data_7IAJ
# 
_entry.id   7IAJ 
# 
_audit_conform.dict_name       mmcif_pdbx.dic 
_audit_conform.dict_version    5.403 
_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   7IAJ         pdb_00007iaj 10.2210/pdb7iaj/pdb 
WWPDB D_1001408522 ?            ?                   
# 
_pdbx_audit_revision_history.ordinal             1 
_pdbx_audit_revision_history.data_content_type   'Structure model' 
_pdbx_audit_revision_history.major_revision      1 
_pdbx_audit_revision_history.minor_revision      0 
_pdbx_audit_revision_history.revision_date       2025-04-23 
_pdbx_audit_revision_history.part_number         ? 
# 
_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             ? 
# 
_pdbx_database_status.entry_id                        7IAJ 
_pdbx_database_status.status_code                     REL 
_pdbx_database_status.status_code_sf                  REL 
_pdbx_database_status.status_code_mr                  ? 
_pdbx_database_status.status_code_cs                  ? 
_pdbx_database_status.recvd_initial_deposition_date   2025-04-10 
_pdbx_database_status.status_code_nmr_data            ? 
_pdbx_database_status.deposit_site                    RCSB 
_pdbx_database_status.process_site                    RCSB 
_pdbx_database_status.SG_entry                        ? 
_pdbx_database_status.pdb_format_compatible           N 
_pdbx_database_status.methods_development_category    ? 
# 
_pdbx_contact_author.id                 1 
_pdbx_contact_author.email              frankfurt.von-delft@diamond.ac.uk 
_pdbx_contact_author.name_first         Frank 
_pdbx_contact_author.name_last          'von Delft' 
_pdbx_contact_author.role               'principal investigator/group leader' 
_pdbx_contact_author.identifier_ORCID   0000-0003-0378-0017 
_pdbx_contact_author.name_mi            ? 
# 
loop_
_audit_author.name 
_audit_author.pdbx_ordinal 
_audit_author.identifier_ORCID 
'Ni, X.'              1  ? 
'Marples, P.G.'       2  ? 
'Godoy, A.S.'         3  ? 
'Koekemoer, L.'       4  ? 
'Aschenbrenner, J.C.' 5  ? 
'Balcomb, B.H.'       6  ? 
'Fairhead, M.'        7  ? 
'Lithgo, R.M.'        8  ? 
'Lee, A.'             9  ? 
'Kenton, N.'          10 ? 
'Thompson, W.'        11 ? 
'Tomlinson, C.W.E.'   12 ? 
'Wild, C.'            13 ? 
'Winokan, M.'         14 ? 
'Williams, E.P.'      15 ? 
'Chandran, A.V.'      16 ? 
'Walsh, M.A.'         17 ? 
'Fearon, D.'          18 ? 
'von Delft, F.'       19 ? 
# 
_citation.id                        primary 
_citation.title                     
'Group deposition of ZIKV NS2B-NS3 protease in complex with inhibitors from ASAP Discovery Consortium' 
_citation.journal_abbrev            'To Be Published' 
_citation.journal_volume            ? 
_citation.page_first                ? 
_citation.page_last                 ? 
_citation.year                      ? 
_citation.journal_id_ASTM           ? 
_citation.country                   ? 
_citation.journal_id_ISSN           ? 
_citation.journal_id_CSD            0353 
_citation.book_publisher            ? 
_citation.pdbx_database_id_PubMed   ? 
_citation.pdbx_database_id_DOI      ? 
# 
loop_
_citation_author.citation_id 
_citation_author.name 
_citation_author.identifier_ORCID 
_citation_author.ordinal 
primary 'Ni, X.'              ? 1  
primary 'Marples, P.G.'       ? 2  
primary 'Godoy, A.S.'         ? 3  
primary 'Koekemoer, L.'       ? 4  
primary 'Aschenbrenner, J.C.' ? 5  
primary 'Balcomb, B.H.'       ? 6  
primary 'Fairhead, M.'        ? 7  
primary 'Lithgo, R.M.'        ? 8  
primary 'Lee, A.'             ? 9  
primary 'Kenton, N.'          ? 10 
primary 'Thompson, W.'        ? 11 
primary 'Tomlinson, C.W.E.'   ? 12 
primary 'Wild, C.'            ? 13 
primary 'Winokan, M.'         ? 14 
primary 'Williams, E.P.'      ? 15 
primary 'Chandran, A.V.'      ? 16 
primary 'Walsh, M.A.'         ? 17 
primary 'Fearon, D.'          ? 18 
primary 'von Delft, F.'       ? 19 
# 
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 'Serine protease subunit NS2B'                                                      5067.486  1  ? ?    ? ? 
2 polymer     man 'Serine protease NS3'                                                               18117.629 1  
3.4.21.91,3.6.1.15,3.6.4.13 None ? ? 
3 non-polymer syn 'DIMETHYL SULFOXIDE'                                                                78.133    1  ? ?    ? ? 
4 non-polymer syn '6-chloro-N-(2,3-dihydro-1H-isoindol-5-yl)-1H-pyrrolo[2,3-b]pyridine-4-carboxamide' 312.754   1  ? ?    ? ? 
5 water       nat water                                                                               18.015    74 ? ?    ? ? 
# 
loop_
_entity_name_com.entity_id 
_entity_name_com.name 
1 'Flavivirin protease NS2B regulatory subunit,Non-structural protein 2B' 
2 'Flavivirin protease NS3 catalytic subunit,Non-structural protein 3'    
# 
loop_
_entity_poly.entity_id 
_entity_poly.type 
_entity_poly.nstd_linkage 
_entity_poly.nstd_monomer 
_entity_poly.pdbx_seq_one_letter_code 
_entity_poly.pdbx_seq_one_letter_code_can 
_entity_poly.pdbx_strand_id 
_entity_poly.pdbx_target_identifier 
1 'polypeptide(L)' no no SMGKSVDMYIERAGDITWEKDAEVTGNSPRLDVALDESGDFSLVEE SMGKSVDMYIERAGDITWEKDAEVTGNSPRLDVALDESGDFSLVEE A ? 
2 'polypeptide(L)' no no 
;MKEVKKGETTDGVYRVMTRRLLGSTQVGVGVMQEGVFHTMWHVTKGAALRSGEGRLDPYWGDVKQDLVSYCGPWKLDAAW
DGLSEVQLLAVPPGERAKNIQTLPGIFKTKDGDIGAVALDYPAGTSGSPILDKCGRVIGLYGNGVVIKNGSYVSAITQGK
REEETPVE
;
;MKEVKKGETTDGVYRVMTRRLLGSTQVGVGVMQEGVFHTMWHVTKGAALRSGEGRLDPYWGDVKQDLVSYCGPWKLDAAW
DGLSEVQLLAVPPGERAKNIQTLPGIFKTKDGDIGAVALDYPAGTSGSPILDKCGRVIGLYGNGVVIKNGSYVSAITQGK
REEETPVE
;
B ? 
# 
loop_
_pdbx_entity_nonpoly.entity_id 
_pdbx_entity_nonpoly.name 
_pdbx_entity_nonpoly.comp_id 
3 'DIMETHYL SULFOXIDE'                                                                DMS   
4 '6-chloro-N-(2,3-dihydro-1H-isoindol-5-yl)-1H-pyrrolo[2,3-b]pyridine-4-carboxamide' A1B82 
5 water                                                                               HOH   
# 
loop_
_entity_poly_seq.entity_id 
_entity_poly_seq.num 
_entity_poly_seq.mon_id 
_entity_poly_seq.hetero 
1 1   SER n 
1 2   MET n 
1 3   GLY n 
1 4   LYS n 
1 5   SER n 
1 6   VAL n 
1 7   ASP n 
1 8   MET n 
1 9   TYR n 
1 10  ILE n 
1 11  GLU n 
1 12  ARG n 
1 13  ALA n 
1 14  GLY n 
1 15  ASP n 
1 16  ILE n 
1 17  THR n 
1 18  TRP n 
1 19  GLU n 
1 20  LYS n 
1 21  ASP n 
1 22  ALA n 
1 23  GLU n 
1 24  VAL n 
1 25  THR n 
1 26  GLY n 
1 27  ASN n 
1 28  SER n 
1 29  PRO n 
1 30  ARG n 
1 31  LEU n 
1 32  ASP n 
1 33  VAL n 
1 34  ALA n 
1 35  LEU n 
1 36  ASP n 
1 37  GLU n 
1 38  SER n 
1 39  GLY n 
1 40  ASP n 
1 41  PHE n 
1 42  SER n 
1 43  LEU n 
1 44  VAL n 
1 45  GLU n 
1 46  GLU n 
2 1   MET n 
2 2   LYS n 
2 3   GLU n 
2 4   VAL n 
2 5   LYS n 
2 6   LYS n 
2 7   GLY n 
2 8   GLU n 
2 9   THR n 
2 10  THR n 
2 11  ASP n 
2 12  GLY n 
2 13  VAL n 
2 14  TYR n 
2 15  ARG n 
2 16  VAL n 
2 17  MET n 
2 18  THR n 
2 19  ARG n 
2 20  ARG n 
2 21  LEU n 
2 22  LEU n 
2 23  GLY n 
2 24  SER n 
2 25  THR n 
2 26  GLN n 
2 27  VAL n 
2 28  GLY n 
2 29  VAL n 
2 30  GLY n 
2 31  VAL n 
2 32  MET n 
2 33  GLN n 
2 34  GLU n 
2 35  GLY n 
2 36  VAL n 
2 37  PHE n 
2 38  HIS n 
2 39  THR n 
2 40  MET n 
2 41  TRP n 
2 42  HIS n 
2 43  VAL n 
2 44  THR n 
2 45  LYS n 
2 46  GLY n 
2 47  ALA n 
2 48  ALA n 
2 49  LEU n 
2 50  ARG n 
2 51  SER n 
2 52  GLY n 
2 53  GLU n 
2 54  GLY n 
2 55  ARG n 
2 56  LEU n 
2 57  ASP n 
2 58  PRO n 
2 59  TYR n 
2 60  TRP n 
2 61  GLY n 
2 62  ASP n 
2 63  VAL n 
2 64  LYS n 
2 65  GLN n 
2 66  ASP n 
2 67  LEU n 
2 68  VAL n 
2 69  SER n 
2 70  TYR n 
2 71  CYS n 
2 72  GLY n 
2 73  PRO n 
2 74  TRP n 
2 75  LYS n 
2 76  LEU n 
2 77  ASP n 
2 78  ALA n 
2 79  ALA n 
2 80  TRP n 
2 81  ASP n 
2 82  GLY n 
2 83  LEU n 
2 84  SER n 
2 85  GLU n 
2 86  VAL n 
2 87  GLN n 
2 88  LEU n 
2 89  LEU n 
2 90  ALA n 
2 91  VAL n 
2 92  PRO n 
2 93  PRO n 
2 94  GLY n 
2 95  GLU n 
2 96  ARG n 
2 97  ALA n 
2 98  LYS n 
2 99  ASN n 
2 100 ILE n 
2 101 GLN n 
2 102 THR n 
2 103 LEU n 
2 104 PRO n 
2 105 GLY n 
2 106 ILE n 
2 107 PHE n 
2 108 LYS n 
2 109 THR n 
2 110 LYS n 
2 111 ASP n 
2 112 GLY n 
2 113 ASP n 
2 114 ILE n 
2 115 GLY n 
2 116 ALA n 
2 117 VAL n 
2 118 ALA n 
2 119 LEU n 
2 120 ASP n 
2 121 TYR n 
2 122 PRO n 
2 123 ALA n 
2 124 GLY n 
2 125 THR n 
2 126 SER n 
2 127 GLY n 
2 128 SER n 
2 129 PRO n 
2 130 ILE n 
2 131 LEU n 
2 132 ASP n 
2 133 LYS n 
2 134 CYS n 
2 135 GLY n 
2 136 ARG n 
2 137 VAL n 
2 138 ILE n 
2 139 GLY n 
2 140 LEU n 
2 141 TYR n 
2 142 GLY n 
2 143 ASN n 
2 144 GLY n 
2 145 VAL n 
2 146 VAL n 
2 147 ILE n 
2 148 LYS n 
2 149 ASN n 
2 150 GLY n 
2 151 SER n 
2 152 TYR n 
2 153 VAL n 
2 154 SER n 
2 155 ALA n 
2 156 ILE n 
2 157 THR n 
2 158 GLN n 
2 159 GLY n 
2 160 LYS n 
2 161 ARG n 
2 162 GLU n 
2 163 GLU n 
2 164 GLU n 
2 165 THR n 
2 166 PRO n 
2 167 VAL n 
2 168 GLU n 
# 
loop_
_entity_src_gen.entity_id 
_entity_src_gen.pdbx_src_id 
_entity_src_gen.pdbx_alt_source_flag 
_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 
_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 
_entity_src_gen.pdbx_gene_src_ncbi_taxonomy_id 
_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 
_entity_src_gen.pdbx_host_org_ncbi_taxonomy_id 
_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 
_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 
_entity_src_gen.pdbx_host_org_vector 
_entity_src_gen.host_org_details 
_entity_src_gen.expression_system_id 
_entity_src_gen.plasmid_name 
_entity_src_gen.plasmid_details 
_entity_src_gen.pdbx_description 
1 1 sample 'Biological sequence' 1 46  ? ? ? ? ? ? ? ? ? 'Zika virus' 64320 ? ? ? ? ? ? ? ? 'Escherichia coli' 562 ? ? ? ? ? ? ? ? 
? ? ? ? ? ? ? ? ? ? ? ? ? 
2 1 sample 'Biological sequence' 1 168 ? ? ? ? ? ? ? ? ? 'Zika virus' 64320 ? ? ? ? ? ? ? ? 'Escherichia coli' 562 ? ? ? ? ? ? ? ? 
? ? ? ? ? ? ? ? ? ? ? ? ? 
# 
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 
A1B82 non-polymer         . '6-chloro-N-(2,3-dihydro-1H-isoindol-5-yl)-1H-pyrrolo[2,3-b]pyridine-4-carboxamide' ? 
'C16 H13 Cl N4 O' 312.754 
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 
DMS   non-polymer         . 'DIMETHYL SULFOXIDE'                                                                ? 'C2 H6 O S' 
78.133  
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  
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 
TRP   'L-peptide linking' y TRYPTOPHAN                                                                          ? 'C11 H12 N2 O2' 
204.225 
TYR   'L-peptide linking' y TYROSINE                                                                            ? 'C9 H11 N O3' 
181.189 
VAL   'L-peptide linking' y VALINE                                                                              ? 'C5 H11 N O2' 
117.146 
# 
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   SER 1   44  ?   ?   ?   A . n 
A 1 2   MET 2   45  ?   ?   ?   A . n 
A 1 3   GLY 3   46  ?   ?   ?   A . n 
A 1 4   LYS 4   47  ?   ?   ?   A . n 
A 1 5   SER 5   48  ?   ?   ?   A . n 
A 1 6   VAL 6   49  ?   ?   ?   A . n 
A 1 7   ASP 7   50  50  ASP ASP A . n 
A 1 8   MET 8   51  51  MET MET A . n 
A 1 9   TYR 9   52  52  TYR TYR A . n 
A 1 10  ILE 10  53  53  ILE ILE A . n 
A 1 11  GLU 11  54  54  GLU GLU A . n 
A 1 12  ARG 12  55  55  ARG ARG A . n 
A 1 13  ALA 13  56  56  ALA ALA A . n 
A 1 14  GLY 14  57  57  GLY GLY A . n 
A 1 15  ASP 15  58  58  ASP ASP A . n 
A 1 16  ILE 16  59  59  ILE ILE A . n 
A 1 17  THR 17  60  60  THR THR A . n 
A 1 18  TRP 18  61  61  TRP TRP A . n 
A 1 19  GLU 19  62  62  GLU GLU A . n 
A 1 20  LYS 20  63  63  LYS LYS A . n 
A 1 21  ASP 21  64  64  ASP ASP A . n 
A 1 22  ALA 22  65  65  ALA ALA A . n 
A 1 23  GLU 23  66  66  GLU GLU A . n 
A 1 24  VAL 24  67  67  VAL VAL A . n 
A 1 25  THR 25  68  68  THR THR A . n 
A 1 26  GLY 26  69  69  GLY GLY A . n 
A 1 27  ASN 27  70  70  ASN ASN A . n 
A 1 28  SER 28  71  71  SER SER A . n 
A 1 29  PRO 29  72  72  PRO PRO A . n 
A 1 30  ARG 30  73  73  ARG ARG A . n 
A 1 31  LEU 31  74  74  LEU LEU A . n 
A 1 32  ASP 32  75  75  ASP ASP A . n 
A 1 33  VAL 33  76  76  VAL VAL A . n 
A 1 34  ALA 34  77  77  ALA ALA A . n 
A 1 35  LEU 35  78  78  LEU LEU A . n 
A 1 36  ASP 36  79  79  ASP ASP A . n 
A 1 37  GLU 37  80  80  GLU GLU A . n 
A 1 38  SER 38  81  81  SER SER A . n 
A 1 39  GLY 39  82  82  GLY GLY A . n 
A 1 40  ASP 40  83  83  ASP ASP A . n 
A 1 41  PHE 41  84  84  PHE PHE A . n 
A 1 42  SER 42  85  85  SER SER A . n 
A 1 43  LEU 43  86  86  LEU LEU A . n 
A 1 44  VAL 44  87  87  VAL VAL A . n 
A 1 45  GLU 45  88  88  GLU GLU A . n 
A 1 46  GLU 46  89  ?   ?   ?   A . n 
B 2 1   MET 1   10  ?   ?   ?   B . n 
B 2 2   LYS 2   11  ?   ?   ?   B . n 
B 2 3   GLU 3   12  ?   ?   ?   B . n 
B 2 4   VAL 4   13  ?   ?   ?   B . n 
B 2 5   LYS 5   14  ?   ?   ?   B . n 
B 2 6   LYS 6   15  ?   ?   ?   B . n 
B 2 7   GLY 7   16  ?   ?   ?   B . n 
B 2 8   GLU 8   17  ?   ?   ?   B . n 
B 2 9   THR 9   18  18  THR THR B . n 
B 2 10  THR 10  19  19  THR THR B . n 
B 2 11  ASP 11  20  20  ASP ASP B . n 
B 2 12  GLY 12  21  21  GLY GLY B . n 
B 2 13  VAL 13  22  22  VAL VAL B . n 
B 2 14  TYR 14  23  23  TYR TYR B . n 
B 2 15  ARG 15  24  24  ARG ARG B . n 
B 2 16  VAL 16  25  25  VAL VAL B . n 
B 2 17  MET 17  26  26  MET MET B . n 
B 2 18  THR 18  27  27  THR THR B . n 
B 2 19  ARG 19  28  28  ARG ARG B . n 
B 2 20  ARG 20  29  29  ARG ARG B . n 
B 2 21  LEU 21  30  30  LEU LEU B . n 
B 2 22  LEU 22  31  31  LEU LEU B . n 
B 2 23  GLY 23  32  32  GLY GLY B . n 
B 2 24  SER 24  33  33  SER SER B . n 
B 2 25  THR 25  34  34  THR THR B . n 
B 2 26  GLN 26  35  35  GLN GLN B . n 
B 2 27  VAL 27  36  36  VAL VAL B . n 
B 2 28  GLY 28  37  37  GLY GLY B . n 
B 2 29  VAL 29  38  38  VAL VAL B . n 
B 2 30  GLY 30  39  39  GLY GLY B . n 
B 2 31  VAL 31  40  40  VAL VAL B . n 
B 2 32  MET 32  41  41  MET MET B . n 
B 2 33  GLN 33  42  42  GLN GLN B . n 
B 2 34  GLU 34  43  43  GLU GLU B . n 
B 2 35  GLY 35  44  44  GLY GLY B . n 
B 2 36  VAL 36  45  45  VAL VAL B . n 
B 2 37  PHE 37  46  46  PHE PHE B . n 
B 2 38  HIS 38  47  47  HIS HIS B . n 
B 2 39  THR 39  48  48  THR THR B . n 
B 2 40  MET 40  49  49  MET MET B . n 
B 2 41  TRP 41  50  50  TRP TRP B . n 
B 2 42  HIS 42  51  51  HIS HIS B . n 
B 2 43  VAL 43  52  52  VAL VAL B . n 
B 2 44  THR 44  53  53  THR THR B . n 
B 2 45  LYS 45  54  54  LYS LYS B . n 
B 2 46  GLY 46  55  55  GLY GLY B . n 
B 2 47  ALA 47  56  56  ALA ALA B . n 
B 2 48  ALA 48  57  57  ALA ALA B . n 
B 2 49  LEU 49  58  58  LEU LEU B . n 
B 2 50  ARG 50  59  59  ARG ARG B . n 
B 2 51  SER 51  60  60  SER SER B . n 
B 2 52  GLY 52  61  61  GLY GLY B . n 
B 2 53  GLU 53  62  62  GLU GLU B . n 
B 2 54  GLY 54  63  63  GLY GLY B . n 
B 2 55  ARG 55  64  64  ARG ARG B . n 
B 2 56  LEU 56  65  65  LEU LEU B . n 
B 2 57  ASP 57  66  66  ASP ASP B . n 
B 2 58  PRO 58  67  67  PRO PRO B . n 
B 2 59  TYR 59  68  68  TYR TYR B . n 
B 2 60  TRP 60  69  69  TRP TRP B . n 
B 2 61  GLY 61  70  70  GLY GLY B . n 
B 2 62  ASP 62  71  71  ASP ASP B . n 
B 2 63  VAL 63  72  72  VAL VAL B . n 
B 2 64  LYS 64  73  73  LYS LYS B . n 
B 2 65  GLN 65  74  74  GLN GLN B . n 
B 2 66  ASP 66  75  75  ASP ASP B . n 
B 2 67  LEU 67  76  76  LEU LEU B . n 
B 2 68  VAL 68  77  77  VAL VAL B . n 
B 2 69  SER 69  78  78  SER SER B . n 
B 2 70  TYR 70  79  79  TYR TYR B . n 
B 2 71  CYS 71  80  80  CYS CYS B . n 
B 2 72  GLY 72  81  81  GLY GLY B . n 
B 2 73  PRO 73  82  82  PRO PRO B . n 
B 2 74  TRP 74  83  83  TRP TRP B . n 
B 2 75  LYS 75  84  84  LYS LYS B . n 
B 2 76  LEU 76  85  85  LEU LEU B . n 
B 2 77  ASP 77  86  86  ASP ASP B . n 
B 2 78  ALA 78  87  87  ALA ALA B . n 
B 2 79  ALA 79  88  88  ALA ALA B . n 
B 2 80  TRP 80  89  89  TRP TRP B . n 
B 2 81  ASP 81  90  90  ASP ASP B . n 
B 2 82  GLY 82  91  91  GLY GLY B . n 
B 2 83  LEU 83  92  92  LEU LEU B . n 
B 2 84  SER 84  93  93  SER SER B . n 
B 2 85  GLU 85  94  94  GLU GLU B . n 
B 2 86  VAL 86  95  95  VAL VAL B . n 
B 2 87  GLN 87  96  96  GLN GLN B . n 
B 2 88  LEU 88  97  97  LEU LEU B . n 
B 2 89  LEU 89  98  98  LEU LEU B . n 
B 2 90  ALA 90  99  99  ALA ALA B . n 
B 2 91  VAL 91  100 100 VAL VAL B . n 
B 2 92  PRO 92  101 101 PRO PRO B . n 
B 2 93  PRO 93  102 102 PRO PRO B . n 
B 2 94  GLY 94  103 103 GLY GLY B . n 
B 2 95  GLU 95  104 104 GLU GLU B . n 
B 2 96  ARG 96  105 105 ARG ARG B . n 
B 2 97  ALA 97  106 106 ALA ALA B . n 
B 2 98  LYS 98  107 107 LYS LYS B . n 
B 2 99  ASN 99  108 108 ASN ASN B . n 
B 2 100 ILE 100 109 109 ILE ILE B . n 
B 2 101 GLN 101 110 110 GLN GLN B . n 
B 2 102 THR 102 111 111 THR THR B . n 
B 2 103 LEU 103 112 112 LEU LEU B . n 
B 2 104 PRO 104 113 113 PRO PRO B . n 
B 2 105 GLY 105 114 114 GLY GLY B . n 
B 2 106 ILE 106 115 115 ILE ILE B . n 
B 2 107 PHE 107 116 116 PHE PHE B . n 
B 2 108 LYS 108 117 117 LYS LYS B . n 
B 2 109 THR 109 118 118 THR THR B . n 
B 2 110 LYS 110 119 119 LYS LYS B . n 
B 2 111 ASP 111 120 120 ASP ASP B . n 
B 2 112 GLY 112 121 121 GLY GLY B . n 
B 2 113 ASP 113 122 122 ASP ASP B . n 
B 2 114 ILE 114 123 123 ILE ILE B . n 
B 2 115 GLY 115 124 124 GLY GLY B . n 
B 2 116 ALA 116 125 125 ALA ALA B . n 
B 2 117 VAL 117 126 126 VAL VAL B . n 
B 2 118 ALA 118 127 127 ALA ALA B . n 
B 2 119 LEU 119 128 128 LEU LEU B . n 
B 2 120 ASP 120 129 129 ASP ASP B . n 
B 2 121 TYR 121 130 130 TYR TYR B . n 
B 2 122 PRO 122 131 131 PRO PRO B . n 
B 2 123 ALA 123 132 132 ALA ALA B . n 
B 2 124 GLY 124 133 133 GLY GLY B . n 
B 2 125 THR 125 134 134 THR THR B . n 
B 2 126 SER 126 135 135 SER SER B . n 
B 2 127 GLY 127 136 136 GLY GLY B . n 
B 2 128 SER 128 137 137 SER SER B . n 
B 2 129 PRO 129 138 138 PRO PRO B . n 
B 2 130 ILE 130 139 139 ILE ILE B . n 
B 2 131 LEU 131 140 140 LEU LEU B . n 
B 2 132 ASP 132 141 141 ASP ASP B . n 
B 2 133 LYS 133 142 142 LYS LYS B . n 
B 2 134 CYS 134 143 143 CYS CYS B . n 
B 2 135 GLY 135 144 144 GLY GLY B . n 
B 2 136 ARG 136 145 145 ARG ARG B . n 
B 2 137 VAL 137 146 146 VAL VAL B . n 
B 2 138 ILE 138 147 147 ILE ILE B . n 
B 2 139 GLY 139 148 148 GLY GLY B . n 
B 2 140 LEU 140 149 149 LEU LEU B . n 
B 2 141 TYR 141 150 150 TYR TYR B . n 
B 2 142 GLY 142 151 151 GLY GLY B . n 
B 2 143 ASN 143 152 152 ASN ASN B . n 
B 2 144 GLY 144 153 153 GLY GLY B . n 
B 2 145 VAL 145 154 154 VAL VAL B . n 
B 2 146 VAL 146 155 155 VAL VAL B . n 
B 2 147 ILE 147 156 156 ILE ILE B . n 
B 2 148 LYS 148 157 157 LYS LYS B . n 
B 2 149 ASN 149 158 158 ASN ASN B . n 
B 2 150 GLY 150 159 159 GLY GLY B . n 
B 2 151 SER 151 160 160 SER SER B . n 
B 2 152 TYR 152 161 161 TYR TYR B . n 
B 2 153 VAL 153 162 162 VAL VAL B . n 
B 2 154 SER 154 163 163 SER SER B . n 
B 2 155 ALA 155 164 164 ALA ALA B . n 
B 2 156 ILE 156 165 165 ILE ILE B . n 
B 2 157 THR 157 166 166 THR THR B . n 
B 2 158 GLN 158 167 167 GLN GLN B . n 
B 2 159 GLY 159 168 168 GLY GLY B . n 
B 2 160 LYS 160 169 169 LYS LYS B . n 
B 2 161 ARG 161 170 170 ARG ARG B . n 
B 2 162 GLU 162 171 171 GLU GLU B . n 
B 2 163 GLU 163 172 ?   ?   ?   B . n 
B 2 164 GLU 164 173 ?   ?   ?   B . n 
B 2 165 THR 165 174 ?   ?   ?   B . n 
B 2 166 PRO 166 175 ?   ?   ?   B . n 
B 2 167 VAL 167 176 ?   ?   ?   B . n 
B 2 168 GLU 168 177 ?   ?   ?   B . 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 
C 3 DMS   1  201 202 DMS   DMS B . 
D 4 A1B82 1  202 203 A1B82 LIG B . 
E 5 HOH   1  101 118 HOH   HOH A . 
E 5 HOH   2  102 48  HOH   HOH A . 
E 5 HOH   3  103 34  HOH   HOH A . 
E 5 HOH   4  104 117 HOH   HOH A . 
E 5 HOH   5  105 16  HOH   HOH A . 
E 5 HOH   6  106 98  HOH   HOH A . 
E 5 HOH   7  107 20  HOH   HOH A . 
E 5 HOH   8  108 65  HOH   HOH A . 
E 5 HOH   9  109 28  HOH   HOH A . 
E 5 HOH   10 110 121 HOH   HOH A . 
E 5 HOH   11 111 83  HOH   HOH A . 
E 5 HOH   12 112 119 HOH   HOH A . 
E 5 HOH   13 113 40  HOH   HOH A . 
E 5 HOH   14 114 120 HOH   HOH A . 
E 5 HOH   15 115 12  HOH   HOH A . 
E 5 HOH   16 116 70  HOH   HOH A . 
F 5 HOH   1  301 14  HOH   HOH B . 
F 5 HOH   2  302 5   HOH   HOH B . 
F 5 HOH   3  303 1   HOH   HOH B . 
F 5 HOH   4  304 100 HOH   HOH B . 
F 5 HOH   5  305 4   HOH   HOH B . 
F 5 HOH   6  306 92  HOH   HOH B . 
F 5 HOH   7  307 58  HOH   HOH B . 
F 5 HOH   8  308 68  HOH   HOH B . 
F 5 HOH   9  309 11  HOH   HOH B . 
F 5 HOH   10 310 61  HOH   HOH B . 
F 5 HOH   11 311 54  HOH   HOH B . 
F 5 HOH   12 312 36  HOH   HOH B . 
F 5 HOH   13 313 32  HOH   HOH B . 
F 5 HOH   14 314 31  HOH   HOH B . 
F 5 HOH   15 315 136 HOH   HOH B . 
F 5 HOH   16 316 2   HOH   HOH B . 
F 5 HOH   17 317 9   HOH   HOH B . 
F 5 HOH   18 318 63  HOH   HOH B . 
F 5 HOH   19 319 129 HOH   HOH B . 
F 5 HOH   20 320 131 HOH   HOH B . 
F 5 HOH   21 321 90  HOH   HOH B . 
F 5 HOH   22 322 13  HOH   HOH B . 
F 5 HOH   23 323 30  HOH   HOH B . 
F 5 HOH   24 324 10  HOH   HOH B . 
F 5 HOH   25 325 116 HOH   HOH B . 
F 5 HOH   26 326 56  HOH   HOH B . 
F 5 HOH   27 327 128 HOH   HOH B . 
F 5 HOH   28 328 35  HOH   HOH B . 
F 5 HOH   29 329 27  HOH   HOH B . 
F 5 HOH   30 330 67  HOH   HOH B . 
F 5 HOH   31 331 29  HOH   HOH B . 
F 5 HOH   32 332 82  HOH   HOH B . 
F 5 HOH   33 333 73  HOH   HOH B . 
F 5 HOH   34 334 62  HOH   HOH B . 
F 5 HOH   35 335 3   HOH   HOH B . 
F 5 HOH   36 336 21  HOH   HOH B . 
F 5 HOH   37 337 135 HOH   HOH B . 
F 5 HOH   38 338 64  HOH   HOH B . 
F 5 HOH   39 339 137 HOH   HOH B . 
F 5 HOH   40 340 87  HOH   HOH B . 
F 5 HOH   41 341 123 HOH   HOH B . 
F 5 HOH   42 342 133 HOH   HOH B . 
F 5 HOH   43 343 49  HOH   HOH B . 
F 5 HOH   44 344 103 HOH   HOH B . 
F 5 HOH   45 345 24  HOH   HOH B . 
F 5 HOH   46 346 17  HOH   HOH B . 
F 5 HOH   47 347 130 HOH   HOH B . 
F 5 HOH   48 348 125 HOH   HOH B . 
F 5 HOH   49 349 72  HOH   HOH B . 
F 5 HOH   50 350 79  HOH   HOH B . 
F 5 HOH   51 351 107 HOH   HOH B . 
F 5 HOH   52 352 132 HOH   HOH B . 
F 5 HOH   53 353 75  HOH   HOH B . 
F 5 HOH   54 354 134 HOH   HOH B . 
F 5 HOH   55 355 126 HOH   HOH B . 
F 5 HOH   56 356 124 HOH   HOH B . 
F 5 HOH   57 357 127 HOH   HOH B . 
F 5 HOH   58 358 109 HOH   HOH B . 
# 
loop_
_software.pdbx_ordinal 
_software.name 
_software.version 
_software.date 
_software.type 
_software.contact_author 
_software.contact_author_email 
_software.classification 
_software.location 
_software.language 
_software.citation_id 
1 BUSTER      '2.10.4 (23-JAN-2024)' ?               program 'Gerard Bricogne' buster-develop@GlobalPhasing.com refinement        
http://www.globalphasing.com/buster/                ?   ? 
2 Aimless     0.7.15                 02/11/23        program 'Phil Evans'      ?                                'data scaling'    
http://www.mrc-lmb.cam.ac.uk/harry/pre/aimless.html ?   ? 
3 PDB_EXTRACT 3.23                   'SEP. 23, 2016' package PDB               deposit@deposit.rcsb.org         'data extraction' 
http://sw-tools.pdb.org/apps/PDB_EXTRACT/           C++ ? 
4 XDS         .                      ?               program ?                 ?                                'data reduction'  
?                                                   ?   ? 
5 PHASER      .                      ?               program ?                 ?                                phasing           
?                                                   ?   ? 
# 
_cell.entry_id           7IAJ 
_cell.length_a           42.238 
_cell.length_b           42.238 
_cell.length_c           216.736 
_cell.angle_alpha        90.000 
_cell.angle_beta         90.000 
_cell.angle_gamma        90.000 
_cell.Z_PDB              8 
_cell.pdbx_unique_axis   ? 
# 
_symmetry.entry_id                         7IAJ 
_symmetry.Int_Tables_number                95 
_symmetry.space_group_name_H-M             'P 43 2 2' 
_symmetry.pdbx_full_space_group_name_H-M   ? 
_symmetry.cell_setting                     ? 
# 
_exptl.crystals_number   1 
_exptl.entry_id          7IAJ 
_exptl.method            'X-RAY DIFFRACTION' 
# 
_exptl_crystal.id                    1 
_exptl_crystal.pdbx_mosaicity        0.210 
_exptl_crystal.pdbx_mosaicity_esd    ? 
_exptl_crystal.density_Matthews      2.08 
_exptl_crystal.density_diffrn        ? 
_exptl_crystal.density_meas          ? 
_exptl_crystal.density_meas_temp     ? 
_exptl_crystal.density_percent_sol   41.00 
_exptl_crystal.size_max              ? 
_exptl_crystal.size_mid              ? 
_exptl_crystal.size_min              ? 
_exptl_crystal.size_rad              ? 
_exptl_crystal.description           ? 
# 
_exptl_crystal_grow.crystal_id      1 
_exptl_crystal_grow.method          'VAPOR DIFFUSION, SITTING DROP' 
_exptl_crystal_grow.pH              4.8 
_exptl_crystal_grow.temp            298 
_exptl_crystal_grow.pdbx_details    '30% w/v PEG 2000, 0.2M Ammonium sulfate, 0.1M acetate (pH 4.8)' 
_exptl_crystal_grow.temp_details    ? 
_exptl_crystal_grow.pdbx_pH_range   ? 
# 
_diffrn.id                     1 
_diffrn.ambient_temp           100 
_diffrn.crystal_id             1 
_diffrn.ambient_temp_details   ? 
# 
_diffrn_detector.detector               PIXEL 
_diffrn_detector.type                   'DECTRIS EIGER2 XE 9M' 
_diffrn_detector.pdbx_collection_date   2024-07-31 
_diffrn_detector.diffrn_id              1 
_diffrn_detector.details                ? 
# 
_diffrn_radiation.diffrn_id                        1 
_diffrn_radiation.wavelength_id                    1 
_diffrn_radiation.pdbx_diffrn_protocol             'SINGLE WAVELENGTH' 
_diffrn_radiation.pdbx_monochromatic_or_laue_m_l   ? 
_diffrn_radiation.monochromator                    ? 
_diffrn_radiation.pdbx_scattering_type             x-ray 
# 
_diffrn_radiation_wavelength.id           1 
_diffrn_radiation_wavelength.wavelength   0.92134 
_diffrn_radiation_wavelength.wt           1.0 
# 
_diffrn_source.diffrn_id                   1 
_diffrn_source.source                      SYNCHROTRON 
_diffrn_source.type                        'DIAMOND BEAMLINE I04-1' 
_diffrn_source.pdbx_wavelength_list        0.92134 
_diffrn_source.pdbx_synchrotron_site       Diamond 
_diffrn_source.pdbx_synchrotron_beamline   I04-1 
_diffrn_source.pdbx_wavelength             ? 
# 
_reflns.entry_id                     7IAJ 
_reflns.pdbx_diffrn_id               1 
_reflns.pdbx_ordinal                 1 
_reflns.observed_criterion_sigma_I   ? 
_reflns.observed_criterion_sigma_F   ? 
_reflns.d_resolution_low             108.370 
_reflns.d_resolution_high            2.200 
_reflns.number_obs                   10902 
_reflns.number_all                   ? 
_reflns.percent_possible_obs         100.000 
_reflns.pdbx_Rmerge_I_obs            0.734 
_reflns.pdbx_Rsym_value              ? 
_reflns.pdbx_netI_over_sigmaI        4.100 
_reflns.B_iso_Wilson_estimate        43.200 
_reflns.pdbx_redundancy              24.100 
_reflns.pdbx_Rrim_I_all              0.750 
_reflns.pdbx_Rpim_I_all              0.151 
_reflns.pdbx_CC_half                 0.983 
_reflns.pdbx_netI_over_av_sigmaI     ? 
_reflns.pdbx_number_measured_all     262685 
_reflns.pdbx_scaling_rejects         260 
_reflns.pdbx_chi_squared             ? 
_reflns.Rmerge_F_all                 ? 
_reflns.Rmerge_F_obs                 ? 
_reflns.observed_criterion_F_max     ? 
_reflns.observed_criterion_F_min     ? 
_reflns.observed_criterion_I_max     ? 
_reflns.observed_criterion_I_min     ? 
_reflns.pdbx_d_res_high_opt          ? 
_reflns.pdbx_d_res_low_opt           ? 
_reflns.details                      ? 
_reflns.pdbx_CC_star                 ? 
# 
loop_
_reflns_shell.pdbx_diffrn_id 
_reflns_shell.pdbx_ordinal 
_reflns_shell.d_res_high 
_reflns_shell.d_res_low 
_reflns_shell.number_measured_obs 
_reflns_shell.number_measured_all 
_reflns_shell.number_unique_obs 
_reflns_shell.pdbx_rejects 
_reflns_shell.Rmerge_I_obs 
_reflns_shell.meanI_over_sigI_obs 
_reflns_shell.pdbx_Rsym_value 
_reflns_shell.pdbx_chi_squared 
_reflns_shell.pdbx_redundancy 
_reflns_shell.percent_possible_obs 
_reflns_shell.pdbx_netI_over_sigmaI_obs 
_reflns_shell.number_possible 
_reflns_shell.number_unique_all 
_reflns_shell.Rmerge_F_all 
_reflns_shell.Rmerge_F_obs 
_reflns_shell.Rmerge_I_all 
_reflns_shell.meanI_over_sigI_all 
_reflns_shell.percent_possible_all 
_reflns_shell.pdbx_Rrim_I_all 
_reflns_shell.pdbx_Rpim_I_all 
_reflns_shell.pdbx_CC_half 
_reflns_shell.pdbx_CC_star 
1 1 2.200 2.320   ? 36657 ? ? 7.622 ? ? ? 24.000 ? 0.500  ? 1530 ? ? ? ? 100.000 7.787 1.576 0.412 ? 
1 2 6.950 108.370 ? 7971  ? ? 0.180 ? ? ? 17.900 ? 11.900 ? 445  ? ? ? ? 99.800  0.186 0.043 0.971 ? 
# 
_refine.entry_id                                 7IAJ 
_refine.pdbx_refine_id                           'X-RAY DIFFRACTION' 
_refine.ls_d_res_high                            2.1990 
_refine.ls_d_res_low                             54.1800 
_refine.pdbx_ls_sigma_F                          0.000 
_refine.pdbx_data_cutoff_high_absF               ? 
_refine.pdbx_data_cutoff_low_absF                ? 
_refine.ls_percent_reflns_obs                    98.7000 
_refine.ls_number_reflns_obs                     10688 
_refine.ls_number_reflns_all                     ? 
_refine.pdbx_ls_cross_valid_method               THROUGHOUT 
_refine.ls_matrix_type                           ? 
_refine.pdbx_R_Free_selection_details            RANDOM 
_refine.details                                  ? 
_refine.ls_R_factor_all                          ? 
_refine.ls_R_factor_obs                          0.2434 
_refine.ls_R_factor_R_work                       0.2407 
_refine.ls_wR_factor_R_work                      ? 
_refine.ls_R_factor_R_free                       0.2936 
_refine.ls_wR_factor_R_free                      ? 
_refine.ls_percent_reflns_R_free                 4.8100 
_refine.ls_number_reflns_R_free                  514 
_refine.ls_number_reflns_R_work                  ? 
_refine.ls_R_factor_R_free_error                 ? 
_refine.B_iso_mean                               49.6400 
_refine.solvent_model_param_bsol                 ? 
_refine.solvent_model_param_ksol                 ? 
_refine.pdbx_isotropic_thermal_model             ? 
_refine.aniso_B[1][1]                            -4.0347 
_refine.aniso_B[2][2]                            -4.0347 
_refine.aniso_B[3][3]                            8.0693 
_refine.aniso_B[1][2]                            0.0000 
_refine.aniso_B[1][3]                            0.0000 
_refine.aniso_B[2][3]                            0.0000 
_refine.correlation_coeff_Fo_to_Fc               0.9300 
_refine.correlation_coeff_Fo_to_Fc_free          0.8990 
_refine.overall_SU_R_Cruickshank_DPI             0.3210 
_refine.pdbx_overall_SU_R_free_Cruickshank_DPI   0.2490 
_refine.pdbx_overall_SU_R_Blow_DPI               0.3700 
_refine.pdbx_overall_SU_R_free_Blow_DPI          0.2600 
_refine.overall_SU_R_free                        ? 
_refine.pdbx_overall_ESU_R                       ? 
_refine.pdbx_overall_ESU_R_Free                  ? 
_refine.overall_SU_ML                            ? 
_refine.overall_SU_B                             ? 
_refine.solvent_model_details                    ? 
_refine.pdbx_solvent_vdw_probe_radii             ? 
_refine.pdbx_solvent_ion_probe_radii             ? 
_refine.pdbx_solvent_shrinkage_radii             ? 
_refine.ls_number_parameters                     ? 
_refine.ls_number_restraints                     ? 
_refine.pdbx_starting_model                      5GPI 
_refine.pdbx_method_to_determine_struct          'FOURIER SYNTHESIS' 
_refine.pdbx_stereochemistry_target_values       ? 
_refine.pdbx_stereochem_target_val_spec_case     ? 
_refine.overall_FOM_work_R_set                   ? 
_refine.B_iso_max                                97.440 
_refine.B_iso_min                                27.290 
_refine.pdbx_overall_phase_error                 ? 
_refine.occupancy_max                            ? 
_refine.occupancy_min                            ? 
_refine.pdbx_diffrn_id                           1 
_refine.pdbx_TLS_residual_ADP_flag               ? 
_refine.pdbx_ls_sigma_I                          ? 
_refine.pdbx_data_cutoff_high_rms_absF           ? 
_refine.ls_R_factor_R_free_error_details         ? 
# 
_refine_analyze.entry_id                        7IAJ 
_refine_analyze.pdbx_refine_id                  'X-RAY DIFFRACTION' 
_refine_analyze.Luzzati_coordinate_error_obs    0.390 
_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_hist.cycle_id                         final 
_refine_hist.pdbx_refine_id                   'X-RAY DIFFRACTION' 
_refine_hist.d_res_high                       2.1990 
_refine_hist.d_res_low                        54.1800 
_refine_hist.pdbx_number_atoms_ligand         26 
_refine_hist.number_atoms_solvent             74 
_refine_hist.number_atoms_total               1563 
_refine_hist.pdbx_number_residues_total       193 
_refine_hist.pdbx_B_iso_mean_ligand           50.38 
_refine_hist.pdbx_B_iso_mean_solvent          45.85 
_refine_hist.pdbx_number_atoms_protein        1463 
_refine_hist.pdbx_number_atoms_nucleic_acid   0 
# 
loop_
_refine_ls_restr.pdbx_refine_id 
_refine_ls_restr.type 
_refine_ls_restr.number 
_refine_ls_restr.dev_ideal 
_refine_ls_restr.dev_ideal_target 
_refine_ls_restr.weight 
_refine_ls_restr.pdbx_restraint_function 
'X-RAY DIFFRACTION' t_dihedral_angle_d        529  ?      ? 2.000  SINUSOIDAL   
'X-RAY DIFFRACTION' t_trig_c_planes           ?    ?      ? ?      ?            
'X-RAY DIFFRACTION' t_gen_planes              266  ?      ? 5.000  HARMONIC     
'X-RAY DIFFRACTION' t_it                      1550 ?      ? 10.000 HARMONIC     
'X-RAY DIFFRACTION' t_nbd                     0    ?      ? 5.000  SEMIHARMONIC 
'X-RAY DIFFRACTION' t_improper_torsion        ?    ?      ? ?      ?            
'X-RAY DIFFRACTION' t_pseud_angle             ?    ?      ? ?      ?            
'X-RAY DIFFRACTION' t_chiral_improper_torsion 193  ?      ? 5.000  SEMIHARMONIC 
'X-RAY DIFFRACTION' t_sum_occupancies         ?    ?      ? ?      ?            
'X-RAY DIFFRACTION' t_utility_distance        ?    ?      ? ?      ?            
'X-RAY DIFFRACTION' t_utility_angle           ?    ?      ? ?      ?            
'X-RAY DIFFRACTION' t_utility_torsion         ?    ?      ? ?      ?            
'X-RAY DIFFRACTION' t_ideal_dist_contact      1158 ?      ? 4.000  SEMIHARMONIC 
'X-RAY DIFFRACTION' t_bond_d                  1550 0.007  ? 2.000  HARMONIC     
'X-RAY DIFFRACTION' t_angle_deg               2111 0.940  ? 2.000  HARMONIC     
'X-RAY DIFFRACTION' t_omega_torsion           ?    2.960  ? ?      ?            
'X-RAY DIFFRACTION' t_other_torsion           ?    17.740 ? ?      ?            
# 
_refine_ls_shell.d_res_high                       2.2000 
_refine_ls_shell.d_res_low                        2.2300 
_refine_ls_shell.pdbx_total_number_of_bins_used   26 
_refine_ls_shell.percent_reflns_obs               92.9500 
_refine_ls_shell.number_reflns_R_work             407 
_refine_ls_shell.R_factor_all                     ? 
_refine_ls_shell.R_factor_R_work                  0.3988 
_refine_ls_shell.R_factor_R_free                  0.4880 
_refine_ls_shell.percent_reflns_R_free            4.9100 
_refine_ls_shell.number_reflns_R_free             21 
_refine_ls_shell.R_factor_R_free_error            ? 
_refine_ls_shell.number_reflns_all                428 
_refine_ls_shell.number_reflns_obs                ? 
_refine_ls_shell.pdbx_refine_id                   'X-RAY DIFFRACTION' 
_refine_ls_shell.R_factor_obs                     ? 
# 
_struct.entry_id                  7IAJ 
_struct.title                     
;Group deposition of ZIKV NS2B-NS3 protease in complex with inhibitors from ASAP Discovery Consortium -- Crystal Structure of ZIKV NS2B-NS3 protease in complex with ASAP-0029751-001
;
_struct.pdbx_model_details        ? 
_struct.pdbx_CASP_flag            ? 
_struct.pdbx_model_type_details   ? 
# 
_struct_keywords.entry_id        7IAJ 
_struct_keywords.pdbx_keywords   'VIRAL PROTEIN' 
_struct_keywords.text            'SGC - Diamond I04-1, XChemExplorer, ASAP Discovery Consortium, VIRAL PROTEIN' 
# 
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 3 ? 
D N N 4 ? 
E N N 5 ? 
F N N 5 ? 
# 
loop_
_struct_ref.id 
_struct_ref.db_name 
_struct_ref.db_code 
_struct_ref.pdbx_db_accession 
_struct_ref.pdbx_db_isoform 
_struct_ref.entity_id 
_struct_ref.pdbx_seq_one_letter_code 
_struct_ref.pdbx_align_begin 
1 UNP POLG_ZIKV Q32ZE1 ? 1 GKSVDMYIERAGDITWEKDAEVTGNSPRLDVALDESGDFSLVEE 1414 
2 UNP POLG_ZIKV Q32ZE1 ? 2 
;KEVKKGETTDGVYRVMTRRLLGSTQVGVGVMQEGVFHTMWHVTKGAALRSGEGRLDPYWGDVKQDLVSYCGPWKLDAAWD
GLSEVQLLAVPPGERARNIQTLPGIFKTKDGDIGAVALDYPAGTSGSPILDKCGRVIGLYGNGVVIKNGSYVSAITQGKR
EEETPVE
;
1509 
# 
loop_
_struct_ref_seq.align_id 
_struct_ref_seq.ref_id 
_struct_ref_seq.pdbx_PDB_id_code 
_struct_ref_seq.pdbx_strand_id 
_struct_ref_seq.seq_align_beg 
_struct_ref_seq.pdbx_seq_align_beg_ins_code 
_struct_ref_seq.seq_align_end 
_struct_ref_seq.pdbx_seq_align_end_ins_code 
_struct_ref_seq.pdbx_db_accession 
_struct_ref_seq.db_align_beg 
_struct_ref_seq.pdbx_db_align_beg_ins_code 
_struct_ref_seq.db_align_end 
_struct_ref_seq.pdbx_db_align_end_ins_code 
_struct_ref_seq.pdbx_auth_seq_align_beg 
_struct_ref_seq.pdbx_auth_seq_align_end 
1 1 7IAJ A 3 ? 46  ? Q32ZE1 1414 ? 1457 ? 46 89  
2 2 7IAJ B 2 ? 168 ? Q32ZE1 1509 ? 1675 ? 11 177 
# 
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 7IAJ SER A 1  ? UNP Q32ZE1 ?   ?    'expression tag'        44  1 
1 7IAJ MET A 2  ? UNP Q32ZE1 ?   ?    'expression tag'        45  2 
2 7IAJ MET B 1  ? UNP Q32ZE1 ?   ?    'initiating methionine' 10  3 
2 7IAJ LYS B 98 ? UNP Q32ZE1 ARG 1605 conflict                107 4 
# 
_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   dimeric 
_pdbx_struct_assembly.oligomeric_count     2 
# 
loop_
_pdbx_struct_assembly_prop.biol_id 
_pdbx_struct_assembly_prop.type 
_pdbx_struct_assembly_prop.value 
_pdbx_struct_assembly_prop.details 
1 'ABSA (A^2)' 4190 ? 
1 MORE         -26  ? 
1 'SSA (A^2)'  9740 ? 
# 
_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,F 
# 
_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_
_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 AA1 MET B 40  ? LYS B 45  ? MET B 49  LYS B 54  1 ? 6 
HELX_P HELX_P2 AA2 PRO B 122 ? SER B 126 ? PRO B 131 SER B 135 5 ? 5 
# 
_struct_conf_type.id          HELX_P 
_struct_conf_type.criteria    ? 
_struct_conf_type.reference   ? 
# 
loop_
_struct_sheet.id 
_struct_sheet.type 
_struct_sheet.number_strands 
_struct_sheet.details 
AA1 ? 8 ? 
AA2 ? 5 ? 
AA3 ? 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 
AA1 1 2 ? anti-parallel 
AA1 2 3 ? parallel      
AA1 3 4 ? anti-parallel 
AA1 4 5 ? anti-parallel 
AA1 5 6 ? anti-parallel 
AA1 6 7 ? anti-parallel 
AA1 7 8 ? anti-parallel 
AA2 1 2 ? parallel      
AA2 2 3 ? anti-parallel 
AA2 3 4 ? anti-parallel 
AA2 4 5 ? anti-parallel 
AA3 1 2 ? anti-parallel 
AA3 2 3 ? parallel      
AA3 3 4 ? anti-parallel 
AA3 4 5 ? anti-parallel 
AA3 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 
AA1 1 GLY B 54  ? LEU B 56  ? GLY B 63  LEU B 65  
AA1 2 LEU B 49  ? SER B 51  ? LEU B 58  SER B 60  
AA1 3 MET A 8   ? GLY A 14  ? MET A 51  GLY A 57  
AA1 4 GLY B 12  ? THR B 18  ? GLY B 21  THR B 27  
AA1 5 THR B 25  ? GLN B 33  ? THR B 34  GLN B 42  
AA1 6 VAL B 36  ? THR B 39  ? VAL B 45  THR B 48  
AA1 7 LEU B 67  ? TYR B 70  ? LEU B 76  TYR B 79  
AA1 8 PRO B 58  ? ASP B 62  ? PRO B 67  ASP B 71  
AA2 1 GLU A 23  ? VAL A 24  ? GLU A 66  VAL A 67  
AA2 2 LYS B 98  ? THR B 102 ? LYS B 107 THR B 111 
AA2 3 VAL B 86  ? ALA B 90  ? VAL B 95  ALA B 99  
AA2 4 SER B 128 ? LEU B 131 ? SER B 137 LEU B 140 
AA2 5 VAL B 137 ? TYR B 141 ? VAL B 146 TYR B 150 
AA3 1 PHE A 41  ? LEU A 43  ? PHE A 84  LEU A 86  
AA3 2 ARG A 30  ? LEU A 35  ? ARG A 73  LEU A 78  
AA3 3 GLY B 105 ? THR B 109 ? GLY B 114 THR B 118 
AA3 4 GLY B 112 ? VAL B 117 ? GLY B 121 VAL B 126 
AA3 5 TYR B 152 ? ALA B 155 ? TYR B 161 ALA B 164 
AA3 6 GLY B 144 ? VAL B 146 ? GLY B 153 VAL B 155 
# 
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 
AA1 1 2 O LEU B 56  ? O LEU B 65  N LEU B 49  ? N LEU B 58  
AA1 2 3 O ARG B 50  ? O ARG B 59  N ILE A 10  ? N ILE A 53  
AA1 3 4 N ALA A 13  ? N ALA A 56  O VAL B 13  ? O VAL B 22  
AA1 4 5 N GLY B 12  ? N GLY B 21  O MET B 32  ? O MET B 41  
AA1 5 6 N VAL B 31  ? N VAL B 40  O HIS B 38  ? O HIS B 47  
AA1 6 7 N THR B 39  ? N THR B 48  O VAL B 68  ? O VAL B 77  
AA1 7 8 O SER B 69  ? O SER B 78  N TRP B 60  ? N TRP B 69  
AA2 1 2 O GLU A 23  ? O GLU A 66  N GLN B 101 ? N GLN B 110 
AA2 2 3 O THR B 102 ? O THR B 111 N VAL B 86  ? N VAL B 95  
AA2 3 4 N GLN B 87  ? N GLN B 96  O LEU B 131 ? O LEU B 140 
AA2 4 5 N ILE B 130 ? N ILE B 139 O GLY B 139 ? O GLY B 148 
AA3 1 2 O SER A 42  ? O SER A 85  N ALA A 34  ? N ALA A 77  
AA3 2 3 N LEU A 31  ? N LEU A 74  O LYS B 108 ? O LYS B 117 
AA3 3 4 N PHE B 107 ? N PHE B 116 O ILE B 114 ? O ILE B 123 
AA3 4 5 N VAL B 117 ? N VAL B 126 O SER B 154 ? O SER B 163 
AA3 5 6 O VAL B 153 ? O VAL B 162 N VAL B 145 ? N VAL B 154 
# 
_pdbx_entry_details.entry_id                   7IAJ 
_pdbx_entry_details.compound_details           ? 
_pdbx_entry_details.source_details             ? 
_pdbx_entry_details.nonpolymer_details         ? 
_pdbx_entry_details.sequence_details           ? 
_pdbx_entry_details.has_ligand_of_interest     ? 
_pdbx_entry_details.has_protein_modification   N 
# 
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 LEU B 30  ? ? -100.88 -154.71 
2 1 CYS B 80  ? ? 80.28   -20.45  
3 1 ALA B 127 ? ? -92.89  48.82   
# 
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 -13.5985 -1.8842 -19.4320 -0.0420 -0.0489 -0.3051 0.1785 0.1446 0.0988 3.8843 4.1165 3.8342 
-1.6367 0.4318  1.3695  0.3714 -0.3834 0.0120  0.5612 0.4141 -0.4483 -0.4152 0.0053 0.3524 
'X-RAY DIFFRACTION' 2 ? refined -17.9569 0.5168  -15.6123 0.0713  0.0141  -0.0960 0.1796 0.0276 0.0250 1.7178 1.0876 2.3380 
-0.8116 -0.0503 -0.5519 0.3328 -0.3023 -0.0305 0.1403 0.1536 0.0720  -0.1404 0.1784 0.1430 
# 
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 50 A 88  '{ A|* }' ? ? ? ? ? 
'X-RAY DIFFRACTION' 2 2 B 18 B 171 '{ B|* }' ? ? ? ? ? 
# 
_phasing.method   MR 
# 
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 SER 44  ? A SER 1   
2  1 Y 1 A MET 45  ? A MET 2   
3  1 Y 1 A GLY 46  ? A GLY 3   
4  1 Y 1 A LYS 47  ? A LYS 4   
5  1 Y 1 A SER 48  ? A SER 5   
6  1 Y 1 A VAL 49  ? A VAL 6   
7  1 Y 1 A GLU 89  ? A GLU 46  
8  1 Y 1 B MET 10  ? B MET 1   
9  1 Y 1 B LYS 11  ? B LYS 2   
10 1 Y 1 B GLU 12  ? B GLU 3   
11 1 Y 1 B VAL 13  ? B VAL 4   
12 1 Y 1 B LYS 14  ? B LYS 5   
13 1 Y 1 B LYS 15  ? B LYS 6   
14 1 Y 1 B GLY 16  ? B GLY 7   
15 1 Y 1 B GLU 17  ? B GLU 8   
16 1 Y 1 B GLU 172 ? B GLU 163 
17 1 Y 1 B GLU 173 ? B GLU 164 
18 1 Y 1 B THR 174 ? B THR 165 
19 1 Y 1 B PRO 175 ? B PRO 166 
20 1 Y 1 B VAL 176 ? B VAL 167 
21 1 Y 1 B GLU 177 ? B GLU 168 
# 
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 
A1B82 N1   N  N N 1   
A1B82 N3   N  Y N 2   
A1B82 C4   C  Y N 3   
A1B82 C5   C  Y N 4   
A1B82 C6   C  Y N 5   
A1B82 C7   C  Y N 6   
A1B82 C8   C  N N 7   
A1B82 C10  C  Y N 8   
A1B82 C13  C  Y N 9   
A1B82 C15  C  Y N 10  
A1B82 O1   O  N N 11  
A1B82 C1   C  N N 12  
A1B82 C2   C  Y N 13  
A1B82 C3   C  Y N 14  
A1B82 N2   N  N N 15  
A1B82 C9   C  N N 16  
A1B82 C11  C  Y N 17  
A1B82 C12  C  Y N 18  
A1B82 CL1  CL N N 19  
A1B82 N4   N  Y N 20  
A1B82 C14  C  Y N 21  
A1B82 C16  C  Y N 22  
A1B82 H1   H  N N 23  
A1B82 H2   H  N N 24  
A1B82 H3   H  N N 25  
A1B82 H4   H  N N 26  
A1B82 H5   H  N N 27  
A1B82 H6   H  N N 28  
A1B82 H7   H  N N 29  
A1B82 H8   H  N N 30  
A1B82 H10  H  N N 31  
A1B82 H11  H  N N 32  
A1B82 H12  H  N N 33  
A1B82 H13  H  N N 34  
A1B82 H14  H  N N 35  
ALA   N    N  N N 36  
ALA   CA   C  N S 37  
ALA   C    C  N N 38  
ALA   O    O  N N 39  
ALA   CB   C  N N 40  
ALA   OXT  O  N N 41  
ALA   H    H  N N 42  
ALA   H2   H  N N 43  
ALA   HA   H  N N 44  
ALA   HB1  H  N N 45  
ALA   HB2  H  N N 46  
ALA   HB3  H  N N 47  
ALA   HXT  H  N N 48  
ARG   N    N  N N 49  
ARG   CA   C  N S 50  
ARG   C    C  N N 51  
ARG   O    O  N N 52  
ARG   CB   C  N N 53  
ARG   CG   C  N N 54  
ARG   CD   C  N N 55  
ARG   NE   N  N N 56  
ARG   CZ   C  N N 57  
ARG   NH1  N  N N 58  
ARG   NH2  N  N N 59  
ARG   OXT  O  N N 60  
ARG   H    H  N N 61  
ARG   H2   H  N N 62  
ARG   HA   H  N N 63  
ARG   HB2  H  N N 64  
ARG   HB3  H  N N 65  
ARG   HG2  H  N N 66  
ARG   HG3  H  N N 67  
ARG   HD2  H  N N 68  
ARG   HD3  H  N N 69  
ARG   HE   H  N N 70  
ARG   HH11 H  N N 71  
ARG   HH12 H  N N 72  
ARG   HH21 H  N N 73  
ARG   HH22 H  N N 74  
ARG   HXT  H  N N 75  
ASN   N    N  N N 76  
ASN   CA   C  N S 77  
ASN   C    C  N N 78  
ASN   O    O  N N 79  
ASN   CB   C  N N 80  
ASN   CG   C  N N 81  
ASN   OD1  O  N N 82  
ASN   ND2  N  N N 83  
ASN   OXT  O  N N 84  
ASN   H    H  N N 85  
ASN   H2   H  N N 86  
ASN   HA   H  N N 87  
ASN   HB2  H  N N 88  
ASN   HB3  H  N N 89  
ASN   HD21 H  N N 90  
ASN   HD22 H  N N 91  
ASN   HXT  H  N N 92  
ASP   N    N  N N 93  
ASP   CA   C  N S 94  
ASP   C    C  N N 95  
ASP   O    O  N N 96  
ASP   CB   C  N N 97  
ASP   CG   C  N N 98  
ASP   OD1  O  N N 99  
ASP   OD2  O  N N 100 
ASP   OXT  O  N N 101 
ASP   H    H  N N 102 
ASP   H2   H  N N 103 
ASP   HA   H  N N 104 
ASP   HB2  H  N N 105 
ASP   HB3  H  N N 106 
ASP   HD2  H  N N 107 
ASP   HXT  H  N N 108 
CYS   N    N  N N 109 
CYS   CA   C  N R 110 
CYS   C    C  N N 111 
CYS   O    O  N N 112 
CYS   CB   C  N N 113 
CYS   SG   S  N N 114 
CYS   OXT  O  N N 115 
CYS   H    H  N N 116 
CYS   H2   H  N N 117 
CYS   HA   H  N N 118 
CYS   HB2  H  N N 119 
CYS   HB3  H  N N 120 
CYS   HG   H  N N 121 
CYS   HXT  H  N N 122 
DMS   S    S  N N 123 
DMS   O    O  N N 124 
DMS   C1   C  N N 125 
DMS   C2   C  N N 126 
DMS   H11  H  N N 127 
DMS   H12  H  N N 128 
DMS   H13  H  N N 129 
DMS   H21  H  N N 130 
DMS   H22  H  N N 131 
DMS   H23  H  N N 132 
GLN   N    N  N N 133 
GLN   CA   C  N S 134 
GLN   C    C  N N 135 
GLN   O    O  N N 136 
GLN   CB   C  N N 137 
GLN   CG   C  N N 138 
GLN   CD   C  N N 139 
GLN   OE1  O  N N 140 
GLN   NE2  N  N N 141 
GLN   OXT  O  N N 142 
GLN   H    H  N N 143 
GLN   H2   H  N N 144 
GLN   HA   H  N N 145 
GLN   HB2  H  N N 146 
GLN   HB3  H  N N 147 
GLN   HG2  H  N N 148 
GLN   HG3  H  N N 149 
GLN   HE21 H  N N 150 
GLN   HE22 H  N N 151 
GLN   HXT  H  N N 152 
GLU   N    N  N N 153 
GLU   CA   C  N S 154 
GLU   C    C  N N 155 
GLU   O    O  N N 156 
GLU   CB   C  N N 157 
GLU   CG   C  N N 158 
GLU   CD   C  N N 159 
GLU   OE1  O  N N 160 
GLU   OE2  O  N N 161 
GLU   OXT  O  N N 162 
GLU   H    H  N N 163 
GLU   H2   H  N N 164 
GLU   HA   H  N N 165 
GLU   HB2  H  N N 166 
GLU   HB3  H  N N 167 
GLU   HG2  H  N N 168 
GLU   HG3  H  N N 169 
GLU   HE2  H  N N 170 
GLU   HXT  H  N N 171 
GLY   N    N  N N 172 
GLY   CA   C  N N 173 
GLY   C    C  N N 174 
GLY   O    O  N N 175 
GLY   OXT  O  N N 176 
GLY   H    H  N N 177 
GLY   H2   H  N N 178 
GLY   HA2  H  N N 179 
GLY   HA3  H  N N 180 
GLY   HXT  H  N N 181 
HIS   N    N  N N 182 
HIS   CA   C  N S 183 
HIS   C    C  N N 184 
HIS   O    O  N N 185 
HIS   CB   C  N N 186 
HIS   CG   C  Y N 187 
HIS   ND1  N  Y N 188 
HIS   CD2  C  Y N 189 
HIS   CE1  C  Y N 190 
HIS   NE2  N  Y N 191 
HIS   OXT  O  N N 192 
HIS   H    H  N N 193 
HIS   H2   H  N N 194 
HIS   HA   H  N N 195 
HIS   HB2  H  N N 196 
HIS   HB3  H  N N 197 
HIS   HD1  H  N N 198 
HIS   HD2  H  N N 199 
HIS   HE1  H  N N 200 
HIS   HE2  H  N N 201 
HIS   HXT  H  N N 202 
HOH   O    O  N N 203 
HOH   H1   H  N N 204 
HOH   H2   H  N N 205 
ILE   N    N  N N 206 
ILE   CA   C  N S 207 
ILE   C    C  N N 208 
ILE   O    O  N N 209 
ILE   CB   C  N S 210 
ILE   CG1  C  N N 211 
ILE   CG2  C  N N 212 
ILE   CD1  C  N N 213 
ILE   OXT  O  N N 214 
ILE   H    H  N N 215 
ILE   H2   H  N N 216 
ILE   HA   H  N N 217 
ILE   HB   H  N N 218 
ILE   HG12 H  N N 219 
ILE   HG13 H  N N 220 
ILE   HG21 H  N N 221 
ILE   HG22 H  N N 222 
ILE   HG23 H  N N 223 
ILE   HD11 H  N N 224 
ILE   HD12 H  N N 225 
ILE   HD13 H  N N 226 
ILE   HXT  H  N N 227 
LEU   N    N  N N 228 
LEU   CA   C  N S 229 
LEU   C    C  N N 230 
LEU   O    O  N N 231 
LEU   CB   C  N N 232 
LEU   CG   C  N N 233 
LEU   CD1  C  N N 234 
LEU   CD2  C  N N 235 
LEU   OXT  O  N N 236 
LEU   H    H  N N 237 
LEU   H2   H  N N 238 
LEU   HA   H  N N 239 
LEU   HB2  H  N N 240 
LEU   HB3  H  N N 241 
LEU   HG   H  N N 242 
LEU   HD11 H  N N 243 
LEU   HD12 H  N N 244 
LEU   HD13 H  N N 245 
LEU   HD21 H  N N 246 
LEU   HD22 H  N N 247 
LEU   HD23 H  N N 248 
LEU   HXT  H  N N 249 
LYS   N    N  N N 250 
LYS   CA   C  N S 251 
LYS   C    C  N N 252 
LYS   O    O  N N 253 
LYS   CB   C  N N 254 
LYS   CG   C  N N 255 
LYS   CD   C  N N 256 
LYS   CE   C  N N 257 
LYS   NZ   N  N N 258 
LYS   OXT  O  N N 259 
LYS   H    H  N N 260 
LYS   H2   H  N N 261 
LYS   HA   H  N N 262 
LYS   HB2  H  N N 263 
LYS   HB3  H  N N 264 
LYS   HG2  H  N N 265 
LYS   HG3  H  N N 266 
LYS   HD2  H  N N 267 
LYS   HD3  H  N N 268 
LYS   HE2  H  N N 269 
LYS   HE3  H  N N 270 
LYS   HZ1  H  N N 271 
LYS   HZ2  H  N N 272 
LYS   HZ3  H  N N 273 
LYS   HXT  H  N N 274 
MET   N    N  N N 275 
MET   CA   C  N S 276 
MET   C    C  N N 277 
MET   O    O  N N 278 
MET   CB   C  N N 279 
MET   CG   C  N N 280 
MET   SD   S  N N 281 
MET   CE   C  N N 282 
MET   OXT  O  N N 283 
MET   H    H  N N 284 
MET   H2   H  N N 285 
MET   HA   H  N N 286 
MET   HB2  H  N N 287 
MET   HB3  H  N N 288 
MET   HG2  H  N N 289 
MET   HG3  H  N N 290 
MET   HE1  H  N N 291 
MET   HE2  H  N N 292 
MET   HE3  H  N N 293 
MET   HXT  H  N N 294 
PHE   N    N  N N 295 
PHE   CA   C  N S 296 
PHE   C    C  N N 297 
PHE   O    O  N N 298 
PHE   CB   C  N N 299 
PHE   CG   C  Y N 300 
PHE   CD1  C  Y N 301 
PHE   CD2  C  Y N 302 
PHE   CE1  C  Y N 303 
PHE   CE2  C  Y N 304 
PHE   CZ   C  Y N 305 
PHE   OXT  O  N N 306 
PHE   H    H  N N 307 
PHE   H2   H  N N 308 
PHE   HA   H  N N 309 
PHE   HB2  H  N N 310 
PHE   HB3  H  N N 311 
PHE   HD1  H  N N 312 
PHE   HD2  H  N N 313 
PHE   HE1  H  N N 314 
PHE   HE2  H  N N 315 
PHE   HZ   H  N N 316 
PHE   HXT  H  N N 317 
PRO   N    N  N N 318 
PRO   CA   C  N S 319 
PRO   C    C  N N 320 
PRO   O    O  N N 321 
PRO   CB   C  N N 322 
PRO   CG   C  N N 323 
PRO   CD   C  N N 324 
PRO   OXT  O  N N 325 
PRO   H    H  N N 326 
PRO   HA   H  N N 327 
PRO   HB2  H  N N 328 
PRO   HB3  H  N N 329 
PRO   HG2  H  N N 330 
PRO   HG3  H  N N 331 
PRO   HD2  H  N N 332 
PRO   HD3  H  N N 333 
PRO   HXT  H  N N 334 
SER   N    N  N N 335 
SER   CA   C  N S 336 
SER   C    C  N N 337 
SER   O    O  N N 338 
SER   CB   C  N N 339 
SER   OG   O  N N 340 
SER   OXT  O  N N 341 
SER   H    H  N N 342 
SER   H2   H  N N 343 
SER   HA   H  N N 344 
SER   HB2  H  N N 345 
SER   HB3  H  N N 346 
SER   HG   H  N N 347 
SER   HXT  H  N N 348 
THR   N    N  N N 349 
THR   CA   C  N S 350 
THR   C    C  N N 351 
THR   O    O  N N 352 
THR   CB   C  N R 353 
THR   OG1  O  N N 354 
THR   CG2  C  N N 355 
THR   OXT  O  N N 356 
THR   H    H  N N 357 
THR   H2   H  N N 358 
THR   HA   H  N N 359 
THR   HB   H  N N 360 
THR   HG1  H  N N 361 
THR   HG21 H  N N 362 
THR   HG22 H  N N 363 
THR   HG23 H  N N 364 
THR   HXT  H  N N 365 
TRP   N    N  N N 366 
TRP   CA   C  N S 367 
TRP   C    C  N N 368 
TRP   O    O  N N 369 
TRP   CB   C  N N 370 
TRP   CG   C  Y N 371 
TRP   CD1  C  Y N 372 
TRP   CD2  C  Y N 373 
TRP   NE1  N  Y N 374 
TRP   CE2  C  Y N 375 
TRP   CE3  C  Y N 376 
TRP   CZ2  C  Y N 377 
TRP   CZ3  C  Y N 378 
TRP   CH2  C  Y N 379 
TRP   OXT  O  N N 380 
TRP   H    H  N N 381 
TRP   H2   H  N N 382 
TRP   HA   H  N N 383 
TRP   HB2  H  N N 384 
TRP   HB3  H  N N 385 
TRP   HD1  H  N N 386 
TRP   HE1  H  N N 387 
TRP   HE3  H  N N 388 
TRP   HZ2  H  N N 389 
TRP   HZ3  H  N N 390 
TRP   HH2  H  N N 391 
TRP   HXT  H  N N 392 
TYR   N    N  N N 393 
TYR   CA   C  N S 394 
TYR   C    C  N N 395 
TYR   O    O  N N 396 
TYR   CB   C  N N 397 
TYR   CG   C  Y N 398 
TYR   CD1  C  Y N 399 
TYR   CD2  C  Y N 400 
TYR   CE1  C  Y N 401 
TYR   CE2  C  Y N 402 
TYR   CZ   C  Y N 403 
TYR   OH   O  N N 404 
TYR   OXT  O  N N 405 
TYR   H    H  N N 406 
TYR   H2   H  N N 407 
TYR   HA   H  N N 408 
TYR   HB2  H  N N 409 
TYR   HB3  H  N N 410 
TYR   HD1  H  N N 411 
TYR   HD2  H  N N 412 
TYR   HE1  H  N N 413 
TYR   HE2  H  N N 414 
TYR   HH   H  N N 415 
TYR   HXT  H  N N 416 
VAL   N    N  N N 417 
VAL   CA   C  N S 418 
VAL   C    C  N N 419 
VAL   O    O  N N 420 
VAL   CB   C  N N 421 
VAL   CG1  C  N N 422 
VAL   CG2  C  N N 423 
VAL   OXT  O  N N 424 
VAL   H    H  N N 425 
VAL   H2   H  N N 426 
VAL   HA   H  N N 427 
VAL   HB   H  N N 428 
VAL   HG11 H  N N 429 
VAL   HG12 H  N N 430 
VAL   HG13 H  N N 431 
VAL   HG21 H  N N 432 
VAL   HG22 H  N N 433 
VAL   HG23 H  N N 434 
VAL   HXT  H  N N 435 
# 
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 
A1B82 CL1 C12  sing N N 1   
A1B82 N3  C12  doub Y N 2   
A1B82 N3  C13  sing Y N 3   
A1B82 N4  C13  sing Y N 4   
A1B82 N4  C14  sing Y N 5   
A1B82 C12 C11  sing Y N 6   
A1B82 C13 C16  doub Y N 7   
A1B82 C14 C15  doub Y N 8   
A1B82 C16 C15  sing Y N 9   
A1B82 C16 C10  sing Y N 10  
A1B82 C11 C10  doub Y N 11  
A1B82 C10 C1   sing N N 12  
A1B82 C1  O1   doub N N 13  
A1B82 C1  N1   sing N N 14  
A1B82 N1  C2   sing N N 15  
A1B82 C2  C7   doub Y N 16  
A1B82 C2  C3   sing Y N 17  
A1B82 C7  C6   sing Y N 18  
A1B82 C3  C4   doub Y N 19  
A1B82 C6  C5   doub Y N 20  
A1B82 C6  C8   sing N N 21  
A1B82 C4  C5   sing Y N 22  
A1B82 C5  C9   sing N N 23  
A1B82 C8  N2   sing N N 24  
A1B82 C9  N2   sing N N 25  
A1B82 N1  H1   sing N N 26  
A1B82 C4  H2   sing N N 27  
A1B82 C7  H3   sing N N 28  
A1B82 C8  H4   sing N N 29  
A1B82 C8  H5   sing N N 30  
A1B82 C15 H6   sing N N 31  
A1B82 C3  H7   sing N N 32  
A1B82 N2  H8   sing N N 33  
A1B82 C9  H10  sing N N 34  
A1B82 C9  H11  sing N N 35  
A1B82 C11 H12  sing N N 36  
A1B82 N4  H13  sing N N 37  
A1B82 C14 H14  sing N N 38  
ALA   N   CA   sing N N 39  
ALA   N   H    sing N N 40  
ALA   N   H2   sing N N 41  
ALA   CA  C    sing N N 42  
ALA   CA  CB   sing N N 43  
ALA   CA  HA   sing N N 44  
ALA   C   O    doub N N 45  
ALA   C   OXT  sing N N 46  
ALA   CB  HB1  sing N N 47  
ALA   CB  HB2  sing N N 48  
ALA   CB  HB3  sing N N 49  
ALA   OXT HXT  sing N N 50  
ARG   N   CA   sing N N 51  
ARG   N   H    sing N N 52  
ARG   N   H2   sing N N 53  
ARG   CA  C    sing N N 54  
ARG   CA  CB   sing N N 55  
ARG   CA  HA   sing N N 56  
ARG   C   O    doub N N 57  
ARG   C   OXT  sing N N 58  
ARG   CB  CG   sing N N 59  
ARG   CB  HB2  sing N N 60  
ARG   CB  HB3  sing N N 61  
ARG   CG  CD   sing N N 62  
ARG   CG  HG2  sing N N 63  
ARG   CG  HG3  sing N N 64  
ARG   CD  NE   sing N N 65  
ARG   CD  HD2  sing N N 66  
ARG   CD  HD3  sing N N 67  
ARG   NE  CZ   sing N N 68  
ARG   NE  HE   sing N N 69  
ARG   CZ  NH1  sing N N 70  
ARG   CZ  NH2  doub N N 71  
ARG   NH1 HH11 sing N N 72  
ARG   NH1 HH12 sing N N 73  
ARG   NH2 HH21 sing N N 74  
ARG   NH2 HH22 sing N N 75  
ARG   OXT HXT  sing N N 76  
ASN   N   CA   sing N N 77  
ASN   N   H    sing N N 78  
ASN   N   H2   sing N N 79  
ASN   CA  C    sing N N 80  
ASN   CA  CB   sing N N 81  
ASN   CA  HA   sing N N 82  
ASN   C   O    doub N N 83  
ASN   C   OXT  sing N N 84  
ASN   CB  CG   sing N N 85  
ASN   CB  HB2  sing N N 86  
ASN   CB  HB3  sing N N 87  
ASN   CG  OD1  doub N N 88  
ASN   CG  ND2  sing N N 89  
ASN   ND2 HD21 sing N N 90  
ASN   ND2 HD22 sing N N 91  
ASN   OXT HXT  sing N N 92  
ASP   N   CA   sing N N 93  
ASP   N   H    sing N N 94  
ASP   N   H2   sing N N 95  
ASP   CA  C    sing N N 96  
ASP   CA  CB   sing N N 97  
ASP   CA  HA   sing N N 98  
ASP   C   O    doub N N 99  
ASP   C   OXT  sing N N 100 
ASP   CB  CG   sing N N 101 
ASP   CB  HB2  sing N N 102 
ASP   CB  HB3  sing N N 103 
ASP   CG  OD1  doub N N 104 
ASP   CG  OD2  sing N N 105 
ASP   OD2 HD2  sing N N 106 
ASP   OXT HXT  sing N N 107 
CYS   N   CA   sing N N 108 
CYS   N   H    sing N N 109 
CYS   N   H2   sing N N 110 
CYS   CA  C    sing N N 111 
CYS   CA  CB   sing N N 112 
CYS   CA  HA   sing N N 113 
CYS   C   O    doub N N 114 
CYS   C   OXT  sing N N 115 
CYS   CB  SG   sing N N 116 
CYS   CB  HB2  sing N N 117 
CYS   CB  HB3  sing N N 118 
CYS   SG  HG   sing N N 119 
CYS   OXT HXT  sing N N 120 
DMS   S   O    doub N N 121 
DMS   S   C1   sing N N 122 
DMS   S   C2   sing N N 123 
DMS   C1  H11  sing N N 124 
DMS   C1  H12  sing N N 125 
DMS   C1  H13  sing N N 126 
DMS   C2  H21  sing N N 127 
DMS   C2  H22  sing N N 128 
DMS   C2  H23  sing N N 129 
GLN   N   CA   sing N N 130 
GLN   N   H    sing N N 131 
GLN   N   H2   sing N N 132 
GLN   CA  C    sing N N 133 
GLN   CA  CB   sing N N 134 
GLN   CA  HA   sing N N 135 
GLN   C   O    doub N N 136 
GLN   C   OXT  sing N N 137 
GLN   CB  CG   sing N N 138 
GLN   CB  HB2  sing N N 139 
GLN   CB  HB3  sing N N 140 
GLN   CG  CD   sing N N 141 
GLN   CG  HG2  sing N N 142 
GLN   CG  HG3  sing N N 143 
GLN   CD  OE1  doub N N 144 
GLN   CD  NE2  sing N N 145 
GLN   NE2 HE21 sing N N 146 
GLN   NE2 HE22 sing N N 147 
GLN   OXT HXT  sing N N 148 
GLU   N   CA   sing N N 149 
GLU   N   H    sing N N 150 
GLU   N   H2   sing N N 151 
GLU   CA  C    sing N N 152 
GLU   CA  CB   sing N N 153 
GLU   CA  HA   sing N N 154 
GLU   C   O    doub N N 155 
GLU   C   OXT  sing N N 156 
GLU   CB  CG   sing N N 157 
GLU   CB  HB2  sing N N 158 
GLU   CB  HB3  sing N N 159 
GLU   CG  CD   sing N N 160 
GLU   CG  HG2  sing N N 161 
GLU   CG  HG3  sing N N 162 
GLU   CD  OE1  doub N N 163 
GLU   CD  OE2  sing N N 164 
GLU   OE2 HE2  sing N N 165 
GLU   OXT HXT  sing N N 166 
GLY   N   CA   sing N N 167 
GLY   N   H    sing N N 168 
GLY   N   H2   sing N N 169 
GLY   CA  C    sing N N 170 
GLY   CA  HA2  sing N N 171 
GLY   CA  HA3  sing N N 172 
GLY   C   O    doub N N 173 
GLY   C   OXT  sing N N 174 
GLY   OXT HXT  sing N N 175 
HIS   N   CA   sing N N 176 
HIS   N   H    sing N N 177 
HIS   N   H2   sing N N 178 
HIS   CA  C    sing N N 179 
HIS   CA  CB   sing N N 180 
HIS   CA  HA   sing N N 181 
HIS   C   O    doub N N 182 
HIS   C   OXT  sing N N 183 
HIS   CB  CG   sing N N 184 
HIS   CB  HB2  sing N N 185 
HIS   CB  HB3  sing N N 186 
HIS   CG  ND1  sing Y N 187 
HIS   CG  CD2  doub Y N 188 
HIS   ND1 CE1  doub Y N 189 
HIS   ND1 HD1  sing N N 190 
HIS   CD2 NE2  sing Y N 191 
HIS   CD2 HD2  sing N N 192 
HIS   CE1 NE2  sing Y N 193 
HIS   CE1 HE1  sing N N 194 
HIS   NE2 HE2  sing N N 195 
HIS   OXT HXT  sing N N 196 
HOH   O   H1   sing N N 197 
HOH   O   H2   sing N N 198 
ILE   N   CA   sing N N 199 
ILE   N   H    sing N N 200 
ILE   N   H2   sing N N 201 
ILE   CA  C    sing N N 202 
ILE   CA  CB   sing N N 203 
ILE   CA  HA   sing N N 204 
ILE   C   O    doub N N 205 
ILE   C   OXT  sing N N 206 
ILE   CB  CG1  sing N N 207 
ILE   CB  CG2  sing N N 208 
ILE   CB  HB   sing N N 209 
ILE   CG1 CD1  sing N N 210 
ILE   CG1 HG12 sing N N 211 
ILE   CG1 HG13 sing N N 212 
ILE   CG2 HG21 sing N N 213 
ILE   CG2 HG22 sing N N 214 
ILE   CG2 HG23 sing N N 215 
ILE   CD1 HD11 sing N N 216 
ILE   CD1 HD12 sing N N 217 
ILE   CD1 HD13 sing N N 218 
ILE   OXT HXT  sing N N 219 
LEU   N   CA   sing N N 220 
LEU   N   H    sing N N 221 
LEU   N   H2   sing N N 222 
LEU   CA  C    sing N N 223 
LEU   CA  CB   sing N N 224 
LEU   CA  HA   sing N N 225 
LEU   C   O    doub N N 226 
LEU   C   OXT  sing N N 227 
LEU   CB  CG   sing N N 228 
LEU   CB  HB2  sing N N 229 
LEU   CB  HB3  sing N N 230 
LEU   CG  CD1  sing N N 231 
LEU   CG  CD2  sing N N 232 
LEU   CG  HG   sing N N 233 
LEU   CD1 HD11 sing N N 234 
LEU   CD1 HD12 sing N N 235 
LEU   CD1 HD13 sing N N 236 
LEU   CD2 HD21 sing N N 237 
LEU   CD2 HD22 sing N N 238 
LEU   CD2 HD23 sing N N 239 
LEU   OXT HXT  sing N N 240 
LYS   N   CA   sing N N 241 
LYS   N   H    sing N N 242 
LYS   N   H2   sing N N 243 
LYS   CA  C    sing N N 244 
LYS   CA  CB   sing N N 245 
LYS   CA  HA   sing N N 246 
LYS   C   O    doub N N 247 
LYS   C   OXT  sing N N 248 
LYS   CB  CG   sing N N 249 
LYS   CB  HB2  sing N N 250 
LYS   CB  HB3  sing N N 251 
LYS   CG  CD   sing N N 252 
LYS   CG  HG2  sing N N 253 
LYS   CG  HG3  sing N N 254 
LYS   CD  CE   sing N N 255 
LYS   CD  HD2  sing N N 256 
LYS   CD  HD3  sing N N 257 
LYS   CE  NZ   sing N N 258 
LYS   CE  HE2  sing N N 259 
LYS   CE  HE3  sing N N 260 
LYS   NZ  HZ1  sing N N 261 
LYS   NZ  HZ2  sing N N 262 
LYS   NZ  HZ3  sing N N 263 
LYS   OXT HXT  sing N N 264 
MET   N   CA   sing N N 265 
MET   N   H    sing N N 266 
MET   N   H2   sing N N 267 
MET   CA  C    sing N N 268 
MET   CA  CB   sing N N 269 
MET   CA  HA   sing N N 270 
MET   C   O    doub N N 271 
MET   C   OXT  sing N N 272 
MET   CB  CG   sing N N 273 
MET   CB  HB2  sing N N 274 
MET   CB  HB3  sing N N 275 
MET   CG  SD   sing N N 276 
MET   CG  HG2  sing N N 277 
MET   CG  HG3  sing N N 278 
MET   SD  CE   sing N N 279 
MET   CE  HE1  sing N N 280 
MET   CE  HE2  sing N N 281 
MET   CE  HE3  sing N N 282 
MET   OXT HXT  sing N N 283 
PHE   N   CA   sing N N 284 
PHE   N   H    sing N N 285 
PHE   N   H2   sing N N 286 
PHE   CA  C    sing N N 287 
PHE   CA  CB   sing N N 288 
PHE   CA  HA   sing N N 289 
PHE   C   O    doub N N 290 
PHE   C   OXT  sing N N 291 
PHE   CB  CG   sing N N 292 
PHE   CB  HB2  sing N N 293 
PHE   CB  HB3  sing N N 294 
PHE   CG  CD1  doub Y N 295 
PHE   CG  CD2  sing Y N 296 
PHE   CD1 CE1  sing Y N 297 
PHE   CD1 HD1  sing N N 298 
PHE   CD2 CE2  doub Y N 299 
PHE   CD2 HD2  sing N N 300 
PHE   CE1 CZ   doub Y N 301 
PHE   CE1 HE1  sing N N 302 
PHE   CE2 CZ   sing Y N 303 
PHE   CE2 HE2  sing N N 304 
PHE   CZ  HZ   sing N N 305 
PHE   OXT HXT  sing N N 306 
PRO   N   CA   sing N N 307 
PRO   N   CD   sing N N 308 
PRO   N   H    sing N N 309 
PRO   CA  C    sing N N 310 
PRO   CA  CB   sing N N 311 
PRO   CA  HA   sing N N 312 
PRO   C   O    doub N N 313 
PRO   C   OXT  sing N N 314 
PRO   CB  CG   sing N N 315 
PRO   CB  HB2  sing N N 316 
PRO   CB  HB3  sing N N 317 
PRO   CG  CD   sing N N 318 
PRO   CG  HG2  sing N N 319 
PRO   CG  HG3  sing N N 320 
PRO   CD  HD2  sing N N 321 
PRO   CD  HD3  sing N N 322 
PRO   OXT HXT  sing N N 323 
SER   N   CA   sing N N 324 
SER   N   H    sing N N 325 
SER   N   H2   sing N N 326 
SER   CA  C    sing N N 327 
SER   CA  CB   sing N N 328 
SER   CA  HA   sing N N 329 
SER   C   O    doub N N 330 
SER   C   OXT  sing N N 331 
SER   CB  OG   sing N N 332 
SER   CB  HB2  sing N N 333 
SER   CB  HB3  sing N N 334 
SER   OG  HG   sing N N 335 
SER   OXT HXT  sing N N 336 
THR   N   CA   sing N N 337 
THR   N   H    sing N N 338 
THR   N   H2   sing N N 339 
THR   CA  C    sing N N 340 
THR   CA  CB   sing N N 341 
THR   CA  HA   sing N N 342 
THR   C   O    doub N N 343 
THR   C   OXT  sing N N 344 
THR   CB  OG1  sing N N 345 
THR   CB  CG2  sing N N 346 
THR   CB  HB   sing N N 347 
THR   OG1 HG1  sing N N 348 
THR   CG2 HG21 sing N N 349 
THR   CG2 HG22 sing N N 350 
THR   CG2 HG23 sing N N 351 
THR   OXT HXT  sing N N 352 
TRP   N   CA   sing N N 353 
TRP   N   H    sing N N 354 
TRP   N   H2   sing N N 355 
TRP   CA  C    sing N N 356 
TRP   CA  CB   sing N N 357 
TRP   CA  HA   sing N N 358 
TRP   C   O    doub N N 359 
TRP   C   OXT  sing N N 360 
TRP   CB  CG   sing N N 361 
TRP   CB  HB2  sing N N 362 
TRP   CB  HB3  sing N N 363 
TRP   CG  CD1  doub Y N 364 
TRP   CG  CD2  sing Y N 365 
TRP   CD1 NE1  sing Y N 366 
TRP   CD1 HD1  sing N N 367 
TRP   CD2 CE2  doub Y N 368 
TRP   CD2 CE3  sing Y N 369 
TRP   NE1 CE2  sing Y N 370 
TRP   NE1 HE1  sing N N 371 
TRP   CE2 CZ2  sing Y N 372 
TRP   CE3 CZ3  doub Y N 373 
TRP   CE3 HE3  sing N N 374 
TRP   CZ2 CH2  doub Y N 375 
TRP   CZ2 HZ2  sing N N 376 
TRP   CZ3 CH2  sing Y N 377 
TRP   CZ3 HZ3  sing N N 378 
TRP   CH2 HH2  sing N N 379 
TRP   OXT HXT  sing N N 380 
TYR   N   CA   sing N N 381 
TYR   N   H    sing N N 382 
TYR   N   H2   sing N N 383 
TYR   CA  C    sing N N 384 
TYR   CA  CB   sing N N 385 
TYR   CA  HA   sing N N 386 
TYR   C   O    doub N N 387 
TYR   C   OXT  sing N N 388 
TYR   CB  CG   sing N N 389 
TYR   CB  HB2  sing N N 390 
TYR   CB  HB3  sing N N 391 
TYR   CG  CD1  doub Y N 392 
TYR   CG  CD2  sing Y N 393 
TYR   CD1 CE1  sing Y N 394 
TYR   CD1 HD1  sing N N 395 
TYR   CD2 CE2  doub Y N 396 
TYR   CD2 HD2  sing N N 397 
TYR   CE1 CZ   doub Y N 398 
TYR   CE1 HE1  sing N N 399 
TYR   CE2 CZ   sing Y N 400 
TYR   CE2 HE2  sing N N 401 
TYR   CZ  OH   sing N N 402 
TYR   OH  HH   sing N N 403 
TYR   OXT HXT  sing N N 404 
VAL   N   CA   sing N N 405 
VAL   N   H    sing N N 406 
VAL   N   H2   sing N N 407 
VAL   CA  C    sing N N 408 
VAL   CA  CB   sing N N 409 
VAL   CA  HA   sing N N 410 
VAL   C   O    doub N N 411 
VAL   C   OXT  sing N N 412 
VAL   CB  CG1  sing N N 413 
VAL   CB  CG2  sing N N 414 
VAL   CB  HB   sing N N 415 
VAL   CG1 HG11 sing N N 416 
VAL   CG1 HG12 sing N N 417 
VAL   CG1 HG13 sing N N 418 
VAL   CG2 HG21 sing N N 419 
VAL   CG2 HG22 sing N N 420 
VAL   CG2 HG23 sing N N 421 
VAL   OXT HXT  sing N N 422 
# 
_pdbx_audit_support.funding_organization   
'National Institutes of Health/National Institute Of Allergy and Infectious Diseases (NIH/NIAID)' 
_pdbx_audit_support.country                'United States' 
_pdbx_audit_support.grant_number           U19AI171399 
_pdbx_audit_support.ordinal                1 
# 
_pdbx_deposit_group.group_id            G_1002345 
_pdbx_deposit_group.group_description   
;XDomainX of XOrganismX None screened against the XXX Fragment Library by X-ray Crystallography at the XChem facility of Diamond Light Source beamline I04-1
;
_pdbx_deposit_group.group_title         
'Group deposition of ZIKV NS2B-NS3 protease in complex with inhibitors from ASAP Discovery Consortium' 
_pdbx_deposit_group.group_type          'changed state' 
# 
_atom_sites.entry_id                    7IAJ 
_atom_sites.fract_transf_matrix[1][1]   0.023675 
_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]   0.023675 
_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]   0.004614 
_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  
CL 
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   . ASP   A 1 7   ? -21.469 19.119  -7.337  1.00 49.34 ? 50  ASP   A N   1 
ATOM   2    C  CA  . ASP   A 1 7   ? -22.539 18.123  -7.430  1.00 48.94 ? 50  ASP   A CA  1 
ATOM   3    C  C   . ASP   A 1 7   ? -22.527 17.382  -8.778  1.00 47.91 ? 50  ASP   A C   1 
ATOM   4    O  O   . ASP   A 1 7   ? -22.720 17.997  -9.834  1.00 48.10 ? 50  ASP   A O   1 
ATOM   5    C  CB  . ASP   A 1 7   ? -23.911 18.763  -7.169  1.00 50.33 ? 50  ASP   A CB  1 
ATOM   6    C  CG  . ASP   A 1 7   ? -24.842 17.885  -6.353  1.00 56.61 ? 50  ASP   A CG  1 
ATOM   7    O  OD1 . ASP   A 1 7   ? -25.692 18.444  -5.618  1.00 57.37 ? 50  ASP   A OD1 1 
ATOM   8    O  OD2 . ASP   A 1 7   ? -24.723 16.628  -6.449  1.00 59.36 ? 50  ASP   A OD2 1 
ATOM   9    N  N   . MET   A 1 8   ? -22.295 16.054  -8.737  1.00 46.32 ? 51  MET   A N   1 
ATOM   10   C  CA  . MET   A 1 8   ? -22.278 15.243  -9.946  1.00 44.85 ? 51  MET   A CA  1 
ATOM   11   C  C   . MET   A 1 8   ? -23.674 14.996  -10.514 1.00 43.53 ? 51  MET   A C   1 
ATOM   12   O  O   . MET   A 1 8   ? -24.650 14.918  -9.768  1.00 43.31 ? 51  MET   A O   1 
ATOM   13   C  CB  . MET   A 1 8   ? -21.538 13.926  -9.717  1.00 45.16 ? 51  MET   A CB  1 
ATOM   14   C  CG  . MET   A 1 8   ? -20.047 14.088  -9.660  1.00 46.47 ? 51  MET   A CG  1 
ATOM   15   S  SD  . MET   A 1 8   ? -19.228 12.540  -9.258  1.00 50.06 ? 51  MET   A SD  1 
ATOM   16   C  CE  . MET   A 1 8   ? -17.506 13.096  -9.178  1.00 47.82 ? 51  MET   A CE  1 
ATOM   17   N  N   . TYR   A 1 9   ? -23.764 14.916  -11.848 1.00 42.79 ? 52  TYR   A N   1 
ATOM   18   C  CA  . TYR   A 1 9   ? -25.013 14.691  -12.574 1.00 42.63 ? 52  TYR   A CA  1 
ATOM   19   C  C   . TYR   A 1 9   ? -24.854 13.688  -13.719 1.00 42.72 ? 52  TYR   A C   1 
ATOM   20   O  O   . TYR   A 1 9   ? -23.731 13.382  -14.117 1.00 42.40 ? 52  TYR   A O   1 
ATOM   21   C  CB  . TYR   A 1 9   ? -25.637 15.998  -13.068 1.00 42.35 ? 52  TYR   A CB  1 
ATOM   22   C  CG  . TYR   A 1 9   ? -24.790 16.799  -14.030 1.00 43.12 ? 52  TYR   A CG  1 
ATOM   23   C  CD1 . TYR   A 1 9   ? -23.868 17.728  -13.565 1.00 43.81 ? 52  TYR   A CD1 1 
ATOM   24   C  CD2 . TYR   A 1 9   ? -25.002 16.727  -15.405 1.00 43.98 ? 52  TYR   A CD2 1 
ATOM   25   C  CE1 . TYR   A 1 9   ? -23.123 18.505  -14.440 1.00 44.83 ? 52  TYR   A CE1 1 
ATOM   26   C  CE2 . TYR   A 1 9   ? -24.268 17.508  -16.292 1.00 44.55 ? 52  TYR   A CE2 1 
ATOM   27   C  CZ  . TYR   A 1 9   ? -23.338 18.409  -15.803 1.00 46.01 ? 52  TYR   A CZ  1 
ATOM   28   O  OH  . TYR   A 1 9   ? -22.618 19.221  -16.654 1.00 48.34 ? 52  TYR   A OH  1 
ATOM   29   N  N   . ILE   A 1 10  ? -25.984 13.134  -14.214 1.00 42.48 ? 53  ILE   A N   1 
ATOM   30   C  CA  . ILE   A 1 10  ? -25.958 12.155  -15.288 1.00 42.24 ? 53  ILE   A CA  1 
ATOM   31   C  C   . ILE   A 1 10  ? -26.845 12.546  -16.490 1.00 42.94 ? 53  ILE   A C   1 
ATOM   32   O  O   . ILE   A 1 10  ? -27.936 13.110  -16.322 1.00 43.09 ? 53  ILE   A O   1 
ATOM   33   C  CB  . ILE   A 1 10  ? -26.272 10.724  -14.771 1.00 42.16 ? 53  ILE   A CB  1 
ATOM   34   C  CG1 . ILE   A 1 10  ? -27.712 10.582  -14.240 1.00 42.22 ? 53  ILE   A CG1 1 
ATOM   35   C  CG2 . ILE   A 1 10  ? -25.251 10.269  -13.735 1.00 42.61 ? 53  ILE   A CG2 1 
ATOM   36   C  CD1 . ILE   A 1 10  ? -28.147 9.145   -14.083 1.00 42.35 ? 53  ILE   A CD1 1 
ATOM   37   N  N   . GLU   A 1 11  ? -26.351 12.259  -17.705 1.00 43.17 ? 54  GLU   A N   1 
ATOM   38   C  CA  . GLU   A 1 11  ? -27.067 12.496  -18.966 1.00 44.17 ? 54  GLU   A CA  1 
ATOM   39   C  C   . GLU   A 1 11  ? -27.006 11.195  -19.778 1.00 44.70 ? 54  GLU   A C   1 
ATOM   40   O  O   . GLU   A 1 11  ? -25.936 10.600  -19.879 1.00 44.01 ? 54  GLU   A O   1 
ATOM   41   C  CB  . GLU   A 1 11  ? -26.390 13.595  -19.807 1.00 46.61 ? 54  GLU   A CB  1 
ATOM   42   C  CG  . GLU   A 1 11  ? -26.281 14.958  -19.156 1.00 52.59 ? 54  GLU   A CG  1 
ATOM   43   C  CD  . GLU   A 1 11  ? -25.360 15.908  -19.898 1.00 59.57 ? 54  GLU   A CD  1 
ATOM   44   O  OE1 . GLU   A 1 11  ? -24.465 15.427  -20.631 1.00 59.44 ? 54  GLU   A OE1 1 
ATOM   45   O  OE2 . GLU   A 1 11  ? -25.528 17.138  -19.739 1.00 63.35 ? 54  GLU   A OE2 1 
ATOM   46   N  N   . ARG   A 1 12  ? -28.123 10.785  -20.399 1.00 45.40 ? 55  ARG   A N   1 
ATOM   47   C  CA  . ARG   A 1 12  ? -28.128 9.563   -21.211 1.00 46.18 ? 55  ARG   A CA  1 
ATOM   48   C  C   . ARG   A 1 12  ? -27.222 9.690   -22.411 1.00 47.75 ? 55  ARG   A C   1 
ATOM   49   O  O   . ARG   A 1 12  ? -27.223 10.714  -23.102 1.00 48.17 ? 55  ARG   A O   1 
ATOM   50   C  CB  . ARG   A 1 12  ? -29.544 9.192   -21.654 1.00 46.67 ? 55  ARG   A CB  1 
ATOM   51   C  CG  . ARG   A 1 12  ? -29.744 7.701   -21.779 1.00 48.66 ? 55  ARG   A CG  1 
ATOM   52   C  CD  . ARG   A 1 12  ? -31.202 7.339   -21.972 1.00 50.51 ? 55  ARG   A CD  1 
ATOM   53   N  NE  . ARG   A 1 12  ? -31.384 5.903   -22.198 1.00 52.47 ? 55  ARG   A NE  1 
ATOM   54   C  CZ  . ARG   A 1 12  ? -31.280 5.317   -23.389 1.00 55.01 ? 55  ARG   A CZ  1 
ATOM   55   N  NH1 . ARG   A 1 12  ? -30.971 6.029   -24.464 1.00 55.79 ? 55  ARG   A NH1 1 
ATOM   56   N  NH2 . ARG   A 1 12  ? -31.453 4.009   -23.508 1.00 54.46 ? 55  ARG   A NH2 1 
ATOM   57   N  N   . ALA   A 1 13  ? -26.437 8.651   -22.655 1.00 48.37 ? 56  ALA   A N   1 
ATOM   58   C  CA  . ALA   A 1 13  ? -25.505 8.593   -23.776 1.00 49.19 ? 56  ALA   A CA  1 
ATOM   59   C  C   . ALA   A 1 13  ? -25.907 7.556   -24.841 1.00 49.97 ? 56  ALA   A C   1 
ATOM   60   O  O   . ALA   A 1 13  ? -25.346 7.585   -25.924 1.00 50.50 ? 56  ALA   A O   1 
ATOM   61   C  CB  . ALA   A 1 13  ? -24.097 8.299   -23.268 1.00 49.37 ? 56  ALA   A CB  1 
ATOM   62   N  N   . GLY   A 1 14  ? -26.850 6.659   -24.543 1.00 49.99 ? 57  GLY   A N   1 
ATOM   63   C  CA  . GLY   A 1 14  ? -27.275 5.650   -25.508 1.00 50.39 ? 57  GLY   A CA  1 
ATOM   64   C  C   . GLY   A 1 14  ? -27.849 4.375   -24.922 1.00 50.77 ? 57  GLY   A C   1 
ATOM   65   O  O   . GLY   A 1 14  ? -28.007 4.265   -23.708 1.00 51.15 ? 57  GLY   A O   1 
ATOM   66   N  N   . ASP   A 1 15  ? -28.206 3.416   -25.796 1.00 50.61 ? 58  ASP   A N   1 
ATOM   67   C  CA  . ASP   A 1 15  ? -28.794 2.122   -25.439 1.00 50.92 ? 58  ASP   A CA  1 
ATOM   68   C  C   . ASP   A 1 15  ? -27.716 1.076   -25.289 1.00 52.40 ? 58  ASP   A C   1 
ATOM   69   O  O   . ASP   A 1 15  ? -26.667 1.178   -25.930 1.00 52.39 ? 58  ASP   A O   1 
ATOM   70   C  CB  . ASP   A 1 15  ? -29.701 1.631   -26.575 1.00 51.50 ? 58  ASP   A CB  1 
ATOM   71   C  CG  . ASP   A 1 15  ? -31.113 2.147   -26.577 1.00 55.51 ? 58  ASP   A CG  1 
ATOM   72   O  OD1 . ASP   A 1 15  ? -31.415 3.033   -25.772 1.00 55.59 ? 58  ASP   A OD1 1 
ATOM   73   O  OD2 . ASP   A 1 15  ? -31.914 1.688   -27.426 1.00 58.31 ? 58  ASP   A OD2 1 
ATOM   74   N  N   . ILE   A 1 16  ? -28.005 0.005   -24.534 1.00 53.32 ? 59  ILE   A N   1 
ATOM   75   C  CA  . ILE   A 1 16  ? -27.067 -1.098  -24.416 1.00 54.43 ? 59  ILE   A CA  1 
ATOM   76   C  C   . ILE   A 1 16  ? -27.534 -2.270  -25.273 1.00 56.01 ? 59  ILE   A C   1 
ATOM   77   O  O   . ILE   A 1 16  ? -28.384 -3.056  -24.855 1.00 56.10 ? 59  ILE   A O   1 
ATOM   78   C  CB  . ILE   A 1 16  ? -26.831 -1.468  -22.956 1.00 55.00 ? 59  ILE   A CB  1 
ATOM   79   C  CG1 . ILE   A 1 16  ? -26.245 -0.271  -22.206 1.00 55.91 ? 59  ILE   A CG1 1 
ATOM   80   C  CG2 . ILE   A 1 16  ? -25.934 -2.689  -22.853 1.00 55.34 ? 59  ILE   A CG2 1 
ATOM   81   C  CD1 . ILE   A 1 16  ? -26.487 -0.320  -20.745 1.00 56.94 ? 59  ILE   A CD1 1 
ATOM   82   N  N   A THR   A 1 17  ? -26.999 -2.348  -26.506 0.50 56.44 ? 60  THR   A N   1 
ATOM   83   N  N   B THR   A 1 17  ? -26.999 -2.362  -26.499 0.50 56.66 ? 60  THR   A N   1 
ATOM   84   C  CA  A THR   A 1 17  ? -27.288 -3.391  -27.493 0.50 57.11 ? 60  THR   A CA  1 
ATOM   85   C  CA  B THR   A 1 17  ? -27.335 -3.402  -27.473 0.50 57.53 ? 60  THR   A CA  1 
ATOM   86   C  C   A THR   A 1 17  ? -26.000 -3.874  -28.152 0.50 58.01 ? 60  THR   A C   1 
ATOM   87   C  C   B THR   A 1 17  ? -26.064 -3.849  -28.222 0.50 58.24 ? 60  THR   A C   1 
ATOM   88   O  O   A THR   A 1 17  ? -25.046 -3.102  -28.287 0.50 57.68 ? 60  THR   A O   1 
ATOM   89   O  O   B THR   A 1 17  ? -25.153 -3.043  -28.421 0.50 57.97 ? 60  THR   A O   1 
ATOM   90   C  CB  A THR   A 1 17  ? -28.187 -2.850  -28.621 0.50 57.99 ? 60  THR   A CB  1 
ATOM   91   C  CB  B THR   A 1 17  ? -28.451 -2.886  -28.410 0.50 58.91 ? 60  THR   A CB  1 
ATOM   92   O  OG1 A THR   A 1 17  ? -27.586 -1.687  -29.201 0.50 58.43 ? 60  THR   A OG1 1 
ATOM   93   O  OG1 B THR   A 1 17  ? -29.642 -2.688  -27.648 0.50 60.06 ? 60  THR   A OG1 1 
ATOM   94   C  CG2 A THR   A 1 17  ? -29.611 -2.573  -28.167 0.50 58.51 ? 60  THR   A CG2 1 
ATOM   95   C  CG2 B THR   A 1 17  ? -28.760 -3.836  -29.549 0.50 59.27 ? 60  THR   A CG2 1 
ATOM   96   N  N   . TRP   A 1 18  ? -25.986 -5.134  -28.606 1.00 59.08 ? 61  TRP   A N   1 
ATOM   97   C  CA  . TRP   A 1 18  ? -24.830 -5.650  -29.336 1.00 61.93 ? 61  TRP   A CA  1 
ATOM   98   C  C   . TRP   A 1 18  ? -24.989 -5.148  -30.775 1.00 65.91 ? 61  TRP   A C   1 
ATOM   99   O  O   . TRP   A 1 18  ? -26.096 -5.188  -31.342 1.00 66.03 ? 61  TRP   A O   1 
ATOM   100  C  CB  . TRP   A 1 18  ? -24.764 -7.187  -29.291 1.00 61.65 ? 61  TRP   A CB  1 
ATOM   101  C  CG  . TRP   A 1 18  ? -23.654 -7.793  -30.118 1.00 62.43 ? 61  TRP   A CG  1 
ATOM   102  C  CD1 . TRP   A 1 18  ? -23.719 -8.172  -31.430 1.00 63.25 ? 61  TRP   A CD1 1 
ATOM   103  C  CD2 . TRP   A 1 18  ? -22.334 -8.143  -29.667 1.00 62.46 ? 61  TRP   A CD2 1 
ATOM   104  N  NE1 . TRP   A 1 18  ? -22.511 -8.685  -31.835 1.00 63.43 ? 61  TRP   A NE1 1 
ATOM   105  C  CE2 . TRP   A 1 18  ? -21.648 -8.693  -30.769 1.00 63.16 ? 61  TRP   A CE2 1 
ATOM   106  C  CE3 . TRP   A 1 18  ? -21.650 -8.002  -28.452 1.00 62.80 ? 61  TRP   A CE3 1 
ATOM   107  C  CZ2 . TRP   A 1 18  ? -20.330 -9.138  -30.678 1.00 63.66 ? 61  TRP   A CZ2 1 
ATOM   108  C  CZ3 . TRP   A 1 18  ? -20.349 -8.455  -28.361 1.00 63.37 ? 61  TRP   A CZ3 1 
ATOM   109  C  CH2 . TRP   A 1 18  ? -19.694 -8.991  -29.468 1.00 63.52 ? 61  TRP   A CH2 1 
ATOM   110  N  N   . GLU   A 1 19  ? -23.901 -4.631  -31.357 1.00 68.60 ? 62  GLU   A N   1 
ATOM   111  C  CA  . GLU   A 1 19  ? -23.955 -4.130  -32.723 1.00 71.14 ? 62  GLU   A CA  1 
ATOM   112  C  C   . GLU   A 1 19  ? -23.056 -4.916  -33.647 1.00 73.47 ? 62  GLU   A C   1 
ATOM   113  O  O   . GLU   A 1 19  ? -21.843 -4.952  -33.443 1.00 73.36 ? 62  GLU   A O   1 
ATOM   114  C  CB  . GLU   A 1 19  ? -23.646 -2.629  -32.776 1.00 74.08 ? 62  GLU   A CB  1 
ATOM   115  C  CG  . GLU   A 1 19  ? -24.690 -1.783  -32.058 1.00 80.10 ? 62  GLU   A CG  1 
ATOM   116  C  CD  . GLU   A 1 19  ? -26.097 -1.809  -32.637 1.00 88.61 ? 62  GLU   A CD  1 
ATOM   117  O  OE1 . GLU   A 1 19  ? -26.240 -1.731  -33.881 1.00 91.10 ? 62  GLU   A OE1 1 
ATOM   118  O  OE2 . GLU   A 1 19  ? -27.060 -1.889  -31.840 1.00 90.69 ? 62  GLU   A OE2 1 
ATOM   119  N  N   . LYS   A 1 20  ? -23.652 -5.577  -34.652 1.00 75.32 ? 63  LYS   A N   1 
ATOM   120  C  CA  . LYS   A 1 20  ? -22.858 -6.339  -35.617 1.00 77.71 ? 63  LYS   A CA  1 
ATOM   121  C  C   . LYS   A 1 20  ? -22.169 -5.348  -36.549 1.00 79.31 ? 63  LYS   A C   1 
ATOM   122  O  O   . LYS   A 1 20  ? -22.699 -4.263  -36.791 1.00 79.79 ? 63  LYS   A O   1 
ATOM   123  C  CB  . LYS   A 1 20  ? -23.707 -7.329  -36.443 1.00 80.55 ? 63  LYS   A CB  1 
ATOM   124  C  CG  . LYS   A 1 20  ? -25.109 -7.640  -35.906 1.00 85.58 ? 63  LYS   A CG  1 
ATOM   125  C  CD  . LYS   A 1 20  ? -25.911 -8.438  -36.945 1.00 90.40 ? 63  LYS   A CD  1 
ATOM   126  C  CE  . LYS   A 1 20  ? -27.341 -8.708  -36.533 1.00 94.61 ? 63  LYS   A CE  1 
ATOM   127  N  NZ  . LYS   A 1 20  ? -28.104 -9.405  -37.612 1.00 97.44 ? 63  LYS   A NZ  1 
ATOM   128  N  N   . ASP   A 1 21  ? -20.997 -5.706  -37.062 1.00 80.10 ? 64  ASP   A N   1 
ATOM   129  C  CA  . ASP   A 1 21  ? -20.228 -4.812  -37.927 1.00 81.57 ? 64  ASP   A CA  1 
ATOM   130  C  C   . ASP   A 1 21  ? -19.753 -3.598  -37.120 1.00 81.77 ? 64  ASP   A C   1 
ATOM   131  O  O   . ASP   A 1 21  ? -20.084 -2.455  -37.440 1.00 82.19 ? 64  ASP   A O   1 
ATOM   132  C  CB  . ASP   A 1 21  ? -21.006 -4.366  -39.193 1.00 84.36 ? 64  ASP   A CB  1 
ATOM   133  C  CG  . ASP   A 1 21  ? -21.396 -5.473  -40.156 1.00 90.68 ? 64  ASP   A CG  1 
ATOM   134  O  OD1 . ASP   A 1 21  ? -20.519 -6.305  -40.492 1.00 92.25 ? 64  ASP   A OD1 1 
ATOM   135  O  OD2 . ASP   A 1 21  ? -22.571 -5.483  -40.607 1.00 92.73 ? 64  ASP   A OD2 1 
ATOM   136  N  N   . ALA   A 1 22  ? -19.021 -3.858  -36.045 1.00 81.30 ? 65  ALA   A N   1 
ATOM   137  C  CA  . ALA   A 1 22  ? -18.430 -2.812  -35.214 1.00 80.99 ? 65  ALA   A CA  1 
ATOM   138  C  C   . ALA   A 1 22  ? -16.899 -2.814  -35.446 1.00 80.60 ? 65  ALA   A C   1 
ATOM   139  O  O   . ALA   A 1 22  ? -16.361 -3.779  -35.995 1.00 80.49 ? 65  ALA   A O   1 
ATOM   140  C  CB  . ALA   A 1 22  ? -18.748 -3.070  -33.749 1.00 81.02 ? 65  ALA   A CB  1 
ATOM   141  N  N   . GLU   A 1 23  ? -16.205 -1.733  -35.063 1.00 80.12 ? 66  GLU   A N   1 
ATOM   142  C  CA  . GLU   A 1 23  ? -14.755 -1.660  -35.225 1.00 79.96 ? 66  GLU   A CA  1 
ATOM   143  C  C   . GLU   A 1 23  ? -14.056 -2.678  -34.284 1.00 79.06 ? 66  GLU   A C   1 
ATOM   144  O  O   . GLU   A 1 23  ? -14.040 -2.475  -33.074 1.00 79.07 ? 66  GLU   A O   1 
ATOM   145  C  CB  . GLU   A 1 23  ? -14.266 -0.227  -34.958 1.00 82.47 ? 66  GLU   A CB  1 
ATOM   146  C  CG  . GLU   A 1 23  ? -12.827 0.011   -35.379 1.00 88.01 ? 66  GLU   A CG  1 
ATOM   147  C  CD  . GLU   A 1 23  ? -11.972 0.713   -34.341 1.00 94.52 ? 66  GLU   A CD  1 
ATOM   148  O  OE1 . GLU   A 1 23  ? -12.518 1.557   -33.594 1.00 95.61 ? 66  GLU   A OE1 1 
ATOM   149  O  OE2 . GLU   A 1 23  ? -10.753 0.425   -34.282 1.00 96.11 ? 66  GLU   A OE2 1 
ATOM   150  N  N   . VAL   A 1 24  ? -13.527 -3.786  -34.845 1.00 78.08 ? 67  VAL   A N   1 
ATOM   151  C  CA  . VAL   A 1 24  ? -12.850 -4.859  -34.100 1.00 77.69 ? 67  VAL   A CA  1 
ATOM   152  C  C   . VAL   A 1 24  ? -11.362 -4.555  -33.906 1.00 76.74 ? 67  VAL   A C   1 
ATOM   153  O  O   . VAL   A 1 24  ? -10.608 -4.593  -34.872 1.00 76.53 ? 67  VAL   A O   1 
ATOM   154  C  CB  . VAL   A 1 24  ? -13.011 -6.244  -34.779 1.00 78.10 ? 67  VAL   A CB  1 
ATOM   155  C  CG1 . VAL   A 1 24  ? -12.500 -7.353  -33.869 1.00 78.51 ? 67  VAL   A CG1 1 
ATOM   156  C  CG2 . VAL   A 1 24  ? -14.453 -6.508  -35.193 1.00 78.41 ? 67  VAL   A CG2 1 
ATOM   157  N  N   . THR   A 1 25  ? -10.931 -4.276  -32.667 1.00 75.59 ? 68  THR   A N   1 
ATOM   158  C  CA  . THR   A 1 25  ? -9.525  -3.967  -32.401 1.00 75.03 ? 68  THR   A CA  1 
ATOM   159  C  C   . THR   A 1 25  ? -9.104  -4.395  -30.993 1.00 74.69 ? 68  THR   A C   1 
ATOM   160  O  O   . THR   A 1 25  ? -9.953  -4.679  -30.148 1.00 74.62 ? 68  THR   A O   1 
ATOM   161  C  CB  . THR   A 1 25  ? -9.251  -2.465  -32.620 1.00 75.72 ? 68  THR   A CB  1 
ATOM   162  O  OG1 . THR   A 1 25  ? -7.837  -2.275  -32.674 1.00 76.42 ? 68  THR   A OG1 1 
ATOM   163  C  CG2 . THR   A 1 25  ? -9.835  -1.604  -31.508 1.00 75.65 ? 68  THR   A CG2 1 
ATOM   164  N  N   . GLY   A 1 26  ? -7.793  -4.449  -30.751 1.00 74.27 ? 69  GLY   A N   1 
ATOM   165  C  CA  . GLY   A 1 26  ? -7.275  -4.787  -29.435 1.00 73.84 ? 69  GLY   A CA  1 
ATOM   166  C  C   . GLY   A 1 26  ? -6.798  -6.210  -29.327 1.00 72.80 ? 69  GLY   A C   1 
ATOM   167  O  O   . GLY   A 1 26  ? -7.398  -7.121  -29.900 1.00 72.85 ? 69  GLY   A O   1 
ATOM   168  N  N   . ASN   A 1 27  ? -5.716  -6.404  -28.578 1.00 71.70 ? 70  ASN   A N   1 
ATOM   169  C  CA  . ASN   A 1 27  ? -5.144  -7.726  -28.381 1.00 70.87 ? 70  ASN   A CA  1 
ATOM   170  C  C   . ASN   A 1 27  ? -5.644  -8.390  -27.056 1.00 68.71 ? 70  ASN   A C   1 
ATOM   171  O  O   . ASN   A 1 27  ? -6.447  -7.785  -26.341 1.00 68.81 ? 70  ASN   A O   1 
ATOM   172  C  CB  . ASN   A 1 27  ? -3.610  -7.671  -28.518 1.00 72.51 ? 70  ASN   A CB  1 
ATOM   173  C  CG  . ASN   A 1 27  ? -2.882  -6.904  -27.445 1.00 76.19 ? 70  ASN   A CG  1 
ATOM   174  O  OD1 . ASN   A 1 27  ? -3.475  -6.194  -26.631 1.00 76.94 ? 70  ASN   A OD1 1 
ATOM   175  N  ND2 . ASN   A 1 27  ? -1.560  -7.034  -27.433 1.00 77.31 ? 70  ASN   A ND2 1 
ATOM   176  N  N   . SER   A 1 28  ? -5.260  -9.658  -26.786 1.00 66.66 ? 71  SER   A N   1 
ATOM   177  C  CA  . SER   A 1 28  ? -5.709  -10.395 -25.596 1.00 65.33 ? 71  SER   A CA  1 
ATOM   178  C  C   . SER   A 1 28  ? -4.523  -10.833 -24.746 1.00 63.61 ? 71  SER   A C   1 
ATOM   179  O  O   . SER   A 1 28  ? -4.066  -11.969 -24.863 1.00 64.14 ? 71  SER   A O   1 
ATOM   180  C  CB  . SER   A 1 28  ? -6.526  -11.626 -25.993 1.00 66.65 ? 71  SER   A CB  1 
ATOM   181  O  OG  . SER   A 1 28  ? -7.366  -11.422 -27.116 1.00 69.01 ? 71  SER   A OG  1 
ATOM   182  N  N   . PRO   A 1 29  ? -3.998  -9.966  -23.877 1.00 61.80 ? 72  PRO   A N   1 
ATOM   183  C  CA  . PRO   A 1 29  ? -2.810  -10.352 -23.095 1.00 60.97 ? 72  PRO   A CA  1 
ATOM   184  C  C   . PRO   A 1 29  ? -3.080  -11.147 -21.823 1.00 59.89 ? 72  PRO   A C   1 
ATOM   185  O  O   . PRO   A 1 29  ? -4.100  -10.922 -21.166 1.00 59.58 ? 72  PRO   A O   1 
ATOM   186  C  CB  . PRO   A 1 29  ? -2.123  -9.011  -22.792 1.00 61.82 ? 72  PRO   A CB  1 
ATOM   187  C  CG  . PRO   A 1 29  ? -3.072  -7.926  -23.289 1.00 62.47 ? 72  PRO   A CG  1 
ATOM   188  C  CD  . PRO   A 1 29  ? -4.382  -8.568  -23.627 1.00 61.02 ? 72  PRO   A CD  1 
ATOM   189  N  N   . ARG   A 1 30  ? -2.152  -12.057 -21.455 1.00 59.04 ? 73  ARG   A N   1 
ATOM   190  C  CA  . ARG   A 1 30  ? -2.260  -12.801 -20.189 1.00 59.05 ? 73  ARG   A CA  1 
ATOM   191  C  C   . ARG   A 1 30  ? -1.268  -12.199 -19.184 1.00 57.52 ? 73  ARG   A C   1 
ATOM   192  O  O   . ARG   A 1 30  ? -0.060  -12.414 -19.291 1.00 57.28 ? 73  ARG   A O   1 
ATOM   193  C  CB  . ARG   A 1 30  ? -2.013  -14.303 -20.370 1.00 61.96 ? 73  ARG   A CB  1 
ATOM   194  C  CG  . ARG   A 1 30  ? -3.269  -15.101 -20.702 1.00 67.35 ? 73  ARG   A CG  1 
ATOM   195  C  CD  . ARG   A 1 30  ? -2.952  -16.588 -20.829 1.00 72.71 ? 73  ARG   A CD  1 
ATOM   196  N  NE  . ARG   A 1 30  ? -3.614  -17.190 -21.993 1.00 77.17 ? 73  ARG   A NE  1 
ATOM   197  C  CZ  . ARG   A 1 30  ? -4.770  -17.847 -21.940 1.00 79.83 ? 73  ARG   A CZ  1 
ATOM   198  N  NH1 . ARG   A 1 30  ? -5.397  -18.012 -20.778 1.00 79.52 ? 73  ARG   A NH1 1 
ATOM   199  N  NH2 . ARG   A 1 30  ? -5.308  -18.349 -23.049 1.00 79.08 ? 73  ARG   A NH2 1 
ATOM   200  N  N   . LEU   A 1 31  ? -1.786  -11.434 -18.217 1.00 56.38 ? 74  LEU   A N   1 
ATOM   201  C  CA  . LEU   A 1 31  ? -0.968  -10.725 -17.233 1.00 55.53 ? 74  LEU   A CA  1 
ATOM   202  C  C   . LEU   A 1 31  ? -1.114  -11.257 -15.811 1.00 54.23 ? 74  LEU   A C   1 
ATOM   203  O  O   . LEU   A 1 31  ? -2.228  -11.391 -15.331 1.00 53.99 ? 74  LEU   A O   1 
ATOM   204  C  CB  . LEU   A 1 31  ? -1.368  -9.235  -17.230 1.00 55.59 ? 74  LEU   A CB  1 
ATOM   205  C  CG  . LEU   A 1 31  ? -1.403  -8.534  -18.579 1.00 56.55 ? 74  LEU   A CG  1 
ATOM   206  C  CD1 . LEU   A 1 31  ? -2.221  -7.290  -18.511 1.00 56.85 ? 74  LEU   A CD1 1 
ATOM   207  C  CD2 . LEU   A 1 31  ? -0.010  -8.221  -19.060 1.00 57.24 ? 74  LEU   A CD2 1 
ATOM   208  N  N   . ASP   A 1 32  ? 0.005   -11.466 -15.109 1.00 53.21 ? 75  ASP   A N   1 
ATOM   209  C  CA  . ASP   A 1 32  ? -0.001  -11.876 -13.709 1.00 52.77 ? 75  ASP   A CA  1 
ATOM   210  C  C   . ASP   A 1 32  ? -0.215  -10.611 -12.876 1.00 50.95 ? 75  ASP   A C   1 
ATOM   211  O  O   . ASP   A 1 32  ? 0.659   -9.744  -12.897 1.00 51.36 ? 75  ASP   A O   1 
ATOM   212  C  CB  . ASP   A 1 32  ? 1.356   -12.481 -13.343 1.00 56.13 ? 75  ASP   A CB  1 
ATOM   213  C  CG  . ASP   A 1 32  ? 1.516   -13.932 -13.733 1.00 63.84 ? 75  ASP   A CG  1 
ATOM   214  O  OD1 . ASP   A 1 32  ? 0.573   -14.719 -13.489 1.00 65.20 ? 75  ASP   A OD1 1 
ATOM   215  O  OD2 . ASP   A 1 32  ? 2.605   -14.294 -14.249 1.00 67.38 ? 75  ASP   A OD2 1 
ATOM   216  N  N   . VAL   A 1 33  ? -1.378  -10.456 -12.199 1.00 48.78 ? 76  VAL   A N   1 
ATOM   217  C  CA  . VAL   A 1 33  ? -1.624  -9.220  -11.439 1.00 47.63 ? 76  VAL   A CA  1 
ATOM   218  C  C   . VAL   A 1 33  ? -1.987  -9.490  -9.953  1.00 46.71 ? 76  VAL   A C   1 
ATOM   219  O  O   . VAL   A 1 33  ? -2.213  -10.635 -9.563  1.00 46.30 ? 76  VAL   A O   1 
ATOM   220  C  CB  . VAL   A 1 33  ? -2.651  -8.263  -12.134 1.00 47.39 ? 76  VAL   A CB  1 
ATOM   221  C  CG1 . VAL   A 1 33  ? -2.209  -7.882  -13.538 1.00 47.46 ? 76  VAL   A CG1 1 
ATOM   222  C  CG2 . VAL   A 1 33  ? -4.051  -8.850  -12.142 1.00 47.46 ? 76  VAL   A CG2 1 
ATOM   223  N  N   . ALA   A 1 34  ? -1.969  -8.434  -9.120  1.00 46.31 ? 77  ALA   A N   1 
ATOM   224  C  CA  . ALA   A 1 34  ? -2.330  -8.501  -7.704  1.00 46.25 ? 77  ALA   A CA  1 
ATOM   225  C  C   . ALA   A 1 34  ? -3.219  -7.316  -7.371  1.00 45.74 ? 77  ALA   A C   1 
ATOM   226  O  O   . ALA   A 1 34  ? -2.987  -6.217  -7.863  1.00 46.20 ? 77  ALA   A O   1 
ATOM   227  C  CB  . ALA   A 1 34  ? -1.088  -8.490  -6.828  1.00 46.41 ? 77  ALA   A CB  1 
ATOM   228  N  N   . LEU   A 1 35  ? -4.252  -7.536  -6.552  1.00 44.91 ? 78  LEU   A N   1 
ATOM   229  C  CA  . LEU   A 1 35  ? -5.206  -6.495  -6.187  1.00 44.07 ? 78  LEU   A CA  1 
ATOM   230  C  C   . LEU   A 1 35  ? -5.089  -6.145  -4.706  1.00 44.13 ? 78  LEU   A C   1 
ATOM   231  O  O   . LEU   A 1 35  ? -5.257  -7.005  -3.833  1.00 44.28 ? 78  LEU   A O   1 
ATOM   232  C  CB  . LEU   A 1 35  ? -6.621  -6.967  -6.535  1.00 43.47 ? 78  LEU   A CB  1 
ATOM   233  C  CG  . LEU   A 1 35  ? -7.746  -5.991  -6.260  1.00 43.40 ? 78  LEU   A CG  1 
ATOM   234  C  CD1 . LEU   A 1 35  ? -7.735  -4.884  -7.247  1.00 43.67 ? 78  LEU   A CD1 1 
ATOM   235  C  CD2 . LEU   A 1 35  ? -9.077  -6.687  -6.286  1.00 43.11 ? 78  LEU   A CD2 1 
ATOM   236  N  N   . ASP   A 1 36  ? -4.765  -4.888  -4.421  1.00 43.81 ? 79  ASP   A N   1 
ATOM   237  C  CA  . ASP   A 1 36  ? -4.635  -4.436  -3.050  1.00 43.90 ? 79  ASP   A CA  1 
ATOM   238  C  C   . ASP   A 1 36  ? -6.014  -4.082  -2.412  1.00 44.34 ? 79  ASP   A C   1 
ATOM   239  O  O   . ASP   A 1 36  ? -7.036  -4.013  -3.106  1.00 43.97 ? 79  ASP   A O   1 
ATOM   240  C  CB  . ASP   A 1 36  ? -3.600  -3.293  -2.957  1.00 45.49 ? 79  ASP   A CB  1 
ATOM   241  C  CG  . ASP   A 1 36  ? -4.033  -1.950  -3.514  1.00 50.73 ? 79  ASP   A CG  1 
ATOM   242  O  OD1 . ASP   A 1 36  ? -5.211  -1.819  -3.901  1.00 52.34 ? 79  ASP   A OD1 1 
ATOM   243  O  OD2 . ASP   A 1 36  ? -3.198  -1.022  -3.543  1.00 52.42 ? 79  ASP   A OD2 1 
ATOM   244  N  N   . GLU   A 1 37  ? -6.020  -3.848  -1.087  1.00 44.75 ? 80  GLU   A N   1 
ATOM   245  C  CA  . GLU   A 1 37  ? -7.194  -3.471  -0.305  1.00 45.36 ? 80  GLU   A CA  1 
ATOM   246  C  C   . GLU   A 1 37  ? -7.878  -2.192  -0.820  1.00 45.18 ? 80  GLU   A C   1 
ATOM   247  O  O   . GLU   A 1 37  ? -9.048  -1.978  -0.540  1.00 45.30 ? 80  GLU   A O   1 
ATOM   248  C  CB  . GLU   A 1 37  ? -6.791  -3.303  1.163   1.00 48.66 ? 80  GLU   A CB  1 
ATOM   249  C  CG  . GLU   A 1 37  ? -7.947  -3.373  2.144   1.00 55.11 ? 80  GLU   A CG  1 
ATOM   250  C  CD  . GLU   A 1 37  ? -7.567  -2.978  3.558   1.00 62.18 ? 80  GLU   A CD  1 
ATOM   251  O  OE1 . GLU   A 1 37  ? -7.278  -1.780  3.779   1.00 63.37 ? 80  GLU   A OE1 1 
ATOM   252  O  OE2 . GLU   A 1 37  ? -7.544  -3.866  4.442   1.00 64.68 ? 80  GLU   A OE2 1 
ATOM   253  N  N   . SER   A 1 38  ? -7.177  -1.370  -1.604  1.00 44.36 ? 81  SER   A N   1 
ATOM   254  C  CA  . SER   A 1 38  ? -7.754  -0.156  -2.180  1.00 43.68 ? 81  SER   A CA  1 
ATOM   255  C  C   . SER   A 1 38  ? -8.398  -0.366  -3.570  1.00 43.15 ? 81  SER   A C   1 
ATOM   256  O  O   . SER   A 1 38  ? -8.885  0.595   -4.173  1.00 43.72 ? 81  SER   A O   1 
ATOM   257  C  CB  . SER   A 1 38  ? -6.700  0.939   -2.258  1.00 44.12 ? 81  SER   A CB  1 
ATOM   258  O  OG  . SER   A 1 38  ? -6.119  1.108   -0.976  1.00 45.80 ? 81  SER   A OG  1 
ATOM   259  N  N   . GLY   A 1 39  ? -8.409  -1.598  -4.065  1.00 41.87 ? 82  GLY   A N   1 
ATOM   260  C  CA  . GLY   A 1 39  ? -8.972  -1.892  -5.373  1.00 41.23 ? 82  GLY   A CA  1 
ATOM   261  C  C   . GLY   A 1 39  ? -8.054  -1.507  -6.521  1.00 40.80 ? 82  GLY   A C   1 
ATOM   262  O  O   . GLY   A 1 39  ? -8.511  -1.359  -7.649  1.00 40.61 ? 82  GLY   A O   1 
ATOM   263  N  N   . ASP   A 1 40  ? -6.746  -1.360  -6.256  1.00 40.15 ? 83  ASP   A N   1 
ATOM   264  C  CA  . ASP   A 1 40  ? -5.784  -1.007  -7.292  1.00 39.53 ? 83  ASP   A CA  1 
ATOM   265  C  C   . ASP   A 1 40  ? -5.019  -2.249  -7.762  1.00 39.30 ? 83  ASP   A C   1 
ATOM   266  O  O   . ASP   A 1 40  ? -4.454  -2.972  -6.938  1.00 39.33 ? 83  ASP   A O   1 
ATOM   267  C  CB  . ASP   A 1 40  ? -4.785  0.044   -6.771  1.00 39.89 ? 83  ASP   A CB  1 
ATOM   268  C  CG  . ASP   A 1 40  ? -5.420  1.340   -6.333  1.00 42.70 ? 83  ASP   A CG  1 
ATOM   269  O  OD1 . ASP   A 1 40  ? -6.456  1.698   -6.886  1.00 43.31 ? 83  ASP   A OD1 1 
ATOM   270  O  OD2 . ASP   A 1 40  ? -4.874  1.990   -5.426  1.00 45.65 ? 83  ASP   A OD2 1 
ATOM   271  N  N   . PHE   A 1 41  ? -4.979  -2.479  -9.079  1.00 39.09 ? 84  PHE   A N   1 
ATOM   272  C  CA  . PHE   A 1 41  ? -4.219  -3.583  -9.660  1.00 39.71 ? 84  PHE   A CA  1 
ATOM   273  C  C   . PHE   A 1 41  ? -2.750  -3.183  -9.850  1.00 41.77 ? 84  PHE   A C   1 
ATOM   274  O  O   . PHE   A 1 41  ? -2.408  -2.002  -9.984  1.00 41.29 ? 84  PHE   A O   1 
ATOM   275  C  CB  . PHE   A 1 41  ? -4.814  -4.044  -11.007 1.00 38.39 ? 84  PHE   A CB  1 
ATOM   276  C  CG  . PHE   A 1 41  ? -6.150  -4.736  -10.910 1.00 37.68 ? 84  PHE   A CG  1 
ATOM   277  C  CD1 . PHE   A 1 41  ? -6.236  -6.058  -10.514 1.00 37.91 ? 84  PHE   A CD1 1 
ATOM   278  C  CD2 . PHE   A 1 41  ? -7.325  -4.058  -11.199 1.00 37.77 ? 84  PHE   A CD2 1 
ATOM   279  C  CE1 . PHE   A 1 41  ? -7.468  -6.693  -10.421 1.00 38.44 ? 84  PHE   A CE1 1 
ATOM   280  C  CE2 . PHE   A 1 41  ? -8.555  -4.696  -11.113 1.00 38.12 ? 84  PHE   A CE2 1 
ATOM   281  C  CZ  . PHE   A 1 41  ? -8.623  -6.004  -10.711 1.00 37.97 ? 84  PHE   A CZ  1 
ATOM   282  N  N   . SER   A 1 42  ? -1.878  -4.177  -9.839  1.00 43.76 ? 85  SER   A N   1 
ATOM   283  C  CA  . SER   A 1 42  ? -0.454  -3.967  -10.047 1.00 46.33 ? 85  SER   A CA  1 
ATOM   284  C  C   . SER   A 1 42  ? 0.116   -5.197  -10.729 1.00 49.02 ? 85  SER   A C   1 
ATOM   285  O  O   . SER   A 1 42  ? -0.337  -6.317  -10.464 1.00 49.05 ? 85  SER   A O   1 
ATOM   286  C  CB  . SER   A 1 42  ? 0.263   -3.684  -8.727  1.00 48.04 ? 85  SER   A CB  1 
ATOM   287  O  OG  . SER   A 1 42  ? 0.197   -4.773  -7.819  1.00 50.47 ? 85  SER   A OG  1 
ATOM   288  N  N   . LEU   A 1 43  ? 1.073   -4.995  -11.643 1.00 50.97 ? 86  LEU   A N   1 
ATOM   289  C  CA  . LEU   A 1 43  ? 1.668   -6.110  -12.361 1.00 53.37 ? 86  LEU   A CA  1 
ATOM   290  C  C   . LEU   A 1 43  ? 2.671   -6.847  -11.506 1.00 55.49 ? 86  LEU   A C   1 
ATOM   291  O  O   . LEU   A 1 43  ? 3.620   -6.254  -10.990 1.00 55.55 ? 86  LEU   A O   1 
ATOM   292  C  CB  . LEU   A 1 43  ? 2.362   -5.632  -13.638 1.00 54.02 ? 86  LEU   A CB  1 
ATOM   293  C  CG  . LEU   A 1 43  ? 1.466   -5.343  -14.826 1.00 56.39 ? 86  LEU   A CG  1 
ATOM   294  C  CD1 . LEU   A 1 43  ? 2.265   -4.743  -15.959 1.00 57.20 ? 86  LEU   A CD1 1 
ATOM   295  C  CD2 . LEU   A 1 43  ? 0.772   -6.600  -15.307 1.00 57.45 ? 86  LEU   A CD2 1 
ATOM   296  N  N   . VAL   A 1 44  ? 2.480   -8.154  -11.391 1.00 56.99 ? 87  VAL   A N   1 
ATOM   297  C  CA  . VAL   A 1 44  ? 3.399   -9.046  -10.697 1.00 58.76 ? 87  VAL   A CA  1 
ATOM   298  C  C   . VAL   A 1 44  ? 4.303   -9.610  -11.782 1.00 61.12 ? 87  VAL   A C   1 
ATOM   299  O  O   . VAL   A 1 44  ? 3.789   -10.073 -12.808 1.00 61.80 ? 87  VAL   A O   1 
ATOM   300  C  CB  . VAL   A 1 44  ? 2.628   -10.189 -10.006 1.00 59.17 ? 87  VAL   A CB  1 
ATOM   301  C  CG1 . VAL   A 1 44  ? 3.584   -11.130 -9.290  1.00 59.55 ? 87  VAL   A CG1 1 
ATOM   302  C  CG2 . VAL   A 1 44  ? 1.574   -9.642  -9.053  1.00 59.61 ? 87  VAL   A CG2 1 
ATOM   303  N  N   . GLU   A 1 45  ? 5.633   -9.553  -11.600 1.00 62.09 ? 88  GLU   A N   1 
ATOM   304  C  CA  . GLU   A 1 45  ? 6.537   -10.081 -12.628 1.00 63.66 ? 88  GLU   A CA  1 
ATOM   305  C  C   . GLU   A 1 45  ? 7.539   -11.135 -12.089 1.00 64.16 ? 88  GLU   A C   1 
ATOM   306  O  O   . GLU   A 1 45  ? 7.680   -12.216 -12.675 1.00 64.15 ? 88  GLU   A O   1 
ATOM   307  C  CB  . GLU   A 1 45  ? 7.252   -8.940  -13.375 1.00 66.68 ? 88  GLU   A CB  1 
ATOM   308  C  CG  . GLU   A 1 45  ? 6.317   -8.031  -14.154 1.00 71.49 ? 88  GLU   A CG  1 
ATOM   309  C  CD  . GLU   A 1 45  ? 5.708   -8.726  -15.353 1.00 76.94 ? 88  GLU   A CD  1 
ATOM   310  O  OE1 . GLU   A 1 45  ? 4.465   -8.665  -15.516 1.00 76.48 ? 88  GLU   A OE1 1 
ATOM   311  O  OE2 . GLU   A 1 45  ? 6.479   -9.366  -16.108 1.00 78.48 ? 88  GLU   A OE2 1 
ATOM   312  N  N   . THR   B 2 9   ? -34.570 8.100   -15.497 1.00 49.54 ? 18  THR   B N   1 
ATOM   313  C  CA  . THR   B 2 9   ? -34.345 6.725   -15.039 1.00 50.62 ? 18  THR   B CA  1 
ATOM   314  C  C   . THR   B 2 9   ? -34.549 5.639   -16.093 1.00 49.86 ? 18  THR   B C   1 
ATOM   315  O  O   . THR   B 2 9   ? -34.662 4.468   -15.727 1.00 50.38 ? 18  THR   B O   1 
ATOM   316  C  CB  . THR   B 2 9   ? -35.182 6.382   -13.807 1.00 53.47 ? 18  THR   B CB  1 
ATOM   317  O  OG1 . THR   B 2 9   ? -36.529 6.839   -13.998 1.00 55.20 ? 18  THR   B OG1 1 
ATOM   318  C  CG2 . THR   B 2 9   ? -34.577 6.933   -12.522 1.00 54.37 ? 18  THR   B CG2 1 
ATOM   319  N  N   . THR   B 2 10  ? -34.592 6.004   -17.381 1.00 48.37 ? 19  THR   B N   1 
ATOM   320  C  CA  . THR   B 2 10  ? -34.750 5.032   -18.466 1.00 47.32 ? 19  THR   B CA  1 
ATOM   321  C  C   . THR   B 2 10  ? -33.492 4.160   -18.526 1.00 45.53 ? 19  THR   B C   1 
ATOM   322  O  O   . THR   B 2 10  ? -32.397 4.683   -18.378 1.00 45.41 ? 19  THR   B O   1 
ATOM   323  C  CB  . THR   B 2 10  ? -34.972 5.775   -19.828 1.00 49.00 ? 19  THR   B CB  1 
ATOM   324  O  OG1 . THR   B 2 10  ? -36.171 6.564   -19.799 1.00 50.08 ? 19  THR   B OG1 1 
ATOM   325  C  CG2 . THR   B 2 10  ? -35.027 4.829   -21.019 1.00 49.35 ? 19  THR   B CG2 1 
ATOM   326  N  N   . ASP   B 2 11  ? -33.629 2.842   -18.762 1.00 44.21 ? 20  ASP   B N   1 
ATOM   327  C  CA  . ASP   B 2 11  ? -32.498 1.916   -18.914 1.00 43.20 ? 20  ASP   B CA  1 
ATOM   328  C  C   . ASP   B 2 11  ? -31.518 2.441   -19.999 1.00 41.66 ? 20  ASP   B C   1 
ATOM   329  O  O   . ASP   B 2 11  ? -31.967 3.095   -20.939 1.00 41.77 ? 20  ASP   B O   1 
ATOM   330  C  CB  . ASP   B 2 11  ? -33.033 0.542   -19.362 1.00 45.65 ? 20  ASP   B CB  1 
ATOM   331  C  CG  . ASP   B 2 11  ? -33.197 -0.505  -18.272 1.00 51.92 ? 20  ASP   B CG  1 
ATOM   332  O  OD1 . ASP   B 2 11  ? -33.974 -0.257  -17.320 1.00 52.82 ? 20  ASP   B OD1 1 
ATOM   333  O  OD2 . ASP   B 2 11  ? -32.566 -1.589  -18.388 1.00 54.65 ? 20  ASP   B OD2 1 
ATOM   334  N  N   . GLY   B 2 12  ? -30.216 2.169   -19.866 1.00 40.01 ? 21  GLY   B N   1 
ATOM   335  C  CA  . GLY   B 2 12  ? -29.234 2.617   -20.846 1.00 39.13 ? 21  GLY   B CA  1 
ATOM   336  C  C   . GLY   B 2 12  ? -27.903 3.051   -20.265 1.00 39.08 ? 21  GLY   B C   1 
ATOM   337  O  O   . GLY   B 2 12  ? -27.675 2.914   -19.071 1.00 39.32 ? 21  GLY   B O   1 
ATOM   338  N  N   . VAL   B 2 13  ? -26.977 3.533   -21.110 1.00 38.71 ? 22  VAL   B N   1 
ATOM   339  C  CA  . VAL   B 2 13  ? -25.667 4.004   -20.651 1.00 38.33 ? 22  VAL   B CA  1 
ATOM   340  C  C   . VAL   B 2 13  ? -25.694 5.540   -20.473 1.00 37.75 ? 22  VAL   B C   1 
ATOM   341  O  O   . VAL   B 2 13  ? -26.389 6.239   -21.216 1.00 37.57 ? 22  VAL   B O   1 
ATOM   342  C  CB  . VAL   B 2 13  ? -24.516 3.482   -21.542 1.00 39.65 ? 22  VAL   B CB  1 
ATOM   343  C  CG1 . VAL   B 2 13  ? -24.621 3.999   -22.977 1.00 40.17 ? 22  VAL   B CG1 1 
ATOM   344  C  CG2 . VAL   B 2 13  ? -23.158 3.797   -20.938 1.00 40.45 ? 22  VAL   B CG2 1 
ATOM   345  N  N   . TYR   B 2 14  ? -25.056 6.048   -19.401 1.00 37.13 ? 23  TYR   B N   1 
ATOM   346  C  CA  . TYR   B 2 14  ? -25.088 7.462   -19.040 1.00 36.38 ? 23  TYR   B CA  1 
ATOM   347  C  C   . TYR   B 2 14  ? -23.704 8.046   -18.776 1.00 36.51 ? 23  TYR   B C   1 
ATOM   348  O  O   . TYR   B 2 14  ? -22.814 7.356   -18.295 1.00 36.66 ? 23  TYR   B O   1 
ATOM   349  C  CB  . TYR   B 2 14  ? -25.923 7.649   -17.755 1.00 35.96 ? 23  TYR   B CB  1 
ATOM   350  C  CG  . TYR   B 2 14  ? -27.415 7.480   -17.937 1.00 35.59 ? 23  TYR   B CG  1 
ATOM   351  C  CD1 . TYR   B 2 14  ? -27.968 6.234   -18.185 1.00 35.78 ? 23  TYR   B CD1 1 
ATOM   352  C  CD2 . TYR   B 2 14  ? -28.279 8.546   -17.753 1.00 36.41 ? 23  TYR   B CD2 1 
ATOM   353  C  CE1 . TYR   B 2 14  ? -29.329 6.073   -18.366 1.00 36.47 ? 23  TYR   B CE1 1 
ATOM   354  C  CE2 . TYR   B 2 14  ? -29.648 8.400   -17.928 1.00 37.20 ? 23  TYR   B CE2 1 
ATOM   355  C  CZ  . TYR   B 2 14  ? -30.172 7.153   -18.210 1.00 37.65 ? 23  TYR   B CZ  1 
ATOM   356  O  OH  . TYR   B 2 14  ? -31.521 6.975   -18.376 1.00 38.50 ? 23  TYR   B OH  1 
ATOM   357  N  N   . ARG   B 2 15  ? -23.542 9.344   -19.034 1.00 36.11 ? 24  ARG   B N   1 
ATOM   358  C  CA  . ARG   B 2 15  ? -22.317 10.045  -18.712 1.00 36.22 ? 24  ARG   B CA  1 
ATOM   359  C  C   . ARG   B 2 15  ? -22.459 10.555  -17.252 1.00 36.32 ? 24  ARG   B C   1 
ATOM   360  O  O   . ARG   B 2 15  ? -23.551 10.906  -16.821 1.00 35.41 ? 24  ARG   B O   1 
ATOM   361  C  CB  . ARG   B 2 15  ? -22.123 11.250  -19.655 1.00 37.48 ? 24  ARG   B CB  1 
ATOM   362  C  CG  . ARG   B 2 15  ? -21.829 10.907  -21.110 1.00 39.93 ? 24  ARG   B CG  1 
ATOM   363  C  CD  . ARG   B 2 15  ? -21.524 12.163  -21.918 1.00 42.92 ? 24  ARG   B CD  1 
ATOM   364  N  NE  . ARG   B 2 15  ? -21.772 11.940  -23.341 1.00 44.85 ? 24  ARG   B NE  1 
ATOM   365  C  CZ  . ARG   B 2 15  ? -20.864 11.503  -24.205 1.00 45.58 ? 24  ARG   B CZ  1 
ATOM   366  N  NH1 . ARG   B 2 15  ? -19.609 11.303  -23.818 1.00 44.40 ? 24  ARG   B NH1 1 
ATOM   367  N  NH2 . ARG   B 2 15  ? -21.200 11.273  -25.464 1.00 45.01 ? 24  ARG   B NH2 1 
ATOM   368  N  N   . VAL   B 2 16  ? -21.354 10.592  -16.509 1.00 36.73 ? 25  VAL   B N   1 
ATOM   369  C  CA  . VAL   B 2 16  ? -21.292 11.110  -15.152 1.00 37.57 ? 25  VAL   B CA  1 
ATOM   370  C  C   . VAL   B 2 16  ? -20.434 12.362  -15.256 1.00 38.60 ? 25  VAL   B C   1 
ATOM   371  O  O   . VAL   B 2 16  ? -19.245 12.283  -15.576 1.00 38.48 ? 25  VAL   B O   1 
ATOM   372  C  CB  . VAL   B 2 16  ? -20.704 10.087  -14.147 1.00 38.13 ? 25  VAL   B CB  1 
ATOM   373  C  CG1 . VAL   B 2 16  ? -20.617 10.690  -12.751 1.00 38.23 ? 25  VAL   B CG1 1 
ATOM   374  C  CG2 . VAL   B 2 16  ? -21.508 8.788   -14.140 1.00 38.48 ? 25  VAL   B CG2 1 
ATOM   375  N  N   . MET   B 2 17  ? -21.056 13.516  -15.059 1.00 39.72 ? 26  MET   B N   1 
ATOM   376  C  CA  . MET   B 2 17  ? -20.437 14.822  -15.233 1.00 41.63 ? 26  MET   B CA  1 
ATOM   377  C  C   . MET   B 2 17  ? -20.286 15.596  -13.925 1.00 44.60 ? 26  MET   B C   1 
ATOM   378  O  O   . MET   B 2 17  ? -20.941 15.267  -12.941 1.00 45.29 ? 26  MET   B O   1 
ATOM   379  C  CB  . MET   B 2 17  ? -21.322 15.660  -16.177 1.00 41.72 ? 26  MET   B CB  1 
ATOM   380  C  CG  . MET   B 2 17  ? -21.820 14.939  -17.424 1.00 42.40 ? 26  MET   B CG  1 
ATOM   381  S  SD  . MET   B 2 17  ? -20.528 14.716  -18.659 1.00 45.42 ? 26  MET   B SD  1 
ATOM   382  C  CE  . MET   B 2 17  ? -19.996 16.408  -18.871 1.00 46.01 ? 26  MET   B CE  1 
ATOM   383  N  N   . THR   B 2 18  ? -19.459 16.659  -13.928 1.00 46.54 ? 27  THR   B N   1 
ATOM   384  C  CA  . THR   B 2 18  ? -19.288 17.556  -12.788 1.00 48.86 ? 27  THR   B CA  1 
ATOM   385  C  C   . THR   B 2 18  ? -19.030 19.029  -13.218 1.00 51.31 ? 27  THR   B C   1 
ATOM   386  O  O   . THR   B 2 18  ? -18.458 19.297  -14.277 1.00 51.15 ? 27  THR   B O   1 
ATOM   387  C  CB  . THR   B 2 18  ? -18.232 17.042  -11.814 1.00 50.28 ? 27  THR   B CB  1 
ATOM   388  O  OG1 . THR   B 2 18  ? -18.444 17.671  -10.550 1.00 52.23 ? 27  THR   B OG1 1 
ATOM   389  C  CG2 . THR   B 2 18  ? -16.827 17.317  -12.282 1.00 50.40 ? 27  THR   B CG2 1 
ATOM   390  N  N   . ARG   B 2 19  ? -19.466 19.980  -12.386 1.00 53.24 ? 28  ARG   B N   1 
ATOM   391  C  CA  . ARG   B 2 19  ? -19.243 21.401  -12.655 1.00 55.51 ? 28  ARG   B CA  1 
ATOM   392  C  C   . ARG   B 2 19  ? -18.222 22.068  -11.695 1.00 56.95 ? 28  ARG   B C   1 
ATOM   393  O  O   . ARG   B 2 19  ? -17.934 23.261  -11.835 1.00 56.92 ? 28  ARG   B O   1 
ATOM   394  C  CB  . ARG   B 2 19  ? -20.572 22.162  -12.677 1.00 57.66 ? 28  ARG   B CB  1 
ATOM   395  C  CG  . ARG   B 2 19  ? -21.505 21.653  -13.762 1.00 62.11 ? 28  ARG   B CG  1 
ATOM   396  C  CD  . ARG   B 2 19  ? -22.201 22.787  -14.485 1.00 66.46 ? 28  ARG   B CD  1 
ATOM   397  N  NE  . ARG   B 2 19  ? -23.202 22.312  -15.445 1.00 70.31 ? 28  ARG   B NE  1 
ATOM   398  C  CZ  . ARG   B 2 19  ? -24.468 22.035  -15.138 1.00 72.91 ? 28  ARG   B CZ  1 
ATOM   399  N  NH1 . ARG   B 2 19  ? -24.899 22.163  -13.886 1.00 72.02 ? 28  ARG   B NH1 1 
ATOM   400  N  NH2 . ARG   B 2 19  ? -25.309 21.616  -16.077 1.00 73.07 ? 28  ARG   B NH2 1 
ATOM   401  N  N   . ARG   B 2 20  ? -17.658 21.272  -10.755 1.00 57.80 ? 29  ARG   B N   1 
ATOM   402  C  CA  . ARG   B 2 20  ? -16.671 21.619  -9.729  1.00 58.81 ? 29  ARG   B CA  1 
ATOM   403  C  C   . ARG   B 2 20  ? -15.358 22.164  -10.348 1.00 58.74 ? 29  ARG   B C   1 
ATOM   404  O  O   . ARG   B 2 20  ? -14.709 23.036  -9.767  1.00 58.78 ? 29  ARG   B O   1 
ATOM   405  C  CB  . ARG   B 2 20  ? -16.398 20.363  -8.865  1.00 61.09 ? 29  ARG   B CB  1 
ATOM   406  C  CG  . ARG   B 2 20  ? -15.481 20.577  -7.663  1.00 66.07 ? 29  ARG   B CG  1 
ATOM   407  C  CD  . ARG   B 2 20  ? -15.150 19.269  -6.939  1.00 70.52 ? 29  ARG   B CD  1 
ATOM   408  N  NE  . ARG   B 2 20  ? -14.142 18.456  -7.631  1.00 74.13 ? 29  ARG   B NE  1 
ATOM   409  C  CZ  . ARG   B 2 20  ? -12.842 18.454  -7.334  1.00 76.95 ? 29  ARG   B CZ  1 
ATOM   410  N  NH1 . ARG   B 2 20  ? -12.374 19.233  -6.364  1.00 76.95 ? 29  ARG   B NH1 1 
ATOM   411  N  NH2 . ARG   B 2 20  ? -12.000 17.679  -8.010  1.00 76.58 ? 29  ARG   B NH2 1 
ATOM   412  N  N   . LEU   B 2 21  ? -14.987 21.663  -11.536 1.00 58.37 ? 30  LEU   B N   1 
ATOM   413  C  CA  . LEU   B 2 21  ? -13.768 22.068  -12.241 1.00 58.19 ? 30  LEU   B CA  1 
ATOM   414  C  C   . LEU   B 2 21  ? -14.086 23.085  -13.380 1.00 57.86 ? 30  LEU   B C   1 
ATOM   415  O  O   . LEU   B 2 21  ? -15.083 23.812  -13.283 1.00 58.17 ? 30  LEU   B O   1 
ATOM   416  C  CB  . LEU   B 2 21  ? -13.029 20.810  -12.756 1.00 58.37 ? 30  LEU   B CB  1 
ATOM   417  C  CG  . LEU   B 2 21  ? -12.535 19.838  -11.692 1.00 60.05 ? 30  LEU   B CG  1 
ATOM   418  C  CD1 . LEU   B 2 21  ? -13.510 18.719  -11.497 1.00 60.90 ? 30  LEU   B CD1 1 
ATOM   419  C  CD2 . LEU   B 2 21  ? -11.200 19.239  -12.084 1.00 60.70 ? 30  LEU   B CD2 1 
ATOM   420  N  N   . LEU   B 2 22  ? -13.234 23.171  -14.432 1.00 56.88 ? 31  LEU   B N   1 
ATOM   421  C  CA  . LEU   B 2 22  ? -13.459 24.071  -15.561 1.00 56.07 ? 31  LEU   B CA  1 
ATOM   422  C  C   . LEU   B 2 22  ? -14.532 23.489  -16.472 1.00 55.07 ? 31  LEU   B C   1 
ATOM   423  O  O   . LEU   B 2 22  ? -14.432 22.325  -16.875 1.00 55.33 ? 31  LEU   B O   1 
ATOM   424  C  CB  . LEU   B 2 22  ? -12.166 24.254  -16.355 1.00 56.09 ? 31  LEU   B CB  1 
ATOM   425  C  CG  . LEU   B 2 22  ? -12.208 25.387  -17.359 1.00 57.21 ? 31  LEU   B CG  1 
ATOM   426  C  CD1 . LEU   B 2 22  ? -11.788 26.696  -16.722 1.00 57.25 ? 31  LEU   B CD1 1 
ATOM   427  C  CD2 . LEU   B 2 22  ? -11.362 25.064  -18.553 1.00 58.00 ? 31  LEU   B CD2 1 
ATOM   428  N  N   . GLY   B 2 23  ? -15.556 24.288  -16.760 1.00 53.80 ? 32  GLY   B N   1 
ATOM   429  C  CA  . GLY   B 2 23  ? -16.683 23.873  -17.587 1.00 53.19 ? 32  GLY   B CA  1 
ATOM   430  C  C   . GLY   B 2 23  ? -17.409 22.649  -17.059 1.00 52.13 ? 32  GLY   B C   1 
ATOM   431  O  O   . GLY   B 2 23  ? -17.506 22.449  -15.844 1.00 51.76 ? 32  GLY   B O   1 
ATOM   432  N  N   . SER   B 2 24  ? -17.892 21.802  -17.980 1.00 51.33 ? 33  SER   B N   1 
ATOM   433  C  CA  . SER   B 2 24  ? -18.546 20.540  -17.637 1.00 50.79 ? 33  SER   B CA  1 
ATOM   434  C  C   . SER   B 2 24  ? -17.547 19.397  -17.913 1.00 49.72 ? 33  SER   B C   1 
ATOM   435  O  O   . SER   B 2 24  ? -17.323 19.047  -19.072 1.00 49.58 ? 33  SER   B O   1 
ATOM   436  C  CB  . SER   B 2 24  ? -19.814 20.351  -18.466 1.00 51.99 ? 33  SER   B CB  1 
ATOM   437  O  OG  . SER   B 2 24  ? -20.764 21.375  -18.213 1.00 54.18 ? 33  SER   B OG  1 
ATOM   438  N  N   . THR   B 2 25  ? -16.921 18.841  -16.858 1.00 48.67 ? 34  THR   B N   1 
ATOM   439  C  CA  . THR   B 2 25  ? -15.937 17.775  -17.048 1.00 48.04 ? 34  THR   B CA  1 
ATOM   440  C  C   . THR   B 2 25  ? -16.577 16.399  -16.835 1.00 47.12 ? 34  THR   B C   1 
ATOM   441  O  O   . THR   B 2 25  ? -17.349 16.221  -15.888 1.00 47.78 ? 34  THR   B O   1 
ATOM   442  C  CB  . THR   B 2 25  ? -14.664 18.024  -16.198 1.00 49.24 ? 34  THR   B CB  1 
ATOM   443  O  OG1 . THR   B 2 25  ? -14.092 19.294  -16.547 1.00 50.71 ? 34  THR   B OG1 1 
ATOM   444  C  CG2 . THR   B 2 25  ? -13.612 16.955  -16.397 1.00 49.22 ? 34  THR   B CG2 1 
ATOM   445  N  N   . GLN   B 2 26  ? -16.294 15.436  -17.740 1.00 45.42 ? 35  GLN   B N   1 
ATOM   446  C  CA  . GLN   B 2 26  ? -16.841 14.086  -17.622 1.00 43.96 ? 35  GLN   B CA  1 
ATOM   447  C  C   . GLN   B 2 26  ? -15.920 13.252  -16.761 1.00 43.78 ? 35  GLN   B C   1 
ATOM   448  O  O   . GLN   B 2 26  ? -14.794 12.979  -17.172 1.00 44.51 ? 35  GLN   B O   1 
ATOM   449  C  CB  . GLN   B 2 26  ? -17.020 13.428  -18.995 1.00 43.07 ? 35  GLN   B CB  1 
ATOM   450  C  CG  . GLN   B 2 26  ? -17.707 12.086  -18.875 1.00 42.63 ? 35  GLN   B CG  1 
ATOM   451  C  CD  . GLN   B 2 26  ? -17.876 11.398  -20.189 1.00 42.49 ? 35  GLN   B CD  1 
ATOM   452  O  OE1 . GLN   B 2 26  ? -18.430 11.956  -21.142 1.00 43.01 ? 35  GLN   B OE1 1 
ATOM   453  N  NE2 . GLN   B 2 26  ? -17.424 10.161  -20.264 1.00 40.44 ? 35  GLN   B NE2 1 
ATOM   454  N  N   . VAL   B 2 27  ? -16.376 12.857  -15.560 1.00 42.67 ? 36  VAL   B N   1 
ATOM   455  C  CA  . VAL   B 2 27  ? -15.549 12.084  -14.621 1.00 41.82 ? 36  VAL   B CA  1 
ATOM   456  C  C   . VAL   B 2 27  ? -15.637 10.551  -14.833 1.00 41.21 ? 36  VAL   B C   1 
ATOM   457  O  O   . VAL   B 2 27  ? -14.735 9.805   -14.439 1.00 41.53 ? 36  VAL   B O   1 
ATOM   458  C  CB  . VAL   B 2 27  ? -15.862 12.491  -13.150 1.00 41.79 ? 36  VAL   B CB  1 
ATOM   459  C  CG1 . VAL   B 2 27  ? -15.618 13.972  -12.941 1.00 42.35 ? 36  VAL   B CG1 1 
ATOM   460  C  CG2 . VAL   B 2 27  ? -17.290 12.151  -12.764 1.00 41.48 ? 36  VAL   B CG2 1 
ATOM   461  N  N   . GLY   B 2 28  ? -16.709 10.100  -15.463 1.00 40.15 ? 37  GLY   B N   1 
ATOM   462  C  CA  . GLY   B 2 28  ? -16.922 8.687   -15.712 1.00 39.44 ? 37  GLY   B CA  1 
ATOM   463  C  C   . GLY   B 2 28  ? -18.229 8.416   -16.418 1.00 39.02 ? 37  GLY   B C   1 
ATOM   464  O  O   . GLY   B 2 28  ? -18.869 9.337   -16.938 1.00 39.46 ? 37  GLY   B O   1 
ATOM   465  N  N   . VAL   B 2 29  ? -18.619 7.129   -16.458 1.00 37.88 ? 38  VAL   B N   1 
ATOM   466  C  CA  . VAL   B 2 29  ? -19.785 6.563   -17.149 1.00 37.19 ? 38  VAL   B CA  1 
ATOM   467  C  C   . VAL   B 2 29  ? -20.486 5.514   -16.234 1.00 36.97 ? 38  VAL   B C   1 
ATOM   468  O  O   . VAL   B 2 29  ? -19.881 4.994   -15.286 1.00 36.48 ? 38  VAL   B O   1 
ATOM   469  C  CB  . VAL   B 2 29  ? -19.284 5.920   -18.489 1.00 36.96 ? 38  VAL   B CB  1 
ATOM   470  C  CG1 . VAL   B 2 29  ? -20.384 5.198   -19.255 1.00 37.12 ? 38  VAL   B CG1 1 
ATOM   471  C  CG2 . VAL   B 2 29  ? -18.603 6.942   -19.380 1.00 36.92 ? 38  VAL   B CG2 1 
ATOM   472  N  N   . GLY   B 2 30  ? -21.745 5.205   -16.529 1.00 36.79 ? 39  GLY   B N   1 
ATOM   473  C  CA  . GLY   B 2 30  ? -22.470 4.195   -15.773 1.00 37.20 ? 39  GLY   B CA  1 
ATOM   474  C  C   . GLY   B 2 30  ? -23.674 3.618   -16.484 1.00 37.46 ? 39  GLY   B C   1 
ATOM   475  O  O   . GLY   B 2 30  ? -24.154 4.188   -17.455 1.00 37.82 ? 39  GLY   B O   1 
ATOM   476  N  N   . VAL   B 2 31  ? -24.209 2.513   -15.963 1.00 37.13 ? 40  VAL   B N   1 
ATOM   477  C  CA  . VAL   B 2 31  ? -25.346 1.814   -16.546 1.00 36.82 ? 40  VAL   B CA  1 
ATOM   478  C  C   . VAL   B 2 31  ? -26.587 1.946   -15.695 1.00 36.88 ? 40  VAL   B C   1 
ATOM   479  O  O   . VAL   B 2 31  ? -26.549 1.630   -14.515 1.00 37.37 ? 40  VAL   B O   1 
ATOM   480  C  CB  . VAL   B 2 31  ? -24.983 0.319   -16.704 1.00 36.99 ? 40  VAL   B CB  1 
ATOM   481  C  CG1 . VAL   B 2 31  ? -26.171 -0.508  -17.182 1.00 37.20 ? 40  VAL   B CG1 1 
ATOM   482  C  CG2 . VAL   B 2 31  ? -23.786 0.150   -17.616 1.00 37.67 ? 40  VAL   B CG2 1 
ATOM   483  N  N   . MET   B 2 32  ? -27.700 2.326   -16.300 1.00 36.62 ? 41  MET   B N   1 
ATOM   484  C  CA  . MET   B 2 32  ? -28.978 2.363   -15.618 1.00 37.22 ? 41  MET   B CA  1 
ATOM   485  C  C   . MET   B 2 32  ? -29.693 1.076   -16.016 1.00 38.04 ? 41  MET   B C   1 
ATOM   486  O  O   . MET   B 2 32  ? -29.866 0.835   -17.204 1.00 38.89 ? 41  MET   B O   1 
ATOM   487  C  CB  . MET   B 2 32  ? -29.795 3.566   -16.095 1.00 37.40 ? 41  MET   B CB  1 
ATOM   488  C  CG  . MET   B 2 32  ? -31.081 3.761   -15.347 1.00 40.23 ? 41  MET   B CG  1 
ATOM   489  S  SD  . MET   B 2 32  ? -30.835 4.276   -13.626 1.00 47.09 ? 41  MET   B SD  1 
ATOM   490  C  CE  . MET   B 2 32  ? -30.171 5.888   -13.889 1.00 44.80 ? 41  MET   B CE  1 
ATOM   491  N  N   . GLN   B 2 33  ? -30.058 0.232   -15.054 1.00 37.93 ? 42  GLN   B N   1 
ATOM   492  C  CA  . GLN   B 2 33  ? -30.773 -1.000  -15.349 1.00 38.75 ? 42  GLN   B CA  1 
ATOM   493  C  C   . GLN   B 2 33  ? -31.704 -1.347  -14.204 1.00 39.65 ? 42  GLN   B C   1 
ATOM   494  O  O   . GLN   B 2 33  ? -31.242 -1.490  -13.074 1.00 40.35 ? 42  GLN   B O   1 
ATOM   495  C  CB  . GLN   B 2 33  ? -29.807 -2.151  -15.612 1.00 40.68 ? 42  GLN   B CB  1 
ATOM   496  C  CG  . GLN   B 2 33  ? -30.520 -3.353  -16.189 1.00 45.69 ? 42  GLN   B CG  1 
ATOM   497  C  CD  . GLN   B 2 33  ? -29.552 -4.432  -16.575 1.00 51.43 ? 42  GLN   B CD  1 
ATOM   498  O  OE1 . GLN   B 2 33  ? -29.504 -5.505  -15.954 1.00 53.17 ? 42  GLN   B OE1 1 
ATOM   499  N  NE2 . GLN   B 2 33  ? -28.757 -4.167  -17.608 1.00 52.50 ? 42  GLN   B NE2 1 
ATOM   500  N  N   . GLU   B 2 34  ? -33.006 -1.485  -14.486 1.00 39.63 ? 43  GLU   B N   1 
ATOM   501  C  CA  . GLU   B 2 34  ? -34.012 -1.793  -13.474 1.00 40.68 ? 43  GLU   B CA  1 
ATOM   502  C  C   . GLU   B 2 34  ? -34.087 -0.732  -12.336 1.00 40.79 ? 43  GLU   B C   1 
ATOM   503  O  O   . GLU   B 2 34  ? -34.230 -1.082  -11.161 1.00 41.45 ? 43  GLU   B O   1 
ATOM   504  C  CB  . GLU   B 2 34  ? -33.843 -3.217  -12.908 1.00 44.09 ? 43  GLU   B CB  1 
ATOM   505  C  CG  . GLU   B 2 34  ? -33.751 -4.317  -13.954 1.00 50.64 ? 43  GLU   B CG  1 
ATOM   506  C  CD  . GLU   B 2 34  ? -33.259 -5.649  -13.414 1.00 59.37 ? 43  GLU   B CD  1 
ATOM   507  O  OE1 . GLU   B 2 34  ? -33.679 -6.025  -12.296 1.00 61.73 ? 43  GLU   B OE1 1 
ATOM   508  O  OE2 . GLU   B 2 34  ? -32.447 -6.314  -14.100 1.00 62.25 ? 43  GLU   B OE2 1 
ATOM   509  N  N   . GLY   B 2 35  ? -33.986 0.546   -12.700 1.00 39.58 ? 44  GLY   B N   1 
ATOM   510  C  CA  . GLY   B 2 35  ? -34.074 1.650   -11.749 1.00 38.73 ? 44  GLY   B CA  1 
ATOM   511  C  C   . GLY   B 2 35  ? -32.868 1.819   -10.848 1.00 37.91 ? 44  GLY   B C   1 
ATOM   512  O  O   . GLY   B 2 35  ? -32.937 2.557   -9.858  1.00 38.35 ? 44  GLY   B O   1 
ATOM   513  N  N   . VAL   B 2 36  ? -31.755 1.127   -11.176 1.00 36.40 ? 45  VAL   B N   1 
ATOM   514  C  CA  . VAL   B 2 36  ? -30.508 1.168   -10.416 1.00 35.48 ? 45  VAL   B CA  1 
ATOM   515  C  C   . VAL   B 2 36  ? -29.382 1.688   -11.329 1.00 34.89 ? 45  VAL   B C   1 
ATOM   516  O  O   . VAL   B 2 36  ? -29.245 1.225   -12.464 1.00 35.09 ? 45  VAL   B O   1 
ATOM   517  C  CB  . VAL   B 2 36  ? -30.148 -0.221  -9.803  1.00 35.26 ? 45  VAL   B CB  1 
ATOM   518  C  CG1 . VAL   B 2 36  ? -28.818 -0.182  -9.077  1.00 35.50 ? 45  VAL   B CG1 1 
ATOM   519  C  CG2 . VAL   B 2 36  ? -31.234 -0.719  -8.872  1.00 35.68 ? 45  VAL   B CG2 1 
ATOM   520  N  N   . PHE   B 2 37  ? -28.594 2.658   -10.832 1.00 33.65 ? 46  PHE   B N   1 
ATOM   521  C  CA  . PHE   B 2 37  ? -27.466 3.203   -11.556 1.00 33.16 ? 46  PHE   B CA  1 
ATOM   522  C  C   . PHE   B 2 37  ? -26.186 2.555   -11.052 1.00 32.55 ? 46  PHE   B C   1 
ATOM   523  O  O   . PHE   B 2 37  ? -25.852 2.704   -9.889  1.00 33.04 ? 46  PHE   B O   1 
ATOM   524  C  CB  . PHE   B 2 37  ? -27.378 4.717   -11.379 1.00 33.12 ? 46  PHE   B CB  1 
ATOM   525  C  CG  . PHE   B 2 37  ? -26.393 5.300   -12.357 1.00 34.20 ? 46  PHE   B CG  1 
ATOM   526  C  CD1 . PHE   B 2 37  ? -26.652 5.286   -13.718 1.00 34.80 ? 46  PHE   B CD1 1 
ATOM   527  C  CD2 . PHE   B 2 37  ? -25.187 5.824   -11.923 1.00 35.23 ? 46  PHE   B CD2 1 
ATOM   528  C  CE1 . PHE   B 2 37  ? -25.748 5.831   -14.619 1.00 35.55 ? 46  PHE   B CE1 1 
ATOM   529  C  CE2 . PHE   B 2 37  ? -24.274 6.351   -12.835 1.00 35.69 ? 46  PHE   B CE2 1 
ATOM   530  C  CZ  . PHE   B 2 37  ? -24.569 6.362   -14.172 1.00 35.28 ? 46  PHE   B CZ  1 
ATOM   531  N  N   . HIS   B 2 38  ? -25.459 1.865   -11.934 1.00 31.83 ? 47  HIS   B N   1 
ATOM   532  C  CA  . HIS   B 2 38  ? -24.226 1.146   -11.644 1.00 31.39 ? 47  HIS   B CA  1 
ATOM   533  C  C   . HIS   B 2 38  ? -23.036 1.900   -12.188 1.00 32.82 ? 47  HIS   B C   1 
ATOM   534  O  O   . HIS   B 2 38  ? -23.099 2.393   -13.301 1.00 32.66 ? 47  HIS   B O   1 
ATOM   535  C  CB  . HIS   B 2 38  ? -24.267 -0.222  -12.314 1.00 30.45 ? 47  HIS   B CB  1 
ATOM   536  C  CG  . HIS   B 2 38  ? -25.506 -1.003  -12.009 1.00 30.46 ? 47  HIS   B CG  1 
ATOM   537  N  ND1 . HIS   B 2 38  ? -26.710 -0.713  -12.629 1.00 31.22 ? 47  HIS   B ND1 1 
ATOM   538  C  CD2 . HIS   B 2 38  ? -25.683 -2.055  -11.177 1.00 30.79 ? 47  HIS   B CD2 1 
ATOM   539  C  CE1 . HIS   B 2 38  ? -27.582 -1.579  -12.140 1.00 31.54 ? 47  HIS   B CE1 1 
ATOM   540  N  NE2 . HIS   B 2 38  ? -27.005 -2.423  -11.281 1.00 31.45 ? 47  HIS   B NE2 1 
ATOM   541  N  N   . THR   B 2 39  ? -21.937 2.007   -11.409 1.00 33.76 ? 48  THR   B N   1 
ATOM   542  C  CA  . THR   B 2 39  ? -20.716 2.672   -11.894 1.00 34.32 ? 48  THR   B CA  1 
ATOM   543  C  C   . THR   B 2 39  ? -19.485 2.187   -11.086 1.00 35.35 ? 48  THR   B C   1 
ATOM   544  O  O   . THR   B 2 39  ? -19.618 1.371   -10.179 1.00 35.81 ? 48  THR   B O   1 
ATOM   545  C  CB  . THR   B 2 39  ? -20.864 4.225   -11.990 1.00 34.90 ? 48  THR   B CB  1 
ATOM   546  O  OG1 . THR   B 2 39  ? -19.815 4.714   -12.820 1.00 34.75 ? 48  THR   B OG1 1 
ATOM   547  C  CG2 . THR   B 2 39  ? -20.807 4.917   -10.640 1.00 35.90 ? 48  THR   B CG2 1 
ATOM   548  N  N   . MET   B 2 40  ? -18.286 2.617   -11.479 1.00 35.47 ? 49  MET   B N   1 
ATOM   549  C  CA  . MET   B 2 40  ? -17.070 2.288   -10.762 1.00 35.48 ? 49  MET   B CA  1 
ATOM   550  C  C   . MET   B 2 40  ? -16.986 3.261   -9.598  1.00 35.55 ? 49  MET   B C   1 
ATOM   551  O  O   . MET   B 2 40  ? -17.268 4.449   -9.763  1.00 36.38 ? 49  MET   B O   1 
ATOM   552  C  CB  . MET   B 2 40  ? -15.863 2.403   -11.704 1.00 35.88 ? 49  MET   B CB  1 
ATOM   553  C  CG  . MET   B 2 40  ? -16.009 1.532   -12.934 1.00 37.37 ? 49  MET   B CG  1 
ATOM   554  S  SD  . MET   B 2 40  ? -14.630 0.408   -13.211 1.00 44.59 ? 49  MET   B SD  1 
ATOM   555  C  CE  . MET   B 2 40  ? -15.033 -0.905  -12.159 1.00 44.07 ? 49  MET   B CE  1 
ATOM   556  N  N   . TRP   B 2 41  ? -16.626 2.754   -8.415  1.00 34.71 ? 50  TRP   B N   1 
ATOM   557  C  CA  A TRP   B 2 41  ? -16.531 3.550   -7.197  0.50 34.70 ? 50  TRP   B CA  1 
ATOM   558  C  CA  B TRP   B 2 41  ? -16.533 3.546   -7.190  0.50 34.38 ? 50  TRP   B CA  1 
ATOM   559  C  C   . TRP   B 2 41  ? -15.643 4.784   -7.334  1.00 34.79 ? 50  TRP   B C   1 
ATOM   560  O  O   . TRP   B 2 41  ? -15.960 5.825   -6.767  1.00 34.65 ? 50  TRP   B O   1 
ATOM   561  C  CB  A TRP   B 2 41  ? -16.064 2.690   -6.013  0.50 34.47 ? 50  TRP   B CB  1 
ATOM   562  C  CB  B TRP   B 2 41  ? -16.076 2.667   -6.006  0.50 33.70 ? 50  TRP   B CB  1 
ATOM   563  C  CG  A TRP   B 2 41  ? -16.290 3.357   -4.693  0.50 35.11 ? 50  TRP   B CG  1 
ATOM   564  C  CG  B TRP   B 2 41  ? -15.902 3.413   -4.715  0.50 33.75 ? 50  TRP   B CG  1 
ATOM   565  C  CD1 A TRP   B 2 41  ? -17.426 3.318   -3.946  0.50 36.19 ? 50  TRP   B CD1 1 
ATOM   566  C  CD1 B TRP   B 2 41  ? -14.812 4.134   -4.324  0.50 34.29 ? 50  TRP   B CD1 1 
ATOM   567  C  CD2 A TRP   B 2 41  ? -15.384 4.232   -4.004  0.50 35.20 ? 50  TRP   B CD2 1 
ATOM   568  C  CD2 B TRP   B 2 41  ? -16.844 3.495   -3.642  0.50 33.86 ? 50  TRP   B CD2 1 
ATOM   569  N  NE1 A TRP   B 2 41  ? -17.280 4.098   -2.824  0.50 36.70 ? 50  TRP   B NE1 1 
ATOM   570  N  NE1 B TRP   B 2 41  ? -15.033 4.693   -3.093  0.50 34.52 ? 50  TRP   B NE1 1 
ATOM   571  C  CE2 A TRP   B 2 41  ? -16.036 4.675   -2.838  0.50 36.26 ? 50  TRP   B CE2 1 
ATOM   572  C  CE2 B TRP   B 2 41  ? -16.269 4.304   -2.642  0.50 34.57 ? 50  TRP   B CE2 1 
ATOM   573  C  CE3 A TRP   B 2 41  ? -14.084 4.679   -4.255  0.50 35.72 ? 50  TRP   B CE3 1 
ATOM   574  C  CE3 B TRP   B 2 41  ? -18.124 2.969   -3.428  0.50 34.47 ? 50  TRP   B CE3 1 
ATOM   575  C  CZ2 A TRP   B 2 41  ? -15.435 5.545   -1.931  0.50 37.03 ? 50  TRP   B CZ2 1 
ATOM   576  C  CZ2 B TRP   B 2 41  ? -16.931 4.601   -1.448  0.50 35.37 ? 50  TRP   B CZ2 1 
ATOM   577  C  CZ3 A TRP   B 2 41  ? -13.493 5.542   -3.359  0.50 36.82 ? 50  TRP   B CZ3 1 
ATOM   578  C  CZ3 B TRP   B 2 41  ? -18.777 3.263   -2.244  0.50 35.48 ? 50  TRP   B CZ3 1 
ATOM   579  C  CH2 A TRP   B 2 41  ? -14.153 5.940   -2.195  0.50 37.15 ? 50  TRP   B CH2 1 
ATOM   580  C  CH2 B TRP   B 2 41  ? -18.182 4.069   -1.271  0.50 35.57 ? 50  TRP   B CH2 1 
ATOM   581  N  N   . HIS   B 2 42  ? -14.521 4.671   -8.046  1.00 34.80 ? 51  HIS   B N   1 
ATOM   582  C  CA  . HIS   B 2 42  ? -13.613 5.796   -8.210  1.00 35.38 ? 51  HIS   B CA  1 
ATOM   583  C  C   . HIS   B 2 42  ? -14.203 6.960   -9.043  1.00 36.57 ? 51  HIS   B C   1 
ATOM   584  O  O   . HIS   B 2 42  ? -13.607 8.032   -9.075  1.00 37.19 ? 51  HIS   B O   1 
ATOM   585  C  CB  . HIS   B 2 42  ? -12.256 5.330   -8.765  1.00 35.44 ? 51  HIS   B CB  1 
ATOM   586  C  CG  . HIS   B 2 42  ? -12.279 4.904   -10.200 1.00 36.62 ? 51  HIS   B CG  1 
ATOM   587  N  ND1 . HIS   B 2 42  ? -12.239 3.566   -10.560 1.00 37.86 ? 51  HIS   B ND1 1 
ATOM   588  C  CD2 . HIS   B 2 42  ? -12.272 5.654   -11.324 1.00 37.16 ? 51  HIS   B CD2 1 
ATOM   589  C  CE1 . HIS   B 2 42  ? -12.250 3.553   -11.878 1.00 37.57 ? 51  HIS   B CE1 1 
ATOM   590  N  NE2 . HIS   B 2 42  ? -12.283 4.787   -12.376 1.00 37.59 ? 51  HIS   B NE2 1 
ATOM   591  N  N   . VAL   B 2 43  ? -15.363 6.768   -9.699  1.00 36.70 ? 52  VAL   B N   1 
ATOM   592  C  CA  . VAL   B 2 43  ? -15.965 7.826   -10.502 1.00 37.21 ? 52  VAL   B CA  1 
ATOM   593  C  C   . VAL   B 2 43  ? -16.657 8.837   -9.597  1.00 38.49 ? 52  VAL   B C   1 
ATOM   594  O  O   . VAL   B 2 43  ? -16.332 10.018  -9.625  1.00 38.30 ? 52  VAL   B O   1 
ATOM   595  C  CB  . VAL   B 2 43  ? -16.911 7.260   -11.596 1.00 37.76 ? 52  VAL   B CB  1 
ATOM   596  C  CG1 . VAL   B 2 43  ? -17.710 8.371   -12.269 1.00 38.36 ? 52  VAL   B CG1 1 
ATOM   597  C  CG2 . VAL   B 2 43  ? -16.141 6.446   -12.624 1.00 38.03 ? 52  VAL   B CG2 1 
ATOM   598  N  N   . THR   B 2 44  ? -17.567 8.358   -8.744  1.00 39.35 ? 53  THR   B N   1 
ATOM   599  C  CA  . THR   B 2 44  ? -18.327 9.216   -7.855  1.00 39.97 ? 53  THR   B CA  1 
ATOM   600  C  C   . THR   B 2 44  ? -17.723 9.361   -6.466  1.00 40.97 ? 53  THR   B C   1 
ATOM   601  O  O   . THR   B 2 44  ? -17.996 10.353  -5.788  1.00 41.48 ? 53  THR   B O   1 
ATOM   602  C  CB  . THR   B 2 44  ? -19.766 8.689   -7.747  1.00 40.46 ? 53  THR   B CB  1 
ATOM   603  O  OG1 . THR   B 2 44  ? -19.771 7.498   -6.968  1.00 40.39 ? 53  THR   B OG1 1 
ATOM   604  C  CG2 . THR   B 2 44  ? -20.408 8.408   -9.118  1.00 41.04 ? 53  THR   B CG2 1 
ATOM   605  N  N   . LYS   B 2 45  ? -16.937 8.360   -6.034  1.00 41.22 ? 54  LYS   B N   1 
ATOM   606  C  CA  . LYS   B 2 45  ? -16.366 8.214   -4.681  1.00 41.97 ? 54  LYS   B CA  1 
ATOM   607  C  C   . LYS   B 2 45  ? -17.465 8.080   -3.605  1.00 41.66 ? 54  LYS   B C   1 
ATOM   608  O  O   . LYS   B 2 45  ? -17.268 8.466   -2.455  1.00 41.99 ? 54  LYS   B O   1 
ATOM   609  C  CB  . LYS   B 2 45  ? -15.335 9.294   -4.344  1.00 44.53 ? 54  LYS   B CB  1 
ATOM   610  C  CG  . LYS   B 2 45  ? -14.263 9.388   -5.405  1.00 50.83 ? 54  LYS   B CG  1 
ATOM   611  C  CD  . LYS   B 2 45  ? -12.992 10.011  -4.875  1.00 58.09 ? 54  LYS   B CD  1 
ATOM   612  C  CE  . LYS   B 2 45  ? -11.901 10.009  -5.922  1.00 63.77 ? 54  LYS   B CE  1 
ATOM   613  N  NZ  . LYS   B 2 45  ? -10.549 10.206  -5.319  1.00 67.45 ? 54  LYS   B NZ  1 
ATOM   614  N  N   . GLY   B 2 46  ? -18.600 7.504   -3.997  1.00 41.07 ? 55  GLY   B N   1 
ATOM   615  C  CA  . GLY   B 2 46  ? -19.757 7.321   -3.136  1.00 41.22 ? 55  GLY   B CA  1 
ATOM   616  C  C   . GLY   B 2 46  ? -20.699 8.505   -3.032  1.00 41.36 ? 55  GLY   B C   1 
ATOM   617  O  O   . GLY   B 2 46  ? -21.723 8.410   -2.360  1.00 41.92 ? 55  GLY   B O   1 
ATOM   618  N  N   . ALA   B 2 47  ? -20.371 9.635   -3.665  1.00 41.24 ? 56  ALA   B N   1 
ATOM   619  C  CA  . ALA   B 2 47  ? -21.196 10.847  -3.592  1.00 41.50 ? 56  ALA   B CA  1 
ATOM   620  C  C   . ALA   B 2 47  ? -22.534 10.683  -4.310  1.00 41.68 ? 56  ALA   B C   1 
ATOM   621  O  O   . ALA   B 2 47  ? -22.608 9.943   -5.282  1.00 42.13 ? 56  ALA   B O   1 
ATOM   622  C  CB  . ALA   B 2 47  ? -20.440 12.030  -4.183  1.00 41.49 ? 56  ALA   B CB  1 
ATOM   623  N  N   . ALA   B 2 48  ? -23.571 11.412  -3.866  1.00 41.16 ? 57  ALA   B N   1 
ATOM   624  C  CA  . ALA   B 2 48  ? -24.895 11.367  -4.474  1.00 41.21 ? 57  ALA   B CA  1 
ATOM   625  C  C   . ALA   B 2 48  ? -24.887 11.978  -5.862  1.00 41.83 ? 57  ALA   B C   1 
ATOM   626  O  O   . ALA   B 2 48  ? -24.059 12.836  -6.163  1.00 42.71 ? 57  ALA   B O   1 
ATOM   627  C  CB  . ALA   B 2 48  ? -25.907 12.079  -3.590  1.00 41.26 ? 57  ALA   B CB  1 
ATOM   628  N  N   . LEU   B 2 49  ? -25.786 11.512  -6.731  1.00 41.32 ? 58  LEU   B N   1 
ATOM   629  C  CA  . LEU   B 2 49  ? -25.867 11.990  -8.110  1.00 41.07 ? 58  LEU   B CA  1 
ATOM   630  C  C   . LEU   B 2 49  ? -27.178 12.753  -8.371  1.00 41.85 ? 58  LEU   B C   1 
ATOM   631  O  O   . LEU   B 2 49  ? -28.121 12.686  -7.589  1.00 41.48 ? 58  LEU   B O   1 
ATOM   632  C  CB  . LEU   B 2 49  ? -25.733 10.803  -9.081  1.00 40.49 ? 58  LEU   B CB  1 
ATOM   633  C  CG  . LEU   B 2 49  ? -24.469 9.983   -8.925  1.00 41.40 ? 58  LEU   B CG  1 
ATOM   634  C  CD1 . LEU   B 2 49  ? -24.546 8.711   -9.735  1.00 41.87 ? 58  LEU   B CD1 1 
ATOM   635  C  CD2 . LEU   B 2 49  ? -23.257 10.789  -9.282  1.00 41.81 ? 58  LEU   B CD2 1 
ATOM   636  N  N   . ARG   B 2 50  ? -27.223 13.484  -9.467  1.00 42.75 ? 59  ARG   B N   1 
ATOM   637  C  CA  . ARG   B 2 50  ? -28.386 14.261  -9.851  1.00 44.07 ? 59  ARG   B CA  1 
ATOM   638  C  C   . ARG   B 2 50  ? -28.813 13.817  -11.264 1.00 44.59 ? 59  ARG   B C   1 
ATOM   639  O  O   . ARG   B 2 50  ? -27.970 13.489  -12.099 1.00 43.54 ? 59  ARG   B O   1 
ATOM   640  C  CB  . ARG   B 2 50  ? -27.985 15.736  -9.823  1.00 46.52 ? 59  ARG   B CB  1 
ATOM   641  C  CG  . ARG   B 2 50  ? -29.127 16.713  -9.946  1.00 52.61 ? 59  ARG   B CG  1 
ATOM   642  C  CD  . ARG   B 2 50  ? -28.685 18.137  -9.616  1.00 57.55 ? 59  ARG   B CD  1 
ATOM   643  N  NE  . ARG   B 2 50  ? -27.491 18.572  -10.355 1.00 61.34 ? 59  ARG   B NE  1 
ATOM   644  C  CZ  . ARG   B 2 50  ? -27.505 19.025  -11.607 1.00 64.53 ? 59  ARG   B CZ  1 
ATOM   645  N  NH1 . ARG   B 2 50  ? -28.644 19.079  -12.291 1.00 64.09 ? 59  ARG   B NH1 1 
ATOM   646  N  NH2 . ARG   B 2 50  ? -26.379 19.415  -12.190 1.00 65.35 ? 59  ARG   B NH2 1 
ATOM   647  N  N   . SER   B 2 51  ? -30.112 13.731  -11.504 1.00 45.95 ? 60  SER   B N   1 
ATOM   648  C  CA  . SER   B 2 51  ? -30.632 13.330  -12.812 1.00 48.15 ? 60  SER   B CA  1 
ATOM   649  C  C   . SER   B 2 51  ? -31.796 14.249  -13.149 1.00 50.58 ? 60  SER   B C   1 
ATOM   650  O  O   . SER   B 2 51  ? -32.962 13.871  -12.993 1.00 51.14 ? 60  SER   B O   1 
ATOM   651  C  CB  . SER   B 2 51  ? -31.087 11.875  -12.794 1.00 49.39 ? 60  SER   B CB  1 
ATOM   652  O  OG  . SER   B 2 51  ? -31.683 11.524  -14.033 1.00 51.73 ? 60  SER   B OG  1 
ATOM   653  N  N   . GLY   B 2 52  ? -31.473 15.470  -13.552 1.00 51.54 ? 61  GLY   B N   1 
ATOM   654  C  CA  . GLY   B 2 52  ? -32.491 16.471  -13.808 1.00 52.83 ? 61  GLY   B CA  1 
ATOM   655  C  C   . GLY   B 2 52  ? -32.967 16.972  -12.468 1.00 54.32 ? 61  GLY   B C   1 
ATOM   656  O  O   . GLY   B 2 52  ? -32.142 17.321  -11.619 1.00 54.91 ? 61  GLY   B O   1 
ATOM   657  N  N   . GLU   B 2 53  ? -34.285 16.959  -12.230 1.00 54.75 ? 62  GLU   B N   1 
ATOM   658  C  CA  . GLU   B 2 53  ? -34.822 17.402  -10.940 1.00 55.46 ? 62  GLU   B CA  1 
ATOM   659  C  C   . GLU   B 2 53  ? -34.686 16.348  -9.811  1.00 55.04 ? 62  GLU   B C   1 
ATOM   660  O  O   . GLU   B 2 53  ? -34.743 16.700  -8.628  1.00 54.94 ? 62  GLU   B O   1 
ATOM   661  C  CB  . GLU   B 2 53  ? -36.271 17.872  -11.091 1.00 59.38 ? 62  GLU   B CB  1 
ATOM   662  C  CG  . GLU   B 2 53  ? -36.604 19.064  -10.214 1.00 66.73 ? 62  GLU   B CG  1 
ATOM   663  C  CD  . GLU   B 2 53  ? -37.843 19.828  -10.642 1.00 76.39 ? 62  GLU   B CD  1 
ATOM   664  O  OE1 . GLU   B 2 53  ? -38.899 19.182  -10.840 1.00 78.14 ? 62  GLU   B OE1 1 
ATOM   665  O  OE2 . GLU   B 2 53  ? -37.760 21.073  -10.773 1.00 79.13 ? 62  GLU   B OE2 1 
ATOM   666  N  N   . GLY   B 2 54  ? -34.483 15.084  -10.187 1.00 54.32 ? 63  GLY   B N   1 
ATOM   667  C  CA  . GLY   B 2 54  ? -34.315 13.986  -9.244  1.00 54.20 ? 63  GLY   B CA  1 
ATOM   668  C  C   . GLY   B 2 54  ? -32.903 13.829  -8.699  1.00 53.38 ? 63  GLY   B C   1 
ATOM   669  O  O   . GLY   B 2 54  ? -31.961 14.454  -9.199  1.00 53.80 ? 63  GLY   B O   1 
ATOM   670  N  N   . ARG   B 2 55  ? -32.760 12.985  -7.655  1.00 51.67 ? 64  ARG   B N   1 
ATOM   671  C  CA  . ARG   B 2 55  ? -31.501 12.701  -6.956  1.00 50.25 ? 64  ARG   B CA  1 
ATOM   672  C  C   . ARG   B 2 55  ? -31.294 11.187  -6.738  1.00 47.85 ? 64  ARG   B C   1 
ATOM   673  O  O   . ARG   B 2 55  ? -32.191 10.497  -6.250  1.00 47.77 ? 64  ARG   B O   1 
ATOM   674  C  CB  . ARG   B 2 55  ? -31.485 13.427  -5.590  1.00 51.53 ? 64  ARG   B CB  1 
ATOM   675  C  CG  . ARG   B 2 55  ? -30.262 13.123  -4.724  1.00 54.37 ? 64  ARG   B CG  1 
ATOM   676  C  CD  . ARG   B 2 55  ? -30.249 13.949  -3.449  1.00 57.70 ? 64  ARG   B CD  1 
ATOM   677  N  NE  . ARG   B 2 55  ? -29.228 13.493  -2.502  1.00 60.50 ? 64  ARG   B NE  1 
ATOM   678  C  CZ  . ARG   B 2 55  ? -28.694 14.250  -1.547  1.00 63.02 ? 64  ARG   B CZ  1 
ATOM   679  N  NH1 . ARG   B 2 55  ? -29.048 15.525  -1.423  1.00 62.73 ? 64  ARG   B NH1 1 
ATOM   680  N  NH2 . ARG   B 2 55  ? -27.782 13.745  -0.724  1.00 63.03 ? 64  ARG   B NH2 1 
ATOM   681  N  N   . LEU   B 2 56  ? -30.102 10.689  -7.054  1.00 45.60 ? 65  LEU   B N   1 
ATOM   682  C  CA  . LEU   B 2 56  ? -29.778 9.287   -6.852  1.00 44.36 ? 65  LEU   B CA  1 
ATOM   683  C  C   . LEU   B 2 56  ? -28.859 9.174   -5.644  1.00 43.37 ? 65  LEU   B C   1 
ATOM   684  O  O   . LEU   B 2 56  ? -27.753 9.722   -5.647  1.00 43.53 ? 65  LEU   B O   1 
ATOM   685  C  CB  . LEU   B 2 56  ? -29.071 8.677   -8.089  1.00 44.42 ? 65  LEU   B CB  1 
ATOM   686  C  CG  . LEU   B 2 56  ? -29.506 9.112   -9.485  1.00 46.04 ? 65  LEU   B CG  1 
ATOM   687  C  CD1 . LEU   B 2 56  ? -28.849 8.251   -10.520 1.00 47.01 ? 65  LEU   B CD1 1 
ATOM   688  C  CD2 . LEU   B 2 56  ? -30.997 8.995   -9.668  1.00 46.98 ? 65  LEU   B CD2 1 
ATOM   689  N  N   . ASP   B 2 57  ? -29.301 8.467   -4.614  1.00 42.18 ? 66  ASP   B N   1 
ATOM   690  C  CA  . ASP   B 2 57  ? -28.485 8.252   -3.422  1.00 41.51 ? 66  ASP   B CA  1 
ATOM   691  C  C   . ASP   B 2 57  ? -27.837 6.858   -3.501  1.00 39.68 ? 66  ASP   B C   1 
ATOM   692  O  O   . ASP   B 2 57  ? -28.453 5.912   -4.004  1.00 39.38 ? 66  ASP   B O   1 
ATOM   693  C  CB  . ASP   B 2 57  ? -29.347 8.380   -2.165  1.00 44.53 ? 66  ASP   B CB  1 
ATOM   694  C  CG  . ASP   B 2 57  ? -29.961 9.753   -2.023  1.00 52.09 ? 66  ASP   B CG  1 
ATOM   695  O  OD1 . ASP   B 2 57  ? -29.313 10.732  -2.434  1.00 53.64 ? 66  ASP   B OD1 1 
ATOM   696  O  OD2 . ASP   B 2 57  ? -31.093 9.849   -1.493  1.00 55.31 ? 66  ASP   B OD2 1 
ATOM   697  N  N   . PRO   B 2 58  ? -26.577 6.720   -3.053  1.00 38.19 ? 67  PRO   B N   1 
ATOM   698  C  CA  . PRO   B 2 58  ? -25.934 5.404   -3.112  1.00 37.32 ? 67  PRO   B CA  1 
ATOM   699  C  C   . PRO   B 2 58  ? -26.652 4.389   -2.230  1.00 37.69 ? 67  PRO   B C   1 
ATOM   700  O  O   . PRO   B 2 58  ? -27.346 4.741   -1.262  1.00 38.33 ? 67  PRO   B O   1 
ATOM   701  C  CB  . PRO   B 2 58  ? -24.506 5.677   -2.647  1.00 37.68 ? 67  PRO   B CB  1 
ATOM   702  C  CG  . PRO   B 2 58  ? -24.590 6.912   -1.856  1.00 38.45 ? 67  PRO   B CG  1 
ATOM   703  C  CD  . PRO   B 2 58  ? -25.704 7.732   -2.427  1.00 37.33 ? 67  PRO   B CD  1 
ATOM   704  N  N   . TYR   B 2 59  ? -26.519 3.127   -2.591  1.00 37.02 ? 68  TYR   B N   1 
ATOM   705  C  CA  . TYR   B 2 59  ? -27.178 2.067   -1.860  1.00 36.72 ? 68  TYR   B CA  1 
ATOM   706  C  C   . TYR   B 2 59  ? -26.170 1.019   -1.442  1.00 37.50 ? 68  TYR   B C   1 
ATOM   707  O  O   . TYR   B 2 59  ? -26.192 0.569   -0.307  1.00 38.88 ? 68  TYR   B O   1 
ATOM   708  C  CB  . TYR   B 2 59  ? -28.321 1.505   -2.715  1.00 35.53 ? 68  TYR   B CB  1 
ATOM   709  C  CG  . TYR   B 2 59  ? -29.042 0.309   -2.140  1.00 34.62 ? 68  TYR   B CG  1 
ATOM   710  C  CD1 . TYR   B 2 59  ? -28.445 -0.950  -2.131  1.00 35.25 ? 68  TYR   B CD1 1 
ATOM   711  C  CD2 . TYR   B 2 59  ? -30.378 0.390   -1.784  1.00 34.03 ? 68  TYR   B CD2 1 
ATOM   712  C  CE1 . TYR   B 2 59  ? -29.117 -2.066  -1.651  1.00 35.92 ? 68  TYR   B CE1 1 
ATOM   713  C  CE2 . TYR   B 2 59  ? -31.078 -0.727  -1.360  1.00 35.10 ? 68  TYR   B CE2 1 
ATOM   714  C  CZ  . TYR   B 2 59  ? -30.440 -1.954  -1.280  1.00 36.79 ? 68  TYR   B CZ  1 
ATOM   715  O  OH  . TYR   B 2 59  ? -31.125 -3.051  -0.815  1.00 39.16 ? 68  TYR   B OH  1 
ATOM   716  N  N   . TRP   B 2 60  ? -25.306 0.617   -2.350  1.00 36.84 ? 69  TRP   B N   1 
ATOM   717  C  CA  . TRP   B 2 60  ? -24.279 -0.385  -2.080  1.00 36.51 ? 69  TRP   B CA  1 
ATOM   718  C  C   . TRP   B 2 60  ? -22.954 0.108   -2.691  1.00 36.13 ? 69  TRP   B C   1 
ATOM   719  O  O   . TRP   B 2 60  ? -22.970 0.728   -3.746  1.00 36.07 ? 69  TRP   B O   1 
ATOM   720  C  CB  . TRP   B 2 60  ? -24.674 -1.754  -2.699  1.00 36.23 ? 69  TRP   B CB  1 
ATOM   721  C  CG  . TRP   B 2 60  ? -23.567 -2.754  -2.577  1.00 36.33 ? 69  TRP   B CG  1 
ATOM   722  C  CD1 . TRP   B 2 60  ? -23.111 -3.318  -1.421  1.00 37.22 ? 69  TRP   B CD1 1 
ATOM   723  C  CD2 . TRP   B 2 60  ? -22.601 -3.078  -3.589  1.00 36.02 ? 69  TRP   B CD2 1 
ATOM   724  N  NE1 . TRP   B 2 60  ? -21.949 -4.011  -1.662  1.00 37.61 ? 69  TRP   B NE1 1 
ATOM   725  C  CE2 . TRP   B 2 60  ? -21.616 -3.885  -2.987  1.00 36.62 ? 69  TRP   B CE2 1 
ATOM   726  C  CE3 . TRP   B 2 60  ? -22.457 -2.736  -4.940  1.00 36.17 ? 69  TRP   B CE3 1 
ATOM   727  C  CZ2 . TRP   B 2 60  ? -20.533 -4.386  -3.694  1.00 36.69 ? 69  TRP   B CZ2 1 
ATOM   728  C  CZ3 . TRP   B 2 60  ? -21.387 -3.250  -5.640  1.00 36.79 ? 69  TRP   B CZ3 1 
ATOM   729  C  CH2 . TRP   B 2 60  ? -20.456 -4.086  -5.026  1.00 36.62 ? 69  TRP   B CH2 1 
ATOM   730  N  N   . GLY   B 2 61  ? -21.828 -0.203  -2.060  1.00 35.91 ? 70  GLY   B N   1 
ATOM   731  C  CA  . GLY   B 2 61  ? -20.527 0.177   -2.597  1.00 36.17 ? 70  GLY   B CA  1 
ATOM   732  C  C   . GLY   B 2 61  ? -19.378 -0.542  -1.940  1.00 36.56 ? 70  GLY   B C   1 
ATOM   733  O  O   . GLY   B 2 61  ? -19.480 -0.918  -0.779  1.00 36.95 ? 70  GLY   B O   1 
ATOM   734  N  N   . ASP   B 2 62  ? -18.272 -0.734  -2.673  1.00 36.55 ? 71  ASP   B N   1 
ATOM   735  C  CA  . ASP   B 2 62  ? -17.071 -1.421  -2.184  1.00 36.42 ? 71  ASP   B CA  1 
ATOM   736  C  C   . ASP   B 2 62  ? -15.845 -0.891  -2.912  1.00 36.05 ? 71  ASP   B C   1 
ATOM   737  O  O   . ASP   B 2 62  ? -15.803 -0.930  -4.132  1.00 36.72 ? 71  ASP   B O   1 
ATOM   738  C  CB  . ASP   B 2 62  ? -17.185 -2.915  -2.470  1.00 38.32 ? 71  ASP   B CB  1 
ATOM   739  C  CG  . ASP   B 2 62  ? -16.198 -3.737  -1.694  1.00 43.21 ? 71  ASP   B CG  1 
ATOM   740  O  OD1 . ASP   B 2 62  ? -15.016 -3.776  -2.089  1.00 43.03 ? 71  ASP   B OD1 1 
ATOM   741  O  OD2 . ASP   B 2 62  ? -16.604 -4.344  -0.686  1.00 47.23 ? 71  ASP   B OD2 1 
ATOM   742  N  N   . VAL   B 2 63  ? -14.846 -0.428  -2.176  1.00 35.40 ? 72  VAL   B N   1 
ATOM   743  C  CA  . VAL   B 2 63  ? -13.623 0.135   -2.733  1.00 34.94 ? 72  VAL   B CA  1 
ATOM   744  C  C   . VAL   B 2 63  ? -12.754 -0.936  -3.409  1.00 35.07 ? 72  VAL   B C   1 
ATOM   745  O  O   . VAL   B 2 63  ? -12.228 -0.677  -4.499  1.00 34.61 ? 72  VAL   B O   1 
ATOM   746  C  CB  . VAL   B 2 63  ? -12.881 0.954   -1.643  1.00 35.41 ? 72  VAL   B CB  1 
ATOM   747  C  CG1 . VAL   B 2 63  ? -11.372 0.990   -1.842  1.00 35.67 ? 72  VAL   B CG1 1 
ATOM   748  C  CG2 . VAL   B 2 63  ? -13.453 2.369   -1.534  1.00 35.89 ? 72  VAL   B CG2 1 
ATOM   749  N  N   . LYS   B 2 64  ? -12.646 -2.148  -2.820  1.00 35.29 ? 73  LYS   B N   1 
ATOM   750  C  CA  . LYS   B 2 64  ? -11.819 -3.207  -3.429  1.00 35.57 ? 73  LYS   B CA  1 
ATOM   751  C  C   . LYS   B 2 64  ? -12.394 -3.714  -4.756  1.00 35.47 ? 73  LYS   B C   1 
ATOM   752  O  O   . LYS   B 2 64  ? -11.679 -3.801  -5.751  1.00 35.04 ? 73  LYS   B O   1 
ATOM   753  C  CB  . LYS   B 2 64  ? -11.596 -4.372  -2.462  1.00 37.71 ? 73  LYS   B CB  1 
ATOM   754  C  CG  . LYS   B 2 64  ? -10.367 -5.186  -2.848  1.00 40.73 ? 73  LYS   B CG  1 
ATOM   755  C  CD  . LYS   B 2 64  ? -10.131 -6.326  -1.893  1.00 43.91 ? 73  LYS   B CD  1 
ATOM   756  C  CE  . LYS   B 2 64  ? -8.818  -6.991  -2.194  1.00 48.19 ? 73  LYS   B CE  1 
ATOM   757  N  NZ  . LYS   B 2 64  ? -8.784  -8.379  -1.675  1.00 51.75 ? 73  LYS   B NZ  1 
ATOM   758  N  N   . GLN   B 2 65  ? -13.689 -4.031  -4.775  1.00 35.55 ? 74  GLN   B N   1 
ATOM   759  C  CA  . GLN   B 2 65  ? -14.359 -4.426  -6.004  1.00 35.94 ? 74  GLN   B CA  1 
ATOM   760  C  C   . GLN   B 2 65  ? -14.422 -3.237  -6.987  1.00 35.67 ? 74  GLN   B C   1 
ATOM   761  O  O   . GLN   B 2 65  ? -14.595 -3.451  -8.184  1.00 35.77 ? 74  GLN   B O   1 
ATOM   762  C  CB  . GLN   B 2 65  ? -15.774 -4.909  -5.693  1.00 38.61 ? 74  GLN   B CB  1 
ATOM   763  C  CG  . GLN   B 2 65  ? -15.850 -6.274  -4.998  1.00 43.82 ? 74  GLN   B CG  1 
ATOM   764  C  CD  . GLN   B 2 65  ? -17.298 -6.657  -4.698  1.00 50.47 ? 74  GLN   B CD  1 
ATOM   765  O  OE1 . GLN   B 2 65  ? -18.193 -6.624  -5.581  1.00 52.99 ? 74  GLN   B OE1 1 
ATOM   766  N  NE2 . GLN   B 2 65  ? -17.563 -7.018  -3.442  1.00 50.57 ? 74  GLN   B NE2 1 
ATOM   767  N  N   . ASP   B 2 66  ? -14.262 -1.993  -6.473  1.00 34.97 ? 75  ASP   B N   1 
ATOM   768  C  CA  . ASP   B 2 66  ? -14.304 -0.734  -7.180  1.00 34.50 ? 75  ASP   B CA  1 
ATOM   769  C  C   . ASP   B 2 66  ? -15.646 -0.613  -7.871  1.00 34.25 ? 75  ASP   B C   1 
ATOM   770  O  O   . ASP   B 2 66  ? -15.704 -0.302  -9.047  1.00 34.15 ? 75  ASP   B O   1 
ATOM   771  C  CB  . ASP   B 2 66  ? -13.125 -0.572  -8.161  1.00 34.77 ? 75  ASP   B CB  1 
ATOM   772  C  CG  . ASP   B 2 66  ? -13.053 0.817   -8.761  1.00 36.70 ? 75  ASP   B CG  1 
ATOM   773  O  OD1 . ASP   B 2 66  ? -13.488 1.774   -8.094  1.00 35.26 ? 75  ASP   B OD1 1 
ATOM   774  O  OD2 . ASP   B 2 66  ? -12.578 0.943   -9.902  1.00 40.35 ? 75  ASP   B OD2 1 
ATOM   775  N  N   . LEU   B 2 67  ? -16.731 -0.867  -7.141  1.00 33.93 ? 76  LEU   B N   1 
ATOM   776  C  CA  . LEU   B 2 67  ? -18.076 -0.766  -7.707  1.00 33.90 ? 76  LEU   B CA  1 
ATOM   777  C  C   . LEU   B 2 67  ? -19.012 -0.018  -6.768  1.00 33.67 ? 76  LEU   B C   1 
ATOM   778  O  O   . LEU   B 2 67  ? -18.693 0.141   -5.594  1.00 34.04 ? 76  LEU   B O   1 
ATOM   779  C  CB  . LEU   B 2 67  ? -18.636 -2.153  -8.032  1.00 34.07 ? 76  LEU   B CB  1 
ATOM   780  C  CG  . LEU   B 2 67  ? -17.929 -2.914  -9.134  1.00 35.57 ? 76  LEU   B CG  1 
ATOM   781  C  CD1 . LEU   B 2 67  ? -18.439 -4.331  -9.205  1.00 35.73 ? 76  LEU   B CD1 1 
ATOM   782  C  CD2 . LEU   B 2 67  ? -18.069 -2.188  -10.492 1.00 36.39 ? 76  LEU   B CD2 1 
ATOM   783  N  N   . VAL   B 2 68  ? -20.150 0.475   -7.290  1.00 33.10 ? 77  VAL   B N   1 
ATOM   784  C  CA  . VAL   B 2 68  ? -21.146 1.213   -6.516  1.00 33.12 ? 77  VAL   B CA  1 
ATOM   785  C  C   . VAL   B 2 68  ? -22.503 1.193   -7.250  1.00 32.45 ? 77  VAL   B C   1 
ATOM   786  O  O   . VAL   B 2 68  ? -22.557 1.326   -8.465  1.00 32.62 ? 77  VAL   B O   1 
ATOM   787  C  CB  . VAL   B 2 68  ? -20.676 2.665   -6.134  1.00 33.92 ? 77  VAL   B CB  1 
ATOM   788  C  CG1 . VAL   B 2 68  ? -20.442 3.525   -7.365  1.00 34.42 ? 77  VAL   B CG1 1 
ATOM   789  C  CG2 . VAL   B 2 68  ? -21.650 3.351   -5.181  1.00 34.28 ? 77  VAL   B CG2 1 
ATOM   790  N  N   . SER   B 2 69  ? -23.591 0.972   -6.515  1.00 31.91 ? 78  SER   B N   1 
ATOM   791  C  CA  . SER   B 2 69  ? -24.937 1.001   -7.089  1.00 31.43 ? 78  SER   B CA  1 
ATOM   792  C  C   . SER   B 2 69  ? -25.746 2.147   -6.418  1.00 31.09 ? 78  SER   B C   1 
ATOM   793  O  O   . SER   B 2 69  ? -25.487 2.494   -5.265  1.00 30.94 ? 78  SER   B O   1 
ATOM   794  C  CB  . SER   B 2 69  ? -25.628 -0.352  -6.932  1.00 31.44 ? 78  SER   B CB  1 
ATOM   795  O  OG  . SER   B 2 69  ? -26.193 -0.508  -5.644  1.00 31.98 ? 78  SER   B OG  1 
ATOM   796  N  N   . TYR   B 2 70  ? -26.708 2.731   -7.148  1.00 30.81 ? 79  TYR   B N   1 
ATOM   797  C  CA  . TYR   B 2 70  ? -27.541 3.847   -6.685  1.00 30.46 ? 79  TYR   B CA  1 
ATOM   798  C  C   . TYR   B 2 70  ? -29.021 3.469   -6.811  1.00 30.77 ? 79  TYR   B C   1 
ATOM   799  O  O   . TYR   B 2 70  ? -29.398 2.890   -7.815  1.00 30.74 ? 79  TYR   B O   1 
ATOM   800  C  CB  . TYR   B 2 70  ? -27.270 5.093   -7.552  1.00 30.05 ? 79  TYR   B CB  1 
ATOM   801  C  CG  . TYR   B 2 70  ? -25.964 5.782   -7.230  1.00 30.62 ? 79  TYR   B CG  1 
ATOM   802  C  CD1 . TYR   B 2 70  ? -24.755 5.274   -7.690  1.00 31.02 ? 79  TYR   B CD1 1 
ATOM   803  C  CD2 . TYR   B 2 70  ? -25.936 6.955   -6.481  1.00 31.47 ? 79  TYR   B CD2 1 
ATOM   804  C  CE1 . TYR   B 2 70  ? -23.547 5.873   -7.360  1.00 31.60 ? 79  TYR   B CE1 1 
ATOM   805  C  CE2 . TYR   B 2 70  ? -24.734 7.557   -6.132  1.00 32.03 ? 79  TYR   B CE2 1 
ATOM   806  C  CZ  . TYR   B 2 70  ? -23.538 7.018   -6.588  1.00 32.77 ? 79  TYR   B CZ  1 
ATOM   807  O  OH  . TYR   B 2 70  ? -22.341 7.632   -6.302  1.00 33.34 ? 79  TYR   B OH  1 
ATOM   808  N  N   . CYS   B 2 71  ? -29.844 3.783   -5.797  1.00 31.02 ? 80  CYS   B N   1 
ATOM   809  C  CA  . CYS   B 2 71  ? -31.304 3.552   -5.742  1.00 31.83 ? 80  CYS   B CA  1 
ATOM   810  C  C   . CYS   B 2 71  ? -31.710 2.111   -5.372  1.00 31.64 ? 80  CYS   B C   1 
ATOM   811  O  O   . CYS   B 2 71  ? -32.833 1.904   -4.902  1.00 31.83 ? 80  CYS   B O   1 
ATOM   812  C  CB  . CYS   B 2 71  ? -32.011 4.012   -7.015  1.00 33.80 ? 80  CYS   B CB  1 
ATOM   813  S  SG  . CYS   B 2 71  ? -31.724 5.752   -7.447  1.00 40.79 ? 80  CYS   B SG  1 
ATOM   814  N  N   . GLY   B 2 72  ? -30.807 1.146   -5.546  1.00 30.31 ? 81  GLY   B N   1 
ATOM   815  C  CA  . GLY   B 2 72  ? -31.087 -0.246  -5.206  1.00 29.27 ? 81  GLY   B CA  1 
ATOM   816  C  C   . GLY   B 2 72  ? -29.858 -1.122  -5.313  1.00 28.92 ? 81  GLY   B C   1 
ATOM   817  O  O   . GLY   B 2 72  ? -28.772 -0.631  -5.614  1.00 29.08 ? 81  GLY   B O   1 
ATOM   818  N  N   . PRO   B 2 73  ? -29.983 -2.438  -5.073  1.00 28.91 ? 82  PRO   B N   1 
ATOM   819  C  CA  . PRO   B 2 73  ? -28.795 -3.311  -5.157  1.00 30.23 ? 82  PRO   B CA  1 
ATOM   820  C  C   . PRO   B 2 73  ? -28.264 -3.572  -6.577  1.00 32.72 ? 82  PRO   B C   1 
ATOM   821  O  O   . PRO   B 2 73  ? -28.978 -3.379  -7.574  1.00 32.56 ? 82  PRO   B O   1 
ATOM   822  C  CB  . PRO   B 2 73  ? -29.261 -4.602  -4.480  1.00 30.66 ? 82  PRO   B CB  1 
ATOM   823  C  CG  . PRO   B 2 73  ? -30.753 -4.597  -4.644  1.00 30.23 ? 82  PRO   B CG  1 
ATOM   824  C  CD  . PRO   B 2 73  ? -31.197 -3.178  -4.671  1.00 27.90 ? 82  PRO   B CD  1 
ATOM   825  N  N   . TRP   B 2 74  ? -26.992 -4.041  -6.681  1.00 33.99 ? 83  TRP   B N   1 
ATOM   826  C  CA  . TRP   B 2 74  ? -26.359 -4.340  -7.973  1.00 35.57 ? 83  TRP   B CA  1 
ATOM   827  C  C   . TRP   B 2 74  ? -27.209 -5.375  -8.721  1.00 36.95 ? 83  TRP   B C   1 
ATOM   828  O  O   . TRP   B 2 74  ? -27.518 -6.425  -8.146  1.00 37.26 ? 83  TRP   B O   1 
ATOM   829  C  CB  . TRP   B 2 74  ? -24.909 -4.834  -7.772  1.00 35.76 ? 83  TRP   B CB  1 
ATOM   830  C  CG  . TRP   B 2 74  ? -24.122 -4.958  -9.041  1.00 36.37 ? 83  TRP   B CG  1 
ATOM   831  C  CD1 . TRP   B 2 74  ? -24.080 -6.032  -9.878  1.00 37.24 ? 83  TRP   B CD1 1 
ATOM   832  C  CD2 . TRP   B 2 74  ? -23.254 -3.970  -9.610  1.00 36.47 ? 83  TRP   B CD2 1 
ATOM   833  N  NE1 . TRP   B 2 74  ? -23.251 -5.767  -10.947 1.00 37.52 ? 83  TRP   B NE1 1 
ATOM   834  C  CE2 . TRP   B 2 74  ? -22.723 -4.512  -10.800 1.00 37.26 ? 83  TRP   B CE2 1 
ATOM   835  C  CE3 . TRP   B 2 74  ? -22.852 -2.689  -9.215  1.00 36.94 ? 83  TRP   B CE3 1 
ATOM   836  C  CZ2 . TRP   B 2 74  ? -21.837 -3.806  -11.610 1.00 38.06 ? 83  TRP   B CZ2 1 
ATOM   837  C  CZ3 . TRP   B 2 74  ? -21.987 -1.987  -10.029 1.00 38.01 ? 83  TRP   B CZ3 1 
ATOM   838  C  CH2 . TRP   B 2 74  ? -21.517 -2.532  -11.227 1.00 38.26 ? 83  TRP   B CH2 1 
ATOM   839  N  N   . LYS   B 2 75  ? -27.702 -5.002  -9.930  1.00 37.16 ? 84  LYS   B N   1 
ATOM   840  C  CA  . LYS   B 2 75  ? -28.612 -5.797  -10.761 1.00 37.58 ? 84  LYS   B CA  1 
ATOM   841  C  C   . LYS   B 2 75  ? -27.923 -6.610  -11.853 1.00 39.44 ? 84  LYS   B C   1 
ATOM   842  O  O   . LYS   B 2 75  ? -28.542 -7.514  -12.416 1.00 39.80 ? 84  LYS   B O   1 
ATOM   843  C  CB  . LYS   B 2 75  ? -29.648 -4.884  -11.430 1.00 37.34 ? 84  LYS   B CB  1 
ATOM   844  C  CG  . LYS   B 2 75  ? -30.560 -4.138  -10.476 1.00 38.93 ? 84  LYS   B CG  1 
ATOM   845  C  CD  . LYS   B 2 75  ? -31.485 -5.081  -9.746  1.00 42.38 ? 84  LYS   B CD  1 
ATOM   846  C  CE  . LYS   B 2 75  ? -32.046 -4.479  -8.482  1.00 44.90 ? 84  LYS   B CE  1 
ATOM   847  N  NZ  . LYS   B 2 75  ? -33.401 -3.919  -8.697  1.00 47.01 ? 84  LYS   B NZ  1 
ATOM   848  N  N   . LEU   B 2 76  ? -26.678 -6.258  -12.199 1.00 40.18 ? 85  LEU   B N   1 
ATOM   849  C  CA  . LEU   B 2 76  ? -25.918 -6.888  -13.272 1.00 41.00 ? 85  LEU   B CA  1 
ATOM   850  C  C   . LEU   B 2 76  ? -25.338 -8.239  -12.834 1.00 43.17 ? 85  LEU   B C   1 
ATOM   851  O  O   . LEU   B 2 76  ? -24.611 -8.301  -11.856 1.00 43.36 ? 85  LEU   B O   1 
ATOM   852  C  CB  . LEU   B 2 76  ? -24.832 -5.924  -13.782 1.00 40.19 ? 85  LEU   B CB  1 
ATOM   853  C  CG  . LEU   B 2 76  ? -25.274 -4.464  -14.027 1.00 40.67 ? 85  LEU   B CG  1 
ATOM   854  C  CD1 . LEU   B 2 76  ? -24.122 -3.593  -14.471 1.00 40.98 ? 85  LEU   B CD1 1 
ATOM   855  C  CD2 . LEU   B 2 76  ? -26.369 -4.375  -15.027 1.00 40.87 ? 85  LEU   B CD2 1 
ATOM   856  N  N   . ASP   B 2 77  ? -25.683 -9.326  -13.532 1.00 45.33 ? 86  ASP   B N   1 
ATOM   857  C  CA  . ASP   B 2 77  ? -25.227 -10.670 -13.144 1.00 47.97 ? 86  ASP   B CA  1 
ATOM   858  C  C   . ASP   B 2 77  ? -24.552 -11.475 -14.265 1.00 49.21 ? 86  ASP   B C   1 
ATOM   859  O  O   . ASP   B 2 77  ? -23.936 -12.505 -13.984 1.00 49.73 ? 86  ASP   B O   1 
ATOM   860  C  CB  . ASP   B 2 77  ? -26.380 -11.490 -12.523 1.00 50.92 ? 86  ASP   B CB  1 
ATOM   861  C  CG  . ASP   B 2 77  ? -27.613 -11.625 -13.402 1.00 58.56 ? 86  ASP   B CG  1 
ATOM   862  O  OD1 . ASP   B 2 77  ? -27.638 -11.011 -14.497 1.00 60.07 ? 86  ASP   B OD1 1 
ATOM   863  O  OD2 . ASP   B 2 77  ? -28.560 -12.342 -12.995 1.00 61.90 ? 86  ASP   B OD2 1 
ATOM   864  N  N   . ALA   B 2 78  ? -24.670 -11.027 -15.515 1.00 49.42 ? 87  ALA   B N   1 
ATOM   865  C  CA  . ALA   B 2 78  ? -24.081 -11.739 -16.654 1.00 50.14 ? 87  ALA   B CA  1 
ATOM   866  C  C   . ALA   B 2 78  ? -22.552 -11.790 -16.575 1.00 50.75 ? 87  ALA   B C   1 
ATOM   867  O  O   . ALA   B 2 78  ? -21.941 -10.915 -15.957 1.00 50.90 ? 87  ALA   B O   1 
ATOM   868  C  CB  . ALA   B 2 78  ? -24.530 -11.107 -17.963 1.00 50.09 ? 87  ALA   B CB  1 
ATOM   869  N  N   . ALA   B 2 79  ? -21.933 -12.829 -17.163 1.00 50.84 ? 88  ALA   B N   1 
ATOM   870  C  CA  . ALA   B 2 79  ? -20.476 -12.964 -17.092 1.00 51.55 ? 88  ALA   B CA  1 
ATOM   871  C  C   . ALA   B 2 79  ? -19.813 -13.355 -18.406 1.00 51.91 ? 88  ALA   B C   1 
ATOM   872  O  O   . ALA   B 2 79  ? -20.441 -14.005 -19.236 1.00 52.20 ? 88  ALA   B O   1 
ATOM   873  C  CB  . ALA   B 2 79  ? -20.108 -13.976 -16.021 1.00 51.71 ? 88  ALA   B CB  1 
ATOM   874  N  N   . TRP   B 2 80  ? -18.530 -12.990 -18.586 1.00 51.87 ? 89  TRP   B N   1 
ATOM   875  C  CA  . TRP   B 2 80  ? -17.775 -13.400 -19.767 1.00 52.75 ? 89  TRP   B CA  1 
ATOM   876  C  C   . TRP   B 2 80  ? -17.601 -14.927 -19.729 1.00 53.25 ? 89  TRP   B C   1 
ATOM   877  O  O   . TRP   B 2 80  ? -17.371 -15.484 -18.661 1.00 53.27 ? 89  TRP   B O   1 
ATOM   878  C  CB  . TRP   B 2 80  ? -16.396 -12.727 -19.815 1.00 52.89 ? 89  TRP   B CB  1 
ATOM   879  C  CG  . TRP   B 2 80  ? -15.600 -13.106 -21.035 1.00 53.58 ? 89  TRP   B CG  1 
ATOM   880  C  CD1 . TRP   B 2 80  ? -16.039 -13.121 -22.327 1.00 54.71 ? 89  TRP   B CD1 1 
ATOM   881  C  CD2 . TRP   B 2 80  ? -14.213 -13.459 -21.078 1.00 53.52 ? 89  TRP   B CD2 1 
ATOM   882  N  NE1 . TRP   B 2 80  ? -15.016 -13.491 -23.169 1.00 54.86 ? 89  TRP   B NE1 1 
ATOM   883  C  CE2 . TRP   B 2 80  ? -13.877 -13.679 -22.429 1.00 54.40 ? 89  TRP   B CE2 1 
ATOM   884  C  CE3 . TRP   B 2 80  ? -13.219 -13.601 -20.108 1.00 54.07 ? 89  TRP   B CE3 1 
ATOM   885  C  CZ2 . TRP   B 2 80  ? -12.599 -14.068 -22.826 1.00 54.87 ? 89  TRP   B CZ2 1 
ATOM   886  C  CZ3 . TRP   B 2 80  ? -11.952 -13.973 -20.507 1.00 54.96 ? 89  TRP   B CZ3 1 
ATOM   887  C  CH2 . TRP   B 2 80  ? -11.652 -14.202 -21.852 1.00 54.96 ? 89  TRP   B CH2 1 
ATOM   888  N  N   . ASP   B 2 81  ? -17.776 -15.598 -20.868 1.00 53.51 ? 90  ASP   B N   1 
ATOM   889  C  CA  . ASP   B 2 81  ? -17.673 -17.054 -20.925 1.00 54.23 ? 90  ASP   B CA  1 
ATOM   890  C  C   . ASP   B 2 81  ? -16.244 -17.592 -21.112 1.00 55.40 ? 90  ASP   B C   1 
ATOM   891  O  O   . ASP   B 2 81  ? -16.062 -18.802 -21.233 1.00 55.29 ? 90  ASP   B O   1 
ATOM   892  C  CB  . ASP   B 2 81  ? -18.605 -17.612 -22.012 1.00 54.77 ? 90  ASP   B CB  1 
ATOM   893  C  CG  . ASP   B 2 81  ? -18.286 -17.168 -23.427 1.00 57.80 ? 90  ASP   B CG  1 
ATOM   894  O  OD1 . ASP   B 2 81  ? -17.380 -16.319 -23.597 1.00 58.49 ? 90  ASP   B OD1 1 
ATOM   895  O  OD2 . ASP   B 2 81  ? -18.942 -17.667 -24.369 1.00 58.83 ? 90  ASP   B OD2 1 
ATOM   896  N  N   . GLY   B 2 82  ? -15.260 -16.698 -21.169 1.00 56.22 ? 91  GLY   B N   1 
ATOM   897  C  CA  . GLY   B 2 82  ? -13.868 -17.064 -21.379 1.00 57.20 ? 91  GLY   B CA  1 
ATOM   898  C  C   . GLY   B 2 82  ? -13.541 -17.469 -22.805 1.00 58.38 ? 91  GLY   B C   1 
ATOM   899  O  O   . GLY   B 2 82  ? -12.386 -17.774 -23.112 1.00 58.75 ? 91  GLY   B O   1 
ATOM   900  N  N   . LEU   B 2 83  ? -14.538 -17.477 -23.696 1.00 58.79 ? 92  LEU   B N   1 
ATOM   901  C  CA  . LEU   B 2 83  ? -14.334 -17.924 -25.055 1.00 59.57 ? 92  LEU   B CA  1 
ATOM   902  C  C   . LEU   B 2 83  ? -14.598 -16.912 -26.132 1.00 59.65 ? 92  LEU   B C   1 
ATOM   903  O  O   . LEU   B 2 83  ? -13.771 -16.777 -27.028 1.00 60.17 ? 92  LEU   B O   1 
ATOM   904  C  CB  . LEU   B 2 83  ? -15.180 -19.169 -25.312 1.00 60.35 ? 92  LEU   B CB  1 
ATOM   905  C  CG  . LEU   B 2 83  ? -14.511 -20.461 -24.978 1.00 63.08 ? 92  LEU   B CG  1 
ATOM   906  C  CD1 . LEU   B 2 83  ? -15.492 -21.599 -25.072 1.00 64.35 ? 92  LEU   B CD1 1 
ATOM   907  C  CD2 . LEU   B 2 83  ? -13.347 -20.702 -25.897 1.00 64.01 ? 92  LEU   B CD2 1 
ATOM   908  N  N   . SER   B 2 84  ? -15.755 -16.245 -26.104 1.00 58.95 ? 93  SER   B N   1 
ATOM   909  C  CA  . SER   B 2 84  ? -16.144 -15.365 -27.202 1.00 58.67 ? 93  SER   B CA  1 
ATOM   910  C  C   . SER   B 2 84  ? -15.673 -13.908 -27.089 1.00 57.97 ? 93  SER   B C   1 
ATOM   911  O  O   . SER   B 2 84  ? -15.166 -13.477 -26.049 1.00 58.62 ? 93  SER   B O   1 
ATOM   912  C  CB  . SER   B 2 84  ? -17.656 -15.424 -27.420 1.00 60.20 ? 93  SER   B CB  1 
ATOM   913  O  OG  . SER   B 2 84  ? -18.393 -15.489 -26.211 1.00 62.64 ? 93  SER   B OG  1 
ATOM   914  N  N   . GLU   B 2 85  ? -15.788 -13.173 -28.204 1.00 56.56 ? 94  GLU   B N   1 
ATOM   915  C  CA  . GLU   B 2 85  ? -15.450 -11.767 -28.254 1.00 55.83 ? 94  GLU   B CA  1 
ATOM   916  C  C   . GLU   B 2 85  ? -16.556 -10.983 -27.557 1.00 54.32 ? 94  GLU   B C   1 
ATOM   917  O  O   . GLU   B 2 85  ? -17.710 -11.414 -27.485 1.00 54.83 ? 94  GLU   B O   1 
ATOM   918  C  CB  . GLU   B 2 85  ? -15.296 -11.281 -29.709 1.00 58.60 ? 94  GLU   B CB  1 
ATOM   919  C  CG  . GLU   B 2 85  ? -14.136 -11.913 -30.469 1.00 63.46 ? 94  GLU   B CG  1 
ATOM   920  C  CD  . GLU   B 2 85  ? -13.568 -11.054 -31.585 1.00 68.24 ? 94  GLU   B CD  1 
ATOM   921  O  OE1 . GLU   B 2 85  ? -14.312 -10.206 -32.132 1.00 68.93 ? 94  GLU   B OE1 1 
ATOM   922  O  OE2 . GLU   B 2 85  ? -12.369 -11.221 -31.904 1.00 69.84 ? 94  GLU   B OE2 1 
ATOM   923  N  N   . VAL   B 2 86  ? -16.189 -9.837  -27.021 1.00 52.23 ? 95  VAL   B N   1 
ATOM   924  C  CA  . VAL   B 2 86  ? -17.086 -8.952  -26.296 1.00 50.59 ? 95  VAL   B CA  1 
ATOM   925  C  C   . VAL   B 2 86  ? -17.063 -7.564  -26.979 1.00 49.64 ? 95  VAL   B C   1 
ATOM   926  O  O   . VAL   B 2 86  ? -16.290 -7.342  -27.920 1.00 49.65 ? 95  VAL   B O   1 
ATOM   927  C  CB  . VAL   B 2 86  ? -16.646 -8.864  -24.800 1.00 50.58 ? 95  VAL   B CB  1 
ATOM   928  C  CG1 . VAL   B 2 86  ? -16.472 -10.250 -24.178 1.00 50.52 ? 95  VAL   B CG1 1 
ATOM   929  C  CG2 . VAL   B 2 86  ? -15.379 -8.025  -24.651 1.00 50.73 ? 95  VAL   B CG2 1 
ATOM   930  N  N   . GLN   B 2 87  ? -17.915 -6.636  -26.523 1.00 48.51 ? 96  GLN   B N   1 
ATOM   931  C  CA  . GLN   B 2 87  ? -17.916 -5.289  -27.054 1.00 47.68 ? 96  GLN   B CA  1 
ATOM   932  C  C   . GLN   B 2 87  ? -17.834 -4.317  -25.886 1.00 46.68 ? 96  GLN   B C   1 
ATOM   933  O  O   . GLN   B 2 87  ? -18.600 -4.437  -24.941 1.00 46.27 ? 96  GLN   B O   1 
ATOM   934  C  CB  . GLN   B 2 87  ? -19.178 -5.032  -27.907 1.00 48.79 ? 96  GLN   B CB  1 
ATOM   935  C  CG  . GLN   B 2 87  ? -18.875 -4.809  -29.390 1.00 51.67 ? 96  GLN   B CG  1 
ATOM   936  C  CD  . GLN   B 2 87  ? -20.066 -4.963  -30.320 1.00 55.34 ? 96  GLN   B CD  1 
ATOM   937  O  OE1 . GLN   B 2 87  ? -21.189 -4.500  -30.055 1.00 55.29 ? 96  GLN   B OE1 1 
ATOM   938  N  NE2 . GLN   B 2 87  ? -19.830 -5.600  -31.466 1.00 56.29 ? 96  GLN   B NE2 1 
ATOM   939  N  N   . LEU   B 2 88  ? -16.901 -3.370  -25.937 1.00 45.91 ? 97  LEU   B N   1 
ATOM   940  C  CA  . LEU   B 2 88  ? -16.846 -2.309  -24.942 1.00 45.29 ? 97  LEU   B CA  1 
ATOM   941  C  C   . LEU   B 2 88  ? -17.696 -1.161  -25.538 1.00 44.98 ? 97  LEU   B C   1 
ATOM   942  O  O   . LEU   B 2 88  ? -17.306 -0.589  -26.551 1.00 45.10 ? 97  LEU   B O   1 
ATOM   943  C  CB  . LEU   B 2 88  ? -15.389 -1.844  -24.705 1.00 45.04 ? 97  LEU   B CB  1 
ATOM   944  C  CG  . LEU   B 2 88  ? -15.201 -0.470  -24.022 1.00 45.56 ? 97  LEU   B CG  1 
ATOM   945  C  CD1 . LEU   B 2 88  ? -15.794 -0.466  -22.623 1.00 45.88 ? 97  LEU   B CD1 1 
ATOM   946  C  CD2 . LEU   B 2 88  ? -13.745 -0.079  -23.978 1.00 45.62 ? 97  LEU   B CD2 1 
ATOM   947  N  N   . LEU   B 2 89  ? -18.862 -0.855  -24.950 1.00 44.49 ? 98  LEU   B N   1 
ATOM   948  C  CA  . LEU   B 2 89  ? -19.662 0.265   -25.416 1.00 44.18 ? 98  LEU   B CA  1 
ATOM   949  C  C   . LEU   B 2 89  ? -18.983 1.468   -24.758 1.00 43.99 ? 98  LEU   B C   1 
ATOM   950  O  O   . LEU   B 2 89  ? -19.326 1.844   -23.643 1.00 44.35 ? 98  LEU   B O   1 
ATOM   951  C  CB  . LEU   B 2 89  ? -21.133 0.090   -24.996 1.00 44.21 ? 98  LEU   B CB  1 
ATOM   952  C  CG  . LEU   B 2 89  ? -22.087 1.297   -25.025 1.00 45.50 ? 98  LEU   B CG  1 
ATOM   953  C  CD1 . LEU   B 2 89  ? -22.026 2.055   -26.330 1.00 46.32 ? 98  LEU   B CD1 1 
ATOM   954  C  CD2 . LEU   B 2 89  ? -23.495 0.861   -24.761 1.00 46.13 ? 98  LEU   B CD2 1 
ATOM   955  N  N   . ALA   B 2 90  ? -17.949 2.011   -25.427 1.00 42.94 ? 99  ALA   B N   1 
ATOM   956  C  CA  . ALA   B 2 90  ? -17.148 3.118   -24.916 1.00 42.15 ? 99  ALA   B CA  1 
ATOM   957  C  C   . ALA   B 2 90  ? -17.853 4.450   -25.041 1.00 41.77 ? 99  ALA   B C   1 
ATOM   958  O  O   . ALA   B 2 90  ? -18.256 4.820   -26.136 1.00 42.21 ? 99  ALA   B O   1 
ATOM   959  C  CB  . ALA   B 2 90  ? -15.827 3.188   -25.651 1.00 41.75 ? 99  ALA   B CB  1 
ATOM   960  N  N   . VAL   B 2 91  ? -17.952 5.199   -23.938 1.00 40.98 ? 100 VAL   B N   1 
ATOM   961  C  CA  . VAL   B 2 91  ? -18.551 6.524   -23.968 1.00 40.67 ? 100 VAL   B CA  1 
ATOM   962  C  C   . VAL   B 2 91  ? -17.444 7.500   -23.570 1.00 41.74 ? 100 VAL   B C   1 
ATOM   963  O  O   . VAL   B 2 91  ? -17.222 7.732   -22.392 1.00 41.83 ? 100 VAL   B O   1 
ATOM   964  C  CB  . VAL   B 2 91  ? -19.786 6.607   -23.045 1.00 39.69 ? 100 VAL   B CB  1 
ATOM   965  C  CG1 . VAL   B 2 91  ? -20.414 7.989   -23.101 1.00 39.89 ? 100 VAL   B CG1 1 
ATOM   966  C  CG2 . VAL   B 2 91  ? -20.802 5.536   -23.401 1.00 39.23 ? 100 VAL   B CG2 1 
ATOM   967  N  N   . PRO   B 2 92  ? -16.679 8.024   -24.542 1.00 42.46 ? 101 PRO   B N   1 
ATOM   968  C  CA  . PRO   B 2 92  ? -15.544 8.895   -24.190 1.00 43.22 ? 101 PRO   B CA  1 
ATOM   969  C  C   . PRO   B 2 92  ? -15.923 10.359  -23.951 1.00 44.19 ? 101 PRO   B C   1 
ATOM   970  O  O   . PRO   B 2 92  ? -16.932 10.828  -24.484 1.00 44.46 ? 101 PRO   B O   1 
ATOM   971  C  CB  . PRO   B 2 92  ? -14.577 8.717   -25.376 1.00 43.73 ? 101 PRO   B CB  1 
ATOM   972  C  CG  . PRO   B 2 92  ? -15.345 7.939   -26.425 1.00 43.95 ? 101 PRO   B CG  1 
ATOM   973  C  CD  . PRO   B 2 92  ? -16.773 7.822   -25.999 1.00 41.85 ? 101 PRO   B CD  1 
ATOM   974  N  N   . PRO   B 2 93  ? -15.140 11.101  -23.143 1.00 44.36 ? 102 PRO   B N   1 
ATOM   975  C  CA  . PRO   B 2 93  ? -15.494 12.513  -22.884 1.00 44.37 ? 102 PRO   B CA  1 
ATOM   976  C  C   . PRO   B 2 93  ? -15.667 13.348  -24.160 1.00 44.59 ? 102 PRO   B C   1 
ATOM   977  O  O   . PRO   B 2 93  ? -14.832 13.277  -25.067 1.00 44.32 ? 102 PRO   B O   1 
ATOM   978  C  CB  . PRO   B 2 93  ? -14.342 13.013  -22.001 1.00 45.10 ? 102 PRO   B CB  1 
ATOM   979  C  CG  . PRO   B 2 93  ? -13.790 11.751  -21.348 1.00 45.35 ? 102 PRO   B CG  1 
ATOM   980  C  CD  . PRO   B 2 93  ? -13.937 10.684  -22.390 1.00 43.68 ? 102 PRO   B CD  1 
ATOM   981  N  N   . GLY   B 2 94  ? -16.792 14.067  -24.250 1.00 44.42 ? 103 GLY   B N   1 
ATOM   982  C  CA  . GLY   B 2 94  ? -17.133 14.903  -25.402 1.00 44.35 ? 103 GLY   B CA  1 
ATOM   983  C  C   . GLY   B 2 94  ? -17.349 14.169  -26.720 1.00 44.58 ? 103 GLY   B C   1 
ATOM   984  O  O   . GLY   B 2 94  ? -17.566 14.794  -27.761 1.00 44.46 ? 103 GLY   B O   1 
ATOM   985  N  N   . GLU   B 2 95  ? -17.270 12.836  -26.703 1.00 44.70 ? 104 GLU   B N   1 
ATOM   986  C  CA  . GLU   B 2 95  ? -17.398 12.037  -27.914 1.00 45.28 ? 104 GLU   B CA  1 
ATOM   987  C  C   . GLU   B 2 95  ? -18.555 11.081  -27.816 1.00 46.76 ? 104 GLU   B C   1 
ATOM   988  O  O   . GLU   B 2 95  ? -18.862 10.597  -26.726 1.00 47.02 ? 104 GLU   B O   1 
ATOM   989  C  CB  . GLU   B 2 95  ? -16.096 11.264  -28.181 1.00 46.27 ? 104 GLU   B CB  1 
ATOM   990  C  CG  . GLU   B 2 95  ? -14.909 12.171  -28.447 1.00 48.77 ? 104 GLU   B CG  1 
ATOM   991  C  CD  . GLU   B 2 95  ? -13.570 11.466  -28.563 1.00 53.42 ? 104 GLU   B CD  1 
ATOM   992  O  OE1 . GLU   B 2 95  ? -13.505 10.248  -28.269 1.00 53.12 ? 104 GLU   B OE1 1 
ATOM   993  O  OE2 . GLU   B 2 95  ? -12.584 12.132  -28.957 1.00 54.93 ? 104 GLU   B OE2 1 
ATOM   994  N  N   . ARG   B 2 96  ? -19.165 10.771  -28.965 1.00 47.84 ? 105 ARG   B N   1 
ATOM   995  C  CA  . ARG   B 2 96  ? -20.317 9.887   -29.098 1.00 49.59 ? 105 ARG   B CA  1 
ATOM   996  C  C   . ARG   B 2 96  ? -20.013 8.461   -28.674 1.00 50.39 ? 105 ARG   B C   1 
ATOM   997  O  O   . ARG   B 2 96  ? -18.908 7.980   -28.920 1.00 51.05 ? 105 ARG   B O   1 
ATOM   998  C  CB  . ARG   B 2 96  ? -20.801 9.913   -30.551 1.00 52.44 ? 105 ARG   B CB  1 
ATOM   999  C  CG  . ARG   B 2 96  ? -22.053 9.092   -30.828 1.00 57.25 ? 105 ARG   B CG  1 
ATOM   1000 C  CD  . ARG   B 2 96  ? -22.924 9.749   -31.887 1.00 61.56 ? 105 ARG   B CD  1 
ATOM   1001 N  NE  . ARG   B 2 96  ? -22.241 9.926   -33.172 1.00 66.06 ? 105 ARG   B NE  1 
ATOM   1002 C  CZ  . ARG   B 2 96  ? -21.956 11.110  -33.717 1.00 69.07 ? 105 ARG   B CZ  1 
ATOM   1003 N  NH1 . ARG   B 2 96  ? -22.254 12.231  -33.078 1.00 68.57 ? 105 ARG   B NH1 1 
ATOM   1004 N  NH2 . ARG   B 2 96  ? -21.355 11.177  -34.899 1.00 69.07 ? 105 ARG   B NH2 1 
ATOM   1005 N  N   . ALA   B 2 97  ? -20.988 7.798   -28.001 1.00 50.24 ? 106 ALA   B N   1 
ATOM   1006 C  CA  . ALA   B 2 97  ? -20.924 6.403   -27.558 1.00 50.38 ? 106 ALA   B CA  1 
ATOM   1007 C  C   . ALA   B 2 97  ? -20.656 5.512   -28.758 1.00 51.05 ? 106 ALA   B C   1 
ATOM   1008 O  O   . ALA   B 2 97  ? -21.269 5.706   -29.808 1.00 51.90 ? 106 ALA   B O   1 
ATOM   1009 C  CB  . ALA   B 2 97  ? -22.248 6.007   -26.926 1.00 50.25 ? 106 ALA   B CB  1 
ATOM   1010 N  N   . LYS   B 2 98  ? -19.729 4.565   -28.631 1.00 50.99 ? 107 LYS   B N   1 
ATOM   1011 C  CA  . LYS   B 2 98  ? -19.368 3.693   -29.748 1.00 51.47 ? 107 LYS   B CA  1 
ATOM   1012 C  C   . LYS   B 2 98  ? -18.913 2.297   -29.259 1.00 50.72 ? 107 LYS   B C   1 
ATOM   1013 O  O   . LYS   B 2 98  ? -18.136 2.213   -28.314 1.00 50.42 ? 107 LYS   B O   1 
ATOM   1014 C  CB  . LYS   B 2 98  ? -18.316 4.426   -30.601 1.00 54.84 ? 107 LYS   B CB  1 
ATOM   1015 C  CG  . LYS   B 2 98  ? -17.386 3.585   -31.473 1.00 61.43 ? 107 LYS   B CG  1 
ATOM   1016 C  CD  . LYS   B 2 98  ? -16.063 4.358   -31.751 1.00 67.30 ? 107 LYS   B CD  1 
ATOM   1017 C  CE  . LYS   B 2 98  ? -15.405 4.850   -30.462 1.00 71.64 ? 107 LYS   B CE  1 
ATOM   1018 N  NZ  . LYS   B 2 98  ? -13.994 5.277   -30.660 1.00 74.18 ? 107 LYS   B NZ  1 
ATOM   1019 N  N   . ASN   B 2 99  ? -19.458 1.215   -29.868 1.00 50.56 ? 108 ASN   B N   1 
ATOM   1020 C  CA  . ASN   B 2 99  ? -19.161 -0.183  -29.530 1.00 51.22 ? 108 ASN   B CA  1 
ATOM   1021 C  C   . ASN   B 2 99  ? -17.836 -0.619  -30.153 1.00 51.91 ? 108 ASN   B C   1 
ATOM   1022 O  O   . ASN   B 2 99  ? -17.682 -0.542  -31.365 1.00 52.52 ? 108 ASN   B O   1 
ATOM   1023 C  CB  . ASN   B 2 99  ? -20.264 -1.132  -30.036 1.00 52.18 ? 108 ASN   B CB  1 
ATOM   1024 C  CG  . ASN   B 2 99  ? -21.634 -0.959  -29.407 1.00 55.52 ? 108 ASN   B CG  1 
ATOM   1025 O  OD1 . ASN   B 2 99  ? -22.114 0.153   -29.194 1.00 56.97 ? 108 ASN   B OD1 1 
ATOM   1026 N  ND2 . ASN   B 2 99  ? -22.321 -2.062  -29.133 1.00 55.64 ? 108 ASN   B ND2 1 
ATOM   1027 N  N   . ILE   B 2 100 ? -16.896 -1.103  -29.346 1.00 51.80 ? 109 ILE   B N   1 
ATOM   1028 C  CA  . ILE   B 2 100 ? -15.599 -1.554  -29.851 1.00 52.34 ? 109 ILE   B CA  1 
ATOM   1029 C  C   . ILE   B 2 100 ? -15.435 -3.030  -29.569 1.00 52.59 ? 109 ILE   B C   1 
ATOM   1030 O  O   . ILE   B 2 100 ? -15.186 -3.397  -28.429 1.00 53.08 ? 109 ILE   B O   1 
ATOM   1031 C  CB  . ILE   B 2 100 ? -14.445 -0.769  -29.204 1.00 53.12 ? 109 ILE   B CB  1 
ATOM   1032 C  CG1 . ILE   B 2 100 ? -14.692 0.747   -29.260 1.00 54.50 ? 109 ILE   B CG1 1 
ATOM   1033 C  CG2 . ILE   B 2 100 ? -13.119 -1.164  -29.844 1.00 53.57 ? 109 ILE   B CG2 1 
ATOM   1034 C  CD1 . ILE   B 2 100 ? -14.627 1.316   -30.679 1.00 55.76 ? 109 ILE   B CD1 1 
ATOM   1035 N  N   . GLN   B 2 101 ? -15.558 -3.875  -30.585 1.00 52.48 ? 110 GLN   B N   1 
ATOM   1036 C  CA  . GLN   B 2 101 ? -15.441 -5.317  -30.397 1.00 52.80 ? 110 GLN   B CA  1 
ATOM   1037 C  C   . GLN   B 2 101 ? -13.999 -5.799  -30.179 1.00 53.18 ? 110 GLN   B C   1 
ATOM   1038 O  O   . GLN   B 2 101 ? -13.113 -5.467  -30.953 1.00 53.94 ? 110 GLN   B O   1 
ATOM   1039 C  CB  . GLN   B 2 101 ? -16.097 -6.059  -31.561 1.00 53.81 ? 110 GLN   B CB  1 
ATOM   1040 C  CG  . GLN   B 2 101 ? -16.159 -7.548  -31.339 1.00 55.62 ? 110 GLN   B CG  1 
ATOM   1041 C  CD  . GLN   B 2 101 ? -17.034 -8.207  -32.357 1.00 58.25 ? 110 GLN   B CD  1 
ATOM   1042 O  OE1 . GLN   B 2 101 ? -18.074 -7.671  -32.773 1.00 58.44 ? 110 GLN   B OE1 1 
ATOM   1043 N  NE2 . GLN   B 2 101 ? -16.621 -9.395  -32.769 1.00 59.07 ? 110 GLN   B NE2 1 
ATOM   1044 N  N   . THR   B 2 102 ? -13.768 -6.597  -29.137 1.00 52.48 ? 111 THR   B N   1 
ATOM   1045 C  CA  . THR   B 2 102 ? -12.445 -7.126  -28.848 1.00 52.46 ? 111 THR   B CA  1 
ATOM   1046 C  C   . THR   B 2 102 ? -12.562 -8.541  -28.272 1.00 52.12 ? 111 THR   B C   1 
ATOM   1047 O  O   . THR   B 2 102 ? -13.660 -8.965  -27.922 1.00 51.94 ? 111 THR   B O   1 
ATOM   1048 C  CB  . THR   B 2 102 ? -11.738 -6.182  -27.849 1.00 54.50 ? 111 THR   B CB  1 
ATOM   1049 O  OG1 . THR   B 2 102 ? -10.344 -6.506  -27.777 1.00 55.82 ? 111 THR   B OG1 1 
ATOM   1050 C  CG2 . THR   B 2 102 ? -12.360 -6.231  -26.446 1.00 54.80 ? 111 THR   B CG2 1 
ATOM   1051 N  N   . LEU   B 2 103 ? -11.440 -9.287  -28.211 1.00 51.96 ? 112 LEU   B N   1 
ATOM   1052 C  CA  . LEU   B 2 103 ? -11.393 -10.582 -27.531 1.00 52.21 ? 112 LEU   B CA  1 
ATOM   1053 C  C   . LEU   B 2 103 ? -10.564 -10.348 -26.272 1.00 52.45 ? 112 LEU   B C   1 
ATOM   1054 O  O   . LEU   B 2 103 ? -9.396  -9.952  -26.359 1.00 52.64 ? 112 LEU   B O   1 
ATOM   1055 C  CB  . LEU   B 2 103 ? -10.758 -11.719 -28.331 1.00 52.12 ? 112 LEU   B CB  1 
ATOM   1056 C  CG  . LEU   B 2 103 ? -10.745 -13.036 -27.531 1.00 53.71 ? 112 LEU   B CG  1 
ATOM   1057 C  CD1 . LEU   B 2 103 ? -12.036 -13.792 -27.682 1.00 54.59 ? 112 LEU   B CD1 1 
ATOM   1058 C  CD2 . LEU   B 2 103 ? -9.521  -13.873 -27.806 1.00 53.95 ? 112 LEU   B CD2 1 
ATOM   1059 N  N   . PRO   B 2 104 ? -11.137 -10.626 -25.098 1.00 52.00 ? 113 PRO   B N   1 
ATOM   1060 C  CA  . PRO   B 2 104 ? -10.411 -10.363 -23.860 1.00 51.77 ? 113 PRO   B CA  1 
ATOM   1061 C  C   . PRO   B 2 104 ? -9.266  -11.310 -23.556 1.00 52.09 ? 113 PRO   B C   1 
ATOM   1062 O  O   . PRO   B 2 104 ? -9.235  -12.456 -23.995 1.00 52.29 ? 113 PRO   B O   1 
ATOM   1063 C  CB  . PRO   B 2 104 ? -11.492 -10.466 -22.783 1.00 52.04 ? 113 PRO   B CB  1 
ATOM   1064 C  CG  . PRO   B 2 104 ? -12.774 -10.433 -23.500 1.00 52.69 ? 113 PRO   B CG  1 
ATOM   1065 C  CD  . PRO   B 2 104 ? -12.515 -11.057 -24.824 1.00 51.35 ? 113 PRO   B CD  1 
ATOM   1066 N  N   . GLY   B 2 105 ? -8.333  -10.782 -22.785 1.00 51.90 ? 114 GLY   B N   1 
ATOM   1067 C  CA  . GLY   B 2 105 ? -7.209  -11.507 -22.221 1.00 52.27 ? 114 GLY   B CA  1 
ATOM   1068 C  C   . GLY   B 2 105 ? -7.520  -11.874 -20.781 1.00 52.41 ? 114 GLY   B C   1 
ATOM   1069 O  O   . GLY   B 2 105 ? -8.673  -11.781 -20.341 1.00 52.58 ? 114 GLY   B O   1 
ATOM   1070 N  N   . ILE   B 2 106 ? -6.506  -12.296 -20.024 1.00 52.12 ? 115 ILE   B N   1 
ATOM   1071 C  CA  . ILE   B 2 106 ? -6.705  -12.721 -18.645 1.00 51.81 ? 115 ILE   B CA  1 
ATOM   1072 C  C   . ILE   B 2 106 ? -5.805  -12.010 -17.649 1.00 52.41 ? 115 ILE   B C   1 
ATOM   1073 O  O   . ILE   B 2 106 ? -4.594  -11.979 -17.816 1.00 52.91 ? 115 ILE   B O   1 
ATOM   1074 C  CB  . ILE   B 2 106 ? -6.462  -14.251 -18.537 1.00 52.16 ? 115 ILE   B CB  1 
ATOM   1075 C  CG1 . ILE   B 2 106 ? -7.348  -15.068 -19.472 1.00 53.09 ? 115 ILE   B CG1 1 
ATOM   1076 C  CG2 . ILE   B 2 106 ? -6.590  -14.742 -17.111 1.00 52.93 ? 115 ILE   B CG2 1 
ATOM   1077 C  CD1 . ILE   B 2 106 ? -8.760  -14.935 -19.223 1.00 54.31 ? 115 ILE   B CD1 1 
ATOM   1078 N  N   . PHE   B 2 107 ? -6.386  -11.522 -16.561 1.00 52.51 ? 116 PHE   B N   1 
ATOM   1079 C  CA  . PHE   B 2 107 ? -5.659  -11.032 -15.406 1.00 52.95 ? 116 PHE   B CA  1 
ATOM   1080 C  C   . PHE   B 2 107 ? -5.600  -12.295 -14.540 1.00 53.63 ? 116 PHE   B C   1 
ATOM   1081 O  O   . PHE   B 2 107 ? -6.650  -12.798 -14.153 1.00 53.49 ? 116 PHE   B O   1 
ATOM   1082 C  CB  . PHE   B 2 107 ? -6.496  -9.986  -14.644 1.00 52.67 ? 116 PHE   B CB  1 
ATOM   1083 C  CG  . PHE   B 2 107 ? -6.298  -8.533  -15.009 1.00 52.72 ? 116 PHE   B CG  1 
ATOM   1084 C  CD1 . PHE   B 2 107 ? -5.580  -8.175  -16.136 1.00 53.41 ? 116 PHE   B CD1 1 
ATOM   1085 C  CD2 . PHE   B 2 107 ? -6.825  -7.528  -14.219 1.00 53.11 ? 116 PHE   B CD2 1 
ATOM   1086 C  CE1 . PHE   B 2 107 ? -5.416  -6.840  -16.480 1.00 53.97 ? 116 PHE   B CE1 1 
ATOM   1087 C  CE2 . PHE   B 2 107 ? -6.629  -6.195  -14.545 1.00 54.04 ? 116 PHE   B CE2 1 
ATOM   1088 C  CZ  . PHE   B 2 107 ? -5.939  -5.859  -15.682 1.00 53.95 ? 116 PHE   B CZ  1 
ATOM   1089 N  N   . LYS   B 2 108 ? -4.412  -12.850 -14.294 1.00 54.45 ? 117 LYS   B N   1 
ATOM   1090 C  CA  . LYS   B 2 108 ? -4.271  -14.039 -13.461 1.00 55.74 ? 117 LYS   B CA  1 
ATOM   1091 C  C   . LYS   B 2 108 ? -3.905  -13.610 -12.039 1.00 56.05 ? 117 LYS   B C   1 
ATOM   1092 O  O   . LYS   B 2 108 ? -2.810  -13.093 -11.816 1.00 56.04 ? 117 LYS   B O   1 
ATOM   1093 C  CB  . LYS   B 2 108 ? -3.199  -14.990 -14.028 1.00 58.78 ? 117 LYS   B CB  1 
ATOM   1094 C  CG  . LYS   B 2 108 ? -3.648  -15.815 -15.240 1.00 64.65 ? 117 LYS   B CG  1 
ATOM   1095 C  CD  . LYS   B 2 108 ? -2.823  -17.119 -15.396 1.00 71.60 ? 117 LYS   B CD  1 
ATOM   1096 C  CE  . LYS   B 2 108 ? -3.312  -17.999 -16.539 1.00 77.34 ? 117 LYS   B CE  1 
ATOM   1097 N  NZ  . LYS   B 2 108 ? -2.206  -18.506 -17.419 1.00 80.02 ? 117 LYS   B NZ  1 
ATOM   1098 N  N   . THR   B 2 109 ? -4.828  -13.794 -11.080 1.00 56.11 ? 118 THR   B N   1 
ATOM   1099 C  CA  . THR   B 2 109 ? -4.603  -13.421 -9.674  1.00 56.52 ? 118 THR   B CA  1 
ATOM   1100 C  C   . THR   B 2 109 ? -4.622  -14.645 -8.737  1.00 56.88 ? 118 THR   B C   1 
ATOM   1101 O  O   . THR   B 2 109 ? -5.072  -15.717 -9.143  1.00 56.80 ? 118 THR   B O   1 
ATOM   1102 C  CB  . THR   B 2 109 ? -5.620  -12.331 -9.208  1.00 57.48 ? 118 THR   B CB  1 
ATOM   1103 O  OG1 . THR   B 2 109 ? -6.905  -12.910 -8.961  1.00 58.31 ? 118 THR   B OG1 1 
ATOM   1104 C  CG2 . THR   B 2 109 ? -5.736  -11.187 -10.173 1.00 57.69 ? 118 THR   B CG2 1 
ATOM   1105 N  N   . LYS   B 2 110 ? -4.166  -14.473 -7.473  1.00 57.26 ? 119 LYS   B N   1 
ATOM   1106 C  CA  . LYS   B 2 110 ? -4.159  -15.536 -6.455  1.00 57.94 ? 119 LYS   B CA  1 
ATOM   1107 C  C   . LYS   B 2 110 ? -5.581  -16.012 -6.083  1.00 58.39 ? 119 LYS   B C   1 
ATOM   1108 O  O   . LYS   B 2 110 ? -5.755  -17.164 -5.664  1.00 58.57 ? 119 LYS   B O   1 
ATOM   1109 C  CB  . LYS   B 2 110 ? -3.383  -15.100 -5.195  1.00 59.01 ? 119 LYS   B CB  1 
ATOM   1110 C  CG  . LYS   B 2 110 ? -4.057  -13.995 -4.385  1.00 62.11 ? 119 LYS   B CG  1 
ATOM   1111 C  CD  . LYS   B 2 110 ? -3.180  -13.551 -3.227  1.00 65.76 ? 119 LYS   B CD  1 
ATOM   1112 C  CE  . LYS   B 2 110 ? -3.933  -12.771 -2.183  1.00 69.50 ? 119 LYS   B CE  1 
ATOM   1113 N  NZ  . LYS   B 2 110 ? -4.250  -11.399 -2.643  1.00 72.11 ? 119 LYS   B NZ  1 
ATOM   1114 N  N   . ASP   B 2 111 ? -6.591  -15.134 -6.255  1.00 57.98 ? 120 ASP   B N   1 
ATOM   1115 C  CA  . ASP   B 2 111 ? -7.983  -15.470 -5.972  1.00 58.07 ? 120 ASP   B CA  1 
ATOM   1116 C  C   . ASP   B 2 111 ? -8.761  -15.980 -7.181  1.00 57.84 ? 120 ASP   B C   1 
ATOM   1117 O  O   . ASP   B 2 111 ? -9.913  -16.369 -7.019  1.00 58.58 ? 120 ASP   B O   1 
ATOM   1118 C  CB  . ASP   B 2 111 ? -8.723  -14.272 -5.380  1.00 60.09 ? 120 ASP   B CB  1 
ATOM   1119 C  CG  . ASP   B 2 111 ? -8.226  -13.850 -4.022  1.00 65.06 ? 120 ASP   B CG  1 
ATOM   1120 O  OD1 . ASP   B 2 111 ? -7.615  -14.695 -3.324  1.00 65.38 ? 120 ASP   B OD1 1 
ATOM   1121 O  OD2 . ASP   B 2 111 ? -8.447  -12.675 -3.652  1.00 67.89 ? 120 ASP   B OD2 1 
ATOM   1122 N  N   . GLY   B 2 112 ? -8.161  -15.956 -8.367  1.00 56.62 ? 121 GLY   B N   1 
ATOM   1123 C  CA  . GLY   B 2 112 ? -8.807  -16.431 -9.579  1.00 55.96 ? 121 GLY   B CA  1 
ATOM   1124 C  C   . GLY   B 2 112 ? -8.453  -15.628 -10.811 1.00 54.89 ? 121 GLY   B C   1 
ATOM   1125 O  O   . GLY   B 2 112 ? -7.770  -14.608 -10.717 1.00 54.92 ? 121 GLY   B O   1 
ATOM   1126 N  N   . ASP   B 2 113 ? -8.903  -16.093 -11.979 1.00 53.73 ? 122 ASP   B N   1 
ATOM   1127 C  CA  . ASP   B 2 113 ? -8.661  -15.380 -13.226 1.00 53.31 ? 122 ASP   B CA  1 
ATOM   1128 C  C   . ASP   B 2 113 ? -9.856  -14.481 -13.575 1.00 52.66 ? 122 ASP   B C   1 
ATOM   1129 O  O   . ASP   B 2 113 ? -10.997 -14.780 -13.209 1.00 52.52 ? 122 ASP   B O   1 
ATOM   1130 C  CB  . ASP   B 2 113 ? -8.360  -16.356 -14.372 1.00 55.10 ? 122 ASP   B CB  1 
ATOM   1131 C  CG  . ASP   B 2 113 ? -7.040  -17.100 -14.252 1.00 60.53 ? 122 ASP   B CG  1 
ATOM   1132 O  OD1 . ASP   B 2 113 ? -6.326  -16.896 -13.238 1.00 60.46 ? 122 ASP   B OD1 1 
ATOM   1133 O  OD2 . ASP   B 2 113 ? -6.716  -17.882 -15.176 1.00 63.99 ? 122 ASP   B OD2 1 
ATOM   1134 N  N   . ILE   B 2 114 ? -9.582  -13.351 -14.249 1.00 51.86 ? 123 ILE   B N   1 
ATOM   1135 C  CA  . ILE   B 2 114 ? -10.600 -12.372 -14.635 1.00 51.33 ? 123 ILE   B CA  1 
ATOM   1136 C  C   . ILE   B 2 114 ? -10.334 -11.972 -16.072 1.00 50.88 ? 123 ILE   B C   1 
ATOM   1137 O  O   . ILE   B 2 114 ? -9.178  -11.831 -16.464 1.00 50.40 ? 123 ILE   B O   1 
ATOM   1138 C  CB  . ILE   B 2 114 ? -10.569 -11.075 -13.756 1.00 51.64 ? 123 ILE   B CB  1 
ATOM   1139 C  CG1 . ILE   B 2 114 ? -10.221 -11.332 -12.287 1.00 52.94 ? 123 ILE   B CG1 1 
ATOM   1140 C  CG2 . ILE   B 2 114 ? -11.864 -10.291 -13.867 1.00 51.93 ? 123 ILE   B CG2 1 
ATOM   1141 C  CD1 . ILE   B 2 114 ? -9.919  -10.028 -11.491 1.00 54.32 ? 123 ILE   B CD1 1 
ATOM   1142 N  N   . GLY   B 2 115 ? -11.394 -11.696 -16.822 1.00 50.55 ? 124 GLY   B N   1 
ATOM   1143 C  CA  . GLY   B 2 115 ? -11.255 -11.207 -18.188 1.00 50.74 ? 124 GLY   B CA  1 
ATOM   1144 C  C   . GLY   B 2 115 ? -10.617 -9.831  -18.203 1.00 50.63 ? 124 GLY   B C   1 
ATOM   1145 O  O   . GLY   B 2 115 ? -10.639 -9.116  -17.186 1.00 50.52 ? 124 GLY   B O   1 
ATOM   1146 N  N   . ALA   B 2 116 ? -10.009 -9.459  -19.340 1.00 50.31 ? 125 ALA   B N   1 
ATOM   1147 C  CA  . ALA   B 2 116 ? -9.360  -8.150  -19.435 1.00 50.23 ? 125 ALA   B CA  1 
ATOM   1148 C  C   . ALA   B 2 116 ? -9.387  -7.555  -20.832 1.00 49.93 ? 125 ALA   B C   1 
ATOM   1149 O  O   . ALA   B 2 116 ? -8.977  -8.186  -21.789 1.00 49.58 ? 125 ALA   B O   1 
ATOM   1150 C  CB  . ALA   B 2 116 ? -7.940  -8.205  -18.890 1.00 50.09 ? 125 ALA   B CB  1 
ATOM   1151 N  N   . VAL   B 2 117 ? -9.881  -6.325  -20.936 1.00 50.00 ? 126 VAL   B N   1 
ATOM   1152 C  CA  A VAL   B 2 117 ? -9.954  -5.639  -22.217 0.50 50.33 ? 126 VAL   B CA  1 
ATOM   1153 C  CA  B VAL   B 2 117 ? -9.999  -5.589  -22.184 0.50 50.24 ? 126 VAL   B CA  1 
ATOM   1154 C  C   . VAL   B 2 117 ? -8.754  -4.699  -22.406 1.00 50.82 ? 126 VAL   B C   1 
ATOM   1155 O  O   . VAL   B 2 117 ? -8.477  -3.822  -21.581 1.00 50.73 ? 126 VAL   B O   1 
ATOM   1156 C  CB  A VAL   B 2 117 ? -11.319 -4.966  -22.480 0.50 50.81 ? 126 VAL   B CB  1 
ATOM   1157 C  CB  B VAL   B 2 117 ? -11.356 -4.830  -22.156 0.50 50.52 ? 126 VAL   B CB  1 
ATOM   1158 C  CG1 A VAL   B 2 117 ? -12.394 -6.020  -22.705 0.50 51.16 ? 126 VAL   B CG1 1 
ATOM   1159 C  CG1 B VAL   B 2 117 ? -11.319 -3.500  -22.898 0.50 50.95 ? 126 VAL   B CG1 1 
ATOM   1160 C  CG2 A VAL   B 2 117 ? -11.711 -4.033  -21.347 0.50 51.39 ? 126 VAL   B CG2 1 
ATOM   1161 C  CG2 B VAL   B 2 117 ? -12.480 -5.719  -22.668 0.50 50.84 ? 126 VAL   B CG2 1 
ATOM   1162 N  N   . ALA   B 2 118 ? -7.981  -4.940  -23.493 1.00 51.12 ? 127 ALA   B N   1 
ATOM   1163 C  CA  . ALA   B 2 118 ? -6.777  -4.151  -23.768 1.00 51.92 ? 127 ALA   B CA  1 
ATOM   1164 C  C   . ALA   B 2 118 ? -7.032  -2.953  -24.687 1.00 53.07 ? 127 ALA   B C   1 
ATOM   1165 O  O   . ALA   B 2 118 ? -6.314  -2.732  -25.660 1.00 54.04 ? 127 ALA   B O   1 
ATOM   1166 C  CB  . ALA   B 2 118 ? -5.674  -5.038  -24.319 1.00 51.90 ? 127 ALA   B CB  1 
ATOM   1167 N  N   . LEU   B 2 119 ? -8.058  -2.173  -24.373 1.00 52.89 ? 128 LEU   B N   1 
ATOM   1168 C  CA  . LEU   B 2 119 ? -8.387  -0.982  -25.140 1.00 53.07 ? 128 LEU   B CA  1 
ATOM   1169 C  C   . LEU   B 2 119 ? -7.984  0.239   -24.319 1.00 53.83 ? 128 LEU   B C   1 
ATOM   1170 O  O   . LEU   B 2 119 ? -8.169  0.247   -23.105 1.00 53.87 ? 128 LEU   B O   1 
ATOM   1171 C  CB  . LEU   B 2 119 ? -9.890  -0.973  -25.477 1.00 52.72 ? 128 LEU   B CB  1 
ATOM   1172 C  CG  . LEU   B 2 119 ? -10.345 -2.184  -26.296 1.00 53.49 ? 128 LEU   B CG  1 
ATOM   1173 C  CD1 . LEU   B 2 119 ? -11.848 -2.319  -26.330 1.00 53.31 ? 128 LEU   B CD1 1 
ATOM   1174 C  CD2 . LEU   B 2 119 ? -9.758  -2.161  -27.681 1.00 54.25 ? 128 LEU   B CD2 1 
ATOM   1175 N  N   . ASP   B 2 120 ? -7.388  1.250   -24.960 1.00 54.55 ? 129 ASP   B N   1 
ATOM   1176 C  CA  . ASP   B 2 120 ? -6.987  2.461   -24.245 1.00 55.30 ? 129 ASP   B CA  1 
ATOM   1177 C  C   . ASP   B 2 120 ? -7.898  3.654   -24.565 1.00 54.66 ? 129 ASP   B C   1 
ATOM   1178 O  O   . ASP   B 2 120 ? -8.056  4.049   -25.716 1.00 55.11 ? 129 ASP   B O   1 
ATOM   1179 C  CB  . ASP   B 2 120 ? -5.499  2.799   -24.443 1.00 58.10 ? 129 ASP   B CB  1 
ATOM   1180 C  CG  . ASP   B 2 120 ? -4.972  3.779   -23.406 1.00 65.52 ? 129 ASP   B CG  1 
ATOM   1181 O  OD1 . ASP   B 2 120 ? -5.326  4.982   -23.482 1.00 67.55 ? 129 ASP   B OD1 1 
ATOM   1182 O  OD2 . ASP   B 2 120 ? -4.220  3.349   -22.517 1.00 68.56 ? 129 ASP   B OD2 1 
ATOM   1183 N  N   . TYR   B 2 121 ? -8.490  4.210   -23.522 1.00 53.58 ? 130 TYR   B N   1 
ATOM   1184 C  CA  . TYR   B 2 121 ? -9.401  5.344   -23.559 1.00 53.01 ? 130 TYR   B CA  1 
ATOM   1185 C  C   . TYR   B 2 121 ? -9.082  6.267   -22.382 1.00 51.68 ? 130 TYR   B C   1 
ATOM   1186 O  O   . TYR   B 2 121 ? -8.448  5.830   -21.416 1.00 51.81 ? 130 TYR   B O   1 
ATOM   1187 C  CB  . TYR   B 2 121 ? -10.866 4.842   -23.495 1.00 53.57 ? 130 TYR   B CB  1 
ATOM   1188 C  CG  . TYR   B 2 121 ? -11.318 4.278   -24.821 1.00 55.13 ? 130 TYR   B CG  1 
ATOM   1189 C  CD1 . TYR   B 2 121 ? -11.797 5.108   -25.825 1.00 56.75 ? 130 TYR   B CD1 1 
ATOM   1190 C  CD2 . TYR   B 2 121 ? -11.151 2.933   -25.118 1.00 56.35 ? 130 TYR   B CD2 1 
ATOM   1191 C  CE1 . TYR   B 2 121 ? -12.106 4.610   -27.087 1.00 58.03 ? 130 TYR   B CE1 1 
ATOM   1192 C  CE2 . TYR   B 2 121 ? -11.452 2.426   -26.373 1.00 57.54 ? 130 TYR   B CE2 1 
ATOM   1193 C  CZ  . TYR   B 2 121 ? -11.934 3.265   -27.355 1.00 58.93 ? 130 TYR   B CZ  1 
ATOM   1194 O  OH  . TYR   B 2 121 ? -12.219 2.756   -28.598 1.00 61.25 ? 130 TYR   B OH  1 
ATOM   1195 N  N   . PRO   B 2 122 ? -9.497  7.550   -22.429 1.00 50.26 ? 131 PRO   B N   1 
ATOM   1196 C  CA  . PRO   B 2 122 ? -9.210  8.451   -21.295 1.00 49.04 ? 131 PRO   B CA  1 
ATOM   1197 C  C   . PRO   B 2 122 ? -9.843  7.971   -19.989 1.00 47.63 ? 131 PRO   B C   1 
ATOM   1198 O  O   . PRO   B 2 122 ? -10.837 7.255   -20.030 1.00 48.27 ? 131 PRO   B O   1 
ATOM   1199 C  CB  . PRO   B 2 122 ? -9.805  9.791   -21.740 1.00 50.06 ? 131 PRO   B CB  1 
ATOM   1200 C  CG  . PRO   B 2 122 ? -9.950  9.687   -23.222 1.00 50.86 ? 131 PRO   B CG  1 
ATOM   1201 C  CD  . PRO   B 2 122 ? -10.235 8.246   -23.501 1.00 49.53 ? 131 PRO   B CD  1 
ATOM   1202 N  N   . ALA   B 2 123 ? -9.283  8.354   -18.829 1.00 45.74 ? 132 ALA   B N   1 
ATOM   1203 C  CA  . ALA   B 2 123 ? -9.821  7.911   -17.540 1.00 44.74 ? 132 ALA   B CA  1 
ATOM   1204 C  C   . ALA   B 2 123 ? -11.301 8.300   -17.294 1.00 43.82 ? 132 ALA   B C   1 
ATOM   1205 O  O   . ALA   B 2 123 ? -11.961 7.652   -16.492 1.00 44.25 ? 132 ALA   B O   1 
ATOM   1206 C  CB  . ALA   B 2 123 ? -8.935  8.375   -16.398 1.00 44.60 ? 132 ALA   B CB  1 
ATOM   1207 N  N   . GLY   B 2 124 ? -11.818 9.295   -18.020 1.00 42.79 ? 133 GLY   B N   1 
ATOM   1208 C  CA  . GLY   B 2 124 ? -13.225 9.703   -17.962 1.00 41.52 ? 133 GLY   B CA  1 
ATOM   1209 C  C   . GLY   B 2 124 ? -14.172 8.731   -18.661 1.00 40.24 ? 133 GLY   B C   1 
ATOM   1210 O  O   . GLY   B 2 124 ? -15.383 8.928   -18.633 1.00 39.50 ? 133 GLY   B O   1 
ATOM   1211 N  N   . THR   B 2 125 ? -13.622 7.686   -19.339 1.00 39.99 ? 134 THR   B N   1 
ATOM   1212 C  CA  . THR   B 2 125 ? -14.373 6.587   -19.972 1.00 39.98 ? 134 THR   B CA  1 
ATOM   1213 C  C   . THR   B 2 125 ? -14.740 5.514   -18.921 1.00 39.84 ? 134 THR   B C   1 
ATOM   1214 O  O   . THR   B 2 125 ? -15.547 4.636   -19.219 1.00 40.33 ? 134 THR   B O   1 
ATOM   1215 C  CB  . THR   B 2 125 ? -13.568 5.969   -21.159 1.00 41.10 ? 134 THR   B CB  1 
ATOM   1216 O  OG1 . THR   B 2 125 ? -13.053 7.020   -21.975 1.00 42.56 ? 134 THR   B OG1 1 
ATOM   1217 C  CG2 . THR   B 2 125 ? -14.399 5.041   -22.050 1.00 40.54 ? 134 THR   B CG2 1 
ATOM   1218 N  N   . SER   B 2 126 ? -14.136 5.571   -17.705 1.00 39.32 ? 135 SER   B N   1 
ATOM   1219 C  CA  . SER   B 2 126 ? -14.344 4.638   -16.596 1.00 39.23 ? 135 SER   B CA  1 
ATOM   1220 C  C   . SER   B 2 126 ? -15.808 4.471   -16.254 1.00 38.88 ? 135 SER   B C   1 
ATOM   1221 O  O   . SER   B 2 126 ? -16.475 5.436   -15.924 1.00 38.57 ? 135 SER   B O   1 
ATOM   1222 C  CB  . SER   B 2 126 ? -13.616 5.132   -15.356 1.00 40.59 ? 135 SER   B CB  1 
ATOM   1223 O  OG  . SER   B 2 126 ? -12.209 5.094   -15.519 1.00 43.26 ? 135 SER   B OG  1 
ATOM   1224 N  N   . GLY   B 2 127 ? -16.276 3.237   -16.305 1.00 38.56 ? 136 GLY   B N   1 
ATOM   1225 C  CA  . GLY   B 2 127 ? -17.650 2.871   -16.018 1.00 38.77 ? 136 GLY   B CA  1 
ATOM   1226 C  C   . GLY   B 2 127 ? -18.407 2.392   -17.236 1.00 39.67 ? 136 GLY   B C   1 
ATOM   1227 O  O   . GLY   B 2 127 ? -19.569 2.005   -17.110 1.00 40.42 ? 136 GLY   B O   1 
ATOM   1228 N  N   . SER   B 2 128 ? -17.775 2.435   -18.434 1.00 39.35 ? 137 SER   B N   1 
ATOM   1229 C  CA  . SER   B 2 128 ? -18.392 1.988   -19.682 1.00 39.25 ? 137 SER   B CA  1 
ATOM   1230 C  C   . SER   B 2 128 ? -18.647 0.494   -19.626 1.00 39.39 ? 137 SER   B C   1 
ATOM   1231 O  O   . SER   B 2 128 ? -17.795 -0.261  -19.168 1.00 39.31 ? 137 SER   B O   1 
ATOM   1232 C  CB  . SER   B 2 128 ? -17.505 2.330   -20.873 1.00 40.20 ? 137 SER   B CB  1 
ATOM   1233 O  OG  . SER   B 2 128 ? -17.373 3.734   -21.007 1.00 43.00 ? 137 SER   B OG  1 
ATOM   1234 N  N   . PRO   B 2 129 ? -19.835 0.052   -20.048 1.00 40.07 ? 138 PRO   B N   1 
ATOM   1235 C  CA  . PRO   B 2 129 ? -20.147 -1.376  -19.951 1.00 40.67 ? 138 PRO   B CA  1 
ATOM   1236 C  C   . PRO   B 2 129 ? -19.469 -2.230  -21.001 1.00 41.41 ? 138 PRO   B C   1 
ATOM   1237 O  O   . PRO   B 2 129 ? -19.206 -1.781  -22.108 1.00 41.73 ? 138 PRO   B O   1 
ATOM   1238 C  CB  . PRO   B 2 129 ? -21.668 -1.416  -20.111 1.00 41.43 ? 138 PRO   B CB  1 
ATOM   1239 C  CG  . PRO   B 2 129 ? -22.009 -0.185  -20.919 1.00 41.58 ? 138 PRO   B CG  1 
ATOM   1240 C  CD  . PRO   B 2 129 ? -20.974 0.840   -20.577 1.00 39.79 ? 138 PRO   B CD  1 
ATOM   1241 N  N   . ILE   B 2 130 ? -19.192 -3.474  -20.631 1.00 41.77 ? 139 ILE   B N   1 
ATOM   1242 C  CA  . ILE   B 2 130 ? -18.645 -4.499  -21.497 1.00 42.26 ? 139 ILE   B CA  1 
ATOM   1243 C  C   . ILE   B 2 130 ? -19.821 -5.443  -21.761 1.00 43.20 ? 139 ILE   B C   1 
ATOM   1244 O  O   . ILE   B 2 130 ? -20.559 -5.794  -20.838 1.00 42.52 ? 139 ILE   B O   1 
ATOM   1245 C  CB  . ILE   B 2 130 ? -17.447 -5.175  -20.829 1.00 42.72 ? 139 ILE   B CB  1 
ATOM   1246 C  CG1 . ILE   B 2 130 ? -16.303 -4.160  -20.667 1.00 43.06 ? 139 ILE   B CG1 1 
ATOM   1247 C  CG2 . ILE   B 2 130 ? -17.005 -6.379  -21.645 1.00 43.49 ? 139 ILE   B CG2 1 
ATOM   1248 C  CD1 . ILE   B 2 130 ? -15.543 -4.313  -19.435 1.00 43.58 ? 139 ILE   B CD1 1 
ATOM   1249 N  N   . LEU   B 2 131 ? -20.083 -5.753  -23.046 1.00 44.23 ? 140 LEU   B N   1 
ATOM   1250 C  CA  . LEU   B 2 131 ? -21.279 -6.498  -23.425 1.00 45.29 ? 140 LEU   B CA  1 
ATOM   1251 C  C   . LEU   B 2 131 ? -21.007 -7.850  -24.030 1.00 46.68 ? 140 LEU   B C   1 
ATOM   1252 O  O   . LEU   B 2 131 ? -19.945 -8.082  -24.593 1.00 46.74 ? 140 LEU   B O   1 
ATOM   1253 C  CB  . LEU   B 2 131 ? -22.132 -5.680  -24.422 1.00 45.52 ? 140 LEU   B CB  1 
ATOM   1254 C  CG  . LEU   B 2 131 ? -22.181 -4.182  -24.235 1.00 46.77 ? 140 LEU   B CG  1 
ATOM   1255 C  CD1 . LEU   B 2 131 ? -22.895 -3.520  -25.371 1.00 46.93 ? 140 LEU   B CD1 1 
ATOM   1256 C  CD2 . LEU   B 2 131 ? -22.738 -3.814  -22.856 1.00 47.20 ? 140 LEU   B CD2 1 
ATOM   1257 N  N   . ASP   B 2 132 ? -21.988 -8.744  -23.931 1.00 47.76 ? 141 ASP   B N   1 
ATOM   1258 C  CA  . ASP   B 2 132 ? -21.916 -10.032 -24.590 1.00 49.41 ? 141 ASP   B CA  1 
ATOM   1259 C  C   . ASP   B 2 132 ? -22.841 -10.005 -25.839 1.00 51.79 ? 141 ASP   B C   1 
ATOM   1260 O  O   . ASP   B 2 132 ? -23.517 -8.988  -26.086 1.00 51.57 ? 141 ASP   B O   1 
ATOM   1261 C  CB  . ASP   B 2 132 ? -22.193 -11.193 -23.619 1.00 50.63 ? 141 ASP   B CB  1 
ATOM   1262 C  CG  . ASP   B 2 132 ? -23.597 -11.336 -23.091 1.00 54.62 ? 141 ASP   B CG  1 
ATOM   1263 O  OD1 . ASP   B 2 132 ? -24.519 -10.787 -23.706 1.00 56.15 ? 141 ASP   B OD1 1 
ATOM   1264 O  OD2 . ASP   B 2 132 ? -23.775 -12.022 -22.070 1.00 56.70 ? 141 ASP   B OD2 1 
ATOM   1265 N  N   . LYS   B 2 133 ? -22.865 -11.104 -26.624 1.00 53.42 ? 142 LYS   B N   1 
ATOM   1266 C  CA  . LYS   B 2 133 ? -23.649 -11.218 -27.857 1.00 55.33 ? 142 LYS   B CA  1 
ATOM   1267 C  C   . LYS   B 2 133 ? -25.154 -10.975 -27.665 1.00 56.11 ? 142 LYS   B C   1 
ATOM   1268 O  O   . LYS   B 2 133 ? -25.819 -10.496 -28.590 1.00 56.49 ? 142 LYS   B O   1 
ATOM   1269 C  CB  . LYS   B 2 133 ? -23.376 -12.565 -28.536 1.00 58.68 ? 142 LYS   B CB  1 
ATOM   1270 C  CG  . LYS   B 2 133 ? -21.888 -12.737 -28.854 1.00 65.29 ? 142 LYS   B CG  1 
ATOM   1271 C  CD  . LYS   B 2 133 ? -21.552 -14.090 -29.467 1.00 71.58 ? 142 LYS   B CD  1 
ATOM   1272 C  CE  . LYS   B 2 133 ? -20.108 -14.153 -29.900 1.00 76.24 ? 142 LYS   B CE  1 
ATOM   1273 N  NZ  . LYS   B 2 133 ? -19.761 -15.482 -30.470 1.00 78.85 ? 142 LYS   B NZ  1 
ATOM   1274 N  N   . CYS   B 2 134 ? -25.678 -11.245 -26.454 1.00 55.97 ? 143 CYS   B N   1 
ATOM   1275 C  CA  . CYS   B 2 134 ? -27.088 -10.997 -26.134 1.00 56.10 ? 143 CYS   B CA  1 
ATOM   1276 C  C   . CYS   B 2 134 ? -27.344 -9.559  -25.654 1.00 55.39 ? 143 CYS   B C   1 
ATOM   1277 O  O   . CYS   B 2 134 ? -28.422 -9.290  -25.128 1.00 56.14 ? 143 CYS   B O   1 
ATOM   1278 C  CB  . CYS   B 2 134 ? -27.584 -12.005 -25.102 1.00 57.78 ? 143 CYS   B CB  1 
ATOM   1279 S  SG  . CYS   B 2 134 ? -27.344 -13.738 -25.578 1.00 64.88 ? 143 CYS   B SG  1 
ATOM   1280 N  N   . GLY   B 2 135 ? -26.360 -8.667  -25.795 1.00 53.84 ? 144 GLY   B N   1 
ATOM   1281 C  CA  . GLY   B 2 135 ? -26.434 -7.296  -25.311 1.00 52.92 ? 144 GLY   B CA  1 
ATOM   1282 C  C   . GLY   B 2 135 ? -26.368 -7.184  -23.795 1.00 51.57 ? 144 GLY   B C   1 
ATOM   1283 O  O   . GLY   B 2 135 ? -26.530 -6.085  -23.255 1.00 51.47 ? 144 GLY   B O   1 
ATOM   1284 N  N   . ARG   B 2 136 ? -26.138 -8.316  -23.085 1.00 50.12 ? 145 ARG   B N   1 
ATOM   1285 C  CA  . ARG   B 2 136 ? -26.094 -8.330  -21.624 1.00 49.35 ? 145 ARG   B CA  1 
ATOM   1286 C  C   . ARG   B 2 136 ? -24.799 -7.747  -21.082 1.00 47.85 ? 145 ARG   B C   1 
ATOM   1287 O  O   . ARG   B 2 136 ? -23.733 -8.012  -21.644 1.00 48.34 ? 145 ARG   B O   1 
ATOM   1288 C  CB  . ARG   B 2 136 ? -26.342 -9.744  -21.083 1.00 50.81 ? 145 ARG   B CB  1 
ATOM   1289 C  CG  . ARG   B 2 136 ? -27.775 -10.204 -21.277 1.00 54.49 ? 145 ARG   B CG  1 
ATOM   1290 C  CD  . ARG   B 2 136 ? -27.971 -11.607 -20.763 1.00 59.05 ? 145 ARG   B CD  1 
ATOM   1291 N  NE  . ARG   B 2 136 ? -27.276 -12.565 -21.620 1.00 63.57 ? 145 ARG   B NE  1 
ATOM   1292 C  CZ  . ARG   B 2 136 ? -26.441 -13.502 -21.183 1.00 66.87 ? 145 ARG   B CZ  1 
ATOM   1293 N  NH1 . ARG   B 2 136 ? -26.196 -13.631 -19.882 1.00 67.02 ? 145 ARG   B NH1 1 
ATOM   1294 N  NH2 . ARG   B 2 136 ? -25.838 -14.314 -22.043 1.00 66.87 ? 145 ARG   B NH2 1 
ATOM   1295 N  N   . VAL   B 2 137 ? -24.887 -6.915  -20.023 1.00 45.76 ? 146 VAL   B N   1 
ATOM   1296 C  CA  . VAL   B 2 137 ? -23.694 -6.311  -19.430 1.00 44.34 ? 146 VAL   B CA  1 
ATOM   1297 C  C   . VAL   B 2 137 ? -22.968 -7.354  -18.578 1.00 43.58 ? 146 VAL   B C   1 
ATOM   1298 O  O   . VAL   B 2 137 ? -23.526 -7.866  -17.609 1.00 43.93 ? 146 VAL   B O   1 
ATOM   1299 C  CB  . VAL   B 2 137 ? -23.982 -5.020  -18.632 1.00 44.02 ? 146 VAL   B CB  1 
ATOM   1300 C  CG1 . VAL   B 2 137 ? -22.690 -4.322  -18.250 1.00 44.26 ? 146 VAL   B CG1 1 
ATOM   1301 C  CG2 . VAL   B 2 137 ? -24.871 -4.078  -19.425 1.00 44.13 ? 146 VAL   B CG2 1 
ATOM   1302 N  N   . ILE   B 2 138 ? -21.734 -7.678  -18.964 1.00 42.04 ? 147 ILE   B N   1 
ATOM   1303 C  CA  . ILE   B 2 138 ? -20.915 -8.662  -18.278 1.00 41.18 ? 147 ILE   B CA  1 
ATOM   1304 C  C   . ILE   B 2 138 ? -19.839 -8.031  -17.354 1.00 40.68 ? 147 ILE   B C   1 
ATOM   1305 O  O   . ILE   B 2 138 ? -19.173 -8.762  -16.623 1.00 41.17 ? 147 ILE   B O   1 
ATOM   1306 C  CB  . ILE   B 2 138 ? -20.312 -9.657  -19.308 1.00 41.21 ? 147 ILE   B CB  1 
ATOM   1307 C  CG1 . ILE   B 2 138 ? -19.501 -8.932  -20.396 1.00 41.44 ? 147 ILE   B CG1 1 
ATOM   1308 C  CG2 . ILE   B 2 138 ? -21.411 -10.501 -19.946 1.00 41.55 ? 147 ILE   B CG2 1 
ATOM   1309 C  CD1 . ILE   B 2 138 ? -18.631 -9.849  -21.156 1.00 42.20 ? 147 ILE   B CD1 1 
ATOM   1310 N  N   . GLY   B 2 139 ? -19.710 -6.703  -17.359 1.00 39.26 ? 148 GLY   B N   1 
ATOM   1311 C  CA  . GLY   B 2 139 ? -18.742 -6.010  -16.520 1.00 38.59 ? 148 GLY   B CA  1 
ATOM   1312 C  C   . GLY   B 2 139 ? -18.599 -4.534  -16.836 1.00 37.67 ? 148 GLY   B C   1 
ATOM   1313 O  O   . GLY   B 2 139 ? -19.225 -4.052  -17.775 1.00 37.80 ? 148 GLY   B O   1 
ATOM   1314 N  N   . LEU   B 2 140 ? -17.767 -3.805  -16.064 1.00 36.71 ? 149 LEU   B N   1 
ATOM   1315 C  CA  . LEU   B 2 140 ? -17.504 -2.371  -16.266 1.00 36.45 ? 149 LEU   B CA  1 
ATOM   1316 C  C   . LEU   B 2 140 ? -16.009 -2.133  -16.500 1.00 37.05 ? 149 LEU   B C   1 
ATOM   1317 O  O   . LEU   B 2 140 ? -15.173 -2.808  -15.896 1.00 37.30 ? 149 LEU   B O   1 
ATOM   1318 C  CB  . LEU   B 2 140 ? -18.007 -1.501  -15.094 1.00 35.67 ? 149 LEU   B CB  1 
ATOM   1319 C  CG  . LEU   B 2 140 ? -19.517 -1.446  -14.860 1.00 35.91 ? 149 LEU   B CG  1 
ATOM   1320 C  CD1 . LEU   B 2 140 ? -19.862 -0.429  -13.807 1.00 34.54 ? 149 LEU   B CD1 1 
ATOM   1321 C  CD2 . LEU   B 2 140 ? -20.271 -1.099  -16.134 1.00 36.80 ? 149 LEU   B CD2 1 
ATOM   1322 N  N   . TYR   B 2 141 ? -15.686 -1.204  -17.412 1.00 37.13 ? 150 TYR   B N   1 
ATOM   1323 C  CA  . TYR   B 2 141 ? -14.326 -0.865  -17.841 1.00 37.87 ? 150 TYR   B CA  1 
ATOM   1324 C  C   . TYR   B 2 141 ? -13.817 0.299   -17.009 1.00 38.07 ? 150 TYR   B C   1 
ATOM   1325 O  O   . TYR   B 2 141 ? -14.551 1.260   -16.836 1.00 37.84 ? 150 TYR   B O   1 
ATOM   1326 C  CB  . TYR   B 2 141 ? -14.361 -0.468  -19.355 1.00 38.23 ? 150 TYR   B CB  1 
ATOM   1327 C  CG  . TYR   B 2 141 ? -13.111 0.206   -19.901 1.00 39.29 ? 150 TYR   B CG  1 
ATOM   1328 C  CD1 . TYR   B 2 141 ? -13.001 1.590   -19.937 1.00 40.29 ? 150 TYR   B CD1 1 
ATOM   1329 C  CD2 . TYR   B 2 141 ? -12.058 -0.542  -20.413 1.00 40.26 ? 150 TYR   B CD2 1 
ATOM   1330 C  CE1 . TYR   B 2 141 ? -11.849 2.212   -20.409 1.00 41.30 ? 150 TYR   B CE1 1 
ATOM   1331 C  CE2 . TYR   B 2 141 ? -10.913 0.069   -20.920 1.00 41.00 ? 150 TYR   B CE2 1 
ATOM   1332 C  CZ  . TYR   B 2 141 ? -10.806 1.448   -20.908 1.00 41.97 ? 150 TYR   B CZ  1 
ATOM   1333 O  OH  . TYR   B 2 141 ? -9.669  2.068   -21.385 1.00 42.87 ? 150 TYR   B OH  1 
ATOM   1334 N  N   . GLY   B 2 142 ? -12.567 0.254   -16.557 1.00 38.21 ? 151 GLY   B N   1 
ATOM   1335 C  CA  . GLY   B 2 142 ? -12.017 1.373   -15.798 1.00 38.73 ? 151 GLY   B CA  1 
ATOM   1336 C  C   . GLY   B 2 142 ? -11.062 1.029   -14.689 1.00 39.17 ? 151 GLY   B C   1 
ATOM   1337 O  O   . GLY   B 2 142 ? -10.456 1.937   -14.109 1.00 39.73 ? 151 GLY   B O   1 
ATOM   1338 N  N   . ASN   B 2 143 ? -10.924 -0.270  -14.365 1.00 39.00 ? 152 ASN   B N   1 
ATOM   1339 C  CA  . ASN   B 2 143 ? -9.997  -0.668  -13.311 1.00 39.78 ? 152 ASN   B CA  1 
ATOM   1340 C  C   . ASN   B 2 143 ? -9.055  -1.748  -13.800 1.00 40.23 ? 152 ASN   B C   1 
ATOM   1341 O  O   . ASN   B 2 143 ? -9.464  -2.882  -14.001 1.00 40.17 ? 152 ASN   B O   1 
ATOM   1342 C  CB  . ASN   B 2 143 ? -10.730 -1.089  -12.043 1.00 41.28 ? 152 ASN   B CB  1 
ATOM   1343 C  CG  . ASN   B 2 143 ? -9.827  -1.205  -10.842 1.00 44.73 ? 152 ASN   B CG  1 
ATOM   1344 O  OD1 . ASN   B 2 143 ? -8.745  -0.608  -10.790 1.00 46.23 ? 152 ASN   B OD1 1 
ATOM   1345 N  ND2 . ASN   B 2 143 ? -10.237 -1.990  -9.852  1.00 44.77 ? 152 ASN   B ND2 1 
ATOM   1346 N  N   . GLY   B 2 144 ? -7.803  -1.384  -13.997 1.00 40.57 ? 153 GLY   B N   1 
ATOM   1347 C  CA  . GLY   B 2 144 ? -6.814  -2.328  -14.470 1.00 42.01 ? 153 GLY   B CA  1 
ATOM   1348 C  C   . GLY   B 2 144 ? -5.391  -1.919  -14.213 1.00 43.86 ? 153 GLY   B C   1 
ATOM   1349 O  O   . GLY   B 2 144 ? -5.059  -1.440  -13.124 1.00 43.81 ? 153 GLY   B O   1 
ATOM   1350 N  N   . VAL   B 2 145 ? -4.535  -2.104  -15.233 1.00 45.28 ? 154 VAL   B N   1 
ATOM   1351 C  CA  . VAL   B 2 145 ? -3.114  -1.871  -15.079 1.00 46.99 ? 154 VAL   B CA  1 
ATOM   1352 C  C   . VAL   B 2 145 ? -2.443  -1.158  -16.278 1.00 48.65 ? 154 VAL   B C   1 
ATOM   1353 O  O   . VAL   B 2 145 ? -2.938  -1.199  -17.403 1.00 48.70 ? 154 VAL   B O   1 
ATOM   1354 C  CB  . VAL   B 2 145 ? -2.480  -3.245  -14.757 1.00 48.05 ? 154 VAL   B CB  1 
ATOM   1355 C  CG1 . VAL   B 2 145 ? -1.948  -3.957  -16.004 1.00 48.50 ? 154 VAL   B CG1 1 
ATOM   1356 C  CG2 . VAL   B 2 145 ? -1.427  -3.128  -13.667 1.00 49.04 ? 154 VAL   B CG2 1 
ATOM   1357 N  N   . VAL   B 2 146 ? -1.319  -0.494  -16.021 1.00 49.68 ? 155 VAL   B N   1 
ATOM   1358 C  CA  . VAL   B 2 146 ? -0.566  0.180   -17.070 1.00 51.24 ? 155 VAL   B CA  1 
ATOM   1359 C  C   . VAL   B 2 146 ? 0.554   -0.764  -17.502 1.00 53.43 ? 155 VAL   B C   1 
ATOM   1360 O  O   . VAL   B 2 146 ? 1.349   -1.193  -16.666 1.00 53.50 ? 155 VAL   B O   1 
ATOM   1361 C  CB  . VAL   B 2 146 ? -0.026  1.539   -16.581 1.00 51.65 ? 155 VAL   B CB  1 
ATOM   1362 C  CG1 . VAL   B 2 146 ? 0.933   2.141   -17.592 1.00 51.82 ? 155 VAL   B CG1 1 
ATOM   1363 C  CG2 . VAL   B 2 146 ? -1.169  2.499   -16.275 1.00 52.12 ? 155 VAL   B CG2 1 
ATOM   1364 N  N   . ILE   B 2 147 ? 0.587   -1.140  -18.792 1.00 55.07 ? 156 ILE   B N   1 
ATOM   1365 C  CA  . ILE   B 2 147 ? 1.587   -2.088  -19.284 1.00 57.13 ? 156 ILE   B CA  1 
ATOM   1366 C  C   . ILE   B 2 147 ? 2.900   -1.398  -19.760 1.00 59.08 ? 156 ILE   B C   1 
ATOM   1367 O  O   . ILE   B 2 147 ? 2.980   -0.168  -19.750 1.00 59.11 ? 156 ILE   B O   1 
ATOM   1368 C  CB  . ILE   B 2 147 ? 0.951   -3.011  -20.352 1.00 57.75 ? 156 ILE   B CB  1 
ATOM   1369 C  CG1 . ILE   B 2 147 ? 0.255   -2.200  -21.470 1.00 58.86 ? 156 ILE   B CG1 1 
ATOM   1370 C  CG2 . ILE   B 2 147 ? -0.006  -3.996  -19.679 1.00 58.16 ? 156 ILE   B CG2 1 
ATOM   1371 C  CD1 . ILE   B 2 147 ? -0.246  -3.046  -22.616 1.00 59.92 ? 156 ILE   B CD1 1 
ATOM   1372 N  N   . LYS   B 2 148 ? 3.941   -2.200  -20.122 1.00 60.42 ? 157 LYS   B N   1 
ATOM   1373 C  CA  . LYS   B 2 148 ? 5.275   -1.756  -20.569 1.00 61.99 ? 157 LYS   B CA  1 
ATOM   1374 C  C   . LYS   B 2 148 ? 5.278   -0.619  -21.601 1.00 63.02 ? 157 LYS   B C   1 
ATOM   1375 O  O   . LYS   B 2 148 ? 6.204   0.193   -21.630 1.00 63.22 ? 157 LYS   B O   1 
ATOM   1376 C  CB  . LYS   B 2 148 ? 6.092   -2.948  -21.105 1.00 64.49 ? 157 LYS   B CB  1 
ATOM   1377 C  CG  . LYS   B 2 148 ? 6.075   -4.167  -20.175 1.00 69.69 ? 157 LYS   B CG  1 
ATOM   1378 C  CD  . LYS   B 2 148 ? 7.188   -5.177  -20.507 1.00 74.87 ? 157 LYS   B CD  1 
ATOM   1379 C  CE  . LYS   B 2 148 ? 8.524   -4.816  -19.886 1.00 78.62 ? 157 LYS   B CE  1 
ATOM   1380 N  NZ  . LYS   B 2 148 ? 8.471   -4.819  -18.393 1.00 80.51 ? 157 LYS   B NZ  1 
ATOM   1381 N  N   . ASN   B 2 149 ? 4.241   -0.550  -22.430 1.00 63.32 ? 158 ASN   B N   1 
ATOM   1382 C  CA  . ASN   B 2 149 ? 4.140   0.477   -23.459 1.00 64.05 ? 158 ASN   B CA  1 
ATOM   1383 C  C   . ASN   B 2 149 ? 3.270   1.695   -23.073 1.00 62.46 ? 158 ASN   B C   1 
ATOM   1384 O  O   . ASN   B 2 149 ? 2.884   2.462   -23.954 1.00 62.51 ? 158 ASN   B O   1 
ATOM   1385 C  CB  . ASN   B 2 149 ? 3.673   -0.124  -24.799 1.00 67.47 ? 158 ASN   B CB  1 
ATOM   1386 C  CG  . ASN   B 2 149 ? 2.717   -1.296  -24.685 1.00 72.92 ? 158 ASN   B CG  1 
ATOM   1387 O  OD1 . ASN   B 2 149 ? 3.119   -2.426  -24.337 1.00 74.34 ? 158 ASN   B OD1 1 
ATOM   1388 N  ND2 . ASN   B 2 149 ? 1.437   -1.044  -24.976 1.00 74.11 ? 158 ASN   B ND2 1 
ATOM   1389 N  N   . GLY   B 2 150 ? 3.014   1.877   -21.775 1.00 60.70 ? 159 GLY   B N   1 
ATOM   1390 C  CA  . GLY   B 2 150 ? 2.251   3.004   -21.245 1.00 59.26 ? 159 GLY   B CA  1 
ATOM   1391 C  C   . GLY   B 2 150 ? 0.744   2.882   -21.351 1.00 57.57 ? 159 GLY   B C   1 
ATOM   1392 O  O   . GLY   B 2 150 ? 0.008   3.591   -20.658 1.00 57.47 ? 159 GLY   B O   1 
ATOM   1393 N  N   . SER   B 2 151 ? 0.271   1.981   -22.228 1.00 56.06 ? 160 SER   B N   1 
ATOM   1394 C  CA  A SER   B 2 151 ? -1.152  1.718   -22.466 0.50 55.47 ? 160 SER   B CA  1 
ATOM   1395 C  CA  B SER   B 2 151 ? -1.162  1.775   -22.435 0.50 55.48 ? 160 SER   B CA  1 
ATOM   1396 C  C   . SER   B 2 151 ? -1.845  1.072   -21.241 1.00 54.57 ? 160 SER   B C   1 
ATOM   1397 O  O   . SER   B 2 151 ? -1.167  0.599   -20.316 1.00 54.08 ? 160 SER   B O   1 
ATOM   1398 C  CB  A SER   B 2 151 ? -1.317  0.835   -23.704 0.50 56.62 ? 160 SER   B CB  1 
ATOM   1399 C  CB  B SER   B 2 151 ? -1.432  1.060   -23.761 0.50 56.72 ? 160 SER   B CB  1 
ATOM   1400 O  OG  A SER   B 2 151 ? -2.664  0.446   -23.919 0.50 58.80 ? 160 SER   B OG  1 
ATOM   1401 O  OG  B SER   B 2 151 ? -0.527  0.001   -24.019 0.50 59.02 ? 160 SER   B OG  1 
ATOM   1402 N  N   . TYR   B 2 152 ? -3.200  1.052   -21.238 1.00 52.66 ? 161 TYR   B N   1 
ATOM   1403 C  CA  . TYR   B 2 152 ? -3.998  0.475   -20.167 1.00 51.22 ? 161 TYR   B CA  1 
ATOM   1404 C  C   . TYR   B 2 152 ? -4.719  -0.828  -20.555 1.00 49.46 ? 161 TYR   B C   1 
ATOM   1405 O  O   . TYR   B 2 152 ? -5.349  -0.914  -21.608 1.00 49.50 ? 161 TYR   B O   1 
ATOM   1406 C  CB  . TYR   B 2 152 ? -5.050  1.512   -19.725 1.00 51.13 ? 161 TYR   B CB  1 
ATOM   1407 C  CG  . TYR   B 2 152 ? -5.487  1.418   -18.279 1.00 51.30 ? 161 TYR   B CG  1 
ATOM   1408 C  CD1 . TYR   B 2 152 ? -4.659  1.844   -17.254 1.00 52.18 ? 161 TYR   B CD1 1 
ATOM   1409 C  CD2 . TYR   B 2 152 ? -6.767  0.998   -17.945 1.00 52.00 ? 161 TYR   B CD2 1 
ATOM   1410 C  CE1 . TYR   B 2 152 ? -5.070  1.800   -15.925 1.00 53.20 ? 161 TYR   B CE1 1 
ATOM   1411 C  CE2 . TYR   B 2 152 ? -7.189  0.947   -16.622 1.00 52.70 ? 161 TYR   B CE2 1 
ATOM   1412 C  CZ  . TYR   B 2 152 ? -6.345  1.366   -15.613 1.00 53.82 ? 161 TYR   B CZ  1 
ATOM   1413 O  OH  . TYR   B 2 152 ? -6.755  1.330   -14.299 1.00 55.30 ? 161 TYR   B OH  1 
ATOM   1414 N  N   . VAL   B 2 153 ? -4.666  -1.822  -19.670 1.00 47.61 ? 162 VAL   B N   1 
ATOM   1415 C  CA  . VAL   B 2 153 ? -5.441  -3.047  -19.823 1.00 46.15 ? 162 VAL   B CA  1 
ATOM   1416 C  C   . VAL   B 2 153 ? -6.390  -3.053  -18.631 1.00 43.67 ? 162 VAL   B C   1 
ATOM   1417 O  O   . VAL   B 2 153 ? -5.938  -3.008  -17.503 1.00 43.09 ? 162 VAL   B O   1 
ATOM   1418 C  CB  . VAL   B 2 153 ? -4.590  -4.331  -19.906 1.00 47.01 ? 162 VAL   B CB  1 
ATOM   1419 C  CG1 . VAL   B 2 153 ? -5.485  -5.561  -20.049 1.00 46.94 ? 162 VAL   B CG1 1 
ATOM   1420 C  CG2 . VAL   B 2 153 ? -3.608  -4.244  -21.074 1.00 48.06 ? 162 VAL   B CG2 1 
ATOM   1421 N  N   . SER   B 2 154 ? -7.690  -2.986  -18.875 1.00 42.45 ? 163 SER   B N   1 
ATOM   1422 C  CA  . SER   B 2 154 ? -8.672  -2.921  -17.798 1.00 41.69 ? 163 SER   B CA  1 
ATOM   1423 C  C   . SER   B 2 154 ? -9.314  -4.270  -17.559 1.00 41.58 ? 163 SER   B C   1 
ATOM   1424 O  O   . SER   B 2 154 ? -9.552  -5.009  -18.500 1.00 42.16 ? 163 SER   B O   1 
ATOM   1425 C  CB  . SER   B 2 154 ? -9.740  -1.886  -18.121 1.00 41.82 ? 163 SER   B CB  1 
ATOM   1426 O  OG  . SER   B 2 154 ? -10.956 -2.102  -17.417 1.00 42.85 ? 163 SER   B OG  1 
ATOM   1427 N  N   . ALA   B 2 155 ? -9.648  -4.560  -16.319 1.00 40.83 ? 164 ALA   B N   1 
ATOM   1428 C  CA  . ALA   B 2 155 ? -10.334 -5.794  -15.970 1.00 40.92 ? 164 ALA   B CA  1 
ATOM   1429 C  C   . ALA   B 2 155 ? -11.822 -5.710  -16.404 1.00 41.10 ? 164 ALA   B C   1 
ATOM   1430 O  O   . ALA   B 2 155 ? -12.344 -4.628  -16.689 1.00 40.00 ? 164 ALA   B O   1 
ATOM   1431 C  CB  . ALA   B 2 155 ? -10.240 -6.016  -14.464 1.00 40.87 ? 164 ALA   B CB  1 
ATOM   1432 N  N   . ILE   B 2 156 ? -12.487 -6.867  -16.485 1.00 41.84 ? 165 ILE   B N   1 
ATOM   1433 C  CA  . ILE   B 2 156 ? -13.914 -6.916  -16.752 1.00 42.66 ? 165 ILE   B CA  1 
ATOM   1434 C  C   . ILE   B 2 156 ? -14.495 -7.072  -15.352 1.00 42.96 ? 165 ILE   B C   1 
ATOM   1435 O  O   . ILE   B 2 156 ? -14.468 -8.172  -14.788 1.00 42.37 ? 165 ILE   B O   1 
ATOM   1436 C  CB  . ILE   B 2 156 ? -14.283 -8.089  -17.687 1.00 43.21 ? 165 ILE   B CB  1 
ATOM   1437 C  CG1 . ILE   B 2 156 ? -13.604 -7.913  -19.049 1.00 43.57 ? 165 ILE   B CG1 1 
ATOM   1438 C  CG2 . ILE   B 2 156 ? -15.816 -8.199  -17.813 1.00 43.89 ? 165 ILE   B CG2 1 
ATOM   1439 C  CD1 . ILE   B 2 156 ? -13.812 -9.023  -19.972 1.00 44.80 ? 165 ILE   B CD1 1 
ATOM   1440 N  N   . THR   B 2 157 ? -14.889 -5.927  -14.732 1.00 43.30 ? 166 THR   B N   1 
ATOM   1441 C  CA  . THR   B 2 157 ? -15.375 -5.897  -13.349 1.00 43.46 ? 166 THR   B CA  1 
ATOM   1442 C  C   . THR   B 2 157 ? -16.873 -6.065  -13.217 1.00 43.48 ? 166 THR   B C   1 
ATOM   1443 O  O   . THR   B 2 157 ? -17.628 -5.160  -13.562 1.00 43.16 ? 166 THR   B O   1 
ATOM   1444 C  CB  . THR   B 2 157 ? -14.953 -4.607  -12.642 1.00 44.72 ? 166 THR   B CB  1 
ATOM   1445 O  OG1 . THR   B 2 157 ? -13.542 -4.418  -12.747 1.00 45.90 ? 166 THR   B OG1 1 
ATOM   1446 C  CG2 . THR   B 2 157 ? -15.332 -4.613  -11.197 1.00 45.03 ? 166 THR   B CG2 1 
ATOM   1447 N  N   . GLN   B 2 158 ? -17.301 -7.190  -12.665 1.00 43.68 ? 167 GLN   B N   1 
ATOM   1448 C  CA  . GLN   B 2 158 ? -18.714 -7.455  -12.458 1.00 44.48 ? 167 GLN   B CA  1 
ATOM   1449 C  C   . GLN   B 2 158 ? -19.008 -7.643  -10.954 1.00 46.05 ? 167 GLN   B C   1 
ATOM   1450 O  O   . GLN   B 2 158 ? -18.205 -8.219  -10.225 1.00 45.70 ? 167 GLN   B O   1 
ATOM   1451 C  CB  . GLN   B 2 158 ? -19.143 -8.694  -13.270 1.00 44.74 ? 167 GLN   B CB  1 
ATOM   1452 C  CG  . GLN   B 2 158 ? -20.603 -9.096  -13.141 1.00 45.78 ? 167 GLN   B CG  1 
ATOM   1453 C  CD  . GLN   B 2 158 ? -21.545 -8.061  -13.689 1.00 48.97 ? 167 GLN   B CD  1 
ATOM   1454 O  OE1 . GLN   B 2 158 ? -21.650 -6.945  -13.169 1.00 50.58 ? 167 GLN   B OE1 1 
ATOM   1455 N  NE2 . GLN   B 2 158 ? -22.271 -8.408  -14.734 1.00 49.21 ? 167 GLN   B NE2 1 
ATOM   1456 N  N   . GLY   B 2 159 ? -20.147 -7.131  -10.508 1.00 47.23 ? 168 GLY   B N   1 
ATOM   1457 C  CA  . GLY   B 2 159 ? -20.570 -7.285  -9.130  1.00 48.96 ? 168 GLY   B CA  1 
ATOM   1458 C  C   . GLY   B 2 159 ? -21.405 -8.529  -8.916  1.00 51.01 ? 168 GLY   B C   1 
ATOM   1459 O  O   . GLY   B 2 159 ? -21.530 -9.373  -9.807  1.00 50.74 ? 168 GLY   B O   1 
ATOM   1460 N  N   . LYS   B 2 160 ? -21.982 -8.645  -7.720  1.00 52.98 ? 169 LYS   B N   1 
ATOM   1461 C  CA  . LYS   B 2 160 ? -22.824 -9.770  -7.331  1.00 55.37 ? 169 LYS   B CA  1 
ATOM   1462 C  C   . LYS   B 2 160 ? -24.307 -9.339  -7.265  1.00 58.11 ? 169 LYS   B C   1 
ATOM   1463 O  O   . LYS   B 2 160 ? -24.617 -8.197  -6.911  1.00 58.47 ? 169 LYS   B O   1 
ATOM   1464 C  CB  . LYS   B 2 160 ? -22.365 -10.312 -5.958  1.00 56.91 ? 169 LYS   B CB  1 
ATOM   1465 C  CG  . LYS   B 2 160 ? -22.997 -11.647 -5.570  1.00 61.30 ? 169 LYS   B CG  1 
ATOM   1466 C  CD  . LYS   B 2 160 ? -22.857 -11.946 -4.082  1.00 65.64 ? 169 LYS   B CD  1 
ATOM   1467 C  CE  . LYS   B 2 160 ? -23.397 -13.307 -3.693  1.00 69.26 ? 169 LYS   B CE  1 
ATOM   1468 N  NZ  . LYS   B 2 160 ? -23.468 -13.477 -2.204  1.00 70.75 ? 169 LYS   B NZ  1 
ATOM   1469 N  N   . ARG   B 2 161 ? -25.219 -10.251 -7.617  1.00 59.84 ? 170 ARG   B N   1 
ATOM   1470 C  CA  . ARG   B 2 161 ? -26.657 -10.009 -7.524  1.00 61.80 ? 170 ARG   B CA  1 
ATOM   1471 C  C   . ARG   B 2 161 ? -27.191 -10.941 -6.420  1.00 63.65 ? 170 ARG   B C   1 
ATOM   1472 O  O   . ARG   B 2 161 ? -26.856 -12.130 -6.405  1.00 64.03 ? 170 ARG   B O   1 
ATOM   1473 C  CB  . ARG   B 2 161 ? -27.355 -10.279 -8.875  1.00 63.18 ? 170 ARG   B CB  1 
ATOM   1474 C  CG  . ARG   B 2 161 ? -28.872 -10.160 -8.800  1.00 66.27 ? 170 ARG   B CG  1 
ATOM   1475 C  CD  . ARG   B 2 161 ? -29.547 -10.052 -10.156 1.00 70.05 ? 170 ARG   B CD  1 
ATOM   1476 N  NE  . ARG   B 2 161 ? -30.905 -9.514  -10.015 1.00 73.49 ? 170 ARG   B NE  1 
ATOM   1477 C  CZ  . ARG   B 2 161 ? -31.586 -8.916  -10.989 1.00 75.24 ? 170 ARG   B CZ  1 
ATOM   1478 N  NH1 . ARG   B 2 161 ? -31.054 -8.783  -12.196 1.00 75.09 ? 170 ARG   B NH1 1 
ATOM   1479 N  NH2 . ARG   B 2 161 ? -32.801 -8.437  -10.758 1.00 74.75 ? 170 ARG   B NH2 1 
ATOM   1480 N  N   . GLU   B 2 162 ? -27.967 -10.402 -5.470  1.00 64.54 ? 171 GLU   B N   1 
ATOM   1481 C  CA  . GLU   B 2 162 ? -28.506 -11.213 -4.383  1.00 66.16 ? 171 GLU   B CA  1 
ATOM   1482 C  C   . GLU   B 2 162 ? -29.930 -11.703 -4.683  1.00 66.89 ? 171 GLU   B C   1 
ATOM   1483 O  O   . GLU   B 2 162 ? -30.354 -12.746 -4.171  1.00 67.18 ? 171 GLU   B O   1 
ATOM   1484 C  CB  . GLU   B 2 162 ? -28.458 -10.444 -3.052  1.00 69.63 ? 171 GLU   B CB  1 
ATOM   1485 C  CG  . GLU   B 2 162 ? -27.053 -10.205 -2.520  1.00 76.25 ? 171 GLU   B CG  1 
ATOM   1486 C  CD  . GLU   B 2 162 ? -26.556 -11.228 -1.513  1.00 85.08 ? 171 GLU   B CD  1 
ATOM   1487 O  OE1 . GLU   B 2 162 ? -25.678 -10.875 -0.692  1.00 86.87 ? 171 GLU   B OE1 1 
ATOM   1488 O  OE2 . GLU   B 2 162 ? -27.046 -12.381 -1.542  1.00 87.86 ? 171 GLU   B OE2 1 
HETATM 1489 S  S   . DMS   C 3 .   ? -18.391 11.820  -0.407  1.00 85.23 ? 201 DMS   B S   1 
HETATM 1490 O  O   . DMS   C 3 .   ? -19.249 10.590  -0.516  1.00 85.08 ? 201 DMS   B O   1 
HETATM 1491 C  C1  . DMS   C 3 .   ? -19.437 13.256  -0.787  1.00 85.31 ? 201 DMS   B C1  1 
HETATM 1492 C  C2  . DMS   C 3 .   ? -17.358 11.943  -1.901  1.00 84.98 ? 201 DMS   B C2  1 
HETATM 1493 N  N1  . A1B82 D 4 .   ? -8.515  4.053   -12.937 1.00 42.90 ? 202 A1B82 B N1  1 
HETATM 1494 N  N3  . A1B82 D 4 .   ? -7.574  4.572   -17.939 1.00 46.62 ? 202 A1B82 B N3  1 
HETATM 1495 C  C4  . A1B82 D 4 .   ? -8.607  5.177   -9.418  1.00 41.65 ? 202 A1B82 B C4  1 
HETATM 1496 C  C5  . A1B82 D 4 .   ? -8.886  3.975   -8.779  1.00 41.55 ? 202 A1B82 B C5  1 
HETATM 1497 C  C6  . A1B82 D 4 .   ? -9.088  2.810   -9.509  1.00 41.58 ? 202 A1B82 B C6  1 
HETATM 1498 C  C7  . A1B82 D 4 .   ? -8.962  2.806   -10.891 1.00 41.72 ? 202 A1B82 B C7  1 
HETATM 1499 C  C8  . A1B82 D 4 .   ? -9.383  1.683   -8.560  1.00 41.01 ? 202 A1B82 B C8  1 
HETATM 1500 C  C10 . A1B82 D 4 .   ? -7.630  4.758   -15.091 1.00 45.41 ? 202 A1B82 B C10 1 
HETATM 1501 C  C13 . A1B82 D 4 .   ? -6.504  4.968   -17.234 1.00 46.72 ? 202 A1B82 B C13 1 
HETATM 1502 C  C15 . A1B82 D 4 .   ? -5.127  5.487   -15.501 1.00 47.02 ? 202 A1B82 B C15 1 
HETATM 1503 O  O1  . A1B82 D 4 .   ? -6.902  5.651   -13.033 1.00 43.56 ? 202 A1B82 B O1  1 
HETATM 1504 C  C1  . A1B82 D 4 .   ? -7.668  4.874   -13.599 1.00 44.00 ? 202 A1B82 B C1  1 
HETATM 1505 C  C2  . A1B82 D 4 .   ? -8.697  4.022   -11.533 1.00 42.05 ? 202 A1B82 B C2  1 
HETATM 1506 C  C3  . A1B82 D 4 .   ? -8.480  5.184   -10.795 1.00 41.88 ? 202 A1B82 B C3  1 
HETATM 1507 N  N2  . A1B82 D 4 .   ? -8.841  2.227   -7.305  1.00 40.76 ? 202 A1B82 B N2  1 
HETATM 1508 C  C9  . A1B82 D 4 .   ? -9.074  3.681   -7.319  1.00 41.00 ? 202 A1B82 B C9  1 
HETATM 1509 C  C11 . A1B82 D 4 .   ? -8.721  4.312   -15.818 1.00 45.85 ? 202 A1B82 B C11 1 
HETATM 1510 C  C12 . A1B82 D 4 .   ? -8.658  4.247   -17.240 1.00 46.43 ? 202 A1B82 B C12 1 
HETATM 1511 CL CL1 . A1B82 D 4 .   ? -10.011 3.686   -18.173 1.00 47.16 ? 202 A1B82 B CL1 1 
HETATM 1512 N  N4  . A1B82 D 4 .   ? -5.277  5.295   -17.732 1.00 47.02 ? 202 A1B82 B N4  1 
HETATM 1513 C  C14 . A1B82 D 4 .   ? -4.457  5.630   -16.678 1.00 47.02 ? 202 A1B82 B C14 1 
HETATM 1514 C  C16 . A1B82 D 4 .   ? -6.457  5.076   -15.832 1.00 46.46 ? 202 A1B82 B C16 1 
HETATM 1515 O  O   . HOH   E 5 .   ? -3.959  -14.390 -25.181 1.00 34.12 ? 101 HOH   A O   1 
HETATM 1516 O  O   . HOH   E 5 .   ? -7.473  0.712   3.400   1.00 46.09 ? 102 HOH   A O   1 
HETATM 1517 O  O   . HOH   E 5 .   ? -1.082  -4.272  -5.548  1.00 44.70 ? 103 HOH   A O   1 
HETATM 1518 O  O   . HOH   E 5 .   ? -8.848  -7.191  -25.264 1.00 64.34 ? 104 HOH   A O   1 
HETATM 1519 O  O   . HOH   E 5 .   ? -29.257 15.317  -15.474 1.00 55.16 ? 105 HOH   A O   1 
HETATM 1520 O  O   . HOH   E 5 .   ? -23.291 18.716  -19.670 1.00 50.98 ? 106 HOH   A O   1 
HETATM 1521 O  O   . HOH   E 5 .   ? -6.454  -9.363  -2.952  1.00 40.43 ? 107 HOH   A O   1 
HETATM 1522 O  O   . HOH   E 5 .   ? -23.478 9.259   -27.341 1.00 38.06 ? 108 HOH   A O   1 
HETATM 1523 O  O   . HOH   E 5 .   ? -2.139  -11.930 -6.928  1.00 44.53 ? 109 HOH   A O   1 
HETATM 1524 O  O   . HOH   E 5 .   ? 0.092   -12.307 -23.466 1.00 44.00 ? 110 HOH   A O   1 
HETATM 1525 O  O   . HOH   E 5 .   ? -8.752  3.661   -3.705  1.00 39.91 ? 111 HOH   A O   1 
HETATM 1526 O  O   . HOH   E 5 .   ? -3.722  -0.650  0.166   1.00 48.20 ? 112 HOH   A O   1 
HETATM 1527 O  O   . HOH   E 5 .   ? -5.283  1.614   -9.924  1.00 28.45 ? 113 HOH   A O   1 
HETATM 1528 O  O   . HOH   E 5 .   ? -21.201 -9.367  -34.817 1.00 46.61 ? 114 HOH   A O   1 
HETATM 1529 O  O   . HOH   E 5 .   ? -6.421  -6.806  0.580   1.00 42.67 ? 115 HOH   A O   1 
HETATM 1530 O  O   . HOH   E 5 .   ? -27.608 -5.122  -34.937 1.00 41.98 ? 116 HOH   A O   1 
HETATM 1531 O  O   . HOH   F 5 .   ? -6.474  -0.743  -10.783 1.00 38.05 ? 301 HOH   B O   1 
HETATM 1532 O  O   . HOH   F 5 .   ? -25.818 -7.952  -16.683 1.00 39.87 ? 302 HOH   B O   1 
HETATM 1533 O  O   . HOH   F 5 .   ? -12.920 -2.434  -14.661 1.00 47.89 ? 303 HOH   B O   1 
HETATM 1534 O  O   . HOH   F 5 .   ? -34.846 4.228   -9.286  1.00 41.80 ? 304 HOH   B O   1 
HETATM 1535 O  O   . HOH   F 5 .   ? -17.669 -10.879 -16.461 1.00 37.22 ? 305 HOH   B O   1 
HETATM 1536 O  O   . HOH   F 5 .   ? -15.604 -10.521 -15.031 1.00 46.82 ? 306 HOH   B O   1 
HETATM 1537 O  O   . HOH   F 5 .   ? -16.951 12.778  -5.608  1.00 44.76 ? 307 HOH   B O   1 
HETATM 1538 O  O   . HOH   F 5 .   ? -21.194 -14.208 -21.794 1.00 49.93 ? 308 HOH   B O   1 
HETATM 1539 O  O   . HOH   F 5 .   ? -33.714 1.685   -15.466 1.00 35.77 ? 309 HOH   B O   1 
HETATM 1540 O  O   . HOH   F 5 .   ? -29.928 -5.454  -1.153  1.00 38.36 ? 310 HOH   B O   1 
HETATM 1541 O  O   . HOH   F 5 .   ? 6.384   -4.443  -16.708 1.00 71.13 ? 311 HOH   B O   1 
HETATM 1542 O  O   . HOH   F 5 .   ? -30.773 11.817  -16.577 1.00 51.14 ? 312 HOH   B O   1 
HETATM 1543 O  O   . HOH   F 5 .   ? -12.230 -3.848  -9.868  1.00 34.28 ? 313 HOH   B O   1 
HETATM 1544 O  O   . HOH   F 5 .   ? -11.522 1.598   -5.908  1.00 27.29 ? 314 HOH   B O   1 
HETATM 1545 O  O   . HOH   F 5 .   ? -20.704 14.341  -34.020 1.00 54.41 ? 315 HOH   B O   1 
HETATM 1546 O  O   . HOH   F 5 .   ? -27.261 -6.439  -18.439 1.00 51.88 ? 316 HOH   B O   1 
HETATM 1547 O  O   . HOH   F 5 .   ? -14.871 -5.209  1.399   1.00 33.26 ? 317 HOH   B O   1 
HETATM 1548 O  O   . HOH   F 5 .   ? -28.618 -7.568  -5.781  1.00 55.94 ? 318 HOH   B O   1 
HETATM 1549 O  O   . HOH   F 5 .   ? -5.187  2.676   -12.334 1.00 48.87 ? 319 HOH   B O   1 
HETATM 1550 O  O   . HOH   F 5 .   ? -8.409  -15.188 -24.169 1.00 45.94 ? 320 HOH   B O   1 
HETATM 1551 O  O   . HOH   F 5 .   ? -19.439 -12.852 -25.694 1.00 39.31 ? 321 HOH   B O   1 
HETATM 1552 O  O   . HOH   F 5 .   ? -29.459 -1.896  -19.227 1.00 49.71 ? 322 HOH   B O   1 
HETATM 1553 O  O   . HOH   F 5 .   ? -10.872 11.828  -19.003 1.00 43.30 ? 323 HOH   B O   1 
HETATM 1554 O  O   . HOH   F 5 .   ? -17.906 15.419  -21.922 1.00 50.12 ? 324 HOH   B O   1 
HETATM 1555 O  O   . HOH   F 5 .   ? -14.147 -12.611 -16.298 1.00 44.17 ? 325 HOH   B O   1 
HETATM 1556 O  O   . HOH   F 5 .   ? -15.741 -14.819 -16.248 1.00 57.32 ? 326 HOH   B O   1 
HETATM 1557 O  O   . HOH   F 5 .   ? -6.752  9.954   -19.019 1.00 43.40 ? 327 HOH   B O   1 
HETATM 1558 O  O   . HOH   F 5 .   ? -16.789 -15.111 -30.935 1.00 58.59 ? 328 HOH   B O   1 
HETATM 1559 O  O   . HOH   F 5 .   ? -2.585  -8.896  -3.042  1.00 44.15 ? 329 HOH   B O   1 
HETATM 1560 O  O   . HOH   F 5 .   ? -23.572 -15.331 -17.671 1.00 69.85 ? 330 HOH   B O   1 
HETATM 1561 O  O   . HOH   F 5 .   ? -4.467  -10.697 -5.640  1.00 37.95 ? 331 HOH   B O   1 
HETATM 1562 O  O   . HOH   F 5 .   ? -11.628 -5.522  -8.357  1.00 38.43 ? 332 HOH   B O   1 
HETATM 1563 O  O   . HOH   F 5 .   ? -10.923 7.797   -13.541 1.00 40.46 ? 333 HOH   B O   1 
HETATM 1564 O  O   . HOH   F 5 .   ? -14.722 -6.805  -1.329  1.00 56.55 ? 334 HOH   B O   1 
HETATM 1565 O  O   . HOH   F 5 .   ? -25.846 -5.387  -4.085  1.00 51.04 ? 335 HOH   B O   1 
HETATM 1566 O  O   . HOH   F 5 .   ? -14.795 16.153  -20.413 1.00 57.70 ? 336 HOH   B O   1 
HETATM 1567 O  O   . HOH   F 5 .   ? -21.776 15.004  -5.776  1.00 46.66 ? 337 HOH   B O   1 
HETATM 1568 O  O   . HOH   F 5 .   ? -22.712 -5.987  0.731   1.00 39.25 ? 338 HOH   B O   1 
HETATM 1569 O  O   . HOH   F 5 .   ? -24.645 -13.000 -9.158  1.00 40.36 ? 339 HOH   B O   1 
HETATM 1570 O  O   . HOH   F 5 .   ? -0.928  -14.937 -9.993  1.00 36.77 ? 340 HOH   B O   1 
HETATM 1571 O  O   . HOH   F 5 .   ? -15.106 8.351   -30.371 1.00 52.66 ? 341 HOH   B O   1 
HETATM 1572 O  O   . HOH   F 5 .   ? -9.976  7.052   -6.041  1.00 40.21 ? 342 HOH   B O   1 
HETATM 1573 O  O   . HOH   F 5 .   ? -35.148 -0.633  -8.008  1.00 41.30 ? 343 HOH   B O   1 
HETATM 1574 O  O   . HOH   F 5 .   ? -21.008 1.647   -32.801 1.00 46.01 ? 344 HOH   B O   1 
HETATM 1575 O  O   . HOH   F 5 .   ? -15.670 -6.877  -8.395  1.00 55.71 ? 345 HOH   B O   1 
HETATM 1576 O  O   . HOH   F 5 .   ? -0.685  0.409   -12.712 1.00 34.51 ? 346 HOH   B O   1 
HETATM 1577 O  O   B HOH   F 5 .   ? -21.591 5.058   -1.056  0.50 74.84 ? 347 HOH   B O   1 
HETATM 1578 O  O   . HOH   F 5 .   ? -21.243 15.444  -24.009 1.00 29.86 ? 348 HOH   B O   1 
HETATM 1579 O  O   . HOH   F 5 .   ? -17.167 13.384  -31.180 1.00 35.59 ? 349 HOH   B O   1 
HETATM 1580 O  O   . HOH   F 5 .   ? -20.524 -8.485  -1.649  1.00 51.40 ? 350 HOH   B O   1 
HETATM 1581 O  O   . HOH   F 5 .   ? -9.987  -11.036 -7.868  1.00 43.30 ? 351 HOH   B O   1 
HETATM 1582 O  O   . HOH   F 5 .   ? -22.471 -14.747 -25.676 1.00 50.97 ? 352 HOH   B O   1 
HETATM 1583 O  O   . HOH   F 5 .   ? -11.705 12.218  -14.777 1.00 38.33 ? 353 HOH   B O   1 
HETATM 1584 O  O   . HOH   F 5 .   ? -33.035 2.502   -1.035  1.00 49.44 ? 354 HOH   B O   1 
HETATM 1585 O  O   . HOH   F 5 .   ? -27.831 13.409  3.182   1.00 63.04 ? 355 HOH   B O   1 
HETATM 1586 O  O   . HOH   F 5 .   ? -15.028 10.495  -32.029 1.00 46.30 ? 356 HOH   B O   1 
HETATM 1587 O  O   . HOH   F 5 .   ? -21.798 19.764  -21.846 1.00 55.49 ? 357 HOH   B O   1 
HETATM 1588 O  O   . HOH   F 5 .   ? -11.677 -8.068  1.574   1.00 48.60 ? 358 HOH   B 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   . ASP   A 7   ? 0.7359 0.3586 0.7802 0.1492  -0.0096 -0.1383 50  ASP   A N   
2    C  CA  . ASP   A 7   ? 0.7260 0.3963 0.7373 0.1643  -0.0010 -0.1414 50  ASP   A CA  
3    C  C   . ASP   A 7   ? 0.7143 0.3950 0.7108 0.1638  0.0138  -0.1026 50  ASP   A C   
4    O  O   . ASP   A 7   ? 0.7277 0.3749 0.7251 0.1754  0.0151  -0.0796 50  ASP   A O   
5    C  CB  . ASP   A 7   ? 0.7463 0.4143 0.7519 0.1934  -0.0091 -0.1679 50  ASP   A CB  
6    C  CG  . ASP   A 7   ? 0.8138 0.5395 0.7976 0.2013  -0.0037 -0.1943 50  ASP   A CG  
7    O  OD1 . ASP   A 7   ? 0.8212 0.5524 0.8060 0.2202  -0.0109 -0.2277 50  ASP   A OD1 
8    O  OD2 . ASP   A 7   ? 0.8415 0.6063 0.8076 0.1886  0.0089  -0.1816 50  ASP   A OD2 
9    N  N   . MET   A 8   ? 0.6856 0.4098 0.6647 0.1523  0.0240  -0.0956 51  MET   A N   
10   C  CA  . MET   A 8   ? 0.6680 0.4056 0.6306 0.1530  0.0366  -0.0641 51  MET   A CA  
11   C  C   . MET   A 8   ? 0.6513 0.4077 0.5948 0.1769  0.0369  -0.0680 51  MET   A C   
12   O  O   . MET   A 8   ? 0.6412 0.4224 0.5818 0.1871  0.0328  -0.0970 51  MET   A O   
13   C  CB  . MET   A 8   ? 0.6636 0.4361 0.6159 0.1343  0.0451  -0.0576 51  MET   A CB  
14   C  CG  . MET   A 8   ? 0.6776 0.4352 0.6527 0.1132  0.0464  -0.0438 51  MET   A CG  
15   S  SD  . MET   A 8   ? 0.7137 0.5126 0.6757 0.0971  0.0521  -0.0413 51  MET   A SD  
16   C  CE  . MET   A 8   ? 0.6768 0.4592 0.6811 0.0752  0.0498  -0.0314 51  MET   A CE  
17   N  N   . TYR   A 9   ? 0.6495 0.3955 0.5810 0.1871  0.0418  -0.0396 52  TYR   A N   
18   C  CA  . TYR   A 9   ? 0.6468 0.4110 0.5619 0.2120  0.0386  -0.0420 52  TYR   A CA  
19   C  C   . TYR   A 9   ? 0.6496 0.4315 0.5422 0.2124  0.0473  -0.0168 52  TYR   A C   
20   O  O   . TYR   A 9   ? 0.6501 0.4216 0.5393 0.1968  0.0572  0.0077  52  TYR   A O   
21   C  CB  . TYR   A 9   ? 0.6555 0.3794 0.5742 0.2383  0.0272  -0.0404 52  TYR   A CB  
22   C  CG  . TYR   A 9   ? 0.6850 0.3530 0.6001 0.2382  0.0308  -0.0035 52  TYR   A CG  
23   C  CD1 . TYR   A 9   ? 0.7008 0.3246 0.6392 0.2220  0.0309  0.0010  52  TYR   A CD1 
24   C  CD2 . TYR   A 9   ? 0.7087 0.3653 0.5969 0.2566  0.0334  0.0253  52  TYR   A CD2 
25   C  CE1 . TYR   A 9   ? 0.7313 0.3017 0.6702 0.2193  0.0376  0.0366  52  TYR   A CE1 
26   C  CE2 . TYR   A 9   ? 0.7368 0.3390 0.6167 0.2575  0.0403  0.0623  52  TYR   A CE2 
27   C  CZ  . TYR   A 9   ? 0.7609 0.3191 0.6681 0.2374  0.0440  0.0691  52  TYR   A CZ  
28   O  OH  . TYR   A 9   ? 0.8106 0.3124 0.7136 0.2347  0.0542  0.1075  52  TYR   A OH  
29   N  N   . ILE   A 10  ? 0.6401 0.4535 0.5203 0.2304  0.0430  -0.0264 53  ILE   A N   
30   C  CA  . ILE   A 10  ? 0.6384 0.4703 0.4961 0.2338  0.0476  -0.0090 53  ILE   A CA  
31   C  C   . ILE   A 10  ? 0.6552 0.4802 0.4960 0.2666  0.0367  -0.0019 53  ILE   A C   
32   O  O   . ILE   A 10  ? 0.6516 0.4831 0.5024 0.2873  0.0239  -0.0229 53  ILE   A O   
33   C  CB  . ILE   A 10  ? 0.6212 0.5022 0.4783 0.2188  0.0526  -0.0272 53  ILE   A CB  
34   C  CG1 . ILE   A 10  ? 0.6051 0.5232 0.4758 0.2290  0.0457  -0.0605 53  ILE   A CG1 
35   C  CG2 . ILE   A 10  ? 0.6244 0.5066 0.4879 0.1905  0.0621  -0.0282 53  ILE   A CG2 
36   C  CD1 . ILE   A 10  ? 0.5927 0.5547 0.4616 0.2159  0.0518  -0.0728 53  ILE   A CD1 
37   N  N   . GLU   A 11  ? 0.6714 0.4839 0.4848 0.2736  0.0414  0.0272  54  GLU   A N   
38   C  CA  . GLU   A 11  ? 0.6955 0.5009 0.4819 0.3071  0.0302  0.0373  54  GLU   A CA  
39   C  C   . GLU   A 11  ? 0.6993 0.5369 0.4622 0.3075  0.0331  0.0418  54  GLU   A C   
40   O  O   . GLU   A 11  ? 0.6938 0.5294 0.4488 0.2879  0.0482  0.0592  54  GLU   A O   
41   C  CB  . GLU   A 11  ? 0.7536 0.4994 0.5181 0.3192  0.0349  0.0750  54  GLU   A CB  
42   C  CG  . GLU   A 11  ? 0.8374 0.5375 0.6232 0.3188  0.0319  0.0753  54  GLU   A CG  
43   C  CD  . GLU   A 11  ? 0.9522 0.5898 0.7213 0.3199  0.0430  0.1171  54  GLU   A CD  
44   O  OE1 . GLU   A 11  ? 0.9580 0.5938 0.7068 0.3100  0.0600  0.1461  54  GLU   A OE1 
45   O  OE2 . GLU   A 11  ? 1.0137 0.6028 0.7905 0.3305  0.0359  0.1209  54  GLU   A OE2 
46   N  N   . ARG   A 12  ? 0.7017 0.5684 0.4549 0.3315  0.0171  0.0249  55  ARG   A N   
47   C  CA  . ARG   A 12  ? 0.7094 0.6046 0.4408 0.3339  0.0163  0.0247  55  ARG   A CA  
48   C  C   . ARG   A 12  ? 0.7545 0.6176 0.4422 0.3461  0.0248  0.0620  55  ARG   A C   
49   O  O   . ARG   A 12  ? 0.7804 0.6058 0.4441 0.3699  0.0216  0.0844  55  ARG   A O   
50   C  CB  . ARG   A 12  ? 0.7013 0.6352 0.4366 0.3583  -0.0059 -0.0046 55  ARG   A CB  
51   C  CG  . ARG   A 12  ? 0.7112 0.6875 0.4501 0.3452  -0.0067 -0.0231 55  ARG   A CG  
52   C  CD  . ARG   A 12  ? 0.7125 0.7344 0.4724 0.3620  -0.0284 -0.0591 55  ARG   A CD  
53   N  NE  . ARG   A 12  ? 0.7240 0.7810 0.4884 0.3487  -0.0304 -0.0769 55  ARG   A NE  
54   C  CZ  . ARG   A 12  ? 0.7670 0.8254 0.4978 0.3667  -0.0408 -0.0724 55  ARG   A CZ  
55   N  NH1 . ARG   A 12  ? 0.8022 0.8300 0.4875 0.3990  -0.0476 -0.0477 55  ARG   A NH1 
56   N  NH2 . ARG   A 12  ? 0.7477 0.8345 0.4869 0.3527  -0.0436 -0.0919 55  ARG   A NH2 
57   N  N   . ALA   A 13  ? 0.7618 0.6383 0.4376 0.3308  0.0370  0.0697  56  ALA   A N   
58   C  CA  . ALA   A 13  ? 0.7931 0.6482 0.4276 0.3409  0.0494  0.1032  56  ALA   A CA  
59   C  C   . ALA   A 13  ? 0.8056 0.6872 0.4060 0.3619  0.0388  0.0942  56  ALA   A C   
60   O  O   . ALA   A 13  ? 0.8321 0.6976 0.3892 0.3792  0.0467  0.1200  56  ALA   A O   
61   C  CB  . ALA   A 13  ? 0.7930 0.6416 0.4412 0.3093  0.0732  0.1200  56  ALA   A CB  
62   N  N   . GLY   A 14  ? 0.7861 0.7075 0.4059 0.3599  0.0222  0.0578  57  GLY   A N   
63   C  CA  . GLY   A 14  ? 0.7916 0.7382 0.3849 0.3783  0.0086  0.0434  57  GLY   A CA  
64   C  C   . GLY   A 14  ? 0.7721 0.7590 0.3978 0.3584  0.0003  0.0068  57  GLY   A C   
65   O  O   . GLY   A 14  ? 0.7596 0.7572 0.4267 0.3305  0.0062  -0.0073 57  GLY   A O   
66   N  N   . ASP   A 15  ? 0.7699 0.7776 0.3753 0.3734  -0.0139 -0.0096 58  ASP   A N   
67   C  CA  . ASP   A 15  ? 0.7529 0.7946 0.3872 0.3557  -0.0233 -0.0447 58  ASP   A CA  
68   C  C   . ASP   A 15  ? 0.7774 0.8110 0.4025 0.3344  -0.0069 -0.0366 58  ASP   A C   
69   O  O   . ASP   A 15  ? 0.7968 0.8093 0.3845 0.3448  0.0055  -0.0097 58  ASP   A O   
70   C  CB  . ASP   A 15  ? 0.7580 0.8237 0.3748 0.3858  -0.0511 -0.0695 58  ASP   A CB  
71   C  CG  . ASP   A 15  ? 0.7903 0.8838 0.4351 0.4026  -0.0752 -0.0964 58  ASP   A CG  
72   O  OD1 . ASP   A 15  ? 0.7829 0.8737 0.4555 0.3957  -0.0698 -0.0932 58  ASP   A OD1 
73   O  OD2 . ASP   A 15  ? 0.8192 0.9384 0.4578 0.4257  -0.1015 -0.1226 58  ASP   A OD2 
74   N  N   . ILE   A 16  ? 0.7724 0.8235 0.4299 0.3070  -0.0072 -0.0606 59  ILE   A N   
75   C  CA  . ILE   A 16  ? 0.7929 0.8343 0.4408 0.2904  0.0042  -0.0563 59  ILE   A CA  
76   C  C   . ILE   A 16  ? 0.8118 0.8679 0.4483 0.3016  -0.0141 -0.0826 59  ILE   A C   
77   O  O   . ILE   A 16  ? 0.7958 0.8704 0.4655 0.2846  -0.0242 -0.1120 59  ILE   A O   
78   C  CB  . ILE   A 16  ? 0.7897 0.8282 0.4721 0.2531  0.0188  -0.0584 59  ILE   A CB  
79   C  CG1 . ILE   A 16  ? 0.8041 0.8266 0.4938 0.2457  0.0341  -0.0345 59  ILE   A CG1 
80   C  CG2 . ILE   A 16  ? 0.8018 0.8279 0.4731 0.2394  0.0267  -0.0561 59  ILE   A CG2 
81   C  CD1 . ILE   A 16  ? 0.8044 0.8310 0.5282 0.2161  0.0424  -0.0435 59  ILE   A CD1 
82   N  N   A THR   A 17  ? 0.8357 0.8837 0.4251 0.3309  -0.0180 -0.0724 60  THR   A N   
83   N  N   B THR   A 17  ? 0.8384 0.8864 0.4280 0.3306  -0.0179 -0.0726 60  THR   A N   
84   C  CA  A THR   A 17  ? 0.8479 0.9061 0.4161 0.3486  -0.0371 -0.0971 60  THR   A CA  
85   C  CA  B THR   A 17  ? 0.8523 0.9114 0.4223 0.3479  -0.0377 -0.0983 60  THR   A CA  
86   C  C   A THR   A 17  ? 0.8798 0.9202 0.4039 0.3610  -0.0240 -0.0787 60  THR   A C   
87   C  C   B THR   A 17  ? 0.8830 0.9243 0.4056 0.3631  -0.0256 -0.0797 60  THR   A C   
88   O  O   A THR   A 17  ? 0.8885 0.9139 0.3891 0.3682  -0.0036 -0.0444 60  THR   A O   
89   O  O   B THR   A 17  ? 0.8931 0.9197 0.3901 0.3724  -0.0061 -0.0455 60  THR   A O   
90   C  CB  A THR   A 17  ? 0.8618 0.9358 0.4058 0.3868  -0.0620 -0.1093 60  THR   A CB  
91   C  CB  B THR   A 17  ? 0.8670 0.9462 0.4252 0.3808  -0.0646 -0.1160 60  THR   A CB  
92   O  OG1 A THR   A 17  ? 0.8880 0.9430 0.3890 0.4121  -0.0506 -0.0731 60  THR   A OG1 
93   O  OG1 B THR   A 17  ? 0.8552 0.9589 0.4677 0.3639  -0.0757 -0.1402 60  THR   A OG1 
94   C  CG2 A THR   A 17  ? 0.8429 0.9452 0.4348 0.3804  -0.0811 -0.1377 60  THR   A CG2 
95   C  CG2 B THR   A 17  ? 0.8771 0.9676 0.4073 0.4056  -0.0885 -0.1433 60  THR   A CG2 
96   N  N   . TRP   A 18  ? 0.8957 0.9385 0.4104 0.3644  -0.0358 -0.1030 61  TRP   A N   
97   C  CA  . TRP   A 18  ? 0.9504 0.9808 0.4216 0.3819  -0.0252 -0.0907 61  TRP   A CA  
98   C  C   . TRP   A 18  ? 1.0170 1.0541 0.4330 0.4265  -0.0360 -0.0873 61  TRP   A C   
99   O  O   . TRP   A 18  ? 1.0146 1.0673 0.4269 0.4444  -0.0639 -0.1142 61  TRP   A O   
100  C  CB  . TRP   A 18  ? 0.9459 0.9714 0.4251 0.3721  -0.0355 -0.1199 61  TRP   A CB  
101  C  CG  . TRP   A 18  ? 0.9739 0.9903 0.4081 0.3954  -0.0277 -0.1139 61  TRP   A CG  
102  C  CD1 . TRP   A 18  ? 0.9976 1.0204 0.3851 0.4323  -0.0428 -0.1301 61  TRP   A CD1 
103  C  CD2 . TRP   A 18  ? 0.9791 0.9816 0.4123 0.3851  -0.0042 -0.0939 61  TRP   A CD2 
104  N  NE1 . TRP   A 18  ? 1.0130 1.0275 0.3694 0.4460  -0.0270 -0.1198 61  TRP   A NE1 
105  C  CE2 . TRP   A 18  ? 1.0032 1.0066 0.3900 0.4173  -0.0038 -0.0981 61  TRP   A CE2 
106  C  CE3 . TRP   A 18  ? 0.9762 0.9682 0.4418 0.3548  0.0155  -0.0736 61  TRP   A CE3 
107  C  CZ2 . TRP   A 18  ? 1.0145 1.0114 0.3928 0.4189  0.0162  -0.0842 61  TRP   A CZ2 
108  C  CZ3 . TRP   A 18  ? 0.9889 0.9734 0.4456 0.3567  0.0323  -0.0603 61  TRP   A CZ3 
109  C  CH2 . TRP   A 18  ? 1.0030 0.9915 0.4188 0.3884  0.0335  -0.0651 61  TRP   A CH2 
110  N  N   . GLU   A 19  ? 1.0688 1.0955 0.4420 0.4449  -0.0135 -0.0535 62  GLU   A N   
111  C  CA  . GLU   A 19  ? 1.1213 1.1498 0.4318 0.4887  -0.0188 -0.0441 62  GLU   A CA  
112  C  C   . GLU   A 19  ? 1.1670 1.1957 0.4290 0.5126  -0.0109 -0.0450 62  GLU   A C   
113  O  O   . GLU   A 19  ? 1.1681 1.1906 0.4286 0.5032  0.0183  -0.0205 62  GLU   A O   
114  C  CB  . GLU   A 19  ? 1.1683 1.1834 0.4629 0.4952  0.0016  -0.0011 62  GLU   A CB  
115  C  CG  . GLU   A 19  ? 1.2313 1.2468 0.5654 0.4822  -0.0117 -0.0052 62  GLU   A CG  
116  C  CD  . GLU   A 19  ? 1.3360 1.3683 0.6624 0.5077  -0.0489 -0.0374 62  GLU   A CD  
117  O  OE1 . GLU   A 19  ? 1.3873 1.4202 0.6539 0.5491  -0.0615 -0.0374 62  GLU   A OE1 
118  O  OE2 . GLU   A 19  ? 1.3392 1.3867 0.7198 0.4871  -0.0652 -0.0633 62  GLU   A OE2 
119  N  N   . LYS   A 20  ? 1.1994 1.2380 0.4245 0.5443  -0.0384 -0.0766 63  LYS   A N   
120  C  CA  . LYS   A 20  ? 1.2466 1.2866 0.4192 0.5729  -0.0330 -0.0820 63  LYS   A CA  
121  C  C   . LYS   A 20  ? 1.2898 1.3259 0.3977 0.6049  -0.0078 -0.0403 63  LYS   A C   
122  O  O   . LYS   A 20  ? 1.3037 1.3344 0.3937 0.6173  -0.0106 -0.0209 63  LYS   A O   
123  C  CB  . LYS   A 20  ? 1.2867 1.3375 0.4363 0.5996  -0.0725 -0.1318 63  LYS   A CB  
124  C  CG  . LYS   A 20  ? 1.3286 1.3890 0.5341 0.5792  -0.1076 -0.1712 63  LYS   A CG  
125  C  CD  . LYS   A 20  ? 1.3946 1.4685 0.5718 0.6120  -0.1483 -0.2197 63  LYS   A CD  
126  C  CE  . LYS   A 20  ? 1.4223 1.5130 0.6595 0.5931  -0.1835 -0.2611 63  LYS   A CE  
127  N  NZ  . LYS   A 20  ? 1.4613 1.5681 0.6728 0.6270  -0.2260 -0.3104 63  LYS   A NZ  
128  N  N   . ASP   A 21  ? 1.3107 1.3487 0.3840 0.6187  0.0178  -0.0260 64  ASP   A N   
129  C  CA  . ASP   A 21  ? 1.3503 1.3856 0.3635 0.6456  0.0493  0.0172  64  ASP   A CA  
130  C  C   . ASP   A 21  ? 1.3446 1.3671 0.3950 0.6145  0.0801  0.0629  64  ASP   A C   
131  O  O   . ASP   A 21  ? 1.3632 1.3718 0.3878 0.6260  0.0850  0.0912  64  ASP   A O   
132  C  CB  . ASP   A 21  ? 1.4115 1.4453 0.3483 0.6941  0.0290  0.0148  64  ASP   A CB  
133  C  CG  . ASP   A 21  ? 1.5026 1.5499 0.3929 0.7313  -0.0019 -0.0307 64  ASP   A CG  
134  O  OD1 . ASP   A 21  ? 1.5260 1.5815 0.3976 0.7406  0.0125  -0.0390 64  ASP   A OD1 
135  O  OD2 . ASP   A 21  ? 1.5335 1.5843 0.4056 0.7536  -0.0417 -0.0596 64  ASP   A OD2 
136  N  N   . ALA   A 22  ? 1.3177 1.3422 0.4292 0.5759  0.0976  0.0676  65  ALA   A N   
137  C  CA  . ALA   A 22  ? 1.3033 1.3179 0.4560 0.5443  0.1261  0.1060  65  ALA   A CA  
138  C  C   . ALA   A 22  ? 1.2964 1.3224 0.4436 0.5432  0.1676  0.1345  65  ALA   A C   
139  O  O   . ALA   A 22  ? 1.2975 1.3401 0.4205 0.5620  0.1709  0.1183  65  ALA   A O   
140  C  CB  . ALA   A 22  ? 1.2795 1.2915 0.5075 0.5019  0.1134  0.0881  65  ALA   A CB  
141  N  N   . GLU   A 23  ? 1.2847 1.3033 0.4562 0.5223  0.1989  0.1748  66  GLU   A N   
142  C  CA  . GLU   A 23  ? 1.2747 1.3102 0.4533 0.5170  0.2400  0.2017  66  GLU   A CA  
143  C  C   . GLU   A 23  ? 1.2375 1.2925 0.4741 0.4931  0.2383  0.1779  66  GLU   A C   
144  O  O   . GLU   A 23  ? 1.2194 1.2683 0.5167 0.4580  0.2332  0.1761  66  GLU   A O   
145  C  CB  . GLU   A 23  ? 1.3039 1.3243 0.5051 0.4954  0.2708  0.2476  66  GLU   A CB  
146  C  CG  . GLU   A 23  ? 1.3664 1.4073 0.5702 0.4931  0.3176  0.2797  66  GLU   A CG  
147  C  CD  . GLU   A 23  ? 1.4225 1.4656 0.7034 0.4498  0.3400  0.3006  66  GLU   A CD  
148  O  OE1 . GLU   A 23  ? 1.4350 1.4508 0.7469 0.4270  0.3284  0.3077  66  GLU   A OE1 
149  O  OE2 . GLU   A 23  ? 1.4218 1.4961 0.7337 0.4402  0.3680  0.3074  66  GLU   A OE2 
150  N  N   . VAL   A 24  ? 1.2260 1.3018 0.4390 0.5154  0.2401  0.1580  67  VAL   A N   
151  C  CA  . VAL   A 24  ? 1.2011 1.2919 0.4588 0.5011  0.2362  0.1343  67  VAL   A CA  
152  C  C   . VAL   A 24  ? 1.1685 1.2857 0.4616 0.4887  0.2753  0.1605  67  VAL   A C   
153  O  O   . VAL   A 24  ? 1.1694 1.3093 0.4290 0.5132  0.3031  0.1738  67  VAL   A O   
154  C  CB  . VAL   A 24  ? 1.2172 1.3146 0.4357 0.5329  0.2160  0.0960  67  VAL   A CB  
155  C  CG1 . VAL   A 24  ? 1.2055 1.3067 0.4708 0.5172  0.2059  0.0708  67  VAL   A CG1 
156  C  CG2 . VAL   A 24  ? 1.2397 1.3171 0.4226 0.5483  0.1781  0.0687  67  VAL   A CG2 
157  N  N   . THR   A 25  ? 1.1310 1.2488 0.4924 0.4519  0.2777  0.1659  68  THR   A N   
158  C  CA  . THR   A 25  ? 1.0989 1.2465 0.5053 0.4377  0.3113  0.1868  68  THR   A CA  
159  C  C   . THR   A 25  ? 1.0708 1.2223 0.5446 0.4086  0.2972  0.1705  68  THR   A C   
160  O  O   . THR   A 25  ? 1.0748 1.2004 0.5602 0.3940  0.2662  0.1513  68  THR   A O   
161  C  CB  . THR   A 25  ? 1.1059 1.2501 0.5212 0.4226  0.3426  0.2299  68  THR   A CB  
162  O  OG1 . THR   A 25  ? 1.0894 1.2708 0.5435 0.4141  0.3795  0.2485  68  THR   A OG1 
163  C  CG2 . THR   A 25  ? 1.1001 1.2159 0.5585 0.3880  0.3269  0.2356  68  THR   A CG2 
164  N  N   . GLY   A 26  ? 1.0396 1.2254 0.5570 0.4015  0.3201  0.1781  69  GLY   A N   
165  C  CA  . GLY   A 26  ? 1.0115 1.2035 0.5907 0.3775  0.3067  0.1645  69  GLY   A CA  
166  C  C   . GLY   A 26  ? 0.9942 1.1991 0.5728 0.3968  0.2925  0.1346  69  GLY   A C   
167  O  O   . GLY   A 26  ? 1.0162 1.2055 0.5464 0.4217  0.2753  0.1131  69  GLY   A O   
168  N  N   . ASN   A 27  ? 0.9528 1.1849 0.5866 0.3863  0.2973  0.1315  70  ASN   A N   
169  C  CA  . ASN   A 27  ? 0.9373 1.1803 0.5752 0.4061  0.2829  0.1041  70  ASN   A CA  
170  C  C   . ASN   A 27  ? 0.9174 1.1235 0.5698 0.3903  0.2452  0.0834  70  ASN   A C   
171  O  O   . ASN   A 27  ? 0.9261 1.1037 0.5848 0.3644  0.2329  0.0898  70  ASN   A O   
172  C  CB  . ASN   A 27  ? 0.9233 1.2237 0.6081 0.4127  0.3108  0.1104  70  ASN   A CB  
173  C  CG  . ASN   A 27  ? 0.9384 1.2597 0.6969 0.3807  0.3153  0.1214  70  ASN   A CG  
174  O  OD1 . ASN   A 27  ? 0.9518 1.2456 0.7261 0.3515  0.3034  0.1301  70  ASN   A OD1 
175  N  ND2 . ASN   A 27  ? 0.9185 1.2925 0.7264 0.3872  0.3318  0.1187  70  ASN   A ND2 
176  N  N   . SER   A 28  ? 0.8934 1.0956 0.5438 0.4085  0.2272  0.0588  71  SER   A N   
177  C  CA  . SER   A 28  ? 0.8885 1.0504 0.5433 0.3968  0.1939  0.0418  71  SER   A CA  
178  C  C   . SER   A 28  ? 0.8449 1.0281 0.5437 0.3995  0.1882  0.0349  71  SER   A C   
179  O  O   . SER   A 28  ? 0.8559 1.0369 0.5441 0.4257  0.1772  0.0155  71  SER   A O   
180  C  CB  . SER   A 28  ? 0.9353 1.0571 0.5400 0.4166  0.1712  0.0171  71  SER   A CB  
181  O  OG  . SER   A 28  ? 0.9817 1.0974 0.5431 0.4276  0.1768  0.0170  71  SER   A OG  
182  N  N   . PRO   A 29  ? 0.7984 1.0022 0.5475 0.3751  0.1930  0.0481  72  PRO   A N   
183  C  CA  . PRO   A 29  ? 0.7640 0.9946 0.5578 0.3810  0.1849  0.0392  72  PRO   A CA  
184  C  C   . PRO   A 29  ? 0.7679 0.9545 0.5533 0.3772  0.1500  0.0252  72  PRO   A C   
185  O  O   . PRO   A 29  ? 0.7846 0.9287 0.5504 0.3551  0.1366  0.0290  72  PRO   A O   
186  C  CB  . PRO   A 29  ? 0.7403 1.0144 0.5943 0.3561  0.2050  0.0576  72  PRO   A CB  
187  C  CG  . PRO   A 29  ? 0.7605 1.0176 0.5953 0.3352  0.2209  0.0781  72  PRO   A CG  
188  C  CD  . PRO   A 29  ? 0.7808 0.9870 0.5508 0.3440  0.2053  0.0698  72  PRO   A CD  
189  N  N   . ARG   A 30  ? 0.7488 0.9462 0.5483 0.4000  0.1362  0.0100  73  ARG   A N   
190  C  CA  . ARG   A 30  ? 0.7668 0.9210 0.5558 0.3992  0.1035  0.0001  73  ARG   A CA  
191  C  C   . ARG   A 30  ? 0.7163 0.9077 0.5615 0.3895  0.0976  0.0023  73  ARG   A C   
192  O  O   . ARG   A 30  ? 0.6845 0.9235 0.5686 0.4101  0.0995  -0.0065 73  ARG   A O   
193  C  CB  . ARG   A 30  ? 0.8228 0.9500 0.5813 0.4340  0.0856  -0.0194 73  ARG   A CB  
194  C  CG  . ARG   A 30  ? 0.9326 0.9947 0.6315 0.4346  0.0747  -0.0260 73  ARG   A CG  
195  C  CD  . ARG   A 30  ? 1.0204 1.0496 0.6925 0.4687  0.0552  -0.0464 73  ARG   A CD  
196  N  NE  . ARG   A 30  ? 1.0971 1.1050 0.7298 0.4836  0.0590  -0.0590 73  ARG   A NE  
197  C  CZ  . ARG   A 30  ? 1.1659 1.1096 0.7576 0.4743  0.0436  -0.0659 73  ARG   A CZ  
198  N  NH1 . ARG   A 30  ? 1.1820 1.0755 0.7639 0.4498  0.0271  -0.0584 73  ARG   A NH1 
199  N  NH2 . ARG   A 30  ? 1.1711 1.1019 0.7318 0.4895  0.0451  -0.0812 73  ARG   A NH2 
200  N  N   . LEU   A 31  ? 0.7058 0.8789 0.5575 0.3594  0.0896  0.0115  74  LEU   A N   
201  C  CA  . LEU   A 31  ? 0.6664 0.8729 0.5707 0.3470  0.0815  0.0114  74  LEU   A CA  
202  C  C   . LEU   A 31  ? 0.6711 0.8356 0.5538 0.3473  0.0479  0.0042  74  LEU   A C   
203  O  O   . LEU   A 31  ? 0.7016 0.8112 0.5387 0.3329  0.0393  0.0093  74  LEU   A O   
204  C  CB  . LEU   A 31  ? 0.6530 0.8744 0.5846 0.3125  0.0996  0.0268  74  LEU   A CB  
205  C  CG  . LEU   A 31  ? 0.6511 0.9030 0.5944 0.3080  0.1348  0.0405  74  LEU   A CG  
206  C  CD1 . LEU   A 31  ? 0.6594 0.8964 0.6042 0.2768  0.1458  0.0563  74  LEU   A CD1 
207  C  CD2 . LEU   A 31  ? 0.6153 0.9379 0.6217 0.3162  0.1542  0.0398  74  LEU   A CD2 
208  N  N   . ASP   A 32  ? 0.6367 0.8307 0.5542 0.3625  0.0297  -0.0071 75  ASP   A N   
209  C  CA  . ASP   A 32  ? 0.6505 0.8086 0.5459 0.3659  -0.0032 -0.0127 75  ASP   A CA  
210  C  C   . ASP   A 32  ? 0.6151 0.7842 0.5364 0.3341  -0.0047 -0.0078 75  ASP   A C   
211  O  O   . ASP   A 32  ? 0.5785 0.8071 0.5659 0.3266  0.0014  -0.0123 75  ASP   A O   
212  C  CB  . ASP   A 32  ? 0.6704 0.8641 0.5983 0.3980  -0.0240 -0.0290 75  ASP   A CB  
213  C  CG  . ASP   A 32  ? 0.7915 0.9542 0.6802 0.4348  -0.0348 -0.0370 75  ASP   A CG  
214  O  OD1 . ASP   A 32  ? 0.8556 0.9440 0.6775 0.4358  -0.0451 -0.0316 75  ASP   A OD1 
215  O  OD2 . ASP   A 32  ? 0.8065 1.0195 0.7341 0.4627  -0.0331 -0.0500 75  ASP   A OD2 
216  N  N   . VAL   A 33  ? 0.6214 0.7364 0.4956 0.3142  -0.0104 0.0001  76  VAL   A N   
217  C  CA  . VAL   A 33  ? 0.5962 0.7206 0.4931 0.2861  -0.0116 0.0021  76  VAL   A CA  
218  C  C   . VAL   A 33  ? 0.6133 0.6941 0.4672 0.2859  -0.0396 -0.0015 76  VAL   A C   
219  O  O   . VAL   A 33  ? 0.6412 0.6762 0.4417 0.3039  -0.0545 -0.0007 76  VAL   A O   
220  C  CB  . VAL   A 33  ? 0.5953 0.7136 0.4917 0.2580  0.0155  0.0152  76  VAL   A CB  
221  C  CG1 . VAL   A 33  ? 0.5691 0.7307 0.5034 0.2595  0.0437  0.0214  76  VAL   A CG1 
222  C  CG2 . VAL   A 33  ? 0.6386 0.6961 0.4685 0.2526  0.0169  0.0224  76  VAL   A CG2 
223  N  N   . ALA   A 34  ? 0.5959 0.6908 0.4731 0.2672  -0.0469 -0.0059 77  ALA   A N   
224  C  CA  . ALA   A 34  ? 0.6212 0.6800 0.4562 0.2664  -0.0709 -0.0099 77  ALA   A CA  
225  C  C   . ALA   A 34  ? 0.6167 0.6682 0.4532 0.2360  -0.0603 -0.0071 77  ALA   A C   
226  O  O   . ALA   A 34  ? 0.5911 0.6806 0.4838 0.2188  -0.0467 -0.0088 77  ALA   A O   
227  C  CB  . ALA   A 34  ? 0.6021 0.6939 0.4675 0.2847  -0.1011 -0.0270 77  ALA   A CB  
228  N  N   . LEU   A 35  ? 0.6432 0.6448 0.4185 0.2296  -0.0647 -0.0023 78  LEU   A N   
229  C  CA  . LEU   A 35  ? 0.6371 0.6293 0.4082 0.2043  -0.0549 -0.0016 78  LEU   A CA  
230  C  C   . LEU   A 35  ? 0.6470 0.6313 0.3984 0.2060  -0.0789 -0.0137 78  LEU   A C   
231  O  O   . LEU   A 35  ? 0.6811 0.6287 0.3727 0.2202  -0.0937 -0.0115 78  LEU   A O   
232  C  CB  . LEU   A 35  ? 0.6612 0.6091 0.3815 0.1940  -0.0360 0.0118  78  LEU   A CB  
233  C  CG  . LEU   A 35  ? 0.6651 0.6041 0.3798 0.1706  -0.0238 0.0120  78  LEU   A CG  
234  C  CD1 . LEU   A 35  ? 0.6395 0.6112 0.4087 0.1567  -0.0070 0.0129  78  LEU   A CD1 
235  C  CD2 . LEU   A 35  ? 0.6932 0.5897 0.3551 0.1634  -0.0107 0.0218  78  LEU   A CD2 
236  N  N   . ASP   A 36  ? 0.6161 0.6327 0.4159 0.1927  -0.0835 -0.0268 79  ASP   A N   
237  C  CA  . ASP   A 36  ? 0.6237 0.6368 0.4076 0.1954  -0.1081 -0.0429 79  ASP   A CA  
238  C  C   . ASP   A 36  ? 0.6594 0.6346 0.3908 0.1813  -0.0981 -0.0397 79  ASP   A C   
239  O  O   . ASP   A 36  ? 0.6631 0.6223 0.3852 0.1664  -0.0723 -0.0269 79  ASP   A O   
240  C  CB  . ASP   A 36  ? 0.6003 0.6647 0.4636 0.1884  -0.1215 -0.0631 79  ASP   A CB  
241  C  CG  . ASP   A 36  ? 0.6459 0.7235 0.5579 0.1604  -0.1015 -0.0637 79  ASP   A CG  
242  O  OD1 . ASP   A 36  ? 0.6861 0.7349 0.5676 0.1483  -0.0791 -0.0502 79  ASP   A OD1 
243  O  OD2 . ASP   A 36  ? 0.6314 0.7470 0.6134 0.1509  -0.1091 -0.0782 79  ASP   A OD2 
244  N  N   . GLU   A 37  ? 0.6793 0.6439 0.3772 0.1881  -0.1194 -0.0534 80  GLU   A N   
245  C  CA  . GLU   A 37  ? 0.7131 0.6488 0.3616 0.1783  -0.1116 -0.0544 80  GLU   A CA  
246  C  C   . GLU   A 37  ? 0.6918 0.6412 0.3836 0.1542  -0.0930 -0.0595 80  GLU   A C   
247  O  O   . GLU   A 37  ? 0.7122 0.6398 0.3693 0.1447  -0.0780 -0.0568 80  GLU   A O   
248  C  CB  . GLU   A 37  ? 0.7679 0.6998 0.3809 0.1940  -0.1416 -0.0728 80  GLU   A CB  
249  C  CG  . GLU   A 37  ? 0.8870 0.7823 0.4245 0.1923  -0.1331 -0.0700 80  GLU   A CG  
250  C  CD  . GLU   A 37  ? 0.9876 0.8836 0.4912 0.2086  -0.1625 -0.0918 80  GLU   A CD  
251  O  OE1 . GLU   A 37  ? 0.9772 0.9020 0.5285 0.2023  -0.1758 -0.1170 80  GLU   A OE1 
252  O  OE2 . GLU   A 37  ? 1.0548 0.9202 0.4826 0.2287  -0.1732 -0.0840 80  GLU   A OE2 
253  N  N   . SER   A 38  ? 0.6445 0.6288 0.4121 0.1447  -0.0919 -0.0654 81  SER   A N   
254  C  CA  . SER   A 38  ? 0.6199 0.6112 0.4286 0.1237  -0.0747 -0.0671 81  SER   A CA  
255  C  C   . SER   A 38  ? 0.6121 0.5982 0.4293 0.1145  -0.0447 -0.0450 81  SER   A C   
256  O  O   . SER   A 38  ? 0.6082 0.5971 0.4560 0.1001  -0.0300 -0.0430 81  SER   A O   
257  C  CB  . SER   A 38  ? 0.5884 0.6143 0.4738 0.1157  -0.0878 -0.0838 81  SER   A CB  
258  O  OG  . SER   A 38  ? 0.6101 0.6427 0.4876 0.1263  -0.1194 -0.1082 81  SER   A OG  
259  N  N   . GLY   A 39  ? 0.6089 0.5851 0.3970 0.1246  -0.0378 -0.0297 82  GLY   A N   
260  C  CA  . GLY   A 39  ? 0.6008 0.5731 0.3928 0.1195  -0.0134 -0.0122 82  GLY   A CA  
261  C  C   . GLY   A 39  ? 0.5644 0.5692 0.4166 0.1178  -0.0052 -0.0066 82  GLY   A C   
262  O  O   . GLY   A 39  ? 0.5588 0.5640 0.4202 0.1124  0.0155  0.0062  82  GLY   A O   
263  N  N   . ASP   A 40  ? 0.5325 0.5672 0.4261 0.1233  -0.0207 -0.0163 83  ASP   A N   
264  C  CA  . ASP   A 40  ? 0.4916 0.5631 0.4473 0.1203  -0.0097 -0.0109 83  ASP   A CA  
265  C  C   . ASP   A 40  ? 0.4859 0.5714 0.4360 0.1405  -0.0115 -0.0059 83  ASP   A C   
266  O  O   . ASP   A 40  ? 0.4917 0.5774 0.4251 0.1567  -0.0344 -0.0161 83  ASP   A O   
267  C  CB  . ASP   A 40  ? 0.4638 0.5673 0.4843 0.1105  -0.0239 -0.0276 83  ASP   A CB  
268  C  CG  . ASP   A 40  ? 0.5006 0.5890 0.5328 0.0920  -0.0242 -0.0357 83  ASP   A CG  
269  O  OD1 . ASP   A 40  ? 0.5225 0.5877 0.5355 0.0838  -0.0051 -0.0232 83  ASP   A OD1 
270  O  OD2 . ASP   A 40  ? 0.5246 0.6246 0.5853 0.0877  -0.0458 -0.0568 83  ASP   A OD2 
271  N  N   . PHE   A 41  ? 0.4756 0.5721 0.4375 0.1424  0.0114  0.0088  84  PHE   A N   
272  C  CA  . PHE   A 41  ? 0.4781 0.5911 0.4395 0.1634  0.0118  0.0114  84  PHE   A CA  
273  C  C   . PHE   A 41  ? 0.4612 0.6299 0.4959 0.1652  0.0099  0.0037  84  PHE   A C   
274  O  O   . PHE   A 41  ? 0.4283 0.6221 0.5185 0.1458  0.0187  0.0029  84  PHE   A O   
275  C  CB  . PHE   A 41  ? 0.4724 0.5751 0.4110 0.1676  0.0365  0.0273  84  PHE   A CB  
276  C  CG  . PHE   A 41  ? 0.5018 0.5557 0.3742 0.1688  0.0366  0.0318  84  PHE   A CG  
277  C  CD1 . PHE   A 41  ? 0.5290 0.5553 0.3560 0.1854  0.0230  0.0289  84  PHE   A CD1 
278  C  CD2 . PHE   A 41  ? 0.5139 0.5489 0.3723 0.1530  0.0499  0.0386  84  PHE   A CD2 
279  C  CE1 . PHE   A 41  ? 0.5685 0.5505 0.3416 0.1822  0.0254  0.0331  84  PHE   A CE1 
280  C  CE2 . PHE   A 41  ? 0.5480 0.5453 0.3549 0.1522  0.0506  0.0403  84  PHE   A CE2 
281  C  CZ  . PHE   A 41  ? 0.5683 0.5397 0.3347 0.1646  0.0394  0.0376  84  PHE   A CZ  
282  N  N   . SER   A 42  ? 0.4791 0.6669 0.5167 0.1886  -0.0018 -0.0030 85  SER   A N   
283  C  CA  . SER   A 42  ? 0.4671 0.7154 0.5779 0.1937  -0.0035 -0.0128 85  SER   A CA  
284  C  C   . SER   A 42  ? 0.4996 0.7625 0.6005 0.2224  -0.0006 -0.0117 85  SER   A C   
285  O  O   . SER   A 42  ? 0.5346 0.7567 0.5725 0.2421  -0.0139 -0.0114 85  SER   A O   
286  C  CB  . SER   A 42  ? 0.4733 0.7395 0.6124 0.1955  -0.0372 -0.0351 85  SER   A CB  
287  O  OG  . SER   A 42  ? 0.5334 0.7698 0.6147 0.2209  -0.0662 -0.0431 85  SER   A OG  
288  N  N   . LEU   A 43  ? 0.4854 0.8040 0.6473 0.2244  0.0191  -0.0107 86  LEU   A N   
289  C  CA  . LEU   A 43  ? 0.5109 0.8492 0.6677 0.2542  0.0237  -0.0125 86  LEU   A CA  
290  C  C   . LEU   A 43  ? 0.5246 0.8855 0.6983 0.2804  -0.0097 -0.0336 86  LEU   A C   
291  O  O   . LEU   A 43  ? 0.4865 0.8968 0.7275 0.2749  -0.0221 -0.0486 86  LEU   A O   
292  C  CB  . LEU   A 43  ? 0.4806 0.8759 0.6960 0.2491  0.0595  -0.0041 86  LEU   A CB  
293  C  CG  . LEU   A 43  ? 0.5296 0.9017 0.7114 0.2386  0.0937  0.0184  86  LEU   A CG  
294  C  CD1 . LEU   A 43  ? 0.5007 0.9311 0.7416 0.2320  0.1304  0.0287  86  LEU   A CD1 
295  C  CD2 . LEU   A 43  ? 0.5820 0.9120 0.6888 0.2640  0.0913  0.0206  86  LEU   A CD2 
296  N  N   . VAL   A 44  ? 0.5755 0.8997 0.6900 0.3100  -0.0252 -0.0357 87  VAL   A N   
297  C  CA  . VAL   A 44  ? 0.5924 0.9295 0.7107 0.3431  -0.0580 -0.0537 87  VAL   A CA  
298  C  C   . VAL   A 44  ? 0.5926 0.9804 0.7494 0.3671  -0.0418 -0.0588 87  VAL   A C   
299  O  O   . VAL   A 44  ? 0.6193 0.9868 0.7419 0.3727  -0.0184 -0.0475 87  VAL   A O   
300  C  CB  . VAL   A 44  ? 0.6547 0.9130 0.6807 0.3624  -0.0816 -0.0499 87  VAL   A CB  
301  C  CG1 . VAL   A 44  ? 0.6581 0.9229 0.6815 0.4009  -0.1173 -0.0664 87  VAL   A CG1 
302  C  CG2 . VAL   A 44  ? 0.6922 0.8997 0.6730 0.3376  -0.0898 -0.0423 87  VAL   A CG2 
303  N  N   . GLU   A 45  ? 0.5572 1.0149 0.7872 0.3818  -0.0535 -0.0778 88  GLU   A N   
304  C  CA  . GLU   A 45  ? 0.5445 1.0584 0.8157 0.4067  -0.0358 -0.0849 88  GLU   A CA  
305  C  C   . GLU   A 45  ? 0.5405 1.0753 0.8220 0.4514  -0.0714 -0.1082 88  GLU   A C   
306  O  O   . GLU   A 45  ? 0.5545 1.0774 0.8056 0.4852  -0.0706 -0.1113 88  GLU   A O   
307  C  CB  . GLU   A 45  ? 0.5241 1.1198 0.8897 0.3811  -0.0008 -0.0833 88  GLU   A CB  
308  C  CG  . GLU   A 45  ? 0.5983 1.1707 0.9473 0.3450  0.0375  -0.0576 88  GLU   A CG  
309  C  CD  . GLU   A 45  ? 0.6964 1.2402 0.9865 0.3604  0.0635  -0.0435 88  GLU   A CD  
310  O  OE1 . GLU   A 45  ? 0.7344 1.2138 0.9577 0.3471  0.0696  -0.0274 88  GLU   A OE1 
311  O  OE2 . GLU   A 45  ? 0.6942 1.2819 1.0056 0.3881  0.0758  -0.0517 88  GLU   A OE2 
312  N  N   . THR   B 9   ? 0.6131 0.6754 0.5939 0.1978  0.0577  0.0128  18  THR   B N   
313  C  CA  . THR   B 9   ? 0.6276 0.6896 0.6063 0.1808  0.0475  0.0081  18  THR   B CA  
314  C  C   . THR   B 9   ? 0.6159 0.6863 0.5923 0.1798  0.0316  0.0070  18  THR   B C   
315  O  O   . THR   B 9   ? 0.6217 0.6938 0.5988 0.1657  0.0225  0.0034  18  THR   B O   
316  C  CB  . THR   B 9   ? 0.6551 0.7313 0.6451 0.1693  0.0502  0.0064  18  THR   B CB  
317  O  OG1 . THR   B 9   ? 0.6633 0.7661 0.6681 0.1774  0.0519  0.0099  18  THR   B OG1 
318  C  CG2 . THR   B 9   ? 0.6733 0.7341 0.6585 0.1647  0.0625  0.0040  18  THR   B CG2 
319  N  N   . THR   B 10  ? 0.5970 0.6712 0.5694 0.1947  0.0279  0.0100  19  THR   B N   
320  C  CA  . THR   B 10  ? 0.5834 0.6642 0.5503 0.1958  0.0119  0.0075  19  THR   B CA  
321  C  C   . THR   B 10  ? 0.5744 0.6314 0.5243 0.1893  0.0063  0.0038  19  THR   B C   
322  O  O   . THR   B 10  ? 0.5816 0.6210 0.5228 0.1930  0.0152  0.0062  19  THR   B O   
323  C  CB  . THR   B 10  ? 0.6025 0.6928 0.5663 0.2165  0.0111  0.0123  19  THR   B CB  
324  O  OG1 . THR   B 10  ? 0.6030 0.7174 0.5825 0.2242  0.0159  0.0163  19  THR   B OG1 
325  C  CG2 . THR   B 10  ? 0.6089 0.7036 0.5626 0.2200  -0.0057 0.0085  19  THR   B CG2 
326  N  N   . ASP   B 11  ? 0.5596 0.6156 0.5047 0.1801  -0.0084 -0.0018 20  ASP   B N   
327  C  CA  . ASP   B 11  ? 0.5604 0.5938 0.4873 0.1766  -0.0147 -0.0054 20  ASP   B CA  
328  C  C   . ASP   B 11  ? 0.5493 0.5731 0.4606 0.1946  -0.0122 -0.0019 20  ASP   B C   
329  O  O   . ASP   B 11  ? 0.5460 0.5823 0.4587 0.2089  -0.0123 0.0013  20  ASP   B O   
330  C  CB  . ASP   B 11  ? 0.5924 0.6266 0.5155 0.1683  -0.0326 -0.0122 20  ASP   B CB  
331  C  CG  . ASP   B 11  ? 0.6729 0.6997 0.6002 0.1480  -0.0362 -0.0153 20  ASP   B CG  
332  O  OD1 . ASP   B 11  ? 0.6736 0.7147 0.6187 0.1378  -0.0301 -0.0128 20  ASP   B OD1 
333  O  OD2 . ASP   B 11  ? 0.7194 0.7258 0.6314 0.1432  -0.0450 -0.0197 20  ASP   B OD2 
334  N  N   . GLY   B 12  ? 0.5395 0.5439 0.4369 0.1946  -0.0094 -0.0014 21  GLY   B N   
335  C  CA  . GLY   B 12  ? 0.5350 0.5328 0.4189 0.2110  -0.0061 0.0035  21  GLY   B CA  
336  C  C   . GLY   B 12  ? 0.5402 0.5245 0.4202 0.2095  0.0054  0.0082  21  GLY   B C   
337  O  O   . GLY   B 12  ? 0.5433 0.5218 0.4288 0.1957  0.0096  0.0063  21  GLY   B O   
338  N  N   . VAL   B 13  ? 0.5397 0.5206 0.4104 0.2236  0.0101  0.0148  22  VAL   B N   
339  C  CA  . VAL   B 13  ? 0.5384 0.5101 0.4077 0.2219  0.0207  0.0204  22  VAL   B CA  
340  C  C   . VAL   B 13  ? 0.5259 0.4999 0.4086 0.2244  0.0349  0.0277  22  VAL   B C   
341  O  O   . VAL   B 13  ? 0.5196 0.5016 0.4062 0.2358  0.0371  0.0318  22  VAL   B O   
342  C  CB  . VAL   B 13  ? 0.5628 0.5296 0.4144 0.2339  0.0178  0.0241  22  VAL   B CB  
343  C  CG1 . VAL   B 13  ? 0.5688 0.5436 0.4140 0.2540  0.0182  0.0307  22  VAL   B CG1 
344  C  CG2 . VAL   B 13  ? 0.5744 0.5355 0.4270 0.2292  0.0272  0.0298  22  VAL   B CG2 
345  N  N   . TYR   B 14  ? 0.5182 0.4847 0.4080 0.2130  0.0439  0.0284  23  TYR   B N   
346  C  CA  . TYR   B 14  ? 0.5057 0.4691 0.4074 0.2125  0.0567  0.0331  23  TYR   B CA  
347  C  C   . TYR   B 14  ? 0.5101 0.4647 0.4125 0.2086  0.0654  0.0388  23  TYR   B C   
348  O  O   . TYR   B 14  ? 0.5143 0.4669 0.4116 0.2008  0.0623  0.0368  23  TYR   B O   
349  C  CB  . TYR   B 14  ? 0.4972 0.4602 0.4090 0.1997  0.0591  0.0257  23  TYR   B CB  
350  C  CG  . TYR   B 14  ? 0.4865 0.4619 0.4039 0.2033  0.0542  0.0225  23  TYR   B CG  
351  C  CD1 . TYR   B 14  ? 0.4876 0.4712 0.4006 0.2010  0.0414  0.0174  23  TYR   B CD1 
352  C  CD2 . TYR   B 14  ? 0.4924 0.4710 0.4200 0.2078  0.0624  0.0241  23  TYR   B CD2 
353  C  CE1 . TYR   B 14  ? 0.4889 0.4873 0.4095 0.2027  0.0361  0.0150  23  TYR   B CE1 
354  C  CE2 . TYR   B 14  ? 0.4948 0.4894 0.4292 0.2119  0.0581  0.0223  23  TYR   B CE2 
355  C  CZ  . TYR   B 14  ? 0.4974 0.5036 0.4296 0.2081  0.0446  0.0177  23  TYR   B CZ  
356  O  OH  . TYR   B 14  ? 0.4988 0.5241 0.4401 0.2101  0.0392  0.0162  23  TYR   B OH  
357  N  N   . ARG   B 15  ? 0.5042 0.4538 0.4140 0.2134  0.0763  0.0464  24  ARG   B N   
358  C  CA  . ARG   B 15  ? 0.5068 0.4482 0.4210 0.2068  0.0847  0.0519  24  ARG   B CA  
359  C  C   . ARG   B 15  ? 0.5086 0.4404 0.4309 0.1906  0.0890  0.0435  24  ARG   B C   
360  O  O   . ARG   B 15  ? 0.4964 0.4261 0.4227 0.1904  0.0906  0.0382  24  ARG   B O   
361  C  CB  . ARG   B 15  ? 0.5227 0.4601 0.4415 0.2184  0.0949  0.0645  24  ARG   B CB  
362  C  CG  . ARG   B 15  ? 0.5532 0.5008 0.4630 0.2359  0.0927  0.0746  24  ARG   B CG  
363  C  CD  . ARG   B 15  ? 0.5909 0.5339 0.5062 0.2461  0.1046  0.0891  24  ARG   B CD  
364  N  NE  . ARG   B 15  ? 0.6148 0.5692 0.5201 0.2671  0.1024  0.0976  24  ARG   B NE  
365  C  CZ  . ARG   B 15  ? 0.6239 0.5873 0.5205 0.2766  0.1017  0.1062  24  ARG   B CZ  
366  N  NH1 . ARG   B 15  ? 0.6080 0.5720 0.5072 0.2669  0.1039  0.1092  24  ARG   B NH1 
367  N  NH2 . ARG   B 15  ? 0.6171 0.5910 0.5021 0.2969  0.0988  0.1122  24  ARG   B NH2 
368  N  N   . VAL   B 16  ? 0.5146 0.4424 0.4387 0.1781  0.0906  0.0424  25  VAL   B N   
369  C  CA  . VAL   B 16  ? 0.5265 0.4450 0.4559 0.1631  0.0942  0.0341  25  VAL   B CA  
370  C  C   . VAL   B 16  ? 0.5406 0.4480 0.4781 0.1594  0.1035  0.0408  25  VAL   B C   
371  O  O   . VAL   B 16  ? 0.5368 0.4490 0.4760 0.1566  0.1037  0.0479  25  VAL   B O   
372  C  CB  . VAL   B 16  ? 0.5333 0.4577 0.4577 0.1507  0.0871  0.0268  25  VAL   B CB  
373  C  CG1 . VAL   B 16  ? 0.5362 0.4520 0.4644 0.1364  0.0907  0.0179  25  VAL   B CG1 
374  C  CG2 . VAL   B 16  ? 0.5374 0.4704 0.4541 0.1538  0.0780  0.0219  25  VAL   B CG2 
375  N  N   . MET   B 17  ? 0.5580 0.4504 0.5006 0.1603  0.1113  0.0395  26  MET   B N   
376  C  CA  . MET   B 17  ? 0.5849 0.4613 0.5354 0.1573  0.1208  0.0462  26  MET   B CA  
377  C  C   . MET   B 17  ? 0.6273 0.4862 0.5809 0.1420  0.1241  0.0354  26  MET   B C   
378  O  O   . MET   B 17  ? 0.6377 0.4967 0.5865 0.1378  0.1209  0.0233  26  MET   B O   
379  C  CB  . MET   B 17  ? 0.5884 0.4565 0.5402 0.1738  0.1282  0.0542  26  MET   B CB  
380  C  CG  . MET   B 17  ? 0.5929 0.4785 0.5394 0.1914  0.1240  0.0620  26  MET   B CG  
381  S  SD  . MET   B 17  ? 0.6277 0.5239 0.5739 0.1976  0.1248  0.0780  26  MET   B SD  
382  C  CE  . MET   B 17  ? 0.6387 0.5131 0.5962 0.1951  0.1392  0.0895  26  MET   B CE  
383  N  N   . THR   B 18  ? 0.6545 0.4979 0.6158 0.1339  0.1306  0.0401  27  THR   B N   
384  C  CA  . THR   B 18  ? 0.6903 0.5124 0.6535 0.1196  0.1336  0.0293  27  THR   B CA  
385  C  C   . THR   B 18  ? 0.7277 0.5235 0.6985 0.1188  0.1439  0.0368  27  THR   B C   
386  O  O   . THR   B 18  ? 0.7224 0.5206 0.7004 0.1231  0.1482  0.0523  27  THR   B O   
387  C  CB  . THR   B 18  ? 0.7050 0.5366 0.6689 0.1014  0.1263  0.0215  27  THR   B CB  
388  O  OG1 . THR   B 18  ? 0.7369 0.5504 0.6972 0.0905  0.1269  0.0066  27  THR   B OG1 
389  C  CG2 . THR   B 18  ? 0.7011 0.5376 0.6761 0.0920  0.1272  0.0324  27  THR   B CG2 
390  N  N   . ARG   B 19  ? 0.7619 0.5311 0.7300 0.1139  0.1483  0.0261  28  ARG   B N   
391  C  CA  . ARG   B 19  ? 0.7992 0.5371 0.7729 0.1117  0.1579  0.0315  28  ARG   B CA  
392  C  C   . ARG   B 19  ? 0.8219 0.5417 0.8003 0.0883  0.1561  0.0222  28  ARG   B C   
393  O  O   . ARG   B 19  ? 0.8294 0.5200 0.8133 0.0827  0.1632  0.0259  28  ARG   B O   
394  C  CB  . ARG   B 19  ? 0.8363 0.5521 0.8024 0.1276  0.1657  0.0284  28  ARG   B CB  
395  C  CG  . ARG   B 19  ? 0.8870 0.6218 0.8510 0.1500  0.1673  0.0393  28  ARG   B CG  
396  C  CD  . ARG   B 19  ? 0.9500 0.6615 0.9137 0.1663  0.1788  0.0489  28  ARG   B CD  
397  N  NE  . ARG   B 19  ? 0.9928 0.7252 0.9537 0.1885  0.1791  0.0577  28  ARG   B NE  
398  C  CZ  . ARG   B 19  ? 1.0248 0.7661 0.9793 0.2006  0.1779  0.0502  28  ARG   B CZ  
399  N  NH1 . ARG   B 19  ? 1.0187 0.7499 0.9677 0.1940  0.1773  0.0342  28  ARG   B NH1 
400  N  NH2 . ARG   B 19  ? 1.0201 0.7825 0.9738 0.2193  0.1770  0.0588  28  ARG   B NH2 
401  N  N   . ARG   B 20  ? 0.8274 0.5650 0.8036 0.0746  0.1462  0.0110  29  ARG   B N   
402  C  CA  . ARG   B 20  ? 0.8417 0.5717 0.8211 0.0518  0.1411  0.0000  29  ARG   B CA  
403  C  C   . ARG   B 20  ? 0.8352 0.5644 0.8320 0.0381  0.1429  0.0134  29  ARG   B C   
404  O  O   . ARG   B 20  ? 0.8408 0.5494 0.8431 0.0200  0.1424  0.0069  29  ARG   B O   
405  C  CB  . ARG   B 20  ? 0.8627 0.6224 0.8362 0.0456  0.1300  -0.0098 29  ARG   B CB  
406  C  CG  . ARG   B 20  ? 0.9264 0.6835 0.9004 0.0237  0.1228  -0.0235 29  ARG   B CG  
407  C  CD  . ARG   B 20  ? 0.9740 0.7634 0.9421 0.0199  0.1126  -0.0297 29  ARG   B CD  
408  N  NE  . ARG   B 20  ? 1.0060 0.8259 0.9848 0.0179  0.1087  -0.0155 29  ARG   B NE  
409  C  CZ  . ARG   B 20  ? 1.0336 0.8677 1.0225 0.0012  0.1031  -0.0142 29  ARG   B CZ  
410  N  NH1 . ARG   B 20  ? 1.0379 0.8577 1.0281 -0.0169 0.0996  -0.0272 29  ARG   B NH1 
411  N  NH2 . ARG   B 20  ? 1.0162 0.8798 1.0138 0.0029  0.1007  -0.0002 29  ARG   B NH2 
412  N  N   . LEU   B 21  ? 0.8203 0.5720 0.8255 0.0470  0.1451  0.0323  30  LEU   B N   
413  C  CA  . LEU   B 21  ? 0.8101 0.5678 0.8330 0.0365  0.1481  0.0485  30  LEU   B CA  
414  C  C   . LEU   B 21  ? 0.8115 0.5464 0.8403 0.0474  0.1609  0.0652  30  LEU   B C   
415  O  O   . LEU   B 21  ? 0.8285 0.5331 0.8486 0.0563  0.1668  0.0597  30  LEU   B O   
416  C  CB  . LEU   B 21  ? 0.7969 0.5971 0.8239 0.0398  0.1424  0.0588  30  LEU   B CB  
417  C  CG  . LEU   B 21  ? 0.8120 0.6348 0.8347 0.0285  0.1306  0.0453  30  LEU   B CG  
418  C  CD1 . LEU   B 21  ? 0.8247 0.6588 0.8304 0.0436  0.1258  0.0368  30  LEU   B CD1 
419  C  CD2 . LEU   B 21  ? 0.8050 0.6615 0.8400 0.0220  0.1269  0.0578  30  LEU   B CD2 
420  N  N   . LEU   B 22  ? 0.7896 0.5389 0.8326 0.0474  0.1658  0.0863  31  LEU   B N   
421  C  CA  . LEU   B 22  ? 0.7837 0.5144 0.8321 0.0587  0.1784  0.1048  31  LEU   B CA  
422  C  C   . LEU   B 22  ? 0.7715 0.5137 0.8070 0.0873  0.1813  0.1114  31  LEU   B C   
423  O  O   . LEU   B 22  ? 0.7651 0.5409 0.7964 0.0968  0.1755  0.1145  31  LEU   B O   
424  C  CB  . LEU   B 22  ? 0.7718 0.5196 0.8397 0.0497  0.1827  0.1262  31  LEU   B CB  
425  C  CG  . LEU   B 22  ? 0.7911 0.5150 0.8675 0.0557  0.1967  0.1461  31  LEU   B CG  
426  C  CD1 . LEU   B 22  ? 0.8007 0.4861 0.8885 0.0319  0.2000  0.1418  31  LEU   B CD1 
427  C  CD2 . LEU   B 22  ? 0.7868 0.5420 0.8749 0.0626  0.2021  0.1715  31  LEU   B CD2 
428  N  N   . GLY   B 23  ? 0.7672 0.4811 0.7959 0.1010  0.1896  0.1127  32  GLY   B N   
429  C  CA  . GLY   B 23  ? 0.7602 0.4838 0.7771 0.1281  0.1920  0.1181  32  GLY   B CA  
430  C  C   . GLY   B 23  ? 0.7434 0.4894 0.7478 0.1346  0.1812  0.1024  32  GLY   B C   
431  O  O   . GLY   B 23  ? 0.7417 0.4827 0.7421 0.1219  0.1746  0.0840  32  GLY   B O   
432  N  N   . SER   B 24  ? 0.7271 0.4983 0.7249 0.1541  0.1790  0.1101  33  SER   B N   
433  C  CA  . SER   B 24  ? 0.7163 0.5102 0.7034 0.1601  0.1683  0.0977  33  SER   B CA  
434  C  C   . SER   B 24  ? 0.6921 0.5165 0.6806 0.1559  0.1606  0.1021  33  SER   B C   
435  O  O   . SER   B 24  ? 0.6851 0.5262 0.6725 0.1698  0.1621  0.1164  33  SER   B O   
436  C  CB  . SER   B 24  ? 0.7323 0.5325 0.7104 0.1842  0.1697  0.1018  33  SER   B CB  
437  O  OG  . SER   B 24  ? 0.7693 0.5437 0.7455 0.1907  0.1773  0.0986  33  SER   B OG  
438  N  N   . THR   B 25  ? 0.6759 0.5076 0.6657 0.1383  0.1528  0.0902  34  THR   B N   
439  C  CA  . THR   B 25  ? 0.6583 0.5182 0.6489 0.1353  0.1460  0.0945  34  THR   B CA  
440  C  C   . THR   B 25  ? 0.6454 0.5225 0.6225 0.1432  0.1358  0.0843  34  THR   B C   
441  O  O   . THR   B 25  ? 0.6581 0.5280 0.6295 0.1388  0.1317  0.0693  34  THR   B O   
442  C  CB  . THR   B 25  ? 0.6692 0.5305 0.6712 0.1123  0.1442  0.0919  34  THR   B CB  
443  O  OG1 . THR   B 25  ? 0.6890 0.5332 0.7047 0.1047  0.1538  0.1032  34  THR   B OG1 
444  C  CG2 . THR   B 25  ? 0.6582 0.5505 0.6613 0.1112  0.1382  0.0980  34  THR   B CG2 
445  N  N   . GLN   B 26  ? 0.6184 0.5174 0.5898 0.1556  0.1319  0.0927  35  GLN   B N   
446  C  CA  . GLN   B 26  ? 0.5998 0.5124 0.5580 0.1624  0.1217  0.0837  35  GLN   B CA  
447  C  C   . GLN   B 26  ? 0.5936 0.5186 0.5513 0.1493  0.1145  0.0775  35  GLN   B C   
448  O  O   . GLN   B 26  ? 0.5968 0.5365 0.5577 0.1491  0.1147  0.0872  35  GLN   B O   
449  C  CB  . GLN   B 26  ? 0.5869 0.5136 0.5360 0.1831  0.1199  0.0938  35  GLN   B CB  
450  C  CG  . GLN   B 26  ? 0.5828 0.5184 0.5184 0.1890  0.1087  0.0832  35  GLN   B CG  
451  C  CD  . GLN   B 26  ? 0.5809 0.5284 0.5050 0.2088  0.1053  0.0905  35  GLN   B CD  
452  O  OE1 . GLN   B 26  ? 0.5884 0.5343 0.5116 0.2228  0.1098  0.0982  35  GLN   B OE1 
453  N  NE2 . GLN   B 26  ? 0.5548 0.5135 0.4681 0.2115  0.0968  0.0877  35  GLN   B NE2 
454  N  N   . VAL   B 27  ? 0.5824 0.5031 0.5359 0.1392  0.1087  0.0624  36  VAL   B N   
455  C  CA  . VAL   B 27  ? 0.5683 0.5004 0.5201 0.1270  0.1019  0.0560  36  VAL   B CA  
456  C  C   . VAL   B 27  ? 0.5602 0.5068 0.4986 0.1363  0.0930  0.0544  36  VAL   B C   
457  O  O   . VAL   B 27  ? 0.5610 0.5203 0.4967 0.1316  0.0882  0.0544  36  VAL   B O   
458  C  CB  . VAL   B 27  ? 0.5714 0.4917 0.5246 0.1112  0.1008  0.0412  36  VAL   B CB  
459  C  CG1 . VAL   B 27  ? 0.5806 0.4834 0.5453 0.1013  0.1086  0.0419  36  VAL   B CG1 
460  C  CG2 . VAL   B 27  ? 0.5730 0.4858 0.5174 0.1167  0.0987  0.0311  36  VAL   B CG2 
461  N  N   . GLY   B 28  ? 0.5506 0.4945 0.4805 0.1493  0.0907  0.0532  37  GLY   B N   
462  C  CA  . GLY   B 28  ? 0.5433 0.4956 0.4598 0.1575  0.0817  0.0506  37  GLY   B CA  
463  C  C   . GLY   B 28  ? 0.5413 0.4898 0.4514 0.1697  0.0789  0.0485  37  GLY   B C   
464  O  O   . GLY   B 28  ? 0.5469 0.4896 0.4626 0.1756  0.0847  0.0519  37  GLY   B O   
465  N  N   . VAL   B 29  ? 0.5298 0.4817 0.4280 0.1736  0.0695  0.0432  38  VAL   B N   
466  C  CA  . VAL   B 29  ? 0.5236 0.4750 0.4145 0.1839  0.0634  0.0401  38  VAL   B CA  
467  C  C   . VAL   B 29  ? 0.5232 0.4724 0.4092 0.1750  0.0551  0.0294  38  VAL   B C   
468  O  O   . VAL   B 29  ? 0.5178 0.4668 0.4014 0.1651  0.0533  0.0261  38  VAL   B O   
469  C  CB  . VAL   B 29  ? 0.5228 0.4800 0.4014 0.2006  0.0593  0.0472  38  VAL   B CB  
470  C  CG1 . VAL   B 29  ? 0.5282 0.4852 0.3969 0.2109  0.0504  0.0426  38  VAL   B CG1 
471  C  CG2 . VAL   B 29  ? 0.5191 0.4806 0.4033 0.2096  0.0687  0.0600  38  VAL   B CG2 
472  N  N   . GLY   B 30  ? 0.5212 0.4706 0.4062 0.1786  0.0502  0.0250  39  GLY   B N   
473  C  CA  . GLY   B 30  ? 0.5277 0.4760 0.4097 0.1699  0.0426  0.0168  39  GLY   B CA  
474  C  C   . GLY   B 30  ? 0.5308 0.4820 0.4104 0.1758  0.0343  0.0137  39  GLY   B C   
475  O  O   . GLY   B 30  ? 0.5331 0.4889 0.4148 0.1869  0.0352  0.0170  39  GLY   B O   
476  N  N   . VAL   B 31  ? 0.5284 0.4778 0.4045 0.1675  0.0262  0.0077  40  VAL   B N   
477  C  CA  . VAL   B 31  ? 0.5238 0.4763 0.3987 0.1695  0.0162  0.0038  40  VAL   B CA  
478  C  C   . VAL   B 31  ? 0.5174 0.4777 0.4062 0.1587  0.0173  0.0003  40  VAL   B C   
479  O  O   . VAL   B 31  ? 0.5234 0.4816 0.4147 0.1465  0.0195  -0.0018 40  VAL   B O   
480  C  CB  . VAL   B 31  ? 0.5347 0.4767 0.3939 0.1683  0.0050  0.0003  40  VAL   B CB  
481  C  CG1 . VAL   B 31  ? 0.5372 0.4803 0.3960 0.1662  -0.0070 -0.0051 40  VAL   B CG1 
482  C  CG2 . VAL   B 31  ? 0.5502 0.4868 0.3942 0.1823  0.0041  0.0042  40  VAL   B CG2 
483  N  N   . MET   B 32  ? 0.5076 0.4791 0.4048 0.1639  0.0155  0.0002  41  MET   B N   
484  C  CA  . MET   B 32  ? 0.5064 0.4899 0.4178 0.1551  0.0158  -0.0021 41  MET   B CA  
485  C  C   . MET   B 32  ? 0.5167 0.5027 0.4258 0.1500  0.0015  -0.0061 41  MET   B C   
486  O  O   . MET   B 32  ? 0.5289 0.5167 0.4321 0.1595  -0.0070 -0.0070 41  MET   B O   
487  C  CB  . MET   B 32  ? 0.5006 0.4973 0.4233 0.1652  0.0221  0.0010  41  MET   B CB  
488  C  CG  . MET   B 32  ? 0.5259 0.5383 0.4643 0.1585  0.0246  -0.0001 41  MET   B CG  
489  S  SD  . MET   B 32  ? 0.6130 0.6205 0.5559 0.1476  0.0374  -0.0012 41  MET   B SD  
490  C  CE  . MET   B 32  ? 0.5876 0.5855 0.5292 0.1598  0.0501  0.0020  41  MET   B CE  
491  N  N   . GLN   B 33  ? 0.5146 0.4993 0.4272 0.1352  -0.0014 -0.0083 42  GLN   B N   
492  C  CA  . GLN   B 33  ? 0.5250 0.5098 0.4373 0.1273  -0.0151 -0.0119 42  GLN   B CA  
493  C  C   . GLN   B 33  ? 0.5279 0.5234 0.4553 0.1114  -0.0132 -0.0110 42  GLN   B C   
494  O  O   . GLN   B 33  ? 0.5394 0.5284 0.4653 0.1036  -0.0063 -0.0095 42  GLN   B O   
495  C  CB  . GLN   B 33  ? 0.5638 0.5258 0.4562 0.1268  -0.0235 -0.0147 42  GLN   B CB  
496  C  CG  . GLN   B 33  ? 0.6298 0.5871 0.5190 0.1208  -0.0394 -0.0198 42  GLN   B CG  
497  C  CD  . GLN   B 33  ? 0.7189 0.6503 0.5849 0.1240  -0.0476 -0.0231 42  GLN   B CD  
498  O  OE1 . GLN   B 33  ? 0.7476 0.6639 0.6088 0.1123  -0.0524 -0.0244 42  GLN   B OE1 
499  N  NE2 . GLN   B 33  ? 0.7395 0.6650 0.5903 0.1411  -0.0486 -0.0238 42  GLN   B NE2 
500  N  N   . GLU   B 34  ? 0.5164 0.5305 0.4587 0.1070  -0.0194 -0.0114 43  GLU   B N   
501  C  CA  . GLU   B 34  ? 0.5189 0.5484 0.4784 0.0922  -0.0172 -0.0088 43  GLU   B CA  
502  C  C   . GLU   B 34  ? 0.5137 0.5541 0.4821 0.0935  -0.0005 -0.0048 43  GLU   B C   
503  O  O   . GLU   B 34  ? 0.5202 0.5620 0.4925 0.0823  0.0047  -0.0024 43  GLU   B O   
504  C  CB  . GLU   B 34  ? 0.5694 0.5827 0.5231 0.0764  -0.0246 -0.0094 43  GLU   B CB  
505  C  CG  . GLU   B 34  ? 0.6617 0.6587 0.6037 0.0750  -0.0414 -0.0148 43  GLU   B CG  
506  C  CD  . GLU   B 34  ? 0.7846 0.7565 0.7148 0.0628  -0.0470 -0.0153 43  GLU   B CD  
507  O  OE1 . GLU   B 34  ? 0.8093 0.7860 0.7501 0.0488  -0.0423 -0.0103 43  GLU   B OE1 
508  O  OE2 . GLU   B 34  ? 0.8361 0.7833 0.7457 0.0687  -0.0555 -0.0200 43  GLU   B OE2 
509  N  N   . GLY   B 35  ? 0.4960 0.5422 0.4657 0.1076  0.0077  -0.0041 44  GLY   B N   
510  C  CA  . GLY   B 35  ? 0.4809 0.5340 0.4566 0.1109  0.0228  -0.0020 44  GLY   B CA  
511  C  C   . GLY   B 35  ? 0.4813 0.5151 0.4441 0.1084  0.0306  -0.0034 44  GLY   B C   
512  O  O   . GLY   B 35  ? 0.4847 0.5221 0.4504 0.1085  0.0420  -0.0032 44  GLY   B O   
513  N  N   . VAL   B 36  ? 0.4738 0.4879 0.4214 0.1070  0.0243  -0.0050 45  VAL   B N   
514  C  CA  . VAL   B 36  ? 0.4715 0.4698 0.4068 0.1047  0.0297  -0.0060 45  VAL   B CA  
515  C  C   . VAL   B 36  ? 0.4718 0.4573 0.3965 0.1159  0.0297  -0.0062 45  VAL   B C   
516  O  O   . VAL   B 36  ? 0.4777 0.4591 0.3966 0.1219  0.0210  -0.0061 45  VAL   B O   
517  C  CB  . VAL   B 36  ? 0.4746 0.4633 0.4018 0.0930  0.0234  -0.0057 45  VAL   B CB  
518  C  CG1 . VAL   B 36  ? 0.4864 0.4620 0.4005 0.0922  0.0282  -0.0061 45  VAL   B CG1 
519  C  CG2 . VAL   B 36  ? 0.4715 0.4738 0.4103 0.0813  0.0248  -0.0033 45  VAL   B CG2 
520  N  N   . PHE   B 37  ? 0.4589 0.4387 0.3810 0.1184  0.0394  -0.0065 46  PHE   B N   
521  C  CA  . PHE   B 37  ? 0.4586 0.4283 0.3731 0.1269  0.0410  -0.0050 46  PHE   B CA  
522  C  C   . PHE   B 37  ? 0.4582 0.4177 0.3609 0.1216  0.0391  -0.0053 46  PHE   B C   
523  O  O   . PHE   B 37  ? 0.4649 0.4237 0.3670 0.1139  0.0442  -0.0071 46  PHE   B O   
524  C  CB  . PHE   B 37  ? 0.4564 0.4253 0.3768 0.1319  0.0523  -0.0047 46  PHE   B CB  
525  C  CG  . PHE   B 37  ? 0.4743 0.4352 0.3901 0.1410  0.0538  -0.0009 46  PHE   B CG  
526  C  CD1 . PHE   B 37  ? 0.4811 0.4450 0.3962 0.1527  0.0495  0.0030  46  PHE   B CD1 
527  C  CD2 . PHE   B 37  ? 0.4913 0.4435 0.4037 0.1378  0.0592  -0.0005 46  PHE   B CD2 
528  C  CE1 . PHE   B 37  ? 0.4939 0.4522 0.4048 0.1620  0.0522  0.0083  46  PHE   B CE1 
529  C  CE2 . PHE   B 37  ? 0.4994 0.4467 0.4099 0.1454  0.0613  0.0050  46  PHE   B CE2 
530  C  CZ  . PHE   B 37  ? 0.4935 0.4438 0.4031 0.1580  0.0585  0.0099  46  PHE   B CZ  
531  N  N   . HIS   B 38  ? 0.4548 0.4075 0.3472 0.1272  0.0321  -0.0033 47  HIS   B N   
532  C  CA  . HIS   B 38  ? 0.4560 0.4006 0.3362 0.1254  0.0295  -0.0024 47  HIS   B CA  
533  C  C   . HIS   B 38  ? 0.4753 0.4186 0.3529 0.1331  0.0341  0.0013  47  HIS   B C   
534  O  O   . HIS   B 38  ? 0.4726 0.4170 0.3514 0.1434  0.0344  0.0042  47  HIS   B O   
535  C  CB  . HIS   B 38  ? 0.4504 0.3874 0.3192 0.1282  0.0184  -0.0026 47  HIS   B CB  
536  C  CG  . HIS   B 38  ? 0.4486 0.3868 0.3220 0.1197  0.0125  -0.0052 47  HIS   B CG  
537  N  ND1 . HIS   B 38  ? 0.4518 0.3989 0.3355 0.1214  0.0099  -0.0065 47  HIS   B ND1 
538  C  CD2 . HIS   B 38  ? 0.4559 0.3885 0.3255 0.1095  0.0089  -0.0057 47  HIS   B CD2 
539  C  CE1 . HIS   B 38  ? 0.4541 0.4024 0.3419 0.1108  0.0046  -0.0078 47  HIS   B CE1 
540  N  NE2 . HIS   B 38  ? 0.4592 0.3974 0.3384 0.1033  0.0040  -0.0071 47  HIS   B NE2 
541  N  N   . THR   B 39  ? 0.4885 0.4312 0.3630 0.1282  0.0376  0.0021  48  THR   B N   
542  C  CA  . THR   B 39  ? 0.4951 0.4394 0.3694 0.1336  0.0417  0.0069  48  THR   B CA  
543  C  C   . THR   B 39  ? 0.5096 0.4561 0.3773 0.1284  0.0410  0.0078  48  THR   B C   
544  O  O   . THR   B 39  ? 0.5178 0.4629 0.3799 0.1218  0.0379  0.0049  48  THR   B O   
545  C  CB  . THR   B 39  ? 0.4980 0.4433 0.3847 0.1336  0.0507  0.0077  48  THR   B CB  
546  O  OG1 . THR   B 39  ? 0.4954 0.4424 0.3825 0.1405  0.0536  0.0147  48  THR   B OG1 
547  C  CG2 . THR   B 39  ? 0.5088 0.4538 0.4013 0.1217  0.0565  0.0025  48  THR   B CG2 
548  N  N   . MET   B 40  ? 0.5093 0.4608 0.3776 0.1323  0.0438  0.0133  49  MET   B N   
549  C  CA  . MET   B 40  ? 0.5084 0.4668 0.3729 0.1280  0.0434  0.0150  49  MET   B CA  
550  C  C   . MET   B 40  ? 0.5050 0.4666 0.3792 0.1149  0.0486  0.0102  49  MET   B C   
551  O  O   . MET   B 40  ? 0.5129 0.4719 0.3975 0.1126  0.0544  0.0091  49  MET   B O   
552  C  CB  . MET   B 40  ? 0.5111 0.4775 0.3748 0.1375  0.0445  0.0238  49  MET   B CB  
553  C  CG  . MET   B 40  ? 0.5356 0.4972 0.3871 0.1528  0.0396  0.0274  49  MET   B CG  
554  S  SD  . MET   B 40  ? 0.6298 0.5980 0.4664 0.1639  0.0357  0.0341  49  MET   B SD  
555  C  CE  . MET   B 40  ? 0.6309 0.5885 0.4549 0.1582  0.0288  0.0277  49  MET   B CE  
556  N  N   . TRP   B 41  ? 0.4946 0.4606 0.3637 0.1072  0.0466  0.0069  50  TRP   B N   
557  C  CA  A TRP   B 41  ? 0.4916 0.4607 0.3661 0.0952  0.0501  0.0005  50  TRP   B CA  
558  C  CA  B TRP   B 41  ? 0.4875 0.4567 0.3620 0.0952  0.0501  0.0005  50  TRP   B CA  
559  C  C   . TRP   B 41  ? 0.4875 0.4612 0.3731 0.0905  0.0543  0.0017  50  TRP   B C   
560  O  O   . TRP   B 41  ? 0.4853 0.4538 0.3774 0.0826  0.0585  -0.0047 50  TRP   B O   
561  C  CB  A TRP   B 41  ? 0.4894 0.4657 0.3544 0.0901  0.0463  -0.0014 50  TRP   B CB  
562  C  CB  B TRP   B 41  ? 0.4798 0.4560 0.3445 0.0902  0.0463  -0.0014 50  TRP   B CB  
563  C  CG  A TRP   B 41  ? 0.4964 0.4746 0.3632 0.0792  0.0491  -0.0098 50  TRP   B CG  
564  C  CG  B TRP   B 41  ? 0.4780 0.4590 0.3453 0.0788  0.0486  -0.0089 50  TRP   B CG  
565  C  CD1 A TRP   B 41  ? 0.5127 0.4856 0.3770 0.0760  0.0511  -0.0156 50  TRP   B CD1 
566  C  CD1 B TRP   B 41  ? 0.4798 0.4705 0.3524 0.0720  0.0489  -0.0102 50  TRP   B CD1 
567  C  CD2 A TRP   B 41  ? 0.4933 0.4793 0.3647 0.0705  0.0502  -0.0139 50  TRP   B CD2 
568  C  CD2 B TRP   B 41  ? 0.4816 0.4591 0.3457 0.0732  0.0507  -0.0164 50  TRP   B CD2 
569  N  NE1 A TRP   B 41  ? 0.5179 0.4940 0.3825 0.0676  0.0537  -0.0234 50  TRP   B NE1 
570  N  NE1 B TRP   B 41  ? 0.4832 0.4740 0.3544 0.0626  0.0502  -0.0197 50  TRP   B NE1 
571  C  CE2 A TRP   B 41  ? 0.5087 0.4916 0.3774 0.0633  0.0524  -0.0234 50  TRP   B CE2 
572  C  CE2 B TRP   B 41  ? 0.4884 0.4716 0.3535 0.0642  0.0519  -0.0233 50  TRP   B CE2 
573  C  CE3 A TRP   B 41  ? 0.4942 0.4909 0.3721 0.0677  0.0491  -0.0103 50  TRP   B CE3 
574  C  CE3 B TRP   B 41  ? 0.4925 0.4640 0.3532 0.0748  0.0515  -0.0176 50  TRP   B CE3 
575  C  CZ2 A TRP   B 41  ? 0.5165 0.5037 0.3867 0.0536  0.0527  -0.0311 50  TRP   B CZ2 
576  C  CZ2 B TRP   B 41  ? 0.5006 0.4824 0.3608 0.0589  0.0543  -0.0319 50  TRP   B CZ2 
577  C  CZ3 A TRP   B 41  ? 0.5047 0.5072 0.3869 0.0561  0.0491  -0.0172 50  TRP   B CZ3 
578  C  CZ3 B TRP   B 41  ? 0.5057 0.4784 0.3640 0.0691  0.0549  -0.0244 50  TRP   B CZ3 
579  C  CH2 A TRP   B 41  ? 0.5126 0.5093 0.3897 0.0493  0.0503  -0.0283 50  TRP   B CH2 
580  C  CH2 B TRP   B 41  ? 0.5059 0.4831 0.3626 0.0622  0.0564  -0.0317 50  TRP   B CH2 
581  N  N   . HIS   B 42  ? 0.4838 0.4671 0.3713 0.0952  0.0534  0.0100  51  HIS   B N   
582  C  CA  . HIS   B 42  ? 0.4849 0.4743 0.3852 0.0891  0.0573  0.0131  51  HIS   B CA  
583  C  C   . HIS   B 42  ? 0.5006 0.4777 0.4111 0.0910  0.0639  0.0147  51  HIS   B C   
584  O  O   . HIS   B 42  ? 0.5046 0.4818 0.4266 0.0836  0.0680  0.0164  51  HIS   B O   
585  C  CB  . HIS   B 42  ? 0.4795 0.4866 0.3806 0.0944  0.0554  0.0235  51  HIS   B CB  
586  C  CG  . HIS   B 42  ? 0.4958 0.5022 0.3934 0.1102  0.0563  0.0331  51  HIS   B CG  
587  N  ND1 . HIS   B 42  ? 0.5161 0.5238 0.3987 0.1225  0.0512  0.0360  51  HIS   B ND1 
588  C  CD2 . HIS   B 42  ? 0.5006 0.5049 0.4063 0.1161  0.0616  0.0404  51  HIS   B CD2 
589  C  CE1 . HIS   B 42  ? 0.5133 0.5198 0.3945 0.1357  0.0530  0.0435  51  HIS   B CE1 
590  N  NE2 . HIS   B 42  ? 0.5092 0.5149 0.4042 0.1326  0.0595  0.0469  51  HIS   B NE2 
591  N  N   . VAL   B 43  ? 0.5072 0.4737 0.4137 0.1005  0.0647  0.0145  52  VAL   B N   
592  C  CA  . VAL   B 43  ? 0.5144 0.4703 0.4291 0.1047  0.0711  0.0170  52  VAL   B CA  
593  C  C   . VAL   B 43  ? 0.5331 0.4766 0.4525 0.0953  0.0754  0.0074  52  VAL   B C   
594  O  O   . VAL   B 43  ? 0.5303 0.4661 0.4588 0.0899  0.0809  0.0079  52  VAL   B O   
595  C  CB  . VAL   B 43  ? 0.5244 0.4770 0.4331 0.1193  0.0694  0.0205  52  VAL   B CB  
596  C  CG1 . VAL   B 43  ? 0.5329 0.4754 0.4492 0.1245  0.0761  0.0224  52  VAL   B CG1 
597  C  CG2 . VAL   B 43  ? 0.5268 0.4889 0.4291 0.1307  0.0660  0.0299  52  VAL   B CG2 
598  N  N   . THR   B 44  ? 0.5472 0.4882 0.4597 0.0933  0.0732  -0.0013 53  THR   B N   
599  C  CA  . THR   B 44  ? 0.5581 0.4883 0.4721 0.0873  0.0776  -0.0108 53  THR   B CA  
600  C  C   . THR   B 44  ? 0.5712 0.5037 0.4820 0.0745  0.0759  -0.0197 53  THR   B C   
601  O  O   . THR   B 44  ? 0.5810 0.5022 0.4930 0.0687  0.0800  -0.0280 53  THR   B O   
602  C  CB  . THR   B 44  ? 0.5662 0.4956 0.4757 0.0936  0.0772  -0.0140 53  THR   B CB  
603  O  OG1 . THR   B 44  ? 0.5650 0.5036 0.4661 0.0899  0.0714  -0.0167 53  THR   B OG1 
604  C  CG2 . THR   B 44  ? 0.5725 0.5027 0.4841 0.1063  0.0766  -0.0063 53  THR   B CG2 
605  N  N   . LYS   B 45  ? 0.5716 0.5180 0.4766 0.0712  0.0697  -0.0183 54  LYS   B N   
606  C  CA  . LYS   B 45  ? 0.5806 0.5342 0.4799 0.0607  0.0664  -0.0261 54  LYS   B CA  
607  C  C   . LYS   B 45  ? 0.5810 0.5301 0.4718 0.0597  0.0678  -0.0354 54  LYS   B C   
608  O  O   . LYS   B 45  ? 0.5867 0.5360 0.4727 0.0518  0.0675  -0.0446 54  LYS   B O   
609  C  CB  . LYS   B 45  ? 0.6108 0.5635 0.5177 0.0494  0.0670  -0.0296 54  LYS   B CB  
610  C  CG  . LYS   B 45  ? 0.6844 0.6453 0.6015 0.0505  0.0666  -0.0180 54  LYS   B CG  
611  C  CD  . LYS   B 45  ? 0.7708 0.7406 0.6958 0.0368  0.0641  -0.0200 54  LYS   B CD  
612  C  CE  . LYS   B 45  ? 0.8345 0.8175 0.7711 0.0385  0.0645  -0.0063 54  LYS   B CE  
613  N  NZ  . LYS   B 45  ? 0.8723 0.8736 0.8167 0.0253  0.0598  -0.0064 54  LYS   B NZ  
614  N  N   . GLY   B 46  ? 0.5748 0.5219 0.4637 0.0679  0.0689  -0.0326 55  GLY   B N   
615  C  CA  . GLY   B 46  ? 0.5789 0.5251 0.4623 0.0683  0.0713  -0.0385 55  GLY   B CA  
616  C  C   . GLY   B 46  ? 0.5833 0.5177 0.4706 0.0706  0.0786  -0.0447 55  GLY   B C   
617  O  O   . GLY   B 46  ? 0.5911 0.5271 0.4746 0.0727  0.0817  -0.0486 55  GLY   B O   
618  N  N   . ALA   B 47  ? 0.5834 0.5058 0.4779 0.0710  0.0822  -0.0448 56  ALA   B N   
619  C  CA  . ALA   B 47  ? 0.5909 0.4982 0.4876 0.0747  0.0898  -0.0505 56  ALA   B CA  
620  C  C   . ALA   B 47  ? 0.5912 0.5002 0.4921 0.0863  0.0933  -0.0453 56  ALA   B C   
621  O  O   . ALA   B 47  ? 0.5931 0.5099 0.4979 0.0912  0.0896  -0.0365 56  ALA   B O   
622  C  CB  . ALA   B 47  ? 0.5935 0.4856 0.4972 0.0719  0.0927  -0.0497 56  ALA   B CB  
623  N  N   . ALA   B 48  ? 0.5874 0.4894 0.4871 0.0915  0.1001  -0.0509 57  ALA   B N   
624  C  CA  . ALA   B 48  ? 0.5844 0.4916 0.4897 0.1029  0.1036  -0.0461 57  ALA   B CA  
625  C  C   . ALA   B 48  ? 0.5923 0.4913 0.5058 0.1111  0.1057  -0.0385 57  ALA   B C   
626  O  O   . ALA   B 48  ? 0.6081 0.4919 0.5230 0.1087  0.1080  -0.0384 57  ALA   B O   
627  C  CB  . ALA   B 48  ? 0.5877 0.4911 0.4890 0.1079  0.1114  -0.0537 57  ALA   B CB  
628  N  N   . LEU   B 49  ? 0.5802 0.4903 0.4995 0.1203  0.1045  -0.0313 58  LEU   B N   
629  C  CA  . LEU   B 49  ? 0.5763 0.4820 0.5020 0.1304  0.1061  -0.0230 58  LEU   B CA  
630  C  C   . LEU   B 49  ? 0.5850 0.4902 0.5151 0.1432  0.1132  -0.0220 58  LEU   B C   
631  O  O   . LEU   B 49  ? 0.5777 0.4909 0.5073 0.1449  0.1159  -0.0265 58  LEU   B O   
632  C  CB  . LEU   B 49  ? 0.5638 0.4836 0.4910 0.1323  0.0973  -0.0154 58  LEU   B CB  
633  C  CG  . LEU   B 49  ? 0.5764 0.4980 0.4985 0.1228  0.0906  -0.0150 58  LEU   B CG  
634  C  CD1 . LEU   B 49  ? 0.5791 0.5124 0.4995 0.1262  0.0819  -0.0095 58  LEU   B CD1 
635  C  CD2 . LEU   B 49  ? 0.5851 0.4950 0.5084 0.1204  0.0936  -0.0123 58  LEU   B CD2 
636  N  N   . ARG   B 50  ? 0.5976 0.4950 0.5319 0.1535  0.1168  -0.0150 59  ARG   B N   
637  C  CA  . ARG   B 50  ? 0.6130 0.5101 0.5512 0.1681  0.1238  -0.0124 59  ARG   B CA  
638  C  C   . ARG   B 50  ? 0.6126 0.5248 0.5566 0.1789  0.1191  -0.0022 59  ARG   B C   
639  O  O   . ARG   B 50  ? 0.5999 0.5112 0.5431 0.1779  0.1145  0.0035  59  ARG   B O   
640  C  CB  . ARG   B 50  ? 0.6541 0.5234 0.5902 0.1716  0.1335  -0.0133 59  ARG   B CB  
641  C  CG  . ARG   B 50  ? 0.7328 0.5962 0.6699 0.1875  0.1428  -0.0122 59  ARG   B CG  
642  C  CD  . ARG   B 50  ? 0.8085 0.6378 0.7403 0.1884  0.1523  -0.0160 59  ARG   B CD  
643  N  NE  . ARG   B 50  ? 0.8615 0.6737 0.7956 0.1830  0.1525  -0.0095 59  ARG   B NE  
644  C  CZ  . ARG   B 50  ? 0.9016 0.7100 0.8403 0.1944  0.1560  0.0030  59  ARG   B CZ  
645  N  NH1 . ARG   B 50  ? 0.8909 0.7123 0.8321 0.2122  0.1585  0.0096  59  ARG   B NH1 
646  N  NH2 . ARG   B 50  ? 0.9158 0.7100 0.8572 0.1884  0.1570  0.0098  59  ARG   B NH2 
647  N  N   . SER   B 51  ? 0.6227 0.5515 0.5719 0.1893  0.1196  -0.0001 60  SER   B N   
648  C  CA  . SER   B 51  ? 0.6434 0.5887 0.5974 0.2001  0.1141  0.0082  60  SER   B CA  
649  C  C   . SER   B 51  ? 0.6708 0.6210 0.6300 0.2169  0.1217  0.0121  60  SER   B C   
650  O  O   . SER   B 51  ? 0.6681 0.6409 0.6339 0.2209  0.1197  0.0117  60  SER   B O   
651  C  CB  . SER   B 51  ? 0.6504 0.6190 0.6071 0.1930  0.1024  0.0066  60  SER   B CB  
652  O  OG  . SER   B 51  ? 0.6734 0.6581 0.6340 0.2034  0.0959  0.0128  60  SER   B OG  
653  N  N   . GLY   B 52  ? 0.6908 0.6200 0.6475 0.2266  0.1309  0.0165  61  GLY   B N   
654  C  CA  . GLY   B 52  ? 0.7062 0.6353 0.6657 0.2445  0.1399  0.0208  61  GLY   B CA  
655  C  C   . GLY   B 52  ? 0.7285 0.6497 0.6858 0.2425  0.1477  0.0119  61  GLY   B C   
656  O  O   . GLY   B 52  ? 0.7461 0.6437 0.6964 0.2316  0.1511  0.0046  61  GLY   B O   
657  N  N   . GLU   B 53  ? 0.7248 0.6678 0.6877 0.2528  0.1500  0.0123  62  GLU   B N   
658  C  CA  . GLU   B 53  ? 0.7364 0.6750 0.6959 0.2534  0.1581  0.0042  62  GLU   B CA  
659  C  C   . GLU   B 53  ? 0.7269 0.6784 0.6860 0.2356  0.1521  -0.0041 62  GLU   B C   
660  O  O   . GLU   B 53  ? 0.7311 0.6732 0.6833 0.2332  0.1585  -0.0123 62  GLU   B O   
661  C  CB  . GLU   B 53  ? 0.7773 0.7358 0.7431 0.2734  0.1647  0.0092  62  GLU   B CB  
662  C  CG  . GLU   B 53  ? 0.8808 0.8170 0.8375 0.2842  0.1784  0.0036  62  GLU   B CG  
663  C  CD  . GLU   B 53  ? 0.9976 0.9465 0.9584 0.3090  0.1870  0.0110  62  GLU   B CD  
664  O  OE1 . GLU   B 53  ? 1.0019 0.9916 0.9754 0.3142  0.1830  0.0161  62  GLU   B OE1 
665  O  OE2 . GLU   B 53  ? 1.0455 0.9636 0.9973 0.3232  0.1977  0.0120  62  GLU   B OE2 
666  N  N   . GLY   B 54  ? 0.7096 0.6802 0.6742 0.2242  0.1402  -0.0019 63  GLY   B N   
667  C  CA  . GLY   B 54  ? 0.7043 0.6865 0.6686 0.2076  0.1340  -0.0075 63  GLY   B CA  
668  C  C   . GLY   B 54  ? 0.7050 0.6643 0.6589 0.1926  0.1317  -0.0138 63  GLY   B C   
669  O  O   . GLY   B 54  ? 0.7196 0.6560 0.6686 0.1928  0.1330  -0.0131 63  GLY   B O   
670  N  N   . ARG   B 55  ? 0.6816 0.6489 0.6327 0.1796  0.1283  -0.0192 64  ARG   B N   
671  C  CA  . ARG   B 55  ? 0.6721 0.6238 0.6134 0.1652  0.1254  -0.0255 64  ARG   B CA  
672  C  C   . ARG   B 55  ? 0.6357 0.6039 0.5783 0.1523  0.1152  -0.0242 64  ARG   B C   
673  O  O   . ARG   B 55  ? 0.6261 0.6150 0.5739 0.1504  0.1142  -0.0229 64  ARG   B O   
674  C  CB  . ARG   B 55  ? 0.6957 0.6351 0.6272 0.1642  0.1338  -0.0352 64  ARG   B CB  
675  C  CG  . ARG   B 55  ? 0.7391 0.6665 0.6602 0.1494  0.1301  -0.0426 64  ARG   B CG  
676  C  CD  . ARG   B 55  ? 0.7900 0.7032 0.6993 0.1498  0.1377  -0.0537 64  ARG   B CD  
677  N  NE  . ARG   B 55  ? 0.8300 0.7393 0.7295 0.1357  0.1329  -0.0608 64  ARG   B NE  
678  C  CZ  . ARG   B 55  ? 0.8721 0.7631 0.7591 0.1323  0.1361  -0.0722 64  ARG   B CZ  
679  N  NH1 . ARG   B 55  ? 0.8771 0.7475 0.7587 0.1418  0.1444  -0.0782 64  ARG   B NH1 
680  N  NH2 . ARG   B 55  ? 0.8746 0.7668 0.7533 0.1199  0.1305  -0.0778 64  ARG   B NH2 
681  N  N   . LEU   B 56  ? 0.6120 0.5707 0.5498 0.1438  0.1084  -0.0238 65  LEU   B N   
682  C  CA  . LEU   B 56  ? 0.5934 0.5624 0.5296 0.1328  0.0992  -0.0226 65  LEU   B CA  
683  C  C   . LEU   B 56  ? 0.5872 0.5476 0.5131 0.1223  0.1001  -0.0291 65  LEU   B C   
684  O  O   . LEU   B 56  ? 0.5964 0.5409 0.5167 0.1195  0.1007  -0.0320 65  LEU   B O   
685  C  CB  . LEU   B 56  ? 0.5950 0.5615 0.5312 0.1329  0.0904  -0.0173 65  LEU   B CB  
686  C  CG  . LEU   B 56  ? 0.6127 0.5813 0.5551 0.1453  0.0898  -0.0113 65  LEU   B CG  
687  C  CD1 . LEU   B 56  ? 0.6260 0.5948 0.5652 0.1449  0.0800  -0.0071 65  LEU   B CD1 
688  C  CD2 . LEU   B 56  ? 0.6148 0.6029 0.5672 0.1516  0.0899  -0.0090 65  LEU   B CD2 
689  N  N   . ASP   B 57  ? 0.5688 0.5412 0.4927 0.1163  0.0999  -0.0308 66  ASP   B N   
690  C  CA  . ASP   B 57  ? 0.5656 0.5333 0.4784 0.1073  0.1000  -0.0364 66  ASP   B CA  
691  C  C   . ASP   B 57  ? 0.5418 0.5144 0.4515 0.0986  0.0907  -0.0321 66  ASP   B C   
692  O  O   . ASP   B 57  ? 0.5325 0.5154 0.4483 0.0979  0.0856  -0.0260 66  ASP   B O   
693  C  CB  . ASP   B 57  ? 0.6013 0.5792 0.5113 0.1081  0.1071  -0.0401 66  ASP   B CB  
694  C  CG  . ASP   B 57  ? 0.6996 0.6702 0.6094 0.1186  0.1168  -0.0453 66  ASP   B CG  
695  O  OD1 . ASP   B 57  ? 0.7268 0.6776 0.6338 0.1213  0.1186  -0.0493 66  ASP   B OD1 
696  O  OD2 . ASP   B 57  ? 0.7348 0.7194 0.6475 0.1246  0.1232  -0.0446 66  ASP   B OD2 
697  N  N   . PRO   B 58  ? 0.5286 0.4934 0.4289 0.0922  0.0878  -0.0351 67  PRO   B N   
698  C  CA  . PRO   B 58  ? 0.5180 0.4862 0.4137 0.0862  0.0796  -0.0304 67  PRO   B CA  
699  C  C   . PRO   B 58  ? 0.5194 0.4995 0.4132 0.0816  0.0793  -0.0278 67  PRO   B C   
700  O  O   . PRO   B 58  ? 0.5252 0.5126 0.4184 0.0816  0.0860  -0.0307 67  PRO   B O   
701  C  CB  . PRO   B 58  ? 0.5280 0.4890 0.4148 0.0815  0.0783  -0.0345 67  PRO   B CB  
702  C  CG  . PRO   B 58  ? 0.5402 0.4958 0.4248 0.0815  0.0855  -0.0431 67  PRO   B CG  
703  C  CD  . PRO   B 58  ? 0.5240 0.4770 0.4174 0.0899  0.0915  -0.0430 67  PRO   B CD  
704  N  N   . TYR   B 59  ? 0.5109 0.4923 0.4035 0.0781  0.0720  -0.0217 68  TYR   B N   
705  C  CA  . TYR   B 59  ? 0.5041 0.4947 0.3962 0.0725  0.0713  -0.0172 68  TYR   B CA  
706  C  C   . TYR   B 59  ? 0.5198 0.5052 0.3997 0.0677  0.0660  -0.0143 68  TYR   B C   
707  O  O   . TYR   B 59  ? 0.5375 0.5287 0.4109 0.0636  0.0686  -0.0129 68  TYR   B O   
708  C  CB  . TYR   B 59  ? 0.4829 0.4796 0.3873 0.0726  0.0676  -0.0118 68  TYR   B CB  
709  C  CG  . TYR   B 59  ? 0.4678 0.4728 0.3746 0.0646  0.0659  -0.0053 68  TYR   B CG  
710  C  CD1 . TYR   B 59  ? 0.4819 0.4773 0.3801 0.0592  0.0588  -0.0010 68  TYR   B CD1 
711  C  CD2 . TYR   B 59  ? 0.4505 0.4726 0.3699 0.0630  0.0708  -0.0021 68  TYR   B CD2 
712  C  CE1 . TYR   B 59  ? 0.4880 0.4878 0.3891 0.0509  0.0572  0.0061  68  TYR   B CE1 
713  C  CE2 . TYR   B 59  ? 0.4595 0.4899 0.3841 0.0542  0.0691  0.0057  68  TYR   B CE2 
714  C  CZ  . TYR   B 59  ? 0.4882 0.5059 0.4035 0.0475  0.0623  0.0097  68  TYR   B CZ  
715  O  OH  . TYR   B 59  ? 0.5147 0.5378 0.4352 0.0377  0.0612  0.0183  68  TYR   B OH  
716  N  N   . TRP   B 60  ? 0.5160 0.4916 0.3922 0.0698  0.0590  -0.0127 69  TRP   B N   
717  C  CA  . TRP   B 60  ? 0.5178 0.4880 0.3816 0.0680  0.0538  -0.0094 69  TRP   B CA  
718  C  C   . TRP   B 60  ? 0.5161 0.4810 0.3757 0.0726  0.0514  -0.0115 69  TRP   B C   
719  O  O   . TRP   B 60  ? 0.5143 0.4757 0.3805 0.0775  0.0509  -0.0125 69  TRP   B O   
720  C  CB  . TRP   B 60  ? 0.5169 0.4798 0.3796 0.0666  0.0465  -0.0029 69  TRP   B CB  
721  C  CG  . TRP   B 60  ? 0.5260 0.4800 0.3743 0.0677  0.0414  0.0008  69  TRP   B CG  
722  C  CD1 . TRP   B 60  ? 0.5398 0.4963 0.3780 0.0646  0.0431  0.0038  69  TRP   B CD1 
723  C  CD2 . TRP   B 60  ? 0.5277 0.4718 0.3690 0.0747  0.0352  0.0017  69  TRP   B CD2 
724  N  NE1 . TRP   B 60  ? 0.5516 0.5000 0.3773 0.0694  0.0380  0.0067  69  TRP   B NE1 
725  C  CE2 . TRP   B 60  ? 0.5410 0.4819 0.3684 0.0758  0.0333  0.0055  69  TRP   B CE2 
726  C  CE3 . TRP   B 60  ? 0.5302 0.4693 0.3747 0.0817  0.0316  0.0002  69  TRP   B CE3 
727  C  CZ2 . TRP   B 60  ? 0.5479 0.4810 0.3652 0.0839  0.0281  0.0078  69  TRP   B CZ2 
728  C  CZ3 . TRP   B 60  ? 0.5443 0.4756 0.3781 0.0895  0.0266  0.0026  69  TRP   B CZ3 
729  C  CH2 . TRP   B 60  ? 0.5475 0.4758 0.3681 0.0907  0.0249  0.0063  69  TRP   B CH2 
730  N  N   . GLY   B 61  ? 0.5162 0.4826 0.3654 0.0715  0.0500  -0.0110 70  GLY   B N   
731  C  CA  . GLY   B 61  ? 0.5206 0.4862 0.3675 0.0751  0.0476  -0.0113 70  GLY   B CA  
732  C  C   . GLY   B 61  ? 0.5279 0.4980 0.3631 0.0748  0.0444  -0.0084 70  GLY   B C   
733  O  O   . GLY   B 61  ? 0.5335 0.5088 0.3618 0.0709  0.0459  -0.0085 70  GLY   B O   
734  N  N   . ASP   B 62  ? 0.5288 0.4988 0.3611 0.0803  0.0405  -0.0048 71  ASP   B N   
735  C  CA  . ASP   B 62  ? 0.5284 0.5053 0.3500 0.0825  0.0373  -0.0008 71  ASP   B CA  
736  C  C   . ASP   B 62  ? 0.5200 0.5043 0.3456 0.0867  0.0359  0.0010  71  ASP   B C   
737  O  O   . ASP   B 62  ? 0.5296 0.5077 0.3579 0.0936  0.0346  0.0043  71  ASP   B O   
738  C  CB  . ASP   B 62  ? 0.5600 0.5261 0.3700 0.0884  0.0327  0.0062  71  ASP   B CB  
739  C  CG  . ASP   B 62  ? 0.6242 0.5966 0.4211 0.0914  0.0305  0.0111  71  ASP   B CG  
740  O  OD1 . ASP   B 62  ? 0.6205 0.6002 0.4144 0.0980  0.0282  0.0143  71  ASP   B OD1 
741  O  OD2 . ASP   B 62  ? 0.6778 0.6494 0.4674 0.0880  0.0316  0.0128  71  ASP   B OD2 
742  N  N   . VAL   B 63  ? 0.5066 0.5057 0.3325 0.0826  0.0360  -0.0007 72  VAL   B N   
743  C  CA  . VAL   B 63  ? 0.4947 0.5053 0.3273 0.0841  0.0350  0.0020  72  VAL   B CA  
744  C  C   . VAL   B 63  ? 0.4981 0.5122 0.3222 0.0959  0.0312  0.0116  72  VAL   B C   
745  O  O   . VAL   B 63  ? 0.4895 0.5062 0.3192 0.1021  0.0314  0.0162  72  VAL   B O   
746  C  CB  . VAL   B 63  ? 0.4941 0.5209 0.3305 0.0741  0.0351  -0.0038 72  VAL   B CB  
747  C  CG1 . VAL   B 63  ? 0.4896 0.5360 0.3298 0.0755  0.0320  0.0018  72  VAL   B CG1 
748  C  CG2 . VAL   B 63  ? 0.4986 0.5187 0.3462 0.0649  0.0393  -0.0130 72  VAL   B CG2 
749  N  N   . LYS   B 64  ? 0.5062 0.5189 0.3156 0.1006  0.0283  0.0153  73  LYS   B N   
750  C  CA  . LYS   B 64  ? 0.5133 0.5266 0.3118 0.1140  0.0249  0.0242  73  LYS   B CA  
751  C  C   . LYS   B 64  ? 0.5199 0.5135 0.3145 0.1236  0.0237  0.0265  73  LYS   B C   
752  O  O   . LYS   B 64  ? 0.5136 0.5107 0.3071 0.1342  0.0229  0.0317  73  LYS   B O   
753  C  CB  . LYS   B 64  ? 0.5456 0.5590 0.3280 0.1176  0.0225  0.0281  73  LYS   B CB  
754  C  CG  . LYS   B 64  ? 0.5845 0.6064 0.3567 0.1318  0.0198  0.0372  73  LYS   B CG  
755  C  CD  . LYS   B 64  ? 0.6308 0.6514 0.3860 0.1370  0.0180  0.0422  73  LYS   B CD  
756  C  CE  . LYS   B 64  ? 0.6840 0.7170 0.4298 0.1524  0.0160  0.0514  73  LYS   B CE  
757  N  NZ  . LYS   B 64  ? 0.7408 0.7600 0.4656 0.1625  0.0145  0.0579  73  LYS   B NZ  
758  N  N   . GLN   B 65  ? 0.5278 0.5024 0.3204 0.1199  0.0233  0.0227  74  GLN   B N   
759  C  CA  . GLN   B 65  ? 0.5397 0.4964 0.3294 0.1271  0.0209  0.0229  74  GLN   B CA  
760  C  C   . GLN   B 65  ? 0.5298 0.4920 0.3335 0.1276  0.0237  0.0211  74  GLN   B C   
761  O  O   . GLN   B 65  ? 0.5353 0.4883 0.3357 0.1371  0.0215  0.0226  74  GLN   B O   
762  C  CB  . GLN   B 65  ? 0.5793 0.5195 0.3680 0.1199  0.0197  0.0192  74  GLN   B CB  
763  C  CG  . GLN   B 65  ? 0.6544 0.5825 0.4280 0.1207  0.0167  0.0229  74  GLN   B CG  
764  C  CD  . GLN   B 65  ? 0.7419 0.6569 0.5187 0.1111  0.0162  0.0204  74  GLN   B CD  
765  O  OE1 . GLN   B 65  ? 0.7755 0.6802 0.5575 0.1105  0.0135  0.0174  74  GLN   B OE1 
766  N  NE2 . GLN   B 65  ? 0.7431 0.6610 0.5175 0.1037  0.0188  0.0223  74  GLN   B NE2 
767  N  N   . ASP   B 66  ? 0.5117 0.4874 0.3296 0.1181  0.0284  0.0179  75  ASP   B N   
768  C  CA  . ASP   B 66  ? 0.4996 0.4794 0.3318 0.1165  0.0325  0.0169  75  ASP   B CA  
769  C  C   . ASP   B 66  ? 0.5003 0.4656 0.3354 0.1177  0.0326  0.0135  75  ASP   B C   
770  O  O   . ASP   B 66  ? 0.4989 0.4616 0.3369 0.1255  0.0330  0.0161  75  ASP   B O   
771  C  CB  . ASP   B 66  ? 0.4990 0.4894 0.3327 0.1264  0.0329  0.0246  75  ASP   B CB  
772  C  CG  . ASP   B 66  ? 0.5164 0.5120 0.3662 0.1231  0.0383  0.0253  75  ASP   B CG  
773  O  OD1 . ASP   B 66  ? 0.4949 0.4897 0.3550 0.1113  0.0416  0.0191  75  ASP   B OD1 
774  O  OD2 . ASP   B 66  ? 0.5610 0.5601 0.4121 0.1333  0.0396  0.0322  75  ASP   B OD2 
775  N  N   . LEU   B 67  ? 0.4989 0.4569 0.3334 0.1104  0.0323  0.0085  76  LEU   B N   
776  C  CA  . LEU   B 67  ? 0.5001 0.4486 0.3394 0.1105  0.0320  0.0056  76  LEU   B CA  
777  C  C   . LEU   B 67  ? 0.4932 0.4444 0.3419 0.1002  0.0369  -0.0001 76  LEU   B C   
778  O  O   . LEU   B 67  ? 0.4961 0.4536 0.3437 0.0931  0.0394  -0.0024 76  LEU   B O   
779  C  CB  . LEU   B 67  ? 0.5103 0.4460 0.3383 0.1143  0.0251  0.0068  76  LEU   B CB  
780  C  CG  . LEU   B 67  ? 0.5356 0.4644 0.3515 0.1273  0.0197  0.0109  76  LEU   B CG  
781  C  CD1 . LEU   B 67  ? 0.5477 0.4596 0.3504 0.1287  0.0124  0.0106  76  LEU   B CD1 
782  C  CD2 . LEU   B 67  ? 0.5438 0.4737 0.3652 0.1359  0.0203  0.0115  76  LEU   B CD2 
783  N  N   . VAL   B 68  ? 0.4841 0.4320 0.3414 0.1007  0.0385  -0.0024 77  VAL   B N   
784  C  CA  . VAL   B 68  ? 0.4805 0.4315 0.3464 0.0939  0.0441  -0.0073 77  VAL   B CA  
785  C  C   . VAL   B 68  ? 0.4702 0.4194 0.3433 0.0968  0.0430  -0.0074 77  VAL   B C   
786  O  O   . VAL   B 68  ? 0.4728 0.4192 0.3475 0.1047  0.0405  -0.0053 77  VAL   B O   
787  C  CB  . VAL   B 68  ? 0.4871 0.4414 0.3600 0.0910  0.0510  -0.0111 77  VAL   B CB  
788  C  CG1 . VAL   B 68  ? 0.4922 0.4434 0.3720 0.0981  0.0530  -0.0083 77  VAL   B CG1 
789  C  CG2 . VAL   B 68  ? 0.4896 0.4455 0.3674 0.0857  0.0570  -0.0171 77  VAL   B CG2 
790  N  N   . SER   B 69  ? 0.4608 0.4138 0.3379 0.0908  0.0446  -0.0092 78  SER   B N   
791  C  CA  . SER   B 69  ? 0.4504 0.4067 0.3370 0.0924  0.0436  -0.0090 78  SER   B CA  
792  C  C   . SER   B 69  ? 0.4402 0.4046 0.3366 0.0911  0.0527  -0.0124 78  SER   B C   
793  O  O   . SER   B 69  ? 0.4385 0.4049 0.3320 0.0863  0.0581  -0.0154 78  SER   B O   
794  C  CB  . SER   B 69  ? 0.4515 0.4071 0.3362 0.0868  0.0371  -0.0066 78  SER   B CB  
795  O  OG  . SER   B 69  ? 0.4549 0.4180 0.3423 0.0785  0.0419  -0.0064 78  SER   B OG  
796  N  N   . TYR   B 70  ? 0.4316 0.4009 0.3383 0.0966  0.0541  -0.0122 79  TYR   B N   
797  C  CA  . TYR   B 70  ? 0.4221 0.3980 0.3374 0.0988  0.0630  -0.0148 79  TYR   B CA  
798  C  C   . TYR   B 70  ? 0.4175 0.4077 0.3438 0.0986  0.0618  -0.0123 79  TYR   B C   
799  O  O   . TYR   B 70  ? 0.4153 0.4078 0.3450 0.1008  0.0541  -0.0096 79  TYR   B O   
800  C  CB  . TYR   B 70  ? 0.4179 0.3874 0.3363 0.1083  0.0672  -0.0151 79  TYR   B CB  
801  C  CG  . TYR   B 70  ? 0.4311 0.3893 0.3431 0.1066  0.0708  -0.0177 79  TYR   B CG  
802  C  CD1 . TYR   B 70  ? 0.4401 0.3932 0.3454 0.1058  0.0654  -0.0150 79  TYR   B CD1 
803  C  CD2 . TYR   B 70  ? 0.4433 0.3963 0.3559 0.1060  0.0793  -0.0229 79  TYR   B CD2 
804  C  CE1 . TYR   B 70  ? 0.4506 0.3976 0.3526 0.1026  0.0681  -0.0166 79  TYR   B CE1 
805  C  CE2 . TYR   B 70  ? 0.4554 0.3985 0.3632 0.1018  0.0812  -0.0260 79  TYR   B CE2 
806  C  CZ  . TYR   B 70  ? 0.4664 0.4084 0.3704 0.0995  0.0755  -0.0223 79  TYR   B CZ  
807  O  OH  . TYR   B 70  ? 0.4762 0.4123 0.3784 0.0944  0.0769  -0.0243 79  TYR   B OH  
808  N  N   . CYS   B 71  ? 0.4153 0.4164 0.3468 0.0962  0.0690  -0.0133 80  CYS   B N   
809  C  CA  . CYS   B 71  ? 0.4149 0.4350 0.3596 0.0957  0.0698  -0.0099 80  CYS   B CA  
810  C  C   . CYS   B 71  ? 0.4092 0.4366 0.3563 0.0843  0.0633  -0.0054 80  CYS   B C   
811  O  O   . CYS   B 71  ? 0.4018 0.4474 0.3602 0.0807  0.0661  -0.0018 80  CYS   B O   
812  C  CB  . CYS   B 71  ? 0.4341 0.4610 0.3891 0.1049  0.0672  -0.0081 80  CYS   B CB  
813  S  SG  . CYS   B 71  ? 0.5265 0.5435 0.4799 0.1192  0.0765  -0.0110 80  CYS   B SG  
814  N  N   . GLY   B 72  ? 0.4006 0.4139 0.3372 0.0789  0.0555  -0.0049 81  GLY   B N   
815  C  CA  . GLY   B 72  ? 0.3871 0.4013 0.3237 0.0680  0.0493  -0.0003 81  GLY   B CA  
816  C  C   . GLY   B 72  ? 0.3945 0.3890 0.3152 0.0657  0.0426  -0.0005 81  GLY   B C   
817  O  O   . GLY   B 72  ? 0.4034 0.3872 0.3143 0.0722  0.0430  -0.0038 81  GLY   B O   
818  N  N   . PRO   B 73  ? 0.3972 0.3864 0.3150 0.0566  0.0366  0.0038  82  PRO   B N   
819  C  CA  . PRO   B 73  ? 0.4263 0.3955 0.3270 0.0566  0.0306  0.0042  82  PRO   B CA  
820  C  C   . PRO   B 73  ? 0.4647 0.4198 0.3586 0.0639  0.0210  0.0014  82  PRO   B C   
821  O  O   . PRO   B 73  ? 0.4583 0.4179 0.3607 0.0667  0.0161  -0.0004 82  PRO   B O   
822  C  CB  . PRO   B 73  ? 0.4328 0.3989 0.3334 0.0452  0.0279  0.0105  82  PRO   B CB  
823  C  CG  . PRO   B 73  ? 0.4152 0.3981 0.3353 0.0385  0.0274  0.0129  82  PRO   B CG  
824  C  CD  . PRO   B 73  ? 0.3761 0.3773 0.3066 0.0461  0.0355  0.0094  82  PRO   B CD  
825  N  N   . TRP   B 74  ? 0.4916 0.4309 0.3688 0.0684  0.0180  0.0013  83  TRP   B N   
826  C  CA  . TRP   B 74  ? 0.5194 0.4453 0.3866 0.0776  0.0098  -0.0008 83  TRP   B CA  
827  C  C   . TRP   B 74  ? 0.5396 0.4567 0.4078 0.0733  -0.0012 -0.0013 83  TRP   B C   
828  O  O   . TRP   B 74  ? 0.5469 0.4558 0.4130 0.0636  -0.0044 0.0017  83  TRP   B O   
829  C  CB  . TRP   B 74  ? 0.5321 0.4452 0.3814 0.0829  0.0091  0.0008  83  TRP   B CB  
830  C  CG  . TRP   B 74  ? 0.5469 0.4498 0.3853 0.0952  0.0032  -0.0006 83  TRP   B CG  
831  C  CD1 . TRP   B 74  ? 0.5677 0.4533 0.3939 0.0994  -0.0069 -0.0015 83  TRP   B CD1 
832  C  CD2 . TRP   B 74  ? 0.5463 0.4554 0.3841 0.1055  0.0073  -0.0010 83  TRP   B CD2 
833  N  NE1 . TRP   B 74  ? 0.5754 0.4579 0.3924 0.1134  -0.0089 -0.0024 83  TRP   B NE1 
834  C  CE2 . TRP   B 74  ? 0.5643 0.4622 0.3894 0.1168  0.0001  -0.0011 83  TRP   B CE2 
835  C  CE3 . TRP   B 74  ? 0.5451 0.4671 0.3914 0.1059  0.0163  -0.0010 83  TRP   B CE3 
836  C  CZ2 . TRP   B 74  ? 0.5738 0.4762 0.3960 0.1288  0.0026  0.0004  83  TRP   B CZ2 
837  C  CZ3 . TRP   B 74  ? 0.5584 0.4827 0.4032 0.1159  0.0182  0.0002  83  TRP   B CZ3 
838  C  CH2 . TRP   B 74  ? 0.5679 0.4842 0.4017 0.1273  0.0119  0.0017  83  TRP   B CH2 
839  N  N   . LYS   B 75  ? 0.5393 0.4602 0.4125 0.0795  -0.0065 -0.0048 84  LYS   B N   
840  C  CA  . LYS   B 75  ? 0.5453 0.4614 0.4212 0.0755  -0.0184 -0.0072 84  LYS   B CA  
841  C  C   . LYS   B 75  ? 0.5828 0.4767 0.4391 0.0843  -0.0293 -0.0110 84  LYS   B C   
842  O  O   . LYS   B 75  ? 0.5914 0.4751 0.4456 0.0794  -0.0409 -0.0142 84  LYS   B O   
843  C  CB  . LYS   B 75  ? 0.5297 0.4666 0.4225 0.0783  -0.0184 -0.0090 84  LYS   B CB  
844  C  CG  . LYS   B 75  ? 0.5357 0.4954 0.4480 0.0711  -0.0084 -0.0057 84  LYS   B CG  
845  C  CD  . LYS   B 75  ? 0.5747 0.5384 0.4970 0.0549  -0.0114 -0.0023 84  LYS   B CD  
846  C  CE  . LYS   B 75  ? 0.5954 0.5790 0.5314 0.0491  0.0011  0.0025  84  LYS   B CE  
847  N  NZ  . LYS   B 75  ? 0.6061 0.6163 0.5638 0.0473  0.0019  0.0038  84  LYS   B NZ  
848  N  N   . LEU   B 76  ? 0.5989 0.4866 0.4413 0.0977  -0.0260 -0.0108 85  LEU   B N   
849  C  CA  . LEU   B 76  ? 0.6222 0.4915 0.4443 0.1101  -0.0345 -0.0138 85  LEU   B CA  
850  C  C   . LEU   B 76  ? 0.6636 0.5083 0.4681 0.1074  -0.0393 -0.0130 85  LEU   B C   
851  O  O   . LEU   B 76  ? 0.6676 0.5115 0.4686 0.1057  -0.0320 -0.0082 85  LEU   B O   
852  C  CB  . LEU   B 76  ? 0.6112 0.4879 0.4280 0.1256  -0.0275 -0.0118 85  LEU   B CB  
853  C  CG  . LEU   B 76  ? 0.6042 0.5027 0.4382 0.1284  -0.0199 -0.0108 85  LEU   B CG  
854  C  CD1 . LEU   B 76  ? 0.6080 0.5113 0.4375 0.1414  -0.0126 -0.0073 85  LEU   B CD1 
855  C  CD2 . LEU   B 76  ? 0.6028 0.5072 0.4427 0.1309  -0.0277 -0.0146 85  LEU   B CD2 
856  N  N   . ASP   B 77  ? 0.7019 0.5257 0.4947 0.1070  -0.0520 -0.0178 86  ASP   B N   
857  C  CA  . ASP   B 77  ? 0.7509 0.5463 0.5257 0.1045  -0.0570 -0.0170 86  ASP   B CA  
858  C  C   . ASP   B 77  ? 0.7841 0.5535 0.5322 0.1199  -0.0670 -0.0226 86  ASP   B C   
859  O  O   . ASP   B 77  ? 0.8054 0.5493 0.5348 0.1225  -0.0697 -0.0214 86  ASP   B O   
860  C  CB  . ASP   B 77  ? 0.7873 0.5748 0.5728 0.0844  -0.0623 -0.0165 86  ASP   B CB  
861  C  CG  . ASP   B 77  ? 0.8799 0.6697 0.6754 0.0771  -0.0740 -0.0233 86  ASP   B CG  
862  O  OD1 . ASP   B 77  ? 0.8964 0.6955 0.6903 0.0887  -0.0778 -0.0288 86  ASP   B OD1 
863  O  OD2 . ASP   B 77  ? 0.9207 0.7047 0.7263 0.0594  -0.0795 -0.0226 86  ASP   B OD2 
864  N  N   . ALA   B 78  ? 0.7859 0.5612 0.5306 0.1315  -0.0723 -0.0282 87  ALA   B N   
865  C  CA  . ALA   B 78  ? 0.8118 0.5639 0.5293 0.1483  -0.0819 -0.0344 87  ALA   B CA  
866  C  C   . ALA   B 78  ? 0.8275 0.5744 0.5264 0.1658  -0.0744 -0.0290 87  ALA   B C   
867  O  O   . ALA   B 78  ? 0.8184 0.5872 0.5285 0.1670  -0.0621 -0.0214 87  ALA   B O   
868  C  CB  . ALA   B 78  ? 0.8066 0.5713 0.5251 0.1582  -0.0877 -0.0404 87  ALA   B CB  
869  N  N   . ALA   B 79  ? 0.8477 0.5657 0.5182 0.1792  -0.0820 -0.0330 88  ALA   B N   
870  C  CA  . ALA   B 79  ? 0.8638 0.5788 0.5163 0.1972  -0.0750 -0.0269 88  ALA   B CA  
871  C  C   . ALA   B 79  ? 0.8822 0.5832 0.5069 0.2215  -0.0811 -0.0318 88  ALA   B C   
872  O  O   . ALA   B 79  ? 0.8980 0.5769 0.5086 0.2234  -0.0940 -0.0420 88  ALA   B O   
873  C  CB  . ALA   B 79  ? 0.8761 0.5692 0.5192 0.1912  -0.0740 -0.0228 88  ALA   B CB  
874  N  N   . TRP   B 80  ? 0.8802 0.5945 0.4962 0.2402  -0.0722 -0.0244 89  TRP   B N   
875  C  CA  . TRP   B 80  ? 0.9046 0.6075 0.4921 0.2663  -0.0761 -0.0272 89  TRP   B CA  
876  C  C   . TRP   B 80  ? 0.9351 0.5954 0.4929 0.2722  -0.0853 -0.0330 89  TRP   B C   
877  O  O   . TRP   B 80  ? 0.9388 0.5880 0.4973 0.2635  -0.0823 -0.0282 89  TRP   B O   
878  C  CB  . TRP   B 80  ? 0.8976 0.6268 0.4850 0.2834  -0.0633 -0.0156 89  TRP   B CB  
879  C  CG  . TRP   B 80  ? 0.9185 0.6404 0.4770 0.3122  -0.0656 -0.0168 89  TRP   B CG  
880  C  CD1 . TRP   B 80  ? 0.9399 0.6549 0.4841 0.3246  -0.0737 -0.0251 89  TRP   B CD1 
881  C  CD2 . TRP   B 80  ? 0.9227 0.6474 0.4634 0.3336  -0.0590 -0.0086 89  TRP   B CD2 
882  N  NE1 . TRP   B 80  ? 0.9521 0.6634 0.4688 0.3530  -0.0724 -0.0230 89  TRP   B NE1 
883  C  CE2 . TRP   B 80  ? 0.9443 0.6629 0.4596 0.3592  -0.0628 -0.0123 89  TRP   B CE2 
884  C  CE3 . TRP   B 80  ? 0.9254 0.6599 0.4692 0.3346  -0.0502 0.0018  89  TRP   B CE3 
885  C  CZ2 . TRP   B 80  ? 0.9569 0.6781 0.4498 0.3860  -0.0576 -0.0055 89  TRP   B CZ2 
886  C  CZ3 . TRP   B 80  ? 0.9422 0.6809 0.4654 0.3604  -0.0456 0.0086  89  TRP   B CZ3 
887  C  CH2 . TRP   B 80  ? 0.9526 0.6847 0.4509 0.3860  -0.0488 0.0053  89  TRP   B CH2 
888  N  N   . ASP   B 81  ? 0.9555 0.5907 0.4870 0.2864  -0.0969 -0.0436 90  ASP   B N   
889  C  CA  . ASP   B 81  ? 0.9903 0.5792 0.4910 0.2926  -0.1068 -0.0509 90  ASP   B CA  
890  C  C   . ASP   B 81  ? 1.0180 0.5971 0.4897 0.3207  -0.1012 -0.0454 90  ASP   B C   
891  O  O   . ASP   B 81  ? 1.0403 0.5782 0.4823 0.3300  -0.1088 -0.0514 90  ASP   B O   
892  C  CB  . ASP   B 81  ? 1.0116 0.5735 0.4957 0.2930  -0.1240 -0.0672 90  ASP   B CB  
893  C  CG  . ASP   B 81  ? 1.0517 0.6253 0.5190 0.3177  -0.1263 -0.0720 90  ASP   B CG  
894  O  OD1 . ASP   B 81  ? 1.0482 0.6540 0.5202 0.3335  -0.1135 -0.0611 90  ASP   B OD1 
895  O  OD2 . ASP   B 81  ? 1.0781 0.6296 0.5275 0.3212  -0.1412 -0.0863 90  ASP   B OD2 
896  N  N   . GLY   B 82  ? 1.0132 0.6296 0.4934 0.3343  -0.0883 -0.0340 91  GLY   B N   
897  C  CA  . GLY   B 82  ? 1.0332 0.6502 0.4900 0.3619  -0.0815 -0.0266 91  GLY   B CA  
898  C  C   . GLY   B 82  ? 1.0643 0.6662 0.4876 0.3906  -0.0878 -0.0342 91  GLY   B C   
899  O  O   . GLY   B 82  ? 1.0754 0.6794 0.4773 0.4170  -0.0819 -0.0280 91  GLY   B O   
900  N  N   . LEU   B 83  ? 1.0758 0.6645 0.4936 0.3872  -0.0997 -0.0476 92  LEU   B N   
901  C  CA  . LEU   B 83  ? 1.1032 0.6743 0.4858 0.4144  -0.1074 -0.0570 92  LEU   B CA  
902  C  C   . LEU   B 83  ? 1.0917 0.6931 0.4815 0.4223  -0.1070 -0.0580 92  LEU   B C   
903  O  O   . LEU   B 83  ? 1.1013 0.7140 0.4710 0.4511  -0.1024 -0.0544 92  LEU   B O   
904  C  CB  . LEU   B 83  ? 1.1399 0.6567 0.4965 0.4092  -0.1256 -0.0751 92  LEU   B CB  
905  C  CG  . LEU   B 83  ? 1.1993 0.6742 0.5234 0.4234  -0.1274 -0.0764 92  LEU   B CG  
906  C  CD1 . LEU   B 83  ? 1.2403 0.6600 0.5446 0.4115  -0.1455 -0.0939 92  LEU   B CD1 
907  C  CD2 . LEU   B 83  ? 1.2220 0.6979 0.5120 0.4626  -0.1228 -0.0744 92  LEU   B CD2 
908  N  N   . SER   B 84  ? 1.0698 0.6839 0.4860 0.3992  -0.1118 -0.0625 93  SER   B N   
909  C  CA  . SER   B 84  ? 1.0568 0.6957 0.4768 0.4078  -0.1131 -0.0644 93  SER   B CA  
910  C  C   . SER   B 84  ? 1.0212 0.7099 0.4715 0.4078  -0.0962 -0.0475 93  SER   B C   
911  O  O   . SER   B 84  ? 1.0159 0.7223 0.4892 0.3963  -0.0843 -0.0354 93  SER   B O   
912  C  CB  . SER   B 84  ? 1.0768 0.7043 0.5062 0.3868  -0.1282 -0.0786 93  SER   B CB  
913  O  OG  . SER   B 84  ? 1.0997 0.7233 0.5571 0.3550  -0.1289 -0.0778 93  SER   B OG  
914  N  N   . GLU   B 85  ? 0.9971 0.7070 0.4448 0.4225  -0.0953 -0.0467 94  GLU   B N   
915  C  CA  . GLU   B 85  ? 0.9642 0.7176 0.4393 0.4227  -0.0803 -0.0312 94  GLU   B CA  
916  C  C   . GLU   B 85  ? 0.9287 0.6949 0.4402 0.3926  -0.0804 -0.0316 94  GLU   B C   
917  O  O   . GLU   B 85  ? 0.9408 0.6888 0.4537 0.3772  -0.0936 -0.0445 94  GLU   B O   
918  C  CB  . GLU   B 85  ? 0.9993 0.7690 0.4582 0.4488  -0.0796 -0.0296 94  GLU   B CB  
919  C  CG  . GLU   B 85  ? 1.0750 0.8383 0.4980 0.4824  -0.0770 -0.0270 94  GLU   B CG  
920  C  CD  . GLU   B 85  ? 1.1261 0.9218 0.5447 0.5073  -0.0669 -0.0151 94  GLU   B CD  
921  O  OE1 . GLU   B 85  ? 1.1250 0.9375 0.5564 0.5036  -0.0679 -0.0149 94  GLU   B OE1 
922  O  OE2 . GLU   B 85  ? 1.1481 0.9542 0.5511 0.5313  -0.0574 -0.0047 94  GLU   B OE2 
923  N  N   . VAL   B 86  ? 0.8819 0.6796 0.4230 0.3843  -0.0657 -0.0173 95  VAL   B N   
924  C  CA  . VAL   B 86  ? 0.8447 0.6572 0.4204 0.3586  -0.0628 -0.0158 95  VAL   B CA  
925  C  C   . VAL   B 86  ? 0.8166 0.6613 0.4083 0.3660  -0.0527 -0.0053 95  VAL   B C   
926  O  O   . VAL   B 86  ? 0.8177 0.6739 0.3948 0.3897  -0.0475 0.0018  95  VAL   B O   
927  C  CB  . VAL   B 86  ? 0.8363 0.6527 0.4329 0.3392  -0.0540 -0.0088 95  VAL   B CB  
928  C  CG1 . VAL   B 86  ? 0.8523 0.6372 0.4301 0.3363  -0.0618 -0.0159 95  VAL   B CG1 
929  C  CG2 . VAL   B 86  ? 0.8252 0.6695 0.4328 0.3476  -0.0381 0.0074  95  VAL   B CG2 
930  N  N   . GLN   B 87  ? 0.7879 0.6467 0.4086 0.3471  -0.0495 -0.0037 96  GLN   B N   
931  C  CA  . GLN   B 87  ? 0.7630 0.6486 0.4000 0.3527  -0.0391 0.0070  96  GLN   B CA  
932  C  C   . GLN   B 87  ? 0.7346 0.6348 0.4042 0.3319  -0.0270 0.0156  96  GLN   B C   
933  O  O   . GLN   B 87  ? 0.7271 0.6200 0.4109 0.3109  -0.0306 0.0091  96  GLN   B O   
934  C  CB  . GLN   B 87  ? 0.7766 0.6644 0.4127 0.3549  -0.0484 -0.0007 96  GLN   B CB  
935  C  CG  . GLN   B 87  ? 0.8167 0.7143 0.4323 0.3829  -0.0483 0.0031  96  GLN   B CG  
936  C  CD  . GLN   B 87  ? 0.8675 0.7627 0.4726 0.3885  -0.0624 -0.0083 96  GLN   B CD  
937  O  OE1 . GLN   B 87  ? 0.8579 0.7597 0.4830 0.3731  -0.0660 -0.0120 96  GLN   B OE1 
938  N  NE2 . GLN   B 87  ? 0.8928 0.7806 0.4654 0.4123  -0.0707 -0.0140 96  GLN   B NE2 
939  N  N   . LEU   B 88  ? 0.7142 0.6347 0.3953 0.3375  -0.0128 0.0301  97  LEU   B N   
940  C  CA  . LEU   B 88  ? 0.6922 0.6256 0.4032 0.3186  -0.0017 0.0373  97  LEU   B CA  
941  C  C   . LEU   B 88  ? 0.6797 0.6246 0.4047 0.3194  0.0020  0.0406  97  LEU   B C   
942  O  O   . LEU   B 88  ? 0.6786 0.6358 0.3990 0.3367  0.0079  0.0501  97  LEU   B O   
943  C  CB  . LEU   B 88  ? 0.6814 0.6309 0.3992 0.3226  0.0111  0.0514  97  LEU   B CB  
944  C  CG  . LEU   B 88  ? 0.6726 0.6379 0.4204 0.3071  0.0237  0.0609  97  LEU   B CG  
945  C  CD1 . LEU   B 88  ? 0.6743 0.6313 0.4376 0.2827  0.0217  0.0527  97  LEU   B CD1 
946  C  CD2 . LEU   B 88  ? 0.6654 0.6486 0.4192 0.3120  0.0345  0.0750  97  LEU   B CD2 
947  N  N   . LEU   B 89  ? 0.6694 0.6110 0.4100 0.3027  -0.0012 0.0336  98  LEU   B N   
948  C  CA  . LEU   B 89  ? 0.6571 0.6099 0.4115 0.3042  0.0033  0.0376  98  LEU   B CA  
949  C  C   . LEU   B 89  ? 0.6440 0.6069 0.4203 0.2953  0.0188  0.0493  98  LEU   B C   
950  O  O   . LEU   B 89  ? 0.6436 0.6042 0.4373 0.2766  0.0219  0.0464  98  LEU   B O   
951  C  CB  . LEU   B 89  ? 0.6562 0.6040 0.4194 0.2905  -0.0057 0.0262  98  LEU   B CB  
952  C  CG  . LEU   B 89  ? 0.6621 0.6216 0.4451 0.2870  0.0001  0.0297  98  LEU   B CG  
953  C  CD1 . LEU   B 89  ? 0.6705 0.6416 0.4479 0.3078  0.0047  0.0389  98  LEU   B CD1 
954  C  CD2 . LEU   B 89  ? 0.6689 0.6267 0.4571 0.2766  -0.0110 0.0184  98  LEU   B CD2 
955  N  N   . ALA   B 90  ? 0.6277 0.6016 0.4021 0.3087  0.0285  0.0626  99  ALA   B N   
956  C  CA  . ALA   B 90  ? 0.6079 0.5911 0.4025 0.3003  0.0426  0.0747  99  ALA   B CA  
957  C  C   . ALA   B 90  ? 0.5963 0.5826 0.4083 0.2970  0.0506  0.0800  99  ALA   B C   
958  O  O   . ALA   B 90  ? 0.6020 0.5935 0.4081 0.3130  0.0515  0.0851  99  ALA   B O   
959  C  CB  . ALA   B 90  ? 0.6009 0.5968 0.3885 0.3158  0.0500  0.0885  99  ALA   B CB  
960  N  N   . VAL   B 91  ? 0.5808 0.5636 0.4129 0.2780  0.0569  0.0792  100 VAL   B N   
961  C  CA  . VAL   B 91  ? 0.5716 0.5539 0.4197 0.2751  0.0657  0.0844  100 VAL   B CA  
962  C  C   . VAL   B 91  ? 0.5790 0.5641 0.4427 0.2666  0.0785  0.0959  100 VAL   B C   
963  O  O   . VAL   B 91  ? 0.5780 0.5578 0.4535 0.2482  0.0804  0.0912  100 VAL   B O   
964  C  CB  . VAL   B 91  ? 0.5591 0.5329 0.4161 0.2611  0.0616  0.0722  100 VAL   B CB  
965  C  CG1 . VAL   B 91  ? 0.5575 0.5293 0.4288 0.2611  0.0713  0.0777  100 VAL   B CG1 
966  C  CG2 . VAL   B 91  ? 0.5579 0.5310 0.4017 0.2664  0.0478  0.0611  100 VAL   B CG2 
967  N  N   . PRO   B 92  ? 0.5851 0.5796 0.4486 0.2796  0.0868  0.1114  101 PRO   B N   
968  C  CA  . PRO   B 92  ? 0.5876 0.5865 0.4679 0.2696  0.0983  0.1234  101 PRO   B CA  
969  C  C   . PRO   B 92  ? 0.5974 0.5860 0.4957 0.2609  0.1086  0.1286  101 PRO   B C   
970  O  O   . PRO   B 92  ? 0.6034 0.5862 0.4997 0.2703  0.1099  0.1290  101 PRO   B O   
971  C  CB  . PRO   B 92  ? 0.5916 0.6068 0.4632 0.2884  0.1028  0.1389  101 PRO   B CB  
972  C  CG  . PRO   B 92  ? 0.6016 0.6179 0.4505 0.3100  0.0944  0.1344  101 PRO   B CG  
973  C  CD  . PRO   B 92  ? 0.5797 0.5828 0.4275 0.3039  0.0860  0.1192  101 PRO   B CD  
974  N  N   . PRO   B 93  ? 0.5947 0.5804 0.5103 0.2431  0.1157  0.1323  102 PRO   B N   
975  C  CA  . PRO   B 93  ? 0.5948 0.5654 0.5259 0.2344  0.1254  0.1362  102 PRO   B CA  
976  C  C   . PRO   B 93  ? 0.5972 0.5682 0.5288 0.2517  0.1351  0.1529  102 PRO   B C   
977  O  O   . PRO   B 93  ? 0.5897 0.5755 0.5189 0.2631  0.1397  0.1678  102 PRO   B O   
978  C  CB  . PRO   B 93  ? 0.5984 0.5692 0.5460 0.2136  0.1300  0.1390  102 PRO   B CB  
979  C  CG  . PRO   B 93  ? 0.5999 0.5832 0.5400 0.2080  0.1199  0.1296  102 PRO   B CG  
980  C  CD  . PRO   B 93  ? 0.5811 0.5763 0.5022 0.2298  0.1143  0.1321  102 PRO   B CD  
981  N  N   . GLY   B 94  ? 0.5995 0.5560 0.5322 0.2558  0.1381  0.1506  103 GLY   B N   
982  C  CA  . GLY   B 94  ? 0.5993 0.5543 0.5313 0.2735  0.1473  0.1660  103 GLY   B CA  
983  C  C   . GLY   B 94  ? 0.6023 0.5751 0.5163 0.2986  0.1430  0.1720  103 GLY   B C   
984  O  O   . GLY   B 94  ? 0.6010 0.5760 0.5124 0.3158  0.1505  0.1862  103 GLY   B O   
985  N  N   . GLU   B 95  ? 0.6045 0.5890 0.5048 0.3017  0.1308  0.1615  104 GLU   B N   
986  C  CA  . GLU   B 95  ? 0.6135 0.6130 0.4938 0.3251  0.1249  0.1647  104 GLU   B CA  
987  C  C   . GLU   B 95  ? 0.6372 0.6357 0.5039 0.3287  0.1101  0.1466  104 GLU   B C   
988  O  O   . GLU   B 95  ? 0.6416 0.6325 0.5123 0.3118  0.1029  0.1316  104 GLU   B O   
989  C  CB  . GLU   B 95  ? 0.6235 0.6378 0.4968 0.3288  0.1242  0.1707  104 GLU   B CB  
990  C  CG  . GLU   B 95  ? 0.6480 0.6690 0.5363 0.3260  0.1390  0.1913  104 GLU   B CG  
991  C  CD  . GLU   B 95  ? 0.7019 0.7412 0.5867 0.3283  0.1393  0.1981  104 GLU   B CD  
992  O  OE1 . GLU   B 95  ? 0.7016 0.7444 0.5722 0.3297  0.1277  0.1850  104 GLU   B OE1 
993  O  OE2 . GLU   B 95  ? 0.7133 0.7639 0.6098 0.3292  0.1514  0.2175  104 GLU   B OE2 
994  N  N   . ARG   B 96  ? 0.6532 0.6607 0.5039 0.3504  0.1051  0.1482  105 ARG   B N   
995  C  CA  . ARG   B 96  ? 0.6791 0.6882 0.5168 0.3555  0.0901  0.1323  105 ARG   B CA  
996  C  C   . ARG   B 96  ? 0.6935 0.7020 0.5192 0.3490  0.0770  0.1182  105 ARG   B C   
997  O  O   . ARG   B 96  ? 0.7030 0.7163 0.5204 0.3537  0.0783  0.1235  105 ARG   B O   
998  C  CB  . ARG   B 96  ? 0.7165 0.7377 0.5382 0.3820  0.0880  0.1392  105 ARG   B CB  
999  C  CG  . ARG   B 96  ? 0.7801 0.8055 0.5896 0.3877  0.0715  0.1235  105 ARG   B CG  
1000 C  CD  . ARG   B 96  ? 0.8328 0.8690 0.6373 0.4084  0.0729  0.1311  105 ARG   B CD  
1001 N  NE  . ARG   B 96  ? 0.8912 0.9382 0.6804 0.4322  0.0788  0.1463  105 ARG   B NE  
1002 C  CZ  . ARG   B 96  ? 0.9263 0.9761 0.7221 0.4434  0.0946  0.1663  105 ARG   B CZ  
1003 N  NH1 . ARG   B 96  ? 0.9164 0.9558 0.7331 0.4324  0.1057  0.1725  105 ARG   B NH1 
1004 N  NH2 . ARG   B 96  ? 0.9272 0.9892 0.7078 0.4660  0.0997  0.1806  105 ARG   B NH2 
1005 N  N   . ALA   B 97  ? 0.6935 0.6962 0.5190 0.3380  0.0652  0.1014  106 ALA   B N   
1006 C  CA  . ALA   B 97  ? 0.7006 0.6990 0.5145 0.3309  0.0518  0.0871  106 ALA   B CA  
1007 C  C   . ALA   B 97  ? 0.7156 0.7197 0.5043 0.3518  0.0433  0.0866  106 ALA   B C   
1008 O  O   . ALA   B 97  ? 0.7267 0.7388 0.5064 0.3689  0.0405  0.0891  106 ALA   B O   
1009 C  CB  . ALA   B 97  ? 0.6988 0.6929 0.5176 0.3191  0.0413  0.0723  106 ALA   B CB  
1010 N  N   . LYS   B 98  ? 0.7202 0.7209 0.4964 0.3522  0.0394  0.0838  107 LYS   B N   
1011 C  CA  . LYS   B 98  ? 0.7342 0.7380 0.4833 0.3739  0.0319  0.0829  107 LYS   B CA  
1012 C  C   . LYS   B 98  ? 0.7338 0.7256 0.4679 0.3689  0.0214  0.0710  107 LYS   B C   
1013 O  O   . LYS   B 98  ? 0.7277 0.7164 0.4714 0.3556  0.0267  0.0730  107 LYS   B O   
1014 C  CB  . LYS   B 98  ? 0.7730 0.7905 0.5200 0.3915  0.0458  0.1023  107 LYS   B CB  
1015 C  CG  . LYS   B 98  ? 0.8634 0.8860 0.5846 0.4128  0.0434  0.1054  107 LYS   B CG  
1016 C  CD  . LYS   B 98  ? 0.9297 0.9678 0.6596 0.4200  0.0608  0.1271  107 LYS   B CD  
1017 C  CE  . LYS   B 98  ? 0.9763 1.0128 0.7329 0.3952  0.0696  0.1314  107 LYS   B CE  
1018 N  NZ  . LYS   B 98  ? 1.0008 1.0535 0.7640 0.4003  0.0830  0.1499  107 LYS   B NZ  
1019 N  N   . ASN   B 99  ? 0.7422 0.7261 0.4529 0.3788  0.0060  0.0581  108 ASN   B N   
1020 C  CA  . ASN   B 99  ? 0.7619 0.7295 0.4546 0.3762  -0.0053 0.0459  108 ASN   B CA  
1021 C  C   . ASN   B 99  ? 0.7766 0.7471 0.4488 0.3964  -0.0009 0.0536  108 ASN   B C   
1022 O  O   . ASN   B 99  ? 0.7873 0.7663 0.4419 0.4197  -0.0006 0.0585  108 ASN   B O   
1023 C  CB  . ASN   B 99  ? 0.7841 0.7398 0.4589 0.3792  -0.0241 0.0288  108 ASN   B CB  
1024 C  CG  . ASN   B 99  ? 0.8204 0.7750 0.5143 0.3593  -0.0308 0.0199  108 ASN   B CG  
1025 O  OD1 . ASN   B 99  ? 0.8270 0.7946 0.5429 0.3532  -0.0220 0.0272  108 ASN   B OD1 
1026 N  ND2 . ASN   B 99  ? 0.8298 0.7689 0.5153 0.3494  -0.0464 0.0044  108 ASN   B ND2 
1027 N  N   . ILE   B 100 ? 0.7767 0.7419 0.4497 0.3891  0.0024  0.0550  109 ILE   B N   
1028 C  CA  . ILE   B 100 ? 0.7879 0.7584 0.4425 0.4086  0.0072  0.0631  109 ILE   B CA  
1029 C  C   . ILE   B 100 ? 0.8062 0.7547 0.4372 0.4106  -0.0050 0.0497  109 ILE   B C   
1030 O  O   . ILE   B 100 ? 0.8120 0.7523 0.4525 0.3935  -0.0051 0.0468  109 ILE   B O   
1031 C  CB  . ILE   B 100 ? 0.7844 0.7725 0.4613 0.4009  0.0233  0.0797  109 ILE   B CB  
1032 C  CG1 . ILE   B 100 ? 0.7878 0.7913 0.4915 0.3933  0.0354  0.0920  109 ILE   B CG1 
1033 C  CG2 . ILE   B 100 ? 0.7920 0.7919 0.4514 0.4237  0.0293  0.0906  109 ILE   B CG2 
1034 C  CD1 . ILE   B 100 ? 0.8024 0.8201 0.4961 0.4174  0.0410  0.1034  109 ILE   B CD1 
1035 N  N   . GLN   B 101 ? 0.8191 0.7568 0.4182 0.4319  -0.0154 0.0414  110 GLN   B N   
1036 C  CA  . GLN   B 101 ? 0.8406 0.7518 0.4139 0.4354  -0.0277 0.0277  110 GLN   B CA  
1037 C  C   . GLN   B 101 ? 0.8480 0.7622 0.4102 0.4478  -0.0197 0.0366  110 GLN   B C   
1038 O  O   . GLN   B 101 ? 0.8540 0.7874 0.4082 0.4695  -0.0101 0.0494  110 GLN   B O   
1039 C  CB  . GLN   B 101 ? 0.8693 0.7648 0.4103 0.4536  -0.0428 0.0137  110 GLN   B CB  
1040 C  CG  . GLN   B 101 ? 0.9124 0.7741 0.4270 0.4541  -0.0573 -0.0026 110 GLN   B CG  
1041 C  CD  . GLN   B 101 ? 0.9608 0.8046 0.4479 0.4653  -0.0748 -0.0194 110 GLN   B CD  
1042 O  OE1 . GLN   B 101 ? 0.9568 0.8096 0.4538 0.4594  -0.0806 -0.0236 110 GLN   B OE1 
1043 N  NE2 . GLN   B 101 ? 0.9919 0.8095 0.4430 0.4821  -0.0841 -0.0297 110 GLN   B NE2 
1044 N  N   . THR   B 102 ? 0.8451 0.7420 0.4067 0.4352  -0.0235 0.0307  111 THR   B N   
1045 C  CA  . THR   B 102 ? 0.8473 0.7475 0.3985 0.4470  -0.0168 0.0387  111 THR   B CA  
1046 C  C   . THR   B 102 ? 0.8614 0.7272 0.3916 0.4438  -0.0287 0.0248  111 THR   B C   
1047 O  O   . THR   B 102 ? 0.8666 0.7092 0.3976 0.4269  -0.0405 0.0109  111 THR   B O   
1048 C  CB  . THR   B 102 ? 0.8528 0.7794 0.4385 0.4299  -0.0023 0.0539  111 THR   B CB  
1049 O  OG1 . THR   B 102 ? 0.8678 0.8076 0.4456 0.4448  0.0057  0.0652  111 THR   B OG1 
1050 C  CG2 . THR   B 102 ? 0.8536 0.7683 0.4603 0.3992  -0.0060 0.0466  111 THR   B CG2 
1051 N  N   . LEU   B 103 ? 0.8670 0.7295 0.3778 0.4609  -0.0255 0.0294  112 LEU   B N   
1052 C  CA  . LEU   B 103 ? 0.8871 0.7169 0.3796 0.4581  -0.0343 0.0193  112 LEU   B CA  
1053 C  C   . LEU   B 103 ? 0.8767 0.7240 0.3920 0.4448  -0.0238 0.0313  112 LEU   B C   
1054 O  O   . LEU   B 103 ? 0.8680 0.7440 0.3882 0.4577  -0.0119 0.0463  112 LEU   B O   
1055 C  CB  . LEU   B 103 ? 0.9075 0.7157 0.3570 0.4892  -0.0395 0.0143  112 LEU   B CB  
1056 C  CG  . LEU   B 103 ? 0.9462 0.7166 0.3780 0.4844  -0.0480 0.0047  112 LEU   B CG  
1057 C  CD1 . LEU   B 103 ? 0.9758 0.7054 0.3930 0.4732  -0.0656 -0.0154 112 LEU   B CD1 
1058 C  CD2 . LEU   B 103 ? 0.9615 0.7258 0.3626 0.5144  -0.0441 0.0097  112 LEU   B CD2 
1059 N  N   . PRO   B 104 ? 0.8716 0.7035 0.4006 0.4194  -0.0283 0.0251  113 PRO   B N   
1060 C  CA  . PRO   B 104 ? 0.8555 0.7055 0.4060 0.4060  -0.0192 0.0355  113 PRO   B CA  
1061 C  C   . PRO   B 104 ? 0.8679 0.7131 0.3981 0.4231  -0.0169 0.0407  113 PRO   B C   
1062 O  O   . PRO   B 104 ? 0.8916 0.7064 0.3887 0.4406  -0.0248 0.0328  113 PRO   B O   
1063 C  CB  . PRO   B 104 ? 0.8595 0.6919 0.4259 0.3765  -0.0255 0.0263  113 PRO   B CB  
1064 C  CG  . PRO   B 104 ? 0.8746 0.6904 0.4371 0.3719  -0.0355 0.0141  113 PRO   B CG  
1065 C  CD  . PRO   B 104 ? 0.8732 0.6757 0.4023 0.4002  -0.0411 0.0097  113 PRO   B CD  
1066 N  N   . GLY   B 105 ? 0.8483 0.7243 0.3993 0.4176  -0.0064 0.0540  114 GLY   B N   
1067 C  CA  . GLY   B 105 ? 0.8553 0.7357 0.3952 0.4298  -0.0028 0.0616  114 GLY   B CA  
1068 C  C   . GLY   B 105 ? 0.8577 0.7256 0.4079 0.4071  -0.0057 0.0581  114 GLY   B C   
1069 O  O   . GLY   B 105 ? 0.8626 0.7122 0.4228 0.3849  -0.0119 0.0482  114 GLY   B O   
1070 N  N   . ILE   B 106 ? 0.8508 0.7306 0.3989 0.4131  -0.0011 0.0669  115 ILE   B N   
1071 C  CA  . ILE   B 106 ? 0.8482 0.7173 0.4029 0.3948  -0.0034 0.0650  115 ILE   B CA  
1072 C  C   . ILE   B 106 ? 0.8333 0.7437 0.4142 0.3846  0.0053  0.0773  115 ILE   B C   
1073 O  O   . ILE   B 106 ? 0.8309 0.7691 0.4103 0.4016  0.0118  0.0891  115 ILE   B O   
1074 C  CB  . ILE   B 106 ? 0.8765 0.7093 0.3960 0.4126  -0.0092 0.0616  115 ILE   B CB  
1075 C  CG1 . ILE   B 106 ? 0.9131 0.7001 0.4041 0.4215  -0.0199 0.0475  115 ILE   B CG1 
1076 C  CG2 . ILE   B 106 ? 0.8879 0.7108 0.4125 0.3961  -0.0105 0.0621  115 ILE   B CG2 
1077 C  CD1 . ILE   B 106 ? 0.9319 0.6974 0.4345 0.3957  -0.0276 0.0358  115 ILE   B CD1 
1078 N  N   . PHE   B 107 ? 0.8259 0.7398 0.4293 0.3574  0.0049  0.0743  116 PHE   B N   
1079 C  CA  . PHE   B 107 ? 0.8139 0.7598 0.4383 0.3452  0.0105  0.0827  116 PHE   B CA  
1080 C  C   . PHE   B 107 ? 0.8374 0.7591 0.4412 0.3492  0.0061  0.0813  116 PHE   B C   
1081 O  O   . PHE   B 107 ? 0.8488 0.7373 0.4461 0.3371  0.0001  0.0719  116 PHE   B O   
1082 C  CB  . PHE   B 107 ? 0.7981 0.7517 0.4513 0.3150  0.0111  0.0775  116 PHE   B CB  
1083 C  CG  . PHE   B 107 ? 0.7791 0.7643 0.4596 0.3059  0.0176  0.0820  116 PHE   B CG  
1084 C  CD1 . PHE   B 107 ? 0.7817 0.7859 0.4616 0.3233  0.0225  0.0904  116 PHE   B CD1 
1085 C  CD2 . PHE   B 107 ? 0.7723 0.7672 0.4783 0.2807  0.0193  0.0785  116 PHE   B CD2 
1086 C  CE1 . PHE   B 107 ? 0.7715 0.8022 0.4770 0.3142  0.0290  0.0959  116 PHE   B CE1 
1087 C  CE2 . PHE   B 107 ? 0.7679 0.7875 0.4979 0.2723  0.0254  0.0828  116 PHE   B CE2 
1088 C  CZ  . PHE   B 107 ? 0.7609 0.7975 0.4912 0.2884  0.0302  0.0918  116 PHE   B CZ  
1089 N  N   . LYS   B 108 ? 0.8462 0.7835 0.4391 0.3672  0.0093  0.0913  117 LYS   B N   
1090 C  CA  . LYS   B 108 ? 0.8768 0.7918 0.4493 0.3733  0.0063  0.0920  117 LYS   B CA  
1091 C  C   . LYS   B 108 ? 0.8641 0.8083 0.4573 0.3560  0.0092  0.0976  117 LYS   B C   
1092 O  O   . LYS   B 108 ? 0.8453 0.8320 0.4520 0.3604  0.0144  0.1078  117 LYS   B O   
1093 C  CB  . LYS   B 108 ? 0.9253 0.8384 0.4698 0.4068  0.0079  0.0999  117 LYS   B CB  
1094 C  CG  . LYS   B 108 ? 1.0244 0.8946 0.5372 0.4265  0.0027  0.0917  117 LYS   B CG  
1095 C  CD  . LYS   B 108 ? 1.1304 0.9821 0.6080 0.4582  0.0027  0.0969  117 LYS   B CD  
1096 C  CE  . LYS   B 108 ? 1.2309 1.0340 0.6735 0.4772  -0.0039 0.0862  117 LYS   B CE  
1097 N  NZ  . LYS   B 108 ? 1.2714 1.0812 0.6878 0.5149  0.0002  0.0933  117 LYS   B NZ  
1098 N  N   . THR   B 109 ? 0.8707 0.7943 0.4671 0.3358  0.0058  0.0911  118 THR   B N   
1099 C  CA  . THR   B 109 ? 0.8620 0.8105 0.4751 0.3194  0.0079  0.0948  118 THR   B CA  
1100 C  C   . THR   B 109 ? 0.8814 0.8064 0.4735 0.3246  0.0057  0.0975  118 THR   B C   
1101 O  O   . THR   B 109 ? 0.9028 0.7854 0.4700 0.3353  0.0020  0.0944  118 THR   B O   
1102 C  CB  . THR   B 109 ? 0.8640 0.8171 0.5030 0.2902  0.0078  0.0864  118 THR   B CB  
1103 O  OG1 . THR   B 109 ? 0.8906 0.8042 0.5206 0.2796  0.0034  0.0781  118 THR   B OG1 
1104 C  CG2 . THR   B 109 ? 0.8554 0.8240 0.5126 0.2857  0.0100  0.0838  118 THR   B CG2 
1105 N  N   . LYS   B 110 ? 0.8743 0.8255 0.4759 0.3164  0.0078  0.1031  119 LYS   B N   
1106 C  CA  . LYS   B 110 ? 0.8950 0.8283 0.4783 0.3206  0.0068  0.1076  119 LYS   B CA  
1107 C  C   . LYS   B 110 ? 0.9169 0.8071 0.4944 0.3045  0.0036  0.0998  119 LYS   B C   
1108 O  O   . LYS   B 110 ? 0.9370 0.7958 0.4927 0.3119  0.0023  0.1032  119 LYS   B O   
1109 C  CB  . LYS   B 110 ? 0.8899 0.8660 0.4864 0.3144  0.0093  0.1147  119 LYS   B CB  
1110 C  CG  . LYS   B 110 ? 0.9149 0.9082 0.5370 0.2858  0.0095  0.1075  119 LYS   B CG  
1111 C  CD  . LYS   B 110 ? 0.9427 0.9801 0.5759 0.2813  0.0106  0.1132  119 LYS   B CD  
1112 C  CE  . LYS   B 110 ? 0.9823 1.0270 0.6313 0.2560  0.0104  0.1057  119 LYS   B CE  
1113 N  NZ  . LYS   B 110 ? 1.0021 1.0611 0.6765 0.2385  0.0109  0.0969  119 LYS   B NZ  
1114 N  N   . ASP   B 111 ? 0.9055 0.7946 0.5029 0.2831  0.0027  0.0902  120 ASP   B N   
1115 C  CA  . ASP   B 111 ? 0.9185 0.7731 0.5149 0.2665  -0.0002 0.0833  120 ASP   B CA  
1116 C  C   . ASP   B 111 ? 0.9326 0.7479 0.5171 0.2707  -0.0055 0.0757  120 ASP   B C   
1117 O  O   . ASP   B 111 ? 0.9520 0.7382 0.5357 0.2571  -0.0087 0.0705  120 ASP   B O   
1118 C  CB  . ASP   B 111 ? 0.9279 0.8036 0.5517 0.2414  0.0018  0.0773  120 ASP   B CB  
1119 C  CG  . ASP   B 111 ? 0.9770 0.8846 0.6102 0.2337  0.0054  0.0821  120 ASP   B CG  
1120 O  OD1 . ASP   B 111 ? 0.9866 0.8934 0.6039 0.2444  0.0061  0.0906  120 ASP   B OD1 
1121 O  OD2 . ASP   B 111 ? 0.9972 0.9298 0.6524 0.2176  0.0074  0.0772  120 ASP   B OD2 
1122 N  N   . GLY   B 112 ? 0.9195 0.7362 0.4956 0.2888  -0.0064 0.0752  121 GLY   B N   
1123 C  CA  . GLY   B 112 ? 0.9277 0.7089 0.4896 0.2953  -0.0123 0.0670  121 GLY   B CA  
1124 C  C   . GLY   B 112 ? 0.9055 0.7060 0.4740 0.3049  -0.0115 0.0645  121 GLY   B C   
1125 O  O   . GLY   B 112 ? 0.8858 0.7275 0.4734 0.3034  -0.0059 0.0694  121 GLY   B O   
1126 N  N   . ASP   B 113 ? 0.9063 0.6768 0.4582 0.3148  -0.0174 0.0570  122 ASP   B N   
1127 C  CA  . ASP   B 113 ? 0.8946 0.6810 0.4500 0.3253  -0.0166 0.0549  122 ASP   B CA  
1128 C  C   . ASP   B 113 ? 0.8788 0.6669 0.4553 0.3050  -0.0191 0.0460  122 ASP   B C   
1129 O  O   . ASP   B 113 ? 0.8840 0.6482 0.4632 0.2879  -0.0242 0.0390  122 ASP   B O   
1130 C  CB  . ASP   B 113 ? 0.9382 0.6946 0.4606 0.3519  -0.0214 0.0518  122 ASP   B CB  
1131 C  CG  . ASP   B 113 ? 1.0129 0.7732 0.5138 0.3778  -0.0175 0.0618  122 ASP   B CG  
1132 O  OD1 . ASP   B 113 ? 0.9988 0.7873 0.5114 0.3745  -0.0115 0.0717  122 ASP   B OD1 
1133 O  OD2 . ASP   B 113 ? 1.0744 0.8108 0.5461 0.4023  -0.0206 0.0594  122 ASP   B OD2 
1134 N  N   . ILE   B 114 ? 0.8531 0.6714 0.4458 0.3069  -0.0147 0.0477  123 ILE   B N   
1135 C  CA  . ILE   B 114 ? 0.8377 0.6619 0.4508 0.2907  -0.0156 0.0410  123 ILE   B CA  
1136 C  C   . ILE   B 114 ? 0.8315 0.6630 0.4387 0.3080  -0.0153 0.0409  123 ILE   B C   
1137 O  O   . ILE   B 114 ? 0.8198 0.6725 0.4226 0.3256  -0.0097 0.0496  123 ILE   B O   
1138 C  CB  . ILE   B 114 ? 0.8192 0.6783 0.4644 0.2709  -0.0082 0.0451  123 ILE   B CB  
1139 C  CG1 . ILE   B 114 ? 0.8318 0.6982 0.4813 0.2609  -0.0056 0.0495  123 ILE   B CG1 
1140 C  CG2 . ILE   B 114 ? 0.8176 0.6743 0.4813 0.2524  -0.0097 0.0373  123 ILE   B CG2 
1141 C  CD1 . ILE   B 114 ? 0.8279 0.7309 0.5053 0.2453  0.0014  0.0531  123 ILE   B CD1 
1142 N  N   . GLY   B 115 ? 0.8307 0.6498 0.4403 0.3026  -0.0205 0.0321  124 GLY   B N   
1143 C  CA  . GLY   B 115 ? 0.8316 0.6596 0.4366 0.3184  -0.0199 0.0322  124 GLY   B CA  
1144 C  C   . GLY   B 115 ? 0.8082 0.6770 0.4386 0.3156  -0.0092 0.0423  124 GLY   B C   
1145 O  O   . GLY   B 115 ? 0.7929 0.6793 0.4472 0.2964  -0.0042 0.0453  124 GLY   B O   
1146 N  N   . ALA   B 116 ? 0.8010 0.6848 0.4256 0.3349  -0.0053 0.0479  125 ALA   B N   
1147 C  CA  . ALA   B 116 ? 0.7792 0.7007 0.4286 0.3320  0.0053  0.0591  125 ALA   B CA  
1148 C  C   . ALA   B 116 ? 0.7732 0.7040 0.4198 0.3471  0.0079  0.0622  125 ALA   B C   
1149 O  O   . ALA   B 116 ? 0.7794 0.7033 0.4012 0.3712  0.0059  0.0629  125 ALA   B O   
1150 C  CB  . ALA   B 116 ? 0.7677 0.7150 0.4206 0.3388  0.0125  0.0713  125 ALA   B CB  
1151 N  N   . VAL   B 117 ? 0.7611 0.7067 0.4320 0.3339  0.0126  0.0642  126 VAL   B N   
1152 C  CA  A VAL   B 117 ? 0.7620 0.7181 0.4324 0.3472  0.0162  0.0689  126 VAL   B CA  
1153 C  CA  B VAL   B 117 ? 0.7603 0.7166 0.4321 0.3460  0.0163  0.0687  126 VAL   B CA  
1154 C  C   . VAL   B 117 ? 0.7504 0.7426 0.4381 0.3522  0.0290  0.0859  126 VAL   B C   
1155 O  O   . VAL   B 117 ? 0.7343 0.7445 0.4489 0.3335  0.0354  0.0915  126 VAL   B O   
1156 C  CB  A VAL   B 117 ? 0.7674 0.7142 0.4489 0.3347  0.0129  0.0610  126 VAL   B CB  
1157 C  CB  B VAL   B 117 ? 0.7611 0.7094 0.4488 0.3285  0.0137  0.0610  126 VAL   B CB  
1158 C  CG1 A VAL   B 117 ? 0.7898 0.7042 0.4499 0.3362  -0.0007 0.0456  126 VAL   B CG1 
1159 C  CG1 B VAL   B 117 ? 0.7538 0.7235 0.4585 0.3308  0.0228  0.0706  126 VAL   B CG1 
1160 C  CG2 A VAL   B 117 ? 0.7621 0.7171 0.4735 0.3078  0.0174  0.0610  126 VAL   B CG2 
1161 C  CG2 B VAL   B 117 ? 0.7822 0.7008 0.4487 0.3328  0.0009  0.0467  126 VAL   B CG2 
1162 N  N   . ALA   B 118 ? 0.7561 0.7593 0.4270 0.3784  0.0326  0.0945  127 ALA   B N   
1163 C  CA  . ALA   B 118 ? 0.7486 0.7886 0.4355 0.3850  0.0451  0.1128  127 ALA   B CA  
1164 C  C   . ALA   B 118 ? 0.7537 0.8079 0.4547 0.3865  0.0526  0.1212  127 ALA   B C   
1165 O  O   . ALA   B 118 ? 0.7610 0.8353 0.4571 0.4065  0.0601  0.1343  127 ALA   B O   
1166 C  CB  . ALA   B 118 ? 0.7529 0.8027 0.4163 0.4131  0.0469  0.1204  127 ALA   B CB  
1167 N  N   . LEU   B 119 ? 0.7491 0.7933 0.4673 0.3664  0.0513  0.1148  128 LEU   B N   
1168 C  CA  . LEU   B 119 ? 0.7430 0.7977 0.4756 0.3664  0.0587  0.1229  128 LEU   B CA  
1169 C  C   . LEU   B 119 ? 0.7351 0.8078 0.5025 0.3431  0.0680  0.1319  128 LEU   B C   
1170 O  O   . LEU   B 119 ? 0.7338 0.7998 0.5132 0.3218  0.0648  0.1240  128 LEU   B O   
1171 C  CB  . LEU   B 119 ? 0.7495 0.7793 0.4743 0.3635  0.0503  0.1091  128 LEU   B CB  
1172 C  CG  . LEU   B 119 ? 0.7775 0.7872 0.4675 0.3846  0.0391  0.0981  128 LEU   B CG  
1173 C  CD1 . LEU   B 119 ? 0.7845 0.7707 0.4704 0.3758  0.0283  0.0825  128 LEU   B CD1 
1174 C  CD2 . LEU   B 119 ? 0.7882 0.8120 0.4610 0.4134  0.0441  0.1088  128 LEU   B CD2 
1175 N  N   . ASP   B 120 ? 0.7315 0.8268 0.5144 0.3471  0.0796  0.1486  129 ASP   B N   
1176 C  CA  . ASP   B 120 ? 0.7252 0.8349 0.5411 0.3241  0.0880  0.1570  129 ASP   B CA  
1177 C  C   . ASP   B 120 ? 0.7157 0.8154 0.5457 0.3153  0.0926  0.1579  129 ASP   B C   
1178 O  O   . ASP   B 120 ? 0.7218 0.8255 0.5465 0.3314  0.0979  0.1670  129 ASP   B O   
1179 C  CB  . ASP   B 120 ? 0.7444 0.8888 0.5742 0.3285  0.0983  0.1767  129 ASP   B CB  
1180 C  CG  . ASP   B 120 ? 0.8232 0.9806 0.6858 0.3006  0.1032  0.1814  129 ASP   B CG  
1181 O  OD1 . ASP   B 120 ? 0.8436 0.9971 0.7258 0.2874  0.1093  0.1856  129 ASP   B OD1 
1182 O  OD2 . ASP   B 120 ? 0.8555 1.0259 0.7234 0.2924  0.1004  0.1803  129 ASP   B OD2 
1183 N  N   . TYR   B 121 ? 0.7009 0.7877 0.5473 0.2912  0.0908  0.1486  130 TYR   B N   
1184 C  CA  . TYR   B 121 ? 0.6932 0.7673 0.5537 0.2805  0.0947  0.1473  130 TYR   B CA  
1185 C  C   . TYR   B 121 ? 0.6670 0.7425 0.5539 0.2536  0.0988  0.1470  130 TYR   B C   
1186 O  O   . TYR   B 121 ? 0.6650 0.7478 0.5557 0.2423  0.0952  0.1428  130 TYR   B O   
1187 C  CB  . TYR   B 121 ? 0.7135 0.7628 0.5590 0.2817  0.0846  0.1300  130 TYR   B CB  
1188 C  CG  . TYR   B 121 ? 0.7419 0.7887 0.5642 0.3069  0.0810  0.1306  130 TYR   B CG  
1189 C  CD1 . TYR   B 121 ? 0.7614 0.8094 0.5855 0.3174  0.0870  0.1388  130 TYR   B CD1 
1190 C  CD2 . TYR   B 121 ? 0.7667 0.8104 0.5638 0.3220  0.0721  0.1242  130 TYR   B CD2 
1191 C  CE1 . TYR   B 121 ? 0.7848 0.8338 0.5862 0.3423  0.0836  0.1401  130 TYR   B CE1 
1192 C  CE2 . TYR   B 121 ? 0.7903 0.8319 0.5640 0.3462  0.0684  0.1243  130 TYR   B CE2 
1193 C  CZ  . TYR   B 121 ? 0.8059 0.8514 0.5816 0.3563  0.0738  0.1319  130 TYR   B CZ  
1194 O  OH  . TYR   B 121 ? 0.8437 0.8888 0.5945 0.3813  0.0694  0.1314  130 TYR   B OH  
1195 N  N   . PRO   B 122 ? 0.6459 0.7138 0.5500 0.2435  0.1061  0.1511  131 PRO   B N   
1196 C  CA  . PRO   B 122 ? 0.6237 0.6890 0.5507 0.2176  0.1092  0.1488  131 PRO   B CA  
1197 C  C   . PRO   B 122 ? 0.6121 0.6626 0.5351 0.2030  0.0998  0.1294  131 PRO   B C   
1198 O  O   . PRO   B 122 ? 0.6302 0.6671 0.5369 0.2104  0.0927  0.1182  131 PRO   B O   
1199 C  CB  . PRO   B 122 ? 0.6369 0.6890 0.5763 0.2145  0.1179  0.1548  131 PRO   B CB  
1200 C  CG  . PRO   B 122 ? 0.6489 0.7072 0.5763 0.2394  0.1222  0.1670  131 PRO   B CG  
1201 C  CD  . PRO   B 122 ? 0.6399 0.6999 0.5419 0.2559  0.1118  0.1577  131 PRO   B CD  
1202 N  N   . ALA   B 123 ? 0.5819 0.6363 0.5197 0.1820  0.0995  0.1256  132 ALA   B N   
1203 C  CA  . ALA   B 123 ? 0.5747 0.6174 0.5079 0.1689  0.0914  0.1083  132 ALA   B CA  
1204 C  C   . ALA   B 123 ? 0.5724 0.5900 0.5025 0.1656  0.0903  0.0964  132 ALA   B C   
1205 O  O   . ALA   B 123 ? 0.5839 0.5925 0.5049 0.1612  0.0833  0.0832  132 ALA   B O   
1206 C  CB  . ALA   B 123 ? 0.5642 0.6169 0.5133 0.1479  0.0914  0.1066  132 ALA   B CB  
1207 N  N   . GLY   B 124 ? 0.5603 0.5682 0.4973 0.1694  0.0976  0.1023  133 GLY   B N   
1208 C  CA  . GLY   B 124 ? 0.5519 0.5395 0.4861 0.1701  0.0976  0.0935  133 GLY   B CA  
1209 C  C   . GLY   B 124 ? 0.5426 0.5276 0.4588 0.1872  0.0910  0.0892  133 GLY   B C   
1210 O  O   . GLY   B 124 ? 0.5381 0.5107 0.4521 0.1886  0.0898  0.0819  133 GLY   B O   
1211 N  N   . THR   B 125 ? 0.5398 0.5370 0.4427 0.2010  0.0866  0.0938  134 THR   B N   
1212 C  CA  . THR   B 125 ? 0.5473 0.5409 0.4306 0.2162  0.0781  0.0881  134 THR   B CA  
1213 C  C   . THR   B 125 ? 0.5507 0.5377 0.4255 0.2072  0.0684  0.0741  134 THR   B C   
1214 O  O   . THR   B 125 ? 0.5638 0.5436 0.4248 0.2146  0.0603  0.0669  134 THR   B O   
1215 C  CB  . THR   B 125 ? 0.5616 0.5682 0.4318 0.2363  0.0780  0.0988  134 THR   B CB  
1216 O  OG1 . THR   B 125 ? 0.5735 0.5892 0.4543 0.2423  0.0888  0.1142  134 THR   B OG1 
1217 C  CG2 . THR   B 125 ? 0.5637 0.5639 0.4127 0.2539  0.0694  0.0930  134 THR   B CG2 
1218 N  N   . SER   B 126 ? 0.5405 0.5302 0.4235 0.1910  0.0688  0.0708  135 SER   B N   
1219 C  CA  . SER   B 126 ? 0.5432 0.5283 0.4191 0.1819  0.0613  0.0598  135 SER   B CA  
1220 C  C   . SER   B 126 ? 0.5442 0.5154 0.4176 0.1780  0.0571  0.0489  135 SER   B C   
1221 O  O   . SER   B 126 ? 0.5384 0.5041 0.4230 0.1705  0.0618  0.0461  135 SER   B O   
1222 C  CB  . SER   B 126 ? 0.5544 0.5456 0.4423 0.1645  0.0641  0.0581  135 SER   B CB  
1223 O  OG  . SER   B 126 ? 0.5811 0.5897 0.4729 0.1664  0.0667  0.0682  135 SER   B OG  
1224 N  N   . GLY   B 127 ? 0.5469 0.5125 0.4057 0.1829  0.0483  0.0431  136 GLY   B N   
1225 C  CA  . GLY   B 127 ? 0.5537 0.5091 0.4105 0.1788  0.0430  0.0338  136 GLY   B CA  
1226 C  C   . GLY   B 127 ? 0.5697 0.5212 0.4164 0.1927  0.0371  0.0332  136 GLY   B C   
1227 O  O   . GLY   B 127 ? 0.5815 0.5271 0.4274 0.1894  0.0314  0.0260  136 GLY   B O   
1228 N  N   . SER   B 128 ? 0.5665 0.5229 0.4057 0.2086  0.0382  0.0410  137 SER   B N   
1229 C  CA  . SER   B 128 ? 0.5704 0.5240 0.3970 0.2241  0.0318  0.0401  137 SER   B CA  
1230 C  C   . SER   B 128 ? 0.5816 0.5243 0.3908 0.2256  0.0198  0.0317  137 SER   B C   
1231 O  O   . SER   B 128 ? 0.5844 0.5243 0.3849 0.2248  0.0182  0.0321  137 SER   B O   
1232 C  CB  . SER   B 128 ? 0.5814 0.5441 0.4020 0.2417  0.0367  0.0513  137 SER   B CB  
1233 O  OG  . SER   B 128 ? 0.6088 0.5788 0.4462 0.2397  0.0479  0.0600  137 SER   B OG  
1234 N  N   . PRO   B 129 ? 0.5939 0.5301 0.3985 0.2268  0.0111  0.0242  138 PRO   B N   
1235 C  CA  . PRO   B 129 ? 0.6114 0.5335 0.4004 0.2255  -0.0010 0.0156  138 PRO   B CA  
1236 C  C   . PRO   B 129 ? 0.6311 0.5464 0.3961 0.2440  -0.0072 0.0161  138 PRO   B C   
1237 O  O   . PRO   B 129 ? 0.6343 0.5574 0.3938 0.2602  -0.0048 0.0213  138 PRO   B O   
1238 C  CB  . PRO   B 129 ? 0.6194 0.5403 0.4147 0.2198  -0.0082 0.0082  138 PRO   B CB  
1239 C  CG  . PRO   B 129 ? 0.6136 0.5480 0.4183 0.2290  -0.0019 0.0137  138 PRO   B CG  
1240 C  CD  . PRO   B 129 ? 0.5851 0.5270 0.3997 0.2286  0.0117  0.0234  138 PRO   B CD  
1241 N  N   . ILE   B 130 ? 0.6459 0.5457 0.3956 0.2427  -0.0146 0.0109  139 ILE   B N   
1242 C  CA  . ILE   B 130 ? 0.6650 0.5524 0.3881 0.2602  -0.0221 0.0088  139 ILE   B CA  
1243 C  C   . ILE   B 130 ? 0.6864 0.5553 0.3996 0.2558  -0.0366 -0.0036 139 ILE   B C   
1244 O  O   . ILE   B 130 ? 0.6770 0.5385 0.4001 0.2374  -0.0401 -0.0086 139 ILE   B O   
1245 C  CB  . ILE   B 130 ? 0.6760 0.5581 0.3892 0.2621  -0.0193 0.0126  139 ILE   B CB  
1246 C  CG1 . ILE   B 130 ? 0.6684 0.5733 0.3944 0.2652  -0.0058 0.0251  139 ILE   B CG1 
1247 C  CG2 . ILE   B 130 ? 0.7019 0.5661 0.3845 0.2808  -0.0279 0.0087  139 ILE   B CG2 
1248 C  CD1 . ILE   B 130 ? 0.6716 0.5800 0.4041 0.2547  -0.0012 0.0285  139 ILE   B CD1 
1249 N  N   . LEU   B 131 ? 0.7070 0.5708 0.4026 0.2718  -0.0450 -0.0083 140 LEU   B N   
1250 C  CA  . LEU   B 131 ? 0.7275 0.5771 0.4163 0.2666  -0.0601 -0.0206 140 LEU   B CA  
1251 C  C   . LEU   B 131 ? 0.7644 0.5874 0.4219 0.2782  -0.0726 -0.0294 140 LEU   B C   
1252 O  O   . LEU   B 131 ? 0.7730 0.5926 0.4102 0.2979  -0.0697 -0.0258 140 LEU   B O   
1253 C  CB  . LEU   B 131 ? 0.7226 0.5888 0.4182 0.2734  -0.0624 -0.0215 140 LEU   B CB  
1254 C  CG  . LEU   B 131 ? 0.7219 0.6132 0.4420 0.2711  -0.0484 -0.0110 140 LEU   B CG  
1255 C  CD1 . LEU   B 131 ? 0.7191 0.6244 0.4398 0.2830  -0.0511 -0.0109 140 LEU   B CD1 
1256 C  CD2 . LEU   B 131 ? 0.7175 0.6130 0.4629 0.2476  -0.0431 -0.0104 140 LEU   B CD2 
1257 N  N   . ASP   B 132 ? 0.7856 0.5897 0.4392 0.2660  -0.0865 -0.0410 141 ASP   B N   
1258 C  CA  . ASP   B 132 ? 0.8268 0.6009 0.4496 0.2758  -0.1007 -0.0519 141 ASP   B CA  
1259 C  C   . ASP   B 132 ? 0.8589 0.6354 0.4734 0.2832  -0.1140 -0.0620 141 ASP   B C   
1260 O  O   . ASP   B 132 ? 0.8406 0.6435 0.4751 0.2804  -0.1108 -0.0587 141 ASP   B O   
1261 C  CB  . ASP   B 132 ? 0.8525 0.5983 0.4728 0.2577  -0.1077 -0.0575 141 ASP   B CB  
1262 C  CG  . ASP   B 132 ? 0.8958 0.6418 0.5377 0.2322  -0.1156 -0.0632 141 ASP   B CG  
1263 O  OD1 . ASP   B 132 ? 0.9057 0.6688 0.5588 0.2301  -0.1209 -0.0670 141 ASP   B OD1 
1264 O  OD2 . ASP   B 132 ? 0.9256 0.6558 0.5728 0.2151  -0.1164 -0.0630 141 ASP   B OD2 
1265 N  N   . LYS   B 133 ? 0.8990 0.6478 0.4828 0.2936  -0.1289 -0.0744 142 LYS   B N   
1266 C  CA  . LYS   B 133 ? 0.9276 0.6764 0.4983 0.3024  -0.1438 -0.0859 142 LYS   B CA  
1267 C  C   . LYS   B 133 ? 0.9243 0.6864 0.5213 0.2797  -0.1528 -0.0914 142 LYS   B C   
1268 O  O   . LYS   B 133 ? 0.9228 0.7029 0.5206 0.2870  -0.1594 -0.0953 142 LYS   B O   
1269 C  CB  . LYS   B 133 ? 0.9958 0.7064 0.5274 0.3150  -0.1591 -0.1000 142 LYS   B CB  
1270 C  CG  . LYS   B 133 ? 1.0912 0.7936 0.5961 0.3416  -0.1493 -0.0935 142 LYS   B CG  
1271 C  CD  . LYS   B 133 ? 1.1986 0.8595 0.6617 0.3565  -0.1632 -0.1075 142 LYS   B CD  
1272 C  CE  . LYS   B 133 ? 1.2667 0.9269 0.7033 0.3872  -0.1526 -0.0998 142 LYS   B CE  
1273 N  NZ  . LYS   B 133 ? 1.3286 0.9460 0.7214 0.4045  -0.1655 -0.1139 142 LYS   B NZ  
1274 N  N   . CYS   B 134 ? 0.9168 0.6738 0.5360 0.2534  -0.1519 -0.0902 143 CYS   B N   
1275 C  CA  . CYS   B 134 ? 0.9033 0.6772 0.5510 0.2310  -0.1584 -0.0931 143 CYS   B CA  
1276 C  C   . CYS   B 134 ? 0.8711 0.6828 0.5506 0.2270  -0.1424 -0.0802 143 CYS   B C   
1277 O  O   . CYS   B 134 ? 0.8663 0.6941 0.5725 0.2080  -0.1438 -0.0797 143 CYS   B O   
1278 C  CB  . CYS   B 134 ? 0.9294 0.6806 0.5855 0.2053  -0.1648 -0.0970 143 CYS   B CB  
1279 S  SG  . CYS   B 134 ? 1.0491 0.7484 0.6676 0.2077  -0.1838 -0.1125 143 CYS   B SG  
1280 N  N   . GLY   B 135 ? 0.8479 0.6728 0.5250 0.2442  -0.1271 -0.0695 144 GLY   B N   
1281 C  CA  . GLY   B 135 ? 0.8173 0.6718 0.5214 0.2414  -0.1110 -0.0572 144 GLY   B CA  
1282 C  C   . GLY   B 135 ? 0.7932 0.6478 0.5184 0.2213  -0.1004 -0.0509 144 GLY   B C   
1283 O  O   . GLY   B 135 ? 0.7772 0.6534 0.5251 0.2164  -0.0879 -0.0425 144 GLY   B O   
1284 N  N   . ARG   B 136 ? 0.7862 0.6155 0.5026 0.2103  -0.1053 -0.0549 145 ARG   B N   
1285 C  CA  . ARG   B 136 ? 0.7708 0.5997 0.5046 0.1918  -0.0961 -0.0490 145 ARG   B CA  
1286 C  C   . ARG   B 136 ? 0.7507 0.5842 0.4833 0.1998  -0.0804 -0.0389 145 ARG   B C   
1287 O  O   . ARG   B 136 ? 0.7675 0.5909 0.4784 0.2171  -0.0795 -0.0378 145 ARG   B O   
1288 C  CB  . ARG   B 136 ? 0.8017 0.6020 0.5267 0.1775  -0.1067 -0.0555 145 ARG   B CB  
1289 C  CG  . ARG   B 136 ? 0.8443 0.6455 0.5806 0.1614  -0.1208 -0.0636 145 ARG   B CG  
1290 C  CD  . ARG   B 136 ? 0.9153 0.6851 0.6430 0.1463  -0.1308 -0.0688 145 ARG   B CD  
1291 N  NE  . ARG   B 136 ? 0.9950 0.7321 0.6883 0.1614  -0.1415 -0.0774 145 ARG   B NE  
1292 C  CZ  . ARG   B 136 ? 1.0540 0.7596 0.7272 0.1637  -0.1410 -0.0770 145 ARG   B CZ  
1293 N  NH1 . ARG   B 136 ? 1.0528 0.7564 0.7372 0.1513  -0.1307 -0.0680 145 ARG   B NH1 
1294 N  NH2 . ARG   B 136 ? 1.0748 0.7509 0.7149 0.1803  -0.1505 -0.0853 145 ARG   B NH2 
1295 N  N   . VAL   B 137 ? 0.7108 0.5612 0.4665 0.1880  -0.0680 -0.0317 146 VAL   B N   
1296 C  CA  . VAL   B 137 ? 0.6903 0.5470 0.4474 0.1927  -0.0540 -0.0228 146 VAL   B CA  
1297 C  C   . VAL   B 137 ? 0.6913 0.5283 0.4362 0.1877  -0.0546 -0.0224 146 VAL   B C   
1298 O  O   . VAL   B 137 ? 0.6952 0.5257 0.4482 0.1709  -0.0561 -0.0236 146 VAL   B O   
1299 C  CB  . VAL   B 137 ? 0.6701 0.5492 0.4532 0.1833  -0.0413 -0.0167 146 VAL   B CB  
1300 C  CG1 . VAL   B 137 ? 0.6708 0.5568 0.4543 0.1893  -0.0287 -0.0086 146 VAL   B CG1 
1301 C  CG2 . VAL   B 137 ? 0.6617 0.5582 0.4568 0.1880  -0.0414 -0.0171 146 VAL   B CG2 
1302 N  N   . ILE   B 138 ? 0.6812 0.5099 0.4064 0.2036  -0.0529 -0.0196 147 ILE   B N   
1303 C  CA  . ILE   B 138 ? 0.6812 0.4918 0.3917 0.2035  -0.0531 -0.0181 147 ILE   B CA  
1304 C  C   . ILE   B 138 ? 0.6667 0.4931 0.3859 0.2028  -0.0397 -0.0085 147 ILE   B C   
1305 O  O   . ILE   B 138 ? 0.6795 0.4954 0.3893 0.2018  -0.0387 -0.0060 147 ILE   B O   
1306 C  CB  . ILE   B 138 ? 0.6992 0.4876 0.3788 0.2229  -0.0618 -0.0224 147 ILE   B CB  
1307 C  CG1 . ILE   B 138 ? 0.6995 0.5036 0.3717 0.2447  -0.0567 -0.0180 147 ILE   B CG1 
1308 C  CG2 . ILE   B 138 ? 0.7139 0.4809 0.3838 0.2187  -0.0774 -0.0340 147 ILE   B CG2 
1309 C  CD1 . ILE   B 138 ? 0.7255 0.5114 0.3666 0.2660  -0.0616 -0.0198 147 ILE   B CD1 
1310 N  N   . GLY   B 139 ? 0.6347 0.4854 0.3718 0.2025  -0.0301 -0.0034 148 GLY   B N   
1311 C  CA  . GLY   B 139 ? 0.6175 0.4841 0.3645 0.1998  -0.0187 0.0044  148 GLY   B CA  
1312 C  C   . GLY   B 139 ? 0.5928 0.4814 0.3570 0.2016  -0.0094 0.0094  148 GLY   B C   
1313 O  O   . GLY   B 139 ? 0.5924 0.4844 0.3595 0.2073  -0.0111 0.0078  148 GLY   B O   
1314 N  N   . LEU   B 140 ? 0.5722 0.4752 0.3474 0.1967  0.0001  0.0155  149 LEU   B N   
1315 C  CA  . LEU   B 140 ? 0.5574 0.4782 0.3493 0.1966  0.0096  0.0210  149 LEU   B CA  
1316 C  C   . LEU   B 140 ? 0.5619 0.4950 0.3509 0.2063  0.0155  0.0300  149 LEU   B C   
1317 O  O   . LEU   B 140 ? 0.5675 0.5009 0.3489 0.2064  0.0148  0.0319  149 LEU   B O   
1318 C  CB  . LEU   B 140 ? 0.5388 0.4663 0.3502 0.1788  0.0157  0.0190  149 LEU   B CB  
1319 C  CG  . LEU   B 140 ? 0.5408 0.4633 0.3602 0.1696  0.0127  0.0122  149 LEU   B CG  
1320 C  CD1 . LEU   B 140 ? 0.5150 0.4456 0.3518 0.1562  0.0207  0.0112  149 LEU   B CD1 
1321 C  CD2 . LEU   B 140 ? 0.5517 0.4749 0.3717 0.1795  0.0100  0.0117  149 LEU   B CD2 
1322 N  N   . TYR   B 141 ? 0.5570 0.5015 0.3523 0.2152  0.0213  0.0367  150 TYR   B N   
1323 C  CA  . TYR   B 141 ? 0.5611 0.5212 0.3565 0.2252  0.0278  0.0475  150 TYR   B CA  
1324 C  C   . TYR   B 141 ? 0.5516 0.5260 0.3689 0.2106  0.0366  0.0520  150 TYR   B C   
1325 O  O   . TYR   B 141 ? 0.5444 0.5172 0.3759 0.2012  0.0404  0.0496  150 TYR   B O   
1326 C  CB  . TYR   B 141 ? 0.5661 0.5303 0.3564 0.2429  0.0297  0.0533  150 TYR   B CB  
1327 C  CG  . TYR   B 141 ? 0.5707 0.5549 0.3671 0.2521  0.0390  0.0671  150 TYR   B CG  
1328 C  CD1 . TYR   B 141 ? 0.5727 0.5681 0.3901 0.2448  0.0485  0.0745  150 TYR   B CD1 
1329 C  CD2 . TYR   B 141 ? 0.5858 0.5773 0.3667 0.2686  0.0386  0.0735  150 TYR   B CD2 
1330 C  CE1 . TYR   B 141 ? 0.5763 0.5910 0.4018 0.2509  0.0574  0.0886  150 TYR   B CE1 
1331 C  CE2 . TYR   B 141 ? 0.5852 0.5990 0.3736 0.2770  0.0477  0.0879  150 TYR   B CE2 
1332 C  CZ  . TYR   B 141 ? 0.5856 0.6116 0.3975 0.2669  0.0571  0.0958  150 TYR   B CZ  
1333 O  OH  . TYR   B 141 ? 0.5859 0.6349 0.4080 0.2728  0.0665  0.1114  150 TYR   B OH  
1334 N  N   . GLY   B 142 ? 0.5478 0.5365 0.3677 0.2096  0.0399  0.0584  151 GLY   B N   
1335 C  CA  . GLY   B 142 ? 0.5428 0.5452 0.3836 0.1946  0.0469  0.0619  151 GLY   B CA  
1336 C  C   . GLY   B 142 ? 0.5438 0.5581 0.3865 0.1862  0.0461  0.0625  151 GLY   B C   
1337 O  O   . GLY   B 142 ? 0.5407 0.5685 0.4003 0.1739  0.0509  0.0654  151 GLY   B O   
1338 N  N   . ASN   B 143 ? 0.5494 0.5580 0.3746 0.1926  0.0397  0.0598  152 ASN   B N   
1339 C  CA  . ASN   B 143 ? 0.5548 0.5765 0.3801 0.1869  0.0387  0.0613  152 ASN   B CA  
1340 C  C   . ASN   B 143 ? 0.5640 0.5923 0.3724 0.2055  0.0365  0.0685  152 ASN   B C   
1341 O  O   . ASN   B 143 ? 0.5761 0.5860 0.3642 0.2157  0.0307  0.0646  152 ASN   B O   
1342 C  CB  . ASN   B 143 ? 0.5791 0.5884 0.4011 0.1738  0.0345  0.0513  152 ASN   B CB  
1343 C  CG  . ASN   B 143 ? 0.6161 0.6420 0.4414 0.1656  0.0342  0.0525  152 ASN   B CG  
1344 O  OD1 . ASN   B 143 ? 0.6235 0.6724 0.4606 0.1634  0.0376  0.0592  152 ASN   B OD1 
1345 N  ND2 . ASN   B 143 ? 0.6230 0.6395 0.4384 0.1608  0.0301  0.0469  152 ASN   B ND2 
1346 N  N   . GLY   B 144 ? 0.5567 0.6111 0.3737 0.2098  0.0411  0.0793  153 GLY   B N   
1347 C  CA  . GLY   B 144 ? 0.5764 0.6416 0.3783 0.2295  0.0404  0.0877  153 GLY   B CA  
1348 C  C   . GLY   B 144 ? 0.5832 0.6839 0.3995 0.2286  0.0450  0.0993  153 GLY   B C   
1349 O  O   . GLY   B 144 ? 0.5729 0.6875 0.4043 0.2112  0.0449  0.0976  153 GLY   B O   
1350 N  N   . VAL   B 145 ? 0.5970 0.7146 0.4088 0.2479  0.0490  0.1113  154 VAL   B N   
1351 C  CA  . VAL   B 145 ? 0.6015 0.7572 0.4266 0.2498  0.0533  0.1244  154 VAL   B CA  
1352 C  C   . VAL   B 145 ? 0.6109 0.7897 0.4479 0.2597  0.0618  0.1391  154 VAL   B C   
1353 O  O   . VAL   B 145 ? 0.6201 0.7846 0.4458 0.2741  0.0639  0.1402  154 VAL   B O   
1354 C  CB  . VAL   B 145 ? 0.6211 0.7801 0.4244 0.2671  0.0492  0.1265  154 VAL   B CB  
1355 C  CG1 . VAL   B 145 ? 0.6322 0.7947 0.4160 0.2970  0.0520  0.1358  154 VAL   B CG1 
1356 C  CG2 . VAL   B 145 ? 0.6177 0.8099 0.4357 0.2571  0.0490  0.1319  154 VAL   B CG2 
1357 N  N   . VAL   B 146 ? 0.6038 0.8196 0.4641 0.2515  0.0665  0.1508  155 VAL   B N   
1358 C  CA  . VAL   B 146 ? 0.6100 0.8524 0.4845 0.2596  0.0756  0.1675  155 VAL   B CA  
1359 C  C   . VAL   B 146 ? 0.6332 0.9021 0.4948 0.2849  0.0775  0.1800  155 VAL   B C   
1360 O  O   . VAL   B 146 ? 0.6258 0.9164 0.4905 0.2828  0.0747  0.1823  155 VAL   B O   
1361 C  CB  . VAL   B 146 ? 0.5951 0.8621 0.5053 0.2336  0.0798  0.1737  155 VAL   B CB  
1362 C  CG1 . VAL   B 146 ? 0.5805 0.8808 0.5077 0.2416  0.0899  0.1943  155 VAL   B CG1 
1363 C  CG2 . VAL   B 146 ? 0.6078 0.8450 0.5276 0.2124  0.0790  0.1615  155 VAL   B CG2 
1364 N  N   . ILE   B 147 ? 0.6604 0.9269 0.5050 0.3108  0.0821  0.1875  156 ILE   B N   
1365 C  CA  . ILE   B 147 ? 0.6846 0.9733 0.5126 0.3390  0.0845  0.1989  156 ILE   B CA  
1366 C  C   . ILE   B 147 ? 0.6838 1.0240 0.5369 0.3424  0.0949  0.2213  156 ILE   B C   
1367 O  O   . ILE   B 147 ? 0.6693 1.0240 0.5526 0.3214  0.0999  0.2276  156 ILE   B O   
1368 C  CB  . ILE   B 147 ? 0.7153 0.9723 0.5066 0.3675  0.0826  0.1932  156 ILE   B CB  
1369 C  CG1 . ILE   B 147 ? 0.7321 0.9781 0.5263 0.3693  0.0876  0.1951  156 ILE   B CG1 
1370 C  CG2 . ILE   B 147 ? 0.7430 0.9571 0.5099 0.3652  0.0715  0.1738  156 ILE   B CG2 
1371 C  CD1 . ILE   B 147 ? 0.7658 0.9867 0.5243 0.3987  0.0855  0.1904  156 ILE   B CD1 
1372 N  N   . LYS   B 148 ? 0.6954 1.0637 0.5367 0.3683  0.0982  0.2338  157 LYS   B N   
1373 C  CA  . LYS   B 148 ? 0.6897 1.1124 0.5531 0.3754  0.1083  0.2570  157 LYS   B CA  
1374 C  C   . LYS   B 148 ? 0.6920 1.1275 0.5750 0.3721  0.1187  0.2704  157 LYS   B C   
1375 O  O   . LYS   B 148 ? 0.6693 1.1480 0.5849 0.3611  0.1262  0.2879  157 LYS   B O   
1376 C  CB  . LYS   B 148 ? 0.7246 1.1645 0.5614 0.4127  0.1109  0.2664  157 LYS   B CB  
1377 C  CG  . LYS   B 148 ? 0.8043 1.2265 0.6170 0.4202  0.1013  0.2542  157 LYS   B CG  
1378 C  CD  . LYS   B 148 ? 0.8666 1.3172 0.6608 0.4546  0.1053  0.2674  157 LYS   B CD  
1379 C  CE  . LYS   B 148 ? 0.8828 1.3953 0.7089 0.4468  0.1093  0.2848  157 LYS   B CE  
1380 N  NZ  . LYS   B 148 ? 0.9025 1.4150 0.7415 0.4209  0.0999  0.2746  157 LYS   B NZ  
1381 N  N   . ASN   B 149 ? 0.7141 1.1130 0.5785 0.3808  0.1190  0.2627  158 ASN   B N   
1382 C  CA  . ASN   B 149 ? 0.7160 1.1229 0.5947 0.3807  0.1292  0.2754  158 ASN   B CA  
1383 C  C   . ASN   B 149 ? 0.6956 1.0801 0.5974 0.3485  0.1282  0.2675  158 ASN   B C   
1384 O  O   . ASN   B 149 ? 0.6967 1.0751 0.6034 0.3505  0.1353  0.2745  158 ASN   B O   
1385 C  CB  . ASN   B 149 ? 0.7773 1.1652 0.6210 0.4148  0.1318  0.2755  158 ASN   B CB  
1386 C  CG  . ASN   B 149 ? 0.8750 1.2163 0.6795 0.4278  0.1198  0.2531  158 ASN   B CG  
1387 O  OD1 . ASN   B 149 ? 0.9003 1.2402 0.6840 0.4427  0.1147  0.2486  158 ASN   B OD1 
1388 N  ND2 . ASN   B 149 ? 0.9062 1.2088 0.7007 0.4221  0.1153  0.2394  158 ASN   B ND2 
1389 N  N   . GLY   B 150 ? 0.6724 1.0465 0.5875 0.3210  0.1201  0.2542  159 GLY   B N   
1390 C  CA  . GLY   B 150 ? 0.6541 1.0071 0.5903 0.2903  0.1187  0.2454  159 GLY   B CA  
1391 C  C   . GLY   B 150 ? 0.6562 0.9599 0.5715 0.2905  0.1129  0.2267  159 GLY   B C   
1392 O  O   . GLY   B 150 ? 0.6578 0.9401 0.5856 0.2663  0.1097  0.2153  159 GLY   B O   
1393 N  N   . SER   B 151 ? 0.6537 0.9397 0.5366 0.3183  0.1112  0.2230  160 SER   B N   
1394 C  CA  A SER   B 151 ? 0.6679 0.9105 0.5292 0.3216  0.1047  0.2059  160 SER   B CA  
1395 C  CA  B SER   B 151 ? 0.6676 0.9102 0.5303 0.3203  0.1048  0.2059  160 SER   B CA  
1396 C  C   . SER   B 151 ? 0.6686 0.8843 0.5205 0.3075  0.0929  0.1854  160 SER   B C   
1397 O  O   . SER   B 151 ? 0.6566 0.8864 0.5119 0.3016  0.0894  0.1845  160 SER   B O   
1398 C  CB  A SER   B 151 ? 0.6962 0.9305 0.5246 0.3554  0.1046  0.2075  160 SER   B CB  
1399 C  CB  B SER   B 151 ? 0.6968 0.9299 0.5286 0.3528  0.1056  0.2079  160 SER   B CB  
1400 O  OG  A SER   B 151 ? 0.7443 0.9387 0.5509 0.3586  0.0964  0.1900  160 SER   B OG  
1401 O  OG  B SER   B 151 ? 0.7264 0.9768 0.5393 0.3768  0.1055  0.2141  160 SER   B OG  
1402 N  N   . TYR   B 152 ? 0.6603 0.8396 0.5011 0.3028  0.0871  0.1699  161 TYR   B N   
1403 C  CA  . TYR   B 152 ? 0.6536 0.8066 0.4858 0.2899  0.0770  0.1517  161 TYR   B CA  
1404 C  C   . TYR   B 152 ? 0.6522 0.7768 0.4504 0.3086  0.0685  0.1402  161 TYR   B C   
1405 O  O   . TYR   B 152 ? 0.6622 0.7728 0.4458 0.3234  0.0680  0.1387  161 TYR   B O   
1406 C  CB  . TYR   B 152 ? 0.6532 0.7876 0.5020 0.2669  0.0769  0.1427  161 TYR   B CB  
1407 C  CG  . TYR   B 152 ? 0.6576 0.7797 0.5117 0.2451  0.0703  0.1289  161 TYR   B CG  
1408 C  CD1 . TYR   B 152 ? 0.6555 0.7983 0.5289 0.2277  0.0714  0.1317  161 TYR   B CD1 
1409 C  CD2 . TYR   B 152 ? 0.6811 0.7724 0.5225 0.2410  0.0632  0.1135  161 TYR   B CD2 
1410 C  CE1 . TYR   B 152 ? 0.6708 0.8031 0.5475 0.2089  0.0657  0.1189  161 TYR   B CE1 
1411 C  CE2 . TYR   B 152 ? 0.6915 0.7732 0.5377 0.2220  0.0584  0.1021  161 TYR   B CE2 
1412 C  CZ  . TYR   B 152 ? 0.6935 0.7951 0.5562 0.2066  0.0599  0.1046  161 TYR   B CZ  
1413 O  OH  . TYR   B 152 ? 0.7142 0.8074 0.5796 0.1893  0.0553  0.0933  161 TYR   B OH  
1414 N  N   . VAL   B 153 ? 0.6361 0.7509 0.4219 0.3069  0.0611  0.1317  162 VAL   B N   
1415 C  CA  . VAL   B 153 ? 0.6384 0.7208 0.3942 0.3190  0.0519  0.1191  162 VAL   B CA  
1416 C  C   . VAL   B 153 ? 0.6118 0.6734 0.3741 0.2954  0.0456  0.1053  162 VAL   B C   
1417 O  O   . VAL   B 153 ? 0.5970 0.6698 0.3706 0.2815  0.0456  0.1055  162 VAL   B O   
1418 C  CB  . VAL   B 153 ? 0.6566 0.7415 0.3882 0.3409  0.0494  0.1224  162 VAL   B CB  
1419 C  CG1 . VAL   B 153 ? 0.6793 0.7243 0.3800 0.3506  0.0391  0.1081  162 VAL   B CG1 
1420 C  CG2 . VAL   B 153 ? 0.6631 0.7734 0.3895 0.3654  0.0572  0.1376  162 VAL   B CG2 
1421 N  N   . SER   B 154 ? 0.6065 0.6422 0.3641 0.2903  0.0410  0.0943  163 SER   B N   
1422 C  CA  . SER   B 154 ? 0.6002 0.6186 0.3652 0.2687  0.0362  0.0825  163 SER   B CA  
1423 C  C   . SER   B 154 ? 0.6162 0.6062 0.3575 0.2732  0.0266  0.0719  163 SER   B C   
1424 O  O   . SER   B 154 ? 0.6360 0.6102 0.3558 0.2905  0.0219  0.0692  163 SER   B O   
1425 C  CB  . SER   B 154 ? 0.5995 0.6108 0.3786 0.2581  0.0381  0.0783  163 SER   B CB  
1426 O  OG  . SER   B 154 ? 0.6196 0.6097 0.3986 0.2438  0.0321  0.0658  163 SER   B OG  
1427 N  N   . ALA   B 155 ? 0.6081 0.5902 0.3531 0.2572  0.0234  0.0657  164 ALA   B N   
1428 C  CA  . ALA   B 155 ? 0.6252 0.5789 0.3506 0.2580  0.0149  0.0566  164 ALA   B CA  
1429 C  C   . ALA   B 155 ? 0.6347 0.5668 0.3601 0.2512  0.0096  0.0465  164 ALA   B C   
1430 O  O   . ALA   B 155 ? 0.6122 0.5528 0.3547 0.2436  0.0133  0.0462  164 ALA   B O   
1431 C  CB  . ALA   B 155 ? 0.6219 0.5775 0.3536 0.2423  0.0146  0.0550  164 ALA   B CB  
1432 N  N   . ILE   B 156 ? 0.6598 0.5642 0.3659 0.2545  0.0007  0.0386  165 ILE   B N   
1433 C  CA  . ILE   B 156 ? 0.6757 0.5619 0.3832 0.2458  -0.0057 0.0289  165 ILE   B CA  
1434 C  C   . ILE   B 156 ? 0.6777 0.5588 0.3957 0.2251  -0.0062 0.0253  165 ILE   B C   
1435 O  O   . ILE   B 156 ? 0.6807 0.5445 0.3848 0.2245  -0.0107 0.0237  165 ILE   B O   
1436 C  CB  . ILE   B 156 ? 0.7007 0.5596 0.3816 0.2601  -0.0160 0.0221  165 ILE   B CB  
1437 C  CG1 . ILE   B 156 ? 0.7068 0.5736 0.3750 0.2833  -0.0145 0.0264  165 ILE   B CG1 
1438 C  CG2 . ILE   B 156 ? 0.7132 0.5557 0.3985 0.2472  -0.0240 0.0118  165 ILE   B CG2 
1439 C  CD1 . ILE   B 156 ? 0.7410 0.5813 0.3799 0.2997  -0.0246 0.0190  165 ILE   B CD1 
1440 N  N   . THR   B 157 ? 0.6688 0.5660 0.4105 0.2094  -0.0002 0.0255  166 THR   B N   
1441 C  CA  . THR   B 157 ? 0.6673 0.5645 0.4196 0.1909  0.0012  0.0229  166 THR   B CA  
1442 C  C   . THR   B 157 ? 0.6702 0.5540 0.4278 0.1791  -0.0035 0.0154  166 THR   B C   
1443 O  O   . THR   B 157 ? 0.6590 0.5501 0.4308 0.1745  -0.0015 0.0131  166 THR   B O   
1444 C  CB  . THR   B 157 ? 0.6686 0.5893 0.4414 0.1808  0.0100  0.0262  166 THR   B CB  
1445 O  OG1 . THR   B 157 ? 0.6784 0.6157 0.4498 0.1896  0.0140  0.0340  166 THR   B OG1 
1446 C  CG2 . THR   B 157 ? 0.6697 0.5915 0.4497 0.1645  0.0115  0.0233  166 THR   B CG2 
1447 N  N   . GLN   B 158 ? 0.6821 0.5477 0.4296 0.1739  -0.0092 0.0128  167 GLN   B N   
1448 C  CA  . GLN   B 158 ? 0.6936 0.5487 0.4478 0.1610  -0.0138 0.0071  167 GLN   B CA  
1449 C  C   . GLN   B 158 ? 0.7104 0.5676 0.4718 0.1457  -0.0102 0.0086  167 GLN   B C   
1450 O  O   . GLN   B 158 ? 0.7101 0.5646 0.4617 0.1475  -0.0087 0.0129  167 GLN   B O   
1451 C  CB  . GLN   B 158 ? 0.7118 0.5403 0.4477 0.1672  -0.0250 0.0025  167 GLN   B CB  
1452 C  CG  . GLN   B 158 ? 0.7260 0.5440 0.4696 0.1527  -0.0315 -0.0029 167 GLN   B CG  
1453 C  CD  . GLN   B 158 ? 0.7549 0.5893 0.5167 0.1488  -0.0308 -0.0062 167 GLN   B CD  
1454 O  OE1 . GLN   B 158 ? 0.7624 0.6174 0.5419 0.1430  -0.0220 -0.0038 167 GLN   B OE1 
1455 N  NE2 . GLN   B 158 ? 0.7626 0.5876 0.5195 0.1523  -0.0405 -0.0122 167 GLN   B NE2 
1456 N  N   . GLY   B 159 ? 0.7176 0.5815 0.4956 0.1322  -0.0084 0.0059  168 GLY   B N   
1457 C  CA  . GLY   B 159 ? 0.7362 0.6035 0.5208 0.1185  -0.0045 0.0076  168 GLY   B CA  
1458 C  C   . GLY   B 159 ? 0.7706 0.6183 0.5493 0.1109  -0.0111 0.0074  168 GLY   B C   
1459 O  O   . GLY   B 159 ? 0.7777 0.6056 0.5444 0.1164  -0.0199 0.0050  168 GLY   B O   
1460 N  N   . LYS   B 160 ? 0.7912 0.6439 0.5779 0.0980  -0.0069 0.0101  169 LYS   B N   
1461 C  CA  . LYS   B 160 ? 0.8275 0.6640 0.6123 0.0877  -0.0116 0.0122  169 LYS   B CA  
1462 C  C   . LYS   B 160 ? 0.8512 0.6998 0.6569 0.0747  -0.0111 0.0103  169 LYS   B C   
1463 O  O   . LYS   B 160 ? 0.8433 0.7143 0.6637 0.0723  -0.0036 0.0094  169 LYS   B O   
1464 C  CB  . LYS   B 160 ? 0.8499 0.6852 0.6274 0.0838  -0.0061 0.0194  169 LYS   B CB  
1465 C  CG  . LYS   B 160 ? 0.9144 0.7280 0.6866 0.0745  -0.0103 0.0241  169 LYS   B CG  
1466 C  CD  . LYS   B 160 ? 0.9679 0.7876 0.7384 0.0685  -0.0025 0.0325  169 LYS   B CD  
1467 C  CE  . LYS   B 160 ? 1.0240 0.8195 0.7880 0.0599  -0.0059 0.0393  169 LYS   B CE  
1468 N  NZ  . LYS   B 160 ? 1.0393 0.8450 0.8040 0.0536  0.0031  0.0489  169 LYS   B NZ  
1469 N  N   . ARG   B 161 ? 0.8775 0.7114 0.6848 0.0665  -0.0193 0.0097  170 ARG   B N   
1470 C  CA  . ARG   B 161 ? 0.8906 0.7385 0.7191 0.0533  -0.0196 0.0095  170 ARG   B CA  
1471 C  C   . ARG   B 161 ? 0.9152 0.7569 0.7465 0.0390  -0.0177 0.0173  170 ARG   B C   
1472 O  O   . ARG   B 161 ? 0.9338 0.7490 0.7500 0.0379  -0.0232 0.0199  170 ARG   B O   
1473 C  CB  . ARG   B 161 ? 0.9099 0.7498 0.7410 0.0533  -0.0317 0.0029  170 ARG   B CB  
1474 C  CG  . ARG   B 161 ? 0.9357 0.7923 0.7901 0.0388  -0.0335 0.0035  170 ARG   B CG  
1475 C  CD  . ARG   B 161 ? 0.9812 0.8396 0.8407 0.0410  -0.0446 -0.0040 170 ARG   B CD  
1476 N  NE  . ARG   B 161 ? 1.0068 0.8930 0.8925 0.0305  -0.0431 -0.0025 170 ARG   B NE  
1477 C  CZ  . ARG   B 161 ? 1.0202 0.9221 0.9164 0.0344  -0.0484 -0.0075 170 ARG   B CZ  
1478 N  NH1 . ARG   B 161 ? 1.0265 0.9182 0.9086 0.0483  -0.0556 -0.0145 170 ARG   B NH1 
1479 N  NH2 . ARG   B 161 ? 0.9967 0.9265 0.9171 0.0258  -0.0459 -0.0048 170 ARG   B NH2 
1480 N  N   . GLU   B 162 ? 0.9127 0.7779 0.7616 0.0296  -0.0089 0.0217  171 GLU   B N   
1481 C  CA  . GLU   B 162 ? 0.9325 0.7958 0.7853 0.0166  -0.0054 0.0311  171 GLU   B CA  
1482 C  C   . GLU   B 162 ? 0.9345 0.8009 0.8061 0.0010  -0.0114 0.0331  171 GLU   B C   
1483 O  O   . GLU   B 162 ? 0.9418 0.7963 0.8145 -0.0113 -0.0127 0.0410  171 GLU   B O   
1484 C  CB  . GLU   B 162 ? 0.9665 0.8543 0.8249 0.0164  0.0084  0.0360  171 GLU   B CB  
1485 C  CG  . GLU   B 162 ? 1.0578 0.9420 0.8975 0.0280  0.0133  0.0357  171 GLU   B CG  
1486 C  CD  . GLU   B 162 ? 1.1786 1.0500 1.0041 0.0260  0.0160  0.0451  171 GLU   B CD  
1487 O  OE1 . GLU   B 162 ? 1.2019 1.0817 1.0172 0.0330  0.0226  0.0465  171 GLU   B OE1 
1488 O  OE2 . GLU   B 162 ? 1.2205 1.0731 1.0448 0.0173  0.0113  0.0512  171 GLU   B OE2 
1489 S  S   . DMS   C .   ? 1.1510 1.0578 1.0296 0.0408  0.0799  -0.0782 201 DMS   B S   
1490 O  O   . DMS   C .   ? 1.1459 1.0659 1.0210 0.0499  0.0800  -0.0711 201 DMS   B O   
1491 C  C1  . DMS   C .   ? 1.1604 1.0393 1.0416 0.0474  0.0897  -0.0834 201 DMS   B C1  
1492 C  C2  . DMS   C .   ? 1.1421 1.0500 1.0369 0.0391  0.0783  -0.0648 201 DMS   B C2  
1493 N  N1  . A1B82 D .   ? 0.5544 0.6200 0.4556 0.1441  0.0605  0.0745  202 A1B82 B N1  
1494 N  N3  . A1B82 D .   ? 0.5953 0.6838 0.4924 0.2031  0.0794  0.1188  202 A1B82 B N3  
1495 C  C4  . A1B82 D .   ? 0.5334 0.5982 0.4509 0.0967  0.0546  0.0487  202 A1B82 B C4  
1496 C  C5  . A1B82 D .   ? 0.5385 0.6011 0.4390 0.1019  0.0489  0.0438  202 A1B82 B C5  
1497 C  C6  . A1B82 D .   ? 0.5457 0.6035 0.4307 0.1192  0.0469  0.0485  202 A1B82 B C6  
1498 C  C7  . A1B82 D .   ? 0.5476 0.6054 0.4323 0.1331  0.0500  0.0577  202 A1B82 B C7  
1499 C  C8  . A1B82 D .   ? 0.5455 0.5983 0.4145 0.1201  0.0412  0.0425  202 A1B82 B C8  
1500 C  C10 . A1B82 D .   ? 0.5769 0.6604 0.4881 0.1633  0.0711  0.0977  202 A1B82 B C10 
1501 C  C13 . A1B82 D .   ? 0.5839 0.6933 0.4979 0.1897  0.0816  0.1242  202 A1B82 B C13 
1502 C  C15 . A1B82 D .   ? 0.5698 0.7071 0.5097 0.1602  0.0798  0.1237  202 A1B82 B C15 
1503 O  O1  . A1B82 D .   ? 0.5417 0.6376 0.4757 0.1288  0.0687  0.0887  202 A1B82 B O1  
1504 C  C1  . A1B82 D .   ? 0.5578 0.6395 0.4744 0.1439  0.0668  0.0864  202 A1B82 B C1  
1505 C  C2  . A1B82 D .   ? 0.5444 0.6072 0.4462 0.1289  0.0564  0.0636  202 A1B82 B C2  
1506 C  C3  . A1B82 D .   ? 0.5355 0.6015 0.4543 0.1103  0.0587  0.0598  202 A1B82 B C3  
1507 N  N2  . A1B82 D .   ? 0.5349 0.6016 0.4122 0.1046  0.0401  0.0376  202 A1B82 B N2  
1508 C  C9  . A1B82 D .   ? 0.5337 0.5962 0.4279 0.0916  0.0445  0.0334  202 A1B82 B C9  
1509 C  C11 . A1B82 D .   ? 0.5944 0.6577 0.4900 0.1765  0.0693  0.0933  202 A1B82 B C11 
1510 C  C12 . A1B82 D .   ? 0.6030 0.6693 0.4920 0.1958  0.0730  0.1035  202 A1B82 B C12 
1511 CL CL1 . A1B82 D .   ? 0.6265 0.6699 0.4955 0.2120  0.0687  0.0968  202 A1B82 B CL1 
1512 N  N4  . A1B82 D .   ? 0.5741 0.7116 0.5007 0.1932  0.0880  0.1405  202 A1B82 B N4  
1513 C  C14 . A1B82 D .   ? 0.5626 0.7174 0.5064 0.1743  0.0868  0.1404  202 A1B82 B C14 
1514 C  C16 . A1B82 D .   ? 0.5785 0.6868 0.5002 0.1695  0.0771  0.1138  202 A1B82 B C16 
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