data_7I1W
# 
_entry.id   7I1W 
# 
_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   7I1W         pdb_00007i1w 10.2210/pdb7i1w/pdb 
WWPDB D_1001408211 ?            ?                   
# 
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                        7I1W 
_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    3  ? ?    ? ? 
4 non-polymer syn '(1r,4r)-4-amino-N-[4-(hydroxymethyl)-2-methylquinolin-8-yl]cyclohexane-1-carboxamide' 313.394   1  ? ?    ? ? 
5 water       nat water                                                                                  18.015    99 ? ?    ? ? 
# 
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 '(1r,4r)-4-amino-N-[4-(hydroxymethyl)-2-methylquinolin-8-yl]cyclohexane-1-carboxamide' A1BXO 
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 
A1BXO non-polymer         . '(1r,4r)-4-amino-N-[4-(hydroxymethyl)-2-methylquinolin-8-yl]cyclohexane-1-carboxamide' ? 
'C18 H23 N3 O2'  313.394 
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        A1BXO 
_pdbx_entity_instance_feature.asym_id        ? 
_pdbx_entity_instance_feature.seq_num        ? 
_pdbx_entity_instance_feature.auth_comp_id   A1BXO 
_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 A1BXO 1  204 301 A1BXO LIG B . 
G 5 HOH   1  101 105 HOH   HOH A . 
G 5 HOH   2  102 48  HOH   HOH A . 
G 5 HOH   3  103 118 HOH   HOH A . 
G 5 HOH   4  104 36  HOH   HOH A . 
G 5 HOH   5  105 34  HOH   HOH A . 
G 5 HOH   6  106 121 HOH   HOH A . 
G 5 HOH   7  107 50  HOH   HOH A . 
G 5 HOH   8  108 98  HOH   HOH A . 
G 5 HOH   9  109 110 HOH   HOH A . 
G 5 HOH   10 110 20  HOH   HOH A . 
G 5 HOH   11 111 16  HOH   HOH A . 
G 5 HOH   12 112 85  HOH   HOH A . 
G 5 HOH   13 113 49  HOH   HOH A . 
G 5 HOH   14 114 120 HOH   HOH A . 
G 5 HOH   15 115 28  HOH   HOH A . 
G 5 HOH   16 116 29  HOH   HOH A . 
G 5 HOH   17 117 129 HOH   HOH A . 
G 5 HOH   18 118 70  HOH   HOH A . 
G 5 HOH   19 119 119 HOH   HOH A . 
G 5 HOH   20 120 27  HOH   HOH A . 
G 5 HOH   21 121 40  HOH   HOH A . 
H 5 HOH   1  301 90  HOH   HOH B . 
H 5 HOH   2  302 11  HOH   HOH B . 
H 5 HOH   3  303 5   HOH   HOH B . 
H 5 HOH   4  304 92  HOH   HOH B . 
H 5 HOH   5  305 51  HOH   HOH B . 
H 5 HOH   6  306 69  HOH   HOH B . 
H 5 HOH   7  307 54  HOH   HOH B . 
H 5 HOH   8  308 128 HOH   HOH B . 
H 5 HOH   9  309 58  HOH   HOH B . 
H 5 HOH   10 310 77  HOH   HOH B . 
H 5 HOH   11 311 117 HOH   HOH B . 
H 5 HOH   12 312 14  HOH   HOH B . 
H 5 HOH   13 313 31  HOH   HOH B . 
H 5 HOH   14 314 46  HOH   HOH B . 
H 5 HOH   15 315 89  HOH   HOH B . 
H 5 HOH   16 316 63  HOH   HOH B . 
H 5 HOH   17 317 123 HOH   HOH B . 
H 5 HOH   18 318 66  HOH   HOH B . 
H 5 HOH   19 319 30  HOH   HOH B . 
H 5 HOH   20 320 1   HOH   HOH B . 
H 5 HOH   21 321 124 HOH   HOH B . 
H 5 HOH   22 322 9   HOH   HOH B . 
H 5 HOH   23 323 115 HOH   HOH B . 
H 5 HOH   24 324 103 HOH   HOH B . 
H 5 HOH   25 325 39  HOH   HOH B . 
H 5 HOH   26 326 81  HOH   HOH B . 
H 5 HOH   27 327 68  HOH   HOH B . 
H 5 HOH   28 328 56  HOH   HOH B . 
H 5 HOH   29 329 13  HOH   HOH B . 
H 5 HOH   30 330 65  HOH   HOH B . 
H 5 HOH   31 331 32  HOH   HOH B . 
H 5 HOH   32 332 107 HOH   HOH B . 
H 5 HOH   33 333 62  HOH   HOH B . 
H 5 HOH   34 334 108 HOH   HOH B . 
H 5 HOH   35 335 72  HOH   HOH B . 
H 5 HOH   36 336 35  HOH   HOH B . 
H 5 HOH   37 337 67  HOH   HOH B . 
H 5 HOH   38 338 23  HOH   HOH B . 
H 5 HOH   39 339 64  HOH   HOH B . 
H 5 HOH   40 340 21  HOH   HOH B . 
H 5 HOH   41 341 3   HOH   HOH B . 
H 5 HOH   42 342 60  HOH   HOH B . 
H 5 HOH   43 343 100 HOH   HOH B . 
H 5 HOH   44 344 82  HOH   HOH B . 
H 5 HOH   45 345 2   HOH   HOH B . 
H 5 HOH   46 346 130 HOH   HOH B . 
H 5 HOH   47 347 4   HOH   HOH B . 
H 5 HOH   48 348 106 HOH   HOH B . 
H 5 HOH   49 349 10  HOH   HOH B . 
H 5 HOH   50 350 73  HOH   HOH B . 
H 5 HOH   51 351 116 HOH   HOH B . 
H 5 HOH   52 352 102 HOH   HOH B . 
H 5 HOH   53 353 132 HOH   HOH B . 
H 5 HOH   54 354 17  HOH   HOH B . 
H 5 HOH   55 355 42  HOH   HOH B . 
H 5 HOH   56 356 131 HOH   HOH B . 
H 5 HOH   57 357 43  HOH   HOH B . 
H 5 HOH   58 358 12  HOH   HOH B . 
H 5 HOH   59 359 122 HOH   HOH B . 
H 5 HOH   60 360 18  HOH   HOH B . 
H 5 HOH   61 361 112 HOH   HOH B . 
H 5 HOH   62 362 24  HOH   HOH B . 
H 5 HOH   63 363 94  HOH   HOH B . 
H 5 HOH   64 364 87  HOH   HOH B . 
H 5 HOH   65 365 61  HOH   HOH B . 
H 5 HOH   66 366 26  HOH   HOH B . 
H 5 HOH   67 367 79  HOH   HOH B . 
H 5 HOH   68 368 125 HOH   HOH B . 
H 5 HOH   69 369 80  HOH   HOH B . 
H 5 HOH   70 370 45  HOH   HOH B . 
H 5 HOH   71 371 59  HOH   HOH B . 
H 5 HOH   72 372 126 HOH   HOH B . 
H 5 HOH   73 373 57  HOH   HOH B . 
H 5 HOH   74 374 127 HOH   HOH B . 
H 5 HOH   75 375 83  HOH   HOH B . 
H 5 HOH   76 376 75  HOH   HOH B . 
H 5 HOH   77 377 44  HOH   HOH B . 
H 5 HOH   78 378 109 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           7I1W 
_cell.length_a           42.550 
_cell.length_b           42.550 
_cell.length_c           216.477 
_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                         7I1W 
_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          7I1W 
_exptl.method            'X-RAY DIFFRACTION' 
_exptl.crystals_number   1 
# 
_exptl_crystal.id                    1 
_exptl_crystal.density_meas          ? 
_exptl_crystal.density_Matthews      2.11 
_exptl_crystal.density_percent_sol   41.79 
_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                     7I1W 
_reflns.pdbx_diffrn_id               1 
_reflns.pdbx_ordinal                 1 
_reflns.d_resolution_low             108.25 
_reflns.d_resolution_high            1.67 
_reflns.number_obs                   24401 
_reflns.percent_possible_obs         100.0 
_reflns.pdbx_Rmerge_I_obs            0.101 
_reflns.pdbx_netI_over_sigmaI        13.6 
_reflns.pdbx_redundancy              25.6 
_reflns.pdbx_Rrim_I_all              0.103 
_reflns.pdbx_Rpim_I_all              0.021 
_reflns.pdbx_CC_half                 0.999 
_reflns.pdbx_number_measured_all     624309 
_reflns.pdbx_chi_squared             0.33 
_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                  1.67 
_reflns_shell.d_res_low                   1.70 
_reflns_shell.number_measured_all         32755 
_reflns_shell.number_unique_obs           1233 
_reflns_shell.Rmerge_I_obs                ? 
_reflns_shell.pdbx_chi_squared            0.11 
_reflns_shell.pdbx_redundancy             26.6 
_reflns_shell.percent_possible_obs        100.0 
_reflns_shell.pdbx_netI_over_sigmaI_obs   0.2 
_reflns_shell.pdbx_Rrim_I_all             12.002 
_reflns_shell.pdbx_Rpim_I_all             2.299 
_reflns_shell.pdbx_CC_half                0.261 
_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                                 7I1W 
_refine.pdbx_diffrn_id                           1 
_refine.pdbx_TLS_residual_ADP_flag               ? 
_refine.ls_number_reflns_obs                     20969 
_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                             54.12 
_refine.ls_d_res_high                            1.67 
_refine.ls_percent_reflns_obs                    90.89 
_refine.ls_R_factor_obs                          0.24493 
_refine.ls_R_factor_all                          ? 
_refine.ls_R_factor_R_work                       0.24131 
_refine.ls_R_factor_R_free                       0.31376 
_refine.ls_R_factor_R_free_error                 ? 
_refine.ls_R_factor_R_free_error_details         ? 
_refine.ls_percent_reflns_R_free                 5.1 
_refine.ls_number_reflns_R_free                  1124 
_refine.ls_number_parameters                     ? 
_refine.ls_number_restraints                     ? 
_refine.occupancy_min                            ? 
_refine.occupancy_max                            ? 
_refine.correlation_coeff_Fo_to_Fc               0.961 
_refine.correlation_coeff_Fo_to_Fc_free          0.935 
_refine.B_iso_mean                               52.110 
_refine.aniso_B[1][1]                            1.77 
_refine.aniso_B[2][2]                            1.77 
_refine.aniso_B[3][3]                            -3.54 
_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                       0.161 
_refine.pdbx_overall_ESU_R_Free                  0.167 
_refine.overall_SU_ML                            0.265 
_refine.pdbx_overall_phase_error                 ? 
_refine.overall_SU_B                             10.027 
_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         35 
_refine_hist.number_atoms_solvent             99 
_refine_hist.number_atoms_total               1610 
_refine_hist.d_res_high                       1.67 
_refine_hist.d_res_low                        54.12 
# 
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             0.009  0.014  ? 2086 'X-RAY DIFFRACTION' ? 
r_bond_other_d               0.001  0.015  ? 1711 'X-RAY DIFFRACTION' ? 
r_angle_refined_deg          1.584  1.634  ? 2531 'X-RAY DIFFRACTION' ? 
r_angle_other_deg            1.217  1.591  ? 3961 'X-RAY DIFFRACTION' ? 
r_dihedral_angle_1_deg       7.915  5.000  ? 247  'X-RAY DIFFRACTION' ? 
r_dihedral_angle_2_deg       32.511 22.771 ? 83   'X-RAY DIFFRACTION' ? 
r_dihedral_angle_3_deg       15.803 15.000 ? 286  'X-RAY DIFFRACTION' ? 
r_dihedral_angle_4_deg       14.114 15.000 ? 10   'X-RAY DIFFRACTION' ? 
r_chiral_restr               0.064  0.200  ? 229  'X-RAY DIFFRACTION' ? 
r_gen_planes_refined         0.008  0.020  ? 2188 'X-RAY DIFFRACTION' ? 
r_gen_planes_other           0.001  0.020  ? 414  '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                  4.226  5.321  ? 1061 'X-RAY DIFFRACTION' ? 
r_mcbond_other               4.305  5.268  ? 1017 'X-RAY DIFFRACTION' ? 
r_mcangle_it                 6.286  7.760  ? 1191 'X-RAY DIFFRACTION' ? 
r_mcangle_other              6.287  7.764  ? 1192 'X-RAY DIFFRACTION' ? 
r_scbond_it                  4.838  5.616  ? 1025 'X-RAY DIFFRACTION' ? 
r_scbond_other               4.835  5.615  ? 1026 'X-RAY DIFFRACTION' ? 
r_scangle_it                 ?      ?      ? ?    'X-RAY DIFFRACTION' ? 
r_scangle_other              7.333  8.120  ? 1341 'X-RAY DIFFRACTION' ? 
r_long_range_B_refined       9.753  56.595 ? 2061 'X-RAY DIFFRACTION' ? 
r_long_range_B_other         9.691  56.306 ? 2035 '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                       1.671 
_refine_ls_shell.d_res_low                        1.714 
_refine_ls_shell.number_reflns_R_work             201 
_refine_ls_shell.R_factor_R_work                  0.833 
_refine_ls_shell.percent_reflns_obs               12.31 
_refine_ls_shell.R_factor_R_free                  0.921 
_refine_ls_shell.R_factor_R_free_error            ? 
_refine_ls_shell.percent_reflns_R_free            ? 
_refine_ls_shell.number_reflns_R_free             14 
_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                  7I1W 
_struct.title                     
'PanDDA analysis group deposition -- Crystal Structure of ZIKV NS2B-NS3 protease in complex with 3632-JP-070-010' 
_struct.pdbx_model_details        ? 
_struct.pdbx_CASP_flag            ? 
_struct.pdbx_model_type_details   ? 
# 
_struct_keywords.entry_id        7I1W 
_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 5 ? 
H 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 7I1W A 3 ? 46  ? Q32ZE1 1414 ? 1457 ? 46 89  
2 2 7I1W 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 7I1W SER A 1  ? UNP Q32ZE1 ?   ?    'expression tag'        44  1 
1 7I1W MET A 2  ? UNP Q32ZE1 ?   ?    'expression tag'        45  2 
2 7I1W MET B 1  ? UNP Q32ZE1 ?   ?    'initiating methionine' 10  3 
2 7I1W 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 
# 
_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   ? 
# 
_struct_conn.id                            disulf1 
_struct_conn.conn_type_id                  disulf 
_struct_conn.pdbx_leaving_atom_flag        ? 
_struct_conn.pdbx_PDB_id                   ? 
_struct_conn.ptnr1_label_asym_id           B 
_struct_conn.ptnr1_label_comp_id           CYS 
_struct_conn.ptnr1_label_seq_id            134 
_struct_conn.ptnr1_label_atom_id           SG 
_struct_conn.pdbx_ptnr1_label_alt_id       ? 
_struct_conn.pdbx_ptnr1_PDB_ins_code       ? 
_struct_conn.pdbx_ptnr1_standard_comp_id   ? 
_struct_conn.ptnr1_symmetry                1_555 
_struct_conn.ptnr2_label_asym_id           B 
_struct_conn.ptnr2_label_comp_id           CYS 
_struct_conn.ptnr2_label_seq_id            134 
_struct_conn.ptnr2_label_atom_id           SG 
_struct_conn.pdbx_ptnr2_label_alt_id       ? 
_struct_conn.pdbx_ptnr2_PDB_ins_code       ? 
_struct_conn.ptnr1_auth_asym_id            B 
_struct_conn.ptnr1_auth_comp_id            CYS 
_struct_conn.ptnr1_auth_seq_id             143 
_struct_conn.ptnr2_auth_asym_id            B 
_struct_conn.ptnr2_auth_comp_id            CYS 
_struct_conn.ptnr2_auth_seq_id             143 
_struct_conn.ptnr2_symmetry                8_444 
_struct_conn.pdbx_ptnr3_label_atom_id      ? 
_struct_conn.pdbx_ptnr3_label_seq_id       ? 
_struct_conn.pdbx_ptnr3_label_comp_id      ? 
_struct_conn.pdbx_ptnr3_label_asym_id      ? 
_struct_conn.pdbx_ptnr3_label_alt_id       ? 
_struct_conn.pdbx_ptnr3_PDB_ins_code       ? 
_struct_conn.details                       ? 
_struct_conn.pdbx_dist_value               2.513 
_struct_conn.pdbx_value_order              ? 
_struct_conn.pdbx_role                     ? 
# 
_struct_conn_type.id          disulf 
_struct_conn_type.criteria    ? 
_struct_conn_type.reference   ? 
# 
_pdbx_modification_feature.ordinal                            1 
_pdbx_modification_feature.label_comp_id                      CYS 
_pdbx_modification_feature.label_asym_id                      B 
_pdbx_modification_feature.label_seq_id                       134 
_pdbx_modification_feature.label_alt_id                       ? 
_pdbx_modification_feature.modified_residue_label_comp_id     CYS 
_pdbx_modification_feature.modified_residue_label_asym_id     B 
_pdbx_modification_feature.modified_residue_label_seq_id      134 
_pdbx_modification_feature.modified_residue_label_alt_id      ? 
_pdbx_modification_feature.auth_comp_id                       CYS 
_pdbx_modification_feature.auth_asym_id                       B 
_pdbx_modification_feature.auth_seq_id                        143 
_pdbx_modification_feature.PDB_ins_code                       ? 
_pdbx_modification_feature.symmetry                           1_555 
_pdbx_modification_feature.modified_residue_auth_comp_id      CYS 
_pdbx_modification_feature.modified_residue_auth_asym_id      B 
_pdbx_modification_feature.modified_residue_auth_seq_id       143 
_pdbx_modification_feature.modified_residue_PDB_ins_code      ? 
_pdbx_modification_feature.modified_residue_symmetry          8_444 
_pdbx_modification_feature.comp_id_linking_atom               SG 
_pdbx_modification_feature.modified_residue_id_linking_atom   SG 
_pdbx_modification_feature.modified_residue_id                . 
_pdbx_modification_feature.ref_pcm_id                         . 
_pdbx_modification_feature.ref_comp_id                        . 
_pdbx_modification_feature.type                               None 
_pdbx_modification_feature.category                           'Disulfide bridge' 
# 
loop_
_struct_sheet.id 
_struct_sheet.type 
_struct_sheet.number_strands 
_struct_sheet.details 
AA1 ? 8 ? 
AA2 ? 5 ? 
AA3 ? 6 ? 
# 
loop_
_struct_sheet_order.sheet_id 
_struct_sheet_order.range_id_1 
_struct_sheet_order.range_id_2 
_struct_sheet_order.offset 
_struct_sheet_order.sense 
AA1 1 2 ? anti-parallel 
AA1 2 3 ? parallel      
AA1 3 4 ? anti-parallel 
AA1 4 5 ? anti-parallel 
AA1 5 6 ? anti-parallel 
AA1 6 7 ? anti-parallel 
AA1 7 8 ? anti-parallel 
AA2 1 2 ? parallel      
AA2 2 3 ? anti-parallel 
AA2 3 4 ? anti-parallel 
AA2 4 5 ? anti-parallel 
AA3 1 2 ? anti-parallel 
AA3 2 3 ? parallel      
AA3 3 4 ? anti-parallel 
AA3 4 5 ? anti-parallel 
AA3 5 6 ? anti-parallel 
# 
loop_
_struct_sheet_range.sheet_id 
_struct_sheet_range.id 
_struct_sheet_range.beg_label_comp_id 
_struct_sheet_range.beg_label_asym_id 
_struct_sheet_range.beg_label_seq_id 
_struct_sheet_range.pdbx_beg_PDB_ins_code 
_struct_sheet_range.end_label_comp_id 
_struct_sheet_range.end_label_asym_id 
_struct_sheet_range.end_label_seq_id 
_struct_sheet_range.pdbx_end_PDB_ins_code 
_struct_sheet_range.beg_auth_comp_id 
_struct_sheet_range.beg_auth_asym_id 
_struct_sheet_range.beg_auth_seq_id 
_struct_sheet_range.end_auth_comp_id 
_struct_sheet_range.end_auth_asym_id 
_struct_sheet_range.end_auth_seq_id 
AA1 1 GLY B 54  ? LEU B 56  ? GLY B 63  LEU B 65  
AA1 2 LEU B 49  ? SER B 51  ? LEU B 58  SER B 60  
AA1 3 MET A 8   ? GLY A 14  ? MET A 51  GLY A 57  
AA1 4 GLY B 12  ? THR B 18  ? GLY B 21  THR B 27  
AA1 5 THR B 25  ? GLN B 33  ? THR B 34  GLN B 42  
AA1 6 VAL B 36  ? THR B 39  ? VAL B 45  THR B 48  
AA1 7 LEU B 67  ? TYR B 70  ? LEU B 76  TYR B 79  
AA1 8 PRO B 58  ? ASP B 62  ? PRO B 67  ASP B 71  
AA2 1 GLU A 23  ? VAL A 24  ? GLU A 66  VAL A 67  
AA2 2 LYS B 98  ? THR B 102 ? LYS B 107 THR B 111 
AA2 3 VAL B 86  ? ALA B 90  ? VAL B 95  ALA B 99  
AA2 4 PRO B 129 ? LEU B 131 ? PRO B 138 LEU B 140 
AA2 5 VAL B 137 ? LEU B 140 ? VAL B 146 LEU B 149 
AA3 1 PHE A 41  ? LEU A 43  ? PHE A 84  LEU A 86  
AA3 2 ARG A 30  ? LEU A 35  ? ARG A 73  LEU A 78  
AA3 3 GLY B 105 ? THR B 109 ? GLY B 114 THR B 118 
AA3 4 GLY B 112 ? VAL B 117 ? GLY B 121 VAL B 126 
AA3 5 TYR B 152 ? ALA B 155 ? TYR B 161 ALA B 164 
AA3 6 GLY B 144 ? VAL B 146 ? GLY B 153 VAL B 155 
# 
loop_
_pdbx_struct_sheet_hbond.sheet_id 
_pdbx_struct_sheet_hbond.range_id_1 
_pdbx_struct_sheet_hbond.range_id_2 
_pdbx_struct_sheet_hbond.range_1_label_atom_id 
_pdbx_struct_sheet_hbond.range_1_label_comp_id 
_pdbx_struct_sheet_hbond.range_1_label_asym_id 
_pdbx_struct_sheet_hbond.range_1_label_seq_id 
_pdbx_struct_sheet_hbond.range_1_PDB_ins_code 
_pdbx_struct_sheet_hbond.range_1_auth_atom_id 
_pdbx_struct_sheet_hbond.range_1_auth_comp_id 
_pdbx_struct_sheet_hbond.range_1_auth_asym_id 
_pdbx_struct_sheet_hbond.range_1_auth_seq_id 
_pdbx_struct_sheet_hbond.range_2_label_atom_id 
_pdbx_struct_sheet_hbond.range_2_label_comp_id 
_pdbx_struct_sheet_hbond.range_2_label_asym_id 
_pdbx_struct_sheet_hbond.range_2_label_seq_id 
_pdbx_struct_sheet_hbond.range_2_PDB_ins_code 
_pdbx_struct_sheet_hbond.range_2_auth_atom_id 
_pdbx_struct_sheet_hbond.range_2_auth_comp_id 
_pdbx_struct_sheet_hbond.range_2_auth_asym_id 
_pdbx_struct_sheet_hbond.range_2_auth_seq_id 
AA1 1 2 O LEU B 56  ? O LEU B 65  N LEU B 49  ? N LEU B 58  
AA1 2 3 O ARG B 50  ? O ARG B 59  N ILE A 10  ? N ILE A 53  
AA1 3 4 N 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 TYR B 59  ? N TYR B 68  
AA2 1 2 N GLU A 23  ? N GLU A 66  O GLN B 101 ? O GLN B 110 
AA2 2 3 O THR B 102 ? O THR B 111 N VAL B 86  ? N VAL B 95  
AA2 3 4 N GLN B 87  ? N GLN B 96  O LEU B 131 ? O LEU B 140 
AA2 4 5 N ILE B 130 ? N ILE B 139 O GLY B 139 ? O GLY B 148 
AA3 1 2 O SER A 42  ? O SER A 85  N ALA A 34  ? N ALA A 77  
AA3 2 3 N LEU A 31  ? N LEU A 74  O LYS B 108 ? O LYS B 117 
AA3 3 4 N PHE B 107 ? N PHE B 116 O ILE B 114 ? O ILE B 123 
AA3 4 5 N VAL B 117 ? N VAL B 126 O SER B 154 ? O SER B 163 
AA3 5 6 O VAL B 153 ? O VAL B 162 N VAL B 145 ? N VAL B 154 
# 
_pdbx_entry_details.entry_id                   7I1W 
_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   Y 
# 
loop_
_pdbx_validate_torsion.id 
_pdbx_validate_torsion.PDB_model_num 
_pdbx_validate_torsion.auth_comp_id 
_pdbx_validate_torsion.auth_asym_id 
_pdbx_validate_torsion.auth_seq_id 
_pdbx_validate_torsion.PDB_ins_code 
_pdbx_validate_torsion.label_alt_id 
_pdbx_validate_torsion.phi 
_pdbx_validate_torsion.psi 
1 1 GLU A 66 ? A -55.19  106.83 
2 1 GLU A 66 ? B -55.19  106.83 
3 1 CYS B 80 ? ? 77.47   -4.34  
4 1 LEU B 92 ? ? -126.28 -51.61 
# 
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 325 ? H HOH . 
2 1 B HOH 370 ? H HOH . 
3 1 B HOH 377 ? H 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 
A1BXO N1   N Y N 1   
A1BXO N3   N N N 2   
A1BXO C4   C Y N 3   
A1BXO C5   C Y N 4   
A1BXO C6   C Y N 5   
A1BXO C7   C Y N 6   
A1BXO C8   C Y N 7   
A1BXO C10  C N N 8   
A1BXO C13  C N N 9   
A1BXO C15  C N N 10  
A1BXO C17  C N N 11  
A1BXO C1   C N N 12  
A1BXO C2   C Y N 13  
A1BXO C3   C Y N 14  
A1BXO N2   N N N 15  
A1BXO C9   C N N 16  
A1BXO O1   O N N 17  
A1BXO C11  C N N 18  
A1BXO C12  C N N 19  
A1BXO C14  C N N 20  
A1BXO C16  C Y N 21  
A1BXO O2   O N N 22  
A1BXO C18  C Y N 23  
A1BXO H16  H N N 24  
A1BXO H15  H N N 25  
A1BXO H4   H N N 26  
A1BXO H5   H N N 27  
A1BXO H6   H N N 28  
A1BXO H8   H N N 29  
A1BXO H13  H N N 30  
A1BXO H19  H N N 31  
A1BXO H20  H N N 32  
A1BXO H22  H N N 33  
A1BXO H21  H N N 34  
A1BXO H1   H N N 35  
A1BXO H3   H N N 36  
A1BXO H2   H N N 37  
A1BXO H7   H N N 38  
A1BXO H10  H N N 39  
A1BXO H9   H N N 40  
A1BXO H12  H N N 41  
A1BXO H11  H N N 42  
A1BXO H17  H N N 43  
A1BXO H18  H N N 44  
A1BXO H23  H N N 45  
A1BXO H24  H N N 46  
ALA   N    N N N 47  
ALA   CA   C N S 48  
ALA   C    C N N 49  
ALA   O    O N N 50  
ALA   CB   C N N 51  
ALA   OXT  O N N 52  
ALA   H    H N N 53  
ALA   H2   H N N 54  
ALA   HA   H N N 55  
ALA   HB1  H N N 56  
ALA   HB2  H N N 57  
ALA   HB3  H N N 58  
ALA   HXT  H N N 59  
ARG   N    N N N 60  
ARG   CA   C N S 61  
ARG   C    C N N 62  
ARG   O    O N N 63  
ARG   CB   C N N 64  
ARG   CG   C N N 65  
ARG   CD   C N N 66  
ARG   NE   N N N 67  
ARG   CZ   C N N 68  
ARG   NH1  N N N 69  
ARG   NH2  N N N 70  
ARG   OXT  O N N 71  
ARG   H    H N N 72  
ARG   H2   H N N 73  
ARG   HA   H N N 74  
ARG   HB2  H N N 75  
ARG   HB3  H N N 76  
ARG   HG2  H N N 77  
ARG   HG3  H N N 78  
ARG   HD2  H N N 79  
ARG   HD3  H N N 80  
ARG   HE   H N N 81  
ARG   HH11 H N N 82  
ARG   HH12 H N N 83  
ARG   HH21 H N N 84  
ARG   HH22 H N N 85  
ARG   HXT  H N N 86  
ASN   N    N N N 87  
ASN   CA   C N S 88  
ASN   C    C N N 89  
ASN   O    O N N 90  
ASN   CB   C N N 91  
ASN   CG   C N N 92  
ASN   OD1  O N N 93  
ASN   ND2  N N N 94  
ASN   OXT  O N N 95  
ASN   H    H N N 96  
ASN   H2   H N N 97  
ASN   HA   H N N 98  
ASN   HB2  H N N 99  
ASN   HB3  H N N 100 
ASN   HD21 H N N 101 
ASN   HD22 H N N 102 
ASN   HXT  H N N 103 
ASP   N    N N N 104 
ASP   CA   C N S 105 
ASP   C    C N N 106 
ASP   O    O N N 107 
ASP   CB   C N N 108 
ASP   CG   C N N 109 
ASP   OD1  O N N 110 
ASP   OD2  O N N 111 
ASP   OXT  O N N 112 
ASP   H    H N N 113 
ASP   H2   H N N 114 
ASP   HA   H N N 115 
ASP   HB2  H N N 116 
ASP   HB3  H N N 117 
ASP   HD2  H N N 118 
ASP   HXT  H N N 119 
CYS   N    N N N 120 
CYS   CA   C N R 121 
CYS   C    C N N 122 
CYS   O    O N N 123 
CYS   CB   C N N 124 
CYS   SG   S N N 125 
CYS   OXT  O N N 126 
CYS   H    H N N 127 
CYS   H2   H N N 128 
CYS   HA   H N N 129 
CYS   HB2  H N N 130 
CYS   HB3  H N N 131 
CYS   HG   H N N 132 
CYS   HXT  H N N 133 
DMS   S    S N N 134 
DMS   O    O N N 135 
DMS   C1   C N N 136 
DMS   C2   C N N 137 
DMS   H11  H N N 138 
DMS   H12  H N N 139 
DMS   H13  H N N 140 
DMS   H21  H N N 141 
DMS   H22  H N N 142 
DMS   H23  H N N 143 
GLN   N    N N N 144 
GLN   CA   C N S 145 
GLN   C    C N N 146 
GLN   O    O N N 147 
GLN   CB   C N N 148 
GLN   CG   C N N 149 
GLN   CD   C N N 150 
GLN   OE1  O N N 151 
GLN   NE2  N N N 152 
GLN   OXT  O N N 153 
GLN   H    H N N 154 
GLN   H2   H N N 155 
GLN   HA   H N N 156 
GLN   HB2  H N N 157 
GLN   HB3  H N N 158 
GLN   HG2  H N N 159 
GLN   HG3  H N N 160 
GLN   HE21 H N N 161 
GLN   HE22 H N N 162 
GLN   HXT  H N N 163 
GLU   N    N N N 164 
GLU   CA   C N S 165 
GLU   C    C N N 166 
GLU   O    O N N 167 
GLU   CB   C N N 168 
GLU   CG   C N N 169 
GLU   CD   C N N 170 
GLU   OE1  O N N 171 
GLU   OE2  O N N 172 
GLU   OXT  O N N 173 
GLU   H    H N N 174 
GLU   H2   H N N 175 
GLU   HA   H N N 176 
GLU   HB2  H N N 177 
GLU   HB3  H N N 178 
GLU   HG2  H N N 179 
GLU   HG3  H N N 180 
GLU   HE2  H N N 181 
GLU   HXT  H N N 182 
GLY   N    N N N 183 
GLY   CA   C N N 184 
GLY   C    C N N 185 
GLY   O    O N N 186 
GLY   OXT  O N N 187 
GLY   H    H N N 188 
GLY   H2   H N N 189 
GLY   HA2  H N N 190 
GLY   HA3  H N N 191 
GLY   HXT  H N N 192 
HIS   N    N N N 193 
HIS   CA   C N S 194 
HIS   C    C N N 195 
HIS   O    O N N 196 
HIS   CB   C N N 197 
HIS   CG   C Y N 198 
HIS   ND1  N Y N 199 
HIS   CD2  C Y N 200 
HIS   CE1  C Y N 201 
HIS   NE2  N Y N 202 
HIS   OXT  O N N 203 
HIS   H    H N N 204 
HIS   H2   H N N 205 
HIS   HA   H N N 206 
HIS   HB2  H N N 207 
HIS   HB3  H N N 208 
HIS   HD1  H N N 209 
HIS   HD2  H N N 210 
HIS   HE1  H N N 211 
HIS   HE2  H N N 212 
HIS   HXT  H N N 213 
HOH   O    O N N 214 
HOH   H1   H N N 215 
HOH   H2   H N N 216 
ILE   N    N N N 217 
ILE   CA   C N S 218 
ILE   C    C N N 219 
ILE   O    O N N 220 
ILE   CB   C N S 221 
ILE   CG1  C N N 222 
ILE   CG2  C N N 223 
ILE   CD1  C N N 224 
ILE   OXT  O N N 225 
ILE   H    H N N 226 
ILE   H2   H N N 227 
ILE   HA   H N N 228 
ILE   HB   H N N 229 
ILE   HG12 H N N 230 
ILE   HG13 H N N 231 
ILE   HG21 H N N 232 
ILE   HG22 H N N 233 
ILE   HG23 H N N 234 
ILE   HD11 H N N 235 
ILE   HD12 H N N 236 
ILE   HD13 H N N 237 
ILE   HXT  H N N 238 
LEU   N    N N N 239 
LEU   CA   C N S 240 
LEU   C    C N N 241 
LEU   O    O N N 242 
LEU   CB   C N N 243 
LEU   CG   C N N 244 
LEU   CD1  C N N 245 
LEU   CD2  C N N 246 
LEU   OXT  O N N 247 
LEU   H    H N N 248 
LEU   H2   H N N 249 
LEU   HA   H N N 250 
LEU   HB2  H N N 251 
LEU   HB3  H N N 252 
LEU   HG   H N N 253 
LEU   HD11 H N N 254 
LEU   HD12 H N N 255 
LEU   HD13 H N N 256 
LEU   HD21 H N N 257 
LEU   HD22 H N N 258 
LEU   HD23 H N N 259 
LEU   HXT  H N N 260 
LYS   N    N N N 261 
LYS   CA   C N S 262 
LYS   C    C N N 263 
LYS   O    O N N 264 
LYS   CB   C N N 265 
LYS   CG   C N N 266 
LYS   CD   C N N 267 
LYS   CE   C N N 268 
LYS   NZ   N N N 269 
LYS   OXT  O N N 270 
LYS   H    H N N 271 
LYS   H2   H N N 272 
LYS   HA   H N N 273 
LYS   HB2  H N N 274 
LYS   HB3  H N N 275 
LYS   HG2  H N N 276 
LYS   HG3  H N N 277 
LYS   HD2  H N N 278 
LYS   HD3  H N N 279 
LYS   HE2  H N N 280 
LYS   HE3  H N N 281 
LYS   HZ1  H N N 282 
LYS   HZ2  H N N 283 
LYS   HZ3  H N N 284 
LYS   HXT  H N N 285 
MET   N    N N N 286 
MET   CA   C N S 287 
MET   C    C N N 288 
MET   O    O N N 289 
MET   CB   C N N 290 
MET   CG   C N N 291 
MET   SD   S N N 292 
MET   CE   C N N 293 
MET   OXT  O N N 294 
MET   H    H N N 295 
MET   H2   H N N 296 
MET   HA   H N N 297 
MET   HB2  H N N 298 
MET   HB3  H N N 299 
MET   HG2  H N N 300 
MET   HG3  H N N 301 
MET   HE1  H N N 302 
MET   HE2  H N N 303 
MET   HE3  H N N 304 
MET   HXT  H N N 305 
PHE   N    N N N 306 
PHE   CA   C N S 307 
PHE   C    C N N 308 
PHE   O    O N N 309 
PHE   CB   C N N 310 
PHE   CG   C Y N 311 
PHE   CD1  C Y N 312 
PHE   CD2  C Y N 313 
PHE   CE1  C Y N 314 
PHE   CE2  C Y N 315 
PHE   CZ   C Y N 316 
PHE   OXT  O N N 317 
PHE   H    H N N 318 
PHE   H2   H N N 319 
PHE   HA   H N N 320 
PHE   HB2  H N N 321 
PHE   HB3  H N N 322 
PHE   HD1  H N N 323 
PHE   HD2  H N N 324 
PHE   HE1  H N N 325 
PHE   HE2  H N N 326 
PHE   HZ   H N N 327 
PHE   HXT  H N N 328 
PRO   N    N N N 329 
PRO   CA   C N S 330 
PRO   C    C N N 331 
PRO   O    O N N 332 
PRO   CB   C N N 333 
PRO   CG   C N N 334 
PRO   CD   C N N 335 
PRO   OXT  O N N 336 
PRO   H    H N N 337 
PRO   HA   H N N 338 
PRO   HB2  H N N 339 
PRO   HB3  H N N 340 
PRO   HG2  H N N 341 
PRO   HG3  H N N 342 
PRO   HD2  H N N 343 
PRO   HD3  H N N 344 
PRO   HXT  H N N 345 
SER   N    N N N 346 
SER   CA   C N S 347 
SER   C    C N N 348 
SER   O    O N N 349 
SER   CB   C N N 350 
SER   OG   O N N 351 
SER   OXT  O N N 352 
SER   H    H N N 353 
SER   H2   H N N 354 
SER   HA   H N N 355 
SER   HB2  H N N 356 
SER   HB3  H N N 357 
SER   HG   H N N 358 
SER   HXT  H N N 359 
THR   N    N N N 360 
THR   CA   C N S 361 
THR   C    C N N 362 
THR   O    O N N 363 
THR   CB   C N R 364 
THR   OG1  O N N 365 
THR   CG2  C N N 366 
THR   OXT  O N N 367 
THR   H    H N N 368 
THR   H2   H N N 369 
THR   HA   H N N 370 
THR   HB   H N N 371 
THR   HG1  H N N 372 
THR   HG21 H N N 373 
THR   HG22 H N N 374 
THR   HG23 H N N 375 
THR   HXT  H N N 376 
TRP   N    N N N 377 
TRP   CA   C N S 378 
TRP   C    C N N 379 
TRP   O    O N N 380 
TRP   CB   C N N 381 
TRP   CG   C Y N 382 
TRP   CD1  C Y N 383 
TRP   CD2  C Y N 384 
TRP   NE1  N Y N 385 
TRP   CE2  C Y N 386 
TRP   CE3  C Y N 387 
TRP   CZ2  C Y N 388 
TRP   CZ3  C Y N 389 
TRP   CH2  C Y N 390 
TRP   OXT  O N N 391 
TRP   H    H N N 392 
TRP   H2   H N N 393 
TRP   HA   H N N 394 
TRP   HB2  H N N 395 
TRP   HB3  H N N 396 
TRP   HD1  H N N 397 
TRP   HE1  H N N 398 
TRP   HE3  H N N 399 
TRP   HZ2  H N N 400 
TRP   HZ3  H N N 401 
TRP   HH2  H N N 402 
TRP   HXT  H N N 403 
TYR   N    N N N 404 
TYR   CA   C N S 405 
TYR   C    C N N 406 
TYR   O    O N N 407 
TYR   CB   C N N 408 
TYR   CG   C Y N 409 
TYR   CD1  C Y N 410 
TYR   CD2  C Y N 411 
TYR   CE1  C Y N 412 
TYR   CE2  C Y N 413 
TYR   CZ   C Y N 414 
TYR   OH   O N N 415 
TYR   OXT  O N N 416 
TYR   H    H N N 417 
TYR   H2   H N N 418 
TYR   HA   H N N 419 
TYR   HB2  H N N 420 
TYR   HB3  H N N 421 
TYR   HD1  H N N 422 
TYR   HD2  H N N 423 
TYR   HE1  H N N 424 
TYR   HE2  H N N 425 
TYR   HH   H N N 426 
TYR   HXT  H N N 427 
VAL   N    N N N 428 
VAL   CA   C N S 429 
VAL   C    C N N 430 
VAL   O    O N N 431 
VAL   CB   C N N 432 
VAL   CG1  C N N 433 
VAL   CG2  C N N 434 
VAL   OXT  O N N 435 
VAL   H    H N N 436 
VAL   H2   H N N 437 
VAL   HA   H N N 438 
VAL   HB   H N N 439 
VAL   HG11 H N N 440 
VAL   HG12 H N N 441 
VAL   HG13 H N N 442 
VAL   HG21 H N N 443 
VAL   HG22 H N N 444 
VAL   HG23 H N N 445 
VAL   HXT  H N N 446 
# 
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 
A1BXO C1  C2   sing N N 1   
A1BXO C2  N1   doub Y N 2   
A1BXO N1  C3   sing Y N 3   
A1BXO C3  C4   doub Y N 4   
A1BXO C4  C5   sing Y N 5   
A1BXO C5  C6   doub Y N 6   
A1BXO C6  C7   sing Y N 7   
A1BXO C7  C8   doub Y N 8   
A1BXO C8  N2   sing N N 9   
A1BXO N2  C9   sing N N 10  
A1BXO C9  O1   doub N N 11  
A1BXO C9  C10  sing N N 12  
A1BXO C10 C11  sing N N 13  
A1BXO C11 C12  sing N N 14  
A1BXO C12 C13  sing N N 15  
A1BXO C13 N3   sing N N 16  
A1BXO C13 C14  sing N N 17  
A1BXO C14 C15  sing N N 18  
A1BXO C4  C16  sing Y N 19  
A1BXO C16 C17  sing N N 20  
A1BXO C17 O2   sing N N 21  
A1BXO C16 C18  doub Y N 22  
A1BXO C2  C18  sing Y N 23  
A1BXO C3  C8   sing Y N 24  
A1BXO C10 C15  sing N N 25  
A1BXO N3  H16  sing N N 26  
A1BXO N3  H15  sing N N 27  
A1BXO C5  H4   sing N N 28  
A1BXO C6  H5   sing N N 29  
A1BXO C7  H6   sing N N 30  
A1BXO C10 H8   sing N N 31  
A1BXO C13 H13  sing N N 32  
A1BXO C15 H19  sing N N 33  
A1BXO C15 H20  sing N N 34  
A1BXO C17 H22  sing N N 35  
A1BXO C17 H21  sing N N 36  
A1BXO C1  H1   sing N N 37  
A1BXO C1  H3   sing N N 38  
A1BXO C1  H2   sing N N 39  
A1BXO N2  H7   sing N N 40  
A1BXO C11 H10  sing N N 41  
A1BXO C11 H9   sing N N 42  
A1BXO C12 H12  sing N N 43  
A1BXO C12 H11  sing N N 44  
A1BXO C14 H17  sing N N 45  
A1BXO C14 H18  sing N N 46  
A1BXO O2  H23  sing N N 47  
A1BXO C18 H24  sing N N 48  
ALA   N   CA   sing N N 49  
ALA   N   H    sing N N 50  
ALA   N   H2   sing N N 51  
ALA   CA  C    sing N N 52  
ALA   CA  CB   sing N N 53  
ALA   CA  HA   sing N N 54  
ALA   C   O    doub N N 55  
ALA   C   OXT  sing N N 56  
ALA   CB  HB1  sing N N 57  
ALA   CB  HB2  sing N N 58  
ALA   CB  HB3  sing N N 59  
ALA   OXT HXT  sing N N 60  
ARG   N   CA   sing N N 61  
ARG   N   H    sing N N 62  
ARG   N   H2   sing N N 63  
ARG   CA  C    sing N N 64  
ARG   CA  CB   sing N N 65  
ARG   CA  HA   sing N N 66  
ARG   C   O    doub N N 67  
ARG   C   OXT  sing N N 68  
ARG   CB  CG   sing N N 69  
ARG   CB  HB2  sing N N 70  
ARG   CB  HB3  sing N N 71  
ARG   CG  CD   sing N N 72  
ARG   CG  HG2  sing N N 73  
ARG   CG  HG3  sing N N 74  
ARG   CD  NE   sing N N 75  
ARG   CD  HD2  sing N N 76  
ARG   CD  HD3  sing N N 77  
ARG   NE  CZ   sing N N 78  
ARG   NE  HE   sing N N 79  
ARG   CZ  NH1  sing N N 80  
ARG   CZ  NH2  doub N N 81  
ARG   NH1 HH11 sing N N 82  
ARG   NH1 HH12 sing N N 83  
ARG   NH2 HH21 sing N N 84  
ARG   NH2 HH22 sing N N 85  
ARG   OXT HXT  sing N N 86  
ASN   N   CA   sing N N 87  
ASN   N   H    sing N N 88  
ASN   N   H2   sing N N 89  
ASN   CA  C    sing N N 90  
ASN   CA  CB   sing N N 91  
ASN   CA  HA   sing N N 92  
ASN   C   O    doub N N 93  
ASN   C   OXT  sing N N 94  
ASN   CB  CG   sing N N 95  
ASN   CB  HB2  sing N N 96  
ASN   CB  HB3  sing N N 97  
ASN   CG  OD1  doub N N 98  
ASN   CG  ND2  sing N N 99  
ASN   ND2 HD21 sing N N 100 
ASN   ND2 HD22 sing N N 101 
ASN   OXT HXT  sing N N 102 
ASP   N   CA   sing N N 103 
ASP   N   H    sing N N 104 
ASP   N   H2   sing N N 105 
ASP   CA  C    sing N N 106 
ASP   CA  CB   sing N N 107 
ASP   CA  HA   sing N N 108 
ASP   C   O    doub N N 109 
ASP   C   OXT  sing N N 110 
ASP   CB  CG   sing N N 111 
ASP   CB  HB2  sing N N 112 
ASP   CB  HB3  sing N N 113 
ASP   CG  OD1  doub N N 114 
ASP   CG  OD2  sing N N 115 
ASP   OD2 HD2  sing N N 116 
ASP   OXT HXT  sing N N 117 
CYS   N   CA   sing N N 118 
CYS   N   H    sing N N 119 
CYS   N   H2   sing N N 120 
CYS   CA  C    sing N N 121 
CYS   CA  CB   sing N N 122 
CYS   CA  HA   sing N N 123 
CYS   C   O    doub N N 124 
CYS   C   OXT  sing N N 125 
CYS   CB  SG   sing N N 126 
CYS   CB  HB2  sing N N 127 
CYS   CB  HB3  sing N N 128 
CYS   SG  HG   sing N N 129 
CYS   OXT HXT  sing N N 130 
DMS   S   O    doub N N 131 
DMS   S   C1   sing N N 132 
DMS   S   C2   sing N N 133 
DMS   C1  H11  sing N N 134 
DMS   C1  H12  sing N N 135 
DMS   C1  H13  sing N N 136 
DMS   C2  H21  sing N N 137 
DMS   C2  H22  sing N N 138 
DMS   C2  H23  sing N N 139 
GLN   N   CA   sing N N 140 
GLN   N   H    sing N N 141 
GLN   N   H2   sing N N 142 
GLN   CA  C    sing N N 143 
GLN   CA  CB   sing N N 144 
GLN   CA  HA   sing N N 145 
GLN   C   O    doub N N 146 
GLN   C   OXT  sing N N 147 
GLN   CB  CG   sing N N 148 
GLN   CB  HB2  sing N N 149 
GLN   CB  HB3  sing N N 150 
GLN   CG  CD   sing N N 151 
GLN   CG  HG2  sing N N 152 
GLN   CG  HG3  sing N N 153 
GLN   CD  OE1  doub N N 154 
GLN   CD  NE2  sing N N 155 
GLN   NE2 HE21 sing N N 156 
GLN   NE2 HE22 sing N N 157 
GLN   OXT HXT  sing N N 158 
GLU   N   CA   sing N N 159 
GLU   N   H    sing N N 160 
GLU   N   H2   sing N N 161 
GLU   CA  C    sing N N 162 
GLU   CA  CB   sing N N 163 
GLU   CA  HA   sing N N 164 
GLU   C   O    doub N N 165 
GLU   C   OXT  sing N N 166 
GLU   CB  CG   sing N N 167 
GLU   CB  HB2  sing N N 168 
GLU   CB  HB3  sing N N 169 
GLU   CG  CD   sing N N 170 
GLU   CG  HG2  sing N N 171 
GLU   CG  HG3  sing N N 172 
GLU   CD  OE1  doub N N 173 
GLU   CD  OE2  sing N N 174 
GLU   OE2 HE2  sing N N 175 
GLU   OXT HXT  sing N N 176 
GLY   N   CA   sing N N 177 
GLY   N   H    sing N N 178 
GLY   N   H2   sing N N 179 
GLY   CA  C    sing N N 180 
GLY   CA  HA2  sing N N 181 
GLY   CA  HA3  sing N N 182 
GLY   C   O    doub N N 183 
GLY   C   OXT  sing N N 184 
GLY   OXT HXT  sing N N 185 
HIS   N   CA   sing N N 186 
HIS   N   H    sing N N 187 
HIS   N   H2   sing N N 188 
HIS   CA  C    sing N N 189 
HIS   CA  CB   sing N N 190 
HIS   CA  HA   sing N N 191 
HIS   C   O    doub N N 192 
HIS   C   OXT  sing N N 193 
HIS   CB  CG   sing N N 194 
HIS   CB  HB2  sing N N 195 
HIS   CB  HB3  sing N N 196 
HIS   CG  ND1  sing Y N 197 
HIS   CG  CD2  doub Y N 198 
HIS   ND1 CE1  doub Y N 199 
HIS   ND1 HD1  sing N N 200 
HIS   CD2 NE2  sing Y N 201 
HIS   CD2 HD2  sing N N 202 
HIS   CE1 NE2  sing Y N 203 
HIS   CE1 HE1  sing N N 204 
HIS   NE2 HE2  sing N N 205 
HIS   OXT HXT  sing N N 206 
HOH   O   H1   sing N N 207 
HOH   O   H2   sing N N 208 
ILE   N   CA   sing N N 209 
ILE   N   H    sing N N 210 
ILE   N   H2   sing N N 211 
ILE   CA  C    sing N N 212 
ILE   CA  CB   sing N N 213 
ILE   CA  HA   sing N N 214 
ILE   C   O    doub N N 215 
ILE   C   OXT  sing N N 216 
ILE   CB  CG1  sing N N 217 
ILE   CB  CG2  sing N N 218 
ILE   CB  HB   sing N N 219 
ILE   CG1 CD1  sing N N 220 
ILE   CG1 HG12 sing N N 221 
ILE   CG1 HG13 sing N N 222 
ILE   CG2 HG21 sing N N 223 
ILE   CG2 HG22 sing N N 224 
ILE   CG2 HG23 sing N N 225 
ILE   CD1 HD11 sing N N 226 
ILE   CD1 HD12 sing N N 227 
ILE   CD1 HD13 sing N N 228 
ILE   OXT HXT  sing N N 229 
LEU   N   CA   sing N N 230 
LEU   N   H    sing N N 231 
LEU   N   H2   sing N N 232 
LEU   CA  C    sing N N 233 
LEU   CA  CB   sing N N 234 
LEU   CA  HA   sing N N 235 
LEU   C   O    doub N N 236 
LEU   C   OXT  sing N N 237 
LEU   CB  CG   sing N N 238 
LEU   CB  HB2  sing N N 239 
LEU   CB  HB3  sing N N 240 
LEU   CG  CD1  sing N N 241 
LEU   CG  CD2  sing N N 242 
LEU   CG  HG   sing N N 243 
LEU   CD1 HD11 sing N N 244 
LEU   CD1 HD12 sing N N 245 
LEU   CD1 HD13 sing N N 246 
LEU   CD2 HD21 sing N N 247 
LEU   CD2 HD22 sing N N 248 
LEU   CD2 HD23 sing N N 249 
LEU   OXT HXT  sing N N 250 
LYS   N   CA   sing N N 251 
LYS   N   H    sing N N 252 
LYS   N   H2   sing N N 253 
LYS   CA  C    sing N N 254 
LYS   CA  CB   sing N N 255 
LYS   CA  HA   sing N N 256 
LYS   C   O    doub N N 257 
LYS   C   OXT  sing N N 258 
LYS   CB  CG   sing N N 259 
LYS   CB  HB2  sing N N 260 
LYS   CB  HB3  sing N N 261 
LYS   CG  CD   sing N N 262 
LYS   CG  HG2  sing N N 263 
LYS   CG  HG3  sing N N 264 
LYS   CD  CE   sing N N 265 
LYS   CD  HD2  sing N N 266 
LYS   CD  HD3  sing N N 267 
LYS   CE  NZ   sing N N 268 
LYS   CE  HE2  sing N N 269 
LYS   CE  HE3  sing N N 270 
LYS   NZ  HZ1  sing N N 271 
LYS   NZ  HZ2  sing N N 272 
LYS   NZ  HZ3  sing N N 273 
LYS   OXT HXT  sing N N 274 
MET   N   CA   sing N N 275 
MET   N   H    sing N N 276 
MET   N   H2   sing N N 277 
MET   CA  C    sing N N 278 
MET   CA  CB   sing N N 279 
MET   CA  HA   sing N N 280 
MET   C   O    doub N N 281 
MET   C   OXT  sing N N 282 
MET   CB  CG   sing N N 283 
MET   CB  HB2  sing N N 284 
MET   CB  HB3  sing N N 285 
MET   CG  SD   sing N N 286 
MET   CG  HG2  sing N N 287 
MET   CG  HG3  sing N N 288 
MET   SD  CE   sing N N 289 
MET   CE  HE1  sing N N 290 
MET   CE  HE2  sing N N 291 
MET   CE  HE3  sing N N 292 
MET   OXT HXT  sing N N 293 
PHE   N   CA   sing N N 294 
PHE   N   H    sing N N 295 
PHE   N   H2   sing N N 296 
PHE   CA  C    sing N N 297 
PHE   CA  CB   sing N N 298 
PHE   CA  HA   sing N N 299 
PHE   C   O    doub N N 300 
PHE   C   OXT  sing N N 301 
PHE   CB  CG   sing N N 302 
PHE   CB  HB2  sing N N 303 
PHE   CB  HB3  sing N N 304 
PHE   CG  CD1  doub Y N 305 
PHE   CG  CD2  sing Y N 306 
PHE   CD1 CE1  sing Y N 307 
PHE   CD1 HD1  sing N N 308 
PHE   CD2 CE2  doub Y N 309 
PHE   CD2 HD2  sing N N 310 
PHE   CE1 CZ   doub Y N 311 
PHE   CE1 HE1  sing N N 312 
PHE   CE2 CZ   sing Y N 313 
PHE   CE2 HE2  sing N N 314 
PHE   CZ  HZ   sing N N 315 
PHE   OXT HXT  sing N N 316 
PRO   N   CA   sing N N 317 
PRO   N   CD   sing N N 318 
PRO   N   H    sing N N 319 
PRO   CA  C    sing N N 320 
PRO   CA  CB   sing N N 321 
PRO   CA  HA   sing N N 322 
PRO   C   O    doub N N 323 
PRO   C   OXT  sing N N 324 
PRO   CB  CG   sing N N 325 
PRO   CB  HB2  sing N N 326 
PRO   CB  HB3  sing N N 327 
PRO   CG  CD   sing N N 328 
PRO   CG  HG2  sing N N 329 
PRO   CG  HG3  sing N N 330 
PRO   CD  HD2  sing N N 331 
PRO   CD  HD3  sing N N 332 
PRO   OXT HXT  sing N N 333 
SER   N   CA   sing N N 334 
SER   N   H    sing N N 335 
SER   N   H2   sing N N 336 
SER   CA  C    sing N N 337 
SER   CA  CB   sing N N 338 
SER   CA  HA   sing N N 339 
SER   C   O    doub N N 340 
SER   C   OXT  sing N N 341 
SER   CB  OG   sing N N 342 
SER   CB  HB2  sing N N 343 
SER   CB  HB3  sing N N 344 
SER   OG  HG   sing N N 345 
SER   OXT HXT  sing N N 346 
THR   N   CA   sing N N 347 
THR   N   H    sing N N 348 
THR   N   H2   sing N N 349 
THR   CA  C    sing N N 350 
THR   CA  CB   sing N N 351 
THR   CA  HA   sing N N 352 
THR   C   O    doub N N 353 
THR   C   OXT  sing N N 354 
THR   CB  OG1  sing N N 355 
THR   CB  CG2  sing N N 356 
THR   CB  HB   sing N N 357 
THR   OG1 HG1  sing N N 358 
THR   CG2 HG21 sing N N 359 
THR   CG2 HG22 sing N N 360 
THR   CG2 HG23 sing N N 361 
THR   OXT HXT  sing N N 362 
TRP   N   CA   sing N N 363 
TRP   N   H    sing N N 364 
TRP   N   H2   sing N N 365 
TRP   CA  C    sing N N 366 
TRP   CA  CB   sing N N 367 
TRP   CA  HA   sing N N 368 
TRP   C   O    doub N N 369 
TRP   C   OXT  sing N N 370 
TRP   CB  CG   sing N N 371 
TRP   CB  HB2  sing N N 372 
TRP   CB  HB3  sing N N 373 
TRP   CG  CD1  doub Y N 374 
TRP   CG  CD2  sing Y N 375 
TRP   CD1 NE1  sing Y N 376 
TRP   CD1 HD1  sing N N 377 
TRP   CD2 CE2  doub Y N 378 
TRP   CD2 CE3  sing Y N 379 
TRP   NE1 CE2  sing Y N 380 
TRP   NE1 HE1  sing N N 381 
TRP   CE2 CZ2  sing Y N 382 
TRP   CE3 CZ3  doub Y N 383 
TRP   CE3 HE3  sing N N 384 
TRP   CZ2 CH2  doub Y N 385 
TRP   CZ2 HZ2  sing N N 386 
TRP   CZ3 CH2  sing Y N 387 
TRP   CZ3 HZ3  sing N N 388 
TRP   CH2 HH2  sing N N 389 
TRP   OXT HXT  sing N N 390 
TYR   N   CA   sing N N 391 
TYR   N   H    sing N N 392 
TYR   N   H2   sing N N 393 
TYR   CA  C    sing N N 394 
TYR   CA  CB   sing N N 395 
TYR   CA  HA   sing N N 396 
TYR   C   O    doub N N 397 
TYR   C   OXT  sing N N 398 
TYR   CB  CG   sing N N 399 
TYR   CB  HB2  sing N N 400 
TYR   CB  HB3  sing N N 401 
TYR   CG  CD1  doub Y N 402 
TYR   CG  CD2  sing Y N 403 
TYR   CD1 CE1  sing Y N 404 
TYR   CD1 HD1  sing N N 405 
TYR   CD2 CE2  doub Y N 406 
TYR   CD2 HD2  sing N N 407 
TYR   CE1 CZ   doub Y N 408 
TYR   CE1 HE1  sing N N 409 
TYR   CE2 CZ   sing Y N 410 
TYR   CE2 HE2  sing N N 411 
TYR   CZ  OH   sing N N 412 
TYR   OH  HH   sing N N 413 
TYR   OXT HXT  sing N N 414 
VAL   N   CA   sing N N 415 
VAL   N   H    sing N N 416 
VAL   N   H2   sing N N 417 
VAL   CA  C    sing N N 418 
VAL   CA  CB   sing N N 419 
VAL   CA  HA   sing N N 420 
VAL   C   O    doub N N 421 
VAL   C   OXT  sing N N 422 
VAL   CB  CG1  sing N N 423 
VAL   CB  CG2  sing N N 424 
VAL   CB  HB   sing N N 425 
VAL   CG1 HG11 sing N N 426 
VAL   CG1 HG12 sing N N 427 
VAL   CG1 HG13 sing N N 428 
VAL   CG2 HG21 sing N N 429 
VAL   CG2 HG22 sing N N 430 
VAL   CG2 HG23 sing N N 431 
VAL   OXT HXT  sing N N 432 
# 
_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                    7I1W 
_atom_sites.fract_transf_matrix[1][1]   0.023502 
_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]   0.023502 
_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]   0.004619 
_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   ? -21.463 19.378  -7.236  1.00 79.77  ? 50  ASP   A N   1 
ATOM   2    C CA  . ASP   A 1 7   ? -22.754 18.612  -7.349  1.00 78.76  ? 50  ASP   A CA  1 
ATOM   3    C C   . ASP   A 1 7   ? -22.853 18.022  -8.763  1.00 72.70  ? 50  ASP   A C   1 
ATOM   4    O O   . ASP   A 1 7   ? -22.897 18.784  -9.751  1.00 73.04  ? 50  ASP   A O   1 
ATOM   5    C CB  . ASP   A 1 7   ? -23.978 19.465  -6.993  1.00 73.51  ? 50  ASP   A CB  1 
ATOM   6    C CG  . ASP   A 1 7   ? -24.827 18.880  -5.870  1.00 87.30  ? 50  ASP   A CG  1 
ATOM   7    O OD1 . ASP   A 1 7   ? -24.838 19.488  -4.768  1.00 94.26  ? 50  ASP   A OD1 1 
ATOM   8    O OD2 . ASP   A 1 7   ? -25.478 17.830  -6.092  1.00 80.61  ? 50  ASP   A OD2 1 
ATOM   9    N N   . MET   A 1 8   ? -22.884 16.698  -8.840  1.00 59.03  ? 51  MET   A N   1 
ATOM   10   C CA  . MET   A 1 8   ? -22.801 15.924  -10.104 1.00 54.09  ? 51  MET   A CA  1 
ATOM   11   C C   . MET   A 1 8   ? -24.201 15.661  -10.628 1.00 40.63  ? 51  MET   A C   1 
ATOM   12   O O   . MET   A 1 8   ? -25.103 15.409  -9.809  1.00 51.63  ? 51  MET   A O   1 
ATOM   13   C CB  . MET   A 1 8   ? -22.072 14.600  -9.865  1.00 47.88  ? 51  MET   A CB  1 
ATOM   14   C CG  . MET   A 1 8   ? -20.669 14.822  -9.418  1.00 52.69  ? 51  MET   A CG  1 
ATOM   15   S SD  . MET   A 1 8   ? -19.890 13.227  -9.160  1.00 57.28  ? 51  MET   A SD  1 
ATOM   16   C CE  . MET   A 1 8   ? -18.197 13.777  -8.986  1.00 55.70  ? 51  MET   A CE  1 
ATOM   17   N N   . TYR   A 1 9   ? -24.375 15.657  -11.941 1.00 36.26  ? 52  TYR   A N   1 
ATOM   18   C CA  . TYR   A 1 9   ? -25.682 15.358  -12.577 1.00 41.50  ? 52  TYR   A CA  1 
ATOM   19   C C   . TYR   A 1 9   ? -25.469 14.384  -13.735 1.00 35.69  ? 52  TYR   A C   1 
ATOM   20   O O   . TYR   A 1 9   ? -24.351 14.321  -14.243 1.00 41.47  ? 52  TYR   A O   1 
ATOM   21   C CB  . TYR   A 1 9   ? -26.394 16.647  -13.030 1.00 42.85  ? 52  TYR   A CB  1 
ATOM   22   C CG  . TYR   A 1 9   ? -25.664 17.446  -14.078 1.00 42.92  ? 52  TYR   A CG  1 
ATOM   23   C CD1 . TYR   A 1 9   ? -24.624 18.300  -13.733 1.00 44.51  ? 52  TYR   A CD1 1 
ATOM   24   C CD2 . TYR   A 1 9   ? -25.993 17.321  -15.418 1.00 43.32  ? 52  TYR   A CD2 1 
ATOM   25   C CE1 . TYR   A 1 9   ? -23.942 19.028  -14.694 1.00 50.73  ? 52  TYR   A CE1 1 
ATOM   26   C CE2 . TYR   A 1 9   ? -25.321 18.050  -16.391 1.00 49.08  ? 52  TYR   A CE2 1 
ATOM   27   C CZ  . TYR   A 1 9   ? -24.290 18.898  -16.030 1.00 48.49  ? 52  TYR   A CZ  1 
ATOM   28   O OH  . TYR   A 1 9   ? -23.610 19.587  -16.999 1.00 56.45  ? 52  TYR   A OH  1 
ATOM   29   N N   . ILE   A 1 10  ? -26.514 13.619  -14.077 1.00 43.01  ? 53  ILE   A N   1 
ATOM   30   C CA  . ILE   A 1 10  ? -26.491 12.601  -15.169 1.00 42.81  ? 53  ILE   A CA  1 
ATOM   31   C C   . ILE   A 1 10  ? -27.325 13.118  -16.363 1.00 48.89  ? 53  ILE   A C   1 
ATOM   32   O O   . ILE   A 1 10  ? -28.349 13.789  -16.135 1.00 45.41  ? 53  ILE   A O   1 
ATOM   33   C CB  . ILE   A 1 10  ? -26.972 11.225  -14.655 1.00 41.92  ? 53  ILE   A CB  1 
ATOM   34   C CG1 . ILE   A 1 10  ? -28.456 11.203  -14.317 1.00 43.48  ? 53  ILE   A CG1 1 
ATOM   35   C CG2 . ILE   A 1 10  ? -26.150 10.755  -13.461 1.00 43.20  ? 53  ILE   A CG2 1 
ATOM   36   C CD1 . ILE   A 1 10  ? -28.923 9.884   -13.780 1.00 44.65  ? 53  ILE   A CD1 1 
ATOM   37   N N   . GLU   A 1 11  ? -26.888 12.825  -17.589 1.00 45.49  ? 54  GLU   A N   1 
ATOM   38   C CA  . GLU   A 1 11  ? -27.585 13.149  -18.867 1.00 48.49  ? 54  GLU   A CA  1 
ATOM   39   C C   . GLU   A 1 11  ? -27.588 11.873  -19.725 1.00 47.51  ? 54  GLU   A C   1 
ATOM   40   O O   . GLU   A 1 11  ? -26.514 11.251  -19.867 1.00 41.66  ? 54  GLU   A O   1 
ATOM   41   C CB  . GLU   A 1 11  ? -26.887 14.235  -19.706 1.00 51.81  ? 54  GLU   A CB  1 
ATOM   42   C CG  . GLU   A 1 11  ? -26.337 15.439  -18.971 1.00 60.27  ? 54  GLU   A CG  1 
ATOM   43   C CD  . GLU   A 1 11  ? -25.627 16.463  -19.864 1.00 71.04  ? 54  GLU   A CD  1 
ATOM   44   O OE1 . GLU   A 1 11  ? -24.828 16.046  -20.726 1.00 71.57  ? 54  GLU   A OE1 1 
ATOM   45   O OE2 . GLU   A 1 11  ? -25.866 17.694  -19.702 1.00 76.96  ? 54  GLU   A OE2 1 
ATOM   46   N N   . ARG   A 1 12  ? -28.729 11.454  -20.259 1.00 42.07  ? 55  ARG   A N   1 
ATOM   47   C CA  . ARG   A 1 12  ? -28.785 10.214  -21.085 1.00 48.99  ? 55  ARG   A CA  1 
ATOM   48   C C   . ARG   A 1 12  ? -27.794 10.303  -22.254 1.00 49.46  ? 55  ARG   A C   1 
ATOM   49   O O   . ARG   A 1 12  ? -27.503 11.422  -22.677 1.00 54.04  ? 55  ARG   A O   1 
ATOM   50   C CB  . ARG   A 1 12  ? -30.206 9.996   -21.577 1.00 47.68  ? 55  ARG   A CB  1 
ATOM   51   C CG  . ARG   A 1 12  ? -30.457 8.578   -22.032 1.00 49.81  ? 55  ARG   A CG  1 
ATOM   52   C CD  . ARG   A 1 12  ? -31.904 8.218   -21.884 1.00 53.77  ? 55  ARG   A CD  1 
ATOM   53   N NE  . ARG   A 1 12  ? -32.197 6.817   -22.106 1.00 55.81  ? 55  ARG   A NE  1 
ATOM   54   C CZ  . ARG   A 1 12  ? -32.105 6.242   -23.293 1.00 56.65  ? 55  ARG   A CZ  1 
ATOM   55   N NH1 . ARG   A 1 12  ? -31.675 6.940   -24.337 1.00 55.14  ? 55  ARG   A NH1 1 
ATOM   56   N NH2 . ARG   A 1 12  ? -32.403 4.959   -23.424 1.00 54.40  ? 55  ARG   A NH2 1 
ATOM   57   N N   . ALA   A 1 13  ? -27.245 9.177   -22.731 1.00 52.10  ? 56  ALA   A N   1 
ATOM   58   C CA  . ALA   A 1 13  ? -26.275 9.136   -23.860 1.00 42.07  ? 56  ALA   A CA  1 
ATOM   59   C C   . ALA   A 1 13  ? -26.627 8.086   -24.920 1.00 40.59  ? 56  ALA   A C   1 
ATOM   60   O O   . ALA   A 1 13  ? -26.006 8.124   -25.995 1.00 42.89  ? 56  ALA   A O   1 
ATOM   61   C CB  . ALA   A 1 13  ? -24.857 8.939   -23.382 1.00 51.60  ? 56  ALA   A CB  1 
ATOM   62   N N   . GLY   A 1 14  ? -27.558 7.176   -24.663 1.00 35.26  ? 57  GLY   A N   1 
ATOM   63   C CA  . GLY   A 1 14  ? -27.910 6.129   -25.624 1.00 31.12  ? 57  GLY   A CA  1 
ATOM   64   C C   . GLY   A 1 14  ? -28.640 5.008   -24.945 1.00 39.27  ? 57  GLY   A C   1 
ATOM   65   O O   . GLY   A 1 14  ? -28.707 5.033   -23.667 1.00 37.83  ? 57  GLY   A O   1 
ATOM   66   N N   . ASP   A 1 15  ? -29.228 4.137   -25.773 1.00 39.92  ? 58  ASP   A N   1 
ATOM   67   C CA  . ASP   A 1 15  ? -29.725 2.781   -25.453 1.00 43.78  ? 58  ASP   A CA  1 
ATOM   68   C C   . ASP   A 1 15  ? -28.505 1.888   -25.231 1.00 47.19  ? 58  ASP   A C   1 
ATOM   69   O O   . ASP   A 1 15  ? -27.399 2.317   -25.646 1.00 49.93  ? 58  ASP   A O   1 
ATOM   70   C CB  . ASP   A 1 15  ? -30.546 2.167   -26.591 1.00 50.46  ? 58  ASP   A CB  1 
ATOM   71   C CG  . ASP   A 1 15  ? -31.900 2.832   -26.769 1.00 62.16  ? 58  ASP   A CG  1 
ATOM   72   O OD1 . ASP   A 1 15  ? -32.066 3.876   -26.128 1.00 45.88  ? 58  ASP   A OD1 1 
ATOM   73   O OD2 . ASP   A 1 15  ? -32.791 2.278   -27.520 1.00 56.01  ? 58  ASP   A OD2 1 
ATOM   74   N N   . ILE   A 1 16  ? -28.708 0.742   -24.573 1.00 51.52  ? 59  ILE   A N   1 
ATOM   75   C CA  . ILE   A 1 16  ? -27.670 -0.325  -24.399 1.00 53.36  ? 59  ILE   A CA  1 
ATOM   76   C C   . ILE   A 1 16  ? -28.085 -1.480  -25.324 1.00 45.25  ? 59  ILE   A C   1 
ATOM   77   O O   . ILE   A 1 16  ? -29.016 -2.222  -25.020 1.00 52.07  ? 59  ILE   A O   1 
ATOM   78   C CB  . ILE   A 1 16  ? -27.483 -0.684  -22.911 1.00 52.94  ? 59  ILE   A CB  1 
ATOM   79   C CG1 . ILE   A 1 16  ? -26.855 0.500   -22.169 1.00 52.64  ? 59  ILE   A CG1 1 
ATOM   80   C CG2 . ILE   A 1 16  ? -26.626 -1.927  -22.772 1.00 56.24  ? 59  ILE   A CG2 1 
ATOM   81   C CD1 . ILE   A 1 16  ? -27.018 0.458   -20.676 1.00 58.24  ? 59  ILE   A CD1 1 
ATOM   82   N N   A THR   A 1 17  ? -27.410 -1.565  -26.471 0.25 48.09  ? 60  THR   A N   1 
ATOM   83   N N   B THR   A 1 17  ? -27.408 -1.592  -26.463 0.25 48.94  ? 60  THR   A N   1 
ATOM   84   N N   C THR   A 1 17  ? -27.410 -1.565  -26.471 0.25 48.09  ? 60  THR   A N   1 
ATOM   85   N N   D THR   A 1 17  ? -27.408 -1.592  -26.463 0.25 48.94  ? 60  THR   A N   1 
ATOM   86   C CA  A THR   A 1 17  ? -27.725 -2.476  -27.606 0.25 49.59  ? 60  THR   A CA  1 
ATOM   87   C CA  B THR   A 1 17  ? -27.757 -2.521  -27.570 0.25 51.36  ? 60  THR   A CA  1 
ATOM   88   C CA  C THR   A 1 17  ? -27.725 -2.476  -27.606 0.25 49.59  ? 60  THR   A CA  1 
ATOM   89   C CA  D THR   A 1 17  ? -27.757 -2.521  -27.570 0.25 51.36  ? 60  THR   A CA  1 
ATOM   90   C C   A THR   A 1 17  ? -26.426 -2.966  -28.256 0.25 48.31  ? 60  THR   A C   1 
ATOM   91   C C   B THR   A 1 17  ? -26.471 -2.955  -28.287 0.25 49.47  ? 60  THR   A C   1 
ATOM   92   C C   C THR   A 1 17  ? -26.426 -2.966  -28.256 0.25 48.31  ? 60  THR   A C   1 
ATOM   93   C C   D THR   A 1 17  ? -26.471 -2.955  -28.287 0.25 49.47  ? 60  THR   A C   1 
ATOM   94   O O   A THR   A 1 17  ? -25.449 -2.171  -28.333 0.25 46.22  ? 60  THR   A O   1 
ATOM   95   O O   B THR   A 1 17  ? -25.533 -2.121  -28.407 0.25 47.85  ? 60  THR   A O   1 
ATOM   96   O O   C THR   A 1 17  ? -25.449 -2.171  -28.333 0.25 46.22  ? 60  THR   A O   1 
ATOM   97   O O   D THR   A 1 17  ? -25.533 -2.121  -28.407 0.25 47.85  ? 60  THR   A O   1 
ATOM   98   C CB  A THR   A 1 17  ? -28.584 -1.785  -28.675 0.25 49.05  ? 60  THR   A CB  1 
ATOM   99   C CB  B THR   A 1 17  ? -28.788 -1.876  -28.512 0.25 52.11  ? 60  THR   A CB  1 
ATOM   100  C CB  C THR   A 1 17  ? -28.584 -1.785  -28.675 0.25 49.05  ? 60  THR   A CB  1 
ATOM   101  C CB  D THR   A 1 17  ? -28.788 -1.876  -28.512 0.25 52.11  ? 60  THR   A CB  1 
ATOM   102  O OG1 A THR   A 1 17  ? -27.770 -0.850  -29.385 0.25 47.25  ? 60  THR   A OG1 1 
ATOM   103  O OG1 B THR   A 1 17  ? -30.060 -1.897  -27.861 0.25 55.43  ? 60  THR   A OG1 1 
ATOM   104  O OG1 C THR   A 1 17  ? -27.770 -0.850  -29.385 0.25 47.25  ? 60  THR   A OG1 1 
ATOM   105  O OG1 D THR   A 1 17  ? -30.060 -1.897  -27.861 0.25 55.43  ? 60  THR   A OG1 1 
ATOM   106  C CG2 A THR   A 1 17  ? -29.791 -1.082  -28.094 0.25 49.45  ? 60  THR   A CG2 1 
ATOM   107  C CG2 B THR   A 1 17  ? -28.911 -2.577  -29.847 0.25 50.85  ? 60  THR   A CG2 1 
ATOM   108  C CG2 C THR   A 1 17  ? -29.791 -1.082  -28.094 0.25 49.45  ? 60  THR   A CG2 1 
ATOM   109  C CG2 D THR   A 1 17  ? -28.911 -2.577  -29.847 0.25 50.85  ? 60  THR   A CG2 1 
ATOM   110  N N   . TRP   A 1 18  ? -26.424 -4.226  -28.702 1.00 51.60  ? 61  TRP   A N   1 
ATOM   111  C CA  . TRP   A 1 18  ? -25.346 -4.777  -29.560 1.00 58.21  ? 61  TRP   A CA  1 
ATOM   112  C C   . TRP   A 1 18  ? -25.598 -4.272  -30.981 1.00 58.69  ? 61  TRP   A C   1 
ATOM   113  O O   . TRP   A 1 18  ? -26.685 -4.566  -31.493 1.00 62.08  ? 61  TRP   A O   1 
ATOM   114  C CB  . TRP   A 1 18  ? -25.373 -6.308  -29.519 1.00 64.97  ? 61  TRP   A CB  1 
ATOM   115  C CG  . TRP   A 1 18  ? -24.268 -6.951  -30.303 1.00 73.45  ? 61  TRP   A CG  1 
ATOM   116  C CD1 . TRP   A 1 18  ? -24.236 -7.172  -31.649 1.00 75.33  ? 61  TRP   A CD1 1 
ATOM   117  C CD2 . TRP   A 1 18  ? -23.025 -7.459  -29.787 1.00 76.39  ? 61  TRP   A CD2 1 
ATOM   118  N NE1 . TRP   A 1 18  ? -23.054 -7.758  -32.004 1.00 74.32  ? 61  TRP   A NE1 1 
ATOM   119  C CE2 . TRP   A 1 18  ? -22.301 -7.967  -30.883 1.00 75.66  ? 61  TRP   A CE2 1 
ATOM   120  C CE3 . TRP   A 1 18  ? -22.450 -7.534  -28.513 1.00 73.87  ? 61  TRP   A CE3 1 
ATOM   121  C CZ2 . TRP   A 1 18  ? -21.039 -8.540  -30.738 1.00 75.15  ? 61  TRP   A CZ2 1 
ATOM   122  C CZ3 . TRP   A 1 18  ? -21.208 -8.108  -28.369 1.00 70.46  ? 61  TRP   A CZ3 1 
ATOM   123  C CH2 . TRP   A 1 18  ? -20.508 -8.596  -29.469 1.00 73.17  ? 61  TRP   A CH2 1 
ATOM   124  N N   . GLU   A 1 19  ? -24.632 -3.580  -31.586 1.00 58.01  ? 62  GLU   A N   1 
ATOM   125  C CA  . GLU   A 1 19  ? -24.712 -3.073  -32.978 1.00 68.54  ? 62  GLU   A CA  1 
ATOM   126  C C   . GLU   A 1 19  ? -23.888 -3.978  -33.912 1.00 70.81  ? 62  GLU   A C   1 
ATOM   127  O O   . GLU   A 1 19  ? -22.639 -3.885  -33.869 1.00 63.29  ? 62  GLU   A O   1 
ATOM   128  C CB  . GLU   A 1 19  ? -24.243 -1.615  -33.007 1.00 78.49  ? 62  GLU   A CB  1 
ATOM   129  C CG  . GLU   A 1 19  ? -25.120 -0.672  -32.165 1.00 99.45  ? 62  GLU   A CG  1 
ATOM   130  C CD  . GLU   A 1 19  ? -26.599 -0.537  -32.544 1.00 105.31 ? 62  GLU   A CD  1 
ATOM   131  O OE1 . GLU   A 1 19  ? -26.910 -0.436  -33.760 1.00 106.05 ? 62  GLU   A OE1 1 
ATOM   132  O OE2 . GLU   A 1 19  ? -27.449 -0.523  -31.623 1.00 96.84  ? 62  GLU   A OE2 1 
ATOM   133  N N   . LYS   A 1 20  ? -24.560 -4.795  -34.742 1.00 67.89  ? 63  LYS   A N   1 
ATOM   134  C CA  . LYS   A 1 20  ? -23.919 -5.627  -35.803 1.00 67.30  ? 63  LYS   A CA  1 
ATOM   135  C C   . LYS   A 1 20  ? -22.964 -4.763  -36.626 1.00 69.54  ? 63  LYS   A C   1 
ATOM   136  O O   . LYS   A 1 20  ? -23.276 -3.593  -36.883 1.00 73.70  ? 63  LYS   A O   1 
ATOM   137  C CB  . LYS   A 1 20  ? -24.978 -6.285  -36.686 1.00 76.97  ? 63  LYS   A CB  1 
ATOM   138  C CG  . LYS   A 1 20  ? -25.543 -7.567  -36.090 1.00 86.54  ? 63  LYS   A CG  1 
ATOM   139  C CD  . LYS   A 1 20  ? -26.980 -7.866  -36.458 1.00 89.99  ? 63  LYS   A CD  1 
ATOM   140  C CE  . LYS   A 1 20  ? -27.325 -9.328  -36.265 1.00 95.02  ? 63  LYS   A CE  1 
ATOM   141  N NZ  . LYS   A 1 20  ? -28.725 -9.620  -36.654 1.00 94.15  ? 63  LYS   A NZ  1 
ATOM   142  N N   . ASP   A 1 21  ? -21.806 -5.315  -36.968 1.00 78.80  ? 64  ASP   A N   1 
ATOM   143  C CA  . ASP   A 1 21  ? -20.762 -4.659  -37.807 1.00 85.97  ? 64  ASP   A CA  1 
ATOM   144  C C   . ASP   A 1 21  ? -20.309 -3.333  -37.167 1.00 79.56  ? 64  ASP   A C   1 
ATOM   145  O O   . ASP   A 1 21  ? -20.397 -2.278  -37.821 1.00 74.39  ? 64  ASP   A O   1 
ATOM   146  C CB  . ASP   A 1 21  ? -21.222 -4.482  -39.267 1.00 103.19 ? 64  ASP   A CB  1 
ATOM   147  C CG  . ASP   A 1 21  ? -21.411 -5.776  -40.055 1.00 104.05 ? 64  ASP   A CG  1 
ATOM   148  O OD1 . ASP   A 1 21  ? -20.395 -6.316  -40.560 1.00 100.97 ? 64  ASP   A OD1 1 
ATOM   149  O OD2 . ASP   A 1 21  ? -22.575 -6.241  -40.154 1.00 101.11 ? 64  ASP   A OD2 1 
ATOM   150  N N   A ALA   A 1 22  ? -19.831 -3.400  -35.918 0.25 75.88  ? 65  ALA   A N   1 
ATOM   151  N N   B ALA   A 1 22  ? -19.831 -3.400  -35.918 0.25 75.88  ? 65  ALA   A N   1 
ATOM   152  N N   C ALA   A 1 22  ? -19.832 -3.399  -35.918 0.25 75.84  ? 65  ALA   A N   1 
ATOM   153  N N   D ALA   A 1 22  ? -19.832 -3.399  -35.918 0.25 75.84  ? 65  ALA   A N   1 
ATOM   154  C CA  A ALA   A 1 22  ? -19.158 -2.294  -35.196 0.25 70.20  ? 65  ALA   A CA  1 
ATOM   155  C CA  B ALA   A 1 22  ? -19.158 -2.294  -35.196 0.25 70.20  ? 65  ALA   A CA  1 
ATOM   156  C CA  C ALA   A 1 22  ? -19.158 -2.292  -35.197 0.25 70.11  ? 65  ALA   A CA  1 
ATOM   157  C CA  D ALA   A 1 22  ? -19.158 -2.292  -35.197 0.25 70.11  ? 65  ALA   A CA  1 
ATOM   158  C C   A ALA   A 1 22  ? -17.642 -2.404  -35.396 0.25 65.48  ? 65  ALA   A C   1 
ATOM   159  C C   B ALA   A 1 22  ? -17.642 -2.404  -35.396 0.25 65.48  ? 65  ALA   A C   1 
ATOM   160  C C   C ALA   A 1 22  ? -17.643 -2.414  -35.400 0.25 65.29  ? 65  ALA   A C   1 
ATOM   161  C C   D ALA   A 1 22  ? -17.643 -2.414  -35.400 0.25 65.29  ? 65  ALA   A C   1 
ATOM   162  O O   A ALA   A 1 22  ? -17.162 -3.514  -35.692 0.25 65.14  ? 65  ALA   A O   1 
ATOM   163  O O   B ALA   A 1 22  ? -17.162 -3.514  -35.692 0.25 65.14  ? 65  ALA   A O   1 
ATOM   164  O O   C ALA   A 1 22  ? -17.180 -3.533  -35.690 0.25 65.05  ? 65  ALA   A O   1 
ATOM   165  O O   D ALA   A 1 22  ? -17.180 -3.533  -35.690 0.25 65.05  ? 65  ALA   A O   1 
ATOM   166  C CB  A ALA   A 1 22  ? -19.528 -2.335  -33.733 0.25 72.26  ? 65  ALA   A CB  1 
ATOM   167  C CB  B ALA   A 1 22  ? -19.528 -2.335  -33.733 0.25 72.26  ? 65  ALA   A CB  1 
ATOM   168  C CB  C ALA   A 1 22  ? -19.529 -2.330  -33.735 0.25 72.22  ? 65  ALA   A CB  1 
ATOM   169  C CB  D ALA   A 1 22  ? -19.529 -2.330  -33.735 0.25 72.22  ? 65  ALA   A CB  1 
ATOM   170  N N   A GLU   A 1 23  ? -16.925 -1.286  -35.243 0.25 68.38  ? 66  GLU   A N   1 
ATOM   171  N N   B GLU   A 1 23  ? -16.925 -1.286  -35.243 0.25 68.38  ? 66  GLU   A N   1 
ATOM   172  N N   C GLU   A 1 23  ? -16.904 -1.309  -35.273 0.25 67.53  ? 66  GLU   A N   1 
ATOM   173  N N   D GLU   A 1 23  ? -16.904 -1.309  -35.273 0.25 67.53  ? 66  GLU   A N   1 
ATOM   174  C CA  A GLU   A 1 23  ? -15.446 -1.190  -35.379 0.25 71.62  ? 66  GLU   A CA  1 
ATOM   175  C CA  B GLU   A 1 23  ? -15.446 -1.190  -35.379 0.25 71.62  ? 66  GLU   A CA  1 
ATOM   176  C CA  C GLU   A 1 23  ? -15.419 -1.281  -35.385 0.25 70.38  ? 66  GLU   A CA  1 
ATOM   177  C CA  D GLU   A 1 23  ? -15.419 -1.281  -35.385 0.25 70.38  ? 66  GLU   A CA  1 
ATOM   178  C C   A GLU   A 1 23  ? -14.786 -2.204  -34.434 0.25 73.40  ? 66  GLU   A C   1 
ATOM   179  C C   B GLU   A 1 23  ? -14.786 -2.204  -34.434 0.25 73.40  ? 66  GLU   A C   1 
ATOM   180  C C   C GLU   A 1 23  ? -14.831 -2.339  -34.442 0.25 72.06  ? 66  GLU   A C   1 
ATOM   181  C C   D GLU   A 1 23  ? -14.831 -2.339  -34.442 0.25 72.06  ? 66  GLU   A C   1 
ATOM   182  O O   A GLU   A 1 23  ? -14.801 -1.971  -33.207 0.25 71.88  ? 66  GLU   A O   1 
ATOM   183  O O   B GLU   A 1 23  ? -14.801 -1.971  -33.207 0.25 71.88  ? 66  GLU   A O   1 
ATOM   184  O O   C GLU   A 1 23  ? -14.943 -2.163  -33.211 0.25 70.02  ? 66  GLU   A O   1 
ATOM   185  O O   D GLU   A 1 23  ? -14.943 -2.163  -33.211 0.25 70.02  ? 66  GLU   A O   1 
ATOM   186  C CB  A GLU   A 1 23  ? -14.987 0.240   -35.082 0.25 76.30  ? 66  GLU   A CB  1 
ATOM   187  C CB  B GLU   A 1 23  ? -14.987 0.240   -35.082 0.25 76.30  ? 66  GLU   A CB  1 
ATOM   188  C CB  C GLU   A 1 23  ? -14.885 0.115   -35.056 0.25 74.68  ? 66  GLU   A CB  1 
ATOM   189  C CB  D GLU   A 1 23  ? -14.885 0.115   -35.056 0.25 74.68  ? 66  GLU   A CB  1 
ATOM   190  C CG  A GLU   A 1 23  ? -13.493 0.464   -35.268 0.25 79.93  ? 66  GLU   A CG  1 
ATOM   191  C CG  B GLU   A 1 23  ? -13.493 0.464   -35.268 0.25 79.93  ? 66  GLU   A CG  1 
ATOM   192  C CG  C GLU   A 1 23  ? -13.394 0.150   -34.752 0.25 77.19  ? 66  GLU   A CG  1 
ATOM   193  C CG  D GLU   A 1 23  ? -13.394 0.150   -34.752 0.25 77.19  ? 66  GLU   A CG  1 
ATOM   194  C CD  A GLU   A 1 23  ? -13.040 1.919   -35.133 0.25 82.52  ? 66  GLU   A CD  1 
ATOM   195  C CD  B GLU   A 1 23  ? -13.040 1.919   -35.133 0.25 82.52  ? 66  GLU   A CD  1 
ATOM   196  C CD  C GLU   A 1 23  ? -12.886 1.474   -34.201 0.25 79.59  ? 66  GLU   A CD  1 
ATOM   197  C CD  D GLU   A 1 23  ? -12.886 1.474   -34.201 0.25 79.59  ? 66  GLU   A CD  1 
ATOM   198  O OE1 A GLU   A 1 23  ? -13.671 2.650   -34.318 0.25 81.62  ? 66  GLU   A OE1 1 
ATOM   199  O OE1 B GLU   A 1 23  ? -13.671 2.650   -34.318 0.25 81.62  ? 66  GLU   A OE1 1 
ATOM   200  O OE1 C GLU   A 1 23  ? -13.684 2.438   -34.134 0.25 80.47  ? 66  GLU   A OE1 1 
ATOM   201  O OE1 D GLU   A 1 23  ? -13.684 2.438   -34.134 0.25 80.47  ? 66  GLU   A OE1 1 
ATOM   202  O OE2 A GLU   A 1 23  ? -12.057 2.324   -35.783 0.25 82.90  ? 66  GLU   A OE2 1 
ATOM   203  O OE2 B GLU   A 1 23  ? -12.057 2.324   -35.783 0.25 82.90  ? 66  GLU   A OE2 1 
ATOM   204  O OE2 C GLU   A 1 23  ? -11.693 1.543   -33.834 0.25 79.93  ? 66  GLU   A OE2 1 
ATOM   205  O OE2 D GLU   A 1 23  ? -11.693 1.543   -33.834 0.25 79.93  ? 66  GLU   A OE2 1 
ATOM   206  N N   A VAL   A 1 24  ? -14.238 -3.289  -34.993 0.25 72.90  ? 67  VAL   A N   1 
ATOM   207  N N   B VAL   A 1 24  ? -14.238 -3.289  -34.993 0.25 72.90  ? 67  VAL   A N   1 
ATOM   208  N N   C VAL   A 1 24  ? -14.245 -3.402  -35.003 0.25 72.06  ? 67  VAL   A N   1 
ATOM   209  N N   D VAL   A 1 24  ? -14.245 -3.402  -35.003 0.25 72.06  ? 67  VAL   A N   1 
ATOM   210  C CA  A VAL   A 1 24  ? -13.557 -4.395  -34.252 0.25 70.24  ? 67  VAL   A CA  1 
ATOM   211  C CA  B VAL   A 1 24  ? -13.557 -4.395  -34.252 0.25 70.24  ? 67  VAL   A CA  1 
ATOM   212  C CA  C VAL   A 1 24  ? -13.542 -4.481  -34.245 0.25 69.50  ? 67  VAL   A CA  1 
ATOM   213  C CA  D VAL   A 1 24  ? -13.542 -4.481  -34.245 0.25 69.50  ? 67  VAL   A CA  1 
ATOM   214  C C   A VAL   A 1 24  ? -12.077 -4.038  -34.067 0.25 70.36  ? 67  VAL   A C   1 
ATOM   215  C C   B VAL   A 1 24  ? -12.077 -4.038  -34.067 0.25 70.36  ? 67  VAL   A C   1 
ATOM   216  C C   C VAL   A 1 24  ? -12.070 -4.083  -34.070 0.25 69.97  ? 67  VAL   A C   1 
ATOM   217  C C   D VAL   A 1 24  ? -12.070 -4.083  -34.070 0.25 69.97  ? 67  VAL   A C   1 
ATOM   218  O O   A VAL   A 1 24  ? -11.425 -3.696  -35.069 0.25 69.78  ? 67  VAL   A O   1 
ATOM   219  O O   B VAL   A 1 24  ? -11.425 -3.696  -35.069 0.25 69.78  ? 67  VAL   A O   1 
ATOM   220  O O   C VAL   A 1 24  ? -11.423 -3.756  -35.079 0.25 69.50  ? 67  VAL   A O   1 
ATOM   221  O O   D VAL   A 1 24  ? -11.423 -3.756  -35.079 0.25 69.50  ? 67  VAL   A O   1 
ATOM   222  C CB  A VAL   A 1 24  ? -13.714 -5.740  -34.985 0.25 66.94  ? 67  VAL   A CB  1 
ATOM   223  C CB  B VAL   A 1 24  ? -13.714 -5.740  -34.985 0.25 66.94  ? 67  VAL   A CB  1 
ATOM   224  C CB  C VAL   A 1 24  ? -13.666 -5.849  -34.938 0.25 66.55  ? 67  VAL   A CB  1 
ATOM   225  C CB  D VAL   A 1 24  ? -13.666 -5.849  -34.938 0.25 66.55  ? 67  VAL   A CB  1 
ATOM   226  C CG1 A VAL   A 1 24  ? -13.034 -6.862  -34.226 0.25 65.49  ? 67  VAL   A CG1 1 
ATOM   227  C CG1 B VAL   A 1 24  ? -13.034 -6.862  -34.226 0.25 65.49  ? 67  VAL   A CG1 1 
ATOM   228  C CG1 C VAL   A 1 24  ? -12.957 -6.921  -34.138 0.25 65.18  ? 67  VAL   A CG1 1 
ATOM   229  C CG1 D VAL   A 1 24  ? -12.957 -6.921  -34.138 0.25 65.18  ? 67  VAL   A CG1 1 
ATOM   230  C CG2 A VAL   A 1 24  ? -15.174 -6.079  -35.248 0.25 66.17  ? 67  VAL   A CG2 1 
ATOM   231  C CG2 B VAL   A 1 24  ? -15.174 -6.079  -35.248 0.25 66.17  ? 67  VAL   A CG2 1 
ATOM   232  C CG2 C VAL   A 1 24  ? -15.114 -6.241  -35.187 0.25 65.96  ? 67  VAL   A CG2 1 
ATOM   233  C CG2 D VAL   A 1 24  ? -15.114 -6.241  -35.187 0.25 65.96  ? 67  VAL   A CG2 1 
ATOM   234  N N   . THR   A 1 25  ? -11.566 -4.116  -32.834 1.00 70.26  ? 68  THR   A N   1 
ATOM   235  C CA  . THR   A 1 25  ? -10.188 -3.663  -32.507 1.00 64.26  ? 68  THR   A CA  1 
ATOM   236  C C   . THR   A 1 25  ? -9.767  -4.128  -31.109 1.00 60.90  ? 68  THR   A C   1 
ATOM   237  O O   . THR   A 1 25  ? -10.555 -4.833  -30.445 1.00 51.48  ? 68  THR   A O   1 
ATOM   238  C CB  . THR   A 1 25  ? -10.089 -2.144  -32.663 1.00 68.84  ? 68  THR   A CB  1 
ATOM   239  O OG1 . THR   A 1 25  ? -8.719  -1.794  -32.521 1.00 73.81  ? 68  THR   A OG1 1 
ATOM   240  C CG2 . THR   A 1 25  ? -10.933 -1.382  -31.665 1.00 75.23  ? 68  THR   A CG2 1 
ATOM   241  N N   . GLY   A 1 26  ? -8.537  -3.777  -30.723 1.00 60.58  ? 69  GLY   A N   1 
ATOM   242  C CA  . GLY   A 1 26  ? -7.887  -4.205  -29.473 1.00 63.38  ? 69  GLY   A CA  1 
ATOM   243  C C   . GLY   A 1 26  ? -7.537  -5.690  -29.437 1.00 58.91  ? 69  GLY   A C   1 
ATOM   244  O O   . GLY   A 1 26  ? -8.268  -6.512  -30.028 1.00 64.77  ? 69  GLY   A O   1 
ATOM   245  N N   . ASN   A 1 27  ? -6.503  -6.019  -28.664 1.00 59.61  ? 70  ASN   A N   1 
ATOM   246  C CA  . ASN   A 1 27  ? -5.962  -7.390  -28.451 1.00 62.69  ? 70  ASN   A CA  1 
ATOM   247  C C   . ASN   A 1 27  ? -6.556  -8.048  -27.177 1.00 62.13  ? 70  ASN   A C   1 
ATOM   248  O O   . ASN   A 1 27  ? -7.534  -7.494  -26.597 1.00 51.88  ? 70  ASN   A O   1 
ATOM   249  C CB  . ASN   A 1 27  ? -4.437  -7.295  -28.445 1.00 65.64  ? 70  ASN   A CB  1 
ATOM   250  C CG  . ASN   A 1 27  ? -3.916  -6.459  -27.300 1.00 68.09  ? 70  ASN   A CG  1 
ATOM   251  O OD1 . ASN   A 1 27  ? -4.243  -5.281  -27.196 1.00 80.10  ? 70  ASN   A OD1 1 
ATOM   252  N ND2 . ASN   A 1 27  ? -3.116  -7.056  -26.436 1.00 80.11  ? 70  ASN   A ND2 1 
ATOM   253  N N   . SER   A 1 28  ? -6.015  -9.209  -26.774 1.00 45.05  ? 71  SER   A N   1 
ATOM   254  C CA  . SER   A 1 28  ? -6.490  -10.080 -25.668 1.00 47.53  ? 71  SER   A CA  1 
ATOM   255  C C   . SER   A 1 28  ? -5.359  -10.486 -24.740 1.00 49.92  ? 71  SER   A C   1 
ATOM   256  O O   . SER   A 1 28  ? -5.159  -11.674 -24.542 1.00 49.95  ? 71  SER   A O   1 
ATOM   257  C CB  . SER   A 1 28  ? -7.160  -11.319 -26.189 1.00 44.01  ? 71  SER   A CB  1 
ATOM   258  O OG  . SER   A 1 28  ? -7.962  -11.004 -27.309 1.00 51.70  ? 71  SER   A OG  1 
ATOM   259  N N   . PRO   A 1 29  ? -4.663  -9.540  -24.076 1.00 56.08  ? 72  PRO   A N   1 
ATOM   260  C CA  . PRO   A 1 29  ? -3.506  -9.879  -23.255 1.00 58.70  ? 72  PRO   A CA  1 
ATOM   261  C C   . PRO   A 1 29  ? -3.903  -10.634 -21.984 1.00 67.59  ? 72  PRO   A C   1 
ATOM   262  O O   . PRO   A 1 29  ? -4.863  -10.233 -21.350 1.00 69.16  ? 72  PRO   A O   1 
ATOM   263  C CB  . PRO   A 1 29  ? -2.904  -8.518  -22.876 1.00 64.94  ? 72  PRO   A CB  1 
ATOM   264  C CG  . PRO   A 1 29  ? -4.084  -7.555  -22.921 1.00 63.07  ? 72  PRO   A CG  1 
ATOM   265  C CD  . PRO   A 1 29  ? -5.012  -8.113  -23.987 1.00 57.85  ? 72  PRO   A CD  1 
ATOM   266  N N   . ARG   A 1 30  ? -3.158  -11.693 -21.662 1.00 64.73  ? 73  ARG   A N   1 
ATOM   267  C CA  . ARG   A 1 30  ? -3.251  -12.441 -20.381 1.00 68.28  ? 73  ARG   A CA  1 
ATOM   268  C C   . ARG   A 1 30  ? -2.236  -11.832 -19.408 1.00 64.83  ? 73  ARG   A C   1 
ATOM   269  O O   . ARG   A 1 30  ? -1.045  -11.891 -19.707 1.00 54.49  ? 73  ARG   A O   1 
ATOM   270  C CB  . ARG   A 1 30  ? -3.042  -13.925 -20.672 1.00 71.73  ? 73  ARG   A CB  1 
ATOM   271  C CG  . ARG   A 1 30  ? -4.107  -14.488 -21.604 1.00 80.67  ? 73  ARG   A CG  1 
ATOM   272  C CD  . ARG   A 1 30  ? -3.687  -15.782 -22.279 1.00 91.21  ? 73  ARG   A CD  1 
ATOM   273  N NE  . ARG   A 1 30  ? -4.749  -16.392 -23.084 1.00 100.84 ? 73  ARG   A NE  1 
ATOM   274  C CZ  . ARG   A 1 30  ? -5.804  -17.064 -22.603 1.00 100.39 ? 73  ARG   A CZ  1 
ATOM   275  N NH1 . ARG   A 1 30  ? -5.978  -17.214 -21.298 1.00 111.51 ? 73  ARG   A NH1 1 
ATOM   276  N NH2 . ARG   A 1 30  ? -6.700  -17.575 -23.432 1.00 83.86  ? 73  ARG   A NH2 1 
ATOM   277  N N   . LEU   A 1 31  ? -2.702  -11.185 -18.336 1.00 60.96  ? 74  LEU   A N   1 
ATOM   278  C CA  . LEU   A 1 31  ? -1.824  -10.418 -17.418 1.00 59.40  ? 74  LEU   A CA  1 
ATOM   279  C C   . LEU   A 1 31  ? -1.983  -10.949 -15.992 1.00 65.64  ? 74  LEU   A C   1 
ATOM   280  O O   . LEU   A 1 31  ? -3.131  -11.069 -15.507 1.00 62.02  ? 74  LEU   A O   1 
ATOM   281  C CB  . LEU   A 1 31  ? -2.162  -8.927  -17.484 1.00 65.86  ? 74  LEU   A CB  1 
ATOM   282  C CG  . LEU   A 1 31  ? -1.977  -8.241  -18.835 1.00 68.49  ? 74  LEU   A CG  1 
ATOM   283  C CD1 . LEU   A 1 31  ? -2.682  -6.895  -18.836 1.00 68.22  ? 74  LEU   A CD1 1 
ATOM   284  C CD2 . LEU   A 1 31  ? -0.498  -8.072  -19.180 1.00 72.65  ? 74  LEU   A CD2 1 
ATOM   285  N N   . ASP   A 1 32  ? -0.851  -11.250 -15.351 1.00 65.21  ? 75  ASP   A N   1 
ATOM   286  C CA  . ASP   A 1 32  ? -0.745  -11.537 -13.898 1.00 65.77  ? 75  ASP   A CA  1 
ATOM   287  C C   . ASP   A 1 32  ? -0.858  -10.218 -13.132 1.00 56.07  ? 75  ASP   A C   1 
ATOM   288  O O   . ASP   A 1 32  ? -0.013  -9.337  -13.321 1.00 55.91  ? 75  ASP   A O   1 
ATOM   289  C CB  . ASP   A 1 32  ? 0.584   -12.215 -13.563 1.00 73.49  ? 75  ASP   A CB  1 
ATOM   290  C CG  . ASP   A 1 32  ? 0.731   -13.587 -14.186 1.00 74.84  ? 75  ASP   A CG  1 
ATOM   291  O OD1 . ASP   A 1 32  ? -0.254  -14.347 -14.173 1.00 75.79  ? 75  ASP   A OD1 1 
ATOM   292  O OD2 . ASP   A 1 32  ? 1.829   -13.875 -14.678 1.00 101.28 ? 75  ASP   A OD2 1 
ATOM   293  N N   . VAL   A 1 33  ? -1.885  -10.059 -12.306 1.00 58.83  ? 76  VAL   A N   1 
ATOM   294  C CA  . VAL   A 1 33  ? -2.145  -8.731  -11.677 1.00 54.16  ? 76  VAL   A CA  1 
ATOM   295  C C   . VAL   A 1 33  ? -2.431  -8.979  -10.198 1.00 49.96  ? 76  VAL   A C   1 
ATOM   296  O O   . VAL   A 1 33  ? -2.883  -10.123 -9.826  1.00 47.77  ? 76  VAL   A O   1 
ATOM   297  C CB  . VAL   A 1 33  ? -3.280  -7.948  -12.388 1.00 49.36  ? 76  VAL   A CB  1 
ATOM   298  C CG1 . VAL   A 1 33  ? -3.107  -7.853  -13.892 1.00 48.87  ? 76  VAL   A CG1 1 
ATOM   299  C CG2 . VAL   A 1 33  ? -4.656  -8.507  -12.088 1.00 52.43  ? 76  VAL   A CG2 1 
ATOM   300  N N   . ALA   A 1 34  ? -2.234  -7.947  -9.384  1.00 46.27  ? 77  ALA   A N   1 
ATOM   301  C CA  . ALA   A 1 34  ? -2.660  -7.948  -7.959  1.00 50.76  ? 77  ALA   A CA  1 
ATOM   302  C C   . ALA   A 1 34  ? -3.632  -6.789  -7.734  1.00 51.83  ? 77  ALA   A C   1 
ATOM   303  O O   . ALA   A 1 34  ? -3.563  -5.779  -8.452  1.00 49.19  ? 77  ALA   A O   1 
ATOM   304  C CB  . ALA   A 1 34  ? -1.491  -7.853  -7.018  1.00 49.48  ? 77  ALA   A CB  1 
ATOM   305  N N   . LEU   A 1 35  ? -4.505  -6.969  -6.757  1.00 46.06  ? 78  LEU   A N   1 
ATOM   306  C CA  . LEU   A 1 35  ? -5.574  -6.014  -6.393  1.00 46.63  ? 78  LEU   A CA  1 
ATOM   307  C C   . LEU   A 1 35  ? -5.376  -5.672  -4.913  1.00 49.36  ? 78  LEU   A C   1 
ATOM   308  O O   . LEU   A 1 35  ? -5.574  -6.580  -4.068  1.00 50.17  ? 78  LEU   A O   1 
ATOM   309  C CB  . LEU   A 1 35  ? -6.924  -6.686  -6.691  1.00 43.04  ? 78  LEU   A CB  1 
ATOM   310  C CG  . LEU   A 1 35  ? -8.171  -5.867  -6.372  1.00 42.58  ? 78  LEU   A CG  1 
ATOM   311  C CD1 . LEU   A 1 35  ? -8.205  -4.569  -7.145  1.00 41.78  ? 78  LEU   A CD1 1 
ATOM   312  C CD2 . LEU   A 1 35  ? -9.427  -6.687  -6.611  1.00 48.51  ? 78  LEU   A CD2 1 
ATOM   313  N N   . ASP   A 1 36  ? -4.953  -4.436  -4.631  1.00 45.57  ? 79  ASP   A N   1 
ATOM   314  C CA  . ASP   A 1 36  ? -4.809  -3.905  -3.251  1.00 53.29  ? 79  ASP   A CA  1 
ATOM   315  C C   . ASP   A 1 36  ? -6.189  -3.464  -2.726  1.00 50.73  ? 79  ASP   A C   1 
ATOM   316  O O   . ASP   A 1 36  ? -7.212  -3.594  -3.466  1.00 48.40  ? 79  ASP   A O   1 
ATOM   317  C CB  . ASP   A 1 36  ? -3.735  -2.813  -3.192  1.00 44.51  ? 79  ASP   A CB  1 
ATOM   318  C CG  . ASP   A 1 36  ? -4.153  -1.461  -3.733  1.00 48.83  ? 79  ASP   A CG  1 
ATOM   319  O OD1 . ASP   A 1 36  ? -5.358  -1.256  -4.009  1.00 48.60  ? 79  ASP   A OD1 1 
ATOM   320  O OD2 . ASP   A 1 36  ? -3.252  -0.604  -3.869  1.00 53.63  ? 79  ASP   A OD2 1 
ATOM   321  N N   . GLU   A 1 37  ? -6.205  -2.972  -1.485  1.00 50.50  ? 80  GLU   A N   1 
ATOM   322  C CA  . GLU   A 1 37  ? -7.420  -2.772  -0.668  1.00 46.89  ? 80  GLU   A CA  1 
ATOM   323  C C   . GLU   A 1 37  ? -8.094  -1.493  -1.165  1.00 43.85  ? 80  GLU   A C   1 
ATOM   324  O O   . GLU   A 1 37  ? -9.305  -1.333  -0.905  1.00 44.93  ? 80  GLU   A O   1 
ATOM   325  C CB  . GLU   A 1 37  ? -7.025  -2.722  0.817   1.00 50.11  ? 80  GLU   A CB  1 
ATOM   326  C CG  . GLU   A 1 37  ? -8.122  -3.097  1.795   1.00 61.38  ? 80  GLU   A CG  1 
ATOM   327  C CD  . GLU   A 1 37  ? -7.637  -3.213  3.243   1.00 75.22  ? 80  GLU   A CD  1 
ATOM   328  O OE1 . GLU   A 1 37  ? -7.347  -2.136  3.882   1.00 62.86  ? 80  GLU   A OE1 1 
ATOM   329  O OE2 . GLU   A 1 37  ? -7.503  -4.374  3.727   1.00 70.56  ? 80  GLU   A OE2 1 
ATOM   330  N N   . SER   A 1 38  ? -7.338  -0.620  -1.847  1.00 43.30  ? 81  SER   A N   1 
ATOM   331  C CA  . SER   A 1 38  ? -7.860  0.622   -2.478  1.00 46.00  ? 81  SER   A CA  1 
ATOM   332  C C   . SER   A 1 38  ? -8.415  0.369   -3.883  1.00 46.44  ? 81  SER   A C   1 
ATOM   333  O O   . SER   A 1 38  ? -8.711  1.360   -4.530  1.00 42.25  ? 81  SER   A O   1 
ATOM   334  C CB  . SER   A 1 38  ? -6.815  1.668   -2.580  1.00 45.79  ? 81  SER   A CB  1 
ATOM   335  O OG  . SER   A 1 38  ? -6.247  1.859   -1.325  1.00 52.78  ? 81  SER   A OG  1 
ATOM   336  N N   . GLY   A 1 39  ? -8.493  -0.874  -4.354  1.00 47.35  ? 82  GLY   A N   1 
ATOM   337  C CA  . GLY   A 1 39  ? -9.051  -1.193  -5.683  1.00 47.20  ? 82  GLY   A CA  1 
ATOM   338  C C   . GLY   A 1 39  ? -8.077  -0.843  -6.807  1.00 48.56  ? 82  GLY   A C   1 
ATOM   339  O O   . GLY   A 1 39  ? -8.552  -0.754  -7.945  1.00 48.04  ? 82  GLY   A O   1 
ATOM   340  N N   . ASP   A 1 40  ? -6.770  -0.686  -6.530  1.00 47.77  ? 83  ASP   A N   1 
ATOM   341  C CA  . ASP   A 1 40  ? -5.721  -0.541  -7.583  1.00 49.35  ? 83  ASP   A CA  1 
ATOM   342  C C   . ASP   A 1 40  ? -5.226  -1.912  -8.070  1.00 53.05  ? 83  ASP   A C   1 
ATOM   343  O O   . ASP   A 1 40  ? -4.640  -2.678  -7.281  1.00 48.55  ? 83  ASP   A O   1 
ATOM   344  C CB  . ASP   A 1 40  ? -4.529  0.273   -7.113  1.00 47.91  ? 83  ASP   A CB  1 
ATOM   345  C CG  . ASP   A 1 40  ? -4.931  1.486   -6.316  1.00 55.21  ? 83  ASP   A CG  1 
ATOM   346  O OD1 . ASP   A 1 40  ? -5.679  2.322   -6.853  1.00 56.62  ? 83  ASP   A OD1 1 
ATOM   347  O OD2 . ASP   A 1 40  ? -4.515  1.561   -5.146  1.00 64.32  ? 83  ASP   A OD2 1 
ATOM   348  N N   . PHE   A 1 41  ? -5.425  -2.188  -9.353  1.00 50.28  ? 84  PHE   A N   1 
ATOM   349  C CA  . PHE   A 1 41  ? -4.761  -3.296  -10.068 1.00 51.84  ? 84  PHE   A CA  1 
ATOM   350  C C   . PHE   A 1 41  ? -3.292  -2.943  -10.286 1.00 52.78  ? 84  PHE   A C   1 
ATOM   351  O O   . PHE   A 1 41  ? -2.966  -1.792  -10.658 1.00 54.26  ? 84  PHE   A O   1 
ATOM   352  C CB  . PHE   A 1 41  ? -5.509  -3.588  -11.359 1.00 49.01  ? 84  PHE   A CB  1 
ATOM   353  C CG  . PHE   A 1 41  ? -6.814  -4.315  -11.146 1.00 48.89  ? 84  PHE   A CG  1 
ATOM   354  C CD1 . PHE   A 1 41  ? -6.822  -5.615  -10.670 1.00 46.43  ? 84  PHE   A CD1 1 
ATOM   355  C CD2 . PHE   A 1 41  ? -8.030  -3.714  -11.436 1.00 44.83  ? 84  PHE   A CD2 1 
ATOM   356  C CE1 . PHE   A 1 41  ? -8.010  -6.294  -10.495 1.00 44.98  ? 84  PHE   A CE1 1 
ATOM   357  C CE2 . PHE   A 1 41  ? -9.220  -4.397  -11.253 1.00 39.83  ? 84  PHE   A CE2 1 
ATOM   358  C CZ  . PHE   A 1 41  ? -9.205  -5.686  -10.789 1.00 41.98  ? 84  PHE   A CZ  1 
ATOM   359  N N   . SER   A 1 42  ? -2.407  -3.905  -10.046 1.00 54.25  ? 85  SER   A N   1 
ATOM   360  C CA  . SER   A 1 42  ? -0.959  -3.764  -10.366 1.00 60.15  ? 85  SER   A CA  1 
ATOM   361  C C   . SER   A 1 42  ? -0.447  -5.023  -11.075 1.00 56.83  ? 85  SER   A C   1 
ATOM   362  O O   . SER   A 1 42  ? -1.021  -6.109  -10.891 1.00 59.58  ? 85  SER   A O   1 
ATOM   363  C CB  . SER   A 1 42  ? -0.153  -3.421  -9.141  1.00 61.30  ? 85  SER   A CB  1 
ATOM   364  O OG  . SER   A 1 42  ? -0.428  -4.336  -8.086  1.00 65.33  ? 85  SER   A OG  1 
ATOM   365  N N   . LEU   A 1 43  ? 0.562   -4.860  -11.921 1.00 61.53  ? 86  LEU   A N   1 
ATOM   366  C CA  . LEU   A 1 43  ? 1.227   -5.992  -12.616 1.00 67.39  ? 86  LEU   A CA  1 
ATOM   367  C C   . LEU   A 1 43  ? 2.186   -6.710  -11.657 1.00 64.01  ? 86  LEU   A C   1 
ATOM   368  O O   . LEU   A 1 43  ? 2.947   -6.034  -10.946 1.00 61.22  ? 86  LEU   A O   1 
ATOM   369  C CB  . LEU   A 1 43  ? 1.919   -5.431  -13.853 1.00 68.43  ? 86  LEU   A CB  1 
ATOM   370  C CG  . LEU   A 1 43  ? 0.920   -5.031  -14.931 1.00 77.60  ? 86  LEU   A CG  1 
ATOM   371  C CD1 . LEU   A 1 43  ? 1.591   -4.227  -16.029 1.00 91.24  ? 86  LEU   A CD1 1 
ATOM   372  C CD2 . LEU   A 1 43  ? 0.237   -6.266  -15.503 1.00 76.82  ? 86  LEU   A CD2 1 
ATOM   373  N N   . VAL   A 1 44  ? 2.054   -8.030  -11.571 1.00 66.44  ? 87  VAL   A N   1 
ATOM   374  C CA  . VAL   A 1 44  ? 2.974   -8.949  -10.836 1.00 79.76  ? 87  VAL   A CA  1 
ATOM   375  C C   . VAL   A 1 44  ? 3.939   -9.495  -11.890 1.00 88.64  ? 87  VAL   A C   1 
ATOM   376  O O   . VAL   A 1 44  ? 3.450   -9.951  -12.940 1.00 102.38 ? 87  VAL   A O   1 
ATOM   377  C CB  . VAL   A 1 44  ? 2.179   -10.076 -10.141 1.00 77.51  ? 87  VAL   A CB  1 
ATOM   378  C CG1 . VAL   A 1 44  ? 3.066   -11.188 -9.603  1.00 73.09  ? 87  VAL   A CG1 1 
ATOM   379  C CG2 . VAL   A 1 44  ? 1.274   -9.525  -9.046  1.00 72.74  ? 87  VAL   A CG2 1 
ATOM   380  N N   . GLU   A 1 45  ? 5.249   -9.411  -11.658 1.00 105.16 ? 88  GLU   A N   1 
ATOM   381  C CA  . GLU   A 1 45  ? 6.270   -9.755  -12.686 1.00 110.77 ? 88  GLU   A CA  1 
ATOM   382  C C   . GLU   A 1 45  ? 7.266   -10.755 -12.089 1.00 105.35 ? 88  GLU   A C   1 
ATOM   383  O O   . GLU   A 1 45  ? 6.929   -11.936 -12.027 1.00 102.76 ? 88  GLU   A O   1 
ATOM   384  C CB  . GLU   A 1 45  ? 6.926   -8.471  -13.200 1.00 114.41 ? 88  GLU   A CB  1 
ATOM   385  C CG  . GLU   A 1 45  ? 6.133   -7.772  -14.298 1.00 109.12 ? 88  GLU   A CG  1 
ATOM   386  C CD  . GLU   A 1 45  ? 6.501   -8.208  -15.706 1.00 113.82 ? 88  GLU   A CD  1 
ATOM   387  O OE1 . GLU   A 1 45  ? 7.173   -9.252  -15.831 1.00 109.50 ? 88  GLU   A OE1 1 
ATOM   388  O OE2 . GLU   A 1 45  ? 6.133   -7.494  -16.674 1.00 117.19 ? 88  GLU   A OE2 1 
ATOM   389  N N   . GLY   B 2 7   ? -36.769 12.589  -11.558 1.00 86.59  ? 16  GLY   B N   1 
ATOM   390  C CA  . GLY   B 2 7   ? -35.679 12.558  -12.593 1.00 84.73  ? 16  GLY   B CA  1 
ATOM   391  C C   . GLY   B 2 7   ? -35.899 11.523  -13.702 1.00 89.09  ? 16  GLY   B C   1 
ATOM   392  O O   . GLY   B 2 7   ? -36.875 10.716  -13.620 1.00 79.19  ? 16  GLY   B O   1 
ATOM   393  N N   . GLU   B 2 8   ? -35.014 11.534  -14.713 1.00 78.54  ? 17  GLU   B N   1 
ATOM   394  C CA  . GLU   B 2 8   ? -34.991 10.560  -15.842 1.00 71.05  ? 17  GLU   B CA  1 
ATOM   395  C C   . GLU   B 2 8   ? -34.510 9.206   -15.298 1.00 69.67  ? 17  GLU   B C   1 
ATOM   396  O O   . GLU   B 2 8   ? -33.338 9.081   -14.911 1.00 64.30  ? 17  GLU   B O   1 
ATOM   397  C CB  . GLU   B 2 8   ? -34.103 11.068  -16.987 1.00 71.16  ? 17  GLU   B CB  1 
ATOM   398  C CG  . GLU   B 2 8   ? -34.281 10.284  -18.282 1.00 67.86  ? 17  GLU   B CG  1 
ATOM   399  C CD  . GLU   B 2 8   ? -33.537 10.782  -19.522 1.00 72.56  ? 17  GLU   B CD  1 
ATOM   400  O OE1 . GLU   B 2 8   ? -32.571 11.594  -19.381 1.00 54.21  ? 17  GLU   B OE1 1 
ATOM   401  O OE2 . GLU   B 2 8   ? -34.003 10.425  -20.658 1.00 71.79  ? 17  GLU   B OE2 1 
ATOM   402  N N   A THR   B 2 9   ? -35.393 8.209   -15.238 0.25 69.65  ? 18  THR   B N   1 
ATOM   403  N N   B THR   B 2 9   ? -35.431 8.235   -15.285 0.25 68.74  ? 18  THR   B N   1 
ATOM   404  N N   C THR   B 2 9   ? -35.393 8.209   -15.238 0.25 69.65  ? 18  THR   B N   1 
ATOM   405  N N   D THR   B 2 9   ? -35.431 8.235   -15.285 0.25 68.74  ? 18  THR   B N   1 
ATOM   406  C CA  A THR   B 2 9   ? -35.042 6.836   -14.789 0.25 69.96  ? 18  THR   B CA  1 
ATOM   407  C CA  B THR   B 2 9   ? -35.257 6.852   -14.772 0.25 68.01  ? 18  THR   B CA  1 
ATOM   408  C CA  C THR   B 2 9   ? -35.042 6.836   -14.789 0.25 69.96  ? 18  THR   B CA  1 
ATOM   409  C CA  D THR   B 2 9   ? -35.257 6.852   -14.772 0.25 68.01  ? 18  THR   B CA  1 
ATOM   410  C C   A THR   B 2 9   ? -35.236 5.843   -15.935 0.25 65.77  ? 18  THR   B C   1 
ATOM   411  C C   B THR   B 2 9   ? -35.128 5.860   -15.933 0.25 64.75  ? 18  THR   B C   1 
ATOM   412  C C   C THR   B 2 9   ? -35.236 5.843   -15.935 0.25 65.77  ? 18  THR   B C   1 
ATOM   413  C C   D THR   B 2 9   ? -35.128 5.860   -15.933 0.25 64.75  ? 18  THR   B C   1 
ATOM   414  O O   A THR   B 2 9   ? -35.366 4.645   -15.642 0.25 69.88  ? 18  THR   B O   1 
ATOM   415  O O   B THR   B 2 9   ? -34.905 4.675   -15.646 0.25 68.75  ? 18  THR   B O   1 
ATOM   416  O O   C THR   B 2 9   ? -35.366 4.645   -15.642 0.25 69.88  ? 18  THR   B O   1 
ATOM   417  O O   D THR   B 2 9   ? -34.905 4.675   -15.646 0.25 68.75  ? 18  THR   B O   1 
ATOM   418  C CB  A THR   B 2 9   ? -35.853 6.415   -13.560 0.25 72.81  ? 18  THR   B CB  1 
ATOM   419  C CB  B THR   B 2 9   ? -36.445 6.450   -13.889 0.25 69.19  ? 18  THR   B CB  1 
ATOM   420  C CB  C THR   B 2 9   ? -35.853 6.415   -13.560 0.25 72.81  ? 18  THR   B CB  1 
ATOM   421  C CB  D THR   B 2 9   ? -36.445 6.450   -13.889 0.25 69.19  ? 18  THR   B CB  1 
ATOM   422  O OG1 A THR   B 2 9   ? -35.498 7.277   -12.479 0.25 74.83  ? 18  THR   B OG1 1 
ATOM   423  O OG1 B THR   B 2 9   ? -37.638 6.659   -14.643 0.25 65.88  ? 18  THR   B OG1 1 
ATOM   424  O OG1 C THR   B 2 9   ? -35.498 7.277   -12.479 0.25 74.83  ? 18  THR   B OG1 1 
ATOM   425  O OG1 D THR   B 2 9   ? -37.638 6.659   -14.643 0.25 65.88  ? 18  THR   B OG1 1 
ATOM   426  C CG2 A THR   B 2 9   ? -35.594 4.977   -13.174 0.25 71.03  ? 18  THR   B CG2 1 
ATOM   427  C CG2 B THR   B 2 9   ? -36.522 7.234   -12.598 0.25 71.71  ? 18  THR   B CG2 1 
ATOM   428  C CG2 C THR   B 2 9   ? -35.594 4.977   -13.174 0.25 71.03  ? 18  THR   B CG2 1 
ATOM   429  C CG2 D THR   B 2 9   ? -36.522 7.234   -12.598 0.25 71.71  ? 18  THR   B CG2 1 
ATOM   430  N N   . THR   B 2 10  ? -35.259 6.323   -17.181 1.00 62.06  ? 19  THR   B N   1 
ATOM   431  C CA  . THR   B 2 10  ? -35.321 5.449   -18.380 1.00 61.00  ? 19  THR   B CA  1 
ATOM   432  C C   . THR   B 2 10  ? -34.013 4.647   -18.440 1.00 48.86  ? 19  THR   B C   1 
ATOM   433  O O   . THR   B 2 10  ? -32.939 5.260   -18.324 1.00 50.55  ? 19  THR   B O   1 
ATOM   434  C CB  . THR   B 2 10  ? -35.490 6.240   -19.693 1.00 58.70  ? 19  THR   B CB  1 
ATOM   435  O OG1 . THR   B 2 10  ? -36.428 7.314   -19.552 1.00 76.79  ? 19  THR   B OG1 1 
ATOM   436  C CG2 . THR   B 2 10  ? -35.961 5.360   -20.828 1.00 55.30  ? 19  THR   B CG2 1 
ATOM   437  N N   A ASP   B 2 11  ? -34.118 3.325   -18.616 0.25 47.31  ? 20  ASP   B N   1 
ATOM   438  N N   B ASP   B 2 11  ? -34.118 3.325   -18.616 0.25 47.31  ? 20  ASP   B N   1 
ATOM   439  N N   C ASP   B 2 11  ? -34.116 3.325   -18.618 0.25 48.51  ? 20  ASP   B N   1 
ATOM   440  N N   D ASP   B 2 11  ? -34.116 3.325   -18.618 0.25 48.51  ? 20  ASP   B N   1 
ATOM   441  C CA  A ASP   B 2 11  ? -32.979 2.396   -18.862 0.25 47.46  ? 20  ASP   B CA  1 
ATOM   442  C CA  B ASP   B 2 11  ? -32.979 2.396   -18.862 0.25 47.46  ? 20  ASP   B CA  1 
ATOM   443  C CA  C ASP   B 2 11  ? -32.974 2.391   -18.829 0.25 49.36  ? 20  ASP   B CA  1 
ATOM   444  C CA  D ASP   B 2 11  ? -32.974 2.391   -18.829 0.25 49.36  ? 20  ASP   B CA  1 
ATOM   445  C C   A ASP   B 2 11  ? -32.004 3.004   -19.878 0.25 48.81  ? 20  ASP   B C   1 
ATOM   446  C C   B ASP   B 2 11  ? -32.004 3.004   -19.878 0.25 48.81  ? 20  ASP   B C   1 
ATOM   447  C C   C ASP   B 2 11  ? -32.013 2.965   -19.882 0.25 49.89  ? 20  ASP   B C   1 
ATOM   448  C C   D ASP   B 2 11  ? -32.013 2.965   -19.882 0.25 49.89  ? 20  ASP   B C   1 
ATOM   449  O O   A ASP   B 2 11  ? -32.467 3.715   -20.807 0.25 48.36  ? 20  ASP   B O   1 
ATOM   450  O O   B ASP   B 2 11  ? -32.467 3.715   -20.807 0.25 48.36  ? 20  ASP   B O   1 
ATOM   451  O O   C ASP   B 2 11  ? -32.497 3.624   -20.834 0.25 50.02  ? 20  ASP   B O   1 
ATOM   452  O O   D ASP   B 2 11  ? -32.497 3.624   -20.834 0.25 50.02  ? 20  ASP   B O   1 
ATOM   453  C CB  A ASP   B 2 11  ? -33.461 1.043   -19.390 0.25 46.34  ? 20  ASP   B CB  1 
ATOM   454  C CB  B ASP   B 2 11  ? -33.461 1.043   -19.390 0.25 46.34  ? 20  ASP   B CB  1 
ATOM   455  C CB  C ASP   B 2 11  ? -33.467 1.005   -19.258 0.25 49.62  ? 20  ASP   B CB  1 
ATOM   456  C CB  D ASP   B 2 11  ? -33.467 1.005   -19.258 0.25 49.62  ? 20  ASP   B CB  1 
ATOM   457  C CG  A ASP   B 2 11  ? -33.742 0.010   -18.312 0.25 48.18  ? 20  ASP   B CG  1 
ATOM   458  C CG  B ASP   B 2 11  ? -33.742 0.010   -18.312 0.25 48.18  ? 20  ASP   B CG  1 
ATOM   459  C CG  C ASP   B 2 11  ? -34.217 0.246   -18.174 0.25 52.83  ? 20  ASP   B CG  1 
ATOM   460  C CG  D ASP   B 2 11  ? -34.217 0.246   -18.174 0.25 52.83  ? 20  ASP   B CG  1 
ATOM   461  O OD1 A ASP   B 2 11  ? -34.069 0.418   -17.176 0.25 43.76  ? 20  ASP   B OD1 1 
ATOM   462  O OD1 B ASP   B 2 11  ? -34.069 0.418   -17.176 0.25 43.76  ? 20  ASP   B OD1 1 
ATOM   463  O OD1 C ASP   B 2 11  ? -34.115 0.657   -17.003 0.25 48.48  ? 20  ASP   B OD1 1 
ATOM   464  O OD1 D ASP   B 2 11  ? -34.115 0.657   -17.003 0.25 48.48  ? 20  ASP   B OD1 1 
ATOM   465  O OD2 A ASP   B 2 11  ? -33.635 -1.201  -18.621 0.25 51.40  ? 20  ASP   B OD2 1 
ATOM   466  O OD2 B ASP   B 2 11  ? -33.635 -1.201  -18.621 0.25 51.40  ? 20  ASP   B OD2 1 
ATOM   467  O OD2 C ASP   B 2 11  ? -34.898 -0.757  -18.511 0.25 58.41  ? 20  ASP   B OD2 1 
ATOM   468  O OD2 D ASP   B 2 11  ? -34.898 -0.757  -18.511 0.25 58.41  ? 20  ASP   B OD2 1 
ATOM   469  N N   . GLY   B 2 12  ? -30.704 2.738   -19.710 1.00 47.23  ? 21  GLY   B N   1 
ATOM   470  C CA  . GLY   B 2 12  ? -29.691 3.073   -20.727 1.00 43.11  ? 21  GLY   B CA  1 
ATOM   471  C C   . GLY   B 2 12  ? -28.436 3.619   -20.125 1.00 40.68  ? 21  GLY   B C   1 
ATOM   472  O O   . GLY   B 2 12  ? -28.245 3.544   -18.908 1.00 40.95  ? 21  GLY   B O   1 
ATOM   473  N N   . VAL   B 2 13  ? -27.629 4.223   -20.954 1.00 37.04  ? 22  VAL   B N   1 
ATOM   474  C CA  . VAL   B 2 13  ? -26.288 4.701   -20.534 1.00 39.93  ? 22  VAL   B CA  1 
ATOM   475  C C   . VAL   B 2 13  ? -26.355 6.206   -20.356 1.00 37.23  ? 22  VAL   B C   1 
ATOM   476  O O   . VAL   B 2 13  ? -27.047 6.870   -21.138 1.00 38.54  ? 22  VAL   B O   1 
ATOM   477  C CB  . VAL   B 2 13  ? -25.199 4.217   -21.494 1.00 42.20  ? 22  VAL   B CB  1 
ATOM   478  C CG1 . VAL   B 2 13  ? -25.391 4.771   -22.916 1.00 45.49  ? 22  VAL   B CG1 1 
ATOM   479  C CG2 . VAL   B 2 13  ? -23.818 4.524   -20.943 1.00 47.94  ? 22  VAL   B CG2 1 
ATOM   480  N N   . TYR   B 2 14  ? -25.700 6.718   -19.319 1.00 41.12  ? 23  TYR   B N   1 
ATOM   481  C CA  . TYR   B 2 14  ? -25.714 8.159   -18.969 1.00 37.62  ? 23  TYR   B CA  1 
ATOM   482  C C   . TYR   B 2 14  ? -24.305 8.655   -18.768 1.00 37.73  ? 23  TYR   B C   1 
ATOM   483  O O   . TYR   B 2 14  ? -23.458 7.929   -18.212 1.00 41.40  ? 23  TYR   B O   1 
ATOM   484  C CB  . TYR   B 2 14  ? -26.485 8.387   -17.672 1.00 34.09  ? 23  TYR   B CB  1 
ATOM   485  C CG  . TYR   B 2 14  ? -27.955 8.179   -17.802 1.00 36.00  ? 23  TYR   B CG  1 
ATOM   486  C CD1 . TYR   B 2 14  ? -28.455 6.919   -18.014 1.00 37.18  ? 23  TYR   B CD1 1 
ATOM   487  C CD2 . TYR   B 2 14  ? -28.839 9.250   -17.745 1.00 36.39  ? 23  TYR   B CD2 1 
ATOM   488  C CE1 . TYR   B 2 14  ? -29.807 6.686   -18.125 1.00 40.82  ? 23  TYR   B CE1 1 
ATOM   489  C CE2 . TYR   B 2 14  ? -30.195 9.043   -17.870 1.00 36.00  ? 23  TYR   B CE2 1 
ATOM   490  C CZ  . TYR   B 2 14  ? -30.681 7.762   -18.041 1.00 46.40  ? 23  TYR   B CZ  1 
ATOM   491  O OH  . TYR   B 2 14  ? -32.015 7.531   -18.122 1.00 44.07  ? 23  TYR   B OH  1 
ATOM   492  N N   . ARG   B 2 15  ? -24.098 9.932   -19.076 1.00 37.33  ? 24  ARG   B N   1 
ATOM   493  C CA  . ARG   B 2 15  ? -22.875 10.671  -18.670 1.00 35.09  ? 24  ARG   B CA  1 
ATOM   494  C C   . ARG   B 2 15  ? -23.043 11.188  -17.246 1.00 38.34  ? 24  ARG   B C   1 
ATOM   495  O O   . ARG   B 2 15  ? -24.152 11.535  -16.875 1.00 39.06  ? 24  ARG   B O   1 
ATOM   496  C CB  . ARG   B 2 15  ? -22.621 11.866  -19.591 1.00 41.18  ? 24  ARG   B CB  1 
ATOM   497  C CG  . ARG   B 2 15  ? -22.842 11.570  -21.074 1.00 42.84  ? 24  ARG   B CG  1 
ATOM   498  C CD  . ARG   B 2 15  ? -22.675 12.777  -21.972 1.00 44.35  ? 24  ARG   B CD  1 
ATOM   499  N NE  . ARG   B 2 15  ? -22.831 12.348  -23.371 1.00 46.86  ? 24  ARG   B NE  1 
ATOM   500  C CZ  . ARG   B 2 15  ? -21.832 12.162  -24.249 1.00 48.81  ? 24  ARG   B CZ  1 
ATOM   501  N NH1 . ARG   B 2 15  ? -20.575 12.406  -23.920 1.00 45.17  ? 24  ARG   B NH1 1 
ATOM   502  N NH2 . ARG   B 2 15  ? -22.111 11.735  -25.475 1.00 60.20  ? 24  ARG   B NH2 1 
ATOM   503  N N   . VAL   B 2 16  ? -21.950 11.201  -16.503 1.00 43.19  ? 25  VAL   B N   1 
ATOM   504  C CA  . VAL   B 2 16  ? -21.830 11.773  -15.146 1.00 43.25  ? 25  VAL   B CA  1 
ATOM   505  C C   . VAL   B 2 16  ? -21.012 13.056  -15.287 1.00 42.75  ? 25  VAL   B C   1 
ATOM   506  O O   . VAL   B 2 16  ? -19.823 12.967  -15.583 1.00 36.93  ? 25  VAL   B O   1 
ATOM   507  C CB  . VAL   B 2 16  ? -21.201 10.773  -14.147 1.00 47.15  ? 25  VAL   B CB  1 
ATOM   508  C CG1 . VAL   B 2 16  ? -21.134 11.372  -12.764 1.00 47.66  ? 25  VAL   B CG1 1 
ATOM   509  C CG2 . VAL   B 2 16  ? -21.943 9.447   -14.110 1.00 44.41  ? 25  VAL   B CG2 1 
ATOM   510  N N   . MET   B 2 17  ? -21.678 14.205  -15.091 1.00 44.50  ? 26  MET   B N   1 
ATOM   511  C CA  . MET   B 2 17  ? -21.119 15.568  -15.297 1.00 48.63  ? 26  MET   B CA  1 
ATOM   512  C C   . MET   B 2 17  ? -20.933 16.233  -13.935 1.00 44.94  ? 26  MET   B C   1 
ATOM   513  O O   . MET   B 2 17  ? -21.725 15.930  -13.053 1.00 43.05  ? 26  MET   B O   1 
ATOM   514  C CB  . MET   B 2 17  ? -22.098 16.404  -16.128 1.00 45.22  ? 26  MET   B CB  1 
ATOM   515  C CG  . MET   B 2 17  ? -22.581 15.689  -17.390 1.00 48.07  ? 26  MET   B CG  1 
ATOM   516  S SD  . MET   B 2 17  ? -21.267 15.351  -18.617 1.00 48.92  ? 26  MET   B SD  1 
ATOM   517  C CE  . MET   B 2 17  ? -20.341 16.890  -18.635 1.00 51.50  ? 26  MET   B CE  1 
ATOM   518  N N   . THR   B 2 18  ? -19.945 17.119  -13.798 1.00 52.35  ? 27  THR   B N   1 
ATOM   519  C CA  . THR   B 2 18  ? -19.846 18.121  -12.698 1.00 59.91  ? 27  THR   B CA  1 
ATOM   520  C C   . THR   B 2 18  ? -19.659 19.524  -13.293 1.00 61.37  ? 27  THR   B C   1 
ATOM   521  O O   . THR   B 2 18  ? -18.991 19.609  -14.369 1.00 52.81  ? 27  THR   B O   1 
ATOM   522  C CB  . THR   B 2 18  ? -18.671 17.835  -11.749 1.00 71.79  ? 27  THR   B CB  1 
ATOM   523  O OG1 . THR   B 2 18  ? -18.657 18.903  -10.794 1.00 62.66  ? 27  THR   B OG1 1 
ATOM   524  C CG2 . THR   B 2 18  ? -17.324 17.714  -12.444 1.00 64.56  ? 27  THR   B CG2 1 
ATOM   525  N N   . ARG   B 2 19  ? -20.156 20.572  -12.606 1.00 61.15  ? 28  ARG   B N   1 
ATOM   526  C CA  . ARG   B 2 19  ? -19.876 22.013  -12.917 1.00 69.45  ? 28  ARG   B CA  1 
ATOM   527  C C   . ARG   B 2 19  ? -18.914 22.661  -11.900 1.00 68.92  ? 28  ARG   B C   1 
ATOM   528  O O   . ARG   B 2 19  ? -18.545 23.843  -12.099 1.00 75.88  ? 28  ARG   B O   1 
ATOM   529  C CB  . ARG   B 2 19  ? -21.189 22.800  -13.006 1.00 76.19  ? 28  ARG   B CB  1 
ATOM   530  C CG  . ARG   B 2 19  ? -22.052 22.392  -14.190 1.00 84.82  ? 28  ARG   B CG  1 
ATOM   531  C CD  . ARG   B 2 19  ? -22.695 23.553  -14.916 1.00 88.84  ? 28  ARG   B CD  1 
ATOM   532  N NE  . ARG   B 2 19  ? -23.726 23.117  -15.853 1.00 91.86  ? 28  ARG   B NE  1 
ATOM   533  C CZ  . ARG   B 2 19  ? -24.977 22.789  -15.520 1.00 96.52  ? 28  ARG   B CZ  1 
ATOM   534  N NH1 . ARG   B 2 19  ? -25.361 22.838  -14.253 1.00 101.82 ? 28  ARG   B NH1 1 
ATOM   535  N NH2 . ARG   B 2 19  ? -25.834 22.393  -16.453 1.00 84.25  ? 28  ARG   B NH2 1 
ATOM   536  N N   . ARG   B 2 20  ? -18.472 21.929  -10.876 1.00 81.85  ? 29  ARG   B N   1 
ATOM   537  C CA  . ARG   B 2 20  ? -17.551 22.445  -9.823  1.00 93.11  ? 29  ARG   B CA  1 
ATOM   538  C C   . ARG   B 2 20  ? -16.307 23.019  -10.508 1.00 91.21  ? 29  ARG   B C   1 
ATOM   539  O O   . ARG   B 2 20  ? -15.881 24.107  -10.092 1.00 93.69  ? 29  ARG   B O   1 
ATOM   540  C CB  . ARG   B 2 20  ? -17.193 21.337  -8.823  1.00 101.45 ? 29  ARG   B CB  1 
ATOM   541  C CG  . ARG   B 2 20  ? -16.876 21.817  -7.413  1.00 104.64 ? 29  ARG   B CG  1 
ATOM   542  C CD  . ARG   B 2 20  ? -16.690 20.637  -6.473  1.00 119.98 ? 29  ARG   B CD  1 
ATOM   543  N NE  . ARG   B 2 20  ? -16.001 19.512  -7.110  1.00 136.36 ? 29  ARG   B NE  1 
ATOM   544  C CZ  . ARG   B 2 20  ? -14.680 19.416  -7.302  1.00 138.50 ? 29  ARG   B CZ  1 
ATOM   545  N NH1 . ARG   B 2 20  ? -13.870 20.384  -6.903  1.00 146.97 ? 29  ARG   B NH1 1 
ATOM   546  N NH2 . ARG   B 2 20  ? -14.169 18.349  -7.897  1.00 127.22 ? 29  ARG   B NH2 1 
ATOM   547  N N   . LEU   B 2 21  ? -15.803 22.337  -11.548 1.00 84.61  ? 30  LEU   B N   1 
ATOM   548  C CA  . LEU   B 2 21  ? -14.580 22.709  -12.319 1.00 84.46  ? 30  LEU   B CA  1 
ATOM   549  C C   . LEU   B 2 21  ? -14.930 23.700  -13.450 1.00 78.58  ? 30  LEU   B C   1 
ATOM   550  O O   . LEU   B 2 21  ? -16.091 24.162  -13.515 1.00 71.37  ? 30  LEU   B O   1 
ATOM   551  C CB  . LEU   B 2 21  ? -13.929 21.429  -12.859 1.00 80.94  ? 30  LEU   B CB  1 
ATOM   552  C CG  . LEU   B 2 21  ? -13.033 20.663  -11.887 1.00 89.08  ? 30  LEU   B CG  1 
ATOM   553  C CD1 . LEU   B 2 21  ? -13.656 20.586  -10.503 1.00 92.53  ? 30  LEU   B CD1 1 
ATOM   554  C CD2 . LEU   B 2 21  ? -12.730 19.260  -12.412 1.00 87.41  ? 30  LEU   B CD2 1 
ATOM   555  N N   . LEU   B 2 22  ? -13.948 24.041  -14.295 1.00 73.93  ? 31  LEU   B N   1 
ATOM   556  C CA  . LEU   B 2 22  ? -14.137 24.935  -15.463 1.00 71.27  ? 31  LEU   B CA  1 
ATOM   557  C C   . LEU   B 2 22  ? -15.155 24.313  -16.416 1.00 66.81  ? 31  LEU   B C   1 
ATOM   558  O O   . LEU   B 2 22  ? -15.009 23.118  -16.703 1.00 75.75  ? 31  LEU   B O   1 
ATOM   559  C CB  . LEU   B 2 22  ? -12.804 25.128  -16.178 1.00 67.88  ? 31  LEU   B CB  1 
ATOM   560  C CG  . LEU   B 2 22  ? -12.839 26.117  -17.338 1.00 66.15  ? 31  LEU   B CG  1 
ATOM   561  C CD1 . LEU   B 2 22  ? -12.742 27.554  -16.826 1.00 58.95  ? 31  LEU   B CD1 1 
ATOM   562  C CD2 . LEU   B 2 22  ? -11.710 25.823  -18.326 1.00 69.27  ? 31  LEU   B CD2 1 
ATOM   563  N N   . GLY   B 2 23  ? -16.120 25.104  -16.902 1.00 58.74  ? 32  GLY   B N   1 
ATOM   564  C CA  . GLY   B 2 23  ? -17.225 24.622  -17.757 1.00 54.62  ? 32  GLY   B CA  1 
ATOM   565  C C   . GLY   B 2 23  ? -17.983 23.446  -17.133 1.00 54.20  ? 32  GLY   B C   1 
ATOM   566  O O   . GLY   B 2 23  ? -18.107 23.381  -15.894 1.00 57.05  ? 32  GLY   B O   1 
ATOM   567  N N   . SER   B 2 24  ? -18.515 22.557  -17.967 1.00 50.93  ? 33  SER   B N   1 
ATOM   568  C CA  . SER   B 2 24  ? -19.117 21.267  -17.546 1.00 54.00  ? 33  SER   B CA  1 
ATOM   569  C C   . SER   B 2 24  ? -18.206 20.143  -18.029 1.00 51.67  ? 33  SER   B C   1 
ATOM   570  O O   . SER   B 2 24  ? -17.948 20.077  -19.226 1.00 52.11  ? 33  SER   B O   1 
ATOM   571  C CB  . SER   B 2 24  ? -20.501 21.107  -18.054 1.00 54.51  ? 33  SER   B CB  1 
ATOM   572  O OG  . SER   B 2 24  ? -21.251 22.284  -17.796 1.00 60.20  ? 33  SER   B OG  1 
ATOM   573  N N   . THR   B 2 25  ? -17.704 19.348  -17.088 1.00 57.41  ? 34  THR   B N   1 
ATOM   574  C CA  . THR   B 2 25  ? -16.669 18.297  -17.271 1.00 51.30  ? 34  THR   B CA  1 
ATOM   575  C C   . THR   B 2 25  ? -17.334 16.931  -17.079 1.00 48.48  ? 34  THR   B C   1 
ATOM   576  O O   . THR   B 2 25  ? -18.051 16.769  -16.089 1.00 46.53  ? 34  THR   B O   1 
ATOM   577  C CB  . THR   B 2 25  ? -15.515 18.570  -16.306 1.00 54.19  ? 34  THR   B CB  1 
ATOM   578  O OG1 . THR   B 2 25  ? -15.020 19.870  -16.643 1.00 57.25  ? 34  THR   B OG1 1 
ATOM   579  C CG2 . THR   B 2 25  ? -14.401 17.552  -16.396 1.00 60.39  ? 34  THR   B CG2 1 
ATOM   580  N N   . GLN   B 2 26  ? -17.122 16.001  -18.003 1.00 46.79  ? 35  GLN   B N   1 
ATOM   581  C CA  . GLN   B 2 26  ? -17.552 14.585  -17.863 1.00 54.88  ? 35  GLN   B CA  1 
ATOM   582  C C   . GLN   B 2 26  ? -16.520 13.864  -16.976 1.00 55.44  ? 35  GLN   B C   1 
ATOM   583  O O   . GLN   B 2 26  ? -15.327 13.811  -17.381 1.00 55.03  ? 35  GLN   B O   1 
ATOM   584  C CB  . GLN   B 2 26  ? -17.700 13.919  -19.233 1.00 49.91  ? 35  GLN   B CB  1 
ATOM   585  C CG  . GLN   B 2 26  ? -18.297 12.527  -19.142 1.00 47.02  ? 35  GLN   B CG  1 
ATOM   586  C CD  . GLN   B 2 26  ? -18.679 11.927  -20.467 1.00 52.89  ? 35  GLN   B CD  1 
ATOM   587  O OE1 . GLN   B 2 26  ? -19.365 12.548  -21.281 1.00 48.60  ? 35  GLN   B OE1 1 
ATOM   588  N NE2 . GLN   B 2 26  ? -18.295 10.674  -20.677 1.00 47.24  ? 35  GLN   B NE2 1 
ATOM   589  N N   . VAL   B 2 27  ? -16.932 13.406  -15.784 1.00 51.53  ? 36  VAL   B N   1 
ATOM   590  C CA  . VAL   B 2 27  ? -16.042 12.652  -14.844 1.00 48.37  ? 36  VAL   B CA  1 
ATOM   591  C C   . VAL   B 2 27  ? -16.234 11.143  -15.056 1.00 41.17  ? 36  VAL   B C   1 
ATOM   592  O O   . VAL   B 2 27  ? -15.317 10.380  -14.677 1.00 46.87  ? 36  VAL   B O   1 
ATOM   593  C CB  . VAL   B 2 27  ? -16.266 13.054  -13.371 1.00 49.01  ? 36  VAL   B CB  1 
ATOM   594  C CG1 . VAL   B 2 27  ? -15.663 14.407  -13.076 1.00 54.82  ? 36  VAL   B CG1 1 
ATOM   595  C CG2 . VAL   B 2 27  ? -17.726 13.017  -12.975 1.00 51.52  ? 36  VAL   B CG2 1 
ATOM   596  N N   . GLY   B 2 28  ? -17.354 10.716  -15.651 1.00 42.71  ? 37  GLY   B N   1 
ATOM   597  C CA  . GLY   B 2 28  ? -17.574 9.299   -15.992 1.00 37.03  ? 37  GLY   B CA  1 
ATOM   598  C C   . GLY   B 2 28  ? -18.922 9.004   -16.603 1.00 35.08  ? 37  GLY   B C   1 
ATOM   599  O O   . GLY   B 2 28  ? -19.551 9.927   -17.157 1.00 41.24  ? 37  GLY   B O   1 
ATOM   600  N N   . VAL   B 2 29  ? -19.349 7.752   -16.495 1.00 32.74  ? 38  VAL   B N   1 
ATOM   601  C CA  . VAL   B 2 29  ? -20.530 7.157   -17.206 1.00 35.99  ? 38  VAL   B CA  1 
ATOM   602  C C   . VAL   B 2 29  ? -21.231 6.156   -16.268 1.00 38.20  ? 38  VAL   B C   1 
ATOM   603  O O   . VAL   B 2 29  ? -20.570 5.683   -15.318 1.00 38.80  ? 38  VAL   B O   1 
ATOM   604  C CB  . VAL   B 2 29  ? -20.063 6.481   -18.513 1.00 36.53  ? 38  VAL   B CB  1 
ATOM   605  C CG1 . VAL   B 2 29  ? -21.178 5.886   -19.317 1.00 35.54  ? 38  VAL   B CG1 1 
ATOM   606  C CG2 . VAL   B 2 29  ? -19.249 7.420   -19.378 1.00 37.93  ? 38  VAL   B CG2 1 
ATOM   607  N N   . GLY   B 2 30  ? -22.508 5.869   -16.483 1.00 33.00  ? 39  GLY   B N   1 
ATOM   608  C CA  . GLY   B 2 30  ? -23.164 4.750   -15.811 1.00 31.52  ? 39  GLY   B CA  1 
ATOM   609  C C   . GLY   B 2 30  ? -24.337 4.201   -16.538 1.00 32.15  ? 39  GLY   B C   1 
ATOM   610  O O   . GLY   B 2 30  ? -24.689 4.685   -17.624 1.00 37.44  ? 39  GLY   B O   1 
ATOM   611  N N   . VAL   B 2 31  ? -24.917 3.177   -15.963 1.00 30.17  ? 40  VAL   B N   1 
ATOM   612  C CA  . VAL   B 2 31  ? -26.030 2.381   -16.540 1.00 32.73  ? 40  VAL   B CA  1 
ATOM   613  C C   . VAL   B 2 31  ? -27.213 2.548   -15.619 1.00 39.51  ? 40  VAL   B C   1 
ATOM   614  O O   . VAL   B 2 31  ? -27.040 2.290   -14.391 1.00 35.12  ? 40  VAL   B O   1 
ATOM   615  C CB  . VAL   B 2 31  ? -25.630 0.891   -16.620 1.00 36.09  ? 40  VAL   B CB  1 
ATOM   616  C CG1 . VAL   B 2 31  ? -26.767 -0.012  -17.058 1.00 37.63  ? 40  VAL   B CG1 1 
ATOM   617  C CG2 . VAL   B 2 31  ? -24.388 0.706   -17.460 1.00 36.03  ? 40  VAL   B CG2 1 
ATOM   618  N N   . MET   B 2 32  ? -28.371 2.891   -16.185 1.00 38.32  ? 41  MET   B N   1 
ATOM   619  C CA  . MET   B 2 32  ? -29.668 2.847   -15.477 1.00 37.30  ? 41  MET   B CA  1 
ATOM   620  C C   . MET   B 2 32  ? -30.351 1.540   -15.883 1.00 38.05  ? 41  MET   B C   1 
ATOM   621  O O   . MET   B 2 32  ? -30.439 1.269   -17.074 1.00 39.10  ? 41  MET   B O   1 
ATOM   622  C CB  . MET   B 2 32  ? -30.540 4.060   -15.837 1.00 39.05  ? 41  MET   B CB  1 
ATOM   623  C CG  . MET   B 2 32  ? -31.778 4.154   -14.966 1.00 42.25  ? 41  MET   B CG  1 
ATOM   624  S SD  . MET   B 2 32  ? -31.345 4.769   -13.317 1.00 44.78  ? 41  MET   B SD  1 
ATOM   625  C CE  . MET   B 2 32  ? -30.637 6.362   -13.724 1.00 47.69  ? 41  MET   B CE  1 
ATOM   626  N N   . GLN   B 2 33  ? -30.760 0.724   -14.921 1.00 33.95  ? 42  GLN   B N   1 
ATOM   627  C CA  . GLN   B 2 33  ? -31.448 -0.557  -15.140 1.00 39.60  ? 42  GLN   B CA  1 
ATOM   628  C C   . GLN   B 2 33  ? -32.295 -0.834  -13.921 1.00 39.70  ? 42  GLN   B C   1 
ATOM   629  O O   . GLN   B 2 33  ? -31.757 -0.732  -12.794 1.00 41.30  ? 42  GLN   B O   1 
ATOM   630  C CB  . GLN   B 2 33  ? -30.492 -1.736  -15.359 1.00 43.52  ? 42  GLN   B CB  1 
ATOM   631  C CG  . GLN   B 2 33  ? -31.252 -2.970  -15.871 1.00 46.20  ? 42  GLN   B CG  1 
ATOM   632  C CD  . GLN   B 2 33  ? -30.372 -3.986  -16.569 1.00 53.12  ? 42  GLN   B CD  1 
ATOM   633  O OE1 . GLN   B 2 33  ? -30.437 -5.175  -16.278 1.00 63.48  ? 42  GLN   B OE1 1 
ATOM   634  N NE2 . GLN   B 2 33  ? -29.497 -3.526  -17.448 1.00 51.56  ? 42  GLN   B NE2 1 
ATOM   635  N N   . GLU   B 2 34  ? -33.559 -1.134  -14.150 1.00 48.90  ? 43  GLU   B N   1 
ATOM   636  C CA  . GLU   B 2 34  ? -34.565 -1.453  -13.105 1.00 49.89  ? 43  GLU   B CA  1 
ATOM   637  C C   . GLU   B 2 34  ? -34.618 -0.355  -12.028 1.00 44.51  ? 43  GLU   B C   1 
ATOM   638  O O   . GLU   B 2 34  ? -34.669 -0.698  -10.867 1.00 48.53  ? 43  GLU   B O   1 
ATOM   639  C CB  . GLU   B 2 34  ? -34.240 -2.831  -12.538 1.00 52.86  ? 43  GLU   B CB  1 
ATOM   640  C CG  . GLU   B 2 34  ? -34.325 -3.941  -13.582 1.00 59.61  ? 43  GLU   B CG  1 
ATOM   641  C CD  . GLU   B 2 34  ? -33.602 -5.231  -13.208 1.00 64.05  ? 43  GLU   B CD  1 
ATOM   642  O OE1 . GLU   B 2 34  ? -34.087 -5.968  -12.326 1.00 65.36  ? 43  GLU   B OE1 1 
ATOM   643  O OE2 . GLU   B 2 34  ? -32.546 -5.490  -13.799 1.00 75.14  ? 43  GLU   B OE2 1 
ATOM   644  N N   . GLY   B 2 35  ? -34.609 0.918   -12.399 1.00 47.96  ? 44  GLY   B N   1 
ATOM   645  C CA  . GLY   B 2 35  ? -34.703 2.025   -11.424 1.00 48.73  ? 44  GLY   B CA  1 
ATOM   646  C C   . GLY   B 2 35  ? -33.420 2.261   -10.642 1.00 47.98  ? 44  GLY   B C   1 
ATOM   647  O O   . GLY   B 2 35  ? -33.430 3.149   -9.733  1.00 43.64  ? 44  GLY   B O   1 
ATOM   648  N N   . VAL   B 2 36  ? -32.327 1.556   -10.972 1.00 37.97  ? 45  VAL   B N   1 
ATOM   649  C CA  . VAL   B 2 36  ? -31.028 1.679   -10.264 1.00 33.01  ? 45  VAL   B CA  1 
ATOM   650  C C   . VAL   B 2 36  ? -29.967 2.191   -11.205 1.00 34.40  ? 45  VAL   B C   1 
ATOM   651  O O   . VAL   B 2 36  ? -29.852 1.661   -12.343 1.00 38.44  ? 45  VAL   B O   1 
ATOM   652  C CB  . VAL   B 2 36  ? -30.557 0.368   -9.592  1.00 39.88  ? 45  VAL   B CB  1 
ATOM   653  C CG1 . VAL   B 2 36  ? -29.143 0.515   -9.015  1.00 38.66  ? 45  VAL   B CG1 1 
ATOM   654  C CG2 . VAL   B 2 36  ? -31.533 -0.119  -8.536  1.00 37.10  ? 45  VAL   B CG2 1 
ATOM   655  N N   . PHE   B 2 37  ? -29.144 3.094   -10.695 1.00 31.44  ? 46  PHE   B N   1 
ATOM   656  C CA  . PHE   B 2 37  ? -28.009 3.667   -11.413 1.00 34.49  ? 46  PHE   B CA  1 
ATOM   657  C C   . PHE   B 2 37  ? -26.681 3.102   -10.908 1.00 39.17  ? 46  PHE   B C   1 
ATOM   658  O O   . PHE   B 2 37  ? -26.334 3.142   -9.725  1.00 39.94  ? 46  PHE   B O   1 
ATOM   659  C CB  . PHE   B 2 37  ? -27.993 5.179   -11.337 1.00 33.15  ? 46  PHE   B CB  1 
ATOM   660  C CG  . PHE   B 2 37  ? -27.021 5.782   -12.303 1.00 28.80  ? 46  PHE   B CG  1 
ATOM   661  C CD1 . PHE   B 2 37  ? -27.185 5.577   -13.667 1.00 33.56  ? 46  PHE   B CD1 1 
ATOM   662  C CD2 . PHE   B 2 37  ? -25.957 6.535   -11.858 1.00 28.26  ? 46  PHE   B CD2 1 
ATOM   663  C CE1 . PHE   B 2 37  ? -26.318 6.175   -14.570 1.00 31.93  ? 46  PHE   B CE1 1 
ATOM   664  C CE2 . PHE   B 2 37  ? -25.078 7.114   -12.757 1.00 33.74  ? 46  PHE   B CE2 1 
ATOM   665  C CZ  . PHE   B 2 37  ? -25.258 6.935   -14.111 1.00 30.93  ? 46  PHE   B CZ  1 
ATOM   666  N N   . HIS   B 2 38  ? -25.897 2.667   -11.864 1.00 33.63  ? 47  HIS   B N   1 
ATOM   667  C CA  . HIS   B 2 38  ? -24.677 1.831   -11.677 1.00 31.48  ? 47  HIS   B CA  1 
ATOM   668  C C   . HIS   B 2 38  ? -23.492 2.574   -12.253 1.00 29.91  ? 47  HIS   B C   1 
ATOM   669  O O   . HIS   B 2 38  ? -23.530 2.919   -13.464 1.00 30.77  ? 47  HIS   B O   1 
ATOM   670  C CB  . HIS   B 2 38  ? -24.844 0.523   -12.403 1.00 32.83  ? 47  HIS   B CB  1 
ATOM   671  C CG  . HIS   B 2 38  ? -25.989 -0.339  -12.004 1.00 29.86  ? 47  HIS   B CG  1 
ATOM   672  N ND1 . HIS   B 2 38  ? -27.236 -0.194  -12.544 1.00 30.16  ? 47  HIS   B ND1 1 
ATOM   673  C CD2 . HIS   B 2 38  ? -26.070 -1.404  -11.176 1.00 32.82  ? 47  HIS   B CD2 1 
ATOM   674  C CE1 . HIS   B 2 38  ? -28.059 -1.081  -12.015 1.00 30.89  ? 47  HIS   B CE1 1 
ATOM   675  N NE2 . HIS   B 2 38  ? -27.361 -1.844  -11.195 1.00 33.89  ? 47  HIS   B NE2 1 
ATOM   676  N N   . THR   B 2 39  ? -22.503 2.874   -11.446 1.00 31.60  ? 48  THR   B N   1 
ATOM   677  C CA  . THR   B 2 39  ? -21.236 3.438   -11.951 1.00 34.42  ? 48  THR   B CA  1 
ATOM   678  C C   . THR   B 2 39  ? -20.073 2.844   -11.157 1.00 33.66  ? 48  THR   B C   1 
ATOM   679  O O   . THR   B 2 39  ? -20.289 1.934   -10.338 1.00 29.74  ? 48  THR   B O   1 
ATOM   680  C CB  . THR   B 2 39  ? -21.320 4.953   -11.968 1.00 37.45  ? 48  THR   B CB  1 
ATOM   681  O OG1 . THR   B 2 39  ? -20.163 5.490   -12.601 1.00 34.97  ? 48  THR   B OG1 1 
ATOM   682  C CG2 . THR   B 2 39  ? -21.455 5.550   -10.587 1.00 38.75  ? 48  THR   B CG2 1 
ATOM   683  N N   . MET   B 2 40  ? -18.892 3.395   -11.353 1.00 33.59  ? 49  MET   B N   1 
ATOM   684  C CA  . MET   B 2 40  ? -17.687 3.000   -10.591 1.00 39.42  ? 49  MET   B CA  1 
ATOM   685  C C   . MET   B 2 40  ? -17.477 4.018   -9.464  1.00 38.67  ? 49  MET   B C   1 
ATOM   686  O O   . MET   B 2 40  ? -17.748 5.219   -9.663  1.00 38.04  ? 49  MET   B O   1 
ATOM   687  C CB  . MET   B 2 40  ? -16.493 2.947   -11.540 1.00 36.50  ? 49  MET   B CB  1 
ATOM   688  C CG  . MET   B 2 40  ? -16.797 2.130   -12.800 1.00 39.29  ? 49  MET   B CG  1 
ATOM   689  S SD  . MET   B 2 40  ? -15.326 1.389   -13.431 1.00 55.97  ? 49  MET   B SD  1 
ATOM   690  C CE  . MET   B 2 40  ? -15.143 -0.043  -12.365 1.00 48.63  ? 49  MET   B CE  1 
ATOM   691  N N   A TRP   B 2 41  ? -16.980 3.544   -8.319  0.16 37.80  ? 50  TRP   B N   1 
ATOM   692  N N   B TRP   B 2 41  ? -16.992 3.547   -8.312  0.28 36.24  ? 50  TRP   B N   1 
ATOM   693  N N   C TRP   B 2 41  ? -16.982 3.545   -8.318  0.25 37.60  ? 50  TRP   B N   1 
ATOM   694  N N   D TRP   B 2 41  ? -16.991 3.547   -8.312  0.25 36.27  ? 50  TRP   B N   1 
ATOM   695  C CA  A TRP   B 2 41  ? -16.781 4.348   -7.085  0.16 37.73  ? 50  TRP   B CA  1 
ATOM   696  C CA  B TRP   B 2 41  ? -16.797 4.362   -7.086  0.28 35.47  ? 50  TRP   B CA  1 
ATOM   697  C CA  C TRP   B 2 41  ? -16.781 4.349   -7.085  0.25 37.54  ? 50  TRP   B CA  1 
ATOM   698  C CA  D TRP   B 2 41  ? -16.797 4.362   -7.085  0.25 35.50  ? 50  TRP   B CA  1 
ATOM   699  C C   A TRP   B 2 41  ? -15.890 5.565   -7.372  0.16 37.83  ? 50  TRP   B C   1 
ATOM   700  C C   B TRP   B 2 41  ? -15.891 5.569   -7.377  0.28 36.37  ? 50  TRP   B C   1 
ATOM   701  C C   C TRP   B 2 41  ? -15.889 5.565   -7.373  0.25 37.67  ? 50  TRP   B C   1 
ATOM   702  C C   D TRP   B 2 41  ? -15.890 5.568   -7.374  0.25 36.40  ? 50  TRP   B C   1 
ATOM   703  O O   A TRP   B 2 41  ? -16.225 6.664   -6.898  0.16 38.96  ? 50  TRP   B O   1 
ATOM   704  O O   B TRP   B 2 41  ? -16.208 6.673   -6.907  0.28 37.78  ? 50  TRP   B O   1 
ATOM   705  O O   C TRP   B 2 41  ? -16.218 6.665   -6.902  0.25 39.09  ? 50  TRP   B O   1 
ATOM   706  O O   D TRP   B 2 41  ? -16.209 6.672   -6.904  0.25 37.77  ? 50  TRP   B O   1 
ATOM   707  C CB  A TRP   B 2 41  ? -16.207 3.491   -5.948  0.16 37.56  ? 50  TRP   B CB  1 
ATOM   708  C CB  B TRP   B 2 41  ? -16.253 3.514   -5.923  0.28 33.93  ? 50  TRP   B CB  1 
ATOM   709  C CB  C TRP   B 2 41  ? -16.206 3.490   -5.950  0.25 37.33  ? 50  TRP   B CB  1 
ATOM   710  C CB  D TRP   B 2 41  ? -16.254 3.515   -5.923  0.25 33.96  ? 50  TRP   B CB  1 
ATOM   711  C CG  A TRP   B 2 41  ? -16.261 4.203   -4.633  0.16 37.43  ? 50  TRP   B CG  1 
ATOM   712  C CG  B TRP   B 2 41  ? -16.101 4.331   -4.678  0.28 32.47  ? 50  TRP   B CG  1 
ATOM   713  C CG  C TRP   B 2 41  ? -16.260 4.201   -4.635  0.25 37.11  ? 50  TRP   B CG  1 
ATOM   714  C CG  D TRP   B 2 41  ? -16.103 4.332   -4.679  0.25 32.51  ? 50  TRP   B CG  1 
ATOM   715  C CD1 A TRP   B 2 41  ? -17.296 4.198   -3.745  0.16 37.69  ? 50  TRP   B CD1 1 
ATOM   716  C CD1 B TRP   B 2 41  ? -15.037 5.117   -4.341  0.28 32.47  ? 50  TRP   B CD1 1 
ATOM   717  C CD1 C TRP   B 2 41  ? -17.295 4.196   -3.747  0.25 37.48  ? 50  TRP   B CD1 1 
ATOM   718  C CD1 D TRP   B 2 41  ? -15.038 5.118   -4.343  0.25 32.49  ? 50  TRP   B CD1 1 
ATOM   719  C CD2 A TRP   B 2 41  ? -15.265 5.085   -4.085  0.16 38.48  ? 50  TRP   B CD2 1 
ATOM   720  C CD2 B TRP   B 2 41  ? -17.081 4.523   -3.644  0.28 32.48  ? 50  TRP   B CD2 1 
ATOM   721  C CD2 C TRP   B 2 41  ? -15.264 5.084   -4.085  0.25 38.45  ? 50  TRP   B CD2 1 
ATOM   722  C CD2 D TRP   B 2 41  ? -17.082 4.524   -3.644  0.25 32.49  ? 50  TRP   B CD2 1 
ATOM   723  N NE1 A TRP   B 2 41  ? -17.002 4.994   -2.672  0.16 37.81  ? 50  TRP   B NE1 1 
ATOM   724  N NE1 B TRP   B 2 41  ? -15.281 5.773   -3.167  0.28 31.62  ? 50  TRP   B NE1 1 
ATOM   725  N NE1 C TRP   B 2 41  ? -17.001 4.992   -2.675  0.25 37.57  ? 50  TRP   B NE1 1 
ATOM   726  N NE1 D TRP   B 2 41  ? -15.282 5.772   -3.168  0.25 31.66  ? 50  TRP   B NE1 1 
ATOM   727  C CE2 A TRP   B 2 41  ? -15.768 5.557   -2.855  0.16 38.38  ? 50  TRP   B CE2 1 
ATOM   728  C CE2 B TRP   B 2 41  ? -16.522 5.418   -2.708  0.28 31.41  ? 50  TRP   B CE2 1 
ATOM   729  C CE2 C TRP   B 2 41  ? -15.768 5.557   -2.857  0.25 38.25  ? 50  TRP   B CE2 1 
ATOM   730  C CE2 D TRP   B 2 41  ? -16.522 5.418   -2.708  0.25 31.46  ? 50  TRP   B CE2 1 
ATOM   731  C CE3 A TRP   B 2 41  ? -13.999 5.514   -4.503  0.16 38.90  ? 50  TRP   B CE3 1 
ATOM   732  C CE3 B TRP   B 2 41  ? -18.366 4.022   -3.407  0.28 31.93  ? 50  TRP   B CE3 1 
ATOM   733  C CE3 C TRP   B 2 41  ? -13.998 5.513   -4.501  0.25 38.95  ? 50  TRP   B CE3 1 
ATOM   734  C CE3 D TRP   B 2 41  ? -18.367 4.023   -3.405  0.25 31.95  ? 50  TRP   B CE3 1 
ATOM   735  C CZ2 A TRP   B 2 41  ? -15.044 6.432   -2.043  0.16 40.78  ? 50  TRP   B CZ2 1 
ATOM   736  C CZ2 B TRP   B 2 41  ? -17.205 5.819   -1.557  0.28 33.20  ? 50  TRP   B CZ2 1 
ATOM   737  C CZ2 C TRP   B 2 41  ? -15.046 6.433   -2.046  0.25 41.43  ? 50  TRP   B CZ2 1 
ATOM   738  C CZ2 D TRP   B 2 41  ? -17.204 5.818   -1.557  0.25 33.16  ? 50  TRP   B CZ2 1 
ATOM   739  C CZ3 A TRP   B 2 41  ? -13.282 6.373   -3.697  0.16 38.93  ? 50  TRP   B CZ3 1 
ATOM   740  C CZ3 B TRP   B 2 41  ? -19.038 4.417   -2.267  0.28 32.76  ? 50  TRP   B CZ3 1 
ATOM   741  C CZ3 C TRP   B 2 41  ? -13.282 6.371   -3.694  0.25 38.88  ? 50  TRP   B CZ3 1 
ATOM   742  C CZ3 D TRP   B 2 41  ? -19.038 4.418   -2.266  0.25 32.71  ? 50  TRP   B CZ3 1 
ATOM   743  C CH2 A TRP   B 2 41  ? -13.801 6.824   -2.484  0.16 39.83  ? 50  TRP   B CH2 1 
ATOM   744  C CH2 B TRP   B 2 41  ? -18.469 5.309   -1.360  0.28 31.96  ? 50  TRP   B CH2 1 
ATOM   745  C CH2 C TRP   B 2 41  ? -13.802 6.823   -2.483  0.25 40.08  ? 50  TRP   B CH2 1 
ATOM   746  C CH2 D TRP   B 2 41  ? -18.468 5.309   -1.359  0.25 31.96  ? 50  TRP   B CH2 1 
ATOM   747  N N   . HIS   B 2 42  ? -14.794 5.387   -8.112  1.00 38.43  ? 51  HIS   B N   1 
ATOM   748  C CA  . HIS   B 2 42  ? -13.812 6.500   -8.355  1.00 38.19  ? 51  HIS   B CA  1 
ATOM   749  C C   . HIS   B 2 42  ? -14.454 7.628   -9.208  1.00 38.37  ? 51  HIS   B C   1 
ATOM   750  O O   . HIS   B 2 42  ? -13.933 8.735   -9.204  1.00 39.56  ? 51  HIS   B O   1 
ATOM   751  C CB  . HIS   B 2 42  ? -12.495 5.975   -8.948  1.00 38.66  ? 51  HIS   B CB  1 
ATOM   752  C CG  . HIS   B 2 42  ? -12.563 5.748   -10.412 1.00 39.78  ? 51  HIS   B CG  1 
ATOM   753  N ND1 . HIS   B 2 42  ? -12.846 4.505   -10.953 1.00 36.45  ? 51  HIS   B ND1 1 
ATOM   754  C CD2 . HIS   B 2 42  ? -12.427 6.603   -11.452 1.00 45.43  ? 51  HIS   B CD2 1 
ATOM   755  C CE1 . HIS   B 2 42  ? -12.870 4.622   -12.276 1.00 42.01  ? 51  HIS   B CE1 1 
ATOM   756  N NE2 . HIS   B 2 42  ? -12.651 5.904   -12.601 1.00 37.30  ? 51  HIS   B NE2 1 
ATOM   757  N N   . VAL   B 2 43  ? -15.588 7.411   -9.859  1.00 40.01  ? 52  VAL   B N   1 
ATOM   758  C CA  . VAL   B 2 43  ? -16.280 8.492   -10.623 1.00 39.64  ? 52  VAL   B CA  1 
ATOM   759  C C   . VAL   B 2 43  ? -16.970 9.488   -9.660  1.00 47.79  ? 52  VAL   B C   1 
ATOM   760  O O   . VAL   B 2 43  ? -16.790 10.712  -9.842  1.00 42.69  ? 52  VAL   B O   1 
ATOM   761  C CB  . VAL   B 2 43  ? -17.292 7.869   -11.587 1.00 39.45  ? 52  VAL   B CB  1 
ATOM   762  C CG1 . VAL   B 2 43  ? -18.220 8.940   -12.144 1.00 37.78  ? 52  VAL   B CG1 1 
ATOM   763  C CG2 . VAL   B 2 43  ? -16.590 7.109   -12.713 1.00 39.90  ? 52  VAL   B CG2 1 
ATOM   764  N N   . THR   B 2 44  ? -17.761 8.997   -8.691  1.00 40.10  ? 53  THR   B N   1 
ATOM   765  C CA  . THR   B 2 44  ? -18.622 9.857   -7.825  1.00 38.81  ? 53  THR   B CA  1 
ATOM   766  C C   . THR   B 2 44  ? -18.015 10.053  -6.440  1.00 44.57  ? 53  THR   B C   1 
ATOM   767  O O   . THR   B 2 44  ? -18.465 11.002  -5.768  1.00 38.81  ? 53  THR   B O   1 
ATOM   768  C CB  . THR   B 2 44  ? -20.049 9.311   -7.737  1.00 41.29  ? 53  THR   B CB  1 
ATOM   769  O OG1 . THR   B 2 44  ? -20.095 8.036   -7.102  1.00 36.24  ? 53  THR   B OG1 1 
ATOM   770  C CG2 . THR   B 2 44  ? -20.699 9.227   -9.102  1.00 39.54  ? 53  THR   B CG2 1 
ATOM   771  N N   . LYS   B 2 45  ? -17.036 9.218   -6.062  1.00 37.60  ? 54  LYS   B N   1 
ATOM   772  C CA  . LYS   B 2 45  ? -16.585 8.974   -4.668  1.00 41.06  ? 54  LYS   B CA  1 
ATOM   773  C C   . LYS   B 2 45  ? -17.764 8.853   -3.693  1.00 41.87  ? 54  LYS   B C   1 
ATOM   774  O O   . LYS   B 2 45  ? -17.599 9.265   -2.502  1.00 46.13  ? 54  LYS   B O   1 
ATOM   775  C CB  . LYS   B 2 45  ? -15.660 10.088  -4.168  1.00 46.81  ? 54  LYS   B CB  1 
ATOM   776  C CG  . LYS   B 2 45  ? -14.725 10.687  -5.196  1.00 58.36  ? 54  LYS   B CG  1 
ATOM   777  C CD  . LYS   B 2 45  ? -13.439 9.933   -5.383  1.00 61.48  ? 54  LYS   B CD  1 
ATOM   778  C CE  . LYS   B 2 45  ? -12.412 10.835  -6.037  1.00 67.67  ? 54  LYS   B CE  1 
ATOM   779  N NZ  . LYS   B 2 45  ? -11.932 10.256  -7.307  1.00 69.40  ? 54  LYS   B NZ  1 
ATOM   780  N N   . GLY   B 2 46  ? -18.912 8.342   -4.123  1.00 44.97  ? 55  GLY   B N   1 
ATOM   781  C CA  . GLY   B 2 46  ? -20.043 8.054   -3.220  1.00 43.68  ? 55  GLY   B CA  1 
ATOM   782  C C   . GLY   B 2 46  ? -20.956 9.253   -3.038  1.00 48.58  ? 55  GLY   B C   1 
ATOM   783  O O   . GLY   B 2 46  ? -21.897 9.133   -2.267  1.00 48.08  ? 55  GLY   B O   1 
ATOM   784  N N   . ALA   B 2 47  ? -20.730 10.345  -3.770  1.00 47.24  ? 56  ALA   B N   1 
ATOM   785  C CA  . ALA   B 2 47  ? -21.554 11.582  -3.727  1.00 44.87  ? 56  ALA   B CA  1 
ATOM   786  C C   . ALA   B 2 47  ? -22.967 11.337  -4.275  1.00 42.85  ? 56  ALA   B C   1 
ATOM   787  O O   . ALA   B 2 47  ? -23.172 10.532  -5.175  1.00 40.08  ? 56  ALA   B O   1 
ATOM   788  C CB  . ALA   B 2 47  ? -20.860 12.681  -4.486  1.00 45.35  ? 56  ALA   B CB  1 
ATOM   789  N N   . ALA   B 2 48  ? -23.938 12.095  -3.790  1.00 43.21  ? 57  ALA   B N   1 
ATOM   790  C CA  . ALA   B 2 48  ? -25.300 12.120  -4.347  1.00 42.45  ? 57  ALA   B CA  1 
ATOM   791  C C   . ALA   B 2 48  ? -25.226 12.683  -5.753  1.00 36.37  ? 57  ALA   B C   1 
ATOM   792  O O   . ALA   B 2 48  ? -24.292 13.400  -6.016  1.00 40.87  ? 57  ALA   B O   1 
ATOM   793  C CB  . ALA   B 2 48  ? -26.227 12.927  -3.480  1.00 45.95  ? 57  ALA   B CB  1 
ATOM   794  N N   . LEU   B 2 49  ? -26.213 12.389  -6.588  1.00 36.26  ? 58  LEU   B N   1 
ATOM   795  C CA  . LEU   B 2 49  ? -26.270 12.833  -7.999  1.00 42.00  ? 58  LEU   B CA  1 
ATOM   796  C C   . LEU   B 2 49  ? -27.629 13.483  -8.259  1.00 44.74  ? 58  LEU   B C   1 
ATOM   797  O O   . LEU   B 2 49  ? -28.606 13.205  -7.534  1.00 46.63  ? 58  LEU   B O   1 
ATOM   798  C CB  . LEU   B 2 49  ? -26.081 11.638  -8.949  1.00 43.17  ? 58  LEU   B CB  1 
ATOM   799  C CG  . LEU   B 2 49  ? -24.793 10.827  -8.808  1.00 43.20  ? 58  LEU   B CG  1 
ATOM   800  C CD1 . LEU   B 2 49  ? -24.870 9.563   -9.643  1.00 44.66  ? 58  LEU   B CD1 1 
ATOM   801  C CD2 . LEU   B 2 49  ? -23.591 11.633  -9.226  1.00 49.70  ? 58  LEU   B CD2 1 
ATOM   802  N N   . ARG   B 2 50  ? -27.679 14.320  -9.276  1.00 46.03  ? 59  ARG   B N   1 
ATOM   803  C CA  . ARG   B 2 50  ? -28.914 15.001  -9.717  1.00 55.47  ? 59  ARG   B CA  1 
ATOM   804  C C   . ARG   B 2 50  ? -29.312 14.414  -11.074 1.00 54.39  ? 59  ARG   B C   1 
ATOM   805  O O   . ARG   B 2 50  ? -28.412 14.167  -11.899 1.00 53.77  ? 59  ARG   B O   1 
ATOM   806  C CB  . ARG   B 2 50  ? -28.681 16.513  -9.741  1.00 64.23  ? 59  ARG   B CB  1 
ATOM   807  C CG  . ARG   B 2 50  ? -29.860 17.308  -10.284 1.00 75.42  ? 59  ARG   B CG  1 
ATOM   808  C CD  . ARG   B 2 50  ? -29.742 18.813  -10.093 1.00 78.56  ? 59  ARG   B CD  1 
ATOM   809  N NE  . ARG   B 2 50  ? -28.380 19.331  -10.241 1.00 80.84  ? 59  ARG   B NE  1 
ATOM   810  C CZ  . ARG   B 2 50  ? -27.775 19.664  -11.389 1.00 78.28  ? 59  ARG   B CZ  1 
ATOM   811  N NH1 . ARG   B 2 50  ? -28.376 19.522  -12.566 1.00 71.41  ? 59  ARG   B NH1 1 
ATOM   812  N NH2 . ARG   B 2 50  ? -26.542 20.147  -11.341 1.00 76.89  ? 59  ARG   B NH2 1 
ATOM   813  N N   . SER   B 2 51  ? -30.615 14.183  -11.252 1.00 56.03  ? 60  SER   B N   1 
ATOM   814  C CA  . SER   B 2 51  ? -31.278 13.822  -12.528 1.00 58.39  ? 60  SER   B CA  1 
ATOM   815  C C   . SER   B 2 51  ? -32.382 14.849  -12.822 1.00 62.50  ? 60  SER   B C   1 
ATOM   816  O O   . SER   B 2 51  ? -33.545 14.589  -12.460 1.00 70.31  ? 60  SER   B O   1 
ATOM   817  C CB  . SER   B 2 51  ? -31.822 12.411  -12.445 1.00 53.48  ? 60  SER   B CB  1 
ATOM   818  O OG  . SER   B 2 51  ? -32.428 12.022  -13.666 1.00 56.98  ? 60  SER   B OG  1 
ATOM   819  N N   . GLY   B 2 52  ? -32.054 15.960  -13.483 1.00 65.04  ? 61  GLY   B N   1 
ATOM   820  C CA  . GLY   B 2 52  ? -33.010 17.067  -13.675 1.00 67.27  ? 61  GLY   B CA  1 
ATOM   821  C C   . GLY   B 2 52  ? -33.201 17.799  -12.360 1.00 65.18  ? 61  GLY   B C   1 
ATOM   822  O O   . GLY   B 2 52  ? -32.253 18.465  -11.928 1.00 60.54  ? 61  GLY   B O   1 
ATOM   823  N N   . GLU   B 2 53  ? -34.340 17.606  -11.699 1.00 64.63  ? 62  GLU   B N   1 
ATOM   824  C CA  . GLU   B 2 53  ? -34.581 18.144  -10.335 1.00 76.39  ? 62  GLU   B CA  1 
ATOM   825  C C   . GLU   B 2 53  ? -34.559 17.020  -9.285  1.00 74.65  ? 62  GLU   B C   1 
ATOM   826  O O   . GLU   B 2 53  ? -34.338 17.352  -8.114  1.00 82.14  ? 62  GLU   B O   1 
ATOM   827  C CB  . GLU   B 2 53  ? -35.894 18.924  -10.305 1.00 84.50  ? 62  GLU   B CB  1 
ATOM   828  C CG  . GLU   B 2 53  ? -35.697 20.405  -10.560 1.00 91.90  ? 62  GLU   B CG  1 
ATOM   829  C CD  . GLU   B 2 53  ? -36.911 21.257  -10.242 1.00 104.39 ? 62  GLU   B CD  1 
ATOM   830  O OE1 . GLU   B 2 53  ? -37.869 20.712  -9.646  1.00 111.41 ? 62  GLU   B OE1 1 
ATOM   831  O OE2 . GLU   B 2 53  ? -36.889 22.462  -10.577 1.00 108.64 ? 62  GLU   B OE2 1 
ATOM   832  N N   . GLY   B 2 54  ? -34.777 15.758  -9.680  1.00 66.29  ? 63  GLY   B N   1 
ATOM   833  C CA  . GLY   B 2 54  ? -34.647 14.565  -8.817  1.00 66.15  ? 63  GLY   B CA  1 
ATOM   834  C C   . GLY   B 2 54  ? -33.231 14.369  -8.291  1.00 67.39  ? 63  GLY   B C   1 
ATOM   835  O O   . GLY   B 2 54  ? -32.262 14.792  -8.958  1.00 68.77  ? 63  GLY   B O   1 
ATOM   836  N N   . ARG   B 2 55  ? -33.115 13.723  -7.130  1.00 61.52  ? 64  ARG   B N   1 
ATOM   837  C CA  . ARG   B 2 55  ? -31.841 13.437  -6.418  1.00 58.48  ? 64  ARG   B CA  1 
ATOM   838  C C   . ARG   B 2 55  ? -31.654 11.916  -6.362  1.00 59.42  ? 64  ARG   B C   1 
ATOM   839  O O   . ARG   B 2 55  ? -32.593 11.233  -5.971  1.00 59.05  ? 64  ARG   B O   1 
ATOM   840  C CB  . ARG   B 2 55  ? -31.913 14.044  -5.013  1.00 61.37  ? 64  ARG   B CB  1 
ATOM   841  C CG  . ARG   B 2 55  ? -30.701 13.840  -4.115  1.00 60.24  ? 64  ARG   B CG  1 
ATOM   842  C CD  . ARG   B 2 55  ? -31.073 14.117  -2.652  1.00 63.86  ? 64  ARG   B CD  1 
ATOM   843  N NE  . ARG   B 2 55  ? -30.044 13.682  -1.711  1.00 68.66  ? 64  ARG   B NE  1 
ATOM   844  C CZ  . ARG   B 2 55  ? -29.032 14.427  -1.238  1.00 71.21  ? 64  ARG   B CZ  1 
ATOM   845  N NH1 . ARG   B 2 55  ? -28.911 15.693  -1.590  1.00 74.60  ? 64  ARG   B NH1 1 
ATOM   846  N NH2 . ARG   B 2 55  ? -28.150 13.911  -0.392  1.00 67.15  ? 64  ARG   B NH2 1 
ATOM   847  N N   . LEU   B 2 56  ? -30.474 11.420  -6.741  1.00 50.87  ? 65  LEU   B N   1 
ATOM   848  C CA  . LEU   B 2 56  ? -30.096 9.987   -6.653  1.00 44.92  ? 65  LEU   B CA  1 
ATOM   849  C C   . LEU   B 2 56  ? -29.204 9.814   -5.428  1.00 39.91  ? 65  LEU   B C   1 
ATOM   850  O O   . LEU   B 2 56  ? -28.147 10.496  -5.348  1.00 37.69  ? 65  LEU   B O   1 
ATOM   851  C CB  . LEU   B 2 56  ? -29.352 9.556   -7.927  1.00 42.71  ? 65  LEU   B CB  1 
ATOM   852  C CG  . LEU   B 2 56  ? -30.128 9.507   -9.235  1.00 48.49  ? 65  LEU   B CG  1 
ATOM   853  C CD1 . LEU   B 2 56  ? -29.540 8.438   -10.150 1.00 51.98  ? 65  LEU   B CD1 1 
ATOM   854  C CD2 . LEU   B 2 56  ? -31.602 9.240   -9.049  1.00 52.07  ? 65  LEU   B CD2 1 
ATOM   855  N N   . ASP   B 2 57  ? -29.623 8.998   -4.463  1.00 37.46  ? 66  ASP   B N   1 
ATOM   856  C CA  . ASP   B 2 57  ? -28.777 8.747   -3.275  1.00 43.82  ? 66  ASP   B CA  1 
ATOM   857  C C   . ASP   B 2 57  ? -28.044 7.415   -3.412  1.00 38.52  ? 66  ASP   B C   1 
ATOM   858  O O   . ASP   B 2 57  ? -28.662 6.402   -3.769  1.00 35.20  ? 66  ASP   B O   1 
ATOM   859  C CB  . ASP   B 2 57  ? -29.617 8.724   -2.003  1.00 54.09  ? 66  ASP   B CB  1 
ATOM   860  C CG  . ASP   B 2 57  ? -30.180 10.093  -1.669  1.00 62.17  ? 66  ASP   B CG  1 
ATOM   861  O OD1 . ASP   B 2 57  ? -29.512 11.088  -1.980  1.00 56.82  ? 66  ASP   B OD1 1 
ATOM   862  O OD2 . ASP   B 2 57  ? -31.290 10.143  -1.139  1.00 65.52  ? 66  ASP   B OD2 1 
ATOM   863  N N   . PRO   B 2 58  ? -26.775 7.353   -2.955  1.00 39.08  ? 67  PRO   B N   1 
ATOM   864  C CA  . PRO   B 2 58  ? -26.022 6.096   -2.912  1.00 39.88  ? 67  PRO   B CA  1 
ATOM   865  C C   . PRO   B 2 58  ? -26.724 5.086   -2.007  1.00 46.28  ? 67  PRO   B C   1 
ATOM   866  O O   . PRO   B 2 58  ? -27.270 5.449   -0.970  1.00 48.47  ? 67  PRO   B O   1 
ATOM   867  C CB  . PRO   B 2 58  ? -24.652 6.499   -2.386  1.00 40.22  ? 67  PRO   B CB  1 
ATOM   868  C CG  . PRO   B 2 58  ? -24.923 7.756   -1.615  1.00 42.94  ? 67  PRO   B CG  1 
ATOM   869  C CD  . PRO   B 2 58  ? -26.005 8.469   -2.388  1.00 41.07  ? 67  PRO   B CD  1 
ATOM   870  N N   . TYR   B 2 59  ? -26.741 3.834   -2.451  1.00 42.01  ? 68  TYR   B N   1 
ATOM   871  C CA  . TYR   B 2 59  ? -27.434 2.716   -1.787  1.00 35.16  ? 68  TYR   B CA  1 
ATOM   872  C C   . TYR   B 2 59  ? -26.417 1.642   -1.375  1.00 37.24  ? 68  TYR   B C   1 
ATOM   873  O O   . TYR   B 2 59  ? -26.472 1.097   -0.242  1.00 32.67  ? 68  TYR   B O   1 
ATOM   874  C CB  . TYR   B 2 59  ? -28.560 2.237   -2.710  1.00 38.24  ? 68  TYR   B CB  1 
ATOM   875  C CG  . TYR   B 2 59  ? -29.345 1.093   -2.149  1.00 35.90  ? 68  TYR   B CG  1 
ATOM   876  C CD1 . TYR   B 2 59  ? -28.806 -0.181  -2.120  1.00 43.37  ? 68  TYR   B CD1 1 
ATOM   877  C CD2 . TYR   B 2 59  ? -30.577 1.287   -1.559  1.00 39.43  ? 68  TYR   B CD2 1 
ATOM   878  C CE1 . TYR   B 2 59  ? -29.497 -1.245  -1.571  1.00 38.38  ? 68  TYR   B CE1 1 
ATOM   879  C CE2 . TYR   B 2 59  ? -31.297 0.216   -1.060  1.00 41.11  ? 68  TYR   B CE2 1 
ATOM   880  C CZ  . TYR   B 2 59  ? -30.748 -1.050  -1.032  1.00 37.89  ? 68  TYR   B CZ  1 
ATOM   881  O OH  . TYR   B 2 59  ? -31.445 -2.129  -0.524  1.00 36.54  ? 68  TYR   B OH  1 
ATOM   882  N N   . TRP   B 2 60  ? -25.503 1.317   -2.274  1.00 32.64  ? 69  TRP   B N   1 
ATOM   883  C CA  . TRP   B 2 60  ? -24.402 0.350   -2.021  1.00 31.54  ? 69  TRP   B CA  1 
ATOM   884  C C   . TRP   B 2 60  ? -23.108 0.836   -2.672  1.00 34.13  ? 69  TRP   B C   1 
ATOM   885  O O   . TRP   B 2 60  ? -23.169 1.417   -3.756  1.00 37.38  ? 69  TRP   B O   1 
ATOM   886  C CB  . TRP   B 2 60  ? -24.767 -1.018  -2.545  1.00 28.48  ? 69  TRP   B CB  1 
ATOM   887  C CG  . TRP   B 2 60  ? -23.617 -1.965  -2.450  1.00 31.09  ? 69  TRP   B CG  1 
ATOM   888  C CD1 . TRP   B 2 60  ? -23.226 -2.717  -1.380  1.00 32.20  ? 69  TRP   B CD1 1 
ATOM   889  C CD2 . TRP   B 2 60  ? -22.763 -2.332  -3.536  1.00 29.51  ? 69  TRP   B CD2 1 
ATOM   890  N NE1 . TRP   B 2 60  ? -22.115 -3.449  -1.701  1.00 29.75  ? 69  TRP   B NE1 1 
ATOM   891  C CE2 . TRP   B 2 60  ? -21.810 -3.238  -3.022  1.00 30.74  ? 69  TRP   B CE2 1 
ATOM   892  C CE3 . TRP   B 2 60  ? -22.723 -1.983  -4.888  1.00 30.96  ? 69  TRP   B CE3 1 
ATOM   893  C CZ2 . TRP   B 2 60  ? -20.831 -3.808  -3.831  1.00 32.27  ? 69  TRP   B CZ2 1 
ATOM   894  C CZ3 . TRP   B 2 60  ? -21.708 -2.491  -5.677  1.00 33.51  ? 69  TRP   B CZ3 1 
ATOM   895  C CH2 . TRP   B 2 60  ? -20.797 -3.428  -5.161  1.00 33.97  ? 69  TRP   B CH2 1 
ATOM   896  N N   . GLY   B 2 61  ? -21.975 0.492   -2.088  1.00 32.63  ? 70  GLY   B N   1 
ATOM   897  C CA  . GLY   B 2 61  ? -20.674 0.881   -2.631  1.00 35.65  ? 70  GLY   B CA  1 
ATOM   898  C C   . GLY   B 2 61  ? -19.553 0.107   -1.992  1.00 32.43  ? 70  GLY   B C   1 
ATOM   899  O O   . GLY   B 2 61  ? -19.697 -0.239  -0.809  1.00 31.85  ? 70  GLY   B O   1 
ATOM   900  N N   . ASP   B 2 62  ? -18.502 -0.139  -2.749  1.00 30.95  ? 71  ASP   B N   1 
ATOM   901  C CA  . ASP   B 2 62  ? -17.273 -0.865  -2.326  1.00 30.47  ? 71  ASP   B CA  1 
ATOM   902  C C   . ASP   B 2 62  ? -16.050 -0.273  -3.039  1.00 33.10  ? 71  ASP   B C   1 
ATOM   903  O O   . ASP   B 2 62  ? -15.906 -0.471  -4.244  1.00 36.60  ? 71  ASP   B O   1 
ATOM   904  C CB  . ASP   B 2 62  ? -17.415 -2.342  -2.593  1.00 32.96  ? 71  ASP   B CB  1 
ATOM   905  C CG  . ASP   B 2 62  ? -16.322 -3.173  -1.922  1.00 43.77  ? 71  ASP   B CG  1 
ATOM   906  O OD1 . ASP   B 2 62  ? -15.144 -3.017  -2.268  1.00 42.65  ? 71  ASP   B OD1 1 
ATOM   907  O OD2 . ASP   B 2 62  ? -16.654 -3.907  -1.002  1.00 48.65  ? 71  ASP   B OD2 1 
ATOM   908  N N   . VAL   B 2 63  ? -15.168 0.399   -2.318  1.00 31.34  ? 72  VAL   B N   1 
ATOM   909  C CA  . VAL   B 2 63  ? -13.936 0.977   -2.895  1.00 32.68  ? 72  VAL   B CA  1 
ATOM   910  C C   . VAL   B 2 63  ? -13.065 -0.121  -3.532  1.00 39.59  ? 72  VAL   B C   1 
ATOM   911  O O   . VAL   B 2 63  ? -12.353 0.182   -4.568  1.00 34.68  ? 72  VAL   B O   1 
ATOM   912  C CB  . VAL   B 2 63  ? -13.166 1.807   -1.859  1.00 33.97  ? 72  VAL   B CB  1 
ATOM   913  C CG1 . VAL   B 2 63  ? -11.705 1.988   -2.194  1.00 35.72  ? 72  VAL   B CG1 1 
ATOM   914  C CG2 . VAL   B 2 63  ? -13.832 3.151   -1.673  1.00 35.57  ? 72  VAL   B CG2 1 
ATOM   915  N N   . LYS   B 2 64  ? -13.109 -1.355  -3.050  1.00 33.68  ? 73  LYS   B N   1 
ATOM   916  C CA  . LYS   B 2 64  ? -12.151 -2.377  -3.592  1.00 38.98  ? 73  LYS   B CA  1 
ATOM   917  C C   . LYS   B 2 64  ? -12.695 -2.971  -4.903  1.00 35.92  ? 73  LYS   B C   1 
ATOM   918  O O   . LYS   B 2 64  ? -11.883 -3.153  -5.826  1.00 41.65  ? 73  LYS   B O   1 
ATOM   919  C CB  . LYS   B 2 64  ? -11.790 -3.459  -2.576  1.00 39.36  ? 73  LYS   B CB  1 
ATOM   920  C CG  . LYS   B 2 64  ? -10.817 -4.504  -3.112  1.00 41.81  ? 73  LYS   B CG  1 
ATOM   921  C CD  . LYS   B 2 64  ? -10.373 -5.501  -2.050  1.00 42.98  ? 73  LYS   B CD  1 
ATOM   922  C CE  . LYS   B 2 64  ? -9.522  -6.596  -2.661  1.00 51.27  ? 73  LYS   B CE  1 
ATOM   923  N NZ  . LYS   B 2 64  ? -8.906  -7.474  -1.642  1.00 57.46  ? 73  LYS   B NZ  1 
ATOM   924  N N   . GLN   B 2 65  ? -13.997 -3.269  -5.000  1.00 37.41  ? 74  GLN   B N   1 
ATOM   925  C CA  . GLN   B 2 65  ? -14.662 -3.582  -6.283  1.00 36.71  ? 74  GLN   B CA  1 
ATOM   926  C C   . GLN   B 2 65  ? -14.671 -2.381  -7.238  1.00 36.83  ? 74  GLN   B C   1 
ATOM   927  O O   . GLN   B 2 65  ? -14.833 -2.645  -8.476  1.00 35.48  ? 74  GLN   B O   1 
ATOM   928  C CB  . GLN   B 2 65  ? -16.087 -4.061  -6.078  1.00 36.82  ? 74  GLN   B CB  1 
ATOM   929  C CG  . GLN   B 2 65  ? -16.120 -5.430  -5.414  1.00 42.78  ? 74  GLN   B CG  1 
ATOM   930  C CD  . GLN   B 2 65  ? -17.542 -5.919  -5.278  1.00 44.44  ? 74  GLN   B CD  1 
ATOM   931  O OE1 . GLN   B 2 65  ? -18.306 -6.019  -6.240  1.00 46.61  ? 74  GLN   B OE1 1 
ATOM   932  N NE2 . GLN   B 2 65  ? -17.937 -6.153  -4.047  1.00 49.31  ? 74  GLN   B NE2 1 
ATOM   933  N N   . ASP   B 2 66  ? -14.517 -1.168  -6.700  1.00 36.64  ? 75  ASP   B N   1 
ATOM   934  C CA  . ASP   B 2 66  ? -14.643 0.174   -7.351  1.00 42.45  ? 75  ASP   B CA  1 
ATOM   935  C C   . ASP   B 2 66  ? -16.018 0.301   -7.998  1.00 42.40  ? 75  ASP   B C   1 
ATOM   936  O O   . ASP   B 2 66  ? -16.059 0.736   -9.150  1.00 36.14  ? 75  ASP   B O   1 
ATOM   937  C CB  . ASP   B 2 66  ? -13.572 0.420   -8.419  1.00 44.29  ? 75  ASP   B CB  1 
ATOM   938  C CG  . ASP   B 2 66  ? -13.417 1.867   -8.900  1.00 46.82  ? 75  ASP   B CG  1 
ATOM   939  O OD1 . ASP   B 2 66  ? -13.644 2.828   -8.116  1.00 38.58  ? 75  ASP   B OD1 1 
ATOM   940  O OD2 . ASP   B 2 66  ? -12.967 2.033   -10.036 1.00 44.67  ? 75  ASP   B OD2 1 
ATOM   941  N N   . LEU   B 2 67  ? -17.085 -0.126  -7.306  1.00 33.25  ? 76  LEU   B N   1 
ATOM   942  C CA  . LEU   B 2 67  ? -18.489 -0.037  -7.792  1.00 33.17  ? 76  LEU   B CA  1 
ATOM   943  C C   . LEU   B 2 67  ? -19.350 0.747   -6.795  1.00 36.02  ? 76  LEU   B C   1 
ATOM   944  O O   . LEU   B 2 67  ? -19.008 0.737   -5.562  1.00 38.30  ? 76  LEU   B O   1 
ATOM   945  C CB  . LEU   B 2 67  ? -19.041 -1.449  -7.970  1.00 32.33  ? 76  LEU   B CB  1 
ATOM   946  C CG  . LEU   B 2 67  ? -18.335 -2.323  -9.047  1.00 31.67  ? 76  LEU   B CG  1 
ATOM   947  C CD1 . LEU   B 2 67  ? -19.064 -3.665  -9.164  1.00 29.99  ? 76  LEU   B CD1 1 
ATOM   948  C CD2 . LEU   B 2 67  ? -18.328 -1.596  -10.399 1.00 34.22  ? 76  LEU   B CD2 1 
ATOM   949  N N   . VAL   B 2 68  ? -20.445 1.320   -7.300  1.00 35.40  ? 77  VAL   B N   1 
ATOM   950  C CA  . VAL   B 2 68  ? -21.482 2.038   -6.491  1.00 39.13  ? 77  VAL   B CA  1 
ATOM   951  C C   . VAL   B 2 68  ? -22.827 1.943   -7.188  1.00 33.44  ? 77  VAL   B C   1 
ATOM   952  O O   . VAL   B 2 68  ? -22.891 2.065   -8.449  1.00 35.17  ? 77  VAL   B O   1 
ATOM   953  C CB  . VAL   B 2 68  ? -21.086 3.505   -6.200  1.00 37.38  ? 77  VAL   B CB  1 
ATOM   954  C CG1 . VAL   B 2 68  ? -20.875 4.346   -7.464  1.00 39.87  ? 77  VAL   B CG1 1 
ATOM   955  C CG2 . VAL   B 2 68  ? -22.113 4.177   -5.285  1.00 35.88  ? 77  VAL   B CG2 1 
ATOM   956  N N   . SER   B 2 69  ? -23.900 1.745   -6.437  1.00 31.36  ? 78  SER   B N   1 
ATOM   957  C CA  . SER   B 2 69  ? -25.284 1.789   -6.983  1.00 31.06  ? 78  SER   B CA  1 
ATOM   958  C C   . SER   B 2 69  ? -26.107 2.884   -6.268  1.00 32.68  ? 78  SER   B C   1 
ATOM   959  O O   . SER   B 2 69  ? -25.860 3.142   -5.039  1.00 30.71  ? 78  SER   B O   1 
ATOM   960  C CB  . SER   B 2 69  ? -25.956 0.450   -6.901  1.00 30.57  ? 78  SER   B CB  1 
ATOM   961  O OG  . SER   B 2 69  ? -26.194 0.076   -5.551  1.00 34.37  ? 78  SER   B OG  1 
ATOM   962  N N   . TYR   B 2 70  ? -27.060 3.459   -6.990  1.00 35.55  ? 79  TYR   B N   1 
ATOM   963  C CA  . TYR   B 2 70  ? -27.970 4.576   -6.569  1.00 33.73  ? 79  TYR   B CA  1 
ATOM   964  C C   . TYR   B 2 70  ? -29.415 4.082   -6.649  1.00 35.34  ? 79  TYR   B C   1 
ATOM   965  O O   . TYR   B 2 70  ? -29.824 3.450   -7.662  1.00 33.20  ? 79  TYR   B O   1 
ATOM   966  C CB  . TYR   B 2 70  ? -27.757 5.853   -7.393  1.00 33.30  ? 79  TYR   B CB  1 
ATOM   967  C CG  . TYR   B 2 70  ? -26.434 6.522   -7.125  1.00 32.24  ? 79  TYR   B CG  1 
ATOM   968  C CD1 . TYR   B 2 70  ? -25.261 6.006   -7.675  1.00 34.48  ? 79  TYR   B CD1 1 
ATOM   969  C CD2 . TYR   B 2 70  ? -26.315 7.626   -6.301  1.00 32.26  ? 79  TYR   B CD2 1 
ATOM   970  C CE1 . TYR   B 2 70  ? -24.026 6.578   -7.420  1.00 34.06  ? 79  TYR   B CE1 1 
ATOM   971  C CE2 . TYR   B 2 70  ? -25.094 8.208   -6.040  1.00 36.84  ? 79  TYR   B CE2 1 
ATOM   972  C CZ  . TYR   B 2 70  ? -23.932 7.670   -6.580  1.00 33.93  ? 79  TYR   B CZ  1 
ATOM   973  O OH  . TYR   B 2 70  ? -22.715 8.225   -6.308  1.00 34.29  ? 79  TYR   B OH  1 
ATOM   974  N N   . CYS   B 2 71  ? -30.188 4.376   -5.579  1.00 38.54  ? 80  CYS   B N   1 
ATOM   975  C CA  . CYS   B 2 71  ? -31.669 4.146   -5.480  1.00 38.74  ? 80  CYS   B CA  1 
ATOM   976  C C   . CYS   B 2 71  ? -32.020 2.692   -5.215  1.00 42.41  ? 80  CYS   B C   1 
ATOM   977  O O   . CYS   B 2 71  ? -33.212 2.388   -5.067  1.00 43.19  ? 80  CYS   B O   1 
ATOM   978  C CB  . CYS   B 2 71  ? -32.415 4.528   -6.748  1.00 36.50  ? 80  CYS   B CB  1 
ATOM   979  S SG  . CYS   B 2 71  ? -31.923 6.168   -7.320  1.00 46.63  ? 80  CYS   B SG  1 
ATOM   980  N N   . GLY   B 2 72  ? -31.032 1.801   -5.191  1.00 39.58  ? 81  GLY   B N   1 
ATOM   981  C CA  . GLY   B 2 72  ? -31.342 0.386   -5.039  1.00 35.11  ? 81  GLY   B CA  1 
ATOM   982  C C   . GLY   B 2 72  ? -30.092 -0.462  -5.173  1.00 32.19  ? 81  GLY   B C   1 
ATOM   983  O O   . GLY   B 2 72  ? -28.990 0.037   -5.370  1.00 34.10  ? 81  GLY   B O   1 
ATOM   984  N N   . PRO   B 2 73  ? -30.223 -1.756  -4.881  1.00 35.15  ? 82  PRO   B N   1 
ATOM   985  C CA  . PRO   B 2 73  ? -29.087 -2.675  -4.883  1.00 36.91  ? 82  PRO   B CA  1 
ATOM   986  C C   . PRO   B 2 73  ? -28.584 -2.934  -6.312  1.00 36.25  ? 82  PRO   B C   1 
ATOM   987  O O   . PRO   B 2 73  ? -29.391 -2.761  -7.208  1.00 36.97  ? 82  PRO   B O   1 
ATOM   988  C CB  . PRO   B 2 73  ? -29.676 -3.934  -4.268  1.00 35.15  ? 82  PRO   B CB  1 
ATOM   989  C CG  . PRO   B 2 73  ? -31.138 -3.845  -4.476  1.00 35.83  ? 82  PRO   B CG  1 
ATOM   990  C CD  . PRO   B 2 73  ? -31.470 -2.382  -4.468  1.00 36.34  ? 82  PRO   B CD  1 
ATOM   991  N N   . TRP   B 2 74  ? -27.322 -3.357  -6.467  1.00 37.58  ? 83  TRP   B N   1 
ATOM   992  C CA  . TRP   B 2 74  ? -26.689 -3.682  -7.775  1.00 37.13  ? 83  TRP   B CA  1 
ATOM   993  C C   . TRP   B 2 74  ? -27.559 -4.697  -8.520  1.00 35.72  ? 83  TRP   B C   1 
ATOM   994  O O   . TRP   B 2 74  ? -27.941 -5.700  -7.918  1.00 38.29  ? 83  TRP   B O   1 
ATOM   995  C CB  . TRP   B 2 74  ? -25.261 -4.186  -7.558  1.00 39.93  ? 83  TRP   B CB  1 
ATOM   996  C CG  . TRP   B 2 74  ? -24.498 -4.343  -8.834  1.00 33.72  ? 83  TRP   B CG  1 
ATOM   997  C CD1 . TRP   B 2 74  ? -24.486 -5.434  -9.660  1.00 34.16  ? 83  TRP   B CD1 1 
ATOM   998  C CD2 . TRP   B 2 74  ? -23.650 -3.355  -9.440  1.00 36.14  ? 83  TRP   B CD2 1 
ATOM   999  N NE1 . TRP   B 2 74  ? -23.699 -5.184  -10.744 1.00 33.26  ? 83  TRP   B NE1 1 
ATOM   1000 C CE2 . TRP   B 2 74  ? -23.166 -3.924  -10.638 1.00 35.03  ? 83  TRP   B CE2 1 
ATOM   1001 C CE3 . TRP   B 2 74  ? -23.249 -2.051  -9.097  1.00 35.34  ? 83  TRP   B CE3 1 
ATOM   1002 C CZ2 . TRP   B 2 74  ? -22.340 -3.215  -11.503 1.00 33.15  ? 83  TRP   B CZ2 1 
ATOM   1003 C CZ3 . TRP   B 2 74  ? -22.413 -1.359  -9.938  1.00 33.93  ? 83  TRP   B CZ3 1 
ATOM   1004 C CH2 . TRP   B 2 74  ? -21.922 -1.963  -11.104 1.00 37.73  ? 83  TRP   B CH2 1 
ATOM   1005 N N   . LYS   B 2 75  ? -27.894 -4.445  -9.787  1.00 34.89  ? 84  LYS   B N   1 
ATOM   1006 C CA  . LYS   B 2 75  ? -28.907 -5.260  -10.519 1.00 36.45  ? 84  LYS   B CA  1 
ATOM   1007 C C   . LYS   B 2 75  ? -28.259 -6.071  -11.656 1.00 38.69  ? 84  LYS   B C   1 
ATOM   1008 O O   . LYS   B 2 75  ? -28.965 -6.934  -12.177 1.00 42.57  ? 84  LYS   B O   1 
ATOM   1009 C CB  . LYS   B 2 75  ? -29.980 -4.373  -11.162 1.00 42.85  ? 84  LYS   B CB  1 
ATOM   1010 C CG  . LYS   B 2 75  ? -30.765 -3.463  -10.217 1.00 42.78  ? 84  LYS   B CG  1 
ATOM   1011 C CD  . LYS   B 2 75  ? -31.818 -4.236  -9.484  1.00 47.60  ? 84  LYS   B CD  1 
ATOM   1012 C CE  . LYS   B 2 75  ? -32.684 -3.376  -8.591  1.00 58.23  ? 84  LYS   B CE  1 
ATOM   1013 N NZ  . LYS   B 2 75  ? -33.677 -4.232  -7.910  1.00 61.11  ? 84  LYS   B NZ  1 
ATOM   1014 N N   . LEU   B 2 76  ? -27.041 -5.740  -12.094 1.00 37.38  ? 85  LEU   B N   1 
ATOM   1015 C CA  . LEU   B 2 76  ? -26.386 -6.310  -13.308 1.00 41.29  ? 85  LEU   B CA  1 
ATOM   1016 C C   . LEU   B 2 76  ? -25.651 -7.589  -12.895 1.00 43.22  ? 85  LEU   B C   1 
ATOM   1017 O O   . LEU   B 2 76  ? -24.774 -7.500  -12.052 1.00 44.65  ? 85  LEU   B O   1 
ATOM   1018 C CB  . LEU   B 2 76  ? -25.405 -5.290  -13.885 1.00 41.34  ? 85  LEU   B CB  1 
ATOM   1019 C CG  . LEU   B 2 76  ? -25.965 -3.875  -14.109 1.00 39.30  ? 85  LEU   B CG  1 
ATOM   1020 C CD1 . LEU   B 2 76  ? -24.865 -2.920  -14.547 1.00 36.90  ? 85  LEU   B CD1 1 
ATOM   1021 C CD2 . LEU   B 2 76  ? -27.093 -3.886  -15.111 1.00 41.97  ? 85  LEU   B CD2 1 
ATOM   1022 N N   . ASP   B 2 77  ? -26.028 -8.744  -13.432 1.00 51.16  ? 86  ASP   B N   1 
ATOM   1023 C CA  . ASP   B 2 77  ? -25.440 -10.036 -12.978 1.00 56.72  ? 86  ASP   B CA  1 
ATOM   1024 C C   . ASP   B 2 77  ? -24.991 -10.886 -14.166 1.00 54.22  ? 86  ASP   B C   1 
ATOM   1025 O O   . ASP   B 2 77  ? -24.579 -12.016 -13.936 1.00 53.05  ? 86  ASP   B O   1 
ATOM   1026 C CB  . ASP   B 2 77  ? -26.416 -10.843 -12.116 1.00 57.25  ? 86  ASP   B CB  1 
ATOM   1027 C CG  . ASP   B 2 77  ? -27.721 -11.141 -12.818 1.00 65.56  ? 86  ASP   B CG  1 
ATOM   1028 O OD1 . ASP   B 2 77  ? -27.925 -10.613 -13.918 1.00 73.24  ? 86  ASP   B OD1 1 
ATOM   1029 O OD2 . ASP   B 2 77  ? -28.531 -11.883 -12.249 1.00 79.09  ? 86  ASP   B OD2 1 
ATOM   1030 N N   . ALA   B 2 78  ? -25.028 -10.383 -15.390 1.00 48.83  ? 87  ALA   B N   1 
ATOM   1031 C CA  . ALA   B 2 78  ? -24.492 -11.136 -16.533 1.00 41.89  ? 87  ALA   B CA  1 
ATOM   1032 C C   . ALA   B 2 78  ? -22.961 -11.146 -16.444 1.00 42.94  ? 87  ALA   B C   1 
ATOM   1033 O O   . ALA   B 2 78  ? -22.342 -10.129 -15.985 1.00 37.86  ? 87  ALA   B O   1 
ATOM   1034 C CB  . ALA   B 2 78  ? -25.023 -10.577 -17.851 1.00 40.55  ? 87  ALA   B CB  1 
ATOM   1035 N N   . ALA   B 2 79  ? -22.342 -12.210 -16.997 1.00 43.95  ? 88  ALA   B N   1 
ATOM   1036 C CA  . ALA   B 2 79  ? -20.880 -12.453 -16.980 1.00 46.46  ? 88  ALA   B CA  1 
ATOM   1037 C C   . ALA   B 2 79  ? -20.356 -12.843 -18.368 1.00 37.03  ? 88  ALA   B C   1 
ATOM   1038 O O   . ALA   B 2 79  ? -21.099 -13.494 -19.096 1.00 40.89  ? 88  ALA   B O   1 
ATOM   1039 C CB  . ALA   B 2 79  ? -20.609 -13.549 -15.991 1.00 54.27  ? 88  ALA   B CB  1 
ATOM   1040 N N   . TRP   B 2 80  ? -19.174 -12.369 -18.743 1.00 35.17  ? 89  TRP   B N   1 
ATOM   1041 C CA  . TRP   B 2 80  ? -18.390 -12.881 -19.914 1.00 46.00  ? 89  TRP   B CA  1 
ATOM   1042 C C   . TRP   B 2 80  ? -18.380 -14.418 -19.871 1.00 51.41  ? 89  TRP   B C   1 
ATOM   1043 O O   . TRP   B 2 80  ? -18.240 -14.961 -18.731 1.00 43.02  ? 89  TRP   B O   1 
ATOM   1044 C CB  . TRP   B 2 80  ? -16.973 -12.287 -19.951 1.00 51.27  ? 89  TRP   B CB  1 
ATOM   1045 C CG  . TRP   B 2 80  ? -16.169 -12.697 -21.151 1.00 53.21  ? 89  TRP   B CG  1 
ATOM   1046 C CD1 . TRP   B 2 80  ? -16.639 -12.885 -22.414 1.00 51.60  ? 89  TRP   B CD1 1 
ATOM   1047 C CD2 . TRP   B 2 80  ? -14.758 -12.989 -21.210 1.00 54.14  ? 89  TRP   B CD2 1 
ATOM   1048 N NE1 . TRP   B 2 80  ? -15.631 -13.283 -23.246 1.00 53.02  ? 89  TRP   B NE1 1 
ATOM   1049 C CE2 . TRP   B 2 80  ? -14.464 -13.359 -22.542 1.00 51.34  ? 89  TRP   B CE2 1 
ATOM   1050 C CE3 . TRP   B 2 80  ? -13.719 -13.029 -20.272 1.00 53.49  ? 89  TRP   B CE3 1 
ATOM   1051 C CZ2 . TRP   B 2 80  ? -13.183 -13.728 -22.954 1.00 50.90  ? 89  TRP   B CZ2 1 
ATOM   1052 C CZ3 . TRP   B 2 80  ? -12.446 -13.375 -20.688 1.00 53.72  ? 89  TRP   B CZ3 1 
ATOM   1053 C CH2 . TRP   B 2 80  ? -12.176 -13.704 -22.018 1.00 46.20  ? 89  TRP   B CH2 1 
ATOM   1054 N N   . ASP   B 2 81  ? -18.622 -15.080 -21.022 1.00 48.92  ? 90  ASP   B N   1 
ATOM   1055 C CA  . ASP   B 2 81  ? -18.734 -16.562 -21.146 1.00 53.18  ? 90  ASP   B CA  1 
ATOM   1056 C C   . ASP   B 2 81  ? -17.322 -17.195 -21.139 1.00 54.98  ? 90  ASP   B C   1 
ATOM   1057 O O   . ASP   B 2 81  ? -17.248 -18.431 -20.969 1.00 64.80  ? 90  ASP   B O   1 
ATOM   1058 C CB  . ASP   B 2 81  ? -19.562 -16.978 -22.377 1.00 48.33  ? 90  ASP   B CB  1 
ATOM   1059 C CG  . ASP   B 2 81  ? -18.965 -16.580 -23.709 1.00 46.60  ? 90  ASP   B CG  1 
ATOM   1060 O OD1 . ASP   B 2 81  ? -17.859 -15.961 -23.716 1.00 54.36  ? 90  ASP   B OD1 1 
ATOM   1061 O OD2 . ASP   B 2 81  ? -19.595 -16.894 -24.761 1.00 56.70  ? 90  ASP   B OD2 1 
ATOM   1062 N N   . GLY   B 2 82  ? -16.265 -16.388 -21.299 1.00 49.02  ? 91  GLY   B N   1 
ATOM   1063 C CA  . GLY   B 2 82  ? -14.849 -16.794 -21.356 1.00 50.22  ? 91  GLY   B CA  1 
ATOM   1064 C C   . GLY   B 2 82  ? -14.374 -17.051 -22.781 1.00 55.65  ? 91  GLY   B C   1 
ATOM   1065 O O   . GLY   B 2 82  ? -13.180 -17.339 -22.951 1.00 52.52  ? 91  GLY   B O   1 
ATOM   1066 N N   . LEU   B 2 83  ? -15.263 -16.921 -23.771 1.00 54.55  ? 92  LEU   B N   1 
ATOM   1067 C CA  . LEU   B 2 83  ? -15.050 -17.334 -25.186 1.00 54.41  ? 92  LEU   B CA  1 
ATOM   1068 C C   . LEU   B 2 83  ? -15.320 -16.190 -26.185 1.00 62.25  ? 92  LEU   B C   1 
ATOM   1069 O O   . LEU   B 2 83  ? -14.442 -15.916 -27.039 1.00 49.12  ? 92  LEU   B O   1 
ATOM   1070 C CB  . LEU   B 2 83  ? -16.003 -18.502 -25.432 1.00 60.53  ? 92  LEU   B CB  1 
ATOM   1071 C CG  . LEU   B 2 83  ? -15.499 -19.854 -24.939 1.00 65.67  ? 92  LEU   B CG  1 
ATOM   1072 C CD1 . LEU   B 2 83  ? -16.448 -20.965 -25.367 1.00 63.86  ? 92  LEU   B CD1 1 
ATOM   1073 C CD2 . LEU   B 2 83  ? -14.077 -20.115 -25.440 1.00 58.97  ? 92  LEU   B CD2 1 
ATOM   1074 N N   . SER   B 2 84  ? -16.486 -15.530 -26.098 1.00 62.11  ? 93  SER   B N   1 
ATOM   1075 C CA  . SER   B 2 84  ? -17.057 -14.703 -27.196 1.00 50.18  ? 93  SER   B CA  1 
ATOM   1076 C C   . SER   B 2 84  ? -16.481 -13.287 -27.192 1.00 55.36  ? 93  SER   B C   1 
ATOM   1077 O O   . SER   B 2 84  ? -15.969 -12.838 -26.136 1.00 56.87  ? 93  SER   B O   1 
ATOM   1078 C CB  . SER   B 2 84  ? -18.526 -14.712 -27.102 1.00 50.39  ? 93  SER   B CB  1 
ATOM   1079 O OG  . SER   B 2 84  ? -18.982 -16.008 -26.738 1.00 55.35  ? 93  SER   B OG  1 
ATOM   1080 N N   . GLU   B 2 85  ? -16.504 -12.622 -28.352 1.00 50.24  ? 94  GLU   B N   1 
ATOM   1081 C CA  . GLU   B 2 85  ? -16.190 -11.167 -28.486 1.00 55.43  ? 94  GLU   B CA  1 
ATOM   1082 C C   . GLU   B 2 85  ? -17.227 -10.401 -27.638 1.00 41.74  ? 94  GLU   B C   1 
ATOM   1083 O O   . GLU   B 2 85  ? -18.287 -10.993 -27.350 1.00 33.29  ? 94  GLU   B O   1 
ATOM   1084 C CB  . GLU   B 2 85  ? -16.194 -10.720 -29.958 1.00 61.50  ? 94  GLU   B CB  1 
ATOM   1085 C CG  . GLU   B 2 85  ? -15.187 -11.469 -30.835 1.00 73.41  ? 94  GLU   B CG  1 
ATOM   1086 C CD  . GLU   B 2 85  ? -14.439 -10.650 -31.883 1.00 74.71  ? 94  GLU   B CD  1 
ATOM   1087 O OE1 . GLU   B 2 85  ? -15.028 -9.698  -32.423 1.00 64.28  ? 94  GLU   B OE1 1 
ATOM   1088 O OE2 . GLU   B 2 85  ? -13.251 -10.955 -32.152 1.00 75.03  ? 94  GLU   B OE2 1 
ATOM   1089 N N   . VAL   B 2 86  ? -16.875 -9.215  -27.153 1.00 41.79  ? 95  VAL   B N   1 
ATOM   1090 C CA  . VAL   B 2 86  ? -17.805 -8.301  -26.394 1.00 43.95  ? 95  VAL   B CA  1 
ATOM   1091 C C   . VAL   B 2 86  ? -17.930 -6.946  -27.120 1.00 45.47  ? 95  VAL   B C   1 
ATOM   1092 O O   . VAL   B 2 86  ? -17.051 -6.628  -27.960 1.00 46.74  ? 95  VAL   B O   1 
ATOM   1093 C CB  . VAL   B 2 86  ? -17.302 -8.098  -24.936 1.00 31.54  ? 95  VAL   B CB  1 
ATOM   1094 C CG1 . VAL   B 2 86  ? -17.152 -9.406  -24.251 1.00 35.06  ? 95  VAL   B CG1 1 
ATOM   1095 C CG2 . VAL   B 2 86  ? -15.997 -7.317  -24.850 1.00 32.02  ? 95  VAL   B CG2 1 
ATOM   1096 N N   . GLN   B 2 87  ? -18.849 -6.070  -26.695 1.00 47.15  ? 96  GLN   B N   1 
ATOM   1097 C CA  . GLN   B 2 87  ? -18.745 -4.628  -27.079 1.00 43.10  ? 96  GLN   B CA  1 
ATOM   1098 C C   . GLN   B 2 87  ? -18.638 -3.703  -25.861 1.00 34.84  ? 96  GLN   B C   1 
ATOM   1099 O O   . GLN   B 2 87  ? -19.454 -3.845  -24.933 1.00 40.47  ? 96  GLN   B O   1 
ATOM   1100 C CB  . GLN   B 2 87  ? -19.952 -4.271  -27.955 1.00 43.69  ? 96  GLN   B CB  1 
ATOM   1101 C CG  . GLN   B 2 87  ? -19.983 -5.100  -29.238 1.00 47.84  ? 96  GLN   B CG  1 
ATOM   1102 C CD  . GLN   B 2 87  ? -20.887 -4.579  -30.328 1.00 51.38  ? 96  GLN   B CD  1 
ATOM   1103 O OE1 . GLN   B 2 87  ? -21.611 -3.597  -30.164 1.00 46.38  ? 96  GLN   B OE1 1 
ATOM   1104 N NE2 . GLN   B 2 87  ? -20.880 -5.276  -31.456 1.00 48.47  ? 96  GLN   B NE2 1 
ATOM   1105 N N   . LEU   B 2 88  ? -17.642 -2.824  -25.890 1.00 32.56  ? 97  LEU   B N   1 
ATOM   1106 C CA  . LEU   B 2 88  ? -17.554 -1.629  -25.041 1.00 36.43  ? 97  LEU   B CA  1 
ATOM   1107 C C   . LEU   B 2 88  ? -18.413 -0.518  -25.657 1.00 44.88  ? 97  LEU   B C   1 
ATOM   1108 O O   . LEU   B 2 88  ? -18.112 -0.057  -26.822 1.00 43.33  ? 97  LEU   B O   1 
ATOM   1109 C CB  . LEU   B 2 88  ? -16.122 -1.152  -24.971 1.00 36.21  ? 97  LEU   B CB  1 
ATOM   1110 C CG  . LEU   B 2 88  ? -15.958 0.151   -24.215 1.00 39.26  ? 97  LEU   B CG  1 
ATOM   1111 C CD1 . LEU   B 2 88  ? -16.338 -0.011  -22.739 1.00 44.35  ? 97  LEU   B CD1 1 
ATOM   1112 C CD2 . LEU   B 2 88  ? -14.554 0.672   -24.357 1.00 40.42  ? 97  LEU   B CD2 1 
ATOM   1113 N N   . LEU   B 2 89  ? -19.472 -0.139  -24.967 1.00 40.90  ? 98  LEU   B N   1 
ATOM   1114 C CA  . LEU   B 2 89  ? -20.309 1.016   -25.392 1.00 34.45  ? 98  LEU   B CA  1 
ATOM   1115 C C   . LEU   B 2 89  ? -19.650 2.216   -24.792 1.00 38.64  ? 98  LEU   B C   1 
ATOM   1116 O O   . LEU   B 2 89  ? -20.079 2.638   -23.677 1.00 38.64  ? 98  LEU   B O   1 
ATOM   1117 C CB  . LEU   B 2 89  ? -21.737 0.795   -24.916 1.00 43.35  ? 98  LEU   B CB  1 
ATOM   1118 C CG  . LEU   B 2 89  ? -22.757 1.911   -25.210 1.00 48.58  ? 98  LEU   B CG  1 
ATOM   1119 C CD1 . LEU   B 2 89  ? -22.689 2.371   -26.646 1.00 57.01  ? 98  LEU   B CD1 1 
ATOM   1120 C CD2 . LEU   B 2 89  ? -24.154 1.405   -24.906 1.00 49.11  ? 98  LEU   B CD2 1 
ATOM   1121 N N   . ALA   B 2 90  ? -18.588 2.674   -25.454 1.00 34.81  ? 99  ALA   B N   1 
ATOM   1122 C CA  . ALA   B 2 90  ? -17.792 3.827   -25.005 1.00 36.85  ? 99  ALA   B CA  1 
ATOM   1123 C C   . ALA   B 2 90  ? -18.664 5.075   -25.098 1.00 45.85  ? 99  ALA   B C   1 
ATOM   1124 O O   . ALA   B 2 90  ? -19.320 5.267   -26.146 1.00 49.00  ? 99  ALA   B O   1 
ATOM   1125 C CB  . ALA   B 2 90  ? -16.541 4.011   -25.810 1.00 35.54  ? 99  ALA   B CB  1 
ATOM   1126 N N   . VAL   B 2 91  ? -18.664 5.876   -24.039 1.00 43.84  ? 100 VAL   B N   1 
ATOM   1127 C CA  . VAL   B 2 91  ? -19.257 7.235   -24.032 1.00 38.44  ? 100 VAL   B CA  1 
ATOM   1128 C C   . VAL   B 2 91  ? -18.171 8.227   -23.652 1.00 40.34  ? 100 VAL   B C   1 
ATOM   1129 O O   . VAL   B 2 91  ? -18.027 8.608   -22.494 1.00 45.78  ? 100 VAL   B O   1 
ATOM   1130 C CB  . VAL   B 2 91  ? -20.473 7.278   -23.114 1.00 44.25  ? 100 VAL   B CB  1 
ATOM   1131 C CG1 . VAL   B 2 91  ? -21.049 8.690   -23.087 1.00 46.88  ? 100 VAL   B CG1 1 
ATOM   1132 C CG2 . VAL   B 2 91  ? -21.533 6.240   -23.521 1.00 40.39  ? 100 VAL   B CG2 1 
ATOM   1133 N N   . PRO   B 2 92  ? -17.336 8.675   -24.622 1.00 40.97  ? 101 PRO   B N   1 
ATOM   1134 C CA  . PRO   B 2 92  ? -16.252 9.612   -24.330 1.00 39.04  ? 101 PRO   B CA  1 
ATOM   1135 C C   . PRO   B 2 92  ? -16.774 11.020  -24.082 1.00 41.66  ? 101 PRO   B C   1 
ATOM   1136 O O   . PRO   B 2 92  ? -17.827 11.379  -24.631 1.00 44.63  ? 101 PRO   B O   1 
ATOM   1137 C CB  . PRO   B 2 92  ? -15.374 9.556   -25.593 1.00 42.52  ? 101 PRO   B CB  1 
ATOM   1138 C CG  . PRO   B 2 92  ? -15.853 8.340   -26.326 1.00 45.29  ? 101 PRO   B CG  1 
ATOM   1139 C CD  . PRO   B 2 92  ? -17.326 8.244   -26.025 1.00 46.35  ? 101 PRO   B CD  1 
ATOM   1140 N N   . PRO   B 2 93  ? -16.009 11.870  -23.348 1.00 42.65  ? 102 PRO   B N   1 
ATOM   1141 C CA  . PRO   B 2 93  ? -16.364 13.277  -23.154 1.00 50.85  ? 102 PRO   B CA  1 
ATOM   1142 C C   . PRO   B 2 93  ? -16.491 14.039  -24.492 1.00 53.82  ? 102 PRO   B C   1 
ATOM   1143 O O   . PRO   B 2 93  ? -15.611 13.916  -25.329 1.00 50.24  ? 102 PRO   B O   1 
ATOM   1144 C CB  . PRO   B 2 93  ? -15.230 13.848  -22.288 1.00 44.02  ? 102 PRO   B CB  1 
ATOM   1145 C CG  . PRO   B 2 93  ? -14.570 12.626  -21.666 1.00 48.14  ? 102 PRO   B CG  1 
ATOM   1146 C CD  . PRO   B 2 93  ? -14.715 11.549  -22.722 1.00 44.67  ? 102 PRO   B CD  1 
ATOM   1147 N N   . GLY   B 2 94  ? -17.589 14.787  -24.650 1.00 52.36  ? 103 GLY   B N   1 
ATOM   1148 C CA  . GLY   B 2 94  ? -17.894 15.619  -25.827 1.00 52.92  ? 103 GLY   B CA  1 
ATOM   1149 C C   . GLY   B 2 94  ? -18.246 14.817  -27.069 1.00 49.59  ? 103 GLY   B C   1 
ATOM   1150 O O   . GLY   B 2 94  ? -18.453 15.447  -28.095 1.00 74.00  ? 103 GLY   B O   1 
ATOM   1151 N N   . GLU   B 2 95  ? -18.367 13.490  -26.996 1.00 51.00  ? 104 GLU   B N   1 
ATOM   1152 C CA  . GLU   B 2 95  ? -18.423 12.609  -28.184 1.00 49.85  ? 104 GLU   B CA  1 
ATOM   1153 C C   . GLU   B 2 95  ? -19.617 11.671  -28.065 1.00 49.46  ? 104 GLU   B C   1 
ATOM   1154 O O   . GLU   B 2 95  ? -20.032 11.360  -26.934 1.00 45.69  ? 104 GLU   B O   1 
ATOM   1155 C CB  . GLU   B 2 95  ? -17.097 11.857  -28.346 1.00 55.09  ? 104 GLU   B CB  1 
ATOM   1156 C CG  . GLU   B 2 95  ? -15.919 12.795  -28.599 1.00 59.93  ? 104 GLU   B CG  1 
ATOM   1157 C CD  . GLU   B 2 95  ? -14.556 12.136  -28.775 1.00 70.20  ? 104 GLU   B CD  1 
ATOM   1158 O OE1 . GLU   B 2 95  ? -14.506 10.892  -28.886 1.00 61.19  ? 104 GLU   B OE1 1 
ATOM   1159 O OE2 . GLU   B 2 95  ? -13.535 12.876  -28.806 1.00 80.59  ? 104 GLU   B OE2 1 
ATOM   1160 N N   . ARG   B 2 96  ? -20.186 11.276  -29.200 1.00 43.44  ? 105 ARG   B N   1 
ATOM   1161 C CA  . ARG   B 2 96  ? -21.387 10.411  -29.228 1.00 49.38  ? 105 ARG   B CA  1 
ATOM   1162 C C   . ARG   B 2 96  ? -20.995 9.010   -28.761 1.00 52.63  ? 105 ARG   B C   1 
ATOM   1163 O O   . ARG   B 2 96  ? -19.824 8.633   -28.935 1.00 47.51  ? 105 ARG   B O   1 
ATOM   1164 C CB  . ARG   B 2 96  ? -21.994 10.434  -30.630 1.00 60.18  ? 105 ARG   B CB  1 
ATOM   1165 C CG  . ARG   B 2 96  ? -23.268 9.614   -30.779 1.00 68.51  ? 105 ARG   B CG  1 
ATOM   1166 C CD  . ARG   B 2 96  ? -24.115 10.046  -31.973 1.00 70.89  ? 105 ARG   B CD  1 
ATOM   1167 N NE  . ARG   B 2 96  ? -23.350 10.128  -33.204 1.00 70.18  ? 105 ARG   B NE  1 
ATOM   1168 C CZ  . ARG   B 2 96  ? -22.704 11.214  -33.650 1.00 81.56  ? 105 ARG   B CZ  1 
ATOM   1169 N NH1 . ARG   B 2 96  ? -22.729 12.362  -32.990 1.00 85.08  ? 105 ARG   B NH1 1 
ATOM   1170 N NH2 . ARG   B 2 96  ? -22.042 11.151  -34.792 1.00 84.87  ? 105 ARG   B NH2 1 
ATOM   1171 N N   . ALA   B 2 97  ? -21.948 8.295   -28.164 1.00 50.82  ? 106 ALA   B N   1 
ATOM   1172 C CA  . ALA   B 2 97  ? -21.812 6.889   -27.747 1.00 52.99  ? 106 ALA   B CA  1 
ATOM   1173 C C   . ALA   B 2 97  ? -21.393 6.090   -28.986 1.00 58.59  ? 106 ALA   B C   1 
ATOM   1174 O O   . ALA   B 2 97  ? -21.917 6.365   -30.055 1.00 54.66  ? 106 ALA   B O   1 
ATOM   1175 C CB  . ALA   B 2 97  ? -23.105 6.370   -27.176 1.00 50.35  ? 106 ALA   B CB  1 
ATOM   1176 N N   . LYS   B 2 98  ? -20.521 5.106   -28.806 1.00 56.65  ? 107 LYS   B N   1 
ATOM   1177 C CA  . LYS   B 2 98  ? -19.850 4.346   -29.887 1.00 58.06  ? 107 LYS   B CA  1 
ATOM   1178 C C   . LYS   B 2 98  ? -19.575 2.938   -29.355 1.00 57.75  ? 107 LYS   B C   1 
ATOM   1179 O O   . LYS   B 2 98  ? -18.903 2.848   -28.305 1.00 49.37  ? 107 LYS   B O   1 
ATOM   1180 C CB  . LYS   B 2 98  ? -18.582 5.141   -30.207 1.00 73.81  ? 107 LYS   B CB  1 
ATOM   1181 C CG  . LYS   B 2 98  ? -17.623 4.537   -31.221 1.00 89.68  ? 107 LYS   B CG  1 
ATOM   1182 C CD  . LYS   B 2 98  ? -16.367 5.373   -31.416 1.00 91.76  ? 107 LYS   B CD  1 
ATOM   1183 C CE  . LYS   B 2 98  ? -15.762 5.833   -30.107 1.00 85.87  ? 107 LYS   B CE  1 
ATOM   1184 N NZ  . LYS   B 2 98  ? -14.368 6.289   -30.294 1.00 94.33  ? 107 LYS   B NZ  1 
ATOM   1185 N N   . ASN   B 2 99  ? -20.154 1.908   -29.981 1.00 49.96  ? 108 ASN   B N   1 
ATOM   1186 C CA  . ASN   B 2 99  ? -19.813 0.485   -29.731 1.00 51.67  ? 108 ASN   B CA  1 
ATOM   1187 C C   . ASN   B 2 99  ? -18.409 0.169   -30.282 1.00 59.45  ? 108 ASN   B C   1 
ATOM   1188 O O   . ASN   B 2 99  ? -18.115 0.571   -31.432 1.00 54.86  ? 108 ASN   B O   1 
ATOM   1189 C CB  . ASN   B 2 99  ? -20.849 -0.470  -30.314 1.00 48.02  ? 108 ASN   B CB  1 
ATOM   1190 C CG  . ASN   B 2 99  ? -22.212 -0.412  -29.648 1.00 55.02  ? 108 ASN   B CG  1 
ATOM   1191 O OD1 . ASN   B 2 99  ? -22.962 0.548   -29.820 1.00 55.00  ? 108 ASN   B OD1 1 
ATOM   1192 N ND2 . ASN   B 2 99  ? -22.609 -1.479  -28.968 1.00 54.88  ? 108 ASN   B ND2 1 
ATOM   1193 N N   . ILE   B 2 100 ? -17.560 -0.540  -29.522 1.00 53.23  ? 109 ILE   B N   1 
ATOM   1194 C CA  . ILE   B 2 100 ? -16.247 -1.081  -30.001 1.00 51.13  ? 109 ILE   B CA  1 
ATOM   1195 C C   . ILE   B 2 100 ? -16.209 -2.575  -29.663 1.00 55.68  ? 109 ILE   B C   1 
ATOM   1196 O O   . ILE   B 2 100 ? -16.326 -2.940  -28.460 1.00 46.54  ? 109 ILE   B O   1 
ATOM   1197 C CB  . ILE   B 2 100 ? -15.067 -0.338  -29.375 1.00 51.51  ? 109 ILE   B CB  1 
ATOM   1198 C CG1 . ILE   B 2 100 ? -15.208 1.176   -29.469 1.00 54.02  ? 109 ILE   B CG1 1 
ATOM   1199 C CG2 . ILE   B 2 100 ? -13.760 -0.827  -29.957 1.00 54.50  ? 109 ILE   B CG2 1 
ATOM   1200 C CD1 . ILE   B 2 100 ? -14.729 1.773   -30.772 1.00 63.82  ? 109 ILE   B CD1 1 
ATOM   1201 N N   . GLN   B 2 101 ? -16.134 -3.426  -30.680 1.00 45.79  ? 110 GLN   B N   1 
ATOM   1202 C CA  . GLN   B 2 101 ? -16.170 -4.895  -30.516 1.00 49.33  ? 110 GLN   B CA  1 
ATOM   1203 C C   . GLN   B 2 101 ? -14.727 -5.364  -30.312 1.00 49.46  ? 110 GLN   B C   1 
ATOM   1204 O O   . GLN   B 2 101 ? -13.818 -4.702  -30.862 1.00 53.03  ? 110 GLN   B O   1 
ATOM   1205 C CB  . GLN   B 2 101 ? -16.867 -5.548  -31.698 1.00 58.60  ? 110 GLN   B CB  1 
ATOM   1206 C CG  . GLN   B 2 101 ? -16.863 -7.058  -31.650 1.00 51.62  ? 110 GLN   B CG  1 
ATOM   1207 C CD  . GLN   B 2 101 ? -18.029 -7.675  -32.383 1.00 58.01  ? 110 GLN   B CD  1 
ATOM   1208 O OE1 . GLN   B 2 101 ? -19.083 -7.067  -32.578 1.00 50.11  ? 110 GLN   B OE1 1 
ATOM   1209 N NE2 . GLN   B 2 101 ? -17.849 -8.905  -32.827 1.00 55.55  ? 110 GLN   B NE2 1 
ATOM   1210 N N   . THR   B 2 102 ? -14.541 -6.349  -29.424 1.00 48.72  ? 111 THR   B N   1 
ATOM   1211 C CA  . THR   B 2 102 ? -13.226 -6.811  -28.902 1.00 44.89  ? 111 THR   B CA  1 
ATOM   1212 C C   . THR   B 2 102 ? -13.427 -8.182  -28.277 1.00 43.86  ? 111 THR   B C   1 
ATOM   1213 O O   . THR   B 2 102 ? -14.560 -8.491  -27.886 1.00 53.55  ? 111 THR   B O   1 
ATOM   1214 C CB  . THR   B 2 102 ? -12.583 -5.742  -28.006 1.00 49.61  ? 111 THR   B CB  1 
ATOM   1215 O OG1 . THR   B 2 102 ? -11.185 -5.973  -28.002 1.00 45.07  ? 111 THR   B OG1 1 
ATOM   1216 C CG2 . THR   B 2 102 ? -13.095 -5.704  -26.577 1.00 49.97  ? 111 THR   B CG2 1 
ATOM   1217 N N   . LEU   B 2 103 ? -12.381 -9.011  -28.300 1.00 48.67  ? 112 LEU   B N   1 
ATOM   1218 C CA  . LEU   B 2 103 ? -12.304 -10.277 -27.528 1.00 43.72  ? 112 LEU   B CA  1 
ATOM   1219 C C   . LEU   B 2 103 ? -11.404 -9.961  -26.337 1.00 42.39  ? 112 LEU   B C   1 
ATOM   1220 O O   . LEU   B 2 103 ? -10.248 -9.513  -26.469 1.00 43.91  ? 112 LEU   B O   1 
ATOM   1221 C CB  . LEU   B 2 103 ? -11.769 -11.460 -28.353 1.00 49.88  ? 112 LEU   B CB  1 
ATOM   1222 C CG  . LEU   B 2 103 ? -11.548 -12.728 -27.535 1.00 49.97  ? 112 LEU   B CG  1 
ATOM   1223 C CD1 . LEU   B 2 103 ? -12.793 -13.584 -27.524 1.00 50.40  ? 112 LEU   B CD1 1 
ATOM   1224 C CD2 . LEU   B 2 103 ? -10.343 -13.522 -28.004 1.00 63.73  ? 112 LEU   B CD2 1 
ATOM   1225 N N   . PRO   B 2 104 ? -11.964 -10.036 -25.117 1.00 39.09  ? 113 PRO   B N   1 
ATOM   1226 C CA  . PRO   B 2 104 ? -11.232 -9.563  -23.952 1.00 40.54  ? 113 PRO   B CA  1 
ATOM   1227 C C   . PRO   B 2 104 ? -10.037 -10.512 -23.683 1.00 42.84  ? 113 PRO   B C   1 
ATOM   1228 O O   . PRO   B 2 104 ? -10.159 -11.660 -23.966 1.00 44.89  ? 113 PRO   B O   1 
ATOM   1229 C CB  . PRO   B 2 104 ? -12.211 -9.650  -22.781 1.00 40.18  ? 113 PRO   B CB  1 
ATOM   1230 C CG  . PRO   B 2 104 ? -13.538 -10.161 -23.393 1.00 43.76  ? 113 PRO   B CG  1 
ATOM   1231 C CD  . PRO   B 2 104 ? -13.258 -10.663 -24.803 1.00 41.78  ? 113 PRO   B CD  1 
ATOM   1232 N N   . GLY   B 2 105 ? -8.948  -9.956  -23.162 1.00 46.76  ? 114 GLY   B N   1 
ATOM   1233 C CA  . GLY   B 2 105 ? -7.887  -10.631 -22.402 1.00 49.50  ? 114 GLY   B CA  1 
ATOM   1234 C C   . GLY   B 2 105 ? -8.340  -11.011 -21.004 1.00 51.50  ? 114 GLY   B C   1 
ATOM   1235 O O   . GLY   B 2 105 ? -9.576  -11.185 -20.787 1.00 48.04  ? 114 GLY   B O   1 
ATOM   1236 N N   . ILE   B 2 106 ? -7.354  -11.275 -20.135 1.00 53.15  ? 115 ILE   B N   1 
ATOM   1237 C CA  . ILE   B 2 106 ? -7.540  -11.910 -18.797 1.00 54.10  ? 115 ILE   B CA  1 
ATOM   1238 C C   . ILE   B 2 106 ? -6.661  -11.200 -17.763 1.00 50.61  ? 115 ILE   B C   1 
ATOM   1239 O O   . ILE   B 2 106 ? -5.508  -10.912 -18.033 1.00 56.61  ? 115 ILE   B O   1 
ATOM   1240 C CB  . ILE   B 2 106 ? -7.225  -13.404 -18.855 1.00 57.94  ? 115 ILE   B CB  1 
ATOM   1241 C CG1 . ILE   B 2 106 ? -8.025  -14.126 -19.939 1.00 68.42  ? 115 ILE   B CG1 1 
ATOM   1242 C CG2 . ILE   B 2 106 ? -7.467  -14.017 -17.501 1.00 64.77  ? 115 ILE   B CG2 1 
ATOM   1243 C CD1 . ILE   B 2 106 ? -9.307  -14.744 -19.465 1.00 64.35  ? 115 ILE   B CD1 1 
ATOM   1244 N N   . PHE   B 2 107 ? -7.251  -10.838 -16.637 1.00 52.81  ? 116 PHE   B N   1 
ATOM   1245 C CA  . PHE   B 2 107 ? -6.538  -10.497 -15.387 1.00 49.34  ? 116 PHE   B CA  1 
ATOM   1246 C C   . PHE   B 2 107 ? -6.471  -11.790 -14.562 1.00 48.27  ? 116 PHE   B C   1 
ATOM   1247 O O   . PHE   B 2 107 ? -7.523  -12.342 -14.203 1.00 55.49  ? 116 PHE   B O   1 
ATOM   1248 C CB  . PHE   B 2 107 ? -7.260  -9.341  -14.685 1.00 47.16  ? 116 PHE   B CB  1 
ATOM   1249 C CG  . PHE   B 2 107 ? -6.913  -7.951  -15.156 1.00 47.13  ? 116 PHE   B CG  1 
ATOM   1250 C CD1 . PHE   B 2 107 ? -6.124  -7.733  -16.277 1.00 48.48  ? 116 PHE   B CD1 1 
ATOM   1251 C CD2 . PHE   B 2 107 ? -7.428  -6.847  -14.490 1.00 49.41  ? 116 PHE   B CD2 1 
ATOM   1252 C CE1 . PHE   B 2 107 ? -5.816  -6.451  -16.699 1.00 42.31  ? 116 PHE   B CE1 1 
ATOM   1253 C CE2 . PHE   B 2 107 ? -7.101  -5.562  -14.892 1.00 46.63  ? 116 PHE   B CE2 1 
ATOM   1254 C CZ  . PHE   B 2 107 ? -6.321  -5.368  -16.017 1.00 50.75  ? 116 PHE   B CZ  1 
ATOM   1255 N N   . LYS   B 2 108 ? -5.269  -12.316 -14.340 1.00 57.89  ? 117 LYS   B N   1 
ATOM   1256 C CA  . LYS   B 2 108 ? -5.052  -13.512 -13.477 1.00 62.95  ? 117 LYS   B CA  1 
ATOM   1257 C C   . LYS   B 2 108 ? -4.606  -12.997 -12.101 1.00 48.60  ? 117 LYS   B C   1 
ATOM   1258 O O   . LYS   B 2 108 ? -3.607  -12.272 -12.044 1.00 49.97  ? 117 LYS   B O   1 
ATOM   1259 C CB  . LYS   B 2 108 ? -4.003  -14.459 -14.076 1.00 72.58  ? 117 LYS   B CB  1 
ATOM   1260 C CG  . LYS   B 2 108 ? -4.411  -15.229 -15.326 1.00 82.33  ? 117 LYS   B CG  1 
ATOM   1261 C CD  . LYS   B 2 108 ? -3.241  -15.839 -16.103 1.00 88.88  ? 117 LYS   B CD  1 
ATOM   1262 C CE  . LYS   B 2 108 ? -3.626  -16.257 -17.514 1.00 108.44 ? 117 LYS   B CE  1 
ATOM   1263 N NZ  . LYS   B 2 108 ? -2.484  -16.753 -18.330 1.00 105.72 ? 117 LYS   B NZ  1 
ATOM   1264 N N   . THR   B 2 109 ? -5.373  -13.299 -11.059 1.00 49.75  ? 118 THR   B N   1 
ATOM   1265 C CA  . THR   B 2 109 ? -5.112  -12.860 -9.669  1.00 56.63  ? 118 THR   B CA  1 
ATOM   1266 C C   . THR   B 2 109 ? -5.154  -14.105 -8.794  1.00 54.56  ? 118 THR   B C   1 
ATOM   1267 O O   . THR   B 2 109 ? -5.854  -15.066 -9.165  1.00 52.21  ? 118 THR   B O   1 
ATOM   1268 C CB  . THR   B 2 109 ? -6.157  -11.840 -9.176  1.00 53.70  ? 118 THR   B CB  1 
ATOM   1269 O OG1 . THR   B 2 109 ? -7.372  -12.519 -8.844  1.00 47.25  ? 118 THR   B OG1 1 
ATOM   1270 C CG2 . THR   B 2 109 ? -6.455  -10.768 -10.200 1.00 51.64  ? 118 THR   B CG2 1 
ATOM   1271 N N   . LYS   B 2 110 ? -4.520  -14.033 -7.632  1.00 55.88  ? 119 LYS   B N   1 
ATOM   1272 C CA  . LYS   B 2 110 ? -4.523  -15.114 -6.612  1.00 56.32  ? 119 LYS   B CA  1 
ATOM   1273 C C   . LYS   B 2 110 ? -5.970  -15.569 -6.332  1.00 61.22  ? 119 LYS   B C   1 
ATOM   1274 O O   . LYS   B 2 110 ? -6.164  -16.731 -5.923  1.00 58.10  ? 119 LYS   B O   1 
ATOM   1275 C CB  . LYS   B 2 110 ? -3.795  -14.614 -5.360  1.00 61.11  ? 119 LYS   B CB  1 
ATOM   1276 C CG  . LYS   B 2 110 ? -4.336  -13.325 -4.758  1.00 67.18  ? 119 LYS   B CG  1 
ATOM   1277 C CD  . LYS   B 2 110 ? -3.510  -12.803 -3.597  1.00 69.80  ? 119 LYS   B CD  1 
ATOM   1278 C CE  . LYS   B 2 110 ? -4.043  -13.255 -2.252  1.00 70.33  ? 119 LYS   B CE  1 
ATOM   1279 N NZ  . LYS   B 2 110 ? -5.296  -12.550 -1.890  1.00 66.21  ? 119 LYS   B NZ  1 
ATOM   1280 N N   . ASP   B 2 111 ? -6.963  -14.698 -6.533  1.00 55.10  ? 120 ASP   B N   1 
ATOM   1281 C CA  . ASP   B 2 111 ? -8.369  -14.974 -6.157  1.00 57.51  ? 120 ASP   B CA  1 
ATOM   1282 C C   . ASP   B 2 111 ? -9.181  -15.375 -7.385  1.00 54.84  ? 120 ASP   B C   1 
ATOM   1283 O O   . ASP   B 2 111 ? -10.411 -15.425 -7.252  1.00 61.83  ? 120 ASP   B O   1 
ATOM   1284 C CB  . ASP   B 2 111 ? -8.977  -13.767 -5.451  1.00 59.22  ? 120 ASP   B CB  1 
ATOM   1285 C CG  . ASP   B 2 111 ? -8.243  -13.430 -4.169  1.00 65.05  ? 120 ASP   B CG  1 
ATOM   1286 O OD1 . ASP   B 2 111 ? -8.114  -14.319 -3.314  1.00 66.53  ? 120 ASP   B OD1 1 
ATOM   1287 O OD2 . ASP   B 2 111 ? -7.767  -12.298 -4.066  1.00 74.88  ? 120 ASP   B OD2 1 
ATOM   1288 N N   . GLY   B 2 112 ? -8.532  -15.676 -8.516  1.00 51.89  ? 121 GLY   B N   1 
ATOM   1289 C CA  . GLY   B 2 112 ? -9.251  -16.047 -9.746  1.00 50.07  ? 121 GLY   B CA  1 
ATOM   1290 C C   . GLY   B 2 112 ? -9.066  -15.066 -10.891 1.00 50.03  ? 121 GLY   B C   1 
ATOM   1291 O O   . GLY   B 2 112 ? -8.222  -14.119 -10.816 1.00 52.75  ? 121 GLY   B O   1 
ATOM   1292 N N   . ASP   B 2 113 ? -9.763  -15.374 -11.978 1.00 50.65  ? 122 ASP   B N   1 
ATOM   1293 C CA  . ASP   B 2 113 ? -9.560  -14.798 -13.332 1.00 55.63  ? 122 ASP   B CA  1 
ATOM   1294 C C   . ASP   B 2 113 ? -10.677 -13.780 -13.583 1.00 47.57  ? 122 ASP   B C   1 
ATOM   1295 O O   . ASP   B 2 113 ? -11.824 -14.164 -13.358 1.00 47.20  ? 122 ASP   B O   1 
ATOM   1296 C CB  . ASP   B 2 113 ? -9.653  -15.875 -14.423 1.00 54.42  ? 122 ASP   B CB  1 
ATOM   1297 C CG  . ASP   B 2 113 ? -8.408  -16.723 -14.627 1.00 66.26  ? 122 ASP   B CG  1 
ATOM   1298 O OD1 . ASP   B 2 113 ? -7.325  -16.324 -14.126 1.00 55.81  ? 122 ASP   B OD1 1 
ATOM   1299 O OD2 . ASP   B 2 113 ? -8.529  -17.762 -15.336 1.00 72.13  ? 122 ASP   B OD2 1 
ATOM   1300 N N   . ILE   B 2 114 ? -10.311 -12.599 -14.083 1.00 46.21  ? 123 ILE   B N   1 
ATOM   1301 C CA  . ILE   B 2 114 ? -11.217 -11.498 -14.510 1.00 57.38  ? 123 ILE   B CA  1 
ATOM   1302 C C   . ILE   B 2 114 ? -10.983 -11.238 -15.998 1.00 49.68  ? 123 ILE   B C   1 
ATOM   1303 O O   . ILE   B 2 114 ? -9.806  -11.129 -16.399 1.00 43.16  ? 123 ILE   B O   1 
ATOM   1304 C CB  . ILE   B 2 114 ? -10.962 -10.209 -13.694 1.00 60.21  ? 123 ILE   B CB  1 
ATOM   1305 C CG1 . ILE   B 2 114 ? -10.541 -10.502 -12.249 1.00 71.29  ? 123 ILE   B CG1 1 
ATOM   1306 C CG2 . ILE   B 2 114 ? -12.182 -9.314  -13.760 1.00 63.82  ? 123 ILE   B CG2 1 
ATOM   1307 C CD1 . ILE   B 2 114 ? -10.162 -9.280  -11.438 1.00 72.42  ? 123 ILE   B CD1 1 
ATOM   1308 N N   . GLY   B 2 115 ? -12.066 -11.000 -16.733 1.00 47.90  ? 124 GLY   B N   1 
ATOM   1309 C CA  . GLY   B 2 115 ? -12.018 -10.416 -18.087 1.00 40.65  ? 124 GLY   B CA  1 
ATOM   1310 C C   . GLY   B 2 115 ? -11.308 -9.087  -18.083 1.00 39.16  ? 124 GLY   B C   1 
ATOM   1311 O O   . GLY   B 2 115 ? -11.249 -8.386  -17.059 1.00 44.86  ? 124 GLY   B O   1 
ATOM   1312 N N   . ALA   B 2 116 ? -10.652 -8.775  -19.176 1.00 36.86  ? 125 ALA   B N   1 
ATOM   1313 C CA  . ALA   B 2 116 ? -10.015 -7.474  -19.371 1.00 42.12  ? 125 ALA   B CA  1 
ATOM   1314 C C   . ALA   B 2 116 ? -10.210 -7.089  -20.837 1.00 46.69  ? 125 ALA   B C   1 
ATOM   1315 O O   . ALA   B 2 116 ? -10.091 -7.945  -21.720 1.00 48.64  ? 125 ALA   B O   1 
ATOM   1316 C CB  . ALA   B 2 116 ? -8.582  -7.511  -18.985 1.00 43.33  ? 125 ALA   B CB  1 
ATOM   1317 N N   A VAL   B 2 117 ? -10.526 -5.817  -21.084 0.25 48.26  ? 126 VAL   B N   1 
ATOM   1318 N N   B VAL   B 2 117 ? -10.518 -5.810  -21.057 0.25 47.64  ? 126 VAL   B N   1 
ATOM   1319 N N   C VAL   B 2 117 ? -10.526 -5.817  -21.084 0.25 48.26  ? 126 VAL   B N   1 
ATOM   1320 N N   D VAL   B 2 117 ? -10.518 -5.810  -21.057 0.25 47.64  ? 126 VAL   B N   1 
ATOM   1321 C CA  A VAL   B 2 117 ? -10.664 -5.243  -22.454 0.25 50.24  ? 126 VAL   B CA  1 
ATOM   1322 C CA  B VAL   B 2 117 ? -10.665 -5.169  -22.395 0.25 49.19  ? 126 VAL   B CA  1 
ATOM   1323 C CA  C VAL   B 2 117 ? -10.664 -5.243  -22.454 0.25 50.24  ? 126 VAL   B CA  1 
ATOM   1324 C CA  D VAL   B 2 117 ? -10.665 -5.169  -22.395 0.25 49.19  ? 126 VAL   B CA  1 
ATOM   1325 C C   A VAL   B 2 117 ? -9.517  -4.255  -22.668 0.25 50.35  ? 126 VAL   B C   1 
ATOM   1326 C C   B VAL   B 2 117 ? -9.449  -4.273  -22.615 0.25 49.99  ? 126 VAL   B C   1 
ATOM   1327 C C   C VAL   B 2 117 ? -9.517  -4.255  -22.668 0.25 50.35  ? 126 VAL   B C   1 
ATOM   1328 C C   D VAL   B 2 117 ? -9.449  -4.273  -22.615 0.25 49.99  ? 126 VAL   B C   1 
ATOM   1329 O O   A VAL   B 2 117 ? -9.377  -3.326  -21.852 0.25 49.96  ? 126 VAL   B O   1 
ATOM   1330 O O   B VAL   B 2 117 ? -9.190  -3.418  -21.746 0.25 50.09  ? 126 VAL   B O   1 
ATOM   1331 O O   C VAL   B 2 117 ? -9.377  -3.326  -21.852 0.25 49.96  ? 126 VAL   B O   1 
ATOM   1332 O O   D VAL   B 2 117 ? -9.190  -3.418  -21.746 0.25 50.09  ? 126 VAL   B O   1 
ATOM   1333 C CB  A VAL   B 2 117 ? -12.047 -4.599  -22.665 0.25 53.53  ? 126 VAL   B CB  1 
ATOM   1334 C CB  B VAL   B 2 117 ? -11.975 -4.366  -22.473 0.25 51.51  ? 126 VAL   B CB  1 
ATOM   1335 C CB  C VAL   B 2 117 ? -12.047 -4.599  -22.665 0.25 53.53  ? 126 VAL   B CB  1 
ATOM   1336 C CB  D VAL   B 2 117 ? -11.975 -4.366  -22.473 0.25 51.51  ? 126 VAL   B CB  1 
ATOM   1337 C CG1 A VAL   B 2 117 ? -13.138 -5.658  -22.691 0.25 53.58  ? 126 VAL   B CG1 1 
ATOM   1338 C CG1 B VAL   B 2 117 ? -11.869 -3.214  -23.457 0.25 50.03  ? 126 VAL   B CG1 1 
ATOM   1339 C CG1 C VAL   B 2 117 ? -13.138 -5.658  -22.691 0.25 53.58  ? 126 VAL   B CG1 1 
ATOM   1340 C CG1 D VAL   B 2 117 ? -11.869 -3.214  -23.457 0.25 50.03  ? 126 VAL   B CG1 1 
ATOM   1341 C CG2 A VAL   B 2 117 ? -12.356 -3.531  -21.624 0.25 53.65  ? 126 VAL   B CG2 1 
ATOM   1342 C CG2 B VAL   B 2 117 ? -13.159 -5.262  -22.797 0.25 51.72  ? 126 VAL   B CG2 1 
ATOM   1343 C CG2 C VAL   B 2 117 ? -12.356 -3.531  -21.624 0.25 53.65  ? 126 VAL   B CG2 1 
ATOM   1344 C CG2 D VAL   B 2 117 ? -13.159 -5.262  -22.797 0.25 51.72  ? 126 VAL   B CG2 1 
ATOM   1345 N N   . ALA   B 2 118 ? -8.715  -4.487  -23.714 1.00 51.12  ? 127 ALA   B N   1 
ATOM   1346 C CA  . ALA   B 2 118 ? -7.561  -3.651  -24.079 1.00 49.58  ? 127 ALA   B CA  1 
ATOM   1347 C C   . ALA   B 2 118 ? -8.060  -2.594  -25.062 1.00 59.26  ? 127 ALA   B C   1 
ATOM   1348 O O   . ALA   B 2 118 ? -8.052  -2.879  -26.277 1.00 60.45  ? 127 ALA   B O   1 
ATOM   1349 C CB  . ALA   B 2 118 ? -6.475  -4.520  -24.659 1.00 61.50  ? 127 ALA   B CB  1 
ATOM   1350 N N   . LEU   B 2 119 ? -8.589  -1.488  -24.522 1.00 56.69  ? 128 LEU   B N   1 
ATOM   1351 C CA  . LEU   B 2 119 ? -9.016  -0.267  -25.254 1.00 51.95  ? 128 LEU   B CA  1 
ATOM   1352 C C   . LEU   B 2 119 ? -8.630  0.919   -24.377 1.00 55.90  ? 128 LEU   B C   1 
ATOM   1353 O O   . LEU   B 2 119 ? -8.955  0.895   -23.178 1.00 64.30  ? 128 LEU   B O   1 
ATOM   1354 C CB  . LEU   B 2 119 ? -10.522 -0.332  -25.527 1.00 48.85  ? 128 LEU   B CB  1 
ATOM   1355 C CG  . LEU   B 2 119 ? -10.961 -1.573  -26.299 1.00 52.51  ? 128 LEU   B CG  1 
ATOM   1356 C CD1 . LEU   B 2 119 ? -12.464 -1.821  -26.233 1.00 47.67  ? 128 LEU   B CD1 1 
ATOM   1357 C CD2 . LEU   B 2 119 ? -10.504 -1.477  -27.753 1.00 56.13  ? 128 LEU   B CD2 1 
ATOM   1358 N N   . ASP   B 2 120 ? -7.907  1.880   -24.922 1.00 44.67  ? 129 ASP   B N   1 
ATOM   1359 C CA  . ASP   B 2 120 ? -7.547  3.104   -24.189 1.00 49.15  ? 129 ASP   B CA  1 
ATOM   1360 C C   . ASP   B 2 120 ? -8.609  4.159   -24.527 1.00 58.26  ? 129 ASP   B C   1 
ATOM   1361 O O   . ASP   B 2 120 ? -8.803  4.423   -25.712 1.00 59.94  ? 129 ASP   B O   1 
ATOM   1362 C CB  . ASP   B 2 120 ? -6.106  3.477   -24.527 1.00 53.98  ? 129 ASP   B CB  1 
ATOM   1363 C CG  . ASP   B 2 120 ? -5.451  4.431   -23.533 1.00 59.34  ? 129 ASP   B CG  1 
ATOM   1364 O OD1 . ASP   B 2 120 ? -6.161  5.318   -22.966 1.00 67.49  ? 129 ASP   B OD1 1 
ATOM   1365 O OD2 . ASP   B 2 120 ? -4.236  4.289   -23.323 1.00 62.86  ? 129 ASP   B OD2 1 
ATOM   1366 N N   . TYR   B 2 121 ? -9.281  4.744   -23.530 1.00 48.59  ? 130 TYR   B N   1 
ATOM   1367 C CA  . TYR   B 2 121 ? -10.147 5.941   -23.705 1.00 48.37  ? 130 TYR   B CA  1 
ATOM   1368 C C   . TYR   B 2 121 ? -9.895  6.912   -22.560 1.00 47.21  ? 130 TYR   B C   1 
ATOM   1369 O O   . TYR   B 2 121 ? -9.175  6.587   -21.606 1.00 54.56  ? 130 TYR   B O   1 
ATOM   1370 C CB  . TYR   B 2 121 ? -11.608 5.519   -23.820 1.00 52.51  ? 130 TYR   B CB  1 
ATOM   1371 C CG  . TYR   B 2 121 ? -12.016 4.912   -25.137 1.00 52.49  ? 130 TYR   B CG  1 
ATOM   1372 C CD1 . TYR   B 2 121 ? -12.289 5.707   -26.238 1.00 57.06  ? 130 TYR   B CD1 1 
ATOM   1373 C CD2 . TYR   B 2 121 ? -12.175 3.549   -25.283 1.00 50.32  ? 130 TYR   B CD2 1 
ATOM   1374 C CE1 . TYR   B 2 121 ? -12.693 5.158   -27.448 1.00 55.23  ? 130 TYR   B CE1 1 
ATOM   1375 C CE2 . TYR   B 2 121 ? -12.575 2.985   -26.484 1.00 53.38  ? 130 TYR   B CE2 1 
ATOM   1376 C CZ  . TYR   B 2 121 ? -12.846 3.792   -27.572 1.00 60.83  ? 130 TYR   B CZ  1 
ATOM   1377 O OH  . TYR   B 2 121 ? -13.243 3.257   -28.764 1.00 69.81  ? 130 TYR   B OH  1 
ATOM   1378 N N   . PRO   B 2 122 ? -10.381 8.174   -22.636 1.00 47.69  ? 131 PRO   B N   1 
ATOM   1379 C CA  . PRO   B 2 122 ? -10.102 9.151   -21.577 1.00 54.53  ? 131 PRO   B CA  1 
ATOM   1380 C C   . PRO   B 2 122 ? -10.685 8.704   -20.215 1.00 42.68  ? 131 PRO   B C   1 
ATOM   1381 O O   . PRO   B 2 122 ? -11.585 7.901   -20.212 1.00 45.07  ? 131 PRO   B O   1 
ATOM   1382 C CB  . PRO   B 2 122 ? -10.748 10.433  -22.126 1.00 57.97  ? 131 PRO   B CB  1 
ATOM   1383 C CG  . PRO   B 2 122 ? -10.753 10.233  -23.621 1.00 53.34  ? 131 PRO   B CG  1 
ATOM   1384 C CD  . PRO   B 2 122 ? -11.090 8.773   -23.781 1.00 55.95  ? 131 PRO   B CD  1 
ATOM   1385 N N   . ALA   B 2 123 ? -10.096 9.158   -19.112 1.00 44.83  ? 132 ALA   B N   1 
ATOM   1386 C CA  . ALA   B 2 123 ? -10.511 8.795   -17.737 1.00 50.16  ? 132 ALA   B CA  1 
ATOM   1387 C C   . ALA   B 2 123 ? -12.033 8.992   -17.602 1.00 51.15  ? 132 ALA   B C   1 
ATOM   1388 O O   . ALA   B 2 123 ? -12.772 8.095   -17.071 1.00 47.63  ? 132 ALA   B O   1 
ATOM   1389 C CB  . ALA   B 2 123 ? -9.716  9.605   -16.741 1.00 52.56  ? 132 ALA   B CB  1 
ATOM   1390 N N   . GLY   B 2 124 ? -12.538 10.057  -18.210 1.00 45.64  ? 133 GLY   B N   1 
ATOM   1391 C CA  . GLY   B 2 124 ? -13.961 10.437  -18.136 1.00 40.73  ? 133 GLY   B CA  1 
ATOM   1392 C C   . GLY   B 2 124 ? -14.873 9.416   -18.793 1.00 39.01  ? 133 GLY   B C   1 
ATOM   1393 O O   . GLY   B 2 124 ? -16.125 9.604   -18.705 1.00 36.45  ? 133 GLY   B O   1 
ATOM   1394 N N   . THR   B 2 125 ? -14.320 8.361   -19.420 1.00 32.96  ? 134 THR   B N   1 
ATOM   1395 C CA  . THR   B 2 125 ? -15.113 7.265   -20.042 1.00 31.77  ? 134 THR   B CA  1 
ATOM   1396 C C   . THR   B 2 125 ? -15.434 6.153   -18.995 1.00 35.63  ? 134 THR   B C   1 
ATOM   1397 O O   . THR   B 2 125 ? -16.252 5.261   -19.300 1.00 35.47  ? 134 THR   B O   1 
ATOM   1398 C CB  . THR   B 2 125 ? -14.350 6.756   -21.280 1.00 43.88  ? 134 THR   B CB  1 
ATOM   1399 O OG1 . THR   B 2 125 ? -13.861 7.878   -22.014 1.00 51.03  ? 134 THR   B OG1 1 
ATOM   1400 C CG2 . THR   B 2 125 ? -15.193 5.931   -22.213 1.00 42.51  ? 134 THR   B CG2 1 
ATOM   1401 N N   . SER   B 2 126 ? -14.857 6.236   -17.794 1.00 36.46  ? 135 SER   B N   1 
ATOM   1402 C CA  . SER   B 2 126 ? -15.042 5.247   -16.688 1.00 38.57  ? 135 SER   B CA  1 
ATOM   1403 C C   . SER   B 2 126 ? -16.537 5.073   -16.405 1.00 37.42  ? 135 SER   B C   1 
ATOM   1404 O O   . SER   B 2 126 ? -17.213 6.109   -16.212 1.00 42.94  ? 135 SER   B O   1 
ATOM   1405 C CB  . SER   B 2 126 ? -14.282 5.686   -15.460 1.00 41.99  ? 135 SER   B CB  1 
ATOM   1406 O OG  . SER   B 2 126 ? -12.865 5.817   -15.674 1.00 41.92  ? 135 SER   B OG  1 
ATOM   1407 N N   . GLY   B 2 127 ? -17.036 3.832   -16.407 1.00 40.29  ? 136 GLY   B N   1 
ATOM   1408 C CA  . GLY   B 2 127 ? -18.441 3.464   -16.150 1.00 34.90  ? 136 GLY   B CA  1 
ATOM   1409 C C   . GLY   B 2 127 ? -19.173 3.089   -17.390 1.00 34.88  ? 136 GLY   B C   1 
ATOM   1410 O O   . GLY   B 2 127 ? -20.280 2.513   -17.292 1.00 32.87  ? 136 GLY   B O   1 
ATOM   1411 N N   . SER   B 2 128 ? -18.569 3.318   -18.568 1.00 37.92  ? 137 SER   B N   1 
ATOM   1412 C CA  . SER   B 2 128 ? -19.180 2.825   -19.822 1.00 39.20  ? 137 SER   B CA  1 
ATOM   1413 C C   . SER   B 2 128 ? -19.369 1.333   -19.709 1.00 34.14  ? 137 SER   B C   1 
ATOM   1414 O O   . SER   B 2 128 ? -18.470 0.614   -19.268 1.00 34.45  ? 137 SER   B O   1 
ATOM   1415 C CB  . SER   B 2 128 ? -18.360 3.187   -21.036 1.00 37.39  ? 137 SER   B CB  1 
ATOM   1416 O OG  . SER   B 2 128 ? -18.257 4.596   -21.169 1.00 39.46  ? 137 SER   B OG  1 
ATOM   1417 N N   . PRO   B 2 129 ? -20.542 0.824   -20.117 1.00 36.26  ? 138 PRO   B N   1 
ATOM   1418 C CA  . PRO   B 2 129 ? -20.820 -0.592  -20.034 1.00 32.33  ? 138 PRO   B CA  1 
ATOM   1419 C C   . PRO   B 2 129 ? -20.148 -1.410  -21.139 1.00 43.92  ? 138 PRO   B C   1 
ATOM   1420 O O   . PRO   B 2 129 ? -20.039 -0.946  -22.311 1.00 37.34  ? 138 PRO   B O   1 
ATOM   1421 C CB  . PRO   B 2 129 ? -22.332 -0.717  -20.269 1.00 39.59  ? 138 PRO   B CB  1 
ATOM   1422 C CG  . PRO   B 2 129 ? -22.734 0.562   -20.989 1.00 35.76  ? 138 PRO   B CG  1 
ATOM   1423 C CD  . PRO   B 2 129 ? -21.686 1.601   -20.633 1.00 36.26  ? 138 PRO   B CD  1 
ATOM   1424 N N   . ILE   B 2 130 ? -19.800 -2.628  -20.764 1.00 38.26  ? 139 ILE   B N   1 
ATOM   1425 C CA  . ILE   B 2 130 ? -19.271 -3.695  -21.667 1.00 39.56  ? 139 ILE   B CA  1 
ATOM   1426 C C   . ILE   B 2 130 ? -20.415 -4.675  -21.816 1.00 34.57  ? 139 ILE   B C   1 
ATOM   1427 O O   . ILE   B 2 130 ? -21.002 -4.985  -20.779 1.00 38.12  ? 139 ILE   B O   1 
ATOM   1428 C CB  . ILE   B 2 130 ? -18.003 -4.320  -21.062 1.00 37.63  ? 139 ILE   B CB  1 
ATOM   1429 C CG1 . ILE   B 2 130 ? -16.931 -3.258  -20.864 1.00 44.91  ? 139 ILE   B CG1 1 
ATOM   1430 C CG2 . ILE   B 2 130 ? -17.479 -5.469  -21.903 1.00 42.64  ? 139 ILE   B CG2 1 
ATOM   1431 C CD1 . ILE   B 2 130 ? -15.887 -3.643  -19.854 1.00 51.83  ? 139 ILE   B CD1 1 
ATOM   1432 N N   . LEU   B 2 131 ? -20.801 -5.028  -23.044 1.00 34.91  ? 140 LEU   B N   1 
ATOM   1433 C CA  . LEU   B 2 131 ? -21.978 -5.920  -23.316 1.00 41.80  ? 140 LEU   B CA  1 
ATOM   1434 C C   . LEU   B 2 131 ? -21.636 -7.279  -23.942 1.00 37.05  ? 140 LEU   B C   1 
ATOM   1435 O O   . LEU   B 2 131 ? -20.743 -7.340  -24.754 1.00 43.09  ? 140 LEU   B O   1 
ATOM   1436 C CB  . LEU   B 2 131 ? -22.905 -5.241  -24.333 1.00 47.18  ? 140 LEU   B CB  1 
ATOM   1437 C CG  . LEU   B 2 131 ? -23.016 -3.727  -24.219 1.00 55.91  ? 140 LEU   B CG  1 
ATOM   1438 C CD1 . LEU   B 2 131 ? -23.824 -3.183  -25.396 1.00 53.71  ? 140 LEU   B CD1 1 
ATOM   1439 C CD2 . LEU   B 2 131 ? -23.640 -3.371  -22.870 1.00 56.03  ? 140 LEU   B CD2 1 
ATOM   1440 N N   . ASP   B 2 132 ? -22.531 -8.240  -23.774 1.00 39.38  ? 141 ASP   B N   1 
ATOM   1441 C CA  . ASP   B 2 132 ? -22.572 -9.501  -24.566 1.00 50.67  ? 141 ASP   B CA  1 
ATOM   1442 C C   . ASP   B 2 132 ? -23.516 -9.385  -25.796 1.00 61.89  ? 141 ASP   B C   1 
ATOM   1443 O O   . ASP   B 2 132 ? -24.130 -8.304  -26.025 1.00 55.83  ? 141 ASP   B O   1 
ATOM   1444 C CB  . ASP   B 2 132 ? -22.945 -10.659 -23.639 1.00 47.64  ? 141 ASP   B CB  1 
ATOM   1445 C CG  . ASP   B 2 132 ? -24.392 -10.684 -23.214 1.00 51.66  ? 141 ASP   B CG  1 
ATOM   1446 O OD1 . ASP   B 2 132 ? -25.160 -9.938  -23.812 1.00 55.62  ? 141 ASP   B OD1 1 
ATOM   1447 O OD2 . ASP   B 2 132 ? -24.738 -11.479 -22.312 1.00 53.02  ? 141 ASP   B OD2 1 
ATOM   1448 N N   . LYS   B 2 133 ? -23.665 -10.470 -26.567 1.00 66.06  ? 142 LYS   B N   1 
ATOM   1449 C CA  . LYS   B 2 133 ? -24.343 -10.458 -27.903 1.00 75.24  ? 142 LYS   B CA  1 
ATOM   1450 C C   . LYS   B 2 133 ? -25.862 -10.325 -27.725 1.00 68.14  ? 142 LYS   B C   1 
ATOM   1451 O O   . LYS   B 2 133 ? -26.530 -10.036 -28.716 1.00 68.77  ? 142 LYS   B O   1 
ATOM   1452 C CB  . LYS   B 2 133 ? -24.016 -11.722 -28.724 1.00 75.35  ? 142 LYS   B CB  1 
ATOM   1453 C CG  . LYS   B 2 133 ? -22.607 -11.802 -29.302 1.00 86.98  ? 142 LYS   B CG  1 
ATOM   1454 C CD  . LYS   B 2 133 ? -22.142 -13.222 -29.644 1.00 96.23  ? 142 LYS   B CD  1 
ATOM   1455 C CE  . LYS   B 2 133 ? -20.698 -13.289 -30.108 1.00 101.94 ? 142 LYS   B CE  1 
ATOM   1456 N NZ  . LYS   B 2 133 ? -20.265 -14.681 -30.391 1.00 107.35 ? 142 LYS   B NZ  1 
ATOM   1457 N N   . CYS   B 2 134 ? -26.381 -10.555 -26.516 1.00 66.48  ? 143 CYS   B N   1 
ATOM   1458 C CA  . CYS   B 2 134 ? -27.823 -10.472 -26.159 1.00 63.90  ? 143 CYS   B CA  1 
ATOM   1459 C C   . CYS   B 2 134 ? -28.142 -9.069  -25.589 1.00 58.16  ? 143 CYS   B C   1 
ATOM   1460 O O   . CYS   B 2 134 ? -29.290 -8.845  -25.151 1.00 61.88  ? 143 CYS   B O   1 
ATOM   1461 C CB  . CYS   B 2 134 ? -28.186 -11.585 -25.173 1.00 69.57  ? 143 CYS   B CB  1 
ATOM   1462 S SG  . CYS   B 2 134 ? -28.660 -13.183 -25.907 1.00 77.07  ? 143 CYS   B SG  1 
ATOM   1463 N N   . GLY   B 2 135 ? -27.174 -8.142  -25.588 1.00 55.92  ? 144 GLY   B N   1 
ATOM   1464 C CA  . GLY   B 2 135 ? -27.317 -6.772  -25.040 1.00 60.41  ? 144 GLY   B CA  1 
ATOM   1465 C C   . GLY   B 2 135 ? -27.176 -6.644  -23.511 1.00 56.52  ? 144 GLY   B C   1 
ATOM   1466 O O   . GLY   B 2 135 ? -27.268 -5.514  -23.012 1.00 51.81  ? 144 GLY   B O   1 
ATOM   1467 N N   . ARG   B 2 136 ? -26.912 -7.721  -22.775 1.00 48.97  ? 145 ARG   B N   1 
ATOM   1468 C CA  . ARG   B 2 136 ? -26.787 -7.674  -21.295 1.00 48.41  ? 145 ARG   B CA  1 
ATOM   1469 C C   . ARG   B 2 136 ? -25.432 -7.099  -20.886 1.00 45.77  ? 145 ARG   B C   1 
ATOM   1470 O O   . ARG   B 2 136 ? -24.403 -7.371  -21.538 1.00 42.98  ? 145 ARG   B O   1 
ATOM   1471 C CB  . ARG   B 2 136 ? -27.056 -9.064  -20.749 1.00 53.20  ? 145 ARG   B CB  1 
ATOM   1472 C CG  . ARG   B 2 136 ? -28.492 -9.500  -20.997 1.00 61.85  ? 145 ARG   B CG  1 
ATOM   1473 C CD  . ARG   B 2 136 ? -28.737 -10.868 -20.426 1.00 67.08  ? 145 ARG   B CD  1 
ATOM   1474 N NE  . ARG   B 2 136 ? -27.807 -11.708 -21.147 1.00 79.97  ? 145 ARG   B NE  1 
ATOM   1475 C CZ  . ARG   B 2 136 ? -27.319 -12.866 -20.733 1.00 88.36  ? 145 ARG   B CZ  1 
ATOM   1476 N NH1 . ARG   B 2 136 ? -27.657 -13.381 -19.557 1.00 90.01  ? 145 ARG   B NH1 1 
ATOM   1477 N NH2 . ARG   B 2 136 ? -26.470 -13.499 -21.521 1.00 86.65  ? 145 ARG   B NH2 1 
ATOM   1478 N N   . VAL   B 2 137 ? -25.431 -6.308  -19.816 1.00 40.80  ? 146 VAL   B N   1 
ATOM   1479 C CA  . VAL   B 2 137 ? -24.216 -5.603  -19.349 1.00 39.55  ? 146 VAL   B CA  1 
ATOM   1480 C C   . VAL   B 2 137 ? -23.459 -6.642  -18.520 1.00 39.22  ? 146 VAL   B C   1 
ATOM   1481 O O   . VAL   B 2 137 ? -24.015 -7.133  -17.554 1.00 41.75  ? 146 VAL   B O   1 
ATOM   1482 C CB  . VAL   B 2 137 ? -24.545 -4.322  -18.549 1.00 38.27  ? 146 VAL   B CB  1 
ATOM   1483 C CG1 . VAL   B 2 137 ? -23.285 -3.624  -18.113 1.00 37.19  ? 146 VAL   B CG1 1 
ATOM   1484 C CG2 . VAL   B 2 137 ? -25.398 -3.357  -19.372 1.00 43.26  ? 146 VAL   B CG2 1 
ATOM   1485 N N   . ILE   B 2 138 ? -22.253 -6.961  -18.926 1.00 44.77  ? 147 ILE   B N   1 
ATOM   1486 C CA  . ILE   B 2 138 ? -21.393 -7.986  -18.262 1.00 44.02  ? 147 ILE   B CA  1 
ATOM   1487 C C   . ILE   B 2 138 ? -20.413 -7.261  -17.342 1.00 39.88  ? 147 ILE   B C   1 
ATOM   1488 O O   . ILE   B 2 138 ? -19.631 -7.948  -16.657 1.00 35.77  ? 147 ILE   B O   1 
ATOM   1489 C CB  . ILE   B 2 138 ? -20.676 -8.881  -19.308 1.00 38.49  ? 147 ILE   B CB  1 
ATOM   1490 C CG1 . ILE   B 2 138 ? -19.906 -8.085  -20.350 1.00 42.82  ? 147 ILE   B CG1 1 
ATOM   1491 C CG2 . ILE   B 2 138 ? -21.661 -9.827  -19.934 1.00 38.36  ? 147 ILE   B CG2 1 
ATOM   1492 C CD1 . ILE   B 2 138 ? -18.764 -8.846  -20.995 1.00 50.82  ? 147 ILE   B CD1 1 
ATOM   1493 N N   . GLY   B 2 139 ? -20.470 -5.925  -17.302 1.00 37.37  ? 148 GLY   B N   1 
ATOM   1494 C CA  . GLY   B 2 139 ? -19.572 -5.140  -16.454 1.00 34.15  ? 148 GLY   B CA  1 
ATOM   1495 C C   . GLY   B 2 139 ? -19.272 -3.769  -16.971 1.00 34.56  ? 148 GLY   B C   1 
ATOM   1496 O O   . GLY   B 2 139 ? -19.744 -3.394  -18.059 1.00 38.68  ? 148 GLY   B O   1 
ATOM   1497 N N   . LEU   B 2 140 ? -18.492 -3.044  -16.197 1.00 33.45  ? 149 LEU   B N   1 
ATOM   1498 C CA  . LEU   B 2 140 ? -18.186 -1.625  -16.428 1.00 35.88  ? 149 LEU   B CA  1 
ATOM   1499 C C   . LEU   B 2 140 ? -16.705 -1.498  -16.670 1.00 37.92  ? 149 LEU   B C   1 
ATOM   1500 O O   . LEU   B 2 140 ? -15.879 -2.286  -16.044 1.00 34.53  ? 149 LEU   B O   1 
ATOM   1501 C CB  . LEU   B 2 140 ? -18.611 -0.717  -15.260 1.00 33.04  ? 149 LEU   B CB  1 
ATOM   1502 C CG  . LEU   B 2 140 ? -20.091 -0.782  -14.904 1.00 34.58  ? 149 LEU   B CG  1 
ATOM   1503 C CD1 . LEU   B 2 140 ? -20.469 0.328   -13.926 1.00 38.31  ? 149 LEU   B CD1 1 
ATOM   1504 C CD2 . LEU   B 2 140 ? -20.988 -0.792  -16.136 1.00 38.50  ? 149 LEU   B CD2 1 
ATOM   1505 N N   . TYR   B 2 141 ? -16.424 -0.547  -17.561 1.00 32.03  ? 150 TYR   B N   1 
ATOM   1506 C CA  . TYR   B 2 141 ? -15.100 -0.133  -18.033 1.00 29.53  ? 150 TYR   B CA  1 
ATOM   1507 C C   . TYR   B 2 141 ? -14.560 0.916   -17.109 1.00 32.98  ? 150 TYR   B C   1 
ATOM   1508 O O   . TYR   B 2 141 ? -15.352 1.778   -16.761 1.00 44.51  ? 150 TYR   B O   1 
ATOM   1509 C CB  . TYR   B 2 141 ? -15.198 0.370   -19.482 1.00 37.10  ? 150 TYR   B CB  1 
ATOM   1510 C CG  . TYR   B 2 141 ? -13.916 0.911   -20.071 1.00 40.53  ? 150 TYR   B CG  1 
ATOM   1511 C CD1 . TYR   B 2 141 ? -13.606 2.258   -19.983 1.00 41.04  ? 150 TYR   B CD1 1 
ATOM   1512 C CD2 . TYR   B 2 141 ? -13.030 0.098   -20.764 1.00 46.30  ? 150 TYR   B CD2 1 
ATOM   1513 C CE1 . TYR   B 2 141 ? -12.423 2.772   -20.492 1.00 49.17  ? 150 TYR   B CE1 1 
ATOM   1514 C CE2 . TYR   B 2 141 ? -11.853 0.606   -21.312 1.00 45.43  ? 150 TYR   B CE2 1 
ATOM   1515 C CZ  . TYR   B 2 141 ? -11.548 1.947   -21.180 1.00 49.80  ? 150 TYR   B CZ  1 
ATOM   1516 O OH  . TYR   B 2 141 ? -10.397 2.485   -21.680 1.00 47.30  ? 150 TYR   B OH  1 
ATOM   1517 N N   . GLY   B 2 142 ? -13.272 0.853   -16.745 1.00 34.21  ? 151 GLY   B N   1 
ATOM   1518 C CA  . GLY   B 2 142 ? -12.527 2.012   -16.184 1.00 35.07  ? 151 GLY   B CA  1 
ATOM   1519 C C   . GLY   B 2 142 ? -11.787 1.792   -14.870 1.00 40.08  ? 151 GLY   B C   1 
ATOM   1520 O O   . GLY   B 2 142 ? -11.272 2.813   -14.295 1.00 44.25  ? 151 GLY   B O   1 
ATOM   1521 N N   . ASN   B 2 143 ? -11.585 0.544   -14.437 1.00 38.46  ? 152 ASN   B N   1 
ATOM   1522 C CA  . ASN   B 2 143 ? -10.557 0.246   -13.400 1.00 40.07  ? 152 ASN   B CA  1 
ATOM   1523 C C   . ASN   B 2 143 ? -9.609  -0.802  -13.991 1.00 32.45  ? 152 ASN   B C   1 
ATOM   1524 O O   . ASN   B 2 143 ? -10.100 -1.924  -14.313 1.00 34.19  ? 152 ASN   B O   1 
ATOM   1525 C CB  . ASN   B 2 143 ? -11.187 -0.273  -12.103 1.00 36.94  ? 152 ASN   B CB  1 
ATOM   1526 C CG  . ASN   B 2 143 ? -10.254 -0.334  -10.913 1.00 38.99  ? 152 ASN   B CG  1 
ATOM   1527 O OD1 . ASN   B 2 143 ? -9.354  0.495   -10.734 1.00 38.95  ? 152 ASN   B OD1 1 
ATOM   1528 N ND2 . ASN   B 2 143 ? -10.537 -1.288  -10.046 1.00 38.47  ? 152 ASN   B ND2 1 
ATOM   1529 N N   . GLY   B 2 144 ? -8.358  -0.431  -14.171 1.00 38.00  ? 153 GLY   B N   1 
ATOM   1530 C CA  . GLY   B 2 144 ? -7.332  -1.339  -14.738 1.00 45.98  ? 153 GLY   B CA  1 
ATOM   1531 C C   . GLY   B 2 144 ? -5.923  -0.811  -14.514 1.00 48.61  ? 153 GLY   B C   1 
ATOM   1532 O O   . GLY   B 2 144 ? -5.681  -0.207  -13.446 1.00 53.73  ? 153 GLY   B O   1 
ATOM   1533 N N   . VAL   B 2 145 ? -5.035  -1.010  -15.496 1.00 49.66  ? 154 VAL   B N   1 
ATOM   1534 C CA  . VAL   B 2 145 ? -3.562  -0.989  -15.297 1.00 48.40  ? 154 VAL   B CA  1 
ATOM   1535 C C   . VAL   B 2 145 ? -2.888  -0.603  -16.622 1.00 56.54  ? 154 VAL   B C   1 
ATOM   1536 O O   . VAL   B 2 145 ? -3.404  -0.973  -17.704 1.00 53.18  ? 154 VAL   B O   1 
ATOM   1537 C CB  . VAL   B 2 145 ? -3.082  -2.345  -14.726 1.00 55.68  ? 154 VAL   B CB  1 
ATOM   1538 C CG1 . VAL   B 2 145 ? -3.079  -3.495  -15.732 1.00 50.43  ? 154 VAL   B CG1 1 
ATOM   1539 C CG2 . VAL   B 2 145 ? -1.722  -2.206  -14.073 1.00 58.10  ? 154 VAL   B CG2 1 
ATOM   1540 N N   . VAL   B 2 146 ? -1.800  0.158   -16.529 1.00 59.21  ? 155 VAL   B N   1 
ATOM   1541 C CA  . VAL   B 2 146 ? -0.994  0.615   -17.692 1.00 68.33  ? 155 VAL   B CA  1 
ATOM   1542 C C   . VAL   B 2 146 ? 0.141   -0.399  -17.883 1.00 69.32  ? 155 VAL   B C   1 
ATOM   1543 O O   . VAL   B 2 146 ? 0.917   -0.542  -16.942 1.00 62.20  ? 155 VAL   B O   1 
ATOM   1544 C CB  . VAL   B 2 146 ? -0.488  2.053   -17.486 1.00 70.86  ? 155 VAL   B CB  1 
ATOM   1545 C CG1 . VAL   B 2 146 ? 0.067   2.612   -18.781 1.00 74.83  ? 155 VAL   B CG1 1 
ATOM   1546 C CG2 . VAL   B 2 146 ? -1.581  2.976   -16.954 1.00 72.43  ? 155 VAL   B CG2 1 
ATOM   1547 N N   . ILE   B 2 147 ? 0.187   -1.115  -19.021 1.00 73.48  ? 156 ILE   B N   1 
ATOM   1548 C CA  . ILE   B 2 147 ? 1.024   -2.347  -19.187 1.00 72.30  ? 156 ILE   B CA  1 
ATOM   1549 C C   . ILE   B 2 147 ? 2.423   -1.952  -19.677 1.00 78.01  ? 156 ILE   B C   1 
ATOM   1550 O O   . ILE   B 2 147 ? 2.649   -0.754  -19.950 1.00 68.27  ? 156 ILE   B O   1 
ATOM   1551 C CB  . ILE   B 2 147 ? 0.353   -3.418  -20.084 1.00 75.06  ? 156 ILE   B CB  1 
ATOM   1552 C CG1 . ILE   B 2 147 ? 0.108   -2.966  -21.529 1.00 73.49  ? 156 ILE   B CG1 1 
ATOM   1553 C CG2 . ILE   B 2 147 ? -0.926  -3.928  -19.441 1.00 80.95  ? 156 ILE   B CG2 1 
ATOM   1554 C CD1 . ILE   B 2 147 ? -0.059  -4.122  -22.491 1.00 67.91  ? 156 ILE   B CD1 1 
ATOM   1555 N N   A LYS   B 2 148 ? 3.329   -2.941  -19.760 0.25 82.69  ? 157 LYS   B N   1 
ATOM   1556 N N   B LYS   B 2 148 ? 3.329   -2.941  -19.760 0.25 82.69  ? 157 LYS   B N   1 
ATOM   1557 N N   C LYS   B 2 148 ? 3.321   -2.941  -19.790 0.25 82.09  ? 157 LYS   B N   1 
ATOM   1558 N N   D LYS   B 2 148 ? 3.321   -2.941  -19.790 0.25 82.09  ? 157 LYS   B N   1 
ATOM   1559 C CA  A LYS   B 2 148 ? 4.741   -2.809  -20.225 0.25 87.03  ? 157 LYS   B CA  1 
ATOM   1560 C CA  B LYS   B 2 148 ? 4.741   -2.809  -20.225 0.25 87.03  ? 157 LYS   B CA  1 
ATOM   1561 C CA  C LYS   B 2 148 ? 4.744   -2.788  -20.207 0.25 85.88  ? 157 LYS   B CA  1 
ATOM   1562 C CA  D LYS   B 2 148 ? 4.744   -2.788  -20.207 0.25 85.88  ? 157 LYS   B CA  1 
ATOM   1563 C C   A LYS   B 2 148 ? 4.837   -1.777  -21.355 0.25 88.25  ? 157 LYS   B C   1 
ATOM   1564 C C   B LYS   B 2 148 ? 4.837   -1.777  -21.355 0.25 88.25  ? 157 LYS   B C   1 
ATOM   1565 C C   C LYS   B 2 148 ? 4.860   -1.799  -21.374 0.25 87.46  ? 157 LYS   B C   1 
ATOM   1566 C C   D LYS   B 2 148 ? 4.860   -1.799  -21.374 0.25 87.46  ? 157 LYS   B C   1 
ATOM   1567 O O   A LYS   B 2 148 ? 5.770   -0.954  -21.317 0.25 91.38  ? 157 LYS   B O   1 
ATOM   1568 O O   B LYS   B 2 148 ? 5.770   -0.954  -21.317 0.25 91.38  ? 157 LYS   B O   1 
ATOM   1569 O O   C LYS   B 2 148 ? 5.836   -1.027  -21.386 0.25 90.36  ? 157 LYS   B O   1 
ATOM   1570 O O   D LYS   B 2 148 ? 5.836   -1.027  -21.386 0.25 90.36  ? 157 LYS   B O   1 
ATOM   1571 C CB  A LYS   B 2 148 ? 5.272   -4.153  -20.736 0.25 89.40  ? 157 LYS   B CB  1 
ATOM   1572 C CB  B LYS   B 2 148 ? 5.272   -4.153  -20.736 0.25 89.40  ? 157 LYS   B CB  1 
ATOM   1573 C CB  C LYS   B 2 148 ? 5.324   -4.146  -20.619 0.25 87.20  ? 157 LYS   B CB  1 
ATOM   1574 C CB  D LYS   B 2 148 ? 5.324   -4.146  -20.619 0.25 87.20  ? 157 LYS   B CB  1 
ATOM   1575 C CG  A LYS   B 2 148 ? 5.477   -5.233  -19.682 0.25 88.30  ? 157 LYS   B CG  1 
ATOM   1576 C CG  B LYS   B 2 148 ? 5.477   -5.233  -19.682 0.25 88.30  ? 157 LYS   B CG  1 
ATOM   1577 C CG  C LYS   B 2 148 ? 4.428   -5.348  -20.339 0.25 86.91  ? 157 LYS   B CG  1 
ATOM   1578 C CG  D LYS   B 2 148 ? 4.428   -5.348  -20.339 0.25 86.91  ? 157 LYS   B CG  1 
ATOM   1579 C CD  A LYS   B 2 148 ? 5.227   -6.637  -20.205 0.25 88.79  ? 157 LYS   B CD  1 
ATOM   1580 C CD  B LYS   B 2 148 ? 5.227   -6.637  -20.205 0.25 88.79  ? 157 LYS   B CD  1 
ATOM   1581 C CD  C LYS   B 2 148 ? 3.501   -5.701  -21.488 0.25 82.92  ? 157 LYS   B CD  1 
ATOM   1582 C CD  D LYS   B 2 148 ? 3.501   -5.701  -21.488 0.25 82.92  ? 157 LYS   B CD  1 
ATOM   1583 C CE  A LYS   B 2 148 ? 6.088   -7.000  -21.399 0.25 87.80  ? 157 LYS   B CE  1 
ATOM   1584 C CE  B LYS   B 2 148 ? 6.088   -7.000  -21.399 0.25 87.80  ? 157 LYS   B CE  1 
ATOM   1585 C CE  C LYS   B 2 148 ? 4.245   -6.109  -22.744 0.25 81.81  ? 157 LYS   B CE  1 
ATOM   1586 C CE  D LYS   B 2 148 ? 4.245   -6.109  -22.744 0.25 81.81  ? 157 LYS   B CE  1 
ATOM   1587 N NZ  A LYS   B 2 148 ? 7.464   -7.367  -20.990 0.25 86.82  ? 157 LYS   B NZ  1 
ATOM   1588 N NZ  B LYS   B 2 148 ? 7.464   -7.367  -20.990 0.25 86.82  ? 157 LYS   B NZ  1 
ATOM   1589 N NZ  C LYS   B 2 148 ? 5.239   -7.178  -22.481 0.25 81.30  ? 157 LYS   B NZ  1 
ATOM   1590 N NZ  D LYS   B 2 148 ? 5.239   -7.178  -22.481 0.25 81.30  ? 157 LYS   B NZ  1 
ATOM   1591 N N   . ASN   B 2 149 ? 3.909   -1.840  -22.317 1.00 87.83  ? 158 ASN   B N   1 
ATOM   1592 C CA  . ASN   B 2 149 ? 3.857   -0.926  -23.497 1.00 87.23  ? 158 ASN   B CA  1 
ATOM   1593 C C   . ASN   B 2 149 ? 3.683   0.535   -23.063 1.00 86.30  ? 158 ASN   B C   1 
ATOM   1594 O O   . ASN   B 2 149 ? 4.402   1.384   -23.598 1.00 92.70  ? 158 ASN   B O   1 
ATOM   1595 C CB  . ASN   B 2 149 ? 2.730   -1.303  -24.469 1.00 84.33  ? 158 ASN   B CB  1 
ATOM   1596 C CG  . ASN   B 2 149 ? 2.465   -2.795  -24.547 1.00 88.03  ? 158 ASN   B CG  1 
ATOM   1597 O OD1 . ASN   B 2 149 ? 3.216   -3.611  -24.014 1.00 99.72  ? 158 ASN   B OD1 1 
ATOM   1598 N ND2 . ASN   B 2 149 ? 1.381   -3.169  -25.199 1.00 97.01  ? 158 ASN   B ND2 1 
ATOM   1599 N N   . GLY   B 2 150 ? 2.770   0.818   -22.126 1.00 91.87  ? 159 GLY   B N   1 
ATOM   1600 C CA  . GLY   B 2 150 ? 2.305   2.191   -21.812 1.00 81.39  ? 159 GLY   B CA  1 
ATOM   1601 C C   . GLY   B 2 150 ? 0.824   2.426   -22.120 1.00 75.98  ? 159 GLY   B C   1 
ATOM   1602 O O   . GLY   B 2 150 ? 0.295   3.530   -21.800 1.00 66.97  ? 159 GLY   B O   1 
ATOM   1603 N N   A SER   B 2 151 ? 0.172   1.419   -22.719 0.25 74.31  ? 160 SER   B N   1 
ATOM   1604 N N   B SER   B 2 151 ? 0.174   1.430   -22.733 0.25 73.13  ? 160 SER   B N   1 
ATOM   1605 N N   C SER   B 2 151 ? 0.172   1.419   -22.719 0.25 74.31  ? 160 SER   B N   1 
ATOM   1606 N N   D SER   B 2 151 ? 0.174   1.430   -22.733 0.25 73.13  ? 160 SER   B N   1 
ATOM   1607 C CA  A SER   B 2 151 ? -1.273  1.389   -23.069 0.25 71.03  ? 160 SER   B CA  1 
ATOM   1608 C CA  B SER   B 2 151 ? -1.275  1.409   -23.062 0.25 69.28  ? 160 SER   B CA  1 
ATOM   1609 C CA  C SER   B 2 151 ? -1.273  1.389   -23.069 0.25 71.03  ? 160 SER   B CA  1 
ATOM   1610 C CA  D SER   B 2 151 ? -1.275  1.409   -23.062 0.25 69.28  ? 160 SER   B CA  1 
ATOM   1611 C C   A SER   B 2 151 ? -2.092  0.897   -21.866 0.25 67.63  ? 160 SER   B C   1 
ATOM   1612 C C   B SER   B 2 151 ? -2.077  0.959   -21.834 0.25 66.56  ? 160 SER   B C   1 
ATOM   1613 C C   C SER   B 2 151 ? -2.092  0.897   -21.866 0.25 67.63  ? 160 SER   B C   1 
ATOM   1614 C C   D SER   B 2 151 ? -2.077  0.959   -21.834 0.25 66.56  ? 160 SER   B C   1 
ATOM   1615 O O   A SER   B 2 151 ? -1.527  0.177   -21.011 0.25 64.54  ? 160 SER   B O   1 
ATOM   1616 O O   B SER   B 2 151 ? -1.483  0.334   -20.926 0.25 63.83  ? 160 SER   B O   1 
ATOM   1617 O O   C SER   B 2 151 ? -1.527  0.177   -21.011 0.25 64.54  ? 160 SER   B O   1 
ATOM   1618 O O   D SER   B 2 151 ? -1.483  0.334   -20.926 0.25 63.83  ? 160 SER   B O   1 
ATOM   1619 C CB  A SER   B 2 151 ? -1.495  0.520   -24.285 0.25 68.60  ? 160 SER   B CB  1 
ATOM   1620 C CB  B SER   B 2 151 ? -1.531  0.506   -24.236 0.25 65.75  ? 160 SER   B CB  1 
ATOM   1621 C CB  C SER   B 2 151 ? -1.495  0.520   -24.285 0.25 68.60  ? 160 SER   B CB  1 
ATOM   1622 C CB  D SER   B 2 151 ? -1.531  0.506   -24.236 0.25 65.75  ? 160 SER   B CB  1 
ATOM   1623 O OG  A SER   B 2 151 ? -2.875  0.405   -24.594 0.25 69.97  ? 160 SER   B OG  1 
ATOM   1624 O OG  B SER   B 2 151 ? -1.013  -0.790  -23.979 0.25 64.77  ? 160 SER   B OG  1 
ATOM   1625 O OG  C SER   B 2 151 ? -2.875  0.405   -24.594 0.25 69.97  ? 160 SER   B OG  1 
ATOM   1626 O OG  D SER   B 2 151 ? -1.013  -0.790  -23.979 0.25 64.77  ? 160 SER   B OG  1 
ATOM   1627 N N   . TYR   B 2 152 ? -3.380  1.254   -21.829 1.00 65.20  ? 161 TYR   B N   1 
ATOM   1628 C CA  . TYR   B 2 152 ? -4.305  0.952   -20.707 1.00 57.26  ? 161 TYR   B CA  1 
ATOM   1629 C C   . TYR   B 2 152 ? -5.097  -0.317  -20.994 1.00 50.15  ? 161 TYR   B C   1 
ATOM   1630 O O   . TYR   B 2 152 ? -5.651  -0.498  -22.078 1.00 45.36  ? 161 TYR   B O   1 
ATOM   1631 C CB  . TYR   B 2 152 ? -5.246  2.137   -20.520 1.00 60.68  ? 161 TYR   B CB  1 
ATOM   1632 C CG  . TYR   B 2 152 ? -6.270  1.984   -19.427 1.00 58.67  ? 161 TYR   B CG  1 
ATOM   1633 C CD1 . TYR   B 2 152 ? -5.915  2.153   -18.096 1.00 51.88  ? 161 TYR   B CD1 1 
ATOM   1634 C CD2 . TYR   B 2 152 ? -7.594  1.695   -19.734 1.00 51.57  ? 161 TYR   B CD2 1 
ATOM   1635 C CE1 . TYR   B 2 152 ? -6.852  2.019   -17.083 1.00 51.76  ? 161 TYR   B CE1 1 
ATOM   1636 C CE2 . TYR   B 2 152 ? -8.552  1.602   -18.739 1.00 52.63  ? 161 TYR   B CE2 1 
ATOM   1637 C CZ  . TYR   B 2 152 ? -8.175  1.739   -17.404 1.00 56.64  ? 161 TYR   B CZ  1 
ATOM   1638 O OH  . TYR   B 2 152 ? -9.128  1.648   -16.419 1.00 48.38  ? 161 TYR   B OH  1 
ATOM   1639 N N   . VAL   B 2 153 ? -5.180  -1.186  -19.999 1.00 52.83  ? 162 VAL   B N   1 
ATOM   1640 C CA  . VAL   B 2 153 ? -6.117  -2.343  -20.024 1.00 46.24  ? 162 VAL   B CA  1 
ATOM   1641 C C   . VAL   B 2 153 ? -7.056  -2.225  -18.811 1.00 48.01  ? 162 VAL   B C   1 
ATOM   1642 O O   . VAL   B 2 153 ? -6.549  -2.087  -17.694 1.00 48.48  ? 162 VAL   B O   1 
ATOM   1643 C CB  . VAL   B 2 153 ? -5.331  -3.667  -20.067 1.00 46.68  ? 162 VAL   B CB  1 
ATOM   1644 C CG1 . VAL   B 2 153 ? -6.225  -4.901  -20.132 1.00 42.82  ? 162 VAL   B CG1 1 
ATOM   1645 C CG2 . VAL   B 2 153 ? -4.358  -3.657  -21.245 1.00 59.29  ? 162 VAL   B CG2 1 
ATOM   1646 N N   . SER   B 2 154 ? -8.366  -2.291  -19.052 1.00 50.01  ? 163 SER   B N   1 
ATOM   1647 C CA  . SER   B 2 154 ? -9.446  -2.249  -18.032 1.00 50.20  ? 163 SER   B CA  1 
ATOM   1648 C C   . SER   B 2 154 ? -9.871  -3.663  -17.663 1.00 45.14  ? 163 SER   B C   1 
ATOM   1649 O O   . SER   B 2 154 ? -10.060 -4.462  -18.544 1.00 40.49  ? 163 SER   B O   1 
ATOM   1650 C CB  . SER   B 2 154 ? -10.663 -1.460  -18.524 1.00 56.95  ? 163 SER   B CB  1 
ATOM   1651 O OG  . SER   B 2 154 ? -11.748 -1.502  -17.590 1.00 47.44  ? 163 SER   B OG  1 
ATOM   1652 N N   . ALA   B 2 155 ? -10.145 -3.917  -16.385 1.00 42.46  ? 164 ALA   B N   1 
ATOM   1653 C CA  . ALA   B 2 155 ? -11.026 -5.036  -16.002 1.00 37.50  ? 164 ALA   B CA  1 
ATOM   1654 C C   . ALA   B 2 155 ? -12.388 -4.865  -16.655 1.00 37.69  ? 164 ALA   B C   1 
ATOM   1655 O O   . ALA   B 2 155 ? -12.891 -3.706  -16.886 1.00 38.43  ? 164 ALA   B O   1 
ATOM   1656 C CB  . ALA   B 2 155 ? -11.167 -5.162  -14.495 1.00 42.78  ? 164 ALA   B CB  1 
ATOM   1657 N N   . ILE   B 2 156 ? -13.011 -5.999  -16.874 1.00 33.04  ? 165 ILE   B N   1 
ATOM   1658 C CA  . ILE   B 2 156 ? -14.486 -6.111  -16.922 1.00 37.97  ? 165 ILE   B CA  1 
ATOM   1659 C C   . ILE   B 2 156 ? -14.947 -6.244  -15.461 1.00 37.46  ? 165 ILE   B C   1 
ATOM   1660 O O   . ILE   B 2 156 ? -14.813 -7.343  -14.943 1.00 35.74  ? 165 ILE   B O   1 
ATOM   1661 C CB  . ILE   B 2 156 ? -14.914 -7.324  -17.749 1.00 37.29  ? 165 ILE   B CB  1 
ATOM   1662 C CG1 . ILE   B 2 156 ? -14.284 -7.301  -19.144 1.00 45.00  ? 165 ILE   B CG1 1 
ATOM   1663 C CG2 . ILE   B 2 156 ? -16.420 -7.368  -17.818 1.00 39.69  ? 165 ILE   B CG2 1 
ATOM   1664 C CD1 . ILE   B 2 156 ? -14.517 -8.542  -19.946 1.00 40.92  ? 165 ILE   B CD1 1 
ATOM   1665 N N   . THR   B 2 157 ? -15.409 -5.153  -14.831 1.00 37.89  ? 166 THR   B N   1 
ATOM   1666 C CA  . THR   B 2 157 ? -15.811 -5.124  -13.389 1.00 34.32  ? 166 THR   B CA  1 
ATOM   1667 C C   . THR   B 2 157 ? -17.319 -5.339  -13.325 1.00 34.51  ? 166 THR   B C   1 
ATOM   1668 O O   . THR   B 2 157 ? -18.087 -4.499  -13.897 1.00 37.06  ? 166 THR   B O   1 
ATOM   1669 C CB  . THR   B 2 157 ? -15.379 -3.832  -12.710 1.00 37.41  ? 166 THR   B CB  1 
ATOM   1670 O OG1 . THR   B 2 157 ? -13.976 -3.612  -12.853 1.00 34.13  ? 166 THR   B OG1 1 
ATOM   1671 C CG2 . THR   B 2 157 ? -15.793 -3.814  -11.254 1.00 36.55  ? 166 THR   B CG2 1 
ATOM   1672 N N   . GLN   B 2 158 ? -17.734 -6.436  -12.709 1.00 32.43  ? 167 GLN   B N   1 
ATOM   1673 C CA  . GLN   B 2 158 ? -19.150 -6.794  -12.496 1.00 34.77  ? 167 GLN   B CA  1 
ATOM   1674 C C   . GLN   B 2 158 ? -19.419 -6.940  -10.995 1.00 37.18  ? 167 GLN   B C   1 
ATOM   1675 O O   . GLN   B 2 158 ? -18.518 -7.432  -10.288 1.00 31.60  ? 167 GLN   B O   1 
ATOM   1676 C CB  . GLN   B 2 158 ? -19.507 -8.067  -13.204 1.00 34.02  ? 167 GLN   B CB  1 
ATOM   1677 C CG  . GLN   B 2 158 ? -20.979 -8.402  -13.139 1.00 34.32  ? 167 GLN   B CG  1 
ATOM   1678 C CD  . GLN   B 2 158 ? -21.884 -7.284  -13.646 1.00 42.93  ? 167 GLN   B CD  1 
ATOM   1679 O OE1 . GLN   B 2 158 ? -21.953 -6.188  -13.075 1.00 36.44  ? 167 GLN   B OE1 1 
ATOM   1680 N NE2 . GLN   B 2 158 ? -22.625 -7.571  -14.701 1.00 36.01  ? 167 GLN   B NE2 1 
ATOM   1681 N N   . GLY   B 2 159 ? -20.598 -6.508  -10.554 1.00 36.82  ? 168 GLY   B N   1 
ATOM   1682 C CA  . GLY   B 2 159 ? -21.017 -6.668  -9.147  1.00 44.17  ? 168 GLY   B CA  1 
ATOM   1683 C C   . GLY   B 2 159 ? -21.744 -7.982  -8.936  1.00 48.95  ? 168 GLY   B C   1 
ATOM   1684 O O   . GLY   B 2 159 ? -21.917 -8.764  -9.893  1.00 61.77  ? 168 GLY   B O   1 
ATOM   1685 N N   . LYS   B 2 160 ? -22.185 -8.208  -7.705  1.00 56.08  ? 169 LYS   B N   1 
ATOM   1686 C CA  . LYS   B 2 160 ? -23.054 -9.344  -7.301  1.00 61.13  ? 169 LYS   B CA  1 
ATOM   1687 C C   . LYS   B 2 160 ? -24.493 -8.817  -7.239  1.00 62.69  ? 169 LYS   B C   1 
ATOM   1688 O O   . LYS   B 2 160 ? -24.704 -7.733  -6.695  1.00 58.91  ? 169 LYS   B O   1 
ATOM   1689 C CB  . LYS   B 2 160 ? -22.578 -9.907  -5.954  1.00 69.84  ? 169 LYS   B CB  1 
ATOM   1690 C CG  . LYS   B 2 160 ? -22.869 -11.384 -5.737  1.00 86.37  ? 169 LYS   B CG  1 
ATOM   1691 C CD  . LYS   B 2 160 ? -22.466 -11.900 -4.371  1.00 89.59  ? 169 LYS   B CD  1 
ATOM   1692 C CE  . LYS   B 2 160 ? -23.082 -13.249 -4.061  1.00 91.41  ? 169 LYS   B CE  1 
ATOM   1693 N NZ  . LYS   B 2 160 ? -23.985 -13.173 -2.886  1.00 96.76  ? 169 LYS   B NZ  1 
ATOM   1694 N N   . ARG   B 2 161 ? -25.452 -9.535  -7.811  1.00 65.59  ? 170 ARG   B N   1 
ATOM   1695 C CA  . ARG   B 2 161 ? -26.897 -9.301  -7.564  1.00 73.73  ? 170 ARG   B CA  1 
ATOM   1696 C C   . ARG   B 2 161 ? -27.357 -10.233 -6.431  1.00 74.62  ? 170 ARG   B C   1 
ATOM   1697 O O   . ARG   B 2 161 ? -27.371 -11.456 -6.654  1.00 72.11  ? 170 ARG   B O   1 
ATOM   1698 C CB  . ARG   B 2 161 ? -27.686 -9.503  -8.863  1.00 68.52  ? 170 ARG   B CB  1 
ATOM   1699 C CG  . ARG   B 2 161 ? -29.163 -9.168  -8.737  1.00 65.48  ? 170 ARG   B CG  1 
ATOM   1700 C CD  . ARG   B 2 161 ? -29.986 -9.709  -9.878  1.00 64.88  ? 170 ARG   B CD  1 
ATOM   1701 N NE  . ARG   B 2 161 ? -31.374 -9.263  -9.787  1.00 68.93  ? 170 ARG   B NE  1 
ATOM   1702 C CZ  . ARG   B 2 161 ? -31.967 -8.373  -10.592 1.00 67.91  ? 170 ARG   B CZ  1 
ATOM   1703 N NH1 . ARG   B 2 161 ? -31.309 -7.797  -11.586 1.00 65.09  ? 170 ARG   B NH1 1 
ATOM   1704 N NH2 . ARG   B 2 161 ? -33.240 -8.069  -10.416 1.00 76.76  ? 170 ARG   B NH2 1 
ATOM   1705 N N   . GLU   B 2 162 ? -27.725 -9.674  -5.270  1.00 83.79  ? 171 GLU   B N   1 
ATOM   1706 C CA  . GLU   B 2 162 ? -28.265 -10.426 -4.098  1.00 94.18  ? 171 GLU   B CA  1 
ATOM   1707 C C   . GLU   B 2 162 ? -29.684 -10.928 -4.390  1.00 84.21  ? 171 GLU   B C   1 
ATOM   1708 O O   . GLU   B 2 162 ? -29.971 -12.063 -4.022  1.00 86.34  ? 171 GLU   B O   1 
ATOM   1709 C CB  . GLU   B 2 162 ? -28.255 -9.556  -2.840  1.00 102.93 ? 171 GLU   B CB  1 
ATOM   1710 C CG  . GLU   B 2 162 ? -26.855 -9.207  -2.346  1.00 114.62 ? 171 GLU   B CG  1 
ATOM   1711 C CD  . GLU   B 2 162 ? -25.933 -10.386 -2.052  1.00 122.92 ? 171 GLU   B CD  1 
ATOM   1712 O OE1 . GLU   B 2 162 ? -25.761 -10.716 -0.858  1.00 118.93 ? 171 GLU   B OE1 1 
ATOM   1713 O OE2 . GLU   B 2 162 ? -25.369 -10.965 -3.015  1.00 121.72 ? 171 GLU   B OE2 1 
HETATM 1714 S S   A DMS   C 3 .   ? -8.183  5.863   -17.790 0.16 85.51  ? 201 DMS   B S   1 
HETATM 1715 S S   B DMS   C 3 .   ? -8.182  5.861   -17.789 0.28 85.61  ? 201 DMS   B S   1 
HETATM 1716 O O   A DMS   C 3 .   ? -6.883  5.107   -17.845 0.16 89.09  ? 201 DMS   B O   1 
HETATM 1717 O O   B DMS   C 3 .   ? -6.880  5.108   -17.845 0.28 90.21  ? 201 DMS   B O   1 
HETATM 1718 C C1  A DMS   C 3 .   ? -8.805  5.658   -16.141 0.16 83.33  ? 201 DMS   B C1  1 
HETATM 1719 C C1  B DMS   C 3 .   ? -8.804  5.656   -16.140 0.28 82.54  ? 201 DMS   B C1  1 
HETATM 1720 C C2  A DMS   C 3 .   ? -9.384  4.855   -18.626 0.16 84.23  ? 201 DMS   B C2  1 
HETATM 1721 C C2  B DMS   C 3 .   ? -9.383  4.851   -18.624 0.28 83.82  ? 201 DMS   B C2  1 
HETATM 1722 S S   . DMS   D 3 .   ? -18.863 12.184  -0.278  1.00 84.12  ? 202 DMS   B S   1 
HETATM 1723 O O   . DMS   D 3 .   ? -19.362 10.760  -0.433  1.00 65.76  ? 202 DMS   B O   1 
HETATM 1724 C C1  . DMS   D 3 .   ? -20.124 13.242  -0.958  1.00 85.70  ? 202 DMS   B C1  1 
HETATM 1725 C C2  . DMS   D 3 .   ? -17.647 12.445  -1.548  1.00 75.89  ? 202 DMS   B C2  1 
HETATM 1726 S S   A DMS   E 3 .   ? -7.607  4.074   -13.360 0.16 121.28 ? 203 DMS   B S   1 
HETATM 1727 S S   B DMS   E 3 .   ? -7.604  4.079   -13.361 0.28 121.32 ? 203 DMS   B S   1 
HETATM 1728 O O   A DMS   E 3 .   ? -7.586  2.663   -13.879 0.16 121.65 ? 203 DMS   B O   1 
HETATM 1729 O O   B DMS   E 3 .   ? -7.583  2.670   -13.883 0.28 121.83 ? 203 DMS   B O   1 
HETATM 1730 C C1  A DMS   E 3 .   ? -8.628  4.043   -11.908 0.16 121.74 ? 203 DMS   B C1  1 
HETATM 1731 C C1  B DMS   E 3 .   ? -8.623  4.044   -11.907 0.28 121.93 ? 203 DMS   B C1  1 
HETATM 1732 C C2  A DMS   E 3 .   ? -6.044  4.322   -12.560 0.16 120.69 ? 203 DMS   B C2  1 
HETATM 1733 C C2  B DMS   E 3 .   ? -6.040  4.326   -12.565 0.28 120.45 ? 203 DMS   B C2  1 
HETATM 1734 N N1  C A1BXO F 4 .   ? -6.141  5.628   -15.722 0.28 44.08  ? 204 A1BXO B N1  1 
HETATM 1735 N N1  D A1BXO F 4 .   ? -6.141  5.628   -15.722 0.28 44.08  ? 204 A1BXO B N1  1 
HETATM 1736 N N3  C A1BXO F 4 .   ? -8.819  2.807   -7.942  0.28 34.78  1 204 A1BXO B N3  1 
HETATM 1737 N N3  D A1BXO F 4 .   ? -8.819  2.807   -7.942  0.28 34.78  1 204 A1BXO B N3  1 
HETATM 1738 C C4  C A1BXO F 4 .   ? -7.619  5.566   -17.653 0.28 43.38  ? 204 A1BXO B C4  1 
HETATM 1739 C C4  D A1BXO F 4 .   ? -7.619  5.566   -17.653 0.28 43.38  ? 204 A1BXO B C4  1 
HETATM 1740 C C5  C A1BXO F 4 .   ? -8.926  5.336   -18.152 0.28 41.41  ? 204 A1BXO B C5  1 
HETATM 1741 C C5  D A1BXO F 4 .   ? -8.926  5.336   -18.152 0.28 41.41  ? 204 A1BXO B C5  1 
HETATM 1742 C C6  C A1BXO F 4 .   ? -9.938  4.983   -17.313 0.28 41.41  ? 204 A1BXO B C6  1 
HETATM 1743 C C6  D A1BXO F 4 .   ? -9.938  4.983   -17.313 0.28 41.41  ? 204 A1BXO B C6  1 
HETATM 1744 C C7  C A1BXO F 4 .   ? -9.716  4.852   -15.935 0.28 38.23  ? 204 A1BXO B C7  1 
HETATM 1745 C C7  D A1BXO F 4 .   ? -9.716  4.852   -15.935 0.28 38.23  ? 204 A1BXO B C7  1 
HETATM 1746 C C8  C A1BXO F 4 .   ? -8.478  5.094   -15.394 0.28 39.16  ? 204 A1BXO B C8  1 
HETATM 1747 C C8  D A1BXO F 4 .   ? -8.478  5.094   -15.394 0.28 39.16  ? 204 A1BXO B C8  1 
HETATM 1748 C C10 C A1BXO F 4 .   ? -8.343  3.493   -11.985 0.28 36.68  ? 204 A1BXO B C10 1 
HETATM 1749 C C10 D A1BXO F 4 .   ? -8.343  3.493   -11.985 0.28 36.68  ? 204 A1BXO B C10 1 
HETATM 1750 C C13 C A1BXO F 4 .   ? -8.665  3.008   -9.419  0.28 34.24  ? 204 A1BXO B C13 1 
HETATM 1751 C C13 D A1BXO F 4 .   ? -8.665  3.008   -9.419  0.28 34.24  ? 204 A1BXO B C13 1 
HETATM 1752 C C15 C A1BXO F 4 .   ? -7.004  3.386   -11.262 0.28 34.56  ? 204 A1BXO B C15 1 
HETATM 1753 C C15 D A1BXO F 4 .   ? -7.004  3.386   -11.262 0.28 34.56  ? 204 A1BXO B C15 1 
HETATM 1754 C C17 C A1BXO F 4 .   ? -6.745  6.088   -19.984 0.28 46.89  ? 204 A1BXO B C17 1 
HETATM 1755 C C17 D A1BXO F 4 .   ? -6.745  6.088   -19.984 0.28 46.89  ? 204 A1BXO B C17 1 
HETATM 1756 C C1  C A1BXO F 4 .   ? -3.801  6.169   -15.883 0.28 42.51  ? 204 A1BXO B C1  1 
HETATM 1757 C C1  D A1BXO F 4 .   ? -3.801  6.168   -15.883 0.28 42.51  ? 204 A1BXO B C1  1 
HETATM 1758 C C2  C A1BXO F 4 .   ? -5.141  5.965   -16.522 0.28 42.55  ? 204 A1BXO B C2  1 
HETATM 1759 C C2  D A1BXO F 4 .   ? -5.141  5.965   -16.522 0.28 42.55  ? 204 A1BXO B C2  1 
HETATM 1760 C C3  C A1BXO F 4 .   ? -7.378  5.418   -16.256 0.28 41.11  ? 204 A1BXO B C3  1 
HETATM 1761 C C3  D A1BXO F 4 .   ? -7.378  5.418   -16.256 0.28 41.11  ? 204 A1BXO B C3  1 
HETATM 1762 N N2  C A1BXO F 4 .   ? -8.218  4.892   -14.028 0.28 37.56  ? 204 A1BXO B N2  1 
HETATM 1763 N N2  D A1BXO F 4 .   ? -8.218  4.892   -14.028 0.28 37.56  ? 204 A1BXO B N2  1 
HETATM 1764 C C9  C A1BXO F 4 .   ? -8.188  3.644   -13.492 0.28 34.97  ? 204 A1BXO B C9  1 
HETATM 1765 C C9  D A1BXO F 4 .   ? -8.188  3.644   -13.492 0.28 34.97  ? 204 A1BXO B C9  1 
HETATM 1766 O O1  C A1BXO F 4 .   ? -8.085  2.638   -14.179 0.28 37.61  ? 204 A1BXO B O1  1 
HETATM 1767 O O1  D A1BXO F 4 .   ? -8.085  2.638   -14.179 0.28 37.61  ? 204 A1BXO B O1  1 
HETATM 1768 C C11 C A1BXO F 4 .   ? -9.189  4.569   -11.318 0.28 34.28  ? 204 A1BXO B C11 1 
HETATM 1769 C C11 D A1BXO F 4 .   ? -9.189  4.569   -11.318 0.28 34.28  ? 204 A1BXO B C11 1 
HETATM 1770 C C12 C A1BXO F 4 .   ? -9.505  4.184   -9.877  0.28 34.39  ? 204 A1BXO B C12 1 
HETATM 1771 C C12 D A1BXO F 4 .   ? -9.505  4.184   -9.877  0.28 34.39  ? 204 A1BXO B C12 1 
HETATM 1772 C C14 C A1BXO F 4 .   ? -7.201  3.177   -9.767  0.28 35.21  ? 204 A1BXO B C14 1 
HETATM 1773 C C14 D A1BXO F 4 .   ? -7.201  3.177   -9.767  0.28 35.21  ? 204 A1BXO B C14 1 
HETATM 1774 C C16 C A1BXO F 4 .   ? -6.524  5.933   -18.496 0.28 45.44  ? 204 A1BXO B C16 1 
HETATM 1775 C C16 D A1BXO F 4 .   ? -6.524  5.933   -18.496 0.28 45.44  ? 204 A1BXO B C16 1 
HETATM 1776 O O2  C A1BXO F 4 .   ? -5.544  6.075   -20.750 0.28 50.54  ? 204 A1BXO B O2  1 
HETATM 1777 O O2  D A1BXO F 4 .   ? -5.544  6.075   -20.750 0.28 50.54  ? 204 A1BXO B O2  1 
HETATM 1778 C C18 C A1BXO F 4 .   ? -5.299  6.128   -17.916 0.28 43.61  ? 204 A1BXO B C18 1 
HETATM 1779 C C18 D A1BXO F 4 .   ? -5.299  6.128   -17.916 0.28 43.61  ? 204 A1BXO B C18 1 
HETATM 1780 O O   . HOH   G 5 .   ? -28.126 -5.603  -28.024 1.00 53.08  ? 101 HOH   A O   1 
HETATM 1781 O O   A HOH   G 5 .   ? -7.853  0.189   3.462   0.50 64.96  ? 102 HOH   A O   1 
HETATM 1782 O O   B HOH   G 5 .   ? -7.853  0.189   3.462   0.50 64.96  ? 102 HOH   A O   1 
HETATM 1783 O O   . HOH   G 5 .   ? -4.413  -13.734 -25.561 1.00 50.88  ? 103 HOH   A O   1 
HETATM 1784 O O   A HOH   G 5 .   ? -30.789 13.213  -16.432 0.50 67.37  ? 104 HOH   A O   1 
HETATM 1785 O O   B HOH   G 5 .   ? -30.789 13.213  -16.432 0.50 67.37  ? 104 HOH   A O   1 
HETATM 1786 O O   . HOH   G 5 .   ? -2.282  -3.422  -6.631  1.00 47.43  ? 105 HOH   A O   1 
HETATM 1787 O O   A HOH   G 5 .   ? -31.686 0.658   -29.145 0.50 58.95  ? 106 HOH   A O   1 
HETATM 1788 O O   B HOH   G 5 .   ? -31.686 0.658   -29.145 0.50 58.95  ? 106 HOH   A O   1 
HETATM 1789 O O   . HOH   G 5 .   ? -30.708 0.934   -22.963 1.00 49.52  ? 107 HOH   A O   1 
HETATM 1790 O O   . HOH   G 5 .   ? -23.912 19.384  -19.670 1.00 56.21  ? 108 HOH   A O   1 
HETATM 1791 O O   . HOH   G 5 .   ? -4.009  -3.424  -0.037  1.00 53.95  ? 109 HOH   A O   1 
HETATM 1792 O O   . HOH   G 5 .   ? -7.023  -8.669  -3.250  1.00 49.98  ? 110 HOH   A O   1 
HETATM 1793 O O   A HOH   G 5 .   ? -29.782 15.732  -14.934 0.50 63.19  ? 111 HOH   A O   1 
HETATM 1794 O O   B HOH   G 5 .   ? -29.782 15.732  -14.934 0.50 63.19  ? 111 HOH   A O   1 
HETATM 1795 O O   A HOH   G 5 .   ? -7.085  2.774   -9.123  0.16 54.13  ? 112 HOH   A O   1 
HETATM 1796 O O   B HOH   G 5 .   ? -7.102  2.776   -9.129  0.28 54.01  ? 112 HOH   A O   1 
HETATM 1797 O O   . HOH   G 5 .   ? -8.338  -1.615  6.399   1.00 54.78  ? 113 HOH   A O   1 
HETATM 1798 O O   . HOH   G 5 .   ? -22.831 -9.081  -34.539 1.00 52.17  ? 114 HOH   A O   1 
HETATM 1799 O O   . HOH   G 5 .   ? -3.147  -11.389 -7.188  1.00 50.05  ? 115 HOH   A O   1 
HETATM 1800 O O   . HOH   G 5 .   ? -4.537  -9.793  -5.719  1.00 52.32  ? 116 HOH   A O   1 
HETATM 1801 O O   C HOH   G 5 .   ? -6.313  -15.245 -25.400 0.50 56.75  ? 117 HOH   A O   1 
HETATM 1802 O O   D HOH   G 5 .   ? -6.313  -15.245 -25.400 0.50 56.75  ? 117 HOH   A O   1 
HETATM 1803 O O   A HOH   G 5 .   ? -27.242 -3.017  -35.390 0.50 76.22  ? 118 HOH   A O   1 
HETATM 1804 O O   B HOH   G 5 .   ? -27.242 -3.017  -35.390 0.50 76.22  ? 118 HOH   A O   1 
HETATM 1805 O O   A HOH   G 5 .   ? -3.845  -0.672  -0.626  0.50 65.81  ? 119 HOH   A O   1 
HETATM 1806 O O   B HOH   G 5 .   ? -3.845  -0.672  -0.626  0.50 65.81  ? 119 HOH   A O   1 
HETATM 1807 O O   . HOH   G 5 .   ? -2.822  -8.694  -3.353  1.00 64.30  ? 120 HOH   A O   1 
HETATM 1808 O O   . HOH   G 5 .   ? -4.183  2.283   -10.140 1.00 59.47  ? 121 HOH   A O   1 
HETATM 1809 O O   A HOH   H 5 .   ? -19.734 -11.924 -26.193 0.50 60.80  ? 301 HOH   B O   1 
HETATM 1810 O O   B HOH   H 5 .   ? -19.734 -11.924 -26.193 0.50 60.80  ? 301 HOH   B O   1 
HETATM 1811 O O   . HOH   H 5 .   ? -34.180 1.901   -15.031 1.00 49.98  ? 302 HOH   B O   1 
HETATM 1812 O O   . HOH   H 5 .   ? -26.085 -7.779  -16.689 1.00 46.88  ? 303 HOH   B O   1 
HETATM 1813 O O   . HOH   H 5 .   ? -15.988 -9.390  -15.295 1.00 53.37  ? 304 HOH   B O   1 
HETATM 1814 O O   . HOH   H 5 .   ? -30.863 13.297  -19.444 1.00 47.83  ? 305 HOH   B O   1 
HETATM 1815 O O   . HOH   H 5 .   ? -7.057  -10.534 -5.581  1.00 54.32  ? 306 HOH   B O   1 
HETATM 1816 O O   A HOH   H 5 .   ? -35.019 -2.002  -16.778 0.50 66.22  ? 307 HOH   B O   1 
HETATM 1817 O O   B HOH   H 5 .   ? -35.019 -2.002  -16.778 0.50 66.22  ? 307 HOH   B O   1 
HETATM 1818 O O   C HOH   H 5 .   ? -16.363 26.380  -12.378 0.50 55.59  ? 308 HOH   B O   1 
HETATM 1819 O O   D HOH   H 5 .   ? -16.363 26.380  -12.378 0.50 55.59  ? 308 HOH   B O   1 
HETATM 1820 O O   . HOH   H 5 .   ? -17.348 13.257  -5.585  1.00 65.27  ? 309 HOH   B O   1 
HETATM 1821 O O   A HOH   H 5 .   ? -9.593  2.354   -9.023  0.16 49.40  ? 310 HOH   B O   1 
HETATM 1822 O O   B HOH   H 5 .   ? -9.582  2.348   -9.032  0.28 49.32  ? 310 HOH   B O   1 
HETATM 1823 O O   A HOH   H 5 .   ? -9.668  -6.287  -25.277 0.50 67.22  ? 311 HOH   B O   1 
HETATM 1824 O O   B HOH   H 5 .   ? -9.668  -6.287  -25.277 0.50 67.22  ? 311 HOH   B O   1 
HETATM 1825 O O   . HOH   H 5 .   ? -6.661  -0.322  -11.061 1.00 43.33  ? 312 HOH   B O   1 
HETATM 1826 O O   . HOH   H 5 .   ? -12.167 2.654   -5.974  1.00 41.49  ? 313 HOH   B O   1 
HETATM 1827 O O   . HOH   H 5 .   ? -16.901 21.181  -14.273 1.00 51.72  ? 314 HOH   B O   1 
HETATM 1828 O O   A HOH   H 5 .   ? -29.053 -3.772  -22.181 0.50 64.85  ? 315 HOH   B O   1 
HETATM 1829 O O   B HOH   H 5 .   ? -29.053 -3.772  -22.181 0.50 64.85  ? 315 HOH   B O   1 
HETATM 1830 O O   A HOH   H 5 .   ? -28.018 -6.779  -5.506  0.50 60.78  ? 316 HOH   B O   1 
HETATM 1831 O O   B HOH   H 5 .   ? -28.018 -6.779  -5.506  0.50 60.78  ? 316 HOH   B O   1 
HETATM 1832 O O   C HOH   H 5 .   ? -21.545 14.326  -34.309 0.50 56.84  ? 317 HOH   B O   1 
HETATM 1833 O O   D HOH   H 5 .   ? -21.545 14.326  -34.309 0.50 56.84  ? 317 HOH   B O   1 
HETATM 1834 O O   A HOH   H 5 .   ? -12.575 -17.598 -27.951 0.50 61.33  ? 318 HOH   B O   1 
HETATM 1835 O O   B HOH   H 5 .   ? -12.575 -17.598 -27.951 0.50 61.33  ? 318 HOH   B O   1 
HETATM 1836 O O   . HOH   H 5 .   ? -11.916 12.216  -19.668 1.00 49.87  ? 319 HOH   B O   1 
HETATM 1837 O O   . HOH   H 5 .   ? -13.450 -1.903  -14.931 1.00 38.00  ? 320 HOH   B O   1 
HETATM 1838 O O   C HOH   H 5 .   ? -23.029 -6.083  -5.360  0.50 55.71  ? 321 HOH   B O   1 
HETATM 1839 O O   D HOH   H 5 .   ? -23.029 -6.083  -5.360  0.50 55.71  ? 321 HOH   B O   1 
HETATM 1840 O O   . HOH   H 5 .   ? -15.314 -4.044  1.350   1.00 38.84  ? 322 HOH   B O   1 
HETATM 1841 O O   . HOH   H 5 .   ? -15.391 9.800   -1.012  1.00 49.43  ? 323 HOH   B O   1 
HETATM 1842 O O   A HOH   H 5 .   ? -24.850 2.505   -29.727 0.50 63.50  ? 324 HOH   B O   1 
HETATM 1843 O O   B HOH   H 5 .   ? -24.850 2.505   -29.727 0.50 63.50  ? 324 HOH   B O   1 
HETATM 1844 O O   . HOH   H 5 .   ? -21.275 7.736   -0.000  0.50 51.62  ? 325 HOH   B O   1 
HETATM 1845 O O   A HOH   H 5 .   ? -35.459 -4.978  -10.165 0.50 61.82  ? 326 HOH   B O   1 
HETATM 1846 O O   B HOH   H 5 .   ? -35.459 -4.978  -10.165 0.50 61.82  ? 326 HOH   B O   1 
HETATM 1847 O O   . HOH   H 5 .   ? -22.137 -13.167 -21.621 1.00 50.22  ? 327 HOH   B O   1 
HETATM 1848 O O   . HOH   H 5 .   ? -16.930 -14.487 -16.344 1.00 48.99  ? 328 HOH   B O   1 
HETATM 1849 O O   A HOH   H 5 .   ? -29.840 -0.875  -18.729 0.50 80.35  ? 329 HOH   B O   1 
HETATM 1850 O O   B HOH   H 5 .   ? -29.840 -0.875  -18.729 0.50 80.35  ? 329 HOH   B O   1 
HETATM 1851 O O   . HOH   H 5 .   ? -24.168 9.844   -27.489 1.00 50.82  ? 330 HOH   B O   1 
HETATM 1852 O O   . HOH   H 5 .   ? -12.662 -3.123  -10.203 1.00 36.54  ? 331 HOH   B O   1 
HETATM 1853 O O   . HOH   H 5 .   ? -8.613  -10.340 -7.560  1.00 54.09  ? 332 HOH   B O   1 
HETATM 1854 O O   . HOH   H 5 .   ? -14.858 -5.841  -2.031  1.00 55.77  ? 333 HOH   B O   1 
HETATM 1855 O O   . HOH   H 5 .   ? -21.992 -12.023 -12.776 1.00 50.55  ? 334 HOH   B O   1 
HETATM 1856 O O   A HOH   H 5 .   ? -17.473 15.602  -30.762 0.50 65.52  ? 335 HOH   B O   1 
HETATM 1857 O O   B HOH   H 5 .   ? -17.473 15.602  -30.762 0.50 65.52  ? 335 HOH   B O   1 
HETATM 1858 O O   . HOH   H 5 .   ? -17.526 -13.883 -30.694 1.00 61.74  ? 336 HOH   B O   1 
HETATM 1859 O O   A HOH   H 5 .   ? -24.156 -14.336 -17.554 0.50 63.62  ? 337 HOH   B O   1 
HETATM 1860 O O   B HOH   H 5 .   ? -24.156 -14.336 -17.554 0.50 63.62  ? 337 HOH   B O   1 
HETATM 1861 O O   . HOH   H 5 .   ? -32.010 7.441   -4.492  1.00 59.76  ? 338 HOH   B O   1 
HETATM 1862 O O   . HOH   H 5 .   ? -19.237 -5.142  -0.873  1.00 45.03  ? 339 HOH   B O   1 
HETATM 1863 O O   . HOH   H 5 .   ? -15.583 16.791  -20.324 1.00 48.69  ? 340 HOH   B O   1 
HETATM 1864 O O   . HOH   H 5 .   ? -26.103 -4.127  -3.950  1.00 44.60  ? 341 HOH   B O   1 
HETATM 1865 O O   . HOH   H 5 .   ? -21.557 6.758   -32.908 1.00 66.84  ? 342 HOH   B O   1 
HETATM 1866 O O   . HOH   H 5 .   ? -35.584 5.112   -9.988  1.00 59.98  ? 343 HOH   B O   1 
HETATM 1867 O O   . HOH   H 5 .   ? -11.481 -4.753  -8.257  1.00 44.95  ? 344 HOH   B O   1 
HETATM 1868 O O   . HOH   H 5 .   ? -28.079 -5.889  -18.476 1.00 44.26  ? 345 HOH   B O   1 
HETATM 1869 O O   C HOH   H 5 .   ? -5.157  5.471   -12.952 0.28 40.21  ? 346 HOH   B O   1 
HETATM 1870 O O   D HOH   H 5 .   ? -5.157  5.471   -12.952 0.28 40.21  ? 346 HOH   B O   1 
HETATM 1871 O O   . HOH   H 5 .   ? -18.289 -10.579 -16.467 1.00 39.43  ? 347 HOH   B O   1 
HETATM 1872 O O   A HOH   H 5 .   ? -18.097 19.567  -22.152 0.50 65.43  ? 348 HOH   B O   1 
HETATM 1873 O O   B HOH   H 5 .   ? -18.097 19.567  -22.152 0.50 65.43  ? 348 HOH   B O   1 
HETATM 1874 O O   . HOH   H 5 .   ? -19.476 15.438  -22.396 1.00 44.28  ? 349 HOH   B O   1 
HETATM 1875 O O   A HOH   H 5 .   ? -11.319 8.231   -13.989 0.16 32.52  ? 350 HOH   B O   1 
HETATM 1876 O O   B HOH   H 5 .   ? -11.319 8.231   -13.990 0.28 32.36  ? 350 HOH   B O   1 
HETATM 1877 O O   . HOH   H 5 .   ? -14.969 -12.036 -16.613 1.00 60.99  ? 351 HOH   B O   1 
HETATM 1878 O O   . HOH   H 5 .   ? -30.894 4.847   -2.309  1.00 56.14  ? 352 HOH   B O   1 
HETATM 1879 O O   C HOH   H 5 .   ? -5.518  -9.858  -0.381  0.50 59.28  ? 353 HOH   B O   1 
HETATM 1880 O O   D HOH   H 5 .   ? -5.518  -9.858  -0.381  0.50 59.28  ? 353 HOH   B O   1 
HETATM 1881 O O   A HOH   H 5 .   ? -0.751  0.684   -13.662 0.50 71.21  ? 354 HOH   B O   1 
HETATM 1882 O O   B HOH   H 5 .   ? -0.751  0.684   -13.662 0.50 71.21  ? 354 HOH   B O   1 
HETATM 1883 O O   . HOH   H 5 .   ? -20.478 -7.424  -2.791  1.00 53.34  ? 355 HOH   B O   1 
HETATM 1884 O O   C HOH   H 5 .   ? -37.183 1.347   -18.577 0.50 60.17  ? 356 HOH   B O   1 
HETATM 1885 O O   D HOH   H 5 .   ? -37.183 1.347   -18.577 0.50 60.17  ? 356 HOH   B O   1 
HETATM 1886 O O   . HOH   H 5 .   ? -19.137 25.960  -14.437 1.00 57.82  ? 357 HOH   B O   1 
HETATM 1887 O O   . HOH   H 5 .   ? -7.348  -5.706  0.437   1.00 61.98  ? 358 HOH   B O   1 
HETATM 1888 O O   A HOH   H 5 .   ? -20.723 25.263  -16.740 0.50 75.09  ? 359 HOH   B O   1 
HETATM 1889 O O   B HOH   H 5 .   ? -20.723 25.263  -16.740 0.50 75.09  ? 359 HOH   B O   1 
HETATM 1890 O O   . HOH   H 5 .   ? -19.953 -12.969 -23.047 1.00 45.37  ? 360 HOH   B O   1 
HETATM 1891 O O   A HOH   H 5 .   ? -30.540 -8.111  -4.811  0.50 86.23  ? 361 HOH   B O   1 
HETATM 1892 O O   B HOH   H 5 .   ? -30.540 -8.111  -4.811  0.50 86.23  ? 361 HOH   B O   1 
HETATM 1893 O O   . HOH   H 5 .   ? -15.496 -7.101  -8.630  1.00 57.93  ? 362 HOH   B O   1 
HETATM 1894 O O   . HOH   H 5 .   ? -10.869 23.311  -12.798 1.00 59.39  ? 363 HOH   B O   1 
HETATM 1895 O O   . HOH   H 5 .   ? -1.787  -14.437 -9.796  1.00 57.69  ? 364 HOH   B O   1 
HETATM 1896 O O   . HOH   H 5 .   ? -29.510 -5.199  -0.675  1.00 57.02  ? 365 HOH   B O   1 
HETATM 1897 O O   A HOH   H 5 .   ? -17.571 17.026  -21.766 0.50 72.56  ? 366 HOH   B O   1 
HETATM 1898 O O   B HOH   H 5 .   ? -17.571 17.026  -21.766 0.50 72.56  ? 366 HOH   B O   1 
HETATM 1899 O O   . HOH   H 5 .   ? -23.697 -6.729  -2.061  1.00 58.53  ? 367 HOH   B O   1 
HETATM 1900 O O   C HOH   H 5 .   ? -29.309 -8.150  -18.311 0.50 68.16  ? 368 HOH   B O   1 
HETATM 1901 O O   D HOH   H 5 .   ? -29.309 -8.150  -18.311 0.50 68.16  ? 368 HOH   B O   1 
HETATM 1902 O O   A HOH   H 5 .   ? -31.657 -7.011  -6.336  0.50 70.57  ? 369 HOH   B O   1 
HETATM 1903 O O   B HOH   H 5 .   ? -31.657 -7.011  -6.336  0.50 70.57  ? 369 HOH   B O   1 
HETATM 1904 O O   A HOH   H 5 .   ? -30.751 -11.799 -27.060 0.25 74.50  ? 370 HOH   B O   1 
HETATM 1905 O O   B HOH   H 5 .   ? -30.751 -11.799 -27.060 0.25 74.50  ? 370 HOH   B O   1 
HETATM 1906 O O   A HOH   H 5 .   ? -19.404 -11.365 -13.811 0.50 61.49  ? 371 HOH   B O   1 
HETATM 1907 O O   B HOH   H 5 .   ? -19.404 -11.365 -13.811 0.50 61.49  ? 371 HOH   B O   1 
HETATM 1908 O O   C HOH   H 5 .   ? -21.618 16.164  -24.249 0.50 69.31  ? 372 HOH   B O   1 
HETATM 1909 O O   D HOH   H 5 .   ? -21.618 16.164  -24.249 0.50 69.31  ? 372 HOH   B O   1 
HETATM 1910 O O   . HOH   H 5 .   ? -17.521 27.839  -14.080 1.00 53.99  ? 373 HOH   B O   1 
HETATM 1911 O O   C HOH   H 5 .   ? -12.909 -6.524  -7.974  0.50 52.76  ? 374 HOH   B O   1 
HETATM 1912 O O   D HOH   H 5 .   ? -12.909 -6.524  -7.974  0.50 52.76  ? 374 HOH   B O   1 
HETATM 1913 O O   A HOH   H 5 .   ? -11.000 4.987   -5.524  0.16 42.35  ? 375 HOH   B O   1 
HETATM 1914 O O   B HOH   H 5 .   ? -11.014 4.986   -5.519  0.28 42.31  ? 375 HOH   B O   1 
HETATM 1915 O O   . HOH   H 5 .   ? -12.024 14.025  -14.461 1.00 63.23  ? 376 HOH   B O   1 
HETATM 1916 O O   A HOH   H 5 .   ? -21.275 4.532   0.000   0.20 77.03  ? 377 HOH   B O   1 
HETATM 1917 O O   B HOH   H 5 .   ? -21.275 4.527   0.000   0.28 76.85  ? 377 HOH   B O   1 
HETATM 1918 O O   A HOH   H 5 .   ? -12.331 -7.018  1.863   0.50 70.69  ? 378 HOH   B O   1 
HETATM 1919 O O   B HOH   H 5 .   ? -12.331 -7.018  1.863   0.50 70.69  ? 378 HOH   B O   1 
# 
