data_7I1T
# 
_entry.id   7I1T 
# 
_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   7I1T         pdb_00007i1t 10.2210/pdb7i1t/pdb 
WWPDB D_1001408208 ?            ?                   
# 
loop_
_pdbx_audit_revision_history.ordinal 
_pdbx_audit_revision_history.data_content_type 
_pdbx_audit_revision_history.major_revision 
_pdbx_audit_revision_history.minor_revision 
_pdbx_audit_revision_history.revision_date 
_pdbx_audit_revision_history.part_number 
1 'Structure model' 1 0 2025-03-05 ? 
2 'Structure model' 1 1 2025-05-28 ? 
# 
_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_audit_revision_group.ordinal             1 
_pdbx_audit_revision_group.revision_ordinal    2 
_pdbx_audit_revision_group.data_content_type   'Structure model' 
_pdbx_audit_revision_group.group               'Structure summary' 
# 
_pdbx_audit_revision_category.ordinal             1 
_pdbx_audit_revision_category.revision_ordinal    2 
_pdbx_audit_revision_category.data_content_type   'Structure model' 
_pdbx_audit_revision_category.category            pdbx_deposit_group 
# 
_pdbx_audit_revision_item.ordinal             1 
_pdbx_audit_revision_item.revision_ordinal    2 
_pdbx_audit_revision_item.data_content_type   'Structure model' 
_pdbx_audit_revision_item.item                '_pdbx_deposit_group.group_description' 
# 
_pdbx_database_status.entry_id                        7I1T 
_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   2025-02-20 
_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 
'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  
'Balaji, G.'          9  
'Phelps, J.'          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                     'PanDDA analysis group deposition' 
_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 'Balaji, G.'          ? 9  
primary 'Phelps, J.'          ? 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    4  ?                           ? 
? ? 
4 non-polymer syn 'N-[4-(hydroxymethyl)-2-methylquinolin-8-yl]piperidine-4-carboxamide' 299.368   1  ?                           ? 
? ? 
5 water       nat water                                                                 18.015    94 ?                           ? 
? ? 
# 
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 'N-[4-(hydroxymethyl)-2-methylquinolin-8-yl]piperidine-4-carboxamide' A1BXM 
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 
A1BXM non-polymer         . 'N-[4-(hydroxymethyl)-2-methylquinolin-8-yl]piperidine-4-carboxamide' ? 'C17 H21 N3 O2'  299.368 
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 
# 
_pdbx_entity_instance_feature.ordinal        1 
_pdbx_entity_instance_feature.comp_id        A1BXM 
_pdbx_entity_instance_feature.asym_id        ? 
_pdbx_entity_instance_feature.seq_num        ? 
_pdbx_entity_instance_feature.auth_comp_id   A1BXM 
_pdbx_entity_instance_feature.auth_asym_id   ? 
_pdbx_entity_instance_feature.auth_seq_num   ? 
_pdbx_entity_instance_feature.feature_type   'SUBJECT OF INVESTIGATION' 
_pdbx_entity_instance_feature.details        ? 
# 
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  201 201 DMS   DMS B . 
D 3 DMS   1  202 202 DMS   DMS B . 
E 3 DMS   1  203 203 DMS   DMS B . 
F 4 A1BXM 1  204 301 A1BXM LIG B . 
G 3 DMS   1  205 302 DMS   DMS B . 
H 5 HOH   1  101 105 HOH   HOH A . 
H 5 HOH   2  102 48  HOH   HOH A . 
H 5 HOH   3  103 118 HOH   HOH A . 
H 5 HOH   4  104 98  HOH   HOH A . 
H 5 HOH   5  105 50  HOH   HOH A . 
H 5 HOH   6  106 20  HOH   HOH A . 
H 5 HOH   7  107 34  HOH   HOH A . 
H 5 HOH   8  108 103 HOH   HOH A . 
H 5 HOH   9  109 121 HOH   HOH A . 
H 5 HOH   10 110 85  HOH   HOH A . 
H 5 HOH   11 111 65  HOH   HOH A . 
H 5 HOH   12 112 28  HOH   HOH A . 
H 5 HOH   13 113 36  HOH   HOH A . 
H 5 HOH   14 114 49  HOH   HOH A . 
H 5 HOH   15 115 89  HOH   HOH A . 
H 5 HOH   16 116 120 HOH   HOH A . 
H 5 HOH   17 117 29  HOH   HOH A . 
H 5 HOH   18 118 110 HOH   HOH A . 
H 5 HOH   19 119 70  HOH   HOH A . 
H 5 HOH   20 120 27  HOH   HOH A . 
H 5 HOH   21 121 119 HOH   HOH A . 
H 5 HOH   22 122 40  HOH   HOH A . 
I 5 HOH   1  301 100 HOH   HOH B . 
I 5 HOH   2  302 58  HOH   HOH B . 
I 5 HOH   3  303 11  HOH   HOH B . 
I 5 HOH   4  304 51  HOH   HOH B . 
I 5 HOH   5  305 5   HOH   HOH B . 
I 5 HOH   6  306 90  HOH   HOH B . 
I 5 HOH   7  307 9   HOH   HOH B . 
I 5 HOH   8  308 1   HOH   HOH B . 
I 5 HOH   9  309 46  HOH   HOH B . 
I 5 HOH   10 310 106 HOH   HOH B . 
I 5 HOH   11 311 31  HOH   HOH B . 
I 5 HOH   12 312 125 HOH   HOH B . 
I 5 HOH   13 313 30  HOH   HOH B . 
I 5 HOH   14 314 14  HOH   HOH B . 
I 5 HOH   15 315 92  HOH   HOH B . 
I 5 HOH   16 316 13  HOH   HOH B . 
I 5 HOH   17 317 23  HOH   HOH B . 
I 5 HOH   18 318 68  HOH   HOH B . 
I 5 HOH   19 319 81  HOH   HOH B . 
I 5 HOH   20 320 63  HOH   HOH B . 
I 5 HOH   21 321 77  HOH   HOH B . 
I 5 HOH   22 322 126 HOH   HOH B . 
I 5 HOH   23 323 54  HOH   HOH B . 
I 5 HOH   24 324 16  HOH   HOH B . 
I 5 HOH   25 325 75  HOH   HOH B . 
I 5 HOH   26 326 123 HOH   HOH B . 
I 5 HOH   27 327 80  HOH   HOH B . 
I 5 HOH   28 328 39  HOH   HOH B . 
I 5 HOH   29 329 117 HOH   HOH B . 
I 5 HOH   30 330 62  HOH   HOH B . 
I 5 HOH   31 331 66  HOH   HOH B . 
I 5 HOH   32 332 108 HOH   HOH B . 
I 5 HOH   33 333 2   HOH   HOH B . 
I 5 HOH   34 334 32  HOH   HOH B . 
I 5 HOH   35 335 56  HOH   HOH B . 
I 5 HOH   36 336 4   HOH   HOH B . 
I 5 HOH   37 337 82  HOH   HOH B . 
I 5 HOH   38 338 60  HOH   HOH B . 
I 5 HOH   39 339 115 HOH   HOH B . 
I 5 HOH   40 340 35  HOH   HOH B . 
I 5 HOH   41 341 24  HOH   HOH B . 
I 5 HOH   42 342 43  HOH   HOH B . 
I 5 HOH   43 343 102 HOH   HOH B . 
I 5 HOH   44 344 64  HOH   HOH B . 
I 5 HOH   45 345 72  HOH   HOH B . 
I 5 HOH   46 346 3   HOH   HOH B . 
I 5 HOH   47 347 10  HOH   HOH B . 
I 5 HOH   48 348 67  HOH   HOH B . 
I 5 HOH   49 349 124 HOH   HOH B . 
I 5 HOH   50 350 17  HOH   HOH B . 
I 5 HOH   51 351 127 HOH   HOH B . 
I 5 HOH   52 352 73  HOH   HOH B . 
I 5 HOH   53 353 21  HOH   HOH B . 
I 5 HOH   54 354 107 HOH   HOH B . 
I 5 HOH   55 355 69  HOH   HOH B . 
I 5 HOH   56 356 42  HOH   HOH B . 
I 5 HOH   57 357 122 HOH   HOH B . 
I 5 HOH   58 358 12  HOH   HOH B . 
I 5 HOH   59 359 116 HOH   HOH B . 
I 5 HOH   60 360 18  HOH   HOH B . 
I 5 HOH   61 361 79  HOH   HOH B . 
I 5 HOH   62 362 87  HOH   HOH B . 
I 5 HOH   63 363 94  HOH   HOH B . 
I 5 HOH   64 364 59  HOH   HOH B . 
I 5 HOH   65 365 26  HOH   HOH B . 
I 5 HOH   66 366 112 HOH   HOH B . 
I 5 HOH   67 367 57  HOH   HOH B . 
I 5 HOH   68 368 61  HOH   HOH B . 
I 5 HOH   69 369 45  HOH   HOH B . 
I 5 HOH   70 370 83  HOH   HOH B . 
I 5 HOH   71 371 44  HOH   HOH B . 
I 5 HOH   72 372 109 HOH   HOH B . 
# 
loop_
_software.classification 
_software.name 
_software.version 
_software.citation_id 
_software.pdbx_ordinal 
_software.date 
_software.type 
_software.location 
_software.language 
refinement       REFMAC  5.8.0267 ? 1 ? ? ? ? 
refinement       BUSTER  .        ? 2 ? ? ? ? 
'data scaling'   Aimless .        ? 3 ? ? ? ? 
phasing          PHASER  .        ? 4 ? ? ? ? 
'data reduction' XDS     .        ? 5 ? ? ? ? 
# 
_cell.entry_id           7I1T 
_cell.length_a           42.600 
_cell.length_b           42.600 
_cell.length_c           217.460 
_cell.angle_alpha        90.00 
_cell.angle_beta         90.00 
_cell.angle_gamma        90.00 
_cell.Z_PDB              8 
_cell.pdbx_unique_axis   ? 
# 
_symmetry.entry_id                         7I1T 
_symmetry.space_group_name_H-M             'P 43 2 2' 
_symmetry.pdbx_full_space_group_name_H-M   ? 
_symmetry.cell_setting                     ? 
_symmetry.Int_Tables_number                95 
# 
_exptl.entry_id          7I1T 
_exptl.method            'X-RAY DIFFRACTION' 
_exptl.crystals_number   1 
# 
_exptl_crystal.id                    1 
_exptl_crystal.density_meas          ? 
_exptl_crystal.density_Matthews      2.13 
_exptl_crystal.density_percent_sol   42.19 
_exptl_crystal.description           ? 
_exptl_crystal.preparation           ? 
# 
_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.pdbx_serial_crystal_experiment   ? 
# 
_diffrn_detector.detector               PIXEL 
_diffrn_detector.type                   'DECTRIS EIGER2 XE 9M' 
_diffrn_detector.pdbx_collection_date   2023-10-10 
_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   0.92124 
_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        0.92124 
_diffrn_source.pdbx_synchrotron_site       Diamond 
_diffrn_source.pdbx_synchrotron_beamline   I04-1 
_diffrn_source.pdbx_wavelength             ? 
# 
_reflns.entry_id                     7I1T 
_reflns.pdbx_diffrn_id               1 
_reflns.pdbx_ordinal                 1 
_reflns.d_resolution_low             54.37 
_reflns.d_resolution_high            1.86 
_reflns.number_obs                   17933 
_reflns.percent_possible_obs         99.8 
_reflns.pdbx_Rmerge_I_obs            0.175 
_reflns.pdbx_netI_over_sigmaI        10.6 
_reflns.pdbx_redundancy              25.1 
_reflns.pdbx_Rrim_I_all              0.178 
_reflns.pdbx_Rpim_I_all              0.036 
_reflns.pdbx_CC_half                 0.998 
_reflns.pdbx_number_measured_all     450281 
_reflns.pdbx_chi_squared             1.00 
_reflns.observed_criterion_sigma_I   ? 
_reflns.observed_criterion_sigma_F   ? 
_reflns.number_all                   ? 
_reflns.pdbx_Rsym_value              ? 
_reflns.B_iso_Wilson_estimate        ? 
_reflns.pdbx_CC_star                 ? 
# 
_reflns_shell.pdbx_diffrn_id              1 
_reflns_shell.pdbx_ordinal                1 
_reflns_shell.d_res_high                  1.86 
_reflns_shell.d_res_low                   1.91 
_reflns_shell.number_measured_all         34361 
_reflns_shell.number_unique_obs           1274 
_reflns_shell.Rmerge_I_obs                ? 
_reflns_shell.pdbx_chi_squared            0.95 
_reflns_shell.pdbx_redundancy             27.0 
_reflns_shell.percent_possible_obs        99.4 
_reflns_shell.pdbx_netI_over_sigmaI_obs   0.4 
_reflns_shell.pdbx_Rrim_I_all             15.577 
_reflns_shell.pdbx_Rpim_I_all             2.938 
_reflns_shell.pdbx_CC_half                0.450 
_reflns_shell.percent_possible_all        ? 
_reflns_shell.pdbx_Rsym_value             ? 
_reflns_shell.meanI_over_sigI_obs         ? 
_reflns_shell.number_measured_obs         ? 
_reflns_shell.number_unique_all           ? 
_reflns_shell.pdbx_CC_star                ? 
# 
_refine.pdbx_refine_id                           'X-RAY DIFFRACTION' 
_refine.entry_id                                 7I1T 
_refine.pdbx_diffrn_id                           1 
_refine.pdbx_TLS_residual_ADP_flag               ? 
_refine.ls_number_reflns_obs                     16811 
_refine.ls_number_reflns_all                     ? 
_refine.pdbx_ls_sigma_I                          ? 
_refine.pdbx_ls_sigma_F                          ? 
_refine.pdbx_data_cutoff_high_absF               ? 
_refine.pdbx_data_cutoff_low_absF                ? 
_refine.pdbx_data_cutoff_high_rms_absF           ? 
_refine.ls_d_res_low                             54.37 
_refine.ls_d_res_high                            1.86 
_refine.ls_percent_reflns_obs                    98.63 
_refine.ls_R_factor_obs                          0.22370 
_refine.ls_R_factor_all                          ? 
_refine.ls_R_factor_R_work                       0.22048 
_refine.ls_R_factor_R_free                       0.28599 
_refine.ls_R_factor_R_free_error                 ? 
_refine.ls_R_factor_R_free_error_details         ? 
_refine.ls_percent_reflns_R_free                 4.9 
_refine.ls_number_reflns_R_free                  873 
_refine.ls_number_parameters                     ? 
_refine.ls_number_restraints                     ? 
_refine.occupancy_min                            ? 
_refine.occupancy_max                            ? 
_refine.correlation_coeff_Fo_to_Fc               0.971 
_refine.correlation_coeff_Fo_to_Fc_free          0.947 
_refine.B_iso_mean                               58.939 
_refine.aniso_B[1][1]                            2.70 
_refine.aniso_B[2][2]                            2.70 
_refine.aniso_B[3][3]                            -5.40 
_refine.aniso_B[1][2]                            -0.00 
_refine.aniso_B[1][3]                            -0.00 
_refine.aniso_B[2][3]                            0.00 
_refine.solvent_model_details                    MASK 
_refine.solvent_model_param_ksol                 ? 
_refine.solvent_model_param_bsol                 ? 
_refine.pdbx_solvent_vdw_probe_radii             1.20 
_refine.pdbx_solvent_ion_probe_radii             0.80 
_refine.pdbx_solvent_shrinkage_radii             0.80 
_refine.pdbx_ls_cross_valid_method               THROUGHOUT 
_refine.details                                  'HYDROGENS HAVE BEEN ADDED IN THE RIDING POSITIONS' 
_refine.pdbx_starting_model                      ? 
_refine.pdbx_method_to_determine_struct          'MOLECULAR REPLACEMENT' 
_refine.pdbx_isotropic_thermal_model             ? 
_refine.pdbx_stereochemistry_target_values       'MAXIMUM LIKELIHOOD' 
_refine.pdbx_stereochem_target_val_spec_case     ? 
_refine.pdbx_R_Free_selection_details            RANDOM 
_refine.pdbx_overall_ESU_R                       0.187 
_refine.pdbx_overall_ESU_R_Free                  0.181 
_refine.overall_SU_ML                            0.265 
_refine.pdbx_overall_phase_error                 ? 
_refine.overall_SU_B                             10.832 
_refine.overall_SU_R_Cruickshank_DPI             ? 
_refine.pdbx_overall_SU_R_free_Cruickshank_DPI   ? 
_refine.pdbx_overall_SU_R_Blow_DPI               ? 
_refine.pdbx_overall_SU_R_free_Blow_DPI          ? 
# 
_refine_hist.pdbx_refine_id                   'X-RAY DIFFRACTION' 
_refine_hist.cycle_id                         1 
_refine_hist.pdbx_number_atoms_protein        1476 
_refine_hist.pdbx_number_atoms_nucleic_acid   0 
_refine_hist.pdbx_number_atoms_ligand         38 
_refine_hist.number_atoms_solvent             94 
_refine_hist.number_atoms_total               1608 
_refine_hist.d_res_high                       1.86 
_refine_hist.d_res_low                        54.37 
# 
loop_
_refine_ls_restr.type 
_refine_ls_restr.dev_ideal 
_refine_ls_restr.dev_ideal_target 
_refine_ls_restr.weight 
_refine_ls_restr.number 
_refine_ls_restr.pdbx_refine_id 
_refine_ls_restr.pdbx_restraint_function 
r_bond_refined_d             0.008  0.013  ? 1976 'X-RAY DIFFRACTION' ? 
r_bond_other_d               0.001  0.015  ? 1642 'X-RAY DIFFRACTION' ? 
r_angle_refined_deg          1.538  1.636  ? 2443 'X-RAY DIFFRACTION' ? 
r_angle_other_deg            1.226  1.585  ? 3797 'X-RAY DIFFRACTION' ? 
r_dihedral_angle_1_deg       8.244  5.000  ? 235  'X-RAY DIFFRACTION' ? 
r_dihedral_angle_2_deg       32.433 22.771 ? 83   'X-RAY DIFFRACTION' ? 
r_dihedral_angle_3_deg       14.501 15.000 ? 274  'X-RAY DIFFRACTION' ? 
r_dihedral_angle_4_deg       14.925 15.000 ? 10   'X-RAY DIFFRACTION' ? 
r_chiral_restr               0.056  0.200  ? 218  'X-RAY DIFFRACTION' ? 
r_gen_planes_refined         0.007  0.020  ? 2104 'X-RAY DIFFRACTION' ? 
r_gen_planes_other           0.001  0.020  ? 402  'X-RAY DIFFRACTION' ? 
r_nbd_refined                ?      ?      ? ?    'X-RAY DIFFRACTION' ? 
r_nbd_other                  ?      ?      ? ?    'X-RAY DIFFRACTION' ? 
r_nbtor_refined              ?      ?      ? ?    'X-RAY DIFFRACTION' ? 
r_nbtor_other                ?      ?      ? ?    'X-RAY DIFFRACTION' ? 
r_xyhbond_nbd_refined        ?      ?      ? ?    'X-RAY DIFFRACTION' ? 
r_xyhbond_nbd_other          ?      ?      ? ?    'X-RAY DIFFRACTION' ? 
r_metal_ion_refined          ?      ?      ? ?    'X-RAY DIFFRACTION' ? 
r_metal_ion_other            ?      ?      ? ?    'X-RAY DIFFRACTION' ? 
r_symmetry_vdw_refined       ?      ?      ? ?    'X-RAY DIFFRACTION' ? 
r_symmetry_vdw_other         ?      ?      ? ?    'X-RAY DIFFRACTION' ? 
r_symmetry_hbond_refined     ?      ?      ? ?    'X-RAY DIFFRACTION' ? 
r_symmetry_hbond_other       ?      ?      ? ?    'X-RAY DIFFRACTION' ? 
r_symmetry_metal_ion_refined ?      ?      ? ?    'X-RAY DIFFRACTION' ? 
r_symmetry_metal_ion_other   ?      ?      ? ?    'X-RAY DIFFRACTION' ? 
r_mcbond_it                  4.345  5.950  ? 989  'X-RAY DIFFRACTION' ? 
r_mcbond_other               4.446  5.861  ? 938  'X-RAY DIFFRACTION' ? 
r_mcangle_it                 6.346  8.738  ? 1137 'X-RAY DIFFRACTION' ? 
r_mcangle_other              6.349  8.743  ? 1138 'X-RAY DIFFRACTION' ? 
r_scbond_it                  5.147  6.375  ? 987  'X-RAY DIFFRACTION' ? 
r_scbond_other               5.145  6.379  ? 988  'X-RAY DIFFRACTION' ? 
r_scangle_it                 ?      ?      ? ?    'X-RAY DIFFRACTION' ? 
r_scangle_other              7.683  9.260  ? 1307 'X-RAY DIFFRACTION' ? 
r_long_range_B_refined       10.741 66.221 ? 2043 'X-RAY DIFFRACTION' ? 
r_long_range_B_other         10.605 66.048 ? 2027 'X-RAY DIFFRACTION' ? 
r_rigid_bond_restr           ?      ?      ? ?    'X-RAY DIFFRACTION' ? 
r_sphericity_free            ?      ?      ? ?    'X-RAY DIFFRACTION' ? 
r_sphericity_bonded          ?      ?      ? ?    'X-RAY DIFFRACTION' ? 
# 
_refine_ls_shell.pdbx_refine_id                   'X-RAY DIFFRACTION' 
_refine_ls_shell.pdbx_total_number_of_bins_used   20 
_refine_ls_shell.d_res_high                       1.860 
_refine_ls_shell.d_res_low                        1.908 
_refine_ls_shell.number_reflns_R_work             1023 
_refine_ls_shell.R_factor_R_work                  0.523 
_refine_ls_shell.percent_reflns_obs               84.67 
_refine_ls_shell.R_factor_R_free                  0.486 
_refine_ls_shell.R_factor_R_free_error            ? 
_refine_ls_shell.percent_reflns_R_free            ? 
_refine_ls_shell.number_reflns_R_free             65 
_refine_ls_shell.number_reflns_all                ? 
_refine_ls_shell.R_factor_all                     ? 
_refine_ls_shell.R_factor_obs                     ? 
_refine_ls_shell.number_reflns_obs                ? 
# 
_struct.entry_id                  7I1T 
_struct.title                     
'PanDDA analysis group deposition -- Crystal Structure of ZIKV NS2B-NS3 protease in complex with MFP-0012466-002-003' 
_struct.pdbx_model_details        ? 
_struct.pdbx_CASP_flag            ? 
_struct.pdbx_model_type_details   ? 
# 
_struct_keywords.entry_id        7I1T 
_struct_keywords.pdbx_keywords   'VIRAL PROTEIN' 
_struct_keywords.text            'SGC - Diamond I04-1, PanDDA, XChemExplorer, 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 3 ? 
E N N 3 ? 
F N N 4 ? 
G N N 3 ? 
H N N 5 ? 
I 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 7I1T A 3 ? 46  ? Q32ZE1 1414 ? 1457 ? 46 89  
2 2 7I1T 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 7I1T SER A 1  ? UNP Q32ZE1 ?   ?    'expression tag'        44  1 
1 7I1T MET A 2  ? UNP Q32ZE1 ?   ?    'expression tag'        45  2 
2 7I1T MET B 1  ? UNP Q32ZE1 ?   ?    'initiating methionine' 10  3 
2 7I1T LYS B 98 ? UNP Q32ZE1 ARG 1605 conflict                107 4 
# 
_pdbx_struct_assembly.id                   1 
_pdbx_struct_assembly.details              author_defined_assembly 
_pdbx_struct_assembly.method_details       ? 
_pdbx_struct_assembly.oligomeric_details   dimeric 
_pdbx_struct_assembly.oligomeric_count     2 
# 
_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,G,H,I 
# 
_pdbx_struct_oper_list.id                   1 
_pdbx_struct_oper_list.type                 'identity operation' 
_pdbx_struct_oper_list.name                 1_555 
_pdbx_struct_oper_list.symmetry_operation   x,y,z 
_pdbx_struct_oper_list.matrix[1][1]         1.0000000000 
_pdbx_struct_oper_list.matrix[1][2]         0.0000000000 
_pdbx_struct_oper_list.matrix[1][3]         0.0000000000 
_pdbx_struct_oper_list.vector[1]            0.0000000000 
_pdbx_struct_oper_list.matrix[2][1]         0.0000000000 
_pdbx_struct_oper_list.matrix[2][2]         1.0000000000 
_pdbx_struct_oper_list.matrix[2][3]         0.0000000000 
_pdbx_struct_oper_list.vector[2]            0.0000000000 
_pdbx_struct_oper_list.matrix[3][1]         0.0000000000 
_pdbx_struct_oper_list.matrix[3][2]         0.0000000000 
_pdbx_struct_oper_list.matrix[3][3]         1.0000000000 
_pdbx_struct_oper_list.vector[3]            0.0000000000 
# 
loop_
_struct_conf.conf_type_id 
_struct_conf.id 
_struct_conf.pdbx_PDB_helix_id 
_struct_conf.beg_label_comp_id 
_struct_conf.beg_label_asym_id 
_struct_conf.beg_label_seq_id 
_struct_conf.pdbx_beg_PDB_ins_code 
_struct_conf.end_label_comp_id 
_struct_conf.end_label_asym_id 
_struct_conf.end_label_seq_id 
_struct_conf.pdbx_end_PDB_ins_code 
_struct_conf.beg_auth_comp_id 
_struct_conf.beg_auth_asym_id 
_struct_conf.beg_auth_seq_id 
_struct_conf.end_auth_comp_id 
_struct_conf.end_auth_asym_id 
_struct_conf.end_auth_seq_id 
_struct_conf.pdbx_PDB_helix_class 
_struct_conf.details 
_struct_conf.pdbx_PDB_helix_length 
HELX_P HELX_P1 AA1 MET B 40  ? LYS B 45  ? MET B 49  LYS B 54  1 ? 6 
HELX_P HELX_P2 AA2 PRO B 122 ? SER B 126 ? PRO B 131 SER B 135 5 ? 5 
# 
_struct_conf_type.id          HELX_P 
_struct_conf_type.criteria    ? 
_struct_conf_type.reference   ? 
# 
loop_
_struct_sheet.id 
_struct_sheet.type 
_struct_sheet.number_strands 
_struct_sheet.details 
AA1 ? 8 ? 
AA2 ? 6 ? 
AA3 ? 4 ? 
# 
loop_
_struct_sheet_order.sheet_id 
_struct_sheet_order.range_id_1 
_struct_sheet_order.range_id_2 
_struct_sheet_order.offset 
_struct_sheet_order.sense 
AA1 1 2 ? anti-parallel 
AA1 2 3 ? parallel      
AA1 3 4 ? anti-parallel 
AA1 4 5 ? anti-parallel 
AA1 5 6 ? anti-parallel 
AA1 6 7 ? anti-parallel 
AA1 7 8 ? anti-parallel 
AA2 1 2 ? anti-parallel 
AA2 2 3 ? parallel      
AA2 3 4 ? anti-parallel 
AA2 4 5 ? anti-parallel 
AA2 5 6 ? anti-parallel 
AA3 1 2 ? anti-parallel 
AA3 2 3 ? anti-parallel 
AA3 3 4 ? anti-parallel 
# 
loop_
_struct_sheet_range.sheet_id 
_struct_sheet_range.id 
_struct_sheet_range.beg_label_comp_id 
_struct_sheet_range.beg_label_asym_id 
_struct_sheet_range.beg_label_seq_id 
_struct_sheet_range.pdbx_beg_PDB_ins_code 
_struct_sheet_range.end_label_comp_id 
_struct_sheet_range.end_label_asym_id 
_struct_sheet_range.end_label_seq_id 
_struct_sheet_range.pdbx_end_PDB_ins_code 
_struct_sheet_range.beg_auth_comp_id 
_struct_sheet_range.beg_auth_asym_id 
_struct_sheet_range.beg_auth_seq_id 
_struct_sheet_range.end_auth_comp_id 
_struct_sheet_range.end_auth_asym_id 
_struct_sheet_range.end_auth_seq_id 
AA1 1 GLY B 54  ? LEU B 56  ? GLY B 63  LEU B 65  
AA1 2 LEU B 49  ? SER B 51  ? LEU B 58  SER B 60  
AA1 3 MET A 8   ? GLY A 14  ? MET A 51  GLY A 57  
AA1 4 GLY B 12  ? THR B 18  ? GLY B 21  THR B 27  
AA1 5 THR B 25  ? GLN B 33  ? THR B 34  GLN B 42  
AA1 6 VAL B 36  ? THR B 39  ? VAL B 45  THR B 48  
AA1 7 LEU B 67  ? TYR B 70  ? LEU B 76  TYR B 79  
AA1 8 PRO B 58  ? ASP B 62  ? PRO B 67  ASP B 71  
AA2 1 PHE A 41  ? LEU A 43  ? PHE A 84  LEU A 86  
AA2 2 ARG A 30  ? LEU A 35  ? ARG A 73  LEU A 78  
AA2 3 GLY B 105 ? THR B 109 ? GLY B 114 THR B 118 
AA2 4 GLY B 112 ? VAL B 117 ? GLY B 121 VAL B 126 
AA2 5 TYR B 152 ? ALA B 155 ? TYR B 161 ALA B 164 
AA2 6 GLY B 144 ? VAL B 146 ? GLY B 153 VAL B 155 
AA3 1 LYS B 98  ? THR B 102 ? LYS B 107 THR B 111 
AA3 2 VAL B 86  ? ALA B 90  ? VAL B 95  ALA B 99  
AA3 3 PRO B 129 ? LEU B 131 ? PRO B 138 LEU B 140 
AA3 4 VAL B 137 ? LEU B 140 ? VAL B 146 LEU B 149 
# 
loop_
_pdbx_struct_sheet_hbond.sheet_id 
_pdbx_struct_sheet_hbond.range_id_1 
_pdbx_struct_sheet_hbond.range_id_2 
_pdbx_struct_sheet_hbond.range_1_label_atom_id 
_pdbx_struct_sheet_hbond.range_1_label_comp_id 
_pdbx_struct_sheet_hbond.range_1_label_asym_id 
_pdbx_struct_sheet_hbond.range_1_label_seq_id 
_pdbx_struct_sheet_hbond.range_1_PDB_ins_code 
_pdbx_struct_sheet_hbond.range_1_auth_atom_id 
_pdbx_struct_sheet_hbond.range_1_auth_comp_id 
_pdbx_struct_sheet_hbond.range_1_auth_asym_id 
_pdbx_struct_sheet_hbond.range_1_auth_seq_id 
_pdbx_struct_sheet_hbond.range_2_label_atom_id 
_pdbx_struct_sheet_hbond.range_2_label_comp_id 
_pdbx_struct_sheet_hbond.range_2_label_asym_id 
_pdbx_struct_sheet_hbond.range_2_label_seq_id 
_pdbx_struct_sheet_hbond.range_2_PDB_ins_code 
_pdbx_struct_sheet_hbond.range_2_auth_atom_id 
_pdbx_struct_sheet_hbond.range_2_auth_comp_id 
_pdbx_struct_sheet_hbond.range_2_auth_asym_id 
_pdbx_struct_sheet_hbond.range_2_auth_seq_id 
AA1 1 2 O LEU B 56  ? O LEU B 65  N LEU B 49  ? N LEU B 58  
AA1 2 3 O ARG B 50  ? O ARG B 59  N MET A 8   ? N MET A 51  
AA1 3 4 N TYR A 9   ? N TYR A 52  O MET B 17  ? O MET B 26  
AA1 4 5 N VAL B 16  ? N VAL B 25  O GLY B 28  ? O GLY B 37  
AA1 5 6 N VAL B 31  ? N VAL B 40  O HIS B 38  ? O HIS B 47  
AA1 6 7 N THR B 39  ? N THR B 48  O VAL B 68  ? O VAL B 77  
AA1 7 8 O SER B 69  ? O SER B 78  N TRP B 60  ? N TRP B 69  
AA2 1 2 O SER A 42  ? O SER A 85  N ALA A 34  ? N ALA A 77  
AA2 2 3 N LEU A 31  ? N LEU A 74  O LYS B 108 ? O LYS B 117 
AA2 3 4 N PHE B 107 ? N PHE B 116 O ILE B 114 ? O ILE B 123 
AA2 4 5 N VAL B 117 ? N VAL B 126 O SER B 154 ? O SER B 163 
AA2 5 6 O VAL B 153 ? O VAL B 162 N VAL B 145 ? N VAL B 154 
AA3 1 2 O THR B 102 ? O THR B 111 N VAL B 86  ? N VAL B 95  
AA3 2 3 N GLN B 87  ? N GLN B 96  O LEU B 131 ? O LEU B 140 
AA3 3 4 N ILE B 130 ? N ILE B 139 O GLY B 139 ? O GLY B 148 
# 
_pdbx_entry_details.entry_id                   7I1T 
_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     Y 
_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 ASN A 70 ? ? -105.53 -162.63 
2 1 SER A 71 ? ? -141.19 60.00   
3 1 CYS B 80 ? ? 83.41   -8.75   
# 
loop_
_pdbx_struct_special_symmetry.id 
_pdbx_struct_special_symmetry.PDB_model_num 
_pdbx_struct_special_symmetry.auth_asym_id 
_pdbx_struct_special_symmetry.auth_comp_id 
_pdbx_struct_special_symmetry.auth_seq_id 
_pdbx_struct_special_symmetry.PDB_ins_code 
_pdbx_struct_special_symmetry.label_asym_id 
_pdbx_struct_special_symmetry.label_comp_id 
_pdbx_struct_special_symmetry.label_seq_id 
1 1 B HOH 328 ? I HOH . 
2 1 B HOH 371 ? I HOH . 
# 
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 
A1BXM N1   N Y N 1   
A1BXM N3   N N N 2   
A1BXM C4   C Y N 3   
A1BXM C5   C Y N 4   
A1BXM C6   C Y N 5   
A1BXM C7   C Y N 6   
A1BXM C8   C Y N 7   
A1BXM C10  C Y N 8   
A1BXM C13  C N N 9   
A1BXM C15  C N N 10  
A1BXM C17  C N N 11  
A1BXM C1   C N N 12  
A1BXM C2   C Y N 13  
A1BXM C3   C Y N 14  
A1BXM C9   C Y N 15  
A1BXM N2   N N N 16  
A1BXM C11  C N N 17  
A1BXM O1   O N N 18  
A1BXM C12  C N N 19  
A1BXM C14  C N N 20  
A1BXM C16  C N N 21  
A1BXM O2   O N N 22  
A1BXM H14  H N N 23  
A1BXM H5   H N N 24  
A1BXM H6   H N N 25  
A1BXM H7   H N N 26  
A1BXM H10  H N N 27  
A1BXM H11  H N N 28  
A1BXM H15  H N N 29  
A1BXM H16  H N N 30  
A1BXM H20  H N N 31  
A1BXM H19  H N N 32  
A1BXM H3   H N N 33  
A1BXM H1   H N N 34  
A1BXM H2   H N N 35  
A1BXM H4   H N N 36  
A1BXM H8   H N N 37  
A1BXM H9   H N N 38  
A1BXM H13  H N N 39  
A1BXM H12  H N N 40  
A1BXM H18  H N N 41  
A1BXM H17  H N N 42  
A1BXM H21  H N N 43  
ALA   N    N N N 44  
ALA   CA   C N S 45  
ALA   C    C N N 46  
ALA   O    O N N 47  
ALA   CB   C N N 48  
ALA   OXT  O N N 49  
ALA   H    H N N 50  
ALA   H2   H N N 51  
ALA   HA   H N N 52  
ALA   HB1  H N N 53  
ALA   HB2  H N N 54  
ALA   HB3  H N N 55  
ALA   HXT  H N N 56  
ARG   N    N N N 57  
ARG   CA   C N S 58  
ARG   C    C N N 59  
ARG   O    O N N 60  
ARG   CB   C N N 61  
ARG   CG   C N N 62  
ARG   CD   C N N 63  
ARG   NE   N N N 64  
ARG   CZ   C N N 65  
ARG   NH1  N N N 66  
ARG   NH2  N N N 67  
ARG   OXT  O N N 68  
ARG   H    H N N 69  
ARG   H2   H N N 70  
ARG   HA   H N N 71  
ARG   HB2  H N N 72  
ARG   HB3  H N N 73  
ARG   HG2  H N N 74  
ARG   HG3  H N N 75  
ARG   HD2  H N N 76  
ARG   HD3  H N N 77  
ARG   HE   H N N 78  
ARG   HH11 H N N 79  
ARG   HH12 H N N 80  
ARG   HH21 H N N 81  
ARG   HH22 H N N 82  
ARG   HXT  H N N 83  
ASN   N    N N N 84  
ASN   CA   C N S 85  
ASN   C    C N N 86  
ASN   O    O N N 87  
ASN   CB   C N N 88  
ASN   CG   C N N 89  
ASN   OD1  O N N 90  
ASN   ND2  N N N 91  
ASN   OXT  O N N 92  
ASN   H    H N N 93  
ASN   H2   H N N 94  
ASN   HA   H N N 95  
ASN   HB2  H N N 96  
ASN   HB3  H N N 97  
ASN   HD21 H N N 98  
ASN   HD22 H N N 99  
ASN   HXT  H N N 100 
ASP   N    N N N 101 
ASP   CA   C N S 102 
ASP   C    C N N 103 
ASP   O    O N N 104 
ASP   CB   C N N 105 
ASP   CG   C N N 106 
ASP   OD1  O N N 107 
ASP   OD2  O N N 108 
ASP   OXT  O N N 109 
ASP   H    H N N 110 
ASP   H2   H N N 111 
ASP   HA   H N N 112 
ASP   HB2  H N N 113 
ASP   HB3  H N N 114 
ASP   HD2  H N N 115 
ASP   HXT  H N N 116 
CYS   N    N N N 117 
CYS   CA   C N R 118 
CYS   C    C N N 119 
CYS   O    O N N 120 
CYS   CB   C N N 121 
CYS   SG   S N N 122 
CYS   OXT  O N N 123 
CYS   H    H N N 124 
CYS   H2   H N N 125 
CYS   HA   H N N 126 
CYS   HB2  H N N 127 
CYS   HB3  H N N 128 
CYS   HG   H N N 129 
CYS   HXT  H N N 130 
DMS   S    S N N 131 
DMS   O    O N N 132 
DMS   C1   C N N 133 
DMS   C2   C N N 134 
DMS   H11  H N N 135 
DMS   H12  H N N 136 
DMS   H13  H N N 137 
DMS   H21  H N N 138 
DMS   H22  H N N 139 
DMS   H23  H N N 140 
GLN   N    N N N 141 
GLN   CA   C N S 142 
GLN   C    C N N 143 
GLN   O    O N N 144 
GLN   CB   C N N 145 
GLN   CG   C N N 146 
GLN   CD   C N N 147 
GLN   OE1  O N N 148 
GLN   NE2  N N N 149 
GLN   OXT  O N N 150 
GLN   H    H N N 151 
GLN   H2   H N N 152 
GLN   HA   H N N 153 
GLN   HB2  H N N 154 
GLN   HB3  H N N 155 
GLN   HG2  H N N 156 
GLN   HG3  H N N 157 
GLN   HE21 H N N 158 
GLN   HE22 H N N 159 
GLN   HXT  H N N 160 
GLU   N    N N N 161 
GLU   CA   C N S 162 
GLU   C    C N N 163 
GLU   O    O N N 164 
GLU   CB   C N N 165 
GLU   CG   C N N 166 
GLU   CD   C N N 167 
GLU   OE1  O N N 168 
GLU   OE2  O N N 169 
GLU   OXT  O N N 170 
GLU   H    H N N 171 
GLU   H2   H N N 172 
GLU   HA   H N N 173 
GLU   HB2  H N N 174 
GLU   HB3  H N N 175 
GLU   HG2  H N N 176 
GLU   HG3  H N N 177 
GLU   HE2  H N N 178 
GLU   HXT  H N N 179 
GLY   N    N N N 180 
GLY   CA   C N N 181 
GLY   C    C N N 182 
GLY   O    O N N 183 
GLY   OXT  O N N 184 
GLY   H    H N N 185 
GLY   H2   H N N 186 
GLY   HA2  H N N 187 
GLY   HA3  H N N 188 
GLY   HXT  H N N 189 
HIS   N    N N N 190 
HIS   CA   C N S 191 
HIS   C    C N N 192 
HIS   O    O N N 193 
HIS   CB   C N N 194 
HIS   CG   C Y N 195 
HIS   ND1  N Y N 196 
HIS   CD2  C Y N 197 
HIS   CE1  C Y N 198 
HIS   NE2  N Y N 199 
HIS   OXT  O N N 200 
HIS   H    H N N 201 
HIS   H2   H N N 202 
HIS   HA   H N N 203 
HIS   HB2  H N N 204 
HIS   HB3  H N N 205 
HIS   HD1  H N N 206 
HIS   HD2  H N N 207 
HIS   HE1  H N N 208 
HIS   HE2  H N N 209 
HIS   HXT  H N N 210 
HOH   O    O N N 211 
HOH   H1   H N N 212 
HOH   H2   H N N 213 
ILE   N    N N N 214 
ILE   CA   C N S 215 
ILE   C    C N N 216 
ILE   O    O N N 217 
ILE   CB   C N S 218 
ILE   CG1  C N N 219 
ILE   CG2  C N N 220 
ILE   CD1  C N N 221 
ILE   OXT  O N N 222 
ILE   H    H N N 223 
ILE   H2   H N N 224 
ILE   HA   H N N 225 
ILE   HB   H N N 226 
ILE   HG12 H N N 227 
ILE   HG13 H N N 228 
ILE   HG21 H N N 229 
ILE   HG22 H N N 230 
ILE   HG23 H N N 231 
ILE   HD11 H N N 232 
ILE   HD12 H N N 233 
ILE   HD13 H N N 234 
ILE   HXT  H N N 235 
LEU   N    N N N 236 
LEU   CA   C N S 237 
LEU   C    C N N 238 
LEU   O    O N N 239 
LEU   CB   C N N 240 
LEU   CG   C N N 241 
LEU   CD1  C N N 242 
LEU   CD2  C N N 243 
LEU   OXT  O N N 244 
LEU   H    H N N 245 
LEU   H2   H N N 246 
LEU   HA   H N N 247 
LEU   HB2  H N N 248 
LEU   HB3  H N N 249 
LEU   HG   H N N 250 
LEU   HD11 H N N 251 
LEU   HD12 H N N 252 
LEU   HD13 H N N 253 
LEU   HD21 H N N 254 
LEU   HD22 H N N 255 
LEU   HD23 H N N 256 
LEU   HXT  H N N 257 
LYS   N    N N N 258 
LYS   CA   C N S 259 
LYS   C    C N N 260 
LYS   O    O N N 261 
LYS   CB   C N N 262 
LYS   CG   C N N 263 
LYS   CD   C N N 264 
LYS   CE   C N N 265 
LYS   NZ   N N N 266 
LYS   OXT  O N N 267 
LYS   H    H N N 268 
LYS   H2   H N N 269 
LYS   HA   H N N 270 
LYS   HB2  H N N 271 
LYS   HB3  H N N 272 
LYS   HG2  H N N 273 
LYS   HG3  H N N 274 
LYS   HD2  H N N 275 
LYS   HD3  H N N 276 
LYS   HE2  H N N 277 
LYS   HE3  H N N 278 
LYS   HZ1  H N N 279 
LYS   HZ2  H N N 280 
LYS   HZ3  H N N 281 
LYS   HXT  H N N 282 
MET   N    N N N 283 
MET   CA   C N S 284 
MET   C    C N N 285 
MET   O    O N N 286 
MET   CB   C N N 287 
MET   CG   C N N 288 
MET   SD   S N N 289 
MET   CE   C N N 290 
MET   OXT  O N N 291 
MET   H    H N N 292 
MET   H2   H N N 293 
MET   HA   H N N 294 
MET   HB2  H N N 295 
MET   HB3  H N N 296 
MET   HG2  H N N 297 
MET   HG3  H N N 298 
MET   HE1  H N N 299 
MET   HE2  H N N 300 
MET   HE3  H N N 301 
MET   HXT  H N N 302 
PHE   N    N N N 303 
PHE   CA   C N S 304 
PHE   C    C N N 305 
PHE   O    O N N 306 
PHE   CB   C N N 307 
PHE   CG   C Y N 308 
PHE   CD1  C Y N 309 
PHE   CD2  C Y N 310 
PHE   CE1  C Y N 311 
PHE   CE2  C Y N 312 
PHE   CZ   C Y N 313 
PHE   OXT  O N N 314 
PHE   H    H N N 315 
PHE   H2   H N N 316 
PHE   HA   H N N 317 
PHE   HB2  H N N 318 
PHE   HB3  H N N 319 
PHE   HD1  H N N 320 
PHE   HD2  H N N 321 
PHE   HE1  H N N 322 
PHE   HE2  H N N 323 
PHE   HZ   H N N 324 
PHE   HXT  H N N 325 
PRO   N    N N N 326 
PRO   CA   C N S 327 
PRO   C    C N N 328 
PRO   O    O N N 329 
PRO   CB   C N N 330 
PRO   CG   C N N 331 
PRO   CD   C N N 332 
PRO   OXT  O N N 333 
PRO   H    H N N 334 
PRO   HA   H N N 335 
PRO   HB2  H N N 336 
PRO   HB3  H N N 337 
PRO   HG2  H N N 338 
PRO   HG3  H N N 339 
PRO   HD2  H N N 340 
PRO   HD3  H N N 341 
PRO   HXT  H N N 342 
SER   N    N N N 343 
SER   CA   C N S 344 
SER   C    C N N 345 
SER   O    O N N 346 
SER   CB   C N N 347 
SER   OG   O N N 348 
SER   OXT  O N N 349 
SER   H    H N N 350 
SER   H2   H N N 351 
SER   HA   H N N 352 
SER   HB2  H N N 353 
SER   HB3  H N N 354 
SER   HG   H N N 355 
SER   HXT  H N N 356 
THR   N    N N N 357 
THR   CA   C N S 358 
THR   C    C N N 359 
THR   O    O N N 360 
THR   CB   C N R 361 
THR   OG1  O N N 362 
THR   CG2  C N N 363 
THR   OXT  O N N 364 
THR   H    H N N 365 
THR   H2   H N N 366 
THR   HA   H N N 367 
THR   HB   H N N 368 
THR   HG1  H N N 369 
THR   HG21 H N N 370 
THR   HG22 H N N 371 
THR   HG23 H N N 372 
THR   HXT  H N N 373 
TRP   N    N N N 374 
TRP   CA   C N S 375 
TRP   C    C N N 376 
TRP   O    O N N 377 
TRP   CB   C N N 378 
TRP   CG   C Y N 379 
TRP   CD1  C Y N 380 
TRP   CD2  C Y N 381 
TRP   NE1  N Y N 382 
TRP   CE2  C Y N 383 
TRP   CE3  C Y N 384 
TRP   CZ2  C Y N 385 
TRP   CZ3  C Y N 386 
TRP   CH2  C Y N 387 
TRP   OXT  O N N 388 
TRP   H    H N N 389 
TRP   H2   H N N 390 
TRP   HA   H N N 391 
TRP   HB2  H N N 392 
TRP   HB3  H N N 393 
TRP   HD1  H N N 394 
TRP   HE1  H N N 395 
TRP   HE3  H N N 396 
TRP   HZ2  H N N 397 
TRP   HZ3  H N N 398 
TRP   HH2  H N N 399 
TRP   HXT  H N N 400 
TYR   N    N N N 401 
TYR   CA   C N S 402 
TYR   C    C N N 403 
TYR   O    O N N 404 
TYR   CB   C N N 405 
TYR   CG   C Y N 406 
TYR   CD1  C Y N 407 
TYR   CD2  C Y N 408 
TYR   CE1  C Y N 409 
TYR   CE2  C Y N 410 
TYR   CZ   C Y N 411 
TYR   OH   O N N 412 
TYR   OXT  O N N 413 
TYR   H    H N N 414 
TYR   H2   H N N 415 
TYR   HA   H N N 416 
TYR   HB2  H N N 417 
TYR   HB3  H N N 418 
TYR   HD1  H N N 419 
TYR   HD2  H N N 420 
TYR   HE1  H N N 421 
TYR   HE2  H N N 422 
TYR   HH   H N N 423 
TYR   HXT  H N N 424 
VAL   N    N N N 425 
VAL   CA   C N S 426 
VAL   C    C N N 427 
VAL   O    O N N 428 
VAL   CB   C N N 429 
VAL   CG1  C N N 430 
VAL   CG2  C N N 431 
VAL   OXT  O N N 432 
VAL   H    H N N 433 
VAL   H2   H N N 434 
VAL   HA   H N N 435 
VAL   HB   H N N 436 
VAL   HG11 H N N 437 
VAL   HG12 H N N 438 
VAL   HG13 H N N 439 
VAL   HG21 H N N 440 
VAL   HG22 H N N 441 
VAL   HG23 H N N 442 
VAL   HXT  H N N 443 
# 
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 
A1BXM C1  C2   sing N N 1   
A1BXM C2  C3   doub Y N 2   
A1BXM C3  C4   sing Y N 3   
A1BXM C4  C5   doub Y N 4   
A1BXM C5  C6   sing Y N 5   
A1BXM C6  C7   doub Y N 6   
A1BXM C7  C8   sing Y N 7   
A1BXM C8  C9   doub Y N 8   
A1BXM C9  C10  sing Y N 9   
A1BXM C10 N1   doub Y N 10  
A1BXM C9  N2   sing N N 11  
A1BXM N2  C11  sing N N 12  
A1BXM C11 O1   doub N N 13  
A1BXM C11 C12  sing N N 14  
A1BXM C12 C13  sing N N 15  
A1BXM C13 C14  sing N N 16  
A1BXM C14 N3   sing N N 17  
A1BXM N3  C15  sing N N 18  
A1BXM C15 C16  sing N N 19  
A1BXM C4  C17  sing N N 20  
A1BXM C17 O2   sing N N 21  
A1BXM C2  N1   sing Y N 22  
A1BXM C12 C16  sing N N 23  
A1BXM C5  C10  sing Y N 24  
A1BXM N3  H14  sing N N 25  
A1BXM C6  H5   sing N N 26  
A1BXM C7  H6   sing N N 27  
A1BXM C8  H7   sing N N 28  
A1BXM C13 H10  sing N N 29  
A1BXM C13 H11  sing N N 30  
A1BXM C15 H15  sing N N 31  
A1BXM C15 H16  sing N N 32  
A1BXM C17 H20  sing N N 33  
A1BXM C17 H19  sing N N 34  
A1BXM C1  H3   sing N N 35  
A1BXM C1  H1   sing N N 36  
A1BXM C1  H2   sing N N 37  
A1BXM C3  H4   sing N N 38  
A1BXM N2  H8   sing N N 39  
A1BXM C12 H9   sing N N 40  
A1BXM C14 H13  sing N N 41  
A1BXM C14 H12  sing N N 42  
A1BXM C16 H18  sing N N 43  
A1BXM C16 H17  sing N N 44  
A1BXM O2  H21  sing N N 45  
ALA   N   CA   sing N N 46  
ALA   N   H    sing N N 47  
ALA   N   H2   sing N N 48  
ALA   CA  C    sing N N 49  
ALA   CA  CB   sing N N 50  
ALA   CA  HA   sing N N 51  
ALA   C   O    doub N N 52  
ALA   C   OXT  sing N N 53  
ALA   CB  HB1  sing N N 54  
ALA   CB  HB2  sing N N 55  
ALA   CB  HB3  sing N N 56  
ALA   OXT HXT  sing N N 57  
ARG   N   CA   sing N N 58  
ARG   N   H    sing N N 59  
ARG   N   H2   sing N N 60  
ARG   CA  C    sing N N 61  
ARG   CA  CB   sing N N 62  
ARG   CA  HA   sing N N 63  
ARG   C   O    doub N N 64  
ARG   C   OXT  sing N N 65  
ARG   CB  CG   sing N N 66  
ARG   CB  HB2  sing N N 67  
ARG   CB  HB3  sing N N 68  
ARG   CG  CD   sing N N 69  
ARG   CG  HG2  sing N N 70  
ARG   CG  HG3  sing N N 71  
ARG   CD  NE   sing N N 72  
ARG   CD  HD2  sing N N 73  
ARG   CD  HD3  sing N N 74  
ARG   NE  CZ   sing N N 75  
ARG   NE  HE   sing N N 76  
ARG   CZ  NH1  sing N N 77  
ARG   CZ  NH2  doub N N 78  
ARG   NH1 HH11 sing N N 79  
ARG   NH1 HH12 sing N N 80  
ARG   NH2 HH21 sing N N 81  
ARG   NH2 HH22 sing N N 82  
ARG   OXT HXT  sing N N 83  
ASN   N   CA   sing N N 84  
ASN   N   H    sing N N 85  
ASN   N   H2   sing N N 86  
ASN   CA  C    sing N N 87  
ASN   CA  CB   sing N N 88  
ASN   CA  HA   sing N N 89  
ASN   C   O    doub N N 90  
ASN   C   OXT  sing N N 91  
ASN   CB  CG   sing N N 92  
ASN   CB  HB2  sing N N 93  
ASN   CB  HB3  sing N N 94  
ASN   CG  OD1  doub N N 95  
ASN   CG  ND2  sing N N 96  
ASN   ND2 HD21 sing N N 97  
ASN   ND2 HD22 sing N N 98  
ASN   OXT HXT  sing N N 99  
ASP   N   CA   sing N N 100 
ASP   N   H    sing N N 101 
ASP   N   H2   sing N N 102 
ASP   CA  C    sing N N 103 
ASP   CA  CB   sing N N 104 
ASP   CA  HA   sing N N 105 
ASP   C   O    doub N N 106 
ASP   C   OXT  sing N N 107 
ASP   CB  CG   sing N N 108 
ASP   CB  HB2  sing N N 109 
ASP   CB  HB3  sing N N 110 
ASP   CG  OD1  doub N N 111 
ASP   CG  OD2  sing N N 112 
ASP   OD2 HD2  sing N N 113 
ASP   OXT HXT  sing N N 114 
CYS   N   CA   sing N N 115 
CYS   N   H    sing N N 116 
CYS   N   H2   sing N N 117 
CYS   CA  C    sing N N 118 
CYS   CA  CB   sing N N 119 
CYS   CA  HA   sing N N 120 
CYS   C   O    doub N N 121 
CYS   C   OXT  sing N N 122 
CYS   CB  SG   sing N N 123 
CYS   CB  HB2  sing N N 124 
CYS   CB  HB3  sing N N 125 
CYS   SG  HG   sing N N 126 
CYS   OXT HXT  sing N N 127 
DMS   S   O    doub N N 128 
DMS   S   C1   sing N N 129 
DMS   S   C2   sing N N 130 
DMS   C1  H11  sing N N 131 
DMS   C1  H12  sing N N 132 
DMS   C1  H13  sing N N 133 
DMS   C2  H21  sing N N 134 
DMS   C2  H22  sing N N 135 
DMS   C2  H23  sing N N 136 
GLN   N   CA   sing N N 137 
GLN   N   H    sing N N 138 
GLN   N   H2   sing N N 139 
GLN   CA  C    sing N N 140 
GLN   CA  CB   sing N N 141 
GLN   CA  HA   sing N N 142 
GLN   C   O    doub N N 143 
GLN   C   OXT  sing N N 144 
GLN   CB  CG   sing N N 145 
GLN   CB  HB2  sing N N 146 
GLN   CB  HB3  sing N N 147 
GLN   CG  CD   sing N N 148 
GLN   CG  HG2  sing N N 149 
GLN   CG  HG3  sing N N 150 
GLN   CD  OE1  doub N N 151 
GLN   CD  NE2  sing N N 152 
GLN   NE2 HE21 sing N N 153 
GLN   NE2 HE22 sing N N 154 
GLN   OXT HXT  sing N N 155 
GLU   N   CA   sing N N 156 
GLU   N   H    sing N N 157 
GLU   N   H2   sing N N 158 
GLU   CA  C    sing N N 159 
GLU   CA  CB   sing N N 160 
GLU   CA  HA   sing N N 161 
GLU   C   O    doub N N 162 
GLU   C   OXT  sing N N 163 
GLU   CB  CG   sing N N 164 
GLU   CB  HB2  sing N N 165 
GLU   CB  HB3  sing N N 166 
GLU   CG  CD   sing N N 167 
GLU   CG  HG2  sing N N 168 
GLU   CG  HG3  sing N N 169 
GLU   CD  OE1  doub N N 170 
GLU   CD  OE2  sing N N 171 
GLU   OE2 HE2  sing N N 172 
GLU   OXT HXT  sing N N 173 
GLY   N   CA   sing N N 174 
GLY   N   H    sing N N 175 
GLY   N   H2   sing N N 176 
GLY   CA  C    sing N N 177 
GLY   CA  HA2  sing N N 178 
GLY   CA  HA3  sing N N 179 
GLY   C   O    doub N N 180 
GLY   C   OXT  sing N N 181 
GLY   OXT HXT  sing N N 182 
HIS   N   CA   sing N N 183 
HIS   N   H    sing N N 184 
HIS   N   H2   sing N N 185 
HIS   CA  C    sing N N 186 
HIS   CA  CB   sing N N 187 
HIS   CA  HA   sing N N 188 
HIS   C   O    doub N N 189 
HIS   C   OXT  sing N N 190 
HIS   CB  CG   sing N N 191 
HIS   CB  HB2  sing N N 192 
HIS   CB  HB3  sing N N 193 
HIS   CG  ND1  sing Y N 194 
HIS   CG  CD2  doub Y N 195 
HIS   ND1 CE1  doub Y N 196 
HIS   ND1 HD1  sing N N 197 
HIS   CD2 NE2  sing Y N 198 
HIS   CD2 HD2  sing N N 199 
HIS   CE1 NE2  sing Y N 200 
HIS   CE1 HE1  sing N N 201 
HIS   NE2 HE2  sing N N 202 
HIS   OXT HXT  sing N N 203 
HOH   O   H1   sing N N 204 
HOH   O   H2   sing N N 205 
ILE   N   CA   sing N N 206 
ILE   N   H    sing N N 207 
ILE   N   H2   sing N N 208 
ILE   CA  C    sing N N 209 
ILE   CA  CB   sing N N 210 
ILE   CA  HA   sing N N 211 
ILE   C   O    doub N N 212 
ILE   C   OXT  sing N N 213 
ILE   CB  CG1  sing N N 214 
ILE   CB  CG2  sing N N 215 
ILE   CB  HB   sing N N 216 
ILE   CG1 CD1  sing N N 217 
ILE   CG1 HG12 sing N N 218 
ILE   CG1 HG13 sing N N 219 
ILE   CG2 HG21 sing N N 220 
ILE   CG2 HG22 sing N N 221 
ILE   CG2 HG23 sing N N 222 
ILE   CD1 HD11 sing N N 223 
ILE   CD1 HD12 sing N N 224 
ILE   CD1 HD13 sing N N 225 
ILE   OXT HXT  sing N N 226 
LEU   N   CA   sing N N 227 
LEU   N   H    sing N N 228 
LEU   N   H2   sing N N 229 
LEU   CA  C    sing N N 230 
LEU   CA  CB   sing N N 231 
LEU   CA  HA   sing N N 232 
LEU   C   O    doub N N 233 
LEU   C   OXT  sing N N 234 
LEU   CB  CG   sing N N 235 
LEU   CB  HB2  sing N N 236 
LEU   CB  HB3  sing N N 237 
LEU   CG  CD1  sing N N 238 
LEU   CG  CD2  sing N N 239 
LEU   CG  HG   sing N N 240 
LEU   CD1 HD11 sing N N 241 
LEU   CD1 HD12 sing N N 242 
LEU   CD1 HD13 sing N N 243 
LEU   CD2 HD21 sing N N 244 
LEU   CD2 HD22 sing N N 245 
LEU   CD2 HD23 sing N N 246 
LEU   OXT HXT  sing N N 247 
LYS   N   CA   sing N N 248 
LYS   N   H    sing N N 249 
LYS   N   H2   sing N N 250 
LYS   CA  C    sing N N 251 
LYS   CA  CB   sing N N 252 
LYS   CA  HA   sing N N 253 
LYS   C   O    doub N N 254 
LYS   C   OXT  sing N N 255 
LYS   CB  CG   sing N N 256 
LYS   CB  HB2  sing N N 257 
LYS   CB  HB3  sing N N 258 
LYS   CG  CD   sing N N 259 
LYS   CG  HG2  sing N N 260 
LYS   CG  HG3  sing N N 261 
LYS   CD  CE   sing N N 262 
LYS   CD  HD2  sing N N 263 
LYS   CD  HD3  sing N N 264 
LYS   CE  NZ   sing N N 265 
LYS   CE  HE2  sing N N 266 
LYS   CE  HE3  sing N N 267 
LYS   NZ  HZ1  sing N N 268 
LYS   NZ  HZ2  sing N N 269 
LYS   NZ  HZ3  sing N N 270 
LYS   OXT HXT  sing N N 271 
MET   N   CA   sing N N 272 
MET   N   H    sing N N 273 
MET   N   H2   sing N N 274 
MET   CA  C    sing N N 275 
MET   CA  CB   sing N N 276 
MET   CA  HA   sing N N 277 
MET   C   O    doub N N 278 
MET   C   OXT  sing N N 279 
MET   CB  CG   sing N N 280 
MET   CB  HB2  sing N N 281 
MET   CB  HB3  sing N N 282 
MET   CG  SD   sing N N 283 
MET   CG  HG2  sing N N 284 
MET   CG  HG3  sing N N 285 
MET   SD  CE   sing N N 286 
MET   CE  HE1  sing N N 287 
MET   CE  HE2  sing N N 288 
MET   CE  HE3  sing N N 289 
MET   OXT HXT  sing N N 290 
PHE   N   CA   sing N N 291 
PHE   N   H    sing N N 292 
PHE   N   H2   sing N N 293 
PHE   CA  C    sing N N 294 
PHE   CA  CB   sing N N 295 
PHE   CA  HA   sing N N 296 
PHE   C   O    doub N N 297 
PHE   C   OXT  sing N N 298 
PHE   CB  CG   sing N N 299 
PHE   CB  HB2  sing N N 300 
PHE   CB  HB3  sing N N 301 
PHE   CG  CD1  doub Y N 302 
PHE   CG  CD2  sing Y N 303 
PHE   CD1 CE1  sing Y N 304 
PHE   CD1 HD1  sing N N 305 
PHE   CD2 CE2  doub Y N 306 
PHE   CD2 HD2  sing N N 307 
PHE   CE1 CZ   doub Y N 308 
PHE   CE1 HE1  sing N N 309 
PHE   CE2 CZ   sing Y N 310 
PHE   CE2 HE2  sing N N 311 
PHE   CZ  HZ   sing N N 312 
PHE   OXT HXT  sing N N 313 
PRO   N   CA   sing N N 314 
PRO   N   CD   sing N N 315 
PRO   N   H    sing N N 316 
PRO   CA  C    sing N N 317 
PRO   CA  CB   sing N N 318 
PRO   CA  HA   sing N N 319 
PRO   C   O    doub N N 320 
PRO   C   OXT  sing N N 321 
PRO   CB  CG   sing N N 322 
PRO   CB  HB2  sing N N 323 
PRO   CB  HB3  sing N N 324 
PRO   CG  CD   sing N N 325 
PRO   CG  HG2  sing N N 326 
PRO   CG  HG3  sing N N 327 
PRO   CD  HD2  sing N N 328 
PRO   CD  HD3  sing N N 329 
PRO   OXT HXT  sing N N 330 
SER   N   CA   sing N N 331 
SER   N   H    sing N N 332 
SER   N   H2   sing N N 333 
SER   CA  C    sing N N 334 
SER   CA  CB   sing N N 335 
SER   CA  HA   sing N N 336 
SER   C   O    doub N N 337 
SER   C   OXT  sing N N 338 
SER   CB  OG   sing N N 339 
SER   CB  HB2  sing N N 340 
SER   CB  HB3  sing N N 341 
SER   OG  HG   sing N N 342 
SER   OXT HXT  sing N N 343 
THR   N   CA   sing N N 344 
THR   N   H    sing N N 345 
THR   N   H2   sing N N 346 
THR   CA  C    sing N N 347 
THR   CA  CB   sing N N 348 
THR   CA  HA   sing N N 349 
THR   C   O    doub N N 350 
THR   C   OXT  sing N N 351 
THR   CB  OG1  sing N N 352 
THR   CB  CG2  sing N N 353 
THR   CB  HB   sing N N 354 
THR   OG1 HG1  sing N N 355 
THR   CG2 HG21 sing N N 356 
THR   CG2 HG22 sing N N 357 
THR   CG2 HG23 sing N N 358 
THR   OXT HXT  sing N N 359 
TRP   N   CA   sing N N 360 
TRP   N   H    sing N N 361 
TRP   N   H2   sing N N 362 
TRP   CA  C    sing N N 363 
TRP   CA  CB   sing N N 364 
TRP   CA  HA   sing N N 365 
TRP   C   O    doub N N 366 
TRP   C   OXT  sing N N 367 
TRP   CB  CG   sing N N 368 
TRP   CB  HB2  sing N N 369 
TRP   CB  HB3  sing N N 370 
TRP   CG  CD1  doub Y N 371 
TRP   CG  CD2  sing Y N 372 
TRP   CD1 NE1  sing Y N 373 
TRP   CD1 HD1  sing N N 374 
TRP   CD2 CE2  doub Y N 375 
TRP   CD2 CE3  sing Y N 376 
TRP   NE1 CE2  sing Y N 377 
TRP   NE1 HE1  sing N N 378 
TRP   CE2 CZ2  sing Y N 379 
TRP   CE3 CZ3  doub Y N 380 
TRP   CE3 HE3  sing N N 381 
TRP   CZ2 CH2  doub Y N 382 
TRP   CZ2 HZ2  sing N N 383 
TRP   CZ3 CH2  sing Y N 384 
TRP   CZ3 HZ3  sing N N 385 
TRP   CH2 HH2  sing N N 386 
TRP   OXT HXT  sing N N 387 
TYR   N   CA   sing N N 388 
TYR   N   H    sing N N 389 
TYR   N   H2   sing N N 390 
TYR   CA  C    sing N N 391 
TYR   CA  CB   sing N N 392 
TYR   CA  HA   sing N N 393 
TYR   C   O    doub N N 394 
TYR   C   OXT  sing N N 395 
TYR   CB  CG   sing N N 396 
TYR   CB  HB2  sing N N 397 
TYR   CB  HB3  sing N N 398 
TYR   CG  CD1  doub Y N 399 
TYR   CG  CD2  sing Y N 400 
TYR   CD1 CE1  sing Y N 401 
TYR   CD1 HD1  sing N N 402 
TYR   CD2 CE2  doub Y N 403 
TYR   CD2 HD2  sing N N 404 
TYR   CE1 CZ   doub Y N 405 
TYR   CE1 HE1  sing N N 406 
TYR   CE2 CZ   sing Y N 407 
TYR   CE2 HE2  sing N N 408 
TYR   CZ  OH   sing N N 409 
TYR   OH  HH   sing N N 410 
TYR   OXT HXT  sing N N 411 
VAL   N   CA   sing N N 412 
VAL   N   H    sing N N 413 
VAL   N   H2   sing N N 414 
VAL   CA  C    sing N N 415 
VAL   CA  CB   sing N N 416 
VAL   CA  HA   sing N N 417 
VAL   C   O    doub N N 418 
VAL   C   OXT  sing N N 419 
VAL   CB  CG1  sing N N 420 
VAL   CB  CG2  sing N N 421 
VAL   CB  HB   sing N N 422 
VAL   CG1 HG11 sing N N 423 
VAL   CG1 HG12 sing N N 424 
VAL   CG1 HG13 sing N N 425 
VAL   CG2 HG21 sing N N 426 
VAL   CG2 HG22 sing N N 427 
VAL   CG2 HG23 sing N N 428 
VAL   OXT HXT  sing N N 429 
# 
_pdbx_audit_support.funding_organization   'Australian Research Council (ARC)' 
_pdbx_audit_support.country                Australia 
_pdbx_audit_support.grant_number           IC180100021 
_pdbx_audit_support.ordinal                1 
# 
_pdbx_deposit_group.group_id            G_1002340 
_pdbx_deposit_group.group_description   
'Crystallographic fragment screen of ZIKV NS2B-NS3 protease at the XChem facility of Diamond Light Source beamline I04-1' 
_pdbx_deposit_group.group_title         'PanDDA analysis group deposition' 
_pdbx_deposit_group.group_type          'changed state' 
# 
_pdbx_initial_refinement_model.accession_code   8PN6 
_pdbx_initial_refinement_model.details          ? 
_pdbx_initial_refinement_model.entity_id_list   ? 
_pdbx_initial_refinement_model.id               1 
_pdbx_initial_refinement_model.source_name      PDB 
_pdbx_initial_refinement_model.type             'experimental model' 
# 
_atom_sites.entry_id                    7I1T 
_atom_sites.fract_transf_matrix[1][1]   0.023474 
_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]   0.023474 
_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]   0.004599 
_atom_sites.fract_transf_vector[1]      0.00000 
_atom_sites.fract_transf_vector[2]      0.00000 
_atom_sites.fract_transf_vector[3]      0.00000 
# 
loop_
_atom_type.symbol 
C 
N 
O 
S 
# 
loop_
_atom_site.group_PDB 
_atom_site.id 
_atom_site.type_symbol 
_atom_site.label_atom_id 
_atom_site.label_alt_id 
_atom_site.label_comp_id 
_atom_site.label_asym_id 
_atom_site.label_entity_id 
_atom_site.label_seq_id 
_atom_site.pdbx_PDB_ins_code 
_atom_site.Cartn_x 
_atom_site.Cartn_y 
_atom_site.Cartn_z 
_atom_site.occupancy 
_atom_site.B_iso_or_equiv 
_atom_site.pdbx_formal_charge 
_atom_site.auth_seq_id 
_atom_site.auth_comp_id 
_atom_site.auth_asym_id 
_atom_site.auth_atom_id 
_atom_site.pdbx_PDB_model_num 
ATOM   1    N N   . ASP   A 1 7   ? -21.242 19.669  -7.453  1.00 78.56  ? 50  ASP   A N   1 
ATOM   2    C CA  . ASP   A 1 7   ? -22.513 18.865  -7.482  1.00 80.66  ? 50  ASP   A CA  1 
ATOM   3    C C   . ASP   A 1 7   ? -22.705 18.231  -8.870  1.00 79.05  ? 50  ASP   A C   1 
ATOM   4    O O   . ASP   A 1 7   ? -22.712 18.965  -9.882  1.00 73.49  ? 50  ASP   A O   1 
ATOM   5    C CB  . ASP   A 1 7   ? -23.728 19.701  -7.077  1.00 77.54  ? 50  ASP   A CB  1 
ATOM   6    C CG  . ASP   A 1 7   ? -24.913 18.839  -6.689  1.00 85.64  ? 50  ASP   A CG  1 
ATOM   7    O OD1 . ASP   A 1 7   ? -25.232 18.772  -5.488  1.00 91.88  ? 50  ASP   A OD1 1 
ATOM   8    O OD2 . ASP   A 1 7   ? -25.486 18.223  -7.588  1.00 95.37  ? 50  ASP   A OD2 1 
ATOM   9    N N   . MET   A 1 8   ? -22.886 16.907  -8.899  1.00 64.65  ? 51  MET   A N   1 
ATOM   10   C CA  . MET   A 1 8   ? -22.806 16.075  -10.127 1.00 60.75  ? 51  MET   A CA  1 
ATOM   11   C C   . MET   A 1 8   ? -24.202 15.780  -10.660 1.00 48.60  ? 51  MET   A C   1 
ATOM   12   O O   . MET   A 1 8   ? -25.108 15.513  -9.838  1.00 55.69  ? 51  MET   A O   1 
ATOM   13   C CB  . MET   A 1 8   ? -22.108 14.744  -9.835  1.00 52.98  ? 51  MET   A CB  1 
ATOM   14   C CG  . MET   A 1 8   ? -20.695 14.922  -9.460  1.00 55.88  ? 51  MET   A CG  1 
ATOM   15   S SD  . MET   A 1 8   ? -19.922 13.314  -9.195  1.00 65.25  ? 51  MET   A SD  1 
ATOM   16   C CE  . MET   A 1 8   ? -18.226 13.872  -9.095  1.00 56.56  ? 51  MET   A CE  1 
ATOM   17   N N   . TYR   A 1 9   ? -24.353 15.728  -11.981 1.00 41.63  ? 52  TYR   A N   1 
ATOM   18   C CA  . TYR   A 1 9   ? -25.685 15.527  -12.611 1.00 49.67  ? 52  TYR   A CA  1 
ATOM   19   C C   . TYR   A 1 9   ? -25.530 14.547  -13.773 1.00 48.73  ? 52  TYR   A C   1 
ATOM   20   O O   . TYR   A 1 9   ? -24.417 14.411  -14.288 1.00 51.34  ? 52  TYR   A O   1 
ATOM   21   C CB  . TYR   A 1 9   ? -26.318 16.881  -13.008 1.00 46.63  ? 52  TYR   A CB  1 
ATOM   22   C CG  . TYR   A 1 9   ? -25.563 17.685  -14.039 1.00 42.86  ? 52  TYR   A CG  1 
ATOM   23   C CD1 . TYR   A 1 9   ? -24.541 18.560  -13.669 1.00 47.72  ? 52  TYR   A CD1 1 
ATOM   24   C CD2 . TYR   A 1 9   ? -25.866 17.583  -15.387 1.00 47.54  ? 52  TYR   A CD2 1 
ATOM   25   C CE1 . TYR   A 1 9   ? -23.829 19.286  -14.617 1.00 49.21  ? 52  TYR   A CE1 1 
ATOM   26   C CE2 . TYR   A 1 9   ? -25.163 18.307  -16.350 1.00 48.85  ? 52  TYR   A CE2 1 
ATOM   27   C CZ  . TYR   A 1 9   ? -24.141 19.159  -15.967 1.00 54.45  ? 52  TYR   A CZ  1 
ATOM   28   O OH  . TYR   A 1 9   ? -23.436 19.834  -16.936 1.00 61.25  ? 52  TYR   A OH  1 
ATOM   29   N N   . ILE   A 1 10  ? -26.620 13.886  -14.163 1.00 53.69  ? 53  ILE   A N   1 
ATOM   30   C CA  . ILE   A 1 10  ? -26.578 12.856  -15.246 1.00 55.02  ? 53  ILE   A CA  1 
ATOM   31   C C   . ILE   A 1 10  ? -27.464 13.248  -16.446 1.00 53.55  ? 53  ILE   A C   1 
ATOM   32   O O   . ILE   A 1 10  ? -28.589 13.773  -16.242 1.00 54.58  ? 53  ILE   A O   1 
ATOM   33   C CB  . ILE   A 1 10  ? -26.953 11.483  -14.671 1.00 49.91  ? 53  ILE   A CB  1 
ATOM   34   C CG1 . ILE   A 1 10  ? -28.428 11.408  -14.284 1.00 51.92  ? 53  ILE   A CG1 1 
ATOM   35   C CG2 . ILE   A 1 10  ? -26.054 11.146  -13.497 1.00 52.93  ? 53  ILE   A CG2 1 
ATOM   36   C CD1 . ILE   A 1 10  ? -28.845 10.069  -13.756 1.00 52.14  ? 53  ILE   A CD1 1 
ATOM   37   N N   . GLU   A 1 11  ? -26.979 12.936  -17.650 1.00 53.01  ? 54  GLU   A N   1 
ATOM   38   C CA  . GLU   A 1 11  ? -27.619 13.225  -18.964 1.00 55.31  ? 54  GLU   A CA  1 
ATOM   39   C C   . GLU   A 1 11  ? -27.688 11.928  -19.772 1.00 57.35  ? 54  GLU   A C   1 
ATOM   40   O O   . GLU   A 1 11  ? -26.639 11.288  -19.950 1.00 48.02  ? 54  GLU   A O   1 
ATOM   41   C CB  . GLU   A 1 11  ? -26.792 14.206  -19.805 1.00 58.43  ? 54  GLU   A CB  1 
ATOM   42   C CG  . GLU   A 1 11  ? -26.375 15.480  -19.091 1.00 66.80  ? 54  GLU   A CG  1 
ATOM   43   C CD  . GLU   A 1 11  ? -25.723 16.545  -19.970 1.00 73.89  ? 54  GLU   A CD  1 
ATOM   44   O OE1 . GLU   A 1 11  ? -25.026 16.175  -20.943 1.00 72.12  ? 54  GLU   A OE1 1 
ATOM   45   O OE2 . GLU   A 1 11  ? -25.900 17.760  -19.675 1.00 84.24  ? 54  GLU   A OE2 1 
ATOM   46   N N   . ARG   A 1 12  ? -28.860 11.556  -20.269 1.00 48.78  ? 55  ARG   A N   1 
ATOM   47   C CA  . ARG   A 1 12  ? -28.979 10.336  -21.104 1.00 60.44  ? 55  ARG   A CA  1 
ATOM   48   C C   . ARG   A 1 12  ? -28.024 10.445  -22.297 1.00 58.23  ? 55  ARG   A C   1 
ATOM   49   O O   . ARG   A 1 12  ? -27.869 11.558  -22.809 1.00 60.57  ? 55  ARG   A O   1 
ATOM   50   C CB  . ARG   A 1 12  ? -30.417 10.151  -21.575 1.00 55.33  ? 55  ARG   A CB  1 
ATOM   51   C CG  . ARG   A 1 12  ? -30.660 8.782   -22.182 1.00 58.56  ? 55  ARG   A CG  1 
ATOM   52   C CD  . ARG   A 1 12  ? -32.087 8.369   -21.965 1.00 61.89  ? 55  ARG   A CD  1 
ATOM   53   N NE  . ARG   A 1 12  ? -32.305 6.948   -22.081 1.00 65.48  ? 55  ARG   A NE  1 
ATOM   54   C CZ  . ARG   A 1 12  ? -32.280 6.296   -23.226 1.00 72.57  ? 55  ARG   A CZ  1 
ATOM   55   N NH1 . ARG   A 1 12  ? -31.987 6.930   -24.350 1.00 75.45  ? 55  ARG   A NH1 1 
ATOM   56   N NH2 . ARG   A 1 12  ? -32.524 4.998   -23.236 1.00 74.71  ? 55  ARG   A NH2 1 
ATOM   57   N N   . ALA   A 1 13  ? -27.385 9.345   -22.706 1.00 57.12  ? 56  ALA   A N   1 
ATOM   58   C CA  . ALA   A 1 13  ? -26.430 9.328   -23.843 1.00 51.52  ? 56  ALA   A CA  1 
ATOM   59   C C   . ALA   A 1 13  ? -26.791 8.284   -24.916 1.00 52.10  ? 56  ALA   A C   1 
ATOM   60   O O   . ALA   A 1 13  ? -26.232 8.363   -26.037 1.00 53.03  ? 56  ALA   A O   1 
ATOM   61   C CB  . ALA   A 1 13  ? -25.026 9.147   -23.347 1.00 57.92  ? 56  ALA   A CB  1 
ATOM   62   N N   . GLY   A 1 14  ? -27.662 7.322   -24.636 1.00 41.41  ? 57  GLY   A N   1 
ATOM   63   C CA  . GLY   A 1 14  ? -27.992 6.286   -25.635 1.00 36.63  ? 57  GLY   A CA  1 
ATOM   64   C C   . GLY   A 1 14  ? -28.729 5.131   -24.995 1.00 42.35  ? 57  GLY   A C   1 
ATOM   65   O O   . GLY   A 1 14  ? -28.807 5.107   -23.727 1.00 44.81  ? 57  GLY   A O   1 
ATOM   66   N N   . ASP   A 1 15  ? -29.303 4.267   -25.832 1.00 44.89  ? 58  ASP   A N   1 
ATOM   67   C CA  . ASP   A 1 15  ? -29.835 2.940   -25.440 1.00 51.35  ? 58  ASP   A CA  1 
ATOM   68   C C   . ASP   A 1 15  ? -28.638 2.012   -25.286 1.00 55.39  ? 58  ASP   A C   1 
ATOM   69   O O   . ASP   A 1 15  ? -27.581 2.385   -25.813 1.00 52.34  ? 58  ASP   A O   1 
ATOM   70   C CB  . ASP   A 1 15  ? -30.736 2.323   -26.509 1.00 56.09  ? 58  ASP   A CB  1 
ATOM   71   C CG  . ASP   A 1 15  ? -32.069 3.028   -26.634 1.00 65.14  ? 58  ASP   A CG  1 
ATOM   72   O OD1 . ASP   A 1 15  ? -32.132 4.170   -26.177 1.00 62.14  ? 58  ASP   A OD1 1 
ATOM   73   O OD2 . ASP   A 1 15  ? -33.033 2.420   -27.183 1.00 68.11  ? 58  ASP   A OD2 1 
ATOM   74   N N   . ILE   A 1 16  ? -28.826 0.871   -24.615 1.00 62.23  ? 59  ILE   A N   1 
ATOM   75   C CA  . ILE   A 1 16  ? -27.790 -0.191  -24.445 1.00 61.51  ? 59  ILE   A CA  1 
ATOM   76   C C   . ILE   A 1 16  ? -28.207 -1.342  -25.363 1.00 55.20  ? 59  ILE   A C   1 
ATOM   77   O O   . ILE   A 1 16  ? -29.114 -2.119  -25.011 1.00 57.67  ? 59  ILE   A O   1 
ATOM   78   C CB  . ILE   A 1 16  ? -27.651 -0.560  -22.957 1.00 59.58  ? 59  ILE   A CB  1 
ATOM   79   C CG1 . ILE   A 1 16  ? -26.959 0.589   -22.218 1.00 59.11  ? 59  ILE   A CG1 1 
ATOM   80   C CG2 . ILE   A 1 16  ? -26.893 -1.855  -22.785 1.00 61.90  ? 59  ILE   A CG2 1 
ATOM   81   C CD1 . ILE   A 1 16  ? -27.112 0.540   -20.727 1.00 62.17  ? 59  ILE   A CD1 1 
ATOM   82   N N   A THR   A 1 17  ? -27.561 -1.407  -26.533 0.25 55.98  ? 60  THR   A N   1 
ATOM   83   N N   B THR   A 1 17  ? -27.571 -1.441  -26.530 0.25 55.93  ? 60  THR   A N   1 
ATOM   84   N N   C THR   A 1 17  ? -27.561 -1.407  -26.533 0.25 55.98  ? 60  THR   A N   1 
ATOM   85   N N   D THR   A 1 17  ? -27.571 -1.441  -26.530 0.25 55.93  ? 60  THR   A N   1 
ATOM   86   C CA  A THR   A 1 17  ? -27.884 -2.320  -27.663 0.25 57.00  ? 60  THR   A CA  1 
ATOM   87   C CA  B THR   A 1 17  ? -27.949 -2.388  -27.612 0.25 57.20  ? 60  THR   A CA  1 
ATOM   88   C CA  C THR   A 1 17  ? -27.884 -2.320  -27.663 0.25 57.00  ? 60  THR   A CA  1 
ATOM   89   C CA  D THR   A 1 17  ? -27.949 -2.388  -27.612 0.25 57.20  ? 60  THR   A CA  1 
ATOM   90   C C   A THR   A 1 17  ? -26.600 -2.887  -28.267 0.25 54.83  ? 60  THR   A C   1 
ATOM   91   C C   B THR   A 1 17  ? -26.678 -2.871  -28.322 0.25 55.16  ? 60  THR   A C   1 
ATOM   92   C C   C THR   A 1 17  ? -26.600 -2.887  -28.267 0.25 54.83  ? 60  THR   A C   1 
ATOM   93   C C   D THR   A 1 17  ? -26.678 -2.871  -28.322 0.25 55.16  ? 60  THR   A C   1 
ATOM   94   O O   A THR   A 1 17  ? -25.606 -2.128  -28.387 0.25 51.73  ? 60  THR   A O   1 
ATOM   95   O O   B THR   A 1 17  ? -25.751 -2.050  -28.520 0.25 53.38  ? 60  THR   A O   1 
ATOM   96   O O   C THR   A 1 17  ? -25.606 -2.128  -28.387 0.25 51.73  ? 60  THR   A O   1 
ATOM   97   O O   D THR   A 1 17  ? -25.751 -2.050  -28.520 0.25 53.38  ? 60  THR   A O   1 
ATOM   98   C CB  A THR   A 1 17  ? -28.653 -1.610  -28.787 0.25 56.35  ? 60  THR   A CB  1 
ATOM   99   C CB  B THR   A 1 17  ? -28.987 -1.748  -28.551 0.25 56.36  ? 60  THR   A CB  1 
ATOM   100  C CB  C THR   A 1 17  ? -28.653 -1.610  -28.787 0.25 56.35  ? 60  THR   A CB  1 
ATOM   101  C CB  D THR   A 1 17  ? -28.987 -1.748  -28.551 0.25 56.36  ? 60  THR   A CB  1 
ATOM   102  O OG1 A THR   A 1 17  ? -27.780 -0.680  -29.436 0.25 53.31  ? 60  THR   A OG1 1 
ATOM   103  O OG1 B THR   A 1 17  ? -30.285 -1.949  -27.988 0.25 56.18  ? 60  THR   A OG1 1 
ATOM   104  O OG1 C THR   A 1 17  ? -27.780 -0.680  -29.436 0.25 53.31  ? 60  THR   A OG1 1 
ATOM   105  O OG1 D THR   A 1 17  ? -30.285 -1.949  -27.988 0.25 56.18  ? 60  THR   A OG1 1 
ATOM   106  C CG2 A THR   A 1 17  ? -29.898 -0.917  -28.282 0.25 55.61  ? 60  THR   A CG2 1 
ATOM   107  C CG2 B THR   A 1 17  ? -28.980 -2.319  -29.951 0.25 55.26  ? 60  THR   A CG2 1 
ATOM   108  C CG2 C THR   A 1 17  ? -29.898 -0.917  -28.282 0.25 55.61  ? 60  THR   A CG2 1 
ATOM   109  C CG2 D THR   A 1 17  ? -28.980 -2.319  -29.951 0.25 55.26  ? 60  THR   A CG2 1 
ATOM   110  N N   . TRP   A 1 18  ? -26.634 -4.171  -28.632 1.00 57.05  ? 61  TRP   A N   1 
ATOM   111  C CA  . TRP   A 1 18  ? -25.592 -4.788  -29.482 1.00 64.78  ? 61  TRP   A CA  1 
ATOM   112  C C   . TRP   A 1 18  ? -25.863 -4.271  -30.887 1.00 63.64  ? 61  TRP   A C   1 
ATOM   113  O O   . TRP   A 1 18  ? -27.006 -4.209  -31.295 1.00 73.15  ? 61  TRP   A O   1 
ATOM   114  C CB  . TRP   A 1 18  ? -25.631 -6.312  -29.426 1.00 68.52  ? 61  TRP   A CB  1 
ATOM   115  C CG  . TRP   A 1 18  ? -24.536 -6.944  -30.226 1.00 75.09  ? 61  TRP   A CG  1 
ATOM   116  C CD1 . TRP   A 1 18  ? -24.564 -7.227  -31.556 1.00 75.23  ? 61  TRP   A CD1 1 
ATOM   117  C CD2 . TRP   A 1 18  ? -23.242 -7.354  -29.754 1.00 78.97  ? 61  TRP   A CD2 1 
ATOM   118  N NE1 . TRP   A 1 18  ? -23.377 -7.775  -31.943 1.00 78.39  ? 61  TRP   A NE1 1 
ATOM   119  C CE2 . TRP   A 1 18  ? -22.553 -7.885  -30.861 1.00 80.26  ? 61  TRP   A CE2 1 
ATOM   120  C CE3 . TRP   A 1 18  ? -22.597 -7.328  -28.515 1.00 74.88  ? 61  TRP   A CE3 1 
ATOM   121  C CZ2 . TRP   A 1 18  ? -21.258 -8.385  -30.766 1.00 80.44  ? 61  TRP   A CZ2 1 
ATOM   122  C CZ3 . TRP   A 1 18  ? -21.321 -7.825  -28.420 1.00 79.21  ? 61  TRP   A CZ3 1 
ATOM   123  C CH2 . TRP   A 1 18  ? -20.665 -8.356  -29.528 1.00 79.87  ? 61  TRP   A CH2 1 
ATOM   124  N N   A GLU   A 1 19  ? -24.809 -3.804  -31.560 0.25 66.20  ? 62  GLU   A N   1 
ATOM   125  N N   B GLU   A 1 19  ? -24.809 -3.804  -31.560 0.25 66.20  ? 62  GLU   A N   1 
ATOM   126  N N   C GLU   A 1 19  ? -24.783 -4.078  -31.639 0.25 68.94  ? 62  GLU   A N   1 
ATOM   127  N N   D GLU   A 1 19  ? -24.783 -4.078  -31.639 0.25 68.94  ? 62  GLU   A N   1 
ATOM   128  C CA  A GLU   A 1 19  ? -24.864 -3.196  -32.915 0.25 68.88  ? 62  GLU   A CA  1 
ATOM   129  C CA  B GLU   A 1 19  ? -24.864 -3.196  -32.915 0.25 68.88  ? 62  GLU   A CA  1 
ATOM   130  C CA  C GLU   A 1 19  ? -24.717 -3.231  -32.850 0.25 69.45  ? 62  GLU   A CA  1 
ATOM   131  C CA  D GLU   A 1 19  ? -24.717 -3.231  -32.850 0.25 69.45  ? 62  GLU   A CA  1 
ATOM   132  C C   A GLU   A 1 19  ? -24.027 -4.043  -33.880 0.25 71.76  ? 62  GLU   A C   1 
ATOM   133  C C   B GLU   A 1 19  ? -24.027 -4.043  -33.880 0.25 71.76  ? 62  GLU   A C   1 
ATOM   134  C C   C GLU   A 1 19  ? -23.957 -4.000  -33.935 0.25 72.28  ? 62  GLU   A C   1 
ATOM   135  C C   D GLU   A 1 19  ? -23.957 -4.000  -33.935 0.25 72.28  ? 62  GLU   A C   1 
ATOM   136  O O   A GLU   A 1 19  ? -22.831 -4.252  -33.600 0.25 73.10  ? 62  GLU   A O   1 
ATOM   137  O O   B GLU   A 1 19  ? -22.831 -4.252  -33.600 0.25 73.10  ? 62  GLU   A O   1 
ATOM   138  O O   C GLU   A 1 19  ? -22.722 -4.121  -33.794 0.25 73.51  ? 62  GLU   A O   1 
ATOM   139  O O   D GLU   A 1 19  ? -22.722 -4.121  -33.794 0.25 73.51  ? 62  GLU   A O   1 
ATOM   140  C CB  A GLU   A 1 19  ? -24.351 -1.757  -32.861 0.25 70.13  ? 62  GLU   A CB  1 
ATOM   141  C CB  B GLU   A 1 19  ? -24.351 -1.757  -32.861 0.25 70.13  ? 62  GLU   A CB  1 
ATOM   142  C CB  C GLU   A 1 19  ? -24.007 -1.949  -32.414 0.25 69.67  ? 62  GLU   A CB  1 
ATOM   143  C CB  D GLU   A 1 19  ? -24.007 -1.949  -32.414 0.25 69.67  ? 62  GLU   A CB  1 
ATOM   144  C CG  A GLU   A 1 19  ? -25.144 -0.864  -31.917 0.25 72.37  ? 62  GLU   A CG  1 
ATOM   145  C CG  B GLU   A 1 19  ? -25.144 -0.864  -31.917 0.25 72.37  ? 62  GLU   A CG  1 
ATOM   146  C CG  C GLU   A 1 19  ? -23.947 -0.858  -33.461 0.25 70.46  ? 62  GLU   A CG  1 
ATOM   147  C CG  D GLU   A 1 19  ? -23.947 -0.858  -33.461 0.25 70.46  ? 62  GLU   A CG  1 
ATOM   148  C CD  A GLU   A 1 19  ? -26.428 -0.292  -32.497 0.25 70.91  ? 62  GLU   A CD  1 
ATOM   149  C CD  B GLU   A 1 19  ? -26.428 -0.292  -32.497 0.25 70.91  ? 62  GLU   A CD  1 
ATOM   150  C CD  C GLU   A 1 19  ? -22.964 -1.116  -34.586 0.25 71.78  ? 62  GLU   A CD  1 
ATOM   151  C CD  D GLU   A 1 19  ? -22.964 -1.116  -34.586 0.25 71.78  ? 62  GLU   A CD  1 
ATOM   152  O OE1 A GLU   A 1 19  ? -26.331 0.566   -33.402 0.25 73.13  ? 62  GLU   A OE1 1 
ATOM   153  O OE1 B GLU   A 1 19  ? -26.331 0.566   -33.402 0.25 73.13  ? 62  GLU   A OE1 1 
ATOM   154  O OE1 C GLU   A 1 19  ? -22.539 -2.276  -34.733 0.25 79.39  ? 62  GLU   A OE1 1 
ATOM   155  O OE1 D GLU   A 1 19  ? -22.539 -2.276  -34.733 0.25 79.39  ? 62  GLU   A OE1 1 
ATOM   156  O OE2 A GLU   A 1 19  ? -27.519 -0.710  -32.052 0.25 63.84  ? 62  GLU   A OE2 1 
ATOM   157  O OE2 B GLU   A 1 19  ? -27.519 -0.710  -32.052 0.25 63.84  ? 62  GLU   A OE2 1 
ATOM   158  O OE2 C GLU   A 1 19  ? -22.623 -0.157  -35.304 0.25 67.47  ? 62  GLU   A OE2 1 
ATOM   159  O OE2 D GLU   A 1 19  ? -22.623 -0.157  -35.304 0.25 67.47  ? 62  GLU   A OE2 1 
ATOM   160  N N   . LYS   A 1 20  ? -24.647 -4.514  -34.964 1.00 74.65  ? 63  LYS   A N   1 
ATOM   161  C CA  . LYS   A 1 20  ? -23.971 -5.310  -36.026 1.00 73.91  ? 63  LYS   A CA  1 
ATOM   162  C C   . LYS   A 1 20  ? -23.012 -4.404  -36.792 1.00 74.82  ? 63  LYS   A C   1 
ATOM   163  O O   . LYS   A 1 20  ? -23.321 -3.206  -36.961 1.00 77.75  ? 63  LYS   A O   1 
ATOM   164  C CB  . LYS   A 1 20  ? -25.004 -5.956  -36.940 1.00 81.62  ? 63  LYS   A CB  1 
ATOM   165  C CG  . LYS   A 1 20  ? -25.878 -6.958  -36.207 1.00 97.19  ? 63  LYS   A CG  1 
ATOM   166  C CD  . LYS   A 1 20  ? -27.354 -6.784  -36.470 1.00 105.80 ? 63  LYS   A CD  1 
ATOM   167  C CE  . LYS   A 1 20  ? -28.213 -7.716  -35.642 1.00 113.89 ? 63  LYS   A CE  1 
ATOM   168  N NZ  . LYS   A 1 20  ? -29.636 -7.655  -36.051 1.00 113.21 ? 63  LYS   A NZ  1 
ATOM   169  N N   . ASP   A 1 21  ? -21.852 -4.941  -37.153 1.00 78.15  ? 64  ASP   A N   1 
ATOM   170  C CA  . ASP   A 1 21  ? -20.818 -4.233  -37.954 1.00 90.92  ? 64  ASP   A CA  1 
ATOM   171  C C   . ASP   A 1 21  ? -20.354 -2.978  -37.204 1.00 85.50  ? 64  ASP   A C   1 
ATOM   172  O O   . ASP   A 1 21  ? -20.078 -1.953  -37.856 1.00 82.13  ? 64  ASP   A O   1 
ATOM   173  C CB  . ASP   A 1 21  ? -21.337 -3.948  -39.370 1.00 114.12 ? 64  ASP   A CB  1 
ATOM   174  C CG  . ASP   A 1 21  ? -21.810 -5.202  -40.097 1.00 121.30 ? 64  ASP   A CG  1 
ATOM   175  O OD1 . ASP   A 1 21  ? -20.944 -6.033  -40.436 1.00 124.12 ? 64  ASP   A OD1 1 
ATOM   176  O OD2 . ASP   A 1 21  ? -23.043 -5.363  -40.280 1.00 115.18 ? 64  ASP   A OD2 1 
ATOM   177  N N   . ALA   A 1 22  ? -20.222 -3.063  -35.879 1.00 81.77  ? 65  ALA   A N   1 
ATOM   178  C CA  . ALA   A 1 22  ? -19.406 -2.108  -35.102 1.00 75.11  ? 65  ALA   A CA  1 
ATOM   179  C C   . ALA   A 1 22  ? -17.945 -2.313  -35.505 1.00 63.95  ? 65  ALA   A C   1 
ATOM   180  O O   . ALA   A 1 22  ? -17.561 -3.458  -35.791 1.00 64.29  ? 65  ALA   A O   1 
ATOM   181  C CB  . ALA   A 1 22  ? -19.605 -2.307  -33.622 1.00 78.38  ? 65  ALA   A CB  1 
ATOM   182  N N   . GLU   A 1 23  ? -17.173 -1.235  -35.554 1.00 68.81  ? 66  GLU   A N   1 
ATOM   183  C CA  . GLU   A 1 23  ? -15.699 -1.275  -35.709 1.00 79.46  ? 66  GLU   A CA  1 
ATOM   184  C C   . GLU   A 1 23  ? -15.132 -2.314  -34.723 1.00 85.42  ? 66  GLU   A C   1 
ATOM   185  O O   . GLU   A 1 23  ? -15.305 -2.147  -33.500 1.00 81.49  ? 66  GLU   A O   1 
ATOM   186  C CB  . GLU   A 1 23  ? -15.189 0.145   -35.484 1.00 89.79  ? 66  GLU   A CB  1 
ATOM   187  C CG  . GLU   A 1 23  ? -13.682 0.311   -35.522 1.00 97.43  ? 66  GLU   A CG  1 
ATOM   188  C CD  . GLU   A 1 23  ? -13.256 1.503   -34.681 1.00 101.36 ? 66  GLU   A CD  1 
ATOM   189  O OE1 . GLU   A 1 23  ? -14.029 2.484   -34.615 1.00 96.25  ? 66  GLU   A OE1 1 
ATOM   190  O OE2 . GLU   A 1 23  ? -12.185 1.435   -34.057 1.00 111.06 ? 66  GLU   A OE2 1 
ATOM   191  N N   . VAL   A 1 24  ? -14.519 -3.378  -35.244 1.00 83.57  ? 67  VAL   A N   1 
ATOM   192  C CA  . VAL   A 1 24  ? -13.862 -4.469  -34.462 1.00 74.99  ? 67  VAL   A CA  1 
ATOM   193  C C   . VAL   A 1 24  ? -12.401 -4.090  -34.232 1.00 72.99  ? 67  VAL   A C   1 
ATOM   194  O O   . VAL   A 1 24  ? -11.767 -3.704  -35.199 1.00 79.98  ? 67  VAL   A O   1 
ATOM   195  C CB  . VAL   A 1 24  ? -13.969 -5.800  -35.215 1.00 68.41  ? 67  VAL   A CB  1 
ATOM   196  C CG1 . VAL   A 1 24  ? -13.260 -6.903  -34.469 1.00 62.02  ? 67  VAL   A CG1 1 
ATOM   197  C CG2 . VAL   A 1 24  ? -15.426 -6.163  -35.486 1.00 70.00  ? 67  VAL   A CG2 1 
ATOM   198  N N   . THR   A 1 25  ? -11.887 -4.172  -33.003 1.00 75.63  ? 68  THR   A N   1 
ATOM   199  C CA  . THR   A 1 25  ? -10.493 -3.742  -32.700 1.00 72.88  ? 68  THR   A CA  1 
ATOM   200  C C   . THR   A 1 25  ? -10.036 -4.151  -31.292 1.00 69.05  ? 68  THR   A C   1 
ATOM   201  O O   . THR   A 1 25  ? -10.740 -4.923  -30.617 1.00 59.61  ? 68  THR   A O   1 
ATOM   202  C CB  . THR   A 1 25  ? -10.325 -2.235  -32.900 1.00 74.03  ? 68  THR   A CB  1 
ATOM   203  O OG1 . THR   A 1 25  ? -8.935  -1.986  -32.732 1.00 81.54  ? 68  THR   A OG1 1 
ATOM   204  C CG2 . THR   A 1 25  ? -11.111 -1.387  -31.927 1.00 84.73  ? 68  THR   A CG2 1 
ATOM   205  N N   . GLY   A 1 26  ? -8.846  -3.684  -30.914 1.00 67.85  ? 69  GLY   A N   1 
ATOM   206  C CA  . GLY   A 1 26  ? -8.089  -4.139  -29.737 1.00 74.15  ? 69  GLY   A CA  1 
ATOM   207  C C   . GLY   A 1 26  ? -7.694  -5.612  -29.796 1.00 69.63  ? 69  GLY   A C   1 
ATOM   208  O O   . GLY   A 1 26  ? -8.323  -6.402  -30.536 1.00 70.12  ? 69  GLY   A O   1 
ATOM   209  N N   . ASN   A 1 27  ? -6.733  -5.966  -28.947 1.00 65.67  ? 70  ASN   A N   1 
ATOM   210  C CA  . ASN   A 1 27  ? -6.168  -7.328  -28.776 1.00 71.90  ? 70  ASN   A CA  1 
ATOM   211  C C   . ASN   A 1 27  ? -6.691  -7.953  -27.467 1.00 67.97  ? 70  ASN   A C   1 
ATOM   212  O O   . ASN   A 1 27  ? -7.713  -7.460  -26.928 1.00 65.71  ? 70  ASN   A O   1 
ATOM   213  C CB  . ASN   A 1 27  ? -4.650  -7.205  -28.829 1.00 74.17  ? 70  ASN   A CB  1 
ATOM   214  C CG  . ASN   A 1 27  ? -4.197  -6.142  -27.863 1.00 77.56  ? 70  ASN   A CG  1 
ATOM   215  O OD1 . ASN   A 1 27  ? -4.563  -4.979  -28.015 1.00 94.11  ? 70  ASN   A OD1 1 
ATOM   216  N ND2 . ASN   A 1 27  ? -3.482  -6.544  -26.833 1.00 78.44  ? 70  ASN   A ND2 1 
ATOM   217  N N   . SER   A 1 28  ? -6.028  -9.008  -26.973 1.00 53.44  ? 71  SER   A N   1 
ATOM   218  C CA  . SER   A 1 28  ? -6.526  -9.912  -25.899 1.00 56.59  ? 71  SER   A CA  1 
ATOM   219  C C   . SER   A 1 28  ? -5.402  -10.312 -24.956 1.00 54.51  ? 71  SER   A C   1 
ATOM   220  O O   . SER   A 1 28  ? -5.179  -11.500 -24.752 1.00 57.61  ? 71  SER   A O   1 
ATOM   221  C CB  . SER   A 1 28  ? -7.187  -11.153 -26.464 1.00 50.25  ? 71  SER   A CB  1 
ATOM   222  O OG  . SER   A 1 28  ? -8.067  -10.794 -27.511 1.00 60.89  ? 71  SER   A OG  1 
ATOM   223  N N   . PRO   A 1 29  ? -4.741  -9.353  -24.276 1.00 61.31  ? 72  PRO   A N   1 
ATOM   224  C CA  . PRO   A 1 29  ? -3.557  -9.653  -23.470 1.00 67.61  ? 72  PRO   A CA  1 
ATOM   225  C C   . PRO   A 1 29  ? -3.883  -10.384 -22.159 1.00 74.01  ? 72  PRO   A C   1 
ATOM   226  O O   . PRO   A 1 29  ? -4.813  -9.951  -21.505 1.00 73.70  ? 72  PRO   A O   1 
ATOM   227  C CB  . PRO   A 1 29  ? -2.970  -8.263  -23.180 1.00 72.63  ? 72  PRO   A CB  1 
ATOM   228  C CG  . PRO   A 1 29  ? -4.160  -7.306  -23.221 1.00 75.12  ? 72  PRO   A CG  1 
ATOM   229  C CD  . PRO   A 1 29  ? -5.158  -7.944  -24.168 1.00 74.77  ? 72  PRO   A CD  1 
ATOM   230  N N   . ARG   A 1 30  ? -3.150  -11.463 -21.837 1.00 72.59  ? 73  ARG   A N   1 
ATOM   231  C CA  . ARG   A 1 30  ? -3.264  -12.234 -20.562 1.00 77.07  ? 73  ARG   A CA  1 
ATOM   232  C C   . ARG   A 1 30  ? -2.237  -11.663 -19.587 1.00 73.28  ? 73  ARG   A C   1 
ATOM   233  O O   . ARG   A 1 30  ? -1.054  -11.758 -19.893 1.00 68.71  ? 73  ARG   A O   1 
ATOM   234  C CB  . ARG   A 1 30  ? -3.014  -13.726 -20.793 1.00 81.63  ? 73  ARG   A CB  1 
ATOM   235  C CG  . ARG   A 1 30  ? -4.026  -14.375 -21.725 1.00 92.66  ? 73  ARG   A CG  1 
ATOM   236  C CD  . ARG   A 1 30  ? -3.505  -15.657 -22.336 1.00 103.08 ? 73  ARG   A CD  1 
ATOM   237  N NE  . ARG   A 1 30  ? -4.548  -16.391 -23.047 1.00 114.51 ? 73  ARG   A NE  1 
ATOM   238  C CZ  . ARG   A 1 30  ? -5.493  -17.148 -22.480 1.00 117.89 ? 73  ARG   A CZ  1 
ATOM   239  N NH1 . ARG   A 1 30  ? -5.548  -17.292 -21.164 1.00 130.36 ? 73  ARG   A NH1 1 
ATOM   240  N NH2 . ARG   A 1 30  ? -6.389  -17.763 -23.238 1.00 104.60 ? 73  ARG   A NH2 1 
ATOM   241  N N   . LEU   A 1 31  ? -2.673  -11.035 -18.496 1.00 71.32  ? 74  LEU   A N   1 
ATOM   242  C CA  . LEU   A 1 31  ? -1.768  -10.282 -17.590 1.00 69.52  ? 74  LEU   A CA  1 
ATOM   243  C C   . LEU   A 1 31  ? -1.918  -10.809 -16.169 1.00 68.46  ? 74  LEU   A C   1 
ATOM   244  O O   . LEU   A 1 31  ? -3.066  -11.079 -15.744 1.00 69.65  ? 74  LEU   A O   1 
ATOM   245  C CB  . LEU   A 1 31  ? -2.110  -8.791  -17.625 1.00 69.73  ? 74  LEU   A CB  1 
ATOM   246  C CG  . LEU   A 1 31  ? -1.999  -8.105  -18.983 1.00 75.64  ? 74  LEU   A CG  1 
ATOM   247  C CD1 . LEU   A 1 31  ? -2.664  -6.741  -18.936 1.00 75.21  ? 74  LEU   A CD1 1 
ATOM   248  C CD2 . LEU   A 1 31  ? -0.543  -7.969  -19.427 1.00 77.66  ? 74  LEU   A CD2 1 
ATOM   249  N N   . ASP   A 1 32  ? -0.782  -10.921 -15.478 1.00 73.29  ? 75  ASP   A N   1 
ATOM   250  C CA  . ASP   A 1 32  ? -0.681  -11.211 -14.027 1.00 69.34  ? 75  ASP   A CA  1 
ATOM   251  C C   . ASP   A 1 32  ? -0.799  -9.890  -13.280 1.00 59.82  ? 75  ASP   A C   1 
ATOM   252  O O   . ASP   A 1 32  ? 0.056   -9.012  -13.492 1.00 67.25  ? 75  ASP   A O   1 
ATOM   253  C CB  . ASP   A 1 32  ? 0.645   -11.886 -13.679 1.00 76.02  ? 75  ASP   A CB  1 
ATOM   254  C CG  . ASP   A 1 32  ? 0.793   -13.256 -14.309 1.00 79.86  ? 75  ASP   A CG  1 
ATOM   255  O OD1 . ASP   A 1 32  ? -0.153  -14.064 -14.208 1.00 82.14  ? 75  ASP   A OD1 1 
ATOM   256  O OD2 . ASP   A 1 32  ? 1.847   -13.491 -14.911 1.00 102.11 ? 75  ASP   A OD2 1 
ATOM   257  N N   . VAL   A 1 33  ? -1.843  -9.744  -12.469 1.00 61.64  ? 76  VAL   A N   1 
ATOM   258  C CA  . VAL   A 1 33  ? -2.137  -8.457  -11.773 1.00 58.62  ? 76  VAL   A CA  1 
ATOM   259  C C   . VAL   A 1 33  ? -2.413  -8.768  -10.304 1.00 54.66  ? 76  VAL   A C   1 
ATOM   260  O O   . VAL   A 1 33  ? -2.889  -9.910  -9.976  1.00 58.38  ? 76  VAL   A O   1 
ATOM   261  C CB  . VAL   A 1 33  ? -3.305  -7.672  -12.420 1.00 54.22  ? 76  VAL   A CB  1 
ATOM   262  C CG1 . VAL   A 1 33  ? -3.067  -7.354  -13.876 1.00 52.96  ? 76  VAL   A CG1 1 
ATOM   263  C CG2 . VAL   A 1 33  ? -4.642  -8.378  -12.268 1.00 57.78  ? 76  VAL   A CG2 1 
ATOM   264  N N   . ALA   A 1 34  ? -2.163  -7.784  -9.450  1.00 51.59  ? 77  ALA   A N   1 
ATOM   265  C CA  . ALA   A 1 34  ? -2.605  -7.803  -8.033  1.00 59.36  ? 77  ALA   A CA  1 
ATOM   266  C C   . ALA   A 1 34  ? -3.574  -6.645  -7.815  1.00 59.11  ? 77  ALA   A C   1 
ATOM   267  O O   . ALA   A 1 34  ? -3.427  -5.583  -8.467  1.00 58.86  ? 77  ALA   A O   1 
ATOM   268  C CB  . ALA   A 1 34  ? -1.434  -7.712  -7.089  1.00 58.10  ? 77  ALA   A CB  1 
ATOM   269  N N   . LEU   A 1 35  ? -4.509  -6.854  -6.906  1.00 51.47  ? 78  LEU   A N   1 
ATOM   270  C CA  . LEU   A 1 35  ? -5.524  -5.857  -6.509  1.00 55.20  ? 78  LEU   A CA  1 
ATOM   271  C C   . LEU   A 1 35  ? -5.323  -5.532  -5.020  1.00 55.35  ? 78  LEU   A C   1 
ATOM   272  O O   . LEU   A 1 35  ? -5.554  -6.437  -4.172  1.00 52.87  ? 78  LEU   A O   1 
ATOM   273  C CB  . LEU   A 1 35  ? -6.897  -6.470  -6.818  1.00 55.26  ? 78  LEU   A CB  1 
ATOM   274  C CG  . LEU   A 1 35  ? -8.120  -5.624  -6.474  1.00 57.21  ? 78  LEU   A CG  1 
ATOM   275  C CD1 . LEU   A 1 35  ? -8.126  -4.298  -7.226  1.00 57.07  ? 78  LEU   A CD1 1 
ATOM   276  C CD2 . LEU   A 1 35  ? -9.394  -6.416  -6.748  1.00 61.51  ? 78  LEU   A CD2 1 
ATOM   277  N N   . ASP   A 1 36  ? -4.903  -4.295  -4.724  1.00 47.23  ? 79  ASP   A N   1 
ATOM   278  C CA  . ASP   A 1 36  ? -4.769  -3.760  -3.350  1.00 55.72  ? 79  ASP   A CA  1 
ATOM   279  C C   . ASP   A 1 36  ? -6.153  -3.338  -2.816  1.00 56.36  ? 79  ASP   A C   1 
ATOM   280  O O   . ASP   A 1 36  ? -7.165  -3.394  -3.576  1.00 53.04  ? 79  ASP   A O   1 
ATOM   281  C CB  . ASP   A 1 36  ? -3.724  -2.635  -3.283  1.00 51.74  ? 79  ASP   A CB  1 
ATOM   282  C CG  . ASP   A 1 36  ? -4.155  -1.273  -3.805  1.00 59.31  ? 79  ASP   A CG  1 
ATOM   283  O OD1 . ASP   A 1 36  ? -5.381  -1.055  -4.013  1.00 59.42  ? 79  ASP   A OD1 1 
ATOM   284  O OD2 . ASP   A 1 36  ? -3.245  -0.427  -4.019  1.00 63.51  ? 79  ASP   A OD2 1 
ATOM   285  N N   . GLU   A 1 37  ? -6.160  -2.939  -1.541  1.00 52.19  ? 80  GLU   A N   1 
ATOM   286  C CA  . GLU   A 1 37  ? -7.357  -2.670  -0.720  1.00 52.90  ? 80  GLU   A CA  1 
ATOM   287  C C   . GLU   A 1 37  ? -7.975  -1.347  -1.181  1.00 50.34  ? 80  GLU   A C   1 
ATOM   288  O O   . GLU   A 1 37  ? -9.177  -1.128  -0.904  1.00 53.87  ? 80  GLU   A O   1 
ATOM   289  C CB  . GLU   A 1 37  ? -6.958  -2.665  0.757   1.00 55.50  ? 80  GLU   A CB  1 
ATOM   290  C CG  . GLU   A 1 37  ? -8.122  -2.874  1.703   1.00 64.07  ? 80  GLU   A CG  1 
ATOM   291  C CD  . GLU   A 1 37  ? -7.748  -2.889  3.178   1.00 74.10  ? 80  GLU   A CD  1 
ATOM   292  O OE1 . GLU   A 1 37  ? -7.281  -1.825  3.705   1.00 65.22  ? 80  GLU   A OE1 1 
ATOM   293  O OE2 . GLU   A 1 37  ? -7.892  -3.972  3.795   1.00 71.08  ? 80  GLU   A OE2 1 
ATOM   294  N N   . SER   A 1 38  ? -7.203  -0.492  -1.851  1.00 48.95  ? 81  SER   A N   1 
ATOM   295  C CA  . SER   A 1 38  ? -7.705  0.761   -2.475  1.00 49.25  ? 81  SER   A CA  1 
ATOM   296  C C   . SER   A 1 38  ? -8.357  0.535   -3.856  1.00 50.95  ? 81  SER   A C   1 
ATOM   297  O O   . SER   A 1 38  ? -8.702  1.550   -4.487  1.00 52.16  ? 81  SER   A O   1 
ATOM   298  C CB  . SER   A 1 38  ? -6.604  1.745   -2.585  1.00 49.10  ? 81  SER   A CB  1 
ATOM   299  O OG  . SER   A 1 38  ? -5.982  1.828   -1.340  1.00 60.18  ? 81  SER   A OG  1 
ATOM   300  N N   . GLY   A 1 39  ? -8.522  -0.708  -4.329  1.00 54.68  ? 82  GLY   A N   1 
ATOM   301  C CA  . GLY   A 1 39  ? -9.117  -1.005  -5.652  1.00 51.18  ? 82  GLY   A CA  1 
ATOM   302  C C   . GLY   A 1 39  ? -8.166  -0.618  -6.790  1.00 56.17  ? 82  GLY   A C   1 
ATOM   303  O O   . GLY   A 1 39  ? -8.655  -0.386  -7.909  1.00 56.04  ? 82  GLY   A O   1 
ATOM   304  N N   . ASP   A 1 40  ? -6.851  -0.562  -6.529  1.00 52.03  ? 83  ASP   A N   1 
ATOM   305  C CA  . ASP   A 1 40  ? -5.805  -0.332  -7.565  1.00 53.74  ? 83  ASP   A CA  1 
ATOM   306  C C   . ASP   A 1 40  ? -5.199  -1.684  -8.003  1.00 59.83  ? 83  ASP   A C   1 
ATOM   307  O O   . ASP   A 1 40  ? -4.624  -2.398  -7.187  1.00 51.02  ? 83  ASP   A O   1 
ATOM   308  C CB  . ASP   A 1 40  ? -4.802  0.716   -7.087  1.00 51.67  ? 83  ASP   A CB  1 
ATOM   309  C CG  . ASP   A 1 40  ? -5.481  2.046   -6.743  1.00 60.83  ? 83  ASP   A CG  1 
ATOM   310  O OD1 . ASP   A 1 40  ? -6.658  2.251   -7.156  1.00 58.05  ? 83  ASP   A OD1 1 
ATOM   311  O OD2 . ASP   A 1 40  ? -4.833  2.885   -6.078  1.00 68.42  ? 83  ASP   A OD2 1 
ATOM   312  N N   . PHE   A 1 41  ? -5.402  -2.024  -9.275  1.00 54.36  ? 84  PHE   A N   1 
ATOM   313  C CA  . PHE   A 1 41  ? -4.702  -3.099  -10.006 1.00 55.84  ? 84  PHE   A CA  1 
ATOM   314  C C   . PHE   A 1 41  ? -3.221  -2.755  -10.184 1.00 60.61  ? 84  PHE   A C   1 
ATOM   315  O O   . PHE   A 1 41  ? -2.907  -1.581  -10.414 1.00 52.63  ? 84  PHE   A O   1 
ATOM   316  C CB  . PHE   A 1 41  ? -5.407  -3.303  -11.342 1.00 50.29  ? 84  PHE   A CB  1 
ATOM   317  C CG  . PHE   A 1 41  ? -6.706  -4.057  -11.213 1.00 52.72  ? 84  PHE   A CG  1 
ATOM   318  C CD1 . PHE   A 1 41  ? -6.715  -5.372  -10.767 1.00 50.08  ? 84  PHE   A CD1 1 
ATOM   319  C CD2 . PHE   A 1 41  ? -7.925  -3.459  -11.515 1.00 54.60  ? 84  PHE   A CD2 1 
ATOM   320  C CE1 . PHE   A 1 41  ? -7.900  -6.080  -10.652 1.00 49.94  ? 84  PHE   A CE1 1 
ATOM   321  C CE2 . PHE   A 1 41  ? -9.112  -4.175  -11.406 1.00 46.02  ? 84  PHE   A CE2 1 
ATOM   322  C CZ  . PHE   A 1 41  ? -9.092  -5.483  -10.987 1.00 48.71  ? 84  PHE   A CZ  1 
ATOM   323  N N   . SER   A 1 42  ? -2.332  -3.753  -10.121 1.00 64.48  ? 85  SER   A N   1 
ATOM   324  C CA  . SER   A 1 42  ? -0.889  -3.586  -10.459 1.00 62.71  ? 85  SER   A CA  1 
ATOM   325  C C   . SER   A 1 42  ? -0.366  -4.816  -11.208 1.00 60.45  ? 85  SER   A C   1 
ATOM   326  O O   . SER   A 1 42  ? -0.936  -5.908  -11.041 1.00 56.86  ? 85  SER   A O   1 
ATOM   327  C CB  . SER   A 1 42  ? -0.068  -3.282  -9.234  1.00 64.57  ? 85  SER   A CB  1 
ATOM   328  O OG  . SER   A 1 42  ? -0.305  -4.253  -8.225  1.00 73.28  ? 85  SER   A OG  1 
ATOM   329  N N   . LEU   A 1 43  ? 0.663   -4.621  -12.037 1.00 72.74  ? 86  LEU   A N   1 
ATOM   330  C CA  . LEU   A 1 43  ? 1.329   -5.703  -12.812 1.00 75.51  ? 86  LEU   A CA  1 
ATOM   331  C C   . LEU   A 1 43  ? 2.323   -6.444  -11.919 1.00 75.63  ? 86  LEU   A C   1 
ATOM   332  O O   . LEU   A 1 43  ? 3.323   -5.825  -11.539 1.00 81.89  ? 86  LEU   A O   1 
ATOM   333  C CB  . LEU   A 1 43  ? 2.024   -5.062  -14.009 1.00 75.14  ? 86  LEU   A CB  1 
ATOM   334  C CG  . LEU   A 1 43  ? 1.054   -4.562  -15.075 1.00 83.00  ? 86  LEU   A CG  1 
ATOM   335  C CD1 . LEU   A 1 43  ? 1.787   -3.867  -16.210 1.00 88.87  ? 86  LEU   A CD1 1 
ATOM   336  C CD2 . LEU   A 1 43  ? 0.215   -5.709  -15.619 1.00 83.54  ? 86  LEU   A CD2 1 
ATOM   337  N N   . VAL   A 1 44  ? 2.012   -7.687  -11.551 1.00 70.67  ? 87  VAL   A N   1 
ATOM   338  C CA  . VAL   A 1 44  ? 2.995   -8.656  -10.980 1.00 85.36  ? 87  VAL   A CA  1 
ATOM   339  C C   . VAL   A 1 44  ? 3.874   -9.092  -12.158 1.00 98.45  ? 87  VAL   A C   1 
ATOM   340  O O   . VAL   A 1 44  ? 3.351   -9.122  -13.301 1.00 99.14  ? 87  VAL   A O   1 
ATOM   341  C CB  . VAL   A 1 44  ? 2.301   -9.856  -10.302 1.00 88.86  ? 87  VAL   A CB  1 
ATOM   342  C CG1 . VAL   A 1 44  ? 3.298   -10.867 -9.759  1.00 84.71  ? 87  VAL   A CG1 1 
ATOM   343  C CG2 . VAL   A 1 44  ? 1.344   -9.412  -9.206  1.00 85.22  ? 87  VAL   A CG2 1 
ATOM   344  N N   . GLU   A 1 45  ? 5.155   -9.377  -11.910 1.00 109.63 ? 88  GLU   A N   1 
ATOM   345  C CA  . GLU   A 1 45  ? 6.179   -9.537  -12.978 1.00 110.27 ? 88  GLU   A CA  1 
ATOM   346  C C   . GLU   A 1 45  ? 7.122   -10.683 -12.612 1.00 100.98 ? 88  GLU   A C   1 
ATOM   347  O O   . GLU   A 1 45  ? 6.716   -11.792 -12.905 1.00 91.18  ? 88  GLU   A O   1 
ATOM   348  C CB  . GLU   A 1 45  ? 6.929   -8.219  -13.165 1.00 115.48 ? 88  GLU   A CB  1 
ATOM   349  C CG  . GLU   A 1 45  ? 6.129   -7.162  -13.913 1.00 113.42 ? 88  GLU   A CG  1 
ATOM   350  C CD  . GLU   A 1 45  ? 6.293   -7.248  -15.416 1.00 114.17 ? 88  GLU   A CD  1 
ATOM   351  O OE1 . GLU   A 1 45  ? 6.605   -8.360  -15.879 1.00 109.74 ? 88  GLU   A OE1 1 
ATOM   352  O OE2 . GLU   A 1 45  ? 6.140   -6.201  -16.110 1.00 110.40 ? 88  GLU   A OE2 1 
ATOM   353  N N   . GLY   B 2 7   ? -36.765 12.755  -11.483 1.00 88.99  ? 16  GLY   B N   1 
ATOM   354  C CA  . GLY   B 2 7   ? -35.786 12.797  -12.624 1.00 91.88  ? 16  GLY   B CA  1 
ATOM   355  C C   . GLY   B 2 7   ? -36.076 11.763  -13.716 1.00 98.38  ? 16  GLY   B C   1 
ATOM   356  O O   . GLY   B 2 7   ? -37.060 10.983  -13.576 1.00 94.56  ? 16  GLY   B O   1 
ATOM   357  N N   . GLU   B 2 8   ? -35.248 11.745  -14.774 1.00 91.07  ? 17  GLU   B N   1 
ATOM   358  C CA  . GLU   B 2 8   ? -35.287 10.740  -15.879 1.00 81.99  ? 17  GLU   B CA  1 
ATOM   359  C C   . GLU   B 2 8   ? -34.792 9.393   -15.337 1.00 78.00  ? 17  GLU   B C   1 
ATOM   360  O O   . GLU   B 2 8   ? -33.654 9.303   -14.871 1.00 73.32  ? 17  GLU   B O   1 
ATOM   361  C CB  . GLU   B 2 8   ? -34.445 11.185  -17.083 1.00 84.94  ? 17  GLU   B CB  1 
ATOM   362  C CG  . GLU   B 2 8   ? -34.597 10.265  -18.289 1.00 79.81  ? 17  GLU   B CG  1 
ATOM   363  C CD  . GLU   B 2 8   ? -33.951 10.716  -19.593 1.00 85.20  ? 17  GLU   B CD  1 
ATOM   364  O OE1 . GLU   B 2 8   ? -33.013 11.589  -19.546 1.00 66.37  ? 17  GLU   B OE1 1 
ATOM   365  O OE2 . GLU   B 2 8   ? -34.401 10.198  -20.670 1.00 75.95  ? 17  GLU   B OE2 1 
ATOM   366  N N   A THR   B 2 9   ? -35.630 8.355   -15.360 0.25 80.60  ? 18  THR   B N   1 
ATOM   367  N N   B THR   B 2 9   ? -35.666 8.386   -15.432 0.25 77.64  ? 18  THR   B N   1 
ATOM   368  N N   C THR   B 2 9   ? -35.630 8.355   -15.360 0.25 80.60  ? 18  THR   B N   1 
ATOM   369  N N   D THR   B 2 9   ? -35.666 8.386   -15.432 0.25 77.64  ? 18  THR   B N   1 
ATOM   370  C CA  A THR   B 2 9   ? -35.237 6.997   -14.895 0.25 80.99  ? 18  THR   B CA  1 
ATOM   371  C CA  B THR   B 2 9   ? -35.502 7.016   -14.882 0.25 75.80  ? 18  THR   B CA  1 
ATOM   372  C CA  C THR   B 2 9   ? -35.237 6.997   -14.895 0.25 80.99  ? 18  THR   B CA  1 
ATOM   373  C CA  D THR   B 2 9   ? -35.502 7.016   -14.882 0.25 75.80  ? 18  THR   B CA  1 
ATOM   374  C C   A THR   B 2 9   ? -35.369 5.974   -16.023 0.25 74.27  ? 18  THR   B C   1 
ATOM   375  C C   B THR   B 2 9   ? -35.314 5.994   -16.012 0.25 71.47  ? 18  THR   B C   1 
ATOM   376  C C   C THR   B 2 9   ? -35.369 5.974   -16.023 0.25 74.27  ? 18  THR   B C   1 
ATOM   377  C C   D THR   B 2 9   ? -35.314 5.994   -16.012 0.25 71.47  ? 18  THR   B C   1 
ATOM   378  O O   A THR   B 2 9   ? -35.457 4.779   -15.705 0.25 76.67  ? 18  THR   B O   1 
ATOM   379  O O   B THR   B 2 9   ? -35.108 4.817   -15.681 0.25 74.17  ? 18  THR   B O   1 
ATOM   380  O O   C THR   B 2 9   ? -35.457 4.779   -15.705 0.25 76.67  ? 18  THR   B O   1 
ATOM   381  O O   D THR   B 2 9   ? -35.108 4.817   -15.681 0.25 74.17  ? 18  THR   B O   1 
ATOM   382  C CB  A THR   B 2 9   ? -36.060 6.535   -13.690 0.25 84.03  ? 18  THR   B CB  1 
ATOM   383  C CB  B THR   B 2 9   ? -36.725 6.644   -14.036 0.25 74.19  ? 18  THR   B CB  1 
ATOM   384  C CB  C THR   B 2 9   ? -36.060 6.535   -13.690 0.25 84.03  ? 18  THR   B CB  1 
ATOM   385  C CB  D THR   B 2 9   ? -36.725 6.644   -14.036 0.25 74.19  ? 18  THR   B CB  1 
ATOM   386  O OG1 A THR   B 2 9   ? -35.800 7.435   -12.613 0.25 88.45  ? 18  THR   B OG1 1 
ATOM   387  O OG1 B THR   B 2 9   ? -37.880 6.932   -14.821 0.25 69.39  ? 18  THR   B OG1 1 
ATOM   388  O OG1 C THR   B 2 9   ? -35.800 7.435   -12.613 0.25 88.45  ? 18  THR   B OG1 1 
ATOM   389  O OG1 D THR   B 2 9   ? -37.880 6.932   -14.821 0.25 69.39  ? 18  THR   B OG1 1 
ATOM   390  C CG2 A THR   B 2 9   ? -35.718 5.118   -13.286 0.25 81.17  ? 18  THR   B CG2 1 
ATOM   391  C CG2 B THR   B 2 9   ? -36.806 7.407   -12.732 0.25 76.25  ? 18  THR   B CG2 1 
ATOM   392  C CG2 C THR   B 2 9   ? -35.718 5.118   -13.286 0.25 81.17  ? 18  THR   B CG2 1 
ATOM   393  C CG2 D THR   B 2 9   ? -36.806 7.407   -12.732 0.25 76.25  ? 18  THR   B CG2 1 
ATOM   394  N N   . THR   B 2 10  ? -35.373 6.422   -17.279 1.00 69.22  ? 19  THR   B N   1 
ATOM   395  C CA  . THR   B 2 10  ? -35.406 5.511   -18.450 1.00 69.70  ? 19  THR   B CA  1 
ATOM   396  C C   . THR   B 2 10  ? -34.125 4.669   -18.431 1.00 60.82  ? 19  THR   B C   1 
ATOM   397  O O   . THR   B 2 10  ? -33.044 5.247   -18.239 1.00 56.73  ? 19  THR   B O   1 
ATOM   398  C CB  . THR   B 2 10  ? -35.566 6.236   -19.798 1.00 64.17  ? 19  THR   B CB  1 
ATOM   399  O OG1 . THR   B 2 10  ? -36.414 7.383   -19.697 1.00 77.84  ? 19  THR   B OG1 1 
ATOM   400  C CG2 . THR   B 2 10  ? -36.133 5.313   -20.856 1.00 60.73  ? 19  THR   B CG2 1 
ATOM   401  N N   . ASP   B 2 11  ? -34.266 3.357   -18.609 1.00 54.57  ? 20  ASP   B N   1 
ATOM   402  C CA  . ASP   B 2 11  ? -33.136 2.422   -18.838 1.00 56.80  ? 20  ASP   B CA  1 
ATOM   403  C C   . ASP   B 2 11  ? -32.194 3.024   -19.885 1.00 57.79  ? 20  ASP   B C   1 
ATOM   404  O O   . ASP   B 2 11  ? -32.666 3.722   -20.821 1.00 58.92  ? 20  ASP   B O   1 
ATOM   405  C CB  . ASP   B 2 11  ? -33.621 1.026   -19.258 1.00 51.69  ? 20  ASP   B CB  1 
ATOM   406  C CG  . ASP   B 2 11  ? -34.231 0.186   -18.144 1.00 57.16  ? 20  ASP   B CG  1 
ATOM   407  O OD1 . ASP   B 2 11  ? -34.202 0.639   -17.005 1.00 56.45  ? 20  ASP   B OD1 1 
ATOM   408  O OD2 . ASP   B 2 11  ? -34.743 -0.932  -18.430 1.00 73.76  ? 20  ASP   B OD2 1 
ATOM   409  N N   . GLY   B 2 12  ? -30.892 2.797   -19.716 1.00 51.00  ? 21  GLY   B N   1 
ATOM   410  C CA  . GLY   B 2 12  ? -29.883 3.124   -20.734 1.00 49.47  ? 21  GLY   B CA  1 
ATOM   411  C C   . GLY   B 2 12  ? -28.623 3.685   -20.131 1.00 45.58  ? 21  GLY   B C   1 
ATOM   412  O O   . GLY   B 2 12  ? -28.420 3.610   -18.902 1.00 43.67  ? 21  GLY   B O   1 
ATOM   413  N N   . VAL   B 2 13  ? -27.812 4.294   -20.965 1.00 44.68  ? 22  VAL   B N   1 
ATOM   414  C CA  . VAL   B 2 13  ? -26.486 4.818   -20.538 1.00 43.66  ? 22  VAL   B CA  1 
ATOM   415  C C   . VAL   B 2 13  ? -26.543 6.340   -20.409 1.00 45.34  ? 22  VAL   B C   1 
ATOM   416  O O   . VAL   B 2 13  ? -27.307 6.980   -21.162 1.00 49.37  ? 22  VAL   B O   1 
ATOM   417  C CB  . VAL   B 2 13  ? -25.396 4.319   -21.481 1.00 44.48  ? 22  VAL   B CB  1 
ATOM   418  C CG1 . VAL   B 2 13  ? -25.600 4.812   -22.916 1.00 51.40  ? 22  VAL   B CG1 1 
ATOM   419  C CG2 . VAL   B 2 13  ? -24.012 4.677   -20.954 1.00 54.37  ? 22  VAL   B CG2 1 
ATOM   420  N N   . TYR   B 2 14  ? -25.817 6.875   -19.426 1.00 50.21  ? 23  TYR   B N   1 
ATOM   421  C CA  . TYR   B 2 14  ? -25.849 8.302   -19.043 1.00 46.39  ? 23  TYR   B CA  1 
ATOM   422  C C   . TYR   B 2 14  ? -24.440 8.812   -18.780 1.00 45.23  ? 23  TYR   B C   1 
ATOM   423  O O   . TYR   B 2 14  ? -23.592 8.091   -18.222 1.00 48.68  ? 23  TYR   B O   1 
ATOM   424  C CB  . TYR   B 2 14  ? -26.681 8.505   -17.780 1.00 44.63  ? 23  TYR   B CB  1 
ATOM   425  C CG  . TYR   B 2 14  ? -28.168 8.306   -17.919 1.00 43.43  ? 23  TYR   B CG  1 
ATOM   426  C CD1 . TYR   B 2 14  ? -28.686 7.035   -18.083 1.00 43.80  ? 23  TYR   B CD1 1 
ATOM   427  C CD2 . TYR   B 2 14  ? -29.067 9.364   -17.816 1.00 43.72  ? 23  TYR   B CD2 1 
ATOM   428  C CE1 . TYR   B 2 14  ? -30.044 6.797   -18.167 1.00 44.55  ? 23  TYR   B CE1 1 
ATOM   429  C CE2 . TYR   B 2 14  ? -30.438 9.148   -17.901 1.00 42.16  ? 23  TYR   B CE2 1 
ATOM   430  C CZ  . TYR   B 2 14  ? -30.925 7.867   -18.076 1.00 49.57  ? 23  TYR   B CZ  1 
ATOM   431  O OH  . TYR   B 2 14  ? -32.257 7.600   -18.130 1.00 50.52  ? 23  TYR   B OH  1 
ATOM   432  N N   . ARG   B 2 15  ? -24.224 10.080  -19.099 1.00 44.10  ? 24  ARG   B N   1 
ATOM   433  C CA  . ARG   B 2 15  ? -22.983 10.818  -18.743 1.00 43.47  ? 24  ARG   B CA  1 
ATOM   434  C C   . ARG   B 2 15  ? -23.088 11.339  -17.321 1.00 44.40  ? 24  ARG   B C   1 
ATOM   435  O O   . ARG   B 2 15  ? -24.164 11.757  -16.922 1.00 48.84  ? 24  ARG   B O   1 
ATOM   436  C CB  . ARG   B 2 15  ? -22.756 12.050  -19.624 1.00 44.99  ? 24  ARG   B CB  1 
ATOM   437  C CG  . ARG   B 2 15  ? -22.802 11.760  -21.115 1.00 47.11  ? 24  ARG   B CG  1 
ATOM   438  C CD  . ARG   B 2 15  ? -22.698 12.979  -22.004 1.00 49.99  ? 24  ARG   B CD  1 
ATOM   439  N NE  . ARG   B 2 15  ? -22.905 12.521  -23.387 1.00 50.85  ? 24  ARG   B NE  1 
ATOM   440  C CZ  . ARG   B 2 15  ? -21.947 12.249  -24.273 1.00 52.19  ? 24  ARG   B CZ  1 
ATOM   441  N NH1 . ARG   B 2 15  ? -20.671 12.414  -23.970 1.00 50.26  ? 24  ARG   B NH1 1 
ATOM   442  N NH2 . ARG   B 2 15  ? -22.282 11.819  -25.480 1.00 61.96  ? 24  ARG   B NH2 1 
ATOM   443  N N   . VAL   B 2 16  ? -21.968 11.342  -16.618 1.00 48.19  ? 25  VAL   B N   1 
ATOM   444  C CA  . VAL   B 2 16  ? -21.851 11.916  -15.268 1.00 46.12  ? 25  VAL   B CA  1 
ATOM   445  C C   . VAL   B 2 16  ? -21.030 13.204  -15.396 1.00 49.77  ? 25  VAL   B C   1 
ATOM   446  O O   . VAL   B 2 16  ? -19.835 13.118  -15.698 1.00 42.19  ? 25  VAL   B O   1 
ATOM   447  C CB  . VAL   B 2 16  ? -21.242 10.892  -14.291 1.00 54.04  ? 25  VAL   B CB  1 
ATOM   448  C CG1 . VAL   B 2 16  ? -21.020 11.525  -12.930 1.00 50.73  ? 25  VAL   B CG1 1 
ATOM   449  C CG2 . VAL   B 2 16  ? -22.113 9.643   -14.156 1.00 46.57  ? 25  VAL   B CG2 1 
ATOM   450  N N   . MET   B 2 17  ? -21.695 14.343  -15.168 1.00 49.96  ? 26  MET   B N   1 
ATOM   451  C CA  . MET   B 2 17  ? -21.159 15.712  -15.358 1.00 54.48  ? 26  MET   B CA  1 
ATOM   452  C C   . MET   B 2 17  ? -20.987 16.389  -14.002 1.00 52.95  ? 26  MET   B C   1 
ATOM   453  O O   . MET   B 2 17  ? -21.770 16.077  -13.085 1.00 50.94  ? 26  MET   B O   1 
ATOM   454  C CB  . MET   B 2 17  ? -22.144 16.545  -16.175 1.00 52.81  ? 26  MET   B CB  1 
ATOM   455  C CG  . MET   B 2 17  ? -22.598 15.874  -17.450 1.00 52.98  ? 26  MET   B CG  1 
ATOM   456  S SD  . MET   B 2 17  ? -21.298 15.543  -18.682 1.00 55.27  ? 26  MET   B SD  1 
ATOM   457  C CE  . MET   B 2 17  ? -20.398 17.092  -18.712 1.00 64.17  ? 26  MET   B CE  1 
ATOM   458  N N   . THR   B 2 18  ? -20.035 17.317  -13.906 1.00 59.93  ? 27  THR   B N   1 
ATOM   459  C CA  . THR   B 2 18  ? -19.933 18.291  -12.786 1.00 64.06  ? 27  THR   B CA  1 
ATOM   460  C C   . THR   B 2 18  ? -19.768 19.687  -13.378 1.00 64.21  ? 27  THR   B C   1 
ATOM   461  O O   . THR   B 2 18  ? -19.156 19.780  -14.460 1.00 57.61  ? 27  THR   B O   1 
ATOM   462  C CB  . THR   B 2 18  ? -18.756 17.983  -11.854 1.00 72.94  ? 27  THR   B CB  1 
ATOM   463  O OG1 . THR   B 2 18  ? -18.692 19.018  -10.871 1.00 70.38  ? 27  THR   B OG1 1 
ATOM   464  C CG2 . THR   B 2 18  ? -17.424 17.882  -12.570 1.00 68.31  ? 27  THR   B CG2 1 
ATOM   465  N N   . ARG   B 2 19  ? -20.271 20.717  -12.692 1.00 66.26  ? 28  ARG   B N   1 
ATOM   466  C CA  . ARG   B 2 19  ? -20.028 22.142  -13.043 1.00 73.05  ? 28  ARG   B CA  1 
ATOM   467  C C   . ARG   B 2 19  ? -19.105 22.807  -12.015 1.00 72.53  ? 28  ARG   B C   1 
ATOM   468  O O   . ARG   B 2 19  ? -18.721 23.973  -12.232 1.00 72.75  ? 28  ARG   B O   1 
ATOM   469  C CB  . ARG   B 2 19  ? -21.358 22.883  -13.191 1.00 79.47  ? 28  ARG   B CB  1 
ATOM   470  C CG  . ARG   B 2 19  ? -22.012 22.630  -14.541 1.00 92.77  ? 28  ARG   B CG  1 
ATOM   471  C CD  . ARG   B 2 19  ? -22.796 23.803  -15.081 1.00 97.67  ? 28  ARG   B CD  1 
ATOM   472  N NE  . ARG   B 2 19  ? -23.959 23.338  -15.822 1.00 108.56 ? 28  ARG   B NE  1 
ATOM   473  C CZ  . ARG   B 2 19  ? -25.055 22.812  -15.272 1.00 114.31 ? 28  ARG   B CZ  1 
ATOM   474  N NH1 . ARG   B 2 19  ? -25.145 22.664  -13.958 1.00 115.20 ? 28  ARG   B NH1 1 
ATOM   475  N NH2 . ARG   B 2 19  ? -26.054 22.416  -16.044 1.00 110.28 ? 28  ARG   B NH2 1 
ATOM   476  N N   . ARG   B 2 20  ? -18.708 22.089  -10.968 1.00 86.48  ? 29  ARG   B N   1 
ATOM   477  C CA  . ARG   B 2 20  ? -17.846 22.645  -9.892  1.00 100.93 ? 29  ARG   B CA  1 
ATOM   478  C C   . ARG   B 2 20  ? -16.543 23.142  -10.526 1.00 94.23  ? 29  ARG   B C   1 
ATOM   479  O O   . ARG   B 2 20  ? -15.932 24.045  -9.945  1.00 104.67 ? 29  ARG   B O   1 
ATOM   480  C CB  . ARG   B 2 20  ? -17.592 21.613  -8.785  1.00 110.08 ? 29  ARG   B CB  1 
ATOM   481  C CG  . ARG   B 2 20  ? -17.418 22.225  -7.400  1.00 116.43 ? 29  ARG   B CG  1 
ATOM   482  C CD  . ARG   B 2 20  ? -17.176 21.185  -6.326  1.00 128.90 ? 29  ARG   B CD  1 
ATOM   483  N NE  . ARG   B 2 20  ? -16.266 20.151  -6.803  1.00 146.48 ? 29  ARG   B NE  1 
ATOM   484  C CZ  . ARG   B 2 20  ? -14.945 20.288  -6.943  1.00 148.04 ? 29  ARG   B CZ  1 
ATOM   485  N NH1 . ARG   B 2 20  ? -14.346 21.427  -6.633  1.00 153.63 ? 29  ARG   B NH1 1 
ATOM   486  N NH2 . ARG   B 2 20  ? -14.221 19.277  -7.397  1.00 138.87 ? 29  ARG   B NH2 1 
ATOM   487  N N   . LEU   B 2 21  ? -16.156 22.599  -11.684 1.00 87.86  ? 30  LEU   B N   1 
ATOM   488  C CA  . LEU   B 2 21  ? -14.887 22.957  -12.378 1.00 90.43  ? 30  LEU   B CA  1 
ATOM   489  C C   . LEU   B 2 21  ? -15.142 24.005  -13.473 1.00 82.44  ? 30  LEU   B C   1 
ATOM   490  O O   . LEU   B 2 21  ? -16.240 24.613  -13.494 1.00 80.66  ? 30  LEU   B O   1 
ATOM   491  C CB  . LEU   B 2 21  ? -14.251 21.678  -12.936 1.00 91.27  ? 30  LEU   B CB  1 
ATOM   492  C CG  . LEU   B 2 21  ? -13.210 21.017  -12.038 1.00 87.73  ? 30  LEU   B CG  1 
ATOM   493  C CD1 . LEU   B 2 21  ? -13.777 20.764  -10.652 1.00 96.44  ? 30  LEU   B CD1 1 
ATOM   494  C CD2 . LEU   B 2 21  ? -12.712 19.718  -12.654 1.00 93.05  ? 30  LEU   B CD2 1 
ATOM   495  N N   . LEU   B 2 22  ? -14.129 24.264  -14.307 1.00 79.69  ? 31  LEU   B N   1 
ATOM   496  C CA  . LEU   B 2 22  ? -14.263 25.133  -15.504 1.00 82.59  ? 31  LEU   B CA  1 
ATOM   497  C C   . LEU   B 2 22  ? -15.258 24.493  -16.474 1.00 80.03  ? 31  LEU   B C   1 
ATOM   498  O O   . LEU   B 2 22  ? -15.224 23.244  -16.594 1.00 81.98  ? 31  LEU   B O   1 
ATOM   499  C CB  . LEU   B 2 22  ? -12.904 25.310  -16.174 1.00 74.65  ? 31  LEU   B CB  1 
ATOM   500  C CG  . LEU   B 2 22  ? -12.931 26.284  -17.343 1.00 76.19  ? 31  LEU   B CG  1 
ATOM   501  C CD1 . LEU   B 2 22  ? -13.041 27.716  -16.837 1.00 73.36  ? 31  LEU   B CD1 1 
ATOM   502  C CD2 . LEU   B 2 22  ? -11.705 26.108  -18.230 1.00 79.32  ? 31  LEU   B CD2 1 
ATOM   503  N N   . GLY   B 2 23  ? -16.110 25.303  -17.120 1.00 68.53  ? 32  GLY   B N   1 
ATOM   504  C CA  . GLY   B 2 23  ? -17.242 24.807  -17.925 1.00 62.38  ? 32  GLY   B CA  1 
ATOM   505  C C   . GLY   B 2 23  ? -17.977 23.653  -17.240 1.00 64.94  ? 32  GLY   B C   1 
ATOM   506  O O   . GLY   B 2 23  ? -18.019 23.603  -15.985 1.00 65.01  ? 32  GLY   B O   1 
ATOM   507  N N   . SER   B 2 24  ? -18.549 22.742  -18.031 1.00 62.13  ? 33  SER   B N   1 
ATOM   508  C CA  . SER   B 2 24  ? -19.168 21.477  -17.558 1.00 62.45  ? 33  SER   B CA  1 
ATOM   509  C C   . SER   B 2 24  ? -18.286 20.312  -18.010 1.00 58.45  ? 33  SER   B C   1 
ATOM   510  O O   . SER   B 2 24  ? -18.026 20.220  -19.192 1.00 55.57  ? 33  SER   B O   1 
ATOM   511  C CB  . SER   B 2 24  ? -20.565 21.359  -18.057 1.00 60.95  ? 33  SER   B CB  1 
ATOM   512  O OG  . SER   B 2 24  ? -21.226 22.621  -17.971 1.00 66.03  ? 33  SER   B OG  1 
ATOM   513  N N   . THR   B 2 25  ? -17.819 19.489  -17.078 1.00 60.59  ? 34  THR   B N   1 
ATOM   514  C CA  . THR   B 2 25  ? -16.824 18.403  -17.307 1.00 55.48  ? 34  THR   B CA  1 
ATOM   515  C C   . THR   B 2 25  ? -17.483 17.030  -17.110 1.00 52.72  ? 34  THR   B C   1 
ATOM   516  O O   . THR   B 2 25  ? -18.154 16.833  -16.079 1.00 54.76  ? 34  THR   B O   1 
ATOM   517  C CB  . THR   B 2 25  ? -15.654 18.545  -16.336 1.00 54.96  ? 34  THR   B CB  1 
ATOM   518  O OG1 . THR   B 2 25  ? -15.078 19.836  -16.541 1.00 62.68  ? 34  THR   B OG1 1 
ATOM   519  C CG2 . THR   B 2 25  ? -14.605 17.476  -16.526 1.00 60.81  ? 34  THR   B CG2 1 
ATOM   520  N N   . GLN   B 2 26  ? -17.285 16.118  -18.056 1.00 53.70  ? 35  GLN   B N   1 
ATOM   521  C CA  . GLN   B 2 26  ? -17.728 14.710  -17.924 1.00 59.32  ? 35  GLN   B CA  1 
ATOM   522  C C   . GLN   B 2 26  ? -16.682 13.950  -17.094 1.00 61.84  ? 35  GLN   B C   1 
ATOM   523  O O   . GLN   B 2 26  ? -15.540 13.793  -17.572 1.00 62.96  ? 35  GLN   B O   1 
ATOM   524  C CB  . GLN   B 2 26  ? -17.926 14.076  -19.296 1.00 57.94  ? 35  GLN   B CB  1 
ATOM   525  C CG  . GLN   B 2 26  ? -18.368 12.629  -19.198 1.00 56.74  ? 35  GLN   B CG  1 
ATOM   526  C CD  . GLN   B 2 26  ? -18.763 12.062  -20.526 1.00 55.75  ? 35  GLN   B CD  1 
ATOM   527  O OE1 . GLN   B 2 26  ? -19.350 12.742  -21.362 1.00 62.20  ? 35  GLN   B OE1 1 
ATOM   528  N NE2 . GLN   B 2 26  ? -18.480 10.785  -20.712 1.00 57.47  ? 35  GLN   B NE2 1 
ATOM   529  N N   . VAL   B 2 27  ? -17.046 13.521  -15.887 1.00 54.70  ? 36  VAL   B N   1 
ATOM   530  C CA  . VAL   B 2 27  ? -16.120 12.814  -14.957 1.00 55.66  ? 36  VAL   B CA  1 
ATOM   531  C C   . VAL   B 2 27  ? -16.343 11.305  -15.145 1.00 50.80  ? 36  VAL   B C   1 
ATOM   532  O O   . VAL   B 2 27  ? -15.450 10.527  -14.803 1.00 49.39  ? 36  VAL   B O   1 
ATOM   533  C CB  . VAL   B 2 27  ? -16.310 13.301  -13.504 1.00 56.62  ? 36  VAL   B CB  1 
ATOM   534  C CG1 . VAL   B 2 27  ? -15.920 14.756  -13.356 1.00 64.27  ? 36  VAL   B CG1 1 
ATOM   535  C CG2 . VAL   B 2 27  ? -17.733 13.136  -13.027 1.00 62.39  ? 36  VAL   B CG2 1 
ATOM   536  N N   . GLY   B 2 28  ? -17.462 10.890  -15.745 1.00 51.91  ? 37  GLY   B N   1 
ATOM   537  C CA  . GLY   B 2 28  ? -17.658 9.458   -16.017 1.00 44.87  ? 37  GLY   B CA  1 
ATOM   538  C C   . GLY   B 2 28  ? -18.982 9.163   -16.664 1.00 46.88  ? 37  GLY   B C   1 
ATOM   539  O O   . GLY   B 2 28  ? -19.607 10.096  -17.176 1.00 46.49  ? 37  GLY   B O   1 
ATOM   540  N N   . VAL   B 2 29  ? -19.399 7.900   -16.570 1.00 40.40  ? 38  VAL   B N   1 
ATOM   541  C CA  . VAL   B 2 29  ? -20.566 7.298   -17.285 1.00 44.08  ? 38  VAL   B CA  1 
ATOM   542  C C   . VAL   B 2 29  ? -21.275 6.317   -16.341 1.00 43.03  ? 38  VAL   B C   1 
ATOM   543  O O   . VAL   B 2 29  ? -20.654 5.883   -15.363 1.00 42.47  ? 38  VAL   B O   1 
ATOM   544  C CB  . VAL   B 2 29  ? -20.093 6.595   -18.581 1.00 42.78  ? 38  VAL   B CB  1 
ATOM   545  C CG1 . VAL   B 2 29  ? -21.228 6.025   -19.398 1.00 42.88  ? 38  VAL   B CG1 1 
ATOM   546  C CG2 . VAL   B 2 29  ? -19.247 7.518   -19.447 1.00 45.41  ? 38  VAL   B CG2 1 
ATOM   547  N N   . GLY   B 2 30  ? -22.535 5.991   -16.609 1.00 38.81  ? 39  GLY   B N   1 
ATOM   548  C CA  . GLY   B 2 30  ? -23.264 4.979   -15.845 1.00 37.27  ? 39  GLY   B CA  1 
ATOM   549  C C   . GLY   B 2 30  ? -24.428 4.376   -16.584 1.00 34.82  ? 39  GLY   B C   1 
ATOM   550  O O   . GLY   B 2 30  ? -24.698 4.751   -17.721 1.00 43.11  ? 39  GLY   B O   1 
ATOM   551  N N   . VAL   B 2 31  ? -25.016 3.363   -15.981 1.00 39.83  ? 40  VAL   B N   1 
ATOM   552  C CA  . VAL   B 2 31  ? -26.094 2.510   -16.555 1.00 39.83  ? 40  VAL   B CA  1 
ATOM   553  C C   . VAL   B 2 31  ? -27.278 2.667   -15.638 1.00 41.84  ? 40  VAL   B C   1 
ATOM   554  O O   . VAL   B 2 31  ? -27.065 2.527   -14.408 1.00 42.37  ? 40  VAL   B O   1 
ATOM   555  C CB  . VAL   B 2 31  ? -25.711 1.018   -16.577 1.00 46.93  ? 40  VAL   B CB  1 
ATOM   556  C CG1 . VAL   B 2 31  ? -26.885 0.143   -17.011 1.00 45.91  ? 40  VAL   B CG1 1 
ATOM   557  C CG2 . VAL   B 2 31  ? -24.460 0.757   -17.399 1.00 49.76  ? 40  VAL   B CG2 1 
ATOM   558  N N   . MET   B 2 32  ? -28.454 2.879   -16.222 1.00 47.54  ? 41  MET   B N   1 
ATOM   559  C CA  . MET   B 2 32  ? -29.744 2.876   -15.512 1.00 43.35  ? 41  MET   B CA  1 
ATOM   560  C C   . MET   B 2 32  ? -30.469 1.602   -15.934 1.00 42.46  ? 41  MET   B C   1 
ATOM   561  O O   . MET   B 2 32  ? -30.640 1.411   -17.131 1.00 46.27  ? 41  MET   B O   1 
ATOM   562  C CB  . MET   B 2 32  ? -30.589 4.097   -15.888 1.00 48.00  ? 41  MET   B CB  1 
ATOM   563  C CG  . MET   B 2 32  ? -31.840 4.238   -15.022 1.00 47.48  ? 41  MET   B CG  1 
ATOM   564  S SD  . MET   B 2 32  ? -31.411 4.874   -13.355 1.00 52.10  ? 41  MET   B SD  1 
ATOM   565  C CE  . MET   B 2 32  ? -30.769 6.488   -13.787 1.00 52.37  ? 41  MET   B CE  1 
ATOM   566  N N   . GLN   B 2 33  ? -30.859 0.776   -14.979 1.00 38.24  ? 42  GLN   B N   1 
ATOM   567  C CA  . GLN   B 2 33  ? -31.578 -0.494  -15.203 1.00 46.44  ? 42  GLN   B CA  1 
ATOM   568  C C   . GLN   B 2 33  ? -32.432 -0.732  -13.975 1.00 45.94  ? 42  GLN   B C   1 
ATOM   569  O O   . GLN   B 2 33  ? -31.895 -0.566  -12.860 1.00 50.40  ? 42  GLN   B O   1 
ATOM   570  C CB  . GLN   B 2 33  ? -30.618 -1.674  -15.415 1.00 48.79  ? 42  GLN   B CB  1 
ATOM   571  C CG  . GLN   B 2 33  ? -31.385 -2.936  -15.828 1.00 52.55  ? 42  GLN   B CG  1 
ATOM   572  C CD  . GLN   B 2 33  ? -30.517 -4.067  -16.327 1.00 56.98  ? 42  GLN   B CD  1 
ATOM   573  O OE1 . GLN   B 2 33  ? -30.554 -5.169  -15.791 1.00 66.81  ? 42  GLN   B OE1 1 
ATOM   574  N NE2 . GLN   B 2 33  ? -29.705 -3.799  -17.336 1.00 56.49  ? 42  GLN   B NE2 1 
ATOM   575  N N   . GLU   B 2 34  ? -33.697 -1.064  -14.172 1.00 55.53  ? 43  GLU   B N   1 
ATOM   576  C CA  . GLU   B 2 34  ? -34.651 -1.411  -13.086 1.00 54.20  ? 43  GLU   B CA  1 
ATOM   577  C C   . GLU   B 2 34  ? -34.650 -0.311  -12.016 1.00 52.05  ? 43  GLU   B C   1 
ATOM   578  O O   . GLU   B 2 34  ? -34.612 -0.627  -10.840 1.00 53.48  ? 43  GLU   B O   1 
ATOM   579  C CB  . GLU   B 2 34  ? -34.300 -2.790  -12.534 1.00 59.20  ? 43  GLU   B CB  1 
ATOM   580  C CG  . GLU   B 2 34  ? -34.297 -3.886  -13.596 1.00 63.96  ? 43  GLU   B CG  1 
ATOM   581  C CD  . GLU   B 2 34  ? -33.590 -5.176  -13.191 1.00 63.85  ? 43  GLU   B CD  1 
ATOM   582  O OE1 . GLU   B 2 34  ? -34.012 -5.812  -12.214 1.00 72.68  ? 43  GLU   B OE1 1 
ATOM   583  O OE2 . GLU   B 2 34  ? -32.614 -5.544  -13.856 1.00 77.93  ? 43  GLU   B OE2 1 
ATOM   584  N N   . GLY   B 2 35  ? -34.706 0.950   -12.426 1.00 56.16  ? 44  GLY   B N   1 
ATOM   585  C CA  . GLY   B 2 35  ? -34.680 2.121   -11.530 1.00 52.79  ? 44  GLY   B CA  1 
ATOM   586  C C   . GLY   B 2 35  ? -33.422 2.263   -10.669 1.00 49.44  ? 44  GLY   B C   1 
ATOM   587  O O   . GLY   B 2 35  ? -33.469 3.062   -9.714  1.00 51.28  ? 44  GLY   B O   1 
ATOM   588  N N   . VAL   B 2 36  ? -32.313 1.590   -10.969 1.00 43.62  ? 45  VAL   B N   1 
ATOM   589  C CA  . VAL   B 2 36  ? -31.029 1.784   -10.224 1.00 39.78  ? 45  VAL   B CA  1 
ATOM   590  C C   . VAL   B 2 36  ? -29.993 2.327   -11.189 1.00 40.26  ? 45  VAL   B C   1 
ATOM   591  O O   . VAL   B 2 36  ? -29.944 1.834   -12.340 1.00 46.40  ? 45  VAL   B O   1 
ATOM   592  C CB  . VAL   B 2 36  ? -30.540 0.488   -9.547  1.00 45.72  ? 45  VAL   B CB  1 
ATOM   593  C CG1 . VAL   B 2 36  ? -29.164 0.658   -8.895  1.00 40.66  ? 45  VAL   B CG1 1 
ATOM   594  C CG2 . VAL   B 2 36  ? -31.592 -0.060  -8.570  1.00 43.44  ? 45  VAL   B CG2 1 
ATOM   595  N N   . PHE   B 2 37  ? -29.179 3.273   -10.717 1.00 37.55  ? 46  PHE   B N   1 
ATOM   596  C CA  . PHE   B 2 37  ? -28.046 3.844   -11.464 1.00 41.46  ? 46  PHE   B CA  1 
ATOM   597  C C   . PHE   B 2 37  ? -26.717 3.217   -11.005 1.00 40.81  ? 46  PHE   B C   1 
ATOM   598  O O   . PHE   B 2 37  ? -26.428 3.187   -9.801  1.00 43.73  ? 46  PHE   B O   1 
ATOM   599  C CB  . PHE   B 2 37  ? -27.979 5.355   -11.294 1.00 38.85  ? 46  PHE   B CB  1 
ATOM   600  C CG  . PHE   B 2 37  ? -27.012 5.981   -12.265 1.00 37.28  ? 46  PHE   B CG  1 
ATOM   601  C CD1 . PHE   B 2 37  ? -27.190 5.811   -13.629 1.00 41.73  ? 46  PHE   B CD1 1 
ATOM   602  C CD2 . PHE   B 2 37  ? -25.914 6.685   -11.819 1.00 36.05  ? 46  PHE   B CD2 1 
ATOM   603  C CE1 . PHE   B 2 37  ? -26.315 6.389   -14.537 1.00 43.39  ? 46  PHE   B CE1 1 
ATOM   604  C CE2 . PHE   B 2 37  ? -25.021 7.233   -12.725 1.00 39.93  ? 46  PHE   B CE2 1 
ATOM   605  C CZ  . PHE   B 2 37  ? -25.230 7.103   -14.078 1.00 38.65  ? 46  PHE   B CZ  1 
ATOM   606  N N   . HIS   B 2 38  ? -25.954 2.700   -11.957 1.00 41.76  ? 47  HIS   B N   1 
ATOM   607  C CA  . HIS   B 2 38  ? -24.731 1.883   -11.704 1.00 38.78  ? 47  HIS   B CA  1 
ATOM   608  C C   . HIS   B 2 38  ? -23.507 2.621   -12.248 1.00 37.71  ? 47  HIS   B C   1 
ATOM   609  O O   . HIS   B 2 38  ? -23.472 2.936   -13.444 1.00 39.33  ? 47  HIS   B O   1 
ATOM   610  C CB  . HIS   B 2 38  ? -24.858 0.515   -12.347 1.00 40.78  ? 47  HIS   B CB  1 
ATOM   611  C CG  . HIS   B 2 38  ? -26.077 -0.265  -11.985 1.00 41.54  ? 47  HIS   B CG  1 
ATOM   612  N ND1 . HIS   B 2 38  ? -27.313 0.001   -12.547 1.00 42.25  ? 47  HIS   B ND1 1 
ATOM   613  C CD2 . HIS   B 2 38  ? -26.252 -1.340  -11.187 1.00 43.31  ? 47  HIS   B CD2 1 
ATOM   614  C CE1 . HIS   B 2 38  ? -28.197 -0.868  -12.085 1.00 42.60  ? 47  HIS   B CE1 1 
ATOM   615  N NE2 . HIS   B 2 38  ? -27.582 -1.693  -11.247 1.00 41.88  ? 47  HIS   B NE2 1 
ATOM   616  N N   . THR   B 2 39  ? -22.538 2.942   -11.420 1.00 40.41  ? 48  THR   B N   1 
ATOM   617  C CA  . THR   B 2 39  ? -21.275 3.515   -11.936 1.00 43.86  ? 48  THR   B CA  1 
ATOM   618  C C   . THR   B 2 39  ? -20.097 2.946   -11.136 1.00 41.98  ? 48  THR   B C   1 
ATOM   619  O O   . THR   B 2 39  ? -20.313 2.037   -10.305 1.00 37.13  ? 48  THR   B O   1 
ATOM   620  C CB  . THR   B 2 39  ? -21.428 5.030   -11.990 1.00 46.67  ? 48  THR   B CB  1 
ATOM   621  O OG1 . THR   B 2 39  ? -20.346 5.647   -12.692 1.00 47.26  ? 48  THR   B OG1 1 
ATOM   622  C CG2 . THR   B 2 39  ? -21.554 5.621   -10.604 1.00 51.17  ? 48  THR   B CG2 1 
ATOM   623  N N   . MET   B 2 40  ? -18.922 3.531   -11.336 1.00 41.99  ? 49  MET   B N   1 
ATOM   624  C CA  . MET   B 2 40  ? -17.679 3.165   -10.618 1.00 45.65  ? 49  MET   B CA  1 
ATOM   625  C C   . MET   B 2 40  ? -17.458 4.179   -9.493  1.00 46.71  ? 49  MET   B C   1 
ATOM   626  O O   . MET   B 2 40  ? -17.733 5.362   -9.681  1.00 47.69  ? 49  MET   B O   1 
ATOM   627  C CB  . MET   B 2 40  ? -16.499 3.139   -11.593 1.00 43.76  ? 49  MET   B CB  1 
ATOM   628  C CG  . MET   B 2 40  ? -16.801 2.301   -12.839 1.00 44.47  ? 49  MET   B CG  1 
ATOM   629  S SD  . MET   B 2 40  ? -15.407 1.463   -13.543 1.00 59.21  ? 49  MET   B SD  1 
ATOM   630  C CE  . MET   B 2 40  ? -15.285 -0.001  -12.513 1.00 53.56  ? 49  MET   B CE  1 
ATOM   631  N N   A TRP   B 2 41  ? -16.976 3.698   -8.343  0.25 47.60  ? 50  TRP   B N   1 
ATOM   632  N N   B TRP   B 2 41  ? -16.963 3.706   -8.347  0.25 44.97  ? 50  TRP   B N   1 
ATOM   633  N N   C TRP   B 2 41  ? -16.976 3.698   -8.343  0.25 47.60  ? 50  TRP   B N   1 
ATOM   634  N N   D TRP   B 2 41  ? -16.963 3.706   -8.347  0.25 44.97  ? 50  TRP   B N   1 
ATOM   635  C CA  A TRP   B 2 41  ? -16.752 4.494   -7.107  0.25 47.70  ? 50  TRP   B CA  1 
ATOM   636  C CA  B TRP   B 2 41  ? -16.784 4.517   -7.115  0.25 43.48  ? 50  TRP   B CA  1 
ATOM   637  C CA  C TRP   B 2 41  ? -16.752 4.494   -7.107  0.25 47.70  ? 50  TRP   B CA  1 
ATOM   638  C CA  D TRP   B 2 41  ? -16.784 4.517   -7.115  0.25 43.48  ? 50  TRP   B CA  1 
ATOM   639  C C   A TRP   B 2 41  ? -15.844 5.697   -7.396  0.25 47.24  ? 50  TRP   B C   1 
ATOM   640  C C   B TRP   B 2 41  ? -15.828 5.694   -7.368  0.25 44.77  ? 50  TRP   B C   1 
ATOM   641  C C   C TRP   B 2 41  ? -15.844 5.697   -7.396  0.25 47.24  ? 50  TRP   B C   1 
ATOM   642  C C   D TRP   B 2 41  ? -15.828 5.694   -7.368  0.25 44.77  ? 50  TRP   B C   1 
ATOM   643  O O   A TRP   B 2 41  ? -16.184 6.812   -6.958  0.25 46.67  ? 50  TRP   B O   1 
ATOM   644  O O   B TRP   B 2 41  ? -16.119 6.799   -6.875  0.25 44.12  ? 50  TRP   B O   1 
ATOM   645  O O   C TRP   B 2 41  ? -16.184 6.812   -6.958  0.25 46.67  ? 50  TRP   B O   1 
ATOM   646  O O   D TRP   B 2 41  ? -16.119 6.799   -6.875  0.25 44.12  ? 50  TRP   B O   1 
ATOM   647  C CB  A TRP   B 2 41  ? -16.176 3.617   -5.988  0.25 47.60  ? 50  TRP   B CB  1 
ATOM   648  C CB  B TRP   B 2 41  ? -16.320 3.645   -5.940  0.25 40.49  ? 50  TRP   B CB  1 
ATOM   649  C CB  C TRP   B 2 41  ? -16.176 3.617   -5.988  0.25 47.60  ? 50  TRP   B CB  1 
ATOM   650  C CB  D TRP   B 2 41  ? -16.320 3.645   -5.940  0.25 40.49  ? 50  TRP   B CB  1 
ATOM   651  C CG  A TRP   B 2 41  ? -16.296 4.247   -4.635  0.25 48.03  ? 50  TRP   B CG  1 
ATOM   652  C CG  B TRP   B 2 41  ? -16.191 4.443   -4.681  0.25 37.85  ? 50  TRP   B CG  1 
ATOM   653  C CG  C TRP   B 2 41  ? -16.296 4.247   -4.635  0.25 48.03  ? 50  TRP   B CG  1 
ATOM   654  C CG  D TRP   B 2 41  ? -16.191 4.443   -4.681  0.25 37.85  ? 50  TRP   B CG  1 
ATOM   655  C CD1 A TRP   B 2 41  ? -17.274 4.021   -3.709  0.25 47.88  ? 50  TRP   B CD1 1 
ATOM   656  C CD1 B TRP   B 2 41  ? -15.123 5.206   -4.316  0.25 36.63  ? 50  TRP   B CD1 1 
ATOM   657  C CD1 C TRP   B 2 41  ? -17.274 4.021   -3.709  0.25 47.88  ? 50  TRP   B CD1 1 
ATOM   658  C CD1 D TRP   B 2 41  ? -15.123 5.206   -4.316  0.25 36.63  ? 50  TRP   B CD1 1 
ATOM   659  C CD2 A TRP   B 2 41  ? -15.428 5.245   -4.066  0.25 48.77  ? 50  TRP   B CD2 1 
ATOM   660  C CD2 B TRP   B 2 41  ? -17.182 4.625   -3.651  0.25 37.48  ? 50  TRP   B CD2 1 
ATOM   661  C CD2 C TRP   B 2 41  ? -15.428 5.245   -4.066  0.25 48.77  ? 50  TRP   B CD2 1 
ATOM   662  C CD2 D TRP   B 2 41  ? -17.182 4.625   -3.651  0.25 37.48  ? 50  TRP   B CD2 1 
ATOM   663  N NE1 A TRP   B 2 41  ? -17.064 4.796   -2.601  0.25 49.20  ? 50  TRP   B NE1 1 
ATOM   664  N NE1 B TRP   B 2 41  ? -15.369 5.829   -3.125  0.25 34.50  ? 50  TRP   B NE1 1 
ATOM   665  N NE1 C TRP   B 2 41  ? -17.064 4.796   -2.601  0.25 49.20  ? 50  TRP   B NE1 1 
ATOM   666  N NE1 D TRP   B 2 41  ? -15.369 5.829   -3.125  0.25 34.50  ? 50  TRP   B NE1 1 
ATOM   667  C CE2 A TRP   B 2 41  ? -15.942 5.560   -2.791  0.25 48.19  ? 50  TRP   B CE2 1 
ATOM   668  C CE2 B TRP   B 2 41  ? -16.624 5.498   -2.694  0.25 36.25  ? 50  TRP   B CE2 1 
ATOM   669  C CE2 C TRP   B 2 41  ? -15.942 5.560   -2.791  0.25 48.19  ? 50  TRP   B CE2 1 
ATOM   670  C CE2 D TRP   B 2 41  ? -16.624 5.498   -2.694  0.25 36.25  ? 50  TRP   B CE2 1 
ATOM   671  C CE3 A TRP   B 2 41  ? -14.266 5.894   -4.499  0.25 51.61  ? 50  TRP   B CE3 1 
ATOM   672  C CE3 B TRP   B 2 41  ? -18.478 4.145   -3.438  0.25 36.30  ? 50  TRP   B CE3 1 
ATOM   673  C CE3 C TRP   B 2 41  ? -14.266 5.894   -4.499  0.25 51.61  ? 50  TRP   B CE3 1 
ATOM   674  C CE3 D TRP   B 2 41  ? -18.478 4.145   -3.438  0.25 36.30  ? 50  TRP   B CE3 1 
ATOM   675  C CZ2 A TRP   B 2 41  ? -15.331 6.493   -1.951  0.25 52.11  ? 50  TRP   B CZ2 1 
ATOM   676  C CZ2 B TRP   B 2 41  ? -17.311 5.888   -1.544  0.25 37.18  ? 50  TRP   B CZ2 1 
ATOM   677  C CZ2 C TRP   B 2 41  ? -15.331 6.493   -1.951  0.25 52.11  ? 50  TRP   B CZ2 1 
ATOM   678  C CZ2 D TRP   B 2 41  ? -17.311 5.888   -1.544  0.25 37.18  ? 50  TRP   B CZ2 1 
ATOM   679  C CZ3 A TRP   B 2 41  ? -13.661 6.812   -3.667  0.25 51.95  ? 50  TRP   B CZ3 1 
ATOM   680  C CZ3 B TRP   B 2 41  ? -19.156 4.533   -2.301  0.25 37.49  ? 50  TRP   B CZ3 1 
ATOM   681  C CZ3 C TRP   B 2 41  ? -13.661 6.812   -3.667  0.25 51.95  ? 50  TRP   B CZ3 1 
ATOM   682  C CZ3 D TRP   B 2 41  ? -19.156 4.533   -2.301  0.25 37.49  ? 50  TRP   B CZ3 1 
ATOM   683  C CH2 A TRP   B 2 41  ? -14.188 7.106   -2.409  0.25 50.76  ? 50  TRP   B CH2 1 
ATOM   684  C CH2 B TRP   B 2 41  ? -18.582 5.391   -1.368  0.25 35.91  ? 50  TRP   B CH2 1 
ATOM   685  C CH2 C TRP   B 2 41  ? -14.188 7.106   -2.409  0.25 50.76  ? 50  TRP   B CH2 1 
ATOM   686  C CH2 D TRP   B 2 41  ? -18.582 5.391   -1.368  0.25 35.91  ? 50  TRP   B CH2 1 
ATOM   687  N N   . HIS   B 2 42  ? -14.738 5.489   -8.114  1.00 47.05  ? 51  HIS   B N   1 
ATOM   688  C CA  . HIS   B 2 42  ? -13.753 6.583   -8.404  1.00 45.33  ? 51  HIS   B CA  1 
ATOM   689  C C   . HIS   B 2 42  ? -14.410 7.712   -9.229  1.00 47.27  ? 51  HIS   B C   1 
ATOM   690  O O   . HIS   B 2 42  ? -13.843 8.815   -9.257  1.00 45.51  ? 51  HIS   B O   1 
ATOM   691  C CB  . HIS   B 2 42  ? -12.463 6.060   -9.069  1.00 41.77  ? 51  HIS   B CB  1 
ATOM   692  C CG  . HIS   B 2 42  ? -12.558 5.839   -10.539 1.00 41.71  ? 51  HIS   B CG  1 
ATOM   693  N ND1 . HIS   B 2 42  ? -12.958 4.627   -11.076 1.00 45.35  ? 51  HIS   B ND1 1 
ATOM   694  C CD2 . HIS   B 2 42  ? -12.310 6.655   -11.593 1.00 46.08  ? 51  HIS   B CD2 1 
ATOM   695  C CE1 . HIS   B 2 42  ? -12.980 4.716   -12.394 1.00 46.19  ? 51  HIS   B CE1 1 
ATOM   696  N NE2 . HIS   B 2 42  ? -12.586 5.953   -12.742 1.00 43.01  ? 51  HIS   B NE2 1 
ATOM   697  N N   . VAL   B 2 43  ? -15.558 7.478   -9.874  1.00 47.44  ? 52  VAL   B N   1 
ATOM   698  C CA  . VAL   B 2 43  ? -16.282 8.544   -10.625 1.00 47.72  ? 52  VAL   B CA  1 
ATOM   699  C C   . VAL   B 2 43  ? -16.948 9.529   -9.648  1.00 52.85  ? 52  VAL   B C   1 
ATOM   700  O O   . VAL   B 2 43  ? -16.649 10.712  -9.762  1.00 48.98  ? 52  VAL   B O   1 
ATOM   701  C CB  . VAL   B 2 43  ? -17.292 7.980   -11.634 1.00 49.05  ? 52  VAL   B CB  1 
ATOM   702  C CG1 . VAL   B 2 43  ? -18.163 9.104   -12.212 1.00 47.09  ? 52  VAL   B CG1 1 
ATOM   703  C CG2 . VAL   B 2 43  ? -16.596 7.193   -12.753 1.00 49.72  ? 52  VAL   B CG2 1 
ATOM   704  N N   . THR   B 2 44  ? -17.814 9.079   -8.733  1.00 51.75  ? 53  THR   B N   1 
ATOM   705  C CA  . THR   B 2 44  ? -18.659 9.980   -7.900  1.00 48.89  ? 53  THR   B CA  1 
ATOM   706  C C   . THR   B 2 44  ? -18.111 10.162  -6.489  1.00 52.75  ? 53  THR   B C   1 
ATOM   707  O O   . THR   B 2 44  ? -18.623 11.076  -5.784  1.00 44.60  ? 53  THR   B O   1 
ATOM   708  C CB  . THR   B 2 44  ? -20.071 9.410   -7.799  1.00 49.52  ? 53  THR   B CB  1 
ATOM   709  O OG1 . THR   B 2 44  ? -20.019 8.173   -7.080  1.00 40.96  ? 53  THR   B OG1 1 
ATOM   710  C CG2 . THR   B 2 44  ? -20.663 9.219   -9.175  1.00 48.54  ? 53  THR   B CG2 1 
ATOM   711  N N   . LYS   B 2 45  ? -17.193 9.279   -6.083  1.00 44.47  ? 54  LYS   B N   1 
ATOM   712  C CA  . LYS   B 2 45  ? -16.735 9.076   -4.685  1.00 48.57  ? 54  LYS   B CA  1 
ATOM   713  C C   . LYS   B 2 45  ? -17.905 8.902   -3.703  1.00 52.59  ? 54  LYS   B C   1 
ATOM   714  O O   . LYS   B 2 45  ? -17.722 9.223   -2.510  1.00 59.03  ? 54  LYS   B O   1 
ATOM   715  C CB  . LYS   B 2 45  ? -15.886 10.252  -4.192  1.00 58.12  ? 54  LYS   B CB  1 
ATOM   716  C CG  . LYS   B 2 45  ? -14.871 10.801  -5.169  1.00 62.66  ? 54  LYS   B CG  1 
ATOM   717  C CD  . LYS   B 2 45  ? -13.627 9.972   -5.309  1.00 67.09  ? 54  LYS   B CD  1 
ATOM   718  C CE  . LYS   B 2 45  ? -12.517 10.798  -5.927  1.00 73.26  ? 54  LYS   B CE  1 
ATOM   719  N NZ  . LYS   B 2 45  ? -11.985 10.152  -7.141  1.00 74.20  ? 54  LYS   B NZ  1 
ATOM   720  N N   . GLY   B 2 46  ? -19.046 8.383   -4.144  1.00 54.01  ? 55  GLY   B N   1 
ATOM   721  C CA  . GLY   B 2 46  ? -20.187 8.093   -3.261  1.00 47.03  ? 55  GLY   B CA  1 
ATOM   722  C C   . GLY   B 2 46  ? -21.044 9.325   -3.044  1.00 51.42  ? 55  GLY   B C   1 
ATOM   723  O O   . GLY   B 2 46  ? -21.943 9.245   -2.203  1.00 53.38  ? 55  GLY   B O   1 
ATOM   724  N N   . ALA   B 2 47  ? -20.789 10.411  -3.778  1.00 52.82  ? 56  ALA   B N   1 
ATOM   725  C CA  . ALA   B 2 47  ? -21.558 11.688  -3.701  1.00 52.40  ? 56  ALA   B CA  1 
ATOM   726  C C   . ALA   B 2 47  ? -22.975 11.491  -4.259  1.00 49.61  ? 56  ALA   B C   1 
ATOM   727  O O   . ALA   B 2 47  ? -23.179 10.673  -5.166  1.00 51.11  ? 56  ALA   B O   1 
ATOM   728  C CB  . ALA   B 2 47  ? -20.834 12.776  -4.454  1.00 48.85  ? 56  ALA   B CB  1 
ATOM   729  N N   . ALA   B 2 48  ? -23.942 12.232  -3.750  1.00 51.70  ? 57  ALA   B N   1 
ATOM   730  C CA  . ALA   B 2 48  ? -25.303 12.273  -4.317  1.00 51.62  ? 57  ALA   B CA  1 
ATOM   731  C C   . ALA   B 2 48  ? -25.200 12.820  -5.734  1.00 45.84  ? 57  ALA   B C   1 
ATOM   732  O O   . ALA   B 2 48  ? -24.260 13.544  -5.990  1.00 50.54  ? 57  ALA   B O   1 
ATOM   733  C CB  . ALA   B 2 48  ? -26.220 13.125  -3.478  1.00 54.45  ? 57  ALA   B CB  1 
ATOM   734  N N   . LEU   B 2 49  ? -26.174 12.501  -6.583  1.00 43.02  ? 58  LEU   B N   1 
ATOM   735  C CA  . LEU   B 2 49  ? -26.275 12.978  -7.983  1.00 50.52  ? 58  LEU   B CA  1 
ATOM   736  C C   . LEU   B 2 49  ? -27.640 13.633  -8.235  1.00 50.71  ? 58  LEU   B C   1 
ATOM   737  O O   . LEU   B 2 49  ? -28.631 13.334  -7.546  1.00 49.87  ? 58  LEU   B O   1 
ATOM   738  C CB  . LEU   B 2 49  ? -26.125 11.787  -8.938  1.00 51.33  ? 58  LEU   B CB  1 
ATOM   739  C CG  . LEU   B 2 49  ? -24.819 11.004  -8.829  1.00 51.62  ? 58  LEU   B CG  1 
ATOM   740  C CD1 . LEU   B 2 49  ? -24.864 9.821   -9.753  1.00 49.20  ? 58  LEU   B CD1 1 
ATOM   741  C CD2 . LEU   B 2 49  ? -23.625 11.883  -9.141  1.00 54.53  ? 58  LEU   B CD2 1 
ATOM   742  N N   . ARG   B 2 50  ? -27.682 14.445  -9.268  1.00 52.27  ? 59  ARG   B N   1 
ATOM   743  C CA  . ARG   B 2 50  ? -28.906 15.146  -9.703  1.00 60.93  ? 59  ARG   B CA  1 
ATOM   744  C C   . ARG   B 2 50  ? -29.307 14.566  -11.063 1.00 54.82  ? 59  ARG   B C   1 
ATOM   745  O O   . ARG   B 2 50  ? -28.414 14.356  -11.928 1.00 54.43  ? 59  ARG   B O   1 
ATOM   746  C CB  . ARG   B 2 50  ? -28.609 16.644  -9.689  1.00 64.84  ? 59  ARG   B CB  1 
ATOM   747  C CG  . ARG   B 2 50  ? -29.766 17.498  -10.177 1.00 80.94  ? 59  ARG   B CG  1 
ATOM   748  C CD  . ARG   B 2 50  ? -29.563 18.974  -9.883  1.00 86.88  ? 59  ARG   B CD  1 
ATOM   749  N NE  . ARG   B 2 50  ? -28.177 19.435  -10.015 1.00 88.45  ? 59  ARG   B NE  1 
ATOM   750  C CZ  . ARG   B 2 50  ? -27.569 19.776  -11.160 1.00 90.72  ? 59  ARG   B CZ  1 
ATOM   751  N NH1 . ARG   B 2 50  ? -28.198 19.693  -12.328 1.00 79.01  ? 59  ARG   B NH1 1 
ATOM   752  N NH2 . ARG   B 2 50  ? -26.309 20.187  -11.125 1.00 90.04  ? 59  ARG   B NH2 1 
ATOM   753  N N   . SER   B 2 51  ? -30.590 14.244  -11.209 1.00 56.18  ? 60  SER   B N   1 
ATOM   754  C CA  . SER   B 2 51  ? -31.239 13.935  -12.505 1.00 61.75  ? 60  SER   B CA  1 
ATOM   755  C C   . SER   B 2 51  ? -32.330 14.979  -12.777 1.00 63.41  ? 60  SER   B C   1 
ATOM   756  O O   . SER   B 2 51  ? -33.481 14.763  -12.353 1.00 64.80  ? 60  SER   B O   1 
ATOM   757  C CB  . SER   B 2 51  ? -31.795 12.541  -12.503 1.00 62.58  ? 60  SER   B CB  1 
ATOM   758  O OG  . SER   B 2 51  ? -32.476 12.296  -13.723 1.00 64.61  ? 60  SER   B OG  1 
ATOM   759  N N   . GLY   B 2 52  ? -31.986 16.062  -13.478 1.00 70.14  ? 61  GLY   B N   1 
ATOM   760  C CA  . GLY   B 2 52  ? -32.880 17.223  -13.641 1.00 69.09  ? 61  GLY   B CA  1 
ATOM   761  C C   . GLY   B 2 52  ? -33.059 17.896  -12.295 1.00 73.98  ? 61  GLY   B C   1 
ATOM   762  O O   . GLY   B 2 52  ? -32.111 18.574  -11.820 1.00 70.86  ? 61  GLY   B O   1 
ATOM   763  N N   A GLU   B 2 53  ? -34.225 17.701  -11.670 0.25 72.72  ? 62  GLU   B N   1 
ATOM   764  N N   B GLU   B 2 53  ? -34.225 17.701  -11.670 0.25 72.72  ? 62  GLU   B N   1 
ATOM   765  N N   C GLU   B 2 53  ? -34.240 17.719  -11.695 0.25 74.51  ? 62  GLU   B N   1 
ATOM   766  N N   D GLU   B 2 53  ? -34.240 17.719  -11.695 0.25 74.51  ? 62  GLU   B N   1 
ATOM   767  C CA  A GLU   B 2 53  ? -34.545 18.214  -10.310 0.25 78.07  ? 62  GLU   B CA  1 
ATOM   768  C CA  B GLU   B 2 53  ? -34.545 18.214  -10.310 0.25 78.07  ? 62  GLU   B CA  1 
ATOM   769  C CA  C GLU   B 2 53  ? -34.593 18.201  -10.332 0.25 81.03  ? 62  GLU   B CA  1 
ATOM   770  C CA  D GLU   B 2 53  ? -34.593 18.201  -10.332 0.25 81.03  ? 62  GLU   B CA  1 
ATOM   771  C C   A GLU   B 2 53  ? -34.520 17.068  -9.291  0.25 77.63  ? 62  GLU   B C   1 
ATOM   772  C C   B GLU   B 2 53  ? -34.520 17.068  -9.291  0.25 77.63  ? 62  GLU   B C   1 
ATOM   773  C C   C GLU   B 2 53  ? -34.449 17.055  -9.327  0.25 79.43  ? 62  GLU   B C   1 
ATOM   774  C C   D GLU   B 2 53  ? -34.449 17.055  -9.327  0.25 79.43  ? 62  GLU   B C   1 
ATOM   775  O O   A GLU   B 2 53  ? -34.161 17.340  -8.130  0.25 82.83  ? 62  GLU   B O   1 
ATOM   776  O O   B GLU   B 2 53  ? -34.161 17.340  -8.130  0.25 82.83  ? 62  GLU   B O   1 
ATOM   777  O O   C GLU   B 2 53  ? -33.932 17.312  -8.223  0.25 84.90  ? 62  GLU   B O   1 
ATOM   778  O O   D GLU   B 2 53  ? -33.932 17.312  -8.223  0.25 84.90  ? 62  GLU   B O   1 
ATOM   779  C CB  A GLU   B 2 53  ? -35.892 18.937  -10.310 0.25 82.61  ? 62  GLU   B CB  1 
ATOM   780  C CB  B GLU   B 2 53  ? -35.892 18.937  -10.310 0.25 82.61  ? 62  GLU   B CB  1 
ATOM   781  C CB  C GLU   B 2 53  ? -36.026 18.728  -10.303 0.25 87.64  ? 62  GLU   B CB  1 
ATOM   782  C CB  D GLU   B 2 53  ? -36.026 18.728  -10.303 0.25 87.64  ? 62  GLU   B CB  1 
ATOM   783  C CG  A GLU   B 2 53  ? -35.778 20.391  -10.727 0.25 84.44  ? 62  GLU   B CG  1 
ATOM   784  C CG  B GLU   B 2 53  ? -35.778 20.391  -10.727 0.25 84.44  ? 62  GLU   B CG  1 
ATOM   785  C CG  C GLU   B 2 53  ? -36.191 20.053  -11.015 0.25 92.17  ? 62  GLU   B CG  1 
ATOM   786  C CG  D GLU   B 2 53  ? -36.191 20.053  -11.015 0.25 92.17  ? 62  GLU   B CG  1 
ATOM   787  C CD  A GLU   B 2 53  ? -36.779 21.329  -10.074 0.25 86.79  ? 62  GLU   B CD  1 
ATOM   788  C CD  B GLU   B 2 53  ? -36.779 21.329  -10.074 0.25 86.79  ? 62  GLU   B CD  1 
ATOM   789  C CD  C GLU   B 2 53  ? -37.632 20.520  -11.124 0.25 96.45  ? 62  GLU   B CD  1 
ATOM   790  C CD  D GLU   B 2 53  ? -37.632 20.520  -11.124 0.25 96.45  ? 62  GLU   B CD  1 
ATOM   791  O OE1 A GLU   B 2 53  ? -37.779 20.831  -9.511  0.25 88.20  ? 62  GLU   B OE1 1 
ATOM   792  O OE1 B GLU   B 2 53  ? -37.779 20.831  -9.511  0.25 88.20  ? 62  GLU   B OE1 1 
ATOM   793  O OE1 C GLU   B 2 53  ? -38.495 19.697  -11.507 0.25 97.21  ? 62  GLU   B OE1 1 
ATOM   794  O OE1 D GLU   B 2 53  ? -38.495 19.697  -11.507 0.25 97.21  ? 62  GLU   B OE1 1 
ATOM   795  O OE2 A GLU   B 2 53  ? -36.551 22.556  -10.124 0.25 85.69  ? 62  GLU   B OE2 1 
ATOM   796  O OE2 B GLU   B 2 53  ? -36.551 22.556  -10.124 0.25 85.69  ? 62  GLU   B OE2 1 
ATOM   797  O OE2 C GLU   B 2 53  ? -37.889 21.703  -10.821 0.25 103.52 ? 62  GLU   B OE2 1 
ATOM   798  O OE2 D GLU   B 2 53  ? -37.889 21.703  -10.821 0.25 103.52 ? 62  GLU   B OE2 1 
ATOM   799  N N   . GLY   B 2 54  ? -34.903 15.851  -9.698  1.00 74.76  ? 63  GLY   B N   1 
ATOM   800  C CA  . GLY   B 2 54  ? -34.712 14.631  -8.886  1.00 73.61  ? 63  GLY   B CA  1 
ATOM   801  C C   . GLY   B 2 54  ? -33.273 14.477  -8.379  1.00 69.97  ? 63  GLY   B C   1 
ATOM   802  O O   . GLY   B 2 54  ? -32.303 14.928  -9.046  1.00 72.01  ? 63  GLY   B O   1 
ATOM   803  N N   . ARG   B 2 55  ? -33.139 13.888  -7.200  1.00 64.82  ? 64  ARG   B N   1 
ATOM   804  C CA  . ARG   B 2 55  ? -31.861 13.652  -6.492  1.00 63.71  ? 64  ARG   B CA  1 
ATOM   805  C C   . ARG   B 2 55  ? -31.670 12.136  -6.425  1.00 66.94  ? 64  ARG   B C   1 
ATOM   806  O O   . ARG   B 2 55  ? -32.640 11.470  -6.064  1.00 64.35  ? 64  ARG   B O   1 
ATOM   807  C CB  . ARG   B 2 55  ? -31.986 14.262  -5.097  1.00 65.75  ? 64  ARG   B CB  1 
ATOM   808  C CG  . ARG   B 2 55  ? -30.848 13.981  -4.130  1.00 71.69  ? 64  ARG   B CG  1 
ATOM   809  C CD  . ARG   B 2 55  ? -31.317 14.165  -2.687  1.00 73.87  ? 64  ARG   B CD  1 
ATOM   810  N NE  . ARG   B 2 55  ? -30.260 13.766  -1.774  1.00 80.28  ? 64  ARG   B NE  1 
ATOM   811  C CZ  . ARG   B 2 55  ? -29.249 14.541  -1.381  1.00 82.69  ? 64  ARG   B CZ  1 
ATOM   812  N NH1 . ARG   B 2 55  ? -29.179 15.795  -1.790  1.00 83.17  ? 64  ARG   B NH1 1 
ATOM   813  N NH2 . ARG   B 2 55  ? -28.318 14.065  -0.564  1.00 78.08  ? 64  ARG   B NH2 1 
ATOM   814  N N   . LEU   B 2 56  ? -30.491 11.609  -6.765  1.00 57.24  ? 65  LEU   B N   1 
ATOM   815  C CA  . LEU   B 2 56  ? -30.179 10.164  -6.599  1.00 52.24  ? 65  LEU   B CA  1 
ATOM   816  C C   . LEU   B 2 56  ? -29.262 10.013  -5.391  1.00 48.95  ? 65  LEU   B C   1 
ATOM   817  O O   . LEU   B 2 56  ? -28.208 10.744  -5.341  1.00 51.78  ? 65  LEU   B O   1 
ATOM   818  C CB  . LEU   B 2 56  ? -29.500 9.605   -7.857  1.00 51.49  ? 65  LEU   B CB  1 
ATOM   819  C CG  . LEU   B 2 56  ? -30.224 9.769   -9.192  1.00 57.77  ? 65  LEU   B CG  1 
ATOM   820  C CD1 . LEU   B 2 56  ? -29.632 8.814   -10.213 1.00 63.71  ? 65  LEU   B CD1 1 
ATOM   821  C CD2 . LEU   B 2 56  ? -31.721 9.535   -9.086  1.00 60.58  ? 65  LEU   B CD2 1 
ATOM   822  N N   . ASP   B 2 57  ? -29.630 9.141   -4.445  1.00 45.04  ? 66  ASP   B N   1 
ATOM   823  C CA  . ASP   B 2 57  ? -28.795 8.899   -3.239  1.00 50.50  ? 66  ASP   B CA  1 
ATOM   824  C C   . ASP   B 2 57  ? -28.081 7.554   -3.350  1.00 50.94  ? 66  ASP   B C   1 
ATOM   825  O O   . ASP   B 2 57  ? -28.689 6.558   -3.775  1.00 43.90  ? 66  ASP   B O   1 
ATOM   826  C CB  . ASP   B 2 57  ? -29.615 8.992   -1.956  1.00 55.46  ? 66  ASP   B CB  1 
ATOM   827  C CG  . ASP   B 2 57  ? -30.218 10.373  -1.767  1.00 66.58  ? 66  ASP   B CG  1 
ATOM   828  O OD1 . ASP   B 2 57  ? -29.549 11.358  -2.138  1.00 69.18  ? 66  ASP   B OD1 1 
ATOM   829  O OD2 . ASP   B 2 57  ? -31.361 10.452  -1.296  1.00 69.94  ? 66  ASP   B OD2 1 
ATOM   830  N N   . PRO   B 2 58  ? -26.801 7.469   -2.906  1.00 44.01  ? 67  PRO   B N   1 
ATOM   831  C CA  . PRO   B 2 58  ? -26.069 6.201   -2.929  1.00 47.92  ? 67  PRO   B CA  1 
ATOM   832  C C   . PRO   B 2 58  ? -26.811 5.190   -2.054  1.00 52.78  ? 67  PRO   B C   1 
ATOM   833  O O   . PRO   B 2 58  ? -27.433 5.580   -1.051  1.00 52.53  ? 67  PRO   B O   1 
ATOM   834  C CB  . PRO   B 2 58  ? -24.670 6.523   -2.388  1.00 47.77  ? 67  PRO   B CB  1 
ATOM   835  C CG  . PRO   B 2 58  ? -24.886 7.799   -1.595  1.00 54.31  ? 67  PRO   B CG  1 
ATOM   836  C CD  . PRO   B 2 58  ? -26.009 8.543   -2.291  1.00 44.44  ? 67  PRO   B CD  1 
ATOM   837  N N   . TYR   B 2 59  ? -26.763 3.921   -2.458  1.00 48.34  ? 68  TYR   B N   1 
ATOM   838  C CA  . TYR   B 2 59  ? -27.456 2.810   -1.766  1.00 43.01  ? 68  TYR   B CA  1 
ATOM   839  C C   . TYR   B 2 59  ? -26.428 1.755   -1.329  1.00 44.61  ? 68  TYR   B C   1 
ATOM   840  O O   . TYR   B 2 59  ? -26.516 1.257   -0.195  1.00 44.64  ? 68  TYR   B O   1 
ATOM   841  C CB  . TYR   B 2 59  ? -28.565 2.272   -2.677  1.00 46.31  ? 68  TYR   B CB  1 
ATOM   842  C CG  . TYR   B 2 59  ? -29.361 1.134   -2.089  1.00 44.98  ? 68  TYR   B CG  1 
ATOM   843  C CD1 . TYR   B 2 59  ? -28.832 -0.147  -2.038  1.00 50.15  ? 68  TYR   B CD1 1 
ATOM   844  C CD2 . TYR   B 2 59  ? -30.625 1.335   -1.552  1.00 45.10  ? 68  TYR   B CD2 1 
ATOM   845  C CE1 . TYR   B 2 59  ? -29.537 -1.204  -1.478  1.00 46.78  ? 68  TYR   B CE1 1 
ATOM   846  C CE2 . TYR   B 2 59  ? -31.360 0.273   -1.039  1.00 46.22  ? 68  TYR   B CE2 1 
ATOM   847  C CZ  . TYR   B 2 59  ? -30.814 -0.999  -0.987  1.00 43.28  ? 68  TYR   B CZ  1 
ATOM   848  O OH  . TYR   B 2 59  ? -31.500 -2.057  -0.442  1.00 45.37  ? 68  TYR   B OH  1 
ATOM   849  N N   . TRP   B 2 60  ? -25.510 1.404   -2.225  1.00 41.03  ? 69  TRP   B N   1 
ATOM   850  C CA  . TRP   B 2 60  ? -24.428 0.420   -1.995  1.00 40.06  ? 69  TRP   B CA  1 
ATOM   851  C C   . TRP   B 2 60  ? -23.168 0.889   -2.710  1.00 40.79  ? 69  TRP   B C   1 
ATOM   852  O O   . TRP   B 2 60  ? -23.274 1.490   -3.792  1.00 47.03  ? 69  TRP   B O   1 
ATOM   853  C CB  . TRP   B 2 60  ? -24.845 -0.953  -2.501  1.00 38.14  ? 69  TRP   B CB  1 
ATOM   854  C CG  . TRP   B 2 60  ? -23.704 -1.918  -2.454  1.00 39.37  ? 69  TRP   B CG  1 
ATOM   855  C CD1 . TRP   B 2 60  ? -23.247 -2.596  -1.369  1.00 39.15  ? 69  TRP   B CD1 1 
ATOM   856  C CD2 . TRP   B 2 60  ? -22.834 -2.251  -3.539  1.00 36.78  ? 69  TRP   B CD2 1 
ATOM   857  N NE1 . TRP   B 2 60  ? -22.135 -3.328  -1.697  1.00 37.69  ? 69  TRP   B NE1 1 
ATOM   858  C CE2 . TRP   B 2 60  ? -21.873 -3.151  -3.029  1.00 38.41  ? 69  TRP   B CE2 1 
ATOM   859  C CE3 . TRP   B 2 60  ? -22.814 -1.927  -4.894  1.00 37.85  ? 69  TRP   B CE3 1 
ATOM   860  C CZ2 . TRP   B 2 60  ? -20.893 -3.716  -3.835  1.00 36.55  ? 69  TRP   B CZ2 1 
ATOM   861  C CZ3 . TRP   B 2 60  ? -21.830 -2.463  -5.691  1.00 42.89  ? 69  TRP   B CZ3 1 
ATOM   862  C CH2 . TRP   B 2 60  ? -20.899 -3.372  -5.168  1.00 43.48  ? 69  TRP   B CH2 1 
ATOM   863  N N   . GLY   B 2 61  ? -22.013 0.530   -2.167  1.00 45.37  ? 70  GLY   B N   1 
ATOM   864  C CA  . GLY   B 2 61  ? -20.717 0.915   -2.736  1.00 44.64  ? 70  GLY   B CA  1 
ATOM   865  C C   . GLY   B 2 61  ? -19.608 0.178   -2.042  1.00 40.11  ? 70  GLY   B C   1 
ATOM   866  O O   . GLY   B 2 61  ? -19.767 -0.098  -0.845  1.00 41.44  ? 70  GLY   B O   1 
ATOM   867  N N   . ASP   B 2 62  ? -18.539 -0.111  -2.772  1.00 40.96  ? 71  ASP   B N   1 
ATOM   868  C CA  . ASP   B 2 62  ? -17.321 -0.808  -2.280  1.00 36.96  ? 71  ASP   B CA  1 
ATOM   869  C C   . ASP   B 2 62  ? -16.099 -0.240  -3.012  1.00 38.85  ? 71  ASP   B C   1 
ATOM   870  O O   . ASP   B 2 62  ? -15.975 -0.467  -4.214  1.00 46.74  ? 71  ASP   B O   1 
ATOM   871  C CB  . ASP   B 2 62  ? -17.461 -2.308  -2.476  1.00 41.69  ? 71  ASP   B CB  1 
ATOM   872  C CG  . ASP   B 2 62  ? -16.303 -3.097  -1.877  1.00 47.81  ? 71  ASP   B CG  1 
ATOM   873  O OD1 . ASP   B 2 62  ? -15.167 -2.940  -2.345  1.00 49.89  ? 71  ASP   B OD1 1 
ATOM   874  O OD2 . ASP   B 2 62  ? -16.539 -3.795  -0.900  1.00 55.54  ? 71  ASP   B OD2 1 
ATOM   875  N N   . VAL   B 2 63  ? -15.229 0.498   -2.325  1.00 41.14  ? 72  VAL   B N   1 
ATOM   876  C CA  . VAL   B 2 63  ? -13.997 1.086   -2.914  1.00 38.98  ? 72  VAL   B CA  1 
ATOM   877  C C   . VAL   B 2 63  ? -13.154 -0.016  -3.577  1.00 46.48  ? 72  VAL   B C   1 
ATOM   878  O O   . VAL   B 2 63  ? -12.492 0.282   -4.629  1.00 46.05  ? 72  VAL   B O   1 
ATOM   879  C CB  . VAL   B 2 63  ? -13.184 1.876   -1.869  1.00 43.69  ? 72  VAL   B CB  1 
ATOM   880  C CG1 . VAL   B 2 63  ? -11.706 1.917   -2.175  1.00 43.53  ? 72  VAL   B CG1 1 
ATOM   881  C CG2 . VAL   B 2 63  ? -13.697 3.297   -1.705  1.00 49.08  ? 72  VAL   B CG2 1 
ATOM   882  N N   . LYS   B 2 64  ? -13.145 -1.245  -3.056  1.00 43.94  ? 73  LYS   B N   1 
ATOM   883  C CA  . LYS   B 2 64  ? -12.183 -2.262  -3.589  1.00 47.67  ? 73  LYS   B CA  1 
ATOM   884  C C   . LYS   B 2 64  ? -12.715 -2.864  -4.907  1.00 48.03  ? 73  LYS   B C   1 
ATOM   885  O O   . LYS   B 2 64  ? -11.906 -3.031  -5.832  1.00 49.89  ? 73  LYS   B O   1 
ATOM   886  C CB  . LYS   B 2 64  ? -11.840 -3.344  -2.566  1.00 49.32  ? 73  LYS   B CB  1 
ATOM   887  C CG  . LYS   B 2 64  ? -10.892 -4.406  -3.111  1.00 50.98  ? 73  LYS   B CG  1 
ATOM   888  C CD  . LYS   B 2 64  ? -10.472 -5.465  -2.109  1.00 50.84  ? 73  LYS   B CD  1 
ATOM   889  C CE  . LYS   B 2 64  ? -9.690  -6.559  -2.812  1.00 60.44  ? 73  LYS   B CE  1 
ATOM   890  N NZ  . LYS   B 2 64  ? -8.995  -7.454  -1.857  1.00 60.34  ? 73  LYS   B NZ  1 
ATOM   891  N N   . GLN   B 2 65  ? -14.011 -3.199  -4.999  1.00 48.66  ? 74  GLN   B N   1 
ATOM   892  C CA  . GLN   B 2 65  ? -14.687 -3.516  -6.281  1.00 44.45  ? 74  GLN   B CA  1 
ATOM   893  C C   . GLN   B 2 65  ? -14.707 -2.303  -7.236  1.00 45.54  ? 74  GLN   B C   1 
ATOM   894  O O   . GLN   B 2 65  ? -14.854 -2.537  -8.477  1.00 49.77  ? 74  GLN   B O   1 
ATOM   895  C CB  . GLN   B 2 65  ? -16.107 -3.985  -6.023  1.00 46.27  ? 74  GLN   B CB  1 
ATOM   896  C CG  . GLN   B 2 65  ? -16.200 -5.332  -5.324  1.00 51.37  ? 74  GLN   B CG  1 
ATOM   897  C CD  . GLN   B 2 65  ? -17.651 -5.761  -5.237  1.00 54.71  ? 74  GLN   B CD  1 
ATOM   898  O OE1 . GLN   B 2 65  ? -18.361 -5.878  -6.234  1.00 56.71  ? 74  GLN   B OE1 1 
ATOM   899  N NE2 . GLN   B 2 65  ? -18.142 -5.918  -4.020  1.00 59.84  ? 74  GLN   B NE2 1 
ATOM   900  N N   . ASP   B 2 66  ? -14.537 -1.083  -6.706  1.00 45.50  ? 75  ASP   B N   1 
ATOM   901  C CA  . ASP   B 2 66  ? -14.649 0.249   -7.389  1.00 49.13  ? 75  ASP   B CA  1 
ATOM   902  C C   . ASP   B 2 66  ? -16.011 0.418   -8.057  1.00 47.18  ? 75  ASP   B C   1 
ATOM   903  O O   . ASP   B 2 66  ? -16.014 0.963   -9.184  1.00 43.81  ? 75  ASP   B O   1 
ATOM   904  C CB  . ASP   B 2 66  ? -13.579 0.480   -8.466  1.00 56.29  ? 75  ASP   B CB  1 
ATOM   905  C CG  . ASP   B 2 66  ? -13.471 1.931   -8.959  1.00 53.77  ? 75  ASP   B CG  1 
ATOM   906  O OD1 . ASP   B 2 66  ? -13.633 2.839   -8.142  1.00 47.55  ? 75  ASP   B OD1 1 
ATOM   907  O OD2 . ASP   B 2 66  ? -13.201 2.139   -10.164 1.00 50.65  ? 75  ASP   B OD2 1 
ATOM   908  N N   . LEU   B 2 67  ? -17.098 -0.017  -7.392  1.00 42.65  ? 76  LEU   B N   1 
ATOM   909  C CA  . LEU   B 2 67  ? -18.518 0.112   -7.852  1.00 39.29  ? 76  LEU   B CA  1 
ATOM   910  C C   . LEU   B 2 67  ? -19.389 0.842   -6.821  1.00 40.16  ? 76  LEU   B C   1 
ATOM   911  O O   . LEU   B 2 67  ? -19.067 0.822   -5.586  1.00 41.55  ? 76  LEU   B O   1 
ATOM   912  C CB  . LEU   B 2 67  ? -19.089 -1.291  -8.070  1.00 42.46  ? 76  LEU   B CB  1 
ATOM   913  C CG  . LEU   B 2 67  ? -18.367 -2.151  -9.129  1.00 46.19  ? 76  LEU   B CG  1 
ATOM   914  C CD1 . LEU   B 2 67  ? -19.061 -3.515  -9.265  1.00 43.19  ? 76  LEU   B CD1 1 
ATOM   915  C CD2 . LEU   B 2 67  ? -18.353 -1.428  -10.481 1.00 47.42  ? 76  LEU   B CD2 1 
ATOM   916  N N   . VAL   B 2 68  ? -20.498 1.402   -7.302  1.00 40.08  ? 77  VAL   B N   1 
ATOM   917  C CA  . VAL   B 2 68  ? -21.497 2.114   -6.458  1.00 42.70  ? 77  VAL   B CA  1 
ATOM   918  C C   . VAL   B 2 68  ? -22.847 2.031   -7.166  1.00 38.38  ? 77  VAL   B C   1 
ATOM   919  O O   . VAL   B 2 68  ? -22.880 2.171   -8.391  1.00 41.59  ? 77  VAL   B O   1 
ATOM   920  C CB  . VAL   B 2 68  ? -21.033 3.558   -6.180  1.00 43.36  ? 77  VAL   B CB  1 
ATOM   921  C CG1 . VAL   B 2 68  ? -20.838 4.364   -7.461  1.00 47.75  ? 77  VAL   B CG1 1 
ATOM   922  C CG2 . VAL   B 2 68  ? -21.994 4.272   -5.226  1.00 48.82  ? 77  VAL   B CG2 1 
ATOM   923  N N   . SER   B 2 69  ? -23.929 1.758   -6.443  1.00 39.19  ? 78  SER   B N   1 
ATOM   924  C CA  . SER   B 2 69  ? -25.302 1.827   -6.996  1.00 38.66  ? 78  SER   B CA  1 
ATOM   925  C C   . SER   B 2 69  ? -26.096 2.946   -6.298  1.00 41.95  ? 78  SER   B C   1 
ATOM   926  O O   . SER   B 2 69  ? -25.835 3.227   -5.099  1.00 38.41  ? 78  SER   B O   1 
ATOM   927  C CB  . SER   B 2 69  ? -26.021 0.487   -6.928  1.00 39.36  ? 78  SER   B CB  1 
ATOM   928  O OG  . SER   B 2 69  ? -26.288 0.106   -5.590  1.00 43.54  ? 78  SER   B OG  1 
ATOM   929  N N   . TYR   B 2 70  ? -27.058 3.539   -7.014  1.00 45.06  ? 79  TYR   B N   1 
ATOM   930  C CA  . TYR   B 2 70  ? -27.933 4.662   -6.553  1.00 41.98  ? 79  TYR   B CA  1 
ATOM   931  C C   . TYR   B 2 70  ? -29.399 4.210   -6.659  1.00 41.18  ? 79  TYR   B C   1 
ATOM   932  O O   . TYR   B 2 70  ? -29.763 3.671   -7.702  1.00 39.19  ? 79  TYR   B O   1 
ATOM   933  C CB  . TYR   B 2 70  ? -27.712 5.946   -7.366  1.00 37.64  ? 79  TYR   B CB  1 
ATOM   934  C CG  . TYR   B 2 70  ? -26.377 6.622   -7.128  1.00 40.41  ? 79  TYR   B CG  1 
ATOM   935  C CD1 . TYR   B 2 70  ? -25.199 6.102   -7.667  1.00 41.59  ? 79  TYR   B CD1 1 
ATOM   936  C CD2 . TYR   B 2 70  ? -26.260 7.759   -6.341  1.00 38.44  ? 79  TYR   B CD2 1 
ATOM   937  C CE1 . TYR   B 2 70  ? -23.956 6.673   -7.398  1.00 41.54  ? 79  TYR   B CE1 1 
ATOM   938  C CE2 . TYR   B 2 70  ? -25.022 8.336   -6.058  1.00 42.62  ? 79  TYR   B CE2 1 
ATOM   939  C CZ  . TYR   B 2 70  ? -23.855 7.777   -6.561  1.00 43.28  ? 79  TYR   B CZ  1 
ATOM   940  O OH  . TYR   B 2 70  ? -22.628 8.361   -6.326  1.00 48.07  ? 79  TYR   B OH  1 
ATOM   941  N N   . CYS   B 2 71  ? -30.181 4.431   -5.587  1.00 44.28  ? 80  CYS   B N   1 
ATOM   942  C CA  . CYS   B 2 71  ? -31.670 4.268   -5.474  1.00 44.35  ? 80  CYS   B CA  1 
ATOM   943  C C   . CYS   B 2 71  ? -32.025 2.812   -5.182  1.00 50.79  ? 80  CYS   B C   1 
ATOM   944  O O   . CYS   B 2 71  ? -33.204 2.539   -4.911  1.00 48.34  ? 80  CYS   B O   1 
ATOM   945  C CB  . CYS   B 2 71  ? -32.429 4.701   -6.724  1.00 46.32  ? 80  CYS   B CB  1 
ATOM   946  S SG  . CYS   B 2 71  ? -31.988 6.369   -7.244  1.00 56.26  ? 80  CYS   B SG  1 
ATOM   947  N N   . GLY   B 2 72  ? -31.054 1.898   -5.247  1.00 45.17  ? 81  GLY   B N   1 
ATOM   948  C CA  . GLY   B 2 72  ? -31.345 0.488   -4.985  1.00 44.40  ? 81  GLY   B CA  1 
ATOM   949  C C   . GLY   B 2 72  ? -30.098 -0.360  -5.125  1.00 42.46  ? 81  GLY   B C   1 
ATOM   950  O O   . GLY   B 2 72  ? -29.008 0.136   -5.399  1.00 46.84  ? 81  GLY   B O   1 
ATOM   951  N N   . PRO   B 2 73  ? -30.241 -1.664  -4.853  1.00 42.07  ? 82  PRO   B N   1 
ATOM   952  C CA  . PRO   B 2 73  ? -29.117 -2.597  -4.895  1.00 45.66  ? 82  PRO   B CA  1 
ATOM   953  C C   . PRO   B 2 73  ? -28.628 -2.871  -6.330  1.00 46.86  ? 82  PRO   B C   1 
ATOM   954  O O   . PRO   B 2 73  ? -29.415 -2.666  -7.259  1.00 49.12  ? 82  PRO   B O   1 
ATOM   955  C CB  . PRO   B 2 73  ? -29.709 -3.851  -4.241  1.00 42.30  ? 82  PRO   B CB  1 
ATOM   956  C CG  . PRO   B 2 73  ? -31.188 -3.773  -4.500  1.00 42.22  ? 82  PRO   B CG  1 
ATOM   957  C CD  . PRO   B 2 73  ? -31.518 -2.297  -4.506  1.00 42.81  ? 82  PRO   B CD  1 
ATOM   958  N N   . TRP   B 2 74  ? -27.360 -3.287  -6.476  1.00 45.19  ? 83  TRP   B N   1 
ATOM   959  C CA  . TRP   B 2 74  ? -26.724 -3.609  -7.776  1.00 45.01  ? 83  TRP   B CA  1 
ATOM   960  C C   . TRP   B 2 74  ? -27.590 -4.639  -8.508  1.00 42.56  ? 83  TRP   B C   1 
ATOM   961  O O   . TRP   B 2 74  ? -27.951 -5.628  -7.892  1.00 46.64  ? 83  TRP   B O   1 
ATOM   962  C CB  . TRP   B 2 74  ? -25.298 -4.107  -7.563  1.00 46.14  ? 83  TRP   B CB  1 
ATOM   963  C CG  . TRP   B 2 74  ? -24.553 -4.288  -8.845  1.00 45.18  ? 83  TRP   B CG  1 
ATOM   964  C CD1 . TRP   B 2 74  ? -24.528 -5.394  -9.658  1.00 42.82  ? 83  TRP   B CD1 1 
ATOM   965  C CD2 . TRP   B 2 74  ? -23.727 -3.295  -9.476  1.00 44.81  ? 83  TRP   B CD2 1 
ATOM   966  N NE1 . TRP   B 2 74  ? -23.757 -5.141  -10.761 1.00 42.58  ? 83  TRP   B NE1 1 
ATOM   967  C CE2 . TRP   B 2 74  ? -23.251 -3.867  -10.674 1.00 43.18  ? 83  TRP   B CE2 1 
ATOM   968  C CE3 . TRP   B 2 74  ? -23.378 -1.976  -9.160  1.00 44.18  ? 83  TRP   B CE3 1 
ATOM   969  C CZ2 . TRP   B 2 74  ? -22.435 -3.155  -11.549 1.00 42.91  ? 83  TRP   B CZ2 1 
ATOM   970  C CZ3 . TRP   B 2 74  ? -22.552 -1.285  -10.009 1.00 43.88  ? 83  TRP   B CZ3 1 
ATOM   971  C CH2 . TRP   B 2 74  ? -22.096 -1.869  -11.199 1.00 44.68  ? 83  TRP   B CH2 1 
ATOM   972  N N   . LYS   B 2 75  ? -27.937 -4.374  -9.766  1.00 44.87  ? 84  LYS   B N   1 
ATOM   973  C CA  . LYS   B 2 75  ? -28.955 -5.123  -10.558 1.00 46.26  ? 84  LYS   B CA  1 
ATOM   974  C C   . LYS   B 2 75  ? -28.323 -5.968  -11.670 1.00 48.04  ? 84  LYS   B C   1 
ATOM   975  O O   . LYS   B 2 75  ? -29.008 -6.881  -12.139 1.00 53.39  ? 84  LYS   B O   1 
ATOM   976  C CB  . LYS   B 2 75  ? -29.909 -4.153  -11.262 1.00 53.28  ? 84  LYS   B CB  1 
ATOM   977  C CG  . LYS   B 2 75  ? -30.787 -3.332  -10.335 1.00 53.11  ? 84  LYS   B CG  1 
ATOM   978  C CD  . LYS   B 2 75  ? -31.767 -4.191  -9.609  1.00 55.48  ? 84  LYS   B CD  1 
ATOM   979  C CE  . LYS   B 2 75  ? -32.573 -3.426  -8.591  1.00 65.96  ? 84  LYS   B CE  1 
ATOM   980  N NZ  . LYS   B 2 75  ? -33.476 -4.350  -7.882  1.00 67.45  ? 84  LYS   B NZ  1 
ATOM   981  N N   . LEU   B 2 76  ? -27.104 -5.653  -12.108 1.00 43.45  ? 85  LEU   B N   1 
ATOM   982  C CA  . LEU   B 2 76  ? -26.490 -6.237  -13.321 1.00 46.49  ? 85  LEU   B CA  1 
ATOM   983  C C   . LEU   B 2 76  ? -25.748 -7.518  -12.902 1.00 48.32  ? 85  LEU   B C   1 
ATOM   984  O O   . LEU   B 2 76  ? -24.820 -7.423  -12.094 1.00 52.50  ? 85  LEU   B O   1 
ATOM   985  C CB  . LEU   B 2 76  ? -25.541 -5.193  -13.928 1.00 52.52  ? 85  LEU   B CB  1 
ATOM   986  C CG  . LEU   B 2 76  ? -26.113 -3.773  -14.061 1.00 50.20  ? 85  LEU   B CG  1 
ATOM   987  C CD1 . LEU   B 2 76  ? -25.050 -2.779  -14.502 1.00 50.63  ? 85  LEU   B CD1 1 
ATOM   988  C CD2 . LEU   B 2 76  ? -27.280 -3.736  -15.020 1.00 51.00  ? 85  LEU   B CD2 1 
ATOM   989  N N   . ASP   B 2 77  ? -26.144 -8.672  -13.417 1.00 53.26  ? 86  ASP   B N   1 
ATOM   990  C CA  . ASP   B 2 77  ? -25.553 -9.974  -13.002 1.00 65.32  ? 86  ASP   B CA  1 
ATOM   991  C C   . ASP   B 2 77  ? -25.088 -10.799 -14.213 1.00 60.61  ? 86  ASP   B C   1 
ATOM   992  O O   . ASP   B 2 77  ? -24.675 -11.930 -14.008 1.00 66.13  ? 86  ASP   B O   1 
ATOM   993  C CB  . ASP   B 2 77  ? -26.558 -10.779 -12.175 1.00 66.61  ? 86  ASP   B CB  1 
ATOM   994  C CG  . ASP   B 2 77  ? -27.846 -11.054 -12.923 1.00 73.42  ? 86  ASP   B CG  1 
ATOM   995  O OD1 . ASP   B 2 77  ? -28.080 -10.388 -13.942 1.00 79.92  ? 86  ASP   B OD1 1 
ATOM   996  O OD2 . ASP   B 2 77  ? -28.608 -11.922 -12.477 1.00 91.27  ? 86  ASP   B OD2 1 
ATOM   997  N N   . ALA   B 2 78  ? -25.150 -10.303 -15.442 1.00 59.77  ? 87  ALA   B N   1 
ATOM   998  C CA  . ALA   B 2 78  ? -24.614 -11.076 -16.581 1.00 50.41  ? 87  ALA   B CA  1 
ATOM   999  C C   . ALA   B 2 78  ? -23.078 -11.075 -16.499 1.00 54.23  ? 87  ALA   B C   1 
ATOM   1000 O O   . ALA   B 2 78  ? -22.470 -10.062 -16.009 1.00 49.03  ? 87  ALA   B O   1 
ATOM   1001 C CB  . ALA   B 2 78  ? -25.122 -10.545 -17.900 1.00 45.36  ? 87  ALA   B CB  1 
ATOM   1002 N N   . ALA   B 2 79  ? -22.471 -12.128 -17.070 1.00 55.86  ? 88  ALA   B N   1 
ATOM   1003 C CA  . ALA   B 2 79  ? -21.022 -12.432 -17.026 1.00 49.95  ? 88  ALA   B CA  1 
ATOM   1004 C C   . ALA   B 2 79  ? -20.458 -12.772 -18.420 1.00 44.42  ? 88  ALA   B C   1 
ATOM   1005 O O   . ALA   B 2 79  ? -21.134 -13.427 -19.201 1.00 45.33  ? 88  ALA   B O   1 
ATOM   1006 C CB  . ALA   B 2 79  ? -20.859 -13.585 -16.074 1.00 57.46  ? 88  ALA   B CB  1 
ATOM   1007 N N   . TRP   B 2 80  ? -19.273 -12.288 -18.757 1.00 42.56  ? 89  TRP   B N   1 
ATOM   1008 C CA  . TRP   B 2 80  ? -18.492 -12.745 -19.947 1.00 54.23  ? 89  TRP   B CA  1 
ATOM   1009 C C   . TRP   B 2 80  ? -18.426 -14.282 -19.942 1.00 55.90  ? 89  TRP   B C   1 
ATOM   1010 O O   . TRP   B 2 80  ? -18.242 -14.850 -18.846 1.00 48.94  ? 89  TRP   B O   1 
ATOM   1011 C CB  . TRP   B 2 80  ? -17.080 -12.138 -19.971 1.00 52.32  ? 89  TRP   B CB  1 
ATOM   1012 C CG  . TRP   B 2 80  ? -16.307 -12.493 -21.203 1.00 55.69  ? 89  TRP   B CG  1 
ATOM   1013 C CD1 . TRP   B 2 80  ? -16.793 -12.530 -22.471 1.00 55.10  ? 89  TRP   B CD1 1 
ATOM   1014 C CD2 . TRP   B 2 80  ? -14.925 -12.889 -21.293 1.00 60.38  ? 89  TRP   B CD2 1 
ATOM   1015 N NE1 . TRP   B 2 80  ? -15.814 -12.901 -23.345 1.00 63.07  ? 89  TRP   B NE1 1 
ATOM   1016 C CE2 . TRP   B 2 80  ? -14.660 -13.144 -22.655 1.00 59.15  ? 89  TRP   B CE2 1 
ATOM   1017 C CE3 . TRP   B 2 80  ? -13.889 -13.073 -20.369 1.00 55.77  ? 89  TRP   B CE3 1 
ATOM   1018 C CZ2 . TRP   B 2 80  ? -13.402 -13.534 -23.116 1.00 60.44  ? 89  TRP   B CZ2 1 
ATOM   1019 C CZ3 . TRP   B 2 80  ? -12.638 -13.436 -20.830 1.00 59.54  ? 89  TRP   B CZ3 1 
ATOM   1020 C CH2 . TRP   B 2 80  ? -12.398 -13.666 -22.188 1.00 56.54  ? 89  TRP   B CH2 1 
ATOM   1021 N N   . ASP   B 2 81  ? -18.657 -14.930 -21.089 1.00 55.71  ? 90  ASP   B N   1 
ATOM   1022 C CA  . ASP   B 2 81  ? -18.822 -16.410 -21.143 1.00 58.95  ? 90  ASP   B CA  1 
ATOM   1023 C C   . ASP   B 2 81  ? -17.432 -17.058 -21.194 1.00 63.10  ? 90  ASP   B C   1 
ATOM   1024 O O   . ASP   B 2 81  ? -17.363 -18.279 -20.976 1.00 71.36  ? 90  ASP   B O   1 
ATOM   1025 C CB  . ASP   B 2 81  ? -19.664 -16.866 -22.330 1.00 52.09  ? 90  ASP   B CB  1 
ATOM   1026 C CG  . ASP   B 2 81  ? -19.062 -16.503 -23.665 1.00 53.42  ? 90  ASP   B CG  1 
ATOM   1027 O OD1 . ASP   B 2 81  ? -17.949 -15.896 -23.701 1.00 63.07  ? 90  ASP   B OD1 1 
ATOM   1028 O OD2 . ASP   B 2 81  ? -19.714 -16.801 -24.668 1.00 67.26  ? 90  ASP   B OD2 1 
ATOM   1029 N N   . GLY   B 2 82  ? -16.398 -16.262 -21.484 1.00 60.23  ? 91  GLY   B N   1 
ATOM   1030 C CA  . GLY   B 2 82  ? -14.985 -16.669 -21.519 1.00 59.80  ? 91  GLY   B CA  1 
ATOM   1031 C C   . GLY   B 2 82  ? -14.492 -16.920 -22.933 1.00 62.02  ? 91  GLY   B C   1 
ATOM   1032 O O   . GLY   B 2 82  ? -13.314 -17.264 -23.066 1.00 60.04  ? 91  GLY   B O   1 
ATOM   1033 N N   . LEU   B 2 83  ? -15.345 -16.730 -23.944 1.00 60.92  ? 92  LEU   B N   1 
ATOM   1034 C CA  . LEU   B 2 83  ? -15.093 -17.119 -25.360 1.00 63.96  ? 92  LEU   B CA  1 
ATOM   1035 C C   . LEU   B 2 83  ? -15.358 -15.976 -26.354 1.00 66.69  ? 92  LEU   B C   1 
ATOM   1036 O O   . LEU   B 2 83  ? -14.530 -15.756 -27.264 1.00 52.19  ? 92  LEU   B O   1 
ATOM   1037 C CB  . LEU   B 2 83  ? -16.041 -18.274 -25.680 1.00 70.41  ? 92  LEU   B CB  1 
ATOM   1038 C CG  . LEU   B 2 83  ? -15.580 -19.664 -25.261 1.00 76.03  ? 92  LEU   B CG  1 
ATOM   1039 C CD1 . LEU   B 2 83  ? -16.525 -20.712 -25.836 1.00 73.01  ? 92  LEU   B CD1 1 
ATOM   1040 C CD2 . LEU   B 2 83  ? -14.130 -19.933 -25.688 1.00 71.30  ? 92  LEU   B CD2 1 
ATOM   1041 N N   . SER   B 2 84  ? -16.512 -15.313 -26.235 1.00 68.27  ? 93  SER   B N   1 
ATOM   1042 C CA  . SER   B 2 84  ? -17.102 -14.462 -27.300 1.00 58.32  ? 93  SER   B CA  1 
ATOM   1043 C C   . SER   B 2 84  ? -16.448 -13.077 -27.356 1.00 60.53  ? 93  SER   B C   1 
ATOM   1044 O O   . SER   B 2 84  ? -15.870 -12.619 -26.343 1.00 59.70  ? 93  SER   B O   1 
ATOM   1045 C CB  . SER   B 2 84  ? -18.565 -14.380 -27.082 1.00 66.52  ? 93  SER   B CB  1 
ATOM   1046 O OG  . SER   B 2 84  ? -19.047 -15.625 -26.579 1.00 71.88  ? 93  SER   B OG  1 
ATOM   1047 N N   . GLU   B 2 85  ? -16.522 -12.427 -28.518 1.00 61.67  ? 94  GLU   B N   1 
ATOM   1048 C CA  . GLU   B 2 85  ? -16.308 -10.959 -28.611 1.00 68.29  ? 94  GLU   B CA  1 
ATOM   1049 C C   . GLU   B 2 85  ? -17.417 -10.298 -27.764 1.00 54.80  ? 94  GLU   B C   1 
ATOM   1050 O O   . GLU   B 2 85  ? -18.485 -10.941 -27.464 1.00 46.34  ? 94  GLU   B O   1 
ATOM   1051 C CB  . GLU   B 2 85  ? -16.236 -10.464 -30.068 1.00 70.77  ? 94  GLU   B CB  1 
ATOM   1052 C CG  . GLU   B 2 85  ? -15.184 -11.171 -30.932 1.00 80.03  ? 94  GLU   B CG  1 
ATOM   1053 C CD  . GLU   B 2 85  ? -14.405 -10.337 -31.951 1.00 85.92  ? 94  GLU   B CD  1 
ATOM   1054 O OE1 . GLU   B 2 85  ? -14.982 -9.410  -32.563 1.00 79.54  ? 94  GLU   B OE1 1 
ATOM   1055 O OE2 . GLU   B 2 85  ? -13.202 -10.616 -32.144 1.00 80.62  ? 94  GLU   B OE2 1 
ATOM   1056 N N   . VAL   B 2 86  ? -17.119 -9.105  -27.284 1.00 54.70  ? 95  VAL   B N   1 
ATOM   1057 C CA  . VAL   B 2 86  ? -18.037 -8.233  -26.486 1.00 53.65  ? 95  VAL   B CA  1 
ATOM   1058 C C   . VAL   B 2 86  ? -18.110 -6.859  -27.174 1.00 53.41  ? 95  VAL   B C   1 
ATOM   1059 O O   . VAL   B 2 86  ? -17.305 -6.632  -28.090 1.00 49.10  ? 95  VAL   B O   1 
ATOM   1060 C CB  . VAL   B 2 86  ? -17.506 -8.101  -25.041 1.00 41.92  ? 95  VAL   B CB  1 
ATOM   1061 C CG1 . VAL   B 2 86  ? -17.405 -9.451  -24.393 1.00 44.60  ? 95  VAL   B CG1 1 
ATOM   1062 C CG2 . VAL   B 2 86  ? -16.161 -7.386  -24.963 1.00 43.19  ? 95  VAL   B CG2 1 
ATOM   1063 N N   . GLN   B 2 87  ? -18.949 -5.936  -26.686 1.00 57.48  ? 96  GLN   B N   1 
ATOM   1064 C CA  . GLN   B 2 87  ? -18.882 -4.514  -27.125 1.00 53.74  ? 96  GLN   B CA  1 
ATOM   1065 C C   . GLN   B 2 87  ? -18.780 -3.572  -25.913 1.00 46.72  ? 96  GLN   B C   1 
ATOM   1066 O O   . GLN   B 2 87  ? -19.580 -3.700  -24.947 1.00 51.76  ? 96  GLN   B O   1 
ATOM   1067 C CB  . GLN   B 2 87  ? -20.066 -4.210  -28.045 1.00 55.73  ? 96  GLN   B CB  1 
ATOM   1068 C CG  . GLN   B 2 87  ? -19.919 -4.837  -29.430 1.00 61.98  ? 96  GLN   B CG  1 
ATOM   1069 C CD  . GLN   B 2 87  ? -21.039 -4.505  -30.387 1.00 63.50  ? 96  GLN   B CD  1 
ATOM   1070 O OE1 . GLN   B 2 87  ? -21.822 -3.585  -30.173 1.00 57.77  ? 96  GLN   B OE1 1 
ATOM   1071 N NE2 . GLN   B 2 87  ? -21.126 -5.270  -31.462 1.00 62.65  ? 96  GLN   B NE2 1 
ATOM   1072 N N   . LEU   B 2 88  ? -17.771 -2.717  -25.955 1.00 42.00  ? 97  LEU   B N   1 
ATOM   1073 C CA  . LEU   B 2 88  ? -17.683 -1.476  -25.153 1.00 50.05  ? 97  LEU   B CA  1 
ATOM   1074 C C   . LEU   B 2 88  ? -18.564 -0.401  -25.793 1.00 53.09  ? 97  LEU   B C   1 
ATOM   1075 O O   . LEU   B 2 88  ? -18.258 0.040   -26.944 1.00 49.27  ? 97  LEU   B O   1 
ATOM   1076 C CB  . LEU   B 2 88  ? -16.241 -0.983  -25.094 1.00 48.42  ? 97  LEU   B CB  1 
ATOM   1077 C CG  . LEU   B 2 88  ? -16.076 0.365   -24.393 1.00 53.73  ? 97  LEU   B CG  1 
ATOM   1078 C CD1 . LEU   B 2 88  ? -16.462 0.287   -22.919 1.00 54.83  ? 97  LEU   B CD1 1 
ATOM   1079 C CD2 . LEU   B 2 88  ? -14.663 0.891   -24.552 1.00 51.88  ? 97  LEU   B CD2 1 
ATOM   1080 N N   . LEU   B 2 89  ? -19.630 -0.019  -25.104 1.00 50.23  ? 98  LEU   B N   1 
ATOM   1081 C CA  . LEU   B 2 89  ? -20.426 1.180   -25.464 1.00 45.40  ? 98  LEU   B CA  1 
ATOM   1082 C C   . LEU   B 2 89  ? -19.712 2.390   -24.889 1.00 48.05  ? 98  LEU   B C   1 
ATOM   1083 O O   . LEU   B 2 89  ? -20.137 2.860   -23.803 1.00 47.82  ? 98  LEU   B O   1 
ATOM   1084 C CB  . LEU   B 2 89  ? -21.833 1.015   -24.901 1.00 51.56  ? 98  LEU   B CB  1 
ATOM   1085 C CG  . LEU   B 2 89  ? -22.902 2.000   -25.384 1.00 54.36  ? 98  LEU   B CG  1 
ATOM   1086 C CD1 . LEU   B 2 89  ? -22.746 2.315   -26.859 1.00 65.77  ? 98  LEU   B CD1 1 
ATOM   1087 C CD2 . LEU   B 2 89  ? -24.291 1.421   -25.133 1.00 57.91  ? 98  LEU   B CD2 1 
ATOM   1088 N N   . ALA   B 2 90  ? -18.627 2.823   -25.536 1.00 42.63  ? 99  ALA   B N   1 
ATOM   1089 C CA  . ALA   B 2 90  ? -17.845 4.015   -25.117 1.00 47.49  ? 99  ALA   B CA  1 
ATOM   1090 C C   . ALA   B 2 90  ? -18.720 5.272   -25.190 1.00 53.95  ? 99  ALA   B C   1 
ATOM   1091 O O   . ALA   B 2 90  ? -19.306 5.541   -26.267 1.00 59.70  ? 99  ALA   B O   1 
ATOM   1092 C CB  . ALA   B 2 90  ? -16.637 4.217   -25.981 1.00 41.97  ? 99  ALA   B CB  1 
ATOM   1093 N N   . VAL   B 2 91  ? -18.743 6.049   -24.114 1.00 50.60  ? 100 VAL   B N   1 
ATOM   1094 C CA  . VAL   B 2 91  ? -19.317 7.416   -24.113 1.00 41.80  ? 100 VAL   B CA  1 
ATOM   1095 C C   . VAL   B 2 91  ? -18.217 8.383   -23.714 1.00 48.71  ? 100 VAL   B C   1 
ATOM   1096 O O   . VAL   B 2 91  ? -18.077 8.729   -22.547 1.00 48.28  ? 100 VAL   B O   1 
ATOM   1097 C CB  . VAL   B 2 91  ? -20.543 7.477   -23.202 1.00 48.89  ? 100 VAL   B CB  1 
ATOM   1098 C CG1 . VAL   B 2 91  ? -21.188 8.856   -23.239 1.00 54.28  ? 100 VAL   B CG1 1 
ATOM   1099 C CG2 . VAL   B 2 91  ? -21.557 6.387   -23.572 1.00 46.86  ? 100 VAL   B CG2 1 
ATOM   1100 N N   . PRO   B 2 92  ? -17.389 8.853   -24.672 1.00 47.30  ? 101 PRO   B N   1 
ATOM   1101 C CA  . PRO   B 2 92  ? -16.256 9.701   -24.335 1.00 49.83  ? 101 PRO   B CA  1 
ATOM   1102 C C   . PRO   B 2 92  ? -16.736 11.122  -24.098 1.00 54.31  ? 101 PRO   B C   1 
ATOM   1103 O O   . PRO   B 2 92  ? -17.783 11.520  -24.614 1.00 53.10  ? 101 PRO   B O   1 
ATOM   1104 C CB  . PRO   B 2 92  ? -15.339 9.630   -25.571 1.00 49.82  ? 101 PRO   B CB  1 
ATOM   1105 C CG  . PRO   B 2 92  ? -15.961 8.579   -26.459 1.00 52.60  ? 101 PRO   B CG  1 
ATOM   1106 C CD  . PRO   B 2 92  ? -17.436 8.547   -26.107 1.00 55.21  ? 101 PRO   B CD  1 
ATOM   1107 N N   . PRO   B 2 93  ? -15.971 11.942  -23.349 1.00 55.24  ? 102 PRO   B N   1 
ATOM   1108 C CA  . PRO   B 2 93  ? -16.343 13.346  -23.164 1.00 59.81  ? 102 PRO   B CA  1 
ATOM   1109 C C   . PRO   B 2 93  ? -16.579 14.052  -24.513 1.00 63.40  ? 102 PRO   B C   1 
ATOM   1110 O O   . PRO   B 2 93  ? -15.832 13.839  -25.450 1.00 63.27  ? 102 PRO   B O   1 
ATOM   1111 C CB  . PRO   B 2 93  ? -15.169 13.941  -22.380 1.00 53.88  ? 102 PRO   B CB  1 
ATOM   1112 C CG  . PRO   B 2 93  ? -14.572 12.726  -21.660 1.00 61.37  ? 102 PRO   B CG  1 
ATOM   1113 C CD  . PRO   B 2 93  ? -14.745 11.571  -22.627 1.00 54.40  ? 102 PRO   B CD  1 
ATOM   1114 N N   . GLY   B 2 94  ? -17.663 14.826  -24.588 1.00 63.78  ? 103 GLY   B N   1 
ATOM   1115 C CA  . GLY   B 2 94  ? -17.973 15.728  -25.710 1.00 59.44  ? 103 GLY   B CA  1 
ATOM   1116 C C   . GLY   B 2 94  ? -18.260 14.997  -27.011 1.00 55.77  ? 103 GLY   B C   1 
ATOM   1117 O O   . GLY   B 2 94  ? -18.451 15.687  -28.003 1.00 78.88  ? 103 GLY   B O   1 
ATOM   1118 N N   . GLU   B 2 95  ? -18.332 13.665  -27.021 1.00 56.53  ? 104 GLU   B N   1 
ATOM   1119 C CA  . GLU   B 2 95  ? -18.453 12.858  -28.258 1.00 53.97  ? 104 GLU   B CA  1 
ATOM   1120 C C   . GLU   B 2 95  ? -19.607 11.873  -28.101 1.00 48.07  ? 104 GLU   B C   1 
ATOM   1121 O O   . GLU   B 2 95  ? -19.936 11.554  -26.964 1.00 46.27  ? 104 GLU   B O   1 
ATOM   1122 C CB  . GLU   B 2 95  ? -17.135 12.136  -28.529 1.00 63.84  ? 104 GLU   B CB  1 
ATOM   1123 C CG  . GLU   B 2 95  ? -15.960 13.083  -28.764 1.00 69.25  ? 104 GLU   B CG  1 
ATOM   1124 C CD  . GLU   B 2 95  ? -14.631 12.356  -28.925 1.00 85.00  ? 104 GLU   B CD  1 
ATOM   1125 O OE1 . GLU   B 2 95  ? -14.667 11.082  -28.934 1.00 62.75  ? 104 GLU   B OE1 1 
ATOM   1126 O OE2 . GLU   B 2 95  ? -13.558 13.051  -29.041 1.00 81.51  ? 104 GLU   B OE2 1 
ATOM   1127 N N   . ARG   B 2 96  ? -20.197 11.438  -29.218 1.00 46.17  ? 105 ARG   B N   1 
ATOM   1128 C CA  . ARG   B 2 96  ? -21.400 10.574  -29.244 1.00 53.38  ? 105 ARG   B CA  1 
ATOM   1129 C C   . ARG   B 2 96  ? -21.016 9.156   -28.816 1.00 60.19  ? 105 ARG   B C   1 
ATOM   1130 O O   . ARG   B 2 96  ? -19.857 8.756   -28.993 1.00 58.12  ? 105 ARG   B O   1 
ATOM   1131 C CB  . ARG   B 2 96  ? -22.052 10.608  -30.632 1.00 61.33  ? 105 ARG   B CB  1 
ATOM   1132 C CG  . ARG   B 2 96  ? -23.348 9.806   -30.743 1.00 71.75  ? 105 ARG   B CG  1 
ATOM   1133 C CD  . ARG   B 2 96  ? -24.218 10.116  -31.964 1.00 77.21  ? 105 ARG   B CD  1 
ATOM   1134 N NE  . ARG   B 2 96  ? -23.512 10.180  -33.238 1.00 75.51  ? 105 ARG   B NE  1 
ATOM   1135 C CZ  . ARG   B 2 96  ? -22.964 11.279  -33.776 1.00 91.42  ? 105 ARG   B CZ  1 
ATOM   1136 N NH1 . ARG   B 2 96  ? -23.022 12.455  -33.167 1.00 97.09  ? 105 ARG   B NH1 1 
ATOM   1137 N NH2 . ARG   B 2 96  ? -22.356 11.199  -34.946 1.00 93.52  ? 105 ARG   B NH2 1 
ATOM   1138 N N   . ALA   B 2 97  ? -21.992 8.436   -28.278 1.00 62.55  ? 106 ALA   B N   1 
ATOM   1139 C CA  . ALA   B 2 97  ? -21.891 7.019   -27.896 1.00 62.51  ? 106 ALA   B CA  1 
ATOM   1140 C C   . ALA   B 2 97  ? -21.498 6.221   -29.141 1.00 65.99  ? 106 ALA   B C   1 
ATOM   1141 O O   . ALA   B 2 97  ? -21.903 6.593   -30.241 1.00 74.32  ? 106 ALA   B O   1 
ATOM   1142 C CB  . ALA   B 2 97  ? -23.194 6.551   -27.296 1.00 53.31  ? 106 ALA   B CB  1 
ATOM   1143 N N   . LYS   B 2 98  ? -20.757 5.139   -28.938 1.00 70.01  ? 107 LYS   B N   1 
ATOM   1144 C CA  . LYS   B 2 98  ? -20.082 4.370   -30.002 1.00 68.38  ? 107 LYS   B CA  1 
ATOM   1145 C C   . LYS   B 2 98  ? -19.796 2.971   -29.459 1.00 62.95  ? 107 LYS   B C   1 
ATOM   1146 O O   . LYS   B 2 98  ? -19.184 2.890   -28.372 1.00 55.73  ? 107 LYS   B O   1 
ATOM   1147 C CB  . LYS   B 2 98  ? -18.813 5.147   -30.341 1.00 83.91  ? 107 LYS   B CB  1 
ATOM   1148 C CG  . LYS   B 2 98  ? -17.961 4.568   -31.459 1.00 98.55  ? 107 LYS   B CG  1 
ATOM   1149 C CD  . LYS   B 2 98  ? -16.701 5.375   -31.713 1.00 101.20 ? 107 LYS   B CD  1 
ATOM   1150 C CE  . LYS   B 2 98  ? -15.993 5.786   -30.437 1.00 99.05  ? 107 LYS   B CE  1 
ATOM   1151 N NZ  . LYS   B 2 98  ? -14.597 6.207   -30.694 1.00 99.77  ? 107 LYS   B NZ  1 
ATOM   1152 N N   . ASN   B 2 99  ? -20.290 1.931   -30.135 1.00 56.87  ? 108 ASN   B N   1 
ATOM   1153 C CA  . ASN   B 2 99  ? -19.948 0.514   -29.844 1.00 62.27  ? 108 ASN   B CA  1 
ATOM   1154 C C   . ASN   B 2 99  ? -18.564 0.199   -30.430 1.00 63.28  ? 108 ASN   B C   1 
ATOM   1155 O O   . ASN   B 2 99  ? -18.337 0.541   -31.580 1.00 67.82  ? 108 ASN   B O   1 
ATOM   1156 C CB  . ASN   B 2 99  ? -20.999 -0.469  -30.358 1.00 59.37  ? 108 ASN   B CB  1 
ATOM   1157 C CG  . ASN   B 2 99  ? -22.378 -0.246  -29.768 1.00 64.90  ? 108 ASN   B CG  1 
ATOM   1158 O OD1 . ASN   B 2 99  ? -22.943 0.832   -29.918 1.00 65.62  ? 108 ASN   B OD1 1 
ATOM   1159 N ND2 . ASN   B 2 99  ? -22.963 -1.268  -29.151 1.00 65.87  ? 108 ASN   B ND2 1 
ATOM   1160 N N   . ILE   B 2 100 ? -17.660 -0.413  -29.656 1.00 64.03  ? 109 ILE   B N   1 
ATOM   1161 C CA  . ILE   B 2 100 ? -16.388 -1.018  -30.160 1.00 57.08  ? 109 ILE   B CA  1 
ATOM   1162 C C   . ILE   B 2 100 ? -16.401 -2.512  -29.825 1.00 61.56  ? 109 ILE   B C   1 
ATOM   1163 O O   . ILE   B 2 100 ? -16.583 -2.881  -28.632 1.00 59.64  ? 109 ILE   B O   1 
ATOM   1164 C CB  . ILE   B 2 100 ? -15.165 -0.328  -29.562 1.00 60.91  ? 109 ILE   B CB  1 
ATOM   1165 C CG1 . ILE   B 2 100 ? -15.286 1.194   -29.562 1.00 66.35  ? 109 ILE   B CG1 1 
ATOM   1166 C CG2 . ILE   B 2 100 ? -13.915 -0.780  -30.274 1.00 69.56  ? 109 ILE   B CG2 1 
ATOM   1167 C CD1 . ILE   B 2 100 ? -14.962 1.837   -30.880 1.00 76.84  ? 109 ILE   B CD1 1 
ATOM   1168 N N   . GLN   B 2 101 ? -16.274 -3.355  -30.840 1.00 54.11  ? 110 GLN   B N   1 
ATOM   1169 C CA  . GLN   B 2 101 ? -16.248 -4.832  -30.682 1.00 59.96  ? 110 GLN   B CA  1 
ATOM   1170 C C   . GLN   B 2 101 ? -14.793 -5.279  -30.462 1.00 62.71  ? 110 GLN   B C   1 
ATOM   1171 O O   . GLN   B 2 101 ? -13.872 -4.657  -31.063 1.00 57.21  ? 110 GLN   B O   1 
ATOM   1172 C CB  . GLN   B 2 101 ? -16.874 -5.499  -31.898 1.00 63.50  ? 110 GLN   B CB  1 
ATOM   1173 C CG  . GLN   B 2 101 ? -16.985 -6.993  -31.755 1.00 60.58  ? 110 GLN   B CG  1 
ATOM   1174 C CD  . GLN   B 2 101 ? -18.168 -7.561  -32.498 1.00 63.00  ? 110 GLN   B CD  1 
ATOM   1175 O OE1 . GLN   B 2 101 ? -19.183 -6.905  -32.711 1.00 60.79  ? 110 GLN   B OE1 1 
ATOM   1176 N NE2 . GLN   B 2 101 ? -18.063 -8.823  -32.864 1.00 62.50  ? 110 GLN   B NE2 1 
ATOM   1177 N N   . THR   B 2 102 ? -14.592 -6.253  -29.566 1.00 60.46  ? 111 THR   B N   1 
ATOM   1178 C CA  . THR   B 2 102 ? -13.252 -6.703  -29.095 1.00 53.73  ? 111 THR   B CA  1 
ATOM   1179 C C   . THR   B 2 102 ? -13.433 -8.083  -28.497 1.00 51.34  ? 111 THR   B C   1 
ATOM   1180 O O   . THR   B 2 102 ? -14.570 -8.422  -28.139 1.00 55.60  ? 111 THR   B O   1 
ATOM   1181 C CB  . THR   B 2 102 ? -12.592 -5.675  -28.165 1.00 58.21  ? 111 THR   B CB  1 
ATOM   1182 O OG1 . THR   B 2 102 ? -11.179 -5.871  -28.160 1.00 59.41  ? 111 THR   B OG1 1 
ATOM   1183 C CG2 . THR   B 2 102 ? -13.097 -5.700  -26.739 1.00 58.19  ? 111 THR   B CG2 1 
ATOM   1184 N N   . LEU   B 2 103 ? -12.363 -8.874  -28.517 1.00 55.05  ? 112 LEU   B N   1 
ATOM   1185 C CA  . LEU   B 2 103 ? -12.256 -10.119 -27.734 1.00 52.26  ? 112 LEU   B CA  1 
ATOM   1186 C C   . LEU   B 2 103 ? -11.420 -9.777  -26.514 1.00 54.84  ? 112 LEU   B C   1 
ATOM   1187 O O   . LEU   B 2 103 ? -10.260 -9.329  -26.630 1.00 56.70  ? 112 LEU   B O   1 
ATOM   1188 C CB  . LEU   B 2 103 ? -11.595 -11.231 -28.546 1.00 61.43  ? 112 LEU   B CB  1 
ATOM   1189 C CG  . LEU   B 2 103 ? -11.467 -12.532 -27.770 1.00 59.34  ? 112 LEU   B CG  1 
ATOM   1190 C CD1 . LEU   B 2 103 ? -12.790 -13.264 -27.750 1.00 53.26  ? 112 LEU   B CD1 1 
ATOM   1191 C CD2 . LEU   B 2 103 ? -10.357 -13.412 -28.326 1.00 72.93  ? 112 LEU   B CD2 1 
ATOM   1192 N N   . PRO   B 2 104 ? -12.021 -9.909  -25.313 1.00 53.73  ? 113 PRO   B N   1 
ATOM   1193 C CA  . PRO   B 2 104 ? -11.338 -9.523  -24.084 1.00 55.00  ? 113 PRO   B CA  1 
ATOM   1194 C C   . PRO   B 2 104 ? -10.146 -10.467 -23.855 1.00 59.86  ? 113 PRO   B C   1 
ATOM   1195 O O   . PRO   B 2 104 ? -10.266 -11.622 -24.177 1.00 52.66  ? 113 PRO   B O   1 
ATOM   1196 C CB  . PRO   B 2 104 ? -12.343 -9.724  -22.952 1.00 53.04  ? 113 PRO   B CB  1 
ATOM   1197 C CG  . PRO   B 2 104 ? -13.671 -10.019 -23.654 1.00 57.48  ? 113 PRO   B CG  1 
ATOM   1198 C CD  . PRO   B 2 104 ? -13.350 -10.478 -25.066 1.00 53.02  ? 113 PRO   B CD  1 
ATOM   1199 N N   . GLY   B 2 105 ? -9.057  -9.915  -23.319 1.00 55.85  ? 114 GLY   B N   1 
ATOM   1200 C CA  . GLY   B 2 105 ? -7.993  -10.626 -22.603 1.00 54.82  ? 114 GLY   B CA  1 
ATOM   1201 C C   . GLY   B 2 105 ? -8.344  -10.874 -21.146 1.00 54.63  ? 114 GLY   B C   1 
ATOM   1202 O O   . GLY   B 2 105 ? -9.528  -10.941 -20.835 1.00 52.19  ? 114 GLY   B O   1 
ATOM   1203 N N   . ILE   B 2 106 ? -7.330  -11.127 -20.307 1.00 63.11  ? 115 ILE   B N   1 
ATOM   1204 C CA  . ILE   B 2 106 ? -7.491  -11.721 -18.945 1.00 63.16  ? 115 ILE   B CA  1 
ATOM   1205 C C   . ILE   B 2 106 ? -6.586  -11.013 -17.930 1.00 61.13  ? 115 ILE   B C   1 
ATOM   1206 O O   . ILE   B 2 106 ? -5.382  -10.803 -18.201 1.00 68.05  ? 115 ILE   B O   1 
ATOM   1207 C CB  . ILE   B 2 106 ? -7.202  -13.228 -18.958 1.00 65.17  ? 115 ILE   B CB  1 
ATOM   1208 C CG1 . ILE   B 2 106 ? -7.978  -13.972 -20.045 1.00 70.32  ? 115 ILE   B CG1 1 
ATOM   1209 C CG2 . ILE   B 2 106 ? -7.487  -13.802 -17.591 1.00 70.86  ? 115 ILE   B CG2 1 
ATOM   1210 C CD1 . ILE   B 2 106 ? -9.318  -14.503 -19.610 1.00 68.33  ? 115 ILE   B CD1 1 
ATOM   1211 N N   . PHE   B 2 107 ? -7.164  -10.663 -16.785 1.00 61.11  ? 116 PHE   B N   1 
ATOM   1212 C CA  . PHE   B 2 107 ? -6.437  -10.359 -15.525 1.00 59.41  ? 116 PHE   B CA  1 
ATOM   1213 C C   . PHE   B 2 107 ? -6.364  -11.650 -14.706 1.00 59.55  ? 116 PHE   B C   1 
ATOM   1214 O O   . PHE   B 2 107 ? -7.434  -12.157 -14.314 1.00 62.15  ? 116 PHE   B O   1 
ATOM   1215 C CB  . PHE   B 2 107 ? -7.145  -9.234  -14.767 1.00 54.06  ? 116 PHE   B CB  1 
ATOM   1216 C CG  . PHE   B 2 107 ? -6.855  -7.848  -15.272 1.00 57.01  ? 116 PHE   B CG  1 
ATOM   1217 C CD1 . PHE   B 2 107 ? -6.058  -7.631  -16.388 1.00 58.45  ? 116 PHE   B CD1 1 
ATOM   1218 C CD2 . PHE   B 2 107 ? -7.433  -6.749  -14.650 1.00 60.93  ? 116 PHE   B CD2 1 
ATOM   1219 C CE1 . PHE   B 2 107 ? -5.812  -6.344  -16.841 1.00 50.59  ? 116 PHE   B CE1 1 
ATOM   1220 C CE2 . PHE   B 2 107 ? -7.173  -5.464  -15.096 1.00 55.90  ? 116 PHE   B CE2 1 
ATOM   1221 C CZ  . PHE   B 2 107 ? -6.380  -5.267  -16.205 1.00 52.12  ? 116 PHE   B CZ  1 
ATOM   1222 N N   . LYS   B 2 108 ? -5.162  -12.203 -14.543 1.00 67.21  ? 117 LYS   B N   1 
ATOM   1223 C CA  . LYS   B 2 108 ? -4.898  -13.366 -13.657 1.00 70.89  ? 117 LYS   B CA  1 
ATOM   1224 C C   . LYS   B 2 108 ? -4.488  -12.805 -12.290 1.00 59.51  ? 117 LYS   B C   1 
ATOM   1225 O O   . LYS   B 2 108 ? -3.513  -12.021 -12.242 1.00 57.57  ? 117 LYS   B O   1 
ATOM   1226 C CB  . LYS   B 2 108 ? -3.802  -14.267 -14.239 1.00 84.01  ? 117 LYS   B CB  1 
ATOM   1227 C CG  . LYS   B 2 108 ? -4.215  -15.189 -15.383 1.00 96.74  ? 117 LYS   B CG  1 
ATOM   1228 C CD  . LYS   B 2 108 ? -3.040  -15.850 -16.107 1.00 105.03 ? 117 LYS   B CD  1 
ATOM   1229 C CE  . LYS   B 2 108 ? -3.426  -16.494 -17.428 1.00 121.43 ? 117 LYS   B CE  1 
ATOM   1230 N NZ  . LYS   B 2 108 ? -2.255  -16.959 -18.218 1.00 119.80 ? 117 LYS   B NZ  1 
ATOM   1231 N N   . THR   B 2 109 ? -5.230  -13.162 -11.244 1.00 56.55  ? 118 THR   B N   1 
ATOM   1232 C CA  . THR   B 2 109 ? -5.022  -12.712 -9.846  1.00 61.02  ? 118 THR   B CA  1 
ATOM   1233 C C   . THR   B 2 109 ? -5.115  -13.939 -8.948  1.00 63.41  ? 118 THR   B C   1 
ATOM   1234 O O   . THR   B 2 109 ? -5.793  -14.913 -9.348  1.00 56.17  ? 118 THR   B O   1 
ATOM   1235 C CB  . THR   B 2 109 ? -6.098  -11.708 -9.398  1.00 59.52  ? 118 THR   B CB  1 
ATOM   1236 O OG1 . THR   B 2 109 ? -7.285  -12.403 -9.016  1.00 52.13  ? 118 THR   B OG1 1 
ATOM   1237 C CG2 . THR   B 2 109 ? -6.457  -10.715 -10.480 1.00 57.54  ? 118 THR   B CG2 1 
ATOM   1238 N N   . LYS   B 2 110 ? -4.572  -13.836 -7.738  1.00 65.23  ? 119 LYS   B N   1 
ATOM   1239 C CA  . LYS   B 2 110 ? -4.596  -14.919 -6.712  1.00 66.37  ? 119 LYS   B CA  1 
ATOM   1240 C C   . LYS   B 2 110 ? -6.039  -15.398 -6.463  1.00 70.73  ? 119 LYS   B C   1 
ATOM   1241 O O   . LYS   B 2 110 ? -6.236  -16.561 -6.057  1.00 62.84  ? 119 LYS   B O   1 
ATOM   1242 C CB  . LYS   B 2 110 ? -3.917  -14.438 -5.422  1.00 71.98  ? 119 LYS   B CB  1 
ATOM   1243 C CG  . LYS   B 2 110 ? -4.408  -13.107 -4.858  1.00 78.43  ? 119 LYS   B CG  1 
ATOM   1244 C CD  . LYS   B 2 110 ? -3.624  -12.634 -3.644  1.00 76.83  ? 119 LYS   B CD  1 
ATOM   1245 C CE  . LYS   B 2 110 ? -4.137  -13.225 -2.347  1.00 80.91  ? 119 LYS   B CE  1 
ATOM   1246 N NZ  . LYS   B 2 110 ? -5.305  -12.476 -1.820  1.00 77.22  ? 119 LYS   B NZ  1 
ATOM   1247 N N   . ASP   B 2 111 ? -7.037  -14.554 -6.700  1.00 66.17  ? 120 ASP   B N   1 
ATOM   1248 C CA  . ASP   B 2 111 ? -8.430  -14.860 -6.315  1.00 67.12  ? 120 ASP   B CA  1 
ATOM   1249 C C   . ASP   B 2 111 ? -9.213  -15.299 -7.548  1.00 67.49  ? 120 ASP   B C   1 
ATOM   1250 O O   . ASP   B 2 111 ? -10.450 -15.375 -7.451  1.00 67.73  ? 120 ASP   B O   1 
ATOM   1251 C CB  . ASP   B 2 111 ? -9.025  -13.660 -5.581  1.00 72.50  ? 120 ASP   B CB  1 
ATOM   1252 C CG  . ASP   B 2 111 ? -8.447  -13.522 -4.186  1.00 76.20  ? 120 ASP   B CG  1 
ATOM   1253 O OD1 . ASP   B 2 111 ? -7.932  -14.531 -3.664  1.00 81.49  ? 120 ASP   B OD1 1 
ATOM   1254 O OD2 . ASP   B 2 111 ? -8.507  -12.418 -3.639  1.00 89.65  ? 120 ASP   B OD2 1 
ATOM   1255 N N   . GLY   B 2 112 ? -8.536  -15.601 -8.654  1.00 62.04  ? 121 GLY   B N   1 
ATOM   1256 C CA  . GLY   B 2 112 ? -9.241  -15.965 -9.891  1.00 60.07  ? 121 GLY   B CA  1 
ATOM   1257 C C   . GLY   B 2 112 ? -8.913  -15.025 -11.028 1.00 64.47  ? 121 GLY   B C   1 
ATOM   1258 O O   . GLY   B 2 112 ? -8.081  -14.086 -10.857 1.00 64.59  ? 121 GLY   B O   1 
ATOM   1259 N N   . ASP   B 2 113 ? -9.514  -15.318 -12.178 1.00 68.11  ? 122 ASP   B N   1 
ATOM   1260 C CA  . ASP   B 2 113 ? -9.271  -14.625 -13.470 1.00 67.45  ? 122 ASP   B CA  1 
ATOM   1261 C C   . ASP   B 2 113 ? -10.448 -13.682 -13.766 1.00 61.83  ? 122 ASP   B C   1 
ATOM   1262 O O   . ASP   B 2 113 ? -11.579 -14.076 -13.500 1.00 56.36  ? 122 ASP   B O   1 
ATOM   1263 C CB  . ASP   B 2 113 ? -9.076  -15.653 -14.588 1.00 72.61  ? 122 ASP   B CB  1 
ATOM   1264 C CG  . ASP   B 2 113 ? -7.728  -16.352 -14.554 1.00 72.41  ? 122 ASP   B CG  1 
ATOM   1265 O OD1 . ASP   B 2 113 ? -6.822  -15.855 -13.863 1.00 77.17  ? 122 ASP   B OD1 1 
ATOM   1266 O OD2 . ASP   B 2 113 ? -7.600  -17.374 -15.234 1.00 80.59  ? 122 ASP   B OD2 1 
ATOM   1267 N N   . ILE   B 2 114 ? -10.165 -12.485 -14.288 1.00 60.83  ? 123 ILE   B N   1 
ATOM   1268 C CA  . ILE   B 2 114 ? -11.171 -11.458 -14.697 1.00 65.77  ? 123 ILE   B CA  1 
ATOM   1269 C C   . ILE   B 2 114 ? -10.977 -11.175 -16.187 1.00 58.07  ? 123 ILE   B C   1 
ATOM   1270 O O   . ILE   B 2 114 ? -9.821  -11.096 -16.602 1.00 52.39  ? 123 ILE   B O   1 
ATOM   1271 C CB  . ILE   B 2 114 ? -11.035 -10.154 -13.869 1.00 64.35  ? 123 ILE   B CB  1 
ATOM   1272 C CG1 . ILE   B 2 114 ? -10.723 -10.432 -12.396 1.00 75.30  ? 123 ILE   B CG1 1 
ATOM   1273 C CG2 . ILE   B 2 114 ? -12.280 -9.295  -14.026 1.00 65.33  ? 123 ILE   B CG2 1 
ATOM   1274 C CD1 . ILE   B 2 114 ? -10.363 -9.213  -11.586 1.00 79.04  ? 123 ILE   B CD1 1 
ATOM   1275 N N   . GLY   B 2 115 ? -12.071 -10.948 -16.917 1.00 54.85  ? 124 GLY   B N   1 
ATOM   1276 C CA  . GLY   B 2 115 ? -12.044 -10.403 -18.288 1.00 46.78  ? 124 GLY   B CA  1 
ATOM   1277 C C   . GLY   B 2 115 ? -11.417 -9.026  -18.292 1.00 46.77  ? 124 GLY   B C   1 
ATOM   1278 O O   . GLY   B 2 115 ? -11.476 -8.324  -17.270 1.00 54.64  ? 124 GLY   B O   1 
ATOM   1279 N N   . ALA   B 2 116 ? -10.730 -8.686  -19.370 1.00 46.04  ? 125 ALA   B N   1 
ATOM   1280 C CA  . ALA   B 2 116 ? -10.103 -7.370  -19.558 1.00 51.43  ? 125 ALA   B CA  1 
ATOM   1281 C C   . ALA   B 2 116 ? -10.296 -6.976  -21.018 1.00 58.00  ? 125 ALA   B C   1 
ATOM   1282 O O   . ALA   B 2 116 ? -10.383 -7.868  -21.904 1.00 57.25  ? 125 ALA   B O   1 
ATOM   1283 C CB  . ALA   B 2 116 ? -8.653  -7.401  -19.188 1.00 49.93  ? 125 ALA   B CB  1 
ATOM   1284 N N   A VAL   B 2 117 ? -10.378 -5.669  -21.274 0.25 57.60  ? 126 VAL   B N   1 
ATOM   1285 N N   B VAL   B 2 117 ? -10.327 -5.662  -21.251 0.25 57.49  ? 126 VAL   B N   1 
ATOM   1286 N N   C VAL   B 2 117 ? -10.378 -5.669  -21.274 0.25 57.60  ? 126 VAL   B N   1 
ATOM   1287 N N   D VAL   B 2 117 ? -10.327 -5.662  -21.251 0.25 57.49  ? 126 VAL   B N   1 
ATOM   1288 C CA  A VAL   B 2 117 ? -10.533 -5.093  -22.640 0.25 57.66  ? 126 VAL   B CA  1 
ATOM   1289 C CA  B VAL   B 2 117 ? -10.544 -5.011  -22.573 0.25 57.24  ? 126 VAL   B CA  1 
ATOM   1290 C CA  C VAL   B 2 117 ? -10.533 -5.093  -22.640 0.25 57.66  ? 126 VAL   B CA  1 
ATOM   1291 C CA  D VAL   B 2 117 ? -10.544 -5.011  -22.573 0.25 57.24  ? 126 VAL   B CA  1 
ATOM   1292 C C   A VAL   B 2 117 ? -9.398  -4.095  -22.867 0.25 57.71  ? 126 VAL   B C   1 
ATOM   1293 C C   B VAL   B 2 117 ? -9.361  -4.081  -22.844 0.25 57.65  ? 126 VAL   B C   1 
ATOM   1294 C C   C VAL   B 2 117 ? -9.398  -4.095  -22.867 0.25 57.71  ? 126 VAL   B C   1 
ATOM   1295 C C   D VAL   B 2 117 ? -9.361  -4.081  -22.844 0.25 57.65  ? 126 VAL   B C   1 
ATOM   1296 O O   A VAL   B 2 117 ? -9.217  -3.210  -22.012 0.25 56.81  ? 126 VAL   B O   1 
ATOM   1297 O O   B VAL   B 2 117 ? -9.113  -3.209  -21.990 0.25 57.03  ? 126 VAL   B O   1 
ATOM   1298 O O   C VAL   B 2 117 ? -9.217  -3.210  -22.012 0.25 56.81  ? 126 VAL   B O   1 
ATOM   1299 O O   D VAL   B 2 117 ? -9.113  -3.209  -21.990 0.25 57.03  ? 126 VAL   B O   1 
ATOM   1300 C CB  A VAL   B 2 117 ? -11.917 -4.444  -22.819 0.25 60.63  ? 126 VAL   B CB  1 
ATOM   1301 C CB  B VAL   B 2 117 ? -11.871 -4.233  -22.573 0.25 60.24  ? 126 VAL   B CB  1 
ATOM   1302 C CB  C VAL   B 2 117 ? -11.917 -4.444  -22.819 0.25 60.63  ? 126 VAL   B CB  1 
ATOM   1303 C CB  D VAL   B 2 117 ? -11.871 -4.233  -22.573 0.25 60.24  ? 126 VAL   B CB  1 
ATOM   1304 C CG1 A VAL   B 2 117 ? -13.030 -5.467  -22.653 0.25 58.62  ? 126 VAL   B CG1 1 
ATOM   1305 C CG1 B VAL   B 2 117 ? -11.845 -3.080  -23.564 0.25 60.07  ? 126 VAL   B CG1 1 
ATOM   1306 C CG1 C VAL   B 2 117 ? -13.030 -5.467  -22.653 0.25 58.62  ? 126 VAL   B CG1 1 
ATOM   1307 C CG1 D VAL   B 2 117 ? -11.845 -3.080  -23.564 0.25 60.07  ? 126 VAL   B CG1 1 
ATOM   1308 C CG2 A VAL   B 2 117 ? -12.117 -3.262  -21.882 0.25 60.74  ? 126 VAL   B CG2 1 
ATOM   1309 C CG2 B VAL   B 2 117 ? -13.058 -5.151  -22.820 0.25 58.34  ? 126 VAL   B CG2 1 
ATOM   1310 C CG2 C VAL   B 2 117 ? -12.117 -3.262  -21.882 0.25 60.74  ? 126 VAL   B CG2 1 
ATOM   1311 C CG2 D VAL   B 2 117 ? -13.058 -5.151  -22.820 0.25 58.34  ? 126 VAL   B CG2 1 
ATOM   1312 N N   . ALA   B 2 118 ? -8.662  -4.261  -23.973 1.00 56.49  ? 127 ALA   B N   1 
ATOM   1313 C CA  . ALA   B 2 118 ? -7.511  -3.404  -24.347 1.00 57.45  ? 127 ALA   B CA  1 
ATOM   1314 C C   . ALA   B 2 118 ? -8.014  -2.306  -25.286 1.00 61.17  ? 127 ALA   B C   1 
ATOM   1315 O O   . ALA   B 2 118 ? -7.954  -2.490  -26.513 1.00 65.64  ? 127 ALA   B O   1 
ATOM   1316 C CB  . ALA   B 2 118 ? -6.423  -4.235  -24.969 1.00 63.83  ? 127 ALA   B CB  1 
ATOM   1317 N N   . LEU   B 2 119 ? -8.585  -1.254  -24.704 1.00 60.33  ? 128 LEU   B N   1 
ATOM   1318 C CA  . LEU   B 2 119 ? -9.127  -0.070  -25.414 1.00 54.83  ? 128 LEU   B CA  1 
ATOM   1319 C C   . LEU   B 2 119 ? -8.802  1.141   -24.549 1.00 59.54  ? 128 LEU   B C   1 
ATOM   1320 O O   . LEU   B 2 119 ? -9.182  1.128   -23.375 1.00 65.70  ? 128 LEU   B O   1 
ATOM   1321 C CB  . LEU   B 2 119 ? -10.625 -0.271  -25.635 1.00 52.30  ? 128 LEU   B CB  1 
ATOM   1322 C CG  . LEU   B 2 119 ? -10.967 -1.497  -26.481 1.00 51.61  ? 128 LEU   B CG  1 
ATOM   1323 C CD1 . LEU   B 2 119 ? -12.448 -1.830  -26.450 1.00 52.27  ? 128 LEU   B CD1 1 
ATOM   1324 C CD2 . LEU   B 2 119 ? -10.487 -1.310  -27.917 1.00 52.95  ? 128 LEU   B CD2 1 
ATOM   1325 N N   . ASP   B 2 120 ? -8.009  2.062   -25.080 1.00 50.56  ? 129 ASP   B N   1 
ATOM   1326 C CA  . ASP   B 2 120 ? -7.593  3.288   -24.378 1.00 53.52  ? 129 ASP   B CA  1 
ATOM   1327 C C   . ASP   B 2 120 ? -8.634  4.372   -24.697 1.00 64.83  ? 129 ASP   B C   1 
ATOM   1328 O O   . ASP   B 2 120 ? -8.739  4.761   -25.870 1.00 64.35  ? 129 ASP   B O   1 
ATOM   1329 C CB  . ASP   B 2 120 ? -6.175  3.655   -24.800 1.00 53.30  ? 129 ASP   B CB  1 
ATOM   1330 C CG  . ASP   B 2 120 ? -5.461  4.596   -23.841 1.00 61.99  ? 129 ASP   B CG  1 
ATOM   1331 O OD1 . ASP   B 2 120 ? -6.126  5.540   -23.314 1.00 67.19  ? 129 ASP   B OD1 1 
ATOM   1332 O OD2 . ASP   B 2 120 ? -4.247  4.381   -23.615 1.00 63.18  ? 129 ASP   B OD2 1 
ATOM   1333 N N   . TYR   B 2 121 ? -9.389  4.842   -23.704 1.00 54.35  ? 130 TYR   B N   1 
ATOM   1334 C CA  . TYR   B 2 121 ? -10.228 6.057   -23.832 1.00 53.35  ? 130 TYR   B CA  1 
ATOM   1335 C C   . TYR   B 2 121 ? -9.951  6.991   -22.667 1.00 55.39  ? 130 TYR   B C   1 
ATOM   1336 O O   . TYR   B 2 121 ? -9.295  6.607   -21.694 1.00 61.61  ? 130 TYR   B O   1 
ATOM   1337 C CB  . TYR   B 2 121 ? -11.705 5.693   -23.919 1.00 57.38  ? 130 TYR   B CB  1 
ATOM   1338 C CG  . TYR   B 2 121 ? -12.115 5.084   -25.234 1.00 60.28  ? 130 TYR   B CG  1 
ATOM   1339 C CD1 . TYR   B 2 121 ? -12.371 5.878   -26.340 1.00 62.56  ? 130 TYR   B CD1 1 
ATOM   1340 C CD2 . TYR   B 2 121 ? -12.245 3.711   -25.381 1.00 62.50  ? 130 TYR   B CD2 1 
ATOM   1341 C CE1 . TYR   B 2 121 ? -12.745 5.324   -27.559 1.00 67.33  ? 130 TYR   B CE1 1 
ATOM   1342 C CE2 . TYR   B 2 121 ? -12.652 3.141   -26.579 1.00 58.38  ? 130 TYR   B CE2 1 
ATOM   1343 C CZ  . TYR   B 2 121 ? -12.902 3.950   -27.677 1.00 71.68  ? 130 TYR   B CZ  1 
ATOM   1344 O OH  . TYR   B 2 121 ? -13.287 3.399   -28.869 1.00 77.89  ? 130 TYR   B OH  1 
ATOM   1345 N N   . PRO   B 2 122 ? -10.381 8.270   -22.762 1.00 53.14  ? 131 PRO   B N   1 
ATOM   1346 C CA  . PRO   B 2 122 ? -10.172 9.227   -21.679 1.00 53.53  ? 131 PRO   B CA  1 
ATOM   1347 C C   . PRO   B 2 122 ? -10.796 8.738   -20.363 1.00 48.15  ? 131 PRO   B C   1 
ATOM   1348 O O   . PRO   B 2 122 ? -11.733 7.959   -20.396 1.00 49.45  ? 131 PRO   B O   1 
ATOM   1349 C CB  . PRO   B 2 122 ? -10.841 10.486  -22.233 1.00 57.18  ? 131 PRO   B CB  1 
ATOM   1350 C CG  . PRO   B 2 122 ? -10.686 10.339  -23.714 1.00 53.38  ? 131 PRO   B CG  1 
ATOM   1351 C CD  . PRO   B 2 122 ? -11.008 8.889   -23.941 1.00 57.61  ? 131 PRO   B CD  1 
ATOM   1352 N N   . ALA   B 2 123 ? -10.221 9.161   -19.246 1.00 48.22  ? 132 ALA   B N   1 
ATOM   1353 C CA  . ALA   B 2 123 ? -10.648 8.763   -17.883 1.00 56.30  ? 132 ALA   B CA  1 
ATOM   1354 C C   . ALA   B 2 123 ? -12.147 9.059   -17.705 1.00 56.50  ? 132 ALA   B C   1 
ATOM   1355 O O   . ALA   B 2 123 ? -12.865 8.232   -17.090 1.00 52.27  ? 132 ALA   B O   1 
ATOM   1356 C CB  . ALA   B 2 123 ? -9.778  9.461   -16.856 1.00 53.83  ? 132 ALA   B CB  1 
ATOM   1357 N N   . GLY   B 2 124 ? -12.643 10.133  -18.325 1.00 53.83  ? 133 GLY   B N   1 
ATOM   1358 C CA  . GLY   B 2 124 ? -14.062 10.545  -18.253 1.00 49.45  ? 133 GLY   B CA  1 
ATOM   1359 C C   . GLY   B 2 124 ? -14.999 9.548   -18.914 1.00 52.43  ? 133 GLY   B C   1 
ATOM   1360 O O   . GLY   B 2 124 ? -16.249 9.788   -18.868 1.00 45.63  ? 133 GLY   B O   1 
ATOM   1361 N N   . THR   B 2 125 ? -14.442 8.495   -19.537 1.00 41.86  ? 134 THR   B N   1 
ATOM   1362 C CA  . THR   B 2 125 ? -15.199 7.377   -20.151 1.00 41.36  ? 134 THR   B CA  1 
ATOM   1363 C C   . THR   B 2 125 ? -15.469 6.286   -19.091 1.00 44.57  ? 134 THR   B C   1 
ATOM   1364 O O   . THR   B 2 125 ? -16.312 5.366   -19.366 1.00 40.70  ? 134 THR   B O   1 
ATOM   1365 C CB  . THR   B 2 125 ? -14.440 6.863   -21.382 1.00 52.85  ? 134 THR   B CB  1 
ATOM   1366 O OG1 . THR   B 2 125 ? -13.885 7.984   -22.077 1.00 60.49  ? 134 THR   B OG1 1 
ATOM   1367 C CG2 . THR   B 2 125 ? -15.313 6.076   -22.327 1.00 52.09  ? 134 THR   B CG2 1 
ATOM   1368 N N   . SER   B 2 126 ? -14.819 6.382   -17.920 1.00 45.11  ? 135 SER   B N   1 
ATOM   1369 C CA  . SER   B 2 126 ? -15.021 5.467   -16.752 1.00 50.02  ? 135 SER   B CA  1 
ATOM   1370 C C   . SER   B 2 126 ? -16.530 5.302   -16.463 1.00 48.35  ? 135 SER   B C   1 
ATOM   1371 O O   . SER   B 2 126 ? -17.218 6.332   -16.268 1.00 50.59  ? 135 SER   B O   1 
ATOM   1372 C CB  . SER   B 2 126 ? -14.283 5.983   -15.533 1.00 49.76  ? 135 SER   B CB  1 
ATOM   1373 O OG  . SER   B 2 126 ? -12.866 5.865   -15.659 1.00 48.37  ? 135 SER   B OG  1 
ATOM   1374 N N   . GLY   B 2 127 ? -17.037 4.066   -16.452 1.00 45.88  ? 136 GLY   B N   1 
ATOM   1375 C CA  . GLY   B 2 127 ? -18.446 3.717   -16.187 1.00 38.81  ? 136 GLY   B CA  1 
ATOM   1376 C C   . GLY   B 2 127 ? -19.167 3.262   -17.424 1.00 41.24  ? 136 GLY   B C   1 
ATOM   1377 O O   . GLY   B 2 127 ? -20.274 2.670   -17.292 1.00 37.65  ? 136 GLY   B O   1 
ATOM   1378 N N   . SER   B 2 128 ? -18.596 3.496   -18.611 1.00 42.31  ? 137 SER   B N   1 
ATOM   1379 C CA  . SER   B 2 128 ? -19.193 2.987   -19.871 1.00 44.50  ? 137 SER   B CA  1 
ATOM   1380 C C   . SER   B 2 128 ? -19.383 1.476   -19.759 1.00 42.81  ? 137 SER   B C   1 
ATOM   1381 O O   . SER   B 2 128 ? -18.516 0.734   -19.326 1.00 42.38  ? 137 SER   B O   1 
ATOM   1382 C CB  . SER   B 2 128 ? -18.367 3.365   -21.074 1.00 47.17  ? 137 SER   B CB  1 
ATOM   1383 O OG  . SER   B 2 128 ? -18.269 4.786   -21.202 1.00 50.37  ? 137 SER   B OG  1 
ATOM   1384 N N   . PRO   B 2 129 ? -20.561 0.959   -20.121 1.00 42.55  ? 138 PRO   B N   1 
ATOM   1385 C CA  . PRO   B 2 129 ? -20.822 -0.472  -20.035 1.00 39.92  ? 138 PRO   B CA  1 
ATOM   1386 C C   . PRO   B 2 129 ? -20.237 -1.331  -21.162 1.00 48.45  ? 138 PRO   B C   1 
ATOM   1387 O O   . PRO   B 2 129 ? -20.166 -0.890  -22.319 1.00 43.08  ? 138 PRO   B O   1 
ATOM   1388 C CB  . PRO   B 2 129 ? -22.343 -0.530  -20.210 1.00 43.47  ? 138 PRO   B CB  1 
ATOM   1389 C CG  . PRO   B 2 129 ? -22.667 0.655   -21.070 1.00 42.19  ? 138 PRO   B CG  1 
ATOM   1390 C CD  . PRO   B 2 129 ? -21.717 1.735   -20.602 1.00 42.82  ? 138 PRO   B CD  1 
ATOM   1391 N N   . ILE   B 2 130 ? -19.893 -2.561  -20.805 1.00 49.03  ? 139 ILE   B N   1 
ATOM   1392 C CA  . ILE   B 2 130 ? -19.430 -3.632  -21.732 1.00 48.39  ? 139 ILE   B CA  1 
ATOM   1393 C C   . ILE   B 2 130 ? -20.594 -4.588  -21.917 1.00 42.76  ? 139 ILE   B C   1 
ATOM   1394 O O   . ILE   B 2 130 ? -21.184 -4.929  -20.876 1.00 45.74  ? 139 ILE   B O   1 
ATOM   1395 C CB  . ILE   B 2 130 ? -18.213 -4.331  -21.123 1.00 53.26  ? 139 ILE   B CB  1 
ATOM   1396 C CG1 . ILE   B 2 130 ? -17.058 -3.344  -20.967 1.00 54.23  ? 139 ILE   B CG1 1 
ATOM   1397 C CG2 . ILE   B 2 130 ? -17.821 -5.564  -21.925 1.00 51.85  ? 139 ILE   B CG2 1 
ATOM   1398 C CD1 . ILE   B 2 130 ? -16.027 -3.797  -19.977 1.00 59.02  ? 139 ILE   B CD1 1 
ATOM   1399 N N   . LEU   B 2 131 ? -20.926 -4.958  -23.162 1.00 43.51  ? 140 LEU   B N   1 
ATOM   1400 C CA  . LEU   B 2 131 ? -22.091 -5.856  -23.470 1.00 55.07  ? 140 LEU   B CA  1 
ATOM   1401 C C   . LEU   B 2 131 ? -21.689 -7.189  -24.094 1.00 51.69  ? 140 LEU   B C   1 
ATOM   1402 O O   . LEU   B 2 131 ? -20.734 -7.204  -24.868 1.00 54.78  ? 140 LEU   B O   1 
ATOM   1403 C CB  . LEU   B 2 131 ? -22.981 -5.178  -24.510 1.00 65.77  ? 140 LEU   B CB  1 
ATOM   1404 C CG  . LEU   B 2 131 ? -23.111 -3.670  -24.364 1.00 71.68  ? 140 LEU   B CG  1 
ATOM   1405 C CD1 . LEU   B 2 131 ? -23.883 -3.091  -25.540 1.00 67.12  ? 140 LEU   B CD1 1 
ATOM   1406 C CD2 . LEU   B 2 131 ? -23.785 -3.360  -23.036 1.00 70.86  ? 140 LEU   B CD2 1 
ATOM   1407 N N   . ASP   B 2 132 ? -22.535 -8.193  -23.890 1.00 49.21  ? 141 ASP   B N   1 
ATOM   1408 C CA  . ASP   B 2 132 ? -22.579 -9.453  -24.667 1.00 60.53  ? 141 ASP   B CA  1 
ATOM   1409 C C   . ASP   B 2 132 ? -23.534 -9.271  -25.868 1.00 69.54  ? 141 ASP   B C   1 
ATOM   1410 O O   . ASP   B 2 132 ? -24.121 -8.187  -26.020 1.00 76.92  ? 141 ASP   B O   1 
ATOM   1411 C CB  . ASP   B 2 132 ? -22.960 -10.600 -23.729 1.00 53.77  ? 141 ASP   B CB  1 
ATOM   1412 C CG  . ASP   B 2 132 ? -24.408 -10.598 -23.296 1.00 61.02  ? 141 ASP   B CG  1 
ATOM   1413 O OD1 . ASP   B 2 132 ? -25.190 -9.797  -23.847 1.00 60.13  ? 141 ASP   B OD1 1 
ATOM   1414 O OD2 . ASP   B 2 132 ? -24.748 -11.421 -22.435 1.00 58.90  ? 141 ASP   B OD2 1 
ATOM   1415 N N   . LYS   B 2 133 ? -23.707 -10.300 -26.695 1.00 71.53  ? 142 LYS   B N   1 
ATOM   1416 C CA  . LYS   B 2 133 ? -24.390 -10.188 -28.016 1.00 77.98  ? 142 LYS   B CA  1 
ATOM   1417 C C   . LYS   B 2 133 ? -25.898 -10.111 -27.817 1.00 73.11  ? 142 LYS   B C   1 
ATOM   1418 O O   . LYS   B 2 133 ? -26.584 -9.764  -28.776 1.00 74.68  ? 142 LYS   B O   1 
ATOM   1419 C CB  . LYS   B 2 133 ? -24.104 -11.401 -28.906 1.00 83.25  ? 142 LYS   B CB  1 
ATOM   1420 C CG  . LYS   B 2 133 ? -22.656 -11.555 -29.334 1.00 97.21  ? 142 LYS   B CG  1 
ATOM   1421 C CD  . LYS   B 2 133 ? -22.230 -12.999 -29.488 1.00 102.92 ? 142 LYS   B CD  1 
ATOM   1422 C CE  . LYS   B 2 133 ? -20.759 -13.137 -29.813 1.00 107.09 ? 142 LYS   B CE  1 
ATOM   1423 N NZ  . LYS   B 2 133 ? -20.390 -14.552 -30.048 1.00 114.95 ? 142 LYS   B NZ  1 
ATOM   1424 N N   . CYS   B 2 134 ? -26.376 -10.483 -26.633 1.00 72.10  ? 143 CYS   B N   1 
ATOM   1425 C CA  . CYS   B 2 134 ? -27.794 -10.378 -26.214 1.00 69.66  ? 143 CYS   B CA  1 
ATOM   1426 C C   . CYS   B 2 134 ? -28.075 -8.974  -25.650 1.00 63.98  ? 143 CYS   B C   1 
ATOM   1427 O O   . CYS   B 2 134 ? -29.192 -8.754  -25.165 1.00 61.10  ? 143 CYS   B O   1 
ATOM   1428 C CB  . CYS   B 2 134 ? -28.113 -11.461 -25.190 1.00 77.46  ? 143 CYS   B CB  1 
ATOM   1429 S SG  . CYS   B 2 134 ? -28.233 -13.134 -25.886 1.00 88.76  ? 143 CYS   B SG  1 
ATOM   1430 N N   . GLY   B 2 135 ? -27.092 -8.065  -25.678 1.00 61.83  ? 144 GLY   B N   1 
ATOM   1431 C CA  . GLY   B 2 135 ? -27.213 -6.698  -25.122 1.00 63.62  ? 144 GLY   B CA  1 
ATOM   1432 C C   . GLY   B 2 135 ? -27.202 -6.601  -23.591 1.00 60.36  ? 144 GLY   B C   1 
ATOM   1433 O O   . GLY   B 2 135 ? -27.375 -5.480  -23.085 1.00 58.58  ? 144 GLY   B O   1 
ATOM   1434 N N   . ARG   B 2 136 ? -26.958 -7.679  -22.847 1.00 56.50  ? 145 ARG   B N   1 
ATOM   1435 C CA  . ARG   B 2 136 ? -26.889 -7.629  -21.363 1.00 53.30  ? 145 ARG   B CA  1 
ATOM   1436 C C   . ARG   B 2 136 ? -25.539 -7.064  -20.947 1.00 50.57  ? 145 ARG   B C   1 
ATOM   1437 O O   . ARG   B 2 136 ? -24.554 -7.335  -21.636 1.00 53.46  ? 145 ARG   B O   1 
ATOM   1438 C CB  . ARG   B 2 136 ? -27.154 -9.020  -20.801 1.00 63.14  ? 145 ARG   B CB  1 
ATOM   1439 C CG  . ARG   B 2 136 ? -28.598 -9.468  -21.002 1.00 67.06  ? 145 ARG   B CG  1 
ATOM   1440 C CD  . ARG   B 2 136 ? -28.781 -10.904 -20.602 1.00 69.58  ? 145 ARG   B CD  1 
ATOM   1441 N NE  . ARG   B 2 136 ? -27.859 -11.684 -21.409 1.00 86.93  ? 145 ARG   B NE  1 
ATOM   1442 C CZ  . ARG   B 2 136 ? -27.260 -12.814 -21.044 1.00 94.41  ? 145 ARG   B CZ  1 
ATOM   1443 N NH1 . ARG   B 2 136 ? -27.461 -13.339 -19.841 1.00 96.33  ? 145 ARG   B NH1 1 
ATOM   1444 N NH2 . ARG   B 2 136 ? -26.446 -13.410 -21.901 1.00 92.85  ? 145 ARG   B NH2 1 
ATOM   1445 N N   . VAL   B 2 137 ? -25.501 -6.270  -19.873 1.00 50.56  ? 146 VAL   B N   1 
ATOM   1446 C CA  . VAL   B 2 137 ? -24.244 -5.612  -19.397 1.00 49.04  ? 146 VAL   B CA  1 
ATOM   1447 C C   . VAL   B 2 137 ? -23.472 -6.654  -18.577 1.00 47.19  ? 146 VAL   B C   1 
ATOM   1448 O O   . VAL   B 2 137 ? -24.034 -7.194  -17.630 1.00 53.90  ? 146 VAL   B O   1 
ATOM   1449 C CB  . VAL   B 2 137 ? -24.524 -4.343  -18.565 1.00 48.89  ? 146 VAL   B CB  1 
ATOM   1450 C CG1 . VAL   B 2 137 ? -23.241 -3.644  -18.149 1.00 51.94  ? 146 VAL   B CG1 1 
ATOM   1451 C CG2 . VAL   B 2 137 ? -25.428 -3.376  -19.307 1.00 53.28  ? 146 VAL   B CG2 1 
ATOM   1452 N N   . ILE   B 2 138 ? -22.227 -6.902  -18.939 1.00 48.08  ? 147 ILE   B N   1 
ATOM   1453 C CA  . ILE   B 2 138 ? -21.350 -7.903  -18.269 1.00 50.11  ? 147 ILE   B CA  1 
ATOM   1454 C C   . ILE   B 2 138 ? -20.339 -7.157  -17.395 1.00 51.59  ? 147 ILE   B C   1 
ATOM   1455 O O   . ILE   B 2 138 ? -19.517 -7.814  -16.745 1.00 46.06  ? 147 ILE   B O   1 
ATOM   1456 C CB  . ILE   B 2 138 ? -20.672 -8.811  -19.316 1.00 46.50  ? 147 ILE   B CB  1 
ATOM   1457 C CG1 . ILE   B 2 138 ? -19.868 -8.013  -20.332 1.00 49.23  ? 147 ILE   B CG1 1 
ATOM   1458 C CG2 . ILE   B 2 138 ? -21.676 -9.707  -20.013 1.00 45.43  ? 147 ILE   B CG2 1 
ATOM   1459 C CD1 . ILE   B 2 138 ? -19.106 -8.901  -21.272 1.00 60.69  ? 147 ILE   B CD1 1 
ATOM   1460 N N   . GLY   B 2 139 ? -20.407 -5.826  -17.387 1.00 44.20  ? 148 GLY   B N   1 
ATOM   1461 C CA  . GLY   B 2 139 ? -19.672 -5.011  -16.420 1.00 42.17  ? 148 GLY   B CA  1 
ATOM   1462 C C   . GLY   B 2 139 ? -19.320 -3.647  -16.957 1.00 43.75  ? 148 GLY   B C   1 
ATOM   1463 O O   . GLY   B 2 139 ? -19.783 -3.279  -18.024 1.00 46.82  ? 148 GLY   B O   1 
ATOM   1464 N N   . LEU   B 2 140 ? -18.508 -2.921  -16.218 1.00 41.49  ? 149 LEU   B N   1 
ATOM   1465 C CA  . LEU   B 2 140 ? -18.210 -1.505  -16.485 1.00 42.44  ? 149 LEU   B CA  1 
ATOM   1466 C C   . LEU   B 2 140 ? -16.725 -1.360  -16.749 1.00 46.26  ? 149 LEU   B C   1 
ATOM   1467 O O   . LEU   B 2 140 ? -15.880 -2.074  -16.103 1.00 43.89  ? 149 LEU   B O   1 
ATOM   1468 C CB  . LEU   B 2 140 ? -18.600 -0.642  -15.281 1.00 39.78  ? 149 LEU   B CB  1 
ATOM   1469 C CG  . LEU   B 2 140 ? -20.083 -0.598  -14.922 1.00 42.36  ? 149 LEU   B CG  1 
ATOM   1470 C CD1 . LEU   B 2 140 ? -20.383 0.599   -14.004 1.00 47.63  ? 149 LEU   B CD1 1 
ATOM   1471 C CD2 . LEU   B 2 140 ? -20.949 -0.562  -16.170 1.00 43.83  ? 149 LEU   B CD2 1 
ATOM   1472 N N   . TYR   B 2 141 ? -16.462 -0.453  -17.675 1.00 42.25  ? 150 TYR   B N   1 
ATOM   1473 C CA  . TYR   B 2 141 ? -15.133 -0.073  -18.163 1.00 39.60  ? 150 TYR   B CA  1 
ATOM   1474 C C   . TYR   B 2 141 ? -14.601 0.997   -17.233 1.00 42.40  ? 150 TYR   B C   1 
ATOM   1475 O O   . TYR   B 2 141 ? -15.386 1.900   -16.962 1.00 51.17  ? 150 TYR   B O   1 
ATOM   1476 C CB  . TYR   B 2 141 ? -15.268 0.403   -19.614 1.00 46.33  ? 150 TYR   B CB  1 
ATOM   1477 C CG  . TYR   B 2 141 ? -14.010 0.992   -20.220 1.00 50.98  ? 150 TYR   B CG  1 
ATOM   1478 C CD1 . TYR   B 2 141 ? -13.708 2.339   -20.081 1.00 47.98  ? 150 TYR   B CD1 1 
ATOM   1479 C CD2 . TYR   B 2 141 ? -13.101 0.206   -20.915 1.00 48.29  ? 150 TYR   B CD2 1 
ATOM   1480 C CE1 . TYR   B 2 141 ? -12.545 2.890   -20.608 1.00 55.63  ? 150 TYR   B CE1 1 
ATOM   1481 C CE2 . TYR   B 2 141 ? -11.944 0.747   -21.470 1.00 55.27  ? 150 TYR   B CE2 1 
ATOM   1482 C CZ  . TYR   B 2 141 ? -11.661 2.094   -21.320 1.00 54.88  ? 150 TYR   B CZ  1 
ATOM   1483 O OH  . TYR   B 2 141 ? -10.519 2.637   -21.836 1.00 53.73  ? 150 TYR   B OH  1 
ATOM   1484 N N   . GLY   B 2 142 ? -13.326 0.950   -16.832 1.00 42.30  ? 151 GLY   B N   1 
ATOM   1485 C CA  . GLY   B 2 142 ? -12.614 2.139   -16.305 1.00 46.86  ? 151 GLY   B CA  1 
ATOM   1486 C C   . GLY   B 2 142 ? -11.834 1.940   -15.005 1.00 52.13  ? 151 GLY   B C   1 
ATOM   1487 O O   . GLY   B 2 142 ? -11.444 2.967   -14.391 1.00 53.40  ? 151 GLY   B O   1 
ATOM   1488 N N   . ASN   B 2 143 ? -11.572 0.699   -14.581 1.00 49.03  ? 152 ASN   B N   1 
ATOM   1489 C CA  . ASN   B 2 143 ? -10.555 0.438   -13.528 1.00 49.34  ? 152 ASN   B CA  1 
ATOM   1490 C C   . ASN   B 2 143 ? -9.583  -0.594  -14.096 1.00 42.66  ? 152 ASN   B C   1 
ATOM   1491 O O   . ASN   B 2 143 ? -10.025 -1.708  -14.382 1.00 42.03  ? 152 ASN   B O   1 
ATOM   1492 C CB  . ASN   B 2 143 ? -11.194 -0.044  -12.226 1.00 47.71  ? 152 ASN   B CB  1 
ATOM   1493 C CG  . ASN   B 2 143 ? -10.235 -0.118  -11.059 1.00 50.24  ? 152 ASN   B CG  1 
ATOM   1494 O OD1 . ASN   B 2 143 ? -9.306  0.695   -10.909 1.00 47.65  ? 152 ASN   B OD1 1 
ATOM   1495 N ND2 . ASN   B 2 143 ? -10.517 -1.069  -10.182 1.00 46.29  ? 152 ASN   B ND2 1 
ATOM   1496 N N   . GLY   B 2 144 ? -8.343  -0.187  -14.313 1.00 44.65  ? 153 GLY   B N   1 
ATOM   1497 C CA  . GLY   B 2 144 ? -7.374  -0.989  -15.070 1.00 56.46  ? 153 GLY   B CA  1 
ATOM   1498 C C   . GLY   B 2 144 ? -5.950  -0.571  -14.764 1.00 56.72  ? 153 GLY   B C   1 
ATOM   1499 O O   . GLY   B 2 144 ? -5.728  0.010   -13.677 1.00 56.56  ? 153 GLY   B O   1 
ATOM   1500 N N   . VAL   B 2 145 ? -5.042  -0.856  -15.700 1.00 55.79  ? 154 VAL   B N   1 
ATOM   1501 C CA  . VAL   B 2 145 ? -3.563  -0.791  -15.515 1.00 61.13  ? 154 VAL   B CA  1 
ATOM   1502 C C   . VAL   B 2 145 ? -2.895  -0.317  -16.828 1.00 66.30  ? 154 VAL   B C   1 
ATOM   1503 O O   . VAL   B 2 145 ? -3.481  -0.507  -17.923 1.00 60.18  ? 154 VAL   B O   1 
ATOM   1504 C CB  . VAL   B 2 145 ? -3.073  -2.162  -15.001 1.00 66.69  ? 154 VAL   B CB  1 
ATOM   1505 C CG1 . VAL   B 2 145 ? -3.280  -3.292  -16.004 1.00 67.22  ? 154 VAL   B CG1 1 
ATOM   1506 C CG2 . VAL   B 2 145 ? -1.635  -2.111  -14.529 1.00 67.37  ? 154 VAL   B CG2 1 
ATOM   1507 N N   . VAL   B 2 146 ? -1.754  0.373   -16.722 1.00 66.64  ? 155 VAL   B N   1 
ATOM   1508 C CA  . VAL   B 2 146 ? -0.921  0.828   -17.876 1.00 72.63  ? 155 VAL   B CA  1 
ATOM   1509 C C   . VAL   B 2 146 ? 0.164   -0.232  -18.098 1.00 74.12  ? 155 VAL   B C   1 
ATOM   1510 O O   . VAL   B 2 146 ? 0.875   -0.543  -17.137 1.00 72.98  ? 155 VAL   B O   1 
ATOM   1511 C CB  . VAL   B 2 146 ? -0.338  2.234   -17.630 1.00 79.02  ? 155 VAL   B CB  1 
ATOM   1512 C CG1 . VAL   B 2 146 ? 0.431   2.737   -18.835 1.00 84.05  ? 155 VAL   B CG1 1 
ATOM   1513 C CG2 . VAL   B 2 146 ? -1.420  3.240   -17.255 1.00 79.33  ? 155 VAL   B CG2 1 
ATOM   1514 N N   . ILE   B 2 147 ? 0.217   -0.851  -19.281 1.00 77.23  ? 156 ILE   B N   1 
ATOM   1515 C CA  . ILE   B 2 147 ? 1.140   -1.998  -19.544 1.00 74.79  ? 156 ILE   B CA  1 
ATOM   1516 C C   . ILE   B 2 147 ? 2.492   -1.451  -20.031 1.00 80.58  ? 156 ILE   B C   1 
ATOM   1517 O O   . ILE   B 2 147 ? 2.603   -0.232  -20.275 1.00 65.79  ? 156 ILE   B O   1 
ATOM   1518 C CB  . ILE   B 2 147 ? 0.506   -3.021  -20.510 1.00 81.74  ? 156 ILE   B CB  1 
ATOM   1519 C CG1 . ILE   B 2 147 ? 0.112   -2.414  -21.861 1.00 83.38  ? 156 ILE   B CG1 1 
ATOM   1520 C CG2 . ILE   B 2 147 ? -0.679  -3.703  -19.842 1.00 86.90  ? 156 ILE   B CG2 1 
ATOM   1521 C CD1 . ILE   B 2 147 ? -0.275  -3.441  -22.906 1.00 73.97  ? 156 ILE   B CD1 1 
ATOM   1522 N N   . LYS   B 2 148 ? 3.497   -2.319  -20.154 1.00 85.57  ? 157 LYS   B N   1 
ATOM   1523 C CA  . LYS   B 2 148 ? 4.887   -1.936  -20.520 1.00 90.53  ? 157 LYS   B CA  1 
ATOM   1524 C C   . LYS   B 2 148 ? 4.885   -0.787  -21.549 1.00 91.17  ? 157 LYS   B C   1 
ATOM   1525 O O   . LYS   B 2 148 ? 5.515   0.255   -21.266 1.00 89.12  ? 157 LYS   B O   1 
ATOM   1526 C CB  . LYS   B 2 148 ? 5.621   -3.199  -20.971 1.00 99.26  ? 157 LYS   B CB  1 
ATOM   1527 C CG  . LYS   B 2 148 ? 5.851   -4.201  -19.843 1.00 109.86 ? 157 LYS   B CG  1 
ATOM   1528 C CD  . LYS   B 2 148 ? 5.998   -5.636  -20.300 1.00 118.45 ? 157 LYS   B CD  1 
ATOM   1529 C CE  . LYS   B 2 148 ? 7.307   -5.910  -21.014 1.00 127.93 ? 157 LYS   B CE  1 
ATOM   1530 N NZ  . LYS   B 2 148 ? 8.439   -6.074  -20.069 1.00 133.75 ? 157 LYS   B NZ  1 
ATOM   1531 N N   . ASN   B 2 149 ? 4.148   -0.928  -22.657 1.00 90.21  ? 158 ASN   B N   1 
ATOM   1532 C CA  . ASN   B 2 149 ? 4.085   0.047   -23.791 1.00 84.30  ? 158 ASN   B CA  1 
ATOM   1533 C C   . ASN   B 2 149 ? 3.809   1.473   -23.293 1.00 94.40  ? 158 ASN   B C   1 
ATOM   1534 O O   . ASN   B 2 149 ? 4.496   2.422   -23.739 1.00 99.35  ? 158 ASN   B O   1 
ATOM   1535 C CB  . ASN   B 2 149 ? 2.989   -0.290  -24.809 1.00 86.75  ? 158 ASN   B CB  1 
ATOM   1536 C CG  . ASN   B 2 149 ? 2.508   -1.727  -24.743 1.00 91.30  ? 158 ASN   B CG  1 
ATOM   1537 O OD1 . ASN   B 2 149 ? 3.049   -2.551  -24.006 1.00 85.84  ? 158 ASN   B OD1 1 
ATOM   1538 N ND2 . ASN   B 2 149 ? 1.479   -2.036  -25.510 1.00 101.21 ? 158 ASN   B ND2 1 
ATOM   1539 N N   . GLY   B 2 150 ? 2.815   1.615   -22.417 1.00 97.58  ? 159 GLY   B N   1 
ATOM   1540 C CA  . GLY   B 2 150 ? 2.192   2.911   -22.082 1.00 88.58  ? 159 GLY   B CA  1 
ATOM   1541 C C   . GLY   B 2 150 ? 0.690   2.969   -22.357 1.00 82.70  ? 159 GLY   B C   1 
ATOM   1542 O O   . GLY   B 2 150 ? 0.065   3.978   -21.995 1.00 81.80  ? 159 GLY   B O   1 
ATOM   1543 N N   A SER   B 2 151 ? 0.130   1.915   -22.966 0.25 81.96  ? 160 SER   B N   1 
ATOM   1544 N N   B SER   B 2 151 ? 0.131   1.920   -22.977 0.25 80.27  ? 160 SER   B N   1 
ATOM   1545 N N   C SER   B 2 151 ? 0.130   1.915   -22.966 0.25 81.96  ? 160 SER   B N   1 
ATOM   1546 N N   D SER   B 2 151 ? 0.131   1.920   -22.977 0.25 80.27  ? 160 SER   B N   1 
ATOM   1547 C CA  A SER   B 2 151 ? -1.309  1.789   -23.323 0.25 78.75  ? 160 SER   B CA  1 
ATOM   1548 C CA  B SER   B 2 151 ? -1.310  1.790   -23.320 0.25 76.13  ? 160 SER   B CA  1 
ATOM   1549 C CA  C SER   B 2 151 ? -1.309  1.789   -23.323 0.25 78.75  ? 160 SER   B CA  1 
ATOM   1550 C CA  D SER   B 2 151 ? -1.310  1.790   -23.320 0.25 76.13  ? 160 SER   B CA  1 
ATOM   1551 C C   A SER   B 2 151 ? -2.107  1.282   -22.113 0.25 76.61  ? 160 SER   B C   1 
ATOM   1552 C C   B SER   B 2 151 ? -2.098  1.315   -22.093 0.25 75.06  ? 160 SER   B C   1 
ATOM   1553 C C   C SER   B 2 151 ? -2.107  1.282   -22.113 0.25 76.61  ? 160 SER   B C   1 
ATOM   1554 C C   D SER   B 2 151 ? -2.098  1.315   -22.093 0.25 75.06  ? 160 SER   B C   1 
ATOM   1555 O O   A SER   B 2 151 ? -1.521  0.567   -21.273 0.25 74.54  ? 160 SER   B O   1 
ATOM   1556 O O   B SER   B 2 151 ? -1.497  0.649   -21.223 0.25 73.12  ? 160 SER   B O   1 
ATOM   1557 O O   C SER   B 2 151 ? -1.521  0.567   -21.273 0.25 74.54  ? 160 SER   B O   1 
ATOM   1558 O O   D SER   B 2 151 ? -1.497  0.649   -21.223 0.25 73.12  ? 160 SER   B O   1 
ATOM   1559 C CB  A SER   B 2 151 ? -1.480  0.884   -24.515 0.25 77.40  ? 160 SER   B CB  1 
ATOM   1560 C CB  B SER   B 2 151 ? -1.503  0.849   -24.478 0.25 73.11  ? 160 SER   B CB  1 
ATOM   1561 C CB  C SER   B 2 151 ? -1.480  0.884   -24.515 0.25 77.40  ? 160 SER   B CB  1 
ATOM   1562 C CB  D SER   B 2 151 ? -1.503  0.849   -24.478 0.25 73.11  ? 160 SER   B CB  1 
ATOM   1563 O OG  A SER   B 2 151 ? -2.833  0.852   -24.941 0.25 80.11  ? 160 SER   B OG  1 
ATOM   1564 O OG  B SER   B 2 151 ? -1.130  -0.471  -24.110 0.25 71.94  ? 160 SER   B OG  1 
ATOM   1565 O OG  C SER   B 2 151 ? -2.833  0.852   -24.941 0.25 80.11  ? 160 SER   B OG  1 
ATOM   1566 O OG  D SER   B 2 151 ? -1.130  -0.471  -24.110 0.25 71.94  ? 160 SER   B OG  1 
ATOM   1567 N N   . TYR   B 2 152 ? -3.398  1.630   -22.048 1.00 72.84  ? 161 TYR   B N   1 
ATOM   1568 C CA  . TYR   B 2 152 ? -4.312  1.284   -20.921 1.00 66.02  ? 161 TYR   B CA  1 
ATOM   1569 C C   . TYR   B 2 152 ? -5.125  0.032   -21.242 1.00 57.45  ? 161 TYR   B C   1 
ATOM   1570 O O   . TYR   B 2 152 ? -5.621  -0.128  -22.371 1.00 56.39  ? 161 TYR   B O   1 
ATOM   1571 C CB  . TYR   B 2 152 ? -5.264  2.455   -20.645 1.00 70.53  ? 161 TYR   B CB  1 
ATOM   1572 C CG  . TYR   B 2 152 ? -6.298  2.245   -19.563 1.00 68.40  ? 161 TYR   B CG  1 
ATOM   1573 C CD1 . TYR   B 2 152 ? -5.985  2.462   -18.228 1.00 68.02  ? 161 TYR   B CD1 1 
ATOM   1574 C CD2 . TYR   B 2 152 ? -7.599  1.862   -19.868 1.00 62.11  ? 161 TYR   B CD2 1 
ATOM   1575 C CE1 . TYR   B 2 152 ? -6.927  2.289   -17.225 1.00 60.68  ? 161 TYR   B CE1 1 
ATOM   1576 C CE2 . TYR   B 2 152 ? -8.559  1.712   -18.881 1.00 60.99  ? 161 TYR   B CE2 1 
ATOM   1577 C CZ  . TYR   B 2 152 ? -8.220  1.921   -17.550 1.00 62.95  ? 161 TYR   B CZ  1 
ATOM   1578 O OH  . TYR   B 2 152 ? -9.146  1.785   -16.548 1.00 55.61  ? 161 TYR   B OH  1 
ATOM   1579 N N   . VAL   B 2 153 ? -5.321  -0.810  -20.229 1.00 62.95  ? 162 VAL   B N   1 
ATOM   1580 C CA  . VAL   B 2 153 ? -6.224  -2.001  -20.286 1.00 53.00  ? 162 VAL   B CA  1 
ATOM   1581 C C   . VAL   B 2 153 ? -7.126  -1.993  -19.046 1.00 55.35  ? 162 VAL   B C   1 
ATOM   1582 O O   . VAL   B 2 153 ? -6.593  -1.864  -17.929 1.00 56.15  ? 162 VAL   B O   1 
ATOM   1583 C CB  . VAL   B 2 153 ? -5.383  -3.287  -20.392 1.00 55.68  ? 162 VAL   B CB  1 
ATOM   1584 C CG1 . VAL   B 2 153 ? -6.230  -4.562  -20.433 1.00 51.82  ? 162 VAL   B CG1 1 
ATOM   1585 C CG2 . VAL   B 2 153 ? -4.464  -3.206  -21.611 1.00 59.55  ? 162 VAL   B CG2 1 
ATOM   1586 N N   . SER   B 2 154 ? -8.436  -2.135  -19.250 1.00 55.21  ? 163 SER   B N   1 
ATOM   1587 C CA  . SER   B 2 154 ? -9.486  -2.088  -18.203 1.00 53.80  ? 163 SER   B CA  1 
ATOM   1588 C C   . SER   B 2 154 ? -9.939  -3.502  -17.876 1.00 52.14  ? 163 SER   B C   1 
ATOM   1589 O O   . SER   B 2 154 ? -10.145 -4.287  -18.783 1.00 50.03  ? 163 SER   B O   1 
ATOM   1590 C CB  . SER   B 2 154 ? -10.704 -1.252  -18.625 1.00 59.33  ? 163 SER   B CB  1 
ATOM   1591 O OG  . SER   B 2 154 ? -11.777 -1.330  -17.672 1.00 47.09  ? 163 SER   B OG  1 
ATOM   1592 N N   . ALA   B 2 155 ? -10.161 -3.763  -16.599 1.00 50.94  ? 164 ALA   B N   1 
ATOM   1593 C CA  . ALA   B 2 155 ? -11.025 -4.856  -16.142 1.00 46.61  ? 164 ALA   B CA  1 
ATOM   1594 C C   . ALA   B 2 155 ? -12.402 -4.695  -16.764 1.00 48.54  ? 164 ALA   B C   1 
ATOM   1595 O O   . ALA   B 2 155 ? -12.905 -3.543  -16.924 1.00 44.93  ? 164 ALA   B O   1 
ATOM   1596 C CB  . ALA   B 2 155 ? -11.128 -4.842  -14.636 1.00 51.74  ? 164 ALA   B CB  1 
ATOM   1597 N N   . ILE   B 2 156 ? -13.021 -5.836  -17.001 1.00 42.32  ? 165 ILE   B N   1 
ATOM   1598 C CA  . ILE   B 2 156 ? -14.496 -5.966  -16.993 1.00 46.10  ? 165 ILE   B CA  1 
ATOM   1599 C C   . ILE   B 2 156 ? -14.959 -6.080  -15.532 1.00 46.21  ? 165 ILE   B C   1 
ATOM   1600 O O   . ILE   B 2 156 ? -14.949 -7.201  -15.037 1.00 46.53  ? 165 ILE   B O   1 
ATOM   1601 C CB  . ILE   B 2 156 ? -14.926 -7.182  -17.818 1.00 44.87  ? 165 ILE   B CB  1 
ATOM   1602 C CG1 . ILE   B 2 156 ? -14.331 -7.125  -19.225 1.00 55.18  ? 165 ILE   B CG1 1 
ATOM   1603 C CG2 . ILE   B 2 156 ? -16.433 -7.270  -17.855 1.00 48.16  ? 165 ILE   B CG2 1 
ATOM   1604 C CD1 . ILE   B 2 156 ? -14.661 -8.325  -20.071 1.00 54.94  ? 165 ILE   B CD1 1 
ATOM   1605 N N   . THR   B 2 157 ? -15.383 -4.969  -14.883 1.00 48.89  ? 166 THR   B N   1 
ATOM   1606 C CA  . THR   B 2 157 ? -15.792 -4.938  -13.447 1.00 38.98  ? 166 THR   B CA  1 
ATOM   1607 C C   . THR   B 2 157 ? -17.303 -5.219  -13.370 1.00 42.23  ? 166 THR   B C   1 
ATOM   1608 O O   . THR   B 2 157 ? -18.086 -4.423  -13.927 1.00 49.80  ? 166 THR   B O   1 
ATOM   1609 C CB  . THR   B 2 157 ? -15.323 -3.644  -12.787 1.00 43.96  ? 166 THR   B CB  1 
ATOM   1610 O OG1 . THR   B 2 157 ? -13.916 -3.448  -12.944 1.00 39.78  ? 166 THR   B OG1 1 
ATOM   1611 C CG2 . THR   B 2 157 ? -15.671 -3.610  -11.321 1.00 45.75  ? 166 THR   B CG2 1 
ATOM   1612 N N   . GLN   B 2 158 ? -17.709 -6.355  -12.797 1.00 39.25  ? 167 GLN   B N   1 
ATOM   1613 C CA  . GLN   B 2 158 ? -19.135 -6.719  -12.559 1.00 42.72  ? 167 GLN   B CA  1 
ATOM   1614 C C   . GLN   B 2 158 ? -19.390 -6.847  -11.048 1.00 48.01  ? 167 GLN   B C   1 
ATOM   1615 O O   . GLN   B 2 158 ? -18.477 -7.283  -10.327 1.00 42.88  ? 167 GLN   B O   1 
ATOM   1616 C CB  . GLN   B 2 158 ? -19.516 -8.007  -13.274 1.00 41.30  ? 167 GLN   B CB  1 
ATOM   1617 C CG  . GLN   B 2 158 ? -20.993 -8.360  -13.162 1.00 44.93  ? 167 GLN   B CG  1 
ATOM   1618 C CD  . GLN   B 2 158 ? -21.911 -7.246  -13.647 1.00 47.74  ? 167 GLN   B CD  1 
ATOM   1619 O OE1 . GLN   B 2 158 ? -21.967 -6.170  -13.061 1.00 47.50  ? 167 GLN   B OE1 1 
ATOM   1620 N NE2 . GLN   B 2 158 ? -22.642 -7.494  -14.719 1.00 45.22  ? 167 GLN   B NE2 1 
ATOM   1621 N N   . GLY   B 2 159 ? -20.560 -6.399  -10.578 1.00 47.82  ? 168 GLY   B N   1 
ATOM   1622 C CA  . GLY   B 2 159 ? -20.956 -6.544  -9.164  1.00 52.15  ? 168 GLY   B CA  1 
ATOM   1623 C C   . GLY   B 2 159 ? -21.759 -7.821  -8.980  1.00 57.47  ? 168 GLY   B C   1 
ATOM   1624 O O   . GLY   B 2 159 ? -22.018 -8.520  -9.984  1.00 66.15  ? 168 GLY   B O   1 
ATOM   1625 N N   . LYS   B 2 160 ? -22.150 -8.107  -7.744  1.00 63.88  ? 169 LYS   B N   1 
ATOM   1626 C CA  . LYS   B 2 160 ? -23.071 -9.208  -7.352  1.00 67.67  ? 169 LYS   B CA  1 
ATOM   1627 C C   . LYS   B 2 160 ? -24.509 -8.660  -7.305  1.00 71.99  ? 169 LYS   B C   1 
ATOM   1628 O O   . LYS   B 2 160 ? -24.717 -7.580  -6.736  1.00 69.55  ? 169 LYS   B O   1 
ATOM   1629 C CB  . LYS   B 2 160 ? -22.621 -9.759  -5.990  1.00 76.80  ? 169 LYS   B CB  1 
ATOM   1630 C CG  . LYS   B 2 160 ? -23.229 -11.098 -5.604  1.00 95.99  ? 169 LYS   B CG  1 
ATOM   1631 C CD  . LYS   B 2 160 ? -22.850 -11.603 -4.226  1.00 99.65  ? 169 LYS   B CD  1 
ATOM   1632 C CE  . LYS   B 2 160 ? -23.481 -12.949 -3.930  1.00 100.43 ? 169 LYS   B CE  1 
ATOM   1633 N NZ  . LYS   B 2 160 ? -24.096 -12.973 -2.583  1.00 110.00 ? 169 LYS   B NZ  1 
ATOM   1634 N N   . ARG   B 2 161 ? -25.485 -9.372  -7.868  1.00 75.65  ? 170 ARG   B N   1 
ATOM   1635 C CA  . ARG   B 2 161 ? -26.927 -9.108  -7.609  1.00 84.64  ? 170 ARG   B CA  1 
ATOM   1636 C C   . ARG   B 2 161 ? -27.390 -9.975  -6.429  1.00 85.28  ? 170 ARG   B C   1 
ATOM   1637 O O   . ARG   B 2 161 ? -27.074 -11.172 -6.445  1.00 88.78  ? 170 ARG   B O   1 
ATOM   1638 C CB  . ARG   B 2 161 ? -27.744 -9.390  -8.875  1.00 81.92  ? 170 ARG   B CB  1 
ATOM   1639 C CG  . ARG   B 2 161 ? -29.231 -9.108  -8.732  1.00 77.38  ? 170 ARG   B CG  1 
ATOM   1640 C CD  . ARG   B 2 161 ? -30.017 -9.685  -9.886  1.00 77.56  ? 170 ARG   B CD  1 
ATOM   1641 N NE  . ARG   B 2 161 ? -31.425 -9.294  -9.854  1.00 79.57  ? 170 ARG   B NE  1 
ATOM   1642 C CZ  . ARG   B 2 161 ? -31.986 -8.341  -10.603 1.00 81.50  ? 170 ARG   B CZ  1 
ATOM   1643 N NH1 . ARG   B 2 161 ? -31.262 -7.637  -11.460 1.00 75.64  ? 170 ARG   B NH1 1 
ATOM   1644 N NH2 . ARG   B 2 161 ? -33.285 -8.103  -10.506 1.00 85.13  ? 170 ARG   B NH2 1 
ATOM   1645 N N   . GLU   B 2 162 ? -28.121 -9.398  -5.464  1.00 96.08  ? 171 GLU   B N   1 
ATOM   1646 C CA  . GLU   B 2 162 ? -28.642 -10.102 -4.256  1.00 101.51 ? 171 GLU   B CA  1 
ATOM   1647 C C   . GLU   B 2 162 ? -30.093 -10.524 -4.502  1.00 90.57  ? 171 GLU   B C   1 
ATOM   1648 O O   . GLU   B 2 162 ? -30.477 -11.578 -4.017  1.00 94.00  ? 171 GLU   B O   1 
ATOM   1649 C CB  . GLU   B 2 162 ? -28.557 -9.218  -3.008  1.00 111.28 ? 171 GLU   B CB  1 
ATOM   1650 C CG  . GLU   B 2 162 ? -27.151 -8.735  -2.665  1.00 125.27 ? 171 GLU   B CG  1 
ATOM   1651 C CD  . GLU   B 2 162 ? -26.192 -9.777  -2.104  1.00 128.74 ? 171 GLU   B CD  1 
ATOM   1652 O OE1 . GLU   B 2 162 ? -25.601 -9.515  -1.040  1.00 123.33 ? 171 GLU   B OE1 1 
ATOM   1653 O OE2 . GLU   B 2 162 ? -26.018 -10.839 -2.741  1.00 134.79 ? 171 GLU   B OE2 1 
HETATM 1654 S S   A DMS   C 3 .   ? -8.377  6.022   -17.860 0.11 81.59  ? 201 DMS   B S   1 
HETATM 1655 S S   B DMS   C 3 .   ? -8.377  6.022   -17.860 0.11 81.59  ? 201 DMS   B S   1 
HETATM 1656 O O   A DMS   C 3 .   ? -7.046  5.332   -17.942 0.11 80.69  ? 201 DMS   B O   1 
HETATM 1657 O O   B DMS   C 3 .   ? -7.046  5.332   -17.942 0.11 80.69  ? 201 DMS   B O   1 
HETATM 1658 C C1  A DMS   C 3 .   ? -9.024  5.650   -16.252 0.11 81.82  ? 201 DMS   B C1  1 
HETATM 1659 C C1  B DMS   C 3 .   ? -9.024  5.650   -16.252 0.11 81.82  ? 201 DMS   B C1  1 
HETATM 1660 C C2  A DMS   C 3 .   ? -9.508  5.029   -18.801 0.11 80.86  ? 201 DMS   B C2  1 
HETATM 1661 C C2  B DMS   C 3 .   ? -9.508  5.029   -18.801 0.11 80.86  ? 201 DMS   B C2  1 
HETATM 1662 S S   . DMS   D 3 .   ? -18.983 12.442  -0.223  1.00 92.52  ? 202 DMS   B S   1 
HETATM 1663 O O   . DMS   D 3 .   ? -19.573 11.046  -0.352  1.00 76.67  ? 202 DMS   B O   1 
HETATM 1664 C C1  . DMS   D 3 .   ? -20.103 13.570  -1.029  1.00 97.55  ? 202 DMS   B C1  1 
HETATM 1665 C C2  . DMS   D 3 .   ? -17.667 12.532  -1.405  1.00 76.76  ? 202 DMS   B C2  1 
HETATM 1666 S S   A DMS   E 3 .   ? -7.945  4.274   -13.406 0.11 110.49 ? 203 DMS   B S   1 
HETATM 1667 S S   B DMS   E 3 .   ? -7.945  4.274   -13.406 0.11 110.49 ? 203 DMS   B S   1 
HETATM 1668 O O   A DMS   E 3 .   ? -7.634  2.807   -13.505 0.11 110.50 ? 203 DMS   B O   1 
HETATM 1669 O O   B DMS   E 3 .   ? -7.634  2.807   -13.505 0.11 110.50 ? 203 DMS   B O   1 
HETATM 1670 C C1  A DMS   E 3 .   ? -8.706  4.512   -11.821 0.11 110.17 ? 203 DMS   B C1  1 
HETATM 1671 C C1  B DMS   E 3 .   ? -8.706  4.512   -11.821 0.11 110.17 ? 203 DMS   B C1  1 
HETATM 1672 C C2  A DMS   E 3 .   ? -6.403  5.083   -13.069 0.11 107.53 ? 203 DMS   B C2  1 
HETATM 1673 C C2  B DMS   E 3 .   ? -6.403  5.083   -13.069 0.11 107.53 ? 203 DMS   B C2  1 
HETATM 1674 N N1  C A1BXM F 4 .   ? -6.171  5.823   -16.014 0.39 55.46  ? 204 A1BXM B N1  1 
HETATM 1675 N N1  D A1BXM F 4 .   ? -6.171  5.823   -16.014 0.39 55.46  ? 204 A1BXM B N1  1 
HETATM 1676 N N3  C A1BXM F 4 .   ? -8.306  2.939   -9.509  0.39 48.26  ? 204 A1BXM B N3  1 
HETATM 1677 N N3  D A1BXM F 4 .   ? -8.306  2.939   -9.509  0.39 48.26  ? 204 A1BXM B N3  1 
HETATM 1678 C C4  C A1BXM F 4 .   ? -6.553  5.972   -18.806 0.39 57.76  ? 204 A1BXM B C4  1 
HETATM 1679 C C4  D A1BXM F 4 .   ? -6.553  5.972   -18.806 0.39 57.76  ? 204 A1BXM B C4  1 
HETATM 1680 C C5  C A1BXM F 4 .   ? -7.643  5.636   -17.948 0.39 55.74  ? 204 A1BXM B C5  1 
HETATM 1681 C C5  D A1BXM F 4 .   ? -7.643  5.636   -17.948 0.39 55.74  ? 204 A1BXM B C5  1 
HETATM 1682 C C6  C A1BXM F 4 .   ? -8.950  5.367   -18.432 0.39 56.89  ? 204 A1BXM B C6  1 
HETATM 1683 C C6  D A1BXM F 4 .   ? -8.950  5.367   -18.432 0.39 56.89  ? 204 A1BXM B C6  1 
HETATM 1684 C C7  C A1BXM F 4 .   ? -9.958  5.048   -17.573 0.39 58.22  ? 204 A1BXM B C7  1 
HETATM 1685 C C7  D A1BXM F 4 .   ? -9.958  5.048   -17.573 0.39 58.22  ? 204 A1BXM B C7  1 
HETATM 1686 C C8  C A1BXM F 4 .   ? -9.729  4.989   -16.189 0.39 55.83  ? 204 A1BXM B C8  1 
HETATM 1687 C C8  D A1BXM F 4 .   ? -9.729  4.989   -16.189 0.39 55.83  ? 204 A1BXM B C8  1 
HETATM 1688 C C10 C A1BXM F 4 .   ? -7.399  5.570   -16.548 0.39 54.51  ? 204 A1BXM B C10 1 
HETATM 1689 C C10 D A1BXM F 4 .   ? -7.399  5.570   -16.548 0.39 54.51  ? 204 A1BXM B C10 1 
HETATM 1690 C C13 C A1BXM F 4 .   ? -6.982  3.230   -11.540 0.39 50.82  ? 204 A1BXM B C13 1 
HETATM 1691 C C13 D A1BXM F 4 .   ? -6.982  3.230   -11.540 0.39 50.82  ? 204 A1BXM B C13 1 
HETATM 1692 C C15 C A1BXM F 4 .   ? -9.246  3.995   -9.900  0.39 49.43  ? 204 A1BXM B C15 1 
HETATM 1693 C C15 D A1BXM F 4 .   ? -9.246  3.995   -9.900  0.39 49.43  ? 204 A1BXM B C15 1 
HETATM 1694 C C17 C A1BXM F 4 .   ? -6.805  6.043   -20.294 0.39 58.34  ? 204 A1BXM B C17 1 
HETATM 1695 C C17 D A1BXM F 4 .   ? -6.805  6.043   -20.294 0.39 58.34  ? 204 A1BXM B C17 1 
HETATM 1696 C C1  C A1BXM F 4 .   ? -3.835  6.375   -16.187 0.39 52.80  ? 204 A1BXM B C1  1 
HETATM 1697 C C1  D A1BXM F 4 .   ? -3.835  6.375   -16.187 0.39 52.80  ? 204 A1BXM B C1  1 
HETATM 1698 C C2  C A1BXM F 4 .   ? -5.169  6.125   -16.825 0.39 55.07  ? 204 A1BXM B C2  1 
HETATM 1699 C C2  D A1BXM F 4 .   ? -5.169  6.125   -16.825 0.39 55.07  ? 204 A1BXM B C2  1 
HETATM 1700 C C3  C A1BXM F 4 .   ? -5.327  6.212   -18.235 0.39 55.70  ? 204 A1BXM B C3  1 
HETATM 1701 C C3  D A1BXM F 4 .   ? -5.327  6.212   -18.235 0.39 55.70  ? 204 A1BXM B C3  1 
HETATM 1702 C C9  C A1BXM F 4 .   ? -8.484  5.254   -15.673 0.39 56.31  ? 204 A1BXM B C9  1 
HETATM 1703 C C9  D A1BXM F 4 .   ? -8.484  5.254   -15.673 0.39 56.31  ? 204 A1BXM B C9  1 
HETATM 1704 N N2  C A1BXM F 4 .   ? -8.191  5.195   -14.306 0.39 54.64  ? 204 A1BXM B N2  1 
HETATM 1705 N N2  D A1BXM F 4 .   ? -8.191  5.195   -14.306 0.39 54.64  ? 204 A1BXM B N2  1 
HETATM 1706 C C11 C A1BXM F 4 .   ? -8.154  4.050   -13.598 0.39 54.27  ? 204 A1BXM B C11 1 
HETATM 1707 C C11 D A1BXM F 4 .   ? -8.154  4.050   -13.598 0.39 54.27  ? 204 A1BXM B C11 1 
HETATM 1708 O O1  C A1BXM F 4 .   ? -8.260  2.943   -14.119 0.39 51.02  ? 204 A1BXM B O1  1 
HETATM 1709 O O1  D A1BXM F 4 .   ? -8.260  2.943   -14.119 0.39 51.02  ? 204 A1BXM B O1  1 
HETATM 1710 C C12 C A1BXM F 4 .   ? -8.006  4.228   -12.094 0.39 51.67  ? 204 A1BXM B C12 1 
HETATM 1711 C C12 D A1BXM F 4 .   ? -8.006  4.228   -12.094 0.39 51.67  ? 204 A1BXM B C12 1 
HETATM 1712 C C14 C A1BXM F 4 .   ? -6.963  3.223   -10.024 0.39 48.55  ? 204 A1BXM B C14 1 
HETATM 1713 C C14 D A1BXM F 4 .   ? -6.963  3.223   -10.024 0.39 48.55  ? 204 A1BXM B C14 1 
HETATM 1714 C C16 C A1BXM F 4 .   ? -9.367  4.057   -11.409 0.39 49.61  ? 204 A1BXM B C16 1 
HETATM 1715 C C16 D A1BXM F 4 .   ? -9.367  4.057   -11.409 0.39 49.61  ? 204 A1BXM B C16 1 
HETATM 1716 O O2  C A1BXM F 4 .   ? -5.645  6.301   -21.071 0.39 61.05  ? 204 A1BXM B O2  1 
HETATM 1717 O O2  D A1BXM F 4 .   ? -5.645  6.301   -21.071 0.39 61.05  ? 204 A1BXM B O2  1 
HETATM 1718 S S   C DMS   G 3 .   ? -8.509  2.905   -29.360 0.50 111.41 ? 205 DMS   B S   1 
HETATM 1719 S S   D DMS   G 3 .   ? -8.509  2.905   -29.360 0.50 111.41 ? 205 DMS   B S   1 
HETATM 1720 O O   C DMS   G 3 .   ? -8.089  2.190   -28.095 0.50 101.27 ? 205 DMS   B O   1 
HETATM 1721 O O   D DMS   G 3 .   ? -8.089  2.190   -28.095 0.50 101.27 ? 205 DMS   B O   1 
HETATM 1722 C C1  C DMS   G 3 .   ? -8.934  4.570   -28.897 0.50 107.42 ? 205 DMS   B C1  1 
HETATM 1723 C C1  D DMS   G 3 .   ? -8.934  4.570   -28.897 0.50 107.42 ? 205 DMS   B C1  1 
HETATM 1724 C C2  C DMS   G 3 .   ? -10.145 2.315   -29.748 0.50 106.04 ? 205 DMS   B C2  1 
HETATM 1725 C C2  D DMS   G 3 .   ? -10.145 2.315   -29.748 0.50 106.04 ? 205 DMS   B C2  1 
HETATM 1726 O O   . HOH   H 5 .   ? -28.460 -5.451  -28.155 1.00 57.54  ? 101 HOH   A O   1 
HETATM 1727 O O   A HOH   H 5 .   ? -7.893  0.532   3.402   0.50 68.27  ? 102 HOH   A O   1 
HETATM 1728 O O   B HOH   H 5 .   ? -7.893  0.532   3.402   0.50 68.27  ? 102 HOH   A O   1 
HETATM 1729 O O   . HOH   H 5 .   ? -4.559  -13.662 -25.787 1.00 53.20  ? 103 HOH   A O   1 
HETATM 1730 O O   . HOH   H 5 .   ? -24.003 19.509  -19.539 1.00 71.24  ? 104 HOH   A O   1 
HETATM 1731 O O   . HOH   H 5 .   ? -30.907 0.867   -23.050 1.00 52.57  ? 105 HOH   A O   1 
HETATM 1732 O O   . HOH   H 5 .   ? -6.924  -8.550  -3.482  1.00 57.41  ? 106 HOH   A O   1 
HETATM 1733 O O   . HOH   H 5 .   ? -2.393  -3.668  -6.660  1.00 58.51  ? 107 HOH   A O   1 
HETATM 1734 O O   A HOH   H 5 .   ? -25.801 1.154   -30.882 0.50 96.72  ? 108 HOH   A O   1 
HETATM 1735 O O   B HOH   H 5 .   ? -25.801 1.154   -30.882 0.50 96.72  ? 108 HOH   A O   1 
HETATM 1736 O O   A HOH   H 5 .   ? -32.033 0.628   -28.862 0.50 70.49  ? 109 HOH   A O   1 
HETATM 1737 O O   B HOH   H 5 .   ? -32.033 0.628   -28.862 0.50 70.49  ? 109 HOH   A O   1 
HETATM 1738 O O   A HOH   H 5 .   ? -9.193  2.993   -6.817  0.11 21.25  ? 110 HOH   A O   1 
HETATM 1739 O O   B HOH   H 5 .   ? -9.193  2.993   -6.817  0.11 21.25  ? 110 HOH   A O   1 
HETATM 1740 O O   A HOH   H 5 .   ? -24.419 9.773   -27.426 0.50 64.38  ? 111 HOH   A O   1 
HETATM 1741 O O   B HOH   H 5 .   ? -24.419 9.773   -27.426 0.50 64.38  ? 111 HOH   A O   1 
HETATM 1742 O O   . HOH   H 5 .   ? -2.987  -11.063 -7.501  1.00 61.46  ? 112 HOH   A O   1 
HETATM 1743 O O   A HOH   H 5 .   ? -31.240 12.838  -16.413 0.50 75.50  ? 113 HOH   A O   1 
HETATM 1744 O O   B HOH   H 5 .   ? -31.240 12.838  -16.413 0.50 75.50  ? 113 HOH   A O   1 
HETATM 1745 O O   . HOH   H 5 .   ? -8.228  -1.819  6.365   1.00 58.04  ? 114 HOH   A O   1 
HETATM 1746 O O   . HOH   H 5 .   ? -29.258 -3.250  -22.414 1.00 58.56  ? 115 HOH   A O   1 
HETATM 1747 O O   . HOH   H 5 .   ? -22.958 -8.933  -34.548 1.00 51.94  ? 116 HOH   A O   1 
HETATM 1748 O O   . HOH   H 5 .   ? -4.865  -9.589  -5.932  1.00 62.12  ? 117 HOH   A O   1 
HETATM 1749 O O   . HOH   H 5 .   ? -3.710  -3.605  0.043   1.00 65.74  ? 118 HOH   A O   1 
HETATM 1750 O O   A HOH   H 5 .   ? -26.899 -2.409  -35.197 0.50 88.11  ? 119 HOH   A O   1 
HETATM 1751 O O   B HOH   H 5 .   ? -26.899 -2.409  -35.197 0.50 88.11  ? 119 HOH   A O   1 
HETATM 1752 O O   . HOH   H 5 .   ? -2.917  -7.991  -3.728  1.00 64.03  ? 120 HOH   A O   1 
HETATM 1753 O O   A HOH   H 5 .   ? -4.069  -0.670  -0.644  0.50 77.64  ? 121 HOH   A O   1 
HETATM 1754 O O   B HOH   H 5 .   ? -4.069  -0.670  -0.644  0.50 77.64  ? 121 HOH   A O   1 
HETATM 1755 O O   A HOH   H 5 .   ? -4.792  4.272   -10.091 0.11 96.92  ? 122 HOH   A O   1 
HETATM 1756 O O   B HOH   H 5 .   ? -4.792  4.272   -10.091 0.11 96.92  ? 122 HOH   A O   1 
HETATM 1757 O O   A HOH   I 5 .   ? -36.312 5.876   -11.580 0.50 110.24 ? 301 HOH   B O   1 
HETATM 1758 O O   B HOH   I 5 .   ? -36.312 5.876   -11.580 0.50 110.24 ? 301 HOH   B O   1 
HETATM 1759 O O   A HOH   I 5 .   ? -17.481 13.029  -5.555  0.50 69.63  ? 302 HOH   B O   1 
HETATM 1760 O O   B HOH   I 5 .   ? -17.481 13.029  -5.555  0.50 69.63  ? 302 HOH   B O   1 
HETATM 1761 O O   . HOH   I 5 .   ? -34.229 2.051   -15.067 1.00 57.63  ? 303 HOH   B O   1 
HETATM 1762 O O   . HOH   I 5 .   ? -31.242 13.209  -19.446 1.00 64.47  ? 304 HOH   B O   1 
HETATM 1763 O O   . HOH   I 5 .   ? -26.234 -7.700  -16.649 1.00 55.38  ? 305 HOH   B O   1 
HETATM 1764 O O   A HOH   I 5 .   ? -20.323 -11.890 -26.032 0.50 82.79  ? 306 HOH   B O   1 
HETATM 1765 O O   B HOH   I 5 .   ? -20.323 -11.890 -26.032 0.50 82.79  ? 306 HOH   B O   1 
HETATM 1766 O O   . HOH   I 5 .   ? -15.473 -4.066  1.392   1.00 48.62  ? 307 HOH   B O   1 
HETATM 1767 O O   . HOH   I 5 .   ? -13.309 -1.954  -14.937 1.00 52.86  ? 308 HOH   B O   1 
HETATM 1768 O O   . HOH   I 5 .   ? -16.891 21.074  -14.551 1.00 57.16  ? 309 HOH   B O   1 
HETATM 1769 O O   A HOH   I 5 .   ? -19.995 19.232  -20.601 0.50 149.88 ? 310 HOH   B O   1 
HETATM 1770 O O   B HOH   I 5 .   ? -19.995 19.232  -20.601 0.50 149.88 ? 310 HOH   B O   1 
HETATM 1771 O O   . HOH   I 5 .   ? -12.190 2.631   -5.964  1.00 49.06  ? 311 HOH   B O   1 
HETATM 1772 O O   C HOH   I 5 .   ? -23.018 -6.133  -5.334  0.50 62.27  ? 312 HOH   B O   1 
HETATM 1773 O O   D HOH   I 5 .   ? -23.018 -6.133  -5.334  0.50 62.27  ? 312 HOH   B O   1 
HETATM 1774 O O   . HOH   I 5 .   ? -11.918 12.165  -19.841 1.00 61.17  ? 313 HOH   B O   1 
HETATM 1775 O O   . HOH   I 5 .   ? -6.637  -0.194  -11.204 1.00 51.54  ? 314 HOH   B O   1 
HETATM 1776 O O   A HOH   I 5 .   ? -15.808 -9.657  -15.504 0.50 64.60  ? 315 HOH   B O   1 
HETATM 1777 O O   B HOH   I 5 .   ? -15.808 -9.657  -15.504 0.50 64.60  ? 315 HOH   B O   1 
HETATM 1778 O O   A HOH   I 5 .   ? -30.140 -0.660  -18.715 0.50 69.33  ? 316 HOH   B O   1 
HETATM 1779 O O   B HOH   I 5 .   ? -30.140 -0.660  -18.715 0.50 69.33  ? 316 HOH   B O   1 
HETATM 1780 O O   . HOH   I 5 .   ? -31.958 7.812   -4.424  1.00 66.83  ? 317 HOH   B O   1 
HETATM 1781 O O   . HOH   I 5 .   ? -22.346 -13.086 -21.572 1.00 57.45  ? 318 HOH   B O   1 
HETATM 1782 O O   A HOH   I 5 .   ? -35.560 -5.249  -10.083 0.50 76.09  ? 319 HOH   B O   1 
HETATM 1783 O O   B HOH   I 5 .   ? -35.560 -5.249  -10.083 0.50 76.09  ? 319 HOH   B O   1 
HETATM 1784 O O   A HOH   I 5 .   ? -27.378 -6.226  -5.325  0.50 70.73  ? 320 HOH   B O   1 
HETATM 1785 O O   B HOH   I 5 .   ? -27.378 -6.226  -5.325  0.50 70.73  ? 320 HOH   B O   1 
HETATM 1786 O O   A HOH   I 5 .   ? -10.225 2.107   -8.796  0.11 48.83  ? 321 HOH   B O   1 
HETATM 1787 O O   B HOH   I 5 .   ? -10.225 2.107   -8.796  0.11 48.83  ? 321 HOH   B O   1 
HETATM 1788 O O   C HOH   I 5 .   ? 5.646   1.682   -18.971 0.50 64.55  ? 322 HOH   B O   1 
HETATM 1789 O O   D HOH   I 5 .   ? 5.646   1.682   -18.971 0.50 64.55  ? 322 HOH   B O   1 
HETATM 1790 O O   A HOH   I 5 .   ? -35.392 -2.941  -16.727 0.50 77.35  ? 323 HOH   B O   1 
HETATM 1791 O O   B HOH   I 5 .   ? -35.392 -2.941  -16.727 0.50 77.35  ? 323 HOH   B O   1 
HETATM 1792 O O   A HOH   I 5 .   ? -29.519 16.325  -14.579 0.50 73.71  ? 324 HOH   B O   1 
HETATM 1793 O O   B HOH   I 5 .   ? -29.519 16.325  -14.579 0.50 73.71  ? 324 HOH   B O   1 
HETATM 1794 O O   A HOH   I 5 .   ? -12.925 11.249  -14.085 0.50 78.01  ? 325 HOH   B O   1 
HETATM 1795 O O   B HOH   I 5 .   ? -12.925 11.249  -14.085 0.50 78.01  ? 325 HOH   B O   1 
HETATM 1796 O O   C HOH   I 5 .   ? -21.333 14.264  -34.312 0.50 69.46  ? 326 HOH   B O   1 
HETATM 1797 O O   D HOH   I 5 .   ? -21.333 14.264  -34.312 0.50 69.46  ? 326 HOH   B O   1 
HETATM 1798 O O   A HOH   I 5 .   ? -32.773 -6.570  -6.456  0.50 67.71  ? 327 HOH   B O   1 
HETATM 1799 O O   B HOH   I 5 .   ? -32.773 -6.570  -6.456  0.50 67.71  ? 327 HOH   B O   1 
HETATM 1800 O O   . HOH   I 5 .   ? -21.300 7.762   0.000   0.50 63.30  ? 328 HOH   B O   1 
HETATM 1801 O O   A HOH   I 5 .   ? -9.960  -6.170  -25.470 0.50 75.66  ? 329 HOH   B O   1 
HETATM 1802 O O   B HOH   I 5 .   ? -9.960  -6.170  -25.470 0.50 75.66  ? 329 HOH   B O   1 
HETATM 1803 O O   . HOH   I 5 .   ? -14.418 -5.573  -1.908  1.00 56.84  ? 330 HOH   B O   1 
HETATM 1804 O O   A HOH   I 5 .   ? -12.761 -17.743 -28.058 0.50 73.84  ? 331 HOH   B O   1 
HETATM 1805 O O   B HOH   I 5 .   ? -12.761 -17.743 -28.058 0.50 73.84  ? 331 HOH   B O   1 
HETATM 1806 O O   A HOH   I 5 .   ? -22.125 -11.726 -12.893 0.50 74.44  ? 332 HOH   B O   1 
HETATM 1807 O O   B HOH   I 5 .   ? -22.125 -11.726 -12.893 0.50 74.44  ? 332 HOH   B O   1 
HETATM 1808 O O   . HOH   I 5 .   ? -28.048 -5.692  -18.564 1.00 52.96  ? 333 HOH   B O   1 
HETATM 1809 O O   . HOH   I 5 .   ? -12.730 -2.956  -10.289 1.00 50.23  ? 334 HOH   B O   1 
HETATM 1810 O O   . HOH   I 5 .   ? -16.841 -14.221 -16.476 1.00 57.95  ? 335 HOH   B O   1 
HETATM 1811 O O   . HOH   I 5 .   ? -18.260 -10.338 -16.561 1.00 50.15  ? 336 HOH   B O   1 
HETATM 1812 O O   A HOH   I 5 .   ? -11.701 -4.410  -8.295  0.50 60.44  ? 337 HOH   B O   1 
HETATM 1813 O O   B HOH   I 5 .   ? -11.701 -4.410  -8.295  0.50 60.44  ? 337 HOH   B O   1 
HETATM 1814 O O   A HOH   I 5 .   ? -21.782 6.652   -33.070 0.50 84.30  ? 338 HOH   B O   1 
HETATM 1815 O O   B HOH   I 5 .   ? -21.782 6.652   -33.070 0.50 84.30  ? 338 HOH   B O   1 
HETATM 1816 O O   . HOH   I 5 .   ? -15.409 9.786   -0.949  1.00 55.61  ? 339 HOH   B O   1 
HETATM 1817 O O   . HOH   I 5 .   ? -17.559 -13.947 -30.763 1.00 62.00  ? 340 HOH   B O   1 
HETATM 1818 O O   A HOH   I 5 .   ? -16.423 -6.674  -8.249  0.50 73.35  ? 341 HOH   B O   1 
HETATM 1819 O O   B HOH   I 5 .   ? -16.423 -6.674  -8.249  0.50 73.35  ? 341 HOH   B O   1 
HETATM 1820 O O   A HOH   I 5 .   ? -19.090 26.054  -14.833 0.50 70.86  ? 342 HOH   B O   1 
HETATM 1821 O O   B HOH   I 5 .   ? -19.090 26.054  -14.833 0.50 70.86  ? 342 HOH   B O   1 
HETATM 1822 O O   . HOH   I 5 .   ? -30.771 5.133   -2.320  1.00 61.92  ? 343 HOH   B O   1 
HETATM 1823 O O   . HOH   I 5 .   ? -19.187 -5.056  -0.897  1.00 58.66  ? 344 HOH   B O   1 
HETATM 1824 O O   A HOH   I 5 .   ? -17.726 15.599  -30.878 0.50 68.83  ? 345 HOH   B O   1 
HETATM 1825 O O   B HOH   I 5 .   ? -17.726 15.599  -30.878 0.50 68.83  ? 345 HOH   B O   1 
HETATM 1826 O O   . HOH   I 5 .   ? -26.294 -4.150  -3.845  1.00 52.51  ? 346 HOH   B O   1 
HETATM 1827 O O   . HOH   I 5 .   ? -19.450 15.652  -22.358 1.00 50.16  ? 347 HOH   B O   1 
HETATM 1828 O O   . HOH   I 5 .   ? -24.542 -14.240 -17.418 1.00 69.57  ? 348 HOH   B O   1 
HETATM 1829 O O   C HOH   I 5 .   ? -7.411  8.042   -24.346 0.39 62.07  ? 349 HOH   B O   1 
HETATM 1830 O O   D HOH   I 5 .   ? -7.411  8.042   -24.346 0.39 62.07  ? 349 HOH   B O   1 
HETATM 1831 O O   A HOH   I 5 .   ? -1.128  1.351   -13.940 0.50 73.82  ? 350 HOH   B O   1 
HETATM 1832 O O   B HOH   I 5 .   ? -1.128  1.351   -13.940 0.50 73.82  ? 350 HOH   B O   1 
HETATM 1833 O O   C HOH   I 5 .   ? -5.970  -9.809  -0.547  0.50 70.66  ? 351 HOH   B O   1 
HETATM 1834 O O   D HOH   I 5 .   ? -5.970  -9.809  -0.547  0.50 70.66  ? 351 HOH   B O   1 
HETATM 1835 O O   . HOH   I 5 .   ? -11.291 8.322   -14.116 1.00 61.43  ? 352 HOH   B O   1 
HETATM 1836 O O   . HOH   I 5 .   ? -15.672 16.823  -20.525 1.00 55.34  ? 353 HOH   B O   1 
HETATM 1837 O O   . HOH   I 5 .   ? -8.880  -10.228 -7.519  1.00 62.68  ? 354 HOH   B O   1 
HETATM 1838 O O   . HOH   I 5 .   ? -6.971  -10.590 -5.597  1.00 59.61  ? 355 HOH   B O   1 
HETATM 1839 O O   . HOH   I 5 .   ? -20.577 -7.429  -2.861  1.00 60.64  ? 356 HOH   B O   1 
HETATM 1840 O O   A HOH   I 5 .   ? -20.563 25.521  -16.980 0.25 62.64  ? 357 HOH   B O   1 
HETATM 1841 O O   B HOH   I 5 .   ? -20.563 25.521  -16.980 0.25 62.64  ? 357 HOH   B O   1 
HETATM 1842 O O   C HOH   I 5 .   ? -22.562 15.622  -5.996  0.25 38.89  ? 357 HOH   B O   1 
HETATM 1843 O O   D HOH   I 5 .   ? -22.562 15.622  -5.996  0.25 38.89  ? 357 HOH   B O   1 
HETATM 1844 O O   A HOH   I 5 .   ? -7.337  -5.669  0.135   0.50 64.10  ? 358 HOH   B O   1 
HETATM 1845 O O   B HOH   I 5 .   ? -7.337  -5.669  0.135   0.50 64.10  ? 358 HOH   B O   1 
HETATM 1846 O O   A HOH   I 5 .   ? -15.199 -11.807 -16.884 0.50 63.39  ? 359 HOH   B O   1 
HETATM 1847 O O   B HOH   I 5 .   ? -15.199 -11.807 -16.884 0.50 63.39  ? 359 HOH   B O   1 
HETATM 1848 O O   . HOH   I 5 .   ? -20.103 -12.811 -23.134 1.00 52.12  ? 360 HOH   B O   1 
HETATM 1849 O O   . HOH   I 5 .   ? -24.548 -6.379  -1.173  1.00 66.52  ? 361 HOH   B O   1 
HETATM 1850 O O   . HOH   I 5 .   ? -2.059  -14.460 -9.965  1.00 66.49  ? 362 HOH   B O   1 
HETATM 1851 O O   A HOH   I 5 .   ? -11.153 23.894  -12.541 0.50 84.06  ? 363 HOH   B O   1 
HETATM 1852 O O   B HOH   I 5 .   ? -11.153 23.894  -12.541 0.50 84.06  ? 363 HOH   B O   1 
HETATM 1853 O O   A HOH   I 5 .   ? -19.533 -11.191 -14.359 0.50 87.47  ? 364 HOH   B O   1 
HETATM 1854 O O   B HOH   I 5 .   ? -19.533 -11.191 -14.359 0.50 87.47  ? 364 HOH   B O   1 
HETATM 1855 O O   A HOH   I 5 .   ? -17.549 17.071  -21.830 0.50 77.90  ? 365 HOH   B O   1 
HETATM 1856 O O   B HOH   I 5 .   ? -17.549 17.071  -21.830 0.50 77.90  ? 365 HOH   B O   1 
HETATM 1857 O O   . HOH   I 5 .   ? -30.878 -7.174  -5.076  1.00 61.19  ? 366 HOH   B O   1 
HETATM 1858 O O   . HOH   I 5 .   ? -17.385 27.955  -14.036 1.00 67.40  ? 367 HOH   B O   1 
HETATM 1859 O O   A HOH   I 5 .   ? -29.378 -5.008  -0.715  0.50 65.06  ? 368 HOH   B O   1 
HETATM 1860 O O   B HOH   I 5 .   ? -29.378 -5.008  -0.715  0.50 65.06  ? 368 HOH   B O   1 
HETATM 1861 O O   A HOH   I 5 .   ? -29.719 -12.386 -27.870 0.50 89.32  ? 369 HOH   B O   1 
HETATM 1862 O O   B HOH   I 5 .   ? -29.719 -12.386 -27.870 0.50 89.32  ? 369 HOH   B O   1 
HETATM 1863 O O   A HOH   I 5 .   ? -11.769 5.826   -4.928  0.50 78.46  ? 370 HOH   B O   1 
HETATM 1864 O O   B HOH   I 5 .   ? -11.769 5.826   -4.928  0.50 78.46  ? 370 HOH   B O   1 
HETATM 1865 O O   . HOH   I 5 .   ? -21.300 4.621   0.000   0.50 70.68  ? 371 HOH   B O   1 
HETATM 1866 O O   A HOH   I 5 .   ? -12.251 -6.736  1.851   0.50 91.65  ? 372 HOH   B O   1 
HETATM 1867 O O   B HOH   I 5 .   ? -12.251 -6.736  1.851   0.50 91.65  ? 372 HOH   B O   1 
# 
