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