data_7HOS
# 
_entry.id   7HOS 
# 
_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   7HOS         pdb_00007hos 10.2210/pdb7hos/pdb 
WWPDB D_1001407742 ?            ?                   
# 
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 2025-02-26 ? 
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                        7HOS 
_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   2024-11-07 
_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  
'Lee, A.'             9  
'Kenton, N.'          10 
'Thompson, W.'        11 
'Tomlinson, C.W.E.'   12 
'Wild, C.'            13 
'Winokan, M.'         14 
'Williams, E.P.'      15 
'Chandran, A.V.'      16 
'Walsh, M.A.'         17 
'Fearon, D.'          18 
'von Delft, F.'       19 
# 
_citation.id                        primary 
_citation.title                     '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 'Lee, A.'             ? 9  
primary 'Kenton, N.'          ? 10 
primary 'Thompson, W.'        ? 11 
primary 'Tomlinson, C.W.E.'   ? 12 
primary 'Wild, C.'            ? 13 
primary 'Winokan, M.'         ? 14 
primary 'Williams, E.P.'      ? 15 
primary 'Chandran, A.V.'      ? 16 
primary 'Walsh, M.A.'         ? 17 
primary 'Fearon, D.'          ? 18 
primary 'von Delft, F.'       ? 19 
# 
loop_
_entity.id 
_entity.type 
_entity.src_method 
_entity.pdbx_description 
_entity.formula_weight 
_entity.pdbx_number_of_molecules 
_entity.pdbx_ec 
_entity.pdbx_mutation 
_entity.pdbx_fragment 
_entity.details 
1 polymer     man 'Serine protease subunit NS2B'                                                 5067.486  1  ? ?    ? ? 
2 polymer     man 'Serine protease NS3'                                                          18117.629 1  
3.4.21.91,3.6.1.15,3.6.4.13 None ? ? 
3 non-polymer syn 'DIMETHYL SULFOXIDE'                                                           78.133    3  ? ?    ? ? 
4 non-polymer syn '5-cyclopropyl-1,2-dimethyl-N-(3-methylpyridin-4-yl)-1H-pyrrole-3-carboxamide' 269.342   1  ? ?    ? ? 
5 non-polymer syn 'SULFATE ION'                                                                  96.063    1  ? ?    ? ? 
6 water       nat water                                                                          18.015    98 ? ?    ? ? 
# 
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 '5-cyclopropyl-1,2-dimethyl-N-(3-methylpyridin-4-yl)-1H-pyrrole-3-carboxamide' A1BGY 
5 'SULFATE ION'                                                                  SO4   
6 water                                                                          HOH   
# 
loop_
_entity_poly_seq.entity_id 
_entity_poly_seq.num 
_entity_poly_seq.mon_id 
_entity_poly_seq.hetero 
1 1   SER n 
1 2   MET n 
1 3   GLY n 
1 4   LYS n 
1 5   SER n 
1 6   VAL n 
1 7   ASP n 
1 8   MET n 
1 9   TYR n 
1 10  ILE n 
1 11  GLU n 
1 12  ARG n 
1 13  ALA n 
1 14  GLY n 
1 15  ASP n 
1 16  ILE n 
1 17  THR n 
1 18  TRP n 
1 19  GLU n 
1 20  LYS n 
1 21  ASP n 
1 22  ALA n 
1 23  GLU n 
1 24  VAL n 
1 25  THR n 
1 26  GLY n 
1 27  ASN n 
1 28  SER n 
1 29  PRO n 
1 30  ARG n 
1 31  LEU n 
1 32  ASP n 
1 33  VAL n 
1 34  ALA n 
1 35  LEU n 
1 36  ASP n 
1 37  GLU n 
1 38  SER n 
1 39  GLY n 
1 40  ASP n 
1 41  PHE n 
1 42  SER n 
1 43  LEU n 
1 44  VAL n 
1 45  GLU n 
1 46  GLU n 
2 1   MET n 
2 2   LYS n 
2 3   GLU n 
2 4   VAL n 
2 5   LYS n 
2 6   LYS n 
2 7   GLY n 
2 8   GLU n 
2 9   THR n 
2 10  THR n 
2 11  ASP n 
2 12  GLY n 
2 13  VAL n 
2 14  TYR n 
2 15  ARG n 
2 16  VAL n 
2 17  MET n 
2 18  THR n 
2 19  ARG n 
2 20  ARG n 
2 21  LEU n 
2 22  LEU n 
2 23  GLY n 
2 24  SER n 
2 25  THR n 
2 26  GLN n 
2 27  VAL n 
2 28  GLY n 
2 29  VAL n 
2 30  GLY n 
2 31  VAL n 
2 32  MET n 
2 33  GLN n 
2 34  GLU n 
2 35  GLY n 
2 36  VAL n 
2 37  PHE n 
2 38  HIS n 
2 39  THR n 
2 40  MET n 
2 41  TRP n 
2 42  HIS n 
2 43  VAL n 
2 44  THR n 
2 45  LYS n 
2 46  GLY n 
2 47  ALA n 
2 48  ALA n 
2 49  LEU n 
2 50  ARG n 
2 51  SER n 
2 52  GLY n 
2 53  GLU n 
2 54  GLY n 
2 55  ARG n 
2 56  LEU n 
2 57  ASP n 
2 58  PRO n 
2 59  TYR n 
2 60  TRP n 
2 61  GLY n 
2 62  ASP n 
2 63  VAL n 
2 64  LYS n 
2 65  GLN n 
2 66  ASP n 
2 67  LEU n 
2 68  VAL n 
2 69  SER n 
2 70  TYR n 
2 71  CYS n 
2 72  GLY n 
2 73  PRO n 
2 74  TRP n 
2 75  LYS n 
2 76  LEU n 
2 77  ASP n 
2 78  ALA n 
2 79  ALA n 
2 80  TRP n 
2 81  ASP n 
2 82  GLY n 
2 83  LEU n 
2 84  SER n 
2 85  GLU n 
2 86  VAL n 
2 87  GLN n 
2 88  LEU n 
2 89  LEU n 
2 90  ALA n 
2 91  VAL n 
2 92  PRO n 
2 93  PRO n 
2 94  GLY n 
2 95  GLU n 
2 96  ARG n 
2 97  ALA n 
2 98  LYS n 
2 99  ASN n 
2 100 ILE n 
2 101 GLN n 
2 102 THR n 
2 103 LEU n 
2 104 PRO n 
2 105 GLY n 
2 106 ILE n 
2 107 PHE n 
2 108 LYS n 
2 109 THR n 
2 110 LYS n 
2 111 ASP n 
2 112 GLY n 
2 113 ASP n 
2 114 ILE n 
2 115 GLY n 
2 116 ALA n 
2 117 VAL n 
2 118 ALA n 
2 119 LEU n 
2 120 ASP n 
2 121 TYR n 
2 122 PRO n 
2 123 ALA n 
2 124 GLY n 
2 125 THR n 
2 126 SER n 
2 127 GLY n 
2 128 SER n 
2 129 PRO n 
2 130 ILE n 
2 131 LEU n 
2 132 ASP n 
2 133 LYS n 
2 134 CYS n 
2 135 GLY n 
2 136 ARG n 
2 137 VAL n 
2 138 ILE n 
2 139 GLY n 
2 140 LEU n 
2 141 TYR n 
2 142 GLY n 
2 143 ASN n 
2 144 GLY n 
2 145 VAL n 
2 146 VAL n 
2 147 ILE n 
2 148 LYS n 
2 149 ASN n 
2 150 GLY n 
2 151 SER n 
2 152 TYR n 
2 153 VAL n 
2 154 SER n 
2 155 ALA n 
2 156 ILE n 
2 157 THR n 
2 158 GLN n 
2 159 GLY n 
2 160 LYS n 
2 161 ARG n 
2 162 GLU n 
2 163 GLU n 
2 164 GLU n 
2 165 THR n 
2 166 PRO n 
2 167 VAL n 
2 168 GLU n 
# 
loop_
_entity_src_gen.entity_id 
_entity_src_gen.pdbx_src_id 
_entity_src_gen.pdbx_alt_source_flag 
_entity_src_gen.pdbx_seq_type 
_entity_src_gen.pdbx_beg_seq_num 
_entity_src_gen.pdbx_end_seq_num 
_entity_src_gen.gene_src_common_name 
_entity_src_gen.gene_src_genus 
_entity_src_gen.pdbx_gene_src_gene 
_entity_src_gen.gene_src_species 
_entity_src_gen.gene_src_strain 
_entity_src_gen.gene_src_tissue 
_entity_src_gen.gene_src_tissue_fraction 
_entity_src_gen.gene_src_details 
_entity_src_gen.pdbx_gene_src_fragment 
_entity_src_gen.pdbx_gene_src_scientific_name 
_entity_src_gen.pdbx_gene_src_ncbi_taxonomy_id 
_entity_src_gen.pdbx_gene_src_variant 
_entity_src_gen.pdbx_gene_src_cell_line 
_entity_src_gen.pdbx_gene_src_atcc 
_entity_src_gen.pdbx_gene_src_organ 
_entity_src_gen.pdbx_gene_src_organelle 
_entity_src_gen.pdbx_gene_src_cell 
_entity_src_gen.pdbx_gene_src_cellular_location 
_entity_src_gen.host_org_common_name 
_entity_src_gen.pdbx_host_org_scientific_name 
_entity_src_gen.pdbx_host_org_ncbi_taxonomy_id 
_entity_src_gen.host_org_genus 
_entity_src_gen.pdbx_host_org_gene 
_entity_src_gen.pdbx_host_org_organ 
_entity_src_gen.host_org_species 
_entity_src_gen.pdbx_host_org_tissue 
_entity_src_gen.pdbx_host_org_tissue_fraction 
_entity_src_gen.pdbx_host_org_strain 
_entity_src_gen.pdbx_host_org_variant 
_entity_src_gen.pdbx_host_org_cell_line 
_entity_src_gen.pdbx_host_org_atcc 
_entity_src_gen.pdbx_host_org_culture_collection 
_entity_src_gen.pdbx_host_org_cell 
_entity_src_gen.pdbx_host_org_organelle 
_entity_src_gen.pdbx_host_org_cellular_location 
_entity_src_gen.pdbx_host_org_vector_type 
_entity_src_gen.pdbx_host_org_vector 
_entity_src_gen.host_org_details 
_entity_src_gen.expression_system_id 
_entity_src_gen.plasmid_name 
_entity_src_gen.plasmid_details 
_entity_src_gen.pdbx_description 
1 1 sample 'Biological sequence' 1 46  ? ? ? ? ? ? ? ? ? 'Zika virus' 64320 ? ? ? ? ? ? ? ? 'Escherichia coli' 562 ? ? ? ? ? ? ? ? 
? ? ? ? ? ? ? ? ? ? ? ? ? 
2 1 sample 'Biological sequence' 1 168 ? ? ? ? ? ? ? ? ? 'Zika virus' 64320 ? ? ? ? ? ? ? ? 'Escherichia coli' 562 ? ? ? ? ? ? ? ? 
? ? ? ? ? ? ? ? ? ? ? ? ? 
# 
loop_
_chem_comp.id 
_chem_comp.type 
_chem_comp.mon_nstd_flag 
_chem_comp.name 
_chem_comp.pdbx_synonyms 
_chem_comp.formula 
_chem_comp.formula_weight 
A1BGY non-polymer         . '5-cyclopropyl-1,2-dimethyl-N-(3-methylpyridin-4-yl)-1H-pyrrole-3-carboxamide' ? 'C16 H19 N3 O'   
269.342 
ALA   'L-peptide linking' y ALANINE                                                                        ? 'C3 H7 N O2'     
89.093  
ARG   'L-peptide linking' y ARGININE                                                                       ? 'C6 H15 N4 O2 1' 
175.209 
ASN   'L-peptide linking' y ASPARAGINE                                                                     ? 'C4 H8 N2 O3'    
132.118 
ASP   'L-peptide linking' y 'ASPARTIC ACID'                                                                ? 'C4 H7 N O4'     
133.103 
CYS   'L-peptide linking' y CYSTEINE                                                                       ? 'C3 H7 N O2 S'   
121.158 
DMS   non-polymer         . 'DIMETHYL SULFOXIDE'                                                           ? 'C2 H6 O S'      
78.133  
GLN   'L-peptide linking' y GLUTAMINE                                                                      ? 'C5 H10 N2 O3'   
146.144 
GLU   'L-peptide linking' y 'GLUTAMIC ACID'                                                                ? 'C5 H9 N O4'     
147.129 
GLY   'peptide linking'   y GLYCINE                                                                        ? 'C2 H5 N O2'     
75.067  
HIS   'L-peptide linking' y HISTIDINE                                                                      ? 'C6 H10 N3 O2 1' 
156.162 
HOH   non-polymer         . WATER                                                                          ? 'H2 O'           
18.015  
ILE   'L-peptide linking' y ISOLEUCINE                                                                     ? 'C6 H13 N O2'    
131.173 
LEU   'L-peptide linking' y LEUCINE                                                                        ? 'C6 H13 N O2'    
131.173 
LYS   'L-peptide linking' y LYSINE                                                                         ? 'C6 H15 N2 O2 1' 
147.195 
MET   'L-peptide linking' y METHIONINE                                                                     ? 'C5 H11 N O2 S'  
149.211 
PHE   'L-peptide linking' y PHENYLALANINE                                                                  ? 'C9 H11 N O2'    
165.189 
PRO   'L-peptide linking' y PROLINE                                                                        ? 'C5 H9 N O2'     
115.130 
SER   'L-peptide linking' y SERINE                                                                         ? 'C3 H7 N O3'     
105.093 
SO4   non-polymer         . 'SULFATE ION'                                                                  ? 'O4 S -2'        
96.063  
THR   'L-peptide linking' y THREONINE                                                                      ? 'C4 H9 N O3'     
119.119 
TRP   'L-peptide linking' y TRYPTOPHAN                                                                     ? 'C11 H12 N2 O2'  
204.225 
TYR   'L-peptide linking' y TYROSINE                                                                       ? 'C9 H11 N O3'    
181.189 
VAL   'L-peptide linking' y VALINE                                                                         ? 'C5 H11 N O2'    
117.146 
# 
loop_
_pdbx_poly_seq_scheme.asym_id 
_pdbx_poly_seq_scheme.entity_id 
_pdbx_poly_seq_scheme.seq_id 
_pdbx_poly_seq_scheme.mon_id 
_pdbx_poly_seq_scheme.ndb_seq_num 
_pdbx_poly_seq_scheme.pdb_seq_num 
_pdbx_poly_seq_scheme.auth_seq_num 
_pdbx_poly_seq_scheme.pdb_mon_id 
_pdbx_poly_seq_scheme.auth_mon_id 
_pdbx_poly_seq_scheme.pdb_strand_id 
_pdbx_poly_seq_scheme.pdb_ins_code 
_pdbx_poly_seq_scheme.hetero 
A 1 1   SER 1   44  ?   ?   ?   A . n 
A 1 2   MET 2   45  ?   ?   ?   A . n 
A 1 3   GLY 3   46  ?   ?   ?   A . n 
A 1 4   LYS 4   47  ?   ?   ?   A . n 
A 1 5   SER 5   48  ?   ?   ?   A . n 
A 1 6   VAL 6   49  ?   ?   ?   A . n 
A 1 7   ASP 7   50  50  ASP ASP A . n 
A 1 8   MET 8   51  51  MET MET A . n 
A 1 9   TYR 9   52  52  TYR TYR A . n 
A 1 10  ILE 10  53  53  ILE ILE A . n 
A 1 11  GLU 11  54  54  GLU GLU A . n 
A 1 12  ARG 12  55  55  ARG ARG A . n 
A 1 13  ALA 13  56  56  ALA ALA A . n 
A 1 14  GLY 14  57  57  GLY GLY A . n 
A 1 15  ASP 15  58  58  ASP ASP A . n 
A 1 16  ILE 16  59  59  ILE ILE A . n 
A 1 17  THR 17  60  60  THR THR A . n 
A 1 18  TRP 18  61  61  TRP TRP A . n 
A 1 19  GLU 19  62  62  GLU GLU A . n 
A 1 20  LYS 20  63  63  LYS LYS A . n 
A 1 21  ASP 21  64  64  ASP ASP A . n 
A 1 22  ALA 22  65  65  ALA ALA A . n 
A 1 23  GLU 23  66  66  GLU GLU A . n 
A 1 24  VAL 24  67  67  VAL VAL A . n 
A 1 25  THR 25  68  68  THR THR A . n 
A 1 26  GLY 26  69  69  GLY GLY A . n 
A 1 27  ASN 27  70  70  ASN ASN A . n 
A 1 28  SER 28  71  71  SER SER A . n 
A 1 29  PRO 29  72  72  PRO PRO A . n 
A 1 30  ARG 30  73  73  ARG ARG A . n 
A 1 31  LEU 31  74  74  LEU LEU A . n 
A 1 32  ASP 32  75  75  ASP ASP A . n 
A 1 33  VAL 33  76  76  VAL VAL A . n 
A 1 34  ALA 34  77  77  ALA ALA A . n 
A 1 35  LEU 35  78  78  LEU LEU A . n 
A 1 36  ASP 36  79  79  ASP ASP A . n 
A 1 37  GLU 37  80  80  GLU GLU A . n 
A 1 38  SER 38  81  81  SER SER A . n 
A 1 39  GLY 39  82  82  GLY GLY A . n 
A 1 40  ASP 40  83  83  ASP ASP A . n 
A 1 41  PHE 41  84  84  PHE PHE A . n 
A 1 42  SER 42  85  85  SER SER A . n 
A 1 43  LEU 43  86  86  LEU LEU A . n 
A 1 44  VAL 44  87  87  VAL VAL A . n 
A 1 45  GLU 45  88  88  GLU GLU A . n 
A 1 46  GLU 46  89  ?   ?   ?   A . n 
B 2 1   MET 1   10  ?   ?   ?   B . n 
B 2 2   LYS 2   11  ?   ?   ?   B . n 
B 2 3   GLU 3   12  ?   ?   ?   B . n 
B 2 4   VAL 4   13  ?   ?   ?   B . n 
B 2 5   LYS 5   14  ?   ?   ?   B . n 
B 2 6   LYS 6   15  ?   ?   ?   B . n 
B 2 7   GLY 7   16  16  GLY GLY B . n 
B 2 8   GLU 8   17  17  GLU GLU B . n 
B 2 9   THR 9   18  18  THR THR B . n 
B 2 10  THR 10  19  19  THR THR B . n 
B 2 11  ASP 11  20  20  ASP ASP B . n 
B 2 12  GLY 12  21  21  GLY GLY B . n 
B 2 13  VAL 13  22  22  VAL VAL B . n 
B 2 14  TYR 14  23  23  TYR TYR B . n 
B 2 15  ARG 15  24  24  ARG ARG B . n 
B 2 16  VAL 16  25  25  VAL VAL B . n 
B 2 17  MET 17  26  26  MET MET B . n 
B 2 18  THR 18  27  27  THR THR B . n 
B 2 19  ARG 19  28  28  ARG ARG B . n 
B 2 20  ARG 20  29  29  ARG ARG B . n 
B 2 21  LEU 21  30  30  LEU LEU B . n 
B 2 22  LEU 22  31  31  LEU LEU B . n 
B 2 23  GLY 23  32  32  GLY GLY B . n 
B 2 24  SER 24  33  33  SER SER B . n 
B 2 25  THR 25  34  34  THR THR B . n 
B 2 26  GLN 26  35  35  GLN GLN B . n 
B 2 27  VAL 27  36  36  VAL VAL B . n 
B 2 28  GLY 28  37  37  GLY GLY B . n 
B 2 29  VAL 29  38  38  VAL VAL B . n 
B 2 30  GLY 30  39  39  GLY GLY B . n 
B 2 31  VAL 31  40  40  VAL VAL B . n 
B 2 32  MET 32  41  41  MET MET B . n 
B 2 33  GLN 33  42  42  GLN GLN B . n 
B 2 34  GLU 34  43  43  GLU GLU B . n 
B 2 35  GLY 35  44  44  GLY GLY B . n 
B 2 36  VAL 36  45  45  VAL VAL B . n 
B 2 37  PHE 37  46  46  PHE PHE B . n 
B 2 38  HIS 38  47  47  HIS HIS B . n 
B 2 39  THR 39  48  48  THR THR B . n 
B 2 40  MET 40  49  49  MET MET B . n 
B 2 41  TRP 41  50  50  TRP TRP B . n 
B 2 42  HIS 42  51  51  HIS HIS B . n 
B 2 43  VAL 43  52  52  VAL VAL B . n 
B 2 44  THR 44  53  53  THR THR B . n 
B 2 45  LYS 45  54  54  LYS LYS B . n 
B 2 46  GLY 46  55  55  GLY GLY B . n 
B 2 47  ALA 47  56  56  ALA ALA B . n 
B 2 48  ALA 48  57  57  ALA ALA B . n 
B 2 49  LEU 49  58  58  LEU LEU B . n 
B 2 50  ARG 50  59  59  ARG ARG B . n 
B 2 51  SER 51  60  60  SER SER B . n 
B 2 52  GLY 52  61  61  GLY GLY B . n 
B 2 53  GLU 53  62  62  GLU GLU B . n 
B 2 54  GLY 54  63  63  GLY GLY B . n 
B 2 55  ARG 55  64  64  ARG ARG B . n 
B 2 56  LEU 56  65  65  LEU LEU B . n 
B 2 57  ASP 57  66  66  ASP ASP B . n 
B 2 58  PRO 58  67  67  PRO PRO B . n 
B 2 59  TYR 59  68  68  TYR TYR B . n 
B 2 60  TRP 60  69  69  TRP TRP B . n 
B 2 61  GLY 61  70  70  GLY GLY B . n 
B 2 62  ASP 62  71  71  ASP ASP B . n 
B 2 63  VAL 63  72  72  VAL VAL B . n 
B 2 64  LYS 64  73  73  LYS LYS B . n 
B 2 65  GLN 65  74  74  GLN GLN B . n 
B 2 66  ASP 66  75  75  ASP ASP B . n 
B 2 67  LEU 67  76  76  LEU LEU B . n 
B 2 68  VAL 68  77  77  VAL VAL B . n 
B 2 69  SER 69  78  78  SER SER B . n 
B 2 70  TYR 70  79  79  TYR TYR B . n 
B 2 71  CYS 71  80  80  CYS CYS B . n 
B 2 72  GLY 72  81  81  GLY GLY B . n 
B 2 73  PRO 73  82  82  PRO PRO B . n 
B 2 74  TRP 74  83  83  TRP TRP B . n 
B 2 75  LYS 75  84  84  LYS LYS B . n 
B 2 76  LEU 76  85  85  LEU LEU B . n 
B 2 77  ASP 77  86  86  ASP ASP B . n 
B 2 78  ALA 78  87  87  ALA ALA B . n 
B 2 79  ALA 79  88  88  ALA ALA B . n 
B 2 80  TRP 80  89  89  TRP TRP B . n 
B 2 81  ASP 81  90  90  ASP ASP B . n 
B 2 82  GLY 82  91  91  GLY GLY B . n 
B 2 83  LEU 83  92  92  LEU LEU B . n 
B 2 84  SER 84  93  93  SER SER B . n 
B 2 85  GLU 85  94  94  GLU GLU B . n 
B 2 86  VAL 86  95  95  VAL VAL B . n 
B 2 87  GLN 87  96  96  GLN GLN B . n 
B 2 88  LEU 88  97  97  LEU LEU B . n 
B 2 89  LEU 89  98  98  LEU LEU B . n 
B 2 90  ALA 90  99  99  ALA ALA B . n 
B 2 91  VAL 91  100 100 VAL VAL B . n 
B 2 92  PRO 92  101 101 PRO PRO B . n 
B 2 93  PRO 93  102 102 PRO PRO B . n 
B 2 94  GLY 94  103 103 GLY GLY B . n 
B 2 95  GLU 95  104 104 GLU GLU B . n 
B 2 96  ARG 96  105 105 ARG ARG B . n 
B 2 97  ALA 97  106 106 ALA ALA B . n 
B 2 98  LYS 98  107 107 LYS LYS B . n 
B 2 99  ASN 99  108 108 ASN ASN B . n 
B 2 100 ILE 100 109 109 ILE ILE B . n 
B 2 101 GLN 101 110 110 GLN GLN B . n 
B 2 102 THR 102 111 111 THR THR B . n 
B 2 103 LEU 103 112 112 LEU LEU B . n 
B 2 104 PRO 104 113 113 PRO PRO B . n 
B 2 105 GLY 105 114 114 GLY GLY B . n 
B 2 106 ILE 106 115 115 ILE ILE B . n 
B 2 107 PHE 107 116 116 PHE PHE B . n 
B 2 108 LYS 108 117 117 LYS LYS B . n 
B 2 109 THR 109 118 118 THR THR B . n 
B 2 110 LYS 110 119 119 LYS LYS B . n 
B 2 111 ASP 111 120 120 ASP ASP B . n 
B 2 112 GLY 112 121 121 GLY GLY B . n 
B 2 113 ASP 113 122 122 ASP ASP B . n 
B 2 114 ILE 114 123 123 ILE ILE B . n 
B 2 115 GLY 115 124 124 GLY GLY B . n 
B 2 116 ALA 116 125 125 ALA ALA B . n 
B 2 117 VAL 117 126 126 VAL VAL B . n 
B 2 118 ALA 118 127 127 ALA ALA B . n 
B 2 119 LEU 119 128 128 LEU LEU B . n 
B 2 120 ASP 120 129 129 ASP ASP B . n 
B 2 121 TYR 121 130 130 TYR TYR B . n 
B 2 122 PRO 122 131 131 PRO PRO B . n 
B 2 123 ALA 123 132 132 ALA ALA B . n 
B 2 124 GLY 124 133 133 GLY GLY B . n 
B 2 125 THR 125 134 134 THR THR B . n 
B 2 126 SER 126 135 135 SER SER B . n 
B 2 127 GLY 127 136 136 GLY GLY B . n 
B 2 128 SER 128 137 137 SER SER B . n 
B 2 129 PRO 129 138 138 PRO PRO B . n 
B 2 130 ILE 130 139 139 ILE ILE B . n 
B 2 131 LEU 131 140 140 LEU LEU B . n 
B 2 132 ASP 132 141 141 ASP ASP B . n 
B 2 133 LYS 133 142 142 LYS LYS B . n 
B 2 134 CYS 134 143 143 CYS CYS B . n 
B 2 135 GLY 135 144 144 GLY GLY B . n 
B 2 136 ARG 136 145 145 ARG ARG B . n 
B 2 137 VAL 137 146 146 VAL VAL B . n 
B 2 138 ILE 138 147 147 ILE ILE B . n 
B 2 139 GLY 139 148 148 GLY GLY B . n 
B 2 140 LEU 140 149 149 LEU LEU B . n 
B 2 141 TYR 141 150 150 TYR TYR B . n 
B 2 142 GLY 142 151 151 GLY GLY B . n 
B 2 143 ASN 143 152 152 ASN ASN B . n 
B 2 144 GLY 144 153 153 GLY GLY B . n 
B 2 145 VAL 145 154 154 VAL VAL B . n 
B 2 146 VAL 146 155 155 VAL VAL B . n 
B 2 147 ILE 147 156 156 ILE ILE B . n 
B 2 148 LYS 148 157 157 LYS LYS B . n 
B 2 149 ASN 149 158 158 ASN ASN B . n 
B 2 150 GLY 150 159 159 GLY GLY B . n 
B 2 151 SER 151 160 160 SER SER B . n 
B 2 152 TYR 152 161 161 TYR TYR B . n 
B 2 153 VAL 153 162 162 VAL VAL B . n 
B 2 154 SER 154 163 163 SER SER B . n 
B 2 155 ALA 155 164 164 ALA ALA B . n 
B 2 156 ILE 156 165 165 ILE ILE B . n 
B 2 157 THR 157 166 166 THR THR B . n 
B 2 158 GLN 158 167 167 GLN GLN B . n 
B 2 159 GLY 159 168 168 GLY GLY B . n 
B 2 160 LYS 160 169 169 LYS LYS B . n 
B 2 161 ARG 161 170 170 ARG ARG B . n 
B 2 162 GLU 162 171 171 GLU GLU B . n 
B 2 163 GLU 163 172 ?   ?   ?   B . n 
B 2 164 GLU 164 173 ?   ?   ?   B . n 
B 2 165 THR 165 174 ?   ?   ?   B . n 
B 2 166 PRO 166 175 ?   ?   ?   B . n 
B 2 167 VAL 167 176 ?   ?   ?   B . n 
B 2 168 GLU 168 177 ?   ?   ?   B . n 
# 
_pdbx_entity_instance_feature.ordinal        1 
_pdbx_entity_instance_feature.comp_id        A1BGY 
_pdbx_entity_instance_feature.asym_id        ? 
_pdbx_entity_instance_feature.seq_num        ? 
_pdbx_entity_instance_feature.auth_comp_id   A1BGY 
_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 A1BGY 1  204 301 A1BGY LIG B . 
G 5 SO4   1  205 302 SO4   SO4 B . 
H 6 HOH   1  101 105 HOH   HOH A . 
H 6 HOH   2  102 98  HOH   HOH A . 
H 6 HOH   3  103 48  HOH   HOH A . 
H 6 HOH   4  104 54  HOH   HOH A . 
H 6 HOH   5  105 20  HOH   HOH A . 
H 6 HOH   6  106 34  HOH   HOH A . 
H 6 HOH   7  107 127 HOH   HOH A . 
H 6 HOH   8  108 121 HOH   HOH A . 
H 6 HOH   9  109 118 HOH   HOH A . 
H 6 HOH   10 110 117 HOH   HOH A . 
H 6 HOH   11 111 65  HOH   HOH A . 
H 6 HOH   12 112 70  HOH   HOH A . 
H 6 HOH   13 113 110 HOH   HOH A . 
H 6 HOH   14 114 49  HOH   HOH A . 
H 6 HOH   15 115 16  HOH   HOH A . 
H 6 HOH   16 116 40  HOH   HOH A . 
H 6 HOH   17 117 120 HOH   HOH A . 
H 6 HOH   18 118 29  HOH   HOH A . 
H 6 HOH   19 119 50  HOH   HOH A . 
H 6 HOH   20 120 119 HOH   HOH A . 
H 6 HOH   21 121 128 HOH   HOH A . 
H 6 HOH   22 122 77  HOH   HOH A . 
H 6 HOH   23 123 27  HOH   HOH A . 
H 6 HOH   24 124 85  HOH   HOH A . 
I 6 HOH   1  301 11  HOH   HOH B . 
I 6 HOH   2  302 57  HOH   HOH B . 
I 6 HOH   3  303 92  HOH   HOH B . 
I 6 HOH   4  304 51  HOH   HOH B . 
I 6 HOH   5  305 90  HOH   HOH B . 
I 6 HOH   6  306 14  HOH   HOH B . 
I 6 HOH   7  307 58  HOH   HOH B . 
I 6 HOH   8  308 5   HOH   HOH B . 
I 6 HOH   9  309 1   HOH   HOH B . 
I 6 HOH   10 310 131 HOH   HOH B . 
I 6 HOH   11 311 31  HOH   HOH B . 
I 6 HOH   12 312 106 HOH   HOH B . 
I 6 HOH   13 313 81  HOH   HOH B . 
I 6 HOH   14 314 89  HOH   HOH B . 
I 6 HOH   15 315 64  HOH   HOH B . 
I 6 HOH   16 316 115 HOH   HOH B . 
I 6 HOH   17 317 123 HOH   HOH B . 
I 6 HOH   18 318 23  HOH   HOH B . 
I 6 HOH   19 319 132 HOH   HOH B . 
I 6 HOH   20 320 108 HOH   HOH B . 
I 6 HOH   21 321 63  HOH   HOH B . 
I 6 HOH   22 322 56  HOH   HOH B . 
I 6 HOH   23 323 2   HOH   HOH B . 
I 6 HOH   24 324 24  HOH   HOH B . 
I 6 HOH   25 325 46  HOH   HOH B . 
I 6 HOH   26 326 124 HOH   HOH B . 
I 6 HOH   27 327 68  HOH   HOH B . 
I 6 HOH   28 328 67  HOH   HOH B . 
I 6 HOH   29 329 69  HOH   HOH B . 
I 6 HOH   30 330 32  HOH   HOH B . 
I 6 HOH   31 331 36  HOH   HOH B . 
I 6 HOH   32 332 100 HOH   HOH B . 
I 6 HOH   33 333 4   HOH   HOH B . 
I 6 HOH   34 334 13  HOH   HOH B . 
I 6 HOH   35 335 35  HOH   HOH B . 
I 6 HOH   36 336 30  HOH   HOH B . 
I 6 HOH   37 337 130 HOH   HOH B . 
I 6 HOH   38 338 60  HOH   HOH B . 
I 6 HOH   39 339 42  HOH   HOH B . 
I 6 HOH   40 340 62  HOH   HOH B . 
I 6 HOH   41 341 72  HOH   HOH B . 
I 6 HOH   42 342 66  HOH   HOH B . 
I 6 HOH   43 343 21  HOH   HOH B . 
I 6 HOH   44 344 28  HOH   HOH B . 
I 6 HOH   45 345 107 HOH   HOH B . 
I 6 HOH   46 346 39  HOH   HOH B . 
I 6 HOH   47 347 102 HOH   HOH B . 
I 6 HOH   48 348 116 HOH   HOH B . 
I 6 HOH   49 349 10  HOH   HOH B . 
I 6 HOH   50 350 17  HOH   HOH B . 
I 6 HOH   51 351 82  HOH   HOH B . 
I 6 HOH   52 352 12  HOH   HOH B . 
I 6 HOH   53 353 103 HOH   HOH B . 
I 6 HOH   54 354 3   HOH   HOH B . 
I 6 HOH   55 355 122 HOH   HOH B . 
I 6 HOH   56 356 9   HOH   HOH B . 
I 6 HOH   57 357 87  HOH   HOH B . 
I 6 HOH   58 358 43  HOH   HOH B . 
I 6 HOH   59 359 94  HOH   HOH B . 
I 6 HOH   60 360 73  HOH   HOH B . 
I 6 HOH   61 361 18  HOH   HOH B . 
I 6 HOH   62 362 112 HOH   HOH B . 
I 6 HOH   63 363 126 HOH   HOH B . 
I 6 HOH   64 364 26  HOH   HOH B . 
I 6 HOH   65 365 125 HOH   HOH B . 
I 6 HOH   66 366 83  HOH   HOH B . 
I 6 HOH   67 367 109 HOH   HOH B . 
I 6 HOH   68 368 45  HOH   HOH B . 
I 6 HOH   69 369 79  HOH   HOH B . 
I 6 HOH   70 370 80  HOH   HOH B . 
I 6 HOH   71 371 61  HOH   HOH B . 
I 6 HOH   72 372 59  HOH   HOH B . 
I 6 HOH   73 373 75  HOH   HOH B . 
I 6 HOH   74 374 44  HOH   HOH B . 
# 
loop_
_software.classification 
_software.name 
_software.version 
_software.citation_id 
_software.pdbx_ordinal 
refinement       REFMAC  5.8.0267 ? 1 
refinement       BUSTER  .        ? 2 
'data scaling'   Aimless .        ? 3 
phasing          PHASER  .        ? 4 
'data reduction' XDS     .        ? 5 
'data reduction' XDS     .        ? 6 
'data reduction' XDS     .        ? 7 
'data reduction' XDS     .        ? 8 
'data reduction' XDS     .        ? 9 
# 
_cell.entry_id           7HOS 
_cell.length_a           42.447 
_cell.length_b           42.447 
_cell.length_c           216.891 
_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                         7HOS 
_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          7HOS 
_exptl.method            'X-RAY DIFFRACTION' 
_exptl.crystals_number   1 
# 
_exptl_crystal.id                    1 
_exptl_crystal.density_meas          ? 
_exptl_crystal.density_Matthews      2.11 
_exptl_crystal.density_percent_sol   41.62 
_exptl_crystal.description           ? 
# 
_exptl_crystal_grow.crystal_id      1 
_exptl_crystal_grow.method          'VAPOR DIFFUSION, SITTING DROP' 
_exptl_crystal_grow.pH              4.8 
_exptl_crystal_grow.temp            298 
_exptl_crystal_grow.pdbx_details    '30% w/v PEG 2000, 0.2M Ammonium sulfate, 0.1M acetate (pH 4.8)' 
_exptl_crystal_grow.temp_details    ? 
_exptl_crystal_grow.pdbx_pH_range   ? 
# 
_diffrn.id                     1 
_diffrn.ambient_temp           100 
_diffrn.crystal_id             1 
_diffrn.ambient_temp_details   ? 
# 
_diffrn_detector.detector               PIXEL 
_diffrn_detector.type                   'DECTRIS EIGER2 XE 9M' 
_diffrn_detector.pdbx_collection_date   2023-09-19 
_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                     7HOS 
_reflns.pdbx_diffrn_id               1 
_reflns.pdbx_ordinal                 1 
_reflns.d_resolution_low             216.97 
_reflns.d_resolution_high            1.60 
_reflns.number_obs                   27569 
_reflns.percent_possible_obs         99.9 
_reflns.pdbx_Rmerge_I_obs            0.126 
_reflns.pdbx_netI_over_sigmaI        8.4 
_reflns.pdbx_redundancy              25.5 
_reflns.pdbx_Rrim_I_all              0.129 
_reflns.pdbx_Rpim_I_all              0.025 
_reflns.pdbx_CC_half                 0.999 
_reflns.pdbx_number_measured_all     701634 
_reflns.pdbx_chi_squared             0.21 
_reflns.observed_criterion_sigma_I   ? 
_reflns.observed_criterion_sigma_F   ? 
_reflns.number_all                   ? 
_reflns.pdbx_Rsym_value              ? 
_reflns.B_iso_Wilson_estimate        ? 
# 
_reflns_shell.pdbx_diffrn_id              1 
_reflns_shell.pdbx_ordinal                1 
_reflns_shell.d_res_high                  1.60 
_reflns_shell.d_res_low                   1.63 
_reflns_shell.number_measured_all         33016 
_reflns_shell.number_unique_obs           1374 
_reflns_shell.Rmerge_I_obs                7.948 
_reflns_shell.pdbx_chi_squared            0.05 
_reflns_shell.pdbx_redundancy             24.0 
_reflns_shell.percent_possible_obs        98.0 
_reflns_shell.pdbx_netI_over_sigmaI_obs   0.1 
_reflns_shell.pdbx_Rrim_I_all             8.119 
_reflns_shell.pdbx_Rpim_I_all             1.644 
_reflns_shell.pdbx_CC_half                0.346 
_reflns_shell.percent_possible_all        ? 
_reflns_shell.pdbx_Rsym_value             ? 
_reflns_shell.meanI_over_sigI_obs         ? 
# 
_refine.pdbx_refine_id                           'X-RAY DIFFRACTION' 
_refine.entry_id                                 7HOS 
_refine.pdbx_diffrn_id                           1 
_refine.pdbx_TLS_residual_ADP_flag               ? 
_refine.ls_number_reflns_obs                     21998 
_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                             54.22 
_refine.ls_d_res_high                            1.60 
_refine.ls_percent_reflns_obs                    84.57 
_refine.ls_R_factor_obs                          0.24488 
_refine.ls_R_factor_all                          ? 
_refine.ls_R_factor_R_work                       0.24241 
_refine.ls_R_factor_R_free                       0.29170 
_refine.ls_R_factor_R_free_error                 ? 
_refine.ls_R_factor_R_free_error_details         ? 
_refine.ls_percent_reflns_R_free                 5.1 
_refine.ls_number_reflns_R_free                  1178 
_refine.ls_number_parameters                     ? 
_refine.ls_number_restraints                     ? 
_refine.occupancy_min                            ? 
_refine.occupancy_max                            ? 
_refine.correlation_coeff_Fo_to_Fc               0.961 
_refine.correlation_coeff_Fo_to_Fc_free          0.946 
_refine.B_iso_mean                               45.656 
_refine.aniso_B[1][1]                            1.50 
_refine.aniso_B[2][2]                            1.50 
_refine.aniso_B[3][3]                            -3.00 
_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                       0.150 
_refine.pdbx_overall_ESU_R_Free                  0.147 
_refine.overall_SU_ML                            0.228 
_refine.pdbx_overall_phase_error                 ? 
_refine.overall_SU_B                             7.986 
_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         37 
_refine_hist.number_atoms_solvent             98 
_refine_hist.number_atoms_total               1611 
_refine_hist.d_res_high                       1.60 
_refine_hist.d_res_low                        54.22 
# 
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             0.007  0.013  ? 2014 'X-RAY DIFFRACTION' ? 
r_bond_other_d               0.001  0.015  ? 1667 'X-RAY DIFFRACTION' ? 
r_angle_refined_deg          1.483  1.640  ? 2498 'X-RAY DIFFRACTION' ? 
r_angle_other_deg            1.208  1.583  ? 3844 'X-RAY DIFFRACTION' ? 
r_dihedral_angle_1_deg       7.916  5.000  ? 238  'X-RAY DIFFRACTION' ? 
r_dihedral_angle_2_deg       30.515 22.410 ? 83   'X-RAY DIFFRACTION' ? 
r_dihedral_angle_3_deg       15.061 15.000 ? 274  'X-RAY DIFFRACTION' ? 
r_dihedral_angle_4_deg       19.343 15.000 ? 10   'X-RAY DIFFRACTION' ? 
r_chiral_restr               0.060  0.200  ? 221  'X-RAY DIFFRACTION' ? 
r_gen_planes_refined         0.006  0.020  ? 2145 'X-RAY DIFFRACTION' ? 
r_gen_planes_other           0.002  0.020  ? 417  'X-RAY DIFFRACTION' ? 
r_nbd_refined                ?      ?      ? ?    'X-RAY DIFFRACTION' ? 
r_nbd_other                  ?      ?      ? ?    'X-RAY DIFFRACTION' ? 
r_nbtor_refined              ?      ?      ? ?    'X-RAY DIFFRACTION' ? 
r_nbtor_other                ?      ?      ? ?    'X-RAY DIFFRACTION' ? 
r_xyhbond_nbd_refined        ?      ?      ? ?    'X-RAY DIFFRACTION' ? 
r_xyhbond_nbd_other          ?      ?      ? ?    'X-RAY DIFFRACTION' ? 
r_metal_ion_refined          ?      ?      ? ?    'X-RAY DIFFRACTION' ? 
r_metal_ion_other            ?      ?      ? ?    'X-RAY DIFFRACTION' ? 
r_symmetry_vdw_refined       ?      ?      ? ?    'X-RAY DIFFRACTION' ? 
r_symmetry_vdw_other         ?      ?      ? ?    'X-RAY DIFFRACTION' ? 
r_symmetry_hbond_refined     ?      ?      ? ?    'X-RAY DIFFRACTION' ? 
r_symmetry_hbond_other       ?      ?      ? ?    'X-RAY DIFFRACTION' ? 
r_symmetry_metal_ion_refined ?      ?      ? ?    'X-RAY DIFFRACTION' ? 
r_symmetry_metal_ion_other   ?      ?      ? ?    'X-RAY DIFFRACTION' ? 
r_mcbond_it                  3.145  4.316  ? 987  'X-RAY DIFFRACTION' ? 
r_mcbond_other               3.181  4.248  ? 962  'X-RAY DIFFRACTION' ? 
r_mcangle_it                 4.840  6.336  ? 1152 'X-RAY DIFFRACTION' ? 
r_mcangle_other              4.838  6.340  ? 1153 'X-RAY DIFFRACTION' ? 
r_scbond_it                  3.397  5.198  ? 1027 'X-RAY DIFFRACTION' ? 
r_scbond_other               3.414  5.139  ? 1015 'X-RAY DIFFRACTION' ? 
r_scangle_it                 ?      ?      ? ?    'X-RAY DIFFRACTION' ? 
r_scangle_other              5.627  7.166  ? 1329 'X-RAY DIFFRACTION' ? 
r_long_range_B_refined       18.342 48.489 ? 2046 'X-RAY DIFFRACTION' ? 
r_long_range_B_other         18.373 48.354 ? 2028 '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                       1.602 
_refine_ls_shell.d_res_low                        1.644 
_refine_ls_shell.number_reflns_R_work             109 
_refine_ls_shell.R_factor_R_work                  0.640 
_refine_ls_shell.percent_reflns_obs               5.78 
_refine_ls_shell.R_factor_R_free                  0.594 
_refine_ls_shell.R_factor_R_free_error            ? 
_refine_ls_shell.percent_reflns_R_free            ? 
_refine_ls_shell.number_reflns_R_free             5 
_refine_ls_shell.number_reflns_all                ? 
_refine_ls_shell.R_factor_all                     ? 
# 
_struct.entry_id                  7HOS 
_struct.title                     
'PanDDA analysis group deposition -- Crystal Structure of ZIKV NS2B-NS3 protease in complex with ASAP-0014657-001' 
_struct.pdbx_model_details        ? 
_struct.pdbx_CASP_flag            ? 
_struct.pdbx_model_type_details   ? 
# 
_struct_keywords.entry_id        7HOS 
_struct_keywords.pdbx_keywords   'VIRAL PROTEIN' 
_struct_keywords.text            'SGC - Diamond I04-1, PanDDA, XChemExplorer, VIRAL PROTEIN' 
# 
loop_
_struct_asym.id 
_struct_asym.pdbx_blank_PDB_chainid_flag 
_struct_asym.pdbx_modified 
_struct_asym.entity_id 
_struct_asym.details 
A N N 1 ? 
B N N 2 ? 
C N N 3 ? 
D N N 3 ? 
E N N 3 ? 
F N N 4 ? 
G N N 5 ? 
H N N 6 ? 
I N N 6 ? 
# 
loop_
_struct_ref.id 
_struct_ref.db_name 
_struct_ref.db_code 
_struct_ref.pdbx_db_accession 
_struct_ref.pdbx_db_isoform 
_struct_ref.entity_id 
_struct_ref.pdbx_seq_one_letter_code 
_struct_ref.pdbx_align_begin 
1 UNP POLG_ZIKV Q32ZE1 ? 1 GKSVDMYIERAGDITWEKDAEVTGNSPRLDVALDESGDFSLVEE 1414 
2 UNP POLG_ZIKV Q32ZE1 ? 2 
;KEVKKGETTDGVYRVMTRRLLGSTQVGVGVMQEGVFHTMWHVTKGAALRSGEGRLDPYWGDVKQDLVSYCGPWKLDAAWD
GLSEVQLLAVPPGERARNIQTLPGIFKTKDGDIGAVALDYPAGTSGSPILDKCGRVIGLYGNGVVIKNGSYVSAITQGKR
EEETPVE
;
1509 
# 
loop_
_struct_ref_seq.align_id 
_struct_ref_seq.ref_id 
_struct_ref_seq.pdbx_PDB_id_code 
_struct_ref_seq.pdbx_strand_id 
_struct_ref_seq.seq_align_beg 
_struct_ref_seq.pdbx_seq_align_beg_ins_code 
_struct_ref_seq.seq_align_end 
_struct_ref_seq.pdbx_seq_align_end_ins_code 
_struct_ref_seq.pdbx_db_accession 
_struct_ref_seq.db_align_beg 
_struct_ref_seq.pdbx_db_align_beg_ins_code 
_struct_ref_seq.db_align_end 
_struct_ref_seq.pdbx_db_align_end_ins_code 
_struct_ref_seq.pdbx_auth_seq_align_beg 
_struct_ref_seq.pdbx_auth_seq_align_end 
1 1 7HOS A 3 ? 46  ? Q32ZE1 1414 ? 1457 ? 46 89  
2 2 7HOS 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 7HOS SER A 1  ? UNP Q32ZE1 ?   ?    'expression tag'        44  1 
1 7HOS MET A 2  ? UNP Q32ZE1 ?   ?    'expression tag'        45  2 
2 7HOS MET B 1  ? UNP Q32ZE1 ?   ?    'initiating methionine' 10  3 
2 7HOS LYS B 98 ? UNP Q32ZE1 ARG 1605 conflict                107 4 
# 
_pdbx_struct_assembly.id                   1 
_pdbx_struct_assembly.details              software_defined_assembly 
_pdbx_struct_assembly.method_details       PISA 
_pdbx_struct_assembly.oligomeric_details   dimeric 
_pdbx_struct_assembly.oligomeric_count     2 
# 
loop_
_pdbx_struct_assembly_prop.biol_id 
_pdbx_struct_assembly_prop.type 
_pdbx_struct_assembly_prop.value 
_pdbx_struct_assembly_prop.details 
1 'ABSA (A^2)' 4700 ? 
1 MORE         -32  ? 
1 'SSA (A^2)'  9890 ? 
# 
_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   ? 
# 
loop_
_struct_sheet.id 
_struct_sheet.type 
_struct_sheet.number_strands 
_struct_sheet.details 
AA1 ? 8 ? 
AA2 ? 5 ? 
AA3 ? 6 ? 
# 
loop_
_struct_sheet_order.sheet_id 
_struct_sheet_order.range_id_1 
_struct_sheet_order.range_id_2 
_struct_sheet_order.offset 
_struct_sheet_order.sense 
AA1 1 2 ? anti-parallel 
AA1 2 3 ? parallel      
AA1 3 4 ? anti-parallel 
AA1 4 5 ? anti-parallel 
AA1 5 6 ? anti-parallel 
AA1 6 7 ? anti-parallel 
AA1 7 8 ? anti-parallel 
AA2 1 2 ? parallel      
AA2 2 3 ? anti-parallel 
AA2 3 4 ? anti-parallel 
AA2 4 5 ? anti-parallel 
AA3 1 2 ? anti-parallel 
AA3 2 3 ? parallel      
AA3 3 4 ? anti-parallel 
AA3 4 5 ? anti-parallel 
AA3 5 6 ? anti-parallel 
# 
loop_
_struct_sheet_range.sheet_id 
_struct_sheet_range.id 
_struct_sheet_range.beg_label_comp_id 
_struct_sheet_range.beg_label_asym_id 
_struct_sheet_range.beg_label_seq_id 
_struct_sheet_range.pdbx_beg_PDB_ins_code 
_struct_sheet_range.end_label_comp_id 
_struct_sheet_range.end_label_asym_id 
_struct_sheet_range.end_label_seq_id 
_struct_sheet_range.pdbx_end_PDB_ins_code 
_struct_sheet_range.beg_auth_comp_id 
_struct_sheet_range.beg_auth_asym_id 
_struct_sheet_range.beg_auth_seq_id 
_struct_sheet_range.end_auth_comp_id 
_struct_sheet_range.end_auth_asym_id 
_struct_sheet_range.end_auth_seq_id 
AA1 1 GLY B 54  ? LEU B 56  ? GLY B 63  LEU B 65  
AA1 2 LEU B 49  ? SER B 51  ? LEU B 58  SER B 60  
AA1 3 MET A 8   ? GLY A 14  ? MET A 51  GLY A 57  
AA1 4 GLY B 12  ? THR B 18  ? GLY B 21  THR B 27  
AA1 5 THR B 25  ? GLN B 33  ? THR B 34  GLN B 42  
AA1 6 VAL B 36  ? 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 GLU A 23  ? VAL A 24  ? GLU A 66  VAL A 67  
AA2 2 LYS B 98  ? THR B 102 ? LYS B 107 THR B 111 
AA2 3 VAL B 86  ? ALA B 90  ? VAL B 95  ALA B 99  
AA2 4 PRO B 129 ? LEU B 131 ? PRO B 138 LEU B 140 
AA2 5 VAL B 137 ? LEU B 140 ? VAL B 146 LEU B 149 
AA3 1 PHE A 41  ? LEU A 43  ? PHE A 84  LEU A 86  
AA3 2 ARG A 30  ? LEU A 35  ? ARG A 73  LEU A 78  
AA3 3 GLY B 105 ? THR B 109 ? GLY B 114 THR B 118 
AA3 4 GLY B 112 ? VAL B 117 ? GLY B 121 VAL B 126 
AA3 5 TYR B 152 ? ALA B 155 ? TYR B 161 ALA B 164 
AA3 6 GLY B 144 ? VAL B 146 ? GLY B 153 VAL B 155 
# 
loop_
_pdbx_struct_sheet_hbond.sheet_id 
_pdbx_struct_sheet_hbond.range_id_1 
_pdbx_struct_sheet_hbond.range_id_2 
_pdbx_struct_sheet_hbond.range_1_label_atom_id 
_pdbx_struct_sheet_hbond.range_1_label_comp_id 
_pdbx_struct_sheet_hbond.range_1_label_asym_id 
_pdbx_struct_sheet_hbond.range_1_label_seq_id 
_pdbx_struct_sheet_hbond.range_1_PDB_ins_code 
_pdbx_struct_sheet_hbond.range_1_auth_atom_id 
_pdbx_struct_sheet_hbond.range_1_auth_comp_id 
_pdbx_struct_sheet_hbond.range_1_auth_asym_id 
_pdbx_struct_sheet_hbond.range_1_auth_seq_id 
_pdbx_struct_sheet_hbond.range_2_label_atom_id 
_pdbx_struct_sheet_hbond.range_2_label_comp_id 
_pdbx_struct_sheet_hbond.range_2_label_asym_id 
_pdbx_struct_sheet_hbond.range_2_label_seq_id 
_pdbx_struct_sheet_hbond.range_2_PDB_ins_code 
_pdbx_struct_sheet_hbond.range_2_auth_atom_id 
_pdbx_struct_sheet_hbond.range_2_auth_comp_id 
_pdbx_struct_sheet_hbond.range_2_auth_asym_id 
_pdbx_struct_sheet_hbond.range_2_auth_seq_id 
AA1 1 2 O LEU B 56  ? O LEU B 65  N LEU B 49  ? N LEU B 58  
AA1 2 3 O ARG B 50  ? O ARG B 59  N ILE A 10  ? N ILE A 53  
AA1 3 4 N ALA A 13  ? N ALA A 56  O VAL B 13  ? O VAL B 22  
AA1 4 5 N VAL B 16  ? N VAL B 25  O GLY B 28  ? O GLY B 37  
AA1 5 6 N VAL B 31  ? N VAL B 40  O HIS B 38  ? O HIS B 47  
AA1 6 7 N THR B 39  ? N THR B 48  O VAL B 68  ? O VAL B 77  
AA1 7 8 O SER B 69  ? O SER B 78  N TYR B 59  ? N TYR B 68  
AA2 1 2 N GLU A 23  ? N GLU A 66  O GLN B 101 ? O GLN B 110 
AA2 2 3 O THR B 102 ? O THR B 111 N VAL B 86  ? N VAL B 95  
AA2 3 4 N GLN B 87  ? N GLN B 96  O LEU B 131 ? O LEU B 140 
AA2 4 5 N ILE B 130 ? N ILE B 139 O GLY B 139 ? O GLY B 148 
AA3 1 2 O SER A 42  ? O SER A 85  N ALA A 34  ? N ALA A 77  
AA3 2 3 N LEU A 31  ? N LEU A 74  O LYS B 108 ? O LYS B 117 
AA3 3 4 N PHE B 107 ? N PHE B 116 O ILE B 114 ? O ILE B 123 
AA3 4 5 N VAL B 117 ? N VAL B 126 O SER B 154 ? O SER B 163 
AA3 5 6 O VAL B 153 ? O VAL B 162 N VAL B 145 ? N VAL B 154 
# 
_pdbx_entry_details.entry_id                   7HOS 
_pdbx_entry_details.compound_details           ? 
_pdbx_entry_details.source_details             ? 
_pdbx_entry_details.nonpolymer_details         ? 
_pdbx_entry_details.sequence_details           ? 
_pdbx_entry_details.has_ligand_of_interest     Y 
_pdbx_entry_details.has_protein_modification   N 
# 
loop_
_pdbx_validate_close_contact.id 
_pdbx_validate_close_contact.PDB_model_num 
_pdbx_validate_close_contact.auth_atom_id_1 
_pdbx_validate_close_contact.auth_asym_id_1 
_pdbx_validate_close_contact.auth_comp_id_1 
_pdbx_validate_close_contact.auth_seq_id_1 
_pdbx_validate_close_contact.PDB_ins_code_1 
_pdbx_validate_close_contact.label_alt_id_1 
_pdbx_validate_close_contact.auth_atom_id_2 
_pdbx_validate_close_contact.auth_asym_id_2 
_pdbx_validate_close_contact.auth_comp_id_2 
_pdbx_validate_close_contact.auth_seq_id_2 
_pdbx_validate_close_contact.PDB_ins_code_2 
_pdbx_validate_close_contact.label_alt_id_2 
_pdbx_validate_close_contact.dist 
1 1 OD1 B ASP 20 ? ? O  B HOH 301 ? ? 2.01 
2 1 OD2 B ASP 90 ? ? OG B SER 93  ? ? 2.14 
3 1 O   B LEU 30 ? ? O  B HOH 302 ? ? 2.18 
# 
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 LEU B 30  ? ? -121.94 -167.57 
2 1 CYS B 80  ? ? 85.07   -6.94   
3 1 LEU B 92  ? ? -132.16 -51.97  
4 1 ALA B 127 ? ? -106.52 74.72   
5 1 ALA B 127 ? ? -107.72 74.72   
6 1 ALA B 127 ? ? -106.45 74.72   
7 1 ALA B 127 ? ? -107.71 74.72   
# 
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 346 ? I HOH . 
2 1 B HOH 365 ? I HOH . 
3 1 B HOH 374 ? 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 
A1BGY N1   N Y N 1   
A1BGY N3   N Y N 2   
A1BGY C4   C Y N 3   
A1BGY C5   C Y N 4   
A1BGY C6   C Y N 5   
A1BGY C7   C N N 6   
A1BGY C8   C Y N 7   
A1BGY C10  C Y N 8   
A1BGY C13  C N N 9   
A1BGY C15  C Y N 10  
A1BGY C1   C N N 11  
A1BGY C2   C Y N 12  
A1BGY C3   C Y N 13  
A1BGY N2   N N N 14  
A1BGY O1   O N N 15  
A1BGY C9   C Y N 16  
A1BGY C11  C N N 17  
A1BGY C12  C N N 18  
A1BGY C14  C N N 19  
A1BGY C16  C N N 20  
A1BGY H5   H N N 21  
A1BGY H6   H N N 22  
A1BGY H13  H N N 23  
A1BGY H12  H N N 24  
A1BGY H1   H N N 25  
A1BGY H3   H N N 26  
A1BGY H2   H N N 27  
A1BGY H4   H N N 28  
A1BGY H7   H N N 29  
A1BGY H8   H N N 30  
A1BGY H9   H N N 31  
A1BGY H11  H N N 32  
A1BGY H10  H N N 33  
A1BGY H16  H N N 34  
A1BGY H14  H N N 35  
A1BGY H15  H N N 36  
A1BGY H19  H N N 37  
A1BGY H17  H N N 38  
A1BGY H18  H N N 39  
ALA   N    N N N 40  
ALA   CA   C N S 41  
ALA   C    C N N 42  
ALA   O    O N N 43  
ALA   CB   C N N 44  
ALA   OXT  O N N 45  
ALA   H    H N N 46  
ALA   H2   H N N 47  
ALA   HA   H N N 48  
ALA   HB1  H N N 49  
ALA   HB2  H N N 50  
ALA   HB3  H N N 51  
ALA   HXT  H N N 52  
ARG   N    N N N 53  
ARG   CA   C N S 54  
ARG   C    C N N 55  
ARG   O    O N N 56  
ARG   CB   C N N 57  
ARG   CG   C N N 58  
ARG   CD   C N N 59  
ARG   NE   N N N 60  
ARG   CZ   C N N 61  
ARG   NH1  N N N 62  
ARG   NH2  N N N 63  
ARG   OXT  O N N 64  
ARG   H    H N N 65  
ARG   H2   H N N 66  
ARG   HA   H N N 67  
ARG   HB2  H N N 68  
ARG   HB3  H N N 69  
ARG   HG2  H N N 70  
ARG   HG3  H N N 71  
ARG   HD2  H N N 72  
ARG   HD3  H N N 73  
ARG   HE   H N N 74  
ARG   HH11 H N N 75  
ARG   HH12 H N N 76  
ARG   HH21 H N N 77  
ARG   HH22 H N N 78  
ARG   HXT  H N N 79  
ASN   N    N N N 80  
ASN   CA   C N S 81  
ASN   C    C N N 82  
ASN   O    O N N 83  
ASN   CB   C N N 84  
ASN   CG   C N N 85  
ASN   OD1  O N N 86  
ASN   ND2  N N N 87  
ASN   OXT  O N N 88  
ASN   H    H N N 89  
ASN   H2   H N N 90  
ASN   HA   H N N 91  
ASN   HB2  H N N 92  
ASN   HB3  H N N 93  
ASN   HD21 H N N 94  
ASN   HD22 H N N 95  
ASN   HXT  H N N 96  
ASP   N    N N N 97  
ASP   CA   C N S 98  
ASP   C    C N N 99  
ASP   O    O N N 100 
ASP   CB   C N N 101 
ASP   CG   C N N 102 
ASP   OD1  O N N 103 
ASP   OD2  O N N 104 
ASP   OXT  O N N 105 
ASP   H    H N N 106 
ASP   H2   H N N 107 
ASP   HA   H N N 108 
ASP   HB2  H N N 109 
ASP   HB3  H N N 110 
ASP   HD2  H N N 111 
ASP   HXT  H N N 112 
CYS   N    N N N 113 
CYS   CA   C N R 114 
CYS   C    C N N 115 
CYS   O    O N N 116 
CYS   CB   C N N 117 
CYS   SG   S N N 118 
CYS   OXT  O N N 119 
CYS   H    H N N 120 
CYS   H2   H N N 121 
CYS   HA   H N N 122 
CYS   HB2  H N N 123 
CYS   HB3  H N N 124 
CYS   HG   H N N 125 
CYS   HXT  H N N 126 
DMS   S    S N N 127 
DMS   O    O N N 128 
DMS   C1   C N N 129 
DMS   C2   C N N 130 
DMS   H11  H N N 131 
DMS   H12  H N N 132 
DMS   H13  H N N 133 
DMS   H21  H N N 134 
DMS   H22  H N N 135 
DMS   H23  H N N 136 
GLN   N    N N N 137 
GLN   CA   C N S 138 
GLN   C    C N N 139 
GLN   O    O N N 140 
GLN   CB   C N N 141 
GLN   CG   C N N 142 
GLN   CD   C N N 143 
GLN   OE1  O N N 144 
GLN   NE2  N N N 145 
GLN   OXT  O N N 146 
GLN   H    H N N 147 
GLN   H2   H N N 148 
GLN   HA   H N N 149 
GLN   HB2  H N N 150 
GLN   HB3  H N N 151 
GLN   HG2  H N N 152 
GLN   HG3  H N N 153 
GLN   HE21 H N N 154 
GLN   HE22 H N N 155 
GLN   HXT  H N N 156 
GLU   N    N N N 157 
GLU   CA   C N S 158 
GLU   C    C N N 159 
GLU   O    O N N 160 
GLU   CB   C N N 161 
GLU   CG   C N N 162 
GLU   CD   C N N 163 
GLU   OE1  O N N 164 
GLU   OE2  O N N 165 
GLU   OXT  O N N 166 
GLU   H    H N N 167 
GLU   H2   H N N 168 
GLU   HA   H N N 169 
GLU   HB2  H N N 170 
GLU   HB3  H N N 171 
GLU   HG2  H N N 172 
GLU   HG3  H N N 173 
GLU   HE2  H N N 174 
GLU   HXT  H N N 175 
GLY   N    N N N 176 
GLY   CA   C N N 177 
GLY   C    C N N 178 
GLY   O    O N N 179 
GLY   OXT  O N N 180 
GLY   H    H N N 181 
GLY   H2   H N N 182 
GLY   HA2  H N N 183 
GLY   HA3  H N N 184 
GLY   HXT  H N N 185 
HIS   N    N N N 186 
HIS   CA   C N S 187 
HIS   C    C N N 188 
HIS   O    O N N 189 
HIS   CB   C N N 190 
HIS   CG   C Y N 191 
HIS   ND1  N Y N 192 
HIS   CD2  C Y N 193 
HIS   CE1  C Y N 194 
HIS   NE2  N Y N 195 
HIS   OXT  O N N 196 
HIS   H    H N N 197 
HIS   H2   H N N 198 
HIS   HA   H N N 199 
HIS   HB2  H N N 200 
HIS   HB3  H N N 201 
HIS   HD1  H N N 202 
HIS   HD2  H N N 203 
HIS   HE1  H N N 204 
HIS   HE2  H N N 205 
HIS   HXT  H N N 206 
HOH   O    O N N 207 
HOH   H1   H N N 208 
HOH   H2   H N N 209 
ILE   N    N N N 210 
ILE   CA   C N S 211 
ILE   C    C N N 212 
ILE   O    O N N 213 
ILE   CB   C N S 214 
ILE   CG1  C N N 215 
ILE   CG2  C N N 216 
ILE   CD1  C N N 217 
ILE   OXT  O N N 218 
ILE   H    H N N 219 
ILE   H2   H N N 220 
ILE   HA   H N N 221 
ILE   HB   H N N 222 
ILE   HG12 H N N 223 
ILE   HG13 H N N 224 
ILE   HG21 H N N 225 
ILE   HG22 H N N 226 
ILE   HG23 H N N 227 
ILE   HD11 H N N 228 
ILE   HD12 H N N 229 
ILE   HD13 H N N 230 
ILE   HXT  H N N 231 
LEU   N    N N N 232 
LEU   CA   C N S 233 
LEU   C    C N N 234 
LEU   O    O N N 235 
LEU   CB   C N N 236 
LEU   CG   C N N 237 
LEU   CD1  C N N 238 
LEU   CD2  C N N 239 
LEU   OXT  O N N 240 
LEU   H    H N N 241 
LEU   H2   H N N 242 
LEU   HA   H N N 243 
LEU   HB2  H N N 244 
LEU   HB3  H N N 245 
LEU   HG   H N N 246 
LEU   HD11 H N N 247 
LEU   HD12 H N N 248 
LEU   HD13 H N N 249 
LEU   HD21 H N N 250 
LEU   HD22 H N N 251 
LEU   HD23 H N N 252 
LEU   HXT  H N N 253 
LYS   N    N N N 254 
LYS   CA   C N S 255 
LYS   C    C N N 256 
LYS   O    O N N 257 
LYS   CB   C N N 258 
LYS   CG   C N N 259 
LYS   CD   C N N 260 
LYS   CE   C N N 261 
LYS   NZ   N N N 262 
LYS   OXT  O N N 263 
LYS   H    H N N 264 
LYS   H2   H N N 265 
LYS   HA   H N N 266 
LYS   HB2  H N N 267 
LYS   HB3  H N N 268 
LYS   HG2  H N N 269 
LYS   HG3  H N N 270 
LYS   HD2  H N N 271 
LYS   HD3  H N N 272 
LYS   HE2  H N N 273 
LYS   HE3  H N N 274 
LYS   HZ1  H N N 275 
LYS   HZ2  H N N 276 
LYS   HZ3  H N N 277 
LYS   HXT  H N N 278 
MET   N    N N N 279 
MET   CA   C N S 280 
MET   C    C N N 281 
MET   O    O N N 282 
MET   CB   C N N 283 
MET   CG   C N N 284 
MET   SD   S N N 285 
MET   CE   C N N 286 
MET   OXT  O N N 287 
MET   H    H N N 288 
MET   H2   H N N 289 
MET   HA   H N N 290 
MET   HB2  H N N 291 
MET   HB3  H N N 292 
MET   HG2  H N N 293 
MET   HG3  H N N 294 
MET   HE1  H N N 295 
MET   HE2  H N N 296 
MET   HE3  H N N 297 
MET   HXT  H N N 298 
PHE   N    N N N 299 
PHE   CA   C N S 300 
PHE   C    C N N 301 
PHE   O    O N N 302 
PHE   CB   C N N 303 
PHE   CG   C Y N 304 
PHE   CD1  C Y N 305 
PHE   CD2  C Y N 306 
PHE   CE1  C Y N 307 
PHE   CE2  C Y N 308 
PHE   CZ   C Y N 309 
PHE   OXT  O N N 310 
PHE   H    H N N 311 
PHE   H2   H N N 312 
PHE   HA   H N N 313 
PHE   HB2  H N N 314 
PHE   HB3  H N N 315 
PHE   HD1  H N N 316 
PHE   HD2  H N N 317 
PHE   HE1  H N N 318 
PHE   HE2  H N N 319 
PHE   HZ   H N N 320 
PHE   HXT  H N N 321 
PRO   N    N N N 322 
PRO   CA   C N S 323 
PRO   C    C N N 324 
PRO   O    O N N 325 
PRO   CB   C N N 326 
PRO   CG   C N N 327 
PRO   CD   C N N 328 
PRO   OXT  O N N 329 
PRO   H    H N N 330 
PRO   HA   H N N 331 
PRO   HB2  H N N 332 
PRO   HB3  H N N 333 
PRO   HG2  H N N 334 
PRO   HG3  H N N 335 
PRO   HD2  H N N 336 
PRO   HD3  H N N 337 
PRO   HXT  H N N 338 
SER   N    N N N 339 
SER   CA   C N S 340 
SER   C    C N N 341 
SER   O    O N N 342 
SER   CB   C N N 343 
SER   OG   O N N 344 
SER   OXT  O N N 345 
SER   H    H N N 346 
SER   H2   H N N 347 
SER   HA   H N N 348 
SER   HB2  H N N 349 
SER   HB3  H N N 350 
SER   HG   H N N 351 
SER   HXT  H N N 352 
SO4   S    S N N 353 
SO4   O1   O N N 354 
SO4   O2   O N N 355 
SO4   O3   O N N 356 
SO4   O4   O N N 357 
THR   N    N N N 358 
THR   CA   C N S 359 
THR   C    C N N 360 
THR   O    O N N 361 
THR   CB   C N R 362 
THR   OG1  O N N 363 
THR   CG2  C N N 364 
THR   OXT  O N N 365 
THR   H    H N N 366 
THR   H2   H N N 367 
THR   HA   H N N 368 
THR   HB   H N N 369 
THR   HG1  H N N 370 
THR   HG21 H N N 371 
THR   HG22 H N N 372 
THR   HG23 H N N 373 
THR   HXT  H N N 374 
TRP   N    N N N 375 
TRP   CA   C N S 376 
TRP   C    C N N 377 
TRP   O    O N N 378 
TRP   CB   C N N 379 
TRP   CG   C Y N 380 
TRP   CD1  C Y N 381 
TRP   CD2  C Y N 382 
TRP   NE1  N Y N 383 
TRP   CE2  C Y N 384 
TRP   CE3  C Y N 385 
TRP   CZ2  C Y N 386 
TRP   CZ3  C Y N 387 
TRP   CH2  C Y N 388 
TRP   OXT  O N N 389 
TRP   H    H N N 390 
TRP   H2   H N N 391 
TRP   HA   H N N 392 
TRP   HB2  H N N 393 
TRP   HB3  H N N 394 
TRP   HD1  H N N 395 
TRP   HE1  H N N 396 
TRP   HE3  H N N 397 
TRP   HZ2  H N N 398 
TRP   HZ3  H N N 399 
TRP   HH2  H N N 400 
TRP   HXT  H N N 401 
TYR   N    N N N 402 
TYR   CA   C N S 403 
TYR   C    C N N 404 
TYR   O    O N N 405 
TYR   CB   C N N 406 
TYR   CG   C Y N 407 
TYR   CD1  C Y N 408 
TYR   CD2  C Y N 409 
TYR   CE1  C Y N 410 
TYR   CE2  C Y N 411 
TYR   CZ   C Y N 412 
TYR   OH   O N N 413 
TYR   OXT  O N N 414 
TYR   H    H N N 415 
TYR   H2   H N N 416 
TYR   HA   H N N 417 
TYR   HB2  H N N 418 
TYR   HB3  H N N 419 
TYR   HD1  H N N 420 
TYR   HD2  H N N 421 
TYR   HE1  H N N 422 
TYR   HE2  H N N 423 
TYR   HH   H N N 424 
TYR   HXT  H N N 425 
VAL   N    N N N 426 
VAL   CA   C N S 427 
VAL   C    C N N 428 
VAL   O    O N N 429 
VAL   CB   C N N 430 
VAL   CG1  C N N 431 
VAL   CG2  C N N 432 
VAL   OXT  O N N 433 
VAL   H    H N N 434 
VAL   H2   H N N 435 
VAL   HA   H N N 436 
VAL   HB   H N N 437 
VAL   HG11 H N N 438 
VAL   HG12 H N N 439 
VAL   HG13 H N N 440 
VAL   HG21 H N N 441 
VAL   HG22 H N N 442 
VAL   HG23 H N N 443 
VAL   HXT  H N N 444 
# 
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 
A1BGY C1  C2   sing N N 1   
A1BGY C2  C3   doub Y N 2   
A1BGY C3  N1   sing Y N 3   
A1BGY N1  C4   doub Y N 4   
A1BGY C4  C5   sing Y N 5   
A1BGY C5  C6   doub Y N 6   
A1BGY C6  N2   sing N N 7   
A1BGY N2  C7   sing N N 8   
A1BGY C7  O1   doub N N 9   
A1BGY C7  C8   sing N N 10  
A1BGY C8  C9   sing Y N 11  
A1BGY C9  C10  doub Y N 12  
A1BGY C10 C11  sing N N 13  
A1BGY C11 C12  sing N N 14  
A1BGY C12 C13  sing N N 15  
A1BGY C10 N3   sing Y N 16  
A1BGY N3  C14  sing N N 17  
A1BGY N3  C15  sing Y N 18  
A1BGY C15 C16  sing N N 19  
A1BGY C2  C6   sing Y N 20  
A1BGY C8  C15  doub Y N 21  
A1BGY C11 C13  sing N N 22  
A1BGY C4  H5   sing N N 23  
A1BGY C5  H6   sing N N 24  
A1BGY C13 H13  sing N N 25  
A1BGY C13 H12  sing N N 26  
A1BGY C1  H1   sing N N 27  
A1BGY C1  H3   sing N N 28  
A1BGY C1  H2   sing N N 29  
A1BGY C3  H4   sing N N 30  
A1BGY N2  H7   sing N N 31  
A1BGY C9  H8   sing N N 32  
A1BGY C11 H9   sing N N 33  
A1BGY C12 H11  sing N N 34  
A1BGY C12 H10  sing N N 35  
A1BGY C14 H16  sing N N 36  
A1BGY C14 H14  sing N N 37  
A1BGY C14 H15  sing N N 38  
A1BGY C16 H19  sing N N 39  
A1BGY C16 H17  sing N N 40  
A1BGY C16 H18  sing N N 41  
ALA   N   CA   sing N N 42  
ALA   N   H    sing N N 43  
ALA   N   H2   sing N N 44  
ALA   CA  C    sing N N 45  
ALA   CA  CB   sing N N 46  
ALA   CA  HA   sing N N 47  
ALA   C   O    doub N N 48  
ALA   C   OXT  sing N N 49  
ALA   CB  HB1  sing N N 50  
ALA   CB  HB2  sing N N 51  
ALA   CB  HB3  sing N N 52  
ALA   OXT HXT  sing N N 53  
ARG   N   CA   sing N N 54  
ARG   N   H    sing N N 55  
ARG   N   H2   sing N N 56  
ARG   CA  C    sing N N 57  
ARG   CA  CB   sing N N 58  
ARG   CA  HA   sing N N 59  
ARG   C   O    doub N N 60  
ARG   C   OXT  sing N N 61  
ARG   CB  CG   sing N N 62  
ARG   CB  HB2  sing N N 63  
ARG   CB  HB3  sing N N 64  
ARG   CG  CD   sing N N 65  
ARG   CG  HG2  sing N N 66  
ARG   CG  HG3  sing N N 67  
ARG   CD  NE   sing N N 68  
ARG   CD  HD2  sing N N 69  
ARG   CD  HD3  sing N N 70  
ARG   NE  CZ   sing N N 71  
ARG   NE  HE   sing N N 72  
ARG   CZ  NH1  sing N N 73  
ARG   CZ  NH2  doub N N 74  
ARG   NH1 HH11 sing N N 75  
ARG   NH1 HH12 sing N N 76  
ARG   NH2 HH21 sing N N 77  
ARG   NH2 HH22 sing N N 78  
ARG   OXT HXT  sing N N 79  
ASN   N   CA   sing N N 80  
ASN   N   H    sing N N 81  
ASN   N   H2   sing N N 82  
ASN   CA  C    sing N N 83  
ASN   CA  CB   sing N N 84  
ASN   CA  HA   sing N N 85  
ASN   C   O    doub N N 86  
ASN   C   OXT  sing N N 87  
ASN   CB  CG   sing N N 88  
ASN   CB  HB2  sing N N 89  
ASN   CB  HB3  sing N N 90  
ASN   CG  OD1  doub N N 91  
ASN   CG  ND2  sing N N 92  
ASN   ND2 HD21 sing N N 93  
ASN   ND2 HD22 sing N N 94  
ASN   OXT HXT  sing N N 95  
ASP   N   CA   sing N N 96  
ASP   N   H    sing N N 97  
ASP   N   H2   sing N N 98  
ASP   CA  C    sing N N 99  
ASP   CA  CB   sing N N 100 
ASP   CA  HA   sing N N 101 
ASP   C   O    doub N N 102 
ASP   C   OXT  sing N N 103 
ASP   CB  CG   sing N N 104 
ASP   CB  HB2  sing N N 105 
ASP   CB  HB3  sing N N 106 
ASP   CG  OD1  doub N N 107 
ASP   CG  OD2  sing N N 108 
ASP   OD2 HD2  sing N N 109 
ASP   OXT HXT  sing N N 110 
CYS   N   CA   sing N N 111 
CYS   N   H    sing N N 112 
CYS   N   H2   sing N N 113 
CYS   CA  C    sing N N 114 
CYS   CA  CB   sing N N 115 
CYS   CA  HA   sing N N 116 
CYS   C   O    doub N N 117 
CYS   C   OXT  sing N N 118 
CYS   CB  SG   sing N N 119 
CYS   CB  HB2  sing N N 120 
CYS   CB  HB3  sing N N 121 
CYS   SG  HG   sing N N 122 
CYS   OXT HXT  sing N N 123 
DMS   S   O    doub N N 124 
DMS   S   C1   sing N N 125 
DMS   S   C2   sing N N 126 
DMS   C1  H11  sing N N 127 
DMS   C1  H12  sing N N 128 
DMS   C1  H13  sing N N 129 
DMS   C2  H21  sing N N 130 
DMS   C2  H22  sing N N 131 
DMS   C2  H23  sing N N 132 
GLN   N   CA   sing N N 133 
GLN   N   H    sing N N 134 
GLN   N   H2   sing N N 135 
GLN   CA  C    sing N N 136 
GLN   CA  CB   sing N N 137 
GLN   CA  HA   sing N N 138 
GLN   C   O    doub N N 139 
GLN   C   OXT  sing N N 140 
GLN   CB  CG   sing N N 141 
GLN   CB  HB2  sing N N 142 
GLN   CB  HB3  sing N N 143 
GLN   CG  CD   sing N N 144 
GLN   CG  HG2  sing N N 145 
GLN   CG  HG3  sing N N 146 
GLN   CD  OE1  doub N N 147 
GLN   CD  NE2  sing N N 148 
GLN   NE2 HE21 sing N N 149 
GLN   NE2 HE22 sing N N 150 
GLN   OXT HXT  sing N N 151 
GLU   N   CA   sing N N 152 
GLU   N   H    sing N N 153 
GLU   N   H2   sing N N 154 
GLU   CA  C    sing N N 155 
GLU   CA  CB   sing N N 156 
GLU   CA  HA   sing N N 157 
GLU   C   O    doub N N 158 
GLU   C   OXT  sing N N 159 
GLU   CB  CG   sing N N 160 
GLU   CB  HB2  sing N N 161 
GLU   CB  HB3  sing N N 162 
GLU   CG  CD   sing N N 163 
GLU   CG  HG2  sing N N 164 
GLU   CG  HG3  sing N N 165 
GLU   CD  OE1  doub N N 166 
GLU   CD  OE2  sing N N 167 
GLU   OE2 HE2  sing N N 168 
GLU   OXT HXT  sing N N 169 
GLY   N   CA   sing N N 170 
GLY   N   H    sing N N 171 
GLY   N   H2   sing N N 172 
GLY   CA  C    sing N N 173 
GLY   CA  HA2  sing N N 174 
GLY   CA  HA3  sing N N 175 
GLY   C   O    doub N N 176 
GLY   C   OXT  sing N N 177 
GLY   OXT HXT  sing N N 178 
HIS   N   CA   sing N N 179 
HIS   N   H    sing N N 180 
HIS   N   H2   sing N N 181 
HIS   CA  C    sing N N 182 
HIS   CA  CB   sing N N 183 
HIS   CA  HA   sing N N 184 
HIS   C   O    doub N N 185 
HIS   C   OXT  sing N N 186 
HIS   CB  CG   sing N N 187 
HIS   CB  HB2  sing N N 188 
HIS   CB  HB3  sing N N 189 
HIS   CG  ND1  sing Y N 190 
HIS   CG  CD2  doub Y N 191 
HIS   ND1 CE1  doub Y N 192 
HIS   ND1 HD1  sing N N 193 
HIS   CD2 NE2  sing Y N 194 
HIS   CD2 HD2  sing N N 195 
HIS   CE1 NE2  sing Y N 196 
HIS   CE1 HE1  sing N N 197 
HIS   NE2 HE2  sing N N 198 
HIS   OXT HXT  sing N N 199 
HOH   O   H1   sing N N 200 
HOH   O   H2   sing N N 201 
ILE   N   CA   sing N N 202 
ILE   N   H    sing N N 203 
ILE   N   H2   sing N N 204 
ILE   CA  C    sing N N 205 
ILE   CA  CB   sing N N 206 
ILE   CA  HA   sing N N 207 
ILE   C   O    doub N N 208 
ILE   C   OXT  sing N N 209 
ILE   CB  CG1  sing N N 210 
ILE   CB  CG2  sing N N 211 
ILE   CB  HB   sing N N 212 
ILE   CG1 CD1  sing N N 213 
ILE   CG1 HG12 sing N N 214 
ILE   CG1 HG13 sing N N 215 
ILE   CG2 HG21 sing N N 216 
ILE   CG2 HG22 sing N N 217 
ILE   CG2 HG23 sing N N 218 
ILE   CD1 HD11 sing N N 219 
ILE   CD1 HD12 sing N N 220 
ILE   CD1 HD13 sing N N 221 
ILE   OXT HXT  sing N N 222 
LEU   N   CA   sing N N 223 
LEU   N   H    sing N N 224 
LEU   N   H2   sing N N 225 
LEU   CA  C    sing N N 226 
LEU   CA  CB   sing N N 227 
LEU   CA  HA   sing N N 228 
LEU   C   O    doub N N 229 
LEU   C   OXT  sing N N 230 
LEU   CB  CG   sing N N 231 
LEU   CB  HB2  sing N N 232 
LEU   CB  HB3  sing N N 233 
LEU   CG  CD1  sing N N 234 
LEU   CG  CD2  sing N N 235 
LEU   CG  HG   sing N N 236 
LEU   CD1 HD11 sing N N 237 
LEU   CD1 HD12 sing N N 238 
LEU   CD1 HD13 sing N N 239 
LEU   CD2 HD21 sing N N 240 
LEU   CD2 HD22 sing N N 241 
LEU   CD2 HD23 sing N N 242 
LEU   OXT HXT  sing N N 243 
LYS   N   CA   sing N N 244 
LYS   N   H    sing N N 245 
LYS   N   H2   sing N N 246 
LYS   CA  C    sing N N 247 
LYS   CA  CB   sing N N 248 
LYS   CA  HA   sing N N 249 
LYS   C   O    doub N N 250 
LYS   C   OXT  sing N N 251 
LYS   CB  CG   sing N N 252 
LYS   CB  HB2  sing N N 253 
LYS   CB  HB3  sing N N 254 
LYS   CG  CD   sing N N 255 
LYS   CG  HG2  sing N N 256 
LYS   CG  HG3  sing N N 257 
LYS   CD  CE   sing N N 258 
LYS   CD  HD2  sing N N 259 
LYS   CD  HD3  sing N N 260 
LYS   CE  NZ   sing N N 261 
LYS   CE  HE2  sing N N 262 
LYS   CE  HE3  sing N N 263 
LYS   NZ  HZ1  sing N N 264 
LYS   NZ  HZ2  sing N N 265 
LYS   NZ  HZ3  sing N N 266 
LYS   OXT HXT  sing N N 267 
MET   N   CA   sing N N 268 
MET   N   H    sing N N 269 
MET   N   H2   sing N N 270 
MET   CA  C    sing N N 271 
MET   CA  CB   sing N N 272 
MET   CA  HA   sing N N 273 
MET   C   O    doub N N 274 
MET   C   OXT  sing N N 275 
MET   CB  CG   sing N N 276 
MET   CB  HB2  sing N N 277 
MET   CB  HB3  sing N N 278 
MET   CG  SD   sing N N 279 
MET   CG  HG2  sing N N 280 
MET   CG  HG3  sing N N 281 
MET   SD  CE   sing N N 282 
MET   CE  HE1  sing N N 283 
MET   CE  HE2  sing N N 284 
MET   CE  HE3  sing N N 285 
MET   OXT HXT  sing N N 286 
PHE   N   CA   sing N N 287 
PHE   N   H    sing N N 288 
PHE   N   H2   sing N N 289 
PHE   CA  C    sing N N 290 
PHE   CA  CB   sing N N 291 
PHE   CA  HA   sing N N 292 
PHE   C   O    doub N N 293 
PHE   C   OXT  sing N N 294 
PHE   CB  CG   sing N N 295 
PHE   CB  HB2  sing N N 296 
PHE   CB  HB3  sing N N 297 
PHE   CG  CD1  doub Y N 298 
PHE   CG  CD2  sing Y N 299 
PHE   CD1 CE1  sing Y N 300 
PHE   CD1 HD1  sing N N 301 
PHE   CD2 CE2  doub Y N 302 
PHE   CD2 HD2  sing N N 303 
PHE   CE1 CZ   doub Y N 304 
PHE   CE1 HE1  sing N N 305 
PHE   CE2 CZ   sing Y N 306 
PHE   CE2 HE2  sing N N 307 
PHE   CZ  HZ   sing N N 308 
PHE   OXT HXT  sing N N 309 
PRO   N   CA   sing N N 310 
PRO   N   CD   sing N N 311 
PRO   N   H    sing N N 312 
PRO   CA  C    sing N N 313 
PRO   CA  CB   sing N N 314 
PRO   CA  HA   sing N N 315 
PRO   C   O    doub N N 316 
PRO   C   OXT  sing N N 317 
PRO   CB  CG   sing N N 318 
PRO   CB  HB2  sing N N 319 
PRO   CB  HB3  sing N N 320 
PRO   CG  CD   sing N N 321 
PRO   CG  HG2  sing N N 322 
PRO   CG  HG3  sing N N 323 
PRO   CD  HD2  sing N N 324 
PRO   CD  HD3  sing N N 325 
PRO   OXT HXT  sing N N 326 
SER   N   CA   sing N N 327 
SER   N   H    sing N N 328 
SER   N   H2   sing N N 329 
SER   CA  C    sing N N 330 
SER   CA  CB   sing N N 331 
SER   CA  HA   sing N N 332 
SER   C   O    doub N N 333 
SER   C   OXT  sing N N 334 
SER   CB  OG   sing N N 335 
SER   CB  HB2  sing N N 336 
SER   CB  HB3  sing N N 337 
SER   OG  HG   sing N N 338 
SER   OXT HXT  sing N N 339 
SO4   S   O1   doub N N 340 
SO4   S   O2   doub N N 341 
SO4   S   O3   sing N N 342 
SO4   S   O4   sing N N 343 
THR   N   CA   sing N N 344 
THR   N   H    sing N N 345 
THR   N   H2   sing N N 346 
THR   CA  C    sing N N 347 
THR   CA  CB   sing N N 348 
THR   CA  HA   sing N N 349 
THR   C   O    doub N N 350 
THR   C   OXT  sing N N 351 
THR   CB  OG1  sing N N 352 
THR   CB  CG2  sing N N 353 
THR   CB  HB   sing N N 354 
THR   OG1 HG1  sing N N 355 
THR   CG2 HG21 sing N N 356 
THR   CG2 HG22 sing N N 357 
THR   CG2 HG23 sing N N 358 
THR   OXT HXT  sing N N 359 
TRP   N   CA   sing N N 360 
TRP   N   H    sing N N 361 
TRP   N   H2   sing N N 362 
TRP   CA  C    sing N N 363 
TRP   CA  CB   sing N N 364 
TRP   CA  HA   sing N N 365 
TRP   C   O    doub N N 366 
TRP   C   OXT  sing N N 367 
TRP   CB  CG   sing N N 368 
TRP   CB  HB2  sing N N 369 
TRP   CB  HB3  sing N N 370 
TRP   CG  CD1  doub Y N 371 
TRP   CG  CD2  sing Y N 372 
TRP   CD1 NE1  sing Y N 373 
TRP   CD1 HD1  sing N N 374 
TRP   CD2 CE2  doub Y N 375 
TRP   CD2 CE3  sing Y N 376 
TRP   NE1 CE2  sing Y N 377 
TRP   NE1 HE1  sing N N 378 
TRP   CE2 CZ2  sing Y N 379 
TRP   CE3 CZ3  doub Y N 380 
TRP   CE3 HE3  sing N N 381 
TRP   CZ2 CH2  doub Y N 382 
TRP   CZ2 HZ2  sing N N 383 
TRP   CZ3 CH2  sing Y N 384 
TRP   CZ3 HZ3  sing N N 385 
TRP   CH2 HH2  sing N N 386 
TRP   OXT HXT  sing N N 387 
TYR   N   CA   sing N N 388 
TYR   N   H    sing N N 389 
TYR   N   H2   sing N N 390 
TYR   CA  C    sing N N 391 
TYR   CA  CB   sing N N 392 
TYR   CA  HA   sing N N 393 
TYR   C   O    doub N N 394 
TYR   C   OXT  sing N N 395 
TYR   CB  CG   sing N N 396 
TYR   CB  HB2  sing N N 397 
TYR   CB  HB3  sing N N 398 
TYR   CG  CD1  doub Y N 399 
TYR   CG  CD2  sing Y N 400 
TYR   CD1 CE1  sing Y N 401 
TYR   CD1 HD1  sing N N 402 
TYR   CD2 CE2  doub Y N 403 
TYR   CD2 HD2  sing N N 404 
TYR   CE1 CZ   doub Y N 405 
TYR   CE1 HE1  sing N N 406 
TYR   CE2 CZ   sing Y N 407 
TYR   CE2 HE2  sing N N 408 
TYR   CZ  OH   sing N N 409 
TYR   OH  HH   sing N N 410 
TYR   OXT HXT  sing N N 411 
VAL   N   CA   sing N N 412 
VAL   N   H    sing N N 413 
VAL   N   H2   sing N N 414 
VAL   CA  C    sing N N 415 
VAL   CA  CB   sing N N 416 
VAL   CA  HA   sing N N 417 
VAL   C   O    doub N N 418 
VAL   C   OXT  sing N N 419 
VAL   CB  CG1  sing N N 420 
VAL   CB  CG2  sing N N 421 
VAL   CB  HB   sing N N 422 
VAL   CG1 HG11 sing N N 423 
VAL   CG1 HG12 sing N N 424 
VAL   CG1 HG13 sing N N 425 
VAL   CG2 HG21 sing N N 426 
VAL   CG2 HG22 sing N N 427 
VAL   CG2 HG23 sing N N 428 
VAL   OXT HXT  sing N N 429 
# 
_pdbx_audit_support.funding_organization   
'National Institutes of Health/National Institute Of Allergy and Infectious Diseases (NIH/NIAID)' 
_pdbx_audit_support.country                'United States' 
_pdbx_audit_support.grant_number           U19AI171399 
_pdbx_audit_support.ordinal                1 
# 
_pdbx_deposit_group.group_id            G_1002322 
_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' 
# 
_atom_sites.entry_id                    7HOS 
_atom_sites.fract_transf_matrix[1][1]   0.023559 
_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]   0.023559 
_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]   0.004611 
_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   ? -20.637 19.127  -7.833  1.00 59.84  ? 50  ASP   A N   1 
ATOM   2    C CA  . ASP   A 1 7   ? -21.962 18.455  -7.646  1.00 56.45  ? 50  ASP   A CA  1 
ATOM   3    C C   . ASP   A 1 7   ? -22.368 17.782  -8.958  1.00 51.05  ? 50  ASP   A C   1 
ATOM   4    O O   . ASP   A 1 7   ? -22.513 18.457  -10.000 1.00 56.00  ? 50  ASP   A O   1 
ATOM   5    C CB  . ASP   A 1 7   ? -23.063 19.411  -7.191  1.00 55.35  ? 50  ASP   A CB  1 
ATOM   6    C CG  . ASP   A 1 7   ? -24.407 18.721  -7.036  1.00 56.54  ? 50  ASP   A CG  1 
ATOM   7    O OD1 . ASP   A 1 7   ? -24.641 18.119  -5.963  1.00 54.80  ? 50  ASP   A OD1 1 
ATOM   8    O OD2 . ASP   A 1 7   ? -25.206 18.784  -7.996  1.00 59.81  ? 50  ASP   A OD2 1 
ATOM   9    N N   . MET   A 1 8   ? -22.568 16.480  -8.899  1.00 42.03  ? 51  MET   A N   1 
ATOM   10   C CA  . MET   A 1 8   ? -22.495 15.648  -10.108 1.00 42.72  ? 51  MET   A CA  1 
ATOM   11   C C   . MET   A 1 8   ? -23.907 15.430  -10.604 1.00 35.32  ? 51  MET   A C   1 
ATOM   12   O O   . MET   A 1 8   ? -24.816 15.358  -9.782  1.00 39.34  ? 51  MET   A O   1 
ATOM   13   C CB  . MET   A 1 8   ? -21.808 14.319  -9.806  1.00 42.08  ? 51  MET   A CB  1 
ATOM   14   C CG  . MET   A 1 8   ? -20.354 14.487  -9.550  1.00 44.19  ? 51  MET   A CG  1 
ATOM   15   S SD  . MET   A 1 8   ? -19.572 12.887  -9.211  1.00 46.05  ? 51  MET   A SD  1 
ATOM   16   C CE  . MET   A 1 8   ? -17.892 13.443  -8.949  1.00 45.08  ? 51  MET   A CE  1 
ATOM   17   N N   . TYR   A 1 9   ? -24.058 15.355  -11.909 1.00 30.74  ? 52  TYR   A N   1 
ATOM   18   C CA  . TYR   A 1 9   ? -25.353 15.086  -12.565 1.00 31.36  ? 52  TYR   A CA  1 
ATOM   19   C C   . TYR   A 1 9   ? -25.105 14.118  -13.708 1.00 31.99  ? 52  TYR   A C   1 
ATOM   20   O O   . TYR   A 1 9   ? -23.945 14.045  -14.155 1.00 33.03  ? 52  TYR   A O   1 
ATOM   21   C CB  . TYR   A 1 9   ? -25.995 16.397  -13.021 1.00 31.55  ? 52  TYR   A CB  1 
ATOM   22   C CG  . TYR   A 1 9   ? -25.203 17.185  -14.031 1.00 32.75  ? 52  TYR   A CG  1 
ATOM   23   C CD1 . TYR   A 1 9   ? -24.148 17.990  -13.631 1.00 33.23  ? 52  TYR   A CD1 1 
ATOM   24   C CD2 . TYR   A 1 9   ? -25.501 17.122  -15.386 1.00 35.05  ? 52  TYR   A CD2 1 
ATOM   25   C CE1 . TYR   A 1 9   ? -23.412 18.727  -14.546 1.00 33.85  ? 52  TYR   A CE1 1 
ATOM   26   C CE2 . TYR   A 1 9   ? -24.782 17.862  -16.318 1.00 36.24  ? 52  TYR   A CE2 1 
ATOM   27   C CZ  . TYR   A 1 9   ? -23.728 18.661  -15.893 1.00 36.40  ? 52  TYR   A CZ  1 
ATOM   28   O OH  . TYR   A 1 9   ? -22.974 19.366  -16.791 1.00 42.71  ? 52  TYR   A OH  1 
ATOM   29   N N   . ILE   A 1 10  ? -26.154 13.410  -14.131 1.00 35.59  ? 53  ILE   A N   1 
ATOM   30   C CA  . ILE   A 1 10  ? -26.113 12.416  -15.243 1.00 34.62  ? 53  ILE   A CA  1 
ATOM   31   C C   . ILE   A 1 10  ? -26.926 12.911  -16.456 1.00 36.94  ? 53  ILE   A C   1 
ATOM   32   O O   . ILE   A 1 10  ? -27.929 13.642  -16.255 1.00 32.89  ? 53  ILE   A O   1 
ATOM   33   C CB  . ILE   A 1 10  ? -26.584 11.033  -14.741 1.00 35.47  ? 53  ILE   A CB  1 
ATOM   34   C CG1 . ILE   A 1 10  ? -28.091 10.927  -14.532 1.00 35.78  ? 53  ILE   A CG1 1 
ATOM   35   C CG2 . ILE   A 1 10  ? -25.824 10.639  -13.487 1.00 38.02  ? 53  ILE   A CG2 1 
ATOM   36   C CD1 . ILE   A 1 10  ? -28.499 9.614   -13.925 1.00 38.24  ? 53  ILE   A CD1 1 
ATOM   37   N N   . GLU   A 1 11  ? -26.500 12.521  -17.672 1.00 36.75  ? 54  GLU   A N   1 
ATOM   38   C CA  . GLU   A 1 11  ? -27.228 12.726  -18.959 1.00 39.23  ? 54  GLU   A CA  1 
ATOM   39   C C   . GLU   A 1 11  ? -27.214 11.423  -19.758 1.00 37.30  ? 54  GLU   A C   1 
ATOM   40   O O   . GLU   A 1 11  ? -26.119 10.779  -19.863 1.00 31.87  ? 54  GLU   A O   1 
ATOM   41   C CB  . GLU   A 1 11  ? -26.589 13.776  -19.877 1.00 42.30  ? 54  GLU   A CB  1 
ATOM   42   C CG  . GLU   A 1 11  ? -26.133 15.057  -19.213 1.00 46.09  ? 54  GLU   A CG  1 
ATOM   43   C CD  . GLU   A 1 11  ? -25.331 15.955  -20.152 1.00 53.64  ? 54  GLU   A CD  1 
ATOM   44   O OE1 . GLU   A 1 11  ? -24.564 15.418  -20.991 1.00 56.29  ? 54  GLU   A OE1 1 
ATOM   45   O OE2 . GLU   A 1 11  ? -25.473 17.188  -20.057 1.00 53.50  ? 54  GLU   A OE2 1 
ATOM   46   N N   . ARG   A 1 12  ? -28.358 11.060  -20.342 1.00 37.26  ? 55  ARG   A N   1 
ATOM   47   C CA  . ARG   A 1 12  ? -28.475 9.812   -21.127 1.00 35.10  ? 55  ARG   A CA  1 
ATOM   48   C C   . ARG   A 1 12  ? -27.582 9.936   -22.355 1.00 37.77  ? 55  ARG   A C   1 
ATOM   49   O O   . ARG   A 1 12  ? -27.426 11.067  -22.849 1.00 38.45  ? 55  ARG   A O   1 
ATOM   50   C CB  . ARG   A 1 12  ? -29.930 9.556   -21.485 1.00 35.54  ? 55  ARG   A CB  1 
ATOM   51   C CG  . ARG   A 1 12  ? -30.189 8.155   -21.997 1.00 38.27  ? 55  ARG   A CG  1 
ATOM   52   C CD  . ARG   A 1 12  ? -31.630 7.764   -21.748 1.00 41.88  ? 55  ARG   A CD  1 
ATOM   53   N NE  . ARG   A 1 12  ? -31.866 6.388   -22.079 1.00 43.40  ? 55  ARG   A NE  1 
ATOM   54   C CZ  . ARG   A 1 12  ? -31.820 5.912   -23.311 1.00 46.24  ? 55  ARG   A CZ  1 
ATOM   55   N NH1 . ARG   A 1 12  ? -31.572 6.724   -24.323 1.00 47.75  ? 55  ARG   A NH1 1 
ATOM   56   N NH2 . ARG   A 1 12  ? -32.030 4.625   -23.530 1.00 48.42  ? 55  ARG   A NH2 1 
ATOM   57   N N   . ALA   A 1 13  ? -26.928 8.846   -22.778 1.00 41.10  ? 56  ALA   A N   1 
ATOM   58   C CA  . ALA   A 1 13  ? -25.979 8.874   -23.920 1.00 34.64  ? 56  ALA   A CA  1 
ATOM   59   C C   . ALA   A 1 13  ? -26.267 7.756   -24.924 1.00 32.75  ? 56  ALA   A C   1 
ATOM   60   O O   . ALA   A 1 13  ? -25.549 7.691   -25.948 1.00 39.89  ? 56  ALA   A O   1 
ATOM   61   C CB  . ALA   A 1 13  ? -24.539 8.865   -23.442 1.00 38.81  ? 56  ALA   A CB  1 
ATOM   62   N N   . GLY   A 1 14  ? -27.246 6.905   -24.668 1.00 30.04  ? 57  GLY   A N   1 
ATOM   63   C CA  . GLY   A 1 14  ? -27.677 5.905   -25.651 1.00 29.46  ? 57  GLY   A CA  1 
ATOM   64   C C   . GLY   A 1 14  ? -28.384 4.761   -24.989 1.00 33.09  ? 57  GLY   A C   1 
ATOM   65   O O   . GLY   A 1 14  ? -28.434 4.763   -23.729 1.00 35.25  ? 57  GLY   A O   1 
ATOM   66   N N   . ASP   A 1 15  ? -28.935 3.871   -25.822 1.00 34.59  ? 58  ASP   A N   1 
ATOM   67   C CA  . ASP   A 1 15  ? -29.400 2.498   -25.493 1.00 38.21  ? 58  ASP   A CA  1 
ATOM   68   C C   . ASP   A 1 15  ? -28.167 1.608   -25.310 1.00 42.68  ? 58  ASP   A C   1 
ATOM   69   O O   . ASP   A 1 15  ? -27.075 1.952   -25.845 1.00 44.11  ? 58  ASP   A O   1 
ATOM   70   C CB  . ASP   A 1 15  ? -30.272 1.890   -26.597 1.00 40.17  ? 58  ASP   A CB  1 
ATOM   71   C CG  . ASP   A 1 15  ? -31.619 2.577   -26.743 1.00 46.44  ? 58  ASP   A CG  1 
ATOM   72   O OD1 . ASP   A 1 15  ? -31.778 3.629   -26.098 1.00 37.99  ? 58  ASP   A OD1 1 
ATOM   73   O OD2 . ASP   A 1 15  ? -32.499 2.053   -27.496 1.00 46.31  ? 58  ASP   A OD2 1 
ATOM   74   N N   . ILE   A 1 16  ? -28.317 0.532   -24.549 1.00 41.63  ? 59  ILE   A N   1 
ATOM   75   C CA  . ILE   A 1 16  ? -27.242 -0.487  -24.398 1.00 43.23  ? 59  ILE   A CA  1 
ATOM   76   C C   . ILE   A 1 16  ? -27.647 -1.632  -25.331 1.00 41.50  ? 59  ILE   A C   1 
ATOM   77   O O   . ILE   A 1 16  ? -28.572 -2.390  -25.018 1.00 41.25  ? 59  ILE   A O   1 
ATOM   78   C CB  . ILE   A 1 16  ? -27.028 -0.838  -22.917 1.00 46.30  ? 59  ILE   A CB  1 
ATOM   79   C CG1 . ILE   A 1 16  ? -26.465 0.374   -22.164 1.00 44.17  ? 59  ILE   A CG1 1 
ATOM   80   C CG2 . ILE   A 1 16  ? -26.108 -2.034  -22.785 1.00 51.77  ? 59  ILE   A CG2 1 
ATOM   81   C CD1 . ILE   A 1 16  ? -26.599 0.302   -20.666 1.00 44.17  ? 59  ILE   A CD1 1 
ATOM   82   N N   A THR   A 1 17  ? -26.963 -1.704  -26.479 0.25 42.38  ? 60  THR   A N   1 
ATOM   83   N N   B THR   A 1 17  ? -26.978 -1.730  -26.482 0.25 42.02  ? 60  THR   A N   1 
ATOM   84   N N   C THR   A 1 17  ? -26.963 -1.704  -26.479 0.25 42.38  ? 60  THR   A N   1 
ATOM   85   N N   D THR   A 1 17  ? -26.978 -1.730  -26.482 0.25 42.02  ? 60  THR   A N   1 
ATOM   86   C CA  A THR   A 1 17  ? -27.257 -2.612  -27.619 0.25 42.41  ? 60  THR   A CA  1 
ATOM   87   C CA  B THR   A 1 17  ? -27.318 -2.675  -27.577 0.25 41.88  ? 60  THR   A CA  1 
ATOM   88   C CA  C THR   A 1 17  ? -27.257 -2.612  -27.619 0.25 42.41  ? 60  THR   A CA  1 
ATOM   89   C CA  D THR   A 1 17  ? -27.318 -2.675  -27.577 0.25 41.88  ? 60  THR   A CA  1 
ATOM   90   C C   A THR   A 1 17  ? -25.954 -3.135  -28.223 0.25 42.14  ? 60  THR   A C   1 
ATOM   91   C C   B THR   A 1 17  ? -26.032 -3.121  -28.281 0.25 42.02  ? 60  THR   A C   1 
ATOM   92   C C   C THR   A 1 17  ? -25.954 -3.135  -28.223 0.25 42.14  ? 60  THR   A C   1 
ATOM   93   C C   D THR   A 1 17  ? -26.032 -3.121  -28.281 0.25 42.02  ? 60  THR   A C   1 
ATOM   94   O O   A THR   A 1 17  ? -24.990 -2.344  -28.355 0.25 42.05  ? 60  THR   A O   1 
ATOM   95   O O   B THR   A 1 17  ? -25.147 -2.266  -28.511 0.25 42.67  ? 60  THR   A O   1 
ATOM   96   O O   C THR   A 1 17  ? -24.990 -2.344  -28.355 0.25 42.05  ? 60  THR   A O   1 
ATOM   97   O O   D THR   A 1 17  ? -25.147 -2.266  -28.511 0.25 42.67  ? 60  THR   A O   1 
ATOM   98   C CB  A THR   A 1 17  ? -28.049 -1.900  -28.724 0.25 41.90  ? 60  THR   A CB  1 
ATOM   99   C CB  B THR   A 1 17  ? -28.342 -2.046  -28.536 0.25 40.96  ? 60  THR   A CB  1 
ATOM   100  C CB  C THR   A 1 17  ? -28.049 -1.900  -28.724 0.25 41.90  ? 60  THR   A CB  1 
ATOM   101  C CB  D THR   A 1 17  ? -28.342 -2.046  -28.536 0.25 40.96  ? 60  THR   A CB  1 
ATOM   102  O OG1 A THR   A 1 17  ? -27.208 -0.913  -29.327 0.25 40.91  ? 60  THR   A OG1 1 
ATOM   103  O OG1 B THR   A 1 17  ? -29.631 -2.146  -27.929 0.25 38.99  ? 60  THR   A OG1 1 
ATOM   104  O OG1 C THR   A 1 17  ? -27.208 -0.913  -29.327 0.25 40.91  ? 60  THR   A OG1 1 
ATOM   105  O OG1 D THR   A 1 17  ? -29.631 -2.146  -27.929 0.25 38.99  ? 60  THR   A OG1 1 
ATOM   106  C CG2 A THR   A 1 17  ? -29.315 -1.258  -28.205 0.25 41.30  ? 60  THR   A CG2 1 
ATOM   107  C CG2 B THR   A 1 17  ? -28.382 -2.703  -29.897 0.25 40.08  ? 60  THR   A CG2 1 
ATOM   108  C CG2 C THR   A 1 17  ? -29.315 -1.258  -28.205 0.25 41.30  ? 60  THR   A CG2 1 
ATOM   109  C CG2 D THR   A 1 17  ? -28.382 -2.703  -29.897 0.25 40.08  ? 60  THR   A CG2 1 
ATOM   110  N N   . TRP   A 1 18  ? -25.938 -4.420  -28.577 1.00 41.52  ? 61  TRP   A N   1 
ATOM   111  C CA  . TRP   A 1 18  ? -24.890 -4.993  -29.443 1.00 49.41  ? 61  TRP   A CA  1 
ATOM   112  C C   . TRP   A 1 18  ? -25.161 -4.438  -30.842 1.00 50.55  ? 61  TRP   A C   1 
ATOM   113  O O   . TRP   A 1 18  ? -26.295 -4.576  -31.322 1.00 54.33  ? 61  TRP   A O   1 
ATOM   114  C CB  . TRP   A 1 18  ? -24.969 -6.520  -29.422 1.00 55.35  ? 61  TRP   A CB  1 
ATOM   115  C CG  . TRP   A 1 18  ? -23.907 -7.156  -30.255 1.00 61.27  ? 61  TRP   A CG  1 
ATOM   116  C CD1 . TRP   A 1 18  ? -23.944 -7.375  -31.598 1.00 66.22  ? 61  TRP   A CD1 1 
ATOM   117  C CD2 . TRP   A 1 18  ? -22.624 -7.616  -29.801 1.00 67.87  ? 61  TRP   A CD2 1 
ATOM   118  N NE1 . TRP   A 1 18  ? -22.771 -7.941  -32.010 1.00 69.15  ? 61  TRP   A NE1 1 
ATOM   119  C CE2 . TRP   A 1 18  ? -21.944 -8.106  -30.932 1.00 69.64  ? 61  TRP   A CE2 1 
ATOM   120  C CE3 . TRP   A 1 18  ? -21.989 -7.671  -28.557 1.00 67.16  ? 61  TRP   A CE3 1 
ATOM   121  C CZ2 . TRP   A 1 18  ? -20.664 -8.648  -30.848 1.00 70.94  ? 61  TRP   A CZ2 1 
ATOM   122  C CZ3 . TRP   A 1 18  ? -20.723 -8.201  -28.475 1.00 67.25  ? 61  TRP   A CZ3 1 
ATOM   123  C CH2 . TRP   A 1 18  ? -20.069 -8.681  -29.607 1.00 70.26  ? 61  TRP   A CH2 1 
ATOM   124  N N   A GLU   A 1 19  ? -24.157 -3.832  -31.478 0.25 52.06  ? 62  GLU   A N   1 
ATOM   125  N N   B GLU   A 1 19  ? -24.157 -3.832  -31.478 0.25 52.06  ? 62  GLU   A N   1 
ATOM   126  N N   C GLU   A 1 19  ? -24.153 -3.785  -31.433 0.25 49.85  ? 62  GLU   A N   1 
ATOM   127  N N   D GLU   A 1 19  ? -24.153 -3.785  -31.433 0.25 49.85  ? 62  GLU   A N   1 
ATOM   128  C CA  A GLU   A 1 19  ? -24.276 -3.273  -32.851 0.25 54.70  ? 62  GLU   A CA  1 
ATOM   129  C CA  B GLU   A 1 19  ? -24.276 -3.273  -32.851 0.25 54.70  ? 62  GLU   A CA  1 
ATOM   130  C CA  C GLU   A 1 19  ? -24.155 -3.276  -32.832 0.25 51.30  ? 62  GLU   A CA  1 
ATOM   131  C CA  D GLU   A 1 19  ? -24.155 -3.276  -32.832 0.25 51.30  ? 62  GLU   A CA  1 
ATOM   132  C C   A GLU   A 1 19  ? -23.394 -4.097  -33.803 0.25 56.84  ? 62  GLU   A C   1 
ATOM   133  C C   B GLU   A 1 19  ? -23.394 -4.097  -33.803 0.25 56.84  ? 62  GLU   A C   1 
ATOM   134  C C   C GLU   A 1 19  ? -23.351 -4.227  -33.726 0.25 54.42  ? 62  GLU   A C   1 
ATOM   135  C C   D GLU   A 1 19  ? -23.351 -4.227  -33.726 0.25 54.42  ? 62  GLU   A C   1 
ATOM   136  O O   A GLU   A 1 19  ? -22.154 -3.929  -33.756 0.25 56.07  ? 62  GLU   A O   1 
ATOM   137  O O   B GLU   A 1 19  ? -22.154 -3.929  -33.756 0.25 56.07  ? 62  GLU   A O   1 
ATOM   138  O O   C GLU   A 1 19  ? -22.113 -4.266  -33.572 0.25 53.73  ? 62  GLU   A O   1 
ATOM   139  O O   D GLU   A 1 19  ? -22.113 -4.266  -33.572 0.25 53.73  ? 62  GLU   A O   1 
ATOM   140  C CB  A GLU   A 1 19  ? -23.909 -1.787  -32.840 0.25 55.40  ? 62  GLU   A CB  1 
ATOM   141  C CB  B GLU   A 1 19  ? -23.909 -1.787  -32.840 0.25 55.40  ? 62  GLU   A CB  1 
ATOM   142  C CB  C GLU   A 1 19  ? -23.509 -1.892  -32.940 0.25 49.26  ? 62  GLU   A CB  1 
ATOM   143  C CB  D GLU   A 1 19  ? -23.509 -1.892  -32.940 0.25 49.26  ? 62  GLU   A CB  1 
ATOM   144  C CG  A GLU   A 1 19  ? -24.435 -1.033  -31.626 0.25 55.02  ? 62  GLU   A CG  1 
ATOM   145  C CG  B GLU   A 1 19  ? -24.435 -1.033  -31.626 0.25 55.02  ? 62  GLU   A CG  1 
ATOM   146  C CG  C GLU   A 1 19  ? -23.246 -1.490  -34.384 0.25 47.34  ? 62  GLU   A CG  1 
ATOM   147  C CG  D GLU   A 1 19  ? -23.246 -1.490  -34.384 0.25 47.34  ? 62  GLU   A CG  1 
ATOM   148  C CD  A GLU   A 1 19  ? -25.939 -0.814  -31.546 0.25 54.16  ? 62  GLU   A CD  1 
ATOM   149  C CD  B GLU   A 1 19  ? -25.939 -0.814  -31.546 0.25 54.16  ? 62  GLU   A CD  1 
ATOM   150  C CD  C GLU   A 1 19  ? -22.231 -0.384  -34.613 0.25 44.55  ? 62  GLU   A CD  1 
ATOM   151  C CD  D GLU   A 1 19  ? -22.231 -0.384  -34.613 0.25 44.55  ? 62  GLU   A CD  1 
ATOM   152  O OE1 A GLU   A 1 19  ? -26.669 -1.354  -32.398 0.25 53.75  ? 62  GLU   A OE1 1 
ATOM   153  O OE1 B GLU   A 1 19  ? -26.669 -1.354  -32.398 0.25 53.75  ? 62  GLU   A OE1 1 
ATOM   154  O OE1 C GLU   A 1 19  ? -21.658 0.116   -33.632 0.25 43.91  ? 62  GLU   A OE1 1 
ATOM   155  O OE1 D GLU   A 1 19  ? -21.658 0.116   -33.632 0.25 43.91  ? 62  GLU   A OE1 1 
ATOM   156  O OE2 A GLU   A 1 19  ? -26.377 -0.101  -30.621 0.25 53.18  ? 62  GLU   A OE2 1 
ATOM   157  O OE2 B GLU   A 1 19  ? -26.377 -0.101  -30.621 0.25 53.18  ? 62  GLU   A OE2 1 
ATOM   158  O OE2 C GLU   A 1 19  ? -22.023 -0.028  -35.785 0.25 44.46  ? 62  GLU   A OE2 1 
ATOM   159  O OE2 D GLU   A 1 19  ? -22.023 -0.028  -35.785 0.25 44.46  ? 62  GLU   A OE2 1 
ATOM   160  N N   . LYS   A 1 20  ? -24.019 -4.944  -34.636 1.00 55.81  ? 63  LYS   A N   1 
ATOM   161  C CA  . LYS   A 1 20  ? -23.324 -5.762  -35.673 1.00 60.16  ? 63  LYS   A CA  1 
ATOM   162  C C   . LYS   A 1 20  ? -22.523 -4.839  -36.588 1.00 62.42  ? 63  LYS   A C   1 
ATOM   163  O O   . LYS   A 1 20  ? -23.032 -3.752  -36.924 1.00 72.42  ? 63  LYS   A O   1 
ATOM   164  C CB  . LYS   A 1 20  ? -24.304 -6.557  -36.533 1.00 64.28  ? 63  LYS   A CB  1 
ATOM   165  C CG  . LYS   A 1 20  ? -25.055 -7.644  -35.780 1.00 73.05  ? 63  LYS   A CG  1 
ATOM   166  C CD  . LYS   A 1 20  ? -26.437 -7.905  -36.327 1.00 77.98  ? 63  LYS   A CD  1 
ATOM   167  C CE  . LYS   A 1 20  ? -27.175 -8.978  -35.557 1.00 86.76  ? 63  LYS   A CE  1 
ATOM   168  N NZ  . LYS   A 1 20  ? -28.463 -9.315  -36.206 1.00 90.55  ? 63  LYS   A NZ  1 
ATOM   169  N N   . ASP   A 1 21  ? -21.305 -5.239  -36.944 1.00 63.48  ? 64  ASP   A N   1 
ATOM   170  C CA  . ASP   A 1 21  ? -20.379 -4.397  -37.746 1.00 71.91  ? 64  ASP   A CA  1 
ATOM   171  C C   . ASP   A 1 21  ? -20.124 -3.107  -36.959 1.00 69.59  ? 64  ASP   A C   1 
ATOM   172  O O   . ASP   A 1 21  ? -20.562 -2.038  -37.419 1.00 72.88  ? 64  ASP   A O   1 
ATOM   173  C CB  . ASP   A 1 21  ? -20.919 -4.132  -39.163 1.00 80.63  ? 64  ASP   A CB  1 
ATOM   174  C CG  . ASP   A 1 21  ? -21.152 -5.376  -40.019 1.00 84.21  ? 64  ASP   A CG  1 
ATOM   175  O OD1 . ASP   A 1 21  ? -20.251 -5.706  -40.829 1.00 85.16  ? 64  ASP   A OD1 1 
ATOM   176  O OD2 . ASP   A 1 21  ? -22.241 -5.997  -39.892 1.00 77.18  ? 64  ASP   A OD2 1 
ATOM   177  N N   . ALA   A 1 22  ? -19.524 -3.242  -35.769 1.00 64.31  ? 65  ALA   A N   1 
ATOM   178  C CA  . ALA   A 1 22  ? -18.802 -2.174  -35.043 1.00 52.04  ? 65  ALA   A CA  1 
ATOM   179  C C   . ALA   A 1 22  ? -17.322 -2.303  -35.394 1.00 48.12  ? 65  ALA   A C   1 
ATOM   180  O O   . ALA   A 1 22  ? -16.912 -3.388  -35.814 1.00 49.70  ? 65  ALA   A O   1 
ATOM   181  C CB  . ALA   A 1 22  ? -19.023 -2.296  -33.557 1.00 54.46  ? 65  ALA   A CB  1 
ATOM   182  N N   . GLU   A 1 23  ? -16.553 -1.233  -35.232 1.00 47.95  ? 66  GLU   A N   1 
ATOM   183  C CA  . GLU   A 1 23  ? -15.077 -1.257  -35.343 1.00 50.32  ? 66  GLU   A CA  1 
ATOM   184  C C   . GLU   A 1 23  ? -14.550 -2.361  -34.414 1.00 57.74  ? 66  GLU   A C   1 
ATOM   185  O O   . GLU   A 1 23  ? -14.872 -2.331  -33.205 1.00 55.11  ? 66  GLU   A O   1 
ATOM   186  C CB  . GLU   A 1 23  ? -14.549 0.129   -34.991 1.00 55.44  ? 66  GLU   A CB  1 
ATOM   187  C CG  . GLU   A 1 23  ? -13.054 0.192   -34.773 1.00 59.14  ? 66  GLU   A CG  1 
ATOM   188  C CD  . GLU   A 1 23  ? -12.613 1.586   -34.379 1.00 66.97  ? 66  GLU   A CD  1 
ATOM   189  O OE1 . GLU   A 1 23  ? -13.098 2.555   -34.997 1.00 72.23  ? 66  GLU   A OE1 1 
ATOM   190  O OE2 . GLU   A 1 23  ? -11.808 1.698   -33.441 1.00 75.90  ? 66  GLU   A OE2 1 
ATOM   191  N N   . VAL   A 1 24  ? -13.832 -3.339  -34.970 1.00 58.90  ? 67  VAL   A N   1 
ATOM   192  C CA  . VAL   A 1 24  ? -13.158 -4.441  -34.216 1.00 55.72  ? 67  VAL   A CA  1 
ATOM   193  C C   . VAL   A 1 24  ? -11.698 -4.044  -34.011 1.00 56.42  ? 67  VAL   A C   1 
ATOM   194  O O   . VAL   A 1 24  ? -11.056 -3.712  -35.002 1.00 55.71  ? 67  VAL   A O   1 
ATOM   195  C CB  . VAL   A 1 24  ? -13.242 -5.793  -34.935 1.00 51.42  ? 67  VAL   A CB  1 
ATOM   196  C CG1 . VAL   A 1 24  ? -12.511 -6.849  -34.132 1.00 51.77  ? 67  VAL   A CG1 1 
ATOM   197  C CG2 . VAL   A 1 24  ? -14.678 -6.223  -35.208 1.00 51.99  ? 67  VAL   A CG2 1 
ATOM   198  N N   . THR   A 1 25  ? -11.188 -4.084  -32.780 1.00 53.41  ? 68  THR   A N   1 
ATOM   199  C CA  . THR   A 1 25  ? -9.803  -3.638  -32.473 1.00 50.28  ? 68  THR   A CA  1 
ATOM   200  C C   . THR   A 1 25  ? -9.378  -4.189  -31.100 1.00 46.84  ? 68  THR   A C   1 
ATOM   201  O O   . THR   A 1 25  ? -10.151 -4.976  -30.540 1.00 42.71  ? 68  THR   A O   1 
ATOM   202  C CB  . THR   A 1 25  ? -9.753  -2.115  -32.616 1.00 52.47  ? 68  THR   A CB  1 
ATOM   203  O OG1 . THR   A 1 25  ? -8.385  -1.718  -32.645 1.00 54.19  ? 68  THR   A OG1 1 
ATOM   204  C CG2 . THR   A 1 25  ? -10.514 -1.397  -31.521 1.00 54.70  ? 68  THR   A CG2 1 
ATOM   205  N N   . GLY   A 1 26  ? -8.181  -3.827  -30.629 1.00 44.17  ? 69  GLY   A N   1 
ATOM   206  C CA  . GLY   A 1 26  ? -7.584  -4.271  -29.352 1.00 48.93  ? 69  GLY   A CA  1 
ATOM   207  C C   . GLY   A 1 26  ? -7.042  -5.697  -29.375 1.00 46.04  ? 69  GLY   A C   1 
ATOM   208  O O   . GLY   A 1 26  ? -7.609  -6.548  -30.078 1.00 50.57  ? 69  GLY   A O   1 
ATOM   209  N N   . ASN   A 1 27  ? -6.018  -5.969  -28.561 1.00 51.37  ? 70  ASN   A N   1 
ATOM   210  C CA  . ASN   A 1 27  ? -5.444  -7.332  -28.358 1.00 50.39  ? 70  ASN   A CA  1 
ATOM   211  C C   . ASN   A 1 27  ? -6.081  -8.006  -27.112 1.00 49.39  ? 70  ASN   A C   1 
ATOM   212  O O   . ASN   A 1 27  ? -7.077  -7.437  -26.547 1.00 40.35  ? 70  ASN   A O   1 
ATOM   213  C CB  . ASN   A 1 27  ? -3.922  -7.227  -28.371 1.00 49.64  ? 70  ASN   A CB  1 
ATOM   214  C CG  . ASN   A 1 27  ? -3.377  -6.365  -27.254 1.00 55.12  ? 70  ASN   A CG  1 
ATOM   215  O OD1 . ASN   A 1 27  ? -3.826  -5.238  -27.045 1.00 58.19  ? 70  ASN   A OD1 1 
ATOM   216  N ND2 . ASN   A 1 27  ? -2.388  -6.878  -26.547 1.00 59.36  ? 70  ASN   A ND2 1 
ATOM   217  N N   . SER   A 1 28  ? -5.588  -9.199  -26.734 1.00 40.50  ? 71  SER   A N   1 
ATOM   218  C CA  . SER   A 1 28  ? -6.117  -10.086 -25.656 1.00 41.56  ? 71  SER   A CA  1 
ATOM   219  C C   . SER   A 1 28  ? -4.990  -10.558 -24.749 1.00 42.45  ? 71  SER   A C   1 
ATOM   220  O O   . SER   A 1 28  ? -4.753  -11.748 -24.665 1.00 44.58  ? 71  SER   A O   1 
ATOM   221  C CB  . SER   A 1 28  ? -6.840  -11.293 -26.213 1.00 41.51  ? 71  SER   A CB  1 
ATOM   222  O OG  . SER   A 1 28  ? -7.555  -10.942 -27.388 1.00 47.93  ? 71  SER   A OG  1 
ATOM   223  N N   . PRO   A 1 29  ? -4.315  -9.657  -24.010 1.00 45.84  ? 72  PRO   A N   1 
ATOM   224  C CA  . PRO   A 1 29  ? -3.149  -10.021 -23.212 1.00 47.95  ? 72  PRO   A CA  1 
ATOM   225  C C   . PRO   A 1 29  ? -3.495  -10.767 -21.912 1.00 51.11  ? 72  PRO   A C   1 
ATOM   226  O O   . PRO   A 1 29  ? -4.457  -10.373 -21.244 1.00 48.41  ? 72  PRO   A O   1 
ATOM   227  C CB  . PRO   A 1 29  ? -2.513  -8.652  -22.907 1.00 50.74  ? 72  PRO   A CB  1 
ATOM   228  C CG  . PRO   A 1 29  ? -3.692  -7.695  -22.835 1.00 48.07  ? 72  PRO   A CG  1 
ATOM   229  C CD  . PRO   A 1 29  ? -4.698  -8.246  -23.830 1.00 50.57  ? 72  PRO   A CD  1 
ATOM   230  N N   . ARG   A 1 30  ? -2.716  -11.813 -21.597 1.00 52.71  ? 73  ARG   A N   1 
ATOM   231  C CA  . ARG   A 1 30  ? -2.781  -12.595 -20.328 1.00 57.74  ? 73  ARG   A CA  1 
ATOM   232  C C   . ARG   A 1 30  ? -1.766  -11.993 -19.344 1.00 54.05  ? 73  ARG   A C   1 
ATOM   233  O O   . ARG   A 1 30  ? -0.582  -12.198 -19.572 1.00 49.70  ? 73  ARG   A O   1 
ATOM   234  C CB  . ARG   A 1 30  ? -2.517  -14.080 -20.604 1.00 62.55  ? 73  ARG   A CB  1 
ATOM   235  C CG  . ARG   A 1 30  ? -3.586  -14.743 -21.465 1.00 74.45  ? 73  ARG   A CG  1 
ATOM   236  C CD  . ARG   A 1 30  ? -3.133  -15.997 -22.210 1.00 88.97  ? 73  ARG   A CD  1 
ATOM   237  N NE  . ARG   A 1 30  ? -4.245  -16.634 -22.926 1.00 94.13  ? 73  ARG   A NE  1 
ATOM   238  C CZ  . ARG   A 1 30  ? -4.805  -17.815 -22.635 1.00 97.69  ? 73  ARG   A CZ  1 
ATOM   239  N NH1 . ARG   A 1 30  ? -4.358  -18.559 -21.635 1.00 102.98 ? 73  ARG   A NH1 1 
ATOM   240  N NH2 . ARG   A 1 30  ? -5.817  -18.261 -23.363 1.00 91.40  ? 73  ARG   A NH2 1 
ATOM   241  N N   . LEU   A 1 31  ? -2.219  -11.256 -18.319 1.00 50.24  ? 74  LEU   A N   1 
ATOM   242  C CA  . LEU   A 1 31  ? -1.348  -10.516 -17.366 1.00 50.15  ? 74  LEU   A CA  1 
ATOM   243  C C   . LEU   A 1 31  ? -1.523  -11.063 -15.939 1.00 50.98  ? 74  LEU   A C   1 
ATOM   244  O O   . LEU   A 1 31  ? -2.680  -11.305 -15.517 1.00 46.00  ? 74  LEU   A O   1 
ATOM   245  C CB  . LEU   A 1 31  ? -1.707  -9.029  -17.418 1.00 51.76  ? 74  LEU   A CB  1 
ATOM   246  C CG  . LEU   A 1 31  ? -1.423  -8.311  -18.738 1.00 52.17  ? 74  LEU   A CG  1 
ATOM   247  C CD1 . LEU   A 1 31  ? -2.089  -6.943  -18.748 1.00 49.98  ? 74  LEU   A CD1 1 
ATOM   248  C CD2 . LEU   A 1 31  ? 0.081   -8.188  -18.988 1.00 48.48  ? 74  LEU   A CD2 1 
ATOM   249  N N   . ASP   A 1 32  ? -0.410  -11.217 -15.215 1.00 47.25  ? 75  ASP   A N   1 
ATOM   250  C CA  . ASP   A 1 32  ? -0.385  -11.519 -13.760 1.00 47.47  ? 75  ASP   A CA  1 
ATOM   251  C C   . ASP   A 1 32  ? -0.505  -10.218 -12.989 1.00 40.73  ? 75  ASP   A C   1 
ATOM   252  O O   . ASP   A 1 32  ? 0.362   -9.337  -13.176 1.00 41.99  ? 75  ASP   A O   1 
ATOM   253  C CB  . ASP   A 1 32  ? 0.913   -12.191 -13.321 1.00 53.05  ? 75  ASP   A CB  1 
ATOM   254  C CG  . ASP   A 1 32  ? 1.049   -13.574 -13.912 1.00 57.57  ? 75  ASP   A CG  1 
ATOM   255  O OD1 . ASP   A 1 32  ? 0.022   -14.109 -14.388 1.00 60.04  ? 75  ASP   A OD1 1 
ATOM   256  O OD2 . ASP   A 1 32  ? 2.176   -14.091 -13.904 1.00 68.34  ? 75  ASP   A OD2 1 
ATOM   257  N N   . VAL   A 1 33  ? -1.547  -10.103 -12.169 1.00 40.20  ? 76  VAL   A N   1 
ATOM   258  C CA  . VAL   A 1 33  ? -1.885  -8.812  -11.494 1.00 43.71  ? 76  VAL   A CA  1 
ATOM   259  C C   . VAL   A 1 33  ? -2.247  -9.114  -10.036 1.00 41.15  ? 76  VAL   A C   1 
ATOM   260  O O   . VAL   A 1 33  ? -2.744  -10.245 -9.746  1.00 38.31  ? 76  VAL   A O   1 
ATOM   261  C CB  . VAL   A 1 33  ? -3.029  -8.037  -12.204 1.00 42.63  ? 76  VAL   A CB  1 
ATOM   262  C CG1 . VAL   A 1 33  ? -2.766  -7.829  -13.685 1.00 44.92  ? 76  VAL   A CG1 1 
ATOM   263  C CG2 . VAL   A 1 33  ? -4.378  -8.714  -12.017 1.00 42.99  ? 76  VAL   A CG2 1 
ATOM   264  N N   . ALA   A 1 34  ? -2.064  -8.112  -9.176  1.00 36.70  ? 77  ALA   A N   1 
ATOM   265  C CA  . ALA   A 1 34  ? -2.495  -8.125  -7.761  1.00 36.29  ? 77  ALA   A CA  1 
ATOM   266  C C   . ALA   A 1 34  ? -3.474  -6.972  -7.552  1.00 36.80  ? 77  ALA   A C   1 
ATOM   267  O O   . ALA   A 1 34  ? -3.289  -5.916  -8.172  1.00 36.50  ? 77  ALA   A O   1 
ATOM   268  C CB  . ALA   A 1 34  ? -1.301  -8.002  -6.855  1.00 34.46  ? 77  ALA   A CB  1 
ATOM   269  N N   . LEU   A 1 35  ? -4.470  -7.192  -6.711  1.00 33.71  ? 78  LEU   A N   1 
ATOM   270  C CA  . LEU   A 1 35  ? -5.512  -6.208  -6.353  1.00 40.04  ? 78  LEU   A CA  1 
ATOM   271  C C   . LEU   A 1 35  ? -5.300  -5.843  -4.879  1.00 40.74  ? 78  LEU   A C   1 
ATOM   272  O O   . LEU   A 1 35  ? -5.321  -6.764  -4.036  1.00 43.80  ? 78  LEU   A O   1 
ATOM   273  C CB  . LEU   A 1 35  ? -6.872  -6.861  -6.640  1.00 36.73  ? 78  LEU   A CB  1 
ATOM   274  C CG  . LEU   A 1 35  ? -8.113  -6.056  -6.252  1.00 36.82  ? 78  LEU   A CG  1 
ATOM   275  C CD1 . LEU   A 1 35  ? -8.208  -4.762  -7.024  1.00 33.17  ? 78  LEU   A CD1 1 
ATOM   276  C CD2 . LEU   A 1 35  ? -9.371  -6.884  -6.446  1.00 37.83  ? 78  LEU   A CD2 1 
ATOM   277  N N   . ASP   A 1 36  ? -5.035  -4.575  -4.577  1.00 37.50  ? 79  ASP   A N   1 
ATOM   278  C CA  . ASP   A 1 36  ? -4.761  -4.134  -3.182  1.00 39.66  ? 79  ASP   A CA  1 
ATOM   279  C C   . ASP   A 1 36  ? -6.076  -3.699  -2.519  1.00 40.56  ? 79  ASP   A C   1 
ATOM   280  O O   . ASP   A 1 36  ? -7.130  -3.681  -3.203  1.00 38.00  ? 79  ASP   A O   1 
ATOM   281  C CB  . ASP   A 1 36  ? -3.665  -3.062  -3.129  1.00 40.62  ? 79  ASP   A CB  1 
ATOM   282  C CG  . ASP   A 1 36  ? -4.068  -1.669  -3.579  1.00 40.43  ? 79  ASP   A CG  1 
ATOM   283  O OD1 . ASP   A 1 36  ? -5.264  -1.425  -3.747  1.00 39.92  ? 79  ASP   A OD1 1 
ATOM   284  O OD2 . ASP   A 1 36  ? -3.163  -0.830  -3.751  1.00 45.49  ? 79  ASP   A OD2 1 
ATOM   285  N N   . GLU   A 1 37  ? -6.013  -3.362  -1.225  1.00 41.56  ? 80  GLU   A N   1 
ATOM   286  C CA  . GLU   A 1 37  ? -7.202  -3.059  -0.389  1.00 39.15  ? 80  GLU   A CA  1 
ATOM   287  C C   . GLU   A 1 37  ? -7.875  -1.764  -0.893  1.00 36.19  ? 80  GLU   A C   1 
ATOM   288  O O   . GLU   A 1 37  ? -9.099  -1.652  -0.703  1.00 33.32  ? 80  GLU   A O   1 
ATOM   289  C CB  . GLU   A 1 37  ? -6.792  -3.012  1.088   1.00 44.35  ? 80  GLU   A CB  1 
ATOM   290  C CG  . GLU   A 1 37  ? -7.974  -3.072  2.049   1.00 48.65  ? 80  GLU   A CG  1 
ATOM   291  C CD  . GLU   A 1 37  ? -7.603  -3.095  3.527   1.00 53.89  ? 80  GLU   A CD  1 
ATOM   292  O OE1 . GLU   A 1 37  ? -7.359  -2.005  4.100   1.00 56.12  ? 80  GLU   A OE1 1 
ATOM   293  O OE2 . GLU   A 1 37  ? -7.540  -4.206  4.100   1.00 55.45  ? 80  GLU   A OE2 1 
ATOM   294  N N   . SER   A 1 38  ? -7.147  -0.863  -1.572  1.00 32.53  ? 81  SER   A N   1 
ATOM   295  C CA  . SER   A 1 38  ? -7.674  0.394   -2.171  1.00 36.78  ? 81  SER   A CA  1 
ATOM   296  C C   . SER   A 1 38  ? -8.327  0.149   -3.529  1.00 37.90  ? 81  SER   A C   1 
ATOM   297  O O   . SER   A 1 38  ? -8.753  1.141   -4.143  1.00 38.91  ? 81  SER   A O   1 
ATOM   298  C CB  . SER   A 1 38  ? -6.613  1.415   -2.308  1.00 39.48  ? 81  SER   A CB  1 
ATOM   299  O OG  . SER   A 1 38  ? -6.087  1.671   -1.036  1.00 45.34  ? 81  SER   A OG  1 
ATOM   300  N N   . GLY   A 1 39  ? -8.404  -1.107  -3.975  1.00 36.37  ? 82  GLY   A N   1 
ATOM   301  C CA  . GLY   A 1 39  ? -8.961  -1.478  -5.287  1.00 36.93  ? 82  GLY   A CA  1 
ATOM   302  C C   . GLY   A 1 39  ? -8.064  -1.054  -6.443  1.00 36.36  ? 82  GLY   A C   1 
ATOM   303  O O   . GLY   A 1 39  ? -8.591  -0.892  -7.534  1.00 39.03  ? 82  GLY   A O   1 
ATOM   304  N N   . ASP   A 1 40  ? -6.757  -0.901  -6.224  1.00 38.34  ? 83  ASP   A N   1 
ATOM   305  C CA  . ASP   A 1 40  ? -5.771  -0.605  -7.295  1.00 40.93  ? 83  ASP   A CA  1 
ATOM   306  C C   . ASP   A 1 40  ? -5.115  -1.922  -7.746  1.00 38.42  ? 83  ASP   A C   1 
ATOM   307  O O   . ASP   A 1 40  ? -4.545  -2.637  -6.913  1.00 38.11  ? 83  ASP   A O   1 
ATOM   308  C CB  . ASP   A 1 40  ? -4.821  0.502   -6.830  1.00 41.30  ? 83  ASP   A CB  1 
ATOM   309  C CG  . ASP   A 1 40  ? -5.565  1.808   -6.576  1.00 49.31  ? 83  ASP   A CG  1 
ATOM   310  O OD1 . ASP   A 1 40  ? -6.597  2.048   -7.247  1.00 52.66  ? 83  ASP   A OD1 1 
ATOM   311  O OD2 . ASP   A 1 40  ? -5.117  2.575   -5.718  1.00 55.21  ? 83  ASP   A OD2 1 
ATOM   312  N N   . PHE   A 1 41  ? -5.207  -2.232  -9.040  1.00 39.25  ? 84  PHE   A N   1 
ATOM   313  C CA  . PHE   A 1 41  ? -4.491  -3.362  -9.692  1.00 39.62  ? 84  PHE   A CA  1 
ATOM   314  C C   . PHE   A 1 41  ? -3.017  -3.001  -9.899  1.00 43.86  ? 84  PHE   A C   1 
ATOM   315  O O   . PHE   A 1 41  ? -2.712  -1.821  -10.149 1.00 45.22  ? 84  PHE   A O   1 
ATOM   316  C CB  . PHE   A 1 41  ? -5.139  -3.725  -11.025 1.00 35.72  ? 84  PHE   A CB  1 
ATOM   317  C CG  . PHE   A 1 41  ? -6.432  -4.490  -10.925 1.00 37.79  ? 84  PHE   A CG  1 
ATOM   318  C CD1 . PHE   A 1 41  ? -6.435  -5.826  -10.549 1.00 36.55  ? 84  PHE   A CD1 1 
ATOM   319  C CD2 . PHE   A 1 41  ? -7.647  -3.896  -11.253 1.00 37.70  ? 84  PHE   A CD2 1 
ATOM   320  C CE1 . PHE   A 1 41  ? -7.623  -6.540  -10.488 1.00 37.74  ? 84  PHE   A CE1 1 
ATOM   321  C CE2 . PHE   A 1 41  ? -8.833  -4.612  -11.192 1.00 34.67  ? 84  PHE   A CE2 1 
ATOM   322  C CZ  . PHE   A 1 41  ? -8.817  -5.935  -10.819 1.00 36.71  ? 84  PHE   A CZ  1 
ATOM   323  N N   . SER   A 1 42  ? -2.110  -3.975  -9.792  1.00 44.18  ? 85  SER   A N   1 
ATOM   324  C CA  . SER   A 1 42  ? -0.679  -3.786  -10.139 1.00 42.56  ? 85  SER   A CA  1 
ATOM   325  C C   . SER   A 1 42  ? -0.162  -5.019  -10.883 1.00 45.73  ? 85  SER   A C   1 
ATOM   326  O O   . SER   A 1 42  ? -0.719  -6.115  -10.676 1.00 45.90  ? 85  SER   A O   1 
ATOM   327  C CB  . SER   A 1 42  ? 0.141   -3.463  -8.913  1.00 47.60  ? 85  SER   A CB  1 
ATOM   328  O OG  . SER   A 1 42  ? -0.033  -4.450  -7.905  1.00 46.09  ? 85  SER   A OG  1 
ATOM   329  N N   . LEU   A 1 43  ? 0.849   -4.844  -11.743 1.00 50.39  ? 86  LEU   A N   1 
ATOM   330  C CA  . LEU   A 1 43  ? 1.511   -5.977  -12.447 1.00 52.15  ? 86  LEU   A CA  1 
ATOM   331  C C   . LEU   A 1 43  ? 2.436   -6.702  -11.471 1.00 52.30  ? 86  LEU   A C   1 
ATOM   332  O O   . LEU   A 1 43  ? 3.338   -6.050  -10.910 1.00 53.06  ? 86  LEU   A O   1 
ATOM   333  C CB  . LEU   A 1 43  ? 2.294   -5.453  -13.651 1.00 53.09  ? 86  LEU   A CB  1 
ATOM   334  C CG  . LEU   A 1 43  ? 1.429   -5.132  -14.860 1.00 55.69  ? 86  LEU   A CG  1 
ATOM   335  C CD1 . LEU   A 1 43  ? 2.219   -4.376  -15.914 1.00 61.19  ? 86  LEU   A CD1 1 
ATOM   336  C CD2 . LEU   A 1 43  ? 0.826   -6.397  -15.446 1.00 56.37  ? 86  LEU   A CD2 1 
ATOM   337  N N   . VAL   A 1 44  ? 2.190   -7.992  -11.264 1.00 55.75  ? 87  VAL   A N   1 
ATOM   338  C CA  . VAL   A 1 44  ? 3.131   -8.946  -10.603 1.00 62.28  ? 87  VAL   A CA  1 
ATOM   339  C C   . VAL   A 1 44  ? 4.137   -9.392  -11.668 1.00 71.68  ? 87  VAL   A C   1 
ATOM   340  O O   . VAL   A 1 44  ? 3.708   -9.685  -12.807 1.00 86.53  ? 87  VAL   A O   1 
ATOM   341  C CB  . VAL   A 1 44  ? 2.355   -10.146 -10.028 1.00 61.48  ? 87  VAL   A CB  1 
ATOM   342  C CG1 . VAL   A 1 44  ? 3.274   -11.243 -9.511  1.00 60.17  ? 87  VAL   A CG1 1 
ATOM   343  C CG2 . VAL   A 1 44  ? 1.362   -9.701  -8.964  1.00 60.19  ? 87  VAL   A CG2 1 
ATOM   344  N N   . GLU   A 1 45  ? 5.423   -9.436  -11.338 1.00 82.55  ? 88  GLU   A N   1 
ATOM   345  C CA  . GLU   A 1 45  ? 6.483   -9.785  -12.321 1.00 90.31  ? 88  GLU   A CA  1 
ATOM   346  C C   . GLU   A 1 45  ? 7.501   -10.729 -11.669 1.00 94.19  ? 88  GLU   A C   1 
ATOM   347  O O   . GLU   A 1 45  ? 7.361   -11.949 -11.741 1.00 91.08  ? 88  GLU   A O   1 
ATOM   348  C CB  . GLU   A 1 45  ? 7.124   -8.494  -12.828 1.00 94.07  ? 88  GLU   A CB  1 
ATOM   349  C CG  . GLU   A 1 45  ? 6.178   -7.610  -13.624 1.00 93.09  ? 88  GLU   A CG  1 
ATOM   350  C CD  . GLU   A 1 45  ? 6.110   -7.933  -15.102 1.00 87.30  ? 88  GLU   A CD  1 
ATOM   351  O OE1 . GLU   A 1 45  ? 6.317   -9.111  -15.461 1.00 81.21  ? 88  GLU   A OE1 1 
ATOM   352  O OE2 . GLU   A 1 45  ? 5.870   -6.996  -15.885 1.00 82.19  ? 88  GLU   A OE2 1 
ATOM   353  N N   . GLY   B 2 7   ? -36.500 12.555  -11.912 1.00 71.55  ? 16  GLY   B N   1 
ATOM   354  C CA  . GLY   B 2 7   ? -35.296 12.316  -12.780 1.00 74.82  ? 16  GLY   B CA  1 
ATOM   355  C C   . GLY   B 2 7   ? -35.531 11.267  -13.867 1.00 75.42  ? 16  GLY   B C   1 
ATOM   356  O O   . GLY   B 2 7   ? -36.486 10.454  -13.733 1.00 74.30  ? 16  GLY   B O   1 
ATOM   357  N N   . GLU   B 2 8   ? -34.689 11.277  -14.911 1.00 63.85  ? 17  GLU   B N   1 
ATOM   358  C CA  . GLU   B 2 8   ? -34.673 10.265  -16.005 1.00 54.59  ? 17  GLU   B CA  1 
ATOM   359  C C   . GLU   B 2 8   ? -34.267 8.908   -15.413 1.00 51.75  ? 17  GLU   B C   1 
ATOM   360  O O   . GLU   B 2 8   ? -33.183 8.786   -14.855 1.00 53.53  ? 17  GLU   B O   1 
ATOM   361  C CB  . GLU   B 2 8   ? -33.720 10.704  -17.117 1.00 56.05  ? 17  GLU   B CB  1 
ATOM   362  C CG  . GLU   B 2 8   ? -33.873 9.931   -18.411 1.00 54.15  ? 17  GLU   B CG  1 
ATOM   363  C CD  . GLU   B 2 8   ? -33.183 10.552  -19.624 1.00 57.75  ? 17  GLU   B CD  1 
ATOM   364  O OE1 . GLU   B 2 8   ? -32.186 11.310  -19.435 1.00 52.86  ? 17  GLU   B OE1 1 
ATOM   365  O OE2 . GLU   B 2 8   ? -33.669 10.310  -20.769 1.00 60.90  ? 17  GLU   B OE2 1 
ATOM   366  N N   A THR   B 2 9   ? -35.143 7.911   -15.527 0.25 52.24  ? 18  THR   B N   1 
ATOM   367  N N   B THR   B 2 9   ? -35.162 7.925   -15.533 0.25 51.15  ? 18  THR   B N   1 
ATOM   368  N N   C THR   B 2 9   ? -35.143 7.911   -15.527 0.25 52.24  ? 18  THR   B N   1 
ATOM   369  N N   D THR   B 2 9   ? -35.162 7.925   -15.533 0.25 51.15  ? 18  THR   B N   1 
ATOM   370  C CA  A THR   B 2 9   ? -34.922 6.540   -15.001 0.25 53.15  ? 18  THR   B CA  1 
ATOM   371  C CA  B THR   B 2 9   ? -35.018 6.548   -14.995 0.25 51.22  ? 18  THR   B CA  1 
ATOM   372  C CA  C THR   B 2 9   ? -34.922 6.540   -15.001 0.25 53.15  ? 18  THR   B CA  1 
ATOM   373  C CA  D THR   B 2 9   ? -35.018 6.548   -14.995 0.25 51.22  ? 18  THR   B CA  1 
ATOM   374  C C   A THR   B 2 9   ? -34.993 5.519   -16.139 0.25 51.42  ? 18  THR   B C   1 
ATOM   375  C C   B THR   B 2 9   ? -34.904 5.533   -16.139 0.25 50.49  ? 18  THR   B C   1 
ATOM   376  C C   C THR   B 2 9   ? -34.993 5.519   -16.139 0.25 51.42  ? 18  THR   B C   1 
ATOM   377  C C   D THR   B 2 9   ? -34.904 5.533   -16.139 0.25 50.49  ? 18  THR   B C   1 
ATOM   378  O O   A THR   B 2 9   ? -35.004 4.312   -15.831 0.25 51.44  ? 18  THR   B O   1 
ATOM   379  O O   B THR   B 2 9   ? -34.680 4.347   -15.833 0.25 51.00  ? 18  THR   B O   1 
ATOM   380  O O   C THR   B 2 9   ? -35.004 4.312   -15.831 0.25 51.44  ? 18  THR   B O   1 
ATOM   381  O O   D THR   B 2 9   ? -34.680 4.347   -15.833 0.25 51.00  ? 18  THR   B O   1 
ATOM   382  C CB  A THR   B 2 9   ? -35.938 6.216   -13.901 0.25 55.01  ? 18  THR   B CB  1 
ATOM   383  C CB  B THR   B 2 9   ? -36.206 6.192   -14.092 0.25 51.30  ? 18  THR   B CB  1 
ATOM   384  C CB  C THR   B 2 9   ? -35.938 6.216   -13.901 0.25 55.01  ? 18  THR   B CB  1 
ATOM   385  C CB  D THR   B 2 9   ? -36.206 6.192   -14.092 0.25 51.30  ? 18  THR   B CB  1 
ATOM   386  O OG1 A THR   B 2 9   ? -36.080 7.387   -13.097 0.25 56.93  ? 18  THR   B OG1 1 
ATOM   387  O OG1 B THR   B 2 9   ? -37.407 6.408   -14.832 0.25 49.29  ? 18  THR   B OG1 1 
ATOM   388  O OG1 C THR   B 2 9   ? -36.080 7.387   -13.097 0.25 56.93  ? 18  THR   B OG1 1 
ATOM   389  O OG1 D THR   B 2 9   ? -37.407 6.408   -14.832 0.25 49.29  ? 18  THR   B OG1 1 
ATOM   390  C CG2 A THR   B 2 9   ? -35.521 5.037   -13.049 0.25 55.36  ? 18  THR   B CG2 1 
ATOM   391  C CG2 B THR   B 2 9   ? -36.238 7.004   -12.816 0.25 52.62  ? 18  THR   B CG2 1 
ATOM   392  C CG2 C THR   B 2 9   ? -35.521 5.037   -13.049 0.25 55.36  ? 18  THR   B CG2 1 
ATOM   393  C CG2 D THR   B 2 9   ? -36.238 7.004   -12.816 0.25 52.62  ? 18  THR   B CG2 1 
ATOM   394  N N   . THR   B 2 10  ? -35.039 5.978   -17.394 1.00 49.67  ? 19  THR   B N   1 
ATOM   395  C CA  . THR   B 2 10  ? -35.058 5.085   -18.581 1.00 48.85  ? 19  THR   B CA  1 
ATOM   396  C C   . THR   B 2 10  ? -33.756 4.286   -18.574 1.00 38.68  ? 19  THR   B C   1 
ATOM   397  O O   . THR   B 2 10  ? -32.702 4.917   -18.382 1.00 39.36  ? 19  THR   B O   1 
ATOM   398  C CB  . THR   B 2 10  ? -35.227 5.847   -19.910 1.00 52.63  ? 19  THR   B CB  1 
ATOM   399  O OG1 . THR   B 2 10  ? -36.185 6.902   -19.786 1.00 60.67  ? 19  THR   B OG1 1 
ATOM   400  C CG2 . THR   B 2 10  ? -35.692 4.936   -21.028 1.00 51.07  ? 19  THR   B CG2 1 
ATOM   401  N N   . ASP   B 2 11  ? -33.838 2.965   -18.730 1.00 35.83  ? 20  ASP   B N   1 
ATOM   402  C CA  . ASP   B 2 11  ? -32.647 2.102   -18.929 1.00 38.87  ? 20  ASP   B CA  1 
ATOM   403  C C   . ASP   B 2 11  ? -31.756 2.717   -20.012 1.00 43.42  ? 20  ASP   B C   1 
ATOM   404  O O   . ASP   B 2 11  ? -32.304 3.388   -20.925 1.00 46.49  ? 20  ASP   B O   1 
ATOM   405  C CB  . ASP   B 2 11  ? -33.028 0.676   -19.311 1.00 37.83  ? 20  ASP   B CB  1 
ATOM   406  C CG  . ASP   B 2 11  ? -33.672 -0.112  -18.181 1.00 42.97  ? 20  ASP   B CG  1 
ATOM   407  O OD1 . ASP   B 2 11  ? -33.745 0.434   -17.068 1.00 35.76  ? 20  ASP   B OD1 1 
ATOM   408  O OD2 . ASP   B 2 11  ? -34.122 -1.259  -18.444 1.00 48.56  ? 20  ASP   B OD2 1 
ATOM   409  N N   . GLY   B 2 12  ? -30.438 2.525   -19.895 1.00 38.44  ? 21  GLY   B N   1 
ATOM   410  C CA  . GLY   B 2 12  ? -29.453 2.936   -20.911 1.00 34.67  ? 21  GLY   B CA  1 
ATOM   411  C C   . GLY   B 2 12  ? -28.153 3.348   -20.281 1.00 35.07  ? 21  GLY   B C   1 
ATOM   412  O O   . GLY   B 2 12  ? -27.986 3.120   -19.077 1.00 32.94  ? 21  GLY   B O   1 
ATOM   413  N N   . VAL   B 2 13  ? -27.304 4.005   -21.061 1.00 32.51  ? 22  VAL   B N   1 
ATOM   414  C CA  . VAL   B 2 13  ? -25.971 4.495   -20.633 1.00 31.43  ? 22  VAL   B CA  1 
ATOM   415  C C   . VAL   B 2 13  ? -26.027 6.012   -20.481 1.00 30.93  ? 22  VAL   B C   1 
ATOM   416  O O   . VAL   B 2 13  ? -26.722 6.697   -21.264 1.00 31.39  ? 22  VAL   B O   1 
ATOM   417  C CB  . VAL   B 2 13  ? -24.856 4.000   -21.580 1.00 34.56  ? 22  VAL   B CB  1 
ATOM   418  C CG1 . VAL   B 2 13  ? -24.956 4.599   -22.986 1.00 35.15  ? 22  VAL   B CG1 1 
ATOM   419  C CG2 . VAL   B 2 13  ? -23.477 4.248   -21.000 1.00 32.88  ? 22  VAL   B CG2 1 
ATOM   420  N N   . TYR   B 2 14  ? -25.343 6.514   -19.460 1.00 32.90  ? 23  TYR   B N   1 
ATOM   421  C CA  . TYR   B 2 14  ? -25.371 7.938   -19.071 1.00 31.89  ? 23  TYR   B CA  1 
ATOM   422  C C   . TYR   B 2 14  ? -23.965 8.410   -18.816 1.00 31.49  ? 23  TYR   B C   1 
ATOM   423  O O   . TYR   B 2 14  ? -23.147 7.638   -18.264 1.00 33.37  ? 23  TYR   B O   1 
ATOM   424  C CB  . TYR   B 2 14  ? -26.146 8.147   -17.774 1.00 32.37  ? 23  TYR   B CB  1 
ATOM   425  C CG  . TYR   B 2 14  ? -27.620 7.944   -17.884 1.00 30.27  ? 23  TYR   B CG  1 
ATOM   426  C CD1 . TYR   B 2 14  ? -28.135 6.698   -18.152 1.00 28.20  ? 23  TYR   B CD1 1 
ATOM   427  C CD2 . TYR   B 2 14  ? -28.497 9.006   -17.701 1.00 31.83  ? 23  TYR   B CD2 1 
ATOM   428  C CE1 . TYR   B 2 14  ? -29.493 6.483   -18.231 1.00 32.44  ? 23  TYR   B CE1 1 
ATOM   429  C CE2 . TYR   B 2 14  ? -29.869 8.813   -17.786 1.00 31.29  ? 23  TYR   B CE2 1 
ATOM   430  C CZ  . TYR   B 2 14  ? -30.366 7.550   -18.041 1.00 34.64  ? 23  TYR   B CZ  1 
ATOM   431  O OH  . TYR   B 2 14  ? -31.710 7.347   -18.128 1.00 35.96  ? 23  TYR   B OH  1 
ATOM   432  N N   . ARG   B 2 15  ? -23.723 9.667   -19.144 1.00 31.86  ? 24  ARG   B N   1 
ATOM   433  C CA  . ARG   B 2 15  ? -22.506 10.387  -18.711 1.00 31.53  ? 24  ARG   B CA  1 
ATOM   434  C C   . ARG   B 2 15  ? -22.698 10.890  -17.277 1.00 33.38  ? 24  ARG   B C   1 
ATOM   435  O O   . ARG   B 2 15  ? -23.784 11.397  -16.964 1.00 32.48  ? 24  ARG   B O   1 
ATOM   436  C CB  . ARG   B 2 15  ? -22.223 11.570  -19.636 1.00 31.58  ? 24  ARG   B CB  1 
ATOM   437  C CG  . ARG   B 2 15  ? -22.183 11.218  -21.114 1.00 34.53  ? 24  ARG   B CG  1 
ATOM   438  C CD  . ARG   B 2 15  ? -22.297 12.469  -21.960 1.00 38.86  ? 24  ARG   B CD  1 
ATOM   439  N NE  . ARG   B 2 15  ? -22.428 12.117  -23.374 1.00 41.03  ? 24  ARG   B NE  1 
ATOM   440  C CZ  . ARG   B 2 15  ? -21.406 11.937  -24.217 1.00 38.50  ? 24  ARG   B CZ  1 
ATOM   441  N NH1 . ARG   B 2 15  ? -20.160 12.076  -23.801 1.00 37.79  ? 24  ARG   B NH1 1 
ATOM   442  N NH2 . ARG   B 2 15  ? -21.648 11.595  -25.470 1.00 44.08  ? 24  ARG   B NH2 1 
ATOM   443  N N   . VAL   B 2 16  ? -21.636 10.833  -16.485 1.00 32.20  ? 25  VAL   B N   1 
ATOM   444  C CA  . VAL   B 2 16  ? -21.537 11.469  -15.150 1.00 34.20  ? 25  VAL   B CA  1 
ATOM   445  C C   . VAL   B 2 16  ? -20.692 12.732  -15.301 1.00 37.49  ? 25  VAL   B C   1 
ATOM   446  O O   . VAL   B 2 16  ? -19.542 12.619  -15.687 1.00 36.03  ? 25  VAL   B O   1 
ATOM   447  C CB  . VAL   B 2 16  ? -20.965 10.479  -14.117 1.00 36.88  ? 25  VAL   B CB  1 
ATOM   448  C CG1 . VAL   B 2 16  ? -20.909 11.105  -12.733 1.00 36.97  ? 25  VAL   B CG1 1 
ATOM   449  C CG2 . VAL   B 2 16  ? -21.745 9.157   -14.113 1.00 34.94  ? 25  VAL   B CG2 1 
ATOM   450  N N   . MET   B 2 17  ? -21.280 13.893  -14.998 1.00 40.44  ? 26  MET   B N   1 
ATOM   451  C CA  . MET   B 2 17  ? -20.709 15.241  -15.240 1.00 37.95  ? 26  MET   B CA  1 
ATOM   452  C C   . MET   B 2 17  ? -20.543 15.962  -13.904 1.00 38.67  ? 26  MET   B C   1 
ATOM   453  O O   . MET   B 2 17  ? -21.322 15.677  -12.990 1.00 39.36  ? 26  MET   B O   1 
ATOM   454  C CB  . MET   B 2 17  ? -21.672 16.050  -16.115 1.00 36.87  ? 26  MET   B CB  1 
ATOM   455  C CG  . MET   B 2 17  ? -22.117 15.339  -17.388 1.00 38.65  ? 26  MET   B CG  1 
ATOM   456  S SD  . MET   B 2 17  ? -20.802 15.119  -18.643 1.00 39.44  ? 26  MET   B SD  1 
ATOM   457  C CE  . MET   B 2 17  ? -20.176 16.796  -18.732 1.00 40.81  ? 26  MET   B CE  1 
ATOM   458  N N   . THR   B 2 18  ? -19.609 16.900  -13.826 1.00 39.75  ? 27  THR   B N   1 
ATOM   459  C CA  . THR   B 2 18  ? -19.469 17.862  -12.704 1.00 47.21  ? 27  THR   B CA  1 
ATOM   460  C C   . THR   B 2 18  ? -19.328 19.280  -13.283 1.00 50.74  ? 27  THR   B C   1 
ATOM   461  O O   . THR   B 2 18  ? -18.836 19.402  -14.448 1.00 43.91  ? 27  THR   B O   1 
ATOM   462  C CB  . THR   B 2 18  ? -18.290 17.479  -11.795 1.00 48.67  ? 27  THR   B CB  1 
ATOM   463  O OG1 . THR   B 2 18  ? -18.205 18.424  -10.722 1.00 45.61  ? 27  THR   B OG1 1 
ATOM   464  C CG2 . THR   B 2 18  ? -16.962 17.413  -12.524 1.00 45.68  ? 27  THR   B CG2 1 
ATOM   465  N N   . ARG   B 2 19  ? -19.725 20.301  -12.508 1.00 52.62  ? 28  ARG   B N   1 
ATOM   466  C CA  . ARG   B 2 19  ? -19.433 21.734  -12.804 1.00 60.11  ? 28  ARG   B CA  1 
ATOM   467  C C   . ARG   B 2 19  ? -18.460 22.322  -11.768 1.00 56.85  ? 28  ARG   B C   1 
ATOM   468  O O   . ARG   B 2 19  ? -18.171 23.529  -11.840 1.00 53.21  ? 28  ARG   B O   1 
ATOM   469  C CB  . ARG   B 2 19  ? -20.742 22.514  -12.915 1.00 62.02  ? 28  ARG   B CB  1 
ATOM   470  C CG  . ARG   B 2 19  ? -21.503 22.180  -14.190 1.00 70.20  ? 28  ARG   B CG  1 
ATOM   471  C CD  . ARG   B 2 19  ? -22.358 23.313  -14.712 1.00 70.97  ? 28  ARG   B CD  1 
ATOM   472  N NE  . ARG   B 2 19  ? -23.427 22.833  -15.576 1.00 73.72  ? 28  ARG   B NE  1 
ATOM   473  C CZ  . ARG   B 2 19  ? -24.532 22.215  -15.155 1.00 81.36  ? 28  ARG   B CZ  1 
ATOM   474  N NH1 . ARG   B 2 19  ? -24.725 21.980  -13.865 1.00 89.68  ? 28  ARG   B NH1 1 
ATOM   475  N NH2 . ARG   B 2 19  ? -25.443 21.822  -16.031 1.00 78.16  ? 28  ARG   B NH2 1 
ATOM   476  N N   . ARG   B 2 20  ? -17.884 21.485  -10.909 1.00 60.89  ? 29  ARG   B N   1 
ATOM   477  C CA  . ARG   B 2 20  ? -17.032 21.946  -9.779  1.00 68.73  ? 29  ARG   B CA  1 
ATOM   478  C C   . ARG   B 2 20  ? -15.662 22.360  -10.325 1.00 69.44  ? 29  ARG   B C   1 
ATOM   479  O O   . ARG   B 2 20  ? -14.828 22.821  -9.526  1.00 75.71  ? 29  ARG   B O   1 
ATOM   480  C CB  . ARG   B 2 20  ? -16.913 20.849  -8.718  1.00 71.13  ? 29  ARG   B CB  1 
ATOM   481  C CG  . ARG   B 2 20  ? -16.689 21.373  -7.307  1.00 80.13  ? 29  ARG   B CG  1 
ATOM   482  C CD  . ARG   B 2 20  ? -16.358 20.244  -6.352  1.00 95.60  ? 29  ARG   B CD  1 
ATOM   483  N NE  . ARG   B 2 20  ? -15.383 19.313  -6.923  1.00 109.31 ? 29  ARG   B NE  1 
ATOM   484  C CZ  . ARG   B 2 20  ? -14.054 19.415  -6.832  1.00 118.25 ? 29  ARG   B CZ  1 
ATOM   485  N NH1 . ARG   B 2 20  ? -13.490 20.418  -6.177  1.00 126.39 ? 29  ARG   B NH1 1 
ATOM   486  N NH2 . ARG   B 2 20  ? -13.285 18.505  -7.407  1.00 114.83 ? 29  ARG   B NH2 1 
ATOM   487  N N   . LEU   B 2 21  ? -15.449 22.180  -11.632 1.00 62.30  ? 30  LEU   B N   1 
ATOM   488  C CA  . LEU   B 2 21  ? -14.195 22.507  -12.361 1.00 62.00  ? 30  LEU   B CA  1 
ATOM   489  C C   . LEU   B 2 21  ? -14.508 23.506  -13.494 1.00 60.07  ? 30  LEU   B C   1 
ATOM   490  O O   . LEU   B 2 21  ? -15.616 24.096  -13.473 1.00 58.60  ? 30  LEU   B O   1 
ATOM   491  C CB  . LEU   B 2 21  ? -13.608 21.182  -12.860 1.00 59.33  ? 30  LEU   B CB  1 
ATOM   492  C CG  . LEU   B 2 21  ? -12.486 20.574  -12.018 1.00 62.54  ? 30  LEU   B CG  1 
ATOM   493  C CD1 . LEU   B 2 21  ? -12.677 20.812  -10.529 1.00 63.46  ? 30  LEU   B CD1 1 
ATOM   494  C CD2 . LEU   B 2 21  ? -12.358 19.086  -12.304 1.00 59.79  ? 30  LEU   B CD2 1 
ATOM   495  N N   . LEU   B 2 22  ? -13.570 23.734  -14.424 1.00 58.56  ? 31  LEU   B N   1 
ATOM   496  C CA  . LEU   B 2 22  ? -13.786 24.625  -15.602 1.00 55.55  ? 31  LEU   B CA  1 
ATOM   497  C C   . LEU   B 2 22  ? -14.868 24.021  -16.504 1.00 55.92  ? 31  LEU   B C   1 
ATOM   498  O O   . LEU   B 2 22  ? -14.814 22.801  -16.718 1.00 62.47  ? 31  LEU   B O   1 
ATOM   499  C CB  . LEU   B 2 22  ? -12.471 24.777  -16.365 1.00 56.50  ? 31  LEU   B CB  1 
ATOM   500  C CG  . LEU   B 2 22  ? -12.462 25.850  -17.454 1.00 55.67  ? 31  LEU   B CG  1 
ATOM   501  C CD1 . LEU   B 2 22  ? -12.195 27.239  -16.859 1.00 48.45  ? 31  LEU   B CD1 1 
ATOM   502  C CD2 . LEU   B 2 22  ? -11.432 25.500  -18.527 1.00 53.53  ? 31  LEU   B CD2 1 
ATOM   503  N N   . GLY   B 2 23  ? -15.804 24.833  -17.017 1.00 50.13  ? 32  GLY   B N   1 
ATOM   504  C CA  . GLY   B 2 23  ? -16.947 24.361  -17.825 1.00 43.72  ? 32  GLY   B CA  1 
ATOM   505  C C   . GLY   B 2 23  ? -17.664 23.168  -17.186 1.00 45.23  ? 32  GLY   B C   1 
ATOM   506  O O   . GLY   B 2 23  ? -17.716 23.062  -15.936 1.00 44.98  ? 32  GLY   B O   1 
ATOM   507  N N   . SER   B 2 24  ? -18.241 22.310  -18.024 1.00 46.94  ? 33  SER   B N   1 
ATOM   508  C CA  . SER   B 2 24  ? -18.924 21.051  -17.642 1.00 44.24  ? 33  SER   B CA  1 
ATOM   509  C C   . SER   B 2 24  ? -18.029 19.873  -18.028 1.00 46.32  ? 33  SER   B C   1 
ATOM   510  O O   . SER   B 2 24  ? -17.847 19.677  -19.231 1.00 44.95  ? 33  SER   B O   1 
ATOM   511  C CB  . SER   B 2 24  ? -20.265 20.971  -18.304 1.00 45.27  ? 33  SER   B CB  1 
ATOM   512  O OG  . SER   B 2 24  ? -21.135 21.962  -17.764 1.00 45.55  ? 33  SER   B OG  1 
ATOM   513  N N   . THR   B 2 25  ? -17.494 19.145  -17.036 1.00 45.21  ? 34  THR   B N   1 
ATOM   514  C CA  . THR   B 2 25  ? -16.450 18.096  -17.192 1.00 42.41  ? 34  THR   B CA  1 
ATOM   515  C C   . THR   B 2 25  ? -17.055 16.705  -16.986 1.00 43.24  ? 34  THR   B C   1 
ATOM   516  O O   . THR   B 2 25  ? -17.716 16.508  -15.943 1.00 43.23  ? 34  THR   B O   1 
ATOM   517  C CB  . THR   B 2 25  ? -15.279 18.318  -16.225 1.00 45.61  ? 34  THR   B CB  1 
ATOM   518  O OG1 . THR   B 2 25  ? -14.830 19.664  -16.385 1.00 47.05  ? 34  THR   B OG1 1 
ATOM   519  C CG2 . THR   B 2 25  ? -14.115 17.371  -16.458 1.00 42.14  ? 34  THR   B CG2 1 
ATOM   520  N N   . GLN   B 2 26  ? -16.827 15.780  -17.930 1.00 39.22  ? 35  GLN   B N   1 
ATOM   521  C CA  . GLN   B 2 26  ? -17.257 14.363  -17.789 1.00 41.50  ? 35  GLN   B CA  1 
ATOM   522  C C   . GLN   B 2 26  ? -16.219 13.647  -16.910 1.00 44.26  ? 35  GLN   B C   1 
ATOM   523  O O   . GLN   B 2 26  ? -15.022 13.636  -17.289 1.00 44.85  ? 35  GLN   B O   1 
ATOM   524  C CB  . GLN   B 2 26  ? -17.432 13.680  -19.144 1.00 37.94  ? 35  GLN   B CB  1 
ATOM   525  C CG  . GLN   B 2 26  ? -18.034 12.280  -19.052 1.00 38.45  ? 35  GLN   B CG  1 
ATOM   526  C CD  . GLN   B 2 26  ? -18.343 11.682  -20.401 1.00 39.00  ? 35  GLN   B CD  1 
ATOM   527  O OE1 . GLN   B 2 26  ? -18.961 12.321  -21.254 1.00 38.41  ? 35  GLN   B OE1 1 
ATOM   528  N NE2 . GLN   B 2 26  ? -17.909 10.449  -20.615 1.00 37.44  ? 35  GLN   B NE2 1 
ATOM   529  N N   . VAL   B 2 27  ? -16.646 13.125  -15.758 1.00 41.38  ? 36  VAL   B N   1 
ATOM   530  C CA  . VAL   B 2 27  ? -15.760 12.394  -14.795 1.00 39.50  ? 36  VAL   B CA  1 
ATOM   531  C C   . VAL   B 2 27  ? -15.924 10.888  -15.012 1.00 34.85  ? 36  VAL   B C   1 
ATOM   532  O O   . VAL   B 2 27  ? -15.085 10.131  -14.549 1.00 41.37  ? 36  VAL   B O   1 
ATOM   533  C CB  . VAL   B 2 27  ? -16.045 12.794  -13.334 1.00 40.34  ? 36  VAL   B CB  1 
ATOM   534  C CG1 . VAL   B 2 27  ? -15.402 14.125  -12.986 1.00 40.86  ? 36  VAL   B CG1 1 
ATOM   535  C CG2 . VAL   B 2 27  ? -17.528 12.829  -13.017 1.00 39.72  ? 36  VAL   B CG2 1 
ATOM   536  N N   . GLY   B 2 28  ? -16.995 10.461  -15.671 1.00 36.23  ? 37  GLY   B N   1 
ATOM   537  C CA  . GLY   B 2 28  ? -17.211 9.043   -15.994 1.00 30.86  ? 37  GLY   B CA  1 
ATOM   538  C C   . GLY   B 2 28  ? -18.561 8.781   -16.624 1.00 29.29  ? 37  GLY   B C   1 
ATOM   539  O O   . GLY   B 2 28  ? -19.169 9.702   -17.153 1.00 32.30  ? 37  GLY   B O   1 
ATOM   540  N N   . VAL   B 2 29  ? -19.000 7.529   -16.534 1.00 28.83  ? 38  VAL   B N   1 
ATOM   541  C CA  . VAL   B 2 29  ? -20.132 6.918   -17.281 1.00 29.10  ? 38  VAL   B CA  1 
ATOM   542  C C   . VAL   B 2 29  ? -20.832 5.960   -16.321 1.00 29.77  ? 38  VAL   B C   1 
ATOM   543  O O   . VAL   B 2 29  ? -20.177 5.525   -15.354 1.00 30.68  ? 38  VAL   B O   1 
ATOM   544  C CB  . VAL   B 2 29  ? -19.631 6.151   -18.525 1.00 31.05  ? 38  VAL   B CB  1 
ATOM   545  C CG1 . VAL   B 2 29  ? -20.782 5.550   -19.325 1.00 34.17  ? 38  VAL   B CG1 1 
ATOM   546  C CG2 . VAL   B 2 29  ? -18.727 6.984   -19.419 1.00 29.80  ? 38  VAL   B CG2 1 
ATOM   547  N N   . GLY   B 2 30  ? -22.079 5.595   -16.597 1.00 27.43  ? 39  GLY   B N   1 
ATOM   548  C CA  . GLY   B 2 30  ? -22.804 4.566   -15.836 1.00 25.82  ? 39  GLY   B CA  1 
ATOM   549  C C   . GLY   B 2 30  ? -23.938 3.977   -16.612 1.00 26.11  ? 39  GLY   B C   1 
ATOM   550  O O   . GLY   B 2 30  ? -24.176 4.426   -17.755 1.00 27.98  ? 39  GLY   B O   1 
ATOM   551  N N   . VAL   B 2 31  ? -24.601 2.998   -16.000 1.00 26.43  ? 40  VAL   B N   1 
ATOM   552  C CA  . VAL   B 2 31  ? -25.687 2.156   -16.563 1.00 27.21  ? 40  VAL   B CA  1 
ATOM   553  C C   . VAL   B 2 31  ? -26.904 2.282   -15.663 1.00 29.39  ? 40  VAL   B C   1 
ATOM   554  O O   . VAL   B 2 31  ? -26.766 1.923   -14.458 1.00 24.58  ? 40  VAL   B O   1 
ATOM   555  C CB  . VAL   B 2 31  ? -25.329 0.663   -16.602 1.00 28.91  ? 40  VAL   B CB  1 
ATOM   556  C CG1 . VAL   B 2 31  ? -26.539 -0.151  -17.035 1.00 30.63  ? 40  VAL   B CG1 1 
ATOM   557  C CG2 . VAL   B 2 31  ? -24.098 0.390   -17.454 1.00 30.14  ? 40  VAL   B CG2 1 
ATOM   558  N N   . MET   B 2 32  ? -28.051 2.656   -16.246 1.00 27.81  ? 41  MET   B N   1 
ATOM   559  C CA  . MET   B 2 32  ? -29.369 2.616   -15.590 1.00 31.30  ? 41  MET   B CA  1 
ATOM   560  C C   . MET   B 2 32  ? -30.066 1.314   -16.011 1.00 29.25  ? 41  MET   B C   1 
ATOM   561  O O   . MET   B 2 32  ? -30.231 1.056   -17.219 1.00 27.80  ? 41  MET   B O   1 
ATOM   562  C CB  . MET   B 2 32  ? -30.183 3.852   -15.987 1.00 31.79  ? 41  MET   B CB  1 
ATOM   563  C CG  . MET   B 2 32  ? -31.394 4.083   -15.106 1.00 38.81  ? 41  MET   B CG  1 
ATOM   564  S SD  . MET   B 2 32  ? -30.942 4.762   -13.491 1.00 35.45  ? 41  MET   B SD  1 
ATOM   565  C CE  . MET   B 2 32  ? -30.595 6.457   -13.951 1.00 38.63  ? 41  MET   B CE  1 
ATOM   566  N N   . GLN   B 2 33  ? -30.437 0.491   -15.044 1.00 28.59  ? 42  GLN   B N   1 
ATOM   567  C CA  . GLN   B 2 33  ? -31.126 -0.783  -15.306 1.00 33.07  ? 42  GLN   B CA  1 
ATOM   568  C C   . GLN   B 2 33  ? -32.019 -1.073  -14.121 1.00 32.35  ? 42  GLN   B C   1 
ATOM   569  O O   . GLN   B 2 33  ? -31.511 -1.007  -12.997 1.00 36.58  ? 42  GLN   B O   1 
ATOM   570  C CB  . GLN   B 2 33  ? -30.157 -1.952  -15.521 1.00 34.66  ? 42  GLN   B CB  1 
ATOM   571  C CG  . GLN   B 2 33  ? -30.913 -3.230  -15.887 1.00 37.63  ? 42  GLN   B CG  1 
ATOM   572  C CD  . GLN   B 2 33  ? -30.045 -4.323  -16.464 1.00 42.42  ? 42  GLN   B CD  1 
ATOM   573  O OE1 . GLN   B 2 33  ? -30.152 -5.486  -16.068 1.00 47.39  ? 42  GLN   B OE1 1 
ATOM   574  N NE2 . GLN   B 2 33  ? -29.138 -3.953  -17.354 1.00 37.40  ? 42  GLN   B NE2 1 
ATOM   575  N N   . GLU   B 2 34  ? -33.276 -1.392  -14.382 1.00 36.57  ? 43  GLU   B N   1 
ATOM   576  C CA  . GLU   B 2 34  ? -34.309 -1.650  -13.349 1.00 38.87  ? 43  GLU   B CA  1 
ATOM   577  C C   . GLU   B 2 34  ? -34.311 -0.536  -12.287 1.00 41.55  ? 43  GLU   B C   1 
ATOM   578  O O   . GLU   B 2 34  ? -34.439 -0.883  -11.114 1.00 39.73  ? 43  GLU   B O   1 
ATOM   579  C CB  . GLU   B 2 34  ? -34.022 -3.017  -12.733 1.00 44.38  ? 43  GLU   B CB  1 
ATOM   580  C CG  . GLU   B 2 34  ? -34.133 -4.153  -13.744 1.00 50.44  ? 43  GLU   B CG  1 
ATOM   581  C CD  . GLU   B 2 34  ? -33.448 -5.453  -13.355 1.00 49.81  ? 43  GLU   B CD  1 
ATOM   582  O OE1 . GLU   B 2 34  ? -33.792 -5.999  -12.301 1.00 50.80  ? 43  GLU   B OE1 1 
ATOM   583  O OE2 . GLU   B 2 34  ? -32.565 -5.906  -14.111 1.00 54.16  ? 43  GLU   B OE2 1 
ATOM   584  N N   . GLY   B 2 35  ? -34.149 0.739   -12.671 1.00 37.23  ? 44  GLY   B N   1 
ATOM   585  C CA  . GLY   B 2 35  ? -34.260 1.913   -11.779 1.00 35.70  ? 44  GLY   B CA  1 
ATOM   586  C C   . GLY   B 2 35  ? -33.047 2.090   -10.876 1.00 36.59  ? 44  GLY   B C   1 
ATOM   587  O O   . GLY   B 2 35  ? -33.107 2.900   -9.914  1.00 34.56  ? 44  GLY   B O   1 
ATOM   588  N N   . VAL   B 2 36  ? -31.971 1.346   -11.130 1.00 29.60  ? 45  VAL   B N   1 
ATOM   589  C CA  . VAL   B 2 36  ? -30.707 1.457   -10.365 1.00 27.35  ? 45  VAL   B CA  1 
ATOM   590  C C   . VAL   B 2 36  ? -29.613 1.977   -11.302 1.00 28.19  ? 45  VAL   B C   1 
ATOM   591  O O   . VAL   B 2 36  ? -29.510 1.486   -12.459 1.00 28.36  ? 45  VAL   B O   1 
ATOM   592  C CB  . VAL   B 2 36  ? -30.381 0.119   -9.676  1.00 29.65  ? 45  VAL   B CB  1 
ATOM   593  C CG1 . VAL   B 2 36  ? -28.995 0.129   -9.050  1.00 31.59  ? 45  VAL   B CG1 1 
ATOM   594  C CG2 . VAL   B 2 36  ? -31.443 -0.198  -8.629  1.00 28.36  ? 45  VAL   B CG2 1 
ATOM   595  N N   . PHE   B 2 37  ? -28.865 2.974   -10.833 1.00 25.56  ? 46  PHE   B N   1 
ATOM   596  C CA  . PHE   B 2 37  ? -27.694 3.526   -11.539 1.00 26.57  ? 46  PHE   B CA  1 
ATOM   597  C C   . PHE   B 2 37  ? -26.410 2.883   -11.012 1.00 27.74  ? 46  PHE   B C   1 
ATOM   598  O O   . PHE   B 2 37  ? -26.128 2.917   -9.805  1.00 26.67  ? 46  PHE   B O   1 
ATOM   599  C CB  . PHE   B 2 37  ? -27.595 5.033   -11.387 1.00 25.57  ? 46  PHE   B CB  1 
ATOM   600  C CG  . PHE   B 2 37  ? -26.627 5.639   -12.369 1.00 27.20  ? 46  PHE   B CG  1 
ATOM   601  C CD1 . PHE   B 2 37  ? -26.800 5.448   -13.730 1.00 26.52  ? 46  PHE   B CD1 1 
ATOM   602  C CD2 . PHE   B 2 37  ? -25.535 6.367   -11.929 1.00 26.49  ? 46  PHE   B CD2 1 
ATOM   603  C CE1 . PHE   B 2 37  ? -25.914 6.001   -14.637 1.00 27.83  ? 46  PHE   B CE1 1 
ATOM   604  C CE2 . PHE   B 2 37  ? -24.654 6.933   -12.835 1.00 30.39  ? 46  PHE   B CE2 1 
ATOM   605  C CZ  . PHE   B 2 37  ? -24.861 6.765   -14.188 1.00 29.68  ? 46  PHE   B CZ  1 
ATOM   606  N N   . HIS   B 2 38  ? -25.637 2.342   -11.935 1.00 27.10  ? 47  HIS   B N   1 
ATOM   607  C CA  . HIS   B 2 38  ? -24.420 1.512   -11.678 1.00 25.66  ? 47  HIS   B CA  1 
ATOM   608  C C   . HIS   B 2 38  ? -23.194 2.234   -12.222 1.00 28.19  ? 47  HIS   B C   1 
ATOM   609  O O   . HIS   B 2 38  ? -23.188 2.572   -13.409 1.00 27.74  ? 47  HIS   B O   1 
ATOM   610  C CB  . HIS   B 2 38  ? -24.556 0.179   -12.380 1.00 26.01  ? 47  HIS   B CB  1 
ATOM   611  C CG  . HIS   B 2 38  ? -25.765 -0.615  -12.036 1.00 23.90  ? 47  HIS   B CG  1 
ATOM   612  N ND1 . HIS   B 2 38  ? -26.991 -0.345  -12.585 1.00 27.98  ? 47  HIS   B ND1 1 
ATOM   613  C CD2 . HIS   B 2 38  ? -25.923 -1.700  -11.248 1.00 23.85  ? 47  HIS   B CD2 1 
ATOM   614  C CE1 . HIS   B 2 38  ? -27.884 -1.187  -12.106 1.00 26.14  ? 47  HIS   B CE1 1 
ATOM   615  N NE2 . HIS   B 2 38  ? -27.255 -2.040  -11.289 1.00 28.17  ? 47  HIS   B NE2 1 
ATOM   616  N N   . THR   B 2 39  ? -22.213 2.534   -11.385 1.00 27.52  ? 48  THR   B N   1 
ATOM   617  C CA  . THR   B 2 39  ? -20.961 3.135   -11.882 1.00 27.33  ? 48  THR   B CA  1 
ATOM   618  C C   . THR   B 2 39  ? -19.772 2.570   -11.099 1.00 27.26  ? 48  THR   B C   1 
ATOM   619  O O   . THR   B 2 39  ? -19.955 1.643   -10.274 1.00 26.90  ? 48  THR   B O   1 
ATOM   620  C CB  . THR   B 2 39  ? -21.132 4.656   -11.951 1.00 28.86  ? 48  THR   B CB  1 
ATOM   621  O OG1 . THR   B 2 39  ? -19.996 5.156   -12.649 1.00 28.30  ? 48  THR   B OG1 1 
ATOM   622  C CG2 . THR   B 2 39  ? -21.235 5.337   -10.601 1.00 31.67  ? 48  THR   B CG2 1 
ATOM   623  N N   . MET   B 2 40  ? -18.584 3.099   -11.368 1.00 28.97  ? 49  MET   B N   1 
ATOM   624  C CA  . MET   B 2 40  ? -17.353 2.726   -10.631 1.00 31.67  ? 49  MET   B CA  1 
ATOM   625  C C   . MET   B 2 40  ? -17.182 3.713   -9.487  1.00 31.89  ? 49  MET   B C   1 
ATOM   626  O O   . MET   B 2 40  ? -17.508 4.920   -9.667  1.00 29.10  ? 49  MET   B O   1 
ATOM   627  C CB  . MET   B 2 40  ? -16.120 2.742   -11.538 1.00 32.49  ? 49  MET   B CB  1 
ATOM   628  C CG  . MET   B 2 40  ? -16.348 2.028   -12.866 1.00 36.33  ? 49  MET   B CG  1 
ATOM   629  S SD  . MET   B 2 40  ? -14.886 1.119   -13.445 1.00 42.25  ? 49  MET   B SD  1 
ATOM   630  C CE  . MET   B 2 40  ? -15.010 -0.353  -12.427 1.00 37.42  ? 49  MET   B CE  1 
ATOM   631  N N   A TRP   B 2 41  ? -16.671 3.233   -8.349  0.13 31.59  ? 50  TRP   B N   1 
ATOM   632  N N   B TRP   B 2 41  ? -16.688 3.241   -8.335  0.19 30.88  ? 50  TRP   B N   1 
ATOM   633  N N   C TRP   B 2 41  ? -16.673 3.231   -8.348  0.35 31.11  ? 50  TRP   B N   1 
ATOM   634  N N   D TRP   B 2 41  ? -16.690 3.239   -8.335  0.33 30.56  ? 50  TRP   B N   1 
ATOM   635  C CA  A TRP   B 2 41  ? -16.508 4.033   -7.106  0.13 32.62  ? 50  TRP   B CA  1 
ATOM   636  C CA  B TRP   B 2 41  ? -16.539 4.067   -7.106  0.19 31.67  ? 50  TRP   B CA  1 
ATOM   637  C CA  C TRP   B 2 41  ? -16.507 4.031   -7.107  0.35 32.53  ? 50  TRP   B CA  1 
ATOM   638  C CA  D TRP   B 2 41  ? -16.538 4.065   -7.107  0.33 31.62  ? 50  TRP   B CA  1 
ATOM   639  C C   A TRP   B 2 41  ? -15.604 5.243   -7.371  0.13 32.74  ? 50  TRP   B C   1 
ATOM   640  C C   B TRP   B 2 41  ? -15.612 5.260   -7.384  0.19 32.24  ? 50  TRP   B C   1 
ATOM   641  C C   C TRP   B 2 41  ? -15.604 5.243   -7.375  0.35 32.93  ? 50  TRP   B C   1 
ATOM   642  C C   D TRP   B 2 41  ? -15.612 5.259   -7.386  0.33 32.38  ? 50  TRP   B C   1 
ATOM   643  O O   A TRP   B 2 41  ? -15.910 6.325   -6.839  0.13 32.65  ? 50  TRP   B O   1 
ATOM   644  O O   B TRP   B 2 41  ? -15.915 6.354   -6.877  0.19 32.20  ? 50  TRP   B O   1 
ATOM   645  O O   C TRP   B 2 41  ? -15.908 6.324   -6.843  0.35 32.73  ? 50  TRP   B O   1 
ATOM   646  O O   D TRP   B 2 41  ? -15.913 6.352   -6.879  0.33 32.27  ? 50  TRP   B O   1 
ATOM   647  C CB  A TRP   B 2 41  ? -15.974 3.185   -5.944  0.13 33.51  ? 50  TRP   B CB  1 
ATOM   648  C CB  B TRP   B 2 41  ? -16.056 3.250   -5.896  0.19 31.89  ? 50  TRP   B CB  1 
ATOM   649  C CB  C TRP   B 2 41  ? -15.971 3.183   -5.944  0.35 33.68  ? 50  TRP   B CB  1 
ATOM   650  C CB  D TRP   B 2 41  ? -16.054 3.248   -5.896  0.33 32.01  ? 50  TRP   B CB  1 
ATOM   651  C CG  A TRP   B 2 41  ? -16.123 3.880   -4.626  0.13 33.95  ? 50  TRP   B CG  1 
ATOM   652  C CG  B TRP   B 2 41  ? -15.951 4.083   -4.652  0.19 31.46  ? 50  TRP   B CG  1 
ATOM   653  C CG  C TRP   B 2 41  ? -16.121 3.878   -4.626  0.35 33.87  ? 50  TRP   B CG  1 
ATOM   654  C CG  D TRP   B 2 41  ? -15.950 4.081   -4.651  0.33 31.38  ? 50  TRP   B CG  1 
ATOM   655  C CD1 A TRP   B 2 41  ? -17.170 3.771   -3.758  0.13 33.93  ? 50  TRP   B CD1 1 
ATOM   656  C CD1 B TRP   B 2 41  ? -14.906 4.883   -4.294  0.19 31.21  ? 50  TRP   B CD1 1 
ATOM   657  C CD1 C TRP   B 2 41  ? -17.171 3.769   -3.761  0.35 33.54  ? 50  TRP   B CD1 1 
ATOM   658  C CD1 D TRP   B 2 41  ? -14.905 4.882   -4.293  0.33 31.06  ? 50  TRP   B CD1 1 
ATOM   659  C CD2 A TRP   B 2 41  ? -15.222 4.844   -4.050  0.13 34.45  ? 50  TRP   B CD2 1 
ATOM   660  C CD2 B TRP   B 2 41  ? -16.949 4.250   -3.627  0.19 31.66  ? 50  TRP   B CD2 1 
ATOM   661  C CD2 C TRP   B 2 41  ? -15.219 4.842   -4.050  0.35 34.26  ? 50  TRP   B CD2 1 
ATOM   662  C CD2 D TRP   B 2 41  ? -16.948 4.249   -3.626  0.33 31.64  ? 50  TRP   B CD2 1 
ATOM   663  N NE1 A TRP   B 2 41  ? -16.972 4.579   -2.671  0.13 34.81  ? 50  TRP   B NE1 1 
ATOM   664  N NE1 B TRP   B 2 41  ? -15.176 5.527   -3.117  0.19 30.74  ? 50  TRP   B NE1 1 
ATOM   665  N NE1 C TRP   B 2 41  ? -16.973 4.578   -2.675  0.35 35.00  ? 50  TRP   B NE1 1 
ATOM   666  N NE1 D TRP   B 2 41  ? -15.177 5.530   -3.119  0.33 30.32  ? 50  TRP   B NE1 1 
ATOM   667  C CE2 A TRP   B 2 41  ? -15.788 5.254   -2.824  0.13 34.90  ? 50  TRP   B CE2 1 
ATOM   668  C CE2 B TRP   B 2 41  ? -16.419 5.155   -2.680  0.19 32.06  ? 50  TRP   B CE2 1 
ATOM   669  C CE2 C TRP   B 2 41  ? -15.788 5.255   -2.827  0.35 34.93  ? 50  TRP   B CE2 1 
ATOM   670  C CE2 D TRP   B 2 41  ? -16.420 5.157   -2.681  0.33 32.27  ? 50  TRP   B CE2 1 
ATOM   671  C CE3 A TRP   B 2 41  ? -13.994 5.393   -4.440  0.13 35.15  ? 50  TRP   B CE3 1 
ATOM   672  C CE3 B TRP   B 2 41  ? -18.226 3.723   -3.404  0.19 31.69  ? 50  TRP   B CE3 1 
ATOM   673  C CE3 C TRP   B 2 41  ? -13.990 5.392   -4.439  0.35 35.45  ? 50  TRP   B CE3 1 
ATOM   674  C CE3 D TRP   B 2 41  ? -18.225 3.723   -3.403  0.33 31.64  ? 50  TRP   B CE3 1 
ATOM   675  C CZ2 A TRP   B 2 41  ? -15.163 6.182   -1.991  0.13 36.11  ? 50  TRP   B CZ2 1 
ATOM   676  C CZ2 B TRP   B 2 41  ? -17.123 5.535   -1.535  0.19 32.15  ? 50  TRP   B CZ2 1 
ATOM   677  C CZ2 C TRP   B 2 41  ? -15.164 6.186   -1.994  0.35 36.97  ? 50  TRP   B CZ2 1 
ATOM   678  C CZ2 D TRP   B 2 41  ? -17.125 5.537   -1.534  0.33 32.31  ? 50  TRP   B CZ2 1 
ATOM   679  C CZ3 A TRP   B 2 41  ? -13.376 6.308   -3.616  0.13 35.52  ? 50  TRP   B CZ3 1 
ATOM   680  C CZ3 B TRP   B 2 41  ? -18.921 4.101   -2.273  0.19 32.28  ? 50  TRP   B CZ3 1 
ATOM   681  C CZ3 C TRP   B 2 41  ? -13.373 6.307   -3.615  0.35 35.81  ? 50  TRP   B CZ3 1 
ATOM   682  C CZ3 D TRP   B 2 41  ? -18.921 4.102   -2.271  0.33 32.49  ? 50  TRP   B CZ3 1 
ATOM   683  C CH2 A TRP   B 2 41  ? -13.956 6.697   -2.406  0.13 36.28  ? 50  TRP   B CH2 1 
ATOM   684  C CH2 B TRP   B 2 41  ? -18.377 4.996   -1.351  0.19 32.09  ? 50  TRP   B CH2 1 
ATOM   685  C CH2 C TRP   B 2 41  ? -13.954 6.699   -2.406  0.35 37.21  ? 50  TRP   B CH2 1 
ATOM   686  C CH2 D TRP   B 2 41  ? -18.379 4.998   -1.349  0.33 32.18  ? 50  TRP   B CH2 1 
ATOM   687  N N   . HIS   B 2 42  ? -14.531 5.070   -8.150  1.00 32.10  ? 51  HIS   B N   1 
ATOM   688  C CA  . HIS   B 2 42  ? -13.535 6.160   -8.396  1.00 32.75  ? 51  HIS   B CA  1 
ATOM   689  C C   . HIS   B 2 42  ? -14.178 7.305   -9.219  1.00 32.26  ? 51  HIS   B C   1 
ATOM   690  O O   . HIS   B 2 42  ? -13.636 8.389   -9.190  1.00 31.28  ? 51  HIS   B O   1 
ATOM   691  C CB  . HIS   B 2 42  ? -12.195 5.643   -8.973  1.00 33.59  ? 51  HIS   B CB  1 
ATOM   692  C CG  . HIS   B 2 42  ? -12.204 5.362   -10.436 1.00 31.90  ? 51  HIS   B CG  1 
ATOM   693  N ND1 . HIS   B 2 42  ? -12.452 4.106   -10.947 1.00 30.67  ? 51  HIS   B ND1 1 
ATOM   694  C CD2 . HIS   B 2 42  ? -12.046 6.180   -11.504 1.00 36.83  ? 51  HIS   B CD2 1 
ATOM   695  C CE1 . HIS   B 2 42  ? -12.418 4.155   -12.267 1.00 31.96  ? 51  HIS   B CE1 1 
ATOM   696  N NE2 . HIS   B 2 42  ? -12.173 5.423   -12.636 1.00 33.35  ? 51  HIS   B NE2 1 
ATOM   697  N N   . VAL   B 2 43  ? -15.331 7.109   -9.858  1.00 31.57  ? 52  VAL   B N   1 
ATOM   698  C CA  . VAL   B 2 43  ? -16.013 8.176   -10.646 1.00 32.76  ? 52  VAL   B CA  1 
ATOM   699  C C   . VAL   B 2 43  ? -16.700 9.176   -9.699  1.00 34.50  ? 52  VAL   B C   1 
ATOM   700  O O   . VAL   B 2 43  ? -16.503 10.389  -9.884  1.00 36.91  ? 52  VAL   B O   1 
ATOM   701  C CB  . VAL   B 2 43  ? -17.025 7.540   -11.609 1.00 35.38  ? 52  VAL   B CB  1 
ATOM   702  C CG1 . VAL   B 2 43  ? -17.948 8.573   -12.249 1.00 35.54  ? 52  VAL   B CG1 1 
ATOM   703  C CG2 . VAL   B 2 43  ? -16.316 6.704   -12.667 1.00 36.04  ? 52  VAL   B CG2 1 
ATOM   704  N N   . THR   B 2 44  ? -17.515 8.681   -8.758  1.00 31.06  ? 53  THR   B N   1 
ATOM   705  C CA  . THR   B 2 44  ? -18.393 9.495   -7.866  1.00 31.26  ? 53  THR   B CA  1 
ATOM   706  C C   . THR   B 2 44  ? -17.783 9.680   -6.477  1.00 31.88  ? 53  THR   B C   1 
ATOM   707  O O   . THR   B 2 44  ? -18.173 10.668  -5.820  1.00 35.24  ? 53  THR   B O   1 
ATOM   708  C CB  . THR   B 2 44  ? -19.796 8.888   -7.756  1.00 27.47  ? 53  THR   B CB  1 
ATOM   709  O OG1 . THR   B 2 44  ? -19.749 7.612   -7.118  1.00 26.63  ? 53  THR   B OG1 1 
ATOM   710  C CG2 . THR   B 2 44  ? -20.459 8.741   -9.111  1.00 28.84  ? 53  THR   B CG2 1 
ATOM   711  N N   . LYS   B 2 45  ? -16.886 8.780   -6.050  1.00 34.62  ? 54  LYS   B N   1 
ATOM   712  C CA  . LYS   B 2 45  ? -16.404 8.627   -4.645  1.00 37.90  ? 54  LYS   B CA  1 
ATOM   713  C C   . LYS   B 2 45  ? -17.589 8.463   -3.675  1.00 36.15  ? 54  LYS   B C   1 
ATOM   714  O O   . LYS   B 2 45  ? -17.440 8.867   -2.521  1.00 40.48  ? 54  LYS   B O   1 
ATOM   715  C CB  . LYS   B 2 45  ? -15.574 9.835   -4.192  1.00 41.62  ? 54  LYS   B CB  1 
ATOM   716  C CG  . LYS   B 2 45  ? -14.481 10.295  -5.139  1.00 48.61  ? 54  LYS   B CG  1 
ATOM   717  C CD  . LYS   B 2 45  ? -13.284 9.392   -5.242  1.00 55.47  ? 54  LYS   B CD  1 
ATOM   718  C CE  . LYS   B 2 45  ? -12.113 10.115  -5.879  1.00 63.11  ? 54  LYS   B CE  1 
ATOM   719  N NZ  . LYS   B 2 45  ? -11.253 9.175   -6.635  1.00 71.21  ? 54  LYS   B NZ  1 
ATOM   720  N N   . GLY   B 2 46  ? -18.724 7.909   -4.101  1.00 37.39  ? 55  GLY   B N   1 
ATOM   721  C CA  . GLY   B 2 46  ? -19.883 7.675   -3.222  1.00 35.59  ? 55  GLY   B CA  1 
ATOM   722  C C   . GLY   B 2 46  ? -20.790 8.892   -3.058  1.00 38.25  ? 55  GLY   B C   1 
ATOM   723  O O   . GLY   B 2 46  ? -21.718 8.810   -2.267  1.00 39.48  ? 55  GLY   B O   1 
ATOM   724  N N   . ALA   B 2 47  ? -20.558 9.976   -3.790  1.00 36.96  ? 56  ALA   B N   1 
ATOM   725  C CA  . ALA   B 2 47  ? -21.347 11.232  -3.702  1.00 38.72  ? 56  ALA   B CA  1 
ATOM   726  C C   . ALA   B 2 47  ? -22.729 11.028  -4.344  1.00 38.22  ? 56  ALA   B C   1 
ATOM   727  O O   . ALA   B 2 47  ? -22.852 10.220  -5.254  1.00 36.09  ? 56  ALA   B O   1 
ATOM   728  C CB  . ALA   B 2 47  ? -20.580 12.357  -4.357  1.00 36.10  ? 56  ALA   B CB  1 
ATOM   729  N N   . ALA   B 2 48  ? -23.736 11.779  -3.902  1.00 39.75  ? 57  ALA   B N   1 
ATOM   730  C CA  . ALA   B 2 48  ? -25.090 11.818  -4.504  1.00 39.77  ? 57  ALA   B CA  1 
ATOM   731  C C   . ALA   B 2 48  ? -25.001 12.433  -5.896  1.00 36.67  ? 57  ALA   B C   1 
ATOM   732  O O   . ALA   B 2 48  ? -24.025 13.133  -6.189  1.00 40.89  ? 57  ALA   B O   1 
ATOM   733  C CB  . ALA   B 2 48  ? -26.066 12.596  -3.646  1.00 42.59  ? 57  ALA   B CB  1 
ATOM   734  N N   . LEU   B 2 49  ? -26.001 12.143  -6.713  1.00 36.49  ? 58  LEU   B N   1 
ATOM   735  C CA  . LEU   B 2 49  ? -26.077 12.547  -8.129  1.00 38.32  ? 58  LEU   B CA  1 
ATOM   736  C C   . LEU   B 2 49  ? -27.398 13.257  -8.362  1.00 37.35  ? 58  LEU   B C   1 
ATOM   737  O O   . LEU   B 2 49  ? -28.387 12.973  -7.662  1.00 39.06  ? 58  LEU   B O   1 
ATOM   738  C CB  . LEU   B 2 49  ? -25.998 11.308  -9.018  1.00 36.07  ? 58  LEU   B CB  1 
ATOM   739  C CG  . LEU   B 2 49  ? -24.710 10.503  -8.900  1.00 37.64  ? 58  LEU   B CG  1 
ATOM   740  C CD1 . LEU   B 2 49  ? -24.815 9.243   -9.734  1.00 35.64  ? 58  LEU   B CD1 1 
ATOM   741  C CD2 . LEU   B 2 49  ? -23.508 11.333  -9.313  1.00 40.29  ? 58  LEU   B CD2 1 
ATOM   742  N N   . ARG   B 2 50  ? -27.398 14.133  -9.339  1.00 39.13  ? 59  ARG   B N   1 
ATOM   743  C CA  . ARG   B 2 50  ? -28.619 14.806  -9.817  1.00 42.26  ? 59  ARG   B CA  1 
ATOM   744  C C   . ARG   B 2 50  ? -28.975 14.155  -11.154 1.00 43.21  ? 59  ARG   B C   1 
ATOM   745  O O   . ARG   B 2 50  ? -28.058 13.812  -11.918 1.00 43.28  ? 59  ARG   B O   1 
ATOM   746  C CB  . ARG   B 2 50  ? -28.337 16.303  -9.882  1.00 47.02  ? 59  ARG   B CB  1 
ATOM   747  C CG  . ARG   B 2 50  ? -29.479 17.135  -10.441 1.00 57.39  ? 59  ARG   B CG  1 
ATOM   748  C CD  . ARG   B 2 50  ? -29.238 18.593  -10.127 1.00 60.34  ? 59  ARG   B CD  1 
ATOM   749  N NE  . ARG   B 2 50  ? -27.814 18.907  -10.220 1.00 64.88  ? 59  ARG   B NE  1 
ATOM   750  C CZ  . ARG   B 2 50  ? -27.179 19.311  -11.321 1.00 63.76  ? 59  ARG   B CZ  1 
ATOM   751  N NH1 . ARG   B 2 50  ? -27.818 19.435  -12.475 1.00 60.56  ? 59  ARG   B NH1 1 
ATOM   752  N NH2 . ARG   B 2 50  ? -25.885 19.577  -11.262 1.00 70.12  ? 59  ARG   B NH2 1 
ATOM   753  N N   . SER   B 2 51  ? -30.254 13.881  -11.356 1.00 41.53  ? 60  SER   B N   1 
ATOM   754  C CA  . SER   B 2 51  ? -30.862 13.586  -12.674 1.00 46.41  ? 60  SER   B CA  1 
ATOM   755  C C   . SER   B 2 51  ? -31.971 14.620  -12.921 1.00 51.05  ? 60  SER   B C   1 
ATOM   756  O O   . SER   B 2 51  ? -33.110 14.374  -12.497 1.00 52.05  ? 60  SER   B O   1 
ATOM   757  C CB  . SER   B 2 51  ? -31.384 12.185  -12.702 1.00 42.41  ? 60  SER   B CB  1 
ATOM   758  O OG  . SER   B 2 51  ? -31.815 11.850  -14.000 1.00 43.34  ? 60  SER   B OG  1 
ATOM   759  N N   . GLY   B 2 52  ? -31.625 15.766  -13.515 1.00 53.36  ? 61  GLY   B N   1 
ATOM   760  C CA  . GLY   B 2 52  ? -32.544 16.909  -13.673 1.00 57.27  ? 61  GLY   B CA  1 
ATOM   761  C C   . GLY   B 2 52  ? -32.768 17.594  -12.341 1.00 57.56  ? 61  GLY   B C   1 
ATOM   762  O O   . GLY   B 2 52  ? -31.809 18.171  -11.807 1.00 68.58  ? 61  GLY   B O   1 
ATOM   763  N N   . GLU   B 2 53  ? -33.973 17.496  -11.790 1.00 59.82  ? 62  GLU   B N   1 
ATOM   764  C CA  . GLU   B 2 53  ? -34.261 18.017  -10.433 1.00 65.03  ? 62  GLU   B CA  1 
ATOM   765  C C   . GLU   B 2 53  ? -34.327 16.863  -9.431  1.00 58.21  ? 62  GLU   B C   1 
ATOM   766  O O   . GLU   B 2 53  ? -34.254 17.156  -8.240  1.00 56.31  ? 62  GLU   B O   1 
ATOM   767  C CB  . GLU   B 2 53  ? -35.509 18.896  -10.453 1.00 74.31  ? 62  GLU   B CB  1 
ATOM   768  C CG  . GLU   B 2 53  ? -35.178 20.346  -10.760 1.00 86.31  ? 62  GLU   B CG  1 
ATOM   769  C CD  . GLU   B 2 53  ? -36.278 21.334  -10.418 1.00 99.35  ? 62  GLU   B CD  1 
ATOM   770  O OE1 . GLU   B 2 53  ? -37.461 20.994  -10.640 1.00 114.58 ? 62  GLU   B OE1 1 
ATOM   771  O OE2 . GLU   B 2 53  ? -35.950 22.433  -9.916  1.00 101.65 ? 62  GLU   B OE2 1 
ATOM   772  N N   . GLY   B 2 54  ? -34.362 15.613  -9.902  1.00 55.77  ? 63  GLY   B N   1 
ATOM   773  C CA  . GLY   B 2 54  ? -34.330 14.401  -9.058  1.00 53.38  ? 63  GLY   B CA  1 
ATOM   774  C C   . GLY   B 2 54  ? -32.948 14.149  -8.476  1.00 53.22  ? 63  GLY   B C   1 
ATOM   775  O O   . GLY   B 2 54  ? -31.947 14.491  -9.140  1.00 53.21  ? 63  GLY   B O   1 
ATOM   776  N N   . ARG   B 2 55  ? -32.893 13.577  -7.270  1.00 47.78  ? 64  ARG   B N   1 
ATOM   777  C CA  . ARG   B 2 55  ? -31.638 13.244  -6.544  1.00 45.05  ? 64  ARG   B CA  1 
ATOM   778  C C   . ARG   B 2 55  ? -31.431 11.721  -6.515  1.00 47.64  ? 64  ARG   B C   1 
ATOM   779  O O   . ARG   B 2 55  ? -32.375 11.002  -6.172  1.00 50.55  ? 64  ARG   B O   1 
ATOM   780  C CB  . ARG   B 2 55  ? -31.729 13.789  -5.121  1.00 47.60  ? 64  ARG   B CB  1 
ATOM   781  C CG  . ARG   B 2 55  ? -30.400 13.861  -4.392  1.00 51.54  ? 64  ARG   B CG  1 
ATOM   782  C CD  . ARG   B 2 55  ? -30.622 14.250  -2.944  1.00 60.98  ? 64  ARG   B CD  1 
ATOM   783  N NE  . ARG   B 2 55  ? -29.512 13.804  -2.117  1.00 62.75  ? 64  ARG   B NE  1 
ATOM   784  C CZ  . ARG   B 2 55  ? -28.742 14.580  -1.356  1.00 64.69  ? 64  ARG   B CZ  1 
ATOM   785  N NH1 . ARG   B 2 55  ? -28.958 15.883  -1.281  1.00 63.13  ? 64  ARG   B NH1 1 
ATOM   786  N NH2 . ARG   B 2 55  ? -27.767 14.032  -0.647  1.00 62.15  ? 64  ARG   B NH2 1 
ATOM   787  N N   . LEU   B 2 56  ? -30.237 11.237  -6.856  1.00 39.69  ? 65  LEU   B N   1 
ATOM   788  C CA  . LEU   B 2 56  ? -29.899 9.795   -6.750  1.00 37.94  ? 65  LEU   B CA  1 
ATOM   789  C C   . LEU   B 2 56  ? -28.999 9.637   -5.527  1.00 32.97  ? 65  LEU   B C   1 
ATOM   790  O O   . LEU   B 2 56  ? -27.951 10.283  -5.506  1.00 30.90  ? 65  LEU   B O   1 
ATOM   791  C CB  . LEU   B 2 56  ? -29.154 9.287   -7.998  1.00 35.84  ? 65  LEU   B CB  1 
ATOM   792  C CG  . LEU   B 2 56  ? -29.734 9.540   -9.387  1.00 39.32  ? 65  LEU   B CG  1 
ATOM   793  C CD1 . LEU   B 2 56  ? -29.290 8.432   -10.333 1.00 38.80  ? 65  LEU   B CD1 1 
ATOM   794  C CD2 . LEU   B 2 56  ? -31.239 9.629   -9.388  1.00 42.11  ? 65  LEU   B CD2 1 
ATOM   795  N N   . ASP   B 2 57  ? -29.378 8.816   -4.548  1.00 33.27  ? 66  ASP   B N   1 
ATOM   796  C CA  . ASP   B 2 57  ? -28.523 8.558   -3.367  1.00 35.32  ? 66  ASP   B CA  1 
ATOM   797  C C   . ASP   B 2 57  ? -27.836 7.196   -3.477  1.00 32.38  ? 66  ASP   B C   1 
ATOM   798  O O   . ASP   B 2 57  ? -28.459 6.215   -3.901  1.00 29.18  ? 66  ASP   B O   1 
ATOM   799  C CB  . ASP   B 2 57  ? -29.370 8.704   -2.107  1.00 44.62  ? 66  ASP   B CB  1 
ATOM   800  C CG  . ASP   B 2 57  ? -29.693 10.162  -1.818  1.00 48.94  ? 66  ASP   B CG  1 
ATOM   801  O OD1 . ASP   B 2 57  ? -28.754 10.991  -1.839  1.00 56.77  ? 66  ASP   B OD1 1 
ATOM   802  O OD2 . ASP   B 2 57  ? -30.871 10.464  -1.634  1.00 50.88  ? 66  ASP   B OD2 1 
ATOM   803  N N   . PRO   B 2 58  ? -26.572 7.066   -3.013  1.00 31.70  ? 67  PRO   B N   1 
ATOM   804  C CA  . PRO   B 2 58  ? -25.870 5.781   -3.035  1.00 31.77  ? 67  PRO   B CA  1 
ATOM   805  C C   . PRO   B 2 58  ? -26.636 4.773   -2.165  1.00 34.68  ? 67  PRO   B C   1 
ATOM   806  O O   . PRO   B 2 58  ? -27.306 5.155   -1.198  1.00 33.35  ? 67  PRO   B O   1 
ATOM   807  C CB  . PRO   B 2 58  ? -24.469 6.113   -2.492  1.00 31.49  ? 67  PRO   B CB  1 
ATOM   808  C CG  . PRO   B 2 58  ? -24.689 7.317   -1.637  1.00 32.18  ? 67  PRO   B CG  1 
ATOM   809  C CD  . PRO   B 2 58  ? -25.773 8.106   -2.348  1.00 31.12  ? 67  PRO   B CD  1 
ATOM   810  N N   . TYR   B 2 59  ? -26.601 3.510   -2.564  1.00 30.48  ? 68  TYR   B N   1 
ATOM   811  C CA  . TYR   B 2 59  ? -27.305 2.406   -1.883  1.00 27.34  ? 68  TYR   B CA  1 
ATOM   812  C C   . TYR   B 2 59  ? -26.278 1.374   -1.413  1.00 28.55  ? 68  TYR   B C   1 
ATOM   813  O O   . TYR   B 2 59  ? -26.400 0.868   -0.311  1.00 27.38  ? 68  TYR   B O   1 
ATOM   814  C CB  . TYR   B 2 59  ? -28.339 1.813   -2.833  1.00 29.41  ? 68  TYR   B CB  1 
ATOM   815  C CG  . TYR   B 2 59  ? -29.207 0.738   -2.230  1.00 29.36  ? 68  TYR   B CG  1 
ATOM   816  C CD1 . TYR   B 2 59  ? -28.727 -0.550  -2.095  1.00 31.74  ? 68  TYR   B CD1 1 
ATOM   817  C CD2 . TYR   B 2 59  ? -30.487 1.001   -1.772  1.00 30.93  ? 68  TYR   B CD2 1 
ATOM   818  C CE1 . TYR   B 2 59  ? -29.519 -1.560  -1.574  1.00 33.68  ? 68  TYR   B CE1 1 
ATOM   819  C CE2 . TYR   B 2 59  ? -31.297 0.002   -1.247  1.00 31.89  ? 68  TYR   B CE2 1 
ATOM   820  C CZ  . TYR   B 2 59  ? -30.811 -1.289  -1.155  1.00 33.84  ? 68  TYR   B CZ  1 
ATOM   821  O OH  . TYR   B 2 59  ? -31.565 -2.297  -0.625  1.00 35.36  ? 68  TYR   B OH  1 
ATOM   822  N N   . TRP   B 2 60  ? -25.345 1.029   -2.285  1.00 26.74  ? 69  TRP   B N   1 
ATOM   823  C CA  . TRP   B 2 60  ? -24.312 -0.019  -2.067  1.00 27.60  ? 69  TRP   B CA  1 
ATOM   824  C C   . TRP   B 2 60  ? -23.001 0.469   -2.692  1.00 28.53  ? 69  TRP   B C   1 
ATOM   825  O O   . TRP   B 2 60  ? -23.036 1.057   -3.791  1.00 28.51  ? 69  TRP   B O   1 
ATOM   826  C CB  . TRP   B 2 60  ? -24.725 -1.401  -2.601  1.00 26.18  ? 69  TRP   B CB  1 
ATOM   827  C CG  . TRP   B 2 60  ? -23.595 -2.379  -2.533  1.00 28.07  ? 69  TRP   B CG  1 
ATOM   828  C CD1 . TRP   B 2 60  ? -23.153 -3.085  -1.441  1.00 28.47  ? 69  TRP   B CD1 1 
ATOM   829  C CD2 . TRP   B 2 60  ? -22.660 -2.657  -3.593  1.00 27.75  ? 69  TRP   B CD2 1 
ATOM   830  N NE1 . TRP   B 2 60  ? -22.029 -3.809  -1.766  1.00 27.92  ? 69  TRP   B NE1 1 
ATOM   831  C CE2 . TRP   B 2 60  ? -21.702 -3.564  -3.075  1.00 26.89  ? 69  TRP   B CE2 1 
ATOM   832  C CE3 . TRP   B 2 60  ? -22.552 -2.240  -4.926  1.00 28.06  ? 69  TRP   B CE3 1 
ATOM   833  C CZ2 . TRP   B 2 60  ? -20.649 -4.041  -3.850  1.00 27.50  ? 69  TRP   B CZ2 1 
ATOM   834  C CZ3 . TRP   B 2 60  ? -21.524 -2.746  -5.697  1.00 27.90  ? 69  TRP   B CZ3 1 
ATOM   835  C CH2 . TRP   B 2 60  ? -20.590 -3.632  -5.165  1.00 27.72  ? 69  TRP   B CH2 1 
ATOM   836  N N   . GLY   B 2 61  ? -21.890 0.190   -2.035  1.00 29.66  ? 70  GLY   B N   1 
ATOM   837  C CA  . GLY   B 2 61  ? -20.574 0.585   -2.549  1.00 31.09  ? 70  GLY   B CA  1 
ATOM   838  C C   . GLY   B 2 61  ? -19.473 -0.230  -1.932  1.00 30.12  ? 70  GLY   B C   1 
ATOM   839  O O   . GLY   B 2 61  ? -19.654 -0.663  -0.787  1.00 30.18  ? 70  GLY   B O   1 
ATOM   840  N N   . ASP   B 2 62  ? -18.367 -0.380  -2.654  1.00 27.94  ? 71  ASP   B N   1 
ATOM   841  C CA  . ASP   B 2 62  ? -17.190 -1.167  -2.207  1.00 27.85  ? 71  ASP   B CA  1 
ATOM   842  C C   . ASP   B 2 62  ? -15.956 -0.670  -2.959  1.00 27.32  ? 71  ASP   B C   1 
ATOM   843  O O   . ASP   B 2 62  ? -15.874 -0.904  -4.170  1.00 28.78  ? 71  ASP   B O   1 
ATOM   844  C CB  . ASP   B 2 62  ? -17.444 -2.653  -2.411  1.00 29.40  ? 71  ASP   B CB  1 
ATOM   845  C CG  . ASP   B 2 62  ? -16.431 -3.573  -1.745  1.00 37.24  ? 71  ASP   B CG  1 
ATOM   846  O OD1 . ASP   B 2 62  ? -15.214 -3.282  -1.753  1.00 38.07  ? 71  ASP   B OD1 1 
ATOM   847  O OD2 . ASP   B 2 62  ? -16.881 -4.550  -1.190  1.00 43.49  ? 71  ASP   B OD2 1 
ATOM   848  N N   . VAL   B 2 63  ? -15.044 -0.007  -2.255  1.00 27.32  ? 72  VAL   B N   1 
ATOM   849  C CA  . VAL   B 2 63  ? -13.819 0.607   -2.829  1.00 28.07  ? 72  VAL   B CA  1 
ATOM   850  C C   . VAL   B 2 63  ? -12.925 -0.506  -3.395  1.00 31.20  ? 72  VAL   B C   1 
ATOM   851  O O   . VAL   B 2 63  ? -12.212 -0.233  -4.378  1.00 31.23  ? 72  VAL   B O   1 
ATOM   852  C CB  . VAL   B 2 63  ? -13.066 1.459   -1.788  1.00 28.81  ? 72  VAL   B CB  1 
ATOM   853  C CG1 . VAL   B 2 63  ? -11.600 1.605   -2.105  1.00 31.51  ? 72  VAL   B CG1 1 
ATOM   854  C CG2 . VAL   B 2 63  ? -13.708 2.817   -1.602  1.00 28.10  ? 72  VAL   B CG2 1 
ATOM   855  N N   . LYS   B 2 64  ? -13.005 -1.737  -2.882  1.00 33.59  ? 73  LYS   B N   1 
ATOM   856  C CA  . LYS   B 2 64  ? -12.075 -2.790  -3.374  1.00 35.38  ? 73  LYS   B CA  1 
ATOM   857  C C   . LYS   B 2 64  ? -12.553 -3.325  -4.731  1.00 33.13  ? 73  LYS   B C   1 
ATOM   858  O O   . LYS   B 2 64  ? -11.703 -3.482  -5.617  1.00 34.33  ? 73  LYS   B O   1 
ATOM   859  C CB  . LYS   B 2 64  ? -11.889 -3.939  -2.394  1.00 33.57  ? 73  LYS   B CB  1 
ATOM   860  C CG  . LYS   B 2 64  ? -10.729 -4.818  -2.836  1.00 38.12  ? 73  LYS   B CG  1 
ATOM   861  C CD  . LYS   B 2 64  ? -10.348 -5.877  -1.865  1.00 37.50  ? 73  LYS   B CD  1 
ATOM   862  C CE  . LYS   B 2 64  ? -9.232  -6.737  -2.414  1.00 41.93  ? 73  LYS   B CE  1 
ATOM   863  N NZ  . LYS   B 2 64  ? -8.870  -7.808  -1.458  1.00 40.84  ? 73  LYS   B NZ  1 
ATOM   864  N N   . GLN   B 2 65  ? -13.858 -3.548  -4.894  1.00 33.93  ? 74  GLN   B N   1 
ATOM   865  C CA  . GLN   B 2 65  ? -14.491 -3.893  -6.191  1.00 31.87  ? 74  GLN   B CA  1 
ATOM   866  C C   . GLN   B 2 65  ? -14.476 -2.704  -7.156  1.00 30.36  ? 74  GLN   B C   1 
ATOM   867  O O   . GLN   B 2 65  ? -14.602 -2.969  -8.379  1.00 30.81  ? 74  GLN   B O   1 
ATOM   868  C CB  . GLN   B 2 65  ? -15.921 -4.355  -5.987  1.00 32.90  ? 74  GLN   B CB  1 
ATOM   869  C CG  . GLN   B 2 65  ? -15.979 -5.687  -5.279  1.00 36.15  ? 74  GLN   B CG  1 
ATOM   870  C CD  . GLN   B 2 65  ? -17.397 -6.174  -5.162  1.00 39.24  ? 74  GLN   B CD  1 
ATOM   871  O OE1 . GLN   B 2 65  ? -18.100 -6.407  -6.159  1.00 41.55  ? 74  GLN   B OE1 1 
ATOM   872  N NE2 . GLN   B 2 65  ? -17.835 -6.285  -3.924  1.00 41.01  ? 74  GLN   B NE2 1 
ATOM   873  N N   . ASP   B 2 66  ? -14.333 -1.490  -6.608  1.00 29.50  ? 75  ASP   B N   1 
ATOM   874  C CA  . ASP   B 2 66  ? -14.430 -0.149  -7.255  1.00 31.76  ? 75  ASP   B CA  1 
ATOM   875  C C   . ASP   B 2 66  ? -15.773 -0.025  -7.944  1.00 33.07  ? 75  ASP   B C   1 
ATOM   876  O O   . ASP   B 2 66  ? -15.757 0.523   -9.062  1.00 31.62  ? 75  ASP   B O   1 
ATOM   877  C CB  . ASP   B 2 66  ? -13.329 0.105   -8.285  1.00 33.16  ? 75  ASP   B CB  1 
ATOM   878  C CG  . ASP   B 2 66  ? -13.185 1.543   -8.782  1.00 35.84  ? 75  ASP   B CG  1 
ATOM   879  O OD1 . ASP   B 2 66  ? -13.474 2.480   -8.017  1.00 33.27  ? 75  ASP   B OD1 1 
ATOM   880  O OD2 . ASP   B 2 66  ? -12.687 1.709   -9.918  1.00 36.54  ? 75  ASP   B OD2 1 
ATOM   881  N N   . LEU   B 2 67  ? -16.859 -0.443  -7.269  1.00 26.85  ? 76  LEU   B N   1 
ATOM   882  C CA  . LEU   B 2 67  ? -18.265 -0.384  -7.759  1.00 27.80  ? 76  LEU   B CA  1 
ATOM   883  C C   . LEU   B 2 67  ? -19.150 0.412   -6.784  1.00 31.34  ? 76  LEU   B C   1 
ATOM   884  O O   . LEU   B 2 67  ? -18.839 0.428   -5.567  1.00 31.11  ? 76  LEU   B O   1 
ATOM   885  C CB  . LEU   B 2 67  ? -18.786 -1.809  -7.926  1.00 26.36  ? 76  LEU   B CB  1 
ATOM   886  C CG  . LEU   B 2 67  ? -18.163 -2.607  -9.079  1.00 26.34  ? 76  LEU   B CG  1 
ATOM   887  C CD1 . LEU   B 2 67  ? -18.852 -3.962  -9.223  1.00 25.07  ? 76  LEU   B CD1 1 
ATOM   888  C CD2 . LEU   B 2 67  ? -18.256 -1.837  -10.411 1.00 28.01  ? 76  LEU   B CD2 1 
ATOM   889  N N   . VAL   B 2 68  ? -20.233 0.997   -7.302  1.00 27.52  ? 77  VAL   B N   1 
ATOM   890  C CA  . VAL   B 2 68  ? -21.283 1.700   -6.494  1.00 30.10  ? 77  VAL   B CA  1 
ATOM   891  C C   . VAL   B 2 68  ? -22.603 1.672   -7.261  1.00 30.42  ? 77  VAL   B C   1 
ATOM   892  O O   . VAL   B 2 68  ? -22.594 1.744   -8.502  1.00 31.04  ? 77  VAL   B O   1 
ATOM   893  C CB  . VAL   B 2 68  ? -20.861 3.135   -6.110  1.00 30.10  ? 77  VAL   B CB  1 
ATOM   894  C CG1 . VAL   B 2 68  ? -20.528 3.986   -7.322  1.00 29.52  ? 77  VAL   B CG1 1 
ATOM   895  C CG2 . VAL   B 2 68  ? -21.902 3.830   -5.237  1.00 28.96  ? 77  VAL   B CG2 1 
ATOM   896  N N   . SER   B 2 69  ? -23.696 1.525   -6.531  1.00 26.85  ? 78  SER   B N   1 
ATOM   897  C CA  . SER   B 2 69  ? -25.081 1.531   -7.046  1.00 27.85  ? 78  SER   B CA  1 
ATOM   898  C C   . SER   B 2 69  ? -25.876 2.644   -6.332  1.00 28.72  ? 78  SER   B C   1 
ATOM   899  O O   . SER   B 2 69  ? -25.559 2.990   -5.165  1.00 24.73  ? 78  SER   B O   1 
ATOM   900  C CB  . SER   B 2 69  ? -25.710 0.141   -6.945  1.00 30.78  ? 78  SER   B CB  1 
ATOM   901  O OG  . SER   B 2 69  ? -26.116 -0.193  -5.616  1.00 30.54  ? 78  SER   B OG  1 
ATOM   902  N N   . TYR   B 2 70  ? -26.806 3.241   -7.069  1.00 28.38  ? 79  TYR   B N   1 
ATOM   903  C CA  . TYR   B 2 70  ? -27.743 4.312   -6.652  1.00 27.80  ? 79  TYR   B CA  1 
ATOM   904  C C   . TYR   B 2 70  ? -29.170 3.774   -6.787  1.00 29.93  ? 79  TYR   B C   1 
ATOM   905  O O   . TYR   B 2 70  ? -29.528 3.160   -7.836  1.00 26.07  ? 79  TYR   B O   1 
ATOM   906  C CB  . TYR   B 2 70  ? -27.511 5.572   -7.491  1.00 28.31  ? 79  TYR   B CB  1 
ATOM   907  C CG  . TYR   B 2 70  ? -26.173 6.221   -7.225  1.00 27.95  ? 79  TYR   B CG  1 
ATOM   908  C CD1 . TYR   B 2 70  ? -25.004 5.706   -7.767  1.00 28.48  ? 79  TYR   B CD1 1 
ATOM   909  C CD2 . TYR   B 2 70  ? -26.056 7.315   -6.383  1.00 30.34  ? 79  TYR   B CD2 1 
ATOM   910  C CE1 . TYR   B 2 70  ? -23.761 6.250   -7.483  1.00 27.82  ? 79  TYR   B CE1 1 
ATOM   911  C CE2 . TYR   B 2 70  ? -24.824 7.896   -6.105  1.00 30.06  ? 79  TYR   B CE2 1 
ATOM   912  C CZ  . TYR   B 2 70  ? -23.672 7.363   -6.662  1.00 26.95  ? 79  TYR   B CZ  1 
ATOM   913  O OH  . TYR   B 2 70  ? -22.455 7.907   -6.376  1.00 30.46  ? 79  TYR   B OH  1 
ATOM   914  N N   . CYS   B 2 71  ? -29.968 4.010   -5.740  1.00 29.34  ? 80  CYS   B N   1 
ATOM   915  C CA  . CYS   B 2 71  ? -31.447 3.875   -5.702  1.00 31.06  ? 80  CYS   B CA  1 
ATOM   916  C C   . CYS   B 2 71  ? -31.823 2.426   -5.396  1.00 33.05  ? 80  CYS   B C   1 
ATOM   917  O O   . CYS   B 2 71  ? -32.984 2.146   -5.102  1.00 37.12  ? 80  CYS   B O   1 
ATOM   918  C CB  . CYS   B 2 71  ? -32.092 4.374   -6.988  1.00 33.57  ? 80  CYS   B CB  1 
ATOM   919  S SG  . CYS   B 2 71  ? -31.650 6.095   -7.376  1.00 41.33  ? 80  CYS   B SG  1 
ATOM   920  N N   . GLY   B 2 72  ? -30.853 1.531   -5.359  1.00 32.00  ? 81  GLY   B N   1 
ATOM   921  C CA  . GLY   B 2 72  ? -31.169 0.118   -5.137  1.00 31.39  ? 81  GLY   B CA  1 
ATOM   922  C C   . GLY   B 2 72  ? -29.910 -0.716  -5.266  1.00 28.27  ? 81  GLY   B C   1 
ATOM   923  O O   . GLY   B 2 72  ? -28.832 -0.190  -5.550  1.00 31.32  ? 81  GLY   B O   1 
ATOM   924  N N   . PRO   B 2 73  ? -30.015 -2.024  -4.974  1.00 27.57  ? 82  PRO   B N   1 
ATOM   925  C CA  . PRO   B 2 73  ? -28.853 -2.905  -4.991  1.00 32.23  ? 82  PRO   B CA  1 
ATOM   926  C C   . PRO   B 2 73  ? -28.352 -3.149  -6.425  1.00 30.36  ? 82  PRO   B C   1 
ATOM   927  O O   . PRO   B 2 73  ? -29.140 -2.986  -7.336  1.00 34.58  ? 82  PRO   B O   1 
ATOM   928  C CB  . PRO   B 2 73  ? -29.419 -4.184  -4.336  1.00 29.20  ? 82  PRO   B CB  1 
ATOM   929  C CG  . PRO   B 2 73  ? -30.874 -4.163  -4.698  1.00 30.18  ? 82  PRO   B CG  1 
ATOM   930  C CD  . PRO   B 2 73  ? -31.259 -2.709  -4.601  1.00 29.29  ? 82  PRO   B CD  1 
ATOM   931  N N   . TRP   B 2 74  ? -27.085 -3.524  -6.574  1.00 30.18  ? 83  TRP   B N   1 
ATOM   932  C CA  . TRP   B 2 74  ? -26.457 -3.896  -7.870  1.00 30.77  ? 83  TRP   B CA  1 
ATOM   933  C C   . TRP   B 2 74  ? -27.349 -4.895  -8.632  1.00 32.73  ? 83  TRP   B C   1 
ATOM   934  O O   . TRP   B 2 74  ? -27.603 -5.968  -8.074  1.00 32.77  ? 83  TRP   B O   1 
ATOM   935  C CB  . TRP   B 2 74  ? -25.058 -4.477  -7.620  1.00 29.91  ? 83  TRP   B CB  1 
ATOM   936  C CG  . TRP   B 2 74  ? -24.258 -4.643  -8.873  1.00 26.76  ? 83  TRP   B CG  1 
ATOM   937  C CD1 . TRP   B 2 74  ? -24.197 -5.738  -9.688  1.00 27.50  ? 83  TRP   B CD1 1 
ATOM   938  C CD2 . TRP   B 2 74  ? -23.446 -3.631  -9.488  1.00 28.77  ? 83  TRP   B CD2 1 
ATOM   939  N NE1 . TRP   B 2 74  ? -23.368 -5.485  -10.751 1.00 26.51  ? 83  TRP   B NE1 1 
ATOM   940  C CE2 . TRP   B 2 74  ? -22.889 -4.203  -10.654 1.00 27.97  ? 83  TRP   B CE2 1 
ATOM   941  C CE3 . TRP   B 2 74  ? -23.105 -2.313  -9.142  1.00 28.57  ? 83  TRP   B CE3 1 
ATOM   942  C CZ2 . TRP   B 2 74  ? -22.051 -3.482  -11.506 1.00 26.16  ? 83  TRP   B CZ2 1 
ATOM   943  C CZ3 . TRP   B 2 74  ? -22.271 -1.607  -9.977  1.00 26.02  ? 83  TRP   B CZ3 1 
ATOM   944  C CH2 . TRP   B 2 74  ? -21.754 -2.190  -11.144 1.00 27.88  ? 83  TRP   B CH2 1 
ATOM   945  N N   . LYS   B 2 75  ? -27.729 -4.603  -9.891  1.00 29.84  ? 84  LYS   B N   1 
ATOM   946  C CA  . LYS   B 2 75  ? -28.685 -5.436  -10.680 1.00 32.88  ? 84  LYS   B CA  1 
ATOM   947  C C   . LYS   B 2 75  ? -27.997 -6.319  -11.741 1.00 33.50  ? 84  LYS   B C   1 
ATOM   948  O O   . LYS   B 2 75  ? -28.661 -7.241  -12.227 1.00 38.18  ? 84  LYS   B O   1 
ATOM   949  C CB  . LYS   B 2 75  ? -29.679 -4.521  -11.391 1.00 36.01  ? 84  LYS   B CB  1 
ATOM   950  C CG  . LYS   B 2 75  ? -30.589 -3.721  -10.473 1.00 37.01  ? 84  LYS   B CG  1 
ATOM   951  C CD  . LYS   B 2 75  ? -31.575 -4.569  -9.751  1.00 41.04  ? 84  LYS   B CD  1 
ATOM   952  C CE  . LYS   B 2 75  ? -32.291 -3.799  -8.668  1.00 45.10  ? 84  LYS   B CE  1 
ATOM   953  N NZ  . LYS   B 2 75  ? -33.733 -4.116  -8.668  1.00 49.07  ? 84  LYS   B NZ  1 
ATOM   954  N N   . LEU   B 2 76  ? -26.744 -6.051  -12.106 1.00 35.61  ? 85  LEU   B N   1 
ATOM   955  C CA  . LEU   B 2 76  ? -26.071 -6.595  -13.318 1.00 36.97  ? 85  LEU   B CA  1 
ATOM   956  C C   . LEU   B 2 76  ? -25.300 -7.867  -12.963 1.00 38.35  ? 85  LEU   B C   1 
ATOM   957  O O   . LEU   B 2 76  ? -24.336 -7.777  -12.184 1.00 34.77  ? 85  LEU   B O   1 
ATOM   958  C CB  . LEU   B 2 76  ? -25.127 -5.525  -13.869 1.00 37.32  ? 85  LEU   B CB  1 
ATOM   959  C CG  . LEU   B 2 76  ? -25.763 -4.143  -14.076 1.00 36.03  ? 85  LEU   B CG  1 
ATOM   960  C CD1 . LEU   B 2 76  ? -24.768 -3.176  -14.668 1.00 34.59  ? 85  LEU   B CD1 1 
ATOM   961  C CD2 . LEU   B 2 76  ? -26.986 -4.239  -14.972 1.00 38.77  ? 85  LEU   B CD2 1 
ATOM   962  N N   . ASP   B 2 77  ? -25.691 -9.010  -13.535 1.00 39.61  ? 86  ASP   B N   1 
ATOM   963  C CA  . ASP   B 2 77  ? -25.117 -10.316 -13.117 1.00 48.24  ? 86  ASP   B CA  1 
ATOM   964  C C   . ASP   B 2 77  ? -24.630 -11.132 -14.321 1.00 45.37  ? 86  ASP   B C   1 
ATOM   965  O O   . ASP   B 2 77  ? -24.047 -12.182 -14.087 1.00 43.79  ? 86  ASP   B O   1 
ATOM   966  C CB  . ASP   B 2 77  ? -26.098 -11.092 -12.236 1.00 51.86  ? 86  ASP   B CB  1 
ATOM   967  C CG  . ASP   B 2 77  ? -27.479 -11.181 -12.840 1.00 59.25  ? 86  ASP   B CG  1 
ATOM   968  O OD1 . ASP   B 2 77  ? -27.717 -10.471 -13.849 1.00 64.66  ? 86  ASP   B OD1 1 
ATOM   969  O OD2 . ASP   B 2 77  ? -28.301 -11.952 -12.304 1.00 60.91  ? 86  ASP   B OD2 1 
ATOM   970  N N   . ALA   B 2 78  ? -24.757 -10.650 -15.552 1.00 42.77  ? 87  ALA   B N   1 
ATOM   971  C CA  . ALA   B 2 78  ? -24.186 -11.336 -16.728 1.00 39.31  ? 87  ALA   B CA  1 
ATOM   972  C C   . ALA   B 2 78  ? -22.665 -11.446 -16.549 1.00 40.59  ? 87  ALA   B C   1 
ATOM   973  O O   . ALA   B 2 78  ? -22.044 -10.530 -15.932 1.00 39.00  ? 87  ALA   B O   1 
ATOM   974  C CB  . ALA   B 2 78  ? -24.577 -10.624 -18.006 1.00 38.80  ? 87  ALA   B CB  1 
ATOM   975  N N   . ALA   B 2 79  ? -22.087 -12.536 -17.077 1.00 37.82  ? 88  ALA   B N   1 
ATOM   976  C CA  . ALA   B 2 79  ? -20.647 -12.877 -16.996 1.00 42.56  ? 88  ALA   B CA  1 
ATOM   977  C C   . ALA   B 2 79  ? -20.083 -13.078 -18.407 1.00 35.02  ? 88  ALA   B C   1 
ATOM   978  O O   . ALA   B 2 79  ? -20.797 -13.673 -19.229 1.00 37.29  ? 88  ALA   B O   1 
ATOM   979  C CB  . ALA   B 2 79  ? -20.492 -14.129 -16.152 1.00 42.51  ? 88  ALA   B CB  1 
ATOM   980  N N   . TRP   B 2 80  ? -18.876 -12.576 -18.682 1.00 34.31  ? 89  TRP   B N   1 
ATOM   981  C CA  . TRP   B 2 80  ? -18.042 -12.977 -19.853 1.00 41.27  ? 89  TRP   B CA  1 
ATOM   982  C C   . TRP   B 2 80  ? -17.950 -14.495 -19.867 1.00 44.16  ? 89  TRP   B C   1 
ATOM   983  O O   . TRP   B 2 80  ? -17.732 -15.056 -18.772 1.00 39.42  ? 89  TRP   B O   1 
ATOM   984  C CB  . TRP   B 2 80  ? -16.637 -12.366 -19.837 1.00 45.73  ? 89  TRP   B CB  1 
ATOM   985  C CG  . TRP   B 2 80  ? -15.848 -12.727 -21.062 1.00 47.32  ? 89  TRP   B CG  1 
ATOM   986  C CD1 . TRP   B 2 80  ? -16.321 -12.778 -22.342 1.00 49.30  ? 89  TRP   B CD1 1 
ATOM   987  C CD2 . TRP   B 2 80  ? -14.457 -13.082 -21.138 1.00 49.06  ? 89  TRP   B CD2 1 
ATOM   988  N NE1 . TRP   B 2 80  ? -15.328 -13.140 -23.205 1.00 48.04  ? 89  TRP   B NE1 1 
ATOM   989  C CE2 . TRP   B 2 80  ? -14.173 -13.340 -22.496 1.00 49.47  ? 89  TRP   B CE2 1 
ATOM   990  C CE3 . TRP   B 2 80  ? -13.431 -13.238 -20.201 1.00 49.09  ? 89  TRP   B CE3 1 
ATOM   991  C CZ2 . TRP   B 2 80  ? -12.906 -13.720 -22.934 1.00 44.67  ? 89  TRP   B CZ2 1 
ATOM   992  C CZ3 . TRP   B 2 80  ? -12.176 -13.607 -20.643 1.00 49.40  ? 89  TRP   B CZ3 1 
ATOM   993  C CH2 . TRP   B 2 80  ? -11.919 -13.846 -21.991 1.00 43.21  ? 89  TRP   B CH2 1 
ATOM   994  N N   . ASP   B 2 81  ? -18.170 -15.122 -21.029 1.00 46.41  ? 90  ASP   B N   1 
ATOM   995  C CA  . ASP   B 2 81  ? -18.261 -16.603 -21.145 1.00 44.63  ? 90  ASP   B CA  1 
ATOM   996  C C   . ASP   B 2 81  ? -16.843 -17.184 -21.207 1.00 45.60  ? 90  ASP   B C   1 
ATOM   997  O O   . ASP   B 2 81  ? -16.723 -18.399 -21.114 1.00 52.43  ? 90  ASP   B O   1 
ATOM   998  C CB  . ASP   B 2 81  ? -19.123 -17.029 -22.331 1.00 41.75  ? 90  ASP   B CB  1 
ATOM   999  C CG  . ASP   B 2 81  ? -18.490 -16.772 -23.674 1.00 40.15  ? 90  ASP   B CG  1 
ATOM   1000 O OD1 . ASP   B 2 81  ? -17.427 -16.090 -23.738 1.00 42.40  ? 90  ASP   B OD1 1 
ATOM   1001 O OD2 . ASP   B 2 81  ? -19.082 -17.214 -24.660 1.00 51.71  ? 90  ASP   B OD2 1 
ATOM   1002 N N   . GLY   B 2 82  ? -15.827 -16.336 -21.357 1.00 43.85  ? 91  GLY   B N   1 
ATOM   1003 C CA  . GLY   B 2 82  ? -14.403 -16.719 -21.377 1.00 44.73  ? 91  GLY   B CA  1 
ATOM   1004 C C   . GLY   B 2 82  ? -13.937 -17.108 -22.773 1.00 46.92  ? 91  GLY   B C   1 
ATOM   1005 O O   . GLY   B 2 82  ? -12.778 -17.548 -22.880 1.00 42.01  ? 91  GLY   B O   1 
ATOM   1006 N N   . LEU   B 2 83  ? -14.794 -16.948 -23.795 1.00 49.46  ? 92  LEU   B N   1 
ATOM   1007 C CA  . LEU   B 2 83  ? -14.587 -17.427 -25.198 1.00 51.39  ? 92  LEU   B CA  1 
ATOM   1008 C C   . LEU   B 2 83  ? -14.892 -16.335 -26.243 1.00 52.75  ? 92  LEU   B C   1 
ATOM   1009 O O   . LEU   B 2 83  ? -14.041 -16.112 -27.135 1.00 48.23  ? 92  LEU   B O   1 
ATOM   1010 C CB  . LEU   B 2 83  ? -15.503 -18.631 -25.435 1.00 52.72  ? 92  LEU   B CB  1 
ATOM   1011 C CG  . LEU   B 2 83  ? -14.969 -19.981 -24.963 1.00 56.31  ? 92  LEU   B CG  1 
ATOM   1012 C CD1 . LEU   B 2 83  ? -15.986 -21.080 -25.239 1.00 53.14  ? 92  LEU   B CD1 1 
ATOM   1013 C CD2 . LEU   B 2 83  ? -13.628 -20.308 -25.615 1.00 54.11  ? 92  LEU   B CD2 1 
ATOM   1014 N N   . SER   B 2 84  ? -16.073 -15.703 -26.172 1.00 55.81  ? 93  SER   B N   1 
ATOM   1015 C CA  . SER   B 2 84  ? -16.668 -14.878 -27.258 1.00 47.68  ? 93  SER   B CA  1 
ATOM   1016 C C   . SER   B 2 84  ? -16.067 -13.471 -27.257 1.00 50.40  ? 93  SER   B C   1 
ATOM   1017 O O   . SER   B 2 84  ? -15.497 -13.067 -26.218 1.00 52.67  ? 93  SER   B O   1 
ATOM   1018 C CB  . SER   B 2 84  ? -18.150 -14.854 -27.122 1.00 44.26  ? 93  SER   B CB  1 
ATOM   1019 O OG  . SER   B 2 84  ? -18.584 -15.926 -26.289 1.00 46.06  ? 93  SER   B OG  1 
ATOM   1020 N N   . GLU   B 2 85  ? -16.162 -12.749 -28.380 1.00 50.60  ? 94  GLU   B N   1 
ATOM   1021 C CA  . GLU   B 2 85  ? -15.791 -11.306 -28.423 1.00 51.48  ? 94  GLU   B CA  1 
ATOM   1022 C C   . GLU   B 2 85  ? -16.859 -10.538 -27.620 1.00 42.70  ? 94  GLU   B C   1 
ATOM   1023 O O   . GLU   B 2 85  ? -17.955 -11.092 -27.378 1.00 29.37  ? 94  GLU   B O   1 
ATOM   1024 C CB  . GLU   B 2 85  ? -15.573 -10.808 -29.864 1.00 56.19  ? 94  GLU   B CB  1 
ATOM   1025 C CG  . GLU   B 2 85  ? -14.192 -11.181 -30.421 1.00 59.91  ? 94  GLU   B CG  1 
ATOM   1026 C CD  . GLU   B 2 85  ? -13.730 -10.653 -31.780 1.00 63.48  ? 94  GLU   B CD  1 
ATOM   1027 O OE1 . GLU   B 2 85  ? -14.368 -9.726  -32.337 1.00 53.05  ? 94  GLU   B OE1 1 
ATOM   1028 O OE2 . GLU   B 2 85  ? -12.689 -11.162 -32.281 1.00 64.15  ? 94  GLU   B OE2 1 
ATOM   1029 N N   . VAL   B 2 86  ? -16.499 -9.347  -27.148 1.00 41.41  ? 95  VAL   B N   1 
ATOM   1030 C CA  . VAL   B 2 86  ? -17.403 -8.413  -26.411 1.00 40.64  ? 95  VAL   B CA  1 
ATOM   1031 C C   . VAL   B 2 86  ? -17.366 -7.056  -27.120 1.00 39.14  ? 95  VAL   B C   1 
ATOM   1032 O O   . VAL   B 2 86  ? -16.429 -6.845  -27.929 1.00 41.65  ? 95  VAL   B O   1 
ATOM   1033 C CB  . VAL   B 2 86  ? -16.963 -8.273  -24.939 1.00 32.56  ? 95  VAL   B CB  1 
ATOM   1034 C CG1 . VAL   B 2 86  ? -16.844 -9.625  -24.289 1.00 33.65  ? 95  VAL   B CG1 1 
ATOM   1035 C CG2 . VAL   B 2 86  ? -15.651 -7.508  -24.813 1.00 35.34  ? 95  VAL   B CG2 1 
ATOM   1036 N N   . GLN   B 2 87  ? -18.271 -6.142  -26.747 1.00 38.12  ? 96  GLN   B N   1 
ATOM   1037 C CA  . GLN   B 2 87  ? -18.193 -4.708  -27.145 1.00 38.10  ? 96  GLN   B CA  1 
ATOM   1038 C C   . GLN   B 2 87  ? -18.119 -3.808  -25.910 1.00 31.63  ? 96  GLN   B C   1 
ATOM   1039 O O   . GLN   B 2 87  ? -18.942 -4.000  -25.025 1.00 34.42  ? 96  GLN   B O   1 
ATOM   1040 C CB  . GLN   B 2 87  ? -19.407 -4.352  -28.007 1.00 41.34  ? 96  GLN   B CB  1 
ATOM   1041 C CG  . GLN   B 2 87  ? -19.460 -5.184  -29.278 1.00 42.97  ? 96  GLN   B CG  1 
ATOM   1042 C CD  . GLN   B 2 87  ? -20.404 -4.680  -30.347 1.00 45.05  ? 96  GLN   B CD  1 
ATOM   1043 O OE1 . GLN   B 2 87  ? -21.153 -3.712  -30.172 1.00 42.13  ? 96  GLN   B OE1 1 
ATOM   1044 N NE2 . GLN   B 2 87  ? -20.364 -5.355  -31.485 1.00 42.11  ? 96  GLN   B NE2 1 
ATOM   1045 N N   . LEU   B 2 88  ? -17.110 -2.938  -25.863 1.00 29.23  ? 97  LEU   B N   1 
ATOM   1046 C CA  . LEU   B 2 88  ? -17.050 -1.710  -25.028 1.00 32.14  ? 97  LEU   B CA  1 
ATOM   1047 C C   . LEU   B 2 88  ? -17.936 -0.648  -25.686 1.00 37.11  ? 97  LEU   B C   1 
ATOM   1048 O O   . LEU   B 2 88  ? -17.582 -0.155  -26.783 1.00 35.16  ? 97  LEU   B O   1 
ATOM   1049 C CB  . LEU   B 2 88  ? -15.614 -1.187  -24.929 1.00 31.06  ? 97  LEU   B CB  1 
ATOM   1050 C CG  . LEU   B 2 88  ? -15.462 0.177   -24.269 1.00 32.25  ? 97  LEU   B CG  1 
ATOM   1051 C CD1 . LEU   B 2 88  ? -15.903 0.149   -22.809 1.00 36.61  ? 97  LEU   B CD1 1 
ATOM   1052 C CD2 . LEU   B 2 88  ? -14.038 0.670   -24.382 1.00 35.75  ? 97  LEU   B CD2 1 
ATOM   1053 N N   . LEU   B 2 89  ? -19.032 -0.296  -25.028 1.00 36.98  ? 98  LEU   B N   1 
ATOM   1054 C CA  . LEU   B 2 89  ? -19.873 0.857   -25.404 1.00 30.84  ? 98  LEU   B CA  1 
ATOM   1055 C C   . LEU   B 2 89  ? -19.213 2.070   -24.752 1.00 34.32  ? 98  LEU   B C   1 
ATOM   1056 O O   . LEU   B 2 89  ? -19.652 2.502   -23.640 1.00 33.81  ? 98  LEU   B O   1 
ATOM   1057 C CB  . LEU   B 2 89  ? -21.297 0.540   -24.935 1.00 32.69  ? 98  LEU   B CB  1 
ATOM   1058 C CG  . LEU   B 2 89  ? -22.391 1.604   -25.121 1.00 33.91  ? 98  LEU   B CG  1 
ATOM   1059 C CD1 . LEU   B 2 89  ? -22.091 2.542   -26.245 1.00 34.50  ? 98  LEU   B CD1 1 
ATOM   1060 C CD2 . LEU   B 2 89  ? -23.748 0.951   -25.352 1.00 34.91  ? 98  LEU   B CD2 1 
ATOM   1061 N N   . ALA   B 2 90  ? -18.143 2.557   -25.386 1.00 30.42  ? 99  ALA   B N   1 
ATOM   1062 C CA  . ALA   B 2 90  ? -17.390 3.743   -24.936 1.00 31.35  ? 99  ALA   B CA  1 
ATOM   1063 C C   . ALA   B 2 90  ? -18.300 4.956   -25.071 1.00 34.96  ? 99  ALA   B C   1 
ATOM   1064 O O   . ALA   B 2 90  ? -18.929 5.090   -26.137 1.00 38.62  ? 99  ALA   B O   1 
ATOM   1065 C CB  . ALA   B 2 90  ? -16.109 3.972   -25.713 1.00 29.80  ? 99  ALA   B CB  1 
ATOM   1066 N N   . VAL   B 2 91  ? -18.303 5.792   -24.032 1.00 36.81  ? 100 VAL   B N   1 
ATOM   1067 C CA  . VAL   B 2 91  ? -18.895 7.150   -24.015 1.00 31.42  ? 100 VAL   B CA  1 
ATOM   1068 C C   . VAL   B 2 91  ? -17.784 8.107   -23.619 1.00 31.57  ? 100 VAL   B C   1 
ATOM   1069 O O   . VAL   B 2 91  ? -17.620 8.469   -22.463 1.00 31.95  ? 100 VAL   B O   1 
ATOM   1070 C CB  . VAL   B 2 91  ? -20.130 7.170   -23.110 1.00 36.09  ? 100 VAL   B CB  1 
ATOM   1071 C CG1 . VAL   B 2 91  ? -20.799 8.537   -23.105 1.00 39.99  ? 100 VAL   B CG1 1 
ATOM   1072 C CG2 . VAL   B 2 91  ? -21.121 6.075   -23.536 1.00 34.04  ? 100 VAL   B CG2 1 
ATOM   1073 N N   . PRO   B 2 92  ? -16.924 8.481   -24.591 1.00 33.38  ? 101 PRO   B N   1 
ATOM   1074 C CA  . PRO   B 2 92  ? -15.856 9.443   -24.339 1.00 31.74  ? 101 PRO   B CA  1 
ATOM   1075 C C   . PRO   B 2 92  ? -16.358 10.854  -24.086 1.00 33.82  ? 101 PRO   B C   1 
ATOM   1076 O O   . PRO   B 2 92  ? -17.411 11.231  -24.597 1.00 40.02  ? 101 PRO   B O   1 
ATOM   1077 C CB  . PRO   B 2 92  ? -14.999 9.433   -25.610 1.00 35.40  ? 101 PRO   B CB  1 
ATOM   1078 C CG  . PRO   B 2 92  ? -15.541 8.317   -26.493 1.00 35.18  ? 101 PRO   B CG  1 
ATOM   1079 C CD  . PRO   B 2 92  ? -16.868 7.879   -25.931 1.00 35.99  ? 101 PRO   B CD  1 
ATOM   1080 N N   . PRO   B 2 93  ? -15.606 11.688  -23.330 1.00 35.17  ? 102 PRO   B N   1 
ATOM   1081 C CA  . PRO   B 2 93  ? -16.011 13.072  -23.081 1.00 38.53  ? 102 PRO   B CA  1 
ATOM   1082 C C   . PRO   B 2 93  ? -16.118 13.895  -24.383 1.00 42.88  ? 102 PRO   B C   1 
ATOM   1083 O O   . PRO   B 2 93  ? -15.217 13.839  -25.191 1.00 44.58  ? 102 PRO   B O   1 
ATOM   1084 C CB  . PRO   B 2 93  ? -14.927 13.610  -22.138 1.00 36.84  ? 102 PRO   B CB  1 
ATOM   1085 C CG  . PRO   B 2 93  ? -14.329 12.364  -21.521 1.00 37.59  ? 102 PRO   B CG  1 
ATOM   1086 C CD  . PRO   B 2 93  ? -14.345 11.352  -22.653 1.00 36.39  ? 102 PRO   B CD  1 
ATOM   1087 N N   . GLY   B 2 94  ? -17.242 14.593  -24.576 1.00 43.46  ? 103 GLY   B N   1 
ATOM   1088 C CA  . GLY   B 2 94  ? -17.550 15.380  -25.790 1.00 46.30  ? 103 GLY   B CA  1 
ATOM   1089 C C   . GLY   B 2 94  ? -17.978 14.542  -26.997 1.00 42.73  ? 103 GLY   B C   1 
ATOM   1090 O O   . GLY   B 2 94  ? -18.389 15.130  -27.997 1.00 49.33  ? 103 GLY   B O   1 
ATOM   1091 N N   . GLU   B 2 95  ? -17.917 13.219  -26.946 1.00 39.33  ? 104 GLU   B N   1 
ATOM   1092 C CA  . GLU   B 2 95  ? -18.011 12.390  -28.173 1.00 41.49  ? 104 GLU   B CA  1 
ATOM   1093 C C   . GLU   B 2 95  ? -19.178 11.426  -28.013 1.00 41.53  ? 104 GLU   B C   1 
ATOM   1094 O O   . GLU   B 2 95  ? -19.563 11.150  -26.849 1.00 42.13  ? 104 GLU   B O   1 
ATOM   1095 C CB  . GLU   B 2 95  ? -16.681 11.681  -28.442 1.00 43.23  ? 104 GLU   B CB  1 
ATOM   1096 C CG  . GLU   B 2 95  ? -15.498 12.649  -28.568 1.00 47.46  ? 104 GLU   B CG  1 
ATOM   1097 C CD  . GLU   B 2 95  ? -14.143 11.977  -28.775 1.00 52.17  ? 104 GLU   B CD  1 
ATOM   1098 O OE1 . GLU   B 2 95  ? -14.123 10.746  -28.815 1.00 49.85  ? 104 GLU   B OE1 1 
ATOM   1099 O OE2 . GLU   B 2 95  ? -13.109 12.680  -28.885 1.00 54.19  ? 104 GLU   B OE2 1 
ATOM   1100 N N   . ARG   B 2 96  ? -19.760 10.991  -29.130 1.00 38.51  ? 105 ARG   B N   1 
ATOM   1101 C CA  . ARG   B 2 96  ? -20.976 10.142  -29.134 1.00 40.12  ? 105 ARG   B CA  1 
ATOM   1102 C C   . ARG   B 2 96  ? -20.631 8.741   -28.636 1.00 38.26  ? 105 ARG   B C   1 
ATOM   1103 O O   . ARG   B 2 96  ? -19.495 8.281   -28.874 1.00 40.01  ? 105 ARG   B O   1 
ATOM   1104 C CB  . ARG   B 2 96  ? -21.601 10.099  -30.531 1.00 47.76  ? 105 ARG   B CB  1 
ATOM   1105 C CG  . ARG   B 2 96  ? -22.787 9.150   -30.641 1.00 53.03  ? 105 ARG   B CG  1 
ATOM   1106 C CD  . ARG   B 2 96  ? -23.769 9.429   -31.763 1.00 65.83  ? 105 ARG   B CD  1 
ATOM   1107 N NE  . ARG   B 2 96  ? -23.161 9.341   -33.080 1.00 69.18  ? 105 ARG   B NE  1 
ATOM   1108 C CZ  . ARG   B 2 96  ? -22.613 10.357  -33.736 1.00 74.83  ? 105 ARG   B CZ  1 
ATOM   1109 N NH1 . ARG   B 2 96  ? -22.597 11.578  -33.223 1.00 75.18  ? 105 ARG   B NH1 1 
ATOM   1110 N NH2 . ARG   B 2 96  ? -22.079 10.147  -34.926 1.00 82.28  ? 105 ARG   B NH2 1 
ATOM   1111 N N   . ALA   B 2 97  ? -21.594 8.069   -28.002 1.00 40.26  ? 106 ALA   B N   1 
ATOM   1112 C CA  . ALA   B 2 97  ? -21.507 6.634   -27.669 1.00 40.26  ? 106 ALA   B CA  1 
ATOM   1113 C C   . ALA   B 2 97  ? -20.980 5.910   -28.914 1.00 42.91  ? 106 ALA   B C   1 
ATOM   1114 O O   . ALA   B 2 97  ? -21.505 6.160   -29.998 1.00 40.29  ? 106 ALA   B O   1 
ATOM   1115 C CB  . ALA   B 2 97  ? -22.852 6.104   -27.242 1.00 42.58  ? 106 ALA   B CB  1 
ATOM   1116 N N   . LYS   B 2 98  ? -19.986 5.038   -28.759 1.00 44.04  ? 107 LYS   B N   1 
ATOM   1117 C CA  . LYS   B 2 98  ? -19.453 4.187   -29.857 1.00 48.76  ? 107 LYS   B CA  1 
ATOM   1118 C C   . LYS   B 2 98  ? -19.188 2.777   -29.322 1.00 46.14  ? 107 LYS   B C   1 
ATOM   1119 O O   . LYS   B 2 98  ? -18.527 2.681   -28.276 1.00 41.00  ? 107 LYS   B O   1 
ATOM   1120 C CB  . LYS   B 2 98  ? -18.165 4.801   -30.407 1.00 56.97  ? 107 LYS   B CB  1 
ATOM   1121 C CG  . LYS   B 2 98  ? -17.624 4.126   -31.666 1.00 68.33  ? 107 LYS   B CG  1 
ATOM   1122 C CD  . LYS   B 2 98  ? -16.300 4.680   -32.155 1.00 74.47  ? 107 LYS   B CD  1 
ATOM   1123 C CE  . LYS   B 2 98  ? -15.379 5.063   -31.013 1.00 79.43  ? 107 LYS   B CE  1 
ATOM   1124 N NZ  . LYS   B 2 98  ? -13.956 4.988   -31.411 1.00 87.89  ? 107 LYS   B NZ  1 
ATOM   1125 N N   . ASN   B 2 99  ? -19.738 1.749   -29.977 1.00 40.54  ? 108 ASN   B N   1 
ATOM   1126 C CA  . ASN   B 2 99  ? -19.396 0.328   -29.732 1.00 45.71  ? 108 ASN   B CA  1 
ATOM   1127 C C   . ASN   B 2 99  ? -18.015 0.045   -30.340 1.00 46.17  ? 108 ASN   B C   1 
ATOM   1128 O O   . ASN   B 2 99  ? -17.809 0.398   -31.510 1.00 48.17  ? 108 ASN   B O   1 
ATOM   1129 C CB  . ASN   B 2 99  ? -20.452 -0.639  -30.285 1.00 43.72  ? 108 ASN   B CB  1 
ATOM   1130 C CG  . ASN   B 2 99  ? -21.812 -0.421  -29.668 1.00 45.63  ? 108 ASN   B CG  1 
ATOM   1131 O OD1 . ASN   B 2 99  ? -22.351 0.677   -29.764 1.00 52.25  ? 108 ASN   B OD1 1 
ATOM   1132 N ND2 . ASN   B 2 99  ? -22.393 -1.450  -29.066 1.00 42.66  ? 108 ASN   B ND2 1 
ATOM   1133 N N   . ILE   B 2 100 ? -17.111 -0.570  -29.572 1.00 41.20  ? 109 ILE   B N   1 
ATOM   1134 C CA  . ILE   B 2 100 ? -15.818 -1.136  -30.047 1.00 39.37  ? 109 ILE   B CA  1 
ATOM   1135 C C   . ILE   B 2 100 ? -15.806 -2.625  -29.705 1.00 44.49  ? 109 ILE   B C   1 
ATOM   1136 O O   . ILE   B 2 100 ? -15.986 -2.972  -28.521 1.00 44.25  ? 109 ILE   B O   1 
ATOM   1137 C CB  . ILE   B 2 100 ? -14.630 -0.413  -29.402 1.00 45.01  ? 109 ILE   B CB  1 
ATOM   1138 C CG1 . ILE   B 2 100 ? -14.808 1.103   -29.401 1.00 46.27  ? 109 ILE   B CG1 1 
ATOM   1139 C CG2 . ILE   B 2 100 ? -13.330 -0.827  -30.065 1.00 46.02  ? 109 ILE   B CG2 1 
ATOM   1140 C CD1 . ILE   B 2 100 ? -14.706 1.711   -30.760 1.00 49.15  ? 109 ILE   B CD1 1 
ATOM   1141 N N   . GLN   B 2 101 ? -15.651 -3.494  -30.699 1.00 41.92  ? 110 GLN   B N   1 
ATOM   1142 C CA  . GLN   B 2 101 ? -15.693 -4.957  -30.492 1.00 39.92  ? 110 GLN   B CA  1 
ATOM   1143 C C   . GLN   B 2 101 ? -14.259 -5.479  -30.311 1.00 43.14  ? 110 GLN   B C   1 
ATOM   1144 O O   . GLN   B 2 101 ? -13.332 -4.922  -30.936 1.00 42.19  ? 110 GLN   B O   1 
ATOM   1145 C CB  . GLN   B 2 101 ? -16.432 -5.630  -31.631 1.00 43.63  ? 110 GLN   B CB  1 
ATOM   1146 C CG  . GLN   B 2 101 ? -16.244 -7.133  -31.627 1.00 42.15  ? 110 GLN   B CG  1 
ATOM   1147 C CD  . GLN   B 2 101 ? -17.382 -7.804  -32.344 1.00 46.86  ? 110 GLN   B CD  1 
ATOM   1148 O OE1 . GLN   B 2 101 ? -18.468 -7.251  -32.482 1.00 44.68  ? 110 GLN   B OE1 1 
ATOM   1149 N NE2 . GLN   B 2 101 ? -17.134 -9.006  -32.828 1.00 46.84  ? 110 GLN   B NE2 1 
ATOM   1150 N N   . THR   B 2 102 ? -14.073 -6.465  -29.421 1.00 43.37  ? 111 THR   B N   1 
ATOM   1151 C CA  . THR   B 2 102 ? -12.737 -6.900  -28.940 1.00 40.98  ? 111 THR   B CA  1 
ATOM   1152 C C   . THR   B 2 102 ? -12.888 -8.271  -28.303 1.00 41.70  ? 111 THR   B C   1 
ATOM   1153 O O   . THR   B 2 102 ? -14.020 -8.605  -27.903 1.00 45.70  ? 111 THR   B O   1 
ATOM   1154 C CB  . THR   B 2 102 ? -12.090 -5.838  -28.038 1.00 42.10  ? 111 THR   B CB  1 
ATOM   1155 O OG1 . THR   B 2 102 ? -10.666 -5.953  -28.074 1.00 42.18  ? 111 THR   B OG1 1 
ATOM   1156 C CG2 . THR   B 2 102 ? -12.553 -5.910  -26.600 1.00 46.11  ? 111 THR   B CG2 1 
ATOM   1157 N N   . LEU   B 2 103 ? -11.806 -9.059  -28.328 1.00 40.86  ? 112 LEU   B N   1 
ATOM   1158 C CA  . LEU   B 2 103 ? -11.666 -10.326 -27.558 1.00 43.63  ? 112 LEU   B CA  1 
ATOM   1159 C C   . LEU   B 2 103 ? -10.875 -9.984  -26.305 1.00 42.21  ? 112 LEU   B C   1 
ATOM   1160 O O   . LEU   B 2 103 ? -9.718  -9.533  -26.396 1.00 39.73  ? 112 LEU   B O   1 
ATOM   1161 C CB  . LEU   B 2 103 ? -10.923 -11.408 -28.354 1.00 48.48  ? 112 LEU   B CB  1 
ATOM   1162 C CG  . LEU   B 2 103 ? -10.710 -12.731 -27.614 1.00 44.00  ? 112 LEU   B CG  1 
ATOM   1163 C CD1 . LEU   B 2 103 ? -12.012 -13.514 -27.531 1.00 42.49  ? 112 LEU   B CD1 1 
ATOM   1164 C CD2 . LEU   B 2 103 ? -9.612  -13.555 -28.276 1.00 46.76  ? 112 LEU   B CD2 1 
ATOM   1165 N N   . PRO   B 2 104 ? -11.477 -10.155 -25.107 1.00 41.16  ? 113 PRO   B N   1 
ATOM   1166 C CA  . PRO   B 2 104 ? -10.780 -9.806  -23.875 1.00 45.47  ? 113 PRO   B CA  1 
ATOM   1167 C C   . PRO   B 2 104 ? -9.607  -10.771 -23.663 1.00 43.59  ? 113 PRO   B C   1 
ATOM   1168 O O   . PRO   B 2 104 ? -9.736  -11.946 -24.003 1.00 41.05  ? 113 PRO   B O   1 
ATOM   1169 C CB  . PRO   B 2 104 ? -11.819 -9.975  -22.755 1.00 46.97  ? 113 PRO   B CB  1 
ATOM   1170 C CG  . PRO   B 2 104 ? -13.152 -10.144 -23.474 1.00 47.26  ? 113 PRO   B CG  1 
ATOM   1171 C CD  . PRO   B 2 104 ? -12.822 -10.696 -24.854 1.00 46.09  ? 113 PRO   B CD  1 
ATOM   1172 N N   . GLY   B 2 105 ? -8.510  -10.231 -23.134 1.00 45.28  ? 114 GLY   B N   1 
ATOM   1173 C CA  . GLY   B 2 105 ? -7.461  -10.984 -22.429 1.00 44.81  ? 114 GLY   B CA  1 
ATOM   1174 C C   . GLY   B 2 105 ? -7.934  -11.400 -21.047 1.00 44.84  ? 114 GLY   B C   1 
ATOM   1175 O O   . GLY   B 2 105 ? -9.161  -11.541 -20.840 1.00 39.22  ? 114 GLY   B O   1 
ATOM   1176 N N   . ILE   B 2 106 ? -6.988  -11.649 -20.146 1.00 44.63  ? 115 ILE   B N   1 
ATOM   1177 C CA  . ILE   B 2 106 ? -7.257  -12.282 -18.826 1.00 45.50  ? 115 ILE   B CA  1 
ATOM   1178 C C   . ILE   B 2 106 ? -6.292  -11.705 -17.789 1.00 44.75  ? 115 ILE   B C   1 
ATOM   1179 O O   . ILE   B 2 106 ? -5.088  -11.788 -17.980 1.00 50.73  ? 115 ILE   B O   1 
ATOM   1180 C CB  . ILE   B 2 106 ? -7.150  -13.811 -18.924 1.00 47.86  ? 115 ILE   B CB  1 
ATOM   1181 C CG1 . ILE   B 2 106 ? -8.230  -14.414 -19.825 1.00 48.66  ? 115 ILE   B CG1 1 
ATOM   1182 C CG2 . ILE   B 2 106 ? -7.220  -14.414 -17.540 1.00 54.58  ? 115 ILE   B CG2 1 
ATOM   1183 C CD1 . ILE   B 2 106 ? -8.221  -15.931 -19.885 1.00 50.20  ? 115 ILE   B CD1 1 
ATOM   1184 N N   . PHE   B 2 107 ? -6.834  -11.109 -16.735 1.00 45.82  ? 116 PHE   B N   1 
ATOM   1185 C CA  . PHE   B 2 107 ? -6.110  -10.777 -15.485 1.00 42.16  ? 116 PHE   B CA  1 
ATOM   1186 C C   . PHE   B 2 107 ? -6.046  -12.056 -14.652 1.00 39.54  ? 116 PHE   B C   1 
ATOM   1187 O O   . PHE   B 2 107 ? -7.114  -12.591 -14.324 1.00 38.32  ? 116 PHE   B O   1 
ATOM   1188 C CB  . PHE   B 2 107 ? -6.852  -9.669  -14.729 1.00 43.25  ? 116 PHE   B CB  1 
ATOM   1189 C CG  . PHE   B 2 107 ? -6.544  -8.252  -15.137 1.00 40.63  ? 116 PHE   B CG  1 
ATOM   1190 C CD1 . PHE   B 2 107 ? -5.891  -7.961  -16.326 1.00 38.82  ? 116 PHE   B CD1 1 
ATOM   1191 C CD2 . PHE   B 2 107 ? -6.953  -7.201  -14.330 1.00 39.37  ? 116 PHE   B CD2 1 
ATOM   1192 C CE1 . PHE   B 2 107 ? -5.615  -6.651  -16.678 1.00 40.94  ? 116 PHE   B CE1 1 
ATOM   1193 C CE2 . PHE   B 2 107 ? -6.677  -5.890  -14.685 1.00 41.14  ? 116 PHE   B CE2 1 
ATOM   1194 C CZ  . PHE   B 2 107 ? -5.997  -5.616  -15.853 1.00 41.41  ? 116 PHE   B CZ  1 
ATOM   1195 N N   . LYS   B 2 108 ? -4.844  -12.557 -14.374 1.00 41.88  ? 117 LYS   B N   1 
ATOM   1196 C CA  . LYS   B 2 108 ? -4.615  -13.726 -13.468 1.00 47.54  ? 117 LYS   B CA  1 
ATOM   1197 C C   . LYS   B 2 108 ? -4.295  -13.196 -12.058 1.00 38.67  ? 117 LYS   B C   1 
ATOM   1198 O O   . LYS   B 2 108 ? -3.279  -12.500 -11.910 1.00 38.23  ? 117 LYS   B O   1 
ATOM   1199 C CB  . LYS   B 2 108 ? -3.482  -14.618 -14.007 1.00 54.21  ? 117 LYS   B CB  1 
ATOM   1200 C CG  . LYS   B 2 108 ? -3.878  -15.623 -15.088 1.00 65.76  ? 117 LYS   B CG  1 
ATOM   1201 C CD  . LYS   B 2 108 ? -2.710  -16.268 -15.837 1.00 72.96  ? 117 LYS   B CD  1 
ATOM   1202 C CE  . LYS   B 2 108 ? -3.087  -17.544 -16.578 1.00 81.28  ? 117 LYS   B CE  1 
ATOM   1203 N NZ  . LYS   B 2 108 ? -2.256  -17.789 -17.791 1.00 81.39  ? 117 LYS   B NZ  1 
ATOM   1204 N N   . THR   B 2 109 ? -5.148  -13.484 -11.073 1.00 41.65  ? 118 THR   B N   1 
ATOM   1205 C CA  . THR   B 2 109 ? -4.937  -13.097 -9.648  1.00 43.40  ? 118 THR   B CA  1 
ATOM   1206 C C   . THR   B 2 109 ? -5.003  -14.334 -8.745  1.00 41.79  ? 118 THR   B C   1 
ATOM   1207 O O   . THR   B 2 109 ? -5.586  -15.353 -9.147  1.00 36.85  ? 118 THR   B O   1 
ATOM   1208 C CB  . THR   B 2 109 ? -5.971  -12.070 -9.159  1.00 42.30  ? 118 THR   B CB  1 
ATOM   1209 O OG1 . THR   B 2 109 ? -7.168  -12.757 -8.798  1.00 39.18  ? 118 THR   B OG1 1 
ATOM   1210 C CG2 . THR   B 2 109 ? -6.297  -11.018 -10.193 1.00 41.70  ? 118 THR   B CG2 1 
ATOM   1211 N N   . LYS   B 2 110 ? -4.482  -14.199 -7.529  1.00 45.28  ? 119 LYS   B N   1 
ATOM   1212 C CA  . LYS   B 2 110 ? -4.508  -15.253 -6.479  1.00 46.72  ? 119 LYS   B CA  1 
ATOM   1213 C C   . LYS   B 2 110 ? -5.959  -15.696 -6.222  1.00 51.24  ? 119 LYS   B C   1 
ATOM   1214 O O   . LYS   B 2 110 ? -6.148  -16.863 -5.815  1.00 53.77  ? 119 LYS   B O   1 
ATOM   1215 C CB  . LYS   B 2 110 ? -3.810  -14.744 -5.213  1.00 49.01  ? 119 LYS   B CB  1 
ATOM   1216 C CG  . LYS   B 2 110 ? -4.448  -13.520 -4.576  1.00 53.04  ? 119 LYS   B CG  1 
ATOM   1217 C CD  . LYS   B 2 110 ? -3.667  -12.953 -3.419  1.00 55.19  ? 119 LYS   B CD  1 
ATOM   1218 C CE  . LYS   B 2 110 ? -4.327  -13.215 -2.084  1.00 59.78  ? 119 LYS   B CE  1 
ATOM   1219 N NZ  . LYS   B 2 110 ? -5.409  -12.243 -1.827  1.00 56.36  ? 119 LYS   B NZ  1 
ATOM   1220 N N   . ASP   B 2 111 ? -6.955  -14.839 -6.468  1.00 46.89  ? 120 ASP   B N   1 
ATOM   1221 C CA  . ASP   B 2 111 ? -8.371  -15.145 -6.122  1.00 49.36  ? 120 ASP   B CA  1 
ATOM   1222 C C   . ASP   B 2 111 ? -9.159  -15.579 -7.356  1.00 49.54  ? 120 ASP   B C   1 
ATOM   1223 O O   . ASP   B 2 111 ? -10.350 -15.852 -7.199  1.00 59.41  ? 120 ASP   B O   1 
ATOM   1224 C CB  . ASP   B 2 111 ? -9.032  -13.958 -5.425  1.00 49.43  ? 120 ASP   B CB  1 
ATOM   1225 C CG  . ASP   B 2 111 ? -8.339  -13.622 -4.121  1.00 51.74  ? 120 ASP   B CG  1 
ATOM   1226 O OD1 . ASP   B 2 111 ? -7.874  -14.552 -3.446  1.00 56.93  ? 120 ASP   B OD1 1 
ATOM   1227 O OD2 . ASP   B 2 111 ? -8.247  -12.445 -3.808  1.00 58.90  ? 120 ASP   B OD2 1 
ATOM   1228 N N   . GLY   B 2 112 ? -8.512  -15.666 -8.518  1.00 48.99  ? 121 GLY   B N   1 
ATOM   1229 C CA  . GLY   B 2 112 ? -9.153  -16.136 -9.757  1.00 48.03  ? 121 GLY   B CA  1 
ATOM   1230 C C   . GLY   B 2 112 ? -8.829  -15.248 -10.944 1.00 49.01  ? 121 GLY   B C   1 
ATOM   1231 O O   . GLY   B 2 112 ? -8.179  -14.191 -10.759 1.00 49.98  ? 121 GLY   B O   1 
ATOM   1232 N N   . ASP   B 2 113 ? -9.269  -15.668 -12.129 1.00 49.99  ? 122 ASP   B N   1 
ATOM   1233 C CA  . ASP   B 2 113 ? -9.035  -14.958 -13.413 1.00 50.90  ? 122 ASP   B CA  1 
ATOM   1234 C C   . ASP   B 2 113 ? -10.216 -14.039 -13.720 1.00 47.72  ? 122 ASP   B C   1 
ATOM   1235 O O   . ASP   B 2 113 ? -11.366 -14.407 -13.402 1.00 45.39  ? 122 ASP   B O   1 
ATOM   1236 C CB  . ASP   B 2 113 ? -8.866  -15.940 -14.568 1.00 55.83  ? 122 ASP   B CB  1 
ATOM   1237 C CG  . ASP   B 2 113 ? -7.589  -16.754 -14.509 1.00 59.12  ? 122 ASP   B CG  1 
ATOM   1238 O OD1 . ASP   B 2 113 ? -6.636  -16.303 -13.852 1.00 61.81  ? 122 ASP   B OD1 1 
ATOM   1239 O OD2 . ASP   B 2 113 ? -7.559  -17.820 -15.149 1.00 72.81  ? 122 ASP   B OD2 1 
ATOM   1240 N N   . ILE   B 2 114 ? -9.930  -12.906 -14.354 1.00 44.92  ? 123 ILE   B N   1 
ATOM   1241 C CA  . ILE   B 2 114 ? -10.944 -11.890 -14.756 1.00 47.12  ? 123 ILE   B CA  1 
ATOM   1242 C C   . ILE   B 2 114 ? -10.683 -11.549 -16.221 1.00 39.46  ? 123 ILE   B C   1 
ATOM   1243 O O   . ILE   B 2 114 ? -9.517  -11.362 -16.538 1.00 35.74  ? 123 ILE   B O   1 
ATOM   1244 C CB  . ILE   B 2 114 ? -10.828 -10.625 -13.877 1.00 49.61  ? 123 ILE   B CB  1 
ATOM   1245 C CG1 . ILE   B 2 114 ? -10.690 -10.961 -12.391 1.00 54.53  ? 123 ILE   B CG1 1 
ATOM   1246 C CG2 . ILE   B 2 114 ? -11.988 -9.672  -14.132 1.00 51.58  ? 123 ILE   B CG2 1 
ATOM   1247 C CD1 . ILE   B 2 114 ? -10.005 -9.878  -11.594 1.00 58.76  ? 123 ILE   B CD1 1 
ATOM   1248 N N   . GLY   B 2 115 ? -11.733 -11.390 -17.027 1.00 38.80  ? 124 GLY   B N   1 
ATOM   1249 C CA  . GLY   B 2 115 ? -11.662 -10.704 -18.335 1.00 34.66  ? 124 GLY   B CA  1 
ATOM   1250 C C   . GLY   B 2 115 ? -10.901 -9.398  -18.215 1.00 36.30  ? 124 GLY   B C   1 
ATOM   1251 O O   . GLY   B 2 115 ? -10.889 -8.768  -17.128 1.00 35.50  ? 124 GLY   B O   1 
ATOM   1252 N N   . ALA   B 2 116 ? -10.212 -9.016  -19.279 1.00 34.53  ? 125 ALA   B N   1 
ATOM   1253 C CA  . ALA   B 2 116 ? -9.561  -7.702  -19.406 1.00 36.86  ? 125 ALA   B CA  1 
ATOM   1254 C C   . ALA   B 2 116 ? -9.701  -7.220  -20.858 1.00 39.61  ? 125 ALA   B C   1 
ATOM   1255 O O   . ALA   B 2 116 ? -9.637  -8.040  -21.777 1.00 43.24  ? 125 ALA   B O   1 
ATOM   1256 C CB  . ALA   B 2 116 ? -8.129  -7.825  -18.985 1.00 40.03  ? 125 ALA   B CB  1 
ATOM   1257 N N   A VAL   B 2 117 ? -9.888  -5.911  -21.049 0.13 40.28  ? 126 VAL   B N   1 
ATOM   1258 N N   B VAL   B 2 117 ? -9.857  -5.902  -21.028 0.19 39.57  ? 126 VAL   B N   1 
ATOM   1259 N N   C VAL   B 2 117 ? -9.891  -5.912  -21.050 0.35 40.42  ? 126 VAL   B N   1 
ATOM   1260 N N   D VAL   B 2 117 ? -9.859  -5.903  -21.029 0.33 39.61  ? 126 VAL   B N   1 
ATOM   1261 C CA  A VAL   B 2 117 ? -9.997  -5.273  -22.396 0.13 40.48  ? 126 VAL   B CA  1 
ATOM   1262 C CA  B VAL   B 2 117 ? -10.022 -5.195  -22.335 0.19 39.31  ? 126 VAL   B CA  1 
ATOM   1263 C CA  C VAL   B 2 117 ? -9.998  -5.273  -22.397 0.35 40.71  ? 126 VAL   B CA  1 
ATOM   1264 C CA  D VAL   B 2 117 ? -10.023 -5.194  -22.334 0.33 39.31  ? 126 VAL   B CA  1 
ATOM   1265 C C   A VAL   B 2 117 ? -8.868  -4.247  -22.546 0.13 40.44  ? 126 VAL   B C   1 
ATOM   1266 C C   B VAL   B 2 117 ? -8.838  -4.240  -22.524 0.19 39.79  ? 126 VAL   B C   1 
ATOM   1267 C C   C VAL   B 2 117 ? -8.870  -4.247  -22.546 0.35 40.78  ? 126 VAL   B C   1 
ATOM   1268 C C   D VAL   B 2 117 ? -8.838  -4.239  -22.523 0.33 39.96  ? 126 VAL   B C   1 
ATOM   1269 O O   A VAL   B 2 117 ? -8.669  -3.443  -21.615 0.13 39.36  ? 126 VAL   B O   1 
ATOM   1270 O O   B VAL   B 2 117 ? -8.579  -3.450  -21.594 0.19 38.55  ? 126 VAL   B O   1 
ATOM   1271 O O   C VAL   B 2 117 ? -8.670  -3.446  -21.614 0.35 39.03  ? 126 VAL   B O   1 
ATOM   1272 O O   D VAL   B 2 117 ? -8.579  -3.451  -21.594 0.33 38.30  ? 126 VAL   B O   1 
ATOM   1273 C CB  A VAL   B 2 117 ? -11.390 -4.657  -22.636 0.13 41.19  ? 126 VAL   B CB  1 
ATOM   1274 C CB  B VAL   B 2 117 ? -11.369 -4.447  -22.374 0.19 39.09  ? 126 VAL   B CB  1 
ATOM   1275 C CB  C VAL   B 2 117 ? -11.390 -4.656  -22.637 0.35 41.66  ? 126 VAL   B CB  1 
ATOM   1276 C CB  D VAL   B 2 117 ? -11.369 -4.445  -22.373 0.33 39.05  ? 126 VAL   B CB  1 
ATOM   1277 C CG1 A VAL   B 2 117 ? -12.445 -5.741  -22.800 0.13 41.53  ? 126 VAL   B CG1 1 
ATOM   1278 C CG1 B VAL   B 2 117 ? -11.454 -3.459  -23.527 0.19 38.18  ? 126 VAL   B CG1 1 
ATOM   1279 C CG1 C VAL   B 2 117 ? -12.442 -5.744  -22.799 0.35 42.07  ? 126 VAL   B CG1 1 
ATOM   1280 C CG1 D VAL   B 2 117 ? -11.455 -3.457  -23.525 0.33 37.73  ? 126 VAL   B CG1 1 
ATOM   1281 C CG2 A VAL   B 2 117 ? -11.797 -3.673  -21.549 0.13 40.81  ? 126 VAL   B CG2 1 
ATOM   1282 C CG2 B VAL   B 2 117 ? -12.537 -5.421  -22.415 0.19 39.52  ? 126 VAL   B CG2 1 
ATOM   1283 C CG2 C VAL   B 2 117 ? -11.798 -3.672  -21.550 0.35 40.80  ? 126 VAL   B CG2 1 
ATOM   1284 C CG2 D VAL   B 2 117 ? -12.535 -5.422  -22.416 0.33 39.70  ? 126 VAL   B CG2 1 
ATOM   1285 N N   . ALA   B 2 118 ? -8.146  -4.310  -23.671 1.00 38.75  ? 127 ALA   B N   1 
ATOM   1286 C CA  . ALA   B 2 118 ? -6.990  -3.426  -23.982 1.00 42.62  ? 127 ALA   B CA  1 
ATOM   1287 C C   . ALA   B 2 118 ? -7.402  -2.409  -25.047 1.00 51.39  ? 127 ALA   B C   1 
ATOM   1288 O O   . ALA   B 2 118 ? -7.039  -2.593  -26.223 1.00 52.37  ? 127 ALA   B O   1 
ATOM   1289 C CB  . ALA   B 2 118 ? -5.817  -4.250  -24.455 1.00 45.08  ? 127 ALA   B CB  1 
ATOM   1290 N N   . LEU   B 2 119 ? -8.186  -1.406  -24.652 1.00 49.51  ? 128 LEU   B N   1 
ATOM   1291 C CA  . LEU   B 2 119 ? -8.561  -0.272  -25.518 1.00 45.60  ? 128 LEU   B CA  1 
ATOM   1292 C C   . LEU   B 2 119 ? -8.188  0.983   -24.737 1.00 52.68  ? 128 LEU   B C   1 
ATOM   1293 O O   . LEU   B 2 119 ? -8.468  1.007   -23.528 1.00 62.60  ? 128 LEU   B O   1 
ATOM   1294 C CB  . LEU   B 2 119 ? -10.054 -0.363  -25.843 1.00 45.02  ? 128 LEU   B CB  1 
ATOM   1295 C CG  . LEU   B 2 119 ? -10.528 -1.714  -26.386 1.00 42.90  ? 128 LEU   B CG  1 
ATOM   1296 C CD1 . LEU   B 2 119 ? -12.040 -1.833  -26.327 1.00 39.71  ? 128 LEU   B CD1 1 
ATOM   1297 C CD2 . LEU   B 2 119 ? -10.050 -1.941  -27.815 1.00 47.79  ? 128 LEU   B CD2 1 
ATOM   1298 N N   . ASP   B 2 120 ? -7.478  1.906   -25.380 1.00 53.84  ? 129 ASP   B N   1 
ATOM   1299 C CA  . ASP   B 2 120 ? -7.139  3.240   -24.833 1.00 61.56  ? 129 ASP   B CA  1 
ATOM   1300 C C   . ASP   B 2 120 ? -8.394  4.111   -24.923 1.00 58.40  ? 129 ASP   B C   1 
ATOM   1301 O O   . ASP   B 2 120 ? -8.946  4.228   -26.015 1.00 65.71  ? 129 ASP   B O   1 
ATOM   1302 C CB  . ASP   B 2 120 ? -5.979  3.882   -25.606 1.00 75.30  ? 129 ASP   B CB  1 
ATOM   1303 C CG  . ASP   B 2 120 ? -4.600  3.392   -25.194 1.00 88.13  ? 129 ASP   B CG  1 
ATOM   1304 O OD1 . ASP   B 2 120 ? -4.260  3.543   -23.993 1.00 91.20  ? 129 ASP   B OD1 1 
ATOM   1305 O OD2 . ASP   B 2 120 ? -3.871  2.878   -26.077 1.00 91.53  ? 129 ASP   B OD2 1 
ATOM   1306 N N   . TYR   B 2 121 ? -8.844  4.687   -23.815 1.00 52.28  ? 130 TYR   B N   1 
ATOM   1307 C CA  . TYR   B 2 121 ? -9.785  5.831   -23.825 1.00 47.11  ? 130 TYR   B CA  1 
ATOM   1308 C C   . TYR   B 2 121 ? -9.419  6.730   -22.655 1.00 44.45  ? 130 TYR   B C   1 
ATOM   1309 O O   . TYR   B 2 121 ? -8.758  6.294   -21.720 1.00 47.97  ? 130 TYR   B O   1 
ATOM   1310 C CB  . TYR   B 2 121 ? -11.228 5.337   -23.783 1.00 47.72  ? 130 TYR   B CB  1 
ATOM   1311 C CG  . TYR   B 2 121 ? -11.812 4.851   -25.087 1.00 50.80  ? 130 TYR   B CG  1 
ATOM   1312 C CD1 . TYR   B 2 121 ? -12.297 5.746   -26.028 1.00 56.42  ? 130 TYR   B CD1 1 
ATOM   1313 C CD2 . TYR   B 2 121 ? -11.955 3.499   -25.361 1.00 54.36  ? 130 TYR   B CD2 1 
ATOM   1314 C CE1 . TYR   B 2 121 ? -12.874 5.315   -27.214 1.00 55.48  ? 130 TYR   B CE1 1 
ATOM   1315 C CE2 . TYR   B 2 121 ? -12.519 3.049   -26.548 1.00 54.37  ? 130 TYR   B CE2 1 
ATOM   1316 C CZ  . TYR   B 2 121 ? -12.981 3.962   -27.479 1.00 56.20  ? 130 TYR   B CZ  1 
ATOM   1317 O OH  . TYR   B 2 121 ? -13.550 3.547   -28.649 1.00 61.83  ? 130 TYR   B OH  1 
ATOM   1318 N N   . PRO   B 2 122 ? -9.815  8.015   -22.645 1.00 42.66  ? 131 PRO   B N   1 
ATOM   1319 C CA  . PRO   B 2 122 ? -9.511  8.870   -21.503 1.00 47.53  ? 131 PRO   B CA  1 
ATOM   1320 C C   . PRO   B 2 122 ? -10.191 8.312   -20.234 1.00 40.95  ? 131 PRO   B C   1 
ATOM   1321 O O   . PRO   B 2 122 ? -11.048 7.458   -20.341 1.00 40.82  ? 131 PRO   B O   1 
ATOM   1322 C CB  . PRO   B 2 122 ? -10.038 10.256  -21.928 1.00 53.09  ? 131 PRO   B CB  1 
ATOM   1323 C CG  . PRO   B 2 122 ? -10.244 10.163  -23.434 1.00 49.14  ? 131 PRO   B CG  1 
ATOM   1324 C CD  . PRO   B 2 122 ? -10.569 8.708   -23.702 1.00 47.47  ? 131 PRO   B CD  1 
ATOM   1325 N N   . ALA   B 2 123 ? -9.753  8.777   -19.067 1.00 40.10  ? 132 ALA   B N   1 
ATOM   1326 C CA  . ALA   B 2 123 ? -10.202 8.272   -17.752 1.00 39.44  ? 132 ALA   B CA  1 
ATOM   1327 C C   . ALA   B 2 123 ? -11.688 8.616   -17.564 1.00 40.52  ? 132 ALA   B C   1 
ATOM   1328 O O   . ALA   B 2 123 ? -12.428 7.773   -16.942 1.00 35.52  ? 132 ALA   B O   1 
ATOM   1329 C CB  . ALA   B 2 123 ? -9.313  8.810   -16.665 1.00 38.15  ? 132 ALA   B CB  1 
ATOM   1330 N N   . GLY   B 2 124 ? -12.137 9.714   -18.203 1.00 39.12  ? 133 GLY   B N   1 
ATOM   1331 C CA  . GLY   B 2 124 ? -13.544 10.172  -18.219 1.00 34.52  ? 133 GLY   B CA  1 
ATOM   1332 C C   . GLY   B 2 124 ? -14.484 9.159   -18.861 1.00 33.40  ? 133 GLY   B C   1 
ATOM   1333 O O   . GLY   B 2 124 ? -15.731 9.340   -18.727 1.00 33.69  ? 133 GLY   B O   1 
ATOM   1334 N N   . THR   B 2 125 ? -13.951 8.128   -19.532 1.00 26.69  ? 134 THR   B N   1 
ATOM   1335 C CA  . THR   B 2 125 ? -14.734 7.008   -20.106 1.00 29.73  ? 134 THR   B CA  1 
ATOM   1336 C C   . THR   B 2 125 ? -15.051 5.936   -19.037 1.00 29.93  ? 134 THR   B C   1 
ATOM   1337 O O   . THR   B 2 125 ? -15.878 5.046   -19.336 1.00 29.10  ? 134 THR   B O   1 
ATOM   1338 C CB  . THR   B 2 125 ? -13.981 6.450   -21.321 1.00 34.31  ? 134 THR   B CB  1 
ATOM   1339 O OG1 . THR   B 2 125 ? -13.677 7.550   -22.176 1.00 40.59  ? 134 THR   B OG1 1 
ATOM   1340 C CG2 . THR   B 2 125 ? -14.766 5.454   -22.136 1.00 34.01  ? 134 THR   B CG2 1 
ATOM   1341 N N   . SER   B 2 126 ? -14.407 5.991   -17.860 1.00 31.87  ? 135 SER   B N   1 
ATOM   1342 C CA  . SER   B 2 126 ? -14.526 4.976   -16.771 1.00 34.54  ? 135 SER   B CA  1 
ATOM   1343 C C   . SER   B 2 126 ? -16.008 4.770   -16.426 1.00 33.40  ? 135 SER   B C   1 
ATOM   1344 O O   . SER   B 2 126 ? -16.675 5.786   -16.236 1.00 33.01  ? 135 SER   B O   1 
ATOM   1345 C CB  . SER   B 2 126 ? -13.760 5.405   -15.549 1.00 35.73  ? 135 SER   B CB  1 
ATOM   1346 O OG  . SER   B 2 126 ? -12.365 5.294   -15.712 1.00 37.82  ? 135 SER   B OG  1 
ATOM   1347 N N   . GLY   B 2 127 ? -16.482 3.523   -16.360 1.00 30.97  ? 136 GLY   B N   1 
ATOM   1348 C CA  . GLY   B 2 127 ? -17.887 3.162   -16.078 1.00 33.59  ? 136 GLY   B CA  1 
ATOM   1349 C C   . GLY   B 2 127 ? -18.660 2.754   -17.309 1.00 31.75  ? 136 GLY   B C   1 
ATOM   1350 O O   . GLY   B 2 127 ? -19.810 2.269   -17.157 1.00 31.42  ? 136 GLY   B O   1 
ATOM   1351 N N   . SER   B 2 128 ? -18.099 2.957   -18.509 1.00 34.02  ? 137 SER   B N   1 
ATOM   1352 C CA  . SER   B 2 128 ? -18.744 2.497   -19.768 1.00 31.09  ? 137 SER   B CA  1 
ATOM   1353 C C   . SER   B 2 128 ? -18.977 1.003   -19.663 1.00 28.05  ? 137 SER   B C   1 
ATOM   1354 O O   . SER   B 2 128 ? -18.108 0.279   -19.188 1.00 32.31  ? 137 SER   B O   1 
ATOM   1355 C CB  . SER   B 2 128 ? -17.924 2.852   -20.992 1.00 33.82  ? 137 SER   B CB  1 
ATOM   1356 O OG  . SER   B 2 128 ? -17.673 4.248   -21.050 1.00 30.52  ? 137 SER   B OG  1 
ATOM   1357 N N   . PRO   B 2 129 ? -20.159 0.498   -20.079 1.00 27.46  ? 138 PRO   B N   1 
ATOM   1358 C CA  . PRO   B 2 129 ? -20.457 -0.920  -20.015 1.00 27.24  ? 138 PRO   B CA  1 
ATOM   1359 C C   . PRO   B 2 129 ? -19.741 -1.724  -21.103 1.00 32.13  ? 138 PRO   B C   1 
ATOM   1360 O O   . PRO   B 2 129 ? -19.603 -1.248  -22.220 1.00 31.17  ? 138 PRO   B O   1 
ATOM   1361 C CB  . PRO   B 2 129 ? -21.979 -0.990  -20.236 1.00 30.97  ? 138 PRO   B CB  1 
ATOM   1362 C CG  . PRO   B 2 129 ? -22.299 0.245   -21.060 1.00 27.43  ? 138 PRO   B CG  1 
ATOM   1363 C CD  . PRO   B 2 129 ? -21.268 1.279   -20.644 1.00 27.55  ? 138 PRO   B CD  1 
ATOM   1364 N N   . ILE   B 2 130 ? -19.355 -2.945  -20.741 1.00 33.19  ? 139 ILE   B N   1 
ATOM   1365 C CA  . ILE   B 2 130 ? -18.894 -4.028  -21.654 1.00 33.34  ? 139 ILE   B CA  1 
ATOM   1366 C C   . ILE   B 2 130 ? -20.091 -4.970  -21.832 1.00 30.45  ? 139 ILE   B C   1 
ATOM   1367 O O   . ILE   B 2 130 ? -20.727 -5.285  -20.821 1.00 28.74  ? 139 ILE   B O   1 
ATOM   1368 C CB  . ILE   B 2 130 ? -17.657 -4.728  -21.052 1.00 34.54  ? 139 ILE   B CB  1 
ATOM   1369 C CG1 . ILE   B 2 130 ? -16.513 -3.755  -20.771 1.00 37.47  ? 139 ILE   B CG1 1 
ATOM   1370 C CG2 . ILE   B 2 130 ? -17.191 -5.884  -21.931 1.00 36.27  ? 139 ILE   B CG2 1 
ATOM   1371 C CD1 . ILE   B 2 130 ? -15.499 -4.306  -19.794 1.00 39.30  ? 139 ILE   B CD1 1 
ATOM   1372 N N   . LEU   B 2 131 ? -20.405 -5.360  -23.072 1.00 34.37  ? 140 LEU   B N   1 
ATOM   1373 C CA  . LEU   B 2 131 ? -21.611 -6.156  -23.433 1.00 40.46  ? 140 LEU   B CA  1 
ATOM   1374 C C   . LEU   B 2 131 ? -21.244 -7.503  -24.039 1.00 36.65  ? 140 LEU   B C   1 
ATOM   1375 O O   . LEU   B 2 131 ? -20.251 -7.567  -24.792 1.00 39.44  ? 140 LEU   B O   1 
ATOM   1376 C CB  . LEU   B 2 131 ? -22.428 -5.414  -24.500 1.00 48.91  ? 140 LEU   B CB  1 
ATOM   1377 C CG  . LEU   B 2 131 ? -22.760 -3.961  -24.209 1.00 52.22  ? 140 LEU   B CG  1 
ATOM   1378 C CD1 . LEU   B 2 131 ? -23.618 -3.379  -25.336 1.00 52.95  ? 140 LEU   B CD1 1 
ATOM   1379 C CD2 . LEU   B 2 131 ? -23.457 -3.870  -22.857 1.00 51.82  ? 140 LEU   B CD2 1 
ATOM   1380 N N   . ASP   B 2 132 ? -22.120 -8.472  -23.823 1.00 38.20  ? 141 ASP   B N   1 
ATOM   1381 C CA  . ASP   B 2 132 ? -22.130 -9.773  -24.532 1.00 44.19  ? 141 ASP   B CA  1 
ATOM   1382 C C   . ASP   B 2 132 ? -23.026 -9.646  -25.768 1.00 50.60  ? 141 ASP   B C   1 
ATOM   1383 O O   . ASP   B 2 132 ? -23.573 -8.540  -25.998 1.00 52.15  ? 141 ASP   B O   1 
ATOM   1384 C CB  . ASP   B 2 132 ? -22.575 -10.906 -23.601 1.00 41.96  ? 141 ASP   B CB  1 
ATOM   1385 C CG  . ASP   B 2 132 ? -24.049 -10.937 -23.276 1.00 42.60  ? 141 ASP   B CG  1 
ATOM   1386 O OD1 . ASP   B 2 132 ? -24.801 -10.154 -23.852 1.00 39.99  ? 141 ASP   B OD1 1 
ATOM   1387 O OD2 . ASP   B 2 132 ? -24.416 -11.735 -22.424 1.00 47.51  ? 141 ASP   B OD2 1 
ATOM   1388 N N   . LYS   B 2 133 ? -23.209 -10.752 -26.498 1.00 58.02  ? 142 LYS   B N   1 
ATOM   1389 C CA  . LYS   B 2 133 ? -23.825 -10.765 -27.854 1.00 63.06  ? 142 LYS   B CA  1 
ATOM   1390 C C   . LYS   B 2 133 ? -25.324 -10.518 -27.712 1.00 57.93  ? 142 LYS   B C   1 
ATOM   1391 O O   . LYS   B 2 133 ? -25.936 -10.107 -28.699 1.00 58.94  ? 142 LYS   B O   1 
ATOM   1392 C CB  . LYS   B 2 133 ? -23.532 -12.077 -28.597 1.00 66.18  ? 142 LYS   B CB  1 
ATOM   1393 C CG  . LYS   B 2 133 ? -22.175 -12.113 -29.292 1.00 73.47  ? 142 LYS   B CG  1 
ATOM   1394 C CD  . LYS   B 2 133 ? -21.534 -13.488 -29.403 1.00 74.48  ? 142 LYS   B CD  1 
ATOM   1395 C CE  . LYS   B 2 133 ? -20.089 -13.396 -29.849 1.00 79.46  ? 142 LYS   B CE  1 
ATOM   1396 N NZ  . LYS   B 2 133 ? -19.560 -14.691 -30.343 1.00 81.43  ? 142 LYS   B NZ  1 
ATOM   1397 N N   . CYS   B 2 134 ? -25.873 -10.731 -26.518 1.00 53.54  ? 143 CYS   B N   1 
ATOM   1398 C CA  . CYS   B 2 134 ? -27.305 -10.494 -26.224 1.00 52.11  ? 143 CYS   B CA  1 
ATOM   1399 C C   . CYS   B 2 134 ? -27.530 -9.110  -25.616 1.00 44.61  ? 143 CYS   B C   1 
ATOM   1400 O O   . CYS   B 2 134 ? -28.632 -8.869  -25.149 1.00 48.62  ? 143 CYS   B O   1 
ATOM   1401 C CB  . CYS   B 2 134 ? -27.821 -11.578 -25.303 1.00 55.80  ? 143 CYS   B CB  1 
ATOM   1402 S SG  . CYS   B 2 134 ? -27.552 -13.209 -26.026 1.00 64.15  ? 143 CYS   B SG  1 
ATOM   1403 N N   . GLY   B 2 135 ? -26.540 -8.222  -25.668 1.00 43.81  ? 144 GLY   B N   1 
ATOM   1404 C CA  . GLY   B 2 135 ? -26.648 -6.851  -25.136 1.00 46.76  ? 144 GLY   B CA  1 
ATOM   1405 C C   . GLY   B 2 135 ? -26.720 -6.794  -23.610 1.00 44.28  ? 144 GLY   B C   1 
ATOM   1406 O O   . GLY   B 2 135 ? -27.055 -5.721  -23.091 1.00 43.13  ? 144 GLY   B O   1 
ATOM   1407 N N   . ARG   B 2 136 ? -26.375 -7.873  -22.902 1.00 44.94  ? 145 ARG   B N   1 
ATOM   1408 C CA  . ARG   B 2 136 ? -26.309 -7.885  -21.416 1.00 42.67  ? 145 ARG   B CA  1 
ATOM   1409 C C   . ARG   B 2 136 ? -24.984 -7.277  -20.960 1.00 40.84  ? 145 ARG   B C   1 
ATOM   1410 O O   . ARG   B 2 136 ? -23.933 -7.511  -21.618 1.00 38.34  ? 145 ARG   B O   1 
ATOM   1411 C CB  . ARG   B 2 136 ? -26.535 -9.289  -20.880 1.00 45.94  ? 145 ARG   B CB  1 
ATOM   1412 C CG  . ARG   B 2 136 ? -28.004 -9.673  -20.865 1.00 47.98  ? 145 ARG   B CG  1 
ATOM   1413 C CD  . ARG   B 2 136 ? -28.190 -11.128 -20.539 1.00 51.69  ? 145 ARG   B CD  1 
ATOM   1414 N NE  . ARG   B 2 136 ? -27.382 -11.891 -21.481 1.00 61.74  ? 145 ARG   B NE  1 
ATOM   1415 C CZ  . ARG   B 2 136 ? -26.827 -13.082 -21.264 1.00 66.94  ? 145 ARG   B CZ  1 
ATOM   1416 N NH1 . ARG   B 2 136 ? -26.966 -13.714 -20.104 1.00 71.02  ? 145 ARG   B NH1 1 
ATOM   1417 N NH2 . ARG   B 2 136 ? -26.111 -13.636 -22.228 1.00 72.15  ? 145 ARG   B NH2 1 
ATOM   1418 N N   . VAL   B 2 137 ? -25.038 -6.481  -19.890 1.00 35.44  ? 146 VAL   B N   1 
ATOM   1419 C CA  . VAL   B 2 137 ? -23.846 -5.794  -19.330 1.00 36.65  ? 146 VAL   B CA  1 
ATOM   1420 C C   . VAL   B 2 137 ? -23.107 -6.852  -18.505 1.00 38.30  ? 146 VAL   B C   1 
ATOM   1421 O O   . VAL   B 2 137 ? -23.712 -7.379  -17.546 1.00 39.81  ? 146 VAL   B O   1 
ATOM   1422 C CB  . VAL   B 2 137 ? -24.211 -4.533  -18.523 1.00 37.96  ? 146 VAL   B CB  1 
ATOM   1423 C CG1 . VAL   B 2 137 ? -22.977 -3.756  -18.102 1.00 39.86  ? 146 VAL   B CG1 1 
ATOM   1424 C CG2 . VAL   B 2 137 ? -25.159 -3.624  -19.301 1.00 41.03  ? 146 VAL   B CG2 1 
ATOM   1425 N N   . ILE   B 2 138 ? -21.879 -7.179  -18.912 1.00 36.28  ? 147 ILE   B N   1 
ATOM   1426 C CA  . ILE   B 2 138 ? -21.021 -8.204  -18.242 1.00 35.45  ? 147 ILE   B CA  1 
ATOM   1427 C C   . ILE   B 2 138 ? -20.027 -7.490  -17.319 1.00 31.98  ? 147 ILE   B C   1 
ATOM   1428 O O   . ILE   B 2 138 ? -19.238 -8.183  -16.656 1.00 34.05  ? 147 ILE   B O   1 
ATOM   1429 C CB  . ILE   B 2 138 ? -20.321 -9.130  -19.269 1.00 32.43  ? 147 ILE   B CB  1 
ATOM   1430 C CG1 . ILE   B 2 138 ? -19.522 -8.346  -20.309 1.00 33.22  ? 147 ILE   B CG1 1 
ATOM   1431 C CG2 . ILE   B 2 138 ? -21.314 -10.078 -19.919 1.00 32.57  ? 147 ILE   B CG2 1 
ATOM   1432 C CD1 . ILE   B 2 138 ? -18.451 -9.157  -20.996 1.00 36.26  ? 147 ILE   B CD1 1 
ATOM   1433 N N   . GLY   B 2 139 ? -20.068 -6.156  -17.257 1.00 31.42  ? 148 GLY   B N   1 
ATOM   1434 C CA  . GLY   B 2 139 ? -19.259 -5.387  -16.294 1.00 32.84  ? 148 GLY   B CA  1 
ATOM   1435 C C   . GLY   B 2 139 ? -18.839 -4.064  -16.862 1.00 29.67  ? 148 GLY   B C   1 
ATOM   1436 O O   . GLY   B 2 139 ? -19.267 -3.752  -17.969 1.00 33.29  ? 148 GLY   B O   1 
ATOM   1437 N N   . LEU   B 2 140 ? -18.027 -3.323  -16.133 1.00 29.58  ? 149 LEU   B N   1 
ATOM   1438 C CA  . LEU   B 2 140 ? -17.702 -1.923  -16.460 1.00 32.03  ? 149 LEU   B CA  1 
ATOM   1439 C C   . LEU   B 2 140 ? -16.199 -1.780  -16.696 1.00 30.85  ? 149 LEU   B C   1 
ATOM   1440 O O   . LEU   B 2 140 ? -15.355 -2.503  -16.080 1.00 31.05  ? 149 LEU   B O   1 
ATOM   1441 C CB  . LEU   B 2 140 ? -18.173 -0.981  -15.339 1.00 28.82  ? 149 LEU   B CB  1 
ATOM   1442 C CG  . LEU   B 2 140 ? -19.613 -1.126  -14.844 1.00 30.53  ? 149 LEU   B CG  1 
ATOM   1443 C CD1 . LEU   B 2 140 ? -19.952 0.028   -13.895 1.00 33.66  ? 149 LEU   B CD1 1 
ATOM   1444 C CD2 . LEU   B 2 140 ? -20.618 -1.230  -15.976 1.00 31.29  ? 149 LEU   B CD2 1 
ATOM   1445 N N   . TYR   B 2 141 ? -15.892 -0.783  -17.508 1.00 30.90  ? 150 TYR   B N   1 
ATOM   1446 C CA  . TYR   B 2 141 ? -14.552 -0.446  -18.011 1.00 30.06  ? 150 TYR   B CA  1 
ATOM   1447 C C   . TYR   B 2 141 ? -14.023 0.710   -17.191 1.00 30.38  ? 150 TYR   B C   1 
ATOM   1448 O O   . TYR   B 2 141 ? -14.779 1.656   -16.998 1.00 35.89  ? 150 TYR   B O   1 
ATOM   1449 C CB  . TYR   B 2 141 ? -14.706 -0.073  -19.490 1.00 36.42  ? 150 TYR   B CB  1 
ATOM   1450 C CG  . TYR   B 2 141 ? -13.494 0.510   -20.168 1.00 36.86  ? 150 TYR   B CG  1 
ATOM   1451 C CD1 . TYR   B 2 141 ? -13.374 1.872   -20.331 1.00 38.30  ? 150 TYR   B CD1 1 
ATOM   1452 C CD2 . TYR   B 2 141 ? -12.482 -0.302  -20.668 1.00 40.76  ? 150 TYR   B CD2 1 
ATOM   1453 C CE1 . TYR   B 2 141 ? -12.275 2.425   -20.968 1.00 44.10  ? 150 TYR   B CE1 1 
ATOM   1454 C CE2 . TYR   B 2 141 ? -11.381 0.230   -21.324 1.00 40.09  ? 150 TYR   B CE2 1 
ATOM   1455 C CZ  . TYR   B 2 141 ? -11.287 1.603   -21.488 1.00 46.86  ? 150 TYR   B CZ  1 
ATOM   1456 O OH  . TYR   B 2 141 ? -10.220 2.193   -22.111 1.00 51.02  ? 150 TYR   B OH  1 
ATOM   1457 N N   . GLY   B 2 142 ? -12.777 0.662   -16.741 1.00 34.21  ? 151 GLY   B N   1 
ATOM   1458 C CA  . GLY   B 2 142 ? -12.132 1.842   -16.122 1.00 35.21  ? 151 GLY   B CA  1 
ATOM   1459 C C   . GLY   B 2 142 ? -11.236 1.517   -14.945 1.00 34.10  ? 151 GLY   B C   1 
ATOM   1460 O O   . GLY   B 2 142 ? -10.499 2.443   -14.505 1.00 32.29  ? 151 GLY   B O   1 
ATOM   1461 N N   . ASN   B 2 143 ? -11.208 0.260   -14.477 1.00 34.54  ? 152 ASN   B N   1 
ATOM   1462 C CA  . ASN   B 2 143 ? -10.222 -0.134  -13.432 1.00 34.10  ? 152 ASN   B CA  1 
ATOM   1463 C C   . ASN   B 2 143 ? -9.304  -1.240  -13.949 1.00 31.58  ? 152 ASN   B C   1 
ATOM   1464 O O   . ASN   B 2 143 ? -9.762  -2.358  -14.192 1.00 30.99  ? 152 ASN   B O   1 
ATOM   1465 C CB  . ASN   B 2 143 ? -10.870 -0.589  -12.124 1.00 31.42  ? 152 ASN   B CB  1 
ATOM   1466 C CG  . ASN   B 2 143 ? -9.926  -0.551  -10.936 1.00 35.96  ? 152 ASN   B CG  1 
ATOM   1467 O OD1 . ASN   B 2 143 ? -8.975  0.249   -10.871 1.00 31.25  ? 152 ASN   B OD1 1 
ATOM   1468 N ND2 . ASN   B 2 143 ? -10.203 -1.417  -9.968  1.00 34.76  ? 152 ASN   B ND2 1 
ATOM   1469 N N   . GLY   B 2 144 ? -8.024  -0.938  -14.042 1.00 32.95  ? 153 GLY   B N   1 
ATOM   1470 C CA  . GLY   B 2 144 ? -7.068  -1.887  -14.615 1.00 36.60  ? 153 GLY   B CA  1 
ATOM   1471 C C   . GLY   B 2 144 ? -5.663  -1.443  -14.344 1.00 38.79  ? 153 GLY   B C   1 
ATOM   1472 O O   . GLY   B 2 144 ? -5.404  -0.867  -13.274 1.00 38.68  ? 153 GLY   B O   1 
ATOM   1473 N N   A VAL   B 2 145 ? -4.765  -1.669  -15.306 0.13 39.70  ? 154 VAL   B N   1 
ATOM   1474 N N   B VAL   B 2 145 ? -4.765  -1.669  -15.306 0.19 39.73  ? 154 VAL   B N   1 
ATOM   1475 N N   C VAL   B 2 145 ? -4.765  -1.670  -15.305 0.35 39.81  ? 154 VAL   B N   1 
ATOM   1476 N N   D VAL   B 2 145 ? -4.781  -1.673  -15.319 0.33 39.77  ? 154 VAL   B N   1 
ATOM   1477 C CA  A VAL   B 2 145 ? -3.292  -1.561  -15.098 0.13 40.29  ? 154 VAL   B CA  1 
ATOM   1478 C CA  B VAL   B 2 145 ? -3.292  -1.561  -15.098 0.19 40.24  ? 154 VAL   B CA  1 
ATOM   1479 C CA  C VAL   B 2 145 ? -3.292  -1.560  -15.097 0.35 40.07  ? 154 VAL   B CA  1 
ATOM   1480 C CA  D VAL   B 2 145 ? -3.299  -1.612  -15.171 0.33 40.16  ? 154 VAL   B CA  1 
ATOM   1481 C C   A VAL   B 2 145 ? -2.623  -0.955  -16.341 0.13 42.78  ? 154 VAL   B C   1 
ATOM   1482 C C   B VAL   B 2 145 ? -2.623  -0.955  -16.342 0.19 42.88  ? 154 VAL   B C   1 
ATOM   1483 C C   C VAL   B 2 145 ? -2.624  -0.954  -16.343 0.35 43.20  ? 154 VAL   B C   1 
ATOM   1484 C C   D VAL   B 2 145 ? -2.697  -0.831  -16.350 0.33 43.14  ? 154 VAL   B C   1 
ATOM   1485 O O   A VAL   B 2 145 ? -3.124  -1.181  -17.467 0.13 41.58  ? 154 VAL   B O   1 
ATOM   1486 O O   B VAL   B 2 145 ? -3.124  -1.182  -17.468 0.19 41.49  ? 154 VAL   B O   1 
ATOM   1487 O O   C VAL   B 2 145 ? -3.124  -1.182  -17.472 0.35 41.20  ? 154 VAL   B O   1 
ATOM   1488 O O   D VAL   B 2 145 ? -3.324  -0.805  -17.437 0.33 41.59  ? 154 VAL   B O   1 
ATOM   1489 C CB  A VAL   B 2 145 ? -2.718  -2.945  -14.731 0.13 39.61  ? 154 VAL   B CB  1 
ATOM   1490 C CB  B VAL   B 2 145 ? -2.719  -2.945  -14.731 0.19 39.57  ? 154 VAL   B CB  1 
ATOM   1491 C CB  C VAL   B 2 145 ? -2.721  -2.946  -14.732 0.35 39.47  ? 154 VAL   B CB  1 
ATOM   1492 C CB  D VAL   B 2 145 ? -2.736  -3.045  -15.088 0.33 39.22  ? 154 VAL   B CB  1 
ATOM   1493 C CG1 A VAL   B 2 145 ? -2.551  -3.850  -15.946 0.13 37.90  ? 154 VAL   B CG1 1 
ATOM   1494 C CG1 B VAL   B 2 145 ? -2.552  -3.850  -15.946 0.19 37.60  ? 154 VAL   B CG1 1 
ATOM   1495 C CG1 C VAL   B 2 145 ? -2.555  -3.852  -15.947 0.35 36.72  ? 154 VAL   B CG1 1 
ATOM   1496 C CG1 D VAL   B 2 145 ? -1.261  -3.103  -15.425 0.33 40.03  ? 154 VAL   B CG1 1 
ATOM   1497 C CG2 A VAL   B 2 145 ? -1.419  -2.824  -13.954 0.13 39.81  ? 154 VAL   B CG2 1 
ATOM   1498 C CG2 B VAL   B 2 145 ? -1.421  -2.823  -13.954 0.19 39.82  ? 154 VAL   B CG2 1 
ATOM   1499 C CG2 C VAL   B 2 145 ? -1.426  -2.822  -13.952 0.35 39.86  ? 154 VAL   B CG2 1 
ATOM   1500 C CG2 D VAL   B 2 145 ? -2.998  -3.682  -13.731 0.33 36.40  ? 154 VAL   B CG2 1 
ATOM   1501 N N   . VAL   B 2 146 ? -1.533  -0.210  -16.124 1.00 44.28  ? 155 VAL   B N   1 
ATOM   1502 C CA  . VAL   B 2 146 ? -0.670  0.366   -17.200 1.00 48.90  ? 155 VAL   B CA  1 
ATOM   1503 C C   . VAL   B 2 146 ? 0.399   -0.683  -17.538 1.00 52.37  ? 155 VAL   B C   1 
ATOM   1504 O O   . VAL   B 2 146 ? 0.909   -1.328  -16.598 1.00 48.74  ? 155 VAL   B O   1 
ATOM   1505 C CB  . VAL   B 2 146 ? -0.069  1.706   -16.738 1.00 52.12  ? 155 VAL   B CB  1 
ATOM   1506 C CG1 . VAL   B 2 146 ? 0.953   2.247   -17.717 1.00 54.46  ? 155 VAL   B CG1 1 
ATOM   1507 C CG2 . VAL   B 2 146 ? -1.166  2.736   -16.490 1.00 53.69  ? 155 VAL   B CG2 1 
ATOM   1508 N N   . ILE   B 2 147 ? 0.688   -0.903  -18.825 1.00 54.30  ? 156 ILE   B N   1 
ATOM   1509 C CA  . ILE   B 2 147 ? 1.540   -2.046  -19.280 1.00 51.19  ? 156 ILE   B CA  1 
ATOM   1510 C C   . ILE   B 2 147 ? 2.832   -1.480  -19.871 1.00 56.50  ? 156 ILE   B C   1 
ATOM   1511 O O   . ILE   B 2 147 ? 2.964   -0.249  -19.867 1.00 56.78  ? 156 ILE   B O   1 
ATOM   1512 C CB  . ILE   B 2 147 ? 0.772   -2.983  -20.235 1.00 55.14  ? 156 ILE   B CB  1 
ATOM   1513 C CG1 . ILE   B 2 147 ? 0.161   -2.260  -21.444 1.00 58.63  ? 156 ILE   B CG1 1 
ATOM   1514 C CG2 . ILE   B 2 147 ? -0.282  -3.759  -19.459 1.00 54.61  ? 156 ILE   B CG2 1 
ATOM   1515 C CD1 . ILE   B 2 147 ? -0.310  -3.196  -22.539 1.00 52.99  ? 156 ILE   B CD1 1 
ATOM   1516 N N   . LYS   B 2 148 ? 3.770   -2.345  -20.274 1.00 65.26  ? 157 LYS   B N   1 
ATOM   1517 C CA  . LYS   B 2 148 ? 5.140   -1.960  -20.722 1.00 72.83  ? 157 LYS   B CA  1 
ATOM   1518 C C   . LYS   B 2 148 ? 5.045   -0.846  -21.774 1.00 78.98  ? 157 LYS   B C   1 
ATOM   1519 O O   . LYS   B 2 148 ? 5.780   0.159   -21.631 1.00 80.51  ? 157 LYS   B O   1 
ATOM   1520 C CB  . LYS   B 2 148 ? 5.896   -3.180  -21.256 1.00 79.63  ? 157 LYS   B CB  1 
ATOM   1521 C CG  . LYS   B 2 148 ? 6.139   -4.284  -20.231 1.00 85.92  ? 157 LYS   B CG  1 
ATOM   1522 C CD  . LYS   B 2 148 ? 6.501   -5.623  -20.840 1.00 91.61  ? 157 LYS   B CD  1 
ATOM   1523 C CE  . LYS   B 2 148 ? 7.899   -5.660  -21.424 1.00 97.24  ? 157 LYS   B CE  1 
ATOM   1524 N NZ  . LYS   B 2 148 ? 8.935   -5.823  -20.376 1.00 101.63 ? 157 LYS   B NZ  1 
ATOM   1525 N N   . ASN   B 2 149 ? 4.134   -0.998  -22.746 1.00 74.97  ? 158 ASN   B N   1 
ATOM   1526 C CA  . ASN   B 2 149 ? 3.885   -0.047  -23.870 1.00 78.03  ? 158 ASN   B CA  1 
ATOM   1527 C C   . ASN   B 2 149 ? 3.726   1.379   -23.327 1.00 80.17  ? 158 ASN   B C   1 
ATOM   1528 O O   . ASN   B 2 149 ? 4.299   2.304   -23.926 1.00 87.98  ? 158 ASN   B O   1 
ATOM   1529 C CB  . ASN   B 2 149 ? 2.644   -0.410  -24.702 1.00 78.38  ? 158 ASN   B CB  1 
ATOM   1530 C CG  . ASN   B 2 149 ? 2.417   -1.900  -24.885 1.00 78.42  ? 158 ASN   B CG  1 
ATOM   1531 O OD1 . ASN   B 2 149 ? 3.096   -2.728  -24.282 1.00 73.49  ? 158 ASN   B OD1 1 
ATOM   1532 N ND2 . ASN   B 2 149 ? 1.445   -2.260  -25.707 1.00 84.45  ? 158 ASN   B ND2 1 
ATOM   1533 N N   . GLY   B 2 150 ? 3.002   1.526   -22.212 1.00 81.37  ? 159 GLY   B N   1 
ATOM   1534 C CA  . GLY   B 2 150 ? 2.449   2.798   -21.701 1.00 66.46  ? 159 GLY   B CA  1 
ATOM   1535 C C   . GLY   B 2 150 ? 0.923   2.827   -21.773 1.00 60.55  ? 159 GLY   B C   1 
ATOM   1536 O O   . GLY   B 2 150 ? 0.307   3.731   -21.174 1.00 55.69  ? 159 GLY   B O   1 
ATOM   1537 N N   A SER   B 2 151 ? 0.339   1.851   -22.478 0.13 59.66  ? 160 SER   B N   1 
ATOM   1538 N N   B SER   B 2 151 ? 0.331   1.856   -22.479 0.19 60.11  ? 160 SER   B N   1 
ATOM   1539 N N   C SER   B 2 151 ? 0.334   1.854   -22.481 0.35 60.68  ? 160 SER   B N   1 
ATOM   1540 N N   D SER   B 2 151 ? 0.326   1.857   -22.480 0.33 60.82  ? 160 SER   B N   1 
ATOM   1541 C CA  A SER   B 2 151 ? -1.119  1.704   -22.729 0.13 57.20  ? 160 SER   B CA  1 
ATOM   1542 C CA  B SER   B 2 151 ? -1.130  1.730   -22.728 0.19 57.50  ? 160 SER   B CA  1 
ATOM   1543 C CA  C SER   B 2 151 ? -1.127  1.703   -22.726 0.35 57.29  ? 160 SER   B CA  1 
ATOM   1544 C CA  D SER   B 2 151 ? -1.138  1.730   -22.725 0.33 57.59  ? 160 SER   B CA  1 
ATOM   1545 C C   A SER   B 2 151 ? -1.846  1.300   -21.441 0.13 55.84  ? 160 SER   B C   1 
ATOM   1546 C C   B SER   B 2 151 ? -1.838  1.155   -21.495 0.19 56.80  ? 160 SER   B C   1 
ATOM   1547 C C   C SER   B 2 151 ? -1.849  1.305   -21.427 0.35 56.49  ? 160 SER   B C   1 
ATOM   1548 C C   D SER   B 2 151 ? -1.844  1.159   -21.484 0.33 57.44  ? 160 SER   B C   1 
ATOM   1549 O O   A SER   B 2 151 ? -1.175  1.126   -20.398 0.13 54.07  ? 160 SER   B O   1 
ATOM   1550 O O   B SER   B 2 151 ? -1.145  0.698   -20.557 0.19 56.40  ? 160 SER   B O   1 
ATOM   1551 O O   C SER   B 2 151 ? -1.157  1.114   -20.399 0.35 53.42  ? 160 SER   B O   1 
ATOM   1552 O O   D SER   B 2 151 ? -1.138  0.688   -20.561 0.33 56.65  ? 160 SER   B O   1 
ATOM   1553 C CB  A SER   B 2 151 ? -1.368  0.701   -23.828 0.13 56.88  ? 160 SER   B CB  1 
ATOM   1554 C CB  B SER   B 2 151 ? -1.392  0.880   -23.941 0.19 56.78  ? 160 SER   B CB  1 
ATOM   1555 C CB  C SER   B 2 151 ? -1.372  0.697   -23.820 0.35 56.49  ? 160 SER   B CB  1 
ATOM   1556 C CB  D SER   B 2 151 ? -1.399  0.877   -23.935 0.33 56.49  ? 160 SER   B CB  1 
ATOM   1557 O OG  A SER   B 2 151 ? -2.730  0.712   -24.227 0.13 57.79  ? 160 SER   B OG  1 
ATOM   1558 O OG  B SER   B 2 151 ? -0.874  -0.427  -23.754 0.19 56.94  ? 160 SER   B OG  1 
ATOM   1559 O OG  C SER   B 2 151 ? -2.729  0.713   -24.229 0.35 58.15  ? 160 SER   B OG  1 
ATOM   1560 O OG  D SER   B 2 151 ? -0.872  -0.427  -23.746 0.33 56.78  ? 160 SER   B OG  1 
ATOM   1561 N N   A TYR   B 2 152 ? -3.168  1.135   -21.543 0.13 53.53  ? 161 TYR   B N   1 
ATOM   1562 N N   B TYR   B 2 152 ? -3.172  1.139   -21.545 0.19 53.99  ? 161 TYR   B N   1 
ATOM   1563 N N   C TYR   B 2 152 ? -3.186  1.203   -21.463 0.35 54.36  ? 161 TYR   B N   1 
ATOM   1564 N N   D TYR   B 2 152 ? -3.186  1.208   -21.462 0.33 54.78  ? 161 TYR   B N   1 
ATOM   1565 C CA  A TYR   B 2 152 ? -4.086  0.792   -20.428 0.13 51.66  ? 161 TYR   B CA  1 
ATOM   1566 C CA  B TYR   B 2 152 ? -4.086  0.790   -20.428 0.19 51.85  ? 161 TYR   B CA  1 
ATOM   1567 C CA  C TYR   B 2 152 ? -4.054  0.792   -20.321 0.35 52.07  ? 161 TYR   B CA  1 
ATOM   1568 C CA  D TYR   B 2 152 ? -4.052  0.791   -20.321 0.33 52.22  ? 161 TYR   B CA  1 
ATOM   1569 C C   A TYR   B 2 152 ? -4.818  -0.518  -20.745 0.13 49.74  ? 161 TYR   B C   1 
ATOM   1570 C C   B TYR   B 2 152 ? -4.819  -0.519  -20.745 0.19 49.73  ? 161 TYR   B C   1 
ATOM   1571 C C   C TYR   B 2 152 ? -4.834  -0.475  -20.704 0.35 49.48  ? 161 TYR   B C   1 
ATOM   1572 C C   D TYR   B 2 152 ? -4.833  -0.475  -20.704 0.33 49.56  ? 161 TYR   B C   1 
ATOM   1573 O O   A TYR   B 2 152 ? -5.223  -0.719  -21.906 0.13 48.21  ? 161 TYR   B O   1 
ATOM   1574 O O   B TYR   B 2 152 ? -5.225  -0.721  -21.905 0.19 47.89  ? 161 TYR   B O   1 
ATOM   1575 O O   C TYR   B 2 152 ? -5.271  -0.617  -21.858 0.35 46.42  ? 161 TYR   B O   1 
ATOM   1576 O O   D TYR   B 2 152 ? -5.271  -0.616  -21.858 0.33 46.53  ? 161 TYR   B O   1 
ATOM   1577 C CB  A TYR   B 2 152 ? -5.070  1.941   -20.201 0.13 51.68  ? 161 TYR   B CB  1 
ATOM   1578 C CB  B TYR   B 2 152 ? -5.069  1.939   -20.200 0.19 51.89  ? 161 TYR   B CB  1 
ATOM   1579 C CB  C TYR   B 2 152 ? -4.986  1.935   -19.896 0.35 52.88  ? 161 TYR   B CB  1 
ATOM   1580 C CB  D TYR   B 2 152 ? -4.986  1.933   -19.895 0.33 52.92  ? 161 TYR   B CB  1 
ATOM   1581 C CG  A TYR   B 2 152 ? -6.151  1.633   -19.200 0.13 51.07  ? 161 TYR   B CG  1 
ATOM   1582 C CG  B TYR   B 2 152 ? -6.152  1.632   -19.200 0.19 51.17  ? 161 TYR   B CG  1 
ATOM   1583 C CG  C TYR   B 2 152 ? -5.457  1.908   -18.457 0.35 51.39  ? 161 TYR   B CG  1 
ATOM   1584 C CG  D TYR   B 2 152 ? -5.457  1.907   -18.457 0.33 51.41  ? 161 TYR   B CG  1 
ATOM   1585 C CD1 A TYR   B 2 152 ? -5.874  1.599   -17.843 0.13 50.44  ? 161 TYR   B CD1 1 
ATOM   1586 C CD1 B TYR   B 2 152 ? -5.875  1.600   -17.843 0.19 50.40  ? 161 TYR   B CD1 1 
ATOM   1587 C CD1 C TYR   B 2 152 ? -4.661  2.387   -17.427 0.35 50.74  ? 161 TYR   B CD1 1 
ATOM   1588 C CD1 D TYR   B 2 152 ? -4.661  2.387   -17.428 0.33 50.75  ? 161 TYR   B CD1 1 
ATOM   1589 C CD2 A TYR   B 2 152 ? -7.445  1.358   -19.610 0.13 49.94  ? 161 TYR   B CD2 1 
ATOM   1590 C CD2 B TYR   B 2 152 ? -7.445  1.356   -19.611 0.19 49.79  ? 161 TYR   B CD2 1 
ATOM   1591 C CD2 C TYR   B 2 152 ? -6.716  1.435   -18.118 0.35 50.49  ? 161 TYR   B CD2 1 
ATOM   1592 C CD2 D TYR   B 2 152 ? -6.716  1.435   -18.118 0.33 50.51  ? 161 TYR   B CD2 1 
ATOM   1593 C CE1 A TYR   B 2 152 ? -6.859  1.308   -16.915 0.13 50.70  ? 161 TYR   B CE1 1 
ATOM   1594 C CE1 B TYR   B 2 152 ? -6.860  1.309   -16.915 0.19 50.78  ? 161 TYR   B CE1 1 
ATOM   1595 C CE1 C TYR   B 2 152 ? -5.085  2.376   -16.105 0.35 48.63  ? 161 TYR   B CE1 1 
ATOM   1596 C CE1 D TYR   B 2 152 ? -5.085  2.376   -16.106 0.33 48.66  ? 161 TYR   B CE1 1 
ATOM   1597 C CE2 A TYR   B 2 152 ? -8.442  1.070   -18.695 0.13 49.69  ? 161 TYR   B CE2 1 
ATOM   1598 C CE2 B TYR   B 2 152 ? -8.443  1.069   -18.696 0.19 49.52  ? 161 TYR   B CE2 1 
ATOM   1599 C CE2 C TYR   B 2 152 ? -7.158  1.419   -16.802 0.35 49.94  ? 161 TYR   B CE2 1 
ATOM   1600 C CE2 D TYR   B 2 152 ? -7.158  1.418   -16.802 0.33 49.94  ? 161 TYR   B CE2 1 
ATOM   1601 C CZ  A TYR   B 2 152 ? -8.147  1.042   -17.342 0.13 49.95  ? 161 TYR   B CZ  1 
ATOM   1602 C CZ  B TYR   B 2 152 ? -8.147  1.041   -17.343 0.19 49.86  ? 161 TYR   B CZ  1 
ATOM   1603 C CZ  C TYR   B 2 152 ? -6.340  1.888   -15.787 0.35 48.35  ? 161 TYR   B CZ  1 
ATOM   1604 C CZ  D TYR   B 2 152 ? -6.340  1.888   -15.787 0.33 48.38  ? 161 TYR   B CZ  1 
ATOM   1605 O OH  A TYR   B 2 152 ? -9.116  0.755   -16.428 0.13 49.95  ? 161 TYR   B OH  1 
ATOM   1606 O OH  B TYR   B 2 152 ? -9.115  0.754   -16.429 0.19 49.92  ? 161 TYR   B OH  1 
ATOM   1607 O OH  C TYR   B 2 152 ? -6.773  1.880   -14.489 0.35 44.68  ? 161 TYR   B OH  1 
ATOM   1608 O OH  D TYR   B 2 152 ? -6.773  1.881   -14.489 0.33 44.77  ? 161 TYR   B OH  1 
ATOM   1609 N N   . VAL   B 2 153 ? -4.973  -1.381  -19.735 1.00 49.19  ? 162 VAL   B N   1 
ATOM   1610 C CA  . VAL   B 2 153 ? -5.780  -2.627  -19.835 1.00 45.63  ? 162 VAL   B CA  1 
ATOM   1611 C C   . VAL   B 2 153 ? -6.748  -2.588  -18.649 1.00 40.93  ? 162 VAL   B C   1 
ATOM   1612 O O   . VAL   B 2 153 ? -6.255  -2.562  -17.509 1.00 38.03  ? 162 VAL   B O   1 
ATOM   1613 C CB  . VAL   B 2 153 ? -4.883  -3.880  -19.782 1.00 40.84  ? 162 VAL   B CB  1 
ATOM   1614 C CG1 . VAL   B 2 153 ? -5.667  -5.159  -20.040 1.00 41.51  ? 162 VAL   B CG1 1 
ATOM   1615 C CG2 . VAL   B 2 153 ? -3.698  -3.764  -20.730 1.00 48.27  ? 162 VAL   B CG2 1 
ATOM   1616 N N   . SER   B 2 154 ? -8.049  -2.611  -18.912 1.00 40.63  ? 163 SER   B N   1 
ATOM   1617 C CA  . SER   B 2 154 ? -9.129  -2.553  -17.898 1.00 40.86  ? 163 SER   B CA  1 
ATOM   1618 C C   . SER   B 2 154 ? -9.597  -3.971  -17.599 1.00 36.32  ? 163 SER   B C   1 
ATOM   1619 O O   . SER   B 2 154 ? -9.863  -4.708  -18.532 1.00 34.71  ? 163 SER   B O   1 
ATOM   1620 C CB  . SER   B 2 154 ? -10.315 -1.694  -18.333 1.00 38.66  ? 163 SER   B CB  1 
ATOM   1621 O OG  . SER   B 2 154 ? -11.459 -1.926  -17.508 1.00 34.47  ? 163 SER   B OG  1 
ATOM   1622 N N   . ALA   B 2 155 ? -9.805  -4.277  -16.324 1.00 33.07  ? 164 ALA   B N   1 
ATOM   1623 C CA  . ALA   B 2 155 ? -10.610 -5.433  -15.918 1.00 30.95  ? 164 ALA   B CA  1 
ATOM   1624 C C   . ALA   B 2 155 ? -11.988 -5.224  -16.509 1.00 33.07  ? 164 ALA   B C   1 
ATOM   1625 O O   . ALA   B 2 155 ? -12.420 -4.063  -16.670 1.00 40.63  ? 164 ALA   B O   1 
ATOM   1626 C CB  . ALA   B 2 155 ? -10.686 -5.564  -14.411 1.00 33.16  ? 164 ALA   B CB  1 
ATOM   1627 N N   . ILE   B 2 156 ? -12.633 -6.325  -16.826 1.00 29.53  ? 165 ILE   B N   1 
ATOM   1628 C CA  . ILE   B 2 156 ? -14.106 -6.429  -16.891 1.00 31.46  ? 165 ILE   B CA  1 
ATOM   1629 C C   . ILE   B 2 156 ? -14.606 -6.517  -15.442 1.00 31.00  ? 165 ILE   B C   1 
ATOM   1630 O O   . ILE   B 2 156 ? -14.641 -7.632  -14.925 1.00 29.08  ? 165 ILE   B O   1 
ATOM   1631 C CB  . ILE   B 2 156 ? -14.499 -7.661  -17.723 1.00 30.88  ? 165 ILE   B CB  1 
ATOM   1632 C CG1 . ILE   B 2 156 ? -13.821 -7.642  -19.104 1.00 33.62  ? 165 ILE   B CG1 1 
ATOM   1633 C CG2 . ILE   B 2 156 ? -16.012 -7.757  -17.835 1.00 31.76  ? 165 ILE   B CG2 1 
ATOM   1634 C CD1 . ILE   B 2 156 ? -14.201 -8.803  -20.002 1.00 34.47  ? 165 ILE   B CD1 1 
ATOM   1635 N N   . THR   B 2 157 ? -14.982 -5.396  -14.808 1.00 32.44  ? 166 THR   B N   1 
ATOM   1636 C CA  . THR   B 2 157 ? -15.435 -5.381  -13.386 1.00 28.26  ? 166 THR   B CA  1 
ATOM   1637 C C   . THR   B 2 157 ? -16.943 -5.628  -13.290 1.00 29.72  ? 166 THR   B C   1 
ATOM   1638 O O   . THR   B 2 157 ? -17.740 -4.798  -13.794 1.00 28.86  ? 166 THR   B O   1 
ATOM   1639 C CB  . THR   B 2 157 ? -15.061 -4.087  -12.693 1.00 31.43  ? 166 THR   B CB  1 
ATOM   1640 O OG1 . THR   B 2 157 ? -13.662 -3.905  -12.860 1.00 30.16  ? 166 THR   B OG1 1 
ATOM   1641 C CG2 . THR   B 2 157 ? -15.449 -4.082  -11.229 1.00 30.47  ? 166 THR   B CG2 1 
ATOM   1642 N N   . GLN   B 2 158 ? -17.335 -6.712  -12.631 1.00 27.26  ? 167 GLN   B N   1 
ATOM   1643 C CA  . GLN   B 2 158 ? -18.752 -7.077  -12.440 1.00 28.62  ? 167 GLN   B CA  1 
ATOM   1644 C C   . GLN   B 2 158 ? -19.036 -7.156  -10.940 1.00 30.88  ? 167 GLN   B C   1 
ATOM   1645 O O   . GLN   B 2 158 ? -18.114 -7.496  -10.192 1.00 31.46  ? 167 GLN   B O   1 
ATOM   1646 C CB  . GLN   B 2 158 ? -19.064 -8.351  -13.201 1.00 29.18  ? 167 GLN   B CB  1 
ATOM   1647 C CG  . GLN   B 2 158 ? -20.537 -8.724  -13.175 1.00 29.54  ? 167 GLN   B CG  1 
ATOM   1648 C CD  . GLN   B 2 158 ? -21.437 -7.601  -13.658 1.00 34.71  ? 167 GLN   B CD  1 
ATOM   1649 O OE1 . GLN   B 2 158 ? -21.487 -6.512  -13.073 1.00 33.59  ? 167 GLN   B OE1 1 
ATOM   1650 N NE2 . GLN   B 2 158 ? -22.170 -7.859  -14.732 1.00 31.59  ? 167 GLN   B NE2 1 
ATOM   1651 N N   . GLY   B 2 159 ? -20.214 -6.700  -10.526 1.00 33.51  ? 168 GLY   B N   1 
ATOM   1652 C CA  . GLY   B 2 159 ? -20.676 -6.802  -9.129  1.00 36.18  ? 168 GLY   B CA  1 
ATOM   1653 C C   . GLY   B 2 159 ? -21.380 -8.120  -8.921  1.00 41.53  ? 168 GLY   B C   1 
ATOM   1654 O O   . GLY   B 2 159 ? -21.376 -8.927  -9.835  1.00 49.28  ? 168 GLY   B O   1 
ATOM   1655 N N   . LYS   B 2 160 ? -21.961 -8.325  -7.747  1.00 54.63  ? 169 LYS   B N   1 
ATOM   1656 C CA  . LYS   B 2 160 ? -22.786 -9.508  -7.391  1.00 57.26  ? 169 LYS   B CA  1 
ATOM   1657 C C   . LYS   B 2 160 ? -24.228 -9.022  -7.199  1.00 63.13  ? 169 LYS   B C   1 
ATOM   1658 O O   . LYS   B 2 160 ? -24.395 -7.947  -6.608  1.00 61.94  ? 169 LYS   B O   1 
ATOM   1659 C CB  . LYS   B 2 160 ? -22.219 -10.192 -6.138  1.00 64.51  ? 169 LYS   B CB  1 
ATOM   1660 C CG  . LYS   B 2 160 ? -23.152 -11.217 -5.499  1.00 71.50  ? 169 LYS   B CG  1 
ATOM   1661 C CD  . LYS   B 2 160 ? -22.486 -12.221 -4.574  1.00 70.85  ? 169 LYS   B CD  1 
ATOM   1662 C CE  . LYS   B 2 160 ? -23.461 -13.265 -4.072  1.00 66.24  ? 169 LYS   B CE  1 
ATOM   1663 N NZ  . LYS   B 2 160 ? -23.367 -13.417 -2.605  1.00 69.54  ? 169 LYS   B NZ  1 
ATOM   1664 N N   . ARG   B 2 161 ? -25.218 -9.762  -7.715  1.00 64.76  ? 170 ARG   B N   1 
ATOM   1665 C CA  . ARG   B 2 161 ? -26.677 -9.547  -7.483  1.00 67.63  ? 170 ARG   B CA  1 
ATOM   1666 C C   . ARG   B 2 161 ? -27.122 -10.519 -6.373  1.00 72.14  ? 170 ARG   B C   1 
ATOM   1667 O O   . ARG   B 2 161 ? -26.612 -11.659 -6.381  1.00 81.00  ? 170 ARG   B O   1 
ATOM   1668 C CB  . ARG   B 2 161 ? -27.399 -9.720  -8.829  1.00 66.52  ? 170 ARG   B CB  1 
ATOM   1669 C CG  . ARG   B 2 161 ? -28.886 -9.400  -8.827  1.00 63.52  ? 170 ARG   B CG  1 
ATOM   1670 C CD  . ARG   B 2 161 ? -29.589 -9.819  -10.106 1.00 62.63  ? 170 ARG   B CD  1 
ATOM   1671 N NE  . ARG   B 2 161 ? -31.021 -9.550  -10.015 1.00 63.56  ? 170 ARG   B NE  1 
ATOM   1672 C CZ  . ARG   B 2 161 ? -31.716 -8.690  -10.762 1.00 62.66  ? 170 ARG   B CZ  1 
ATOM   1673 N NH1 . ARG   B 2 161 ? -31.141 -7.970  -11.714 1.00 58.53  ? 170 ARG   B NH1 1 
ATOM   1674 N NH2 . ARG   B 2 161 ? -33.012 -8.552  -10.547 1.00 66.83  ? 170 ARG   B NH2 1 
ATOM   1675 N N   . GLU   B 2 162 ? -27.978 -10.091 -5.428  1.00 75.62  ? 171 GLU   B N   1 
ATOM   1676 C CA  . GLU   B 2 162 ? -28.487 -10.922 -4.291  1.00 77.19  ? 171 GLU   B CA  1 
ATOM   1677 C C   . GLU   B 2 162 ? -29.994 -11.161 -4.469  1.00 75.11  ? 171 GLU   B C   1 
ATOM   1678 O O   . GLU   B 2 162 ? -30.588 -12.157 -4.029  1.00 79.84  ? 171 GLU   B O   1 
ATOM   1679 C CB  . GLU   B 2 162 ? -28.193 -10.254 -2.940  1.00 83.83  ? 171 GLU   B CB  1 
ATOM   1680 C CG  . GLU   B 2 162 ? -26.707 -10.074 -2.625  1.00 87.69  ? 171 GLU   B CG  1 
ATOM   1681 C CD  . GLU   B 2 162 ? -26.063 -11.125 -1.727  1.00 91.62  ? 171 GLU   B CD  1 
ATOM   1682 O OE1 . GLU   B 2 162 ? -25.685 -10.779 -0.592  1.00 85.06  ? 171 GLU   B OE1 1 
ATOM   1683 O OE2 . GLU   B 2 162 ? -25.911 -12.282 -2.171  1.00 94.39  ? 171 GLU   B OE2 1 
HETATM 1684 S S   A DMS   C 3 .   ? -8.106  5.464   -18.103 0.13 76.82  ? 201 DMS   B S   1 
HETATM 1685 S S   B DMS   C 3 .   ? -8.107  5.465   -18.103 0.19 76.73  ? 201 DMS   B S   1 
HETATM 1686 O O   A DMS   C 3 .   ? -6.857  4.666   -18.352 0.13 78.07  ? 201 DMS   B O   1 
HETATM 1687 O O   B DMS   C 3 .   ? -6.858  4.668   -18.352 0.19 78.24  ? 201 DMS   B O   1 
HETATM 1688 C C1  A DMS   C 3 .   ? -8.499  5.245   -16.386 0.13 77.68  ? 201 DMS   B C1  1 
HETATM 1689 C C1  B DMS   C 3 .   ? -8.500  5.245   -16.386 0.19 77.80  ? 201 DMS   B C1  1 
HETATM 1690 C C2  A DMS   C 3 .   ? -9.441  4.510   -18.779 0.13 76.78  ? 201 DMS   B C2  1 
HETATM 1691 C C2  B DMS   C 3 .   ? -9.441  4.510   -18.779 0.19 76.69  ? 201 DMS   B C2  1 
HETATM 1692 S S   A DMS   D 3 .   ? -17.622 11.774  -0.214  0.35 565.40 ? 202 DMS   B S   1 
HETATM 1693 S S   B DMS   D 3 .   ? -17.622 11.774  -0.214  0.35 565.40 ? 202 DMS   B S   1 
HETATM 1694 O O   A DMS   D 3 .   ? -17.742 10.281  -0.085  0.35 561.50 ? 202 DMS   B O   1 
HETATM 1695 O O   B DMS   D 3 .   ? -17.742 10.281  -0.085  0.35 561.50 ? 202 DMS   B O   1 
HETATM 1696 C C1  A DMS   D 3 .   ? -19.250 12.364  -0.598  0.35 565.80 ? 202 DMS   B C1  1 
HETATM 1697 C C1  B DMS   D 3 .   ? -19.250 12.364  -0.598  0.35 565.80 ? 202 DMS   B C1  1 
HETATM 1698 C C2  A DMS   D 3 .   ? -16.881 12.081  -1.797  0.35 553.76 ? 202 DMS   B C2  1 
HETATM 1699 C C2  B DMS   D 3 .   ? -16.881 12.081  -1.797  0.35 553.76 ? 202 DMS   B C2  1 
HETATM 1700 S S   A DMS   E 3 .   ? -7.247  3.562   -13.368 0.13 92.82  ? 203 DMS   B S   1 
HETATM 1701 S S   B DMS   E 3 .   ? -7.247  3.562   -13.368 0.19 93.24  ? 203 DMS   B S   1 
HETATM 1702 O O   A DMS   E 3 .   ? -7.071  2.071   -13.413 0.13 88.63  ? 203 DMS   B O   1 
HETATM 1703 O O   B DMS   E 3 .   ? -7.071  2.071   -13.414 0.19 88.08  ? 203 DMS   B O   1 
HETATM 1704 C C1  A DMS   E 3 .   ? -8.434  3.881   -12.088 0.13 92.83  ? 203 DMS   B C1  1 
HETATM 1705 C C1  B DMS   E 3 .   ? -8.434  3.880   -12.088 0.19 93.16  ? 203 DMS   B C1  1 
HETATM 1706 C C2  A DMS   E 3 .   ? -5.817  4.206   -12.535 0.13 91.15  ? 203 DMS   B C2  1 
HETATM 1707 C C2  B DMS   E 3 .   ? -5.816  4.205   -12.534 0.19 91.11  ? 203 DMS   B C2  1 
HETATM 1708 N N1  C A1BGY F 4 .   ? -8.702  4.338   -9.044  0.35 45.07  ? 204 A1BGY B N1  1 
HETATM 1709 N N1  D A1BGY F 4 .   ? -8.702  4.337   -9.044  0.33 45.08  ? 204 A1BGY B N1  1 
HETATM 1710 N N3  C A1BGY F 4 .   ? -7.114  5.542   -17.592 0.35 51.52  ? 204 A1BGY B N3  1 
HETATM 1711 N N3  D A1BGY F 4 .   ? -7.114  5.542   -17.592 0.33 51.49  ? 204 A1BGY B N3  1 
HETATM 1712 C C4  C A1BGY F 4 .   ? -8.674  3.290   -9.871  0.35 45.93  ? 204 A1BGY B C4  1 
HETATM 1713 C C4  D A1BGY F 4 .   ? -8.673  3.290   -9.872  0.33 45.92  ? 204 A1BGY B C4  1 
HETATM 1714 C C5  C A1BGY F 4 .   ? -8.606  3.396   -11.236 0.35 46.30  ? 204 A1BGY B C5  1 
HETATM 1715 C C5  D A1BGY F 4 .   ? -8.606  3.396   -11.237 0.33 46.30  ? 204 A1BGY B C5  1 
HETATM 1716 C C6  C A1BGY F 4 .   ? -8.577  4.659   -11.809 0.35 46.18  ? 204 A1BGY B C6  1 
HETATM 1717 C C6  D A1BGY F 4 .   ? -8.577  4.659   -11.810 0.33 46.19  ? 204 A1BGY B C6  1 
HETATM 1718 C C7  C A1BGY F 4 .   ? -7.460  5.365   -13.915 0.35 49.40  ? 204 A1BGY B C7  1 
HETATM 1719 C C7  D A1BGY F 4 .   ? -7.460  5.365   -13.915 0.33 49.40  ? 204 A1BGY B C7  1 
HETATM 1720 C C8  C A1BGY F 4 .   ? -7.577  5.324   -15.381 0.35 52.46  ? 204 A1BGY B C8  1 
HETATM 1721 C C8  D A1BGY F 4 .   ? -7.577  5.324   -15.381 0.33 52.39  ? 204 A1BGY B C8  1 
HETATM 1722 C C10 C A1BGY F 4 .   ? -8.371  4.978   -17.486 0.35 49.41  ? 204 A1BGY B C10 1 
HETATM 1723 C C10 D A1BGY F 4 .   ? -8.371  4.978   -17.485 0.33 49.41  ? 204 A1BGY B C10 1 
HETATM 1724 C C13 C A1BGY F 4 .   ? -10.579 4.331   -18.639 0.35 46.64  ? 204 A1BGY B C13 1 
HETATM 1725 C C13 D A1BGY F 4 .   ? -10.579 4.331   -18.638 0.33 46.67  ? 204 A1BGY B C13 1 
HETATM 1726 C C15 C A1BGY F 4 .   ? -6.609  5.754   -16.286 0.35 52.20  ? 204 A1BGY B C15 1 
HETATM 1727 C C15 D A1BGY F 4 .   ? -6.609  5.754   -16.287 0.33 52.16  ? 204 A1BGY B C15 1 
HETATM 1728 C C1  C A1BGY F 4 .   ? -8.579  7.177   -11.514 0.35 44.59  ? 204 A1BGY B C1  1 
HETATM 1729 C C1  D A1BGY F 4 .   ? -8.579  7.177   -11.514 0.33 44.61  ? 204 A1BGY B C1  1 
HETATM 1730 C C2  C A1BGY F 4 .   ? -8.609  5.772   -10.968 0.35 43.31  ? 204 A1BGY B C2  1 
HETATM 1731 C C2  D A1BGY F 4 .   ? -8.609  5.773   -10.968 0.33 43.37  ? 204 A1BGY B C2  1 
HETATM 1732 C C3  C A1BGY F 4 .   ? -8.670  5.560   -9.599  0.35 44.21  ? 204 A1BGY B C3  1 
HETATM 1733 C C3  D A1BGY F 4 .   ? -8.670  5.560   -9.599  0.33 44.24  ? 204 A1BGY B C3  1 
HETATM 1734 N N2  C A1BGY F 4 .   ? -8.507  4.835   -13.214 0.35 49.02  ? 204 A1BGY B N2  1 
HETATM 1735 N N2  D A1BGY F 4 .   ? -8.507  4.835   -13.214 0.33 48.98  ? 204 A1BGY B N2  1 
HETATM 1736 O O1  C A1BGY F 4 .   ? -6.475  5.844   -13.364 0.35 49.87  ? 204 A1BGY B O1  1 
HETATM 1737 O O1  D A1BGY F 4 .   ? -6.474  5.844   -13.364 0.33 49.86  ? 204 A1BGY B O1  1 
HETATM 1738 C C9  C A1BGY F 4 .   ? -8.668  4.837   -16.149 0.35 50.97  ? 204 A1BGY B C9  1 
HETATM 1739 C C9  D A1BGY F 4 .   ? -8.668  4.837   -16.148 0.33 50.94  ? 204 A1BGY B C9  1 
HETATM 1740 C C11 C A1BGY F 4 .   ? -9.115  4.639   -18.704 0.35 47.30  ? 204 A1BGY B C11 1 
HETATM 1741 C C11 D A1BGY F 4 .   ? -9.115  4.639   -18.703 0.33 47.33  ? 204 A1BGY B C11 1 
HETATM 1742 C C12 C A1BGY F 4 .   ? -9.617  3.240   -18.884 0.35 45.38  ? 204 A1BGY B C12 1 
HETATM 1743 C C12 D A1BGY F 4 .   ? -9.617  3.240   -18.884 0.33 45.45  ? 204 A1BGY B C12 1 
HETATM 1744 C C14 C A1BGY F 4 .   ? -6.415  5.851   -18.839 0.35 50.72  ? 204 A1BGY B C14 1 
HETATM 1745 C C14 D A1BGY F 4 .   ? -6.415  5.851   -18.839 0.33 50.72  ? 204 A1BGY B C14 1 
HETATM 1746 C C16 C A1BGY F 4 .   ? -5.259  6.351   -16.079 0.35 53.14  ? 204 A1BGY B C16 1 
HETATM 1747 C C16 D A1BGY F 4 .   ? -5.259  6.351   -16.079 0.33 53.09  ? 204 A1BGY B C16 1 
HETATM 1748 S S   C SO4   G 5 .   ? -18.699 11.652  -0.444  0.50 98.77  ? 205 SO4   B S   1 
HETATM 1749 S S   D SO4   G 5 .   ? -18.699 11.652  -0.444  0.50 98.77  ? 205 SO4   B S   1 
HETATM 1750 O O1  C SO4   G 5 .   ? -17.622 11.992  -1.343  0.50 97.39  ? 205 SO4   B O1  1 
HETATM 1751 O O1  D SO4   G 5 .   ? -17.622 11.992  -1.343  0.50 97.39  ? 205 SO4   B O1  1 
HETATM 1752 O O2  C SO4   G 5 .   ? -18.296 11.921  0.907   0.50 100.57 ? 205 SO4   B O2  1 
HETATM 1753 O O2  D SO4   G 5 .   ? -18.296 11.921  0.907   0.50 100.57 ? 205 SO4   B O2  1 
HETATM 1754 O O3  C SO4   G 5 .   ? -19.857 12.440  -0.764  0.50 97.30  ? 205 SO4   B O3  1 
HETATM 1755 O O3  D SO4   G 5 .   ? -19.857 12.440  -0.764  0.50 97.30  ? 205 SO4   B O3  1 
HETATM 1756 O O4  C SO4   G 5 .   ? -19.025 10.254  -0.566  0.50 97.79  ? 205 SO4   B O4  1 
HETATM 1757 O O4  D SO4   G 5 .   ? -19.025 10.254  -0.566  0.50 97.79  ? 205 SO4   B O4  1 
HETATM 1758 O O   . HOH   H 6 .   ? -27.740 -5.733  -28.128 1.00 37.36  ? 101 HOH   A O   1 
HETATM 1759 O O   . HOH   H 6 .   ? -23.778 18.965  -19.434 1.00 50.25  ? 102 HOH   A O   1 
HETATM 1760 O O   . HOH   H 6 .   ? -8.004  0.390   3.344   1.00 46.03  ? 103 HOH   A O   1 
HETATM 1761 O O   . HOH   H 6 .   ? 6.446   -4.782  -17.154 1.00 64.53  ? 104 HOH   A O   1 
HETATM 1762 O O   . HOH   H 6 .   ? -6.997  -8.636  -3.289  1.00 42.99  ? 105 HOH   A O   1 
HETATM 1763 O O   . HOH   H 6 .   ? -2.320  -3.908  -6.307  1.00 42.24  ? 106 HOH   A O   1 
HETATM 1764 O O   C HOH   H 6 .   ? -25.336 12.543  -23.672 0.50 44.43  ? 107 HOH   A O   1 
HETATM 1765 O O   D HOH   H 6 .   ? -25.336 12.543  -23.672 0.50 44.43  ? 107 HOH   A O   1 
HETATM 1766 O O   . HOH   H 6 .   ? -31.318 0.519   -29.374 1.00 66.68  ? 108 HOH   A O   1 
HETATM 1767 O O   . HOH   H 6 .   ? -4.036  -14.193 -25.555 1.00 45.08  ? 109 HOH   A O   1 
HETATM 1768 O O   . HOH   H 6 .   ? -9.189  -6.081  -25.518 1.00 48.19  ? 110 HOH   A O   1 
HETATM 1769 O O   . HOH   H 6 .   ? -24.112 9.318   -27.577 1.00 36.23  ? 111 HOH   A O   1 
HETATM 1770 O O   A HOH   H 6 .   ? -26.299 -3.500  -35.248 0.50 65.46  ? 112 HOH   A O   1 
HETATM 1771 O O   B HOH   H 6 .   ? -26.299 -3.500  -35.248 0.50 65.46  ? 112 HOH   A O   1 
HETATM 1772 O O   . HOH   H 6 .   ? -3.669  -4.000  0.144   1.00 44.38  ? 113 HOH   A O   1 
HETATM 1773 O O   . HOH   H 6 .   ? -8.357  -1.762  6.700   1.00 51.56  ? 114 HOH   A O   1 
HETATM 1774 O O   . HOH   H 6 .   ? -28.992 15.826  -14.845 1.00 51.05  ? 115 HOH   A O   1 
HETATM 1775 O O   A HOH   H 6 .   ? -5.228  2.073   -9.755  0.13 19.52  ? 116 HOH   A O   1 
HETATM 1776 O O   B HOH   H 6 .   ? -5.228  2.074   -9.755  0.19 19.52  ? 116 HOH   A O   1 
HETATM 1777 O O   . HOH   H 6 .   ? -22.517 -9.276  -34.536 1.00 43.90  ? 117 HOH   A O   1 
HETATM 1778 O O   . HOH   H 6 .   ? -4.526  -10.004 -5.676  1.00 43.19  ? 118 HOH   A O   1 
HETATM 1779 O O   . HOH   H 6 .   ? -30.958 0.566   -22.899 1.00 41.59  ? 119 HOH   A O   1 
HETATM 1780 O O   . HOH   H 6 .   ? -4.029  -0.608  -0.429  1.00 51.34  ? 120 HOH   A O   1 
HETATM 1781 O O   C HOH   H 6 .   ? -5.553  5.071   -7.864  0.35 48.92  ? 121 HOH   A O   1 
HETATM 1782 O O   D HOH   H 6 .   ? -5.553  5.071   -7.864  0.33 48.93  ? 121 HOH   A O   1 
HETATM 1783 O O   A HOH   H 6 .   ? -9.629  2.486   -8.386  0.13 25.17  ? 122 HOH   A O   1 
HETATM 1784 O O   B HOH   H 6 .   ? -9.630  2.486   -8.386  0.19 25.18  ? 122 HOH   A O   1 
HETATM 1785 O O   . HOH   H 6 .   ? -2.929  -8.995  -3.546  1.00 51.50  ? 123 HOH   A O   1 
HETATM 1786 O O   A HOH   H 6 .   ? -9.363  5.310   -6.975  0.13 18.69  ? 124 HOH   A O   1 
HETATM 1787 O O   B HOH   H 6 .   ? -9.363  5.309   -6.974  0.19 18.77  ? 124 HOH   A O   1 
HETATM 1788 O O   . HOH   I 6 .   ? -33.976 1.560   -15.416 1.00 40.20  ? 301 HOH   B O   1 
HETATM 1789 O O   . HOH   I 6 .   ? -16.526 25.756  -12.382 1.00 56.16  ? 302 HOH   B O   1 
HETATM 1790 O O   . HOH   I 6 .   ? -15.783 -9.514  -15.105 1.00 42.79  ? 303 HOH   B O   1 
HETATM 1791 O O   . HOH   I 6 .   ? -30.578 12.960  -19.570 1.00 39.90  ? 304 HOH   B O   1 
HETATM 1792 O O   . HOH   I 6 .   ? -19.364 -12.046 -25.799 1.00 44.75  ? 305 HOH   B O   1 
HETATM 1793 O O   A HOH   I 6 .   ? -6.817  -0.669  -11.439 0.13 19.88  ? 306 HOH   B O   1 
HETATM 1794 O O   B HOH   I 6 .   ? -6.818  -0.671  -11.440 0.19 19.89  ? 306 HOH   B O   1 
HETATM 1795 O O   . HOH   I 6 .   ? -17.288 12.853  -5.485  1.00 50.41  ? 307 HOH   B O   1 
HETATM 1796 O O   . HOH   I 6 .   ? -25.870 -7.930  -16.701 1.00 40.65  ? 308 HOH   B O   1 
HETATM 1797 O O   . HOH   I 6 .   ? -13.211 -2.121  -14.788 1.00 31.97  ? 309 HOH   B O   1 
HETATM 1798 O O   C HOH   I 6 .   ? -7.841  4.221   -6.656  0.35 46.65  ? 310 HOH   B O   1 
HETATM 1799 O O   D HOH   I 6 .   ? -7.841  4.221   -6.655  0.33 46.65  ? 310 HOH   B O   1 
HETATM 1800 O O   A HOH   I 6 .   ? -12.181 2.044   -5.828  0.13 17.42  ? 311 HOH   B O   1 
HETATM 1801 O O   B HOH   I 6 .   ? -12.177 2.055   -5.829  0.19 17.45  ? 311 HOH   B O   1 
HETATM 1802 O O   A HOH   I 6 .   ? -18.355 19.401  -21.746 0.50 50.58  ? 312 HOH   B O   1 
HETATM 1803 O O   B HOH   I 6 .   ? -18.355 19.401  -21.746 0.50 50.58  ? 312 HOH   B O   1 
HETATM 1804 O O   . HOH   I 6 .   ? -35.571 -5.414  -10.525 1.00 50.48  ? 313 HOH   B O   1 
HETATM 1805 O O   . HOH   I 6 .   ? -28.330 -3.566  -22.461 1.00 59.71  ? 314 HOH   B O   1 
HETATM 1806 O O   . HOH   I 6 .   ? -19.247 -5.507  -0.799  1.00 39.12  ? 315 HOH   B O   1 
HETATM 1807 O O   . HOH   I 6 .   ? -15.373 9.421   -0.682  1.00 47.21  ? 316 HOH   B O   1 
HETATM 1808 O O   C HOH   I 6 .   ? -9.526  8.422   -8.446  0.35 44.67  ? 317 HOH   B O   1 
HETATM 1809 O O   D HOH   I 6 .   ? -9.526  8.423   -8.447  0.33 44.68  ? 317 HOH   B O   1 
HETATM 1810 O O   . HOH   I 6 .   ? -31.595 7.483   -4.928  1.00 53.45  ? 318 HOH   B O   1 
HETATM 1811 O O   C HOH   I 6 .   ? -10.052 6.862   -6.424  0.35 41.81  ? 319 HOH   B O   1 
HETATM 1812 O O   D HOH   I 6 .   ? -10.052 6.861   -6.424  0.33 41.81  ? 319 HOH   B O   1 
HETATM 1813 O O   . HOH   I 6 .   ? -21.737 -12.134 -12.854 1.00 45.68  ? 320 HOH   B O   1 
HETATM 1814 O O   . HOH   I 6 .   ? -27.741 -6.952  -5.638  1.00 49.97  ? 321 HOH   B O   1 
HETATM 1815 O O   . HOH   I 6 .   ? -16.452 -14.609 -16.506 1.00 44.07  ? 322 HOH   B O   1 
HETATM 1816 O O   . HOH   I 6 .   ? -27.923 -5.959  -18.583 1.00 37.86  ? 323 HOH   B O   1 
HETATM 1817 O O   . HOH   I 6 .   ? -16.351 -7.164  -8.203  1.00 53.13  ? 324 HOH   B O   1 
HETATM 1818 O O   . HOH   I 6 .   ? -16.631 20.929  -14.363 1.00 50.93  ? 325 HOH   B O   1 
HETATM 1819 O O   C HOH   I 6 .   ? -20.176 13.673  1.685   0.50 47.01  ? 326 HOH   B O   1 
HETATM 1820 O O   D HOH   I 6 .   ? -20.176 13.673  1.685   0.50 47.01  ? 326 HOH   B O   1 
HETATM 1821 O O   . HOH   I 6 .   ? -21.797 -13.518 -21.735 1.00 44.26  ? 327 HOH   B O   1 
HETATM 1822 O O   . HOH   I 6 .   ? -23.789 -14.441 -17.981 1.00 57.79  ? 328 HOH   B O   1 
HETATM 1823 O O   . HOH   I 6 .   ? -6.837  -10.788 -5.504  1.00 46.89  ? 329 HOH   B O   1 
HETATM 1824 O O   . HOH   I 6 .   ? -12.321 -3.189  -10.147 1.00 35.68  ? 330 HOH   B O   1 
HETATM 1825 O O   . HOH   I 6 .   ? -30.625 12.498  -16.419 1.00 53.68  ? 331 HOH   B O   1 
HETATM 1826 O O   . HOH   I 6 .   ? -35.268 4.476   -9.170  1.00 53.80  ? 332 HOH   B O   1 
HETATM 1827 O O   . HOH   I 6 .   ? -17.940 -10.635 -16.530 1.00 34.19  ? 333 HOH   B O   1 
HETATM 1828 O O   . HOH   I 6 .   ? -29.875 -1.002  -19.055 1.00 48.70  ? 334 HOH   B O   1 
HETATM 1829 O O   . HOH   I 6 .   ? -15.975 -13.920 -30.926 1.00 44.72  ? 335 HOH   B O   1 
HETATM 1830 O O   A HOH   I 6 .   ? -11.477 11.928  -19.825 0.50 61.79  ? 336 HOH   B O   1 
HETATM 1831 O O   B HOH   I 6 .   ? -11.477 11.928  -19.825 0.50 61.79  ? 336 HOH   B O   1 
HETATM 1832 O O   C HOH   I 6 .   ? -6.046  0.015   -10.667 0.35 32.20  ? 337 HOH   B O   1 
HETATM 1833 O O   D HOH   I 6 .   ? -6.046  0.015   -10.668 0.33 32.19  ? 337 HOH   B O   1 
HETATM 1834 O O   . HOH   I 6 .   ? -21.553 6.342   -32.820 1.00 60.74  ? 338 HOH   B O   1 
HETATM 1835 O O   . HOH   I 6 .   ? -20.004 -7.744  -2.806  1.00 52.39  ? 339 HOH   B O   1 
HETATM 1836 O O   A HOH   I 6 .   ? -14.587 -6.129  -1.959  0.50 65.43  ? 340 HOH   B O   1 
HETATM 1837 O O   B HOH   I 6 .   ? -14.587 -6.129  -1.959  0.50 65.43  ? 340 HOH   B O   1 
HETATM 1838 O O   . HOH   I 6 .   ? -17.330 15.064  -30.691 1.00 51.45  ? 341 HOH   B O   1 
HETATM 1839 O O   . HOH   I 6 .   ? -11.746 -17.637 -28.052 1.00 51.35  ? 342 HOH   B O   1 
HETATM 1840 O O   . HOH   I 6 .   ? -15.392 16.637  -20.306 1.00 47.19  ? 343 HOH   B O   1 
HETATM 1841 O O   . HOH   I 6 .   ? -3.012  -11.703 -7.061  1.00 36.63  ? 344 HOH   B O   1 
HETATM 1842 O O   . HOH   I 6 .   ? -8.461  -10.459 -7.486  1.00 50.36  ? 345 HOH   B O   1 
HETATM 1843 O O   . HOH   I 6 .   ? -21.223 6.990   0.000   0.50 54.11  ? 346 HOH   B O   1 
HETATM 1844 O O   . HOH   I 6 .   ? -30.522 4.655   -2.463  1.00 54.08  ? 347 HOH   B O   1 
HETATM 1845 O O   . HOH   I 6 .   ? -14.515 -12.317 -16.586 1.00 38.85  ? 348 HOH   B O   1 
HETATM 1846 O O   . HOH   I 6 .   ? -18.762 15.246  -22.080 1.00 34.86  ? 349 HOH   B O   1 
HETATM 1847 O O   . HOH   I 6 .   ? -0.483  0.276   -13.359 1.00 54.27  ? 350 HOH   B O   1 
HETATM 1848 O O   . HOH   I 6 .   ? -11.593 -4.962  -8.246  1.00 46.56  ? 351 HOH   B O   1 
HETATM 1849 O O   . HOH   I 6 .   ? -7.455  -6.185  0.660   1.00 56.59  ? 352 HOH   B O   1 
HETATM 1850 O O   . HOH   I 6 .   ? -20.829 2.869   -32.573 1.00 49.96  ? 353 HOH   B O   1 
HETATM 1851 O O   . HOH   I 6 .   ? -25.869 -4.505  -3.972  1.00 42.37  ? 354 HOH   B O   1 
HETATM 1852 O O   A HOH   I 6 .   ? -20.084 24.818  -16.670 0.50 56.41  ? 355 HOH   B O   1 
HETATM 1853 O O   B HOH   I 6 .   ? -20.084 24.818  -16.670 0.50 56.41  ? 355 HOH   B O   1 
HETATM 1854 O O   . HOH   I 6 .   ? -15.187 -4.404  1.404   1.00 37.06  ? 356 HOH   B O   1 
HETATM 1855 O O   . HOH   I 6 .   ? -1.217  -13.393 -9.760  1.00 48.50  ? 357 HOH   B O   1 
HETATM 1856 O O   . HOH   I 6 .   ? -19.008 25.526  -14.512 1.00 52.54  ? 358 HOH   B O   1 
HETATM 1857 O O   A HOH   I 6 .   ? -10.883 23.509  -12.824 0.50 75.26  ? 359 HOH   B O   1 
HETATM 1858 O O   B HOH   I 6 .   ? -10.883 23.509  -12.824 0.50 75.26  ? 359 HOH   B O   1 
HETATM 1859 O O   A HOH   I 6 .   ? -10.877 7.995   -13.974 0.13 19.12  ? 360 HOH   B O   1 
HETATM 1860 O O   B HOH   I 6 .   ? -10.875 7.995   -13.976 0.19 19.14  ? 360 HOH   B O   1 
HETATM 1861 O O   . HOH   I 6 .   ? -19.619 -13.251 -23.158 1.00 42.67  ? 361 HOH   B O   1 
HETATM 1862 O O   . HOH   I 6 .   ? -30.388 -7.916  -5.110  1.00 66.73  ? 362 HOH   B O   1 
HETATM 1863 O O   C HOH   I 6 .   ? -21.641 -13.543 -25.816 0.50 53.87  ? 363 HOH   B O   1 
HETATM 1864 O O   D HOH   I 6 .   ? -21.641 -13.543 -25.816 0.50 53.87  ? 363 HOH   B O   1 
HETATM 1865 O O   . HOH   I 6 .   ? -17.213 16.849  -22.009 1.00 42.68  ? 364 HOH   B O   1 
HETATM 1866 O O   C HOH   I 6 .   ? -21.223 -6.767  -0.000  0.50 75.48  ? 365 HOH   B O   1 
HETATM 1867 O O   D HOH   I 6 .   ? -21.223 -6.767  -0.000  0.50 75.48  ? 365 HOH   B O   1 
HETATM 1868 O O   A HOH   I 6 .   ? -11.368 4.099   -5.573  0.13 8.70   ? 366 HOH   B O   1 
HETATM 1869 O O   B HOH   I 6 .   ? -11.556 5.026   -4.914  0.19 21.20  ? 366 HOH   B O   1 
HETATM 1870 O O   . HOH   I 6 .   ? -11.776 -9.223  0.204   1.00 56.07  ? 367 HOH   B O   1 
HETATM 1871 O O   . HOH   I 6 .   ? -28.609 -12.682 -28.093 1.00 58.42  ? 368 HOH   B O   1 
HETATM 1872 O O   . HOH   I 6 .   ? -23.186 -7.378  -2.278  1.00 56.54  ? 369 HOH   B O   1 
HETATM 1873 O O   . HOH   I 6 .   ? -31.568 -6.892  -7.151  1.00 72.91  ? 370 HOH   B O   1 
HETATM 1874 O O   . HOH   I 6 .   ? -29.416 -5.578  -0.739  1.00 56.52  ? 371 HOH   B O   1 
HETATM 1875 O O   . HOH   I 6 .   ? -19.064 -11.671 -13.526 1.00 51.98  ? 372 HOH   B O   1 
HETATM 1876 O O   . HOH   I 6 .   ? -12.019 13.453  -14.608 1.00 64.09  ? 373 HOH   B O   1 
HETATM 1877 O O   . HOH   I 6 .   ? -21.223 4.271   0.000   0.50 65.00  ? 374 HOH   B O   1 
# 
