data_7I1Z
# 
_entry.id   7I1Z 
# 
_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   7I1Z         pdb_00007i1z 10.2210/pdb7i1z/pdb 
WWPDB D_1001408214 ?            ?                   
# 
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                        7I1Z 
_pdbx_database_status.status_code                     REL 
_pdbx_database_status.status_code_sf                  REL 
_pdbx_database_status.status_code_mr                  ? 
_pdbx_database_status.status_code_cs                  ? 
_pdbx_database_status.recvd_initial_deposition_date   2025-02-20 
_pdbx_database_status.status_code_nmr_data            ? 
_pdbx_database_status.deposit_site                    RCSB 
_pdbx_database_status.process_site                    RCSB 
_pdbx_database_status.SG_entry                        ? 
_pdbx_database_status.pdb_format_compatible           N 
_pdbx_database_status.methods_development_category    ? 
# 
_pdbx_contact_author.id                 1 
_pdbx_contact_author.email              frankfurt.von-delft@diamond.ac.uk 
_pdbx_contact_author.name_first         Frank 
_pdbx_contact_author.name_last          'von Delft' 
_pdbx_contact_author.role               'principal investigator/group leader' 
_pdbx_contact_author.identifier_ORCID   0000-0003-0378-0017 
_pdbx_contact_author.name_mi            ? 
# 
loop_
_audit_author.name 
_audit_author.pdbx_ordinal 
'Ni, X.'              1  
'Marples, P.G.'       2  
'Godoy, A.S.'         3  
'Koekemoer, L.'       4  
'Aschenbrenner, J.C.' 5  
'Balcomb, B.H.'       6  
'Fairhead, M.'        7  
'Lithgo, R.M.'        8  
'Balaji, G.'          9  
'Phelps, J.'          10 
'Thompson, W.'        11 
'Tomlinson, C.W.E.'   12 
'Wild, C.'            13 
'Winokan, M.'         14 
'Williams, E.P.'      15 
'Chandran, A.V.'      16 
'Walsh, M.A.'         17 
'Fearon, D.'          18 
'von Delft, F.'       19 
# 
_citation.id                        primary 
_citation.title                     'PanDDA analysis group deposition' 
_citation.journal_abbrev            'To Be Published' 
_citation.journal_volume            ? 
_citation.page_first                ? 
_citation.page_last                 ? 
_citation.year                      ? 
_citation.journal_id_ASTM           ? 
_citation.country                   ? 
_citation.journal_id_ISSN           ? 
_citation.journal_id_CSD            0353 
_citation.book_publisher            ? 
_citation.pdbx_database_id_PubMed   ? 
_citation.pdbx_database_id_DOI      ? 
# 
loop_
_citation_author.citation_id 
_citation_author.name 
_citation_author.identifier_ORCID 
_citation_author.ordinal 
primary 'Ni, X.'              ? 1  
primary 'Marples, P.G.'       ? 2  
primary 'Godoy, A.S.'         ? 3  
primary 'Koekemoer, L.'       ? 4  
primary 'Aschenbrenner, J.C.' ? 5  
primary 'Balcomb, B.H.'       ? 6  
primary 'Fairhead, M.'        ? 7  
primary 'Lithgo, R.M.'        ? 8  
primary 'Balaji, G.'          ? 9  
primary 'Phelps, J.'          ? 10 
primary 'Thompson, W.'        ? 11 
primary 'Tomlinson, C.W.E.'   ? 12 
primary 'Wild, C.'            ? 13 
primary 'Winokan, M.'         ? 14 
primary 'Williams, E.P.'      ? 15 
primary 'Chandran, A.V.'      ? 16 
primary 'Walsh, M.A.'         ? 17 
primary 'Fearon, D.'          ? 18 
primary 'von Delft, F.'       ? 19 
# 
loop_
_entity.id 
_entity.type 
_entity.src_method 
_entity.pdbx_description 
_entity.formula_weight 
_entity.pdbx_number_of_molecules 
_entity.pdbx_ec 
_entity.pdbx_mutation 
_entity.pdbx_fragment 
_entity.details 
1 polymer     man 'Serine protease subunit NS2B'                                                                      5067.486  1  
?                           ?    ? ? 
2 polymer     man 'Serine protease NS3'                                                                               18117.629 1  
3.4.21.91,3.6.1.15,3.6.4.13 None ? ? 
3 non-polymer syn 'DIMETHYL SULFOXIDE'                                                                                78.133    4  
?                           ?    ? ? 
4 non-polymer syn '[(3R)-3-aminopyrrolidin-1-yl](2-{[4-(hydroxymethyl)-2-methylquinolin-8-yl]methyl}phenyl)methanone' 375.464   1  
?                           ?    ? ? 
5 water       nat water                                                                                               18.015    96 
?                           ?    ? ? 
# 
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 '[(3R)-3-aminopyrrolidin-1-yl](2-{[4-(hydroxymethyl)-2-methylquinolin-8-yl]methyl}phenyl)methanone' A1BXQ 
5 water                                                                                               HOH   
# 
loop_
_entity_poly_seq.entity_id 
_entity_poly_seq.num 
_entity_poly_seq.mon_id 
_entity_poly_seq.hetero 
1 1   SER n 
1 2   MET n 
1 3   GLY n 
1 4   LYS n 
1 5   SER n 
1 6   VAL n 
1 7   ASP n 
1 8   MET n 
1 9   TYR n 
1 10  ILE n 
1 11  GLU n 
1 12  ARG n 
1 13  ALA n 
1 14  GLY n 
1 15  ASP n 
1 16  ILE n 
1 17  THR n 
1 18  TRP n 
1 19  GLU n 
1 20  LYS n 
1 21  ASP n 
1 22  ALA n 
1 23  GLU n 
1 24  VAL n 
1 25  THR n 
1 26  GLY n 
1 27  ASN n 
1 28  SER n 
1 29  PRO n 
1 30  ARG n 
1 31  LEU n 
1 32  ASP n 
1 33  VAL n 
1 34  ALA n 
1 35  LEU n 
1 36  ASP n 
1 37  GLU n 
1 38  SER n 
1 39  GLY n 
1 40  ASP n 
1 41  PHE n 
1 42  SER n 
1 43  LEU n 
1 44  VAL n 
1 45  GLU n 
1 46  GLU n 
2 1   MET n 
2 2   LYS n 
2 3   GLU n 
2 4   VAL n 
2 5   LYS n 
2 6   LYS n 
2 7   GLY n 
2 8   GLU n 
2 9   THR n 
2 10  THR n 
2 11  ASP n 
2 12  GLY n 
2 13  VAL n 
2 14  TYR n 
2 15  ARG n 
2 16  VAL n 
2 17  MET n 
2 18  THR n 
2 19  ARG n 
2 20  ARG n 
2 21  LEU n 
2 22  LEU n 
2 23  GLY n 
2 24  SER n 
2 25  THR n 
2 26  GLN n 
2 27  VAL n 
2 28  GLY n 
2 29  VAL n 
2 30  GLY n 
2 31  VAL n 
2 32  MET n 
2 33  GLN n 
2 34  GLU n 
2 35  GLY n 
2 36  VAL n 
2 37  PHE n 
2 38  HIS n 
2 39  THR n 
2 40  MET n 
2 41  TRP n 
2 42  HIS n 
2 43  VAL n 
2 44  THR n 
2 45  LYS n 
2 46  GLY n 
2 47  ALA n 
2 48  ALA n 
2 49  LEU n 
2 50  ARG n 
2 51  SER n 
2 52  GLY n 
2 53  GLU n 
2 54  GLY n 
2 55  ARG n 
2 56  LEU n 
2 57  ASP n 
2 58  PRO n 
2 59  TYR n 
2 60  TRP n 
2 61  GLY n 
2 62  ASP n 
2 63  VAL n 
2 64  LYS n 
2 65  GLN n 
2 66  ASP n 
2 67  LEU n 
2 68  VAL n 
2 69  SER n 
2 70  TYR n 
2 71  CYS n 
2 72  GLY n 
2 73  PRO n 
2 74  TRP n 
2 75  LYS n 
2 76  LEU n 
2 77  ASP n 
2 78  ALA n 
2 79  ALA n 
2 80  TRP n 
2 81  ASP n 
2 82  GLY n 
2 83  LEU n 
2 84  SER n 
2 85  GLU n 
2 86  VAL n 
2 87  GLN n 
2 88  LEU n 
2 89  LEU n 
2 90  ALA n 
2 91  VAL n 
2 92  PRO n 
2 93  PRO n 
2 94  GLY n 
2 95  GLU n 
2 96  ARG n 
2 97  ALA n 
2 98  LYS n 
2 99  ASN n 
2 100 ILE n 
2 101 GLN n 
2 102 THR n 
2 103 LEU n 
2 104 PRO n 
2 105 GLY n 
2 106 ILE n 
2 107 PHE n 
2 108 LYS n 
2 109 THR n 
2 110 LYS n 
2 111 ASP n 
2 112 GLY n 
2 113 ASP n 
2 114 ILE n 
2 115 GLY n 
2 116 ALA n 
2 117 VAL n 
2 118 ALA n 
2 119 LEU n 
2 120 ASP n 
2 121 TYR n 
2 122 PRO n 
2 123 ALA n 
2 124 GLY n 
2 125 THR n 
2 126 SER n 
2 127 GLY n 
2 128 SER n 
2 129 PRO n 
2 130 ILE n 
2 131 LEU n 
2 132 ASP n 
2 133 LYS n 
2 134 CYS n 
2 135 GLY n 
2 136 ARG n 
2 137 VAL n 
2 138 ILE n 
2 139 GLY n 
2 140 LEU n 
2 141 TYR n 
2 142 GLY n 
2 143 ASN n 
2 144 GLY n 
2 145 VAL n 
2 146 VAL n 
2 147 ILE n 
2 148 LYS n 
2 149 ASN n 
2 150 GLY n 
2 151 SER n 
2 152 TYR n 
2 153 VAL n 
2 154 SER n 
2 155 ALA n 
2 156 ILE n 
2 157 THR n 
2 158 GLN n 
2 159 GLY n 
2 160 LYS n 
2 161 ARG n 
2 162 GLU n 
2 163 GLU n 
2 164 GLU n 
2 165 THR n 
2 166 PRO n 
2 167 VAL n 
2 168 GLU n 
# 
loop_
_entity_src_gen.entity_id 
_entity_src_gen.pdbx_src_id 
_entity_src_gen.pdbx_alt_source_flag 
_entity_src_gen.pdbx_seq_type 
_entity_src_gen.pdbx_beg_seq_num 
_entity_src_gen.pdbx_end_seq_num 
_entity_src_gen.gene_src_common_name 
_entity_src_gen.gene_src_genus 
_entity_src_gen.pdbx_gene_src_gene 
_entity_src_gen.gene_src_species 
_entity_src_gen.gene_src_strain 
_entity_src_gen.gene_src_tissue 
_entity_src_gen.gene_src_tissue_fraction 
_entity_src_gen.gene_src_details 
_entity_src_gen.pdbx_gene_src_fragment 
_entity_src_gen.pdbx_gene_src_scientific_name 
_entity_src_gen.pdbx_gene_src_ncbi_taxonomy_id 
_entity_src_gen.pdbx_gene_src_variant 
_entity_src_gen.pdbx_gene_src_cell_line 
_entity_src_gen.pdbx_gene_src_atcc 
_entity_src_gen.pdbx_gene_src_organ 
_entity_src_gen.pdbx_gene_src_organelle 
_entity_src_gen.pdbx_gene_src_cell 
_entity_src_gen.pdbx_gene_src_cellular_location 
_entity_src_gen.host_org_common_name 
_entity_src_gen.pdbx_host_org_scientific_name 
_entity_src_gen.pdbx_host_org_ncbi_taxonomy_id 
_entity_src_gen.host_org_genus 
_entity_src_gen.pdbx_host_org_gene 
_entity_src_gen.pdbx_host_org_organ 
_entity_src_gen.host_org_species 
_entity_src_gen.pdbx_host_org_tissue 
_entity_src_gen.pdbx_host_org_tissue_fraction 
_entity_src_gen.pdbx_host_org_strain 
_entity_src_gen.pdbx_host_org_variant 
_entity_src_gen.pdbx_host_org_cell_line 
_entity_src_gen.pdbx_host_org_atcc 
_entity_src_gen.pdbx_host_org_culture_collection 
_entity_src_gen.pdbx_host_org_cell 
_entity_src_gen.pdbx_host_org_organelle 
_entity_src_gen.pdbx_host_org_cellular_location 
_entity_src_gen.pdbx_host_org_vector_type 
_entity_src_gen.pdbx_host_org_vector 
_entity_src_gen.host_org_details 
_entity_src_gen.expression_system_id 
_entity_src_gen.plasmid_name 
_entity_src_gen.plasmid_details 
_entity_src_gen.pdbx_description 
1 1 sample 'Biological sequence' 1 46  ? ? ? ? ? ? ? ? ? 'Zika virus' 64320 ? ? ? ? ? ? ? ? 'Escherichia coli' 562 ? ? ? ? ? ? ? ? 
? ? ? ? ? ? ? ? ? ? ? ? ? 
2 1 sample 'Biological sequence' 1 168 ? ? ? ? ? ? ? ? ? 'Zika virus' 64320 ? ? ? ? ? ? ? ? 'Escherichia coli' 562 ? ? ? ? ? ? ? ? 
? ? ? ? ? ? ? ? ? ? ? ? ? 
# 
loop_
_chem_comp.id 
_chem_comp.type 
_chem_comp.mon_nstd_flag 
_chem_comp.name 
_chem_comp.pdbx_synonyms 
_chem_comp.formula 
_chem_comp.formula_weight 
A1BXQ non-polymer         . '[(3R)-3-aminopyrrolidin-1-yl](2-{[4-(hydroxymethyl)-2-methylquinolin-8-yl]methyl}phenyl)methanone' ? 
'C23 H25 N3 O2'  375.464 
ALA   'L-peptide linking' y ALANINE                                                                                             ? 
'C3 H7 N O2'     89.093  
ARG   'L-peptide linking' y ARGININE                                                                                            ? 
'C6 H15 N4 O2 1' 175.209 
ASN   'L-peptide linking' y ASPARAGINE                                                                                          ? 
'C4 H8 N2 O3'    132.118 
ASP   'L-peptide linking' y 'ASPARTIC ACID'                                                                                     ? 
'C4 H7 N O4'     133.103 
CYS   'L-peptide linking' y CYSTEINE                                                                                            ? 
'C3 H7 N O2 S'   121.158 
DMS   non-polymer         . 'DIMETHYL SULFOXIDE'                                                                                ? 
'C2 H6 O S'      78.133  
GLN   'L-peptide linking' y GLUTAMINE                                                                                           ? 
'C5 H10 N2 O3'   146.144 
GLU   'L-peptide linking' y 'GLUTAMIC ACID'                                                                                     ? 
'C5 H9 N O4'     147.129 
GLY   'peptide linking'   y GLYCINE                                                                                             ? 
'C2 H5 N O2'     75.067  
HIS   'L-peptide linking' y HISTIDINE                                                                                           ? 
'C6 H10 N3 O2 1' 156.162 
HOH   non-polymer         . WATER                                                                                               ? 
'H2 O'           18.015  
ILE   'L-peptide linking' y ISOLEUCINE                                                                                          ? 
'C6 H13 N O2'    131.173 
LEU   'L-peptide linking' y LEUCINE                                                                                             ? 
'C6 H13 N O2'    131.173 
LYS   'L-peptide linking' y LYSINE                                                                                              ? 
'C6 H15 N2 O2 1' 147.195 
MET   'L-peptide linking' y METHIONINE                                                                                          ? 
'C5 H11 N O2 S'  149.211 
PHE   'L-peptide linking' y PHENYLALANINE                                                                                       ? 
'C9 H11 N O2'    165.189 
PRO   'L-peptide linking' y PROLINE                                                                                             ? 
'C5 H9 N O2'     115.130 
SER   'L-peptide linking' y SERINE                                                                                              ? 
'C3 H7 N O3'     105.093 
THR   'L-peptide linking' y THREONINE                                                                                           ? 
'C4 H9 N O3'     119.119 
TRP   'L-peptide linking' y TRYPTOPHAN                                                                                          ? 
'C11 H12 N2 O2'  204.225 
TYR   'L-peptide linking' y TYROSINE                                                                                            ? 
'C9 H11 N O3'    181.189 
VAL   'L-peptide linking' y VALINE                                                                                              ? 
'C5 H11 N O2'    117.146 
# 
loop_
_pdbx_poly_seq_scheme.asym_id 
_pdbx_poly_seq_scheme.entity_id 
_pdbx_poly_seq_scheme.seq_id 
_pdbx_poly_seq_scheme.mon_id 
_pdbx_poly_seq_scheme.ndb_seq_num 
_pdbx_poly_seq_scheme.pdb_seq_num 
_pdbx_poly_seq_scheme.auth_seq_num 
_pdbx_poly_seq_scheme.pdb_mon_id 
_pdbx_poly_seq_scheme.auth_mon_id 
_pdbx_poly_seq_scheme.pdb_strand_id 
_pdbx_poly_seq_scheme.pdb_ins_code 
_pdbx_poly_seq_scheme.hetero 
A 1 1   SER 1   44  ?   ?   ?   A . n 
A 1 2   MET 2   45  ?   ?   ?   A . n 
A 1 3   GLY 3   46  ?   ?   ?   A . n 
A 1 4   LYS 4   47  ?   ?   ?   A . n 
A 1 5   SER 5   48  ?   ?   ?   A . n 
A 1 6   VAL 6   49  ?   ?   ?   A . n 
A 1 7   ASP 7   50  50  ASP ASP A . n 
A 1 8   MET 8   51  51  MET MET A . n 
A 1 9   TYR 9   52  52  TYR TYR A . n 
A 1 10  ILE 10  53  53  ILE ILE A . n 
A 1 11  GLU 11  54  54  GLU GLU A . n 
A 1 12  ARG 12  55  55  ARG ARG A . n 
A 1 13  ALA 13  56  56  ALA ALA A . n 
A 1 14  GLY 14  57  57  GLY GLY A . n 
A 1 15  ASP 15  58  58  ASP ASP A . n 
A 1 16  ILE 16  59  59  ILE ILE A . n 
A 1 17  THR 17  60  60  THR THR A . n 
A 1 18  TRP 18  61  61  TRP TRP A . n 
A 1 19  GLU 19  62  62  GLU GLU A . n 
A 1 20  LYS 20  63  63  LYS LYS A . n 
A 1 21  ASP 21  64  64  ASP ASP A . n 
A 1 22  ALA 22  65  65  ALA ALA A . n 
A 1 23  GLU 23  66  66  GLU GLU A . n 
A 1 24  VAL 24  67  67  VAL VAL A . n 
A 1 25  THR 25  68  68  THR THR A . n 
A 1 26  GLY 26  69  69  GLY GLY A . n 
A 1 27  ASN 27  70  70  ASN ASN A . n 
A 1 28  SER 28  71  71  SER SER A . n 
A 1 29  PRO 29  72  72  PRO PRO A . n 
A 1 30  ARG 30  73  73  ARG ARG A . n 
A 1 31  LEU 31  74  74  LEU LEU A . n 
A 1 32  ASP 32  75  75  ASP ASP A . n 
A 1 33  VAL 33  76  76  VAL VAL A . n 
A 1 34  ALA 34  77  77  ALA ALA A . n 
A 1 35  LEU 35  78  78  LEU LEU A . n 
A 1 36  ASP 36  79  79  ASP ASP A . n 
A 1 37  GLU 37  80  80  GLU GLU A . n 
A 1 38  SER 38  81  81  SER SER A . n 
A 1 39  GLY 39  82  82  GLY GLY A . n 
A 1 40  ASP 40  83  83  ASP ASP A . n 
A 1 41  PHE 41  84  84  PHE PHE A . n 
A 1 42  SER 42  85  85  SER SER A . n 
A 1 43  LEU 43  86  86  LEU LEU A . n 
A 1 44  VAL 44  87  87  VAL VAL A . n 
A 1 45  GLU 45  88  88  GLU GLU A . n 
A 1 46  GLU 46  89  ?   ?   ?   A . n 
B 2 1   MET 1   10  ?   ?   ?   B . n 
B 2 2   LYS 2   11  ?   ?   ?   B . n 
B 2 3   GLU 3   12  ?   ?   ?   B . n 
B 2 4   VAL 4   13  ?   ?   ?   B . n 
B 2 5   LYS 5   14  ?   ?   ?   B . n 
B 2 6   LYS 6   15  ?   ?   ?   B . n 
B 2 7   GLY 7   16  16  GLY GLY B . n 
B 2 8   GLU 8   17  17  GLU GLU B . n 
B 2 9   THR 9   18  18  THR THR B . n 
B 2 10  THR 10  19  19  THR THR B . n 
B 2 11  ASP 11  20  20  ASP ASP B . n 
B 2 12  GLY 12  21  21  GLY GLY B . n 
B 2 13  VAL 13  22  22  VAL VAL B . n 
B 2 14  TYR 14  23  23  TYR TYR B . n 
B 2 15  ARG 15  24  24  ARG ARG B . n 
B 2 16  VAL 16  25  25  VAL VAL B . n 
B 2 17  MET 17  26  26  MET MET B . n 
B 2 18  THR 18  27  27  THR THR B . n 
B 2 19  ARG 19  28  28  ARG ARG B . n 
B 2 20  ARG 20  29  29  ARG ARG B . n 
B 2 21  LEU 21  30  30  LEU LEU B . n 
B 2 22  LEU 22  31  31  LEU LEU B . n 
B 2 23  GLY 23  32  32  GLY GLY B . n 
B 2 24  SER 24  33  33  SER SER B . n 
B 2 25  THR 25  34  34  THR THR B . n 
B 2 26  GLN 26  35  35  GLN GLN B . n 
B 2 27  VAL 27  36  36  VAL VAL B . n 
B 2 28  GLY 28  37  37  GLY GLY B . n 
B 2 29  VAL 29  38  38  VAL VAL B . n 
B 2 30  GLY 30  39  39  GLY GLY B . n 
B 2 31  VAL 31  40  40  VAL VAL B . n 
B 2 32  MET 32  41  41  MET MET B . n 
B 2 33  GLN 33  42  42  GLN GLN B . n 
B 2 34  GLU 34  43  43  GLU GLU B . n 
B 2 35  GLY 35  44  44  GLY GLY B . n 
B 2 36  VAL 36  45  45  VAL VAL B . n 
B 2 37  PHE 37  46  46  PHE PHE B . n 
B 2 38  HIS 38  47  47  HIS HIS B . n 
B 2 39  THR 39  48  48  THR THR B . n 
B 2 40  MET 40  49  49  MET MET B . n 
B 2 41  TRP 41  50  50  TRP TRP B . n 
B 2 42  HIS 42  51  51  HIS HIS B . n 
B 2 43  VAL 43  52  52  VAL VAL B . n 
B 2 44  THR 44  53  53  THR THR B . n 
B 2 45  LYS 45  54  54  LYS LYS B . n 
B 2 46  GLY 46  55  55  GLY GLY B . n 
B 2 47  ALA 47  56  56  ALA ALA B . n 
B 2 48  ALA 48  57  57  ALA ALA B . n 
B 2 49  LEU 49  58  58  LEU LEU B . n 
B 2 50  ARG 50  59  59  ARG ARG B . n 
B 2 51  SER 51  60  60  SER SER B . n 
B 2 52  GLY 52  61  61  GLY GLY B . n 
B 2 53  GLU 53  62  62  GLU GLU B . n 
B 2 54  GLY 54  63  63  GLY GLY B . n 
B 2 55  ARG 55  64  64  ARG ARG B . n 
B 2 56  LEU 56  65  65  LEU LEU B . n 
B 2 57  ASP 57  66  66  ASP ASP B . n 
B 2 58  PRO 58  67  67  PRO PRO B . n 
B 2 59  TYR 59  68  68  TYR TYR B . n 
B 2 60  TRP 60  69  69  TRP TRP B . n 
B 2 61  GLY 61  70  70  GLY GLY B . n 
B 2 62  ASP 62  71  71  ASP ASP B . n 
B 2 63  VAL 63  72  72  VAL VAL B . n 
B 2 64  LYS 64  73  73  LYS LYS B . n 
B 2 65  GLN 65  74  74  GLN GLN B . n 
B 2 66  ASP 66  75  75  ASP ASP B . n 
B 2 67  LEU 67  76  76  LEU LEU B . n 
B 2 68  VAL 68  77  77  VAL VAL B . n 
B 2 69  SER 69  78  78  SER SER B . n 
B 2 70  TYR 70  79  79  TYR TYR B . n 
B 2 71  CYS 71  80  80  CYS CYS B . n 
B 2 72  GLY 72  81  81  GLY GLY B . n 
B 2 73  PRO 73  82  82  PRO PRO B . n 
B 2 74  TRP 74  83  83  TRP TRP B . n 
B 2 75  LYS 75  84  84  LYS LYS B . n 
B 2 76  LEU 76  85  85  LEU LEU B . n 
B 2 77  ASP 77  86  86  ASP ASP B . n 
B 2 78  ALA 78  87  87  ALA ALA B . n 
B 2 79  ALA 79  88  88  ALA ALA B . n 
B 2 80  TRP 80  89  89  TRP TRP B . n 
B 2 81  ASP 81  90  90  ASP ASP B . n 
B 2 82  GLY 82  91  91  GLY GLY B . n 
B 2 83  LEU 83  92  92  LEU LEU B . n 
B 2 84  SER 84  93  93  SER SER B . n 
B 2 85  GLU 85  94  94  GLU GLU B . n 
B 2 86  VAL 86  95  95  VAL VAL B . n 
B 2 87  GLN 87  96  96  GLN GLN B . n 
B 2 88  LEU 88  97  97  LEU LEU B . n 
B 2 89  LEU 89  98  98  LEU LEU B . n 
B 2 90  ALA 90  99  99  ALA ALA B . n 
B 2 91  VAL 91  100 100 VAL VAL B . n 
B 2 92  PRO 92  101 101 PRO PRO B . n 
B 2 93  PRO 93  102 102 PRO PRO B . n 
B 2 94  GLY 94  103 103 GLY GLY B . n 
B 2 95  GLU 95  104 104 GLU GLU B . n 
B 2 96  ARG 96  105 105 ARG ARG B . n 
B 2 97  ALA 97  106 106 ALA ALA B . n 
B 2 98  LYS 98  107 107 LYS LYS B . n 
B 2 99  ASN 99  108 108 ASN ASN B . n 
B 2 100 ILE 100 109 109 ILE ILE B . n 
B 2 101 GLN 101 110 110 GLN GLN B . n 
B 2 102 THR 102 111 111 THR THR B . n 
B 2 103 LEU 103 112 112 LEU LEU B . n 
B 2 104 PRO 104 113 113 PRO PRO B . n 
B 2 105 GLY 105 114 114 GLY GLY B . n 
B 2 106 ILE 106 115 115 ILE ILE B . n 
B 2 107 PHE 107 116 116 PHE PHE B . n 
B 2 108 LYS 108 117 117 LYS LYS B . n 
B 2 109 THR 109 118 118 THR THR B . n 
B 2 110 LYS 110 119 119 LYS LYS B . n 
B 2 111 ASP 111 120 120 ASP ASP B . n 
B 2 112 GLY 112 121 121 GLY GLY B . n 
B 2 113 ASP 113 122 122 ASP ASP B . n 
B 2 114 ILE 114 123 123 ILE ILE B . n 
B 2 115 GLY 115 124 124 GLY GLY B . n 
B 2 116 ALA 116 125 125 ALA ALA B . n 
B 2 117 VAL 117 126 126 VAL VAL B . n 
B 2 118 ALA 118 127 127 ALA ALA B . n 
B 2 119 LEU 119 128 128 LEU LEU B . n 
B 2 120 ASP 120 129 129 ASP ASP B . n 
B 2 121 TYR 121 130 130 TYR TYR B . n 
B 2 122 PRO 122 131 131 PRO PRO B . n 
B 2 123 ALA 123 132 132 ALA ALA B . n 
B 2 124 GLY 124 133 133 GLY GLY B . n 
B 2 125 THR 125 134 134 THR THR B . n 
B 2 126 SER 126 135 135 SER SER B . n 
B 2 127 GLY 127 136 136 GLY GLY B . n 
B 2 128 SER 128 137 137 SER SER B . n 
B 2 129 PRO 129 138 138 PRO PRO B . n 
B 2 130 ILE 130 139 139 ILE ILE B . n 
B 2 131 LEU 131 140 140 LEU LEU B . n 
B 2 132 ASP 132 141 141 ASP ASP B . n 
B 2 133 LYS 133 142 142 LYS LYS B . n 
B 2 134 CYS 134 143 143 CYS CYS B . n 
B 2 135 GLY 135 144 144 GLY GLY B . n 
B 2 136 ARG 136 145 145 ARG ARG B . n 
B 2 137 VAL 137 146 146 VAL VAL B . n 
B 2 138 ILE 138 147 147 ILE ILE B . n 
B 2 139 GLY 139 148 148 GLY GLY B . n 
B 2 140 LEU 140 149 149 LEU LEU B . n 
B 2 141 TYR 141 150 150 TYR TYR B . n 
B 2 142 GLY 142 151 151 GLY GLY B . n 
B 2 143 ASN 143 152 152 ASN ASN B . n 
B 2 144 GLY 144 153 153 GLY GLY B . n 
B 2 145 VAL 145 154 154 VAL VAL B . n 
B 2 146 VAL 146 155 155 VAL VAL B . n 
B 2 147 ILE 147 156 156 ILE ILE B . n 
B 2 148 LYS 148 157 157 LYS LYS B . n 
B 2 149 ASN 149 158 158 ASN ASN B . n 
B 2 150 GLY 150 159 159 GLY GLY B . n 
B 2 151 SER 151 160 160 SER SER B . n 
B 2 152 TYR 152 161 161 TYR TYR B . n 
B 2 153 VAL 153 162 162 VAL VAL B . n 
B 2 154 SER 154 163 163 SER SER B . n 
B 2 155 ALA 155 164 164 ALA ALA B . n 
B 2 156 ILE 156 165 165 ILE ILE B . n 
B 2 157 THR 157 166 166 THR THR B . n 
B 2 158 GLN 158 167 167 GLN GLN B . n 
B 2 159 GLY 159 168 168 GLY GLY B . n 
B 2 160 LYS 160 169 169 LYS LYS B . n 
B 2 161 ARG 161 170 170 ARG ARG B . n 
B 2 162 GLU 162 171 171 GLU GLU B . n 
B 2 163 GLU 163 172 ?   ?   ?   B . n 
B 2 164 GLU 164 173 ?   ?   ?   B . n 
B 2 165 THR 165 174 ?   ?   ?   B . n 
B 2 166 PRO 166 175 ?   ?   ?   B . n 
B 2 167 VAL 167 176 ?   ?   ?   B . n 
B 2 168 GLU 168 177 ?   ?   ?   B . n 
# 
_pdbx_entity_instance_feature.ordinal        1 
_pdbx_entity_instance_feature.comp_id        A1BXQ 
_pdbx_entity_instance_feature.asym_id        ? 
_pdbx_entity_instance_feature.seq_num        ? 
_pdbx_entity_instance_feature.auth_comp_id   A1BXQ 
_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 A1BXQ 1  204 301 A1BXQ LIG B . 
G 3 DMS   1  205 302 DMS   DMS B . 
H 5 HOH   1  101 105 HOH   HOH A . 
H 5 HOH   2  102 20  HOH   HOH A . 
H 5 HOH   3  103 34  HOH   HOH A . 
H 5 HOH   4  104 98  HOH   HOH A . 
H 5 HOH   5  105 65  HOH   HOH A . 
H 5 HOH   6  106 48  HOH   HOH A . 
H 5 HOH   7  107 129 HOH   HOH A . 
H 5 HOH   8  108 16  HOH   HOH A . 
H 5 HOH   9  109 77  HOH   HOH A . 
H 5 HOH   10 110 117 HOH   HOH A . 
H 5 HOH   11 111 49  HOH   HOH A . 
H 5 HOH   12 112 119 HOH   HOH A . 
H 5 HOH   13 113 110 HOH   HOH A . 
H 5 HOH   14 114 60  HOH   HOH A . 
H 5 HOH   15 115 121 HOH   HOH A . 
H 5 HOH   16 116 120 HOH   HOH A . 
H 5 HOH   17 117 118 HOH   HOH A . 
H 5 HOH   18 118 50  HOH   HOH A . 
H 5 HOH   19 119 29  HOH   HOH A . 
H 5 HOH   20 120 70  HOH   HOH A . 
H 5 HOH   21 121 127 HOH   HOH A . 
H 5 HOH   22 122 40  HOH   HOH A . 
H 5 HOH   23 123 27  HOH   HOH A . 
H 5 HOH   24 124 85  HOH   HOH A . 
I 5 HOH   1  301 51  HOH   HOH B . 
I 5 HOH   2  302 123 HOH   HOH B . 
I 5 HOH   3  303 100 HOH   HOH B . 
I 5 HOH   4  304 11  HOH   HOH B . 
I 5 HOH   5  305 58  HOH   HOH B . 
I 5 HOH   6  306 92  HOH   HOH B . 
I 5 HOH   7  307 5   HOH   HOH B . 
I 5 HOH   8  308 90  HOH   HOH B . 
I 5 HOH   9  309 57  HOH   HOH B . 
I 5 HOH   10 310 68  HOH   HOH B . 
I 5 HOH   11 311 13  HOH   HOH B . 
I 5 HOH   12 312 108 HOH   HOH B . 
I 5 HOH   13 313 56  HOH   HOH B . 
I 5 HOH   14 314 94  HOH   HOH B . 
I 5 HOH   15 315 30  HOH   HOH B . 
I 5 HOH   16 316 14  HOH   HOH B . 
I 5 HOH   17 317 46  HOH   HOH B . 
I 5 HOH   18 318 89  HOH   HOH B . 
I 5 HOH   19 319 24  HOH   HOH B . 
I 5 HOH   20 320 64  HOH   HOH B . 
I 5 HOH   21 321 31  HOH   HOH B . 
I 5 HOH   22 322 2   HOH   HOH B . 
I 5 HOH   23 323 62  HOH   HOH B . 
I 5 HOH   24 324 69  HOH   HOH B . 
I 5 HOH   25 325 43  HOH   HOH B . 
I 5 HOH   26 326 42  HOH   HOH B . 
I 5 HOH   27 327 63  HOH   HOH B . 
I 5 HOH   28 328 115 HOH   HOH B . 
I 5 HOH   29 329 106 HOH   HOH B . 
I 5 HOH   30 330 81  HOH   HOH B . 
I 5 HOH   31 331 32  HOH   HOH B . 
I 5 HOH   32 332 4   HOH   HOH B . 
I 5 HOH   33 333 1   HOH   HOH B . 
I 5 HOH   34 334 9   HOH   HOH B . 
I 5 HOH   35 335 39  HOH   HOH B . 
I 5 HOH   36 336 35  HOH   HOH B . 
I 5 HOH   37 337 116 HOH   HOH B . 
I 5 HOH   38 338 36  HOH   HOH B . 
I 5 HOH   39 339 28  HOH   HOH B . 
I 5 HOH   40 340 72  HOH   HOH B . 
I 5 HOH   41 341 67  HOH   HOH B . 
I 5 HOH   42 342 125 HOH   HOH B . 
I 5 HOH   43 343 10  HOH   HOH B . 
I 5 HOH   44 344 122 HOH   HOH B . 
I 5 HOH   45 345 66  HOH   HOH B . 
I 5 HOH   46 346 82  HOH   HOH B . 
I 5 HOH   47 347 23  HOH   HOH B . 
I 5 HOH   48 348 17  HOH   HOH B . 
I 5 HOH   49 349 103 HOH   HOH B . 
I 5 HOH   50 350 107 HOH   HOH B . 
I 5 HOH   51 351 102 HOH   HOH B . 
I 5 HOH   52 352 21  HOH   HOH B . 
I 5 HOH   53 353 18  HOH   HOH B . 
I 5 HOH   54 354 3   HOH   HOH B . 
I 5 HOH   55 355 12  HOH   HOH B . 
I 5 HOH   56 356 80  HOH   HOH B . 
I 5 HOH   57 357 61  HOH   HOH B . 
I 5 HOH   58 358 87  HOH   HOH B . 
I 5 HOH   59 359 112 HOH   HOH B . 
I 5 HOH   60 360 126 HOH   HOH B . 
I 5 HOH   61 361 54  HOH   HOH B . 
I 5 HOH   62 362 124 HOH   HOH B . 
I 5 HOH   63 363 26  HOH   HOH B . 
I 5 HOH   64 364 128 HOH   HOH B . 
I 5 HOH   65 365 79  HOH   HOH B . 
I 5 HOH   66 366 73  HOH   HOH B . 
I 5 HOH   67 367 59  HOH   HOH B . 
I 5 HOH   68 368 75  HOH   HOH B . 
I 5 HOH   69 369 45  HOH   HOH B . 
I 5 HOH   70 370 83  HOH   HOH B . 
I 5 HOH   71 371 109 HOH   HOH B . 
I 5 HOH   72 372 44  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           7I1Z 
_cell.length_a           42.306 
_cell.length_b           42.306 
_cell.length_c           216.732 
_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                         7I1Z 
_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          7I1Z 
_exptl.method            'X-RAY DIFFRACTION' 
_exptl.crystals_number   1 
# 
_exptl_crystal.id                    1 
_exptl_crystal.density_meas          ? 
_exptl_crystal.density_Matthews      2.09 
_exptl_crystal.density_percent_sol   41.19 
_exptl_crystal.description           ? 
_exptl_crystal.preparation           ? 
# 
_exptl_crystal_grow.crystal_id      1 
_exptl_crystal_grow.method          'VAPOR DIFFUSION, SITTING DROP' 
_exptl_crystal_grow.pH              4.8 
_exptl_crystal_grow.temp            298 
_exptl_crystal_grow.pdbx_details    '30% w/v PEG 2000, 0.2M Ammonium sulfate, 0.1M acetate (pH 4.8)' 
_exptl_crystal_grow.temp_details    ? 
_exptl_crystal_grow.pdbx_pH_range   ? 
# 
_diffrn.id                               1 
_diffrn.ambient_temp                     100 
_diffrn.crystal_id                       1 
_diffrn.ambient_temp_details             ? 
_diffrn.pdbx_serial_crystal_experiment   ? 
# 
_diffrn_detector.detector               PIXEL 
_diffrn_detector.type                   'DECTRIS EIGER2 XE 9M' 
_diffrn_detector.pdbx_collection_date   2023-10-10 
_diffrn_detector.diffrn_id              1 
_diffrn_detector.details                ? 
# 
_diffrn_radiation.diffrn_id                        1 
_diffrn_radiation.wavelength_id                    1 
_diffrn_radiation.pdbx_diffrn_protocol             'SINGLE WAVELENGTH' 
_diffrn_radiation.pdbx_monochromatic_or_laue_m_l   ? 
_diffrn_radiation.monochromator                    ? 
_diffrn_radiation.pdbx_scattering_type             x-ray 
# 
_diffrn_radiation_wavelength.id           1 
_diffrn_radiation_wavelength.wavelength   0.92124 
_diffrn_radiation_wavelength.wt           1.0 
# 
_diffrn_source.diffrn_id                   1 
_diffrn_source.source                      SYNCHROTRON 
_diffrn_source.type                        'DIAMOND BEAMLINE I04-1' 
_diffrn_source.pdbx_wavelength_list        0.92124 
_diffrn_source.pdbx_synchrotron_site       Diamond 
_diffrn_source.pdbx_synchrotron_beamline   I04-1 
_diffrn_source.pdbx_wavelength             ? 
# 
_reflns.entry_id                     7I1Z 
_reflns.pdbx_diffrn_id               1 
_reflns.pdbx_ordinal                 1 
_reflns.d_resolution_low             108.40 
_reflns.d_resolution_high            1.72 
_reflns.number_obs                   22292 
_reflns.percent_possible_obs         99.9 
_reflns.pdbx_Rmerge_I_obs            0.158 
_reflns.pdbx_netI_over_sigmaI        8.2 
_reflns.pdbx_redundancy              25.3 
_reflns.pdbx_Rrim_I_all              0.162 
_reflns.pdbx_Rpim_I_all              0.033 
_reflns.pdbx_CC_half                 0.999 
_reflns.pdbx_number_measured_all     564011 
_reflns.pdbx_chi_squared             0.32 
_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                  1.72 
_reflns_shell.d_res_low                   1.75 
_reflns_shell.number_measured_all         29240 
_reflns_shell.number_unique_obs           1123 
_reflns_shell.Rmerge_I_obs                ? 
_reflns_shell.pdbx_chi_squared            0.12 
_reflns_shell.pdbx_redundancy             26.0 
_reflns_shell.percent_possible_obs        97.6 
_reflns_shell.pdbx_netI_over_sigmaI_obs   0.2 
_reflns_shell.pdbx_Rrim_I_all             11.049 
_reflns_shell.pdbx_Rpim_I_all             2.150 
_reflns_shell.pdbx_CC_half                0.345 
_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                                 7I1Z 
_refine.pdbx_diffrn_id                           1 
_refine.pdbx_TLS_residual_ADP_flag               ? 
_refine.ls_number_reflns_obs                     19115 
_refine.ls_number_reflns_all                     ? 
_refine.pdbx_ls_sigma_I                          ? 
_refine.pdbx_ls_sigma_F                          ? 
_refine.pdbx_data_cutoff_high_absF               ? 
_refine.pdbx_data_cutoff_low_absF                ? 
_refine.pdbx_data_cutoff_high_rms_absF           ? 
_refine.ls_d_res_low                             54.18 
_refine.ls_d_res_high                            1.72 
_refine.ls_percent_reflns_obs                    90.63 
_refine.ls_R_factor_obs                          0.24009 
_refine.ls_R_factor_all                          ? 
_refine.ls_R_factor_R_work                       0.23690 
_refine.ls_R_factor_R_free                       0.30088 
_refine.ls_R_factor_R_free_error                 ? 
_refine.ls_R_factor_R_free_error_details         ? 
_refine.ls_percent_reflns_R_free                 5.0 
_refine.ls_number_reflns_R_free                  1008 
_refine.ls_number_parameters                     ? 
_refine.ls_number_restraints                     ? 
_refine.occupancy_min                            ? 
_refine.occupancy_max                            ? 
_refine.correlation_coeff_Fo_to_Fc               0.963 
_refine.correlation_coeff_Fo_to_Fc_free          0.943 
_refine.B_iso_mean                               54.068 
_refine.aniso_B[1][1]                            2.43 
_refine.aniso_B[2][2]                            2.43 
_refine.aniso_B[3][3]                            -4.87 
_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                       0.176 
_refine.pdbx_overall_ESU_R_Free                  0.172 
_refine.overall_SU_ML                            0.204 
_refine.pdbx_overall_phase_error                 ? 
_refine.overall_SU_B                             7.145 
_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             96 
_refine_hist.number_atoms_total               1616 
_refine_hist.d_res_high                       1.72 
_refine_hist.d_res_low                        54.18 
# 
loop_
_refine_ls_restr.type 
_refine_ls_restr.dev_ideal 
_refine_ls_restr.dev_ideal_target 
_refine_ls_restr.weight 
_refine_ls_restr.number 
_refine_ls_restr.pdbx_refine_id 
_refine_ls_restr.pdbx_restraint_function 
r_bond_refined_d             0.008  0.014  ? 2069 'X-RAY DIFFRACTION' ? 
r_bond_other_d               0.001  0.015  ? 1722 'X-RAY DIFFRACTION' ? 
r_angle_refined_deg          1.554  1.639  ? 2528 'X-RAY DIFFRACTION' ? 
r_angle_other_deg            1.214  1.588  ? 3973 'X-RAY DIFFRACTION' ? 
r_dihedral_angle_1_deg       7.440  5.000  ? 241  'X-RAY DIFFRACTION' ? 
r_dihedral_angle_2_deg       34.024 22.471 ? 85   'X-RAY DIFFRACTION' ? 
r_dihedral_angle_3_deg       16.591 15.000 ? 289  'X-RAY DIFFRACTION' ? 
r_dihedral_angle_4_deg       16.760 15.000 ? 10   'X-RAY DIFFRACTION' ? 
r_chiral_restr               0.060  0.200  ? 227  'X-RAY DIFFRACTION' ? 
r_gen_planes_refined         0.008  0.020  ? 2170 'X-RAY DIFFRACTION' ? 
r_gen_planes_other           0.001  0.020  ? 420  'X-RAY DIFFRACTION' ? 
r_nbd_refined                ?      ?      ? ?    'X-RAY DIFFRACTION' ? 
r_nbd_other                  ?      ?      ? ?    'X-RAY DIFFRACTION' ? 
r_nbtor_refined              ?      ?      ? ?    'X-RAY DIFFRACTION' ? 
r_nbtor_other                ?      ?      ? ?    'X-RAY DIFFRACTION' ? 
r_xyhbond_nbd_refined        ?      ?      ? ?    'X-RAY DIFFRACTION' ? 
r_xyhbond_nbd_other          ?      ?      ? ?    'X-RAY DIFFRACTION' ? 
r_metal_ion_refined          ?      ?      ? ?    'X-RAY DIFFRACTION' ? 
r_metal_ion_other            ?      ?      ? ?    'X-RAY DIFFRACTION' ? 
r_symmetry_vdw_refined       ?      ?      ? ?    'X-RAY DIFFRACTION' ? 
r_symmetry_vdw_other         ?      ?      ? ?    'X-RAY DIFFRACTION' ? 
r_symmetry_hbond_refined     ?      ?      ? ?    'X-RAY DIFFRACTION' ? 
r_symmetry_hbond_other       ?      ?      ? ?    'X-RAY DIFFRACTION' ? 
r_symmetry_metal_ion_refined ?      ?      ? ?    'X-RAY DIFFRACTION' ? 
r_symmetry_metal_ion_other   ?      ?      ? ?    'X-RAY DIFFRACTION' ? 
r_mcbond_it                  4.135  5.386  ? 1022 'X-RAY DIFFRACTION' ? 
r_mcbond_other               4.217  5.329  ? 978  'X-RAY DIFFRACTION' ? 
r_mcangle_it                 6.071  7.866  ? 1167 'X-RAY DIFFRACTION' ? 
r_mcangle_other              6.071  7.873  ? 1168 'X-RAY DIFFRACTION' ? 
r_scbond_it                  4.713  6.070  ? 1047 'X-RAY DIFFRACTION' ? 
r_scbond_other               4.711  6.074  ? 1048 'X-RAY DIFFRACTION' ? 
r_scangle_it                 ?      ?      ? ?    'X-RAY DIFFRACTION' ? 
r_scangle_other              7.189  8.666  ? 1362 'X-RAY DIFFRACTION' ? 
r_long_range_B_refined       9.834  57.614 ? 2002 'X-RAY DIFFRACTION' ? 
r_long_range_B_other         9.789  57.448 ? 1985 '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                       1.718 
_refine_ls_shell.d_res_low                        1.763 
_refine_ls_shell.number_reflns_R_work             317 
_refine_ls_shell.R_factor_R_work                  0.614 
_refine_ls_shell.percent_reflns_obs               20.79 
_refine_ls_shell.R_factor_R_free                  0.822 
_refine_ls_shell.R_factor_R_free_error            ? 
_refine_ls_shell.percent_reflns_R_free            ? 
_refine_ls_shell.number_reflns_R_free             20 
_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                  7I1Z 
_struct.title                     
'PanDDA analysis group deposition -- Crystal Structure of ZIKV NS2B-NS3 protease in complex with NegAcid1-Am02' 
_struct.pdbx_model_details        ? 
_struct.pdbx_CASP_flag            ? 
_struct.pdbx_model_type_details   ? 
# 
_struct_keywords.entry_id        7I1Z 
_struct_keywords.pdbx_keywords   'VIRAL PROTEIN' 
_struct_keywords.text            'SGC - Diamond I04-1, PanDDA, XChemExplorer, VIRAL PROTEIN' 
# 
loop_
_struct_asym.id 
_struct_asym.pdbx_blank_PDB_chainid_flag 
_struct_asym.pdbx_modified 
_struct_asym.entity_id 
_struct_asym.details 
A N N 1 ? 
B N N 2 ? 
C N N 3 ? 
D N N 3 ? 
E N N 3 ? 
F N N 4 ? 
G N N 3 ? 
H N N 5 ? 
I N N 5 ? 
# 
loop_
_struct_ref.id 
_struct_ref.db_name 
_struct_ref.db_code 
_struct_ref.pdbx_db_accession 
_struct_ref.pdbx_db_isoform 
_struct_ref.entity_id 
_struct_ref.pdbx_seq_one_letter_code 
_struct_ref.pdbx_align_begin 
1 UNP POLG_ZIKV Q32ZE1 ? 1 GKSVDMYIERAGDITWEKDAEVTGNSPRLDVALDESGDFSLVEE 1414 
2 UNP POLG_ZIKV Q32ZE1 ? 2 
;KEVKKGETTDGVYRVMTRRLLGSTQVGVGVMQEGVFHTMWHVTKGAALRSGEGRLDPYWGDVKQDLVSYCGPWKLDAAWD
GLSEVQLLAVPPGERARNIQTLPGIFKTKDGDIGAVALDYPAGTSGSPILDKCGRVIGLYGNGVVIKNGSYVSAITQGKR
EEETPVE
;
1509 
# 
loop_
_struct_ref_seq.align_id 
_struct_ref_seq.ref_id 
_struct_ref_seq.pdbx_PDB_id_code 
_struct_ref_seq.pdbx_strand_id 
_struct_ref_seq.seq_align_beg 
_struct_ref_seq.pdbx_seq_align_beg_ins_code 
_struct_ref_seq.seq_align_end 
_struct_ref_seq.pdbx_seq_align_end_ins_code 
_struct_ref_seq.pdbx_db_accession 
_struct_ref_seq.db_align_beg 
_struct_ref_seq.pdbx_db_align_beg_ins_code 
_struct_ref_seq.db_align_end 
_struct_ref_seq.pdbx_db_align_end_ins_code 
_struct_ref_seq.pdbx_auth_seq_align_beg 
_struct_ref_seq.pdbx_auth_seq_align_end 
1 1 7I1Z A 3 ? 46  ? Q32ZE1 1414 ? 1457 ? 46 89  
2 2 7I1Z 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 7I1Z SER A 1  ? UNP Q32ZE1 ?   ?    'expression tag'        44  1 
1 7I1Z MET A 2  ? UNP Q32ZE1 ?   ?    'expression tag'        45  2 
2 7I1Z MET B 1  ? UNP Q32ZE1 ?   ?    'initiating methionine' 10  3 
2 7I1Z LYS B 98 ? UNP Q32ZE1 ARG 1605 conflict                107 4 
# 
_pdbx_struct_assembly.id                   1 
_pdbx_struct_assembly.details              author_defined_assembly 
_pdbx_struct_assembly.method_details       ? 
_pdbx_struct_assembly.oligomeric_details   dimeric 
_pdbx_struct_assembly.oligomeric_count     2 
# 
_pdbx_struct_assembly_gen.assembly_id       1 
_pdbx_struct_assembly_gen.oper_expression   1 
_pdbx_struct_assembly_gen.asym_id_list      A,B,C,D,E,F,G,H,I 
# 
_pdbx_struct_oper_list.id                   1 
_pdbx_struct_oper_list.type                 'identity operation' 
_pdbx_struct_oper_list.name                 1_555 
_pdbx_struct_oper_list.symmetry_operation   x,y,z 
_pdbx_struct_oper_list.matrix[1][1]         1.0000000000 
_pdbx_struct_oper_list.matrix[1][2]         0.0000000000 
_pdbx_struct_oper_list.matrix[1][3]         0.0000000000 
_pdbx_struct_oper_list.vector[1]            0.0000000000 
_pdbx_struct_oper_list.matrix[2][1]         0.0000000000 
_pdbx_struct_oper_list.matrix[2][2]         1.0000000000 
_pdbx_struct_oper_list.matrix[2][3]         0.0000000000 
_pdbx_struct_oper_list.vector[2]            0.0000000000 
_pdbx_struct_oper_list.matrix[3][1]         0.0000000000 
_pdbx_struct_oper_list.matrix[3][2]         0.0000000000 
_pdbx_struct_oper_list.matrix[3][3]         1.0000000000 
_pdbx_struct_oper_list.vector[3]            0.0000000000 
# 
loop_
_struct_conf.conf_type_id 
_struct_conf.id 
_struct_conf.pdbx_PDB_helix_id 
_struct_conf.beg_label_comp_id 
_struct_conf.beg_label_asym_id 
_struct_conf.beg_label_seq_id 
_struct_conf.pdbx_beg_PDB_ins_code 
_struct_conf.end_label_comp_id 
_struct_conf.end_label_asym_id 
_struct_conf.end_label_seq_id 
_struct_conf.pdbx_end_PDB_ins_code 
_struct_conf.beg_auth_comp_id 
_struct_conf.beg_auth_asym_id 
_struct_conf.beg_auth_seq_id 
_struct_conf.end_auth_comp_id 
_struct_conf.end_auth_asym_id 
_struct_conf.end_auth_seq_id 
_struct_conf.pdbx_PDB_helix_class 
_struct_conf.details 
_struct_conf.pdbx_PDB_helix_length 
HELX_P HELX_P1 AA1 TRP B 41  ? LYS B 45  ? TRP B 50  LYS B 54  1 ? 5 
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               2.642 
_struct_conn.pdbx_value_order              ? 
_struct_conn.pdbx_role                     ? 
# 
_struct_conn_type.id          disulf 
_struct_conn_type.criteria    ? 
_struct_conn_type.reference   ? 
# 
_pdbx_modification_feature.ordinal                            1 
_pdbx_modification_feature.label_comp_id                      CYS 
_pdbx_modification_feature.label_asym_id                      B 
_pdbx_modification_feature.label_seq_id                       134 
_pdbx_modification_feature.label_alt_id                       ? 
_pdbx_modification_feature.modified_residue_label_comp_id     CYS 
_pdbx_modification_feature.modified_residue_label_asym_id     B 
_pdbx_modification_feature.modified_residue_label_seq_id      134 
_pdbx_modification_feature.modified_residue_label_alt_id      ? 
_pdbx_modification_feature.auth_comp_id                       CYS 
_pdbx_modification_feature.auth_asym_id                       B 
_pdbx_modification_feature.auth_seq_id                        143 
_pdbx_modification_feature.PDB_ins_code                       ? 
_pdbx_modification_feature.symmetry                           1_555 
_pdbx_modification_feature.modified_residue_auth_comp_id      CYS 
_pdbx_modification_feature.modified_residue_auth_asym_id      B 
_pdbx_modification_feature.modified_residue_auth_seq_id       143 
_pdbx_modification_feature.modified_residue_PDB_ins_code      ? 
_pdbx_modification_feature.modified_residue_symmetry          8_444 
_pdbx_modification_feature.comp_id_linking_atom               SG 
_pdbx_modification_feature.modified_residue_id_linking_atom   SG 
_pdbx_modification_feature.modified_residue_id                . 
_pdbx_modification_feature.ref_pcm_id                         . 
_pdbx_modification_feature.ref_comp_id                        . 
_pdbx_modification_feature.type                               None 
_pdbx_modification_feature.category                           'Disulfide bridge' 
# 
loop_
_struct_sheet.id 
_struct_sheet.type 
_struct_sheet.number_strands 
_struct_sheet.details 
AA1 ? 8 ? 
AA2 ? 6 ? 
AA3 ? 4 ? 
# 
loop_
_struct_sheet_order.sheet_id 
_struct_sheet_order.range_id_1 
_struct_sheet_order.range_id_2 
_struct_sheet_order.offset 
_struct_sheet_order.sense 
AA1 1 2 ? anti-parallel 
AA1 2 3 ? parallel      
AA1 3 4 ? anti-parallel 
AA1 4 5 ? anti-parallel 
AA1 5 6 ? anti-parallel 
AA1 6 7 ? anti-parallel 
AA1 7 8 ? anti-parallel 
AA2 1 2 ? anti-parallel 
AA2 2 3 ? parallel      
AA2 3 4 ? anti-parallel 
AA2 4 5 ? anti-parallel 
AA2 5 6 ? anti-parallel 
AA3 1 2 ? anti-parallel 
AA3 2 3 ? anti-parallel 
AA3 3 4 ? anti-parallel 
# 
loop_
_struct_sheet_range.sheet_id 
_struct_sheet_range.id 
_struct_sheet_range.beg_label_comp_id 
_struct_sheet_range.beg_label_asym_id 
_struct_sheet_range.beg_label_seq_id 
_struct_sheet_range.pdbx_beg_PDB_ins_code 
_struct_sheet_range.end_label_comp_id 
_struct_sheet_range.end_label_asym_id 
_struct_sheet_range.end_label_seq_id 
_struct_sheet_range.pdbx_end_PDB_ins_code 
_struct_sheet_range.beg_auth_comp_id 
_struct_sheet_range.beg_auth_asym_id 
_struct_sheet_range.beg_auth_seq_id 
_struct_sheet_range.end_auth_comp_id 
_struct_sheet_range.end_auth_asym_id 
_struct_sheet_range.end_auth_seq_id 
AA1 1 GLY B 54  ? LEU B 56  ? GLY B 63  LEU B 65  
AA1 2 LEU B 49  ? SER B 51  ? LEU B 58  SER B 60  
AA1 3 MET A 8   ? GLY A 14  ? MET A 51  GLY A 57  
AA1 4 GLY B 12  ? THR B 18  ? GLY B 21  THR B 27  
AA1 5 THR B 25  ? GLN B 33  ? THR B 34  GLN B 42  
AA1 6 VAL B 36  ? MET B 40  ? VAL B 45  MET B 49  
AA1 7 LEU B 67  ? TYR B 70  ? LEU B 76  TYR B 79  
AA1 8 PRO B 58  ? ASP B 62  ? PRO B 67  ASP B 71  
AA2 1 PHE A 41  ? LEU A 43  ? PHE A 84  LEU A 86  
AA2 2 ARG A 30  ? LEU A 35  ? ARG A 73  LEU A 78  
AA2 3 GLY B 105 ? THR B 109 ? GLY B 114 THR B 118 
AA2 4 GLY B 112 ? VAL B 117 ? GLY B 121 VAL B 126 
AA2 5 TYR B 152 ? ALA B 155 ? TYR B 161 ALA B 164 
AA2 6 GLY B 144 ? VAL B 146 ? GLY B 153 VAL B 155 
AA3 1 LYS B 98  ? THR B 102 ? LYS B 107 THR B 111 
AA3 2 VAL B 86  ? ALA B 90  ? VAL B 95  ALA B 99  
AA3 3 PRO B 129 ? LEU B 131 ? PRO B 138 LEU B 140 
AA3 4 VAL B 137 ? LEU B 140 ? VAL B 146 LEU B 149 
# 
loop_
_pdbx_struct_sheet_hbond.sheet_id 
_pdbx_struct_sheet_hbond.range_id_1 
_pdbx_struct_sheet_hbond.range_id_2 
_pdbx_struct_sheet_hbond.range_1_label_atom_id 
_pdbx_struct_sheet_hbond.range_1_label_comp_id 
_pdbx_struct_sheet_hbond.range_1_label_asym_id 
_pdbx_struct_sheet_hbond.range_1_label_seq_id 
_pdbx_struct_sheet_hbond.range_1_PDB_ins_code 
_pdbx_struct_sheet_hbond.range_1_auth_atom_id 
_pdbx_struct_sheet_hbond.range_1_auth_comp_id 
_pdbx_struct_sheet_hbond.range_1_auth_asym_id 
_pdbx_struct_sheet_hbond.range_1_auth_seq_id 
_pdbx_struct_sheet_hbond.range_2_label_atom_id 
_pdbx_struct_sheet_hbond.range_2_label_comp_id 
_pdbx_struct_sheet_hbond.range_2_label_asym_id 
_pdbx_struct_sheet_hbond.range_2_label_seq_id 
_pdbx_struct_sheet_hbond.range_2_PDB_ins_code 
_pdbx_struct_sheet_hbond.range_2_auth_atom_id 
_pdbx_struct_sheet_hbond.range_2_auth_comp_id 
_pdbx_struct_sheet_hbond.range_2_auth_asym_id 
_pdbx_struct_sheet_hbond.range_2_auth_seq_id 
AA1 1 2 O LEU B 56  ? O LEU B 65  N LEU B 49  ? N LEU B 58  
AA1 2 3 O ARG B 50  ? O ARG B 59  N ILE A 10  ? N ILE A 53  
AA1 3 4 N ALA A 13  ? N ALA A 56  O VAL B 13  ? O VAL B 22  
AA1 4 5 N GLY B 12  ? N GLY B 21  O MET B 32  ? O MET B 41  
AA1 5 6 N GLN B 33  ? N GLN B 42  O VAL B 36  ? O VAL B 45  
AA1 6 7 N THR B 39  ? N THR B 48  O VAL B 68  ? O VAL B 77  
AA1 7 8 O SER B 69  ? O SER B 78  N TRP B 60  ? N TRP B 69  
AA2 1 2 O SER A 42  ? O SER A 85  N ALA A 34  ? N ALA A 77  
AA2 2 3 N LEU A 31  ? N LEU A 74  O LYS B 108 ? O LYS B 117 
AA2 3 4 N PHE B 107 ? N PHE B 116 O ILE B 114 ? O ILE B 123 
AA2 4 5 N VAL B 117 ? N VAL B 126 O SER B 154 ? O SER B 163 
AA2 5 6 O VAL B 153 ? O VAL B 162 N VAL B 145 ? N VAL B 154 
AA3 1 2 O THR B 102 ? O THR B 111 N VAL B 86  ? N VAL B 95  
AA3 2 3 N LEU B 89  ? N LEU B 98  O PRO B 129 ? O PRO B 138 
AA3 3 4 N ILE B 130 ? N ILE B 139 O GLY B 139 ? O GLY B 148 
# 
_pdbx_entry_details.entry_id                   7I1Z 
_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 
# 
_pdbx_validate_close_contact.id               1 
_pdbx_validate_close_contact.PDB_model_num    1 
_pdbx_validate_close_contact.auth_atom_id_1   OE1 
_pdbx_validate_close_contact.auth_asym_id_1   B 
_pdbx_validate_close_contact.auth_comp_id_1   GLU 
_pdbx_validate_close_contact.auth_seq_id_1    17 
_pdbx_validate_close_contact.PDB_ins_code_1   ? 
_pdbx_validate_close_contact.label_alt_id_1   ? 
_pdbx_validate_close_contact.auth_atom_id_2   O 
_pdbx_validate_close_contact.auth_asym_id_2   B 
_pdbx_validate_close_contact.auth_comp_id_2   HOH 
_pdbx_validate_close_contact.auth_seq_id_2    301 
_pdbx_validate_close_contact.PDB_ins_code_2   ? 
_pdbx_validate_close_contact.label_alt_id_2   ? 
_pdbx_validate_close_contact.dist             1.97 
# 
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 ? ? 60.23   70.50   
2 1 LEU B 30 ? ? -108.77 -168.90 
3 1 CYS B 80 ? ? 80.59   -4.63   
4 1 LEU B 92 ? ? -124.78 -55.96  
# 
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 335 ? I HOH . 
2 1 B HOH 369 ? I HOH . 
3 1 B HOH 372 ? I HOH . 
# 
loop_
_pdbx_unobs_or_zero_occ_residues.id 
_pdbx_unobs_or_zero_occ_residues.PDB_model_num 
_pdbx_unobs_or_zero_occ_residues.polymer_flag 
_pdbx_unobs_or_zero_occ_residues.occupancy_flag 
_pdbx_unobs_or_zero_occ_residues.auth_asym_id 
_pdbx_unobs_or_zero_occ_residues.auth_comp_id 
_pdbx_unobs_or_zero_occ_residues.auth_seq_id 
_pdbx_unobs_or_zero_occ_residues.PDB_ins_code 
_pdbx_unobs_or_zero_occ_residues.label_asym_id 
_pdbx_unobs_or_zero_occ_residues.label_comp_id 
_pdbx_unobs_or_zero_occ_residues.label_seq_id 
1  1 Y 1 A SER 44  ? A SER 1   
2  1 Y 1 A MET 45  ? A MET 2   
3  1 Y 1 A GLY 46  ? A GLY 3   
4  1 Y 1 A LYS 47  ? A LYS 4   
5  1 Y 1 A SER 48  ? A SER 5   
6  1 Y 1 A VAL 49  ? A VAL 6   
7  1 Y 1 A GLU 89  ? A GLU 46  
8  1 Y 1 B MET 10  ? B MET 1   
9  1 Y 1 B LYS 11  ? B LYS 2   
10 1 Y 1 B GLU 12  ? B GLU 3   
11 1 Y 1 B VAL 13  ? B VAL 4   
12 1 Y 1 B LYS 14  ? B LYS 5   
13 1 Y 1 B LYS 15  ? B LYS 6   
14 1 Y 1 B GLU 172 ? B GLU 163 
15 1 Y 1 B GLU 173 ? B GLU 164 
16 1 Y 1 B THR 174 ? B THR 165 
17 1 Y 1 B PRO 175 ? B PRO 166 
18 1 Y 1 B VAL 176 ? B VAL 167 
19 1 Y 1 B GLU 177 ? B GLU 168 
# 
loop_
_chem_comp_atom.comp_id 
_chem_comp_atom.atom_id 
_chem_comp_atom.type_symbol 
_chem_comp_atom.pdbx_aromatic_flag 
_chem_comp_atom.pdbx_stereo_config 
_chem_comp_atom.pdbx_ordinal 
A1BXQ N1   N N N 1   
A1BXQ N3   N Y N 2   
A1BXQ C4   C Y N 3   
A1BXQ C5   C N N 4   
A1BXQ C6   C Y N 5   
A1BXQ C7   C Y N 6   
A1BXQ C8   C Y N 7   
A1BXQ C10  C Y N 8   
A1BXQ C13  C Y N 9   
A1BXQ C15  C Y N 10  
A1BXQ C17  C Y N 11  
A1BXQ C20  C N N 12  
A1BXQ C21  C N R 13  
A1BXQ C22  C N N 14  
A1BXQ C1   C N N 15  
A1BXQ C2   C Y N 16  
A1BXQ C3   C Y N 17  
A1BXQ O1   O N N 18  
A1BXQ C9   C Y N 19  
A1BXQ C11  C N N 20  
A1BXQ C12  C Y N 21  
A1BXQ C14  C Y N 22  
A1BXQ C16  C Y N 23  
A1BXQ C18  C N N 24  
A1BXQ O2   O N N 25  
A1BXQ C19  C N N 26  
A1BXQ N2   N N N 27  
A1BXQ C23  C Y N 28  
A1BXQ H6   H N N 29  
A1BXQ H5   H N N 30  
A1BXQ H8   H N N 31  
A1BXQ H9   H N N 32  
A1BXQ H13  H N N 33  
A1BXQ H15  H N N 34  
A1BXQ H20  H N N 35  
A1BXQ H19  H N N 36  
A1BXQ H21  H N N 37  
A1BXQ H25  H N N 38  
A1BXQ H24  H N N 39  
A1BXQ H3   H N N 40  
A1BXQ H1   H N N 41  
A1BXQ H2   H N N 42  
A1BXQ H4   H N N 43  
A1BXQ H7   H N N 44  
A1BXQ H10  H N N 45  
A1BXQ H11  H N N 46  
A1BXQ H12  H N N 47  
A1BXQ H14  H N N 48  
A1BXQ H16  H N N 49  
A1BXQ H18  H N N 50  
A1BXQ H17  H N N 51  
A1BXQ H26  H N N 52  
A1BXQ H22  H N N 53  
ALA   N    N N N 54  
ALA   CA   C N S 55  
ALA   C    C N N 56  
ALA   O    O N N 57  
ALA   CB   C N N 58  
ALA   OXT  O N N 59  
ALA   H    H N N 60  
ALA   H2   H N N 61  
ALA   HA   H N N 62  
ALA   HB1  H N N 63  
ALA   HB2  H N N 64  
ALA   HB3  H N N 65  
ALA   HXT  H N N 66  
ARG   N    N N N 67  
ARG   CA   C N S 68  
ARG   C    C N N 69  
ARG   O    O N N 70  
ARG   CB   C N N 71  
ARG   CG   C N N 72  
ARG   CD   C N N 73  
ARG   NE   N N N 74  
ARG   CZ   C N N 75  
ARG   NH1  N N N 76  
ARG   NH2  N N N 77  
ARG   OXT  O N N 78  
ARG   H    H N N 79  
ARG   H2   H N N 80  
ARG   HA   H N N 81  
ARG   HB2  H N N 82  
ARG   HB3  H N N 83  
ARG   HG2  H N N 84  
ARG   HG3  H N N 85  
ARG   HD2  H N N 86  
ARG   HD3  H N N 87  
ARG   HE   H N N 88  
ARG   HH11 H N N 89  
ARG   HH12 H N N 90  
ARG   HH21 H N N 91  
ARG   HH22 H N N 92  
ARG   HXT  H N N 93  
ASN   N    N N N 94  
ASN   CA   C N S 95  
ASN   C    C N N 96  
ASN   O    O N N 97  
ASN   CB   C N N 98  
ASN   CG   C N N 99  
ASN   OD1  O N N 100 
ASN   ND2  N N N 101 
ASN   OXT  O N N 102 
ASN   H    H N N 103 
ASN   H2   H N N 104 
ASN   HA   H N N 105 
ASN   HB2  H N N 106 
ASN   HB3  H N N 107 
ASN   HD21 H N N 108 
ASN   HD22 H N N 109 
ASN   HXT  H N N 110 
ASP   N    N N N 111 
ASP   CA   C N S 112 
ASP   C    C N N 113 
ASP   O    O N N 114 
ASP   CB   C N N 115 
ASP   CG   C N N 116 
ASP   OD1  O N N 117 
ASP   OD2  O N N 118 
ASP   OXT  O N N 119 
ASP   H    H N N 120 
ASP   H2   H N N 121 
ASP   HA   H N N 122 
ASP   HB2  H N N 123 
ASP   HB3  H N N 124 
ASP   HD2  H N N 125 
ASP   HXT  H N N 126 
CYS   N    N N N 127 
CYS   CA   C N R 128 
CYS   C    C N N 129 
CYS   O    O N N 130 
CYS   CB   C N N 131 
CYS   SG   S N N 132 
CYS   OXT  O N N 133 
CYS   H    H N N 134 
CYS   H2   H N N 135 
CYS   HA   H N N 136 
CYS   HB2  H N N 137 
CYS   HB3  H N N 138 
CYS   HG   H N N 139 
CYS   HXT  H N N 140 
DMS   S    S N N 141 
DMS   O    O N N 142 
DMS   C1   C N N 143 
DMS   C2   C N N 144 
DMS   H11  H N N 145 
DMS   H12  H N N 146 
DMS   H13  H N N 147 
DMS   H21  H N N 148 
DMS   H22  H N N 149 
DMS   H23  H N N 150 
GLN   N    N N N 151 
GLN   CA   C N S 152 
GLN   C    C N N 153 
GLN   O    O N N 154 
GLN   CB   C N N 155 
GLN   CG   C N N 156 
GLN   CD   C N N 157 
GLN   OE1  O N N 158 
GLN   NE2  N N N 159 
GLN   OXT  O N N 160 
GLN   H    H N N 161 
GLN   H2   H N N 162 
GLN   HA   H N N 163 
GLN   HB2  H N N 164 
GLN   HB3  H N N 165 
GLN   HG2  H N N 166 
GLN   HG3  H N N 167 
GLN   HE21 H N N 168 
GLN   HE22 H N N 169 
GLN   HXT  H N N 170 
GLU   N    N N N 171 
GLU   CA   C N S 172 
GLU   C    C N N 173 
GLU   O    O N N 174 
GLU   CB   C N N 175 
GLU   CG   C N N 176 
GLU   CD   C N N 177 
GLU   OE1  O N N 178 
GLU   OE2  O N N 179 
GLU   OXT  O N N 180 
GLU   H    H N N 181 
GLU   H2   H N N 182 
GLU   HA   H N N 183 
GLU   HB2  H N N 184 
GLU   HB3  H N N 185 
GLU   HG2  H N N 186 
GLU   HG3  H N N 187 
GLU   HE2  H N N 188 
GLU   HXT  H N N 189 
GLY   N    N N N 190 
GLY   CA   C N N 191 
GLY   C    C N N 192 
GLY   O    O N N 193 
GLY   OXT  O N N 194 
GLY   H    H N N 195 
GLY   H2   H N N 196 
GLY   HA2  H N N 197 
GLY   HA3  H N N 198 
GLY   HXT  H N N 199 
HIS   N    N N N 200 
HIS   CA   C N S 201 
HIS   C    C N N 202 
HIS   O    O N N 203 
HIS   CB   C N N 204 
HIS   CG   C Y N 205 
HIS   ND1  N Y N 206 
HIS   CD2  C Y N 207 
HIS   CE1  C Y N 208 
HIS   NE2  N Y N 209 
HIS   OXT  O N N 210 
HIS   H    H N N 211 
HIS   H2   H N N 212 
HIS   HA   H N N 213 
HIS   HB2  H N N 214 
HIS   HB3  H N N 215 
HIS   HD1  H N N 216 
HIS   HD2  H N N 217 
HIS   HE1  H N N 218 
HIS   HE2  H N N 219 
HIS   HXT  H N N 220 
HOH   O    O N N 221 
HOH   H1   H N N 222 
HOH   H2   H N N 223 
ILE   N    N N N 224 
ILE   CA   C N S 225 
ILE   C    C N N 226 
ILE   O    O N N 227 
ILE   CB   C N S 228 
ILE   CG1  C N N 229 
ILE   CG2  C N N 230 
ILE   CD1  C N N 231 
ILE   OXT  O N N 232 
ILE   H    H N N 233 
ILE   H2   H N N 234 
ILE   HA   H N N 235 
ILE   HB   H N N 236 
ILE   HG12 H N N 237 
ILE   HG13 H N N 238 
ILE   HG21 H N N 239 
ILE   HG22 H N N 240 
ILE   HG23 H N N 241 
ILE   HD11 H N N 242 
ILE   HD12 H N N 243 
ILE   HD13 H N N 244 
ILE   HXT  H N N 245 
LEU   N    N N N 246 
LEU   CA   C N S 247 
LEU   C    C N N 248 
LEU   O    O N N 249 
LEU   CB   C N N 250 
LEU   CG   C N N 251 
LEU   CD1  C N N 252 
LEU   CD2  C N N 253 
LEU   OXT  O N N 254 
LEU   H    H N N 255 
LEU   H2   H N N 256 
LEU   HA   H N N 257 
LEU   HB2  H N N 258 
LEU   HB3  H N N 259 
LEU   HG   H N N 260 
LEU   HD11 H N N 261 
LEU   HD12 H N N 262 
LEU   HD13 H N N 263 
LEU   HD21 H N N 264 
LEU   HD22 H N N 265 
LEU   HD23 H N N 266 
LEU   HXT  H N N 267 
LYS   N    N N N 268 
LYS   CA   C N S 269 
LYS   C    C N N 270 
LYS   O    O N N 271 
LYS   CB   C N N 272 
LYS   CG   C N N 273 
LYS   CD   C N N 274 
LYS   CE   C N N 275 
LYS   NZ   N N N 276 
LYS   OXT  O N N 277 
LYS   H    H N N 278 
LYS   H2   H N N 279 
LYS   HA   H N N 280 
LYS   HB2  H N N 281 
LYS   HB3  H N N 282 
LYS   HG2  H N N 283 
LYS   HG3  H N N 284 
LYS   HD2  H N N 285 
LYS   HD3  H N N 286 
LYS   HE2  H N N 287 
LYS   HE3  H N N 288 
LYS   HZ1  H N N 289 
LYS   HZ2  H N N 290 
LYS   HZ3  H N N 291 
LYS   HXT  H N N 292 
MET   N    N N N 293 
MET   CA   C N S 294 
MET   C    C N N 295 
MET   O    O N N 296 
MET   CB   C N N 297 
MET   CG   C N N 298 
MET   SD   S N N 299 
MET   CE   C N N 300 
MET   OXT  O N N 301 
MET   H    H N N 302 
MET   H2   H N N 303 
MET   HA   H N N 304 
MET   HB2  H N N 305 
MET   HB3  H N N 306 
MET   HG2  H N N 307 
MET   HG3  H N N 308 
MET   HE1  H N N 309 
MET   HE2  H N N 310 
MET   HE3  H N N 311 
MET   HXT  H N N 312 
PHE   N    N N N 313 
PHE   CA   C N S 314 
PHE   C    C N N 315 
PHE   O    O N N 316 
PHE   CB   C N N 317 
PHE   CG   C Y N 318 
PHE   CD1  C Y N 319 
PHE   CD2  C Y N 320 
PHE   CE1  C Y N 321 
PHE   CE2  C Y N 322 
PHE   CZ   C Y N 323 
PHE   OXT  O N N 324 
PHE   H    H N N 325 
PHE   H2   H N N 326 
PHE   HA   H N N 327 
PHE   HB2  H N N 328 
PHE   HB3  H N N 329 
PHE   HD1  H N N 330 
PHE   HD2  H N N 331 
PHE   HE1  H N N 332 
PHE   HE2  H N N 333 
PHE   HZ   H N N 334 
PHE   HXT  H N N 335 
PRO   N    N N N 336 
PRO   CA   C N S 337 
PRO   C    C N N 338 
PRO   O    O N N 339 
PRO   CB   C N N 340 
PRO   CG   C N N 341 
PRO   CD   C N N 342 
PRO   OXT  O N N 343 
PRO   H    H N N 344 
PRO   HA   H N N 345 
PRO   HB2  H N N 346 
PRO   HB3  H N N 347 
PRO   HG2  H N N 348 
PRO   HG3  H N N 349 
PRO   HD2  H N N 350 
PRO   HD3  H N N 351 
PRO   HXT  H N N 352 
SER   N    N N N 353 
SER   CA   C N S 354 
SER   C    C N N 355 
SER   O    O N N 356 
SER   CB   C N N 357 
SER   OG   O N N 358 
SER   OXT  O N N 359 
SER   H    H N N 360 
SER   H2   H N N 361 
SER   HA   H N N 362 
SER   HB2  H N N 363 
SER   HB3  H N N 364 
SER   HG   H N N 365 
SER   HXT  H N N 366 
THR   N    N N N 367 
THR   CA   C N S 368 
THR   C    C N N 369 
THR   O    O N N 370 
THR   CB   C N R 371 
THR   OG1  O N N 372 
THR   CG2  C N N 373 
THR   OXT  O N N 374 
THR   H    H N N 375 
THR   H2   H N N 376 
THR   HA   H N N 377 
THR   HB   H N N 378 
THR   HG1  H N N 379 
THR   HG21 H N N 380 
THR   HG22 H N N 381 
THR   HG23 H N N 382 
THR   HXT  H N N 383 
TRP   N    N N N 384 
TRP   CA   C N S 385 
TRP   C    C N N 386 
TRP   O    O N N 387 
TRP   CB   C N N 388 
TRP   CG   C Y N 389 
TRP   CD1  C Y N 390 
TRP   CD2  C Y N 391 
TRP   NE1  N Y N 392 
TRP   CE2  C Y N 393 
TRP   CE3  C Y N 394 
TRP   CZ2  C Y N 395 
TRP   CZ3  C Y N 396 
TRP   CH2  C Y N 397 
TRP   OXT  O N N 398 
TRP   H    H N N 399 
TRP   H2   H N N 400 
TRP   HA   H N N 401 
TRP   HB2  H N N 402 
TRP   HB3  H N N 403 
TRP   HD1  H N N 404 
TRP   HE1  H N N 405 
TRP   HE3  H N N 406 
TRP   HZ2  H N N 407 
TRP   HZ3  H N N 408 
TRP   HH2  H N N 409 
TRP   HXT  H N N 410 
TYR   N    N N N 411 
TYR   CA   C N S 412 
TYR   C    C N N 413 
TYR   O    O N N 414 
TYR   CB   C N N 415 
TYR   CG   C Y N 416 
TYR   CD1  C Y N 417 
TYR   CD2  C Y N 418 
TYR   CE1  C Y N 419 
TYR   CE2  C Y N 420 
TYR   CZ   C Y N 421 
TYR   OH   O N N 422 
TYR   OXT  O N N 423 
TYR   H    H N N 424 
TYR   H2   H N N 425 
TYR   HA   H N N 426 
TYR   HB2  H N N 427 
TYR   HB3  H N N 428 
TYR   HD1  H N N 429 
TYR   HD2  H N N 430 
TYR   HE1  H N N 431 
TYR   HE2  H N N 432 
TYR   HH   H N N 433 
TYR   HXT  H N N 434 
VAL   N    N N N 435 
VAL   CA   C N S 436 
VAL   C    C N N 437 
VAL   O    O N N 438 
VAL   CB   C N N 439 
VAL   CG1  C N N 440 
VAL   CG2  C N N 441 
VAL   OXT  O N N 442 
VAL   H    H N N 443 
VAL   H2   H N N 444 
VAL   HA   H N N 445 
VAL   HB   H N N 446 
VAL   HG11 H N N 447 
VAL   HG12 H N N 448 
VAL   HG13 H N N 449 
VAL   HG21 H N N 450 
VAL   HG22 H N N 451 
VAL   HG23 H N N 452 
VAL   HXT  H N N 453 
# 
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 
A1BXQ C1  C2   sing N N 1   
A1BXQ C2  C3   doub Y N 2   
A1BXQ C3  C4   sing Y N 3   
A1BXQ C4  C5   sing N N 4   
A1BXQ C5  O1   sing N N 5   
A1BXQ C4  C6   doub Y N 6   
A1BXQ C6  C7   sing Y N 7   
A1BXQ C7  C8   doub Y N 8   
A1BXQ C8  C9   sing Y N 9   
A1BXQ C9  C10  doub Y N 10  
A1BXQ C10 C11  sing N N 11  
A1BXQ C11 C12  sing N N 12  
A1BXQ C12 C13  doub Y N 13  
A1BXQ C13 C14  sing Y N 14  
A1BXQ C14 C15  doub Y N 15  
A1BXQ C15 C16  sing Y N 16  
A1BXQ C16 C17  doub Y N 17  
A1BXQ C17 C18  sing N N 18  
A1BXQ C18 O2   doub N N 19  
A1BXQ C18 N1   sing N N 20  
A1BXQ N1  C19  sing N N 21  
A1BXQ C19 C20  sing N N 22  
A1BXQ C20 C21  sing N N 23  
A1BXQ C21 N2   sing N N 24  
A1BXQ C21 C22  sing N N 25  
A1BXQ C10 C23  sing Y N 26  
A1BXQ C23 N3   doub Y N 27  
A1BXQ C2  N3   sing Y N 28  
A1BXQ C6  C23  sing Y N 29  
A1BXQ C12 C17  sing Y N 30  
A1BXQ N1  C22  sing N N 31  
A1BXQ C5  H6   sing N N 32  
A1BXQ C5  H5   sing N N 33  
A1BXQ C7  H8   sing N N 34  
A1BXQ C8  H9   sing N N 35  
A1BXQ C13 H13  sing N N 36  
A1BXQ C15 H15  sing N N 37  
A1BXQ C20 H20  sing N N 38  
A1BXQ C20 H19  sing N N 39  
A1BXQ C21 H21  sing N N 40  
A1BXQ C22 H25  sing N N 41  
A1BXQ C22 H24  sing N N 42  
A1BXQ C1  H3   sing N N 43  
A1BXQ C1  H1   sing N N 44  
A1BXQ C1  H2   sing N N 45  
A1BXQ C3  H4   sing N N 46  
A1BXQ O1  H7   sing N N 47  
A1BXQ C9  H10  sing N N 48  
A1BXQ C11 H11  sing N N 49  
A1BXQ C11 H12  sing N N 50  
A1BXQ C14 H14  sing N N 51  
A1BXQ C16 H16  sing N N 52  
A1BXQ C19 H18  sing N N 53  
A1BXQ C19 H17  sing N N 54  
A1BXQ N2  H26  sing N N 55  
A1BXQ N2  H22  sing N N 56  
ALA   N   CA   sing N N 57  
ALA   N   H    sing N N 58  
ALA   N   H2   sing N N 59  
ALA   CA  C    sing N N 60  
ALA   CA  CB   sing N N 61  
ALA   CA  HA   sing N N 62  
ALA   C   O    doub N N 63  
ALA   C   OXT  sing N N 64  
ALA   CB  HB1  sing N N 65  
ALA   CB  HB2  sing N N 66  
ALA   CB  HB3  sing N N 67  
ALA   OXT HXT  sing N N 68  
ARG   N   CA   sing N N 69  
ARG   N   H    sing N N 70  
ARG   N   H2   sing N N 71  
ARG   CA  C    sing N N 72  
ARG   CA  CB   sing N N 73  
ARG   CA  HA   sing N N 74  
ARG   C   O    doub N N 75  
ARG   C   OXT  sing N N 76  
ARG   CB  CG   sing N N 77  
ARG   CB  HB2  sing N N 78  
ARG   CB  HB3  sing N N 79  
ARG   CG  CD   sing N N 80  
ARG   CG  HG2  sing N N 81  
ARG   CG  HG3  sing N N 82  
ARG   CD  NE   sing N N 83  
ARG   CD  HD2  sing N N 84  
ARG   CD  HD3  sing N N 85  
ARG   NE  CZ   sing N N 86  
ARG   NE  HE   sing N N 87  
ARG   CZ  NH1  sing N N 88  
ARG   CZ  NH2  doub N N 89  
ARG   NH1 HH11 sing N N 90  
ARG   NH1 HH12 sing N N 91  
ARG   NH2 HH21 sing N N 92  
ARG   NH2 HH22 sing N N 93  
ARG   OXT HXT  sing N N 94  
ASN   N   CA   sing N N 95  
ASN   N   H    sing N N 96  
ASN   N   H2   sing N N 97  
ASN   CA  C    sing N N 98  
ASN   CA  CB   sing N N 99  
ASN   CA  HA   sing N N 100 
ASN   C   O    doub N N 101 
ASN   C   OXT  sing N N 102 
ASN   CB  CG   sing N N 103 
ASN   CB  HB2  sing N N 104 
ASN   CB  HB3  sing N N 105 
ASN   CG  OD1  doub N N 106 
ASN   CG  ND2  sing N N 107 
ASN   ND2 HD21 sing N N 108 
ASN   ND2 HD22 sing N N 109 
ASN   OXT HXT  sing N N 110 
ASP   N   CA   sing N N 111 
ASP   N   H    sing N N 112 
ASP   N   H2   sing N N 113 
ASP   CA  C    sing N N 114 
ASP   CA  CB   sing N N 115 
ASP   CA  HA   sing N N 116 
ASP   C   O    doub N N 117 
ASP   C   OXT  sing N N 118 
ASP   CB  CG   sing N N 119 
ASP   CB  HB2  sing N N 120 
ASP   CB  HB3  sing N N 121 
ASP   CG  OD1  doub N N 122 
ASP   CG  OD2  sing N N 123 
ASP   OD2 HD2  sing N N 124 
ASP   OXT HXT  sing N N 125 
CYS   N   CA   sing N N 126 
CYS   N   H    sing N N 127 
CYS   N   H2   sing N N 128 
CYS   CA  C    sing N N 129 
CYS   CA  CB   sing N N 130 
CYS   CA  HA   sing N N 131 
CYS   C   O    doub N N 132 
CYS   C   OXT  sing N N 133 
CYS   CB  SG   sing N N 134 
CYS   CB  HB2  sing N N 135 
CYS   CB  HB3  sing N N 136 
CYS   SG  HG   sing N N 137 
CYS   OXT HXT  sing N N 138 
DMS   S   O    doub N N 139 
DMS   S   C1   sing N N 140 
DMS   S   C2   sing N N 141 
DMS   C1  H11  sing N N 142 
DMS   C1  H12  sing N N 143 
DMS   C1  H13  sing N N 144 
DMS   C2  H21  sing N N 145 
DMS   C2  H22  sing N N 146 
DMS   C2  H23  sing N N 147 
GLN   N   CA   sing N N 148 
GLN   N   H    sing N N 149 
GLN   N   H2   sing N N 150 
GLN   CA  C    sing N N 151 
GLN   CA  CB   sing N N 152 
GLN   CA  HA   sing N N 153 
GLN   C   O    doub N N 154 
GLN   C   OXT  sing N N 155 
GLN   CB  CG   sing N N 156 
GLN   CB  HB2  sing N N 157 
GLN   CB  HB3  sing N N 158 
GLN   CG  CD   sing N N 159 
GLN   CG  HG2  sing N N 160 
GLN   CG  HG3  sing N N 161 
GLN   CD  OE1  doub N N 162 
GLN   CD  NE2  sing N N 163 
GLN   NE2 HE21 sing N N 164 
GLN   NE2 HE22 sing N N 165 
GLN   OXT HXT  sing N N 166 
GLU   N   CA   sing N N 167 
GLU   N   H    sing N N 168 
GLU   N   H2   sing N N 169 
GLU   CA  C    sing N N 170 
GLU   CA  CB   sing N N 171 
GLU   CA  HA   sing N N 172 
GLU   C   O    doub N N 173 
GLU   C   OXT  sing N N 174 
GLU   CB  CG   sing N N 175 
GLU   CB  HB2  sing N N 176 
GLU   CB  HB3  sing N N 177 
GLU   CG  CD   sing N N 178 
GLU   CG  HG2  sing N N 179 
GLU   CG  HG3  sing N N 180 
GLU   CD  OE1  doub N N 181 
GLU   CD  OE2  sing N N 182 
GLU   OE2 HE2  sing N N 183 
GLU   OXT HXT  sing N N 184 
GLY   N   CA   sing N N 185 
GLY   N   H    sing N N 186 
GLY   N   H2   sing N N 187 
GLY   CA  C    sing N N 188 
GLY   CA  HA2  sing N N 189 
GLY   CA  HA3  sing N N 190 
GLY   C   O    doub N N 191 
GLY   C   OXT  sing N N 192 
GLY   OXT HXT  sing N N 193 
HIS   N   CA   sing N N 194 
HIS   N   H    sing N N 195 
HIS   N   H2   sing N N 196 
HIS   CA  C    sing N N 197 
HIS   CA  CB   sing N N 198 
HIS   CA  HA   sing N N 199 
HIS   C   O    doub N N 200 
HIS   C   OXT  sing N N 201 
HIS   CB  CG   sing N N 202 
HIS   CB  HB2  sing N N 203 
HIS   CB  HB3  sing N N 204 
HIS   CG  ND1  sing Y N 205 
HIS   CG  CD2  doub Y N 206 
HIS   ND1 CE1  doub Y N 207 
HIS   ND1 HD1  sing N N 208 
HIS   CD2 NE2  sing Y N 209 
HIS   CD2 HD2  sing N N 210 
HIS   CE1 NE2  sing Y N 211 
HIS   CE1 HE1  sing N N 212 
HIS   NE2 HE2  sing N N 213 
HIS   OXT HXT  sing N N 214 
HOH   O   H1   sing N N 215 
HOH   O   H2   sing N N 216 
ILE   N   CA   sing N N 217 
ILE   N   H    sing N N 218 
ILE   N   H2   sing N N 219 
ILE   CA  C    sing N N 220 
ILE   CA  CB   sing N N 221 
ILE   CA  HA   sing N N 222 
ILE   C   O    doub N N 223 
ILE   C   OXT  sing N N 224 
ILE   CB  CG1  sing N N 225 
ILE   CB  CG2  sing N N 226 
ILE   CB  HB   sing N N 227 
ILE   CG1 CD1  sing N N 228 
ILE   CG1 HG12 sing N N 229 
ILE   CG1 HG13 sing N N 230 
ILE   CG2 HG21 sing N N 231 
ILE   CG2 HG22 sing N N 232 
ILE   CG2 HG23 sing N N 233 
ILE   CD1 HD11 sing N N 234 
ILE   CD1 HD12 sing N N 235 
ILE   CD1 HD13 sing N N 236 
ILE   OXT HXT  sing N N 237 
LEU   N   CA   sing N N 238 
LEU   N   H    sing N N 239 
LEU   N   H2   sing N N 240 
LEU   CA  C    sing N N 241 
LEU   CA  CB   sing N N 242 
LEU   CA  HA   sing N N 243 
LEU   C   O    doub N N 244 
LEU   C   OXT  sing N N 245 
LEU   CB  CG   sing N N 246 
LEU   CB  HB2  sing N N 247 
LEU   CB  HB3  sing N N 248 
LEU   CG  CD1  sing N N 249 
LEU   CG  CD2  sing N N 250 
LEU   CG  HG   sing N N 251 
LEU   CD1 HD11 sing N N 252 
LEU   CD1 HD12 sing N N 253 
LEU   CD1 HD13 sing N N 254 
LEU   CD2 HD21 sing N N 255 
LEU   CD2 HD22 sing N N 256 
LEU   CD2 HD23 sing N N 257 
LEU   OXT HXT  sing N N 258 
LYS   N   CA   sing N N 259 
LYS   N   H    sing N N 260 
LYS   N   H2   sing N N 261 
LYS   CA  C    sing N N 262 
LYS   CA  CB   sing N N 263 
LYS   CA  HA   sing N N 264 
LYS   C   O    doub N N 265 
LYS   C   OXT  sing N N 266 
LYS   CB  CG   sing N N 267 
LYS   CB  HB2  sing N N 268 
LYS   CB  HB3  sing N N 269 
LYS   CG  CD   sing N N 270 
LYS   CG  HG2  sing N N 271 
LYS   CG  HG3  sing N N 272 
LYS   CD  CE   sing N N 273 
LYS   CD  HD2  sing N N 274 
LYS   CD  HD3  sing N N 275 
LYS   CE  NZ   sing N N 276 
LYS   CE  HE2  sing N N 277 
LYS   CE  HE3  sing N N 278 
LYS   NZ  HZ1  sing N N 279 
LYS   NZ  HZ2  sing N N 280 
LYS   NZ  HZ3  sing N N 281 
LYS   OXT HXT  sing N N 282 
MET   N   CA   sing N N 283 
MET   N   H    sing N N 284 
MET   N   H2   sing N N 285 
MET   CA  C    sing N N 286 
MET   CA  CB   sing N N 287 
MET   CA  HA   sing N N 288 
MET   C   O    doub N N 289 
MET   C   OXT  sing N N 290 
MET   CB  CG   sing N N 291 
MET   CB  HB2  sing N N 292 
MET   CB  HB3  sing N N 293 
MET   CG  SD   sing N N 294 
MET   CG  HG2  sing N N 295 
MET   CG  HG3  sing N N 296 
MET   SD  CE   sing N N 297 
MET   CE  HE1  sing N N 298 
MET   CE  HE2  sing N N 299 
MET   CE  HE3  sing N N 300 
MET   OXT HXT  sing N N 301 
PHE   N   CA   sing N N 302 
PHE   N   H    sing N N 303 
PHE   N   H2   sing N N 304 
PHE   CA  C    sing N N 305 
PHE   CA  CB   sing N N 306 
PHE   CA  HA   sing N N 307 
PHE   C   O    doub N N 308 
PHE   C   OXT  sing N N 309 
PHE   CB  CG   sing N N 310 
PHE   CB  HB2  sing N N 311 
PHE   CB  HB3  sing N N 312 
PHE   CG  CD1  doub Y N 313 
PHE   CG  CD2  sing Y N 314 
PHE   CD1 CE1  sing Y N 315 
PHE   CD1 HD1  sing N N 316 
PHE   CD2 CE2  doub Y N 317 
PHE   CD2 HD2  sing N N 318 
PHE   CE1 CZ   doub Y N 319 
PHE   CE1 HE1  sing N N 320 
PHE   CE2 CZ   sing Y N 321 
PHE   CE2 HE2  sing N N 322 
PHE   CZ  HZ   sing N N 323 
PHE   OXT HXT  sing N N 324 
PRO   N   CA   sing N N 325 
PRO   N   CD   sing N N 326 
PRO   N   H    sing N N 327 
PRO   CA  C    sing N N 328 
PRO   CA  CB   sing N N 329 
PRO   CA  HA   sing N N 330 
PRO   C   O    doub N N 331 
PRO   C   OXT  sing N N 332 
PRO   CB  CG   sing N N 333 
PRO   CB  HB2  sing N N 334 
PRO   CB  HB3  sing N N 335 
PRO   CG  CD   sing N N 336 
PRO   CG  HG2  sing N N 337 
PRO   CG  HG3  sing N N 338 
PRO   CD  HD2  sing N N 339 
PRO   CD  HD3  sing N N 340 
PRO   OXT HXT  sing N N 341 
SER   N   CA   sing N N 342 
SER   N   H    sing N N 343 
SER   N   H2   sing N N 344 
SER   CA  C    sing N N 345 
SER   CA  CB   sing N N 346 
SER   CA  HA   sing N N 347 
SER   C   O    doub N N 348 
SER   C   OXT  sing N N 349 
SER   CB  OG   sing N N 350 
SER   CB  HB2  sing N N 351 
SER   CB  HB3  sing N N 352 
SER   OG  HG   sing N N 353 
SER   OXT HXT  sing N N 354 
THR   N   CA   sing N N 355 
THR   N   H    sing N N 356 
THR   N   H2   sing N N 357 
THR   CA  C    sing N N 358 
THR   CA  CB   sing N N 359 
THR   CA  HA   sing N N 360 
THR   C   O    doub N N 361 
THR   C   OXT  sing N N 362 
THR   CB  OG1  sing N N 363 
THR   CB  CG2  sing N N 364 
THR   CB  HB   sing N N 365 
THR   OG1 HG1  sing N N 366 
THR   CG2 HG21 sing N N 367 
THR   CG2 HG22 sing N N 368 
THR   CG2 HG23 sing N N 369 
THR   OXT HXT  sing N N 370 
TRP   N   CA   sing N N 371 
TRP   N   H    sing N N 372 
TRP   N   H2   sing N N 373 
TRP   CA  C    sing N N 374 
TRP   CA  CB   sing N N 375 
TRP   CA  HA   sing N N 376 
TRP   C   O    doub N N 377 
TRP   C   OXT  sing N N 378 
TRP   CB  CG   sing N N 379 
TRP   CB  HB2  sing N N 380 
TRP   CB  HB3  sing N N 381 
TRP   CG  CD1  doub Y N 382 
TRP   CG  CD2  sing Y N 383 
TRP   CD1 NE1  sing Y N 384 
TRP   CD1 HD1  sing N N 385 
TRP   CD2 CE2  doub Y N 386 
TRP   CD2 CE3  sing Y N 387 
TRP   NE1 CE2  sing Y N 388 
TRP   NE1 HE1  sing N N 389 
TRP   CE2 CZ2  sing Y N 390 
TRP   CE3 CZ3  doub Y N 391 
TRP   CE3 HE3  sing N N 392 
TRP   CZ2 CH2  doub Y N 393 
TRP   CZ2 HZ2  sing N N 394 
TRP   CZ3 CH2  sing Y N 395 
TRP   CZ3 HZ3  sing N N 396 
TRP   CH2 HH2  sing N N 397 
TRP   OXT HXT  sing N N 398 
TYR   N   CA   sing N N 399 
TYR   N   H    sing N N 400 
TYR   N   H2   sing N N 401 
TYR   CA  C    sing N N 402 
TYR   CA  CB   sing N N 403 
TYR   CA  HA   sing N N 404 
TYR   C   O    doub N N 405 
TYR   C   OXT  sing N N 406 
TYR   CB  CG   sing N N 407 
TYR   CB  HB2  sing N N 408 
TYR   CB  HB3  sing N N 409 
TYR   CG  CD1  doub Y N 410 
TYR   CG  CD2  sing Y N 411 
TYR   CD1 CE1  sing Y N 412 
TYR   CD1 HD1  sing N N 413 
TYR   CD2 CE2  doub Y N 414 
TYR   CD2 HD2  sing N N 415 
TYR   CE1 CZ   doub Y N 416 
TYR   CE1 HE1  sing N N 417 
TYR   CE2 CZ   sing Y N 418 
TYR   CE2 HE2  sing N N 419 
TYR   CZ  OH   sing N N 420 
TYR   OH  HH   sing N N 421 
TYR   OXT HXT  sing N N 422 
VAL   N   CA   sing N N 423 
VAL   N   H    sing N N 424 
VAL   N   H2   sing N N 425 
VAL   CA  C    sing N N 426 
VAL   CA  CB   sing N N 427 
VAL   CA  HA   sing N N 428 
VAL   C   O    doub N N 429 
VAL   C   OXT  sing N N 430 
VAL   CB  CG1  sing N N 431 
VAL   CB  CG2  sing N N 432 
VAL   CB  HB   sing N N 433 
VAL   CG1 HG11 sing N N 434 
VAL   CG1 HG12 sing N N 435 
VAL   CG1 HG13 sing N N 436 
VAL   CG2 HG21 sing N N 437 
VAL   CG2 HG22 sing N N 438 
VAL   CG2 HG23 sing N N 439 
VAL   OXT HXT  sing N N 440 
# 
_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                    7I1Z 
_atom_sites.fract_transf_matrix[1][1]   0.023637 
_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]   0.023637 
_atom_sites.fract_transf_matrix[2][3]   0.000000 
_atom_sites.fract_transf_matrix[3][1]   0.000000 
_atom_sites.fract_transf_matrix[3][2]   -0.000000 
_atom_sites.fract_transf_matrix[3][3]   0.004614 
_atom_sites.fract_transf_vector[1]      0.00000 
_atom_sites.fract_transf_vector[2]      0.00000 
_atom_sites.fract_transf_vector[3]      0.00000 
# 
loop_
_atom_type.symbol 
C 
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   ? -20.800 19.262  -7.382  1.00 72.98  ? 50  ASP   A N   1 
ATOM   2    C CA  . ASP   A 1 7   ? -22.101 18.524  -7.406  1.00 70.70  ? 50  ASP   A CA  1 
ATOM   3    C C   . ASP   A 1 7   ? -22.319 17.950  -8.815  1.00 67.87  ? 50  ASP   A C   1 
ATOM   4    O O   . ASP   A 1 7   ? -21.983 18.622  -9.817  1.00 74.21  ? 50  ASP   A O   1 
ATOM   5    C CB  . ASP   A 1 7   ? -23.264 19.392  -6.931  1.00 68.54  ? 50  ASP   A CB  1 
ATOM   6    C CG  . ASP   A 1 7   ? -24.570 18.631  -6.811  1.00 73.87  ? 50  ASP   A CG  1 
ATOM   7    O OD1 . ASP   A 1 7   ? -24.812 17.996  -5.757  1.00 77.94  ? 50  ASP   A OD1 1 
ATOM   8    O OD2 . ASP   A 1 7   ? -25.335 18.669  -7.780  1.00 84.80  ? 50  ASP   A OD2 1 
ATOM   9    N N   . MET   A 1 8   ? -22.841 16.730  -8.874  1.00 52.54  ? 51  MET   A N   1 
ATOM   10   C CA  . MET   A 1 8   ? -22.632 15.809  -10.018 1.00 49.32  ? 51  MET   A CA  1 
ATOM   11   C C   . MET   A 1 8   ? -23.983 15.468  -10.611 1.00 42.96  ? 51  MET   A C   1 
ATOM   12   O O   . MET   A 1 8   ? -24.937 15.318  -9.844  1.00 47.60  ? 51  MET   A O   1 
ATOM   13   C CB  . MET   A 1 8   ? -21.947 14.508  -9.590  1.00 53.10  ? 51  MET   A CB  1 
ATOM   14   C CG  . MET   A 1 8   ? -20.462 14.636  -9.410  1.00 54.46  ? 51  MET   A CG  1 
ATOM   15   S SD  . MET   A 1 8   ? -19.732 12.982  -9.207  1.00 57.37  ? 51  MET   A SD  1 
ATOM   16   C CE  . MET   A 1 8   ? -18.018 13.456  -8.983  1.00 53.50  ? 51  MET   A CE  1 
ATOM   17   N N   . TYR   A 1 9   ? -24.044 15.330  -11.921 1.00 39.58  ? 52  TYR   A N   1 
ATOM   18   C CA  . TYR   A 1 9   ? -25.328 15.072  -12.619 1.00 43.49  ? 52  TYR   A CA  1 
ATOM   19   C C   . TYR   A 1 9   ? -25.092 14.132  -13.788 1.00 43.76  ? 52  TYR   A C   1 
ATOM   20   O O   . TYR   A 1 9   ? -23.983 14.078  -14.320 1.00 44.88  ? 52  TYR   A O   1 
ATOM   21   C CB  . TYR   A 1 9   ? -25.991 16.398  -13.029 1.00 46.33  ? 52  TYR   A CB  1 
ATOM   22   C CG  . TYR   A 1 9   ? -25.285 17.161  -14.120 1.00 44.31  ? 52  TYR   A CG  1 
ATOM   23   C CD1 . TYR   A 1 9   ? -24.203 17.960  -13.807 1.00 45.98  ? 52  TYR   A CD1 1 
ATOM   24   C CD2 . TYR   A 1 9   ? -25.678 17.074  -15.450 1.00 46.32  ? 52  TYR   A CD2 1 
ATOM   25   C CE1 . TYR   A 1 9   ? -23.521 18.670  -14.778 1.00 47.27  ? 52  TYR   A CE1 1 
ATOM   26   C CE2 . TYR   A 1 9   ? -24.998 17.768  -16.438 1.00 49.57  ? 52  TYR   A CE2 1 
ATOM   27   C CZ  . TYR   A 1 9   ? -23.926 18.582  -16.092 1.00 48.25  ? 52  TYR   A CZ  1 
ATOM   28   O OH  . TYR   A 1 9   ? -23.211 19.251  -17.045 1.00 59.92  ? 52  TYR   A OH  1 
ATOM   29   N N   . ILE   A 1 10  ? -26.158 13.461  -14.196 1.00 43.90  ? 53  ILE   A N   1 
ATOM   30   C CA  . ILE   A 1 10  ? -26.138 12.453  -15.289 1.00 42.87  ? 53  ILE   A CA  1 
ATOM   31   C C   . ILE   A 1 10  ? -26.938 12.961  -16.512 1.00 44.40  ? 53  ILE   A C   1 
ATOM   32   O O   . ILE   A 1 10  ? -27.946 13.663  -16.342 1.00 47.89  ? 53  ILE   A O   1 
ATOM   33   C CB  . ILE   A 1 10  ? -26.632 11.092  -14.749 1.00 41.80  ? 53  ILE   A CB  1 
ATOM   34   C CG1 . ILE   A 1 10  ? -28.112 11.072  -14.408 1.00 43.27  ? 53  ILE   A CG1 1 
ATOM   35   C CG2 . ILE   A 1 10  ? -25.806 10.652  -13.553 1.00 44.67  ? 53  ILE   A CG2 1 
ATOM   36   C CD1 . ILE   A 1 10  ? -28.542 9.755   -13.834 1.00 48.37  ? 53  ILE   A CD1 1 
ATOM   37   N N   . GLU   A 1 11  ? -26.535 12.549  -17.709 1.00 45.39  ? 54  GLU   A N   1 
ATOM   38   C CA  . GLU   A 1 11  ? -27.230 12.817  -19.006 1.00 49.51  ? 54  GLU   A CA  1 
ATOM   39   C C   . GLU   A 1 11  ? -27.242 11.510  -19.808 1.00 47.75  ? 54  GLU   A C   1 
ATOM   40   O O   . GLU   A 1 11  ? -26.162 10.856  -19.936 1.00 39.12  ? 54  GLU   A O   1 
ATOM   41   C CB  . GLU   A 1 11  ? -26.504 13.875  -19.853 1.00 52.81  ? 54  GLU   A CB  1 
ATOM   42   C CG  . GLU   A 1 11  ? -26.369 15.241  -19.220 1.00 59.12  ? 54  GLU   A CG  1 
ATOM   43   C CD  . GLU   A 1 11  ? -25.517 16.225  -20.018 1.00 68.58  ? 54  GLU   A CD  1 
ATOM   44   O OE1 . GLU   A 1 11  ? -24.614 15.784  -20.759 1.00 64.92  ? 54  GLU   A OE1 1 
ATOM   45   O OE2 . GLU   A 1 11  ? -25.744 17.447  -19.888 1.00 79.32  ? 54  GLU   A OE2 1 
ATOM   46   N N   . ARG   A 1 12  ? -28.382 11.111  -20.357 1.00 47.67  ? 55  ARG   A N   1 
ATOM   47   C CA  . ARG   A 1 12  ? -28.454 9.859   -21.160 1.00 46.14  ? 55  ARG   A CA  1 
ATOM   48   C C   . ARG   A 1 12  ? -27.523 9.939   -22.376 1.00 46.61  ? 55  ARG   A C   1 
ATOM   49   O O   . ARG   A 1 12  ? -27.404 11.055  -22.990 1.00 47.95  ? 55  ARG   A O   1 
ATOM   50   C CB  . ARG   A 1 12  ? -29.887 9.627   -21.619 1.00 48.47  ? 55  ARG   A CB  1 
ATOM   51   C CG  . ARG   A 1 12  ? -30.153 8.226   -22.135 1.00 50.79  ? 55  ARG   A CG  1 
ATOM   52   C CD  . ARG   A 1 12  ? -31.580 7.765   -21.872 1.00 54.72  ? 55  ARG   A CD  1 
ATOM   53   N NE  . ARG   A 1 12  ? -31.778 6.352   -22.164 1.00 55.69  ? 55  ARG   A NE  1 
ATOM   54   C CZ  . ARG   A 1 12  ? -31.712 5.841   -23.389 1.00 54.34  ? 55  ARG   A CZ  1 
ATOM   55   N NH1 . ARG   A 1 12  ? -31.484 6.620   -24.433 1.00 63.46  ? 55  ARG   A NH1 1 
ATOM   56   N NH2 . ARG   A 1 12  ? -31.863 4.547   -23.580 1.00 53.13  ? 55  ARG   A NH2 1 
ATOM   57   N N   . ALA   A 1 13  ? -26.865 8.826   -22.758 1.00 47.36  ? 56  ALA   A N   1 
ATOM   58   C CA  . ALA   A 1 13  ? -25.886 8.820   -23.890 1.00 43.47  ? 56  ALA   A CA  1 
ATOM   59   C C   . ALA   A 1 13  ? -26.200 7.779   -24.962 1.00 38.64  ? 56  ALA   A C   1 
ATOM   60   O O   . ALA   A 1 13  ? -25.588 7.854   -26.021 1.00 40.56  ? 56  ALA   A O   1 
ATOM   61   C CB  . ALA   A 1 13  ? -24.457 8.706   -23.402 1.00 48.33  ? 56  ALA   A CB  1 
ATOM   62   N N   . GLY   A 1 14  ? -27.121 6.849   -24.729 1.00 33.41  ? 57  GLY   A N   1 
ATOM   63   C CA  . GLY   A 1 14  ? -27.462 5.828   -25.708 1.00 32.50  ? 57  GLY   A CA  1 
ATOM   64   C C   . GLY   A 1 14  ? -28.180 4.662   -25.077 1.00 40.42  ? 57  GLY   A C   1 
ATOM   65   O O   . GLY   A 1 14  ? -28.256 4.650   -23.835 1.00 41.54  ? 57  GLY   A O   1 
ATOM   66   N N   . ASP   A 1 15  ? -28.685 3.756   -25.916 1.00 43.25  ? 58  ASP   A N   1 
ATOM   67   C CA  . ASP   A 1 15  ? -29.209 2.411   -25.569 1.00 46.25  ? 58  ASP   A CA  1 
ATOM   68   C C   . ASP   A 1 15  ? -28.015 1.465   -25.373 1.00 52.26  ? 58  ASP   A C   1 
ATOM   69   O O   . ASP   A 1 15  ? -26.935 1.727   -25.941 1.00 52.51  ? 58  ASP   A O   1 
ATOM   70   C CB  . ASP   A 1 15  ? -30.110 1.850   -26.673 1.00 47.04  ? 58  ASP   A CB  1 
ATOM   71   C CG  . ASP   A 1 15  ? -31.442 2.570   -26.836 1.00 56.81  ? 58  ASP   A CG  1 
ATOM   72   O OD1 . ASP   A 1 15  ? -31.643 3.571   -26.119 1.00 42.09  ? 58  ASP   A OD1 1 
ATOM   73   O OD2 . ASP   A 1 15  ? -32.280 2.113   -27.667 1.00 53.10  ? 58  ASP   A OD2 1 
ATOM   74   N N   . ILE   A 1 16  ? -28.200 0.415   -24.575 1.00 54.96  ? 59  ILE   A N   1 
ATOM   75   C CA  . ILE   A 1 16  ? -27.185 -0.661  -24.396 1.00 54.46  ? 59  ILE   A CA  1 
ATOM   76   C C   . ILE   A 1 16  ? -27.618 -1.791  -25.334 1.00 46.17  ? 59  ILE   A C   1 
ATOM   77   O O   . ILE   A 1 16  ? -28.531 -2.555  -24.997 1.00 48.76  ? 59  ILE   A O   1 
ATOM   78   C CB  . ILE   A 1 16  ? -27.057 -1.039  -22.912 1.00 55.38  ? 59  ILE   A CB  1 
ATOM   79   C CG1 . ILE   A 1 16  ? -26.369 0.105   -22.153 1.00 49.16  ? 59  ILE   A CG1 1 
ATOM   80   C CG2 . ILE   A 1 16  ? -26.321 -2.360  -22.755 1.00 60.40  ? 59  ILE   A CG2 1 
ATOM   81   C CD1 . ILE   A 1 16  ? -26.662 0.158   -20.669 1.00 57.52  ? 59  ILE   A CD1 1 
ATOM   82   N N   A THR   A 1 17  ? -26.981 -1.841  -26.509 0.25 51.61  ? 60  THR   A N   1 
ATOM   83   N N   B THR   A 1 17  ? -26.976 -1.874  -26.499 0.25 50.76  ? 60  THR   A N   1 
ATOM   84   N N   C THR   A 1 17  ? -26.981 -1.841  -26.509 0.25 51.61  ? 60  THR   A N   1 
ATOM   85   N N   D THR   A 1 17  ? -26.976 -1.874  -26.499 0.25 50.76  ? 60  THR   A N   1 
ATOM   86   C CA  A THR   A 1 17  ? -27.280 -2.758  -27.641 0.25 50.94  ? 60  THR   A CA  1 
ATOM   87   C CA  B THR   A 1 17  ? -27.317 -2.815  -27.597 0.25 49.88  ? 60  THR   A CA  1 
ATOM   88   C CA  C THR   A 1 17  ? -27.280 -2.758  -27.641 0.25 50.94  ? 60  THR   A CA  1 
ATOM   89   C CA  D THR   A 1 17  ? -27.317 -2.815  -27.597 0.25 49.88  ? 60  THR   A CA  1 
ATOM   90   C C   A THR   A 1 17  ? -25.973 -3.252  -28.266 0.25 48.63  ? 60  THR   A C   1 
ATOM   91   C C   B THR   A 1 17  ? -26.028 -3.244  -28.307 0.25 48.24  ? 60  THR   A C   1 
ATOM   92   C C   C THR   A 1 17  ? -25.973 -3.252  -28.266 0.25 48.63  ? 60  THR   A C   1 
ATOM   93   C C   D THR   A 1 17  ? -26.028 -3.244  -28.307 0.25 48.24  ? 60  THR   A C   1 
ATOM   94   O O   A THR   A 1 17  ? -25.035 -2.435  -28.423 0.25 46.32  ? 60  THR   A O   1 
ATOM   95   O O   B THR   A 1 17  ? -25.150 -2.381  -28.535 0.25 46.47  ? 60  THR   A O   1 
ATOM   96   O O   C THR   A 1 17  ? -25.035 -2.435  -28.423 0.25 46.32  ? 60  THR   A O   1 
ATOM   97   O O   D THR   A 1 17  ? -25.150 -2.381  -28.535 0.25 46.47  ? 60  THR   A O   1 
ATOM   98   C CB  A THR   A 1 17  ? -28.110 -2.070  -28.736 0.25 51.49  ? 60  THR   A CB  1 
ATOM   99   C CB  B THR   A 1 17  ? -28.345 -2.190  -28.553 0.25 49.40  ? 60  THR   A CB  1 
ATOM   100  C CB  C THR   A 1 17  ? -28.110 -2.070  -28.736 0.25 51.49  ? 60  THR   A CB  1 
ATOM   101  C CB  D THR   A 1 17  ? -28.345 -2.190  -28.553 0.25 49.40  ? 60  THR   A CB  1 
ATOM   102  O OG1 A THR   A 1 17  ? -27.248 -1.193  -29.465 0.25 51.19  ? 60  THR   A OG1 1 
ATOM   103  O OG1 B THR   A 1 17  ? -29.623 -2.249  -27.920 0.25 49.72  ? 60  THR   A OG1 1 
ATOM   104  O OG1 C THR   A 1 17  ? -27.248 -1.193  -29.465 0.25 51.19  ? 60  THR   A OG1 1 
ATOM   105  O OG1 D THR   A 1 17  ? -29.623 -2.249  -27.920 0.25 49.72  ? 60  THR   A OG1 1 
ATOM   106  C CG2 A THR   A 1 17  ? -29.290 -1.301  -28.186 0.25 51.47  ? 60  THR   A CG2 1 
ATOM   107  C CG2 B THR   A 1 17  ? -28.420 -2.880  -29.897 0.25 48.07  ? 60  THR   A CG2 1 
ATOM   108  C CG2 C THR   A 1 17  ? -29.290 -1.301  -28.186 0.25 51.47  ? 60  THR   A CG2 1 
ATOM   109  C CG2 D THR   A 1 17  ? -28.420 -2.880  -29.897 0.25 48.07  ? 60  THR   A CG2 1 
ATOM   110  N N   . TRP   A 1 18  ? -25.925 -4.539  -28.615 1.00 46.17  ? 61  TRP   A N   1 
ATOM   111  C CA  . TRP   A 1 18  ? -24.861 -5.097  -29.483 1.00 60.24  ? 61  TRP   A CA  1 
ATOM   112  C C   . TRP   A 1 18  ? -25.119 -4.577  -30.901 1.00 61.37  ? 61  TRP   A C   1 
ATOM   113  O O   . TRP   A 1 18  ? -26.228 -4.789  -31.413 1.00 63.29  ? 61  TRP   A O   1 
ATOM   114  C CB  . TRP   A 1 18  ? -24.900 -6.629  -29.447 1.00 62.84  ? 61  TRP   A CB  1 
ATOM   115  C CG  . TRP   A 1 18  ? -23.798 -7.259  -30.239 1.00 70.22  ? 61  TRP   A CG  1 
ATOM   116  C CD1 . TRP   A 1 18  ? -23.795 -7.508  -31.577 1.00 74.75  ? 61  TRP   A CD1 1 
ATOM   117  C CD2 . TRP   A 1 18  ? -22.535 -7.726  -29.738 1.00 76.12  ? 61  TRP   A CD2 1 
ATOM   118  N NE1 . TRP   A 1 18  ? -22.608 -8.073  -31.947 1.00 77.52  ? 61  TRP   A NE1 1 
ATOM   119  C CE2 . TRP   A 1 18  ? -21.824 -8.238  -30.840 1.00 80.59  ? 61  TRP   A CE2 1 
ATOM   120  C CE3 . TRP   A 1 18  ? -21.941 -7.773  -28.474 1.00 72.38  ? 61  TRP   A CE3 1 
ATOM   121  C CZ2 . TRP   A 1 18  ? -20.550 -8.786  -30.712 1.00 84.78  ? 61  TRP   A CZ2 1 
ATOM   122  C CZ3 . TRP   A 1 18  ? -20.681 -8.305  -28.350 1.00 77.65  ? 61  TRP   A CZ3 1 
ATOM   123  C CH2 . TRP   A 1 18  ? -19.993 -8.802  -29.455 1.00 82.33  ? 61  TRP   A CH2 1 
ATOM   124  N N   A GLU   A 1 19  ? -24.121 -3.933  -31.513 0.25 61.39  ? 62  GLU   A N   1 
ATOM   125  N N   B GLU   A 1 19  ? -24.121 -3.933  -31.513 0.25 61.39  ? 62  GLU   A N   1 
ATOM   126  N N   C GLU   A 1 19  ? -24.129 -3.886  -31.481 0.25 58.64  ? 62  GLU   A N   1 
ATOM   127  N N   D GLU   A 1 19  ? -24.129 -3.886  -31.481 0.25 58.64  ? 62  GLU   A N   1 
ATOM   128  C CA  A GLU   A 1 19  ? -24.208 -3.353  -32.881 0.25 65.95  ? 62  GLU   A CA  1 
ATOM   129  C CA  B GLU   A 1 19  ? -24.208 -3.353  -32.881 0.25 65.95  ? 62  GLU   A CA  1 
ATOM   130  C CA  C GLU   A 1 19  ? -24.151 -3.369  -32.876 0.25 61.49  ? 62  GLU   A CA  1 
ATOM   131  C CA  D GLU   A 1 19  ? -24.151 -3.369  -32.876 0.25 61.49  ? 62  GLU   A CA  1 
ATOM   132  C C   A GLU   A 1 19  ? -23.417 -4.236  -33.857 0.25 64.88  ? 62  GLU   A C   1 
ATOM   133  C C   B GLU   A 1 19  ? -23.417 -4.236  -33.857 0.25 64.88  ? 62  GLU   A C   1 
ATOM   134  C C   C GLU   A 1 19  ? -23.404 -4.342  -33.792 0.25 61.75  ? 62  GLU   A C   1 
ATOM   135  C C   D GLU   A 1 19  ? -23.404 -4.342  -33.792 0.25 61.75  ? 62  GLU   A C   1 
ATOM   136  O O   A GLU   A 1 19  ? -22.170 -4.169  -33.813 0.25 61.55  ? 62  GLU   A O   1 
ATOM   137  O O   B GLU   A 1 19  ? -22.170 -4.169  -33.813 0.25 61.55  ? 62  GLU   A O   1 
ATOM   138  O O   C GLU   A 1 19  ? -22.173 -4.446  -33.641 0.25 58.91  ? 62  GLU   A O   1 
ATOM   139  O O   D GLU   A 1 19  ? -22.173 -4.446  -33.641 0.25 58.91  ? 62  GLU   A O   1 
ATOM   140  C CB  A GLU   A 1 19  ? -23.668 -1.920  -32.882 0.25 66.43  ? 62  GLU   A CB  1 
ATOM   141  C CB  B GLU   A 1 19  ? -23.668 -1.920  -32.882 0.25 66.43  ? 62  GLU   A CB  1 
ATOM   142  C CB  C GLU   A 1 19  ? -23.466 -2.003  -32.996 0.25 58.24  ? 62  GLU   A CB  1 
ATOM   143  C CB  D GLU   A 1 19  ? -23.466 -2.003  -32.996 0.25 58.24  ? 62  GLU   A CB  1 
ATOM   144  C CG  A GLU   A 1 19  ? -24.330 -1.009  -31.858 0.25 66.68  ? 62  GLU   A CG  1 
ATOM   145  C CG  B GLU   A 1 19  ? -24.330 -1.009  -31.858 0.25 66.68  ? 62  GLU   A CG  1 
ATOM   146  C CG  C GLU   A 1 19  ? -23.328 -1.553  -34.442 0.25 56.64  ? 62  GLU   A CG  1 
ATOM   147  C CG  D GLU   A 1 19  ? -23.328 -1.553  -34.442 0.25 56.64  ? 62  GLU   A CG  1 
ATOM   148  C CD  A GLU   A 1 19  ? -25.787 -0.670  -32.125 0.25 69.35  ? 62  GLU   A CD  1 
ATOM   149  C CD  B GLU   A 1 19  ? -25.787 -0.670  -32.125 0.25 69.35  ? 62  GLU   A CD  1 
ATOM   150  C CD  C GLU   A 1 19  ? -22.320 -0.452  -34.721 0.25 53.90  ? 62  GLU   A CD  1 
ATOM   151  C CD  D GLU   A 1 19  ? -22.320 -0.452  -34.721 0.25 53.90  ? 62  GLU   A CD  1 
ATOM   152  O OE1 A GLU   A 1 19  ? -26.077 -0.107  -33.207 0.25 69.54  ? 62  GLU   A OE1 1 
ATOM   153  O OE1 B GLU   A 1 19  ? -26.077 -0.107  -33.207 0.25 69.54  ? 62  GLU   A OE1 1 
ATOM   154  O OE1 C GLU   A 1 19  ? -21.586 -0.067  -33.796 0.25 50.12  ? 62  GLU   A OE1 1 
ATOM   155  O OE1 D GLU   A 1 19  ? -21.586 -0.067  -33.796 0.25 50.12  ? 62  GLU   A OE1 1 
ATOM   156  O OE2 A GLU   A 1 19  ? -26.626 -0.972  -31.252 0.25 68.11  ? 62  GLU   A OE2 1 
ATOM   157  O OE2 B GLU   A 1 19  ? -26.626 -0.972  -31.252 0.25 68.11  ? 62  GLU   A OE2 1 
ATOM   158  O OE2 C GLU   A 1 19  ? -22.280 0.014   -35.870 0.25 52.96  ? 62  GLU   A OE2 1 
ATOM   159  O OE2 D GLU   A 1 19  ? -22.280 0.014   -35.870 0.25 52.96  ? 62  GLU   A OE2 1 
ATOM   160  N N   . LYS   A 1 20  ? -24.112 -5.001  -34.715 1.00 63.44  ? 63  LYS   A N   1 
ATOM   161  C CA  . LYS   A 1 20  ? -23.467 -5.871  -35.753 1.00 67.75  ? 63  LYS   A CA  1 
ATOM   162  C C   . LYS   A 1 20  ? -22.622 -4.992  -36.662 1.00 68.37  ? 63  LYS   A C   1 
ATOM   163  O O   . LYS   A 1 20  ? -23.118 -3.916  -37.028 1.00 82.78  ? 63  LYS   A O   1 
ATOM   164  C CB  . LYS   A 1 20  ? -24.467 -6.641  -36.615 1.00 72.80  ? 63  LYS   A CB  1 
ATOM   165  C CG  . LYS   A 1 20  ? -24.761 -8.043  -36.103 1.00 87.24  ? 63  LYS   A CG  1 
ATOM   166  C CD  . LYS   A 1 20  ? -26.174 -8.530  -36.373 1.00 92.97  ? 63  LYS   A CD  1 
ATOM   167  C CE  . LYS   A 1 20  ? -26.355 -10.000 -36.039 1.00 101.66 ? 63  LYS   A CE  1 
ATOM   168  N NZ  . LYS   A 1 20  ? -27.745 -10.461 -36.277 1.00 98.29  ? 63  LYS   A NZ  1 
ATOM   169  N N   . ASP   A 1 21  ? -21.390 -5.418  -36.961 1.00 67.38  ? 64  ASP   A N   1 
ATOM   170  C CA  . ASP   A 1 21  ? -20.416 -4.634  -37.770 1.00 81.12  ? 64  ASP   A CA  1 
ATOM   171  C C   . ASP   A 1 21  ? -20.154 -3.319  -37.038 1.00 74.71  ? 64  ASP   A C   1 
ATOM   172  O O   . ASP   A 1 21  ? -20.680 -2.278  -37.468 1.00 79.21  ? 64  ASP   A O   1 
ATOM   173  C CB  . ASP   A 1 21  ? -20.897 -4.377  -39.209 1.00 94.66  ? 64  ASP   A CB  1 
ATOM   174  C CG  . ASP   A 1 21  ? -21.112 -5.628  -40.053 1.00 100.70 ? 64  ASP   A CG  1 
ATOM   175  O OD1 . ASP   A 1 21  ? -20.102 -6.172  -40.584 1.00 102.97 ? 64  ASP   A OD1 1 
ATOM   176  O OD2 . ASP   A 1 21  ? -22.291 -6.062  -40.161 1.00 89.42  ? 64  ASP   A OD2 1 
ATOM   177  N N   . ALA   A 1 22  ? -19.451 -3.422  -35.908 1.00 74.76  ? 65  ALA   A N   1 
ATOM   178  C CA  . ALA   A 1 22  ? -18.758 -2.322  -35.207 1.00 59.98  ? 65  ALA   A CA  1 
ATOM   179  C C   . ALA   A 1 22  ? -17.258 -2.518  -35.385 1.00 55.97  ? 65  ALA   A C   1 
ATOM   180  O O   . ALA   A 1 22  ? -16.829 -3.649  -35.688 1.00 61.11  ? 65  ALA   A O   1 
ATOM   181  C CB  . ALA   A 1 22  ? -19.130 -2.341  -33.752 1.00 68.61  ? 65  ALA   A CB  1 
ATOM   182  N N   . GLU   A 1 23  ? -16.491 -1.452  -35.216 1.00 57.10  ? 66  GLU   A N   1 
ATOM   183  C CA  . GLU   A 1 23  ? -15.009 -1.478  -35.284 1.00 59.73  ? 66  GLU   A CA  1 
ATOM   184  C C   . GLU   A 1 23  ? -14.517 -2.627  -34.386 1.00 68.93  ? 66  GLU   A C   1 
ATOM   185  O O   . GLU   A 1 23  ? -14.773 -2.595  -33.159 1.00 56.05  ? 66  GLU   A O   1 
ATOM   186  C CB  . GLU   A 1 23  ? -14.552 -0.080  -34.877 1.00 68.48  ? 66  GLU   A CB  1 
ATOM   187  C CG  . GLU   A 1 23  ? -13.054 0.149   -34.822 1.00 73.91  ? 66  GLU   A CG  1 
ATOM   188  C CD  . GLU   A 1 23  ? -12.723 1.521   -34.244 1.00 87.16  ? 66  GLU   A CD  1 
ATOM   189  O OE1 . GLU   A 1 23  ? -13.655 2.364   -34.103 1.00 92.76  ? 66  GLU   A OE1 1 
ATOM   190  O OE2 . GLU   A 1 23  ? -11.542 1.752   -33.909 1.00 97.99  ? 66  GLU   A OE2 1 
ATOM   191  N N   . VAL   A 1 24  ? -13.910 -3.660  -34.975 1.00 72.90  ? 67  VAL   A N   1 
ATOM   192  C CA  . VAL   A 1 24  ? -13.212 -4.756  -34.235 1.00 64.62  ? 67  VAL   A CA  1 
ATOM   193  C C   . VAL   A 1 24  ? -11.758 -4.323  -33.996 1.00 65.67  ? 67  VAL   A C   1 
ATOM   194  O O   . VAL   A 1 24  ? -11.148 -3.823  -34.933 1.00 62.93  ? 67  VAL   A O   1 
ATOM   195  C CB  . VAL   A 1 24  ? -13.316 -6.100  -34.972 1.00 66.02  ? 67  VAL   A CB  1 
ATOM   196  C CG1 . VAL   A 1 24  ? -12.603 -7.180  -34.193 1.00 64.13  ? 67  VAL   A CG1 1 
ATOM   197  C CG2 . VAL   A 1 24  ? -14.763 -6.503  -35.227 1.00 59.32  ? 67  VAL   A CG2 1 
ATOM   198  N N   . THR   A 1 25  ? -11.239 -4.418  -32.766 1.00 65.67  ? 68  THR   A N   1 
ATOM   199  C CA  . THR   A 1 25  ? -9.854  -3.960  -32.442 1.00 64.07  ? 68  THR   A CA  1 
ATOM   200  C C   . THR   A 1 25  ? -9.448  -4.398  -31.031 1.00 60.43  ? 68  THR   A C   1 
ATOM   201  O O   . THR   A 1 25  ? -10.275 -5.020  -30.380 1.00 56.42  ? 68  THR   A O   1 
ATOM   202  C CB  . THR   A 1 25  ? -9.740  -2.446  -32.638 1.00 63.82  ? 68  THR   A CB  1 
ATOM   203  O OG1 . THR   A 1 25  ? -8.371  -2.107  -32.442 1.00 69.53  ? 68  THR   A OG1 1 
ATOM   204  C CG2 . THR   A 1 25  ? -10.625 -1.653  -31.701 1.00 63.88  ? 68  THR   A CG2 1 
ATOM   205  N N   . GLY   A 1 26  ? -8.215  -4.092  -30.610 1.00 52.15  ? 69  GLY   A N   1 
ATOM   206  C CA  . GLY   A 1 26  ? -7.622  -4.493  -29.320 1.00 57.37  ? 69  GLY   A CA  1 
ATOM   207  C C   . GLY   A 1 26  ? -7.102  -5.926  -29.278 1.00 50.21  ? 69  GLY   A C   1 
ATOM   208  O O   . GLY   A 1 26  ? -7.785  -6.828  -29.773 1.00 56.73  ? 69  GLY   A O   1 
ATOM   209  N N   . ASN   A 1 27  ? -5.987  -6.126  -28.580 1.00 57.00  ? 70  ASN   A N   1 
ATOM   210  C CA  . ASN   A 1 27  ? -5.349  -7.448  -28.291 1.00 60.81  ? 70  ASN   A CA  1 
ATOM   211  C C   . ASN   A 1 27  ? -6.001  -8.111  -27.052 1.00 61.57  ? 70  ASN   A C   1 
ATOM   212  O O   . ASN   A 1 27  ? -6.994  -7.552  -26.516 1.00 55.52  ? 70  ASN   A O   1 
ATOM   213  C CB  . ASN   A 1 27  ? -3.836  -7.260  -28.166 1.00 62.15  ? 70  ASN   A CB  1 
ATOM   214  C CG  . ASN   A 1 27  ? -3.468  -6.229  -27.126 1.00 66.01  ? 70  ASN   A CG  1 
ATOM   215  O OD1 . ASN   A 1 27  ? -4.039  -5.139  -27.095 1.00 83.60  ? 70  ASN   A OD1 1 
ATOM   216  N ND2 . ASN   A 1 27  ? -2.512  -6.552  -26.274 1.00 81.33  ? 70  ASN   A ND2 1 
ATOM   217  N N   . SER   A 1 28  ? -5.512  -9.293  -26.648 1.00 54.85  ? 71  SER   A N   1 
ATOM   218  C CA  . SER   A 1 28  ? -6.084  -10.176 -25.589 1.00 51.77  ? 71  SER   A CA  1 
ATOM   219  C C   . SER   A 1 28  ? -4.992  -10.697 -24.664 1.00 46.94  ? 71  SER   A C   1 
ATOM   220  O O   . SER   A 1 28  ? -4.878  -11.896 -24.508 1.00 49.41  ? 71  SER   A O   1 
ATOM   221  C CB  . SER   A 1 28  ? -6.843  -11.351 -26.164 1.00 48.00  ? 71  SER   A CB  1 
ATOM   222  O OG  . SER   A 1 28  ? -7.606  -10.948 -27.293 1.00 59.85  ? 71  SER   A OG  1 
ATOM   223  N N   . PRO   A 1 29  ? -4.242  -9.826  -23.958 1.00 48.74  ? 72  PRO   A N   1 
ATOM   224  C CA  . PRO   A 1 29  ? -3.148  -10.258 -23.084 1.00 54.21  ? 72  PRO   A CA  1 
ATOM   225  C C   . PRO   A 1 29  ? -3.585  -11.011 -21.817 1.00 60.86  ? 72  PRO   A C   1 
ATOM   226  O O   . PRO   A 1 29  ? -4.595  -10.618 -21.183 1.00 52.04  ? 72  PRO   A O   1 
ATOM   227  C CB  . PRO   A 1 29  ? -2.473  -8.937  -22.673 1.00 55.49  ? 72  PRO   A CB  1 
ATOM   228  C CG  . PRO   A 1 29  ? -3.594  -7.906  -22.748 1.00 56.56  ? 72  PRO   A CG  1 
ATOM   229  C CD  . PRO   A 1 29  ? -4.462  -8.370  -23.903 1.00 54.78  ? 72  PRO   A CD  1 
ATOM   230  N N   . ARG   A 1 30  ? -2.819  -12.055 -21.478 1.00 58.65  ? 73  ARG   A N   1 
ATOM   231  C CA  . ARG   A 1 30  ? -2.870  -12.792 -20.186 1.00 65.01  ? 73  ARG   A CA  1 
ATOM   232  C C   . ARG   A 1 30  ? -1.837  -12.179 -19.232 1.00 68.25  ? 73  ARG   A C   1 
ATOM   233  O O   . ARG   A 1 30  ? -0.648  -12.322 -19.500 1.00 58.07  ? 73  ARG   A O   1 
ATOM   234  C CB  . ARG   A 1 30  ? -2.619  -14.283 -20.409 1.00 72.22  ? 73  ARG   A CB  1 
ATOM   235  C CG  . ARG   A 1 30  ? -3.706  -14.952 -21.236 1.00 84.89  ? 73  ARG   A CG  1 
ATOM   236  C CD  . ARG   A 1 30  ? -3.279  -16.300 -21.782 1.00 102.00 ? 73  ARG   A CD  1 
ATOM   237  N NE  . ARG   A 1 30  ? -4.276  -16.859 -22.695 1.00 107.31 ? 73  ARG   A NE  1 
ATOM   238  C CZ  . ARG   A 1 30  ? -5.290  -17.654 -22.346 1.00 110.67 ? 73  ARG   A CZ  1 
ATOM   239  N NH1 . ARG   A 1 30  ? -5.467  -18.013 -21.084 1.00 121.40 ? 73  ARG   A NH1 1 
ATOM   240  N NH2 . ARG   A 1 30  ? -6.132  -18.092 -23.268 1.00 98.41  ? 73  ARG   A NH2 1 
ATOM   241  N N   . LEU   A 1 31  ? -2.300  -11.496 -18.179 1.00 63.64  ? 74  LEU   A N   1 
ATOM   242  C CA  . LEU   A 1 31  ? -1.456  -10.710 -17.248 1.00 59.65  ? 74  LEU   A CA  1 
ATOM   243  C C   . LEU   A 1 31  ? -1.609  -11.266 -15.825 1.00 61.85  ? 74  LEU   A C   1 
ATOM   244  O O   . LEU   A 1 31  ? -2.745  -11.511 -15.365 1.00 63.04  ? 74  LEU   A O   1 
ATOM   245  C CB  . LEU   A 1 31  ? -1.862  -9.235  -17.321 1.00 62.45  ? 74  LEU   A CB  1 
ATOM   246  C CG  . LEU   A 1 31  ? -1.654  -8.533  -18.666 1.00 66.17  ? 74  LEU   A CG  1 
ATOM   247  C CD1 . LEU   A 1 31  ? -2.277  -7.143  -18.640 1.00 60.80  ? 74  LEU   A CD1 1 
ATOM   248  C CD2 . LEU   A 1 31  ? -0.172  -8.433  -19.045 1.00 61.80  ? 74  LEU   A CD2 1 
ATOM   249  N N   . ASP   A 1 32  ? -0.482  -11.461 -15.150 1.00 58.13  ? 75  ASP   A N   1 
ATOM   250  C CA  . ASP   A 1 32  ? -0.406  -11.758 -13.700 1.00 60.93  ? 75  ASP   A CA  1 
ATOM   251  C C   . ASP   A 1 32  ? -0.547  -10.447 -12.942 1.00 50.39  ? 75  ASP   A C   1 
ATOM   252  O O   . ASP   A 1 32  ? 0.334   -9.571  -13.120 1.00 51.30  ? 75  ASP   A O   1 
ATOM   253  C CB  . ASP   A 1 32  ? 0.911   -12.456 -13.357 1.00 67.61  ? 75  ASP   A CB  1 
ATOM   254  C CG  . ASP   A 1 32  ? 0.913   -13.903 -13.810 1.00 70.57  ? 75  ASP   A CG  1 
ATOM   255  O OD1 . ASP   A 1 32  ? -0.190  -14.449 -14.041 1.00 78.43  ? 75  ASP   A OD1 1 
ATOM   256  O OD2 . ASP   A 1 32  ? 2.007   -14.470 -13.914 1.00 77.16  ? 75  ASP   A OD2 1 
ATOM   257  N N   . VAL   A 1 33  ? -1.601  -10.310 -12.133 1.00 50.11  ? 76  VAL   A N   1 
ATOM   258  C CA  . VAL   A 1 33  ? -1.887  -9.018  -11.436 1.00 53.07  ? 76  VAL   A CA  1 
ATOM   259  C C   . VAL   A 1 33  ? -2.248  -9.304  -9.973  1.00 49.96  ? 76  VAL   A C   1 
ATOM   260  O O   . VAL   A 1 33  ? -2.757  -10.423 -9.627  1.00 42.22  ? 76  VAL   A O   1 
ATOM   261  C CB  . VAL   A 1 33  ? -2.972  -8.156  -12.145 1.00 51.08  ? 76  VAL   A CB  1 
ATOM   262  C CG1 . VAL   A 1 33  ? -2.695  -7.939  -13.619 1.00 55.88  ? 76  VAL   A CG1 1 
ATOM   263  C CG2 . VAL   A 1 33  ? -4.367  -8.726  -11.985 1.00 51.85  ? 76  VAL   A CG2 1 
ATOM   264  N N   . ALA   A 1 34  ? -2.007  -8.303  -9.137  1.00 49.26  ? 77  ALA   A N   1 
ATOM   265  C CA  . ALA   A 1 34  ? -2.430  -8.261  -7.719  1.00 47.95  ? 77  ALA   A CA  1 
ATOM   266  C C   . ALA   A 1 34  ? -3.448  -7.123  -7.574  1.00 46.57  ? 77  ALA   A C   1 
ATOM   267  O O   . ALA   A 1 34  ? -3.324  -6.109  -8.279  1.00 44.94  ? 77  ALA   A O   1 
ATOM   268  C CB  . ALA   A 1 34  ? -1.223  -8.056  -6.839  1.00 47.31  ? 77  ALA   A CB  1 
ATOM   269  N N   . LEU   A 1 35  ? -4.420  -7.309  -6.702  1.00 41.56  ? 78  LEU   A N   1 
ATOM   270  C CA  . LEU   A 1 35  ? -5.425  -6.293  -6.299  1.00 48.51  ? 78  LEU   A CA  1 
ATOM   271  C C   . LEU   A 1 35  ? -5.236  -5.974  -4.798  1.00 49.82  ? 78  LEU   A C   1 
ATOM   272  O O   . LEU   A 1 35  ? -5.381  -6.903  -3.955  1.00 51.18  ? 78  LEU   A O   1 
ATOM   273  C CB  . LEU   A 1 35  ? -6.804  -6.885  -6.641  1.00 44.60  ? 78  LEU   A CB  1 
ATOM   274  C CG  . LEU   A 1 35  ? -8.016  -6.031  -6.278  1.00 43.53  ? 78  LEU   A CG  1 
ATOM   275  C CD1 . LEU   A 1 35  ? -8.008  -4.720  -7.027  1.00 44.80  ? 78  LEU   A CD1 1 
ATOM   276  C CD2 . LEU   A 1 35  ? -9.313  -6.788  -6.530  1.00 47.88  ? 78  LEU   A CD2 1 
ATOM   277  N N   . ASP   A 1 36  ? -4.896  -4.720  -4.471  1.00 45.21  ? 79  ASP   A N   1 
ATOM   278  C CA  . ASP   A 1 36  ? -4.678  -4.224  -3.083  1.00 44.80  ? 79  ASP   A CA  1 
ATOM   279  C C   . ASP   A 1 36  ? -6.015  -3.762  -2.482  1.00 49.07  ? 79  ASP   A C   1 
ATOM   280  O O   . ASP   A 1 36  ? -7.013  -3.665  -3.231  1.00 48.24  ? 79  ASP   A O   1 
ATOM   281  C CB  . ASP   A 1 36  ? -3.586  -3.146  -3.021  1.00 43.67  ? 79  ASP   A CB  1 
ATOM   282  C CG  . ASP   A 1 36  ? -3.977  -1.759  -3.494  1.00 52.15  ? 79  ASP   A CG  1 
ATOM   283  O OD1 . ASP   A 1 36  ? -5.185  -1.516  -3.737  1.00 49.01  ? 79  ASP   A OD1 1 
ATOM   284  O OD2 . ASP   A 1 36  ? -3.059  -0.912  -3.616  1.00 57.32  ? 79  ASP   A OD2 1 
ATOM   285  N N   . GLU   A 1 37  ? -6.006  -3.485  -1.167  1.00 49.19  ? 80  GLU   A N   1 
ATOM   286  C CA  . GLU   A 1 37  ? -7.187  -3.107  -0.346  1.00 49.76  ? 80  GLU   A CA  1 
ATOM   287  C C   . GLU   A 1 37  ? -7.844  -1.828  -0.919  1.00 43.99  ? 80  GLU   A C   1 
ATOM   288  O O   . GLU   A 1 37  ? -9.087  -1.711  -0.810  1.00 45.37  ? 80  GLU   A O   1 
ATOM   289  C CB  . GLU   A 1 37  ? -6.735  -2.990  1.116   1.00 50.01  ? 80  GLU   A CB  1 
ATOM   290  C CG  . GLU   A 1 37  ? -7.855  -3.200  2.132   1.00 58.84  ? 80  GLU   A CG  1 
ATOM   291  C CD  . GLU   A 1 37  ? -7.442  -3.169  3.608   1.00 62.78  ? 80  GLU   A CD  1 
ATOM   292  O OE1 . GLU   A 1 37  ? -7.111  -2.061  4.126   1.00 58.32  ? 80  GLU   A OE1 1 
ATOM   293  O OE2 . GLU   A 1 37  ? -7.452  -4.243  4.245   1.00 60.57  ? 80  GLU   A OE2 1 
ATOM   294  N N   . SER   A 1 38  ? -7.064  -0.896  -1.472  1.00 40.61  ? 81  SER   A N   1 
ATOM   295  C CA  . SER   A 1 38  ? -7.530  0.370   -2.113  1.00 46.98  ? 81  SER   A CA  1 
ATOM   296  C C   . SER   A 1 38  ? -8.145  0.158   -3.508  1.00 46.01  ? 81  SER   A C   1 
ATOM   297  O O   . SER   A 1 38  ? -8.513  1.166   -4.119  1.00 46.99  ? 81  SER   A O   1 
ATOM   298  C CB  . SER   A 1 38  ? -6.428  1.357   -2.236  1.00 48.62  ? 81  SER   A CB  1 
ATOM   299  O OG  . SER   A 1 38  ? -5.577  1.251   -1.126  1.00 64.18  ? 81  SER   A OG  1 
ATOM   300  N N   . GLY   A 1 39  ? -8.262  -1.077  -4.015  1.00 44.46  ? 82  GLY   A N   1 
ATOM   301  C CA  . GLY   A 1 39  ? -8.876  -1.361  -5.333  1.00 44.45  ? 82  GLY   A CA  1 
ATOM   302  C C   . GLY   A 1 39  ? -7.965  -1.001  -6.518  1.00 42.43  ? 82  GLY   A C   1 
ATOM   303  O O   . GLY   A 1 39  ? -8.491  -0.891  -7.611  1.00 42.69  ? 82  GLY   A O   1 
ATOM   304  N N   . ASP   A 1 40  ? -6.644  -0.925  -6.303  1.00 44.02  ? 83  ASP   A N   1 
ATOM   305  C CA  . ASP   A 1 40  ? -5.587  -0.661  -7.316  1.00 50.32  ? 83  ASP   A CA  1 
ATOM   306  C C   . ASP   A 1 40  ? -4.975  -1.993  -7.775  1.00 48.61  ? 83  ASP   A C   1 
ATOM   307  O O   . ASP   A 1 40  ? -4.393  -2.729  -6.944  1.00 49.09  ? 83  ASP   A O   1 
ATOM   308  C CB  . ASP   A 1 40  ? -4.578  0.346   -6.765  1.00 50.75  ? 83  ASP   A CB  1 
ATOM   309  C CG  . ASP   A 1 40  ? -5.222  1.713   -6.567  1.00 59.65  ? 83  ASP   A CG  1 
ATOM   310  O OD1 . ASP   A 1 40  ? -6.244  1.986   -7.232  1.00 73.81  ? 83  ASP   A OD1 1 
ATOM   311  O OD2 . ASP   A 1 40  ? -4.728  2.482   -5.736  1.00 74.29  ? 83  ASP   A OD2 1 
ATOM   312  N N   . PHE   A 1 41  ? -5.149  -2.306  -9.060  1.00 52.74  ? 84  PHE   A N   1 
ATOM   313  C CA  . PHE   A 1 41  ? -4.502  -3.452  -9.736  1.00 50.96  ? 84  PHE   A CA  1 
ATOM   314  C C   . PHE   A 1 41  ? -3.040  -3.106  -9.982  1.00 55.17  ? 84  PHE   A C   1 
ATOM   315  O O   . PHE   A 1 41  ? -2.755  -1.933  -10.303 1.00 56.64  ? 84  PHE   A O   1 
ATOM   316  C CB  . PHE   A 1 41  ? -5.208  -3.771  -11.044 1.00 44.38  ? 84  PHE   A CB  1 
ATOM   317  C CG  . PHE   A 1 41  ? -6.507  -4.514  -10.895 1.00 46.01  ? 84  PHE   A CG  1 
ATOM   318  C CD1 . PHE   A 1 41  ? -6.516  -5.855  -10.526 1.00 43.29  ? 84  PHE   A CD1 1 
ATOM   319  C CD2 . PHE   A 1 41  ? -7.720  -3.900  -11.209 1.00 48.21  ? 84  PHE   A CD2 1 
ATOM   320  C CE1 . PHE   A 1 41  ? -7.710  -6.557  -10.451 1.00 46.09  ? 84  PHE   A CE1 1 
ATOM   321  C CE2 . PHE   A 1 41  ? -8.912  -4.606  -11.125 1.00 42.90  ? 84  PHE   A CE2 1 
ATOM   322  C CZ  . PHE   A 1 41  ? -8.902  -5.930  -10.759 1.00 43.70  ? 84  PHE   A CZ  1 
ATOM   323  N N   . SER   A 1 42  ? -2.139  -4.073  -9.815  1.00 50.69  ? 85  SER   A N   1 
ATOM   324  C CA  . SER   A 1 42  ? -0.715  -3.900  -10.197 1.00 53.18  ? 85  SER   A CA  1 
ATOM   325  C C   . SER   A 1 42  ? -0.179  -5.171  -10.877 1.00 55.08  ? 85  SER   A C   1 
ATOM   326  O O   . SER   A 1 42  ? -0.677  -6.292  -10.598 1.00 51.32  ? 85  SER   A O   1 
ATOM   327  C CB  . SER   A 1 42  ? 0.108   -3.472  -9.020  1.00 55.33  ? 85  SER   A CB  1 
ATOM   328  O OG  . SER   A 1 42  ? 0.035   -4.422  -7.967  1.00 59.12  ? 85  SER   A OG  1 
ATOM   329  N N   . LEU   A 1 43  ? 0.781   -5.003  -11.785 1.00 64.53  ? 86  LEU   A N   1 
ATOM   330  C CA  . LEU   A 1 43  ? 1.479   -6.142  -12.442 1.00 69.38  ? 86  LEU   A CA  1 
ATOM   331  C C   . LEU   A 1 43  ? 2.418   -6.814  -11.436 1.00 63.66  ? 86  LEU   A C   1 
ATOM   332  O O   . LEU   A 1 43  ? 3.335   -6.146  -10.925 1.00 64.84  ? 86  LEU   A O   1 
ATOM   333  C CB  . LEU   A 1 43  ? 2.229   -5.616  -13.663 1.00 71.74  ? 86  LEU   A CB  1 
ATOM   334  C CG  . LEU   A 1 43  ? 1.301   -5.169  -14.783 1.00 75.62  ? 86  LEU   A CG  1 
ATOM   335  C CD1 . LEU   A 1 43  ? 2.007   -4.235  -15.752 1.00 79.17  ? 86  LEU   A CD1 1 
ATOM   336  C CD2 . LEU   A 1 43  ? 0.721   -6.381  -15.498 1.00 75.37  ? 86  LEU   A CD2 1 
ATOM   337  N N   . VAL   A 1 44  ? 2.127   -8.070  -11.123 1.00 66.78  ? 87  VAL   A N   1 
ATOM   338  C CA  . VAL   A 1 44  ? 3.020   -9.031  -10.414 1.00 74.56  ? 87  VAL   A CA  1 
ATOM   339  C C   . VAL   A 1 44  ? 4.052   -9.514  -11.431 1.00 83.28  ? 87  VAL   A C   1 
ATOM   340  O O   . VAL   A 1 44  ? 3.648   -10.165 -12.407 1.00 89.56  ? 87  VAL   A O   1 
ATOM   341  C CB  . VAL   A 1 44  ? 2.202   -10.215 -9.860  1.00 70.39  ? 87  VAL   A CB  1 
ATOM   342  C CG1 . VAL   A 1 44  ? 3.089   -11.360 -9.379  1.00 71.58  ? 87  VAL   A CG1 1 
ATOM   343  C CG2 . VAL   A 1 44  ? 1.237   -9.760  -8.774  1.00 70.12  ? 87  VAL   A CG2 1 
ATOM   344  N N   . GLU   A 1 45  ? 5.329   -9.214  -11.226 1.00 96.13  ? 88  GLU   A N   1 
ATOM   345  C CA  . GLU   A 1 45  ? 6.385   -9.551  -12.216 1.00 112.65 ? 88  GLU   A CA  1 
ATOM   346  C C   . GLU   A 1 45  ? 7.375   -10.541 -11.586 1.00 116.20 ? 88  GLU   A C   1 
ATOM   347  O O   . GLU   A 1 45  ? 7.100   -11.743 -11.520 1.00 101.28 ? 88  GLU   A O   1 
ATOM   348  C CB  . GLU   A 1 45  ? 7.019   -8.250  -12.703 1.00 118.85 ? 88  GLU   A CB  1 
ATOM   349  C CG  . GLU   A 1 45  ? 6.182   -7.512  -13.737 1.00 116.68 ? 88  GLU   A CG  1 
ATOM   350  C CD  . GLU   A 1 45  ? 6.453   -7.924  -15.172 1.00 104.35 ? 88  GLU   A CD  1 
ATOM   351  O OE1 . GLU   A 1 45  ? 6.762   -9.114  -15.386 1.00 99.97  ? 88  GLU   A OE1 1 
ATOM   352  O OE2 . GLU   A 1 45  ? 6.375   -7.048  -16.066 1.00 91.18  ? 88  GLU   A OE2 1 
ATOM   353  N N   . GLY   B 2 7   ? -36.653 12.289  -11.820 1.00 91.69  ? 16  GLY   B N   1 
ATOM   354  C CA  . GLY   B 2 7   ? -35.493 12.310  -12.772 1.00 93.98  ? 16  GLY   B CA  1 
ATOM   355  C C   . GLY   B 2 7   ? -35.606 11.268  -13.883 1.00 96.28  ? 16  GLY   B C   1 
ATOM   356  O O   . GLY   B 2 7   ? -36.571 10.468  -13.860 1.00 94.45  ? 16  GLY   B O   1 
ATOM   357  N N   . GLU   B 2 8   ? -34.652 11.272  -14.828 1.00 84.29  ? 17  GLU   B N   1 
ATOM   358  C CA  . GLU   B 2 8   ? -34.570 10.311  -15.968 1.00 74.29  ? 17  GLU   B CA  1 
ATOM   359  C C   . GLU   B 2 8   ? -34.208 8.920   -15.415 1.00 67.24  ? 17  GLU   B C   1 
ATOM   360  O O   . GLU   B 2 8   ? -33.117 8.738   -14.882 1.00 61.26  ? 17  GLU   B O   1 
ATOM   361  C CB  . GLU   B 2 8   ? -33.569 10.792  -17.028 1.00 75.56  ? 17  GLU   B CB  1 
ATOM   362  C CG  . GLU   B 2 8   ? -33.587 9.954   -18.300 1.00 70.16  ? 17  GLU   B CG  1 
ATOM   363  C CD  . GLU   B 2 8   ? -32.984 10.575  -19.554 1.00 74.00  ? 17  GLU   B CD  1 
ATOM   364  O OE1 . GLU   B 2 8   ? -32.088 11.476  -19.448 1.00 60.59  ? 17  GLU   B OE1 1 
ATOM   365  O OE2 . GLU   B 2 8   ? -33.444 10.186  -20.658 1.00 78.25  ? 17  GLU   B OE2 1 
ATOM   366  N N   A THR   B 2 9   ? -35.117 7.951   -15.529 0.25 67.69  ? 18  THR   B N   1 
ATOM   367  N N   B THR   B 2 9   ? -35.144 7.979   -15.573 0.25 64.48  ? 18  THR   B N   1 
ATOM   368  N N   C THR   B 2 9   ? -35.117 7.951   -15.529 0.25 67.69  ? 18  THR   B N   1 
ATOM   369  N N   D THR   B 2 9   ? -35.144 7.979   -15.573 0.25 64.48  ? 18  THR   B N   1 
ATOM   370  C CA  A THR   B 2 9   ? -34.907 6.572   -15.016 0.25 69.14  ? 18  THR   B CA  1 
ATOM   371  C CA  B THR   B 2 9   ? -35.112 6.601   -15.022 0.25 63.61  ? 18  THR   B CA  1 
ATOM   372  C CA  C THR   B 2 9   ? -34.907 6.572   -15.016 0.25 69.14  ? 18  THR   B CA  1 
ATOM   373  C CA  D THR   B 2 9   ? -35.112 6.601   -15.022 0.25 63.61  ? 18  THR   B CA  1 
ATOM   374  C C   A THR   B 2 9   ? -34.947 5.552   -16.156 0.25 64.77  ? 18  THR   B C   1 
ATOM   375  C C   B THR   B 2 9   ? -34.925 5.572   -16.145 0.25 61.64  ? 18  THR   B C   1 
ATOM   376  C C   C THR   B 2 9   ? -34.947 5.552   -16.156 0.25 64.77  ? 18  THR   B C   1 
ATOM   377  C C   D THR   B 2 9   ? -34.925 5.572   -16.145 0.25 61.64  ? 18  THR   B C   1 
ATOM   378  O O   A THR   B 2 9   ? -34.972 4.346   -15.844 0.25 66.23  ? 18  THR   B O   1 
ATOM   379  O O   B THR   B 2 9   ? -34.752 4.384   -15.808 0.25 62.86  ? 18  THR   B O   1 
ATOM   380  O O   C THR   B 2 9   ? -34.972 4.346   -15.844 0.25 66.23  ? 18  THR   B O   1 
ATOM   381  O O   D THR   B 2 9   ? -34.752 4.384   -15.808 0.25 62.86  ? 18  THR   B O   1 
ATOM   382  C CB  A THR   B 2 9   ? -35.946 6.197   -13.954 0.25 71.87  ? 18  THR   B CB  1 
ATOM   383  C CB  B THR   B 2 9   ? -36.396 6.312   -14.233 0.25 61.83  ? 18  THR   B CB  1 
ATOM   384  C CB  C THR   B 2 9   ? -35.946 6.197   -13.954 0.25 71.87  ? 18  THR   B CB  1 
ATOM   385  C CB  D THR   B 2 9   ? -36.396 6.312   -14.233 0.25 61.83  ? 18  THR   B CB  1 
ATOM   386  O OG1 A THR   B 2 9   ? -36.141 7.334   -13.111 0.25 75.90  ? 18  THR   B OG1 1 
ATOM   387  O OG1 B THR   B 2 9   ? -37.508 6.781   -14.997 0.25 59.44  ? 18  THR   B OG1 1 
ATOM   388  O OG1 C THR   B 2 9   ? -36.141 7.334   -13.111 0.25 75.90  ? 18  THR   B OG1 1 
ATOM   389  O OG1 D THR   B 2 9   ? -37.508 6.781   -14.997 0.25 59.44  ? 18  THR   B OG1 1 
ATOM   390  C CG2 A THR   B 2 9   ? -35.518 4.991   -13.147 0.25 71.35  ? 18  THR   B CG2 1 
ATOM   391  C CG2 B THR   B 2 9   ? -36.408 6.970   -12.871 0.25 64.12  ? 18  THR   B CG2 1 
ATOM   392  C CG2 C THR   B 2 9   ? -35.518 4.991   -13.147 0.25 71.35  ? 18  THR   B CG2 1 
ATOM   393  C CG2 D THR   B 2 9   ? -36.408 6.970   -12.871 0.25 64.12  ? 18  THR   B CG2 1 
ATOM   394  N N   . THR   B 2 10  ? -34.937 6.005   -17.412 1.00 60.47  ? 19  THR   B N   1 
ATOM   395  C CA  . THR   B 2 10  ? -34.946 5.097   -18.586 1.00 55.49  ? 19  THR   B CA  1 
ATOM   396  C C   . THR   B 2 10  ? -33.657 4.261   -18.562 1.00 49.79  ? 19  THR   B C   1 
ATOM   397  O O   . THR   B 2 10  ? -32.576 4.863   -18.375 1.00 47.81  ? 19  THR   B O   1 
ATOM   398  C CB  . THR   B 2 10  ? -35.113 5.856   -19.918 1.00 58.70  ? 19  THR   B CB  1 
ATOM   399  O OG1 . THR   B 2 10  ? -36.012 6.963   -19.799 1.00 67.00  ? 19  THR   B OG1 1 
ATOM   400  C CG2 . THR   B 2 10  ? -35.629 4.953   -21.021 1.00 55.70  ? 19  THR   B CG2 1 
ATOM   401  N N   . ASP   B 2 11  ? -33.765 2.941   -18.749 1.00 41.07  ? 20  ASP   B N   1 
ATOM   402  C CA  . ASP   B 2 11  ? -32.594 2.067   -18.988 1.00 44.27  ? 20  ASP   B CA  1 
ATOM   403  C C   . ASP   B 2 11  ? -31.698 2.718   -20.043 1.00 50.61  ? 20  ASP   B C   1 
ATOM   404  O O   . ASP   B 2 11  ? -32.244 3.366   -20.956 1.00 52.35  ? 20  ASP   B O   1 
ATOM   405  C CB  . ASP   B 2 11  ? -32.973 0.656   -19.431 1.00 46.09  ? 20  ASP   B CB  1 
ATOM   406  C CG  . ASP   B 2 11  ? -33.546 -0.226  -18.333 1.00 53.98  ? 20  ASP   B CG  1 
ATOM   407  O OD1 . ASP   B 2 11  ? -33.770 0.295   -17.225 1.00 47.64  ? 20  ASP   B OD1 1 
ATOM   408  O OD2 . ASP   B 2 11  ? -33.780 -1.448  -18.617 1.00 61.38  ? 20  ASP   B OD2 1 
ATOM   409  N N   . GLY   B 2 12  ? -30.378 2.557   -19.913 1.00 42.15  ? 21  GLY   B N   1 
ATOM   410  C CA  . GLY   B 2 12  ? -29.390 2.926   -20.940 1.00 39.45  ? 21  GLY   B CA  1 
ATOM   411  C C   . GLY   B 2 12  ? -28.106 3.354   -20.284 1.00 34.22  ? 21  GLY   B C   1 
ATOM   412  O O   . GLY   B 2 12  ? -27.935 3.115   -19.078 1.00 41.40  ? 21  GLY   B O   1 
ATOM   413  N N   . VAL   B 2 13  ? -27.250 3.995   -21.059 1.00 38.94  ? 22  VAL   B N   1 
ATOM   414  C CA  . VAL   B 2 13  ? -25.912 4.436   -20.600 1.00 37.38  ? 22  VAL   B CA  1 
ATOM   415  C C   . VAL   B 2 13  ? -25.968 5.948   -20.450 1.00 40.07  ? 22  VAL   B C   1 
ATOM   416  O O   . VAL   B 2 13  ? -26.690 6.604   -21.237 1.00 38.25  ? 22  VAL   B O   1 
ATOM   417  C CB  . VAL   B 2 13  ? -24.807 3.938   -21.538 1.00 39.23  ? 22  VAL   B CB  1 
ATOM   418  C CG1 . VAL   B 2 13  ? -24.998 4.407   -22.995 1.00 45.23  ? 22  VAL   B CG1 1 
ATOM   419  C CG2 . VAL   B 2 13  ? -23.428 4.321   -21.026 1.00 41.44  ? 22  VAL   B CG2 1 
ATOM   420  N N   . TYR   B 2 14  ? -25.279 6.479   -19.445 1.00 40.12  ? 23  TYR   B N   1 
ATOM   421  C CA  . TYR   B 2 14  ? -25.349 7.913   -19.070 1.00 40.48  ? 23  TYR   B CA  1 
ATOM   422  C C   . TYR   B 2 14  ? -23.959 8.435   -18.824 1.00 41.79  ? 23  TYR   B C   1 
ATOM   423  O O   . TYR   B 2 14  ? -23.130 7.687   -18.273 1.00 43.89  ? 23  TYR   B O   1 
ATOM   424  C CB  . TYR   B 2 14  ? -26.150 8.112   -17.790 1.00 39.30  ? 23  TYR   B CB  1 
ATOM   425  C CG  . TYR   B 2 14  ? -27.619 7.894   -17.930 1.00 40.04  ? 23  TYR   B CG  1 
ATOM   426  C CD1 . TYR   B 2 14  ? -28.114 6.631   -18.185 1.00 38.46  ? 23  TYR   B CD1 1 
ATOM   427  C CD2 . TYR   B 2 14  ? -28.505 8.952   -17.815 1.00 40.52  ? 23  TYR   B CD2 1 
ATOM   428  C CE1 . TYR   B 2 14  ? -29.470 6.397   -18.264 1.00 40.78  ? 23  TYR   B CE1 1 
ATOM   429  C CE2 . TYR   B 2 14  ? -29.867 8.746   -17.959 1.00 42.06  ? 23  TYR   B CE2 1 
ATOM   430  C CZ  . TYR   B 2 14  ? -30.350 7.470   -18.176 1.00 46.16  ? 23  TYR   B CZ  1 
ATOM   431  O OH  . TYR   B 2 14  ? -31.688 7.253   -18.294 1.00 46.08  ? 23  TYR   B OH  1 
ATOM   432  N N   . ARG   B 2 15  ? -23.766 9.708   -19.122 1.00 38.60  ? 24  ARG   B N   1 
ATOM   433  C CA  . ARG   B 2 15  ? -22.560 10.451  -18.696 1.00 43.25  ? 24  ARG   B CA  1 
ATOM   434  C C   . ARG   B 2 15  ? -22.756 10.961  -17.270 1.00 43.31  ? 24  ARG   B C   1 
ATOM   435  O O   . ARG   B 2 15  ? -23.858 11.379  -16.913 1.00 39.62  ? 24  ARG   B O   1 
ATOM   436  C CB  . ARG   B 2 15  ? -22.264 11.630  -19.627 1.00 41.11  ? 24  ARG   B CB  1 
ATOM   437  C CG  . ARG   B 2 15  ? -22.236 11.267  -21.104 1.00 44.47  ? 24  ARG   B CG  1 
ATOM   438  C CD  . ARG   B 2 15  ? -22.225 12.488  -22.015 1.00 52.95  ? 24  ARG   B CD  1 
ATOM   439  N NE  . ARG   B 2 15  ? -22.317 12.099  -23.430 1.00 51.92  ? 24  ARG   B NE  1 
ATOM   440  C CZ  . ARG   B 2 15  ? -21.277 11.913  -24.253 1.00 46.87  ? 24  ARG   B CZ  1 
ATOM   441  N NH1 . ARG   B 2 15  ? -20.042 12.086  -23.814 1.00 47.18  ? 24  ARG   B NH1 1 
ATOM   442  N NH2 . ARG   B 2 15  ? -21.499 11.537  -25.505 1.00 56.60  ? 24  ARG   B NH2 1 
ATOM   443  N N   . VAL   B 2 16  ? -21.683 10.923  -16.504 1.00 42.30  ? 25  VAL   B N   1 
ATOM   444  C CA  . VAL   B 2 16  ? -21.569 11.530  -15.168 1.00 40.65  ? 25  VAL   B CA  1 
ATOM   445  C C   . VAL   B 2 16  ? -20.713 12.780  -15.328 1.00 44.06  ? 25  VAL   B C   1 
ATOM   446  O O   . VAL   B 2 16  ? -19.537 12.647  -15.662 1.00 39.61  ? 25  VAL   B O   1 
ATOM   447  C CB  . VAL   B 2 16  ? -20.982 10.515  -14.170 1.00 44.28  ? 25  VAL   B CB  1 
ATOM   448  C CG1 . VAL   B 2 16  ? -20.987 11.041  -12.740 1.00 45.91  ? 25  VAL   B CG1 1 
ATOM   449  C CG2 . VAL   B 2 16  ? -21.720 9.185   -14.259 1.00 49.24  ? 25  VAL   B CG2 1 
ATOM   450  N N   . MET   B 2 17  ? -21.336 13.935  -15.101 1.00 47.97  ? 26  MET   B N   1 
ATOM   451  C CA  . MET   B 2 17  ? -20.793 15.302  -15.298 1.00 44.50  ? 26  MET   B CA  1 
ATOM   452  C C   . MET   B 2 17  ? -20.664 16.001  -13.940 1.00 50.27  ? 26  MET   B C   1 
ATOM   453  O O   . MET   B 2 17  ? -21.540 15.792  -13.069 1.00 50.56  ? 26  MET   B O   1 
ATOM   454  C CB  . MET   B 2 17  ? -21.770 16.119  -16.141 1.00 47.15  ? 26  MET   B CB  1 
ATOM   455  C CG  . MET   B 2 17  ? -22.198 15.438  -17.425 1.00 50.02  ? 26  MET   B CG  1 
ATOM   456  S SD  . MET   B 2 17  ? -20.833 15.205  -18.609 1.00 49.28  ? 26  MET   B SD  1 
ATOM   457  C CE  . MET   B 2 17  ? -20.131 16.853  -18.730 1.00 51.38  ? 26  MET   B CE  1 
ATOM   458  N N   . THR   B 2 18  ? -19.650 16.848  -13.793 1.00 49.11  ? 27  THR   B N   1 
ATOM   459  C CA  . THR   B 2 18  ? -19.516 17.810  -12.679 1.00 55.65  ? 27  THR   B CA  1 
ATOM   460  C C   . THR   B 2 18  ? -19.390 19.224  -13.275 1.00 53.26  ? 27  THR   B C   1 
ATOM   461  O O   . THR   B 2 18  ? -18.854 19.345  -14.424 1.00 42.89  ? 27  THR   B O   1 
ATOM   462  C CB  . THR   B 2 18  ? -18.339 17.422  -11.771 1.00 58.93  ? 27  THR   B CB  1 
ATOM   463  O OG1 . THR   B 2 18  ? -18.321 18.358  -10.685 1.00 59.31  ? 27  THR   B OG1 1 
ATOM   464  C CG2 . THR   B 2 18  ? -16.997 17.406  -12.483 1.00 57.04  ? 27  THR   B CG2 1 
ATOM   465  N N   . ARG   B 2 19  ? -19.875 20.238  -12.543 1.00 61.49  ? 28  ARG   B N   1 
ATOM   466  C CA  . ARG   B 2 19  ? -19.660 21.689  -12.832 1.00 68.86  ? 28  ARG   B CA  1 
ATOM   467  C C   . ARG   B 2 19  ? -18.715 22.327  -11.796 1.00 62.58  ? 28  ARG   B C   1 
ATOM   468  O O   . ARG   B 2 19  ? -18.592 23.561  -11.786 1.00 64.50  ? 28  ARG   B O   1 
ATOM   469  C CB  . ARG   B 2 19  ? -21.002 22.420  -12.901 1.00 73.17  ? 28  ARG   B CB  1 
ATOM   470  C CG  . ARG   B 2 19  ? -21.854 21.983  -14.083 1.00 82.22  ? 28  ARG   B CG  1 
ATOM   471  C CD  . ARG   B 2 19  ? -22.535 23.112  -14.826 1.00 80.99  ? 28  ARG   B CD  1 
ATOM   472  N NE  . ARG   B 2 19  ? -23.621 22.626  -15.668 1.00 89.41  ? 28  ARG   B NE  1 
ATOM   473  C CZ  . ARG   B 2 19  ? -24.801 22.188  -15.224 1.00 102.04 ? 28  ARG   B CZ  1 
ATOM   474  N NH1 . ARG   B 2 19  ? -25.062 22.162  -13.926 1.00 110.06 ? 28  ARG   B NH1 1 
ATOM   475  N NH2 . ARG   B 2 19  ? -25.719 21.767  -16.081 1.00 100.49 ? 28  ARG   B NH2 1 
ATOM   476  N N   . ARG   B 2 20  ? -17.996 21.522  -11.017 1.00 65.90  ? 29  ARG   B N   1 
ATOM   477  C CA  . ARG   B 2 20  ? -17.169 22.013  -9.876  1.00 81.18  ? 29  ARG   B CA  1 
ATOM   478  C C   . ARG   B 2 20  ? -15.778 22.385  -10.389 1.00 78.22  ? 29  ARG   B C   1 
ATOM   479  O O   . ARG   B 2 20  ? -15.007 22.979  -9.627  1.00 87.28  ? 29  ARG   B O   1 
ATOM   480  C CB  . ARG   B 2 20  ? -17.081 20.952  -8.773  1.00 87.09  ? 29  ARG   B CB  1 
ATOM   481  C CG  . ARG   B 2 20  ? -16.901 21.512  -7.369  1.00 95.71  ? 29  ARG   B CG  1 
ATOM   482  C CD  . ARG   B 2 20  ? -16.743 20.388  -6.365  1.00 114.36 ? 29  ARG   B CD  1 
ATOM   483  N NE  . ARG   B 2 20  ? -15.898 19.319  -6.900  1.00 133.69 ? 29  ARG   B NE  1 
ATOM   484  C CZ  . ARG   B 2 20  ? -14.560 19.303  -6.895  1.00 139.94 ? 29  ARG   B CZ  1 
ATOM   485  N NH1 . ARG   B 2 20  ? -13.868 20.299  -6.364  1.00 145.23 ? 29  ARG   B NH1 1 
ATOM   486  N NH2 . ARG   B 2 20  ? -13.912 18.276  -7.423  1.00 131.09 ? 29  ARG   B NH2 1 
ATOM   487  N N   . LEU   B 2 21  ? -15.465 22.015  -11.629 1.00 76.44  ? 30  LEU   B N   1 
ATOM   488  C CA  . LEU   B 2 21  ? -14.210 22.404  -12.320 1.00 75.64  ? 30  LEU   B CA  1 
ATOM   489  C C   . LEU   B 2 21  ? -14.549 23.421  -13.422 1.00 76.37  ? 30  LEU   B C   1 
ATOM   490  O O   . LEU   B 2 21  ? -15.711 23.954  -13.416 1.00 65.53  ? 30  LEU   B O   1 
ATOM   491  C CB  . LEU   B 2 21  ? -13.556 21.131  -12.863 1.00 77.90  ? 30  LEU   B CB  1 
ATOM   492  C CG  . LEU   B 2 21  ? -12.496 20.497  -11.966 1.00 83.79  ? 30  LEU   B CG  1 
ATOM   493  C CD1 . LEU   B 2 21  ? -12.909 20.523  -10.501 1.00 85.62  ? 30  LEU   B CD1 1 
ATOM   494  C CD2 . LEU   B 2 21  ? -12.196 19.072  -12.414 1.00 77.47  ? 30  LEU   B CD2 1 
ATOM   495  N N   . LEU   B 2 22  ? -13.574 23.711  -14.299 1.00 73.84  ? 31  LEU   B N   1 
ATOM   496  C CA  . LEU   B 2 22  ? -13.758 24.553  -15.511 1.00 66.14  ? 31  LEU   B CA  1 
ATOM   497  C C   . LEU   B 2 22  ? -14.843 23.942  -16.395 1.00 66.49  ? 31  LEU   B C   1 
ATOM   498  O O   . LEU   B 2 22  ? -14.753 22.732  -16.627 1.00 68.79  ? 31  LEU   B O   1 
ATOM   499  C CB  . LEU   B 2 22  ? -12.449 24.606  -16.289 1.00 66.72  ? 31  LEU   B CB  1 
ATOM   500  C CG  . LEU   B 2 22  ? -12.446 25.622  -17.428 1.00 69.19  ? 31  LEU   B CG  1 
ATOM   501  C CD1 . LEU   B 2 22  ? -12.399 27.043  -16.870 1.00 61.27  ? 31  LEU   B CD1 1 
ATOM   502  C CD2 . LEU   B 2 22  ? -11.279 25.361  -18.383 1.00 69.91  ? 31  LEU   B CD2 1 
ATOM   503  N N   . GLY   B 2 23  ? -15.822 24.731  -16.863 1.00 58.22  ? 32  GLY   B N   1 
ATOM   504  C CA  . GLY   B 2 23  ? -16.907 24.232  -17.731 1.00 51.67  ? 32  GLY   B CA  1 
ATOM   505  C C   . GLY   B 2 23  ? -17.682 23.080  -17.093 1.00 48.80  ? 32  GLY   B C   1 
ATOM   506  O O   . GLY   B 2 23  ? -17.695 22.960  -15.867 1.00 62.91  ? 32  GLY   B O   1 
ATOM   507  N N   . SER   B 2 24  ? -18.334 22.278  -17.930 1.00 55.45  ? 33  SER   B N   1 
ATOM   508  C CA  . SER   B 2 24  ? -18.990 20.995  -17.574 1.00 55.80  ? 33  SER   B CA  1 
ATOM   509  C C   . SER   B 2 24  ? -18.060 19.849  -17.986 1.00 53.52  ? 33  SER   B C   1 
ATOM   510  O O   . SER   B 2 24  ? -17.863 19.674  -19.187 1.00 54.04  ? 33  SER   B O   1 
ATOM   511  C CB  . SER   B 2 24  ? -20.328 20.888  -18.235 1.00 58.23  ? 33  SER   B CB  1 
ATOM   512  O OG  . SER   B 2 24  ? -21.182 21.929  -17.779 1.00 59.28  ? 33  SER   B OG  1 
ATOM   513  N N   . THR   B 2 25  ? -17.488 19.142  -17.009 1.00 55.36  ? 34  THR   B N   1 
ATOM   514  C CA  . THR   B 2 25  ? -16.445 18.102  -17.173 1.00 50.33  ? 34  THR   B CA  1 
ATOM   515  C C   . THR   B 2 25  ? -17.056 16.717  -16.950 1.00 50.40  ? 34  THR   B C   1 
ATOM   516  O O   . THR   B 2 25  ? -17.739 16.538  -15.938 1.00 53.01  ? 34  THR   B O   1 
ATOM   517  C CB  . THR   B 2 25  ? -15.282 18.338  -16.210 1.00 52.78  ? 34  THR   B CB  1 
ATOM   518  O OG1 . THR   B 2 25  ? -14.742 19.632  -16.502 1.00 54.19  ? 34  THR   B OG1 1 
ATOM   519  C CG2 . THR   B 2 25  ? -14.205 17.277  -16.343 1.00 51.55  ? 34  THR   B CG2 1 
ATOM   520  N N   . GLN   B 2 26  ? -16.824 15.779  -17.866 1.00 49.41  ? 35  GLN   B N   1 
ATOM   521  C CA  . GLN   B 2 26  ? -17.313 14.386  -17.709 1.00 51.45  ? 35  GLN   B CA  1 
ATOM   522  C C   . GLN   B 2 26  ? -16.302 13.646  -16.833 1.00 57.02  ? 35  GLN   B C   1 
ATOM   523  O O   . GLN   B 2 26  ? -15.116 13.633  -17.208 1.00 57.68  ? 35  GLN   B O   1 
ATOM   524  C CB  . GLN   B 2 26  ? -17.470 13.712  -19.059 1.00 46.40  ? 35  GLN   B CB  1 
ATOM   525  C CG  . GLN   B 2 26  ? -18.200 12.384  -18.982 1.00 49.33  ? 35  GLN   B CG  1 
ATOM   526  C CD  . GLN   B 2 26  ? -18.322 11.759  -20.345 1.00 46.27  ? 35  GLN   B CD  1 
ATOM   527  O OE1 . GLN   B 2 26  ? -18.971 12.310  -21.231 1.00 44.92  ? 35  GLN   B OE1 1 
ATOM   528  N NE2 . GLN   B 2 26  ? -17.705 10.601  -20.536 1.00 40.16  ? 35  GLN   B NE2 1 
ATOM   529  N N   . VAL   B 2 27  ? -16.722 13.130  -15.675 1.00 50.16  ? 36  VAL   B N   1 
ATOM   530  C CA  . VAL   B 2 27  ? -15.800 12.406  -14.751 1.00 50.02  ? 36  VAL   B CA  1 
ATOM   531  C C   . VAL   B 2 27  ? -15.943 10.904  -14.999 1.00 44.21  ? 36  VAL   B C   1 
ATOM   532  O O   . VAL   B 2 27  ? -15.078 10.161  -14.612 1.00 45.95  ? 36  VAL   B O   1 
ATOM   533  C CB  . VAL   B 2 27  ? -16.037 12.798  -13.274 1.00 51.71  ? 36  VAL   B CB  1 
ATOM   534  C CG1 . VAL   B 2 27  ? -15.640 14.235  -13.025 1.00 56.32  ? 36  VAL   B CG1 1 
ATOM   535  C CG2 . VAL   B 2 27  ? -17.467 12.583  -12.821 1.00 50.77  ? 36  VAL   B CG2 1 
ATOM   536  N N   . GLY   B 2 28  ? -17.024 10.468  -15.625 1.00 46.06  ? 37  GLY   B N   1 
ATOM   537  C CA  . GLY   B 2 28  ? -17.201 9.038   -15.918 1.00 38.54  ? 37  GLY   B CA  1 
ATOM   538  C C   . GLY   B 2 28  ? -18.542 8.803   -16.555 1.00 37.51  ? 37  GLY   B C   1 
ATOM   539  O O   . GLY   B 2 28  ? -19.119 9.770   -17.067 1.00 42.10  ? 37  GLY   B O   1 
ATOM   540  N N   . VAL   B 2 29  ? -19.020 7.562   -16.441 1.00 33.59  ? 38  VAL   B N   1 
ATOM   541  C CA  . VAL   B 2 29  ? -20.092 6.926   -17.248 1.00 34.16  ? 38  VAL   B CA  1 
ATOM   542  C C   . VAL   B 2 29  ? -20.800 5.925   -16.339 1.00 35.16  ? 38  VAL   B C   1 
ATOM   543  O O   . VAL   B 2 29  ? -20.175 5.464   -15.398 1.00 37.32  ? 38  VAL   B O   1 
ATOM   544  C CB  . VAL   B 2 29  ? -19.555 6.185   -18.500 1.00 40.04  ? 38  VAL   B CB  1 
ATOM   545  C CG1 . VAL   B 2 29  ? -20.679 5.540   -19.295 1.00 40.55  ? 38  VAL   B CG1 1 
ATOM   546  C CG2 . VAL   B 2 29  ? -18.707 7.058   -19.398 1.00 37.79  ? 38  VAL   B CG2 1 
ATOM   547  N N   . GLY   B 2 30  ? -22.050 5.595   -16.620 1.00 34.25  ? 39  GLY   B N   1 
ATOM   548  C CA  . GLY   B 2 30  ? -22.724 4.543   -15.857 1.00 32.02  ? 39  GLY   B CA  1 
ATOM   549  C C   . GLY   B 2 30  ? -23.907 3.976   -16.566 1.00 28.75  ? 39  GLY   B C   1 
ATOM   550  O O   . GLY   B 2 30  ? -24.201 4.413   -17.727 1.00 35.20  ? 39  GLY   B O   1 
ATOM   551  N N   . VAL   B 2 31  ? -24.557 3.010   -15.928 1.00 32.10  ? 40  VAL   B N   1 
ATOM   552  C CA  . VAL   B 2 31  ? -25.658 2.193   -16.530 1.00 32.43  ? 40  VAL   B CA  1 
ATOM   553  C C   . VAL   B 2 31  ? -26.904 2.307   -15.648 1.00 35.58  ? 40  VAL   B C   1 
ATOM   554  O O   . VAL   B 2 31  ? -26.825 1.978   -14.460 1.00 35.30  ? 40  VAL   B O   1 
ATOM   555  C CB  . VAL   B 2 31  ? -25.327 0.689   -16.612 1.00 36.68  ? 40  VAL   B CB  1 
ATOM   556  C CG1 . VAL   B 2 31  ? -26.525 -0.098  -17.123 1.00 39.23  ? 40  VAL   B CG1 1 
ATOM   557  C CG2 . VAL   B 2 31  ? -24.097 0.439   -17.457 1.00 41.60  ? 40  VAL   B CG2 1 
ATOM   558  N N   . MET   B 2 32  ? -28.048 2.589   -16.262 1.00 35.66  ? 41  MET   B N   1 
ATOM   559  C CA  . MET   B 2 32  ? -29.341 2.620   -15.576 1.00 37.00  ? 41  MET   B CA  1 
ATOM   560  C C   . MET   B 2 32  ? -30.020 1.308   -15.990 1.00 34.36  ? 41  MET   B C   1 
ATOM   561  O O   . MET   B 2 32  ? -30.073 1.050   -17.186 1.00 37.55  ? 41  MET   B O   1 
ATOM   562  C CB  . MET   B 2 32  ? -30.124 3.864   -16.012 1.00 37.91  ? 41  MET   B CB  1 
ATOM   563  C CG  . MET   B 2 32  ? -31.407 4.083   -15.219 1.00 43.00  ? 41  MET   B CG  1 
ATOM   564  S SD  . MET   B 2 32  ? -31.118 4.616   -13.506 1.00 45.03  ? 41  MET   B SD  1 
ATOM   565  C CE  . MET   B 2 32  ? -30.345 6.215   -13.763 1.00 45.22  ? 41  MET   B CE  1 
ATOM   566  N N   . GLN   B 2 33  ? -30.352 0.442   -15.024 1.00 41.26  ? 42  GLN   B N   1 
ATOM   567  C CA  . GLN   B 2 33  ? -31.099 -0.802  -15.278 1.00 41.46  ? 42  GLN   B CA  1 
ATOM   568  C C   . GLN   B 2 33  ? -32.025 -1.033  -14.103 1.00 42.75  ? 42  GLN   B C   1 
ATOM   569  O O   . GLN   B 2 33  ? -31.554 -0.906  -12.964 1.00 44.59  ? 42  GLN   B O   1 
ATOM   570  C CB  . GLN   B 2 33  ? -30.185 -2.024  -15.446 1.00 43.81  ? 42  GLN   B CB  1 
ATOM   571  C CG  . GLN   B 2 33  ? -30.955 -3.206  -16.033 1.00 49.48  ? 42  GLN   B CG  1 
ATOM   572  C CD  . GLN   B 2 33  ? -30.074 -4.337  -16.506 1.00 52.93  ? 42  GLN   B CD  1 
ATOM   573  O OE1 . GLN   B 2 33  ? -30.248 -5.479  -16.081 1.00 55.05  ? 42  GLN   B OE1 1 
ATOM   574  N NE2 . GLN   B 2 33  ? -29.086 -4.021  -17.334 1.00 49.31  ? 42  GLN   B NE2 1 
ATOM   575  N N   . GLU   B 2 34  ? -33.266 -1.401  -14.377 1.00 45.70  ? 43  GLU   B N   1 
ATOM   576  C CA  . GLU   B 2 34  ? -34.302 -1.671  -13.347 1.00 41.73  ? 43  GLU   B CA  1 
ATOM   577  C C   . GLU   B 2 34  ? -34.327 -0.550  -12.308 1.00 49.42  ? 43  GLU   B C   1 
ATOM   578  O O   . GLU   B 2 34  ? -34.448 -0.867  -11.136 1.00 47.04  ? 43  GLU   B O   1 
ATOM   579  C CB  . GLU   B 2 34  ? -34.000 -3.036  -12.735 1.00 52.94  ? 43  GLU   B CB  1 
ATOM   580  C CG  . GLU   B 2 34  ? -34.200 -4.205  -13.711 1.00 52.66  ? 43  GLU   B CG  1 
ATOM   581  C CD  . GLU   B 2 34  ? -33.343 -5.434  -13.421 1.00 59.81  ? 43  GLU   B CD  1 
ATOM   582  O OE1 . GLU   B 2 34  ? -33.566 -6.076  -12.391 1.00 60.49  ? 43  GLU   B OE1 1 
ATOM   583  O OE2 . GLU   B 2 34  ? -32.432 -5.738  -14.218 1.00 71.40  ? 43  GLU   B OE2 1 
ATOM   584  N N   . GLY   B 2 35  ? -34.168 0.712   -12.700 1.00 48.52  ? 44  GLY   B N   1 
ATOM   585  C CA  . GLY   B 2 35  ? -34.291 1.848   -11.759 1.00 45.28  ? 44  GLY   B CA  1 
ATOM   586  C C   . GLY   B 2 35  ? -33.071 2.033   -10.869 1.00 48.61  ? 44  GLY   B C   1 
ATOM   587  O O   . GLY   B 2 35  ? -33.137 2.850   -9.920  1.00 43.40  ? 44  GLY   B O   1 
ATOM   588  N N   . VAL   B 2 36  ? -31.967 1.337   -11.157 1.00 39.92  ? 45  VAL   B N   1 
ATOM   589  C CA  . VAL   B 2 36  ? -30.709 1.461   -10.371 1.00 34.32  ? 45  VAL   B CA  1 
ATOM   590  C C   . VAL   B 2 36  ? -29.628 1.992   -11.307 1.00 34.67  ? 45  VAL   B C   1 
ATOM   591  O O   . VAL   B 2 36  ? -29.538 1.519   -12.447 1.00 39.47  ? 45  VAL   B O   1 
ATOM   592  C CB  . VAL   B 2 36  ? -30.335 0.116   -9.698  1.00 41.56  ? 45  VAL   B CB  1 
ATOM   593  C CG1 . VAL   B 2 36  ? -28.934 0.118   -9.056  1.00 41.83  ? 45  VAL   B CG1 1 
ATOM   594  C CG2 . VAL   B 2 36  ? -31.384 -0.263  -8.659  1.00 39.11  ? 45  VAL   B CG2 1 
ATOM   595  N N   . PHE   B 2 37  ? -28.844 2.955   -10.830 1.00 32.87  ? 46  PHE   B N   1 
ATOM   596  C CA  . PHE   B 2 37  ? -27.705 3.524   -11.553 1.00 34.07  ? 46  PHE   B CA  1 
ATOM   597  C C   . PHE   B 2 37  ? -26.426 2.888   -11.029 1.00 30.22  ? 46  PHE   B C   1 
ATOM   598  O O   . PHE   B 2 37  ? -26.241 2.856   -9.800  1.00 29.50  ? 46  PHE   B O   1 
ATOM   599  C CB  . PHE   B 2 37  ? -27.696 5.041   -11.416 1.00 35.94  ? 46  PHE   B CB  1 
ATOM   600  C CG  . PHE   B 2 37  ? -26.722 5.660   -12.370 1.00 34.97  ? 46  PHE   B CG  1 
ATOM   601  C CD1 . PHE   B 2 37  ? -26.845 5.460   -13.727 1.00 34.47  ? 46  PHE   B CD1 1 
ATOM   602  C CD2 . PHE   B 2 37  ? -25.642 6.367   -11.878 1.00 38.69  ? 46  PHE   B CD2 1 
ATOM   603  C CE1 . PHE   B 2 37  ? -25.911 5.998   -14.586 1.00 41.37  ? 46  PHE   B CE1 1 
ATOM   604  C CE2 . PHE   B 2 37  ? -24.702 6.902   -12.731 1.00 38.90  ? 46  PHE   B CE2 1 
ATOM   605  C CZ  . PHE   B 2 37  ? -24.847 6.729   -14.090 1.00 35.90  ? 46  PHE   B CZ  1 
ATOM   606  N N   . HIS   B 2 38  ? -25.620 2.396   -11.928 1.00 35.48  ? 47  HIS   B N   1 
ATOM   607  C CA  . HIS   B 2 38  ? -24.421 1.543   -11.678 1.00 32.03  ? 47  HIS   B CA  1 
ATOM   608  C C   . HIS   B 2 38  ? -23.193 2.270   -12.221 1.00 29.98  ? 47  HIS   B C   1 
ATOM   609  O O   . HIS   B 2 38  ? -23.190 2.560   -13.426 1.00 32.21  ? 47  HIS   B O   1 
ATOM   610  C CB  . HIS   B 2 38  ? -24.589 0.263   -12.463 1.00 30.21  ? 47  HIS   B CB  1 
ATOM   611  C CG  . HIS   B 2 38  ? -25.745 -0.574  -12.031 1.00 31.18  ? 47  HIS   B CG  1 
ATOM   612  N ND1 . HIS   B 2 38  ? -27.013 -0.378  -12.538 1.00 32.38  ? 47  HIS   B ND1 1 
ATOM   613  C CD2 . HIS   B 2 38  ? -25.821 -1.645  -11.221 1.00 36.26  ? 47  HIS   B CD2 1 
ATOM   614  C CE1 . HIS   B 2 38  ? -27.836 -1.289  -12.036 1.00 34.70  ? 47  HIS   B CE1 1 
ATOM   615  N NE2 . HIS   B 2 38  ? -27.133 -2.048  -11.184 1.00 39.65  ? 47  HIS   B NE2 1 
ATOM   616  N N   . THR   B 2 39  ? -22.191 2.561   -11.406 1.00 34.97  ? 48  THR   B N   1 
ATOM   617  C CA  . THR   B 2 39  ? -20.958 3.194   -11.942 1.00 37.11  ? 48  THR   B CA  1 
ATOM   618  C C   . THR   B 2 39  ? -19.759 2.662   -11.154 1.00 34.17  ? 48  THR   B C   1 
ATOM   619  O O   . THR   B 2 39  ? -19.920 1.765   -10.284 1.00 33.60  ? 48  THR   B O   1 
ATOM   620  C CB  . THR   B 2 39  ? -21.099 4.726   -11.988 1.00 36.05  ? 48  THR   B CB  1 
ATOM   621  O OG1 . THR   B 2 39  ? -19.960 5.247   -12.683 1.00 39.20  ? 48  THR   B OG1 1 
ATOM   622  C CG2 . THR   B 2 39  ? -21.186 5.392   -10.635 1.00 43.61  ? 48  THR   B CG2 1 
ATOM   623  N N   . MET   B 2 40  ? -18.576 3.224   -11.397 1.00 40.71  ? 49  MET   B N   1 
ATOM   624  C CA  . MET   B 2 40  ? -17.369 2.861   -10.623 1.00 38.87  ? 49  MET   B CA  1 
ATOM   625  C C   . MET   B 2 40  ? -17.186 3.845   -9.472  1.00 42.80  ? 49  MET   B C   1 
ATOM   626  O O   . MET   B 2 40  ? -17.493 5.061   -9.622  1.00 36.53  ? 49  MET   B O   1 
ATOM   627  C CB  . MET   B 2 40  ? -16.137 2.823   -11.526 1.00 36.73  ? 49  MET   B CB  1 
ATOM   628  C CG  . MET   B 2 40  ? -16.381 1.975   -12.774 1.00 42.33  ? 49  MET   B CG  1 
ATOM   629  S SD  . MET   B 2 40  ? -14.888 1.168   -13.340 1.00 48.49  ? 49  MET   B SD  1 
ATOM   630  C CE  . MET   B 2 40  ? -14.917 -0.301  -12.311 1.00 46.02  ? 49  MET   B CE  1 
ATOM   631  N N   A TRP   B 2 41  ? -16.693 3.342   -8.336  0.08 41.83  ? 50  TRP   B N   1 
ATOM   632  N N   B TRP   B 2 41  ? -16.701 3.350   -8.332  0.13 40.66  ? 50  TRP   B N   1 
ATOM   633  N N   C TRP   B 2 41  ? -16.694 3.337   -8.341  0.39 41.45  ? 50  TRP   B N   1 
ATOM   634  N N   D TRP   B 2 41  ? -16.700 3.347   -8.335  0.39 40.32  ? 50  TRP   B N   1 
ATOM   635  C CA  A TRP   B 2 41  ? -16.543 4.118   -7.077  0.08 43.07  ? 50  TRP   B CA  1 
ATOM   636  C CA  B TRP   B 2 41  ? -16.577 4.145   -7.081  0.13 41.28  ? 50  TRP   B CA  1 
ATOM   637  C CA  C TRP   B 2 41  ? -16.538 4.108   -7.080  0.39 43.11  ? 50  TRP   B CA  1 
ATOM   638  C CA  D TRP   B 2 41  ? -16.574 4.138   -7.084  0.39 41.33  ? 50  TRP   B CA  1 
ATOM   639  C C   A TRP   B 2 41  ? -15.670 5.352   -7.325  0.08 42.92  ? 50  TRP   B C   1 
ATOM   640  C C   B TRP   B 2 41  ? -15.664 5.356   -7.314  0.13 41.79  ? 50  TRP   B C   1 
ATOM   641  C C   C TRP   B 2 41  ? -15.670 5.347   -7.328  0.39 43.27  ? 50  TRP   B C   1 
ATOM   642  C C   D TRP   B 2 41  ? -15.664 5.353   -7.316  0.39 42.01  ? 50  TRP   B C   1 
ATOM   643  O O   A TRP   B 2 41  ? -16.025 6.430   -6.807  0.08 41.17  ? 50  TRP   B O   1 
ATOM   644  O O   B TRP   B 2 41  ? -15.986 6.435   -6.773  0.13 39.24  ? 50  TRP   B O   1 
ATOM   645  O O   C TRP   B 2 41  ? -16.016 6.421   -6.796  0.39 39.51  ? 50  TRP   B O   1 
ATOM   646  O O   D TRP   B 2 41  ? -15.975 6.427   -6.759  0.39 37.53  ? 50  TRP   B O   1 
ATOM   647  C CB  A TRP   B 2 41  ? -15.975 3.267   -5.932  0.08 44.10  ? 50  TRP   B CB  1 
ATOM   648  C CB  B TRP   B 2 41  ? -16.092 3.296   -5.896  0.13 41.10  ? 50  TRP   B CB  1 
ATOM   649  C CB  C TRP   B 2 41  ? -15.963 3.253   -5.938  0.39 44.22  ? 50  TRP   B CB  1 
ATOM   650  C CB  D TRP   B 2 41  ? -16.088 3.286   -5.899  0.39 41.36  ? 50  TRP   B CB  1 
ATOM   651  C CG  A TRP   B 2 41  ? -16.087 3.965   -4.612  0.08 45.04  ? 50  TRP   B CG  1 
ATOM   652  C CG  B TRP   B 2 41  ? -15.992 4.100   -4.637  0.13 40.69  ? 50  TRP   B CG  1 
ATOM   653  C CG  C TRP   B 2 41  ? -16.079 3.948   -4.617  0.39 45.04  ? 50  TRP   B CG  1 
ATOM   654  C CG  D TRP   B 2 41  ? -15.995 4.086   -4.636  0.39 40.90  ? 50  TRP   B CG  1 
ATOM   655  C CD1 A TRP   B 2 41  ? -17.136 3.902   -3.741  0.08 44.87  ? 50  TRP   B CD1 1 
ATOM   656  C CD1 B TRP   B 2 41  ? -14.933 4.865   -4.246  0.13 39.96  ? 50  TRP   B CD1 1 
ATOM   657  C CD1 C TRP   B 2 41  ? -17.135 3.891   -3.755  0.39 43.61  ? 50  TRP   B CD1 1 
ATOM   658  C CD1 D TRP   B 2 41  ? -14.936 4.851   -4.245  0.39 39.56  ? 50  TRP   B CD1 1 
ATOM   659  C CD2 A TRP   B 2 41  ? -15.148 4.894   -4.040  0.08 45.67  ? 50  TRP   B CD2 1 
ATOM   660  C CD2 B TRP   B 2 41  ? -17.010 4.287   -3.635  0.13 39.87  ? 50  TRP   B CD2 1 
ATOM   661  C CD2 C TRP   B 2 41  ? -15.140 4.880   -4.044  0.39 45.16  ? 50  TRP   B CD2 1 
ATOM   662  C CD2 D TRP   B 2 41  ? -17.014 4.276   -3.634  0.39 39.33  ? 50  TRP   B CD2 1 
ATOM   663  N NE1 A TRP   B 2 41  ? -16.905 4.710   -2.661  0.08 46.65  ? 50  TRP   B NE1 1 
ATOM   664  N NE1 B TRP   B 2 41  ? -15.213 5.501   -3.068  0.13 39.92  ? 50  TRP   B NE1 1 
ATOM   665  N NE1 C TRP   B 2 41  ? -16.910 4.709   -2.681  0.39 47.85  ? 50  TRP   B NE1 1 
ATOM   666  N NE1 D TRP   B 2 41  ? -15.222 5.493   -3.075  0.39 39.56  ? 50  TRP   B NE1 1 
ATOM   667  C CE2 A TRP   B 2 41  ? -15.694 5.330   -2.814  0.08 46.37  ? 50  TRP   B CE2 1 
ATOM   668  C CE2 B TRP   B 2 41  ? -16.479 5.169   -2.669  0.13 39.71  ? 50  TRP   B CE2 1 
ATOM   669  C CE2 C TRP   B 2 41  ? -15.697 5.329   -2.828  0.39 46.41  ? 50  TRP   B CE2 1 
ATOM   670  C CE2 D TRP   B 2 41  ? -16.489 5.169   -2.675  0.39 39.10  ? 50  TRP   B CE2 1 
ATOM   671  C CE3 A TRP   B 2 41  ? -13.899 5.389   -4.434  0.08 46.42  ? 50  TRP   B CE3 1 
ATOM   672  C CE3 B TRP   B 2 41  ? -18.312 3.806   -3.453  0.13 40.07  ? 50  TRP   B CE3 1 
ATOM   673  C CE3 C TRP   B 2 41  ? -13.887 5.374   -4.432  0.39 46.78  ? 50  TRP   B CE3 1 
ATOM   674  C CE3 D TRP   B 2 41  ? -18.318 3.806   -3.452  0.39 39.82  ? 50  TRP   B CE3 1 
ATOM   675  C CZ2 A TRP   B 2 41  ? -15.029 6.231   -1.981  0.08 47.93  ? 50  TRP   B CZ2 1 
ATOM   676  C CZ2 B TRP   B 2 41  ? -17.193 5.552   -1.533  0.13 40.49  ? 50  TRP   B CZ2 1 
ATOM   677  C CZ2 C TRP   B 2 41  ? -15.034 6.234   -1.994  0.39 50.00  ? 50  TRP   B CZ2 1 
ATOM   678  C CZ2 D TRP   B 2 41  ? -17.199 5.554   -1.535  0.39 40.79  ? 50  TRP   B CZ2 1 
ATOM   679  C CZ3 A TRP   B 2 41  ? -13.243 6.280   -3.612  0.08 46.99  ? 50  TRP   B CZ3 1 
ATOM   680  C CZ3 B TRP   B 2 41  ? -19.021 4.191   -2.332  0.13 40.80  ? 50  TRP   B CZ3 1 
ATOM   681  C CZ3 C TRP   B 2 41  ? -13.232 6.270   -3.610  0.39 47.61  ? 50  TRP   B CZ3 1 
ATOM   682  C CZ3 D TRP   B 2 41  ? -19.026 4.196   -2.329  0.39 41.41  ? 50  TRP   B CZ3 1 
ATOM   683  C CH2 A TRP   B 2 41  ? -13.802 6.692   -2.401  0.08 48.00  ? 50  TRP   B CH2 1 
ATOM   684  C CH2 B TRP   B 2 41  ? -18.469 5.055   -1.386  0.13 39.76  ? 50  TRP   B CH2 1 
ATOM   685  C CH2 C TRP   B 2 41  ? -13.798 6.690   -2.402  0.39 49.92  ? 50  TRP   B CH2 1 
ATOM   686  C CH2 D TRP   B 2 41  ? -18.478 5.065   -1.386  0.39 39.16  ? 50  TRP   B CH2 1 
ATOM   687  N N   . HIS   B 2 42  ? -14.570 5.199   -8.070  1.00 42.71  ? 51  HIS   B N   1 
ATOM   688  C CA  . HIS   B 2 42  ? -13.592 6.317   -8.272  1.00 43.75  ? 51  HIS   B CA  1 
ATOM   689  C C   . HIS   B 2 42  ? -14.241 7.457   -9.088  1.00 42.40  ? 51  HIS   B C   1 
ATOM   690  O O   . HIS   B 2 42  ? -13.707 8.531   -9.049  1.00 40.05  ? 51  HIS   B O   1 
ATOM   691  C CB  . HIS   B 2 42  ? -12.245 5.846   -8.833  1.00 40.44  ? 51  HIS   B CB  1 
ATOM   692  C CG  . HIS   B 2 42  ? -12.265 5.554   -10.291 1.00 39.16  ? 51  HIS   B CG  1 
ATOM   693  N ND1 . HIS   B 2 42  ? -12.450 4.273   -10.798 1.00 41.23  ? 51  HIS   B ND1 1 
ATOM   694  C CD2 . HIS   B 2 42  ? -12.208 6.380   -11.358 1.00 40.36  ? 51  HIS   B CD2 1 
ATOM   695  C CE1 . HIS   B 2 42  ? -12.441 4.322   -12.118 1.00 40.22  ? 51  HIS   B CE1 1 
ATOM   696  N NE2 . HIS   B 2 42  ? -12.321 5.611   -12.488 1.00 36.06  ? 51  HIS   B NE2 1 
ATOM   697  N N   . VAL   B 2 43  ? -15.353 7.228   -9.785  1.00 39.54  ? 52  VAL   B N   1 
ATOM   698  C CA  . VAL   B 2 43  ? -16.079 8.277   -10.552 1.00 42.39  ? 52  VAL   B CA  1 
ATOM   699  C C   . VAL   B 2 43  ? -16.742 9.266   -9.589  1.00 44.42  ? 52  VAL   B C   1 
ATOM   700  O O   . VAL   B 2 43  ? -16.492 10.456  -9.734  1.00 48.65  ? 52  VAL   B O   1 
ATOM   701  C CB  . VAL   B 2 43  ? -17.075 7.636   -11.531 1.00 41.62  ? 52  VAL   B CB  1 
ATOM   702  C CG1 . VAL   B 2 43  ? -18.022 8.644   -12.162 1.00 42.01  ? 52  VAL   B CG1 1 
ATOM   703  C CG2 . VAL   B 2 43  ? -16.347 6.874   -12.626 1.00 41.62  ? 52  VAL   B CG2 1 
ATOM   704  N N   . THR   B 2 44  ? -17.592 8.788   -8.685  1.00 44.14  ? 53  THR   B N   1 
ATOM   705  C CA  . THR   B 2 44  ? -18.462 9.619   -7.794  1.00 42.35  ? 53  THR   B CA  1 
ATOM   706  C C   . THR   B 2 44  ? -17.824 9.824   -6.420  1.00 46.72  ? 53  THR   B C   1 
ATOM   707  O O   . THR   B 2 44  ? -18.203 10.825  -5.735  1.00 45.24  ? 53  THR   B O   1 
ATOM   708  C CB  . THR   B 2 44  ? -19.868 9.010   -7.732  1.00 40.89  ? 53  THR   B CB  1 
ATOM   709  O OG1 . THR   B 2 44  ? -19.827 7.770   -7.030  1.00 37.24  ? 53  THR   B OG1 1 
ATOM   710  C CG2 . THR   B 2 44  ? -20.442 8.814   -9.121  1.00 44.79  ? 53  THR   B CG2 1 
ATOM   711  N N   . LYS   B 2 45  ? -16.912 8.937   -6.006  1.00 47.20  ? 54  LYS   B N   1 
ATOM   712  C CA  . LYS   B 2 45  ? -16.447 8.804   -4.594  1.00 48.14  ? 54  LYS   B CA  1 
ATOM   713  C C   . LYS   B 2 45  ? -17.626 8.568   -3.640  1.00 44.76  ? 54  LYS   B C   1 
ATOM   714  O O   . LYS   B 2 45  ? -17.514 8.908   -2.436  1.00 48.87  ? 54  LYS   B O   1 
ATOM   715  C CB  . LYS   B 2 45  ? -15.735 10.053  -4.064  1.00 52.63  ? 54  LYS   B CB  1 
ATOM   716  C CG  . LYS   B 2 45  ? -14.650 10.624  -4.948  1.00 61.04  ? 54  LYS   B CG  1 
ATOM   717  C CD  . LYS   B 2 45  ? -13.514 9.684   -5.240  1.00 63.18  ? 54  LYS   B CD  1 
ATOM   718  C CE  . LYS   B 2 45  ? -12.409 10.428  -5.963  1.00 68.77  ? 54  LYS   B CE  1 
ATOM   719  N NZ  . LYS   B 2 45  ? -11.861 9.623   -7.074  1.00 73.37  ? 54  LYS   B NZ  1 
ATOM   720  N N   . GLY   B 2 46  ? -18.738 8.031   -4.112  1.00 47.53  ? 55  GLY   B N   1 
ATOM   721  C CA  . GLY   B 2 46  ? -19.893 7.770   -3.235  1.00 47.53  ? 55  GLY   B CA  1 
ATOM   722  C C   . GLY   B 2 46  ? -20.777 8.991   -3.033  1.00 48.04  ? 55  GLY   B C   1 
ATOM   723  O O   . GLY   B 2 46  ? -21.692 8.896   -2.234  1.00 52.81  ? 55  GLY   B O   1 
ATOM   724  N N   . ALA   B 2 47  ? -20.563 10.084  -3.766  1.00 48.48  ? 56  ALA   B N   1 
ATOM   725  C CA  . ALA   B 2 47  ? -21.381 11.320  -3.649  1.00 39.28  ? 56  ALA   B CA  1 
ATOM   726  C C   . ALA   B 2 47  ? -22.772 11.125  -4.270  1.00 40.27  ? 56  ALA   B C   1 
ATOM   727  O O   . ALA   B 2 47  ? -22.934 10.326  -5.201  1.00 41.31  ? 56  ALA   B O   1 
ATOM   728  C CB  . ALA   B 2 47  ? -20.660 12.471  -4.312  1.00 38.65  ? 56  ALA   B CB  1 
ATOM   729  N N   . ALA   B 2 48  ? -23.737 11.951  -3.875  1.00 44.90  ? 57  ALA   B N   1 
ATOM   730  C CA  . ALA   B 2 48  ? -25.087 12.015  -4.472  1.00 46.43  ? 57  ALA   B CA  1 
ATOM   731  C C   . ALA   B 2 48  ? -25.001 12.560  -5.899  1.00 37.31  ? 57  ALA   B C   1 
ATOM   732  O O   . ALA   B 2 48  ? -24.032 13.213  -6.234  1.00 51.14  ? 57  ALA   B O   1 
ATOM   733  C CB  . ALA   B 2 48  ? -26.015 12.854  -3.626  1.00 46.70  ? 57  ALA   B CB  1 
ATOM   734  N N   . LEU   B 2 49  ? -25.974 12.201  -6.726  1.00 37.78  ? 58  LEU   B N   1 
ATOM   735  C CA  . LEU   B 2 49  ? -26.112 12.601  -8.147  1.00 41.13  ? 58  LEU   B CA  1 
ATOM   736  C C   . LEU   B 2 49  ? -27.466 13.268  -8.385  1.00 41.24  ? 58  LEU   B C   1 
ATOM   737  O O   . LEU   B 2 49  ? -28.466 12.928  -7.716  1.00 49.88  ? 58  LEU   B O   1 
ATOM   738  C CB  . LEU   B 2 49  ? -25.985 11.372  -9.064  1.00 37.21  ? 58  LEU   B CB  1 
ATOM   739  C CG  . LEU   B 2 49  ? -24.701 10.538  -8.922  1.00 41.32  ? 58  LEU   B CG  1 
ATOM   740  C CD1 . LEU   B 2 49  ? -24.844 9.213   -9.647  1.00 40.71  ? 58  LEU   B CD1 1 
ATOM   741  C CD2 . LEU   B 2 49  ? -23.497 11.286  -9.453  1.00 46.43  ? 58  LEU   B CD2 1 
ATOM   742  N N   . ARG   B 2 50  ? -27.500 14.113  -9.405  1.00 43.86  ? 59  ARG   B N   1 
ATOM   743  C CA  . ARG   B 2 50  ? -28.745 14.759  -9.887  1.00 53.51  ? 59  ARG   B CA  1 
ATOM   744  C C   . ARG   B 2 50  ? -29.135 14.134  -11.232 1.00 51.82  ? 59  ARG   B C   1 
ATOM   745  O O   . ARG   B 2 50  ? -28.242 13.838  -12.024 1.00 54.03  ? 59  ARG   B O   1 
ATOM   746  C CB  . ARG   B 2 50  ? -28.496 16.269  -9.920  1.00 62.98  ? 59  ARG   B CB  1 
ATOM   747  C CG  . ARG   B 2 50  ? -29.664 17.086  -10.448 1.00 77.74  ? 59  ARG   B CG  1 
ATOM   748  C CD  . ARG   B 2 50  ? -29.461 18.577  -10.245 1.00 76.81  ? 59  ARG   B CD  1 
ATOM   749  N NE  . ARG   B 2 50  ? -28.106 19.057  -10.526 1.00 83.42  ? 59  ARG   B NE  1 
ATOM   750  C CZ  . ARG   B 2 50  ? -27.618 19.373  -11.736 1.00 79.69  ? 59  ARG   B CZ  1 
ATOM   751  N NH1 . ARG   B 2 50  ? -28.341 19.210  -12.837 1.00 75.83  ? 59  ARG   B NH1 1 
ATOM   752  N NH2 . ARG   B 2 50  ? -26.388 19.850  -11.833 1.00 78.56  ? 59  ARG   B NH2 1 
ATOM   753  N N   . SER   B 2 51  ? -30.426 13.881  -11.434 1.00 56.06  ? 60  SER   B N   1 
ATOM   754  C CA  . SER   B 2 51  ? -31.051 13.576  -12.746 1.00 60.57  ? 60  SER   B CA  1 
ATOM   755  C C   . SER   B 2 51  ? -32.210 14.562  -13.013 1.00 63.65  ? 60  SER   B C   1 
ATOM   756  O O   . SER   B 2 51  ? -33.371 14.269  -12.644 1.00 59.82  ? 60  SER   B O   1 
ATOM   757  C CB  . SER   B 2 51  ? -31.507 12.146  -12.798 1.00 49.85  ? 60  SER   B CB  1 
ATOM   758  O OG  . SER   B 2 51  ? -31.927 11.841  -14.103 1.00 56.12  ? 60  SER   B OG  1 
ATOM   759  N N   . GLY   B 2 52  ? -31.909 15.706  -13.624 1.00 69.55  ? 61  GLY   B N   1 
ATOM   760  C CA  . GLY   B 2 52  ? -32.847 16.843  -13.711 1.00 79.65  ? 61  GLY   B CA  1 
ATOM   761  C C   . GLY   B 2 52  ? -33.121 17.442  -12.335 1.00 75.92  ? 61  GLY   B C   1 
ATOM   762  O O   . GLY   B 2 52  ? -32.185 17.996  -11.738 1.00 79.94  ? 61  GLY   B O   1 
ATOM   763  N N   . GLU   B 2 53  ? -34.358 17.314  -11.847 1.00 75.88  ? 62  GLU   B N   1 
ATOM   764  C CA  . GLU   B 2 53  ? -34.791 17.725  -10.487 1.00 84.11  ? 62  GLU   B CA  1 
ATOM   765  C C   . GLU   B 2 53  ? -34.483 16.609  -9.486  1.00 77.00  ? 62  GLU   B C   1 
ATOM   766  O O   . GLU   B 2 53  ? -34.099 16.949  -8.358  1.00 83.55  ? 62  GLU   B O   1 
ATOM   767  C CB  . GLU   B 2 53  ? -36.296 17.976  -10.442 1.00 100.50 ? 62  GLU   B CB  1 
ATOM   768  C CG  . GLU   B 2 53  ? -36.698 19.422  -10.654 1.00 109.17 ? 62  GLU   B CG  1 
ATOM   769  C CD  . GLU   B 2 53  ? -38.194 19.582  -10.891 1.00 115.79 ? 62  GLU   B CD  1 
ATOM   770  O OE1 . GLU   B 2 53  ? -38.969 19.474  -9.909  1.00 96.19  ? 62  GLU   B OE1 1 
ATOM   771  O OE2 . GLU   B 2 53  ? -38.586 19.778  -12.061 1.00 122.14 ? 62  GLU   B OE2 1 
ATOM   772  N N   . GLY   B 2 54  ? -34.684 15.347  -9.891  1.00 70.82  ? 63  GLY   B N   1 
ATOM   773  C CA  . GLY   B 2 54  ? -34.480 14.126  -9.082  1.00 65.63  ? 63  GLY   B CA  1 
ATOM   774  C C   . GLY   B 2 54  ? -33.074 14.020  -8.511  1.00 64.64  ? 63  GLY   B C   1 
ATOM   775  O O   . GLY   B 2 54  ? -32.116 14.372  -9.220  1.00 62.52  ? 63  GLY   B O   1 
ATOM   776  N N   . ARG   B 2 55  ? -32.972 13.552  -7.262  1.00 55.87  ? 64  ARG   B N   1 
ATOM   777  C CA  . ARG   B 2 55  ? -31.710 13.232  -6.543  1.00 52.42  ? 64  ARG   B CA  1 
ATOM   778  C C   . ARG   B 2 55  ? -31.495 11.703  -6.573  1.00 59.93  ? 64  ARG   B C   1 
ATOM   779  O O   . ARG   B 2 55  ? -32.474 10.946  -6.447  1.00 54.53  ? 64  ARG   B O   1 
ATOM   780  C CB  . ARG   B 2 55  ? -31.789 13.749  -5.103  1.00 59.14  ? 64  ARG   B CB  1 
ATOM   781  C CG  . ARG   B 2 55  ? -30.470 13.785  -4.344  1.00 63.45  ? 64  ARG   B CG  1 
ATOM   782  C CD  . ARG   B 2 55  ? -30.657 14.116  -2.866  1.00 74.24  ? 64  ARG   B CD  1 
ATOM   783  N NE  . ARG   B 2 55  ? -29.487 13.762  -2.056  1.00 76.14  ? 64  ARG   B NE  1 
ATOM   784  C CZ  . ARG   B 2 55  ? -28.700 14.613  -1.383  1.00 74.24  ? 64  ARG   B CZ  1 
ATOM   785  N NH1 . ARG   B 2 55  ? -28.943 15.911  -1.392  1.00 72.80  ? 64  ARG   B NH1 1 
ATOM   786  N NH2 . ARG   B 2 55  ? -27.672 14.156  -0.681  1.00 71.68  ? 64  ARG   B NH2 1 
ATOM   787  N N   . LEU   B 2 56  ? -30.257 11.252  -6.774  1.00 50.29  ? 65  LEU   B N   1 
ATOM   788  C CA  . LEU   B 2 56  ? -29.895 9.815   -6.729  1.00 47.24  ? 65  LEU   B CA  1 
ATOM   789  C C   . LEU   B 2 56  ? -28.952 9.638   -5.537  1.00 42.97  ? 65  LEU   B C   1 
ATOM   790  O O   . LEU   B 2 56  ? -27.846 10.264  -5.549  1.00 43.58  ? 65  LEU   B O   1 
ATOM   791  C CB  . LEU   B 2 56  ? -29.205 9.380   -8.037  1.00 48.38  ? 65  LEU   B CB  1 
ATOM   792  C CG  . LEU   B 2 56  ? -29.982 9.405   -9.350  1.00 56.03  ? 65  LEU   B CG  1 
ATOM   793  C CD1 . LEU   B 2 56  ? -29.301 8.492   -10.360 1.00 56.28  ? 65  LEU   B CD1 1 
ATOM   794  C CD2 . LEU   B 2 56  ? -31.422 8.969   -9.179  1.00 60.58  ? 65  LEU   B CD2 1 
ATOM   795  N N   . ASP   B 2 57  ? -29.356 8.852   -4.537  1.00 39.08  ? 66  ASP   B N   1 
ATOM   796  C CA  . ASP   B 2 57  ? -28.536 8.564   -3.335  1.00 42.11  ? 66  ASP   B CA  1 
ATOM   797  C C   . ASP   B 2 57  ? -27.866 7.196   -3.441  1.00 41.48  ? 66  ASP   B C   1 
ATOM   798  O O   . ASP   B 2 57  ? -28.494 6.206   -3.866  1.00 39.96  ? 66  ASP   B O   1 
ATOM   799  C CB  . ASP   B 2 57  ? -29.372 8.635   -2.060  1.00 52.29  ? 66  ASP   B CB  1 
ATOM   800  C CG  . ASP   B 2 57  ? -29.950 10.025  -1.817  1.00 57.50  ? 66  ASP   B CG  1 
ATOM   801  O OD1 . ASP   B 2 57  ? -29.211 11.009  -1.988  1.00 59.84  ? 66  ASP   B OD1 1 
ATOM   802  O OD2 . ASP   B 2 57  ? -31.137 10.107  -1.513  1.00 55.75  ? 66  ASP   B OD2 1 
ATOM   803  N N   . PRO   B 2 58  ? -26.596 7.087   -2.983  1.00 42.22  ? 67  PRO   B N   1 
ATOM   804  C CA  . PRO   B 2 58  ? -25.902 5.798   -2.939  1.00 39.40  ? 67  PRO   B CA  1 
ATOM   805  C C   . PRO   B 2 58  ? -26.677 4.785   -2.079  1.00 42.14  ? 67  PRO   B C   1 
ATOM   806  O O   . PRO   B 2 58  ? -27.321 5.133   -1.102  1.00 43.43  ? 67  PRO   B O   1 
ATOM   807  C CB  . PRO   B 2 58  ? -24.523 6.157   -2.366  1.00 40.54  ? 67  PRO   B CB  1 
ATOM   808  C CG  . PRO   B 2 58  ? -24.776 7.419   -1.589  1.00 41.72  ? 67  PRO   B CG  1 
ATOM   809  C CD  . PRO   B 2 58  ? -25.776 8.181   -2.429  1.00 41.30  ? 67  PRO   B CD  1 
ATOM   810  N N   . TYR   B 2 59  ? -26.625 3.519   -2.480  1.00 34.13  ? 68  TYR   B N   1 
ATOM   811  C CA  . TYR   B 2 59  ? -27.311 2.398   -1.806  1.00 34.91  ? 68  TYR   B CA  1 
ATOM   812  C C   . TYR   B 2 59  ? -26.268 1.364   -1.414  1.00 32.50  ? 68  TYR   B C   1 
ATOM   813  O O   . TYR   B 2 59  ? -26.310 0.898   -0.306  1.00 35.67  ? 68  TYR   B O   1 
ATOM   814  C CB  . TYR   B 2 59  ? -28.369 1.821   -2.732  1.00 35.13  ? 68  TYR   B CB  1 
ATOM   815  C CG  . TYR   B 2 59  ? -29.162 0.680   -2.157  1.00 35.40  ? 68  TYR   B CG  1 
ATOM   816  C CD1 . TYR   B 2 59  ? -28.640 -0.598  -2.141  1.00 38.97  ? 68  TYR   B CD1 1 
ATOM   817  C CD2 . TYR   B 2 59  ? -30.450 0.872   -1.684  1.00 42.15  ? 68  TYR   B CD2 1 
ATOM   818  C CE1 . TYR   B 2 59  ? -29.388 -1.662  -1.652  1.00 41.76  ? 68  TYR   B CE1 1 
ATOM   819  C CE2 . TYR   B 2 59  ? -31.209 -0.184  -1.191  1.00 42.17  ? 68  TYR   B CE2 1 
ATOM   820  C CZ  . TYR   B 2 59  ? -30.673 -1.461  -1.178  1.00 42.77  ? 68  TYR   B CZ  1 
ATOM   821  O OH  . TYR   B 2 59  ? -31.383 -2.526  -0.675  1.00 41.56  ? 68  TYR   B OH  1 
ATOM   822  N N   . TRP   B 2 60  ? -25.335 1.076   -2.313  1.00 32.93  ? 69  TRP   B N   1 
ATOM   823  C CA  . TRP   B 2 60  ? -24.256 0.078   -2.027  1.00 35.67  ? 69  TRP   B CA  1 
ATOM   824  C C   . TRP   B 2 60  ? -22.954 0.579   -2.659  1.00 33.15  ? 69  TRP   B C   1 
ATOM   825  O O   . TRP   B 2 60  ? -22.995 1.119   -3.795  1.00 37.45  ? 69  TRP   B O   1 
ATOM   826  C CB  . TRP   B 2 60  ? -24.645 -1.303  -2.564  1.00 33.20  ? 69  TRP   B CB  1 
ATOM   827  C CG  . TRP   B 2 60  ? -23.502 -2.269  -2.477  1.00 32.15  ? 69  TRP   B CG  1 
ATOM   828  C CD1 . TRP   B 2 60  ? -23.111 -3.025  -1.408  1.00 37.71  ? 69  TRP   B CD1 1 
ATOM   829  C CD2 . TRP   B 2 60  ? -22.609 -2.610  -3.556  1.00 36.99  ? 69  TRP   B CD2 1 
ATOM   830  N NE1 . TRP   B 2 60  ? -22.006 -3.772  -1.738  1.00 33.86  ? 69  TRP   B NE1 1 
ATOM   831  C CE2 . TRP   B 2 60  ? -21.665 -3.531  -3.030  1.00 32.91  ? 69  TRP   B CE2 1 
ATOM   832  C CE3 . TRP   B 2 60  ? -22.482 -2.182  -4.877  1.00 40.65  ? 69  TRP   B CE3 1 
ATOM   833  C CZ2 . TRP   B 2 60  ? -20.609 -4.018  -3.796  1.00 34.35  ? 69  TRP   B CZ2 1 
ATOM   834  C CZ3 . TRP   B 2 60  ? -21.473 -2.719  -5.656  1.00 42.38  ? 69  TRP   B CZ3 1 
ATOM   835  C CH2 . TRP   B 2 60  ? -20.548 -3.622  -5.112  1.00 36.40  ? 69  TRP   B CH2 1 
ATOM   836  N N   . GLY   B 2 61  ? -21.835 0.281   -2.055  1.00 35.09  ? 70  GLY   B N   1 
ATOM   837  C CA  . GLY   B 2 61  ? -20.537 0.588   -2.668  1.00 37.42  ? 70  GLY   B CA  1 
ATOM   838  C C   . GLY   B 2 61  ? -19.407 -0.166  -2.006  1.00 30.34  ? 70  GLY   B C   1 
ATOM   839  O O   . GLY   B 2 61  ? -19.538 -0.517  -0.801  1.00 35.24  ? 70  GLY   B O   1 
ATOM   840  N N   . ASP   B 2 62  ? -18.293 -0.301  -2.724  1.00 32.53  ? 71  ASP   B N   1 
ATOM   841  C CA  . ASP   B 2 62  ? -17.122 -1.085  -2.241  1.00 33.56  ? 71  ASP   B CA  1 
ATOM   842  C C   . ASP   B 2 62  ? -15.864 -0.586  -2.946  1.00 30.20  ? 71  ASP   B C   1 
ATOM   843  O O   . ASP   B 2 62  ? -15.792 -0.735  -4.166  1.00 34.55  ? 71  ASP   B O   1 
ATOM   844  C CB  . ASP   B 2 62  ? -17.377 -2.564  -2.491  1.00 35.27  ? 71  ASP   B CB  1 
ATOM   845  C CG  . ASP   B 2 62  ? -16.307 -3.446  -1.875  1.00 44.21  ? 71  ASP   B CG  1 
ATOM   846  O OD1 . ASP   B 2 62  ? -15.120 -3.243  -2.176  1.00 46.52  ? 71  ASP   B OD1 1 
ATOM   847  O OD2 . ASP   B 2 62  ? -16.660 -4.274  -1.054  1.00 53.09  ? 71  ASP   B OD2 1 
ATOM   848  N N   . VAL   B 2 63  ? -14.964 0.075   -2.232  1.00 34.48  ? 72  VAL   B N   1 
ATOM   849  C CA  . VAL   B 2 63  ? -13.749 0.714   -2.809  1.00 32.72  ? 72  VAL   B CA  1 
ATOM   850  C C   . VAL   B 2 63  ? -12.850 -0.374  -3.414  1.00 37.30  ? 72  VAL   B C   1 
ATOM   851  O O   . VAL   B 2 63  ? -12.165 -0.097  -4.440  1.00 41.41  ? 72  VAL   B O   1 
ATOM   852  C CB  . VAL   B 2 63  ? -13.000 1.550   -1.761  1.00 36.86  ? 72  VAL   B CB  1 
ATOM   853  C CG1 . VAL   B 2 63  ? -11.537 1.719   -2.132  1.00 41.25  ? 72  VAL   B CG1 1 
ATOM   854  C CG2 . VAL   B 2 63  ? -13.666 2.900   -1.584  1.00 41.47  ? 72  VAL   B CG2 1 
ATOM   855  N N   . LYS   B 2 64  ? -12.923 -1.606  -2.913  1.00 42.23  ? 73  LYS   B N   1 
ATOM   856  C CA  . LYS   B 2 64  ? -12.004 -2.648  -3.447  1.00 41.65  ? 73  LYS   B CA  1 
ATOM   857  C C   . LYS   B 2 64  ? -12.504 -3.172  -4.801  1.00 40.24  ? 73  LYS   B C   1 
ATOM   858  O O   . LYS   B 2 64  ? -11.678 -3.271  -5.757  1.00 43.86  ? 73  LYS   B O   1 
ATOM   859  C CB  . LYS   B 2 64  ? -11.804 -3.809  -2.483  1.00 36.01  ? 73  LYS   B CB  1 
ATOM   860  C CG  . LYS   B 2 64  ? -10.738 -4.769  -3.016  1.00 37.58  ? 73  LYS   B CG  1 
ATOM   861  C CD  . LYS   B 2 64  ? -10.291 -5.772  -2.003  1.00 36.75  ? 73  LYS   B CD  1 
ATOM   862  C CE  . LYS   B 2 64  ? -9.307  -6.779  -2.568  1.00 46.60  ? 73  LYS   B CE  1 
ATOM   863  N NZ  . LYS   B 2 64  ? -9.040  -7.829  -1.552  1.00 44.90  ? 73  LYS   B NZ  1 
ATOM   864  N N   . GLN   B 2 65  ? -13.804 -3.459  -4.909  1.00 40.24  ? 74  GLN   B N   1 
ATOM   865  C CA  . GLN   B 2 65  ? -14.453 -3.794  -6.186  1.00 38.60  ? 74  GLN   B CA  1 
ATOM   866  C C   . GLN   B 2 65  ? -14.467 -2.588  -7.147  1.00 37.13  ? 74  GLN   B C   1 
ATOM   867  O O   . GLN   B 2 65  ? -14.582 -2.821  -8.398  1.00 42.64  ? 74  GLN   B O   1 
ATOM   868  C CB  . GLN   B 2 65  ? -15.869 -4.296  -5.938  1.00 40.40  ? 74  GLN   B CB  1 
ATOM   869  C CG  . GLN   B 2 65  ? -15.905 -5.634  -5.221  1.00 45.72  ? 74  GLN   B CG  1 
ATOM   870  C CD  . GLN   B 2 65  ? -17.342 -6.092  -5.106  1.00 46.81  ? 74  GLN   B CD  1 
ATOM   871  O OE1 . GLN   B 2 65  ? -18.070 -6.220  -6.107  1.00 51.85  ? 74  GLN   B OE1 1 
ATOM   872  N NE2 . GLN   B 2 65  ? -17.783 -6.273  -3.876  1.00 48.14  ? 74  GLN   B NE2 1 
ATOM   873  N N   . ASP   B 2 66  ? -14.314 -1.382  -6.600  1.00 37.87  ? 75  ASP   B N   1 
ATOM   874  C CA  . ASP   B 2 66  ? -14.384 -0.052  -7.277  1.00 37.07  ? 75  ASP   B CA  1 
ATOM   875  C C   . ASP   B 2 66  ? -15.745 0.082   -7.939  1.00 36.59  ? 75  ASP   B C   1 
ATOM   876  O O   . ASP   B 2 66  ? -15.775 0.549   -9.080  1.00 39.88  ? 75  ASP   B O   1 
ATOM   877  C CB  . ASP   B 2 66  ? -13.283 0.173   -8.316  1.00 41.15  ? 75  ASP   B CB  1 
ATOM   878  C CG  . ASP   B 2 66  ? -13.175 1.608   -8.819  1.00 40.84  ? 75  ASP   B CG  1 
ATOM   879  O OD1 . ASP   B 2 66  ? -13.534 2.549   -8.074  1.00 41.82  ? 75  ASP   B OD1 1 
ATOM   880  O OD2 . ASP   B 2 66  ? -12.738 1.768   -9.988  1.00 38.91  ? 75  ASP   B OD2 1 
ATOM   881  N N   . LEU   B 2 67  ? -16.819 -0.347  -7.246  1.00 32.19  ? 76  LEU   B N   1 
ATOM   882  C CA  . LEU   B 2 67  ? -18.217 -0.256  -7.768  1.00 30.31  ? 76  LEU   B CA  1 
ATOM   883  C C   . LEU   B 2 67  ? -19.118 0.506   -6.795  1.00 32.23  ? 76  LEU   B C   1 
ATOM   884  O O   . LEU   B 2 67  ? -18.793 0.563   -5.577  1.00 36.21  ? 76  LEU   B O   1 
ATOM   885  C CB  . LEU   B 2 67  ? -18.750 -1.661  -7.982  1.00 32.55  ? 76  LEU   B CB  1 
ATOM   886  C CG  . LEU   B 2 67  ? -18.060 -2.444  -9.106  1.00 34.21  ? 76  LEU   B CG  1 
ATOM   887  C CD1 . LEU   B 2 67  ? -18.685 -3.839  -9.227  1.00 32.47  ? 76  LEU   B CD1 1 
ATOM   888  C CD2 . LEU   B 2 67  ? -18.167 -1.683  -10.449 1.00 35.46  ? 76  LEU   B CD2 1 
ATOM   889  N N   . VAL   B 2 68  ? -20.235 1.015   -7.316  1.00 33.35  ? 77  VAL   B N   1 
ATOM   890  C CA  . VAL   B 2 68  ? -21.275 1.712   -6.504  1.00 37.69  ? 77  VAL   B CA  1 
ATOM   891  C C   . VAL   B 2 68  ? -22.608 1.669   -7.246  1.00 32.85  ? 77  VAL   B C   1 
ATOM   892  O O   . VAL   B 2 68  ? -22.634 1.819   -8.485  1.00 33.70  ? 77  VAL   B O   1 
ATOM   893  C CB  . VAL   B 2 68  ? -20.817 3.144   -6.166  1.00 36.60  ? 77  VAL   B CB  1 
ATOM   894  C CG1 . VAL   B 2 68  ? -20.497 3.930   -7.411  1.00 35.52  ? 77  VAL   B CG1 1 
ATOM   895  C CG2 . VAL   B 2 68  ? -21.842 3.909   -5.341  1.00 36.99  ? 77  VAL   B CG2 1 
ATOM   896  N N   . SER   B 2 69  ? -23.697 1.474   -6.519  1.00 35.08  ? 78  SER   B N   1 
ATOM   897  C CA  . SER   B 2 69  ? -25.081 1.502   -7.069  1.00 33.11  ? 78  SER   B CA  1 
ATOM   898  C C   . SER   B 2 69  ? -25.870 2.626   -6.361  1.00 31.80  ? 78  SER   B C   1 
ATOM   899  O O   . SER   B 2 69  ? -25.596 2.916   -5.150  1.00 31.32  ? 78  SER   B O   1 
ATOM   900  C CB  . SER   B 2 69  ? -25.785 0.160   -6.910  1.00 32.19  ? 78  SER   B CB  1 
ATOM   901  O OG  . SER   B 2 69  ? -26.030 -0.151  -5.543  1.00 36.33  ? 78  SER   B OG  1 
ATOM   902  N N   . TYR   B 2 70  ? -26.839 3.188   -7.078  1.00 35.23  ? 79  TYR   B N   1 
ATOM   903  C CA  . TYR   B 2 70  ? -27.723 4.297   -6.615  1.00 36.37  ? 79  TYR   B CA  1 
ATOM   904  C C   . TYR   B 2 70  ? -29.176 3.808   -6.735  1.00 36.19  ? 79  TYR   B C   1 
ATOM   905  O O   . TYR   B 2 70  ? -29.517 3.135   -7.736  1.00 36.67  ? 79  TYR   B O   1 
ATOM   906  C CB  . TYR   B 2 70  ? -27.470 5.570   -7.431  1.00 38.90  ? 79  TYR   B CB  1 
ATOM   907  C CG  . TYR   B 2 70  ? -26.141 6.237   -7.161  1.00 36.43  ? 79  TYR   B CG  1 
ATOM   908  C CD1 . TYR   B 2 70  ? -24.964 5.687   -7.645  1.00 38.38  ? 79  TYR   B CD1 1 
ATOM   909  C CD2 . TYR   B 2 70  ? -26.037 7.396   -6.401  1.00 40.17  ? 79  TYR   B CD2 1 
ATOM   910  C CE1 . TYR   B 2 70  ? -23.726 6.256   -7.366  1.00 41.30  ? 79  TYR   B CE1 1 
ATOM   911  C CE2 . TYR   B 2 70  ? -24.813 8.003   -6.145  1.00 39.95  ? 79  TYR   B CE2 1 
ATOM   912  C CZ  . TYR   B 2 70  ? -23.645 7.427   -6.626  1.00 41.01  ? 79  TYR   B CZ  1 
ATOM   913  O OH  . TYR   B 2 70  ? -22.414 7.980   -6.351  1.00 38.03  ? 79  TYR   B OH  1 
ATOM   914  N N   . CYS   B 2 71  ? -29.978 4.089   -5.701  1.00 39.88  ? 80  CYS   B N   1 
ATOM   915  C CA  . CYS   B 2 71  ? -31.462 3.908   -5.643  1.00 41.15  ? 80  CYS   B CA  1 
ATOM   916  C C   . CYS   B 2 71  ? -31.811 2.454   -5.347  1.00 43.72  ? 80  CYS   B C   1 
ATOM   917  O O   . CYS   B 2 71  ? -33.001 2.169   -5.135  1.00 44.56  ? 80  CYS   B O   1 
ATOM   918  C CB  . CYS   B 2 71  ? -32.156 4.365   -6.922  1.00 42.48  ? 80  CYS   B CB  1 
ATOM   919  S SG  . CYS   B 2 71  ? -31.737 6.079   -7.379  1.00 49.98  ? 80  CYS   B SG  1 
ATOM   920  N N   . GLY   B 2 72  ? -30.819 1.558   -5.279  1.00 38.69  ? 81  GLY   B N   1 
ATOM   921  C CA  . GLY   B 2 72  ? -31.136 0.135   -5.075  1.00 38.45  ? 81  GLY   B CA  1 
ATOM   922  C C   . GLY   B 2 72  ? -29.917 -0.757  -5.271  1.00 37.32  ? 81  GLY   B C   1 
ATOM   923  O O   . GLY   B 2 72  ? -28.808 -0.264  -5.466  1.00 36.92  ? 81  GLY   B O   1 
ATOM   924  N N   . PRO   B 2 73  ? -30.085 -2.074  -5.034  1.00 37.14  ? 82  PRO   B N   1 
ATOM   925  C CA  . PRO   B 2 73  ? -28.965 -3.012  -5.047  1.00 41.91  ? 82  PRO   B CA  1 
ATOM   926  C C   . PRO   B 2 73  ? -28.440 -3.219  -6.472  1.00 38.92  ? 82  PRO   B C   1 
ATOM   927  O O   . PRO   B 2 73  ? -29.230 -3.105  -7.393  1.00 36.88  ? 82  PRO   B O   1 
ATOM   928  C CB  . PRO   B 2 73  ? -29.546 -4.310  -4.447  1.00 40.85  ? 82  PRO   B CB  1 
ATOM   929  C CG  . PRO   B 2 73  ? -31.068 -4.178  -4.595  1.00 42.66  ? 82  PRO   B CG  1 
ATOM   930  C CD  . PRO   B 2 73  ? -31.355 -2.695  -4.634  1.00 40.19  ? 82  PRO   B CD  1 
ATOM   931  N N   . TRP   B 2 74  ? -27.141 -3.485  -6.622  1.00 38.70  ? 83  TRP   B N   1 
ATOM   932  C CA  . TRP   B 2 74  ? -26.503 -3.909  -7.896  1.00 42.26  ? 83  TRP   B CA  1 
ATOM   933  C C   . TRP   B 2 74  ? -27.394 -4.927  -8.634  1.00 38.39  ? 83  TRP   B C   1 
ATOM   934  O O   . TRP   B 2 74  ? -27.675 -5.975  -8.049  1.00 40.83  ? 83  TRP   B O   1 
ATOM   935  C CB  . TRP   B 2 74  ? -25.099 -4.474  -7.625  1.00 42.07  ? 83  TRP   B CB  1 
ATOM   936  C CG  . TRP   B 2 74  ? -24.295 -4.633  -8.878  1.00 39.24  ? 83  TRP   B CG  1 
ATOM   937  C CD1 . TRP   B 2 74  ? -24.221 -5.728  -9.692  1.00 35.69  ? 83  TRP   B CD1 1 
ATOM   938  C CD2 . TRP   B 2 74  ? -23.472 -3.622  -9.478  1.00 34.16  ? 83  TRP   B CD2 1 
ATOM   939  N NE1 . TRP   B 2 74  ? -23.393 -5.467  -10.754 1.00 37.70  ? 83  TRP   B NE1 1 
ATOM   940  C CE2 . TRP   B 2 74  ? -22.905 -4.185  -10.643 1.00 35.92  ? 83  TRP   B CE2 1 
ATOM   941  C CE3 . TRP   B 2 74  ? -23.147 -2.301  -9.127  1.00 36.35  ? 83  TRP   B CE3 1 
ATOM   942  C CZ2 . TRP   B 2 74  ? -22.084 -3.455  -11.499 1.00 38.14  ? 83  TRP   B CZ2 1 
ATOM   943  C CZ3 . TRP   B 2 74  ? -22.288 -1.596  -9.935  1.00 35.53  ? 83  TRP   B CZ3 1 
ATOM   944  C CH2 . TRP   B 2 74  ? -21.789 -2.162  -11.122 1.00 41.54  ? 83  TRP   B CH2 1 
ATOM   945  N N   . LYS   B 2 75  ? -27.735 -4.667  -9.905  1.00 37.74  ? 84  LYS   B N   1 
ATOM   946  C CA  . LYS   B 2 75  ? -28.692 -5.493  -10.699 1.00 39.93  ? 84  LYS   B CA  1 
ATOM   947  C C   . LYS   B 2 75  ? -27.992 -6.306  -11.796 1.00 42.02  ? 84  LYS   B C   1 
ATOM   948  O O   . LYS   B 2 75  ? -28.625 -7.231  -12.280 1.00 49.72  ? 84  LYS   B O   1 
ATOM   949  C CB  . LYS   B 2 75  ? -29.726 -4.601  -11.390 1.00 47.64  ? 84  LYS   B CB  1 
ATOM   950  C CG  . LYS   B 2 75  ? -30.588 -3.745  -10.482 1.00 48.48  ? 84  LYS   B CG  1 
ATOM   951  C CD  . LYS   B 2 75  ? -31.572 -4.560  -9.721  1.00 53.08  ? 84  LYS   B CD  1 
ATOM   952  C CE  . LYS   B 2 75  ? -32.387 -3.698  -8.791  1.00 53.30  ? 84  LYS   B CE  1 
ATOM   953  N NZ  . LYS   B 2 75  ? -33.685 -4.331  -8.506  1.00 59.46  ? 84  LYS   B NZ  1 
ATOM   954  N N   . LEU   B 2 76  ? -26.755 -5.977  -12.179 1.00 41.65  ? 85  LEU   B N   1 
ATOM   955  C CA  . LEU   B 2 76  ? -26.085 -6.492  -13.400 1.00 43.08  ? 85  LEU   B CA  1 
ATOM   956  C C   . LEU   B 2 76  ? -25.314 -7.764  -13.041 1.00 47.86  ? 85  LEU   B C   1 
ATOM   957  O O   . LEU   B 2 76  ? -24.411 -7.681  -12.211 1.00 42.14  ? 85  LEU   B O   1 
ATOM   958  C CB  . LEU   B 2 76  ? -25.156 -5.400  -13.935 1.00 46.57  ? 85  LEU   B CB  1 
ATOM   959  C CG  . LEU   B 2 76  ? -25.822 -4.029  -14.139 1.00 44.43  ? 85  LEU   B CG  1 
ATOM   960  C CD1 . LEU   B 2 76  ? -24.865 -3.065  -14.800 1.00 43.48  ? 85  LEU   B CD1 1 
ATOM   961  C CD2 . LEU   B 2 76  ? -27.099 -4.129  -14.956 1.00 47.19  ? 85  LEU   B CD2 1 
ATOM   962  N N   . ASP   B 2 77  ? -25.696 -8.912  -13.602 1.00 46.69  ? 86  ASP   B N   1 
ATOM   963  C CA  . ASP   B 2 77  ? -25.168 -10.224 -13.147 1.00 57.97  ? 86  ASP   B CA  1 
ATOM   964  C C   . ASP   B 2 77  ? -24.679 -11.067 -14.331 1.00 53.54  ? 86  ASP   B C   1 
ATOM   965  O O   . ASP   B 2 77  ? -24.120 -12.129 -14.098 1.00 50.72  ? 86  ASP   B O   1 
ATOM   966  C CB  . ASP   B 2 77  ? -26.209 -10.975 -12.320 1.00 65.31  ? 86  ASP   B CB  1 
ATOM   967  C CG  . ASP   B 2 77  ? -27.537 -11.029 -13.024 1.00 72.89  ? 86  ASP   B CG  1 
ATOM   968  O OD1 . ASP   B 2 77  ? -27.647 -10.402 -14.101 1.00 82.74  ? 86  ASP   B OD1 1 
ATOM   969  O OD2 . ASP   B 2 77  ? -28.447 -11.671 -12.487 1.00 83.87  ? 86  ASP   B OD2 1 
ATOM   970  N N   . ALA   B 2 78  ? -24.782 -10.594 -15.558 1.00 50.49  ? 87  ALA   B N   1 
ATOM   971  C CA  . ALA   B 2 78  ? -24.260 -11.354 -16.697 1.00 44.98  ? 87  ALA   B CA  1 
ATOM   972  C C   . ALA   B 2 78  ? -22.740 -11.438 -16.500 1.00 47.35  ? 87  ALA   B C   1 
ATOM   973  O O   . ALA   B 2 78  ? -22.156 -10.506 -15.855 1.00 42.71  ? 87  ALA   B O   1 
ATOM   974  C CB  . ALA   B 2 78  ? -24.687 -10.752 -18.011 1.00 40.75  ? 87  ALA   B CB  1 
ATOM   975  N N   . ALA   B 2 79  ? -22.128 -12.491 -17.055 1.00 45.88  ? 88  ALA   B N   1 
ATOM   976  C CA  . ALA   B 2 79  ? -20.687 -12.823 -16.938 1.00 50.61  ? 88  ALA   B CA  1 
ATOM   977  C C   . ALA   B 2 79  ? -20.074 -13.090 -18.304 1.00 37.51  ? 88  ALA   B C   1 
ATOM   978  O O   . ALA   B 2 79  ? -20.727 -13.720 -19.140 1.00 40.28  ? 88  ALA   B O   1 
ATOM   979  C CB  . ALA   B 2 79  ? -20.544 -14.048 -16.083 1.00 52.43  ? 88  ALA   B CB  1 
ATOM   980  N N   . TRP   B 2 80  ? -18.860 -12.610 -18.554 1.00 40.77  ? 89  TRP   B N   1 
ATOM   981  C CA  . TRP   B 2 80  ? -18.051 -13.049 -19.716 1.00 45.83  ? 89  TRP   B CA  1 
ATOM   982  C C   . TRP   B 2 80  ? -18.026 -14.583 -19.728 1.00 48.59  ? 89  TRP   B C   1 
ATOM   983  O O   . TRP   B 2 80  ? -17.902 -15.171 -18.632 1.00 42.31  ? 89  TRP   B O   1 
ATOM   984  C CB  . TRP   B 2 80  ? -16.638 -12.458 -19.716 1.00 49.41  ? 89  TRP   B CB  1 
ATOM   985  C CG  . TRP   B 2 80  ? -15.892 -12.839 -20.963 1.00 55.82  ? 89  TRP   B CG  1 
ATOM   986  C CD1 . TRP   B 2 80  ? -16.431 -12.956 -22.214 1.00 57.30  ? 89  TRP   B CD1 1 
ATOM   987  C CD2 . TRP   B 2 80  ? -14.493 -13.171 -21.100 1.00 54.60  ? 89  TRP   B CD2 1 
ATOM   988  N NE1 . TRP   B 2 80  ? -15.475 -13.339 -23.114 1.00 55.32  ? 89  TRP   B NE1 1 
ATOM   989  C CE2 . TRP   B 2 80  ? -14.272 -13.468 -22.468 1.00 51.95  ? 89  TRP   B CE2 1 
ATOM   990  C CE3 . TRP   B 2 80  ? -13.416 -13.289 -20.214 1.00 51.10  ? 89  TRP   B CE3 1 
ATOM   991  C CZ2 . TRP   B 2 80  ? -13.026 -13.847 -22.964 1.00 44.63  ? 89  TRP   B CZ2 1 
ATOM   992  C CZ3 . TRP   B 2 80  ? -12.178 -13.646 -20.715 1.00 51.99  ? 89  TRP   B CZ3 1 
ATOM   993  C CH2 . TRP   B 2 80  ? -11.991 -13.949 -22.069 1.00 46.47  ? 89  TRP   B CH2 1 
ATOM   994  N N   . ASP   B 2 81  ? -18.262 -15.198 -20.889 1.00 51.24  ? 90  ASP   B N   1 
ATOM   995  C CA  . ASP   B 2 81  ? -18.331 -16.676 -21.037 1.00 49.55  ? 90  ASP   B CA  1 
ATOM   996  C C   . ASP   B 2 81  ? -16.909 -17.268 -21.112 1.00 51.77  ? 90  ASP   B C   1 
ATOM   997  O O   . ASP   B 2 81  ? -16.827 -18.497 -21.037 1.00 58.41  ? 90  ASP   B O   1 
ATOM   998  C CB  . ASP   B 2 81  ? -19.211 -17.089 -22.219 1.00 50.13  ? 90  ASP   B CB  1 
ATOM   999  C CG  . ASP   B 2 81  ? -18.631 -16.824 -23.586 1.00 44.05  ? 90  ASP   B CG  1 
ATOM   1000 O OD1 . ASP   B 2 81  ? -17.527 -16.191 -23.698 1.00 52.22  ? 90  ASP   B OD1 1 
ATOM   1001 O OD2 . ASP   B 2 81  ? -19.303 -17.200 -24.582 1.00 62.74  ? 90  ASP   B OD2 1 
ATOM   1002 N N   . GLY   B 2 82  ? -15.853 -16.446 -21.225 1.00 48.24  ? 91  GLY   B N   1 
ATOM   1003 C CA  . GLY   B 2 82  ? -14.437 -16.870 -21.329 1.00 50.96  ? 91  GLY   B CA  1 
ATOM   1004 C C   . GLY   B 2 82  ? -13.956 -17.164 -22.757 1.00 57.24  ? 91  GLY   B C   1 
ATOM   1005 O O   . GLY   B 2 82  ? -12.746 -17.453 -22.911 1.00 49.85  ? 91  GLY   B O   1 
ATOM   1006 N N   . LEU   B 2 83  ? -14.831 -17.076 -23.769 1.00 54.55  ? 92  LEU   B N   1 
ATOM   1007 C CA  . LEU   B 2 83  ? -14.578 -17.492 -25.182 1.00 57.35  ? 92  LEU   B CA  1 
ATOM   1008 C C   . LEU   B 2 83  ? -14.846 -16.339 -26.152 1.00 58.76  ? 92  LEU   B C   1 
ATOM   1009 O O   . LEU   B 2 83  ? -13.957 -16.041 -26.968 1.00 52.51  ? 92  LEU   B O   1 
ATOM   1010 C CB  . LEU   B 2 83  ? -15.516 -18.651 -25.542 1.00 60.57  ? 92  LEU   B CB  1 
ATOM   1011 C CG  . LEU   B 2 83  ? -15.096 -20.043 -25.086 1.00 65.15  ? 92  LEU   B CG  1 
ATOM   1012 C CD1 . LEU   B 2 83  ? -16.128 -21.070 -25.534 1.00 64.25  ? 92  LEU   B CD1 1 
ATOM   1013 C CD2 . LEU   B 2 83  ? -13.698 -20.393 -25.591 1.00 57.96  ? 92  LEU   B CD2 1 
ATOM   1014 N N   . SER   B 2 84  ? -16.063 -15.777 -26.106 1.00 61.69  ? 93  SER   B N   1 
ATOM   1015 C CA  . SER   B 2 84  ? -16.657 -14.923 -27.166 1.00 54.60  ? 93  SER   B CA  1 
ATOM   1016 C C   . SER   B 2 84  ? -16.047 -13.517 -27.136 1.00 54.60  ? 93  SER   B C   1 
ATOM   1017 O O   . SER   B 2 84  ? -15.498 -13.093 -26.100 1.00 51.63  ? 93  SER   B O   1 
ATOM   1018 C CB  . SER   B 2 84  ? -18.145 -14.879 -27.040 1.00 54.85  ? 93  SER   B CB  1 
ATOM   1019 O OG  . SER   B 2 84  ? -18.643 -16.048 -26.392 1.00 54.46  ? 93  SER   B OG  1 
ATOM   1020 N N   . GLU   B 2 85  ? -16.119 -12.814 -28.260 1.00 53.03  ? 94  GLU   B N   1 
ATOM   1021 C CA  . GLU   B 2 85  ? -15.809 -11.366 -28.319 1.00 56.74  ? 94  GLU   B CA  1 
ATOM   1022 C C   . GLU   B 2 85  ? -16.911 -10.627 -27.536 1.00 47.43  ? 94  GLU   B C   1 
ATOM   1023 O O   . GLU   B 2 85  ? -18.003 -11.202 -27.295 1.00 36.56  ? 94  GLU   B O   1 
ATOM   1024 C CB  . GLU   B 2 85  ? -15.665 -10.901 -29.774 1.00 64.14  ? 94  GLU   B CB  1 
ATOM   1025 C CG  . GLU   B 2 85  ? -14.446 -11.503 -30.475 1.00 69.78  ? 94  GLU   B CG  1 
ATOM   1026 C CD  . GLU   B 2 85  ? -13.934 -10.851 -31.753 1.00 71.19  ? 94  GLU   B CD  1 
ATOM   1027 O OE1 . GLU   B 2 85  ? -14.559 -9.882  -32.248 1.00 63.10  ? 94  GLU   B OE1 1 
ATOM   1028 O OE2 . GLU   B 2 85  ? -12.885 -11.311 -32.250 1.00 72.27  ? 94  GLU   B OE2 1 
ATOM   1029 N N   . VAL   B 2 86  ? -16.566 -9.438  -27.070 1.00 46.00  ? 95  VAL   B N   1 
ATOM   1030 C CA  . VAL   B 2 86  ? -17.475 -8.504  -26.342 1.00 44.28  ? 95  VAL   B CA  1 
ATOM   1031 C C   . VAL   B 2 86  ? -17.416 -7.142  -27.036 1.00 48.22  ? 95  VAL   B C   1 
ATOM   1032 O O   . VAL   B 2 86  ? -16.437 -6.920  -27.811 1.00 47.38  ? 95  VAL   B O   1 
ATOM   1033 C CB  . VAL   B 2 86  ? -17.033 -8.355  -24.876 1.00 32.90  ? 95  VAL   B CB  1 
ATOM   1034 C CG1 . VAL   B 2 86  ? -16.874 -9.703  -24.238 1.00 33.51  ? 95  VAL   B CG1 1 
ATOM   1035 C CG2 . VAL   B 2 86  ? -15.739 -7.544  -24.768 1.00 34.86  ? 95  VAL   B CG2 1 
ATOM   1036 N N   . GLN   B 2 87  ? -18.345 -6.245  -26.678 1.00 46.01  ? 96  GLN   B N   1 
ATOM   1037 C CA  . GLN   B 2 87  ? -18.289 -4.811  -27.069 1.00 47.14  ? 96  GLN   B CA  1 
ATOM   1038 C C   . GLN   B 2 87  ? -18.212 -3.908  -25.839 1.00 40.28  ? 96  GLN   B C   1 
ATOM   1039 O O   . GLN   B 2 87  ? -19.011 -4.073  -24.916 1.00 45.12  ? 96  GLN   B O   1 
ATOM   1040 C CB  . GLN   B 2 87  ? -19.493 -4.459  -27.947 1.00 48.79  ? 96  GLN   B CB  1 
ATOM   1041 C CG  . GLN   B 2 87  ? -19.427 -5.191  -29.279 1.00 52.85  ? 96  GLN   B CG  1 
ATOM   1042 C CD  . GLN   B 2 87  ? -20.512 -4.842  -30.270 1.00 58.10  ? 96  GLN   B CD  1 
ATOM   1043 O OE1 . GLN   B 2 87  ? -21.320 -3.928  -30.072 1.00 52.25  ? 96  GLN   B OE1 1 
ATOM   1044 N NE2 . GLN   B 2 87  ? -20.537 -5.597  -31.361 1.00 56.16  ? 96  GLN   B NE2 1 
ATOM   1045 N N   . LEU   B 2 88  ? -17.222 -3.029  -25.855 1.00 38.07  ? 97  LEU   B N   1 
ATOM   1046 C CA  . LEU   B 2 88  ? -17.116 -1.856  -24.978 1.00 44.05  ? 97  LEU   B CA  1 
ATOM   1047 C C   . LEU   B 2 88  ? -17.974 -0.758  -25.600 1.00 47.55  ? 97  LEU   B C   1 
ATOM   1048 O O   . LEU   B 2 88  ? -17.637 -0.307  -26.695 1.00 43.11  ? 97  LEU   B O   1 
ATOM   1049 C CB  . LEU   B 2 88  ? -15.668 -1.374  -24.882 1.00 40.66  ? 97  LEU   B CB  1 
ATOM   1050 C CG  . LEU   B 2 88  ? -15.520 -0.017  -24.231 1.00 41.03  ? 97  LEU   B CG  1 
ATOM   1051 C CD1 . LEU   B 2 88  ? -16.057 -0.065  -22.806 1.00 45.21  ? 97  LEU   B CD1 1 
ATOM   1052 C CD2 . LEU   B 2 88  ? -14.095 0.447   -24.254 1.00 43.03  ? 97  LEU   B CD2 1 
ATOM   1053 N N   . LEU   B 2 89  ? -19.024 -0.337  -24.918 1.00 41.01  ? 98  LEU   B N   1 
ATOM   1054 C CA  . LEU   B 2 89  ? -19.866 0.774   -25.390 1.00 36.18  ? 98  LEU   B CA  1 
ATOM   1055 C C   . LEU   B 2 89  ? -19.207 1.986   -24.776 1.00 38.62  ? 98  LEU   B C   1 
ATOM   1056 O O   . LEU   B 2 89  ? -19.669 2.458   -23.681 1.00 43.66  ? 98  LEU   B O   1 
ATOM   1057 C CB  . LEU   B 2 89  ? -21.309 0.473   -24.965 1.00 39.61  ? 98  LEU   B CB  1 
ATOM   1058 C CG  . LEU   B 2 89  ? -22.384 1.559   -25.166 1.00 44.35  ? 98  LEU   B CG  1 
ATOM   1059 C CD1 . LEU   B 2 89  ? -22.079 2.492   -26.305 1.00 49.47  ? 98  LEU   B CD1 1 
ATOM   1060 C CD2 . LEU   B 2 89  ? -23.745 0.914   -25.375 1.00 46.39  ? 98  LEU   B CD2 1 
ATOM   1061 N N   . ALA   B 2 90  ? -18.081 2.377   -25.384 1.00 35.82  ? 99  ALA   B N   1 
ATOM   1062 C CA  . ALA   B 2 90  ? -17.303 3.537   -24.932 1.00 37.54  ? 99  ALA   B CA  1 
ATOM   1063 C C   . ALA   B 2 90  ? -18.151 4.794   -25.086 1.00 40.88  ? 99  ALA   B C   1 
ATOM   1064 O O   . ALA   B 2 90  ? -18.778 4.938   -26.142 1.00 43.30  ? 99  ALA   B O   1 
ATOM   1065 C CB  . ALA   B 2 90  ? -16.038 3.698   -25.708 1.00 37.87  ? 99  ALA   B CB  1 
ATOM   1066 N N   . VAL   B 2 91  ? -18.128 5.644   -24.057 1.00 46.53  ? 100 VAL   B N   1 
ATOM   1067 C CA  . VAL   B 2 91  ? -18.742 6.995   -24.050 1.00 39.28  ? 100 VAL   B CA  1 
ATOM   1068 C C   . VAL   B 2 91  ? -17.671 7.998   -23.646 1.00 39.55  ? 100 VAL   B C   1 
ATOM   1069 O O   . VAL   B 2 91  ? -17.660 8.452   -22.533 1.00 40.39  ? 100 VAL   B O   1 
ATOM   1070 C CB  . VAL   B 2 91  ? -19.978 7.026   -23.153 1.00 43.45  ? 100 VAL   B CB  1 
ATOM   1071 C CG1 . VAL   B 2 91  ? -20.689 8.376   -23.214 1.00 51.17  ? 100 VAL   B CG1 1 
ATOM   1072 C CG2 . VAL   B 2 91  ? -20.938 5.894   -23.511 1.00 41.07  ? 100 VAL   B CG2 1 
ATOM   1073 N N   . PRO   B 2 92  ? -16.807 8.457   -24.587 1.00 39.52  ? 101 PRO   B N   1 
ATOM   1074 C CA  . PRO   B 2 92  ? -15.739 9.409   -24.252 1.00 39.68  ? 101 PRO   B CA  1 
ATOM   1075 C C   . PRO   B 2 92  ? -16.249 10.823  -24.036 1.00 40.17  ? 101 PRO   B C   1 
ATOM   1076 O O   . PRO   B 2 92  ? -17.277 11.202  -24.584 1.00 43.39  ? 101 PRO   B O   1 
ATOM   1077 C CB  . PRO   B 2 92  ? -14.810 9.394   -25.477 1.00 46.54  ? 101 PRO   B CB  1 
ATOM   1078 C CG  . PRO   B 2 92  ? -15.319 8.262   -26.361 1.00 45.01  ? 101 PRO   B CG  1 
ATOM   1079 C CD  . PRO   B 2 92  ? -16.766 8.023   -25.990 1.00 44.54  ? 101 PRO   B CD  1 
ATOM   1080 N N   . PRO   B 2 93  ? -15.534 11.680  -23.291 1.00 39.93  ? 102 PRO   B N   1 
ATOM   1081 C CA  . PRO   B 2 93  ? -15.978 13.057  -23.088 1.00 48.67  ? 102 PRO   B CA  1 
ATOM   1082 C C   . PRO   B 2 93  ? -16.125 13.785  -24.431 1.00 49.19  ? 102 PRO   B C   1 
ATOM   1083 O O   . PRO   B 2 93  ? -15.286 13.626  -25.290 1.00 52.09  ? 102 PRO   B O   1 
ATOM   1084 C CB  . PRO   B 2 93  ? -14.883 13.641  -22.194 1.00 46.29  ? 102 PRO   B CB  1 
ATOM   1085 C CG  . PRO   B 2 93  ? -14.364 12.432  -21.472 1.00 45.55  ? 102 PRO   B CG  1 
ATOM   1086 C CD  . PRO   B 2 93  ? -14.290 11.402  -22.577 1.00 43.14  ? 102 PRO   B CD  1 
ATOM   1087 N N   . GLY   B 2 94  ? -17.231 14.510  -24.587 1.00 54.38  ? 103 GLY   B N   1 
ATOM   1088 C CA  . GLY   B 2 94  ? -17.557 15.286  -25.797 1.00 52.01  ? 103 GLY   B CA  1 
ATOM   1089 C C   . GLY   B 2 94  ? -17.838 14.452  -27.043 1.00 48.57  ? 103 GLY   B C   1 
ATOM   1090 O O   . GLY   B 2 94  ? -17.968 15.048  -28.090 1.00 56.81  ? 103 GLY   B O   1 
ATOM   1091 N N   . GLU   B 2 95  ? -17.935 13.125  -26.982 1.00 45.77  ? 104 GLU   B N   1 
ATOM   1092 C CA  . GLU   B 2 95  ? -17.981 12.302  -28.217 1.00 44.92  ? 104 GLU   B CA  1 
ATOM   1093 C C   . GLU   B 2 95  ? -19.160 11.340  -28.086 1.00 48.14  ? 104 GLU   B C   1 
ATOM   1094 O O   . GLU   B 2 95  ? -19.525 11.008  -26.948 1.00 48.29  ? 104 GLU   B O   1 
ATOM   1095 C CB  . GLU   B 2 95  ? -16.626 11.609  -28.447 1.00 46.08  ? 104 GLU   B CB  1 
ATOM   1096 C CG  . GLU   B 2 95  ? -15.427 12.583  -28.508 1.00 49.68  ? 104 GLU   B CG  1 
ATOM   1097 C CD  . GLU   B 2 95  ? -14.069 11.898  -28.678 1.00 58.46  ? 104 GLU   B CD  1 
ATOM   1098 O OE1 . GLU   B 2 95  ? -14.076 10.669  -28.642 1.00 51.65  ? 104 GLU   B OE1 1 
ATOM   1099 O OE2 . GLU   B 2 95  ? -12.994 12.581  -28.811 1.00 56.32  ? 104 GLU   B OE2 1 
ATOM   1100 N N   . ARG   B 2 96  ? -19.793 10.994  -29.196 1.00 44.82  ? 105 ARG   B N   1 
ATOM   1101 C CA  . ARG   B 2 96  ? -20.976 10.101  -29.217 1.00 51.35  ? 105 ARG   B CA  1 
ATOM   1102 C C   . ARG   B 2 96  ? -20.586 8.719   -28.695 1.00 47.53  ? 105 ARG   B C   1 
ATOM   1103 O O   . ARG   B 2 96  ? -19.423 8.306   -28.884 1.00 47.73  ? 105 ARG   B O   1 
ATOM   1104 C CB  . ARG   B 2 96  ? -21.524 10.016  -30.643 1.00 58.41  ? 105 ARG   B CB  1 
ATOM   1105 C CG  . ARG   B 2 96  ? -22.811 9.216   -30.779 1.00 69.11  ? 105 ARG   B CG  1 
ATOM   1106 C CD  . ARG   B 2 96  ? -23.645 9.539   -32.017 1.00 78.71  ? 105 ARG   B CD  1 
ATOM   1107 N NE  . ARG   B 2 96  ? -22.875 9.619   -33.252 1.00 75.21  ? 105 ARG   B NE  1 
ATOM   1108 C CZ  . ARG   B 2 96  ? -22.346 10.732  -33.768 1.00 83.63  ? 105 ARG   B CZ  1 
ATOM   1109 N NH1 . ARG   B 2 96  ? -22.504 11.911  -33.186 1.00 80.36  ? 105 ARG   B NH1 1 
ATOM   1110 N NH2 . ARG   B 2 96  ? -21.663 10.664  -34.899 1.00 86.53  ? 105 ARG   B NH2 1 
ATOM   1111 N N   . ALA   B 2 97  ? -21.542 8.046   -28.058 1.00 44.47  ? 106 ALA   B N   1 
ATOM   1112 C CA  . ALA   B 2 97  ? -21.465 6.625   -27.687 1.00 47.80  ? 106 ALA   B CA  1 
ATOM   1113 C C   . ALA   B 2 97  ? -21.008 5.843   -28.928 1.00 49.90  ? 106 ALA   B C   1 
ATOM   1114 O O   . ALA   B 2 97  ? -21.514 6.096   -30.039 1.00 49.44  ? 106 ALA   B O   1 
ATOM   1115 C CB  . ALA   B 2 97  ? -22.805 6.169   -27.182 1.00 49.79  ? 106 ALA   B CB  1 
ATOM   1116 N N   . LYS   B 2 98  ? -20.081 4.913   -28.751 1.00 52.94  ? 107 LYS   B N   1 
ATOM   1117 C CA  . LYS   B 2 98  ? -19.467 4.114   -29.845 1.00 55.35  ? 107 LYS   B CA  1 
ATOM   1118 C C   . LYS   B 2 98  ? -19.155 2.702   -29.326 1.00 48.71  ? 107 LYS   B C   1 
ATOM   1119 O O   . LYS   B 2 98  ? -18.386 2.633   -28.338 1.00 46.11  ? 107 LYS   B O   1 
ATOM   1120 C CB  . LYS   B 2 98  ? -18.211 4.885   -30.263 1.00 65.36  ? 107 LYS   B CB  1 
ATOM   1121 C CG  . LYS   B 2 98  ? -17.195 4.130   -31.110 1.00 80.39  ? 107 LYS   B CG  1 
ATOM   1122 C CD  . LYS   B 2 98  ? -15.895 4.908   -31.320 1.00 90.09  ? 107 LYS   B CD  1 
ATOM   1123 C CE  . LYS   B 2 98  ? -15.152 5.203   -30.029 1.00 88.28  ? 107 LYS   B CE  1 
ATOM   1124 N NZ  . LYS   B 2 98  ? -14.334 6.438   -30.127 1.00 94.94  ? 107 LYS   B NZ  1 
ATOM   1125 N N   . ASN   B 2 99  ? -19.745 1.652   -29.924 1.00 44.49  ? 108 ASN   B N   1 
ATOM   1126 C CA  . ASN   B 2 99  ? -19.405 0.224   -29.644 1.00 52.47  ? 108 ASN   B CA  1 
ATOM   1127 C C   . ASN   B 2 99  ? -18.046 -0.136  -30.256 1.00 54.87  ? 108 ASN   B C   1 
ATOM   1128 O O   . ASN   B 2 99  ? -17.858 0.133   -31.442 1.00 53.26  ? 108 ASN   B O   1 
ATOM   1129 C CB  . ASN   B 2 99  ? -20.433 -0.795  -30.150 1.00 47.70  ? 108 ASN   B CB  1 
ATOM   1130 C CG  . ASN   B 2 99  ? -21.821 -0.517  -29.635 1.00 54.75  ? 108 ASN   B CG  1 
ATOM   1131 O OD1 . ASN   B 2 99  ? -22.343 0.565   -29.892 1.00 67.00  ? 108 ASN   B OD1 1 
ATOM   1132 N ND2 . ASN   B 2 99  ? -22.427 -1.453  -28.916 1.00 53.72  ? 108 ASN   B ND2 1 
ATOM   1133 N N   . ILE   B 2 100 ? -17.148 -0.755  -29.483 1.00 53.89  ? 109 ILE   B N   1 
ATOM   1134 C CA  . ILE   B 2 100 ? -15.832 -1.303  -29.938 1.00 48.15  ? 109 ILE   B CA  1 
ATOM   1135 C C   . ILE   B 2 100 ? -15.804 -2.794  -29.592 1.00 54.26  ? 109 ILE   B C   1 
ATOM   1136 O O   . ILE   B 2 100 ? -15.936 -3.124  -28.384 1.00 51.80  ? 109 ILE   B O   1 
ATOM   1137 C CB  . ILE   B 2 100 ? -14.681 -0.545  -29.282 1.00 53.34  ? 109 ILE   B CB  1 
ATOM   1138 C CG1 . ILE   B 2 100 ? -14.916 0.962   -29.320 1.00 60.02  ? 109 ILE   B CG1 1 
ATOM   1139 C CG2 . ILE   B 2 100 ? -13.355 -0.925  -29.915 1.00 57.45  ? 109 ILE   B CG2 1 
ATOM   1140 C CD1 . ILE   B 2 100 ? -14.590 1.588   -30.643 1.00 64.04  ? 109 ILE   B CD1 1 
ATOM   1141 N N   . GLN   B 2 101 ? -15.721 -3.668  -30.597 1.00 49.45  ? 110 GLN   B N   1 
ATOM   1142 C CA  . GLN   B 2 101 ? -15.775 -5.146  -30.434 1.00 48.65  ? 110 GLN   B CA  1 
ATOM   1143 C C   . GLN   B 2 101 ? -14.337 -5.630  -30.185 1.00 52.90  ? 110 GLN   B C   1 
ATOM   1144 O O   . GLN   B 2 101 ? -13.426 -5.096  -30.829 1.00 50.24  ? 110 GLN   B O   1 
ATOM   1145 C CB  . GLN   B 2 101 ? -16.461 -5.797  -31.629 1.00 54.32  ? 110 GLN   B CB  1 
ATOM   1146 C CG  . GLN   B 2 101 ? -16.350 -7.312  -31.648 1.00 52.56  ? 110 GLN   B CG  1 
ATOM   1147 C CD  . GLN   B 2 101 ? -17.511 -7.969  -32.348 1.00 56.11  ? 110 GLN   B CD  1 
ATOM   1148 O OE1 . GLN   B 2 101 ? -18.607 -7.429  -32.434 1.00 54.06  ? 110 GLN   B OE1 1 
ATOM   1149 N NE2 . GLN   B 2 101 ? -17.277 -9.144  -32.896 1.00 61.76  ? 110 GLN   B NE2 1 
ATOM   1150 N N   . THR   B 2 102 ? -14.121 -6.486  -29.170 1.00 50.84  ? 111 THR   B N   1 
ATOM   1151 C CA  . THR   B 2 102 ? -12.765 -6.960  -28.793 1.00 46.72  ? 111 THR   B CA  1 
ATOM   1152 C C   . THR   B 2 102 ? -12.911 -8.348  -28.196 1.00 45.49  ? 111 THR   B C   1 
ATOM   1153 O O   . THR   B 2 102 ? -14.041 -8.717  -27.817 1.00 51.42  ? 111 THR   B O   1 
ATOM   1154 C CB  . THR   B 2 102 ? -11.995 -5.941  -27.937 1.00 46.46  ? 111 THR   B CB  1 
ATOM   1155 O OG1 . THR   B 2 102 ? -10.610 -6.319  -27.884 1.00 44.09  ? 111 THR   B OG1 1 
ATOM   1156 C CG2 . THR   B 2 102 ? -12.538 -5.804  -26.528 1.00 51.78  ? 111 THR   B CG2 1 
ATOM   1157 N N   . LEU   B 2 103 ? -11.832 -9.133  -28.261 1.00 46.68  ? 112 LEU   B N   1 
ATOM   1158 C CA  . LEU   B 2 103 ? -11.734 -10.423 -27.526 1.00 45.94  ? 112 LEU   B CA  1 
ATOM   1159 C C   . LEU   B 2 103 ? -10.954 -10.113 -26.261 1.00 42.45  ? 112 LEU   B C   1 
ATOM   1160 O O   . LEU   B 2 103 ? -9.821  -9.603  -26.291 1.00 49.42  ? 112 LEU   B O   1 
ATOM   1161 C CB  . LEU   B 2 103 ? -11.062 -11.547 -28.326 1.00 46.75  ? 112 LEU   B CB  1 
ATOM   1162 C CG  . LEU   B 2 103 ? -10.843 -12.834 -27.526 1.00 46.67  ? 112 LEU   B CG  1 
ATOM   1163 C CD1 . LEU   B 2 103 ? -12.097 -13.673 -27.514 1.00 42.56  ? 112 LEU   B CD1 1 
ATOM   1164 C CD2 . LEU   B 2 103 ? -9.652  -13.626 -28.034 1.00 48.21  ? 112 LEU   B CD2 1 
ATOM   1165 N N   . PRO   B 2 104 ? -11.589 -10.267 -25.091 1.00 40.55  ? 113 PRO   B N   1 
ATOM   1166 C CA  . PRO   B 2 104 ? -10.900 -9.936  -23.848 1.00 46.77  ? 113 PRO   B CA  1 
ATOM   1167 C C   . PRO   B 2 104 ? -9.683  -10.847 -23.632 1.00 47.53  ? 113 PRO   B C   1 
ATOM   1168 O O   . PRO   B 2 104 ? -9.756  -12.022 -23.978 1.00 47.97  ? 113 PRO   B O   1 
ATOM   1169 C CB  . PRO   B 2 104 ? -11.934 -10.231 -22.762 1.00 47.39  ? 113 PRO   B CB  1 
ATOM   1170 C CG  . PRO   B 2 104 ? -13.268 -10.236 -23.490 1.00 47.48  ? 113 PRO   B CG  1 
ATOM   1171 C CD  . PRO   B 2 104 ? -12.967 -10.760 -24.883 1.00 43.46  ? 113 PRO   B CD  1 
ATOM   1172 N N   . GLY   B 2 105 ? -8.639  -10.271 -23.048 1.00 47.09  ? 114 GLY   B N   1 
ATOM   1173 C CA  . GLY   B 2 105 ? -7.570  -10.970 -22.313 1.00 49.71  ? 114 GLY   B CA  1 
ATOM   1174 C C   . GLY   B 2 105 ? -8.010  -11.363 -20.913 1.00 48.81  ? 114 GLY   B C   1 
ATOM   1175 O O   . GLY   B 2 105 ? -9.227  -11.493 -20.681 1.00 46.94  ? 114 GLY   B O   1 
ATOM   1176 N N   . ILE   B 2 106 ? -7.040  -11.635 -20.040 1.00 49.90  ? 115 ILE   B N   1 
ATOM   1177 C CA  . ILE   B 2 106 ? -7.237  -12.278 -18.711 1.00 49.77  ? 115 ILE   B CA  1 
ATOM   1178 C C   . ILE   B 2 106 ? -6.316  -11.614 -17.680 1.00 47.72  ? 115 ILE   B C   1 
ATOM   1179 O O   . ILE   B 2 106 ? -5.097  -11.601 -17.865 1.00 54.89  ? 115 ILE   B O   1 
ATOM   1180 C CB  . ILE   B 2 106 ? -6.939  -13.775 -18.819 1.00 55.72  ? 115 ILE   B CB  1 
ATOM   1181 C CG1 . ILE   B 2 106 ? -7.707  -14.436 -19.965 1.00 61.19  ? 115 ILE   B CG1 1 
ATOM   1182 C CG2 . ILE   B 2 106 ? -7.189  -14.454 -17.496 1.00 65.24  ? 115 ILE   B CG2 1 
ATOM   1183 C CD1 . ILE   B 2 106 ? -8.804  -15.352 -19.539 1.00 61.82  ? 115 ILE   B CD1 1 
ATOM   1184 N N   . PHE   B 2 107 ? -6.880  -11.102 -16.595 1.00 50.08  ? 116 PHE   B N   1 
ATOM   1185 C CA  . PHE   B 2 107 ? -6.135  -10.833 -15.344 1.00 48.55  ? 116 PHE   B CA  1 
ATOM   1186 C C   . PHE   B 2 107 ? -6.115  -12.125 -14.519 1.00 48.41  ? 116 PHE   B C   1 
ATOM   1187 O O   . PHE   B 2 107 ? -7.212  -12.586 -14.133 1.00 47.58  ? 116 PHE   B O   1 
ATOM   1188 C CB  . PHE   B 2 107 ? -6.812  -9.722  -14.544 1.00 50.12  ? 116 PHE   B CB  1 
ATOM   1189 C CG  . PHE   B 2 107 ? -6.541  -8.311  -14.989 1.00 49.85  ? 116 PHE   B CG  1 
ATOM   1190 C CD1 . PHE   B 2 107 ? -5.835  -8.040  -16.153 1.00 48.26  ? 116 PHE   B CD1 1 
ATOM   1191 C CD2 . PHE   B 2 107 ? -7.048  -7.246  -14.245 1.00 51.01  ? 116 PHE   B CD2 1 
ATOM   1192 C CE1 . PHE   B 2 107 ? -5.623  -6.733  -16.560 1.00 50.34  ? 116 PHE   B CE1 1 
ATOM   1193 C CE2 . PHE   B 2 107 ? -6.822  -5.941  -14.642 1.00 49.14  ? 116 PHE   B CE2 1 
ATOM   1194 C CZ  . PHE   B 2 107 ? -6.113  -5.686  -15.804 1.00 52.68  ? 116 PHE   B CZ  1 
ATOM   1195 N N   . LYS   B 2 108 ? -4.925  -12.701 -14.324 1.00 52.29  ? 117 LYS   B N   1 
ATOM   1196 C CA  . LYS   B 2 108 ? -4.647  -13.866 -13.434 1.00 56.14  ? 117 LYS   B CA  1 
ATOM   1197 C C   . LYS   B 2 108 ? -4.295  -13.334 -12.028 1.00 48.06  ? 117 LYS   B C   1 
ATOM   1198 O O   . LYS   B 2 108 ? -3.263  -12.670 -11.873 1.00 43.51  ? 117 LYS   B O   1 
ATOM   1199 C CB  . LYS   B 2 108 ? -3.499  -14.717 -14.008 1.00 65.04  ? 117 LYS   B CB  1 
ATOM   1200 C CG  . LYS   B 2 108 ? -3.825  -15.592 -15.221 1.00 73.21  ? 117 LYS   B CG  1 
ATOM   1201 C CD  . LYS   B 2 108 ? -2.616  -16.246 -15.922 1.00 76.24  ? 117 LYS   B CD  1 
ATOM   1202 C CE  . LYS   B 2 108 ? -2.992  -17.415 -16.830 1.00 92.20  ? 117 LYS   B CE  1 
ATOM   1203 N NZ  . LYS   B 2 108 ? -2.124  -17.577 -18.036 1.00 86.38  ? 117 LYS   B NZ  1 
ATOM   1204 N N   . THR   B 2 109 ? -5.142  -13.566 -11.030 1.00 49.67  ? 118 THR   B N   1 
ATOM   1205 C CA  . THR   B 2 109 ? -4.876  -13.162 -9.623  1.00 52.59  ? 118 THR   B CA  1 
ATOM   1206 C C   . THR   B 2 109 ? -4.886  -14.416 -8.742  1.00 52.84  ? 118 THR   B C   1 
ATOM   1207 O O   . THR   B 2 109 ? -5.383  -15.476 -9.170  1.00 53.24  ? 118 THR   B O   1 
ATOM   1208 C CB  . THR   B 2 109 ? -5.893  -12.132 -9.097  1.00 51.04  ? 118 THR   B CB  1 
ATOM   1209 O OG1 . THR   B 2 109 ? -7.093  -12.822 -8.733  1.00 46.40  ? 118 THR   B OG1 1 
ATOM   1210 C CG2 . THR   B 2 109 ? -6.220  -11.053 -10.108 1.00 51.57  ? 118 THR   B CG2 1 
ATOM   1211 N N   . LYS   B 2 110 ? -4.455  -14.248 -7.501  1.00 60.24  ? 119 LYS   B N   1 
ATOM   1212 C CA  . LYS   B 2 110 ? -4.430  -15.322 -6.481  1.00 56.00  ? 119 LYS   B CA  1 
ATOM   1213 C C   . LYS   B 2 110 ? -5.872  -15.742 -6.157  1.00 63.31  ? 119 LYS   B C   1 
ATOM   1214 O O   . LYS   B 2 110 ? -6.051  -16.879 -5.679  1.00 62.55  ? 119 LYS   B O   1 
ATOM   1215 C CB  . LYS   B 2 110 ? -3.612  -14.833 -5.280  1.00 62.50  ? 119 LYS   B CB  1 
ATOM   1216 C CG  . LYS   B 2 110 ? -4.300  -13.835 -4.360  1.00 63.35  ? 119 LYS   B CG  1 
ATOM   1217 C CD  . LYS   B 2 110 ? -3.340  -12.826 -3.775  1.00 66.82  ? 119 LYS   B CD  1 
ATOM   1218 C CE  . LYS   B 2 110 ? -3.601  -12.492 -2.321  1.00 69.26  ? 119 LYS   B CE  1 
ATOM   1219 N NZ  . LYS   B 2 110 ? -5.041  -12.296 -2.032  1.00 62.10  ? 119 LYS   B NZ  1 
ATOM   1220 N N   . ASP   B 2 111 ? -6.874  -14.911 -6.467  1.00 59.82  ? 120 ASP   B N   1 
ATOM   1221 C CA  . ASP   B 2 111 ? -8.288  -15.203 -6.115  1.00 57.93  ? 120 ASP   B CA  1 
ATOM   1222 C C   . ASP   B 2 111 ? -9.062  -15.696 -7.328  1.00 61.14  ? 120 ASP   B C   1 
ATOM   1223 O O   . ASP   B 2 111 ? -10.237 -16.045 -7.156  1.00 72.19  ? 120 ASP   B O   1 
ATOM   1224 C CB  . ASP   B 2 111 ? -8.941  -13.983 -5.474  1.00 62.57  ? 120 ASP   B CB  1 
ATOM   1225 C CG  . ASP   B 2 111 ? -8.403  -13.806 -4.072  1.00 66.55  ? 120 ASP   B CG  1 
ATOM   1226 O OD1 . ASP   B 2 111 ? -8.464  -14.788 -3.313  1.00 71.82  ? 120 ASP   B OD1 1 
ATOM   1227 O OD2 . ASP   B 2 111 ? -7.843  -12.741 -3.789  1.00 68.31  ? 120 ASP   B OD2 1 
ATOM   1228 N N   . GLY   B 2 112 ? -8.420  -15.774 -8.485  1.00 55.23  ? 121 GLY   B N   1 
ATOM   1229 C CA  . GLY   B 2 112 ? -9.110  -16.188 -9.711  1.00 53.41  ? 121 GLY   B CA  1 
ATOM   1230 C C   . GLY   B 2 112 ? -8.715  -15.329 -10.887 1.00 56.32  ? 121 GLY   B C   1 
ATOM   1231 O O   . GLY   B 2 112 ? -7.919  -14.353 -10.729 1.00 54.50  ? 121 GLY   B O   1 
ATOM   1232 N N   . ASP   B 2 113 ? -9.250  -15.718 -12.033 1.00 56.37  ? 122 ASP   B N   1 
ATOM   1233 C CA  . ASP   B 2 113 ? -9.035  -15.079 -13.356 1.00 59.08  ? 122 ASP   B CA  1 
ATOM   1234 C C   . ASP   B 2 113 ? -10.203 -14.125 -13.618 1.00 56.10  ? 122 ASP   B C   1 
ATOM   1235 O O   . ASP   B 2 113 ? -11.357 -14.481 -13.271 1.00 45.50  ? 122 ASP   B O   1 
ATOM   1236 C CB  . ASP   B 2 113 ? -8.940  -16.135 -14.457 1.00 64.24  ? 122 ASP   B CB  1 
ATOM   1237 C CG  . ASP   B 2 113 ? -7.627  -16.905 -14.519 1.00 65.42  ? 122 ASP   B CG  1 
ATOM   1238 O OD1 . ASP   B 2 113 ? -6.657  -16.479 -13.880 1.00 66.58  ? 122 ASP   B OD1 1 
ATOM   1239 O OD2 . ASP   B 2 113 ? -7.584  -17.907 -15.273 1.00 84.68  ? 122 ASP   B OD2 1 
ATOM   1240 N N   . ILE   B 2 114 ? -9.906  -12.966 -14.199 1.00 53.67  ? 123 ILE   B N   1 
ATOM   1241 C CA  . ILE   B 2 114 ? -10.908 -11.932 -14.584 1.00 53.01  ? 123 ILE   B CA  1 
ATOM   1242 C C   . ILE   B 2 114 ? -10.676 -11.568 -16.052 1.00 48.03  ? 123 ILE   B C   1 
ATOM   1243 O O   . ILE   B 2 114 ? -9.508  -11.447 -16.443 1.00 44.40  ? 123 ILE   B O   1 
ATOM   1244 C CB  . ILE   B 2 114 ? -10.795 -10.673 -13.696 1.00 57.08  ? 123 ILE   B CB  1 
ATOM   1245 C CG1 . ILE   B 2 114 ? -10.606 -11.015 -12.219 1.00 62.96  ? 123 ILE   B CG1 1 
ATOM   1246 C CG2 . ILE   B 2 114 ? -11.990 -9.752  -13.909 1.00 55.54  ? 123 ILE   B CG2 1 
ATOM   1247 C CD1 . ILE   B 2 114 ? -9.967  -9.902  -11.424 1.00 67.98  ? 123 ILE   B CD1 1 
ATOM   1248 N N   . GLY   B 2 115 ? -11.758 -11.330 -16.799 1.00 48.30  ? 124 GLY   B N   1 
ATOM   1249 C CA  . GLY   B 2 115 ? -11.714 -10.736 -18.155 1.00 39.56  ? 124 GLY   B CA  1 
ATOM   1250 C C   . GLY   B 2 115 ? -11.024 -9.386  -18.108 1.00 40.35  ? 124 GLY   B C   1 
ATOM   1251 O O   . GLY   B 2 115 ? -11.082 -8.691  -17.064 1.00 38.82  ? 124 GLY   B O   1 
ATOM   1252 N N   . ALA   B 2 116 ? -10.251 -9.074  -19.137 1.00 43.14  ? 125 ALA   B N   1 
ATOM   1253 C CA  . ALA   B 2 116 ? -9.643  -7.746  -19.287 1.00 46.38  ? 125 ALA   B CA  1 
ATOM   1254 C C   . ALA   B 2 116 ? -9.771  -7.330  -20.757 1.00 48.12  ? 125 ALA   B C   1 
ATOM   1255 O O   . ALA   B 2 116 ? -9.690  -8.197  -21.661 1.00 55.03  ? 125 ALA   B O   1 
ATOM   1256 C CB  . ALA   B 2 116 ? -8.237  -7.802  -18.790 1.00 42.17  ? 125 ALA   B CB  1 
ATOM   1257 N N   A VAL   B 2 117 ? -10.001 -6.036  -20.998 0.25 47.85  ? 126 VAL   B N   1 
ATOM   1258 N N   B VAL   B 2 117 ? -9.956  -6.026  -20.977 0.25 48.71  ? 126 VAL   B N   1 
ATOM   1259 N N   C VAL   B 2 117 ? -10.001 -6.036  -20.998 0.25 47.85  ? 126 VAL   B N   1 
ATOM   1260 N N   D VAL   B 2 117 ? -9.956  -6.026  -20.977 0.25 48.71  ? 126 VAL   B N   1 
ATOM   1261 C CA  A VAL   B 2 117 ? -10.098 -5.445  -22.367 0.25 47.34  ? 126 VAL   B CA  1 
ATOM   1262 C CA  B VAL   B 2 117 ? -10.110 -5.389  -22.317 0.25 48.76  ? 126 VAL   B CA  1 
ATOM   1263 C CA  C VAL   B 2 117 ? -10.098 -5.445  -22.367 0.25 47.34  ? 126 VAL   B CA  1 
ATOM   1264 C CA  D VAL   B 2 117 ? -10.110 -5.389  -22.317 0.25 48.76  ? 126 VAL   B CA  1 
ATOM   1265 C C   A VAL   B 2 117 ? -8.957  -4.439  -22.550 0.25 48.36  ? 126 VAL   B C   1 
ATOM   1266 C C   B VAL   B 2 117 ? -8.940  -4.423  -22.537 0.25 49.15  ? 126 VAL   B C   1 
ATOM   1267 C C   C VAL   B 2 117 ? -8.957  -4.439  -22.550 0.25 48.36  ? 126 VAL   B C   1 
ATOM   1268 C C   D VAL   B 2 117 ? -8.940  -4.423  -22.537 0.25 49.15  ? 126 VAL   B C   1 
ATOM   1269 O O   A VAL   B 2 117 ? -8.796  -3.559  -21.679 0.25 48.11  ? 126 VAL   B O   1 
ATOM   1270 O O   B VAL   B 2 117 ? -8.739  -3.542  -21.674 0.25 48.45  ? 126 VAL   B O   1 
ATOM   1271 O O   C VAL   B 2 117 ? -8.796  -3.559  -21.679 0.25 48.11  ? 126 VAL   B O   1 
ATOM   1272 O O   D VAL   B 2 117 ? -8.739  -3.542  -21.674 0.25 48.45  ? 126 VAL   B O   1 
ATOM   1273 C CB  A VAL   B 2 117 ? -11.475 -4.804  -22.603 0.25 47.43  ? 126 VAL   B CB  1 
ATOM   1274 C CB  B VAL   B 2 117 ? -11.467 -4.672  -22.407 0.25 50.12  ? 126 VAL   B CB  1 
ATOM   1275 C CB  C VAL   B 2 117 ? -11.475 -4.804  -22.603 0.25 47.43  ? 126 VAL   B CB  1 
ATOM   1276 C CB  D VAL   B 2 117 ? -11.467 -4.672  -22.407 0.25 50.12  ? 126 VAL   B CB  1 
ATOM   1277 C CG1 A VAL   B 2 117 ? -12.576 -5.852  -22.566 0.25 47.65  ? 126 VAL   B CG1 1 
ATOM   1278 C CG1 B VAL   B 2 117 ? -11.404 -3.458  -23.315 0.25 51.29  ? 126 VAL   B CG1 1 
ATOM   1279 C CG1 C VAL   B 2 117 ? -12.576 -5.852  -22.566 0.25 47.65  ? 126 VAL   B CG1 1 
ATOM   1280 C CG1 D VAL   B 2 117 ? -11.404 -3.458  -23.315 0.25 51.29  ? 126 VAL   B CG1 1 
ATOM   1281 C CG2 A VAL   B 2 117 ? -11.755 -3.683  -21.615 0.25 47.36  ? 126 VAL   B CG2 1 
ATOM   1282 C CG2 B VAL   B 2 117 ? -12.569 -5.627  -22.836 0.25 50.51  ? 126 VAL   B CG2 1 
ATOM   1283 C CG2 C VAL   B 2 117 ? -11.755 -3.683  -21.615 0.25 47.36  ? 126 VAL   B CG2 1 
ATOM   1284 C CG2 D VAL   B 2 117 ? -12.569 -5.627  -22.836 0.25 50.51  ? 126 VAL   B CG2 1 
ATOM   1285 N N   . ALA   B 2 118 ? -8.174  -4.601  -23.622 1.00 47.56  ? 127 ALA   B N   1 
ATOM   1286 C CA  . ALA   B 2 118 ? -7.015  -3.730  -23.930 1.00 50.41  ? 127 ALA   B CA  1 
ATOM   1287 C C   . ALA   B 2 118 ? -7.489  -2.658  -24.916 1.00 62.38  ? 127 ALA   B C   1 
ATOM   1288 O O   . ALA   B 2 118 ? -7.278  -2.809  -26.136 1.00 62.52  ? 127 ALA   B O   1 
ATOM   1289 C CB  . ALA   B 2 118 ? -5.857  -4.547  -24.461 1.00 56.24  ? 127 ALA   B CB  1 
ATOM   1290 N N   . LEU   B 2 119 ? -8.202  -1.662  -24.397 1.00 53.79  ? 128 LEU   B N   1 
ATOM   1291 C CA  . LEU   B 2 119 ? -8.681  -0.481  -25.148 1.00 49.03  ? 128 LEU   B CA  1 
ATOM   1292 C C   . LEU   B 2 119 ? -8.295  0.726   -24.303 1.00 51.89  ? 128 LEU   B C   1 
ATOM   1293 O O   . LEU   B 2 119 ? -8.432  0.631   -23.066 1.00 54.32  ? 128 LEU   B O   1 
ATOM   1294 C CB  . LEU   B 2 119 ? -10.193 -0.616  -25.356 1.00 52.52  ? 128 LEU   B CB  1 
ATOM   1295 C CG  . LEU   B 2 119 ? -10.616 -1.823  -26.196 1.00 48.26  ? 128 LEU   B CG  1 
ATOM   1296 C CD1 . LEU   B 2 119 ? -12.115 -2.084  -26.127 1.00 46.54  ? 128 LEU   B CD1 1 
ATOM   1297 C CD2 . LEU   B 2 119 ? -10.188 -1.640  -27.645 1.00 56.39  ? 128 LEU   B CD2 1 
ATOM   1298 N N   . ASP   B 2 120 ? -7.736  1.763   -24.921 1.00 46.46  ? 129 ASP   B N   1 
ATOM   1299 C CA  . ASP   B 2 120 ? -7.312  2.976   -24.199 1.00 56.58  ? 129 ASP   B CA  1 
ATOM   1300 C C   . ASP   B 2 120 ? -8.346  4.058   -24.488 1.00 59.54  ? 129 ASP   B C   1 
ATOM   1301 O O   . ASP   B 2 120 ? -8.678  4.250   -25.654 1.00 63.25  ? 129 ASP   B O   1 
ATOM   1302 C CB  . ASP   B 2 120 ? -5.883  3.358   -24.564 1.00 60.05  ? 129 ASP   B CB  1 
ATOM   1303 C CG  . ASP   B 2 120 ? -5.225  4.229   -23.502 1.00 64.15  ? 129 ASP   B CG  1 
ATOM   1304 O OD1 . ASP   B 2 120 ? -5.949  5.021   -22.840 1.00 70.79  ? 129 ASP   B OD1 1 
ATOM   1305 O OD2 . ASP   B 2 120 ? -4.003  4.120   -23.347 1.00 65.21  ? 129 ASP   B OD2 1 
ATOM   1306 N N   . TYR   B 2 121 ? -8.881  4.705   -23.461 1.00 52.37  ? 130 TYR   B N   1 
ATOM   1307 C CA  . TYR   B 2 121 ? -9.765  5.879   -23.649 1.00 51.49  ? 130 TYR   B CA  1 
ATOM   1308 C C   . TYR   B 2 121 ? -9.465  6.878   -22.550 1.00 49.20  ? 130 TYR   B C   1 
ATOM   1309 O O   . TYR   B 2 121 ? -8.757  6.562   -21.588 1.00 47.91  ? 130 TYR   B O   1 
ATOM   1310 C CB  . TYR   B 2 121 ? -11.224 5.441   -23.689 1.00 50.00  ? 130 TYR   B CB  1 
ATOM   1311 C CG  . TYR   B 2 121 ? -11.658 4.770   -24.964 1.00 57.61  ? 130 TYR   B CG  1 
ATOM   1312 C CD1 . TYR   B 2 121 ? -11.999 5.518   -26.079 1.00 60.73  ? 130 TYR   B CD1 1 
ATOM   1313 C CD2 . TYR   B 2 121 ? -11.757 3.390   -25.062 1.00 60.88  ? 130 TYR   B CD2 1 
ATOM   1314 C CE1 . TYR   B 2 121 ? -12.411 4.917   -27.262 1.00 59.25  ? 130 TYR   B CE1 1 
ATOM   1315 C CE2 . TYR   B 2 121 ? -12.169 2.774   -26.236 1.00 63.43  ? 130 TYR   B CE2 1 
ATOM   1316 C CZ  . TYR   B 2 121 ? -12.484 3.539   -27.345 1.00 61.19  ? 130 TYR   B CZ  1 
ATOM   1317 O OH  . TYR   B 2 121 ? -12.894 2.957   -28.506 1.00 73.63  ? 130 TYR   B OH  1 
ATOM   1318 N N   . PRO   B 2 122 ? -9.958  8.131   -22.646 1.00 47.31  ? 131 PRO   B N   1 
ATOM   1319 C CA  . PRO   B 2 122 ? -9.662  9.100   -21.595 1.00 51.12  ? 131 PRO   B CA  1 
ATOM   1320 C C   . PRO   B 2 122 ? -10.273 8.631   -20.256 1.00 47.02  ? 131 PRO   B C   1 
ATOM   1321 O O   . PRO   B 2 122 ? -11.184 7.817   -20.265 1.00 47.54  ? 131 PRO   B O   1 
ATOM   1322 C CB  . PRO   B 2 122 ? -10.229 10.412  -22.178 1.00 54.00  ? 131 PRO   B CB  1 
ATOM   1323 C CG  . PRO   B 2 122 ? -10.250 10.180  -23.675 1.00 48.84  ? 131 PRO   B CG  1 
ATOM   1324 C CD  . PRO   B 2 122 ? -10.660 8.726   -23.803 1.00 51.81  ? 131 PRO   B CD  1 
ATOM   1325 N N   . ALA   B 2 123 ? -9.712  9.115   -19.151 1.00 48.80  ? 132 ALA   B N   1 
ATOM   1326 C CA  . ALA   B 2 123 ? -10.094 8.794   -17.756 1.00 49.86  ? 132 ALA   B CA  1 
ATOM   1327 C C   . ALA   B 2 123 ? -11.618 8.892   -17.597 1.00 56.07  ? 132 ALA   B C   1 
ATOM   1328 O O   . ALA   B 2 123 ? -12.254 7.973   -16.955 1.00 45.75  ? 132 ALA   B O   1 
ATOM   1329 C CB  . ALA   B 2 123 ? -9.375  9.729   -16.820 1.00 58.10  ? 132 ALA   B CB  1 
ATOM   1330 N N   . GLY   B 2 124 ? -12.193 9.932   -18.207 1.00 47.03  ? 133 GLY   B N   1 
ATOM   1331 C CA  . GLY   B 2 124 ? -13.625 10.263  -18.089 1.00 40.25  ? 133 GLY   B CA  1 
ATOM   1332 C C   . GLY   B 2 124 ? -14.498 9.200   -18.717 1.00 42.65  ? 133 GLY   B C   1 
ATOM   1333 O O   . GLY   B 2 124 ? -15.741 9.335   -18.632 1.00 42.05  ? 133 GLY   B O   1 
ATOM   1334 N N   . THR   B 2 125 ? -13.898 8.202   -19.382 1.00 36.72  ? 134 THR   B N   1 
ATOM   1335 C CA  . THR   B 2 125 ? -14.657 7.093   -20.009 1.00 37.44  ? 134 THR   B CA  1 
ATOM   1336 C C   . THR   B 2 125 ? -14.968 5.996   -18.961 1.00 39.25  ? 134 THR   B C   1 
ATOM   1337 O O   . THR   B 2 125 ? -15.791 5.076   -19.274 1.00 39.42  ? 134 THR   B O   1 
ATOM   1338 C CB  . THR   B 2 125 ? -13.898 6.587   -21.253 1.00 42.37  ? 134 THR   B CB  1 
ATOM   1339 O OG1 . THR   B 2 125 ? -13.653 7.709   -22.090 1.00 52.36  ? 134 THR   B OG1 1 
ATOM   1340 C CG2 . THR   B 2 125 ? -14.658 5.593   -22.100 1.00 41.44  ? 134 THR   B CG2 1 
ATOM   1341 N N   . SER   B 2 126 ? -14.378 6.098   -17.763 1.00 44.28  ? 135 SER   B N   1 
ATOM   1342 C CA  . SER   B 2 126 ? -14.549 5.144   -16.629 1.00 42.14  ? 135 SER   B CA  1 
ATOM   1343 C C   . SER   B 2 126 ? -16.031 4.886   -16.357 1.00 41.55  ? 135 SER   B C   1 
ATOM   1344 O O   . SER   B 2 126 ? -16.763 5.861   -16.180 1.00 40.14  ? 135 SER   B O   1 
ATOM   1345 C CB  . SER   B 2 126 ? -13.873 5.667   -15.421 1.00 49.92  ? 135 SER   B CB  1 
ATOM   1346 O OG  . SER   B 2 126 ? -12.478 5.491   -15.525 1.00 46.62  ? 135 SER   B OG  1 
ATOM   1347 N N   . GLY   B 2 127 ? -16.462 3.631   -16.326 1.00 37.21  ? 136 GLY   B N   1 
ATOM   1348 C CA  . GLY   B 2 127 ? -17.867 3.273   -16.041 1.00 38.83  ? 136 GLY   B CA  1 
ATOM   1349 C C   . GLY   B 2 127 ? -18.617 2.853   -17.274 1.00 39.65  ? 136 GLY   B C   1 
ATOM   1350 O O   . GLY   B 2 127 ? -19.742 2.338   -17.141 1.00 44.50  ? 136 GLY   B O   1 
ATOM   1351 N N   . SER   B 2 128 ? -18.038 3.047   -18.458 1.00 39.95  ? 137 SER   B N   1 
ATOM   1352 C CA  . SER   B 2 128 ? -18.635 2.596   -19.751 1.00 38.98  ? 137 SER   B CA  1 
ATOM   1353 C C   . SER   B 2 128 ? -18.870 1.100   -19.695 1.00 36.36  ? 137 SER   B C   1 
ATOM   1354 O O   . SER   B 2 128 ? -17.985 0.367   -19.303 1.00 38.70  ? 137 SER   B O   1 
ATOM   1355 C CB  . SER   B 2 128 ? -17.761 2.971   -20.939 1.00 43.43  ? 137 SER   B CB  1 
ATOM   1356 O OG  . SER   B 2 128 ? -17.868 4.364   -21.216 1.00 37.62  ? 137 SER   B OG  1 
ATOM   1357 N N   . PRO   B 2 129 ? -20.059 0.611   -20.077 1.00 36.27  ? 138 PRO   B N   1 
ATOM   1358 C CA  . PRO   B 2 129 ? -20.366 -0.805  -20.028 1.00 35.65  ? 138 PRO   B CA  1 
ATOM   1359 C C   . PRO   B 2 129 ? -19.744 -1.685  -21.112 1.00 38.54  ? 138 PRO   B C   1 
ATOM   1360 O O   . PRO   B 2 129 ? -19.610 -1.300  -22.300 1.00 37.05  ? 138 PRO   B O   1 
ATOM   1361 C CB  . PRO   B 2 129 ? -21.889 -0.871  -20.213 1.00 38.50  ? 138 PRO   B CB  1 
ATOM   1362 C CG  . PRO   B 2 129 ? -22.211 0.349   -21.023 1.00 36.50  ? 138 PRO   B CG  1 
ATOM   1363 C CD  . PRO   B 2 129 ? -21.197 1.393   -20.586 1.00 39.37  ? 138 PRO   B CD  1 
ATOM   1364 N N   . ILE   B 2 130 ? -19.490 -2.929  -20.704 1.00 42.54  ? 139 ILE   B N   1 
ATOM   1365 C CA  . ILE   B 2 130 ? -18.988 -4.016  -21.582 1.00 37.14  ? 139 ILE   B CA  1 
ATOM   1366 C C   . ILE   B 2 130 ? -20.149 -4.981  -21.728 1.00 36.90  ? 139 ILE   B C   1 
ATOM   1367 O O   . ILE   B 2 130 ? -20.777 -5.223  -20.689 1.00 39.67  ? 139 ILE   B O   1 
ATOM   1368 C CB  . ILE   B 2 130 ? -17.726 -4.644  -20.989 1.00 38.49  ? 139 ILE   B CB  1 
ATOM   1369 C CG1 . ILE   B 2 130 ? -16.625 -3.604  -20.793 1.00 43.87  ? 139 ILE   B CG1 1 
ATOM   1370 C CG2 . ILE   B 2 130 ? -17.218 -5.803  -21.841 1.00 42.92  ? 139 ILE   B CG2 1 
ATOM   1371 C CD1 . ILE   B 2 130 ? -15.576 -4.048  -19.820 1.00 49.88  ? 139 ILE   B CD1 1 
ATOM   1372 N N   . LEU   B 2 131 ? -20.498 -5.359  -22.964 1.00 39.14  ? 140 LEU   B N   1 
ATOM   1373 C CA  . LEU   B 2 131 ? -21.692 -6.193  -23.287 1.00 46.73  ? 140 LEU   B CA  1 
ATOM   1374 C C   . LEU   B 2 131 ? -21.320 -7.514  -23.944 1.00 45.17  ? 140 LEU   B C   1 
ATOM   1375 O O   . LEU   B 2 131 ? -20.337 -7.543  -24.696 1.00 51.83  ? 140 LEU   B O   1 
ATOM   1376 C CB  . LEU   B 2 131 ? -22.594 -5.465  -24.291 1.00 54.28  ? 140 LEU   B CB  1 
ATOM   1377 C CG  . LEU   B 2 131 ? -22.563 -3.949  -24.238 1.00 62.62  ? 140 LEU   B CG  1 
ATOM   1378 C CD1 . LEU   B 2 131 ? -23.436 -3.371  -25.349 1.00 63.72  ? 140 LEU   B CD1 1 
ATOM   1379 C CD2 . LEU   B 2 131 ? -23.034 -3.502  -22.863 1.00 63.93  ? 140 LEU   B CD2 1 
ATOM   1380 N N   . ASP   B 2 132 ? -22.212 -8.484  -23.794 1.00 44.33  ? 141 ASP   B N   1 
ATOM   1381 C CA  . ASP   B 2 132 ? -22.211 -9.784  -24.521 1.00 54.57  ? 141 ASP   B CA  1 
ATOM   1382 C C   . ASP   B 2 132 ? -23.139 -9.681  -25.744 1.00 63.79  ? 141 ASP   B C   1 
ATOM   1383 O O   . ASP   B 2 132 ? -23.761 -8.598  -25.943 1.00 63.82  ? 141 ASP   B O   1 
ATOM   1384 C CB  . ASP   B 2 132 ? -22.591 -10.942 -23.584 1.00 47.99  ? 141 ASP   B CB  1 
ATOM   1385 C CG  . ASP   B 2 132 ? -24.026 -10.971 -23.099 1.00 50.23  ? 141 ASP   B CG  1 
ATOM   1386 O OD1 . ASP   B 2 132 ? -24.842 -10.213 -23.609 1.00 44.71  ? 141 ASP   B OD1 1 
ATOM   1387 O OD2 . ASP   B 2 132 ? -24.301 -11.731 -22.162 1.00 58.03  ? 141 ASP   B OD2 1 
ATOM   1388 N N   . LYS   B 2 133 ? -23.251 -10.768 -26.518 1.00 61.86  ? 142 LYS   B N   1 
ATOM   1389 C CA  . LYS   B 2 133 ? -23.892 -10.771 -27.866 1.00 71.19  ? 142 LYS   B CA  1 
ATOM   1390 C C   . LYS   B 2 133 ? -25.397 -10.586 -27.679 1.00 66.59  ? 142 LYS   B C   1 
ATOM   1391 O O   . LYS   B 2 133 ? -26.049 -10.126 -28.614 1.00 67.21  ? 142 LYS   B O   1 
ATOM   1392 C CB  . LYS   B 2 133 ? -23.559 -12.044 -28.664 1.00 71.16  ? 142 LYS   B CB  1 
ATOM   1393 C CG  . LYS   B 2 133 ? -22.220 -12.008 -29.399 1.00 83.98  ? 142 LYS   B CG  1 
ATOM   1394 C CD  . LYS   B 2 133 ? -21.523 -13.361 -29.600 1.00 84.89  ? 142 LYS   B CD  1 
ATOM   1395 C CE  . LYS   B 2 133 ? -20.118 -13.186 -30.154 1.00 90.11  ? 142 LYS   B CE  1 
ATOM   1396 N NZ  . LYS   B 2 133 ? -19.408 -14.470 -30.379 1.00 90.89  ? 142 LYS   B NZ  1 
ATOM   1397 N N   . CYS   B 2 134 ? -25.907 -10.889 -26.489 1.00 63.75  ? 143 CYS   B N   1 
ATOM   1398 C CA  . CYS   B 2 134 ? -27.334 -10.732 -26.130 1.00 58.54  ? 143 CYS   B CA  1 
ATOM   1399 C C   . CYS   B 2 134 ? -27.595 -9.305  -25.589 1.00 55.08  ? 143 CYS   B C   1 
ATOM   1400 O O   . CYS   B 2 134 ? -28.732 -9.041  -25.193 1.00 53.86  ? 143 CYS   B O   1 
ATOM   1401 C CB  . CYS   B 2 134 ? -27.738 -11.810 -25.129 1.00 68.46  ? 143 CYS   B CB  1 
ATOM   1402 S SG  . CYS   B 2 134 ? -28.255 -13.394 -25.855 1.00 72.13  ? 143 CYS   B SG  1 
ATOM   1403 N N   . GLY   B 2 135 ? -26.612 -8.394  -25.615 1.00 52.02  ? 144 GLY   B N   1 
ATOM   1404 C CA  . GLY   B 2 135 ? -26.729 -7.020  -25.059 1.00 54.97  ? 144 GLY   B CA  1 
ATOM   1405 C C   . GLY   B 2 135 ? -26.720 -6.916  -23.523 1.00 50.54  ? 144 GLY   B C   1 
ATOM   1406 O O   . GLY   B 2 135 ? -26.931 -5.818  -22.992 1.00 47.32  ? 144 GLY   B O   1 
ATOM   1407 N N   . ARG   B 2 136 ? -26.453 -7.988  -22.793 1.00 53.78  ? 145 ARG   B N   1 
ATOM   1408 C CA  . ARG   B 2 136 ? -26.382 -7.954  -21.310 1.00 45.65  ? 145 ARG   B CA  1 
ATOM   1409 C C   . ARG   B 2 136 ? -25.058 -7.338  -20.879 1.00 44.41  ? 145 ARG   B C   1 
ATOM   1410 O O   . ARG   B 2 136 ? -24.043 -7.603  -21.529 1.00 43.82  ? 145 ARG   B O   1 
ATOM   1411 C CB  . ARG   B 2 136 ? -26.595 -9.364  -20.804 1.00 49.98  ? 145 ARG   B CB  1 
ATOM   1412 C CG  . ARG   B 2 136 ? -28.052 -9.777  -20.889 1.00 53.36  ? 145 ARG   B CG  1 
ATOM   1413 C CD  . ARG   B 2 136 ? -28.167 -11.199 -20.436 1.00 55.64  ? 145 ARG   B CD  1 
ATOM   1414 N NE  . ARG   B 2 136 ? -27.348 -11.987 -21.344 1.00 69.99  ? 145 ARG   B NE  1 
ATOM   1415 C CZ  . ARG   B 2 136 ? -26.773 -13.163 -21.080 1.00 76.79  ? 145 ARG   B CZ  1 
ATOM   1416 N NH1 . ARG   B 2 136 ? -26.870 -13.739 -19.885 1.00 74.94  ? 145 ARG   B NH1 1 
ATOM   1417 N NH2 . ARG   B 2 136 ? -26.073 -13.744 -22.041 1.00 78.40  ? 145 ARG   B NH2 1 
ATOM   1418 N N   . VAL   B 2 137 ? -25.079 -6.502  -19.835 1.00 42.46  ? 146 VAL   B N   1 
ATOM   1419 C CA  . VAL   B 2 137 ? -23.866 -5.801  -19.334 1.00 41.05  ? 146 VAL   B CA  1 
ATOM   1420 C C   . VAL   B 2 137 ? -23.135 -6.828  -18.479 1.00 42.51  ? 146 VAL   B C   1 
ATOM   1421 O O   . VAL   B 2 137 ? -23.737 -7.351  -17.508 1.00 45.33  ? 146 VAL   B O   1 
ATOM   1422 C CB  . VAL   B 2 137 ? -24.208 -4.522  -18.547 1.00 40.25  ? 146 VAL   B CB  1 
ATOM   1423 C CG1 . VAL   B 2 137 ? -22.965 -3.810  -18.070 1.00 42.76  ? 146 VAL   B CG1 1 
ATOM   1424 C CG2 . VAL   B 2 137 ? -25.050 -3.585  -19.404 1.00 43.62  ? 146 VAL   B CG2 1 
ATOM   1425 N N   . ILE   B 2 138 ? -21.921 -7.163  -18.889 1.00 40.58  ? 147 ILE   B N   1 
ATOM   1426 C CA  . ILE   B 2 138 ? -21.075 -8.177  -18.195 1.00 41.22  ? 147 ILE   B CA  1 
ATOM   1427 C C   . ILE   B 2 138 ? -20.050 -7.454  -17.313 1.00 40.40  ? 147 ILE   B C   1 
ATOM   1428 O O   . ILE   B 2 138 ? -19.285 -8.135  -16.631 1.00 40.17  ? 147 ILE   B O   1 
ATOM   1429 C CB  . ILE   B 2 138 ? -20.443 -9.139  -19.233 1.00 39.78  ? 147 ILE   B CB  1 
ATOM   1430 C CG1 . ILE   B 2 138 ? -19.723 -8.386  -20.346 1.00 41.30  ? 147 ILE   B CG1 1 
ATOM   1431 C CG2 . ILE   B 2 138 ? -21.482 -10.098 -19.796 1.00 39.93  ? 147 ILE   B CG2 1 
ATOM   1432 C CD1 . ILE   B 2 138 ? -18.567 -9.157  -20.936 1.00 50.47  ? 147 ILE   B CD1 1 
ATOM   1433 N N   . GLY   B 2 139 ? -20.055 -6.114  -17.268 1.00 39.21  ? 148 GLY   B N   1 
ATOM   1434 C CA  . GLY   B 2 139 ? -19.166 -5.369  -16.356 1.00 39.27  ? 148 GLY   B CA  1 
ATOM   1435 C C   . GLY   B 2 139 ? -18.872 -3.976  -16.853 1.00 35.71  ? 148 GLY   B C   1 
ATOM   1436 O O   . GLY   B 2 139 ? -19.396 -3.644  -17.930 1.00 34.27  ? 148 GLY   B O   1 
ATOM   1437 N N   . LEU   B 2 140 ? -18.075 -3.218  -16.107 1.00 35.76  ? 149 LEU   B N   1 
ATOM   1438 C CA  . LEU   B 2 140 ? -17.721 -1.821  -16.433 1.00 39.57  ? 149 LEU   B CA  1 
ATOM   1439 C C   . LEU   B 2 140 ? -16.208 -1.706  -16.650 1.00 39.86  ? 149 LEU   B C   1 
ATOM   1440 O O   . LEU   B 2 140 ? -15.417 -2.465  -16.003 1.00 41.18  ? 149 LEU   B O   1 
ATOM   1441 C CB  . LEU   B 2 140 ? -18.181 -0.892  -15.295 1.00 36.45  ? 149 LEU   B CB  1 
ATOM   1442 C CG  . LEU   B 2 140 ? -19.652 -0.976  -14.867 1.00 41.50  ? 149 LEU   B CG  1 
ATOM   1443 C CD1 . LEU   B 2 140 ? -19.991 0.185   -13.918 1.00 45.52  ? 149 LEU   B CD1 1 
ATOM   1444 C CD2 . LEU   B 2 140 ? -20.623 -1.012  -16.038 1.00 38.03  ? 149 LEU   B CD2 1 
ATOM   1445 N N   . TYR   B 2 141 ? -15.856 -0.705  -17.450 1.00 39.35  ? 150 TYR   B N   1 
ATOM   1446 C CA  . TYR   B 2 141 ? -14.507 -0.350  -17.947 1.00 36.06  ? 150 TYR   B CA  1 
ATOM   1447 C C   . TYR   B 2 141 ? -13.983 0.756   -17.060 1.00 41.37  ? 150 TYR   B C   1 
ATOM   1448 O O   . TYR   B 2 141 ? -14.791 1.650   -16.776 1.00 44.87  ? 150 TYR   B O   1 
ATOM   1449 C CB  . TYR   B 2 141 ? -14.623 0.106   -19.414 1.00 43.80  ? 150 TYR   B CB  1 
ATOM   1450 C CG  . TYR   B 2 141 ? -13.361 0.699   -20.008 1.00 39.48  ? 150 TYR   B CG  1 
ATOM   1451 C CD1 . TYR   B 2 141 ? -13.143 2.068   -19.999 1.00 44.32  ? 150 TYR   B CD1 1 
ATOM   1452 C CD2 . TYR   B 2 141 ? -12.364 -0.107  -20.529 1.00 44.59  ? 150 TYR   B CD2 1 
ATOM   1453 C CE1 . TYR   B 2 141 ? -11.961 2.621   -20.483 1.00 50.78  ? 150 TYR   B CE1 1 
ATOM   1454 C CE2 . TYR   B 2 141 ? -11.200 0.428   -21.065 1.00 41.02  ? 150 TYR   B CE2 1 
ATOM   1455 C CZ  . TYR   B 2 141 ? -10.994 1.799   -21.055 1.00 50.23  ? 150 TYR   B CZ  1 
ATOM   1456 O OH  . TYR   B 2 141 ? -9.840  2.343   -21.569 1.00 47.04  ? 150 TYR   B OH  1 
ATOM   1457 N N   . GLY   B 2 142 ? -12.707 0.756   -16.686 1.00 43.48  ? 151 GLY   B N   1 
ATOM   1458 C CA  . GLY   B 2 142 ? -12.109 1.938   -16.026 1.00 44.79  ? 151 GLY   B CA  1 
ATOM   1459 C C   . GLY   B 2 142 ? -11.244 1.636   -14.813 1.00 45.96  ? 151 GLY   B C   1 
ATOM   1460 O O   . GLY   B 2 142 ? -10.624 2.596   -14.304 1.00 54.35  ? 151 GLY   B O   1 
ATOM   1461 N N   . ASN   B 2 143 ? -11.168 0.375   -14.356 1.00 42.22  ? 152 ASN   B N   1 
ATOM   1462 C CA  . ASN   B 2 143 ? -10.181 -0.038  -13.325 1.00 44.99  ? 152 ASN   B CA  1 
ATOM   1463 C C   . ASN   B 2 143 ? -9.296  -1.155  -13.890 1.00 42.45  ? 152 ASN   B C   1 
ATOM   1464 O O   . ASN   B 2 143 ? -9.799  -2.249  -14.195 1.00 38.47  ? 152 ASN   B O   1 
ATOM   1465 C CB  . ASN   B 2 143 ? -10.834 -0.491  -12.018 1.00 43.84  ? 152 ASN   B CB  1 
ATOM   1466 C CG  . ASN   B 2 143 ? -9.869  -0.532  -10.854 1.00 45.16  ? 152 ASN   B CG  1 
ATOM   1467 O OD1 . ASN   B 2 143 ? -8.940  0.287   -10.745 1.00 41.09  ? 152 ASN   B OD1 1 
ATOM   1468 N ND2 . ASN   B 2 143 ? -10.107 -1.487  -9.966  1.00 44.49  ? 152 ASN   B ND2 1 
ATOM   1469 N N   . GLY   B 2 144 ? -8.008  -0.889  -13.953 1.00 40.58  ? 153 GLY   B N   1 
ATOM   1470 C CA  . GLY   B 2 144 ? -7.050  -1.821  -14.571 1.00 42.27  ? 153 GLY   B CA  1 
ATOM   1471 C C   . GLY   B 2 144 ? -5.631  -1.332  -14.373 1.00 45.16  ? 153 GLY   B C   1 
ATOM   1472 O O   . GLY   B 2 144 ? -5.355  -0.744  -13.321 1.00 52.96  ? 153 GLY   B O   1 
ATOM   1473 N N   . VAL   B 2 145 ? -4.776  -1.498  -15.379 1.00 47.92  ? 154 VAL   B N   1 
ATOM   1474 C CA  . VAL   B 2 145 ? -3.301  -1.471  -15.204 1.00 48.60  ? 154 VAL   B CA  1 
ATOM   1475 C C   . VAL   B 2 145 ? -2.646  -0.942  -16.492 1.00 58.38  ? 154 VAL   B C   1 
ATOM   1476 O O   . VAL   B 2 145 ? -3.232  -1.132  -17.591 1.00 56.23  ? 154 VAL   B O   1 
ATOM   1477 C CB  . VAL   B 2 145 ? -2.865  -2.895  -14.791 1.00 54.18  ? 154 VAL   B CB  1 
ATOM   1478 C CG1 . VAL   B 2 145 ? -2.724  -3.858  -15.965 1.00 48.23  ? 154 VAL   B CG1 1 
ATOM   1479 C CG2 . VAL   B 2 145 ? -1.617  -2.860  -13.948 1.00 60.43  ? 154 VAL   B CG2 1 
ATOM   1480 N N   . VAL   B 2 146 ? -1.513  -0.250  -16.348 1.00 62.34  ? 155 VAL   B N   1 
ATOM   1481 C CA  . VAL   B 2 146 ? -0.649  0.245   -17.463 1.00 69.14  ? 155 VAL   B CA  1 
ATOM   1482 C C   . VAL   B 2 146 ? 0.463   -0.795  -17.688 1.00 71.95  ? 155 VAL   B C   1 
ATOM   1483 O O   . VAL   B 2 146 ? 1.112   -1.178  -16.706 1.00 70.32  ? 155 VAL   B O   1 
ATOM   1484 C CB  . VAL   B 2 146 ? -0.121  1.646   -17.106 1.00 67.37  ? 155 VAL   B CB  1 
ATOM   1485 C CG1 . VAL   B 2 146 ? 0.807   2.192   -18.161 1.00 72.00  ? 155 VAL   B CG1 1 
ATOM   1486 C CG2 . VAL   B 2 146 ? -1.273  2.615   -16.878 1.00 73.22  ? 155 VAL   B CG2 1 
ATOM   1487 N N   A ILE   B 2 147 ? 0.666   -1.232  -18.940 0.25 72.31  ? 156 ILE   B N   1 
ATOM   1488 N N   B ILE   B 2 147 ? 0.666   -1.232  -18.940 0.25 72.31  ? 156 ILE   B N   1 
ATOM   1489 N N   C ILE   B 2 147 ? 0.653   -1.230  -18.941 0.25 72.68  ? 156 ILE   B N   1 
ATOM   1490 N N   D ILE   B 2 147 ? 0.653   -1.230  -18.941 0.25 72.68  ? 156 ILE   B N   1 
ATOM   1491 C CA  A ILE   B 2 147 ? 1.539   -2.394  -19.304 0.25 74.25  ? 156 ILE   B CA  1 
ATOM   1492 C CA  B ILE   B 2 147 ? 1.539   -2.394  -19.304 0.25 74.25  ? 156 ILE   B CA  1 
ATOM   1493 C CA  C ILE   B 2 147 ? 1.606   -2.312  -19.338 0.25 74.88  ? 156 ILE   B CA  1 
ATOM   1494 C CA  D ILE   B 2 147 ? 1.606   -2.312  -19.338 0.25 74.88  ? 156 ILE   B CA  1 
ATOM   1495 C C   A ILE   B 2 147 ? 2.855   -1.891  -19.912 0.25 76.03  ? 156 ILE   B C   1 
ATOM   1496 C C   B ILE   B 2 147 ? 2.855   -1.891  -19.912 0.25 76.03  ? 156 ILE   B C   1 
ATOM   1497 C C   C ILE   B 2 147 ? 2.889   -1.671  -19.879 0.25 76.98  ? 156 ILE   B C   1 
ATOM   1498 C C   D ILE   B 2 147 ? 2.889   -1.671  -19.879 0.25 76.98  ? 156 ILE   B C   1 
ATOM   1499 O O   A ILE   B 2 147 ? 2.965   -0.679  -20.167 0.25 72.77  ? 156 ILE   B O   1 
ATOM   1500 O O   B ILE   B 2 147 ? 2.965   -0.679  -20.167 0.25 72.77  ? 156 ILE   B O   1 
ATOM   1501 O O   C ILE   B 2 147 ? 2.873   -0.456  -20.137 0.25 75.31  ? 156 ILE   B O   1 
ATOM   1502 O O   D ILE   B 2 147 ? 2.873   -0.456  -20.137 0.25 75.31  ? 156 ILE   B O   1 
ATOM   1503 C CB  A ILE   B 2 147 ? 0.802   -3.364  -20.252 0.25 76.49  ? 156 ILE   B CB  1 
ATOM   1504 C CB  B ILE   B 2 147 ? 0.802   -3.364  -20.252 0.25 76.49  ? 156 ILE   B CB  1 
ATOM   1505 C CB  C ILE   B 2 147 ? 0.959   -3.267  -20.365 0.25 77.12  ? 156 ILE   B CB  1 
ATOM   1506 C CB  D ILE   B 2 147 ? 0.959   -3.267  -20.365 0.25 77.12  ? 156 ILE   B CB  1 
ATOM   1507 C CG1 A ILE   B 2 147 ? 0.353   -2.680  -21.547 0.25 77.62  ? 156 ILE   B CG1 1 
ATOM   1508 C CG1 B ILE   B 2 147 ? 0.353   -2.680  -21.547 0.25 77.62  ? 156 ILE   B CG1 1 
ATOM   1509 C CG1 C ILE   B 2 147 ? 0.561   -2.542  -21.655 0.25 77.94  ? 156 ILE   B CG1 1 
ATOM   1510 C CG1 D ILE   B 2 147 ? 0.561   -2.542  -21.655 0.25 77.94  ? 156 ILE   B CG1 1 
ATOM   1511 C CG2 A ILE   B 2 147 ? -0.362  -4.032  -19.535 0.25 76.89  ? 156 ILE   B CG2 1 
ATOM   1512 C CG2 B ILE   B 2 147 ? -0.362  -4.032  -19.535 0.25 76.89  ? 156 ILE   B CG2 1 
ATOM   1513 C CG2 C ILE   B 2 147 ? -0.220  -4.002  -19.746 0.25 77.76  ? 156 ILE   B CG2 1 
ATOM   1514 C CG2 D ILE   B 2 147 ? -0.220  -4.002  -19.746 0.25 77.76  ? 156 ILE   B CG2 1 
ATOM   1515 C CD1 A ILE   B 2 147 ? -0.212  -3.629  -22.582 0.25 73.67  ? 156 ILE   B CD1 1 
ATOM   1516 C CD1 B ILE   B 2 147 ? -0.212  -3.629  -22.582 0.25 73.67  ? 156 ILE   B CD1 1 
ATOM   1517 C CD1 C ILE   B 2 147 ? -0.165  -3.416  -22.655 0.25 73.83  ? 156 ILE   B CD1 1 
ATOM   1518 C CD1 D ILE   B 2 147 ? -0.165  -3.416  -22.655 0.25 73.83  ? 156 ILE   B CD1 1 
ATOM   1519 N N   A LYS   B 2 148 ? 3.814   -2.802  -20.126 0.25 81.86  ? 157 LYS   B N   1 
ATOM   1520 N N   B LYS   B 2 148 ? 3.814   -2.802  -20.126 0.25 81.86  ? 157 LYS   B N   1 
ATOM   1521 N N   C LYS   B 2 148 ? 3.958   -2.460  -20.032 0.25 82.95  ? 157 LYS   B N   1 
ATOM   1522 N N   D LYS   B 2 148 ? 3.958   -2.460  -20.032 0.25 82.95  ? 157 LYS   B N   1 
ATOM   1523 C CA  A LYS   B 2 148 ? 5.174   -2.506  -20.661 0.25 87.66  ? 157 LYS   B CA  1 
ATOM   1524 C CA  B LYS   B 2 148 ? 5.174   -2.506  -20.661 0.25 87.66  ? 157 LYS   B CA  1 
ATOM   1525 C CA  C LYS   B 2 148 ? 5.280   -1.994  -20.536 0.25 88.41  ? 157 LYS   B CA  1 
ATOM   1526 C CA  D LYS   B 2 148 ? 5.280   -1.994  -20.536 0.25 88.41  ? 157 LYS   B CA  1 
ATOM   1527 C C   A LYS   B 2 148 ? 5.082   -1.400  -21.719 0.25 89.42  ? 157 LYS   B C   1 
ATOM   1528 C C   B LYS   B 2 148 ? 5.082   -1.400  -21.719 0.25 89.42  ? 157 LYS   B C   1 
ATOM   1529 C C   C LYS   B 2 148 ? 5.045   -1.003  -21.679 0.25 89.19  ? 157 LYS   B C   1 
ATOM   1530 C C   D LYS   B 2 148 ? 5.045   -1.003  -21.679 0.25 89.19  ? 157 LYS   B C   1 
ATOM   1531 O O   A LYS   B 2 148 ? 5.880   -0.445  -21.644 0.25 93.60  ? 157 LYS   B O   1 
ATOM   1532 O O   B LYS   B 2 148 ? 5.880   -0.445  -21.644 0.25 93.60  ? 157 LYS   B O   1 
ATOM   1533 O O   C LYS   B 2 148 ? 5.528   0.145   -21.589 0.25 88.53  ? 157 LYS   B O   1 
ATOM   1534 O O   D LYS   B 2 148 ? 5.528   0.145   -21.589 0.25 88.53  ? 157 LYS   B O   1 
ATOM   1535 C CB  A LYS   B 2 148 ? 5.807   -3.768  -21.258 0.25 91.74  ? 157 LYS   B CB  1 
ATOM   1536 C CB  B LYS   B 2 148 ? 5.807   -3.768  -21.258 0.25 91.74  ? 157 LYS   B CB  1 
ATOM   1537 C CB  C LYS   B 2 148 ? 6.120   -3.183  -21.010 0.25 92.85  ? 157 LYS   B CB  1 
ATOM   1538 C CB  D LYS   B 2 148 ? 6.120   -3.183  -21.010 0.25 92.85  ? 157 LYS   B CB  1 
ATOM   1539 C CG  A LYS   B 2 148 ? 6.211   -4.840  -20.250 0.25 95.55  ? 157 LYS   B CG  1 
ATOM   1540 C CG  B LYS   B 2 148 ? 6.211   -4.840  -20.250 0.25 95.55  ? 157 LYS   B CG  1 
ATOM   1541 C CG  C LYS   B 2 148 ? 5.535   -4.554  -20.693 0.25 99.82  ? 157 LYS   B CG  1 
ATOM   1542 C CG  D LYS   B 2 148 ? 5.535   -4.554  -20.693 0.25 99.82  ? 157 LYS   B CG  1 
ATOM   1543 C CD  A LYS   B 2 148 ? 6.788   -6.097  -20.883 0.25 98.35  ? 157 LYS   B CD  1 
ATOM   1544 C CD  B LYS   B 2 148 ? 6.788   -6.097  -20.883 0.25 98.35  ? 157 LYS   B CD  1 
ATOM   1545 C CD  C LYS   B 2 148 ? 6.566   -5.561  -20.228 0.25 103.66 ? 157 LYS   B CD  1 
ATOM   1546 C CD  D LYS   B 2 148 ? 6.566   -5.561  -20.228 0.25 103.66 ? 157 LYS   B CD  1 
ATOM   1547 C CE  A LYS   B 2 148 ? 8.177   -5.906  -21.460 0.25 100.71 ? 157 LYS   B CE  1 
ATOM   1548 C CE  B LYS   B 2 148 ? 8.177   -5.906  -21.460 0.25 100.71 ? 157 LYS   B CE  1 
ATOM   1549 C CE  C LYS   B 2 148 ? 7.988   -5.076  -20.421 0.25 108.37 ? 157 LYS   B CE  1 
ATOM   1550 C CE  D LYS   B 2 148 ? 7.988   -5.076  -20.421 0.25 108.37 ? 157 LYS   B CE  1 
ATOM   1551 N NZ  A LYS   B 2 148 ? 9.233   -6.021  -20.424 0.25 101.20 ? 157 LYS   B NZ  1 
ATOM   1552 N NZ  B LYS   B 2 148 ? 9.233   -6.021  -20.424 0.25 101.20 ? 157 LYS   B NZ  1 
ATOM   1553 N NZ  C LYS   B 2 148 ? 8.957   -6.198  -20.452 0.25 109.77 ? 157 LYS   B NZ  1 
ATOM   1554 N NZ  D LYS   B 2 148 ? 8.957   -6.198  -20.452 0.25 109.77 ? 157 LYS   B NZ  1 
ATOM   1555 N N   A ASN   B 2 149 ? 4.132   -1.530  -22.650 0.25 90.93  ? 158 ASN   B N   1 
ATOM   1556 N N   B ASN   B 2 149 ? 4.132   -1.530  -22.650 0.25 90.93  ? 158 ASN   B N   1 
ATOM   1557 N N   C ASN   B 2 149 ? 4.298   -1.439  -22.697 0.25 89.40  ? 158 ASN   B N   1 
ATOM   1558 N N   D ASN   B 2 149 ? 4.298   -1.439  -22.697 0.25 89.40  ? 158 ASN   B N   1 
ATOM   1559 C CA  A ASN   B 2 149 ? 3.943   -0.643  -23.831 0.25 91.66  ? 158 ASN   B CA  1 
ATOM   1560 C CA  B ASN   B 2 149 ? 3.943   -0.643  -23.831 0.25 91.66  ? 158 ASN   B CA  1 
ATOM   1561 C CA  C ASN   B 2 149 ? 3.899   -0.632  -23.882 0.25 90.48  ? 158 ASN   B CA  1 
ATOM   1562 C CA  D ASN   B 2 149 ? 3.899   -0.632  -23.882 0.25 90.48  ? 158 ASN   B CA  1 
ATOM   1563 C C   A ASN   B 2 149 ? 3.689   0.800   -23.378 0.25 92.20  ? 158 ASN   B C   1 
ATOM   1564 C C   B ASN   B 2 149 ? 3.689   0.800   -23.378 0.25 92.20  ? 158 ASN   B C   1 
ATOM   1565 C C   C ASN   B 2 149 ? 3.587   0.805   -23.448 0.25 91.61  ? 158 ASN   B C   1 
ATOM   1566 C C   D ASN   B 2 149 ? 3.587   0.805   -23.448 0.25 91.61  ? 158 ASN   B C   1 
ATOM   1567 O O   A ASN   B 2 149 ? 4.220   1.721   -24.025 0.25 95.55  ? 158 ASN   B O   1 
ATOM   1568 O O   B ASN   B 2 149 ? 4.220   1.721   -24.025 0.25 95.55  ? 158 ASN   B O   1 
ATOM   1569 O O   C ASN   B 2 149 ? 3.963   1.732   -24.189 0.25 94.13  ? 158 ASN   B O   1 
ATOM   1570 O O   D ASN   B 2 149 ? 3.963   1.732   -24.189 0.25 94.13  ? 158 ASN   B O   1 
ATOM   1571 C CB  A ASN   B 2 149 ? 2.794   -1.136  -24.716 0.25 91.20  ? 158 ASN   B CB  1 
ATOM   1572 C CB  B ASN   B 2 149 ? 2.794   -1.136  -24.716 0.25 91.20  ? 158 ASN   B CB  1 
ATOM   1573 C CB  C ASN   B 2 149 ? 2.701   -1.255  -24.607 0.25 89.73  ? 158 ASN   B CB  1 
ATOM   1574 C CB  D ASN   B 2 149 ? 2.701   -1.255  -24.607 0.25 89.73  ? 158 ASN   B CB  1 
ATOM   1575 C CG  A ASN   B 2 149 ? 2.731   -2.647  -24.809 0.25 92.99  ? 158 ASN   B CG  1 
ATOM   1576 C CG  B ASN   B 2 149 ? 2.731   -2.647  -24.809 0.25 92.99  ? 158 ASN   B CG  1 
ATOM   1577 C CG  C ASN   B 2 149 ? 2.767   -2.768  -24.667 0.25 90.54  ? 158 ASN   B CG  1 
ATOM   1578 C CG  D ASN   B 2 149 ? 2.767   -2.768  -24.667 0.25 90.54  ? 158 ASN   B CG  1 
ATOM   1579 O OD1 A ASN   B 2 149 ? 3.712   -3.334  -24.534 0.25 95.08  ? 158 ASN   B OD1 1 
ATOM   1580 O OD1 B ASN   B 2 149 ? 3.712   -3.334  -24.534 0.25 95.08  ? 158 ASN   B OD1 1 
ATOM   1581 O OD1 C ASN   B 2 149 ? 3.666   -3.380  -24.093 0.25 92.09  ? 158 ASN   B OD1 1 
ATOM   1582 O OD1 D ASN   B 2 149 ? 3.666   -3.380  -24.093 0.25 92.09  ? 158 ASN   B OD1 1 
ATOM   1583 N ND2 A ASN   B 2 149 ? 1.580   -3.176  -25.192 0.25 93.17  ? 158 ASN   B ND2 1 
ATOM   1584 N ND2 B ASN   B 2 149 ? 1.580   -3.176  -25.192 0.25 93.17  ? 158 ASN   B ND2 1 
ATOM   1585 N ND2 C ASN   B 2 149 ? 1.818   -3.383  -25.354 0.25 89.89  ? 158 ASN   B ND2 1 
ATOM   1586 N ND2 D ASN   B 2 149 ? 1.818   -3.383  -25.354 0.25 89.89  ? 158 ASN   B ND2 1 
ATOM   1587 N N   . GLY   B 2 150 ? 2.911   0.977   -22.306 1.00 94.57  ? 159 GLY   B N   1 
ATOM   1588 C CA  . GLY   B 2 150 ? 2.409   2.289   -21.847 1.00 84.86  ? 159 GLY   B CA  1 
ATOM   1589 C C   . GLY   B 2 150 ? 0.901   2.369   -22.049 1.00 76.07  ? 159 GLY   B C   1 
ATOM   1590 O O   . GLY   B 2 150 ? 0.265   3.355   -21.593 1.00 69.87  ? 159 GLY   B O   1 
ATOM   1591 N N   A SER   B 2 151 ? 0.324   1.366   -22.722 0.25 76.92  ? 160 SER   B N   1 
ATOM   1592 N N   B SER   B 2 151 ? 0.345   1.346   -22.711 0.25 74.23  ? 160 SER   B N   1 
ATOM   1593 N N   C SER   B 2 151 ? 0.324   1.366   -22.722 0.25 76.92  ? 160 SER   B N   1 
ATOM   1594 N N   D SER   B 2 151 ? 0.345   1.346   -22.711 0.25 74.23  ? 160 SER   B N   1 
ATOM   1595 C CA  A SER   B 2 151 ? -1.129  1.281   -23.027 0.25 73.90  ? 160 SER   B CA  1 
ATOM   1596 C CA  B SER   B 2 151 ? -1.097  1.165   -23.028 0.25 70.12  ? 160 SER   B CA  1 
ATOM   1597 C CA  C SER   B 2 151 ? -1.129  1.281   -23.027 0.25 73.90  ? 160 SER   B CA  1 
ATOM   1598 C CA  D SER   B 2 151 ? -1.097  1.165   -23.028 0.25 70.12  ? 160 SER   B CA  1 
ATOM   1599 C C   A SER   B 2 151 ? -1.887  0.705   -21.825 0.25 68.72  ? 160 SER   B C   1 
ATOM   1600 C C   B SER   B 2 151 ? -1.873  0.760   -21.768 0.25 66.63  ? 160 SER   B C   1 
ATOM   1601 C C   C SER   B 2 151 ? -1.887  0.705   -21.825 0.25 68.72  ? 160 SER   B C   1 
ATOM   1602 C C   D SER   B 2 151 ? -1.873  0.760   -21.768 0.25 66.63  ? 160 SER   B C   1 
ATOM   1603 O O   A SER   B 2 151 ? -1.271  -0.004  -21.002 0.25 65.49  ? 160 SER   B O   1 
ATOM   1604 O O   B SER   B 2 151 ? -1.246  0.220   -20.834 0.25 65.08  ? 160 SER   B O   1 
ATOM   1605 O O   C SER   B 2 151 ? -1.271  -0.004  -21.002 0.25 65.49  ? 160 SER   B O   1 
ATOM   1606 O O   D SER   B 2 151 ? -1.246  0.220   -20.834 0.25 65.08  ? 160 SER   B O   1 
ATOM   1607 C CB  A SER   B 2 151 ? -1.383  0.473   -24.271 0.25 72.92  ? 160 SER   B CB  1 
ATOM   1608 C CB  B SER   B 2 151 ? -1.254  0.124   -24.100 0.25 66.35  ? 160 SER   B CB  1 
ATOM   1609 C CB  C SER   B 2 151 ? -1.383  0.473   -24.271 0.25 72.92  ? 160 SER   B CB  1 
ATOM   1610 C CB  D SER   B 2 151 ? -1.254  0.124   -24.100 0.25 66.35  ? 160 SER   B CB  1 
ATOM   1611 O OG  A SER   B 2 151 ? -2.704  0.689   -24.745 0.25 72.83  ? 160 SER   B OG  1 
ATOM   1612 O OG  B SER   B 2 151 ? -0.616  -1.084  -23.707 0.25 60.26  ? 160 SER   B OG  1 
ATOM   1613 O OG  C SER   B 2 151 ? -2.704  0.689   -24.745 0.25 72.83  ? 160 SER   B OG  1 
ATOM   1614 O OG  D SER   B 2 151 ? -0.616  -1.084  -23.707 0.25 60.26  ? 160 SER   B OG  1 
ATOM   1615 N N   . TYR   B 2 152 ? -3.190  0.985   -21.772 1.00 64.00  ? 161 TYR   B N   1 
ATOM   1616 C CA  . TYR   B 2 152 ? -4.099  0.618   -20.660 1.00 62.28  ? 161 TYR   B CA  1 
ATOM   1617 C C   . TYR   B 2 152 ? -4.793  -0.724  -20.927 1.00 50.28  ? 161 TYR   B C   1 
ATOM   1618 O O   . TYR   B 2 152 ? -5.316  -0.957  -21.988 1.00 48.68  ? 161 TYR   B O   1 
ATOM   1619 C CB  . TYR   B 2 152 ? -5.159  1.713   -20.527 1.00 65.38  ? 161 TYR   B CB  1 
ATOM   1620 C CG  . TYR   B 2 152 ? -5.959  1.641   -19.256 1.00 68.56  ? 161 TYR   B CG  1 
ATOM   1621 C CD1 . TYR   B 2 152 ? -5.358  1.864   -18.027 1.00 66.86  ? 161 TYR   B CD1 1 
ATOM   1622 C CD2 . TYR   B 2 152 ? -7.315  1.348   -19.285 1.00 75.68  ? 161 TYR   B CD2 1 
ATOM   1623 C CE1 . TYR   B 2 152 ? -6.080  1.792   -16.850 1.00 66.85  ? 161 TYR   B CE1 1 
ATOM   1624 C CE2 . TYR   B 2 152 ? -8.051  1.264   -18.113 1.00 79.52  ? 161 TYR   B CE2 1 
ATOM   1625 C CZ  . TYR   B 2 152 ? -7.430  1.483   -16.892 1.00 79.18  ? 161 TYR   B CZ  1 
ATOM   1626 O OH  . TYR   B 2 152 ? -8.162  1.409   -15.739 1.00 85.77  ? 161 TYR   B OH  1 
ATOM   1627 N N   . VAL   B 2 153 ? -4.850  -1.573  -19.918 1.00 52.11  ? 162 VAL   B N   1 
ATOM   1628 C CA  . VAL   B 2 153 ? -5.740  -2.762  -19.896 1.00 50.51  ? 162 VAL   B CA  1 
ATOM   1629 C C   . VAL   B 2 153 ? -6.716  -2.584  -18.712 1.00 47.56  ? 162 VAL   B C   1 
ATOM   1630 O O   . VAL   B 2 153 ? -6.269  -2.500  -17.581 1.00 45.63  ? 162 VAL   B O   1 
ATOM   1631 C CB  . VAL   B 2 153 ? -4.902  -4.056  -19.794 1.00 49.06  ? 162 VAL   B CB  1 
ATOM   1632 C CG1 . VAL   B 2 153 ? -5.742  -5.316  -20.001 1.00 45.32  ? 162 VAL   B CG1 1 
ATOM   1633 C CG2 . VAL   B 2 153 ? -3.722  -4.037  -20.759 1.00 57.52  ? 162 VAL   B CG2 1 
ATOM   1634 N N   . SER   B 2 154 ? -8.015  -2.535  -18.980 1.00 50.26  ? 163 SER   B N   1 
ATOM   1635 C CA  . SER   B 2 154 ? -9.086  -2.492  -17.959 1.00 50.95  ? 163 SER   B CA  1 
ATOM   1636 C C   . SER   B 2 154 ? -9.542  -3.913  -17.664 1.00 41.79  ? 163 SER   B C   1 
ATOM   1637 O O   . SER   B 2 154 ? -9.787  -4.625  -18.613 1.00 41.67  ? 163 SER   B O   1 
ATOM   1638 C CB  . SER   B 2 154 ? -10.298 -1.675  -18.395 1.00 49.49  ? 163 SER   B CB  1 
ATOM   1639 O OG  . SER   B 2 154 ? -11.372 -1.857  -17.465 1.00 42.98  ? 163 SER   B OG  1 
ATOM   1640 N N   . ALA   B 2 155 ? -9.754  -4.230  -16.390 1.00 41.61  ? 164 ALA   B N   1 
ATOM   1641 C CA  . ALA   B 2 155 ? -10.586 -5.351  -15.924 1.00 39.04  ? 164 ALA   B CA  1 
ATOM   1642 C C   . ALA   B 2 155 ? -11.986 -5.145  -16.469 1.00 43.95  ? 164 ALA   B C   1 
ATOM   1643 O O   . ALA   B 2 155 ? -12.433 -3.990  -16.593 1.00 42.92  ? 164 ALA   B O   1 
ATOM   1644 C CB  . ALA   B 2 155 ? -10.636 -5.421  -14.416 1.00 41.30  ? 164 ALA   B CB  1 
ATOM   1645 N N   . ILE   B 2 156 ? -12.641 -6.251  -16.744 1.00 37.09  ? 165 ILE   B N   1 
ATOM   1646 C CA  . ILE   B 2 156 ? -14.115 -6.318  -16.812 1.00 44.60  ? 165 ILE   B CA  1 
ATOM   1647 C C   . ILE   B 2 156 ? -14.634 -6.448  -15.366 1.00 42.69  ? 165 ILE   B C   1 
ATOM   1648 O O   . ILE   B 2 156 ? -14.715 -7.583  -14.856 1.00 39.93  ? 165 ILE   B O   1 
ATOM   1649 C CB  . ILE   B 2 156 ? -14.534 -7.495  -17.709 1.00 42.13  ? 165 ILE   B CB  1 
ATOM   1650 C CG1 . ILE   B 2 156 ? -13.865 -7.412  -19.092 1.00 45.74  ? 165 ILE   B CG1 1 
ATOM   1651 C CG2 . ILE   B 2 156 ? -16.056 -7.563  -17.822 1.00 41.46  ? 165 ILE   B CG2 1 
ATOM   1652 C CD1 . ILE   B 2 156 ? -14.097 -8.598  -19.943 1.00 47.25  ? 165 ILE   B CD1 1 
ATOM   1653 N N   . THR   B 2 157 ? -14.960 -5.337  -14.694 1.00 48.03  ? 166 THR   B N   1 
ATOM   1654 C CA  . THR   B 2 157 ? -15.430 -5.328  -13.279 1.00 39.03  ? 166 THR   B CA  1 
ATOM   1655 C C   . THR   B 2 157 ? -16.944 -5.610  -13.203 1.00 41.55  ? 166 THR   B C   1 
ATOM   1656 O O   . THR   B 2 157 ? -17.745 -4.778  -13.691 1.00 36.97  ? 166 THR   B O   1 
ATOM   1657 C CB  . THR   B 2 157 ? -15.056 -4.010  -12.618 1.00 44.57  ? 166 THR   B CB  1 
ATOM   1658 O OG1 . THR   B 2 157 ? -13.652 -3.832  -12.756 1.00 38.71  ? 166 THR   B OG1 1 
ATOM   1659 C CG2 . THR   B 2 157 ? -15.456 -3.948  -11.163 1.00 44.50  ? 166 THR   B CG2 1 
ATOM   1660 N N   . GLN   B 2 158 ? -17.348 -6.740  -12.620 1.00 36.57  ? 167 GLN   B N   1 
ATOM   1661 C CA  . GLN   B 2 158 ? -18.775 -7.061  -12.381 1.00 39.71  ? 167 GLN   B CA  1 
ATOM   1662 C C   . GLN   B 2 158 ? -19.024 -7.145  -10.867 1.00 39.86  ? 167 GLN   B C   1 
ATOM   1663 O O   . GLN   B 2 158 ? -18.129 -7.563  -10.128 1.00 37.04  ? 167 GLN   B O   1 
ATOM   1664 C CB  . GLN   B 2 158 ? -19.139 -8.317  -13.160 1.00 36.89  ? 167 GLN   B CB  1 
ATOM   1665 C CG  . GLN   B 2 158 ? -20.606 -8.704  -13.103 1.00 35.96  ? 167 GLN   B CG  1 
ATOM   1666 C CD  . GLN   B 2 158 ? -21.531 -7.625  -13.641 1.00 43.05  ? 167 GLN   B CD  1 
ATOM   1667 O OE1 . GLN   B 2 158 ? -21.616 -6.515  -13.123 1.00 41.55  ? 167 GLN   B OE1 1 
ATOM   1668 N NE2 . GLN   B 2 158 ? -22.270 -7.945  -14.684 1.00 40.40  ? 167 GLN   B NE2 1 
ATOM   1669 N N   . GLY   B 2 159 ? -20.180 -6.681  -10.410 1.00 43.06  ? 168 GLY   B N   1 
ATOM   1670 C CA  . GLY   B 2 159 ? -20.650 -6.909  -9.030  1.00 49.33  ? 168 GLY   B CA  1 
ATOM   1671 C C   . GLY   B 2 159 ? -21.407 -8.222  -8.900  1.00 55.35  ? 168 GLY   B C   1 
ATOM   1672 O O   . GLY   B 2 159 ? -21.560 -8.923  -9.889  1.00 65.21  ? 168 GLY   B O   1 
ATOM   1673 N N   . LYS   B 2 160 ? -21.900 -8.518  -7.702  1.00 68.97  ? 169 LYS   B N   1 
ATOM   1674 C CA  . LYS   B 2 160 ? -22.769 -9.682  -7.385  1.00 75.68  ? 169 LYS   B CA  1 
ATOM   1675 C C   . LYS   B 2 160 ? -24.200 -9.157  -7.197  1.00 81.95  ? 169 LYS   B C   1 
ATOM   1676 O O   . LYS   B 2 160 ? -24.340 -8.058  -6.660  1.00 77.00  ? 169 LYS   B O   1 
ATOM   1677 C CB  . LYS   B 2 160 ? -22.214 -10.390 -6.143  1.00 86.44  ? 169 LYS   B CB  1 
ATOM   1678 C CG  . LYS   B 2 160 ? -22.516 -11.880 -6.066  1.00 98.46  ? 169 LYS   B CG  1 
ATOM   1679 C CD  . LYS   B 2 160 ? -22.408 -12.441 -4.664  1.00 104.05 ? 169 LYS   B CD  1 
ATOM   1680 C CE  . LYS   B 2 160 ? -23.296 -13.647 -4.440  1.00 103.58 ? 169 LYS   B CE  1 
ATOM   1681 N NZ  . LYS   B 2 160 ? -23.780 -13.703 -3.041  1.00 105.96 ? 169 LYS   B NZ  1 
ATOM   1682 N N   . ARG   B 2 161 ? -25.219 -9.884  -7.663  1.00 88.45  ? 170 ARG   B N   1 
ATOM   1683 C CA  . ARG   B 2 161 ? -26.656 -9.514  -7.512  1.00 90.88  ? 170 ARG   B CA  1 
ATOM   1684 C C   . ARG   B 2 161 ? -27.301 -10.427 -6.452  1.00 97.25  ? 170 ARG   B C   1 
ATOM   1685 O O   . ARG   B 2 161 ? -27.308 -11.658 -6.667  1.00 90.26  ? 170 ARG   B O   1 
ATOM   1686 C CB  . ARG   B 2 161 ? -27.360 -9.611  -8.874  1.00 85.05  ? 170 ARG   B CB  1 
ATOM   1687 C CG  . ARG   B 2 161 ? -28.860 -9.336  -8.843  1.00 79.83  ? 170 ARG   B CG  1 
ATOM   1688 C CD  . ARG   B 2 161 ? -29.602 -9.839  -10.072 1.00 77.43  ? 170 ARG   B CD  1 
ATOM   1689 N NE  . ARG   B 2 161 ? -31.019 -9.510  -9.981  1.00 78.36  ? 170 ARG   B NE  1 
ATOM   1690 C CZ  . ARG   B 2 161 ? -31.686 -8.656  -10.763 1.00 84.23  ? 170 ARG   B CZ  1 
ATOM   1691 N NH1 . ARG   B 2 161 ? -31.094 -8.006  -11.757 1.00 71.85  ? 170 ARG   B NH1 1 
ATOM   1692 N NH2 . ARG   B 2 161 ? -32.973 -8.452  -10.534 1.00 89.17  ? 170 ARG   B NH2 1 
ATOM   1693 N N   . GLU   B 2 162 ? -27.841 -9.851  -5.366  1.00 107.68 ? 171 GLU   B N   1 
ATOM   1694 C CA  . GLU   B 2 162 ? -28.494 -10.594 -4.244  1.00 111.95 ? 171 GLU   B CA  1 
ATOM   1695 C C   . GLU   B 2 162 ? -29.982 -10.810 -4.554  1.00 103.17 ? 171 GLU   B C   1 
ATOM   1696 O O   . GLU   B 2 162 ? -30.510 -11.920 -4.477  1.00 101.89 ? 171 GLU   B O   1 
ATOM   1697 C CB  . GLU   B 2 162 ? -28.325 -9.838  -2.921  1.00 116.65 ? 171 GLU   B CB  1 
ATOM   1698 C CG  . GLU   B 2 162 ? -26.880 -9.494  -2.569  1.00 116.12 ? 171 GLU   B CG  1 
ATOM   1699 C CD  . GLU   B 2 162 ? -25.900 -10.662 -2.499  1.00 122.30 ? 171 GLU   B CD  1 
ATOM   1700 O OE1 . GLU   B 2 162 ? -25.670 -11.182 -1.379  1.00 111.12 ? 171 GLU   B OE1 1 
ATOM   1701 O OE2 . GLU   B 2 162 ? -25.344 -11.038 -3.560  1.00 113.45 ? 171 GLU   B OE2 1 
HETATM 1702 S S   A DMS   C 3 .   ? -8.409  5.727   -17.869 0.08 53.71  ? 201 DMS   B S   1 
HETATM 1703 S S   B DMS   C 3 .   ? -8.408  5.729   -17.872 0.13 53.81  ? 201 DMS   B S   1 
HETATM 1704 O O   A DMS   C 3 .   ? -7.003  5.336   -18.220 0.08 54.29  ? 201 DMS   B O   1 
HETATM 1705 O O   B DMS   C 3 .   ? -7.001  5.344   -18.231 0.13 54.50  ? 201 DMS   B O   1 
HETATM 1706 C C1  A DMS   C 3 .   ? -8.645  5.283   -16.168 0.08 53.79  ? 201 DMS   B C1  1 
HETATM 1707 C C1  B DMS   C 3 .   ? -8.640  5.280   -16.170 0.13 53.83  ? 201 DMS   B C1  1 
HETATM 1708 C C2  A DMS   C 3 .   ? -9.465  4.495   -18.591 0.08 52.53  ? 201 DMS   B C2  1 
HETATM 1709 C C2  B DMS   C 3 .   ? -9.463  4.494   -18.594 0.13 52.15  ? 201 DMS   B C2  1 
HETATM 1710 S S   . DMS   D 3 .   ? -18.742 12.085  -0.140  1.00 86.43  ? 202 DMS   B S   1 
HETATM 1711 O O   . DMS   D 3 .   ? -19.265 10.682  -0.336  1.00 78.12  ? 202 DMS   B O   1 
HETATM 1712 C C1  . DMS   D 3 .   ? -19.898 13.166  -0.943  1.00 96.93  ? 202 DMS   B C1  1 
HETATM 1713 C C2  . DMS   D 3 .   ? -17.384 12.299  -1.270  1.00 77.40  ? 202 DMS   B C2  1 
HETATM 1714 S S   A DMS   E 3 .   ? -7.154  3.684   -13.389 0.08 85.11  ? 203 DMS   B S   1 
HETATM 1715 S S   B DMS   E 3 .   ? -7.156  3.688   -13.390 0.13 85.08  ? 203 DMS   B S   1 
HETATM 1716 O O   A DMS   E 3 .   ? -6.975  2.196   -13.487 0.08 85.22  ? 203 DMS   B O   1 
HETATM 1717 O O   B DMS   E 3 .   ? -6.977  2.200   -13.494 0.13 85.22  ? 203 DMS   B O   1 
HETATM 1718 C C1  A DMS   E 3 .   ? -8.316  3.955   -12.076 0.08 85.44  ? 203 DMS   B C1  1 
HETATM 1719 C C1  B DMS   E 3 .   ? -8.316  3.956   -12.075 0.13 85.50  ? 203 DMS   B C1  1 
HETATM 1720 C C2  A DMS   E 3 .   ? -5.709  4.298   -12.564 0.08 85.03  ? 203 DMS   B C2  1 
HETATM 1721 C C2  B DMS   E 3 .   ? -5.709  4.299   -12.564 0.13 84.93  ? 203 DMS   B C2  1 
HETATM 1722 N N1  C A1BXQ F 4 .   ? -7.827  5.016   -10.767 0.39 76.52  ? 204 A1BXQ B N1  1 
HETATM 1723 N N1  D A1BXQ F 4 .   ? -7.827  5.017   -10.767 0.39 76.52  ? 204 A1BXQ B N1  1 
HETATM 1724 N N3  C A1BXQ F 4 .   ? -6.194  5.534   -15.362 0.39 82.78  ? 204 A1BXQ B N3  1 
HETATM 1725 N N3  D A1BXQ F 4 .   ? -6.194  5.534   -15.362 0.39 82.76  ? 204 A1BXQ B N3  1 
HETATM 1726 C C4  C A1BXQ F 4 .   ? -5.609  5.627   -18.114 0.39 81.48  ? 204 A1BXQ B C4  1 
HETATM 1727 C C4  D A1BXQ F 4 .   ? -5.609  5.627   -18.114 0.39 81.48  ? 204 A1BXQ B C4  1 
HETATM 1728 C C5  C A1BXQ F 4 .   ? -5.259  5.679   -19.582 0.39 83.58  ? 204 A1BXQ B C5  1 
HETATM 1729 C C5  D A1BXQ F 4 .   ? -5.259  5.678   -19.583 0.39 83.56  ? 204 A1BXQ B C5  1 
HETATM 1730 C C6  C A1BXQ F 4 .   ? -6.953  5.402   -17.679 0.39 82.03  ? 204 A1BXQ B C6  1 
HETATM 1731 C C6  D A1BXQ F 4 .   ? -6.953  5.402   -17.679 0.39 82.02  ? 204 A1BXQ B C6  1 
HETATM 1732 C C7  C A1BXQ F 4 .   ? -8.034  5.210   -18.577 0.39 80.46  ? 204 A1BXQ B C7  1 
HETATM 1733 C C7  D A1BXQ F 4 .   ? -8.034  5.210   -18.577 0.39 80.46  ? 204 A1BXQ B C7  1 
HETATM 1734 C C8  C A1BXQ F 4 .   ? -9.293  4.995   -18.107 0.39 80.32  ? 204 A1BXQ B C8  1 
HETATM 1735 C C8  D A1BXQ F 4 .   ? -9.293  4.995   -18.107 0.39 80.32  ? 204 A1BXQ B C8  1 
HETATM 1736 C C10 C A1BXQ F 4 .   ? -8.512  5.141   -15.810 0.39 77.94  ? 204 A1BXQ B C10 1 
HETATM 1737 C C10 D A1BXQ F 4 .   ? -8.512  5.141   -15.811 0.39 77.95  ? 204 A1BXQ B C10 1 
HETATM 1738 C C13 C A1BXQ F 4 .   ? -9.722  7.441   -14.144 0.39 71.76  ? 204 A1BXQ B C13 1 
HETATM 1739 C C13 D A1BXQ F 4 .   ? -9.722  7.442   -14.144 0.39 71.79  ? 204 A1BXQ B C13 1 
HETATM 1740 C C15 C A1BXQ F 4 .   ? -9.109  8.940   -12.389 0.39 73.87  ? 204 A1BXQ B C15 1 
HETATM 1741 C C15 D A1BXQ F 4 .   ? -9.109  8.940   -12.389 0.39 73.88  ? 204 A1BXQ B C15 1 
HETATM 1742 C C17 C A1BXQ F 4 .   ? -8.175  6.709   -12.458 0.39 74.77  ? 204 A1BXQ B C17 1 
HETATM 1743 C C17 D A1BXQ F 4 .   ? -8.175  6.709   -12.458 0.39 74.78  ? 204 A1BXQ B C17 1 
HETATM 1744 C C20 C A1BXQ F 4 .   ? -8.754  4.579   -8.636  0.39 76.03  ? 204 A1BXQ B C20 1 
HETATM 1745 C C20 D A1BXQ F 4 .   ? -8.754  4.579   -8.636  0.39 76.02  ? 204 A1BXQ B C20 1 
HETATM 1746 C C21 C A1BXQ F 4 .   ? -8.256  3.278   -9.270  0.39 73.55  ? 204 A1BXQ B C21 1 
HETATM 1747 C C21 D A1BXQ F 4 .   ? -8.256  3.278   -9.270  0.39 73.55  ? 204 A1BXQ B C21 1 
HETATM 1748 C C22 C A1BXQ F 4 .   ? -8.172  3.586   -10.757 0.39 73.04  ? 204 A1BXQ B C22 1 
HETATM 1749 C C22 D A1BXQ F 4 .   ? -8.172  3.586   -10.757 0.39 73.06  ? 204 A1BXQ B C22 1 
HETATM 1750 C C1  C A1BXQ F 4 .   ? -3.884  5.929   -14.770 0.39 77.78  ? 204 A1BXQ B C1  1 
HETATM 1751 C C1  D A1BXQ F 4 .   ? -3.884  5.929   -14.770 0.39 77.81  ? 204 A1BXQ B C1  1 
HETATM 1752 C C2  C A1BXQ F 4 .   ? -4.960  5.741   -15.797 0.39 81.81  ? 204 A1BXQ B C2  1 
HETATM 1753 C C2  D A1BXQ F 4 .   ? -4.960  5.741   -15.797 0.39 81.80  ? 204 A1BXQ B C2  1 
HETATM 1754 C C3  C A1BXQ F 4 .   ? -4.635  5.789   -17.168 0.39 80.53  ? 204 A1BXQ B C3  1 
HETATM 1755 C C3  D A1BXQ F 4 .   ? -4.635  5.789   -17.168 0.39 80.53  ? 204 A1BXQ B C3  1 
HETATM 1756 O O1  C A1BXQ F 4 .   ? -3.922  5.258   -19.855 0.39 79.49  ? 204 A1BXQ B O1  1 
HETATM 1757 O O1  D A1BXQ F 4 .   ? -3.922  5.258   -19.855 0.39 79.51  ? 204 A1BXQ B O1  1 
HETATM 1758 C C9  C A1BXQ F 4 .   ? -9.525  4.962   -16.718 0.39 79.57  ? 204 A1BXQ B C9  1 
HETATM 1759 C C9  D A1BXQ F 4 .   ? -9.525  4.962   -16.718 0.39 79.57  ? 204 A1BXQ B C9  1 
HETATM 1760 C C11 C A1BXQ F 4 .   ? -8.825  5.091   -14.320 0.39 73.31  ? 204 A1BXQ B C11 1 
HETATM 1761 C C11 D A1BXQ F 4 .   ? -8.825  5.091   -14.320 0.39 73.35  ? 204 A1BXQ B C11 1 
HETATM 1762 C C12 C A1BXQ F 4 .   ? -8.900  6.443   -13.627 0.39 74.18  ? 204 A1BXQ B C12 1 
HETATM 1763 C C12 D A1BXQ F 4 .   ? -8.900  6.443   -13.627 0.39 74.20  ? 204 A1BXQ B C12 1 
HETATM 1764 C C14 C A1BXQ F 4 .   ? -9.821  8.678   -13.538 0.39 72.75  ? 204 A1BXQ B C14 1 
HETATM 1765 C C14 D A1BXQ F 4 .   ? -9.821  8.678   -13.538 0.39 72.77  ? 204 A1BXQ B C14 1 
HETATM 1766 C C16 C A1BXQ F 4 .   ? -8.295  7.965   -11.843 0.39 76.17  ? 204 A1BXQ B C16 1 
HETATM 1767 C C16 D A1BXQ F 4 .   ? -8.295  7.965   -11.843 0.39 76.16  ? 204 A1BXQ B C16 1 
HETATM 1768 C C18 C A1BXQ F 4 .   ? -7.305  5.666   -11.823 0.39 79.77  ? 204 A1BXQ B C18 1 
HETATM 1769 C C18 D A1BXQ F 4 .   ? -7.305  5.666   -11.823 0.39 79.74  ? 204 A1BXQ B C18 1 
HETATM 1770 O O2  C A1BXQ F 4 .   ? -6.213  5.357   -12.303 0.39 78.50  ? 204 A1BXQ B O2  1 
HETATM 1771 O O2  D A1BXQ F 4 .   ? -6.213  5.357   -12.303 0.39 78.49  ? 204 A1BXQ B O2  1 
HETATM 1772 C C19 C A1BXQ F 4 .   ? -8.218  5.687   -9.517  0.39 79.49  ? 204 A1BXQ B C19 1 
HETATM 1773 C C19 D A1BXQ F 4 .   ? -8.218  5.687   -9.516  0.39 79.46  ? 204 A1BXQ B C19 1 
HETATM 1774 N N2  C A1BXQ F 4 .   ? -9.144  2.159   -8.957  0.39 69.58  ? 204 A1BXQ B N2  1 
HETATM 1775 N N2  D A1BXQ F 4 .   ? -9.143  2.159   -8.957  0.39 69.62  ? 204 A1BXQ B N2  1 
HETATM 1776 C C23 C A1BXQ F 4 .   ? -7.203  5.361   -16.275 0.39 81.96  ? 204 A1BXQ B C23 1 
HETATM 1777 C C23 D A1BXQ F 4 .   ? -7.203  5.361   -16.275 0.39 81.95  ? 204 A1BXQ B C23 1 
HETATM 1778 S S   C DMS   G 3 .   ? -7.782  12.232  -19.672 0.50 114.33 ? 205 DMS   B S   1 
HETATM 1779 S S   D DMS   G 3 .   ? -7.782  12.232  -19.672 0.50 114.33 ? 205 DMS   B S   1 
HETATM 1780 O O   C DMS   G 3 .   ? -7.104  10.907  -19.432 0.50 98.11  ? 205 DMS   B O   1 
HETATM 1781 O O   D DMS   G 3 .   ? -7.104  10.907  -19.432 0.50 98.11  ? 205 DMS   B O   1 
HETATM 1782 C C1  C DMS   G 3 .   ? -6.498  13.463  -19.679 0.50 112.44 ? 205 DMS   B C1  1 
HETATM 1783 C C1  D DMS   G 3 .   ? -6.498  13.463  -19.679 0.50 112.44 ? 205 DMS   B C1  1 
HETATM 1784 C C2  C DMS   G 3 .   ? -8.548  12.678  -18.132 0.50 106.42 ? 205 DMS   B C2  1 
HETATM 1785 C C2  D DMS   G 3 .   ? -8.548  12.678  -18.132 0.50 106.42 ? 205 DMS   B C2  1 
HETATM 1786 O O   . HOH   H 5 .   ? -27.737 -5.875  -28.219 1.00 51.73  ? 101 HOH   A O   1 
HETATM 1787 O O   . HOH   H 5 .   ? -6.863  -8.637  -3.147  1.00 45.79  ? 102 HOH   A O   1 
HETATM 1788 O O   . HOH   H 5 .   ? -2.217  -3.796  -6.417  1.00 50.81  ? 103 HOH   A O   1 
HETATM 1789 O O   . HOH   H 5 .   ? -23.830 19.109  -19.514 1.00 63.63  ? 104 HOH   A O   1 
HETATM 1790 O O   . HOH   H 5 .   ? -24.091 9.328   -27.513 1.00 47.68  ? 105 HOH   A O   1 
HETATM 1791 O O   A HOH   H 5 .   ? -7.963  0.328   3.588   0.50 61.47  ? 106 HOH   A O   1 
HETATM 1792 O O   B HOH   H 5 .   ? -7.963  0.328   3.588   0.50 61.47  ? 106 HOH   A O   1 
HETATM 1793 O O   C HOH   H 5 .   ? -25.346 12.477  -23.804 0.50 52.90  ? 107 HOH   A O   1 
HETATM 1794 O O   D HOH   H 5 .   ? -25.346 12.477  -23.804 0.50 52.90  ? 107 HOH   A O   1 
HETATM 1795 O O   A HOH   H 5 .   ? -28.902 15.815  -15.092 0.50 78.50  ? 108 HOH   A O   1 
HETATM 1796 O O   B HOH   H 5 .   ? -28.902 15.815  -15.092 0.50 78.50  ? 108 HOH   A O   1 
HETATM 1797 O O   A HOH   H 5 .   ? -8.546  2.703   -8.435  0.08 33.49  ? 109 HOH   A O   1 
HETATM 1798 O O   B HOH   H 5 .   ? -8.541  2.705   -8.427  0.13 33.49  ? 109 HOH   A O   1 
HETATM 1799 O O   . HOH   H 5 .   ? -9.332  -6.648  -25.513 1.00 55.86  ? 110 HOH   A O   1 
HETATM 1800 O O   A HOH   H 5 .   ? -8.027  -1.729  6.689   0.50 67.79  ? 111 HOH   A O   1 
HETATM 1801 O O   B HOH   H 5 .   ? -8.027  -1.729  6.689   0.50 67.79  ? 111 HOH   A O   1 
HETATM 1802 O O   . HOH   H 5 .   ? -3.867  -0.776  -0.349  1.00 57.38  ? 112 HOH   A O   1 
HETATM 1803 O O   . HOH   H 5 .   ? -3.609  -3.954  0.181   1.00 65.51  ? 113 HOH   A O   1 
HETATM 1804 O O   . HOH   H 5 .   ? -6.400  -20.646 -21.334 1.00 67.83  ? 114 HOH   A O   1 
HETATM 1805 O O   A HOH   H 5 .   ? -30.971 0.274   -29.374 0.50 73.74  ? 115 HOH   A O   1 
HETATM 1806 O O   B HOH   H 5 .   ? -30.971 0.274   -29.374 0.50 73.74  ? 115 HOH   A O   1 
HETATM 1807 O O   . HOH   H 5 .   ? -22.405 -9.371  -34.479 1.00 50.61  ? 116 HOH   A O   1 
HETATM 1808 O O   . HOH   H 5 .   ? -4.267  -14.551 -25.392 1.00 50.58  ? 117 HOH   A O   1 
HETATM 1809 O O   . HOH   H 5 .   ? -30.609 0.518   -22.996 1.00 59.77  ? 118 HOH   A O   1 
HETATM 1810 O O   . HOH   H 5 .   ? -4.526  -10.132 -5.630  1.00 51.30  ? 119 HOH   A O   1 
HETATM 1811 O O   A HOH   H 5 .   ? -26.356 -2.966  -35.369 0.50 75.36  ? 120 HOH   A O   1 
HETATM 1812 O O   B HOH   H 5 .   ? -26.356 -2.966  -35.369 0.50 75.36  ? 120 HOH   A O   1 
HETATM 1813 O O   C HOH   H 5 .   ? -26.621 1.913   -29.442 0.50 67.38  ? 121 HOH   A O   1 
HETATM 1814 O O   D HOH   H 5 .   ? -26.621 1.913   -29.442 0.50 67.38  ? 121 HOH   A O   1 
HETATM 1815 O O   A HOH   H 5 .   ? -4.068  1.855   -9.794  0.08 25.26  ? 122 HOH   A O   1 
HETATM 1816 O O   B HOH   H 5 .   ? -4.074  1.849   -9.798  0.13 25.43  ? 122 HOH   A O   1 
HETATM 1817 O O   . HOH   H 5 .   ? -2.698  -8.856  -3.382  1.00 62.87  ? 123 HOH   A O   1 
HETATM 1818 O O   A HOH   H 5 .   ? -9.031  5.574   -7.438  0.08 35.10  ? 124 HOH   A O   1 
HETATM 1819 O O   B HOH   H 5 .   ? -9.025  5.638   -7.454  0.13 35.38  ? 124 HOH   A O   1 
HETATM 1820 O O   . HOH   I 5 .   ? -30.735 12.906  -19.400 1.00 50.56  ? 301 HOH   B O   1 
HETATM 1821 O O   C HOH   I 5 .   ? -7.050  1.975   -13.947 0.39 55.55  ? 302 HOH   B O   1 
HETATM 1822 O O   D HOH   I 5 .   ? -7.050  1.980   -13.947 0.39 55.59  ? 302 HOH   B O   1 
HETATM 1823 O O   A HOH   I 5 .   ? -34.911 6.017   -11.826 0.50 95.40  ? 303 HOH   B O   1 
HETATM 1824 O O   B HOH   I 5 .   ? -34.911 6.017   -11.826 0.50 95.40  ? 303 HOH   B O   1 
HETATM 1825 O O   . HOH   I 5 .   ? -33.843 1.570   -15.403 1.00 50.56  ? 304 HOH   B O   1 
HETATM 1826 O O   . HOH   I 5 .   ? -17.252 12.877  -5.478  1.00 61.83  ? 305 HOH   B O   1 
HETATM 1827 O O   A HOH   I 5 .   ? -15.670 -9.724  -15.116 0.50 45.53  ? 306 HOH   B O   1 
HETATM 1828 O O   B HOH   I 5 .   ? -15.670 -9.724  -15.116 0.50 45.53  ? 306 HOH   B O   1 
HETATM 1829 O O   . HOH   I 5 .   ? -25.906 -7.937  -16.654 1.00 45.08  ? 307 HOH   B O   1 
HETATM 1830 O O   . HOH   I 5 .   ? -19.641 -12.209 -25.822 1.00 61.81  ? 308 HOH   B O   1 
HETATM 1831 O O   . HOH   I 5 .   ? -16.220 26.203  -12.480 1.00 60.44  ? 309 HOH   B O   1 
HETATM 1832 O O   . HOH   I 5 .   ? -21.727 -13.415 -21.445 1.00 51.57  ? 310 HOH   B O   1 
HETATM 1833 O O   A HOH   I 5 .   ? -29.065 -1.982  -18.869 0.50 66.15  ? 311 HOH   B O   1 
HETATM 1834 O O   B HOH   I 5 .   ? -29.065 -1.982  -18.869 0.50 66.15  ? 311 HOH   B O   1 
HETATM 1835 O O   . HOH   I 5 .   ? -21.824 -12.095 -12.910 1.00 51.82  ? 312 HOH   B O   1 
HETATM 1836 O O   . HOH   I 5 .   ? -16.516 -14.550 -16.535 1.00 55.27  ? 313 HOH   B O   1 
HETATM 1837 O O   A HOH   I 5 .   ? -10.744 -17.875 -12.047 0.50 79.97  ? 314 HOH   B O   1 
HETATM 1838 O O   B HOH   I 5 .   ? -10.744 -17.875 -12.047 0.50 79.97  ? 314 HOH   B O   1 
HETATM 1839 O O   A HOH   I 5 .   ? -11.410 12.009  -19.617 0.50 60.05  ? 315 HOH   B O   1 
HETATM 1840 O O   B HOH   I 5 .   ? -11.410 12.009  -19.617 0.50 60.05  ? 315 HOH   B O   1 
HETATM 1841 O O   . HOH   I 5 .   ? -6.245  -0.356  -10.869 1.00 42.77  ? 316 HOH   B O   1 
HETATM 1842 O O   . HOH   I 5 .   ? -16.771 20.933  -14.085 1.00 51.39  ? 317 HOH   B O   1 
HETATM 1843 O O   . HOH   I 5 .   ? -28.758 -4.070  -22.203 1.00 54.80  ? 318 HOH   B O   1 
HETATM 1844 O O   . HOH   I 5 .   ? -16.332 -7.093  -8.234  1.00 61.81  ? 319 HOH   B O   1 
HETATM 1845 O O   . HOH   I 5 .   ? -19.080 -5.368  -0.904  1.00 47.22  ? 320 HOH   B O   1 
HETATM 1846 O O   . HOH   I 5 .   ? -12.104 2.406   -5.822  1.00 52.82  ? 321 HOH   B O   1 
HETATM 1847 O O   . HOH   I 5 .   ? -27.876 -6.125  -18.484 1.00 49.85  ? 322 HOH   B O   1 
HETATM 1848 O O   A HOH   I 5 .   ? -14.295 -5.803  -1.938  0.50 60.91  ? 323 HOH   B O   1 
HETATM 1849 O O   B HOH   I 5 .   ? -14.295 -5.803  -1.938  0.50 60.91  ? 323 HOH   B O   1 
HETATM 1850 O O   . HOH   I 5 .   ? -6.784  -10.928 -5.491  1.00 61.55  ? 324 HOH   B O   1 
HETATM 1851 O O   A HOH   I 5 .   ? -17.898 25.457  -13.945 0.50 83.62  ? 325 HOH   B O   1 
HETATM 1852 O O   B HOH   I 5 .   ? -17.898 25.457  -13.945 0.50 83.62  ? 325 HOH   B O   1 
HETATM 1853 O O   A HOH   I 5 .   ? -19.885 -7.736  -2.963  0.50 63.36  ? 326 HOH   B O   1 
HETATM 1854 O O   B HOH   I 5 .   ? -19.885 -7.736  -2.963  0.50 63.36  ? 326 HOH   B O   1 
HETATM 1855 O O   A HOH   I 5 .   ? -27.593 -7.144  -5.442  0.50 77.04  ? 327 HOH   B O   1 
HETATM 1856 O O   B HOH   I 5 .   ? -27.593 -7.144  -5.442  0.50 77.04  ? 327 HOH   B O   1 
HETATM 1857 O O   . HOH   I 5 .   ? -15.440 9.568   -0.739  1.00 53.60  ? 328 HOH   B O   1 
HETATM 1858 O O   A HOH   I 5 .   ? -18.423 19.428  -21.881 0.50 56.18  ? 329 HOH   B O   1 
HETATM 1859 O O   B HOH   I 5 .   ? -18.423 19.428  -21.881 0.50 56.18  ? 329 HOH   B O   1 
HETATM 1860 O O   A HOH   I 5 .   ? -35.431 -5.409  -10.363 0.50 60.47  ? 330 HOH   B O   1 
HETATM 1861 O O   B HOH   I 5 .   ? -35.431 -5.409  -10.363 0.50 60.47  ? 330 HOH   B O   1 
HETATM 1862 O O   . HOH   I 5 .   ? -12.512 -3.254  -10.189 1.00 42.19  ? 331 HOH   B O   1 
HETATM 1863 O O   . HOH   I 5 .   ? -17.933 -10.566 -16.467 1.00 41.77  ? 332 HOH   B O   1 
HETATM 1864 O O   . HOH   I 5 .   ? -12.946 -1.931  -14.688 1.00 42.42  ? 333 HOH   B O   1 
HETATM 1865 O O   . HOH   I 5 .   ? -15.314 -4.525  1.398   1.00 47.41  ? 334 HOH   B O   1 
HETATM 1866 O O   A HOH   I 5 .   ? -21.153 7.272   0.000   0.23 55.36  ? 335 HOH   B O   1 
HETATM 1867 O O   B HOH   I 5 .   ? -21.153 7.286   -0.000  0.13 55.99  ? 335 HOH   B O   1 
HETATM 1868 O O   . HOH   I 5 .   ? -16.367 -13.904 -30.844 1.00 60.34  ? 336 HOH   B O   1 
HETATM 1869 O O   . HOH   I 5 .   ? -14.453 -12.136 -16.503 1.00 52.49  ? 337 HOH   B O   1 
HETATM 1870 O O   . HOH   I 5 .   ? -30.696 12.700  -16.504 1.00 63.64  ? 338 HOH   B O   1 
HETATM 1871 O O   . HOH   I 5 .   ? -2.993  -11.878 -6.964  1.00 53.18  ? 339 HOH   B O   1 
HETATM 1872 O O   . HOH   I 5 .   ? -17.252 14.971  -30.861 1.00 55.47  ? 340 HOH   B O   1 
HETATM 1873 O O   . HOH   I 5 .   ? -23.938 -14.699 -17.313 1.00 57.64  ? 341 HOH   B O   1 
HETATM 1874 O O   C HOH   I 5 .   ? 3.441   -5.218  -20.887 0.50 68.70  ? 342 HOH   B O   1 
HETATM 1875 O O   D HOH   I 5 .   ? 3.441   -5.218  -20.887 0.50 68.70  ? 342 HOH   B O   1 
HETATM 1876 O O   . HOH   I 5 .   ? -18.820 15.137  -22.080 1.00 41.22  ? 343 HOH   B O   1 
HETATM 1877 O O   A HOH   I 5 .   ? -19.655 25.094  -15.114 0.50 109.96 ? 344 HOH   B O   1 
HETATM 1878 O O   B HOH   I 5 .   ? -19.655 25.094  -15.114 0.50 109.96 ? 344 HOH   B O   1 
HETATM 1879 O O   A HOH   I 5 .   ? -11.816 -17.902 -27.938 0.50 71.47  ? 345 HOH   B O   1 
HETATM 1880 O O   B HOH   I 5 .   ? -11.816 -17.902 -27.938 0.50 71.47  ? 345 HOH   B O   1 
HETATM 1881 O O   . HOH   I 5 .   ? -11.419 -4.941  -8.283  1.00 47.96  ? 346 HOH   B O   1 
HETATM 1882 O O   . HOH   I 5 .   ? -31.919 7.214   -4.625  1.00 62.27  ? 347 HOH   B O   1 
HETATM 1883 O O   A HOH   I 5 .   ? 0.009   -0.092  -13.684 0.50 63.17  ? 348 HOH   B O   1 
HETATM 1884 O O   B HOH   I 5 .   ? 0.009   -0.092  -13.684 0.50 63.17  ? 348 HOH   B O   1 
HETATM 1885 O O   A HOH   I 5 .   ? -23.083 2.116   -32.451 0.50 86.98  ? 349 HOH   B O   1 
HETATM 1886 O O   B HOH   I 5 .   ? -23.083 2.116   -32.451 0.50 86.98  ? 349 HOH   B O   1 
HETATM 1887 O O   . HOH   I 5 .   ? -8.598  -10.516 -7.341  1.00 63.37  ? 350 HOH   B O   1 
HETATM 1888 O O   . HOH   I 5 .   ? -30.802 4.694   -2.457  1.00 55.95  ? 351 HOH   B O   1 
HETATM 1889 O O   . HOH   I 5 .   ? -14.983 16.629  -20.327 1.00 56.23  ? 352 HOH   B O   1 
HETATM 1890 O O   A HOH   I 5 .   ? -19.678 -13.203 -22.937 0.50 46.78  ? 353 HOH   B O   1 
HETATM 1891 O O   B HOH   I 5 .   ? -19.678 -13.203 -22.937 0.50 46.78  ? 353 HOH   B O   1 
HETATM 1892 O O   . HOH   I 5 .   ? -25.832 -4.568  -3.908  1.00 52.91  ? 354 HOH   B O   1 
HETATM 1893 O O   A HOH   I 5 .   ? -7.159  -6.131  0.464   0.50 62.01  ? 355 HOH   B O   1 
HETATM 1894 O O   B HOH   I 5 .   ? -7.159  -6.131  0.464   0.50 62.01  ? 355 HOH   B O   1 
HETATM 1895 O O   A HOH   I 5 .   ? -32.190 -6.686  -6.856  0.50 56.45  ? 356 HOH   B O   1 
HETATM 1896 O O   B HOH   I 5 .   ? -32.190 -6.686  -6.856  0.50 56.45  ? 356 HOH   B O   1 
HETATM 1897 O O   A HOH   I 5 .   ? -29.451 -5.150  -0.878  0.50 56.92  ? 357 HOH   B O   1 
HETATM 1898 O O   B HOH   I 5 .   ? -29.451 -5.150  -0.878  0.50 56.92  ? 357 HOH   B O   1 
HETATM 1899 O O   . HOH   I 5 .   ? -1.463  -14.179 -9.581  1.00 63.40  ? 358 HOH   B O   1 
HETATM 1900 O O   . HOH   I 5 .   ? -30.379 -7.745  -5.506  1.00 65.59  ? 359 HOH   B O   1 
HETATM 1901 O O   C HOH   I 5 .   ? -18.499 -10.839 -9.946  0.50 60.77  ? 360 HOH   B O   1 
HETATM 1902 O O   D HOH   I 5 .   ? -18.499 -10.839 -9.946  0.50 60.77  ? 360 HOH   B O   1 
HETATM 1903 O O   A HOH   I 5 .   ? 8.264   -4.687  -17.563 0.50 71.15  ? 361 HOH   B O   1 
HETATM 1904 O O   B HOH   I 5 .   ? 8.264   -4.687  -17.563 0.50 71.15  ? 361 HOH   B O   1 
HETATM 1905 O O   C HOH   I 5 .   ? -10.061 6.595   -6.509  0.39 56.43  ? 362 HOH   B O   1 
HETATM 1906 O O   D HOH   I 5 .   ? -10.058 6.598   -6.507  0.39 56.45  ? 362 HOH   B O   1 
HETATM 1907 O O   . HOH   I 5 .   ? -17.043 16.809  -21.865 1.00 51.82  ? 363 HOH   B O   1 
HETATM 1908 O O   C HOH   I 5 .   ? -21.064 -6.903  -0.271  0.50 55.17  ? 364 HOH   B O   1 
HETATM 1909 O O   D HOH   I 5 .   ? -21.064 -6.903  -0.271  0.50 55.17  ? 364 HOH   B O   1 
HETATM 1910 O O   . HOH   I 5 .   ? -23.284 -7.176  -1.919  1.00 56.31  ? 365 HOH   B O   1 
HETATM 1911 O O   A HOH   I 5 .   ? -10.157 8.539   -13.113 0.08 10.73  ? 366 HOH   B O   1 
HETATM 1912 O O   B HOH   I 5 .   ? -11.043 7.770   -13.937 0.13 21.38  ? 366 HOH   B O   1 
HETATM 1913 O O   A HOH   I 5 .   ? -19.205 -11.776 -13.798 0.50 61.93  ? 367 HOH   B O   1 
HETATM 1914 O O   B HOH   I 5 .   ? -19.205 -11.776 -13.798 0.50 61.93  ? 367 HOH   B O   1 
HETATM 1915 O O   A HOH   I 5 .   ? -11.972 12.396  -14.659 0.50 73.70  ? 368 HOH   B O   1 
HETATM 1916 O O   B HOH   I 5 .   ? -11.972 12.396  -14.659 0.50 73.70  ? 368 HOH   B O   1 
HETATM 1917 O O   A HOH   I 5 .   ? -30.308 -11.998 -27.092 0.25 92.84  ? 369 HOH   B O   1 
HETATM 1918 O O   B HOH   I 5 .   ? -30.308 -11.998 -27.092 0.25 92.84  ? 369 HOH   B O   1 
HETATM 1919 O O   A HOH   I 5 .   ? -11.125 5.198   -5.740  0.08 12.09  ? 370 HOH   B O   1 
HETATM 1920 O O   B HOH   I 5 .   ? -11.581 4.835   -5.040  0.13 27.99  ? 370 HOH   B O   1 
HETATM 1921 O O   A HOH   I 5 .   ? -11.994 -6.878  1.823   0.50 61.78  ? 371 HOH   B O   1 
HETATM 1922 O O   B HOH   I 5 .   ? -11.994 -6.878  1.823   0.50 61.78  ? 371 HOH   B O   1 
HETATM 1923 O O   . HOH   I 5 .   ? -21.153 4.474   0.000   0.50 62.50  ? 372 HOH   B O   1 
# 
