diff --git a/content/3.defense-systems/abiq.md b/content/3.defense-systems/abiq.md
index c322ca514b03f2af1c3b3d56f440f4173c35adfd..1aa0d2349cc9c25b66854f6d1fa7485bea5c6319 100644
--- a/content/3.defense-systems/abiq.md
+++ b/content/3.defense-systems/abiq.md
@@ -10,13 +10,33 @@ tableColumns:
Activator: Unknown
Effector: Unknown
PFAM: PF13958
+contributors:
+ - Florian Tesson
relevantAbstracts:
- doi: 10.1023/A:1002027321171
- doi: 10.1016/j.mib.2005.06.006
- doi: 10.1128/AEM.64.12.4748-4756.1998
+ - doi: 10.1111/mmi.12129
---
# AbiQ
+
+## Description
+
+AbiQ was discovered in 1998 on *Lactococcus lactis* plasmid :ref{doi=10.1128/AEM.64.12.4748-4756.1998}.
+
+AbiQ is one of the so-called "Abi" systems for "Abortive infection" discovered in the 90's in research related to the dairy industry :ref{doi=10.1016/j.mib.2005.06.006}. AbiQ is classified as abortive infection in :ref{doi=10.1016/j.mib.2023.102312}.
+
+AbiQ is composed of a single protein AbiQ and an RNA antitoxin (antiQ) :ref{doi=10.1111/mmi.12129}.
+
+## Molecular mechanism
+
+AbiQ act as an anti-toxin type III. AbiQ is an RNAase that will bind its antitoxin antiQ :ref{doi=10.1111/mmi.12129}.
+
+The AbiQ is constitutively expressed and bind to its antiQ RNA resulting in an inactivated AbiQ.
+To get activated, AbiQ needs the concentration of antiQ to decrease.
+However, during phage infection, the expression of the antiQ is constant and the authors do not know how the AbiQ is activated :ref{doi=10.1111/mmi.12129}.
+
## Example of genomic structure
The AbiQ is composed of 1 protein: AbiQ.
@@ -38,6 +58,18 @@ The system was detected in 111 different species.
Proportion of genome encoding the AbiQ system for the 14 phyla with more than 50 genomes in the RefSeq database.
+## Structure
+### Experimentally determined structure
+
+From :ref{doi=10.1111/mmi.12129} in *Lactococcus lactis*:
+
+::molstar-pdbe-plugin
+---
+height: 700
+dataUrl: /abiq/4glk_LlAbiQ_1mer.cif
+---
+::
+
## Structure
### AbiQ
diff --git a/public/abiq/4glk_LlAbiQ_1mer.cif b/public/abiq/4glk_LlAbiQ_1mer.cif
new file mode 100644
index 0000000000000000000000000000000000000000..bdb30bc57f46d14e1030127b4a07615d946dc588
--- /dev/null
+++ b/public/abiq/4glk_LlAbiQ_1mer.cif
@@ -0,0 +1,5005 @@
+data_4GLK
+#
+_entry.id 4GLK
+#
+_audit_conform.dict_name mmcif_pdbx.dic
+_audit_conform.dict_version 5.379
+_audit_conform.dict_location http://mmcif.pdb.org/dictionaries/ascii/mmcif_pdbx.dic
+#
+loop_
+_database_2.database_id
+_database_2.database_code
+_database_2.pdbx_database_accession
+_database_2.pdbx_DOI
+PDB 4GLK pdb_00004glk 10.2210/pdb4glk/pdb
+RCSB RCSB074335 ? ?
+WWPDB D_1000074335 ? ?
+#
+_pdbx_database_status.status_code REL
+_pdbx_database_status.entry_id 4GLK
+_pdbx_database_status.recvd_initial_deposition_date 2012-08-14
+_pdbx_database_status.deposit_site RCSB
+_pdbx_database_status.process_site RCSB
+_pdbx_database_status.status_code_sf REL
+_pdbx_database_status.status_code_mr ?
+_pdbx_database_status.SG_entry ?
+_pdbx_database_status.status_code_cs ?
+_pdbx_database_status.methods_development_category ?
+_pdbx_database_status.pdb_format_compatible Y
+_pdbx_database_status.status_code_nmr_data ?
+#
+loop_
+_audit_author.name
+_audit_author.pdbx_ordinal
+'Samson, J.' 1
+'Spinelli, S.' 2
+'Cambillau, C.' 3
+'Moineau, S.' 4
+#
+_citation.id primary
+_citation.title
+'Structure and activity of AbiQ, a lactococcal endoribonuclease belonging to the type III toxin-antitoxin system.'
+_citation.journal_abbrev Mol.Microbiol.
+_citation.journal_volume 87
+_citation.page_first 756
+_citation.page_last 768
+_citation.year 2013
+_citation.journal_id_ASTM MOMIEE
+_citation.country UK
+_citation.journal_id_ISSN 0950-382X
+_citation.journal_id_CSD 2007
+_citation.book_publisher ?
+_citation.pdbx_database_id_PubMed 23279123
+_citation.pdbx_database_id_DOI 10.1111/mmi.12129
+#
+loop_
+_citation_author.citation_id
+_citation_author.name
+_citation_author.ordinal
+_citation_author.identifier_ORCID
+primary 'Samson, J.E.' 1 ?
+primary 'Spinelli, S.' 2 ?
+primary 'Cambillau, C.' 3 ?
+primary 'Moineau, S.' 4 ?
+#
+_cell.entry_id 4GLK
+_cell.length_a 50.140
+_cell.length_b 54.510
+_cell.length_c 64.240
+_cell.angle_alpha 90.00
+_cell.angle_beta 90.00
+_cell.angle_gamma 90.00
+_cell.Z_PDB 4
+_cell.pdbx_unique_axis ?
+_cell.length_a_esd ?
+_cell.length_b_esd ?
+_cell.length_c_esd ?
+_cell.angle_alpha_esd ?
+_cell.angle_beta_esd ?
+_cell.angle_gamma_esd ?
+#
+_symmetry.entry_id 4GLK
+_symmetry.space_group_name_H-M 'P 21 21 21'
+_symmetry.pdbx_full_space_group_name_H-M ?
+_symmetry.cell_setting ?
+_symmetry.Int_Tables_number 19
+_symmetry.space_group_name_Hall ?
+#
+loop_
+_entity.id
+_entity.type
+_entity.src_method
+_entity.pdbx_description
+_entity.formula_weight
+_entity.pdbx_number_of_molecules
+_entity.pdbx_ec
+_entity.pdbx_mutation
+_entity.pdbx_fragment
+_entity.details
+1 polymer man AbiQ 20308.732 1 3.1.-.- S51L 'UNP residues 13-183' ?
+2 non-polymer syn GLYCEROL 92.094 3 ? ? ? ?
+3 water nat water 18.015 69 ? ? ? ?
+#
+_entity_poly.entity_id 1
+_entity_poly.type 'polypeptide(L)'
+_entity_poly.nstd_linkage no
+_entity_poly.nstd_monomer no
+_entity_poly.pdbx_seq_one_letter_code
+;GTLRFFTVTDEYIAYLRKFESKVHYQYENNASTYVGVVLKKNDFNYFIPLLSYKKGNPEKDKAMKKRSRIVTRLFEIGNI
+NNPLGYLLHHNMIPVPDSELIPLPLDLKKPKHKMMQKQLIYMKSISEKIENKSEVVYRKAAHEKDGYYLKFSCDFKLLEA
+KATLYSKKSTFQ
+;
+_entity_poly.pdbx_seq_one_letter_code_can
+;GTLRFFTVTDEYIAYLRKFESKVHYQYENNASTYVGVVLKKNDFNYFIPLLSYKKGNPEKDKAMKKRSRIVTRLFEIGNI
+NNPLGYLLHHNMIPVPDSELIPLPLDLKKPKHKMMQKQLIYMKSISEKIENKSEVVYRKAAHEKDGYYLKFSCDFKLLEA
+KATLYSKKSTFQ
+;
+_entity_poly.pdbx_strand_id A
+_entity_poly.pdbx_target_identifier ?
+#
+loop_
+_entity_poly_seq.entity_id
+_entity_poly_seq.num
+_entity_poly_seq.mon_id
+_entity_poly_seq.hetero
+1 1 GLY n
+1 2 THR n
+1 3 LEU n
+1 4 ARG n
+1 5 PHE n
+1 6 PHE n
+1 7 THR n
+1 8 VAL n
+1 9 THR n
+1 10 ASP n
+1 11 GLU n
+1 12 TYR n
+1 13 ILE n
+1 14 ALA n
+1 15 TYR n
+1 16 LEU n
+1 17 ARG n
+1 18 LYS n
+1 19 PHE n
+1 20 GLU n
+1 21 SER n
+1 22 LYS n
+1 23 VAL n
+1 24 HIS n
+1 25 TYR n
+1 26 GLN n
+1 27 TYR n
+1 28 GLU n
+1 29 ASN n
+1 30 ASN n
+1 31 ALA n
+1 32 SER n
+1 33 THR n
+1 34 TYR n
+1 35 VAL n
+1 36 GLY n
+1 37 VAL n
+1 38 VAL n
+1 39 LEU n
+1 40 LYS n
+1 41 LYS n
+1 42 ASN n
+1 43 ASP n
+1 44 PHE n
+1 45 ASN n
+1 46 TYR n
+1 47 PHE n
+1 48 ILE n
+1 49 PRO n
+1 50 LEU n
+1 51 LEU n
+1 52 SER n
+1 53 TYR n
+1 54 LYS n
+1 55 LYS n
+1 56 GLY n
+1 57 ASN n
+1 58 PRO n
+1 59 GLU n
+1 60 LYS n
+1 61 ASP n
+1 62 LYS n
+1 63 ALA n
+1 64 MET n
+1 65 LYS n
+1 66 LYS n
+1 67 ARG n
+1 68 SER n
+1 69 ARG n
+1 70 ILE n
+1 71 VAL n
+1 72 THR n
+1 73 ARG n
+1 74 LEU n
+1 75 PHE n
+1 76 GLU n
+1 77 ILE n
+1 78 GLY n
+1 79 ASN n
+1 80 ILE n
+1 81 ASN n
+1 82 ASN n
+1 83 PRO n
+1 84 LEU n
+1 85 GLY n
+1 86 TYR n
+1 87 LEU n
+1 88 LEU n
+1 89 HIS n
+1 90 HIS n
+1 91 ASN n
+1 92 MET n
+1 93 ILE n
+1 94 PRO n
+1 95 VAL n
+1 96 PRO n
+1 97 ASP n
+1 98 SER n
+1 99 GLU n
+1 100 LEU n
+1 101 ILE n
+1 102 PRO n
+1 103 LEU n
+1 104 PRO n
+1 105 LEU n
+1 106 ASP n
+1 107 LEU n
+1 108 LYS n
+1 109 LYS n
+1 110 PRO n
+1 111 LYS n
+1 112 HIS n
+1 113 LYS n
+1 114 MET n
+1 115 MET n
+1 116 GLN n
+1 117 LYS n
+1 118 GLN n
+1 119 LEU n
+1 120 ILE n
+1 121 TYR n
+1 122 MET n
+1 123 LYS n
+1 124 SER n
+1 125 ILE n
+1 126 SER n
+1 127 GLU n
+1 128 LYS n
+1 129 ILE n
+1 130 GLU n
+1 131 ASN n
+1 132 LYS n
+1 133 SER n
+1 134 GLU n
+1 135 VAL n
+1 136 VAL n
+1 137 TYR n
+1 138 ARG n
+1 139 LYS n
+1 140 ALA n
+1 141 ALA n
+1 142 HIS n
+1 143 GLU n
+1 144 LYS n
+1 145 ASP n
+1 146 GLY n
+1 147 TYR n
+1 148 TYR n
+1 149 LEU n
+1 150 LYS n
+1 151 PHE n
+1 152 SER n
+1 153 CYS n
+1 154 ASP n
+1 155 PHE n
+1 156 LYS n
+1 157 LEU n
+1 158 LEU n
+1 159 GLU n
+1 160 ALA n
+1 161 LYS n
+1 162 ALA n
+1 163 THR n
+1 164 LEU n
+1 165 TYR n
+1 166 SER n
+1 167 LYS n
+1 168 LYS n
+1 169 SER n
+1 170 THR n
+1 171 PHE n
+1 172 GLN n
+#
+_entity_src_gen.entity_id 1
+_entity_src_gen.pdbx_src_id 1
+_entity_src_gen.pdbx_alt_source_flag sample
+_entity_src_gen.pdbx_seq_type ?
+_entity_src_gen.pdbx_beg_seq_num ?
+_entity_src_gen.pdbx_end_seq_num ?
+_entity_src_gen.gene_src_common_name ?
+_entity_src_gen.gene_src_genus ?
+_entity_src_gen.pdbx_gene_src_gene abiQ
+_entity_src_gen.gene_src_species ?
+_entity_src_gen.gene_src_strain ?
+_entity_src_gen.gene_src_tissue ?
+_entity_src_gen.gene_src_tissue_fraction ?
+_entity_src_gen.gene_src_details ?
+_entity_src_gen.pdbx_gene_src_fragment ?
+_entity_src_gen.pdbx_gene_src_scientific_name 'Lactococcus lactis'
+_entity_src_gen.pdbx_gene_src_ncbi_taxonomy_id 1358
+_entity_src_gen.pdbx_gene_src_variant ?
+_entity_src_gen.pdbx_gene_src_cell_line ?
+_entity_src_gen.pdbx_gene_src_atcc ?
+_entity_src_gen.pdbx_gene_src_organ ?
+_entity_src_gen.pdbx_gene_src_organelle ?
+_entity_src_gen.pdbx_gene_src_cell ?
+_entity_src_gen.pdbx_gene_src_cellular_location ?
+_entity_src_gen.host_org_common_name ?
+_entity_src_gen.pdbx_host_org_scientific_name 'Escherichia coli'
+_entity_src_gen.pdbx_host_org_ncbi_taxonomy_id 83333
+_entity_src_gen.host_org_genus ?
+_entity_src_gen.pdbx_host_org_gene ?
+_entity_src_gen.pdbx_host_org_organ ?
+_entity_src_gen.host_org_species ?
+_entity_src_gen.pdbx_host_org_tissue ?
+_entity_src_gen.pdbx_host_org_tissue_fraction ?
+_entity_src_gen.pdbx_host_org_strain K12
+_entity_src_gen.pdbx_host_org_variant ?
+_entity_src_gen.pdbx_host_org_cell_line ?
+_entity_src_gen.pdbx_host_org_atcc ?
+_entity_src_gen.pdbx_host_org_culture_collection ?
+_entity_src_gen.pdbx_host_org_cell ?
+_entity_src_gen.pdbx_host_org_organelle ?
+_entity_src_gen.pdbx_host_org_cellular_location ?
+_entity_src_gen.pdbx_host_org_vector_type plasmid
+_entity_src_gen.pdbx_host_org_vector ?
+_entity_src_gen.host_org_details ?
+_entity_src_gen.expression_system_id ?
+_entity_src_gen.plasmid_name pDEST17
+_entity_src_gen.plasmid_details ?
+_entity_src_gen.pdbx_description ?
+#
+_struct_ref.id 1
+_struct_ref.db_name UNP
+_struct_ref.db_code Q9ZJ19_9LACT
+_struct_ref.pdbx_db_accession Q9ZJ19
+_struct_ref.entity_id 1
+_struct_ref.pdbx_seq_one_letter_code
+;TLRFFTVTDEYIAYLRKFESKVHYQYENNASTYVGVVLKKNDFNYFIPLSSYKKGNPEKDKAMKKRSRIVTRLFEIGNIN
+NPLGYLLHHNMIPVPDSELIPLPLDLKKPKHKMMQKQLIYMKSISEKIENKSEVVYRKAAHEKDGYYLKFSCDFKLLEAK
+ATLYSKKSTFQ
+;
+_struct_ref.pdbx_align_begin 13
+_struct_ref.pdbx_db_isoform ?
+#
+_struct_ref_seq.align_id 1
+_struct_ref_seq.ref_id 1
+_struct_ref_seq.pdbx_PDB_id_code 4GLK
+_struct_ref_seq.pdbx_strand_id A
+_struct_ref_seq.seq_align_beg 2
+_struct_ref_seq.pdbx_seq_align_beg_ins_code ?
+_struct_ref_seq.seq_align_end 172
+_struct_ref_seq.pdbx_seq_align_end_ins_code ?
+_struct_ref_seq.pdbx_db_accession Q9ZJ19
+_struct_ref_seq.db_align_beg 13
+_struct_ref_seq.pdbx_db_align_beg_ins_code ?
+_struct_ref_seq.db_align_end 183
+_struct_ref_seq.pdbx_db_align_end_ins_code ?
+_struct_ref_seq.pdbx_auth_seq_align_beg 2
+_struct_ref_seq.pdbx_auth_seq_align_end 172
+#
+loop_
+_struct_ref_seq_dif.align_id
+_struct_ref_seq_dif.pdbx_pdb_id_code
+_struct_ref_seq_dif.mon_id
+_struct_ref_seq_dif.pdbx_pdb_strand_id
+_struct_ref_seq_dif.seq_num
+_struct_ref_seq_dif.pdbx_pdb_ins_code
+_struct_ref_seq_dif.pdbx_seq_db_name
+_struct_ref_seq_dif.pdbx_seq_db_accession_code
+_struct_ref_seq_dif.db_mon_id
+_struct_ref_seq_dif.pdbx_seq_db_seq_num
+_struct_ref_seq_dif.details
+_struct_ref_seq_dif.pdbx_auth_seq_num
+_struct_ref_seq_dif.pdbx_ordinal
+1 4GLK GLY A 1 ? UNP Q9ZJ19 ? ? 'expression tag' 1 1
+1 4GLK LEU A 51 ? UNP Q9ZJ19 SER 62 'engineered mutation' 51 2
+#
+loop_
+_chem_comp.id
+_chem_comp.type
+_chem_comp.mon_nstd_flag
+_chem_comp.name
+_chem_comp.pdbx_synonyms
+_chem_comp.formula
+_chem_comp.formula_weight
+ALA 'L-peptide linking' y ALANINE ? 'C3 H7 N O2' 89.093
+ARG 'L-peptide linking' y ARGININE ? 'C6 H15 N4 O2 1' 175.209
+ASN 'L-peptide linking' y ASPARAGINE ? 'C4 H8 N2 O3' 132.118
+ASP 'L-peptide linking' y 'ASPARTIC ACID' ? 'C4 H7 N O4' 133.103
+CYS 'L-peptide linking' y CYSTEINE ? 'C3 H7 N O2 S' 121.158
+GLN 'L-peptide linking' y GLUTAMINE ? 'C5 H10 N2 O3' 146.144
+GLU 'L-peptide linking' y 'GLUTAMIC ACID' ? 'C5 H9 N O4' 147.129
+GLY 'peptide linking' y GLYCINE ? 'C2 H5 N O2' 75.067
+GOL non-polymer . GLYCEROL 'GLYCERIN; PROPANE-1,2,3-TRIOL' 'C3 H8 O3' 92.094
+HIS 'L-peptide linking' y HISTIDINE ? 'C6 H10 N3 O2 1' 156.162
+HOH non-polymer . WATER ? 'H2 O' 18.015
+ILE 'L-peptide linking' y ISOLEUCINE ? 'C6 H13 N O2' 131.173
+LEU 'L-peptide linking' y LEUCINE ? 'C6 H13 N O2' 131.173
+LYS 'L-peptide linking' y LYSINE ? 'C6 H15 N2 O2 1' 147.195
+MET 'L-peptide linking' y METHIONINE ? 'C5 H11 N O2 S' 149.211
+PHE 'L-peptide linking' y PHENYLALANINE ? 'C9 H11 N O2' 165.189
+PRO 'L-peptide linking' y PROLINE ? 'C5 H9 N O2' 115.130
+SER 'L-peptide linking' y SERINE ? 'C3 H7 N O3' 105.093
+THR 'L-peptide linking' y THREONINE ? 'C4 H9 N O3' 119.119
+TYR 'L-peptide linking' y TYROSINE ? 'C9 H11 N O3' 181.189
+VAL 'L-peptide linking' y VALINE ? 'C5 H11 N O2' 117.146
+#
+_exptl.entry_id 4GLK
+_exptl.method 'X-RAY DIFFRACTION'
+_exptl.crystals_number 1
+#
+_exptl_crystal.id 1
+_exptl_crystal.density_meas ?
+_exptl_crystal.density_Matthews 2.16
+_exptl_crystal.density_percent_sol 43.09
+_exptl_crystal.description ?
+_exptl_crystal.F_000 ?
+_exptl_crystal.preparation ?
+#
+_exptl_crystal_grow.crystal_id 1
+_exptl_crystal_grow.method 'VAPOR DIFFUSION, SITTING DROP'
+_exptl_crystal_grow.temp 293
+_exptl_crystal_grow.temp_details ?
+_exptl_crystal_grow.pH 6.0
+_exptl_crystal_grow.pdbx_details
+;buffer: 1 M potassium/sodium tartrate, 0.1 M MES, pH 6.0, drop: 200 nL 4.6 mg/mL protein + 100 nL buffer, VAPOR DIFFUSION, SITTING DROP, temperature 293K
+;
+_exptl_crystal_grow.pdbx_pH_range ?
+#
+_diffrn.id 1
+_diffrn.ambient_temp 100
+_diffrn.ambient_temp_details ?
+_diffrn.crystal_id 1
+#
+_diffrn_detector.diffrn_id 1
+_diffrn_detector.detector PIXEL
+_diffrn_detector.type 'PSI PILATUS 6M'
+_diffrn_detector.pdbx_collection_date 2011-10-14
+_diffrn_detector.details ?
+#
+_diffrn_radiation.diffrn_id 1
+_diffrn_radiation.wavelength_id 1
+_diffrn_radiation.pdbx_monochromatic_or_laue_m_l M
+_diffrn_radiation.monochromator 'channel cut Si(111)'
+_diffrn_radiation.pdbx_diffrn_protocol 'SINGLE WAVELENGTH'
+_diffrn_radiation.pdbx_scattering_type x-ray
+#
+_diffrn_radiation_wavelength.id 1
+_diffrn_radiation_wavelength.wavelength 0.9791
+_diffrn_radiation_wavelength.wt 1.0
+#
+_diffrn_source.diffrn_id 1
+_diffrn_source.source SYNCHROTRON
+_diffrn_source.type 'SOLEIL BEAMLINE PROXIMA 1'
+_diffrn_source.pdbx_synchrotron_site SOLEIL
+_diffrn_source.pdbx_synchrotron_beamline 'PROXIMA 1'
+_diffrn_source.pdbx_wavelength ?
+_diffrn_source.pdbx_wavelength_list 0.9791
+#
+_reflns.entry_id 4GLK
+_reflns.observed_criterion_sigma_I 0
+_reflns.observed_criterion_sigma_F 0
+_reflns.d_resolution_low 45
+_reflns.d_resolution_high 2.16
+_reflns.number_obs 9880
+_reflns.number_all 9880
+_reflns.percent_possible_obs 99.7
+_reflns.pdbx_Rmerge_I_obs 0.090
+_reflns.pdbx_Rsym_value ?
+_reflns.pdbx_netI_over_sigmaI 17.1
+_reflns.B_iso_Wilson_estimate 35.49
+_reflns.pdbx_redundancy 13.7
+_reflns.R_free_details ?
+_reflns.limit_h_max ?
+_reflns.limit_h_min ?
+_reflns.limit_k_max ?
+_reflns.limit_k_min ?
+_reflns.limit_l_max ?
+_reflns.limit_l_min ?
+_reflns.observed_criterion_F_max ?
+_reflns.observed_criterion_F_min ?
+_reflns.pdbx_chi_squared ?
+_reflns.pdbx_scaling_rejects ?
+_reflns.pdbx_ordinal 1
+_reflns.pdbx_diffrn_id 1
+#
+_reflns_shell.d_res_high 2.16
+_reflns_shell.d_res_low 2.22
+_reflns_shell.percent_possible_all 99.6
+_reflns_shell.Rmerge_I_obs 0.6
+_reflns_shell.pdbx_Rsym_value ?
+_reflns_shell.meanI_over_sigI_obs 3.7
+_reflns_shell.pdbx_redundancy 13.1
+_reflns_shell.percent_possible_obs ?
+_reflns_shell.number_unique_all 753
+_reflns_shell.number_measured_all ?
+_reflns_shell.number_measured_obs ?
+_reflns_shell.number_unique_obs ?
+_reflns_shell.pdbx_chi_squared ?
+_reflns_shell.pdbx_ordinal 1
+_reflns_shell.pdbx_diffrn_id 1
+#
+_refine.entry_id 4GLK
+_refine.ls_number_reflns_obs 9880
+_refine.ls_number_reflns_all 9880
+_refine.pdbx_ls_sigma_I ?
+_refine.pdbx_ls_sigma_F 0.0
+_refine.pdbx_data_cutoff_high_absF ?
+_refine.pdbx_data_cutoff_low_absF ?
+_refine.pdbx_data_cutoff_high_rms_absF ?
+_refine.ls_d_res_low 27.67
+_refine.ls_d_res_high 2.16
+_refine.ls_percent_reflns_obs ?
+_refine.ls_R_factor_obs 0.1958
+_refine.ls_R_factor_all 0.1958
+_refine.ls_R_factor_R_work 0.1937
+_refine.ls_R_factor_R_free 0.2232
+_refine.ls_R_factor_R_free_error ?
+_refine.ls_R_factor_R_free_error_details ?
+_refine.ls_percent_reflns_R_free 7.02
+_refine.ls_number_reflns_R_free 694
+_refine.ls_number_parameters ?
+_refine.ls_number_restraints ?
+_refine.occupancy_min ?
+_refine.occupancy_max ?
+_refine.correlation_coeff_Fo_to_Fc 0.9300
+_refine.correlation_coeff_Fo_to_Fc_free 0.9239
+_refine.B_iso_mean 38.47
+_refine.aniso_B[1][1] 6.2090
+_refine.aniso_B[2][2] 5.4018
+_refine.aniso_B[3][3] -11.6108
+_refine.aniso_B[1][2] 0.0000
+_refine.aniso_B[1][3] 0.0000
+_refine.aniso_B[2][3] 0.0000
+_refine.solvent_model_details ?
+_refine.solvent_model_param_ksol ?
+_refine.solvent_model_param_bsol ?
+_refine.pdbx_solvent_vdw_probe_radii ?
+_refine.pdbx_solvent_ion_probe_radii ?
+_refine.pdbx_solvent_shrinkage_radii ?
+_refine.pdbx_ls_cross_valid_method THROUGHOUT
+_refine.details ?
+_refine.pdbx_starting_model 'PDB ENTRY 2XDD'
+_refine.pdbx_method_to_determine_struct 'MOLECULAR REPLACEMENT'
+_refine.pdbx_isotropic_thermal_model ?
+_refine.pdbx_stereochemistry_target_values 'Engh & Huber'
+_refine.pdbx_stereochem_target_val_spec_case ?
+_refine.pdbx_R_Free_selection_details RANDOM
+_refine.pdbx_overall_ESU_R ?
+_refine.pdbx_overall_ESU_R_Free ?
+_refine.overall_SU_ML ?
+_refine.pdbx_overall_phase_error ?
+_refine.overall_SU_B ?
+_refine.overall_SU_R_Cruickshank_DPI ?
+_refine.ls_redundancy_reflns_obs ?
+_refine.B_iso_min ?
+_refine.B_iso_max ?
+_refine.overall_SU_R_free ?
+_refine.ls_wR_factor_R_free ?
+_refine.ls_wR_factor_R_work ?
+_refine.overall_FOM_free_R_set ?
+_refine.overall_FOM_work_R_set ?
+_refine.pdbx_diffrn_id 1
+_refine.pdbx_refine_id 'X-RAY DIFFRACTION'
+_refine.pdbx_TLS_residual_ADP_flag ?
+_refine.pdbx_overall_SU_R_free_Cruickshank_DPI ?
+_refine.pdbx_overall_SU_R_Blow_DPI ?
+_refine.pdbx_overall_SU_R_free_Blow_DPI ?
+#
+_refine_analyze.entry_id 4GLK
+_refine_analyze.Luzzati_coordinate_error_obs 0.272
+_refine_analyze.Luzzati_sigma_a_obs ?
+_refine_analyze.Luzzati_d_res_low_obs ?
+_refine_analyze.Luzzati_coordinate_error_free ?
+_refine_analyze.Luzzati_sigma_a_free ?
+_refine_analyze.Luzzati_d_res_low_free ?
+_refine_analyze.number_disordered_residues ?
+_refine_analyze.occupancy_sum_hydrogen ?
+_refine_analyze.occupancy_sum_non_hydrogen ?
+_refine_analyze.pdbx_Luzzati_d_res_high_obs ?
+_refine_analyze.pdbx_refine_id 'X-RAY DIFFRACTION'
+#
+_refine_hist.pdbx_refine_id 'X-RAY DIFFRACTION'
+_refine_hist.cycle_id LAST
+_refine_hist.pdbx_number_atoms_protein 1353
+_refine_hist.pdbx_number_atoms_nucleic_acid 0
+_refine_hist.pdbx_number_atoms_ligand 18
+_refine_hist.number_atoms_solvent 69
+_refine_hist.number_atoms_total 1440
+_refine_hist.d_res_high 2.16
+_refine_hist.d_res_low 27.67
+#
+loop_
+_refine_ls_restr.type
+_refine_ls_restr.dev_ideal
+_refine_ls_restr.dev_ideal_target
+_refine_ls_restr.weight
+_refine_ls_restr.number
+_refine_ls_restr.pdbx_restraint_function
+_refine_ls_restr.pdbx_refine_id
+t_bond_d 0.009 ? 2.00 1397 HARMONIC 'X-RAY DIFFRACTION'
+t_angle_deg 1.18 ? 2.00 1876 HARMONIC 'X-RAY DIFFRACTION'
+t_dihedral_angle_d 0 ? 2.00 493 SINUSOIDAL 'X-RAY DIFFRACTION'
+t_trig_c_planes 0 ? 2.00 28 HARMONIC 'X-RAY DIFFRACTION'
+t_gen_planes 0 ? 5.00 195 HARMONIC 'X-RAY DIFFRACTION'
+t_it 0 ? 20.00 1397 HARMONIC 'X-RAY DIFFRACTION'
+t_omega_torsion 3.77 ? ? ? ? 'X-RAY DIFFRACTION'
+t_other_torsion 23.96 ? ? ? ? 'X-RAY DIFFRACTION'
+t_chiral_improper_torsion 0 ? 5.00 177 SEMIHARMONIC 'X-RAY DIFFRACTION'
+t_ideal_dist_contact 0 ? 4.00 1651 SEMIHARMONIC 'X-RAY DIFFRACTION'
+#
+_refine_ls_shell.pdbx_total_number_of_bins_used 5
+_refine_ls_shell.d_res_high 2.16
+_refine_ls_shell.d_res_low 2.42
+_refine_ls_shell.number_reflns_R_work 2561
+_refine_ls_shell.R_factor_R_work 0.2274
+_refine_ls_shell.percent_reflns_obs ?
+_refine_ls_shell.R_factor_R_free 0.3178
+_refine_ls_shell.R_factor_R_free_error ?
+_refine_ls_shell.percent_reflns_R_free 6.33
+_refine_ls_shell.number_reflns_R_free 173
+_refine_ls_shell.number_reflns_all 2734
+_refine_ls_shell.R_factor_all 0.2327
+_refine_ls_shell.number_reflns_obs 2734
+_refine_ls_shell.redundancy_reflns_obs ?
+_refine_ls_shell.pdbx_refine_id 'X-RAY DIFFRACTION'
+#
+_struct.entry_id 4GLK
+_struct.title
+'Structure and activity of AbiQ, a lactococcal anti-phage endoribonuclease belonging to the type-III toxin-antitoxin system'
+_struct.pdbx_model_details ?
+_struct.pdbx_CASP_flag ?
+_struct.pdbx_model_type_details ?
+#
+_struct_keywords.entry_id 4GLK
+_struct_keywords.pdbx_keywords HYDROLASE
+_struct_keywords.text 'Alpha Beta, endonuclease, RNA antiQ, HYDROLASE'
+#
+loop_
+_struct_asym.id
+_struct_asym.pdbx_blank_PDB_chainid_flag
+_struct_asym.pdbx_modified
+_struct_asym.entity_id
+_struct_asym.details
+A N N 1 ?
+B N N 2 ?
+C N N 2 ?
+D N N 2 ?
+E N N 3 ?
+#
+_struct_biol.id 1
+_struct_biol.details ?
+#
+loop_
+_struct_conf.conf_type_id
+_struct_conf.id
+_struct_conf.pdbx_PDB_helix_id
+_struct_conf.beg_label_comp_id
+_struct_conf.beg_label_asym_id
+_struct_conf.beg_label_seq_id
+_struct_conf.pdbx_beg_PDB_ins_code
+_struct_conf.end_label_comp_id
+_struct_conf.end_label_asym_id
+_struct_conf.end_label_seq_id
+_struct_conf.pdbx_end_PDB_ins_code
+_struct_conf.beg_auth_comp_id
+_struct_conf.beg_auth_asym_id
+_struct_conf.beg_auth_seq_id
+_struct_conf.end_auth_comp_id
+_struct_conf.end_auth_asym_id
+_struct_conf.end_auth_seq_id
+_struct_conf.pdbx_PDB_helix_class
+_struct_conf.details
+_struct_conf.pdbx_PDB_helix_length
+HELX_P HELX_P1 1 THR A 9 ? ARG A 17 ? THR A 9 ARG A 17 1 ? 9
+HELX_P HELX_P2 2 PRO A 58 ? ARG A 67 ? PRO A 58 ARG A 67 1 ? 10
+HELX_P HELX_P3 3 HIS A 90 ? MET A 92 ? HIS A 90 MET A 92 5 ? 3
+HELX_P HELX_P4 4 PRO A 96 ? SER A 98 ? PRO A 96 SER A 98 5 ? 3
+HELX_P HELX_P5 5 LYS A 109 ? ILE A 125 ? LYS A 109 ILE A 125 1 ? 17
+HELX_P HELX_P6 6 ILE A 125 ? HIS A 142 ? ILE A 125 HIS A 142 1 ? 18
+HELX_P HELX_P7 7 ASP A 145 ? SER A 152 ? ASP A 145 SER A 152 1 ? 8
+HELX_P HELX_P8 8 ASP A 154 ? LYS A 167 ? ASP A 154 LYS A 167 1 ? 14
+#
+_struct_conf_type.id HELX_P
+_struct_conf_type.criteria ?
+_struct_conf_type.reference ?
+#
+loop_
+_struct_mon_prot_cis.pdbx_id
+_struct_mon_prot_cis.label_comp_id
+_struct_mon_prot_cis.label_seq_id
+_struct_mon_prot_cis.label_asym_id
+_struct_mon_prot_cis.label_alt_id
+_struct_mon_prot_cis.pdbx_PDB_ins_code
+_struct_mon_prot_cis.auth_comp_id
+_struct_mon_prot_cis.auth_seq_id
+_struct_mon_prot_cis.auth_asym_id
+_struct_mon_prot_cis.pdbx_label_comp_id_2
+_struct_mon_prot_cis.pdbx_label_seq_id_2
+_struct_mon_prot_cis.pdbx_label_asym_id_2
+_struct_mon_prot_cis.pdbx_PDB_ins_code_2
+_struct_mon_prot_cis.pdbx_auth_comp_id_2
+_struct_mon_prot_cis.pdbx_auth_seq_id_2
+_struct_mon_prot_cis.pdbx_auth_asym_id_2
+_struct_mon_prot_cis.pdbx_PDB_model_num
+_struct_mon_prot_cis.pdbx_omega_angle
+1 GLY 36 A . ? GLY 36 A VAL 37 A ? VAL 37 A 1 -1.47
+2 LYS 41 A . ? LYS 41 A ASN 42 A ? ASN 42 A 1 -5.24
+#
+loop_
+_struct_sheet.id
+_struct_sheet.type
+_struct_sheet.number_strands
+_struct_sheet.details
+A ? 4 ?
+B ? 6 ?
+#
+loop_
+_struct_sheet_order.sheet_id
+_struct_sheet_order.range_id_1
+_struct_sheet_order.range_id_2
+_struct_sheet_order.offset
+_struct_sheet_order.sense
+A 1 2 ? anti-parallel
+A 2 3 ? anti-parallel
+A 3 4 ? anti-parallel
+B 1 2 ? anti-parallel
+B 2 3 ? anti-parallel
+B 3 4 ? anti-parallel
+B 4 5 ? anti-parallel
+B 5 6 ? anti-parallel
+#
+loop_
+_struct_sheet_range.sheet_id
+_struct_sheet_range.id
+_struct_sheet_range.beg_label_comp_id
+_struct_sheet_range.beg_label_asym_id
+_struct_sheet_range.beg_label_seq_id
+_struct_sheet_range.pdbx_beg_PDB_ins_code
+_struct_sheet_range.end_label_comp_id
+_struct_sheet_range.end_label_asym_id
+_struct_sheet_range.end_label_seq_id
+_struct_sheet_range.pdbx_end_PDB_ins_code
+_struct_sheet_range.beg_auth_comp_id
+_struct_sheet_range.beg_auth_asym_id
+_struct_sheet_range.beg_auth_seq_id
+_struct_sheet_range.end_auth_comp_id
+_struct_sheet_range.end_auth_asym_id
+_struct_sheet_range.end_auth_seq_id
+A 1 VAL A 71 ? GLU A 76 ? VAL A 71 GLU A 76
+A 2 ASN A 79 ? LEU A 88 ? ASN A 79 LEU A 88
+A 3 ASN A 45 ? SER A 52 ? ASN A 45 SER A 52
+A 4 ILE A 93 ? PRO A 94 ? ILE A 93 PRO A 94
+B 1 VAL A 71 ? GLU A 76 ? VAL A 71 GLU A 76
+B 2 ASN A 79 ? LEU A 88 ? ASN A 79 LEU A 88
+B 3 ASN A 45 ? SER A 52 ? ASN A 45 SER A 52
+B 4 THR A 33 ? LYS A 40 ? THR A 33 LYS A 40
+B 5 ARG A 4 ? VAL A 8 ? ARG A 4 VAL A 8
+B 6 LEU A 100 ? PRO A 102 ? LEU A 100 PRO A 102
+#
+loop_
+_pdbx_struct_sheet_hbond.sheet_id
+_pdbx_struct_sheet_hbond.range_id_1
+_pdbx_struct_sheet_hbond.range_id_2
+_pdbx_struct_sheet_hbond.range_1_label_atom_id
+_pdbx_struct_sheet_hbond.range_1_label_comp_id
+_pdbx_struct_sheet_hbond.range_1_label_asym_id
+_pdbx_struct_sheet_hbond.range_1_label_seq_id
+_pdbx_struct_sheet_hbond.range_1_PDB_ins_code
+_pdbx_struct_sheet_hbond.range_1_auth_atom_id
+_pdbx_struct_sheet_hbond.range_1_auth_comp_id
+_pdbx_struct_sheet_hbond.range_1_auth_asym_id
+_pdbx_struct_sheet_hbond.range_1_auth_seq_id
+_pdbx_struct_sheet_hbond.range_2_label_atom_id
+_pdbx_struct_sheet_hbond.range_2_label_comp_id
+_pdbx_struct_sheet_hbond.range_2_label_asym_id
+_pdbx_struct_sheet_hbond.range_2_label_seq_id
+_pdbx_struct_sheet_hbond.range_2_PDB_ins_code
+_pdbx_struct_sheet_hbond.range_2_auth_atom_id
+_pdbx_struct_sheet_hbond.range_2_auth_comp_id
+_pdbx_struct_sheet_hbond.range_2_auth_asym_id
+_pdbx_struct_sheet_hbond.range_2_auth_seq_id
+A 1 2 N LEU A 74 ? N LEU A 74 O GLY A 85 ? O GLY A 85
+A 2 3 O TYR A 86 ? O TYR A 86 N LEU A 51 ? N LEU A 51
+A 3 4 N PHE A 47 ? N PHE A 47 O ILE A 93 ? O ILE A 93
+B 1 2 N LEU A 74 ? N LEU A 74 O GLY A 85 ? O GLY A 85
+B 2 3 O TYR A 86 ? O TYR A 86 N LEU A 51 ? N LEU A 51
+B 3 4 O LEU A 50 ? O LEU A 50 N THR A 33 ? N THR A 33
+B 4 5 O TYR A 34 ? O TYR A 34 N PHE A 6 ? N PHE A 6
+B 5 6 N THR A 7 ? N THR A 7 O ILE A 101 ? O ILE A 101
+#
+loop_
+_struct_site.id
+_struct_site.pdbx_evidence_code
+_struct_site.pdbx_auth_asym_id
+_struct_site.pdbx_auth_comp_id
+_struct_site.pdbx_auth_seq_id
+_struct_site.pdbx_auth_ins_code
+_struct_site.pdbx_num_residues
+_struct_site.details
+AC1 Software A GOL 201 ? 6 'BINDING SITE FOR RESIDUE GOL A 201'
+AC2 Software A GOL 202 ? 7 'BINDING SITE FOR RESIDUE GOL A 202'
+AC3 Software A GOL 203 ? 9 'BINDING SITE FOR RESIDUE GOL A 203'
+#
+loop_
+_struct_site_gen.id
+_struct_site_gen.site_id
+_struct_site_gen.pdbx_num_res
+_struct_site_gen.label_comp_id
+_struct_site_gen.label_asym_id
+_struct_site_gen.label_seq_id
+_struct_site_gen.pdbx_auth_ins_code
+_struct_site_gen.auth_comp_id
+_struct_site_gen.auth_asym_id
+_struct_site_gen.auth_seq_id
+_struct_site_gen.label_atom_id
+_struct_site_gen.label_alt_id
+_struct_site_gen.symmetry
+_struct_site_gen.details
+1 AC1 6 ARG A 73 ? ARG A 73 . ? 3_544 ?
+2 AC1 6 PHE A 75 ? PHE A 75 . ? 3_544 ?
+3 AC1 6 ASP A 97 ? ASP A 97 . ? 1_555 ?
+4 AC1 6 TYR A 121 ? TYR A 121 . ? 3_544 ?
+5 AC1 6 LYS A 128 ? LYS A 128 . ? 3_544 ?
+6 AC1 6 GOL D . ? GOL A 203 . ? 1_555 ?
+7 AC2 7 LEU A 3 ? LEU A 3 . ? 1_555 ?
+8 AC2 7 ARG A 4 ? ARG A 4 . ? 1_555 ?
+9 AC2 7 ARG A 69 ? ARG A 69 . ? 3_544 ?
+10 AC2 7 LEU A 119 ? LEU A 119 . ? 1_555 ?
+11 AC2 7 LYS A 123 ? LYS A 123 . ? 1_555 ?
+12 AC2 7 LYS A 139 ? LYS A 139 . ? 3_544 ?
+13 AC2 7 TYR A 148 ? TYR A 148 . ? 3_544 ?
+14 AC3 9 ARG A 4 ? ARG A 4 . ? 1_555 ?
+15 AC3 9 PHE A 6 ? PHE A 6 . ? 1_555 ?
+16 AC3 9 SER A 68 ? SER A 68 . ? 3_544 ?
+17 AC3 9 PRO A 102 ? PRO A 102 . ? 1_555 ?
+18 AC3 9 LYS A 128 ? LYS A 128 . ? 3_544 ?
+19 AC3 9 LYS A 132 ? LYS A 132 . ? 3_544 ?
+20 AC3 9 GOL B . ? GOL A 201 . ? 1_555 ?
+21 AC3 9 HOH E . ? HOH A 346 . ? 3_544 ?
+22 AC3 9 HOH E . ? HOH A 368 . ? 1_555 ?
+#
+_database_PDB_matrix.entry_id 4GLK
+_database_PDB_matrix.origx[1][1] 1.000000
+_database_PDB_matrix.origx[1][2] 0.000000
+_database_PDB_matrix.origx[1][3] 0.000000
+_database_PDB_matrix.origx[2][1] 0.000000
+_database_PDB_matrix.origx[2][2] 1.000000
+_database_PDB_matrix.origx[2][3] 0.000000
+_database_PDB_matrix.origx[3][1] 0.000000
+_database_PDB_matrix.origx[3][2] 0.000000
+_database_PDB_matrix.origx[3][3] 1.000000
+_database_PDB_matrix.origx_vector[1] 0.00000
+_database_PDB_matrix.origx_vector[2] 0.00000
+_database_PDB_matrix.origx_vector[3] 0.00000
+#
+_atom_sites.entry_id 4GLK
+_atom_sites.fract_transf_matrix[1][1] 0.019944
+_atom_sites.fract_transf_matrix[1][2] 0.000000
+_atom_sites.fract_transf_matrix[1][3] 0.000000
+_atom_sites.fract_transf_matrix[2][1] 0.000000
+_atom_sites.fract_transf_matrix[2][2] 0.018345
+_atom_sites.fract_transf_matrix[2][3] 0.000000
+_atom_sites.fract_transf_matrix[3][1] 0.000000
+_atom_sites.fract_transf_matrix[3][2] 0.000000
+_atom_sites.fract_transf_matrix[3][3] 0.015567
+_atom_sites.fract_transf_vector[1] 0.00000
+_atom_sites.fract_transf_vector[2] 0.00000
+_atom_sites.fract_transf_vector[3] 0.00000
+#
+loop_
+_atom_type.symbol
+C
+N
+O
+S
+#
+loop_
+_atom_site.group_PDB
+_atom_site.id
+_atom_site.type_symbol
+_atom_site.label_atom_id
+_atom_site.label_alt_id
+_atom_site.label_comp_id
+_atom_site.label_asym_id
+_atom_site.label_entity_id
+_atom_site.label_seq_id
+_atom_site.pdbx_PDB_ins_code
+_atom_site.Cartn_x
+_atom_site.Cartn_y
+_atom_site.Cartn_z
+_atom_site.occupancy
+_atom_site.B_iso_or_equiv
+_atom_site.pdbx_formal_charge
+_atom_site.auth_seq_id
+_atom_site.auth_comp_id
+_atom_site.auth_asym_id
+_atom_site.auth_atom_id
+_atom_site.pdbx_PDB_model_num
+ATOM 1 N N . GLY A 1 1 ? 9.477 14.555 -21.103 1.00 45.02 ? 1 GLY A N 1
+ATOM 2 C CA . GLY A 1 1 ? 8.332 13.887 -20.463 1.00 44.15 ? 1 GLY A CA 1
+ATOM 3 C C . GLY A 1 1 ? 6.973 14.426 -20.962 1.00 44.59 ? 1 GLY A C 1
+ATOM 4 O O . GLY A 1 1 ? 6.854 15.624 -21.216 1.00 44.94 ? 1 GLY A O 1
+ATOM 5 N N . THR A 1 2 ? 5.967 13.536 -21.128 1.00 36.69 ? 2 THR A N 1
+ATOM 6 C CA . THR A 1 2 ? 4.661 13.867 -21.718 1.00 34.73 ? 2 THR A CA 1
+ATOM 7 C C . THR A 1 2 ? 3.439 13.896 -20.794 1.00 31.36 ? 2 THR A C 1
+ATOM 8 O O . THR A 1 2 ? 3.265 13.005 -19.975 1.00 30.54 ? 2 THR A O 1
+ATOM 9 C CB . THR A 1 2 ? 4.363 12.946 -22.904 1.00 45.87 ? 2 THR A CB 1
+ATOM 10 O OG1 . THR A 1 2 ? 5.516 12.172 -23.220 1.00 51.22 ? 2 THR A OG1 1
+ATOM 11 C CG2 . THR A 1 2 ? 3.906 13.705 -24.121 1.00 46.46 ? 2 THR A CG2 1
+ATOM 12 N N . LEU A 1 3 ? 2.546 14.869 -21.012 1.00 23.44 ? 3 LEU A N 1
+ATOM 13 C CA . LEU A 1 3 ? 1.274 14.987 -20.293 1.00 23.27 ? 3 LEU A CA 1
+ATOM 14 C C . LEU A 1 3 ? 0.305 13.847 -20.734 1.00 26.84 ? 3 LEU A C 1
+ATOM 15 O O . LEU A 1 3 ? 0.192 13.558 -21.925 1.00 24.69 ? 3 LEU A O 1
+ATOM 16 C CB . LEU A 1 3 ? 0.654 16.362 -20.614 1.00 23.46 ? 3 LEU A CB 1
+ATOM 17 C CG . LEU A 1 3 ? 0.573 17.442 -19.537 1.00 27.43 ? 3 LEU A CG 1
+ATOM 18 C CD1 . LEU A 1 3 ? 1.602 17.280 -18.450 1.00 24.00 ? 3 LEU A CD1 1
+ATOM 19 C CD2 . LEU A 1 3 ? 0.657 18.841 -20.167 1.00 27.60 ? 3 LEU A CD2 1
+ATOM 20 N N . ARG A 1 4 ? -0.374 13.209 -19.769 1.00 23.86 ? 4 ARG A N 1
+ATOM 21 C CA . ARG A 1 4 ? -1.301 12.108 -20.014 1.00 23.17 ? 4 ARG A CA 1
+ATOM 22 C C . ARG A 1 4 ? -2.410 12.169 -19.017 1.00 26.70 ? 4 ARG A C 1
+ATOM 23 O O . ARG A 1 4 ? -2.252 12.813 -17.986 1.00 26.16 ? 4 ARG A O 1
+ATOM 24 C CB . ARG A 1 4 ? -0.586 10.775 -19.767 1.00 27.58 ? 4 ARG A CB 1
+ATOM 25 C CG . ARG A 1 4 ? 0.120 10.203 -20.934 1.00 38.23 ? 4 ARG A CG 1
+ATOM 26 C CD . ARG A 1 4 ? 1.584 10.198 -20.670 1.00 50.31 ? 4 ARG A CD 1
+ATOM 27 N NE . ARG A 1 4 ? 2.000 9.141 -19.752 1.00 52.89 ? 4 ARG A NE 1
+ATOM 28 C CZ . ARG A 1 4 ? 3.200 9.104 -19.185 1.00 62.15 ? 4 ARG A CZ 1
+ATOM 29 N NH1 . ARG A 1 4 ? 4.078 10.070 -19.423 1.00 44.53 ? 4 ARG A NH1 1
+ATOM 30 N NH2 . ARG A 1 4 ? 3.534 8.112 -18.384 1.00 51.55 ? 4 ARG A NH2 1
+ATOM 31 N N . PHE A 1 5 ? -3.464 11.359 -19.233 1.00 24.17 ? 5 PHE A N 1
+ATOM 32 C CA . PHE A 1 5 ? -4.600 11.260 -18.321 1.00 23.28 ? 5 PHE A CA 1
+ATOM 33 C C . PHE A 1 5 ? -4.413 10.114 -17.360 1.00 24.76 ? 5 PHE A C 1
+ATOM 34 O O . PHE A 1 5 ? -3.959 9.030 -17.734 1.00 23.20 ? 5 PHE A O 1
+ATOM 35 C CB . PHE A 1 5 ? -5.929 11.097 -19.077 1.00 24.73 ? 5 PHE A CB 1
+ATOM 36 C CG . PHE A 1 5 ? -6.450 12.308 -19.819 1.00 26.01 ? 5 PHE A CG 1
+ATOM 37 C CD1 . PHE A 1 5 ? -6.764 13.477 -19.140 1.00 29.23 ? 5 PHE A CD1 1
+ATOM 38 C CD2 . PHE A 1 5 ? -6.708 12.249 -21.183 1.00 27.72 ? 5 PHE A CD2 1
+ATOM 39 C CE1 . PHE A 1 5 ? -7.314 14.571 -19.810 1.00 30.18 ? 5 PHE A CE1 1
+ATOM 40 C CE2 . PHE A 1 5 ? -7.221 13.358 -21.862 1.00 31.28 ? 5 PHE A CE2 1
+ATOM 41 C CZ . PHE A 1 5 ? -7.530 14.511 -21.166 1.00 29.52 ? 5 PHE A CZ 1
+ATOM 42 N N . PHE A 1 6 ? -4.788 10.346 -16.117 1.00 20.14 ? 6 PHE A N 1
+ATOM 43 C CA . PHE A 1 6 ? -4.671 9.322 -15.092 1.00 19.13 ? 6 PHE A CA 1
+ATOM 44 C C . PHE A 1 6 ? -5.832 9.422 -14.160 1.00 25.86 ? 6 PHE A C 1
+ATOM 45 O O . PHE A 1 6 ? -6.516 10.457 -14.100 1.00 25.25 ? 6 PHE A O 1
+ATOM 46 C CB . PHE A 1 6 ? -3.414 9.560 -14.232 1.00 20.33 ? 6 PHE A CB 1
+ATOM 47 C CG . PHE A 1 6 ? -2.090 9.414 -14.936 1.00 22.64 ? 6 PHE A CG 1
+ATOM 48 C CD1 . PHE A 1 6 ? -1.475 8.171 -15.046 1.00 26.24 ? 6 PHE A CD1 1
+ATOM 49 C CD2 . PHE A 1 6 ? -1.439 10.521 -15.455 1.00 25.31 ? 6 PHE A CD2 1
+ATOM 50 C CE1 . PHE A 1 6 ? -0.256 8.035 -15.716 1.00 27.75 ? 6 PHE A CE1 1
+ATOM 51 C CE2 . PHE A 1 6 ? -0.221 10.383 -16.121 1.00 29.27 ? 6 PHE A CE2 1
+ATOM 52 C CZ . PHE A 1 6 ? 0.373 9.143 -16.228 1.00 27.20 ? 6 PHE A CZ 1
+ATOM 53 N N . THR A 1 7 ? -6.001 8.353 -13.373 1.00 22.22 ? 7 THR A N 1
+ATOM 54 C CA . THR A 1 7 ? -6.870 8.319 -12.226 1.00 22.10 ? 7 THR A CA 1
+ATOM 55 C C . THR A 1 7 ? -5.931 7.938 -11.093 1.00 23.88 ? 7 THR A C 1
+ATOM 56 O O . THR A 1 7 ? -4.779 7.535 -11.321 1.00 20.45 ? 7 THR A O 1
+ATOM 57 C CB . THR A 1 7 ? -8.109 7.400 -12.381 1.00 34.21 ? 7 THR A CB 1
+ATOM 58 O OG1 . THR A 1 7 ? -7.721 6.036 -12.493 1.00 36.06 ? 7 THR A OG1 1
+ATOM 59 C CG2 . THR A 1 7 ? -9.055 7.832 -13.525 1.00 32.36 ? 7 THR A CG2 1
+ATOM 60 N N . VAL A 1 8 ? -6.393 8.132 -9.871 1.00 20.60 ? 8 VAL A N 1
+ATOM 61 C CA . VAL A 1 8 ? -5.622 7.801 -8.686 1.00 20.85 ? 8 VAL A CA 1
+ATOM 62 C C . VAL A 1 8 ? -6.446 6.754 -7.937 1.00 27.29 ? 8 VAL A C 1
+ATOM 63 O O . VAL A 1 8 ? -7.681 6.736 -8.082 1.00 26.59 ? 8 VAL A O 1
+ATOM 64 C CB . VAL A 1 8 ? -5.299 9.069 -7.836 1.00 24.37 ? 8 VAL A CB 1
+ATOM 65 C CG1 . VAL A 1 8 ? -4.390 8.728 -6.652 1.00 24.12 ? 8 VAL A CG1 1
+ATOM 66 C CG2 . VAL A 1 8 ? -4.643 10.152 -8.697 1.00 24.32 ? 8 VAL A CG2 1
+ATOM 67 N N . THR A 1 9 ? -5.785 5.835 -7.192 1.00 25.02 ? 9 THR A N 1
+ATOM 68 C CA . THR A 1 9 ? -6.536 4.818 -6.445 1.00 24.53 ? 9 THR A CA 1
+ATOM 69 C C . THR A 1 9 ? -7.430 5.509 -5.397 1.00 29.56 ? 9 THR A C 1
+ATOM 70 O O . THR A 1 9 ? -7.002 6.490 -4.769 1.00 28.31 ? 9 THR A O 1
+ATOM 71 C CB . THR A 1 9 ? -5.604 3.806 -5.744 1.00 31.00 ? 9 THR A CB 1
+ATOM 72 O OG1 . THR A 1 9 ? -4.808 4.482 -4.784 1.00 27.91 ? 9 THR A OG1 1
+ATOM 73 C CG2 . THR A 1 9 ? -4.718 3.026 -6.706 1.00 27.47 ? 9 THR A CG2 1
+ATOM 74 N N . ASP A 1 10 ? -8.662 4.989 -5.215 1.00 27.34 ? 10 ASP A N 1
+ATOM 75 C CA . ASP A 1 10 ? -9.639 5.463 -4.236 1.00 27.13 ? 10 ASP A CA 1
+ATOM 76 C C . ASP A 1 10 ? -9.026 5.400 -2.846 1.00 31.98 ? 10 ASP A C 1
+ATOM 77 O O . ASP A 1 10 ? -9.254 6.300 -2.038 1.00 31.69 ? 10 ASP A O 1
+ATOM 78 C CB . ASP A 1 10 ? -10.939 4.626 -4.317 1.00 29.54 ? 10 ASP A CB 1
+ATOM 79 C CG . ASP A 1 10 ? -11.775 4.806 -5.598 1.00 37.50 ? 10 ASP A CG 1
+ATOM 80 O OD1 . ASP A 1 10 ? -11.738 5.915 -6.191 1.00 38.07 ? 10 ASP A OD1 1
+ATOM 81 O OD2 . ASP A 1 10 ? -12.502 3.851 -5.980 1.00 39.07 ? 10 ASP A OD2 1
+ATOM 82 N N . GLU A 1 11 ? -8.164 4.379 -2.601 1.00 29.93 ? 11 GLU A N 1
+ATOM 83 C CA . GLU A 1 11 ? -7.471 4.159 -1.328 1.00 29.92 ? 11 GLU A CA 1
+ATOM 84 C C . GLU A 1 11 ? -6.492 5.292 -1.008 1.00 31.17 ? 11 GLU A C 1
+ATOM 85 O O . GLU A 1 11 ? -6.560 5.869 0.081 1.00 30.85 ? 11 GLU A O 1
+ATOM 86 C CB . GLU A 1 11 ? -6.789 2.778 -1.304 1.00 32.14 ? 11 GLU A CB 1
+ATOM 87 C CG . GLU A 1 11 ? -7.773 1.607 -1.340 1.00 49.33 ? 11 GLU A CG 1
+ATOM 88 C CD . GLU A 1 11 ? -8.182 1.040 -2.695 1.00 77.24 ? 11 GLU A CD 1
+ATOM 89 O OE1 . GLU A 1 11 ? -8.407 -0.191 -2.766 1.00 84.75 ? 11 GLU A OE1 1
+ATOM 90 O OE2 . GLU A 1 11 ? -8.300 1.813 -3.676 1.00 64.11 ? 11 GLU A OE2 1
+ATOM 91 N N . TYR A 1 12 ? -5.607 5.642 -1.970 1.00 26.84 ? 12 TYR A N 1
+ATOM 92 C CA . TYR A 1 12 ? -4.670 6.746 -1.815 1.00 24.85 ? 12 TYR A CA 1
+ATOM 93 C C . TYR A 1 12 ? -5.398 8.094 -1.640 1.00 28.54 ? 12 TYR A C 1
+ATOM 94 O O . TYR A 1 12 ? -4.977 8.903 -0.814 1.00 29.35 ? 12 TYR A O 1
+ATOM 95 C CB . TYR A 1 12 ? -3.730 6.844 -3.014 1.00 24.77 ? 12 TYR A CB 1
+ATOM 96 C CG . TYR A 1 12 ? -2.693 7.917 -2.805 1.00 24.92 ? 12 TYR A CG 1
+ATOM 97 C CD1 . TYR A 1 12 ? -1.761 7.830 -1.776 1.00 26.86 ? 12 TYR A CD1 1
+ATOM 98 C CD2 . TYR A 1 12 ? -2.696 9.071 -3.590 1.00 25.16 ? 12 TYR A CD2 1
+ATOM 99 C CE1 . TYR A 1 12 ? -0.812 8.825 -1.568 1.00 27.39 ? 12 TYR A CE1 1
+ATOM 100 C CE2 . TYR A 1 12 ? -1.755 10.079 -3.388 1.00 25.45 ? 12 TYR A CE2 1
+ATOM 101 C CZ . TYR A 1 12 ? -0.816 9.951 -2.376 1.00 30.57 ? 12 TYR A CZ 1
+ATOM 102 O OH . TYR A 1 12 ? 0.112 10.928 -2.162 1.00 27.30 ? 12 TYR A OH 1
+ATOM 103 N N . ILE A 1 13 ? -6.460 8.350 -2.431 1.00 24.53 ? 13 ILE A N 1
+ATOM 104 C CA . ILE A 1 13 ? -7.242 9.596 -2.315 1.00 23.75 ? 13 ILE A CA 1
+ATOM 105 C C . ILE A 1 13 ? -7.894 9.694 -0.933 1.00 28.12 ? 13 ILE A C 1
+ATOM 106 O O . ILE A 1 13 ? -7.778 10.739 -0.284 1.00 28.66 ? 13 ILE A O 1
+ATOM 107 C CB . ILE A 1 13 ? -8.265 9.726 -3.480 1.00 25.78 ? 13 ILE A CB 1
+ATOM 108 C CG1 . ILE A 1 13 ? -7.531 9.891 -4.835 1.00 24.78 ? 13 ILE A CG1 1
+ATOM 109 C CG2 . ILE A 1 13 ? -9.293 10.855 -3.243 1.00 25.42 ? 13 ILE A CG2 1
+ATOM 110 C CD1 . ILE A 1 13 ? -6.712 11.221 -5.055 1.00 24.90 ? 13 ILE A CD1 1
+ATOM 111 N N . ALA A 1 14 ? -8.529 8.591 -0.467 1.00 23.95 ? 14 ALA A N 1
+ATOM 112 C CA . ALA A 1 14 ? -9.180 8.537 0.848 1.00 24.90 ? 14 ALA A CA 1
+ATOM 113 C C . ALA A 1 14 ? -8.154 8.808 1.938 1.00 31.37 ? 14 ALA A C 1
+ATOM 114 O O . ALA A 1 14 ? -8.482 9.474 2.909 1.00 31.72 ? 14 ALA A O 1
+ATOM 115 C CB . ALA A 1 14 ? -9.855 7.187 1.075 1.00 25.55 ? 14 ALA A CB 1
+ATOM 116 N N . TYR A 1 15 ? -6.902 8.350 1.735 1.00 28.74 ? 15 TYR A N 1
+ATOM 117 C CA . TYR A 1 15 ? -5.797 8.562 2.657 1.00 29.68 ? 15 TYR A CA 1
+ATOM 118 C C . TYR A 1 15 ? -5.358 10.036 2.696 1.00 35.87 ? 15 TYR A C 1
+ATOM 119 O O . TYR A 1 15 ? -5.130 10.557 3.789 1.00 35.98 ? 15 TYR A O 1
+ATOM 120 C CB . TYR A 1 15 ? -4.638 7.623 2.337 1.00 30.80 ? 15 TYR A CB 1
+ATOM 121 C CG . TYR A 1 15 ? -3.338 7.964 3.035 1.00 33.41 ? 15 TYR A CG 1
+ATOM 122 C CD1 . TYR A 1 15 ? -3.070 7.494 4.323 1.00 35.45 ? 15 TYR A CD1 1
+ATOM 123 C CD2 . TYR A 1 15 ? -2.339 8.677 2.379 1.00 34.35 ? 15 TYR A CD2 1
+ATOM 124 C CE1 . TYR A 1 15 ? -1.842 7.738 4.939 1.00 34.98 ? 15 TYR A CE1 1
+ATOM 125 C CE2 . TYR A 1 15 ? -1.110 8.923 2.981 1.00 35.65 ? 15 TYR A CE2 1
+ATOM 126 C CZ . TYR A 1 15 ? -0.868 8.462 4.265 1.00 41.05 ? 15 TYR A CZ 1
+ATOM 127 O OH . TYR A 1 15 ? 0.341 8.741 4.845 1.00 38.51 ? 15 TYR A OH 1
+ATOM 128 N N . LEU A 1 16 ? -5.218 10.699 1.519 1.00 31.19 ? 16 LEU A N 1
+ATOM 129 C CA . LEU A 1 16 ? -4.839 12.114 1.487 1.00 30.58 ? 16 LEU A CA 1
+ATOM 130 C C . LEU A 1 16 ? -5.933 12.978 2.100 1.00 33.42 ? 16 LEU A C 1
+ATOM 131 O O . LEU A 1 16 ? -5.607 13.932 2.794 1.00 32.31 ? 16 LEU A O 1
+ATOM 132 C CB . LEU A 1 16 ? -4.508 12.631 0.080 1.00 30.30 ? 16 LEU A CB 1
+ATOM 133 C CG . LEU A 1 16 ? -3.253 12.127 -0.616 1.00 35.51 ? 16 LEU A CG 1
+ATOM 134 C CD1 . LEU A 1 16 ? -2.997 12.940 -1.864 1.00 35.67 ? 16 LEU A CD1 1
+ATOM 135 C CD2 . LEU A 1 16 ? -2.014 12.184 0.296 1.00 39.06 ? 16 LEU A CD2 1
+ATOM 136 N N . ARG A 1 17 ? -7.219 12.633 1.859 1.00 30.45 ? 17 ARG A N 1
+ATOM 137 C CA . ARG A 1 17 ? -8.372 13.374 2.385 1.00 30.61 ? 17 ARG A CA 1
+ATOM 138 C C . ARG A 1 17 ? -8.493 13.311 3.921 1.00 36.82 ? 17 ARG A C 1
+ATOM 139 O O . ARG A 1 17 ? -9.235 14.108 4.500 1.00 36.88 ? 17 ARG A O 1
+ATOM 140 C CB . ARG A 1 17 ? -9.686 13.002 1.677 1.00 29.88 ? 17 ARG A CB 1
+ATOM 141 C CG . ARG A 1 17 ? -9.700 13.331 0.190 1.00 34.23 ? 17 ARG A CG 1
+ATOM 142 C CD . ARG A 1 17 ? -11.064 13.170 -0.448 1.00 37.08 ? 17 ARG A CD 1
+ATOM 143 N NE . ARG A 1 17 ? -11.812 14.432 -0.380 1.00 49.59 ? 17 ARG A NE 1
+ATOM 144 C CZ . ARG A 1 17 ? -12.852 14.633 0.414 1.00 58.10 ? 17 ARG A CZ 1
+ATOM 145 N NH1 . ARG A 1 17 ? -13.320 13.663 1.178 1.00 42.52 ? 17 ARG A NH1 1
+ATOM 146 N NH2 . ARG A 1 17 ? -13.451 15.821 0.431 1.00 54.34 ? 17 ARG A NH2 1
+ATOM 147 N N . LYS A 1 18 ? -7.748 12.389 4.584 1.00 35.30 ? 18 LYS A N 1
+ATOM 148 C CA . LYS A 1 18 ? -7.642 12.330 6.050 1.00 36.08 ? 18 LYS A CA 1
+ATOM 149 C C . LYS A 1 18 ? -6.984 13.627 6.567 1.00 40.39 ? 18 LYS A C 1
+ATOM 150 O O . LYS A 1 18 ? -7.371 14.136 7.610 1.00 40.26 ? 18 LYS A O 1
+ATOM 151 C CB . LYS A 1 18 ? -6.733 11.171 6.478 1.00 39.46 ? 18 LYS A CB 1
+ATOM 152 C CG . LYS A 1 18 ? -7.448 9.873 6.794 1.00 56.13 ? 18 LYS A CG 1
+ATOM 153 C CD . LYS A 1 18 ? -6.594 8.646 6.461 1.00 64.11 ? 18 LYS A CD 1
+ATOM 154 C CE . LYS A 1 18 ? -7.378 7.678 5.582 1.00 64.62 ? 18 LYS A CE 1
+ATOM 155 N NZ . LYS A 1 18 ? -6.738 6.336 5.466 1.00 53.70 ? 18 LYS A NZ 1
+ATOM 156 N N . PHE A 1 19 ? -5.990 14.142 5.811 1.00 35.94 ? 19 PHE A N 1
+ATOM 157 C CA . PHE A 1 19 ? -5.151 15.306 6.155 1.00 35.29 ? 19 PHE A CA 1
+ATOM 158 C C . PHE A 1 19 ? -5.482 16.581 5.377 1.00 37.12 ? 19 PHE A C 1
+ATOM 159 O O . PHE A 1 19 ? -5.313 17.666 5.925 1.00 36.90 ? 19 PHE A O 1
+ATOM 160 C CB . PHE A 1 19 ? -3.668 14.954 5.974 1.00 37.36 ? 19 PHE A CB 1
+ATOM 161 C CG . PHE A 1 19 ? -3.286 13.579 6.473 1.00 39.34 ? 19 PHE A CG 1
+ATOM 162 C CD1 . PHE A 1 19 ? -3.075 13.345 7.829 1.00 43.08 ? 19 PHE A CD1 1
+ATOM 163 C CD2 . PHE A 1 19 ? -3.133 12.519 5.589 1.00 41.82 ? 19 PHE A CD2 1
+ATOM 164 C CE1 . PHE A 1 19 ? -2.719 12.071 8.288 1.00 44.58 ? 19 PHE A CE1 1
+ATOM 165 C CE2 . PHE A 1 19 ? -2.791 11.242 6.053 1.00 45.06 ? 19 PHE A CE2 1
+ATOM 166 C CZ . PHE A 1 19 ? -2.573 11.030 7.398 1.00 43.22 ? 19 PHE A CZ 1
+ATOM 167 N N . GLU A 1 20 ? -5.965 16.458 4.118 1.00 31.58 ? 20 GLU A N 1
+ATOM 168 C CA . GLU A 1 20 ? -6.324 17.589 3.270 1.00 29.89 ? 20 GLU A CA 1
+ATOM 169 C C . GLU A 1 20 ? -7.703 17.417 2.615 1.00 32.77 ? 20 GLU A C 1
+ATOM 170 O O . GLU A 1 20 ? -7.817 16.728 1.607 1.00 31.65 ? 20 GLU A O 1
+ATOM 171 C CB . GLU A 1 20 ? -5.213 17.859 2.223 1.00 30.77 ? 20 GLU A CB 1
+ATOM 172 C CG . GLU A 1 20 ? -5.397 19.131 1.398 1.00 37.26 ? 20 GLU A CG 1
+ATOM 173 C CD . GLU A 1 20 ? -5.612 20.406 2.196 1.00 54.27 ? 20 GLU A CD 1
+ATOM 174 O OE1 . GLU A 1 20 ? -4.605 21.036 2.594 1.00 42.04 ? 20 GLU A OE1 1
+ATOM 175 O OE2 . GLU A 1 20 ? -6.786 20.752 2.463 1.00 43.78 ? 20 GLU A OE2 1
+ATOM 176 N N . SER A 1 21 ? -8.732 18.106 3.151 1.00 30.59 ? 21 SER A N 1
+ATOM 177 C CA . SER A 1 21 ? -10.123 18.079 2.651 1.00 30.25 ? 21 SER A CA 1
+ATOM 178 C C . SER A 1 21 ? -10.275 18.727 1.260 1.00 33.69 ? 21 SER A C 1
+ATOM 179 O O . SER A 1 21 ? -11.316 18.562 0.603 1.00 32.05 ? 21 SER A O 1
+ATOM 180 C CB . SER A 1 21 ? -11.064 18.784 3.628 1.00 35.05 ? 21 SER A CB 1
+ATOM 181 O OG . SER A 1 21 ? -10.580 18.819 4.960 1.00 50.41 ? 21 SER A OG 1
+ATOM 182 N N . LYS A 1 22 ? -9.254 19.504 0.830 1.00 29.29 ? 22 LYS A N 1
+ATOM 183 C CA . LYS A 1 22 ? -9.273 20.178 -0.462 1.00 28.20 ? 22 LYS A CA 1
+ATOM 184 C C . LYS A 1 22 ? -9.049 19.191 -1.596 1.00 32.06 ? 22 LYS A C 1
+ATOM 185 O O . LYS A 1 22 ? -9.376 19.494 -2.750 1.00 31.86 ? 22 LYS A O 1
+ATOM 186 C CB . LYS A 1 22 ? -8.228 21.294 -0.495 1.00 29.98 ? 22 LYS A CB 1
+ATOM 187 C CG . LYS A 1 22 ? -8.693 22.544 0.224 1.00 25.22 ? 22 LYS A CG 1
+ATOM 188 C CD . LYS A 1 22 ? -7.581 23.569 0.303 1.00 18.26 ? 22 LYS A CD 1
+ATOM 189 C CE . LYS A 1 22 ? -7.932 24.615 1.350 1.00 28.11 ? 22 LYS A CE 1
+ATOM 190 N NZ . LYS A 1 22 ? -6.786 25.525 1.620 1.00 48.85 ? 22 LYS A NZ 1
+ATOM 191 N N . VAL A 1 23 ? -8.454 18.020 -1.267 1.00 27.20 ? 23 VAL A N 1
+ATOM 192 C CA . VAL A 1 23 ? -8.189 16.935 -2.225 1.00 26.14 ? 23 VAL A CA 1
+ATOM 193 C C . VAL A 1 23 ? -9.560 16.496 -2.765 1.00 29.75 ? 23 VAL A C 1
+ATOM 194 O O . VAL A 1 23 ? -10.494 16.317 -1.982 1.00 29.00 ? 23 VAL A O 1
+ATOM 195 C CB . VAL A 1 23 ? -7.390 15.766 -1.569 1.00 27.80 ? 23 VAL A CB 1
+ATOM 196 C CG1 . VAL A 1 23 ? -7.296 14.551 -2.500 1.00 26.72 ? 23 VAL A CG1 1
+ATOM 197 C CG2 . VAL A 1 23 ? -5.998 16.230 -1.149 1.00 27.17 ? 23 VAL A CG2 1
+ATOM 198 N N . HIS A 1 24 ? -9.690 16.407 -4.089 1.00 28.27 ? 24 HIS A N 1
+ATOM 199 C CA . HIS A 1 24 ? -10.953 16.074 -4.749 1.00 28.43 ? 24 HIS A CA 1
+ATOM 200 C C . HIS A 1 24 ? -11.534 14.770 -4.319 1.00 29.22 ? 24 HIS A C 1
+ATOM 201 O O . HIS A 1 24 ? -10.827 13.761 -4.267 1.00 27.26 ? 24 HIS A O 1
+ATOM 202 C CB . HIS A 1 24 ? -10.832 16.139 -6.283 1.00 30.57 ? 24 HIS A CB 1
+ATOM 203 C CG . HIS A 1 24 ? -10.906 17.533 -6.843 1.00 34.58 ? 24 HIS A CG 1
+ATOM 204 N ND1 . HIS A 1 24 ? -11.597 17.801 -8.004 1.00 36.62 ? 24 HIS A ND1 1
+ATOM 205 C CD2 . HIS A 1 24 ? -10.362 18.684 -6.379 1.00 36.29 ? 24 HIS A CD2 1
+ATOM 206 C CE1 . HIS A 1 24 ? -11.458 19.096 -8.214 1.00 36.26 ? 24 HIS A CE1 1
+ATOM 207 N NE2 . HIS A 1 24 ? -10.714 19.669 -7.264 1.00 36.43 ? 24 HIS A NE2 1
+ATOM 208 N N . TYR A 1 25 ? -12.824 14.798 -3.956 1.00 25.36 ? 25 TYR A N 1
+ATOM 209 C CA . TYR A 1 25 ? -13.517 13.594 -3.576 1.00 25.30 ? 25 TYR A CA 1
+ATOM 210 C C . TYR A 1 25 ? -13.668 12.709 -4.799 1.00 30.80 ? 25 TYR A C 1
+ATOM 211 O O . TYR A 1 25 ? -13.934 13.197 -5.905 1.00 29.43 ? 25 TYR A O 1
+ATOM 212 C CB . TYR A 1 25 ? -14.917 13.884 -2.969 1.00 26.11 ? 25 TYR A CB 1
+ATOM 213 C CG . TYR A 1 25 ? -15.643 12.605 -2.616 1.00 26.46 ? 25 TYR A CG 1
+ATOM 214 C CD1 . TYR A 1 25 ? -15.349 11.916 -1.446 1.00 28.74 ? 25 TYR A CD1 1
+ATOM 215 C CD2 . TYR A 1 25 ? -16.505 11.997 -3.529 1.00 26.50 ? 25 TYR A CD2 1
+ATOM 216 C CE1 . TYR A 1 25 ? -15.937 10.682 -1.164 1.00 29.11 ? 25 TYR A CE1 1
+ATOM 217 C CE2 . TYR A 1 25 ? -17.089 10.761 -3.262 1.00 26.58 ? 25 TYR A CE2 1
+ATOM 218 C CZ . TYR A 1 25 ? -16.813 10.116 -2.072 1.00 32.44 ? 25 TYR A CZ 1
+ATOM 219 O OH . TYR A 1 25 ? -17.424 8.925 -1.778 1.00 30.65 ? 25 TYR A OH 1
+ATOM 220 N N . GLN A 1 26 ? -13.484 11.404 -4.586 1.00 28.78 ? 26 GLN A N 1
+ATOM 221 C CA . GLN A 1 26 ? -13.729 10.403 -5.602 1.00 29.99 ? 26 GLN A CA 1
+ATOM 222 C C . GLN A 1 26 ? -14.082 9.061 -4.971 1.00 41.75 ? 26 GLN A C 1
+ATOM 223 O O . GLN A 1 26 ? -13.688 8.792 -3.835 1.00 42.86 ? 26 GLN A O 1
+ATOM 224 C CB . GLN A 1 26 ? -12.536 10.246 -6.562 1.00 30.43 ? 26 GLN A CB 1
+ATOM 225 C CG . GLN A 1 26 ? -11.379 9.482 -5.936 1.00 27.26 ? 26 GLN A CG 1
+ATOM 226 C CD . GLN A 1 26 ? -10.285 9.191 -6.898 1.00 36.11 ? 26 GLN A CD 1
+ATOM 227 O OE1 . GLN A 1 26 ? -9.679 10.098 -7.460 1.00 32.58 ? 26 GLN A OE1 1
+ATOM 228 N NE2 . GLN A 1 26 ? -9.936 7.922 -7.004 1.00 21.83 ? 26 GLN A NE2 1
+ATOM 229 N N . TYR A 1 27 ? -14.808 8.227 -5.726 1.00 42.51 ? 27 TYR A N 1
+ATOM 230 C CA . TYR A 1 27 ? -15.122 6.832 -5.439 1.00 45.32 ? 27 TYR A CA 1
+ATOM 231 C C . TYR A 1 27 ? -15.716 6.164 -6.658 1.00 53.03 ? 27 TYR A C 1
+ATOM 232 O O . TYR A 1 27 ? -16.593 6.749 -7.284 1.00 53.44 ? 27 TYR A O 1
+ATOM 233 C CB . TYR A 1 27 ? -16.003 6.603 -4.199 1.00 48.20 ? 27 TYR A CB 1
+ATOM 234 C CG . TYR A 1 27 ? -15.839 5.179 -3.697 1.00 51.90 ? 27 TYR A CG 1
+ATOM 235 C CD1 . TYR A 1 27 ? -14.721 4.804 -2.957 1.00 53.81 ? 27 TYR A CD1 1
+ATOM 236 C CD2 . TYR A 1 27 ? -16.743 4.182 -4.063 1.00 53.11 ? 27 TYR A CD2 1
+ATOM 237 C CE1 . TYR A 1 27 ? -14.515 3.480 -2.576 1.00 54.58 ? 27 TYR A CE1 1
+ATOM 238 C CE2 . TYR A 1 27 ? -16.566 2.861 -3.654 1.00 54.08 ? 27 TYR A CE2 1
+ATOM 239 C CZ . TYR A 1 27 ? -15.443 2.512 -2.924 1.00 61.83 ? 27 TYR A CZ 1
+ATOM 240 O OH . TYR A 1 27 ? -15.257 1.212 -2.522 1.00 63.01 ? 27 TYR A OH 1
+ATOM 241 N N . GLU A 1 28 ? -15.226 4.953 -7.007 1.00 52.13 ? 28 GLU A N 1
+ATOM 242 C CA . GLU A 1 28 ? -15.682 4.142 -8.147 1.00 53.55 ? 28 GLU A CA 1
+ATOM 243 C C . GLU A 1 28 ? -16.039 4.941 -9.418 1.00 61.26 ? 28 GLU A C 1
+ATOM 244 O O . GLU A 1 28 ? -15.145 5.182 -10.227 1.00 62.63 ? 28 GLU A O 1
+ATOM 245 C CB . GLU A 1 28 ? -16.798 3.190 -7.719 1.00 55.11 ? 28 GLU A CB 1
+ATOM 246 C CG . GLU A 1 28 ? -16.268 1.835 -7.286 1.00 69.20 ? 28 GLU A CG 1
+ATOM 247 C CD . GLU A 1 28 ? -17.179 0.991 -6.410 1.00 94.70 ? 28 GLU A CD 1
+ATOM 248 O OE1 . GLU A 1 28 ? -18.404 1.249 -6.372 1.00 88.42 ? 28 GLU A OE1 1
+ATOM 249 O OE2 . GLU A 1 28 ? -16.651 0.077 -5.735 1.00 92.20 ? 28 GLU A OE2 1
+ATOM 250 N N . ASN A 1 29 ? -17.318 5.386 -9.565 1.00 59.19 ? 29 ASN A N 1
+ATOM 251 C CA . ASN A 1 29 ? -17.796 6.203 -10.696 1.00 59.49 ? 29 ASN A CA 1
+ATOM 252 C C . ASN A 1 29 ? -18.169 7.672 -10.375 1.00 62.67 ? 29 ASN A C 1
+ATOM 253 O O . ASN A 1 29 ? -18.803 8.377 -11.169 1.00 63.18 ? 29 ASN A O 1
+ATOM 254 C CB . ASN A 1 29 ? -18.789 5.462 -11.591 1.00 63.17 ? 29 ASN A CB 1
+ATOM 255 C CG . ASN A 1 29 ? -18.098 4.634 -12.652 1.00 94.44 ? 29 ASN A CG 1
+ATOM 256 O OD1 . ASN A 1 29 ? -18.011 5.026 -13.825 1.00 91.87 ? 29 ASN A OD1 1
+ATOM 257 N ND2 . ASN A 1 29 ? -17.554 3.485 -12.258 1.00 85.80 ? 29 ASN A ND2 1
+ATOM 258 N N . ASN A 1 30 ? -17.715 8.125 -9.207 1.00 57.56 ? 30 ASN A N 1
+ATOM 259 C CA . ASN A 1 30 ? -17.747 9.502 -8.736 1.00 57.01 ? 30 ASN A CA 1
+ATOM 260 C C . ASN A 1 30 ? -16.224 9.764 -8.781 1.00 60.06 ? 30 ASN A C 1
+ATOM 261 O O . ASN A 1 30 ? -15.639 10.188 -7.787 1.00 61.08 ? 30 ASN A O 1
+ATOM 262 C CB . ASN A 1 30 ? -18.297 9.600 -7.273 1.00 54.89 ? 30 ASN A CB 1
+ATOM 263 C CG . ASN A 1 30 ? -19.529 8.769 -6.964 1.00 64.40 ? 30 ASN A CG 1
+ATOM 264 O OD1 . ASN A 1 30 ? -20.656 9.112 -7.341 1.00 58.80 ? 30 ASN A OD1 1
+ATOM 265 N ND2 . ASN A 1 30 ? -19.344 7.668 -6.243 1.00 49.36 ? 30 ASN A ND2 1
+ATOM 266 N N . ALA A 1 31 ? -15.579 9.434 -9.942 1.00 52.98 ? 31 ALA A N 1
+ATOM 267 C CA . ALA A 1 31 ? -14.130 9.465 -10.157 1.00 51.02 ? 31 ALA A CA 1
+ATOM 268 C C . ALA A 1 31 ? -13.552 10.743 -10.764 1.00 50.30 ? 31 ALA A C 1
+ATOM 269 O O . ALA A 1 31 ? -14.220 11.404 -11.562 1.00 51.70 ? 31 ALA A O 1
+ATOM 270 C CB . ALA A 1 31 ? -13.693 8.248 -10.957 1.00 51.78 ? 31 ALA A CB 1
+ATOM 271 N N . SER A 1 32 ? -12.307 11.079 -10.377 1.00 39.61 ? 32 SER A N 1
+ATOM 272 C CA . SER A 1 32 ? -11.595 12.271 -10.813 1.00 37.14 ? 32 SER A CA 1
+ATOM 273 C C . SER A 1 32 ? -10.564 11.972 -11.904 1.00 35.88 ? 32 SER A C 1
+ATOM 274 O O . SER A 1 32 ? -9.842 10.982 -11.817 1.00 35.74 ? 32 SER A O 1
+ATOM 275 C CB . SER A 1 32 ? -10.895 12.913 -9.623 1.00 40.83 ? 32 SER A CB 1
+ATOM 276 O OG . SER A 1 32 ? -11.813 13.491 -8.712 1.00 52.55 ? 32 SER A OG 1
+ATOM 277 N N . THR A 1 33 ? -10.505 12.815 -12.929 1.00 28.64 ? 33 THR A N 1
+ATOM 278 C CA . THR A 1 33 ? -9.487 12.672 -13.969 1.00 26.52 ? 33 THR A CA 1
+ATOM 279 C C . THR A 1 33 ? -8.399 13.662 -13.668 1.00 25.93 ? 33 THR A C 1
+ATOM 280 O O . THR A 1 33 ? -8.664 14.826 -13.363 1.00 23.18 ? 33 THR A O 1
+ATOM 281 C CB . THR A 1 33 ? -10.011 12.633 -15.417 1.00 31.24 ? 33 THR A CB 1
+ATOM 282 O OG1 . THR A 1 33 ? -9.357 13.617 -16.230 1.00 39.83 ? 33 THR A OG1 1
+ATOM 283 C CG2 . THR A 1 33 ? -11.501 12.712 -15.515 1.00 21.29 ? 33 THR A CG2 1
+ATOM 284 N N . TYR A 1 34 ? -7.183 13.152 -13.659 1.00 22.91 ? 34 TYR A N 1
+ATOM 285 C CA . TYR A 1 34 ? -5.977 13.885 -13.352 1.00 22.15 ? 34 TYR A CA 1
+ATOM 286 C C . TYR A 1 34 ? -5.117 13.943 -14.594 1.00 27.28 ? 34 TYR A C 1
+ATOM 287 O O . TYR A 1 34 ? -5.203 13.067 -15.460 1.00 26.23 ? 34 TYR A O 1
+ATOM 288 C CB . TYR A 1 34 ? -5.211 13.157 -12.220 1.00 23.14 ? 34 TYR A CB 1
+ATOM 289 C CG . TYR A 1 34 ? -5.798 13.409 -10.851 1.00 24.49 ? 34 TYR A CG 1
+ATOM 290 C CD1 . TYR A 1 34 ? -6.825 12.623 -10.350 1.00 25.51 ? 34 TYR A CD1 1
+ATOM 291 C CD2 . TYR A 1 34 ? -5.338 14.465 -10.065 1.00 24.85 ? 34 TYR A CD2 1
+ATOM 292 C CE1 . TYR A 1 34 ? -7.393 12.881 -9.105 1.00 26.49 ? 34 TYR A CE1 1
+ATOM 293 C CE2 . TYR A 1 34 ? -5.884 14.720 -8.814 1.00 25.60 ? 34 TYR A CE2 1
+ATOM 294 C CZ . TYR A 1 34 ? -6.911 13.928 -8.336 1.00 30.48 ? 34 TYR A CZ 1
+ATOM 295 O OH . TYR A 1 34 ? -7.443 14.203 -7.104 1.00 30.64 ? 34 TYR A OH 1
+ATOM 296 N N . VAL A 1 35 ? -4.265 14.965 -14.667 1.00 24.57 ? 35 VAL A N 1
+ATOM 297 C CA . VAL A 1 35 ? -3.300 15.140 -15.736 1.00 24.11 ? 35 VAL A CA 1
+ATOM 298 C C . VAL A 1 35 ? -1.932 15.339 -15.103 1.00 28.92 ? 35 VAL A C 1
+ATOM 299 O O . VAL A 1 35 ? -1.802 16.035 -14.091 1.00 26.45 ? 35 VAL A O 1
+ATOM 300 C CB . VAL A 1 35 ? -3.631 16.280 -16.737 1.00 28.25 ? 35 VAL A CB 1
+ATOM 301 C CG1 . VAL A 1 35 ? -2.785 16.123 -18.003 1.00 27.73 ? 35 VAL A CG1 1
+ATOM 302 C CG2 . VAL A 1 35 ? -5.126 16.319 -17.094 1.00 27.89 ? 35 VAL A CG2 1
+ATOM 303 N N . GLY A 1 36 ? -0.925 14.733 -15.713 1.00 26.50 ? 36 GLY A N 1
+ATOM 304 C CA . GLY A 1 36 ? 0.444 14.858 -15.241 1.00 26.69 ? 36 GLY A CA 1
+ATOM 305 C C . GLY A 1 36 ? 1.478 14.251 -16.155 1.00 29.43 ? 36 GLY A C 1
+ATOM 306 O O . GLY A 1 36 ? 1.124 13.597 -17.141 1.00 28.52 ? 36 GLY A O 1
+ATOM 307 N N . VAL A 1 37 ? 2.774 14.430 -15.831 1.00 26.58 ? 37 VAL A N 1
+ATOM 308 C CA . VAL A 1 37 ? 3.309 15.189 -14.682 1.00 26.77 ? 37 VAL A CA 1
+ATOM 309 C C . VAL A 1 37 ? 3.407 16.667 -15.072 1.00 34.54 ? 37 VAL A C 1
+ATOM 310 O O . VAL A 1 37 ? 3.909 17.007 -16.141 1.00 32.29 ? 37 VAL A O 1
+ATOM 311 C CB . VAL A 1 37 ? 4.675 14.634 -14.194 1.00 29.29 ? 37 VAL A CB 1
+ATOM 312 C CG1 . VAL A 1 37 ? 5.143 15.328 -12.925 1.00 28.08 ? 37 VAL A CG1 1
+ATOM 313 C CG2 . VAL A 1 37 ? 4.607 13.124 -13.983 1.00 29.20 ? 37 VAL A CG2 1
+ATOM 314 N N . VAL A 1 38 ? 2.881 17.525 -14.207 1.00 33.42 ? 38 VAL A N 1
+ATOM 315 C CA . VAL A 1 38 ? 2.849 18.965 -14.414 1.00 33.48 ? 38 VAL A CA 1
+ATOM 316 C C . VAL A 1 38 ? 4.007 19.621 -13.665 1.00 37.50 ? 38 VAL A C 1
+ATOM 317 O O . VAL A 1 38 ? 4.409 20.733 -13.990 1.00 34.96 ? 38 VAL A O 1
+ATOM 318 C CB . VAL A 1 38 ? 1.476 19.534 -13.964 1.00 37.79 ? 38 VAL A CB 1
+ATOM 319 C CG1 . VAL A 1 38 ? 0.326 18.865 -14.720 1.00 38.26 ? 38 VAL A CG1 1
+ATOM 320 C CG2 . VAL A 1 38 ? 1.278 19.417 -12.444 1.00 36.89 ? 38 VAL A CG2 1
+ATOM 321 N N . LEU A 1 39 ? 4.509 18.938 -12.634 1.00 36.41 ? 39 LEU A N 1
+ATOM 322 C CA . LEU A 1 39 ? 5.549 19.450 -11.747 1.00 37.63 ? 39 LEU A CA 1
+ATOM 323 C C . LEU A 1 39 ? 6.254 18.255 -11.104 1.00 44.02 ? 39 LEU A C 1
+ATOM 324 O O . LEU A 1 39 ? 5.620 17.429 -10.440 1.00 43.48 ? 39 LEU A O 1
+ATOM 325 C CB . LEU A 1 39 ? 4.897 20.323 -10.636 1.00 37.53 ? 39 LEU A CB 1
+ATOM 326 C CG . LEU A 1 39 ? 5.434 21.738 -10.296 1.00 41.96 ? 39 LEU A CG 1
+ATOM 327 C CD1 . LEU A 1 39 ? 5.087 22.092 -8.858 1.00 41.14 ? 39 LEU A CD1 1
+ATOM 328 C CD2 . LEU A 1 39 ? 6.936 21.867 -10.487 1.00 43.32 ? 39 LEU A CD2 1
+ATOM 329 N N . LYS A 1 40 ? 7.546 18.135 -11.361 1.00 43.20 ? 40 LYS A N 1
+ATOM 330 C CA . LYS A 1 40 ? 8.391 17.096 -10.802 1.00 44.60 ? 40 LYS A CA 1
+ATOM 331 C C . LYS A 1 40 ? 9.210 17.909 -9.796 1.00 53.27 ? 40 LYS A C 1
+ATOM 332 O O . LYS A 1 40 ? 10.188 18.569 -10.169 1.00 54.08 ? 40 LYS A O 1
+ATOM 333 C CB . LYS A 1 40 ? 9.236 16.465 -11.928 1.00 46.91 ? 40 LYS A CB 1
+ATOM 334 C CG . LYS A 1 40 ? 10.268 15.450 -11.472 1.00 58.87 ? 40 LYS A CG 1
+ATOM 335 C CD . LYS A 1 40 ? 11.626 15.755 -12.101 1.00 68.73 ? 40 LYS A CD 1
+ATOM 336 C CE . LYS A 1 40 ? 12.807 15.185 -11.344 1.00 72.86 ? 40 LYS A CE 1
+ATOM 337 N NZ . LYS A 1 40 ? 12.810 13.696 -11.329 1.00 73.43 ? 40 LYS A NZ 1
+ATOM 338 N N . LYS A 1 41 ? 8.722 17.981 -8.550 1.00 52.05 ? 41 LYS A N 1
+ATOM 339 C CA . LYS A 1 41 ? 9.356 18.833 -7.551 1.00 53.97 ? 41 LYS A CA 1
+ATOM 340 C C . LYS A 1 41 ? 9.688 18.155 -6.211 1.00 61.85 ? 41 LYS A C 1
+ATOM 341 O O . LYS A 1 41 ? 9.071 18.500 -5.198 1.00 62.91 ? 41 LYS A O 1
+ATOM 342 C CB . LYS A 1 41 ? 8.548 20.136 -7.360 1.00 56.90 ? 41 LYS A CB 1
+ATOM 343 N N . ASN A 1 42 ? 10.706 17.244 -6.162 1.00 58.77 ? 42 ASN A N 1
+ATOM 344 C CA . ASN A 1 42 ? 11.499 16.725 -7.294 1.00 57.79 ? 42 ASN A CA 1
+ATOM 345 C C . ASN A 1 42 ? 11.380 15.210 -7.396 1.00 59.38 ? 42 ASN A C 1
+ATOM 346 O O . ASN A 1 42 ? 11.331 14.667 -8.502 1.00 59.41 ? 42 ASN A O 1
+ATOM 347 C CB . ASN A 1 42 ? 12.956 17.183 -7.255 1.00 60.92 ? 42 ASN A CB 1
+ATOM 348 C CG . ASN A 1 42 ? 13.235 18.389 -8.134 1.00 89.47 ? 42 ASN A CG 1
+ATOM 349 O OD1 . ASN A 1 42 ? 13.214 18.317 -9.372 1.00 82.52 ? 42 ASN A OD1 1
+ATOM 350 N ND2 . ASN A 1 42 ? 13.518 19.525 -7.514 1.00 83.06 ? 42 ASN A ND2 1
+ATOM 351 N N . ASP A 1 43 ? 11.290 14.528 -6.241 1.00 53.02 ? 43 ASP A N 1
+ATOM 352 C CA . ASP A 1 43 ? 11.081 13.080 -6.174 1.00 50.95 ? 43 ASP A CA 1
+ATOM 353 C C . ASP A 1 43 ? 9.591 12.831 -6.408 1.00 47.89 ? 43 ASP A C 1
+ATOM 354 O O . ASP A 1 43 ? 9.186 11.737 -6.814 1.00 48.26 ? 43 ASP A O 1
+ATOM 355 C CB . ASP A 1 43 ? 11.488 12.547 -4.783 1.00 53.62 ? 43 ASP A CB 1
+ATOM 356 C CG . ASP A 1 43 ? 11.237 11.061 -4.569 1.00 66.20 ? 43 ASP A CG 1
+ATOM 357 O OD1 . ASP A 1 43 ? 11.555 10.265 -5.483 1.00 66.61 ? 43 ASP A OD1 1
+ATOM 358 O OD2 . ASP A 1 43 ? 10.713 10.697 -3.490 1.00 72.65 ? 43 ASP A OD2 1
+ATOM 359 N N . PHE A 1 44 ? 8.781 13.873 -6.157 1.00 38.44 ? 44 PHE A N 1
+ATOM 360 C CA . PHE A 1 44 ? 7.333 13.857 -6.279 1.00 35.45 ? 44 PHE A CA 1
+ATOM 361 C C . PHE A 1 44 ? 6.830 14.265 -7.627 1.00 36.10 ? 44 PHE A C 1
+ATOM 362 O O . PHE A 1 44 ? 7.269 15.270 -8.183 1.00 36.21 ? 44 PHE A O 1
+ATOM 363 C CB . PHE A 1 44 ? 6.699 14.745 -5.207 1.00 36.21 ? 44 PHE A CB 1
+ATOM 364 C CG . PHE A 1 44 ? 7.083 14.339 -3.809 1.00 37.12 ? 44 PHE A CG 1
+ATOM 365 C CD1 . PHE A 1 44 ? 6.433 13.289 -3.171 1.00 38.94 ? 44 PHE A CD1 1
+ATOM 366 C CD2 . PHE A 1 44 ? 8.127 14.973 -3.146 1.00 39.46 ? 44 PHE A CD2 1
+ATOM 367 C CE1 . PHE A 1 44 ? 6.792 12.914 -1.875 1.00 40.10 ? 44 PHE A CE1 1
+ATOM 368 C CE2 . PHE A 1 44 ? 8.482 14.600 -1.850 1.00 41.96 ? 44 PHE A CE2 1
+ATOM 369 C CZ . PHE A 1 44 ? 7.803 13.585 -1.219 1.00 39.50 ? 44 PHE A CZ 1
+ATOM 370 N N . ASN A 1 45 ? 5.882 13.487 -8.139 1.00 30.13 ? 45 ASN A N 1
+ATOM 371 C CA . ASN A 1 45 ? 5.193 13.782 -9.386 1.00 28.01 ? 45 ASN A CA 1
+ATOM 372 C C . ASN A 1 45 ? 3.820 14.320 -9.045 1.00 27.32 ? 45 ASN A C 1
+ATOM 373 O O . ASN A 1 45 ? 3.082 13.692 -8.294 1.00 27.06 ? 45 ASN A O 1
+ATOM 374 C CB . ASN A 1 45 ? 5.106 12.558 -10.270 1.00 28.00 ? 45 ASN A CB 1
+ATOM 375 C CG . ASN A 1 45 ? 6.441 12.099 -10.822 1.00 43.88 ? 45 ASN A CG 1
+ATOM 376 O OD1 . ASN A 1 45 ? 7.283 12.890 -11.291 1.00 33.74 ? 45 ASN A OD1 1
+ATOM 377 N ND2 . ASN A 1 45 ? 6.639 10.797 -10.805 1.00 31.80 ? 45 ASN A ND2 1
+ATOM 378 N N . TYR A 1 46 ? 3.515 15.509 -9.558 1.00 21.60 ? 46 TYR A N 1
+ATOM 379 C CA . TYR A 1 46 ? 2.280 16.241 -9.311 1.00 21.61 ? 46 TYR A CA 1
+ATOM 380 C C . TYR A 1 46 ? 1.287 16.104 -10.432 1.00 25.82 ? 46 TYR A C 1
+ATOM 381 O O . TYR A 1 46 ? 1.631 16.214 -11.606 1.00 25.57 ? 46 TYR A O 1
+ATOM 382 C CB . TYR A 1 46 ? 2.591 17.710 -9.053 1.00 22.60 ? 46 TYR A CB 1
+ATOM 383 C CG . TYR A 1 46 ? 2.871 17.982 -7.597 1.00 23.10 ? 46 TYR A CG 1
+ATOM 384 C CD1 . TYR A 1 46 ? 4.140 17.778 -7.058 1.00 23.81 ? 46 TYR A CD1 1
+ATOM 385 C CD2 . TYR A 1 46 ? 1.852 18.390 -6.740 1.00 23.73 ? 46 TYR A CD2 1
+ATOM 386 C CE1 . TYR A 1 46 ? 4.399 18.020 -5.712 1.00 24.82 ? 46 TYR A CE1 1
+ATOM 387 C CE2 . TYR A 1 46 ? 2.099 18.636 -5.395 1.00 24.85 ? 46 TYR A CE2 1
+ATOM 388 C CZ . TYR A 1 46 ? 3.372 18.451 -4.886 1.00 27.65 ? 46 TYR A CZ 1
+ATOM 389 O OH . TYR A 1 46 ? 3.569 18.655 -3.554 1.00 24.46 ? 46 TYR A OH 1
+ATOM 390 N N . PHE A 1 47 ? 0.047 15.850 -10.049 1.00 22.47 ? 47 PHE A N 1
+ATOM 391 C CA . PHE A 1 47 ? -1.070 15.656 -10.956 1.00 21.14 ? 47 PHE A CA 1
+ATOM 392 C C . PHE A 1 47 ? -2.188 16.636 -10.633 1.00 23.19 ? 47 PHE A C 1
+ATOM 393 O O . PHE A 1 47 ? -2.522 16.793 -9.473 1.00 21.68 ? 47 PHE A O 1
+ATOM 394 C CB . PHE A 1 47 ? -1.535 14.188 -10.882 1.00 21.84 ? 47 PHE A CB 1
+ATOM 395 C CG . PHE A 1 47 ? -0.425 13.260 -11.340 1.00 21.45 ? 47 PHE A CG 1
+ATOM 396 C CD1 . PHE A 1 47 ? -0.309 12.898 -12.675 1.00 22.39 ? 47 PHE A CD1 1
+ATOM 397 C CD2 . PHE A 1 47 ? 0.559 12.832 -10.453 1.00 23.01 ? 47 PHE A CD2 1
+ATOM 398 C CE1 . PHE A 1 47 ? 0.766 12.128 -13.120 1.00 22.43 ? 47 PHE A CE1 1
+ATOM 399 C CE2 . PHE A 1 47 ? 1.623 12.042 -10.895 1.00 25.12 ? 47 PHE A CE2 1
+ATOM 400 C CZ . PHE A 1 47 ? 1.710 11.686 -12.224 1.00 22.37 ? 47 PHE A CZ 1
+ATOM 401 N N . ILE A 1 48 ? -2.733 17.315 -11.665 1.00 21.15 ? 48 ILE A N 1
+ATOM 402 C CA . ILE A 1 48 ? -3.813 18.305 -11.554 1.00 19.80 ? 48 ILE A CA 1
+ATOM 403 C C . ILE A 1 48 ? -5.165 17.658 -11.884 1.00 22.79 ? 48 ILE A C 1
+ATOM 404 O O . ILE A 1 48 ? -5.305 17.032 -12.950 1.00 21.08 ? 48 ILE A O 1
+ATOM 405 C CB . ILE A 1 48 ? -3.568 19.527 -12.478 1.00 24.03 ? 48 ILE A CB 1
+ATOM 406 C CG1 . ILE A 1 48 ? -2.178 20.145 -12.261 1.00 26.08 ? 48 ILE A CG1 1
+ATOM 407 C CG2 . ILE A 1 48 ? -4.637 20.605 -12.283 1.00 27.50 ? 48 ILE A CG2 1
+ATOM 408 C CD1 . ILE A 1 48 ? -1.841 21.273 -13.221 1.00 32.86 ? 48 ILE A CD1 1
+ATOM 409 N N . PRO A 1 49 ? -6.196 17.850 -11.037 1.00 16.77 ? 49 PRO A N 1
+ATOM 410 C CA . PRO A 1 49 ? -7.525 17.358 -11.423 1.00 18.42 ? 49 PRO A CA 1
+ATOM 411 C C . PRO A 1 49 ? -8.113 18.272 -12.510 1.00 25.42 ? 49 PRO A C 1
+ATOM 412 O O . PRO A 1 49 ? -7.879 19.466 -12.518 1.00 22.62 ? 49 PRO A O 1
+ATOM 413 C CB . PRO A 1 49 ? -8.318 17.391 -10.119 1.00 20.10 ? 49 PRO A CB 1
+ATOM 414 C CG . PRO A 1 49 ? -7.649 18.459 -9.294 1.00 22.76 ? 49 PRO A CG 1
+ATOM 415 C CD . PRO A 1 49 ? -6.229 18.592 -9.758 1.00 17.92 ? 49 PRO A CD 1
+ATOM 416 N N . LEU A 1 50 ? -8.813 17.676 -13.463 1.00 27.25 ? 50 LEU A N 1
+ATOM 417 C CA . LEU A 1 50 ? -9.418 18.352 -14.601 1.00 28.85 ? 50 LEU A CA 1
+ATOM 418 C C . LEU A 1 50 ? -10.935 18.319 -14.425 1.00 34.18 ? 50 LEU A C 1
+ATOM 419 O O . LEU A 1 50 ? -11.486 17.257 -14.095 1.00 32.89 ? 50 LEU A O 1
+ATOM 420 C CB . LEU A 1 50 ? -8.998 17.591 -15.890 1.00 29.96 ? 50 LEU A CB 1
+ATOM 421 C CG . LEU A 1 50 ? -9.638 17.993 -17.242 1.00 36.49 ? 50 LEU A CG 1
+ATOM 422 C CD1 . LEU A 1 50 ? -8.594 18.031 -18.356 1.00 35.84 ? 50 LEU A CD1 1
+ATOM 423 C CD2 . LEU A 1 50 ? -10.726 16.979 -17.644 1.00 41.94 ? 50 LEU A CD2 1
+ATOM 424 N N . LEU A 1 51 ? -11.599 19.478 -14.624 1.00 31.55 ? 51 LEU A N 1
+ATOM 425 C CA . LEU A 1 51 ? -13.062 19.594 -14.613 1.00 33.44 ? 51 LEU A CA 1
+ATOM 426 C C . LEU A 1 51 ? -13.540 19.962 -16.019 1.00 40.28 ? 51 LEU A C 1
+ATOM 427 O O . LEU A 1 51 ? -13.013 20.909 -16.602 1.00 38.95 ? 51 LEU A O 1
+ATOM 428 C CB . LEU A 1 51 ? -13.568 20.655 -13.610 1.00 33.93 ? 51 LEU A CB 1
+ATOM 429 C CG . LEU A 1 51 ? -13.272 20.448 -12.124 1.00 39.47 ? 51 LEU A CG 1
+ATOM 430 C CD1 . LEU A 1 51 ? -13.984 21.512 -11.291 1.00 40.37 ? 51 LEU A CD1 1
+ATOM 431 C CD2 . LEU A 1 51 ? -13.699 19.051 -11.641 1.00 41.67 ? 51 LEU A CD2 1
+ATOM 432 N N . SER A 1 52 ? -14.528 19.234 -16.561 1.00 39.88 ? 52 SER A N 1
+ATOM 433 C CA . SER A 1 52 ? -15.082 19.524 -17.891 1.00 41.94 ? 52 SER A CA 1
+ATOM 434 C C . SER A 1 52 ? -15.957 20.773 -17.888 1.00 48.31 ? 52 SER A C 1
+ATOM 435 O O . SER A 1 52 ? -16.560 21.087 -16.861 1.00 48.30 ? 52 SER A O 1
+ATOM 436 C CB . SER A 1 52 ? -15.869 18.329 -18.419 1.00 47.25 ? 52 SER A CB 1
+ATOM 437 O OG . SER A 1 52 ? -14.969 17.349 -18.916 1.00 60.04 ? 52 SER A OG 1
+ATOM 438 N N . TYR A 1 53 ? -16.008 21.501 -19.025 1.00 46.81 ? 53 TYR A N 1
+ATOM 439 C CA . TYR A 1 53 ? -16.828 22.713 -19.166 1.00 47.32 ? 53 TYR A CA 1
+ATOM 440 C C . TYR A 1 53 ? -18.325 22.365 -19.239 1.00 52.00 ? 53 TYR A C 1
+ATOM 441 O O . TYR A 1 53 ? -18.700 21.443 -19.963 1.00 51.43 ? 53 TYR A O 1
+ATOM 442 C CB . TYR A 1 53 ? -16.419 23.525 -20.412 1.00 48.72 ? 53 TYR A CB 1
+ATOM 443 C CG . TYR A 1 53 ? -17.219 24.798 -20.610 1.00 51.20 ? 53 TYR A CG 1
+ATOM 444 C CD1 . TYR A 1 53 ? -16.903 25.958 -19.909 1.00 52.90 ? 53 TYR A CD1 1
+ATOM 445 C CD2 . TYR A 1 53 ? -18.277 24.851 -21.516 1.00 52.35 ? 53 TYR A CD2 1
+ATOM 446 C CE1 . TYR A 1 53 ? -17.641 27.130 -20.076 1.00 53.76 ? 53 TYR A CE1 1
+ATOM 447 C CE2 . TYR A 1 53 ? -19.026 26.018 -21.689 1.00 53.42 ? 53 TYR A CE2 1
+ATOM 448 C CZ . TYR A 1 53 ? -18.696 27.159 -20.973 1.00 59.60 ? 53 TYR A CZ 1
+ATOM 449 O OH . TYR A 1 53 ? -19.399 28.326 -21.145 1.00 59.26 ? 53 TYR A OH 1
+ATOM 450 N N . ASN A 1 57 ? -22.962 26.482 -14.861 1.00 76.81 ? 57 ASN A N 1
+ATOM 451 C CA . ASN A 1 57 ? -23.092 27.189 -16.115 1.00 76.58 ? 57 ASN A CA 1
+ATOM 452 C C . ASN A 1 57 ? -22.561 28.568 -15.916 1.00 80.63 ? 57 ASN A C 1
+ATOM 453 O O . ASN A 1 57 ? -21.573 28.716 -15.243 1.00 80.58 ? 57 ASN A O 1
+ATOM 454 C CB . ASN A 1 57 ? -24.542 27.212 -16.547 1.00 77.94 ? 57 ASN A CB 1
+ATOM 455 N N . PRO A 1 58 ? -23.235 29.615 -16.556 1.00 73.69 ? 58 PRO A N 1
+ATOM 456 C CA . PRO A 1 58 ? -22.701 30.955 -16.249 1.00 73.06 ? 58 PRO A CA 1
+ATOM 457 C C . PRO A 1 58 ? -22.236 31.291 -14.831 1.00 75.93 ? 58 PRO A C 1
+ATOM 458 O O . PRO A 1 58 ? -21.544 32.271 -14.633 1.00 74.66 ? 58 PRO A O 1
+ATOM 459 C CB . PRO A 1 58 ? -23.877 31.854 -16.579 1.00 20.00 ? 58 PRO A CB 1
+ATOM 460 C CG . PRO A 1 58 ? -24.375 31.309 -17.835 1.00 20.00 ? 58 PRO A CG 1
+ATOM 461 C CD . PRO A 1 58 ? -24.312 29.829 -17.654 1.00 20.00 ? 58 PRO A CD 1
+ATOM 462 N N . GLU A 1 59 ? -22.644 30.463 -13.871 1.00 72.10 ? 59 GLU A N 1
+ATOM 463 C CA . GLU A 1 59 ? -22.269 30.630 -12.475 1.00 71.35 ? 59 GLU A CA 1
+ATOM 464 C C . GLU A 1 59 ? -20.794 30.370 -12.384 1.00 72.94 ? 59 GLU A C 1
+ATOM 465 O O . GLU A 1 59 ? -19.971 31.236 -12.100 1.00 72.47 ? 59 GLU A O 1
+ATOM 466 C CB . GLU A 1 59 ? -22.984 29.595 -11.570 1.00 20.00 ? 59 GLU A CB 1
+ATOM 467 C CG . GLU A 1 59 ? -23.365 28.249 -12.226 1.00 20.00 ? 59 GLU A CG 1
+ATOM 468 C CD . GLU A 1 59 ? -23.081 27.007 -11.387 1.00 20.00 ? 59 GLU A CD 1
+ATOM 469 O OE1 . GLU A 1 59 ? -22.993 25.915 -11.972 1.00 20.00 ? 59 GLU A OE1 1
+ATOM 470 O OE2 . GLU A 1 59 ? -22.939 27.105 -10.150 1.00 20.00 ? 59 GLU A OE2 1
+ATOM 471 N N . LYS A 1 60 ? -20.526 29.118 -12.663 1.00 67.27 ? 60 LYS A N 1
+ATOM 472 C CA . LYS A 1 60 ? -19.269 28.435 -12.534 1.00 65.80 ? 60 LYS A CA 1
+ATOM 473 C C . LYS A 1 60 ? -18.177 29.026 -13.391 1.00 66.37 ? 60 LYS A C 1
+ATOM 474 O O . LYS A 1 60 ? -17.107 29.334 -12.909 1.00 64.52 ? 60 LYS A O 1
+ATOM 475 C CB . LYS A 1 60 ? -19.506 26.992 -12.944 1.00 68.00 ? 60 LYS A CB 1
+ATOM 476 C CG . LYS A 1 60 ? -18.425 26.024 -12.541 1.00 76.61 ? 60 LYS A CG 1
+ATOM 477 C CD . LYS A 1 60 ? -18.308 24.956 -13.590 1.00 81.26 ? 60 LYS A CD 1
+ATOM 478 C CE . LYS A 1 60 ? -17.076 24.137 -13.371 1.00 87.33 ? 60 LYS A CE 1
+ATOM 479 N NZ . LYS A 1 60 ? -17.439 22.773 -12.970 1.00 99.70 ? 60 LYS A NZ 1
+ATOM 480 N N . ASP A 1 61 ? -18.472 29.125 -14.676 1.00 61.58 ? 61 ASP A N 1
+ATOM 481 C CA . ASP A 1 61 ? -17.582 29.674 -15.686 1.00 60.29 ? 61 ASP A CA 1
+ATOM 482 C C . ASP A 1 61 ? -17.052 31.036 -15.273 1.00 61.73 ? 61 ASP A C 1
+ATOM 483 O O . ASP A 1 61 ? -15.931 31.384 -15.637 1.00 61.53 ? 61 ASP A O 1
+ATOM 484 C CB . ASP A 1 61 ? -18.312 29.776 -17.025 1.00 61.79 ? 61 ASP A CB 1
+ATOM 485 N N . LYS A 1 62 ? -17.862 31.805 -14.525 1.00 55.68 ? 62 LYS A N 1
+ATOM 486 C CA . LYS A 1 62 ? -17.510 33.143 -14.063 1.00 54.21 ? 62 LYS A CA 1
+ATOM 487 C C . LYS A 1 62 ? -16.602 33.087 -12.856 1.00 55.21 ? 62 LYS A C 1
+ATOM 488 O O . LYS A 1 62 ? -15.677 33.886 -12.749 1.00 55.00 ? 62 LYS A O 1
+ATOM 489 C CB . LYS A 1 62 ? -18.766 33.938 -13.728 1.00 56.78 ? 62 LYS A CB 1
+ATOM 490 N N . ALA A 1 63 ? -16.873 32.145 -11.943 1.00 49.46 ? 63 ALA A N 1
+ATOM 491 C CA . ALA A 1 63 ? -16.078 31.910 -10.755 1.00 48.20 ? 63 ALA A CA 1
+ATOM 492 C C . ALA A 1 63 ? -14.664 31.462 -11.128 1.00 48.84 ? 63 ALA A C 1
+ATOM 493 O O . ALA A 1 63 ? -13.717 31.901 -10.491 1.00 47.35 ? 63 ALA A O 1
+ATOM 494 C CB . ALA A 1 63 ? -16.748 30.874 -9.889 1.00 48.92 ? 63 ALA A CB 1
+ATOM 495 N N . MET A 1 64 ? -14.534 30.639 -12.180 1.00 43.98 ? 64 MET A N 1
+ATOM 496 C CA . MET A 1 64 ? -13.276 30.091 -12.675 1.00 43.29 ? 64 MET A CA 1
+ATOM 497 C C . MET A 1 64 ? -12.415 31.169 -13.317 1.00 48.38 ? 64 MET A C 1
+ATOM 498 O O . MET A 1 64 ? -11.197 31.151 -13.148 1.00 47.82 ? 64 MET A O 1
+ATOM 499 C CB . MET A 1 64 ? -13.568 28.973 -13.672 1.00 45.25 ? 64 MET A CB 1
+ATOM 500 C CG . MET A 1 64 ? -13.038 27.615 -13.289 1.00 48.28 ? 64 MET A CG 1
+ATOM 501 S SD . MET A 1 64 ? -13.349 26.944 -11.648 1.00 51.40 ? 64 MET A SD 1
+ATOM 502 C CE . MET A 1 64 ? -13.510 25.259 -12.056 1.00 48.04 ? 64 MET A CE 1
+ATOM 503 N N . LYS A 1 65 ? -13.053 32.115 -14.030 1.00 45.12 ? 65 LYS A N 1
+ATOM 504 C CA . LYS A 1 65 ? -12.415 33.254 -14.697 1.00 44.85 ? 65 LYS A CA 1
+ATOM 505 C C . LYS A 1 65 ? -11.785 34.166 -13.649 1.00 49.00 ? 65 LYS A C 1
+ATOM 506 O O . LYS A 1 65 ? -10.714 34.716 -13.887 1.00 49.34 ? 65 LYS A O 1
+ATOM 507 C CB . LYS A 1 65 ? -13.456 34.038 -15.517 1.00 46.93 ? 65 LYS A CB 1
+ATOM 508 C CG . LYS A 1 65 ? -13.321 33.907 -17.017 1.00 59.31 ? 65 LYS A CG 1
+ATOM 509 C CD . LYS A 1 65 ? -13.327 35.288 -17.691 1.00 69.79 ? 65 LYS A CD 1
+ATOM 510 C CE . LYS A 1 65 ? -13.950 35.312 -19.087 1.00 77.35 ? 65 LYS A CE 1
+ATOM 511 N NZ . LYS A 1 65 ? -12.958 35.629 -20.136 1.00 82.44 ? 65 LYS A NZ 1
+ATOM 512 N N . LYS A 1 66 ? -12.440 34.313 -12.487 1.00 44.11 ? 66 LYS A N 1
+ATOM 513 C CA . LYS A 1 66 ? -11.970 35.155 -11.393 1.00 43.43 ? 66 LYS A CA 1
+ATOM 514 C C . LYS A 1 66 ? -10.769 34.509 -10.678 1.00 45.31 ? 66 LYS A C 1
+ATOM 515 O O . LYS A 1 66 ? -10.017 35.205 -9.988 1.00 44.82 ? 66 LYS A O 1
+ATOM 516 C CB . LYS A 1 66 ? -13.111 35.420 -10.399 1.00 46.26 ? 66 LYS A CB 1
+ATOM 517 N N . ARG A 1 67 ? -10.598 33.182 -10.842 1.00 38.70 ? 67 ARG A N 1
+ATOM 518 C CA . ARG A 1 67 ? -9.469 32.495 -10.237 1.00 36.14 ? 67 ARG A CA 1
+ATOM 519 C C . ARG A 1 67 ? -8.366 32.091 -11.241 1.00 32.88 ? 67 ARG A C 1
+ATOM 520 O O . ARG A 1 67 ? -7.742 31.041 -11.107 1.00 30.74 ? 67 ARG A O 1
+ATOM 521 C CB . ARG A 1 67 ? -9.901 31.403 -9.243 1.00 38.27 ? 67 ARG A CB 1
+ATOM 522 C CG . ARG A 1 67 ? -10.916 30.386 -9.743 1.00 50.85 ? 67 ARG A CG 1
+ATOM 523 C CD . ARG A 1 67 ? -11.500 29.569 -8.596 1.00 53.52 ? 67 ARG A CD 1
+ATOM 524 N NE . ARG A 1 67 ? -12.274 30.376 -7.648 1.00 52.96 ? 67 ARG A NE 1
+ATOM 525 C CZ . ARG A 1 67 ? -13.011 29.868 -6.662 1.00 75.56 ? 67 ARG A CZ 1
+ATOM 526 N NH1 . ARG A 1 67 ? -13.083 28.554 -6.485 1.00 63.61 ? 67 ARG A NH1 1
+ATOM 527 N NH2 . ARG A 1 67 ? -13.688 30.670 -5.850 1.00 67.32 ? 67 ARG A NH2 1
+ATOM 528 N N . SER A 1 68 ? -8.085 32.980 -12.209 1.00 27.22 ? 68 SER A N 1
+ATOM 529 C CA . SER A 1 68 ? -7.056 32.774 -13.235 1.00 26.57 ? 68 SER A CA 1
+ATOM 530 C C . SER A 1 68 ? -5.631 32.541 -12.682 1.00 27.75 ? 68 SER A C 1
+ATOM 531 O O . SER A 1 68 ? -4.810 32.004 -13.399 1.00 25.05 ? 68 SER A O 1
+ATOM 532 C CB . SER A 1 68 ? -7.084 33.885 -14.282 1.00 29.23 ? 68 SER A CB 1
+ATOM 533 O OG . SER A 1 68 ? -6.453 35.064 -13.814 1.00 40.14 ? 68 SER A OG 1
+ATOM 534 N N . ARG A 1 69 ? -5.351 32.904 -11.405 1.00 26.35 ? 69 ARG A N 1
+ATOM 535 C CA . ARG A 1 69 ? -4.050 32.646 -10.759 1.00 26.33 ? 69 ARG A CA 1
+ATOM 536 C C . ARG A 1 69 ? -3.861 31.164 -10.379 1.00 28.08 ? 69 ARG A C 1
+ATOM 537 O O . ARG A 1 69 ? -2.743 30.729 -10.098 1.00 27.10 ? 69 ARG A O 1
+ATOM 538 C CB . ARG A 1 69 ? -3.951 33.447 -9.456 1.00 27.81 ? 69 ARG A CB 1
+ATOM 539 C CG . ARG A 1 69 ? -3.493 34.879 -9.648 1.00 37.34 ? 69 ARG A CG 1
+ATOM 540 C CD . ARG A 1 69 ? -3.515 35.623 -8.333 1.00 36.48 ? 69 ARG A CD 1
+ATOM 541 N NE . ARG A 1 69 ? -4.862 36.054 -7.999 1.00 44.12 ? 69 ARG A NE 1
+ATOM 542 C CZ . ARG A 1 69 ? -5.176 36.819 -6.961 1.00 61.02 ? 69 ARG A CZ 1
+ATOM 543 N NH1 . ARG A 1 69 ? -4.220 37.226 -6.126 1.00 48.95 ? 69 ARG A NH1 1
+ATOM 544 N NH2 . ARG A 1 69 ? -6.429 37.185 -6.743 1.00 44.52 ? 69 ARG A NH2 1
+ATOM 545 N N . ILE A 1 70 ? -4.951 30.411 -10.360 1.00 24.38 ? 70 ILE A N 1
+ATOM 546 C CA . ILE A 1 70 ? -5.031 29.049 -9.843 1.00 24.09 ? 70 ILE A CA 1
+ATOM 547 C C . ILE A 1 70 ? -5.682 28.034 -10.774 1.00 25.05 ? 70 ILE A C 1
+ATOM 548 O O . ILE A 1 70 ? -5.507 26.842 -10.591 1.00 22.90 ? 70 ILE A O 1
+ATOM 549 C CB . ILE A 1 70 ? -5.798 29.260 -8.500 1.00 28.45 ? 70 ILE A CB 1
+ATOM 550 C CG1 . ILE A 1 70 ? -4.992 28.876 -7.304 1.00 28.55 ? 70 ILE A CG1 1
+ATOM 551 C CG2 . ILE A 1 70 ? -7.274 28.909 -8.439 1.00 31.76 ? 70 ILE A CG2 1
+ATOM 552 C CD1 . ILE A 1 70 ? -4.295 29.958 -6.875 1.00 30.24 ? 70 ILE A CD1 1
+ATOM 553 N N . VAL A 1 71 ? -6.441 28.506 -11.746 1.00 21.82 ? 71 VAL A N 1
+ATOM 554 C CA . VAL A 1 71 ? -7.154 27.656 -12.691 1.00 22.19 ? 71 VAL A CA 1
+ATOM 555 C C . VAL A 1 71 ? -6.698 27.991 -14.107 1.00 25.51 ? 71 VAL A C 1
+ATOM 556 O O . VAL A 1 71 ? -6.616 29.175 -14.447 1.00 22.91 ? 71 VAL A O 1
+ATOM 557 C CB . VAL A 1 71 ? -8.694 27.846 -12.551 1.00 26.22 ? 71 VAL A CB 1
+ATOM 558 C CG1 . VAL A 1 71 ? -9.441 27.317 -13.775 1.00 26.46 ? 71 VAL A CG1 1
+ATOM 559 C CG2 . VAL A 1 71 ? -9.226 27.208 -11.274 1.00 25.49 ? 71 VAL A CG2 1
+ATOM 560 N N . THR A 1 72 ? -6.389 26.948 -14.918 1.00 22.21 ? 72 THR A N 1
+ATOM 561 C CA . THR A 1 72 ? -6.104 27.116 -16.338 1.00 22.80 ? 72 THR A CA 1
+ATOM 562 C C . THR A 1 72 ? -7.339 26.675 -17.116 1.00 27.69 ? 72 THR A C 1
+ATOM 563 O O . THR A 1 72 ? -7.831 25.561 -16.934 1.00 26.59 ? 72 THR A O 1
+ATOM 564 C CB . THR A 1 72 ? -4.851 26.360 -16.806 1.00 27.45 ? 72 THR A CB 1
+ATOM 565 O OG1 . THR A 1 72 ? -3.745 26.867 -16.102 1.00 30.61 ? 72 THR A OG1 1
+ATOM 566 C CG2 . THR A 1 72 ? -4.564 26.577 -18.286 1.00 24.26 ? 72 THR A CG2 1
+ATOM 567 N N . ARG A 1 73 ? -7.785 27.531 -18.025 1.00 26.19 ? 73 ARG A N 1
+ATOM 568 C CA . ARG A 1 73 ? -8.929 27.279 -18.902 1.00 26.48 ? 73 ARG A CA 1
+ATOM 569 C C . ARG A 1 73 ? -8.477 26.523 -20.154 1.00 28.69 ? 73 ARG A C 1
+ATOM 570 O O . ARG A 1 73 ? -7.494 26.890 -20.789 1.00 26.98 ? 73 ARG A O 1
+ATOM 571 C CB . ARG A 1 73 ? -9.588 28.605 -19.265 1.00 27.42 ? 73 ARG A CB 1
+ATOM 572 C CG . ARG A 1 73 ? -10.115 29.361 -18.059 1.00 37.11 ? 73 ARG A CG 1
+ATOM 573 C CD . ARG A 1 73 ? -10.566 30.746 -18.449 1.00 47.83 ? 73 ARG A CD 1
+ATOM 574 N NE . ARG A 1 73 ? -11.678 30.709 -19.399 1.00 56.31 ? 73 ARG A NE 1
+ATOM 575 C CZ . ARG A 1 73 ? -12.025 31.723 -20.181 1.00 63.21 ? 73 ARG A CZ 1
+ATOM 576 N NH1 . ARG A 1 73 ? -11.337 32.857 -20.156 1.00 46.28 ? 73 ARG A NH1 1
+ATOM 577 N NH2 . ARG A 1 73 ? -13.055 31.605 -21.007 1.00 46.37 ? 73 ARG A NH2 1
+ATOM 578 N N . LEU A 1 74 ? -9.160 25.438 -20.473 1.00 25.61 ? 74 LEU A N 1
+ATOM 579 C CA . LEU A 1 74 ? -8.790 24.599 -21.617 1.00 25.25 ? 74 LEU A CA 1
+ATOM 580 C C . LEU A 1 74 ? -9.645 24.986 -22.794 1.00 30.84 ? 74 LEU A C 1
+ATOM 581 O O . LEU A 1 74 ? -10.818 25.310 -22.621 1.00 30.54 ? 74 LEU A O 1
+ATOM 582 C CB . LEU A 1 74 ? -8.993 23.110 -21.292 1.00 24.80 ? 74 LEU A CB 1
+ATOM 583 C CG . LEU A 1 74 ? -7.924 22.318 -20.502 1.00 28.43 ? 74 LEU A CG 1
+ATOM 584 C CD1 . LEU A 1 74 ? -6.713 23.148 -20.074 1.00 26.23 ? 74 LEU A CD1 1
+ATOM 585 C CD2 . LEU A 1 74 ? -8.551 21.566 -19.346 1.00 30.79 ? 74 LEU A CD2 1
+ATOM 586 N N . PHE A 1 75 ? -9.049 25.015 -23.977 1.00 28.64 ? 75 PHE A N 1
+ATOM 587 C CA . PHE A 1 75 ? -9.737 25.376 -25.207 1.00 29.33 ? 75 PHE A CA 1
+ATOM 588 C C . PHE A 1 75 ? -9.493 24.317 -26.261 1.00 32.71 ? 75 PHE A C 1
+ATOM 589 O O . PHE A 1 75 ? -8.747 23.370 -26.012 1.00 31.45 ? 75 PHE A O 1
+ATOM 590 C CB . PHE A 1 75 ? -9.312 26.787 -25.673 1.00 32.01 ? 75 PHE A CB 1
+ATOM 591 C CG . PHE A 1 75 ? -9.629 27.853 -24.648 1.00 34.35 ? 75 PHE A CG 1
+ATOM 592 C CD1 . PHE A 1 75 ? -10.912 28.384 -24.545 1.00 37.81 ? 75 PHE A CD1 1
+ATOM 593 C CD2 . PHE A 1 75 ? -8.659 28.285 -23.745 1.00 36.24 ? 75 PHE A CD2 1
+ATOM 594 C CE1 . PHE A 1 75 ? -11.217 29.325 -23.554 1.00 38.25 ? 75 PHE A CE1 1
+ATOM 595 C CE2 . PHE A 1 75 ? -8.954 29.262 -22.788 1.00 38.64 ? 75 PHE A CE2 1
+ATOM 596 C CZ . PHE A 1 75 ? -10.231 29.774 -22.701 1.00 36.73 ? 75 PHE A CZ 1
+ATOM 597 N N . GLU A 1 76 ? -10.139 24.461 -27.416 1.00 29.75 ? 76 GLU A N 1
+ATOM 598 C CA . GLU A 1 76 ? -9.996 23.511 -28.503 1.00 29.69 ? 76 GLU A CA 1
+ATOM 599 C C . GLU A 1 76 ? -9.027 24.062 -29.530 1.00 34.61 ? 76 GLU A C 1
+ATOM 600 O O . GLU A 1 76 ? -9.225 25.170 -29.984 1.00 34.56 ? 76 GLU A O 1
+ATOM 601 C CB . GLU A 1 76 ? -11.373 23.243 -29.134 1.00 30.64 ? 76 GLU A CB 1
+ATOM 602 C CG . GLU A 1 76 ? -11.375 22.254 -30.265 1.00 38.78 ? 76 GLU A CG 1
+ATOM 603 C CD . GLU A 1 76 ? -12.744 21.882 -30.783 1.00 54.41 ? 76 GLU A CD 1
+ATOM 604 O OE1 . GLU A 1 76 ? -13.755 22.492 -30.377 1.00 49.29 ? 76 GLU A OE1 1
+ATOM 605 O OE2 . GLU A 1 76 ? -12.807 20.974 -31.631 1.00 44.48 ? 76 GLU A OE2 1
+ATOM 606 N N . ILE A 1 77 ? -7.986 23.317 -29.903 1.00 32.24 ? 77 ILE A N 1
+ATOM 607 C CA . ILE A 1 77 ? -7.066 23.807 -30.948 1.00 33.76 ? 77 ILE A CA 1
+ATOM 608 C C . ILE A 1 77 ? -7.780 23.760 -32.304 1.00 39.98 ? 77 ILE A C 1
+ATOM 609 O O . ILE A 1 77 ? -8.393 22.762 -32.640 1.00 40.37 ? 77 ILE A O 1
+ATOM 610 C CB . ILE A 1 77 ? -5.742 23.023 -30.941 1.00 37.79 ? 77 ILE A CB 1
+ATOM 611 C CG1 . ILE A 1 77 ? -4.806 23.624 -29.882 1.00 38.53 ? 77 ILE A CG1 1
+ATOM 612 C CG2 . ILE A 1 77 ? -5.066 22.995 -32.330 1.00 37.84 ? 77 ILE A CG2 1
+ATOM 613 C CD1 . ILE A 1 77 ? -3.846 22.696 -29.383 1.00 46.16 ? 77 ILE A CD1 1
+ATOM 614 N N . GLY A 1 78 ? -7.713 24.851 -33.055 1.00 37.72 ? 78 GLY A N 1
+ATOM 615 C CA . GLY A 1 78 ? -8.440 24.967 -34.313 1.00 38.45 ? 78 GLY A CA 1
+ATOM 616 C C . GLY A 1 78 ? -9.880 25.403 -34.131 1.00 41.99 ? 78 GLY A C 1
+ATOM 617 O O . GLY A 1 78 ? -10.667 25.373 -35.061 1.00 42.03 ? 78 GLY A O 1
+ATOM 618 N N . ASN A 1 79 ? -10.236 25.795 -32.897 1.00 37.42 ? 79 ASN A N 1
+ATOM 619 C CA . ASN A 1 79 ? -11.542 26.300 -32.493 1.00 36.72 ? 79 ASN A CA 1
+ATOM 620 C C . ASN A 1 79 ? -11.332 26.891 -31.106 1.00 37.77 ? 79 ASN A C 1
+ATOM 621 O O . ASN A 1 79 ? -12.029 26.546 -30.165 1.00 35.43 ? 79 ASN A O 1
+ATOM 622 C CB . ASN A 1 79 ? -12.568 25.150 -32.456 1.00 38.06 ? 79 ASN A CB 1
+ATOM 623 C CG . ASN A 1 79 ? -14.013 25.551 -32.206 1.00 49.59 ? 79 ASN A CG 1
+ATOM 624 O OD1 . ASN A 1 79 ? -14.391 26.707 -32.285 1.00 36.29 ? 79 ASN A OD1 1
+ATOM 625 N ND2 . ASN A 1 79 ? -14.836 24.585 -31.863 1.00 43.85 ? 79 ASN A ND2 1
+ATOM 626 N N . ILE A 1 80 ? -10.339 27.793 -31.010 1.00 35.65 ? 80 ILE A N 1
+ATOM 627 C CA . ILE A 1 80 ? -9.763 28.378 -29.793 1.00 35.59 ? 80 ILE A CA 1
+ATOM 628 C C . ILE A 1 80 ? -10.718 29.119 -28.865 1.00 40.61 ? 80 ILE A C 1
+ATOM 629 O O . ILE A 1 80 ? -10.391 29.313 -27.700 1.00 41.62 ? 80 ILE A O 1
+ATOM 630 C CB . ILE A 1 80 ? -8.465 29.162 -30.130 1.00 38.77 ? 80 ILE A CB 1
+ATOM 631 C CG1 . ILE A 1 80 ? -7.431 29.061 -29.009 1.00 38.89 ? 80 ILE A CG1 1
+ATOM 632 C CG2 . ILE A 1 80 ? -8.741 30.627 -30.553 1.00 40.43 ? 80 ILE A CG2 1
+ATOM 633 C CD1 . ILE A 1 80 ? -6.577 27.781 -29.013 1.00 44.30 ? 80 ILE A CD1 1
+ATOM 634 N N . ASN A 1 81 ? -11.883 29.538 -29.377 1.00 37.75 ? 81 ASN A N 1
+ATOM 635 C CA . ASN A 1 81 ? -12.892 30.233 -28.590 1.00 38.00 ? 81 ASN A CA 1
+ATOM 636 C C . ASN A 1 81 ? -13.932 29.308 -27.970 1.00 41.58 ? 81 ASN A C 1
+ATOM 637 O O . ASN A 1 81 ? -14.829 29.779 -27.279 1.00 43.05 ? 81 ASN A O 1
+ATOM 638 C CB . ASN A 1 81 ? -13.550 31.341 -29.410 1.00 38.78 ? 81 ASN A CB 1
+ATOM 639 C CG . ASN A 1 81 ? -12.610 32.475 -29.658 1.00 59.44 ? 81 ASN A CG 1
+ATOM 640 O OD1 . ASN A 1 81 ? -12.114 33.103 -28.728 1.00 61.30 ? 81 ASN A OD1 1
+ATOM 641 N ND2 . ASN A 1 81 ? -12.230 32.663 -30.897 1.00 46.82 ? 81 ASN A ND2 1
+ATOM 642 N N . ASN A 1 82 ? -13.792 28.002 -28.195 1.00 37.09 ? 82 ASN A N 1
+ATOM 643 C CA . ASN A 1 82 ? -14.675 26.988 -27.616 1.00 36.65 ? 82 ASN A CA 1
+ATOM 644 C C . ASN A 1 82 ? -14.020 26.400 -26.331 1.00 38.94 ? 82 ASN A C 1
+ATOM 645 O O . ASN A 1 82 ? -13.031 25.672 -26.442 1.00 37.14 ? 82 ASN A O 1
+ATOM 646 C CB . ASN A 1 82 ? -14.998 25.894 -28.647 1.00 35.35 ? 82 ASN A CB 1
+ATOM 647 C CG . ASN A 1 82 ? -15.810 24.743 -28.101 1.00 46.73 ? 82 ASN A CG 1
+ATOM 648 O OD1 . ASN A 1 82 ? -16.814 24.933 -27.430 1.00 33.89 ? 82 ASN A OD1 1
+ATOM 649 N ND2 . ASN A 1 82 ? -15.384 23.516 -28.374 1.00 44.54 ? 82 ASN A ND2 1
+ATOM 650 N N . PRO A 1 83 ? -14.522 26.757 -25.118 1.00 35.98 ? 83 PRO A N 1
+ATOM 651 C CA . PRO A 1 83 ? -13.911 26.228 -23.878 1.00 36.06 ? 83 PRO A CA 1
+ATOM 652 C C . PRO A 1 83 ? -14.237 24.750 -23.665 1.00 39.99 ? 83 PRO A C 1
+ATOM 653 O O . PRO A 1 83 ? -15.334 24.312 -23.992 1.00 42.50 ? 83 PRO A O 1
+ATOM 654 C CB . PRO A 1 83 ? -14.479 27.136 -22.776 1.00 37.81 ? 83 PRO A CB 1
+ATOM 655 C CG . PRO A 1 83 ? -15.764 27.634 -23.312 1.00 42.52 ? 83 PRO A CG 1
+ATOM 656 C CD . PRO A 1 83 ? -15.681 27.629 -24.822 1.00 38.05 ? 83 PRO A CD 1
+ATOM 657 N N . LEU A 1 84 ? -13.276 23.975 -23.155 1.00 35.11 ? 84 LEU A N 1
+ATOM 658 C CA . LEU A 1 84 ? -13.388 22.520 -22.992 1.00 33.91 ? 84 LEU A CA 1
+ATOM 659 C C . LEU A 1 84 ? -13.361 22.048 -21.539 1.00 34.67 ? 84 LEU A C 1
+ATOM 660 O O . LEU A 1 84 ? -13.850 20.955 -21.240 1.00 33.60 ? 84 LEU A O 1
+ATOM 661 C CB . LEU A 1 84 ? -12.226 21.866 -23.769 1.00 34.07 ? 84 LEU A CB 1
+ATOM 662 C CG . LEU A 1 84 ? -12.469 21.263 -25.171 1.00 39.07 ? 84 LEU A CG 1
+ATOM 663 C CD1 . LEU A 1 84 ? -13.364 22.109 -26.031 1.00 39.30 ? 84 LEU A CD1 1
+ATOM 664 C CD2 . LEU A 1 84 ? -11.155 21.017 -25.882 1.00 39.64 ? 84 LEU A CD2 1
+ATOM 665 N N . GLY A 1 85 ? -12.761 22.847 -20.663 1.00 28.12 ? 85 GLY A N 1
+ATOM 666 C CA . GLY A 1 85 ? -12.644 22.499 -19.253 1.00 26.80 ? 85 GLY A CA 1
+ATOM 667 C C . GLY A 1 85 ? -11.683 23.353 -18.453 1.00 27.56 ? 85 GLY A C 1
+ATOM 668 O O . GLY A 1 85 ? -11.295 24.433 -18.904 1.00 26.41 ? 85 GLY A O 1
+ATOM 669 N N . TYR A 1 86 ? -11.320 22.885 -17.241 1.00 24.06 ? 86 TYR A N 1
+ATOM 670 C CA . TYR A 1 86 ? -10.454 23.618 -16.300 1.00 25.34 ? 86 TYR A CA 1
+ATOM 671 C C . TYR A 1 86 ? -9.487 22.737 -15.557 1.00 28.86 ? 86 TYR A C 1
+ATOM 672 O O . TYR A 1 86 ? -9.875 21.700 -15.008 1.00 26.37 ? 86 TYR A O 1
+ATOM 673 C CB . TYR A 1 86 ? -11.290 24.348 -15.218 1.00 28.45 ? 86 TYR A CB 1
+ATOM 674 C CG . TYR A 1 86 ? -12.477 25.111 -15.761 1.00 32.76 ? 86 TYR A CG 1
+ATOM 675 C CD1 . TYR A 1 86 ? -12.315 26.363 -16.347 1.00 35.85 ? 86 TYR A CD1 1
+ATOM 676 C CD2 . TYR A 1 86 ? -13.754 24.551 -15.752 1.00 33.35 ? 86 TYR A CD2 1
+ATOM 677 C CE1 . TYR A 1 86 ? -13.397 27.051 -16.892 1.00 39.42 ? 86 TYR A CE1 1
+ATOM 678 C CE2 . TYR A 1 86 ? -14.843 25.226 -16.300 1.00 34.19 ? 86 TYR A CE2 1
+ATOM 679 C CZ . TYR A 1 86 ? -14.661 26.481 -16.859 1.00 45.69 ? 86 TYR A CZ 1
+ATOM 680 O OH . TYR A 1 86 ? -15.732 27.182 -17.359 1.00 49.65 ? 86 TYR A OH 1
+ATOM 681 N N . LEU A 1 87 ? -8.256 23.234 -15.423 1.00 26.22 ? 87 LEU A N 1
+ATOM 682 C CA . LEU A 1 87 ? -7.227 22.611 -14.623 1.00 26.47 ? 87 LEU A CA 1
+ATOM 683 C C . LEU A 1 87 ? -7.191 23.361 -13.330 1.00 28.23 ? 87 LEU A C 1
+ATOM 684 O O . LEU A 1 87 ? -7.060 24.582 -13.326 1.00 27.11 ? 87 LEU A O 1
+ATOM 685 C CB . LEU A 1 87 ? -5.865 22.704 -15.286 1.00 27.00 ? 87 LEU A CB 1
+ATOM 686 C CG . LEU A 1 87 ? -5.595 21.793 -16.417 1.00 32.08 ? 87 LEU A CG 1
+ATOM 687 C CD1 . LEU A 1 87 ? -4.274 22.169 -17.009 1.00 33.63 ? 87 LEU A CD1 1
+ATOM 688 C CD2 . LEU A 1 87 ? -5.582 20.339 -15.954 1.00 33.96 ? 87 LEU A CD2 1
+ATOM 689 N N . LEU A 1 88 ? -7.309 22.641 -12.230 1.00 22.92 ? 88 LEU A N 1
+ATOM 690 C CA . LEU A 1 88 ? -7.341 23.240 -10.904 1.00 21.62 ? 88 LEU A CA 1
+ATOM 691 C C . LEU A 1 88 ? -5.989 23.064 -10.206 1.00 22.14 ? 88 LEU A C 1
+ATOM 692 O O . LEU A 1 88 ? -5.842 22.177 -9.384 1.00 19.86 ? 88 LEU A O 1
+ATOM 693 C CB . LEU A 1 88 ? -8.470 22.551 -10.123 1.00 21.96 ? 88 LEU A CB 1
+ATOM 694 C CG . LEU A 1 88 ? -9.885 23.154 -10.220 1.00 26.76 ? 88 LEU A CG 1
+ATOM 695 C CD1 . LEU A 1 88 ? -10.433 23.113 -11.625 1.00 26.19 ? 88 LEU A CD1 1
+ATOM 696 C CD2 . LEU A 1 88 ? -10.831 22.413 -9.294 1.00 30.99 ? 88 LEU A CD2 1
+ATOM 697 N N . HIS A 1 89 ? -4.984 23.881 -10.579 1.00 17.99 ? 89 HIS A N 1
+ATOM 698 C CA . HIS A 1 89 ? -3.608 23.867 -10.026 1.00 17.85 ? 89 HIS A CA 1
+ATOM 699 C C . HIS A 1 89 ? -3.565 23.862 -8.504 1.00 24.44 ? 89 HIS A C 1
+ATOM 700 O O . HIS A 1 89 ? -2.731 23.166 -7.918 1.00 23.66 ? 89 HIS A O 1
+ATOM 701 C CB . HIS A 1 89 ? -2.787 25.060 -10.549 1.00 18.63 ? 89 HIS A CB 1
+ATOM 702 C CG . HIS A 1 89 ? -2.596 25.081 -12.028 1.00 21.65 ? 89 HIS A CG 1
+ATOM 703 N ND1 . HIS A 1 89 ? -1.456 24.557 -12.615 1.00 23.80 ? 89 HIS A ND1 1
+ATOM 704 C CD2 . HIS A 1 89 ? -3.394 25.576 -12.997 1.00 22.67 ? 89 HIS A CD2 1
+ATOM 705 C CE1 . HIS A 1 89 ? -1.601 24.749 -13.918 1.00 22.55 ? 89 HIS A CE1 1
+ATOM 706 N NE2 . HIS A 1 89 ? -2.741 25.361 -14.194 1.00 22.71 ? 89 HIS A NE2 1
+ATOM 707 N N . HIS A 1 90 ? -4.469 24.634 -7.866 1.00 21.43 ? 90 HIS A N 1
+ATOM 708 C CA . HIS A 1 90 ? -4.590 24.722 -6.412 1.00 22.17 ? 90 HIS A CA 1
+ATOM 709 C C . HIS A 1 90 ? -4.961 23.400 -5.751 1.00 23.17 ? 90 HIS A C 1
+ATOM 710 O O . HIS A 1 90 ? -4.717 23.235 -4.561 1.00 23.43 ? 90 HIS A O 1
+ATOM 711 C CB . HIS A 1 90 ? -5.567 25.836 -6.003 1.00 23.96 ? 90 HIS A CB 1
+ATOM 712 C CG . HIS A 1 90 ? -6.992 25.637 -6.426 1.00 27.53 ? 90 HIS A CG 1
+ATOM 713 N ND1 . HIS A 1 90 ? -7.365 25.667 -7.758 1.00 29.73 ? 90 HIS A ND1 1
+ATOM 714 C CD2 . HIS A 1 90 ? -8.106 25.520 -5.667 1.00 29.61 ? 90 HIS A CD2 1
+ATOM 715 C CE1 . HIS A 1 90 ? -8.681 25.544 -7.769 1.00 28.87 ? 90 HIS A CE1 1
+ATOM 716 N NE2 . HIS A 1 90 ? -9.175 25.457 -6.538 1.00 29.23 ? 90 HIS A NE2 1
+ATOM 717 N N . ASN A 1 91 ? -5.505 22.453 -6.517 1.00 18.53 ? 91 ASN A N 1
+ATOM 718 C CA . ASN A 1 91 ? -5.885 21.124 -6.015 1.00 18.79 ? 91 ASN A CA 1
+ATOM 719 C C . ASN A 1 91 ? -4.983 20.004 -6.535 1.00 22.21 ? 91 ASN A C 1
+ATOM 720 O O . ASN A 1 91 ? -5.330 18.820 -6.413 1.00 21.03 ? 91 ASN A O 1
+ATOM 721 C CB . ASN A 1 91 ? -7.343 20.834 -6.302 1.00 18.26 ? 91 ASN A CB 1
+ATOM 722 C CG . ASN A 1 91 ? -8.269 21.705 -5.507 1.00 33.23 ? 91 ASN A CG 1
+ATOM 723 O OD1 . ASN A 1 91 ? -7.982 22.119 -4.372 1.00 33.52 ? 91 ASN A OD1 1
+ATOM 724 N ND2 . ASN A 1 91 ? -9.361 22.067 -6.123 1.00 25.24 ? 91 ASN A ND2 1
+ATOM 725 N N . MET A 1 92 ? -3.817 20.364 -7.070 1.00 18.35 ? 92 MET A N 1
+ATOM 726 C CA . MET A 1 92 ? -2.871 19.347 -7.539 1.00 19.35 ? 92 MET A CA 1
+ATOM 727 C C . MET A 1 92 ? -2.315 18.566 -6.335 1.00 24.30 ? 92 MET A C 1
+ATOM 728 O O . MET A 1 92 ? -2.315 19.072 -5.202 1.00 22.94 ? 92 MET A O 1
+ATOM 729 C CB . MET A 1 92 ? -1.756 19.956 -8.406 1.00 21.41 ? 92 MET A CB 1
+ATOM 730 C CG . MET A 1 92 ? -0.810 20.803 -7.629 1.00 25.29 ? 92 MET A CG 1
+ATOM 731 S SD . MET A 1 92 ? 0.479 21.470 -8.663 1.00 29.96 ? 92 MET A SD 1
+ATOM 732 C CE . MET A 1 92 ? 1.521 22.182 -7.376 1.00 27.32 ? 92 MET A CE 1
+ATOM 733 N N . ILE A 1 93 ? -1.876 17.322 -6.581 1.00 20.61 ? 93 ILE A N 1
+ATOM 734 C CA . ILE A 1 93 ? -1.401 16.450 -5.520 1.00 19.61 ? 93 ILE A CA 1
+ATOM 735 C C . ILE A 1 93 ? -0.184 15.647 -5.918 1.00 25.06 ? 93 ILE A C 1
+ATOM 736 O O . ILE A 1 93 ? -0.060 15.238 -7.084 1.00 23.58 ? 93 ILE A O 1
+ATOM 737 C CB . ILE A 1 93 ? -2.559 15.473 -5.058 1.00 22.05 ? 93 ILE A CB 1
+ATOM 738 C CG1 . ILE A 1 93 ? -3.161 14.684 -6.256 1.00 22.48 ? 93 ILE A CG1 1
+ATOM 739 C CG2 . ILE A 1 93 ? -3.650 16.196 -4.211 1.00 20.56 ? 93 ILE A CG2 1
+ATOM 740 C CD1 . ILE A 1 93 ? -4.036 13.452 -5.890 1.00 25.52 ? 93 ILE A CD1 1
+ATOM 741 N N . PRO A 1 94 ? 0.674 15.296 -4.929 1.00 23.57 ? 94 PRO A N 1
+ATOM 742 C CA . PRO A 1 94 ? 1.771 14.370 -5.224 1.00 23.00 ? 94 PRO A CA 1
+ATOM 743 C C . PRO A 1 94 ? 1.205 12.941 -5.199 1.00 26.70 ? 94 PRO A C 1
+ATOM 744 O O . PRO A 1 94 ? 0.430 12.584 -4.296 1.00 26.78 ? 94 PRO A O 1
+ATOM 745 C CB . PRO A 1 94 ? 2.756 14.629 -4.079 1.00 24.40 ? 94 PRO A CB 1
+ATOM 746 C CG . PRO A 1 94 ? 1.897 15.028 -2.933 1.00 28.16 ? 94 PRO A CG 1
+ATOM 747 C CD . PRO A 1 94 ? 0.652 15.663 -3.494 1.00 24.22 ? 94 PRO A CD 1
+ATOM 748 N N . VAL A 1 95 ? 1.540 12.138 -6.213 1.00 22.38 ? 95 VAL A N 1
+ATOM 749 C CA . VAL A 1 95 ? 1.032 10.766 -6.286 1.00 21.74 ? 95 VAL A CA 1
+ATOM 750 C C . VAL A 1 95 ? 2.203 9.794 -6.434 1.00 26.29 ? 95 VAL A C 1
+ATOM 751 O O . VAL A 1 95 ? 2.963 9.900 -7.406 1.00 23.83 ? 95 VAL A O 1
+ATOM 752 C CB . VAL A 1 95 ? -0.029 10.549 -7.424 1.00 23.83 ? 95 VAL A CB 1
+ATOM 753 C CG1 . VAL A 1 95 ? -0.557 9.102 -7.421 1.00 22.87 ? 95 VAL A CG1 1
+ATOM 754 C CG2 . VAL A 1 95 ? -1.183 11.535 -7.313 1.00 23.10 ? 95 VAL A CG2 1
+ATOM 755 N N . PRO A 1 96 ? 2.347 8.820 -5.507 1.00 26.26 ? 96 PRO A N 1
+ATOM 756 C CA . PRO A 1 96 ? 3.422 7.812 -5.667 1.00 26.32 ? 96 PRO A CA 1
+ATOM 757 C C . PRO A 1 96 ? 3.131 6.977 -6.910 1.00 31.04 ? 96 PRO A C 1
+ATOM 758 O O . PRO A 1 96 ? 1.970 6.828 -7.290 1.00 28.59 ? 96 PRO A O 1
+ATOM 759 C CB . PRO A 1 96 ? 3.295 6.951 -4.404 1.00 27.50 ? 96 PRO A CB 1
+ATOM 760 C CG . PRO A 1 96 ? 2.428 7.730 -3.465 1.00 31.59 ? 96 PRO A CG 1
+ATOM 761 C CD . PRO A 1 96 ? 1.511 8.533 -4.327 1.00 26.87 ? 96 PRO A CD 1
+ATOM 762 N N . ASP A 1 97 ? 4.177 6.473 -7.565 1.00 30.56 ? 97 ASP A N 1
+ATOM 763 C CA . ASP A 1 97 ? 4.071 5.654 -8.774 1.00 31.14 ? 97 ASP A CA 1
+ATOM 764 C C . ASP A 1 97 ? 3.010 4.529 -8.689 1.00 32.05 ? 97 ASP A C 1
+ATOM 765 O O . ASP A 1 97 ? 2.311 4.276 -9.666 1.00 31.58 ? 97 ASP A O 1
+ATOM 766 C CB . ASP A 1 97 ? 5.449 5.059 -9.125 1.00 34.36 ? 97 ASP A CB 1
+ATOM 767 C CG . ASP A 1 97 ? 6.533 6.066 -9.483 1.00 59.39 ? 97 ASP A CG 1
+ATOM 768 O OD1 . ASP A 1 97 ? 6.276 6.942 -10.350 1.00 62.84 ? 97 ASP A OD1 1
+ATOM 769 O OD2 . ASP A 1 97 ? 7.656 5.950 -8.934 1.00 70.14 ? 97 ASP A OD2 1
+ATOM 770 N N . SER A 1 98 ? 2.909 3.864 -7.529 1.00 26.94 ? 98 SER A N 1
+ATOM 771 C CA . SER A 1 98 ? 1.999 2.736 -7.288 1.00 27.00 ? 98 SER A CA 1
+ATOM 772 C C . SER A 1 98 ? 0.514 3.065 -7.334 1.00 31.17 ? 98 SER A C 1
+ATOM 773 O O . SER A 1 98 ? -0.300 2.172 -7.602 1.00 32.64 ? 98 SER A O 1
+ATOM 774 C CB . SER A 1 98 ? 2.317 2.085 -5.947 1.00 29.06 ? 98 SER A CB 1
+ATOM 775 O OG . SER A 1 98 ? 2.071 2.993 -4.886 1.00 37.68 ? 98 SER A OG 1
+ATOM 776 N N . GLU A 1 99 ? 0.153 4.325 -7.040 1.00 26.88 ? 99 GLU A N 1
+ATOM 777 C CA . GLU A 1 99 ? -1.248 4.758 -6.954 1.00 25.45 ? 99 GLU A CA 1
+ATOM 778 C C . GLU A 1 99 ? -1.768 5.429 -8.210 1.00 26.02 ? 99 GLU A C 1
+ATOM 779 O O . GLU A 1 99 ? -2.941 5.775 -8.290 1.00 23.95 ? 99 GLU A O 1
+ATOM 780 C CB . GLU A 1 99 ? -1.440 5.626 -5.683 1.00 26.86 ? 99 GLU A CB 1
+ATOM 781 C CG . GLU A 1 99 ? -0.941 4.952 -4.404 1.00 35.15 ? 99 GLU A CG 1
+ATOM 782 C CD . GLU A 1 99 ? -1.403 3.521 -4.168 1.00 61.92 ? 99 GLU A CD 1
+ATOM 783 O OE1 . GLU A 1 99 ? -0.537 2.616 -4.160 1.00 56.01 ? 99 GLU A OE1 1
+ATOM 784 O OE2 . GLU A 1 99 ? -2.625 3.301 -3.993 1.00 54.00 ? 99 GLU A OE2 1
+ATOM 785 N N . LEU A 1 100 ? -0.895 5.585 -9.211 1.00 25.17 ? 100 LEU A N 1
+ATOM 786 C CA . LEU A 1 100 ? -1.222 6.209 -10.487 1.00 25.73 ? 100 LEU A CA 1
+ATOM 787 C C . LEU A 1 100 ? -1.831 5.191 -11.459 1.00 27.59 ? 100 LEU A C 1
+ATOM 788 O O . LEU A 1 100 ? -1.234 4.150 -11.698 1.00 27.28 ? 100 LEU A O 1
+ATOM 789 C CB . LEU A 1 100 ? 0.057 6.772 -11.094 1.00 26.38 ? 100 LEU A CB 1
+ATOM 790 C CG . LEU A 1 100 ? 0.275 8.265 -11.114 1.00 32.48 ? 100 LEU A CG 1
+ATOM 791 C CD1 . LEU A 1 100 ? 1.098 8.600 -12.325 1.00 34.00 ? 100 LEU A CD1 1
+ATOM 792 C CD2 . LEU A 1 100 ? -1.055 9.088 -11.095 1.00 32.90 ? 100 LEU A CD2 1
+ATOM 793 N N . ILE A 1 101 ? -3.011 5.490 -12.029 1.00 22.65 ? 101 ILE A N 1
+ATOM 794 C CA . ILE A 1 101 ? -3.669 4.554 -12.928 1.00 22.78 ? 101 ILE A CA 1
+ATOM 795 C C . ILE A 1 101 ? -3.891 5.192 -14.276 1.00 27.22 ? 101 ILE A C 1
+ATOM 796 O O . ILE A 1 101 ? -4.727 6.087 -14.379 1.00 27.36 ? 101 ILE A O 1
+ATOM 797 C CB . ILE A 1 101 ? -4.986 4.000 -12.303 1.00 26.22 ? 101 ILE A CB 1
+ATOM 798 C CG1 . ILE A 1 101 ? -4.742 3.455 -10.871 1.00 27.79 ? 101 ILE A CG1 1
+ATOM 799 C CG2 . ILE A 1 101 ? -5.617 2.933 -13.212 1.00 23.44 ? 101 ILE A CG2 1
+ATOM 800 C CD1 . ILE A 1 101 ? -5.996 3.310 -10.028 1.00 42.84 ? 101 ILE A CD1 1
+ATOM 801 N N . PRO A 1 102 ? -3.188 4.745 -15.337 1.00 24.73 ? 102 PRO A N 1
+ATOM 802 C CA . PRO A 1 102 ? -3.412 5.347 -16.665 1.00 24.86 ? 102 PRO A CA 1
+ATOM 803 C C . PRO A 1 102 ? -4.882 5.276 -17.091 1.00 30.61 ? 102 PRO A C 1
+ATOM 804 O O . PRO A 1 102 ? -5.559 4.291 -16.797 1.00 31.08 ? 102 PRO A O 1
+ATOM 805 C CB . PRO A 1 102 ? -2.516 4.514 -17.585 1.00 26.19 ? 102 PRO A CB 1
+ATOM 806 C CG . PRO A 1 102 ? -1.466 3.979 -16.696 1.00 30.98 ? 102 PRO A CG 1
+ATOM 807 C CD . PRO A 1 102 ? -2.150 3.691 -15.398 1.00 26.73 ? 102 PRO A CD 1
+ATOM 808 N N . LEU A 1 103 ? -5.395 6.334 -17.715 1.00 27.68 ? 103 LEU A N 1
+ATOM 809 C CA . LEU A 1 103 ? -6.797 6.325 -18.099 1.00 28.48 ? 103 LEU A CA 1
+ATOM 810 C C . LEU A 1 103 ? -7.025 5.984 -19.568 1.00 32.73 ? 103 LEU A C 1
+ATOM 811 O O . LEU A 1 103 ? -6.693 6.778 -20.448 1.00 32.85 ? 103 LEU A O 1
+ATOM 812 C CB . LEU A 1 103 ? -7.517 7.612 -17.677 1.00 28.69 ? 103 LEU A CB 1
+ATOM 813 C CG . LEU A 1 103 ? -8.960 7.761 -18.122 1.00 33.73 ? 103 LEU A CG 1
+ATOM 814 C CD1 . LEU A 1 103 ? -9.914 7.075 -17.154 1.00 35.04 ? 103 LEU A CD1 1
+ATOM 815 C CD2 . LEU A 1 103 ? -9.311 9.206 -18.264 1.00 35.57 ? 103 LEU A CD2 1
+ATOM 816 N N . PRO A 1 104 ? -7.632 4.815 -19.843 1.00 29.81 ? 104 PRO A N 1
+ATOM 817 C CA . PRO A 1 104 ? -7.908 4.443 -21.240 1.00 29.74 ? 104 PRO A CA 1
+ATOM 818 C C . PRO A 1 104 ? -9.116 5.202 -21.780 1.00 33.62 ? 104 PRO A C 1
+ATOM 819 O O . PRO A 1 104 ? -10.117 5.369 -21.076 1.00 31.89 ? 104 PRO A O 1
+ATOM 820 C CB . PRO A 1 104 ? -8.172 2.927 -21.162 1.00 31.54 ? 104 PRO A CB 1
+ATOM 821 C CG . PRO A 1 104 ? -7.862 2.527 -19.729 1.00 36.01 ? 104 PRO A CG 1
+ATOM 822 C CD . PRO A 1 104 ? -8.076 3.754 -18.921 1.00 31.22 ? 104 PRO A CD 1
+ATOM 823 N N . LEU A 1 105 ? -8.993 5.713 -23.013 1.00 31.31 ? 105 LEU A N 1
+ATOM 824 C CA . LEU A 1 105 ? -10.082 6.435 -23.647 1.00 31.35 ? 105 LEU A CA 1
+ATOM 825 C C . LEU A 1 105 ? -10.639 5.606 -24.766 1.00 38.99 ? 105 LEU A C 1
+ATOM 826 O O . LEU A 1 105 ? -9.886 5.042 -25.566 1.00 39.35 ? 105 LEU A O 1
+ATOM 827 C CB . LEU A 1 105 ? -9.654 7.806 -24.216 1.00 30.92 ? 105 LEU A CB 1
+ATOM 828 C CG . LEU A 1 105 ? -9.198 8.895 -23.244 1.00 35.68 ? 105 LEU A CG 1
+ATOM 829 C CD1 . LEU A 1 105 ? -8.772 10.132 -24.009 1.00 36.00 ? 105 LEU A CD1 1
+ATOM 830 C CD2 . LEU A 1 105 ? -10.303 9.270 -22.247 1.00 37.53 ? 105 LEU A CD2 1
+ATOM 831 N N . ASP A 1 106 ? -11.960 5.556 -24.830 1.00 37.34 ? 106 ASP A N 1
+ATOM 832 C CA . ASP A 1 106 ? -12.709 4.917 -25.898 1.00 38.52 ? 106 ASP A CA 1
+ATOM 833 C C . ASP A 1 106 ? -13.190 6.091 -26.765 1.00 44.43 ? 106 ASP A C 1
+ATOM 834 O O . ASP A 1 106 ? -14.153 6.766 -26.410 1.00 44.13 ? 106 ASP A O 1
+ATOM 835 C CB . ASP A 1 106 ? -13.878 4.101 -25.311 1.00 40.85 ? 106 ASP A CB 1
+ATOM 836 C CG . ASP A 1 106 ? -14.899 3.599 -26.321 1.00 55.95 ? 106 ASP A CG 1
+ATOM 837 O OD1 . ASP A 1 106 ? -14.499 3.272 -27.468 1.00 62.92 ? 106 ASP A OD1 1
+ATOM 838 O OD2 . ASP A 1 106 ? -16.091 3.525 -25.965 1.00 56.74 ? 106 ASP A OD2 1
+ATOM 839 N N . LEU A 1 107 ? -12.480 6.368 -27.870 1.00 43.71 ? 107 LEU A N 1
+ATOM 840 C CA . LEU A 1 107 ? -12.798 7.484 -28.766 1.00 45.74 ? 107 LEU A CA 1
+ATOM 841 C C . LEU A 1 107 ? -14.162 7.391 -29.475 1.00 53.61 ? 107 LEU A C 1
+ATOM 842 O O . LEU A 1 107 ? -14.575 8.345 -30.136 1.00 52.89 ? 107 LEU A O 1
+ATOM 843 C CB . LEU A 1 107 ? -11.668 7.756 -29.769 1.00 46.13 ? 107 LEU A CB 1
+ATOM 844 C CG . LEU A 1 107 ? -10.276 8.102 -29.212 1.00 51.40 ? 107 LEU A CG 1
+ATOM 845 C CD1 . LEU A 1 107 ? -9.393 8.579 -30.323 1.00 52.42 ? 107 LEU A CD1 1
+ATOM 846 C CD2 . LEU A 1 107 ? -10.321 9.171 -28.099 1.00 51.45 ? 107 LEU A CD2 1
+ATOM 847 N N . LYS A 1 108 ? -14.869 6.261 -29.301 1.00 52.69 ? 108 LYS A N 1
+ATOM 848 C CA . LYS A 1 108 ? -16.212 6.053 -29.835 1.00 53.43 ? 108 LYS A CA 1
+ATOM 849 C C . LYS A 1 108 ? -17.181 6.918 -29.003 1.00 57.93 ? 108 LYS A C 1
+ATOM 850 O O . LYS A 1 108 ? -18.175 7.410 -29.540 1.00 58.12 ? 108 LYS A O 1
+ATOM 851 C CB . LYS A 1 108 ? -16.588 4.562 -29.771 1.00 55.97 ? 108 LYS A CB 1
+ATOM 852 N N . LYS A 1 109 ? -16.852 7.138 -27.704 1.00 53.30 ? 109 LYS A N 1
+ATOM 853 C CA . LYS A 1 109 ? -17.619 7.969 -26.772 1.00 52.82 ? 109 LYS A CA 1
+ATOM 854 C C . LYS A 1 109 ? -17.302 9.455 -27.023 1.00 56.07 ? 109 LYS A C 1
+ATOM 855 O O . LYS A 1 109 ? -16.118 9.813 -27.022 1.00 54.61 ? 109 LYS A O 1
+ATOM 856 C CB . LYS A 1 109 ? -17.267 7.637 -25.309 1.00 55.15 ? 109 LYS A CB 1
+ATOM 857 C CG . LYS A 1 109 ? -17.690 6.263 -24.828 1.00 65.79 ? 109 LYS A CG 1
+ATOM 858 C CD . LYS A 1 109 ? -17.295 6.081 -23.375 1.00 74.41 ? 109 LYS A CD 1
+ATOM 859 C CE . LYS A 1 109 ? -17.200 4.629 -22.977 1.00 86.52 ? 109 LYS A CE 1
+ATOM 860 N NZ . LYS A 1 109 ? -16.631 4.472 -21.610 1.00 95.46 ? 109 LYS A NZ 1
+ATOM 861 N N . PRO A 1 110 ? -18.334 10.336 -27.190 1.00 51.95 ? 110 PRO A N 1
+ATOM 862 C CA . PRO A 1 110 ? -18.060 11.774 -27.409 1.00 50.90 ? 110 PRO A CA 1
+ATOM 863 C C . PRO A 1 110 ? -17.387 12.457 -26.219 1.00 50.57 ? 110 PRO A C 1
+ATOM 864 O O . PRO A 1 110 ? -16.694 13.457 -26.402 1.00 49.73 ? 110 PRO A O 1
+ATOM 865 C CB . PRO A 1 110 ? -19.452 12.369 -27.683 1.00 53.20 ? 110 PRO A CB 1
+ATOM 866 C CG . PRO A 1 110 ? -20.317 11.195 -28.044 1.00 58.23 ? 110 PRO A CG 1
+ATOM 867 C CD . PRO A 1 110 ? -19.784 10.067 -27.214 1.00 53.76 ? 110 PRO A CD 1
+ATOM 868 N N . LYS A 1 111 ? -17.607 11.907 -25.010 1.00 45.03 ? 111 LYS A N 1
+ATOM 869 C CA . LYS A 1 111 ? -17.036 12.319 -23.726 1.00 44.17 ? 111 LYS A CA 1
+ATOM 870 C C . LYS A 1 111 ? -15.504 12.214 -23.820 1.00 44.08 ? 111 LYS A C 1
+ATOM 871 O O . LYS A 1 111 ? -14.789 13.165 -23.512 1.00 42.00 ? 111 LYS A O 1
+ATOM 872 C CB . LYS A 1 111 ? -17.552 11.357 -22.630 1.00 47.58 ? 111 LYS A CB 1
+ATOM 873 C CG . LYS A 1 111 ? -17.649 11.926 -21.221 1.00 68.05 ? 111 LYS A CG 1
+ATOM 874 C CD . LYS A 1 111 ? -17.920 10.795 -20.219 1.00 81.62 ? 111 LYS A CD 1
+ATOM 875 C CE . LYS A 1 111 ? -19.177 10.994 -19.405 1.00 98.51 ? 111 LYS A CE 1
+ATOM 876 N NZ . LYS A 1 111 ? -18.873 11.499 -18.038 1.00 109.50 ? 111 LYS A NZ 1
+ATOM 877 N N . HIS A 1 112 ? -15.019 11.050 -24.276 1.00 40.15 ? 112 HIS A N 1
+ATOM 878 C CA . HIS A 1 112 ? -13.603 10.738 -24.423 1.00 39.80 ? 112 HIS A CA 1
+ATOM 879 C C . HIS A 1 112 ? -12.990 11.437 -25.622 1.00 41.61 ? 112 HIS A C 1
+ATOM 880 O O . HIS A 1 112 ? -11.809 11.763 -25.580 1.00 39.61 ? 112 HIS A O 1
+ATOM 881 C CB . HIS A 1 112 ? -13.390 9.224 -24.478 1.00 40.75 ? 112 HIS A CB 1
+ATOM 882 C CG . HIS A 1 112 ? -13.746 8.507 -23.206 1.00 44.23 ? 112 HIS A CG 1
+ATOM 883 N ND1 . HIS A 1 112 ? -14.358 9.158 -22.144 1.00 46.33 ? 112 HIS A ND1 1
+ATOM 884 C CD2 . HIS A 1 112 ? -13.571 7.210 -22.876 1.00 46.11 ? 112 HIS A CD2 1
+ATOM 885 C CE1 . HIS A 1 112 ? -14.534 8.239 -21.212 1.00 46.03 ? 112 HIS A CE1 1
+ATOM 886 N NE2 . HIS A 1 112 ? -14.069 7.050 -21.606 1.00 46.41 ? 112 HIS A NE2 1
+ATOM 887 N N . LYS A 1 113 ? -13.795 11.686 -26.671 1.00 39.03 ? 113 LYS A N 1
+ATOM 888 C CA . LYS A 1 113 ? -13.392 12.407 -27.886 1.00 39.76 ? 113 LYS A CA 1
+ATOM 889 C C . LYS A 1 113 ? -13.035 13.873 -27.524 1.00 43.11 ? 113 LYS A C 1
+ATOM 890 O O . LYS A 1 113 ? -12.123 14.455 -28.108 1.00 42.69 ? 113 LYS A O 1
+ATOM 891 C CB . LYS A 1 113 ? -14.523 12.355 -28.926 1.00 42.79 ? 113 LYS A CB 1
+ATOM 892 C CG . LYS A 1 113 ? -14.038 12.467 -30.368 1.00 61.18 ? 113 LYS A CG 1
+ATOM 893 C CD . LYS A 1 113 ? -15.176 12.215 -31.357 1.00 76.02 ? 113 LYS A CD 1
+ATOM 894 C CE . LYS A 1 113 ? -14.930 10.999 -32.220 1.00 91.44 ? 113 LYS A CE 1
+ATOM 895 N NZ . LYS A 1 113 ? -16.004 9.979 -32.061 1.00 100.73 ? 113 LYS A NZ 1
+ATOM 896 N N . MET A 1 114 ? -13.749 14.439 -26.542 1.00 40.94 ? 114 MET A N 1
+ATOM 897 C CA . MET A 1 114 ? -13.542 15.776 -26.006 1.00 41.97 ? 114 MET A CA 1
+ATOM 898 C C . MET A 1 114 ? -12.312 15.763 -25.091 1.00 41.03 ? 114 MET A C 1
+ATOM 899 O O . MET A 1 114 ? -11.538 16.726 -25.093 1.00 39.17 ? 114 MET A O 1
+ATOM 900 C CB . MET A 1 114 ? -14.794 16.230 -25.249 1.00 46.26 ? 114 MET A CB 1
+ATOM 901 C CG . MET A 1 114 ? -14.720 17.663 -24.748 1.00 52.75 ? 114 MET A CG 1
+ATOM 902 S SD . MET A 1 114 ? -15.436 17.847 -23.099 1.00 60.17 ? 114 MET A SD 1
+ATOM 903 C CE . MET A 1 114 ? -14.332 16.849 -22.134 1.00 56.68 ? 114 MET A CE 1
+ATOM 904 N N . MET A 1 115 ? -12.107 14.662 -24.331 1.00 36.19 ? 115 MET A N 1
+ATOM 905 C CA . MET A 1 115 ? -10.921 14.524 -23.477 1.00 34.65 ? 115 MET A CA 1
+ATOM 906 C C . MET A 1 115 ? -9.666 14.546 -24.343 1.00 34.53 ? 115 MET A C 1
+ATOM 907 O O . MET A 1 115 ? -8.722 15.255 -24.016 1.00 34.21 ? 115 MET A O 1
+ATOM 908 C CB . MET A 1 115 ? -10.969 13.254 -22.645 1.00 37.78 ? 115 MET A CB 1
+ATOM 909 C CG . MET A 1 115 ? -12.052 13.277 -21.610 1.00 43.63 ? 115 MET A CG 1
+ATOM 910 S SD . MET A 1 115 ? -11.668 12.151 -20.271 1.00 50.81 ? 115 MET A SD 1
+ATOM 911 C CE . MET A 1 115 ? -10.790 13.288 -19.173 1.00 48.13 ? 115 MET A CE 1
+ATOM 912 N N . GLN A 1 116 ? -9.693 13.842 -25.488 1.00 29.45 ? 116 GLN A N 1
+ATOM 913 C CA . GLN A 1 116 ? -8.593 13.787 -26.447 1.00 29.28 ? 116 GLN A CA 1
+ATOM 914 C C . GLN A 1 116 ? -8.205 15.226 -26.837 1.00 33.38 ? 116 GLN A C 1
+ATOM 915 O O . GLN A 1 116 ? -7.032 15.597 -26.730 1.00 32.98 ? 116 GLN A O 1
+ATOM 916 C CB . GLN A 1 116 ? -9.025 12.951 -27.667 1.00 31.00 ? 116 GLN A CB 1
+ATOM 917 C CG . GLN A 1 116 ? -7.949 12.727 -28.740 1.00 56.70 ? 116 GLN A CG 1
+ATOM 918 C CD . GLN A 1 116 ? -8.471 12.106 -30.030 1.00 84.52 ? 116 GLN A CD 1
+ATOM 919 O OE1 . GLN A 1 116 ? -7.747 11.389 -30.726 1.00 83.15 ? 116 GLN A OE1 1
+ATOM 920 N NE2 . GLN A 1 116 ? -9.714 12.393 -30.414 1.00 79.72 ? 116 GLN A NE2 1
+ATOM 921 N N . LYS A 1 117 ? -9.226 16.051 -27.184 1.00 28.97 ? 117 LYS A N 1
+ATOM 922 C CA . LYS A 1 117 ? -9.105 17.459 -27.571 1.00 28.55 ? 117 LYS A CA 1
+ATOM 923 C C . LYS A 1 117 ? -8.505 18.291 -26.442 1.00 29.16 ? 117 LYS A C 1
+ATOM 924 O O . LYS A 1 117 ? -7.652 19.132 -26.708 1.00 26.92 ? 117 LYS A O 1
+ATOM 925 C CB . LYS A 1 117 ? -10.469 18.024 -28.013 1.00 31.74 ? 117 LYS A CB 1
+ATOM 926 C CG . LYS A 1 117 ? -10.953 17.428 -29.327 1.00 44.63 ? 117 LYS A CG 1
+ATOM 927 C CD . LYS A 1 117 ? -12.350 17.891 -29.685 1.00 54.46 ? 117 LYS A CD 1
+ATOM 928 C CE . LYS A 1 117 ? -12.729 17.462 -31.086 1.00 65.93 ? 117 LYS A CE 1
+ATOM 929 N NZ . LYS A 1 117 ? -11.875 18.109 -32.128 1.00 67.22 ? 117 LYS A NZ 1
+ATOM 930 N N . GLN A 1 118 ? -8.928 18.037 -25.185 1.00 24.94 ? 118 GLN A N 1
+ATOM 931 C CA . GLN A 1 118 ? -8.376 18.718 -24.004 1.00 24.74 ? 118 GLN A CA 1
+ATOM 932 C C . GLN A 1 118 ? -6.871 18.439 -23.849 1.00 27.38 ? 118 GLN A C 1
+ATOM 933 O O . GLN A 1 118 ? -6.122 19.353 -23.514 1.00 26.49 ? 118 GLN A O 1
+ATOM 934 C CB . GLN A 1 118 ? -9.082 18.266 -22.727 1.00 25.74 ? 118 GLN A CB 1
+ATOM 935 C CG . GLN A 1 118 ? -10.522 18.745 -22.601 1.00 37.71 ? 118 GLN A CG 1
+ATOM 936 C CD . GLN A 1 118 ? -11.165 18.167 -21.368 1.00 46.47 ? 118 GLN A CD 1
+ATOM 937 O OE1 . GLN A 1 118 ? -11.033 16.972 -21.059 1.00 39.55 ? 118 GLN A OE1 1
+ATOM 938 N NE2 . GLN A 1 118 ? -11.900 18.994 -20.654 1.00 37.55 ? 118 GLN A NE2 1
+ATOM 939 N N . LEU A 1 119 ? -6.451 17.173 -24.038 1.00 24.34 ? 119 LEU A N 1
+ATOM 940 C CA . LEU A 1 119 ? -5.048 16.743 -23.960 1.00 24.34 ? 119 LEU A CA 1
+ATOM 941 C C . LEU A 1 119 ? -4.220 17.352 -25.074 1.00 29.63 ? 119 LEU A C 1
+ATOM 942 O O . LEU A 1 119 ? -3.121 17.821 -24.790 1.00 29.86 ? 119 LEU A O 1
+ATOM 943 C CB . LEU A 1 119 ? -4.931 15.216 -24.025 1.00 24.07 ? 119 LEU A CB 1
+ATOM 944 C CG . LEU A 1 119 ? -3.615 14.608 -23.557 1.00 27.41 ? 119 LEU A CG 1
+ATOM 945 C CD1 . LEU A 1 119 ? -3.253 15.063 -22.137 1.00 23.68 ? 119 LEU A CD1 1
+ATOM 946 C CD2 . LEU A 1 119 ? -3.723 13.113 -23.589 1.00 27.52 ? 119 LEU A CD2 1
+ATOM 947 N N . ILE A 1 120 ? -4.718 17.356 -26.339 1.00 26.40 ? 120 ILE A N 1
+ATOM 948 C CA . ILE A 1 120 ? -3.938 18.011 -27.408 1.00 27.55 ? 120 ILE A CA 1
+ATOM 949 C C . ILE A 1 120 ? -3.683 19.500 -27.062 1.00 29.91 ? 120 ILE A C 1
+ATOM 950 O O . ILE A 1 120 ? -2.567 19.984 -27.256 1.00 30.12 ? 120 ILE A O 1
+ATOM 951 C CB . ILE A 1 120 ? -4.350 17.741 -28.900 1.00 31.85 ? 120 ILE A CB 1
+ATOM 952 C CG1 . ILE A 1 120 ? -4.970 18.950 -29.606 1.00 33.04 ? 120 ILE A CG1 1
+ATOM 953 C CG2 . ILE A 1 120 ? -5.135 16.443 -29.132 1.00 33.83 ? 120 ILE A CG2 1
+ATOM 954 C CD1 . ILE A 1 120 ? -4.287 19.270 -30.895 1.00 44.34 ? 120 ILE A CD1 1
+ATOM 955 N N . TYR A 1 121 ? -4.704 20.190 -26.483 1.00 23.48 ? 121 TYR A N 1
+ATOM 956 C CA . TYR A 1 121 ? -4.563 21.577 -26.073 1.00 21.77 ? 121 TYR A CA 1
+ATOM 957 C C . TYR A 1 121 ? -3.536 21.714 -24.949 1.00 25.02 ? 121 TYR A C 1
+ATOM 958 O O . TYR A 1 121 ? -2.647 22.551 -25.034 1.00 22.43 ? 121 TYR A O 1
+ATOM 959 C CB . TYR A 1 121 ? -5.895 22.215 -25.676 1.00 21.40 ? 121 TYR A CB 1
+ATOM 960 C CG . TYR A 1 121 ? -5.723 23.670 -25.287 1.00 20.37 ? 121 TYR A CG 1
+ATOM 961 C CD1 . TYR A 1 121 ? -5.459 24.644 -26.250 1.00 22.84 ? 121 TYR A CD1 1
+ATOM 962 C CD2 . TYR A 1 121 ? -5.753 24.063 -23.954 1.00 19.61 ? 121 TYR A CD2 1
+ATOM 963 C CE1 . TYR A 1 121 ? -5.245 25.973 -25.894 1.00 23.20 ? 121 TYR A CE1 1
+ATOM 964 C CE2 . TYR A 1 121 ? -5.518 25.382 -23.585 1.00 19.75 ? 121 TYR A CE2 1
+ATOM 965 C CZ . TYR A 1 121 ? -5.269 26.335 -24.558 1.00 24.73 ? 121 TYR A CZ 1
+ATOM 966 O OH . TYR A 1 121 ? -5.103 27.646 -24.203 1.00 24.66 ? 121 TYR A OH 1
+ATOM 967 N N . MET A 1 122 ? -3.659 20.877 -23.921 1.00 23.77 ? 122 MET A N 1
+ATOM 968 C CA . MET A 1 122 ? -2.757 20.861 -22.761 1.00 23.82 ? 122 MET A CA 1
+ATOM 969 C C . MET A 1 122 ? -1.304 20.631 -23.166 1.00 28.61 ? 122 MET A C 1
+ATOM 970 O O . MET A 1 122 ? -0.424 21.338 -22.685 1.00 28.51 ? 122 MET A O 1
+ATOM 971 C CB . MET A 1 122 ? -3.219 19.819 -21.750 1.00 25.33 ? 122 MET A CB 1
+ATOM 972 C CG . MET A 1 122 ? -4.454 20.244 -21.018 1.00 28.20 ? 122 MET A CG 1
+ATOM 973 S SD . MET A 1 122 ? -4.862 19.071 -19.720 1.00 31.14 ? 122 MET A SD 1
+ATOM 974 C CE . MET A 1 122 ? -3.513 19.344 -18.711 1.00 29.63 ? 122 MET A CE 1
+ATOM 975 N N . LYS A 1 123 ? -1.068 19.707 -24.113 1.00 25.62 ? 123 LYS A N 1
+ATOM 976 C CA . LYS A 1 123 ? 0.277 19.435 -24.650 1.00 25.83 ? 123 LYS A CA 1
+ATOM 977 C C . LYS A 1 123 ? 0.861 20.657 -25.342 1.00 27.53 ? 123 LYS A C 1
+ATOM 978 O O . LYS A 1 123 ? 2.033 20.956 -25.124 1.00 25.87 ? 123 LYS A O 1
+ATOM 979 C CB . LYS A 1 123 ? 0.273 18.233 -25.606 1.00 28.13 ? 123 LYS A CB 1
+ATOM 980 C CG . LYS A 1 123 ? 0.164 16.905 -24.892 1.00 33.29 ? 123 LYS A CG 1
+ATOM 981 C CD . LYS A 1 123 ? 0.737 15.814 -25.774 1.00 46.34 ? 123 LYS A CD 1
+ATOM 982 C CE . LYS A 1 123 ? 0.565 14.457 -25.165 1.00 56.75 ? 123 LYS A CE 1
+ATOM 983 N NZ . LYS A 1 123 ? -0.775 13.890 -25.438 1.00 74.12 ? 123 LYS A NZ 1
+ATOM 984 N N . SER A 1 124 ? 0.024 21.415 -26.105 1.00 24.66 ? 124 SER A N 1
+ATOM 985 C CA . SER A 1 124 ? 0.437 22.644 -26.783 1.00 24.84 ? 124 SER A CA 1
+ATOM 986 C C . SER A 1 124 ? 0.777 23.781 -25.799 1.00 29.53 ? 124 SER A C 1
+ATOM 987 O O . SER A 1 124 ? 1.500 24.710 -26.171 1.00 30.75 ? 124 SER A O 1
+ATOM 988 C CB . SER A 1 124 ? -0.640 23.109 -27.761 1.00 29.74 ? 124 SER A CB 1
+ATOM 989 O OG . SER A 1 124 ? -1.703 23.786 -27.101 1.00 37.69 ? 124 SER A OG 1
+ATOM 990 N N . ILE A 1 125 ? 0.194 23.747 -24.582 1.00 25.27 ? 125 ILE A N 1
+ATOM 991 C CA . ILE A 1 125 ? 0.449 24.755 -23.538 1.00 24.36 ? 125 ILE A CA 1
+ATOM 992 C C . ILE A 1 125 ? 1.163 24.129 -22.305 1.00 25.38 ? 125 ILE A C 1
+ATOM 993 O O . ILE A 1 125 ? 0.997 24.619 -21.190 1.00 26.99 ? 125 ILE A O 1
+ATOM 994 C CB . ILE A 1 125 ? -0.845 25.562 -23.170 1.00 28.12 ? 125 ILE A CB 1
+ATOM 995 C CG1 . ILE A 1 125 ? -1.911 24.699 -22.450 1.00 28.16 ? 125 ILE A CG1 1
+ATOM 996 C CG2 . ILE A 1 125 ? -1.433 26.278 -24.398 1.00 28.96 ? 125 ILE A CG2 1
+ATOM 997 C CD1 . ILE A 1 125 ? -2.708 25.460 -21.369 1.00 29.66 ? 125 ILE A CD1 1
+ATOM 998 N N . SER A 1 126 ? 1.957 23.056 -22.507 1.00 20.13 ? 126 SER A N 1
+ATOM 999 C CA . SER A 1 126 ? 2.646 22.360 -21.410 1.00 20.56 ? 126 SER A CA 1
+ATOM 1000 C C . SER A 1 126 ? 3.614 23.224 -20.613 1.00 25.77 ? 126 SER A C 1
+ATOM 1001 O O . SER A 1 126 ? 3.709 23.031 -19.406 1.00 25.87 ? 126 SER A O 1
+ATOM 1002 C CB . SER A 1 126 ? 3.309 21.071 -21.888 1.00 23.30 ? 126 SER A CB 1
+ATOM 1003 O OG . SER A 1 126 ? 4.254 21.363 -22.898 1.00 33.07 ? 126 SER A OG 1
+ATOM 1004 N N . GLU A 1 127 ? 4.306 24.192 -21.267 1.00 24.48 ? 127 GLU A N 1
+ATOM 1005 C CA . GLU A 1 127 ? 5.215 25.134 -20.585 1.00 24.59 ? 127 GLU A CA 1
+ATOM 1006 C C . GLU A 1 127 ? 4.426 26.039 -19.595 1.00 26.77 ? 127 GLU A C 1
+ATOM 1007 O O . GLU A 1 127 ? 4.878 26.298 -18.483 1.00 26.58 ? 127 GLU A O 1
+ATOM 1008 C CB . GLU A 1 127 ? 5.947 26.001 -21.613 1.00 26.46 ? 127 GLU A CB 1
+ATOM 1009 C CG . GLU A 1 127 ? 7.142 26.721 -21.016 1.00 42.72 ? 127 GLU A CG 1
+ATOM 1010 C CD . GLU A 1 127 ? 7.916 27.657 -21.926 1.00 81.04 ? 127 GLU A CD 1
+ATOM 1011 O OE1 . GLU A 1 127 ? 7.743 27.584 -23.166 1.00 84.39 ? 127 GLU A OE1 1
+ATOM 1012 O OE2 . GLU A 1 127 ? 8.695 28.478 -21.387 1.00 79.43 ? 127 GLU A OE2 1
+ATOM 1013 N N . LYS A 1 128 ? 3.259 26.516 -20.015 1.00 23.00 ? 128 LYS A N 1
+ATOM 1014 C CA . LYS A 1 128 ? 2.401 27.353 -19.182 1.00 22.24 ? 128 LYS A CA 1
+ATOM 1015 C C . LYS A 1 128 ? 1.877 26.506 -18.026 1.00 24.22 ? 128 LYS A C 1
+ATOM 1016 O O . LYS A 1 128 ? 1.879 26.977 -16.902 1.00 23.74 ? 128 LYS A O 1
+ATOM 1017 C CB . LYS A 1 128 ? 1.235 27.869 -20.017 1.00 23.48 ? 128 LYS A CB 1
+ATOM 1018 C CG . LYS A 1 128 ? 0.154 28.559 -19.241 1.00 25.81 ? 128 LYS A CG 1
+ATOM 1019 C CD . LYS A 1 128 ? -1.045 28.695 -20.139 1.00 37.58 ? 128 LYS A CD 1
+ATOM 1020 C CE . LYS A 1 128 ? -2.097 29.535 -19.517 1.00 40.80 ? 128 LYS A CE 1
+ATOM 1021 N NZ . LYS A 1 128 ? -1.904 30.954 -19.872 1.00 55.47 ? 128 LYS A NZ 1
+ATOM 1022 N N . ILE A 1 129 ? 1.468 25.251 -18.304 1.00 22.47 ? 129 ILE A N 1
+ATOM 1023 C CA . ILE A 1 129 ? 0.964 24.331 -17.267 1.00 20.96 ? 129 ILE A CA 1
+ATOM 1024 C C . ILE A 1 129 ? 2.031 24.097 -16.227 1.00 26.18 ? 129 ILE A C 1
+ATOM 1025 O O . ILE A 1 129 ? 1.761 24.222 -15.030 1.00 26.21 ? 129 ILE A O 1
+ATOM 1026 C CB . ILE A 1 129 ? 0.402 23.012 -17.870 1.00 22.15 ? 129 ILE A CB 1
+ATOM 1027 C CG1 . ILE A 1 129 ? -0.857 23.320 -18.701 1.00 22.81 ? 129 ILE A CG1 1
+ATOM 1028 C CG2 . ILE A 1 129 ? 0.074 21.994 -16.761 1.00 20.85 ? 129 ILE A CG2 1
+ATOM 1029 C CD1 . ILE A 1 129 ? -1.354 22.197 -19.503 1.00 28.09 ? 129 ILE A CD1 1
+ATOM 1030 N N . GLU A 1 130 ? 3.244 23.762 -16.683 1.00 24.76 ? 130 GLU A N 1
+ATOM 1031 C CA . GLU A 1 130 ? 4.382 23.492 -15.800 1.00 24.91 ? 130 GLU A CA 1
+ATOM 1032 C C . GLU A 1 130 ? 4.739 24.716 -14.961 1.00 25.34 ? 130 GLU A C 1
+ATOM 1033 O O . GLU A 1 130 ? 4.839 24.587 -13.741 1.00 24.80 ? 130 GLU A O 1
+ATOM 1034 C CB . GLU A 1 130 ? 5.590 22.974 -16.594 1.00 26.99 ? 130 GLU A CB 1
+ATOM 1035 C CG . GLU A 1 130 ? 5.422 21.531 -17.060 1.00 49.69 ? 130 GLU A CG 1
+ATOM 1036 C CD . GLU A 1 130 ? 6.534 20.902 -17.884 1.00 79.26 ? 130 GLU A CD 1
+ATOM 1037 O OE1 . GLU A 1 130 ? 7.554 21.578 -18.158 1.00 84.76 ? 130 GLU A OE1 1
+ATOM 1038 O OE2 . GLU A 1 130 ? 6.383 19.716 -18.252 1.00 74.83 ? 130 GLU A OE2 1
+ATOM 1039 N N . ASN A 1 131 ? 4.797 25.909 -15.594 1.00 21.70 ? 131 ASN A N 1
+ATOM 1040 C CA . ASN A 1 131 ? 5.124 27.177 -14.914 1.00 22.87 ? 131 ASN A CA 1
+ATOM 1041 C C . ASN A 1 131 ? 4.081 27.682 -13.947 1.00 24.62 ? 131 ASN A C 1
+ATOM 1042 O O . ASN A 1 131 ? 4.441 28.122 -12.858 1.00 23.93 ? 131 ASN A O 1
+ATOM 1043 C CB . ASN A 1 131 ? 5.558 28.250 -15.875 1.00 23.31 ? 131 ASN A CB 1
+ATOM 1044 C CG . ASN A 1 131 ? 6.979 28.037 -16.320 1.00 38.58 ? 131 ASN A CG 1
+ATOM 1045 O OD1 . ASN A 1 131 ? 7.910 28.487 -15.676 1.00 35.77 ? 131 ASN A OD1 1
+ATOM 1046 N ND2 . ASN A 1 131 ? 7.177 27.309 -17.404 1.00 25.90 ? 131 ASN A ND2 1
+ATOM 1047 N N . LYS A 1 132 ? 2.804 27.560 -14.297 1.00 21.28 ? 132 LYS A N 1
+ATOM 1048 C CA . LYS A 1 132 ? 1.736 27.958 -13.383 1.00 21.78 ? 132 LYS A CA 1
+ATOM 1049 C C . LYS A 1 132 ? 1.659 27.048 -12.157 1.00 25.28 ? 132 LYS A C 1
+ATOM 1050 O O . LYS A 1 132 ? 1.314 27.518 -11.084 1.00 23.91 ? 132 LYS A O 1
+ATOM 1051 C CB . LYS A 1 132 ? 0.371 28.021 -14.065 1.00 24.45 ? 132 LYS A CB 1
+ATOM 1052 C CG . LYS A 1 132 ? -0.552 28.896 -13.236 1.00 30.28 ? 132 LYS A CG 1
+ATOM 1053 C CD . LYS A 1 132 ? -1.969 28.549 -13.343 1.00 37.07 ? 132 LYS A CD 1
+ATOM 1054 C CE . LYS A 1 132 ? -2.590 29.295 -14.465 1.00 32.85 ? 132 LYS A CE 1
+ATOM 1055 N NZ . LYS A 1 132 ? -3.923 29.790 -14.098 1.00 37.57 ? 132 LYS A NZ 1
+ATOM 1056 N N . SER A 1 133 ? 1.949 25.743 -12.321 1.00 22.30 ? 133 SER A N 1
+ATOM 1057 C CA . SER A 1 133 ? 1.984 24.806 -11.193 1.00 21.42 ? 133 SER A CA 1
+ATOM 1058 C C . SER A 1 133 ? 3.087 25.208 -10.222 1.00 24.03 ? 133 SER A C 1
+ATOM 1059 O O . SER A 1 133 ? 2.864 25.202 -9.011 1.00 23.73 ? 133 SER A O 1
+ATOM 1060 C CB . SER A 1 133 ? 2.146 23.372 -11.682 1.00 22.80 ? 133 SER A CB 1
+ATOM 1061 O OG . SER A 1 133 ? 0.944 23.021 -12.348 1.00 30.69 ? 133 SER A OG 1
+ATOM 1062 N N . GLU A 1 134 ? 4.246 25.610 -10.759 1.00 21.43 ? 134 GLU A N 1
+ATOM 1063 C CA . GLU A 1 134 ? 5.414 26.096 -10.016 1.00 21.96 ? 134 GLU A CA 1
+ATOM 1064 C C . GLU A 1 134 ? 5.065 27.365 -9.267 1.00 23.75 ? 134 GLU A C 1
+ATOM 1065 O O . GLU A 1 134 ? 5.391 27.447 -8.090 1.00 22.57 ? 134 GLU A O 1
+ATOM 1066 C CB . GLU A 1 134 ? 6.585 26.396 -10.966 1.00 24.11 ? 134 GLU A CB 1
+ATOM 1067 C CG . GLU A 1 134 ? 7.838 25.611 -10.673 1.00 38.73 ? 134 GLU A CG 1
+ATOM 1068 C CD . GLU A 1 134 ? 9.021 26.145 -11.456 1.00 72.25 ? 134 GLU A CD 1
+ATOM 1069 O OE1 . GLU A 1 134 ? 9.810 26.919 -10.867 1.00 68.94 ? 134 GLU A OE1 1
+ATOM 1070 O OE2 . GLU A 1 134 ? 9.141 25.824 -12.662 1.00 68.76 ? 134 GLU A OE2 1
+ATOM 1071 N N . VAL A 1 135 ? 4.421 28.358 -9.943 1.00 20.06 ? 135 VAL A N 1
+ATOM 1072 C CA . VAL A 1 135 ? 3.978 29.597 -9.285 1.00 20.76 ? 135 VAL A CA 1
+ATOM 1073 C C . VAL A 1 135 ? 3.045 29.218 -8.110 1.00 23.41 ? 135 VAL A C 1
+ATOM 1074 O O . VAL A 1 135 ? 3.284 29.614 -6.996 1.00 23.48 ? 135 VAL A O 1
+ATOM 1075 C CB . VAL A 1 135 ? 3.276 30.579 -10.264 1.00 25.64 ? 135 VAL A CB 1
+ATOM 1076 C CG1 . VAL A 1 135 ? 2.590 31.727 -9.516 1.00 24.85 ? 135 VAL A CG1 1
+ATOM 1077 C CG2 . VAL A 1 135 ? 4.257 31.139 -11.285 1.00 26.14 ? 135 VAL A CG2 1
+ATOM 1078 N N . VAL A 1 136 ? 2.032 28.420 -8.351 1.00 20.95 ? 136 VAL A N 1
+ATOM 1079 C CA . VAL A 1 136 ? 1.064 28.010 -7.310 1.00 21.36 ? 136 VAL A CA 1
+ATOM 1080 C C . VAL A 1 136 ? 1.796 27.314 -6.130 1.00 25.78 ? 136 VAL A C 1
+ATOM 1081 O O . VAL A 1 136 ? 1.543 27.637 -4.964 1.00 25.35 ? 136 VAL A O 1
+ATOM 1082 C CB . VAL A 1 136 ? -0.066 27.130 -7.925 1.00 23.57 ? 136 VAL A CB 1
+ATOM 1083 C CG1 . VAL A 1 136 ? -0.978 26.567 -6.851 1.00 22.68 ? 136 VAL A CG1 1
+ATOM 1084 C CG2 . VAL A 1 136 ? -0.881 27.925 -8.946 1.00 23.03 ? 136 VAL A CG2 1
+ATOM 1085 N N . TYR A 1 137 ? 2.718 26.395 -6.451 1.00 21.47 ? 137 TYR A N 1
+ATOM 1086 C CA . TYR A 1 137 ? 3.506 25.648 -5.454 1.00 20.90 ? 137 TYR A CA 1
+ATOM 1087 C C . TYR A 1 137 ? 4.315 26.585 -4.557 1.00 24.18 ? 137 TYR A C 1
+ATOM 1088 O O . TYR A 1 137 ? 4.171 26.527 -3.336 1.00 22.75 ? 137 TYR A O 1
+ATOM 1089 C CB . TYR A 1 137 ? 4.424 24.642 -6.150 1.00 21.93 ? 137 TYR A CB 1
+ATOM 1090 C CG . TYR A 1 137 ? 5.152 23.705 -5.212 1.00 25.95 ? 137 TYR A CG 1
+ATOM 1091 C CD1 . TYR A 1 137 ? 4.546 22.541 -4.751 1.00 27.73 ? 137 TYR A CD1 1
+ATOM 1092 C CD2 . TYR A 1 137 ? 6.463 23.959 -4.819 1.00 27.53 ? 137 TYR A CD2 1
+ATOM 1093 C CE1 . TYR A 1 137 ? 5.225 21.655 -3.917 1.00 29.20 ? 137 TYR A CE1 1
+ATOM 1094 C CE2 . TYR A 1 137 ? 7.154 23.076 -3.987 1.00 28.43 ? 137 TYR A CE2 1
+ATOM 1095 C CZ . TYR A 1 137 ? 6.527 21.931 -3.533 1.00 34.16 ? 137 TYR A CZ 1
+ATOM 1096 O OH . TYR A 1 137 ? 7.196 21.061 -2.711 1.00 37.46 ? 137 TYR A OH 1
+ATOM 1097 N N . ARG A 1 138 ? 5.109 27.483 -5.163 1.00 21.29 ? 138 ARG A N 1
+ATOM 1098 C CA . ARG A 1 138 ? 5.969 28.422 -4.451 1.00 21.78 ? 138 ARG A CA 1
+ATOM 1099 C C . ARG A 1 138 ? 5.178 29.438 -3.635 1.00 27.68 ? 138 ARG A C 1
+ATOM 1100 O O . ARG A 1 138 ? 5.497 29.650 -2.459 1.00 28.04 ? 138 ARG A O 1
+ATOM 1101 C CB . ARG A 1 138 ? 6.933 29.127 -5.413 1.00 19.65 ? 138 ARG A CB 1
+ATOM 1102 C CG . ARG A 1 138 ? 7.942 28.192 -6.069 1.00 19.53 ? 138 ARG A CG 1
+ATOM 1103 C CD . ARG A 1 138 ? 8.941 29.016 -6.846 1.00 28.64 ? 138 ARG A CD 1
+ATOM 1104 N NE . ARG A 1 138 ? 9.679 28.243 -7.851 1.00 31.01 ? 138 ARG A NE 1
+ATOM 1105 C CZ . ARG A 1 138 ? 10.996 28.084 -7.849 1.00 56.25 ? 138 ARG A CZ 1
+ATOM 1106 N NH1 . ARG A 1 138 ? 11.736 28.585 -6.869 1.00 57.64 ? 138 ARG A NH1 1
+ATOM 1107 N NH2 . ARG A 1 138 ? 11.584 27.397 -8.819 1.00 47.53 ? 138 ARG A NH2 1
+ATOM 1108 N N . LYS A 1 139 ? 4.145 30.041 -4.233 1.00 23.19 ? 139 LYS A N 1
+ATOM 1109 C CA . LYS A 1 139 ? 3.304 31.036 -3.535 1.00 24.52 ? 139 LYS A CA 1
+ATOM 1110 C C . LYS A 1 139 ? 2.599 30.437 -2.317 1.00 29.83 ? 139 LYS A C 1
+ATOM 1111 O O . LYS A 1 139 ? 2.571 31.070 -1.268 1.00 30.82 ? 139 LYS A O 1
+ATOM 1112 C CB . LYS A 1 139 ? 2.286 31.673 -4.494 1.00 26.08 ? 139 LYS A CB 1
+ATOM 1113 C CG . LYS A 1 139 ? 2.925 32.596 -5.537 1.00 31.15 ? 139 LYS A CG 1
+ATOM 1114 C CD . LYS A 1 139 ? 2.788 34.062 -5.180 1.00 29.73 ? 139 LYS A CD 1
+ATOM 1115 C CE . LYS A 1 139 ? 3.577 34.950 -6.105 1.00 38.86 ? 139 LYS A CE 1
+ATOM 1116 N NZ . LYS A 1 139 ? 3.521 36.370 -5.666 1.00 49.05 ? 139 LYS A NZ 1
+ATOM 1117 N N . ALA A 1 140 ? 2.093 29.199 -2.431 1.00 27.07 ? 140 ALA A N 1
+ATOM 1118 C CA . ALA A 1 140 ? 1.396 28.549 -1.302 1.00 27.19 ? 140 ALA A CA 1
+ATOM 1119 C C . ALA A 1 140 ? 2.311 27.933 -0.234 1.00 34.39 ? 140 ALA A C 1
+ATOM 1120 O O . ALA A 1 140 ? 2.032 28.059 0.962 1.00 33.77 ? 140 ALA A O 1
+ATOM 1121 C CB . ALA A 1 140 ? 0.431 27.490 -1.821 1.00 26.92 ? 140 ALA A CB 1
+ATOM 1122 N N . ALA A 1 141 ? 3.354 27.206 -0.671 1.00 32.73 ? 141 ALA A N 1
+ATOM 1123 C CA . ALA A 1 141 ? 4.249 26.467 0.220 1.00 32.85 ? 141 ALA A CA 1
+ATOM 1124 C C . ALA A 1 141 ? 5.504 27.184 0.683 1.00 38.37 ? 141 ALA A C 1
+ATOM 1125 O O . ALA A 1 141 ? 5.984 26.898 1.782 1.00 39.35 ? 141 ALA A O 1
+ATOM 1126 C CB . ALA A 1 141 ? 4.613 25.141 -0.423 1.00 33.62 ? 141 ALA A CB 1
+ATOM 1127 N N . HIS A 1 142 ? 6.056 28.100 -0.123 1.00 34.67 ? 142 HIS A N 1
+ATOM 1128 C CA . HIS A 1 142 ? 7.295 28.790 0.235 1.00 35.47 ? 142 HIS A CA 1
+ATOM 1129 C C . HIS A 1 142 ? 7.081 30.248 0.653 1.00 41.92 ? 142 HIS A C 1
+ATOM 1130 O O . HIS A 1 142 ? 7.642 30.679 1.658 1.00 41.44 ? 142 HIS A O 1
+ATOM 1131 C CB . HIS A 1 142 ? 8.322 28.704 -0.909 1.00 36.68 ? 142 HIS A CB 1
+ATOM 1132 C CG . HIS A 1 142 ? 8.760 27.304 -1.260 1.00 40.76 ? 142 HIS A CG 1
+ATOM 1133 N ND1 . HIS A 1 142 ? 9.485 27.060 -2.400 1.00 42.99 ? 142 HIS A ND1 1
+ATOM 1134 C CD2 . HIS A 1 142 ? 8.577 26.133 -0.614 1.00 43.19 ? 142 HIS A CD2 1
+ATOM 1135 C CE1 . HIS A 1 142 ? 9.722 25.756 -2.423 1.00 42.72 ? 142 HIS A CE1 1
+ATOM 1136 N NE2 . HIS A 1 142 ? 9.184 25.163 -1.358 1.00 43.02 ? 142 HIS A NE2 1
+ATOM 1137 N N . GLU A 1 143 ? 6.296 30.998 -0.134 1.00 37.14 ? 143 GLU A N 1
+ATOM 1138 C CA . GLU A 1 143 ? 6.013 32.406 0.098 1.00 37.31 ? 143 GLU A CA 1
+ATOM 1139 C C . GLU A 1 143 ? 4.924 32.574 1.138 1.00 43.07 ? 143 GLU A C 1
+ATOM 1140 O O . GLU A 1 143 ? 4.915 33.583 1.845 1.00 42.90 ? 143 GLU A O 1
+ATOM 1141 C CB . GLU A 1 143 ? 5.565 33.073 -1.206 1.00 38.77 ? 143 GLU A CB 1
+ATOM 1142 C CG . GLU A 1 143 ? 5.984 34.508 -1.353 1.00 52.20 ? 143 GLU A CG 1
+ATOM 1143 C CD . GLU A 1 143 ? 5.650 35.165 -2.680 1.00 74.13 ? 143 GLU A CD 1
+ATOM 1144 O OE1 . GLU A 1 143 ? 5.242 36.344 -2.663 1.00 70.87 ? 143 GLU A OE1 1
+ATOM 1145 O OE2 . GLU A 1 143 ? 5.841 34.536 -3.743 1.00 69.95 ? 143 GLU A OE2 1
+ATOM 1146 N N . LYS A 1 144 ? 3.995 31.602 1.216 1.00 41.37 ? 144 LYS A N 1
+ATOM 1147 C CA . LYS A 1 144 ? 2.862 31.630 2.137 1.00 41.66 ? 144 LYS A CA 1
+ATOM 1148 C C . LYS A 1 144 ? 1.941 32.843 1.842 1.00 45.44 ? 144 LYS A C 1
+ATOM 1149 O O . LYS A 1 144 ? 1.337 33.402 2.754 1.00 45.34 ? 144 LYS A O 1
+ATOM 1150 C CB . LYS A 1 144 ? 3.332 31.567 3.614 1.00 44.43 ? 144 LYS A CB 1
+ATOM 1151 C CG . LYS A 1 144 ? 3.122 30.218 4.329 1.00 55.56 ? 144 LYS A CG 1
+ATOM 1152 C CD . LYS A 1 144 ? 4.126 29.074 4.030 1.00 65.22 ? 144 LYS A CD 1
+ATOM 1153 C CE . LYS A 1 144 ? 5.588 29.458 4.073 1.00 82.46 ? 144 LYS A CE 1
+ATOM 1154 N NZ . LYS A 1 144 ? 6.026 30.050 5.376 1.00 92.24 ? 144 LYS A NZ 1
+ATOM 1155 N N . ASP A 1 145 ? 1.832 33.205 0.535 1.00 41.25 ? 145 ASP A N 1
+ATOM 1156 C CA . ASP A 1 145 ? 0.969 34.272 -0.024 1.00 39.64 ? 145 ASP A CA 1
+ATOM 1157 C C . ASP A 1 145 ? -0.471 33.935 0.306 1.00 42.26 ? 145 ASP A C 1
+ATOM 1158 O O . ASP A 1 145 ? -0.917 32.814 0.053 1.00 41.93 ? 145 ASP A O 1
+ATOM 1159 C CB . ASP A 1 145 ? 1.142 34.379 -1.550 1.00 40.22 ? 145 ASP A CB 1
+ATOM 1160 C CG . ASP A 1 145 ? 0.266 35.402 -2.260 1.00 48.06 ? 145 ASP A CG 1
+ATOM 1161 O OD1 . ASP A 1 145 ? -0.967 35.175 -2.353 1.00 48.51 ? 145 ASP A OD1 1
+ATOM 1162 O OD2 . ASP A 1 145 ? 0.824 36.371 -2.819 1.00 50.04 ? 145 ASP A OD2 1
+ATOM 1163 N N . GLY A 1 146 ? -1.163 34.925 0.865 1.00 37.75 ? 146 GLY A N 1
+ATOM 1164 C CA . GLY A 1 146 ? -2.545 34.859 1.320 1.00 36.50 ? 146 GLY A CA 1
+ATOM 1165 C C . GLY A 1 146 ? -3.532 34.180 0.402 1.00 37.17 ? 146 GLY A C 1
+ATOM 1166 O O . GLY A 1 146 ? -4.194 33.232 0.815 1.00 37.33 ? 146 GLY A O 1
+ATOM 1167 N N . TYR A 1 147 ? -3.638 34.662 -0.844 1.00 32.13 ? 147 TYR A N 1
+ATOM 1168 C CA . TYR A 1 147 ? -4.595 34.143 -1.816 1.00 30.75 ? 147 TYR A CA 1
+ATOM 1169 C C . TYR A 1 147 ? -4.344 32.675 -2.167 1.00 33.47 ? 147 TYR A C 1
+ATOM 1170 O O . TYR A 1 147 ? -5.278 31.877 -2.186 1.00 33.75 ? 147 TYR A O 1
+ATOM 1171 C CB . TYR A 1 147 ? -4.671 35.043 -3.073 1.00 30.69 ? 147 TYR A CB 1
+ATOM 1172 C CG . TYR A 1 147 ? -5.637 34.536 -4.129 1.00 30.22 ? 147 TYR A CG 1
+ATOM 1173 C CD1 . TYR A 1 147 ? -6.973 34.914 -4.118 1.00 31.19 ? 147 TYR A CD1 1
+ATOM 1174 C CD2 . TYR A 1 147 ? -5.210 33.671 -5.135 1.00 30.19 ? 147 TYR A CD2 1
+ATOM 1175 C CE1 . TYR A 1 147 ? -7.863 34.451 -5.083 1.00 32.88 ? 147 TYR A CE1 1
+ATOM 1176 C CE2 . TYR A 1 147 ? -6.095 33.177 -6.088 1.00 30.79 ? 147 TYR A CE2 1
+ATOM 1177 C CZ . TYR A 1 147 ? -7.420 33.575 -6.063 1.00 39.51 ? 147 TYR A CZ 1
+ATOM 1178 O OH . TYR A 1 147 ? -8.287 33.093 -7.010 1.00 39.21 ? 147 TYR A OH 1
+ATOM 1179 N N . TYR A 1 148 ? -3.089 32.331 -2.442 1.00 28.66 ? 148 TYR A N 1
+ATOM 1180 C CA . TYR A 1 148 ? -2.707 30.978 -2.825 1.00 27.74 ? 148 TYR A CA 1
+ATOM 1181 C C . TYR A 1 148 ? -2.809 29.967 -1.685 1.00 31.44 ? 148 TYR A C 1
+ATOM 1182 O O . TYR A 1 148 ? -3.301 28.863 -1.916 1.00 30.40 ? 148 TYR A O 1
+ATOM 1183 C CB . TYR A 1 148 ? -1.307 30.971 -3.442 1.00 28.28 ? 148 TYR A CB 1
+ATOM 1184 C CG . TYR A 1 148 ? -1.221 31.683 -4.775 1.00 28.37 ? 148 TYR A CG 1
+ATOM 1185 C CD1 . TYR A 1 148 ? -1.096 33.068 -4.846 1.00 29.54 ? 148 TYR A CD1 1
+ATOM 1186 C CD2 . TYR A 1 148 ? -1.158 30.962 -5.962 1.00 29.09 ? 148 TYR A CD2 1
+ATOM 1187 C CE1 . TYR A 1 148 ? -0.956 33.722 -6.070 1.00 31.54 ? 148 TYR A CE1 1
+ATOM 1188 C CE2 . TYR A 1 148 ? -1.023 31.601 -7.192 1.00 30.58 ? 148 TYR A CE2 1
+ATOM 1189 C CZ . TYR A 1 148 ? -0.927 32.982 -7.243 1.00 40.09 ? 148 TYR A CZ 1
+ATOM 1190 O OH . TYR A 1 148 ? -0.781 33.596 -8.460 1.00 42.21 ? 148 TYR A OH 1
+ATOM 1191 N N . LEU A 1 149 ? -2.341 30.330 -0.473 1.00 29.35 ? 149 LEU A N 1
+ATOM 1192 C CA . LEU A 1 149 ? -2.345 29.462 0.719 1.00 30.93 ? 149 LEU A CA 1
+ATOM 1193 C C . LEU A 1 149 ? -3.744 28.977 1.041 1.00 34.15 ? 149 LEU A C 1
+ATOM 1194 O O . LEU A 1 149 ? -3.933 27.788 1.276 1.00 33.18 ? 149 LEU A O 1
+ATOM 1195 C CB . LEU A 1 149 ? -1.822 30.234 1.949 1.00 31.98 ? 149 LEU A CB 1
+ATOM 1196 C CG . LEU A 1 149 ? -0.566 29.748 2.675 1.00 38.08 ? 149 LEU A CG 1
+ATOM 1197 C CD1 . LEU A 1 149 ? -0.346 30.590 3.906 1.00 38.71 ? 149 LEU A CD1 1
+ATOM 1198 C CD2 . LEU A 1 149 ? -0.681 28.279 3.114 1.00 40.45 ? 149 LEU A CD2 1
+ATOM 1199 N N . LYS A 1 150 ? -4.721 29.911 1.054 1.00 31.08 ? 150 LYS A N 1
+ATOM 1200 C CA . LYS A 1 150 ? -6.121 29.639 1.371 1.00 30.51 ? 150 LYS A CA 1
+ATOM 1201 C C . LYS A 1 150 ? -6.870 28.746 0.371 1.00 33.17 ? 150 LYS A C 1
+ATOM 1202 O O . LYS A 1 150 ? -7.788 28.024 0.770 1.00 34.00 ? 150 LYS A O 1
+ATOM 1203 C CB . LYS A 1 150 ? -6.877 30.937 1.678 1.00 32.21 ? 150 LYS A CB 1
+ATOM 1204 C CG . LYS A 1 150 ? -7.256 31.789 0.470 1.00 40.09 ? 150 LYS A CG 1
+ATOM 1205 C CD . LYS A 1 150 ? -8.016 33.021 0.916 1.00 45.57 ? 150 LYS A CD 1
+ATOM 1206 C CE . LYS A 1 150 ? -8.665 33.727 -0.239 1.00 51.50 ? 150 LYS A CE 1
+ATOM 1207 N NZ . LYS A 1 150 ? -9.853 32.984 -0.724 1.00 53.42 ? 150 LYS A NZ 1
+ATOM 1208 N N . PHE A 1 151 ? -6.507 28.825 -0.920 1.00 29.05 ? 151 PHE A N 1
+ATOM 1209 C CA . PHE A 1 151 ? -7.131 28.023 -1.986 1.00 28.09 ? 151 PHE A CA 1
+ATOM 1210 C C . PHE A 1 151 ? -6.434 26.718 -2.245 1.00 30.55 ? 151 PHE A C 1
+ATOM 1211 O O . PHE A 1 151 ? -7.044 25.775 -2.740 1.00 30.84 ? 151 PHE A O 1
+ATOM 1212 C CB . PHE A 1 151 ? -7.194 28.804 -3.313 1.00 29.44 ? 151 PHE A CB 1
+ATOM 1213 C CG . PHE A 1 151 ? -8.459 29.609 -3.484 1.00 30.88 ? 151 PHE A CG 1
+ATOM 1214 C CD1 . PHE A 1 151 ? -9.695 28.980 -3.586 1.00 32.80 ? 151 PHE A CD1 1
+ATOM 1215 C CD2 . PHE A 1 151 ? -8.420 30.999 -3.511 1.00 34.44 ? 151 PHE A CD2 1
+ATOM 1216 C CE1 . PHE A 1 151 ? -10.870 29.727 -3.726 1.00 36.01 ? 151 PHE A CE1 1
+ATOM 1217 C CE2 . PHE A 1 151 ? -9.597 31.745 -3.670 1.00 35.27 ? 151 PHE A CE2 1
+ATOM 1218 C CZ . PHE A 1 151 ? -10.814 31.102 -3.765 1.00 33.83 ? 151 PHE A CZ 1
+ATOM 1219 N N . SER A 1 152 ? -5.165 26.657 -1.966 1.00 28.24 ? 152 SER A N 1
+ATOM 1220 C CA . SER A 1 152 ? -4.454 25.449 -2.319 1.00 29.69 ? 152 SER A CA 1
+ATOM 1221 C C . SER A 1 152 ? -4.281 24.439 -1.240 1.00 32.28 ? 152 SER A C 1
+ATOM 1222 O O . SER A 1 152 ? -4.439 24.747 -0.059 1.00 29.95 ? 152 SER A O 1
+ATOM 1223 C CB . SER A 1 152 ? -3.143 25.764 -3.030 1.00 36.20 ? 152 SER A CB 1
+ATOM 1224 O OG . SER A 1 152 ? -2.345 26.585 -2.200 1.00 52.95 ? 152 SER A OG 1
+ATOM 1225 N N . CYS A 1 153 ? -4.024 23.196 -1.669 1.00 31.11 ? 153 CYS A N 1
+ATOM 1226 C CA . CYS A 1 153 ? -3.738 22.038 -0.835 1.00 32.51 ? 153 CYS A CA 1
+ATOM 1227 C C . CYS A 1 153 ? -2.493 22.386 -0.045 1.00 34.81 ? 153 CYS A C 1
+ATOM 1228 O O . CYS A 1 153 ? -1.650 23.153 -0.527 1.00 33.99 ? 153 CYS A O 1
+ATOM 1229 C CB . CYS A 1 153 ? -3.483 20.815 -1.713 1.00 34.09 ? 153 CYS A CB 1
+ATOM 1230 S SG . CYS A 1 153 ? -4.965 20.112 -2.492 1.00 39.12 ? 153 CYS A SG 1
+ATOM 1231 N N . ASP A 1 154 ? -2.338 21.807 1.141 1.00 30.53 ? 154 ASP A N 1
+ATOM 1232 C CA . ASP A 1 154 ? -1.117 22.017 1.916 1.00 28.59 ? 154 ASP A CA 1
+ATOM 1233 C C . ASP A 1 154 ? -0.127 21.039 1.256 1.00 29.85 ? 154 ASP A C 1
+ATOM 1234 O O . ASP A 1 154 ? -0.060 19.878 1.653 1.00 29.56 ? 154 ASP A O 1
+ATOM 1235 C CB . ASP A 1 154 ? -1.374 21.693 3.399 1.00 30.15 ? 154 ASP A CB 1
+ATOM 1236 C CG . ASP A 1 154 ? -0.203 21.948 4.332 1.00 40.08 ? 154 ASP A CG 1
+ATOM 1237 O OD1 . ASP A 1 154 ? 0.935 22.101 3.832 1.00 40.42 ? 154 ASP A OD1 1
+ATOM 1238 O OD2 . ASP A 1 154 ? -0.420 21.947 5.573 1.00 43.25 ? 154 ASP A OD2 1
+ATOM 1239 N N . PHE A 1 155 ? 0.554 21.499 0.173 1.00 23.95 ? 155 PHE A N 1
+ATOM 1240 C CA . PHE A 1 155 ? 1.463 20.701 -0.652 1.00 22.60 ? 155 PHE A CA 1
+ATOM 1241 C C . PHE A 1 155 ? 2.530 19.920 0.101 1.00 28.53 ? 155 PHE A C 1
+ATOM 1242 O O . PHE A 1 155 ? 2.743 18.747 -0.191 1.00 28.77 ? 155 PHE A O 1
+ATOM 1243 C CB . PHE A 1 155 ? 2.056 21.529 -1.807 1.00 23.43 ? 155 PHE A CB 1
+ATOM 1244 C CG . PHE A 1 155 ? 1.036 22.098 -2.765 1.00 23.40 ? 155 PHE A CG 1
+ATOM 1245 C CD1 . PHE A 1 155 ? 0.116 21.269 -3.403 1.00 23.52 ? 155 PHE A CD1 1
+ATOM 1246 C CD2 . PHE A 1 155 ? 1.018 23.456 -3.059 1.00 24.48 ? 155 PHE A CD2 1
+ATOM 1247 C CE1 . PHE A 1 155 ? -0.848 21.800 -4.257 1.00 24.03 ? 155 PHE A CE1 1
+ATOM 1248 C CE2 . PHE A 1 155 ? 0.047 23.988 -3.918 1.00 27.60 ? 155 PHE A CE2 1
+ATOM 1249 C CZ . PHE A 1 155 ? -0.867 23.152 -4.528 1.00 24.41 ? 155 PHE A CZ 1
+ATOM 1250 N N . LYS A 1 156 ? 3.201 20.567 1.060 1.00 28.09 ? 156 LYS A N 1
+ATOM 1251 C CA . LYS A 1 156 ? 4.248 19.955 1.879 1.00 27.60 ? 156 LYS A CA 1
+ATOM 1252 C C . LYS A 1 156 ? 3.780 18.843 2.803 1.00 30.92 ? 156 LYS A C 1
+ATOM 1253 O O . LYS A 1 156 ? 4.460 17.819 2.922 1.00 29.84 ? 156 LYS A O 1
+ATOM 1254 C CB . LYS A 1 156 ? 5.038 21.027 2.614 1.00 30.35 ? 156 LYS A CB 1
+ATOM 1255 C CG . LYS A 1 156 ? 6.361 21.334 1.919 1.00 43.43 ? 156 LYS A CG 1
+ATOM 1256 C CD . LYS A 1 156 ? 6.280 22.005 0.570 1.00 47.97 ? 156 LYS A CD 1
+ATOM 1257 C CE . LYS A 1 156 ? 7.598 22.657 0.228 1.00 51.27 ? 156 LYS A CE 1
+ATOM 1258 N NZ . LYS A 1 156 ? 8.548 21.703 -0.390 1.00 53.69 ? 156 LYS A NZ 1
+ATOM 1259 N N . LEU A 1 157 ? 2.619 19.025 3.432 1.00 29.45 ? 157 LEU A N 1
+ATOM 1260 C CA . LEU A 1 157 ? 2.001 18.008 4.288 1.00 30.31 ? 157 LEU A CA 1
+ATOM 1261 C C . LEU A 1 157 ? 1.648 16.770 3.417 1.00 33.12 ? 157 LEU A C 1
+ATOM 1262 O O . LEU A 1 157 ? 1.909 15.637 3.824 1.00 31.97 ? 157 LEU A O 1
+ATOM 1263 C CB . LEU A 1 157 ? 0.738 18.592 4.963 1.00 31.12 ? 157 LEU A CB 1
+ATOM 1264 C CG . LEU A 1 157 ? -0.195 17.612 5.697 1.00 36.82 ? 157 LEU A CG 1
+ATOM 1265 C CD1 . LEU A 1 157 ? 0.372 17.224 7.047 1.00 36.74 ? 157 LEU A CD1 1
+ATOM 1266 C CD2 . LEU A 1 157 ? -1.589 18.205 5.875 1.00 38.77 ? 157 LEU A CD2 1
+ATOM 1267 N N . LEU A 1 158 ? 1.121 17.007 2.199 1.00 28.69 ? 158 LEU A N 1
+ATOM 1268 C CA . LEU A 1 158 ? 0.765 15.941 1.264 1.00 28.66 ? 158 LEU A CA 1
+ATOM 1269 C C . LEU A 1 158 ? 2.014 15.159 0.838 1.00 29.55 ? 158 LEU A C 1
+ATOM 1270 O O . LEU A 1 158 ? 1.966 13.942 0.792 1.00 28.03 ? 158 LEU A O 1
+ATOM 1271 C CB . LEU A 1 158 ? 0.005 16.485 0.043 1.00 28.46 ? 158 LEU A CB 1
+ATOM 1272 C CG . LEU A 1 158 ? -1.419 17.023 0.242 1.00 33.60 ? 158 LEU A CG 1
+ATOM 1273 C CD1 . LEU A 1 158 ? -1.949 17.578 -1.056 1.00 32.48 ? 158 LEU A CD1 1
+ATOM 1274 C CD2 . LEU A 1 158 ? -2.397 15.914 0.645 1.00 37.39 ? 158 LEU A CD2 1
+ATOM 1275 N N . GLU A 1 159 ? 3.132 15.856 0.613 1.00 25.98 ? 159 GLU A N 1
+ATOM 1276 C CA . GLU A 1 159 ? 4.425 15.261 0.281 1.00 26.70 ? 159 GLU A CA 1
+ATOM 1277 C C . GLU A 1 159 ? 4.926 14.375 1.417 1.00 32.81 ? 159 GLU A C 1
+ATOM 1278 O O . GLU A 1 159 ? 5.352 13.262 1.144 1.00 32.38 ? 159 GLU A O 1
+ATOM 1279 C CB . GLU A 1 159 ? 5.467 16.340 -0.031 1.00 27.90 ? 159 GLU A CB 1
+ATOM 1280 C CG . GLU A 1 159 ? 5.313 16.947 -1.414 1.00 33.31 ? 159 GLU A CG 1
+ATOM 1281 C CD . GLU A 1 159 ? 6.253 18.091 -1.747 1.00 36.61 ? 159 GLU A CD 1
+ATOM 1282 O OE1 . GLU A 1 159 ? 6.091 18.688 -2.832 1.00 34.12 ? 159 GLU A OE1 1
+ATOM 1283 O OE2 . GLU A 1 159 ? 7.170 18.372 -0.947 1.00 36.39 ? 159 GLU A OE2 1
+ATOM 1284 N N . ALA A 1 160 ? 4.806 14.837 2.684 1.00 31.08 ? 160 ALA A N 1
+ATOM 1285 C CA . ALA A 1 160 ? 5.190 14.084 3.881 1.00 32.63 ? 160 ALA A CA 1
+ATOM 1286 C C . ALA A 1 160 ? 4.344 12.835 4.006 1.00 36.90 ? 160 ALA A C 1
+ATOM 1287 O O . ALA A 1 160 ? 4.881 11.764 4.292 1.00 36.46 ? 160 ALA A O 1
+ATOM 1288 C CB . ALA A 1 160 ? 5.038 14.944 5.134 1.00 33.80 ? 160 ALA A CB 1
+ATOM 1289 N N . LYS A 1 161 ? 3.038 12.958 3.736 1.00 33.09 ? 161 LYS A N 1
+ATOM 1290 C CA . LYS A 1 161 ? 2.151 11.813 3.810 1.00 33.11 ? 161 LYS A CA 1
+ATOM 1291 C C . LYS A 1 161 ? 2.220 10.871 2.593 1.00 37.54 ? 161 LYS A C 1
+ATOM 1292 O O . LYS A 1 161 ? 1.990 9.678 2.758 1.00 36.38 ? 161 LYS A O 1
+ATOM 1293 C CB . LYS A 1 161 ? 0.748 12.200 4.284 1.00 35.33 ? 161 LYS A CB 1
+ATOM 1294 C CG . LYS A 1 161 ? 0.623 12.084 5.807 1.00 48.25 ? 161 LYS A CG 1
+ATOM 1295 C CD . LYS A 1 161 ? 1.060 13.319 6.586 1.00 55.56 ? 161 LYS A CD 1
+ATOM 1296 C CE . LYS A 1 161 ? 0.896 13.124 8.077 1.00 70.36 ? 161 LYS A CE 1
+ATOM 1297 N NZ . LYS A 1 161 ? 2.091 12.499 8.706 1.00 84.28 ? 161 LYS A NZ 1
+ATOM 1298 N N . ALA A 1 162 ? 2.659 11.374 1.411 1.00 33.64 ? 162 ALA A N 1
+ATOM 1299 C CA . ALA A 1 162 ? 2.846 10.549 0.211 1.00 32.80 ? 162 ALA A CA 1
+ATOM 1300 C C . ALA A 1 162 ? 4.013 9.578 0.400 1.00 36.41 ? 162 ALA A C 1
+ATOM 1301 O O . ALA A 1 162 ? 3.894 8.409 0.035 1.00 35.76 ? 162 ALA A O 1
+ATOM 1302 C CB . ALA A 1 162 ? 3.094 11.424 -1.007 1.00 33.06 ? 162 ALA A CB 1
+ATOM 1303 N N . THR A 1 163 ? 5.126 10.038 0.998 1.00 33.72 ? 163 THR A N 1
+ATOM 1304 C CA . THR A 1 163 ? 6.288 9.170 1.221 1.00 33.58 ? 163 THR A CA 1
+ATOM 1305 C C . THR A 1 163 ? 5.970 8.110 2.273 1.00 38.83 ? 163 THR A C 1
+ATOM 1306 O O . THR A 1 163 ? 6.431 6.984 2.149 1.00 39.10 ? 163 THR A O 1
+ATOM 1307 C CB . THR A 1 163 ? 7.640 9.932 1.373 1.00 39.18 ? 163 THR A CB 1
+ATOM 1308 O OG1 . THR A 1 163 ? 8.448 9.362 2.424 1.00 39.98 ? 163 THR A OG1 1
+ATOM 1309 C CG2 . THR A 1 163 ? 7.463 11.401 1.613 1.00 29.09 ? 163 THR A CG2 1
+ATOM 1310 N N . LEU A 1 164 ? 5.144 8.480 3.274 1.00 36.90 ? 164 LEU A N 1
+ATOM 1311 C CA . LEU A 1 164 ? 4.654 7.625 4.362 1.00 37.71 ? 164 LEU A CA 1
+ATOM 1312 C C . LEU A 1 164 ? 3.767 6.514 3.822 1.00 39.68 ? 164 LEU A C 1
+ATOM 1313 O O . LEU A 1 164 ? 3.861 5.400 4.306 1.00 39.25 ? 164 LEU A O 1
+ATOM 1314 C CB . LEU A 1 164 ? 3.831 8.477 5.337 1.00 38.60 ? 164 LEU A CB 1
+ATOM 1315 C CG . LEU A 1 164 ? 4.401 8.766 6.717 1.00 44.84 ? 164 LEU A CG 1
+ATOM 1316 C CD1 . LEU A 1 164 ? 5.743 9.433 6.655 1.00 49.75 ? 164 LEU A CD1 1
+ATOM 1317 C CD2 . LEU A 1 164 ? 3.428 9.558 7.532 1.00 43.71 ? 164 LEU A CD2 1
+ATOM 1318 N N . TYR A 1 165 ? 2.938 6.838 2.851 1.00 35.36 ? 165 TYR A N 1
+ATOM 1319 C CA . TYR A 1 165 ? 2.070 5.890 2.251 1.00 35.52 ? 165 TYR A CA 1
+ATOM 1320 C C . TYR A 1 165 ? 2.922 4.870 1.574 1.00 44.91 ? 165 TYR A C 1
+ATOM 1321 O O . TYR A 1 165 ? 2.712 3.710 1.744 1.00 44.91 ? 165 TYR A O 1
+ATOM 1322 C CB . TYR A 1 165 ? 1.128 6.548 1.241 1.00 34.93 ? 165 TYR A CB 1
+ATOM 1323 C CG . TYR A 1 165 ? -0.010 5.675 0.799 1.00 34.47 ? 165 TYR A CG 1
+ATOM 1324 C CD1 . TYR A 1 165 ? 0.098 4.870 -0.288 1.00 34.94 ? 165 TYR A CD1 1
+ATOM 1325 C CD2 . TYR A 1 165 ? -1.178 5.655 1.490 1.00 35.36 ? 165 TYR A CD2 1
+ATOM 1326 C CE1 . TYR A 1 165 ? -0.944 4.085 -0.680 1.00 35.64 ? 165 TYR A CE1 1
+ATOM 1327 C CE2 . TYR A 1 165 ? -2.206 4.871 1.114 1.00 35.44 ? 165 TYR A CE2 1
+ATOM 1328 C CZ . TYR A 1 165 ? -2.079 4.098 0.030 1.00 41.73 ? 165 TYR A CZ 1
+ATOM 1329 O OH . TYR A 1 165 ? -3.110 3.339 -0.318 1.00 43.90 ? 165 TYR A OH 1
+ATOM 1330 N N . SER A 1 166 ? 3.890 5.305 0.798 1.00 45.65 ? 166 SER A N 1
+ATOM 1331 C CA . SER A 1 166 ? 4.650 4.373 -0.014 1.00 47.14 ? 166 SER A CA 1
+ATOM 1332 C C . SER A 1 166 ? 5.752 3.612 0.710 1.00 53.23 ? 166 SER A C 1
+ATOM 1333 O O . SER A 1 166 ? 6.275 2.683 0.189 1.00 52.87 ? 166 SER A O 1
+ATOM 1334 C CB . SER A 1 166 ? 5.102 4.981 -1.352 1.00 20.00 ? 166 SER A CB 1
+ATOM 1335 O OG . SER A 1 166 ? 5.823 6.172 -1.228 1.00 20.00 ? 166 SER A OG 1
+ATOM 1336 N N . LYS A 1 167 ? 6.061 4.003 1.926 1.00 51.86 ? 167 LYS A N 1
+ATOM 1337 C CA . LYS A 1 167 ? 6.987 3.275 2.765 1.00 52.67 ? 167 LYS A CA 1
+ATOM 1338 C C . LYS A 1 167 ? 6.202 2.253 3.571 1.00 58.01 ? 167 LYS A C 1
+ATOM 1339 O O . LYS A 1 167 ? 6.758 1.461 4.292 1.00 58.56 ? 167 LYS A O 1
+ATOM 1340 C CB . LYS A 1 167 ? 7.673 4.219 3.750 1.00 55.18 ? 167 LYS A CB 1
+ATOM 1341 C CG . LYS A 1 167 ? 8.858 5.023 3.241 1.00 68.88 ? 167 LYS A CG 1
+ATOM 1342 C CD . LYS A 1 167 ? 9.830 5.263 4.390 1.00 76.77 ? 167 LYS A CD 1
+ATOM 1343 C CE . LYS A 1 167 ? 10.501 6.618 4.349 1.00 89.30 ? 167 LYS A CE 1
+ATOM 1344 N NZ . LYS A 1 167 ? 10.492 7.316 5.668 1.00 96.00 ? 167 LYS A NZ 1
+ATOM 1345 N N . LYS A 1 168 ? 4.897 2.275 3.454 1.00 54.19 ? 168 LYS A N 1
+ATOM 1346 C CA . LYS A 1 168 ? 4.085 1.310 4.225 1.00 71.52 ? 168 LYS A CA 1
+ATOM 1347 C C . LYS A 1 168 ? 4.522 -0.171 4.173 1.00 110.07 ? 168 LYS A C 1
+ATOM 1348 O O . LYS A 1 168 ? 4.895 -0.690 3.121 1.00 74.07 ? 168 LYS A O 1
+ATOM 1349 C CB . LYS A 1 168 ? 2.574 1.471 3.961 1.00 73.01 ? 168 LYS A CB 1
+ATOM 1350 C CG . LYS A 1 168 ? 2.088 0.901 2.630 1.00 76.92 ? 168 LYS A CG 1
+ATOM 1351 C CD . LYS A 1 168 ? 0.677 1.353 2.288 1.00 81.62 ? 168 LYS A CD 1
+ATOM 1352 C CE . LYS A 1 168 ? 0.390 1.099 0.834 1.00 86.89 ? 168 LYS A CE 1
+ATOM 1353 N NZ . LYS A 1 168 ? -0.970 0.535 0.641 1.00 93.84 ? 168 LYS A NZ 1
+HETATM 1354 C C1 . GOL B 2 . ? 5.914 2.154 -10.922 1.00 39.37 ? 201 GOL A C1 1
+HETATM 1355 O O1 . GOL B 2 . ? 5.122 1.037 -10.506 1.00 35.40 ? 201 GOL A O1 1
+HETATM 1356 C C2 . GOL B 2 . ? 5.367 2.815 -12.205 1.00 39.14 ? 201 GOL A C2 1
+HETATM 1357 O O2 . GOL B 2 . ? 4.747 4.018 -11.895 1.00 42.35 ? 201 GOL A O2 1
+HETATM 1358 C C3 . GOL B 2 . ? 6.290 3.119 -13.324 1.00 38.50 ? 201 GOL A C3 1
+HETATM 1359 O O3 . GOL B 2 . ? 5.297 3.169 -14.321 1.00 39.15 ? 201 GOL A O3 1
+HETATM 1360 C C1 . GOL C 2 . ? 0.570 11.166 -24.213 1.00 59.64 ? 202 GOL A C1 1
+HETATM 1361 O O1 . GOL C 2 . ? -0.738 11.658 -23.866 1.00 59.84 ? 202 GOL A O1 1
+HETATM 1362 C C2 . GOL C 2 . ? 0.537 9.717 -24.648 1.00 59.18 ? 202 GOL A C2 1
+HETATM 1363 O O2 . GOL C 2 . ? 0.935 9.717 -26.034 1.00 60.29 ? 202 GOL A O2 1
+HETATM 1364 C C3 . GOL C 2 . ? -0.818 9.031 -24.424 1.00 58.99 ? 202 GOL A C3 1
+HETATM 1365 O O3 . GOL C 2 . ? -0.923 8.355 -23.173 1.00 57.86 ? 202 GOL A O3 1
+HETATM 1366 C C1 . GOL D 2 . ? 1.682 4.386 -15.478 1.00 50.78 ? 203 GOL A C1 1
+HETATM 1367 O O1 . GOL D 2 . ? 1.404 5.088 -14.303 1.00 50.83 ? 203 GOL A O1 1
+HETATM 1368 C C2 . GOL D 2 . ? 2.716 5.116 -16.290 1.00 50.56 ? 203 GOL A C2 1
+HETATM 1369 O O2 . GOL D 2 . ? 3.611 5.723 -15.359 1.00 52.85 ? 203 GOL A O2 1
+HETATM 1370 C C3 . GOL D 2 . ? 2.119 6.177 -17.197 1.00 50.33 ? 203 GOL A C3 1
+HETATM 1371 O O3 . GOL D 2 . ? 1.333 5.850 -18.346 1.00 49.75 ? 203 GOL A O3 1
+HETATM 1372 O O . HOH E 3 . ? -7.343 16.808 -5.868 1.00 19.10 ? 301 HOH A O 1
+HETATM 1373 O O . HOH E 3 . ? 3.432 17.259 -23.091 1.00 23.99 ? 302 HOH A O 1
+HETATM 1374 O O . HOH E 3 . ? -8.694 9.662 -9.784 1.00 21.85 ? 303 HOH A O 1
+HETATM 1375 O O . HOH E 3 . ? 4.297 24.558 -24.253 1.00 38.76 ? 304 HOH A O 1
+HETATM 1376 O O . HOH E 3 . ? -6.438 4.814 -24.609 1.00 32.10 ? 305 HOH A O 1
+HETATM 1377 O O . HOH E 3 . ? -1.982 25.766 1.287 1.00 33.06 ? 306 HOH A O 1
+HETATM 1378 O O . HOH E 3 . ? -14.693 17.175 -5.224 1.00 40.63 ? 307 HOH A O 1
+HETATM 1379 O O . HOH E 3 . ? -9.024 30.880 -15.305 1.00 38.38 ? 308 HOH A O 1
+HETATM 1380 O O . HOH E 3 . ? -3.689 9.896 -22.054 1.00 27.22 ? 309 HOH A O 1
+HETATM 1381 O O . HOH E 3 . ? 7.775 18.630 -15.473 1.00 50.92 ? 310 HOH A O 1
+HETATM 1382 O O . HOH E 3 . ? 4.815 9.331 -9.326 1.00 34.81 ? 311 HOH A O 1
+HETATM 1383 O O . HOH E 3 . ? 10.697 16.864 -19.189 1.00 57.14 ? 312 HOH A O 1
+HETATM 1384 O O . HOH E 3 . ? 5.384 10.979 -6.625 1.00 33.21 ? 313 HOH A O 1
+HETATM 1385 O O . HOH E 3 . ? -9.697 24.361 -2.756 1.00 34.77 ? 314 HOH A O 1
+HETATM 1386 O O . HOH E 3 . ? -12.226 10.249 -1.756 1.00 40.28 ? 315 HOH A O 1
+HETATM 1387 O O . HOH E 3 . ? -10.699 10.229 4.074 1.00 44.09 ? 316 HOH A O 1
+HETATM 1388 O O . HOH E 3 . ? -11.567 7.773 -2.521 1.00 39.67 ? 317 HOH A O 1
+HETATM 1389 O O . HOH E 3 . ? -11.856 4.482 -19.078 1.00 42.40 ? 318 HOH A O 1
+HETATM 1390 O O . HOH E 3 . ? 0.279 37.620 1.434 1.00 55.46 ? 319 HOH A O 1
+HETATM 1391 O O . HOH E 3 . ? -8.936 2.443 -7.035 1.00 42.59 ? 320 HOH A O 1
+HETATM 1392 O O . HOH E 3 . ? -18.267 27.389 -28.094 1.00 44.15 ? 321 HOH A O 1
+HETATM 1393 O O . HOH E 3 . ? 9.391 9.094 -9.758 1.00 58.20 ? 322 HOH A O 1
+HETATM 1394 O O . HOH E 3 . ? -12.626 10.209 1.348 1.00 30.21 ? 323 HOH A O 1
+HETATM 1395 O O . HOH E 3 . ? -6.961 34.688 -9.550 1.00 26.28 ? 324 HOH A O 1
+HETATM 1396 O O . HOH E 3 . ? -8.074 19.402 6.024 1.00 54.08 ? 325 HOH A O 1
+HETATM 1397 O O . HOH E 3 . ? -19.352 7.159 -14.746 1.00 69.15 ? 326 HOH A O 1
+HETATM 1398 O O . HOH E 3 . ? 5.053 15.846 -18.235 1.00 45.79 ? 327 HOH A O 1
+HETATM 1399 O O . HOH E 3 . ? -5.207 23.677 3.197 1.00 24.74 ? 328 HOH A O 1
+HETATM 1400 O O . HOH E 3 . ? -2.394 0.417 -8.835 1.00 44.07 ? 329 HOH A O 1
+HETATM 1401 O O . HOH E 3 . ? -9.025 31.167 -25.832 1.00 39.98 ? 330 HOH A O 1
+HETATM 1402 O O . HOH E 3 . ? -4.441 20.215 5.401 1.00 31.47 ? 331 HOH A O 1
+HETATM 1403 O O . HOH E 3 . ? 2.634 23.581 1.904 1.00 36.89 ? 332 HOH A O 1
+HETATM 1404 O O . HOH E 3 . ? -5.635 38.684 -3.538 1.00 41.98 ? 333 HOH A O 1
+HETATM 1405 O O . HOH E 3 . ? -2.428 7.629 -19.684 1.00 43.97 ? 334 HOH A O 1
+HETATM 1406 O O . HOH E 3 . ? -7.738 20.740 -28.694 1.00 29.68 ? 335 HOH A O 1
+HETATM 1407 O O . HOH E 3 . ? -6.967 37.027 -0.871 1.00 52.38 ? 336 HOH A O 1
+HETATM 1408 O O . HOH E 3 . ? -13.177 3.613 -21.528 1.00 54.00 ? 337 HOH A O 1
+HETATM 1409 O O . HOH E 3 . ? -9.698 15.876 6.451 1.00 44.19 ? 338 HOH A O 1
+HETATM 1410 O O . HOH E 3 . ? -18.018 24.313 -25.020 1.00 50.03 ? 339 HOH A O 1
+HETATM 1411 O O . HOH E 3 . ? -13.613 29.282 -32.277 1.00 37.82 ? 340 HOH A O 1
+HETATM 1412 O O . HOH E 3 . ? 7.722 29.220 8.826 1.00 58.97 ? 341 HOH A O 1
+HETATM 1413 O O . HOH E 3 . ? 5.103 26.943 -25.238 1.00 42.88 ? 342 HOH A O 1
+HETATM 1414 O O . HOH E 3 . ? 8.299 18.095 -19.837 1.00 62.29 ? 343 HOH A O 1
+HETATM 1415 O O . HOH E 3 . ? 2.999 37.247 1.440 1.00 61.21 ? 344 HOH A O 1
+HETATM 1416 O O . HOH E 3 . ? -14.556 13.722 -8.544 1.00 33.28 ? 345 HOH A O 1
+HETATM 1417 O O . HOH E 3 . ? -0.410 31.805 -11.158 1.00 33.12 ? 346 HOH A O 1
+HETATM 1418 O O . HOH E 3 . ? -12.637 26.490 -20.419 1.00 37.87 ? 347 HOH A O 1
+HETATM 1419 O O . HOH E 3 . ? -7.147 4.324 2.407 1.00 37.81 ? 348 HOH A O 1
+HETATM 1420 O O . HOH E 3 . ? 5.111 3.647 -5.121 1.00 45.43 ? 349 HOH A O 1
+HETATM 1421 O O . HOH E 3 . ? -4.356 1.800 1.404 1.00 45.30 ? 350 HOH A O 1
+HETATM 1422 O O . HOH E 3 . ? -20.102 9.619 -23.887 1.00 48.17 ? 351 HOH A O 1
+HETATM 1423 O O . HOH E 3 . ? -17.142 21.189 -27.430 1.00 47.03 ? 352 HOH A O 1
+HETATM 1424 O O . HOH E 3 . ? -11.986 15.385 -12.257 1.00 32.45 ? 353 HOH A O 1
+HETATM 1425 O O . HOH E 3 . ? -8.030 4.928 -14.877 1.00 43.46 ? 354 HOH A O 1
+HETATM 1426 O O . HOH E 3 . ? -14.988 8.691 1.926 1.00 45.43 ? 355 HOH A O 1
+HETATM 1427 O O . HOH E 3 . ? -19.708 21.137 -28.563 1.00 59.52 ? 356 HOH A O 1
+HETATM 1428 O O . HOH E 3 . ? 10.619 23.095 -4.119 1.00 51.94 ? 357 HOH A O 1
+HETATM 1429 O O . HOH E 3 . ? -10.722 34.297 -6.979 1.00 58.28 ? 358 HOH A O 1
+HETATM 1430 O O . HOH E 3 . ? 0.585 25.089 0.892 1.00 58.55 ? 359 HOH A O 1
+HETATM 1431 O O . HOH E 3 . ? 3.137 37.049 -1.241 1.00 47.47 ? 360 HOH A O 1
+HETATM 1432 O O . HOH E 3 . ? -9.499 12.786 -6.641 1.00 26.89 ? 361 HOH A O 1
+HETATM 1433 O O . HOH E 3 . ? -6.335 27.097 -32.364 1.00 56.38 ? 362 HOH A O 1
+HETATM 1434 O O . HOH E 3 . ? 9.018 31.948 -4.188 1.00 44.62 ? 363 HOH A O 1
+HETATM 1435 O O . HOH E 3 . ? -12.286 15.997 -9.813 1.00 32.55 ? 364 HOH A O 1
+HETATM 1436 O O . HOH E 3 . ? 11.137 15.589 -3.245 1.00 49.23 ? 365 HOH A O 1
+HETATM 1437 O O . HOH E 3 . ? -21.509 25.149 -10.371 1.00 40.99 ? 366 HOH A O 1
+HETATM 1438 O O . HOH E 3 . ? -16.137 17.693 -14.325 1.00 39.35 ? 367 HOH A O 1
+HETATM 1439 O O . HOH E 3 . ? 5.141 7.182 -13.695 1.00 80.02 ? 368 HOH A O 1
+HETATM 1440 O O . HOH E 3 . ? -8.786 5.080 -10.051 1.00 83.79 ? 369 HOH A O 1
+#
+loop_
+_atom_site_anisotrop.id
+_atom_site_anisotrop.type_symbol
+_atom_site_anisotrop.pdbx_label_atom_id
+_atom_site_anisotrop.pdbx_label_alt_id
+_atom_site_anisotrop.pdbx_label_comp_id
+_atom_site_anisotrop.pdbx_label_asym_id
+_atom_site_anisotrop.pdbx_label_seq_id
+_atom_site_anisotrop.pdbx_PDB_ins_code
+_atom_site_anisotrop.U[1][1]
+_atom_site_anisotrop.U[2][2]
+_atom_site_anisotrop.U[3][3]
+_atom_site_anisotrop.U[1][2]
+_atom_site_anisotrop.U[1][3]
+_atom_site_anisotrop.U[2][3]
+_atom_site_anisotrop.pdbx_auth_seq_id
+_atom_site_anisotrop.pdbx_auth_comp_id
+_atom_site_anisotrop.pdbx_auth_asym_id
+_atom_site_anisotrop.pdbx_auth_atom_id
+1 N N . GLY A 1 ? 0.5238 0.6197 0.5668 -0.0101 0.0025 -0.0076 1 GLY A N
+2 C CA . GLY A 1 ? 0.5164 0.6050 0.5560 -0.0103 0.0028 -0.0113 1 GLY A CA
+3 C C . GLY A 1 ? 0.5215 0.6107 0.5619 -0.0105 0.0039 -0.0104 1 GLY A C
+4 O O . GLY A 1 ? 0.5243 0.6152 0.5679 -0.0114 0.0043 -0.0068 1 GLY A O
+5 N N . THR A 2 ? 0.4227 0.5109 0.4605 -0.0096 0.0043 -0.0136 2 THR A N
+6 C CA . THR A 2 ? 0.3972 0.4870 0.4354 -0.0095 0.0054 -0.0132 2 THR A CA
+7 C C . THR A 2 ? 0.3580 0.4395 0.3941 -0.0107 0.0058 -0.0149 2 THR A C
+8 O O . THR A 2 ? 0.3504 0.4262 0.3839 -0.0108 0.0054 -0.0180 2 THR A O
+9 C CB . THR A 2 ? 0.5358 0.6334 0.5735 -0.0073 0.0057 -0.0152 2 THR A CB
+10 O OG1 . THR A 2 ? 0.6021 0.7042 0.6397 -0.0059 0.0048 -0.0162 2 THR A OG1
+11 C CG2 . THR A 2 ? 0.5398 0.6456 0.5800 -0.0065 0.0068 -0.0123 2 THR A CG2
+12 N N . LEU A 3 ? 0.2571 0.3389 0.2947 -0.0113 0.0067 -0.0128 3 LEU A N
+13 C CA . LEU A 3 ? 0.2576 0.3330 0.2936 -0.0123 0.0072 -0.0142 3 LEU A CA
+14 C C . LEU A 3 ? 0.3032 0.3797 0.3369 -0.0112 0.0077 -0.0174 3 LEU A C
+15 O O . LEU A 3 ? 0.2732 0.3572 0.3078 -0.0097 0.0081 -0.0175 3 LEU A O
+16 C CB . LEU A 3 ? 0.2585 0.3354 0.2973 -0.0129 0.0079 -0.0109 3 LEU A CB
+17 C CG . LEU A 3 ? 0.3107 0.3808 0.3507 -0.0146 0.0074 -0.0096 3 LEU A CG
+18 C CD1 . LEU A 3 ? 0.2691 0.3342 0.3085 -0.0153 0.0062 -0.0105 3 LEU A CD1
+19 C CD2 . LEU A 3 ? 0.3100 0.3839 0.3546 -0.0150 0.0075 -0.0053 3 LEU A CD2
+20 N N . ARG A 4 ? 0.2686 0.3382 0.2997 -0.0118 0.0076 -0.0201 4 ARG A N
+21 C CA . ARG A 4 ? 0.2605 0.3299 0.2899 -0.0112 0.0079 -0.0232 4 ARG A CA
+22 C C . ARG A 4 ? 0.3082 0.3707 0.3357 -0.0124 0.0083 -0.0241 4 ARG A C
+23 O O . ARG A 4 ? 0.3031 0.3605 0.3302 -0.0136 0.0080 -0.0230 4 ARG A O
+24 C CB . ARG A 4 ? 0.3172 0.3853 0.3453 -0.0105 0.0068 -0.0260 4 ARG A CB
+25 C CG . ARG A 4 ? 0.4491 0.5250 0.4785 -0.0086 0.0064 -0.0268 4 ARG A CG
+26 C CD . ARG A 4 ? 0.6018 0.6781 0.6315 -0.0084 0.0054 -0.0260 4 ARG A CD
+27 N NE . ARG A 4 ? 0.6370 0.7074 0.6651 -0.0086 0.0044 -0.0284 4 ARG A NE
+28 C CZ . ARG A 4 ? 0.7550 0.8237 0.7828 -0.0088 0.0036 -0.0279 4 ARG A CZ
+29 N NH1 . ARG A 4 ? 0.5301 0.6023 0.5593 -0.0089 0.0036 -0.0251 4 ARG A NH1
+30 N NH2 . ARG A 4 ? 0.6229 0.6865 0.6492 -0.0089 0.0027 -0.0300 4 ARG A NH2
+31 N N . PHE A 5 ? 0.2764 0.3388 0.3029 -0.0121 0.0086 -0.0264 5 PHE A N
+32 C CA . PHE A 5 ? 0.2676 0.3243 0.2924 -0.0132 0.0091 -0.0273 5 PHE A CA
+33 C C . PHE A 5 ? 0.2887 0.3402 0.3119 -0.0136 0.0083 -0.0293 5 PHE A C
+34 O O . PHE A 5 ? 0.2683 0.3213 0.2920 -0.0127 0.0075 -0.0312 5 PHE A O
+35 C CB . PHE A 5 ? 0.2850 0.3447 0.3100 -0.0127 0.0100 -0.0283 5 PHE A CB
+36 C CG . PHE A 5 ? 0.2994 0.3632 0.3256 -0.0125 0.0110 -0.0261 5 PHE A CG
+37 C CD1 . PHE A 5 ? 0.3413 0.4017 0.3675 -0.0136 0.0113 -0.0240 5 PHE A CD1
+38 C CD2 . PHE A 5 ? 0.3181 0.3894 0.3458 -0.0111 0.0115 -0.0262 5 PHE A CD2
+39 C CE1 . PHE A 5 ? 0.3518 0.4156 0.3795 -0.0134 0.0121 -0.0219 5 PHE A CE1
+40 C CE2 . PHE A 5 ? 0.3614 0.4367 0.3904 -0.0109 0.0125 -0.0237 5 PHE A CE2
+41 C CZ . PHE A 5 ? 0.3405 0.4117 0.3696 -0.0122 0.0128 -0.0215 5 PHE A CZ
+42 N N . PHE A 6 ? 0.2326 0.2783 0.2543 -0.0147 0.0083 -0.0289 6 PHE A N
+43 C CA . PHE A 6 ? 0.2219 0.2627 0.2422 -0.0152 0.0077 -0.0302 6 PHE A CA
+44 C C . PHE A 6 ? 0.3090 0.3458 0.3278 -0.0162 0.0082 -0.0301 6 PHE A C
+45 O O . PHE A 6 ? 0.3013 0.3383 0.3198 -0.0166 0.0089 -0.0290 6 PHE A O
+46 C CB . PHE A 6 ? 0.2381 0.2763 0.2579 -0.0154 0.0068 -0.0293 6 PHE A CB
+47 C CG . PHE A 6 ? 0.2657 0.3075 0.2868 -0.0145 0.0061 -0.0292 6 PHE A CG
+48 C CD1 . PHE A 6 ? 0.3114 0.3533 0.3325 -0.0137 0.0053 -0.0310 6 PHE A CD1
+49 C CD2 . PHE A 6 ? 0.2980 0.3432 0.3205 -0.0143 0.0062 -0.0273 6 PHE A CD2
+50 C CE1 . PHE A 6 ? 0.3288 0.3745 0.3510 -0.0127 0.0045 -0.0311 6 PHE A CE1
+51 C CE2 . PHE A 6 ? 0.3464 0.3955 0.3701 -0.0134 0.0056 -0.0270 6 PHE A CE2
+52 C CZ . PHE A 6 ? 0.3202 0.3697 0.3435 -0.0126 0.0048 -0.0290 6 PHE A CZ
+53 N N . THR A 7 ? 0.2644 0.2977 0.2823 -0.0166 0.0078 -0.0311 7 THR A N
+54 C CA . THR A 7 ? 0.2646 0.2941 0.2810 -0.0175 0.0081 -0.0307 7 THR A CA
+55 C C . THR A 7 ? 0.2886 0.3147 0.3040 -0.0177 0.0073 -0.0303 7 THR A C
+56 O O . THR A 7 ? 0.2448 0.2714 0.2608 -0.0171 0.0065 -0.0306 7 THR A O
+57 C CB . THR A 7 ? 0.4179 0.4471 0.4347 -0.0179 0.0085 -0.0317 7 THR A CB
+58 O OG1 . THR A 7 ? 0.4412 0.4697 0.4593 -0.0177 0.0076 -0.0330 7 THR A OG1
+59 C CG2 . THR A 7 ? 0.3931 0.4258 0.4106 -0.0177 0.0094 -0.0322 7 THR A CG2
+60 N N . VAL A 8 ? 0.2486 0.2718 0.2623 -0.0183 0.0075 -0.0295 8 VAL A N
+61 C CA . VAL A 8 ? 0.2530 0.2736 0.2656 -0.0183 0.0068 -0.0290 8 VAL A CA
+62 C C . VAL A 8 ? 0.3354 0.3540 0.3476 -0.0189 0.0070 -0.0287 8 VAL A C
+63 O O . VAL A 8 ? 0.3263 0.3454 0.3385 -0.0194 0.0077 -0.0287 8 VAL A O
+64 C CB . VAL A 8 ? 0.2982 0.3180 0.3096 -0.0182 0.0067 -0.0282 8 VAL A CB
+65 C CG1 . VAL A 8 ? 0.2962 0.3139 0.3064 -0.0180 0.0060 -0.0279 8 VAL A CG1
+66 C CG2 . VAL A 8 ? 0.2964 0.3185 0.3092 -0.0179 0.0066 -0.0281 8 VAL A CG2
+67 N N . THR A 9 ? 0.3073 0.3238 0.3194 -0.0188 0.0063 -0.0283 9 THR A N
+68 C CA . THR A 9 ? 0.3016 0.3164 0.3139 -0.0194 0.0064 -0.0274 9 THR A CA
+69 C C . THR A 9 ? 0.3660 0.3810 0.3762 -0.0198 0.0071 -0.0262 9 THR A C
+70 O O . THR A 9 ? 0.3506 0.3659 0.3592 -0.0193 0.0071 -0.0260 9 THR A O
+71 C CB . THR A 9 ? 0.3841 0.3969 0.3967 -0.0192 0.0054 -0.0268 9 THR A CB
+72 O OG1 . THR A 9 ? 0.3458 0.3582 0.3564 -0.0187 0.0053 -0.0261 9 THR A OG1
+73 C CG2 . THR A 9 ? 0.3387 0.3515 0.3535 -0.0187 0.0045 -0.0283 9 THR A CG2
+74 N N . ASP A 10 ? 0.3376 0.3528 0.3483 -0.0205 0.0077 -0.0255 10 ASP A N
+75 C CA . ASP A 10 ? 0.3354 0.3513 0.3443 -0.0208 0.0084 -0.0243 10 ASP A CA
+76 C C . ASP A 10 ? 0.3975 0.4130 0.4048 -0.0203 0.0081 -0.0229 10 ASP A C
+77 O O . ASP A 10 ? 0.3940 0.4108 0.3993 -0.0198 0.0083 -0.0227 10 ASP A O
+78 C CB . ASP A 10 ? 0.3653 0.3816 0.3756 -0.0217 0.0090 -0.0235 10 ASP A CB
+79 C CG . ASP A 10 ? 0.4653 0.4828 0.4769 -0.0221 0.0095 -0.0249 10 ASP A CG
+80 O OD1 . ASP A 10 ? 0.4723 0.4911 0.4829 -0.0216 0.0098 -0.0261 10 ASP A OD1
+81 O OD2 . ASP A 10 ? 0.4845 0.5018 0.4983 -0.0229 0.0095 -0.0249 10 ASP A OD2
+82 N N . GLU A 11 ? 0.3717 0.3856 0.3801 -0.0202 0.0073 -0.0222 11 GLU A N
+83 C CA . GLU A 11 ? 0.3720 0.3857 0.3791 -0.0197 0.0070 -0.0208 11 GLU A CA
+84 C C . GLU A 11 ? 0.3883 0.4025 0.3935 -0.0186 0.0066 -0.0219 11 GLU A C
+85 O O . GLU A 11 ? 0.3843 0.4001 0.3876 -0.0180 0.0066 -0.0214 11 GLU A O
+86 C CB . GLU A 11 ? 0.4001 0.4118 0.4093 -0.0199 0.0062 -0.0199 11 GLU A CB
+87 C CG . GLU A 11 ? 0.6171 0.6282 0.6289 -0.0210 0.0063 -0.0183 11 GLU A CG
+88 C CD . GLU A 11 ? 0.9700 0.9801 0.9847 -0.0216 0.0061 -0.0199 11 GLU A CD
+89 O OE1 . GLU A 11 ? 1.0645 1.0731 1.0824 -0.0223 0.0055 -0.0190 11 GLU A OE1
+90 O OE2 . GLU A 11 ? 0.8036 0.8146 0.8178 -0.0214 0.0064 -0.0220 11 GLU A OE2
+91 N N . TYR A 12 ? 0.3334 0.3469 0.3394 -0.0184 0.0061 -0.0235 12 TYR A N
+92 C CA . TYR A 12 ? 0.3085 0.3223 0.3135 -0.0177 0.0056 -0.0246 12 TYR A CA
+93 C C . TYR A 12 ? 0.3550 0.3704 0.3591 -0.0174 0.0059 -0.0253 12 TYR A C
+94 O O . TYR A 12 ? 0.3654 0.3814 0.3684 -0.0167 0.0055 -0.0257 12 TYR A O
+95 C CB . TYR A 12 ? 0.3071 0.3205 0.3137 -0.0176 0.0051 -0.0258 12 TYR A CB
+96 C CG . TYR A 12 ? 0.3089 0.3227 0.3151 -0.0170 0.0045 -0.0265 12 TYR A CG
+97 C CD1 . TYR A 12 ? 0.3340 0.3474 0.3392 -0.0163 0.0038 -0.0263 12 TYR A CD1
+98 C CD2 . TYR A 12 ? 0.3113 0.3261 0.3184 -0.0170 0.0045 -0.0273 12 TYR A CD2
+99 C CE1 . TYR A 12 ? 0.3406 0.3544 0.3458 -0.0158 0.0031 -0.0271 12 TYR A CE1
+100 C CE2 . TYR A 12 ? 0.3147 0.3298 0.3222 -0.0166 0.0038 -0.0278 12 TYR A CE2
+101 C CZ . TYR A 12 ? 0.3801 0.3946 0.3867 -0.0160 0.0030 -0.0278 12 TYR A CZ
+102 O OH . TYR A 12 ? 0.3384 0.3531 0.3458 -0.0156 0.0021 -0.0285 12 TYR A OH
+103 N N . ILE A 13 ? 0.3038 0.3198 0.3085 -0.0180 0.0067 -0.0256 13 ILE A N
+104 C CA . ILE A 13 ? 0.2937 0.3110 0.2977 -0.0178 0.0070 -0.0262 13 ILE A CA
+105 C C . ILE A 13 ? 0.3493 0.3679 0.3513 -0.0172 0.0071 -0.0256 13 ILE A C
+106 O O . ILE A 13 ? 0.3560 0.3756 0.3572 -0.0163 0.0066 -0.0266 13 ILE A O
+107 C CB . ILE A 13 ? 0.3188 0.3368 0.3238 -0.0184 0.0078 -0.0265 13 ILE A CB
+108 C CG1 . ILE A 13 ? 0.3055 0.3235 0.3125 -0.0186 0.0076 -0.0272 13 ILE A CG1
+109 C CG2 . ILE A 13 ? 0.3141 0.3335 0.3183 -0.0182 0.0081 -0.0270 13 ILE A CG2
+110 C CD1 . ILE A 13 ? 0.3067 0.3249 0.3144 -0.0181 0.0069 -0.0277 13 ILE A CD1
+111 N N . ALA A 14 ? 0.2965 0.3155 0.2981 -0.0177 0.0076 -0.0241 14 ALA A N
+112 C CA . ALA A 14 ? 0.3083 0.3296 0.3082 -0.0171 0.0079 -0.0230 14 ALA A CA
+113 C C . ALA A 14 ? 0.3903 0.4124 0.3891 -0.0159 0.0070 -0.0232 14 ALA A C
+114 O O . ALA A 14 ? 0.3945 0.4191 0.3917 -0.0148 0.0068 -0.0237 14 ALA A O
+115 C CB . ALA A 14 ? 0.3163 0.3378 0.3168 -0.0180 0.0085 -0.0206 14 ALA A CB
+116 N N . TYR A 15 ? 0.3574 0.3775 0.3570 -0.0159 0.0064 -0.0233 15 TYR A N
+117 C CA . TYR A 15 ? 0.3695 0.3900 0.3682 -0.0148 0.0055 -0.0237 15 TYR A CA
+118 C C . TYR A 15 ? 0.4478 0.4688 0.4464 -0.0139 0.0047 -0.0260 15 TYR A C
+119 O O . TYR A 15 ? 0.4488 0.4720 0.4462 -0.0126 0.0041 -0.0268 15 TYR A O
+120 C CB . TYR A 15 ? 0.3842 0.4024 0.3838 -0.0151 0.0051 -0.0230 15 TYR A CB
+121 C CG . TYR A 15 ? 0.4173 0.4359 0.4162 -0.0140 0.0042 -0.0238 15 TYR A CG
+122 C CD1 . TYR A 15 ? 0.4430 0.4635 0.4405 -0.0130 0.0040 -0.0226 15 TYR A CD1
+123 C CD2 . TYR A 15 ? 0.4294 0.4466 0.4293 -0.0139 0.0034 -0.0255 15 TYR A CD2
+124 C CE1 . TYR A 15 ? 0.4371 0.4581 0.4341 -0.0119 0.0031 -0.0234 15 TYR A CE1
+125 C CE2 . TYR A 15 ? 0.4459 0.4634 0.4454 -0.0129 0.0025 -0.0262 15 TYR A CE2
+126 C CZ . TYR A 15 ? 0.5141 0.5334 0.5121 -0.0119 0.0023 -0.0254 15 TYR A CZ
+127 O OH . TYR A 15 ? 0.4819 0.5017 0.4795 -0.0109 0.0014 -0.0263 15 TYR A OH
+128 N N . LEU A 16 ? 0.3884 0.4078 0.3887 -0.0145 0.0046 -0.0272 16 LEU A N
+129 C CA . LEU A 16 ? 0.3804 0.3999 0.3815 -0.0139 0.0037 -0.0291 16 LEU A CA
+130 C C . LEU A 16 ? 0.4159 0.4376 0.4163 -0.0131 0.0037 -0.0301 16 LEU A C
+131 O O . LEU A 16 ? 0.4015 0.4242 0.4020 -0.0119 0.0026 -0.0318 16 LEU A O
+132 C CB . LEU A 16 ? 0.3766 0.3945 0.3800 -0.0147 0.0036 -0.0295 16 LEU A CB
+133 C CG . LEU A 16 ? 0.4427 0.4592 0.4473 -0.0152 0.0034 -0.0290 16 LEU A CG
+134 C CD1 . LEU A 16 ? 0.4439 0.4602 0.4510 -0.0157 0.0032 -0.0293 16 LEU A CD1
+135 C CD2 . LEU A 16 ? 0.4877 0.5042 0.4921 -0.0144 0.0023 -0.0296 16 LEU A CD2
+136 N N . ARG A 17 ? 0.3782 0.4008 0.3778 -0.0136 0.0048 -0.0292 17 ARG A N
+137 C CA . ARG A 17 ? 0.3799 0.4048 0.3785 -0.0129 0.0048 -0.0300 17 ARG A CA
+138 C C . ARG A 17 ? 0.4581 0.4864 0.4547 -0.0113 0.0044 -0.0302 17 ARG A C
+139 O O . ARG A 17 ? 0.4582 0.4892 0.4541 -0.0102 0.0041 -0.0316 17 ARG A O
+140 C CB . ARG A 17 ? 0.3706 0.3958 0.3690 -0.0139 0.0061 -0.0289 17 ARG A CB
+141 C CG . ARG A 17 ? 0.4258 0.4488 0.4261 -0.0150 0.0065 -0.0292 17 ARG A CG
+142 C CD . ARG A 17 ? 0.4616 0.4855 0.4617 -0.0157 0.0076 -0.0286 17 ARG A CD
+143 N NE . ARG A 17 ? 0.6196 0.6447 0.6198 -0.0149 0.0073 -0.0300 17 ARG A NE
+144 C CZ . ARG A 17 ? 0.7271 0.7548 0.7256 -0.0142 0.0075 -0.0303 17 ARG A CZ
+145 N NH1 . ARG A 17 ? 0.5298 0.5594 0.5265 -0.0142 0.0081 -0.0289 17 ARG A NH1
+146 N NH2 . ARG A 17 ? 0.6790 0.7077 0.6778 -0.0133 0.0070 -0.0319 17 ARG A NH2
+147 N N . LYS A 18 ? 0.4614 0.4210 0.4588 -0.0092 0.0254 -0.0173 18 LYS A N
+148 C CA . LYS A 18 ? 0.4738 0.4299 0.4670 -0.0105 0.0246 -0.0174 18 LYS A CA
+149 C C . LYS A 18 ? 0.5300 0.4837 0.5210 -0.0119 0.0229 -0.0170 18 LYS A C
+150 O O . LYS A 18 ? 0.5312 0.4808 0.5177 -0.0129 0.0231 -0.0179 18 LYS A O
+151 C CB . LYS A 18 ? 0.5162 0.4731 0.5099 -0.0108 0.0233 -0.0159 18 LYS A CB
+152 C CG . LYS A 18 ? 0.7278 0.6842 0.7206 -0.0103 0.0247 -0.0164 18 LYS A CG
+153 C CD . LYS A 18 ? 0.8274 0.7858 0.8227 -0.0096 0.0240 -0.0148 18 LYS A CD
+154 C CE . LYS A 18 ? 0.8326 0.7927 0.8300 -0.0083 0.0261 -0.0156 18 LYS A CE
+155 N NZ . LYS A 18 ? 0.6942 0.6542 0.6919 -0.0076 0.0264 -0.0148 18 LYS A NZ
+156 N N . PHE A 19 ? 0.4718 0.4278 0.4659 -0.0122 0.0215 -0.0157 19 PHE A N
+157 C CA . PHE A 19 ? 0.4647 0.4190 0.4574 -0.0139 0.0196 -0.0149 19 PHE A CA
+158 C C . PHE A 19 ? 0.4878 0.4415 0.4810 -0.0136 0.0203 -0.0156 19 PHE A C
+159 O O . PHE A 19 ? 0.4873 0.4374 0.4773 -0.0150 0.0194 -0.0158 19 PHE A O
+160 C CB . PHE A 19 ? 0.4886 0.4463 0.4847 -0.0147 0.0173 -0.0126 19 PHE A CB
+161 C CG . PHE A 19 ? 0.5129 0.4720 0.5097 -0.0144 0.0168 -0.0116 19 PHE A CG
+162 C CD1 . PHE A 19 ? 0.5626 0.5187 0.5554 -0.0159 0.0152 -0.0113 19 PHE A CD1
+163 C CD2 . PHE A 19 ? 0.5417 0.5045 0.5427 -0.0125 0.0179 -0.0109 19 PHE A CD2
+164 C CE1 . PHE A 19 ? 0.5810 0.5383 0.5744 -0.0155 0.0147 -0.0101 19 PHE A CE1
+165 C CE2 . PHE A 19 ? 0.5823 0.5459 0.5838 -0.0120 0.0176 -0.0099 19 PHE A CE2
+166 C CZ . PHE A 19 ? 0.5611 0.5220 0.5590 -0.0134 0.0160 -0.0094 19 PHE A CZ
+167 N N . GLU A 20 ? 0.4154 0.3723 0.4123 -0.0117 0.0218 -0.0158 20 GLU A N
+168 C CA . GLU A 20 ? 0.3939 0.3504 0.3915 -0.0112 0.0225 -0.0162 20 GLU A CA
+169 C C . GLU A 20 ? 0.4296 0.3871 0.4282 -0.0092 0.0248 -0.0174 20 GLU A C
+170 O O . GLU A 20 ? 0.4132 0.3743 0.4150 -0.0081 0.0254 -0.0171 20 GLU A O
+171 C CB . GLU A 20 ? 0.4026 0.3626 0.4041 -0.0115 0.0214 -0.0145 20 GLU A CB
+172 C CG . GLU A 20 ? 0.4849 0.4441 0.4868 -0.0112 0.0217 -0.0145 20 GLU A CG
+173 C CD . GLU A 20 ? 0.7036 0.6574 0.7011 -0.0125 0.0213 -0.0152 20 GLU A CD
+174 O OE1 . GLU A 20 ? 0.5495 0.5018 0.5459 -0.0146 0.0194 -0.0142 20 GLU A OE1
+175 O OE2 . GLU A 20 ? 0.5724 0.5234 0.5676 -0.0113 0.0229 -0.0167 20 GLU A OE2
+176 N N . SER A 21 ? 0.4041 0.3582 0.3998 -0.0088 0.0260 -0.0187 21 SER A N
+177 C CA . SER A 21 ? 0.3991 0.3543 0.3960 -0.0070 0.0281 -0.0197 21 SER A CA
+178 C C . SER A 21 ? 0.4407 0.3984 0.4408 -0.0058 0.0283 -0.0191 21 SER A C
+179 O O . SER A 21 ? 0.4186 0.3784 0.4206 -0.0044 0.0295 -0.0195 21 SER A O
+180 C CB . SER A 21 ? 0.4626 0.4135 0.4559 -0.0066 0.0295 -0.0210 21 SER A CB
+181 O OG . SER A 21 ? 0.6600 0.6066 0.6487 -0.0083 0.0288 -0.0213 21 SER A OG
+182 N N . LYS A 22 ? 0.3850 0.3423 0.3855 -0.0066 0.0269 -0.0181 22 LYS A N
+183 C CA . LYS A 22 ? 0.3698 0.3289 0.3727 -0.0058 0.0269 -0.0173 22 LYS A CA
+184 C C . LYS A 22 ? 0.4159 0.3798 0.4223 -0.0053 0.0269 -0.0166 22 LYS A C
+185 O O . LYS A 22 ? 0.4122 0.3779 0.4203 -0.0044 0.0273 -0.0162 22 LYS A O
+186 C CB . LYS A 22 ? 0.3934 0.3503 0.3953 -0.0072 0.0255 -0.0164 22 LYS A CB
+187 C CG . LYS A 22 ? 0.3362 0.2876 0.3344 -0.0073 0.0259 -0.0172 22 LYS A CG
+188 C CD . LYS A 22 ? 0.2495 0.1981 0.2461 -0.0093 0.0243 -0.0162 22 LYS A CD
+189 C CE . LYS A 22 ? 0.3783 0.3201 0.3697 -0.0099 0.0247 -0.0173 22 LYS A CE
+190 N NZ . LYS A 22 ? 0.6428 0.5814 0.6320 -0.0124 0.0228 -0.0165 22 LYS A NZ
+191 N N . VAL A 23 ? 0.3537 0.3191 0.3606 -0.0059 0.0265 -0.0164 23 VAL A N
+192 C CA . VAL A 23 ? 0.3382 0.3073 0.3477 -0.0054 0.0269 -0.0160 23 VAL A CA
+193 C C . VAL A 23 ? 0.3833 0.3537 0.3932 -0.0042 0.0282 -0.0169 23 VAL A C
+194 O O . VAL A 23 ? 0.3747 0.3439 0.3834 -0.0040 0.0289 -0.0180 23 VAL A O
+195 C CB . VAL A 23 ? 0.3591 0.3287 0.3686 -0.0060 0.0264 -0.0156 23 VAL A CB
+196 C CG1 . VAL A 23 ? 0.3439 0.3163 0.3553 -0.0052 0.0273 -0.0154 23 VAL A CG1
+197 C CG2 . VAL A 23 ? 0.3511 0.3203 0.3608 -0.0072 0.0248 -0.0143 23 VAL A CG2
+198 N N . HIS A 24 ? 0.3632 0.3360 0.3748 -0.0036 0.0284 -0.0165 24 HIS A N
+199 C CA . HIS A 24 ? 0.3646 0.3390 0.3767 -0.0028 0.0292 -0.0171 24 HIS A CA
+200 C C . HIS A 24 ? 0.3745 0.3495 0.3863 -0.0030 0.0299 -0.0180 24 HIS A C
+201 O O . HIS A 24 ? 0.3497 0.3249 0.3613 -0.0034 0.0299 -0.0180 24 HIS A O
+202 C CB . HIS A 24 ? 0.3905 0.3671 0.4038 -0.0025 0.0291 -0.0164 24 HIS A CB
+203 C CG . HIS A 24 ? 0.4413 0.4175 0.4549 -0.0021 0.0287 -0.0156 24 HIS A CG
+204 N ND1 . HIS A 24 ? 0.4664 0.4443 0.4807 -0.0015 0.0286 -0.0152 24 HIS A ND1
+205 C CD2 . HIS A 24 ? 0.4639 0.4379 0.4770 -0.0023 0.0281 -0.0151 24 HIS A CD2
+206 C CE1 . HIS A 24 ? 0.4622 0.4389 0.4766 -0.0011 0.0282 -0.0144 24 HIS A CE1
+207 N NE2 . HIS A 24 ? 0.4656 0.4396 0.4790 -0.0016 0.0280 -0.0144 24 HIS A NE2
+208 N N . TYR A 25 ? 0.3255 0.3007 0.3373 -0.0026 0.0305 -0.0188 25 TYR A N
+209 C CA . TYR A 25 ? 0.3246 0.3005 0.3361 -0.0030 0.0312 -0.0196 25 TYR A CA
+210 C C . TYR A 25 ? 0.3933 0.3714 0.4055 -0.0033 0.0312 -0.0196 25 TYR A C
+211 O O . TYR A 25 ? 0.3751 0.3548 0.3882 -0.0030 0.0308 -0.0191 25 TYR A O
+212 C CB . TYR A 25 ? 0.3347 0.3109 0.3466 -0.0026 0.0321 -0.0202 25 TYR A CB
+213 C CG . TYR A 25 ? 0.3388 0.3159 0.3505 -0.0034 0.0329 -0.0209 25 TYR A CG
+214 C CD1 . TYR A 25 ? 0.3692 0.3441 0.3789 -0.0040 0.0334 -0.0215 25 TYR A CD1
+215 C CD2 . TYR A 25 ? 0.3379 0.3180 0.3511 -0.0037 0.0329 -0.0210 25 TYR A CD2
+216 C CE1 . TYR A 25 ? 0.3738 0.3491 0.3831 -0.0049 0.0341 -0.0220 25 TYR A CE1
+217 C CE2 . TYR A 25 ? 0.3389 0.3195 0.3516 -0.0048 0.0335 -0.0216 25 TYR A CE2
+218 C CZ . TYR A 25 ? 0.4146 0.3927 0.4254 -0.0053 0.0342 -0.0221 25 TYR A CZ
+219 O OH . TYR A 25 ? 0.3920 0.3703 0.4022 -0.0064 0.0348 -0.0226 25 TYR A OH
+220 N N . GLN A 26 ? 0.3683 0.3459 0.3795 -0.0040 0.0316 -0.0200 26 GLN A N
+221 C CA . GLN A 26 ? 0.3834 0.3620 0.3942 -0.0045 0.0318 -0.0203 26 GLN A CA
+222 C C . GLN A 26 ? 0.5331 0.5106 0.5426 -0.0053 0.0325 -0.0211 26 GLN A C
+223 O O . GLN A 26 ? 0.5480 0.5238 0.5567 -0.0054 0.0328 -0.0212 26 GLN A O
+224 C CB . GLN A 26 ? 0.3891 0.3675 0.3995 -0.0042 0.0317 -0.0196 26 GLN A CB
+225 C CG . GLN A 26 ? 0.3498 0.3263 0.3595 -0.0041 0.0321 -0.0194 26 GLN A CG
+226 C CD . GLN A 26 ? 0.4619 0.4384 0.4716 -0.0037 0.0325 -0.0188 26 GLN A CD
+227 O OE1 . GLN A 26 ? 0.4166 0.3941 0.4272 -0.0033 0.0322 -0.0179 26 GLN A OE1
+228 N NE2 . GLN A 26 ? 0.2820 0.2571 0.2904 -0.0036 0.0334 -0.0190 26 GLN A NE2
+229 N N . TYR A 27 ? 0.5426 0.5210 0.5515 -0.0062 0.0327 -0.0215 27 TYR A N
+230 C CA . TYR A 27 ? 0.5793 0.5563 0.5865 -0.0073 0.0334 -0.0223 27 TYR A CA
+231 C C . TYR A 27 ? 0.6770 0.6547 0.6832 -0.0084 0.0332 -0.0227 27 TYR A C
+232 O O . TYR A 27 ? 0.6808 0.6612 0.6883 -0.0087 0.0325 -0.0224 27 TYR A O
+233 C CB . TYR A 27 ? 0.6157 0.5926 0.6231 -0.0079 0.0339 -0.0227 27 TYR A CB
+234 C CG . TYR A 27 ? 0.6643 0.6385 0.6693 -0.0088 0.0346 -0.0232 27 TYR A CG
+235 C CD1 . TYR A 27 ? 0.6898 0.6613 0.6936 -0.0081 0.0348 -0.0229 27 TYR A CD1
+236 C CD2 . TYR A 27 ? 0.6799 0.6542 0.6840 -0.0104 0.0349 -0.0239 27 TYR A CD2
+237 C CE1 . TYR A 27 ? 0.7011 0.6698 0.7027 -0.0087 0.0355 -0.0232 27 TYR A CE1
+238 C CE2 . TYR A 27 ? 0.6941 0.6653 0.6956 -0.0113 0.0356 -0.0243 27 TYR A CE2
+239 C CZ . TYR A 27 ? 0.7936 0.7619 0.7938 -0.0103 0.0360 -0.0240 27 TYR A CZ
+240 O OH . TYR A 27 ? 0.8105 0.7753 0.8082 -0.0109 0.0367 -0.0242 27 TYR A OH
+241 N N . GLU A 28 ? 0.6675 0.6425 0.6710 -0.0090 0.0339 -0.0232 28 GLU A N
+242 C CA . GLU A 28 ? 0.6864 0.6607 0.6876 -0.0104 0.0338 -0.0237 28 GLU A CA
+243 C C . GLU A 28 ? 0.7830 0.7598 0.7847 -0.0106 0.0328 -0.0233 28 GLU A C
+244 O O . GLU A 28 ? 0.8010 0.7769 0.8017 -0.0098 0.0330 -0.0230 28 GLU A O
+245 C CB . GLU A 28 ? 0.7065 0.6806 0.7068 -0.0124 0.0339 -0.0245 28 GLU A CB
+246 C CG . GLU A 28 ? 0.8875 0.8571 0.8845 -0.0129 0.0351 -0.0251 28 GLU A CG
+247 C CD . GLU A 28 ? 1.2109 1.1798 1.2074 -0.0144 0.0355 -0.0256 28 GLU A CD
+248 O OE1 . GLU A 28 ? 1.1297 1.1018 1.1280 -0.0158 0.0349 -0.0256 28 GLU A OE1
+249 O OE2 . GLU A 28 ? 1.1811 1.1464 1.1757 -0.0142 0.0365 -0.0258 28 GLU A OE2
+250 N N . ASN A 29 ? 0.7550 0.7352 0.7586 -0.0116 0.0317 -0.0231 29 ASN A N
+251 C CA . ASN A 29 ? 0.7577 0.7406 0.7621 -0.0118 0.0304 -0.0225 29 ASN A CA
+252 C C . ASN A 29 ? 0.7956 0.7818 0.8038 -0.0104 0.0297 -0.0214 29 ASN A C
+253 O O . ASN A 29 ? 0.8006 0.7897 0.8102 -0.0105 0.0285 -0.0206 29 ASN A O
+254 C CB . ASN A 29 ? 0.8047 0.7883 0.8072 -0.0142 0.0295 -0.0228 29 ASN A CB
+255 C CG . ASN A 29 ? 1.2036 1.1834 1.2012 -0.0151 0.0299 -0.0235 29 ASN A CG
+256 O OD1 . ASN A 29 ? 1.1715 1.1516 1.1675 -0.0154 0.0291 -0.0231 29 ASN A OD1
+257 N ND2 . ASN A 29 ? 1.0966 1.0722 1.0914 -0.0153 0.0314 -0.0245 29 ASN A ND2
+258 N N . ASN A 30 ? 0.7305 0.7161 0.7403 -0.0090 0.0305 -0.0214 30 ASN A N
+259 C CA . ASN A 30 ? 0.7223 0.7092 0.7347 -0.0073 0.0303 -0.0206 30 ASN A CA
+260 C C . ASN A 30 ? 0.7622 0.7465 0.7733 -0.0064 0.0307 -0.0204 30 ASN A C
+261 O O . ASN A 30 ? 0.7754 0.7584 0.7870 -0.0055 0.0312 -0.0204 30 ASN A O
+262 C CB . ASN A 30 ? 0.6948 0.6820 0.7089 -0.0070 0.0312 -0.0209 30 ASN A CB
+263 C CG . ASN A 30 ? 0.8144 0.8033 0.8291 -0.0084 0.0314 -0.0213 30 ASN A CG
+264 O OD1 . ASN A 30 ? 0.7414 0.7339 0.7586 -0.0087 0.0309 -0.0207 30 ASN A OD1
+265 N ND2 . ASN A 30 ? 0.6254 0.6120 0.6382 -0.0094 0.0323 -0.0221 30 ASN A ND2
+266 N N . ALA A 31 ? 0.6734 0.6569 0.6826 -0.0067 0.0306 -0.0203 31 ALA A N
+267 C CA . ALA A 31 ? 0.6496 0.6310 0.6577 -0.0059 0.0312 -0.0200 31 ALA A CA
+268 C C . ALA A 31 ? 0.6399 0.6221 0.6490 -0.0049 0.0307 -0.0189 31 ALA A C
+269 O O . ALA A 31 ? 0.6569 0.6409 0.6665 -0.0050 0.0298 -0.0183 31 ALA A O
+270 C CB . ALA A 31 ? 0.6609 0.6404 0.6660 -0.0066 0.0320 -0.0206 31 ALA A CB
+271 N N . SER A 32 ? 0.5048 0.4859 0.5144 -0.0042 0.0311 -0.0184 32 SER A N
+272 C CA . SER A 32 ? 0.4731 0.4545 0.4836 -0.0035 0.0307 -0.0172 32 SER A CA
+273 C C . SER A 32 ? 0.4577 0.4387 0.4669 -0.0035 0.0315 -0.0167 32 SER A C
+274 O O . SER A 32 ? 0.4567 0.4364 0.4650 -0.0034 0.0326 -0.0171 32 SER A O
+275 C CB . SER A 32 ? 0.5196 0.5002 0.5315 -0.0030 0.0306 -0.0168 32 SER A CB
+276 O OG . SER A 32 ? 0.6678 0.6485 0.6806 -0.0029 0.0301 -0.0172 32 SER A OG
+277 N N . THR A 33 ? 0.3658 0.3474 0.3747 -0.0034 0.0311 -0.0159 33 THR A N
+278 C CA . THR A 33 ? 0.3397 0.3208 0.3473 -0.0033 0.0321 -0.0153 33 THR A CA
+279 C C . THR A 33 ? 0.3313 0.3128 0.3410 -0.0028 0.0321 -0.0140 33 THR A C
+280 O O . THR A 33 ? 0.2959 0.2778 0.3069 -0.0027 0.0310 -0.0134 33 THR A O
+281 C CB . THR A 33 ? 0.4004 0.3815 0.4052 -0.0039 0.0320 -0.0152 33 THR A CB
+282 O OG1 . THR A 33 ? 0.5090 0.4904 0.5139 -0.0037 0.0320 -0.0139 33 THR A OG1
+283 C CG2 . THR A 33 ? 0.2741 0.2563 0.2786 -0.0046 0.0305 -0.0157 33 THR A CG2
+284 N N . TYR A 34 ? 0.2702 0.3171 0.2832 0.0532 -0.0167 0.0305 34 TYR A N
+285 C CA . TYR A 34 ? 0.2613 0.3050 0.2752 0.0555 -0.0154 0.0277 34 TYR A CA
+286 C C . TYR A 34 ? 0.3264 0.3703 0.3398 0.0539 -0.0149 0.0249 34 TYR A C
+287 O O . TYR A 34 ? 0.3134 0.3578 0.3253 0.0511 -0.0157 0.0237 34 TYR A O
+288 C CB . TYR A 34 ? 0.2751 0.3143 0.2899 0.0570 -0.0161 0.0250 34 TYR A CB
+289 C CG . TYR A 34 ? 0.2921 0.3306 0.3079 0.0596 -0.0162 0.0274 34 TYR A CG
+290 C CD1 . TYR A 34 ? 0.3045 0.3440 0.3207 0.0596 -0.0176 0.0298 34 TYR A CD1
+291 C CD2 . TYR A 34 ? 0.2973 0.3337 0.3132 0.0621 -0.0150 0.0275 34 TYR A CD2
+292 C CE1 . TYR A 34 ? 0.3169 0.3555 0.3340 0.0626 -0.0178 0.0325 34 TYR A CE1
+293 C CE2 . TYR A 34 ? 0.3072 0.3421 0.3232 0.0646 -0.0150 0.0299 34 TYR A CE2
+294 C CZ . TYR A 34 ? 0.3684 0.4045 0.3852 0.0652 -0.0164 0.0324 34 TYR A CZ
+295 O OH . TYR A 34 ? 0.3709 0.4053 0.3879 0.0682 -0.0164 0.0351 34 TYR A OH
+296 N N . VAL A 35 ? 0.2920 0.3350 0.3064 0.0557 -0.0134 0.0239 35 VAL A N
+297 C CA . VAL A 35 ? 0.2862 0.3291 0.3008 0.0552 -0.0129 0.0214 35 VAL A CA
+298 C C . VAL A 35 ? 0.3482 0.3869 0.3637 0.0571 -0.0126 0.0188 35 VAL A C
+299 O O . VAL A 35 ? 0.3172 0.3546 0.3332 0.0589 -0.0120 0.0194 35 VAL A O
+300 C CB . VAL A 35 ? 0.3367 0.3845 0.3523 0.0555 -0.0112 0.0234 35 VAL A CB
+301 C CG1 . VAL A 35 ? 0.3299 0.3779 0.3457 0.0547 -0.0112 0.0209 35 VAL A CG1
+302 C CG2 . VAL A 35 ? 0.3303 0.3839 0.3455 0.0539 -0.0110 0.0275 35 VAL A CG2
+303 N N . GLY A 36 ? 0.3184 0.3549 0.3334 0.0566 -0.0128 0.0164 36 GLY A N
+304 C CA . GLY A 36 ? 0.3216 0.3549 0.3374 0.0581 -0.0126 0.0146 36 GLY A CA
+305 C C . GLY A 36 ? 0.3574 0.3886 0.3723 0.0577 -0.0125 0.0131 36 GLY A C
+306 O O . GLY A 36 ? 0.3464 0.3776 0.3595 0.0561 -0.0126 0.0128 36 GLY A O
+307 N N . VAL A 37 ? 0.3218 0.3508 0.3375 0.0591 -0.0121 0.0124 37 VAL A N
+308 C CA . VAL A 37 ? 0.3237 0.3527 0.3409 0.0604 -0.0121 0.0126 37 VAL A CA
+309 C C . VAL A 37 ? 0.4211 0.4518 0.4397 0.0613 -0.0115 0.0130 37 VAL A C
+310 O O . VAL A 37 ? 0.3920 0.4233 0.4115 0.0619 -0.0112 0.0128 37 VAL A O
+311 C CB . VAL A 37 ? 0.3562 0.3831 0.3736 0.0609 -0.0120 0.0123 37 VAL A CB
+312 C CG1 . VAL A 37 ? 0.3404 0.3679 0.3588 0.0614 -0.0122 0.0125 37 VAL A CG1
+313 C CG2 . VAL A 37 ? 0.3561 0.3813 0.3721 0.0603 -0.0115 0.0121 37 VAL A CG2
+314 N N . VAL A 38 ? 0.4066 0.4378 0.4254 0.0616 -0.0111 0.0136 38 VAL A N
+315 C CA . VAL A 38 ? 0.4068 0.4390 0.4265 0.0625 -0.0097 0.0142 38 VAL A CA
+316 C C . VAL A 38 ? 0.4583 0.4884 0.4781 0.0627 -0.0097 0.0133 38 VAL A C
+317 O O . VAL A 38 ? 0.4258 0.4560 0.4464 0.0633 -0.0085 0.0133 38 VAL A O
+318 C CB . VAL A 38 ? 0.4612 0.4946 0.4800 0.0626 -0.0084 0.0161 38 VAL A CB
+319 C CG1 . VAL A 38 ? 0.4662 0.5027 0.4849 0.0618 -0.0087 0.0175 38 VAL A CG1
+320 C CG2 . VAL A 38 ? 0.4513 0.4819 0.4685 0.0627 -0.0088 0.0163 38 VAL A CG2
+321 N N . LEU A 39 ? 0.4453 0.4738 0.4643 0.0621 -0.0108 0.0128 39 LEU A N
+322 C CA . LEU A 39 ? 0.4613 0.4885 0.4799 0.0617 -0.0111 0.0123 39 LEU A CA
+323 C C . LEU A 39 ? 0.5421 0.5695 0.5609 0.0612 -0.0122 0.0123 39 LEU A C
+324 O O . LEU A 39 ? 0.5354 0.5629 0.5538 0.0612 -0.0125 0.0124 39 LEU A O
+325 C CB . LEU A 39 ? 0.4613 0.4867 0.4779 0.0614 -0.0102 0.0124 39 LEU A CB
+326 C CG . LEU A 39 ? 0.5185 0.5419 0.5338 0.0608 -0.0090 0.0119 39 LEU A CG
+327 C CD1 . LEU A 39 ? 0.5101 0.5307 0.5223 0.0600 -0.0086 0.0118 39 LEU A CD1
+328 C CD2 . LEU A 39 ? 0.5352 0.5591 0.5515 0.0599 -0.0101 0.0113 39 LEU A CD2
+329 N N . LYS A 40 ? 0.5313 0.5592 0.5508 0.0611 -0.0126 0.0127 40 LYS A N
+330 C CA . LYS A 40 ? 0.5487 0.5775 0.5685 0.0609 -0.0129 0.0136 40 LYS A CA
+331 C C . LYS A 40 ? 0.6583 0.6880 0.6778 0.0596 -0.0134 0.0138 40 LYS A C
+332 O O . LYS A 40 ? 0.6683 0.6983 0.6881 0.0592 -0.0138 0.0146 40 LYS A O
+333 C CB . LYS A 40 ? 0.5778 0.6064 0.5982 0.0618 -0.0126 0.0148 40 LYS A CB
+334 C CG . LYS A 40 ? 0.7288 0.7585 0.7494 0.0619 -0.0120 0.0167 40 LYS A CG
+335 C CD . LYS A 40 ? 0.8535 0.8835 0.8746 0.0624 -0.0120 0.0190 40 LYS A CD
+336 C CE . LYS A 40 ? 0.9047 0.9374 0.9262 0.0621 -0.0114 0.0219 40 LYS A CE
+337 N NZ . LYS A 40 ? 0.9122 0.9445 0.9332 0.0631 -0.0093 0.0233 40 LYS A NZ
+338 N N . LYS A 41 ? 0.6431 0.6728 0.6616 0.0588 -0.0136 0.0132 41 LYS A N
+339 C CA . LYS A 41 ? 0.6678 0.6978 0.6849 0.0570 -0.0141 0.0130 41 LYS A CA
+340 C C . LYS A 41 ? 0.7666 0.7994 0.7839 0.0562 -0.0144 0.0136 41 LYS A C
+341 O O . LYS A 41 ? 0.7810 0.8126 0.7966 0.0557 -0.0145 0.0127 41 LYS A O
+342 C CB . LYS A 41 ? 0.7070 0.7335 0.7216 0.0565 -0.0134 0.0116 41 LYS A CB
+343 N N . ASN A 42 ? 0.7257 0.7623 0.7449 0.0561 -0.0143 0.0156 42 ASN A N
+344 C CA . ASN A 42 ? 0.7126 0.7500 0.7331 0.0571 -0.0138 0.0175 42 ASN A CA
+345 C C . ASN A 42 ? 0.7318 0.7705 0.7538 0.0588 -0.0124 0.0187 42 ASN A C
+346 O O . ASN A 42 ? 0.7330 0.7696 0.7550 0.0601 -0.0116 0.0191 42 ASN A O
+347 C CB . ASN A 42 ? 0.7514 0.7914 0.7720 0.0555 -0.0144 0.0198 42 ASN A CB
+348 C CG . ASN A 42 ? 1.1141 1.1515 1.1340 0.0551 -0.0153 0.0191 42 ASN A CG
+349 O OD1 . ASN A 42 ? 1.0264 1.0619 1.0471 0.0569 -0.0149 0.0194 42 ASN A OD1
+350 N ND2 . ASN A 42 ? 1.0336 1.0706 1.0517 0.0527 -0.0161 0.0182 42 ASN A ND2
+351 N N . ASP A 43 ? 0.6498 0.6917 0.6729 0.0588 -0.0117 0.0192 43 ASP A N
+352 C CA . ASP A 43 ? 0.6226 0.6657 0.6474 0.0605 -0.0097 0.0202 43 ASP A CA
+353 C C . ASP A 43 ? 0.5852 0.6249 0.6096 0.0615 -0.0100 0.0177 43 ASP A C
+354 O O . ASP A 43 ? 0.5900 0.6287 0.6149 0.0626 -0.0085 0.0178 43 ASP A O
+355 C CB . ASP A 43 ? 0.6538 0.7027 0.6807 0.0604 -0.0087 0.0217 43 ASP A CB
+356 C CG . ASP A 43 ? 0.8118 0.8624 0.8410 0.0624 -0.0061 0.0226 43 ASP A CG
+357 O OD1 . ASP A 43 ? 0.8179 0.8665 0.8466 0.0635 -0.0039 0.0239 43 ASP A OD1
+358 O OD2 . ASP A 43 ? 0.8919 0.9454 0.9231 0.0631 -0.0058 0.0220 43 ASP A OD2
+359 N N . PHE A 44 ? 0.4666 0.5043 0.4897 0.0609 -0.0117 0.0158 44 PHE A N
+360 C CA . PHE A 44 ? 0.4298 0.4649 0.4524 0.0617 -0.0121 0.0143 44 PHE A CA
+361 C C . PHE A 44 ? 0.4394 0.4715 0.4606 0.0616 -0.0124 0.0136 44 PHE A C
+362 O O . PHE A 44 ? 0.4415 0.4725 0.4617 0.0609 -0.0128 0.0135 44 PHE A O
+363 C CB . PHE A 44 ? 0.4398 0.4744 0.4615 0.0615 -0.0131 0.0135 44 PHE A CB
+364 C CG . PHE A 44 ? 0.4496 0.4878 0.4728 0.0617 -0.0130 0.0140 44 PHE A CG
+365 C CD1 . PHE A 44 ? 0.4714 0.5113 0.4970 0.0635 -0.0124 0.0143 44 PHE A CD1
+366 C CD2 . PHE A 44 ? 0.4788 0.5191 0.5013 0.0599 -0.0134 0.0144 44 PHE A CD2
+367 C CE1 . PHE A 44 ? 0.4839 0.5281 0.5117 0.0641 -0.0121 0.0149 44 PHE A CE1
+368 C CE2 . PHE A 44 ? 0.5086 0.5532 0.5326 0.0599 -0.0132 0.0151 44 PHE A CE2
+369 C CZ . PHE A 44 ? 0.4757 0.5224 0.5026 0.0622 -0.0125 0.0153 44 PHE A CZ
+370 N N . ASN A 45 ? 0.3765 0.3618 0.4065 0.0312 -0.0458 -0.0585 45 ASN A N
+371 C CA . ASN A 45 ? 0.3476 0.3371 0.3796 0.0263 -0.0410 -0.0559 45 ASN A CA
+372 C C . ASN A 45 ? 0.3412 0.3298 0.3672 0.0248 -0.0373 -0.0467 45 ASN A C
+373 O O . ASN A 45 ? 0.3415 0.3248 0.3621 0.0256 -0.0395 -0.0413 45 ASN A O
+374 C CB . ASN A 45 ? 0.3466 0.3355 0.3818 0.0242 -0.0436 -0.0566 45 ASN A CB
+375 C CG . ASN A 45 ? 0.5443 0.5355 0.5874 0.0245 -0.0468 -0.0669 45 ASN A CG
+376 O OD1 . ASN A 45 ? 0.4128 0.4088 0.4605 0.0231 -0.0442 -0.0743 45 ASN A OD1
+377 N ND2 . ASN A 45 ? 0.3918 0.3796 0.4369 0.0258 -0.0525 -0.0683 45 ASN A ND2
+378 N N . TYR A 46 ? 0.2669 0.2600 0.2937 0.0224 -0.0319 -0.0458 46 TYR A N
+379 C CA . TYR A 46 ? 0.2682 0.2617 0.2912 0.0210 -0.0284 -0.0386 46 TYR A CA
+380 C C . TYR A 46 ? 0.3212 0.3159 0.3441 0.0174 -0.0264 -0.0347 46 TYR A C
+381 O O . TYR A 46 ? 0.3160 0.3134 0.3420 0.0151 -0.0250 -0.0377 46 TYR A O
+382 C CB . TYR A 46 ? 0.2790 0.2764 0.3032 0.0214 -0.0242 -0.0402 46 TYR A CB
+383 C CG . TYR A 46 ? 0.2861 0.2827 0.3088 0.0246 -0.0252 -0.0402 46 TYR A CG
+384 C CD1 . TYR A 46 ? 0.2945 0.2910 0.3192 0.0280 -0.0278 -0.0468 46 TYR A CD1
+385 C CD2 . TYR A 46 ? 0.2954 0.2913 0.3149 0.0241 -0.0239 -0.0341 46 TYR A CD2
+386 C CE1 . TYR A 46 ? 0.3082 0.3039 0.3311 0.0311 -0.0289 -0.0468 46 TYR A CE1
+387 C CE2 . TYR A 46 ? 0.3103 0.3057 0.3283 0.0263 -0.0247 -0.0340 46 TYR A CE2
+388 C CZ . TYR A 46 ? 0.3454 0.3406 0.3647 0.0299 -0.0272 -0.0400 46 TYR A CZ
+389 O OH . TYR A 46 ? 0.3058 0.3004 0.3233 0.0321 -0.0282 -0.0397 46 TYR A OH
+390 N N . PHE A 47 ? 0.2807 0.2733 0.2998 0.0168 -0.0262 -0.0286 47 PHE A N
+391 C CA . PHE A 47 ? 0.2635 0.2573 0.2822 0.0141 -0.0245 -0.0249 47 PHE A CA
+392 C C . PHE A 47 ? 0.2899 0.2848 0.3065 0.0133 -0.0217 -0.0206 47 PHE A C
+393 O O . PHE A 47 ? 0.2722 0.2652 0.2863 0.0142 -0.0219 -0.0188 47 PHE A O
+394 C CB . PHE A 47 ? 0.2743 0.2646 0.2911 0.0139 -0.0270 -0.0232 47 PHE A CB
+395 C CG . PHE A 47 ? 0.2681 0.2582 0.2887 0.0144 -0.0301 -0.0280 47 PHE A CG
+396 C CD1 . PHE A 47 ? 0.2772 0.2712 0.3025 0.0118 -0.0293 -0.0298 47 PHE A CD1
+397 C CD2 . PHE A 47 ? 0.2893 0.2756 0.3094 0.0174 -0.0341 -0.0313 47 PHE A CD2
+398 C CE1 . PHE A 47 ? 0.2757 0.2706 0.3061 0.0116 -0.0320 -0.0354 47 PHE A CE1
+399 C CE2 . PHE A 47 ? 0.3143 0.3008 0.3393 0.0181 -0.0375 -0.0369 47 PHE A CE2
+400 C CZ . PHE A 47 ? 0.2761 0.2672 0.3067 0.0149 -0.0363 -0.0391 47 PHE A CZ
+401 N N . ILE A 48 ? 0.2627 0.2605 0.2805 0.0115 -0.0193 -0.0195 48 ILE A N
+402 C CA . ILE A 48 ? 0.2454 0.2445 0.2624 0.0109 -0.0172 -0.0163 48 ILE A CA
+403 C C . ILE A 48 ? 0.2837 0.2827 0.2996 0.0096 -0.0174 -0.0135 48 ILE A C
+404 O O . ILE A 48 ? 0.2615 0.2614 0.2780 0.0084 -0.0176 -0.0137 48 ILE A O
+405 C CB . ILE A 48 ? 0.2981 0.2990 0.3159 0.0100 -0.0151 -0.0171 48 ILE A CB
+406 C CG1 . ILE A 48 ? 0.3236 0.3249 0.3425 0.0109 -0.0139 -0.0212 48 ILE A CG1
+407 C CG2 . ILE A 48 ? 0.3418 0.3437 0.3595 0.0099 -0.0138 -0.0141 48 ILE A CG2
+408 C CD1 . ILE A 48 ? 0.4097 0.4111 0.4276 0.0092 -0.0112 -0.0226 48 ILE A CD1
+409 N N . PRO A 49 ? 0.2080 0.2065 0.2227 0.0093 -0.0169 -0.0116 49 PRO A N
+410 C CA . PRO A 49 ? 0.2290 0.2280 0.2430 0.0080 -0.0165 -0.0104 49 PRO A CA
+411 C C . PRO A 49 ? 0.3159 0.3179 0.3320 0.0079 -0.0158 -0.0098 49 PRO A C
+412 O O . PRO A 49 ? 0.2798 0.2826 0.2970 0.0084 -0.0153 -0.0096 49 PRO A O
+413 C CB . PRO A 49 ? 0.2514 0.2487 0.2636 0.0072 -0.0160 -0.0100 49 PRO A CB
+414 C CG . PRO A 49 ? 0.2843 0.2825 0.2981 0.0080 -0.0157 -0.0101 49 PRO A CG
+415 C CD . PRO A 49 ? 0.2227 0.2210 0.2373 0.0097 -0.0163 -0.0113 49 PRO A CD
+416 N N . LEU A 50 ? 0.3386 0.3419 0.3548 0.0072 -0.0158 -0.0097 50 LEU A N
+417 C CA . LEU A 50 ? 0.3579 0.3632 0.3750 0.0072 -0.0159 -0.0092 50 LEU A CA
+418 C C . LEU A 50 ? 0.4247 0.4315 0.4425 0.0073 -0.0158 -0.0097 50 LEU A C
+419 O O . LEU A 50 ? 0.4084 0.4154 0.4257 0.0065 -0.0150 -0.0107 50 LEU A O
+420 C CB . LEU A 50 ? 0.3716 0.3781 0.3887 0.0061 -0.0160 -0.0095 50 LEU A CB
+421 C CG . LEU A 50 ? 0.4539 0.4618 0.4706 0.0058 -0.0164 -0.0088 50 LEU A CG
+422 C CD1 . LEU A 50 ? 0.4462 0.4538 0.4620 0.0037 -0.0162 -0.0093 50 LEU A CD1
+423 C CD2 . LEU A 50 ? 0.5214 0.5326 0.5395 0.0057 -0.0159 -0.0094 50 LEU A CD2
+424 N N . LEU A 51 ? 0.3907 0.3983 0.4099 0.0081 -0.0167 -0.0096 51 LEU A N
+425 C CA . LEU A 51 ? 0.4133 0.4230 0.4345 0.0084 -0.0172 -0.0115 51 LEU A CA
+426 C C . LEU A 51 ? 0.4997 0.5102 0.5207 0.0097 -0.0190 -0.0112 51 LEU A C
+427 O O . LEU A 51 ? 0.4840 0.4923 0.5034 0.0104 -0.0203 -0.0094 51 LEU A O
+428 C CB . LEU A 51 ? 0.4184 0.4285 0.4425 0.0085 -0.0177 -0.0126 51 LEU A CB
+429 C CG . LEU A 51 ? 0.4887 0.4980 0.5128 0.0067 -0.0161 -0.0132 51 LEU A CG
+430 C CD1 . LEU A 51 ? 0.4980 0.5093 0.5266 0.0060 -0.0164 -0.0150 51 LEU A CD1
+431 C CD2 . LEU A 51 ? 0.5178 0.5261 0.5394 0.0048 -0.0145 -0.0149 51 LEU A CD2
+432 N N . SER A 52 ? 0.4933 0.5066 0.5153 0.0100 -0.0189 -0.0133 52 SER A N
+433 C CA . SER A 52 ? 0.5192 0.5334 0.5408 0.0115 -0.0209 -0.0133 52 SER A CA
+434 C C . SER A 52 ? 0.5996 0.6130 0.6228 0.0136 -0.0241 -0.0147 52 SER A C
+435 O O . SER A 52 ? 0.5979 0.6125 0.6246 0.0135 -0.0240 -0.0173 52 SER A O
+436 C CB . SER A 52 ? 0.5846 0.6030 0.6075 0.0114 -0.0195 -0.0158 52 SER A CB
+437 O OG . SER A 52 ? 0.7469 0.7660 0.7684 0.0097 -0.0177 -0.0139 52 SER A OG
+438 N N . TYR A 53 ? 0.5824 0.5934 0.6029 0.0151 -0.0270 -0.0130 53 TYR A N
+439 C CA . TYR A 53 ? 0.5892 0.5982 0.6107 0.0177 -0.0311 -0.0142 53 TYR A CA
+440 C C . TYR A 53 ? 0.6454 0.6588 0.6714 0.0197 -0.0327 -0.0195 53 TYR A C
+441 O O . TYR A 53 ? 0.6375 0.6539 0.6629 0.0199 -0.0318 -0.0207 53 TYR A O
+442 C CB . TYR A 53 ? 0.6110 0.6140 0.6260 0.0186 -0.0341 -0.0107 53 TYR A CB
+443 C CG . TYR A 53 ? 0.6436 0.6431 0.6586 0.0217 -0.0391 -0.0116 53 TYR A CG
+444 C CD1 . TYR A 53 ? 0.6658 0.6622 0.6818 0.0220 -0.0399 -0.0106 53 TYR A CD1
+445 C CD2 . TYR A 53 ? 0.6584 0.6578 0.6729 0.0246 -0.0433 -0.0137 53 TYR A CD2
+446 C CE1 . TYR A 53 ? 0.6777 0.6705 0.6944 0.0250 -0.0450 -0.0116 53 TYR A CE1
+447 C CE2 . TYR A 53 ? 0.6732 0.6687 0.6880 0.0279 -0.0490 -0.0150 53 TYR A CE2
+448 C CZ . TYR A 53 ? 0.7522 0.7441 0.7681 0.0281 -0.0499 -0.0138 53 TYR A CZ
+449 O OH . TYR A 53 ? 0.7491 0.7367 0.7657 0.0314 -0.0558 -0.0151 53 TYR A OH
+450 N N . ASN A 57 ? 0.9364 0.9665 1.0154 0.0220 -0.0497 -0.0583 57 ASN A N
+451 C CA . ASN A 57 ? 0.9390 0.9634 1.0072 0.0248 -0.0498 -0.0500 57 ASN A CA
+452 C C . ASN A 57 ? 0.9939 1.0118 1.0580 0.0269 -0.0527 -0.0424 57 ASN A C
+453 O O . ASN A 57 ? 0.9971 1.0113 1.0534 0.0258 -0.0494 -0.0351 57 ASN A O
+454 C CB . ASN A 57 ? 0.9569 0.9815 1.0229 0.0286 -0.0529 -0.0535 57 ASN A CB
+455 N N . PRO A 58 ? 0.9103 0.9523 0.9374 0.0115 -0.0396 0.0252 58 PRO A N
+456 C CA . PRO A 58 ? 0.9021 0.9444 0.9293 0.0118 -0.0391 0.0245 58 PRO A CA
+457 C C . PRO A 58 ? 0.9385 0.9810 0.9655 0.0123 -0.0388 0.0242 58 PRO A C
+458 O O . PRO A 58 ? 0.9223 0.9649 0.9493 0.0125 -0.0386 0.0236 58 PRO A O
+462 N N . GLU A 59 ? 0.8900 0.9326 0.9168 0.0125 -0.0389 0.0247 59 GLU A N
+463 C CA . GLU A 59 ? 0.8806 0.9234 0.9071 0.0130 -0.0387 0.0244 59 GLU A CA
+464 C C . GLU A 59 ? 0.9008 0.9433 0.9272 0.0129 -0.0390 0.0236 59 GLU A C
+465 O O . GLU A 59 ? 0.8951 0.9372 0.9211 0.0131 -0.0388 0.0231 59 GLU A O
+471 N N . LYS A 60 ? 0.8291 0.8714 0.8556 0.0127 -0.0394 0.0237 60 LYS A N
+472 C CA . LYS A 60 ? 0.8105 0.8525 0.8369 0.0125 -0.0396 0.0232 60 LYS A CA
+473 C C . LYS A 60 ? 0.8181 0.8595 0.8440 0.0125 -0.0395 0.0227 60 LYS A C
+474 O O . LYS A 60 ? 0.7948 0.8360 0.8205 0.0126 -0.0393 0.0225 60 LYS A O
+475 C CB . LYS A 60 ? 0.8384 0.8803 0.8650 0.0123 -0.0401 0.0235 60 LYS A CB
+476 C CG . LYS A 60 ? 0.9476 0.9892 0.9740 0.0122 -0.0402 0.0231 60 LYS A CG
+477 C CD . LYS A 60 ? 1.0068 1.0478 1.0331 0.0120 -0.0407 0.0231 60 LYS A CD
+478 C CE . LYS A 60 ? 1.0835 1.1246 1.1100 0.0119 -0.0407 0.0230 60 LYS A CE
+479 N NZ . LYS A 60 ? 1.2397 1.2818 1.2668 0.0118 -0.0402 0.0230 60 LYS A NZ
+480 N N . ASP A 61 ? 0.7576 0.7988 0.7835 0.0125 -0.0396 0.0227 61 ASP A N
+481 C CA . ASP A 61 ? 0.7413 0.7824 0.7672 0.0126 -0.0396 0.0225 61 ASP A CA
+482 C C . ASP A 61 ? 0.7593 0.8007 0.7855 0.0128 -0.0394 0.0224 61 ASP A C
+483 O O . ASP A 61 ? 0.7568 0.7981 0.7829 0.0130 -0.0395 0.0223 61 ASP A O
+484 C CB . ASP A 61 ? 0.7602 0.8014 0.7863 0.0125 -0.0397 0.0226 61 ASP A CB
+485 N N . LYS A 62 ? 0.6825 0.7242 0.7089 0.0128 -0.0392 0.0224 62 LYS A N
+486 C CA . LYS A 62 ? 0.6638 0.7056 0.6903 0.0130 -0.0391 0.0223 62 LYS A CA
+487 C C . LYS A 62 ? 0.6769 0.7181 0.7027 0.0132 -0.0392 0.0221 62 LYS A C
+488 O O . LYS A 62 ? 0.6743 0.7152 0.7001 0.0133 -0.0394 0.0221 62 LYS A O
+489 C CB . LYS A 62 ? 0.6962 0.7383 0.7228 0.0131 -0.0387 0.0224 62 LYS A CB
+490 N N . ALA A 63 ? 0.6042 0.6453 0.6297 0.0131 -0.0391 0.0222 63 ALA A N
+491 C CA . ALA A 63 ? 0.5884 0.6293 0.6135 0.0131 -0.0391 0.0221 63 ALA A CA
+492 C C . ALA A 63 ? 0.5968 0.6372 0.6218 0.0129 -0.0392 0.0223 63 ALA A C
+493 O O . ALA A 63 ? 0.5781 0.6181 0.6028 0.0129 -0.0394 0.0223 63 ALA A O
+494 C CB . ALA A 63 ? 0.5973 0.6387 0.6226 0.0131 -0.0389 0.0223 63 ALA A CB
+495 N N . MET A 64 ? 0.5351 0.5756 0.5603 0.0128 -0.0393 0.0224 64 MET A N
+496 C CA . MET A 64 ? 0.5266 0.5668 0.5515 0.0127 -0.0393 0.0226 64 MET A CA
+497 C C . MET A 64 ? 0.5911 0.6312 0.6161 0.0130 -0.0396 0.0230 64 MET A C
+498 O O . MET A 64 ? 0.5842 0.6239 0.6090 0.0130 -0.0397 0.0235 64 MET A O
+499 C CB . MET A 64 ? 0.5514 0.5917 0.5763 0.0128 -0.0394 0.0226 64 MET A CB
+500 C CG . MET A 64 ? 0.5900 0.6300 0.6146 0.0126 -0.0393 0.0227 64 MET A CG
+501 S SD . MET A 64 ? 0.6291 0.6696 0.6543 0.0121 -0.0391 0.0227 64 MET A SD
+502 C CE . MET A 64 ? 0.5865 0.6271 0.6119 0.0119 -0.0392 0.0227 64 MET A CE
+503 N N . LYS A 65 ? 0.5494 0.5899 0.5749 0.0133 -0.0398 0.0228 65 LYS A N
+504 C CA . LYS A 65 ? 0.5457 0.5866 0.5718 0.0136 -0.0401 0.0231 65 LYS A CA
+505 C C . LYS A 65 ? 0.5984 0.6388 0.6244 0.0135 -0.0405 0.0233 65 LYS A C
+506 O O . LYS A 65 ? 0.6027 0.6430 0.6289 0.0137 -0.0410 0.0240 65 LYS A O
+507 C CB . LYS A 65 ? 0.5715 0.6131 0.5984 0.0136 -0.0401 0.0228 65 LYS A CB
+508 C CG . LYS A 65 ? 0.7278 0.7703 0.7554 0.0139 -0.0402 0.0231 65 LYS A CG
+509 C CD . LYS A 65 ? 0.8597 0.9033 0.8887 0.0141 -0.0405 0.0232 65 LYS A CD
+510 C CE . LYS A 65 ? 0.9548 0.9996 0.9847 0.0142 -0.0403 0.0232 65 LYS A CE
+511 N NZ . LYS A 65 ? 1.0186 1.0645 1.0494 0.0148 -0.0408 0.0238 65 LYS A NZ
+512 N N . LYS A 66 ? 0.5368 0.5767 0.5623 0.0133 -0.0403 0.0229 66 LYS A N
+513 C CA . LYS A 66 ? 0.5287 0.5678 0.5537 0.0133 -0.0407 0.0229 66 LYS A CA
+514 C C . LYS A 66 ? 0.5529 0.5913 0.5773 0.0130 -0.0407 0.0234 66 LYS A C
+515 O O . LYS A 66 ? 0.5472 0.5847 0.5712 0.0129 -0.0413 0.0238 66 LYS A O
+516 C CB . LYS A 66 ? 0.5647 0.6036 0.5892 0.0134 -0.0404 0.0223 66 LYS A CB
+517 N N . ARG A 67 ? 0.4692 0.5079 0.4935 0.0128 -0.0402 0.0236 67 ARG A N
+518 C CA . ARG A 67 ? 0.4370 0.4752 0.4609 0.0124 -0.0401 0.0242 67 ARG A CA
+519 C C . ARG A 67 ? 0.3957 0.4339 0.4198 0.0125 -0.0402 0.0252 67 ARG A C
+520 O O . ARG A 67 ? 0.3687 0.4068 0.3925 0.0122 -0.0398 0.0256 67 ARG A O
+521 C CB . ARG A 67 ? 0.4639 0.5024 0.4878 0.0120 -0.0396 0.0238 67 ARG A CB
+522 C CG . ARG A 67 ? 0.6228 0.6621 0.6470 0.0121 -0.0392 0.0233 67 ARG A CG
+523 C CD . ARG A 67 ? 0.6564 0.6963 0.6809 0.0118 -0.0389 0.0230 67 ARG A CD
+524 N NE . ARG A 67 ? 0.6494 0.6893 0.6737 0.0121 -0.0389 0.0227 67 ARG A NE
+525 C CZ . ARG A 67 ? 0.9351 0.9759 0.9598 0.0122 -0.0387 0.0225 67 ARG A CZ
+526 N NH1 . ARG A 67 ? 0.7832 0.8250 0.8087 0.0119 -0.0385 0.0226 67 ARG A NH1
+527 N NH2 . ARG A 67 ? 0.8309 0.8716 0.8551 0.0126 -0.0388 0.0222 67 ARG A NH2
+528 N N . SER A 68 ? 0.3238 0.3623 0.3483 0.0130 -0.0407 0.0256 68 SER A N
+529 C CA . SER A 68 ? 0.3153 0.3541 0.3400 0.0134 -0.0409 0.0267 68 SER A CA
+530 C C . SER A 68 ? 0.3307 0.3688 0.3549 0.0131 -0.0409 0.0281 68 SER A C
+531 O O . SER A 68 ? 0.2965 0.3347 0.3206 0.0135 -0.0408 0.0291 68 SER A O
+532 C CB . SER A 68 ? 0.3485 0.3880 0.3741 0.0140 -0.0415 0.0270 68 SER A CB
+533 O OG . SER A 68 ? 0.4867 0.5259 0.5127 0.0140 -0.0424 0.0276 68 SER A OG
+534 N N . ARG A 69 ? 0.3237 0.3588 0.3187 -0.0251 -0.0136 0.0383 69 ARG A N
+535 C CA . ARG A 69 ? 0.3240 0.3603 0.3160 -0.0296 -0.0142 0.0417 69 ARG A CA
+536 C C . ARG A 69 ? 0.3426 0.3847 0.3396 -0.0313 -0.0151 0.0435 69 ARG A C
+537 O O . ARG A 69 ? 0.3296 0.3738 0.3264 -0.0344 -0.0158 0.0473 69 ARG A O
+538 C CB . ARG A 69 ? 0.3456 0.3789 0.3321 -0.0345 -0.0122 0.0411 69 ARG A CB
+539 C CG . ARG A 69 ? 0.4704 0.4978 0.4504 -0.0350 -0.0118 0.0411 69 ARG A CG
+540 C CD . ARG A 69 ? 0.4629 0.4866 0.4368 -0.0401 -0.0094 0.0400 69 ARG A CD
+541 N NE . ARG A 69 ? 0.5599 0.5814 0.5351 -0.0382 -0.0068 0.0353 69 ARG A NE
+542 C CZ . ARG A 69 ? 0.7769 0.7944 0.7472 -0.0417 -0.0039 0.0329 69 ARG A CZ
+543 N NH1 . ARG A 69 ? 0.6271 0.6423 0.5903 -0.0480 -0.0035 0.0349 69 ARG A NH1
+544 N NH2 . ARG A 69 ? 0.5679 0.5835 0.5401 -0.0393 -0.0013 0.0289 69 ARG A NH2
+545 N N . ILE A 70 ? 0.2933 0.3380 0.2949 -0.0293 -0.0151 0.0413 70 ILE A N
+546 C CA . ILE A 70 ? 0.2860 0.3364 0.2929 -0.0308 -0.0161 0.0424 70 ILE A CA
+547 C C . ILE A 70 ? 0.2957 0.3483 0.3077 -0.0264 -0.0176 0.0417 70 ILE A C
+548 O O . ILE A 70 ? 0.2655 0.3226 0.2821 -0.0273 -0.0188 0.0433 70 ILE A O
+549 C CB . ILE A 70 ? 0.3411 0.3925 0.3472 -0.0339 -0.0147 0.0402 70 ILE A CB
+550 C CG1 . ILE A 70 ? 0.3412 0.3963 0.3472 -0.0405 -0.0147 0.0427 70 ILE A CG1
+551 C CG2 . ILE A 70 ? 0.3812 0.4346 0.3909 -0.0309 -0.0150 0.0376 70 ILE A CG2
+552 C CD1 . ILE A 70 ? 0.3659 0.4173 0.3658 -0.0440 -0.0136 0.0443 70 ILE A CD1
+553 N N . VAL A 71 ? 0.2559 0.3056 0.2674 -0.0221 -0.0175 0.0397 71 VAL A N
+554 C CA . VAL A 71 ? 0.2590 0.3100 0.2740 -0.0185 -0.0188 0.0391 71 VAL A CA
+555 C C . VAL A 71 ? 0.3023 0.3508 0.3162 -0.0157 -0.0191 0.0394 71 VAL A C
+556 O O . VAL A 71 ? 0.2715 0.3167 0.2823 -0.0151 -0.0184 0.0389 71 VAL A O
+557 C CB . VAL A 71 ? 0.3098 0.3607 0.3258 -0.0166 -0.0184 0.0369 71 VAL A CB
+558 C CG1 . VAL A 71 ? 0.3122 0.3628 0.3302 -0.0129 -0.0195 0.0368 71 VAL A CG1
+559 C CG2 . VAL A 71 ? 0.2984 0.3534 0.3166 -0.0190 -0.0187 0.0368 71 VAL A CG2
+560 N N . THR A 72 ? 0.2592 0.3092 0.2757 -0.0142 -0.0203 0.0403 72 THR A N
+561 C CA . THR A 72 ? 0.2675 0.3157 0.2831 -0.0117 -0.0206 0.0403 72 THR A CA
+562 C C . THR A 72 ? 0.3289 0.3770 0.3461 -0.0094 -0.0213 0.0389 72 THR A C
+563 O O . THR A 72 ? 0.3136 0.3636 0.3333 -0.0092 -0.0220 0.0389 72 THR A O
+564 C CB . THR A 72 ? 0.3256 0.3750 0.3423 -0.0118 -0.0209 0.0423 72 THR A CB
+565 O OG1 . THR A 72 ? 0.3663 0.4157 0.3811 -0.0143 -0.0205 0.0445 72 THR A OG1
+566 C CG2 . THR A 72 ? 0.2860 0.3340 0.3016 -0.0094 -0.0212 0.0419 72 THR A CG2
+567 N N . ARG A 73 ? 0.3109 0.3571 0.3270 -0.0078 -0.0212 0.0382 73 ARG A N
+568 C CA . ARG A 73 ? 0.3143 0.3603 0.3315 -0.0063 -0.0217 0.0377 73 ARG A CA
+569 C C . ARG A 73 ? 0.3423 0.3884 0.3595 -0.0056 -0.0225 0.0380 73 ARG A C
+570 O O . ARG A 73 ? 0.3211 0.3669 0.3371 -0.0056 -0.0225 0.0382 73 ARG A O
+571 C CB . ARG A 73 ? 0.3267 0.3712 0.3438 -0.0057 -0.0211 0.0375 73 ARG A CB
+572 C CG . ARG A 73 ? 0.4498 0.4935 0.4668 -0.0061 -0.0198 0.0369 73 ARG A CG
+573 C CD . ARG A 73 ? 0.5860 0.6278 0.6034 -0.0054 -0.0188 0.0368 73 ARG A CD
+574 N NE . ARG A 73 ? 0.6923 0.7348 0.7124 -0.0043 -0.0193 0.0379 73 ARG A NE
+575 C CZ . ARG A 73 ? 0.7793 0.8213 0.8013 -0.0039 -0.0191 0.0386 73 ARG A CZ
+576 N NH1 . ARG A 73 ? 0.5656 0.6061 0.5869 -0.0042 -0.0187 0.0380 73 ARG A NH1
+577 N NH2 . ARG A 73 ? 0.5645 0.6077 0.5895 -0.0037 -0.0195 0.0404 73 ARG A NH2
+578 N N . LEU A 74 ? 0.3028 0.3493 0.3209 -0.0052 -0.0232 0.0379 74 LEU A N
+579 C CA . LEU A 74 ? 0.2987 0.3446 0.3162 -0.0049 -0.0235 0.0377 74 LEU A CA
+580 C C . LEU A 74 ? 0.3700 0.4152 0.3865 -0.0050 -0.0240 0.0379 74 LEU A C
+581 O O . LEU A 74 ? 0.3660 0.4113 0.3831 -0.0050 -0.0243 0.0387 74 LEU A O
+582 C CB . LEU A 74 ? 0.2924 0.3388 0.3112 -0.0050 -0.0242 0.0377 74 LEU A CB
+583 C CG . LEU A 74 ? 0.3372 0.3849 0.3582 -0.0054 -0.0238 0.0381 74 LEU A CG
+584 C CD1 . LEU A 74 ? 0.3092 0.3574 0.3300 -0.0059 -0.0227 0.0389 74 LEU A CD1
+585 C CD2 . LEU A 74 ? 0.3654 0.4155 0.3890 -0.0061 -0.0249 0.0386 74 LEU A CD2
+586 N N . PHE A 75 ? 0.3426 0.3874 0.3579 -0.0053 -0.0238 0.0376 75 PHE A N
+587 C CA . PHE A 75 ? 0.3516 0.3964 0.3663 -0.0063 -0.0244 0.0381 75 PHE A CA
+588 C C . PHE A 75 ? 0.3955 0.4392 0.4081 -0.0071 -0.0243 0.0373 75 PHE A C
+589 O O . PHE A 75 ? 0.3801 0.4228 0.3922 -0.0063 -0.0236 0.0363 75 PHE A O
+590 C CB . PHE A 75 ? 0.3849 0.4311 0.4004 -0.0066 -0.0245 0.0384 75 PHE A CB
+591 C CG . PHE A 75 ? 0.4139 0.4603 0.4311 -0.0059 -0.0243 0.0389 75 PHE A CG
+592 C CD1 . PHE A 75 ? 0.4570 0.5035 0.4762 -0.0062 -0.0242 0.0401 75 PHE A CD1
+593 C CD2 . PHE A 75 ? 0.4381 0.4841 0.4546 -0.0053 -0.0238 0.0384 75 PHE A CD2
+594 C CE1 . PHE A 75 ? 0.4622 0.5082 0.4828 -0.0054 -0.0234 0.0402 75 PHE A CE1
+595 C CE2 . PHE A 75 ? 0.4685 0.5139 0.4858 -0.0051 -0.0232 0.0386 75 PHE A CE2
+596 C CZ . PHE A 75 ? 0.4437 0.4889 0.4631 -0.0050 -0.0229 0.0391 75 PHE A CZ
+597 N N . GLU A 76 ? 0.3583 0.4021 0.3698 -0.0090 -0.0248 0.0380 76 GLU A N
+598 C CA . GLU A 76 ? 0.3591 0.4014 0.3677 -0.0105 -0.0244 0.0370 76 GLU A CA
+599 C C . GLU A 76 ? 0.4210 0.4649 0.4292 -0.0113 -0.0240 0.0361 76 GLU A C
+600 O O . GLU A 76 ? 0.4189 0.4655 0.4287 -0.0125 -0.0249 0.0373 76 GLU A O
+601 C CB . GLU A 76 ? 0.3718 0.4134 0.3788 -0.0130 -0.0253 0.0389 76 GLU A CB
+602 C CG . GLU A 76 ? 0.4771 0.5164 0.4799 -0.0155 -0.0249 0.0380 76 GLU A CG
+603 C CD . GLU A 76 ? 0.6762 0.7145 0.6766 -0.0185 -0.0260 0.0406 76 GLU A CD
+604 O OE1 . GLU A 76 ? 0.6101 0.6500 0.6127 -0.0187 -0.0271 0.0436 76 GLU A OE1
+605 O OE2 . GLU A 76 ? 0.5529 0.5884 0.5489 -0.0209 -0.0256 0.0398 76 GLU A OE2
+606 N N . ILE A 77 ? 0.3919 0.4346 0.3983 -0.0106 -0.0227 0.0343 77 ILE A N
+607 C CA . ILE A 77 ? 0.4108 0.4554 0.4165 -0.0115 -0.0224 0.0335 77 ILE A CA
+608 C C . ILE A 77 ? 0.4901 0.5353 0.4937 -0.0153 -0.0229 0.0336 77 ILE A C
+609 O O . ILE A 77 ? 0.4970 0.5391 0.4978 -0.0169 -0.0223 0.0332 77 ILE A O
+610 C CB . ILE A 77 ? 0.4626 0.5058 0.4674 -0.0095 -0.0204 0.0319 77 ILE A CB
+611 C CG1 . ILE A 77 ? 0.4707 0.5155 0.4779 -0.0070 -0.0206 0.0332 77 ILE A CG1
+612 C CG2 . ILE A 77 ? 0.4638 0.5078 0.4662 -0.0110 -0.0194 0.0305 77 ILE A CG2
+613 C CD1 . ILE A 77 ? 0.5677 0.6107 0.5756 -0.0050 -0.0188 0.0330 77 ILE A CD1
+614 N N . GLY A 78 ? 0.4595 0.5089 0.4648 -0.0172 -0.0242 0.0346 78 GLY A N
+615 C CA . GLY A 78 ? 0.4683 0.5199 0.4729 -0.0218 -0.0251 0.0355 78 GLY A CA
+616 C C . GLY A 78 ? 0.5123 0.5644 0.5188 -0.0240 -0.0263 0.0385 78 GLY A C
+617 O O . GLY A 78 ? 0.5129 0.5658 0.5181 -0.0285 -0.0267 0.0401 78 GLY A O
+618 N N . ASN A 79 ? 0.4537 0.5052 0.4630 -0.0211 -0.0266 0.0397 79 ASN A N
+619 C CA . ASN A 79 ? 0.4438 0.4957 0.4558 -0.0217 -0.0274 0.0428 79 ASN A CA
+620 C C . ASN A 79 ? 0.4564 0.5078 0.4710 -0.0176 -0.0272 0.0424 79 ASN A C
+621 O O . ASN A 79 ? 0.4274 0.4767 0.4420 -0.0161 -0.0269 0.0431 79 ASN A O
+622 C CB . ASN A 79 ? 0.4632 0.5116 0.4715 -0.0231 -0.0271 0.0439 79 ASN A CB
+623 C CG . ASN A 79 ? 0.6081 0.6574 0.6189 -0.0244 -0.0280 0.0481 79 ASN A CG
+624 O OD1 . ASN A 79 ? 0.4369 0.4896 0.4526 -0.0253 -0.0285 0.0505 79 ASN A OD1
+625 N ND2 . ASN A 79 ? 0.5373 0.5836 0.5451 -0.0245 -0.0282 0.0494 79 ASN A ND2
+626 N N . ILE A 80 ? 0.4282 0.4818 0.4447 -0.0162 -0.0275 0.0414 80 ILE A N
+627 C CA . ILE A 80 ? 0.4272 0.4802 0.4450 -0.0130 -0.0273 0.0408 80 ILE A CA
+628 C C . ILE A 80 ? 0.4898 0.5424 0.5107 -0.0122 -0.0271 0.0424 80 ILE A C
+629 O O . ILE A 80 ? 0.5033 0.5542 0.5239 -0.0099 -0.0264 0.0415 80 ILE A O
+630 C CB . ILE A 80 ? 0.4664 0.5219 0.4846 -0.0126 -0.0281 0.0401 80 ILE A CB
+631 C CG1 . ILE A 80 ? 0.4692 0.5228 0.4856 -0.0097 -0.0274 0.0390 80 ILE A CG1
+632 C CG2 . ILE A 80 ? 0.4846 0.5440 0.5073 -0.0139 -0.0299 0.0420 80 ILE A CG2
+633 C CD1 . ILE A 80 ? 0.5395 0.5910 0.5527 -0.0088 -0.0260 0.0375 80 ILE A CD1
+634 N N . ASN A 81 ? 0.4619 0.4983 0.4740 0.0153 -0.0015 0.0350 81 ASN A N
+635 C CA . ASN A 81 ? 0.4625 0.5023 0.4790 0.0164 -0.0016 0.0363 81 ASN A CA
+636 C C . ASN A 81 ? 0.5059 0.5494 0.5244 0.0147 -0.0036 0.0353 81 ASN A C
+637 O O . ASN A 81 ? 0.5224 0.5686 0.5448 0.0155 -0.0035 0.0363 81 ASN A O
+638 C CB . ASN A 81 ? 0.4714 0.5137 0.4885 0.0190 -0.0015 0.0396 81 ASN A CB
+639 C CG . ASN A 81 ? 0.7345 0.7726 0.7513 0.0210 0.0015 0.0405 81 ASN A CG
+640 O OD1 . ASN A 81 ? 0.7581 0.7936 0.7775 0.0214 0.0039 0.0398 81 ASN A OD1
+641 N ND2 . ASN A 81 ? 0.5762 0.6131 0.5895 0.0219 0.0015 0.0415 81 ASN A ND2
+642 N N . ASN A 82 ? 0.4501 0.4933 0.4660 0.0123 -0.0048 0.0333 82 ASN A N
+643 C CA . ASN A 82 ? 0.4430 0.4891 0.4606 0.0104 -0.0062 0.0320 82 ASN A CA
+644 C C . ASN A 82 ? 0.4725 0.5156 0.4915 0.0095 -0.0047 0.0299 82 ASN A C
+645 O O . ASN A 82 ? 0.4517 0.4915 0.4681 0.0084 -0.0038 0.0284 82 ASN A O
+646 C CB . ASN A 82 ? 0.4272 0.4748 0.4409 0.0080 -0.0082 0.0310 82 ASN A CB
+647 C CG . ASN A 82 ? 0.5702 0.6202 0.5853 0.0057 -0.0092 0.0293 82 ASN A CG
+648 O OD1 . ASN A 82 ? 0.4049 0.4585 0.4243 0.0062 -0.0099 0.0300 82 ASN A OD1
+649 N ND2 . ASN A 82 ? 0.5443 0.5920 0.5561 0.0033 -0.0089 0.0270 82 ASN A ND2
+650 N N . PRO A 83 ? 0.4332 0.4775 0.4563 0.0102 -0.0041 0.0300 83 PRO A N
+651 C CA . PRO A 83 ? 0.4347 0.4767 0.4589 0.0095 -0.0027 0.0282 83 PRO A CA
+652 C C . PRO A 83 ? 0.4843 0.5271 0.5080 0.0074 -0.0034 0.0265 83 PRO A C
+653 O O . PRO A 83 ? 0.5149 0.5609 0.5392 0.0066 -0.0050 0.0266 83 PRO A O
+654 C CB . PRO A 83 ? 0.4553 0.4981 0.4834 0.0107 -0.0018 0.0290 83 PRO A CB
+655 C CG . PRO A 83 ? 0.5131 0.5596 0.5430 0.0117 -0.0030 0.0310 83 PRO A CG
+656 C CD . PRO A 83 ? 0.4571 0.5048 0.4840 0.0117 -0.0044 0.0320 83 PRO A CD
+657 N N . LEU A 84 ? 0.4238 0.4638 0.4464 0.0066 -0.0021 0.0251 84 LEU A N
+658 C CA . LEU A 84 ? 0.4090 0.4488 0.4308 0.0049 -0.0018 0.0235 84 LEU A CA
+659 C C . LEU A 84 ? 0.4177 0.4574 0.4421 0.0050 -0.0006 0.0228 84 LEU A C
+660 O O . LEU A 84 ? 0.4038 0.4440 0.4287 0.0038 -0.0004 0.0217 84 LEU A O
+661 C CB . LEU A 84 ? 0.4134 0.4496 0.4313 0.0041 -0.0006 0.0230 84 LEU A CB
+662 C CG . LEU A 84 ? 0.4782 0.5140 0.4922 0.0024 -0.0013 0.0225 84 LEU A CG
+663 C CD1 . LEU A 84 ? 0.4803 0.5192 0.4939 0.0028 -0.0036 0.0236 84 LEU A CD1
+664 C CD2 . LEU A 84 ? 0.4881 0.5196 0.4986 0.0023 0.0004 0.0224 84 LEU A CD2
+665 N N . GLY A 85 ? 0.3346 0.3734 0.3604 0.0062 0.0002 0.0233 85 GLY A N
+666 C CA . GLY A 85 ? 0.3172 0.3561 0.3450 0.0063 0.0013 0.0228 85 GLY A CA
+667 C C . GLY A 85 ? 0.3271 0.3649 0.3553 0.0071 0.0022 0.0231 85 GLY A C
+668 O O . GLY A 85 ? 0.3129 0.3499 0.3406 0.0076 0.0022 0.0237 85 GLY A O
+669 N N . TYR A 86 ? 0.2824 0.3204 0.3115 0.0070 0.0031 0.0227 86 TYR A N
+670 C CA . TYR A 86 ? 0.2985 0.3363 0.3280 0.0071 0.0038 0.0227 86 TYR A CA
+671 C C . TYR A 86 ? 0.3430 0.3813 0.3723 0.0068 0.0047 0.0227 86 TYR A C
+672 O O . TYR A 86 ? 0.3110 0.3500 0.3409 0.0069 0.0052 0.0226 86 TYR A O
+673 C CB . TYR A 86 ? 0.3371 0.3754 0.3683 0.0074 0.0040 0.0224 86 TYR A CB
+674 C CG . TYR A 86 ? 0.3913 0.4297 0.4236 0.0080 0.0035 0.0229 86 TYR A CG
+675 C CD1 . TYR A 86 ? 0.4310 0.4683 0.4630 0.0085 0.0037 0.0236 86 TYR A CD1
+676 C CD2 . TYR A 86 ? 0.3978 0.4375 0.4318 0.0082 0.0030 0.0230 86 TYR A CD2
+677 C CE1 . TYR A 86 ? 0.4755 0.5134 0.5089 0.0095 0.0035 0.0247 86 TYR A CE1
+678 C CE2 . TYR A 86 ? 0.4077 0.4484 0.4432 0.0089 0.0024 0.0240 86 TYR A CE2
+679 C CZ . TYR A 86 ? 0.5536 0.5935 0.5889 0.0096 0.0027 0.0250 86 TYR A CZ
+680 O OH . TYR A 86 ? 0.6027 0.6440 0.6398 0.0107 0.0024 0.0265 86 TYR A OH
+681 N N . LEU A 87 ? 0.3097 0.3479 0.3385 0.0067 0.0051 0.0231 87 LEU A N
+682 C CA . LEU A 87 ? 0.3124 0.3521 0.3414 0.0065 0.0058 0.0237 87 LEU A CA
+683 C C . LEU A 87 ? 0.3340 0.3751 0.3636 0.0060 0.0056 0.0232 87 LEU A C
+684 O O . LEU A 87 ? 0.3201 0.3604 0.3494 0.0055 0.0055 0.0226 87 LEU A O
+685 C CB . LEU A 87 ? 0.3194 0.3586 0.3478 0.0063 0.0062 0.0246 87 LEU A CB
+686 C CG . LEU A 87 ? 0.3846 0.4222 0.4121 0.0066 0.0069 0.0253 87 LEU A CG
+687 C CD1 . LEU A 87 ? 0.4046 0.4414 0.4317 0.0066 0.0075 0.0262 87 LEU A CD1
+688 C CD2 . LEU A 87 ? 0.4080 0.4464 0.4359 0.0069 0.0083 0.0259 87 LEU A CD2
+689 N N . LEU A 88 ? 0.2661 0.3089 0.2960 0.0061 0.0060 0.0233 88 LEU A N
+690 C CA . LEU A 88 ? 0.2491 0.2932 0.2790 0.0055 0.0059 0.0227 88 LEU A CA
+691 C C . LEU A 88 ? 0.2548 0.3019 0.2844 0.0049 0.0059 0.0236 88 LEU A C
+692 O O . LEU A 88 ? 0.2250 0.2744 0.2549 0.0053 0.0063 0.0244 88 LEU A O
+693 C CB . LEU A 88 ? 0.2533 0.2973 0.2837 0.0061 0.0064 0.0224 88 LEU A CB
+694 C CG . LEU A 88 ? 0.3147 0.3565 0.3457 0.0064 0.0063 0.0215 88 LEU A CG
+695 C CD1 . LEU A 88 ? 0.3076 0.3483 0.3392 0.0068 0.0058 0.0216 88 LEU A CD1
+696 C CD2 . LEU A 88 ? 0.3680 0.4099 0.3997 0.0070 0.0070 0.0213 88 LEU A CD2
+697 N N . HIS A 89 ? 0.2021 0.2497 0.2316 0.0039 0.0056 0.0236 89 HIS A N
+698 C CA . HIS A 89 ? 0.1991 0.2503 0.2288 0.0030 0.0053 0.0246 89 HIS A CA
+699 C C . HIS A 89 ? 0.2817 0.3361 0.3107 0.0021 0.0049 0.0243 89 HIS A C
+700 O O . HIS A 89 ? 0.2704 0.3288 0.2999 0.0022 0.0048 0.0260 89 HIS A O
+701 C CB . HIS A 89 ? 0.2092 0.2599 0.2389 0.0016 0.0051 0.0239 89 HIS A CB
+702 C CG . HIS A 89 ? 0.2482 0.2961 0.2782 0.0025 0.0055 0.0244 89 HIS A CG
+703 N ND1 . HIS A 89 ? 0.2747 0.3239 0.3058 0.0029 0.0058 0.0262 89 HIS A ND1
+704 C CD2 . HIS A 89 ? 0.2626 0.3068 0.2921 0.0032 0.0057 0.0237 89 HIS A CD2
+705 C CE1 . HIS A 89 ? 0.2601 0.3057 0.2908 0.0036 0.0062 0.0261 89 HIS A CE1
+706 N NE2 . HIS A 89 ? 0.2634 0.3063 0.2931 0.0038 0.0061 0.0247 89 HIS A NE2
+707 N N . HIS A 90 ? 0.2448 0.2972 0.2724 0.0013 0.0050 0.0225 90 HIS A N
+708 C CA . HIS A 90 ? 0.2539 0.3083 0.2800 0.0003 0.0049 0.0219 90 HIS A CA
+709 C C . HIS A 90 ? 0.2659 0.3221 0.2924 0.0019 0.0052 0.0233 90 HIS A C
+710 O O . HIS A 90 ? 0.2685 0.3277 0.2938 0.0013 0.0050 0.0235 90 HIS A O
+711 C CB . HIS A 90 ? 0.2784 0.3291 0.3030 -0.0008 0.0056 0.0196 90 HIS A CB
+712 C CG . HIS A 90 ? 0.3246 0.3715 0.3500 0.0009 0.0064 0.0194 90 HIS A CG
+713 N ND1 . HIS A 90 ? 0.3526 0.3974 0.3795 0.0021 0.0064 0.0198 90 HIS A ND1
+714 C CD2 . HIS A 90 ? 0.3516 0.3968 0.3765 0.0014 0.0072 0.0188 90 HIS A CD2
+715 C CE1 . HIS A 90 ? 0.3422 0.3847 0.3698 0.0032 0.0070 0.0196 90 HIS A CE1
+716 N NE2 . HIS A 90 ? 0.3471 0.3896 0.3737 0.0028 0.0076 0.0190 90 HIS A NE2
+717 N N . ASN A 91 ? 0.2072 0.2618 0.2352 0.0039 0.0059 0.0242 91 ASN A N
+718 C CA . ASN A 91 ? 0.2098 0.2655 0.2386 0.0056 0.0068 0.0255 91 ASN A CA
+719 C C . ASN A 91 ? 0.2518 0.3098 0.2821 0.0069 0.0075 0.0279 91 ASN A C
+720 O O . ASN A 91 ? 0.2367 0.2945 0.2678 0.0085 0.0090 0.0290 91 ASN A O
+721 C CB . ASN A 91 ? 0.2042 0.2561 0.2335 0.0066 0.0076 0.0244 91 ASN A CB
+722 C CG . ASN A 91 ? 0.3949 0.4449 0.4229 0.0059 0.0076 0.0227 91 ASN A CG
+723 O OD1 . ASN A 91 ? 0.3986 0.4502 0.4249 0.0049 0.0075 0.0224 91 ASN A OD1
+724 N ND2 . ASN A 91 ? 0.2945 0.3412 0.3234 0.0062 0.0078 0.0217 91 ASN A ND2
+725 N N . MET A 92 ? 0.2023 0.2620 0.2331 0.0061 0.0069 0.0287 92 MET A N
+726 C CA . MET A 92 ? 0.2137 0.2754 0.2462 0.0074 0.0080 0.0314 92 MET A CA
+727 C C . MET A 92 ? 0.2745 0.3414 0.3076 0.0083 0.0085 0.0338 92 MET A C
+728 O O . MET A 92 ? 0.2568 0.3265 0.2885 0.0073 0.0073 0.0333 92 MET A O
+729 C CB . MET A 92 ? 0.2394 0.3016 0.2725 0.0065 0.0074 0.0319 92 MET A CB
+730 C CG . MET A 92 ? 0.2870 0.3537 0.3200 0.0047 0.0058 0.0320 92 MET A CG
+731 S SD . MET A 92 ? 0.3456 0.4129 0.3800 0.0037 0.0055 0.0327 92 MET A SD
+732 C CE . MET A 92 ? 0.3097 0.3840 0.3442 0.0014 0.0037 0.0331 92 MET A CE
+733 N N . ILE A 93 ? 0.2550 0.2399 0.2881 0.0200 -0.0415 -0.0313 93 ILE A N
+734 C CA . ILE A 93 ? 0.2416 0.2272 0.2763 0.0220 -0.0423 -0.0319 93 ILE A CA
+735 C C . ILE A 93 ? 0.3104 0.2947 0.3470 0.0221 -0.0401 -0.0326 93 ILE A C
+736 O O . ILE A 93 ? 0.2929 0.2755 0.3277 0.0204 -0.0378 -0.0320 93 ILE A O
+737 C CB . ILE A 93 ? 0.2744 0.2593 0.3039 0.0221 -0.0426 -0.0313 93 ILE A CB
+738 C CG1 . ILE A 93 ? 0.2822 0.2647 0.3074 0.0199 -0.0401 -0.0309 93 ILE A CG1
+739 C CG2 . ILE A 93 ? 0.2555 0.2424 0.2835 0.0229 -0.0457 -0.0310 93 ILE A CG2
+740 C CD1 . ILE A 93 ? 0.3221 0.3036 0.3439 0.0199 -0.0395 -0.0307 93 ILE A CD1
+741 N N . PRO A 94 ? 0.2902 0.2754 0.3299 0.0246 -0.0409 -0.0342 94 PRO A N
+742 C CA . PRO A 94 ? 0.2834 0.2672 0.3233 0.0247 -0.0391 -0.0353 94 PRO A CA
+743 C C . PRO A 94 ? 0.3329 0.3147 0.3670 0.0245 -0.0381 -0.0345 94 PRO A C
+744 O O . PRO A 94 ? 0.3346 0.3164 0.3664 0.0259 -0.0391 -0.0341 94 PRO A O
+745 C CB . PRO A 94 ? 0.2990 0.2844 0.3436 0.0281 -0.0405 -0.0379 94 PRO A CB
+746 C CG . PRO A 94 ? 0.3460 0.3332 0.3907 0.0306 -0.0431 -0.0377 94 PRO A CG
+747 C CD . PRO A 94 ? 0.2968 0.2843 0.3392 0.0280 -0.0436 -0.0353 94 PRO A CD
+748 N N . VAL A 95 ? 0.2793 0.2596 0.3114 0.0228 -0.0363 -0.0341 95 VAL A N
+749 C CA . VAL A 95 ? 0.2734 0.2520 0.3008 0.0225 -0.0355 -0.0334 95 VAL A CA
+750 C C . VAL A 95 ? 0.3315 0.3092 0.3580 0.0230 -0.0348 -0.0347 95 VAL A C
+751 O O . VAL A 95 ? 0.2999 0.2779 0.3277 0.0218 -0.0342 -0.0347 95 VAL A O
+752 C CB . VAL A 95 ? 0.3008 0.2788 0.3258 0.0203 -0.0345 -0.0318 95 VAL A CB
+753 C CG1 . VAL A 95 ? 0.2902 0.2668 0.3118 0.0202 -0.0337 -0.0315 95 VAL A CG1
+754 C CG2 . VAL A 95 ? 0.2914 0.2702 0.3162 0.0198 -0.0353 -0.0312 95 VAL A CG2
+755 N N . PRO A 96 ? 0.3325 0.3089 0.3561 0.0250 -0.0348 -0.0357 96 PRO A N
+756 C CA . PRO A 96 ? 0.3345 0.3098 0.3557 0.0255 -0.0344 -0.0372 96 PRO A CA
+757 C C . PRO A 96 ? 0.3953 0.3701 0.4142 0.0230 -0.0337 -0.0355 96 PRO A C
+758 O O . PRO A 96 ? 0.3645 0.3391 0.3828 0.0218 -0.0332 -0.0337 96 PRO A O
+759 C CB . PRO A 96 ? 0.3513 0.3247 0.3688 0.0284 -0.0342 -0.0383 96 PRO A CB
+760 C CG . PRO A 96 ? 0.4023 0.3764 0.4215 0.0300 -0.0348 -0.0376 96 PRO A CG
+761 C CD . PRO A 96 ? 0.3412 0.3168 0.3628 0.0270 -0.0350 -0.0354 96 PRO A CD
+762 N N . ASP A 97 ? 0.3894 0.3643 0.4074 0.0226 -0.0339 -0.0363 97 ASP A N
+763 C CA . ASP A 97 ? 0.3972 0.3724 0.4135 0.0211 -0.0339 -0.0349 97 ASP A CA
+764 C C . ASP A 97 ? 0.4101 0.3840 0.4235 0.0209 -0.0335 -0.0338 97 ASP A C
+765 O O . ASP A 97 ? 0.4037 0.3785 0.4179 0.0199 -0.0334 -0.0323 97 ASP A O
+766 C CB . ASP A 97 ? 0.4386 0.4141 0.4530 0.0213 -0.0347 -0.0364 97 ASP A CB
+767 C CG . ASP A 97 ? 0.7538 0.7308 0.7719 0.0211 -0.0347 -0.0375 97 ASP A CG
+768 O OD1 . ASP A 97 ? 0.7959 0.7741 0.8176 0.0201 -0.0340 -0.0356 97 ASP A OD1
+769 O OD2 . ASP A 97 ? 0.8904 0.8671 0.9077 0.0222 -0.0352 -0.0404 97 ASP A OD2
+770 N N . SER A 98 ? 0.3472 0.3190 0.3575 0.0223 -0.0331 -0.0347 98 SER A N
+771 C CA . SER A 98 ? 0.3493 0.3193 0.3571 0.0223 -0.0322 -0.0338 98 SER A CA
+772 C C . SER A 98 ? 0.4013 0.3715 0.4115 0.0213 -0.0312 -0.0323 98 SER A C
+773 O O . SER A 98 ? 0.4203 0.3898 0.4302 0.0207 -0.0305 -0.0316 98 SER A O
+774 C CB . SER A 98 ? 0.3777 0.3449 0.3814 0.0247 -0.0314 -0.0352 98 SER A CB
+775 O OG . SER A 98 ? 0.4864 0.4536 0.4916 0.0266 -0.0311 -0.0356 98 SER A OG
+776 N N . GLU A 99 ? 0.3458 0.3171 0.3584 0.0214 -0.0314 -0.0321 99 GLU A N
+777 C CA . GLU A 99 ? 0.3272 0.2987 0.3411 0.0207 -0.0309 -0.0312 99 GLU A CA
+778 C C . GLU A 99 ? 0.3330 0.3063 0.3492 0.0191 -0.0312 -0.0308 99 GLU A C
+779 O O . GLU A 99 ? 0.3067 0.2802 0.3233 0.0185 -0.0309 -0.0307 99 GLU A O
+780 C CB . GLU A 99 ? 0.3450 0.3164 0.3591 0.0223 -0.0313 -0.0313 99 GLU A CB
+781 C CG . GLU A 99 ? 0.4515 0.4209 0.4631 0.0250 -0.0307 -0.0319 99 GLU A CG
+782 C CD . GLU A 99 ? 0.7924 0.7591 0.8011 0.0252 -0.0289 -0.0314 99 GLU A CD
+783 O OE1 . GLU A 99 ? 0.7190 0.6841 0.7249 0.0260 -0.0285 -0.0322 99 GLU A OE1
+784 O OE2 . GLU A 99 ? 0.6922 0.6582 0.7012 0.0246 -0.0277 -0.0302 99 GLU A OE2
+785 N N . LEU A 100 ? 0.3217 0.2961 0.3387 0.0189 -0.0318 -0.0309 100 LEU A N
+786 C CA . LEU A 100 ? 0.3276 0.3035 0.3464 0.0184 -0.0317 -0.0305 100 LEU A CA
+787 C C . LEU A 100 ? 0.3510 0.3275 0.3700 0.0186 -0.0315 -0.0305 100 LEU A C
+788 O O . LEU A 100 ? 0.3471 0.3237 0.3656 0.0189 -0.0320 -0.0304 100 LEU A O
+789 C CB . LEU A 100 ? 0.3351 0.3120 0.3552 0.0186 -0.0321 -0.0303 100 LEU A CB
+790 C CG . LEU A 100 ? 0.4116 0.3891 0.4336 0.0185 -0.0319 -0.0301 100 LEU A CG
+791 C CD1 . LEU A 100 ? 0.4300 0.4083 0.4534 0.0188 -0.0313 -0.0294 100 LEU A CD1
+792 C CD2 . LEU A 100 ? 0.4170 0.3944 0.4385 0.0182 -0.0317 -0.0301 100 LEU A CD2
+793 N N . ILE A 101 ? 0.2879 0.2648 0.3077 0.0188 -0.0310 -0.0311 101 ILE A N
+794 C CA . ILE A 101 ? 0.2889 0.2667 0.3100 0.0196 -0.0309 -0.0319 101 ILE A CA
+795 C C . ILE A 101 ? 0.3442 0.3235 0.3663 0.0214 -0.0309 -0.0324 101 ILE A C
+796 O O . ILE A 101 ? 0.3464 0.3254 0.3678 0.0216 -0.0303 -0.0334 101 ILE A O
+797 C CB . ILE A 101 ? 0.3327 0.3094 0.3543 0.0190 -0.0300 -0.0330 101 ILE A CB
+798 C CG1 . ILE A 101 ? 0.3538 0.3284 0.3738 0.0180 -0.0296 -0.0322 101 ILE A CG1
+799 C CG2 . ILE A 101 ? 0.2961 0.2740 0.3205 0.0202 -0.0300 -0.0344 101 ILE A CG2
+800 C CD1 . ILE A 101 ? 0.5448 0.5180 0.5648 0.0173 -0.0283 -0.0327 101 ILE A CD1
+801 N N . PRO A 102 ? 0.3118 0.2928 0.3351 0.0231 -0.0316 -0.0318 102 PRO A N
+802 C CA . PRO A 102 ? 0.3127 0.2950 0.3367 0.0259 -0.0313 -0.0323 102 PRO A CA
+803 C C . PRO A 102 ? 0.3852 0.3678 0.4100 0.0275 -0.0307 -0.0349 102 PRO A C
+804 O O . PRO A 102 ? 0.3905 0.3733 0.4171 0.0271 -0.0310 -0.0363 102 PRO A O
+805 C CB . PRO A 102 ? 0.3283 0.3129 0.3539 0.0279 -0.0327 -0.0312 102 PRO A CB
+806 C CG . PRO A 102 ? 0.3896 0.3736 0.4140 0.0255 -0.0336 -0.0300 102 PRO A CG
+807 C CD . PRO A 102 ? 0.3368 0.3186 0.3602 0.0231 -0.0329 -0.0308 102 PRO A CD
+808 N N . LEU A 103 ? 0.3486 0.3310 0.3721 0.0294 -0.0298 -0.0360 103 LEU A N
+809 C CA . LEU A 103 ? 0.3587 0.3412 0.3823 0.0313 -0.0292 -0.0394 103 LEU A CA
+810 C C . LEU A 103 ? 0.4112 0.3957 0.4368 0.0364 -0.0294 -0.0412 103 LEU A C
+811 O O . LEU A 103 ? 0.4131 0.3977 0.4371 0.0395 -0.0286 -0.0407 103 LEU A O
+812 C CB . LEU A 103 ? 0.3633 0.3439 0.3830 0.0302 -0.0283 -0.0406 103 LEU A CB
+813 C CG . LEU A 103 ? 0.4275 0.4080 0.4463 0.0322 -0.0278 -0.0449 103 LEU A CG
+814 C CD1 . LEU A 103 ? 0.4438 0.4238 0.4636 0.0291 -0.0281 -0.0463 103 LEU A CD1
+815 C CD2 . LEU A 103 ? 0.4529 0.4319 0.4668 0.0332 -0.0270 -0.0461 103 LEU A CD2
+816 N N . PRO A 104 ? 0.3722 0.3586 0.4017 0.0379 -0.0302 -0.0435 104 PRO A N
+817 C CA . PRO A 104 ? 0.3695 0.3586 0.4019 0.0438 -0.0308 -0.0457 104 PRO A CA
+818 C C . PRO A 104 ? 0.4195 0.4079 0.4500 0.0472 -0.0294 -0.0501 104 PRO A C
+819 O O . PRO A 104 ? 0.3985 0.3853 0.4279 0.0449 -0.0287 -0.0528 104 PRO A O
+820 C CB . PRO A 104 ? 0.3897 0.3810 0.4277 0.0438 -0.0323 -0.0469 104 PRO A CB
+821 C CG . PRO A 104 ? 0.4474 0.4364 0.4843 0.0378 -0.0321 -0.0447 104 PRO A CG
+822 C CD . PRO A 104 ? 0.3894 0.3755 0.4214 0.0348 -0.0306 -0.0441 104 PRO A CD
+823 N N . LEU A 105 ? 0.3836 0.3715 0.4345 -0.0101 -0.0823 -0.0112 105 LEU A N
+824 C CA . LEU A 105 ? 0.3842 0.3737 0.4334 -0.0089 -0.0813 -0.0114 105 LEU A CA
+825 C C . LEU A 105 ? 0.4801 0.4712 0.5302 -0.0084 -0.0816 -0.0122 105 LEU A C
+826 O O . LEU A 105 ? 0.4842 0.4753 0.5355 -0.0082 -0.0818 -0.0131 105 LEU A O
+827 C CB . LEU A 105 ? 0.3793 0.3684 0.4273 -0.0079 -0.0805 -0.0112 105 LEU A CB
+828 C CG . LEU A 105 ? 0.4407 0.4277 0.4874 -0.0080 -0.0806 -0.0104 105 LEU A CG
+829 C CD1 . LEU A 105 ? 0.4447 0.4319 0.4912 -0.0070 -0.0805 -0.0099 105 LEU A CD1
+830 C CD2 . LEU A 105 ? 0.4646 0.4517 0.5095 -0.0080 -0.0804 -0.0105 105 LEU A CD2
+831 N N . ASP A 106 ? 0.4589 0.4512 0.5086 -0.0083 -0.0817 -0.0120 106 ASP A N
+832 C CA . ASP A 106 ? 0.4735 0.4667 0.5236 -0.0078 -0.0823 -0.0124 106 ASP A CA
+833 C C . ASP A 106 ? 0.5488 0.5423 0.5973 -0.0070 -0.0812 -0.0123 106 ASP A C
+834 O O . ASP A 106 ? 0.5448 0.5387 0.5930 -0.0069 -0.0808 -0.0116 106 ASP A O
+835 C CB . ASP A 106 ? 0.5022 0.4965 0.5536 -0.0083 -0.0834 -0.0115 106 ASP A CB
+836 C CG . ASP A 106 ? 0.6932 0.6878 0.7450 -0.0078 -0.0845 -0.0114 106 ASP A CG
+837 O OD1 . ASP A 106 ? 0.7819 0.7757 0.8332 -0.0072 -0.0849 -0.0125 106 ASP A OD1
+838 O OD2 . ASP A 106 ? 0.7027 0.6982 0.7551 -0.0079 -0.0848 -0.0101 106 ASP A OD2
+839 N N . LEU A 107 ? 0.5399 0.5333 0.5876 -0.0065 -0.0808 -0.0130 107 LEU A N
+840 C CA . LEU A 107 ? 0.5659 0.5598 0.6124 -0.0062 -0.0802 -0.0127 107 LEU A CA
+841 C C . LEU A 107 ? 0.6657 0.6595 0.7118 -0.0063 -0.0808 -0.0124 107 LEU A C
+842 O O . LEU A 107 ? 0.6566 0.6507 0.7023 -0.0065 -0.0807 -0.0119 107 LEU A O
+843 C CB . LEU A 107 ? 0.5710 0.5653 0.6166 -0.0060 -0.0796 -0.0132 107 LEU A CB
+844 C CG . LEU A 107 ? 0.6374 0.6316 0.6838 -0.0059 -0.0791 -0.0129 107 LEU A CG
+845 C CD1 . LEU A 107 ? 0.6502 0.6457 0.6960 -0.0056 -0.0783 -0.0128 107 LEU A CD1
+846 C CD2 . LEU A 107 ? 0.6383 0.6317 0.6849 -0.0060 -0.0792 -0.0118 107 LEU A CD2
+847 N N . LYS A 108 ? 0.6538 0.6474 0.7009 -0.0064 -0.0819 -0.0124 108 LYS A N
+848 C CA . LYS A 108 ? 0.6632 0.6563 0.7105 -0.0065 -0.0829 -0.0116 108 LYS A CA
+849 C C . LYS A 108 ? 0.7195 0.7134 0.7681 -0.0066 -0.0823 -0.0104 108 LYS A C
+850 O O . LYS A 108 ? 0.7219 0.7153 0.7710 -0.0068 -0.0826 -0.0096 108 LYS A O
+851 C CB . LYS A 108 ? 0.6951 0.6878 0.7435 -0.0064 -0.0847 -0.0116 108 LYS A CB
+852 N N . LYS A 109 ? 0.6605 0.6552 0.7096 -0.0066 -0.0814 -0.0104 109 LYS A N
+853 C CA . LYS A 109 ? 0.6538 0.6492 0.7037 -0.0065 -0.0805 -0.0098 109 LYS A CA
+854 C C . LYS A 109 ? 0.6953 0.6904 0.7446 -0.0062 -0.0798 -0.0102 109 LYS A C
+855 O O . LYS A 109 ? 0.6774 0.6721 0.7256 -0.0061 -0.0796 -0.0108 109 LYS A O
+856 C CB . LYS A 109 ? 0.6831 0.6793 0.7330 -0.0066 -0.0799 -0.0097 109 LYS A CB
+857 C CG . LYS A 109 ? 0.8172 0.8142 0.8683 -0.0072 -0.0810 -0.0089 109 LYS A CG
+858 C CD . LYS A 109 ? 0.9263 0.9241 0.9770 -0.0079 -0.0805 -0.0086 109 LYS A CD
+859 C CE . LYS A 109 ? 1.0790 1.0775 1.1311 -0.0090 -0.0822 -0.0079 109 LYS A CE
+860 N NZ . LYS A 109 ? 1.1923 1.1911 1.2436 -0.0101 -0.0821 -0.0076 109 LYS A NZ
+861 N N . PRO A 110 ? 0.6425 0.6380 0.6933 -0.0060 -0.0797 -0.0098 110 PRO A N
+862 C CA . PRO A 110 ? 0.6292 0.6245 0.6802 -0.0059 -0.0797 -0.0102 110 PRO A CA
+863 C C . PRO A 110 ? 0.6253 0.6205 0.6756 -0.0052 -0.0791 -0.0109 110 PRO A C
+864 O O . PRO A 110 ? 0.6149 0.6096 0.6650 -0.0050 -0.0797 -0.0111 110 PRO A O
+865 C CB . PRO A 110 ? 0.6574 0.6530 0.7111 -0.0059 -0.0800 -0.0096 110 PRO A CB
+866 C CG . PRO A 110 ? 0.7208 0.7163 0.7753 -0.0063 -0.0803 -0.0086 110 PRO A CG
+867 C CD . PRO A 110 ? 0.6645 0.6605 0.7175 -0.0061 -0.0798 -0.0088 110 PRO A CD
+868 N N . LYS A 111 ? 0.5552 0.5508 0.6050 -0.0049 -0.0781 -0.0110 111 LYS A N
+869 C CA . LYS A 111 ? 0.5451 0.5400 0.5932 -0.0044 -0.0775 -0.0117 111 LYS A CA
+870 C C . LYS A 111 ? 0.5450 0.5383 0.5915 -0.0048 -0.0783 -0.0117 111 LYS A C
+871 O O . LYS A 111 ? 0.5194 0.5115 0.5651 -0.0043 -0.0787 -0.0119 111 LYS A O
+872 C CB . LYS A 111 ? 0.5880 0.5841 0.6357 -0.0047 -0.0766 -0.0113 111 LYS A CB
+873 C CG . LYS A 111 ? 0.8477 0.8439 0.8938 -0.0041 -0.0755 -0.0120 111 LYS A CG
+874 C CD . LYS A 111 ? 1.0195 1.0169 1.0647 -0.0050 -0.0748 -0.0113 111 LYS A CD
+875 C CE . LYS A 111 ? 1.2324 1.2323 1.2781 -0.0044 -0.0731 -0.0113 111 LYS A CE
+876 N NZ . LYS A 111 ? 1.3730 1.3723 1.4154 -0.0041 -0.0721 -0.0123 111 LYS A NZ
+877 N N . HIS A 112 ? 0.4952 0.4887 0.5417 -0.0055 -0.0785 -0.0113 112 HIS A N
+878 C CA . HIS A 112 ? 0.4913 0.4836 0.5371 -0.0058 -0.0790 -0.0113 112 HIS A CA
+879 C C . HIS A 112 ? 0.5142 0.5065 0.5603 -0.0056 -0.0795 -0.0111 112 HIS A C
+880 O O . HIS A 112 ? 0.4893 0.4808 0.5351 -0.0056 -0.0798 -0.0107 112 HIS A O
+881 C CB . HIS A 112 ? 0.5031 0.4956 0.5494 -0.0066 -0.0793 -0.0113 112 HIS A CB
+882 C CG . HIS A 112 ? 0.5473 0.5399 0.5934 -0.0072 -0.0793 -0.0110 112 HIS A CG
+883 N ND1 . HIS A 112 ? 0.5742 0.5669 0.6192 -0.0070 -0.0785 -0.0109 112 HIS A ND1
+884 C CD2 . HIS A 112 ? 0.5706 0.5635 0.6178 -0.0082 -0.0801 -0.0107 112 HIS A CD2
+885 C CE1 . HIS A 112 ? 0.5702 0.5635 0.6152 -0.0080 -0.0787 -0.0105 112 HIS A CE1
+886 N NE2 . HIS A 112 ? 0.5745 0.5679 0.6210 -0.0089 -0.0799 -0.0102 112 HIS A NE2
+887 N N . LYS A 113 ? 0.4809 0.4744 0.5277 -0.0057 -0.0796 -0.0110 113 LYS A N
+888 C CA . LYS A 113 ? 0.4898 0.4840 0.5368 -0.0058 -0.0802 -0.0106 113 LYS A CA
+889 C C . LYS A 113 ? 0.5322 0.5261 0.5798 -0.0055 -0.0811 -0.0101 113 LYS A C
+890 O O . LYS A 113 ? 0.5267 0.5210 0.5745 -0.0056 -0.0818 -0.0093 113 LYS A O
+891 C CB . LYS A 113 ? 0.5279 0.5227 0.5754 -0.0063 -0.0806 -0.0105 113 LYS A CB
+892 C CG . LYS A 113 ? 0.7608 0.7564 0.8075 -0.0070 -0.0810 -0.0101 113 LYS A CG
+893 C CD . LYS A 113 ? 0.9487 0.9442 0.9955 -0.0077 -0.0816 -0.0099 113 LYS A CD
+894 C CE . LYS A 113 ? 1.1448 1.1400 1.1895 -0.0078 -0.0814 -0.0105 113 LYS A CE
+895 N NZ . LYS A 113 ? 1.2628 1.2567 1.3078 -0.0077 -0.0819 -0.0107 113 LYS A NZ
+896 N N . MET A 114 ? 0.5047 0.4980 0.5527 -0.0049 -0.0811 -0.0105 114 MET A N
+897 C CA . MET A 114 ? 0.5179 0.5103 0.5665 -0.0043 -0.0823 -0.0105 114 MET A CA
+898 C C . MET A 114 ? 0.5072 0.4977 0.5543 -0.0040 -0.0825 -0.0102 114 MET A C
+899 O O . MET A 114 ? 0.4837 0.4734 0.5313 -0.0037 -0.0841 -0.0094 114 MET A O
+900 C CB . MET A 114 ? 0.5719 0.5644 0.6214 -0.0036 -0.0819 -0.0115 114 MET A CB
+901 C CG . MET A 114 ? 0.6540 0.6457 0.7044 -0.0027 -0.0834 -0.0119 114 MET A CG
+902 S SD . MET A 114 ? 0.7487 0.7395 0.7979 -0.0013 -0.0820 -0.0137 114 MET A SD
+903 C CE . MET A 114 ? 0.7066 0.6953 0.7519 -0.0017 -0.0813 -0.0134 114 MET A CE
+904 N N . MET A 115 ? 0.4467 0.4362 0.4922 -0.0042 -0.0814 -0.0105 115 MET A N
+905 C CA . MET A 115 ? 0.4283 0.4155 0.4727 -0.0043 -0.0818 -0.0100 115 MET A CA
+906 C C . MET A 115 ? 0.4264 0.4138 0.4719 -0.0046 -0.0825 -0.0087 115 MET A C
+907 O O . MET A 115 ? 0.4229 0.4085 0.4684 -0.0044 -0.0838 -0.0076 115 MET A O
+908 C CB . MET A 115 ? 0.4685 0.4551 0.5117 -0.0051 -0.0808 -0.0104 115 MET A CB
+909 C CG . MET A 115 ? 0.5430 0.5298 0.5849 -0.0048 -0.0800 -0.0113 115 MET A CG
+910 S SD . MET A 115 ? 0.6351 0.6203 0.6752 -0.0060 -0.0798 -0.0111 115 MET A SD
+911 C CE . MET A 115 ? 0.6034 0.5846 0.6408 -0.0055 -0.0810 -0.0111 115 MET A CE
+912 N N . GLN A 116 ? 0.3611 0.3506 0.4073 -0.0051 -0.0817 -0.0088 116 GLN A N
+913 C CA . GLN A 116 ? 0.3582 0.3488 0.4054 -0.0053 -0.0818 -0.0078 116 GLN A CA
+914 C C . GLN A 116 ? 0.4098 0.4008 0.4579 -0.0050 -0.0834 -0.0063 116 GLN A C
+915 O O . GLN A 116 ? 0.4047 0.3949 0.4536 -0.0049 -0.0843 -0.0047 116 GLN A O
+916 C CB . GLN A 116 ? 0.3793 0.3722 0.4264 -0.0056 -0.0807 -0.0085 116 GLN A CB
+917 C CG . GLN A 116 ? 0.7041 0.6985 0.7517 -0.0057 -0.0802 -0.0079 116 GLN A CG
+918 C CD . GLN A 116 ? 1.0561 1.0526 1.1028 -0.0059 -0.0793 -0.0089 116 GLN A CD
+919 O OE1 . GLN A 116 ? 1.0384 1.0360 1.0849 -0.0057 -0.0784 -0.0093 116 GLN A OE1
+920 N NE2 . GLN A 116 ? 0.9954 0.9923 1.0414 -0.0062 -0.0798 -0.0092 116 GLN A NE2
+921 N N . LYS A 117 ? 0.3900 0.3405 0.3703 -0.0195 -0.0212 0.0220 117 LYS A N
+922 C CA . LYS A 117 ? 0.3833 0.3356 0.3657 -0.0191 -0.0204 0.0224 117 LYS A CA
+923 C C . LYS A 117 ? 0.3889 0.3435 0.3754 -0.0169 -0.0195 0.0215 117 LYS A C
+924 O O . LYS A 117 ? 0.3603 0.3150 0.3477 -0.0163 -0.0182 0.0205 117 LYS A O
+925 C CB . LYS A 117 ? 0.4232 0.3774 0.4054 -0.0206 -0.0216 0.0254 117 LYS A CB
+926 C CG . LYS A 117 ? 0.5886 0.5407 0.5663 -0.0236 -0.0224 0.0266 117 LYS A CG
+927 C CD . LYS A 117 ? 0.7122 0.6672 0.6900 -0.0254 -0.0236 0.0305 117 LYS A CD
+928 C CE . LYS A 117 ? 0.8595 0.8128 0.8329 -0.0290 -0.0242 0.0317 117 LYS A CE
+929 N NZ . LYS A 117 ? 0.8761 0.8286 0.8495 -0.0293 -0.0226 0.0300 117 LYS A NZ
+930 N N . GLN A 118 ? 0.3341 0.2907 0.3228 -0.0159 -0.0202 0.0219 118 GLN A N
+931 C CA . GLN A 118 ? 0.3298 0.2883 0.3219 -0.0142 -0.0193 0.0211 118 GLN A CA
+932 C C . GLN A 118 ? 0.3634 0.3212 0.3558 -0.0136 -0.0179 0.0189 118 GLN A C
+933 O O . GLN A 118 ? 0.3513 0.3100 0.3451 -0.0131 -0.0168 0.0183 118 GLN A O
+934 C CB . GLN A 118 ? 0.3411 0.3016 0.3352 -0.0134 -0.0205 0.0219 118 GLN A CB
+935 C CG . GLN A 118 ? 0.4922 0.4541 0.4867 -0.0134 -0.0215 0.0247 118 GLN A CG
+936 C CD . GLN A 118 ? 0.6017 0.5657 0.5983 -0.0123 -0.0229 0.0255 118 GLN A CD
+937 O OE1 . GLN A 118 ? 0.5139 0.4781 0.5106 -0.0124 -0.0240 0.0248 118 GLN A OE1
+938 N NE2 . GLN A 118 ? 0.4877 0.4531 0.4861 -0.0112 -0.0227 0.0272 118 GLN A NE2
+939 N N . LEU A 119 ? 0.3258 0.2822 0.3168 -0.0138 -0.0179 0.0182 119 LEU A N
+940 C CA . LEU A 119 ? 0.3259 0.2818 0.3171 -0.0132 -0.0163 0.0170 119 LEU A CA
+941 C C . LEU A 119 ? 0.3942 0.3481 0.3835 -0.0133 -0.0151 0.0166 119 LEU A C
+942 O O . LEU A 119 ? 0.3962 0.3513 0.3869 -0.0126 -0.0139 0.0162 119 LEU A O
+943 C CB . LEU A 119 ? 0.3235 0.2777 0.3132 -0.0132 -0.0161 0.0168 119 LEU A CB
+944 C CG . LEU A 119 ? 0.3651 0.3200 0.3562 -0.0122 -0.0141 0.0163 119 LEU A CG
+945 C CD1 . LEU A 119 ? 0.3149 0.2744 0.3106 -0.0115 -0.0140 0.0165 119 LEU A CD1
+946 C CD2 . LEU A 119 ? 0.3679 0.3207 0.3573 -0.0121 -0.0136 0.0163 119 LEU A CD2
+947 N N . ILE A 120 ? 0.3552 0.3066 0.3414 -0.0144 -0.0155 0.0168 120 ILE A N
+948 C CA . ILE A 120 ? 0.3706 0.3206 0.3555 -0.0145 -0.0145 0.0164 120 ILE A CA
+949 C C . ILE A 120 ? 0.3986 0.3514 0.3863 -0.0139 -0.0143 0.0164 120 ILE A C
+950 O O . ILE A 120 ? 0.4011 0.3541 0.3891 -0.0132 -0.0133 0.0160 120 ILE A O
+951 C CB . ILE A 120 ? 0.4274 0.3743 0.4084 -0.0160 -0.0148 0.0165 120 ILE A CB
+952 C CG1 . ILE A 120 ? 0.4417 0.3902 0.4235 -0.0169 -0.0154 0.0173 120 ILE A CG1
+953 C CG2 . ILE A 120 ? 0.4545 0.3987 0.4321 -0.0174 -0.0155 0.0169 120 ILE A CG2
+954 C CD1 . ILE A 120 ? 0.5859 0.5328 0.5662 -0.0171 -0.0146 0.0167 120 ILE A CD1
+955 N N . TYR A 121 ? 0.3159 0.2706 0.3054 -0.0141 -0.0151 0.0172 121 TYR A N
+956 C CA . TYR A 121 ? 0.2931 0.2495 0.2845 -0.0137 -0.0146 0.0173 121 TYR A CA
+957 C C . TYR A 121 ? 0.3333 0.2910 0.3263 -0.0130 -0.0139 0.0166 121 TYR A C
+958 O O . TYR A 121 ? 0.3004 0.2584 0.2936 -0.0128 -0.0131 0.0162 121 TYR A O
+959 C CB . TYR A 121 ? 0.2877 0.2453 0.2803 -0.0138 -0.0151 0.0187 121 TYR A CB
+960 C CG . TYR A 121 ? 0.2738 0.2322 0.2678 -0.0133 -0.0140 0.0187 121 TYR A CG
+961 C CD1 . TYR A 121 ? 0.3052 0.2635 0.2990 -0.0135 -0.0132 0.0188 121 TYR A CD1
+962 C CD2 . TYR A 121 ? 0.2636 0.2226 0.2588 -0.0128 -0.0135 0.0186 121 TYR A CD2
+963 C CE1 . TYR A 121 ? 0.3094 0.2680 0.3041 -0.0131 -0.0120 0.0187 121 TYR A CE1
+964 C CE2 . TYR A 121 ? 0.2655 0.2242 0.2608 -0.0126 -0.0122 0.0185 121 TYR A CE2
+965 C CZ . TYR A 121 ? 0.3287 0.2871 0.3238 -0.0127 -0.0114 0.0185 121 TYR A CZ
+966 O OH . TYR A 121 ? 0.3281 0.2858 0.3230 -0.0126 -0.0099 0.0184 121 TYR A OH
+967 N N . MET A 122 ? 0.3168 0.2754 0.3108 -0.0127 -0.0142 0.0166 122 MET A N
+968 C CA . MET A 122 ? 0.3163 0.2767 0.3120 -0.0125 -0.0135 0.0162 122 MET A CA
+969 C C . MET A 122 ? 0.3771 0.3376 0.3722 -0.0123 -0.0124 0.0162 122 MET A C
+970 O O . MET A 122 ? 0.3753 0.3371 0.3709 -0.0126 -0.0118 0.0163 122 MET A O
+971 C CB . MET A 122 ? 0.3344 0.2964 0.3317 -0.0123 -0.0141 0.0164 122 MET A CB
+972 C CG . MET A 122 ? 0.3702 0.3329 0.3686 -0.0122 -0.0151 0.0169 122 MET A CG
+973 S SD . MET A 122 ? 0.4056 0.3709 0.4066 -0.0118 -0.0160 0.0171 122 MET A SD
+974 C CE . MET A 122 ? 0.3851 0.3528 0.3880 -0.0123 -0.0146 0.0166 122 MET A CE
+975 N N . LYS A 123 ? 0.3406 0.2991 0.3340 -0.0120 -0.0122 0.0162 123 LYS A N
+976 C CA . LYS A 123 ? 0.3437 0.3016 0.3361 -0.0114 -0.0109 0.0166 123 LYS A CA
+977 C C . LYS A 123 ? 0.3655 0.3233 0.3573 -0.0115 -0.0108 0.0166 123 LYS A C
+978 O O . LYS A 123 ? 0.3438 0.3031 0.3360 -0.0113 -0.0100 0.0174 123 LYS A O
+979 C CB . LYS A 123 ? 0.3747 0.3294 0.3646 -0.0110 -0.0103 0.0165 123 LYS A CB
+980 C CG . LYS A 123 ? 0.4398 0.3947 0.4303 -0.0107 -0.0097 0.0168 123 LYS A CG
+981 C CD . LYS A 123 ? 0.6073 0.5585 0.5948 -0.0101 -0.0081 0.0171 123 LYS A CD
+982 C CE . LYS A 123 ? 0.7391 0.6902 0.7271 -0.0097 -0.0072 0.0173 123 LYS A CE
+983 N NZ . LYS A 123 ? 0.9606 0.9093 0.9465 -0.0107 -0.0088 0.0165 123 LYS A NZ
+984 N N . SER A 124 ? 0.3297 0.2865 0.3208 -0.0119 -0.0116 0.0161 124 SER A N
+985 C CA . SER A 124 ? 0.3320 0.2889 0.3229 -0.0119 -0.0116 0.0160 124 SER A CA
+986 C C . SER A 124 ? 0.3903 0.3492 0.3824 -0.0123 -0.0114 0.0161 124 SER A C
+987 O O . SER A 124 ? 0.4057 0.3651 0.3976 -0.0123 -0.0113 0.0162 124 SER A O
+988 C CB . SER A 124 ? 0.3946 0.3505 0.3850 -0.0123 -0.0122 0.0157 124 SER A CB
+989 O OG . SER A 124 ? 0.4945 0.4513 0.4861 -0.0128 -0.0126 0.0159 124 SER A OG
+990 N N . ILE A 125 ? 0.3357 0.2955 0.3289 -0.0128 -0.0115 0.0160 125 ILE A N
+991 C CA . ILE A 125 ? 0.3238 0.2846 0.3173 -0.0136 -0.0112 0.0160 125 ILE A CA
+992 C C . ILE A 125 ? 0.3356 0.2985 0.3300 -0.0142 -0.0109 0.0166 125 ILE A C
+993 O O . ILE A 125 ? 0.3557 0.3193 0.3505 -0.0152 -0.0107 0.0165 125 ILE A O
+994 C CB . ILE A 125 ? 0.3716 0.3314 0.3653 -0.0138 -0.0111 0.0157 125 ILE A CB
+995 C CG1 . ILE A 125 ? 0.3716 0.3318 0.3664 -0.0135 -0.0117 0.0159 125 ILE A CG1
+996 C CG2 . ILE A 125 ? 0.3827 0.3415 0.3761 -0.0134 -0.0111 0.0157 125 ILE A CG2
+997 C CD1 . ILE A 125 ? 0.3906 0.3505 0.3857 -0.0137 -0.0112 0.0160 125 ILE A CD1
+998 N N . SER A 126 ? 0.2687 0.2326 0.2636 -0.0137 -0.0106 0.0174 126 SER A N
+999 C CA . SER A 126 ? 0.2727 0.2394 0.2691 -0.0143 -0.0100 0.0184 126 SER A CA
+1000 C C . SER A 126 ? 0.3381 0.3069 0.3342 -0.0159 -0.0097 0.0194 126 SER A C
+1001 O O . SER A 126 ? 0.3380 0.3093 0.3355 -0.0172 -0.0095 0.0199 126 SER A O
+1002 C CB . SER A 126 ? 0.3071 0.2742 0.3039 -0.0132 -0.0091 0.0195 126 SER A CB
+1003 O OG . SER A 126 ? 0.4317 0.3979 0.4269 -0.0125 -0.0087 0.0204 126 SER A OG
+1004 N N . GLU A 127 ? 0.3225 0.2907 0.3168 -0.0162 -0.0097 0.0199 127 GLU A N
+1005 C CA . GLU A 127 ? 0.3239 0.2936 0.3169 -0.0183 -0.0096 0.0210 127 GLU A CA
+1006 C C . GLU A 127 ? 0.3523 0.3207 0.3443 -0.0199 -0.0097 0.0196 127 GLU A C
+1007 O O . GLU A 127 ? 0.3495 0.3195 0.3410 -0.0222 -0.0094 0.0204 127 GLU A O
+1008 C CB . GLU A 127 ? 0.3485 0.3173 0.3396 -0.0180 -0.0099 0.0216 127 GLU A CB
+1009 C CG . GLU A 127 ? 0.5543 0.5252 0.5438 -0.0203 -0.0099 0.0235 127 GLU A CG
+1010 C CD . GLU A 127 ? 1.0405 1.0108 1.0280 -0.0201 -0.0105 0.0243 127 GLU A CD
+1011 O OE1 . GLU A 127 ? 1.0832 1.0522 1.0712 -0.0179 -0.0108 0.0236 127 GLU A OE1
+1012 O OE2 . GLU A 127 ? 1.0204 0.9917 1.0058 -0.0224 -0.0108 0.0257 127 GLU A OE2
+1013 N N . LYS A 128 ? 0.3056 0.2710 0.2973 -0.0189 -0.0098 0.0179 128 LYS A N
+1014 C CA . LYS A 128 ? 0.2971 0.2605 0.2876 -0.0198 -0.0094 0.0168 128 LYS A CA
+1015 C C . LYS A 128 ? 0.3210 0.2859 0.3134 -0.0202 -0.0094 0.0168 128 LYS A C
+1016 O O . LYS A 128 ? 0.3153 0.2801 0.3067 -0.0219 -0.0090 0.0167 128 LYS A O
+1017 C CB . LYS A 128 ? 0.3138 0.2744 0.3041 -0.0183 -0.0093 0.0158 128 LYS A CB
+1018 C CG . LYS A 128 ? 0.3443 0.3025 0.3337 -0.0185 -0.0084 0.0152 128 LYS A CG
+1019 C CD . LYS A 128 ? 0.4936 0.4504 0.4839 -0.0167 -0.0083 0.0151 128 LYS A CD
+1020 C CE . LYS A 128 ? 0.5357 0.4898 0.5249 -0.0165 -0.0070 0.0152 128 LYS A CE
+1021 N NZ . LYS A 128 ? 0.7231 0.6747 0.7100 -0.0170 -0.0056 0.0149 128 LYS A NZ
+1022 N N . ILE A 129 ? 0.2975 0.2638 0.2925 -0.0186 -0.0100 0.0169 129 ILE A N
+1023 C CA . ILE A 129 ? 0.2768 0.2453 0.2742 -0.0186 -0.0102 0.0169 129 ILE A CA
+1024 C C . ILE A 129 ? 0.3414 0.3135 0.3398 -0.0206 -0.0098 0.0180 129 ILE A C
+1025 O O . ILE A 129 ? 0.3413 0.3144 0.3401 -0.0220 -0.0097 0.0179 129 ILE A O
+1026 C CB . ILE A 129 ? 0.2911 0.2601 0.2906 -0.0166 -0.0109 0.0168 129 ILE A CB
+1027 C CG1 . ILE A 129 ? 0.3008 0.2667 0.2993 -0.0153 -0.0114 0.0161 129 ILE A CG1
+1028 C CG2 . ILE A 129 ? 0.2726 0.2446 0.2751 -0.0167 -0.0112 0.0171 129 ILE A CG2
+1029 C CD1 . ILE A 129 ? 0.3676 0.3332 0.3667 -0.0140 -0.0121 0.0162 129 ILE A CD1
+1030 N N . GLU A 130 ? 0.2861 0.2920 0.3628 -0.0087 -0.0157 0.0154 130 GLU A N
+1031 C CA . GLU A 130 ? 0.2867 0.2953 0.3644 -0.0087 -0.0154 0.0153 130 GLU A CA
+1032 C C . GLU A 130 ? 0.2915 0.3017 0.3696 -0.0101 -0.0142 0.0157 130 GLU A C
+1033 O O . GLU A 130 ? 0.2842 0.2950 0.3633 -0.0105 -0.0144 0.0160 130 GLU A O
+1034 C CB . GLU A 130 ? 0.3128 0.3227 0.3900 -0.0074 -0.0152 0.0146 130 GLU A CB
+1035 C CG . GLU A 130 ? 0.6008 0.6093 0.6777 -0.0057 -0.0169 0.0141 130 GLU A CG
+1036 C CD . GLU A 130 ? 0.9752 0.9849 1.0513 -0.0040 -0.0170 0.0133 130 GLU A CD
+1037 O OE1 . GLU A 130 ? 1.0442 1.0563 1.1201 -0.0041 -0.0154 0.0131 130 GLU A OE1
+1038 O OE2 . GLU A 130 ? 0.9197 0.9282 0.9955 -0.0024 -0.0188 0.0128 130 GLU A OE2
+1039 N N . ASN A 131 ? 0.2455 0.2560 0.3229 -0.0107 -0.0134 0.0156 131 ASN A N
+1040 C CA . ASN A 131 ? 0.2597 0.2716 0.3375 -0.0120 -0.0128 0.0160 131 ASN A CA
+1041 C C . ASN A 131 ? 0.2823 0.2931 0.3601 -0.0127 -0.0131 0.0164 131 ASN A C
+1042 O O . ASN A 131 ? 0.2730 0.2847 0.3513 -0.0132 -0.0131 0.0167 131 ASN A O
+1043 C CB . ASN A 131 ? 0.2653 0.2780 0.3425 -0.0125 -0.0121 0.0160 131 ASN A CB
+1044 C CG . ASN A 131 ? 0.4578 0.4727 0.5354 -0.0118 -0.0115 0.0160 131 ASN A CG
+1045 O OD1 . ASN A 131 ? 0.4211 0.4379 0.5000 -0.0123 -0.0113 0.0164 131 ASN A OD1
+1046 N ND2 . ASN A 131 ? 0.2975 0.3123 0.3743 -0.0107 -0.0112 0.0155 131 ASN A ND2
+1047 N N . LYS A 132 ? 0.2409 0.2496 0.3183 -0.0128 -0.0135 0.0164 132 LYS A N
+1048 C CA . LYS A 132 ? 0.2473 0.2552 0.3249 -0.0133 -0.0137 0.0169 132 LYS A CA
+1049 C C . LYS A 132 ? 0.2912 0.2996 0.3697 -0.0129 -0.0139 0.0175 132 LYS A C
+1050 O O . LYS A 132 ? 0.2737 0.2825 0.3523 -0.0131 -0.0138 0.0180 132 LYS A O
+1051 C CB . LYS A 132 ? 0.2820 0.2876 0.3594 -0.0136 -0.0140 0.0169 132 LYS A CB
+1052 C CG . LYS A 132 ? 0.3559 0.3613 0.4333 -0.0143 -0.0139 0.0173 132 LYS A CG
+1053 C CD . LYS A 132 ? 0.4423 0.4457 0.5203 -0.0142 -0.0143 0.0178 132 LYS A CD
+1054 C CE . LYS A 132 ? 0.3898 0.3912 0.4671 -0.0149 -0.0145 0.0171 132 LYS A CE
+1055 N NZ . LYS A 132 ? 0.4498 0.4500 0.5277 -0.0154 -0.0146 0.0175 132 LYS A NZ
+1056 N N . SER A 133 ? 0.2533 0.2616 0.3325 -0.0121 -0.0145 0.0175 133 SER A N
+1057 C CA . SER A 133 ? 0.2416 0.2505 0.3218 -0.0117 -0.0150 0.0181 133 SER A CA
+1058 C C . SER A 133 ? 0.2742 0.2846 0.3543 -0.0119 -0.0145 0.0180 133 SER A C
+1059 O O . SER A 133 ? 0.2704 0.2809 0.3505 -0.0120 -0.0145 0.0185 133 SER A O
+1060 C CB . SER A 133 ? 0.2590 0.2673 0.3398 -0.0109 -0.0161 0.0180 133 SER A CB
+1061 O OG . SER A 133 ? 0.3595 0.3659 0.4406 -0.0106 -0.0168 0.0185 133 SER A OG
+1062 N N . GLU A 134 ? 0.2410 0.2524 0.3209 -0.0120 -0.0142 0.0173 134 GLU A N
+1063 C CA . GLU A 134 ? 0.2473 0.2598 0.3274 -0.0121 -0.0140 0.0172 134 GLU A CA
+1064 C C . GLU A 134 ? 0.2702 0.2825 0.3496 -0.0127 -0.0139 0.0176 134 GLU A C
+1065 O O . GLU A 134 ? 0.2553 0.2676 0.3346 -0.0125 -0.0141 0.0178 134 GLU A O
+1066 C CB . GLU A 134 ? 0.2740 0.2878 0.3543 -0.0121 -0.0136 0.0167 134 GLU A CB
+1067 C CG . GLU A 134 ? 0.4584 0.4733 0.5398 -0.0116 -0.0139 0.0164 134 GLU A CG
+1068 C CD . GLU A 134 ? 0.8823 0.8988 0.9642 -0.0116 -0.0133 0.0163 134 GLU A CD
+1069 O OE1 . GLU A 134 ? 0.8399 0.8570 0.9225 -0.0121 -0.0133 0.0167 134 GLU A OE1
+1070 O OE2 . GLU A 134 ? 0.8379 0.8550 0.9195 -0.0111 -0.0128 0.0160 134 GLU A OE2
+1071 N N . VAL A 135 ? 0.2239 0.2359 0.3026 -0.0132 -0.0137 0.0175 135 VAL A N
+1072 C CA . VAL A 135 ? 0.2330 0.2448 0.3109 -0.0135 -0.0139 0.0177 135 VAL A CA
+1073 C C . VAL A 135 ? 0.2670 0.2780 0.3445 -0.0131 -0.0139 0.0183 135 VAL A C
+1074 O O . VAL A 135 ? 0.2680 0.2790 0.3449 -0.0127 -0.0142 0.0185 135 VAL A O
+1075 C CB . VAL A 135 ? 0.2952 0.3065 0.3726 -0.0142 -0.0139 0.0175 135 VAL A CB
+1076 C CG1 . VAL A 135 ? 0.2857 0.2965 0.3621 -0.0144 -0.0144 0.0175 135 VAL A CG1
+1077 C CG2 . VAL A 135 ? 0.3011 0.3133 0.3787 -0.0147 -0.0138 0.0172 135 VAL A CG2
+1078 N N . VAL A 136 ? 0.2359 0.2464 0.3138 -0.0129 -0.0137 0.0186 136 VAL A N
+1079 C CA . VAL A 136 ? 0.2411 0.2514 0.3190 -0.0125 -0.0136 0.0194 136 VAL A CA
+1080 C C . VAL A 136 ? 0.2969 0.3076 0.3749 -0.0120 -0.0138 0.0198 136 VAL A C
+1081 O O . VAL A 136 ? 0.2919 0.3025 0.3690 -0.0115 -0.0137 0.0203 136 VAL A O
+1082 C CB . VAL A 136 ? 0.2690 0.2785 0.3480 -0.0125 -0.0136 0.0200 136 VAL A CB
+1083 C CG1 . VAL A 136 ? 0.2574 0.2672 0.3370 -0.0121 -0.0135 0.0213 136 VAL A CG1
+1084 C CG2 . VAL A 136 ? 0.2626 0.2710 0.3413 -0.0130 -0.0135 0.0196 136 VAL A CG2
+1085 N N . TYR A 137 ? 0.2420 0.2530 0.3209 -0.0120 -0.0141 0.0194 137 TYR A N
+1086 C CA . TYR A 137 ? 0.2346 0.2457 0.3137 -0.0117 -0.0145 0.0195 137 TYR A CA
+1087 C C . TYR A 137 ? 0.2767 0.2875 0.3547 -0.0115 -0.0146 0.0193 137 TYR A C
+1088 O O . TYR A 137 ? 0.2590 0.2692 0.3361 -0.0110 -0.0147 0.0197 137 TYR A O
+1089 C CB . TYR A 137 ? 0.2472 0.2586 0.3274 -0.0117 -0.0150 0.0188 137 TYR A CB
+1090 C CG . TYR A 137 ? 0.2979 0.3093 0.3786 -0.0115 -0.0157 0.0188 137 TYR A CG
+1091 C CD1 . TYR A 137 ? 0.3203 0.3316 0.4017 -0.0115 -0.0163 0.0194 137 TYR A CD1
+1092 C CD2 . TYR A 137 ? 0.3180 0.3293 0.3987 -0.0116 -0.0159 0.0182 137 TYR A CD2
+1093 C CE1 . TYR A 137 ? 0.3388 0.3499 0.4207 -0.0115 -0.0172 0.0193 137 TYR A CE1
+1094 C CE2 . TYR A 137 ? 0.3294 0.3403 0.4106 -0.0115 -0.0167 0.0179 137 TYR A CE2
+1095 C CZ . TYR A 137 ? 0.4019 0.4126 0.4834 -0.0115 -0.0173 0.0184 137 TYR A CZ
+1096 O OH . TYR A 137 ? 0.4437 0.4540 0.5257 -0.0116 -0.0183 0.0181 137 TYR A OH
+1097 N N . ARG A 138 ? 0.2400 0.2510 0.3180 -0.0118 -0.0147 0.0187 138 ARG A N
+1098 C CA . ARG A 138 ? 0.2466 0.2571 0.3240 -0.0116 -0.0153 0.0186 138 ARG A CA
+1099 C C . ARG A 138 ? 0.3221 0.3319 0.3977 -0.0110 -0.0155 0.0190 138 ARG A C
+1100 O O . ARG A 138 ? 0.3275 0.3361 0.4020 -0.0103 -0.0161 0.0191 138 ARG A O
+1101 C CB . ARG A 138 ? 0.2190 0.2303 0.2973 -0.0121 -0.0155 0.0183 138 ARG A CB
+1102 C CG . ARG A 138 ? 0.2166 0.2288 0.2965 -0.0123 -0.0153 0.0179 138 ARG A CG
+1103 C CD . ARG A 138 ? 0.3313 0.3446 0.4122 -0.0127 -0.0153 0.0179 138 ARG A CD
+1104 N NE . ARG A 138 ? 0.3605 0.3752 0.4427 -0.0127 -0.0148 0.0176 138 ARG A NE
+1105 C CZ . ARG A 138 ? 0.6794 0.6948 0.7630 -0.0126 -0.0149 0.0176 138 ARG A CZ
+1106 N NH1 . ARG A 138 ? 0.6971 0.7117 0.7813 -0.0127 -0.0158 0.0180 138 ARG A NH1
+1107 N NH2 . ARG A 138 ? 0.5682 0.5851 0.6528 -0.0124 -0.0143 0.0173 138 ARG A NH2
+1108 N N . LYS A 139 ? 0.2653 0.2754 0.3405 -0.0113 -0.0151 0.0190 139 LYS A N
+1109 C CA . LYS A 139 ? 0.2828 0.2924 0.3563 -0.0106 -0.0154 0.0192 139 LYS A CA
+1110 C C . LYS A 139 ? 0.3506 0.3598 0.4230 -0.0096 -0.0150 0.0199 139 LYS A C
+1111 O O . LYS A 139 ? 0.3640 0.3725 0.4347 -0.0086 -0.0155 0.0200 139 LYS A O
+1112 C CB . LYS A 139 ? 0.3024 0.3124 0.3760 -0.0113 -0.0151 0.0190 139 LYS A CB
+1113 C CG . LYS A 139 ? 0.3664 0.3766 0.4404 -0.0122 -0.0158 0.0184 139 LYS A CG
+1114 C CD . LYS A 139 ? 0.3490 0.3588 0.4217 -0.0119 -0.0171 0.0182 139 LYS A CD
+1115 C CE . LYS A 139 ? 0.4643 0.4745 0.5377 -0.0129 -0.0181 0.0180 139 LYS A CE
+1116 N NZ . LYS A 139 ? 0.5939 0.6036 0.6662 -0.0126 -0.0199 0.0178 139 LYS A NZ
+1117 N N . ALA A 140 ? 0.3151 0.3249 0.3887 -0.0098 -0.0142 0.0204 140 ALA A N
+1118 C CA . ALA A 140 ? 0.3167 0.3266 0.3897 -0.0090 -0.0137 0.0214 140 ALA A CA
+1119 C C . ALA A 140 ? 0.4083 0.4174 0.4807 -0.0085 -0.0141 0.0215 140 ALA A C
+1120 O O . ALA A 140 ? 0.4013 0.4098 0.4720 -0.0074 -0.0140 0.0220 140 ALA A O
+1121 C CB . ALA A 140 ? 0.3124 0.3232 0.3872 -0.0095 -0.0130 0.0222 140 ALA A CB
+1122 N N . ALA A 141 ? 0.3869 0.3959 0.4608 -0.0092 -0.0146 0.0209 141 ALA A N
+1123 C CA . ALA A 141 ? 0.3888 0.3968 0.4625 -0.0090 -0.0152 0.0208 141 ALA A CA
+1124 C C . ALA A 141 ? 0.4595 0.4659 0.5323 -0.0087 -0.0161 0.0201 141 ALA A C
+1125 O O . ALA A 141 ? 0.4728 0.4776 0.5446 -0.0081 -0.0166 0.0202 141 ALA A O
+1126 C CB . ALA A 141 ? 0.3977 0.4063 0.4735 -0.0099 -0.0154 0.0206 141 ALA A CB
+1127 N N . HIS A 142 ? 0.4125 0.4190 0.4859 -0.0090 -0.0165 0.0196 142 HIS A N
+1128 C CA . HIS A 142 ? 0.4232 0.4281 0.4963 -0.0088 -0.0177 0.0192 142 HIS A CA
+1129 C C . HIS A 142 ? 0.5058 0.5097 0.5771 -0.0079 -0.0186 0.0193 142 HIS A C
+1130 O O . HIS A 142 ? 0.5009 0.5026 0.5709 -0.0069 -0.0198 0.0193 142 HIS A O
+1131 C CB . HIS A 142 ? 0.4374 0.4434 0.5129 -0.0098 -0.0178 0.0187 142 HIS A CB
+1132 C CG . HIS A 142 ? 0.4883 0.4950 0.5655 -0.0104 -0.0175 0.0184 142 HIS A CG
+1133 N ND1 . HIS A 142 ? 0.5154 0.5235 0.5945 -0.0111 -0.0173 0.0179 142 HIS A ND1
+1134 C CD2 . HIS A 142 ? 0.5192 0.5255 0.5963 -0.0103 -0.0175 0.0184 142 HIS A CD2
+1135 C CE1 . HIS A 142 ? 0.5116 0.5200 0.5916 -0.0113 -0.0173 0.0175 142 HIS A CE1
+1136 N NE2 . HIS A 142 ? 0.5160 0.5234 0.5950 -0.0110 -0.0175 0.0178 142 HIS A NE2
+1137 N N . GLU A 143 ? 0.4652 0.4930 0.4530 0.0239 -0.0432 -0.0218 143 GLU A N
+1138 C CA . GLU A 143 ? 0.4672 0.4944 0.4560 0.0242 -0.0438 -0.0198 143 GLU A CA
+1139 C C . GLU A 143 ? 0.5415 0.5660 0.5291 0.0253 -0.0440 -0.0196 143 GLU A C
+1140 O O . GLU A 143 ? 0.5397 0.5624 0.5281 0.0265 -0.0453 -0.0187 143 GLU A O
+1141 C CB . GLU A 143 ? 0.4841 0.5154 0.4736 0.0229 -0.0437 -0.0182 143 GLU A CB
+1142 C CG . GLU A 143 ? 0.6535 0.6854 0.6446 0.0224 -0.0452 -0.0163 143 GLU A CG
+1143 C CD . GLU A 143 ? 0.9299 0.9652 0.9214 0.0206 -0.0456 -0.0148 143 GLU A CD
+1144 O OE1 . GLU A 143 ? 0.8888 0.9233 0.8807 0.0204 -0.0476 -0.0134 143 GLU A OE1
+1145 O OE2 . GLU A 143 ? 0.8758 0.9147 0.8673 0.0195 -0.0443 -0.0151 143 GLU A OE2
+1146 N N . LYS A 144 ? 0.5204 0.5451 0.5065 0.0250 -0.0432 -0.0204 144 LYS A N
+1147 C CA . LYS A 144 ? 0.5248 0.5484 0.5097 0.0256 -0.0432 -0.0203 144 LYS A CA
+1148 C C . LYS A 144 ? 0.5720 0.5972 0.5574 0.0258 -0.0438 -0.0191 144 LYS A C
+1149 O O . LYS A 144 ? 0.5711 0.5955 0.5563 0.0271 -0.0447 -0.0191 144 LYS A O
+1150 C CB . LYS A 144 ? 0.5614 0.5811 0.5457 0.0270 -0.0437 -0.0209 144 LYS A CB
+1151 C CG . LYS A 144 ? 0.7037 0.7215 0.6860 0.0265 -0.0434 -0.0222 144 LYS A CG
+1152 C CD . LYS A 144 ? 0.8268 0.8427 0.8086 0.0257 -0.0439 -0.0240 144 LYS A CD
+1153 C CE . LYS A 144 ? 1.0453 1.0593 1.0284 0.0263 -0.0443 -0.0249 144 LYS A CE
+1154 N NZ . LYS A 144 ? 1.1708 1.1798 1.1540 0.0280 -0.0448 -0.0251 144 LYS A NZ
+1155 N N . ASP A 145 ? 0.5179 0.5455 0.5040 0.0246 -0.0437 -0.0185 145 ASP A N
+1156 C CA . ASP A 145 ? 0.4970 0.5257 0.4834 0.0241 -0.0447 -0.0180 145 ASP A CA
+1157 C C . ASP A 145 ? 0.5306 0.5594 0.5157 0.0244 -0.0442 -0.0188 145 ASP A C
+1158 O O . ASP A 145 ? 0.5267 0.5557 0.5109 0.0240 -0.0426 -0.0191 145 ASP A O
+1159 C CB . ASP A 145 ? 0.5035 0.5342 0.4905 0.0225 -0.0444 -0.0174 145 ASP A CB
+1160 C CG . ASP A 145 ? 0.6027 0.6337 0.5896 0.0216 -0.0457 -0.0172 145 ASP A CG
+1161 O OD1 . ASP A 145 ? 0.6089 0.6394 0.5948 0.0216 -0.0451 -0.0182 145 ASP A OD1
+1162 O OD2 . ASP A 145 ? 0.6273 0.6590 0.6151 0.0206 -0.0476 -0.0162 145 ASP A OD2
+1163 N N . GLY A 146 ? 0.4735 0.5023 0.4584 0.0253 -0.0459 -0.0191 146 GLY A N
+1164 C CA . GLY A 146 ? 0.4579 0.4875 0.4416 0.0257 -0.0458 -0.0201 146 GLY A CA
+1165 C C . GLY A 146 ? 0.4665 0.4964 0.4494 0.0245 -0.0441 -0.0205 146 GLY A C
+1166 O O . GLY A 146 ? 0.4687 0.4991 0.4507 0.0246 -0.0427 -0.0207 146 GLY A O
+1167 N N . TYR A 147 ? 0.4026 0.4322 0.3860 0.0234 -0.0445 -0.0206 147 TYR A N
+1168 C CA . TYR A 147 ? 0.3855 0.4145 0.3684 0.0226 -0.0431 -0.0211 147 TYR A CA
+1169 C C . TYR A 147 ? 0.4199 0.4490 0.4029 0.0227 -0.0411 -0.0202 147 TYR A C
+1170 O O . TYR A 147 ? 0.4237 0.4524 0.4061 0.0229 -0.0401 -0.0204 147 TYR A O
+1171 C CB . TYR A 147 ? 0.3850 0.4130 0.3682 0.0214 -0.0442 -0.0214 147 TYR A CB
+1172 C CG . TYR A 147 ? 0.3797 0.4059 0.3624 0.0210 -0.0429 -0.0221 147 TYR A CG
+1173 C CD1 . TYR A 147 ? 0.3929 0.4175 0.3746 0.0210 -0.0435 -0.0240 147 TYR A CD1
+1174 C CD2 . TYR A 147 ? 0.3791 0.4053 0.3625 0.0210 -0.0412 -0.0211 147 TYR A CD2
+1175 C CE1 . TYR A 147 ? 0.4153 0.4373 0.3967 0.0209 -0.0422 -0.0247 147 TYR A CE1
+1176 C CE2 . TYR A 147 ? 0.3875 0.4115 0.3707 0.0212 -0.0402 -0.0216 147 TYR A CE2
+1177 C CZ . TYR A 147 ? 0.4992 0.5206 0.4814 0.0212 -0.0405 -0.0234 147 TYR A CZ
+1178 O OH . TYR A 147 ? 0.4964 0.5148 0.4787 0.0217 -0.0395 -0.0240 147 TYR A OH
+1179 N N . TYR A 148 ? 0.3584 0.3881 0.3422 0.0226 -0.0409 -0.0194 148 TYR A N
+1180 C CA . TYR A 148 ? 0.3465 0.3768 0.3307 0.0228 -0.0400 -0.0191 148 TYR A CA
+1181 C C . TYR A 148 ? 0.3938 0.4238 0.3771 0.0233 -0.0400 -0.0191 148 TYR A C
+1182 O O . TYR A 148 ? 0.3806 0.4106 0.3637 0.0235 -0.0399 -0.0188 148 TYR A O
+1183 C CB . TYR A 148 ? 0.3526 0.3844 0.3377 0.0226 -0.0402 -0.0188 148 TYR A CB
+1184 C CG . TYR A 148 ? 0.3531 0.3859 0.3390 0.0218 -0.0401 -0.0184 148 TYR A CG
+1185 C CD1 . TYR A 148 ? 0.3679 0.4005 0.3540 0.0207 -0.0412 -0.0181 148 TYR A CD1
+1186 C CD2 . TYR A 148 ? 0.3615 0.3957 0.3480 0.0222 -0.0396 -0.0183 148 TYR A CD2
+1187 C CE1 . TYR A 148 ? 0.3928 0.4263 0.3793 0.0195 -0.0415 -0.0176 148 TYR A CE1
+1188 C CE2 . TYR A 148 ? 0.3798 0.4151 0.3669 0.0214 -0.0394 -0.0179 148 TYR A CE2
+1189 C CZ . TYR A 148 ? 0.5005 0.5353 0.4874 0.0198 -0.0403 -0.0175 148 TYR A CZ
+1190 O OH . TYR A 148 ? 0.5268 0.5627 0.5141 0.0185 -0.0405 -0.0170 148 TYR A OH
+1191 N N . LEU A 149 ? 0.3675 0.3971 0.3504 0.0235 -0.0405 -0.0193 149 LEU A N
+1192 C CA . LEU A 149 ? 0.3882 0.4171 0.3700 0.0236 -0.0406 -0.0193 149 LEU A CA
+1193 C C . LEU A 149 ? 0.4291 0.4587 0.4099 0.0234 -0.0402 -0.0190 149 LEU A C
+1194 O O . LEU A 149 ? 0.4170 0.4465 0.3972 0.0229 -0.0406 -0.0185 149 LEU A O
+1195 C CB . LEU A 149 ? 0.4018 0.4298 0.3833 0.0243 -0.0412 -0.0196 149 LEU A CB
+1196 C CG . LEU A 149 ? 0.4799 0.5058 0.4612 0.0244 -0.0417 -0.0201 149 LEU A CG
+1197 C CD1 . LEU A 149 ? 0.4884 0.5129 0.4696 0.0257 -0.0422 -0.0203 149 LEU A CD1
+1198 C CD2 . LEU A 149 ? 0.5106 0.5357 0.4906 0.0236 -0.0421 -0.0204 149 LEU A CD2
+1199 N N . LYS A 150 ? 0.3900 0.4203 0.3706 0.0236 -0.0399 -0.0193 150 LYS A N
+1200 C CA . LYS A 150 ? 0.3827 0.4142 0.3625 0.0234 -0.0395 -0.0193 150 LYS A CA
+1201 C C . LYS A 150 ? 0.4164 0.4474 0.3966 0.0231 -0.0390 -0.0186 150 LYS A C
+1202 O O . LYS A 150 ? 0.4268 0.4586 0.4064 0.0228 -0.0388 -0.0179 150 LYS A O
+1203 C CB . LYS A 150 ? 0.4038 0.4366 0.3834 0.0240 -0.0399 -0.0206 150 LYS A CB
+1204 C CG . LYS A 150 ? 0.5038 0.5354 0.4839 0.0238 -0.0402 -0.0216 150 LYS A CG
+1205 C CD . LYS A 150 ? 0.5730 0.6059 0.5526 0.0244 -0.0417 -0.0234 150 LYS A CD
+1206 C CE . LYS A 150 ? 0.6486 0.6796 0.6284 0.0238 -0.0423 -0.0248 150 LYS A CE
+1207 N NZ . LYS A 150 ? 0.6735 0.7036 0.6528 0.0235 -0.0409 -0.0253 150 LYS A NZ
+1208 N N . PHE A 151 ? 0.3643 0.3940 0.3456 0.0234 -0.0389 -0.0187 151 PHE A N
+1209 C CA . PHE A 151 ? 0.3522 0.3808 0.3342 0.0238 -0.0387 -0.0181 151 PHE A CA
+1210 C C . PHE A 151 ? 0.3831 0.4119 0.3658 0.0242 -0.0399 -0.0171 151 PHE A C
+1211 O O . PHE A 151 ? 0.3868 0.4149 0.3700 0.0249 -0.0405 -0.0162 151 PHE A O
+1212 C CB . PHE A 151 ? 0.3696 0.3966 0.3524 0.0241 -0.0383 -0.0189 151 PHE A CB
+1213 C CG . PHE A 151 ? 0.3885 0.4140 0.3707 0.0240 -0.0378 -0.0201 151 PHE A CG
+1214 C CD1 . PHE A 151 ? 0.4133 0.4376 0.3955 0.0245 -0.0373 -0.0200 151 PHE A CD1
+1215 C CD2 . PHE A 151 ? 0.4338 0.4591 0.4156 0.0234 -0.0384 -0.0217 151 PHE A CD2
+1216 C CE1 . PHE A 151 ? 0.4547 0.4774 0.4362 0.0243 -0.0370 -0.0217 151 PHE A CE1
+1217 C CE2 . PHE A 151 ? 0.4451 0.4688 0.4261 0.0232 -0.0386 -0.0236 151 PHE A CE2
+1218 C CZ . PHE A 151 ? 0.4274 0.4498 0.4083 0.0237 -0.0378 -0.0238 151 PHE A CZ
+1219 N N . SER A 152 ? 0.3536 0.3830 0.3363 0.0240 -0.0405 -0.0175 152 SER A N
+1220 C CA . SER A 152 ? 0.3716 0.4014 0.3549 0.0245 -0.0423 -0.0172 152 SER A CA
+1221 C C . SER A 152 ? 0.4049 0.4345 0.3871 0.0237 -0.0441 -0.0170 152 SER A C
+1222 O O . SER A 152 ? 0.3759 0.4053 0.3568 0.0227 -0.0435 -0.0170 152 SER A O
+1223 C CB . SER A 152 ? 0.4534 0.4843 0.4376 0.0249 -0.0425 -0.0182 152 SER A CB
+1224 O OG . SER A 152 ? 0.6658 0.6966 0.6494 0.0241 -0.0419 -0.0189 152 SER A OG
+1225 N N . CYS A 153 ? 0.3898 0.4197 0.3725 0.0243 -0.0467 -0.0167 153 CYS A N
+1226 C CA . CYS A 153 ? 0.4080 0.4374 0.3897 0.0234 -0.0497 -0.0167 153 CYS A CA
+1227 C C . CYS A 153 ? 0.4378 0.4663 0.4184 0.0226 -0.0496 -0.0185 153 CYS A C
+1228 O O . CYS A 153 ? 0.4270 0.4561 0.4084 0.0232 -0.0483 -0.0196 153 CYS A O
+1229 C CB . CYS A 153 ? 0.4275 0.4575 0.4103 0.0247 -0.0535 -0.0167 153 CYS A CB
+1230 S SG . CYS A 153 ? 0.4907 0.5206 0.4750 0.0262 -0.0547 -0.0142 153 CYS A SG
+1231 N N . ASP A 154 ? 0.3847 0.4117 0.3636 0.0211 -0.0513 -0.0187 154 ASP A N
+1232 C CA . ASP A 154 ? 0.3611 0.3861 0.3389 0.0205 -0.0515 -0.0207 154 ASP A CA
+1233 C C . ASP A 154 ? 0.3769 0.4020 0.3552 0.0210 -0.0550 -0.0226 154 ASP A C
+1234 O O . ASP A 154 ? 0.3741 0.3979 0.3513 0.0200 -0.0589 -0.0232 154 ASP A O
+1235 C CB . ASP A 154 ? 0.3823 0.4053 0.3580 0.0188 -0.0521 -0.0203 154 ASP A CB
+1236 C CG . ASP A 154 ? 0.5096 0.5292 0.4841 0.0185 -0.0522 -0.0224 154 ASP A CG
+1237 O OD1 . ASP A 154 ? 0.5138 0.5326 0.4891 0.0193 -0.0526 -0.0244 154 ASP A OD1
+1238 O OD2 . ASP A 154 ? 0.5509 0.5687 0.5237 0.0174 -0.0521 -0.0221 154 ASP A OD2
+1239 N N . PHE A 155 ? 0.3009 0.3281 0.2809 0.0224 -0.0542 -0.0236 155 PHE A N
+1240 C CA . PHE A 155 ? 0.2831 0.3119 0.2638 0.0234 -0.0574 -0.0257 155 PHE A CA
+1241 C C . PHE A 155 ? 0.3594 0.3859 0.3387 0.0225 -0.0608 -0.0287 155 PHE A C
+1242 O O . PHE A 155 ? 0.3622 0.3894 0.3414 0.0228 -0.0655 -0.0301 155 PHE A O
+1243 C CB . PHE A 155 ? 0.2918 0.3240 0.2744 0.0248 -0.0552 -0.0262 155 PHE A CB
+1244 C CG . PHE A 155 ? 0.2903 0.3244 0.2743 0.0258 -0.0527 -0.0239 155 PHE A CG
+1245 C CD1 . PHE A 155 ? 0.2913 0.3261 0.2761 0.0270 -0.0546 -0.0226 155 PHE A CD1
+1246 C CD2 . PHE A 155 ? 0.3036 0.3382 0.2882 0.0256 -0.0491 -0.0231 155 PHE A CD2
+1247 C CE1 . PHE A 155 ? 0.2972 0.3326 0.2832 0.0280 -0.0523 -0.0208 155 PHE A CE1
+1248 C CE2 . PHE A 155 ? 0.3426 0.3780 0.3281 0.0262 -0.0473 -0.0214 155 PHE A CE2
+1249 C CZ . PHE A 155 ? 0.3020 0.3375 0.2882 0.0275 -0.0487 -0.0204 155 PHE A CZ
+1250 N N . LYS A 156 ? 0.3733 0.3545 0.3395 0.0182 -0.1303 0.0163 156 LYS A N
+1251 C CA . LYS A 156 ? 0.3679 0.3487 0.3319 0.0199 -0.1284 0.0186 156 LYS A CA
+1252 C C . LYS A 156 ? 0.4104 0.3900 0.3744 0.0218 -0.1235 0.0181 156 LYS A C
+1253 O O . LYS A 156 ? 0.3964 0.3765 0.3607 0.0219 -0.1208 0.0194 156 LYS A O
+1254 C CB . LYS A 156 ? 0.4046 0.3836 0.3649 0.0210 -0.1332 0.0206 156 LYS A CB
+1255 C CG . LYS A 156 ? 0.5698 0.5510 0.5296 0.0191 -0.1364 0.0236 156 LYS A CG
+1256 C CD . LYS A 156 ? 0.6253 0.6100 0.5872 0.0158 -0.1401 0.0230 156 LYS A CD
+1257 C CE . LYS A 156 ? 0.6670 0.6542 0.6270 0.0143 -0.1452 0.0268 156 LYS A CE
+1258 N NZ . LYS A 156 ? 0.6958 0.6868 0.6573 0.0136 -0.1416 0.0286 156 LYS A NZ
+1259 N N . LEU A 157 ? 0.3920 0.3709 0.3559 0.0232 -0.1227 0.0163 157 LEU A N
+1260 C CA . LEU A 157 ? 0.4029 0.3820 0.3670 0.0245 -0.1186 0.0160 157 LEU A CA
+1261 C C . LEU A 157 ? 0.4370 0.4175 0.4040 0.0231 -0.1156 0.0161 157 LEU A C
+1262 O O . LEU A 157 ? 0.4223 0.4030 0.3893 0.0233 -0.1133 0.0171 157 LEU A O
+1263 C CB . LEU A 157 ? 0.4132 0.3925 0.3769 0.0262 -0.1188 0.0140 157 LEU A CB
+1264 C CG . LEU A 157 ? 0.4844 0.4657 0.4489 0.0270 -0.1149 0.0137 157 LEU A CG
+1265 C CD1 . LEU A 157 ? 0.4844 0.4652 0.4464 0.0279 -0.1137 0.0148 157 LEU A CD1
+1266 C CD2 . LEU A 157 ? 0.5084 0.4911 0.4737 0.0284 -0.1150 0.0117 157 LEU A CD2
+1267 N N . LEU A 158 ? 0.3802 0.3608 0.3492 0.0215 -0.1163 0.0153 158 LEU A N
+1268 C CA . LEU A 158 ? 0.3791 0.3596 0.3501 0.0203 -0.1141 0.0157 158 LEU A CA
+1269 C C . LEU A 158 ? 0.3902 0.3714 0.3609 0.0199 -0.1134 0.0168 158 LEU A C
+1270 O O . LEU A 158 ? 0.3710 0.3520 0.3421 0.0203 -0.1115 0.0174 158 LEU A O
+1271 C CB . LEU A 158 ? 0.3763 0.3557 0.3493 0.0180 -0.1154 0.0148 158 LEU A CB
+1272 C CG . LEU A 158 ? 0.4413 0.4197 0.4156 0.0181 -0.1156 0.0137 158 LEU A CG
+1273 C CD1 . LEU A 158 ? 0.4271 0.4034 0.4038 0.0149 -0.1175 0.0129 158 LEU A CD1
+1274 C CD2 . LEU A 158 ? 0.4893 0.4675 0.4640 0.0192 -0.1125 0.0150 158 LEU A CD2
+1275 N N . GLU A 159 ? 0.3450 0.3272 0.3150 0.0194 -0.1156 0.0173 159 GLU A N
+1276 C CA . GLU A 159 ? 0.3536 0.3373 0.3235 0.0193 -0.1150 0.0185 159 GLU A CA
+1277 C C . GLU A 159 ? 0.4315 0.4145 0.4007 0.0209 -0.1134 0.0193 159 GLU A C
+1278 O O . GLU A 159 ? 0.4255 0.4090 0.3956 0.0211 -0.1118 0.0194 159 GLU A O
+1279 C CB . GLU A 159 ? 0.3685 0.3541 0.3376 0.0183 -0.1183 0.0196 159 GLU A CB
+1280 C CG . GLU A 159 ? 0.4359 0.4234 0.4063 0.0156 -0.1203 0.0190 159 GLU A CG
+1281 C CD . GLU A 159 ? 0.4770 0.4674 0.4466 0.0140 -0.1247 0.0205 159 GLU A CD
+1282 O OE1 . GLU A 159 ? 0.4443 0.4368 0.4151 0.0110 -0.1271 0.0200 159 GLU A OE1
+1283 O OE2 . GLU A 159 ? 0.4749 0.4653 0.4425 0.0153 -0.1261 0.0226 159 GLU A OE2
+1284 N N . ALA A 160 ? 0.4106 0.3920 0.3782 0.0218 -0.1139 0.0197 160 ALA A N
+1285 C CA . ALA A 160 ? 0.4309 0.4110 0.3978 0.0224 -0.1127 0.0205 160 ALA A CA
+1286 C C . ALA A 160 ? 0.4844 0.4650 0.4526 0.0224 -0.1108 0.0198 160 ALA A C
+1287 O O . ALA A 160 ? 0.4786 0.4591 0.4477 0.0221 -0.1103 0.0202 160 ALA A O
+1288 C CB . ALA A 160 ? 0.4472 0.4252 0.4116 0.0232 -0.1138 0.0209 160 ALA A CB
+1289 N N . LYS A 161 ? 0.4358 0.4170 0.4045 0.0225 -0.1103 0.0189 161 LYS A N
+1290 C CA . LYS A 161 ? 0.4356 0.4174 0.4052 0.0224 -0.1093 0.0191 161 LYS A CA
+1291 C C . LYS A 161 ? 0.4915 0.4729 0.4621 0.0221 -0.1092 0.0193 161 LYS A C
+1292 O O . LYS A 161 ? 0.4767 0.4581 0.4477 0.0221 -0.1094 0.0200 161 LYS A O
+1293 C CB . LYS A 161 ? 0.4634 0.4462 0.4327 0.0228 -0.1088 0.0189 161 LYS A CB
+1294 C CG . LYS A 161 ? 0.6270 0.6110 0.5951 0.0231 -0.1085 0.0191 161 LYS A CG
+1295 C CD . LYS A 161 ? 0.7206 0.7035 0.6867 0.0240 -0.1091 0.0184 161 LYS A CD
+1296 C CE . LYS A 161 ? 0.9084 0.8921 0.8730 0.0240 -0.1086 0.0187 161 LYS A CE
+1297 N NZ . LYS A 161 ? 1.0854 1.0670 1.0497 0.0225 -0.1090 0.0198 161 LYS A NZ
+1298 N N . ALA A 162 ? 0.4420 0.4231 0.4130 0.0217 -0.1094 0.0188 162 ALA A N
+1299 C CA . ALA A 162 ? 0.4314 0.4120 0.4030 0.0216 -0.1092 0.0188 162 ALA A CA
+1300 C C . ALA A 162 ? 0.4767 0.4581 0.4485 0.0224 -0.1094 0.0187 162 ALA A C
+1301 O O . ALA A 162 ? 0.4689 0.4493 0.4407 0.0231 -0.1098 0.0188 162 ALA A O
+1302 C CB . ALA A 162 ? 0.4344 0.4153 0.4064 0.0204 -0.1096 0.0181 162 ALA A CB
+1303 N N . THR A 163 ? 0.4422 0.4248 0.4141 0.0225 -0.1095 0.0188 163 THR A N
+1304 C CA . THR A 163 ? 0.4399 0.4231 0.4128 0.0231 -0.1097 0.0188 163 THR A CA
+1305 C C . THR A 163 ? 0.5068 0.4886 0.4801 0.0229 -0.1106 0.0189 163 THR A C
+1306 O O . THR A 163 ? 0.5099 0.4916 0.4841 0.0234 -0.1116 0.0184 163 THR A O
+1307 C CB . THR A 163 ? 0.5104 0.4949 0.4834 0.0229 -0.1099 0.0196 163 THR A CB
+1308 O OG1 . THR A 163 ? 0.5207 0.5039 0.4944 0.0228 -0.1102 0.0202 163 THR A OG1
+1309 C CG2 . THR A 163 ? 0.3831 0.3675 0.3546 0.0222 -0.1106 0.0205 163 THR A CG2
+1310 N N . LEU A 164 ? 0.4828 0.4640 0.4552 0.0221 -0.1106 0.0195 164 LEU A N
+1311 C CA . LEU A 164 ? 0.4930 0.4740 0.4657 0.0211 -0.1117 0.0200 164 LEU A CA
+1312 C C . LEU A 164 ? 0.5179 0.4991 0.4907 0.0214 -0.1132 0.0203 164 LEU A C
+1313 O O . LEU A 164 ? 0.5123 0.4934 0.4857 0.0206 -0.1156 0.0205 164 LEU A O
+1314 C CB . LEU A 164 ? 0.5046 0.4861 0.4760 0.0206 -0.1110 0.0205 164 LEU A CB
+1315 C CG . LEU A 164 ? 0.5842 0.5646 0.5550 0.0195 -0.1110 0.0209 164 LEU A CG
+1316 C CD1 . LEU A 164 ? 0.6471 0.6255 0.6178 0.0197 -0.1109 0.0212 164 LEU A CD1
+1317 C CD2 . LEU A 164 ? 0.5701 0.5514 0.5392 0.0197 -0.1103 0.0210 164 LEU A CD2
+1318 N N . TYR A 165 ? 0.4636 0.4444 0.4355 0.0221 -0.1124 0.0206 165 TYR A N
+1319 C CA . TYR A 165 ? 0.4662 0.4458 0.4375 0.0225 -0.1140 0.0217 165 TYR A CA
+1320 C C . TYR A 165 ? 0.5855 0.5639 0.5570 0.0236 -0.1155 0.0208 165 TYR A C
+1321 O O . TYR A 165 ? 0.5857 0.5635 0.5570 0.0237 -0.1186 0.0214 165 TYR A O
+1322 C CB . TYR A 165 ? 0.4596 0.4377 0.4301 0.0227 -0.1126 0.0224 165 TYR A CB
+1323 C CG . TYR A 165 ? 0.4548 0.4307 0.4241 0.0228 -0.1144 0.0248 165 TYR A CG
+1324 C CD1 . TYR A 165 ? 0.4623 0.4349 0.4304 0.0237 -0.1158 0.0251 165 TYR A CD1
+1325 C CD2 . TYR A 165 ? 0.4658 0.4429 0.4349 0.0221 -0.1151 0.0269 165 TYR A CD2
+1326 C CE1 . TYR A 165 ? 0.4728 0.4421 0.4391 0.0238 -0.1182 0.0281 165 TYR A CE1
+1327 C CE2 . TYR A 165 ? 0.4679 0.4428 0.4356 0.0220 -0.1173 0.0301 165 TYR A CE2
+1328 C CZ . TYR A 165 ? 0.5497 0.5201 0.5158 0.0229 -0.1191 0.0309 165 TYR A CZ
+1329 O OH . TYR A 165 ? 0.5789 0.5461 0.5430 0.0229 -0.1219 0.0346 165 TYR A OH
+1330 N N . SER A 166 ? 0.5947 0.5732 0.5665 0.0245 -0.1138 0.0193 166 SER A N
+1331 C CA . SER A 166 ? 0.6136 0.5920 0.5856 0.0261 -0.1146 0.0180 166 SER A CA
+1332 C C . SER A 166 ? 0.6899 0.6690 0.6635 0.0262 -0.1169 0.0171 166 SER A C
+1333 O O . SER A 166 ? 0.6858 0.6638 0.6592 0.0275 -0.1196 0.0164 166 SER A O
+1336 N N . LYS A 167 ? 0.6718 0.6519 0.6467 0.0246 -0.1163 0.0173 167 LYS A N
+1337 C CA . LYS A 167 ? 0.6815 0.6614 0.6585 0.0237 -0.1185 0.0167 167 LYS A CA
+1338 C C . LYS A 167 ? 0.7492 0.7284 0.7264 0.0220 -0.1225 0.0174 167 LYS A C
+1339 O O . LYS A 167 ? 0.7557 0.7344 0.7349 0.0207 -0.1254 0.0166 167 LYS A O
+1340 C CB . LYS A 167 ? 0.7128 0.6928 0.6908 0.0221 -0.1166 0.0173 167 LYS A CB
+1341 C CG . LYS A 167 ? 0.8857 0.8669 0.8644 0.0232 -0.1146 0.0170 167 LYS A CG
+1342 C CD . LYS A 167 ? 0.9857 0.9653 0.9658 0.0215 -0.1146 0.0180 167 LYS A CD
+1343 C CE . LYS A 167 ? 1.1448 1.1246 1.1236 0.0215 -0.1126 0.0198 167 LYS A CE
+1344 N NZ . LYS A 167 ? 1.2310 1.2075 1.2090 0.0193 -0.1129 0.0214 167 LYS A NZ
+1345 N N . LYS A 168 ? 0.7016 0.6808 0.6768 0.0217 -0.1232 0.0192 168 LYS A N
+1346 C CA . LYS A 168 ? 0.9209 0.9006 0.8960 0.0198 -0.1275 0.0207 168 LYS A CA
+1347 C C . LYS A 168 ? 1.4092 1.3879 1.3852 0.0197 -0.1333 0.0200 168 LYS A C
+1348 O O . LYS A 168 ? 0.9541 0.9310 0.9293 0.0223 -0.1345 0.0190 168 LYS A O
+1349 C CB . LYS A 168 ? 0.9404 0.9205 0.9132 0.0200 -0.1275 0.0233 168 LYS A CB
+1350 C CG . LYS A 168 ? 0.9916 0.9688 0.9622 0.0223 -0.1289 0.0242 168 LYS A CG
+1351 C CD . LYS A 168 ? 1.0519 1.0287 1.0206 0.0222 -0.1278 0.0271 168 LYS A CD
+1352 C CE . LYS A 168 ? 1.1208 1.0933 1.0873 0.0243 -0.1280 0.0277 168 LYS A CE
+1353 N NZ . LYS A 168 ? 1.2103 1.1806 1.1744 0.0241 -0.1312 0.0319 168 LYS A NZ
+#
+loop_
+_pdbx_poly_seq_scheme.asym_id
+_pdbx_poly_seq_scheme.entity_id
+_pdbx_poly_seq_scheme.seq_id
+_pdbx_poly_seq_scheme.mon_id
+_pdbx_poly_seq_scheme.ndb_seq_num
+_pdbx_poly_seq_scheme.pdb_seq_num
+_pdbx_poly_seq_scheme.auth_seq_num
+_pdbx_poly_seq_scheme.pdb_mon_id
+_pdbx_poly_seq_scheme.auth_mon_id
+_pdbx_poly_seq_scheme.pdb_strand_id
+_pdbx_poly_seq_scheme.pdb_ins_code
+_pdbx_poly_seq_scheme.hetero
+A 1 1 GLY 1 1 1 GLY ALA A . n
+A 1 2 THR 2 2 2 THR THR A . n
+A 1 3 LEU 3 3 3 LEU LEU A . n
+A 1 4 ARG 4 4 4 ARG ARG A . n
+A 1 5 PHE 5 5 5 PHE PHE A . n
+A 1 6 PHE 6 6 6 PHE PHE A . n
+A 1 7 THR 7 7 7 THR THR A . n
+A 1 8 VAL 8 8 8 VAL VAL A . n
+A 1 9 THR 9 9 9 THR THR A . n
+A 1 10 ASP 10 10 10 ASP ASP A . n
+A 1 11 GLU 11 11 11 GLU GLU A . n
+A 1 12 TYR 12 12 12 TYR TYR A . n
+A 1 13 ILE 13 13 13 ILE ILE A . n
+A 1 14 ALA 14 14 14 ALA ALA A . n
+A 1 15 TYR 15 15 15 TYR TYR A . n
+A 1 16 LEU 16 16 16 LEU LEU A . n
+A 1 17 ARG 17 17 17 ARG ARG A . n
+A 1 18 LYS 18 18 18 LYS LYS A . n
+A 1 19 PHE 19 19 19 PHE PHE A . n
+A 1 20 GLU 20 20 20 GLU GLU A . n
+A 1 21 SER 21 21 21 SER SER A . n
+A 1 22 LYS 22 22 22 LYS LYS A . n
+A 1 23 VAL 23 23 23 VAL VAL A . n
+A 1 24 HIS 24 24 24 HIS HIS A . n
+A 1 25 TYR 25 25 25 TYR TYR A . n
+A 1 26 GLN 26 26 26 GLN GLN A . n
+A 1 27 TYR 27 27 27 TYR TYR A . n
+A 1 28 GLU 28 28 28 GLU GLU A . n
+A 1 29 ASN 29 29 29 ASN ASN A . n
+A 1 30 ASN 30 30 30 ASN ASN A . n
+A 1 31 ALA 31 31 31 ALA ALA A . n
+A 1 32 SER 32 32 32 SER SER A . n
+A 1 33 THR 33 33 33 THR THR A . n
+A 1 34 TYR 34 34 34 TYR TYR A . n
+A 1 35 VAL 35 35 35 VAL VAL A . n
+A 1 36 GLY 36 36 36 GLY GLY A . n
+A 1 37 VAL 37 37 37 VAL VAL A . n
+A 1 38 VAL 38 38 38 VAL VAL A . n
+A 1 39 LEU 39 39 39 LEU LEU A . n
+A 1 40 LYS 40 40 40 LYS LYS A . n
+A 1 41 LYS 41 41 41 LYS LYS A . n
+A 1 42 ASN 42 42 42 ASN ASN A . n
+A 1 43 ASP 43 43 43 ASP ASP A . n
+A 1 44 PHE 44 44 44 PHE PHE A . n
+A 1 45 ASN 45 45 45 ASN ASN A . n
+A 1 46 TYR 46 46 46 TYR TYR A . n
+A 1 47 PHE 47 47 47 PHE PHE A . n
+A 1 48 ILE 48 48 48 ILE ILE A . n
+A 1 49 PRO 49 49 49 PRO PRO A . n
+A 1 50 LEU 50 50 50 LEU LEU A . n
+A 1 51 LEU 51 51 51 LEU LEU A . n
+A 1 52 SER 52 52 52 SER SER A . n
+A 1 53 TYR 53 53 53 TYR TYR A . n
+A 1 54 LYS 54 54 ? ? ? A . n
+A 1 55 LYS 55 55 ? ? ? A . n
+A 1 56 GLY 56 56 ? ? ? A . n
+A 1 57 ASN 57 57 57 ASN ASN A . n
+A 1 58 PRO 58 58 58 PRO PRO A . n
+A 1 59 GLU 59 59 59 GLU GLU A . n
+A 1 60 LYS 60 60 60 LYS LYS A . n
+A 1 61 ASP 61 61 61 ASP ASP A . n
+A 1 62 LYS 62 62 62 LYS LYS A . n
+A 1 63 ALA 63 63 63 ALA ALA A . n
+A 1 64 MET 64 64 64 MET MET A . n
+A 1 65 LYS 65 65 65 LYS LYS A . n
+A 1 66 LYS 66 66 66 LYS LYS A . n
+A 1 67 ARG 67 67 67 ARG ARG A . n
+A 1 68 SER 68 68 68 SER SER A . n
+A 1 69 ARG 69 69 69 ARG ARG A . n
+A 1 70 ILE 70 70 70 ILE ILE A . n
+A 1 71 VAL 71 71 71 VAL VAL A . n
+A 1 72 THR 72 72 72 THR THR A . n
+A 1 73 ARG 73 73 73 ARG ARG A . n
+A 1 74 LEU 74 74 74 LEU LEU A . n
+A 1 75 PHE 75 75 75 PHE PHE A . n
+A 1 76 GLU 76 76 76 GLU GLU A . n
+A 1 77 ILE 77 77 77 ILE ILE A . n
+A 1 78 GLY 78 78 78 GLY GLY A . n
+A 1 79 ASN 79 79 79 ASN ASN A . n
+A 1 80 ILE 80 80 80 ILE ILE A . n
+A 1 81 ASN 81 81 81 ASN ASN A . n
+A 1 82 ASN 82 82 82 ASN ASN A . n
+A 1 83 PRO 83 83 83 PRO PRO A . n
+A 1 84 LEU 84 84 84 LEU LEU A . n
+A 1 85 GLY 85 85 85 GLY GLY A . n
+A 1 86 TYR 86 86 86 TYR TYR A . n
+A 1 87 LEU 87 87 87 LEU LEU A . n
+A 1 88 LEU 88 88 88 LEU LEU A . n
+A 1 89 HIS 89 89 89 HIS HIS A . n
+A 1 90 HIS 90 90 90 HIS HIS A . n
+A 1 91 ASN 91 91 91 ASN ASN A . n
+A 1 92 MET 92 92 92 MET MET A . n
+A 1 93 ILE 93 93 93 ILE ILE A . n
+A 1 94 PRO 94 94 94 PRO PRO A . n
+A 1 95 VAL 95 95 95 VAL VAL A . n
+A 1 96 PRO 96 96 96 PRO PRO A . n
+A 1 97 ASP 97 97 97 ASP ASP A . n
+A 1 98 SER 98 98 98 SER SER A . n
+A 1 99 GLU 99 99 99 GLU GLU A . n
+A 1 100 LEU 100 100 100 LEU LEU A . n
+A 1 101 ILE 101 101 101 ILE ILE A . n
+A 1 102 PRO 102 102 102 PRO PRO A . n
+A 1 103 LEU 103 103 103 LEU LEU A . n
+A 1 104 PRO 104 104 104 PRO PRO A . n
+A 1 105 LEU 105 105 105 LEU LEU A . n
+A 1 106 ASP 106 106 106 ASP ASP A . n
+A 1 107 LEU 107 107 107 LEU LEU A . n
+A 1 108 LYS 108 108 108 LYS LYS A . n
+A 1 109 LYS 109 109 109 LYS LYS A . n
+A 1 110 PRO 110 110 110 PRO PRO A . n
+A 1 111 LYS 111 111 111 LYS LYS A . n
+A 1 112 HIS 112 112 112 HIS HIS A . n
+A 1 113 LYS 113 113 113 LYS LYS A . n
+A 1 114 MET 114 114 114 MET MET A . n
+A 1 115 MET 115 115 115 MET MET A . n
+A 1 116 GLN 116 116 116 GLN GLN A . n
+A 1 117 LYS 117 117 117 LYS LYS A . n
+A 1 118 GLN 118 118 118 GLN GLN A . n
+A 1 119 LEU 119 119 119 LEU LEU A . n
+A 1 120 ILE 120 120 120 ILE ILE A . n
+A 1 121 TYR 121 121 121 TYR TYR A . n
+A 1 122 MET 122 122 122 MET MET A . n
+A 1 123 LYS 123 123 123 LYS LYS A . n
+A 1 124 SER 124 124 124 SER SER A . n
+A 1 125 ILE 125 125 125 ILE ILE A . n
+A 1 126 SER 126 126 126 SER SER A . n
+A 1 127 GLU 127 127 127 GLU GLU A . n
+A 1 128 LYS 128 128 128 LYS LYS A . n
+A 1 129 ILE 129 129 129 ILE ILE A . n
+A 1 130 GLU 130 130 130 GLU GLU A . n
+A 1 131 ASN 131 131 131 ASN ASN A . n
+A 1 132 LYS 132 132 132 LYS LYS A . n
+A 1 133 SER 133 133 133 SER SER A . n
+A 1 134 GLU 134 134 134 GLU GLU A . n
+A 1 135 VAL 135 135 135 VAL VAL A . n
+A 1 136 VAL 136 136 136 VAL VAL A . n
+A 1 137 TYR 137 137 137 TYR TYR A . n
+A 1 138 ARG 138 138 138 ARG ARG A . n
+A 1 139 LYS 139 139 139 LYS LYS A . n
+A 1 140 ALA 140 140 140 ALA ALA A . n
+A 1 141 ALA 141 141 141 ALA ALA A . n
+A 1 142 HIS 142 142 142 HIS HIS A . n
+A 1 143 GLU 143 143 143 GLU GLU A . n
+A 1 144 LYS 144 144 144 LYS LYS A . n
+A 1 145 ASP 145 145 145 ASP ASP A . n
+A 1 146 GLY 146 146 146 GLY GLY A . n
+A 1 147 TYR 147 147 147 TYR TYR A . n
+A 1 148 TYR 148 148 148 TYR TYR A . n
+A 1 149 LEU 149 149 149 LEU LEU A . n
+A 1 150 LYS 150 150 150 LYS LYS A . n
+A 1 151 PHE 151 151 151 PHE PHE A . n
+A 1 152 SER 152 152 152 SER SER A . n
+A 1 153 CYS 153 153 153 CYS CYS A . n
+A 1 154 ASP 154 154 154 ASP ASP A . n
+A 1 155 PHE 155 155 155 PHE PHE A . n
+A 1 156 LYS 156 156 156 LYS LYS A . n
+A 1 157 LEU 157 157 157 LEU LEU A . n
+A 1 158 LEU 158 158 158 LEU LEU A . n
+A 1 159 GLU 159 159 159 GLU GLU A . n
+A 1 160 ALA 160 160 160 ALA ALA A . n
+A 1 161 LYS 161 161 161 LYS LYS A . n
+A 1 162 ALA 162 162 162 ALA ALA A . n
+A 1 163 THR 163 163 163 THR THR A . n
+A 1 164 LEU 164 164 164 LEU LEU A . n
+A 1 165 TYR 165 165 165 TYR TYR A . n
+A 1 166 SER 166 166 166 SER SER A . n
+A 1 167 LYS 167 167 167 LYS LYS A . n
+A 1 168 LYS 168 168 168 LYS LYS A . n
+A 1 169 SER 169 169 ? ? ? A . n
+A 1 170 THR 170 170 ? ? ? A . n
+A 1 171 PHE 171 171 ? ? ? A . n
+A 1 172 GLN 172 172 ? ? ? A . n
+#
+loop_
+_pdbx_nonpoly_scheme.asym_id
+_pdbx_nonpoly_scheme.entity_id
+_pdbx_nonpoly_scheme.mon_id
+_pdbx_nonpoly_scheme.ndb_seq_num
+_pdbx_nonpoly_scheme.pdb_seq_num
+_pdbx_nonpoly_scheme.auth_seq_num
+_pdbx_nonpoly_scheme.pdb_mon_id
+_pdbx_nonpoly_scheme.auth_mon_id
+_pdbx_nonpoly_scheme.pdb_strand_id
+_pdbx_nonpoly_scheme.pdb_ins_code
+B 2 GOL 1 201 1 GOL GOL A .
+C 2 GOL 1 202 2 GOL GOL A .
+D 2 GOL 1 203 3 GOL GOL A .
+E 3 HOH 1 301 1 HOH HOH A .
+E 3 HOH 2 302 2 HOH HOH A .
+E 3 HOH 3 303 3 HOH HOH A .
+E 3 HOH 4 304 4 HOH HOH A .
+E 3 HOH 5 305 5 HOH HOH A .
+E 3 HOH 6 306 6 HOH HOH A .
+E 3 HOH 7 307 7 HOH HOH A .
+E 3 HOH 8 308 8 HOH HOH A .
+E 3 HOH 9 309 9 HOH HOH A .
+E 3 HOH 10 310 10 HOH HOH A .
+E 3 HOH 11 311 11 HOH HOH A .
+E 3 HOH 12 312 12 HOH HOH A .
+E 3 HOH 13 313 13 HOH HOH A .
+E 3 HOH 14 314 14 HOH HOH A .
+E 3 HOH 15 315 15 HOH HOH A .
+E 3 HOH 16 316 16 HOH HOH A .
+E 3 HOH 17 317 17 HOH HOH A .
+E 3 HOH 18 318 18 HOH HOH A .
+E 3 HOH 19 319 19 HOH HOH A .
+E 3 HOH 20 320 20 HOH HOH A .
+E 3 HOH 21 321 21 HOH HOH A .
+E 3 HOH 22 322 22 HOH HOH A .
+E 3 HOH 23 323 23 HOH HOH A .
+E 3 HOH 24 324 24 HOH HOH A .
+E 3 HOH 25 325 25 HOH HOH A .
+E 3 HOH 26 326 26 HOH HOH A .
+E 3 HOH 27 327 27 HOH HOH A .
+E 3 HOH 28 328 28 HOH HOH A .
+E 3 HOH 29 329 29 HOH HOH A .
+E 3 HOH 30 330 30 HOH HOH A .
+E 3 HOH 31 331 31 HOH HOH A .
+E 3 HOH 32 332 32 HOH HOH A .
+E 3 HOH 33 333 33 HOH HOH A .
+E 3 HOH 34 334 34 HOH HOH A .
+E 3 HOH 35 335 35 HOH HOH A .
+E 3 HOH 36 336 36 HOH HOH A .
+E 3 HOH 37 337 37 HOH HOH A .
+E 3 HOH 38 338 38 HOH HOH A .
+E 3 HOH 39 339 39 HOH HOH A .
+E 3 HOH 40 340 40 HOH HOH A .
+E 3 HOH 41 341 41 HOH HOH A .
+E 3 HOH 42 342 42 HOH HOH A .
+E 3 HOH 43 343 43 HOH HOH A .
+E 3 HOH 44 344 44 HOH HOH A .
+E 3 HOH 45 345 45 HOH HOH A .
+E 3 HOH 46 346 46 HOH HOH A .
+E 3 HOH 47 347 47 HOH HOH A .
+E 3 HOH 48 348 48 HOH HOH A .
+E 3 HOH 49 349 49 HOH HOH A .
+E 3 HOH 50 350 50 HOH HOH A .
+E 3 HOH 51 351 51 HOH HOH A .
+E 3 HOH 52 352 52 HOH HOH A .
+E 3 HOH 53 353 53 HOH HOH A .
+E 3 HOH 54 354 54 HOH HOH A .
+E 3 HOH 55 355 55 HOH HOH A .
+E 3 HOH 56 356 56 HOH HOH A .
+E 3 HOH 57 357 57 HOH HOH A .
+E 3 HOH 58 358 58 HOH HOH A .
+E 3 HOH 59 359 59 HOH HOH A .
+E 3 HOH 60 360 60 HOH HOH A .
+E 3 HOH 61 361 61 HOH HOH A .
+E 3 HOH 62 362 62 HOH HOH A .
+E 3 HOH 63 363 63 HOH HOH A .
+E 3 HOH 64 364 64 HOH HOH A .
+E 3 HOH 65 365 65 HOH HOH A .
+E 3 HOH 66 366 66 HOH HOH A .
+E 3 HOH 67 367 67 HOH HOH A .
+E 3 HOH 68 368 68 HOH HOH A .
+E 3 HOH 69 369 69 HOH HOH A .
+#
+_pdbx_struct_assembly.id 1
+_pdbx_struct_assembly.details author_and_software_defined_assembly
+_pdbx_struct_assembly.method_details PISA
+_pdbx_struct_assembly.oligomeric_details monomeric
+_pdbx_struct_assembly.oligomeric_count 1
+#
+_pdbx_struct_assembly_gen.assembly_id 1
+_pdbx_struct_assembly_gen.oper_expression 1
+_pdbx_struct_assembly_gen.asym_id_list A,B,C,D,E
+#
+_pdbx_struct_oper_list.id 1
+_pdbx_struct_oper_list.type 'identity operation'
+_pdbx_struct_oper_list.name 1_555
+_pdbx_struct_oper_list.symmetry_operation x,y,z
+_pdbx_struct_oper_list.matrix[1][1] 1.0000000000
+_pdbx_struct_oper_list.matrix[1][2] 0.0000000000
+_pdbx_struct_oper_list.matrix[1][3] 0.0000000000
+_pdbx_struct_oper_list.vector[1] 0.0000000000
+_pdbx_struct_oper_list.matrix[2][1] 0.0000000000
+_pdbx_struct_oper_list.matrix[2][2] 1.0000000000
+_pdbx_struct_oper_list.matrix[2][3] 0.0000000000
+_pdbx_struct_oper_list.vector[2] 0.0000000000
+_pdbx_struct_oper_list.matrix[3][1] 0.0000000000
+_pdbx_struct_oper_list.matrix[3][2] 0.0000000000
+_pdbx_struct_oper_list.matrix[3][3] 1.0000000000
+_pdbx_struct_oper_list.vector[3] 0.0000000000
+#
+loop_
+_pdbx_audit_revision_history.ordinal
+_pdbx_audit_revision_history.data_content_type
+_pdbx_audit_revision_history.major_revision
+_pdbx_audit_revision_history.minor_revision
+_pdbx_audit_revision_history.revision_date
+1 'Structure model' 1 0 2013-01-16
+2 'Structure model' 1 1 2013-02-20
+3 'Structure model' 1 2 2023-09-13
+#
+_pdbx_audit_revision_details.ordinal 1
+_pdbx_audit_revision_details.revision_ordinal 1
+_pdbx_audit_revision_details.data_content_type 'Structure model'
+_pdbx_audit_revision_details.provider repository
+_pdbx_audit_revision_details.type 'Initial release'
+_pdbx_audit_revision_details.description ?
+_pdbx_audit_revision_details.details ?
+#
+loop_
+_pdbx_audit_revision_group.ordinal
+_pdbx_audit_revision_group.revision_ordinal
+_pdbx_audit_revision_group.data_content_type
+_pdbx_audit_revision_group.group
+1 2 'Structure model' 'Database references'
+2 3 'Structure model' 'Data collection'
+3 3 'Structure model' 'Database references'
+4 3 'Structure model' 'Derived calculations'
+5 3 'Structure model' 'Refinement description'
+#
+loop_
+_pdbx_audit_revision_category.ordinal
+_pdbx_audit_revision_category.revision_ordinal
+_pdbx_audit_revision_category.data_content_type
+_pdbx_audit_revision_category.category
+1 3 'Structure model' chem_comp_atom
+2 3 'Structure model' chem_comp_bond
+3 3 'Structure model' database_2
+4 3 'Structure model' pdbx_initial_refinement_model
+5 3 'Structure model' struct_ref_seq_dif
+6 3 'Structure model' struct_site
+#
+loop_
+_pdbx_audit_revision_item.ordinal
+_pdbx_audit_revision_item.revision_ordinal
+_pdbx_audit_revision_item.data_content_type
+_pdbx_audit_revision_item.item
+1 3 'Structure model' '_database_2.pdbx_DOI'
+2 3 'Structure model' '_database_2.pdbx_database_accession'
+3 3 'Structure model' '_struct_ref_seq_dif.details'
+4 3 'Structure model' '_struct_site.pdbx_auth_asym_id'
+5 3 'Structure model' '_struct_site.pdbx_auth_comp_id'
+6 3 'Structure model' '_struct_site.pdbx_auth_seq_id'
+#
+loop_
+_pdbx_refine_tls.pdbx_refine_id
+_pdbx_refine_tls.id
+_pdbx_refine_tls.details
+_pdbx_refine_tls.method
+_pdbx_refine_tls.origin_x
+_pdbx_refine_tls.origin_y
+_pdbx_refine_tls.origin_z
+_pdbx_refine_tls.T[1][1]
+_pdbx_refine_tls.T[2][2]
+_pdbx_refine_tls.T[3][3]
+_pdbx_refine_tls.T[1][2]
+_pdbx_refine_tls.T[1][3]
+_pdbx_refine_tls.T[2][3]
+_pdbx_refine_tls.L[1][1]
+_pdbx_refine_tls.L[2][2]
+_pdbx_refine_tls.L[3][3]
+_pdbx_refine_tls.L[1][2]
+_pdbx_refine_tls.L[1][3]
+_pdbx_refine_tls.L[2][3]
+_pdbx_refine_tls.S[1][1]
+_pdbx_refine_tls.S[2][2]
+_pdbx_refine_tls.S[3][3]
+_pdbx_refine_tls.S[1][2]
+_pdbx_refine_tls.S[1][3]
+_pdbx_refine_tls.S[2][3]
+_pdbx_refine_tls.S[2][1]
+_pdbx_refine_tls.S[3][1]
+_pdbx_refine_tls.S[3][2]
+'X-RAY DIFFRACTION' 1 ? refined -4.2370 9.7849 -8.4216 -0.0153 0.0060 -0.0027 -0.0178 0.0063 -0.0282 0.5346 0.0035 0.1401
+-0.1421 0.1281 -0.0091 0.0034 -0.0029 -0.0005 0.0205 -0.0105 -0.0111 0.0346 0.0164 -0.0004
+'X-RAY DIFFRACTION' 2 ? refined -11.6035 12.1350 -3.6199 0.0082 -0.0168 0.0187 -0.0038 0.0308 -0.0191 0.1613 0.3875 0.3830
+0.0871 -0.0568 -0.1545 -0.0029 -0.0157 0.0186 0.0161 0.0139 0.0000 0.0236 -0.0024 -0.0143
+'X-RAY DIFFRACTION' 3 ? refined 4.6029 15.8531 -10.3077 -0.0071 0.0209 0.0115 0.0615 -0.0127 0.0126 0.1406 0.0000 0.3075
+-0.0553 -0.3807 -0.4888 -0.0004 0.0050 -0.0045 -0.0013 -0.0027 -0.0108 -0.0019 -0.0077 0.0019
+'X-RAY DIFFRACTION' 4 ? refined -7.9765 19.0957 -13.6104 -0.0081 -0.0048 0.0087 0.0079 -0.0156 -0.0096 0.1954 0.3649 0.2286
+0.3321 -0.0618 0.8137 -0.0020 0.0214 -0.0194 0.0201 0.0047 0.0075 -0.0042 0.0064 -0.0228
+'X-RAY DIFFRACTION' 5 ? refined -14.6242 31.1730 -12.7675 -0.0243 0.0163 0.0010 0.0129 -0.0394 0.0223 0.0636 0.0000 0.0003
+-0.0439 0.0587 -0.1771 0.0000 -0.0039 0.0039 -0.0023 0.0025 0.0049 0.0052 0.0003 -0.0081
+'X-RAY DIFFRACTION' 6 ? refined -8.3530 27.3597 -21.7348 -0.0198 0.0256 -0.0036 -0.0051 -0.0229 0.0380 0.3186 0.0410 0.1217
+0.4046 0.0407 -0.4669 0.0061 -0.0047 -0.0014 0.0066 0.0020 0.0243 -0.0054 -0.0076 0.0030
+'X-RAY DIFFRACTION' 7 ? refined -9.1418 24.1527 -15.8550 -0.0233 0.0141 0.0057 0.0069 0.0045 0.0229 0.2875 0.3091 0.2779
+0.0482 -0.3700 -0.1493 0.0021 -0.0072 0.0051 -0.0023 0.0168 0.0173 -0.0208 -0.0135 -0.0042
+'X-RAY DIFFRACTION' 8 ? refined -1.4932 7.3490 -10.2771 0.0018 -0.0219 0.0214 0.0183 -0.0318 -0.0305 0.0817 0.0000 0.0341
+-0.5586 0.0298 0.3223 -0.0039 -0.0004 0.0043 0.0036 0.0110 -0.0137 0.0148 0.0133 0.0053
+'X-RAY DIFFRACTION' 9 ? refined -13.7104 10.3151 -25.7781 -0.0066 -0.0135 0.0399 -0.0060 -0.0793 -0.0113 0.3186 0.3591 0.0000
+0.1042 0.3329 -0.1747 0.0009 0.0005 -0.0014 0.0059 -0.0002 0.0118 0.0073 -0.0041 -0.0190
+'X-RAY DIFFRACTION' 10 ? refined -2.2191 21.6364 -23.4358 0.0122 -0.0280 0.0070 -0.0126 -0.0130 0.0161 0.0737 0.0018 0.2394
+0.1287 -0.1610 -0.4035 0.0048 0.0023 -0.0071 -0.0021 -0.0018 0.0019 -0.0368 0.0030 0.0105
+'X-RAY DIFFRACTION' 11 ? refined 4.5887 27.1871 -7.8214 -0.0263 -0.0145 0.0527 -0.0124 -0.0141 0.0181 0.0656 0.2088 0.0209
+-0.1076 0.2472 -0.0807 -0.0012 0.0092 -0.0079 -0.0013 -0.0169 -0.0094 0.0067 0.0007 0.0146
+'X-RAY DIFFRACTION' 12 ? refined -2.0543 29.2585 -1.0962 -0.0077 0.0221 -0.0246 0.0234 -0.0404 -0.0192 0.0465 0.0214 0.0181
+-0.1037 0.5807 0.1399 0.0023 0.0050 -0.0073 -0.0009 0.0069 -0.0118 0.0200 -0.0004 0.0032
+'X-RAY DIFFRACTION' 13 ? refined 3.5622 10.5932 2.3426 0.0305 0.0120 0.0014 0.0221 -0.1095 0.0192 0.0070 0.1256 0.1130
+0.2251 0.6630 -0.2637 -0.0017 0.0010 0.0007 -0.0110 -0.0170 -0.0034 0.0114 0.0040 0.0073
+#
+loop_
+_pdbx_refine_tls_group.pdbx_refine_id
+_pdbx_refine_tls_group.id
+_pdbx_refine_tls_group.refine_tls_id
+_pdbx_refine_tls_group.beg_auth_asym_id
+_pdbx_refine_tls_group.beg_auth_seq_id
+_pdbx_refine_tls_group.end_auth_asym_id
+_pdbx_refine_tls_group.end_auth_seq_id
+_pdbx_refine_tls_group.selection_details
+_pdbx_refine_tls_group.beg_label_asym_id
+_pdbx_refine_tls_group.beg_label_seq_id
+_pdbx_refine_tls_group.end_label_asym_id
+_pdbx_refine_tls_group.end_label_seq_id
+_pdbx_refine_tls_group.selection
+'X-RAY DIFFRACTION' 1 1 A 1 A 17 '{A|1 - A|17}' ? ? ? ? ?
+'X-RAY DIFFRACTION' 2 2 A 18 A 33 '{A|18 - A|33}' ? ? ? ? ?
+'X-RAY DIFFRACTION' 3 3 A 34 A 44 '{A|34 - A|44}' ? ? ? ? ?
+'X-RAY DIFFRACTION' 4 4 A 45 A 57 '{A|45 - A|57}' ? ? ? ? ?
+'X-RAY DIFFRACTION' 5 5 A 58 A 68 '{A|58 - A|68}' ? ? ? ? ?
+'X-RAY DIFFRACTION' 6 6 A 69 A 80 '{A|69 - A|80}' ? ? ? ? ?
+'X-RAY DIFFRACTION' 7 7 A 81 A 92 '{A|81 - A|92}' ? ? ? ? ?
+'X-RAY DIFFRACTION' 8 8 A 93 A 104 '{A|93 - A|104}' ? ? ? ? ?
+'X-RAY DIFFRACTION' 9 9 A 105 A 116 '{A|105 - A|116}' ? ? ? ? ?
+'X-RAY DIFFRACTION' 10 10 A 117 A 129 '{A|117 - A|129}' ? ? ? ? ?
+'X-RAY DIFFRACTION' 11 11 A 130 A 142 '{A|130 - A|142}' ? ? ? ? ?
+'X-RAY DIFFRACTION' 12 12 A 143 A 155 '{A|143 - A|155}' ? ? ? ? ?
+'X-RAY DIFFRACTION' 13 13 A 156 A 168 '{A|156 - A|168}' ? ? ? ? ?
+#
+loop_
+_software.name
+_software.classification
+_software.version
+_software.citation_id
+_software.pdbx_ordinal
+DNA 'data collection' . ? 1
+MOLREP phasing . ? 2
+BUSTER refinement 2.9.2 ? 3
+XDS 'data reduction' . ? 4
+XSCALE 'data scaling' . ? 5
+#
+loop_
+_pdbx_validate_torsion.id
+_pdbx_validate_torsion.PDB_model_num
+_pdbx_validate_torsion.auth_comp_id
+_pdbx_validate_torsion.auth_asym_id
+_pdbx_validate_torsion.auth_seq_id
+_pdbx_validate_torsion.PDB_ins_code
+_pdbx_validate_torsion.label_alt_id
+_pdbx_validate_torsion.phi
+_pdbx_validate_torsion.psi
+1 1 GLU A 28 ? ? 37.87 -89.48
+2 1 PRO A 58 ? ? -39.10 -16.18
+3 1 ASN A 79 ? ? -167.40 53.23
+4 1 LEU A 88 ? ? -102.89 77.48
+#
+loop_
+_pdbx_unobs_or_zero_occ_atoms.id
+_pdbx_unobs_or_zero_occ_atoms.PDB_model_num
+_pdbx_unobs_or_zero_occ_atoms.polymer_flag
+_pdbx_unobs_or_zero_occ_atoms.occupancy_flag
+_pdbx_unobs_or_zero_occ_atoms.auth_asym_id
+_pdbx_unobs_or_zero_occ_atoms.auth_comp_id
+_pdbx_unobs_or_zero_occ_atoms.auth_seq_id
+_pdbx_unobs_or_zero_occ_atoms.PDB_ins_code
+_pdbx_unobs_or_zero_occ_atoms.auth_atom_id
+_pdbx_unobs_or_zero_occ_atoms.label_alt_id
+_pdbx_unobs_or_zero_occ_atoms.label_asym_id
+_pdbx_unobs_or_zero_occ_atoms.label_comp_id
+_pdbx_unobs_or_zero_occ_atoms.label_seq_id
+_pdbx_unobs_or_zero_occ_atoms.label_atom_id
+1 1 Y 1 A LYS 41 ? CG ? A LYS 41 CG
+2 1 Y 1 A LYS 41 ? CD ? A LYS 41 CD
+3 1 Y 1 A LYS 41 ? CE ? A LYS 41 CE
+4 1 Y 1 A LYS 41 ? NZ ? A LYS 41 NZ
+5 1 Y 1 A ASN 57 ? CG ? A ASN 57 CG
+6 1 Y 1 A ASN 57 ? OD1 ? A ASN 57 OD1
+7 1 Y 1 A ASN 57 ? ND2 ? A ASN 57 ND2
+8 1 Y 1 A ASP 61 ? CG ? A ASP 61 CG
+9 1 Y 1 A ASP 61 ? OD1 ? A ASP 61 OD1
+10 1 Y 1 A ASP 61 ? OD2 ? A ASP 61 OD2
+11 1 Y 1 A LYS 62 ? CG ? A LYS 62 CG
+12 1 Y 1 A LYS 62 ? CD ? A LYS 62 CD
+13 1 Y 1 A LYS 62 ? CE ? A LYS 62 CE
+14 1 Y 1 A LYS 62 ? NZ ? A LYS 62 NZ
+15 1 Y 1 A LYS 66 ? CG ? A LYS 66 CG
+16 1 Y 1 A LYS 66 ? CD ? A LYS 66 CD
+17 1 Y 1 A LYS 66 ? CE ? A LYS 66 CE
+18 1 Y 1 A LYS 66 ? NZ ? A LYS 66 NZ
+19 1 Y 1 A LYS 108 ? CG ? A LYS 108 CG
+20 1 Y 1 A LYS 108 ? CD ? A LYS 108 CD
+21 1 Y 1 A LYS 108 ? CE ? A LYS 108 CE
+22 1 Y 1 A LYS 108 ? NZ ? A LYS 108 NZ
+#
+loop_
+_pdbx_unobs_or_zero_occ_residues.id
+_pdbx_unobs_or_zero_occ_residues.PDB_model_num
+_pdbx_unobs_or_zero_occ_residues.polymer_flag
+_pdbx_unobs_or_zero_occ_residues.occupancy_flag
+_pdbx_unobs_or_zero_occ_residues.auth_asym_id
+_pdbx_unobs_or_zero_occ_residues.auth_comp_id
+_pdbx_unobs_or_zero_occ_residues.auth_seq_id
+_pdbx_unobs_or_zero_occ_residues.PDB_ins_code
+_pdbx_unobs_or_zero_occ_residues.label_asym_id
+_pdbx_unobs_or_zero_occ_residues.label_comp_id
+_pdbx_unobs_or_zero_occ_residues.label_seq_id
+1 1 Y 1 A LYS 54 ? A LYS 54
+2 1 Y 1 A LYS 55 ? A LYS 55
+3 1 Y 1 A GLY 56 ? A GLY 56
+4 1 Y 1 A SER 169 ? A SER 169
+5 1 Y 1 A THR 170 ? A THR 170
+6 1 Y 1 A PHE 171 ? A PHE 171
+7 1 Y 1 A GLN 172 ? A GLN 172
+#
+loop_
+_chem_comp_atom.comp_id
+_chem_comp_atom.atom_id
+_chem_comp_atom.type_symbol
+_chem_comp_atom.pdbx_aromatic_flag
+_chem_comp_atom.pdbx_stereo_config
+_chem_comp_atom.pdbx_ordinal
+ALA N N N N 1
+ALA CA C N S 2
+ALA C C N N 3
+ALA O O N N 4
+ALA CB C N N 5
+ALA OXT O N N 6
+ALA H H N N 7
+ALA H2 H N N 8
+ALA HA H N N 9
+ALA HB1 H N N 10
+ALA HB2 H N N 11
+ALA HB3 H N N 12
+ALA HXT H N N 13
+ARG N N N N 14
+ARG CA C N S 15
+ARG C C N N 16
+ARG O O N N 17
+ARG CB C N N 18
+ARG CG C N N 19
+ARG CD C N N 20
+ARG NE N N N 21
+ARG CZ C N N 22
+ARG NH1 N N N 23
+ARG NH2 N N N 24
+ARG OXT O N N 25
+ARG H H N N 26
+ARG H2 H N N 27
+ARG HA H N N 28
+ARG HB2 H N N 29
+ARG HB3 H N N 30
+ARG HG2 H N N 31
+ARG HG3 H N N 32
+ARG HD2 H N N 33
+ARG HD3 H N N 34
+ARG HE H N N 35
+ARG HH11 H N N 36
+ARG HH12 H N N 37
+ARG HH21 H N N 38
+ARG HH22 H N N 39
+ARG HXT H N N 40
+ASN N N N N 41
+ASN CA C N S 42
+ASN C C N N 43
+ASN O O N N 44
+ASN CB C N N 45
+ASN CG C N N 46
+ASN OD1 O N N 47
+ASN ND2 N N N 48
+ASN OXT O N N 49
+ASN H H N N 50
+ASN H2 H N N 51
+ASN HA H N N 52
+ASN HB2 H N N 53
+ASN HB3 H N N 54
+ASN HD21 H N N 55
+ASN HD22 H N N 56
+ASN HXT H N N 57
+ASP N N N N 58
+ASP CA C N S 59
+ASP C C N N 60
+ASP O O N N 61
+ASP CB C N N 62
+ASP CG C N N 63
+ASP OD1 O N N 64
+ASP OD2 O N N 65
+ASP OXT O N N 66
+ASP H H N N 67
+ASP H2 H N N 68
+ASP HA H N N 69
+ASP HB2 H N N 70
+ASP HB3 H N N 71
+ASP HD2 H N N 72
+ASP HXT H N N 73
+CYS N N N N 74
+CYS CA C N R 75
+CYS C C N N 76
+CYS O O N N 77
+CYS CB C N N 78
+CYS SG S N N 79
+CYS OXT O N N 80
+CYS H H N N 81
+CYS H2 H N N 82
+CYS HA H N N 83
+CYS HB2 H N N 84
+CYS HB3 H N N 85
+CYS HG H N N 86
+CYS HXT H N N 87
+GLN N N N N 88
+GLN CA C N S 89
+GLN C C N N 90
+GLN O O N N 91
+GLN CB C N N 92
+GLN CG C N N 93
+GLN CD C N N 94
+GLN OE1 O N N 95
+GLN NE2 N N N 96
+GLN OXT O N N 97
+GLN H H N N 98
+GLN H2 H N N 99
+GLN HA H N N 100
+GLN HB2 H N N 101
+GLN HB3 H N N 102
+GLN HG2 H N N 103
+GLN HG3 H N N 104
+GLN HE21 H N N 105
+GLN HE22 H N N 106
+GLN HXT H N N 107
+GLU N N N N 108
+GLU CA C N S 109
+GLU C C N N 110
+GLU O O N N 111
+GLU CB C N N 112
+GLU CG C N N 113
+GLU CD C N N 114
+GLU OE1 O N N 115
+GLU OE2 O N N 116
+GLU OXT O N N 117
+GLU H H N N 118
+GLU H2 H N N 119
+GLU HA H N N 120
+GLU HB2 H N N 121
+GLU HB3 H N N 122
+GLU HG2 H N N 123
+GLU HG3 H N N 124
+GLU HE2 H N N 125
+GLU HXT H N N 126
+GLY N N N N 127
+GLY CA C N N 128
+GLY C C N N 129
+GLY O O N N 130
+GLY OXT O N N 131
+GLY H H N N 132
+GLY H2 H N N 133
+GLY HA2 H N N 134
+GLY HA3 H N N 135
+GLY HXT H N N 136
+GOL C1 C N N 137
+GOL O1 O N N 138
+GOL C2 C N N 139
+GOL O2 O N N 140
+GOL C3 C N N 141
+GOL O3 O N N 142
+GOL H11 H N N 143
+GOL H12 H N N 144
+GOL HO1 H N N 145
+GOL H2 H N N 146
+GOL HO2 H N N 147
+GOL H31 H N N 148
+GOL H32 H N N 149
+GOL HO3 H N N 150
+HIS N N N N 151
+HIS CA C N S 152
+HIS C C N N 153
+HIS O O N N 154
+HIS CB C N N 155
+HIS CG C Y N 156
+HIS ND1 N Y N 157
+HIS CD2 C Y N 158
+HIS CE1 C Y N 159
+HIS NE2 N Y N 160
+HIS OXT O N N 161
+HIS H H N N 162
+HIS H2 H N N 163
+HIS HA H N N 164
+HIS HB2 H N N 165
+HIS HB3 H N N 166
+HIS HD1 H N N 167
+HIS HD2 H N N 168
+HIS HE1 H N N 169
+HIS HE2 H N N 170
+HIS HXT H N N 171
+HOH O O N N 172
+HOH H1 H N N 173
+HOH H2 H N N 174
+ILE N N N N 175
+ILE CA C N S 176
+ILE C C N N 177
+ILE O O N N 178
+ILE CB C N S 179
+ILE CG1 C N N 180
+ILE CG2 C N N 181
+ILE CD1 C N N 182
+ILE OXT O N N 183
+ILE H H N N 184
+ILE H2 H N N 185
+ILE HA H N N 186
+ILE HB H N N 187
+ILE HG12 H N N 188
+ILE HG13 H N N 189
+ILE HG21 H N N 190
+ILE HG22 H N N 191
+ILE HG23 H N N 192
+ILE HD11 H N N 193
+ILE HD12 H N N 194
+ILE HD13 H N N 195
+ILE HXT H N N 196
+LEU N N N N 197
+LEU CA C N S 198
+LEU C C N N 199
+LEU O O N N 200
+LEU CB C N N 201
+LEU CG C N N 202
+LEU CD1 C N N 203
+LEU CD2 C N N 204
+LEU OXT O N N 205
+LEU H H N N 206
+LEU H2 H N N 207
+LEU HA H N N 208
+LEU HB2 H N N 209
+LEU HB3 H N N 210
+LEU HG H N N 211
+LEU HD11 H N N 212
+LEU HD12 H N N 213
+LEU HD13 H N N 214
+LEU HD21 H N N 215
+LEU HD22 H N N 216
+LEU HD23 H N N 217
+LEU HXT H N N 218
+LYS N N N N 219
+LYS CA C N S 220
+LYS C C N N 221
+LYS O O N N 222
+LYS CB C N N 223
+LYS CG C N N 224
+LYS CD C N N 225
+LYS CE C N N 226
+LYS NZ N N N 227
+LYS OXT O N N 228
+LYS H H N N 229
+LYS H2 H N N 230
+LYS HA H N N 231
+LYS HB2 H N N 232
+LYS HB3 H N N 233
+LYS HG2 H N N 234
+LYS HG3 H N N 235
+LYS HD2 H N N 236
+LYS HD3 H N N 237
+LYS HE2 H N N 238
+LYS HE3 H N N 239
+LYS HZ1 H N N 240
+LYS HZ2 H N N 241
+LYS HZ3 H N N 242
+LYS HXT H N N 243
+MET N N N N 244
+MET CA C N S 245
+MET C C N N 246
+MET O O N N 247
+MET CB C N N 248
+MET CG C N N 249
+MET SD S N N 250
+MET CE C N N 251
+MET OXT O N N 252
+MET H H N N 253
+MET H2 H N N 254
+MET HA H N N 255
+MET HB2 H N N 256
+MET HB3 H N N 257
+MET HG2 H N N 258
+MET HG3 H N N 259
+MET HE1 H N N 260
+MET HE2 H N N 261
+MET HE3 H N N 262
+MET HXT H N N 263
+PHE N N N N 264
+PHE CA C N S 265
+PHE C C N N 266
+PHE O O N N 267
+PHE CB C N N 268
+PHE CG C Y N 269
+PHE CD1 C Y N 270
+PHE CD2 C Y N 271
+PHE CE1 C Y N 272
+PHE CE2 C Y N 273
+PHE CZ C Y N 274
+PHE OXT O N N 275
+PHE H H N N 276
+PHE H2 H N N 277
+PHE HA H N N 278
+PHE HB2 H N N 279
+PHE HB3 H N N 280
+PHE HD1 H N N 281
+PHE HD2 H N N 282
+PHE HE1 H N N 283
+PHE HE2 H N N 284
+PHE HZ H N N 285
+PHE HXT H N N 286
+PRO N N N N 287
+PRO CA C N S 288
+PRO C C N N 289
+PRO O O N N 290
+PRO CB C N N 291
+PRO CG C N N 292
+PRO CD C N N 293
+PRO OXT O N N 294
+PRO H H N N 295
+PRO HA H N N 296
+PRO HB2 H N N 297
+PRO HB3 H N N 298
+PRO HG2 H N N 299
+PRO HG3 H N N 300
+PRO HD2 H N N 301
+PRO HD3 H N N 302
+PRO HXT H N N 303
+SER N N N N 304
+SER CA C N S 305
+SER C C N N 306
+SER O O N N 307
+SER CB C N N 308
+SER OG O N N 309
+SER OXT O N N 310
+SER H H N N 311
+SER H2 H N N 312
+SER HA H N N 313
+SER HB2 H N N 314
+SER HB3 H N N 315
+SER HG H N N 316
+SER HXT H N N 317
+THR N N N N 318
+THR CA C N S 319
+THR C C N N 320
+THR O O N N 321
+THR CB C N R 322
+THR OG1 O N N 323
+THR CG2 C N N 324
+THR OXT O N N 325
+THR H H N N 326
+THR H2 H N N 327
+THR HA H N N 328
+THR HB H N N 329
+THR HG1 H N N 330
+THR HG21 H N N 331
+THR HG22 H N N 332
+THR HG23 H N N 333
+THR HXT H N N 334
+TYR N N N N 335
+TYR CA C N S 336
+TYR C C N N 337
+TYR O O N N 338
+TYR CB C N N 339
+TYR CG C Y N 340
+TYR CD1 C Y N 341
+TYR CD2 C Y N 342
+TYR CE1 C Y N 343
+TYR CE2 C Y N 344
+TYR CZ C Y N 345
+TYR OH O N N 346
+TYR OXT O N N 347
+TYR H H N N 348
+TYR H2 H N N 349
+TYR HA H N N 350
+TYR HB2 H N N 351
+TYR HB3 H N N 352
+TYR HD1 H N N 353
+TYR HD2 H N N 354
+TYR HE1 H N N 355
+TYR HE2 H N N 356
+TYR HH H N N 357
+TYR HXT H N N 358
+VAL N N N N 359
+VAL CA C N S 360
+VAL C C N N 361
+VAL O O N N 362
+VAL CB C N N 363
+VAL CG1 C N N 364
+VAL CG2 C N N 365
+VAL OXT O N N 366
+VAL H H N N 367
+VAL H2 H N N 368
+VAL HA H N N 369
+VAL HB H N N 370
+VAL HG11 H N N 371
+VAL HG12 H N N 372
+VAL HG13 H N N 373
+VAL HG21 H N N 374
+VAL HG22 H N N 375
+VAL HG23 H N N 376
+VAL HXT H N N 377
+#
+loop_
+_chem_comp_bond.comp_id
+_chem_comp_bond.atom_id_1
+_chem_comp_bond.atom_id_2
+_chem_comp_bond.value_order
+_chem_comp_bond.pdbx_aromatic_flag
+_chem_comp_bond.pdbx_stereo_config
+_chem_comp_bond.pdbx_ordinal
+ALA N CA sing N N 1
+ALA N H sing N N 2
+ALA N H2 sing N N 3
+ALA CA C sing N N 4
+ALA CA CB sing N N 5
+ALA CA HA sing N N 6
+ALA C O doub N N 7
+ALA C OXT sing N N 8
+ALA CB HB1 sing N N 9
+ALA CB HB2 sing N N 10
+ALA CB HB3 sing N N 11
+ALA OXT HXT sing N N 12
+ARG N CA sing N N 13
+ARG N H sing N N 14
+ARG N H2 sing N N 15
+ARG CA C sing N N 16
+ARG CA CB sing N N 17
+ARG CA HA sing N N 18
+ARG C O doub N N 19
+ARG C OXT sing N N 20
+ARG CB CG sing N N 21
+ARG CB HB2 sing N N 22
+ARG CB HB3 sing N N 23
+ARG CG CD sing N N 24
+ARG CG HG2 sing N N 25
+ARG CG HG3 sing N N 26
+ARG CD NE sing N N 27
+ARG CD HD2 sing N N 28
+ARG CD HD3 sing N N 29
+ARG NE CZ sing N N 30
+ARG NE HE sing N N 31
+ARG CZ NH1 sing N N 32
+ARG CZ NH2 doub N N 33
+ARG NH1 HH11 sing N N 34
+ARG NH1 HH12 sing N N 35
+ARG NH2 HH21 sing N N 36
+ARG NH2 HH22 sing N N 37
+ARG OXT HXT sing N N 38
+ASN N CA sing N N 39
+ASN N H sing N N 40
+ASN N H2 sing N N 41
+ASN CA C sing N N 42
+ASN CA CB sing N N 43
+ASN CA HA sing N N 44
+ASN C O doub N N 45
+ASN C OXT sing N N 46
+ASN CB CG sing N N 47
+ASN CB HB2 sing N N 48
+ASN CB HB3 sing N N 49
+ASN CG OD1 doub N N 50
+ASN CG ND2 sing N N 51
+ASN ND2 HD21 sing N N 52
+ASN ND2 HD22 sing N N 53
+ASN OXT HXT sing N N 54
+ASP N CA sing N N 55
+ASP N H sing N N 56
+ASP N H2 sing N N 57
+ASP CA C sing N N 58
+ASP CA CB sing N N 59
+ASP CA HA sing N N 60
+ASP C O doub N N 61
+ASP C OXT sing N N 62
+ASP CB CG sing N N 63
+ASP CB HB2 sing N N 64
+ASP CB HB3 sing N N 65
+ASP CG OD1 doub N N 66
+ASP CG OD2 sing N N 67
+ASP OD2 HD2 sing N N 68
+ASP OXT HXT sing N N 69
+CYS N CA sing N N 70
+CYS N H sing N N 71
+CYS N H2 sing N N 72
+CYS CA C sing N N 73
+CYS CA CB sing N N 74
+CYS CA HA sing N N 75
+CYS C O doub N N 76
+CYS C OXT sing N N 77
+CYS CB SG sing N N 78
+CYS CB HB2 sing N N 79
+CYS CB HB3 sing N N 80
+CYS SG HG sing N N 81
+CYS OXT HXT sing N N 82
+GLN N CA sing N N 83
+GLN N H sing N N 84
+GLN N H2 sing N N 85
+GLN CA C sing N N 86
+GLN CA CB sing N N 87
+GLN CA HA sing N N 88
+GLN C O doub N N 89
+GLN C OXT sing N N 90
+GLN CB CG sing N N 91
+GLN CB HB2 sing N N 92
+GLN CB HB3 sing N N 93
+GLN CG CD sing N N 94
+GLN CG HG2 sing N N 95
+GLN CG HG3 sing N N 96
+GLN CD OE1 doub N N 97
+GLN CD NE2 sing N N 98
+GLN NE2 HE21 sing N N 99
+GLN NE2 HE22 sing N N 100
+GLN OXT HXT sing N N 101
+GLU N CA sing N N 102
+GLU N H sing N N 103
+GLU N H2 sing N N 104
+GLU CA C sing N N 105
+GLU CA CB sing N N 106
+GLU CA HA sing N N 107
+GLU C O doub N N 108
+GLU C OXT sing N N 109
+GLU CB CG sing N N 110
+GLU CB HB2 sing N N 111
+GLU CB HB3 sing N N 112
+GLU CG CD sing N N 113
+GLU CG HG2 sing N N 114
+GLU CG HG3 sing N N 115
+GLU CD OE1 doub N N 116
+GLU CD OE2 sing N N 117
+GLU OE2 HE2 sing N N 118
+GLU OXT HXT sing N N 119
+GLY N CA sing N N 120
+GLY N H sing N N 121
+GLY N H2 sing N N 122
+GLY CA C sing N N 123
+GLY CA HA2 sing N N 124
+GLY CA HA3 sing N N 125
+GLY C O doub N N 126
+GLY C OXT sing N N 127
+GLY OXT HXT sing N N 128
+GOL C1 O1 sing N N 129
+GOL C1 C2 sing N N 130
+GOL C1 H11 sing N N 131
+GOL C1 H12 sing N N 132
+GOL O1 HO1 sing N N 133
+GOL C2 O2 sing N N 134
+GOL C2 C3 sing N N 135
+GOL C2 H2 sing N N 136
+GOL O2 HO2 sing N N 137
+GOL C3 O3 sing N N 138
+GOL C3 H31 sing N N 139
+GOL C3 H32 sing N N 140
+GOL O3 HO3 sing N N 141
+HIS N CA sing N N 142
+HIS N H sing N N 143
+HIS N H2 sing N N 144
+HIS CA C sing N N 145
+HIS CA CB sing N N 146
+HIS CA HA sing N N 147
+HIS C O doub N N 148
+HIS C OXT sing N N 149
+HIS CB CG sing N N 150
+HIS CB HB2 sing N N 151
+HIS CB HB3 sing N N 152
+HIS CG ND1 sing Y N 153
+HIS CG CD2 doub Y N 154
+HIS ND1 CE1 doub Y N 155
+HIS ND1 HD1 sing N N 156
+HIS CD2 NE2 sing Y N 157
+HIS CD2 HD2 sing N N 158
+HIS CE1 NE2 sing Y N 159
+HIS CE1 HE1 sing N N 160
+HIS NE2 HE2 sing N N 161
+HIS OXT HXT sing N N 162
+HOH O H1 sing N N 163
+HOH O H2 sing N N 164
+ILE N CA sing N N 165
+ILE N H sing N N 166
+ILE N H2 sing N N 167
+ILE CA C sing N N 168
+ILE CA CB sing N N 169
+ILE CA HA sing N N 170
+ILE C O doub N N 171
+ILE C OXT sing N N 172
+ILE CB CG1 sing N N 173
+ILE CB CG2 sing N N 174
+ILE CB HB sing N N 175
+ILE CG1 CD1 sing N N 176
+ILE CG1 HG12 sing N N 177
+ILE CG1 HG13 sing N N 178
+ILE CG2 HG21 sing N N 179
+ILE CG2 HG22 sing N N 180
+ILE CG2 HG23 sing N N 181
+ILE CD1 HD11 sing N N 182
+ILE CD1 HD12 sing N N 183
+ILE CD1 HD13 sing N N 184
+ILE OXT HXT sing N N 185
+LEU N CA sing N N 186
+LEU N H sing N N 187
+LEU N H2 sing N N 188
+LEU CA C sing N N 189
+LEU CA CB sing N N 190
+LEU CA HA sing N N 191
+LEU C O doub N N 192
+LEU C OXT sing N N 193
+LEU CB CG sing N N 194
+LEU CB HB2 sing N N 195
+LEU CB HB3 sing N N 196
+LEU CG CD1 sing N N 197
+LEU CG CD2 sing N N 198
+LEU CG HG sing N N 199
+LEU CD1 HD11 sing N N 200
+LEU CD1 HD12 sing N N 201
+LEU CD1 HD13 sing N N 202
+LEU CD2 HD21 sing N N 203
+LEU CD2 HD22 sing N N 204
+LEU CD2 HD23 sing N N 205
+LEU OXT HXT sing N N 206
+LYS N CA sing N N 207
+LYS N H sing N N 208
+LYS N H2 sing N N 209
+LYS CA C sing N N 210
+LYS CA CB sing N N 211
+LYS CA HA sing N N 212
+LYS C O doub N N 213
+LYS C OXT sing N N 214
+LYS CB CG sing N N 215
+LYS CB HB2 sing N N 216
+LYS CB HB3 sing N N 217
+LYS CG CD sing N N 218
+LYS CG HG2 sing N N 219
+LYS CG HG3 sing N N 220
+LYS CD CE sing N N 221
+LYS CD HD2 sing N N 222
+LYS CD HD3 sing N N 223
+LYS CE NZ sing N N 224
+LYS CE HE2 sing N N 225
+LYS CE HE3 sing N N 226
+LYS NZ HZ1 sing N N 227
+LYS NZ HZ2 sing N N 228
+LYS NZ HZ3 sing N N 229
+LYS OXT HXT sing N N 230
+MET N CA sing N N 231
+MET N H sing N N 232
+MET N H2 sing N N 233
+MET CA C sing N N 234
+MET CA CB sing N N 235
+MET CA HA sing N N 236
+MET C O doub N N 237
+MET C OXT sing N N 238
+MET CB CG sing N N 239
+MET CB HB2 sing N N 240
+MET CB HB3 sing N N 241
+MET CG SD sing N N 242
+MET CG HG2 sing N N 243
+MET CG HG3 sing N N 244
+MET SD CE sing N N 245
+MET CE HE1 sing N N 246
+MET CE HE2 sing N N 247
+MET CE HE3 sing N N 248
+MET OXT HXT sing N N 249
+PHE N CA sing N N 250
+PHE N H sing N N 251
+PHE N H2 sing N N 252
+PHE CA C sing N N 253
+PHE CA CB sing N N 254
+PHE CA HA sing N N 255
+PHE C O doub N N 256
+PHE C OXT sing N N 257
+PHE CB CG sing N N 258
+PHE CB HB2 sing N N 259
+PHE CB HB3 sing N N 260
+PHE CG CD1 doub Y N 261
+PHE CG CD2 sing Y N 262
+PHE CD1 CE1 sing Y N 263
+PHE CD1 HD1 sing N N 264
+PHE CD2 CE2 doub Y N 265
+PHE CD2 HD2 sing N N 266
+PHE CE1 CZ doub Y N 267
+PHE CE1 HE1 sing N N 268
+PHE CE2 CZ sing Y N 269
+PHE CE2 HE2 sing N N 270
+PHE CZ HZ sing N N 271
+PHE OXT HXT sing N N 272
+PRO N CA sing N N 273
+PRO N CD sing N N 274
+PRO N H sing N N 275
+PRO CA C sing N N 276
+PRO CA CB sing N N 277
+PRO CA HA sing N N 278
+PRO C O doub N N 279
+PRO C OXT sing N N 280
+PRO CB CG sing N N 281
+PRO CB HB2 sing N N 282
+PRO CB HB3 sing N N 283
+PRO CG CD sing N N 284
+PRO CG HG2 sing N N 285
+PRO CG HG3 sing N N 286
+PRO CD HD2 sing N N 287
+PRO CD HD3 sing N N 288
+PRO OXT HXT sing N N 289
+SER N CA sing N N 290
+SER N H sing N N 291
+SER N H2 sing N N 292
+SER CA C sing N N 293
+SER CA CB sing N N 294
+SER CA HA sing N N 295
+SER C O doub N N 296
+SER C OXT sing N N 297
+SER CB OG sing N N 298
+SER CB HB2 sing N N 299
+SER CB HB3 sing N N 300
+SER OG HG sing N N 301
+SER OXT HXT sing N N 302
+THR N CA sing N N 303
+THR N H sing N N 304
+THR N H2 sing N N 305
+THR CA C sing N N 306
+THR CA CB sing N N 307
+THR CA HA sing N N 308
+THR C O doub N N 309
+THR C OXT sing N N 310
+THR CB OG1 sing N N 311
+THR CB CG2 sing N N 312
+THR CB HB sing N N 313
+THR OG1 HG1 sing N N 314
+THR CG2 HG21 sing N N 315
+THR CG2 HG22 sing N N 316
+THR CG2 HG23 sing N N 317
+THR OXT HXT sing N N 318
+TYR N CA sing N N 319
+TYR N H sing N N 320
+TYR N H2 sing N N 321
+TYR CA C sing N N 322
+TYR CA CB sing N N 323
+TYR CA HA sing N N 324
+TYR C O doub N N 325
+TYR C OXT sing N N 326
+TYR CB CG sing N N 327
+TYR CB HB2 sing N N 328
+TYR CB HB3 sing N N 329
+TYR CG CD1 doub Y N 330
+TYR CG CD2 sing Y N 331
+TYR CD1 CE1 sing Y N 332
+TYR CD1 HD1 sing N N 333
+TYR CD2 CE2 doub Y N 334
+TYR CD2 HD2 sing N N 335
+TYR CE1 CZ doub Y N 336
+TYR CE1 HE1 sing N N 337
+TYR CE2 CZ sing Y N 338
+TYR CE2 HE2 sing N N 339
+TYR CZ OH sing N N 340
+TYR OH HH sing N N 341
+TYR OXT HXT sing N N 342
+VAL N CA sing N N 343
+VAL N H sing N N 344
+VAL N H2 sing N N 345
+VAL CA C sing N N 346
+VAL CA CB sing N N 347
+VAL CA HA sing N N 348
+VAL C O doub N N 349
+VAL C OXT sing N N 350
+VAL CB CG1 sing N N 351
+VAL CB CG2 sing N N 352
+VAL CB HB sing N N 353
+VAL CG1 HG11 sing N N 354
+VAL CG1 HG12 sing N N 355
+VAL CG1 HG13 sing N N 356
+VAL CG2 HG21 sing N N 357
+VAL CG2 HG22 sing N N 358
+VAL CG2 HG23 sing N N 359
+VAL OXT HXT sing N N 360
+#
+loop_
+_pdbx_entity_nonpoly.entity_id
+_pdbx_entity_nonpoly.name
+_pdbx_entity_nonpoly.comp_id
+2 GLYCEROL GOL
+3 water HOH
+#
+_pdbx_initial_refinement_model.id 1
+_pdbx_initial_refinement_model.entity_id_list ?
+_pdbx_initial_refinement_model.type 'experimental model'
+_pdbx_initial_refinement_model.source_name PDB
+_pdbx_initial_refinement_model.accession_code 2XDD
+_pdbx_initial_refinement_model.details 'PDB ENTRY 2XDD'
+#