data_7I1S
# 
_entry.id   7I1S 
# 
_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   7I1S         pdb_00007i1s 10.2210/pdb7i1s/pdb 
WWPDB D_1001408207 ?            ?                   
# 
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                        7I1S 
_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    5  ?                           ?    ? ? 
4 non-polymer syn 'N-(quinolin-8-yl)piperidine-4-carboxamide' 255.315   1  ?                           ?    ? ? 
5 non-polymer syn 'SULFATE ION'                               96.063    1  ?                           ?    ? ? 
6 water       nat water                                       18.015    97 ?                           ?    ? ? 
# 
loop_
_entity_name_com.entity_id 
_entity_name_com.name 
1 'Flavivirin protease NS2B regulatory subunit,Non-structural protein 2B' 
2 'Flavivirin protease NS3 catalytic subunit,Non-structural protein 3'    
# 
loop_
_entity_poly.entity_id 
_entity_poly.type 
_entity_poly.nstd_linkage 
_entity_poly.nstd_monomer 
_entity_poly.pdbx_seq_one_letter_code 
_entity_poly.pdbx_seq_one_letter_code_can 
_entity_poly.pdbx_strand_id 
_entity_poly.pdbx_target_identifier 
1 'polypeptide(L)' no no SMGKSVDMYIERAGDITWEKDAEVTGNSPRLDVALDESGDFSLVEE SMGKSVDMYIERAGDITWEKDAEVTGNSPRLDVALDESGDFSLVEE A ? 
2 'polypeptide(L)' no no 
;MKEVKKGETTDGVYRVMTRRLLGSTQVGVGVMQEGVFHTMWHVTKGAALRSGEGRLDPYWGDVKQDLVSYCGPWKLDAAW
DGLSEVQLLAVPPGERAKNIQTLPGIFKTKDGDIGAVALDYPAGTSGSPILDKCGRVIGLYGNGVVIKNGSYVSAITQGK
REEETPVE
;
;MKEVKKGETTDGVYRVMTRRLLGSTQVGVGVMQEGVFHTMWHVTKGAALRSGEGRLDPYWGDVKQDLVSYCGPWKLDAAW
DGLSEVQLLAVPPGERAKNIQTLPGIFKTKDGDIGAVALDYPAGTSGSPILDKCGRVIGLYGNGVVIKNGSYVSAITQGK
REEETPVE
;
B ? 
# 
loop_
_pdbx_entity_nonpoly.entity_id 
_pdbx_entity_nonpoly.name 
_pdbx_entity_nonpoly.comp_id 
3 'DIMETHYL SULFOXIDE'                        DMS   
4 'N-(quinolin-8-yl)piperidine-4-carboxamide' A1BXL 
5 'SULFATE ION'                               SO4   
6 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 
A1BXL non-polymer         . 'N-(quinolin-8-yl)piperidine-4-carboxamide' ? 'C15 H17 N3 O'   255.315 
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 
SO4   non-polymer         . 'SULFATE ION'                               ? 'O4 S -2'        96.063  
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        A1BXL 
_pdbx_entity_instance_feature.asym_id        ? 
_pdbx_entity_instance_feature.seq_num        ? 
_pdbx_entity_instance_feature.auth_comp_id   A1BXL 
_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 A1BXL 1  204 301 A1BXL LIG B . 
G 5 SO4   1  205 302 SO4   SO4 B . 
H 3 DMS   1  206 303 DMS   DMS B . 
I 3 DMS   1  207 304 DMS   DMS B . 
J 6 HOH   1  101 98  HOH   HOH A . 
J 6 HOH   2  102 34  HOH   HOH A . 
J 6 HOH   3  103 128 HOH   HOH A . 
J 6 HOH   4  104 20  HOH   HOH A . 
J 6 HOH   5  105 40  HOH   HOH A . 
J 6 HOH   6  106 65  HOH   HOH A . 
J 6 HOH   7  107 16  HOH   HOH A . 
J 6 HOH   8  108 105 HOH   HOH A . 
J 6 HOH   9  109 118 HOH   HOH A . 
J 6 HOH   10 110 29  HOH   HOH A . 
J 6 HOH   11 111 121 HOH   HOH A . 
J 6 HOH   12 112 77  HOH   HOH A . 
J 6 HOH   13 113 120 HOH   HOH A . 
J 6 HOH   14 114 50  HOH   HOH A . 
J 6 HOH   15 115 87  HOH   HOH A . 
J 6 HOH   16 116 119 HOH   HOH A . 
J 6 HOH   17 117 110 HOH   HOH A . 
J 6 HOH   18 118 70  HOH   HOH A . 
J 6 HOH   19 119 54  HOH   HOH A . 
K 6 HOH   1  301 11  HOH   HOH B . 
K 6 HOH   2  302 59  HOH   HOH B . 
K 6 HOH   3  303 92  HOH   HOH B . 
K 6 HOH   4  304 90  HOH   HOH B . 
K 6 HOH   5  305 48  HOH   HOH B . 
K 6 HOH   6  306 5   HOH   HOH B . 
K 6 HOH   7  307 24  HOH   HOH B . 
K 6 HOH   8  308 56  HOH   HOH B . 
K 6 HOH   9  309 81  HOH   HOH B . 
K 6 HOH   10 310 32  HOH   HOH B . 
K 6 HOH   11 311 60  HOH   HOH B . 
K 6 HOH   12 312 10  HOH   HOH B . 
K 6 HOH   13 313 51  HOH   HOH B . 
K 6 HOH   14 314 39  HOH   HOH B . 
K 6 HOH   15 315 115 HOH   HOH B . 
K 6 HOH   16 316 85  HOH   HOH B . 
K 6 HOH   17 317 58  HOH   HOH B . 
K 6 HOH   18 318 89  HOH   HOH B . 
K 6 HOH   19 319 2   HOH   HOH B . 
K 6 HOH   20 320 124 HOH   HOH B . 
K 6 HOH   21 321 9   HOH   HOH B . 
K 6 HOH   22 322 108 HOH   HOH B . 
K 6 HOH   23 323 1   HOH   HOH B . 
K 6 HOH   24 324 36  HOH   HOH B . 
K 6 HOH   25 325 42  HOH   HOH B . 
K 6 HOH   26 326 18  HOH   HOH B . 
K 6 HOH   27 327 66  HOH   HOH B . 
K 6 HOH   28 328 46  HOH   HOH B . 
K 6 HOH   29 329 31  HOH   HOH B . 
K 6 HOH   30 330 17  HOH   HOH B . 
K 6 HOH   31 331 63  HOH   HOH B . 
K 6 HOH   32 332 107 HOH   HOH B . 
K 6 HOH   33 333 117 HOH   HOH B . 
K 6 HOH   34 334 126 HOH   HOH B . 
K 6 HOH   35 335 62  HOH   HOH B . 
K 6 HOH   36 336 67  HOH   HOH B . 
K 6 HOH   37 337 100 HOH   HOH B . 
K 6 HOH   38 338 68  HOH   HOH B . 
K 6 HOH   39 339 4   HOH   HOH B . 
K 6 HOH   40 340 35  HOH   HOH B . 
K 6 HOH   41 341 123 HOH   HOH B . 
K 6 HOH   42 342 14  HOH   HOH B . 
K 6 HOH   43 343 21  HOH   HOH B . 
K 6 HOH   44 344 28  HOH   HOH B . 
K 6 HOH   45 345 106 HOH   HOH B . 
K 6 HOH   46 346 72  HOH   HOH B . 
K 6 HOH   47 347 3   HOH   HOH B . 
K 6 HOH   48 348 116 HOH   HOH B . 
K 6 HOH   49 349 26  HOH   HOH B . 
K 6 HOH   50 350 12  HOH   HOH B . 
K 6 HOH   51 351 13  HOH   HOH B . 
K 6 HOH   52 352 122 HOH   HOH B . 
K 6 HOH   53 353 132 HOH   HOH B . 
K 6 HOH   54 354 43  HOH   HOH B . 
K 6 HOH   55 355 102 HOH   HOH B . 
K 6 HOH   56 356 82  HOH   HOH B . 
K 6 HOH   57 357 94  HOH   HOH B . 
K 6 HOH   58 358 69  HOH   HOH B . 
K 6 HOH   59 359 103 HOH   HOH B . 
K 6 HOH   60 360 30  HOH   HOH B . 
K 6 HOH   61 361 49  HOH   HOH B . 
K 6 HOH   62 362 80  HOH   HOH B . 
K 6 HOH   63 363 64  HOH   HOH B . 
K 6 HOH   64 364 73  HOH   HOH B . 
K 6 HOH   65 365 23  HOH   HOH B . 
K 6 HOH   66 366 79  HOH   HOH B . 
K 6 HOH   67 367 125 HOH   HOH B . 
K 6 HOH   68 368 109 HOH   HOH B . 
K 6 HOH   69 369 45  HOH   HOH B . 
K 6 HOH   70 370 61  HOH   HOH B . 
K 6 HOH   71 371 127 HOH   HOH B . 
K 6 HOH   72 372 83  HOH   HOH B . 
K 6 HOH   73 373 57  HOH   HOH B . 
K 6 HOH   74 374 112 HOH   HOH B . 
K 6 HOH   75 375 44  HOH   HOH B . 
K 6 HOH   76 376 27  HOH   HOH B . 
K 6 HOH   77 377 75  HOH   HOH B . 
K 6 HOH   78 378 129 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           7I1S 
_cell.length_a           42.466 
_cell.length_b           42.466 
_cell.length_c           215.566 
_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                         7I1S 
_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          7I1S 
_exptl.method            'X-RAY DIFFRACTION' 
_exptl.crystals_number   1 
# 
_exptl_crystal.id                    1 
_exptl_crystal.density_meas          ? 
_exptl_crystal.density_Matthews      2.10 
_exptl_crystal.density_percent_sol   41.31 
_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                     7I1S 
_reflns.pdbx_diffrn_id               1 
_reflns.pdbx_ordinal                 1 
_reflns.d_resolution_low             107.84 
_reflns.d_resolution_high            1.86 
_reflns.number_obs                   17704 
_reflns.percent_possible_obs         99.7 
_reflns.pdbx_Rmerge_I_obs            0.206 
_reflns.pdbx_netI_over_sigmaI        5.6 
_reflns.pdbx_redundancy              25.3 
_reflns.pdbx_Rrim_I_all              0.210 
_reflns.pdbx_Rpim_I_all              0.042 
_reflns.pdbx_CC_half                 0.998 
_reflns.pdbx_number_measured_all     447881 
_reflns.pdbx_chi_squared             0.24 
_reflns.observed_criterion_sigma_I   ? 
_reflns.observed_criterion_sigma_F   ? 
_reflns.number_all                   ? 
_reflns.pdbx_Rsym_value              ? 
_reflns.B_iso_Wilson_estimate        ? 
_reflns.pdbx_CC_star                 ? 
# 
_reflns_shell.pdbx_diffrn_id              1 
_reflns_shell.pdbx_ordinal                1 
_reflns_shell.d_res_high                  1.86 
_reflns_shell.d_res_low                   1.90 
_reflns_shell.number_measured_all         28495 
_reflns_shell.number_unique_obs           1055 
_reflns_shell.Rmerge_I_obs                6.358 
_reflns_shell.pdbx_chi_squared            0.03 
_reflns_shell.pdbx_redundancy             27.0 
_reflns_shell.percent_possible_obs        95.6 
_reflns_shell.pdbx_netI_over_sigmaI_obs   0.1 
_reflns_shell.pdbx_Rrim_I_all             6.479 
_reflns_shell.pdbx_Rpim_I_all             1.234 
_reflns_shell.pdbx_CC_half                0.443 
_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                                 7I1S 
_refine.pdbx_diffrn_id                           1 
_refine.pdbx_TLS_residual_ADP_flag               ? 
_refine.ls_number_reflns_obs                     14302 
_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                             53.89 
_refine.ls_d_res_high                            1.86 
_refine.ls_percent_reflns_obs                    85.35 
_refine.ls_R_factor_obs                          0.25508 
_refine.ls_R_factor_all                          ? 
_refine.ls_R_factor_R_work                       0.25160 
_refine.ls_R_factor_R_free                       0.32180 
_refine.ls_R_factor_R_free_error                 ? 
_refine.ls_R_factor_R_free_error_details         ? 
_refine.ls_percent_reflns_R_free                 4.7 
_refine.ls_number_reflns_R_free                  712 
_refine.ls_number_parameters                     ? 
_refine.ls_number_restraints                     ? 
_refine.occupancy_min                            ? 
_refine.occupancy_max                            ? 
_refine.correlation_coeff_Fo_to_Fc               0.945 
_refine.correlation_coeff_Fo_to_Fc_free          0.907 
_refine.B_iso_mean                               54.141 
_refine.aniso_B[1][1]                            0.79 
_refine.aniso_B[2][2]                            0.79 
_refine.aniso_B[3][3]                            -1.58 
_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                       0.287 
_refine.pdbx_overall_ESU_R_Free                  0.242 
_refine.overall_SU_ML                            0.344 
_refine.pdbx_overall_phase_error                 ? 
_refine.overall_SU_B                             13.159 
_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         44 
_refine_hist.number_atoms_solvent             97 
_refine_hist.number_atoms_total               1617 
_refine_hist.d_res_high                       1.86 
_refine_hist.d_res_low                        53.89 
# 
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             0.006  0.014  ? 2245 'X-RAY DIFFRACTION' ? 
r_bond_other_d               0.001  0.015  ? 1831 'X-RAY DIFFRACTION' ? 
r_angle_refined_deg          1.540  1.632  ? 2667 'X-RAY DIFFRACTION' ? 
r_angle_other_deg            1.129  1.589  ? 4230 'X-RAY DIFFRACTION' ? 
r_dihedral_angle_1_deg       7.836  5.000  ? 259  'X-RAY DIFFRACTION' ? 
r_dihedral_angle_2_deg       36.369 23.023 ? 86   'X-RAY DIFFRACTION' ? 
r_dihedral_angle_3_deg       17.630 15.000 ? 310  'X-RAY DIFFRACTION' ? 
r_dihedral_angle_4_deg       23.425 15.000 ? 10   'X-RAY DIFFRACTION' ? 
r_chiral_restr               0.055  0.200  ? 242  'X-RAY DIFFRACTION' ? 
r_gen_planes_refined         0.006  0.020  ? 2286 'X-RAY DIFFRACTION' ? 
r_gen_planes_other           0.002  0.020  ? 436  '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                  3.192  5.241  ? 1124 'X-RAY DIFFRACTION' ? 
r_mcbond_other               3.254  5.127  ? 1081 'X-RAY DIFFRACTION' ? 
r_mcangle_it                 5.089  7.564  ? 1251 'X-RAY DIFFRACTION' ? 
r_mcangle_other              5.088  7.567  ? 1252 'X-RAY DIFFRACTION' ? 
r_scbond_it                  3.201  6.125  ? 1121 'X-RAY DIFFRACTION' ? 
r_scbond_other               3.200  6.126  ? 1122 'X-RAY DIFFRACTION' ? 
r_scangle_it                 ?      ?      ? ?    'X-RAY DIFFRACTION' ? 
r_scangle_other              5.254  8.452  ? 1417 'X-RAY DIFFRACTION' ? 
r_long_range_B_refined       22.546 55.808 ? 2114 'X-RAY DIFFRACTION' ? 
r_long_range_B_other         22.651 55.670 ? 2092 '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                       1.862 
_refine_ls_shell.d_res_low                        1.910 
_refine_ls_shell.number_reflns_R_work             53 
_refine_ls_shell.R_factor_R_work                  0.344 
_refine_ls_shell.percent_reflns_obs               4.45 
_refine_ls_shell.R_factor_R_free                  0.225 
_refine_ls_shell.R_factor_R_free_error            ? 
_refine_ls_shell.percent_reflns_R_free            ? 
_refine_ls_shell.number_reflns_R_free             2 
_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                  7I1S 
_struct.title                     
'PanDDA analysis group deposition -- Crystal Structure of ZIKV NS2B-NS3 protease in complex with MFP-0012445-001-001' 
_struct.pdbx_model_details        ? 
_struct.pdbx_CASP_flag            ? 
_struct.pdbx_model_type_details   ? 
# 
_struct_keywords.entry_id        7I1S 
_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 3 ? 
I N N 3 ? 
J N N 6 ? 
K N N 6 ? 
# 
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 7I1S A 3 ? 46  ? Q32ZE1 1414 ? 1457 ? 46 89  
2 2 7I1S 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 7I1S SER A 1  ? UNP Q32ZE1 ?   ?    'expression tag'        44  1 
1 7I1S MET A 2  ? UNP Q32ZE1 ?   ?    'expression tag'        45  2 
2 7I1S MET B 1  ? UNP Q32ZE1 ?   ?    'initiating methionine' 10  3 
2 7I1S LYS B 98 ? UNP Q32ZE1 ARG 1605 conflict                107 4 
# 
_pdbx_struct_assembly.id                   1 
_pdbx_struct_assembly.details              author_defined_assembly 
_pdbx_struct_assembly.method_details       ? 
_pdbx_struct_assembly.oligomeric_details   dimeric 
_pdbx_struct_assembly.oligomeric_count     2 
# 
_pdbx_struct_assembly_gen.assembly_id       1 
_pdbx_struct_assembly_gen.oper_expression   1 
_pdbx_struct_assembly_gen.asym_id_list      A,B,C,D,E,F,G,H,I,J,K 
# 
_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               2.578 
_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 ? 6 ? 
AA2 ? 6 ? 
AA3 ? 2 ? 
AA4 ? 4 ? 
# 
loop_
_struct_sheet_order.sheet_id 
_struct_sheet_order.range_id_1 
_struct_sheet_order.range_id_2 
_struct_sheet_order.offset 
_struct_sheet_order.sense 
AA1 1 2 ? anti-parallel 
AA1 2 3 ? anti-parallel 
AA1 3 4 ? anti-parallel 
AA1 4 5 ? anti-parallel 
AA1 5 6 ? anti-parallel 
AA2 1 2 ? anti-parallel 
AA2 2 3 ? parallel      
AA2 3 4 ? anti-parallel 
AA2 4 5 ? anti-parallel 
AA2 5 6 ? anti-parallel 
AA3 1 2 ? anti-parallel 
AA4 1 2 ? anti-parallel 
AA4 2 3 ? anti-parallel 
AA4 3 4 ? anti-parallel 
# 
loop_
_struct_sheet_range.sheet_id 
_struct_sheet_range.id 
_struct_sheet_range.beg_label_comp_id 
_struct_sheet_range.beg_label_asym_id 
_struct_sheet_range.beg_label_seq_id 
_struct_sheet_range.pdbx_beg_PDB_ins_code 
_struct_sheet_range.end_label_comp_id 
_struct_sheet_range.end_label_asym_id 
_struct_sheet_range.end_label_seq_id 
_struct_sheet_range.pdbx_end_PDB_ins_code 
_struct_sheet_range.beg_auth_comp_id 
_struct_sheet_range.beg_auth_asym_id 
_struct_sheet_range.beg_auth_seq_id 
_struct_sheet_range.end_auth_comp_id 
_struct_sheet_range.end_auth_asym_id 
_struct_sheet_range.end_auth_seq_id 
AA1 1 MET A 8   ? GLY A 14  ? MET A 51  GLY A 57  
AA1 2 GLY B 12  ? THR B 18  ? GLY B 21  THR B 27  
AA1 3 THR B 25  ? GLN B 33  ? THR B 34  GLN B 42  
AA1 4 VAL B 36  ? THR B 39  ? VAL B 45  THR B 48  
AA1 5 LEU B 67  ? TYR B 70  ? LEU B 76  TYR B 79  
AA1 6 PRO B 58  ? ASP B 62  ? PRO B 67  ASP B 71  
AA2 1 PHE A 41  ? LEU A 43  ? PHE A 84  LEU A 86  
AA2 2 ARG A 30  ? LEU A 35  ? ARG A 73  LEU A 78  
AA2 3 GLY B 105 ? LYS B 108 ? GLY B 114 LYS B 117 
AA2 4 ASP B 113 ? VAL B 117 ? ASP B 122 VAL B 126 
AA2 5 TYR B 152 ? ALA B 155 ? TYR B 161 ALA B 164 
AA2 6 GLY B 144 ? VAL B 146 ? GLY B 153 VAL B 155 
AA3 1 LEU B 49  ? SER B 51  ? LEU B 58  SER B 60  
AA3 2 GLY B 54  ? LEU B 56  ? GLY B 63  LEU B 65  
AA4 1 LYS B 98  ? THR B 102 ? LYS B 107 THR B 111 
AA4 2 VAL B 86  ? ALA B 90  ? VAL B 95  ALA B 99  
AA4 3 PRO B 129 ? LEU B 131 ? PRO B 138 LEU B 140 
AA4 4 VAL B 137 ? LEU B 140 ? VAL B 146 LEU B 149 
# 
loop_
_pdbx_struct_sheet_hbond.sheet_id 
_pdbx_struct_sheet_hbond.range_id_1 
_pdbx_struct_sheet_hbond.range_id_2 
_pdbx_struct_sheet_hbond.range_1_label_atom_id 
_pdbx_struct_sheet_hbond.range_1_label_comp_id 
_pdbx_struct_sheet_hbond.range_1_label_asym_id 
_pdbx_struct_sheet_hbond.range_1_label_seq_id 
_pdbx_struct_sheet_hbond.range_1_PDB_ins_code 
_pdbx_struct_sheet_hbond.range_1_auth_atom_id 
_pdbx_struct_sheet_hbond.range_1_auth_comp_id 
_pdbx_struct_sheet_hbond.range_1_auth_asym_id 
_pdbx_struct_sheet_hbond.range_1_auth_seq_id 
_pdbx_struct_sheet_hbond.range_2_label_atom_id 
_pdbx_struct_sheet_hbond.range_2_label_comp_id 
_pdbx_struct_sheet_hbond.range_2_label_asym_id 
_pdbx_struct_sheet_hbond.range_2_label_seq_id 
_pdbx_struct_sheet_hbond.range_2_PDB_ins_code 
_pdbx_struct_sheet_hbond.range_2_auth_atom_id 
_pdbx_struct_sheet_hbond.range_2_auth_comp_id 
_pdbx_struct_sheet_hbond.range_2_auth_asym_id 
_pdbx_struct_sheet_hbond.range_2_auth_seq_id 
AA1 1 2 N ALA A 13  ? N ALA A 56  O VAL B 13  ? O VAL B 22  
AA1 2 3 N VAL B 16  ? N VAL B 25  O GLY B 28  ? O GLY B 37  
AA1 3 4 N VAL B 31  ? N VAL B 40  O HIS B 38  ? O HIS B 47  
AA1 4 5 N THR B 39  ? N THR B 48  O VAL B 68  ? O VAL B 77  
AA1 5 6 O SER B 69  ? O SER B 78  N TRP B 60  ? N TRP B 69  
AA2 1 2 O SER A 42  ? O SER A 85  N ALA A 34  ? N ALA A 77  
AA2 2 3 N LEU A 31  ? N LEU A 74  O LYS B 108 ? O LYS B 117 
AA2 3 4 N PHE B 107 ? N PHE B 116 O ILE B 114 ? O ILE B 123 
AA2 4 5 N VAL B 117 ? N VAL B 126 O SER B 154 ? O SER B 163 
AA2 5 6 O VAL B 153 ? O VAL B 162 N VAL B 145 ? N VAL B 154 
AA3 1 2 N SER B 51  ? N SER B 60  O GLY B 54  ? O GLY B 63  
AA4 1 2 O THR B 102 ? O THR B 111 N VAL B 86  ? N VAL B 95  
AA4 2 3 N GLN B 87  ? N GLN B 96  O LEU B 131 ? O LEU B 140 
AA4 3 4 N ILE B 130 ? N ILE B 139 O ILE B 138 ? O ILE B 147 
# 
_pdbx_entry_details.entry_id                   7I1S 
_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_close_contact.id 
_pdbx_validate_close_contact.PDB_model_num 
_pdbx_validate_close_contact.auth_atom_id_1 
_pdbx_validate_close_contact.auth_asym_id_1 
_pdbx_validate_close_contact.auth_comp_id_1 
_pdbx_validate_close_contact.auth_seq_id_1 
_pdbx_validate_close_contact.PDB_ins_code_1 
_pdbx_validate_close_contact.label_alt_id_1 
_pdbx_validate_close_contact.auth_atom_id_2 
_pdbx_validate_close_contact.auth_asym_id_2 
_pdbx_validate_close_contact.auth_comp_id_2 
_pdbx_validate_close_contact.auth_seq_id_2 
_pdbx_validate_close_contact.PDB_ins_code_2 
_pdbx_validate_close_contact.label_alt_id_2 
_pdbx_validate_close_contact.dist 
1 1 OD1 B ASP 20 ? ? O  B HOH 301 ? ? 1.86 
2 1 OD2 B ASP 90 ? ? OG B SER 93  ? ? 2.09 
# 
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 ASP A 64  ? C 84.11   34.82  
2  1 ASP A 64  ? D 84.11   34.82  
3  1 GLU A 66  ? A -67.44  79.78  
4  1 GLU A 66  ? B -67.44  79.78  
5  1 GLU A 66  ? C -48.94  107.01 
6  1 GLU A 66  ? D -48.94  107.01 
7  1 ASP B 71  ? ? -160.43 112.44 
8  1 CYS B 80  ? A 91.11   -21.26 
9  1 CYS B 80  ? B 91.11   -21.26 
10 1 LEU B 92  ? ? -130.96 -71.61 
11 1 LYS B 157 ? C -28.17  -45.97 
12 1 LYS B 157 ? D -28.17  -45.97 
# 
_pdbx_validate_peptide_omega.id               1 
_pdbx_validate_peptide_omega.PDB_model_num    1 
_pdbx_validate_peptide_omega.auth_comp_id_1   GLY 
_pdbx_validate_peptide_omega.auth_asym_id_1   B 
_pdbx_validate_peptide_omega.auth_seq_id_1    153 
_pdbx_validate_peptide_omega.PDB_ins_code_1   ? 
_pdbx_validate_peptide_omega.label_alt_id_1   ? 
_pdbx_validate_peptide_omega.auth_comp_id_2   VAL 
_pdbx_validate_peptide_omega.auth_asym_id_2   B 
_pdbx_validate_peptide_omega.auth_seq_id_2    154 
_pdbx_validate_peptide_omega.PDB_ins_code_2   ? 
_pdbx_validate_peptide_omega.label_alt_id_2   ? 
_pdbx_validate_peptide_omega.omega            -149.15 
# 
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 314 ? K HOH . 
2 1 B HOH 369 ? K HOH . 
3 1 B HOH 375 ? K HOH . 
# 
_pdbx_distant_solvent_atoms.id                                1 
_pdbx_distant_solvent_atoms.PDB_model_num                     1 
_pdbx_distant_solvent_atoms.auth_atom_id                      O 
_pdbx_distant_solvent_atoms.label_alt_id                      C 
_pdbx_distant_solvent_atoms.auth_asym_id                      B 
_pdbx_distant_solvent_atoms.auth_comp_id                      HOH 
_pdbx_distant_solvent_atoms.auth_seq_id                       378 
_pdbx_distant_solvent_atoms.PDB_ins_code                      ? 
_pdbx_distant_solvent_atoms.neighbor_macromolecule_distance   5.99 
_pdbx_distant_solvent_atoms.neighbor_ligand_distance          . 
# 
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 
A1BXL N1   N N N 1   
A1BXL N3   N N N 2   
A1BXL C4   C Y N 3   
A1BXL C5   C Y N 4   
A1BXL C6   C Y N 5   
A1BXL C7   C Y N 6   
A1BXL C8   C Y N 7   
A1BXL C10  C Y N 8   
A1BXL C13  C N N 9   
A1BXL C15  C N N 10  
A1BXL O1   O N N 11  
A1BXL C1   C N N 12  
A1BXL C2   C Y N 13  
A1BXL C3   C Y N 14  
A1BXL C9   C Y N 15  
A1BXL N2   N Y N 16  
A1BXL C11  C N N 17  
A1BXL C12  C N N 18  
A1BXL C14  C N N 19  
A1BXL H1   H N N 20  
A1BXL H13  H N N 21  
A1BXL H3   H N N 22  
A1BXL H4   H N N 23  
A1BXL H5   H N N 24  
A1BXL H6   H N N 25  
A1BXL H12  H N N 26  
A1BXL H11  H N N 27  
A1BXL H16  H N N 28  
A1BXL H17  H N N 29  
A1BXL H2   H N N 30  
A1BXL H7   H N N 31  
A1BXL H8   H N N 32  
A1BXL H9   H N N 33  
A1BXL H10  H N N 34  
A1BXL H14  H N N 35  
A1BXL H15  H N N 36  
ALA   N    N N N 37  
ALA   CA   C N S 38  
ALA   C    C N N 39  
ALA   O    O N N 40  
ALA   CB   C N N 41  
ALA   OXT  O N N 42  
ALA   H    H N N 43  
ALA   H2   H N N 44  
ALA   HA   H N N 45  
ALA   HB1  H N N 46  
ALA   HB2  H N N 47  
ALA   HB3  H N N 48  
ALA   HXT  H N N 49  
ARG   N    N N N 50  
ARG   CA   C N S 51  
ARG   C    C N N 52  
ARG   O    O N N 53  
ARG   CB   C N N 54  
ARG   CG   C N N 55  
ARG   CD   C N N 56  
ARG   NE   N N N 57  
ARG   CZ   C N N 58  
ARG   NH1  N N N 59  
ARG   NH2  N N N 60  
ARG   OXT  O N N 61  
ARG   H    H N N 62  
ARG   H2   H N N 63  
ARG   HA   H N N 64  
ARG   HB2  H N N 65  
ARG   HB3  H N N 66  
ARG   HG2  H N N 67  
ARG   HG3  H N N 68  
ARG   HD2  H N N 69  
ARG   HD3  H N N 70  
ARG   HE   H N N 71  
ARG   HH11 H N N 72  
ARG   HH12 H N N 73  
ARG   HH21 H N N 74  
ARG   HH22 H N N 75  
ARG   HXT  H N N 76  
ASN   N    N N N 77  
ASN   CA   C N S 78  
ASN   C    C N N 79  
ASN   O    O N N 80  
ASN   CB   C N N 81  
ASN   CG   C N N 82  
ASN   OD1  O N N 83  
ASN   ND2  N N N 84  
ASN   OXT  O N N 85  
ASN   H    H N N 86  
ASN   H2   H N N 87  
ASN   HA   H N N 88  
ASN   HB2  H N N 89  
ASN   HB3  H N N 90  
ASN   HD21 H N N 91  
ASN   HD22 H N N 92  
ASN   HXT  H N N 93  
ASP   N    N N N 94  
ASP   CA   C N S 95  
ASP   C    C N N 96  
ASP   O    O N N 97  
ASP   CB   C N N 98  
ASP   CG   C N N 99  
ASP   OD1  O N N 100 
ASP   OD2  O N N 101 
ASP   OXT  O N N 102 
ASP   H    H N N 103 
ASP   H2   H N N 104 
ASP   HA   H N N 105 
ASP   HB2  H N N 106 
ASP   HB3  H N N 107 
ASP   HD2  H N N 108 
ASP   HXT  H N N 109 
CYS   N    N N N 110 
CYS   CA   C N R 111 
CYS   C    C N N 112 
CYS   O    O N N 113 
CYS   CB   C N N 114 
CYS   SG   S N N 115 
CYS   OXT  O N N 116 
CYS   H    H N N 117 
CYS   H2   H N N 118 
CYS   HA   H N N 119 
CYS   HB2  H N N 120 
CYS   HB3  H N N 121 
CYS   HG   H N N 122 
CYS   HXT  H N N 123 
DMS   S    S N N 124 
DMS   O    O N N 125 
DMS   C1   C N N 126 
DMS   C2   C N N 127 
DMS   H11  H N N 128 
DMS   H12  H N N 129 
DMS   H13  H N N 130 
DMS   H21  H N N 131 
DMS   H22  H N N 132 
DMS   H23  H N N 133 
GLN   N    N N N 134 
GLN   CA   C N S 135 
GLN   C    C N N 136 
GLN   O    O N N 137 
GLN   CB   C N N 138 
GLN   CG   C N N 139 
GLN   CD   C N N 140 
GLN   OE1  O N N 141 
GLN   NE2  N N N 142 
GLN   OXT  O N N 143 
GLN   H    H N N 144 
GLN   H2   H N N 145 
GLN   HA   H N N 146 
GLN   HB2  H N N 147 
GLN   HB3  H N N 148 
GLN   HG2  H N N 149 
GLN   HG3  H N N 150 
GLN   HE21 H N N 151 
GLN   HE22 H N N 152 
GLN   HXT  H N N 153 
GLU   N    N N N 154 
GLU   CA   C N S 155 
GLU   C    C N N 156 
GLU   O    O N N 157 
GLU   CB   C N N 158 
GLU   CG   C N N 159 
GLU   CD   C N N 160 
GLU   OE1  O N N 161 
GLU   OE2  O N N 162 
GLU   OXT  O N N 163 
GLU   H    H N N 164 
GLU   H2   H N N 165 
GLU   HA   H N N 166 
GLU   HB2  H N N 167 
GLU   HB3  H N N 168 
GLU   HG2  H N N 169 
GLU   HG3  H N N 170 
GLU   HE2  H N N 171 
GLU   HXT  H N N 172 
GLY   N    N N N 173 
GLY   CA   C N N 174 
GLY   C    C N N 175 
GLY   O    O N N 176 
GLY   OXT  O N N 177 
GLY   H    H N N 178 
GLY   H2   H N N 179 
GLY   HA2  H N N 180 
GLY   HA3  H N N 181 
GLY   HXT  H N N 182 
HIS   N    N N N 183 
HIS   CA   C N S 184 
HIS   C    C N N 185 
HIS   O    O N N 186 
HIS   CB   C N N 187 
HIS   CG   C Y N 188 
HIS   ND1  N Y N 189 
HIS   CD2  C Y N 190 
HIS   CE1  C Y N 191 
HIS   NE2  N Y N 192 
HIS   OXT  O N N 193 
HIS   H    H N N 194 
HIS   H2   H N N 195 
HIS   HA   H N N 196 
HIS   HB2  H N N 197 
HIS   HB3  H N N 198 
HIS   HD1  H N N 199 
HIS   HD2  H N N 200 
HIS   HE1  H N N 201 
HIS   HE2  H N N 202 
HIS   HXT  H N N 203 
HOH   O    O N N 204 
HOH   H1   H N N 205 
HOH   H2   H N N 206 
ILE   N    N N N 207 
ILE   CA   C N S 208 
ILE   C    C N N 209 
ILE   O    O N N 210 
ILE   CB   C N S 211 
ILE   CG1  C N N 212 
ILE   CG2  C N N 213 
ILE   CD1  C N N 214 
ILE   OXT  O N N 215 
ILE   H    H N N 216 
ILE   H2   H N N 217 
ILE   HA   H N N 218 
ILE   HB   H N N 219 
ILE   HG12 H N N 220 
ILE   HG13 H N N 221 
ILE   HG21 H N N 222 
ILE   HG22 H N N 223 
ILE   HG23 H N N 224 
ILE   HD11 H N N 225 
ILE   HD12 H N N 226 
ILE   HD13 H N N 227 
ILE   HXT  H N N 228 
LEU   N    N N N 229 
LEU   CA   C N S 230 
LEU   C    C N N 231 
LEU   O    O N N 232 
LEU   CB   C N N 233 
LEU   CG   C N N 234 
LEU   CD1  C N N 235 
LEU   CD2  C N N 236 
LEU   OXT  O N N 237 
LEU   H    H N N 238 
LEU   H2   H N N 239 
LEU   HA   H N N 240 
LEU   HB2  H N N 241 
LEU   HB3  H N N 242 
LEU   HG   H N N 243 
LEU   HD11 H N N 244 
LEU   HD12 H N N 245 
LEU   HD13 H N N 246 
LEU   HD21 H N N 247 
LEU   HD22 H N N 248 
LEU   HD23 H N N 249 
LEU   HXT  H N N 250 
LYS   N    N N N 251 
LYS   CA   C N S 252 
LYS   C    C N N 253 
LYS   O    O N N 254 
LYS   CB   C N N 255 
LYS   CG   C N N 256 
LYS   CD   C N N 257 
LYS   CE   C N N 258 
LYS   NZ   N N N 259 
LYS   OXT  O N N 260 
LYS   H    H N N 261 
LYS   H2   H N N 262 
LYS   HA   H N N 263 
LYS   HB2  H N N 264 
LYS   HB3  H N N 265 
LYS   HG2  H N N 266 
LYS   HG3  H N N 267 
LYS   HD2  H N N 268 
LYS   HD3  H N N 269 
LYS   HE2  H N N 270 
LYS   HE3  H N N 271 
LYS   HZ1  H N N 272 
LYS   HZ2  H N N 273 
LYS   HZ3  H N N 274 
LYS   HXT  H N N 275 
MET   N    N N N 276 
MET   CA   C N S 277 
MET   C    C N N 278 
MET   O    O N N 279 
MET   CB   C N N 280 
MET   CG   C N N 281 
MET   SD   S N N 282 
MET   CE   C N N 283 
MET   OXT  O N N 284 
MET   H    H N N 285 
MET   H2   H N N 286 
MET   HA   H N N 287 
MET   HB2  H N N 288 
MET   HB3  H N N 289 
MET   HG2  H N N 290 
MET   HG3  H N N 291 
MET   HE1  H N N 292 
MET   HE2  H N N 293 
MET   HE3  H N N 294 
MET   HXT  H N N 295 
PHE   N    N N N 296 
PHE   CA   C N S 297 
PHE   C    C N N 298 
PHE   O    O N N 299 
PHE   CB   C N N 300 
PHE   CG   C Y N 301 
PHE   CD1  C Y N 302 
PHE   CD2  C Y N 303 
PHE   CE1  C Y N 304 
PHE   CE2  C Y N 305 
PHE   CZ   C Y N 306 
PHE   OXT  O N N 307 
PHE   H    H N N 308 
PHE   H2   H N N 309 
PHE   HA   H N N 310 
PHE   HB2  H N N 311 
PHE   HB3  H N N 312 
PHE   HD1  H N N 313 
PHE   HD2  H N N 314 
PHE   HE1  H N N 315 
PHE   HE2  H N N 316 
PHE   HZ   H N N 317 
PHE   HXT  H N N 318 
PRO   N    N N N 319 
PRO   CA   C N S 320 
PRO   C    C N N 321 
PRO   O    O N N 322 
PRO   CB   C N N 323 
PRO   CG   C N N 324 
PRO   CD   C N N 325 
PRO   OXT  O N N 326 
PRO   H    H N N 327 
PRO   HA   H N N 328 
PRO   HB2  H N N 329 
PRO   HB3  H N N 330 
PRO   HG2  H N N 331 
PRO   HG3  H N N 332 
PRO   HD2  H N N 333 
PRO   HD3  H N N 334 
PRO   HXT  H N N 335 
SER   N    N N N 336 
SER   CA   C N S 337 
SER   C    C N N 338 
SER   O    O N N 339 
SER   CB   C N N 340 
SER   OG   O N N 341 
SER   OXT  O N N 342 
SER   H    H N N 343 
SER   H2   H N N 344 
SER   HA   H N N 345 
SER   HB2  H N N 346 
SER   HB3  H N N 347 
SER   HG   H N N 348 
SER   HXT  H N N 349 
SO4   S    S N N 350 
SO4   O1   O N N 351 
SO4   O2   O N N 352 
SO4   O3   O N N 353 
SO4   O4   O N N 354 
THR   N    N N N 355 
THR   CA   C N S 356 
THR   C    C N N 357 
THR   O    O N N 358 
THR   CB   C N R 359 
THR   OG1  O N N 360 
THR   CG2  C N N 361 
THR   OXT  O N N 362 
THR   H    H N N 363 
THR   H2   H N N 364 
THR   HA   H N N 365 
THR   HB   H N N 366 
THR   HG1  H N N 367 
THR   HG21 H N N 368 
THR   HG22 H N N 369 
THR   HG23 H N N 370 
THR   HXT  H N N 371 
TRP   N    N N N 372 
TRP   CA   C N S 373 
TRP   C    C N N 374 
TRP   O    O N N 375 
TRP   CB   C N N 376 
TRP   CG   C Y N 377 
TRP   CD1  C Y N 378 
TRP   CD2  C Y N 379 
TRP   NE1  N Y N 380 
TRP   CE2  C Y N 381 
TRP   CE3  C Y N 382 
TRP   CZ2  C Y N 383 
TRP   CZ3  C Y N 384 
TRP   CH2  C Y N 385 
TRP   OXT  O N N 386 
TRP   H    H N N 387 
TRP   H2   H N N 388 
TRP   HA   H N N 389 
TRP   HB2  H N N 390 
TRP   HB3  H N N 391 
TRP   HD1  H N N 392 
TRP   HE1  H N N 393 
TRP   HE3  H N N 394 
TRP   HZ2  H N N 395 
TRP   HZ3  H N N 396 
TRP   HH2  H N N 397 
TRP   HXT  H N N 398 
TYR   N    N N N 399 
TYR   CA   C N S 400 
TYR   C    C N N 401 
TYR   O    O N N 402 
TYR   CB   C N N 403 
TYR   CG   C Y N 404 
TYR   CD1  C Y N 405 
TYR   CD2  C Y N 406 
TYR   CE1  C Y N 407 
TYR   CE2  C Y N 408 
TYR   CZ   C Y N 409 
TYR   OH   O N N 410 
TYR   OXT  O N N 411 
TYR   H    H N N 412 
TYR   H2   H N N 413 
TYR   HA   H N N 414 
TYR   HB2  H N N 415 
TYR   HB3  H N N 416 
TYR   HD1  H N N 417 
TYR   HD2  H N N 418 
TYR   HE1  H N N 419 
TYR   HE2  H N N 420 
TYR   HH   H N N 421 
TYR   HXT  H N N 422 
VAL   N    N N N 423 
VAL   CA   C N S 424 
VAL   C    C N N 425 
VAL   O    O N N 426 
VAL   CB   C N N 427 
VAL   CG1  C N N 428 
VAL   CG2  C N N 429 
VAL   OXT  O N N 430 
VAL   H    H N N 431 
VAL   H2   H N N 432 
VAL   HA   H N N 433 
VAL   HB   H N N 434 
VAL   HG11 H N N 435 
VAL   HG12 H N N 436 
VAL   HG13 H N N 437 
VAL   HG21 H N N 438 
VAL   HG22 H N N 439 
VAL   HG23 H N N 440 
VAL   HXT  H N N 441 
# 
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 
A1BXL O1  C1   doub N N 1   
A1BXL C1  N1   sing N N 2   
A1BXL N1  C2   sing N N 3   
A1BXL C2  C3   doub Y N 4   
A1BXL C3  C4   sing Y N 5   
A1BXL C4  C5   doub Y N 6   
A1BXL C5  C6   sing Y N 7   
A1BXL C6  C7   doub Y N 8   
A1BXL C7  C8   sing Y N 9   
A1BXL C8  C9   doub Y N 10  
A1BXL C9  N2   sing Y N 11  
A1BXL N2  C10  doub Y N 12  
A1BXL C1  C11  sing N N 13  
A1BXL C11 C12  sing N N 14  
A1BXL C12 C13  sing N N 15  
A1BXL C13 N3   sing N N 16  
A1BXL N3  C14  sing N N 17  
A1BXL C14 C15  sing N N 18  
A1BXL C2  C10  sing Y N 19  
A1BXL C11 C15  sing N N 20  
A1BXL C6  C10  sing Y N 21  
A1BXL N1  H1   sing N N 22  
A1BXL N3  H13  sing N N 23  
A1BXL C4  H3   sing N N 24  
A1BXL C5  H4   sing N N 25  
A1BXL C7  H5   sing N N 26  
A1BXL C8  H6   sing N N 27  
A1BXL C13 H12  sing N N 28  
A1BXL C13 H11  sing N N 29  
A1BXL C15 H16  sing N N 30  
A1BXL C15 H17  sing N N 31  
A1BXL C3  H2   sing N N 32  
A1BXL C9  H7   sing N N 33  
A1BXL C11 H8   sing N N 34  
A1BXL C12 H9   sing N N 35  
A1BXL C12 H10  sing N N 36  
A1BXL C14 H14  sing N N 37  
A1BXL C14 H15  sing N N 38  
ALA   N   CA   sing N N 39  
ALA   N   H    sing N N 40  
ALA   N   H2   sing N N 41  
ALA   CA  C    sing N N 42  
ALA   CA  CB   sing N N 43  
ALA   CA  HA   sing N N 44  
ALA   C   O    doub N N 45  
ALA   C   OXT  sing N N 46  
ALA   CB  HB1  sing N N 47  
ALA   CB  HB2  sing N N 48  
ALA   CB  HB3  sing N N 49  
ALA   OXT HXT  sing N N 50  
ARG   N   CA   sing N N 51  
ARG   N   H    sing N N 52  
ARG   N   H2   sing N N 53  
ARG   CA  C    sing N N 54  
ARG   CA  CB   sing N N 55  
ARG   CA  HA   sing N N 56  
ARG   C   O    doub N N 57  
ARG   C   OXT  sing N N 58  
ARG   CB  CG   sing N N 59  
ARG   CB  HB2  sing N N 60  
ARG   CB  HB3  sing N N 61  
ARG   CG  CD   sing N N 62  
ARG   CG  HG2  sing N N 63  
ARG   CG  HG3  sing N N 64  
ARG   CD  NE   sing N N 65  
ARG   CD  HD2  sing N N 66  
ARG   CD  HD3  sing N N 67  
ARG   NE  CZ   sing N N 68  
ARG   NE  HE   sing N N 69  
ARG   CZ  NH1  sing N N 70  
ARG   CZ  NH2  doub N N 71  
ARG   NH1 HH11 sing N N 72  
ARG   NH1 HH12 sing N N 73  
ARG   NH2 HH21 sing N N 74  
ARG   NH2 HH22 sing N N 75  
ARG   OXT HXT  sing N N 76  
ASN   N   CA   sing N N 77  
ASN   N   H    sing N N 78  
ASN   N   H2   sing N N 79  
ASN   CA  C    sing N N 80  
ASN   CA  CB   sing N N 81  
ASN   CA  HA   sing N N 82  
ASN   C   O    doub N N 83  
ASN   C   OXT  sing N N 84  
ASN   CB  CG   sing N N 85  
ASN   CB  HB2  sing N N 86  
ASN   CB  HB3  sing N N 87  
ASN   CG  OD1  doub N N 88  
ASN   CG  ND2  sing N N 89  
ASN   ND2 HD21 sing N N 90  
ASN   ND2 HD22 sing N N 91  
ASN   OXT HXT  sing N N 92  
ASP   N   CA   sing N N 93  
ASP   N   H    sing N N 94  
ASP   N   H2   sing N N 95  
ASP   CA  C    sing N N 96  
ASP   CA  CB   sing N N 97  
ASP   CA  HA   sing N N 98  
ASP   C   O    doub N N 99  
ASP   C   OXT  sing N N 100 
ASP   CB  CG   sing N N 101 
ASP   CB  HB2  sing N N 102 
ASP   CB  HB3  sing N N 103 
ASP   CG  OD1  doub N N 104 
ASP   CG  OD2  sing N N 105 
ASP   OD2 HD2  sing N N 106 
ASP   OXT HXT  sing N N 107 
CYS   N   CA   sing N N 108 
CYS   N   H    sing N N 109 
CYS   N   H2   sing N N 110 
CYS   CA  C    sing N N 111 
CYS   CA  CB   sing N N 112 
CYS   CA  HA   sing N N 113 
CYS   C   O    doub N N 114 
CYS   C   OXT  sing N N 115 
CYS   CB  SG   sing N N 116 
CYS   CB  HB2  sing N N 117 
CYS   CB  HB3  sing N N 118 
CYS   SG  HG   sing N N 119 
CYS   OXT HXT  sing N N 120 
DMS   S   O    doub N N 121 
DMS   S   C1   sing N N 122 
DMS   S   C2   sing N N 123 
DMS   C1  H11  sing N N 124 
DMS   C1  H12  sing N N 125 
DMS   C1  H13  sing N N 126 
DMS   C2  H21  sing N N 127 
DMS   C2  H22  sing N N 128 
DMS   C2  H23  sing N N 129 
GLN   N   CA   sing N N 130 
GLN   N   H    sing N N 131 
GLN   N   H2   sing N N 132 
GLN   CA  C    sing N N 133 
GLN   CA  CB   sing N N 134 
GLN   CA  HA   sing N N 135 
GLN   C   O    doub N N 136 
GLN   C   OXT  sing N N 137 
GLN   CB  CG   sing N N 138 
GLN   CB  HB2  sing N N 139 
GLN   CB  HB3  sing N N 140 
GLN   CG  CD   sing N N 141 
GLN   CG  HG2  sing N N 142 
GLN   CG  HG3  sing N N 143 
GLN   CD  OE1  doub N N 144 
GLN   CD  NE2  sing N N 145 
GLN   NE2 HE21 sing N N 146 
GLN   NE2 HE22 sing N N 147 
GLN   OXT HXT  sing N N 148 
GLU   N   CA   sing N N 149 
GLU   N   H    sing N N 150 
GLU   N   H2   sing N N 151 
GLU   CA  C    sing N N 152 
GLU   CA  CB   sing N N 153 
GLU   CA  HA   sing N N 154 
GLU   C   O    doub N N 155 
GLU   C   OXT  sing N N 156 
GLU   CB  CG   sing N N 157 
GLU   CB  HB2  sing N N 158 
GLU   CB  HB3  sing N N 159 
GLU   CG  CD   sing N N 160 
GLU   CG  HG2  sing N N 161 
GLU   CG  HG3  sing N N 162 
GLU   CD  OE1  doub N N 163 
GLU   CD  OE2  sing N N 164 
GLU   OE2 HE2  sing N N 165 
GLU   OXT HXT  sing N N 166 
GLY   N   CA   sing N N 167 
GLY   N   H    sing N N 168 
GLY   N   H2   sing N N 169 
GLY   CA  C    sing N N 170 
GLY   CA  HA2  sing N N 171 
GLY   CA  HA3  sing N N 172 
GLY   C   O    doub N N 173 
GLY   C   OXT  sing N N 174 
GLY   OXT HXT  sing N N 175 
HIS   N   CA   sing N N 176 
HIS   N   H    sing N N 177 
HIS   N   H2   sing N N 178 
HIS   CA  C    sing N N 179 
HIS   CA  CB   sing N N 180 
HIS   CA  HA   sing N N 181 
HIS   C   O    doub N N 182 
HIS   C   OXT  sing N N 183 
HIS   CB  CG   sing N N 184 
HIS   CB  HB2  sing N N 185 
HIS   CB  HB3  sing N N 186 
HIS   CG  ND1  sing Y N 187 
HIS   CG  CD2  doub Y N 188 
HIS   ND1 CE1  doub Y N 189 
HIS   ND1 HD1  sing N N 190 
HIS   CD2 NE2  sing Y N 191 
HIS   CD2 HD2  sing N N 192 
HIS   CE1 NE2  sing Y N 193 
HIS   CE1 HE1  sing N N 194 
HIS   NE2 HE2  sing N N 195 
HIS   OXT HXT  sing N N 196 
HOH   O   H1   sing N N 197 
HOH   O   H2   sing N N 198 
ILE   N   CA   sing N N 199 
ILE   N   H    sing N N 200 
ILE   N   H2   sing N N 201 
ILE   CA  C    sing N N 202 
ILE   CA  CB   sing N N 203 
ILE   CA  HA   sing N N 204 
ILE   C   O    doub N N 205 
ILE   C   OXT  sing N N 206 
ILE   CB  CG1  sing N N 207 
ILE   CB  CG2  sing N N 208 
ILE   CB  HB   sing N N 209 
ILE   CG1 CD1  sing N N 210 
ILE   CG1 HG12 sing N N 211 
ILE   CG1 HG13 sing N N 212 
ILE   CG2 HG21 sing N N 213 
ILE   CG2 HG22 sing N N 214 
ILE   CG2 HG23 sing N N 215 
ILE   CD1 HD11 sing N N 216 
ILE   CD1 HD12 sing N N 217 
ILE   CD1 HD13 sing N N 218 
ILE   OXT HXT  sing N N 219 
LEU   N   CA   sing N N 220 
LEU   N   H    sing N N 221 
LEU   N   H2   sing N N 222 
LEU   CA  C    sing N N 223 
LEU   CA  CB   sing N N 224 
LEU   CA  HA   sing N N 225 
LEU   C   O    doub N N 226 
LEU   C   OXT  sing N N 227 
LEU   CB  CG   sing N N 228 
LEU   CB  HB2  sing N N 229 
LEU   CB  HB3  sing N N 230 
LEU   CG  CD1  sing N N 231 
LEU   CG  CD2  sing N N 232 
LEU   CG  HG   sing N N 233 
LEU   CD1 HD11 sing N N 234 
LEU   CD1 HD12 sing N N 235 
LEU   CD1 HD13 sing N N 236 
LEU   CD2 HD21 sing N N 237 
LEU   CD2 HD22 sing N N 238 
LEU   CD2 HD23 sing N N 239 
LEU   OXT HXT  sing N N 240 
LYS   N   CA   sing N N 241 
LYS   N   H    sing N N 242 
LYS   N   H2   sing N N 243 
LYS   CA  C    sing N N 244 
LYS   CA  CB   sing N N 245 
LYS   CA  HA   sing N N 246 
LYS   C   O    doub N N 247 
LYS   C   OXT  sing N N 248 
LYS   CB  CG   sing N N 249 
LYS   CB  HB2  sing N N 250 
LYS   CB  HB3  sing N N 251 
LYS   CG  CD   sing N N 252 
LYS   CG  HG2  sing N N 253 
LYS   CG  HG3  sing N N 254 
LYS   CD  CE   sing N N 255 
LYS   CD  HD2  sing N N 256 
LYS   CD  HD3  sing N N 257 
LYS   CE  NZ   sing N N 258 
LYS   CE  HE2  sing N N 259 
LYS   CE  HE3  sing N N 260 
LYS   NZ  HZ1  sing N N 261 
LYS   NZ  HZ2  sing N N 262 
LYS   NZ  HZ3  sing N N 263 
LYS   OXT HXT  sing N N 264 
MET   N   CA   sing N N 265 
MET   N   H    sing N N 266 
MET   N   H2   sing N N 267 
MET   CA  C    sing N N 268 
MET   CA  CB   sing N N 269 
MET   CA  HA   sing N N 270 
MET   C   O    doub N N 271 
MET   C   OXT  sing N N 272 
MET   CB  CG   sing N N 273 
MET   CB  HB2  sing N N 274 
MET   CB  HB3  sing N N 275 
MET   CG  SD   sing N N 276 
MET   CG  HG2  sing N N 277 
MET   CG  HG3  sing N N 278 
MET   SD  CE   sing N N 279 
MET   CE  HE1  sing N N 280 
MET   CE  HE2  sing N N 281 
MET   CE  HE3  sing N N 282 
MET   OXT HXT  sing N N 283 
PHE   N   CA   sing N N 284 
PHE   N   H    sing N N 285 
PHE   N   H2   sing N N 286 
PHE   CA  C    sing N N 287 
PHE   CA  CB   sing N N 288 
PHE   CA  HA   sing N N 289 
PHE   C   O    doub N N 290 
PHE   C   OXT  sing N N 291 
PHE   CB  CG   sing N N 292 
PHE   CB  HB2  sing N N 293 
PHE   CB  HB3  sing N N 294 
PHE   CG  CD1  doub Y N 295 
PHE   CG  CD2  sing Y N 296 
PHE   CD1 CE1  sing Y N 297 
PHE   CD1 HD1  sing N N 298 
PHE   CD2 CE2  doub Y N 299 
PHE   CD2 HD2  sing N N 300 
PHE   CE1 CZ   doub Y N 301 
PHE   CE1 HE1  sing N N 302 
PHE   CE2 CZ   sing Y N 303 
PHE   CE2 HE2  sing N N 304 
PHE   CZ  HZ   sing N N 305 
PHE   OXT HXT  sing N N 306 
PRO   N   CA   sing N N 307 
PRO   N   CD   sing N N 308 
PRO   N   H    sing N N 309 
PRO   CA  C    sing N N 310 
PRO   CA  CB   sing N N 311 
PRO   CA  HA   sing N N 312 
PRO   C   O    doub N N 313 
PRO   C   OXT  sing N N 314 
PRO   CB  CG   sing N N 315 
PRO   CB  HB2  sing N N 316 
PRO   CB  HB3  sing N N 317 
PRO   CG  CD   sing N N 318 
PRO   CG  HG2  sing N N 319 
PRO   CG  HG3  sing N N 320 
PRO   CD  HD2  sing N N 321 
PRO   CD  HD3  sing N N 322 
PRO   OXT HXT  sing N N 323 
SER   N   CA   sing N N 324 
SER   N   H    sing N N 325 
SER   N   H2   sing N N 326 
SER   CA  C    sing N N 327 
SER   CA  CB   sing N N 328 
SER   CA  HA   sing N N 329 
SER   C   O    doub N N 330 
SER   C   OXT  sing N N 331 
SER   CB  OG   sing N N 332 
SER   CB  HB2  sing N N 333 
SER   CB  HB3  sing N N 334 
SER   OG  HG   sing N N 335 
SER   OXT HXT  sing N N 336 
SO4   S   O1   doub N N 337 
SO4   S   O2   doub N N 338 
SO4   S   O3   sing N N 339 
SO4   S   O4   sing N N 340 
THR   N   CA   sing N N 341 
THR   N   H    sing N N 342 
THR   N   H2   sing N N 343 
THR   CA  C    sing N N 344 
THR   CA  CB   sing N N 345 
THR   CA  HA   sing N N 346 
THR   C   O    doub N N 347 
THR   C   OXT  sing N N 348 
THR   CB  OG1  sing N N 349 
THR   CB  CG2  sing N N 350 
THR   CB  HB   sing N N 351 
THR   OG1 HG1  sing N N 352 
THR   CG2 HG21 sing N N 353 
THR   CG2 HG22 sing N N 354 
THR   CG2 HG23 sing N N 355 
THR   OXT HXT  sing N N 356 
TRP   N   CA   sing N N 357 
TRP   N   H    sing N N 358 
TRP   N   H2   sing N N 359 
TRP   CA  C    sing N N 360 
TRP   CA  CB   sing N N 361 
TRP   CA  HA   sing N N 362 
TRP   C   O    doub N N 363 
TRP   C   OXT  sing N N 364 
TRP   CB  CG   sing N N 365 
TRP   CB  HB2  sing N N 366 
TRP   CB  HB3  sing N N 367 
TRP   CG  CD1  doub Y N 368 
TRP   CG  CD2  sing Y N 369 
TRP   CD1 NE1  sing Y N 370 
TRP   CD1 HD1  sing N N 371 
TRP   CD2 CE2  doub Y N 372 
TRP   CD2 CE3  sing Y N 373 
TRP   NE1 CE2  sing Y N 374 
TRP   NE1 HE1  sing N N 375 
TRP   CE2 CZ2  sing Y N 376 
TRP   CE3 CZ3  doub Y N 377 
TRP   CE3 HE3  sing N N 378 
TRP   CZ2 CH2  doub Y N 379 
TRP   CZ2 HZ2  sing N N 380 
TRP   CZ3 CH2  sing Y N 381 
TRP   CZ3 HZ3  sing N N 382 
TRP   CH2 HH2  sing N N 383 
TRP   OXT HXT  sing N N 384 
TYR   N   CA   sing N N 385 
TYR   N   H    sing N N 386 
TYR   N   H2   sing N N 387 
TYR   CA  C    sing N N 388 
TYR   CA  CB   sing N N 389 
TYR   CA  HA   sing N N 390 
TYR   C   O    doub N N 391 
TYR   C   OXT  sing N N 392 
TYR   CB  CG   sing N N 393 
TYR   CB  HB2  sing N N 394 
TYR   CB  HB3  sing N N 395 
TYR   CG  CD1  doub Y N 396 
TYR   CG  CD2  sing Y N 397 
TYR   CD1 CE1  sing Y N 398 
TYR   CD1 HD1  sing N N 399 
TYR   CD2 CE2  doub Y N 400 
TYR   CD2 HD2  sing N N 401 
TYR   CE1 CZ   doub Y N 402 
TYR   CE1 HE1  sing N N 403 
TYR   CE2 CZ   sing Y N 404 
TYR   CE2 HE2  sing N N 405 
TYR   CZ  OH   sing N N 406 
TYR   OH  HH   sing N N 407 
TYR   OXT HXT  sing N N 408 
VAL   N   CA   sing N N 409 
VAL   N   H    sing N N 410 
VAL   N   H2   sing N N 411 
VAL   CA  C    sing N N 412 
VAL   CA  CB   sing N N 413 
VAL   CA  HA   sing N N 414 
VAL   C   O    doub N N 415 
VAL   C   OXT  sing N N 416 
VAL   CB  CG1  sing N N 417 
VAL   CB  CG2  sing N N 418 
VAL   CB  HB   sing N N 419 
VAL   CG1 HG11 sing N N 420 
VAL   CG1 HG12 sing N N 421 
VAL   CG1 HG13 sing N N 422 
VAL   CG2 HG21 sing N N 423 
VAL   CG2 HG22 sing N N 424 
VAL   CG2 HG23 sing N N 425 
VAL   OXT HXT  sing N N 426 
# 
_pdbx_audit_support.funding_organization   '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                    7I1S 
_atom_sites.fract_transf_matrix[1][1]   0.023548 
_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]   0.023548 
_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]   0.004639 
_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   ? -20.507 18.821  -7.100  1.00 64.46  ? 50  ASP   A N   1 
ATOM   2    C CA  . ASP   A 1 7   ? -21.878 18.262  -7.291  1.00 61.10  ? 50  ASP   A CA  1 
ATOM   3    C C   . ASP   A 1 7   ? -21.989 17.700  -8.724  1.00 58.24  ? 50  ASP   A C   1 
ATOM   4    O O   . ASP   A 1 7   ? -21.451 18.339  -9.676  1.00 59.73  ? 50  ASP   A O   1 
ATOM   5    C CB  . ASP   A 1 7   ? -22.930 19.316  -6.914  1.00 65.75  ? 50  ASP   A CB  1 
ATOM   6    C CG  . ASP   A 1 7   ? -24.323 18.748  -6.691  1.00 65.53  ? 50  ASP   A CG  1 
ATOM   7    O OD1 . ASP   A 1 7   ? -24.743 18.605  -5.510  1.00 66.63  ? 50  ASP   A OD1 1 
ATOM   8    O OD2 . ASP   A 1 7   ? -24.980 18.460  -7.701  1.00 69.12  ? 50  ASP   A OD2 1 
ATOM   9    N N   . MET   A 1 8   ? -22.660 16.550  -8.865  1.00 45.51  ? 51  MET   A N   1 
ATOM   10   C CA  . MET   A 1 8   ? -22.495 15.596  -9.993  1.00 46.42  ? 51  MET   A CA  1 
ATOM   11   C C   . MET   A 1 8   ? -23.858 15.174  -10.501 1.00 40.56  ? 51  MET   A C   1 
ATOM   12   O O   . MET   A 1 8   ? -24.714 14.919  -9.646  1.00 39.63  ? 51  MET   A O   1 
ATOM   13   C CB  . MET   A 1 8   ? -21.815 14.303  -9.541  1.00 49.88  ? 51  MET   A CB  1 
ATOM   14   C CG  . MET   A 1 8   ? -20.327 14.302  -9.631  1.00 50.70  ? 51  MET   A CG  1 
ATOM   15   S SD  . MET   A 1 8   ? -19.751 12.606  -9.354  1.00 57.74  ? 51  MET   A SD  1 
ATOM   16   C CE  . MET   A 1 8   ? -18.013 12.945  -9.060  1.00 56.95  ? 51  MET   A CE  1 
ATOM   17   N N   . TYR   A 1 9   ? -23.994 15.005  -11.817 1.00 35.63  ? 52  TYR   A N   1 
ATOM   18   C CA  . TYR   A 1 9   ? -25.287 14.738  -12.497 1.00 35.78  ? 52  TYR   A CA  1 
ATOM   19   C C   . TYR   A 1 9   ? -25.051 13.812  -13.690 1.00 37.48  ? 52  TYR   A C   1 
ATOM   20   O O   . TYR   A 1 9   ? -23.930 13.793  -14.196 1.00 38.95  ? 52  TYR   A O   1 
ATOM   21   C CB  . TYR   A 1 9   ? -25.948 16.051  -12.924 1.00 33.65  ? 52  TYR   A CB  1 
ATOM   22   C CG  . TYR   A 1 9   ? -25.207 16.826  -13.984 1.00 32.01  ? 52  TYR   A CG  1 
ATOM   23   C CD1 . TYR   A 1 9   ? -24.213 17.723  -13.623 1.00 32.05  ? 52  TYR   A CD1 1 
ATOM   24   C CD2 . TYR   A 1 9   ? -25.492 16.672  -15.338 1.00 32.19  ? 52  TYR   A CD2 1 
ATOM   25   C CE1 . TYR   A 1 9   ? -23.502 18.435  -14.576 1.00 30.76  ? 52  TYR   A CE1 1 
ATOM   26   C CE2 . TYR   A 1 9   ? -24.803 17.389  -16.309 1.00 32.85  ? 52  TYR   A CE2 1 
ATOM   27   C CZ  . TYR   A 1 9   ? -23.804 18.275  -15.918 1.00 32.92  ? 52  TYR   A CZ  1 
ATOM   28   O OH  . TYR   A 1 9   ? -23.090 19.006  -16.819 1.00 33.89  ? 52  TYR   A OH  1 
ATOM   29   N N   . ILE   A 1 10  ? -26.088 13.082  -14.106 1.00 41.16  ? 53  ILE   A N   1 
ATOM   30   C CA  . ILE   A 1 10  ? -26.028 12.099  -15.223 1.00 41.37  ? 53  ILE   A CA  1 
ATOM   31   C C   . ILE   A 1 10  ? -26.764 12.659  -16.455 1.00 44.39  ? 53  ILE   A C   1 
ATOM   32   O O   . ILE   A 1 10  ? -27.704 13.472  -16.274 1.00 47.26  ? 53  ILE   A O   1 
ATOM   33   C CB  . ILE   A 1 10  ? -26.569 10.725  -14.758 1.00 41.86  ? 53  ILE   A CB  1 
ATOM   34   C CG1 . ILE   A 1 10  ? -28.064 10.745  -14.442 1.00 43.77  ? 53  ILE   A CG1 1 
ATOM   35   C CG2 . ILE   A 1 10  ? -25.758 10.196  -13.583 1.00 43.57  ? 53  ILE   A CG2 1 
ATOM   36   C CD1 . ILE   A 1 10  ? -28.659 9.383   -14.171 1.00 45.82  ? 53  ILE   A CD1 1 
ATOM   37   N N   . GLU   A 1 11  ? -26.346 12.243  -17.659 1.00 45.20  ? 54  GLU   A N   1 
ATOM   38   C CA  . GLU   A 1 11  ? -27.073 12.458  -18.946 1.00 45.37  ? 54  GLU   A CA  1 
ATOM   39   C C   . GLU   A 1 11  ? -27.089 11.170  -19.775 1.00 43.08  ? 54  GLU   A C   1 
ATOM   40   O O   . GLU   A 1 11  ? -26.009 10.598  -19.993 1.00 38.12  ? 54  GLU   A O   1 
ATOM   41   C CB  . GLU   A 1 11  ? -26.402 13.515  -19.823 1.00 47.80  ? 54  GLU   A CB  1 
ATOM   42   C CG  . GLU   A 1 11  ? -25.950 14.754  -19.090 1.00 52.75  ? 54  GLU   A CG  1 
ATOM   43   C CD  . GLU   A 1 11  ? -25.272 15.774  -19.985 1.00 56.02  ? 54  GLU   A CD  1 
ATOM   44   O OE1 . GLU   A 1 11  ? -24.581 15.364  -20.949 1.00 58.53  ? 54  GLU   A OE1 1 
ATOM   45   O OE2 . GLU   A 1 11  ? -25.442 16.975  -19.721 1.00 61.28  ? 54  GLU   A OE2 1 
ATOM   46   N N   . ARG   A 1 12  ? -28.257 10.755  -20.270 1.00 42.33  ? 55  ARG   A N   1 
ATOM   47   C CA  . ARG   A 1 12  ? -28.390 9.538   -21.116 1.00 43.64  ? 55  ARG   A CA  1 
ATOM   48   C C   . ARG   A 1 12  ? -27.472 9.669   -22.340 1.00 45.35  ? 55  ARG   A C   1 
ATOM   49   O O   . ARG   A 1 12  ? -27.369 10.807  -22.849 1.00 47.07  ? 55  ARG   A O   1 
ATOM   50   C CB  . ARG   A 1 12  ? -29.847 9.324   -21.512 1.00 43.62  ? 55  ARG   A CB  1 
ATOM   51   C CG  . ARG   A 1 12  ? -30.123 7.940   -22.077 1.00 43.63  ? 55  ARG   A CG  1 
ATOM   52   C CD  . ARG   A 1 12  ? -31.472 7.420   -21.618 1.00 50.19  ? 55  ARG   A CD  1 
ATOM   53   N NE  . ARG   A 1 12  ? -31.748 6.069   -22.067 1.00 53.00  ? 55  ARG   A NE  1 
ATOM   54   C CZ  . ARG   A 1 12  ? -31.812 5.707   -23.344 1.00 56.87  ? 55  ARG   A CZ  1 
ATOM   55   N NH1 . ARG   A 1 12  ? -31.624 6.595   -24.309 1.00 67.97  ? 55  ARG   A NH1 1 
ATOM   56   N NH2 . ARG   A 1 12  ? -32.084 4.456   -23.660 1.00 58.06  ? 55  ARG   A NH2 1 
ATOM   57   N N   . ALA   A 1 13  ? -26.760 8.586   -22.724 1.00 44.95  ? 56  ALA   A N   1 
ATOM   58   C CA  . ALA   A 1 13  ? -25.763 8.573   -23.834 1.00 39.48  ? 56  ALA   A CA  1 
ATOM   59   C C   . ALA   A 1 13  ? -26.046 7.465   -24.842 1.00 35.17  ? 56  ALA   A C   1 
ATOM   60   O O   . ALA   A 1 13  ? -25.354 7.457   -25.866 1.00 35.57  ? 56  ALA   A O   1 
ATOM   61   C CB  . ALA   A 1 13  ? -24.346 8.458   -23.324 1.00 42.24  ? 56  ALA   A CB  1 
ATOM   62   N N   . GLY   A 1 14  ? -27.016 6.581   -24.597 1.00 32.70  ? 57  GLY   A N   1 
ATOM   63   C CA  . GLY   A 1 14  ? -27.447 5.614   -25.618 1.00 32.63  ? 57  GLY   A CA  1 
ATOM   64   C C   . GLY   A 1 14  ? -28.269 4.490   -25.038 1.00 36.67  ? 57  GLY   A C   1 
ATOM   65   O O   . GLY   A 1 14  ? -28.426 4.465   -23.799 1.00 38.87  ? 57  GLY   A O   1 
ATOM   66   N N   . ASP   A 1 15  ? -28.770 3.611   -25.915 1.00 38.78  ? 58  ASP   A N   1 
ATOM   67   C CA  . ASP   A 1 15  ? -29.236 2.240   -25.582 1.00 46.73  ? 58  ASP   A CA  1 
ATOM   68   C C   . ASP   A 1 15  ? -28.013 1.351   -25.356 1.00 50.02  ? 58  ASP   A C   1 
ATOM   69   O O   . ASP   A 1 15  ? -26.930 1.611   -25.952 1.00 49.04  ? 58  ASP   A O   1 
ATOM   70   C CB  . ASP   A 1 15  ? -30.059 1.585   -26.695 1.00 48.37  ? 58  ASP   A CB  1 
ATOM   71   C CG  . ASP   A 1 15  ? -31.516 1.984   -26.686 1.00 53.40  ? 58  ASP   A CG  1 
ATOM   72   O OD1 . ASP   A 1 15  ? -31.922 2.620   -25.720 1.00 54.03  ? 58  ASP   A OD1 1 
ATOM   73   O OD2 . ASP   A 1 15  ? -32.226 1.661   -27.654 1.00 62.09  ? 58  ASP   A OD2 1 
ATOM   74   N N   . ILE   A 1 16  ? -28.183 0.318   -24.543 1.00 53.86  ? 59  ILE   A N   1 
ATOM   75   C CA  . ILE   A 1 16  ? -27.158 -0.750  -24.433 1.00 54.04  ? 59  ILE   A CA  1 
ATOM   76   C C   . ILE   A 1 16  ? -27.700 -1.911  -25.274 1.00 53.33  ? 59  ILE   A C   1 
ATOM   77   O O   . ILE   A 1 16  ? -28.668 -2.570  -24.873 1.00 47.63  ? 59  ILE   A O   1 
ATOM   78   C CB  . ILE   A 1 16  ? -26.799 -1.038  -22.967 1.00 51.41  ? 59  ILE   A CB  1 
ATOM   79   C CG1 . ILE   A 1 16  ? -26.465 0.264   -22.236 1.00 44.59  ? 59  ILE   A CG1 1 
ATOM   80   C CG2 . ILE   A 1 16  ? -25.641 -2.025  -22.906 1.00 52.64  ? 59  ILE   A CG2 1 
ATOM   81   C CD1 . ILE   A 1 16  ? -26.424 0.155   -20.726 1.00 48.04  ? 59  ILE   A CD1 1 
ATOM   82   N N   A THR   A 1 17  ? -27.072 -2.109  -26.439 0.25 54.07  ? 60  THR   A N   1 
ATOM   83   N N   B THR   A 1 17  ? -27.084 -2.122  -26.440 0.25 54.28  ? 60  THR   A N   1 
ATOM   84   N N   C THR   A 1 17  ? -27.072 -2.109  -26.439 0.25 54.07  ? 60  THR   A N   1 
ATOM   85   N N   D THR   A 1 17  ? -27.084 -2.122  -26.440 0.25 54.28  ? 60  THR   A N   1 
ATOM   86   C CA  A THR   A 1 17  ? -27.467 -3.050  -27.521 0.25 53.96  ? 60  THR   A CA  1 
ATOM   87   C CA  B THR   A 1 17  ? -27.492 -3.109  -27.474 0.25 54.32  ? 60  THR   A CA  1 
ATOM   88   C CA  C THR   A 1 17  ? -27.467 -3.050  -27.521 0.25 53.96  ? 60  THR   A CA  1 
ATOM   89   C CA  D THR   A 1 17  ? -27.492 -3.109  -27.474 0.25 54.32  ? 60  THR   A CA  1 
ATOM   90   C C   A THR   A 1 17  ? -26.195 -3.585  -28.188 0.25 53.56  ? 60  THR   A C   1 
ATOM   91   C C   B THR   A 1 17  ? -26.235 -3.580  -28.213 0.25 53.90  ? 60  THR   A C   1 
ATOM   92   C C   C THR   A 1 17  ? -26.195 -3.585  -28.188 0.25 53.56  ? 60  THR   A C   1 
ATOM   93   C C   D THR   A 1 17  ? -26.235 -3.580  -28.213 0.25 53.90  ? 60  THR   A C   1 
ATOM   94   O O   A THR   A 1 17  ? -25.232 -2.796  -28.332 0.25 51.95  ? 60  THR   A O   1 
ATOM   95   O O   B THR   A 1 17  ? -25.321 -2.747  -28.416 0.25 52.79  ? 60  THR   A O   1 
ATOM   96   O O   C THR   A 1 17  ? -25.232 -2.796  -28.332 0.25 51.95  ? 60  THR   A O   1 
ATOM   97   O O   D THR   A 1 17  ? -25.321 -2.747  -28.416 0.25 52.79  ? 60  THR   A O   1 
ATOM   98   C CB  A THR   A 1 17  ? -28.355 -2.354  -28.564 0.25 53.32  ? 60  THR   A CB  1 
ATOM   99   C CB  B THR   A 1 17  ? -28.547 -2.506  -28.414 0.25 54.02  ? 60  THR   A CB  1 
ATOM   100  C CB  C THR   A 1 17  ? -28.355 -2.354  -28.564 0.25 53.32  ? 60  THR   A CB  1 
ATOM   101  C CB  D THR   A 1 17  ? -28.547 -2.506  -28.414 0.25 54.02  ? 60  THR   A CB  1 
ATOM   102  O OG1 A THR   A 1 17  ? -27.743 -1.112  -28.910 0.25 51.48  ? 60  THR   A OG1 1 
ATOM   103  O OG1 B THR   A 1 17  ? -29.842 -2.828  -27.903 0.25 54.00  ? 60  THR   A OG1 1 
ATOM   104  O OG1 C THR   A 1 17  ? -27.743 -1.112  -28.910 0.25 51.48  ? 60  THR   A OG1 1 
ATOM   105  O OG1 D THR   A 1 17  ? -29.842 -2.828  -27.903 0.25 54.00  ? 60  THR   A OG1 1 
ATOM   106  C CG2 A THR   A 1 17  ? -29.764 -2.090  -28.080 0.25 53.74  ? 60  THR   A CG2 1 
ATOM   107  C CG2 B THR   A 1 17  ? -28.438 -3.007  -29.837 0.25 52.95  ? 60  THR   A CG2 1 
ATOM   108  C CG2 C THR   A 1 17  ? -29.764 -2.090  -28.080 0.25 53.74  ? 60  THR   A CG2 1 
ATOM   109  C CG2 D THR   A 1 17  ? -28.438 -3.007  -29.837 0.25 52.95  ? 60  THR   A CG2 1 
ATOM   110  N N   . TRP   A 1 18  ? -26.182 -4.867  -28.568 1.00 52.60  ? 61  TRP   A N   1 
ATOM   111  C CA  . TRP   A 1 18  ? -25.077 -5.437  -29.385 1.00 59.92  ? 61  TRP   A CA  1 
ATOM   112  C C   . TRP   A 1 18  ? -25.215 -4.860  -30.807 1.00 63.33  ? 61  TRP   A C   1 
ATOM   113  O O   . TRP   A 1 18  ? -26.333 -4.909  -31.339 1.00 59.54  ? 61  TRP   A O   1 
ATOM   114  C CB  . TRP   A 1 18  ? -25.086 -6.973  -29.360 1.00 64.81  ? 61  TRP   A CB  1 
ATOM   115  C CG  . TRP   A 1 18  ? -23.991 -7.590  -30.178 1.00 72.56  ? 61  TRP   A CG  1 
ATOM   116  C CD1 . TRP   A 1 18  ? -23.998 -7.748  -31.533 1.00 76.42  ? 61  TRP   A CD1 1 
ATOM   117  C CD2 . TRP   A 1 18  ? -22.721 -8.106  -29.720 1.00 76.24  ? 61  TRP   A CD2 1 
ATOM   118  N NE1 . TRP   A 1 18  ? -22.828 -8.320  -31.949 1.00 82.55  ? 61  TRP   A NE1 1 
ATOM   119  C CE2 . TRP   A 1 18  ? -22.026 -8.562  -30.864 1.00 83.46  ? 61  TRP   A CE2 1 
ATOM   120  C CE3 . TRP   A 1 18  ? -22.099 -8.243  -28.471 1.00 76.33  ? 61  TRP   A CE3 1 
ATOM   121  C CZ2 . TRP   A 1 18  ? -20.754 -9.143  -30.789 1.00 76.77  ? 61  TRP   A CZ2 1 
ATOM   122  C CZ3 . TRP   A 1 18  ? -20.842 -8.812  -28.395 1.00 75.15  ? 61  TRP   A CZ3 1 
ATOM   123  C CH2 . TRP   A 1 18  ? -20.179 -9.255  -29.541 1.00 74.86  ? 61  TRP   A CH2 1 
ATOM   124  N N   . GLU   A 1 19  ? -24.150 -4.272  -31.371 1.00 67.14  ? 62  GLU   A N   1 
ATOM   125  C CA  . GLU   A 1 19  ? -24.167 -3.634  -32.721 1.00 73.01  ? 62  GLU   A CA  1 
ATOM   126  C C   . GLU   A 1 19  ? -23.263 -4.408  -33.697 1.00 68.78  ? 62  GLU   A C   1 
ATOM   127  O O   . GLU   A 1 19  ? -22.044 -4.141  -33.725 1.00 65.38  ? 62  GLU   A O   1 
ATOM   128  C CB  . GLU   A 1 19  ? -23.728 -2.170  -32.624 1.00 82.42  ? 62  GLU   A CB  1 
ATOM   129  C CG  . GLU   A 1 19  ? -24.279 -1.427  -31.406 1.00 98.61  ? 62  GLU   A CG  1 
ATOM   130  C CD  . GLU   A 1 19  ? -25.708 -0.892  -31.446 1.00 100.64 ? 62  GLU   A CD  1 
ATOM   131  O OE1 . GLU   A 1 19  ? -26.391 -1.072  -32.474 1.00 100.99 ? 62  GLU   A OE1 1 
ATOM   132  O OE2 . GLU   A 1 19  ? -26.130 -0.275  -30.437 1.00 99.51  ? 62  GLU   A OE2 1 
ATOM   133  N N   A LYS   A 1 20  ? -23.858 -5.318  -34.483 0.25 69.47  ? 63  LYS   A N   1 
ATOM   134  N N   B LYS   A 1 20  ? -23.858 -5.318  -34.483 0.25 69.47  ? 63  LYS   A N   1 
ATOM   135  N N   C LYS   A 1 20  ? -23.849 -5.342  -34.461 0.25 68.48  ? 63  LYS   A N   1 
ATOM   136  N N   D LYS   A 1 20  ? -23.849 -5.342  -34.461 0.25 68.48  ? 63  LYS   A N   1 
ATOM   137  C CA  A LYS   A 1 20  ? -23.175 -6.156  -35.512 0.25 69.39  ? 63  LYS   A CA  1 
ATOM   138  C CA  B LYS   A 1 20  ? -23.175 -6.156  -35.512 0.25 69.39  ? 63  LYS   A CA  1 
ATOM   139  C CA  C LYS   A 1 20  ? -23.147 -6.182  -35.473 0.25 67.81  ? 63  LYS   A CA  1 
ATOM   140  C CA  D LYS   A 1 20  ? -23.147 -6.182  -35.473 0.25 67.81  ? 63  LYS   A CA  1 
ATOM   141  C C   A LYS   A 1 20  ? -22.321 -5.276  -36.430 0.25 68.07  ? 63  LYS   A C   1 
ATOM   142  C C   B LYS   A 1 20  ? -22.321 -5.276  -36.430 0.25 68.07  ? 63  LYS   A C   1 
ATOM   143  C C   C LYS   A 1 20  ? -22.427 -5.279  -36.479 0.25 65.48  ? 63  LYS   A C   1 
ATOM   144  C C   D LYS   A 1 20  ? -22.427 -5.279  -36.479 0.25 65.48  ? 63  LYS   A C   1 
ATOM   145  O O   A LYS   A 1 20  ? -22.803 -4.199  -36.831 0.25 69.49  ? 63  LYS   A O   1 
ATOM   146  O O   B LYS   A 1 20  ? -22.803 -4.199  -36.831 0.25 69.49  ? 63  LYS   A O   1 
ATOM   147  O O   C LYS   A 1 20  ? -23.056 -4.316  -36.956 0.25 66.27  ? 63  LYS   A O   1 
ATOM   148  O O   D LYS   A 1 20  ? -23.056 -4.316  -36.956 0.25 66.27  ? 63  LYS   A O   1 
ATOM   149  C CB  A LYS   A 1 20  ? -24.193 -6.919  -36.366 0.25 69.65  ? 63  LYS   A CB  1 
ATOM   150  C CB  B LYS   A 1 20  ? -24.193 -6.919  -36.366 0.25 69.65  ? 63  LYS   A CB  1 
ATOM   151  C CB  C LYS   A 1 20  ? -24.125 -7.076  -36.242 0.25 68.18  ? 63  LYS   A CB  1 
ATOM   152  C CB  D LYS   A 1 20  ? -24.125 -7.076  -36.242 0.25 68.18  ? 63  LYS   A CB  1 
ATOM   153  C CG  A LYS   A 1 20  ? -25.036 -7.946  -35.624 0.25 71.50  ? 63  LYS   A CG  1 
ATOM   154  C CG  B LYS   A 1 20  ? -25.036 -7.946  -35.624 0.25 71.50  ? 63  LYS   A CG  1 
ATOM   155  C CG  C LYS   A 1 20  ? -25.259 -7.676  -35.424 0.25 70.42  ? 63  LYS   A CG  1 
ATOM   156  C CG  D LYS   A 1 20  ? -25.259 -7.676  -35.424 0.25 70.42  ? 63  LYS   A CG  1 
ATOM   157  C CD  A LYS   A 1 20  ? -26.243 -8.409  -36.415 0.25 72.99  ? 63  LYS   A CD  1 
ATOM   158  C CD  B LYS   A 1 20  ? -26.243 -8.409  -36.415 0.25 72.99  ? 63  LYS   A CD  1 
ATOM   159  C CD  C LYS   A 1 20  ? -26.388 -8.211  -36.284 0.25 71.71  ? 63  LYS   A CD  1 
ATOM   160  C CD  D LYS   A 1 20  ? -26.388 -8.211  -36.284 0.25 71.71  ? 63  LYS   A CD  1 
ATOM   161  C CE  A LYS   A 1 20  ? -27.292 -9.081  -35.554 0.25 74.60  ? 63  LYS   A CE  1 
ATOM   162  C CE  B LYS   A 1 20  ? -27.292 -9.081  -35.554 0.25 74.60  ? 63  LYS   A CE  1 
ATOM   163  C CE  C LYS   A 1 20  ? -27.570 -8.702  -35.475 0.25 72.84  ? 63  LYS   A CE  1 
ATOM   164  C CE  D LYS   A 1 20  ? -27.570 -8.702  -35.475 0.25 72.84  ? 63  LYS   A CE  1 
ATOM   165  N NZ  A LYS   A 1 20  ? -28.615 -9.106  -36.220 0.25 75.06  ? 63  LYS   A NZ  1 
ATOM   166  N NZ  B LYS   A 1 20  ? -28.615 -9.106  -36.220 0.25 75.06  ? 63  LYS   A NZ  1 
ATOM   167  N NZ  C LYS   A 1 20  ? -28.777 -8.869  -36.318 0.25 73.35  ? 63  LYS   A NZ  1 
ATOM   168  N NZ  D LYS   A 1 20  ? -28.777 -8.869  -36.318 0.25 73.35  ? 63  LYS   A NZ  1 
ATOM   169  N N   A ASP   A 1 21  ? -21.108 -5.734  -36.754 0.25 66.27  ? 64  ASP   A N   1 
ATOM   170  N N   B ASP   A 1 21  ? -21.108 -5.734  -36.754 0.25 66.27  ? 64  ASP   A N   1 
ATOM   171  N N   C ASP   A 1 21  ? -21.163 -5.586  -36.785 0.25 63.06  ? 64  ASP   A N   1 
ATOM   172  N N   D ASP   A 1 21  ? -21.163 -5.586  -36.785 0.25 63.06  ? 64  ASP   A N   1 
ATOM   173  C CA  A ASP   A 1 21  ? -20.152 -5.042  -37.660 0.25 66.98  ? 64  ASP   A CA  1 
ATOM   174  C CA  B ASP   A 1 21  ? -20.152 -5.042  -37.660 0.25 66.98  ? 64  ASP   A CA  1 
ATOM   175  C CA  C ASP   A 1 21  ? -20.346 -4.864  -37.797 0.25 62.96  ? 64  ASP   A CA  1 
ATOM   176  C CA  D ASP   A 1 21  ? -20.346 -4.864  -37.797 0.25 62.96  ? 64  ASP   A CA  1 
ATOM   177  C C   A ASP   A 1 21  ? -19.685 -3.737  -37.004 0.25 65.17  ? 64  ASP   A C   1 
ATOM   178  C C   B ASP   A 1 21  ? -19.685 -3.737  -37.004 0.25 65.17  ? 64  ASP   A C   1 
ATOM   179  C C   C ASP   A 1 21  ? -19.716 -3.625  -37.149 0.25 60.19  ? 64  ASP   A C   1 
ATOM   180  C C   D ASP   A 1 21  ? -19.716 -3.625  -37.149 0.25 60.19  ? 64  ASP   A C   1 
ATOM   181  O O   A ASP   A 1 21  ? -19.761 -2.682  -37.663 0.25 64.17  ? 64  ASP   A O   1 
ATOM   182  O O   B ASP   A 1 21  ? -19.761 -2.682  -37.663 0.25 64.17  ? 64  ASP   A O   1 
ATOM   183  O O   C ASP   A 1 21  ? -19.560 -2.605  -37.847 0.25 59.09  ? 64  ASP   A O   1 
ATOM   184  O O   D ASP   A 1 21  ? -19.560 -2.605  -37.847 0.25 59.09  ? 64  ASP   A O   1 
ATOM   185  C CB  A ASP   A 1 21  ? -20.766 -4.800  -39.043 0.25 68.79  ? 64  ASP   A CB  1 
ATOM   186  C CB  B ASP   A 1 21  ? -20.766 -4.800  -39.043 0.25 68.79  ? 64  ASP   A CB  1 
ATOM   187  C CB  C ASP   A 1 21  ? -21.189 -4.499  -39.022 0.25 64.87  ? 64  ASP   A CB  1 
ATOM   188  C CB  D ASP   A 1 21  ? -21.189 -4.499  -39.022 0.25 64.87  ? 64  ASP   A CB  1 
ATOM   189  C CG  A ASP   A 1 21  ? -20.640 -5.987  -39.986 0.25 70.31  ? 64  ASP   A CG  1 
ATOM   190  C CG  B ASP   A 1 21  ? -20.640 -5.987  -39.986 0.25 70.31  ? 64  ASP   A CG  1 
ATOM   191  C CG  C ASP   A 1 21  ? -21.630 -5.704  -39.837 0.25 66.89  ? 64  ASP   A CG  1 
ATOM   192  C CG  D ASP   A 1 21  ? -21.630 -5.704  -39.837 0.25 66.89  ? 64  ASP   A CG  1 
ATOM   193  O OD1 A ASP   A 1 21  ? -19.507 -6.264  -40.438 0.25 67.71  ? 64  ASP   A OD1 1 
ATOM   194  O OD1 B ASP   A 1 21  ? -19.507 -6.264  -40.438 0.25 67.71  ? 64  ASP   A OD1 1 
ATOM   195  O OD1 C ASP   A 1 21  ? -20.742 -6.439  -40.321 0.25 68.99  ? 64  ASP   A OD1 1 
ATOM   196  O OD1 D ASP   A 1 21  ? -20.742 -6.439  -40.321 0.25 68.99  ? 64  ASP   A OD1 1 
ATOM   197  O OD2 A ASP   A 1 21  ? -21.675 -6.633  -40.256 0.25 72.40  ? 64  ASP   A OD2 1 
ATOM   198  O OD2 B ASP   A 1 21  ? -21.675 -6.633  -40.256 0.25 72.40  ? 64  ASP   A OD2 1 
ATOM   199  O OD2 C ASP   A 1 21  ? -22.856 -5.909  -39.969 0.25 65.86  ? 64  ASP   A OD2 1 
ATOM   200  O OD2 D ASP   A 1 21  ? -22.856 -5.909  -39.969 0.25 65.86  ? 64  ASP   A OD2 1 
ATOM   201  N N   A ALA   A 1 22  ? -19.209 -3.819  -35.757 0.25 63.33  ? 65  ALA   A N   1 
ATOM   202  N N   B ALA   A 1 22  ? -19.209 -3.819  -35.757 0.25 63.33  ? 65  ALA   A N   1 
ATOM   203  N N   C ALA   A 1 22  ? -19.350 -3.726  -35.867 0.25 57.55  ? 65  ALA   A N   1 
ATOM   204  N N   D ALA   A 1 22  ? -19.350 -3.726  -35.867 0.25 57.55  ? 65  ALA   A N   1 
ATOM   205  C CA  A ALA   A 1 22  ? -18.553 -2.715  -35.018 0.25 61.59  ? 65  ALA   A CA  1 
ATOM   206  C CA  B ALA   A 1 22  ? -18.553 -2.715  -35.018 0.25 61.59  ? 65  ALA   A CA  1 
ATOM   207  C CA  C ALA   A 1 22  ? -18.666 -2.664  -35.093 0.25 55.08  ? 65  ALA   A CA  1 
ATOM   208  C CA  D ALA   A 1 22  ? -18.666 -2.664  -35.093 0.25 55.08  ? 65  ALA   A CA  1 
ATOM   209  C C   A ALA   A 1 22  ? -17.040 -2.772  -35.268 0.25 60.17  ? 65  ALA   A C   1 
ATOM   210  C C   B ALA   A 1 22  ? -17.040 -2.772  -35.268 0.25 60.17  ? 65  ALA   A C   1 
ATOM   211  C C   C ALA   A 1 22  ? -17.152 -2.769  -35.301 0.25 52.82  ? 65  ALA   A C   1 
ATOM   212  C C   D ALA   A 1 22  ? -17.152 -2.769  -35.301 0.25 52.82  ? 65  ALA   A C   1 
ATOM   213  O O   A ALA   A 1 22  ? -16.549 -3.843  -35.673 0.25 55.27  ? 65  ALA   A O   1 
ATOM   214  O O   B ALA   A 1 22  ? -16.549 -3.843  -35.673 0.25 55.27  ? 65  ALA   A O   1 
ATOM   215  O O   C ALA   A 1 22  ? -16.666 -3.883  -35.578 0.25 48.44  ? 65  ALA   A O   1 
ATOM   216  O O   D ALA   A 1 22  ? -16.666 -3.883  -35.578 0.25 48.44  ? 65  ALA   A O   1 
ATOM   217  C CB  A ALA   A 1 22  ? -18.880 -2.812  -33.548 0.25 62.79  ? 65  ALA   A CB  1 
ATOM   218  C CB  B ALA   A 1 22  ? -18.880 -2.812  -33.548 0.25 62.79  ? 65  ALA   A CB  1 
ATOM   219  C CB  C ALA   A 1 22  ? -19.028 -2.780  -33.633 0.25 56.25  ? 65  ALA   A CB  1 
ATOM   220  C CB  D ALA   A 1 22  ? -19.028 -2.780  -33.633 0.25 56.25  ? 65  ALA   A CB  1 
ATOM   221  N N   A GLU   A 1 23  ? -16.343 -1.656  -35.025 0.25 62.31  ? 66  GLU   A N   1 
ATOM   222  N N   B GLU   A 1 23  ? -16.343 -1.656  -35.025 0.25 62.31  ? 66  GLU   A N   1 
ATOM   223  N N   C GLU   A 1 23  ? -16.447 -1.639  -35.178 0.25 53.74  ? 66  GLU   A N   1 
ATOM   224  N N   D GLU   A 1 23  ? -16.447 -1.639  -35.178 0.25 53.74  ? 66  GLU   A N   1 
ATOM   225  C CA  A GLU   A 1 23  ? -14.898 -1.446  -35.327 0.25 63.84  ? 66  GLU   A CA  1 
ATOM   226  C CA  B GLU   A 1 23  ? -14.898 -1.446  -35.327 0.25 63.84  ? 66  GLU   A CA  1 
ATOM   227  C CA  C GLU   A 1 23  ? -14.963 -1.550  -35.219 0.25 54.13  ? 66  GLU   A CA  1 
ATOM   228  C CA  D GLU   A 1 23  ? -14.963 -1.550  -35.219 0.25 54.13  ? 66  GLU   A CA  1 
ATOM   229  C C   A GLU   A 1 23  ? -14.040 -2.349  -34.429 0.25 67.03  ? 66  GLU   A C   1 
ATOM   230  C C   B GLU   A 1 23  ? -14.040 -2.349  -34.429 0.25 67.03  ? 66  GLU   A C   1 
ATOM   231  C C   C GLU   A 1 23  ? -14.397 -2.612  -34.269 0.25 57.44  ? 66  GLU   A C   1 
ATOM   232  C C   D GLU   A 1 23  ? -14.397 -2.612  -34.269 0.25 57.44  ? 66  GLU   A C   1 
ATOM   233  O O   A GLU   A 1 23  ? -13.494 -1.840  -33.429 0.25 72.37  ? 66  GLU   A O   1 
ATOM   234  O O   B GLU   A 1 23  ? -13.494 -1.840  -33.429 0.25 72.37  ? 66  GLU   A O   1 
ATOM   235  O O   C GLU   A 1 23  ? -14.541 -2.450  -33.038 0.25 56.40  ? 66  GLU   A O   1 
ATOM   236  O O   D GLU   A 1 23  ? -14.541 -2.450  -33.038 0.25 56.40  ? 66  GLU   A O   1 
ATOM   237  C CB  A GLU   A 1 23  ? -14.561 0.035   -35.131 0.25 64.80  ? 66  GLU   A CB  1 
ATOM   238  C CB  B GLU   A 1 23  ? -14.561 0.035   -35.131 0.25 64.80  ? 66  GLU   A CB  1 
ATOM   239  C CB  C GLU   A 1 23  ? -14.521 -0.130  -34.847 0.25 54.26  ? 66  GLU   A CB  1 
ATOM   240  C CB  D GLU   A 1 23  ? -14.521 -0.130  -34.847 0.25 54.26  ? 66  GLU   A CB  1 
ATOM   241  C CG  A GLU   A 1 23  ? -13.120 0.401   -35.445 0.25 64.94  ? 66  GLU   A CG  1 
ATOM   242  C CG  B GLU   A 1 23  ? -13.120 0.401   -35.445 0.25 64.94  ? 66  GLU   A CG  1 
ATOM   243  C CG  C GLU   A 1 23  ? -13.069 -0.017  -34.407 0.25 53.15  ? 66  GLU   A CG  1 
ATOM   244  C CG  D GLU   A 1 23  ? -13.069 -0.017  -34.407 0.25 53.15  ? 66  GLU   A CG  1 
ATOM   245  C CD  A GLU   A 1 23  ? -12.904 1.893   -35.658 0.25 64.80  ? 66  GLU   A CD  1 
ATOM   246  C CD  B GLU   A 1 23  ? -12.904 1.893   -35.658 0.25 64.80  ? 66  GLU   A CD  1 
ATOM   247  C CD  C GLU   A 1 23  ? -12.704 1.327   -33.793 0.25 52.74  ? 66  GLU   A CD  1 
ATOM   248  C CD  D GLU   A 1 23  ? -12.704 1.327   -33.793 0.25 52.74  ? 66  GLU   A CD  1 
ATOM   249  O OE1 A GLU   A 1 23  ? -13.643 2.484   -36.473 0.25 62.42  ? 66  GLU   A OE1 1 
ATOM   250  O OE1 B GLU   A 1 23  ? -13.643 2.484   -36.473 0.25 62.42  ? 66  GLU   A OE1 1 
ATOM   251  O OE1 C GLU   A 1 23  ? -13.573 2.229   -33.777 0.25 49.73  ? 66  GLU   A OE1 1 
ATOM   252  O OE1 D GLU   A 1 23  ? -13.573 2.229   -33.777 0.25 49.73  ? 66  GLU   A OE1 1 
ATOM   253  O OE2 A GLU   A 1 23  ? -12.011 2.465   -34.999 0.25 65.26  ? 66  GLU   A OE2 1 
ATOM   254  O OE2 B GLU   A 1 23  ? -12.011 2.465   -34.999 0.25 65.26  ? 66  GLU   A OE2 1 
ATOM   255  O OE2 C GLU   A 1 23  ? -11.550 1.475   -33.336 0.25 50.71  ? 66  GLU   A OE2 1 
ATOM   256  O OE2 D GLU   A 1 23  ? -11.550 1.475   -33.336 0.25 50.71  ? 66  GLU   A OE2 1 
ATOM   257  N N   A VAL   A 1 24  ? -13.917 -3.634  -34.787 0.25 67.64  ? 67  VAL   A N   1 
ATOM   258  N N   B VAL   A 1 24  ? -13.917 -3.634  -34.787 0.25 67.64  ? 67  VAL   A N   1 
ATOM   259  N N   C VAL   A 1 24  ? -13.827 -3.686  -34.825 0.25 60.25  ? 67  VAL   A N   1 
ATOM   260  N N   D VAL   A 1 24  ? -13.827 -3.686  -34.825 0.25 60.25  ? 67  VAL   A N   1 
ATOM   261  C CA  A VAL   A 1 24  ? -13.155 -4.668  -34.021 0.25 62.68  ? 67  VAL   A CA  1 
ATOM   262  C CA  B VAL   A 1 24  ? -13.155 -4.668  -34.021 0.25 62.68  ? 67  VAL   A CA  1 
ATOM   263  C CA  C VAL   A 1 24  ? -13.114 -4.746  -34.053 0.25 57.69  ? 67  VAL   A CA  1 
ATOM   264  C CA  D VAL   A 1 24  ? -13.114 -4.746  -34.053 0.25 57.69  ? 67  VAL   A CA  1 
ATOM   265  C C   A VAL   A 1 24  ? -11.702 -4.199  -33.862 0.25 61.76  ? 67  VAL   A C   1 
ATOM   266  C C   B VAL   A 1 24  ? -11.702 -4.199  -33.862 0.25 61.76  ? 67  VAL   A C   1 
ATOM   267  C C   C VAL   A 1 24  ? -11.656 -4.303  -33.893 0.25 58.89  ? 67  VAL   A C   1 
ATOM   268  C C   D VAL   A 1 24  ? -11.656 -4.303  -33.893 0.25 58.89  ? 67  VAL   A C   1 
ATOM   269  O O   A VAL   A 1 24  ? -11.158 -3.646  -34.832 0.25 62.19  ? 67  VAL   A O   1 
ATOM   270  O O   B VAL   A 1 24  ? -11.158 -3.646  -34.832 0.25 62.19  ? 67  VAL   A O   1 
ATOM   271  O O   C VAL   A 1 24  ? -11.066 -3.862  -34.893 0.25 59.63  ? 67  VAL   A O   1 
ATOM   272  O O   D VAL   A 1 24  ? -11.066 -3.862  -34.893 0.25 59.63  ? 67  VAL   A O   1 
ATOM   273  C CB  A VAL   A 1 24  ? -13.223 -6.046  -34.706 0.25 60.11  ? 67  VAL   A CB  1 
ATOM   274  C CB  B VAL   A 1 24  ? -13.223 -6.046  -34.706 0.25 60.11  ? 67  VAL   A CB  1 
ATOM   275  C CB  C VAL   A 1 24  ? -13.214 -6.127  -34.727 0.25 55.65  ? 67  VAL   A CB  1 
ATOM   276  C CB  D VAL   A 1 24  ? -13.214 -6.127  -34.727 0.25 55.65  ? 67  VAL   A CB  1 
ATOM   277  C CG1 A VAL   A 1 24  ? -12.381 -7.075  -33.972 0.25 59.14  ? 67  VAL   A CG1 1 
ATOM   278  C CG1 B VAL   A 1 24  ? -12.381 -7.075  -33.972 0.25 59.14  ? 67  VAL   A CG1 1 
ATOM   279  C CG1 C VAL   A 1 24  ? -12.404 -7.166  -33.973 0.25 54.91  ? 67  VAL   A CG1 1 
ATOM   280  C CG1 D VAL   A 1 24  ? -12.404 -7.166  -33.973 0.25 54.91  ? 67  VAL   A CG1 1 
ATOM   281  C CG2 A VAL   A 1 24  ? -14.655 -6.537  -34.859 0.25 59.72  ? 67  VAL   A CG2 1 
ATOM   282  C CG2 B VAL   A 1 24  ? -14.655 -6.537  -34.859 0.25 59.72  ? 67  VAL   A CG2 1 
ATOM   283  C CG2 C VAL   A 1 24  ? -14.658 -6.586  -34.881 0.25 55.23  ? 67  VAL   A CG2 1 
ATOM   284  C CG2 D VAL   A 1 24  ? -14.658 -6.586  -34.881 0.25 55.23  ? 67  VAL   A CG2 1 
ATOM   285  N N   . THR   A 1 25  ? -11.112 -4.406  -32.680 1.00 61.91  ? 68  THR   A N   1 
ATOM   286  C CA  . THR   A 1 25  ? -9.716  -4.001  -32.372 1.00 64.39  ? 68  THR   A CA  1 
ATOM   287  C C   . THR   A 1 25  ? -9.274  -4.627  -31.042 1.00 66.93  ? 68  THR   A C   1 
ATOM   288  O O   . THR   A 1 25  ? -10.043 -5.430  -30.480 1.00 61.37  ? 68  THR   A O   1 
ATOM   289  C CB  . THR   A 1 25  ? -9.609  -2.470  -32.361 1.00 69.77  ? 68  THR   A CB  1 
ATOM   290  O OG1 . THR   A 1 25  ? -8.298  -2.105  -31.934 1.00 69.99  ? 68  THR   A OG1 1 
ATOM   291  C CG2 . THR   A 1 25  ? -10.634 -1.815  -31.461 1.00 71.60  ? 68  THR   A CG2 1 
ATOM   292  N N   . GLY   A 1 26  ? -8.067  -4.284  -30.579 1.00 67.15  ? 69  GLY   A N   1 
ATOM   293  C CA  . GLY   A 1 26  ? -7.518  -4.683  -29.269 1.00 66.54  ? 69  GLY   A CA  1 
ATOM   294  C C   . GLY   A 1 26  ? -7.106  -6.146  -29.219 1.00 63.51  ? 69  GLY   A C   1 
ATOM   295  O O   . GLY   A 1 26  ? -7.779  -6.973  -29.847 1.00 61.22  ? 69  GLY   A O   1 
ATOM   296  N N   . ASN   A 1 27  ? -6.070  -6.450  -28.433 1.00 66.70  ? 70  ASN   A N   1 
ATOM   297  C CA  . ASN   A 1 27  ? -5.504  -7.816  -28.237 1.00 70.50  ? 70  ASN   A CA  1 
ATOM   298  C C   . ASN   A 1 27  ? -6.060  -8.452  -26.948 1.00 62.52  ? 70  ASN   A C   1 
ATOM   299  O O   . ASN   A 1 27  ? -6.979  -7.852  -26.327 1.00 60.66  ? 70  ASN   A O   1 
ATOM   300  C CB  . ASN   A 1 27  ? -3.977  -7.766  -28.240 1.00 76.26  ? 70  ASN   A CB  1 
ATOM   301  C CG  . ASN   A 1 27  ? -3.446  -6.735  -27.275 1.00 82.19  ? 70  ASN   A CG  1 
ATOM   302  O OD1 . ASN   A 1 27  ? -3.759  -5.555  -27.412 1.00 89.62  ? 70  ASN   A OD1 1 
ATOM   303  N ND2 . ASN   A 1 27  ? -2.667  -7.174  -26.297 1.00 88.07  ? 70  ASN   A ND2 1 
ATOM   304  N N   . SER   A 1 28  ? -5.550  -9.633  -26.575 1.00 51.19  ? 71  SER   A N   1 
ATOM   305  C CA  . SER   A 1 28  ? -6.101  -10.484 -25.486 1.00 52.70  ? 71  SER   A CA  1 
ATOM   306  C C   . SER   A 1 28  ? -4.996  -10.954 -24.548 1.00 51.48  ? 71  SER   A C   1 
ATOM   307  O O   . SER   A 1 28  ? -4.796  -12.151 -24.398 1.00 54.83  ? 71  SER   A O   1 
ATOM   308  C CB  . SER   A 1 28  ? -6.838  -11.666 -26.058 1.00 49.71  ? 71  SER   A CB  1 
ATOM   309  O OG  . SER   A 1 28  ? -7.817  -11.257 -26.997 1.00 52.29  ? 71  SER   A OG  1 
ATOM   310  N N   . PRO   A 1 29  ? -4.285  -10.049 -23.840 1.00 53.90  ? 72  PRO   A N   1 
ATOM   311  C CA  . PRO   A 1 29  ? -3.132  -10.448 -23.036 1.00 54.02  ? 72  PRO   A CA  1 
ATOM   312  C C   . PRO   A 1 29  ? -3.535  -11.252 -21.792 1.00 53.59  ? 72  PRO   A C   1 
ATOM   313  O O   . PRO   A 1 29  ? -4.593  -11.032 -21.241 1.00 51.08  ? 72  PRO   A O   1 
ATOM   314  C CB  . PRO   A 1 29  ? -2.460  -9.116  -22.650 1.00 55.42  ? 72  PRO   A CB  1 
ATOM   315  C CG  . PRO   A 1 29  ? -3.581  -8.080  -22.708 1.00 57.18  ? 72  PRO   A CG  1 
ATOM   316  C CD  . PRO   A 1 29  ? -4.584  -8.611  -23.720 1.00 59.68  ? 72  PRO   A CD  1 
ATOM   317  N N   . ARG   A 1 30  ? -2.683  -12.192 -21.396 1.00 61.61  ? 73  ARG   A N   1 
ATOM   318  C CA  . ARG   A 1 30  ? -2.795  -12.911 -20.101 1.00 65.70  ? 73  ARG   A CA  1 
ATOM   319  C C   . ARG   A 1 30  ? -1.800  -12.232 -19.155 1.00 62.12  ? 73  ARG   A C   1 
ATOM   320  O O   . ARG   A 1 30  ? -0.594  -12.340 -19.410 1.00 55.60  ? 73  ARG   A O   1 
ATOM   321  C CB  . ARG   A 1 30  ? -2.539  -14.409 -20.304 1.00 72.43  ? 73  ARG   A CB  1 
ATOM   322  C CG  . ARG   A 1 30  ? -3.478  -15.077 -21.301 1.00 81.31  ? 73  ARG   A CG  1 
ATOM   323  C CD  . ARG   A 1 30  ? -2.838  -16.211 -22.087 1.00 89.59  ? 73  ARG   A CD  1 
ATOM   324  N NE  . ARG   A 1 30  ? -3.831  -16.940 -22.868 1.00 99.30  ? 73  ARG   A NE  1 
ATOM   325  C CZ  . ARG   A 1 30  ? -4.604  -17.926 -22.407 1.00 100.27 ? 73  ARG   A CZ  1 
ATOM   326  N NH1 . ARG   A 1 30  ? -4.494  -18.340 -21.155 1.00 107.91 ? 73  ARG   A NH1 1 
ATOM   327  N NH2 . ARG   A 1 30  ? -5.494  -18.497 -23.201 1.00 92.78  ? 73  ARG   A NH2 1 
ATOM   328  N N   . LEU   A 1 31  ? -2.280  -11.470 -18.171 1.00 63.96  ? 74  LEU   A N   1 
ATOM   329  C CA  . LEU   A 1 31  ? -1.396  -10.684 -17.271 1.00 63.90  ? 74  LEU   A CA  1 
ATOM   330  C C   . LEU   A 1 31  ? -1.528  -11.213 -15.840 1.00 63.22  ? 74  LEU   A C   1 
ATOM   331  O O   . LEU   A 1 31  ? -2.645  -11.630 -15.454 1.00 57.45  ? 74  LEU   A O   1 
ATOM   332  C CB  . LEU   A 1 31  ? -1.766  -9.208  -17.388 1.00 68.63  ? 74  LEU   A CB  1 
ATOM   333  C CG  . LEU   A 1 31  ? -1.446  -8.572  -18.740 1.00 72.76  ? 74  LEU   A CG  1 
ATOM   334  C CD1 . LEU   A 1 31  ? -2.144  -7.226  -18.879 1.00 69.24  ? 74  LEU   A CD1 1 
ATOM   335  C CD2 . LEU   A 1 31  ? 0.063   -8.427  -18.942 1.00 69.79  ? 74  LEU   A CD2 1 
ATOM   336  N N   . ASP   A 1 32  ? -0.406  -11.270 -15.118 1.00 57.89  ? 75  ASP   A N   1 
ATOM   337  C CA  . ASP   A 1 32  ? -0.362  -11.689 -13.694 1.00 56.14  ? 75  ASP   A CA  1 
ATOM   338  C C   . ASP   A 1 32  ? -0.506  -10.443 -12.831 1.00 49.65  ? 75  ASP   A C   1 
ATOM   339  O O   . ASP   A 1 32  ? 0.424   -9.589  -12.875 1.00 52.77  ? 75  ASP   A O   1 
ATOM   340  C CB  . ASP   A 1 32  ? 0.887   -12.520 -13.387 1.00 58.30  ? 75  ASP   A CB  1 
ATOM   341  C CG  . ASP   A 1 32  ? 0.613   -13.983 -13.675 1.00 59.46  ? 75  ASP   A CG  1 
ATOM   342  O OD1 . ASP   A 1 32  ? 0.256   -14.708 -12.727 1.00 56.55  ? 75  ASP   A OD1 1 
ATOM   343  O OD2 . ASP   A 1 32  ? 0.641   -14.352 -14.862 1.00 69.61  ? 75  ASP   A OD2 1 
ATOM   344  N N   . VAL   A 1 33  ? -1.630  -10.328 -12.113 1.00 42.05  ? 76  VAL   A N   1 
ATOM   345  C CA  . VAL   A 1 33  ? -1.981  -9.072  -11.382 1.00 47.18  ? 76  VAL   A CA  1 
ATOM   346  C C   . VAL   A 1 33  ? -2.269  -9.405  -9.917  1.00 45.68  ? 76  VAL   A C   1 
ATOM   347  O O   . VAL   A 1 33  ? -2.596  -10.567 -9.608  1.00 48.02  ? 76  VAL   A O   1 
ATOM   348  C CB  . VAL   A 1 33  ? -3.147  -8.296  -12.039 1.00 44.37  ? 76  VAL   A CB  1 
ATOM   349  C CG1 . VAL   A 1 33  ? -2.907  -8.049  -13.522 1.00 45.01  ? 76  VAL   A CG1 1 
ATOM   350  C CG2 . VAL   A 1 33  ? -4.485  -8.994  -11.849 1.00 44.28  ? 76  VAL   A CG2 1 
ATOM   351  N N   . ALA   A 1 34  ? -2.114  -8.400  -9.065  1.00 43.04  ? 77  ALA   A N   1 
ATOM   352  C CA  . ALA   A 1 34  ? -2.466  -8.399  -7.630  1.00 43.05  ? 77  ALA   A CA  1 
ATOM   353  C C   . ALA   A 1 34  ? -3.473  -7.273  -7.416  1.00 45.85  ? 77  ALA   A C   1 
ATOM   354  O O   . ALA   A 1 34  ? -3.268  -6.200  -7.979  1.00 47.55  ? 77  ALA   A O   1 
ATOM   355  C CB  . ALA   A 1 34  ? -1.242  -8.165  -6.794  1.00 40.30  ? 77  ALA   A CB  1 
ATOM   356  N N   . LEU   A 1 35  ? -4.529  -7.537  -6.657  1.00 53.59  ? 78  LEU   A N   1 
ATOM   357  C CA  . LEU   A 1 35  ? -5.540  -6.528  -6.255  1.00 57.17  ? 78  LEU   A CA  1 
ATOM   358  C C   . LEU   A 1 35  ? -5.279  -6.144  -4.790  1.00 59.18  ? 78  LEU   A C   1 
ATOM   359  O O   . LEU   A 1 35  ? -5.334  -7.029  -3.916  1.00 64.60  ? 78  LEU   A O   1 
ATOM   360  C CB  . LEU   A 1 35  ? -6.927  -7.140  -6.476  1.00 54.97  ? 78  LEU   A CB  1 
ATOM   361  C CG  . LEU   A 1 35  ? -8.120  -6.263  -6.095  1.00 53.99  ? 78  LEU   A CG  1 
ATOM   362  C CD1 . LEU   A 1 35  ? -8.048  -4.910  -6.780  1.00 56.14  ? 78  LEU   A CD1 1 
ATOM   363  C CD2 . LEU   A 1 35  ? -9.425  -6.975  -6.423  1.00 55.76  ? 78  LEU   A CD2 1 
ATOM   364  N N   . ASP   A 1 36  ? -4.983  -4.875  -4.530  1.00 58.01  ? 79  ASP   A N   1 
ATOM   365  C CA  . ASP   A 1 36  ? -4.718  -4.346  -3.165  1.00 56.13  ? 79  ASP   A CA  1 
ATOM   366  C C   . ASP   A 1 36  ? -6.047  -3.918  -2.511  1.00 52.49  ? 79  ASP   A C   1 
ATOM   367  O O   . ASP   A 1 36  ? -7.081  -3.912  -3.197  1.00 50.77  ? 79  ASP   A O   1 
ATOM   368  C CB  . ASP   A 1 36  ? -3.689  -3.206  -3.215  1.00 53.76  ? 79  ASP   A CB  1 
ATOM   369  C CG  . ASP   A 1 36  ? -4.283  -1.862  -3.589  1.00 51.71  ? 79  ASP   A CG  1 
ATOM   370  O OD1 . ASP   A 1 36  ? -5.484  -1.838  -3.892  1.00 54.83  ? 79  ASP   A OD1 1 
ATOM   371  O OD2 . ASP   A 1 36  ? -3.540  -0.855  -3.572  1.00 54.03  ? 79  ASP   A OD2 1 
ATOM   372  N N   . GLU   A 1 37  ? -5.988  -3.551  -1.226  1.00 46.78  ? 80  GLU   A N   1 
ATOM   373  C CA  . GLU   A 1 37  ? -7.145  -3.230  -0.360  1.00 44.88  ? 80  GLU   A CA  1 
ATOM   374  C C   . GLU   A 1 37  ? -7.854  -1.980  -0.894  1.00 43.82  ? 80  GLU   A C   1 
ATOM   375  O O   . GLU   A 1 37  ? -9.077  -1.915  -0.728  1.00 38.87  ? 80  GLU   A O   1 
ATOM   376  C CB  . GLU   A 1 37  ? -6.667  -3.080  1.089   1.00 48.41  ? 80  GLU   A CB  1 
ATOM   377  C CG  . GLU   A 1 37  ? -7.793  -3.047  2.114   1.00 52.28  ? 80  GLU   A CG  1 
ATOM   378  C CD  . GLU   A 1 37  ? -7.355  -2.941  3.574   1.00 55.51  ? 80  GLU   A CD  1 
ATOM   379  O OE1 . GLU   A 1 37  ? -6.990  -1.819  4.036   1.00 45.57  ? 80  GLU   A OE1 1 
ATOM   380  O OE2 . GLU   A 1 37  ? -7.376  -3.988  4.256   1.00 62.26  ? 80  GLU   A OE2 1 
ATOM   381  N N   . SER   A 1 38  ? -7.108  -1.051  -1.519  1.00 44.98  ? 81  SER   A N   1 
ATOM   382  C CA  . SER   A 1 38  ? -7.582  0.202   -2.177  1.00 41.85  ? 81  SER   A CA  1 
ATOM   383  C C   . SER   A 1 38  ? -8.274  -0.068  -3.521  1.00 41.25  ? 81  SER   A C   1 
ATOM   384  O O   . SER   A 1 38  ? -8.639  0.929   -4.189  1.00 41.15  ? 81  SER   A O   1 
ATOM   385  C CB  . SER   A 1 38  ? -6.429  1.152   -2.403  1.00 45.66  ? 81  SER   A CB  1 
ATOM   386  O OG  . SER   A 1 38  ? -5.763  1.444   -1.181  1.00 50.96  ? 81  SER   A OG  1 
ATOM   387  N N   . GLY   A 1 39  ? -8.412  -1.332  -3.951  1.00 39.31  ? 82  GLY   A N   1 
ATOM   388  C CA  . GLY   A 1 39  ? -8.979  -1.682  -5.273  1.00 39.54  ? 82  GLY   A CA  1 
ATOM   389  C C   . GLY   A 1 39  ? -8.070  -1.357  -6.463  1.00 40.51  ? 82  GLY   A C   1 
ATOM   390  O O   . GLY   A 1 39  ? -8.593  -1.338  -7.592  1.00 37.53  ? 82  GLY   A O   1 
ATOM   391  N N   . ASP   A 1 40  ? -6.755  -1.172  -6.256  1.00 47.84  ? 83  ASP   A N   1 
ATOM   392  C CA  . ASP   A 1 40  ? -5.762  -0.873  -7.331  1.00 48.62  ? 83  ASP   A CA  1 
ATOM   393  C C   . ASP   A 1 40  ? -5.009  -2.157  -7.718  1.00 47.22  ? 83  ASP   A C   1 
ATOM   394  O O   . ASP   A 1 40  ? -4.249  -2.672  -6.889  1.00 41.24  ? 83  ASP   A O   1 
ATOM   395  C CB  . ASP   A 1 40  ? -4.765  0.221   -6.938  1.00 45.31  ? 83  ASP   A CB  1 
ATOM   396  C CG  . ASP   A 1 40  ? -5.396  1.509   -6.454  1.00 46.21  ? 83  ASP   A CG  1 
ATOM   397  O OD1 . ASP   A 1 40  ? -6.289  2.019   -7.126  1.00 54.72  ? 83  ASP   A OD1 1 
ATOM   398  O OD2 . ASP   A 1 40  ? -4.997  1.984   -5.392  1.00 53.43  ? 83  ASP   A OD2 1 
ATOM   399  N N   . PHE   A 1 41  ? -5.219  -2.619  -8.958  1.00 49.22  ? 84  PHE   A N   1 
ATOM   400  C CA  . PHE   A 1 41  ? -4.465  -3.693  -9.649  1.00 42.18  ? 84  PHE   A CA  1 
ATOM   401  C C   . PHE   A 1 41  ? -3.016  -3.277  -9.880  1.00 48.37  ? 84  PHE   A C   1 
ATOM   402  O O   . PHE   A 1 41  ? -2.744  -2.061  -9.942  1.00 45.93  ? 84  PHE   A O   1 
ATOM   403  C CB  . PHE   A 1 41  ? -5.094  -4.005  -10.997 1.00 38.85  ? 84  PHE   A CB  1 
ATOM   404  C CG  . PHE   A 1 41  ? -6.390  -4.761  -10.880 1.00 41.60  ? 84  PHE   A CG  1 
ATOM   405  C CD1 . PHE   A 1 41  ? -6.394  -6.092  -10.479 1.00 38.95  ? 84  PHE   A CD1 1 
ATOM   406  C CD2 . PHE   A 1 41  ? -7.604  -4.145  -11.161 1.00 40.47  ? 84  PHE   A CD2 1 
ATOM   407  C CE1 . PHE   A 1 41  ? -7.582  -6.796  -10.376 1.00 39.74  ? 84  PHE   A CE1 1 
ATOM   408  C CE2 . PHE   A 1 41  ? -8.790  -4.861  -11.062 1.00 41.66  ? 84  PHE   A CE2 1 
ATOM   409  C CZ  . PHE   A 1 41  ? -8.778  -6.181  -10.675 1.00 36.88  ? 84  PHE   A CZ  1 
ATOM   410  N N   . SER   A 1 42  ? -2.137  -4.275  -10.033 1.00 45.80  ? 85  SER   A N   1 
ATOM   411  C CA  . SER   A 1 42  ? -0.678  -4.109  -10.229 1.00 50.84  ? 85  SER   A CA  1 
ATOM   412  C C   . SER   A 1 42  ? -0.126  -5.369  -10.892 1.00 52.11  ? 85  SER   A C   1 
ATOM   413  O O   . SER   A 1 42  ? -0.606  -6.454  -10.542 1.00 50.76  ? 85  SER   A O   1 
ATOM   414  C CB  . SER   A 1 42  ? -0.018  -3.869  -8.914  1.00 54.32  ? 85  SER   A CB  1 
ATOM   415  O OG  . SER   A 1 42  ? -0.315  -4.936  -8.026  1.00 58.01  ? 85  SER   A OG  1 
ATOM   416  N N   . LEU   A 1 43  ? 0.823   -5.239  -11.821 1.00 57.35  ? 86  LEU   A N   1 
ATOM   417  C CA  . LEU   A 1 43  ? 1.432   -6.421  -12.488 1.00 61.63  ? 86  LEU   A CA  1 
ATOM   418  C C   . LEU   A 1 43  ? 2.354   -7.125  -11.498 1.00 59.06  ? 86  LEU   A C   1 
ATOM   419  O O   . LEU   A 1 43  ? 3.388   -6.534  -11.144 1.00 59.95  ? 86  LEU   A O   1 
ATOM   420  C CB  . LEU   A 1 43  ? 2.190   -5.987  -13.741 1.00 63.97  ? 86  LEU   A CB  1 
ATOM   421  C CG  . LEU   A 1 43  ? 1.292   -5.485  -14.863 1.00 67.99  ? 86  LEU   A CG  1 
ATOM   422  C CD1 . LEU   A 1 43  ? 2.122   -4.995  -16.035 1.00 76.25  ? 86  LEU   A CD1 1 
ATOM   423  C CD2 . LEU   A 1 43  ? 0.329   -6.579  -15.308 1.00 70.83  ? 86  LEU   A CD2 1 
ATOM   424  N N   . VAL   A 1 44  ? 1.947   -8.313  -11.047 1.00 60.86  ? 87  VAL   A N   1 
ATOM   425  C CA  . VAL   A 1 44  ? 2.770   -9.253  -10.226 1.00 70.16  ? 87  VAL   A CA  1 
ATOM   426  C C   . VAL   A 1 44  ? 3.824   -9.908  -11.125 1.00 77.65  ? 87  VAL   A C   1 
ATOM   427  O O   . VAL   A 1 44  ? 3.433   -10.644 -12.068 1.00 82.07  ? 87  VAL   A O   1 
ATOM   428  C CB  . VAL   A 1 44  ? 1.905   -10.335 -9.556  1.00 67.97  ? 87  VAL   A CB  1 
ATOM   429  C CG1 . VAL   A 1 44  ? 2.727   -11.559 -9.158  1.00 67.76  ? 87  VAL   A CG1 1 
ATOM   430  C CG2 . VAL   A 1 44  ? 1.154   -9.768  -8.366  1.00 65.99  ? 87  VAL   A CG2 1 
ATOM   431  N N   . GLU   A 1 45  ? 5.105   -9.694  -10.816 1.00 74.09  ? 88  GLU   A N   1 
ATOM   432  C CA  . GLU   A 1 45  ? 6.239   -10.242 -11.601 1.00 77.12  ? 88  GLU   A CA  1 
ATOM   433  C C   . GLU   A 1 45  ? 7.260   -10.889 -10.650 1.00 78.63  ? 88  GLU   A C   1 
ATOM   434  O O   . GLU   A 1 45  ? 7.547   -12.095 -10.699 1.00 71.49  ? 88  GLU   A O   1 
ATOM   435  C CB  . GLU   A 1 45  ? 6.809   -9.098  -12.429 1.00 72.45  ? 88  GLU   A CB  1 
ATOM   436  C CG  . GLU   A 1 45  ? 5.816   -8.527  -13.419 1.00 67.22  ? 88  GLU   A CG  1 
ATOM   437  C CD  . GLU   A 1 45  ? 5.943   -9.098  -14.813 1.00 62.61  ? 88  GLU   A CD  1 
ATOM   438  O OE1 . GLU   A 1 45  ? 6.946   -9.782  -15.086 1.00 65.74  ? 88  GLU   A OE1 1 
ATOM   439  O OE2 . GLU   A 1 45  ? 5.052   -8.843  -15.617 1.00 60.20  ? 88  GLU   A OE2 1 
ATOM   440  N N   . GLY   B 2 7   ? -35.992 12.286  -11.561 1.00 83.75  ? 16  GLY   B N   1 
ATOM   441  C CA  . GLY   B 2 7   ? -35.050 12.195  -12.712 1.00 78.42  ? 16  GLY   B CA  1 
ATOM   442  C C   . GLY   B 2 7   ? -35.282 10.962  -13.577 1.00 79.89  ? 16  GLY   B C   1 
ATOM   443  O O   . GLY   B 2 7   ? -35.936 9.999   -13.099 1.00 75.51  ? 16  GLY   B O   1 
ATOM   444  N N   . GLU   B 2 8   ? -34.734 10.995  -14.801 1.00 72.52  ? 17  GLU   B N   1 
ATOM   445  C CA  . GLU   B 2 8   ? -34.858 9.950   -15.856 1.00 66.43  ? 17  GLU   B CA  1 
ATOM   446  C C   . GLU   B 2 8   ? -34.424 8.582   -15.314 1.00 60.41  ? 17  GLU   B C   1 
ATOM   447  O O   . GLU   B 2 8   ? -33.269 8.434   -14.893 1.00 54.77  ? 17  GLU   B O   1 
ATOM   448  C CB  . GLU   B 2 8   ? -34.007 10.319  -17.072 1.00 68.68  ? 17  GLU   B CB  1 
ATOM   449  C CG  . GLU   B 2 8   ? -34.107 9.315   -18.205 1.00 69.29  ? 17  GLU   B CG  1 
ATOM   450  C CD  . GLU   B 2 8   ? -33.512 9.791   -19.519 1.00 75.18  ? 17  GLU   B CD  1 
ATOM   451  O OE1 . GLU   B 2 8   ? -32.546 10.598  -19.472 1.00 69.01  ? 17  GLU   B OE1 1 
ATOM   452  O OE2 . GLU   B 2 8   ? -34.057 9.401   -20.591 1.00 84.11  ? 17  GLU   B OE2 1 
ATOM   453  N N   A THR   B 2 9   ? -35.335 7.601   -15.329 0.25 60.02  ? 18  THR   B N   1 
ATOM   454  N N   B THR   B 2 9   ? -35.346 7.616   -15.365 0.25 61.56  ? 18  THR   B N   1 
ATOM   455  N N   C THR   B 2 9   ? -35.335 7.601   -15.329 0.25 60.02  ? 18  THR   B N   1 
ATOM   456  N N   D THR   B 2 9   ? -35.346 7.616   -15.365 0.25 61.56  ? 18  THR   B N   1 
ATOM   457  C CA  A THR   B 2 9   ? -35.095 6.213   -14.844 0.25 59.81  ? 18  THR   B CA  1 
ATOM   458  C CA  B THR   B 2 9   ? -35.195 6.229   -14.853 0.25 62.12  ? 18  THR   B CA  1 
ATOM   459  C CA  C THR   B 2 9   ? -35.095 6.213   -14.844 0.25 59.81  ? 18  THR   B CA  1 
ATOM   460  C CA  D THR   B 2 9   ? -35.195 6.229   -14.853 0.25 62.12  ? 18  THR   B CA  1 
ATOM   461  C C   A THR   B 2 9   ? -34.877 5.251   -16.021 0.25 58.76  ? 18  THR   B C   1 
ATOM   462  C C   B THR   B 2 9   ? -34.953 5.251   -16.014 0.25 60.24  ? 18  THR   B C   1 
ATOM   463  C C   C THR   B 2 9   ? -34.877 5.251   -16.021 0.25 58.76  ? 18  THR   B C   1 
ATOM   464  C C   D THR   B 2 9   ? -34.953 5.251   -16.014 0.25 60.24  ? 18  THR   B C   1 
ATOM   465  O O   A THR   B 2 9   ? -34.586 4.068   -15.750 0.25 60.21  ? 18  THR   B O   1 
ATOM   466  O O   B THR   B 2 9   ? -34.718 4.059   -15.725 0.25 61.83  ? 18  THR   B O   1 
ATOM   467  O O   C THR   B 2 9   ? -34.586 4.068   -15.750 0.25 60.21  ? 18  THR   B O   1 
ATOM   468  O O   D THR   B 2 9   ? -34.718 4.059   -15.725 0.25 61.83  ? 18  THR   B O   1 
ATOM   469  C CB  A THR   B 2 9   ? -36.257 5.705   -13.980 0.25 59.21  ? 18  THR   B CB  1 
ATOM   470  C CB  B THR   B 2 9   ? -36.433 5.845   -14.034 0.25 63.43  ? 18  THR   B CB  1 
ATOM   471  C CB  C THR   B 2 9   ? -36.257 5.705   -13.980 0.25 59.21  ? 18  THR   B CB  1 
ATOM   472  C CB  D THR   B 2 9   ? -36.433 5.845   -14.034 0.25 63.43  ? 18  THR   B CB  1 
ATOM   473  O OG1 A THR   B 2 9   ? -36.773 6.793   -13.211 0.25 59.98  ? 18  THR   B OG1 1 
ATOM   474  O OG1 B THR   B 2 9   ? -37.570 6.422   -14.678 0.25 63.62  ? 18  THR   B OG1 1 
ATOM   475  O OG1 C THR   B 2 9   ? -36.773 6.793   -13.211 0.25 59.98  ? 18  THR   B OG1 1 
ATOM   476  O OG1 D THR   B 2 9   ? -37.570 6.422   -14.678 0.25 63.62  ? 18  THR   B OG1 1 
ATOM   477  C CG2 A THR   B 2 9   ? -35.842 4.568   -13.071 0.25 57.54  ? 18  THR   B CG2 1 
ATOM   478  C CG2 B THR   B 2 9   ? -36.375 6.332   -12.603 0.25 64.71  ? 18  THR   B CG2 1 
ATOM   479  C CG2 C THR   B 2 9   ? -35.842 4.568   -13.071 0.25 57.54  ? 18  THR   B CG2 1 
ATOM   480  C CG2 D THR   B 2 9   ? -36.375 6.332   -12.603 0.25 64.71  ? 18  THR   B CG2 1 
ATOM   481  N N   . THR   B 2 10  ? -35.003 5.732   -17.264 1.00 57.27  ? 19  THR   B N   1 
ATOM   482  C CA  . THR   B 2 10  ? -34.945 4.887   -18.490 1.00 54.93  ? 19  THR   B CA  1 
ATOM   483  C C   . THR   B 2 10  ? -33.663 4.046   -18.508 1.00 49.88  ? 19  THR   B C   1 
ATOM   484  O O   . THR   B 2 10  ? -32.579 4.626   -18.341 1.00 47.10  ? 19  THR   B O   1 
ATOM   485  C CB  . THR   B 2 10  ? -34.999 5.705   -19.797 1.00 60.20  ? 19  THR   B CB  1 
ATOM   486  O OG1 . THR   B 2 10  ? -35.956 6.767   -19.773 1.00 63.17  ? 19  THR   B OG1 1 
ATOM   487  C CG2 . THR   B 2 10  ? -35.327 4.838   -20.995 1.00 59.99  ? 19  THR   B CG2 1 
ATOM   488  N N   . ASP   B 2 11  ? -33.798 2.737   -18.741 1.00 47.42  ? 20  ASP   B N   1 
ATOM   489  C CA  . ASP   B 2 11  ? -32.673 1.791   -18.969 1.00 47.31  ? 20  ASP   B CA  1 
ATOM   490  C C   . ASP   B 2 11  ? -31.769 2.322   -20.086 1.00 45.74  ? 20  ASP   B C   1 
ATOM   491  O O   . ASP   B 2 11  ? -32.313 2.915   -21.026 1.00 49.01  ? 20  ASP   B O   1 
ATOM   492  C CB  . ASP   B 2 11  ? -33.203 0.394   -19.299 1.00 50.09  ? 20  ASP   B CB  1 
ATOM   493  C CG  . ASP   B 2 11  ? -33.684 -0.349  -18.068 1.00 50.67  ? 20  ASP   B CG  1 
ATOM   494  O OD1 . ASP   B 2 11  ? -33.913 0.321   -17.044 1.00 38.93  ? 20  ASP   B OD1 1 
ATOM   495  O OD2 . ASP   B 2 11  ? -33.809 -1.587  -18.141 1.00 60.88  ? 20  ASP   B OD2 1 
ATOM   496  N N   . GLY   B 2 12  ? -30.453 2.114   -19.969 1.00 41.14  ? 21  GLY   B N   1 
ATOM   497  C CA  . GLY   B 2 12  ? -29.439 2.509   -20.966 1.00 40.87  ? 21  GLY   B CA  1 
ATOM   498  C C   . GLY   B 2 12  ? -28.208 3.077   -20.295 1.00 35.97  ? 21  GLY   B C   1 
ATOM   499  O O   . GLY   B 2 12  ? -28.086 2.939   -19.070 1.00 35.68  ? 21  GLY   B O   1 
ATOM   500  N N   . VAL   B 2 13  ? -27.329 3.716   -21.054 1.00 37.78  ? 22  VAL   B N   1 
ATOM   501  C CA  . VAL   B 2 13  ? -26.002 4.169   -20.541 1.00 37.59  ? 22  VAL   B CA  1 
ATOM   502  C C   . VAL   B 2 13  ? -26.030 5.687   -20.360 1.00 40.08  ? 22  VAL   B C   1 
ATOM   503  O O   . VAL   B 2 13  ? -26.726 6.397   -21.115 1.00 43.85  ? 22  VAL   B O   1 
ATOM   504  C CB  . VAL   B 2 13  ? -24.840 3.703   -21.435 1.00 37.40  ? 22  VAL   B CB  1 
ATOM   505  C CG1 . VAL   B 2 13  ? -24.957 4.191   -22.879 1.00 36.86  ? 22  VAL   B CG1 1 
ATOM   506  C CG2 . VAL   B 2 13  ? -23.504 4.097   -20.846 1.00 39.85  ? 22  VAL   B CG2 1 
ATOM   507  N N   . TYR   B 2 14  ? -25.296 6.174   -19.366 1.00 45.80  ? 23  TYR   B N   1 
ATOM   508  C CA  . TYR   B 2 14  ? -25.302 7.601   -18.958 1.00 40.65  ? 23  TYR   B CA  1 
ATOM   509  C C   . TYR   B 2 14  ? -23.878 8.072   -18.733 1.00 37.48  ? 23  TYR   B C   1 
ATOM   510  O O   . TYR   B 2 14  ? -23.026 7.245   -18.340 1.00 42.63  ? 23  TYR   B O   1 
ATOM   511  C CB  . TYR   B 2 14  ? -26.068 7.802   -17.651 1.00 36.94  ? 23  TYR   B CB  1 
ATOM   512  C CG  . TYR   B 2 14  ? -27.541 7.610   -17.796 1.00 30.01  ? 23  TYR   B CG  1 
ATOM   513  C CD1 . TYR   B 2 14  ? -28.051 6.370   -18.109 1.00 30.36  ? 23  TYR   B CD1 1 
ATOM   514  C CD2 . TYR   B 2 14  ? -28.413 8.680   -17.657 1.00 32.07  ? 23  TYR   B CD2 1 
ATOM   515  C CE1 . TYR   B 2 14  ? -29.410 6.178   -18.276 1.00 32.68  ? 23  TYR   B CE1 1 
ATOM   516  C CE2 . TYR   B 2 14  ? -29.776 8.509   -17.828 1.00 32.26  ? 23  TYR   B CE2 1 
ATOM   517  C CZ  . TYR   B 2 14  ? -30.273 7.255   -18.137 1.00 33.80  ? 23  TYR   B CZ  1 
ATOM   518  O OH  . TYR   B 2 14  ? -31.615 7.059   -18.282 1.00 37.17  ? 23  TYR   B OH  1 
ATOM   519  N N   . ARG   B 2 15  ? -23.656 9.356   -18.992 1.00 35.85  ? 24  ARG   B N   1 
ATOM   520  C CA  . ARG   B 2 15  ? -22.408 10.056  -18.635 1.00 34.96  ? 24  ARG   B CA  1 
ATOM   521  C C   . ARG   B 2 15  ? -22.552 10.591  -17.221 1.00 38.58  ? 24  ARG   B C   1 
ATOM   522  O O   . ARG   B 2 15  ? -23.622 11.108  -16.890 1.00 41.28  ? 24  ARG   B O   1 
ATOM   523  C CB  . ARG   B 2 15  ? -22.155 11.214  -19.592 1.00 38.28  ? 24  ARG   B CB  1 
ATOM   524  C CG  . ARG   B 2 15  ? -22.161 10.802  -21.050 1.00 41.31  ? 24  ARG   B CG  1 
ATOM   525  C CD  . ARG   B 2 15  ? -21.976 11.996  -21.947 1.00 45.52  ? 24  ARG   B CD  1 
ATOM   526  N NE  . ARG   B 2 15  ? -22.147 11.571  -23.327 1.00 45.55  ? 24  ARG   B NE  1 
ATOM   527  C CZ  . ARG   B 2 15  ? -21.208 11.592  -24.264 1.00 47.14  ? 24  ARG   B CZ  1 
ATOM   528  N NH1 . ARG   B 2 15  ? -19.995 12.066  -24.000 1.00 44.73  ? 24  ARG   B NH1 1 
ATOM   529  N NH2 . ARG   B 2 15  ? -21.513 11.156  -25.478 1.00 46.72  ? 24  ARG   B NH2 1 
ATOM   530  N N   . VAL   B 2 16  ? -21.475 10.533  -16.454 1.00 41.31  ? 25  VAL   B N   1 
ATOM   531  C CA  . VAL   B 2 16  ? -21.397 11.105  -15.089 1.00 42.95  ? 25  VAL   B CA  1 
ATOM   532  C C   . VAL   B 2 16  ? -20.589 12.416  -15.210 1.00 43.55  ? 25  VAL   B C   1 
ATOM   533  O O   . VAL   B 2 16  ? -19.355 12.351  -15.416 1.00 37.51  ? 25  VAL   B O   1 
ATOM   534  C CB  . VAL   B 2 16  ? -20.831 10.041  -14.114 1.00 43.84  ? 25  VAL   B CB  1 
ATOM   535  C CG1 . VAL   B 2 16  ? -20.717 10.557  -12.688 1.00 45.34  ? 25  VAL   B CG1 1 
ATOM   536  C CG2 . VAL   B 2 16  ? -21.677 8.765   -14.133 1.00 41.63  ? 25  VAL   B CG2 1 
ATOM   537  N N   . MET   B 2 17  ? -21.288 13.560  -15.147 1.00 44.01  ? 26  MET   B N   1 
ATOM   538  C CA  . MET   B 2 17  ? -20.748 14.935  -15.300 1.00 44.51  ? 26  MET   B CA  1 
ATOM   539  C C   . MET   B 2 17  ? -20.615 15.631  -13.930 1.00 48.22  ? 26  MET   B C   1 
ATOM   540  O O   . MET   B 2 17  ? -21.406 15.294  -13.017 1.00 45.08  ? 26  MET   B O   1 
ATOM   541  C CB  . MET   B 2 17  ? -21.666 15.791  -16.181 1.00 45.90  ? 26  MET   B CB  1 
ATOM   542  C CG  . MET   B 2 17  ? -22.047 15.176  -17.525 1.00 50.46  ? 26  MET   B CG  1 
ATOM   543  S SD  . MET   B 2 17  ? -20.689 14.640  -18.637 1.00 54.45  ? 26  MET   B SD  1 
ATOM   544  C CE  . MET   B 2 17  ? -19.724 16.143  -18.773 1.00 56.40  ? 26  MET   B CE  1 
ATOM   545  N N   . THR   B 2 18  ? -19.657 16.575  -13.836 1.00 48.97  ? 27  THR   B N   1 
ATOM   546  C CA  . THR   B 2 18  ? -19.467 17.588  -12.759 1.00 56.04  ? 27  THR   B CA  1 
ATOM   547  C C   . THR   B 2 18  ? -19.217 18.991  -13.344 1.00 59.65  ? 27  THR   B C   1 
ATOM   548  O O   . THR   B 2 18  ? -18.684 19.115  -14.481 1.00 50.96  ? 27  THR   B O   1 
ATOM   549  C CB  . THR   B 2 18  ? -18.294 17.250  -11.824 1.00 59.11  ? 27  THR   B CB  1 
ATOM   550  O OG1 . THR   B 2 18  ? -18.288 18.244  -10.794 1.00 56.53  ? 27  THR   B OG1 1 
ATOM   551  C CG2 . THR   B 2 18  ? -16.946 17.197  -12.513 1.00 54.81  ? 27  THR   B CG2 1 
ATOM   552  N N   . ARG   B 2 19  ? -19.573 20.022  -12.570 1.00 65.09  ? 28  ARG   B N   1 
ATOM   553  C CA  . ARG   B 2 19  ? -19.317 21.452  -12.904 1.00 69.41  ? 28  ARG   B CA  1 
ATOM   554  C C   . ARG   B 2 19  ? -18.378 22.072  -11.868 1.00 66.22  ? 28  ARG   B C   1 
ATOM   555  O O   . ARG   B 2 19  ? -18.206 23.302  -11.897 1.00 67.42  ? 28  ARG   B O   1 
ATOM   556  C CB  . ARG   B 2 19  ? -20.634 22.233  -12.978 1.00 66.52  ? 28  ARG   B CB  1 
ATOM   557  C CG  . ARG   B 2 19  ? -21.473 21.866  -14.191 1.00 66.04  ? 28  ARG   B CG  1 
ATOM   558  C CD  . ARG   B 2 19  ? -22.278 23.020  -14.735 1.00 64.23  ? 28  ARG   B CD  1 
ATOM   559  N NE  . ARG   B 2 19  ? -23.180 22.549  -15.776 1.00 66.88  ? 28  ARG   B NE  1 
ATOM   560  C CZ  . ARG   B 2 19  ? -24.331 21.893  -15.558 1.00 66.73  ? 28  ARG   B CZ  1 
ATOM   561  N NH1 . ARG   B 2 19  ? -24.736 21.613  -14.327 1.00 70.91  ? 28  ARG   B NH1 1 
ATOM   562  N NH2 . ARG   B 2 19  ? -25.072 21.499  -16.580 1.00 60.46  ? 28  ARG   B NH2 1 
ATOM   563  N N   . ARG   B 2 20  ? -17.785 21.247  -11.004 1.00 71.65  ? 29  ARG   B N   1 
ATOM   564  C CA  . ARG   B 2 20  ? -16.917 21.701  -9.885  1.00 77.47  ? 29  ARG   B CA  1 
ATOM   565  C C   . ARG   B 2 20  ? -15.637 22.283  -10.497 1.00 73.24  ? 29  ARG   B C   1 
ATOM   566  O O   . ARG   B 2 20  ? -15.152 23.312  -9.990  1.00 66.96  ? 29  ARG   B O   1 
ATOM   567  C CB  . ARG   B 2 20  ? -16.647 20.540  -8.923  1.00 78.84  ? 29  ARG   B CB  1 
ATOM   568  C CG  . ARG   B 2 20  ? -16.420 20.957  -7.478  1.00 86.87  ? 29  ARG   B CG  1 
ATOM   569  C CD  . ARG   B 2 20  ? -16.215 19.734  -6.604  1.00 101.05 ? 29  ARG   B CD  1 
ATOM   570  N NE  . ARG   B 2 20  ? -15.496 18.683  -7.322  1.00 113.50 ? 29  ARG   B NE  1 
ATOM   571  C CZ  . ARG   B 2 20  ? -14.182 18.669  -7.565  1.00 121.35 ? 29  ARG   B CZ  1 
ATOM   572  N NH1 . ARG   B 2 20  ? -13.407 19.655  -7.141  1.00 128.87 ? 29  ARG   B NH1 1 
ATOM   573  N NH2 . ARG   B 2 20  ? -13.642 17.667  -8.240  1.00 119.05 ? 29  ARG   B NH2 1 
ATOM   574  N N   . LEU   B 2 21  ? -15.149 21.656  -11.572 1.00 75.37  ? 30  LEU   B N   1 
ATOM   575  C CA  . LEU   B 2 21  ? -13.978 22.108  -12.372 1.00 72.50  ? 30  LEU   B CA  1 
ATOM   576  C C   . LEU   B 2 21  ? -14.441 23.125  -13.426 1.00 66.55  ? 30  LEU   B C   1 
ATOM   577  O O   . LEU   B 2 21  ? -15.630 23.513  -13.414 1.00 64.75  ? 30  LEU   B O   1 
ATOM   578  C CB  . LEU   B 2 21  ? -13.317 20.878  -13.010 1.00 75.27  ? 30  LEU   B CB  1 
ATOM   579  C CG  . LEU   B 2 21  ? -12.418 20.015  -12.118 1.00 76.28  ? 30  LEU   B CG  1 
ATOM   580  C CD1 . LEU   B 2 21  ? -12.226 20.605  -10.723 1.00 72.81  ? 30  LEU   B CD1 1 
ATOM   581  C CD2 . LEU   B 2 21  ? -12.954 18.589  -12.044 1.00 78.13  ? 30  LEU   B CD2 1 
ATOM   582  N N   . LEU   B 2 22  ? -13.512 23.579  -14.271 1.00 69.05  ? 31  LEU   B N   1 
ATOM   583  C CA  . LEU   B 2 22  ? -13.779 24.505  -15.402 1.00 65.09  ? 31  LEU   B CA  1 
ATOM   584  C C   . LEU   B 2 22  ? -14.747 23.826  -16.364 1.00 63.32  ? 31  LEU   B C   1 
ATOM   585  O O   . LEU   B 2 22  ? -14.561 22.622  -16.590 1.00 74.60  ? 31  LEU   B O   1 
ATOM   586  C CB  . LEU   B 2 22  ? -12.466 24.809  -16.117 1.00 61.70  ? 31  LEU   B CB  1 
ATOM   587  C CG  . LEU   B 2 22  ? -12.590 25.801  -17.265 1.00 60.27  ? 31  LEU   B CG  1 
ATOM   588  C CD1 . LEU   B 2 22  ? -12.282 27.212  -16.780 1.00 57.49  ? 31  LEU   B CD1 1 
ATOM   589  C CD2 . LEU   B 2 22  ? -11.681 25.389  -18.413 1.00 58.94  ? 31  LEU   B CD2 1 
ATOM   590  N N   . GLY   B 2 23  ? -15.718 24.566  -16.908 1.00 57.18  ? 32  GLY   B N   1 
ATOM   591  C CA  . GLY   B 2 23  ? -16.785 24.004  -17.760 1.00 53.24  ? 32  GLY   B CA  1 
ATOM   592  C C   . GLY   B 2 23  ? -17.493 22.848  -17.069 1.00 48.88  ? 32  GLY   B C   1 
ATOM   593  O O   . GLY   B 2 23  ? -17.503 22.828  -15.824 1.00 45.96  ? 32  GLY   B O   1 
ATOM   594  N N   . SER   B 2 24  ? -18.093 21.952  -17.860 1.00 52.82  ? 33  SER   B N   1 
ATOM   595  C CA  . SER   B 2 24  ? -18.683 20.649  -17.456 1.00 48.83  ? 33  SER   B CA  1 
ATOM   596  C C   . SER   B 2 24  ? -17.708 19.552  -17.873 1.00 53.40  ? 33  SER   B C   1 
ATOM   597  O O   . SER   B 2 24  ? -17.371 19.535  -19.059 1.00 55.30  ? 33  SER   B O   1 
ATOM   598  C CB  . SER   B 2 24  ? -20.007 20.443  -18.115 1.00 47.01  ? 33  SER   B CB  1 
ATOM   599  O OG  . SER   B 2 24  ? -20.896 21.507  -17.796 1.00 54.73  ? 33  SER   B OG  1 
ATOM   600  N N   . THR   B 2 25  ? -17.281 18.692  -16.941 1.00 55.58  ? 34  THR   B N   1 
ATOM   601  C CA  . THR   B 2 25  ? -16.223 17.658  -17.114 1.00 49.48  ? 34  THR   B CA  1 
ATOM   602  C C   . THR   B 2 25  ? -16.869 16.282  -16.942 1.00 52.55  ? 34  THR   B C   1 
ATOM   603  O O   . THR   B 2 25  ? -17.517 16.094  -15.902 1.00 51.80  ? 34  THR   B O   1 
ATOM   604  C CB  . THR   B 2 25  ? -15.103 17.878  -16.089 1.00 49.96  ? 34  THR   B CB  1 
ATOM   605  O OG1 . THR   B 2 25  ? -14.650 19.224  -16.202 1.00 47.58  ? 34  THR   B OG1 1 
ATOM   606  C CG2 . THR   B 2 25  ? -13.910 16.967  -16.262 1.00 51.30  ? 34  THR   B CG2 1 
ATOM   607  N N   . GLN   B 2 26  ? -16.697 15.363  -17.899 1.00 51.75  ? 35  GLN   B N   1 
ATOM   608  C CA  . GLN   B 2 26  ? -17.152 13.946  -17.771 1.00 51.41  ? 35  GLN   B CA  1 
ATOM   609  C C   . GLN   B 2 26  ? -16.168 13.151  -16.898 1.00 53.67  ? 35  GLN   B C   1 
ATOM   610  O O   . GLN   B 2 26  ? -15.130 12.693  -17.415 1.00 60.46  ? 35  GLN   B O   1 
ATOM   611  C CB  . GLN   B 2 26  ? -17.290 13.255  -19.127 1.00 50.65  ? 35  GLN   B CB  1 
ATOM   612  C CG  . GLN   B 2 26  ? -17.595 11.765  -19.013 1.00 50.83  ? 35  GLN   B CG  1 
ATOM   613  C CD  . GLN   B 2 26  ? -18.187 11.190  -20.272 1.00 50.26  ? 35  GLN   B CD  1 
ATOM   614  O OE1 . GLN   B 2 26  ? -18.809 11.894  -21.062 1.00 50.12  ? 35  GLN   B OE1 1 
ATOM   615  N NE2 . GLN   B 2 26  ? -18.045 9.886   -20.446 1.00 53.17  ? 35  GLN   B NE2 1 
ATOM   616  N N   . VAL   B 2 27  ? -16.512 12.957  -15.627 1.00 47.22  ? 36  VAL   B N   1 
ATOM   617  C CA  . VAL   B 2 27  ? -15.687 12.214  -14.632 1.00 48.21  ? 36  VAL   B CA  1 
ATOM   618  C C   . VAL   B 2 27  ? -15.793 10.700  -14.896 1.00 45.44  ? 36  VAL   B C   1 
ATOM   619  O O   . VAL   B 2 27  ? -14.866 9.978   -14.506 1.00 48.20  ? 36  VAL   B O   1 
ATOM   620  C CB  . VAL   B 2 27  ? -16.121 12.603  -13.205 1.00 48.75  ? 36  VAL   B CB  1 
ATOM   621  C CG1 . VAL   B 2 27  ? -15.797 14.052  -12.907 1.00 48.73  ? 36  VAL   B CG1 1 
ATOM   622  C CG2 . VAL   B 2 27  ? -17.601 12.360  -12.964 1.00 50.02  ? 36  VAL   B CG2 1 
ATOM   623  N N   . GLY   B 2 28  ? -16.874 10.228  -15.537 1.00 44.63  ? 37  GLY   B N   1 
ATOM   624  C CA  . GLY   B 2 28  ? -17.124 8.789   -15.759 1.00 38.11  ? 37  GLY   B CA  1 
ATOM   625  C C   . GLY   B 2 28  ? -18.424 8.500   -16.494 1.00 35.42  ? 37  GLY   B C   1 
ATOM   626  O O   . GLY   B 2 28  ? -19.012 9.450   -17.029 1.00 36.87  ? 37  GLY   B O   1 
ATOM   627  N N   . VAL   B 2 29  ? -18.885 7.242   -16.430 1.00 32.30  ? 38  VAL   B N   1 
ATOM   628  C CA  . VAL   B 2 29  ? -20.050 6.654   -17.159 1.00 32.00  ? 38  VAL   B CA  1 
ATOM   629  C C   . VAL   B 2 29  ? -20.787 5.668   -16.235 1.00 33.54  ? 38  VAL   B C   1 
ATOM   630  O O   . VAL   B 2 29  ? -20.158 5.137   -15.286 1.00 33.81  ? 38  VAL   B O   1 
ATOM   631  C CB  . VAL   B 2 29  ? -19.547 5.910   -18.414 1.00 34.16  ? 38  VAL   B CB  1 
ATOM   632  C CG1 . VAL   B 2 29  ? -20.611 5.033   -19.072 1.00 36.18  ? 38  VAL   B CG1 1 
ATOM   633  C CG2 . VAL   B 2 29  ? -18.895 6.839   -19.419 1.00 35.04  ? 38  VAL   B CG2 1 
ATOM   634  N N   . GLY   B 2 30  ? -22.057 5.358   -16.510 1.00 32.28  ? 39  GLY   B N   1 
ATOM   635  C CA  . GLY   B 2 30  ? -22.770 4.344   -15.722 1.00 29.16  ? 39  GLY   B CA  1 
ATOM   636  C C   . GLY   B 2 30  ? -23.845 3.645   -16.508 1.00 28.58  ? 39  GLY   B C   1 
ATOM   637  O O   . GLY   B 2 30  ? -24.029 3.959   -17.673 1.00 35.07  ? 39  GLY   B O   1 
ATOM   638  N N   . VAL   B 2 31  ? -24.468 2.657   -15.900 1.00 28.28  ? 40  VAL   B N   1 
ATOM   639  C CA  . VAL   B 2 31  ? -25.544 1.847   -16.527 1.00 29.42  ? 40  VAL   B CA  1 
ATOM   640  C C   . VAL   B 2 31  ? -26.756 1.996   -15.623 1.00 32.50  ? 40  VAL   B C   1 
ATOM   641  O O   . VAL   B 2 31  ? -26.602 1.734   -14.398 1.00 28.42  ? 40  VAL   B O   1 
ATOM   642  C CB  . VAL   B 2 31  ? -25.187 0.359   -16.637 1.00 32.00  ? 40  VAL   B CB  1 
ATOM   643  C CG1 . VAL   B 2 31  ? -26.362 -0.451  -17.160 1.00 30.77  ? 40  VAL   B CG1 1 
ATOM   644  C CG2 . VAL   B 2 31  ? -23.938 0.122   -17.471 1.00 34.77  ? 40  VAL   B CG2 1 
ATOM   645  N N   . MET   B 2 32  ? -27.871 2.456   -16.200 1.00 34.92  ? 41  MET   B N   1 
ATOM   646  C CA  . MET   B 2 32  ? -29.215 2.405   -15.578 1.00 35.85  ? 41  MET   B CA  1 
ATOM   647  C C   . MET   B 2 32  ? -29.868 1.079   -15.981 1.00 36.08  ? 41  MET   B C   1 
ATOM   648  O O   . MET   B 2 32  ? -29.989 0.842   -17.197 1.00 33.96  ? 41  MET   B O   1 
ATOM   649  C CB  . MET   B 2 32  ? -30.076 3.583   -16.050 1.00 36.34  ? 41  MET   B CB  1 
ATOM   650  C CG  . MET   B 2 32  ? -31.301 3.818   -15.194 1.00 40.42  ? 41  MET   B CG  1 
ATOM   651  S SD  . MET   B 2 32  ? -30.899 4.373   -13.512 1.00 41.01  ? 41  MET   B SD  1 
ATOM   652  C CE  . MET   B 2 32  ? -30.190 5.978   -13.878 1.00 44.06  ? 41  MET   B CE  1 
ATOM   653  N N   . GLN   B 2 33  ? -30.253 0.238   -15.014 1.00 33.86  ? 42  GLN   B N   1 
ATOM   654  C CA  . GLN   B 2 33  ? -31.092 -0.970  -15.283 1.00 38.90  ? 42  GLN   B CA  1 
ATOM   655  C C   . GLN   B 2 33  ? -32.024 -1.229  -14.105 1.00 39.02  ? 42  GLN   B C   1 
ATOM   656  O O   . GLN   B 2 33  ? -31.561 -1.119  -12.966 1.00 45.31  ? 42  GLN   B O   1 
ATOM   657  C CB  . GLN   B 2 33  ? -30.240 -2.222  -15.527 1.00 39.37  ? 42  GLN   B CB  1 
ATOM   658  C CG  . GLN   B 2 33  ? -31.019 -3.305  -16.269 1.00 45.02  ? 42  GLN   B CG  1 
ATOM   659  C CD  . GLN   B 2 33  ? -30.189 -4.534  -16.533 1.00 50.67  ? 42  GLN   B CD  1 
ATOM   660  O OE1 . GLN   B 2 33  ? -30.472 -5.617  -16.020 1.00 59.53  ? 42  GLN   B OE1 1 
ATOM   661  N NE2 . GLN   B 2 33  ? -29.129 -4.361  -17.307 1.00 52.73  ? 42  GLN   B NE2 1 
ATOM   662  N N   . GLU   B 2 34  ? -33.273 -1.585  -14.364 1.00 43.30  ? 43  GLU   B N   1 
ATOM   663  C CA  . GLU   B 2 34  ? -34.254 -1.915  -13.296 1.00 52.37  ? 43  GLU   B CA  1 
ATOM   664  C C   . GLU   B 2 34  ? -34.253 -0.820  -12.207 1.00 49.95  ? 43  GLU   B C   1 
ATOM   665  O O   . GLU   B 2 34  ? -34.311 -1.159  -11.016 1.00 54.60  ? 43  GLU   B O   1 
ATOM   666  C CB  . GLU   B 2 34  ? -33.920 -3.306  -12.741 1.00 57.56  ? 43  GLU   B CB  1 
ATOM   667  C CG  . GLU   B 2 34  ? -34.300 -4.447  -13.678 1.00 57.82  ? 43  GLU   B CG  1 
ATOM   668  C CD  . GLU   B 2 34  ? -33.635 -5.770  -13.353 1.00 62.03  ? 43  GLU   B CD  1 
ATOM   669  O OE1 . GLU   B 2 34  ? -34.100 -6.438  -12.425 1.00 59.08  ? 43  GLU   B OE1 1 
ATOM   670  O OE2 . GLU   B 2 34  ? -32.639 -6.114  -14.025 1.00 62.35  ? 43  GLU   B OE2 1 
ATOM   671  N N   . GLY   B 2 35  ? -34.171 0.453   -12.592 1.00 47.32  ? 44  GLY   B N   1 
ATOM   672  C CA  . GLY   B 2 35  ? -34.311 1.603   -11.673 1.00 48.52  ? 44  GLY   B CA  1 
ATOM   673  C C   . GLY   B 2 35  ? -33.064 1.874   -10.843 1.00 51.76  ? 44  GLY   B C   1 
ATOM   674  O O   . GLY   B 2 35  ? -33.055 2.876   -10.091 1.00 51.58  ? 44  GLY   B O   1 
ATOM   675  N N   . VAL   B 2 36  ? -32.037 1.027   -10.971 1.00 48.98  ? 45  VAL   B N   1 
ATOM   676  C CA  . VAL   B 2 36  ? -30.740 1.148   -10.256 1.00 40.04  ? 45  VAL   B CA  1 
ATOM   677  C C   . VAL   B 2 36  ? -29.689 1.646   -11.249 1.00 38.01  ? 45  VAL   B C   1 
ATOM   678  O O   . VAL   B 2 36  ? -29.652 1.112   -12.411 1.00 37.43  ? 45  VAL   B O   1 
ATOM   679  C CB  . VAL   B 2 36  ? -30.346 -0.192  -9.617  1.00 44.77  ? 45  VAL   B CB  1 
ATOM   680  C CG1 . VAL   B 2 36  ? -28.884 -0.228  -9.162  1.00 46.28  ? 45  VAL   B CG1 1 
ATOM   681  C CG2 . VAL   B 2 36  ? -31.283 -0.514  -8.468  1.00 47.17  ? 45  VAL   B CG2 1 
ATOM   682  N N   . PHE   B 2 37  ? -28.870 2.617   -10.805 1.00 31.65  ? 46  PHE   B N   1 
ATOM   683  C CA  . PHE   B 2 37  ? -27.742 3.197   -11.568 1.00 29.41  ? 46  PHE   B CA  1 
ATOM   684  C C   . PHE   B 2 37  ? -26.464 2.520   -11.074 1.00 26.56  ? 46  PHE   B C   1 
ATOM   685  O O   . PHE   B 2 37  ? -26.248 2.500   -9.871  1.00 26.03  ? 46  PHE   B O   1 
ATOM   686  C CB  . PHE   B 2 37  ? -27.669 4.711   -11.408 1.00 28.84  ? 46  PHE   B CB  1 
ATOM   687  C CG  . PHE   B 2 37  ? -26.699 5.345   -12.373 1.00 28.43  ? 46  PHE   B CG  1 
ATOM   688  C CD1 . PHE   B 2 37  ? -26.856 5.175   -13.739 1.00 29.84  ? 46  PHE   B CD1 1 
ATOM   689  C CD2 . PHE   B 2 37  ? -25.580 6.014   -11.921 1.00 27.74  ? 46  PHE   B CD2 1 
ATOM   690  C CE1 . PHE   B 2 37  ? -25.958 5.727   -14.637 1.00 27.06  ? 46  PHE   B CE1 1 
ATOM   691  C CE2 . PHE   B 2 37  ? -24.664 6.533   -12.818 1.00 27.31  ? 46  PHE   B CE2 1 
ATOM   692  C CZ  . PHE   B 2 37  ? -24.870 6.405   -14.171 1.00 27.10  ? 46  PHE   B CZ  1 
ATOM   693  N N   . HIS   B 2 38  ? -25.697 1.930   -11.988 1.00 27.82  ? 47  HIS   B N   1 
ATOM   694  C CA  . HIS   B 2 38  ? -24.468 1.153   -11.686 1.00 26.67  ? 47  HIS   B CA  1 
ATOM   695  C C   . HIS   B 2 38  ? -23.228 1.883   -12.186 1.00 28.28  ? 47  HIS   B C   1 
ATOM   696  O O   . HIS   B 2 38  ? -23.117 2.142   -13.378 1.00 34.38  ? 47  HIS   B O   1 
ATOM   697  C CB  . HIS   B 2 38  ? -24.550 -0.188  -12.368 1.00 26.91  ? 47  HIS   B CB  1 
ATOM   698  C CG  . HIS   B 2 38  ? -25.758 -0.969  -12.010 1.00 25.79  ? 47  HIS   B CG  1 
ATOM   699  N ND1 . HIS   B 2 38  ? -26.941 -0.838  -12.697 1.00 28.17  ? 47  HIS   B ND1 1 
ATOM   700  C CD2 . HIS   B 2 38  ? -25.963 -1.924  -11.091 1.00 29.49  ? 47  HIS   B CD2 1 
ATOM   701  C CE1 . HIS   B 2 38  ? -27.835 -1.657  -12.202 1.00 26.38  ? 47  HIS   B CE1 1 
ATOM   702  N NE2 . HIS   B 2 38  ? -27.277 -2.314  -11.195 1.00 30.24  ? 47  HIS   B NE2 1 
ATOM   703  N N   . THR   B 2 39  ? -22.310 2.240   -11.313 1.00 29.05  ? 48  THR   B N   1 
ATOM   704  C CA  . THR   B 2 39  ? -21.075 2.867   -11.821 1.00 31.75  ? 48  THR   B CA  1 
ATOM   705  C C   . THR   B 2 39  ? -19.879 2.306   -11.049 1.00 34.99  ? 48  THR   B C   1 
ATOM   706  O O   . THR   B 2 39  ? -20.059 1.337   -10.261 1.00 34.78  ? 48  THR   B O   1 
ATOM   707  C CB  . THR   B 2 39  ? -21.257 4.377   -11.826 1.00 30.32  ? 48  THR   B CB  1 
ATOM   708  O OG1 . THR   B 2 39  ? -20.294 4.922   -12.721 1.00 30.39  ? 48  THR   B OG1 1 
ATOM   709  C CG2 . THR   B 2 39  ? -21.159 4.954   -10.437 1.00 30.82  ? 48  THR   B CG2 1 
ATOM   710  N N   . MET   B 2 40  ? -18.707 2.877   -11.290 1.00 37.75  ? 49  MET   B N   1 
ATOM   711  C CA  . MET   B 2 40  ? -17.479 2.506   -10.555 1.00 37.90  ? 49  MET   B CA  1 
ATOM   712  C C   . MET   B 2 40  ? -17.246 3.517   -9.434  1.00 39.73  ? 49  MET   B C   1 
ATOM   713  O O   . MET   B 2 40  ? -17.414 4.719   -9.662  1.00 36.22  ? 49  MET   B O   1 
ATOM   714  C CB  . MET   B 2 40  ? -16.304 2.470   -11.528 1.00 38.49  ? 49  MET   B CB  1 
ATOM   715  C CG  . MET   B 2 40  ? -16.590 1.578   -12.725 1.00 38.29  ? 49  MET   B CG  1 
ATOM   716  S SD  . MET   B 2 40  ? -15.104 0.830   -13.412 1.00 41.41  ? 49  MET   B SD  1 
ATOM   717  C CE  . MET   B 2 40  ? -14.733 -0.459  -12.233 1.00 41.10  ? 49  MET   B CE  1 
ATOM   718  N N   A TRP   B 2 41  ? -16.846 3.022   -8.258  0.25 39.51  ? 50  TRP   B N   1 
ATOM   719  N N   B TRP   B 2 41  ? -16.858 3.028   -8.251  0.25 40.35  ? 50  TRP   B N   1 
ATOM   720  N N   C TRP   B 2 41  ? -16.846 3.022   -8.258  0.25 39.51  ? 50  TRP   B N   1 
ATOM   721  N N   D TRP   B 2 41  ? -16.858 3.028   -8.251  0.25 40.35  ? 50  TRP   B N   1 
ATOM   722  C CA  A TRP   B 2 41  ? -16.720 3.800   -6.996  0.25 39.87  ? 50  TRP   B CA  1 
ATOM   723  C CA  B TRP   B 2 41  ? -16.739 3.828   -7.002  0.25 41.25  ? 50  TRP   B CA  1 
ATOM   724  C CA  C TRP   B 2 41  ? -16.720 3.800   -6.996  0.25 39.87  ? 50  TRP   B CA  1 
ATOM   725  C CA  D TRP   B 2 41  ? -16.739 3.828   -7.002  0.25 41.25  ? 50  TRP   B CA  1 
ATOM   726  C C   A TRP   B 2 41  ? -15.801 5.013   -7.201  0.25 41.93  ? 50  TRP   B C   1 
ATOM   727  C C   B TRP   B 2 41  ? -15.811 5.031   -7.221  0.25 42.74  ? 50  TRP   B C   1 
ATOM   728  C C   C TRP   B 2 41  ? -15.801 5.013   -7.201  0.25 41.93  ? 50  TRP   B C   1 
ATOM   729  C C   D TRP   B 2 41  ? -15.811 5.031   -7.221  0.25 42.74  ? 50  TRP   B C   1 
ATOM   730  O O   A TRP   B 2 41  ? -16.143 6.093   -6.690  0.25 42.71  ? 50  TRP   B O   1 
ATOM   731  O O   B TRP   B 2 41  ? -16.157 6.123   -6.740  0.25 43.61  ? 50  TRP   B O   1 
ATOM   732  O O   C TRP   B 2 41  ? -16.143 6.093   -6.690  0.25 42.71  ? 50  TRP   B O   1 
ATOM   733  O O   D TRP   B 2 41  ? -16.157 6.123   -6.740  0.25 43.61  ? 50  TRP   B O   1 
ATOM   734  C CB  A TRP   B 2 41  ? -16.228 2.903   -5.850  0.25 39.24  ? 50  TRP   B CB  1 
ATOM   735  C CB  B TRP   B 2 41  ? -16.263 2.967   -5.822  0.25 41.66  ? 50  TRP   B CB  1 
ATOM   736  C CB  C TRP   B 2 41  ? -16.228 2.903   -5.850  0.25 39.24  ? 50  TRP   B CB  1 
ATOM   737  C CB  D TRP   B 2 41  ? -16.263 2.967   -5.822  0.25 41.66  ? 50  TRP   B CB  1 
ATOM   738  C CG  A TRP   B 2 41  ? -16.344 3.554   -4.507  0.25 38.91  ? 50  TRP   B CG  1 
ATOM   739  C CG  B TRP   B 2 41  ? -16.123 3.758   -4.557  0.25 42.39  ? 50  TRP   B CG  1 
ATOM   740  C CG  C TRP   B 2 41  ? -16.344 3.554   -4.507  0.25 38.91  ? 50  TRP   B CG  1 
ATOM   741  C CG  D TRP   B 2 41  ? -16.123 3.758   -4.557  0.25 42.39  ? 50  TRP   B CG  1 
ATOM   742  C CD1 A TRP   B 2 41  ? -17.345 3.388   -3.594  0.25 39.60  ? 50  TRP   B CD1 1 
ATOM   743  C CD1 B TRP   B 2 41  ? -15.083 4.574   -4.212  0.25 42.47  ? 50  TRP   B CD1 1 
ATOM   744  C CD1 C TRP   B 2 41  ? -17.345 3.388   -3.594  0.25 39.60  ? 50  TRP   B CD1 1 
ATOM   745  C CD1 D TRP   B 2 41  ? -15.083 4.574   -4.212  0.25 42.47  ? 50  TRP   B CD1 1 
ATOM   746  C CD2 A TRP   B 2 41  ? -15.437 4.515   -3.936  0.25 38.75  ? 50  TRP   B CD2 1 
ATOM   747  C CD2 B TRP   B 2 41  ? -17.078 3.852   -3.485  0.25 43.51  ? 50  TRP   B CD2 1 
ATOM   748  C CD2 C TRP   B 2 41  ? -15.437 4.515   -3.936  0.25 38.75  ? 50  TRP   B CD2 1 
ATOM   749  C CD2 D TRP   B 2 41  ? -17.078 3.852   -3.485  0.25 43.51  ? 50  TRP   B CD2 1 
ATOM   750  N NE1 A TRP   B 2 41  ? -17.115 4.164   -2.490  0.25 39.85  ? 50  TRP   B NE1 1 
ATOM   751  N NE1 B TRP   B 2 41  ? -15.315 5.152   -2.993  0.25 43.07  ? 50  TRP   B NE1 1 
ATOM   752  N NE1 C TRP   B 2 41  ? -17.115 4.164   -2.490  0.25 39.85  ? 50  TRP   B NE1 1 
ATOM   753  N NE1 D TRP   B 2 41  ? -15.315 5.152   -2.993  0.25 43.07  ? 50  TRP   B NE1 1 
ATOM   754  C CE2 A TRP   B 2 41  ? -15.953 4.869   -2.672  0.25 39.33  ? 50  TRP   B CE2 1 
ATOM   755  C CE2 B TRP   B 2 41  ? -16.532 4.730   -2.524  0.25 43.72  ? 50  TRP   B CE2 1 
ATOM   756  C CE2 C TRP   B 2 41  ? -15.953 4.869   -2.672  0.25 39.33  ? 50  TRP   B CE2 1 
ATOM   757  C CE2 D TRP   B 2 41  ? -16.532 4.730   -2.524  0.25 43.72  ? 50  TRP   B CE2 1 
ATOM   758  C CE3 A TRP   B 2 41  ? -14.242 5.103   -4.364  0.25 37.74  ? 50  TRP   B CE3 1 
ATOM   759  C CE3 B TRP   B 2 41  ? -18.331 3.279   -3.237  0.25 43.60  ? 50  TRP   B CE3 1 
ATOM   760  C CE3 C TRP   B 2 41  ? -14.242 5.103   -4.364  0.25 37.74  ? 50  TRP   B CE3 1 
ATOM   761  C CE3 D TRP   B 2 41  ? -18.331 3.279   -3.237  0.25 43.60  ? 50  TRP   B CE3 1 
ATOM   762  C CZ2 A TRP   B 2 41  ? -15.312 5.782   -1.836  0.25 39.05  ? 50  TRP   B CZ2 1 
ATOM   763  C CZ2 B TRP   B 2 41  ? -17.198 5.041   -1.340  0.25 43.78  ? 50  TRP   B CZ2 1 
ATOM   764  C CZ2 C TRP   B 2 41  ? -15.312 5.782   -1.836  0.25 39.05  ? 50  TRP   B CZ2 1 
ATOM   765  C CZ2 D TRP   B 2 41  ? -17.198 5.041   -1.340  0.25 43.78  ? 50  TRP   B CZ2 1 
ATOM   766  C CZ3 A TRP   B 2 41  ? -13.608 6.000   -3.534  0.25 38.27  ? 50  TRP   B CZ3 1 
ATOM   767  C CZ3 B TRP   B 2 41  ? -18.985 3.585   -2.063  0.25 44.31  ? 50  TRP   B CZ3 1 
ATOM   768  C CZ3 C TRP   B 2 41  ? -13.608 6.000   -3.534  0.25 38.27  ? 50  TRP   B CZ3 1 
ATOM   769  C CZ3 D TRP   B 2 41  ? -18.985 3.585   -2.063  0.25 44.31  ? 50  TRP   B CZ3 1 
ATOM   770  C CH2 A TRP   B 2 41  ? -14.138 6.335   -2.288  0.25 38.02  ? 50  TRP   B CH2 1 
ATOM   771  C CH2 B TRP   B 2 41  ? -18.424 4.453   -1.127  0.25 43.69  ? 50  TRP   B CH2 1 
ATOM   772  C CH2 C TRP   B 2 41  ? -14.138 6.335   -2.288  0.25 38.02  ? 50  TRP   B CH2 1 
ATOM   773  C CH2 D TRP   B 2 41  ? -18.424 4.453   -1.127  0.25 43.69  ? 50  TRP   B CH2 1 
ATOM   774  N N   . HIS   B 2 42  ? -14.682 4.842   -7.914  1.00 41.92  ? 51  HIS   B N   1 
ATOM   775  C CA  . HIS   B 2 42  ? -13.680 5.932   -8.142  1.00 42.66  ? 51  HIS   B CA  1 
ATOM   776  C C   . HIS   B 2 42  ? -14.264 7.094   -8.983  1.00 43.08  ? 51  HIS   B C   1 
ATOM   777  O O   . HIS   B 2 42  ? -13.664 8.177   -8.978  1.00 41.34  ? 51  HIS   B O   1 
ATOM   778  C CB  . HIS   B 2 42  ? -12.369 5.373   -8.715  1.00 38.29  ? 51  HIS   B CB  1 
ATOM   779  C CG  . HIS   B 2 42  ? -12.384 5.091   -10.176 1.00 37.99  ? 51  HIS   B CG  1 
ATOM   780  N ND1 . HIS   B 2 42  ? -12.606 3.832   -10.683 1.00 41.60  ? 51  HIS   B ND1 1 
ATOM   781  C CD2 . HIS   B 2 42  ? -12.150 5.880   -11.243 1.00 40.33  ? 51  HIS   B CD2 1 
ATOM   782  C CE1 . HIS   B 2 42  ? -12.553 3.870   -12.001 1.00 40.38  ? 51  HIS   B CE1 1 
ATOM   783  N NE2 . HIS   B 2 42  ? -12.296 5.118   -12.369 1.00 38.91  ? 51  HIS   B NE2 1 
ATOM   784  N N   . VAL   B 2 43  ? -15.373 6.893   -9.693  1.00 38.88  ? 52  VAL   B N   1 
ATOM   785  C CA  . VAL   B 2 43  ? -16.022 7.964   -10.498 1.00 45.83  ? 52  VAL   B CA  1 
ATOM   786  C C   . VAL   B 2 43  ? -16.734 8.934   -9.543  1.00 45.08  ? 52  VAL   B C   1 
ATOM   787  O O   . VAL   B 2 43  ? -16.349 10.125  -9.524  1.00 47.42  ? 52  VAL   B O   1 
ATOM   788  C CB  . VAL   B 2 43  ? -16.963 7.346   -11.548 1.00 45.30  ? 52  VAL   B CB  1 
ATOM   789  C CG1 . VAL   B 2 43  ? -17.815 8.380   -12.271 1.00 46.75  ? 52  VAL   B CG1 1 
ATOM   790  C CG2 . VAL   B 2 43  ? -16.167 6.517   -12.533 1.00 44.61  ? 52  VAL   B CG2 1 
ATOM   791  N N   . THR   B 2 44  ? -17.662 8.423   -8.727  1.00 43.29  ? 53  THR   B N   1 
ATOM   792  C CA  . THR   B 2 44  ? -18.573 9.228   -7.862  1.00 40.90  ? 53  THR   B CA  1 
ATOM   793  C C   . THR   B 2 44  ? -17.971 9.426   -6.474  1.00 42.70  ? 53  THR   B C   1 
ATOM   794  O O   . THR   B 2 44  ? -18.324 10.429  -5.848  1.00 43.69  ? 53  THR   B O   1 
ATOM   795  C CB  . THR   B 2 44  ? -19.953 8.578   -7.758  1.00 39.83  ? 53  THR   B CB  1 
ATOM   796  O OG1 . THR   B 2 44  ? -19.846 7.440   -6.906  1.00 43.19  ? 53  THR   B OG1 1 
ATOM   797  C CG2 . THR   B 2 44  ? -20.489 8.154   -9.108  1.00 42.61  ? 53  THR   B CG2 1 
ATOM   798  N N   . LYS   B 2 45  ? -17.080 8.530   -6.041  1.00 45.04  ? 54  LYS   B N   1 
ATOM   799  C CA  . LYS   B 2 45  ? -16.494 8.494   -4.675  1.00 49.24  ? 54  LYS   B CA  1 
ATOM   800  C C   . LYS   B 2 45  ? -17.597 8.131   -3.671  1.00 46.02  ? 54  LYS   B C   1 
ATOM   801  O O   . LYS   B 2 45  ? -17.412 8.413   -2.479  1.00 44.62  ? 54  LYS   B O   1 
ATOM   802  C CB  . LYS   B 2 45  ? -15.822 9.825   -4.323  1.00 50.38  ? 54  LYS   B CB  1 
ATOM   803  C CG  . LYS   B 2 45  ? -14.484 10.052  -5.000  1.00 58.05  ? 54  LYS   B CG  1 
ATOM   804  C CD  . LYS   B 2 45  ? -13.384 9.192   -4.413  1.00 61.19  ? 54  LYS   B CD  1 
ATOM   805  C CE  . LYS   B 2 45  ? -11.984 9.664   -4.749  1.00 63.52  ? 54  LYS   B CE  1 
ATOM   806  N NZ  . LYS   B 2 45  ? -11.743 9.603   -6.214  1.00 67.81  ? 54  LYS   B NZ  1 
ATOM   807  N N   . GLY   B 2 46  ? -18.686 7.508   -4.137  1.00 47.29  ? 55  GLY   B N   1 
ATOM   808  C CA  . GLY   B 2 46  ? -19.880 7.179   -3.330  1.00 44.65  ? 55  GLY   B CA  1 
ATOM   809  C C   . GLY   B 2 46  ? -20.777 8.382   -3.081  1.00 45.41  ? 55  GLY   B C   1 
ATOM   810  O O   . GLY   B 2 46  ? -21.717 8.239   -2.296  1.00 47.80  ? 55  GLY   B O   1 
ATOM   811  N N   . ALA   B 2 47  ? -20.513 9.518   -3.738  1.00 46.10  ? 56  ALA   B N   1 
ATOM   812  C CA  . ALA   B 2 47  ? -21.299 10.774  -3.646  1.00 45.30  ? 56  ALA   B CA  1 
ATOM   813  C C   . ALA   B 2 47  ? -22.670 10.587  -4.309  1.00 46.69  ? 56  ALA   B C   1 
ATOM   814  O O   . ALA   B 2 47  ? -22.778 9.725   -5.204  1.00 50.01  ? 56  ALA   B O   1 
ATOM   815  C CB  . ALA   B 2 47  ? -20.543 11.916  -4.290  1.00 42.76  ? 56  ALA   B CB  1 
ATOM   816  N N   . ALA   B 2 48  ? -23.660 11.401  -3.918  1.00 46.21  ? 57  ALA   B N   1 
ATOM   817  C CA  . ALA   B 2 48  ? -25.019 11.410  -4.496  1.00 45.86  ? 57  ALA   B CA  1 
ATOM   818  C C   . ALA   B 2 48  ? -24.932 12.024  -5.891  1.00 48.36  ? 57  ALA   B C   1 
ATOM   819  O O   . ALA   B 2 48  ? -23.988 12.800  -6.107  1.00 48.06  ? 57  ALA   B O   1 
ATOM   820  C CB  . ALA   B 2 48  ? -25.977 12.175  -3.619  1.00 47.50  ? 57  ALA   B CB  1 
ATOM   821  N N   . LEU   B 2 49  ? -25.898 11.698  -6.763  1.00 48.42  ? 58  LEU   B N   1 
ATOM   822  C CA  . LEU   B 2 49  ? -26.001 12.190  -8.166  1.00 49.96  ? 58  LEU   B CA  1 
ATOM   823  C C   . LEU   B 2 49  ? -27.340 12.906  -8.374  1.00 51.64  ? 58  LEU   B C   1 
ATOM   824  O O   . LEU   B 2 49  ? -28.270 12.668  -7.588  1.00 51.11  ? 58  LEU   B O   1 
ATOM   825  C CB  . LEU   B 2 49  ? -25.893 11.008  -9.130  1.00 46.13  ? 58  LEU   B CB  1 
ATOM   826  C CG  . LEU   B 2 49  ? -24.676 10.099  -8.948  1.00 42.82  ? 58  LEU   B CG  1 
ATOM   827  C CD1 . LEU   B 2 49  ? -24.843 8.848   -9.783  1.00 38.13  ? 58  LEU   B CD1 1 
ATOM   828  C CD2 . LEU   B 2 49  ? -23.375 10.815  -9.300  1.00 44.90  ? 58  LEU   B CD2 1 
ATOM   829  N N   . ARG   B 2 50  ? -27.417 13.750  -9.404  1.00 52.13  ? 59  ARG   B N   1 
ATOM   830  C CA  . ARG   B 2 50  ? -28.661 14.425  -9.850  1.00 55.42  ? 59  ARG   B CA  1 
ATOM   831  C C   . ARG   B 2 50  ? -29.040 13.891  -11.237 1.00 52.76  ? 59  ARG   B C   1 
ATOM   832  O O   . ARG   B 2 50  ? -28.144 13.466  -11.990 1.00 50.62  ? 59  ARG   B O   1 
ATOM   833  C CB  . ARG   B 2 50  ? -28.477 15.945  -9.816  1.00 61.67  ? 59  ARG   B CB  1 
ATOM   834  C CG  . ARG   B 2 50  ? -29.638 16.735  -10.407 1.00 66.34  ? 59  ARG   B CG  1 
ATOM   835  C CD  . ARG   B 2 50  ? -29.510 18.218  -10.122 1.00 69.34  ? 59  ARG   B CD  1 
ATOM   836  N NE  . ARG   B 2 50  ? -28.132 18.683  -10.277 1.00 66.85  ? 59  ARG   B NE  1 
ATOM   837  C CZ  . ARG   B 2 50  ? -27.587 19.146  -11.406 1.00 70.27  ? 59  ARG   B CZ  1 
ATOM   838  N NH1 . ARG   B 2 50  ? -28.288 19.218  -12.530 1.00 64.93  ? 59  ARG   B NH1 1 
ATOM   839  N NH2 . ARG   B 2 50  ? -26.324 19.548  -11.402 1.00 74.72  ? 59  ARG   B NH2 1 
ATOM   840  N N   . SER   B 2 51  ? -30.342 13.857  -11.506 1.00 52.26  ? 60  SER   B N   1 
ATOM   841  C CA  . SER   B 2 51  ? -30.976 13.506  -12.799 1.00 55.24  ? 60  SER   B CA  1 
ATOM   842  C C   . SER   B 2 51  ? -32.225 14.389  -12.972 1.00 59.69  ? 60  SER   B C   1 
ATOM   843  O O   . SER   B 2 51  ? -33.206 14.192  -12.234 1.00 67.15  ? 60  SER   B O   1 
ATOM   844  C CB  . SER   B 2 51  ? -31.310 12.039  -12.822 1.00 51.73  ? 60  SER   B CB  1 
ATOM   845  O OG  . SER   B 2 51  ? -31.848 11.661  -14.076 1.00 50.70  ? 60  SER   B OG  1 
ATOM   846  N N   . GLY   B 2 52  ? -32.186 15.360  -13.882 1.00 64.94  ? 61  GLY   B N   1 
ATOM   847  C CA  . GLY   B 2 52  ? -33.177 16.451  -13.914 1.00 70.40  ? 61  GLY   B CA  1 
ATOM   848  C C   . GLY   B 2 52  ? -33.086 17.239  -12.625 1.00 70.68  ? 61  GLY   B C   1 
ATOM   849  O O   . GLY   B 2 52  ? -32.004 17.800  -12.349 1.00 77.72  ? 61  GLY   B O   1 
ATOM   850  N N   . GLU   B 2 53  ? -34.148 17.232  -11.827 1.00 69.65  ? 62  GLU   B N   1 
ATOM   851  C CA  . GLU   B 2 53  ? -34.109 17.767  -10.444 1.00 73.28  ? 62  GLU   B CA  1 
ATOM   852  C C   . GLU   B 2 53  ? -34.317 16.622  -9.452  1.00 67.84  ? 62  GLU   B C   1 
ATOM   853  O O   . GLU   B 2 53  ? -34.486 16.910  -8.254  1.00 69.39  ? 62  GLU   B O   1 
ATOM   854  C CB  . GLU   B 2 53  ? -35.125 18.894  -10.302 1.00 80.25  ? 62  GLU   B CB  1 
ATOM   855  C CG  . GLU   B 2 53  ? -34.554 20.237  -10.710 1.00 89.24  ? 62  GLU   B CG  1 
ATOM   856  C CD  . GLU   B 2 53  ? -35.509 21.390  -10.478 1.00 97.85  ? 62  GLU   B CD  1 
ATOM   857  O OE1 . GLU   B 2 53  ? -36.706 21.214  -10.794 1.00 102.90 ? 62  GLU   B OE1 1 
ATOM   858  O OE2 . GLU   B 2 53  ? -35.062 22.448  -9.961  1.00 99.39  ? 62  GLU   B OE2 1 
ATOM   859  N N   . GLY   B 2 54  ? -34.251 15.379  -9.934  1.00 63.52  ? 63  GLY   B N   1 
ATOM   860  C CA  . GLY   B 2 54  ? -34.259 14.161  -9.102  1.00 67.44  ? 63  GLY   B CA  1 
ATOM   861  C C   . GLY   B 2 54  ? -32.888 13.876  -8.513  1.00 61.85  ? 63  GLY   B C   1 
ATOM   862  O O   . GLY   B 2 54  ? -31.893 14.364  -9.065  1.00 60.18  ? 63  GLY   B O   1 
ATOM   863  N N   . ARG   B 2 55  ? -32.843 13.092  -7.438  1.00 54.56  ? 64  ARG   B N   1 
ATOM   864  C CA  . ARG   B 2 55  ? -31.604 12.747  -6.703  1.00 55.90  ? 64  ARG   B CA  1 
ATOM   865  C C   . ARG   B 2 55  ? -31.470 11.221  -6.602  1.00 53.92  ? 64  ARG   B C   1 
ATOM   866  O O   . ARG   B 2 55  ? -32.441 10.550  -6.205  1.00 49.57  ? 64  ARG   B O   1 
ATOM   867  C CB  . ARG   B 2 55  ? -31.648 13.395  -5.320  1.00 60.14  ? 64  ARG   B CB  1 
ATOM   868  C CG  . ARG   B 2 55  ? -30.360 13.281  -4.520  1.00 65.85  ? 64  ARG   B CG  1 
ATOM   869  C CD  . ARG   B 2 55  ? -30.605 13.873  -3.144  1.00 76.94  ? 64  ARG   B CD  1 
ATOM   870  N NE  . ARG   B 2 55  ? -29.797 13.262  -2.094  1.00 80.86  ? 64  ARG   B NE  1 
ATOM   871  C CZ  . ARG   B 2 55  ? -28.935 13.899  -1.296  1.00 80.55  ? 64  ARG   B CZ  1 
ATOM   872  N NH1 . ARG   B 2 55  ? -28.733 15.205  -1.409  1.00 75.19  ? 64  ARG   B NH1 1 
ATOM   873  N NH2 . ARG   B 2 55  ? -28.279 13.212  -0.372  1.00 78.83  ? 64  ARG   B NH2 1 
ATOM   874  N N   . LEU   B 2 56  ? -30.303 10.691  -6.966  1.00 47.32  ? 65  LEU   B N   1 
ATOM   875  C CA  . LEU   B 2 56  ? -29.952 9.270   -6.752  1.00 43.41  ? 65  LEU   B CA  1 
ATOM   876  C C   . LEU   B 2 56  ? -29.026 9.225   -5.539  1.00 42.91  ? 65  LEU   B C   1 
ATOM   877  O O   . LEU   B 2 56  ? -27.941 9.894   -5.545  1.00 43.87  ? 65  LEU   B O   1 
ATOM   878  C CB  . LEU   B 2 56  ? -29.273 8.651   -7.979  1.00 43.97  ? 65  LEU   B CB  1 
ATOM   879  C CG  . LEU   B 2 56  ? -29.564 9.239   -9.358  1.00 47.89  ? 65  LEU   B CG  1 
ATOM   880  C CD1 . LEU   B 2 56  ? -29.155 8.242   -10.430 1.00 49.34  ? 65  LEU   B CD1 1 
ATOM   881  C CD2 . LEU   B 2 56  ? -31.018 9.615   -9.542  1.00 50.97  ? 65  LEU   B CD2 1 
ATOM   882  N N   . ASP   B 2 57  ? -29.437 8.482   -4.526  1.00 40.38  ? 66  ASP   B N   1 
ATOM   883  C CA  . ASP   B 2 57  ? -28.622 8.280   -3.313  1.00 42.49  ? 66  ASP   B CA  1 
ATOM   884  C C   . ASP   B 2 57  ? -27.912 6.942   -3.434  1.00 43.07  ? 66  ASP   B C   1 
ATOM   885  O O   . ASP   B 2 57  ? -28.522 5.969   -3.886  1.00 42.55  ? 66  ASP   B O   1 
ATOM   886  C CB  . ASP   B 2 57  ? -29.519 8.369   -2.087  1.00 48.93  ? 66  ASP   B CB  1 
ATOM   887  C CG  . ASP   B 2 57  ? -29.948 9.805   -1.871  1.00 52.49  ? 66  ASP   B CG  1 
ATOM   888  O OD1 . ASP   B 2 57  ? -29.061 10.630  -1.589  1.00 60.50  ? 66  ASP   B OD1 1 
ATOM   889  O OD2 . ASP   B 2 57  ? -31.133 10.102  -2.079  1.00 53.41  ? 66  ASP   B OD2 1 
ATOM   890  N N   . PRO   B 2 58  ? -26.634 6.836   -2.994  1.00 42.88  ? 67  PRO   B N   1 
ATOM   891  C CA  . PRO   B 2 58  ? -25.954 5.544   -2.974  1.00 45.04  ? 67  PRO   B CA  1 
ATOM   892  C C   . PRO   B 2 58  ? -26.787 4.578   -2.112  1.00 48.13  ? 67  PRO   B C   1 
ATOM   893  O O   . PRO   B 2 58  ? -27.471 5.036   -1.180  1.00 51.58  ? 67  PRO   B O   1 
ATOM   894  C CB  . PRO   B 2 58  ? -24.567 5.850   -2.399  1.00 42.54  ? 67  PRO   B CB  1 
ATOM   895  C CG  . PRO   B 2 58  ? -24.779 7.131   -1.623  1.00 42.10  ? 67  PRO   B CG  1 
ATOM   896  C CD  . PRO   B 2 58  ? -25.807 7.906   -2.418  1.00 41.43  ? 67  PRO   B CD  1 
ATOM   897  N N   . TYR   B 2 59  ? -26.780 3.300   -2.493  1.00 40.16  ? 68  TYR   B N   1 
ATOM   898  C CA  . TYR   B 2 59  ? -27.430 2.173   -1.778  1.00 39.95  ? 68  TYR   B CA  1 
ATOM   899  C C   . TYR   B 2 59  ? -26.347 1.166   -1.353  1.00 39.74  ? 68  TYR   B C   1 
ATOM   900  O O   . TYR   B 2 59  ? -26.333 0.765   -0.187  1.00 40.98  ? 68  TYR   B O   1 
ATOM   901  C CB  . TYR   B 2 59  ? -28.517 1.569   -2.666  1.00 37.21  ? 68  TYR   B CB  1 
ATOM   902  C CG  . TYR   B 2 59  ? -29.294 0.416   -2.079  1.00 37.15  ? 68  TYR   B CG  1 
ATOM   903  C CD1 . TYR   B 2 59  ? -28.730 -0.846  -2.032  1.00 38.87  ? 68  TYR   B CD1 1 
ATOM   904  C CD2 . TYR   B 2 59  ? -30.603 0.549   -1.646  1.00 37.63  ? 68  TYR   B CD2 1 
ATOM   905  C CE1 . TYR   B 2 59  ? -29.433 -1.934  -1.544  1.00 42.23  ? 68  TYR   B CE1 1 
ATOM   906  C CE2 . TYR   B 2 59  ? -31.325 -0.533  -1.154  1.00 40.74  ? 68  TYR   B CE2 1 
ATOM   907  C CZ  . TYR   B 2 59  ? -30.730 -1.788  -1.086  1.00 43.44  ? 68  TYR   B CZ  1 
ATOM   908  O OH  . TYR   B 2 59  ? -31.354 -2.918  -0.606  1.00 44.76  ? 68  TYR   B OH  1 
ATOM   909  N N   . TRP   B 2 60  ? -25.450 0.781   -2.263  1.00 39.31  ? 69  TRP   B N   1 
ATOM   910  C CA  . TRP   B 2 60  ? -24.348 -0.192  -2.005  1.00 34.75  ? 69  TRP   B CA  1 
ATOM   911  C C   . TRP   B 2 60  ? -23.072 0.351   -2.620  1.00 34.40  ? 69  TRP   B C   1 
ATOM   912  O O   . TRP   B 2 60  ? -23.165 0.992   -3.672  1.00 35.08  ? 69  TRP   B O   1 
ATOM   913  C CB  . TRP   B 2 60  ? -24.622 -1.578  -2.598  1.00 31.19  ? 69  TRP   B CB  1 
ATOM   914  C CG  . TRP   B 2 60  ? -23.426 -2.495  -2.543  1.00 32.51  ? 69  TRP   B CG  1 
ATOM   915  C CD1 . TRP   B 2 60  ? -22.951 -3.159  -1.448  1.00 33.24  ? 69  TRP   B CD1 1 
ATOM   916  C CD2 . TRP   B 2 60  ? -22.520 -2.838  -3.615  1.00 29.10  ? 69  TRP   B CD2 1 
ATOM   917  N NE1 . TRP   B 2 60  ? -21.824 -3.882  -1.753  1.00 30.73  ? 69  TRP   B NE1 1 
ATOM   918  C CE2 . TRP   B 2 60  ? -21.556 -3.728  -3.083  1.00 28.20  ? 69  TRP   B CE2 1 
ATOM   919  C CE3 . TRP   B 2 60  ? -22.456 -2.512  -4.973  1.00 28.17  ? 69  TRP   B CE3 1 
ATOM   920  C CZ2 . TRP   B 2 60  ? -20.550 -4.285  -3.855  1.00 25.26  ? 69  TRP   B CZ2 1 
ATOM   921  C CZ3 . TRP   B 2 60  ? -21.481 -3.089  -5.751  1.00 28.27  ? 69  TRP   B CZ3 1 
ATOM   922  C CH2 . TRP   B 2 60  ? -20.539 -3.966  -5.199  1.00 28.66  ? 69  TRP   B CH2 1 
ATOM   923  N N   . GLY   B 2 61  ? -21.930 -0.042  -2.073  1.00 37.34  ? 70  GLY   B N   1 
ATOM   924  C CA  . GLY   B 2 61  ? -20.638 0.189   -2.738  1.00 40.58  ? 70  GLY   B CA  1 
ATOM   925  C C   . GLY   B 2 61  ? -19.514 -0.462  -1.994  1.00 37.83  ? 70  GLY   B C   1 
ATOM   926  O O   . GLY   B 2 61  ? -19.695 -0.759  -0.806  1.00 39.31  ? 70  GLY   B O   1 
ATOM   927  N N   . ASP   B 2 62  ? -18.380 -0.617  -2.658  1.00 36.81  ? 71  ASP   B N   1 
ATOM   928  C CA  . ASP   B 2 62  ? -17.218 -1.372  -2.124  1.00 37.38  ? 71  ASP   B CA  1 
ATOM   929  C C   . ASP   B 2 62  ? -15.974 -0.942  -2.896  1.00 37.91  ? 71  ASP   B C   1 
ATOM   930  O O   . ASP   B 2 62  ? -15.915 -1.195  -4.111  1.00 41.95  ? 71  ASP   B O   1 
ATOM   931  C CB  . ASP   B 2 62  ? -17.453 -2.872  -2.208  1.00 36.02  ? 71  ASP   B CB  1 
ATOM   932  C CG  . ASP   B 2 62  ? -16.230 -3.664  -1.821  1.00 39.77  ? 71  ASP   B CG  1 
ATOM   933  O OD1 . ASP   B 2 62  ? -15.615 -4.225  -2.709  1.00 51.49  ? 71  ASP   B OD1 1 
ATOM   934  O OD2 . ASP   B 2 62  ? -15.888 -3.673  -0.642  1.00 50.92  ? 71  ASP   B OD2 1 
ATOM   935  N N   . VAL   B 2 63  ? -15.061 -0.263  -2.210  1.00 37.28  ? 72  VAL   B N   1 
ATOM   936  C CA  . VAL   B 2 63  ? -13.849 0.351   -2.805  1.00 38.63  ? 72  VAL   B CA  1 
ATOM   937  C C   . VAL   B 2 63  ? -12.984 -0.734  -3.464  1.00 44.28  ? 72  VAL   B C   1 
ATOM   938  O O   . VAL   B 2 63  ? -12.405 -0.436  -4.522  1.00 49.57  ? 72  VAL   B O   1 
ATOM   939  C CB  . VAL   B 2 63  ? -13.072 1.134   -1.736  1.00 39.45  ? 72  VAL   B CB  1 
ATOM   940  C CG1 . VAL   B 2 63  ? -11.574 1.149   -1.992  1.00 38.27  ? 72  VAL   B CG1 1 
ATOM   941  C CG2 . VAL   B 2 63  ? -13.622 2.548   -1.603  1.00 42.49  ? 72  VAL   B CG2 1 
ATOM   942  N N   . LYS   B 2 64  ? -12.893 -1.944  -2.896  1.00 44.11  ? 73  LYS   B N   1 
ATOM   943  C CA  . LYS   B 2 64  ? -11.954 -2.970  -3.417  1.00 43.95  ? 73  LYS   B CA  1 
ATOM   944  C C   . LYS   B 2 64  ? -12.450 -3.502  -4.769  1.00 46.77  ? 73  LYS   B C   1 
ATOM   945  O O   . LYS   B 2 64  ? -11.616 -3.620  -5.684  1.00 49.56  ? 73  LYS   B O   1 
ATOM   946  C CB  . LYS   B 2 64  ? -11.747 -4.123  -2.443  1.00 39.42  ? 73  LYS   B CB  1 
ATOM   947  C CG  . LYS   B 2 64  ? -10.655 -5.083  -2.899  1.00 39.85  ? 73  LYS   B CG  1 
ATOM   948  C CD  . LYS   B 2 64  ? -10.375 -6.170  -1.908  1.00 39.88  ? 73  LYS   B CD  1 
ATOM   949  C CE  . LYS   B 2 64  ? -9.278  -7.105  -2.361  1.00 42.77  ? 73  LYS   B CE  1 
ATOM   950  N NZ  . LYS   B 2 64  ? -8.788  -7.888  -1.210  1.00 42.30  ? 73  LYS   B NZ  1 
ATOM   951  N N   . GLN   B 2 65  ? -13.734 -3.872  -4.852  1.00 45.86  ? 74  GLN   B N   1 
ATOM   952  C CA  . GLN   B 2 65  ? -14.447 -4.265  -6.095  1.00 44.86  ? 74  GLN   B CA  1 
ATOM   953  C C   . GLN   B 2 65  ? -14.490 -3.100  -7.084  1.00 40.11  ? 74  GLN   B C   1 
ATOM   954  O O   . GLN   B 2 65  ? -14.659 -3.358  -8.304  1.00 36.03  ? 74  GLN   B O   1 
ATOM   955  C CB  . GLN   B 2 65  ? -15.888 -4.649  -5.780  1.00 45.85  ? 74  GLN   B CB  1 
ATOM   956  C CG  . GLN   B 2 65  ? -16.012 -6.079  -5.295  1.00 47.16  ? 74  GLN   B CG  1 
ATOM   957  C CD  . GLN   B 2 65  ? -17.463 -6.427  -5.095  1.00 43.31  ? 74  GLN   B CD  1 
ATOM   958  O OE1 . GLN   B 2 65  ? -18.209 -6.679  -6.052  1.00 41.88  ? 74  GLN   B OE1 1 
ATOM   959  N NE2 . GLN   B 2 65  ? -17.863 -6.420  -3.838  1.00 35.97  ? 74  GLN   B NE2 1 
ATOM   960  N N   . ASP   B 2 66  ? -14.366 -1.893  -6.524  1.00 43.67  ? 75  ASP   B N   1 
ATOM   961  C CA  . ASP   B 2 66  ? -14.429 -0.545  -7.151  1.00 42.30  ? 75  ASP   B CA  1 
ATOM   962  C C   . ASP   B 2 66  ? -15.784 -0.362  -7.829  1.00 40.71  ? 75  ASP   B C   1 
ATOM   963  O O   . ASP   B 2 66  ? -15.767 0.174   -8.945  1.00 35.87  ? 75  ASP   B O   1 
ATOM   964  C CB  . ASP   B 2 66  ? -13.296 -0.316  -8.151  1.00 44.27  ? 75  ASP   B CB  1 
ATOM   965  C CG  . ASP   B 2 66  ? -13.358 1.062   -8.780  1.00 41.45  ? 75  ASP   B CG  1 
ATOM   966  O OD1 . ASP   B 2 66  ? -13.699 1.997   -8.068  1.00 40.44  ? 75  ASP   B OD1 1 
ATOM   967  O OD2 . ASP   B 2 66  ? -13.124 1.167   -9.988  1.00 40.48  ? 75  ASP   B OD2 1 
ATOM   968  N N   . LEU   B 2 67  ? -16.882 -0.802  -7.185  1.00 37.20  ? 76  LEU   B N   1 
ATOM   969  C CA  . LEU   B 2 67  ? -18.270 -0.734  -7.729  1.00 35.04  ? 76  LEU   B CA  1 
ATOM   970  C C   . LEU   B 2 67  ? -19.200 0.063   -6.793  1.00 37.12  ? 76  LEU   B C   1 
ATOM   971  O O   . LEU   B 2 67  ? -18.955 0.111   -5.556  1.00 38.54  ? 76  LEU   B O   1 
ATOM   972  C CB  . LEU   B 2 67  ? -18.778 -2.158  -7.938  1.00 32.17  ? 76  LEU   B CB  1 
ATOM   973  C CG  . LEU   B 2 67  ? -18.175 -2.950  -9.103  1.00 29.70  ? 76  LEU   B CG  1 
ATOM   974  C CD1 . LEU   B 2 67  ? -18.941 -4.261  -9.266  1.00 29.78  ? 76  LEU   B CD1 1 
ATOM   975  C CD2 . LEU   B 2 67  ? -18.195 -2.176  -10.422 1.00 29.89  ? 76  LEU   B CD2 1 
ATOM   976  N N   . VAL   B 2 68  ? -20.258 0.663   -7.346  1.00 38.98  ? 77  VAL   B N   1 
ATOM   977  C CA  . VAL   B 2 68  ? -21.281 1.403   -6.540  1.00 34.36  ? 77  VAL   B CA  1 
ATOM   978  C C   . VAL   B 2 68  ? -22.601 1.375   -7.300  1.00 30.54  ? 77  VAL   B C   1 
ATOM   979  O O   . VAL   B 2 68  ? -22.570 1.540   -8.521  1.00 34.04  ? 77  VAL   B O   1 
ATOM   980  C CB  . VAL   B 2 68  ? -20.812 2.836   -6.192  1.00 33.84  ? 77  VAL   B CB  1 
ATOM   981  C CG1 . VAL   B 2 68  ? -20.638 3.716   -7.414  1.00 29.90  ? 77  VAL   B CG1 1 
ATOM   982  C CG2 . VAL   B 2 68  ? -21.714 3.514   -5.174  1.00 36.60  ? 77  VAL   B CG2 1 
ATOM   983  N N   . SER   B 2 69  ? -23.700 1.104   -6.593  1.00 30.64  ? 78  SER   B N   1 
ATOM   984  C CA  . SER   B 2 69  ? -25.080 1.129   -7.121  1.00 31.90  ? 78  SER   B CA  1 
ATOM   985  C C   . SER   B 2 69  ? -25.837 2.275   -6.439  1.00 32.63  ? 78  SER   B C   1 
ATOM   986  O O   . SER   B 2 69  ? -25.482 2.616   -5.284  1.00 28.96  ? 78  SER   B O   1 
ATOM   987  C CB  . SER   B 2 69  ? -25.759 -0.218  -6.935  1.00 32.04  ? 78  SER   B CB  1 
ATOM   988  O OG  . SER   B 2 69  ? -26.161 -0.413  -5.587  1.00 32.82  ? 78  SER   B OG  1 
ATOM   989  N N   . TYR   B 2 70  ? -26.830 2.839   -7.133  1.00 36.14  ? 79  TYR   B N   1 
ATOM   990  C CA  . TYR   B 2 70  ? -27.691 3.967   -6.671  1.00 31.32  ? 79  TYR   B CA  1 
ATOM   991  C C   . TYR   B 2 70  ? -29.169 3.570   -6.825  1.00 30.50  ? 79  TYR   B C   1 
ATOM   992  O O   . TYR   B 2 70  ? -29.535 3.094   -7.886  1.00 27.15  ? 79  TYR   B O   1 
ATOM   993  C CB  . TYR   B 2 70  ? -27.395 5.238   -7.474  1.00 32.39  ? 79  TYR   B CB  1 
ATOM   994  C CG  . TYR   B 2 70  ? -26.046 5.867   -7.212  1.00 32.20  ? 79  TYR   B CG  1 
ATOM   995  C CD1 . TYR   B 2 70  ? -24.874 5.314   -7.721  1.00 34.84  ? 79  TYR   B CD1 1 
ATOM   996  C CD2 . TYR   B 2 70  ? -25.934 7.015   -6.443  1.00 34.92  ? 79  TYR   B CD2 1 
ATOM   997  C CE1 . TYR   B 2 70  ? -23.630 5.871   -7.461  1.00 34.43  ? 79  TYR   B CE1 1 
ATOM   998  C CE2 . TYR   B 2 70  ? -24.702 7.586   -6.167  1.00 33.30  ? 79  TYR   B CE2 1 
ATOM   999  C CZ  . TYR   B 2 70  ? -23.550 7.012   -6.681  1.00 37.01  ? 79  TYR   B CZ  1 
ATOM   1000 O OH  . TYR   B 2 70  ? -22.337 7.576   -6.420  1.00 41.75  ? 79  TYR   B OH  1 
ATOM   1001 N N   A CYS   B 2 71  ? -29.972 3.794   -5.776  0.25 30.56  ? 80  CYS   B N   1 
ATOM   1002 N N   B CYS   B 2 71  ? -29.972 3.794   -5.776  0.25 30.56  ? 80  CYS   B N   1 
ATOM   1003 N N   C CYS   B 2 71  ? -29.953 3.757   -5.752  0.25 31.67  ? 80  CYS   B N   1 
ATOM   1004 N N   D CYS   B 2 71  ? -29.953 3.757   -5.752  0.25 31.67  ? 80  CYS   B N   1 
ATOM   1005 C CA  A CYS   B 2 71  ? -31.460 3.647   -5.727  0.25 29.79  ? 80  CYS   B CA  1 
ATOM   1006 C CA  B CYS   B 2 71  ? -31.460 3.647   -5.727  0.25 29.79  ? 80  CYS   B CA  1 
ATOM   1007 C CA  C CYS   B 2 71  ? -31.443 3.651   -5.680  0.25 31.69  ? 80  CYS   B CA  1 
ATOM   1008 C CA  D CYS   B 2 71  ? -31.443 3.651   -5.680  0.25 31.69  ? 80  CYS   B CA  1 
ATOM   1009 C C   A CYS   B 2 71  ? -31.846 2.231   -5.276  0.25 29.52  ? 80  CYS   B C   1 
ATOM   1010 C C   B CYS   B 2 71  ? -31.846 2.231   -5.276  0.25 29.52  ? 80  CYS   B C   1 
ATOM   1011 C C   C CYS   B 2 71  ? -31.886 2.185   -5.582  0.25 30.66  ? 80  CYS   B C   1 
ATOM   1012 C C   D CYS   B 2 71  ? -31.886 2.185   -5.582  0.25 30.66  ? 80  CYS   B C   1 
ATOM   1013 O O   A CYS   B 2 71  ? -32.985 2.058   -4.774  0.25 29.25  ? 80  CYS   B O   1 
ATOM   1014 O O   B CYS   B 2 71  ? -32.985 2.058   -4.774  0.25 29.25  ? 80  CYS   B O   1 
ATOM   1015 O O   C CYS   B 2 71  ? -33.110 1.922   -5.675  0.25 30.17  ? 80  CYS   B O   1 
ATOM   1016 O O   D CYS   B 2 71  ? -33.110 1.922   -5.675  0.25 30.17  ? 80  CYS   B O   1 
ATOM   1017 C CB  A CYS   B 2 71  ? -32.133 3.932   -7.068  0.25 29.15  ? 80  CYS   B CB  1 
ATOM   1018 C CB  B CYS   B 2 71  ? -32.133 3.932   -7.068  0.25 29.15  ? 80  CYS   B CB  1 
ATOM   1019 C CB  C CYS   B 2 71  ? -32.123 4.325   -6.866  0.25 32.27  ? 80  CYS   B CB  1 
ATOM   1020 C CB  D CYS   B 2 71  ? -32.123 4.325   -6.866  0.25 32.27  ? 80  CYS   B CB  1 
ATOM   1021 S SG  A CYS   B 2 71  ? -31.459 5.360   -7.959  0.25 28.50  ? 80  CYS   B SG  1 
ATOM   1022 S SG  B CYS   B 2 71  ? -31.459 5.360   -7.959  0.25 28.50  ? 80  CYS   B SG  1 
ATOM   1023 S SG  C CYS   B 2 71  ? -31.761 6.096   -6.981  0.25 34.85  ? 80  CYS   B SG  1 
ATOM   1024 S SG  D CYS   B 2 71  ? -31.761 6.096   -6.981  0.25 34.85  ? 80  CYS   B SG  1 
ATOM   1025 N N   . GLY   B 2 72  ? -30.935 1.263   -5.420  1.00 28.04  ? 81  GLY   B N   1 
ATOM   1026 C CA  . GLY   B 2 72  ? -31.261 -0.146  -5.190  1.00 27.55  ? 81  GLY   B CA  1 
ATOM   1027 C C   . GLY   B 2 72  ? -30.008 -1.001  -5.238  1.00 27.83  ? 81  GLY   B C   1 
ATOM   1028 O O   . GLY   B 2 72  ? -28.905 -0.515  -5.484  1.00 27.84  ? 81  GLY   B O   1 
ATOM   1029 N N   . PRO   B 2 73  ? -30.151 -2.299  -4.936  1.00 27.29  ? 82  PRO   B N   1 
ATOM   1030 C CA  . PRO   B 2 73  ? -29.016 -3.216  -5.026  1.00 31.03  ? 82  PRO   B CA  1 
ATOM   1031 C C   . PRO   B 2 73  ? -28.481 -3.417  -6.461  1.00 34.78  ? 82  PRO   B C   1 
ATOM   1032 O O   . PRO   B 2 73  ? -29.215 -3.206  -7.406  1.00 37.10  ? 82  PRO   B O   1 
ATOM   1033 C CB  . PRO   B 2 73  ? -29.607 -4.527  -4.468  1.00 30.75  ? 82  PRO   B CB  1 
ATOM   1034 C CG  . PRO   B 2 73  ? -31.132 -4.369  -4.467  1.00 27.71  ? 82  PRO   B CG  1 
ATOM   1035 C CD  . PRO   B 2 73  ? -31.391 -2.896  -4.421  1.00 26.48  ? 82  PRO   B CD  1 
ATOM   1036 N N   . TRP   B 2 74  ? -27.239 -3.890  -6.586  1.00 39.58  ? 83  TRP   B N   1 
ATOM   1037 C CA  . TRP   B 2 74  ? -26.591 -4.282  -7.866  1.00 38.15  ? 83  TRP   B CA  1 
ATOM   1038 C C   . TRP   B 2 74  ? -27.543 -5.213  -8.637  1.00 40.49  ? 83  TRP   B C   1 
ATOM   1039 O O   . TRP   B 2 74  ? -28.101 -6.115  -8.032  1.00 37.05  ? 83  TRP   B O   1 
ATOM   1040 C CB  . TRP   B 2 74  ? -25.214 -4.916  -7.594  1.00 37.09  ? 83  TRP   B CB  1 
ATOM   1041 C CG  . TRP   B 2 74  ? -24.372 -5.071  -8.822  1.00 34.76  ? 83  TRP   B CG  1 
ATOM   1042 C CD1 . TRP   B 2 74  ? -24.286 -6.170  -9.623  1.00 32.99  ? 83  TRP   B CD1 1 
ATOM   1043 C CD2 . TRP   B 2 74  ? -23.517 -4.081  -9.413  1.00 33.64  ? 83  TRP   B CD2 1 
ATOM   1044 N NE1 . TRP   B 2 74  ? -23.439 -5.930  -10.666 1.00 33.47  ? 83  TRP   B NE1 1 
ATOM   1045 C CE2 . TRP   B 2 74  ? -22.964 -4.656  -10.575 1.00 30.03  ? 83  TRP   B CE2 1 
ATOM   1046 C CE3 . TRP   B 2 74  ? -23.193 -2.753  -9.094  1.00 34.50  ? 83  TRP   B CE3 1 
ATOM   1047 C CZ2 . TRP   B 2 74  ? -22.104 -3.960  -11.416 1.00 29.80  ? 83  TRP   B CZ2 1 
ATOM   1048 C CZ3 . TRP   B 2 74  ? -22.348 -2.061  -9.928  1.00 33.52  ? 83  TRP   B CZ3 1 
ATOM   1049 C CH2 . TRP   B 2 74  ? -21.817 -2.659  -11.076 1.00 32.39  ? 83  TRP   B CH2 1 
ATOM   1050 N N   . LYS   B 2 75  ? -27.723 -4.988  -9.940  1.00 45.03  ? 84  LYS   B N   1 
ATOM   1051 C CA  . LYS   B 2 75  ? -28.703 -5.716  -10.787 1.00 44.79  ? 84  LYS   B CA  1 
ATOM   1052 C C   . LYS   B 2 75  ? -28.014 -6.625  -11.810 1.00 45.02  ? 84  LYS   B C   1 
ATOM   1053 O O   . LYS   B 2 75  ? -28.708 -7.502  -12.314 1.00 43.16  ? 84  LYS   B O   1 
ATOM   1054 C CB  . LYS   B 2 75  ? -29.562 -4.693  -11.528 1.00 49.05  ? 84  LYS   B CB  1 
ATOM   1055 C CG  . LYS   B 2 75  ? -30.389 -3.800  -10.615 1.00 47.48  ? 84  LYS   B CG  1 
ATOM   1056 C CD  . LYS   B 2 75  ? -31.551 -4.540  -10.017 1.00 47.14  ? 84  LYS   B CD  1 
ATOM   1057 C CE  . LYS   B 2 75  ? -32.246 -3.775  -8.915  1.00 47.70  ? 84  LYS   B CE  1 
ATOM   1058 N NZ  . LYS   B 2 75  ? -33.300 -4.617  -8.313  1.00 49.61  ? 84  LYS   B NZ  1 
ATOM   1059 N N   . LEU   B 2 76  ? -26.716 -6.427  -12.081 1.00 44.56  ? 85  LEU   B N   1 
ATOM   1060 C CA  . LEU   B 2 76  ? -25.996 -6.914  -13.291 1.00 45.53  ? 85  LEU   B CA  1 
ATOM   1061 C C   . LEU   B 2 76  ? -25.251 -8.205  -12.956 1.00 47.02  ? 85  LEU   B C   1 
ATOM   1062 O O   . LEU   B 2 76  ? -24.222 -8.130  -12.259 1.00 45.05  ? 85  LEU   B O   1 
ATOM   1063 C CB  . LEU   B 2 76  ? -25.023 -5.826  -13.771 1.00 46.06  ? 85  LEU   B CB  1 
ATOM   1064 C CG  . LEU   B 2 76  ? -25.674 -4.472  -14.065 1.00 44.93  ? 85  LEU   B CG  1 
ATOM   1065 C CD1 . LEU   B 2 76  ? -24.674 -3.478  -14.657 1.00 46.84  ? 85  LEU   B CD1 1 
ATOM   1066 C CD2 . LEU   B 2 76  ? -26.875 -4.641  -14.985 1.00 43.09  ? 85  LEU   B CD2 1 
ATOM   1067 N N   . ASP   B 2 77  ? -25.747 -9.340  -13.448 1.00 47.34  ? 86  ASP   B N   1 
ATOM   1068 C CA  . ASP   B 2 77  ? -25.282 -10.670 -12.991 1.00 53.28  ? 86  ASP   B CA  1 
ATOM   1069 C C   . ASP   B 2 77  ? -24.684 -11.453 -14.168 1.00 52.42  ? 86  ASP   B C   1 
ATOM   1070 O O   . ASP   B 2 77  ? -24.186 -12.555 -13.922 1.00 53.61  ? 86  ASP   B O   1 
ATOM   1071 C CB  . ASP   B 2 77  ? -26.417 -11.415 -12.282 1.00 58.95  ? 86  ASP   B CB  1 
ATOM   1072 C CG  . ASP   B 2 77  ? -27.696 -11.456 -13.095 1.00 64.06  ? 86  ASP   B CG  1 
ATOM   1073 O OD1 . ASP   B 2 77  ? -27.718 -10.787 -14.149 1.00 67.29  ? 86  ASP   B OD1 1 
ATOM   1074 O OD2 . ASP   B 2 77  ? -28.656 -12.152 -12.673 1.00 63.30  ? 86  ASP   B OD2 1 
ATOM   1075 N N   . ALA   B 2 78  ? -24.673 -10.905 -15.386 1.00 51.86  ? 87  ALA   B N   1 
ATOM   1076 C CA  . ALA   B 2 78  ? -24.206 -11.616 -16.599 1.00 47.52  ? 87  ALA   B CA  1 
ATOM   1077 C C   . ALA   B 2 78  ? -22.669 -11.664 -16.592 1.00 51.78  ? 87  ALA   B C   1 
ATOM   1078 O O   . ALA   B 2 78  ? -22.066 -10.648 -16.152 1.00 56.65  ? 87  ALA   B O   1 
ATOM   1079 C CB  . ALA   B 2 78  ? -24.745 -10.947 -17.838 1.00 47.50  ? 87  ALA   B CB  1 
ATOM   1080 N N   . ALA   B 2 79  ? -22.069 -12.771 -17.071 1.00 45.13  ? 88  ALA   B N   1 
ATOM   1081 C CA  . ALA   B 2 79  ? -20.612 -13.077 -17.010 1.00 45.37  ? 88  ALA   B CA  1 
ATOM   1082 C C   . ALA   B 2 79  ? -20.009 -13.302 -18.409 1.00 42.83  ? 88  ALA   B C   1 
ATOM   1083 O O   . ALA   B 2 79  ? -20.694 -13.888 -19.239 1.00 38.38  ? 88  ALA   B O   1 
ATOM   1084 C CB  . ALA   B 2 79  ? -20.404 -14.306 -16.158 1.00 48.16  ? 88  ALA   B CB  1 
ATOM   1085 N N   . TRP   B 2 80  ? -18.766 -12.867 -18.651 1.00 40.38  ? 89  TRP   B N   1 
ATOM   1086 C CA  . TRP   B 2 80  ? -17.941 -13.311 -19.814 1.00 44.88  ? 89  TRP   B CA  1 
ATOM   1087 C C   . TRP   B 2 80  ? -17.927 -14.846 -19.835 1.00 47.46  ? 89  TRP   B C   1 
ATOM   1088 O O   . TRP   B 2 80  ? -17.742 -15.440 -18.735 1.00 43.24  ? 89  TRP   B O   1 
ATOM   1089 C CB  . TRP   B 2 80  ? -16.516 -12.725 -19.783 1.00 46.21  ? 89  TRP   B CB  1 
ATOM   1090 C CG  . TRP   B 2 80  ? -15.704 -13.098 -20.987 1.00 51.28  ? 89  TRP   B CG  1 
ATOM   1091 C CD1 . TRP   B 2 80  ? -16.144 -13.175 -22.278 1.00 49.02  ? 89  TRP   B CD1 1 
ATOM   1092 C CD2 . TRP   B 2 80  ? -14.313 -13.473 -21.021 1.00 54.12  ? 89  TRP   B CD2 1 
ATOM   1093 N NE1 . TRP   B 2 80  ? -15.129 -13.560 -23.111 1.00 49.70  ? 89  TRP   B NE1 1 
ATOM   1094 C CE2 . TRP   B 2 80  ? -13.993 -13.754 -22.370 1.00 50.53  ? 89  TRP   B CE2 1 
ATOM   1095 C CE3 . TRP   B 2 80  ? -13.312 -13.612 -20.051 1.00 55.07  ? 89  TRP   B CE3 1 
ATOM   1096 C CZ2 . TRP   B 2 80  ? -12.716 -14.153 -22.768 1.00 49.60  ? 89  TRP   B CZ2 1 
ATOM   1097 C CZ3 . TRP   B 2 80  ? -12.047 -14.002 -20.447 1.00 53.96  ? 89  TRP   B CZ3 1 
ATOM   1098 C CH2 . TRP   B 2 80  ? -11.757 -14.262 -21.789 1.00 50.05  ? 89  TRP   B CH2 1 
ATOM   1099 N N   . ASP   B 2 81  ? -18.157 -15.462 -21.011 1.00 45.46  ? 90  ASP   B N   1 
ATOM   1100 C CA  . ASP   B 2 81  ? -18.252 -16.944 -21.161 1.00 47.40  ? 90  ASP   B CA  1 
ATOM   1101 C C   . ASP   B 2 81  ? -16.849 -17.559 -21.213 1.00 45.58  ? 90  ASP   B C   1 
ATOM   1102 O O   . ASP   B 2 81  ? -16.767 -18.778 -21.224 1.00 55.24  ? 90  ASP   B O   1 
ATOM   1103 C CB  . ASP   B 2 81  ? -19.133 -17.381 -22.344 1.00 45.97  ? 90  ASP   B CB  1 
ATOM   1104 C CG  . ASP   B 2 81  ? -18.621 -17.070 -23.740 1.00 47.54  ? 90  ASP   B CG  1 
ATOM   1105 O OD1 . ASP   B 2 81  ? -17.591 -16.352 -23.877 1.00 45.39  ? 90  ASP   B OD1 1 
ATOM   1106 O OD2 . ASP   B 2 81  ? -19.281 -17.527 -24.695 1.00 48.89  ? 90  ASP   B OD2 1 
ATOM   1107 N N   . GLY   B 2 82  ? -15.801 -16.743 -21.225 1.00 47.74  ? 91  GLY   B N   1 
ATOM   1108 C CA  . GLY   B 2 82  ? -14.399 -17.185 -21.281 1.00 49.17  ? 91  GLY   B CA  1 
ATOM   1109 C C   . GLY   B 2 82  ? -13.941 -17.452 -22.702 1.00 52.46  ? 91  GLY   B C   1 
ATOM   1110 O O   . GLY   B 2 82  ? -12.748 -17.792 -22.848 1.00 52.97  ? 91  GLY   B O   1 
ATOM   1111 N N   . LEU   B 2 83  ? -14.827 -17.277 -23.703 1.00 56.21  ? 92  LEU   B N   1 
ATOM   1112 C CA  . LEU   B 2 83  ? -14.640 -17.713 -25.120 1.00 55.67  ? 92  LEU   B CA  1 
ATOM   1113 C C   . LEU   B 2 83  ? -14.962 -16.574 -26.106 1.00 60.92  ? 92  LEU   B C   1 
ATOM   1114 O O   . LEU   B 2 83  ? -14.027 -16.026 -26.749 1.00 52.47  ? 92  LEU   B O   1 
ATOM   1115 C CB  . LEU   B 2 83  ? -15.565 -18.908 -25.375 1.00 59.52  ? 92  LEU   B CB  1 
ATOM   1116 C CG  . LEU   B 2 83  ? -15.083 -20.244 -24.813 1.00 65.85  ? 92  LEU   B CG  1 
ATOM   1117 C CD1 . LEU   B 2 83  ? -16.007 -21.382 -25.230 1.00 68.43  ? 92  LEU   B CD1 1 
ATOM   1118 C CD2 . LEU   B 2 83  ? -13.648 -20.530 -25.238 1.00 64.68  ? 92  LEU   B CD2 1 
ATOM   1119 N N   . SER   B 2 84  ? -16.253 -16.247 -26.234 1.00 59.13  ? 93  SER   B N   1 
ATOM   1120 C CA  . SER   B 2 84  ? -16.829 -15.285 -27.210 1.00 52.11  ? 93  SER   B CA  1 
ATOM   1121 C C   . SER   B 2 84  ? -16.108 -13.929 -27.141 1.00 48.38  ? 93  SER   B C   1 
ATOM   1122 O O   . SER   B 2 84  ? -15.610 -13.562 -26.053 1.00 46.20  ? 93  SER   B O   1 
ATOM   1123 C CB  . SER   B 2 84  ? -18.306 -15.146 -26.956 1.00 50.87  ? 93  SER   B CB  1 
ATOM   1124 O OG  . SER   B 2 84  ? -18.819 -16.322 -26.337 1.00 45.14  ? 93  SER   B OG  1 
ATOM   1125 N N   . GLU   B 2 85  ? -16.028 -13.224 -28.274 1.00 52.93  ? 94  GLU   B N   1 
ATOM   1126 C CA  . GLU   B 2 85  ? -15.631 -11.790 -28.324 1.00 57.26  ? 94  GLU   B CA  1 
ATOM   1127 C C   . GLU   B 2 85  ? -16.695 -10.992 -27.559 1.00 48.69  ? 94  GLU   B C   1 
ATOM   1128 O O   . GLU   B 2 85  ? -17.835 -11.522 -27.358 1.00 36.09  ? 94  GLU   B O   1 
ATOM   1129 C CB  . GLU   B 2 85  ? -15.477 -11.256 -29.759 1.00 66.96  ? 94  GLU   B CB  1 
ATOM   1130 C CG  . GLU   B 2 85  ? -14.156 -11.628 -30.439 1.00 74.03  ? 94  GLU   B CG  1 
ATOM   1131 C CD  . GLU   B 2 85  ? -13.614 -10.679 -31.509 1.00 76.28  ? 94  GLU   B CD  1 
ATOM   1132 O OE1 . GLU   B 2 85  ? -14.398 -9.872  -32.046 1.00 76.26  ? 94  GLU   B OE1 1 
ATOM   1133 O OE2 . GLU   B 2 85  ? -12.394 -10.746 -31.812 1.00 67.80  ? 94  GLU   B OE2 1 
ATOM   1134 N N   . VAL   B 2 86  ? -16.321 -9.791  -27.117 1.00 41.52  ? 95  VAL   B N   1 
ATOM   1135 C CA  . VAL   B 2 86  ? -17.215 -8.859  -26.353 1.00 49.08  ? 95  VAL   B CA  1 
ATOM   1136 C C   . VAL   B 2 86  ? -17.249 -7.505  -27.069 1.00 46.90  ? 95  VAL   B C   1 
ATOM   1137 O O   . VAL   B 2 86  ? -16.333 -7.240  -27.893 1.00 47.85  ? 95  VAL   B O   1 
ATOM   1138 C CB  . VAL   B 2 86  ? -16.798 -8.701  -24.866 1.00 40.06  ? 95  VAL   B CB  1 
ATOM   1139 C CG1 . VAL   B 2 86  ? -16.526 -10.043 -24.215 1.00 42.09  ? 95  VAL   B CG1 1 
ATOM   1140 C CG2 . VAL   B 2 86  ? -15.612 -7.765  -24.666 1.00 38.71  ? 95  VAL   B CG2 1 
ATOM   1141 N N   . GLN   B 2 87  ? -18.252 -6.678  -26.739 1.00 50.75  ? 96  GLN   B N   1 
ATOM   1142 C CA  . GLN   B 2 87  ? -18.310 -5.236  -27.113 1.00 49.27  ? 96  GLN   B CA  1 
ATOM   1143 C C   . GLN   B 2 87  ? -18.245 -4.369  -25.850 1.00 44.61  ? 96  GLN   B C   1 
ATOM   1144 O O   . GLN   B 2 87  ? -19.091 -4.553  -24.959 1.00 45.45  ? 96  GLN   B O   1 
ATOM   1145 C CB  . GLN   B 2 87  ? -19.548 -4.923  -27.959 1.00 50.85  ? 96  GLN   B CB  1 
ATOM   1146 C CG  . GLN   B 2 87  ? -19.225 -4.844  -29.444 1.00 57.72  ? 96  GLN   B CG  1 
ATOM   1147 C CD  . GLN   B 2 87  ? -20.439 -4.969  -30.334 1.00 56.66  ? 96  GLN   B CD  1 
ATOM   1148 O OE1 . GLN   B 2 87  ? -21.366 -4.167  -30.281 1.00 54.87  ? 96  GLN   B OE1 1 
ATOM   1149 N NE2 . GLN   B 2 87  ? -20.442 -5.993  -31.168 1.00 59.76  ? 96  GLN   B NE2 1 
ATOM   1150 N N   . LEU   B 2 88  ? -17.232 -3.495  -25.795 1.00 40.36  ? 97  LEU   B N   1 
ATOM   1151 C CA  . LEU   B 2 88  ? -17.170 -2.278  -24.957 1.00 40.36  ? 97  LEU   B CA  1 
ATOM   1152 C C   . LEU   B 2 88  ? -18.040 -1.211  -25.617 1.00 42.17  ? 97  LEU   B C   1 
ATOM   1153 O O   . LEU   B 2 88  ? -17.620 -0.708  -26.680 1.00 49.55  ? 97  LEU   B O   1 
ATOM   1154 C CB  . LEU   B 2 88  ? -15.720 -1.787  -24.878 1.00 36.04  ? 97  LEU   B CB  1 
ATOM   1155 C CG  . LEU   B 2 88  ? -15.511 -0.434  -24.191 1.00 36.81  ? 97  LEU   B CG  1 
ATOM   1156 C CD1 . LEU   B 2 88  ? -15.939 -0.486  -22.732 1.00 39.55  ? 97  LEU   B CD1 1 
ATOM   1157 C CD2 . LEU   B 2 88  ? -14.071 0.039   -24.291 1.00 36.12  ? 97  LEU   B CD2 1 
ATOM   1158 N N   . LEU   B 2 89  ? -19.179 -0.880  -25.007 1.00 44.45  ? 98  LEU   B N   1 
ATOM   1159 C CA  . LEU   B 2 89  ? -19.993 0.322   -25.336 1.00 38.52  ? 98  LEU   B CA  1 
ATOM   1160 C C   . LEU   B 2 89  ? -19.264 1.518   -24.738 1.00 41.60  ? 98  LEU   B C   1 
ATOM   1161 O O   . LEU   B 2 89  ? -19.690 2.004   -23.654 1.00 49.77  ? 98  LEU   B O   1 
ATOM   1162 C CB  . LEU   B 2 89  ? -21.412 0.132   -24.790 1.00 39.45  ? 98  LEU   B CB  1 
ATOM   1163 C CG  . LEU   B 2 89  ? -22.428 1.250   -25.055 1.00 38.74  ? 98  LEU   B CG  1 
ATOM   1164 C CD1 . LEU   B 2 89  ? -22.159 1.979   -26.349 1.00 43.28  ? 98  LEU   B CD1 1 
ATOM   1165 C CD2 . LEU   B 2 89  ? -23.837 0.700   -25.090 1.00 39.25  ? 98  LEU   B CD2 1 
ATOM   1166 N N   . ALA   B 2 90  ? -18.160 1.926   -25.375 1.00 36.82  ? 99  ALA   B N   1 
ATOM   1167 C CA  . ALA   B 2 90  ? -17.330 3.056   -24.905 1.00 39.78  ? 99  ALA   B CA  1 
ATOM   1168 C C   . ALA   B 2 90  ? -18.143 4.341   -25.039 1.00 43.59  ? 99  ALA   B C   1 
ATOM   1169 O O   . ALA   B 2 90  ? -18.724 4.561   -26.127 1.00 41.53  ? 99  ALA   B O   1 
ATOM   1170 C CB  . ALA   B 2 90  ? -16.053 3.172   -25.685 1.00 43.04  ? 99  ALA   B CB  1 
ATOM   1171 N N   . VAL   B 2 91  ? -18.159 5.158   -23.983 1.00 44.20  ? 100 VAL   B N   1 
ATOM   1172 C CA  . VAL   B 2 91  ? -18.764 6.520   -23.987 1.00 41.14  ? 100 VAL   B CA  1 
ATOM   1173 C C   . VAL   B 2 91  ? -17.696 7.534   -23.570 1.00 40.76  ? 100 VAL   B C   1 
ATOM   1174 O O   . VAL   B 2 91  ? -17.666 7.991   -22.431 1.00 39.69  ? 100 VAL   B O   1 
ATOM   1175 C CB  . VAL   B 2 91  ? -20.029 6.550   -23.111 1.00 43.66  ? 100 VAL   B CB  1 
ATOM   1176 C CG1 . VAL   B 2 91  ? -20.521 7.958   -22.826 1.00 49.09  ? 100 VAL   B CG1 1 
ATOM   1177 C CG2 . VAL   B 2 91  ? -21.153 5.701   -23.706 1.00 42.52  ? 100 VAL   B CG2 1 
ATOM   1178 N N   . PRO   B 2 92  ? -16.786 7.937   -24.491 1.00 43.01  ? 101 PRO   B N   1 
ATOM   1179 C CA  . PRO   B 2 92  ? -15.707 8.879   -24.161 1.00 42.18  ? 101 PRO   B CA  1 
ATOM   1180 C C   . PRO   B 2 92  ? -16.179 10.318  -23.951 1.00 40.51  ? 101 PRO   B C   1 
ATOM   1181 O O   . PRO   B 2 92  ? -17.187 10.718  -24.519 1.00 38.03  ? 101 PRO   B O   1 
ATOM   1182 C CB  . PRO   B 2 92  ? -14.763 8.858   -25.381 1.00 38.22  ? 101 PRO   B CB  1 
ATOM   1183 C CG  . PRO   B 2 92  ? -15.289 7.765   -26.300 1.00 41.22  ? 101 PRO   B CG  1 
ATOM   1184 C CD  . PRO   B 2 92  ? -16.723 7.488   -25.892 1.00 44.04  ? 101 PRO   B CD  1 
ATOM   1185 N N   . PRO   B 2 93  ? -15.443 11.150  -23.181 1.00 44.09  ? 102 PRO   B N   1 
ATOM   1186 C CA  . PRO   B 2 93  ? -15.765 12.570  -23.030 1.00 46.45  ? 102 PRO   B CA  1 
ATOM   1187 C C   . PRO   B 2 93  ? -15.845 13.391  -24.337 1.00 53.03  ? 102 PRO   B C   1 
ATOM   1188 O O   . PRO   B 2 93  ? -14.922 13.325  -25.157 1.00 57.15  ? 102 PRO   B O   1 
ATOM   1189 C CB  . PRO   B 2 93  ? -14.632 13.097  -22.127 1.00 44.78  ? 102 PRO   B CB  1 
ATOM   1190 C CG  . PRO   B 2 93  ? -14.164 11.884  -21.357 1.00 45.20  ? 102 PRO   B CG  1 
ATOM   1191 C CD  . PRO   B 2 93  ? -14.287 10.753  -22.358 1.00 46.36  ? 102 PRO   B CD  1 
ATOM   1192 N N   . GLY   B 2 94  ? -16.956 14.134  -24.504 1.00 52.31  ? 103 GLY   B N   1 
ATOM   1193 C CA  . GLY   B 2 94  ? -17.260 15.000  -25.664 1.00 52.43  ? 103 GLY   B CA  1 
ATOM   1194 C C   . GLY   B 2 94  ? -17.726 14.251  -26.909 1.00 48.77  ? 103 GLY   B C   1 
ATOM   1195 O O   . GLY   B 2 94  ? -18.124 14.919  -27.880 1.00 51.86  ? 103 GLY   B O   1 
ATOM   1196 N N   . GLU   B 2 95  ? -17.714 12.917  -26.898 1.00 54.76  ? 104 GLU   B N   1 
ATOM   1197 C CA  . GLU   B 2 95  ? -17.825 12.074  -28.120 1.00 54.22  ? 104 GLU   B CA  1 
ATOM   1198 C C   . GLU   B 2 95  ? -19.007 11.128  -27.934 1.00 54.42  ? 104 GLU   B C   1 
ATOM   1199 O O   . GLU   B 2 95  ? -19.312 10.833  -26.765 1.00 66.86  ? 104 GLU   B O   1 
ATOM   1200 C CB  . GLU   B 2 95  ? -16.503 11.335  -28.356 1.00 57.07  ? 104 GLU   B CB  1 
ATOM   1201 C CG  . GLU   B 2 95  ? -15.309 12.264  -28.619 1.00 59.90  ? 104 GLU   B CG  1 
ATOM   1202 C CD  . GLU   B 2 95  ? -13.954 11.562  -28.683 1.00 66.12  ? 104 GLU   B CD  1 
ATOM   1203 O OE1 . GLU   B 2 95  ? -13.954 10.312  -28.697 1.00 61.65  ? 104 GLU   B OE1 1 
ATOM   1204 O OE2 . GLU   B 2 95  ? -12.894 12.260  -28.711 1.00 62.97  ? 104 GLU   B OE2 1 
ATOM   1205 N N   . ARG   B 2 96  ? -19.663 10.710  -29.021 1.00 49.82  ? 105 ARG   B N   1 
ATOM   1206 C CA  . ARG   B 2 96  ? -20.872 9.844   -28.979 1.00 52.09  ? 105 ARG   B CA  1 
ATOM   1207 C C   . ARG   B 2 96  ? -20.472 8.420   -28.580 1.00 52.34  ? 105 ARG   B C   1 
ATOM   1208 O O   . ARG   B 2 96  ? -19.287 8.078   -28.686 1.00 47.49  ? 105 ARG   B O   1 
ATOM   1209 C CB  . ARG   B 2 96  ? -21.609 9.866   -30.326 1.00 59.65  ? 105 ARG   B CB  1 
ATOM   1210 C CG  . ARG   B 2 96  ? -22.711 8.821   -30.463 1.00 61.80  ? 105 ARG   B CG  1 
ATOM   1211 C CD  . ARG   B 2 96  ? -23.822 9.166   -31.438 1.00 67.52  ? 105 ARG   B CD  1 
ATOM   1212 N NE  . ARG   B 2 96  ? -23.498 8.873   -32.828 1.00 67.28  ? 105 ARG   B NE  1 
ATOM   1213 C CZ  . ARG   B 2 96  ? -22.930 9.725   -33.672 1.00 73.04  ? 105 ARG   B CZ  1 
ATOM   1214 N NH1 . ARG   B 2 96  ? -22.601 10.948  -33.281 1.00 73.88  ? 105 ARG   B NH1 1 
ATOM   1215 N NH2 . ARG   B 2 96  ? -22.692 9.346   -34.916 1.00 76.45  ? 105 ARG   B NH2 1 
ATOM   1216 N N   . ALA   B 2 97  ? -21.441 7.648   -28.077 1.00 51.80  ? 106 ALA   B N   1 
ATOM   1217 C CA  . ALA   B 2 97  ? -21.314 6.216   -27.749 1.00 47.98  ? 106 ALA   B CA  1 
ATOM   1218 C C   . ALA   B 2 97  ? -20.744 5.459   -28.951 1.00 48.54  ? 106 ALA   B C   1 
ATOM   1219 O O   . ALA   B 2 97  ? -21.300 5.566   -30.047 1.00 51.85  ? 106 ALA   B O   1 
ATOM   1220 C CB  . ALA   B 2 97  ? -22.654 5.680   -27.333 1.00 49.06  ? 106 ALA   B CB  1 
ATOM   1221 N N   . LYS   B 2 98  ? -19.672 4.710   -28.723 1.00 53.58  ? 107 LYS   B N   1 
ATOM   1222 C CA  . LYS   B 2 98  ? -18.924 3.924   -29.738 1.00 57.85  ? 107 LYS   B CA  1 
ATOM   1223 C C   . LYS   B 2 98  ? -18.757 2.497   -29.219 1.00 54.13  ? 107 LYS   B C   1 
ATOM   1224 O O   . LYS   B 2 98  ? -18.129 2.336   -28.156 1.00 52.57  ? 107 LYS   B O   1 
ATOM   1225 C CB  . LYS   B 2 98  ? -17.550 4.562   -29.971 1.00 63.71  ? 107 LYS   B CB  1 
ATOM   1226 C CG  . LYS   B 2 98  ? -16.834 4.155   -31.254 1.00 69.78  ? 107 LYS   B CG  1 
ATOM   1227 C CD  . LYS   B 2 98  ? -15.631 5.021   -31.569 1.00 75.59  ? 107 LYS   B CD  1 
ATOM   1228 C CE  . LYS   B 2 98  ? -14.960 5.559   -30.319 1.00 79.47  ? 107 LYS   B CE  1 
ATOM   1229 N NZ  . LYS   B 2 98  ? -13.671 6.226   -30.616 1.00 87.29  ? 107 LYS   B NZ  1 
ATOM   1230 N N   . ASN   B 2 99  ? -19.337 1.515   -29.907 1.00 50.65  ? 108 ASN   B N   1 
ATOM   1231 C CA  . ASN   B 2 99  ? -19.016 0.081   -29.681 1.00 52.57  ? 108 ASN   B CA  1 
ATOM   1232 C C   . ASN   B 2 99  ? -17.625 -0.194  -30.259 1.00 52.71  ? 108 ASN   B C   1 
ATOM   1233 O O   . ASN   B 2 99  ? -17.327 0.299   -31.364 1.00 60.34  ? 108 ASN   B O   1 
ATOM   1234 C CB  . ASN   B 2 99  ? -20.095 -0.848  -30.223 1.00 45.40  ? 108 ASN   B CB  1 
ATOM   1235 C CG  . ASN   B 2 99  ? -21.413 -0.529  -29.566 1.00 51.77  ? 108 ASN   B CG  1 
ATOM   1236 O OD1 . ASN   B 2 99  ? -21.708 0.651   -29.387 1.00 57.83  ? 108 ASN   B OD1 1 
ATOM   1237 N ND2 . ASN   B 2 99  ? -22.190 -1.543  -29.195 1.00 49.33  ? 108 ASN   B ND2 1 
ATOM   1238 N N   . ILE   B 2 100 ? -16.796 -0.916  -29.508 1.00 46.81  ? 109 ILE   B N   1 
ATOM   1239 C CA  . ILE   B 2 100 ? -15.429 -1.315  -29.930 1.00 46.14  ? 109 ILE   B CA  1 
ATOM   1240 C C   . ILE   B 2 100 ? -15.258 -2.774  -29.531 1.00 42.47  ? 109 ILE   B C   1 
ATOM   1241 O O   . ILE   B 2 100 ? -15.213 -3.042  -28.323 1.00 50.23  ? 109 ILE   B O   1 
ATOM   1242 C CB  . ILE   B 2 100 ? -14.366 -0.413  -29.285 1.00 51.47  ? 109 ILE   B CB  1 
ATOM   1243 C CG1 . ILE   B 2 100 ? -14.700 1.079   -29.411 1.00 52.35  ? 109 ILE   B CG1 1 
ATOM   1244 C CG2 . ILE   B 2 100 ? -12.997 -0.751  -29.849 1.00 55.01  ? 109 ILE   B CG2 1 
ATOM   1245 C CD1 . ILE   B 2 100 ? -14.174 1.739   -30.670 1.00 53.92  ? 109 ILE   B CD1 1 
ATOM   1246 N N   . GLN   B 2 101 ? -15.219 -3.681  -30.500 1.00 41.58  ? 110 GLN   B N   1 
ATOM   1247 C CA  . GLN   B 2 101 ? -15.386 -5.136  -30.253 1.00 48.56  ? 110 GLN   B CA  1 
ATOM   1248 C C   . GLN   B 2 101 ? -13.997 -5.775  -30.111 1.00 51.03  ? 110 GLN   B C   1 
ATOM   1249 O O   . GLN   B 2 101 ? -13.106 -5.417  -30.883 1.00 51.85  ? 110 GLN   B O   1 
ATOM   1250 C CB  . GLN   B 2 101 ? -16.248 -5.774  -31.340 1.00 50.29  ? 110 GLN   B CB  1 
ATOM   1251 C CG  . GLN   B 2 101 ? -16.131 -7.287  -31.394 1.00 52.24  ? 110 GLN   B CG  1 
ATOM   1252 C CD  . GLN   B 2 101 ? -17.251 -7.934  -32.170 1.00 53.20  ? 110 GLN   B CD  1 
ATOM   1253 O OE1 . GLN   B 2 101 ? -18.397 -7.490  -32.153 1.00 52.46  ? 110 GLN   B OE1 1 
ATOM   1254 N NE2 . GLN   B 2 101 ? -16.928 -9.023  -32.841 1.00 52.60  ? 110 GLN   B NE2 1 
ATOM   1255 N N   . THR   B 2 102 ? -13.816 -6.644  -29.105 1.00 52.88  ? 111 THR   B N   1 
ATOM   1256 C CA  . THR   B 2 102 ? -12.510 -7.243  -28.732 1.00 50.74  ? 111 THR   B CA  1 
ATOM   1257 C C   . THR   B 2 102 ? -12.793 -8.608  -28.102 1.00 53.28  ? 111 THR   B C   1 
ATOM   1258 O O   . THR   B 2 102 ? -13.937 -8.792  -27.621 1.00 59.88  ? 111 THR   B O   1 
ATOM   1259 C CB  . THR   B 2 102 ? -11.717 -6.247  -27.875 1.00 54.27  ? 111 THR   B CB  1 
ATOM   1260 O OG1 . THR   B 2 102 ? -10.372 -6.714  -27.737 1.00 59.08  ? 111 THR   B OG1 1 
ATOM   1261 C CG2 . THR   B 2 102 ? -12.344 -6.010  -26.519 1.00 55.14  ? 111 THR   B CG2 1 
ATOM   1262 N N   . LEU   B 2 103 ? -11.849 -9.550  -28.219 1.00 45.10  ? 112 LEU   B N   1 
ATOM   1263 C CA  . LEU   B 2 103 ? -11.780 -10.782 -27.390 1.00 42.18  ? 112 LEU   B CA  1 
ATOM   1264 C C   . LEU   B 2 103 ? -11.004 -10.396 -26.134 1.00 45.25  ? 112 LEU   B C   1 
ATOM   1265 O O   . LEU   B 2 103 ? -9.871  -9.903  -26.230 1.00 47.08  ? 112 LEU   B O   1 
ATOM   1266 C CB  . LEU   B 2 103 ? -11.067 -11.913 -28.143 1.00 43.04  ? 112 LEU   B CB  1 
ATOM   1267 C CG  . LEU   B 2 103 ? -10.835 -13.204 -27.351 1.00 42.19  ? 112 LEU   B CG  1 
ATOM   1268 C CD1 . LEU   B 2 103 ? -12.048 -14.119 -27.406 1.00 42.79  ? 112 LEU   B CD1 1 
ATOM   1269 C CD2 . LEU   B 2 103 ? -9.609  -13.946 -27.852 1.00 43.59  ? 112 LEU   B CD2 1 
ATOM   1270 N N   . PRO   B 2 104 ? -11.586 -10.543 -24.924 1.00 39.33  ? 113 PRO   B N   1 
ATOM   1271 C CA  . PRO   B 2 104 ? -10.871 -10.165 -23.717 1.00 45.18  ? 113 PRO   B CA  1 
ATOM   1272 C C   . PRO   B 2 104 ? -9.708  -11.135 -23.439 1.00 49.75  ? 113 PRO   B C   1 
ATOM   1273 O O   . PRO   B 2 104 ? -9.810  -12.350 -23.720 1.00 43.02  ? 113 PRO   B O   1 
ATOM   1274 C CB  . PRO   B 2 104 ? -11.916 -10.179 -22.587 1.00 42.06  ? 113 PRO   B CB  1 
ATOM   1275 C CG  . PRO   B 2 104 ? -13.236 -10.455 -23.267 1.00 45.37  ? 113 PRO   B CG  1 
ATOM   1276 C CD  . PRO   B 2 104 ? -12.937 -11.034 -24.639 1.00 43.94  ? 113 PRO   B CD  1 
ATOM   1277 N N   . GLY   B 2 105 ? -8.625  -10.547 -22.924 1.00 49.23  ? 114 GLY   B N   1 
ATOM   1278 C CA  . GLY   B 2 105 ? -7.591  -11.211 -22.122 1.00 50.69  ? 114 GLY   B CA  1 
ATOM   1279 C C   . GLY   B 2 105 ? -8.114  -11.693 -20.778 1.00 50.41  ? 114 GLY   B C   1 
ATOM   1280 O O   . GLY   B 2 105 ? -9.296  -12.126 -20.691 1.00 45.80  ? 114 GLY   B O   1 
ATOM   1281 N N   . ILE   B 2 106 ? -7.223  -11.678 -19.787 1.00 53.36  ? 115 ILE   B N   1 
ATOM   1282 C CA  . ILE   B 2 106 ? -7.299  -12.465 -18.520 1.00 52.71  ? 115 ILE   B CA  1 
ATOM   1283 C C   . ILE   B 2 106 ? -6.393  -11.781 -17.486 1.00 49.38  ? 115 ILE   B C   1 
ATOM   1284 O O   . ILE   B 2 106 ? -5.186  -11.715 -17.703 1.00 46.77  ? 115 ILE   B O   1 
ATOM   1285 C CB  . ILE   B 2 106 ? -6.846  -13.927 -18.724 1.00 54.85  ? 115 ILE   B CB  1 
ATOM   1286 C CG1 . ILE   B 2 106 ? -7.710  -14.726 -19.701 1.00 55.47  ? 115 ILE   B CG1 1 
ATOM   1287 C CG2 . ILE   B 2 106 ? -6.759  -14.645 -17.387 1.00 62.12  ? 115 ILE   B CG2 1 
ATOM   1288 C CD1 . ILE   B 2 106 ? -8.886  -15.400 -19.067 1.00 51.88  ? 115 ILE   B CD1 1 
ATOM   1289 N N   . PHE   B 2 107 ? -6.973  -11.282 -16.403 1.00 53.77  ? 116 PHE   B N   1 
ATOM   1290 C CA  . PHE   B 2 107 ? -6.263  -10.946 -15.145 1.00 49.70  ? 116 PHE   B CA  1 
ATOM   1291 C C   . PHE   B 2 107 ? -6.181  -12.209 -14.306 1.00 47.17  ? 116 PHE   B C   1 
ATOM   1292 O O   . PHE   B 2 107 ? -7.258  -12.597 -13.810 1.00 52.46  ? 116 PHE   B O   1 
ATOM   1293 C CB  . PHE   B 2 107 ? -7.042  -9.873  -14.385 1.00 51.90  ? 116 PHE   B CB  1 
ATOM   1294 C CG  . PHE   B 2 107 ? -6.794  -8.472  -14.872 1.00 51.79  ? 116 PHE   B CG  1 
ATOM   1295 C CD1 . PHE   B 2 107 ? -6.104  -8.239  -16.053 1.00 48.91  ? 116 PHE   B CD1 1 
ATOM   1296 C CD2 . PHE   B 2 107 ? -7.254  -7.396  -14.140 1.00 49.46  ? 116 PHE   B CD2 1 
ATOM   1297 C CE1 . PHE   B 2 107 ? -5.869  -6.953  -16.490 1.00 51.75  ? 116 PHE   B CE1 1 
ATOM   1298 C CE2 . PHE   B 2 107 ? -7.017  -6.109  -14.584 1.00 56.05  ? 116 PHE   B CE2 1 
ATOM   1299 C CZ  . PHE   B 2 107 ? -6.329  -5.891  -15.755 1.00 55.10  ? 116 PHE   B CZ  1 
ATOM   1300 N N   . LYS   B 2 108 ? -5.003  -12.844 -14.251 1.00 45.14  ? 117 LYS   B N   1 
ATOM   1301 C CA  . LYS   B 2 108 ? -4.653  -13.956 -13.318 1.00 45.17  ? 117 LYS   B CA  1 
ATOM   1302 C C   . LYS   B 2 108 ? -4.332  -13.372 -11.937 1.00 38.54  ? 117 LYS   B C   1 
ATOM   1303 O O   . LYS   B 2 108 ? -3.356  -12.616 -11.831 1.00 36.25  ? 117 LYS   B O   1 
ATOM   1304 C CB  . LYS   B 2 108 ? -3.430  -14.741 -13.827 1.00 54.20  ? 117 LYS   B CB  1 
ATOM   1305 C CG  . LYS   B 2 108 ? -3.723  -15.970 -14.687 1.00 57.09  ? 117 LYS   B CG  1 
ATOM   1306 C CD  . LYS   B 2 108 ? -2.653  -16.309 -15.739 1.00 56.44  ? 117 LYS   B CD  1 
ATOM   1307 C CE  . LYS   B 2 108 ? -3.276  -16.573 -17.101 1.00 62.45  ? 117 LYS   B CE  1 
ATOM   1308 N NZ  . LYS   B 2 108 ? -2.315  -17.027 -18.141 1.00 62.73  ? 117 LYS   B NZ  1 
ATOM   1309 N N   . THR   B 2 109 ? -5.125  -13.698 -10.920 1.00 39.89  ? 118 THR   B N   1 
ATOM   1310 C CA  . THR   B 2 109 ? -4.983  -13.197 -9.522  1.00 41.27  ? 118 THR   B CA  1 
ATOM   1311 C C   . THR   B 2 109 ? -4.862  -14.415 -8.617  1.00 43.32  ? 118 THR   B C   1 
ATOM   1312 O O   . THR   B 2 109 ? -5.231  -15.510 -9.075  1.00 46.95  ? 118 THR   B O   1 
ATOM   1313 C CB  . THR   B 2 109 ? -6.152  -12.285 -9.093  1.00 40.97  ? 118 THR   B CB  1 
ATOM   1314 O OG1 . THR   B 2 109 ? -7.284  -13.002 -8.595  1.00 36.35  ? 118 THR   B OG1 1 
ATOM   1315 C CG2 . THR   B 2 109 ? -6.640  -11.417 -10.226 1.00 42.80  ? 118 THR   B CG2 1 
ATOM   1316 N N   . LYS   B 2 110 ? -4.369  -14.222 -7.393  1.00 50.01  ? 119 LYS   B N   1 
ATOM   1317 C CA  . LYS   B 2 110 ? -4.207  -15.304 -6.388  1.00 51.57  ? 119 LYS   B CA  1 
ATOM   1318 C C   . LYS   B 2 110 ? -5.591  -15.833 -5.992  1.00 58.24  ? 119 LYS   B C   1 
ATOM   1319 O O   . LYS   B 2 110 ? -5.656  -17.024 -5.594  1.00 61.21  ? 119 LYS   B O   1 
ATOM   1320 C CB  . LYS   B 2 110 ? -3.392  -14.817 -5.182  1.00 53.84  ? 119 LYS   B CB  1 
ATOM   1321 C CG  . LYS   B 2 110 ? -4.064  -13.792 -4.280  1.00 56.57  ? 119 LYS   B CG  1 
ATOM   1322 C CD  . LYS   B 2 110 ? -3.109  -13.119 -3.322  1.00 59.90  ? 119 LYS   B CD  1 
ATOM   1323 C CE  . LYS   B 2 110 ? -3.172  -13.650 -1.904  1.00 67.50  ? 119 LYS   B CE  1 
ATOM   1324 N NZ  . LYS   B 2 110 ? -4.271  -13.022 -1.135  1.00 69.43  ? 119 LYS   B NZ  1 
ATOM   1325 N N   . ASP   B 2 111 ? -6.650  -15.013 -6.142  1.00 58.96  ? 120 ASP   B N   1 
ATOM   1326 C CA  . ASP   B 2 111 ? -8.063  -15.356 -5.804  1.00 51.73  ? 120 ASP   B CA  1 
ATOM   1327 C C   . ASP   B 2 111 ? -8.821  -15.936 -7.008  1.00 49.96  ? 120 ASP   B C   1 
ATOM   1328 O O   . ASP   B 2 111 ? -9.847  -16.612 -6.772  1.00 61.13  ? 120 ASP   B O   1 
ATOM   1329 C CB  . ASP   B 2 111 ? -8.809  -14.135 -5.262  1.00 55.64  ? 120 ASP   B CB  1 
ATOM   1330 C CG  . ASP   B 2 111 ? -8.424  -13.767 -3.840  1.00 56.37  ? 120 ASP   B CG  1 
ATOM   1331 O OD1 . ASP   B 2 111 ? -7.453  -14.361 -3.330  1.00 51.43  ? 120 ASP   B OD1 1 
ATOM   1332 O OD2 . ASP   B 2 111 ? -9.114  -12.904 -3.246  1.00 59.49  ? 120 ASP   B OD2 1 
ATOM   1333 N N   . GLY   B 2 112 ? -8.387  -15.674 -8.244  1.00 47.64  ? 121 GLY   B N   1 
ATOM   1334 C CA  . GLY   B 2 112 ? -9.066  -16.177 -9.454  1.00 46.00  ? 121 GLY   B CA  1 
ATOM   1335 C C   . GLY   B 2 112 ? -8.752  -15.361 -10.691 1.00 47.66  ? 121 GLY   B C   1 
ATOM   1336 O O   . GLY   B 2 112 ? -8.185  -14.268 -10.532 1.00 60.13  ? 121 GLY   B O   1 
ATOM   1337 N N   . ASP   B 2 113 ? -9.129  -15.876 -11.871 1.00 51.01  ? 122 ASP   B N   1 
ATOM   1338 C CA  . ASP   B 2 113 ? -8.962  -15.247 -13.214 1.00 51.31  ? 122 ASP   B CA  1 
ATOM   1339 C C   . ASP   B 2 113 ? -10.156 -14.334 -13.510 1.00 52.88  ? 122 ASP   B C   1 
ATOM   1340 O O   . ASP   B 2 113 ? -11.297 -14.758 -13.221 1.00 48.02  ? 122 ASP   B O   1 
ATOM   1341 C CB  . ASP   B 2 113 ? -8.902  -16.283 -14.338 1.00 52.52  ? 122 ASP   B CB  1 
ATOM   1342 C CG  . ASP   B 2 113 ? -7.611  -17.080 -14.434 1.00 59.06  ? 122 ASP   B CG  1 
ATOM   1343 O OD1 . ASP   B 2 113 ? -6.782  -16.986 -13.505 1.00 63.45  ? 122 ASP   B OD1 1 
ATOM   1344 O OD2 . ASP   B 2 113 ? -7.446  -17.788 -15.455 1.00 64.49  ? 122 ASP   B OD2 1 
ATOM   1345 N N   . ILE   B 2 114 ? -9.899  -13.154 -14.092 1.00 52.47  ? 123 ILE   B N   1 
ATOM   1346 C CA  . ILE   B 2 114 ? -10.931 -12.133 -14.440 1.00 49.63  ? 123 ILE   B CA  1 
ATOM   1347 C C   . ILE   B 2 114 ? -10.779 -11.776 -15.925 1.00 50.15  ? 123 ILE   B C   1 
ATOM   1348 O O   . ILE   B 2 114 ? -9.628  -11.680 -16.407 1.00 40.58  ? 123 ILE   B O   1 
ATOM   1349 C CB  . ILE   B 2 114 ? -10.810 -10.890 -13.532 1.00 49.86  ? 123 ILE   B CB  1 
ATOM   1350 C CG1 . ILE   B 2 114 ? -10.787 -11.258 -12.048 1.00 53.18  ? 123 ILE   B CG1 1 
ATOM   1351 C CG2 . ILE   B 2 114 ? -11.910 -9.885  -13.820 1.00 52.31  ? 123 ILE   B CG2 1 
ATOM   1352 C CD1 . ILE   B 2 114 ? -9.865  -10.379 -11.226 1.00 59.09  ? 123 ILE   B CD1 1 
ATOM   1353 N N   . GLY   B 2 115 ? -11.906 -11.572 -16.620 1.00 50.17  ? 124 GLY   B N   1 
ATOM   1354 C CA  . GLY   B 2 115 ? -11.913 -10.988 -17.971 1.00 45.51  ? 124 GLY   B CA  1 
ATOM   1355 C C   . GLY   B 2 115 ? -11.074 -9.732  -17.975 1.00 46.91  ? 124 GLY   B C   1 
ATOM   1356 O O   . GLY   B 2 115 ? -10.928 -9.083  -16.915 1.00 47.95  ? 124 GLY   B O   1 
ATOM   1357 N N   . ALA   B 2 116 ? -10.491 -9.406  -19.111 1.00 44.66  ? 125 ALA   B N   1 
ATOM   1358 C CA  . ALA   B 2 116 ? -9.741  -8.151  -19.269 1.00 46.02  ? 125 ALA   B CA  1 
ATOM   1359 C C   . ALA   B 2 116 ? -9.863  -7.719  -20.723 1.00 46.54  ? 125 ALA   B C   1 
ATOM   1360 O O   . ALA   B 2 116 ? -9.640  -8.525  -21.619 1.00 46.32  ? 125 ALA   B O   1 
ATOM   1361 C CB  . ALA   B 2 116 ? -8.308  -8.317  -18.851 1.00 46.65  ? 125 ALA   B CB  1 
ATOM   1362 N N   A VAL   B 2 117 ? -10.258 -6.464  -20.943 0.25 46.59  ? 126 VAL   B N   1 
ATOM   1363 N N   B VAL   B 2 117 ? -10.225 -6.452  -20.922 0.25 46.20  ? 126 VAL   B N   1 
ATOM   1364 N N   C VAL   B 2 117 ? -10.258 -6.464  -20.943 0.25 46.59  ? 126 VAL   B N   1 
ATOM   1365 N N   D VAL   B 2 117 ? -10.225 -6.452  -20.922 0.25 46.20  ? 126 VAL   B N   1 
ATOM   1366 C CA  A VAL   B 2 117 ? -10.300 -5.826  -22.290 0.25 48.32  ? 126 VAL   B CA  1 
ATOM   1367 C CA  B VAL   B 2 117 ? -10.313 -5.777  -22.247 0.25 47.64  ? 126 VAL   B CA  1 
ATOM   1368 C CA  C VAL   B 2 117 ? -10.300 -5.826  -22.290 0.25 48.32  ? 126 VAL   B CA  1 
ATOM   1369 C CA  D VAL   B 2 117 ? -10.313 -5.777  -22.247 0.25 47.64  ? 126 VAL   B CA  1 
ATOM   1370 C C   A VAL   B 2 117 ? -9.108  -4.868  -22.387 0.25 48.12  ? 126 VAL   B C   1 
ATOM   1371 C C   B VAL   B 2 117 ? -9.099  -4.850  -22.379 0.25 47.70  ? 126 VAL   B C   1 
ATOM   1372 C C   C VAL   B 2 117 ? -9.108  -4.868  -22.387 0.25 48.12  ? 126 VAL   B C   1 
ATOM   1373 C C   D VAL   B 2 117 ? -9.099  -4.850  -22.379 0.25 47.70  ? 126 VAL   B C   1 
ATOM   1374 O O   A VAL   B 2 117 ? -8.864  -4.130  -21.411 0.25 44.58  ? 126 VAL   B O   1 
ATOM   1375 O O   B VAL   B 2 117 ? -8.829  -4.107  -21.415 0.25 44.24  ? 126 VAL   B O   1 
ATOM   1376 O O   C VAL   B 2 117 ? -8.864  -4.130  -21.411 0.25 44.58  ? 126 VAL   B O   1 
ATOM   1377 O O   D VAL   B 2 117 ? -8.829  -4.107  -21.415 0.25 44.24  ? 126 VAL   B O   1 
ATOM   1378 C CB  A VAL   B 2 117 ? -11.639 -5.109  -22.545 0.25 48.81  ? 126 VAL   B CB  1 
ATOM   1379 C CB  B VAL   B 2 117 ? -11.642 -5.009  -22.371 0.25 47.64  ? 126 VAL   B CB  1 
ATOM   1380 C CB  C VAL   B 2 117 ? -11.639 -5.109  -22.545 0.25 48.81  ? 126 VAL   B CB  1 
ATOM   1381 C CB  D VAL   B 2 117 ? -11.642 -5.009  -22.371 0.25 47.64  ? 126 VAL   B CB  1 
ATOM   1382 C CG1 A VAL   B 2 117 ? -12.817 -6.061  -22.401 0.25 49.17  ? 126 VAL   B CG1 1 
ATOM   1383 C CG1 B VAL   B 2 117 ? -11.512 -3.794  -23.271 0.25 47.24  ? 126 VAL   B CG1 1 
ATOM   1384 C CG1 C VAL   B 2 117 ? -12.817 -6.061  -22.401 0.25 49.17  ? 126 VAL   B CG1 1 
ATOM   1385 C CG1 D VAL   B 2 117 ? -11.512 -3.794  -23.271 0.25 47.24  ? 126 VAL   B CG1 1 
ATOM   1386 C CG2 A VAL   B 2 117 ? -11.813 -3.892  -21.649 0.25 49.04  ? 126 VAL   B CG2 1 
ATOM   1387 C CG2 B VAL   B 2 117 ? -12.775 -5.915  -22.834 0.25 47.90  ? 126 VAL   B CG2 1 
ATOM   1388 C CG2 C VAL   B 2 117 ? -11.813 -3.892  -21.649 0.25 49.04  ? 126 VAL   B CG2 1 
ATOM   1389 C CG2 D VAL   B 2 117 ? -12.775 -5.915  -22.834 0.25 47.90  ? 126 VAL   B CG2 1 
ATOM   1390 N N   . ALA   B 2 118 ? -8.380  -4.918  -23.506 1.00 46.92  ? 127 ALA   B N   1 
ATOM   1391 C CA  . ALA   B 2 118 ? -7.204  -4.050  -23.767 1.00 55.75  ? 127 ALA   B CA  1 
ATOM   1392 C C   . ALA   B 2 118 ? -7.601  -3.053  -24.850 1.00 59.37  ? 127 ALA   B C   1 
ATOM   1393 O O   . ALA   B 2 118 ? -7.424  -3.368  -26.044 1.00 58.24  ? 127 ALA   B O   1 
ATOM   1394 C CB  . ALA   B 2 118 ? -5.994  -4.862  -24.160 1.00 61.97  ? 127 ALA   B CB  1 
ATOM   1395 N N   . LEU   B 2 119 ? -8.241  -1.968  -24.409 1.00 61.90  ? 128 LEU   B N   1 
ATOM   1396 C CA  . LEU   B 2 119 ? -8.622  -0.774  -25.198 1.00 51.78  ? 128 LEU   B CA  1 
ATOM   1397 C C   . LEU   B 2 119 ? -8.224  0.433   -24.351 1.00 50.20  ? 128 LEU   B C   1 
ATOM   1398 O O   . LEU   B 2 119 ? -8.406  0.369   -23.128 1.00 54.80  ? 128 LEU   B O   1 
ATOM   1399 C CB  . LEU   B 2 119 ? -10.123 -0.843  -25.488 1.00 50.11  ? 128 LEU   B CB  1 
ATOM   1400 C CG  . LEU   B 2 119 ? -10.601 -2.139  -26.150 1.00 50.83  ? 128 LEU   B CG  1 
ATOM   1401 C CD1 . LEU   B 2 119 ? -12.117 -2.239  -26.140 1.00 46.87  ? 128 LEU   B CD1 1 
ATOM   1402 C CD2 . LEU   B 2 119 ? -10.087 -2.257  -27.581 1.00 57.00  ? 128 LEU   B CD2 1 
ATOM   1403 N N   . ASP   B 2 120 ? -7.607  1.442   -24.958 1.00 49.14  ? 129 ASP   B N   1 
ATOM   1404 C CA  . ASP   B 2 120 ? -7.072  2.629   -24.251 1.00 51.12  ? 129 ASP   B CA  1 
ATOM   1405 C C   . ASP   B 2 120 ? -8.040  3.781   -24.564 1.00 53.46  ? 129 ASP   B C   1 
ATOM   1406 O O   . ASP   B 2 120 ? -8.475  3.858   -25.718 1.00 60.87  ? 129 ASP   B O   1 
ATOM   1407 C CB  . ASP   B 2 120 ? -5.614  2.843   -24.657 1.00 54.76  ? 129 ASP   B CB  1 
ATOM   1408 C CG  . ASP   B 2 120 ? -4.699  3.450   -23.595 1.00 63.50  ? 129 ASP   B CG  1 
ATOM   1409 O OD1 . ASP   B 2 120 ? -5.164  4.321   -22.812 1.00 65.89  ? 129 ASP   B OD1 1 
ATOM   1410 O OD2 . ASP   B 2 120 ? -3.507  3.059   -23.567 1.00 67.02  ? 129 ASP   B OD2 1 
ATOM   1411 N N   . TYR   B 2 121 ? -8.412  4.580   -23.556 1.00 47.62  ? 130 TYR   B N   1 
ATOM   1412 C CA  . TYR   B 2 121 ? -9.398  5.692   -23.611 1.00 47.07  ? 130 TYR   B CA  1 
ATOM   1413 C C   . TYR   B 2 121 ? -9.161  6.610   -22.414 1.00 47.06  ? 130 TYR   B C   1 
ATOM   1414 O O   . TYR   B 2 121 ? -8.528  6.214   -21.435 1.00 45.74  ? 130 TYR   B O   1 
ATOM   1415 C CB  . TYR   B 2 121 ? -10.838 5.166   -23.576 1.00 47.93  ? 130 TYR   B CB  1 
ATOM   1416 C CG  . TYR   B 2 121 ? -11.364 4.590   -24.868 1.00 53.07  ? 130 TYR   B CG  1 
ATOM   1417 C CD1 . TYR   B 2 121 ? -11.827 5.407   -25.886 1.00 54.94  ? 130 TYR   B CD1 1 
ATOM   1418 C CD2 . TYR   B 2 121 ? -11.425 3.216   -25.069 1.00 57.12  ? 130 TYR   B CD2 1 
ATOM   1419 C CE1 . TYR   B 2 121 ? -12.307 4.875   -27.073 1.00 59.17  ? 130 TYR   B CE1 1 
ATOM   1420 C CE2 . TYR   B 2 121 ? -11.903 2.668   -26.250 1.00 53.91  ? 130 TYR   B CE2 1 
ATOM   1421 C CZ  . TYR   B 2 121 ? -12.341 3.502   -27.260 1.00 56.85  ? 130 TYR   B CZ  1 
ATOM   1422 O OH  . TYR   B 2 121 ? -12.815 2.971   -28.424 1.00 61.49  ? 130 TYR   B OH  1 
ATOM   1423 N N   . PRO   B 2 122 ? -9.701  7.849   -22.403 1.00 47.83  ? 131 PRO   B N   1 
ATOM   1424 C CA  . PRO   B 2 122 ? -9.460  8.751   -21.282 1.00 46.33  ? 131 PRO   B CA  1 
ATOM   1425 C C   . PRO   B 2 122 ? -10.146 8.185   -20.027 1.00 42.60  ? 131 PRO   B C   1 
ATOM   1426 O O   . PRO   B 2 122 ? -11.103 7.446   -20.164 1.00 41.59  ? 131 PRO   B O   1 
ATOM   1427 C CB  . PRO   B 2 122 ? -10.033 10.104  -21.753 1.00 49.94  ? 131 PRO   B CB  1 
ATOM   1428 C CG  . PRO   B 2 122 ? -10.297 9.934   -23.242 1.00 49.52  ? 131 PRO   B CG  1 
ATOM   1429 C CD  . PRO   B 2 122 ? -10.564 8.455   -23.431 1.00 49.85  ? 131 PRO   B CD  1 
ATOM   1430 N N   . ALA   B 2 123 ? -9.643  8.547   -18.848 1.00 39.20  ? 132 ALA   B N   1 
ATOM   1431 C CA  . ALA   B 2 123 ? -10.134 8.066   -17.538 1.00 38.95  ? 132 ALA   B CA  1 
ATOM   1432 C C   . ALA   B 2 123 ? -11.616 8.412   -17.393 1.00 43.86  ? 132 ALA   B C   1 
ATOM   1433 O O   . ALA   B 2 123 ? -12.366 7.605   -16.786 1.00 42.52  ? 132 ALA   B O   1 
ATOM   1434 C CB  . ALA   B 2 123 ? -9.310  8.657   -16.433 1.00 38.60  ? 132 ALA   B CB  1 
ATOM   1435 N N   . GLY   B 2 124 ? -12.042 9.527   -18.000 1.00 45.54  ? 133 GLY   B N   1 
ATOM   1436 C CA  . GLY   B 2 124 ? -13.455 9.942   -18.040 1.00 41.04  ? 133 GLY   B CA  1 
ATOM   1437 C C   . GLY   B 2 124 ? -14.348 8.888   -18.686 1.00 42.20  ? 133 GLY   B C   1 
ATOM   1438 O O   . GLY   B 2 124 ? -15.586 9.062   -18.572 1.00 38.90  ? 133 GLY   B O   1 
ATOM   1439 N N   . THR   B 2 125 ? -13.794 7.860   -19.367 1.00 35.93  ? 134 THR   B N   1 
ATOM   1440 C CA  . THR   B 2 125 ? -14.601 6.772   -19.985 1.00 34.88  ? 134 THR   B CA  1 
ATOM   1441 C C   . THR   B 2 125 ? -14.930 5.706   -18.935 1.00 35.34  ? 134 THR   B C   1 
ATOM   1442 O O   . THR   B 2 125 ? -15.825 4.867   -19.215 1.00 36.88  ? 134 THR   B O   1 
ATOM   1443 C CB  . THR   B 2 125 ? -13.952 6.186   -21.247 1.00 38.63  ? 134 THR   B CB  1 
ATOM   1444 O OG1 . THR   B 2 125 ? -13.283 7.195   -22.000 1.00 44.67  ? 134 THR   B OG1 1 
ATOM   1445 C CG2 . THR   B 2 125 ? -14.964 5.572   -22.184 1.00 36.86  ? 134 THR   B CG2 1 
ATOM   1446 N N   . SER   B 2 126 ? -14.266 5.726   -17.772 1.00 33.67  ? 135 SER   B N   1 
ATOM   1447 C CA  . SER   B 2 126 ? -14.551 4.809   -16.634 1.00 34.16  ? 135 SER   B CA  1 
ATOM   1448 C C   . SER   B 2 126 ? -16.065 4.645   -16.416 1.00 34.67  ? 135 SER   B C   1 
ATOM   1449 O O   . SER   B 2 126 ? -16.718 5.662   -16.126 1.00 36.15  ? 135 SER   B O   1 
ATOM   1450 C CB  . SER   B 2 126 ? -13.937 5.303   -15.373 1.00 34.92  ? 135 SER   B CB  1 
ATOM   1451 O OG  . SER   B 2 126 ? -12.570 4.974   -15.331 1.00 39.92  ? 135 SER   B OG  1 
ATOM   1452 N N   . GLY   B 2 127 ? -16.567 3.407   -16.451 1.00 31.44  ? 136 GLY   B N   1 
ATOM   1453 C CA  . GLY   B 2 127 ? -17.947 3.051   -16.091 1.00 27.79  ? 136 GLY   B CA  1 
ATOM   1454 C C   . GLY   B 2 127 ? -18.669 2.508   -17.281 1.00 28.70  ? 136 GLY   B C   1 
ATOM   1455 O O   . GLY   B 2 127 ? -19.639 1.774   -17.063 1.00 34.21  ? 136 GLY   B O   1 
ATOM   1456 N N   . SER   B 2 128 ? -18.199 2.821   -18.496 1.00 28.05  ? 137 SER   B N   1 
ATOM   1457 C CA  . SER   B 2 128 ? -18.801 2.310   -19.746 1.00 29.24  ? 137 SER   B CA  1 
ATOM   1458 C C   . SER   B 2 128 ? -18.931 0.794   -19.630 1.00 32.44  ? 137 SER   B C   1 
ATOM   1459 O O   . SER   B 2 128 ? -17.978 0.092   -19.269 1.00 31.39  ? 137 SER   B O   1 
ATOM   1460 C CB  . SER   B 2 128 ? -18.018 2.697   -20.978 1.00 31.59  ? 137 SER   B CB  1 
ATOM   1461 O OG  . SER   B 2 128 ? -17.448 3.977   -20.853 1.00 33.15  ? 137 SER   B OG  1 
ATOM   1462 N N   . PRO   B 2 129 ? -20.097 0.236   -20.011 1.00 32.42  ? 138 PRO   B N   1 
ATOM   1463 C CA  . PRO   B 2 129 ? -20.298 -1.206  -19.958 1.00 31.98  ? 138 PRO   B CA  1 
ATOM   1464 C C   . PRO   B 2 129 ? -19.577 -1.997  -21.063 1.00 39.80  ? 138 PRO   B C   1 
ATOM   1465 O O   . PRO   B 2 129 ? -19.258 -1.462  -22.126 1.00 41.61  ? 138 PRO   B O   1 
ATOM   1466 C CB  . PRO   B 2 129 ? -21.826 -1.306  -20.132 1.00 33.47  ? 138 PRO   B CB  1 
ATOM   1467 C CG  . PRO   B 2 129 ? -22.203 -0.126  -21.004 1.00 30.46  ? 138 PRO   B CG  1 
ATOM   1468 C CD  . PRO   B 2 129 ? -21.255 0.963   -20.558 1.00 30.16  ? 138 PRO   B CD  1 
ATOM   1469 N N   . ILE   B 2 130 ? -19.353 -3.276  -20.776 1.00 38.77  ? 139 ILE   B N   1 
ATOM   1470 C CA  . ILE   B 2 130 ? -18.875 -4.342  -21.700 1.00 36.42  ? 139 ILE   B CA  1 
ATOM   1471 C C   . ILE   B 2 130 ? -20.044 -5.324  -21.880 1.00 36.90  ? 139 ILE   B C   1 
ATOM   1472 O O   . ILE   B 2 130 ? -20.594 -5.740  -20.845 1.00 29.32  ? 139 ILE   B O   1 
ATOM   1473 C CB  . ILE   B 2 130 ? -17.652 -5.029  -21.064 1.00 35.66  ? 139 ILE   B CB  1 
ATOM   1474 C CG1 . ILE   B 2 130 ? -16.517 -4.047  -20.817 1.00 33.28  ? 139 ILE   B CG1 1 
ATOM   1475 C CG2 . ILE   B 2 130 ? -17.185 -6.260  -21.842 1.00 36.95  ? 139 ILE   B CG2 1 
ATOM   1476 C CD1 . ILE   B 2 130 ? -15.789 -4.369  -19.560 1.00 36.93  ? 139 ILE   B CD1 1 
ATOM   1477 N N   . LEU   B 2 131 ? -20.394 -5.695  -23.125 1.00 38.95  ? 140 LEU   B N   1 
ATOM   1478 C CA  . LEU   B 2 131 ? -21.617 -6.490  -23.431 1.00 46.61  ? 140 LEU   B CA  1 
ATOM   1479 C C   . LEU   B 2 131 ? -21.268 -7.860  -24.012 1.00 46.97  ? 140 LEU   B C   1 
ATOM   1480 O O   . LEU   B 2 131 ? -20.192 -7.985  -24.609 1.00 53.59  ? 140 LEU   B O   1 
ATOM   1481 C CB  . LEU   B 2 131 ? -22.483 -5.726  -24.443 1.00 53.74  ? 140 LEU   B CB  1 
ATOM   1482 C CG  . LEU   B 2 131 ? -22.671 -4.233  -24.192 1.00 50.39  ? 140 LEU   B CG  1 
ATOM   1483 C CD1 . LEU   B 2 131 ? -23.603 -3.644  -25.247 1.00 50.07  ? 140 LEU   B CD1 1 
ATOM   1484 C CD2 . LEU   B 2 131 ? -23.196 -3.988  -22.781 1.00 48.53  ? 140 LEU   B CD2 1 
ATOM   1485 N N   . ASP   B 2 132 ? -22.202 -8.808  -23.889 1.00 46.35  ? 141 ASP   B N   1 
ATOM   1486 C CA  . ASP   B 2 132 ? -22.199 -10.119 -24.586 1.00 55.93  ? 141 ASP   B CA  1 
ATOM   1487 C C   . ASP   B 2 132 ? -23.068 -10.014 -25.850 1.00 62.79  ? 141 ASP   B C   1 
ATOM   1488 O O   . ASP   B 2 132 ? -23.689 -8.939  -26.063 1.00 54.71  ? 141 ASP   B O   1 
ATOM   1489 C CB  . ASP   B 2 132 ? -22.645 -11.244 -23.643 1.00 54.94  ? 141 ASP   B CB  1 
ATOM   1490 C CG  . ASP   B 2 132 ? -24.126 -11.275 -23.296 1.00 56.14  ? 141 ASP   B CG  1 
ATOM   1491 O OD1 . ASP   B 2 132 ? -24.880 -10.449 -23.832 1.00 54.21  ? 141 ASP   B OD1 1 
ATOM   1492 O OD2 . ASP   B 2 132 ? -24.516 -12.136 -22.481 1.00 56.14  ? 141 ASP   B OD2 1 
ATOM   1493 N N   . LYS   B 2 133 ? -23.145 -11.113 -26.618 1.00 68.03  ? 142 LYS   B N   1 
ATOM   1494 C CA  . LYS   B 2 133 ? -23.819 -11.204 -27.948 1.00 68.58  ? 142 LYS   B CA  1 
ATOM   1495 C C   . LYS   B 2 133 ? -25.330 -10.929 -27.808 1.00 65.00  ? 142 LYS   B C   1 
ATOM   1496 O O   . LYS   B 2 133 ? -25.986 -10.743 -28.848 1.00 63.79  ? 142 LYS   B O   1 
ATOM   1497 C CB  . LYS   B 2 133 ? -23.503 -12.557 -28.605 1.00 66.62  ? 142 LYS   B CB  1 
ATOM   1498 C CG  . LYS   B 2 133 ? -22.137 -12.633 -29.283 1.00 69.81  ? 142 LYS   B CG  1 
ATOM   1499 C CD  . LYS   B 2 133 ? -21.494 -14.011 -29.260 1.00 73.65  ? 142 LYS   B CD  1 
ATOM   1500 C CE  . LYS   B 2 133 ? -20.158 -14.062 -29.981 1.00 74.79  ? 142 LYS   B CE  1 
ATOM   1501 N NZ  . LYS   B 2 133 ? -19.602 -15.440 -30.079 1.00 73.30  ? 142 LYS   B NZ  1 
ATOM   1502 N N   . CYS   B 2 134 ? -25.867 -10.869 -26.584 1.00 55.45  ? 143 CYS   B N   1 
ATOM   1503 C CA  . CYS   B 2 134 ? -27.307 -10.603 -26.329 1.00 54.46  ? 143 CYS   B CA  1 
ATOM   1504 C C   . CYS   B 2 134 ? -27.524 -9.230  -25.683 1.00 49.66  ? 143 CYS   B C   1 
ATOM   1505 O O   . CYS   B 2 134 ? -28.623 -9.020  -25.122 1.00 44.92  ? 143 CYS   B O   1 
ATOM   1506 C CB  . CYS   B 2 134 ? -27.893 -11.682 -25.439 1.00 56.83  ? 143 CYS   B CB  1 
ATOM   1507 S SG  . CYS   B 2 134 ? -27.697 -13.321 -26.163 1.00 62.14  ? 143 CYS   B SG  1 
ATOM   1508 N N   . GLY   B 2 135 ? -26.533 -8.334  -25.781 1.00 47.69  ? 144 GLY   B N   1 
ATOM   1509 C CA  . GLY   B 2 135 ? -26.548 -6.996  -25.151 1.00 50.23  ? 144 GLY   B CA  1 
ATOM   1510 C C   . GLY   B 2 135 ? -26.765 -7.018  -23.637 1.00 45.99  ? 144 GLY   B C   1 
ATOM   1511 O O   . GLY   B 2 135 ? -27.342 -6.049  -23.115 1.00 51.57  ? 144 GLY   B O   1 
ATOM   1512 N N   . ARG   B 2 136 ? -26.289 -8.049  -22.937 1.00 50.70  ? 145 ARG   B N   1 
ATOM   1513 C CA  . ARG   B 2 136 ? -26.338 -8.143  -21.449 1.00 50.84  ? 145 ARG   B CA  1 
ATOM   1514 C C   . ARG   B 2 136 ? -25.022 -7.601  -20.888 1.00 47.66  ? 145 ARG   B C   1 
ATOM   1515 O O   . ARG   B 2 136 ? -23.967 -7.902  -21.484 1.00 48.08  ? 145 ARG   B O   1 
ATOM   1516 C CB  . ARG   B 2 136 ? -26.657 -9.579  -21.032 1.00 50.85  ? 145 ARG   B CB  1 
ATOM   1517 C CG  . ARG   B 2 136 ? -28.148 -9.867  -21.084 1.00 56.55  ? 145 ARG   B CG  1 
ATOM   1518 C CD  . ARG   B 2 136 ? -28.539 -11.219 -20.543 1.00 58.31  ? 145 ARG   B CD  1 
ATOM   1519 N NE  . ARG   B 2 136 ? -28.220 -12.211 -21.549 1.00 66.47  ? 145 ARG   B NE  1 
ATOM   1520 C CZ  . ARG   B 2 136 ? -27.677 -13.398 -21.313 1.00 76.11  ? 145 ARG   B CZ  1 
ATOM   1521 N NH1 . ARG   B 2 136 ? -27.366 -13.776 -20.081 1.00 76.74  ? 145 ARG   B NH1 1 
ATOM   1522 N NH2 . ARG   B 2 136 ? -27.447 -14.209 -22.329 1.00 82.51  ? 145 ARG   B NH2 1 
ATOM   1523 N N   . VAL   B 2 137 ? -25.064 -6.780  -19.831 1.00 45.32  ? 146 VAL   B N   1 
ATOM   1524 C CA  . VAL   B 2 137 ? -23.814 -6.127  -19.331 1.00 45.04  ? 146 VAL   B CA  1 
ATOM   1525 C C   . VAL   B 2 137 ? -23.065 -7.175  -18.507 1.00 43.55  ? 146 VAL   B C   1 
ATOM   1526 O O   . VAL   B 2 137 ? -23.646 -7.694  -17.555 1.00 43.91  ? 146 VAL   B O   1 
ATOM   1527 C CB  . VAL   B 2 137 ? -24.026 -4.831  -18.528 1.00 42.60  ? 146 VAL   B CB  1 
ATOM   1528 C CG1 . VAL   B 2 137 ? -22.698 -4.148  -18.254 1.00 46.49  ? 146 VAL   B CG1 1 
ATOM   1529 C CG2 . VAL   B 2 137 ? -24.986 -3.866  -19.205 1.00 46.86  ? 146 VAL   B CG2 1 
ATOM   1530 N N   . ILE   B 2 138 ? -21.829 -7.471  -18.897 1.00 47.35  ? 147 ILE   B N   1 
ATOM   1531 C CA  . ILE   B 2 138 ? -20.946 -8.463  -18.212 1.00 45.16  ? 147 ILE   B CA  1 
ATOM   1532 C C   . ILE   B 2 138 ? -19.926 -7.710  -17.339 1.00 41.94  ? 147 ILE   B C   1 
ATOM   1533 O O   . ILE   B 2 138 ? -19.104 -8.379  -16.704 1.00 36.62  ? 147 ILE   B O   1 
ATOM   1534 C CB  . ILE   B 2 138 ? -20.276 -9.419  -19.225 1.00 41.51  ? 147 ILE   B CB  1 
ATOM   1535 C CG1 . ILE   B 2 138 ? -19.508 -8.680  -20.314 1.00 41.69  ? 147 ILE   B CG1 1 
ATOM   1536 C CG2 . ILE   B 2 138 ? -21.279 -10.374 -19.834 1.00 41.81  ? 147 ILE   B CG2 1 
ATOM   1537 C CD1 . ILE   B 2 138 ? -18.625 -9.603  -21.127 1.00 44.83  ? 147 ILE   B CD1 1 
ATOM   1538 N N   . GLY   B 2 139 ? -19.993 -6.380  -17.277 1.00 36.15  ? 148 GLY   B N   1 
ATOM   1539 C CA  . GLY   B 2 139 ? -19.262 -5.631  -16.249 1.00 37.45  ? 148 GLY   B CA  1 
ATOM   1540 C C   . GLY   B 2 139 ? -18.803 -4.277  -16.740 1.00 38.09  ? 148 GLY   B C   1 
ATOM   1541 O O   . GLY   B 2 139 ? -19.167 -3.855  -17.828 1.00 38.19  ? 148 GLY   B O   1 
ATOM   1542 N N   . LEU   B 2 140 ? -18.008 -3.590  -15.952 1.00 35.13  ? 149 LEU   B N   1 
ATOM   1543 C CA  . LEU   B 2 140 ? -17.742 -2.186  -16.255 1.00 36.75  ? 149 LEU   B CA  1 
ATOM   1544 C C   . LEU   B 2 140 ? -16.270 -2.045  -16.551 1.00 38.43  ? 149 LEU   B C   1 
ATOM   1545 O O   . LEU   B 2 140 ? -15.438 -2.803  -15.963 1.00 37.98  ? 149 LEU   B O   1 
ATOM   1546 C CB  . LEU   B 2 140 ? -18.204 -1.310  -15.091 1.00 37.41  ? 149 LEU   B CB  1 
ATOM   1547 C CG  . LEU   B 2 140 ? -19.718 -1.296  -14.878 1.00 36.09  ? 149 LEU   B CG  1 
ATOM   1548 C CD1 . LEU   B 2 140 ? -20.110 -0.147  -13.955 1.00 40.53  ? 149 LEU   B CD1 1 
ATOM   1549 C CD2 . LEU   B 2 140 ? -20.461 -1.203  -16.198 1.00 36.24  ? 149 LEU   B CD2 1 
ATOM   1550 N N   . TYR   B 2 141 ? -16.024 -1.157  -17.507 1.00 36.46  ? 150 TYR   B N   1 
ATOM   1551 C CA  . TYR   B 2 141 ? -14.694 -0.837  -18.059 1.00 42.54  ? 150 TYR   B CA  1 
ATOM   1552 C C   . TYR   B 2 141 ? -14.156 0.271   -17.183 1.00 35.81  ? 150 TYR   B C   1 
ATOM   1553 O O   . TYR   B 2 141 ? -14.962 1.153   -16.901 1.00 30.94  ? 150 TYR   B O   1 
ATOM   1554 C CB  . TYR   B 2 141 ? -14.797 -0.409  -19.533 1.00 46.84  ? 150 TYR   B CB  1 
ATOM   1555 C CG  . TYR   B 2 141 ? -13.537 0.210   -20.090 1.00 50.23  ? 150 TYR   B CG  1 
ATOM   1556 C CD1 . TYR   B 2 141 ? -13.388 1.588   -20.165 1.00 49.36  ? 150 TYR   B CD1 1 
ATOM   1557 C CD2 . TYR   B 2 141 ? -12.478 -0.583  -20.514 1.00 50.69  ? 150 TYR   B CD2 1 
ATOM   1558 C CE1 . TYR   B 2 141 ? -12.222 2.161   -20.653 1.00 60.08  ? 150 TYR   B CE1 1 
ATOM   1559 C CE2 . TYR   B 2 141 ? -11.316 -0.026  -21.028 1.00 53.03  ? 150 TYR   B CE2 1 
ATOM   1560 C CZ  . TYR   B 2 141 ? -11.181 1.354   -21.101 1.00 58.93  ? 150 TYR   B CZ  1 
ATOM   1561 O OH  . TYR   B 2 141 ? -10.040 1.926   -21.610 1.00 50.19  ? 150 TYR   B OH  1 
ATOM   1562 N N   . GLY   B 2 142 ? -12.881 0.217   -16.794 1.00 39.35  ? 151 GLY   B N   1 
ATOM   1563 C CA  . GLY   B 2 142 ? -12.178 1.388   -16.227 1.00 40.82  ? 151 GLY   B CA  1 
ATOM   1564 C C   . GLY   B 2 142 ? -11.466 1.130   -14.910 1.00 42.04  ? 151 GLY   B C   1 
ATOM   1565 O O   . GLY   B 2 142 ? -11.101 2.137   -14.254 1.00 44.93  ? 151 GLY   B O   1 
ATOM   1566 N N   . ASN   B 2 143 ? -11.222 -0.137  -14.537 1.00 42.70  ? 152 ASN   B N   1 
ATOM   1567 C CA  . ASN   B 2 143 ? -10.235 -0.485  -13.476 1.00 40.64  ? 152 ASN   B CA  1 
ATOM   1568 C C   . ASN   B 2 143 ? -9.300  -1.599  -13.965 1.00 39.48  ? 152 ASN   B C   1 
ATOM   1569 O O   . ASN   B 2 143 ? -9.744  -2.768  -14.113 1.00 45.17  ? 152 ASN   B O   1 
ATOM   1570 C CB  . ASN   B 2 143 ? -10.918 -0.869  -12.162 1.00 39.52  ? 152 ASN   B CB  1 
ATOM   1571 C CG  . ASN   B 2 143 ? -9.993  -0.817  -10.966 1.00 39.55  ? 152 ASN   B CG  1 
ATOM   1572 O OD1 . ASN   B 2 143 ? -9.153  0.086   -10.828 1.00 38.02  ? 152 ASN   B OD1 1 
ATOM   1573 N ND2 . ASN   B 2 143 ? -10.167 -1.774  -10.074 1.00 39.79  ? 152 ASN   B ND2 1 
ATOM   1574 N N   . GLY   B 2 144 ? -8.043  -1.228  -14.186 1.00 44.30  ? 153 GLY   B N   1 
ATOM   1575 C CA  . GLY   B 2 144 ? -6.903  -2.142  -14.379 1.00 42.68  ? 153 GLY   B CA  1 
ATOM   1576 C C   . GLY   B 2 144 ? -5.586  -1.387  -14.320 1.00 47.05  ? 153 GLY   B C   1 
ATOM   1577 O O   . GLY   B 2 144 ? -5.363  -0.593  -13.360 1.00 45.47  ? 153 GLY   B O   1 
ATOM   1578 N N   . VAL   B 2 145 ? -4.749  -1.596  -15.333 1.00 47.37  ? 154 VAL   B N   1 
ATOM   1579 C CA  . VAL   B 2 145 ? -3.274  -1.535  -15.181 1.00 47.87  ? 154 VAL   B CA  1 
ATOM   1580 C C   . VAL   B 2 145 ? -2.659  -0.995  -16.484 1.00 53.95  ? 154 VAL   B C   1 
ATOM   1581 O O   . VAL   B 2 145 ? -3.272  -1.161  -17.578 1.00 48.85  ? 154 VAL   B O   1 
ATOM   1582 C CB  . VAL   B 2 145 ? -2.774  -2.932  -14.728 1.00 55.03  ? 154 VAL   B CB  1 
ATOM   1583 C CG1 . VAL   B 2 145 ? -2.858  -4.003  -15.805 1.00 50.50  ? 154 VAL   B CG1 1 
ATOM   1584 C CG2 . VAL   B 2 145 ? -1.380  -2.896  -14.118 1.00 60.80  ? 154 VAL   B CG2 1 
ATOM   1585 N N   . VAL   B 2 146 ? -1.542  -0.274  -16.337 1.00 54.47  ? 155 VAL   B N   1 
ATOM   1586 C CA  . VAL   B 2 146 ? -0.645  0.185   -17.432 1.00 61.75  ? 155 VAL   B CA  1 
ATOM   1587 C C   . VAL   B 2 146 ? 0.452   -0.880  -17.558 1.00 65.65  ? 155 VAL   B C   1 
ATOM   1588 O O   . VAL   B 2 146 ? 1.100   -1.180  -16.543 1.00 63.75  ? 155 VAL   B O   1 
ATOM   1589 C CB  . VAL   B 2 146 ? -0.125  1.594   -17.095 1.00 69.30  ? 155 VAL   B CB  1 
ATOM   1590 C CG1 . VAL   B 2 146 ? 0.960   2.057   -18.053 1.00 75.30  ? 155 VAL   B CG1 1 
ATOM   1591 C CG2 . VAL   B 2 146 ? -1.279  2.595   -17.041 1.00 67.98  ? 155 VAL   B CG2 1 
ATOM   1592 N N   A ILE   B 2 147 ? 0.634   -1.443  -18.761 0.25 67.70  ? 156 ILE   B N   1 
ATOM   1593 N N   B ILE   B 2 147 ? 0.634   -1.443  -18.761 0.25 67.70  ? 156 ILE   B N   1 
ATOM   1594 N N   C ILE   B 2 147 ? 0.635   -1.440  -18.761 0.25 66.27  ? 156 ILE   B N   1 
ATOM   1595 N N   D ILE   B 2 147 ? 0.635   -1.440  -18.761 0.25 66.27  ? 156 ILE   B N   1 
ATOM   1596 C CA  A ILE   B 2 147 ? 1.504   -2.634  -19.018 0.25 68.34  ? 156 ILE   B CA  1 
ATOM   1597 C CA  B ILE   B 2 147 ? 1.504   -2.634  -19.018 0.25 68.34  ? 156 ILE   B CA  1 
ATOM   1598 C CA  C ILE   B 2 147 ? 1.559   -2.585  -19.028 0.25 65.86  ? 156 ILE   B CA  1 
ATOM   1599 C CA  D ILE   B 2 147 ? 1.559   -2.585  -19.028 0.25 65.86  ? 156 ILE   B CA  1 
ATOM   1600 C C   A ILE   B 2 147 ? 2.828   -2.186  -19.650 0.25 70.09  ? 156 ILE   B C   1 
ATOM   1601 C C   B ILE   B 2 147 ? 2.828   -2.186  -19.650 0.25 70.09  ? 156 ILE   B C   1 
ATOM   1602 C C   C ILE   B 2 147 ? 2.859   -2.055  -19.642 0.25 66.56  ? 156 ILE   B C   1 
ATOM   1603 C C   D ILE   B 2 147 ? 2.859   -2.055  -19.642 0.25 66.56  ? 156 ILE   B C   1 
ATOM   1604 O O   A ILE   B 2 147 ? 2.971   -0.984  -19.936 0.25 68.94  ? 156 ILE   B O   1 
ATOM   1605 O O   B ILE   B 2 147 ? 2.971   -0.984  -19.936 0.25 68.94  ? 156 ILE   B O   1 
ATOM   1606 O O   C ILE   B 2 147 ? 2.880   -0.883  -20.057 0.25 65.28  ? 156 ILE   B O   1 
ATOM   1607 O O   D ILE   B 2 147 ? 2.880   -0.883  -20.057 0.25 65.28  ? 156 ILE   B O   1 
ATOM   1608 C CB  A ILE   B 2 147 ? 0.781   -3.677  -19.895 0.25 69.27  ? 156 ILE   B CB  1 
ATOM   1609 C CB  B ILE   B 2 147 ? 0.781   -3.677  -19.895 0.25 69.27  ? 156 ILE   B CB  1 
ATOM   1610 C CB  C ILE   B 2 147 ? 0.891   -3.647  -19.927 0.25 66.79  ? 156 ILE   B CB  1 
ATOM   1611 C CB  D ILE   B 2 147 ? 0.891   -3.647  -19.927 0.25 66.79  ? 156 ILE   B CB  1 
ATOM   1612 C CG1 A ILE   B 2 147 ? 0.412   -3.120  -21.273 0.25 69.24  ? 156 ILE   B CG1 1 
ATOM   1613 C CG1 B ILE   B 2 147 ? 0.412   -3.120  -21.273 0.25 69.24  ? 156 ILE   B CG1 1 
ATOM   1614 C CG1 C ILE   B 2 147 ? 0.581   -3.108  -21.326 0.25 66.80  ? 156 ILE   B CG1 1 
ATOM   1615 C CG1 D ILE   B 2 147 ? 0.581   -3.108  -21.326 0.25 66.80  ? 156 ILE   B CG1 1 
ATOM   1616 C CG2 A ILE   B 2 147 ? -0.435  -4.239  -19.174 0.25 69.73  ? 156 ILE   B CG2 1 
ATOM   1617 C CG2 B ILE   B 2 147 ? -0.435  -4.239  -19.174 0.25 69.73  ? 156 ILE   B CG2 1 
ATOM   1618 C CG2 C ILE   B 2 147 ? -0.350  -4.216  -19.259 0.25 67.26  ? 156 ILE   B CG2 1 
ATOM   1619 C CG2 D ILE   B 2 147 ? -0.350  -4.216  -19.259 0.25 67.26  ? 156 ILE   B CG2 1 
ATOM   1620 C CD1 A ILE   B 2 147 ? -0.081  -4.169  -22.248 0.25 67.09  ? 156 ILE   B CD1 1 
ATOM   1621 C CD1 B ILE   B 2 147 ? -0.081  -4.169  -22.248 0.25 67.09  ? 156 ILE   B CD1 1 
ATOM   1622 C CD1 C ILE   B 2 147 ? -0.022  -4.136  -22.261 0.25 64.79  ? 156 ILE   B CD1 1 
ATOM   1623 C CD1 D ILE   B 2 147 ? -0.022  -4.136  -22.261 0.25 64.79  ? 156 ILE   B CD1 1 
ATOM   1624 N N   A LYS   B 2 148 ? 3.747   -3.140  -19.849 0.25 73.60  ? 157 LYS   B N   1 
ATOM   1625 N N   B LYS   B 2 148 ? 3.747   -3.140  -19.849 0.25 73.60  ? 157 LYS   B N   1 
ATOM   1626 N N   C LYS   B 2 148 ? 3.895   -2.901  -19.676 0.25 68.65  ? 157 LYS   B N   1 
ATOM   1627 N N   D LYS   B 2 148 ? 3.895   -2.901  -19.676 0.25 68.65  ? 157 LYS   B N   1 
ATOM   1628 C CA  A LYS   B 2 148 ? 5.111   -2.942  -20.414 0.25 74.87  ? 157 LYS   B CA  1 
ATOM   1629 C CA  B LYS   B 2 148 ? 5.111   -2.942  -20.414 0.25 74.87  ? 157 LYS   B CA  1 
ATOM   1630 C CA  C LYS   B 2 148 ? 5.239   -2.623  -20.255 0.25 69.71  ? 157 LYS   B CA  1 
ATOM   1631 C CA  D LYS   B 2 148 ? 5.239   -2.623  -20.255 0.25 69.71  ? 157 LYS   B CA  1 
ATOM   1632 C C   A LYS   B 2 148 ? 5.100   -1.810  -21.449 0.25 75.12  ? 157 LYS   B C   1 
ATOM   1633 C C   B LYS   B 2 148 ? 5.100   -1.810  -21.449 0.25 75.12  ? 157 LYS   B C   1 
ATOM   1634 C C   C LYS   B 2 148 ? 5.139   -1.592  -21.385 0.25 71.58  ? 157 LYS   B C   1 
ATOM   1635 C C   D LYS   B 2 148 ? 5.139   -1.592  -21.385 0.25 71.58  ? 157 LYS   B C   1 
ATOM   1636 O O   A LYS   B 2 148 ? 6.011   -0.960  -21.393 0.25 79.49  ? 157 LYS   B O   1 
ATOM   1637 O O   B LYS   B 2 148 ? 6.011   -0.960  -21.393 0.25 79.49  ? 157 LYS   B O   1 
ATOM   1638 O O   C LYS   B 2 148 ? 5.955   -0.648  -21.388 0.25 75.18  ? 157 LYS   B O   1 
ATOM   1639 O O   D LYS   B 2 148 ? 5.955   -0.648  -21.388 0.25 75.18  ? 157 LYS   B O   1 
ATOM   1640 C CB  A LYS   B 2 148 ? 5.610   -4.245  -21.051 0.25 76.53  ? 157 LYS   B CB  1 
ATOM   1641 C CB  B LYS   B 2 148 ? 5.610   -4.245  -21.051 0.25 76.53  ? 157 LYS   B CB  1 
ATOM   1642 C CB  C LYS   B 2 148 ? 5.859   -3.933  -20.751 0.25 69.90  ? 157 LYS   B CB  1 
ATOM   1643 C CB  D LYS   B 2 148 ? 5.859   -3.933  -20.751 0.25 69.90  ? 157 LYS   B CB  1 
ATOM   1644 C CG  A LYS   B 2 148 ? 5.804   -5.411  -20.088 0.25 77.74  ? 157 LYS   B CG  1 
ATOM   1645 C CG  B LYS   B 2 148 ? 5.804   -5.411  -20.088 0.25 77.74  ? 157 LYS   B CG  1 
ATOM   1646 C CG  C LYS   B 2 148 ? 4.970   -5.163  -20.589 0.25 70.75  ? 157 LYS   B CG  1 
ATOM   1647 C CG  D LYS   B 2 148 ? 4.970   -5.163  -20.589 0.25 70.75  ? 157 LYS   B CG  1 
ATOM   1648 C CD  A LYS   B 2 148 ? 5.642   -6.781  -20.731 0.25 77.43  ? 157 LYS   B CD  1 
ATOM   1649 C CD  B LYS   B 2 148 ? 5.642   -6.781  -20.731 0.25 77.43  ? 157 LYS   B CD  1 
ATOM   1650 C CD  C LYS   B 2 148 ? 3.904   -5.324  -21.658 0.25 68.84  ? 157 LYS   B CD  1 
ATOM   1651 C CD  D LYS   B 2 148 ? 3.904   -5.324  -21.658 0.25 68.84  ? 157 LYS   B CD  1 
ATOM   1652 C CE  A LYS   B 2 148 ? 6.613   -7.038  -21.864 0.25 76.46  ? 157 LYS   B CE  1 
ATOM   1653 C CE  B LYS   B 2 148 ? 6.613   -7.038  -21.864 0.25 76.46  ? 157 LYS   B CE  1 
ATOM   1654 C CE  C LYS   B 2 148 ? 4.280   -6.333  -22.723 0.25 67.73  ? 157 LYS   B CE  1 
ATOM   1655 C CE  D LYS   B 2 148 ? 4.280   -6.333  -22.723 0.25 67.73  ? 157 LYS   B CE  1 
ATOM   1656 N NZ  A LYS   B 2 148 ? 8.017   -7.043  -21.389 0.25 76.40  ? 157 LYS   B NZ  1 
ATOM   1657 N NZ  B LYS   B 2 148 ? 8.017   -7.043  -21.389 0.25 76.40  ? 157 LYS   B NZ  1 
ATOM   1658 N NZ  C LYS   B 2 148 ? 3.106   -6.744  -23.529 0.25 67.18  ? 157 LYS   B NZ  1 
ATOM   1659 N NZ  D LYS   B 2 148 ? 3.106   -6.744  -23.529 0.25 67.18  ? 157 LYS   B NZ  1 
ATOM   1660 N N   A ASN   B 2 149 ? 4.104   -1.800  -22.344 0.25 74.51  ? 158 ASN   B N   1 
ATOM   1661 N N   B ASN   B 2 149 ? 4.104   -1.800  -22.344 0.25 74.51  ? 158 ASN   B N   1 
ATOM   1662 N N   C ASN   B 2 149 ? 4.170   -1.761  -22.292 0.25 72.18  ? 158 ASN   B N   1 
ATOM   1663 N N   D ASN   B 2 149 ? 4.170   -1.761  -22.292 0.25 72.18  ? 158 ASN   B N   1 
ATOM   1664 C CA  A ASN   B 2 149 ? 4.017   -0.905  -23.534 0.25 74.54  ? 158 ASN   B CA  1 
ATOM   1665 C CA  B ASN   B 2 149 ? 4.017   -0.905  -23.534 0.25 74.54  ? 158 ASN   B CA  1 
ATOM   1666 C CA  C ASN   B 2 149 ? 3.985   -0.935  -23.520 0.25 73.28  ? 158 ASN   B CA  1 
ATOM   1667 C CA  D ASN   B 2 149 ? 3.985   -0.935  -23.520 0.25 73.28  ? 158 ASN   B CA  1 
ATOM   1668 C C   A ASN   B 2 149 ? 3.811   0.561   -23.128 0.25 73.42  ? 158 ASN   B C   1 
ATOM   1669 C C   B ASN   B 2 149 ? 3.811   0.561   -23.128 0.25 73.42  ? 158 ASN   B C   1 
ATOM   1670 C C   C ASN   B 2 149 ? 3.706   0.534   -23.168 0.25 72.38  ? 158 ASN   B C   1 
ATOM   1671 C C   D ASN   B 2 149 ? 3.706   0.534   -23.168 0.25 72.38  ? 158 ASN   B C   1 
ATOM   1672 O O   A ASN   B 2 149 ? 4.165   1.442   -23.940 0.25 72.07  ? 158 ASN   B O   1 
ATOM   1673 O O   B ASN   B 2 149 ? 4.165   1.442   -23.940 0.25 72.07  ? 158 ASN   B O   1 
ATOM   1674 O O   C ASN   B 2 149 ? 3.899   1.389   -24.057 0.25 70.07  ? 158 ASN   B O   1 
ATOM   1675 O O   D ASN   B 2 149 ? 3.899   1.389   -24.057 0.25 70.07  ? 158 ASN   B O   1 
ATOM   1676 C CB  A ASN   B 2 149 ? 2.871   -1.308  -24.465 0.25 74.52  ? 158 ASN   B CB  1 
ATOM   1677 C CB  B ASN   B 2 149 ? 2.871   -1.308  -24.465 0.25 74.52  ? 158 ASN   B CB  1 
ATOM   1678 C CB  C ASN   B 2 149 ? 2.850   -1.478  -24.391 0.25 74.07  ? 158 ASN   B CB  1 
ATOM   1679 C CB  D ASN   B 2 149 ? 2.850   -1.478  -24.391 0.25 74.07  ? 158 ASN   B CB  1 
ATOM   1680 C CG  A ASN   B 2 149 ? 2.804   -2.799  -24.711 0.25 76.04  ? 158 ASN   B CG  1 
ATOM   1681 C CG  B ASN   B 2 149 ? 2.804   -2.799  -24.711 0.25 76.04  ? 158 ASN   B CG  1 
ATOM   1682 C CG  C ASN   B 2 149 ? 2.983   -2.959  -24.674 0.25 76.45  ? 158 ASN   B CG  1 
ATOM   1683 C CG  D ASN   B 2 149 ? 2.983   -2.959  -24.674 0.25 76.45  ? 158 ASN   B CG  1 
ATOM   1684 O OD1 A ASN   B 2 149 ? 3.797   -3.509  -24.554 0.25 76.89  ? 158 ASN   B OD1 1 
ATOM   1685 O OD1 B ASN   B 2 149 ? 3.797   -3.509  -24.554 0.25 76.89  ? 158 ASN   B OD1 1 
ATOM   1686 O OD1 C ASN   B 2 149 ? 4.061   -3.532  -24.522 0.25 77.34  ? 158 ASN   B OD1 1 
ATOM   1687 O OD1 D ASN   B 2 149 ? 4.061   -3.532  -24.522 0.25 77.34  ? 158 ASN   B OD1 1 
ATOM   1688 N ND2 A ASN   B 2 149 ? 1.635   -3.281  -25.099 0.25 76.79  ? 158 ASN   B ND2 1 
ATOM   1689 N ND2 B ASN   B 2 149 ? 1.635   -3.281  -25.099 0.25 76.79  ? 158 ASN   B ND2 1 
ATOM   1690 N ND2 C ASN   B 2 149 ? 1.893   -3.586  -25.083 0.25 78.22  ? 158 ASN   B ND2 1 
ATOM   1691 N ND2 D ASN   B 2 149 ? 1.893   -3.586  -25.083 0.25 78.22  ? 158 ASN   B ND2 1 
ATOM   1692 N N   . GLY   B 2 150 ? 3.249   0.809   -21.940 1.00 73.72  ? 159 GLY   B N   1 
ATOM   1693 C CA  . GLY   B 2 150 ? 2.804   2.153   -21.508 1.00 70.34  ? 159 GLY   B CA  1 
ATOM   1694 C C   . GLY   B 2 150 ? 1.309   2.313   -21.760 1.00 66.45  ? 159 GLY   B C   1 
ATOM   1695 O O   . GLY   B 2 150 ? 0.728   3.350   -21.371 1.00 64.14  ? 159 GLY   B O   1 
ATOM   1696 N N   A SER   B 2 151 ? 0.697   1.305   -22.393 0.25 66.35  ? 160 SER   B N   1 
ATOM   1697 N N   B SER   B 2 151 ? 0.710   1.294   -22.391 0.25 65.05  ? 160 SER   B N   1 
ATOM   1698 N N   C SER   B 2 151 ? 0.697   1.305   -22.393 0.25 66.35  ? 160 SER   B N   1 
ATOM   1699 N N   D SER   B 2 151 ? 0.710   1.294   -22.391 0.25 65.05  ? 160 SER   B N   1 
ATOM   1700 C CA  A SER   B 2 151 ? -0.742  1.262   -22.761 0.25 64.54  ? 160 SER   B CA  1 
ATOM   1701 C CA  B SER   B 2 151 ? -0.725  1.197   -22.765 0.25 62.53  ? 160 SER   B CA  1 
ATOM   1702 C CA  C SER   B 2 151 ? -0.742  1.262   -22.761 0.25 64.54  ? 160 SER   B CA  1 
ATOM   1703 C CA  D SER   B 2 151 ? -0.725  1.197   -22.765 0.25 62.53  ? 160 SER   B CA  1 
ATOM   1704 C C   A SER   B 2 151 ? -1.554  0.664   -21.605 0.25 64.72  ? 160 SER   B C   1 
ATOM   1705 C C   B SER   B 2 151 ? -1.552  0.729   -21.563 0.25 63.53  ? 160 SER   B C   1 
ATOM   1706 C C   C SER   B 2 151 ? -1.554  0.664   -21.605 0.25 64.72  ? 160 SER   B C   1 
ATOM   1707 C C   D SER   B 2 151 ? -1.552  0.729   -21.563 0.25 63.53  ? 160 SER   B C   1 
ATOM   1708 O O   A SER   B 2 151 ? -0.943  0.089   -20.680 0.25 63.44  ? 160 SER   B O   1 
ATOM   1709 O O   B SER   B 2 151 ? -0.946  0.309   -20.556 0.25 62.39  ? 160 SER   B O   1 
ATOM   1710 O O   C SER   B 2 151 ? -0.943  0.089   -20.680 0.25 63.44  ? 160 SER   B O   1 
ATOM   1711 O O   D SER   B 2 151 ? -0.946  0.309   -20.556 0.25 62.39  ? 160 SER   B O   1 
ATOM   1712 C CB  A SER   B 2 151 ? -0.942  0.487   -24.039 0.25 64.45  ? 160 SER   B CB  1 
ATOM   1713 C CB  B SER   B 2 151 ? -0.889  0.255   -23.925 0.25 61.05  ? 160 SER   B CB  1 
ATOM   1714 C CB  C SER   B 2 151 ? -0.942  0.487   -24.039 0.25 64.45  ? 160 SER   B CB  1 
ATOM   1715 C CB  D SER   B 2 151 ? -0.889  0.255   -23.925 0.25 61.05  ? 160 SER   B CB  1 
ATOM   1716 O OG  A SER   B 2 151 ? -1.883  1.134   -24.883 0.25 63.95  ? 160 SER   B OG  1 
ATOM   1717 O OG  B SER   B 2 151 ? -0.290  -0.999  -23.634 0.25 57.92  ? 160 SER   B OG  1 
ATOM   1718 O OG  C SER   B 2 151 ? -1.883  1.134   -24.883 0.25 63.95  ? 160 SER   B OG  1 
ATOM   1719 O OG  D SER   B 2 151 ? -0.290  -0.999  -23.634 0.25 57.92  ? 160 SER   B OG  1 
ATOM   1720 N N   . TYR   B 2 152 ? -2.883  0.779   -21.690 1.00 64.41  ? 161 TYR   B N   1 
ATOM   1721 C CA  . TYR   B 2 152 ? -3.842  0.433   -20.608 1.00 59.79  ? 161 TYR   B CA  1 
ATOM   1722 C C   . TYR   B 2 152 ? -4.580  -0.883  -20.891 1.00 54.18  ? 161 TYR   B C   1 
ATOM   1723 O O   . TYR   B 2 152 ? -5.040  -1.063  -22.015 1.00 52.71  ? 161 TYR   B O   1 
ATOM   1724 C CB  . TYR   B 2 152 ? -4.847  1.583   -20.503 1.00 61.73  ? 161 TYR   B CB  1 
ATOM   1725 C CG  . TYR   B 2 152 ? -5.820  1.434   -19.370 1.00 55.61  ? 161 TYR   B CG  1 
ATOM   1726 C CD1 . TYR   B 2 152 ? -5.374  1.485   -18.063 1.00 53.30  ? 161 TYR   B CD1 1 
ATOM   1727 C CD2 . TYR   B 2 152 ? -7.160  1.185   -19.607 1.00 54.71  ? 161 TYR   B CD2 1 
ATOM   1728 C CE1 . TYR   B 2 152 ? -6.242  1.330   -17.004 1.00 51.12  ? 161 TYR   B CE1 1 
ATOM   1729 C CE2 . TYR   B 2 152 ? -8.045  1.032   -18.556 1.00 59.42  ? 161 TYR   B CE2 1 
ATOM   1730 C CZ  . TYR   B 2 152 ? -7.582  1.105   -17.250 1.00 58.12  ? 161 TYR   B CZ  1 
ATOM   1731 O OH  . TYR   B 2 152 ? -8.434  0.942   -16.199 1.00 66.63  ? 161 TYR   B OH  1 
ATOM   1732 N N   . VAL   B 2 153 ? -4.728  -1.741  -19.873 1.00 53.82  ? 162 VAL   B N   1 
ATOM   1733 C CA  . VAL   B 2 153 ? -5.619  -2.947  -19.867 1.00 49.75  ? 162 VAL   B CA  1 
ATOM   1734 C C   . VAL   B 2 153 ? -6.563  -2.849  -18.660 1.00 44.46  ? 162 VAL   B C   1 
ATOM   1735 O O   . VAL   B 2 153 ? -6.057  -2.798  -17.530 1.00 41.15  ? 162 VAL   B O   1 
ATOM   1736 C CB  . VAL   B 2 153 ? -4.811  -4.264  -19.811 1.00 51.89  ? 162 VAL   B CB  1 
ATOM   1737 C CG1 . VAL   B 2 153 ? -5.696  -5.496  -19.990 1.00 52.81  ? 162 VAL   B CG1 1 
ATOM   1738 C CG2 . VAL   B 2 153 ? -3.673  -4.277  -20.823 1.00 57.78  ? 162 VAL   B CG2 1 
ATOM   1739 N N   . SER   B 2 154 ? -7.877  -2.866  -18.898 1.00 45.79  ? 163 SER   B N   1 
ATOM   1740 C CA  . SER   B 2 154 ? -8.955  -2.776  -17.882 1.00 44.39  ? 163 SER   B CA  1 
ATOM   1741 C C   . SER   B 2 154 ? -9.495  -4.172  -17.602 1.00 42.71  ? 163 SER   B C   1 
ATOM   1742 O O   . SER   B 2 154 ? -9.608  -4.944  -18.567 1.00 40.60  ? 163 SER   B O   1 
ATOM   1743 C CB  . SER   B 2 154 ? -10.096 -1.859  -18.322 1.00 47.21  ? 163 SER   B CB  1 
ATOM   1744 O OG  . SER   B 2 154 ? -11.281 -2.087  -17.550 1.00 39.66  ? 163 SER   B OG  1 
ATOM   1745 N N   . ALA   B 2 155 ? -9.840  -4.437  -16.332 1.00 41.28  ? 164 ALA   B N   1 
ATOM   1746 C CA  . ALA   B 2 155 ? -10.660 -5.584  -15.875 1.00 40.98  ? 164 ALA   B CA  1 
ATOM   1747 C C   . ALA   B 2 155 ? -12.082 -5.482  -16.437 1.00 43.14  ? 164 ALA   B C   1 
ATOM   1748 O O   . ALA   B 2 155 ? -12.646 -4.361  -16.586 1.00 39.35  ? 164 ALA   B O   1 
ATOM   1749 C CB  . ALA   B 2 155 ? -10.699 -5.622  -14.359 1.00 43.58  ? 164 ALA   B CB  1 
ATOM   1750 N N   . ILE   B 2 156 ? -12.680 -6.632  -16.692 1.00 41.19  ? 165 ILE   B N   1 
ATOM   1751 C CA  . ILE   B 2 156 ? -14.153 -6.748  -16.813 1.00 40.14  ? 165 ILE   B CA  1 
ATOM   1752 C C   . ILE   B 2 156 ? -14.690 -6.839  -15.379 1.00 45.89  ? 165 ILE   B C   1 
ATOM   1753 O O   . ILE   B 2 156 ? -14.797 -7.978  -14.874 1.00 41.24  ? 165 ILE   B O   1 
ATOM   1754 C CB  . ILE   B 2 156 ? -14.529 -7.973  -17.662 1.00 37.56  ? 165 ILE   B CB  1 
ATOM   1755 C CG1 . ILE   B 2 156 ? -13.910 -7.901  -19.060 1.00 42.62  ? 165 ILE   B CG1 1 
ATOM   1756 C CG2 . ILE   B 2 156 ? -16.034 -8.131  -17.748 1.00 37.08  ? 165 ILE   B CG2 1 
ATOM   1757 C CD1 . ILE   B 2 156 ? -14.364 -9.022  -19.965 1.00 41.78  ? 165 ILE   B CD1 1 
ATOM   1758 N N   . THR   B 2 157 ? -14.978 -5.695  -14.736 1.00 44.56  ? 166 THR   B N   1 
ATOM   1759 C CA  . THR   B 2 157 ? -15.408 -5.628  -13.313 1.00 37.88  ? 166 THR   B CA  1 
ATOM   1760 C C   . THR   B 2 157 ? -16.911 -5.861  -13.220 1.00 39.65  ? 166 THR   B C   1 
ATOM   1761 O O   . THR   B 2 157 ? -17.655 -4.962  -13.650 1.00 40.27  ? 166 THR   B O   1 
ATOM   1762 C CB  . THR   B 2 157 ? -15.024 -4.303  -12.675 1.00 38.19  ? 166 THR   B CB  1 
ATOM   1763 O OG1 . THR   B 2 157 ? -13.625 -4.251  -12.919 1.00 40.91  ? 166 THR   B OG1 1 
ATOM   1764 C CG2 . THR   B 2 157 ? -15.328 -4.216  -11.197 1.00 38.67  ? 166 THR   B CG2 1 
ATOM   1765 N N   . GLN   B 2 158 ? -17.327 -7.024  -12.694 1.00 40.18  ? 167 GLN   B N   1 
ATOM   1766 C CA  . GLN   B 2 158 ? -18.752 -7.350  -12.444 1.00 36.40  ? 167 GLN   B CA  1 
ATOM   1767 C C   . GLN   B 2 158 ? -18.977 -7.474  -10.934 1.00 41.00  ? 167 GLN   B C   1 
ATOM   1768 O O   . GLN   B 2 158 ? -18.069 -7.954  -10.219 1.00 37.98  ? 167 GLN   B O   1 
ATOM   1769 C CB  . GLN   B 2 158 ? -19.183 -8.621  -13.167 1.00 36.79  ? 167 GLN   B CB  1 
ATOM   1770 C CG  . GLN   B 2 158 ? -20.666 -8.953  -13.011 1.00 38.64  ? 167 GLN   B CG  1 
ATOM   1771 C CD  . GLN   B 2 158 ? -21.580 -7.870  -13.554 1.00 42.79  ? 167 GLN   B CD  1 
ATOM   1772 O OE1 . GLN   B 2 158 ? -21.508 -6.709  -13.155 1.00 43.92  ? 167 GLN   B OE1 1 
ATOM   1773 N NE2 . GLN   B 2 158 ? -22.463 -8.247  -14.472 1.00 40.63  ? 167 GLN   B NE2 1 
ATOM   1774 N N   . GLY   B 2 159 ? -20.149 -7.027  -10.482 1.00 42.73  ? 168 GLY   B N   1 
ATOM   1775 C CA  . GLY   B 2 159 ? -20.619 -7.171  -9.095  1.00 45.03  ? 168 GLY   B CA  1 
ATOM   1776 C C   . GLY   B 2 159 ? -21.455 -8.422  -8.932  1.00 45.05  ? 168 GLY   B C   1 
ATOM   1777 O O   . GLY   B 2 159 ? -21.776 -9.055  -9.927  1.00 41.86  ? 168 GLY   B O   1 
ATOM   1778 N N   . LYS   B 2 160 ? -21.773 -8.773  -7.694  1.00 52.71  ? 169 LYS   B N   1 
ATOM   1779 C CA  . LYS   B 2 160 ? -22.666 -9.903  -7.353  1.00 57.81  ? 169 LYS   B CA  1 
ATOM   1780 C C   . LYS   B 2 160 ? -24.071 -9.321  -7.143  1.00 64.14  ? 169 LYS   B C   1 
ATOM   1781 O O   . LYS   B 2 160 ? -24.176 -8.276  -6.468  1.00 73.09  ? 169 LYS   B O   1 
ATOM   1782 C CB  . LYS   B 2 160 ? -22.102 -10.644 -6.134  1.00 57.92  ? 169 LYS   B CB  1 
ATOM   1783 C CG  . LYS   B 2 160 ? -22.543 -12.095 -6.009  1.00 58.09  ? 169 LYS   B CG  1 
ATOM   1784 C CD  . LYS   B 2 160 ? -22.542 -12.599 -4.588  1.00 58.27  ? 169 LYS   B CD  1 
ATOM   1785 C CE  . LYS   B 2 160 ? -23.630 -13.616 -4.326  1.00 57.14  ? 169 LYS   B CE  1 
ATOM   1786 N NZ  . LYS   B 2 160 ? -23.922 -13.707 -2.878  1.00 59.11  ? 169 LYS   B NZ  1 
ATOM   1787 N N   . ARG   B 2 161 ? -25.091 -9.924  -7.764  1.00 69.03  ? 170 ARG   B N   1 
ATOM   1788 C CA  . ARG   B 2 161 ? -26.534 -9.635  -7.524  1.00 70.02  ? 170 ARG   B CA  1 
ATOM   1789 C C   . ARG   B 2 161 ? -26.965 -10.352 -6.230  1.00 75.02  ? 170 ARG   B C   1 
ATOM   1790 O O   . ARG   B 2 161 ? -26.181 -11.198 -5.741  1.00 85.42  ? 170 ARG   B O   1 
ATOM   1791 C CB  . ARG   B 2 161 ? -27.326 -10.067 -8.765  1.00 68.78  ? 170 ARG   B CB  1 
ATOM   1792 C CG  . ARG   B 2 161 ? -28.809 -9.721  -8.723  1.00 70.67  ? 170 ARG   B CG  1 
ATOM   1793 C CD  . ARG   B 2 161 ? -29.604 -10.131 -9.954  1.00 72.28  ? 170 ARG   B CD  1 
ATOM   1794 N NE  . ARG   B 2 161 ? -31.006 -9.716  -9.840  1.00 69.16  ? 170 ARG   B NE  1 
ATOM   1795 C CZ  . ARG   B 2 161 ? -31.652 -8.884  -10.659 1.00 66.66  ? 170 ARG   B CZ  1 
ATOM   1796 N NH1 . ARG   B 2 161 ? -31.053 -8.344  -11.707 1.00 65.24  ? 170 ARG   B NH1 1 
ATOM   1797 N NH2 . ARG   B 2 161 ? -32.921 -8.603  -10.427 1.00 67.78  ? 170 ARG   B NH2 1 
ATOM   1798 N N   . GLU   B 2 162 ? -28.137 -10.021 -5.669  1.00 74.76  ? 171 GLU   B N   1 
ATOM   1799 C CA  . GLU   B 2 162 ? -28.732 -10.721 -4.491  1.00 75.47  ? 171 GLU   B CA  1 
ATOM   1800 C C   . GLU   B 2 162 ? -30.188 -11.107 -4.783  1.00 73.01  ? 171 GLU   B C   1 
ATOM   1801 O O   . GLU   B 2 162 ? -30.742 -12.034 -4.182  1.00 73.01  ? 171 GLU   B O   1 
ATOM   1802 C CB  . GLU   B 2 162 ? -28.622 -9.841  -3.244  1.00 77.77  ? 171 GLU   B CB  1 
ATOM   1803 C CG  . GLU   B 2 162 ? -27.277 -9.950  -2.542  1.00 84.44  ? 171 GLU   B CG  1 
ATOM   1804 C CD  . GLU   B 2 162 ? -27.083 -11.208 -1.703  1.00 90.22  ? 171 GLU   B CD  1 
ATOM   1805 O OE1 . GLU   B 2 162 ? -27.217 -11.114 -0.464  1.00 85.73  ? 171 GLU   B OE1 1 
ATOM   1806 O OE2 . GLU   B 2 162 ? -26.788 -12.280 -2.283  1.00 89.94  ? 171 GLU   B OE2 1 
HETATM 1807 S S   A DMS   C 3 .   ? -7.820  5.521   -18.353 0.12 94.66  ? 201 DMS   B S   1 
HETATM 1808 S S   B DMS   C 3 .   ? -7.820  5.521   -18.353 0.12 94.66  ? 201 DMS   B S   1 
HETATM 1809 O O   A DMS   C 3 .   ? -6.508  4.884   -18.712 0.12 96.65  ? 201 DMS   B O   1 
HETATM 1810 O O   B DMS   C 3 .   ? -6.508  4.884   -18.712 0.12 96.65  ? 201 DMS   B O   1 
HETATM 1811 C C1  A DMS   C 3 .   ? -8.022  5.280   -16.608 0.12 95.11  ? 201 DMS   B C1  1 
HETATM 1812 C C1  B DMS   C 3 .   ? -8.022  5.280   -16.608 0.12 95.11  ? 201 DMS   B C1  1 
HETATM 1813 C C2  A DMS   C 3 .   ? -9.079  4.393   -18.894 0.12 96.56  ? 201 DMS   B C2  1 
HETATM 1814 C C2  B DMS   C 3 .   ? -9.079  4.393   -18.894 0.12 96.56  ? 201 DMS   B C2  1 
HETATM 1815 S S   A DMS   D 3 .   ? -17.879 11.590  -0.328  0.50 679.53 ? 202 DMS   B S   1 
HETATM 1816 S S   B DMS   D 3 .   ? -17.879 11.590  -0.328  0.50 679.53 ? 202 DMS   B S   1 
HETATM 1817 O O   A DMS   D 3 .   ? -18.332 10.181  -0.586  0.50 671.83 ? 202 DMS   B O   1 
HETATM 1818 O O   B DMS   D 3 .   ? -18.332 10.181  -0.586  0.50 671.83 ? 202 DMS   B O   1 
HETATM 1819 C C1  A DMS   D 3 .   ? -19.350 12.580  -0.322  0.50 687.87 ? 202 DMS   B C1  1 
HETATM 1820 C C1  B DMS   D 3 .   ? -19.350 12.580  -0.322  0.50 687.87 ? 202 DMS   B C1  1 
HETATM 1821 C C2  A DMS   D 3 .   ? -17.201 12.185  -1.858  0.50 668.95 ? 202 DMS   B C2  1 
HETATM 1822 C C2  B DMS   D 3 .   ? -17.201 12.185  -1.858  0.50 668.95 ? 202 DMS   B C2  1 
HETATM 1823 S S   A DMS   E 3 .   ? -7.531  3.717   -13.647 0.12 195.65 ? 203 DMS   B S   1 
HETATM 1824 S S   B DMS   E 3 .   ? -7.531  3.717   -13.647 0.12 195.65 ? 203 DMS   B S   1 
HETATM 1825 O O   A DMS   E 3 .   ? -7.860  2.270   -13.888 0.12 193.97 ? 203 DMS   B O   1 
HETATM 1826 O O   B DMS   E 3 .   ? -7.860  2.270   -13.888 0.12 193.97 ? 203 DMS   B O   1 
HETATM 1827 C C1  A DMS   E 3 .   ? -8.242  4.129   -12.076 0.12 195.18 ? 203 DMS   B C1  1 
HETATM 1828 C C1  B DMS   E 3 .   ? -8.242  4.129   -12.076 0.12 195.18 ? 203 DMS   B C1  1 
HETATM 1829 C C2  A DMS   E 3 .   ? -5.825  3.759   -13.164 0.12 196.25 ? 203 DMS   B C2  1 
HETATM 1830 C C2  B DMS   E 3 .   ? -5.825  3.759   -13.164 0.12 196.25 ? 203 DMS   B C2  1 
HETATM 1831 N N1  C A1BXL F 4 .   ? -8.273  4.167   -14.450 0.38 44.24  ? 204 A1BXL B N1  1 
HETATM 1832 N N1  D A1BXL F 4 .   ? -8.273  4.167   -14.450 0.38 44.24  ? 204 A1BXL B N1  1 
HETATM 1833 N N3  C A1BXL F 4 .   ? -8.306  2.526   -9.739  0.38 41.64  ? 204 A1BXL B N3  1 
HETATM 1834 N N3  D A1BXL F 4 .   ? -8.306  2.526   -9.739  0.38 41.64  ? 204 A1BXL B N3  1 
HETATM 1835 C C4  C A1BXL F 4 .   ? -9.882  3.918   -17.799 0.38 45.59  ? 204 A1BXL B C4  1 
HETATM 1836 C C4  D A1BXL F 4 .   ? -9.882  3.918   -17.799 0.38 45.59  ? 204 A1BXL B C4  1 
HETATM 1837 C C5  C A1BXL F 4 .   ? -8.863  4.310   -18.618 0.38 47.33  ? 204 A1BXL B C5  1 
HETATM 1838 C C5  D A1BXL F 4 .   ? -8.863  4.310   -18.618 0.38 47.33  ? 204 A1BXL B C5  1 
HETATM 1839 C C6  C A1BXL F 4 .   ? -7.613  4.676   -18.076 0.38 46.88  ? 204 A1BXL B C6  1 
HETATM 1840 C C6  D A1BXL F 4 .   ? -7.613  4.676   -18.076 0.38 46.88  ? 204 A1BXL B C6  1 
HETATM 1841 C C7  C A1BXL F 4 .   ? -6.534  5.082   -18.888 0.38 46.81  ? 204 A1BXL B C7  1 
HETATM 1842 C C7  D A1BXL F 4 .   ? -6.534  5.082   -18.888 0.38 46.81  ? 204 A1BXL B C7  1 
HETATM 1843 C C8  C A1BXL F 4 .   ? -5.349  5.408   -18.303 0.38 47.75  ? 204 A1BXL B C8  1 
HETATM 1844 C C8  D A1BXL F 4 .   ? -5.349  5.408   -18.303 0.38 47.75  ? 204 A1BXL B C8  1 
HETATM 1845 C C10 C A1BXL F 4 .   ? -7.422  4.626   -16.676 0.38 46.56  ? 204 A1BXL B C10 1 
HETATM 1846 C C10 D A1BXL F 4 .   ? -7.422  4.626   -16.676 0.38 46.56  ? 204 A1BXL B C10 1 
HETATM 1847 C C13 C A1BXL F 4 .   ? -6.884  2.516   -10.100 0.38 41.18  ? 204 A1BXL B C13 1 
HETATM 1848 C C13 D A1BXL F 4 .   ? -6.884  2.516   -10.100 0.38 41.18  ? 204 A1BXL B C13 1 
HETATM 1849 C C15 C A1BXL F 4 .   ? -8.582  4.106   -11.620 0.38 42.28  ? 204 A1BXL B C15 1 
HETATM 1850 C C15 D A1BXL F 4 .   ? -8.582  4.106   -11.620 0.38 42.28  ? 204 A1BXL B C15 1 
HETATM 1851 O O1  C A1BXL F 4 .   ? -6.790  2.465   -14.370 0.38 45.01  ? 204 A1BXL B O1  1 
HETATM 1852 O O1  D A1BXL F 4 .   ? -6.790  2.465   -14.370 0.38 45.01  ? 204 A1BXL B O1  1 
HETATM 1853 C C1  C A1BXL F 4 .   ? -7.618  3.167   -13.810 0.38 42.23  ? 204 A1BXL B C1  1 
HETATM 1854 C C1  D A1BXL F 4 .   ? -7.618  3.167   -13.810 0.38 42.23  ? 204 A1BXL B C1  1 
HETATM 1855 C C2  C A1BXL F 4 .   ? -8.508  4.215   -15.835 0.38 45.77  ? 204 A1BXL B C2  1 
HETATM 1856 C C2  D A1BXL F 4 .   ? -8.508  4.215   -15.835 0.38 45.77  ? 204 A1BXL B C2  1 
HETATM 1857 C C3  C A1BXL F 4 .   ? -9.708  3.864   -16.408 0.38 44.29  ? 204 A1BXL B C3  1 
HETATM 1858 C C3  D A1BXL F 4 .   ? -9.708  3.864   -16.408 0.38 44.29  ? 204 A1BXL B C3  1 
HETATM 1859 C C9  C A1BXL F 4 .   ? -5.243  5.332   -16.900 0.38 46.84  ? 204 A1BXL B C9  1 
HETATM 1860 C C9  D A1BXL F 4 .   ? -5.243  5.332   -16.900 0.38 46.84  ? 204 A1BXL B C9  1 
HETATM 1861 N N2  C A1BXL F 4 .   ? -6.227  4.959   -16.100 0.38 48.26  ? 204 A1BXL B N2  1 
HETATM 1862 N N2  D A1BXL F 4 .   ? -6.227  4.959   -16.100 0.38 48.26  ? 204 A1BXL B N2  1 
HETATM 1863 C C11 C A1BXL F 4 .   ? -7.968  2.909   -12.351 0.38 43.07  ? 204 A1BXL B C11 1 
HETATM 1864 C C11 D A1BXL F 4 .   ? -7.968  2.909   -12.351 0.38 43.07  ? 204 A1BXL B C11 1 
HETATM 1865 C C12 C A1BXL F 4 .   ? -6.712  2.443   -11.604 0.38 40.67  ? 204 A1BXL B C12 1 
HETATM 1866 C C12 D A1BXL F 4 .   ? -6.712  2.443   -11.604 0.38 40.67  ? 204 A1BXL B C12 1 
HETATM 1867 C C14 C A1BXL F 4 .   ? -8.980  3.749   -10.200 0.38 42.46  ? 204 A1BXL B C14 1 
HETATM 1868 C C14 D A1BXL F 4 .   ? -8.980  3.749   -10.200 0.38 42.46  ? 204 A1BXL B C14 1 
HETATM 1869 S S   C SO4   G 5 .   ? -18.586 11.653  -0.402  0.50 113.81 ? 205 SO4   B S   1 
HETATM 1870 S S   D SO4   G 5 .   ? -18.586 11.653  -0.402  0.50 113.81 ? 205 SO4   B S   1 
HETATM 1871 O O1  C SO4   G 5 .   ? -18.296 11.974  0.972   0.50 111.92 ? 205 SO4   B O1  1 
HETATM 1872 O O1  D SO4   G 5 .   ? -18.296 11.974  0.972   0.50 111.92 ? 205 SO4   B O1  1 
HETATM 1873 O O2  C SO4   G 5 .   ? -17.377 11.735  -1.184  0.50 111.40 ? 205 SO4   B O2  1 
HETATM 1874 O O2  D SO4   G 5 .   ? -17.377 11.735  -1.184  0.50 111.40 ? 205 SO4   B O2  1 
HETATM 1875 O O3  C SO4   G 5 .   ? -19.134 10.320  -0.478  0.50 111.68 ? 205 SO4   B O3  1 
HETATM 1876 O O3  D SO4   G 5 .   ? -19.134 10.320  -0.478  0.50 111.68 ? 205 SO4   B O3  1 
HETATM 1877 O O4  C SO4   G 5 .   ? -19.544 12.592  -0.916  0.50 118.31 ? 205 SO4   B O4  1 
HETATM 1878 O O4  D SO4   G 5 .   ? -19.544 12.592  -0.916  0.50 118.31 ? 205 SO4   B O4  1 
HETATM 1879 S S   C DMS   H 3 .   ? -7.479  12.045  -18.787 0.50 117.24 ? 206 DMS   B S   1 
HETATM 1880 S S   D DMS   H 3 .   ? -7.479  12.045  -18.787 0.50 117.24 ? 206 DMS   B S   1 
HETATM 1881 O O   C DMS   H 3 .   ? -6.296  11.114  -18.756 0.50 116.26 ? 206 DMS   B O   1 
HETATM 1882 O O   D DMS   H 3 .   ? -6.296  11.114  -18.756 0.50 116.26 ? 206 DMS   B O   1 
HETATM 1883 C C1  C DMS   H 3 .   ? -7.430  12.965  -17.268 0.50 112.23 ? 206 DMS   B C1  1 
HETATM 1884 C C1  D DMS   H 3 .   ? -7.430  12.965  -17.268 0.50 112.23 ? 206 DMS   B C1  1 
HETATM 1885 C C2  C DMS   H 3 .   ? -7.037  13.364  -19.889 0.50 112.38 ? 206 DMS   B C2  1 
HETATM 1886 C C2  D DMS   H 3 .   ? -7.037  13.364  -19.889 0.50 112.38 ? 206 DMS   B C2  1 
HETATM 1887 S S   C DMS   I 3 .   ? -4.559  5.227   -12.236 0.38 76.53  ? 207 DMS   B S   1 
HETATM 1888 S S   D DMS   I 3 .   ? -4.559  5.227   -12.236 0.38 76.53  ? 207 DMS   B S   1 
HETATM 1889 O O   C DMS   I 3 .   ? -4.137  5.010   -13.669 0.38 64.17  ? 207 DMS   B O   1 
HETATM 1890 O O   D DMS   I 3 .   ? -4.137  5.010   -13.669 0.38 64.17  ? 207 DMS   B O   1 
HETATM 1891 C C1  C DMS   I 3 .   ? -5.477  6.746   -12.219 0.38 75.74  ? 207 DMS   B C1  1 
HETATM 1892 C C1  D DMS   I 3 .   ? -5.477  6.746   -12.219 0.38 75.74  ? 207 DMS   B C1  1 
HETATM 1893 C C2  C DMS   I 3 .   ? -3.129  5.786   -11.346 0.38 72.05  ? 207 DMS   B C2  1 
HETATM 1894 C C2  D DMS   I 3 .   ? -3.129  5.786   -11.346 0.38 72.05  ? 207 DMS   B C2  1 
HETATM 1895 O O   A HOH   J 6 .   ? -23.443 18.861  -19.224 0.50 49.66  ? 101 HOH   A O   1 
HETATM 1896 O O   B HOH   J 6 .   ? -23.443 18.861  -19.224 0.50 49.66  ? 101 HOH   A O   1 
HETATM 1897 O O   . HOH   J 6 .   ? -1.747  -3.804  -6.237  1.00 48.06  ? 102 HOH   A O   1 
HETATM 1898 O O   C HOH   J 6 .   ? -26.869 1.462   -28.713 0.50 53.87  ? 103 HOH   A O   1 
HETATM 1899 O O   D HOH   J 6 .   ? -26.869 1.462   -28.713 0.50 53.87  ? 103 HOH   A O   1 
HETATM 1900 O O   A HOH   J 6 .   ? -6.867  -8.995  -3.245  0.50 51.78  ? 104 HOH   A O   1 
HETATM 1901 O O   B HOH   J 6 .   ? -6.867  -8.995  -3.245  0.50 51.78  ? 104 HOH   A O   1 
HETATM 1902 O O   A HOH   J 6 .   ? -6.363  2.245   -9.720  0.12 40.66  ? 105 HOH   A O   1 
HETATM 1903 O O   B HOH   J 6 .   ? -6.363  2.245   -9.720  0.12 40.66  ? 105 HOH   A O   1 
HETATM 1904 O O   . HOH   J 6 .   ? -23.912 9.076   -27.433 1.00 31.66  ? 106 HOH   A O   1 
HETATM 1905 O O   . HOH   J 6 .   ? -28.843 15.502  -14.927 1.00 56.30  ? 107 HOH   A O   1 
HETATM 1906 O O   . HOH   J 6 .   ? -28.522 -6.134  -27.992 1.00 55.83  ? 108 HOH   A O   1 
HETATM 1907 O O   . HOH   J 6 .   ? -3.880  -14.590 -25.262 1.00 32.33  ? 109 HOH   A O   1 
HETATM 1908 O O   . HOH   J 6 .   ? -5.240  -10.016 -5.711  1.00 47.20  ? 110 HOH   A O   1 
HETATM 1909 O O   . HOH   J 6 .   ? -29.536 0.729   -29.984 1.00 56.73  ? 111 HOH   A O   1 
HETATM 1910 O O   . HOH   J 6 .   ? -9.589  1.415   -7.196  1.00 42.06  ? 112 HOH   A O   1 
HETATM 1911 O O   A HOH   J 6 .   ? -22.238 -9.407  -34.686 0.50 58.94  ? 113 HOH   A O   1 
HETATM 1912 O O   B HOH   J 6 .   ? -22.238 -9.407  -34.686 0.50 58.94  ? 113 HOH   A O   1 
HETATM 1913 O O   . HOH   J 6 .   ? -30.756 0.639   -22.905 1.00 50.94  ? 114 HOH   A O   1 
HETATM 1914 O O   . HOH   J 6 .   ? -1.191  -14.846 -9.921  1.00 49.93  ? 115 HOH   A O   1 
HETATM 1915 O O   . HOH   J 6 .   ? -3.849  -1.124  -0.419  1.00 50.43  ? 116 HOH   A O   1 
HETATM 1916 O O   . HOH   J 6 .   ? -3.056  -4.098  0.019   1.00 55.72  ? 117 HOH   A O   1 
HETATM 1917 O O   A HOH   J 6 .   ? -27.365 -5.399  -34.594 0.50 65.30  ? 118 HOH   A O   1 
HETATM 1918 O O   B HOH   J 6 .   ? -27.365 -5.399  -34.594 0.50 65.30  ? 118 HOH   A O   1 
HETATM 1919 O O   A HOH   J 6 .   ? 6.435   -5.668  -17.500 0.50 77.05  ? 119 HOH   A O   1 
HETATM 1920 O O   B HOH   J 6 .   ? 6.435   -5.668  -17.500 0.50 77.05  ? 119 HOH   A O   1 
HETATM 1921 O O   . HOH   K 6 .   ? -33.914 1.112   -15.360 1.00 32.69  ? 301 HOH   B O   1 
HETATM 1922 O O   A HOH   K 6 .   ? -20.173 -10.204 -15.698 0.50 77.05  ? 302 HOH   B O   1 
HETATM 1923 O O   B HOH   K 6 .   ? -20.173 -10.204 -15.698 0.50 77.05  ? 302 HOH   B O   1 
HETATM 1924 O O   A HOH   K 6 .   ? -16.164 -9.611  -14.901 0.50 55.97  ? 303 HOH   B O   1 
HETATM 1925 O O   B HOH   K 6 .   ? -16.164 -9.611  -14.901 0.50 55.97  ? 303 HOH   B O   1 
HETATM 1926 O O   A HOH   K 6 .   ? -18.816 -11.716 -25.441 0.50 62.72  ? 304 HOH   B O   1 
HETATM 1927 O O   B HOH   K 6 .   ? -18.816 -11.716 -25.441 0.50 62.72  ? 304 HOH   B O   1 
HETATM 1928 O O   . HOH   K 6 .   ? -34.137 0.559   -3.647  1.00 67.55  ? 305 HOH   B O   1 
HETATM 1929 O O   . HOH   K 6 .   ? -25.713 -8.184  -16.840 1.00 39.99  ? 306 HOH   B O   1 
HETATM 1930 O O   . HOH   K 6 .   ? -17.165 -7.666  -7.858  1.00 42.10  ? 307 HOH   B O   1 
HETATM 1931 O O   . HOH   K 6 .   ? -16.808 -14.855 -16.629 1.00 38.78  ? 308 HOH   B O   1 
HETATM 1932 O O   A HOH   K 6 .   ? -35.016 -6.153  -10.240 0.50 67.66  ? 309 HOH   B O   1 
HETATM 1933 O O   B HOH   K 6 .   ? -35.016 -6.153  -10.240 0.50 67.66  ? 309 HOH   B O   1 
HETATM 1934 O O   . HOH   K 6 .   ? -11.812 -3.565  -10.077 1.00 46.74  ? 310 HOH   B O   1 
HETATM 1935 O O   . HOH   K 6 .   ? -20.843 6.230   -32.349 1.00 66.27  ? 311 HOH   B O   1 
HETATM 1936 O O   . HOH   K 6 .   ? -19.229 14.051  -22.215 1.00 60.71  ? 312 HOH   B O   1 
HETATM 1937 O O   . HOH   K 6 .   ? -30.836 12.421  -19.314 1.00 43.15  ? 313 HOH   B O   1 
HETATM 1938 O O   . HOH   K 6 .   ? -21.233 7.306   0.000   0.50 33.74  ? 314 HOH   B O   1 
HETATM 1939 O O   . HOH   K 6 .   ? -15.796 9.561   -0.913  1.00 41.36  ? 315 HOH   B O   1 
HETATM 1940 O O   A HOH   K 6 .   ? -8.947  2.202   -9.441  0.12 39.41  ? 316 HOH   B O   1 
HETATM 1941 O O   B HOH   K 6 .   ? -8.947  2.202   -9.441  0.12 39.41  ? 316 HOH   B O   1 
HETATM 1942 O O   . HOH   K 6 .   ? -17.246 12.736  -5.729  1.00 43.70  ? 317 HOH   B O   1 
HETATM 1943 O O   A HOH   K 6 .   ? -28.094 -3.665  -22.612 0.50 59.01  ? 318 HOH   B O   1 
HETATM 1944 O O   B HOH   K 6 .   ? -28.094 -3.665  -22.612 0.50 59.01  ? 318 HOH   B O   1 
HETATM 1945 O O   . HOH   K 6 .   ? -27.997 -6.202  -18.668 1.00 40.65  ? 319 HOH   B O   1 
HETATM 1946 O O   C HOH   K 6 .   ? -33.142 11.591  -2.627  0.50 56.09  ? 320 HOH   B O   1 
HETATM 1947 O O   D HOH   K 6 .   ? -33.142 11.591  -2.627  0.50 56.09  ? 320 HOH   B O   1 
HETATM 1948 O O   . HOH   K 6 .   ? -15.008 -4.907  1.440   1.00 33.79  ? 321 HOH   B O   1 
HETATM 1949 O O   A HOH   K 6 .   ? -21.692 -12.332 -13.302 0.50 55.76  ? 322 HOH   B O   1 
HETATM 1950 O O   B HOH   K 6 .   ? -21.692 -12.332 -13.302 0.50 55.76  ? 322 HOH   B O   1 
HETATM 1951 O O   . HOH   K 6 .   ? -12.929 -2.070  -14.612 1.00 44.09  ? 323 HOH   B O   1 
HETATM 1952 O O   . HOH   K 6 .   ? -30.760 12.326  -16.322 1.00 56.78  ? 324 HOH   B O   1 
HETATM 1953 O O   . HOH   K 6 .   ? -19.704 -7.726  -2.579  1.00 44.89  ? 325 HOH   B O   1 
HETATM 1954 O O   A HOH   K 6 .   ? -19.535 -14.180 -22.792 0.50 53.04  ? 326 HOH   B O   1 
HETATM 1955 O O   B HOH   K 6 .   ? -19.535 -14.180 -22.792 0.50 53.04  ? 326 HOH   B O   1 
HETATM 1956 O O   A HOH   K 6 .   ? -20.181 8.549   -25.861 0.50 114.95 ? 327 HOH   B O   1 
HETATM 1957 O O   B HOH   K 6 .   ? -20.181 8.549   -25.861 0.50 114.95 ? 327 HOH   B O   1 
HETATM 1958 O O   A HOH   K 6 .   ? -16.261 20.067  -14.261 0.50 69.67  ? 328 HOH   B O   1 
HETATM 1959 O O   B HOH   K 6 .   ? -16.261 20.067  -14.261 0.50 69.67  ? 328 HOH   B O   1 
HETATM 1960 O O   A HOH   K 6 .   ? -12.362 2.041   -5.820  0.50 61.48  ? 329 HOH   B O   1 
HETATM 1961 O O   B HOH   K 6 .   ? -12.362 2.041   -5.820  0.50 61.48  ? 329 HOH   B O   1 
HETATM 1962 O O   . HOH   K 6 .   ? -0.597  0.140   -13.917 1.00 47.14  ? 330 HOH   B O   1 
HETATM 1963 O O   A HOH   K 6 .   ? -27.745 -6.958  -5.559  0.50 66.29  ? 331 HOH   B O   1 
HETATM 1964 O O   B HOH   K 6 .   ? -27.745 -6.958  -5.559  0.50 66.29  ? 331 HOH   B O   1 
HETATM 1965 O O   . HOH   K 6 .   ? -8.511  -10.928 -7.504  1.00 53.99  ? 332 HOH   B O   1 
HETATM 1966 O O   . HOH   K 6 .   ? -9.220  -6.664  -25.321 1.00 41.76  ? 333 HOH   B O   1 
HETATM 1967 O O   C HOH   K 6 .   ? -15.811 -9.097  -11.913 0.50 46.83  ? 334 HOH   B O   1 
HETATM 1968 O O   D HOH   K 6 .   ? -15.811 -9.097  -11.913 0.50 46.83  ? 334 HOH   B O   1 
HETATM 1969 O O   . HOH   K 6 .   ? -14.078 -6.056  -1.455  1.00 51.53  ? 335 HOH   B O   1 
HETATM 1970 O O   . HOH   K 6 .   ? -23.842 -14.748 -17.632 1.00 55.51  ? 336 HOH   B O   1 
HETATM 1971 O O   . HOH   K 6 .   ? -35.346 4.183   -9.382  1.00 49.63  ? 337 HOH   B O   1 
HETATM 1972 O O   . HOH   K 6 .   ? -21.710 -13.304 -21.710 1.00 45.23  ? 338 HOH   B O   1 
HETATM 1973 O O   . HOH   K 6 .   ? -17.484 -10.596 -16.536 1.00 39.47  ? 339 HOH   B O   1 
HETATM 1974 O O   . HOH   K 6 .   ? -16.284 -14.018 -30.921 1.00 62.54  ? 340 HOH   B O   1 
HETATM 1975 O O   C HOH   K 6 .   ? -21.787 14.081  -1.608  0.50 45.59  ? 341 HOH   B O   1 
HETATM 1976 O O   D HOH   K 6 .   ? -21.787 14.081  -1.608  0.50 45.59  ? 341 HOH   B O   1 
HETATM 1977 O O   . HOH   K 6 .   ? -6.521  -0.856  -10.780 1.00 38.10  ? 342 HOH   B O   1 
HETATM 1978 O O   A HOH   K 6 .   ? -15.516 16.114  -20.363 0.50 66.92  ? 343 HOH   B O   1 
HETATM 1979 O O   B HOH   K 6 .   ? -15.516 16.114  -20.363 0.50 66.92  ? 343 HOH   B O   1 
HETATM 1980 O O   . HOH   K 6 .   ? -2.623  -12.056 -6.649  1.00 50.34  ? 344 HOH   B O   1 
HETATM 1981 O O   A HOH   K 6 .   ? -18.061 -20.738 -22.897 0.50 74.98  ? 345 HOH   B O   1 
HETATM 1982 O O   B HOH   K 6 .   ? -18.061 -20.738 -22.897 0.50 74.98  ? 345 HOH   B O   1 
HETATM 1983 O O   . HOH   K 6 .   ? -17.075 14.709  -30.604 1.00 56.06  ? 346 HOH   B O   1 
HETATM 1984 O O   . HOH   K 6 .   ? -26.231 -5.159  -4.091  1.00 40.95  ? 347 HOH   B O   1 
HETATM 1985 O O   . HOH   K 6 .   ? -14.772 -12.363 -16.440 1.00 39.05  ? 348 HOH   B O   1 
HETATM 1986 O O   . HOH   K 6 .   ? -17.592 15.686  -22.042 1.00 52.02  ? 349 HOH   B O   1 
HETATM 1987 O O   A HOH   K 6 .   ? -7.120  -6.211  0.664   0.50 59.95  ? 350 HOH   B O   1 
HETATM 1988 O O   B HOH   K 6 .   ? -7.120  -6.211  0.664   0.50 59.95  ? 350 HOH   B O   1 
HETATM 1989 O O   A HOH   K 6 .   ? -28.735 -1.164  -19.168 0.50 83.83  ? 351 HOH   B O   1 
HETATM 1990 O O   B HOH   K 6 .   ? -28.735 -1.164  -19.168 0.50 83.83  ? 351 HOH   B O   1 
HETATM 1991 O O   A HOH   K 6 .   ? -21.024 -16.933 -19.558 0.50 77.97  ? 352 HOH   B O   1 
HETATM 1992 O O   B HOH   K 6 .   ? -21.024 -16.933 -19.558 0.50 77.97  ? 352 HOH   B O   1 
HETATM 1993 O O   C HOH   K 6 .   ? -10.949 9.276   -9.929  0.50 43.69  ? 353 HOH   B O   1 
HETATM 1994 O O   D HOH   K 6 .   ? -10.949 9.276   -9.929  0.50 43.69  ? 353 HOH   B O   1 
HETATM 1995 O O   A HOH   K 6 .   ? -21.059 24.545  -16.969 0.50 88.65  ? 354 HOH   B O   1 
HETATM 1996 O O   B HOH   K 6 .   ? -21.059 24.545  -16.969 0.50 88.65  ? 354 HOH   B O   1 
HETATM 1997 O O   . HOH   K 6 .   ? -30.782 4.129   -2.656  1.00 48.07  ? 355 HOH   B O   1 
HETATM 1998 O O   . HOH   K 6 .   ? -11.145 -5.405  -8.289  1.00 48.34  ? 356 HOH   B O   1 
HETATM 1999 O O   . HOH   K 6 .   ? -10.742 22.172  -13.384 1.00 61.48  ? 357 HOH   B O   1 
HETATM 2000 O O   . HOH   K 6 .   ? -7.677  -10.942 -5.423  1.00 48.64  ? 358 HOH   B O   1 
HETATM 2001 O O   . HOH   K 6 .   ? -21.366 1.684   -32.487 1.00 53.41  ? 359 HOH   B O   1 
HETATM 2002 O O   A HOH   K 6 .   ? -9.317  11.900  -18.787 0.50 58.59  ? 360 HOH   B O   1 
HETATM 2003 O O   B HOH   K 6 .   ? -9.317  11.900  -18.787 0.50 58.59  ? 360 HOH   B O   1 
HETATM 2004 O O   . HOH   K 6 .   ? -35.064 -0.233  -7.865  1.00 56.50  ? 361 HOH   B O   1 
HETATM 2005 O O   . HOH   K 6 .   ? -30.581 -7.520  -6.113  1.00 49.86  ? 362 HOH   B O   1 
HETATM 2006 O O   . HOH   K 6 .   ? -19.098 -5.871  -0.669  1.00 56.97  ? 363 HOH   B O   1 
HETATM 2007 O O   . HOH   K 6 .   ? -9.021  7.465   -13.349 1.00 36.85  ? 364 HOH   B O   1 
HETATM 2008 O O   . HOH   K 6 .   ? -32.505 6.587   -4.148  1.00 51.68  ? 365 HOH   B O   1 
HETATM 2009 O O   A HOH   K 6 .   ? -23.926 -8.915  -2.787  0.50 67.18  ? 366 HOH   B O   1 
HETATM 2010 O O   B HOH   K 6 .   ? -23.926 -8.915  -2.787  0.50 67.18  ? 366 HOH   B O   1 
HETATM 2011 O O   C HOH   K 6 .   ? -29.717 -7.245  -20.383 0.50 41.12  ? 367 HOH   B O   1 
HETATM 2012 O O   D HOH   K 6 .   ? -29.717 -7.245  -20.383 0.50 41.12  ? 367 HOH   B O   1 
HETATM 2013 O O   . HOH   K 6 .   ? -11.617 -8.168  1.371   1.00 52.99  ? 368 HOH   B O   1 
HETATM 2014 O O   . HOH   K 6 .   ? -31.567 -10.899 -26.946 0.50 54.26  ? 369 HOH   B O   1 
HETATM 2015 O O   . HOH   K 6 .   ? -29.337 -6.294  -1.085  1.00 37.15  ? 370 HOH   B O   1 
HETATM 2016 O O   C HOH   K 6 .   ? -18.039 -10.539 -6.973  0.50 53.20  ? 371 HOH   B O   1 
HETATM 2017 O O   D HOH   K 6 .   ? -18.039 -10.539 -6.973  0.50 53.20  ? 371 HOH   B O   1 
HETATM 2018 O O   A HOH   K 6 .   ? -11.374 4.089   -5.484  0.50 63.26  ? 372 HOH   B O   1 
HETATM 2019 O O   B HOH   K 6 .   ? -11.374 4.089   -5.484  0.50 63.26  ? 372 HOH   B O   1 
HETATM 2020 O O   . HOH   K 6 .   ? -17.623 27.396  -14.336 1.00 56.40  ? 373 HOH   B O   1 
HETATM 2021 O O   A HOH   K 6 .   ? -31.343 -7.754  -3.604  0.50 65.42  ? 374 HOH   B O   1 
HETATM 2022 O O   B HOH   K 6 .   ? -31.343 -7.754  -3.604  0.50 65.42  ? 374 HOH   B O   1 
HETATM 2023 O O   . HOH   K 6 .   ? -21.233 4.425   0.000   0.50 50.64  ? 375 HOH   B O   1 
HETATM 2024 O O   A HOH   K 6 .   ? -1.372  -10.334 -3.390  0.50 59.21  ? 376 HOH   B O   1 
HETATM 2025 O O   B HOH   K 6 .   ? -1.372  -10.334 -3.390  0.50 59.21  ? 376 HOH   B O   1 
HETATM 2026 O O   . HOH   K 6 .   ? -12.099 15.175  -14.372 1.00 63.75  ? 377 HOH   B O   1 
HETATM 2027 O O   C HOH   K 6 .   ? 1.251   -15.797 -6.065  0.50 46.37  ? 378 HOH   B O   1 
HETATM 2028 O O   D HOH   K 6 .   ? 1.251   -15.797 -6.065  0.50 46.37  ? 378 HOH   B O   1 
# 
