
+HETATM 6687  O   HOH A 736      -9.369  39.014   3.626  1.00 37.15           O  
+HETATM 6688  O   HOH A 737      -6.195  54.103 -10.241  1.00 30.96           O  
+HETATM 6689  O   HOH A 738       8.667  54.130 -17.372  1.00 35.71           O  
+HETATM 6690  O   HOH A 739     -26.933  25.082 -13.821  1.00 38.78           O  
+HETATM 6691  O   HOH A 740      -0.635  49.721   6.479  1.00 30.75           O  
+HETATM 6692  O   HOH A 741      10.731  52.811 -15.124  1.00 41.34           O  
+HETATM 6693  O   HOH A 742     -13.773  42.186  -0.622  1.00 31.72           O  
+HETATM 6694  O   HOH A 743       6.548  48.470   5.073  1.00 38.75           O  
+HETATM 6695  O   HOH A 744       1.462  51.707   5.130  1.00 32.95           O  
+HETATM 6696  O   HOH A 745     -18.484  27.664   1.259  1.00 31.73           O  
+HETATM 6697  O   HOH A 746       9.127  24.967  -6.410  1.00 26.18           O  
+HETATM 6698  O   HOH A 747      -8.486  40.923   2.250  1.00 32.12           O  
+HETATM 6699  O   HOH A 748      13.023  52.121   2.357  1.00 39.51           O  
+HETATM 6700  O   HOH A 749      -1.681  32.643 -27.860  1.00 31.92           O  
+HETATM 6701  O   HOH A 750      -6.305  32.644 -28.743  1.00 32.67           O  
+HETATM 6702  O   HOH A 751       9.504  51.876 -20.143  1.00 40.95           O  
+HETATM 6703  O   HOH A 752     -25.295  21.990 -12.202  1.00 25.33           O  
+HETATM 6704  O   HOH A 753      -6.156  53.445   3.817  1.00 28.84           O  
+HETATM 6705  O   HOH A 754     -22.903  28.221 -16.129  1.00 33.15           O  
+HETATM 6706  O   HOH A 755     -20.307  26.731 -19.547  1.00 35.63           O  
+HETATM 6707  O   HOH A 756      12.502  45.945 -15.714  1.00 37.23           O  
+HETATM 6708  O   HOH A 757      -7.063  30.765   5.949  1.00 25.17           O  
+HETATM 6709  O   HOH A 758      -1.822  40.561 -33.428  1.00 26.93           O  
+HETATM 6710  O   HOH A 759     -11.416  48.909 -14.501  1.00 34.15           O  
+HETATM 6711  O   HOH A 760       5.126  13.959 -23.164  1.00 43.40           O  
+HETATM 6712  O   HOH A 761      -9.325  24.527   2.604  1.00 37.41           O  
+HETATM 6713  O   HOH A 762     -21.979  18.955  -1.271  1.00 32.82           O  
+HETATM 6714  O   HOH A 763      10.122  53.755  -4.991  1.00 32.94           O  
+HETATM 6715  O   HOH A 764       9.774  26.046   0.115  1.00 25.74           O  
+HETATM 6716  O   HOH A 765     -18.374  31.553  -4.236  1.00 26.46           O  
+HETATM 6717  O   HOH A 766     -12.636  33.374 -23.037  1.00 33.22           O  
+HETATM 6718  O   HOH A 767     -23.167  25.789 -17.411  1.00 37.81           O  
+HETATM 6719  O   HOH A 768     -18.709  24.558 -19.335  1.00 28.09           O  
+HETATM 6720  O   HOH A 769     -16.719  30.817 -22.294  1.00 33.77           O  
+HETATM 6721  O   HOH A 770      -2.695  18.203 -10.507  1.00 24.36           O  
+HETATM 6722  O   HOH A 771      16.069  41.068  -0.517  1.00 43.57           O  
+HETATM 6723  O   HOH A 772      -8.329  31.797   8.188  1.00 32.94           O  
+HETATM 6724  O   HOH A 773     -17.016  34.092 -16.285  1.00 17.00           O  
+HETATM 6725  O   HOH A 774     -20.317  29.456  -0.985  1.00 40.17           O  
+HETATM 6726  O   HOH A 775      -7.239  50.768 -14.883  1.00 32.90           O  
+HETATM 6727  O   HOH A 776     -15.148  42.455  -6.702  1.00 33.43           O  
+HETATM 6728  O   HOH A 777      12.067  48.658 -16.496  1.00 36.58           O  
+HETATM 6729  O   HOH A 778      -6.773  38.134   7.501  1.00 37.67           O  
+HETATM 6730  O   HOH A 779     -17.354  47.452 -23.328  1.00 43.56           O  
+HETATM 6731  O   HOH A 780      -9.088  33.139 -24.931  1.00 25.04           O  
+HETATM 6732  O   HOH A 781     -16.069  41.482  -4.519  1.00 36.58           O  
+HETATM 6733  O   HOH A 782      16.749  43.008  -3.613  1.00 39.58           O  
+HETATM 6734  O   HOH A 783       3.791  54.125  -7.017  1.00 33.11           O  
+HETATM 6735  O   HOH A 784     -13.284  25.871   3.425  1.00 29.35           O  
+HETATM 6736  O   HOH A 785     -19.809  32.675  -6.934  1.00 43.74           O  
+HETATM 6737  O   HOH A 786     -16.307  35.468 -22.278  1.00 23.74           O  
+HETATM 6738  O   HOH A 787     -16.060  36.868 -24.633  1.00 35.75           O  
+CONECT 6230 6231 6233                                                           
+CONECT 6231 6230 6247 6265                                                      
+CONECT 6232 6242 6245                                                           
+CONECT 6233 6230 6234 6250                                                      
+CONECT 6234 6233 6235 6249                                                      
+CONECT 6235 6234 6247 6248                                                      
+CONECT 6236 6237 6260 6266 6267                                                 
+CONECT 6237 6236 6238 6261 6268                                                 
+CONECT 6238 6237 6239 6253 6269                                                 
+CONECT 6239 6238 6240 6252 6270                                                 
+CONECT 6240 6239 6261 6262 6271                                                 
+CONECT 6241 6248 6249 6272                                                      
+CONECT 6242 6232 6243 6248 6273                                                 
+CONECT 6243 6242 6244 6254 6274                                                 
+CONECT 6244 6243 6245 6262 6275                                                 
+CONECT 6245 6232 6244 6246 6276                                                 
+CONECT 6246 6245 6251 6277 6278                                                 
+CONECT 6247 6231 6235                                                           
+CONECT 6248 6235 6241 6242                                                      
+CONECT 6249 6234 6241                                                           
+CONECT 6250 6233 6279 6280                                                      
+CONECT 6251 6246 6263                                                           
+CONECT 6252 6239 6281                                                           
+CONECT 6253 6238 6282                                                           
+CONECT 6254 6243 6283                                                           
+CONECT 6255 6263                                                                
+CONECT 6256 6263 6284                                                           
+CONECT 6257 6263 6264                                                           
+CONECT 6258 6264                                                                
+CONECT 6259 6264 6285                                                           
+CONECT 6260 6236 6264                                                           
+CONECT 6261 6237 6240                                                           
+CONECT 6262 6240 6244                                                           
+CONECT 6263 6251 6255 6256 6257                                                 
+CONECT 6264 6257 6258 6259 6260                                                 
+CONECT 6265 6231                                                                
+CONECT 6266 6236                                                                
+CONECT 6267 6236                                                                
+CONECT 6268 6237                                                                
+CONECT 6269 6238                                                                
+CONECT 6270 6239                                                                
+CONECT 6271 6240                                                                
+CONECT 6272 6241                                                                
+CONECT 6273 6242                                                                
+CONECT 6274 6243                                                                
+CONECT 6275 6244                                                                
+CONECT 6276 6245                                                                
+CONECT 6277 6246                                                                
+CONECT 6278 6246                                                                
+CONECT 6279 6250                                                                
+CONECT 6280 6250                                                                
+CONECT 6281 6252                                                                
+CONECT 6282 6253                                                                
+CONECT 6283 6254                                                                
+CONECT 6284 6256                                                                
+CONECT 6285 6259                                                                
+CONECT 6286 6287 6288 6292 6293                                                 
+CONECT 6287 6286 6294                                                           
+CONECT 6288 6286 6289 6290 6295                                                 
+CONECT 6289 6288 6296                                                           
+CONECT 6290 6288 6291 6297 6298                                                 
+CONECT 6291 6290 6299                                                           
+CONECT 6292 6286                                                                
+CONECT 6293 6286                                                                
+CONECT 6294 6287                                                                
+CONECT 6295 6288                                                                
+CONECT 6296 6289                                                                
+CONECT 6297 6290                                                                
+CONECT 6298 6290                                                                
+CONECT 6299 6291                                                                
+CONECT 6300 6301 6302 6303 6304                                                 
+CONECT 6301 6300                                                                
+CONECT 6302 6300                                                                
+CONECT 6303 6300                                                                
+CONECT 6304 6300                                                                
+CONECT 6305 6306 6308                                                           
+CONECT 6306 6305 6322 6340                                                      
+CONECT 6307 6317 6320                                                           
+CONECT 6308 6305 6309 6325                                                      
+CONECT 6309 6308 6310 6324                                                      
+CONECT 6310 6309 6322 6323                                                      
+CONECT 6311 6312 6335 6341 6342                                                 
+CONECT 6312 6311 6313 6336 6343                                                 
+CONECT 6313 6312 6314 6328 6344                                                 
+CONECT 6314 6313 6315 6327 6345                                                 
+CONECT 6315 6314 6336 6337 6346                                                 
+CONECT 6316 6323 6324 6347                                                      
+CONECT 6317 6307 6318 6323 6348                                                 
+CONECT 6318 6317 6319 6329 6349                                                 
+CONECT 6319 6318 6320 6337 6350                                                 
+CONECT 6320 6307 6319 6321 6351                                                 
+CONECT 6321 6320 6326 6352 6353                                                 
+CONECT 6322 6306 6310                                                           
+CONECT 6323 6310 6316 6317                                                      
+CONECT 6324 6309 6316                                                           
+CONECT 6325 6308 6354 6355                                                      
+CONECT 6326 6321 6338                                                           
+CONECT 6327 6314 6356                                                           
+CONECT 6328 6313 6357                                                           
+CONECT 6329 6318 6358                                                           
+CONECT 6330 6338                                                                
+CONECT 6331 6338 6359                                                           
+CONECT 6332 6338 6339                                                           
+CONECT 6333 6339                                                                
+CONECT 6334 6339 6360                                                           
+CONECT 6335 6311 6339                                                           
+CONECT 6336 6312 6315                                                           
+CONECT 6337 6315 6319                                                           
+CONECT 6338 6326 6330 6331 6332                                                 
+CONECT 6339 6332 6333 6334 6335                                                 
+CONECT 6340 6306                                                                
+CONECT 6341 6311                                                                
+CONECT 6342 6311                                                                
+CONECT 6343 6312                                                                
+CONECT 6344 6313                                                                
+CONECT 6345 6314                                                                
+CONECT 6346 6315                                                                
+CONECT 6347 6316                                                                
+CONECT 6348 6317                                                                
+CONECT 6349 6318                                                                
+CONECT 6350 6319                                                                
+CONECT 6351 6320                                                                
+CONECT 6352 6321                                                                
+CONECT 6353 6321                                                                
+CONECT 6354 6325                                                                
+CONECT 6355 6325                                                                
+CONECT 6356 6327                                                                
+CONECT 6357 6328                                                                
+CONECT 6358 6329                                                                
+CONECT 6359 6331                                                                
+CONECT 6360 6334                                                                
+CONECT 6361 6362 6363 6367 6368                                                 
+CONECT 6362 6361 6369                                                           
+CONECT 6363 6361 6364 6365 6370                                                 
+CONECT 6364 6363                                                                
+CONECT 6365 6363 6366 6371 6372                                                 
+CONECT 6366 6365 6373                                                           
+CONECT 6367 6361                                                                
+CONECT 6368 6361                                                                
+CONECT 6369 6362                                                                
+CONECT 6370 6363                                                                
+CONECT 6371 6365                                                                
+CONECT 6372 6365                                                                
+CONECT 6373 6366                                                                
+MASTER      255    0    5   22   14    0    0    6 3596    2  144   32          
+END