data_7I9V
# 
_entry.id   7I9V 
# 
_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   7I9V         pdb_00007i9v 10.2210/pdb7i9v/pdb 
WWPDB D_1001408498 ?            ?                   
# 
_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                        7I9V 
_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-(2,3,4,5-tetrahydro-1,4-benzoxazepin-7-yl)-1H-indazole-4-carboxamide' 342.780   1  ? ?    ? ? 
5 water       nat water                                                                             18.015    48 ? ?    ? ? 
# 
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-(2,3,4,5-tetrahydro-1,4-benzoxazepin-7-yl)-1H-indazole-4-carboxamide' A1B9G 
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 
A1B9G non-polymer         . '6-chloro-N-(2,3,4,5-tetrahydro-1,4-benzoxazepin-7-yl)-1H-indazole-4-carboxamide' ? 'C17 H15 Cl N4 O2' 
342.780 
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  16  GLY GLY B . n 
B 2 8   GLU 8   17  17  GLU GLU 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 A1B9G 1  202 203 A1B9G LIG B . 
E 5 HOH   1  101 34  HOH   HOH A . 
E 5 HOH   2  102 124 HOH   HOH A . 
E 5 HOH   3  103 118 HOH   HOH A . 
E 5 HOH   4  104 65  HOH   HOH A . 
E 5 HOH   5  105 128 HOH   HOH A . 
E 5 HOH   6  106 125 HOH   HOH A . 
E 5 HOH   7  107 129 HOH   HOH A . 
E 5 HOH   8  108 105 HOH   HOH A . 
E 5 HOH   9  109 28  HOH   HOH A . 
E 5 HOH   10 110 29  HOH   HOH A . 
E 5 HOH   11 111 70  HOH   HOH A . 
F 5 HOH   1  301 126 HOH   HOH B . 
F 5 HOH   2  302 58  HOH   HOH B . 
F 5 HOH   3  303 5   HOH   HOH B . 
F 5 HOH   4  304 123 HOH   HOH B . 
F 5 HOH   5  305 11  HOH   HOH B . 
F 5 HOH   6  306 31  HOH   HOH B . 
F 5 HOH   7  307 1   HOH   HOH B . 
F 5 HOH   8  308 80  HOH   HOH B . 
F 5 HOH   9  309 131 HOH   HOH B . 
F 5 HOH   10 310 2   HOH   HOH B . 
F 5 HOH   11 311 56  HOH   HOH B . 
F 5 HOH   12 312 4   HOH   HOH B . 
F 5 HOH   13 313 61  HOH   HOH B . 
F 5 HOH   14 314 69  HOH   HOH B . 
F 5 HOH   15 315 26  HOH   HOH B . 
F 5 HOH   16 316 9   HOH   HOH B . 
F 5 HOH   17 317 30  HOH   HOH B . 
F 5 HOH   18 318 116 HOH   HOH B . 
F 5 HOH   19 319 68  HOH   HOH B . 
F 5 HOH   20 320 67  HOH   HOH B . 
F 5 HOH   21 321 64  HOH   HOH B . 
F 5 HOH   22 322 35  HOH   HOH B . 
F 5 HOH   23 323 39  HOH   HOH B . 
F 5 HOH   24 324 102 HOH   HOH B . 
F 5 HOH   25 325 43  HOH   HOH B . 
F 5 HOH   26 326 62  HOH   HOH B . 
F 5 HOH   27 327 72  HOH   HOH B . 
F 5 HOH   28 328 107 HOH   HOH B . 
F 5 HOH   29 329 27  HOH   HOH B . 
F 5 HOH   30 330 3   HOH   HOH B . 
F 5 HOH   31 331 130 HOH   HOH B . 
F 5 HOH   32 332 42  HOH   HOH B . 
F 5 HOH   33 333 108 HOH   HOH B . 
F 5 HOH   34 334 87  HOH   HOH B . 
F 5 HOH   35 335 57  HOH   HOH B . 
F 5 HOH   36 336 94  HOH   HOH B . 
F 5 HOH   37 337 127 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           7I9V 
_cell.length_a           42.580 
_cell.length_b           42.580 
_cell.length_c           216.380 
_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                         7I9V 
_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.entry_id          7I9V 
_exptl.method            'X-RAY DIFFRACTION' 
_exptl.crystals_number   1 
# 
_exptl_crystal.id                    1 
_exptl_crystal.pdbx_mosaicity        0.000 
_exptl_crystal.pdbx_mosaicity_esd    ? 
_exptl_crystal.density_Matthews      2.12 
_exptl_crystal.density_diffrn        ? 
_exptl_crystal.density_meas          ? 
_exptl_crystal.density_meas_temp     ? 
_exptl_crystal.density_percent_sol   41.85 
_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   2024-07-23 
_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                     7I9V 
_reflns.pdbx_diffrn_id               1 
_reflns.pdbx_ordinal                 1 
_reflns.observed_criterion_sigma_I   ? 
_reflns.observed_criterion_sigma_F   ? 
_reflns.d_resolution_low             42.580 
_reflns.d_resolution_high            2.350 
_reflns.number_obs                   9121 
_reflns.number_all                   ? 
_reflns.percent_possible_obs         100.000 
_reflns.pdbx_Rmerge_I_obs            0.605 
_reflns.pdbx_Rsym_value              ? 
_reflns.pdbx_netI_over_sigmaI        4.000 
_reflns.B_iso_Wilson_estimate        59.760 
_reflns.pdbx_redundancy              20.300 
_reflns.pdbx_Rrim_I_all              0.621 
_reflns.pdbx_Rpim_I_all              0.136 
_reflns.pdbx_CC_half                 0.990 
_reflns.pdbx_netI_over_av_sigmaI     ? 
_reflns.pdbx_number_measured_all     185294 
_reflns.pdbx_scaling_rejects         0 
_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 2.350  2.410  ? 11838 ? ? 7.803 ? ? ? 18.400 ? 0.400 ? 645 ? ? ? ? 100.000 8.025 1.851 0.472 ? 
1 2 10.510 42.580 ? 1940  ? ? 0.213 ? ? ? 13.300 ? 9.300 ? 146 ? ? ? ? 99.600  0.220 0.054 0.994 ? 
# 
_refine.entry_id                                 7I9V 
_refine.pdbx_refine_id                           'X-RAY DIFFRACTION' 
_refine.ls_d_res_high                            2.3510 
_refine.ls_d_res_low                             42.5800 
_refine.pdbx_ls_sigma_F                          0.000 
_refine.pdbx_data_cutoff_high_absF               ? 
_refine.pdbx_data_cutoff_low_absF                ? 
_refine.ls_percent_reflns_obs                    99.8000 
_refine.ls_number_reflns_obs                     9049 
_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                          0.2416 
_refine.ls_R_factor_R_work                       0.2389 
_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                 4.7600 
_refine.ls_number_reflns_R_free                  431 
_refine.ls_number_reflns_R_work                  ? 
_refine.ls_R_factor_R_free_error                 ? 
_refine.B_iso_mean                               60.5300 
_refine.solvent_model_param_bsol                 ? 
_refine.solvent_model_param_ksol                 ? 
_refine.pdbx_isotropic_thermal_model             ? 
_refine.aniso_B[1][1]                            -5.1294 
_refine.aniso_B[2][2]                            -5.1294 
_refine.aniso_B[3][3]                            10.2588 
_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               0.9350 
_refine.correlation_coeff_Fo_to_Fc_free          0.9100 
_refine.overall_SU_R_Cruickshank_DPI             0.4220 
_refine.pdbx_overall_SU_R_free_Cruickshank_DPI   0.2870 
_refine.pdbx_overall_SU_R_Blow_DPI               0.5060 
_refine.pdbx_overall_SU_R_free_Blow_DPI          0.2970 
_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                                109.670 
_refine.B_iso_min                                22.190 
_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                        7I9V 
_refine_analyze.pdbx_refine_id                  'X-RAY DIFFRACTION' 
_refine_analyze.Luzzati_coordinate_error_obs    0.360 
_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                       2.3510 
_refine_hist.d_res_low                        42.5800 
_refine_hist.pdbx_number_atoms_ligand         28 
_refine_hist.number_atoms_solvent             48 
_refine_hist.number_atoms_total               1552 
_refine_hist.pdbx_number_residues_total       195 
_refine_hist.pdbx_B_iso_mean_ligand           60.20 
_refine_hist.pdbx_B_iso_mean_solvent          54.39 
_refine_hist.pdbx_number_atoms_protein        1476 
_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        533  ?      ? 2.000  SINUSOIDAL   
'X-RAY DIFFRACTION' t_trig_c_planes           ?    ?      ? ?      ?            
'X-RAY DIFFRACTION' t_gen_planes              267  ?      ? 5.000  HARMONIC     
'X-RAY DIFFRACTION' t_it                      1557 ?      ? 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 192  ?      ? 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      1115 ?      ? 4.000  SEMIHARMONIC 
'X-RAY DIFFRACTION' t_bond_d                  1557 0.007  ? 2.000  HARMONIC     
'X-RAY DIFFRACTION' t_angle_deg               2117 0.920  ? 2.000  HARMONIC     
'X-RAY DIFFRACTION' t_omega_torsion           ?    2.890  ? ?      ?            
'X-RAY DIFFRACTION' t_other_torsion           ?    18.490 ? ?      ?            
# 
_refine_ls_shell.d_res_high                       2.3500 
_refine_ls_shell.d_res_low                        2.3900 
_refine_ls_shell.pdbx_total_number_of_bins_used   22 
_refine_ls_shell.percent_reflns_obs               99.0600 
_refine_ls_shell.number_reflns_R_work             411 
_refine_ls_shell.R_factor_all                     ? 
_refine_ls_shell.R_factor_R_work                  0.3889 
_refine_ls_shell.R_factor_R_free                  0.5246 
_refine_ls_shell.percent_reflns_R_free            4.6400 
_refine_ls_shell.number_reflns_R_free             20 
_refine_ls_shell.R_factor_R_free_error            ? 
_refine_ls_shell.number_reflns_all                431 
_refine_ls_shell.number_reflns_obs                ? 
_refine_ls_shell.pdbx_refine_id                   'X-RAY DIFFRACTION' 
_refine_ls_shell.R_factor_obs                     ? 
# 
_struct.entry_id                  7I9V 
_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-0029424-001
;
_struct.pdbx_model_details        ? 
_struct.pdbx_CASP_flag            ? 
_struct.pdbx_model_type_details   ? 
# 
_struct_keywords.entry_id        7I9V 
_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 7I9V A 3 ? 46  ? Q32ZE1 1414 ? 1457 ? 46 89  
2 2 7I9V 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 7I9V SER A 1  ? UNP Q32ZE1 ?   ?    'expression tag'        44  1 
1 7I9V MET A 2  ? UNP Q32ZE1 ?   ?    'expression tag'        45  2 
2 7I9V MET B 1  ? UNP Q32ZE1 ?   ?    'initiating methionine' 10  3 
2 7I9V 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)' 4230 ? 
1 MORE         -26  ? 
1 'SSA (A^2)'  9670 ? 
# 
_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 ? 6 ? 
AA2 ? 5 ? 
AA3 ? 6 ? 
AA4 ? 2 ? 
# 
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 ? anti-parallel 
AA1 3 4 ? anti-parallel 
AA1 4 5 ? anti-parallel 
AA1 5 6 ? 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 
AA4 1 2 ? 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 MET A 8   ? GLY A 14  ? MET A 51  GLY A 57  
AA1 2 GLY B 12  ? THR B 18  ? GLY B 21  THR B 27  
AA1 3 THR B 25  ? GLN B 33  ? THR B 34  GLN B 42  
AA1 4 VAL B 36  ? THR B 39  ? VAL B 45  THR B 48  
AA1 5 LEU B 67  ? TYR B 70  ? LEU B 76  TYR B 79  
AA1 6 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 
AA4 1 LEU B 49  ? SER B 51  ? LEU B 58  SER B 60  
AA4 2 GLY B 54  ? LEU B 56  ? GLY B 63  LEU B 65  
# 
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 N TYR A 9   ? N TYR A 52  O MET B 17  ? O MET B 26  
AA1 2 3 N VAL B 16  ? N VAL B 25  O GLY B 28  ? O GLY B 37  
AA1 3 4 N VAL B 31  ? N VAL B 40  O HIS B 38  ? O HIS B 47  
AA1 4 5 N THR B 39  ? N THR B 48  O VAL B 68  ? O VAL B 77  
AA1 5 6 O SER B 69  ? O SER B 78  N TYR B 59  ? N TYR B 68  
AA2 1 2 N GLU A 23  ? N GLU A 66  O GLN B 101 ? O 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 ILE B 106 ? O ILE B 115 
AA3 3 4 N GLY B 105 ? N GLY B 114 O ALA B 116 ? O ALA B 125 
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 
AA4 1 2 N LEU B 49  ? N LEU B 58  O LEU B 56  ? O LEU B 65  
# 
_pdbx_entry_details.entry_id                   7I9V 
_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 SER A 71 ? ? -119.47 77.69  
2 1 CYS B 80 ? ? 77.25   -14.31 
# 
_pdbx_struct_special_symmetry.id              1 
_pdbx_struct_special_symmetry.PDB_model_num   1 
_pdbx_struct_special_symmetry.auth_asym_id    B 
_pdbx_struct_special_symmetry.auth_comp_id    HOH 
_pdbx_struct_special_symmetry.auth_seq_id     323 
_pdbx_struct_special_symmetry.PDB_ins_code    ? 
_pdbx_struct_special_symmetry.label_asym_id   F 
_pdbx_struct_special_symmetry.label_comp_id   HOH 
_pdbx_struct_special_symmetry.label_seq_id    . 
# 
loop_
_pdbx_refine_tls.pdbx_refine_id 
_pdbx_refine_tls.id 
_pdbx_refine_tls.details 
_pdbx_refine_tls.method 
_pdbx_refine_tls.origin_x 
_pdbx_refine_tls.origin_y 
_pdbx_refine_tls.origin_z 
_pdbx_refine_tls.T[1][1] 
_pdbx_refine_tls.T[2][2] 
_pdbx_refine_tls.T[3][3] 
_pdbx_refine_tls.T[1][2] 
_pdbx_refine_tls.T[1][3] 
_pdbx_refine_tls.T[2][3] 
_pdbx_refine_tls.L[1][1] 
_pdbx_refine_tls.L[2][2] 
_pdbx_refine_tls.L[3][3] 
_pdbx_refine_tls.L[1][2] 
_pdbx_refine_tls.L[1][3] 
_pdbx_refine_tls.L[2][3] 
_pdbx_refine_tls.S[1][1] 
_pdbx_refine_tls.S[2][2] 
_pdbx_refine_tls.S[3][3] 
_pdbx_refine_tls.S[1][2] 
_pdbx_refine_tls.S[1][3] 
_pdbx_refine_tls.S[2][3] 
_pdbx_refine_tls.S[2][1] 
_pdbx_refine_tls.S[3][1] 
_pdbx_refine_tls.S[3][2] 
'X-RAY DIFFRACTION' 1 ? refined -13.4665 -1.8859 -19.2258 -0.0708 -0.1713 -0.2676 0.1631 0.1072 0.0689 4.3190 4.4845 5.0353 
-1.6803 0.4335 0.0198  0.3765 -0.3441 -0.0324 0.4728 0.2337 -0.4106 -0.5318 -0.1017 0.4209 
'X-RAY DIFFRACTION' 2 ? refined -18.3833 0.6617  -15.6498 0.0325  -0.0253 -0.0888 0.1968 0.0422 0.0601 2.0154 2.0848 2.4537 
-1.2648 0.6693 -0.1628 0.4054 -0.3940 -0.0114 0.1785 0.1993 -0.0569 -0.1838 0.0315  0.1257 
# 
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 16 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 GLU 172 ? B GLU 163 
15 1 Y 1 B GLU 173 ? B GLU 164 
16 1 Y 1 B THR 174 ? B THR 165 
17 1 Y 1 B PRO 175 ? B PRO 166 
18 1 Y 1 B VAL 176 ? B VAL 167 
19 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 
A1B9G N1   N  N N 1   
A1B9G N3   N  Y N 2   
A1B9G C4   C  Y N 3   
A1B9G C5   C  Y N 4   
A1B9G C6   C  Y N 5   
A1B9G C7   C  Y N 6   
A1B9G C8   C  N N 7   
A1B9G C10  C  N N 8   
A1B9G C13  C  Y N 9   
A1B9G C15  C  Y N 10  
A1B9G C17  C  Y N 11  
A1B9G O1   O  N N 12  
A1B9G C1   C  N N 13  
A1B9G C2   C  Y N 14  
A1B9G C3   C  Y N 15  
A1B9G N2   N  N N 16  
A1B9G C9   C  N N 17  
A1B9G O2   O  N N 18  
A1B9G C11  C  Y N 19  
A1B9G C12  C  Y N 20  
A1B9G CL1  CL N N 21  
A1B9G C14  C  Y N 22  
A1B9G N4   N  Y N 23  
A1B9G C16  C  Y N 24  
A1B9G H1   H  N N 25  
A1B9G H2   H  N N 26  
A1B9G H3   H  N N 27  
A1B9G H4   H  N N 28  
A1B9G H5   H  N N 29  
A1B9G H6   H  N N 30  
A1B9G H7   H  N N 31  
A1B9G H8   H  N N 32  
A1B9G H9   H  N N 33  
A1B9G H10  H  N N 34  
A1B9G H12  H  N N 35  
A1B9G H13  H  N N 36  
A1B9G H14  H  N N 37  
A1B9G H15  H  N N 38  
A1B9G H16  H  N N 39  
ALA   N    N  N N 40  
ALA   CA   C  N S 41  
ALA   C    C  N N 42  
ALA   O    O  N N 43  
ALA   CB   C  N N 44  
ALA   OXT  O  N N 45  
ALA   H    H  N N 46  
ALA   H2   H  N N 47  
ALA   HA   H  N N 48  
ALA   HB1  H  N N 49  
ALA   HB2  H  N N 50  
ALA   HB3  H  N N 51  
ALA   HXT  H  N N 52  
ARG   N    N  N N 53  
ARG   CA   C  N S 54  
ARG   C    C  N N 55  
ARG   O    O  N N 56  
ARG   CB   C  N N 57  
ARG   CG   C  N N 58  
ARG   CD   C  N N 59  
ARG   NE   N  N N 60  
ARG   CZ   C  N N 61  
ARG   NH1  N  N N 62  
ARG   NH2  N  N N 63  
ARG   OXT  O  N N 64  
ARG   H    H  N N 65  
ARG   H2   H  N N 66  
ARG   HA   H  N N 67  
ARG   HB2  H  N N 68  
ARG   HB3  H  N N 69  
ARG   HG2  H  N N 70  
ARG   HG3  H  N N 71  
ARG   HD2  H  N N 72  
ARG   HD3  H  N N 73  
ARG   HE   H  N N 74  
ARG   HH11 H  N N 75  
ARG   HH12 H  N N 76  
ARG   HH21 H  N N 77  
ARG   HH22 H  N N 78  
ARG   HXT  H  N N 79  
ASN   N    N  N N 80  
ASN   CA   C  N S 81  
ASN   C    C  N N 82  
ASN   O    O  N N 83  
ASN   CB   C  N N 84  
ASN   CG   C  N N 85  
ASN   OD1  O  N N 86  
ASN   ND2  N  N N 87  
ASN   OXT  O  N N 88  
ASN   H    H  N N 89  
ASN   H2   H  N N 90  
ASN   HA   H  N N 91  
ASN   HB2  H  N N 92  
ASN   HB3  H  N N 93  
ASN   HD21 H  N N 94  
ASN   HD22 H  N N 95  
ASN   HXT  H  N N 96  
ASP   N    N  N N 97  
ASP   CA   C  N S 98  
ASP   C    C  N N 99  
ASP   O    O  N N 100 
ASP   CB   C  N N 101 
ASP   CG   C  N N 102 
ASP   OD1  O  N N 103 
ASP   OD2  O  N N 104 
ASP   OXT  O  N N 105 
ASP   H    H  N N 106 
ASP   H2   H  N N 107 
ASP   HA   H  N N 108 
ASP   HB2  H  N N 109 
ASP   HB3  H  N N 110 
ASP   HD2  H  N N 111 
ASP   HXT  H  N N 112 
CYS   N    N  N N 113 
CYS   CA   C  N R 114 
CYS   C    C  N N 115 
CYS   O    O  N N 116 
CYS   CB   C  N N 117 
CYS   SG   S  N N 118 
CYS   OXT  O  N N 119 
CYS   H    H  N N 120 
CYS   H2   H  N N 121 
CYS   HA   H  N N 122 
CYS   HB2  H  N N 123 
CYS   HB3  H  N N 124 
CYS   HG   H  N N 125 
CYS   HXT  H  N N 126 
DMS   S    S  N N 127 
DMS   O    O  N N 128 
DMS   C1   C  N N 129 
DMS   C2   C  N N 130 
DMS   H11  H  N N 131 
DMS   H12  H  N N 132 
DMS   H13  H  N N 133 
DMS   H21  H  N N 134 
DMS   H22  H  N N 135 
DMS   H23  H  N N 136 
GLN   N    N  N N 137 
GLN   CA   C  N S 138 
GLN   C    C  N N 139 
GLN   O    O  N N 140 
GLN   CB   C  N N 141 
GLN   CG   C  N N 142 
GLN   CD   C  N N 143 
GLN   OE1  O  N N 144 
GLN   NE2  N  N N 145 
GLN   OXT  O  N N 146 
GLN   H    H  N N 147 
GLN   H2   H  N N 148 
GLN   HA   H  N N 149 
GLN   HB2  H  N N 150 
GLN   HB3  H  N N 151 
GLN   HG2  H  N N 152 
GLN   HG3  H  N N 153 
GLN   HE21 H  N N 154 
GLN   HE22 H  N N 155 
GLN   HXT  H  N N 156 
GLU   N    N  N N 157 
GLU   CA   C  N S 158 
GLU   C    C  N N 159 
GLU   O    O  N N 160 
GLU   CB   C  N N 161 
GLU   CG   C  N N 162 
GLU   CD   C  N N 163 
GLU   OE1  O  N N 164 
GLU   OE2  O  N N 165 
GLU   OXT  O  N N 166 
GLU   H    H  N N 167 
GLU   H2   H  N N 168 
GLU   HA   H  N N 169 
GLU   HB2  H  N N 170 
GLU   HB3  H  N N 171 
GLU   HG2  H  N N 172 
GLU   HG3  H  N N 173 
GLU   HE2  H  N N 174 
GLU   HXT  H  N N 175 
GLY   N    N  N N 176 
GLY   CA   C  N N 177 
GLY   C    C  N N 178 
GLY   O    O  N N 179 
GLY   OXT  O  N N 180 
GLY   H    H  N N 181 
GLY   H2   H  N N 182 
GLY   HA2  H  N N 183 
GLY   HA3  H  N N 184 
GLY   HXT  H  N N 185 
HIS   N    N  N N 186 
HIS   CA   C  N S 187 
HIS   C    C  N N 188 
HIS   O    O  N N 189 
HIS   CB   C  N N 190 
HIS   CG   C  Y N 191 
HIS   ND1  N  Y N 192 
HIS   CD2  C  Y N 193 
HIS   CE1  C  Y N 194 
HIS   NE2  N  Y N 195 
HIS   OXT  O  N N 196 
HIS   H    H  N N 197 
HIS   H2   H  N N 198 
HIS   HA   H  N N 199 
HIS   HB2  H  N N 200 
HIS   HB3  H  N N 201 
HIS   HD1  H  N N 202 
HIS   HD2  H  N N 203 
HIS   HE1  H  N N 204 
HIS   HE2  H  N N 205 
HIS   HXT  H  N N 206 
HOH   O    O  N N 207 
HOH   H1   H  N N 208 
HOH   H2   H  N N 209 
ILE   N    N  N N 210 
ILE   CA   C  N S 211 
ILE   C    C  N N 212 
ILE   O    O  N N 213 
ILE   CB   C  N S 214 
ILE   CG1  C  N N 215 
ILE   CG2  C  N N 216 
ILE   CD1  C  N N 217 
ILE   OXT  O  N N 218 
ILE   H    H  N N 219 
ILE   H2   H  N N 220 
ILE   HA   H  N N 221 
ILE   HB   H  N N 222 
ILE   HG12 H  N N 223 
ILE   HG13 H  N N 224 
ILE   HG21 H  N N 225 
ILE   HG22 H  N N 226 
ILE   HG23 H  N N 227 
ILE   HD11 H  N N 228 
ILE   HD12 H  N N 229 
ILE   HD13 H  N N 230 
ILE   HXT  H  N N 231 
LEU   N    N  N N 232 
LEU   CA   C  N S 233 
LEU   C    C  N N 234 
LEU   O    O  N N 235 
LEU   CB   C  N N 236 
LEU   CG   C  N N 237 
LEU   CD1  C  N N 238 
LEU   CD2  C  N N 239 
LEU   OXT  O  N N 240 
LEU   H    H  N N 241 
LEU   H2   H  N N 242 
LEU   HA   H  N N 243 
LEU   HB2  H  N N 244 
LEU   HB3  H  N N 245 
LEU   HG   H  N N 246 
LEU   HD11 H  N N 247 
LEU   HD12 H  N N 248 
LEU   HD13 H  N N 249 
LEU   HD21 H  N N 250 
LEU   HD22 H  N N 251 
LEU   HD23 H  N N 252 
LEU   HXT  H  N N 253 
LYS   N    N  N N 254 
LYS   CA   C  N S 255 
LYS   C    C  N N 256 
LYS   O    O  N N 257 
LYS   CB   C  N N 258 
LYS   CG   C  N N 259 
LYS   CD   C  N N 260 
LYS   CE   C  N N 261 
LYS   NZ   N  N N 262 
LYS   OXT  O  N N 263 
LYS   H    H  N N 264 
LYS   H2   H  N N 265 
LYS   HA   H  N N 266 
LYS   HB2  H  N N 267 
LYS   HB3  H  N N 268 
LYS   HG2  H  N N 269 
LYS   HG3  H  N N 270 
LYS   HD2  H  N N 271 
LYS   HD3  H  N N 272 
LYS   HE2  H  N N 273 
LYS   HE3  H  N N 274 
LYS   HZ1  H  N N 275 
LYS   HZ2  H  N N 276 
LYS   HZ3  H  N N 277 
LYS   HXT  H  N N 278 
MET   N    N  N N 279 
MET   CA   C  N S 280 
MET   C    C  N N 281 
MET   O    O  N N 282 
MET   CB   C  N N 283 
MET   CG   C  N N 284 
MET   SD   S  N N 285 
MET   CE   C  N N 286 
MET   OXT  O  N N 287 
MET   H    H  N N 288 
MET   H2   H  N N 289 
MET   HA   H  N N 290 
MET   HB2  H  N N 291 
MET   HB3  H  N N 292 
MET   HG2  H  N N 293 
MET   HG3  H  N N 294 
MET   HE1  H  N N 295 
MET   HE2  H  N N 296 
MET   HE3  H  N N 297 
MET   HXT  H  N N 298 
PHE   N    N  N N 299 
PHE   CA   C  N S 300 
PHE   C    C  N N 301 
PHE   O    O  N N 302 
PHE   CB   C  N N 303 
PHE   CG   C  Y N 304 
PHE   CD1  C  Y N 305 
PHE   CD2  C  Y N 306 
PHE   CE1  C  Y N 307 
PHE   CE2  C  Y N 308 
PHE   CZ   C  Y N 309 
PHE   OXT  O  N N 310 
PHE   H    H  N N 311 
PHE   H2   H  N N 312 
PHE   HA   H  N N 313 
PHE   HB2  H  N N 314 
PHE   HB3  H  N N 315 
PHE   HD1  H  N N 316 
PHE   HD2  H  N N 317 
PHE   HE1  H  N N 318 
PHE   HE2  H  N N 319 
PHE   HZ   H  N N 320 
PHE   HXT  H  N N 321 
PRO   N    N  N N 322 
PRO   CA   C  N S 323 
PRO   C    C  N N 324 
PRO   O    O  N N 325 
PRO   CB   C  N N 326 
PRO   CG   C  N N 327 
PRO   CD   C  N N 328 
PRO   OXT  O  N N 329 
PRO   H    H  N N 330 
PRO   HA   H  N N 331 
PRO   HB2  H  N N 332 
PRO   HB3  H  N N 333 
PRO   HG2  H  N N 334 
PRO   HG3  H  N N 335 
PRO   HD2  H  N N 336 
PRO   HD3  H  N N 337 
PRO   HXT  H  N N 338 
SER   N    N  N N 339 
SER   CA   C  N S 340 
SER   C    C  N N 341 
SER   O    O  N N 342 
SER   CB   C  N N 343 
SER   OG   O  N N 344 
SER   OXT  O  N N 345 
SER   H    H  N N 346 
SER   H2   H  N N 347 
SER   HA   H  N N 348 
SER   HB2  H  N N 349 
SER   HB3  H  N N 350 
SER   HG   H  N N 351 
SER   HXT  H  N N 352 
THR   N    N  N N 353 
THR   CA   C  N S 354 
THR   C    C  N N 355 
THR   O    O  N N 356 
THR   CB   C  N R 357 
THR   OG1  O  N N 358 
THR   CG2  C  N N 359 
THR   OXT  O  N N 360 
THR   H    H  N N 361 
THR   H2   H  N N 362 
THR   HA   H  N N 363 
THR   HB   H  N N 364 
THR   HG1  H  N N 365 
THR   HG21 H  N N 366 
THR   HG22 H  N N 367 
THR   HG23 H  N N 368 
THR   HXT  H  N N 369 
TRP   N    N  N N 370 
TRP   CA   C  N S 371 
TRP   C    C  N N 372 
TRP   O    O  N N 373 
TRP   CB   C  N N 374 
TRP   CG   C  Y N 375 
TRP   CD1  C  Y N 376 
TRP   CD2  C  Y N 377 
TRP   NE1  N  Y N 378 
TRP   CE2  C  Y N 379 
TRP   CE3  C  Y N 380 
TRP   CZ2  C  Y N 381 
TRP   CZ3  C  Y N 382 
TRP   CH2  C  Y N 383 
TRP   OXT  O  N N 384 
TRP   H    H  N N 385 
TRP   H2   H  N N 386 
TRP   HA   H  N N 387 
TRP   HB2  H  N N 388 
TRP   HB3  H  N N 389 
TRP   HD1  H  N N 390 
TRP   HE1  H  N N 391 
TRP   HE3  H  N N 392 
TRP   HZ2  H  N N 393 
TRP   HZ3  H  N N 394 
TRP   HH2  H  N N 395 
TRP   HXT  H  N N 396 
TYR   N    N  N N 397 
TYR   CA   C  N S 398 
TYR   C    C  N N 399 
TYR   O    O  N N 400 
TYR   CB   C  N N 401 
TYR   CG   C  Y N 402 
TYR   CD1  C  Y N 403 
TYR   CD2  C  Y N 404 
TYR   CE1  C  Y N 405 
TYR   CE2  C  Y N 406 
TYR   CZ   C  Y N 407 
TYR   OH   O  N N 408 
TYR   OXT  O  N N 409 
TYR   H    H  N N 410 
TYR   H2   H  N N 411 
TYR   HA   H  N N 412 
TYR   HB2  H  N N 413 
TYR   HB3  H  N N 414 
TYR   HD1  H  N N 415 
TYR   HD2  H  N N 416 
TYR   HE1  H  N N 417 
TYR   HE2  H  N N 418 
TYR   HH   H  N N 419 
TYR   HXT  H  N N 420 
VAL   N    N  N N 421 
VAL   CA   C  N S 422 
VAL   C    C  N N 423 
VAL   O    O  N N 424 
VAL   CB   C  N N 425 
VAL   CG1  C  N N 426 
VAL   CG2  C  N N 427 
VAL   OXT  O  N N 428 
VAL   H    H  N N 429 
VAL   H2   H  N N 430 
VAL   HA   H  N N 431 
VAL   HB   H  N N 432 
VAL   HG11 H  N N 433 
VAL   HG12 H  N N 434 
VAL   HG13 H  N N 435 
VAL   HG21 H  N N 436 
VAL   HG22 H  N N 437 
VAL   HG23 H  N N 438 
VAL   HXT  H  N N 439 
# 
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 
A1B9G N3  C15  sing Y N 1   
A1B9G N3  N4   sing Y N 2   
A1B9G C14 C15  doub Y N 3   
A1B9G C14 C13  sing Y N 4   
A1B9G CL1 C13  sing N N 5   
A1B9G C15 C17  sing Y N 6   
A1B9G C13 C12  doub Y N 7   
A1B9G N4  C16  doub Y N 8   
A1B9G C17 C16  sing Y N 9   
A1B9G C17 C11  doub Y N 10  
A1B9G C12 C11  sing Y N 11  
A1B9G C11 C1   sing N N 12  
A1B9G C1  O1   doub N N 13  
A1B9G C1  N1   sing N N 14  
A1B9G N1  C2   sing N N 15  
A1B9G C2  C3   doub Y N 16  
A1B9G C2  C7   sing Y N 17  
A1B9G C3  C4   sing Y N 18  
A1B9G C7  C6   doub Y N 19  
A1B9G C4  C5   doub Y N 20  
A1B9G C6  C5   sing Y N 21  
A1B9G C6  C8   sing N N 22  
A1B9G C5  O2   sing N N 23  
A1B9G C8  N2   sing N N 24  
A1B9G N2  C9   sing N N 25  
A1B9G O2  C10  sing N N 26  
A1B9G C10 C9   sing N N 27  
A1B9G N1  H1   sing N N 28  
A1B9G N3  H2   sing N N 29  
A1B9G C4  H3   sing N N 30  
A1B9G C7  H4   sing N N 31  
A1B9G C8  H5   sing N N 32  
A1B9G C8  H6   sing N N 33  
A1B9G C10 H7   sing N N 34  
A1B9G C10 H8   sing N N 35  
A1B9G C3  H9   sing N N 36  
A1B9G N2  H10  sing N N 37  
A1B9G C9  H12  sing N N 38  
A1B9G C9  H13  sing N N 39  
A1B9G C12 H14  sing N N 40  
A1B9G C14 H15  sing N N 41  
A1B9G C16 H16  sing N N 42  
ALA   N   CA   sing N N 43  
ALA   N   H    sing N N 44  
ALA   N   H2   sing N N 45  
ALA   CA  C    sing N N 46  
ALA   CA  CB   sing N N 47  
ALA   CA  HA   sing N N 48  
ALA   C   O    doub N N 49  
ALA   C   OXT  sing N N 50  
ALA   CB  HB1  sing N N 51  
ALA   CB  HB2  sing N N 52  
ALA   CB  HB3  sing N N 53  
ALA   OXT HXT  sing N N 54  
ARG   N   CA   sing N N 55  
ARG   N   H    sing N N 56  
ARG   N   H2   sing N N 57  
ARG   CA  C    sing N N 58  
ARG   CA  CB   sing N N 59  
ARG   CA  HA   sing N N 60  
ARG   C   O    doub N N 61  
ARG   C   OXT  sing N N 62  
ARG   CB  CG   sing N N 63  
ARG   CB  HB2  sing N N 64  
ARG   CB  HB3  sing N N 65  
ARG   CG  CD   sing N N 66  
ARG   CG  HG2  sing N N 67  
ARG   CG  HG3  sing N N 68  
ARG   CD  NE   sing N N 69  
ARG   CD  HD2  sing N N 70  
ARG   CD  HD3  sing N N 71  
ARG   NE  CZ   sing N N 72  
ARG   NE  HE   sing N N 73  
ARG   CZ  NH1  sing N N 74  
ARG   CZ  NH2  doub N N 75  
ARG   NH1 HH11 sing N N 76  
ARG   NH1 HH12 sing N N 77  
ARG   NH2 HH21 sing N N 78  
ARG   NH2 HH22 sing N N 79  
ARG   OXT HXT  sing N N 80  
ASN   N   CA   sing N N 81  
ASN   N   H    sing N N 82  
ASN   N   H2   sing N N 83  
ASN   CA  C    sing N N 84  
ASN   CA  CB   sing N N 85  
ASN   CA  HA   sing N N 86  
ASN   C   O    doub N N 87  
ASN   C   OXT  sing N N 88  
ASN   CB  CG   sing N N 89  
ASN   CB  HB2  sing N N 90  
ASN   CB  HB3  sing N N 91  
ASN   CG  OD1  doub N N 92  
ASN   CG  ND2  sing N N 93  
ASN   ND2 HD21 sing N N 94  
ASN   ND2 HD22 sing N N 95  
ASN   OXT HXT  sing N N 96  
ASP   N   CA   sing N N 97  
ASP   N   H    sing N N 98  
ASP   N   H2   sing N N 99  
ASP   CA  C    sing N N 100 
ASP   CA  CB   sing N N 101 
ASP   CA  HA   sing N N 102 
ASP   C   O    doub N N 103 
ASP   C   OXT  sing N N 104 
ASP   CB  CG   sing N N 105 
ASP   CB  HB2  sing N N 106 
ASP   CB  HB3  sing N N 107 
ASP   CG  OD1  doub N N 108 
ASP   CG  OD2  sing N N 109 
ASP   OD2 HD2  sing N N 110 
ASP   OXT HXT  sing N N 111 
CYS   N   CA   sing N N 112 
CYS   N   H    sing N N 113 
CYS   N   H2   sing N N 114 
CYS   CA  C    sing N N 115 
CYS   CA  CB   sing N N 116 
CYS   CA  HA   sing N N 117 
CYS   C   O    doub N N 118 
CYS   C   OXT  sing N N 119 
CYS   CB  SG   sing N N 120 
CYS   CB  HB2  sing N N 121 
CYS   CB  HB3  sing N N 122 
CYS   SG  HG   sing N N 123 
CYS   OXT HXT  sing N N 124 
DMS   S   O    doub N N 125 
DMS   S   C1   sing N N 126 
DMS   S   C2   sing N N 127 
DMS   C1  H11  sing N N 128 
DMS   C1  H12  sing N N 129 
DMS   C1  H13  sing N N 130 
DMS   C2  H21  sing N N 131 
DMS   C2  H22  sing N N 132 
DMS   C2  H23  sing N N 133 
GLN   N   CA   sing N N 134 
GLN   N   H    sing N N 135 
GLN   N   H2   sing N N 136 
GLN   CA  C    sing N N 137 
GLN   CA  CB   sing N N 138 
GLN   CA  HA   sing N N 139 
GLN   C   O    doub N N 140 
GLN   C   OXT  sing N N 141 
GLN   CB  CG   sing N N 142 
GLN   CB  HB2  sing N N 143 
GLN   CB  HB3  sing N N 144 
GLN   CG  CD   sing N N 145 
GLN   CG  HG2  sing N N 146 
GLN   CG  HG3  sing N N 147 
GLN   CD  OE1  doub N N 148 
GLN   CD  NE2  sing N N 149 
GLN   NE2 HE21 sing N N 150 
GLN   NE2 HE22 sing N N 151 
GLN   OXT HXT  sing N N 152 
GLU   N   CA   sing N N 153 
GLU   N   H    sing N N 154 
GLU   N   H2   sing N N 155 
GLU   CA  C    sing N N 156 
GLU   CA  CB   sing N N 157 
GLU   CA  HA   sing N N 158 
GLU   C   O    doub N N 159 
GLU   C   OXT  sing N N 160 
GLU   CB  CG   sing N N 161 
GLU   CB  HB2  sing N N 162 
GLU   CB  HB3  sing N N 163 
GLU   CG  CD   sing N N 164 
GLU   CG  HG2  sing N N 165 
GLU   CG  HG3  sing N N 166 
GLU   CD  OE1  doub N N 167 
GLU   CD  OE2  sing N N 168 
GLU   OE2 HE2  sing N N 169 
GLU   OXT HXT  sing N N 170 
GLY   N   CA   sing N N 171 
GLY   N   H    sing N N 172 
GLY   N   H2   sing N N 173 
GLY   CA  C    sing N N 174 
GLY   CA  HA2  sing N N 175 
GLY   CA  HA3  sing N N 176 
GLY   C   O    doub N N 177 
GLY   C   OXT  sing N N 178 
GLY   OXT HXT  sing N N 179 
HIS   N   CA   sing N N 180 
HIS   N   H    sing N N 181 
HIS   N   H2   sing N N 182 
HIS   CA  C    sing N N 183 
HIS   CA  CB   sing N N 184 
HIS   CA  HA   sing N N 185 
HIS   C   O    doub N N 186 
HIS   C   OXT  sing N N 187 
HIS   CB  CG   sing N N 188 
HIS   CB  HB2  sing N N 189 
HIS   CB  HB3  sing N N 190 
HIS   CG  ND1  sing Y N 191 
HIS   CG  CD2  doub Y N 192 
HIS   ND1 CE1  doub Y N 193 
HIS   ND1 HD1  sing N N 194 
HIS   CD2 NE2  sing Y N 195 
HIS   CD2 HD2  sing N N 196 
HIS   CE1 NE2  sing Y N 197 
HIS   CE1 HE1  sing N N 198 
HIS   NE2 HE2  sing N N 199 
HIS   OXT HXT  sing N N 200 
HOH   O   H1   sing N N 201 
HOH   O   H2   sing N N 202 
ILE   N   CA   sing N N 203 
ILE   N   H    sing N N 204 
ILE   N   H2   sing N N 205 
ILE   CA  C    sing N N 206 
ILE   CA  CB   sing N N 207 
ILE   CA  HA   sing N N 208 
ILE   C   O    doub N N 209 
ILE   C   OXT  sing N N 210 
ILE   CB  CG1  sing N N 211 
ILE   CB  CG2  sing N N 212 
ILE   CB  HB   sing N N 213 
ILE   CG1 CD1  sing N N 214 
ILE   CG1 HG12 sing N N 215 
ILE   CG1 HG13 sing N N 216 
ILE   CG2 HG21 sing N N 217 
ILE   CG2 HG22 sing N N 218 
ILE   CG2 HG23 sing N N 219 
ILE   CD1 HD11 sing N N 220 
ILE   CD1 HD12 sing N N 221 
ILE   CD1 HD13 sing N N 222 
ILE   OXT HXT  sing N N 223 
LEU   N   CA   sing N N 224 
LEU   N   H    sing N N 225 
LEU   N   H2   sing N N 226 
LEU   CA  C    sing N N 227 
LEU   CA  CB   sing N N 228 
LEU   CA  HA   sing N N 229 
LEU   C   O    doub N N 230 
LEU   C   OXT  sing N N 231 
LEU   CB  CG   sing N N 232 
LEU   CB  HB2  sing N N 233 
LEU   CB  HB3  sing N N 234 
LEU   CG  CD1  sing N N 235 
LEU   CG  CD2  sing N N 236 
LEU   CG  HG   sing N N 237 
LEU   CD1 HD11 sing N N 238 
LEU   CD1 HD12 sing N N 239 
LEU   CD1 HD13 sing N N 240 
LEU   CD2 HD21 sing N N 241 
LEU   CD2 HD22 sing N N 242 
LEU   CD2 HD23 sing N N 243 
LEU   OXT HXT  sing N N 244 
LYS   N   CA   sing N N 245 
LYS   N   H    sing N N 246 
LYS   N   H2   sing N N 247 
LYS   CA  C    sing N N 248 
LYS   CA  CB   sing N N 249 
LYS   CA  HA   sing N N 250 
LYS   C   O    doub N N 251 
LYS   C   OXT  sing N N 252 
LYS   CB  CG   sing N N 253 
LYS   CB  HB2  sing N N 254 
LYS   CB  HB3  sing N N 255 
LYS   CG  CD   sing N N 256 
LYS   CG  HG2  sing N N 257 
LYS   CG  HG3  sing N N 258 
LYS   CD  CE   sing N N 259 
LYS   CD  HD2  sing N N 260 
LYS   CD  HD3  sing N N 261 
LYS   CE  NZ   sing N N 262 
LYS   CE  HE2  sing N N 263 
LYS   CE  HE3  sing N N 264 
LYS   NZ  HZ1  sing N N 265 
LYS   NZ  HZ2  sing N N 266 
LYS   NZ  HZ3  sing N N 267 
LYS   OXT HXT  sing N N 268 
MET   N   CA   sing N N 269 
MET   N   H    sing N N 270 
MET   N   H2   sing N N 271 
MET   CA  C    sing N N 272 
MET   CA  CB   sing N N 273 
MET   CA  HA   sing N N 274 
MET   C   O    doub N N 275 
MET   C   OXT  sing N N 276 
MET   CB  CG   sing N N 277 
MET   CB  HB2  sing N N 278 
MET   CB  HB3  sing N N 279 
MET   CG  SD   sing N N 280 
MET   CG  HG2  sing N N 281 
MET   CG  HG3  sing N N 282 
MET   SD  CE   sing N N 283 
MET   CE  HE1  sing N N 284 
MET   CE  HE2  sing N N 285 
MET   CE  HE3  sing N N 286 
MET   OXT HXT  sing N N 287 
PHE   N   CA   sing N N 288 
PHE   N   H    sing N N 289 
PHE   N   H2   sing N N 290 
PHE   CA  C    sing N N 291 
PHE   CA  CB   sing N N 292 
PHE   CA  HA   sing N N 293 
PHE   C   O    doub N N 294 
PHE   C   OXT  sing N N 295 
PHE   CB  CG   sing N N 296 
PHE   CB  HB2  sing N N 297 
PHE   CB  HB3  sing N N 298 
PHE   CG  CD1  doub Y N 299 
PHE   CG  CD2  sing Y N 300 
PHE   CD1 CE1  sing Y N 301 
PHE   CD1 HD1  sing N N 302 
PHE   CD2 CE2  doub Y N 303 
PHE   CD2 HD2  sing N N 304 
PHE   CE1 CZ   doub Y N 305 
PHE   CE1 HE1  sing N N 306 
PHE   CE2 CZ   sing Y N 307 
PHE   CE2 HE2  sing N N 308 
PHE   CZ  HZ   sing N N 309 
PHE   OXT HXT  sing N N 310 
PRO   N   CA   sing N N 311 
PRO   N   CD   sing N N 312 
PRO   N   H    sing N N 313 
PRO   CA  C    sing N N 314 
PRO   CA  CB   sing N N 315 
PRO   CA  HA   sing N N 316 
PRO   C   O    doub N N 317 
PRO   C   OXT  sing N N 318 
PRO   CB  CG   sing N N 319 
PRO   CB  HB2  sing N N 320 
PRO   CB  HB3  sing N N 321 
PRO   CG  CD   sing N N 322 
PRO   CG  HG2  sing N N 323 
PRO   CG  HG3  sing N N 324 
PRO   CD  HD2  sing N N 325 
PRO   CD  HD3  sing N N 326 
PRO   OXT HXT  sing N N 327 
SER   N   CA   sing N N 328 
SER   N   H    sing N N 329 
SER   N   H2   sing N N 330 
SER   CA  C    sing N N 331 
SER   CA  CB   sing N N 332 
SER   CA  HA   sing N N 333 
SER   C   O    doub N N 334 
SER   C   OXT  sing N N 335 
SER   CB  OG   sing N N 336 
SER   CB  HB2  sing N N 337 
SER   CB  HB3  sing N N 338 
SER   OG  HG   sing N N 339 
SER   OXT HXT  sing N N 340 
THR   N   CA   sing N N 341 
THR   N   H    sing N N 342 
THR   N   H2   sing N N 343 
THR   CA  C    sing N N 344 
THR   CA  CB   sing N N 345 
THR   CA  HA   sing N N 346 
THR   C   O    doub N N 347 
THR   C   OXT  sing N N 348 
THR   CB  OG1  sing N N 349 
THR   CB  CG2  sing N N 350 
THR   CB  HB   sing N N 351 
THR   OG1 HG1  sing N N 352 
THR   CG2 HG21 sing N N 353 
THR   CG2 HG22 sing N N 354 
THR   CG2 HG23 sing N N 355 
THR   OXT HXT  sing N N 356 
TRP   N   CA   sing N N 357 
TRP   N   H    sing N N 358 
TRP   N   H2   sing N N 359 
TRP   CA  C    sing N N 360 
TRP   CA  CB   sing N N 361 
TRP   CA  HA   sing N N 362 
TRP   C   O    doub N N 363 
TRP   C   OXT  sing N N 364 
TRP   CB  CG   sing N N 365 
TRP   CB  HB2  sing N N 366 
TRP   CB  HB3  sing N N 367 
TRP   CG  CD1  doub Y N 368 
TRP   CG  CD2  sing Y N 369 
TRP   CD1 NE1  sing Y N 370 
TRP   CD1 HD1  sing N N 371 
TRP   CD2 CE2  doub Y N 372 
TRP   CD2 CE3  sing Y N 373 
TRP   NE1 CE2  sing Y N 374 
TRP   NE1 HE1  sing N N 375 
TRP   CE2 CZ2  sing Y N 376 
TRP   CE3 CZ3  doub Y N 377 
TRP   CE3 HE3  sing N N 378 
TRP   CZ2 CH2  doub Y N 379 
TRP   CZ2 HZ2  sing N N 380 
TRP   CZ3 CH2  sing Y N 381 
TRP   CZ3 HZ3  sing N N 382 
TRP   CH2 HH2  sing N N 383 
TRP   OXT HXT  sing N N 384 
TYR   N   CA   sing N N 385 
TYR   N   H    sing N N 386 
TYR   N   H2   sing N N 387 
TYR   CA  C    sing N N 388 
TYR   CA  CB   sing N N 389 
TYR   CA  HA   sing N N 390 
TYR   C   O    doub N N 391 
TYR   C   OXT  sing N N 392 
TYR   CB  CG   sing N N 393 
TYR   CB  HB2  sing N N 394 
TYR   CB  HB3  sing N N 395 
TYR   CG  CD1  doub Y N 396 
TYR   CG  CD2  sing Y N 397 
TYR   CD1 CE1  sing Y N 398 
TYR   CD1 HD1  sing N N 399 
TYR   CD2 CE2  doub Y N 400 
TYR   CD2 HD2  sing N N 401 
TYR   CE1 CZ   doub Y N 402 
TYR   CE1 HE1  sing N N 403 
TYR   CE2 CZ   sing Y N 404 
TYR   CE2 HE2  sing N N 405 
TYR   CZ  OH   sing N N 406 
TYR   OH  HH   sing N N 407 
TYR   OXT HXT  sing N N 408 
VAL   N   CA   sing N N 409 
VAL   N   H    sing N N 410 
VAL   N   H2   sing N N 411 
VAL   CA  C    sing N N 412 
VAL   CA  CB   sing N N 413 
VAL   CA  HA   sing N N 414 
VAL   C   O    doub N N 415 
VAL   C   OXT  sing N N 416 
VAL   CB  CG1  sing N N 417 
VAL   CB  CG2  sing N N 418 
VAL   CB  HB   sing N N 419 
VAL   CG1 HG11 sing N N 420 
VAL   CG1 HG12 sing N N 421 
VAL   CG1 HG13 sing N N 422 
VAL   CG2 HG21 sing N N 423 
VAL   CG2 HG22 sing N N 424 
VAL   CG2 HG23 sing N N 425 
VAL   OXT HXT  sing N N 426 
# 
_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                    7I9V 
_atom_sites.fract_transf_matrix[1][1]   0.023485 
_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]   0.023485 
_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]   0.004621 
_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   ? -20.878 19.280  -7.860  1.00 65.68  ? 50  ASP   A N   1 
ATOM   2    C  CA  . ASP   A 1 7   ? -22.003 18.356  -7.718  1.00 65.84  ? 50  ASP   A CA  1 
ATOM   3    C  C   . ASP   A 1 7   ? -22.206 17.588  -9.011  1.00 64.09  ? 50  ASP   A C   1 
ATOM   4    O  O   . ASP   A 1 7   ? -22.374 18.197  -10.069 1.00 64.46  ? 50  ASP   A O   1 
ATOM   5    C  CB  . ASP   A 1 7   ? -23.292 19.104  -7.325  1.00 69.34  ? 50  ASP   A CB  1 
ATOM   6    C  CG  . ASP   A 1 7   ? -24.322 18.213  -6.652  1.00 76.56  ? 50  ASP   A CG  1 
ATOM   7    O  OD1 . ASP   A 1 7   ? -24.655 18.473  -5.461  1.00 77.40  ? 50  ASP   A OD1 1 
ATOM   8    O  OD2 . ASP   A 1 7   ? -24.789 17.242  -7.305  1.00 79.82  ? 50  ASP   A OD2 1 
ATOM   9    N  N   . MET   A 1 8   ? -22.219 16.254  -8.920  1.00 62.11  ? 51  MET   A N   1 
ATOM   10   C  CA  . MET   A 1 8   ? -22.340 15.377  -10.081 1.00 60.79  ? 51  MET   A CA  1 
ATOM   11   C  C   . MET   A 1 8   ? -23.770 15.124  -10.557 1.00 59.40  ? 51  MET   A C   1 
ATOM   12   O  O   . MET   A 1 8   ? -24.704 15.113  -9.756  1.00 59.59  ? 51  MET   A O   1 
ATOM   13   C  CB  . MET   A 1 8   ? -21.616 14.049  -9.841  1.00 60.90  ? 51  MET   A CB  1 
ATOM   14   C  CG  . MET   A 1 8   ? -20.153 14.225  -9.591  1.00 61.65  ? 51  MET   A CG  1 
ATOM   15   S  SD  . MET   A 1 8   ? -19.335 12.664  -9.259  1.00 62.65  ? 51  MET   A SD  1 
ATOM   16   C  CE  . MET   A 1 8   ? -17.697 13.266  -8.862  1.00 60.08  ? 51  MET   A CE  1 
ATOM   17   N  N   . TYR   A 1 9   ? -23.924 14.930  -11.884 1.00 57.74  ? 52  TYR   A N   1 
ATOM   18   C  CA  . TYR   A 1 9   ? -25.208 14.705  -12.546 1.00 56.57  ? 52  TYR   A CA  1 
ATOM   19   C  C   . TYR   A 1 9   ? -25.103 13.743  -13.734 1.00 55.93  ? 52  TYR   A C   1 
ATOM   20   O  O   . TYR   A 1 9   ? -24.024 13.562  -14.285 1.00 55.34  ? 52  TYR   A O   1 
ATOM   21   C  CB  . TYR   A 1 9   ? -25.840 16.030  -12.983 1.00 56.02  ? 52  TYR   A CB  1 
ATOM   22   C  CG  . TYR   A 1 9   ? -25.068 16.786  -14.042 1.00 56.80  ? 52  TYR   A CG  1 
ATOM   23   C  CD1 . TYR   A 1 9   ? -24.105 17.722  -13.693 1.00 57.95  ? 52  TYR   A CD1 1 
ATOM   24   C  CD2 . TYR   A 1 9   ? -25.387 16.656  -15.391 1.00 57.46  ? 52  TYR   A CD2 1 
ATOM   25   C  CE1 . TYR   A 1 9   ? -23.436 18.465  -14.659 1.00 58.85  ? 52  TYR   A CE1 1 
ATOM   26   C  CE2 . TYR   A 1 9   ? -24.734 17.402  -16.364 1.00 58.17  ? 52  TYR   A CE2 1 
ATOM   27   C  CZ  . TYR   A 1 9   ? -23.761 18.310  -15.993 1.00 59.54  ? 52  TYR   A CZ  1 
ATOM   28   O  OH  . TYR   A 1 9   ? -23.087 19.029  -16.952 1.00 61.30  ? 52  TYR   A OH  1 
ATOM   29   N  N   . ILE   A 1 10  ? -26.231 13.133  -14.137 1.00 55.62  ? 53  ILE   A N   1 
ATOM   30   C  CA  . ILE   A 1 10  ? -26.229 12.192  -15.251 1.00 55.50  ? 53  ILE   A CA  1 
ATOM   31   C  C   . ILE   A 1 10  ? -27.104 12.653  -16.453 1.00 56.11  ? 53  ILE   A C   1 
ATOM   32   O  O   . ILE   A 1 10  ? -28.187 13.239  -16.287 1.00 55.99  ? 53  ILE   A O   1 
ATOM   33   C  CB  . ILE   A 1 10  ? -26.574 10.741  -14.793 1.00 55.46  ? 53  ILE   A CB  1 
ATOM   34   C  CG1 . ILE   A 1 10  ? -28.029 10.599  -14.321 1.00 56.00  ? 53  ILE   A CG1 1 
ATOM   35   C  CG2 . ILE   A 1 10  ? -25.602 10.241  -13.725 1.00 55.74  ? 53  ILE   A CG2 1 
ATOM   36   C  CD1 . ILE   A 1 10  ? -28.482 9.163   -14.166 1.00 56.80  ? 53  ILE   A CD1 1 
ATOM   37   N  N   . GLU   A 1 11  ? -26.589 12.385  -17.672 1.00 56.40  ? 54  GLU   A N   1 
ATOM   38   C  CA  . GLU   A 1 11  ? -27.222 12.660  -18.968 1.00 56.97  ? 54  GLU   A CA  1 
ATOM   39   C  C   . GLU   A 1 11  ? -27.223 11.327  -19.758 1.00 57.11  ? 54  GLU   A C   1 
ATOM   40   O  O   . GLU   A 1 11  ? -26.199 10.641  -19.783 1.00 56.93  ? 54  GLU   A O   1 
ATOM   41   C  CB  . GLU   A 1 11  ? -26.396 13.681  -19.772 1.00 59.32  ? 54  GLU   A CB  1 
ATOM   42   C  CG  . GLU   A 1 11  ? -26.260 15.073  -19.176 1.00 64.65  ? 54  GLU   A CG  1 
ATOM   43   C  CD  . GLU   A 1 11  ? -25.384 16.016  -19.989 1.00 72.32  ? 54  GLU   A CD  1 
ATOM   44   O  OE1 . GLU   A 1 11  ? -24.644 15.531  -20.878 1.00 74.09  ? 54  GLU   A OE1 1 
ATOM   45   O  OE2 . GLU   A 1 11  ? -25.427 17.241  -19.732 1.00 74.82  ? 54  GLU   A OE2 1 
ATOM   46   N  N   . ARG   A 1 12  ? -28.350 10.966  -20.405 1.00 56.72  ? 55  ARG   A N   1 
ATOM   47   C  CA  . ARG   A 1 12  ? -28.405 9.725   -21.167 1.00 56.66  ? 55  ARG   A CA  1 
ATOM   48   C  C   . ARG   A 1 12  ? -27.454 9.779   -22.351 1.00 57.42  ? 55  ARG   A C   1 
ATOM   49   O  O   . ARG   A 1 12  ? -27.280 10.837  -22.945 1.00 58.19  ? 55  ARG   A O   1 
ATOM   50   C  CB  . ARG   A 1 12  ? -29.835 9.408   -21.614 1.00 57.06  ? 55  ARG   A CB  1 
ATOM   51   C  CG  . ARG   A 1 12  ? -30.046 7.923   -21.863 1.00 58.39  ? 55  ARG   A CG  1 
ATOM   52   C  CD  . ARG   A 1 12  ? -31.504 7.552   -22.014 1.00 59.77  ? 55  ARG   A CD  1 
ATOM   53   N  NE  . ARG   A 1 12  ? -31.671 6.112   -22.226 1.00 61.32  ? 55  ARG   A NE  1 
ATOM   54   C  CZ  . ARG   A 1 12  ? -31.655 5.528   -23.420 1.00 62.96  ? 55  ARG   A CZ  1 
ATOM   55   N  NH1 . ARG   A 1 12  ? -31.468 6.249   -24.518 1.00 63.16  ? 55  ARG   A NH1 1 
ATOM   56   N  NH2 . ARG   A 1 12  ? -31.804 4.214   -23.524 1.00 61.82  ? 55  ARG   A NH2 1 
ATOM   57   N  N   . ALA   A 1 13  ? -26.784 8.661   -22.650 1.00 57.32  ? 56  ALA   A N   1 
ATOM   58   C  CA  . ALA   A 1 13  ? -25.847 8.540   -23.774 1.00 57.63  ? 56  ALA   A CA  1 
ATOM   59   C  C   . ALA   A 1 13  ? -26.286 7.505   -24.823 1.00 58.22  ? 56  ALA   A C   1 
ATOM   60   O  O   . ALA   A 1 13  ? -25.698 7.461   -25.900 1.00 58.40  ? 56  ALA   A O   1 
ATOM   61   C  CB  . ALA   A 1 13  ? -24.444 8.213   -23.278 1.00 57.40  ? 56  ALA   A CB  1 
ATOM   62   N  N   . GLY   A 1 14  ? -27.298 6.691   -24.517 1.00 58.59  ? 57  GLY   A N   1 
ATOM   63   C  CA  . GLY   A 1 14  ? -27.802 5.718   -25.474 1.00 59.76  ? 57  GLY   A CA  1 
ATOM   64   C  C   . GLY   A 1 14  ? -28.340 4.416   -24.923 1.00 60.79  ? 57  GLY   A C   1 
ATOM   65   O  O   . GLY   A 1 14  ? -28.442 4.237   -23.713 1.00 60.96  ? 57  GLY   A O   1 
ATOM   66   N  N   . ASP   A 1 15  ? -28.718 3.504   -25.836 1.00 61.51  ? 58  ASP   A N   1 
ATOM   67   C  CA  . ASP   A 1 15  ? -29.222 2.166   -25.527 1.00 62.31  ? 58  ASP   A CA  1 
ATOM   68   C  C   . ASP   A 1 15  ? -28.075 1.204   -25.341 1.00 63.30  ? 58  ASP   A C   1 
ATOM   69   O  O   . ASP   A 1 15  ? -26.976 1.439   -25.845 1.00 63.41  ? 58  ASP   A O   1 
ATOM   70   C  CB  . ASP   A 1 15  ? -30.098 1.636   -26.675 1.00 63.46  ? 58  ASP   A CB  1 
ATOM   71   C  CG  . ASP   A 1 15  ? -31.435 2.309   -26.814 1.00 68.14  ? 58  ASP   A CG  1 
ATOM   72   O  OD1 . ASP   A 1 15  ? -31.623 3.376   -26.207 1.00 69.18  ? 58  ASP   A OD1 1 
ATOM   73   O  OD2 . ASP   A 1 15  ? -32.287 1.786   -27.561 1.00 70.45  ? 58  ASP   A OD2 1 
ATOM   74   N  N   . ILE   A 1 16  ? -28.339 0.090   -24.664 1.00 63.90  ? 59  ILE   A N   1 
ATOM   75   C  CA  . ILE   A 1 16  ? -27.337 -0.938  -24.486 1.00 65.03  ? 59  ILE   A CA  1 
ATOM   76   C  C   . ILE   A 1 16  ? -27.692 -2.139  -25.351 1.00 66.52  ? 59  ILE   A C   1 
ATOM   77   O  O   . ILE   A 1 16  ? -28.520 -2.976  -24.986 1.00 66.53  ? 59  ILE   A O   1 
ATOM   78   C  CB  . ILE   A 1 16  ? -27.128 -1.220  -23.001 1.00 65.34  ? 59  ILE   A CB  1 
ATOM   79   C  CG1 . ILE   A 1 16  ? -26.297 -0.083  -22.407 1.00 66.23  ? 59  ILE   A CG1 1 
ATOM   80   C  CG2 . ILE   A 1 16  ? -26.484 -2.568  -22.763 1.00 65.72  ? 59  ILE   A CG2 1 
ATOM   81   C  CD1 . ILE   A 1 16  ? -26.387 0.026   -20.942 1.00 67.81  ? 59  ILE   A CD1 1 
ATOM   82   N  N   . THR   A 1 17  ? -27.131 -2.138  -26.569 1.00 67.61  ? 60  THR   A N   1 
ATOM   83   C  CA  . THR   A 1 17  ? -27.345 -3.167  -27.578 1.00 69.26  ? 60  THR   A CA  1 
ATOM   84   C  C   . THR   A 1 17  ? -26.033 -3.583  -28.232 1.00 70.75  ? 60  THR   A C   1 
ATOM   85   O  O   . THR   A 1 17  ? -25.105 -2.784  -28.345 1.00 70.52  ? 60  THR   A O   1 
ATOM   86   C  CB  . THR   A 1 17  ? -28.261 -2.638  -28.701 1.00 70.44  ? 60  THR   A CB  1 
ATOM   87   O  OG1 . THR   A 1 17  ? -27.685 -1.453  -29.254 1.00 71.28  ? 60  THR   A OG1 1 
ATOM   88   C  CG2 . THR   A 1 17  ? -29.682 -2.380  -28.236 1.00 70.90  ? 60  THR   A CG2 1 
ATOM   89   N  N   . TRP   A 1 18  ? -25.987 -4.811  -28.725 1.00 72.26  ? 61  TRP   A N   1 
ATOM   90   C  CA  . TRP   A 1 18  ? -24.838 -5.300  -29.462 1.00 74.44  ? 61  TRP   A CA  1 
ATOM   91   C  C   . TRP   A 1 18  ? -24.992 -4.781  -30.907 1.00 77.28  ? 61  TRP   A C   1 
ATOM   92   O  O   . TRP   A 1 18  ? -26.055 -4.942  -31.508 1.00 77.15  ? 61  TRP   A O   1 
ATOM   93   C  CB  . TRP   A 1 18  ? -24.827 -6.839  -29.431 1.00 74.17  ? 61  TRP   A CB  1 
ATOM   94   C  CG  . TRP   A 1 18  ? -23.747 -7.483  -30.251 1.00 74.51  ? 61  TRP   A CG  1 
ATOM   95   C  CD1 . TRP   A 1 18  ? -23.809 -7.817  -31.572 1.00 75.15  ? 61  TRP   A CD1 1 
ATOM   96   C  CD2 . TRP   A 1 18  ? -22.488 -7.977  -29.772 1.00 74.54  ? 61  TRP   A CD2 1 
ATOM   97   N  NE1 . TRP   A 1 18  ? -22.642 -8.428  -31.960 1.00 75.36  ? 61  TRP   A NE1 1 
ATOM   98   C  CE2 . TRP   A 1 18  ? -21.817 -8.547  -30.872 1.00 75.20  ? 61  TRP   A CE2 1 
ATOM   99   C  CE3 . TRP   A 1 18  ? -21.843 -7.955  -28.531 1.00 74.71  ? 61  TRP   A CE3 1 
ATOM   100  C  CZ2 . TRP   A 1 18  ? -20.548 -9.113  -30.756 1.00 75.58  ? 61  TRP   A CZ2 1 
ATOM   101  C  CZ3 . TRP   A 1 18  ? -20.596 -8.530  -28.418 1.00 75.26  ? 61  TRP   A CZ3 1 
ATOM   102  C  CH2 . TRP   A 1 18  ? -19.949 -9.071  -29.525 1.00 75.44  ? 61  TRP   A CH2 1 
ATOM   103  N  N   . GLU   A 1 19  ? -23.957 -4.131  -31.446 1.00 79.44  ? 62  GLU   A N   1 
ATOM   104  C  CA  . GLU   A 1 19  ? -23.989 -3.645  -32.818 1.00 82.10  ? 62  GLU   A CA  1 
ATOM   105  C  C   . GLU   A 1 19  ? -23.202 -4.619  -33.685 1.00 83.99  ? 62  GLU   A C   1 
ATOM   106  O  O   . GLU   A 1 19  ? -21.996 -4.753  -33.487 1.00 84.03  ? 62  GLU   A O   1 
ATOM   107  C  CB  . GLU   A 1 19  ? -23.368 -2.235  -32.934 1.00 85.42  ? 62  GLU   A CB  1 
ATOM   108  C  CG  . GLU   A 1 19  ? -23.289 -1.731  -34.376 1.00 92.17  ? 62  GLU   A CG  1 
ATOM   109  C  CD  . GLU   A 1 19  ? -22.135 -0.801  -34.717 1.00 100.11 ? 62  GLU   A CD  1 
ATOM   110  O  OE1 . GLU   A 1 19  ? -21.431 -0.353  -33.781 1.00 102.43 ? 62  GLU   A OE1 1 
ATOM   111  O  OE2 . GLU   A 1 19  ? -21.937 -0.515  -35.921 1.00 102.26 ? 62  GLU   A OE2 1 
ATOM   112  N  N   . LYS   A 1 20  ? -23.866 -5.306  -34.623 1.00 85.49  ? 63  LYS   A N   1 
ATOM   113  C  CA  . LYS   A 1 20  ? -23.146 -6.212  -35.527 1.00 87.63  ? 63  LYS   A CA  1 
ATOM   114  C  C   . LYS   A 1 20  ? -22.398 -5.329  -36.537 1.00 89.23  ? 63  LYS   A C   1 
ATOM   115  O  O   . LYS   A 1 20  ? -22.857 -4.223  -36.839 1.00 89.77  ? 63  LYS   A O   1 
ATOM   116  C  CB  . LYS   A 1 20  ? -24.094 -7.168  -36.274 1.00 90.37  ? 63  LYS   A CB  1 
ATOM   117  C  CG  . LYS   A 1 20  ? -25.383 -7.553  -35.540 1.00 95.62  ? 63  LYS   A CG  1 
ATOM   118  C  CD  . LYS   A 1 20  ? -26.395 -8.168  -36.535 1.00 100.51 ? 63  LYS   A CD  1 
ATOM   119  C  CE  . LYS   A 1 20  ? -27.798 -8.307  -35.981 1.00 104.15 ? 63  LYS   A CE  1 
ATOM   120  N  NZ  . LYS   A 1 20  ? -28.729 -8.893  -36.986 1.00 106.10 ? 63  LYS   A NZ  1 
ATOM   121  N  N   . ASP   A 1 21  ? -21.258 -5.797  -37.050 1.00 89.88  ? 64  ASP   A N   1 
ATOM   122  C  CA  . ASP   A 1 21  ? -20.439 -5.020  -37.993 1.00 91.11  ? 64  ASP   A CA  1 
ATOM   123  C  C   . ASP   A 1 21  ? -19.813 -3.792  -37.304 1.00 91.03  ? 64  ASP   A C   1 
ATOM   124  O  O   . ASP   A 1 21  ? -19.705 -2.721  -37.910 1.00 91.61  ? 64  ASP   A O   1 
ATOM   125  C  CB  . ASP   A 1 21  ? -21.219 -4.585  -39.257 1.00 94.17  ? 64  ASP   A CB  1 
ATOM   126  C  CG  . ASP   A 1 21  ? -21.704 -5.700  -40.166 1.00 101.24 ? 64  ASP   A CG  1 
ATOM   127  O  OD1 . ASP   A 1 21  ? -20.946 -6.684  -40.362 1.00 103.10 ? 64  ASP   A OD1 1 
ATOM   128  O  OD2 . ASP   A 1 21  ? -22.828 -5.575  -40.710 1.00 103.37 ? 64  ASP   A OD2 1 
ATOM   129  N  N   . ALA   A 1 22  ? -19.420 -3.942  -36.036 1.00 90.05  ? 65  ALA   A N   1 
ATOM   130  C  CA  . ALA   A 1 22  ? -18.768 -2.863  -35.298 1.00 89.51  ? 65  ALA   A CA  1 
ATOM   131  C  C   . ALA   A 1 22  ? -17.233 -2.956  -35.473 1.00 88.86  ? 65  ALA   A C   1 
ATOM   132  O  O   . ALA   A 1 22  ? -16.726 -3.987  -35.917 1.00 88.92  ? 65  ALA   A O   1 
ATOM   133  C  CB  . ALA   A 1 22  ? -19.143 -2.945  -33.825 1.00 89.54  ? 65  ALA   A CB  1 
ATOM   134  N  N   . GLU   A 1 23  ? -16.499 -1.879  -35.153 1.00 88.06  ? 66  GLU   A N   1 
ATOM   135  C  CA  . GLU   A 1 23  ? -15.040 -1.852  -35.258 1.00 87.82  ? 66  GLU   A CA  1 
ATOM   136  C  C   . GLU   A 1 23  ? -14.385 -2.900  -34.318 1.00 86.63  ? 66  GLU   A C   1 
ATOM   137  O  O   . GLU   A 1 23  ? -14.421 -2.731  -33.099 1.00 86.54  ? 66  GLU   A O   1 
ATOM   138  C  CB  . GLU   A 1 23  ? -14.536 -0.436  -34.929 1.00 90.98  ? 66  GLU   A CB  1 
ATOM   139  C  CG  . GLU   A 1 23  ? -13.052 -0.225  -35.166 1.00 97.73  ? 66  GLU   A CG  1 
ATOM   140  C  CD  . GLU   A 1 23  ? -12.460 0.947   -34.406 1.00 106.43 ? 66  GLU   A CD  1 
ATOM   141  O  OE1 . GLU   A 1 23  ? -13.228 1.855   -34.011 1.00 107.86 ? 66  GLU   A OE1 1 
ATOM   142  O  OE2 . GLU   A 1 23  ? -11.223 0.956   -34.204 1.00 109.67 ? 66  GLU   A OE2 1 
ATOM   143  N  N   . VAL   A 1 24  ? -13.805 -3.984  -34.891 1.00 85.35  ? 67  VAL   A N   1 
ATOM   144  C  CA  . VAL   A 1 24  ? -13.149 -5.062  -34.135 1.00 84.30  ? 67  VAL   A CA  1 
ATOM   145  C  C   . VAL   A 1 24  ? -11.649 -4.797  -33.960 1.00 83.39  ? 67  VAL   A C   1 
ATOM   146  O  O   . VAL   A 1 24  ? -10.886 -5.052  -34.877 1.00 83.79  ? 67  VAL   A O   1 
ATOM   147  C  CB  . VAL   A 1 24  ? -13.365 -6.475  -34.752 1.00 84.50  ? 67  VAL   A CB  1 
ATOM   148  C  CG1 . VAL   A 1 24  ? -12.988 -7.557  -33.756 1.00 84.87  ? 67  VAL   A CG1 1 
ATOM   149  C  CG2 . VAL   A 1 24  ? -14.797 -6.676  -35.231 1.00 84.76  ? 67  VAL   A CG2 1 
ATOM   150  N  N   . THR   A 1 25  ? -11.217 -4.332  -32.785 1.00 82.29  ? 68  THR   A N   1 
ATOM   151  C  CA  . THR   A 1 25  ? -9.796  -4.065  -32.533 1.00 81.50  ? 68  THR   A CA  1 
ATOM   152  C  C   . THR   A 1 25  ? -9.391  -4.531  -31.121 1.00 80.67  ? 68  THR   A C   1 
ATOM   153  O  O   . THR   A 1 25  ? -10.253 -4.874  -30.327 1.00 80.66  ? 68  THR   A O   1 
ATOM   154  C  CB  . THR   A 1 25  ? -9.506  -2.572  -32.770 1.00 82.37  ? 68  THR   A CB  1 
ATOM   155  O  OG1 . THR   A 1 25  ? -8.131  -2.312  -32.504 1.00 83.03  ? 68  THR   A OG1 1 
ATOM   156  C  CG2 . THR   A 1 25  ? -10.347 -1.681  -31.893 1.00 82.62  ? 68  THR   A CG2 1 
ATOM   157  N  N   . GLY   A 1 26  ? -8.093  -4.569  -30.827 1.00 79.93  ? 69  GLY   A N   1 
ATOM   158  C  CA  . GLY   A 1 26  ? -7.616  -4.933  -29.500 1.00 79.57  ? 69  GLY   A CA  1 
ATOM   159  C  C   . GLY   A 1 26  ? -7.126  -6.354  -29.341 1.00 79.04  ? 69  GLY   A C   1 
ATOM   160  O  O   . GLY   A 1 26  ? -7.687  -7.285  -29.920 1.00 79.06  ? 69  GLY   A O   1 
ATOM   161  N  N   . ASN   A 1 27  ? -6.093  -6.525  -28.509 1.00 78.39  ? 70  ASN   A N   1 
ATOM   162  C  CA  . ASN   A 1 27  ? -5.484  -7.823  -28.235 1.00 77.99  ? 70  ASN   A CA  1 
ATOM   163  C  C   . ASN   A 1 27  ? -6.023  -8.500  -26.932 1.00 76.71  ? 70  ASN   A C   1 
ATOM   164  O  O   . ASN   A 1 27  ? -6.802  -7.888  -26.203 1.00 76.77  ? 70  ASN   A O   1 
ATOM   165  C  CB  . ASN   A 1 27  ? -3.954  -7.690  -28.240 1.00 79.64  ? 70  ASN   A CB  1 
ATOM   166  C  CG  . ASN   A 1 27  ? -3.412  -6.972  -27.037 1.00 83.96  ? 70  ASN   A CG  1 
ATOM   167  O  OD1 . ASN   A 1 27  ? -3.794  -5.837  -26.740 1.00 85.56  ? 70  ASN   A OD1 1 
ATOM   168  N  ND2 . ASN   A 1 27  ? -2.509  -7.624  -26.313 1.00 84.80  ? 70  ASN   A ND2 1 
ATOM   169  N  N   . SER   A 1 28  ? -5.643  -9.776  -26.672 1.00 75.61  ? 71  SER   A N   1 
ATOM   170  C  CA  . SER   A 1 28  ? -6.084  -10.556 -25.500 1.00 74.87  ? 71  SER   A CA  1 
ATOM   171  C  C   . SER   A 1 28  ? -4.891  -10.983 -24.617 1.00 73.69  ? 71  SER   A C   1 
ATOM   172  O  O   . SER   A 1 28  ? -4.474  -12.142 -24.666 1.00 74.16  ? 71  SER   A O   1 
ATOM   173  C  CB  . SER   A 1 28  ? -6.861  -11.801 -25.939 1.00 76.21  ? 71  SER   A CB  1 
ATOM   174  O  OG  . SER   A 1 28  ? -7.611  -11.653 -27.134 1.00 78.58  ? 71  SER   A OG  1 
ATOM   175  N  N   . PRO   A 1 29  ? -4.325  -10.085 -23.791 1.00 72.42  ? 72  PRO   A N   1 
ATOM   176  C  CA  . PRO   A 1 29  ? -3.161  -10.482 -22.978 1.00 71.80  ? 72  PRO   A CA  1 
ATOM   177  C  C   . PRO   A 1 29  ? -3.483  -11.260 -21.704 1.00 71.21  ? 72  PRO   A C   1 
ATOM   178  O  O   . PRO   A 1 29  ? -4.452  -10.938 -21.014 1.00 71.33  ? 72  PRO   A O   1 
ATOM   179  C  CB  . PRO   A 1 29  ? -2.478  -9.150  -22.668 1.00 72.57  ? 72  PRO   A CB  1 
ATOM   180  C  CG  . PRO   A 1 29  ? -3.588  -8.139  -22.692 1.00 72.97  ? 72  PRO   A CG  1 
ATOM   181  C  CD  . PRO   A 1 29  ? -4.676  -8.662  -23.592 1.00 71.63  ? 72  PRO   A CD  1 
ATOM   182  N  N   . ARG   A 1 30  ? -2.651  -12.264 -21.372 1.00 70.41  ? 73  ARG   A N   1 
ATOM   183  C  CA  . ARG   A 1 30  ? -2.797  -13.027 -20.130 1.00 70.14  ? 73  ARG   A CA  1 
ATOM   184  C  C   . ARG   A 1 30  ? -1.755  -12.481 -19.165 1.00 68.83  ? 73  ARG   A C   1 
ATOM   185  O  O   . ARG   A 1 30  ? -0.568  -12.697 -19.366 1.00 68.91  ? 73  ARG   A O   1 
ATOM   186  C  CB  . ARG   A 1 30  ? -2.598  -14.529 -20.362 1.00 72.38  ? 73  ARG   A CB  1 
ATOM   187  C  CG  . ARG   A 1 30  ? -3.664  -15.142 -21.260 1.00 77.15  ? 73  ARG   A CG  1 
ATOM   188  C  CD  . ARG   A 1 30  ? -3.511  -16.653 -21.366 1.00 81.95  ? 73  ARG   A CD  1 
ATOM   189  N  NE  . ARG   A 1 30  ? -4.218  -17.201 -22.531 1.00 85.73  ? 73  ARG   A NE  1 
ATOM   190  C  CZ  . ARG   A 1 30  ? -5.488  -17.599 -22.519 1.00 87.98  ? 73  ARG   A CZ  1 
ATOM   191  N  NH1 . ARG   A 1 30  ? -6.208  -17.512 -21.408 1.00 88.01  ? 73  ARG   A NH1 1 
ATOM   192  N  NH2 . ARG   A 1 30  ? -6.047  -18.086 -23.619 1.00 87.41  ? 73  ARG   A NH2 1 
ATOM   193  N  N   . LEU   A 1 31  ? -2.190  -11.716 -18.156 1.00 67.70  ? 74  LEU   A N   1 
ATOM   194  C  CA  . LEU   A 1 31  ? -1.277  -11.057 -17.223 1.00 66.80  ? 74  LEU   A CA  1 
ATOM   195  C  C   . LEU   A 1 31  ? -1.429  -11.519 -15.775 1.00 65.87  ? 74  LEU   A C   1 
ATOM   196  O  O   . LEU   A 1 31  ? -2.550  -11.571 -15.267 1.00 66.14  ? 74  LEU   A O   1 
ATOM   197  C  CB  . LEU   A 1 31  ? -1.518  -9.539  -17.274 1.00 66.66  ? 74  LEU   A CB  1 
ATOM   198  C  CG  . LEU   A 1 31  ? -1.485  -8.899  -18.650 1.00 67.77  ? 74  LEU   A CG  1 
ATOM   199  C  CD1 . LEU   A 1 31  ? -2.469  -7.752  -18.750 1.00 68.08  ? 74  LEU   A CD1 1 
ATOM   200  C  CD2 . LEU   A 1 31  ? -0.081  -8.478  -19.018 1.00 68.36  ? 74  LEU   A CD2 1 
ATOM   201  N  N   . ASP   A 1 32  ? -0.302  -11.780 -15.089 1.00 64.58  ? 75  ASP   A N   1 
ATOM   202  C  CA  . ASP   A 1 32  ? -0.333  -12.123 -13.671 1.00 64.19  ? 75  ASP   A CA  1 
ATOM   203  C  C   . ASP   A 1 32  ? -0.548  -10.812 -12.877 1.00 62.39  ? 75  ASP   A C   1 
ATOM   204  O  O   . ASP   A 1 32  ? 0.315   -9.934  -12.917 1.00 62.63  ? 75  ASP   A O   1 
ATOM   205  C  CB  . ASP   A 1 32  ? 0.978   -12.812 -13.240 1.00 67.22  ? 75  ASP   A CB  1 
ATOM   206  C  CG  . ASP   A 1 32  ? 0.947   -14.337 -13.296 1.00 74.66  ? 75  ASP   A CG  1 
ATOM   207  O  OD1 . ASP   A 1 32  ? -0.035  -14.894 -13.849 1.00 76.09  ? 75  ASP   A OD1 1 
ATOM   208  O  OD2 . ASP   A 1 32  ? 1.914   -14.978 -12.786 1.00 77.38  ? 75  ASP   A OD2 1 
ATOM   209  N  N   . VAL   A 1 33  ? -1.718  -10.644 -12.218 1.00 60.33  ? 76  VAL   A N   1 
ATOM   210  C  CA  . VAL   A 1 33  ? -1.998  -9.403  -11.485 1.00 59.15  ? 76  VAL   A CA  1 
ATOM   211  C  C   . VAL   A 1 33  ? -2.355  -9.646  -9.984  1.00 57.73  ? 76  VAL   A C   1 
ATOM   212  O  O   . VAL   A 1 33  ? -2.588  -10.787 -9.569  1.00 57.30  ? 76  VAL   A O   1 
ATOM   213  C  CB  . VAL   A 1 33  ? -3.053  -8.487  -12.191 1.00 59.50  ? 76  VAL   A CB  1 
ATOM   214  C  CG1 . VAL   A 1 33  ? -2.836  -8.425  -13.701 1.00 59.91  ? 76  VAL   A CG1 1 
ATOM   215  C  CG2 . VAL   A 1 33  ? -4.478  -8.912  -11.855 1.00 59.84  ? 76  VAL   A CG2 1 
ATOM   216  N  N   . ALA   A 1 34  ? -2.342  -8.556  -9.174  1.00 56.70  ? 77  ALA   A N   1 
ATOM   217  C  CA  . ALA   A 1 34  ? -2.656  -8.573  -7.747  1.00 56.18  ? 77  ALA   A CA  1 
ATOM   218  C  C   . ALA   A 1 34  ? -3.626  -7.446  -7.403  1.00 55.25  ? 77  ALA   A C   1 
ATOM   219  O  O   . ALA   A 1 34  ? -3.470  -6.333  -7.899  1.00 55.84  ? 77  ALA   A O   1 
ATOM   220  C  CB  . ALA   A 1 34  ? -1.385  -8.427  -6.929  1.00 56.40  ? 77  ALA   A CB  1 
ATOM   221  N  N   . LEU   A 1 35  ? -4.630  -7.727  -6.570  1.00 53.81  ? 78  LEU   A N   1 
ATOM   222  C  CA  . LEU   A 1 35  ? -5.608  -6.717  -6.186  1.00 53.01  ? 78  LEU   A CA  1 
ATOM   223  C  C   . LEU   A 1 35  ? -5.448  -6.366  -4.712  1.00 53.08  ? 78  LEU   A C   1 
ATOM   224  O  O   . LEU   A 1 35  ? -5.539  -7.248  -3.848  1.00 53.48  ? 78  LEU   A O   1 
ATOM   225  C  CB  . LEU   A 1 35  ? -7.036  -7.194  -6.491  1.00 52.30  ? 78  LEU   A CB  1 
ATOM   226  C  CG  . LEU   A 1 35  ? -8.143  -6.203  -6.145  1.00 51.98  ? 78  LEU   A CG  1 
ATOM   227  C  CD1 . LEU   A 1 35  ? -8.033  -4.950  -6.978  1.00 51.72  ? 78  LEU   A CD1 1 
ATOM   228  C  CD2 . LEU   A 1 35  ? -9.500  -6.840  -6.291  1.00 51.89  ? 78  LEU   A CD2 1 
ATOM   229  N  N   . ASP   A 1 36  ? -5.153  -5.092  -4.420  1.00 52.62  ? 79  ASP   A N   1 
ATOM   230  C  CA  . ASP   A 1 36  ? -4.951  -4.675  -3.031  1.00 52.65  ? 79  ASP   A CA  1 
ATOM   231  C  C   . ASP   A 1 36  ? -6.292  -4.281  -2.343  1.00 52.82  ? 79  ASP   A C   1 
ATOM   232  O  O   . ASP   A 1 36  ? -7.332  -4.233  -3.004  1.00 52.62  ? 79  ASP   A O   1 
ATOM   233  C  CB  . ASP   A 1 36  ? -3.861  -3.579  -2.928  1.00 53.22  ? 79  ASP   A CB  1 
ATOM   234  C  CG  . ASP   A 1 36  ? -4.281  -2.196  -3.395  1.00 56.13  ? 79  ASP   A CG  1 
ATOM   235  O  OD1 . ASP   A 1 36  ? -5.465  -2.014  -3.707  1.00 56.63  ? 79  ASP   A OD1 1 
ATOM   236  O  OD2 . ASP   A 1 36  ? -3.421  -1.295  -3.440  1.00 57.87  ? 79  ASP   A OD2 1 
ATOM   237  N  N   . GLU   A 1 37  ? -6.252  -4.003  -1.028  1.00 52.93  ? 80  GLU   A N   1 
ATOM   238  C  CA  . GLU   A 1 37  ? -7.404  -3.614  -0.234  1.00 53.79  ? 80  GLU   A CA  1 
ATOM   239  C  C   . GLU   A 1 37  ? -8.063  -2.337  -0.764  1.00 54.22  ? 80  GLU   A C   1 
ATOM   240  O  O   . GLU   A 1 37  ? -9.265  -2.189  -0.620  1.00 54.56  ? 80  GLU   A O   1 
ATOM   241  C  CB  . GLU   A 1 37  ? -6.969  -3.420  1.226   1.00 57.57  ? 80  GLU   A CB  1 
ATOM   242  C  CG  . GLU   A 1 37  ? -8.116  -3.402  2.224   1.00 64.65  ? 80  GLU   A CG  1 
ATOM   243  C  CD  . GLU   A 1 37  ? -7.712  -3.628  3.667   1.00 72.54  ? 80  GLU   A CD  1 
ATOM   244  O  OE1 . GLU   A 1 37  ? -6.905  -2.830  4.197   1.00 74.55  ? 80  GLU   A OE1 1 
ATOM   245  O  OE2 . GLU   A 1 37  ? -8.203  -4.611  4.268   1.00 75.32  ? 80  GLU   A OE2 1 
ATOM   246  N  N   . SER   A 1 38  ? -7.295  -1.434  -1.408  1.00 53.72  ? 81  SER   A N   1 
ATOM   247  C  CA  . SER   A 1 38  ? -7.786  -0.161  -1.945  1.00 53.27  ? 81  SER   A CA  1 
ATOM   248  C  C   . SER   A 1 38  ? -8.363  -0.229  -3.361  1.00 52.95  ? 81  SER   A C   1 
ATOM   249  O  O   . SER   A 1 38  ? -8.621  0.817   -3.951  1.00 53.19  ? 81  SER   A O   1 
ATOM   250  C  CB  . SER   A 1 38  ? -6.674  0.878   -1.929  1.00 54.62  ? 81  SER   A CB  1 
ATOM   251  O  OG  . SER   A 1 38  ? -6.058  0.942   -0.653  1.00 57.96  ? 81  SER   A OG  1 
ATOM   252  N  N   . GLY   A 1 39  ? -8.533  -1.427  -3.909  1.00 52.34  ? 82  GLY   A N   1 
ATOM   253  C  CA  . GLY   A 1 39  ? -9.076  -1.595  -5.252  1.00 52.35  ? 82  GLY   A CA  1 
ATOM   254  C  C   . GLY   A 1 39  ? -8.112  -1.249  -6.373  1.00 52.48  ? 82  GLY   A C   1 
ATOM   255  O  O   . GLY   A 1 39  ? -8.550  -0.894  -7.467  1.00 52.49  ? 82  GLY   A O   1 
ATOM   256  N  N   . ASP   A 1 40  ? -6.785  -1.347  -6.120  1.00 52.33  ? 83  ASP   A N   1 
ATOM   257  C  CA  . ASP   A 1 40  ? -5.756  -1.057  -7.125  1.00 52.56  ? 83  ASP   A CA  1 
ATOM   258  C  C   . ASP   A 1 40  ? -5.188  -2.356  -7.687  1.00 52.83  ? 83  ASP   A C   1 
ATOM   259  O  O   . ASP   A 1 40  ? -4.690  -3.180  -6.922  1.00 53.04  ? 83  ASP   A O   1 
ATOM   260  C  CB  . ASP   A 1 40  ? -4.565  -0.275  -6.517  1.00 54.20  ? 83  ASP   A CB  1 
ATOM   261  C  CG  . ASP   A 1 40  ? -4.847  1.013   -5.759  1.00 59.05  ? 83  ASP   A CG  1 
ATOM   262  O  OD1 . ASP   A 1 40  ? -5.476  1.920   -6.338  1.00 58.73  ? 83  ASP   A OD1 1 
ATOM   263  O  OD2 . ASP   A 1 40  ? -4.378  1.137   -4.602  1.00 62.59  ? 83  ASP   A OD2 1 
ATOM   264  N  N   . PHE   A 1 41  ? -5.205  -2.526  -9.010  1.00 52.99  ? 84  PHE   A N   1 
ATOM   265  C  CA  . PHE   A 1 41  ? -4.579  -3.692  -9.639  1.00 53.68  ? 84  PHE   A CA  1 
ATOM   266  C  C   . PHE   A 1 41  ? -3.099  -3.390  -9.887  1.00 55.26  ? 84  PHE   A C   1 
ATOM   267  O  O   . PHE   A 1 41  ? -2.720  -2.235  -10.107 1.00 55.34  ? 84  PHE   A O   1 
ATOM   268  C  CB  . PHE   A 1 41  ? -5.247  -4.041  -10.973 1.00 52.97  ? 84  PHE   A CB  1 
ATOM   269  C  CG  . PHE   A 1 41  ? -6.576  -4.735  -10.849 1.00 52.80  ? 84  PHE   A CG  1 
ATOM   270  C  CD1 . PHE   A 1 41  ? -6.653  -6.044  -10.409 1.00 53.12  ? 84  PHE   A CD1 1 
ATOM   271  C  CD2 . PHE   A 1 41  ? -7.751  -4.091  -11.206 1.00 53.02  ? 84  PHE   A CD2 1 
ATOM   272  C  CE1 . PHE   A 1 41  ? -7.884  -6.688  -10.318 1.00 53.67  ? 84  PHE   A CE1 1 
ATOM   273  C  CE2 . PHE   A 1 41  ? -8.978  -4.740  -11.113 1.00 53.06  ? 84  PHE   A CE2 1 
ATOM   274  C  CZ  . PHE   A 1 41  ? -9.039  -6.028  -10.667 1.00 52.88  ? 84  PHE   A CZ  1 
ATOM   275  N  N   . SER   A 1 42  ? -2.259  -4.418  -9.849  1.00 56.56  ? 85  SER   A N   1 
ATOM   276  C  CA  . SER   A 1 42  ? -0.829  -4.240  -10.108 1.00 58.61  ? 85  SER   A CA  1 
ATOM   277  C  C   . SER   A 1 42  ? -0.260  -5.448  -10.822 1.00 61.29  ? 85  SER   A C   1 
ATOM   278  O  O   . SER   A 1 42  ? -0.757  -6.557  -10.624 1.00 61.67  ? 85  SER   A O   1 
ATOM   279  C  CB  . SER   A 1 42  ? -0.066  -3.968  -8.814  1.00 59.12  ? 85  SER   A CB  1 
ATOM   280  O  OG  . SER   A 1 42  ? -0.281  -4.982  -7.847  1.00 60.81  ? 85  SER   A OG  1 
ATOM   281  N  N   . LEU   A 1 43  ? 0.768   -5.248  -11.657 1.00 62.98  ? 86  LEU   A N   1 
ATOM   282  C  CA  . LEU   A 1 43  ? 1.386   -6.375  -12.348 1.00 65.10  ? 86  LEU   A CA  1 
ATOM   283  C  C   . LEU   A 1 43  ? 2.338   -7.114  -11.431 1.00 66.93  ? 86  LEU   A C   1 
ATOM   284  O  O   . LEU   A 1 43  ? 3.067   -6.497  -10.653 1.00 67.11  ? 86  LEU   A O   1 
ATOM   285  C  CB  . LEU   A 1 43  ? 2.058   -5.947  -13.653 1.00 65.53  ? 86  LEU   A CB  1 
ATOM   286  C  CG  . LEU   A 1 43  ? 1.054   -5.672  -14.763 1.00 67.41  ? 86  LEU   A CG  1 
ATOM   287  C  CD1 . LEU   A 1 43  ? 1.693   -4.972  -15.925 1.00 68.01  ? 86  LEU   A CD1 1 
ATOM   288  C  CD2 . LEU   A 1 43  ? 0.360   -6.954  -15.211 1.00 68.26  ? 86  LEU   A CD2 1 
ATOM   289  N  N   . VAL   A 1 44  ? 2.300   -8.442  -11.492 1.00 67.96  ? 87  VAL   A N   1 
ATOM   290  C  CA  . VAL   A 1 44  ? 3.145   -9.300  -10.668 1.00 69.09  ? 87  VAL   A CA  1 
ATOM   291  C  C   . VAL   A 1 44  ? 4.202   -9.933  -11.552 1.00 70.63  ? 87  VAL   A C   1 
ATOM   292  O  O   . VAL   A 1 44  ? 3.857   -10.459 -12.612 1.00 70.80  ? 87  VAL   A O   1 
ATOM   293  C  CB  . VAL   A 1 44  ? 2.287   -10.388 -9.997  1.00 69.39  ? 87  VAL   A CB  1 
ATOM   294  C  CG1 . VAL   A 1 44  ? 3.151   -11.313 -9.144  1.00 70.08  ? 87  VAL   A CG1 1 
ATOM   295  C  CG2 . VAL   A 1 44  ? 1.166   -9.765  -9.178  1.00 69.43  ? 87  VAL   A CG2 1 
ATOM   296  N  N   . GLU   A 1 45  ? 5.481   -9.884  -11.147 1.00 71.56  ? 88  GLU   A N   1 
ATOM   297  C  CA  . GLU   A 1 45  ? 6.540   -10.482 -11.966 1.00 73.40  ? 88  GLU   A CA  1 
ATOM   298  C  C   . GLU   A 1 45  ? 7.505   -11.428 -11.187 1.00 74.03  ? 88  GLU   A C   1 
ATOM   299  O  O   . GLU   A 1 45  ? 7.160   -12.001 -10.147 1.00 74.14  ? 88  GLU   A O   1 
ATOM   300  C  CB  . GLU   A 1 45  ? 7.330   -9.396  -12.727 1.00 76.62  ? 88  GLU   A CB  1 
ATOM   301  C  CG  . GLU   A 1 45  ? 6.483   -8.462  -13.578 1.00 81.65  ? 88  GLU   A CG  1 
ATOM   302  C  CD  . GLU   A 1 45  ? 6.020   -9.059  -14.891 1.00 88.06  ? 88  GLU   A CD  1 
ATOM   303  O  OE1 . GLU   A 1 45  ? 4.804   -8.971  -15.180 1.00 89.34  ? 88  GLU   A OE1 1 
ATOM   304  O  OE2 . GLU   A 1 45  ? 6.865   -9.628  -15.622 1.00 89.73  ? 88  GLU   A OE2 1 
ATOM   305  N  N   . GLY   B 2 7   ? -35.321 11.373  -11.350 1.00 75.95  ? 16  GLY   B N   1 
ATOM   306  C  CA  . GLY   B 2 7   ? -35.625 12.086  -12.586 1.00 76.48  ? 16  GLY   B CA  1 
ATOM   307  C  C   . GLY   B 2 7   ? -35.705 11.159  -13.783 1.00 76.76  ? 16  GLY   B C   1 
ATOM   308  O  O   . GLY   B 2 7   ? -36.748 10.536  -14.002 1.00 77.56  ? 16  GLY   B O   1 
ATOM   309  N  N   . GLU   B 2 8   ? -34.610 11.045  -14.569 1.00 75.70  ? 17  GLU   B N   1 
ATOM   310  C  CA  . GLU   B 2 8   ? -34.594 10.127  -15.712 1.00 75.08  ? 17  GLU   B CA  1 
ATOM   311  C  C   . GLU   B 2 8   ? -34.315 8.689   -15.248 1.00 73.64  ? 17  GLU   B C   1 
ATOM   312  O  O   . GLU   B 2 8   ? -33.236 8.370   -14.743 1.00 73.85  ? 17  GLU   B O   1 
ATOM   313  C  CB  . GLU   B 2 8   ? -33.611 10.562  -16.813 1.00 77.80  ? 17  GLU   B CB  1 
ATOM   314  C  CG  . GLU   B 2 8   ? -33.905 9.863   -18.132 1.00 83.16  ? 17  GLU   B CG  1 
ATOM   315  C  CD  . GLU   B 2 8   ? -33.131 10.333  -19.349 1.00 90.09  ? 17  GLU   B CD  1 
ATOM   316  O  OE1 . GLU   B 2 8   ? -32.165 11.114  -19.182 1.00 91.71  ? 17  GLU   B OE1 1 
ATOM   317  O  OE2 . GLU   B 2 8   ? -33.506 9.934   -20.476 1.00 92.20  ? 17  GLU   B OE2 1 
ATOM   318  N  N   . THR   B 2 9   ? -35.315 7.836   -15.396 1.00 71.98  ? 18  THR   B N   1 
ATOM   319  C  CA  . THR   B 2 9   ? -35.261 6.444   -14.958 1.00 70.76  ? 18  THR   B CA  1 
ATOM   320  C  C   . THR   B 2 9   ? -35.082 5.431   -16.098 1.00 68.67  ? 18  THR   B C   1 
ATOM   321  O  O   . THR   B 2 9   ? -35.050 4.230   -15.837 1.00 68.96  ? 18  THR   B O   1 
ATOM   322  C  CB  . THR   B 2 9   ? -36.562 6.146   -14.199 1.00 72.51  ? 18  THR   B CB  1 
ATOM   323  O  OG1 . THR   B 2 9   ? -37.678 6.449   -15.052 1.00 73.57  ? 18  THR   B OG1 1 
ATOM   324  C  CG2 . THR   B 2 9   ? -36.682 6.962   -12.917 1.00 72.93  ? 18  THR   B CG2 1 
ATOM   325  N  N   . THR   B 2 10  ? -34.997 5.905   -17.349 1.00 66.43  ? 19  THR   B N   1 
ATOM   326  C  CA  . THR   B 2 10  ? -34.908 5.087   -18.552 1.00 64.58  ? 19  THR   B CA  1 
ATOM   327  C  C   . THR   B 2 10  ? -33.699 4.187   -18.557 1.00 62.16  ? 19  THR   B C   1 
ATOM   328  O  O   . THR   B 2 10  ? -32.583 4.657   -18.374 1.00 62.08  ? 19  THR   B O   1 
ATOM   329  C  CB  . THR   B 2 10  ? -34.890 5.983   -19.818 1.00 66.08  ? 19  THR   B CB  1 
ATOM   330  O  OG1 . THR   B 2 10  ? -35.855 7.040   -19.705 1.00 67.87  ? 19  THR   B OG1 1 
ATOM   331  C  CG2 . THR   B 2 10  ? -35.121 5.190   -21.100 1.00 65.90  ? 19  THR   B CG2 1 
ATOM   332  N  N   . ASP   B 2 11  ? -33.906 2.902   -18.844 1.00 60.06  ? 20  ASP   B N   1 
ATOM   333  C  CA  . ASP   B 2 11  ? -32.842 1.911   -18.977 1.00 58.65  ? 20  ASP   B CA  1 
ATOM   334  C  C   . ASP   B 2 11  ? -31.862 2.366   -20.082 1.00 56.97  ? 20  ASP   B C   1 
ATOM   335  O  O   . ASP   B 2 11  ? -32.309 2.881   -21.102 1.00 57.25  ? 20  ASP   B O   1 
ATOM   336  C  CB  . ASP   B 2 11  ? -33.476 0.580   -19.404 1.00 60.46  ? 20  ASP   B CB  1 
ATOM   337  C  CG  . ASP   B 2 11  ? -33.530 -0.491  -18.336 1.00 65.15  ? 20  ASP   B CG  1 
ATOM   338  O  OD1 . ASP   B 2 11  ? -34.009 -0.191  -17.214 1.00 64.75  ? 20  ASP   B OD1 1 
ATOM   339  O  OD2 . ASP   B 2 11  ? -33.113 -1.641  -18.629 1.00 68.26  ? 20  ASP   B OD2 1 
ATOM   340  N  N   . GLY   B 2 12  ? -30.558 2.208   -19.866 1.00 55.12  ? 21  GLY   B N   1 
ATOM   341  C  CA  . GLY   B 2 12  ? -29.567 2.604   -20.860 1.00 53.95  ? 21  GLY   B CA  1 
ATOM   342  C  C   . GLY   B 2 12  ? -28.248 3.077   -20.284 1.00 52.76  ? 21  GLY   B C   1 
ATOM   343  O  O   . GLY   B 2 12  ? -28.030 3.013   -19.076 1.00 52.60  ? 21  GLY   B O   1 
ATOM   344  N  N   . VAL   B 2 13  ? -27.336 3.526   -21.154 1.00 51.77  ? 22  VAL   B N   1 
ATOM   345  C  CA  . VAL   B 2 13  ? -26.031 4.029   -20.728 1.00 50.85  ? 22  VAL   B CA  1 
ATOM   346  C  C   . VAL   B 2 13  ? -26.091 5.560   -20.535 1.00 50.35  ? 22  VAL   B C   1 
ATOM   347  O  O   . VAL   B 2 13  ? -26.864 6.253   -21.201 1.00 50.06  ? 22  VAL   B O   1 
ATOM   348  C  CB  . VAL   B 2 13  ? -24.891 3.544   -21.648 1.00 51.08  ? 22  VAL   B CB  1 
ATOM   349  C  CG1 . VAL   B 2 13  ? -25.068 4.042   -23.080 1.00 51.05  ? 22  VAL   B CG1 1 
ATOM   350  C  CG2 . VAL   B 2 13  ? -23.518 3.898   -21.087 1.00 51.25  ? 22  VAL   B CG2 1 
ATOM   351  N  N   . TYR   B 2 14  ? -25.370 6.059   -19.531 1.00 49.84  ? 23  TYR   B N   1 
ATOM   352  C  CA  . TYR   B 2 14  ? -25.404 7.455   -19.135 1.00 49.44  ? 23  TYR   B CA  1 
ATOM   353  C  C   . TYR   B 2 14  ? -24.009 8.003   -18.874 1.00 48.97  ? 23  TYR   B C   1 
ATOM   354  O  O   . TYR   B 2 14  ? -23.141 7.278   -18.425 1.00 48.52  ? 23  TYR   B O   1 
ATOM   355  C  CB  . TYR   B 2 14  ? -26.193 7.566   -17.813 1.00 49.29  ? 23  TYR   B CB  1 
ATOM   356  C  CG  . TYR   B 2 14  ? -27.694 7.482   -17.964 1.00 49.93  ? 23  TYR   B CG  1 
ATOM   357  C  CD1 . TYR   B 2 14  ? -28.320 6.271   -18.215 1.00 50.69  ? 23  TYR   B CD1 1 
ATOM   358  C  CD2 . TYR   B 2 14  ? -28.497 8.594   -17.759 1.00 50.97  ? 23  TYR   B CD2 1 
ATOM   359  C  CE1 . TYR   B 2 14  ? -29.695 6.191   -18.382 1.00 51.64  ? 23  TYR   B CE1 1 
ATOM   360  C  CE2 . TYR   B 2 14  ? -29.879 8.520   -17.889 1.00 52.01  ? 23  TYR   B CE2 1 
ATOM   361  C  CZ  . TYR   B 2 14  ? -30.475 7.312   -18.198 1.00 52.93  ? 23  TYR   B CZ  1 
ATOM   362  O  OH  . TYR   B 2 14  ? -31.840 7.211   -18.318 1.00 54.67  ? 23  TYR   B OH  1 
ATOM   363  N  N   . ARG   B 2 15  ? -23.825 9.304   -19.060 1.00 49.10  ? 24  ARG   B N   1 
ATOM   364  C  CA  . ARG   B 2 15  ? -22.571 9.965   -18.718 1.00 49.27  ? 24  ARG   B CA  1 
ATOM   365  C  C   . ARG   B 2 15  ? -22.726 10.547  -17.311 1.00 49.12  ? 24  ARG   B C   1 
ATOM   366  O  O   . ARG   B 2 15  ? -23.793 11.039  -16.968 1.00 48.98  ? 24  ARG   B O   1 
ATOM   367  C  CB  . ARG   B 2 15  ? -22.269 11.130  -19.680 1.00 50.02  ? 24  ARG   B CB  1 
ATOM   368  C  CG  . ARG   B 2 15  ? -22.514 10.852  -21.138 1.00 52.14  ? 24  ARG   B CG  1 
ATOM   369  C  CD  . ARG   B 2 15  ? -22.169 12.088  -21.948 1.00 55.26  ? 24  ARG   B CD  1 
ATOM   370  N  NE  . ARG   B 2 15  ? -22.392 11.894  -23.381 1.00 57.34  ? 24  ARG   B NE  1 
ATOM   371  C  CZ  . ARG   B 2 15  ? -21.442 11.550  -24.246 1.00 59.22  ? 24  ARG   B CZ  1 
ATOM   372  N  NH1 . ARG   B 2 15  ? -20.186 11.386  -23.836 1.00 58.91  ? 24  ARG   B NH1 1 
ATOM   373  N  NH2 . ARG   B 2 15  ? -21.736 11.383  -25.530 1.00 58.30  ? 24  ARG   B NH2 1 
ATOM   374  N  N   . VAL   B 2 16  ? -21.650 10.540  -16.532 1.00 48.96  ? 25  VAL   B N   1 
ATOM   375  C  CA  . VAL   B 2 16  ? -21.565 11.118  -15.196 1.00 49.51  ? 25  VAL   B CA  1 
ATOM   376  C  C   . VAL   B 2 16  ? -20.717 12.405  -15.322 1.00 50.49  ? 25  VAL   B C   1 
ATOM   377  O  O   . VAL   B 2 16  ? -19.532 12.348  -15.626 1.00 50.54  ? 25  VAL   B O   1 
ATOM   378  C  CB  . VAL   B 2 16  ? -20.992 10.113  -14.154 1.00 49.85  ? 25  VAL   B CB  1 
ATOM   379  C  CG1 . VAL   B 2 16  ? -21.133 10.660  -12.737 1.00 50.54  ? 25  VAL   B CG1 1 
ATOM   380  C  CG2 . VAL   B 2 16  ? -21.669 8.750   -14.269 1.00 49.71  ? 25  VAL   B CG2 1 
ATOM   381  N  N   . MET   B 2 17  ? -21.352 13.560  -15.165 1.00 51.61  ? 26  MET   B N   1 
ATOM   382  C  CA  . MET   B 2 17  ? -20.747 14.872  -15.362 1.00 53.40  ? 26  MET   B CA  1 
ATOM   383  C  C   . MET   B 2 17  ? -20.588 15.665  -14.070 1.00 56.08  ? 26  MET   B C   1 
ATOM   384  O  O   . MET   B 2 17  ? -21.295 15.398  -13.114 1.00 56.31  ? 26  MET   B O   1 
ATOM   385  C  CB  . MET   B 2 17  ? -21.656 15.704  -16.289 1.00 53.35  ? 26  MET   B CB  1 
ATOM   386  C  CG  . MET   B 2 17  ? -22.091 15.027  -17.567 1.00 53.90  ? 26  MET   B CG  1 
ATOM   387  S  SD  . MET   B 2 17  ? -20.745 14.860  -18.754 1.00 56.86  ? 26  MET   B SD  1 
ATOM   388  C  CE  . MET   B 2 17  ? -20.121 16.569  -18.787 1.00 54.13  ? 26  MET   B CE  1 
ATOM   389  N  N   . THR   B 2 18  ? -19.712 16.693  -14.065 1.00 58.32  ? 27  THR   B N   1 
ATOM   390  C  CA  . THR   B 2 18  ? -19.550 17.601  -12.928 1.00 61.12  ? 27  THR   B CA  1 
ATOM   391  C  C   . THR   B 2 18  ? -19.276 19.062  -13.367 1.00 63.64  ? 27  THR   B C   1 
ATOM   392  O  O   . THR   B 2 18  ? -18.542 19.323  -14.329 1.00 63.41  ? 27  THR   B O   1 
ATOM   393  C  CB  . THR   B 2 18  ? -18.517 17.107  -11.900 1.00 62.85  ? 27  THR   B CB  1 
ATOM   394  O  OG1 . THR   B 2 18  ? -18.619 17.940  -10.739 1.00 64.72  ? 27  THR   B OG1 1 
ATOM   395  C  CG2 . THR   B 2 18  ? -17.099 17.150  -12.422 1.00 62.78  ? 27  THR   B CG2 1 
ATOM   396  N  N   . ARG   B 2 19  ? -19.890 20.012  -12.656 1.00 65.57  ? 28  ARG   B N   1 
ATOM   397  C  CA  . ARG   B 2 19  ? -19.687 21.432  -12.937 1.00 67.96  ? 28  ARG   B CA  1 
ATOM   398  C  C   . ARG   B 2 19  ? -18.718 22.104  -11.926 1.00 69.89  ? 28  ARG   B C   1 
ATOM   399  O  O   . ARG   B 2 19  ? -18.558 23.330  -11.955 1.00 70.24  ? 28  ARG   B O   1 
ATOM   400  C  CB  . ARG   B 2 19  ? -21.036 22.179  -12.995 1.00 69.99  ? 28  ARG   B CB  1 
ATOM   401  C  CG  . ARG   B 2 19  ? -21.961 21.694  -14.108 1.00 74.67  ? 28  ARG   B CG  1 
ATOM   402  C  CD  . ARG   B 2 19  ? -22.968 22.754  -14.533 1.00 80.07  ? 28  ARG   B CD  1 
ATOM   403  N  NE  . ARG   B 2 19  ? -23.988 22.235  -15.454 1.00 84.92  ? 28  ARG   B NE  1 
ATOM   404  C  CZ  . ARG   B 2 19  ? -25.188 21.796  -15.073 1.00 88.58  ? 28  ARG   B CZ  1 
ATOM   405  N  NH1 . ARG   B 2 19  ? -25.531 21.808  -13.788 1.00 88.96  ? 28  ARG   B NH1 1 
ATOM   406  N  NH2 . ARG   B 2 19  ? -26.050 21.337  -15.972 1.00 88.49  ? 28  ARG   B NH2 1 
ATOM   407  N  N   . ARG   B 2 20  ? -18.077 21.303  -11.041 1.00 70.88  ? 29  ARG   B N   1 
ATOM   408  C  CA  . ARG   B 2 20  ? -17.146 21.775  -10.011 1.00 72.25  ? 29  ARG   B CA  1 
ATOM   409  C  C   . ARG   B 2 20  ? -15.819 22.282  -10.614 1.00 72.10  ? 29  ARG   B C   1 
ATOM   410  O  O   . ARG   B 2 20  ? -15.197 23.207  -10.085 1.00 72.10  ? 29  ARG   B O   1 
ATOM   411  C  CB  . ARG   B 2 20  ? -16.908 20.666  -8.962  1.00 74.99  ? 29  ARG   B CB  1 
ATOM   412  C  CG  . ARG   B 2 20  ? -16.164 21.139  -7.720  1.00 80.36  ? 29  ARG   B CG  1 
ATOM   413  C  CD  . ARG   B 2 20  ? -15.669 19.979  -6.879  1.00 86.12  ? 29  ARG   B CD  1 
ATOM   414  N  NE  . ARG   B 2 20  ? -14.695 19.135  -7.583  1.00 91.00  ? 29  ARG   B NE  1 
ATOM   415  C  CZ  . ARG   B 2 20  ? -13.415 19.014  -7.235  1.00 94.26  ? 29  ARG   B CZ  1 
ATOM   416  N  NH1 . ARG   B 2 20  ? -12.936 19.687  -6.195  1.00 94.51  ? 29  ARG   B NH1 1 
ATOM   417  N  NH2 . ARG   B 2 20  ? -12.607 18.213  -7.922  1.00 94.05  ? 29  ARG   B NH2 1 
ATOM   418  N  N   . LEU   B 2 21  ? -15.407 21.697  -11.737 1.00 71.74  ? 30  LEU   B N   1 
ATOM   419  C  CA  . LEU   B 2 21  ? -14.191 22.114  -12.424 1.00 71.77  ? 30  LEU   B CA  1 
ATOM   420  C  C   . LEU   B 2 21  ? -14.522 23.147  -13.553 1.00 71.57  ? 30  LEU   B C   1 
ATOM   421  O  O   . LEU   B 2 21  ? -15.661 23.632  -13.626 1.00 71.89  ? 30  LEU   B O   1 
ATOM   422  C  CB  . LEU   B 2 21  ? -13.441 20.874  -12.946 1.00 71.86  ? 30  LEU   B CB  1 
ATOM   423  C  CG  . LEU   B 2 21  ? -12.709 20.059  -11.888 1.00 73.16  ? 30  LEU   B CG  1 
ATOM   424  C  CD1 . LEU   B 2 21  ? -13.652 19.132  -11.158 1.00 73.81  ? 30  LEU   B CD1 1 
ATOM   425  C  CD2 . LEU   B 2 21  ? -11.590 19.247  -12.509 1.00 73.68  ? 30  LEU   B CD2 1 
ATOM   426  N  N   . LEU   B 2 22  ? -13.531 23.531  -14.385 1.00 70.63  ? 31  LEU   B N   1 
ATOM   427  C  CA  . LEU   B 2 22  ? -13.761 24.494  -15.466 1.00 70.12  ? 31  LEU   B CA  1 
ATOM   428  C  C   . LEU   B 2 22  ? -14.755 23.914  -16.474 1.00 69.71  ? 31  LEU   B C   1 
ATOM   429  O  O   . LEU   B 2 22  ? -14.485 22.862  -17.057 1.00 70.59  ? 31  LEU   B O   1 
ATOM   430  C  CB  . LEU   B 2 22  ? -12.437 24.800  -16.164 1.00 69.89  ? 31  LEU   B CB  1 
ATOM   431  C  CG  . LEU   B 2 22  ? -12.510 25.822  -17.258 1.00 70.44  ? 31  LEU   B CG  1 
ATOM   432  C  CD1 . LEU   B 2 22  ? -12.001 27.153  -16.778 1.00 70.41  ? 31  LEU   B CD1 1 
ATOM   433  C  CD2 . LEU   B 2 22  ? -11.753 25.344  -18.463 1.00 71.13  ? 31  LEU   B CD2 1 
ATOM   434  N  N   . GLY   B 2 23  ? -15.901 24.570  -16.645 1.00 68.13  ? 32  GLY   B N   1 
ATOM   435  C  CA  . GLY   B 2 23  ? -16.946 24.064  -17.527 1.00 66.87  ? 32  GLY   B CA  1 
ATOM   436  C  C   . GLY   B 2 23  ? -17.548 22.768  -17.005 1.00 65.11  ? 32  GLY   B C   1 
ATOM   437  O  O   . GLY   B 2 23  ? -17.455 22.473  -15.811 1.00 64.92  ? 32  GLY   B O   1 
ATOM   438  N  N   . SER   B 2 24  ? -18.169 21.980  -17.888 1.00 63.78  ? 33  SER   B N   1 
ATOM   439  C  CA  . SER   B 2 24  ? -18.751 20.695  -17.495 1.00 63.01  ? 33  SER   B CA  1 
ATOM   440  C  C   . SER   B 2 24  ? -17.761 19.596  -17.868 1.00 62.03  ? 33  SER   B C   1 
ATOM   441  O  O   . SER   B 2 24  ? -17.332 19.533  -19.017 1.00 62.32  ? 33  SER   B O   1 
ATOM   442  C  CB  . SER   B 2 24  ? -20.086 20.470  -18.195 1.00 64.12  ? 33  SER   B CB  1 
ATOM   443  O  OG  . SER   B 2 24  ? -21.025 21.470  -17.833 1.00 66.28  ? 33  SER   B OG  1 
ATOM   444  N  N   . THR   B 2 25  ? -17.369 18.753  -16.902 1.00 60.65  ? 34  THR   B N   1 
ATOM   445  C  CA  . THR   B 2 25  ? -16.371 17.712  -17.154 1.00 59.67  ? 34  THR   B CA  1 
ATOM   446  C  C   . THR   B 2 25  ? -16.928 16.296  -16.950 1.00 57.92  ? 34  THR   B C   1 
ATOM   447  O  O   . THR   B 2 25  ? -17.554 16.040  -15.929 1.00 58.05  ? 34  THR   B O   1 
ATOM   448  C  CB  . THR   B 2 25  ? -15.142 17.975  -16.260 1.00 61.19  ? 34  THR   B CB  1 
ATOM   449  O  OG1 . THR   B 2 25  ? -14.679 19.323  -16.452 1.00 62.29  ? 34  THR   B OG1 1 
ATOM   450  C  CG2 . THR   B 2 25  ? -14.017 16.986  -16.510 1.00 61.51  ? 34  THR   B CG2 1 
ATOM   451  N  N   . GLN   B 2 26  ? -16.699 15.375  -17.903 1.00 56.25  ? 35  GLN   B N   1 
ATOM   452  C  CA  . GLN   B 2 26  ? -17.189 14.000  -17.766 1.00 55.48  ? 35  GLN   B CA  1 
ATOM   453  C  C   . GLN   B 2 26  ? -16.255 13.118  -16.920 1.00 55.63  ? 35  GLN   B C   1 
ATOM   454  O  O   . GLN   B 2 26  ? -15.199 12.689  -17.398 1.00 56.41  ? 35  GLN   B O   1 
ATOM   455  C  CB  . GLN   B 2 26  ? -17.435 13.338  -19.128 1.00 55.21  ? 35  GLN   B CB  1 
ATOM   456  C  CG  . GLN   B 2 26  ? -18.038 11.950  -18.995 1.00 54.43  ? 35  GLN   B CG  1 
ATOM   457  C  CD  . GLN   B 2 26  ? -18.197 11.260  -20.312 1.00 54.67  ? 35  GLN   B CD  1 
ATOM   458  O  OE1 . GLN   B 2 26  ? -18.851 11.765  -21.235 1.00 55.36  ? 35  GLN   B OE1 1 
ATOM   459  N  NE2 . GLN   B 2 26  ? -17.619 10.074  -20.416 1.00 53.92  ? 35  GLN   B NE2 1 
ATOM   460  N  N   . VAL   B 2 27  ? -16.662 12.820  -15.680 1.00 54.19  ? 36  VAL   B N   1 
ATOM   461  C  CA  . VAL   B 2 27  ? -15.859 12.000  -14.776 1.00 53.14  ? 36  VAL   B CA  1 
ATOM   462  C  C   . VAL   B 2 27  ? -15.991 10.479  -15.021 1.00 52.49  ? 36  VAL   B C   1 
ATOM   463  O  O   . VAL   B 2 27  ? -15.159 9.691   -14.553 1.00 52.61  ? 36  VAL   B O   1 
ATOM   464  C  CB  . VAL   B 2 27  ? -16.186 12.367  -13.306 1.00 53.24  ? 36  VAL   B CB  1 
ATOM   465  C  CG1 . VAL   B 2 27  ? -15.983 13.853  -13.065 1.00 53.58  ? 36  VAL   B CG1 1 
ATOM   466  C  CG2 . VAL   B 2 27  ? -17.606 11.957  -12.931 1.00 53.21  ? 36  VAL   B CG2 1 
ATOM   467  N  N   . GLY   B 2 28  ? -17.046 10.079  -15.716 1.00 51.46  ? 37  GLY   B N   1 
ATOM   468  C  CA  . GLY   B 2 28  ? -17.306 8.676   -15.953 1.00 50.80  ? 37  GLY   B CA  1 
ATOM   469  C  C   . GLY   B 2 28  ? -18.622 8.419   -16.638 1.00 49.99  ? 37  GLY   B C   1 
ATOM   470  O  O   . GLY   B 2 28  ? -19.226 9.324   -17.211 1.00 50.12  ? 37  GLY   B O   1 
ATOM   471  N  N   . VAL   B 2 29  ? -19.047 7.159   -16.589 1.00 49.01  ? 38  VAL   B N   1 
ATOM   472  C  CA  . VAL   B 2 29  ? -20.196 6.560   -17.260 1.00 48.40  ? 38  VAL   B CA  1 
ATOM   473  C  C   . VAL   B 2 29  ? -20.889 5.563   -16.296 1.00 47.52  ? 38  VAL   B C   1 
ATOM   474  O  O   . VAL   B 2 29  ? -20.280 5.091   -15.332 1.00 47.61  ? 38  VAL   B O   1 
ATOM   475  C  CB  . VAL   B 2 29  ? -19.660 5.831   -18.545 1.00 48.88  ? 38  VAL   B CB  1 
ATOM   476  C  CG1 . VAL   B 2 29  ? -20.730 5.009   -19.241 1.00 49.62  ? 38  VAL   B CG1 1 
ATOM   477  C  CG2 . VAL   B 2 29  ? -19.017 6.801   -19.527 1.00 48.96  ? 38  VAL   B CG2 1 
ATOM   478  N  N   . GLY   B 2 30  ? -22.142 5.240   -16.569 1.00 46.59  ? 39  GLY   B N   1 
ATOM   479  C  CA  . GLY   B 2 30  ? -22.873 4.271   -15.774 1.00 46.51  ? 39  GLY   B CA  1 
ATOM   480  C  C   . GLY   B 2 30  ? -24.006 3.612   -16.523 1.00 46.85  ? 39  GLY   B C   1 
ATOM   481  O  O   . GLY   B 2 30  ? -24.390 4.053   -17.605 1.00 46.82  ? 39  GLY   B O   1 
ATOM   482  N  N   . VAL   B 2 31  ? -24.563 2.559   -15.941 1.00 47.17  ? 40  VAL   B N   1 
ATOM   483  C  CA  . VAL   B 2 31  ? -25.646 1.799   -16.549 1.00 47.91  ? 40  VAL   B CA  1 
ATOM   484  C  C   . VAL   B 2 31  ? -26.892 1.884   -15.707 1.00 48.47  ? 40  VAL   B C   1 
ATOM   485  O  O   . VAL   B 2 31  ? -26.861 1.543   -14.536 1.00 48.99  ? 40  VAL   B O   1 
ATOM   486  C  CB  . VAL   B 2 31  ? -25.224 0.320   -16.722 1.00 48.69  ? 40  VAL   B CB  1 
ATOM   487  C  CG1 . VAL   B 2 31  ? -26.372 -0.517  -17.270 1.00 49.53  ? 40  VAL   B CG1 1 
ATOM   488  C  CG2 . VAL   B 2 31  ? -23.998 0.208   -17.614 1.00 48.83  ? 40  VAL   B CG2 1 
ATOM   489  N  N   . MET   B 2 32  ? -27.990 2.315   -16.293 1.00 48.54  ? 41  MET   B N   1 
ATOM   490  C  CA  . MET   B 2 32  ? -29.274 2.355   -15.615 1.00 48.98  ? 41  MET   B CA  1 
ATOM   491  C  C   . MET   B 2 32  ? -29.982 1.057   -16.023 1.00 50.06  ? 41  MET   B C   1 
ATOM   492  O  O   . MET   B 2 32  ? -30.143 0.811   -17.217 1.00 50.35  ? 41  MET   B O   1 
ATOM   493  C  CB  . MET   B 2 32  ? -30.079 3.570   -16.103 1.00 48.72  ? 41  MET   B CB  1 
ATOM   494  C  CG  . MET   B 2 32  ? -31.370 3.786   -15.355 1.00 50.10  ? 41  MET   B CG  1 
ATOM   495  S  SD  . MET   B 2 32  ? -31.125 4.394   -13.667 1.00 53.55  ? 41  MET   B SD  1 
ATOM   496  C  CE  . MET   B 2 32  ? -30.382 5.967   -14.009 1.00 51.51  ? 41  MET   B CE  1 
ATOM   497  N  N   . GLN   B 2 33  ? -30.340 0.195   -15.062 1.00 50.40  ? 42  GLN   B N   1 
ATOM   498  C  CA  . GLN   B 2 33  ? -31.050 -1.046  -15.386 1.00 51.12  ? 42  GLN   B CA  1 
ATOM   499  C  C   . GLN   B 2 33  ? -31.942 -1.426  -14.244 1.00 51.40  ? 42  GLN   B C   1 
ATOM   500  O  O   . GLN   B 2 33  ? -31.469 -1.485  -13.122 1.00 52.28  ? 42  GLN   B O   1 
ATOM   501  C  CB  . GLN   B 2 33  ? -30.102 -2.199  -15.700 1.00 53.06  ? 42  GLN   B CB  1 
ATOM   502  C  CG  . GLN   B 2 33  ? -30.874 -3.424  -16.177 1.00 58.06  ? 42  GLN   B CG  1 
ATOM   503  C  CD  . GLN   B 2 33  ? -29.970 -4.541  -16.600 1.00 63.85  ? 42  GLN   B CD  1 
ATOM   504  O  OE1 . GLN   B 2 33  ? -29.961 -5.633  -16.012 1.00 65.51  ? 42  GLN   B OE1 1 
ATOM   505  N  NE2 . GLN   B 2 33  ? -29.176 -4.284  -17.627 1.00 65.20  ? 42  GLN   B NE2 1 
ATOM   506  N  N   . GLU   B 2 34  ? -33.224 -1.660  -14.512 1.00 50.97  ? 43  GLU   B N   1 
ATOM   507  C  CA  . GLU   B 2 34  ? -34.202 -2.021  -13.497 1.00 51.15  ? 43  GLU   B CA  1 
ATOM   508  C  C   . GLU   B 2 34  ? -34.275 -0.975  -12.368 1.00 50.94  ? 43  GLU   B C   1 
ATOM   509  O  O   . GLU   B 2 34  ? -34.341 -1.339  -11.202 1.00 51.43  ? 43  GLU   B O   1 
ATOM   510  C  CB  . GLU   B 2 34  ? -33.932 -3.432  -12.936 1.00 53.87  ? 43  GLU   B CB  1 
ATOM   511  C  CG  . GLU   B 2 34  ? -33.908 -4.554  -13.965 1.00 58.70  ? 43  GLU   B CG  1 
ATOM   512  C  CD  . GLU   B 2 34  ? -33.310 -5.862  -13.461 1.00 66.58  ? 43  GLU   B CD  1 
ATOM   513  O  OE1 . GLU   B 2 34  ? -33.524 -6.209  -12.274 1.00 68.28  ? 43  GLU   B OE1 1 
ATOM   514  O  OE2 . GLU   B 2 34  ? -32.621 -6.542  -14.259 1.00 68.37  ? 43  GLU   B OE2 1 
ATOM   515  N  N   . GLY   B 2 35  ? -34.209 0.306   -12.724 1.00 50.12  ? 44  GLY   B N   1 
ATOM   516  C  CA  . GLY   B 2 35  ? -34.287 1.420   -11.781 1.00 49.40  ? 44  GLY   B CA  1 
ATOM   517  C  C   . GLY   B 2 35  ? -33.041 1.686   -10.962 1.00 48.84  ? 44  GLY   B C   1 
ATOM   518  O  O   . GLY   B 2 35  ? -33.052 2.546   -10.076 1.00 49.46  ? 44  GLY   B O   1 
ATOM   519  N  N   . VAL   B 2 36  ? -31.961 0.936   -11.218 1.00 47.41  ? 45  VAL   B N   1 
ATOM   520  C  CA  . VAL   B 2 36  ? -30.724 1.079   -10.466 1.00 46.18  ? 45  VAL   B CA  1 
ATOM   521  C  C   . VAL   B 2 36  ? -29.622 1.645   -11.363 1.00 45.43  ? 45  VAL   B C   1 
ATOM   522  O  O   . VAL   B 2 36  ? -29.457 1.206   -12.504 1.00 45.14  ? 45  VAL   B O   1 
ATOM   523  C  CB  . VAL   B 2 36  ? -30.342 -0.269  -9.783  1.00 46.24  ? 45  VAL   B CB  1 
ATOM   524  C  CG1 . VAL   B 2 36  ? -28.956 -0.233  -9.145  1.00 46.51  ? 45  VAL   B CG1 1 
ATOM   525  C  CG2 . VAL   B 2 36  ? -31.382 -0.656  -8.751  1.00 46.47  ? 45  VAL   B CG2 1 
ATOM   526  N  N   . PHE   B 2 37  ? -28.911 2.670   -10.868 1.00 44.71  ? 46  PHE   B N   1 
ATOM   527  C  CA  . PHE   B 2 37  ? -27.797 3.242   -11.597 1.00 44.45  ? 46  PHE   B CA  1 
ATOM   528  C  C   . PHE   B 2 37  ? -26.523 2.567   -11.086 1.00 43.88  ? 46  PHE   B C   1 
ATOM   529  O  O   . PHE   B 2 37  ? -26.254 2.621   -9.899  1.00 43.81  ? 46  PHE   B O   1 
ATOM   530  C  CB  . PHE   B 2 37  ? -27.726 4.759   -11.404 1.00 44.71  ? 46  PHE   B CB  1 
ATOM   531  C  CG  . PHE   B 2 37  ? -26.719 5.387   -12.338 1.00 45.97  ? 46  PHE   B CG  1 
ATOM   532  C  CD1 . PHE   B 2 37  ? -26.882 5.311   -13.709 1.00 46.46  ? 46  PHE   B CD1 1 
ATOM   533  C  CD2 . PHE   B 2 37  ? -25.565 5.977   -11.846 1.00 47.10  ? 46  PHE   B CD2 1 
ATOM   534  C  CE1 . PHE   B 2 37  ? -25.943 5.864   -14.569 1.00 47.20  ? 46  PHE   B CE1 1 
ATOM   535  C  CE2 . PHE   B 2 37  ? -24.620 6.511   -12.710 1.00 47.74  ? 46  PHE   B CE2 1 
ATOM   536  C  CZ  . PHE   B 2 37  ? -24.828 6.472   -14.065 1.00 47.27  ? 46  PHE   B CZ  1 
ATOM   537  N  N   . HIS   B 2 38  ? -25.769 1.884   -11.971 1.00 43.22  ? 47  HIS   B N   1 
ATOM   538  C  CA  . HIS   B 2 38  ? -24.547 1.165   -11.626 1.00 42.55  ? 47  HIS   B CA  1 
ATOM   539  C  C   . HIS   B 2 38  ? -23.362 1.892   -12.216 1.00 42.65  ? 47  HIS   B C   1 
ATOM   540  O  O   . HIS   B 2 38  ? -23.358 2.148   -13.407 1.00 42.71  ? 47  HIS   B O   1 
ATOM   541  C  CB  . HIS   B 2 38  ? -24.570 -0.237  -12.250 1.00 42.61  ? 47  HIS   B CB  1 
ATOM   542  C  CG  . HIS   B 2 38  ? -25.809 -1.014  -11.968 1.00 43.88  ? 47  HIS   B CG  1 
ATOM   543  N  ND1 . HIS   B 2 38  ? -27.018 -0.682  -12.558 1.00 45.03  ? 47  HIS   B ND1 1 
ATOM   544  C  CD2 . HIS   B 2 38  ? -25.992 -2.086  -11.162 1.00 44.70  ? 47  HIS   B CD2 1 
ATOM   545  C  CE1 . HIS   B 2 38  ? -27.896 -1.553  -12.087 1.00 45.52  ? 47  HIS   B CE1 1 
ATOM   546  N  NE2 . HIS   B 2 38  ? -27.323 -2.413  -11.239 1.00 45.77  ? 47  HIS   B NE2 1 
ATOM   547  N  N   . THR   B 2 39  ? -22.336 2.190   -11.417 1.00 42.44  ? 48  THR   B N   1 
ATOM   548  C  CA  . THR   B 2 39  ? -21.124 2.832   -11.942 1.00 42.37  ? 48  THR   B CA  1 
ATOM   549  C  C   . THR   B 2 39  ? -19.897 2.321   -11.135 1.00 41.75  ? 48  THR   B C   1 
ATOM   550  O  O   . THR   B 2 39  ? -20.026 1.395   -10.326 1.00 41.12  ? 48  THR   B O   1 
ATOM   551  C  CB  . THR   B 2 39  ? -21.307 4.388   -12.052 1.00 43.87  ? 48  THR   B CB  1 
ATOM   552  O  OG1 . THR   B 2 39  ? -20.215 4.942   -12.793 1.00 44.45  ? 48  THR   B OG1 1 
ATOM   553  C  CG2 . THR   B 2 39  ? -21.425 5.079   -10.684 1.00 44.56  ? 48  THR   B CG2 1 
ATOM   554  N  N   . MET   B 2 40  ? -18.710 2.862   -11.405 1.00 41.59  ? 49  MET   B N   1 
ATOM   555  C  CA  . MET   B 2 40  ? -17.509 2.491   -10.674 1.00 41.81  ? 49  MET   B CA  1 
ATOM   556  C  C   . MET   B 2 40  ? -17.360 3.452   -9.500  1.00 42.44  ? 49  MET   B C   1 
ATOM   557  O  O   . MET   B 2 40  ? -17.623 4.641   -9.645  1.00 43.09  ? 49  MET   B O   1 
ATOM   558  C  CB  . MET   B 2 40  ? -16.279 2.525   -11.601 1.00 42.17  ? 49  MET   B CB  1 
ATOM   559  C  CG  . MET   B 2 40  ? -16.475 1.721   -12.878 1.00 43.99  ? 49  MET   B CG  1 
ATOM   560  S  SD  . MET   B 2 40  ? -14.999 0.818   -13.429 1.00 47.94  ? 49  MET   B SD  1 
ATOM   561  C  CE  . MET   B 2 40  ? -15.018 -0.579  -12.321 1.00 45.14  ? 49  MET   B CE  1 
ATOM   562  N  N   . TRP   B 2 41  ? -16.942 2.943   -8.341  1.00 42.53  ? 50  TRP   B N   1 
ATOM   563  C  CA  A TRP   B 2 41  ? -16.776 3.743   -7.136  0.50 43.06  ? 50  TRP   B CA  1 
ATOM   564  C  CA  B TRP   B 2 41  ? -16.786 3.752   -7.132  0.50 42.94  ? 50  TRP   B CA  1 
ATOM   565  C  C   . TRP   B 2 41  ? -15.851 4.948   -7.318  1.00 43.63  ? 50  TRP   B C   1 
ATOM   566  O  O   . TRP   B 2 41  ? -16.127 6.009   -6.773  1.00 44.09  ? 50  TRP   B O   1 
ATOM   567  C  CB  A TRP   B 2 41  ? -16.307 2.869   -5.953  0.50 42.82  ? 50  TRP   B CB  1 
ATOM   568  C  CB  B TRP   B 2 41  ? -16.361 2.900   -5.905  0.50 42.53  ? 50  TRP   B CB  1 
ATOM   569  C  CG  A TRP   B 2 41  ? -16.561 3.508   -4.623  0.50 43.10  ? 50  TRP   B CG  1 
ATOM   570  C  CG  B TRP   B 2 41  ? -16.202 3.697   -4.636  0.50 42.55  ? 50  TRP   B CG  1 
ATOM   571  C  CD1 A TRP   B 2 41  ? -17.698 3.417   -3.877  0.50 44.05  ? 50  TRP   B CD1 1 
ATOM   572  C  CD1 B TRP   B 2 41  ? -15.115 4.431   -4.260  0.50 43.24  ? 50  TRP   B CD1 1 
ATOM   573  C  CD2 A TRP   B 2 41  ? -15.694 4.415   -3.926  0.50 43.14  ? 50  TRP   B CD2 1 
ATOM   574  C  CD2 B TRP   B 2 41  ? -17.174 3.861   -3.594  0.50 42.54  ? 50  TRP   B CD2 1 
ATOM   575  N  NE1 A TRP   B 2 41  ? -17.581 4.187   -2.742  0.50 44.46  ? 50  TRP   B NE1 1 
ATOM   576  N  NE1 B TRP   B 2 41  ? -15.363 5.070   -3.068  0.50 43.43  ? 50  TRP   B NE1 1 
ATOM   577  C  CE2 A TRP   B 2 41  ? -16.365 4.822   -2.756  0.50 43.98  ? 50  TRP   B CE2 1 
ATOM   578  C  CE2 B TRP   B 2 41  ? -16.616 4.729   -2.631  0.50 43.15  ? 50  TRP   B CE2 1 
ATOM   579  C  CE3 A TRP   B 2 41  ? -14.406 4.907   -4.165  0.50 43.64  ? 50  TRP   B CE3 1 
ATOM   580  C  CE3 B TRP   B 2 41  ? -18.466 3.365   -3.383  0.50 42.96  ? 50  TRP   B CE3 1 
ATOM   581  C  CZ2 A TRP   B 2 41  ? -15.798 5.703   -1.841  0.50 44.48  ? 50  TRP   B CZ2 1 
ATOM   582  C  CZ2 B TRP   B 2 41  ? -17.301 5.102   -1.473  0.50 43.52  ? 50  TRP   B CZ2 1 
ATOM   583  C  CZ3 A TRP   B 2 41  ? -13.845 5.775   -3.252  0.50 44.49  ? 50  TRP   B CZ3 1 
ATOM   584  C  CZ3 B TRP   B 2 41  ? -19.140 3.735   -2.233  0.50 43.81  ? 50  TRP   B CZ3 1 
ATOM   585  C  CH2 A TRP   B 2 41  ? -14.530 6.147   -2.095  0.50 44.58  ? 50  TRP   B CH2 1 
ATOM   586  C  CH2 B TRP   B 2 41  ? -18.556 4.589   -1.292  0.50 43.69  ? 50  TRP   B CH2 1 
ATOM   587  N  N   . HIS   B 2 42  ? -14.744 4.786   -8.046  1.00 43.81  ? 51  HIS   B N   1 
ATOM   588  C  CA  . HIS   B 2 42  ? -13.787 5.881   -8.226  1.00 44.51  ? 51  HIS   B CA  1 
ATOM   589  C  C   . HIS   B 2 42  ? -14.323 7.068   -9.047  1.00 45.83  ? 51  HIS   B C   1 
ATOM   590  O  O   . HIS   B 2 42  ? -13.690 8.121   -9.079  1.00 46.09  ? 51  HIS   B O   1 
ATOM   591  C  CB  . HIS   B 2 42  ? -12.469 5.359   -8.800  1.00 44.64  ? 51  HIS   B CB  1 
ATOM   592  C  CG  . HIS   B 2 42  ? -12.497 5.106   -10.275 1.00 45.69  ? 51  HIS   B CG  1 
ATOM   593  N  ND1 . HIS   B 2 42  ? -12.814 3.861   -10.790 1.00 47.11  ? 51  HIS   B ND1 1 
ATOM   594  C  CD2 . HIS   B 2 42  ? -12.219 5.945   -11.297 1.00 46.19  ? 51  HIS   B CD2 1 
ATOM   595  C  CE1 . HIS   B 2 42  ? -12.742 3.991   -12.099 1.00 47.28  ? 51  HIS   B CE1 1 
ATOM   596  N  NE2 . HIS   B 2 42  ? -12.393 5.231   -12.449 1.00 47.20  ? 51  HIS   B NE2 1 
ATOM   597  N  N   . VAL   B 2 43  ? -15.469 6.893   -9.721  1.00 46.22  ? 52  VAL   B N   1 
ATOM   598  C  CA  . VAL   B 2 43  ? -16.082 7.939   -10.527 1.00 46.66  ? 52  VAL   B CA  1 
ATOM   599  C  C   . VAL   B 2 43  ? -16.859 8.914   -9.628  1.00 47.03  ? 52  VAL   B C   1 
ATOM   600  O  O   . VAL   B 2 43  ? -16.640 10.117  -9.692  1.00 47.29  ? 52  VAL   B O   1 
ATOM   601  C  CB  . VAL   B 2 43  ? -16.984 7.292   -11.602 1.00 47.45  ? 52  VAL   B CB  1 
ATOM   602  C  CG1 . VAL   B 2 43  ? -17.872 8.330   -12.292 1.00 47.89  ? 52  VAL   B CG1 1 
ATOM   603  C  CG2 . VAL   B 2 43  ? -16.150 6.506   -12.612 1.00 47.84  ? 52  VAL   B CG2 1 
ATOM   604  N  N   . THR   B 2 44  ? -17.718 8.390   -8.751  1.00 46.81  ? 53  THR   B N   1 
ATOM   605  C  CA  . THR   B 2 44  ? -18.543 9.226   -7.892  1.00 47.17  ? 53  THR   B CA  1 
ATOM   606  C  C   . THR   B 2 44  ? -18.012 9.397   -6.481  1.00 48.33  ? 53  THR   B C   1 
ATOM   607  O  O   . THR   B 2 44  ? -18.391 10.360  -5.812  1.00 48.91  ? 53  THR   B O   1 
ATOM   608  C  CB  . THR   B 2 44  ? -19.992 8.705   -7.853  1.00 47.55  ? 53  THR   B CB  1 
ATOM   609  O  OG1 . THR   B 2 44  ? -20.080 7.549   -7.018  1.00 47.99  ? 53  THR   B OG1 1 
ATOM   610  C  CG2 . THR   B 2 44  ? -20.544 8.375   -9.230  1.00 48.02  ? 53  THR   B CG2 1 
ATOM   611  N  N   . LYS   B 2 45  ? -17.190 8.455   -6.008  1.00 48.54  ? 54  LYS   B N   1 
ATOM   612  C  CA  . LYS   B 2 45  ? -16.689 8.399   -4.630  1.00 49.80  ? 54  LYS   B CA  1 
ATOM   613  C  C   . LYS   B 2 45  ? -17.826 8.172   -3.614  1.00 50.28  ? 54  LYS   B C   1 
ATOM   614  O  O   . LYS   B 2 45  ? -17.676 8.513   -2.442  1.00 50.41  ? 54  LYS   B O   1 
ATOM   615  C  CB  . LYS   B 2 45  ? -15.873 9.643   -4.253  1.00 52.19  ? 54  LYS   B CB  1 
ATOM   616  C  CG  . LYS   B 2 45  ? -14.699 9.889   -5.170  1.00 57.24  ? 54  LYS   B CG  1 
ATOM   617  C  CD  . LYS   B 2 45  ? -13.564 8.982   -4.826  1.00 63.41  ? 54  LYS   B CD  1 
ATOM   618  C  CE  . LYS   B 2 45  ? -12.302 9.448   -5.503  1.00 69.16  ? 54  LYS   B CE  1 
ATOM   619  N  NZ  . LYS   B 2 45  ? -12.359 9.245   -6.980  1.00 72.13  ? 54  LYS   B NZ  1 
ATOM   620  N  N   . GLY   B 2 46  ? -18.939 7.599   -4.071  1.00 50.52  ? 55  GLY   B N   1 
ATOM   621  C  CA  . GLY   B 2 46  ? -20.121 7.390   -3.254  1.00 51.49  ? 55  GLY   B CA  1 
ATOM   622  C  C   . GLY   B 2 46  ? -20.940 8.648   -3.034  1.00 52.71  ? 55  GLY   B C   1 
ATOM   623  O  O   . GLY   B 2 46  ? -21.812 8.664   -2.170  1.00 53.33  ? 55  GLY   B O   1 
ATOM   624  N  N   . ALA   B 2 47  ? -20.663 9.727   -3.779  1.00 53.14  ? 56  ALA   B N   1 
ATOM   625  C  CA  . ALA   B 2 47  ? -21.419 10.966  -3.656  1.00 53.89  ? 56  ALA   B CA  1 
ATOM   626  C  C   . ALA   B 2 47  ? -22.768 10.806  -4.345  1.00 54.53  ? 56  ALA   B C   1 
ATOM   627  O  O   . ALA   B 2 47  ? -22.878 10.038  -5.291  1.00 54.97  ? 56  ALA   B O   1 
ATOM   628  C  CB  . ALA   B 2 47  ? -20.654 12.109  -4.302  1.00 54.13  ? 56  ALA   B CB  1 
ATOM   629  N  N   . ALA   B 2 48  ? -23.782 11.542  -3.896  1.00 54.60  ? 57  ALA   B N   1 
ATOM   630  C  CA  . ALA   B 2 48  ? -25.100 11.495  -4.503  1.00 55.51  ? 57  ALA   B CA  1 
ATOM   631  C  C   . ALA   B 2 48  ? -25.067 12.102  -5.899  1.00 56.64  ? 57  ALA   B C   1 
ATOM   632  O  O   . ALA   B 2 48  ? -24.293 13.020  -6.168  1.00 56.92  ? 57  ALA   B O   1 
ATOM   633  C  CB  . ALA   B 2 48  ? -26.102 12.242  -3.639  1.00 55.70  ? 57  ALA   B CB  1 
ATOM   634  N  N   . LEU   B 2 49  ? -25.896 11.567  -6.797  1.00 57.19  ? 58  LEU   B N   1 
ATOM   635  C  CA  . LEU   B 2 49  ? -25.983 12.036  -8.173  1.00 58.01  ? 58  LEU   B CA  1 
ATOM   636  C  C   . LEU   B 2 49  ? -27.320 12.701  -8.433  1.00 59.11  ? 58  LEU   B C   1 
ATOM   637  O  O   . LEU   B 2 49  ? -28.314 12.384  -7.796  1.00 59.31  ? 58  LEU   B O   1 
ATOM   638  C  CB  . LEU   B 2 49  ? -25.799 10.868  -9.147  1.00 58.21  ? 58  LEU   B CB  1 
ATOM   639  C  CG  . LEU   B 2 49  ? -24.546 10.029  -8.969  1.00 59.32  ? 58  LEU   B CG  1 
ATOM   640  C  CD1 . LEU   B 2 49  ? -24.532 8.905   -9.952  1.00 59.80  ? 58  LEU   B CD1 1 
ATOM   641  C  CD2 . LEU   B 2 49  ? -23.291 10.863  -9.110  1.00 59.88  ? 58  LEU   B CD2 1 
ATOM   642  N  N   . ARG   B 2 50  ? -27.349 13.624  -9.376  1.00 59.95  ? 59  ARG   B N   1 
ATOM   643  C  CA  . ARG   B 2 50  ? -28.559 14.353  -9.725  1.00 61.09  ? 59  ARG   B CA  1 
ATOM   644  C  C   . ARG   B 2 50  ? -29.013 13.911  -11.122 1.00 61.95  ? 59  ARG   B C   1 
ATOM   645  O  O   . ARG   B 2 50  ? -28.176 13.678  -11.991 1.00 61.67  ? 59  ARG   B O   1 
ATOM   646  C  CB  . ARG   B 2 50  ? -28.251 15.859  -9.643  1.00 62.95  ? 59  ARG   B CB  1 
ATOM   647  C  CG  . ARG   B 2 50  ? -29.226 16.777  -10.353 1.00 67.65  ? 59  ARG   B CG  1 
ATOM   648  C  CD  . ARG   B 2 50  ? -28.935 18.247  -10.081 1.00 71.78  ? 59  ARG   B CD  1 
ATOM   649  N  NE  . ARG   B 2 50  ? -27.581 18.650  -10.474 1.00 75.56  ? 59  ARG   B NE  1 
ATOM   650  C  CZ  . ARG   B 2 50  ? -27.264 19.174  -11.657 1.00 78.70  ? 59  ARG   B CZ  1 
ATOM   651  N  NH1 . ARG   B 2 50  ? -28.196 19.336  -12.593 1.00 78.28  ? 59  ARG   B NH1 1 
ATOM   652  N  NH2 . ARG   B 2 50  ? -26.010 19.521  -11.921 1.00 79.28  ? 59  ARG   B NH2 1 
ATOM   653  N  N   . SER   B 2 51  ? -30.313 13.706  -11.316 1.00 62.99  ? 60  SER   B N   1 
ATOM   654  C  CA  . SER   B 2 51  ? -30.828 13.293  -12.624 1.00 64.75  ? 60  SER   B CA  1 
ATOM   655  C  C   . SER   B 2 51  ? -31.912 14.273  -13.006 1.00 66.62  ? 60  SER   B C   1 
ATOM   656  O  O   . SER   B 2 51  ? -33.096 14.028  -12.780 1.00 67.22  ? 60  SER   B O   1 
ATOM   657  C  CB  . SER   B 2 51  ? -31.380 11.876  -12.576 1.00 66.09  ? 60  SER   B CB  1 
ATOM   658  O  OG  . SER   B 2 51  ? -31.572 11.405  -13.897 1.00 68.49  ? 60  SER   B OG  1 
ATOM   659  N  N   . GLY   B 2 52  ? -31.489 15.418  -13.518 1.00 67.02  ? 61  GLY   B N   1 
ATOM   660  C  CA  . GLY   B 2 52  ? -32.404 16.496  -13.834 1.00 67.46  ? 61  GLY   B CA  1 
ATOM   661  C  C   . GLY   B 2 52  ? -32.824 17.130  -12.532 1.00 67.88  ? 61  GLY   B C   1 
ATOM   662  O  O   . GLY   B 2 52  ? -31.986 17.628  -11.775 1.00 68.17  ? 61  GLY   B O   1 
ATOM   663  N  N   . GLU   B 2 53  ? -34.112 17.043  -12.227 1.00 67.69  ? 62  GLU   B N   1 
ATOM   664  C  CA  . GLU   B 2 53  ? -34.639 17.565  -10.976 1.00 67.78  ? 62  GLU   B CA  1 
ATOM   665  C  C   . GLU   B 2 53  ? -34.497 16.547  -9.820  1.00 67.22  ? 62  GLU   B C   1 
ATOM   666  O  O   . GLU   B 2 53  ? -34.398 16.950  -8.660  1.00 67.71  ? 62  GLU   B O   1 
ATOM   667  C  CB  . GLU   B 2 53  ? -36.111 17.919  -11.174 1.00 70.92  ? 62  GLU   B CB  1 
ATOM   668  C  CG  . GLU   B 2 53  ? -36.622 19.016  -10.263 1.00 76.77  ? 62  GLU   B CG  1 
ATOM   669  C  CD  . GLU   B 2 53  ? -38.072 19.389  -10.516 1.00 84.31  ? 62  GLU   B CD  1 
ATOM   670  O  OE1 . GLU   B 2 53  ? -38.714 19.924  -9.582  1.00 86.22  ? 62  GLU   B OE1 1 
ATOM   671  O  OE2 . GLU   B 2 53  ? -38.569 19.141  -11.641 1.00 86.10  ? 62  GLU   B OE2 1 
ATOM   672  N  N   . GLY   B 2 54  ? -34.505 15.252  -10.144 1.00 66.11  ? 63  GLY   B N   1 
ATOM   673  C  CA  . GLY   B 2 54  ? -34.437 14.173  -9.162  1.00 65.53  ? 63  GLY   B CA  1 
ATOM   674  C  C   . GLY   B 2 54  ? -33.086 13.867  -8.545  1.00 64.40  ? 63  GLY   B C   1 
ATOM   675  O  O   . GLY   B 2 54  ? -32.042 14.257  -9.072  1.00 65.13  ? 63  GLY   B O   1 
ATOM   676  N  N   . ARG   B 2 55  ? -33.098 13.128  -7.432  1.00 62.44  ? 64  ARG   B N   1 
ATOM   677  C  CA  . ARG   B 2 55  ? -31.873 12.751  -6.727  1.00 61.27  ? 64  ARG   B CA  1 
ATOM   678  C  C   . ARG   B 2 55  ? -31.660 11.225  -6.632  1.00 58.75  ? 64  ARG   B C   1 
ATOM   679  O  O   . ARG   B 2 55  ? -32.564 10.489  -6.247  1.00 58.68  ? 64  ARG   B O   1 
ATOM   680  C  CB  . ARG   B 2 55  ? -31.875 13.360  -5.312  1.00 63.08  ? 64  ARG   B CB  1 
ATOM   681  C  CG  . ARG   B 2 55  ? -30.569 13.167  -4.549  1.00 67.29  ? 64  ARG   B CG  1 
ATOM   682  C  CD  . ARG   B 2 55  ? -30.730 13.573  -3.098  1.00 72.13  ? 64  ARG   B CD  1 
ATOM   683  N  NE  . ARG   B 2 55  ? -29.483 13.466  -2.333  1.00 76.38  ? 64  ARG   B NE  1 
ATOM   684  C  CZ  . ARG   B 2 55  ? -29.063 14.376  -1.456  1.00 79.55  ? 64  ARG   B CZ  1 
ATOM   685  N  NH1 . ARG   B 2 55  ? -29.766 15.486  -1.248  1.00 79.71  ? 64  ARG   B NH1 1 
ATOM   686  N  NH2 . ARG   B 2 55  ? -27.929 14.191  -0.789  1.00 79.13  ? 64  ARG   B NH2 1 
ATOM   687  N  N   . LEU   B 2 56  ? -30.447 10.769  -6.930  1.00 56.50  ? 65  LEU   B N   1 
ATOM   688  C  CA  . LEU   B 2 56  ? -30.067 9.367   -6.815  1.00 54.96  ? 65  LEU   B CA  1 
ATOM   689  C  C   . LEU   B 2 56  ? -29.122 9.248   -5.633  1.00 53.63  ? 65  LEU   B C   1 
ATOM   690  O  O   . LEU   B 2 56  ? -28.051 9.855   -5.635  1.00 53.54  ? 65  LEU   B O   1 
ATOM   691  C  CB  . LEU   B 2 56  ? -29.320 8.886   -8.067  1.00 54.87  ? 65  LEU   B CB  1 
ATOM   692  C  CG  . LEU   B 2 56  ? -29.905 9.221   -9.407  1.00 56.50  ? 65  LEU   B CG  1 
ATOM   693  C  CD1 . LEU   B 2 56  ? -28.911 8.949   -10.484 1.00 57.34  ? 65  LEU   B CD1 1 
ATOM   694  C  CD2 . LEU   B 2 56  ? -31.161 8.433   -9.669  1.00 57.34  ? 65  LEU   B CD2 1 
ATOM   695  N  N   . ASP   B 2 57  ? -29.494 8.461   -4.637  1.00 52.73  ? 66  ASP   B N   1 
ATOM   696  C  CA  . ASP   B 2 57  ? -28.643 8.263   -3.469  1.00 52.50  ? 66  ASP   B CA  1 
ATOM   697  C  C   . ASP   B 2 57  ? -27.932 6.913   -3.543  1.00 51.25  ? 66  ASP   B C   1 
ATOM   698  O  O   . ASP   B 2 57  ? -28.482 5.963   -4.103  1.00 51.67  ? 66  ASP   B O   1 
ATOM   699  C  CB  . ASP   B 2 57  ? -29.482 8.378   -2.205  1.00 55.69  ? 66  ASP   B CB  1 
ATOM   700  C  CG  . ASP   B 2 57  ? -30.055 9.763   -2.037  1.00 63.25  ? 66  ASP   B CG  1 
ATOM   701  O  OD1 . ASP   B 2 57  ? -29.265 10.706  -1.809  1.00 64.92  ? 66  ASP   B OD1 1 
ATOM   702  O  OD2 . ASP   B 2 57  ? -31.299 9.910   -2.139  1.00 66.54  ? 66  ASP   B OD2 1 
ATOM   703  N  N   . PRO   B 2 58  ? -26.683 6.812   -3.055  1.00 49.67  ? 67  PRO   B N   1 
ATOM   704  C  CA  . PRO   B 2 58  ? -25.990 5.515   -3.115  1.00 48.78  ? 67  PRO   B CA  1 
ATOM   705  C  C   . PRO   B 2 58  ? -26.689 4.474   -2.237  1.00 48.25  ? 67  PRO   B C   1 
ATOM   706  O  O   . PRO   B 2 58  ? -27.336 4.816   -1.243  1.00 48.83  ? 67  PRO   B O   1 
ATOM   707  C  CB  . PRO   B 2 58  ? -24.573 5.847   -2.642  1.00 49.37  ? 67  PRO   B CB  1 
ATOM   708  C  CG  . PRO   B 2 58  ? -24.737 7.067   -1.800  1.00 49.81  ? 67  PRO   B CG  1 
ATOM   709  C  CD  . PRO   B 2 58  ? -25.874 7.840   -2.366  1.00 48.56  ? 67  PRO   B CD  1 
ATOM   710  N  N   . TYR   B 2 59  ? -26.607 3.209   -2.623  1.00 46.91  ? 68  TYR   B N   1 
ATOM   711  C  CA  . TYR   B 2 59  ? -27.271 2.140   -1.884  1.00 45.88  ? 68  TYR   B CA  1 
ATOM   712  C  C   . TYR   B 2 59  ? -26.257 1.097   -1.442  1.00 44.97  ? 68  TYR   B C   1 
ATOM   713  O  O   . TYR   B 2 59  ? -26.323 0.602   -0.332  1.00 45.31  ? 68  TYR   B O   1 
ATOM   714  C  CB  . TYR   B 2 59  ? -28.383 1.536   -2.765  1.00 45.35  ? 68  TYR   B CB  1 
ATOM   715  C  CG  . TYR   B 2 59  ? -29.164 0.394   -2.152  1.00 45.44  ? 68  TYR   B CG  1 
ATOM   716  C  CD1 . TYR   B 2 59  ? -28.616 -0.881  -2.061  1.00 46.36  ? 68  TYR   B CD1 1 
ATOM   717  C  CD2 . TYR   B 2 59  ? -30.495 0.551   -1.801  1.00 45.78  ? 68  TYR   B CD2 1 
ATOM   718  C  CE1 . TYR   B 2 59  ? -29.338 -1.945  -1.535  1.00 47.06  ? 68  TYR   B CE1 1 
ATOM   719  C  CE2 . TYR   B 2 59  ? -31.241 -0.514  -1.312  1.00 46.80  ? 68  TYR   B CE2 1 
ATOM   720  C  CZ  . TYR   B 2 59  ? -30.657 -1.764  -1.180  1.00 47.83  ? 68  TYR   B CZ  1 
ATOM   721  O  OH  . TYR   B 2 59  ? -31.389 -2.814  -0.671  1.00 48.66  ? 68  TYR   B OH  1 
ATOM   722  N  N   . TRP   B 2 60  ? -25.345 0.739   -2.323  1.00 44.17  ? 69  TRP   B N   1 
ATOM   723  C  CA  . TRP   B 2 60  ? -24.303 -0.244  -2.052  1.00 43.59  ? 69  TRP   B CA  1 
ATOM   724  C  C   . TRP   B 2 60  ? -23.003 0.240   -2.706  1.00 42.45  ? 69  TRP   B C   1 
ATOM   725  O  O   . TRP   B 2 60  ? -23.030 0.833   -3.769  1.00 42.20  ? 69  TRP   B O   1 
ATOM   726  C  CB  . TRP   B 2 60  ? -24.710 -1.659  -2.557  1.00 43.56  ? 69  TRP   B CB  1 
ATOM   727  C  CG  . TRP   B 2 60  ? -23.563 -2.626  -2.542  1.00 43.91  ? 69  TRP   B CG  1 
ATOM   728  C  CD1 . TRP   B 2 60  ? -23.035 -3.251  -1.449  1.00 44.60  ? 69  TRP   B CD1 1 
ATOM   729  C  CD2 . TRP   B 2 60  ? -22.651 -2.874  -3.624  1.00 43.82  ? 69  TRP   B CD2 1 
ATOM   730  N  NE1 . TRP   B 2 60  ? -21.883 -3.920  -1.799  1.00 44.90  ? 69  TRP   B NE1 1 
ATOM   731  C  CE2 . TRP   B 2 60  ? -21.631 -3.712  -3.130  1.00 44.43  ? 69  TRP   B CE2 1 
ATOM   732  C  CE3 . TRP   B 2 60  ? -22.605 -2.472  -4.969  1.00 44.08  ? 69  TRP   B CE3 1 
ATOM   733  C  CZ2 . TRP   B 2 60  ? -20.584 -4.165  -3.936  1.00 44.90  ? 69  TRP   B CZ2 1 
ATOM   734  C  CZ3 . TRP   B 2 60  ? -21.585 -2.944  -5.769  1.00 44.70  ? 69  TRP   B CZ3 1 
ATOM   735  C  CH2 . TRP   B 2 60  ? -20.598 -3.793  -5.255  1.00 44.87  ? 69  TRP   B CH2 1 
ATOM   736  N  N   . GLY   B 2 61  ? -21.884 -0.011  -2.058  1.00 42.18  ? 70  GLY   B N   1 
ATOM   737  C  CA  . GLY   B 2 61  ? -20.576 0.374   -2.568  1.00 42.30  ? 70  GLY   B CA  1 
ATOM   738  C  C   . GLY   B 2 61  ? -19.466 -0.445  -1.947  1.00 41.96  ? 70  GLY   B C   1 
ATOM   739  O  O   . GLY   B 2 61  ? -19.615 -0.958  -0.836  1.00 42.21  ? 70  GLY   B O   1 
ATOM   740  N  N   . ASP   B 2 62  ? -18.360 -0.586  -2.661  1.00 41.31  ? 71  ASP   B N   1 
ATOM   741  C  CA  . ASP   B 2 62  ? -17.216 -1.359  -2.197  1.00 41.30  ? 71  ASP   B CA  1 
ATOM   742  C  C   . ASP   B 2 62  ? -15.984 -0.856  -2.969  1.00 40.73  ? 71  ASP   B C   1 
ATOM   743  O  O   . ASP   B 2 62  ? -15.946 -0.964  -4.187  1.00 40.37  ? 71  ASP   B O   1 
ATOM   744  C  CB  . ASP   B 2 62  ? -17.460 -2.852  -2.468  1.00 43.56  ? 71  ASP   B CB  1 
ATOM   745  C  CG  . ASP   B 2 62  ? -16.474 -3.786  -1.811  1.00 50.16  ? 71  ASP   B CG  1 
ATOM   746  O  OD1 . ASP   B 2 62  ? -15.297 -3.803  -2.232  1.00 51.03  ? 71  ASP   B OD1 1 
ATOM   747  O  OD2 . ASP   B 2 62  ? -16.883 -4.526  -0.897  1.00 54.50  ? 71  ASP   B OD2 1 
ATOM   748  N  N   . VAL   B 2 63  ? -15.012 -0.263  -2.254  1.00 40.19  ? 72  VAL   B N   1 
ATOM   749  C  CA  . VAL   B 2 63  ? -13.783 0.299   -2.809  1.00 39.64  ? 72  VAL   B CA  1 
ATOM   750  C  C   . VAL   B 2 63  ? -12.938 -0.788  -3.462  1.00 40.27  ? 72  VAL   B C   1 
ATOM   751  O  O   . VAL   B 2 63  ? -12.504 -0.595  -4.595  1.00 40.74  ? 72  VAL   B O   1 
ATOM   752  C  CB  . VAL   B 2 63  ? -13.020 1.134   -1.743  1.00 39.15  ? 72  VAL   B CB  1 
ATOM   753  C  CG1 . VAL   B 2 63  ? -11.563 1.357   -2.114  1.00 39.29  ? 72  VAL   B CG1 1 
ATOM   754  C  CG2 . VAL   B 2 63  ? -13.719 2.457   -1.489  1.00 38.86  ? 72  VAL   B CG2 1 
ATOM   755  N  N   . LYS   B 2 64  ? -12.789 -1.958  -2.824  1.00 40.32  ? 73  LYS   B N   1 
ATOM   756  C  CA  . LYS   B 2 64  ? -12.020 -3.057  -3.423  1.00 40.98  ? 73  LYS   B CA  1 
ATOM   757  C  C   . LYS   B 2 64  ? -12.606 -3.557  -4.752  1.00 42.19  ? 73  LYS   B C   1 
ATOM   758  O  O   . LYS   B 2 64  ? -11.866 -3.635  -5.734  1.00 42.66  ? 73  LYS   B O   1 
ATOM   759  C  CB  . LYS   B 2 64  ? -11.800 -4.210  -2.450  1.00 41.87  ? 73  LYS   B CB  1 
ATOM   760  C  CG  . LYS   B 2 64  ? -10.727 -5.161  -2.955  1.00 44.11  ? 73  LYS   B CG  1 
ATOM   761  C  CD  . LYS   B 2 64  ? -10.269 -6.120  -1.902  1.00 46.42  ? 73  LYS   B CD  1 
ATOM   762  C  CE  . LYS   B 2 64  ? -9.510  -7.254  -2.521  1.00 49.73  ? 73  LYS   B CE  1 
ATOM   763  N  NZ  . LYS   B 2 64  ? -9.250  -8.321  -1.523  1.00 52.56  ? 73  LYS   B NZ  1 
ATOM   764  N  N   . GLN   B 2 65  ? -13.926 -3.858  -4.813  1.00 42.37  ? 74  GLN   B N   1 
ATOM   765  C  CA  . GLN   B 2 65  ? -14.547 -4.242  -6.097  1.00 42.78  ? 74  GLN   B CA  1 
ATOM   766  C  C   . GLN   B 2 65  ? -14.584 -3.049  -7.077  1.00 42.95  ? 74  GLN   B C   1 
ATOM   767  O  O   . GLN   B 2 65  ? -14.686 -3.259  -8.281  1.00 43.34  ? 74  GLN   B O   1 
ATOM   768  C  CB  . GLN   B 2 65  ? -15.985 -4.744  -5.903  1.00 44.98  ? 74  GLN   B CB  1 
ATOM   769  C  CG  . GLN   B 2 65  ? -16.127 -6.042  -5.107  1.00 50.10  ? 74  GLN   B CG  1 
ATOM   770  C  CD  . GLN   B 2 65  ? -17.587 -6.463  -4.918  1.00 55.27  ? 74  GLN   B CD  1 
ATOM   771  O  OE1 . GLN   B 2 65  ? -18.425 -6.393  -5.843  1.00 56.52  ? 74  GLN   B OE1 1 
ATOM   772  N  NE2 . GLN   B 2 65  ? -17.916 -6.933  -3.712  1.00 55.98  ? 74  GLN   B NE2 1 
ATOM   773  N  N   . ASP   B 2 66  ? -14.506 -1.807  -6.548  1.00 42.71  ? 75  ASP   B N   1 
ATOM   774  C  CA  . ASP   B 2 66  ? -14.565 -0.511  -7.225  1.00 42.66  ? 75  ASP   B CA  1 
ATOM   775  C  C   . ASP   B 2 66  ? -15.877 -0.381  -7.962  1.00 42.26  ? 75  ASP   B C   1 
ATOM   776  O  O   . ASP   B 2 66  ? -15.905 -0.001  -9.121  1.00 42.24  ? 75  ASP   B O   1 
ATOM   777  C  CB  . ASP   B 2 66  ? -13.349 -0.248  -8.133  1.00 43.62  ? 75  ASP   B CB  1 
ATOM   778  C  CG  . ASP   B 2 66  ? -13.361 1.126   -8.769  1.00 46.56  ? 75  ASP   B CG  1 
ATOM   779  O  OD1 . ASP   B 2 66  ? -13.678 2.099   -8.064  1.00 48.24  ? 75  ASP   B OD1 1 
ATOM   780  O  OD2 . ASP   B 2 66  ? -13.060 1.223   -9.972  1.00 47.29  ? 75  ASP   B OD2 1 
ATOM   781  N  N   . LEU   B 2 67  ? -16.973 -0.704  -7.278  1.00 41.63  ? 76  LEU   B N   1 
ATOM   782  C  CA  . LEU   B 2 67  ? -18.317 -0.613  -7.834  1.00 41.15  ? 76  LEU   B CA  1 
ATOM   783  C  C   . LEU   B 2 67  ? -19.244 0.142   -6.874  1.00 40.94  ? 76  LEU   B C   1 
ATOM   784  O  O   . LEU   B 2 67  ? -18.964 0.214   -5.677  1.00 41.09  ? 76  LEU   B O   1 
ATOM   785  C  CB  . LEU   B 2 67  ? -18.870 -2.017  -8.101  1.00 41.05  ? 76  LEU   B CB  1 
ATOM   786  C  CG  . LEU   B 2 67  ? -18.173 -2.833  -9.185  1.00 41.88  ? 76  LEU   B CG  1 
ATOM   787  C  CD1 . LEU   B 2 67  ? -18.741 -4.210  -9.249  1.00 41.85  ? 76  LEU   B CD1 1 
ATOM   788  C  CD2 . LEU   B 2 67  ? -18.281 -2.152  -10.570 1.00 42.49  ? 76  LEU   B CD2 1 
ATOM   789  N  N   . VAL   B 2 68  ? -20.346 0.714   -7.398  1.00 40.51  ? 77  VAL   B N   1 
ATOM   790  C  CA  . VAL   B 2 68  ? -21.338 1.455   -6.605  1.00 40.13  ? 77  VAL   B CA  1 
ATOM   791  C  C   . VAL   B 2 68  ? -22.713 1.429   -7.292  1.00 40.48  ? 77  VAL   B C   1 
ATOM   792  O  O   . VAL   B 2 68  ? -22.798 1.597   -8.498  1.00 40.20  ? 77  VAL   B O   1 
ATOM   793  C  CB  . VAL   B 2 68  ? -20.872 2.889   -6.218  1.00 40.07  ? 77  VAL   B CB  1 
ATOM   794  C  CG1 . VAL   B 2 68  ? -20.656 3.770   -7.437  1.00 40.39  ? 77  VAL   B CG1 1 
ATOM   795  C  CG2 . VAL   B 2 68  ? -21.829 3.551   -5.241  1.00 40.58  ? 77  VAL   B CG2 1 
ATOM   796  N  N   . SER   B 2 69  ? -23.783 1.141   -6.537  1.00 41.11  ? 78  SER   B N   1 
ATOM   797  C  CA  . SER   B 2 69  ? -25.140 1.132   -7.092  1.00 41.71  ? 78  SER   B CA  1 
ATOM   798  C  C   . SER   B 2 69  ? -25.999 2.224   -6.427  1.00 42.37  ? 78  SER   B C   1 
ATOM   799  O  O   . SER   B 2 69  ? -25.797 2.532   -5.259  1.00 42.21  ? 78  SER   B O   1 
ATOM   800  C  CB  . SER   B 2 69  ? -25.786 -0.244  -6.963  1.00 42.04  ? 78  SER   B CB  1 
ATOM   801  O  OG  . SER   B 2 69  ? -26.254 -0.472  -5.647  1.00 43.24  ? 78  SER   B OG  1 
ATOM   802  N  N   . TYR   B 2 70  ? -26.922 2.836   -7.191  1.00 43.03  ? 79  TYR   B N   1 
ATOM   803  C  CA  . TYR   B 2 70  ? -27.803 3.922   -6.733  1.00 43.79  ? 79  TYR   B CA  1 
ATOM   804  C  C   . TYR   B 2 70  ? -29.255 3.467   -6.852  1.00 44.47  ? 79  TYR   B C   1 
ATOM   805  O  O   . TYR   B 2 70  ? -29.601 2.825   -7.842  1.00 44.57  ? 79  TYR   B O   1 
ATOM   806  C  CB  . TYR   B 2 70  ? -27.581 5.196   -7.598  1.00 43.58  ? 79  TYR   B CB  1 
ATOM   807  C  CG  . TYR   B 2 70  ? -26.268 5.893   -7.311  1.00 44.22  ? 79  TYR   B CG  1 
ATOM   808  C  CD1 . TYR   B 2 70  ? -25.060 5.339   -7.719  1.00 45.04  ? 79  TYR   B CD1 1 
ATOM   809  C  CD2 . TYR   B 2 70  ? -26.228 7.065   -6.570  1.00 45.20  ? 79  TYR   B CD2 1 
ATOM   810  C  CE1 . TYR   B 2 70  ? -23.845 5.925   -7.382  1.00 45.80  ? 79  TYR   B CE1 1 
ATOM   811  C  CE2 . TYR   B 2 70  ? -25.021 7.664   -6.231  1.00 45.93  ? 79  TYR   B CE2 1 
ATOM   812  C  CZ  . TYR   B 2 70  ? -23.830 7.100   -6.656  1.00 46.70  ? 79  TYR   B CZ  1 
ATOM   813  O  OH  . TYR   B 2 70  ? -22.637 7.701   -6.348  1.00 47.75  ? 79  TYR   B OH  1 
ATOM   814  N  N   . CYS   B 2 71  ? -30.094 3.787   -5.845  1.00 44.66  ? 80  CYS   B N   1 
ATOM   815  C  CA  . CYS   B 2 71  ? -31.543 3.490   -5.795  1.00 45.46  ? 80  CYS   B CA  1 
ATOM   816  C  C   . CYS   B 2 71  ? -31.889 2.031   -5.449  1.00 44.76  ? 80  CYS   B C   1 
ATOM   817  O  O   . CYS   B 2 71  ? -33.049 1.735   -5.132  1.00 45.04  ? 80  CYS   B O   1 
ATOM   818  C  CB  . CYS   B 2 71  ? -32.265 3.934   -7.064  1.00 47.50  ? 80  CYS   B CB  1 
ATOM   819  S  SG  . CYS   B 2 71  ? -32.027 5.680   -7.487  1.00 54.49  ? 80  CYS   B SG  1 
ATOM   820  N  N   . GLY   B 2 72  ? -30.913 1.141   -5.519  1.00 43.41  ? 81  GLY   B N   1 
ATOM   821  C  CA  . GLY   B 2 72  ? -31.158 -0.254  -5.189  1.00 42.73  ? 81  GLY   B CA  1 
ATOM   822  C  C   . GLY   B 2 72  ? -29.920 -1.099  -5.253  1.00 41.89  ? 81  GLY   B C   1 
ATOM   823  O  O   . GLY   B 2 72  ? -28.824 -0.599  -5.521  1.00 41.48  ? 81  GLY   B O   1 
ATOM   824  N  N   . PRO   B 2 73  ? -30.088 -2.395  -4.954  1.00 41.47  ? 82  PRO   B N   1 
ATOM   825  C  CA  . PRO   B 2 73  ? -28.935 -3.312  -5.008  1.00 41.47  ? 82  PRO   B CA  1 
ATOM   826  C  C   . PRO   B 2 73  ? -28.440 -3.573  -6.432  1.00 42.07  ? 82  PRO   B C   1 
ATOM   827  O  O   . PRO   B 2 73  ? -29.210 -3.403  -7.383  1.00 42.37  ? 82  PRO   B O   1 
ATOM   828  C  CB  . PRO   B 2 73  ? -29.475 -4.599  -4.375  1.00 41.79  ? 82  PRO   B CB  1 
ATOM   829  C  CG  . PRO   B 2 73  ? -30.942 -4.531  -4.546  1.00 41.96  ? 82  PRO   B CG  1 
ATOM   830  C  CD  . PRO   B 2 73  ? -31.336 -3.086  -4.573  1.00 40.54  ? 82  PRO   B CD  1 
ATOM   831  N  N   . TRP   B 2 74  ? -27.166 -4.027  -6.582  1.00 41.89  ? 83  TRP   B N   1 
ATOM   832  C  CA  . TRP   B 2 74  ? -26.561 -4.358  -7.882  1.00 41.84  ? 83  TRP   B CA  1 
ATOM   833  C  C   . TRP   B 2 74  ? -27.449 -5.353  -8.646  1.00 43.83  ? 83  TRP   B C   1 
ATOM   834  O  O   . TRP   B 2 74  ? -27.794 -6.402  -8.103  1.00 44.12  ? 83  TRP   B O   1 
ATOM   835  C  CB  . TRP   B 2 74  ? -25.131 -4.921  -7.699  1.00 40.54  ? 83  TRP   B CB  1 
ATOM   836  C  CG  . TRP   B 2 74  ? -24.337 -5.012  -8.971  1.00 39.28  ? 83  TRP   B CG  1 
ATOM   837  C  CD1 . TRP   B 2 74  ? -24.267 -6.075  -9.816  1.00 39.50  ? 83  TRP   B CD1 1 
ATOM   838  C  CD2 . TRP   B 2 74  ? -23.510 -3.986  -9.547  1.00 38.59  ? 83  TRP   B CD2 1 
ATOM   839  N  NE1 . TRP   B 2 74  ? -23.468 -5.772  -10.896 1.00 39.57  ? 83  TRP   B NE1 1 
ATOM   840  C  CE2 . TRP   B 2 74  ? -23.004 -4.490  -10.763 1.00 39.10  ? 83  TRP   B CE2 1 
ATOM   841  C  CE3 . TRP   B 2 74  ? -23.165 -2.680  -9.159  1.00 38.46  ? 83  TRP   B CE3 1 
ATOM   842  C  CZ2 . TRP   B 2 74  ? -22.187 -3.731  -11.605 1.00 39.50  ? 83  TRP   B CZ2 1 
ATOM   843  C  CZ3 . TRP   B 2 74  ? -22.359 -1.930  -9.992  1.00 38.97  ? 83  TRP   B CZ3 1 
ATOM   844  C  CH2 . TRP   B 2 74  ? -21.881 -2.453  -11.201 1.00 39.36  ? 83  TRP   B CH2 1 
ATOM   845  N  N   . LYS   B 2 75  ? -27.887 -4.977  -9.872  1.00 44.91  ? 84  LYS   B N   1 
ATOM   846  C  CA  . LYS   B 2 75  ? -28.784 -5.782  -10.710 1.00 45.89  ? 84  LYS   B CA  1 
ATOM   847  C  C   . LYS   B 2 75  ? -28.078 -6.548  -11.828 1.00 47.59  ? 84  LYS   B C   1 
ATOM   848  O  O   . LYS   B 2 75  ? -28.697 -7.421  -12.429 1.00 48.29  ? 84  LYS   B O   1 
ATOM   849  C  CB  . LYS   B 2 75  ? -29.863 -4.903  -11.363 1.00 46.59  ? 84  LYS   B CB  1 
ATOM   850  C  CG  . LYS   B 2 75  ? -30.676 -4.070  -10.413 1.00 49.54  ? 84  LYS   B CG  1 
ATOM   851  C  CD  . LYS   B 2 75  ? -31.664 -4.894  -9.636  1.00 52.95  ? 84  LYS   B CD  1 
ATOM   852  C  CE  . LYS   B 2 75  ? -32.806 -4.026  -9.192  1.00 56.31  ? 84  LYS   B CE  1 
ATOM   853  N  NZ  . LYS   B 2 75  ? -33.394 -4.516  -7.932  1.00 59.20  ? 84  LYS   B NZ  1 
ATOM   854  N  N   . LEU   B 2 76  ? -26.839 -6.190  -12.167 1.00 48.15  ? 85  LEU   B N   1 
ATOM   855  C  CA  . LEU   B 2 76  ? -26.137 -6.826  -13.283 1.00 49.14  ? 85  LEU   B CA  1 
ATOM   856  C  C   . LEU   B 2 76  ? -25.488 -8.144  -12.855 1.00 50.68  ? 85  LEU   B C   1 
ATOM   857  O  O   . LEU   B 2 76  ? -24.673 -8.163  -11.943 1.00 50.54  ? 85  LEU   B O   1 
ATOM   858  C  CB  . LEU   B 2 76  ? -25.123 -5.864  -13.923 1.00 48.85  ? 85  LEU   B CB  1 
ATOM   859  C  CG  . LEU   B 2 76  ? -25.595 -4.425  -14.145 1.00 49.87  ? 85  LEU   B CG  1 
ATOM   860  C  CD1 . LEU   B 2 76  ? -24.490 -3.568  -14.702 1.00 50.20  ? 85  LEU   B CD1 1 
ATOM   861  C  CD2 . LEU   B 2 76  ? -26.783 -4.369  -15.053 1.00 50.41  ? 85  LEU   B CD2 1 
ATOM   862  N  N   . ASP   B 2 77  ? -25.846 -9.243  -13.520 1.00 52.03  ? 86  ASP   B N   1 
ATOM   863  C  CA  . ASP   B 2 77  ? -25.354 -10.565 -13.136 1.00 54.02  ? 86  ASP   B CA  1 
ATOM   864  C  C   . ASP   B 2 77  ? -24.779 -11.417 -14.278 1.00 54.73  ? 86  ASP   B C   1 
ATOM   865  O  O   . ASP   B 2 77  ? -24.399 -12.557 -14.024 1.00 55.28  ? 86  ASP   B O   1 
ATOM   866  C  CB  . ASP   B 2 77  ? -26.458 -11.358 -12.391 1.00 57.12  ? 86  ASP   B CB  1 
ATOM   867  C  CG  . ASP   B 2 77  ? -27.779 -11.496 -13.150 1.00 64.21  ? 86  ASP   B CG  1 
ATOM   868  O  OD1 . ASP   B 2 77  ? -27.921 -10.867 -14.233 1.00 65.71  ? 86  ASP   B OD1 1 
ATOM   869  O  OD2 . ASP   B 2 77  ? -28.675 -12.222 -12.660 1.00 66.87  ? 86  ASP   B OD2 1 
ATOM   870  N  N   . ALA   B 2 78  ? -24.708 -10.896 -15.506 1.00 54.63  ? 87  ALA   B N   1 
ATOM   871  C  CA  . ALA   B 2 78  ? -24.171 -11.666 -16.635 1.00 54.99  ? 87  ALA   B CA  1 
ATOM   872  C  C   . ALA   B 2 78  ? -22.652 -11.795 -16.543 1.00 55.44  ? 87  ALA   B C   1 
ATOM   873  O  O   . ALA   B 2 78  ? -21.986 -10.911 -16.006 1.00 55.27  ? 87  ALA   B O   1 
ATOM   874  C  CB  . ALA   B 2 78  ? -24.569 -11.021 -17.962 1.00 54.79  ? 87  ALA   B CB  1 
ATOM   875  N  N   . ALA   B 2 79  ? -22.103 -12.888 -17.075 1.00 55.90  ? 88  ALA   B N   1 
ATOM   876  C  CA  . ALA   B 2 79  ? -20.666 -13.111 -17.027 1.00 56.74  ? 88  ALA   B CA  1 
ATOM   877  C  C   . ALA   B 2 79  ? -20.073 -13.496 -18.377 1.00 57.50  ? 88  ALA   B C   1 
ATOM   878  O  O   . ALA   B 2 79  ? -20.762 -14.108 -19.188 1.00 58.28  ? 88  ALA   B O   1 
ATOM   879  C  CB  . ALA   B 2 79  ? -20.360 -14.188 -16.010 1.00 57.30  ? 88  ALA   B CB  1 
ATOM   880  N  N   . TRP   B 2 80  ? -18.793 -13.144 -18.620 1.00 57.28  ? 89  TRP   B N   1 
ATOM   881  C  CA  . TRP   B 2 80  ? -18.081 -13.513 -19.845 1.00 57.74  ? 89  TRP   B CA  1 
ATOM   882  C  C   . TRP   B 2 80  ? -17.942 -15.034 -19.871 1.00 58.30  ? 89  TRP   B C   1 
ATOM   883  O  O   . TRP   B 2 80  ? -17.623 -15.625 -18.843 1.00 58.00  ? 89  TRP   B O   1 
ATOM   884  C  CB  . TRP   B 2 80  ? -16.682 -12.862 -19.885 1.00 57.56  ? 89  TRP   B CB  1 
ATOM   885  C  CG  . TRP   B 2 80  ? -15.858 -13.216 -21.095 1.00 57.60  ? 89  TRP   B CG  1 
ATOM   886  C  CD1 . TRP   B 2 80  ? -16.259 -13.191 -22.399 1.00 58.36  ? 89  TRP   B CD1 1 
ATOM   887  C  CD2 . TRP   B 2 80  ? -14.463 -13.547 -21.112 1.00 57.57  ? 89  TRP   B CD2 1 
ATOM   888  N  NE1 . TRP   B 2 80  ? -15.212 -13.532 -23.225 1.00 58.63  ? 89  TRP   B NE1 1 
ATOM   889  C  CE2 . TRP   B 2 80  ? -14.094 -13.751 -22.459 1.00 58.32  ? 89  TRP   B CE2 1 
ATOM   890  C  CE3 . TRP   B 2 80  ? -13.495 -13.732 -20.117 1.00 57.96  ? 89  TRP   B CE3 1 
ATOM   891  C  CZ2 . TRP   B 2 80  ? -12.797 -14.112 -22.832 1.00 58.59  ? 89  TRP   B CZ2 1 
ATOM   892  C  CZ3 . TRP   B 2 80  ? -12.217 -14.103 -20.491 1.00 58.60  ? 89  TRP   B CZ3 1 
ATOM   893  C  CH2 . TRP   B 2 80  ? -11.881 -14.292 -21.833 1.00 58.50  ? 89  TRP   B CH2 1 
ATOM   894  N  N   . ASP   B 2 81  ? -18.231 -15.671 -21.014 1.00 59.08  ? 90  ASP   B N   1 
ATOM   895  C  CA  . ASP   B 2 81  ? -18.142 -17.130 -21.106 1.00 60.48  ? 90  ASP   B CA  1 
ATOM   896  C  C   . ASP   B 2 81  ? -16.708 -17.679 -21.184 1.00 61.75  ? 90  ASP   B C   1 
ATOM   897  O  O   . ASP   B 2 81  ? -16.522 -18.893 -21.120 1.00 62.03  ? 90  ASP   B O   1 
ATOM   898  C  CB  . ASP   B 2 81  ? -18.992 -17.683 -22.263 1.00 61.81  ? 90  ASP   B CB  1 
ATOM   899  C  CG  . ASP   B 2 81  ? -18.634 -17.159 -23.637 1.00 65.58  ? 90  ASP   B CG  1 
ATOM   900  O  OD1 . ASP   B 2 81  ? -17.602 -16.470 -23.759 1.00 67.08  ? 90  ASP   B OD1 1 
ATOM   901  O  OD2 . ASP   B 2 81  ? -19.393 -17.433 -24.596 1.00 65.98  ? 90  ASP   B OD2 1 
ATOM   902  N  N   . GLY   B 2 82  ? -15.725 -16.795 -21.322 1.00 62.11  ? 91  GLY   B N   1 
ATOM   903  C  CA  . GLY   B 2 82  ? -14.325 -17.173 -21.426 1.00 62.84  ? 91  GLY   B CA  1 
ATOM   904  C  C   . GLY   B 2 82  ? -13.869 -17.423 -22.848 1.00 63.85  ? 91  GLY   B C   1 
ATOM   905  O  O   . GLY   B 2 82  ? -12.668 -17.499 -23.103 1.00 64.02  ? 91  GLY   B O   1 
ATOM   906  N  N   . LEU   B 2 83  ? -14.811 -17.521 -23.799 1.00 64.43  ? 92  LEU   B N   1 
ATOM   907  C  CA  . LEU   B 2 83  ? -14.466 -17.822 -25.176 1.00 65.53  ? 92  LEU   B CA  1 
ATOM   908  C  C   . LEU   B 2 83  ? -14.831 -16.795 -26.196 1.00 66.26  ? 92  LEU   B C   1 
ATOM   909  O  O   . LEU   B 2 83  ? -14.154 -16.692 -27.217 1.00 66.77  ? 92  LEU   B O   1 
ATOM   910  C  CB  . LEU   B 2 83  ? -15.103 -19.148 -25.596 1.00 66.00  ? 92  LEU   B CB  1 
ATOM   911  C  CG  . LEU   B 2 83  ? -14.703 -20.396 -24.834 1.00 68.00  ? 92  LEU   B CG  1 
ATOM   912  C  CD1 . LEU   B 2 83  ? -15.245 -21.612 -25.537 1.00 68.85  ? 92  LEU   B CD1 1 
ATOM   913  C  CD2 . LEU   B 2 83  ? -13.194 -20.530 -24.726 1.00 68.70  ? 92  LEU   B CD2 1 
ATOM   914  N  N   . SER   B 2 84  ? -15.950 -16.119 -25.998 1.00 66.34  ? 93  SER   B N   1 
ATOM   915  C  CA  . SER   B 2 84  ? -16.474 -15.192 -26.983 1.00 66.86  ? 93  SER   B CA  1 
ATOM   916  C  C   . SER   B 2 84  ? -15.882 -13.807 -26.950 1.00 66.68  ? 93  SER   B C   1 
ATOM   917  O  O   . SER   B 2 84  ? -15.412 -13.327 -25.904 1.00 66.97  ? 93  SER   B O   1 
ATOM   918  C  CB  . SER   B 2 84  ? -17.988 -15.071 -26.830 1.00 68.85  ? 93  SER   B CB  1 
ATOM   919  O  OG  . SER   B 2 84  ? -18.611 -16.341 -26.800 1.00 71.78  ? 93  SER   B OG  1 
ATOM   920  N  N   . GLU   B 2 85  ? -15.959 -13.145 -28.112 1.00 65.74  ? 94  GLU   B N   1 
ATOM   921  C  CA  . GLU   B 2 85  ? -15.605 -11.749 -28.237 1.00 65.37  ? 94  GLU   B CA  1 
ATOM   922  C  C   . GLU   B 2 85  ? -16.755 -10.971 -27.579 1.00 64.11  ? 94  GLU   B C   1 
ATOM   923  O  O   . GLU   B 2 85  ? -17.909 -11.417 -27.537 1.00 64.43  ? 94  GLU   B O   1 
ATOM   924  C  CB  . GLU   B 2 85  ? -15.451 -11.331 -29.721 1.00 67.98  ? 94  GLU   B CB  1 
ATOM   925  C  CG  . GLU   B 2 85  ? -14.082 -11.631 -30.316 1.00 73.17  ? 94  GLU   B CG  1 
ATOM   926  C  CD  . GLU   B 2 85  ? -13.771 -10.891 -31.603 1.00 79.56  ? 94  GLU   B CD  1 
ATOM   927  O  OE1 . GLU   B 2 85  ? -14.728 -10.446 -32.274 1.00 80.88  ? 94  GLU   B OE1 1 
ATOM   928  O  OE2 . GLU   B 2 85  ? -12.574 -10.747 -31.942 1.00 81.57  ? 94  GLU   B OE2 1 
ATOM   929  N  N   . VAL   B 2 86  ? -16.416 -9.834  -27.008 1.00 62.33  ? 95  VAL   B N   1 
ATOM   930  C  CA  . VAL   B 2 86  ? -17.365 -8.972  -26.320 1.00 60.60  ? 95  VAL   B CA  1 
ATOM   931  C  C   . VAL   B 2 86  ? -17.352 -7.585  -26.995 1.00 59.50  ? 95  VAL   B C   1 
ATOM   932  O  O   . VAL   B 2 86  ? -16.537 -7.331  -27.892 1.00 59.53  ? 95  VAL   B O   1 
ATOM   933  C  CB  . VAL   B 2 86  ? -16.990 -8.879  -24.814 1.00 60.22  ? 95  VAL   B CB  1 
ATOM   934  C  CG1 . VAL   B 2 86  ? -16.824 -10.262 -24.189 1.00 60.17  ? 95  VAL   B CG1 1 
ATOM   935  C  CG2 . VAL   B 2 86  ? -15.738 -8.034  -24.627 1.00 60.51  ? 95  VAL   B CG2 1 
ATOM   936  N  N   . GLN   B 2 87  ? -18.257 -6.687  -26.570 1.00 58.24  ? 96  GLN   B N   1 
ATOM   937  C  CA  . GLN   B 2 87  ? -18.281 -5.332  -27.087 1.00 57.28  ? 96  GLN   B CA  1 
ATOM   938  C  C   . GLN   B 2 87  ? -18.195 -4.323  -25.946 1.00 55.74  ? 96  GLN   B C   1 
ATOM   939  O  O   . GLN   B 2 87  ? -18.954 -4.413  -24.999 1.00 55.57  ? 96  GLN   B O   1 
ATOM   940  C  CB  . GLN   B 2 87  ? -19.524 -5.081  -27.964 1.00 58.17  ? 96  GLN   B CB  1 
ATOM   941  C  CG  . GLN   B 2 87  ? -19.142 -4.716  -29.387 1.00 61.17  ? 96  GLN   B CG  1 
ATOM   942  C  CD  . GLN   B 2 87  ? -20.274 -4.878  -30.368 1.00 64.85  ? 96  GLN   B CD  1 
ATOM   943  O  OE1 . GLN   B 2 87  ? -21.423 -4.503  -30.112 1.00 65.99  ? 96  GLN   B OE1 1 
ATOM   944  N  NE2 . GLN   B 2 87  ? -19.966 -5.439  -31.521 1.00 64.75  ? 96  GLN   B NE2 1 
ATOM   945  N  N   . LEU   B 2 88  ? -17.260 -3.385  -26.024 1.00 54.57  ? 97  LEU   B N   1 
ATOM   946  C  CA  . LEU   B 2 88  ? -17.170 -2.307  -25.060 1.00 54.07  ? 97  LEU   B CA  1 
ATOM   947  C  C   . LEU   B 2 88  ? -18.037 -1.173  -25.624 1.00 54.56  ? 97  LEU   B C   1 
ATOM   948  O  O   . LEU   B 2 88  ? -17.745 -0.653  -26.702 1.00 54.85  ? 97  LEU   B O   1 
ATOM   949  C  CB  . LEU   B 2 88  ? -15.714 -1.829  -24.885 1.00 53.42  ? 97  LEU   B CB  1 
ATOM   950  C  CG  . LEU   B 2 88  ? -15.543 -0.520  -24.117 1.00 53.94  ? 97  LEU   B CG  1 
ATOM   951  C  CD1 . LEU   B 2 88  ? -16.070 -0.637  -22.697 1.00 54.08  ? 97  LEU   B CD1 1 
ATOM   952  C  CD2 . LEU   B 2 88  ? -14.125 -0.013  -24.182 1.00 54.12  ? 97  LEU   B CD2 1 
ATOM   953  N  N   . LEU   B 2 89  ? -19.101 -0.805  -24.916 1.00 54.37  ? 98  LEU   B N   1 
ATOM   954  C  CA  . LEU   B 2 89  ? -19.921 0.317   -25.334 1.00 54.57  ? 98  LEU   B CA  1 
ATOM   955  C  C   . LEU   B 2 89  ? -19.216 1.507   -24.721 1.00 54.83  ? 98  LEU   B C   1 
ATOM   956  O  O   . LEU   B 2 89  ? -19.532 1.905   -23.596 1.00 54.88  ? 98  LEU   B O   1 
ATOM   957  C  CB  . LEU   B 2 89  ? -21.354 0.171   -24.792 1.00 54.66  ? 98  LEU   B CB  1 
ATOM   958  C  CG  . LEU   B 2 89  ? -22.429 1.233   -25.135 1.00 55.42  ? 98  LEU   B CG  1 
ATOM   959  C  CD1 . LEU   B 2 89  ? -22.184 1.938   -26.453 1.00 56.42  ? 98  LEU   B CD1 1 
ATOM   960  C  CD2 . LEU   B 2 89  ? -23.784 0.610   -25.159 1.00 55.57  ? 98  LEU   B CD2 1 
ATOM   961  N  N   . ALA   B 2 90  ? -18.180 2.001   -25.406 1.00 54.64  ? 99  ALA   B N   1 
ATOM   962  C  CA  . ALA   B 2 90  ? -17.399 3.110   -24.886 1.00 55.26  ? 99  ALA   B CA  1 
ATOM   963  C  C   . ALA   B 2 90  ? -18.151 4.413   -25.045 1.00 56.28  ? 99  ALA   B C   1 
ATOM   964  O  O   . ALA   B 2 90  ? -18.711 4.675   -26.106 1.00 56.66  ? 99  ALA   B O   1 
ATOM   965  C  CB  . ALA   B 2 90  ? -16.065 3.194   -25.599 1.00 55.12  ? 99  ALA   B CB  1 
ATOM   966  N  N   . VAL   B 2 91  ? -18.195 5.224   -23.984 1.00 56.37  ? 100 VAL   B N   1 
ATOM   967  C  CA  . VAL   B 2 91  ? -18.844 6.529   -24.038 1.00 56.73  ? 100 VAL   B CA  1 
ATOM   968  C  C   . VAL   B 2 91  ? -17.776 7.561   -23.642 1.00 57.74  ? 100 VAL   B C   1 
ATOM   969  O  O   . VAL   B 2 91  ? -17.594 7.878   -22.460 1.00 58.04  ? 100 VAL   B O   1 
ATOM   970  C  CB  . VAL   B 2 91  ? -20.093 6.586   -23.139 1.00 56.49  ? 100 VAL   B CB  1 
ATOM   971  C  CG1 . VAL   B 2 91  ? -20.755 7.950   -23.223 1.00 56.96  ? 100 VAL   B CG1 1 
ATOM   972  C  CG2 . VAL   B 2 91  ? -21.075 5.477   -23.494 1.00 56.35  ? 100 VAL   B CG2 1 
ATOM   973  N  N   . PRO   B 2 92  ? -17.005 8.044   -24.627 1.00 57.76  ? 101 PRO   B N   1 
ATOM   974  C  CA  . PRO   B 2 92  ? -15.891 8.943   -24.306 1.00 58.11  ? 101 PRO   B CA  1 
ATOM   975  C  C   . PRO   B 2 92  ? -16.288 10.399  -24.081 1.00 59.05  ? 101 PRO   B C   1 
ATOM   976  O  O   . PRO   B 2 92  ? -17.285 10.867  -24.631 1.00 59.02  ? 101 PRO   B O   1 
ATOM   977  C  CB  . PRO   B 2 92  ? -14.931 8.760   -25.494 1.00 58.63  ? 101 PRO   B CB  1 
ATOM   978  C  CG  . PRO   B 2 92  ? -15.573 7.721   -26.396 1.00 59.09  ? 101 PRO   B CG  1 
ATOM   979  C  CD  . PRO   B 2 92  ? -17.029 7.719   -26.060 1.00 57.32  ? 101 PRO   B CD  1 
ATOM   980  N  N   . PRO   B 2 93  ? -15.513 11.129  -23.258 1.00 59.75  ? 102 PRO   B N   1 
ATOM   981  C  CA  . PRO   B 2 93  ? -15.853 12.537  -22.991 1.00 60.46  ? 102 PRO   B CA  1 
ATOM   982  C  C   . PRO   B 2 93  ? -15.950 13.384  -24.253 1.00 61.88  ? 102 PRO   B C   1 
ATOM   983  O  O   . PRO   B 2 93  ? -15.015 13.398  -25.052 1.00 62.34  ? 102 PRO   B O   1 
ATOM   984  C  CB  . PRO   B 2 93  ? -14.710 13.022  -22.090 1.00 60.92  ? 102 PRO   B CB  1 
ATOM   985  C  CG  . PRO   B 2 93  ? -14.120 11.781  -21.498 1.00 61.23  ? 102 PRO   B CG  1 
ATOM   986  C  CD  . PRO   B 2 93  ? -14.318 10.693  -22.503 1.00 59.38  ? 102 PRO   B CD  1 
ATOM   987  N  N   . GLY   B 2 94  ? -17.099 14.041  -24.438 1.00 62.23  ? 103 GLY   B N   1 
ATOM   988  C  CA  . GLY   B 2 94  ? -17.378 14.897  -25.590 1.00 62.78  ? 103 GLY   B CA  1 
ATOM   989  C  C   . GLY   B 2 94  ? -17.560 14.182  -26.921 1.00 63.36  ? 103 GLY   B C   1 
ATOM   990  O  O   . GLY   B 2 94  ? -17.594 14.819  -27.982 1.00 63.70  ? 103 GLY   B O   1 
ATOM   991  N  N   . GLU   B 2 95  ? -17.642 12.854  -26.888 1.00 63.33  ? 104 GLU   B N   1 
ATOM   992  C  CA  . GLU   B 2 95  ? -17.794 12.047  -28.090 1.00 64.11  ? 104 GLU   B CA  1 
ATOM   993  C  C   . GLU   B 2 95  ? -18.988 11.098  -27.954 1.00 64.58  ? 104 GLU   B C   1 
ATOM   994  O  O   . GLU   B 2 95  ? -19.427 10.798  -26.845 1.00 64.58  ? 104 GLU   B O   1 
ATOM   995  C  CB  . GLU   B 2 95  ? -16.495 11.267  -28.391 1.00 66.58  ? 104 GLU   B CB  1 
ATOM   996  C  CG  . GLU   B 2 95  ? -15.311 12.156  -28.737 1.00 71.66  ? 104 GLU   B CG  1 
ATOM   997  C  CD  . GLU   B 2 95  ? -13.951 11.483  -28.681 1.00 79.83  ? 104 GLU   B CD  1 
ATOM   998  O  OE1 . GLU   B 2 95  ? -13.898 10.257  -28.432 1.00 81.21  ? 104 GLU   B OE1 1 
ATOM   999  O  OE2 . GLU   B 2 95  ? -12.934 12.182  -28.897 1.00 82.93  ? 104 GLU   B OE2 1 
ATOM   1000 N  N   . ARG   B 2 96  ? -19.501 10.617  -29.084 1.00 64.84  ? 105 ARG   B N   1 
ATOM   1001 C  CA  . ARG   B 2 96  ? -20.652 9.728   -29.138 1.00 65.77  ? 105 ARG   B CA  1 
ATOM   1002 C  C   . ARG   B 2 96  ? -20.345 8.333   -28.618 1.00 66.35  ? 105 ARG   B C   1 
ATOM   1003 O  O   . ARG   B 2 96  ? -19.205 7.868   -28.726 1.00 66.71  ? 105 ARG   B O   1 
ATOM   1004 C  CB  . ARG   B 2 96  ? -21.113 9.616   -30.593 1.00 67.55  ? 105 ARG   B CB  1 
ATOM   1005 C  CG  . ARG   B 2 96  ? -22.617 9.595   -30.794 1.00 71.27  ? 105 ARG   B CG  1 
ATOM   1006 C  CD  . ARG   B 2 96  ? -23.042 10.585  -31.870 1.00 75.17  ? 105 ARG   B CD  1 
ATOM   1007 N  NE  . ARG   B 2 96  ? -22.397 10.335  -33.159 1.00 79.74  ? 105 ARG   B NE  1 
ATOM   1008 C  CZ  . ARG   B 2 96  ? -21.925 11.286  -33.964 1.00 83.28  ? 105 ARG   B CZ  1 
ATOM   1009 N  NH1 . ARG   B 2 96  ? -22.018 12.568  -33.619 1.00 82.91  ? 105 ARG   B NH1 1 
ATOM   1010 N  NH2 . ARG   B 2 96  ? -21.354 10.964  -35.119 1.00 83.78  ? 105 ARG   B NH2 1 
ATOM   1011 N  N   . ALA   B 2 97  ? -21.383 7.636   -28.109 1.00 66.04  ? 106 ALA   B N   1 
ATOM   1012 C  CA  . ALA   B 2 97  ? -21.282 6.247   -27.670 1.00 66.49  ? 106 ALA   B CA  1 
ATOM   1013 C  C   . ALA   B 2 97  ? -20.872 5.378   -28.874 1.00 67.22  ? 106 ALA   B C   1 
ATOM   1014 O  O   . ALA   B 2 97  ? -21.397 5.568   -29.971 1.00 67.65  ? 106 ALA   B O   1 
ATOM   1015 C  CB  . ALA   B 2 97  ? -22.625 5.783   -27.136 1.00 66.56  ? 106 ALA   B CB  1 
ATOM   1016 N  N   . LYS   B 2 98  ? -19.914 4.465   -28.690 1.00 67.23  ? 107 LYS   B N   1 
ATOM   1017 C  CA  . LYS   B 2 98  ? -19.400 3.644   -29.786 1.00 67.37  ? 107 LYS   B CA  1 
ATOM   1018 C  C   . LYS   B 2 98  ? -19.122 2.212   -29.333 1.00 66.48  ? 107 LYS   B C   1 
ATOM   1019 O  O   . LYS   B 2 98  ? -18.506 2.026   -28.298 1.00 66.37  ? 107 LYS   B O   1 
ATOM   1020 C  CB  . LYS   B 2 98  ? -18.103 4.293   -30.280 1.00 70.25  ? 107 LYS   B CB  1 
ATOM   1021 C  CG  . LYS   B 2 98  ? -17.499 3.719   -31.557 1.00 75.71  ? 107 LYS   B CG  1 
ATOM   1022 C  CD  . LYS   B 2 98  ? -16.178 4.441   -31.935 1.00 81.00  ? 107 LYS   B CD  1 
ATOM   1023 C  CE  . LYS   B 2 98  ? -15.308 4.778   -30.724 1.00 84.70  ? 107 LYS   B CE  1 
ATOM   1024 N  NZ  . LYS   B 2 98  ? -13.869 4.467   -30.943 1.00 86.76  ? 107 LYS   B NZ  1 
ATOM   1025 N  N   . ASN   B 2 99  ? -19.559 1.204   -30.107 1.00 66.04  ? 108 ASN   B N   1 
ATOM   1026 C  CA  . ASN   B 2 99  ? -19.315 -0.207  -29.776 1.00 66.01  ? 108 ASN   B CA  1 
ATOM   1027 C  C   . ASN   B 2 99  ? -18.010 -0.685  -30.374 1.00 66.32  ? 108 ASN   B C   1 
ATOM   1028 O  O   . ASN   B 2 99  ? -17.820 -0.583  -31.582 1.00 66.86  ? 108 ASN   B O   1 
ATOM   1029 C  CB  . ASN   B 2 99  ? -20.439 -1.112  -30.284 1.00 66.41  ? 108 ASN   B CB  1 
ATOM   1030 C  CG  . ASN   B 2 99  ? -21.760 -0.899  -29.598 1.00 68.81  ? 108 ASN   B CG  1 
ATOM   1031 O  OD1 . ASN   B 2 99  ? -22.232 0.226   -29.455 1.00 70.05  ? 108 ASN   B OD1 1 
ATOM   1032 N  ND2 . ASN   B 2 99  ? -22.399 -1.975  -29.179 1.00 68.85  ? 108 ASN   B ND2 1 
ATOM   1033 N  N   . ILE   B 2 100 ? -17.117 -1.228  -29.550 1.00 66.01  ? 109 ILE   B N   1 
ATOM   1034 C  CA  . ILE   B 2 100 ? -15.841 -1.740  -30.040 1.00 66.02  ? 109 ILE   B CA  1 
ATOM   1035 C  C   . ILE   B 2 100 ? -15.746 -3.208  -29.698 1.00 65.69  ? 109 ILE   B C   1 
ATOM   1036 O  O   . ILE   B 2 100 ? -15.694 -3.549  -28.526 1.00 65.90  ? 109 ILE   B O   1 
ATOM   1037 C  CB  . ILE   B 2 100 ? -14.661 -0.984  -29.409 1.00 66.80  ? 109 ILE   B CB  1 
ATOM   1038 C  CG1 . ILE   B 2 100 ? -14.829 0.541   -29.496 1.00 67.87  ? 109 ILE   B CG1 1 
ATOM   1039 C  CG2 . ILE   B 2 100 ? -13.347 -1.455  -30.012 1.00 67.27  ? 109 ILE   B CG2 1 
ATOM   1040 C  CD1 . ILE   B 2 100 ? -14.838 1.088   -30.876 1.00 68.88  ? 109 ILE   B CD1 1 
ATOM   1041 N  N   . GLN   B 2 101 ? -15.706 -4.077  -30.699 1.00 65.27  ? 110 GLN   B N   1 
ATOM   1042 C  CA  . GLN   B 2 101 ? -15.623 -5.516  -30.471 1.00 65.49  ? 110 GLN   B CA  1 
ATOM   1043 C  C   . GLN   B 2 101 ? -14.191 -5.978  -30.242 1.00 65.61  ? 110 GLN   B C   1 
ATOM   1044 O  O   . GLN   B 2 101 ? -13.293 -5.548  -30.960 1.00 65.74  ? 110 GLN   B O   1 
ATOM   1045 C  CB  . GLN   B 2 101 ? -16.228 -6.269  -31.654 1.00 66.96  ? 110 GLN   B CB  1 
ATOM   1046 C  CG  . GLN   B 2 101 ? -16.506 -7.722  -31.368 1.00 70.01  ? 110 GLN   B CG  1 
ATOM   1047 C  CD  . GLN   B 2 101 ? -17.368 -8.295  -32.448 1.00 74.78  ? 110 GLN   B CD  1 
ATOM   1048 O  OE1 . GLN   B 2 101 ? -18.323 -7.666  -32.921 1.00 76.27  ? 110 GLN   B OE1 1 
ATOM   1049 N  NE2 . GLN   B 2 101 ? -17.038 -9.500  -32.877 1.00 76.28  ? 110 GLN   B NE2 1 
ATOM   1050 N  N   . THR   B 2 102 ? -13.968 -6.850  -29.236 1.00 65.28  ? 111 THR   B N   1 
ATOM   1051 C  CA  . THR   B 2 102 ? -12.639 -7.384  -28.930 1.00 65.30  ? 111 THR   B CA  1 
ATOM   1052 C  C   . THR   B 2 102 ? -12.725 -8.731  -28.226 1.00 65.52  ? 111 THR   B C   1 
ATOM   1053 O  O   . THR   B 2 102 ? -13.758 -9.046  -27.635 1.00 65.93  ? 111 THR   B O   1 
ATOM   1054 C  CB  . THR   B 2 102 ? -11.846 -6.394  -28.058 1.00 66.67  ? 111 THR   B CB  1 
ATOM   1055 O  OG1 . THR   B 2 102 ? -10.479 -6.799  -28.005 1.00 67.86  ? 111 THR   B OG1 1 
ATOM   1056 C  CG2 . THR   B 2 102 ? -12.401 -6.269  -26.653 1.00 67.09  ? 111 THR   B CG2 1 
ATOM   1057 N  N   . LEU   B 2 103 ? -11.642 -9.533  -28.268 1.00 65.12  ? 112 LEU   B N   1 
ATOM   1058 C  CA  . LEU   B 2 103 ? -11.615 -10.780 -27.507 1.00 64.91  ? 112 LEU   B CA  1 
ATOM   1059 C  C   . LEU   B 2 103 ? -10.850 -10.473 -26.245 1.00 64.99  ? 112 LEU   B C   1 
ATOM   1060 O  O   . LEU   B 2 103 ? -9.678  -10.096 -26.312 1.00 65.13  ? 112 LEU   B O   1 
ATOM   1061 C  CB  . LEU   B 2 103 ? -10.929 -11.936 -28.227 1.00 64.97  ? 112 LEU   B CB  1 
ATOM   1062 C  CG  . LEU   B 2 103 ? -10.945 -13.220 -27.413 1.00 66.26  ? 112 LEU   B CG  1 
ATOM   1063 C  CD1 . LEU   B 2 103 ? -12.290 -13.859 -27.461 1.00 66.80  ? 112 LEU   B CD1 1 
ATOM   1064 C  CD2 . LEU   B 2 103 ? -9.875  -14.160 -27.844 1.00 66.75  ? 112 LEU   B CD2 1 
ATOM   1065 N  N   . PRO   B 2 104 ? -11.493 -10.634 -25.081 1.00 64.58  ? 113 PRO   B N   1 
ATOM   1066 C  CA  . PRO   B 2 104 ? -10.803 -10.327 -23.833 1.00 64.44  ? 113 PRO   B CA  1 
ATOM   1067 C  C   . PRO   B 2 104 ? -9.656  -11.268 -23.491 1.00 64.67  ? 113 PRO   B C   1 
ATOM   1068 O  O   . PRO   B 2 104 ? -9.651  -12.437 -23.871 1.00 65.00  ? 113 PRO   B O   1 
ATOM   1069 C  CB  . PRO   B 2 104 ? -11.909 -10.424 -22.777 1.00 64.93  ? 113 PRO   B CB  1 
ATOM   1070 C  CG  . PRO   B 2 104 ? -13.173 -10.438 -23.529 1.00 65.42  ? 113 PRO   B CG  1 
ATOM   1071 C  CD  . PRO   B 2 104 ? -12.883 -11.051 -24.841 1.00 63.86  ? 113 PRO   B CD  1 
ATOM   1072 N  N   . GLY   B 2 105 ? -8.695  -10.720 -22.759 1.00 64.21  ? 114 GLY   B N   1 
ATOM   1073 C  CA  . GLY   B 2 105 ? -7.562  -11.437 -22.202 1.00 64.08  ? 114 GLY   B CA  1 
ATOM   1074 C  C   . GLY   B 2 105 ? -7.886  -11.908 -20.796 1.00 63.76  ? 114 GLY   B C   1 
ATOM   1075 O  O   . GLY   B 2 105 ? -9.060  -12.034 -20.437 1.00 64.20  ? 114 GLY   B O   1 
ATOM   1076 N  N   . ILE   B 2 106 ? -6.862  -12.181 -19.980 1.00 63.00  ? 115 ILE   B N   1 
ATOM   1077 C  CA  . ILE   B 2 106 ? -7.077  -12.696 -18.629 1.00 62.92  ? 115 ILE   B CA  1 
ATOM   1078 C  C   . ILE   B 2 106 ? -6.207  -11.982 -17.605 1.00 62.95  ? 115 ILE   B C   1 
ATOM   1079 O  O   . ILE   B 2 106 ? -5.028  -11.752 -17.844 1.00 63.19  ? 115 ILE   B O   1 
ATOM   1080 C  CB  . ILE   B 2 106 ? -6.743  -14.226 -18.580 1.00 63.38  ? 115 ILE   B CB  1 
ATOM   1081 C  CG1 . ILE   B 2 106 ? -7.559  -15.054 -19.580 1.00 64.40  ? 115 ILE   B CG1 1 
ATOM   1082 C  CG2 . ILE   B 2 106 ? -6.866  -14.797 -17.164 1.00 63.91  ? 115 ILE   B CG2 1 
ATOM   1083 C  CD1 . ILE   B 2 106 ? -8.993  -15.189 -19.264 1.00 65.81  ? 115 ILE   B CD1 1 
ATOM   1084 N  N   . PHE   B 2 107 ? -6.769  -11.706 -16.433 1.00 62.55  ? 116 PHE   B N   1 
ATOM   1085 C  CA  . PHE   B 2 107 ? -6.050  -11.220 -15.275 1.00 62.61  ? 116 PHE   B CA  1 
ATOM   1086 C  C   . PHE   B 2 107 ? -5.996  -12.464 -14.403 1.00 63.44  ? 116 PHE   B C   1 
ATOM   1087 O  O   . PHE   B 2 107 ? -7.047  -12.925 -13.960 1.00 63.65  ? 116 PHE   B O   1 
ATOM   1088 C  CB  . PHE   B 2 107 ? -6.875  -10.163 -14.530 1.00 62.08  ? 116 PHE   B CB  1 
ATOM   1089 C  CG  . PHE   B 2 107 ? -6.669  -8.726  -14.930 1.00 62.19  ? 116 PHE   B CG  1 
ATOM   1090 C  CD1 . PHE   B 2 107 ? -5.979  -8.401  -16.085 1.00 62.88  ? 116 PHE   B CD1 1 
ATOM   1091 C  CD2 . PHE   B 2 107 ? -7.184  -7.699  -14.164 1.00 62.70  ? 116 PHE   B CD2 1 
ATOM   1092 C  CE1 . PHE   B 2 107 ? -5.811  -7.077  -16.464 1.00 63.44  ? 116 PHE   B CE1 1 
ATOM   1093 C  CE2 . PHE   B 2 107 ? -7.003  -6.377  -14.541 1.00 63.48  ? 116 PHE   B CE2 1 
ATOM   1094 C  CZ  . PHE   B 2 107 ? -6.329  -6.074  -15.695 1.00 63.21  ? 116 PHE   B CZ  1 
ATOM   1095 N  N   . LYS   B 2 108 ? -4.812  -13.050 -14.204 1.00 63.75  ? 117 LYS   B N   1 
ATOM   1096 C  CA  . LYS   B 2 108 ? -4.684  -14.229 -13.355 1.00 64.56  ? 117 LYS   B CA  1 
ATOM   1097 C  C   . LYS   B 2 108 ? -4.370  -13.737 -11.947 1.00 64.67  ? 117 LYS   B C   1 
ATOM   1098 O  O   . LYS   B 2 108 ? -3.353  -13.081 -11.748 1.00 64.55  ? 117 LYS   B O   1 
ATOM   1099 C  CB  . LYS   B 2 108 ? -3.573  -15.158 -13.880 1.00 67.27  ? 117 LYS   B CB  1 
ATOM   1100 C  CG  . LYS   B 2 108 ? -3.800  -15.605 -15.323 1.00 73.37  ? 117 LYS   B CG  1 
ATOM   1101 C  CD  . LYS   B 2 108 ? -2.643  -16.449 -15.889 1.00 80.08  ? 117 LYS   B CD  1 
ATOM   1102 C  CE  . LYS   B 2 108 ? -2.886  -16.828 -17.342 1.00 85.57  ? 117 LYS   B CE  1 
ATOM   1103 N  NZ  . LYS   B 2 108 ? -1.741  -17.565 -17.965 1.00 88.02  ? 117 LYS   B NZ  1 
ATOM   1104 N  N   . THR   B 2 109 ? -5.268  -13.983 -10.980 1.00 64.89  ? 118 THR   B N   1 
ATOM   1105 C  CA  . THR   B 2 109 ? -5.060  -13.532 -9.596  1.00 65.39  ? 118 THR   B CA  1 
ATOM   1106 C  C   . THR   B 2 109 ? -5.000  -14.719 -8.616  1.00 65.62  ? 118 THR   B C   1 
ATOM   1107 O  O   . THR   B 2 109 ? -5.370  -15.834 -8.983  1.00 65.62  ? 118 THR   B O   1 
ATOM   1108 C  CB  . THR   B 2 109 ? -6.135  -12.472 -9.166  1.00 66.67  ? 118 THR   B CB  1 
ATOM   1109 O  OG1 . THR   B 2 109 ? -7.359  -13.105 -8.784  1.00 67.82  ? 118 THR   B OG1 1 
ATOM   1110 C  CG2 . THR   B 2 109 ? -6.398  -11.426 -10.219 1.00 66.96  ? 118 THR   B CG2 1 
ATOM   1111 N  N   . LYS   B 2 110 ? -4.580  -14.472 -7.360  1.00 65.69  ? 119 LYS   B N   1 
ATOM   1112 C  CA  . LYS   B 2 110 ? -4.559  -15.496 -6.312  1.00 66.51  ? 119 LYS   B CA  1 
ATOM   1113 C  C   . LYS   B 2 110 ? -5.988  -15.992 -5.954  1.00 67.25  ? 119 LYS   B C   1 
ATOM   1114 O  O   . LYS   B 2 110 ? -6.161  -17.124 -5.488  1.00 67.53  ? 119 LYS   B O   1 
ATOM   1115 C  CB  . LYS   B 2 110 ? -3.822  -14.980 -5.050  1.00 67.59  ? 119 LYS   B CB  1 
ATOM   1116 C  CG  . LYS   B 2 110 ? -4.540  -13.862 -4.297  1.00 69.74  ? 119 LYS   B CG  1 
ATOM   1117 C  CD  . LYS   B 2 110 ? -3.622  -13.203 -3.265  1.00 72.55  ? 119 LYS   B CD  1 
ATOM   1118 C  CE  . LYS   B 2 110 ? -4.297  -12.936 -1.938  1.00 74.99  ? 119 LYS   B CE  1 
ATOM   1119 N  NZ  . LYS   B 2 110 ? -5.091  -11.677 -1.944  1.00 76.36  ? 119 LYS   B NZ  1 
ATOM   1120 N  N   . ASP   B 2 111 ? -7.002  -15.156 -6.195  1.00 67.17  ? 120 ASP   B N   1 
ATOM   1121 C  CA  . ASP   B 2 111 ? -8.388  -15.501 -5.936  1.00 67.61  ? 120 ASP   B CA  1 
ATOM   1122 C  C   . ASP   B 2 111 ? -9.149  -15.957 -7.196  1.00 67.52  ? 120 ASP   B C   1 
ATOM   1123 O  O   . ASP   B 2 111 ? -10.365 -16.115 -7.120  1.00 68.04  ? 120 ASP   B O   1 
ATOM   1124 C  CB  . ASP   B 2 111 ? -9.113  -14.301 -5.308  1.00 69.74  ? 120 ASP   B CB  1 
ATOM   1125 C  CG  . ASP   B 2 111 ? -8.541  -13.858 -3.980  1.00 74.36  ? 120 ASP   B CG  1 
ATOM   1126 O  OD1 . ASP   B 2 111 ? -8.051  -14.730 -3.225  1.00 74.87  ? 120 ASP   B OD1 1 
ATOM   1127 O  OD2 . ASP   B 2 111 ? -8.596  -12.637 -3.687  1.00 76.53  ? 120 ASP   B OD2 1 
ATOM   1128 N  N   . GLY   B 2 112 ? -8.468  -16.133 -8.332  1.00 66.68  ? 121 GLY   B N   1 
ATOM   1129 C  CA  . GLY   B 2 112 ? -9.126  -16.571 -9.559  1.00 66.53  ? 121 GLY   B CA  1 
ATOM   1130 C  C   . GLY   B 2 112 ? -8.889  -15.699 -10.775 1.00 66.18  ? 121 GLY   B C   1 
ATOM   1131 O  O   . GLY   B 2 112 ? -8.298  -14.626 -10.662 1.00 66.64  ? 121 GLY   B O   1 
ATOM   1132 N  N   . ASP   B 2 113 ? -9.345  -16.151 -11.952 1.00 65.30  ? 122 ASP   B N   1 
ATOM   1133 C  CA  . ASP   B 2 113 ? -9.165  -15.395 -13.194 1.00 65.37  ? 122 ASP   B CA  1 
ATOM   1134 C  C   . ASP   B 2 113 ? -10.311 -14.449 -13.503 1.00 64.92  ? 122 ASP   B C   1 
ATOM   1135 O  O   . ASP   B 2 113 ? -11.465 -14.714 -13.159 1.00 65.06  ? 122 ASP   B O   1 
ATOM   1136 C  CB  . ASP   B 2 113 ? -8.970  -16.328 -14.392 1.00 66.98  ? 122 ASP   B CB  1 
ATOM   1137 C  CG  . ASP   B 2 113 ? -7.754  -17.212 -14.326 1.00 72.52  ? 122 ASP   B CG  1 
ATOM   1138 O  OD1 . ASP   B 2 113 ? -6.969  -17.083 -13.346 1.00 73.27  ? 122 ASP   B OD1 1 
ATOM   1139 O  OD2 . ASP   B 2 113 ? -7.578  -18.038 -15.248 1.00 75.31  ? 122 ASP   B OD2 1 
ATOM   1140 N  N   . ILE   B 2 114 ? -9.992  -13.343 -14.173 1.00 63.99  ? 123 ILE   B N   1 
ATOM   1141 C  CA  . ILE   B 2 114 ? -10.991 -12.346 -14.550 1.00 63.70  ? 123 ILE   B CA  1 
ATOM   1142 C  C   . ILE   B 2 114 ? -10.740 -11.966 -16.010 1.00 63.04  ? 123 ILE   B C   1 
ATOM   1143 O  O   . ILE   B 2 114 ? -9.591  -11.912 -16.439 1.00 62.64  ? 123 ILE   B O   1 
ATOM   1144 C  CB  . ILE   B 2 114 ? -10.955 -11.056 -13.655 1.00 64.38  ? 123 ILE   B CB  1 
ATOM   1145 C  CG1 . ILE   B 2 114 ? -10.518 -11.309 -12.211 1.00 65.65  ? 123 ILE   B CG1 1 
ATOM   1146 C  CG2 . ILE   B 2 114 ? -12.280 -10.317 -13.678 1.00 64.90  ? 123 ILE   B CG2 1 
ATOM   1147 C  CD1 . ILE   B 2 114 ? -10.140 -10.051 -11.478 1.00 67.35  ? 123 ILE   B CD1 1 
ATOM   1148 N  N   . GLY   B 2 115 ? -11.801 -11.658 -16.747 1.00 62.60  ? 124 GLY   B N   1 
ATOM   1149 C  CA  . GLY   B 2 115 ? -11.661 -11.193 -18.121 1.00 62.81  ? 124 GLY   B CA  1 
ATOM   1150 C  C   . GLY   B 2 115 ? -11.001 -9.828  -18.160 1.00 62.74  ? 124 GLY   B C   1 
ATOM   1151 O  O   . GLY   B 2 115 ? -11.035 -9.086  -17.167 1.00 62.81  ? 124 GLY   B O   1 
ATOM   1152 N  N   . ALA   B 2 116 ? -10.383 -9.486  -19.289 1.00 62.54  ? 125 ALA   B N   1 
ATOM   1153 C  CA  . ALA   B 2 116 ? -9.713  -8.194  -19.411 1.00 63.01  ? 125 ALA   B CA  1 
ATOM   1154 C  C   . ALA   B 2 116 ? -9.802  -7.575  -20.806 1.00 63.44  ? 125 ALA   B C   1 
ATOM   1155 O  O   . ALA   B 2 116 ? -9.479  -8.220  -21.789 1.00 63.20  ? 125 ALA   B O   1 
ATOM   1156 C  CB  . ALA   B 2 116 ? -8.261  -8.303  -18.965 1.00 62.96  ? 125 ALA   B CB  1 
ATOM   1157 N  N   . VAL   B 2 117 ? -10.233 -6.315  -20.887 1.00 63.80  ? 126 VAL   B N   1 
ATOM   1158 C  CA  A VAL   B 2 117 ? -10.321 -5.616  -22.165 0.50 64.41  ? 126 VAL   B CA  1 
ATOM   1159 C  CA  B VAL   B 2 117 ? -10.350 -5.597  -22.147 0.50 64.45  ? 126 VAL   B CA  1 
ATOM   1160 C  C   . VAL   B 2 117 ? -9.119  -4.690  -22.351 1.00 64.80  ? 126 VAL   B C   1 
ATOM   1161 O  O   . VAL   B 2 117 ? -8.855  -3.820  -21.516 1.00 64.78  ? 126 VAL   B O   1 
ATOM   1162 C  CB  A VAL   B 2 117 ? -11.677 -4.916  -22.409 0.50 65.23  ? 126 VAL   B CB  1 
ATOM   1163 C  CB  B VAL   B 2 117 ? -11.690 -4.828  -22.158 0.50 65.31  ? 126 VAL   B CB  1 
ATOM   1164 C  CG1 A VAL   B 2 117 ? -12.715 -5.914  -22.911 0.50 65.82  ? 126 VAL   B CG1 1 
ATOM   1165 C  CG1 B VAL   B 2 117 ? -11.709 -3.735  -23.214 0.50 65.87  ? 126 VAL   B CG1 1 
ATOM   1166 C  CG2 A VAL   B 2 117 ? -12.171 -4.196  -21.159 0.50 65.72  ? 126 VAL   B CG2 1 
ATOM   1167 C  CG2 B VAL   B 2 117 ? -12.854 -5.791  -22.351 0.50 65.90  ? 126 VAL   B CG2 1 
ATOM   1168 N  N   . ALA   B 2 118 ? -8.350  -4.908  -23.440 1.00 64.91  ? 127 ALA   B N   1 
ATOM   1169 C  CA  . ALA   B 2 118 ? -7.137  -4.125  -23.693 1.00 65.48  ? 127 ALA   B CA  1 
ATOM   1170 C  C   . ALA   B 2 118 ? -7.331  -2.843  -24.510 1.00 66.10  ? 127 ALA   B C   1 
ATOM   1171 O  O   . ALA   B 2 118 ? -6.365  -2.327  -25.067 1.00 66.39  ? 127 ALA   B O   1 
ATOM   1172 C  CB  . ALA   B 2 118 ? -6.081  -4.997  -24.344 1.00 65.33  ? 127 ALA   B CB  1 
ATOM   1173 N  N   . LEU   B 2 119 ? -8.552  -2.309  -24.557 1.00 65.99  ? 128 LEU   B N   1 
ATOM   1174 C  CA  . LEU   B 2 119 ? -8.836  -1.083  -25.299 1.00 65.90  ? 128 LEU   B CA  1 
ATOM   1175 C  C   . LEU   B 2 119 ? -8.359  0.155   -24.529 1.00 66.35  ? 128 LEU   B C   1 
ATOM   1176 O  O   . LEU   B 2 119 ? -8.341  0.163   -23.299 1.00 66.50  ? 128 LEU   B O   1 
ATOM   1177 C  CB  . LEU   B 2 119 ? -10.331 -1.007  -25.641 1.00 65.59  ? 128 LEU   B CB  1 
ATOM   1178 C  CG  . LEU   B 2 119 ? -10.835 -2.193  -26.461 1.00 66.57  ? 128 LEU   B CG  1 
ATOM   1179 C  CD1 . LEU   B 2 119 ? -12.334 -2.294  -26.425 1.00 67.06  ? 128 LEU   B CD1 1 
ATOM   1180 C  CD2 . LEU   B 2 119 ? -10.327 -2.142  -27.880 1.00 66.91  ? 128 LEU   B CD2 1 
ATOM   1181 N  N   . ASP   B 2 120 ? -7.942  1.187   -25.253 1.00 66.61  ? 129 ASP   B N   1 
ATOM   1182 C  CA  . ASP   B 2 120 ? -7.395  2.393   -24.643 1.00 67.27  ? 129 ASP   B CA  1 
ATOM   1183 C  C   . ASP   B 2 120 ? -8.281  3.610   -24.803 1.00 66.52  ? 129 ASP   B C   1 
ATOM   1184 O  O   . ASP   B 2 120 ? -8.527  4.057   -25.914 1.00 66.61  ? 129 ASP   B O   1 
ATOM   1185 C  CB  . ASP   B 2 120 ? -6.018  2.680   -25.230 1.00 70.69  ? 129 ASP   B CB  1 
ATOM   1186 C  CG  . ASP   B 2 120 ? -4.943  2.782   -24.180 1.00 78.07  ? 129 ASP   B CG  1 
ATOM   1187 O  OD1 . ASP   B 2 120 ? -5.245  3.273   -23.062 1.00 79.35  ? 129 ASP   B OD1 1 
ATOM   1188 O  OD2 . ASP   B 2 120 ? -3.804  2.373   -24.466 1.00 81.74  ? 129 ASP   B OD2 1 
ATOM   1189 N  N   . TYR   B 2 121 ? -8.717  4.173   -23.690 1.00 65.99  ? 130 TYR   B N   1 
ATOM   1190 C  CA  . TYR   B 2 121 ? -9.610  5.323   -23.659 1.00 65.81  ? 130 TYR   B CA  1 
ATOM   1191 C  C   . TYR   B 2 121 ? -9.232  6.272   -22.522 1.00 64.64  ? 130 TYR   B C   1 
ATOM   1192 O  O   . TYR   B 2 121 ? -8.573  5.846   -21.571 1.00 65.01  ? 130 TYR   B O   1 
ATOM   1193 C  CB  . TYR   B 2 121 ? -11.059 4.824   -23.472 1.00 66.55  ? 130 TYR   B CB  1 
ATOM   1194 C  CG  . TYR   B 2 121 ? -11.677 4.398   -24.780 1.00 68.13  ? 130 TYR   B CG  1 
ATOM   1195 C  CD1 . TYR   B 2 121 ? -12.211 5.332   -25.652 1.00 69.37  ? 130 TYR   B CD1 1 
ATOM   1196 C  CD2 . TYR   B 2 121 ? -11.633 3.072   -25.194 1.00 69.46  ? 130 TYR   B CD2 1 
ATOM   1197 C  CE1 . TYR   B 2 121 ? -12.713 4.958   -26.889 1.00 70.74  ? 130 TYR   B CE1 1 
ATOM   1198 C  CE2 . TYR   B 2 121 ? -12.120 2.687   -26.435 1.00 70.57  ? 130 TYR   B CE2 1 
ATOM   1199 C  CZ  . TYR   B 2 121 ? -12.668 3.633   -27.277 1.00 71.94  ? 130 TYR   B CZ  1 
ATOM   1200 O  OH  . TYR   B 2 121 ? -13.162 3.272   -28.506 1.00 74.49  ? 130 TYR   B OH  1 
ATOM   1201 N  N   . PRO   B 2 122 ? -9.642  7.561   -22.578 1.00 62.92  ? 131 PRO   B N   1 
ATOM   1202 C  CA  . PRO   B 2 122 ? -9.334  8.469   -21.459 1.00 61.23  ? 131 PRO   B CA  1 
ATOM   1203 C  C   . PRO   B 2 122 ? -10.018 8.028   -20.166 1.00 58.91  ? 131 PRO   B C   1 
ATOM   1204 O  O   . PRO   B 2 122 ? -11.054 7.364   -20.210 1.00 58.93  ? 131 PRO   B O   1 
ATOM   1205 C  CB  . PRO   B 2 122 ? -9.866  9.831   -21.931 1.00 62.21  ? 131 PRO   B CB  1 
ATOM   1206 C  CG  . PRO   B 2 122 ? -10.162 9.680   -23.372 1.00 63.04  ? 131 PRO   B CG  1 
ATOM   1207 C  CD  . PRO   B 2 122 ? -10.432 8.239   -23.624 1.00 62.10  ? 131 PRO   B CD  1 
ATOM   1208 N  N   . ALA   B 2 123 ? -9.442  8.393   -19.013 1.00 56.79  ? 132 ALA   B N   1 
ATOM   1209 C  CA  . ALA   B 2 123 ? -9.986  8.003   -17.707 1.00 55.17  ? 132 ALA   B CA  1 
ATOM   1210 C  C   . ALA   B 2 123 ? -11.474 8.359   -17.496 1.00 53.69  ? 132 ALA   B C   1 
ATOM   1211 O  O   . ALA   B 2 123 ? -12.143 7.701   -16.704 1.00 53.94  ? 132 ALA   B O   1 
ATOM   1212 C  CB  . ALA   B 2 123 ? -9.133  8.568   -16.586 1.00 54.79  ? 132 ALA   B CB  1 
ATOM   1213 N  N   . GLY   B 2 124 ? -11.978 9.353   -18.233 1.00 51.92  ? 133 GLY   B N   1 
ATOM   1214 C  CA  . GLY   B 2 124 ? -13.378 9.762   -18.182 1.00 50.57  ? 133 GLY   B CA  1 
ATOM   1215 C  C   . GLY   B 2 124 ? -14.346 8.765   -18.805 1.00 49.04  ? 133 GLY   B C   1 
ATOM   1216 O  O   . GLY   B 2 124 ? -15.560 8.916   -18.681 1.00 48.57  ? 133 GLY   B O   1 
ATOM   1217 N  N   . THR   B 2 125 ? -13.821 7.741   -19.494 1.00 48.25  ? 134 THR   B N   1 
ATOM   1218 C  CA  . THR   B 2 125 ? -14.622 6.667   -20.088 1.00 47.99  ? 134 THR   B CA  1 
ATOM   1219 C  C   . THR   B 2 125 ? -15.005 5.598   -19.027 1.00 47.10  ? 134 THR   B C   1 
ATOM   1220 O  O   . THR   B 2 125 ? -15.789 4.713   -19.342 1.00 47.31  ? 134 THR   B O   1 
ATOM   1221 C  CB  . THR   B 2 125 ? -13.887 6.066   -21.331 1.00 49.45  ? 134 THR   B CB  1 
ATOM   1222 O  OG1 . THR   B 2 125 ? -13.407 7.120   -22.174 1.00 50.53  ? 134 THR   B OG1 1 
ATOM   1223 C  CG2 . THR   B 2 125 ? -14.771 5.157   -22.174 1.00 49.66  ? 134 THR   B CG2 1 
ATOM   1224 N  N   . SER   B 2 126 ? -14.456 5.678   -17.782 1.00 46.37  ? 135 SER   B N   1 
ATOM   1225 C  CA  . SER   B 2 126 ? -14.699 4.738   -16.673 1.00 46.39  ? 135 SER   B CA  1 
ATOM   1226 C  C   . SER   B 2 126 ? -16.180 4.528   -16.346 1.00 46.56  ? 135 SER   B C   1 
ATOM   1227 O  O   . SER   B 2 126 ? -16.883 5.480   -16.066 1.00 46.89  ? 135 SER   B O   1 
ATOM   1228 C  CB  . SER   B 2 126 ? -14.005 5.222   -15.413 1.00 47.09  ? 135 SER   B CB  1 
ATOM   1229 O  OG  . SER   B 2 126 ? -12.602 5.083   -15.490 1.00 49.10  ? 135 SER   B OG  1 
ATOM   1230 N  N   . GLY   B 2 127 ? -16.611 3.284   -16.303 1.00 45.90  ? 136 GLY   B N   1 
ATOM   1231 C  CA  . GLY   B 2 127 ? -17.995 2.928   -16.049 1.00 46.04  ? 136 GLY   B CA  1 
ATOM   1232 C  C   . GLY   B 2 127 ? -18.725 2.464   -17.292 1.00 46.66  ? 136 GLY   B C   1 
ATOM   1233 O  O   . GLY   B 2 127 ? -19.908 2.145   -17.220 1.00 47.42  ? 136 GLY   B O   1 
ATOM   1234 N  N   . SER   B 2 128 ? -18.043 2.432   -18.447 1.00 46.28  ? 137 SER   B N   1 
ATOM   1235 C  CA  . SER   B 2 128 ? -18.629 1.998   -19.704 1.00 46.57  ? 137 SER   B CA  1 
ATOM   1236 C  C   . SER   B 2 128 ? -18.925 0.496   -19.680 1.00 46.50  ? 137 SER   B C   1 
ATOM   1237 O  O   . SER   B 2 128 ? -18.090 -0.306  -19.257 1.00 45.90  ? 137 SER   B O   1 
ATOM   1238 C  CB  . SER   B 2 128 ? -17.716 2.363   -20.874 1.00 47.80  ? 137 SER   B CB  1 
ATOM   1239 O  OG  . SER   B 2 128 ? -17.805 3.742   -21.191 1.00 49.71  ? 137 SER   B OG  1 
ATOM   1240 N  N   . PRO   B 2 129 ? -20.135 0.103   -20.115 1.00 46.96  ? 138 PRO   B N   1 
ATOM   1241 C  CA  . PRO   B 2 129 ? -20.493 -1.321  -20.056 1.00 47.70  ? 138 PRO   B CA  1 
ATOM   1242 C  C   . PRO   B 2 129 ? -19.831 -2.199  -21.107 1.00 49.16  ? 138 PRO   B C   1 
ATOM   1243 O  O   . PRO   B 2 129 ? -19.692 -1.806  -22.260 1.00 49.58  ? 138 PRO   B O   1 
ATOM   1244 C  CB  . PRO   B 2 129 ? -22.012 -1.318  -20.229 1.00 47.90  ? 138 PRO   B CB  1 
ATOM   1245 C  CG  . PRO   B 2 129 ? -22.315 -0.049  -20.961 1.00 48.02  ? 138 PRO   B CG  1 
ATOM   1246 C  CD  . PRO   B 2 129 ? -21.248 0.939   -20.613 1.00 46.30  ? 138 PRO   B CD  1 
ATOM   1247 N  N   . ILE   B 2 130 ? -19.435 -3.398  -20.696 1.00 49.84  ? 139 ILE   B N   1 
ATOM   1248 C  CA  . ILE   B 2 130 ? -18.910 -4.414  -21.588 1.00 51.05  ? 139 ILE   B CA  1 
ATOM   1249 C  C   . ILE   B 2 130 ? -20.101 -5.357  -21.826 1.00 52.47  ? 139 ILE   B C   1 
ATOM   1250 O  O   . ILE   B 2 130 ? -20.769 -5.770  -20.874 1.00 52.30  ? 139 ILE   B O   1 
ATOM   1251 C  CB  . ILE   B 2 130 ? -17.700 -5.102  -20.954 1.00 51.49  ? 139 ILE   B CB  1 
ATOM   1252 C  CG1 . ILE   B 2 130 ? -16.587 -4.083  -20.697 1.00 52.51  ? 139 ILE   B CG1 1 
ATOM   1253 C  CG2 . ILE   B 2 130 ? -17.211 -6.252  -21.811 1.00 51.79  ? 139 ILE   B CG2 1 
ATOM   1254 C  CD1 . ILE   B 2 130 ? -15.586 -4.558  -19.709 1.00 53.62  ? 139 ILE   B CD1 1 
ATOM   1255 N  N   . LEU   B 2 131 ? -20.430 -5.613  -23.098 1.00 53.45  ? 140 LEU   B N   1 
ATOM   1256 C  CA  . LEU   B 2 131 ? -21.607 -6.389  -23.459 1.00 55.00  ? 140 LEU   B CA  1 
ATOM   1257 C  C   . LEU   B 2 131 ? -21.301 -7.722  -24.096 1.00 56.94  ? 140 LEU   B C   1 
ATOM   1258 O  O   . LEU   B 2 131 ? -20.335 -7.858  -24.845 1.00 57.21  ? 140 LEU   B O   1 
ATOM   1259 C  CB  . LEU   B 2 131 ? -22.489 -5.608  -24.443 1.00 55.31  ? 140 LEU   B CB  1 
ATOM   1260 C  CG  . LEU   B 2 131 ? -22.616 -4.102  -24.264 1.00 56.87  ? 140 LEU   B CG  1 
ATOM   1261 C  CD1 . LEU   B 2 131 ? -23.419 -3.502  -25.398 1.00 57.04  ? 140 LEU   B CD1 1 
ATOM   1262 C  CD2 . LEU   B 2 131 ? -23.198 -3.750  -22.883 1.00 57.33  ? 140 LEU   B CD2 1 
ATOM   1263 N  N   . ASP   B 2 132 ? -22.179 -8.696  -23.862 1.00 58.20  ? 141 ASP   B N   1 
ATOM   1264 C  CA  . ASP   B 2 132 ? -22.077 -9.985  -24.531 1.00 59.85  ? 141 ASP   B CA  1 
ATOM   1265 C  C   . ASP   B 2 132 ? -22.952 -9.953  -25.829 1.00 61.96  ? 141 ASP   B C   1 
ATOM   1266 O  O   . ASP   B 2 132 ? -23.653 -8.959  -26.075 1.00 61.97  ? 141 ASP   B O   1 
ATOM   1267 C  CB  . ASP   B 2 132 ? -22.455 -11.136 -23.582 1.00 60.68  ? 141 ASP   B CB  1 
ATOM   1268 C  CG  . ASP   B 2 132 ? -23.929 -11.304 -23.277 1.00 64.80  ? 141 ASP   B CG  1 
ATOM   1269 O  OD1 . ASP   B 2 132 ? -24.741 -10.504 -23.786 1.00 64.66  ? 141 ASP   B OD1 1 
ATOM   1270 O  OD2 . ASP   B 2 132 ? -24.270 -12.237 -22.526 1.00 67.93  ? 141 ASP   B OD2 1 
ATOM   1271 N  N   . LYS   B 2 133 ? -22.939 -11.044 -26.623 1.00 63.18  ? 142 LYS   B N   1 
ATOM   1272 C  CA  . LYS   B 2 133 ? -23.704 -11.176 -27.861 1.00 64.83  ? 142 LYS   B CA  1 
ATOM   1273 C  C   . LYS   B 2 133 ? -25.212 -10.843 -27.735 1.00 65.21  ? 142 LYS   B C   1 
ATOM   1274 O  O   . LYS   B 2 133 ? -25.817 -10.423 -28.722 1.00 65.45  ? 142 LYS   B O   1 
ATOM   1275 C  CB  . LYS   B 2 133 ? -23.502 -12.575 -28.465 1.00 68.36  ? 142 LYS   B CB  1 
ATOM   1276 C  CG  . LYS   B 2 133 ? -22.250 -12.684 -29.342 1.00 74.76  ? 142 LYS   B CG  1 
ATOM   1277 C  CD  . LYS   B 2 133 ? -21.071 -13.404 -28.655 1.00 80.84  ? 142 LYS   B CD  1 
ATOM   1278 C  CE  . LYS   B 2 133 ? -19.869 -13.432 -29.581 1.00 85.88  ? 142 LYS   B CE  1 
ATOM   1279 N  NZ  . LYS   B 2 133 ? -19.004 -14.628 -29.374 1.00 88.98  ? 142 LYS   B NZ  1 
ATOM   1280 N  N   . CYS   B 2 134 ? -25.811 -11.007 -26.538 1.00 64.94  ? 143 CYS   B N   1 
ATOM   1281 C  CA  . CYS   B 2 134 ? -27.233 -10.676 -26.327 1.00 65.21  ? 143 CYS   B CA  1 
ATOM   1282 C  C   . CYS   B 2 134 ? -27.479 -9.247  -25.847 1.00 64.02  ? 143 CYS   B C   1 
ATOM   1283 O  O   . CYS   B 2 134 ? -28.618 -8.910  -25.521 1.00 64.14  ? 143 CYS   B O   1 
ATOM   1284 C  CB  . CYS   B 2 134 ? -27.890 -11.669 -25.377 1.00 67.27  ? 143 CYS   B CB  1 
ATOM   1285 S  SG  . CYS   B 2 134 ? -27.585 -13.398 -25.787 1.00 74.07  ? 143 CYS   B SG  1 
ATOM   1286 N  N   . GLY   B 2 135 ? -26.424 -8.443  -25.760 1.00 62.62  ? 144 GLY   B N   1 
ATOM   1287 C  CA  . GLY   B 2 135 ? -26.497 -7.080  -25.254 1.00 61.43  ? 144 GLY   B CA  1 
ATOM   1288 C  C   . GLY   B 2 135 ? -26.560 -7.004  -23.740 1.00 59.40  ? 144 GLY   B C   1 
ATOM   1289 O  O   . GLY   B 2 135 ? -26.889 -5.951  -23.193 1.00 59.73  ? 144 GLY   B O   1 
ATOM   1290 N  N   . ARG   B 2 136 ? -26.251 -8.114  -23.047 1.00 57.26  ? 145 ARG   B N   1 
ATOM   1291 C  CA  . ARG   B 2 136 ? -26.262 -8.159  -21.590 1.00 55.78  ? 145 ARG   B CA  1 
ATOM   1292 C  C   . ARG   B 2 136 ? -24.965 -7.604  -21.013 1.00 53.62  ? 145 ARG   B C   1 
ATOM   1293 O  O   . ARG   B 2 136 ? -23.892 -7.858  -21.561 1.00 53.42  ? 145 ARG   B O   1 
ATOM   1294 C  CB  . ARG   B 2 136 ? -26.534 -9.579  -21.096 1.00 57.23  ? 145 ARG   B CB  1 
ATOM   1295 C  CG  . ARG   B 2 136 ? -27.958 -10.011 -21.367 1.00 61.45  ? 145 ARG   B CG  1 
ATOM   1296 C  CD  . ARG   B 2 136 ? -28.258 -11.343 -20.727 1.00 66.87  ? 145 ARG   B CD  1 
ATOM   1297 N  NE  . ARG   B 2 136 ? -27.505 -12.416 -21.371 1.00 72.23  ? 145 ARG   B NE  1 
ATOM   1298 C  CZ  . ARG   B 2 136 ? -26.857 -13.378 -20.720 1.00 76.39  ? 145 ARG   B CZ  1 
ATOM   1299 N  NH1 . ARG   B 2 136 ? -26.849 -13.403 -19.390 1.00 76.42  ? 145 ARG   B NH1 1 
ATOM   1300 N  NH2 . ARG   B 2 136 ? -26.191 -14.309 -21.392 1.00 77.39  ? 145 ARG   B NH2 1 
ATOM   1301 N  N   . VAL   B 2 137 ? -25.065 -6.807  -19.935 1.00 51.64  ? 146 VAL   B N   1 
ATOM   1302 C  CA  . VAL   B 2 137 ? -23.881 -6.203  -19.337 1.00 50.11  ? 146 VAL   B CA  1 
ATOM   1303 C  C   . VAL   B 2 137 ? -23.135 -7.218  -18.494 1.00 48.82  ? 146 VAL   B C   1 
ATOM   1304 O  O   . VAL   B 2 137 ? -23.635 -7.649  -17.459 1.00 48.83  ? 146 VAL   B O   1 
ATOM   1305 C  CB  . VAL   B 2 137 ? -24.201 -4.929  -18.538 1.00 50.20  ? 146 VAL   B CB  1 
ATOM   1306 C  CG1 . VAL   B 2 137 ? -22.921 -4.242  -18.090 1.00 50.27  ? 146 VAL   B CG1 1 
ATOM   1307 C  CG2 . VAL   B 2 137 ? -25.072 -3.979  -19.350 1.00 50.90  ? 146 VAL   B CG2 1 
ATOM   1308 N  N   . ILE   B 2 138 ? -21.942 -7.609  -18.949 1.00 47.41  ? 147 ILE   B N   1 
ATOM   1309 C  CA  . ILE   B 2 138 ? -21.113 -8.591  -18.256 1.00 46.50  ? 147 ILE   B CA  1 
ATOM   1310 C  C   . ILE   B 2 138 ? -20.092 -7.947  -17.279 1.00 46.09  ? 147 ILE   B C   1 
ATOM   1311 O  O   . ILE   B 2 138 ? -19.465 -8.669  -16.512 1.00 46.30  ? 147 ILE   B O   1 
ATOM   1312 C  CB  . ILE   B 2 138 ? -20.431 -9.558  -19.274 1.00 46.07  ? 147 ILE   B CB  1 
ATOM   1313 C  CG1 . ILE   B 2 138 ? -19.639 -8.778  -20.331 1.00 46.34  ? 147 ILE   B CG1 1 
ATOM   1314 C  CG2 . ILE   B 2 138 ? -21.455 -10.472 -19.941 1.00 46.21  ? 147 ILE   B CG2 1 
ATOM   1315 C  CD1 . ILE   B 2 138 ? -18.721 -9.596  -21.111 1.00 47.06  ? 147 ILE   B CD1 1 
ATOM   1316 N  N   . GLY   B 2 139 ? -19.959 -6.621  -17.289 1.00 45.36  ? 148 GLY   B N   1 
ATOM   1317 C  CA  . GLY   B 2 139 ? -19.043 -5.908  -16.405 1.00 45.34  ? 148 GLY   B CA  1 
ATOM   1318 C  C   . GLY   B 2 139 ? -18.835 -4.457  -16.793 1.00 45.73  ? 148 GLY   B C   1 
ATOM   1319 O  O   . GLY   B 2 139 ? -19.353 -4.014  -17.819 1.00 45.79  ? 148 GLY   B O   1 
ATOM   1320 N  N   . LEU   B 2 140 ? -18.070 -3.692  -15.987 1.00 45.82  ? 149 LEU   B N   1 
ATOM   1321 C  CA  . LEU   B 2 140 ? -17.780 -2.282  -16.280 1.00 46.14  ? 149 LEU   B CA  1 
ATOM   1322 C  C   . LEU   B 2 140 ? -16.293 -2.079  -16.514 1.00 46.45  ? 149 LEU   B C   1 
ATOM   1323 O  O   . LEU   B 2 140 ? -15.465 -2.718  -15.867 1.00 46.63  ? 149 LEU   B O   1 
ATOM   1324 C  CB  . LEU   B 2 140 ? -18.267 -1.329  -15.174 1.00 46.46  ? 149 LEU   B CB  1 
ATOM   1325 C  CG  . LEU   B 2 140 ? -19.744 -1.393  -14.785 1.00 47.99  ? 149 LEU   B CG  1 
ATOM   1326 C  CD1 . LEU   B 2 140 ? -20.063 -0.377  -13.694 1.00 48.25  ? 149 LEU   B CD1 1 
ATOM   1327 C  CD2 . LEU   B 2 140 ? -20.652 -1.184  -15.992 1.00 48.90  ? 149 LEU   B CD2 1 
ATOM   1328 N  N   . TYR   B 2 141 ? -15.967 -1.180  -17.438 1.00 46.56  ? 150 TYR   B N   1 
ATOM   1329 C  CA  . TYR   B 2 141 ? -14.618 -0.854  -17.880 1.00 47.42  ? 150 TYR   B CA  1 
ATOM   1330 C  C   . TYR   B 2 141 ? -14.120 0.362   -17.116 1.00 47.01  ? 150 TYR   B C   1 
ATOM   1331 O  O   . TYR   B 2 141 ? -14.851 1.319   -17.019 1.00 46.78  ? 150 TYR   B O   1 
ATOM   1332 C  CB  . TYR   B 2 141 ? -14.686 -0.569  -19.404 1.00 48.44  ? 150 TYR   B CB  1 
ATOM   1333 C  CG  . TYR   B 2 141 ? -13.483 0.111   -20.032 1.00 50.28  ? 150 TYR   B CG  1 
ATOM   1334 C  CD1 . TYR   B 2 141 ? -13.456 1.488   -20.224 1.00 51.45  ? 150 TYR   B CD1 1 
ATOM   1335 C  CD2 . TYR   B 2 141 ? -12.422 -0.633  -20.532 1.00 51.60  ? 150 TYR   B CD2 1 
ATOM   1336 C  CE1 . TYR   B 2 141 ? -12.365 2.113   -20.820 1.00 52.55  ? 150 TYR   B CE1 1 
ATOM   1337 C  CE2 . TYR   B 2 141 ? -11.334 -0.022  -21.146 1.00 52.61  ? 150 TYR   B CE2 1 
ATOM   1338 C  CZ  . TYR   B 2 141 ? -11.312 1.351   -21.295 1.00 53.52  ? 150 TYR   B CZ  1 
ATOM   1339 O  OH  . TYR   B 2 141 ? -10.230 1.955   -21.891 1.00 55.00  ? 150 TYR   B OH  1 
ATOM   1340 N  N   . GLY   B 2 142 ? -12.896 0.333   -16.593 1.00 47.10  ? 151 GLY   B N   1 
ATOM   1341 C  CA  . GLY   B 2 142 ? -12.350 1.477   -15.865 1.00 47.65  ? 151 GLY   B CA  1 
ATOM   1342 C  C   . GLY   B 2 142 ? -11.380 1.170   -14.739 1.00 48.00  ? 151 GLY   B C   1 
ATOM   1343 O  O   . GLY   B 2 142 ? -10.717 2.081   -14.236 1.00 47.92  ? 151 GLY   B O   1 
ATOM   1344 N  N   . ASN   B 2 143 ? -11.285 -0.100  -14.321 1.00 48.12  ? 152 ASN   B N   1 
ATOM   1345 C  CA  . ASN   B 2 143 ? -10.341 -0.484  -13.274 1.00 49.09  ? 152 ASN   B CA  1 
ATOM   1346 C  C   . ASN   B 2 143 ? -9.418  -1.581  -13.773 1.00 50.33  ? 152 ASN   B C   1 
ATOM   1347 O  O   . ASN   B 2 143 ? -9.853  -2.703  -14.017 1.00 50.83  ? 152 ASN   B O   1 
ATOM   1348 C  CB  . ASN   B 2 143 ? -11.052 -0.923  -11.997 1.00 49.95  ? 152 ASN   B CB  1 
ATOM   1349 C  CG  . ASN   B 2 143 ? -10.107 -1.106  -10.827 1.00 52.06  ? 152 ASN   B CG  1 
ATOM   1350 O  OD1 . ASN   B 2 143 ? -9.004  -0.535  -10.797 1.00 52.75  ? 152 ASN   B OD1 1 
ATOM   1351 N  ND2 . ASN   B 2 143 ? -10.521 -1.907  -9.832  1.00 51.88  ? 152 ASN   B ND2 1 
ATOM   1352 N  N   . GLY   B 2 144 ? -8.148  -1.257  -13.901 1.00 50.79  ? 153 GLY   B N   1 
ATOM   1353 C  CA  . GLY   B 2 144 ? -7.173  -2.212  -14.384 1.00 52.16  ? 153 GLY   B CA  1 
ATOM   1354 C  C   . GLY   B 2 144 ? -5.747  -1.811  -14.120 1.00 53.93  ? 153 GLY   B C   1 
ATOM   1355 O  O   . GLY   B 2 144 ? -5.425  -1.285  -13.051 1.00 54.20  ? 153 GLY   B O   1 
ATOM   1356 N  N   . VAL   B 2 145 ? -4.891  -2.040  -15.112 1.00 55.10  ? 154 VAL   B N   1 
ATOM   1357 C  CA  . VAL   B 2 145 ? -3.462  -1.831  -14.981 1.00 56.89  ? 154 VAL   B CA  1 
ATOM   1358 C  C   . VAL   B 2 145 ? -2.801  -1.178  -16.235 1.00 58.99  ? 154 VAL   B C   1 
ATOM   1359 O  O   . VAL   B 2 145 ? -3.384  -1.161  -17.319 1.00 59.37  ? 154 VAL   B O   1 
ATOM   1360 C  CB  . VAL   B 2 145 ? -2.857  -3.218  -14.634 1.00 57.17  ? 154 VAL   B CB  1 
ATOM   1361 C  CG1 . VAL   B 2 145 ? -2.652  -4.066  -15.881 1.00 57.30  ? 154 VAL   B CG1 1 
ATOM   1362 C  CG2 . VAL   B 2 145 ? -1.576  -3.087  -13.836 1.00 58.08  ? 154 VAL   B CG2 1 
ATOM   1363 N  N   . VAL   B 2 146 ? -1.604  -0.606  -16.067 1.00 60.28  ? 155 VAL   B N   1 
ATOM   1364 C  CA  . VAL   B 2 146 ? -0.856  0.001   -17.164 1.00 62.33  ? 155 VAL   B CA  1 
ATOM   1365 C  C   . VAL   B 2 146 ? 0.319   -0.922  -17.487 1.00 65.08  ? 155 VAL   B C   1 
ATOM   1366 O  O   . VAL   B 2 146 ? 1.068   -1.300  -16.584 1.00 65.27  ? 155 VAL   B O   1 
ATOM   1367 C  CB  . VAL   B 2 146 ? -0.404  1.435   -16.823 1.00 62.57  ? 155 VAL   B CB  1 
ATOM   1368 C  CG1 . VAL   B 2 146 ? 0.348   2.054   -17.984 1.00 62.85  ? 155 VAL   B CG1 1 
ATOM   1369 C  CG2 . VAL   B 2 146 ? -1.602  2.299   -16.442 1.00 62.98  ? 155 VAL   B CG2 1 
ATOM   1370 N  N   . ILE   B 2 147 ? 0.433   -1.353  -18.751 1.00 67.10  ? 156 ILE   B N   1 
ATOM   1371 C  CA  . ILE   B 2 147 ? 1.466   -2.297  -19.179 1.00 69.92  ? 156 ILE   B CA  1 
ATOM   1372 C  C   . ILE   B 2 147 ? 2.784   -1.602  -19.634 1.00 72.12  ? 156 ILE   B C   1 
ATOM   1373 O  O   . ILE   B 2 147 ? 2.845   -0.374  -19.640 1.00 72.41  ? 156 ILE   B O   1 
ATOM   1374 C  CB  . ILE   B 2 147 ? 0.874   -3.251  -20.257 1.00 71.25  ? 156 ILE   B CB  1 
ATOM   1375 C  CG1 . ILE   B 2 147 ? 0.204   -2.470  -21.407 1.00 72.74  ? 156 ILE   B CG1 1 
ATOM   1376 C  CG2 . ILE   B 2 147 ? -0.081  -4.265  -19.626 1.00 71.81  ? 156 ILE   B CG2 1 
ATOM   1377 C  CD1 . ILE   B 2 147 ? -0.219  -3.330  -22.584 1.00 74.21  ? 156 ILE   B CD1 1 
ATOM   1378 N  N   . LYS   B 2 148 ? 3.841   -2.389  -19.970 1.00 73.52  ? 157 LYS   B N   1 
ATOM   1379 C  CA  . LYS   B 2 148 ? 5.166   -1.911  -20.411 1.00 75.29  ? 157 LYS   B CA  1 
ATOM   1380 C  C   . LYS   B 2 148 ? 5.126   -0.759  -21.445 1.00 76.76  ? 157 LYS   B C   1 
ATOM   1381 O  O   . LYS   B 2 148 ? 5.906   0.198   -21.361 1.00 77.18  ? 157 LYS   B O   1 
ATOM   1382 C  CB  . LYS   B 2 148 ? 6.003   -3.076  -20.974 1.00 77.12  ? 157 LYS   B CB  1 
ATOM   1383 C  CG  . LYS   B 2 148 ? 5.988   -4.327  -20.104 1.00 81.32  ? 157 LYS   B CG  1 
ATOM   1384 C  CD  . LYS   B 2 148 ? 7.094   -5.313  -20.497 1.00 85.83  ? 157 LYS   B CD  1 
ATOM   1385 C  CE  . LYS   B 2 148 ? 8.437   -4.979  -19.878 1.00 89.52  ? 157 LYS   B CE  1 
ATOM   1386 N  NZ  . LYS   B 2 148 ? 8.434   -5.143  -18.394 1.00 91.60  ? 157 LYS   B NZ  1 
ATOM   1387 N  N   . ASN   B 2 149 ? 4.221   -0.857  -22.419 1.00 76.95  ? 158 ASN   B N   1 
ATOM   1388 C  CA  . ASN   B 2 149 ? 4.086   0.149   -23.469 1.00 77.52  ? 158 ASN   B CA  1 
ATOM   1389 C  C   . ASN   B 2 149 ? 3.122   1.298   -23.118 1.00 76.96  ? 158 ASN   B C   1 
ATOM   1390 O  O   . ASN   B 2 149 ? 2.606   1.959   -24.022 1.00 77.42  ? 158 ASN   B O   1 
ATOM   1391 C  CB  . ASN   B 2 149 ? 3.705   -0.493  -24.819 1.00 79.75  ? 158 ASN   B CB  1 
ATOM   1392 C  CG  . ASN   B 2 149 ? 2.879   -1.763  -24.727 1.00 84.08  ? 158 ASN   B CG  1 
ATOM   1393 O  OD1 . ASN   B 2 149 ? 3.390   -2.836  -24.377 1.00 85.10  ? 158 ASN   B OD1 1 
ATOM   1394 N  ND2 . ASN   B 2 149 ? 1.589   -1.664  -25.038 1.00 85.34  ? 158 ASN   B ND2 1 
ATOM   1395 N  N   . GLY   B 2 150 ? 2.903   1.531   -21.825 1.00 75.60  ? 159 GLY   B N   1 
ATOM   1396 C  CA  . GLY   B 2 150 ? 2.043   2.603   -21.338 1.00 74.85  ? 159 GLY   B CA  1 
ATOM   1397 C  C   . GLY   B 2 150 ? 0.561   2.426   -21.607 1.00 73.76  ? 159 GLY   B C   1 
ATOM   1398 O  O   . GLY   B 2 150 ? -0.246  3.248   -21.166 1.00 73.71  ? 159 GLY   B O   1 
ATOM   1399 N  N   . SER   B 2 151 ? 0.186   1.352   -22.333 1.00 72.50  ? 160 SER   B N   1 
ATOM   1400 C  CA  A SER   B 2 151 ? -1.214  1.085   -22.659 0.50 72.04  ? 160 SER   B CA  1 
ATOM   1401 C  CA  B SER   B 2 151 ? -1.210  1.080   -22.665 0.50 72.19  ? 160 SER   B CA  1 
ATOM   1402 C  C   . SER   B 2 151 ? -2.031  0.671   -21.434 1.00 71.12  ? 160 SER   B C   1 
ATOM   1403 O  O   . SER   B 2 151 ? -1.467  0.274   -20.417 1.00 70.63  ? 160 SER   B O   1 
ATOM   1404 C  CB  A SER   B 2 151 ? -1.322  0.033   -23.760 0.50 73.34  ? 160 SER   B CB  1 
ATOM   1405 C  CB  B SER   B 2 151 ? -1.305  0.017   -23.757 0.50 73.92  ? 160 SER   B CB  1 
ATOM   1406 O  OG  A SER   B 2 151 ? -2.677  -0.273  -24.048 0.50 75.31  ? 160 SER   B OG  1 
ATOM   1407 O  OG  B SER   B 2 151 ? -0.519  0.347   -24.892 0.50 76.59  ? 160 SER   B OG  1 
ATOM   1408 N  N   . TYR   B 2 152 ? -3.368  0.788   -21.527 1.00 69.46  ? 161 TYR   B N   1 
ATOM   1409 C  CA  . TYR   B 2 152 ? -4.270  0.445   -20.442 1.00 68.11  ? 161 TYR   B CA  1 
ATOM   1410 C  C   . TYR   B 2 152 ? -5.009  -0.848  -20.706 1.00 66.10  ? 161 TYR   B C   1 
ATOM   1411 O  O   . TYR   B 2 152 ? -5.593  -1.022  -21.771 1.00 66.35  ? 161 TYR   B O   1 
ATOM   1412 C  CB  . TYR   B 2 152 ? -5.306  1.556   -20.218 1.00 68.41  ? 161 TYR   B CB  1 
ATOM   1413 C  CG  . TYR   B 2 152 ? -5.930  1.500   -18.839 1.00 69.38  ? 161 TYR   B CG  1 
ATOM   1414 C  CD1 . TYR   B 2 152 ? -5.178  1.761   -17.704 1.00 70.29  ? 161 TYR   B CD1 1 
ATOM   1415 C  CD2 . TYR   B 2 152 ? -7.267  1.168   -18.670 1.00 70.18  ? 161 TYR   B CD2 1 
ATOM   1416 C  CE1 . TYR   B 2 152 ? -5.737  1.698   -16.436 1.00 71.22  ? 161 TYR   B CE1 1 
ATOM   1417 C  CE2 . TYR   B 2 152 ? -7.841  1.107   -17.402 1.00 71.02  ? 161 TYR   B CE2 1 
ATOM   1418 C  CZ  . TYR   B 2 152 ? -7.071  1.377   -16.286 1.00 71.88  ? 161 TYR   B CZ  1 
ATOM   1419 O  OH  . TYR   B 2 152 ? -7.608  1.348   -15.020 1.00 73.17  ? 161 TYR   B OH  1 
ATOM   1420 N  N   . VAL   B 2 153 ? -5.016  -1.745  -19.723 1.00 63.73  ? 162 VAL   B N   1 
ATOM   1421 C  CA  . VAL   B 2 153 ? -5.769  -2.983  -19.820 1.00 61.85  ? 162 VAL   B CA  1 
ATOM   1422 C  C   . VAL   B 2 153 ? -6.687  -3.008  -18.614 1.00 59.42  ? 162 VAL   B C   1 
ATOM   1423 O  O   . VAL   B 2 153 ? -6.224  -2.974  -17.486 1.00 59.18  ? 162 VAL   B O   1 
ATOM   1424 C  CB  . VAL   B 2 153 ? -4.866  -4.233  -19.924 1.00 62.69  ? 162 VAL   B CB  1 
ATOM   1425 C  CG1 . VAL   B 2 153 ? -5.672  -5.516  -19.725 1.00 63.00  ? 162 VAL   B CG1 1 
ATOM   1426 C  CG2 . VAL   B 2 153 ? -4.130  -4.254  -21.265 1.00 63.28  ? 162 VAL   B CG2 1 
ATOM   1427 N  N   . SER   B 2 154 ? -7.984  -2.955  -18.851 1.00 57.71  ? 163 SER   B N   1 
ATOM   1428 C  CA  . SER   B 2 154 ? -8.977  -2.929  -17.784 1.00 56.47  ? 163 SER   B CA  1 
ATOM   1429 C  C   . SER   B 2 154 ? -9.541  -4.312  -17.525 1.00 55.19  ? 163 SER   B C   1 
ATOM   1430 O  O   . SER   B 2 154 ? -9.589  -5.130  -18.424 1.00 55.27  ? 163 SER   B O   1 
ATOM   1431 C  CB  . SER   B 2 154 ? -10.108 -1.963  -18.148 1.00 56.84  ? 163 SER   B CB  1 
ATOM   1432 O  OG  . SER   B 2 154 ? -11.314 -2.188  -17.433 1.00 58.00  ? 163 SER   B OG  1 
ATOM   1433 N  N   . ALA   B 2 155 ? -10.017 -4.550  -16.319 1.00 54.09  ? 164 ALA   B N   1 
ATOM   1434 C  CA  . ALA   B 2 155 ? -10.682 -5.799  -15.992 1.00 53.54  ? 164 ALA   B CA  1 
ATOM   1435 C  C   . ALA   B 2 155 ? -12.174 -5.700  -16.414 1.00 53.18  ? 164 ALA   B C   1 
ATOM   1436 O  O   . ALA   B 2 155 ? -12.700 -4.601  -16.652 1.00 52.58  ? 164 ALA   B O   1 
ATOM   1437 C  CB  . ALA   B 2 155 ? -10.581 -6.043  -14.496 1.00 53.35  ? 164 ALA   B CB  1 
ATOM   1438 N  N   . ILE   B 2 156 ? -12.850 -6.851  -16.524 1.00 53.18  ? 165 ILE   B N   1 
ATOM   1439 C  CA  . ILE   B 2 156 ? -14.288 -6.870  -16.772 1.00 53.41  ? 165 ILE   B CA  1 
ATOM   1440 C  C   . ILE   B 2 156 ? -14.864 -7.013  -15.362 1.00 53.29  ? 165 ILE   B C   1 
ATOM   1441 O  O   . ILE   B 2 156 ? -14.985 -8.137  -14.844 1.00 53.30  ? 165 ILE   B O   1 
ATOM   1442 C  CB  . ILE   B 2 156 ? -14.711 -8.033  -17.692 1.00 54.01  ? 165 ILE   B CB  1 
ATOM   1443 C  CG1 . ILE   B 2 156 ? -13.932 -7.976  -19.023 1.00 55.14  ? 165 ILE   B CG1 1 
ATOM   1444 C  CG2 . ILE   B 2 156 ? -16.236 -8.012  -17.912 1.00 54.32  ? 165 ILE   B CG2 1 
ATOM   1445 C  CD1 . ILE   B 2 156 ? -14.153 -9.122  -19.924 1.00 56.41  ? 165 ILE   B CD1 1 
ATOM   1446 N  N   . THR   B 2 157 ? -15.091 -5.852  -14.703 1.00 52.70  ? 166 THR   B N   1 
ATOM   1447 C  CA  . THR   B 2 157 ? -15.550 -5.759  -13.318 1.00 52.46  ? 166 THR   B CA  1 
ATOM   1448 C  C   . THR   B 2 157 ? -17.047 -5.949  -13.179 1.00 52.61  ? 166 THR   B C   1 
ATOM   1449 O  O   . THR   B 2 157 ? -17.816 -5.060  -13.542 1.00 52.48  ? 166 THR   B O   1 
ATOM   1450 C  CB  . THR   B 2 157 ? -15.113 -4.425  -12.706 1.00 52.91  ? 166 THR   B CB  1 
ATOM   1451 O  OG1 . THR   B 2 157 ? -13.712 -4.252  -12.895 1.00 53.84  ? 166 THR   B OG1 1 
ATOM   1452 C  CG2 . THR   B 2 157 ? -15.421 -4.336  -11.249 1.00 52.81  ? 166 THR   B CG2 1 
ATOM   1453 N  N   . GLN   B 2 158 ? -17.466 -7.089  -12.630 1.00 52.56  ? 167 GLN   B N   1 
ATOM   1454 C  CA  . GLN   B 2 158 ? -18.883 -7.358  -12.428 1.00 52.95  ? 167 GLN   B CA  1 
ATOM   1455 C  C   . GLN   B 2 158 ? -19.199 -7.417  -10.915 1.00 54.77  ? 167 GLN   B C   1 
ATOM   1456 O  O   . GLN   B 2 158 ? -18.340 -7.786  -10.109 1.00 54.78  ? 167 GLN   B O   1 
ATOM   1457 C  CB  . GLN   B 2 158 ? -19.277 -8.660  -13.167 1.00 52.58  ? 167 GLN   B CB  1 
ATOM   1458 C  CG  . GLN   B 2 158 ? -20.756 -9.061  -13.138 1.00 53.36  ? 167 GLN   B CG  1 
ATOM   1459 C  CD  . GLN   B 2 158 ? -21.723 -8.045  -13.718 1.00 55.51  ? 167 GLN   B CD  1 
ATOM   1460 O  OE1 . GLN   B 2 158 ? -21.860 -6.919  -13.229 1.00 57.25  ? 167 GLN   B OE1 1 
ATOM   1461 N  NE2 . GLN   B 2 158 ? -22.470 -8.438  -14.718 1.00 54.48  ? 167 GLN   B NE2 1 
ATOM   1462 N  N   . GLY   B 2 159 ? -20.407 -7.011  -10.547 1.00 55.88  ? 168 GLY   B N   1 
ATOM   1463 C  CA  . GLY   B 2 159 ? -20.864 -7.066  -9.172  1.00 57.78  ? 168 GLY   B CA  1 
ATOM   1464 C  C   . GLY   B 2 159 ? -21.668 -8.314  -8.880  1.00 60.06  ? 168 GLY   B C   1 
ATOM   1465 O  O   . GLY   B 2 159 ? -21.953 -9.106  -9.779  1.00 60.26  ? 168 GLY   B O   1 
ATOM   1466 N  N   . LYS   B 2 160 ? -22.041 -8.509  -7.613  1.00 61.96  ? 169 LYS   B N   1 
ATOM   1467 C  CA  . LYS   B 2 160 ? -22.839 -9.672  -7.223  1.00 64.03  ? 169 LYS   B CA  1 
ATOM   1468 C  C   . LYS   B 2 160 ? -24.316 -9.291  -7.030  1.00 65.84  ? 169 LYS   B C   1 
ATOM   1469 O  O   . LYS   B 2 160 ? -24.635 -8.367  -6.273  1.00 66.18  ? 169 LYS   B O   1 
ATOM   1470 C  CB  . LYS   B 2 160 ? -22.278 -10.339 -5.952  1.00 65.99  ? 169 LYS   B CB  1 
ATOM   1471 C  CG  . LYS   B 2 160 ? -22.987 -11.639 -5.615  1.00 70.70  ? 169 LYS   B CG  1 
ATOM   1472 C  CD  . LYS   B 2 160 ? -22.972 -11.949 -4.129  1.00 76.18  ? 169 LYS   B CD  1 
ATOM   1473 C  CE  . LYS   B 2 160 ? -23.764 -13.199 -3.818  1.00 80.57  ? 169 LYS   B CE  1 
ATOM   1474 N  NZ  . LYS   B 2 160 ? -23.630 -13.595 -2.388  1.00 83.57  ? 169 LYS   B NZ  1 
ATOM   1475 N  N   . ARG   B 2 161 ? -25.212 -9.990  -7.733  1.00 66.67  ? 170 ARG   B N   1 
ATOM   1476 C  CA  . ARG   B 2 161 ? -26.644 -9.749  -7.600  1.00 67.75  ? 170 ARG   B CA  1 
ATOM   1477 C  C   . ARG   B 2 161 ? -27.147 -10.650 -6.465  1.00 69.19  ? 170 ARG   B C   1 
ATOM   1478 O  O   . ARG   B 2 161 ? -26.981 -11.866 -6.530  1.00 69.35  ? 170 ARG   B O   1 
ATOM   1479 C  CB  . ARG   B 2 161 ? -27.369 -10.071 -8.924  1.00 68.46  ? 170 ARG   B CB  1 
ATOM   1480 C  CG  . ARG   B 2 161 ? -28.795 -9.568  -8.967  1.00 70.32  ? 170 ARG   B CG  1 
ATOM   1481 C  CD  . ARG   B 2 161 ? -29.596 -10.103 -10.137 1.00 72.78  ? 170 ARG   B CD  1 
ATOM   1482 N  NE  . ARG   B 2 161 ? -31.032 -9.878  -9.931  1.00 74.90  ? 170 ARG   B NE  1 
ATOM   1483 C  CZ  . ARG   B 2 161 ? -31.767 -9.012  -10.622 1.00 75.98  ? 170 ARG   B CZ  1 
ATOM   1484 N  NH1 . ARG   B 2 161 ? -31.224 -8.304  -11.604 1.00 74.52  ? 170 ARG   B NH1 1 
ATOM   1485 N  NH2 . ARG   B 2 161 ? -33.053 -8.854  -10.343 1.00 75.94  ? 170 ARG   B NH2 1 
ATOM   1486 N  N   . GLU   B 2 162 ? -27.708 -10.062 -5.406  1.00 70.17  ? 171 GLU   B N   1 
ATOM   1487 C  CA  . GLU   B 2 162 ? -28.209 -10.826 -4.261  1.00 71.61  ? 171 GLU   B CA  1 
ATOM   1488 C  C   . GLU   B 2 162 ? -29.580 -11.446 -4.558  1.00 71.84  ? 171 GLU   B C   1 
ATOM   1489 O  O   . GLU   B 2 162 ? -30.299 -11.839 -3.639  1.00 72.01  ? 171 GLU   B O   1 
ATOM   1490 C  CB  . GLU   B 2 162 ? -28.291 -9.934  -3.008  1.00 75.42  ? 171 GLU   B CB  1 
ATOM   1491 C  CG  . GLU   B 2 162 ? -27.023 -9.148  -2.711  1.00 82.96  ? 171 GLU   B CG  1 
ATOM   1492 C  CD  . GLU   B 2 162 ? -25.913 -9.945  -2.053  1.00 93.59  ? 171 GLU   B CD  1 
ATOM   1493 O  OE1 . GLU   B 2 162 ? -24.739 -9.520  -2.158  1.00 96.00  ? 171 GLU   B OE1 1 
ATOM   1494 O  OE2 . GLU   B 2 162 ? -26.215 -10.991 -1.432  1.00 97.06  ? 171 GLU   B OE2 1 
HETATM 1495 S  S   . DMS   C 3 .   ? -18.691 11.812  -0.342  1.00 83.75  ? 201 DMS   B S   1 
HETATM 1496 O  O   . DMS   C 3 .   ? -19.453 10.516  -0.395  1.00 83.69  ? 201 DMS   B O   1 
HETATM 1497 C  C1  . DMS   C 3 .   ? -19.748 13.146  -0.957  1.00 83.88  ? 201 DMS   B C1  1 
HETATM 1498 C  C2  . DMS   C 3 .   ? -17.566 11.899  -1.764  1.00 83.60  ? 201 DMS   B C2  1 
HETATM 1499 N  N1  . A1B9G D 4 .   ? -9.033  4.356   -13.575 1.00 55.56  ? 202 A1B9G B N1  1 
HETATM 1500 N  N3  . A1B9G D 4 .   ? -6.183  5.034   -18.688 1.00 59.60  ? 202 A1B9G B N3  1 
HETATM 1501 C  C4  . A1B9G D 4 .   ? -8.822  5.708   -10.135 1.00 53.72  ? 202 A1B9G B C4  1 
HETATM 1502 C  C5  . A1B9G D 4 .   ? -9.109  4.581   -9.384  1.00 53.52  ? 202 A1B9G B C5  1 
HETATM 1503 C  C6  . A1B9G D 4 .   ? -9.467  3.383   -10.006 1.00 53.52  ? 202 A1B9G B C6  1 
HETATM 1504 C  C7  . A1B9G D 4 .   ? -9.433  3.322   -11.395 1.00 53.98  ? 202 A1B9G B C7  1 
HETATM 1505 C  C8  . A1B9G D 4 .   ? -9.863  2.187   -9.178  1.00 53.09  ? 202 A1B9G B C8  1 
HETATM 1506 C  C10 . A1B9G D 4 .   ? -8.245  3.886   -7.243  1.00 53.14  ? 202 A1B9G B C10 1 
HETATM 1507 C  C13 . A1B9G D 4 .   ? -9.689  4.354   -17.803 1.00 59.09  ? 202 A1B9G B C13 1 
HETATM 1508 C  C15 . A1B9G D 4 .   ? -7.397  4.847   -18.124 1.00 59.20  ? 202 A1B9G B C15 1 
HETATM 1509 C  C17 . A1B9G D 4 .   ? -7.237  5.033   -16.738 1.00 59.02  ? 202 A1B9G B C17 1 
HETATM 1510 O  O1  . A1B9G D 4 .   ? -7.337  5.819   -13.937 1.00 57.25  ? 202 A1B9G B O1  1 
HETATM 1511 C  C1  . A1B9G D 4 .   ? -8.212  5.074   -14.377 1.00 57.07  ? 202 A1B9G B C1  1 
HETATM 1512 C  C2  . A1B9G D 4 .   ? -9.113  4.443   -12.158 1.00 54.57  ? 202 A1B9G B C2  1 
HETATM 1513 C  C3  . A1B9G D 4 .   ? -8.764  5.621   -11.510 1.00 54.13  ? 202 A1B9G B C3  1 
HETATM 1514 N  N2  . A1B9G D 4 .   ? -8.820  1.711   -8.282  1.00 53.16  ? 202 A1B9G B N2  1 
HETATM 1515 C  C9  . A1B9G D 4 .   ? -8.732  2.471   -7.033  1.00 53.12  ? 202 A1B9G B C9  1 
HETATM 1516 O  O2  . A1B9G D 4 .   ? -9.214  4.597   -8.019  1.00 53.31  ? 202 A1B9G B O2  1 
HETATM 1517 C  C11 . A1B9G D 4 .   ? -8.355  4.886   -15.861 1.00 58.43  ? 202 A1B9G B C11 1 
HETATM 1518 C  C12 . A1B9G D 4 .   ? -9.566  4.516   -16.437 1.00 58.93  ? 202 A1B9G B C12 1 
HETATM 1519 CL CL1 . A1B9G D 4 .   ? -11.248 3.942   -18.473 1.00 59.39  ? 202 A1B9G B CL1 1 
HETATM 1520 C  C14 . A1B9G D 4 .   ? -8.623  4.487   -18.675 1.00 58.94  ? 202 A1B9G B C14 1 
HETATM 1521 N  N4  . A1B9G D 4 .   ? -5.244  5.329   -17.746 1.00 59.64  ? 202 A1B9G B N4  1 
HETATM 1522 C  C16 . A1B9G D 4 .   ? -5.861  5.329   -16.578 1.00 59.31  ? 202 A1B9G B C16 1 
HETATM 1523 O  O   . HOH   E 5 .   ? -1.856  -4.401  -5.823  1.00 47.06  ? 101 HOH   A O   1 
HETATM 1524 O  O   . HOH   E 5 .   ? -26.352 15.814  -5.662  1.00 51.77  ? 102 HOH   A O   1 
HETATM 1525 O  O   . HOH   E 5 .   ? -4.433  -14.767 -25.230 1.00 50.89  ? 103 HOH   A O   1 
HETATM 1526 O  O   . HOH   E 5 .   ? -24.252 9.081   -27.592 1.00 49.68  ? 104 HOH   A O   1 
HETATM 1527 O  O   . HOH   E 5 .   ? -6.840  -9.516  -2.974  1.00 54.26  ? 105 HOH   A O   1 
HETATM 1528 O  O   . HOH   E 5 .   ? -26.667 1.112   -29.517 1.00 58.39  ? 106 HOH   A O   1 
HETATM 1529 O  O   . HOH   E 5 .   ? -26.745 -1.425  -31.971 1.00 56.99  ? 107 HOH   A O   1 
HETATM 1530 O  O   . HOH   E 5 .   ? -28.266 -6.489  -28.094 1.00 67.92  ? 108 HOH   A O   1 
HETATM 1531 O  O   . HOH   E 5 .   ? -3.003  -11.955 -6.851  1.00 46.57  ? 109 HOH   A O   1 
HETATM 1532 O  O   . HOH   E 5 .   ? -4.608  -10.483 -5.412  1.00 44.15  ? 110 HOH   A O   1 
HETATM 1533 O  O   . HOH   E 5 .   ? -28.108 -3.494  -33.467 1.00 59.34  ? 111 HOH   A O   1 
HETATM 1534 O  O   . HOH   F 5 .   ? -6.544  -0.758  -10.788 0.50 22.19  ? 301 HOH   B O   1 
HETATM 1535 O  O   . HOH   F 5 .   ? -17.371 12.662  -5.391  1.00 64.42  ? 302 HOH   B O   1 
HETATM 1536 O  O   . HOH   F 5 .   ? -26.121 -8.063  -16.773 1.00 53.30  ? 303 HOH   B O   1 
HETATM 1537 O  O   . HOH   F 5 .   ? -6.097  2.356   -13.115 1.00 48.97  ? 304 HOH   B O   1 
HETATM 1538 O  O   . HOH   F 5 .   ? -34.094 1.670   -15.306 1.00 51.66  ? 305 HOH   B O   1 
HETATM 1539 O  O   . HOH   F 5 .   ? -12.263 2.110   -5.797  1.00 45.75  ? 306 HOH   B O   1 
HETATM 1540 O  O   . HOH   F 5 .   ? -12.947 -2.455  -14.743 1.00 38.36  ? 307 HOH   B O   1 
HETATM 1541 O  O   . HOH   F 5 .   ? -28.746 -7.405  -5.742  1.00 61.04  ? 308 HOH   B O   1 
HETATM 1542 O  O   . HOH   F 5 .   ? -16.657 25.839  -12.190 1.00 61.84  ? 309 HOH   B O   1 
HETATM 1543 O  O   . HOH   F 5 .   ? -27.940 -6.707  -18.356 1.00 57.34  ? 310 HOH   B O   1 
HETATM 1544 O  O   . HOH   F 5 .   ? -16.268 -14.955 -16.439 1.00 60.08  ? 311 HOH   B O   1 
HETATM 1545 O  O   . HOH   F 5 .   ? -17.864 -11.048 -16.453 1.00 49.28  ? 312 HOH   B O   1 
HETATM 1546 O  O   . HOH   F 5 .   ? -30.114 -5.385  -0.963  1.00 55.75  ? 313 HOH   B O   1 
HETATM 1547 O  O   . HOH   F 5 .   ? -7.152  -10.986 -5.573  1.00 54.83  ? 314 HOH   B O   1 
HETATM 1548 O  O   . HOH   F 5 .   ? -17.725 15.544  -22.041 1.00 58.42  ? 315 HOH   B O   1 
HETATM 1549 O  O   . HOH   F 5 .   ? -15.055 -5.242  1.311   1.00 49.08  ? 316 HOH   B O   1 
HETATM 1550 O  O   . HOH   F 5 .   ? -10.569 11.887  -18.993 1.00 35.94  ? 317 HOH   B O   1 
HETATM 1551 O  O   . HOH   F 5 .   ? -14.672 -12.474 -16.336 1.00 43.81  ? 318 HOH   B O   1 
HETATM 1552 O  O   . HOH   F 5 .   ? -20.747 -14.305 -22.206 1.00 58.60  ? 319 HOH   B O   1 
HETATM 1553 O  O   . HOH   F 5 .   ? -23.935 -15.153 -17.920 1.00 73.34  ? 320 HOH   B O   1 
HETATM 1554 O  O   . HOH   F 5 .   ? -19.895 -6.124  -0.929  1.00 58.59  ? 321 HOH   B O   1 
HETATM 1555 O  O   . HOH   F 5 .   ? -15.701 -14.653 -30.820 1.00 58.63  ? 322 HOH   B O   1 
HETATM 1556 O  O   . HOH   F 5 .   ? -21.290 6.491   -0.000  0.50 40.28  ? 323 HOH   B O   1 
HETATM 1557 O  O   . HOH   F 5 .   ? -30.938 4.696   -2.655  1.00 56.36  ? 324 HOH   B O   1 
HETATM 1558 O  O   . HOH   F 5 .   ? -20.607 24.374  -16.471 1.00 61.54  ? 325 HOH   B O   1 
HETATM 1559 O  O   . HOH   F 5 .   ? -14.344 -6.860  -1.725  1.00 54.48  ? 326 HOH   B O   1 
HETATM 1560 O  O   . HOH   F 5 .   ? -17.471 14.458  -31.258 1.00 53.63  ? 327 HOH   B O   1 
HETATM 1561 O  O   . HOH   F 5 .   ? -9.942  -11.195 -7.771  1.00 64.98  ? 328 HOH   B O   1 
HETATM 1562 O  O   . HOH   F 5 .   ? -2.404  -9.876  -2.974  1.00 54.12  ? 329 HOH   B O   1 
HETATM 1563 O  O   . HOH   F 5 .   ? -25.392 -5.815  -4.150  1.00 52.42  ? 330 HOH   B O   1 
HETATM 1564 O  O   . HOH   F 5 .   ? -14.877 -9.018  -11.540 1.00 53.55  ? 331 HOH   B O   1 
HETATM 1565 O  O   . HOH   F 5 .   ? -20.834 -8.281  -2.485  1.00 63.73  ? 332 HOH   B O   1 
HETATM 1566 O  O   . HOH   F 5 .   ? -21.131 -12.715 -12.954 1.00 50.58  ? 333 HOH   B O   1 
HETATM 1567 O  O   . HOH   F 5 .   ? -1.069  -14.977 -9.854  1.00 45.59  ? 334 HOH   B O   1 
HETATM 1568 O  O   . HOH   F 5 .   ? -18.325 25.935  -14.371 1.00 69.04  ? 335 HOH   B O   1 
HETATM 1569 O  O   . HOH   F 5 .   ? -10.306 22.546  -13.209 1.00 64.59  ? 336 HOH   B O   1 
HETATM 1570 O  O   . HOH   F 5 .   ? -11.705 -13.195 -8.790  1.00 54.41  ? 337 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   ? 1.2301 0.3859 0.8793 0.2152  0.0399  -0.1372 50  ASP   A N   
2    C  CA  . ASP   A 7   ? 1.2090 0.4406 0.8521 0.2478  0.0499  -0.1365 50  ASP   A CA  
3    C  C   . ASP   A 7   ? 1.1636 0.4433 0.8284 0.2471  0.0610  -0.0982 50  ASP   A C   
4    O  O   . ASP   A 7   ? 1.1821 0.4215 0.8456 0.2566  0.0653  -0.0749 50  ASP   A O   
5    C  CB  . ASP   A 7   ? 1.2723 0.4754 0.8867 0.2976  0.0530  -0.1560 50  ASP   A CB  
6    C  CG  . ASP   A 7   ? 1.3379 0.6228 0.9480 0.3251  0.0622  -0.1675 50  ASP   A CG  
7    O  OD1 . ASP   A 7   ? 1.3590 0.6388 0.9432 0.3427  0.0606  -0.2006 50  ASP   A OD1 
8    O  OD2 . ASP   A 7   ? 1.3488 0.7031 0.9810 0.3282  0.0713  -0.1436 50  ASP   A OD2 
9    N  N   . MET   A 8   ? 1.1059 0.4678 0.7861 0.2380  0.0648  -0.0922 51  MET   A N   
10   C  CA  . MET   A 8   ? 1.0670 0.4770 0.7657 0.2353  0.0723  -0.0612 51  MET   A CA  
11   C  C   . MET   A 8   ? 1.0380 0.4844 0.7344 0.2739  0.0781  -0.0544 51  MET   A C   
12   O  O   . MET   A 8   ? 1.0353 0.5042 0.7247 0.2991  0.0800  -0.0740 51  MET   A O   
13   C  CB  . MET   A 8   ? 1.0410 0.5141 0.7588 0.2063  0.0717  -0.0576 51  MET   A CB  
14   C  CG  . MET   A 8   ? 1.0546 0.5037 0.7842 0.1685  0.0647  -0.0596 51  MET   A CG  
15   S  SD  . MET   A 8   ? 1.0357 0.5584 0.7865 0.1419  0.0624  -0.0559 51  MET   A SD  
16   C  CE  . MET   A 8   ? 1.0087 0.4969 0.7772 0.1029  0.0506  -0.0643 51  MET   A CE  
17   N  N   . TYR   A 9   ? 1.0122 0.4669 0.7149 0.2791  0.0808  -0.0264 52  TYR   A N   
18   C  CA  . TYR   A 9   ? 0.9846 0.4756 0.6892 0.3140  0.0816  -0.0177 52  TYR   A CA  
19   C  C   . TYR   A 9   ? 0.9584 0.4925 0.6742 0.3054  0.0814  0.0069  52  TYR   A C   
20   O  O   . TYR   A 9   ? 0.9563 0.4747 0.6719 0.2789  0.0837  0.0227  52  TYR   A O   
21   C  CB  . TYR   A 9   ? 1.0050 0.4339 0.6895 0.3492  0.0800  -0.0141 52  TYR   A CB  
22   C  CG  . TYR   A 9   ? 1.0426 0.4032 0.7123 0.3397  0.0809  0.0126  52  TYR   A CG  
23   C  CD1 . TYR   A 9   ? 1.0860 0.3697 0.7463 0.3180  0.0816  0.0092  52  TYR   A CD1 
24   C  CD2 . TYR   A 9   ? 1.0505 0.4196 0.7132 0.3554  0.0807  0.0410  52  TYR   A CD2 
25   C  CE1 . TYR   A 9   ? 1.1226 0.3416 0.7718 0.3078  0.0859  0.0374  52  TYR   A CE1 
26   C  CE2 . TYR   A 9   ? 1.0877 0.3918 0.7307 0.3499  0.0851  0.0693  52  TYR   A CE2 
27   C  CZ  . TYR   A 9   ? 1.1317 0.3606 0.7699 0.3250  0.0895  0.0693  52  TYR   A CZ  
28   O  OH  . TYR   A 9   ? 1.1804 0.3459 0.8028 0.3153  0.0974  0.1012  52  TYR   A OH  
29   N  N   . ILE   A 10  ? 0.9320 0.5225 0.6588 0.3285  0.0781  0.0088  53  ILE   A N   
30   C  CA  . ILE   A 10  ? 0.9150 0.5451 0.6487 0.3232  0.0741  0.0268  53  ILE   A CA  
31   C  C   . ILE   A 10  ? 0.9284 0.5536 0.6500 0.3588  0.0664  0.0421  53  ILE   A C   
32   O  O   . ILE   A 10  ? 0.9245 0.5543 0.6484 0.3926  0.0622  0.0343  53  ILE   A O   
33   C  CB  . ILE   A 10  ? 0.8803 0.5862 0.6406 0.3089  0.0725  0.0168  53  ILE   A CB  
34   C  CG1 . ILE   A 10  ? 0.8633 0.6201 0.6442 0.3345  0.0705  0.0033  53  ILE   A CG1 
35   C  CG2 . ILE   A 10  ? 0.8816 0.5892 0.6470 0.2761  0.0784  0.0065  53  ILE   A CG2 
36   C  CD1 . ILE   A 10  ? 0.8396 0.6685 0.6500 0.3197  0.0684  -0.0002 53  ILE   A CD1 
37   N  N   . GLU   A 11  ? 0.9399 0.5570 0.6460 0.3532  0.0646  0.0641  54  GLU   A N   
38   C  CA  . GLU   A 11  ? 0.9551 0.5686 0.6408 0.3847  0.0553  0.0820  54  GLU   A CA  
39   C  C   . GLU   A 11  ? 0.9361 0.6065 0.6275 0.3751  0.0471  0.0853  54  GLU   A C   
40   O  O   . GLU   A 11  ? 0.9326 0.6059 0.6246 0.3445  0.0546  0.0884  54  GLU   A O   
41   C  CB  . GLU   A 11  ? 1.0228 0.5594 0.6717 0.3864  0.0636  0.1088  54  GLU   A CB  
42   C  CG  . GLU   A 11  ? 1.1187 0.5810 0.7568 0.3935  0.0702  0.1081  54  GLU   A CG  
43   C  CD  . GLU   A 11  ? 1.2527 0.6365 0.8586 0.3881  0.0807  0.1387  54  GLU   A CD  
44   O  OE1 . GLU   A 11  ? 1.2763 0.6681 0.8708 0.3717  0.0878  0.1599  54  GLU   A OE1 
45   O  OE2 . GLU   A 11  ? 1.3130 0.6253 0.9047 0.4004  0.0831  0.1419  54  GLU   A OE2 
46   N  N   . ARG   A 12  ? 0.9147 0.6294 0.6110 0.4020  0.0301  0.0829  55  ARG   A N   
47   C  CA  . ARG   A 12  ? 0.8969 0.6594 0.5964 0.3938  0.0184  0.0817  55  ARG   A CA  
48   C  C   . ARG   A 12  ? 0.9336 0.6589 0.5893 0.3922  0.0230  0.1044  55  ARG   A C   
49   O  O   . ARG   A 12  ? 0.9721 0.6456 0.5934 0.4115  0.0281  0.1252  55  ARG   A O   
50   C  CB  . ARG   A 12  ? 0.8772 0.6959 0.5948 0.4223  -0.0045 0.0720  55  ARG   A CB  
51   C  CG  . ARG   A 12  ? 0.8667 0.7447 0.6073 0.4033  -0.0179 0.0587  55  ARG   A CG  
52   C  CD  . ARG   A 12  ? 0.8502 0.7942 0.6267 0.4228  -0.0410 0.0444  55  ARG   A CD  
53   N  NE  . ARG   A 12  ? 0.8455 0.8382 0.6463 0.3995  -0.0549 0.0304  55  ARG   A NE  
54   C  CZ  . ARG   A 12  ? 0.8721 0.8714 0.6486 0.4060  -0.0751 0.0302  55  ARG   A CZ  
55   N  NH1 . ARG   A 12  ? 0.9038 0.8679 0.6281 0.4359  -0.0818 0.0462  55  ARG   A NH1 
56   N  NH2 . ARG   A 12  ? 0.8374 0.8739 0.6374 0.3831  -0.0886 0.0143  55  ARG   A NH2 
57   N  N   . ALA   A 13  ? 0.9248 0.6728 0.5804 0.3692  0.0240  0.1018  56  ALA   A N   
58   C  CA  . ALA   A 13  ? 0.9507 0.6738 0.5651 0.3684  0.0315  0.1216  56  ALA   A CA  
59   C  C   . ALA   A 13  ? 0.9508 0.7127 0.5486 0.3813  0.0120  0.1149  56  ALA   A C   
60   O  O   . ALA   A 13  ? 0.9737 0.7173 0.5279 0.3902  0.0166  0.1310  56  ALA   A O   
61   C  CB  . ALA   A 13  ? 0.9497 0.6583 0.5729 0.3329  0.0526  0.1249  56  ALA   A CB  
62   N  N   . GLY   A 14  ? 0.9268 0.7410 0.5584 0.3819  -0.0092 0.0914  57  GLY   A N   
63   C  CA  . GLY   A 14  ? 0.9340 0.7831 0.5535 0.3925  -0.0329 0.0802  57  GLY   A CA  
64   C  C   . GLY   A 14  ? 0.9143 0.8150 0.5804 0.3709  -0.0481 0.0534  57  GLY   A C   
65   O  O   . GLY   A 14  ? 0.8969 0.8125 0.6067 0.3486  -0.0390 0.0446  57  GLY   A O   
66   N  N   . ASP   A 15  ? 0.9192 0.8448 0.5730 0.3782  -0.0723 0.0404  58  ASP   A N   
67   C  CA  . ASP   A 15  ? 0.9018 0.8693 0.5963 0.3561  -0.0900 0.0152  58  ASP   A CA  
68   C  C   . ASP   A 15  ? 0.9235 0.8716 0.6100 0.3296  -0.0762 0.0119  58  ASP   A C   
69   O  O   . ASP   A 15  ? 0.9513 0.8633 0.5947 0.3345  -0.0589 0.0263  58  ASP   A O   
70   C  CB  . ASP   A 15  ? 0.9111 0.9075 0.5926 0.3761  -0.1264 -0.0004 58  ASP   A CB  
71   C  CG  . ASP   A 15  ? 0.9502 0.9839 0.6550 0.4014  -0.1480 -0.0031 58  ASP   A CG  
72   O  OD1 . ASP   A 15  ? 0.9612 0.9882 0.6791 0.4115  -0.1324 0.0106  58  ASP   A OD1 
73   O  OD2 . ASP   A 15  ? 0.9662 1.0353 0.6751 0.4135  -0.1824 -0.0202 58  ASP   A OD2 
74   N  N   . ILE   A 16  ? 0.9088 0.8817 0.6375 0.3027  -0.0834 -0.0060 59  ILE   A N   
75   C  CA  . ILE   A 16  ? 0.9315 0.8857 0.6537 0.2811  -0.0742 -0.0108 59  ILE   A CA  
76   C  C   . ILE   A 16  ? 0.9501 0.9141 0.6633 0.2817  -0.1023 -0.0328 59  ILE   A C   
77   O  O   . ILE   A 16  ? 0.9268 0.9180 0.6829 0.2634  -0.1204 -0.0502 59  ILE   A O   
78   C  CB  . ILE   A 16  ? 0.9190 0.8785 0.6851 0.2513  -0.0568 -0.0097 59  ILE   A CB  
79   C  CG1 . ILE   A 16  ? 0.9428 0.8763 0.6974 0.2529  -0.0293 0.0098  59  ILE   A CG1 
80   C  CG2 . ILE   A 16  ? 0.9256 0.8751 0.6965 0.2292  -0.0570 -0.0195 59  ILE   A CG2 
81   C  CD1 . ILE   A 16  ? 0.9471 0.8900 0.7394 0.2326  -0.0155 0.0104  59  ILE   A CD1 
82   N  N   . THR   A 17  ? 0.9909 0.9324 0.6457 0.3048  -0.1066 -0.0319 60  THR   A N   
83   C  CA  . THR   A 17  ? 1.0202 0.9620 0.6493 0.3128  -0.1347 -0.0552 60  THR   A CA  
84   C  C   . THR   A 17  ? 1.0692 0.9755 0.6435 0.3227  -0.1195 -0.0528 60  THR   A C   
85   O  O   . THR   A 17  ? 1.0825 0.9697 0.6273 0.3334  -0.0910 -0.0291 60  THR   A O   
86   C  CB  . THR   A 17  ? 1.0394 0.9981 0.6390 0.3447  -0.1626 -0.0601 60  THR   A CB  
87   O  OG1 . THR   A 17  ? 1.0750 1.0105 0.6229 0.3725  -0.1424 -0.0332 60  THR   A OG1 
88   C  CG2 . THR   A 17  ? 1.0103 1.0152 0.6684 0.3393  -0.1842 -0.0680 60  THR   A CG2 
89   N  N   . TRP   A 18  ? 1.0956 0.9936 0.6564 0.3207  -0.1393 -0.0781 61  TRP   A N   
90   C  CA  . TRP   A 18  ? 1.1516 1.0198 0.6572 0.3365  -0.1274 -0.0805 61  TRP   A CA  
91   C  C   . TRP   A 18  ? 1.2119 1.0770 0.6474 0.3757  -0.1386 -0.0797 61  TRP   A C   
92   O  O   . TRP   A 18  ? 1.2072 1.0880 0.6360 0.3865  -0.1745 -0.0988 61  TRP   A O   
93   C  CB  . TRP   A 18  ? 1.1497 1.0039 0.6646 0.3224  -0.1476 -0.1113 61  TRP   A CB  
94   C  CG  . TRP   A 18  ? 1.1834 1.0078 0.6399 0.3440  -0.1393 -0.1205 61  TRP   A CG  
95   C  CD1 . TRP   A 18  ? 1.2167 1.0294 0.6091 0.3747  -0.1588 -0.1403 61  TRP   A CD1 
96   C  CD2 . TRP   A 18  ? 1.1897 0.9945 0.6479 0.3382  -0.1118 -0.1139 61  TRP   A CD2 
97   N  NE1 . TRP   A 18  ? 1.2415 1.0286 0.5933 0.3902  -0.1409 -0.1451 61  TRP   A NE1 
98   C  CE2 . TRP   A 18  ? 1.2262 1.0099 0.6209 0.3683  -0.1124 -0.1289 61  TRP   A CE2 
99   C  CE3 . TRP   A 18  ? 1.1761 0.9818 0.6807 0.3139  -0.0870 -0.0967 61  TRP   A CE3 
100  C  CZ2 . TRP   A 18  ? 1.2405 1.0074 0.6236 0.3749  -0.0881 -0.1271 61  TRP   A CZ2 
101  C  CZ3 . TRP   A 18  ? 1.1924 0.9813 0.6857 0.3193  -0.0667 -0.0951 61  TRP   A CZ3 
102  C  CH2 . TRP   A 18  ? 1.2196 0.9914 0.6553 0.3500  -0.0659 -0.1092 61  TRP   A CH2 
103  N  N   . GLU   A 19  ? 1.2617 1.1097 0.6470 0.3965  -0.1081 -0.0562 62  GLU   A N   
104  C  CA  . GLU   A 19  ? 1.3230 1.1641 0.6322 0.4358  -0.1131 -0.0503 62  GLU   A CA  
105  C  C   . GLU   A 19  ? 1.3721 1.1949 0.6244 0.4546  -0.1123 -0.0690 62  GLU   A C   
106  O  O   . GLU   A 19  ? 1.3777 1.1895 0.6255 0.4515  -0.0783 -0.0568 62  GLU   A O   
107  C  CB  . GLU   A 19  ? 1.3760 1.2076 0.6618 0.4478  -0.0762 -0.0078 62  GLU   A CB  
108  C  CG  . GLU   A 19  ? 1.4944 1.3147 0.6929 0.4901  -0.0758 0.0047  62  GLU   A CG  
109  C  CD  . GLU   A 19  ? 1.6135 1.4154 0.7747 0.5010  -0.0290 0.0458  62  GLU   A CD  
110  O  OE1 . GLU   A 19  ? 1.6276 1.4266 0.8376 0.4739  0.0016  0.0662  62  GLU   A OE1 
111  O  OE2 . GLU   A 19  ? 1.6704 1.4616 0.7533 0.5361  -0.0231 0.0579  62  GLU   A OE2 
112  N  N   . LYS   A 20  ? 1.4056 1.2269 0.6160 0.4753  -0.1504 -0.1004 63  LYS   A N   
113  C  CA  . LYS   A 20  ? 1.4613 1.2611 0.6071 0.4995  -0.1508 -0.1218 63  LYS   A CA  
114  C  C   . LYS   A 20  ? 1.5099 1.3036 0.5767 0.5372  -0.1193 -0.0916 63  LYS   A C   
115  O  O   . LYS   A 20  ? 1.5201 1.3216 0.5692 0.5501  -0.1177 -0.0660 63  LYS   A O   
116  C  CB  . LYS   A 20  ? 1.5063 1.3026 0.6248 0.5116  -0.2044 -0.1673 63  LYS   A CB  
117  C  CG  . LYS   A 20  ? 1.5403 1.3559 0.7368 0.4773  -0.2438 -0.1895 63  LYS   A CG  
118  C  CD  . LYS   A 20  ? 1.6125 1.4314 0.7752 0.4942  -0.2999 -0.2310 63  LYS   A CD  
119  C  CE  . LYS   A 20  ? 1.6211 1.4734 0.8629 0.4639  -0.3395 -0.2477 63  LYS   A CE  
120  N  NZ  . LYS   A 20  ? 1.6534 1.5127 0.8652 0.4795  -0.3970 -0.2896 63  LYS   A NZ  
121  N  N   . ASP   A 21  ? 1.5385 1.3183 0.5582 0.5560  -0.0927 -0.0926 64  ASP   A N   
122  C  CA  . ASP   A 21  ? 1.5794 1.3567 0.5256 0.5900  -0.0556 -0.0604 64  ASP   A CA  
123  C  C   . ASP   A 21  ? 1.5616 1.3472 0.5500 0.5697  -0.0109 -0.0107 64  ASP   A C   
124  O  O   . ASP   A 21  ? 1.5843 1.3670 0.5296 0.5885  0.0091  0.0241  64  ASP   A O   
125  C  CB  . ASP   A 21  ? 1.6472 1.4215 0.5094 0.6300  -0.0815 -0.0624 64  ASP   A CB  
126  C  CG  . ASP   A 21  ? 1.7603 1.5241 0.5623 0.6571  -0.1247 -0.1120 64  ASP   A CG  
127  O  OD1 . ASP   A 21  ? 1.7956 1.5460 0.5757 0.6656  -0.1154 -0.1351 64  ASP   A OD1 
128  O  OD2 . ASP   A 21  ? 1.7946 1.5632 0.5697 0.6722  -0.1693 -0.1287 64  ASP   A OD2 
129  N  N   . ALA   A 22  ? 1.5196 1.3118 0.5900 0.5314  0.0027  -0.0076 65  ALA   A N   
130  C  CA  . ALA   A 22  ? 1.4960 1.2942 0.6109 0.5088  0.0415  0.0333  65  ALA   A CA  
131  C  C   . ALA   A 22  ? 1.4884 1.2936 0.5942 0.5135  0.0882  0.0515  65  ALA   A C   
132  O  O   . ALA   A 22  ? 1.4982 1.3044 0.5761 0.5312  0.0885  0.0281  65  ALA   A O   
133  C  CB  . ALA   A 22  ? 1.4641 1.2691 0.6688 0.4671  0.0299  0.0263  65  ALA   A CB  
134  N  N   . GLU   A 23  ? 1.4682 1.2790 0.5985 0.4989  0.1271  0.0922  66  GLU   A N   
135  C  CA  . GLU   A 23  ? 1.4578 1.2853 0.5935 0.4990  0.1733  0.1133  66  GLU   A CA  
136  C  C   . GLU   A 23  ? 1.4170 1.2605 0.6140 0.4789  0.1729  0.0900  66  GLU   A C   
137  O  O   . GLU   A 23  ? 1.3908 1.2384 0.6589 0.4440  0.1683  0.0917  66  GLU   A O   
138  C  CB  . GLU   A 23  ? 1.4882 1.3158 0.6528 0.4780  0.2083  0.1599  66  GLU   A CB  
139  C  CG  . GLU   A 23  ? 1.5630 1.4143 0.7360 0.4765  0.2591  0.1879  66  GLU   A CG  
140  C  CD  . GLU   A 23  ? 1.6509 1.5049 0.8879 0.4389  0.2863  0.2233  66  GLU   A CD  
141  O  OE1 . GLU   A 23  ? 1.6743 1.5014 0.9226 0.4243  0.2725  0.2352  66  GLU   A OE1 
142  O  OE2 . GLU   A 23  ? 1.6682 1.5522 0.9463 0.4248  0.3202  0.2374  66  GLU   A OE2 
143  N  N   . VAL   A 24  ? 1.4098 1.2596 0.5736 0.5047  0.1767  0.0676  67  VAL   A N   
144  C  CA  . VAL   A 24  ? 1.3773 1.2375 0.5882 0.4947  0.1753  0.0451  67  VAL   A CA  
145  C  C   . VAL   A 24  ? 1.3431 1.2381 0.5872 0.4912  0.2224  0.0712  67  VAL   A C   
146  O  O   . VAL   A 24  ? 1.3577 1.2680 0.5581 0.5227  0.2491  0.0745  67  VAL   A O   
147  C  CB  . VAL   A 24  ? 1.4019 1.2440 0.5646 0.5250  0.1494  0.0017  67  VAL   A CB  
148  C  CG1 . VAL   A 24  ? 1.3888 1.2287 0.6073 0.5092  0.1382  -0.0213 67  VAL   A CG1 
149  C  CG2 . VAL   A 24  ? 1.4284 1.2424 0.5497 0.5329  0.1039  -0.0236 67  VAL   A CG2 
150  N  N   . THR   A 25  ? 1.2977 1.2089 0.6198 0.4542  0.2317  0.0875  68  THR   A N   
151  C  CA  . THR   A 25  ? 1.2594 1.2110 0.6264 0.4462  0.2723  0.1108  68  THR   A CA  
152  C  C   . THR   A 25  ? 1.2180 1.1829 0.6643 0.4174  0.2602  0.0995  68  THR   A C   
153  O  O   . THR   A 25  ? 1.2206 1.1604 0.6839 0.4013  0.2253  0.0796  68  THR   A O   
154  C  CB  . THR   A 25  ? 1.2651 1.2258 0.6388 0.4304  0.3046  0.1547  68  THR   A CB  
155  O  OG1 . THR   A 25  ? 1.2406 1.2460 0.6680 0.4176  0.3426  0.1768  68  THR   A OG1 
156  C  CG2 . THR   A 25  ? 1.2653 1.2008 0.6731 0.3962  0.2837  0.1629  68  THR   A CG2 
157  N  N   . GLY   A 26  ? 1.1787 1.1859 0.6722 0.4129  0.2889  0.1123  69  GLY   A N   
158  C  CA  . GLY   A 26  ? 1.1445 1.1682 0.7105 0.3885  0.2774  0.1044  69  GLY   A CA  
159  C  C   . GLY   A 26  ? 1.1345 1.1651 0.7034 0.4125  0.2678  0.0772  69  GLY   A C   
160  O  O   . GLY   A 26  ? 1.1633 1.1619 0.6788 0.4395  0.2489  0.0507  69  GLY   A O   
161  N  N   . ASN   A 27  ? 1.0919 1.1619 0.7247 0.4025  0.2777  0.0823  70  ASN   A N   
162  C  CA  . ASN   A 27  ? 1.0803 1.1592 0.7239 0.4267  0.2698  0.0601  70  ASN   A CA  
163  C  C   . ASN   A 27  ? 1.0650 1.1127 0.7368 0.4077  0.2309  0.0419  70  ASN   A C   
164  O  O   . ASN   A 27  ? 1.0671 1.0950 0.7546 0.3747  0.2136  0.0474  70  ASN   A O   
165  C  CB  . ASN   A 27  ? 1.0612 1.2091 0.7556 0.4352  0.3048  0.0769  70  ASN   A CB  
166  C  CG  . ASN   A 27  ? 1.0769 1.2604 0.8527 0.3956  0.3044  0.0945  70  ASN   A CG  
167  O  OD1 . ASN   A 27  ? 1.0939 1.2708 0.8862 0.3607  0.3052  0.1125  70  ASN   A OD1 
168  N  ND2 . ASN   A 27  ? 1.0584 1.2784 0.8851 0.4023  0.3007  0.0880  70  ASN   A ND2 
169  N  N   . SER   A 28  ? 1.0535 1.0930 0.7263 0.4314  0.2182  0.0209  71  SER   A N   
170  C  CA  . SER   A 28  ? 1.0489 1.0546 0.7413 0.4178  0.1843  0.0067  71  SER   A CA  
171  C  C   . SER   A 28  ? 1.0026 1.0470 0.7503 0.4233  0.1875  0.0110  71  SER   A C   
172  O  O   . SER   A 28  ? 1.0160 1.0484 0.7534 0.4548  0.1808  -0.0055 71  SER   A O   
173  C  CB  . SER   A 28  ? 1.1042 1.0490 0.7424 0.4405  0.1593  -0.0232 71  SER   A CB  
174  O  OG  . SER   A 28  ? 1.1621 1.0825 0.7410 0.4528  0.1593  -0.0329 71  SER   A OG  
175  N  N   . PRO   A 29  ? 0.9519 1.0413 0.7585 0.3949  0.1950  0.0314  72  PRO   A N   
176  C  CA  . PRO   A 29  ? 0.9111 1.0447 0.7724 0.4023  0.1947  0.0344  72  PRO   A CA  
177  C  C   . PRO   A 29  ? 0.9120 1.0113 0.7822 0.3953  0.1607  0.0251  72  PRO   A C   
178  O  O   . PRO   A 29  ? 0.9282 0.9915 0.7905 0.3656  0.1416  0.0259  72  PRO   A O   
179  C  CB  . PRO   A 29  ? 0.8814 1.0752 0.8008 0.3717  0.2136  0.0580  72  PRO   A CB  
180  C  CG  . PRO   A 29  ? 0.9058 1.0639 0.8030 0.3385  0.2091  0.0654  72  PRO   A CG  
181  C  CD  . PRO   A 29  ? 0.9314 1.0330 0.7573 0.3570  0.2027  0.0510  72  PRO   A CD  
182  N  N   . ARG   A 30  ? 0.8923 1.0045 0.7787 0.4246  0.1548  0.0180  73  ARG   A N   
183  C  CA  . ARG   A 30  ? 0.8963 0.9781 0.7905 0.4215  0.1246  0.0141  73  ARG   A CA  
184  C  C   . ARG   A 30  ? 0.8356 0.9843 0.7955 0.4094  0.1243  0.0284  73  ARG   A C   
185  O  O   . ARG   A 30  ? 0.8051 1.0118 0.8013 0.4343  0.1380  0.0306  73  ARG   A O   
186  C  CB  . ARG   A 30  ? 0.9478 0.9900 0.8122 0.4644  0.1140  -0.0030 73  ARG   A CB  
187  C  CG  . ARG   A 30  ? 1.0538 1.0239 0.8536 0.4734  0.1077  -0.0218 73  ARG   A CG  
188  C  CD  . ARG   A 30  ? 1.1422 1.0596 0.9121 0.5124  0.0928  -0.0406 73  ARG   A CD  
189  N  NE  . ARG   A 30  ? 1.2282 1.0906 0.9387 0.5299  0.0913  -0.0638 73  ARG   A NE  
190  C  CZ  . ARG   A 30  ? 1.2922 1.0836 0.9671 0.5102  0.0685  -0.0754 73  ARG   A CZ  
191  N  NH1 . ARG   A 30  ? 1.2949 1.0626 0.9866 0.4731  0.0498  -0.0636 73  ARG   A NH1 
192  N  NH2 . ARG   A 30  ? 1.3171 1.0637 0.9402 0.5277  0.0643  -0.0997 73  ARG   A NH2 
193  N  N   . LEU   A 31  ? 0.8164 0.9623 0.7934 0.3713  0.1095  0.0370  74  LEU   A N   
194  C  CA  . LEU   A 31  ? 0.7644 0.9719 0.8018 0.3547  0.1049  0.0474  74  LEU   A CA  
195  C  C   . LEU   A 31  ? 0.7597 0.9455 0.7976 0.3487  0.0729  0.0471  74  LEU   A C   
196  O  O   . LEU   A 31  ? 0.7945 0.9233 0.7953 0.3304  0.0587  0.0458  74  LEU   A O   
197  C  CB  . LEU   A 31  ? 0.7491 0.9769 0.8069 0.3138  0.1170  0.0575  74  LEU   A CB  
198  C  CG  . LEU   A 31  ? 0.7597 1.0037 0.8114 0.3147  0.1499  0.0636  74  LEU   A CG  
199  C  CD1 . LEU   A 31  ? 0.7786 0.9942 0.8139 0.2790  0.1538  0.0704  74  LEU   A CD1 
200  C  CD2 . LEU   A 31  ? 0.7194 1.0462 0.8318 0.3217  0.1734  0.0737  74  LEU   A CD2 
201  N  N   . ASP   A 32  ? 0.7117 0.9486 0.7933 0.3633  0.0621  0.0498  75  ASP   A N   
202  C  CA  . ASP   A 32  ? 0.7121 0.9349 0.7920 0.3595  0.0312  0.0519  75  ASP   A CA  
203  C  C   . ASP   A 32  ? 0.6752 0.9184 0.7769 0.3161  0.0236  0.0559  75  ASP   A C   
204  O  O   . ASP   A 32  ? 0.6375 0.9471 0.7949 0.3024  0.0302  0.0582  75  ASP   A O   
205  C  CB  . ASP   A 32  ? 0.7198 0.9950 0.8392 0.3939  0.0193  0.0526  75  ASP   A CB  
206  C  CG  . ASP   A 32  ? 0.8438 1.0683 0.9246 0.4375  0.0090  0.0489  75  ASP   A CG  
207  O  OD1 . ASP   A 32  ? 0.9050 1.0550 0.9312 0.4400  0.0135  0.0439  75  ASP   A OD1 
208  O  OD2 . ASP   A 32  ? 0.8584 1.1168 0.9650 0.4696  -0.0053 0.0505  75  ASP   A OD2 
209  N  N   . VAL   A 33  ? 0.6822 0.8684 0.7418 0.2937  0.0117  0.0561  76  VAL   A N   
210  C  CA  . VAL   A 33  ? 0.6590 0.8567 0.7315 0.2563  0.0050  0.0566  76  VAL   A CA  
211  C  C   . VAL   A 33  ? 0.6580 0.8307 0.7048 0.2512  -0.0233 0.0573  76  VAL   A C   
212  O  O   . VAL   A 33  ? 0.6766 0.8116 0.6890 0.2729  -0.0349 0.0611  76  VAL   A O   
213  C  CB  . VAL   A 33  ? 0.6803 0.8476 0.7329 0.2295  0.0238  0.0562  76  VAL   A CB  
214  C  CG1 . VAL   A 33  ? 0.6790 0.8590 0.7384 0.2405  0.0517  0.0578  76  VAL   A CG1 
215  C  CG2 . VAL   A 33  ? 0.7260 0.8250 0.7227 0.2237  0.0168  0.0551  76  VAL   A CG2 
216  N  N   . ALA   A 34  ? 0.6330 0.8259 0.6955 0.2235  -0.0340 0.0538  77  ALA   A N   
217  C  CA  . ALA   A 34  ? 0.6415 0.8168 0.6762 0.2176  -0.0590 0.0529  77  ALA   A CA  
218  C  C   . ALA   A 34  ? 0.6447 0.7946 0.6599 0.1853  -0.0553 0.0475  77  ALA   A C   
219  O  O   . ALA   A 34  ? 0.6351 0.8053 0.6812 0.1636  -0.0442 0.0423  77  ALA   A O   
220  C  CB  . ALA   A 34  ? 0.6108 0.8460 0.6862 0.2238  -0.0834 0.0489  77  ALA   A CB  
221  N  N   . LEU   A 35  ? 0.6586 0.7633 0.6228 0.1832  -0.0629 0.0499  78  LEU   A N   
222  C  CA  . LEU   A 35  ? 0.6636 0.7445 0.6061 0.1582  -0.0587 0.0437  78  LEU   A CA  
223  C  C   . LEU   A 35  ? 0.6680 0.7562 0.5925 0.1543  -0.0827 0.0372  78  LEU   A C   
224  O  O   . LEU   A 35  ? 0.6903 0.7630 0.5789 0.1708  -0.0956 0.0452  78  LEU   A O   
225  C  CB  . LEU   A 35  ? 0.6864 0.7145 0.5863 0.1576  -0.0433 0.0505  78  LEU   A CB  
226  C  CG  . LEU   A 35  ? 0.6966 0.7030 0.5752 0.1369  -0.0365 0.0445  78  LEU   A CG  
227  C  CD1 . LEU   A 35  ? 0.6787 0.6984 0.5880 0.1200  -0.0246 0.0364  78  LEU   A CD1 
228  C  CD2 . LEU   A 35  ? 0.7211 0.6861 0.5644 0.1377  -0.0246 0.0525  78  LEU   A CD2 
229  N  N   . ASP   A 36  ? 0.6474 0.7570 0.5947 0.1334  -0.0899 0.0228  79  ASP   A N   
230  C  CA  . ASP   A 36  ? 0.6521 0.7689 0.5794 0.1303  -0.1160 0.0114  79  ASP   A CA  
231  C  C   . ASP   A 36  ? 0.6885 0.7598 0.5585 0.1233  -0.1097 0.0080  79  ASP   A C   
232  O  O   . ASP   A 36  ? 0.7007 0.7411 0.5574 0.1179  -0.0859 0.0139  79  ASP   A O   
233  C  CB  . ASP   A 36  ? 0.6263 0.7883 0.6075 0.1116  -0.1324 -0.0058 79  ASP   A CB  
234  C  CG  . ASP   A 36  ? 0.6633 0.8092 0.6603 0.0828  -0.1189 -0.0170 79  ASP   A CG  
235  O  OD1 . ASP   A 36  ? 0.6956 0.7978 0.6583 0.0801  -0.0987 -0.0132 79  ASP   A OD1 
236  O  OD2 . ASP   A 36  ? 0.6587 0.8354 0.7047 0.0629  -0.1295 -0.0292 79  ASP   A OD2 
237  N  N   . GLU   A 37  ? 0.7009 0.7725 0.5375 0.1255  -0.1314 -0.0025 80  GLU   A N   
238  C  CA  . GLU   A 37  ? 0.7422 0.7788 0.5228 0.1231  -0.1258 -0.0073 80  GLU   A CA  
239  C  C   . GLU   A 37  ? 0.7493 0.7685 0.5423 0.1023  -0.1100 -0.0214 80  GLU   A C   
240  O  O   . GLU   A 37  ? 0.7754 0.7646 0.5328 0.1027  -0.0928 -0.0193 80  GLU   A O   
241  C  CB  . GLU   A 37  ? 0.7983 0.8458 0.5432 0.1314  -0.1559 -0.0204 80  GLU   A CB  
242  C  CG  . GLU   A 37  ? 0.9227 0.9375 0.5961 0.1389  -0.1486 -0.0200 80  GLU   A CG  
243  C  CD  . GLU   A 37  ? 1.0372 1.0599 0.6590 0.1567  -0.1764 -0.0246 80  GLU   A CD  
244  O  OE1 . GLU   A 37  ? 1.0519 1.0968 0.6840 0.1520  -0.2061 -0.0498 80  GLU   A OE1 
245  O  OE2 . GLU   A 37  ? 1.0954 1.1008 0.6654 0.1749  -0.1694 -0.0025 80  GLU   A OE2 
246  N  N   . SER   A 38  ? 0.7190 0.7572 0.5648 0.0846  -0.1141 -0.0333 81  SER   A N   
247  C  CA  . SER   A 38  ? 0.7160 0.7326 0.5755 0.0652  -0.1010 -0.0448 81  SER   A CA  
248  C  C   . SER   A 38  ? 0.7100 0.7131 0.5888 0.0621  -0.0714 -0.0294 81  SER   A C   
249  O  O   . SER   A 38  ? 0.7130 0.6998 0.6081 0.0476  -0.0610 -0.0353 81  SER   A O   
250  C  CB  . SER   A 38  ? 0.7099 0.7482 0.6171 0.0444  -0.1194 -0.0626 81  SER   A CB  
251  O  OG  . SER   A 38  ? 0.7523 0.8064 0.6435 0.0472  -0.1521 -0.0807 81  SER   A OG  
252  N  N   . GLY   A 39  ? 0.7022 0.7090 0.5774 0.0764  -0.0601 -0.0107 82  GLY   A N   
253  C  CA  . GLY   A 39  ? 0.7022 0.6970 0.5898 0.0763  -0.0358 0.0015  82  GLY   A CA  
254  C  C   . GLY   A 39  ? 0.6789 0.6979 0.6172 0.0681  -0.0287 0.0051  82  GLY   A C   
255  O  O   . GLY   A 39  ? 0.6812 0.6867 0.6265 0.0644  -0.0092 0.0114  82  GLY   A O   
256  N  N   . ASP   A 40  ? 0.6517 0.7104 0.6263 0.0662  -0.0439 0.0023  83  ASP   A N   
257  C  CA  . ASP   A 40  ? 0.6248 0.7176 0.6545 0.0581  -0.0347 0.0078  83  ASP   A CA  
258  C  C   . ASP   A 40  ? 0.6155 0.7348 0.6570 0.0806  -0.0298 0.0202  83  ASP   A C   
259  O  O   . ASP   A 40  ? 0.6134 0.7510 0.6510 0.0956  -0.0485 0.0194  83  ASP   A O   
260  C  CB  . ASP   A 40  ? 0.6178 0.7481 0.6936 0.0397  -0.0551 -0.0048 83  ASP   A CB  
261  C  CG  . ASP   A 40  ? 0.6904 0.7953 0.7581 0.0175  -0.0680 -0.0232 83  ASP   A CG  
262  O  OD1 . ASP   A 40  ? 0.6988 0.7697 0.7630 0.0041  -0.0511 -0.0223 83  ASP   A OD1 
263  O  OD2 . ASP   A 40  ? 0.7319 0.8501 0.7962 0.0151  -0.0967 -0.0395 83  ASP   A OD2 
264  N  N   . PHE   A 41  ? 0.6129 0.7338 0.6666 0.0857  -0.0060 0.0311  84  PHE   A N   
265  C  CA  . PHE   A 41  ? 0.6096 0.7550 0.6752 0.1098  -0.0001 0.0397  84  PHE   A CA  
266  C  C   . PHE   A 41  ? 0.5873 0.7951 0.7170 0.1053  0.0004  0.0409  84  PHE   A C   
267  O  O   . PHE   A 41  ? 0.5710 0.7953 0.7365 0.0800  0.0069  0.0400  84  PHE   A O   
268  C  CB  . PHE   A 41  ? 0.6160 0.7362 0.6605 0.1206  0.0246  0.0480  84  PHE   A CB  
269  C  CG  . PHE   A 41  ? 0.6483 0.7180 0.6398 0.1297  0.0230  0.0477  84  PHE   A CG  
270  C  CD1 . PHE   A 41  ? 0.6638 0.7211 0.6335 0.1495  0.0120  0.0491  84  PHE   A CD1 
271  C  CD2 . PHE   A 41  ? 0.6708 0.7061 0.6376 0.1186  0.0329  0.0470  84  PHE   A CD2 
272  C  CE1 . PHE   A 41  ? 0.6998 0.7117 0.6278 0.1530  0.0119  0.0504  84  PHE   A CE1 
273  C  CE2 . PHE   A 41  ? 0.6967 0.6946 0.6246 0.1247  0.0316  0.0467  84  PHE   A CE2 
274  C  CZ  . PHE   A 41  ? 0.7039 0.6907 0.6145 0.1394  0.0217  0.0486  84  PHE   A CZ  
275  N  N   . SER   A 42  ? 0.5862 0.8291 0.7336 0.1296  -0.0060 0.0437  85  SER   A N   
276  C  CA  . SER   A 42  ? 0.5659 0.8796 0.7815 0.1291  -0.0043 0.0455  85  SER   A CA  
277  C  C   . SER   A 42  ? 0.5899 0.9273 0.8117 0.1651  0.0063  0.0524  85  SER   A C   
278  O  O   . SER   A 42  ? 0.6224 0.9226 0.7983 0.1905  -0.0013 0.0525  85  SER   A O   
279  C  CB  . SER   A 42  ? 0.5494 0.9008 0.7961 0.1198  -0.0374 0.0347  85  SER   A CB  
280  O  OG  . SER   A 42  ? 0.5912 0.9232 0.7963 0.1441  -0.0616 0.0319  85  SER   A OG  
281  N  N   . LEU   A 43  ? 0.5723 0.9698 0.8507 0.1678  0.0251  0.0585  86  LEU   A N   
282  C  CA  . LEU   A 43  ? 0.5875 1.0124 0.8735 0.2068  0.0366  0.0627  86  LEU   A CA  
283  C  C   . LEU   A 43  ? 0.5848 1.0562 0.9022 0.2289  0.0088  0.0580  86  LEU   A C   
284  O  O   . LEU   A 43  ? 0.5530 1.0752 0.9215 0.2102  -0.0103 0.0535  86  LEU   A O   
285  C  CB  . LEU   A 43  ? 0.5631 1.0356 0.8910 0.2062  0.0729  0.0726  86  LEU   A CB  
286  C  CG  . LEU   A 43  ? 0.6222 1.0400 0.8990 0.2027  0.1005  0.0787  86  LEU   A CG  
287  C  CD1 . LEU   A 43  ? 0.6019 1.0648 0.9173 0.1941  0.1371  0.0924  86  LEU   A CD1 
288  C  CD2 . LEU   A 43  ? 0.6708 1.0381 0.8847 0.2400  0.1011  0.0736  86  LEU   A CD2 
289  N  N   . VAL   A 44  ? 0.6161 1.0657 0.9003 0.2694  0.0037  0.0580  87  VAL   A N   
290  C  CA  . VAL   A 44  ? 0.6123 1.0967 0.9162 0.2995  -0.0232 0.0559  87  VAL   A CA  
291  C  C   . VAL   A 44  ? 0.5978 1.1410 0.9450 0.3354  -0.0046 0.0584  87  VAL   A C   
292  O  O   . VAL   A 44  ? 0.6209 1.1327 0.9366 0.3555  0.0210  0.0599  87  VAL   A O   
293  C  CB  . VAL   A 44  ? 0.6668 1.0732 0.8967 0.3214  -0.0428 0.0564  87  VAL   A CB  
294  C  CG1 . VAL   A 44  ? 0.6617 1.0965 0.9043 0.3573  -0.0715 0.0573  87  VAL   A CG1 
295  C  CG2 . VAL   A 44  ? 0.7005 1.0521 0.8855 0.2880  -0.0552 0.0549  87  VAL   A CG2 
296  N  N   . GLU   A 45  ? 0.5563 1.1873 0.9755 0.3450  -0.0174 0.0575  88  GLU   A N   
297  C  CA  . GLU   A 45  ? 0.5417 1.2391 1.0083 0.3830  0.0024  0.0598  88  GLU   A CA  
298  C  C   . GLU   A 45  ? 0.5248 1.2681 1.0199 0.4260  -0.0279 0.0570  88  GLU   A C   
299  O  O   . GLU   A 45  ? 0.5566 1.2529 1.0075 0.4380  -0.0618 0.0555  88  GLU   A O   
300  C  CB  . GLU   A 45  ? 0.5268 1.3102 1.0742 0.3555  0.0321  0.0653  88  GLU   A CB  
301  C  CG  . GLU   A 45  ? 0.6144 1.3541 1.1339 0.3183  0.0634  0.0715  88  GLU   A CG  
302  C  CD  . GLU   A 45  ? 0.7258 1.4259 1.1942 0.3468  0.0988  0.0750  88  GLU   A CD  
303  O  OE1 . GLU   A 45  ? 0.7933 1.4098 1.1915 0.3345  0.1041  0.0743  88  GLU   A OE1 
304  O  OE2 . GLU   A 45  ? 0.7191 1.4734 1.2169 0.3836  0.1198  0.0767  88  GLU   A OE2 
305  N  N   . GLY   B 7   ? 0.9605 0.9948 0.9304 0.2596  0.0757  -0.0577 16  GLY   B N   
306  C  CA  . GLY   B 7   ? 0.9721 0.9950 0.9388 0.2799  0.0701  -0.0567 16  GLY   B CA  
307  C  C   . GLY   B 7   ? 0.9706 1.0025 0.9435 0.2805  0.0606  -0.0511 16  GLY   B C   
308  O  O   . GLY   B 7   ? 0.9640 1.0277 0.9551 0.2818  0.0556  -0.0559 16  GLY   B O   
309  N  N   . GLU   B 8   ? 0.9709 0.9761 0.9293 0.2797  0.0577  -0.0412 17  GLU   B N   
310  C  CA  . GLU   B 8   ? 0.9608 0.9717 0.9202 0.2824  0.0479  -0.0368 17  GLU   B CA  
311  C  C   . GLU   B 8   ? 0.9349 0.9602 0.9030 0.2613  0.0451  -0.0357 17  GLU   B C   
312  O  O   . GLU   B 8   ? 0.9449 0.9561 0.9049 0.2469  0.0492  -0.0298 17  GLU   B O   
313  C  CB  . GLU   B 8   ? 1.0121 0.9925 0.9513 0.2928  0.0471  -0.0257 17  GLU   B CB  
314  C  CG  . GLU   B 8   ? 1.0786 1.0661 1.0150 0.3052  0.0358  -0.0244 17  GLU   B CG  
315  C  CD  . GLU   B 8   ? 1.1823 1.1440 1.0968 0.3211  0.0358  -0.0130 17  GLU   B CD  
316  O  OE1 . GLU   B 8   ? 1.2146 1.1516 1.1184 0.3185  0.0454  -0.0033 17  GLU   B OE1 
317  O  OE2 . GLU   B 8   ? 1.2094 1.1762 1.1176 0.3366  0.0259  -0.0135 17  GLU   B OE2 
318  N  N   . THR   B 9   ? 0.8984 0.9519 0.8845 0.2594  0.0374  -0.0415 18  THR   B N   
319  C  CA  . THR   B 9   ? 0.8750 0.9419 0.8717 0.2395  0.0334  -0.0407 18  THR   B CA  
320  C  C   . THR   B 9   ? 0.8506 0.9136 0.8448 0.2420  0.0191  -0.0391 18  THR   B C   
321  O  O   . THR   B 9   ? 0.8488 0.9196 0.8516 0.2265  0.0134  -0.0388 18  THR   B O   
322  C  CB  . THR   B 9   ? 0.8764 0.9794 0.8993 0.2323  0.0351  -0.0478 18  THR   B CB  
323  O  OG1 . THR   B 9   ? 0.8790 1.0008 0.9154 0.2493  0.0267  -0.0547 18  THR   B OG1 
324  C  CG2 . THR   B 9   ? 0.8803 0.9882 0.9026 0.2295  0.0496  -0.0500 18  THR   B CG2 
325  N  N   . THR   B 10  ? 0.8312 0.8811 0.8119 0.2627  0.0130  -0.0381 19  THR   B N   
326  C  CA  . THR   B 10  ? 0.8116 0.8569 0.7852 0.2712  -0.0016 -0.0384 19  THR   B CA  
327  C  C   . THR   B 10  ? 0.7917 0.8188 0.7512 0.2605  -0.0026 -0.0314 19  THR   B C   
328  O  O   . THR   B 10  ? 0.8023 0.8101 0.7462 0.2594  0.0076  -0.0226 19  THR   B O   
329  C  CB  . THR   B 10  ? 0.8413 0.8728 0.7965 0.2984  -0.0045 -0.0364 19  THR   B CB  
330  O  OG1 . THR   B 10  ? 0.8568 0.9005 0.8215 0.3104  -0.0014 -0.0418 19  THR   B OG1 
331  C  CG2 . THR   B 10  ? 0.8418 0.8731 0.7891 0.3120  -0.0218 -0.0401 19  THR   B CG2 
332  N  N   . ASP   B 11  ? 0.7614 0.7940 0.7267 0.2538  -0.0161 -0.0353 20  ASP   B N   
333  C  CA  . ASP   B 11  ? 0.7542 0.7694 0.7049 0.2470  -0.0200 -0.0302 20  ASP   B CA  
334  C  C   . ASP   B 11  ? 0.7494 0.7431 0.6722 0.2676  -0.0185 -0.0232 20  ASP   B C   
335  O  O   . ASP   B 11  ? 0.7557 0.7490 0.6707 0.2885  -0.0234 -0.0253 20  ASP   B O   
336  C  CB  . ASP   B 11  ? 0.7716 0.7935 0.7321 0.2427  -0.0390 -0.0382 20  ASP   B CB  
337  C  CG  . ASP   B 11  ? 0.8242 0.8512 0.7999 0.2167  -0.0399 -0.0377 20  ASP   B CG  
338  O  OD1 . ASP   B 11  ? 0.8076 0.8514 0.8014 0.2018  -0.0291 -0.0367 20  ASP   B OD1 
339  O  OD2 . ASP   B 11  ? 0.8709 0.8841 0.8387 0.2125  -0.0515 -0.0381 20  ASP   B OD2 
340  N  N   . GLY   B 12  ? 0.7359 0.7140 0.6446 0.2624  -0.0111 -0.0140 21  GLY   B N   
341  C  CA  . GLY   B 12  ? 0.7345 0.6961 0.6192 0.2806  -0.0072 -0.0049 21  GLY   B CA  
342  C  C   . GLY   B 12  ? 0.7248 0.6760 0.6039 0.2721  0.0080  0.0071  21  GLY   B C   
343  O  O   . GLY   B 12  ? 0.7178 0.6722 0.6086 0.2521  0.0138  0.0071  21  GLY   B O   
344  N  N   . VAL   B 13  ? 0.7220 0.6617 0.5832 0.2874  0.0142  0.0178  22  VAL   B N   
345  C  CA  . VAL   B 13  ? 0.7135 0.6456 0.5728 0.2797  0.0281  0.0304  22  VAL   B CA  
346  C  C   . VAL   B 13  ? 0.7076 0.6336 0.5719 0.2805  0.0403  0.0363  22  VAL   B C   
347  O  O   . VAL   B 13  ? 0.7061 0.6299 0.5660 0.2958  0.0392  0.0350  22  VAL   B O   
348  C  CB  . VAL   B 13  ? 0.7245 0.6508 0.5654 0.2929  0.0294  0.0403  22  VAL   B CB  
349  C  CG1 . VAL   B 13  ? 0.7321 0.6533 0.5541 0.3198  0.0296  0.0456  22  VAL   B CG1 
350  C  CG2 . VAL   B 13  ? 0.7260 0.6499 0.5713 0.2816  0.0425  0.0528  22  VAL   B CG2 
351  N  N   . TYR   B 14  ? 0.6991 0.6214 0.5732 0.2634  0.0497  0.0408  23  TYR   B N   
352  C  CA  . TYR   B 14  ? 0.6951 0.6079 0.5754 0.2608  0.0591  0.0443  23  TYR   B CA  
353  C  C   . TYR   B 14  ? 0.6914 0.5947 0.5744 0.2516  0.0694  0.0573  23  TYR   B C   
354  O  O   . TYR   B 14  ? 0.6829 0.5916 0.5689 0.2405  0.0692  0.0596  23  TYR   B O   
355  C  CB  . TYR   B 14  ? 0.6863 0.6059 0.5807 0.2457  0.0575  0.0316  23  TYR   B CB  
356  C  CG  . TYR   B 14  ? 0.6891 0.6203 0.5876 0.2542  0.0503  0.0199  23  TYR   B CG  
357  C  CD1 . TYR   B 14  ? 0.6934 0.6389 0.5939 0.2548  0.0394  0.0127  23  TYR   B CD1 
358  C  CD2 . TYR   B 14  ? 0.7017 0.6303 0.6044 0.2604  0.0536  0.0153  23  TYR   B CD2 
359  C  CE1 . TYR   B 14  ? 0.6977 0.6575 0.6068 0.2616  0.0319  0.0022  23  TYR   B CE1 
360  C  CE2 . TYR   B 14  ? 0.7076 0.6515 0.6172 0.2689  0.0471  0.0046  23  TYR   B CE2 
361  C  CZ  . TYR   B 14  ? 0.7117 0.6730 0.6263 0.2686  0.0363  -0.0017 23  TYR   B CZ  
362  O  OH  . TYR   B 14  ? 0.7235 0.7038 0.6499 0.2754  0.0289  -0.0122 23  TYR   B OH  
363  N  N   . ARG   B 15  ? 0.6976 0.5863 0.5816 0.2549  0.0776  0.0652  24  ARG   B N   
364  C  CA  . ARG   B 15  ? 0.7002 0.5796 0.5924 0.2431  0.0866  0.0772  24  ARG   B CA  
365  C  C   . ARG   B 15  ? 0.6960 0.5693 0.6010 0.2252  0.0858  0.0672  24  ARG   B C   
366  O  O   . ARG   B 15  ? 0.6959 0.5650 0.6003 0.2289  0.0834  0.0567  24  ARG   B O   
367  C  CB  . ARG   B 15  ? 0.7169 0.5798 0.6039 0.2552  0.0958  0.0930  24  ARG   B CB  
368  C  CG  . ARG   B 15  ? 0.7490 0.6146 0.6174 0.2791  0.0966  0.1013  24  ARG   B CG  
369  C  CD  . ARG   B 15  ? 0.7964 0.6436 0.6595 0.2893  0.1074  0.1190  24  ARG   B CD  
370  N  NE  . ARG   B 15  ? 0.8298 0.6782 0.6708 0.3153  0.1089  0.1280  24  ARG   B NE  
371  C  CZ  . ARG   B 15  ? 0.8544 0.7094 0.6864 0.3242  0.1168  0.1443  24  ARG   B CZ  
372  N  NH1 . ARG   B 15  ? 0.8429 0.7057 0.6898 0.3082  0.1243  0.1541  24  ARG   B NH1 
373  N  NH2 . ARG   B 15  ? 0.8507 0.7059 0.6584 0.3506  0.1173  0.1509  24  ARG   B NH2 
374  N  N   . VAL   B 16  ? 0.6905 0.5638 0.6061 0.2080  0.0877  0.0703  25  VAL   B N   
375  C  CA  . VAL   B 16  ? 0.6966 0.5624 0.6219 0.1917  0.0861  0.0612  25  VAL   B CA  
376  C  C   . VAL   B 16  ? 0.7127 0.5585 0.6471 0.1865  0.0921  0.0725  25  VAL   B C   
377  O  O   . VAL   B 16  ? 0.7095 0.5583 0.6526 0.1802  0.0962  0.0859  25  VAL   B O   
378  C  CB  . VAL   B 16  ? 0.6947 0.5745 0.6248 0.1760  0.0812  0.0551  25  VAL   B CB  
379  C  CG1 . VAL   B 16  ? 0.7044 0.5770 0.6390 0.1628  0.0781  0.0427  25  VAL   B CG1 
380  C  CG2 . VAL   B 16  ? 0.6901 0.5868 0.6118 0.1808  0.0758  0.0487  25  VAL   B CG2 
381  N  N   . MET   B 17  ? 0.7341 0.5597 0.6671 0.1902  0.0925  0.0681  26  MET   B N   
382  C  CA  . MET   B 17  ? 0.7626 0.5632 0.7032 0.1863  0.0970  0.0787  26  MET   B CA  
383  C  C   . MET   B 17  ? 0.7994 0.5831 0.7484 0.1713  0.0915  0.0669  26  MET   B C   
384  O  O   . MET   B 17  ? 0.8021 0.5915 0.7457 0.1700  0.0857  0.0493  26  MET   B O   
385  C  CB  . MET   B 17  ? 0.7717 0.5549 0.7005 0.2058  0.1005  0.0830  26  MET   B CB  
386  C  CG  . MET   B 17  ? 0.7784 0.5757 0.6938 0.2253  0.1033  0.0907  26  MET   B CG  
387  S  SD  . MET   B 17  ? 0.8136 0.6157 0.7310 0.2273  0.1138  0.1169  26  MET   B SD  
388  C  CE  . MET   B 17  ? 0.7867 0.5547 0.7154 0.2191  0.1211  0.1322  26  MET   B CE  
389  N  N   . THR   B 18  ? 0.8308 0.5925 0.7925 0.1610  0.0931  0.0765  27  THR   B N   
390  C  CA  . THR   B 18  ? 0.8717 0.6110 0.8399 0.1484  0.0856  0.0643  27  THR   B CA  
391  C  C   . THR   B 18  ? 0.9134 0.6165 0.8883 0.1471  0.0877  0.0750  27  THR   B C   
392  O  O   . THR   B 18  ? 0.9083 0.6079 0.8931 0.1454  0.0958  0.0967  27  THR   B O   
393  C  CB  . THR   B 18  ? 0.8848 0.6368 0.8665 0.1283  0.0791  0.0587  27  THR   B CB  
394  O  OG1 . THR   B 18  ? 0.9160 0.6453 0.8977 0.1205  0.0695  0.0422  27  THR   B OG1 
395  C  CG2 . THR   B 18  ? 0.8747 0.6323 0.8783 0.1152  0.0831  0.0781  27  THR   B CG2 
396  N  N   . ARG   B 19  ? 0.9493 0.6244 0.9176 0.1490  0.0807  0.0600  28  ARG   B N   
397  C  CA  . ARG   B 19  ? 0.9915 0.6259 0.9648 0.1473  0.0802  0.0678  28  ARG   B CA  
398  C  C   . ARG   B 19  ? 1.0169 0.6307 1.0081 0.1246  0.0699  0.0615  28  ARG   B C   
399  O  O   . ARG   B 19  ? 1.0327 0.6074 1.0288 0.1207  0.0663  0.0644  28  ARG   B O   
400  C  CB  . ARG   B 19  ? 1.0320 0.6430 0.9844 0.1685  0.0785  0.0565  28  ARG   B CB  
401  C  CG  . ARG   B 19  ? 1.0906 0.7185 1.0280 0.1912  0.0867  0.0639  28  ARG   B CG  
402  C  CD  . ARG   B 19  ? 1.1744 0.7719 1.0960 0.2118  0.0863  0.0615  28  ARG   B CD  
403  N  NE  . ARG   B 19  ? 1.2342 0.8515 1.1410 0.2351  0.0911  0.0638  28  ARG   B NE  
404  C  CZ  . ARG   B 19  ? 1.2772 0.9144 1.1739 0.2490  0.0874  0.0454  28  ARG   B CZ  
405  N  NH1 . ARG   B 19  ? 1.2809 0.9213 1.1780 0.2436  0.0809  0.0243  28  ARG   B NH1 
406  N  NH2 . ARG   B 19  ? 1.2733 0.9288 1.1600 0.2689  0.0900  0.0481  28  ARG   B NH2 
407  N  N   . ARG   B 20  ? 1.0181 0.6564 1.0185 0.1101  0.0639  0.0526  29  ARG   B N   
408  C  CA  . ARG   B 20  ? 1.0345 0.6591 1.0517 0.0890  0.0516  0.0441  29  ARG   B CA  
409  C  C   . ARG   B 20  ? 1.0248 0.6419 1.0728 0.0704  0.0545  0.0669  29  ARG   B C   
410  O  O   . ARG   B 20  ? 1.0287 0.6178 1.0930 0.0545  0.0443  0.0638  29  ARG   B O   
411  C  CB  . ARG   B 20  ? 1.0593 0.7156 1.0744 0.0822  0.0449  0.0293  29  ARG   B CB  
412  C  CG  . ARG   B 20  ? 1.1288 0.7704 1.1542 0.0648  0.0288  0.0141  29  ARG   B CG  
413  C  CD  . ARG   B 20  ? 1.1903 0.8658 1.2159 0.0574  0.0236  0.0057  29  ARG   B CD  
414  N  NE  . ARG   B 20  ? 1.2348 0.9418 1.2809 0.0488  0.0311  0.0258  29  ARG   B NE  
415  C  CZ  . ARG   B 20  ? 1.2640 0.9825 1.3351 0.0304  0.0240  0.0300  29  ARG   B CZ  
416  N  NH1 . ARG   B 20  ? 1.2706 0.9703 1.3499 0.0173  0.0077  0.0151  29  ARG   B NH1 
417  N  NH2 . ARG   B 20  ? 1.2452 0.9952 1.3333 0.0263  0.0322  0.0483  29  ARG   B NH2 
418  N  N   . LEU   B 21  ? 1.0092 0.6513 1.0654 0.0730  0.0685  0.0901  30  LEU   B N   
419  C  CA  . LEU   B 21  ? 0.9996 0.6415 1.0858 0.0573  0.0750  0.1153  30  LEU   B CA  
420  C  C   . LEU   B 21  ? 1.0090 0.6188 1.0916 0.0663  0.0854  0.1350  30  LEU   B C   
421  O  O   . LEU   B 21  ? 1.0299 0.6141 1.0875 0.0836  0.0839  0.1252  30  LEU   B O   
422  C  CB  . LEU   B 21  ? 0.9816 0.6706 1.0783 0.0561  0.0847  0.1296  30  LEU   B CB  
423  C  CG  . LEU   B 21  ? 0.9847 0.7006 1.0943 0.0417  0.0739  0.1165  30  LEU   B CG  
424  C  CD1 . LEU   B 21  ? 0.9982 0.7267 1.0794 0.0542  0.0678  0.0934  30  LEU   B CD1 
425  C  CD2 . LEU   B 21  ? 0.9713 0.7262 1.1022 0.0360  0.0833  0.1365  30  LEU   B CD2 
426  N  N   . LEU   B 22  ? 0.9885 0.5990 1.0962 0.0548  0.0957  0.1630  31  LEU   B N   
427  C  CA  . LEU   B 22  ? 0.9937 0.5733 1.0972 0.0629  0.1066  0.1849  31  LEU   B CA  
428  C  C   . LEU   B 22  ? 0.9949 0.5878 1.0660 0.0925  0.1186  0.1904  31  LEU   B C   
429  O  O   . LEU   B 22  ? 0.9935 0.6260 1.0625 0.0995  0.1280  0.1994  31  LEU   B O   
430  C  CB  . LEU   B 22  ? 0.9765 0.5642 1.1149 0.0444  0.1180  0.2164  31  LEU   B CB  
431  C  CG  . LEU   B 22  ? 0.9950 0.5504 1.1311 0.0502  0.1307  0.2433  31  LEU   B CG  
432  C  CD1 . LEU   B 22  ? 1.0013 0.5112 1.1627 0.0269  0.1211  0.2467  31  LEU   B CD1 
433  C  CD2 . LEU   B 22  ? 0.9888 0.5781 1.1356 0.0533  0.1519  0.2761  31  LEU   B CD2 
434  N  N   . GLY   B 23  ? 0.9943 0.5546 1.0397 0.1107  0.1164  0.1829  32  GLY   B N   
435  C  CA  . GLY   B 23  ? 0.9847 0.5566 0.9994 0.1396  0.1243  0.1843  32  GLY   B CA  
436  C  C   . GLY   B 23  ? 0.9545 0.5634 0.9559 0.1483  0.1188  0.1620  32  GLY   B C   
437  O  O   . GLY   B 23  ? 0.9473 0.5634 0.9560 0.1356  0.1075  0.1414  32  GLY   B O   
438  N  N   . SER   B 24  ? 0.9369 0.5683 0.9180 0.1701  0.1260  0.1662  33  SER   B N   
439  C  CA  . SER   B 24  ? 0.9195 0.5852 0.8894 0.1777  0.1210  0.1475  33  SER   B CA  
440  C  C   . SER   B 24  ? 0.8913 0.5936 0.8721 0.1712  0.1275  0.1597  33  SER   B C   
441  O  O   . SER   B 24  ? 0.8933 0.6025 0.8722 0.1797  0.1393  0.1821  33  SER   B O   
442  C  CB  . SER   B 24  ? 0.9417 0.6097 0.8847 0.2053  0.1219  0.1422  33  SER   B CB  
443  O  OG  . SER   B 24  ? 0.9829 0.6198 0.9157 0.2137  0.1156  0.1298  33  SER   B OG  
444  N  N   . THR   B 25  ? 0.8629 0.5880 0.8536 0.1576  0.1201  0.1456  34  THR   B N   
445  C  CA  . THR   B 25  ? 0.8356 0.5945 0.8373 0.1517  0.1249  0.1558  34  THR   B CA  
446  C  C   . THR   B 25  ? 0.8091 0.5962 0.7954 0.1611  0.1199  0.1409  34  THR   B C   
447  O  O   . THR   B 25  ? 0.8125 0.5994 0.7939 0.1572  0.1099  0.1197  34  THR   B O   
448  C  CB  . THR   B 25  ? 0.8444 0.6051 0.8757 0.1253  0.1204  0.1567  34  THR   B CB  
449  O  OG1 . THR   B 25  ? 0.8627 0.5936 0.9103 0.1148  0.1236  0.1703  34  THR   B OG1 
450  C  CG2 . THR   B 25  ? 0.8316 0.6283 0.8774 0.1196  0.1256  0.1684  34  THR   B CG2 
451  N  N   . GLN   B 26  ? 0.7828 0.5932 0.7611 0.1737  0.1266  0.1519  35  GLN   B N   
452  C  CA  . GLN   B 26  ? 0.7700 0.6035 0.7345 0.1819  0.1206  0.1386  35  GLN   B CA  
453  C  C   . GLN   B 26  ? 0.7601 0.6150 0.7386 0.1659  0.1157  0.1339  35  GLN   B C   
454  O  O   . GLN   B 26  ? 0.7608 0.6332 0.7491 0.1646  0.1219  0.1484  35  GLN   B O   
455  C  CB  . GLN   B 26  ? 0.7688 0.6145 0.7144 0.2048  0.1266  0.1489  35  GLN   B CB  
456  C  CG  . GLN   B 26  ? 0.7573 0.6217 0.6891 0.2126  0.1179  0.1337  35  GLN   B CG  
457  C  CD  . GLN   B 26  ? 0.7634 0.6380 0.6757 0.2356  0.1212  0.1417  35  GLN   B CD  
458  O  OE1 . GLN   B 26  ? 0.7808 0.6444 0.6784 0.2532  0.1244  0.1471  35  GLN   B OE1 
459  N  NE2 . GLN   B 26  ? 0.7482 0.6428 0.6577 0.2377  0.1191  0.1417  35  GLN   B NE2 
460  N  N   . VAL   B 27  ? 0.7419 0.5968 0.7201 0.1558  0.1051  0.1141  36  VAL   B N   
461  C  CA  . VAL   B 27  ? 0.7194 0.5921 0.7077 0.1418  0.0990  0.1083  36  VAL   B CA  
462  C  C   . VAL   B 27  ? 0.7083 0.6029 0.6831 0.1514  0.0964  0.1051  36  VAL   B C   
463  O  O   . VAL   B 27  ? 0.7021 0.6130 0.6837 0.1438  0.0930  0.1049  36  VAL   B O   
464  C  CB  . VAL   B 27  ? 0.7236 0.5850 0.7145 0.1278  0.0889  0.0896  36  VAL   B CB  
465  C  CG1 . VAL   B 27  ? 0.7322 0.5679 0.7356 0.1188  0.0891  0.0914  36  VAL   B CG1 
466  C  CG2 . VAL   B 27  ? 0.7303 0.5901 0.7014 0.1368  0.0844  0.0730  36  VAL   B CG2 
467  N  N   . GLY   B 28  ? 0.7019 0.5955 0.6579 0.1681  0.0966  0.1016  37  GLY   B N   
468  C  CA  . GLY   B 28  ? 0.6928 0.6019 0.6355 0.1770  0.0918  0.0967  37  GLY   B CA  
469  C  C   . GLY   B 28  ? 0.6896 0.5950 0.6149 0.1935  0.0895  0.0903  37  GLY   B C   
470  O  O   . GLY   B 28  ? 0.6965 0.5896 0.6181 0.2025  0.0935  0.0932  37  GLY   B O   
471  N  N   . VAL   B 29  ? 0.6771 0.5926 0.5923 0.1975  0.0818  0.0819  38  VAL   B N   
472  C  CA  . VAL   B 29  ? 0.6738 0.5904 0.5747 0.2122  0.0762  0.0747  38  VAL   B CA  
473  C  C   . VAL   B 29  ? 0.6607 0.5836 0.5612 0.2023  0.0664  0.0601  38  VAL   B C   
474  O  O   . VAL   B 29  ? 0.6588 0.5858 0.5645 0.1883  0.0643  0.0580  38  VAL   B O   
475  C  CB  . VAL   B 29  ? 0.6822 0.6051 0.5701 0.2301  0.0770  0.0843  38  VAL   B CB  
476  C  CG1 . VAL   B 29  ? 0.6963 0.6201 0.5689 0.2453  0.0674  0.0752  38  VAL   B CG1 
477  C  CG2 . VAL   B 29  ? 0.6848 0.6034 0.5721 0.2406  0.0889  0.1015  38  VAL   B CG2 
478  N  N   . GLY   B 30  ? 0.6501 0.5747 0.5452 0.2096  0.0604  0.0509  39  GLY   B N   
479  C  CA  . GLY   B 30  ? 0.6463 0.5780 0.5431 0.2001  0.0522  0.0396  39  GLY   B CA  
480  C  C   . GLY   B 30  ? 0.6508 0.5868 0.5425 0.2112  0.0434  0.0326  39  GLY   B C   
481  O  O   . GLY   B 30  ? 0.6533 0.5868 0.5389 0.2279  0.0433  0.0345  39  GLY   B O   
482  N  N   . VAL   B 31  ? 0.6517 0.5941 0.5464 0.2017  0.0354  0.0249  40  VAL   B N   
483  C  CA  . VAL   B 31  ? 0.6595 0.6069 0.5539 0.2086  0.0245  0.0173  40  VAL   B CA  
484  C  C   . VAL   B 31  ? 0.6578 0.6169 0.5669 0.1978  0.0238  0.0086  40  VAL   B C   
485  O  O   . VAL   B 31  ? 0.6610 0.6242 0.5761 0.1813  0.0261  0.0074  40  VAL   B O   
486  C  CB  . VAL   B 31  ? 0.6734 0.6170 0.5598 0.2072  0.0138  0.0167  40  VAL   B CB  
487  C  CG1 . VAL   B 31  ? 0.6820 0.6289 0.5709 0.2114  -0.0001 0.0075  40  VAL   B CG1 
488  C  CG2 . VAL   B 31  ? 0.6830 0.6185 0.5537 0.2215  0.0152  0.0251  40  VAL   B CG2 
489  N  N   . MET   B 32  ? 0.6544 0.6207 0.5691 0.2083  0.0207  0.0029  41  MET   B N   
490  C  CA  . MET   B 32  ? 0.6487 0.6318 0.5805 0.2005  0.0200  -0.0053 41  MET   B CA  
491  C  C   . MET   B 32  ? 0.6578 0.6482 0.5961 0.1980  0.0056  -0.0107 41  MET   B C   
492  O  O   . MET   B 32  ? 0.6650 0.6515 0.5966 0.2132  -0.0046 -0.0131 41  MET   B O   
493  C  CB  . MET   B 32  ? 0.6425 0.6305 0.5781 0.2153  0.0232  -0.0088 41  MET   B CB  
494  C  CG  . MET   B 32  ? 0.6466 0.6557 0.6011 0.2095  0.0249  -0.0170 41  MET   B CG  
495  S  SD  . MET   B 32  ? 0.6886 0.6999 0.6462 0.1938  0.0390  -0.0167 41  MET   B SD  
496  C  CE  . MET   B 32  ? 0.6743 0.6640 0.6187 0.2072  0.0471  -0.0129 41  MET   B CE  
497  N  N   . GLN   B 33  ? 0.6554 0.6544 0.6053 0.1793  0.0041  -0.0122 42  GLN   B N   
498  C  CA  . GLN   B 33  ? 0.6594 0.6635 0.6193 0.1737  -0.0105 -0.0168 42  GLN   B CA  
499  C  C   . GLN   B 33  ? 0.6497 0.6726 0.6307 0.1541  -0.0069 -0.0178 42  GLN   B C   
500  O  O   . GLN   B 33  ? 0.6624 0.6836 0.6402 0.1409  0.0029  -0.0124 42  GLN   B O   
501  C  CB  . GLN   B 33  ? 0.6959 0.6799 0.6400 0.1723  -0.0200 -0.0136 42  GLN   B CB  
502  C  CG  . GLN   B 33  ? 0.7561 0.7403 0.7096 0.1685  -0.0381 -0.0200 42  GLN   B CG  
503  C  CD  . GLN   B 33  ? 0.8436 0.8042 0.7783 0.1711  -0.0493 -0.0186 42  GLN   B CD  
504  O  OE1 . GLN   B 33  ? 0.8660 0.8190 0.8042 0.1554  -0.0557 -0.0172 42  GLN   B OE1 
505  N  NE2 . GLN   B 33  ? 0.8720 0.8202 0.7852 0.1921  -0.0514 -0.0181 42  GLN   B NE2 
506  N  N   . GLU   B 34  ? 0.6303 0.6729 0.6334 0.1526  -0.0144 -0.0241 43  GLU   B N   
507  C  CA  . GLU   B 34  ? 0.6164 0.6829 0.6444 0.1343  -0.0098 -0.0236 43  GLU   B CA  
508  C  C   . GLU   B 34  ? 0.6089 0.6888 0.6379 0.1317  0.0095  -0.0213 43  GLU   B C   
509  O  O   . GLU   B 34  ? 0.6107 0.6987 0.6446 0.1155  0.0182  -0.0162 43  GLU   B O   
510  C  CB  . GLU   B 34  ? 0.6536 0.7102 0.6829 0.1142  -0.0156 -0.0179 43  GLU   B CB  
511  C  CG  . GLU   B 34  ? 0.7210 0.7608 0.7483 0.1163  -0.0367 -0.0217 43  GLU   B CG  
512  C  CD  . GLU   B 34  ? 0.8304 0.8494 0.8499 0.1003  -0.0426 -0.0153 43  GLU   B CD  
513  O  OE1 . GLU   B 34  ? 0.8461 0.8733 0.8748 0.0812  -0.0331 -0.0077 43  GLU   B OE1 
514  O  OE2 . GLU   B 34  ? 0.8673 0.8612 0.8693 0.1086  -0.0568 -0.0177 43  GLU   B OE2 
515  N  N   . GLY   B 35  ? 0.6012 0.6804 0.6228 0.1489  0.0155  -0.0248 44  GLY   B N   
516  C  CA  . GLY   B 35  ? 0.5898 0.6775 0.6098 0.1506  0.0314  -0.0252 44  GLY   B CA  
517  C  C   . GLY   B 35  ? 0.5967 0.6639 0.5952 0.1449  0.0404  -0.0198 44  GLY   B C   
518  O  O   . GLY   B 35  ? 0.6042 0.6756 0.5992 0.1452  0.0520  -0.0213 44  GLY   B O   
519  N  N   . VAL   B 36  ? 0.5905 0.6362 0.5746 0.1405  0.0342  -0.0144 45  VAL   B N   
520  C  CA  . VAL   B 36  ? 0.5865 0.6151 0.5529 0.1346  0.0405  -0.0093 45  VAL   B CA  
521  C  C   . VAL   B 36  ? 0.5891 0.5965 0.5405 0.1473  0.0383  -0.0069 45  VAL   B C   
522  O  O   . VAL   B 36  ? 0.5889 0.5891 0.5371 0.1562  0.0292  -0.0060 45  VAL   B O   
523  C  CB  . VAL   B 36  ? 0.5897 0.6142 0.5529 0.1178  0.0371  -0.0034 45  VAL   B CB  
524  C  CG1 . VAL   B 36  ? 0.6054 0.6121 0.5496 0.1137  0.0405  0.0016  45  VAL   B CG1 
525  C  CG2 . VAL   B 36  ? 0.5805 0.6270 0.5580 0.1045  0.0433  -0.0029 45  VAL   B CG2 
526  N  N   . PHE   B 37  ? 0.5859 0.5840 0.5287 0.1489  0.0467  -0.0059 46  PHE   B N   
527  C  CA  . PHE   B 37  ? 0.5923 0.5723 0.5244 0.1579  0.0467  -0.0011 46  PHE   B CA  
528  C  C   . PHE   B 37  ? 0.5914 0.5616 0.5142 0.1477  0.0457  0.0049  46  PHE   B C   
529  O  O   . PHE   B 37  ? 0.5910 0.5620 0.5116 0.1367  0.0499  0.0041  46  PHE   B O   
530  C  CB  . PHE   B 37  ? 0.5981 0.5715 0.5291 0.1645  0.0547  -0.0032 46  PHE   B CB  
531  C  CG  . PHE   B 37  ? 0.6221 0.5785 0.5459 0.1739  0.0553  0.0040  46  PHE   B CG  
532  C  CD1 . PHE   B 37  ? 0.6300 0.5842 0.5511 0.1885  0.0513  0.0073  46  PHE   B CD1 
533  C  CD2 . PHE   B 37  ? 0.6419 0.5857 0.5620 0.1677  0.0596  0.0083  46  PHE   B CD2 
534  C  CE1 . PHE   B 37  ? 0.6463 0.5868 0.5600 0.1976  0.0540  0.0164  46  PHE   B CE1 
535  C  CE2 . PHE   B 37  ? 0.6552 0.5864 0.5724 0.1746  0.0615  0.0174  46  PHE   B CE2 
536  C  CZ  . PHE   B 37  ? 0.6509 0.5808 0.5643 0.1899  0.0600  0.0223  46  PHE   B CZ  
537  N  N   . HIS   B 38  ? 0.5881 0.5500 0.5041 0.1529  0.0394  0.0103  47  HIS   B N   
538  C  CA  . HIS   B 38  ? 0.5850 0.5393 0.4926 0.1463  0.0371  0.0160  47  HIS   B CA  
539  C  C   . HIS   B 38  ? 0.5901 0.5363 0.4939 0.1542  0.0410  0.0226  47  HIS   B C   
540  O  O   . HIS   B 38  ? 0.5925 0.5360 0.4941 0.1681  0.0406  0.0256  47  HIS   B O   
541  C  CB  . HIS   B 38  ? 0.5883 0.5397 0.4908 0.1487  0.0265  0.0171  47  HIS   B CB  
542  C  CG  . HIS   B 38  ? 0.5992 0.5583 0.5096 0.1410  0.0211  0.0120  47  HIS   B CG  
543  N  ND1 . HIS   B 38  ? 0.6068 0.5760 0.5280 0.1472  0.0194  0.0063  47  HIS   B ND1 
544  C  CD2 . HIS   B 38  ? 0.6096 0.5686 0.5202 0.1274  0.0171  0.0129  47  HIS   B CD2 
545  C  CE1 . HIS   B 38  ? 0.6072 0.5844 0.5380 0.1358  0.0147  0.0039  47  HIS   B CE1 
546  N  NE2 . HIS   B 38  ? 0.6149 0.5850 0.5391 0.1232  0.0137  0.0085  47  HIS   B NE2 
547  N  N   . THR   B 39  ? 0.5887 0.5318 0.4920 0.1457  0.0443  0.0257  48  THR   B N   
548  C  CA  . THR   B 39  ? 0.5890 0.5275 0.4936 0.1506  0.0481  0.0337  48  THR   B CA  
549  C  C   . THR   B 39  ? 0.5810 0.5206 0.4845 0.1409  0.0459  0.0370  48  THR   B C   
550  O  O   . THR   B 39  ? 0.5745 0.5156 0.4724 0.1330  0.0409  0.0337  48  THR   B O   
551  C  CB  . THR   B 39  ? 0.6074 0.5403 0.5191 0.1531  0.0555  0.0337  48  THR   B CB  
552  O  OG1 . THR   B 39  ? 0.6149 0.5440 0.5301 0.1583  0.0598  0.0443  48  THR   B OG1 
553  C  CG2 . THR   B 39  ? 0.6158 0.5462 0.5310 0.1408  0.0574  0.0264  48  THR   B CG2 
554  N  N   . MET   B 40  ? 0.5769 0.5167 0.4865 0.1420  0.0492  0.0446  49  MET   B N   
555  C  CA  . MET   B 40  ? 0.5776 0.5215 0.4894 0.1338  0.0463  0.0474  49  MET   B CA  
556  C  C   . MET   B 40  ? 0.5842 0.5251 0.5031 0.1211  0.0473  0.0419  49  MET   B C   
557  O  O   . MET   B 40  ? 0.5922 0.5269 0.5183 0.1210  0.0521  0.0409  49  MET   B O   
558  C  CB  . MET   B 40  ? 0.5779 0.5283 0.4960 0.1418  0.0492  0.0589  49  MET   B CB  
559  C  CG  . MET   B 40  ? 0.6040 0.5557 0.5115 0.1586  0.0484  0.0632  49  MET   B CG  
560  S  SD  . MET   B 40  ? 0.6509 0.6140 0.5565 0.1685  0.0471  0.0731  49  MET   B SD  
561  C  CE  . MET   B 40  ? 0.6207 0.5799 0.5145 0.1611  0.0350  0.0651  49  MET   B CE  
562  N  N   . TRP   B 41  ? 0.5862 0.5292 0.5006 0.1117  0.0418  0.0378  50  TRP   B N   
563  C  CA  A TRP   B 41  ? 0.5933 0.5327 0.5103 0.1011  0.0404  0.0305  50  TRP   B CA  
564  C  CA  B TRP   B 41  ? 0.5917 0.5310 0.5087 0.1011  0.0404  0.0304  50  TRP   B CA  
565  C  C   . TRP   B 41  ? 0.5955 0.5325 0.5296 0.0975  0.0418  0.0338  50  TRP   B C   
566  O  O   . TRP   B 41  ? 0.6035 0.5310 0.5408 0.0927  0.0422  0.0268  50  TRP   B O   
567  C  CB  A TRP   B 41  ? 0.5925 0.5353 0.4993 0.0940  0.0331  0.0273  50  TRP   B CB  
568  C  CB  B TRP   B 41  ? 0.5890 0.5315 0.4954 0.0938  0.0332  0.0268  50  TRP   B CB  
569  C  CG  A TRP   B 41  ? 0.5996 0.5375 0.5005 0.0861  0.0311  0.0169  50  TRP   B CG  
570  C  CG  B TRP   B 41  ? 0.5912 0.5293 0.4961 0.0851  0.0300  0.0176  50  TRP   B CG  
571  C  CD1 A TRP   B 41  ? 0.6169 0.5525 0.5044 0.0851  0.0335  0.0096  50  TRP   B CD1 
572  C  CD1 B TRP   B 41  ? 0.5961 0.5340 0.5127 0.0791  0.0252  0.0164  50  TRP   B CD1 
573  C  CD2 A TRP   B 41  ? 0.5985 0.5335 0.5070 0.0793  0.0262  0.0121  50  TRP   B CD2 
574  C  CD2 B TRP   B 41  ? 0.5972 0.5311 0.4881 0.0826  0.0310  0.0077  50  TRP   B CD2 
575  N  NE1 A TRP   B 41  ? 0.6254 0.5563 0.5077 0.0803  0.0308  0.0001  50  TRP   B NE1 
576  N  NE1 B TRP   B 41  ? 0.6037 0.5342 0.5123 0.0737  0.0214  0.0047  50  TRP   B NE1 
577  C  CE2 A TRP   B 41  ? 0.6158 0.5445 0.5108 0.0763  0.0250  0.0005  50  TRP   B CE2 
578  C  CE2 B TRP   B 41  ? 0.6065 0.5351 0.4978 0.0768  0.0258  -0.0005 50  TRP   B CE2 
579  C  CE3 A TRP   B 41  ? 0.5977 0.5362 0.5244 0.0753  0.0221  0.0166  50  TRP   B CE3 
580  C  CE3 B TRP   B 41  ? 0.6058 0.5413 0.4850 0.0847  0.0359  0.0052  50  TRP   B CE3 
581  C  CZ2 A TRP   B 41  ? 0.6240 0.5461 0.5200 0.0706  0.0181  -0.0086 50  TRP   B CZ2 
582  C  CZ2 B TRP   B 41  ? 0.6180 0.5418 0.4939 0.0758  0.0257  -0.0117 50  TRP   B CZ2 
583  C  CZ3 A TRP   B 41  ? 0.6083 0.5417 0.5404 0.0671  0.0150  0.0083  50  TRP   B CZ3 
584  C  CZ3 B TRP   B 41  ? 0.6210 0.5553 0.4882 0.0825  0.0376  -0.0040 50  TRP   B CZ3 
585  C  CH2 A TRP   B 41  ? 0.6183 0.5420 0.5336 0.0653  0.0120  -0.0050 50  TRP   B CH2 
586  C  CH2 B TRP   B 41  ? 0.6229 0.5508 0.4862 0.0794  0.0327  -0.0127 50  TRP   B CH2 
587  N  N   . HIS   B 42  ? 0.5910 0.5367 0.5368 0.0998  0.0424  0.0445  51  HIS   B N   
588  C  CA  . HIS   B 42  ? 0.5928 0.5388 0.5596 0.0939  0.0442  0.0502  51  HIS   B CA  
589  C  C   . HIS   B 42  ? 0.6111 0.5451 0.5850 0.0976  0.0523  0.0540  51  HIS   B C   
590  O  O   . HIS   B 42  ? 0.6103 0.5391 0.6018 0.0903  0.0534  0.0579  51  HIS   B O   
591  C  CB  . HIS   B 42  ? 0.5842 0.5479 0.5640 0.0962  0.0445  0.0624  51  HIS   B CB  
592  C  CG  . HIS   B 42  ? 0.5958 0.5651 0.5751 0.1103  0.0534  0.0747  51  HIS   B CG  
593  N  ND1 . HIS   B 42  ? 0.6181 0.5918 0.5803 0.1228  0.0523  0.0755  51  HIS   B ND1 
594  C  CD2 . HIS   B 42  ? 0.5975 0.5674 0.5900 0.1143  0.0628  0.0866  51  HIS   B CD2 
595  C  CE1 . HIS   B 42  ? 0.6184 0.5959 0.5820 0.1354  0.0605  0.0862  51  HIS   B CE1 
596  N  NE2 . HIS   B 42  ? 0.6121 0.5882 0.5932 0.1310  0.0680  0.0942  51  HIS   B NE2 
597  N  N   . VAL   B 43  ? 0.6222 0.5511 0.5831 0.1088  0.0570  0.0531  52  VAL   B N   
598  C  CA  . VAL   B 43  ? 0.6309 0.5476 0.5944 0.1154  0.0640  0.0565  52  VAL   B CA  
599  C  C   . VAL   B 43  ? 0.6418 0.5424 0.6027 0.1099  0.0617  0.0436  52  VAL   B C   
600  O  O   . VAL   B 43  ? 0.6465 0.5328 0.6175 0.1065  0.0634  0.0454  52  VAL   B O   
601  C  CB  . VAL   B 43  ? 0.6444 0.5641 0.5946 0.1313  0.0675  0.0593  52  VAL   B CB  
602  C  CG1 . VAL   B 43  ? 0.6549 0.5613 0.6036 0.1401  0.0731  0.0600  52  VAL   B CG1 
603  C  CG2 . VAL   B 43  ? 0.6449 0.5774 0.5956 0.1401  0.0701  0.0720  52  VAL   B CG2 
604  N  N   . THR   B 44  ? 0.6429 0.5455 0.5902 0.1092  0.0578  0.0311  53  THR   B N   
605  C  CA  . THR   B 44  ? 0.6534 0.5437 0.5950 0.1076  0.0566  0.0181  53  THR   B CA  
606  C  C   . THR   B 44  ? 0.6698 0.5569 0.6095 0.0961  0.0491  0.0080  53  THR   B C   
607  O  O   . THR   B 44  ? 0.6830 0.5560 0.6195 0.0951  0.0471  -0.0026 53  THR   B O   
608  C  CB  . THR   B 44  ? 0.6605 0.5572 0.5891 0.1160  0.0591  0.0111  53  THR   B CB  
609  O  OG1 . THR   B 44  ? 0.6648 0.5741 0.5844 0.1107  0.0556  0.0071  53  THR   B OG1 
610  C  CG2 . THR   B 44  ? 0.6649 0.5661 0.5938 0.1283  0.0634  0.0190  53  THR   B CG2 
611  N  N   . LYS   B 45  ? 0.6686 0.5680 0.6078 0.0895  0.0440  0.0102  54  LYS   B N   
612  C  CA  . LYS   B 45  ? 0.6865 0.5855 0.6201 0.0805  0.0354  0.0005  54  LYS   B CA  
613  C  C   . LYS   B 45  ? 0.6998 0.5983 0.6125 0.0834  0.0358  -0.0119 54  LYS   B C   
614  O  O   . LYS   B 45  ? 0.7063 0.5991 0.6098 0.0794  0.0297  -0.0228 54  LYS   B O   
615  C  CB  . LYS   B 45  ? 0.7168 0.6019 0.6642 0.0721  0.0291  -0.0037 54  LYS   B CB  
616  C  CG  . LYS   B 45  ? 0.7712 0.6606 0.7432 0.0671  0.0299  0.0105  54  LYS   B CG  
617  C  CD  . LYS   B 45  ? 0.8411 0.7490 0.8191 0.0613  0.0238  0.0149  54  LYS   B CD  
618  C  CE  . LYS   B 45  ? 0.9020 0.8166 0.9090 0.0542  0.0236  0.0272  54  LYS   B CE  
619  N  NZ  . LYS   B 45  ? 0.9346 0.8574 0.9486 0.0631  0.0358  0.0439  54  LYS   B NZ  
620  N  N   . GLY   B 46  ? 0.7027 0.6084 0.6083 0.0909  0.0428  -0.0099 55  GLY   B N   
621  C  CA  . GLY   B 46  ? 0.7188 0.6288 0.6088 0.0941  0.0461  -0.0188 55  GLY   B CA  
622  C  C   . GLY   B 46  ? 0.7386 0.6379 0.6263 0.1005  0.0492  -0.0292 55  GLY   B C   
623  O  O   . GLY   B 46  ? 0.7493 0.6533 0.6239 0.1041  0.0522  -0.0381 55  GLY   B O   
624  N  N   . ALA   B 47  ? 0.7450 0.6295 0.6446 0.1030  0.0490  -0.0278 56  ALA   B N   
625  C  CA  . ALA   B 47  ? 0.7604 0.6302 0.6570 0.1110  0.0509  -0.0376 56  ALA   B CA  
626  C  C   . ALA   B 47  ? 0.7654 0.6454 0.6613 0.1228  0.0592  -0.0365 56  ALA   B C   
627  O  O   . ALA   B 47  ? 0.7649 0.6562 0.6675 0.1243  0.0620  -0.0262 56  ALA   B O   
628  C  CB  . ALA   B 47  ? 0.7662 0.6142 0.6764 0.1089  0.0478  -0.0339 56  ALA   B CB  
629  N  N   . ALA   B 48  ? 0.7701 0.6465 0.6581 0.1324  0.0622  -0.0477 57  ALA   B N   
630  C  CA  . ALA   B 48  ? 0.7768 0.6656 0.6669 0.1445  0.0691  -0.0479 57  ALA   B CA  
631  C  C   . ALA   B 48  ? 0.7917 0.6682 0.6923 0.1518  0.0698  -0.0397 57  ALA   B C   
632  O  O   . ALA   B 48  ? 0.8018 0.6549 0.7059 0.1501  0.0666  -0.0376 57  ALA   B O   
633  C  CB  . ALA   B 48  ? 0.7828 0.6714 0.6621 0.1551  0.0721  -0.0623 57  ALA   B CB  
634  N  N   . LEU   B 49  ? 0.7916 0.6839 0.6976 0.1596  0.0735  -0.0345 58  LEU   B N   
635  C  CA  . LEU   B 49  ? 0.8031 0.6859 0.7152 0.1695  0.0743  -0.0263 58  LEU   B CA  
636  C  C   . LEU   B 49  ? 0.8165 0.7018 0.7275 0.1861  0.0772  -0.0336 58  LEU   B C   
637  O  O   . LEU   B 49  ? 0.8128 0.7178 0.7229 0.1895  0.0796  -0.0424 58  LEU   B O   
638  C  CB  . LEU   B 49  ? 0.7989 0.6965 0.7162 0.1683  0.0737  -0.0151 58  LEU   B CB  
639  C  CG  . LEU   B 49  ? 0.8121 0.7113 0.7303 0.1547  0.0709  -0.0076 58  LEU   B CG  
640  C  CD1 . LEU   B 49  ? 0.8133 0.7253 0.7334 0.1574  0.0696  0.0010  58  LEU   B CD1 
641  C  CD2 . LEU   B 49  ? 0.8247 0.7037 0.7470 0.1496  0.0701  -0.0012 58  LEU   B CD2 
642  N  N   . ARG   B 50  ? 0.8332 0.6998 0.7448 0.1972  0.0774  -0.0291 59  ARG   B N   
643  C  CA  . ARG   B 50  ? 0.8482 0.7146 0.7581 0.2156  0.0790  -0.0355 59  ARG   B CA  
644  C  C   . ARG   B 50  ? 0.8540 0.7313 0.7683 0.2265  0.0786  -0.0267 59  ARG   B C   
645  O  O   . ARG   B 50  ? 0.8532 0.7222 0.7677 0.2237  0.0780  -0.0140 59  ARG   B O   
646  C  CB  . ARG   B 50  ? 0.8858 0.7166 0.7895 0.2217  0.0779  -0.0380 59  ARG   B CB  
647  C  CG  . ARG   B 50  ? 0.9497 0.7710 0.8498 0.2432  0.0787  -0.0405 59  ARG   B CG  
648  C  CD  . ARG   B 50  ? 1.0177 0.7996 0.9099 0.2483  0.0765  -0.0447 59  ARG   B CD  
649  N  NE  . ARG   B 50  ? 1.0741 0.8275 0.9695 0.2355  0.0750  -0.0317 59  ARG   B NE  
650  C  CZ  . ARG   B 50  ? 1.1200 0.8540 1.0161 0.2415  0.0767  -0.0167 59  ARG   B CZ  
651  N  NH1 . ARG   B 50  ? 1.1151 0.8530 1.0062 0.2615  0.0786  -0.0140 59  ARG   B NH1 
652  N  NH2 . ARG   B 50  ? 1.1326 0.8448 1.0350 0.2278  0.0768  -0.0037 59  ARG   B NH2 
653  N  N   . SER   B 51  ? 0.8588 0.7577 0.7769 0.2389  0.0786  -0.0334 60  SER   B N   
654  C  CA  . SER   B 51  ? 0.8764 0.7861 0.7979 0.2508  0.0756  -0.0275 60  SER   B CA  
655  C  C   . SER   B 51  ? 0.9013 0.8086 0.8213 0.2722  0.0754  -0.0338 60  SER   B C   
656  O  O   . SER   B 51  ? 0.8971 0.8312 0.8257 0.2795  0.0748  -0.0432 60  SER   B O   
657  C  CB  . SER   B 51  ? 0.8788 0.8217 0.8106 0.2439  0.0727  -0.0296 60  SER   B CB  
658  O  OG  . SER   B 51  ? 0.9073 0.8552 0.8398 0.2536  0.0672  -0.0236 60  SER   B OG  
659  N  N   . GLY   B 52  ? 0.9205 0.7955 0.8307 0.2818  0.0762  -0.0282 61  GLY   B N   
660  C  CA  . GLY   B 52  ? 0.9307 0.7962 0.8362 0.3036  0.0755  -0.0338 61  GLY   B CA  
661  C  C   . GLY   B 52  ? 0.9369 0.8008 0.8414 0.3037  0.0778  -0.0481 61  GLY   B C   
662  O  O   . GLY   B 52  ? 0.9505 0.7905 0.8491 0.2925  0.0790  -0.0492 61  GLY   B O   
663  N  N   . GLU   B 53  ? 0.9227 0.8154 0.8340 0.3158  0.0781  -0.0597 62  GLU   B N   
664  C  CA  . GLU   B 53  ? 0.9229 0.8204 0.8320 0.3193  0.0815  -0.0742 62  GLU   B CA  
665  C  C   . GLU   B 53  ? 0.9048 0.8290 0.8203 0.2998  0.0855  -0.0782 62  GLU   B C   
666  O  O   . GLU   B 53  ? 0.9157 0.8340 0.8231 0.2974  0.0884  -0.0877 62  GLU   B O   
667  C  CB  . GLU   B 53  ? 0.9527 0.8741 0.8680 0.3429  0.0815  -0.0838 62  GLU   B CB  
668  C  CG  . GLU   B 53  ? 1.0338 0.9442 0.9390 0.3576  0.0841  -0.0979 62  GLU   B CG  
669  C  CD  . GLU   B 53  ? 1.1185 1.0542 1.0308 0.3837  0.0841  -0.1070 62  GLU   B CD  
670  O  OE1 . GLU   B 53  ? 1.1408 1.0857 1.0495 0.3956  0.0881  -0.1204 62  GLU   B OE1 
671  O  OE2 . GLU   B 53  ? 1.1343 1.0821 1.0551 0.3938  0.0795  -0.1012 62  GLU   B OE2 
672  N  N   . GLY   B 54  ? 0.8777 0.8288 0.8055 0.2872  0.0848  -0.0713 63  GLY   B N   
673  C  CA  . GLY   B 54  ? 0.8598 0.8364 0.7938 0.2690  0.0884  -0.0726 63  GLY   B CA  
674  C  C   . GLY   B 54  ? 0.8553 0.8118 0.7797 0.2494  0.0883  -0.0679 63  GLY   B C   
675  O  O   . GLY   B 54  ? 0.8772 0.8029 0.7946 0.2459  0.0849  -0.0607 63  GLY   B O   
676  N  N   . ARG   B 55  ? 0.8239 0.7998 0.7489 0.2366  0.0922  -0.0708 64  ARG   B N   
677  C  CA  . ARG   B 55  ? 0.8171 0.7780 0.7328 0.2188  0.0911  -0.0673 64  ARG   B CA  
678  C  C   . ARG   B 55  ? 0.7754 0.7583 0.6986 0.2020  0.0910  -0.0592 64  ARG   B C   
679  O  O   . ARG   B 55  ? 0.7612 0.7750 0.6935 0.2000  0.0950  -0.0604 64  ARG   B O   
680  C  CB  . ARG   B 55  ? 0.8465 0.8019 0.7482 0.2202  0.0945  -0.0791 64  ARG   B CB  
681  C  CG  . ARG   B 55  ? 0.9097 0.8467 0.8002 0.2041  0.0910  -0.0777 64  ARG   B CG  
682  C  CD  . ARG   B 55  ? 0.9762 0.9136 0.8507 0.2072  0.0939  -0.0905 64  ARG   B CD  
683  N  NE  . ARG   B 55  ? 1.0400 0.9592 0.9028 0.1935  0.0883  -0.0910 64  ARG   B NE  
684  C  CZ  . ARG   B 55  ? 1.0933 0.9894 0.9397 0.1971  0.0838  -0.1032 64  ARG   B CZ  
685  N  NH1 . ARG   B 55  ? 1.1019 0.9869 0.9399 0.2148  0.0846  -0.1157 64  ARG   B NH1 
686  N  NH2 . ARG   B 55  ? 1.0954 0.9781 0.9333 0.1842  0.0770  -0.1038 64  ARG   B NH2 
687  N  N   . LEU   B 56  ? 0.7533 0.7202 0.6733 0.1899  0.0864  -0.0505 65  LEU   B N   
688  C  CA  . LEU   B 56  ? 0.7281 0.7085 0.6515 0.1749  0.0848  -0.0430 65  LEU   B CA  
689  C  C   . LEU   B 56  ? 0.7185 0.6894 0.6295 0.1628  0.0850  -0.0442 65  LEU   B C   
690  O  O   . LEU   B 56  ? 0.7276 0.6745 0.6323 0.1602  0.0813  -0.0434 65  LEU   B O   
691  C  CB  . LEU   B 56  ? 0.7294 0.6992 0.6562 0.1731  0.0787  -0.0325 65  LEU   B CB  
692  C  CG  . LEU   B 56  ? 0.7480 0.7175 0.6812 0.1878  0.0764  -0.0306 65  LEU   B CG  
693  C  CD1 . LEU   B 56  ? 0.7644 0.7194 0.6950 0.1877  0.0720  -0.0201 65  LEU   B CD1 
694  C  CD2 . LEU   B 56  ? 0.7448 0.7430 0.6907 0.1911  0.0754  -0.0336 65  LEU   B CD2 
695  N  N   . ASP   B 57  ? 0.7017 0.6917 0.6100 0.1551  0.0889  -0.0453 66  ASP   B N   
696  C  CA  . ASP   B 57  ? 0.7063 0.6886 0.5998 0.1451  0.0883  -0.0465 66  ASP   B CA  
697  C  C   . ASP   B 57  ? 0.6894 0.6745 0.5834 0.1313  0.0843  -0.0359 66  ASP   B C   
698  O  O   . ASP   B 57  ? 0.6863 0.6862 0.5909 0.1282  0.0843  -0.0295 66  ASP   B O   
699  C  CB  . ASP   B 57  ? 0.7441 0.7434 0.6286 0.1484  0.0964  -0.0543 66  ASP   B CB  
700  C  CG  . ASP   B 57  ? 0.8435 0.8363 0.7235 0.1644  0.0992  -0.0666 66  ASP   B CG  
701  O  OD1 . ASP   B 57  ? 0.8772 0.8424 0.7468 0.1672  0.0936  -0.0730 66  ASP   B OD1 
702  O  OD2 . ASP   B 57  ? 0.8749 0.8902 0.7631 0.1744  0.1062  -0.0700 66  ASP   B OD2 
703  N  N   . PRO   B 58  ? 0.6779 0.6477 0.5616 0.1234  0.0792  -0.0343 67  PRO   B N   
704  C  CA  . PRO   B 58  ? 0.6663 0.6381 0.5490 0.1124  0.0748  -0.0245 67  PRO   B CA  
705  C  C   . PRO   B 58  ? 0.6554 0.6452 0.5327 0.1058  0.0796  -0.0217 67  PRO   B C   
706  O  O   . PRO   B 58  ? 0.6621 0.6617 0.5313 0.1082  0.0866  -0.0276 67  PRO   B O   
707  C  CB  . PRO   B 58  ? 0.6827 0.6369 0.5563 0.1076  0.0684  -0.0255 67  PRO   B CB  
708  C  CG  . PRO   B 58  ? 0.6937 0.6401 0.5587 0.1129  0.0700  -0.0375 67  PRO   B CG  
709  C  CD  . PRO   B 58  ? 0.6739 0.6245 0.5468 0.1243  0.0759  -0.0422 67  PRO   B CD  
710  N  N   . TYR   B 59  ? 0.6356 0.6296 0.5172 0.0981  0.0764  -0.0123 68  TYR   B N   
711  C  CA  . TYR   B 59  ? 0.6185 0.6273 0.4974 0.0897  0.0809  -0.0067 68  TYR   B CA  
712  C  C   . TYR   B 59  ? 0.6150 0.6129 0.4808 0.0805  0.0749  0.0011  68  TYR   B C   
713  O  O   . TYR   B 59  ? 0.6222 0.6246 0.4748 0.0748  0.0788  0.0042  68  TYR   B O   
714  C  CB  . TYR   B 59  ? 0.6002 0.6240 0.4991 0.0889  0.0814  -0.0029 68  TYR   B CB  
715  C  CG  . TYR   B 59  ? 0.5947 0.6345 0.4974 0.0777  0.0858  0.0049  68  TYR   B CG  
716  C  CD1 . TYR   B 59  ? 0.6118 0.6413 0.5083 0.0670  0.0797  0.0145  68  TYR   B CD1 
717  C  CD2 . TYR   B 59  ? 0.5861 0.6518 0.5014 0.0781  0.0958  0.0038  68  TYR   B CD2 
718  C  CE1 . TYR   B 59  ? 0.6154 0.6564 0.5164 0.0552  0.0836  0.0236  68  TYR   B CE1 
719  C  CE2 . TYR   B 59  ? 0.5909 0.6731 0.5142 0.0659  0.1007  0.0133  68  TYR   B CE2 
720  C  CZ  . TYR   B 59  ? 0.6111 0.6791 0.5270 0.0536  0.0945  0.0237  68  TYR   B CZ  
721  O  OH  . TYR   B 59  ? 0.6145 0.6959 0.5386 0.0401  0.0995  0.0349  68  TYR   B OH  
722  N  N   . TRP   B 60  ? 0.6083 0.5929 0.4770 0.0805  0.0658  0.0048  69  TRP   B N   
723  C  CA  . TRP   B 60  ? 0.6085 0.5821 0.4656 0.0745  0.0586  0.0118  69  TRP   B CA  
724  C  C   . TRP   B 60  ? 0.5977 0.5589 0.4561 0.0795  0.0514  0.0107  69  TRP   B C   
725  O  O   . TRP   B 60  ? 0.5911 0.5508 0.4615 0.0862  0.0510  0.0093  69  TRP   B O   
726  C  CB  . TRP   B 60  ? 0.6067 0.5801 0.4683 0.0687  0.0545  0.0206  69  TRP   B CB  
727  C  CG  . TRP   B 60  ? 0.6199 0.5786 0.4698 0.0664  0.0453  0.0270  69  TRP   B CG  
728  C  CD1 . TRP   B 60  ? 0.6364 0.5895 0.4687 0.0607  0.0441  0.0317  69  TRP   B CD1 
729  C  CD2 . TRP   B 60  ? 0.6213 0.5695 0.4741 0.0728  0.0365  0.0285  69  TRP   B CD2 
730  N  NE1 . TRP   B 60  ? 0.6469 0.5868 0.4724 0.0631  0.0341  0.0357  69  TRP   B NE1 
731  C  CE2 . TRP   B 60  ? 0.6374 0.5752 0.4757 0.0706  0.0299  0.0339  69  TRP   B CE2 
732  C  CE3 . TRP   B 60  ? 0.6208 0.5684 0.4855 0.0818  0.0342  0.0264  69  TRP   B CE3 
733  C  CZ2 . TRP   B 60  ? 0.6466 0.5755 0.4838 0.0774  0.0213  0.0366  69  TRP   B CZ2 
734  C  CZ3 . TRP   B 60  ? 0.6327 0.5711 0.4946 0.0884  0.0265  0.0300  69  TRP   B CZ3 
735  C  CH2 . TRP   B 60  ? 0.6418 0.5720 0.4911 0.0863  0.0203  0.0347  69  TRP   B CH2 
736  N  N   . GLY   B 61  ? 0.6007 0.5547 0.4474 0.0766  0.0462  0.0122  70  GLY   B N   
737  C  CA  . GLY   B 61  ? 0.6030 0.5498 0.4543 0.0799  0.0398  0.0126  70  GLY   B CA  
738  C  C   . GLY   B 61  ? 0.6042 0.5466 0.4436 0.0766  0.0321  0.0169  70  GLY   B C   
739  O  O   . GLY   B 61  ? 0.6126 0.5549 0.4361 0.0721  0.0321  0.0174  70  GLY   B O   
740  N  N   . ASP   B 62  ? 0.5943 0.5345 0.4407 0.0800  0.0261  0.0209  71  ASP   B N   
741  C  CA  . ASP   B 62  ? 0.5978 0.5359 0.4353 0.0794  0.0177  0.0249  71  ASP   B CA  
742  C  C   . ASP   B 62  ? 0.5841 0.5262 0.4371 0.0838  0.0141  0.0268  71  ASP   B C   
743  O  O   . ASP   B 62  ? 0.5759 0.5193 0.4388 0.0902  0.0159  0.0315  71  ASP   B O   
744  C  CB  . ASP   B 62  ? 0.6317 0.5640 0.4594 0.0805  0.0143  0.0325  71  ASP   B CB  
745  C  CG  . ASP   B 62  ? 0.7217 0.6493 0.5350 0.0809  0.0056  0.0368  71  ASP   B CG  
746  O  OD1 . ASP   B 62  ? 0.7294 0.6605 0.5490 0.0864  -0.0002 0.0384  71  ASP   B OD1 
747  O  OD2 . ASP   B 62  ? 0.7844 0.7058 0.5805 0.0762  0.0050  0.0396  71  ASP   B OD2 
748  N  N   . VAL   B 63  ? 0.5753 0.5206 0.4310 0.0805  0.0090  0.0232  72  VAL   B N   
749  C  CA  . VAL   B 63  ? 0.5594 0.5124 0.4344 0.0819  0.0058  0.0258  72  VAL   B CA  
750  C  C   . VAL   B 63  ? 0.5651 0.5240 0.4409 0.0892  0.0015  0.0346  72  VAL   B C   
751  O  O   . VAL   B 63  ? 0.5637 0.5296 0.4548 0.0950  0.0048  0.0406  72  VAL   B O   
752  C  CB  . VAL   B 63  ? 0.5512 0.5062 0.4302 0.0750  -0.0011 0.0182  72  VAL   B CB  
753  C  CG1 . VAL   B 63  ? 0.5416 0.5090 0.4422 0.0746  -0.0068 0.0226  72  VAL   B CG1 
754  C  CG2 . VAL   B 63  ? 0.5486 0.4961 0.4316 0.0708  0.0034  0.0093  72  VAL   B CG2 
755  N  N   . LYS   B 64  ? 0.5733 0.5282 0.4305 0.0907  -0.0050 0.0362  73  LYS   B N   
756  C  CA  . LYS   B 64  ? 0.5816 0.5393 0.4364 0.1001  -0.0102 0.0436  73  LYS   B CA  
757  C  C   . LYS   B 64  ? 0.5983 0.5513 0.4535 0.1087  -0.0055 0.0482  73  LYS   B C   
758  O  O   . LYS   B 64  ? 0.5980 0.5596 0.4633 0.1184  -0.0050 0.0533  73  LYS   B O   
759  C  CB  . LYS   B 64  ? 0.6028 0.5528 0.4352 0.1007  -0.0189 0.0446  73  LYS   B CB  
760  C  CG  . LYS   B 64  ? 0.6299 0.5844 0.4616 0.1123  -0.0262 0.0507  73  LYS   B CG  
761  C  CD  . LYS   B 64  ? 0.6682 0.6160 0.4794 0.1138  -0.0364 0.0516  73  LYS   B CD  
762  C  CE  . LYS   B 64  ? 0.7126 0.6589 0.5179 0.1278  -0.0433 0.0574  73  LYS   B CE  
763  N  NZ  . LYS   B 64  ? 0.7612 0.6945 0.5414 0.1303  -0.0534 0.0594  73  LYS   B NZ  
764  N  N   . GLN   B 65  ? 0.6078 0.5488 0.4531 0.1060  -0.0021 0.0464  74  GLN   B N   
765  C  CA  . GLN   B 65  ? 0.6142 0.5504 0.4607 0.1143  0.0002  0.0487  74  GLN   B CA  
766  C  C   . GLN   B 65  ? 0.6074 0.5527 0.4718 0.1183  0.0083  0.0489  74  GLN   B C   
767  O  O   . GLN   B 65  ? 0.6120 0.5570 0.4777 0.1293  0.0096  0.0519  74  GLN   B O   
768  C  CB  . GLN   B 65  ? 0.6490 0.5739 0.4863 0.1084  0.0011  0.0463  74  GLN   B CB  
769  C  CG  . GLN   B 65  ? 0.7241 0.6362 0.5431 0.1041  -0.0060 0.0489  74  GLN   B CG  
770  C  CD  . GLN   B 65  ? 0.7934 0.6977 0.6090 0.0956  -0.0036 0.0483  74  GLN   B CD  
771  O  OE1 . GLN   B 65  ? 0.8065 0.7105 0.6307 0.0980  -0.0021 0.0463  74  GLN   B OE1 
772  N  NE2 . GLN   B 65  ? 0.8081 0.7073 0.6114 0.0858  -0.0034 0.0507  74  GLN   B NE2 
773  N  N   . ASP   B 66  ? 0.5987 0.5496 0.4746 0.1101  0.0131  0.0456  75  ASP   B N   
774  C  CA  . ASP   B 66  ? 0.5910 0.5465 0.4835 0.1111  0.0209  0.0461  75  ASP   B CA  
775  C  C   . ASP   B 66  ? 0.5890 0.5380 0.4787 0.1153  0.0258  0.0440  75  ASP   B C   
776  O  O   . ASP   B 66  ? 0.5859 0.5367 0.4822 0.1244  0.0303  0.0481  75  ASP   B O   
777  C  CB  . ASP   B 66  ? 0.5945 0.5616 0.5014 0.1187  0.0230  0.0547  75  ASP   B CB  
778  C  CG  . ASP   B 66  ? 0.6252 0.5945 0.5492 0.1181  0.0315  0.0576  75  ASP   B CG  
779  O  OD1 . ASP   B 66  ? 0.6464 0.6105 0.5761 0.1080  0.0326  0.0516  75  ASP   B OD1 
780  O  OD2 . ASP   B 66  ? 0.6307 0.6056 0.5604 0.1287  0.0371  0.0660  75  ASP   B OD2 
781  N  N   . LEU   B 67  ? 0.5860 0.5294 0.4664 0.1093  0.0251  0.0382  76  LEU   B N   
782  C  CA  . LEU   B 67  ? 0.5807 0.5215 0.4613 0.1121  0.0285  0.0352  76  LEU   B CA  
783  C  C   . LEU   B 67  ? 0.5775 0.5192 0.4588 0.1037  0.0334  0.0280  76  LEU   B C   
784  O  O   . LEU   B 67  ? 0.5813 0.5232 0.4568 0.0957  0.0325  0.0251  76  LEU   B O   
785  C  CB  . LEU   B 67  ? 0.5845 0.5202 0.4551 0.1141  0.0222  0.0363  76  LEU   B CB  
786  C  CG  . LEU   B 67  ? 0.5976 0.5299 0.4637 0.1263  0.0164  0.0413  76  LEU   B CG  
787  C  CD1 . LEU   B 67  ? 0.6043 0.5264 0.4595 0.1263  0.0078  0.0406  76  LEU   B CD1 
788  C  CD2 . LEU   B 67  ? 0.6021 0.5375 0.4748 0.1393  0.0206  0.0428  76  LEU   B CD2 
789  N  N   . VAL   B 68  ? 0.5696 0.5128 0.4569 0.1076  0.0382  0.0245  77  VAL   B N   
790  C  CA  . VAL   B 68  ? 0.5634 0.5098 0.4517 0.1033  0.0437  0.0172  77  VAL   B CA  
791  C  C   . VAL   B 68  ? 0.5640 0.5159 0.4583 0.1086  0.0462  0.0147  77  VAL   B C   
792  O  O   . VAL   B 68  ? 0.5593 0.5096 0.4586 0.1183  0.0452  0.0168  77  VAL   B O   
793  C  CB  . VAL   B 68  ? 0.5626 0.5047 0.4553 0.1028  0.0471  0.0129  77  VAL   B CB  
794  C  CG1 . VAL   B 68  ? 0.5647 0.5022 0.4678 0.1115  0.0498  0.0163  77  VAL   B CG1 
795  C  CG2 . VAL   B 68  ? 0.5695 0.5138 0.4584 0.1004  0.0518  0.0037  77  VAL   B CG2 
796  N  N   . SER   B 69  ? 0.5694 0.5297 0.4631 0.1029  0.0490  0.0109  78  SER   B N   
797  C  CA  . SER   B 69  ? 0.5703 0.5406 0.4739 0.1070  0.0508  0.0080  78  SER   B CA  
798  C  C   . SER   B 69  ? 0.5745 0.5536 0.4817 0.1086  0.0591  0.0006  78  SER   B C   
799  O  O   . SER   B 69  ? 0.5751 0.5544 0.4741 0.1034  0.0631  -0.0021 78  SER   B O   
800  C  CB  . SER   B 69  ? 0.5720 0.5482 0.4771 0.0991  0.0468  0.0112  78  SER   B CB  
801  O  OG  . SER   B 69  ? 0.5857 0.5703 0.4870 0.0888  0.0526  0.0113  78  SER   B OG  
802  N  N   . TYR   B 70  ? 0.5772 0.5629 0.4948 0.1181  0.0610  -0.0032 79  TYR   B N   
803  C  CA  . TYR   B 70  ? 0.5828 0.5770 0.5041 0.1237  0.0683  -0.0111 79  TYR   B CA  
804  C  C   . TYR   B 70  ? 0.5793 0.5960 0.5144 0.1242  0.0702  -0.0131 79  TYR   B C   
805  O  O   . TYR   B 70  ? 0.5763 0.5966 0.5204 0.1261  0.0636  -0.0105 79  TYR   B O   
806  C  CB  . TYR   B 70  ? 0.5838 0.5653 0.5066 0.1367  0.0685  -0.0134 79  TYR   B CB  
807  C  CG  . TYR   B 70  ? 0.6013 0.5633 0.5156 0.1344  0.0681  -0.0121 79  TYR   B CG  
808  C  CD1 . TYR   B 70  ? 0.6155 0.5686 0.5273 0.1300  0.0633  -0.0041 79  TYR   B CD1 
809  C  CD2 . TYR   B 70  ? 0.6181 0.5715 0.5279 0.1364  0.0716  -0.0194 79  TYR   B CD2 
810  C  CE1 . TYR   B 70  ? 0.6306 0.5704 0.5393 0.1259  0.0624  -0.0025 79  TYR   B CE1 
811  C  CE2 . TYR   B 70  ? 0.6347 0.5706 0.5398 0.1318  0.0691  -0.0189 79  TYR   B CE2 
812  C  CZ  . TYR   B 70  ? 0.6456 0.5764 0.5523 0.1258  0.0647  -0.0099 79  TYR   B CZ  
813  O  OH  . TYR   B 70  ? 0.6633 0.5807 0.5704 0.1203  0.0618  -0.0090 79  TYR   B OH  
814  N  N   . CYS   B 71  ? 0.5756 0.6086 0.5126 0.1231  0.0786  -0.0178 80  CYS   B N   
815  C  CA  . CYS   B 71  ? 0.5707 0.6316 0.5251 0.1233  0.0826  -0.0195 80  CYS   B CA  
816  C  C   . CYS   B 71  ? 0.5549 0.6287 0.5170 0.1077  0.0814  -0.0116 80  CYS   B C   
817  O  O   . CYS   B 71  ? 0.5441 0.6444 0.5227 0.1040  0.0867  -0.0112 80  CYS   B O   
818  C  CB  . CYS   B 71  ? 0.5897 0.6563 0.5586 0.1362  0.0778  -0.0233 80  CYS   B CB  
819  S  SG  . CYS   B 71  ? 0.6868 0.7366 0.6470 0.1552  0.0800  -0.0308 80  CYS   B SG  
820  N  N   . GLY   B 72  ? 0.5472 0.6031 0.4992 0.0989  0.0744  -0.0049 81  GLY   B N   
821  C  CA  . GLY   B 72  ? 0.5350 0.5965 0.4920 0.0840  0.0720  0.0033  81  GLY   B CA  
822  C  C   . GLY   B 72  ? 0.5377 0.5749 0.4789 0.0780  0.0637  0.0095  81  GLY   B C   
823  O  O   . GLY   B 72  ? 0.5429 0.5623 0.4709 0.0849  0.0606  0.0078  81  GLY   B O   
824  N  N   . PRO   B 73  ? 0.5319 0.5686 0.4752 0.0648  0.0603  0.0175  82  PRO   B N   
825  C  CA  . PRO   B 73  ? 0.5454 0.5578 0.4725 0.0606  0.0512  0.0235  82  PRO   B CA  
826  C  C   . PRO   B 73  ? 0.5576 0.5548 0.4859 0.0695  0.0381  0.0210  82  PRO   B C   
827  O  O   . PRO   B 73  ? 0.5536 0.5591 0.4972 0.0754  0.0339  0.0163  82  PRO   B O   
828  C  CB  . PRO   B 73  ? 0.5472 0.5625 0.4782 0.0445  0.0510  0.0329  82  PRO   B CB  
829  C  CG  . PRO   B 73  ? 0.5320 0.5730 0.4893 0.0405  0.0551  0.0315  82  PRO   B CG  
830  C  CD  . PRO   B 73  ? 0.5068 0.5649 0.4686 0.0531  0.0643  0.0223  82  PRO   B CD  
831  N  N   . TRP   B 74  ? 0.5678 0.5443 0.4793 0.0720  0.0314  0.0242  83  TRP   B N   
832  C  CA  . TRP   B 74  ? 0.5731 0.5351 0.4813 0.0828  0.0199  0.0229  83  TRP   B CA  
833  C  C   . TRP   B 74  ? 0.5950 0.5556 0.5147 0.0801  0.0089  0.0219  83  TRP   B C   
834  O  O   . TRP   B 74  ? 0.5994 0.5559 0.5209 0.0669  0.0052  0.0269  83  TRP   B O   
835  C  CB  . TRP   B 74  ? 0.5690 0.5128 0.4585 0.0843  0.0151  0.0278  83  TRP   B CB  
836  C  CG  . TRP   B 74  ? 0.5587 0.4914 0.4425 0.0990  0.0069  0.0266  83  TRP   B CG  
837  C  CD1 . TRP   B 74  ? 0.5675 0.4869 0.4466 0.1042  -0.0057 0.0266  83  TRP   B CD1 
838  C  CD2 . TRP   B 74  ? 0.5502 0.4843 0.4318 0.1114  0.0112  0.0257  83  TRP   B CD2 
839  N  NE1 . TRP   B 74  ? 0.5723 0.4869 0.4444 0.1210  -0.0085 0.0255  83  TRP   B NE1 
840  C  CE2 . TRP   B 74  ? 0.5620 0.4866 0.4372 0.1248  0.0026  0.0262  83  TRP   B CE2 
841  C  CE3 . TRP   B 74  ? 0.5451 0.4866 0.4298 0.1124  0.0212  0.0248  83  TRP   B CE3 
842  C  CZ2 . TRP   B 74  ? 0.5675 0.4932 0.4402 0.1389  0.0060  0.0279  83  TRP   B CZ2 
843  C  CZ3 . TRP   B 74  ? 0.5522 0.4919 0.4367 0.1242  0.0231  0.0263  83  TRP   B CZ3 
844  C  CH2 . TRP   B 74  ? 0.5610 0.4946 0.4400 0.1371  0.0167  0.0289  83  TRP   B CH2 
845  N  N   . LYS   B 75  ? 0.6048 0.5690 0.5328 0.0923  0.0033  0.0155  84  LYS   B N   
846  C  CA  . LYS   B 75  ? 0.6132 0.5771 0.5535 0.0918  -0.0098 0.0117  84  LYS   B CA  
847  C  C   . LYS   B 75  ? 0.6468 0.5884 0.5728 0.1037  -0.0250 0.0096  84  LYS   B C   
848  O  O   . LYS   B 75  ? 0.6553 0.5910 0.5883 0.1024  -0.0391 0.0057  84  LYS   B O   
849  C  CB  . LYS   B 75  ? 0.6093 0.5934 0.5675 0.0999  -0.0084 0.0043  84  LYS   B CB  
850  C  CG  . LYS   B 75  ? 0.6337 0.6423 0.6064 0.0928  0.0062  0.0043  84  LYS   B CG  
851  C  CD  . LYS   B 75  ? 0.6658 0.6889 0.6570 0.0738  0.0071  0.0082  84  LYS   B CD  
852  C  CE  . LYS   B 75  ? 0.6913 0.7456 0.7027 0.0732  0.0186  0.0052  84  LYS   B CE  
853  N  NZ  . LYS   B 75  ? 0.7185 0.7894 0.7416 0.0546  0.0280  0.0129  84  LYS   B NZ  
854  N  N   . LEU   B 76  ? 0.6638 0.5944 0.5712 0.1165  -0.0227 0.0116  85  LEU   B N   
855  C  CA  . LEU   B 76  ? 0.6877 0.6001 0.5793 0.1319  -0.0353 0.0096  85  LEU   B CA  
856  C  C   . LEU   B 76  ? 0.7183 0.6103 0.5972 0.1254  -0.0442 0.0136  85  LEU   B C   
857  O  O   . LEU   B 76  ? 0.7201 0.6094 0.5908 0.1193  -0.0370 0.0201  85  LEU   B O   
858  C  CB  . LEU   B 76  ? 0.6874 0.6011 0.5674 0.1497  -0.0277 0.0115  85  LEU   B CB  
859  C  CG  . LEU   B 76  ? 0.6917 0.6215 0.5818 0.1553  -0.0167 0.0098  85  LEU   B CG  
860  C  CD1 . LEU   B 76  ? 0.6997 0.6280 0.5795 0.1697  -0.0087 0.0147  85  LEU   B CD1 
861  C  CD2 . LEU   B 76  ? 0.6935 0.6293 0.5926 0.1631  -0.0251 0.0021  85  LEU   B CD2 
862  N  N   . ASP   B 77  ? 0.7417 0.6174 0.6178 0.1276  -0.0613 0.0090  86  ASP   B N   
863  C  CA  . ASP   B 77  ? 0.7792 0.6307 0.6427 0.1215  -0.0718 0.0123  86  ASP   B CA  
864  C  C   . ASP   B 77  ? 0.8026 0.6303 0.6465 0.1405  -0.0891 0.0064  86  ASP   B C   
865  O  O   . ASP   B 77  ? 0.8215 0.6254 0.6536 0.1372  -0.1000 0.0081  86  ASP   B O   
866  C  CB  . ASP   B 77  ? 0.8136 0.6628 0.6941 0.0980  -0.0767 0.0147  86  ASP   B CB  
867  C  CG  . ASP   B 77  ? 0.8944 0.7499 0.7955 0.0953  -0.0881 0.0063  86  ASP   B CG  
868  O  OD1 . ASP   B 77  ? 0.9111 0.7739 0.8117 0.1129  -0.0917 -0.0022 86  ASP   B OD1 
869  O  OD2 . ASP   B 77  ? 0.9226 0.7769 0.8413 0.0754  -0.0934 0.0089  86  ASP   B OD2 
870  N  N   . ALA   B 78  ? 0.8019 0.6341 0.6399 0.1615  -0.0920 -0.0003 87  ALA   B N   
871  C  CA  . ALA   B 78  ? 0.8209 0.6317 0.6366 0.1834  -0.1080 -0.0070 87  ALA   B CA  
872  C  C   . ALA   B 78  ? 0.8359 0.6404 0.6303 0.1968  -0.1022 -0.0007 87  ALA   B C   
873  O  O   . ALA   B 78  ? 0.8266 0.6489 0.6246 0.1949  -0.0849 0.0073  87  ALA   B O   
874  C  CB  . ALA   B 78  ? 0.8164 0.6359 0.6297 0.2038  -0.1114 -0.0151 87  ALA   B CB  
875  N  N   . ALA   B 79  ? 0.8571 0.6368 0.6301 0.2110  -0.1176 -0.0049 88  ALA   B N   
876  C  CA  . ALA   B 79  ? 0.8755 0.6513 0.6290 0.2259  -0.1134 0.0006  88  ALA   B CA  
877  C  C   . ALA   B 79  ? 0.8968 0.6622 0.6256 0.2575  -0.1232 -0.0062 88  ALA   B C   
878  O  O   . ALA   B 79  ? 0.9154 0.6629 0.6363 0.2659  -0.1409 -0.0173 88  ALA   B O   
879  C  CB  . ALA   B 79  ? 0.8917 0.6463 0.6394 0.2127  -0.1205 0.0046  88  ALA   B CB  
880  N  N   . TRP   B 80  ? 0.8938 0.6717 0.6110 0.2757  -0.1121 0.0002  89  TRP   B N   
881  C  CA  . TRP   B 80  ? 0.9103 0.6820 0.6016 0.3087  -0.1184 -0.0043 89  TRP   B CA  
882  C  C   . TRP   B 80  ? 0.9362 0.6725 0.6064 0.3160  -0.1404 -0.0125 89  TRP   B C   
883  O  O   . TRP   B 80  ? 0.9353 0.6605 0.6077 0.3014  -0.1425 -0.0080 89  TRP   B O   
884  C  CB  . TRP   B 80  ? 0.9004 0.6972 0.5893 0.3225  -0.0999 0.0072  89  TRP   B CB  
885  C  CG  . TRP   B 80  ? 0.9101 0.7059 0.5724 0.3582  -0.1029 0.0048  89  TRP   B CG  
886  C  CD1 . TRP   B 80  ? 0.9273 0.7181 0.5719 0.3817  -0.1096 -0.0031 89  TRP   B CD1 
887  C  CD2 . TRP   B 80  ? 0.9110 0.7150 0.5614 0.3762  -0.0977 0.0110  89  TRP   B CD2 
888  N  NE1 . TRP   B 80  ? 0.9380 0.7320 0.5579 0.4141  -0.1085 -0.0021 89  TRP   B NE1 
889  C  CE2 . TRP   B 80  ? 0.9292 0.7329 0.5539 0.4112  -0.1006 0.0068  89  TRP   B CE2 
890  C  CE3 . TRP   B 80  ? 0.9105 0.7229 0.5687 0.3677  -0.0919 0.0192  89  TRP   B CE3 
891  C  CZ2 . TRP   B 80  ? 0.9345 0.7485 0.5430 0.4376  -0.0961 0.0113  89  TRP   B CZ2 
892  C  CZ3 . TRP   B 80  ? 0.9200 0.7425 0.5641 0.3931  -0.0890 0.0230  89  TRP   B CZ3 
893  C  CH2 . TRP   B 80  ? 0.9261 0.7503 0.5463 0.4276  -0.0904 0.0194  89  TRP   B CH2 
894  N  N   . ASP   B 81  ? 0.9600 0.6760 0.6087 0.3384  -0.1581 -0.0251 90  ASP   B N   
895  C  CA  . ASP   B 81  ? 0.9981 0.6749 0.6250 0.3466  -0.1818 -0.0347 90  ASP   B CA  
896  C  C   . ASP   B 81  ? 1.0237 0.6961 0.6263 0.3710  -0.1805 -0.0315 90  ASP   B C   
897  O  O   . ASP   B 81  ? 1.0451 0.6831 0.6289 0.3776  -0.1993 -0.0382 90  ASP   B O   
898  C  CB  . ASP   B 81  ? 1.0282 0.6808 0.6397 0.3620  -0.2049 -0.0518 90  ASP   B CB  
899  C  CG  . ASP   B 81  ? 1.0783 0.7450 0.6682 0.3974  -0.2013 -0.0565 90  ASP   B CG  
900  O  OD1 . ASP   B 81  ? 1.0899 0.7835 0.6751 0.4123  -0.1807 -0.0455 90  ASP   B OD1 
901  O  OD2 . ASP   B 81  ? 1.0925 0.7440 0.6705 0.4104  -0.2192 -0.0709 90  ASP   B OD2 
902  N  N   . GLY   B 82  ? 1.0162 0.7231 0.6208 0.3840  -0.1590 -0.0210 91  GLY   B N   
903  C  CA  . GLY   B 82  ? 1.0296 0.7421 0.6161 0.4082  -0.1550 -0.0166 91  GLY   B CA  
904  C  C   . GLY   B 82  ? 1.0531 0.7638 0.6091 0.4489  -0.1601 -0.0243 91  GLY   B C   
905  O  O   . GLY   B 82  ? 1.0543 0.7804 0.5977 0.4729  -0.1517 -0.0189 91  GLY   B O   
906  N  N   . LEU   B 83  ? 1.0698 0.7645 0.6137 0.4584  -0.1734 -0.0369 92  LEU   B N   
907  C  CA  . LEU   B 83  ? 1.0970 0.7862 0.6064 0.4996  -0.1806 -0.0461 92  LEU   B CA  
908  C  C   . LEU   B 83  ? 1.0990 0.8119 0.6069 0.5130  -0.1693 -0.0447 92  LEU   B C   
909  O  O   . LEU   B 83  ? 1.1100 0.8346 0.5924 0.5486  -0.1634 -0.0443 92  LEU   B O   
910  C  CB  . LEU   B 83  ? 1.1282 0.7676 0.6118 0.5095  -0.2136 -0.0664 92  LEU   B CB  
911  C  CG  . LEU   B 83  ? 1.1684 0.7733 0.6419 0.5058  -0.2299 -0.0702 92  LEU   B CG  
912  C  CD1 . LEU   B 83  ? 1.2059 0.7610 0.6489 0.5234  -0.2629 -0.0913 92  LEU   B CD1 
913  C  CD2 . LEU   B 83  ? 1.1756 0.7989 0.6359 0.5295  -0.2165 -0.0609 92  LEU   B CD2 
914  N  N   . SER   B 84  ? 1.0906 0.8080 0.6221 0.4878  -0.1681 -0.0450 93  SER   B N   
915  C  CA  . SER   B 84  ? 1.0926 0.8269 0.6208 0.5004  -0.1610 -0.0452 93  SER   B CA  
916  C  C   . SER   B 84  ? 1.0706 0.8467 0.6162 0.4985  -0.1298 -0.0256 93  SER   B C   
917  O  O   . SER   B 84  ? 1.0591 0.8534 0.6319 0.4743  -0.1136 -0.0124 93  SER   B O   
918  C  CB  . SER   B 84  ? 1.1159 0.8374 0.6626 0.4762  -0.1751 -0.0550 93  SER   B CB  
919  O  OG  . SER   B 84  ? 1.1697 0.8516 0.7058 0.4734  -0.2051 -0.0724 93  SER   B OG  
920  N  N   . GLU   B 85  ? 1.0598 0.8492 0.5888 0.5239  -0.1224 -0.0239 94  GLU   B N   
921  C  CA  . GLU   B 85  ? 1.0381 0.8628 0.5829 0.5220  -0.0943 -0.0053 94  GLU   B CA  
922  C  C   . GLU   B 85  ? 1.0110 0.8377 0.5874 0.4883  -0.0929 -0.0051 94  GLU   B C   
923  O  O   . GLU   B 85  ? 1.0215 0.8271 0.5995 0.4784  -0.1132 -0.0200 94  GLU   B O   
924  C  CB  . GLU   B 85  ? 1.0784 0.9125 0.5922 0.5606  -0.0882 -0.0033 94  GLU   B CB  
925  C  CG  . GLU   B 85  ? 1.1471 0.9962 0.6370 0.5936  -0.0765 0.0052  94  GLU   B CG  
926  C  CD  . GLU   B 85  ? 1.2289 1.0985 0.6957 0.6269  -0.0599 0.0158  94  GLU   B CD  
927  O  OE1 . GLU   B 85  ? 1.2515 1.1134 0.7081 0.6329  -0.0657 0.0104  94  GLU   B OE1 
928  O  OE2 . GLU   B 85  ? 1.2485 1.1432 0.7076 0.6474  -0.0408 0.0304  94  GLU   B OE2 
929  N  N   . VAL   B 86  ? 0.9707 0.8233 0.5741 0.4699  -0.0696 0.0116  95  VAL   B N   
930  C  CA  . VAL   B 86  ? 0.9374 0.7950 0.5703 0.4401  -0.0650 0.0132  95  VAL   B CA  
931  C  C   . VAL   B 86  ? 0.9155 0.7941 0.5512 0.4493  -0.0450 0.0263  95  VAL   B C   
932  O  O   . VAL   B 86  ? 0.9180 0.8088 0.5351 0.4759  -0.0332 0.0361  95  VAL   B O   
933  C  CB  . VAL   B 86  ? 0.9203 0.7848 0.5831 0.4070  -0.0570 0.0202  95  VAL   B CB  
934  C  CG1 . VAL   B 86  ? 0.9291 0.7719 0.5852 0.4011  -0.0747 0.0107  95  VAL   B CG1 
935  C  CG2 . VAL   B 86  ? 0.9110 0.8027 0.5853 0.4077  -0.0329 0.0388  95  VAL   B CG2 
936  N  N   . GLN   B 87  ? 0.8907 0.7733 0.5488 0.4285  -0.0408 0.0272  96  GLN   B N   
937  C  CA  . GLN   B 87  ? 0.8720 0.7702 0.5342 0.4345  -0.0225 0.0402  96  GLN   B CA  
938  C  C   . GLN   B 87  ? 0.8368 0.7476 0.5333 0.4037  -0.0066 0.0508  96  GLN   B C   
939  O  O   . GLN   B 87  ? 0.8303 0.7353 0.5459 0.3790  -0.0141 0.0426  96  GLN   B O   
940  C  CB  . GLN   B 87  ? 0.8906 0.7798 0.5399 0.4479  -0.0341 0.0301  96  GLN   B CB  
941  C  CG  . GLN   B 87  ? 0.9375 0.8313 0.5556 0.4842  -0.0268 0.0376  96  GLN   B CG  
942  C  CD  . GLN   B 87  ? 0.9957 0.8765 0.5920 0.5043  -0.0455 0.0229  96  GLN   B CD  
943  O  OE1 . GLN   B 87  ? 1.0059 0.8835 0.6181 0.4903  -0.0539 0.0147  96  GLN   B OE1 
944  N  NE2 . GLN   B 87  ? 1.0089 0.8834 0.5678 0.5392  -0.0529 0.0186  96  GLN   B NE2 
945  N  N   . LEU   B 88  ? 0.8138 0.7418 0.5181 0.4053  0.0149  0.0691  97  LEU   B N   
946  C  CA  . LEU   B 88  ? 0.7941 0.7314 0.5288 0.3786  0.0289  0.0784  97  LEU   B CA  
947  C  C   . LEU   B 88  ? 0.8012 0.7362 0.5358 0.3831  0.0344  0.0814  97  LEU   B C   
948  O  O   . LEU   B 88  ? 0.8087 0.7481 0.5272 0.4056  0.0441  0.0922  97  LEU   B O   
949  C  CB  . LEU   B 88  ? 0.7755 0.7319 0.5222 0.3767  0.0480  0.0969  97  LEU   B CB  
950  C  CG  . LEU   B 88  ? 0.7696 0.7338 0.5460 0.3525  0.0626  0.1078  97  LEU   B CG  
951  C  CD1 . LEU   B 88  ? 0.7672 0.7244 0.5633 0.3234  0.0539  0.0964  97  LEU   B CD1 
952  C  CD2 . LEU   B 88  ? 0.7606 0.7453 0.5504 0.3527  0.0806  0.1271  97  LEU   B CD2 
953  N  N   . LEU   B 89  ? 0.7953 0.7240 0.5463 0.3637  0.0286  0.0724  98  LEU   B N   
954  C  CA  . LEU   B 89  ? 0.7980 0.7246 0.5508 0.3675  0.0337  0.0749  98  LEU   B CA  
955  C  C   . LEU   B 89  ? 0.7917 0.7255 0.5659 0.3512  0.0528  0.0904  98  LEU   B C   
956  O  O   . LEU   B 89  ? 0.7854 0.7183 0.5815 0.3272  0.0533  0.0862  98  LEU   B O   
957  C  CB  . LEU   B 89  ? 0.7979 0.7180 0.5610 0.3548  0.0190  0.0580  98  LEU   B CB  
958  C  CG  . LEU   B 89  ? 0.8070 0.7253 0.5732 0.3592  0.0206  0.0568  98  LEU   B CG  
959  C  CD1 . LEU   B 89  ? 0.8275 0.7442 0.5719 0.3866  0.0291  0.0686  98  LEU   B CD1 
960  C  CD2 . LEU   B 89  ? 0.8093 0.7250 0.5772 0.3588  0.0012  0.0384  98  LEU   B CD2 
961  N  N   . ALA   B 90  ? 0.7887 0.7303 0.5571 0.3638  0.0682  0.1084  99  ALA   B N   
962  C  CA  . ALA   B 90  ? 0.7869 0.7349 0.5780 0.3476  0.0855  0.1243  99  ALA   B CA  
963  C  C   . ALA   B 90  ? 0.8017 0.7394 0.5973 0.3459  0.0916  0.1287  99  ALA   B C   
964  O  O   . ALA   B 90  ? 0.8153 0.7471 0.5905 0.3679  0.0917  0.1311  99  ALA   B O   
965  C  CB  . ALA   B 90  ? 0.7817 0.7441 0.5684 0.3610  0.1007  0.1439  99  ALA   B CB  
966  N  N   . VAL   B 91  ? 0.7958 0.7299 0.6160 0.3214  0.0956  0.1286  100 VAL   B N   
967  C  CA  . VAL   B 91  ? 0.8029 0.7244 0.6281 0.3194  0.1013  0.1326  100 VAL   B CA  
968  C  C   . VAL   B 91  ? 0.8085 0.7304 0.6550 0.3038  0.1167  0.1500  100 VAL   B C   
969  O  O   . VAL   B 91  ? 0.8056 0.7258 0.6739 0.2801  0.1155  0.1450  100 VAL   B O   
970  C  CB  . VAL   B 91  ? 0.7997 0.7136 0.6331 0.3066  0.0895  0.1135  100 VAL   B CB  
971  C  CG1 . VAL   B 91  ? 0.8091 0.7091 0.6459 0.3076  0.0950  0.1169  100 VAL   B CG1 
972  C  CG2 . VAL   B 91  ? 0.8022 0.7185 0.6204 0.3187  0.0734  0.0972  100 VAL   B CG2 
973  N  N   . PRO   B 92  ? 0.8096 0.7350 0.6502 0.3171  0.1310  0.1711  101 PRO   B N   
974  C  CA  . PRO   B 92  ? 0.8048 0.7333 0.6700 0.3007  0.1453  0.1895  101 PRO   B CA  
975  C  C   . PRO   B 92  ? 0.8201 0.7270 0.6963 0.2905  0.1506  0.1953  101 PRO   B C   
976  O  O   . PRO   B 92  ? 0.8308 0.7219 0.6898 0.3047  0.1486  0.1928  101 PRO   B O   
977  C  CB  . PRO   B 92  ? 0.8098 0.7538 0.6640 0.3203  0.1595  0.2109  101 PRO   B CB  
978  C  CG  . PRO   B 92  ? 0.8263 0.7727 0.6463 0.3485  0.1504  0.2007  101 PRO   B CG  
979  C  CD  . PRO   B 92  ? 0.8124 0.7413 0.6243 0.3476  0.1348  0.1798  101 PRO   B CD  
980  N  N   . PRO   B 93  ? 0.8202 0.7250 0.7251 0.2662  0.1558  0.2022  102 PRO   B N   
981  C  CA  . PRO   B 93  ? 0.8341 0.7137 0.7494 0.2560  0.1592  0.2067  102 PRO   B CA  
982  C  C   . PRO   B 93  ? 0.8612 0.7278 0.7620 0.2743  0.1721  0.2278  102 PRO   B C   
983  O  O   . PRO   B 93  ? 0.8623 0.7418 0.7644 0.2810  0.1861  0.2501  102 PRO   B O   
984  C  CB  . PRO   B 93  ? 0.8274 0.7109 0.7764 0.2285  0.1625  0.2134  102 PRO   B CB  
985  C  CG  . PRO   B 93  ? 0.8206 0.7298 0.7761 0.2220  0.1556  0.2032  102 PRO   B CG  
986  C  CD  . PRO   B 93  ? 0.8009 0.7251 0.7301 0.2476  0.1567  0.2044  102 PRO   B CD  
987  N  N   . GLY   B 94  ? 0.8785 0.7216 0.7644 0.2841  0.1675  0.2211  103 GLY   B N   
988  C  CA  . GLY   B 94  ? 0.8973 0.7231 0.7650 0.3037  0.1777  0.2395  103 GLY   B CA  
989  C  C   . GLY   B 94  ? 0.9108 0.7495 0.7470 0.3348  0.1812  0.2464  103 GLY   B C   
990  O  O   . GLY   B 94  ? 0.9247 0.7525 0.7431 0.3532  0.1921  0.2658  103 GLY   B O   
991  N  N   . GLU   B 95  ? 0.9062 0.7665 0.7335 0.3415  0.1717  0.2312  104 GLU   B N   
992  C  CA  . GLU   B 95  ? 0.9226 0.7948 0.7185 0.3716  0.1717  0.2339  104 GLU   B CA  
993  C  C   . GLU   B 95  ? 0.9330 0.8073 0.7133 0.3816  0.1512  0.2060  104 GLU   B C   
994  O  O   . GLU   B 95  ? 0.9272 0.8022 0.7243 0.3625  0.1396  0.1867  104 GLU   B O   
995  C  CB  . GLU   B 95  ? 0.9440 0.8422 0.7437 0.3731  0.1815  0.2465  104 GLU   B CB  
996  C  CG  . GLU   B 95  ? 1.0016 0.9035 0.8175 0.3662  0.2034  0.2774  104 GLU   B CG  
997  C  CD  . GLU   B 95  ? 1.0898 1.0221 0.9214 0.3606  0.2128  0.2882  104 GLU   B CD  
998  O  OE1 . GLU   B 95  ? 1.1038 1.0522 0.9295 0.3646  0.2017  0.2714  104 GLU   B OE1 
999  O  OE2 . GLU   B 95  ? 1.1200 1.0603 0.9708 0.3524  0.2311  0.3142  104 GLU   B OE2 
1000 N  N   . ARG   B 96  ? 0.9464 0.8226 0.6947 0.4115  0.1468  0.2046  105 ARG   B N   
1001 C  CA  . ARG   B 96  ? 0.9624 0.8406 0.6961 0.4230  0.1263  0.1796  105 ARG   B CA  
1002 C  C   . ARG   B 96  ? 0.9624 0.8571 0.7014 0.4148  0.1156  0.1646  105 ARG   B C   
1003 O  O   . ARG   B 96  ? 0.9623 0.8697 0.7026 0.4142  0.1242  0.1753  105 ARG   B O   
1004 C  CB  . ARG   B 96  ? 0.9985 0.8733 0.6948 0.4591  0.1242  0.1839  105 ARG   B CB  
1005 C  CG  . ARG   B 96  ? 1.0522 0.9189 0.7370 0.4718  0.1058  0.1641  105 ARG   B CG  
1006 C  CD  . ARG   B 96  ? 1.1150 0.9670 0.7743 0.4981  0.1118  0.1777  105 ARG   B CD  
1007 N  NE  . ARG   B 96  ? 1.1825 1.0384 0.8089 0.5267  0.1206  0.1941  105 ARG   B NE  
1008 C  CZ  . ARG   B 96  ? 1.2360 1.0819 0.8462 0.5414  0.1389  0.2207  105 ARG   B CZ  
1009 N  NH1 . ARG   B 96  ? 1.2326 1.0605 0.8572 0.5292  0.1492  0.2334  105 ARG   B NH1 
1010 N  NH2 . ARG   B 96  ? 1.2507 1.1034 0.8290 0.5691  0.1475  0.2352  105 ARG   B NH2 
1011 N  N   . ALA   B 97  ? 0.9574 0.8525 0.6992 0.4100  0.0966  0.1404  106 ALA   B N   
1012 C  CA  . ALA   B 97  ? 0.9589 0.8648 0.7029 0.4035  0.0835  0.1248  106 ALA   B CA  
1013 C  C   . ALA   B 97  ? 0.9765 0.8876 0.6900 0.4318  0.0807  0.1276  106 ALA   B C   
1014 O  O   . ALA   B 97  ? 0.9924 0.8981 0.6801 0.4583  0.0775  0.1286  106 ALA   B O   
1015 C  CB  . ALA   B 97  ? 0.9581 0.8623 0.7086 0.3968  0.0646  0.1015  106 ALA   B CB  
1016 N  N   . LYS   B 98  ? 0.9729 0.8944 0.6873 0.4286  0.0818  0.1290  107 LYS   B N   
1017 C  CA  . LYS   B 98  ? 0.9829 0.9097 0.6673 0.4570  0.0802  0.1317  107 LYS   B CA  
1018 C  C   . LYS   B 98  ? 0.9702 0.9010 0.6548 0.4518  0.0660  0.1165  107 LYS   B C   
1019 O  O   . LYS   B 98  ? 0.9587 0.8958 0.6673 0.4278  0.0695  0.1173  107 LYS   B O   
1020 C  CB  . LYS   B 98  ? 1.0163 0.9539 0.6992 0.4644  0.1045  0.1587  107 LYS   B CB  
1021 C  CG  . LYS   B 98  ? 1.0944 1.0399 0.7425 0.4992  0.1086  0.1667  107 LYS   B CG  
1022 C  CD  . LYS   B 98  ? 1.1543 1.1156 0.8078 0.5029  0.1361  0.1968  107 LYS   B CD  
1023 C  CE  . LYS   B 98  ? 1.1833 1.1560 0.8789 0.4687  0.1464  0.2051  107 LYS   B CE  
1024 N  NZ  . LYS   B 98  ? 1.1997 1.1971 0.8997 0.4750  0.1624  0.2226  107 LYS   B NZ  
1025 N  N   . ASN   B 99  ? 0.9756 0.9010 0.6324 0.4749  0.0490  0.1024  108 ASN   B N   
1026 C  CA  . ASN   B 99  ? 0.9770 0.9009 0.6300 0.4727  0.0336  0.0877  108 ASN   B CA  
1027 C  C   . ASN   B 99  ? 0.9837 0.9178 0.6183 0.4929  0.0435  0.0992  108 ASN   B C   
1028 O  O   . ASN   B 99  ? 1.0002 0.9358 0.6045 0.5244  0.0480  0.1059  108 ASN   B O   
1029 C  CB  . ASN   B 99  ? 0.9932 0.9032 0.6267 0.4868  0.0072  0.0650  108 ASN   B CB  
1030 C  CG  . ASN   B 99  ? 1.0181 0.9224 0.6738 0.4657  -0.0055 0.0510  108 ASN   B CG  
1031 O  OD1 . ASN   B 99  ? 1.0286 0.9355 0.6974 0.4582  0.0038  0.0575  108 ASN   B OD1 
1032 N  ND2 . ASN   B 99  ? 1.0198 0.9161 0.6800 0.4565  -0.0272 0.0318  108 ASN   B ND2 
1033 N  N   . ILE   B 100 ? 0.9716 0.9140 0.6227 0.4772  0.0469  0.1013  109 ILE   B N   
1034 C  CA  . ILE   B 100 ? 0.9720 0.9279 0.6086 0.4967  0.0562  0.1116  109 ILE   B CA  
1035 C  C   . ILE   B 100 ? 0.9741 0.9207 0.6010 0.4989  0.0365  0.0936  109 ILE   B C   
1036 O  O   . ILE   B 100 ? 0.9696 0.9142 0.6202 0.4720  0.0310  0.0878  109 ILE   B O   
1037 C  CB  . ILE   B 100 ? 0.9648 0.9422 0.6311 0.4786  0.0794  0.1329  109 ILE   B CB  
1038 C  CG1 . ILE   B 100 ? 0.9718 0.9527 0.6540 0.4689  0.0973  0.1502  109 ILE   B CG1 
1039 C  CG2 . ILE   B 100 ? 0.9685 0.9657 0.6216 0.5015  0.0908  0.1451  109 ILE   B CG2 
1040 C  CD1 . ILE   B 100 ? 0.9933 0.9762 0.6476 0.4997  0.1085  0.1638  109 ILE   B CD1 
1041 N  N   . GLN   B 101 ? 0.9835 0.9227 0.5740 0.5316  0.0255  0.0851  110 GLN   B N   
1042 C  CA  . GLN   B 101 ? 0.9953 0.9203 0.5727 0.5367  0.0046  0.0673  110 GLN   B CA  
1043 C  C   . GLN   B 101 ? 0.9907 0.9324 0.5697 0.5428  0.0158  0.0774  110 GLN   B C   
1044 O  O   . GLN   B 101 ? 0.9885 0.9514 0.5579 0.5639  0.0351  0.0944  110 GLN   B O   
1045 C  CB  . GLN   B 101 ? 1.0340 0.9405 0.5698 0.5708  -0.0151 0.0511  110 GLN   B CB  
1046 C  CG  . GLN   B 101 ? 1.0843 0.9668 0.6090 0.5711  -0.0425 0.0287  110 GLN   B CG  
1047 C  CD  . GLN   B 101 ? 1.1636 1.0244 0.6533 0.5984  -0.0660 0.0098  110 GLN   B CD  
1048 O  OE1 . GLN   B 101 ? 1.1839 1.0422 0.6717 0.6006  -0.0697 0.0067  110 GLN   B OE1 
1049 N  NE2 . GLN   B 101 ? 1.1981 1.0419 0.6582 0.6215  -0.0835 -0.0040 110 GLN   B NE2 
1050 N  N   . THR   B 102 ? 0.9849 0.9187 0.5770 0.5247  0.0042  0.0681  111 THR   B N   
1051 C  CA  . THR   B 102 ? 0.9790 0.9284 0.5737 0.5305  0.0118  0.0757  111 THR   B CA  
1052 C  C   . THR   B 102 ? 0.9910 0.9177 0.5806 0.5238  -0.0109 0.0581  111 THR   B C   
1053 O  O   . THR   B 102 ? 1.0012 0.9050 0.5988 0.5023  -0.0278 0.0446  111 THR   B O   
1054 C  CB  . THR   B 102 ? 0.9741 0.9508 0.6084 0.5040  0.0341  0.0951  111 THR   B CB  
1055 O  OG1 . THR   B 102 ? 0.9809 0.9801 0.6173 0.5158  0.0439  0.1049  111 THR   B OG1 
1056 C  CG2 . THR   B 102 ? 0.9728 0.9390 0.6374 0.4646  0.0264  0.0884  111 THR   B CG2 
1057 N  N   . LEU   B 103 ? 0.9879 0.9211 0.5652 0.5420  -0.0111 0.0593  112 LEU   B N   
1058 C  CA  . LEU   B 103 ? 0.9943 0.9043 0.5676 0.5346  -0.0316 0.0450  112 LEU   B CA  
1059 C  C   . LEU   B 103 ? 0.9774 0.9068 0.5852 0.5072  -0.0200 0.0566  112 LEU   B C   
1060 O  O   . LEU   B 103 ? 0.9654 0.9262 0.5830 0.5160  -0.0019 0.0716  112 LEU   B O   
1061 C  CB  . LEU   B 103 ? 1.0103 0.9110 0.5472 0.5720  -0.0423 0.0367  112 LEU   B CB  
1062 C  CG  . LEU   B 103 ? 1.0381 0.9093 0.5701 0.5634  -0.0648 0.0225  112 LEU   B CG  
1063 C  CD1 . LEU   B 103 ? 1.0626 0.8930 0.5824 0.5550  -0.0911 0.0028  112 LEU   B CD1 
1064 C  CD2 . LEU   B 103 ? 1.0530 0.9251 0.5582 0.5975  -0.0686 0.0199  112 LEU   B CD2 
1065 N  N   . PRO   B 104 ? 0.9714 0.8840 0.5984 0.4744  -0.0304 0.0498  113 PRO   B N   
1066 C  CA  . PRO   B 104 ? 0.9539 0.8835 0.6112 0.4490  -0.0211 0.0594  113 PRO   B CA  
1067 C  C   . PRO   B 104 ? 0.9578 0.8915 0.6078 0.4616  -0.0254 0.0598  113 PRO   B C   
1068 O  O   . PRO   B 104 ? 0.9794 0.8897 0.6005 0.4825  -0.0424 0.0480  113 PRO   B O   
1069 C  CB  . PRO   B 104 ? 0.9630 0.8697 0.6343 0.4159  -0.0332 0.0503  113 PRO   B CB  
1070 C  CG  . PRO   B 104 ? 0.9804 0.8674 0.6381 0.4208  -0.0435 0.0396  113 PRO   B CG  
1071 C  CD  . PRO   B 104 ? 0.9741 0.8545 0.5977 0.4587  -0.0501 0.0342  113 PRO   B CD  
1072 N  N   . GLY   B 105 ? 0.9331 0.8961 0.6105 0.4485  -0.0111 0.0729  114 GLY   B N   
1073 C  CA  . GLY   B 105 ? 0.9276 0.9006 0.6065 0.4552  -0.0138 0.0749  114 GLY   B CA  
1074 C  C   . GLY   B 105 ? 0.9270 0.8797 0.6161 0.4267  -0.0268 0.0685  114 GLY   B C   
1075 O  O   . GLY   B 105 ? 0.9426 0.8675 0.6293 0.4080  -0.0373 0.0596  114 GLY   B O   
1076 N  N   . ILE   B 106 ? 0.9083 0.8762 0.6090 0.4237  -0.0262 0.0734  115 ILE   B N   
1077 C  CA  . ILE   B 106 ? 0.9122 0.8605 0.6178 0.4002  -0.0387 0.0683  115 ILE   B CA  
1078 C  C   . ILE   B 106 ? 0.8915 0.8713 0.6290 0.3816  -0.0283 0.0787  115 ILE   B C   
1079 O  O   . ILE   B 106 ? 0.8792 0.8929 0.6289 0.3954  -0.0186 0.0876  115 ILE   B O   
1080 C  CB  . ILE   B 106 ? 0.9369 0.8582 0.6129 0.4204  -0.0577 0.0593  115 ILE   B CB  
1081 C  CG1 . ILE   B 106 ? 0.9730 0.8582 0.6157 0.4397  -0.0724 0.0465  115 ILE   B CG1 
1082 C  CG2 . ILE   B 106 ? 0.9495 0.8506 0.6281 0.3982  -0.0696 0.0567  115 ILE   B CG2 
1083 C  CD1 . ILE   B 106 ? 1.0026 0.8545 0.6435 0.4163  -0.0834 0.0380  115 ILE   B CD1 
1084 N  N   . PHE   B 107 ? 0.8857 0.8547 0.6361 0.3515  -0.0316 0.0768  116 PHE   B N   
1085 C  CA  . PHE   B 107 ? 0.8711 0.8616 0.6463 0.3331  -0.0276 0.0828  116 PHE   B CA  
1086 C  C   . PHE   B 107 ? 0.8969 0.8610 0.6525 0.3333  -0.0452 0.0762  116 PHE   B C   
1087 O  O   . PHE   B 107 ? 0.9155 0.8459 0.6571 0.3200  -0.0551 0.0693  116 PHE   B O   
1088 C  CB  . PHE   B 107 ? 0.8585 0.8471 0.6530 0.3019  -0.0219 0.0830  116 PHE   B CB  
1089 C  CG  . PHE   B 107 ? 0.8412 0.8585 0.6632 0.2944  -0.0044 0.0918  116 PHE   B CG  
1090 C  CD1 . PHE   B 107 ? 0.8398 0.8820 0.6672 0.3146  0.0074  0.1006  116 PHE   B CD1 
1091 C  CD2 . PHE   B 107 ? 0.8412 0.8590 0.6820 0.2681  0.0004  0.0918  116 PHE   B CD2 
1092 C  CE1 . PHE   B 107 ? 0.8307 0.8963 0.6834 0.3065  0.0238  0.1108  116 PHE   B CE1 
1093 C  CE2 . PHE   B 107 ? 0.8358 0.8750 0.7010 0.2611  0.0152  0.1001  116 PHE   B CE2 
1094 C  CZ  . PHE   B 107 ? 0.8227 0.8847 0.6942 0.2794  0.0269  0.1102  116 PHE   B CZ  
1095 N  N   . LYS   B 108 ? 0.8966 0.8752 0.6504 0.3492  -0.0492 0.0788  117 LYS   B N   
1096 C  CA  . LYS   B 108 ? 0.9224 0.8745 0.6559 0.3510  -0.0662 0.0738  117 LYS   B CA  
1097 C  C   . LYS   B 108 ? 0.9131 0.8781 0.6661 0.3271  -0.0657 0.0773  117 LYS   B C   
1098 O  O   . LYS   B 108 ? 0.8903 0.8937 0.6686 0.3271  -0.0580 0.0836  117 LYS   B O   
1099 C  CB  . LYS   B 108 ? 0.9592 0.9189 0.6777 0.3843  -0.0722 0.0738  117 LYS   B CB  
1100 C  CG  . LYS   B 108 ? 1.0479 0.9958 0.7438 0.4120  -0.0731 0.0692  117 LYS   B CG  
1101 C  CD  . LYS   B 108 ? 1.1342 1.0936 0.8147 0.4488  -0.0774 0.0689  117 LYS   B CD  
1102 C  CE  . LYS   B 108 ? 1.2161 1.1640 0.8711 0.4783  -0.0780 0.0632  117 LYS   B CE  
1103 N  NZ  . LYS   B 108 ? 1.2461 1.2117 0.8868 0.5175  -0.0789 0.0634  117 LYS   B NZ  
1104 N  N   . THR   B 109 ? 0.9294 0.8642 0.6721 0.3061  -0.0735 0.0736  118 THR   B N   
1105 C  CA  . THR   B 109 ? 0.9286 0.8722 0.6840 0.2846  -0.0740 0.0757  118 THR   B CA  
1106 C  C   . THR   B 109 ? 0.9499 0.8637 0.6795 0.2856  -0.0897 0.0741  118 THR   B C   
1107 O  O   . THR   B 109 ? 0.9700 0.8500 0.6732 0.2972  -0.1000 0.0710  118 THR   B O   
1108 C  CB  . THR   B 109 ? 0.9408 0.8822 0.7099 0.2570  -0.0651 0.0747  118 THR   B CB  
1109 O  OG1 . THR   B 109 ? 0.9750 0.8786 0.7233 0.2461  -0.0720 0.0708  118 THR   B OG1 
1110 C  CG2 . THR   B 109 ? 0.9320 0.8923 0.7200 0.2574  -0.0512 0.0764  118 THR   B CG2 
1111 N  N   . LYS   B 110 ? 0.9456 0.8689 0.6814 0.2731  -0.0924 0.0760  119 LYS   B N   
1112 C  CA  . LYS   B 110 ? 0.9741 0.8689 0.6840 0.2727  -0.1062 0.0763  119 LYS   B CA  
1113 C  C   . LYS   B 110 ? 1.0045 0.8571 0.6938 0.2563  -0.1091 0.0755  119 LYS   B C   
1114 O  O   . LYS   B 110 ? 1.0284 0.8468 0.6909 0.2599  -0.1209 0.0770  119 LYS   B O   
1115 C  CB  . LYS   B 110 ? 0.9766 0.8938 0.6976 0.2632  -0.1081 0.0780  119 LYS   B CB  
1116 C  CG  . LYS   B 110 ? 0.9965 0.9212 0.7321 0.2364  -0.0995 0.0769  119 LYS   B CG  
1117 C  CD  . LYS   B 110 ? 1.0174 0.9707 0.7685 0.2308  -0.1025 0.0764  119 LYS   B CD  
1118 C  CE  . LYS   B 110 ? 1.0573 0.9960 0.7961 0.2114  -0.1042 0.0748  119 LYS   B CE  
1119 N  NZ  . LYS   B 110 ? 1.0660 1.0126 0.8229 0.1916  -0.0919 0.0716  119 LYS   B NZ  
1120 N  N   . ASP   B 111 ? 0.9980 0.8534 0.7009 0.2388  -0.0984 0.0739  120 ASP   B N   
1121 C  CA  . ASP   B 111 ? 1.0184 0.8418 0.7088 0.2224  -0.0994 0.0736  120 ASP   B CA  
1122 C  C   . ASP   B 111 ? 1.0256 0.8294 0.7106 0.2300  -0.1016 0.0696  120 ASP   B C   
1123 O  O   . ASP   B 111 ? 1.0401 0.8230 0.7220 0.2149  -0.1016 0.0689  120 ASP   B O   
1124 C  CB  . ASP   B 111 ? 1.0343 0.8732 0.7423 0.1988  -0.0872 0.0734  120 ASP   B CB  
1125 C  CG  . ASP   B 111 ? 1.0874 0.9408 0.7970 0.1903  -0.0871 0.0754  120 ASP   B CG  
1126 O  OD1 . ASP   B 111 ? 1.1055 0.9444 0.7948 0.1960  -0.0973 0.0787  120 ASP   B OD1 
1127 O  OD2 . ASP   B 111 ? 1.1004 0.9775 0.8299 0.1788  -0.0778 0.0731  120 ASP   B OD2 
1128 N  N   . GLY   B 112 ? 1.0121 0.8248 0.6968 0.2533  -0.1034 0.0669  121 GLY   B N   
1129 C  CA  . GLY   B 112 ? 1.0193 0.8130 0.6954 0.2640  -0.1075 0.0614  121 GLY   B CA  
1130 C  C   . GLY   B 112 ? 1.0000 0.8227 0.6917 0.2767  -0.0967 0.0594  121 GLY   B C   
1131 O  O   . GLY   B 112 ? 0.9865 0.8449 0.7004 0.2731  -0.0842 0.0634  121 GLY   B O   
1132 N  N   . ASP   B 113 ? 0.9985 0.8047 0.6779 0.2918  -0.1022 0.0535  122 ASP   B N   
1133 C  CA  . ASP   B 113 ? 0.9881 0.8189 0.6769 0.3070  -0.0920 0.0525  122 ASP   B CA  
1134 C  C   . ASP   B 113 ? 0.9758 0.8113 0.6795 0.2904  -0.0831 0.0509  122 ASP   B C   
1135 O  O   . ASP   B 113 ? 0.9866 0.7982 0.6874 0.2736  -0.0893 0.0471  122 ASP   B O   
1136 C  CB  . ASP   B 113 ? 1.0227 0.8356 0.6866 0.3374  -0.1028 0.0459  122 ASP   B CB  
1137 C  CG  . ASP   B 113 ? 1.0983 0.9105 0.7465 0.3610  -0.1106 0.0468  122 ASP   B CG  
1138 O  OD1 . ASP   B 113 ? 1.0987 0.9277 0.7574 0.3538  -0.1076 0.0532  122 ASP   B OD1 
1139 O  OD2 . ASP   B 113 ? 1.1474 0.9421 0.7718 0.3881  -0.1207 0.0402  122 ASP   B OD2 
1140 N  N   . ILE   B 114 ? 0.9479 0.8149 0.6684 0.2958  -0.0683 0.0548  123 ILE   B N   
1141 C  CA  . ILE   B 114 ? 0.9378 0.8108 0.6719 0.2835  -0.0593 0.0538  123 ILE   B CA  
1142 C  C   . ILE   B 114 ? 0.9260 0.8129 0.6565 0.3074  -0.0526 0.0545  123 ILE   B C   
1143 O  O   . ILE   B 114 ? 0.9137 0.8218 0.6445 0.3261  -0.0466 0.0601  123 ILE   B O   
1144 C  CB  . ILE   B 114 ? 0.9293 0.8264 0.6904 0.2602  -0.0454 0.0598  123 ILE   B CB  
1145 C  CG1 . ILE   B 114 ? 0.9449 0.8409 0.7088 0.2450  -0.0490 0.0620  123 ILE   B CG1 
1146 C  CG2 . ILE   B 114 ? 0.9344 0.8266 0.7048 0.2437  -0.0407 0.0566  123 ILE   B CG2 
1147 C  CD1 . ILE   B 114 ? 0.9493 0.8721 0.7375 0.2299  -0.0373 0.0669  123 ILE   B CD1 
1148 N  N   . GLY   B 115 ? 0.9242 0.8021 0.6522 0.3072  -0.0528 0.0495  124 GLY   B N   
1149 C  CA  . GLY   B 115 ? 0.9246 0.8152 0.6468 0.3299  -0.0455 0.0510  124 GLY   B CA  
1150 C  C   . GLY   B 115 ? 0.9039 0.8297 0.6501 0.3257  -0.0250 0.0632  124 GLY   B C   
1151 O  O   . GLY   B 115 ? 0.8942 0.8299 0.6626 0.3015  -0.0181 0.0672  124 GLY   B O   
1152 N  N   . ALA   B 116 ? 0.8968 0.8411 0.6384 0.3492  -0.0151 0.0696  125 ALA   B N   
1153 C  CA  . ALA   B 116 ? 0.8837 0.8607 0.6498 0.3449  0.0049  0.0836  125 ALA   B CA  
1154 C  C   . ALA   B 116 ? 0.8882 0.8758 0.6466 0.3657  0.0163  0.0898  125 ALA   B C   
1155 O  O   . ALA   B 116 ? 0.8930 0.8801 0.6280 0.3945  0.0138  0.0887  125 ALA   B O   
1156 C  CB  . ALA   B 116 ? 0.8697 0.8728 0.6496 0.3479  0.0106  0.0924  125 ALA   B CB  
1157 N  N   . VAL   B 117 ? 0.8842 0.8799 0.6599 0.3524  0.0286  0.0966  126 VAL   B N   
1158 C  CA  A VAL   B 117 ? 0.8914 0.8965 0.6596 0.3712  0.0408  0.1049  126 VAL   B CA  
1159 C  CA  B VAL   B 117 ? 0.8918 0.8965 0.6605 0.3704  0.0408  0.1048  126 VAL   B CA  
1160 C  C   . VAL   B 117 ? 0.8772 0.9165 0.6686 0.3719  0.0618  0.1246  126 VAL   B C   
1161 O  O   . VAL   B 117 ? 0.8632 0.9135 0.6847 0.3470  0.0693  0.1312  126 VAL   B O   
1162 C  CB  A VAL   B 117 ? 0.9080 0.8962 0.6743 0.3627  0.0394  0.0997  126 VAL   B CB  
1163 C  CB  B VAL   B 117 ? 0.9071 0.8957 0.6786 0.3567  0.0397  0.0998  126 VAL   B CB  
1164 C  CG1 A VAL   B 117 ? 0.9340 0.8950 0.6719 0.3757  0.0202  0.0830  126 VAL   B CG1 
1165 C  CG1 B VAL   B 117 ? 0.9105 0.9107 0.6818 0.3691  0.0558  0.1124  126 VAL   B CG1 
1166 C  CG2 A VAL   B 117 ? 0.9066 0.8915 0.6991 0.3292  0.0402  0.0979  126 VAL   B CG2 
1167 C  CG2 B VAL   B 117 ? 0.9320 0.8917 0.6801 0.3623  0.0197  0.0821  126 VAL   B CG2 
1168 N  N   . ALA   B 118 ? 0.8771 0.9342 0.6548 0.4011  0.0710  0.1339  127 ALA   B N   
1169 C  CA  . ALA   B 118 ? 0.8641 0.9582 0.6658 0.4034  0.0921  0.1548  127 ALA   B CA  
1170 C  C   . ALA   B 118 ? 0.8667 0.9694 0.6752 0.4049  0.1107  0.1707  127 ALA   B C   
1171 O  O   . ALA   B 118 ? 0.8561 0.9890 0.6774 0.4144  0.1294  0.1900  127 ALA   B O   
1172 C  CB  . ALA   B 118 ? 0.8602 0.9749 0.6471 0.4340  0.0950  0.1591  127 ALA   B CB  
1173 N  N   . LEU   B 119 ? 0.8758 0.9536 0.6777 0.3953  0.1062  0.1639  128 LEU   B N   
1174 C  CA  . LEU   B 119 ? 0.8727 0.9531 0.6781 0.3972  0.1221  0.1783  128 LEU   B CA  
1175 C  C   . LEU   B 119 ? 0.8603 0.9537 0.7070 0.3672  0.1346  0.1920  128 LEU   B C   
1176 O  O   . LEU   B 119 ? 0.8565 0.9457 0.7244 0.3413  0.1260  0.1835  128 LEU   B O   
1177 C  CB  . LEU   B 119 ? 0.8867 0.9362 0.6693 0.4003  0.1106  0.1647  128 LEU   B CB  
1178 C  CG  . LEU   B 119 ? 0.9174 0.9519 0.6600 0.4295  0.0957  0.1501  128 LEU   B CG  
1179 C  CD1 . LEU   B 119 ? 0.9378 0.9434 0.6670 0.4250  0.0794  0.1328  128 LEU   B CD1 
1180 C  CD2 . LEU   B 119 ? 0.9251 0.9739 0.6432 0.4645  0.1087  0.1632  128 LEU   B CD2 
1181 N  N   . ASP   B 120 ? 0.8552 0.9632 0.7124 0.3712  0.1546  0.2133  129 ASP   B N   
1182 C  CA  . ASP   B 120 ? 0.8465 0.9655 0.7441 0.3436  0.1663  0.2278  129 ASP   B CA  
1183 C  C   . ASP   B 120 ? 0.8438 0.9403 0.7433 0.3331  0.1711  0.2320  129 ASP   B C   
1184 O  O   . ASP   B 120 ? 0.8518 0.9455 0.7334 0.3520  0.1823  0.2441  129 ASP   B O   
1185 C  CB  . ASP   B 120 ? 0.8705 1.0272 0.7881 0.3516  0.1869  0.2527  129 ASP   B CB  
1186 C  CG  . ASP   B 120 ? 0.9422 1.1229 0.9012 0.3276  0.1865  0.2560  129 ASP   B CG  
1187 O  OD1 . ASP   B 120 ? 0.9563 1.1222 0.9364 0.2985  0.1768  0.2465  129 ASP   B OD1 
1188 O  OD2 . ASP   B 120 ? 0.9734 1.1887 0.9436 0.3392  0.1955  0.2674  129 ASP   B OD2 
1189 N  N   . TYR   B 121 ? 0.8354 0.9163 0.7555 0.3045  0.1629  0.2225  130 TYR   B N   
1190 C  CA  . TYR   B 121 ? 0.8404 0.8971 0.7631 0.2932  0.1648  0.2232  130 TYR   B CA  
1191 C  C   . TYR   B 121 ? 0.8136 0.8684 0.7740 0.2605  0.1650  0.2251  130 TYR   B C   
1192 O  O   . TYR   B 121 ? 0.8076 0.8753 0.7871 0.2456  0.1580  0.2187  130 TYR   B O   
1193 C  CB  . TYR   B 121 ? 0.8674 0.8974 0.7636 0.2979  0.1476  0.2001  130 TYR   B CB  
1194 C  CG  . TYR   B 121 ? 0.9016 0.9255 0.7616 0.3292  0.1479  0.2001  130 TYR   B CG  
1195 C  CD1 . TYR   B 121 ? 0.9247 0.9373 0.7737 0.3402  0.1573  0.2110  130 TYR   B CD1 
1196 C  CD2 . TYR   B 121 ? 0.9249 0.9541 0.7603 0.3499  0.1387  0.1904  130 TYR   B CD2 
1197 C  CE1 . TYR   B 121 ? 0.9552 0.9636 0.7690 0.3713  0.1571  0.2114  130 TYR   B CE1 
1198 C  CE2 . TYR   B 121 ? 0.9524 0.9760 0.7531 0.3807  0.1377  0.1898  130 TYR   B CE2 
1199 C  CZ  . TYR   B 121 ? 0.9766 0.9908 0.7662 0.3915  0.1467  0.2000  130 TYR   B CZ  
1200 O  OH  . TYR   B 121 ? 1.0230 1.0315 0.7759 0.4236  0.1445  0.1987  130 TYR   B OH  
1201 N  N   . PRO   B 122 ? 0.7946 0.8313 0.7646 0.2498  0.1715  0.2327  131 PRO   B N   
1202 C  CA  . PRO   B 122 ? 0.7642 0.7944 0.7678 0.2193  0.1687  0.2315  131 PRO   B CA  
1203 C  C   . PRO   B 122 ? 0.7404 0.7567 0.7411 0.2052  0.1498  0.2056  131 PRO   B C   
1204 O  O   . PRO   B 122 ? 0.7537 0.7577 0.7276 0.2165  0.1404  0.1900  131 PRO   B O   
1205 C  CB  . PRO   B 122 ? 0.7842 0.7905 0.7888 0.2168  0.1775  0.2426  131 PRO   B CB  
1206 C  CG  . PRO   B 122 ? 0.8038 0.8116 0.7800 0.2459  0.1886  0.2554  131 PRO   B CG  
1207 C  CD  . PRO   B 122 ? 0.7974 0.8161 0.7461 0.2662  0.1795  0.2414  131 PRO   B CD  
1208 N  N   . ALA   B 123 ? 0.7033 0.7223 0.7320 0.1806  0.1440  0.2012  132 ALA   B N   
1209 C  CA  . ALA   B 123 ? 0.6877 0.6954 0.7130 0.1673  0.1274  0.1782  132 ALA   B CA  
1210 C  C   . ALA   B 123 ? 0.6853 0.6641 0.6906 0.1689  0.1211  0.1635  132 ALA   B C   
1211 O  O   . ALA   B 123 ? 0.6945 0.6673 0.6874 0.1662  0.1093  0.1454  132 ALA   B O   
1212 C  CB  . ALA   B 123 ? 0.6705 0.6833 0.7280 0.1421  0.1223  0.1768  132 ALA   B CB  
1213 N  N   . GLY   B 124 ? 0.6694 0.6320 0.6713 0.1745  0.1296  0.1725  133 GLY   B N   
1214 C  CA  . GLY   B 124 ? 0.6665 0.6045 0.6504 0.1794  0.1248  0.1604  133 GLY   B CA  
1215 C  C   . GLY   B 124 ? 0.6565 0.5956 0.6113 0.2002  0.1202  0.1514  133 GLY   B C   
1216 O  O   . GLY   B 124 ? 0.6597 0.5840 0.6017 0.2040  0.1143  0.1390  133 GLY   B O   
1217 N  N   . THR   B 125 ? 0.6437 0.6009 0.5886 0.2145  0.1220  0.1572  134 THR   B N   
1218 C  CA  . THR   B 125 ? 0.6494 0.6067 0.5672 0.2339  0.1148  0.1476  134 THR   B CA  
1219 C  C   . THR   B 125 ? 0.6388 0.5971 0.5536 0.2242  0.1002  0.1284  134 THR   B C   
1220 O  O   . THR   B 125 ? 0.6488 0.6040 0.5446 0.2358  0.0917  0.1182  134 THR   B O   
1221 C  CB  . THR   B 125 ? 0.6670 0.6400 0.5718 0.2562  0.1225  0.1614  134 THR   B CB  
1222 O  OG1 . THR   B 125 ? 0.6785 0.6524 0.5891 0.2621  0.1384  0.1824  134 THR   B OG1 
1223 C  CG2 . THR   B 125 ? 0.6817 0.6497 0.5556 0.2796  0.1142  0.1519  134 THR   B CG2 
1224 N  N   . SER   B 126 ? 0.6224 0.5841 0.5553 0.2031  0.0968  0.1240  135 SER   B N   
1225 C  CA  . SER   B 126 ? 0.6235 0.5859 0.5534 0.1929  0.0845  0.1087  135 SER   B CA  
1226 C  C   . SER   B 126 ? 0.6342 0.5835 0.5515 0.1926  0.0766  0.0934  135 SER   B C   
1227 O  O   . SER   B 126 ? 0.6404 0.5792 0.5621 0.1872  0.0785  0.0895  135 SER   B O   
1228 C  CB  . SER   B 126 ? 0.6247 0.5897 0.5749 0.1714  0.0829  0.1067  135 SER   B CB  
1229 O  OG  . SER   B 126 ? 0.6393 0.6221 0.6039 0.1697  0.0867  0.1181  135 SER   B OG  
1230 N  N   . GLY   B 127 ? 0.6299 0.5805 0.5336 0.1975  0.0673  0.0849  136 GLY   B N   
1231 C  CA  . GLY   B 127 ? 0.6371 0.5799 0.5324 0.1967  0.0596  0.0718  136 GLY   B CA  
1232 C  C   . GLY   B 127 ? 0.6510 0.5911 0.5309 0.2163  0.0559  0.0705  136 GLY   B C   
1233 O  O   . GLY   B 127 ? 0.6633 0.5995 0.5390 0.2165  0.0486  0.0600  136 GLY   B O   
1234 N  N   . SER   B 128 ? 0.6478 0.5914 0.5192 0.2337  0.0607  0.0810  137 SER   B N   
1235 C  CA  . SER   B 128 ? 0.6588 0.5992 0.5116 0.2557  0.0562  0.0795  137 SER   B CA  
1236 C  C   . SER   B 128 ? 0.6628 0.6007 0.5031 0.2594  0.0416  0.0687  137 SER   B C   
1237 O  O   . SER   B 128 ? 0.6546 0.5956 0.4940 0.2556  0.0388  0.0698  137 SER   B O   
1238 C  CB  . SER   B 128 ? 0.6752 0.6212 0.5199 0.2742  0.0669  0.0950  137 SER   B CB  
1239 O  OG  . SER   B 128 ? 0.6982 0.6407 0.5498 0.2749  0.0785  0.1048  137 SER   B OG  
1240 N  N   . PRO   B 129 ? 0.6737 0.6050 0.5055 0.2665  0.0308  0.0579  138 PRO   B N   
1241 C  CA  . PRO   B 129 ? 0.6882 0.6135 0.5107 0.2672  0.0150  0.0472  138 PRO   B CA  
1242 C  C   . PRO   B 129 ? 0.7152 0.6369 0.5158 0.2897  0.0091  0.0487  138 PRO   B C   
1243 O  O   . PRO   B 129 ? 0.7246 0.6476 0.5116 0.3112  0.0130  0.0537  138 PRO   B O   
1244 C  CB  . PRO   B 129 ? 0.6908 0.6129 0.5162 0.2667  0.0054  0.0357  138 PRO   B CB  
1245 C  CG  . PRO   B 129 ? 0.6916 0.6165 0.5164 0.2787  0.0146  0.0409  138 PRO   B CG  
1246 C  CD  . PRO   B 129 ? 0.6659 0.5949 0.4986 0.2728  0.0314  0.0545  138 PRO   B CD  
1247 N  N   . ILE   B 130 ? 0.7275 0.6436 0.5227 0.2861  -0.0006 0.0442  139 ILE   B N   
1248 C  CA  . ILE   B 130 ? 0.7527 0.6620 0.5249 0.3080  -0.0095 0.0422  139 ILE   B CA  
1249 C  C   . ILE   B 130 ? 0.7786 0.6720 0.5429 0.3093  -0.0299 0.0267  139 ILE   B C   
1250 O  O   . ILE   B 130 ? 0.7737 0.6619 0.5517 0.2879  -0.0371 0.0202  139 ILE   B O   
1251 C  CB  . ILE   B 130 ? 0.7578 0.6690 0.5294 0.3038  -0.0085 0.0469  139 ILE   B CB  
1252 C  CG1 . ILE   B 130 ? 0.7597 0.6900 0.5454 0.2999  0.0106  0.0619  139 ILE   B CG1 
1253 C  CG2 . ILE   B 130 ? 0.7733 0.6751 0.5192 0.3280  -0.0196 0.0427  139 ILE   B CG2 
1254 C  CD1 . ILE   B 130 ? 0.7695 0.7050 0.5628 0.2888  0.0111  0.0652  139 ILE   B CD1 
1255 N  N   . LEU   B 131 ? 0.8001 0.6869 0.5438 0.3340  -0.0389 0.0211  140 LEU   B N   
1256 C  CA  . LEU   B 131 ? 0.8261 0.6988 0.5648 0.3361  -0.0600 0.0055  140 LEU   B CA  
1257 C  C   . LEU   B 131 ? 0.8653 0.7193 0.5790 0.3539  -0.0782 -0.0037 140 LEU   B C   
1258 O  O   . LEU   B 131 ? 0.8760 0.7303 0.5674 0.3778  -0.0742 0.0010  140 LEU   B O   
1259 C  CB  . LEU   B 131 ? 0.8299 0.7073 0.5644 0.3510  -0.0609 0.0023  140 LEU   B CB  
1260 C  CG  . LEU   B 131 ? 0.8394 0.7325 0.5889 0.3451  -0.0415 0.0131  140 LEU   B CG  
1261 C  CD1 . LEU   B 131 ? 0.8449 0.7390 0.5833 0.3659  -0.0452 0.0096  140 LEU   B CD1 
1262 C  CD2 . LEU   B 131 ? 0.8332 0.7326 0.6126 0.3138  -0.0372 0.0121  140 LEU   B CD2 
1263 N  N   . ASP   B 132 ? 0.8854 0.7230 0.6031 0.3434  -0.0989 -0.0171 141 ASP   B N   
1264 C  CA  . ASP   B 132 ? 0.9223 0.7362 0.6156 0.3604  -0.1207 -0.0289 141 ASP   B CA  
1265 C  C   . ASP   B 132 ? 0.9561 0.7642 0.6340 0.3830  -0.1362 -0.0415 141 ASP   B C   
1266 O  O   . ASP   B 132 ? 0.9475 0.7710 0.6362 0.3827  -0.1293 -0.0399 141 ASP   B O   
1267 C  CB  . ASP   B 132 ? 0.9351 0.7300 0.6403 0.3363  -0.1360 -0.0356 141 ASP   B CB  
1268 C  CG  . ASP   B 132 ? 0.9805 0.7726 0.7088 0.3157  -0.1498 -0.0452 141 ASP   B CG  
1269 O  OD1 . ASP   B 132 ? 0.9714 0.7775 0.7079 0.3202  -0.1486 -0.0485 141 ASP   B OD1 
1270 O  OD2 . ASP   B 132 ? 1.0219 0.7984 0.7608 0.2953  -0.1616 -0.0487 141 ASP   B OD2 
1271 N  N   . LYS   B 133 ? 0.9880 0.7725 0.6401 0.4028  -0.1588 -0.0551 142 LYS   B N   
1272 C  CA  . LYS   B 133 ? 1.0181 0.7938 0.6515 0.4265  -0.1779 -0.0696 142 LYS   B CA  
1273 C  C   . LYS   B 133 ? 1.0113 0.7939 0.6724 0.4084  -0.1886 -0.0784 142 LYS   B C   
1274 O  O   . LYS   B 133 ? 1.0166 0.8033 0.6668 0.4282  -0.1963 -0.0857 142 LYS   B O   
1275 C  CB  . LYS   B 133 ? 1.0829 0.8271 0.6871 0.4455  -0.2041 -0.0852 142 LYS   B CB  
1276 C  CG  . LYS   B 133 ? 1.1781 0.9205 0.7421 0.4832  -0.1967 -0.0811 142 LYS   B CG  
1277 C  CD  . LYS   B 133 ? 1.2603 0.9936 0.8177 0.4809  -0.1915 -0.0747 142 LYS   B CD  
1278 C  CE  . LYS   B 133 ? 1.3353 1.0729 0.8549 0.5207  -0.1829 -0.0704 142 LYS   B CE  
1279 N  NZ  . LYS   B 133 ? 1.3875 1.1045 0.8889 0.5300  -0.1922 -0.0744 142 LYS   B NZ  
1280 N  N   . CYS   B 134 ? 0.9950 0.7812 0.6913 0.3727  -0.1884 -0.0769 143 CYS   B N   
1281 C  CA  . CYS   B 134 ? 0.9839 0.7826 0.7112 0.3544  -0.1960 -0.0837 143 CYS   B CA  
1282 C  C   . CYS   B 134 ? 0.9520 0.7801 0.7004 0.3445  -0.1713 -0.0714 143 CYS   B C   
1283 O  O   . CYS   B 134 ? 0.9392 0.7817 0.7160 0.3283  -0.1743 -0.0754 143 CYS   B O   
1284 C  CB  . CYS   B 134 ? 1.0046 0.7926 0.7589 0.3225  -0.2100 -0.0888 143 CYS   B CB  
1285 S  SG  . CYS   B 134 ? 1.1123 0.8586 0.8436 0.3303  -0.2405 -0.1028 143 CYS   B SG  
1286 N  N   . GLY   B 135 ? 0.9351 0.7721 0.6720 0.3528  -0.1475 -0.0566 144 GLY   B N   
1287 C  CA  . GLY   B 135 ? 0.9065 0.7661 0.6613 0.3432  -0.1241 -0.0444 144 GLY   B CA  
1288 C  C   . GLY   B 135 ? 0.8684 0.7363 0.6523 0.3098  -0.1128 -0.0377 144 GLY   B C   
1289 O  O   . GLY   B 135 ? 0.8606 0.7458 0.6630 0.2987  -0.0973 -0.0313 144 GLY   B O   
1290 N  N   . ARG   B 136 ? 0.8453 0.6992 0.6310 0.2949  -0.1208 -0.0393 145 ARG   B N   
1291 C  CA  . ARG   B 136 ? 0.8170 0.6769 0.6256 0.2649  -0.1107 -0.0324 145 ARG   B CA  
1292 C  C   . ARG   B 136 ? 0.7901 0.6552 0.5921 0.2641  -0.0900 -0.0186 145 ARG   B C   
1293 O  O   . ARG   B 136 ? 0.7978 0.6548 0.5773 0.2823  -0.0889 -0.0151 145 ARG   B O   
1294 C  CB  . ARG   B 136 ? 0.8401 0.6812 0.6531 0.2491  -0.1283 -0.0384 145 ARG   B CB  
1295 C  CG  . ARG   B 136 ? 0.8870 0.7288 0.7189 0.2408  -0.1470 -0.0504 145 ARG   B CG  
1296 C  CD  . ARG   B 136 ? 0.9587 0.7817 0.8001 0.2200  -0.1624 -0.0534 145 ARG   B CD  
1297 N  NE  . ARG   B 136 ? 1.0467 0.8385 0.8590 0.2365  -0.1794 -0.0594 145 ARG   B NE  
1298 C  CZ  . ARG   B 136 ? 1.1096 0.8795 0.9134 0.2272  -0.1830 -0.0552 145 ARG   B CZ  
1299 N  NH1 . ARG   B 136 ? 1.1020 0.8782 0.9234 0.2008  -0.1704 -0.0441 145 ARG   B NH1 
1300 N  NH2 . ARG   B 136 ? 1.1414 0.8823 0.9167 0.2461  -0.1995 -0.0622 145 ARG   B NH2 
1301 N  N   . VAL   B 137 ? 0.7532 0.6335 0.5753 0.2444  -0.0738 -0.0112 146 VAL   B N   
1302 C  CA  . VAL   B 137 ? 0.7328 0.6189 0.5524 0.2416  -0.0559 0.0006  146 VAL   B CA  
1303 C  C   . VAL   B 137 ? 0.7217 0.5965 0.5367 0.2302  -0.0592 0.0035  146 VAL   B C   
1304 O  O   . VAL   B 137 ? 0.7178 0.5914 0.5460 0.2086  -0.0611 0.0029  146 VAL   B O   
1305 C  CB  . VAL   B 137 ? 0.7216 0.6250 0.5607 0.2276  -0.0392 0.0057  146 VAL   B CB  
1306 C  CG1 . VAL   B 137 ? 0.7218 0.6299 0.5584 0.2267  -0.0233 0.0169  146 VAL   B CG1 
1307 C  CG2 . VAL   B 137 ? 0.7262 0.6385 0.5693 0.2395  -0.0376 0.0023  146 VAL   B CG2 
1308 N  N   . ILE   B 138 ? 0.7127 0.5801 0.5084 0.2463  -0.0596 0.0073  147 ILE   B N   
1309 C  CA  . ILE   B 138 ? 0.7076 0.5634 0.4957 0.2403  -0.0638 0.0101  147 ILE   B CA  
1310 C  C   . ILE   B 138 ? 0.6954 0.5647 0.4911 0.2304  -0.0472 0.0210  147 ILE   B C   
1311 O  O   . ILE   B 138 ? 0.7020 0.5640 0.4934 0.2235  -0.0500 0.0237  147 ILE   B O   
1312 C  CB  . ILE   B 138 ? 0.7163 0.5557 0.4782 0.2652  -0.0765 0.0060  147 ILE   B CB  
1313 C  CG1 . ILE   B 138 ? 0.7193 0.5720 0.4693 0.2904  -0.0655 0.0116  147 ILE   B CG1 
1314 C  CG2 . ILE   B 138 ? 0.7271 0.5468 0.4819 0.2700  -0.0981 -0.0072 147 ILE   B CG2 
1315 C  CD1 . ILE   B 138 ? 0.7403 0.5831 0.4647 0.3156  -0.0727 0.0103  147 ILE   B CD1 
1316 N  N   . GLY   B 139 ? 0.6764 0.5635 0.4835 0.2294  -0.0318 0.0266  148 GLY   B N   
1317 C  CA  . GLY   B 139 ? 0.6689 0.5683 0.4856 0.2193  -0.0182 0.0354  148 GLY   B CA  
1318 C  C   . GLY   B 139 ? 0.6656 0.5798 0.4920 0.2236  -0.0034 0.0417  148 GLY   B C   
1319 O  O   . GLY   B 139 ? 0.6673 0.5822 0.4901 0.2368  -0.0027 0.0403  148 GLY   B O   
1320 N  N   . LEU   B 140 ? 0.6594 0.5840 0.4977 0.2128  0.0076  0.0487  149 LEU   B N   
1321 C  CA  . LEU   B 140 ? 0.6561 0.5915 0.5055 0.2142  0.0212  0.0558  149 LEU   B CA  
1322 C  C   . LEU   B 140 ? 0.6554 0.6019 0.5074 0.2211  0.0288  0.0668  149 LEU   B C   
1323 O  O   . LEU   B 140 ? 0.6567 0.6061 0.5089 0.2163  0.0254  0.0680  149 LEU   B O   
1324 C  CB  . LEU   B 140 ? 0.6540 0.5918 0.5193 0.1946  0.0271  0.0536  149 LEU   B CB  
1325 C  CG  . LEU   B 140 ? 0.6742 0.6074 0.5418 0.1865  0.0227  0.0439  149 LEU   B CG  
1326 C  CD1 . LEU   B 140 ? 0.6720 0.6090 0.5524 0.1708  0.0300  0.0420  149 LEU   B CD1 
1327 C  CD2 . LEU   B 140 ? 0.6877 0.6192 0.5511 0.2016  0.0209  0.0413  149 LEU   B CD2 
1328 N  N   . TYR   B 141 ? 0.6535 0.6073 0.5082 0.2326  0.0393  0.0758  150 TYR   B N   
1329 C  CA  . TYR   B 141 ? 0.6576 0.6263 0.5181 0.2407  0.0493  0.0890  150 TYR   B CA  
1330 C  C   . TYR   B 141 ? 0.6416 0.6181 0.5262 0.2225  0.0590  0.0956  150 TYR   B C   
1331 O  O   . TYR   B 141 ? 0.6390 0.6084 0.5299 0.2154  0.0629  0.0940  150 TYR   B O   
1332 C  CB  . TYR   B 141 ? 0.6741 0.6446 0.5218 0.2644  0.0558  0.0962  150 TYR   B CB  
1333 C  CG  . TYR   B 141 ? 0.6886 0.6768 0.5451 0.2729  0.0710  0.1137  150 TYR   B CG  
1334 C  CD1 . TYR   B 141 ? 0.6977 0.6884 0.5689 0.2670  0.0840  0.1245  150 TYR   B CD1 
1335 C  CD2 . TYR   B 141 ? 0.7030 0.7052 0.5525 0.2887  0.0728  0.1203  150 TYR   B CD2 
1336 C  CE1 . TYR   B 141 ? 0.7022 0.7098 0.5845 0.2730  0.0990  0.1429  150 TYR   B CE1 
1337 C  CE2 . TYR   B 141 ? 0.7052 0.7283 0.5655 0.2967  0.0886  0.1382  150 TYR   B CE2 
1338 C  CZ  . TYR   B 141 ? 0.7099 0.7360 0.5877 0.2878  0.1020  0.1503  150 TYR   B CZ  
1339 O  OH  . TYR   B 141 ? 0.7169 0.7644 0.6084 0.2936  0.1185  0.1703  150 TYR   B OH  
1340 N  N   . GLY   B 142 ? 0.6337 0.6241 0.5318 0.2157  0.0616  0.1020  151 GLY   B N   
1341 C  CA  . GLY   B 142 ? 0.6303 0.6272 0.5531 0.1977  0.0682  0.1071  151 GLY   B CA  
1342 C  C   . GLY   B 142 ? 0.6268 0.6343 0.5627 0.1842  0.0629  0.1056  151 GLY   B C   
1343 O  O   . GLY   B 142 ? 0.6157 0.6311 0.5741 0.1706  0.0670  0.1103  151 GLY   B O   
1344 N  N   . ASN   B 143 ? 0.6334 0.6396 0.5552 0.1880  0.0526  0.0988  152 ASN   B N   
1345 C  CA  . ASN   B 143 ? 0.6392 0.6556 0.5702 0.1782  0.0463  0.0975  152 ASN   B CA  
1346 C  C   . ASN   B 143 ? 0.6531 0.6824 0.5766 0.1952  0.0436  0.1024  152 ASN   B C   
1347 O  O   . ASN   B 143 ? 0.6713 0.6884 0.5717 0.2067  0.0357  0.0965  152 ASN   B O   
1348 C  CB  . ASN   B 143 ? 0.6587 0.6596 0.5793 0.1648  0.0357  0.0848  152 ASN   B CB  
1349 C  CG  . ASN   B 143 ? 0.6793 0.6897 0.6091 0.1540  0.0291  0.0833  152 ASN   B CG  
1350 O  OD1 . ASN   B 143 ? 0.6744 0.7036 0.6261 0.1508  0.0325  0.0902  152 ASN   B OD1 
1351 N  ND2 . ASN   B 143 ? 0.6861 0.6847 0.6003 0.1482  0.0193  0.0748  152 ASN   B ND2 
1352 N  N   . GLY   B 144 ? 0.6439 0.6979 0.5880 0.1967  0.0496  0.1128  153 GLY   B N   
1353 C  CA  . GLY   B 144 ? 0.6572 0.7282 0.5965 0.2150  0.0485  0.1181  153 GLY   B CA  
1354 C  C   . GLY   B 144 ? 0.6590 0.7617 0.6283 0.2105  0.0529  0.1280  153 GLY   B C   
1355 O  O   . GLY   B 144 ? 0.6546 0.7616 0.6431 0.1909  0.0482  0.1249  153 GLY   B O   
1356 N  N   . VAL   B 145 ? 0.6643 0.7910 0.6381 0.2296  0.0618  0.1397  154 VAL   B N   
1357 C  CA  . VAL   B 145 ? 0.6646 0.8278 0.6690 0.2285  0.0663  0.1504  154 VAL   B CA  
1358 C  C   . VAL   B 145 ? 0.6758 0.8671 0.6984 0.2399  0.0856  0.1696  154 VAL   B C   
1359 O  O   . VAL   B 145 ? 0.6905 0.8719 0.6934 0.2555  0.0943  0.1739  154 VAL   B O   
1360 C  CB  . VAL   B 145 ? 0.6711 0.8406 0.6603 0.2439  0.0544  0.1443  154 VAL   B CB  
1361 C  CG1 . VAL   B 145 ? 0.6782 0.8539 0.6451 0.2755  0.0597  0.1491  154 VAL   B CG1 
1362 C  CG2 . VAL   B 145 ? 0.6614 0.8630 0.6826 0.2350  0.0509  0.1482  154 VAL   B CG2 
1363 N  N   . VAL   B 146 ? 0.6675 0.8943 0.7288 0.2313  0.0923  0.1817  155 VAL   B N   
1364 C  CA  . VAL   B 146 ? 0.6755 0.9340 0.7589 0.2401  0.1121  0.2029  155 VAL   B CA  
1365 C  C   . VAL   B 146 ? 0.6963 0.9919 0.7844 0.2619  0.1142  0.2092  155 VAL   B C   
1366 O  O   . VAL   B 146 ? 0.6875 0.9998 0.7925 0.2550  0.1031  0.2038  155 VAL   B O   
1367 C  CB  . VAL   B 146 ? 0.6587 0.9310 0.7875 0.2123  0.1196  0.2142  155 VAL   B CB  
1368 C  CG1 . VAL   B 146 ? 0.6436 0.9486 0.7958 0.2207  0.1420  0.2392  155 VAL   B CG1 
1369 C  CG2 . VAL   B 146 ? 0.6800 0.9123 0.8005 0.1933  0.1157  0.2055  155 VAL   B CG2 
1370 N  N   . ILE   B 147 ? 0.7248 1.0315 0.7934 0.2909  0.1267  0.2187  156 ILE   B N   
1371 C  CA  . ILE   B 147 ? 0.7497 1.0904 0.8165 0.3175  0.1294  0.2238  156 ILE   B CA  
1372 C  C   . ILE   B 147 ? 0.7438 1.1398 0.8568 0.3168  0.1490  0.2476  156 ILE   B C   
1373 O  O   . ILE   B 147 ? 0.7342 1.1373 0.8796 0.2940  0.1599  0.2604  156 ILE   B O   
1374 C  CB  . ILE   B 147 ? 0.7899 1.1110 0.8062 0.3524  0.1299  0.2185  156 ILE   B CB  
1375 C  CG1 . ILE   B 147 ? 0.8156 1.1278 0.8203 0.3593  0.1469  0.2302  156 ILE   B CG1 
1376 C  CG2 . ILE   B 147 ? 0.8250 1.1001 0.8034 0.3530  0.1072  0.1949  156 ILE   B CG2 
1377 C  CD1 . ILE   B 147 ? 0.8544 1.1536 0.8115 0.3966  0.1481  0.2264  156 ILE   B CD1 
1378 N  N   . LYS   B 148 ? 0.7469 1.1820 0.8645 0.3412  0.1529  0.2535  157 LYS   B N   
1379 C  CA  . LYS   B 148 ? 0.7341 1.2294 0.8971 0.3440  0.1719  0.2766  157 LYS   B CA  
1380 C  C   . LYS   B 148 ? 0.7430 1.2513 0.9222 0.3404  0.1977  0.3008  157 LYS   B C   
1381 O  O   . LYS   B 148 ? 0.7191 1.2631 0.9501 0.3200  0.2102  0.3196  157 LYS   B O   
1382 C  CB  . LYS   B 148 ? 0.7516 1.2794 0.8992 0.3825  0.1749  0.2783  157 LYS   B CB  
1383 C  CG  . LYS   B 148 ? 0.8187 1.3285 0.9426 0.3915  0.1497  0.2555  157 LYS   B CG  
1384 C  CD  . LYS   B 148 ? 0.8622 1.4142 0.9847 0.4263  0.1526  0.2592  157 LYS   B CD  
1385 C  CE  . LYS   B 148 ? 0.8694 1.4805 1.0513 0.4137  0.1556  0.2704  157 LYS   B CE  
1386 N  NZ  . LYS   B 148 ? 0.8966 1.4926 1.0913 0.3894  0.1306  0.2536  157 LYS   B NZ  
1387 N  N   . ASN   B 149 ? 0.7700 1.2487 0.9051 0.3601  0.2047  0.3006  158 ASN   B N   
1388 C  CA  . ASN   B 149 ? 0.7727 1.2586 0.9141 0.3612  0.2289  0.3236  158 ASN   B CA  
1389 C  C   . ASN   B 149 ? 0.7768 1.2228 0.9244 0.3300  0.2264  0.3221  158 ASN   B C   
1390 O  O   . ASN   B 149 ? 0.7913 1.2249 0.9252 0.3358  0.2415  0.3352  158 ASN   B O   
1391 C  CB  . ASN   B 149 ? 0.8199 1.3002 0.9102 0.4033  0.2395  0.3265  158 ASN   B CB  
1392 C  CG  . ASN   B 149 ? 0.9064 1.3466 0.9418 0.4251  0.2175  0.2990  158 ASN   B CG  
1393 O  OD1 . ASN   B 149 ? 0.9183 1.3692 0.9459 0.4401  0.2055  0.2875  158 ASN   B OD1 
1394 N  ND2 . ASN   B 149 ? 0.9505 1.3435 0.9485 0.4270  0.2109  0.2883  158 ASN   B ND2 
1395 N  N   . GLY   B 150 ? 0.7598 1.1865 0.9261 0.2992  0.2075  0.3066  159 GLY   B N   
1396 C  CA  . GLY   B 150 ? 0.7601 1.1498 0.9339 0.2696  0.2029  0.3027  159 GLY   B CA  
1397 C  C   . GLY   B 150 ? 0.7801 1.1183 0.9041 0.2786  0.1952  0.2874  159 GLY   B C   
1398 O  O   . GLY   B 150 ? 0.7894 1.0953 0.9158 0.2567  0.1901  0.2817  159 GLY   B O   
1399 N  N   . SER   B 151 ? 0.7817 1.1123 0.8608 0.3115  0.1934  0.2799  160 SER   B N   
1400 C  CA  A SER   B 151 ? 0.8063 1.0914 0.8394 0.3219  0.1845  0.2647  160 SER   B CA  
1401 C  CA  B SER   B 151 ? 0.8081 1.0935 0.8412 0.3221  0.1846  0.2648  160 SER   B CA  
1402 C  C   . SER   B 151 ? 0.8095 1.0602 0.8324 0.3039  0.1606  0.2392  160 SER   B C   
1403 O  O   . SER   B 151 ? 0.7938 1.0552 0.8348 0.2914  0.1493  0.2313  160 SER   B O   
1404 C  CB  A SER   B 151 ? 0.8368 1.1234 0.8265 0.3619  0.1868  0.2627  160 SER   B CB  
1405 C  CB  B SER   B 151 ? 0.8437 1.1310 0.8337 0.3622  0.1869  0.2628  160 SER   B CB  
1406 O  OG  A SER   B 151 ? 0.8898 1.1335 0.8381 0.3708  0.1756  0.2467  160 SER   B OG  
1407 O  OG  B SER   B 151 ? 0.8632 1.1864 0.8604 0.3819  0.2105  0.2873  160 SER   B OG  
1408 N  N   . TYR   B 152 ? 0.8111 1.0222 0.8058 0.3029  0.1533  0.2271  161 TYR   B N   
1409 C  CA  . TYR   B 152 ? 0.8084 0.9874 0.7921 0.2867  0.1333  0.2049  161 TYR   B CA  
1410 C  C   . TYR   B 152 ? 0.8044 0.9613 0.7457 0.3082  0.1197  0.1885  161 TYR   B C   
1411 O  O   . TYR   B 152 ? 0.8202 0.9672 0.7335 0.3305  0.1237  0.1895  161 TYR   B O   
1412 C  CB  . TYR   B 152 ? 0.8202 0.9716 0.8074 0.2673  0.1339  0.2024  161 TYR   B CB  
1413 C  CG  . TYR   B 152 ? 0.8391 0.9680 0.8291 0.2438  0.1170  0.1836  161 TYR   B CG  
1414 C  CD1 . TYR   B 152 ? 0.8363 0.9780 0.8564 0.2219  0.1117  0.1822  161 TYR   B CD1 
1415 C  CD2 . TYR   B 152 ? 0.8690 0.9658 0.8317 0.2445  0.1061  0.1675  161 TYR   B CD2 
1416 C  CE1 . TYR   B 152 ? 0.8553 0.9768 0.8738 0.2031  0.0969  0.1654  161 TYR   B CE1 
1417 C  CE2 . TYR   B 152 ? 0.8849 0.9640 0.8494 0.2244  0.0928  0.1520  161 TYR   B CE2 
1418 C  CZ  . TYR   B 152 ? 0.8834 0.9741 0.8737 0.2045  0.0886  0.1511  161 TYR   B CZ  
1419 O  OH  . TYR   B 152 ? 0.9057 0.9797 0.8948 0.1866  0.0763  0.1364  161 TYR   B OH  
1420 N  N   . VAL   B 153 ? 0.7795 0.9268 0.7154 0.3014  0.1028  0.1731  162 VAL   B N   
1421 C  CA  . VAL   B 153 ? 0.7767 0.8980 0.6754 0.3169  0.0874  0.1569  162 VAL   B CA  
1422 C  C   . VAL   B 153 ? 0.7550 0.8490 0.6535 0.2923  0.0732  0.1418  162 VAL   B C   
1423 O  O   . VAL   B 153 ? 0.7436 0.8441 0.6610 0.2739  0.0680  0.1393  162 VAL   B O   
1424 C  CB  . VAL   B 153 ? 0.7865 0.9219 0.6736 0.3383  0.0813  0.1550  162 VAL   B CB  
1425 C  CG1 . VAL   B 153 ? 0.8133 0.9147 0.6656 0.3471  0.0615  0.1365  162 VAL   B CG1 
1426 C  CG2 . VAL   B 153 ? 0.7873 0.9491 0.6680 0.3679  0.0966  0.1692  162 VAL   B CG2 
1427 N  N   . SER   B 154 ? 0.7489 0.8153 0.6285 0.2915  0.0682  0.1327  163 SER   B N   
1428 C  CA  . SER   B 154 ? 0.7410 0.7840 0.6204 0.2694  0.0572  0.1196  163 SER   B CA  
1429 C  C   . SER   B 154 ? 0.7410 0.7618 0.5943 0.2757  0.0402  0.1056  163 SER   B C   
1430 O  O   . SER   B 154 ? 0.7517 0.7662 0.5821 0.2985  0.0358  0.1032  163 SER   B O   
1431 C  CB  . SER   B 154 ? 0.7504 0.7795 0.6297 0.2631  0.0625  0.1188  163 SER   B CB  
1432 O  OG  . SER   B 154 ? 0.7754 0.7814 0.6470 0.2494  0.0515  0.1049  163 SER   B OG  
1433 N  N   . ALA   B 155 ? 0.7308 0.7379 0.5866 0.2559  0.0306  0.0966  164 ALA   B N   
1434 C  CA  . ALA   B 155 ? 0.7394 0.7223 0.5727 0.2577  0.0150  0.0850  164 ALA   B CA  
1435 C  C   . ALA   B 155 ? 0.7452 0.7076 0.5679 0.2557  0.0114  0.0770  164 ALA   B C   
1436 O  O   . ALA   B 155 ? 0.7326 0.6990 0.5664 0.2494  0.0205  0.0795  164 ALA   B O   
1437 C  CB  . ALA   B 155 ? 0.7362 0.7145 0.5762 0.2371  0.0080  0.0809  164 ALA   B CB  
1438 N  N   . ILE   B 156 ? 0.7593 0.6994 0.5616 0.2614  -0.0028 0.0675  165 ILE   B N   
1439 C  CA  . ILE   B 156 ? 0.7699 0.6928 0.5665 0.2567  -0.0088 0.0590  165 ILE   B CA  
1440 C  C   . ILE   B 156 ? 0.7685 0.6828 0.5736 0.2313  -0.0132 0.0547  165 ILE   B C   
1441 O  O   . ILE   B 156 ? 0.7778 0.6757 0.5718 0.2277  -0.0251 0.0502  165 ILE   B O   
1442 C  CB  . ILE   B 156 ? 0.7922 0.6954 0.5645 0.2759  -0.0231 0.0507  165 ILE   B CB  
1443 C  CG1 . ILE   B 156 ? 0.8073 0.7211 0.5666 0.3051  -0.0179 0.0557  165 ILE   B CG1 
1444 C  CG2 . ILE   B 156 ? 0.8008 0.6900 0.5730 0.2687  -0.0303 0.0416  165 ILE   B CG2 
1445 C  CD1 . ILE   B 156 ? 0.8391 0.7333 0.5711 0.3275  -0.0331 0.0465  165 ILE   B CD1 
1446 N  N   . THR   B 157 ? 0.7512 0.6765 0.5747 0.2147  -0.0028 0.0571  166 THR   B N   
1447 C  CA  . THR   B 157 ? 0.7467 0.6685 0.5779 0.1923  -0.0037 0.0541  166 THR   B CA  
1448 C  C   . THR   B 157 ? 0.7529 0.6630 0.5831 0.1831  -0.0084 0.0468  166 THR   B C   
1449 O  O   . THR   B 157 ? 0.7466 0.6618 0.5857 0.1819  -0.0023 0.0449  166 THR   B O   
1450 C  CB  . THR   B 157 ? 0.7411 0.6786 0.5907 0.1810  0.0080  0.0584  166 THR   B CB  
1451 O  OG1 . THR   B 157 ? 0.7460 0.6980 0.6016 0.1886  0.0121  0.0661  166 THR   B OG1 
1452 C  CG2 . THR   B 157 ? 0.7394 0.6743 0.5927 0.1615  0.0068  0.0549  166 THR   B CG2 
1453 N  N   . GLN   B 158 ? 0.7603 0.6554 0.5814 0.1761  -0.0189 0.0434  167 GLN   B N   
1454 C  CA  . GLN   B 158 ? 0.7668 0.6537 0.5912 0.1650  -0.0233 0.0378  167 GLN   B CA  
1455 C  C   . GLN   B 158 ? 0.7883 0.6755 0.6171 0.1441  -0.0204 0.0393  167 GLN   B C   
1456 O  O   . GLN   B 158 ? 0.7917 0.6763 0.6133 0.1407  -0.0214 0.0433  167 GLN   B O   
1457 C  CB  . GLN   B 158 ? 0.7730 0.6402 0.5846 0.1737  -0.0388 0.0332  167 GLN   B CB  
1458 C  CG  . GLN   B 158 ? 0.7828 0.6427 0.6019 0.1621  -0.0459 0.0274  167 GLN   B CG  
1459 C  CD  . GLN   B 158 ? 0.8005 0.6749 0.6337 0.1635  -0.0401 0.0232  167 GLN   B CD  
1460 O  OE1 . GLN   B 158 ? 0.8133 0.7037 0.6582 0.1566  -0.0271 0.0253  167 GLN   B OE1 
1461 N  NE2 . GLN   B 158 ? 0.7902 0.6578 0.6220 0.1726  -0.0510 0.0163  167 GLN   B NE2 
1462 N  N   . GLY   B 159 ? 0.7970 0.6894 0.6367 0.1323  -0.0164 0.0362  168 GLY   B N   
1463 C  CA  . GLY   B 159 ? 0.8196 0.7141 0.6617 0.1145  -0.0122 0.0380  168 GLY   B CA  
1464 C  C   . GLY   B 159 ? 0.8541 0.7350 0.6931 0.1046  -0.0209 0.0390  168 GLY   B C   
1465 O  O   . GLY   B 159 ? 0.8615 0.7300 0.6981 0.1110  -0.0321 0.0363  168 GLY   B O   
1466 N  N   . LYS   B 160 ? 0.8778 0.7601 0.7162 0.0891  -0.0162 0.0432  169 LYS   B N   
1467 C  CA  . LYS   B 160 ? 0.9083 0.7783 0.7463 0.0765  -0.0226 0.0471  169 LYS   B CA  
1468 C  C   . LYS   B 160 ? 0.9191 0.8056 0.7769 0.0647  -0.0156 0.0456  169 LYS   B C   
1469 O  O   . LYS   B 160 ? 0.9154 0.8203 0.7789 0.0597  -0.0027 0.0457  169 LYS   B O   
1470 C  CB  . LYS   B 160 ? 0.9419 0.8014 0.7639 0.0677  -0.0218 0.0556  169 LYS   B CB  
1471 C  CG  . LYS   B 160 ? 1.0078 0.8503 0.8284 0.0543  -0.0285 0.0623  169 LYS   B CG  
1472 C  CD  . LYS   B 160 ? 1.0819 0.9220 0.8904 0.0420  -0.0215 0.0726  169 LYS   B CD  
1473 C  CE  . LYS   B 160 ? 1.1432 0.9656 0.9526 0.0271  -0.0270 0.0818  169 LYS   B CE  
1474 N  NZ  . LYS   B 160 ? 1.1887 1.0055 0.9812 0.0172  -0.0202 0.0942  169 LYS   B NZ  
1475 N  N   . ARG   B 161 ? 0.9277 0.8086 0.7968 0.0613  -0.0252 0.0434  170 ARG   B N   
1476 C  CA  . ARG   B 161 ? 0.9273 0.8273 0.8197 0.0498  -0.0200 0.0424  170 ARG   B CA  
1477 C  C   . ARG   B 161 ? 0.9463 0.8424 0.8402 0.0299  -0.0172 0.0531  170 ARG   B C   
1478 O  O   . ARG   B 161 ? 0.9588 0.8307 0.8456 0.0245  -0.0291 0.0579  170 ARG   B O   
1479 C  CB  . ARG   B 161 ? 0.9325 0.8300 0.8388 0.0553  -0.0334 0.0344  170 ARG   B CB  
1480 C  CG  . ARG   B 161 ? 0.9381 0.8615 0.8722 0.0467  -0.0284 0.0316  170 ARG   B CG  
1481 C  CD  . ARG   B 161 ? 0.9654 0.8855 0.9145 0.0497  -0.0450 0.0236  170 ARG   B CD  
1482 N  NE  . ARG   B 161 ? 0.9727 0.9203 0.9528 0.0374  -0.0408 0.0229  170 ARG   B NE  
1483 C  CZ  . ARG   B 161 ? 0.9737 0.9432 0.9700 0.0469  -0.0401 0.0141  170 ARG   B CZ  
1484 N  NH1 . ARG   B 161 ? 0.9614 0.9258 0.9443 0.0684  -0.0433 0.0062  170 ARG   B NH1 
1485 N  NH2 . ARG   B 161 ? 0.9538 0.9515 0.9800 0.0357  -0.0359 0.0141  170 ARG   B NH2 
1486 N  N   . GLU   B 162 ? 0.9490 0.8672 0.8498 0.0204  -0.0013 0.0576  171 GLU   B N   
1487 C  CA  . GLU   B 162 ? 0.9671 0.8856 0.8684 0.0023  0.0049  0.0701  171 GLU   B CA  
1488 C  C   . GLU   B 162 ? 0.9567 0.8856 0.8873 -0.0124 0.0017  0.0728  171 GLU   B C   
1489 O  O   . GLU   B 162 ? 0.9529 0.8911 0.8919 -0.0291 0.0106  0.0844  171 GLU   B O   
1490 C  CB  . GLU   B 162 ? 1.0103 0.9503 0.9050 0.0006  0.0239  0.0734  171 GLU   B CB  
1491 C  CG  . GLU   B 162 ? 1.1157 1.0495 0.9870 0.0141  0.0260  0.0687  171 GLU   B CG  
1492 C  CD  . GLU   B 162 ? 1.2670 1.1771 1.1117 0.0132  0.0210  0.0768  171 GLU   B CD  
1493 O  OE1 . GLU   B 162 ? 1.3051 1.2080 1.1345 0.0249  0.0177  0.0721  171 GLU   B OE1 
1494 O  OE2 . GLU   B 162 ? 1.3162 1.2153 1.1564 0.0008  0.0202  0.0884  171 GLU   B OE2 
1495 S  S   . DMS   C .   ? 1.1525 0.9955 1.0342 0.0864  0.0192  -0.0639 201 DMS   B S   
1496 O  O   . DMS   C .   ? 1.1474 1.0136 1.0188 0.0906  0.0284  -0.0572 201 DMS   B O   
1497 C  C1  . DMS   C .   ? 1.1604 0.9834 1.0433 0.0980  0.0252  -0.0695 201 DMS   B C1  
1498 C  C2  . DMS   C .   ? 1.1403 0.9826 1.0535 0.0776  0.0193  -0.0458 201 DMS   B C2  
1499 N  N1  . A1B9G D .   ? 0.6865 0.7207 0.7038 0.1413  0.0772  0.1260  202 A1B9G B N1  
1500 N  N3  . A1B9G D .   ? 0.7015 0.8149 0.7482 0.1996  0.1381  0.2062  202 A1B9G B N3  
1501 C  C4  . A1B9G D .   ? 0.6608 0.6760 0.7044 0.0928  0.0523  0.0974  202 A1B9G B C4  
1502 C  C5  . A1B9G D .   ? 0.6657 0.6800 0.6879 0.0960  0.0429  0.0866  202 A1B9G B C5  
1503 C  C6  . A1B9G D .   ? 0.6719 0.6885 0.6730 0.1118  0.0444  0.0885  202 A1B9G B C6  
1504 C  C7  . A1B9G D .   ? 0.6757 0.6986 0.6767 0.1261  0.0549  0.1006  202 A1B9G B C7  
1505 C  C8  . A1B9G D .   ? 0.6763 0.6869 0.6539 0.1136  0.0343  0.0781  202 A1B9G B C8  
1506 C  C10 . A1B9G D .   ? 0.6589 0.6809 0.6792 0.0822  0.0215  0.0708  202 A1B9G B C10 
1507 C  C13 . A1B9G D .   ? 0.7419 0.7806 0.7226 0.2005  0.1095  0.1593  202 A1B9G B C13 
1508 C  C15 . A1B9G D .   ? 0.7135 0.7974 0.7385 0.1957  0.1256  0.1871  202 A1B9G B C15 
1509 C  C17 . A1B9G D .   ? 0.7067 0.7868 0.7492 0.1725  0.1140  0.1756  202 A1B9G B C17 
1510 O  O1  . A1B9G D .   ? 0.6821 0.7424 0.7506 0.1273  0.0897  0.1490  202 A1B9G B O1  
1511 C  C1  . A1B9G D .   ? 0.6933 0.7427 0.7323 0.1426  0.0890  0.1432  202 A1B9G B C1  
1512 C  C2  . A1B9G D .   ? 0.6753 0.7019 0.6961 0.1244  0.0657  0.1125  202 A1B9G B C2  
1513 C  C3  . A1B9G D .   ? 0.6633 0.6862 0.7071 0.1066  0.0644  0.1117  202 A1B9G B C3  
1514 N  N2  . A1B9G D .   ? 0.6708 0.6944 0.6546 0.1085  0.0247  0.0762  202 A1B9G B N2  
1515 C  C9  . A1B9G D .   ? 0.6697 0.6880 0.6609 0.0926  0.0174  0.0667  202 A1B9G B C9  
1516 O  O2  . A1B9G D .   ? 0.6674 0.6741 0.6841 0.0849  0.0317  0.0731  202 A1B9G B O2  
1517 C  C11 . A1B9G D .   ? 0.7136 0.7675 0.7392 0.1643  0.1012  0.1559  202 A1B9G B C11 
1518 C  C12 . A1B9G D .   ? 0.7360 0.7713 0.7319 0.1786  0.1001  0.1489  202 A1B9G B C12 
1519 CL CL1 . A1B9G D .   ? 0.7650 0.7805 0.7112 0.2173  0.1046  0.1482  202 A1B9G B CL1 
1520 C  C14 . A1B9G D .   ? 0.7285 0.7904 0.7205 0.2108  0.1225  0.1783  202 A1B9G B C14 
1521 N  N4  . A1B9G D .   ? 0.6852 0.8151 0.7658 0.1789  0.1341  0.2072  202 A1B9G B N4  
1522 C  C16 . A1B9G D .   ? 0.6894 0.7981 0.7659 0.1632  0.1189  0.1883  202 A1B9G B C16 
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