data_7I21
# 
_entry.id   7I21 
# 
_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   7I21         pdb_00007i21 10.2210/pdb7i21/pdb 
WWPDB D_1001408216 ?            ?                   
# 
loop_
_pdbx_audit_revision_history.ordinal 
_pdbx_audit_revision_history.data_content_type 
_pdbx_audit_revision_history.major_revision 
_pdbx_audit_revision_history.minor_revision 
_pdbx_audit_revision_history.revision_date 
_pdbx_audit_revision_history.part_number 
1 'Structure model' 1 0 2025-03-05 ? 
2 'Structure model' 1 1 2025-05-28 ? 
# 
_pdbx_audit_revision_details.ordinal             1 
_pdbx_audit_revision_details.revision_ordinal    1 
_pdbx_audit_revision_details.data_content_type   'Structure model' 
_pdbx_audit_revision_details.provider            repository 
_pdbx_audit_revision_details.type                'Initial release' 
_pdbx_audit_revision_details.description         ? 
_pdbx_audit_revision_details.details             ? 
# 
_pdbx_audit_revision_group.ordinal             1 
_pdbx_audit_revision_group.revision_ordinal    2 
_pdbx_audit_revision_group.data_content_type   'Structure model' 
_pdbx_audit_revision_group.group               'Structure summary' 
# 
_pdbx_audit_revision_category.ordinal             1 
_pdbx_audit_revision_category.revision_ordinal    2 
_pdbx_audit_revision_category.data_content_type   'Structure model' 
_pdbx_audit_revision_category.category            pdbx_deposit_group 
# 
_pdbx_audit_revision_item.ordinal             1 
_pdbx_audit_revision_item.revision_ordinal    2 
_pdbx_audit_revision_item.data_content_type   'Structure model' 
_pdbx_audit_revision_item.item                '_pdbx_deposit_group.group_description' 
# 
_pdbx_database_status.entry_id                        7I21 
_pdbx_database_status.status_code                     REL 
_pdbx_database_status.status_code_sf                  REL 
_pdbx_database_status.status_code_mr                  ? 
_pdbx_database_status.status_code_cs                  ? 
_pdbx_database_status.recvd_initial_deposition_date   2025-02-20 
_pdbx_database_status.status_code_nmr_data            ? 
_pdbx_database_status.deposit_site                    RCSB 
_pdbx_database_status.process_site                    RCSB 
_pdbx_database_status.SG_entry                        ? 
_pdbx_database_status.pdb_format_compatible           N 
_pdbx_database_status.methods_development_category    ? 
# 
_pdbx_contact_author.id                 1 
_pdbx_contact_author.email              frankfurt.von-delft@diamond.ac.uk 
_pdbx_contact_author.name_first         Frank 
_pdbx_contact_author.name_last          'von Delft' 
_pdbx_contact_author.role               'principal investigator/group leader' 
_pdbx_contact_author.identifier_ORCID   0000-0003-0378-0017 
_pdbx_contact_author.name_mi            ? 
# 
loop_
_audit_author.name 
_audit_author.pdbx_ordinal 
'Ni, X.'              1  
'Marples, P.G.'       2  
'Godoy, A.S.'         3  
'Koekemoer, L.'       4  
'Aschenbrenner, J.C.' 5  
'Balcomb, B.H.'       6  
'Fairhead, M.'        7  
'Lithgo, R.M.'        8  
'Balaji, G.'          9  
'Phelps, J.'          10 
'Thompson, W.'        11 
'Tomlinson, C.W.E.'   12 
'Wild, C.'            13 
'Winokan, M.'         14 
'Williams, E.P.'      15 
'Chandran, A.V.'      16 
'Walsh, M.A.'         17 
'Fearon, D.'          18 
'von Delft, F.'       19 
# 
_citation.id                        primary 
_citation.title                     'PanDDA analysis group deposition' 
_citation.journal_abbrev            'To Be Published' 
_citation.journal_volume            ? 
_citation.page_first                ? 
_citation.page_last                 ? 
_citation.year                      ? 
_citation.journal_id_ASTM           ? 
_citation.country                   ? 
_citation.journal_id_ISSN           ? 
_citation.journal_id_CSD            0353 
_citation.book_publisher            ? 
_citation.pdbx_database_id_PubMed   ? 
_citation.pdbx_database_id_DOI      ? 
# 
loop_
_citation_author.citation_id 
_citation_author.name 
_citation_author.identifier_ORCID 
_citation_author.ordinal 
primary 'Ni, X.'              ? 1  
primary 'Marples, P.G.'       ? 2  
primary 'Godoy, A.S.'         ? 3  
primary 'Koekemoer, L.'       ? 4  
primary 'Aschenbrenner, J.C.' ? 5  
primary 'Balcomb, B.H.'       ? 6  
primary 'Fairhead, M.'        ? 7  
primary 'Lithgo, R.M.'        ? 8  
primary 'Balaji, G.'          ? 9  
primary 'Phelps, J.'          ? 10 
primary 'Thompson, W.'        ? 11 
primary 'Tomlinson, C.W.E.'   ? 12 
primary 'Wild, C.'            ? 13 
primary 'Winokan, M.'         ? 14 
primary 'Williams, E.P.'      ? 15 
primary 'Chandran, A.V.'      ? 16 
primary 'Walsh, M.A.'         ? 17 
primary 'Fearon, D.'          ? 18 
primary 'von Delft, F.'       ? 19 
# 
loop_
_entity.id 
_entity.type 
_entity.src_method 
_entity.pdbx_description 
_entity.formula_weight 
_entity.pdbx_number_of_molecules 
_entity.pdbx_ec 
_entity.pdbx_mutation 
_entity.pdbx_fragment 
_entity.details 
1 polymer     man 'Serine protease subunit NS2B'                                                                   5067.486  1  ? 
?    ? ? 
2 polymer     man 'Serine protease NS3'                                                                            18117.629 1  
3.4.21.91,3.6.1.15,3.6.4.13 None ? ? 
3 non-polymer syn 'DIMETHYL SULFOXIDE'                                                                             78.133    4  ? 
?    ? ? 
4 non-polymer syn '1-[(3S)-3-(aminomethyl)pyrrolidin-1-yl]-2-[4-(hydroxymethyl)-2-methylquinolin-8-yl]ethan-1-one' 313.394   1  ? 
?    ? ? 
5 non-polymer syn 'SULFATE ION'                                                                                    96.063    2  ? 
?    ? ? 
6 water       nat water                                                                                            18.015    99 ? 
?    ? ? 
# 
loop_
_entity_name_com.entity_id 
_entity_name_com.name 
1 'Flavivirin protease NS2B regulatory subunit,Non-structural protein 2B' 
2 'Flavivirin protease NS3 catalytic subunit,Non-structural protein 3'    
# 
loop_
_entity_poly.entity_id 
_entity_poly.type 
_entity_poly.nstd_linkage 
_entity_poly.nstd_monomer 
_entity_poly.pdbx_seq_one_letter_code 
_entity_poly.pdbx_seq_one_letter_code_can 
_entity_poly.pdbx_strand_id 
_entity_poly.pdbx_target_identifier 
1 'polypeptide(L)' no no SMGKSVDMYIERAGDITWEKDAEVTGNSPRLDVALDESGDFSLVEE SMGKSVDMYIERAGDITWEKDAEVTGNSPRLDVALDESGDFSLVEE A ? 
2 'polypeptide(L)' no no 
;MKEVKKGETTDGVYRVMTRRLLGSTQVGVGVMQEGVFHTMWHVTKGAALRSGEGRLDPYWGDVKQDLVSYCGPWKLDAAW
DGLSEVQLLAVPPGERAKNIQTLPGIFKTKDGDIGAVALDYPAGTSGSPILDKCGRVIGLYGNGVVIKNGSYVSAITQGK
REEETPVE
;
;MKEVKKGETTDGVYRVMTRRLLGSTQVGVGVMQEGVFHTMWHVTKGAALRSGEGRLDPYWGDVKQDLVSYCGPWKLDAAW
DGLSEVQLLAVPPGERAKNIQTLPGIFKTKDGDIGAVALDYPAGTSGSPILDKCGRVIGLYGNGVVIKNGSYVSAITQGK
REEETPVE
;
B ? 
# 
loop_
_pdbx_entity_nonpoly.entity_id 
_pdbx_entity_nonpoly.name 
_pdbx_entity_nonpoly.comp_id 
3 'DIMETHYL SULFOXIDE'                                                                             DMS   
4 '1-[(3S)-3-(aminomethyl)pyrrolidin-1-yl]-2-[4-(hydroxymethyl)-2-methylquinolin-8-yl]ethan-1-one' A1BXS 
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 
A1BXS non-polymer         . '1-[(3S)-3-(aminomethyl)pyrrolidin-1-yl]-2-[4-(hydroxymethyl)-2-methylquinolin-8-yl]ethan-1-one' ? 
'C18 H23 N3 O2'  313.394 
ALA   'L-peptide linking' y ALANINE                                                                                          ? 
'C3 H7 N O2'     89.093  
ARG   'L-peptide linking' y ARGININE                                                                                         ? 
'C6 H15 N4 O2 1' 175.209 
ASN   'L-peptide linking' y ASPARAGINE                                                                                       ? 
'C4 H8 N2 O3'    132.118 
ASP   'L-peptide linking' y 'ASPARTIC ACID'                                                                                  ? 
'C4 H7 N O4'     133.103 
CYS   'L-peptide linking' y CYSTEINE                                                                                         ? 
'C3 H7 N O2 S'   121.158 
DMS   non-polymer         . 'DIMETHYL SULFOXIDE'                                                                             ? 
'C2 H6 O S'      78.133  
GLN   'L-peptide linking' y GLUTAMINE                                                                                        ? 
'C5 H10 N2 O3'   146.144 
GLU   'L-peptide linking' y 'GLUTAMIC ACID'                                                                                  ? 
'C5 H9 N O4'     147.129 
GLY   'peptide linking'   y GLYCINE                                                                                          ? 
'C2 H5 N O2'     75.067  
HIS   'L-peptide linking' y HISTIDINE                                                                                        ? 
'C6 H10 N3 O2 1' 156.162 
HOH   non-polymer         . WATER                                                                                            ? 
'H2 O'           18.015  
ILE   'L-peptide linking' y ISOLEUCINE                                                                                       ? 
'C6 H13 N O2'    131.173 
LEU   'L-peptide linking' y LEUCINE                                                                                          ? 
'C6 H13 N O2'    131.173 
LYS   'L-peptide linking' y LYSINE                                                                                           ? 
'C6 H15 N2 O2 1' 147.195 
MET   'L-peptide linking' y METHIONINE                                                                                       ? 
'C5 H11 N O2 S'  149.211 
PHE   'L-peptide linking' y PHENYLALANINE                                                                                    ? 
'C9 H11 N O2'    165.189 
PRO   'L-peptide linking' y PROLINE                                                                                          ? 
'C5 H9 N O2'     115.130 
SER   'L-peptide linking' y SERINE                                                                                           ? 
'C3 H7 N O3'     105.093 
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        A1BXS 
_pdbx_entity_instance_feature.asym_id        ? 
_pdbx_entity_instance_feature.seq_num        ? 
_pdbx_entity_instance_feature.auth_comp_id   A1BXS 
_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 A1BXS 1  204 301 A1BXS LIG B . 
G 5 SO4   1  205 302 SO4   SO4 B . 
H 3 DMS   1  206 303 DMS   DMS B . 
I 5 SO4   1  207 304 SO4   SO4 B . 
J 6 HOH   1  101 48  HOH   HOH A . 
J 6 HOH   2  102 65  HOH   HOH A . 
J 6 HOH   3  103 105 HOH   HOH A . 
J 6 HOH   4  104 124 HOH   HOH A . 
J 6 HOH   5  105 98  HOH   HOH A . 
J 6 HOH   6  106 117 HOH   HOH A . 
J 6 HOH   7  107 110 HOH   HOH A . 
J 6 HOH   8  108 119 HOH   HOH A . 
J 6 HOH   9  109 34  HOH   HOH A . 
J 6 HOH   10 110 16  HOH   HOH A . 
J 6 HOH   11 111 36  HOH   HOH A . 
J 6 HOH   12 112 20  HOH   HOH A . 
J 6 HOH   13 113 77  HOH   HOH A . 
J 6 HOH   14 114 118 HOH   HOH A . 
J 6 HOH   15 115 120 HOH   HOH A . 
J 6 HOH   16 116 50  HOH   HOH A . 
J 6 HOH   17 117 129 HOH   HOH A . 
J 6 HOH   18 118 29  HOH   HOH A . 
J 6 HOH   19 119 70  HOH   HOH A . 
J 6 HOH   20 120 121 HOH   HOH A . 
J 6 HOH   21 121 40  HOH   HOH A . 
J 6 HOH   22 122 27  HOH   HOH A . 
J 6 HOH   23 123 85  HOH   HOH A . 
K 6 HOH   1  301 5   HOH   HOH B . 
K 6 HOH   2  302 51  HOH   HOH B . 
K 6 HOH   3  303 58  HOH   HOH B . 
K 6 HOH   4  304 11  HOH   HOH B . 
K 6 HOH   5  305 90  HOH   HOH B . 
K 6 HOH   6  306 92  HOH   HOH B . 
K 6 HOH   7  307 56  HOH   HOH B . 
K 6 HOH   8  308 54  HOH   HOH B . 
K 6 HOH   9  309 62  HOH   HOH B . 
K 6 HOH   10 310 32  HOH   HOH B . 
K 6 HOH   11 311 63  HOH   HOH B . 
K 6 HOH   12 312 128 HOH   HOH B . 
K 6 HOH   13 313 17  HOH   HOH B . 
K 6 HOH   14 314 106 HOH   HOH B . 
K 6 HOH   15 315 89  HOH   HOH B . 
K 6 HOH   16 316 31  HOH   HOH B . 
K 6 HOH   17 317 68  HOH   HOH B . 
K 6 HOH   18 318 103 HOH   HOH B . 
K 6 HOH   19 319 60  HOH   HOH B . 
K 6 HOH   20 320 14  HOH   HOH B . 
K 6 HOH   21 321 115 HOH   HOH B . 
K 6 HOH   22 322 67  HOH   HOH B . 
K 6 HOH   23 323 24  HOH   HOH B . 
K 6 HOH   24 324 100 HOH   HOH B . 
K 6 HOH   25 325 30  HOH   HOH B . 
K 6 HOH   26 326 69  HOH   HOH B . 
K 6 HOH   27 327 1   HOH   HOH B . 
K 6 HOH   28 328 108 HOH   HOH B . 
K 6 HOH   29 329 123 HOH   HOH B . 
K 6 HOH   30 330 42  HOH   HOH B . 
K 6 HOH   31 331 46  HOH   HOH B . 
K 6 HOH   32 332 4   HOH   HOH B . 
K 6 HOH   33 333 72  HOH   HOH B . 
K 6 HOH   34 334 2   HOH   HOH B . 
K 6 HOH   35 335 81  HOH   HOH B . 
K 6 HOH   36 336 21  HOH   HOH B . 
K 6 HOH   37 337 35  HOH   HOH B . 
K 6 HOH   38 338 127 HOH   HOH B . 
K 6 HOH   39 339 23  HOH   HOH B . 
K 6 HOH   40 340 12  HOH   HOH B . 
K 6 HOH   41 341 28  HOH   HOH B . 
K 6 HOH   42 342 116 HOH   HOH B . 
K 6 HOH   43 343 64  HOH   HOH B . 
K 6 HOH   44 344 107 HOH   HOH B . 
K 6 HOH   45 345 66  HOH   HOH B . 
K 6 HOH   46 346 39  HOH   HOH B . 
K 6 HOH   47 347 13  HOH   HOH B . 
K 6 HOH   48 348 122 HOH   HOH B . 
K 6 HOH   49 349 9   HOH   HOH B . 
K 6 HOH   50 350 43  HOH   HOH B . 
K 6 HOH   51 351 132 HOH   HOH B . 
K 6 HOH   52 352 102 HOH   HOH B . 
K 6 HOH   53 353 10  HOH   HOH B . 
K 6 HOH   54 354 82  HOH   HOH B . 
K 6 HOH   55 355 26  HOH   HOH B . 
K 6 HOH   56 356 18  HOH   HOH B . 
K 6 HOH   57 357 49  HOH   HOH B . 
K 6 HOH   58 358 73  HOH   HOH B . 
K 6 HOH   59 359 3   HOH   HOH B . 
K 6 HOH   60 360 57  HOH   HOH B . 
K 6 HOH   61 361 130 HOH   HOH B . 
K 6 HOH   62 362 79  HOH   HOH B . 
K 6 HOH   63 363 131 HOH   HOH B . 
K 6 HOH   64 364 87  HOH   HOH B . 
K 6 HOH   65 365 45  HOH   HOH B . 
K 6 HOH   66 366 83  HOH   HOH B . 
K 6 HOH   67 367 80  HOH   HOH B . 
K 6 HOH   68 368 44  HOH   HOH B . 
K 6 HOH   69 369 61  HOH   HOH B . 
K 6 HOH   70 370 112 HOH   HOH B . 
K 6 HOH   71 371 94  HOH   HOH B . 
K 6 HOH   72 372 126 HOH   HOH B . 
K 6 HOH   73 373 59  HOH   HOH B . 
K 6 HOH   74 374 75  HOH   HOH B . 
K 6 HOH   75 375 109 HOH   HOH B . 
K 6 HOH   76 376 125 HOH   HOH B . 
# 
loop_
_software.classification 
_software.name 
_software.version 
_software.citation_id 
_software.pdbx_ordinal 
_software.date 
_software.type 
_software.location 
_software.language 
refinement       REFMAC  5.8.0267 ? 1 ? ? ? ? 
refinement       BUSTER  .        ? 2 ? ? ? ? 
'data scaling'   Aimless .        ? 3 ? ? ? ? 
phasing          PHASER  .        ? 4 ? ? ? ? 
'data reduction' XDS     .        ? 5 ? ? ? ? 
# 
_cell.entry_id           7I21 
_cell.length_a           42.581 
_cell.length_b           42.581 
_cell.length_c           216.368 
_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                         7I21 
_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          7I21 
_exptl.method            'X-RAY DIFFRACTION' 
_exptl.crystals_number   1 
# 
_exptl_crystal.id                    1 
_exptl_crystal.density_meas          ? 
_exptl_crystal.density_Matthews      2.12 
_exptl_crystal.density_percent_sol   41.85 
_exptl_crystal.description           ? 
_exptl_crystal.preparation           ? 
# 
_exptl_crystal_grow.crystal_id      1 
_exptl_crystal_grow.method          'VAPOR DIFFUSION, SITTING DROP' 
_exptl_crystal_grow.pH              4.8 
_exptl_crystal_grow.temp            298 
_exptl_crystal_grow.pdbx_details    '30% w/v PEG 2000, 0.2M Ammonium sulfate, 0.1M acetate (pH 4.8)' 
_exptl_crystal_grow.temp_details    ? 
_exptl_crystal_grow.pdbx_pH_range   ? 
# 
_diffrn.id                               1 
_diffrn.ambient_temp                     100 
_diffrn.crystal_id                       1 
_diffrn.ambient_temp_details             ? 
_diffrn.pdbx_serial_crystal_experiment   ? 
# 
_diffrn_detector.detector               PIXEL 
_diffrn_detector.type                   'DECTRIS EIGER2 XE 9M' 
_diffrn_detector.pdbx_collection_date   2023-10-10 
_diffrn_detector.diffrn_id              1 
_diffrn_detector.details                ? 
# 
_diffrn_radiation.diffrn_id                        1 
_diffrn_radiation.wavelength_id                    1 
_diffrn_radiation.pdbx_diffrn_protocol             'SINGLE WAVELENGTH' 
_diffrn_radiation.pdbx_monochromatic_or_laue_m_l   ? 
_diffrn_radiation.monochromator                    ? 
_diffrn_radiation.pdbx_scattering_type             x-ray 
# 
_diffrn_radiation_wavelength.id           1 
_diffrn_radiation_wavelength.wavelength   0.92124 
_diffrn_radiation_wavelength.wt           1.0 
# 
_diffrn_source.diffrn_id                   1 
_diffrn_source.source                      SYNCHROTRON 
_diffrn_source.type                        'DIAMOND BEAMLINE I04-1' 
_diffrn_source.pdbx_wavelength_list        0.92124 
_diffrn_source.pdbx_synchrotron_site       Diamond 
_diffrn_source.pdbx_synchrotron_beamline   I04-1 
_diffrn_source.pdbx_wavelength             ? 
# 
_reflns.entry_id                     7I21 
_reflns.pdbx_diffrn_id               1 
_reflns.pdbx_ordinal                 1 
_reflns.d_resolution_low             54.11 
_reflns.d_resolution_high            1.83 
_reflns.number_obs                   18759 
_reflns.percent_possible_obs         100.0 
_reflns.pdbx_Rmerge_I_obs            0.171 
_reflns.pdbx_netI_over_sigmaI        6.8 
_reflns.pdbx_redundancy              25.4 
_reflns.pdbx_Rrim_I_all              0.175 
_reflns.pdbx_Rpim_I_all              0.035 
_reflns.pdbx_CC_half                 0.998 
_reflns.pdbx_number_measured_all     476792 
_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.pdbx_CC_star                 ? 
# 
_reflns_shell.pdbx_diffrn_id              1 
_reflns_shell.pdbx_ordinal                1 
_reflns_shell.d_res_high                  1.83 
_reflns_shell.d_res_low                   1.87 
_reflns_shell.number_measured_all         30327 
_reflns_shell.number_unique_obs           1123 
_reflns_shell.Rmerge_I_obs                5.454 
_reflns_shell.pdbx_chi_squared            0.05 
_reflns_shell.pdbx_redundancy             27.0 
_reflns_shell.percent_possible_obs        99.9 
_reflns_shell.pdbx_netI_over_sigmaI_obs   0.2 
_reflns_shell.pdbx_Rrim_I_all             5.557 
_reflns_shell.pdbx_Rpim_I_all             1.061 
_reflns_shell.pdbx_CC_half                0.207 
_reflns_shell.percent_possible_all        ? 
_reflns_shell.pdbx_Rsym_value             ? 
_reflns_shell.meanI_over_sigI_obs         ? 
_reflns_shell.number_measured_obs         ? 
_reflns_shell.number_unique_all           ? 
_reflns_shell.pdbx_CC_star                ? 
# 
_refine.pdbx_refine_id                           'X-RAY DIFFRACTION' 
_refine.entry_id                                 7I21 
_refine.pdbx_diffrn_id                           1 
_refine.pdbx_TLS_residual_ADP_flag               ? 
_refine.ls_number_reflns_obs                     16249 
_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                             54.09 
_refine.ls_d_res_high                            1.83 
_refine.ls_percent_reflns_obs                    91.51 
_refine.ls_R_factor_obs                          0.24270 
_refine.ls_R_factor_all                          ? 
_refine.ls_R_factor_R_work                       0.23944 
_refine.ls_R_factor_R_free                       0.30459 
_refine.ls_R_factor_R_free_error                 ? 
_refine.ls_R_factor_R_free_error_details         ? 
_refine.ls_percent_reflns_R_free                 4.9 
_refine.ls_number_reflns_R_free                  838 
_refine.ls_number_parameters                     ? 
_refine.ls_number_restraints                     ? 
_refine.occupancy_min                            ? 
_refine.occupancy_max                            ? 
_refine.correlation_coeff_Fo_to_Fc               0.959 
_refine.correlation_coeff_Fo_to_Fc_free          0.933 
_refine.B_iso_mean                               54.396 
_refine.aniso_B[1][1]                            1.70 
_refine.aniso_B[2][2]                            1.70 
_refine.aniso_B[3][3]                            -3.41 
_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                       0.221 
_refine.pdbx_overall_ESU_R_Free                  0.202 
_refine.overall_SU_ML                            0.278 
_refine.pdbx_overall_phase_error                 ? 
_refine.overall_SU_B                             10.757 
_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         49 
_refine_hist.number_atoms_solvent             99 
_refine_hist.number_atoms_total               1624 
_refine_hist.d_res_high                       1.83 
_refine_hist.d_res_low                        54.09 
# 
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  0.014  ? 2107 'X-RAY DIFFRACTION' ? 
r_bond_other_d               0.001  0.015  ? 1724 'X-RAY DIFFRACTION' ? 
r_angle_refined_deg          1.526  1.639  ? 2555 'X-RAY DIFFRACTION' ? 
r_angle_other_deg            1.180  1.595  ? 3994 'X-RAY DIFFRACTION' ? 
r_dihedral_angle_1_deg       7.524  5.000  ? 247  'X-RAY DIFFRACTION' ? 
r_dihedral_angle_2_deg       33.989 22.471 ? 85   'X-RAY DIFFRACTION' ? 
r_dihedral_angle_3_deg       15.667 15.000 ? 295  'X-RAY DIFFRACTION' ? 
r_dihedral_angle_4_deg       19.189 15.000 ? 10   'X-RAY DIFFRACTION' ? 
r_chiral_restr               0.058  0.200  ? 224  'X-RAY DIFFRACTION' ? 
r_gen_planes_refined         0.007  0.020  ? 2190 'X-RAY DIFFRACTION' ? 
r_gen_planes_other           0.002  0.020  ? 412  '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                  3.970  5.387  ? 1040 'X-RAY DIFFRACTION' ? 
r_mcbond_other               4.061  5.271  ? 984  'X-RAY DIFFRACTION' ? 
r_mcangle_it                 6.270  7.834  ? 1185 'X-RAY DIFFRACTION' ? 
r_mcangle_other              6.275  7.840  ? 1186 'X-RAY DIFFRACTION' ? 
r_scbond_it                  4.287  6.063  ? 1067 'X-RAY DIFFRACTION' ? 
r_scbond_other               4.296  6.044  ? 1055 'X-RAY DIFFRACTION' ? 
r_scangle_it                 ?      ?      ? ?    'X-RAY DIFFRACTION' ? 
r_scangle_other              6.731  8.497  ? 1359 'X-RAY DIFFRACTION' ? 
r_long_range_B_refined       15.135 58.504 ? 2110 'X-RAY DIFFRACTION' ? 
r_long_range_B_other         15.117 58.330 ? 2093 '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                       1.830 
_refine_ls_shell.d_res_low                        1.878 
_refine_ls_shell.number_reflns_R_work             288 
_refine_ls_shell.R_factor_R_work                  0.514 
_refine_ls_shell.percent_reflns_obs               23.27 
_refine_ls_shell.R_factor_R_free                  0.557 
_refine_ls_shell.R_factor_R_free_error            ? 
_refine_ls_shell.percent_reflns_R_free            ? 
_refine_ls_shell.number_reflns_R_free             22 
_refine_ls_shell.number_reflns_all                ? 
_refine_ls_shell.R_factor_all                     ? 
_refine_ls_shell.R_factor_obs                     ? 
_refine_ls_shell.number_reflns_obs                ? 
# 
_struct.entry_id                  7I21 
_struct.title                     
'PanDDA analysis group deposition -- Crystal Structure of ZIKV NS2B-NS3 protease in complex with NegAcid3-Am03' 
_struct.pdbx_model_details        ? 
_struct.pdbx_CASP_flag            ? 
_struct.pdbx_model_type_details   ? 
# 
_struct_keywords.entry_id        7I21 
_struct_keywords.pdbx_keywords   'VIRAL PROTEIN' 
_struct_keywords.text            'SGC - Diamond I04-1, PanDDA, XChemExplorer, VIRAL PROTEIN' 
# 
loop_
_struct_asym.id 
_struct_asym.pdbx_blank_PDB_chainid_flag 
_struct_asym.pdbx_modified 
_struct_asym.entity_id 
_struct_asym.details 
A N N 1 ? 
B N N 2 ? 
C N N 3 ? 
D N N 3 ? 
E N N 3 ? 
F N N 4 ? 
G N N 5 ? 
H N N 3 ? 
I N N 5 ? 
J N N 6 ? 
K N N 6 ? 
# 
loop_
_struct_ref.id 
_struct_ref.db_name 
_struct_ref.db_code 
_struct_ref.pdbx_db_accession 
_struct_ref.pdbx_db_isoform 
_struct_ref.entity_id 
_struct_ref.pdbx_seq_one_letter_code 
_struct_ref.pdbx_align_begin 
1 UNP POLG_ZIKV Q32ZE1 ? 1 GKSVDMYIERAGDITWEKDAEVTGNSPRLDVALDESGDFSLVEE 1414 
2 UNP POLG_ZIKV Q32ZE1 ? 2 
;KEVKKGETTDGVYRVMTRRLLGSTQVGVGVMQEGVFHTMWHVTKGAALRSGEGRLDPYWGDVKQDLVSYCGPWKLDAAWD
GLSEVQLLAVPPGERARNIQTLPGIFKTKDGDIGAVALDYPAGTSGSPILDKCGRVIGLYGNGVVIKNGSYVSAITQGKR
EEETPVE
;
1509 
# 
loop_
_struct_ref_seq.align_id 
_struct_ref_seq.ref_id 
_struct_ref_seq.pdbx_PDB_id_code 
_struct_ref_seq.pdbx_strand_id 
_struct_ref_seq.seq_align_beg 
_struct_ref_seq.pdbx_seq_align_beg_ins_code 
_struct_ref_seq.seq_align_end 
_struct_ref_seq.pdbx_seq_align_end_ins_code 
_struct_ref_seq.pdbx_db_accession 
_struct_ref_seq.db_align_beg 
_struct_ref_seq.pdbx_db_align_beg_ins_code 
_struct_ref_seq.db_align_end 
_struct_ref_seq.pdbx_db_align_end_ins_code 
_struct_ref_seq.pdbx_auth_seq_align_beg 
_struct_ref_seq.pdbx_auth_seq_align_end 
1 1 7I21 A 3 ? 46  ? Q32ZE1 1414 ? 1457 ? 46 89  
2 2 7I21 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 7I21 SER A 1  ? UNP Q32ZE1 ?   ?    'expression tag'        44  1 
1 7I21 MET A 2  ? UNP Q32ZE1 ?   ?    'expression tag'        45  2 
2 7I21 MET B 1  ? UNP Q32ZE1 ?   ?    'initiating methionine' 10  3 
2 7I21 LYS B 98 ? UNP Q32ZE1 ARG 1605 conflict                107 4 
# 
_pdbx_struct_assembly.id                   1 
_pdbx_struct_assembly.details              author_defined_assembly 
_pdbx_struct_assembly.method_details       ? 
_pdbx_struct_assembly.oligomeric_details   dimeric 
_pdbx_struct_assembly.oligomeric_count     2 
# 
_pdbx_struct_assembly_gen.assembly_id       1 
_pdbx_struct_assembly_gen.oper_expression   1 
_pdbx_struct_assembly_gen.asym_id_list      A,B,C,D,E,F,G,H,I,J,K 
# 
_pdbx_struct_oper_list.id                   1 
_pdbx_struct_oper_list.type                 'identity operation' 
_pdbx_struct_oper_list.name                 1_555 
_pdbx_struct_oper_list.symmetry_operation   x,y,z 
_pdbx_struct_oper_list.matrix[1][1]         1.0000000000 
_pdbx_struct_oper_list.matrix[1][2]         0.0000000000 
_pdbx_struct_oper_list.matrix[1][3]         0.0000000000 
_pdbx_struct_oper_list.vector[1]            0.0000000000 
_pdbx_struct_oper_list.matrix[2][1]         0.0000000000 
_pdbx_struct_oper_list.matrix[2][2]         1.0000000000 
_pdbx_struct_oper_list.matrix[2][3]         0.0000000000 
_pdbx_struct_oper_list.vector[2]            0.0000000000 
_pdbx_struct_oper_list.matrix[3][1]         0.0000000000 
_pdbx_struct_oper_list.matrix[3][2]         0.0000000000 
_pdbx_struct_oper_list.matrix[3][3]         1.0000000000 
_pdbx_struct_oper_list.vector[3]            0.0000000000 
# 
loop_
_struct_conf.conf_type_id 
_struct_conf.id 
_struct_conf.pdbx_PDB_helix_id 
_struct_conf.beg_label_comp_id 
_struct_conf.beg_label_asym_id 
_struct_conf.beg_label_seq_id 
_struct_conf.pdbx_beg_PDB_ins_code 
_struct_conf.end_label_comp_id 
_struct_conf.end_label_asym_id 
_struct_conf.end_label_seq_id 
_struct_conf.pdbx_end_PDB_ins_code 
_struct_conf.beg_auth_comp_id 
_struct_conf.beg_auth_asym_id 
_struct_conf.beg_auth_seq_id 
_struct_conf.end_auth_comp_id 
_struct_conf.end_auth_asym_id 
_struct_conf.end_auth_seq_id 
_struct_conf.pdbx_PDB_helix_class 
_struct_conf.details 
_struct_conf.pdbx_PDB_helix_length 
HELX_P HELX_P1 AA1 MET B 40  ? LYS B 45  ? MET B 49  LYS B 54  1 ? 6 
HELX_P HELX_P2 AA2 PRO B 122 ? SER B 126 ? PRO B 131 SER B 135 5 ? 5 
# 
_struct_conf_type.id          HELX_P 
_struct_conf_type.criteria    ? 
_struct_conf_type.reference   ? 
# 
_struct_conn.id                            disulf1 
_struct_conn.conn_type_id                  disulf 
_struct_conn.pdbx_leaving_atom_flag        ? 
_struct_conn.pdbx_PDB_id                   ? 
_struct_conn.ptnr1_label_asym_id           B 
_struct_conn.ptnr1_label_comp_id           CYS 
_struct_conn.ptnr1_label_seq_id            134 
_struct_conn.ptnr1_label_atom_id           SG 
_struct_conn.pdbx_ptnr1_label_alt_id       ? 
_struct_conn.pdbx_ptnr1_PDB_ins_code       ? 
_struct_conn.pdbx_ptnr1_standard_comp_id   ? 
_struct_conn.ptnr1_symmetry                1_555 
_struct_conn.ptnr2_label_asym_id           B 
_struct_conn.ptnr2_label_comp_id           CYS 
_struct_conn.ptnr2_label_seq_id            134 
_struct_conn.ptnr2_label_atom_id           SG 
_struct_conn.pdbx_ptnr2_label_alt_id       ? 
_struct_conn.pdbx_ptnr2_PDB_ins_code       ? 
_struct_conn.ptnr1_auth_asym_id            B 
_struct_conn.ptnr1_auth_comp_id            CYS 
_struct_conn.ptnr1_auth_seq_id             143 
_struct_conn.ptnr2_auth_asym_id            B 
_struct_conn.ptnr2_auth_comp_id            CYS 
_struct_conn.ptnr2_auth_seq_id             143 
_struct_conn.ptnr2_symmetry                8_444 
_struct_conn.pdbx_ptnr3_label_atom_id      ? 
_struct_conn.pdbx_ptnr3_label_seq_id       ? 
_struct_conn.pdbx_ptnr3_label_comp_id      ? 
_struct_conn.pdbx_ptnr3_label_asym_id      ? 
_struct_conn.pdbx_ptnr3_label_alt_id       ? 
_struct_conn.pdbx_ptnr3_PDB_ins_code       ? 
_struct_conn.details                       ? 
_struct_conn.pdbx_dist_value               2.273 
_struct_conn.pdbx_value_order              ? 
_struct_conn.pdbx_role                     ? 
# 
_struct_conn_type.id          disulf 
_struct_conn_type.criteria    ? 
_struct_conn_type.reference   ? 
# 
_pdbx_modification_feature.ordinal                            1 
_pdbx_modification_feature.label_comp_id                      CYS 
_pdbx_modification_feature.label_asym_id                      B 
_pdbx_modification_feature.label_seq_id                       134 
_pdbx_modification_feature.label_alt_id                       ? 
_pdbx_modification_feature.modified_residue_label_comp_id     CYS 
_pdbx_modification_feature.modified_residue_label_asym_id     B 
_pdbx_modification_feature.modified_residue_label_seq_id      134 
_pdbx_modification_feature.modified_residue_label_alt_id      ? 
_pdbx_modification_feature.auth_comp_id                       CYS 
_pdbx_modification_feature.auth_asym_id                       B 
_pdbx_modification_feature.auth_seq_id                        143 
_pdbx_modification_feature.PDB_ins_code                       ? 
_pdbx_modification_feature.symmetry                           1_555 
_pdbx_modification_feature.modified_residue_auth_comp_id      CYS 
_pdbx_modification_feature.modified_residue_auth_asym_id      B 
_pdbx_modification_feature.modified_residue_auth_seq_id       143 
_pdbx_modification_feature.modified_residue_PDB_ins_code      ? 
_pdbx_modification_feature.modified_residue_symmetry          8_444 
_pdbx_modification_feature.comp_id_linking_atom               SG 
_pdbx_modification_feature.modified_residue_id_linking_atom   SG 
_pdbx_modification_feature.modified_residue_id                . 
_pdbx_modification_feature.ref_pcm_id                         . 
_pdbx_modification_feature.ref_comp_id                        . 
_pdbx_modification_feature.type                               None 
_pdbx_modification_feature.category                           'Disulfide bridge' 
# 
loop_
_struct_sheet.id 
_struct_sheet.type 
_struct_sheet.number_strands 
_struct_sheet.details 
AA1 ? 8 ? 
AA2 ? 5 ? 
AA3 ? 6 ? 
# 
loop_
_struct_sheet_order.sheet_id 
_struct_sheet_order.range_id_1 
_struct_sheet_order.range_id_2 
_struct_sheet_order.offset 
_struct_sheet_order.sense 
AA1 1 2 ? anti-parallel 
AA1 2 3 ? parallel      
AA1 3 4 ? anti-parallel 
AA1 4 5 ? anti-parallel 
AA1 5 6 ? anti-parallel 
AA1 6 7 ? anti-parallel 
AA1 7 8 ? anti-parallel 
AA2 1 2 ? parallel      
AA2 2 3 ? anti-parallel 
AA2 3 4 ? anti-parallel 
AA2 4 5 ? anti-parallel 
AA3 1 2 ? anti-parallel 
AA3 2 3 ? parallel      
AA3 3 4 ? anti-parallel 
AA3 4 5 ? anti-parallel 
AA3 5 6 ? anti-parallel 
# 
loop_
_struct_sheet_range.sheet_id 
_struct_sheet_range.id 
_struct_sheet_range.beg_label_comp_id 
_struct_sheet_range.beg_label_asym_id 
_struct_sheet_range.beg_label_seq_id 
_struct_sheet_range.pdbx_beg_PDB_ins_code 
_struct_sheet_range.end_label_comp_id 
_struct_sheet_range.end_label_asym_id 
_struct_sheet_range.end_label_seq_id 
_struct_sheet_range.pdbx_end_PDB_ins_code 
_struct_sheet_range.beg_auth_comp_id 
_struct_sheet_range.beg_auth_asym_id 
_struct_sheet_range.beg_auth_seq_id 
_struct_sheet_range.end_auth_comp_id 
_struct_sheet_range.end_auth_asym_id 
_struct_sheet_range.end_auth_seq_id 
AA1 1 GLY B 54  ? LEU B 56  ? GLY B 63  LEU B 65  
AA1 2 LEU B 49  ? SER B 51  ? LEU B 58  SER B 60  
AA1 3 MET A 8   ? GLY A 14  ? MET A 51  GLY A 57  
AA1 4 GLY B 12  ? THR B 18  ? GLY B 21  THR B 27  
AA1 5 THR B 25  ? GLN B 33  ? THR B 34  GLN B 42  
AA1 6 VAL B 36  ? THR B 39  ? VAL B 45  THR B 48  
AA1 7 LEU B 67  ? TYR B 70  ? LEU B 76  TYR B 79  
AA1 8 PRO B 58  ? ASP B 62  ? PRO B 67  ASP B 71  
AA2 1 GLU A 23  ? VAL A 24  ? GLU A 66  VAL A 67  
AA2 2 LYS B 98  ? THR B 102 ? LYS B 107 THR B 111 
AA2 3 VAL B 86  ? ALA B 90  ? VAL B 95  ALA B 99  
AA2 4 PRO B 129 ? LEU B 131 ? PRO B 138 LEU B 140 
AA2 5 VAL B 137 ? LEU B 140 ? VAL B 146 LEU B 149 
AA3 1 PHE A 41  ? LEU A 43  ? PHE A 84  LEU A 86  
AA3 2 ARG A 30  ? LEU A 35  ? ARG A 73  LEU A 78  
AA3 3 GLY B 105 ? THR B 109 ? GLY B 114 THR B 118 
AA3 4 GLY B 112 ? VAL B 117 ? GLY B 121 VAL B 126 
AA3 5 TYR B 152 ? ALA B 155 ? TYR B 161 ALA B 164 
AA3 6 GLY B 144 ? VAL B 146 ? GLY B 153 VAL B 155 
# 
loop_
_pdbx_struct_sheet_hbond.sheet_id 
_pdbx_struct_sheet_hbond.range_id_1 
_pdbx_struct_sheet_hbond.range_id_2 
_pdbx_struct_sheet_hbond.range_1_label_atom_id 
_pdbx_struct_sheet_hbond.range_1_label_comp_id 
_pdbx_struct_sheet_hbond.range_1_label_asym_id 
_pdbx_struct_sheet_hbond.range_1_label_seq_id 
_pdbx_struct_sheet_hbond.range_1_PDB_ins_code 
_pdbx_struct_sheet_hbond.range_1_auth_atom_id 
_pdbx_struct_sheet_hbond.range_1_auth_comp_id 
_pdbx_struct_sheet_hbond.range_1_auth_asym_id 
_pdbx_struct_sheet_hbond.range_1_auth_seq_id 
_pdbx_struct_sheet_hbond.range_2_label_atom_id 
_pdbx_struct_sheet_hbond.range_2_label_comp_id 
_pdbx_struct_sheet_hbond.range_2_label_asym_id 
_pdbx_struct_sheet_hbond.range_2_label_seq_id 
_pdbx_struct_sheet_hbond.range_2_PDB_ins_code 
_pdbx_struct_sheet_hbond.range_2_auth_atom_id 
_pdbx_struct_sheet_hbond.range_2_auth_comp_id 
_pdbx_struct_sheet_hbond.range_2_auth_asym_id 
_pdbx_struct_sheet_hbond.range_2_auth_seq_id 
AA1 1 2 O LEU B 56  ? O LEU B 65  N LEU B 49  ? N LEU B 58  
AA1 2 3 O ARG B 50  ? O ARG B 59  N MET A 8   ? N MET A 51  
AA1 3 4 N TYR A 9   ? N TYR A 52  O MET B 17  ? O MET B 26  
AA1 4 5 N VAL B 16  ? N VAL B 25  O GLY B 28  ? O GLY B 37  
AA1 5 6 N VAL B 31  ? N VAL B 40  O HIS B 38  ? O HIS B 47  
AA1 6 7 N THR B 39  ? N THR B 48  O VAL B 68  ? O VAL B 77  
AA1 7 8 O SER B 69  ? O SER B 78  N 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                   7I21 
_pdbx_entry_details.compound_details           ? 
_pdbx_entry_details.source_details             ? 
_pdbx_entry_details.nonpolymer_details         ? 
_pdbx_entry_details.sequence_details           ? 
_pdbx_entry_details.has_ligand_of_interest     Y 
_pdbx_entry_details.has_protein_modification   Y 
# 
loop_
_pdbx_validate_close_contact.id 
_pdbx_validate_close_contact.PDB_model_num 
_pdbx_validate_close_contact.auth_atom_id_1 
_pdbx_validate_close_contact.auth_asym_id_1 
_pdbx_validate_close_contact.auth_comp_id_1 
_pdbx_validate_close_contact.auth_seq_id_1 
_pdbx_validate_close_contact.PDB_ins_code_1 
_pdbx_validate_close_contact.label_alt_id_1 
_pdbx_validate_close_contact.auth_atom_id_2 
_pdbx_validate_close_contact.auth_asym_id_2 
_pdbx_validate_close_contact.auth_comp_id_2 
_pdbx_validate_close_contact.auth_seq_id_2 
_pdbx_validate_close_contact.PDB_ins_code_2 
_pdbx_validate_close_contact.label_alt_id_2 
_pdbx_validate_close_contact.dist 
1 1 O   B VAL 146 ? ? O  B HOH 301 ? ? 2.11 
2 1 OE1 B GLU 17  ? ? O  B HOH 302 ? ? 2.15 
3 1 OD2 B ASP 90  ? ? OG B SER 93  ? ? 2.19 
# 
loop_
_pdbx_validate_torsion.id 
_pdbx_validate_torsion.PDB_model_num 
_pdbx_validate_torsion.auth_comp_id 
_pdbx_validate_torsion.auth_asym_id 
_pdbx_validate_torsion.auth_seq_id 
_pdbx_validate_torsion.PDB_ins_code 
_pdbx_validate_torsion.label_alt_id 
_pdbx_validate_torsion.phi 
_pdbx_validate_torsion.psi 
1  1 ASP A 64  ? A 65.59   66.35  
2  1 ASP A 64  ? B 65.59   66.35  
3  1 ASP A 64  ? C 70.76   61.54  
4  1 ASP A 64  ? D 70.76   61.54  
5  1 GLU A 66  ? A -58.03  100.19 
6  1 GLU A 66  ? B -58.03  100.19 
7  1 GLU A 66  ? C -54.71  102.21 
8  1 GLU A 66  ? D -54.71  102.21 
9  1 ASP B 20  ? ? -47.72  150.04 
10 1 CYS B 80  ? ? 82.84   -5.79  
11 1 LEU B 92  ? ? -126.50 -54.74 
12 1 LYS B 157 ? A -26.98  -50.10 
13 1 LYS B 157 ? B -26.98  -50.10 
# 
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 ? K HOH . 
2 1 B HOH 365 ? K 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 
A1BXS N1   N N N 1   
A1BXS N3   N Y N 2   
A1BXS C4   C Y N 3   
A1BXS C5   C N N 4   
A1BXS C6   C Y N 5   
A1BXS C7   C Y N 6   
A1BXS C8   C Y N 7   
A1BXS C10  C Y N 8   
A1BXS C13  C N N 9   
A1BXS C15  C N S 10  
A1BXS C17  C N N 11  
A1BXS C1   C N N 12  
A1BXS C2   C Y N 13  
A1BXS C3   C Y N 14  
A1BXS O1   O N N 15  
A1BXS C9   C Y N 16  
A1BXS C11  C N N 17  
A1BXS C12  C N N 18  
A1BXS O2   O N N 19  
A1BXS C14  C N N 20  
A1BXS C16  C N N 21  
A1BXS N2   N N N 22  
A1BXS C18  C Y N 23  
A1BXS H6   H N N 24  
A1BXS H5   H N N 25  
A1BXS H8   H N N 26  
A1BXS H9   H N N 27  
A1BXS H14  H N N 28  
A1BXS H13  H N N 29  
A1BXS H17  H N N 30  
A1BXS H23  H N N 31  
A1BXS H22  H N N 32  
A1BXS H3   H N N 33  
A1BXS H1   H N N 34  
A1BXS H2   H N N 35  
A1BXS H4   H N N 36  
A1BXS H7   H N N 37  
A1BXS H10  H N N 38  
A1BXS H12  H N N 39  
A1BXS H11  H N N 40  
A1BXS H16  H N N 41  
A1BXS H15  H N N 42  
A1BXS H19  H N N 43  
A1BXS H18  H N N 44  
A1BXS H24  H N N 45  
A1BXS H20  H N N 46  
ALA   N    N N N 47  
ALA   CA   C N S 48  
ALA   C    C N N 49  
ALA   O    O N N 50  
ALA   CB   C N N 51  
ALA   OXT  O N N 52  
ALA   H    H N N 53  
ALA   H2   H N N 54  
ALA   HA   H N N 55  
ALA   HB1  H N N 56  
ALA   HB2  H N N 57  
ALA   HB3  H N N 58  
ALA   HXT  H N N 59  
ARG   N    N N N 60  
ARG   CA   C N S 61  
ARG   C    C N N 62  
ARG   O    O N N 63  
ARG   CB   C N N 64  
ARG   CG   C N N 65  
ARG   CD   C N N 66  
ARG   NE   N N N 67  
ARG   CZ   C N N 68  
ARG   NH1  N N N 69  
ARG   NH2  N N N 70  
ARG   OXT  O N N 71  
ARG   H    H N N 72  
ARG   H2   H N N 73  
ARG   HA   H N N 74  
ARG   HB2  H N N 75  
ARG   HB3  H N N 76  
ARG   HG2  H N N 77  
ARG   HG3  H N N 78  
ARG   HD2  H N N 79  
ARG   HD3  H N N 80  
ARG   HE   H N N 81  
ARG   HH11 H N N 82  
ARG   HH12 H N N 83  
ARG   HH21 H N N 84  
ARG   HH22 H N N 85  
ARG   HXT  H N N 86  
ASN   N    N N N 87  
ASN   CA   C N S 88  
ASN   C    C N N 89  
ASN   O    O N N 90  
ASN   CB   C N N 91  
ASN   CG   C N N 92  
ASN   OD1  O N N 93  
ASN   ND2  N N N 94  
ASN   OXT  O N N 95  
ASN   H    H N N 96  
ASN   H2   H N N 97  
ASN   HA   H N N 98  
ASN   HB2  H N N 99  
ASN   HB3  H N N 100 
ASN   HD21 H N N 101 
ASN   HD22 H N N 102 
ASN   HXT  H N N 103 
ASP   N    N N N 104 
ASP   CA   C N S 105 
ASP   C    C N N 106 
ASP   O    O N N 107 
ASP   CB   C N N 108 
ASP   CG   C N N 109 
ASP   OD1  O N N 110 
ASP   OD2  O N N 111 
ASP   OXT  O N N 112 
ASP   H    H N N 113 
ASP   H2   H N N 114 
ASP   HA   H N N 115 
ASP   HB2  H N N 116 
ASP   HB3  H N N 117 
ASP   HD2  H N N 118 
ASP   HXT  H N N 119 
CYS   N    N N N 120 
CYS   CA   C N R 121 
CYS   C    C N N 122 
CYS   O    O N N 123 
CYS   CB   C N N 124 
CYS   SG   S N N 125 
CYS   OXT  O N N 126 
CYS   H    H N N 127 
CYS   H2   H N N 128 
CYS   HA   H N N 129 
CYS   HB2  H N N 130 
CYS   HB3  H N N 131 
CYS   HG   H N N 132 
CYS   HXT  H N N 133 
DMS   S    S N N 134 
DMS   O    O N N 135 
DMS   C1   C N N 136 
DMS   C2   C N N 137 
DMS   H11  H N N 138 
DMS   H12  H N N 139 
DMS   H13  H N N 140 
DMS   H21  H N N 141 
DMS   H22  H N N 142 
DMS   H23  H N N 143 
GLN   N    N N N 144 
GLN   CA   C N S 145 
GLN   C    C N N 146 
GLN   O    O N N 147 
GLN   CB   C N N 148 
GLN   CG   C N N 149 
GLN   CD   C N N 150 
GLN   OE1  O N N 151 
GLN   NE2  N N N 152 
GLN   OXT  O N N 153 
GLN   H    H N N 154 
GLN   H2   H N N 155 
GLN   HA   H N N 156 
GLN   HB2  H N N 157 
GLN   HB3  H N N 158 
GLN   HG2  H N N 159 
GLN   HG3  H N N 160 
GLN   HE21 H N N 161 
GLN   HE22 H N N 162 
GLN   HXT  H N N 163 
GLU   N    N N N 164 
GLU   CA   C N S 165 
GLU   C    C N N 166 
GLU   O    O N N 167 
GLU   CB   C N N 168 
GLU   CG   C N N 169 
GLU   CD   C N N 170 
GLU   OE1  O N N 171 
GLU   OE2  O N N 172 
GLU   OXT  O N N 173 
GLU   H    H N N 174 
GLU   H2   H N N 175 
GLU   HA   H N N 176 
GLU   HB2  H N N 177 
GLU   HB3  H N N 178 
GLU   HG2  H N N 179 
GLU   HG3  H N N 180 
GLU   HE2  H N N 181 
GLU   HXT  H N N 182 
GLY   N    N N N 183 
GLY   CA   C N N 184 
GLY   C    C N N 185 
GLY   O    O N N 186 
GLY   OXT  O N N 187 
GLY   H    H N N 188 
GLY   H2   H N N 189 
GLY   HA2  H N N 190 
GLY   HA3  H N N 191 
GLY   HXT  H N N 192 
HIS   N    N N N 193 
HIS   CA   C N S 194 
HIS   C    C N N 195 
HIS   O    O N N 196 
HIS   CB   C N N 197 
HIS   CG   C Y N 198 
HIS   ND1  N Y N 199 
HIS   CD2  C Y N 200 
HIS   CE1  C Y N 201 
HIS   NE2  N Y N 202 
HIS   OXT  O N N 203 
HIS   H    H N N 204 
HIS   H2   H N N 205 
HIS   HA   H N N 206 
HIS   HB2  H N N 207 
HIS   HB3  H N N 208 
HIS   HD1  H N N 209 
HIS   HD2  H N N 210 
HIS   HE1  H N N 211 
HIS   HE2  H N N 212 
HIS   HXT  H N N 213 
HOH   O    O N N 214 
HOH   H1   H N N 215 
HOH   H2   H N N 216 
ILE   N    N N N 217 
ILE   CA   C N S 218 
ILE   C    C N N 219 
ILE   O    O N N 220 
ILE   CB   C N S 221 
ILE   CG1  C N N 222 
ILE   CG2  C N N 223 
ILE   CD1  C N N 224 
ILE   OXT  O N N 225 
ILE   H    H N N 226 
ILE   H2   H N N 227 
ILE   HA   H N N 228 
ILE   HB   H N N 229 
ILE   HG12 H N N 230 
ILE   HG13 H N N 231 
ILE   HG21 H N N 232 
ILE   HG22 H N N 233 
ILE   HG23 H N N 234 
ILE   HD11 H N N 235 
ILE   HD12 H N N 236 
ILE   HD13 H N N 237 
ILE   HXT  H N N 238 
LEU   N    N N N 239 
LEU   CA   C N S 240 
LEU   C    C N N 241 
LEU   O    O N N 242 
LEU   CB   C N N 243 
LEU   CG   C N N 244 
LEU   CD1  C N N 245 
LEU   CD2  C N N 246 
LEU   OXT  O N N 247 
LEU   H    H N N 248 
LEU   H2   H N N 249 
LEU   HA   H N N 250 
LEU   HB2  H N N 251 
LEU   HB3  H N N 252 
LEU   HG   H N N 253 
LEU   HD11 H N N 254 
LEU   HD12 H N N 255 
LEU   HD13 H N N 256 
LEU   HD21 H N N 257 
LEU   HD22 H N N 258 
LEU   HD23 H N N 259 
LEU   HXT  H N N 260 
LYS   N    N N N 261 
LYS   CA   C N S 262 
LYS   C    C N N 263 
LYS   O    O N N 264 
LYS   CB   C N N 265 
LYS   CG   C N N 266 
LYS   CD   C N N 267 
LYS   CE   C N N 268 
LYS   NZ   N N N 269 
LYS   OXT  O N N 270 
LYS   H    H N N 271 
LYS   H2   H N N 272 
LYS   HA   H N N 273 
LYS   HB2  H N N 274 
LYS   HB3  H N N 275 
LYS   HG2  H N N 276 
LYS   HG3  H N N 277 
LYS   HD2  H N N 278 
LYS   HD3  H N N 279 
LYS   HE2  H N N 280 
LYS   HE3  H N N 281 
LYS   HZ1  H N N 282 
LYS   HZ2  H N N 283 
LYS   HZ3  H N N 284 
LYS   HXT  H N N 285 
MET   N    N N N 286 
MET   CA   C N S 287 
MET   C    C N N 288 
MET   O    O N N 289 
MET   CB   C N N 290 
MET   CG   C N N 291 
MET   SD   S N N 292 
MET   CE   C N N 293 
MET   OXT  O N N 294 
MET   H    H N N 295 
MET   H2   H N N 296 
MET   HA   H N N 297 
MET   HB2  H N N 298 
MET   HB3  H N N 299 
MET   HG2  H N N 300 
MET   HG3  H N N 301 
MET   HE1  H N N 302 
MET   HE2  H N N 303 
MET   HE3  H N N 304 
MET   HXT  H N N 305 
PHE   N    N N N 306 
PHE   CA   C N S 307 
PHE   C    C N N 308 
PHE   O    O N N 309 
PHE   CB   C N N 310 
PHE   CG   C Y N 311 
PHE   CD1  C Y N 312 
PHE   CD2  C Y N 313 
PHE   CE1  C Y N 314 
PHE   CE2  C Y N 315 
PHE   CZ   C Y N 316 
PHE   OXT  O N N 317 
PHE   H    H N N 318 
PHE   H2   H N N 319 
PHE   HA   H N N 320 
PHE   HB2  H N N 321 
PHE   HB3  H N N 322 
PHE   HD1  H N N 323 
PHE   HD2  H N N 324 
PHE   HE1  H N N 325 
PHE   HE2  H N N 326 
PHE   HZ   H N N 327 
PHE   HXT  H N N 328 
PRO   N    N N N 329 
PRO   CA   C N S 330 
PRO   C    C N N 331 
PRO   O    O N N 332 
PRO   CB   C N N 333 
PRO   CG   C N N 334 
PRO   CD   C N N 335 
PRO   OXT  O N N 336 
PRO   H    H N N 337 
PRO   HA   H N N 338 
PRO   HB2  H N N 339 
PRO   HB3  H N N 340 
PRO   HG2  H N N 341 
PRO   HG3  H N N 342 
PRO   HD2  H N N 343 
PRO   HD3  H N N 344 
PRO   HXT  H N N 345 
SER   N    N N N 346 
SER   CA   C N S 347 
SER   C    C N N 348 
SER   O    O N N 349 
SER   CB   C N N 350 
SER   OG   O N N 351 
SER   OXT  O N N 352 
SER   H    H N N 353 
SER   H2   H N N 354 
SER   HA   H N N 355 
SER   HB2  H N N 356 
SER   HB3  H N N 357 
SER   HG   H N N 358 
SER   HXT  H N N 359 
SO4   S    S N N 360 
SO4   O1   O N N 361 
SO4   O2   O N N 362 
SO4   O3   O N N 363 
SO4   O4   O N N 364 
THR   N    N N N 365 
THR   CA   C N S 366 
THR   C    C N N 367 
THR   O    O N N 368 
THR   CB   C N R 369 
THR   OG1  O N N 370 
THR   CG2  C N N 371 
THR   OXT  O N N 372 
THR   H    H N N 373 
THR   H2   H N N 374 
THR   HA   H N N 375 
THR   HB   H N N 376 
THR   HG1  H N N 377 
THR   HG21 H N N 378 
THR   HG22 H N N 379 
THR   HG23 H N N 380 
THR   HXT  H N N 381 
TRP   N    N N N 382 
TRP   CA   C N S 383 
TRP   C    C N N 384 
TRP   O    O N N 385 
TRP   CB   C N N 386 
TRP   CG   C Y N 387 
TRP   CD1  C Y N 388 
TRP   CD2  C Y N 389 
TRP   NE1  N Y N 390 
TRP   CE2  C Y N 391 
TRP   CE3  C Y N 392 
TRP   CZ2  C Y N 393 
TRP   CZ3  C Y N 394 
TRP   CH2  C Y N 395 
TRP   OXT  O N N 396 
TRP   H    H N N 397 
TRP   H2   H N N 398 
TRP   HA   H N N 399 
TRP   HB2  H N N 400 
TRP   HB3  H N N 401 
TRP   HD1  H N N 402 
TRP   HE1  H N N 403 
TRP   HE3  H N N 404 
TRP   HZ2  H N N 405 
TRP   HZ3  H N N 406 
TRP   HH2  H N N 407 
TRP   HXT  H N N 408 
TYR   N    N N N 409 
TYR   CA   C N S 410 
TYR   C    C N N 411 
TYR   O    O N N 412 
TYR   CB   C N N 413 
TYR   CG   C Y N 414 
TYR   CD1  C Y N 415 
TYR   CD2  C Y N 416 
TYR   CE1  C Y N 417 
TYR   CE2  C Y N 418 
TYR   CZ   C Y N 419 
TYR   OH   O N N 420 
TYR   OXT  O N N 421 
TYR   H    H N N 422 
TYR   H2   H N N 423 
TYR   HA   H N N 424 
TYR   HB2  H N N 425 
TYR   HB3  H N N 426 
TYR   HD1  H N N 427 
TYR   HD2  H N N 428 
TYR   HE1  H N N 429 
TYR   HE2  H N N 430 
TYR   HH   H N N 431 
TYR   HXT  H N N 432 
VAL   N    N N N 433 
VAL   CA   C N S 434 
VAL   C    C N N 435 
VAL   O    O N N 436 
VAL   CB   C N N 437 
VAL   CG1  C N N 438 
VAL   CG2  C N N 439 
VAL   OXT  O N N 440 
VAL   H    H N N 441 
VAL   H2   H N N 442 
VAL   HA   H N N 443 
VAL   HB   H N N 444 
VAL   HG11 H N N 445 
VAL   HG12 H N N 446 
VAL   HG13 H N N 447 
VAL   HG21 H N N 448 
VAL   HG22 H N N 449 
VAL   HG23 H N N 450 
VAL   HXT  H N N 451 
# 
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 
A1BXS C1  C2   sing N N 1   
A1BXS C2  C3   doub Y N 2   
A1BXS C3  C4   sing Y N 3   
A1BXS C4  C5   sing N N 4   
A1BXS C5  O1   sing N N 5   
A1BXS C4  C6   doub Y N 6   
A1BXS C6  C7   sing Y N 7   
A1BXS C7  C8   doub Y N 8   
A1BXS C8  C9   sing Y N 9   
A1BXS C9  C10  doub Y N 10  
A1BXS C10 C11  sing N N 11  
A1BXS C11 C12  sing N N 12  
A1BXS C12 O2   doub N N 13  
A1BXS C12 N1   sing N N 14  
A1BXS N1  C13  sing N N 15  
A1BXS C13 C14  sing N N 16  
A1BXS C14 C15  sing N N 17  
A1BXS C15 C16  sing N N 18  
A1BXS C16 N2   sing N N 19  
A1BXS C15 C17  sing N N 20  
A1BXS C10 C18  sing Y N 21  
A1BXS C18 N3   doub Y N 22  
A1BXS C2  N3   sing Y N 23  
A1BXS C6  C18  sing Y N 24  
A1BXS N1  C17  sing N N 25  
A1BXS C5  H6   sing N N 26  
A1BXS C5  H5   sing N N 27  
A1BXS C7  H8   sing N N 28  
A1BXS C8  H9   sing N N 29  
A1BXS C13 H14  sing N N 30  
A1BXS C13 H13  sing N N 31  
A1BXS C15 H17  sing N N 32  
A1BXS C17 H23  sing N N 33  
A1BXS C17 H22  sing N N 34  
A1BXS C1  H3   sing N N 35  
A1BXS C1  H1   sing N N 36  
A1BXS C1  H2   sing N N 37  
A1BXS C3  H4   sing N N 38  
A1BXS O1  H7   sing N N 39  
A1BXS C9  H10  sing N N 40  
A1BXS C11 H12  sing N N 41  
A1BXS C11 H11  sing N N 42  
A1BXS C14 H16  sing N N 43  
A1BXS C14 H15  sing N N 44  
A1BXS C16 H19  sing N N 45  
A1BXS C16 H18  sing N N 46  
A1BXS N2  H24  sing N N 47  
A1BXS N2  H20  sing N N 48  
ALA   N   CA   sing N N 49  
ALA   N   H    sing N N 50  
ALA   N   H2   sing N N 51  
ALA   CA  C    sing N N 52  
ALA   CA  CB   sing N N 53  
ALA   CA  HA   sing N N 54  
ALA   C   O    doub N N 55  
ALA   C   OXT  sing N N 56  
ALA   CB  HB1  sing N N 57  
ALA   CB  HB2  sing N N 58  
ALA   CB  HB3  sing N N 59  
ALA   OXT HXT  sing N N 60  
ARG   N   CA   sing N N 61  
ARG   N   H    sing N N 62  
ARG   N   H2   sing N N 63  
ARG   CA  C    sing N N 64  
ARG   CA  CB   sing N N 65  
ARG   CA  HA   sing N N 66  
ARG   C   O    doub N N 67  
ARG   C   OXT  sing N N 68  
ARG   CB  CG   sing N N 69  
ARG   CB  HB2  sing N N 70  
ARG   CB  HB3  sing N N 71  
ARG   CG  CD   sing N N 72  
ARG   CG  HG2  sing N N 73  
ARG   CG  HG3  sing N N 74  
ARG   CD  NE   sing N N 75  
ARG   CD  HD2  sing N N 76  
ARG   CD  HD3  sing N N 77  
ARG   NE  CZ   sing N N 78  
ARG   NE  HE   sing N N 79  
ARG   CZ  NH1  sing N N 80  
ARG   CZ  NH2  doub N N 81  
ARG   NH1 HH11 sing N N 82  
ARG   NH1 HH12 sing N N 83  
ARG   NH2 HH21 sing N N 84  
ARG   NH2 HH22 sing N N 85  
ARG   OXT HXT  sing N N 86  
ASN   N   CA   sing N N 87  
ASN   N   H    sing N N 88  
ASN   N   H2   sing N N 89  
ASN   CA  C    sing N N 90  
ASN   CA  CB   sing N N 91  
ASN   CA  HA   sing N N 92  
ASN   C   O    doub N N 93  
ASN   C   OXT  sing N N 94  
ASN   CB  CG   sing N N 95  
ASN   CB  HB2  sing N N 96  
ASN   CB  HB3  sing N N 97  
ASN   CG  OD1  doub N N 98  
ASN   CG  ND2  sing N N 99  
ASN   ND2 HD21 sing N N 100 
ASN   ND2 HD22 sing N N 101 
ASN   OXT HXT  sing N N 102 
ASP   N   CA   sing N N 103 
ASP   N   H    sing N N 104 
ASP   N   H2   sing N N 105 
ASP   CA  C    sing N N 106 
ASP   CA  CB   sing N N 107 
ASP   CA  HA   sing N N 108 
ASP   C   O    doub N N 109 
ASP   C   OXT  sing N N 110 
ASP   CB  CG   sing N N 111 
ASP   CB  HB2  sing N N 112 
ASP   CB  HB3  sing N N 113 
ASP   CG  OD1  doub N N 114 
ASP   CG  OD2  sing N N 115 
ASP   OD2 HD2  sing N N 116 
ASP   OXT HXT  sing N N 117 
CYS   N   CA   sing N N 118 
CYS   N   H    sing N N 119 
CYS   N   H2   sing N N 120 
CYS   CA  C    sing N N 121 
CYS   CA  CB   sing N N 122 
CYS   CA  HA   sing N N 123 
CYS   C   O    doub N N 124 
CYS   C   OXT  sing N N 125 
CYS   CB  SG   sing N N 126 
CYS   CB  HB2  sing N N 127 
CYS   CB  HB3  sing N N 128 
CYS   SG  HG   sing N N 129 
CYS   OXT HXT  sing N N 130 
DMS   S   O    doub N N 131 
DMS   S   C1   sing N N 132 
DMS   S   C2   sing N N 133 
DMS   C1  H11  sing N N 134 
DMS   C1  H12  sing N N 135 
DMS   C1  H13  sing N N 136 
DMS   C2  H21  sing N N 137 
DMS   C2  H22  sing N N 138 
DMS   C2  H23  sing N N 139 
GLN   N   CA   sing N N 140 
GLN   N   H    sing N N 141 
GLN   N   H2   sing N N 142 
GLN   CA  C    sing N N 143 
GLN   CA  CB   sing N N 144 
GLN   CA  HA   sing N N 145 
GLN   C   O    doub N N 146 
GLN   C   OXT  sing N N 147 
GLN   CB  CG   sing N N 148 
GLN   CB  HB2  sing N N 149 
GLN   CB  HB3  sing N N 150 
GLN   CG  CD   sing N N 151 
GLN   CG  HG2  sing N N 152 
GLN   CG  HG3  sing N N 153 
GLN   CD  OE1  doub N N 154 
GLN   CD  NE2  sing N N 155 
GLN   NE2 HE21 sing N N 156 
GLN   NE2 HE22 sing N N 157 
GLN   OXT HXT  sing N N 158 
GLU   N   CA   sing N N 159 
GLU   N   H    sing N N 160 
GLU   N   H2   sing N N 161 
GLU   CA  C    sing N N 162 
GLU   CA  CB   sing N N 163 
GLU   CA  HA   sing N N 164 
GLU   C   O    doub N N 165 
GLU   C   OXT  sing N N 166 
GLU   CB  CG   sing N N 167 
GLU   CB  HB2  sing N N 168 
GLU   CB  HB3  sing N N 169 
GLU   CG  CD   sing N N 170 
GLU   CG  HG2  sing N N 171 
GLU   CG  HG3  sing N N 172 
GLU   CD  OE1  doub N N 173 
GLU   CD  OE2  sing N N 174 
GLU   OE2 HE2  sing N N 175 
GLU   OXT HXT  sing N N 176 
GLY   N   CA   sing N N 177 
GLY   N   H    sing N N 178 
GLY   N   H2   sing N N 179 
GLY   CA  C    sing N N 180 
GLY   CA  HA2  sing N N 181 
GLY   CA  HA3  sing N N 182 
GLY   C   O    doub N N 183 
GLY   C   OXT  sing N N 184 
GLY   OXT HXT  sing N N 185 
HIS   N   CA   sing N N 186 
HIS   N   H    sing N N 187 
HIS   N   H2   sing N N 188 
HIS   CA  C    sing N N 189 
HIS   CA  CB   sing N N 190 
HIS   CA  HA   sing N N 191 
HIS   C   O    doub N N 192 
HIS   C   OXT  sing N N 193 
HIS   CB  CG   sing N N 194 
HIS   CB  HB2  sing N N 195 
HIS   CB  HB3  sing N N 196 
HIS   CG  ND1  sing Y N 197 
HIS   CG  CD2  doub Y N 198 
HIS   ND1 CE1  doub Y N 199 
HIS   ND1 HD1  sing N N 200 
HIS   CD2 NE2  sing Y N 201 
HIS   CD2 HD2  sing N N 202 
HIS   CE1 NE2  sing Y N 203 
HIS   CE1 HE1  sing N N 204 
HIS   NE2 HE2  sing N N 205 
HIS   OXT HXT  sing N N 206 
HOH   O   H1   sing N N 207 
HOH   O   H2   sing N N 208 
ILE   N   CA   sing N N 209 
ILE   N   H    sing N N 210 
ILE   N   H2   sing N N 211 
ILE   CA  C    sing N N 212 
ILE   CA  CB   sing N N 213 
ILE   CA  HA   sing N N 214 
ILE   C   O    doub N N 215 
ILE   C   OXT  sing N N 216 
ILE   CB  CG1  sing N N 217 
ILE   CB  CG2  sing N N 218 
ILE   CB  HB   sing N N 219 
ILE   CG1 CD1  sing N N 220 
ILE   CG1 HG12 sing N N 221 
ILE   CG1 HG13 sing N N 222 
ILE   CG2 HG21 sing N N 223 
ILE   CG2 HG22 sing N N 224 
ILE   CG2 HG23 sing N N 225 
ILE   CD1 HD11 sing N N 226 
ILE   CD1 HD12 sing N N 227 
ILE   CD1 HD13 sing N N 228 
ILE   OXT HXT  sing N N 229 
LEU   N   CA   sing N N 230 
LEU   N   H    sing N N 231 
LEU   N   H2   sing N N 232 
LEU   CA  C    sing N N 233 
LEU   CA  CB   sing N N 234 
LEU   CA  HA   sing N N 235 
LEU   C   O    doub N N 236 
LEU   C   OXT  sing N N 237 
LEU   CB  CG   sing N N 238 
LEU   CB  HB2  sing N N 239 
LEU   CB  HB3  sing N N 240 
LEU   CG  CD1  sing N N 241 
LEU   CG  CD2  sing N N 242 
LEU   CG  HG   sing N N 243 
LEU   CD1 HD11 sing N N 244 
LEU   CD1 HD12 sing N N 245 
LEU   CD1 HD13 sing N N 246 
LEU   CD2 HD21 sing N N 247 
LEU   CD2 HD22 sing N N 248 
LEU   CD2 HD23 sing N N 249 
LEU   OXT HXT  sing N N 250 
LYS   N   CA   sing N N 251 
LYS   N   H    sing N N 252 
LYS   N   H2   sing N N 253 
LYS   CA  C    sing N N 254 
LYS   CA  CB   sing N N 255 
LYS   CA  HA   sing N N 256 
LYS   C   O    doub N N 257 
LYS   C   OXT  sing N N 258 
LYS   CB  CG   sing N N 259 
LYS   CB  HB2  sing N N 260 
LYS   CB  HB3  sing N N 261 
LYS   CG  CD   sing N N 262 
LYS   CG  HG2  sing N N 263 
LYS   CG  HG3  sing N N 264 
LYS   CD  CE   sing N N 265 
LYS   CD  HD2  sing N N 266 
LYS   CD  HD3  sing N N 267 
LYS   CE  NZ   sing N N 268 
LYS   CE  HE2  sing N N 269 
LYS   CE  HE3  sing N N 270 
LYS   NZ  HZ1  sing N N 271 
LYS   NZ  HZ2  sing N N 272 
LYS   NZ  HZ3  sing N N 273 
LYS   OXT HXT  sing N N 274 
MET   N   CA   sing N N 275 
MET   N   H    sing N N 276 
MET   N   H2   sing N N 277 
MET   CA  C    sing N N 278 
MET   CA  CB   sing N N 279 
MET   CA  HA   sing N N 280 
MET   C   O    doub N N 281 
MET   C   OXT  sing N N 282 
MET   CB  CG   sing N N 283 
MET   CB  HB2  sing N N 284 
MET   CB  HB3  sing N N 285 
MET   CG  SD   sing N N 286 
MET   CG  HG2  sing N N 287 
MET   CG  HG3  sing N N 288 
MET   SD  CE   sing N N 289 
MET   CE  HE1  sing N N 290 
MET   CE  HE2  sing N N 291 
MET   CE  HE3  sing N N 292 
MET   OXT HXT  sing N N 293 
PHE   N   CA   sing N N 294 
PHE   N   H    sing N N 295 
PHE   N   H2   sing N N 296 
PHE   CA  C    sing N N 297 
PHE   CA  CB   sing N N 298 
PHE   CA  HA   sing N N 299 
PHE   C   O    doub N N 300 
PHE   C   OXT  sing N N 301 
PHE   CB  CG   sing N N 302 
PHE   CB  HB2  sing N N 303 
PHE   CB  HB3  sing N N 304 
PHE   CG  CD1  doub Y N 305 
PHE   CG  CD2  sing Y N 306 
PHE   CD1 CE1  sing Y N 307 
PHE   CD1 HD1  sing N N 308 
PHE   CD2 CE2  doub Y N 309 
PHE   CD2 HD2  sing N N 310 
PHE   CE1 CZ   doub Y N 311 
PHE   CE1 HE1  sing N N 312 
PHE   CE2 CZ   sing Y N 313 
PHE   CE2 HE2  sing N N 314 
PHE   CZ  HZ   sing N N 315 
PHE   OXT HXT  sing N N 316 
PRO   N   CA   sing N N 317 
PRO   N   CD   sing N N 318 
PRO   N   H    sing N N 319 
PRO   CA  C    sing N N 320 
PRO   CA  CB   sing N N 321 
PRO   CA  HA   sing N N 322 
PRO   C   O    doub N N 323 
PRO   C   OXT  sing N N 324 
PRO   CB  CG   sing N N 325 
PRO   CB  HB2  sing N N 326 
PRO   CB  HB3  sing N N 327 
PRO   CG  CD   sing N N 328 
PRO   CG  HG2  sing N N 329 
PRO   CG  HG3  sing N N 330 
PRO   CD  HD2  sing N N 331 
PRO   CD  HD3  sing N N 332 
PRO   OXT HXT  sing N N 333 
SER   N   CA   sing N N 334 
SER   N   H    sing N N 335 
SER   N   H2   sing N N 336 
SER   CA  C    sing N N 337 
SER   CA  CB   sing N N 338 
SER   CA  HA   sing N N 339 
SER   C   O    doub N N 340 
SER   C   OXT  sing N N 341 
SER   CB  OG   sing N N 342 
SER   CB  HB2  sing N N 343 
SER   CB  HB3  sing N N 344 
SER   OG  HG   sing N N 345 
SER   OXT HXT  sing N N 346 
SO4   S   O1   doub N N 347 
SO4   S   O2   doub N N 348 
SO4   S   O3   sing N N 349 
SO4   S   O4   sing N N 350 
THR   N   CA   sing N N 351 
THR   N   H    sing N N 352 
THR   N   H2   sing N N 353 
THR   CA  C    sing N N 354 
THR   CA  CB   sing N N 355 
THR   CA  HA   sing N N 356 
THR   C   O    doub N N 357 
THR   C   OXT  sing N N 358 
THR   CB  OG1  sing N N 359 
THR   CB  CG2  sing N N 360 
THR   CB  HB   sing N N 361 
THR   OG1 HG1  sing N N 362 
THR   CG2 HG21 sing N N 363 
THR   CG2 HG22 sing N N 364 
THR   CG2 HG23 sing N N 365 
THR   OXT HXT  sing N N 366 
TRP   N   CA   sing N N 367 
TRP   N   H    sing N N 368 
TRP   N   H2   sing N N 369 
TRP   CA  C    sing N N 370 
TRP   CA  CB   sing N N 371 
TRP   CA  HA   sing N N 372 
TRP   C   O    doub N N 373 
TRP   C   OXT  sing N N 374 
TRP   CB  CG   sing N N 375 
TRP   CB  HB2  sing N N 376 
TRP   CB  HB3  sing N N 377 
TRP   CG  CD1  doub Y N 378 
TRP   CG  CD2  sing Y N 379 
TRP   CD1 NE1  sing Y N 380 
TRP   CD1 HD1  sing N N 381 
TRP   CD2 CE2  doub Y N 382 
TRP   CD2 CE3  sing Y N 383 
TRP   NE1 CE2  sing Y N 384 
TRP   NE1 HE1  sing N N 385 
TRP   CE2 CZ2  sing Y N 386 
TRP   CE3 CZ3  doub Y N 387 
TRP   CE3 HE3  sing N N 388 
TRP   CZ2 CH2  doub Y N 389 
TRP   CZ2 HZ2  sing N N 390 
TRP   CZ3 CH2  sing Y N 391 
TRP   CZ3 HZ3  sing N N 392 
TRP   CH2 HH2  sing N N 393 
TRP   OXT HXT  sing N N 394 
TYR   N   CA   sing N N 395 
TYR   N   H    sing N N 396 
TYR   N   H2   sing N N 397 
TYR   CA  C    sing N N 398 
TYR   CA  CB   sing N N 399 
TYR   CA  HA   sing N N 400 
TYR   C   O    doub N N 401 
TYR   C   OXT  sing N N 402 
TYR   CB  CG   sing N N 403 
TYR   CB  HB2  sing N N 404 
TYR   CB  HB3  sing N N 405 
TYR   CG  CD1  doub Y N 406 
TYR   CG  CD2  sing Y N 407 
TYR   CD1 CE1  sing Y N 408 
TYR   CD1 HD1  sing N N 409 
TYR   CD2 CE2  doub Y N 410 
TYR   CD2 HD2  sing N N 411 
TYR   CE1 CZ   doub Y N 412 
TYR   CE1 HE1  sing N N 413 
TYR   CE2 CZ   sing Y N 414 
TYR   CE2 HE2  sing N N 415 
TYR   CZ  OH   sing N N 416 
TYR   OH  HH   sing N N 417 
TYR   OXT HXT  sing N N 418 
VAL   N   CA   sing N N 419 
VAL   N   H    sing N N 420 
VAL   N   H2   sing N N 421 
VAL   CA  C    sing N N 422 
VAL   CA  CB   sing N N 423 
VAL   CA  HA   sing N N 424 
VAL   C   O    doub N N 425 
VAL   C   OXT  sing N N 426 
VAL   CB  CG1  sing N N 427 
VAL   CB  CG2  sing N N 428 
VAL   CB  HB   sing N N 429 
VAL   CG1 HG11 sing N N 430 
VAL   CG1 HG12 sing N N 431 
VAL   CG1 HG13 sing N N 432 
VAL   CG2 HG21 sing N N 433 
VAL   CG2 HG22 sing N N 434 
VAL   CG2 HG23 sing N N 435 
VAL   OXT HXT  sing N N 436 
# 
_pdbx_audit_support.funding_organization   'Australian Research Council (ARC)' 
_pdbx_audit_support.country                Australia 
_pdbx_audit_support.grant_number           IC180100021 
_pdbx_audit_support.ordinal                1 
# 
_pdbx_deposit_group.group_id            G_1002340 
_pdbx_deposit_group.group_description   
'Crystallographic fragment screen of ZIKV NS2B-NS3 protease at the XChem facility of Diamond Light Source beamline I04-1' 
_pdbx_deposit_group.group_title         'PanDDA analysis group deposition' 
_pdbx_deposit_group.group_type          'changed state' 
# 
_pdbx_initial_refinement_model.accession_code   8PN6 
_pdbx_initial_refinement_model.details          ? 
_pdbx_initial_refinement_model.entity_id_list   ? 
_pdbx_initial_refinement_model.id               1 
_pdbx_initial_refinement_model.source_name      PDB 
_pdbx_initial_refinement_model.type             'experimental model' 
# 
_atom_sites.entry_id                    7I21 
_atom_sites.fract_transf_matrix[1][1]   0.023485 
_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]   0.023485 
_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]   0.004622 
_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   ? -20.922 19.210  -7.367  1.00 67.85  ? 50  ASP   A N   1 
ATOM   2    C CA  . ASP   A 1 7   ? -22.185 18.446  -7.453  1.00 69.11  ? 50  ASP   A CA  1 
ATOM   3    C C   . ASP   A 1 7   ? -22.292 17.839  -8.861  1.00 67.22  ? 50  ASP   A C   1 
ATOM   4    O O   . ASP   A 1 7   ? -21.913 18.505  -9.855  1.00 67.13  ? 50  ASP   A O   1 
ATOM   5    C CB  . ASP   A 1 7   ? -23.383 19.316  -7.067  1.00 72.96  ? 50  ASP   A CB  1 
ATOM   6    C CG  . ASP   A 1 7   ? -24.711 18.576  -7.022  1.00 80.39  ? 50  ASP   A CG  1 
ATOM   7    O OD1 . ASP   A 1 7   ? -25.047 18.014  -5.941  1.00 79.07  ? 50  ASP   A OD1 1 
ATOM   8    O OD2 . ASP   A 1 7   ? -25.406 18.569  -8.071  1.00 89.86  ? 50  ASP   A OD2 1 
ATOM   9    N N   . MET   A 1 8   ? -22.769 16.598  -8.922  1.00 57.54  ? 51  MET   A N   1 
ATOM   10   C CA  . MET   A 1 8   ? -22.580 15.681  -10.070 1.00 56.87  ? 51  MET   A CA  1 
ATOM   11   C C   . MET   A 1 8   ? -23.952 15.366  -10.617 1.00 44.76  ? 51  MET   A C   1 
ATOM   12   O O   . MET   A 1 8   ? -24.854 15.204  -9.800  1.00 43.97  ? 51  MET   A O   1 
ATOM   13   C CB  . MET   A 1 8   ? -21.927 14.365  -9.643  1.00 58.21  ? 51  MET   A CB  1 
ATOM   14   C CG  . MET   A 1 8   ? -20.446 14.471  -9.425  1.00 57.88  ? 51  MET   A CG  1 
ATOM   15   S SD  . MET   A 1 8   ? -19.715 12.823  -9.275  1.00 59.93  ? 51  MET   A SD  1 
ATOM   16   C CE  . MET   A 1 8   ? -18.027 13.300  -8.908  1.00 61.87  ? 51  MET   A CE  1 
ATOM   17   N N   . TYR   A 1 9   ? -24.081 15.238  -11.929 1.00 42.67  ? 52  TYR   A N   1 
ATOM   18   C CA  . TYR   A 1 9   ? -25.388 14.970  -12.579 1.00 43.72  ? 52  TYR   A CA  1 
ATOM   19   C C   . TYR   A 1 9   ? -25.169 14.003  -13.746 1.00 41.80  ? 52  TYR   A C   1 
ATOM   20   O O   . TYR   A 1 9   ? -24.015 13.855  -14.207 1.00 37.09  ? 52  TYR   A O   1 
ATOM   21   C CB  . TYR   A 1 9   ? -26.059 16.301  -12.952 1.00 43.95  ? 52  TYR   A CB  1 
ATOM   22   C CG  . TYR   A 1 9   ? -25.350 17.071  -14.037 1.00 39.91  ? 52  TYR   A CG  1 
ATOM   23   C CD1 . TYR   A 1 9   ? -24.300 17.915  -13.731 1.00 42.54  ? 52  TYR   A CD1 1 
ATOM   24   C CD2 . TYR   A 1 9   ? -25.702 16.921  -15.372 1.00 40.98  ? 52  TYR   A CD2 1 
ATOM   25   C CE1 . TYR   A 1 9   ? -23.611 18.604  -14.717 1.00 38.34  ? 52  TYR   A CE1 1 
ATOM   26   C CE2 . TYR   A 1 9   ? -25.018 17.594  -16.374 1.00 41.78  ? 52  TYR   A CE2 1 
ATOM   27   C CZ  . TYR   A 1 9   ? -23.972 18.437  -16.038 1.00 40.51  ? 52  TYR   A CZ  1 
ATOM   28   O OH  . TYR   A 1 9   ? -23.297 19.115  -17.004 1.00 48.05  ? 52  TYR   A OH  1 
ATOM   29   N N   . ILE   A 1 10  ? -26.257 13.372  -14.199 1.00 44.23  ? 53  ILE   A N   1 
ATOM   30   C CA  . ILE   A 1 10  ? -26.249 12.358  -15.295 1.00 47.12  ? 53  ILE   A CA  1 
ATOM   31   C C   . ILE   A 1 10  ? -27.091 12.833  -16.500 1.00 46.90  ? 53  ILE   A C   1 
ATOM   32   O O   . ILE   A 1 10  ? -28.158 13.451  -16.304 1.00 46.52  ? 53  ILE   A O   1 
ATOM   33   C CB  . ILE   A 1 10  ? -26.706 10.980  -14.757 1.00 45.28  ? 53  ILE   A CB  1 
ATOM   34   C CG1 . ILE   A 1 10  ? -28.170 10.964  -14.337 1.00 46.79  ? 53  ILE   A CG1 1 
ATOM   35   C CG2 . ILE   A 1 10  ? -25.801 10.511  -13.621 1.00 46.93  ? 53  ILE   A CG2 1 
ATOM   36   C CD1 . ILE   A 1 10  ? -28.650 9.598   -13.920 1.00 50.45  ? 53  ILE   A CD1 1 
ATOM   37   N N   . GLU   A 1 11  ? -26.626 12.522  -17.712 1.00 48.07  ? 54  GLU   A N   1 
ATOM   38   C CA  . GLU   A 1 11  ? -27.339 12.735  -19.007 1.00 49.23  ? 54  GLU   A CA  1 
ATOM   39   C C   . GLU   A 1 11  ? -27.311 11.435  -19.817 1.00 46.14  ? 54  GLU   A C   1 
ATOM   40   O O   . GLU   A 1 11  ? -26.234 10.803  -19.918 1.00 39.63  ? 54  GLU   A O   1 
ATOM   41   C CB  . GLU   A 1 11  ? -26.664 13.824  -19.830 1.00 47.64  ? 54  GLU   A CB  1 
ATOM   42   C CG  . GLU   A 1 11  ? -26.614 15.170  -19.151 1.00 54.13  ? 54  GLU   A CG  1 
ATOM   43   C CD  . GLU   A 1 11  ? -25.743 16.179  -19.884 1.00 61.52  ? 54  GLU   A CD  1 
ATOM   44   O OE1 . GLU   A 1 11  ? -24.820 15.761  -20.620 1.00 59.16  ? 54  GLU   A OE1 1 
ATOM   45   O OE2 . GLU   A 1 11  ? -25.990 17.384  -19.719 1.00 78.18  ? 54  GLU   A OE2 1 
ATOM   46   N N   . ARG   A 1 12  ? -28.455 11.021  -20.355 1.00 46.24  ? 55  ARG   A N   1 
ATOM   47   C CA  . ARG   A 1 12  ? -28.536 9.772   -21.150 1.00 42.92  ? 55  ARG   A CA  1 
ATOM   48   C C   . ARG   A 1 12  ? -27.597 9.878   -22.354 1.00 45.29  ? 55  ARG   A C   1 
ATOM   49   O O   . ARG   A 1 12  ? -27.390 11.016  -22.850 1.00 47.00  ? 55  ARG   A O   1 
ATOM   50   C CB  . ARG   A 1 12  ? -29.984 9.509   -21.534 1.00 43.95  ? 55  ARG   A CB  1 
ATOM   51   C CG  . ARG   A 1 12  ? -30.222 8.090   -22.012 1.00 48.02  ? 55  ARG   A CG  1 
ATOM   52   C CD  . ARG   A 1 12  ? -31.671 7.664   -21.895 1.00 49.53  ? 55  ARG   A CD  1 
ATOM   53   N NE  . ARG   A 1 12  ? -31.835 6.260   -22.192 1.00 51.75  ? 55  ARG   A NE  1 
ATOM   54   C CZ  . ARG   A 1 12  ? -31.729 5.740   -23.412 1.00 57.28  ? 55  ARG   A CZ  1 
ATOM   55   N NH1 . ARG   A 1 12  ? -31.488 6.514   -24.463 1.00 63.14  ? 55  ARG   A NH1 1 
ATOM   56   N NH2 . ARG   A 1 12  ? -31.852 4.434   -23.577 1.00 58.38  ? 55  ARG   A NH2 1 
ATOM   57   N N   . ALA   A 1 13  ? -26.950 8.770   -22.758 1.00 50.73  ? 56  ALA   A N   1 
ATOM   58   C CA  . ALA   A 1 13  ? -25.966 8.762   -23.887 1.00 43.44  ? 56  ALA   A CA  1 
ATOM   59   C C   . ALA   A 1 13  ? -26.292 7.699   -24.933 1.00 37.41  ? 56  ALA   A C   1 
ATOM   60   O O   . ALA   A 1 13  ? -25.675 7.739   -25.991 1.00 42.64  ? 56  ALA   A O   1 
ATOM   61   C CB  . ALA   A 1 13  ? -24.540 8.625   -23.397 1.00 48.82  ? 56  ALA   A CB  1 
ATOM   62   N N   . GLY   A 1 14  ? -27.216 6.778   -24.667 1.00 33.09  ? 57  GLY   A N   1 
ATOM   63   C CA  . GLY   A 1 14  ? -27.630 5.803   -25.680 1.00 30.66  ? 57  GLY   A CA  1 
ATOM   64   C C   . GLY   A 1 14  ? -28.325 4.629   -25.047 1.00 39.25  ? 57  GLY   A C   1 
ATOM   65   O O   . GLY   A 1 14  ? -28.328 4.598   -23.778 1.00 41.53  ? 57  GLY   A O   1 
ATOM   66   N N   . ASP   A 1 15  ? -28.882 3.738   -25.892 1.00 40.72  ? 58  ASP   A N   1 
ATOM   67   C CA  . ASP   A 1 15  ? -29.377 2.380   -25.539 1.00 45.05  ? 58  ASP   A CA  1 
ATOM   68   C C   . ASP   A 1 15  ? -28.195 1.430   -25.355 1.00 52.11  ? 58  ASP   A C   1 
ATOM   69   O O   . ASP   A 1 15  ? -27.081 1.729   -25.849 1.00 49.73  ? 58  ASP   A O   1 
ATOM   70   C CB  . ASP   A 1 15  ? -30.262 1.748   -26.609 1.00 48.05  ? 58  ASP   A CB  1 
ATOM   71   C CG  . ASP   A 1 15  ? -31.537 2.525   -26.790 1.00 55.16  ? 58  ASP   A CG  1 
ATOM   72   O OD1 . ASP   A 1 15  ? -31.682 3.490   -26.046 1.00 51.71  ? 58  ASP   A OD1 1 
ATOM   73   O OD2 . ASP   A 1 15  ? -32.354 2.170   -27.678 1.00 58.58  ? 58  ASP   A OD2 1 
ATOM   74   N N   . ILE   A 1 16  ? -28.440 0.334   -24.639 1.00 49.47  ? 59  ILE   A N   1 
ATOM   75   C CA  . ILE   A 1 16  ? -27.429 -0.736  -24.446 1.00 51.04  ? 59  ILE   A CA  1 
ATOM   76   C C   . ILE   A 1 16  ? -27.837 -1.862  -25.388 1.00 45.25  ? 59  ILE   A C   1 
ATOM   77   O O   . ILE   A 1 16  ? -28.729 -2.634  -25.053 1.00 42.63  ? 59  ILE   A O   1 
ATOM   78   C CB  . ILE   A 1 16  ? -27.346 -1.128  -22.966 1.00 55.66  ? 59  ILE   A CB  1 
ATOM   79   C CG1 . ILE   A 1 16  ? -26.610 -0.024  -22.197 1.00 50.48  ? 59  ILE   A CG1 1 
ATOM   80   C CG2 . ILE   A 1 16  ? -26.700 -2.500  -22.811 1.00 52.30  ? 59  ILE   A CG2 1 
ATOM   81   C CD1 . ILE   A 1 16  ? -26.927 0.012   -20.730 1.00 58.41  ? 59  ILE   A CD1 1 
ATOM   82   N N   A THR   A 1 17  ? -27.180 -1.910  -26.555 0.25 45.91  ? 60  THR   A N   1 
ATOM   83   N N   B THR   A 1 17  ? -27.204 -1.926  -26.561 0.25 45.68  ? 60  THR   A N   1 
ATOM   84   N N   C THR   A 1 17  ? -27.180 -1.910  -26.555 0.25 45.91  ? 60  THR   A N   1 
ATOM   85   N N   D THR   A 1 17  ? -27.204 -1.926  -26.561 0.25 45.68  ? 60  THR   A N   1 
ATOM   86   C CA  A THR   A 1 17  ? -27.485 -2.814  -27.698 0.25 45.70  ? 60  THR   A CA  1 
ATOM   87   C CA  B THR   A 1 17  ? -27.530 -2.913  -27.622 0.25 45.36  ? 60  THR   A CA  1 
ATOM   88   C CA  C THR   A 1 17  ? -27.485 -2.814  -27.698 0.25 45.70  ? 60  THR   A CA  1 
ATOM   89   C CA  D THR   A 1 17  ? -27.530 -2.913  -27.622 0.25 45.36  ? 60  THR   A CA  1 
ATOM   90   C C   A THR   A 1 17  ? -26.186 -3.363  -28.298 0.25 44.71  ? 60  THR   A C   1 
ATOM   91   C C   B THR   A 1 17  ? -26.242 -3.361  -28.320 0.25 44.61  ? 60  THR   A C   1 
ATOM   92   C C   C THR   A 1 17  ? -26.186 -3.363  -28.298 0.25 44.71  ? 60  THR   A C   1 
ATOM   93   C C   D THR   A 1 17  ? -26.242 -3.361  -28.320 0.25 44.61  ? 60  THR   A C   1 
ATOM   94   O O   A THR   A 1 17  ? -25.227 -2.576  -28.471 0.25 39.60  ? 60  THR   A O   1 
ATOM   95   O O   B THR   A 1 17  ? -25.342 -2.519  -28.540 0.25 39.65  ? 60  THR   A O   1 
ATOM   96   O O   C THR   A 1 17  ? -25.227 -2.576  -28.471 0.25 39.60  ? 60  THR   A O   1 
ATOM   97   O O   D THR   A 1 17  ? -25.342 -2.519  -28.540 0.25 39.65  ? 60  THR   A O   1 
ATOM   98   C CB  A THR   A 1 17  ? -28.278 -2.086  -28.794 0.25 44.95  ? 60  THR   A CB  1 
ATOM   99   C CB  B THR   A 1 17  ? -28.598 -2.356  -28.576 0.25 44.67  ? 60  THR   A CB  1 
ATOM   100  C CB  C THR   A 1 17  ? -28.278 -2.086  -28.794 0.25 44.95  ? 60  THR   A CB  1 
ATOM   101  C CB  D THR   A 1 17  ? -28.598 -2.356  -28.576 0.25 44.67  ? 60  THR   A CB  1 
ATOM   102  O OG1 A THR   A 1 17  ? -27.389 -1.195  -29.465 0.25 42.71  ? 60  THR   A OG1 1 
ATOM   103  O OG1 B THR   A 1 17  ? -29.878 -2.665  -28.023 0.25 43.30  ? 60  THR   A OG1 1 
ATOM   104  O OG1 C THR   A 1 17  ? -27.389 -1.195  -29.465 0.25 42.71  ? 60  THR   A OG1 1 
ATOM   105  O OG1 D THR   A 1 17  ? -29.878 -2.665  -28.023 0.25 43.30  ? 60  THR   A OG1 1 
ATOM   106  C CG2 A THR   A 1 17  ? -29.460 -1.312  -28.254 0.25 45.32  ? 60  THR   A CG2 1 
ATOM   107  C CG2 B THR   A 1 17  ? -28.521 -2.933  -29.970 0.25 42.57  ? 60  THR   A CG2 1 
ATOM   108  C CG2 C THR   A 1 17  ? -29.460 -1.312  -28.254 0.25 45.32  ? 60  THR   A CG2 1 
ATOM   109  C CG2 D THR   A 1 17  ? -28.521 -2.933  -29.970 0.25 42.57  ? 60  THR   A CG2 1 
ATOM   110  N N   . TRP   A 1 18  ? -26.166 -4.660  -28.616 1.00 45.94  ? 61  TRP   A N   1 
ATOM   111  C CA  . TRP   A 1 18  ? -25.094 -5.260  -29.444 1.00 57.35  ? 61  TRP   A CA  1 
ATOM   112  C C   . TRP   A 1 18  ? -25.262 -4.684  -30.857 1.00 60.59  ? 61  TRP   A C   1 
ATOM   113  O O   . TRP   A 1 18  ? -26.404 -4.695  -31.319 1.00 54.00  ? 61  TRP   A O   1 
ATOM   114  C CB  . TRP   A 1 18  ? -25.252 -6.785  -29.414 1.00 65.15  ? 61  TRP   A CB  1 
ATOM   115  C CG  . TRP   A 1 18  ? -24.209 -7.528  -30.187 1.00 78.71  ? 61  TRP   A CG  1 
ATOM   116  C CD1 . TRP   A 1 18  ? -24.316 -7.992  -31.465 1.00 79.44  ? 61  TRP   A CD1 1 
ATOM   117  C CD2 . TRP   A 1 18  ? -22.899 -7.906  -29.722 1.00 83.75  ? 61  TRP   A CD2 1 
ATOM   118  N NE1 . TRP   A 1 18  ? -23.159 -8.622  -31.829 1.00 89.32  ? 61  TRP   A NE1 1 
ATOM   119  C CE2 . TRP   A 1 18  ? -22.275 -8.594  -30.781 1.00 89.15  ? 61  TRP   A CE2 1 
ATOM   120  C CE3 . TRP   A 1 18  ? -22.197 -7.739  -28.523 1.00 82.10  ? 61  TRP   A CE3 1 
ATOM   121  C CZ2 . TRP   A 1 18  ? -20.980 -9.101  -30.672 1.00 88.37  ? 61  TRP   A CZ2 1 
ATOM   122  C CZ3 . TRP   A 1 18  ? -20.919 -8.240  -28.417 1.00 80.67  ? 61  TRP   A CZ3 1 
ATOM   123  C CH2 . TRP   A 1 18  ? -20.320 -8.912  -29.478 1.00 81.91  ? 61  TRP   A CH2 1 
ATOM   124  N N   . GLU   A 1 19  ? -24.203 -4.160  -31.486 1.00 65.11  ? 62  GLU   A N   1 
ATOM   125  C CA  . GLU   A 1 19  ? -24.259 -3.579  -32.856 1.00 75.76  ? 62  GLU   A CA  1 
ATOM   126  C C   . GLU   A 1 19  ? -23.497 -4.472  -33.845 1.00 76.12  ? 62  GLU   A C   1 
ATOM   127  O O   . GLU   A 1 19  ? -22.260 -4.311  -33.928 1.00 73.90  ? 62  GLU   A O   1 
ATOM   128  C CB  . GLU   A 1 19  ? -23.676 -2.164  -32.880 1.00 88.44  ? 62  GLU   A CB  1 
ATOM   129  C CG  . GLU   A 1 19  ? -24.408 -1.176  -31.973 1.00 108.80 ? 62  GLU   A CG  1 
ATOM   130  C CD  . GLU   A 1 19  ? -25.765 -0.668  -32.444 1.00 119.53 ? 62  GLU   A CD  1 
ATOM   131  O OE1 . GLU   A 1 19  ? -25.792 0.189   -33.361 1.00 115.25 ? 62  GLU   A OE1 1 
ATOM   132  O OE2 . GLU   A 1 19  ? -26.792 -1.116  -31.884 1.00 124.68 ? 62  GLU   A OE2 1 
ATOM   133  N N   . LYS   A 1 20  ? -24.206 -5.345  -34.581 1.00 76.73  ? 63  LYS   A N   1 
ATOM   134  C CA  . LYS   A 1 20  ? -23.645 -6.194  -35.677 1.00 76.04  ? 63  LYS   A CA  1 
ATOM   135  C C   . LYS   A 1 20  ? -22.885 -5.290  -36.641 1.00 71.95  ? 63  LYS   A C   1 
ATOM   136  O O   . LYS   A 1 20  ? -23.443 -4.271  -37.054 1.00 79.87  ? 63  LYS   A O   1 
ATOM   137  C CB  . LYS   A 1 20  ? -24.731 -6.929  -36.466 1.00 79.28  ? 63  LYS   A CB  1 
ATOM   138  C CG  . LYS   A 1 20  ? -24.868 -8.399  -36.120 1.00 90.53  ? 63  LYS   A CG  1 
ATOM   139  C CD  . LYS   A 1 20  ? -26.065 -9.080  -36.743 1.00 100.22 ? 63  LYS   A CD  1 
ATOM   140  C CE  . LYS   A 1 20  ? -26.128 -10.556 -36.400 1.00 104.20 ? 63  LYS   A CE  1 
ATOM   141  N NZ  . LYS   A 1 20  ? -27.465 -11.122 -36.688 1.00 103.93 ? 63  LYS   A NZ  1 
ATOM   142  N N   A ASP   A 1 21  ? -21.652 -5.681  -36.988 0.25 72.91  ? 64  ASP   A N   1 
ATOM   143  N N   B ASP   A 1 21  ? -21.652 -5.681  -36.988 0.25 72.91  ? 64  ASP   A N   1 
ATOM   144  N N   C ASP   A 1 21  ? -21.644 -5.659  -36.973 0.25 73.37  ? 64  ASP   A N   1 
ATOM   145  N N   D ASP   A 1 21  ? -21.644 -5.659  -36.973 0.25 73.37  ? 64  ASP   A N   1 
ATOM   146  C CA  A ASP   A 1 21  ? -20.707 -4.933  -37.865 0.25 76.94  ? 64  ASP   A CA  1 
ATOM   147  C CA  B ASP   A 1 21  ? -20.707 -4.933  -37.865 0.25 76.94  ? 64  ASP   A CA  1 
ATOM   148  C CA  C ASP   A 1 21  ? -20.741 -4.902  -37.883 0.25 77.79  ? 64  ASP   A CA  1 
ATOM   149  C CA  D ASP   A 1 21  ? -20.741 -4.902  -37.883 0.25 77.79  ? 64  ASP   A CA  1 
ATOM   150  C C   A ASP   A 1 21  ? -20.299 -3.626  -37.169 0.25 74.70  ? 64  ASP   A C   1 
ATOM   151  C C   B ASP   A 1 21  ? -20.299 -3.626  -37.169 0.25 74.70  ? 64  ASP   A C   1 
ATOM   152  C C   C ASP   A 1 21  ? -20.278 -3.614  -37.183 0.25 75.17  ? 64  ASP   A C   1 
ATOM   153  C C   D ASP   A 1 21  ? -20.278 -3.614  -37.183 0.25 75.17  ? 64  ASP   A C   1 
ATOM   154  O O   A ASP   A 1 21  ? -20.664 -2.546  -37.677 0.25 73.75  ? 64  ASP   A O   1 
ATOM   155  O O   B ASP   A 1 21  ? -20.664 -2.546  -37.677 0.25 73.75  ? 64  ASP   A O   1 
ATOM   156  O O   C ASP   A 1 21  ? -20.580 -2.524  -37.709 0.25 74.22  ? 64  ASP   A O   1 
ATOM   157  O O   D ASP   A 1 21  ? -20.580 -2.524  -37.709 0.25 74.22  ? 64  ASP   A O   1 
ATOM   158  C CB  A ASP   A 1 21  ? -21.285 -4.689  -39.267 0.25 79.91  ? 64  ASP   A CB  1 
ATOM   159  C CB  B ASP   A 1 21  ? -21.285 -4.689  -39.267 0.25 79.91  ? 64  ASP   A CB  1 
ATOM   160  C CB  C ASP   A 1 21  ? -21.413 -4.582  -39.228 0.25 81.28  ? 64  ASP   A CB  1 
ATOM   161  C CB  D ASP   A 1 21  ? -21.413 -4.582  -39.228 0.25 81.28  ? 64  ASP   A CB  1 
ATOM   162  C CG  A ASP   A 1 21  ? -21.233 -5.903  -40.186 0.25 80.65  ? 64  ASP   A CG  1 
ATOM   163  C CG  B ASP   A 1 21  ? -21.233 -5.903  -40.186 0.25 80.65  ? 64  ASP   A CG  1 
ATOM   164  C CG  C ASP   A 1 21  ? -22.273 -5.696  -39.814 0.25 81.93  ? 64  ASP   A CG  1 
ATOM   165  C CG  D ASP   A 1 21  ? -22.273 -5.696  -39.814 0.25 81.93  ? 64  ASP   A CG  1 
ATOM   166  O OD1 A ASP   A 1 21  ? -20.141 -6.179  -40.736 0.25 76.72  ? 64  ASP   A OD1 1 
ATOM   167  O OD1 B ASP   A 1 21  ? -20.141 -6.179  -40.736 0.25 76.72  ? 64  ASP   A OD1 1 
ATOM   168  O OD1 C ASP   A 1 21  ? -22.037 -6.876  -39.473 0.25 84.45  ? 64  ASP   A OD1 1 
ATOM   169  O OD1 D ASP   A 1 21  ? -22.037 -6.876  -39.473 0.25 84.45  ? 64  ASP   A OD1 1 
ATOM   170  O OD2 A ASP   A 1 21  ? -22.286 -6.567  -40.346 0.25 79.20  ? 64  ASP   A OD2 1 
ATOM   171  O OD2 B ASP   A 1 21  ? -22.286 -6.567  -40.346 0.25 79.20  ? 64  ASP   A OD2 1 
ATOM   172  O OD2 C ASP   A 1 21  ? -23.181 -5.374  -40.611 0.25 78.48  ? 64  ASP   A OD2 1 
ATOM   173  O OD2 D ASP   A 1 21  ? -23.181 -5.374  -40.611 0.25 78.48  ? 64  ASP   A OD2 1 
ATOM   174  N N   . ALA   A 1 22  ? -19.572 -3.742  -36.050 1.00 75.28  ? 65  ALA   A N   1 
ATOM   175  C CA  . ALA   A 1 22  ? -18.962 -2.606  -35.300 1.00 67.70  ? 65  ALA   A CA  1 
ATOM   176  C C   . ALA   A 1 22  ? -17.436 -2.712  -35.414 1.00 64.26  ? 65  ALA   A C   1 
ATOM   177  O O   . ALA   A 1 22  ? -16.933 -3.801  -35.699 1.00 61.71  ? 65  ALA   A O   1 
ATOM   178  C CB  . ALA   A 1 22  ? -19.390 -2.648  -33.857 1.00 68.96  ? 65  ALA   A CB  1 
ATOM   179  N N   A GLU   A 1 23  ? -16.727 -1.603  -35.178 0.25 66.81  ? 66  GLU   A N   1 
ATOM   180  N N   B GLU   A 1 23  ? -16.727 -1.603  -35.178 0.25 66.81  ? 66  GLU   A N   1 
ATOM   181  N N   C GLU   A 1 23  ? -16.732 -1.596  -35.199 0.25 65.00  ? 66  GLU   A N   1 
ATOM   182  N N   D GLU   A 1 23  ? -16.732 -1.596  -35.199 0.25 65.00  ? 66  GLU   A N   1 
ATOM   183  C CA  A GLU   A 1 23  ? -15.246 -1.498  -35.304 0.25 70.45  ? 66  GLU   A CA  1 
ATOM   184  C CA  B GLU   A 1 23  ? -15.246 -1.498  -35.304 0.25 70.45  ? 66  GLU   A CA  1 
ATOM   185  C CA  C GLU   A 1 23  ? -15.249 -1.502  -35.284 0.25 67.47  ? 66  GLU   A CA  1 
ATOM   186  C CA  D GLU   A 1 23  ? -15.249 -1.502  -35.284 0.25 67.47  ? 66  GLU   A CA  1 
ATOM   187  C C   A GLU   A 1 23  ? -14.579 -2.528  -34.380 0.25 74.60  ? 66  GLU   A C   1 
ATOM   188  C C   B GLU   A 1 23  ? -14.579 -2.528  -34.380 0.25 74.60  ? 66  GLU   A C   1 
ATOM   189  C C   C GLU   A 1 23  ? -14.619 -2.555  -34.363 0.25 72.72  ? 66  GLU   A C   1 
ATOM   190  C C   D GLU   A 1 23  ? -14.619 -2.555  -34.363 0.25 72.72  ? 66  GLU   A C   1 
ATOM   191  O O   A GLU   A 1 23  ? -14.493 -2.260  -33.165 0.25 78.50  ? 66  GLU   A O   1 
ATOM   192  O O   B GLU   A 1 23  ? -14.493 -2.260  -33.165 0.25 78.50  ? 66  GLU   A O   1 
ATOM   193  O O   C GLU   A 1 23  ? -14.609 -2.336  -33.135 0.25 75.90  ? 66  GLU   A O   1 
ATOM   194  O O   D GLU   A 1 23  ? -14.609 -2.336  -33.135 0.25 75.90  ? 66  GLU   A O   1 
ATOM   195  C CB  A GLU   A 1 23  ? -14.789 -0.075  -34.978 0.25 72.44  ? 66  GLU   A CB  1 
ATOM   196  C CB  B GLU   A 1 23  ? -14.789 -0.075  -34.978 0.25 72.44  ? 66  GLU   A CB  1 
ATOM   197  C CB  C GLU   A 1 23  ? -14.776 -0.102  -34.893 0.25 67.16  ? 66  GLU   A CB  1 
ATOM   198  C CB  D GLU   A 1 23  ? -14.776 -0.102  -34.893 0.25 67.16  ? 66  GLU   A CB  1 
ATOM   199  C CG  A GLU   A 1 23  ? -13.346 0.204   -35.358 0.25 75.09  ? 66  GLU   A CG  1 
ATOM   200  C CG  B GLU   A 1 23  ? -13.346 0.204   -35.358 0.25 75.09  ? 66  GLU   A CG  1 
ATOM   201  C CG  C GLU   A 1 23  ? -13.289 -0.027  -34.602 0.25 67.49  ? 66  GLU   A CG  1 
ATOM   202  C CG  D GLU   A 1 23  ? -13.289 -0.027  -34.602 0.25 67.49  ? 66  GLU   A CG  1 
ATOM   203  C CD  A GLU   A 1 23  ? -12.998 1.677   -35.499 0.25 76.72  ? 66  GLU   A CD  1 
ATOM   204  C CD  B GLU   A 1 23  ? -12.998 1.677   -35.499 0.25 76.72  ? 66  GLU   A CD  1 
ATOM   205  C CD  C GLU   A 1 23  ? -12.848 1.293   -33.996 0.25 67.09  ? 66  GLU   A CD  1 
ATOM   206  C CD  D GLU   A 1 23  ? -12.848 1.293   -33.996 0.25 67.09  ? 66  GLU   A CD  1 
ATOM   207  O OE1 A GLU   A 1 23  ? -13.333 2.455   -34.583 0.25 79.05  ? 66  GLU   A OE1 1 
ATOM   208  O OE1 B GLU   A 1 23  ? -13.333 2.455   -34.583 0.25 79.05  ? 66  GLU   A OE1 1 
ATOM   209  O OE1 C GLU   A 1 23  ? -13.709 2.182   -33.837 0.25 67.46  ? 66  GLU   A OE1 1 
ATOM   210  O OE1 D GLU   A 1 23  ? -13.709 2.182   -33.837 0.25 67.46  ? 66  GLU   A OE1 1 
ATOM   211  O OE2 A GLU   A 1 23  ? -12.401 2.045   -36.532 0.25 77.16  ? 66  GLU   A OE2 1 
ATOM   212  O OE2 B GLU   A 1 23  ? -12.401 2.045   -36.532 0.25 77.16  ? 66  GLU   A OE2 1 
ATOM   213  O OE2 C GLU   A 1 23  ? -11.650 1.429   -33.683 0.25 66.43  ? 66  GLU   A OE2 1 
ATOM   214  O OE2 D GLU   A 1 23  ? -11.650 1.429   -33.683 0.25 66.43  ? 66  GLU   A OE2 1 
ATOM   215  N N   . VAL   A 1 24  ? -14.141 -3.662  -34.942 1.00 75.84  ? 67  VAL   A N   1 
ATOM   216  C CA  . VAL   A 1 24  ? -13.420 -4.747  -34.203 1.00 67.06  ? 67  VAL   A CA  1 
ATOM   217  C C   . VAL   A 1 24  ? -11.950 -4.349  -34.031 1.00 64.73  ? 67  VAL   A C   1 
ATOM   218  O O   . VAL   A 1 24  ? -11.329 -3.930  -35.006 1.00 68.73  ? 67  VAL   A O   1 
ATOM   219  C CB  . VAL   A 1 24  ? -13.507 -6.098  -34.930 1.00 62.53  ? 67  VAL   A CB  1 
ATOM   220  C CG1 . VAL   A 1 24  ? -12.688 -7.145  -34.203 1.00 60.36  ? 67  VAL   A CG1 1 
ATOM   221  C CG2 . VAL   A 1 24  ? -14.937 -6.575  -35.132 1.00 60.52  ? 67  VAL   A CG2 1 
ATOM   222  N N   . THR   A 1 25  ? -11.398 -4.467  -32.827 1.00 64.37  ? 68  THR   A N   1 
ATOM   223  C CA  . THR   A 1 25  ? -10.015 -4.004  -32.536 1.00 62.63  ? 68  THR   A CA  1 
ATOM   224  C C   . THR   A 1 25  ? -9.571  -4.556  -31.177 1.00 60.01  ? 68  THR   A C   1 
ATOM   225  O O   . THR   A 1 25  ? -10.308 -5.403  -30.650 1.00 50.09  ? 68  THR   A O   1 
ATOM   226  C CB  . THR   A 1 25  ? -9.930  -2.477  -32.655 1.00 62.93  ? 68  THR   A CB  1 
ATOM   227  O OG1 . THR   A 1 25  ? -8.550  -2.170  -32.485 1.00 68.20  ? 68  THR   A OG1 1 
ATOM   228  C CG2 . THR   A 1 25  ? -10.775 -1.716  -31.652 1.00 64.10  ? 68  THR   A CG2 1 
ATOM   229  N N   . GLY   A 1 26  ? -8.405  -4.120  -30.675 1.00 56.14  ? 69  GLY   A N   1 
ATOM   230  C CA  . GLY   A 1 26  ? -7.777  -4.578  -29.418 1.00 57.59  ? 69  GLY   A CA  1 
ATOM   231  C C   . GLY   A 1 26  ? -7.288  -6.027  -29.430 1.00 54.54  ? 69  GLY   A C   1 
ATOM   232  O O   . GLY   A 1 26  ? -7.895  -6.861  -30.127 1.00 63.35  ? 69  GLY   A O   1 
ATOM   233  N N   . ASN   A 1 27  ? -6.293  -6.333  -28.586 1.00 60.55  ? 70  ASN   A N   1 
ATOM   234  C CA  . ASN   A 1 27  ? -5.715  -7.696  -28.366 1.00 65.25  ? 70  ASN   A CA  1 
ATOM   235  C C   . ASN   A 1 27  ? -6.269  -8.361  -27.078 1.00 59.44  ? 70  ASN   A C   1 
ATOM   236  O O   . ASN   A 1 27  ? -7.245  -7.833  -26.505 1.00 57.26  ? 70  ASN   A O   1 
ATOM   237  C CB  . ASN   A 1 27  ? -4.188  -7.608  -28.401 1.00 62.19  ? 70  ASN   A CB  1 
ATOM   238  C CG  . ASN   A 1 27  ? -3.638  -6.765  -27.279 1.00 67.33  ? 70  ASN   A CG  1 
ATOM   239  O OD1 . ASN   A 1 27  ? -3.991  -5.593  -27.152 1.00 74.55  ? 70  ASN   A OD1 1 
ATOM   240  N ND2 . ASN   A 1 27  ? -2.786  -7.352  -26.457 1.00 73.33  ? 70  ASN   A ND2 1 
ATOM   241  N N   . SER   A 1 28  ? -5.716  -9.514  -26.670 1.00 58.55  ? 71  SER   A N   1 
ATOM   242  C CA  . SER   A 1 28  ? -6.221  -10.392 -25.571 1.00 58.08  ? 71  SER   A CA  1 
ATOM   243  C C   . SER   A 1 28  ? -5.094  -10.835 -24.649 1.00 53.36  ? 71  SER   A C   1 
ATOM   244  O O   . SER   A 1 28  ? -4.862  -12.026 -24.530 1.00 54.90  ? 71  SER   A O   1 
ATOM   245  C CB  . SER   A 1 28  ? -6.914  -11.615 -26.111 1.00 54.88  ? 71  SER   A CB  1 
ATOM   246  O OG  . SER   A 1 28  ? -8.004  -11.244 -26.926 1.00 69.14  ? 71  SER   A OG  1 
ATOM   247  N N   . PRO   A 1 29  ? -4.405  -9.922  -23.933 1.00 58.65  ? 72  PRO   A N   1 
ATOM   248  C CA  . PRO   A 1 29  ? -3.269  -10.303 -23.090 1.00 63.03  ? 72  PRO   A CA  1 
ATOM   249  C C   . PRO   A 1 29  ? -3.684  -11.101 -21.845 1.00 68.38  ? 72  PRO   A C   1 
ATOM   250  O O   . PRO   A 1 29  ? -4.717  -10.783 -21.259 1.00 67.39  ? 72  PRO   A O   1 
ATOM   251  C CB  . PRO   A 1 29  ? -2.635  -8.957  -22.687 1.00 63.91  ? 72  PRO   A CB  1 
ATOM   252  C CG  . PRO   A 1 29  ? -3.771  -7.951  -22.775 1.00 61.56  ? 72  PRO   A CG  1 
ATOM   253  C CD  . PRO   A 1 29  ? -4.692  -8.481  -23.861 1.00 63.26  ? 72  PRO   A CD  1 
ATOM   254  N N   . ARG   A 1 30  ? -2.893  -12.121 -21.494 1.00 65.70  ? 73  ARG   A N   1 
ATOM   255  C CA  . ARG   A 1 30  ? -2.956  -12.822 -20.183 1.00 69.58  ? 73  ARG   A CA  1 
ATOM   256  C C   . ARG   A 1 30  ? -1.934  -12.165 -19.239 1.00 66.50  ? 73  ARG   A C   1 
ATOM   257  O O   . ARG   A 1 30  ? -0.733  -12.230 -19.531 1.00 54.63  ? 73  ARG   A O   1 
ATOM   258  C CB  . ARG   A 1 30  ? -2.746  -14.325 -20.378 1.00 75.59  ? 73  ARG   A CB  1 
ATOM   259  C CG  . ARG   A 1 30  ? -3.807  -14.993 -21.246 1.00 86.53  ? 73  ARG   A CG  1 
ATOM   260  C CD  . ARG   A 1 30  ? -3.551  -16.483 -21.460 1.00 99.59  ? 73  ARG   A CD  1 
ATOM   261  N NE  . ARG   A 1 30  ? -4.339  -17.075 -22.545 1.00 103.97 ? 73  ARG   A NE  1 
ATOM   262  C CZ  . ARG   A 1 30  ? -5.546  -17.637 -22.422 1.00 106.77 ? 73  ARG   A CZ  1 
ATOM   263  N NH1 . ARG   A 1 30  ? -6.150  -17.702 -21.247 1.00 123.55 ? 73  ARG   A NH1 1 
ATOM   264  N NH2 . ARG   A 1 30  ? -6.154  -18.134 -23.486 1.00 90.12  ? 73  ARG   A NH2 1 
ATOM   265  N N   . LEU   A 1 31  ? -2.409  -11.502 -18.178 1.00 64.82  ? 74  LEU   A N   1 
ATOM   266  C CA  . LEU   A 1 31  ? -1.585  -10.649 -17.290 1.00 62.04  ? 74  LEU   A CA  1 
ATOM   267  C C   . LEU   A 1 31  ? -1.699  -11.185 -15.859 1.00 64.23  ? 74  LEU   A C   1 
ATOM   268  O O   . LEU   A 1 31  ? -2.833  -11.401 -15.396 1.00 59.68  ? 74  LEU   A O   1 
ATOM   269  C CB  . LEU   A 1 31  ? -2.055  -9.194  -17.405 1.00 67.21  ? 74  LEU   A CB  1 
ATOM   270  C CG  . LEU   A 1 31  ? -1.784  -8.492  -18.743 1.00 70.55  ? 74  LEU   A CG  1 
ATOM   271  C CD1 . LEU   A 1 31  ? -2.435  -7.118  -18.768 1.00 65.82  ? 74  LEU   A CD1 1 
ATOM   272  C CD2 . LEU   A 1 31  ? -0.288  -8.356  -19.050 1.00 67.57  ? 74  LEU   A CD2 1 
ATOM   273  N N   . ASP   A 1 32  ? -0.551  -11.453 -15.226 1.00 62.32  ? 75  ASP   A N   1 
ATOM   274  C CA  . ASP   A 1 32  ? -0.413  -11.724 -13.770 1.00 63.61  ? 75  ASP   A CA  1 
ATOM   275  C C   . ASP   A 1 32  ? -0.578  -10.420 -12.997 1.00 53.16  ? 75  ASP   A C   1 
ATOM   276  O O   . ASP   A 1 32  ? 0.260   -9.509  -13.198 1.00 54.11  ? 75  ASP   A O   1 
ATOM   277  C CB  . ASP   A 1 32  ? 0.971   -12.280 -13.436 1.00 70.22  ? 75  ASP   A CB  1 
ATOM   278  C CG  . ASP   A 1 32  ? 1.058   -13.774 -13.631 1.00 72.06  ? 75  ASP   A CG  1 
ATOM   279  O OD1 . ASP   A 1 32  ? -0.011  -14.410 -13.730 1.00 66.56  ? 75  ASP   A OD1 1 
ATOM   280  O OD2 . ASP   A 1 32  ? 2.188   -14.277 -13.668 1.00 82.70  ? 75  ASP   A OD2 1 
ATOM   281  N N   . VAL   A 1 33  ? -1.605  -10.313 -12.156 1.00 46.74  ? 76  VAL   A N   1 
ATOM   282  C CA  . VAL   A 1 33  ? -1.891  -9.020  -11.466 1.00 48.00  ? 76  VAL   A CA  1 
ATOM   283  C C   . VAL   A 1 33  ? -2.213  -9.308  -10.001 1.00 47.21  ? 76  VAL   A C   1 
ATOM   284  O O   . VAL   A 1 33  ? -2.666  -10.426 -9.683  1.00 42.43  ? 76  VAL   A O   1 
ATOM   285  C CB  . VAL   A 1 33  ? -3.027  -8.224  -12.151 1.00 48.14  ? 76  VAL   A CB  1 
ATOM   286  C CG1 . VAL   A 1 33  ? -2.724  -7.903  -13.599 1.00 52.68  ? 76  VAL   A CG1 1 
ATOM   287  C CG2 . VAL   A 1 33  ? -4.358  -8.946  -12.061 1.00 46.93  ? 76  VAL   A CG2 1 
ATOM   288  N N   . ALA   A 1 34  ? -1.999  -8.306  -9.151  1.00 49.89  ? 77  ALA   A N   1 
ATOM   289  C CA  . ALA   A 1 34  ? -2.422  -8.268  -7.732  1.00 48.72  ? 77  ALA   A CA  1 
ATOM   290  C C   . ALA   A 1 34  ? -3.445  -7.141  -7.578  1.00 47.62  ? 77  ALA   A C   1 
ATOM   291  O O   . ALA   A 1 34  ? -3.305  -6.114  -8.248  1.00 49.72  ? 77  ALA   A O   1 
ATOM   292  C CB  . ALA   A 1 34  ? -1.236  -8.042  -6.821  1.00 40.90  ? 77  ALA   A CB  1 
ATOM   293  N N   . LEU   A 1 35  ? -4.435  -7.350  -6.727  1.00 44.01  ? 78  LEU   A N   1 
ATOM   294  C CA  . LEU   A 1 35  ? -5.477  -6.363  -6.365  1.00 49.50  ? 78  LEU   A CA  1 
ATOM   295  C C   . LEU   A 1 35  ? -5.308  -6.028  -4.876  1.00 48.94  ? 78  LEU   A C   1 
ATOM   296  O O   . LEU   A 1 35  ? -5.413  -6.947  -4.040  1.00 53.97  ? 78  LEU   A O   1 
ATOM   297  C CB  . LEU   A 1 35  ? -6.851  -6.970  -6.691  1.00 46.00  ? 78  LEU   A CB  1 
ATOM   298  C CG  . LEU   A 1 35  ? -8.075  -6.127  -6.315  1.00 47.56  ? 78  LEU   A CG  1 
ATOM   299  C CD1 . LEU   A 1 35  ? -8.137  -4.837  -7.116  1.00 49.25  ? 78  LEU   A CD1 1 
ATOM   300  C CD2 . LEU   A 1 35  ? -9.363  -6.922  -6.490  1.00 46.06  ? 78  LEU   A CD2 1 
ATOM   301  N N   . ASP   A 1 36  ? -5.050  -4.759  -4.561  1.00 50.75  ? 79  ASP   A N   1 
ATOM   302  C CA  . ASP   A 1 36  ? -4.785  -4.283  -3.178  1.00 50.34  ? 79  ASP   A CA  1 
ATOM   303  C C   . ASP   A 1 36  ? -6.120  -3.865  -2.535  1.00 49.28  ? 79  ASP   A C   1 
ATOM   304  O O   . ASP   A 1 36  ? -7.163  -3.944  -3.218  1.00 49.79  ? 79  ASP   A O   1 
ATOM   305  C CB  . ASP   A 1 36  ? -3.688  -3.205  -3.184  1.00 49.28  ? 79  ASP   A CB  1 
ATOM   306  C CG  . ASP   A 1 36  ? -4.128  -1.829  -3.644  1.00 53.14  ? 79  ASP   A CG  1 
ATOM   307  O OD1 . ASP   A 1 36  ? -5.318  -1.673  -3.979  1.00 53.65  ? 79  ASP   A OD1 1 
ATOM   308  O OD2 . ASP   A 1 36  ? -3.279  -0.912  -3.629  1.00 56.93  ? 79  ASP   A OD2 1 
ATOM   309  N N   . GLU   A 1 37  ? -6.074  -3.423  -1.274  1.00 48.31  ? 80  GLU   A N   1 
ATOM   310  C CA  . GLU   A 1 37  ? -7.262  -3.140  -0.428  1.00 48.57  ? 80  GLU   A CA  1 
ATOM   311  C C   . GLU   A 1 37  ? -7.923  -1.840  -0.933  1.00 46.07  ? 80  GLU   A C   1 
ATOM   312  O O   . GLU   A 1 37  ? -9.140  -1.669  -0.708  1.00 44.54  ? 80  GLU   A O   1 
ATOM   313  C CB  . GLU   A 1 37  ? -6.802  -3.142  1.033   1.00 52.60  ? 80  GLU   A CB  1 
ATOM   314  C CG  . GLU   A 1 37  ? -7.921  -3.172  2.062   1.00 61.44  ? 80  GLU   A CG  1 
ATOM   315  C CD  . GLU   A 1 37  ? -7.458  -3.037  3.518   1.00 64.01  ? 80  GLU   A CD  1 
ATOM   316  O OE1 . GLU   A 1 37  ? -7.276  -1.889  4.007   1.00 54.91  ? 80  GLU   A OE1 1 
ATOM   317  O OE2 . GLU   A 1 37  ? -7.254  -4.085  4.163   1.00 66.13  ? 80  GLU   A OE2 1 
ATOM   318  N N   . SER   A 1 38  ? -7.183  -0.968  -1.625  1.00 42.76  ? 81  SER   A N   1 
ATOM   319  C CA  . SER   A 1 38  ? -7.713  0.275   -2.250  1.00 46.46  ? 81  SER   A CA  1 
ATOM   320  C C   . SER   A 1 38  ? -8.379  -0.018  -3.600  1.00 43.90  ? 81  SER   A C   1 
ATOM   321  O O   . SER   A 1 38  ? -8.698  0.962   -4.277  1.00 45.57  ? 81  SER   A O   1 
ATOM   322  C CB  . SER   A 1 38  ? -6.641  1.303   -2.458  1.00 50.51  ? 81  SER   A CB  1 
ATOM   323  O OG  . SER   A 1 38  ? -5.633  1.179   -1.478  1.00 61.06  ? 81  SER   A OG  1 
ATOM   324  N N   . GLY   A 1 39  ? -8.554  -1.288  -3.996  1.00 40.50  ? 82  GLY   A N   1 
ATOM   325  C CA  . GLY   A 1 39  ? -9.123  -1.659  -5.309  1.00 43.48  ? 82  GLY   A CA  1 
ATOM   326  C C   . GLY   A 1 39  ? -8.254  -1.259  -6.509  1.00 42.77  ? 82  GLY   A C   1 
ATOM   327  O O   . GLY   A 1 39  ? -8.830  -1.105  -7.604  1.00 43.68  ? 82  GLY   A O   1 
ATOM   328  N N   . ASP   A 1 40  ? -6.931  -1.129  -6.343  1.00 42.59  ? 83  ASP   A N   1 
ATOM   329  C CA  . ASP   A 1 40  ? -5.955  -0.814  -7.429  1.00 48.32  ? 83  ASP   A CA  1 
ATOM   330  C C   . ASP   A 1 40  ? -5.272  -2.101  -7.919  1.00 49.26  ? 83  ASP   A C   1 
ATOM   331  O O   . ASP   A 1 40  ? -4.669  -2.805  -7.084  1.00 45.25  ? 83  ASP   A O   1 
ATOM   332  C CB  . ASP   A 1 40  ? -4.905  0.189   -6.953  1.00 48.56  ? 83  ASP   A CB  1 
ATOM   333  C CG  . ASP   A 1 40  ? -5.469  1.561   -6.646  1.00 55.89  ? 83  ASP   A CG  1 
ATOM   334  O OD1 . ASP   A 1 40  ? -6.524  1.894   -7.185  1.00 54.83  ? 83  ASP   A OD1 1 
ATOM   335  O OD2 . ASP   A 1 40  ? -4.849  2.290   -5.867  1.00 67.43  ? 83  ASP   A OD2 1 
ATOM   336  N N   . PHE   A 1 41  ? -5.361  -2.401  -9.223  1.00 49.08  ? 84  PHE   A N   1 
ATOM   337  C CA  . PHE   A 1 41  ? -4.651  -3.538  -9.873  1.00 47.06  ? 84  PHE   A CA  1 
ATOM   338  C C   . PHE   A 1 41  ? -3.169  -3.202  -10.034 1.00 53.56  ? 84  PHE   A C   1 
ATOM   339  O O   . PHE   A 1 41  ? -2.836  -2.009  -10.143 1.00 62.21  ? 84  PHE   A O   1 
ATOM   340  C CB  . PHE   A 1 41  ? -5.287  -3.884  -11.214 1.00 43.57  ? 84  PHE   A CB  1 
ATOM   341  C CG  . PHE   A 1 41  ? -6.577  -4.649  -11.077 1.00 45.95  ? 84  PHE   A CG  1 
ATOM   342  C CD1 . PHE   A 1 41  ? -6.574  -5.946  -10.591 1.00 40.73  ? 84  PHE   A CD1 1 
ATOM   343  C CD2 . PHE   A 1 41  ? -7.796  -4.052  -11.377 1.00 42.85  ? 84  PHE   A CD2 1 
ATOM   344  C CE1 . PHE   A 1 41  ? -7.760  -6.647  -10.472 1.00 44.99  ? 84  PHE   A CE1 1 
ATOM   345  C CE2 . PHE   A 1 41  ? -8.981  -4.748  -11.221 1.00 38.61  ? 84  PHE   A CE2 1 
ATOM   346  C CZ  . PHE   A 1 41  ? -8.961  -6.051  -10.795 1.00 42.85  ? 84  PHE   A CZ  1 
ATOM   347  N N   . SER   A 1 42  ? -2.298  -4.211  -10.037 1.00 51.87  ? 85  SER   A N   1 
ATOM   348  C CA  . SER   A 1 42  ? -0.844  -4.022  -10.266 1.00 54.02  ? 85  SER   A CA  1 
ATOM   349  C C   . SER   A 1 42  ? -0.249  -5.310  -10.844 1.00 57.02  ? 85  SER   A C   1 
ATOM   350  O O   . SER   A 1 42  ? -0.794  -6.403  -10.561 1.00 56.44  ? 85  SER   A O   1 
ATOM   351  C CB  . SER   A 1 42  ? -0.143  -3.579  -9.007  1.00 56.79  ? 85  SER   A CB  1 
ATOM   352  O OG  . SER   A 1 42  ? -0.155  -4.601  -8.010  1.00 64.26  ? 85  SER   A OG  1 
ATOM   353  N N   . LEU   A 1 43  ? 0.808   -5.183  -11.646 1.00 62.64  ? 86  LEU   A N   1 
ATOM   354  C CA  . LEU   A 1 43  ? 1.454   -6.340  -12.321 1.00 65.92  ? 86  LEU   A CA  1 
ATOM   355  C C   . LEU   A 1 43  ? 2.409   -7.053  -11.361 1.00 64.26  ? 86  LEU   A C   1 
ATOM   356  O O   . LEU   A 1 43  ? 3.322   -6.404  -10.838 1.00 60.47  ? 86  LEU   A O   1 
ATOM   357  C CB  . LEU   A 1 43  ? 2.161   -5.839  -13.574 1.00 66.04  ? 86  LEU   A CB  1 
ATOM   358  C CG  . LEU   A 1 43  ? 1.177   -5.419  -14.656 1.00 70.16  ? 86  LEU   A CG  1 
ATOM   359  C CD1 . LEU   A 1 43  ? 1.834   -4.480  -15.651 1.00 77.52  ? 86  LEU   A CD1 1 
ATOM   360  C CD2 . LEU   A 1 43  ? 0.592   -6.646  -15.347 1.00 70.93  ? 86  LEU   A CD2 1 
ATOM   361  N N   . VAL   A 1 44  ? 2.127   -8.332  -11.120 1.00 69.93  ? 87  VAL   A N   1 
ATOM   362  C CA  . VAL   A 1 44  ? 2.982   -9.325  -10.408 1.00 75.75  ? 87  VAL   A CA  1 
ATOM   363  C C   . VAL   A 1 44  ? 3.974   -9.889  -11.419 1.00 84.30  ? 87  VAL   A C   1 
ATOM   364  O O   . VAL   A 1 44  ? 3.542   -10.673 -12.286 1.00 100.16 ? 87  VAL   A O   1 
ATOM   365  C CB  . VAL   A 1 44  ? 2.120   -10.464 -9.835  1.00 75.30  ? 87  VAL   A CB  1 
ATOM   366  C CG1 . VAL   A 1 44  ? 2.970   -11.604 -9.282  1.00 72.56  ? 87  VAL   A CG1 1 
ATOM   367  C CG2 . VAL   A 1 44  ? 1.135   -9.941  -8.801  1.00 72.24  ? 87  VAL   A CG2 1 
ATOM   368  N N   . GLU   A 1 45  ? 5.246   -9.525  -11.312 1.00 91.19  ? 88  GLU   A N   1 
ATOM   369  C CA  . GLU   A 1 45  ? 6.267   -9.937  -12.306 1.00 102.42 ? 88  GLU   A CA  1 
ATOM   370  C C   . GLU   A 1 45  ? 7.157   -11.032 -11.705 1.00 105.34 ? 88  GLU   A C   1 
ATOM   371  O O   . GLU   A 1 45  ? 6.858   -12.214 -11.908 1.00 99.23  ? 88  GLU   A O   1 
ATOM   372  C CB  . GLU   A 1 45  ? 7.006   -8.685  -12.764 1.00 107.01 ? 88  GLU   A CB  1 
ATOM   373  C CG  . GLU   A 1 45  ? 6.222   -7.895  -13.801 1.00 105.47 ? 88  GLU   A CG  1 
ATOM   374  C CD  . GLU   A 1 45  ? 6.389   -8.409  -15.219 1.00 99.62  ? 88  GLU   A CD  1 
ATOM   375  O OE1 . GLU   A 1 45  ? 6.799   -9.578  -15.374 1.00 95.10  ? 88  GLU   A OE1 1 
ATOM   376  O OE2 . GLU   A 1 45  ? 6.127   -7.634  -16.163 1.00 102.84 ? 88  GLU   A OE2 1 
ATOM   377  N N   . GLY   B 2 7   ? -36.438 12.138  -11.427 1.00 94.37  ? 16  GLY   B N   1 
ATOM   378  C CA  . GLY   B 2 7   ? -35.397 12.131  -12.503 1.00 92.63  ? 16  GLY   B CA  1 
ATOM   379  C C   . GLY   B 2 7   ? -35.634 11.053  -13.559 1.00 94.06  ? 16  GLY   B C   1 
ATOM   380  O O   . GLY   B 2 7   ? -36.644 10.316  -13.448 1.00 98.20  ? 16  GLY   B O   1 
ATOM   381  N N   . GLU   B 2 8   ? -34.721 10.950  -14.538 1.00 84.50  ? 17  GLU   B N   1 
ATOM   382  C CA  . GLU   B 2 8   ? -34.809 10.052  -15.729 1.00 78.90  ? 17  GLU   B CA  1 
ATOM   383  C C   . GLU   B 2 8   ? -34.391 8.622   -15.346 1.00 73.23  ? 17  GLU   B C   1 
ATOM   384  O O   . GLU   B 2 8   ? -33.193 8.360   -15.193 1.00 69.73  ? 17  GLU   B O   1 
ATOM   385  C CB  . GLU   B 2 8   ? -33.925 10.576  -16.869 1.00 78.62  ? 17  GLU   B CB  1 
ATOM   386  C CG  . GLU   B 2 8   ? -34.117 9.811   -18.174 1.00 75.30  ? 17  GLU   B CG  1 
ATOM   387  C CD  . GLU   B 2 8   ? -33.491 10.395  -19.435 1.00 71.75  ? 17  GLU   B CD  1 
ATOM   388  O OE1 . GLU   B 2 8   ? -32.505 11.172  -19.333 1.00 54.83  ? 17  GLU   B OE1 1 
ATOM   389  O OE2 . GLU   B 2 8   ? -34.015 10.074  -20.536 1.00 78.42  ? 17  GLU   B OE2 1 
ATOM   390  N N   A THR   B 2 9   ? -35.351 7.709   -15.176 0.25 73.49  ? 18  THR   B N   1 
ATOM   391  N N   B THR   B 2 9   ? -35.386 7.732   -15.260 0.25 71.13  ? 18  THR   B N   1 
ATOM   392  N N   C THR   B 2 9   ? -35.351 7.709   -15.176 0.25 73.49  ? 18  THR   B N   1 
ATOM   393  N N   D THR   B 2 9   ? -35.386 7.732   -15.260 0.25 71.13  ? 18  THR   B N   1 
ATOM   394  C CA  A THR   B 2 9   ? -35.070 6.306   -14.768 0.25 74.59  ? 18  THR   B CA  1 
ATOM   395  C CA  B THR   B 2 9   ? -35.276 6.331   -14.775 0.25 70.50  ? 18  THR   B CA  1 
ATOM   396  C CA  C THR   B 2 9   ? -35.070 6.306   -14.768 0.25 74.59  ? 18  THR   B CA  1 
ATOM   397  C CA  D THR   B 2 9   ? -35.276 6.331   -14.775 0.25 70.50  ? 18  THR   B CA  1 
ATOM   398  C C   A THR   B 2 9   ? -35.208 5.354   -15.960 0.25 71.90  ? 18  THR   B C   1 
ATOM   399  C C   B THR   B 2 9   ? -35.109 5.355   -15.947 0.25 69.53  ? 18  THR   B C   1 
ATOM   400  C C   C THR   B 2 9   ? -35.208 5.354   -15.960 0.25 71.90  ? 18  THR   B C   1 
ATOM   401  C C   D THR   B 2 9   ? -35.109 5.355   -15.947 0.25 69.53  ? 18  THR   B C   1 
ATOM   402  O O   A THR   B 2 9   ? -35.462 4.160   -15.717 0.25 76.55  ? 18  THR   B O   1 
ATOM   403  O O   B THR   B 2 9   ? -35.027 4.142   -15.672 0.25 73.10  ? 18  THR   B O   1 
ATOM   404  O O   C THR   B 2 9   ? -35.462 4.160   -15.717 0.25 76.55  ? 18  THR   B O   1 
ATOM   405  O O   D THR   B 2 9   ? -35.027 4.142   -15.672 0.25 73.10  ? 18  THR   B O   1 
ATOM   406  C CB  A THR   B 2 9   ? -35.980 5.847   -13.625 0.25 76.94  ? 18  THR   B CB  1 
ATOM   407  C CB  B THR   B 2 9   ? -36.513 5.964   -13.945 0.25 70.23  ? 18  THR   B CB  1 
ATOM   408  C CB  C THR   B 2 9   ? -35.980 5.847   -13.625 0.25 76.94  ? 18  THR   B CB  1 
ATOM   409  C CB  D THR   B 2 9   ? -36.513 5.964   -13.945 0.25 70.23  ? 18  THR   B CB  1 
ATOM   410  O OG1 A THR   B 2 9   ? -35.828 6.747   -12.527 0.25 83.24  ? 18  THR   B OG1 1 
ATOM   411  O OG1 B THR   B 2 9   ? -37.672 6.297   -14.708 0.25 64.91  ? 18  THR   B OG1 1 
ATOM   412  O OG1 C THR   B 2 9   ? -35.828 6.747   -12.527 0.25 83.24  ? 18  THR   B OG1 1 
ATOM   413  O OG1 D THR   B 2 9   ? -37.672 6.297   -14.708 0.25 64.91  ? 18  THR   B OG1 1 
ATOM   414  C CG2 A THR   B 2 9   ? -35.651 4.443   -13.175 0.25 74.62  ? 18  THR   B CG2 1 
ATOM   415  C CG2 B THR   B 2 9   ? -36.567 6.687   -12.617 0.25 72.67  ? 18  THR   B CG2 1 
ATOM   416  C CG2 C THR   B 2 9   ? -35.651 4.443   -13.175 0.25 74.62  ? 18  THR   B CG2 1 
ATOM   417  C CG2 D THR   B 2 9   ? -36.567 6.687   -12.617 0.25 72.67  ? 18  THR   B CG2 1 
ATOM   418  N N   . THR   B 2 10  ? -35.038 5.856   -17.186 1.00 65.03  ? 19  THR   B N   1 
ATOM   419  C CA  . THR   B 2 10  ? -35.023 5.021   -18.414 1.00 63.34  ? 19  THR   B CA  1 
ATOM   420  C C   . THR   B 2 10  ? -33.735 4.184   -18.468 1.00 52.03  ? 19  THR   B C   1 
ATOM   421  O O   . THR   B 2 10  ? -32.632 4.770   -18.353 1.00 45.78  ? 19  THR   B O   1 
ATOM   422  C CB  . THR   B 2 10  ? -35.142 5.855   -19.702 1.00 69.12  ? 19  THR   B CB  1 
ATOM   423  O OG1 . THR   B 2 10  ? -36.057 6.943   -19.549 1.00 78.26  ? 19  THR   B OG1 1 
ATOM   424  C CG2 . THR   B 2 10  ? -35.603 5.019   -20.880 1.00 70.46  ? 19  THR   B CG2 1 
ATOM   425  N N   . ASP   B 2 11  ? -33.867 2.872   -18.686 1.00 44.11  ? 20  ASP   B N   1 
ATOM   426  C CA  . ASP   B 2 11  ? -32.714 1.962   -18.939 1.00 49.76  ? 20  ASP   B CA  1 
ATOM   427  C C   . ASP   B 2 11  ? -31.785 2.573   -19.993 1.00 49.11  ? 20  ASP   B C   1 
ATOM   428  O O   . ASP   B 2 11  ? -32.266 3.334   -20.840 1.00 51.29  ? 20  ASP   B O   1 
ATOM   429  C CB  . ASP   B 2 11  ? -33.153 0.564   -19.366 1.00 51.46  ? 20  ASP   B CB  1 
ATOM   430  C CG  . ASP   B 2 11  ? -33.759 -0.230  -18.227 1.00 57.39  ? 20  ASP   B CG  1 
ATOM   431  O OD1 . ASP   B 2 11  ? -33.955 0.374   -17.144 1.00 52.24  ? 20  ASP   B OD1 1 
ATOM   432  O OD2 . ASP   B 2 11  ? -34.068 -1.434  -18.444 1.00 57.56  ? 20  ASP   B OD2 1 
ATOM   433  N N   . GLY   B 2 12  ? -30.488 2.272   -19.916 1.00 46.98  ? 21  GLY   B N   1 
ATOM   434  C CA  . GLY   B 2 12  ? -29.499 2.737   -20.902 1.00 42.15  ? 21  GLY   B CA  1 
ATOM   435  C C   . GLY   B 2 12  ? -28.247 3.211   -20.223 1.00 37.37  ? 21  GLY   B C   1 
ATOM   436  O O   . GLY   B 2 12  ? -28.139 3.041   -19.018 1.00 37.33  ? 21  GLY   B O   1 
ATOM   437  N N   . VAL   B 2 13  ? -27.376 3.847   -20.985 1.00 35.59  ? 22  VAL   B N   1 
ATOM   438  C CA  . VAL   B 2 13  ? -26.048 4.321   -20.539 1.00 37.04  ? 22  VAL   B CA  1 
ATOM   439  C C   . VAL   B 2 13  ? -26.113 5.846   -20.448 1.00 41.19  ? 22  VAL   B C   1 
ATOM   440  O O   . VAL   B 2 13  ? -26.905 6.463   -21.202 1.00 38.42  ? 22  VAL   B O   1 
ATOM   441  C CB  . VAL   B 2 13  ? -24.964 3.778   -21.474 1.00 40.06  ? 22  VAL   B CB  1 
ATOM   442  C CG1 . VAL   B 2 13  ? -25.183 4.228   -22.923 1.00 41.49  ? 22  VAL   B CG1 1 
ATOM   443  C CG2 . VAL   B 2 13  ? -23.570 4.110   -20.977 1.00 37.18  ? 22  VAL   B CG2 1 
ATOM   444  N N   . TYR   B 2 14  ? -25.387 6.414   -19.487 1.00 42.14  ? 23  TYR   B N   1 
ATOM   445  C CA  . TYR   B 2 14  ? -25.488 7.836   -19.085 1.00 40.22  ? 23  TYR   B CA  1 
ATOM   446  C C   . TYR   B 2 14  ? -24.097 8.386   -18.860 1.00 38.53  ? 23  TYR   B C   1 
ATOM   447  O O   . TYR   B 2 14  ? -23.254 7.638   -18.348 1.00 42.37  ? 23  TYR   B O   1 
ATOM   448  C CB  . TYR   B 2 14  ? -26.260 7.963   -17.779 1.00 37.54  ? 23  TYR   B CB  1 
ATOM   449  C CG  . TYR   B 2 14  ? -27.733 7.754   -17.924 1.00 35.25  ? 23  TYR   B CG  1 
ATOM   450  C CD1 . TYR   B 2 14  ? -28.244 6.500   -18.177 1.00 34.59  ? 23  TYR   B CD1 1 
ATOM   451  C CD2 . TYR   B 2 14  ? -28.610 8.814   -17.787 1.00 36.94  ? 23  TYR   B CD2 1 
ATOM   452  C CE1 . TYR   B 2 14  ? -29.605 6.300   -18.287 1.00 35.02  ? 23  TYR   B CE1 1 
ATOM   453  C CE2 . TYR   B 2 14  ? -29.979 8.637   -17.925 1.00 33.49  ? 23  TYR   B CE2 1 
ATOM   454  C CZ  . TYR   B 2 14  ? -30.473 7.378   -18.177 1.00 39.01  ? 23  TYR   B CZ  1 
ATOM   455  O OH  . TYR   B 2 14  ? -31.821 7.191   -18.277 1.00 39.64  ? 23  TYR   B OH  1 
ATOM   456  N N   . ARG   B 2 15  ? -23.895 9.652   -19.192 1.00 37.29  ? 24  ARG   B N   1 
ATOM   457  C CA  . ARG   B 2 15  ? -22.667 10.383  -18.803 1.00 39.26  ? 24  ARG   B CA  1 
ATOM   458  C C   . ARG   B 2 15  ? -22.808 10.808  -17.342 1.00 42.48  ? 24  ARG   B C   1 
ATOM   459  O O   . ARG   B 2 15  ? -23.922 11.178  -16.945 1.00 36.09  ? 24  ARG   B O   1 
ATOM   460  C CB  . ARG   B 2 15  ? -22.448 11.583  -19.720 1.00 42.02  ? 24  ARG   B CB  1 
ATOM   461  C CG  . ARG   B 2 15  ? -22.293 11.202  -21.184 1.00 44.82  ? 24  ARG   B CG  1 
ATOM   462  C CD  . ARG   B 2 15  ? -22.338 12.398  -22.115 1.00 52.69  ? 24  ARG   B CD  1 
ATOM   463  N NE  . ARG   B 2 15  ? -22.454 11.931  -23.500 1.00 55.12  ? 24  ARG   B NE  1 
ATOM   464  C CZ  . ARG   B 2 15  ? -21.439 11.781  -24.344 1.00 50.43  ? 24  ARG   B CZ  1 
ATOM   465  N NH1 . ARG   B 2 15  ? -20.213 12.084  -23.957 1.00 44.98  ? 24  ARG   B NH1 1 
ATOM   466  N NH2 . ARG   B 2 15  ? -21.665 11.314  -25.564 1.00 53.32  ? 24  ARG   B NH2 1 
ATOM   467  N N   . VAL   B 2 16  ? -21.710 10.750  -16.591 1.00 41.29  ? 25  VAL   B N   1 
ATOM   468  C CA  . VAL   B 2 16  ? -21.590 11.312  -15.222 1.00 44.67  ? 25  VAL   B CA  1 
ATOM   469  C C   . VAL   B 2 16  ? -20.749 12.592  -15.335 1.00 43.95  ? 25  VAL   B C   1 
ATOM   470  O O   . VAL   B 2 16  ? -19.540 12.520  -15.613 1.00 41.70  ? 25  VAL   B O   1 
ATOM   471  C CB  . VAL   B 2 16  ? -20.997 10.289  -14.218 1.00 51.57  ? 25  VAL   B CB  1 
ATOM   472  C CG1 . VAL   B 2 16  ? -20.959 10.854  -12.799 1.00 49.65  ? 25  VAL   B CG1 1 
ATOM   473  C CG2 . VAL   B 2 16  ? -21.743 8.953   -14.231 1.00 49.50  ? 25  VAL   B CG2 1 
ATOM   474  N N   . MET   B 2 17  ? -21.394 13.730  -15.110 1.00 43.90  ? 26  MET   B N   1 
ATOM   475  C CA  . MET   B 2 17  ? -20.851 15.099  -15.270 1.00 46.03  ? 26  MET   B CA  1 
ATOM   476  C C   . MET   B 2 17  ? -20.699 15.774  -13.901 1.00 46.16  ? 26  MET   B C   1 
ATOM   477  O O   . MET   B 2 17  ? -21.459 15.414  -12.987 1.00 49.88  ? 26  MET   B O   1 
ATOM   478  C CB  . MET   B 2 17  ? -21.852 15.903  -16.096 1.00 45.75  ? 26  MET   B CB  1 
ATOM   479  C CG  . MET   B 2 17  ? -22.288 15.213  -17.383 1.00 48.69  ? 26  MET   B CG  1 
ATOM   480  S SD  . MET   B 2 17  ? -20.954 15.065  -18.618 1.00 50.05  ? 26  MET   B SD  1 
ATOM   481  C CE  . MET   B 2 17  ? -20.346 16.748  -18.665 1.00 47.62  ? 26  MET   B CE  1 
ATOM   482  N N   . THR   B 2 18  ? -19.775 16.731  -13.799 1.00 46.23  ? 27  THR   B N   1 
ATOM   483  C CA  . THR   B 2 18  ? -19.659 17.740  -12.719 1.00 53.43  ? 27  THR   B CA  1 
ATOM   484  C C   . THR   B 2 18  ? -19.450 19.151  -13.311 1.00 57.02  ? 27  THR   B C   1 
ATOM   485  O O   . THR   B 2 18  ? -18.913 19.275  -14.458 1.00 45.83  ? 27  THR   B O   1 
ATOM   486  C CB  . THR   B 2 18  ? -18.495 17.390  -11.783 1.00 54.56  ? 27  THR   B CB  1 
ATOM   487  O OG1 . THR   B 2 18  ? -18.440 18.402  -10.772 1.00 50.91  ? 27  THR   B OG1 1 
ATOM   488  C CG2 . THR   B 2 18  ? -17.162 17.291  -12.500 1.00 52.74  ? 27  THR   B CG2 1 
ATOM   489  N N   . ARG   B 2 19  ? -19.822 20.183  -12.540 1.00 64.27  ? 28  ARG   B N   1 
ATOM   490  C CA  . ARG   B 2 19  ? -19.534 21.620  -12.837 1.00 74.30  ? 28  ARG   B CA  1 
ATOM   491  C C   . ARG   B 2 19  ? -18.517 22.193  -11.828 1.00 67.82  ? 28  ARG   B C   1 
ATOM   492  O O   . ARG   B 2 19  ? -18.188 23.389  -11.934 1.00 67.26  ? 28  ARG   B O   1 
ATOM   493  C CB  . ARG   B 2 19  ? -20.845 22.414  -12.871 1.00 75.80  ? 28  ARG   B CB  1 
ATOM   494  C CG  . ARG   B 2 19  ? -21.821 21.916  -13.928 1.00 81.89  ? 28  ARG   B CG  1 
ATOM   495  C CD  . ARG   B 2 19  ? -22.433 23.013  -14.776 1.00 82.89  ? 28  ARG   B CD  1 
ATOM   496  N NE  . ARG   B 2 19  ? -23.527 22.515  -15.597 1.00 86.59  ? 28  ARG   B NE  1 
ATOM   497  C CZ  . ARG   B 2 19  ? -24.747 22.222  -15.149 1.00 95.55  ? 28  ARG   B CZ  1 
ATOM   498  N NH1 . ARG   B 2 19  ? -25.052 22.370  -13.868 1.00 102.74 ? 28  ARG   B NH1 1 
ATOM   499  N NH2 . ARG   B 2 19  ? -25.663 21.771  -15.990 1.00 93.28  ? 28  ARG   B NH2 1 
ATOM   500  N N   . ARG   B 2 20  ? -17.966 21.356  -10.945 1.00 69.79  ? 29  ARG   B N   1 
ATOM   501  C CA  . ARG   B 2 20  ? -17.083 21.777  -9.821  1.00 79.19  ? 29  ARG   B CA  1 
ATOM   502  C C   . ARG   B 2 20  ? -15.718 22.220  -10.363 1.00 78.89  ? 29  ARG   B C   1 
ATOM   503  O O   . ARG   B 2 20  ? -14.890 22.672  -9.561  1.00 86.86  ? 29  ARG   B O   1 
ATOM   504  C CB  . ARG   B 2 20  ? -16.926 20.638  -8.807  1.00 78.88  ? 29  ARG   B CB  1 
ATOM   505  C CG  . ARG   B 2 20  ? -16.585 21.096  -7.397  1.00 88.07  ? 29  ARG   B CG  1 
ATOM   506  C CD  . ARG   B 2 20  ? -16.370 19.920  -6.461  1.00 106.69 ? 29  ARG   B CD  1 
ATOM   507  N NE  . ARG   B 2 20  ? -15.352 18.981  -6.940  1.00 118.54 ? 29  ARG   B NE  1 
ATOM   508  C CZ  . ARG   B 2 20  ? -14.075 18.919  -6.535  1.00 120.37 ? 29  ARG   B CZ  1 
ATOM   509  N NH1 . ARG   B 2 20  ? -13.601 19.746  -5.615  1.00 115.20 ? 29  ARG   B NH1 1 
ATOM   510  N NH2 . ARG   B 2 20  ? -13.266 18.015  -7.064  1.00 116.47 ? 29  ARG   B NH2 1 
ATOM   511  N N   . LEU   B 2 21  ? -15.478 22.060  -11.666 1.00 76.07  ? 30  LEU   B N   1 
ATOM   512  C CA  . LEU   B 2 21  ? -14.237 22.504  -12.353 1.00 74.21  ? 30  LEU   B CA  1 
ATOM   513  C C   . LEU   B 2 21  ? -14.623 23.502  -13.443 1.00 72.54  ? 30  LEU   B C   1 
ATOM   514  O O   . LEU   B 2 21  ? -15.827 23.848  -13.538 1.00 71.27  ? 30  LEU   B O   1 
ATOM   515  C CB  . LEU   B 2 21  ? -13.528 21.286  -12.955 1.00 74.39  ? 30  LEU   B CB  1 
ATOM   516  C CG  . LEU   B 2 21  ? -12.528 20.558  -12.063 1.00 77.74  ? 30  LEU   B CG  1 
ATOM   517  C CD1 . LEU   B 2 21  ? -12.920 20.613  -10.598 1.00 80.13  ? 30  LEU   B CD1 1 
ATOM   518  C CD2 . LEU   B 2 21  ? -12.367 19.115  -12.523 1.00 74.03  ? 30  LEU   B CD2 1 
ATOM   519  N N   . LEU   B 2 22  ? -13.635 23.930  -14.233 1.00 69.37  ? 31  LEU   B N   1 
ATOM   520  C CA  . LEU   B 2 22  ? -13.845 24.746  -15.452 1.00 66.52  ? 31  LEU   B CA  1 
ATOM   521  C C   . LEU   B 2 22  ? -14.862 24.037  -16.337 1.00 63.39  ? 31  LEU   B C   1 
ATOM   522  O O   . LEU   B 2 22  ? -14.675 22.835  -16.530 1.00 68.56  ? 31  LEU   B O   1 
ATOM   523  C CB  . LEU   B 2 22  ? -12.523 24.893  -16.200 1.00 65.05  ? 31  LEU   B CB  1 
ATOM   524  C CG  . LEU   B 2 22  ? -12.578 25.936  -17.312 1.00 66.24  ? 31  LEU   B CG  1 
ATOM   525  C CD1 . LEU   B 2 22  ? -12.448 27.342  -16.727 1.00 56.43  ? 31  LEU   B CD1 1 
ATOM   526  C CD2 . LEU   B 2 22  ? -11.513 25.658  -18.371 1.00 66.17  ? 31  LEU   B CD2 1 
ATOM   527  N N   . GLY   B 2 23  ? -15.885 24.749  -16.829 1.00 62.39  ? 32  GLY   B N   1 
ATOM   528  C CA  . GLY   B 2 23  ? -16.953 24.197  -17.692 1.00 53.50  ? 32  GLY   B CA  1 
ATOM   529  C C   . GLY   B 2 23  ? -17.668 23.009  -17.055 1.00 54.32  ? 32  GLY   B C   1 
ATOM   530  O O   . GLY   B 2 23  ? -17.609 22.836  -15.820 1.00 61.76  ? 32  GLY   B O   1 
ATOM   531  N N   . SER   B 2 24  ? -18.366 22.239  -17.879 1.00 56.71  ? 33  SER   B N   1 
ATOM   532  C CA  . SER   B 2 24  ? -19.014 20.957  -17.522 1.00 54.19  ? 33  SER   B CA  1 
ATOM   533  C C   . SER   B 2 24  ? -18.062 19.832  -17.912 1.00 55.80  ? 33  SER   B C   1 
ATOM   534  O O   . SER   B 2 24  ? -17.751 19.778  -19.083 1.00 52.37  ? 33  SER   B O   1 
ATOM   535  C CB  . SER   B 2 24  ? -20.342 20.842  -18.203 1.00 56.91  ? 33  SER   B CB  1 
ATOM   536  O OG  . SER   B 2 24  ? -21.241 21.821  -17.680 1.00 59.88  ? 33  SER   B OG  1 
ATOM   537  N N   . THR   B 2 25  ? -17.568 19.033  -16.954 1.00 59.12  ? 34  THR   B N   1 
ATOM   538  C CA  . THR   B 2 25  ? -16.512 18.002  -17.171 1.00 54.11  ? 34  THR   B CA  1 
ATOM   539  C C   . THR   B 2 25  ? -17.122 16.609  -16.990 1.00 56.00  ? 34  THR   B C   1 
ATOM   540  O O   . THR   B 2 25  ? -17.846 16.429  -15.999 1.00 61.02  ? 34  THR   B O   1 
ATOM   541  C CB  . THR   B 2 25  ? -15.332 18.214  -16.213 1.00 57.28  ? 34  THR   B CB  1 
ATOM   542  O OG1 . THR   B 2 25  ? -14.762 19.504  -16.456 1.00 54.28  ? 34  THR   B OG1 1 
ATOM   543  C CG2 . THR   B 2 25  ? -14.265 17.147  -16.350 1.00 51.05  ? 34  THR   B CG2 1 
ATOM   544  N N   . GLN   B 2 26  ? -16.834 15.658  -17.886 1.00 50.76  ? 35  GLN   B N   1 
ATOM   545  C CA  . GLN   B 2 26  ? -17.344 14.262  -17.771 1.00 50.81  ? 35  GLN   B CA  1 
ATOM   546  C C   . GLN   B 2 26  ? -16.339 13.411  -16.980 1.00 58.60  ? 35  GLN   B C   1 
ATOM   547  O O   . GLN   B 2 26  ? -15.235 13.149  -17.525 1.00 61.03  ? 35  GLN   B O   1 
ATOM   548  C CB  . GLN   B 2 26  ? -17.576 13.626  -19.132 1.00 45.53  ? 35  GLN   B CB  1 
ATOM   549  C CG  . GLN   B 2 26  ? -18.198 12.240  -19.037 1.00 48.84  ? 35  GLN   B CG  1 
ATOM   550  C CD  . GLN   B 2 26  ? -18.402 11.591  -20.384 1.00 45.78  ? 35  GLN   B CD  1 
ATOM   551  O OE1 . GLN   B 2 26  ? -19.036 12.141  -21.277 1.00 48.70  ? 35  GLN   B OE1 1 
ATOM   552  N NE2 . GLN   B 2 26  ? -17.895 10.385  -20.530 1.00 46.78  ? 35  GLN   B NE2 1 
ATOM   553  N N   . VAL   B 2 27  ? -16.709 12.971  -15.768 1.00 48.63  ? 36  VAL   B N   1 
ATOM   554  C CA  . VAL   B 2 27  ? -15.805 12.222  -14.835 1.00 48.40  ? 36  VAL   B CA  1 
ATOM   555  C C   . VAL   B 2 27  ? -15.980 10.717  -15.057 1.00 42.97  ? 36  VAL   B C   1 
ATOM   556  O O   . VAL   B 2 27  ? -15.087 9.973   -14.684 1.00 47.35  ? 36  VAL   B O   1 
ATOM   557  C CB  . VAL   B 2 27  ? -16.045 12.620  -13.362 1.00 52.70  ? 36  VAL   B CB  1 
ATOM   558  C CG1 . VAL   B 2 27  ? -15.511 14.008  -13.069 1.00 54.72  ? 36  VAL   B CG1 1 
ATOM   559  C CG2 . VAL   B 2 27  ? -17.506 12.541  -12.951 1.00 50.80  ? 36  VAL   B CG2 1 
ATOM   560  N N   . GLY   B 2 28  ? -17.090 10.295  -15.663 1.00 46.21  ? 37  GLY   B N   1 
ATOM   561  C CA  . GLY   B 2 28  ? -17.390 8.866   -15.861 1.00 36.13  ? 37  GLY   B CA  1 
ATOM   562  C C   . GLY   B 2 28  ? -18.718 8.627   -16.557 1.00 36.58  ? 37  GLY   B C   1 
ATOM   563  O O   . GLY   B 2 28  ? -19.302 9.578   -17.068 1.00 40.93  ? 37  GLY   B O   1 
ATOM   564  N N   . VAL   B 2 29  ? -19.160 7.367   -16.528 1.00 33.11  ? 38  VAL   B N   1 
ATOM   565  C CA  . VAL   B 2 29  ? -20.299 6.762   -17.279 1.00 31.61  ? 38  VAL   B CA  1 
ATOM   566  C C   . VAL   B 2 29  ? -20.970 5.778   -16.325 1.00 29.85  ? 38  VAL   B C   1 
ATOM   567  O O   . VAL   B 2 29  ? -20.315 5.328   -15.417 1.00 38.41  ? 38  VAL   B O   1 
ATOM   568  C CB  . VAL   B 2 29  ? -19.810 6.003   -18.533 1.00 36.70  ? 38  VAL   B CB  1 
ATOM   569  C CG1 . VAL   B 2 29  ? -20.949 5.334   -19.299 1.00 40.56  ? 38  VAL   B CG1 1 
ATOM   570  C CG2 . VAL   B 2 29  ? -18.993 6.862   -19.469 1.00 35.84  ? 38  VAL   B CG2 1 
ATOM   571  N N   . GLY   B 2 30  ? -22.206 5.385   -16.582 1.00 33.17  ? 39  GLY   B N   1 
ATOM   572  C CA  . GLY   B 2 30  ? -22.866 4.354   -15.779 1.00 28.28  ? 39  GLY   B CA  1 
ATOM   573  C C   . GLY   B 2 30  ? -24.049 3.816   -16.519 1.00 30.65  ? 39  GLY   B C   1 
ATOM   574  O O   . GLY   B 2 30  ? -24.334 4.345   -17.594 1.00 34.03  ? 39  GLY   B O   1 
ATOM   575  N N   . VAL   B 2 31  ? -24.685 2.798   -15.958 1.00 34.14  ? 40  VAL   B N   1 
ATOM   576  C CA  . VAL   B 2 31  ? -25.810 2.029   -16.561 1.00 31.99  ? 40  VAL   B CA  1 
ATOM   577  C C   . VAL   B 2 31  ? -27.021 2.178   -15.648 1.00 37.43  ? 40  VAL   B C   1 
ATOM   578  O O   . VAL   B 2 31  ? -26.892 1.814   -14.437 1.00 39.74  ? 40  VAL   B O   1 
ATOM   579  C CB  . VAL   B 2 31  ? -25.489 0.527   -16.669 1.00 32.17  ? 40  VAL   B CB  1 
ATOM   580  C CG1 . VAL   B 2 31  ? -26.671 -0.268  -17.188 1.00 32.78  ? 40  VAL   B CG1 1 
ATOM   581  C CG2 . VAL   B 2 31  ? -24.254 0.252   -17.505 1.00 35.59  ? 40  VAL   B CG2 1 
ATOM   582  N N   . MET   B 2 32  ? -28.166 2.563   -16.220 1.00 35.60  ? 41  MET   B N   1 
ATOM   583  C CA  . MET   B 2 32  ? -29.497 2.497   -15.572 1.00 36.62  ? 41  MET   B CA  1 
ATOM   584  C C   . MET   B 2 32  ? -30.176 1.187   -15.984 1.00 37.01  ? 41  MET   B C   1 
ATOM   585  O O   . MET   B 2 32  ? -30.403 0.969   -17.178 1.00 31.99  ? 41  MET   B O   1 
ATOM   586  C CB  . MET   B 2 32  ? -30.342 3.708   -15.993 1.00 40.68  ? 41  MET   B CB  1 
ATOM   587  C CG  . MET   B 2 32  ? -31.612 3.899   -15.194 1.00 47.88  ? 41  MET   B CG  1 
ATOM   588  S SD  . MET   B 2 32  ? -31.271 4.421   -13.489 1.00 48.11  ? 41  MET   B SD  1 
ATOM   589  C CE  . MET   B 2 32  ? -30.644 6.080   -13.733 1.00 44.28  ? 41  MET   B CE  1 
ATOM   590  N N   . GLN   B 2 33  ? -30.476 0.314   -15.031 1.00 37.46  ? 42  GLN   B N   1 
ATOM   591  C CA  . GLN   B 2 33  ? -31.283 -0.900  -15.289 1.00 42.26  ? 42  GLN   B CA  1 
ATOM   592  C C   . GLN   B 2 33  ? -32.182 -1.124  -14.092 1.00 43.03  ? 42  GLN   B C   1 
ATOM   593  O O   . GLN   B 2 33  ? -31.715 -0.904  -12.970 1.00 45.06  ? 42  GLN   B O   1 
ATOM   594  C CB  . GLN   B 2 33  ? -30.390 -2.116  -15.540 1.00 44.44  ? 42  GLN   B CB  1 
ATOM   595  C CG  . GLN   B 2 33  ? -31.154 -3.284  -16.152 1.00 50.46  ? 42  GLN   B CG  1 
ATOM   596  C CD  . GLN   B 2 33  ? -30.248 -4.444  -16.493 1.00 54.59  ? 42  GLN   B CD  1 
ATOM   597  O OE1 . GLN   B 2 33  ? -30.446 -5.562  -16.007 1.00 53.46  ? 42  GLN   B OE1 1 
ATOM   598  N NE2 . GLN   B 2 33  ? -29.216 -4.178  -17.287 1.00 51.24  ? 42  GLN   B NE2 1 
ATOM   599  N N   . GLU   B 2 34  ? -33.419 -1.528  -14.331 1.00 48.41  ? 43  GLU   B N   1 
ATOM   600  C CA  . GLU   B 2 34  ? -34.418 -1.819  -13.271 1.00 49.96  ? 43  GLU   B CA  1 
ATOM   601  C C   . GLU   B 2 34  ? -34.456 -0.697  -12.220 1.00 48.56  ? 43  GLU   B C   1 
ATOM   602  O O   . GLU   B 2 34  ? -34.662 -1.000  -11.045 1.00 52.72  ? 43  GLU   B O   1 
ATOM   603  C CB  . GLU   B 2 34  ? -34.081 -3.178  -12.656 1.00 58.01  ? 43  GLU   B CB  1 
ATOM   604  C CG  . GLU   B 2 34  ? -34.373 -4.344  -13.596 1.00 63.34  ? 43  GLU   B CG  1 
ATOM   605  C CD  . GLU   B 2 34  ? -33.629 -5.639  -13.305 1.00 64.53  ? 43  GLU   B CD  1 
ATOM   606  O OE1 . GLU   B 2 34  ? -34.034 -6.350  -12.383 1.00 67.11  ? 43  GLU   B OE1 1 
ATOM   607  O OE2 . GLU   B 2 34  ? -32.649 -5.930  -14.012 1.00 69.08  ? 43  GLU   B OE2 1 
ATOM   608  N N   . GLY   B 2 35  ? -34.281 0.561   -12.613 1.00 43.45  ? 44  GLY   B N   1 
ATOM   609  C CA  . GLY   B 2 35  ? -34.467 1.704   -11.698 1.00 43.94  ? 44  GLY   B CA  1 
ATOM   610  C C   . GLY   B 2 35  ? -33.256 1.957   -10.834 1.00 46.22  ? 44  GLY   B C   1 
ATOM   611  O O   . GLY   B 2 35  ? -33.305 2.880   -9.989  1.00 52.69  ? 44  GLY   B O   1 
ATOM   612  N N   . VAL   B 2 36  ? -32.171 1.225   -11.078 1.00 43.70  ? 45  VAL   B N   1 
ATOM   613  C CA  . VAL   B 2 36  ? -30.912 1.306   -10.287 1.00 39.86  ? 45  VAL   B CA  1 
ATOM   614  C C   . VAL   B 2 36  ? -29.823 1.807   -11.213 1.00 39.00  ? 45  VAL   B C   1 
ATOM   615  O O   . VAL   B 2 36  ? -29.752 1.287   -12.342 1.00 40.11  ? 45  VAL   B O   1 
ATOM   616  C CB  . VAL   B 2 36  ? -30.570 -0.051  -9.636  1.00 40.90  ? 45  VAL   B CB  1 
ATOM   617  C CG1 . VAL   B 2 36  ? -29.125 -0.118  -9.128  1.00 40.24  ? 45  VAL   B CG1 1 
ATOM   618  C CG2 . VAL   B 2 36  ? -31.548 -0.325  -8.511  1.00 42.75  ? 45  VAL   B CG2 1 
ATOM   619  N N   . PHE   B 2 37  ? -29.045 2.799   -10.769 1.00 36.26  ? 46  PHE   B N   1 
ATOM   620  C CA  . PHE   B 2 37  ? -27.912 3.345   -11.545 1.00 34.60  ? 46  PHE   B CA  1 
ATOM   621  C C   . PHE   B 2 37  ? -26.605 2.742   -11.022 1.00 33.73  ? 46  PHE   B C   1 
ATOM   622  O O   . PHE   B 2 37  ? -26.313 2.896   -9.841  1.00 36.02  ? 46  PHE   B O   1 
ATOM   623  C CB  . PHE   B 2 37  ? -27.864 4.863   -11.461 1.00 33.56  ? 46  PHE   B CB  1 
ATOM   624  C CG  . PHE   B 2 37  ? -26.862 5.466   -12.406 1.00 32.44  ? 46  PHE   B CG  1 
ATOM   625  C CD1 . PHE   B 2 37  ? -27.048 5.372   -13.778 1.00 33.47  ? 46  PHE   B CD1 1 
ATOM   626  C CD2 . PHE   B 2 37  ? -25.742 6.122   -11.928 1.00 32.85  ? 46  PHE   B CD2 1 
ATOM   627  C CE1 . PHE   B 2 37  ? -26.129 5.925   -14.656 1.00 36.94  ? 46  PHE   B CE1 1 
ATOM   628  C CE2 . PHE   B 2 37  ? -24.804 6.645   -12.807 1.00 35.26  ? 46  PHE   B CE2 1 
ATOM   629  C CZ  . PHE   B 2 37  ? -25.008 6.561   -14.170 1.00 35.14  ? 46  PHE   B CZ  1 
ATOM   630  N N   . HIS   B 2 38  ? -25.836 2.136   -11.928 1.00 34.33  ? 47  HIS   B N   1 
ATOM   631  C CA  . HIS   B 2 38  ? -24.578 1.387   -11.654 1.00 30.65  ? 47  HIS   B CA  1 
ATOM   632  C C   . HIS   B 2 38  ? -23.361 2.137   -12.204 1.00 28.60  ? 47  HIS   B C   1 
ATOM   633  O O   . HIS   B 2 38  ? -23.311 2.437   -13.424 1.00 31.84  ? 47  HIS   B O   1 
ATOM   634  C CB  . HIS   B 2 38  ? -24.654 0.033   -12.333 1.00 29.67  ? 47  HIS   B CB  1 
ATOM   635  C CG  . HIS   B 2 38  ? -25.862 -0.764  -12.015 1.00 29.00  ? 47  HIS   B CG  1 
ATOM   636  N ND1 . HIS   B 2 38  ? -27.092 -0.483  -12.564 1.00 32.44  ? 47  HIS   B ND1 1 
ATOM   637  C CD2 . HIS   B 2 38  ? -26.019 -1.870  -11.264 1.00 29.34  ? 47  HIS   B CD2 1 
ATOM   638  C CE1 . HIS   B 2 38  ? -27.984 -1.377  -12.138 1.00 31.96  ? 47  HIS   B CE1 1 
ATOM   639  N NE2 . HIS   B 2 38  ? -27.342 -2.234  -11.313 1.00 34.50  ? 47  HIS   B NE2 1 
ATOM   640  N N   . THR   B 2 39  ? -22.369 2.429   -11.373 1.00 31.94  ? 48  THR   B N   1 
ATOM   641  C CA  . THR   B 2 39  ? -21.129 3.037   -11.903 1.00 32.13  ? 48  THR   B CA  1 
ATOM   642  C C   . THR   B 2 39  ? -19.950 2.470   -11.118 1.00 33.89  ? 48  THR   B C   1 
ATOM   643  O O   . THR   B 2 39  ? -20.148 1.582   -10.265 1.00 30.01  ? 48  THR   B O   1 
ATOM   644  C CB  . THR   B 2 39  ? -21.287 4.563   -11.935 1.00 35.16  ? 48  THR   B CB  1 
ATOM   645  O OG1 . THR   B 2 39  ? -20.226 5.150   -12.676 1.00 34.56  ? 48  THR   B OG1 1 
ATOM   646  C CG2 . THR   B 2 39  ? -21.285 5.205   -10.569 1.00 36.02  ? 48  THR   B CG2 1 
ATOM   647  N N   . MET   B 2 40  ? -18.769 3.011   -11.360 1.00 39.18  ? 49  MET   B N   1 
ATOM   648  C CA  . MET   B 2 40  ? -17.547 2.687   -10.590 1.00 38.69  ? 49  MET   B CA  1 
ATOM   649  C C   . MET   B 2 40  ? -17.337 3.690   -9.448  1.00 40.21  ? 49  MET   B C   1 
ATOM   650  O O   . MET   B 2 40  ? -17.557 4.910   -9.630  1.00 36.06  ? 49  MET   B O   1 
ATOM   651  C CB  . MET   B 2 40  ? -16.363 2.713   -11.550 1.00 43.36  ? 49  MET   B CB  1 
ATOM   652  C CG  . MET   B 2 40  ? -16.624 1.841   -12.807 1.00 39.19  ? 49  MET   B CG  1 
ATOM   653  S SD  . MET   B 2 40  ? -15.146 0.936   -13.176 1.00 54.73  ? 49  MET   B SD  1 
ATOM   654  C CE  . MET   B 2 40  ? -15.366 -0.575  -12.240 1.00 46.65  ? 49  MET   B CE  1 
ATOM   655  N N   A TRP   B 2 41  ? -16.888 3.182   -8.297  0.19 37.35  ? 50  TRP   B N   1 
ATOM   656  N N   B TRP   B 2 41  ? -16.892 3.193   -8.293  0.23 36.85  ? 50  TRP   B N   1 
ATOM   657  N N   C TRP   B 2 41  ? -16.888 3.183   -8.296  0.25 37.12  ? 50  TRP   B N   1 
ATOM   658  N N   D TRP   B 2 41  ? -16.892 3.193   -8.293  0.25 36.76  ? 50  TRP   B N   1 
ATOM   659  C CA  A TRP   B 2 41  ? -16.714 3.956   -7.041  0.19 37.13  ? 50  TRP   B CA  1 
ATOM   660  C CA  B TRP   B 2 41  ? -16.750 3.994   -7.052  0.23 36.46  ? 50  TRP   B CA  1 
ATOM   661  C CA  C TRP   B 2 41  ? -16.713 3.956   -7.041  0.25 36.88  ? 50  TRP   B CA  1 
ATOM   662  C CA  D TRP   B 2 41  ? -16.750 3.994   -7.052  0.25 36.37  ? 50  TRP   B CA  1 
ATOM   663  C C   A TRP   B 2 41  ? -15.818 5.175   -7.290  0.19 37.82  ? 50  TRP   B C   1 
ATOM   664  C C   B TRP   B 2 41  ? -15.816 5.188   -7.288  0.23 37.40  ? 50  TRP   B C   1 
ATOM   665  C C   C TRP   B 2 41  ? -15.815 5.174   -7.285  0.25 37.69  ? 50  TRP   B C   1 
ATOM   666  C C   D TRP   B 2 41  ? -15.815 5.187   -7.285  0.25 37.36  ? 50  TRP   B C   1 
ATOM   667  O O   A TRP   B 2 41  ? -16.154 6.259   -6.782  0.19 38.20  ? 50  TRP   B O   1 
ATOM   668  O O   B TRP   B 2 41  ? -16.120 6.273   -6.762  0.23 37.78  ? 50  TRP   B O   1 
ATOM   669  O O   C TRP   B 2 41  ? -16.148 6.256   -6.773  0.25 38.16  ? 50  TRP   B O   1 
ATOM   670  O O   D TRP   B 2 41  ? -16.119 6.271   -6.760  0.25 37.76  ? 50  TRP   B O   1 
ATOM   671  C CB  A TRP   B 2 41  ? -16.156 3.076   -5.916  0.19 36.97  ? 50  TRP   B CB  1 
ATOM   672  C CB  B TRP   B 2 41  ? -16.268 3.132   -5.880  0.23 36.09  ? 50  TRP   B CB  1 
ATOM   673  C CB  C TRP   B 2 41  ? -16.156 3.073   -5.918  0.25 36.81  ? 50  TRP   B CB  1 
ATOM   674  C CB  D TRP   B 2 41  ? -16.269 3.132   -5.881  0.25 36.04  ? 50  TRP   B CB  1 
ATOM   675  C CG  A TRP   B 2 41  ? -16.239 3.743   -4.579  0.19 37.06  ? 50  TRP   B CG  1 
ATOM   676  C CG  B TRP   B 2 41  ? -16.060 3.948   -4.644  0.23 35.93  ? 50  TRP   B CG  1 
ATOM   677  C CG  C TRP   B 2 41  ? -16.239 3.739   -4.581  0.25 36.98  ? 50  TRP   B CG  1 
ATOM   678  C CG  D TRP   B 2 41  ? -16.060 3.949   -4.646  0.25 35.91  ? 50  TRP   B CG  1 
ATOM   679  C CD1 A TRP   B 2 41  ? -17.223 3.592   -3.647  0.19 36.97  ? 50  TRP   B CD1 1 
ATOM   680  C CD1 B TRP   B 2 41  ? -14.939 4.646   -4.309  0.23 35.04  ? 50  TRP   B CD1 1 
ATOM   681  C CD1 C TRP   B 2 41  ? -17.223 3.588   -3.649  0.25 36.90  ? 50  TRP   B CD1 1 
ATOM   682  C CD1 D TRP   B 2 41  ? -14.939 4.648   -4.312  0.25 34.99  ? 50  TRP   B CD1 1 
ATOM   683  C CD2 A TRP   B 2 41  ? -15.332 4.725   -4.047  0.19 36.59  ? 50  TRP   B CD2 1 
ATOM   684  C CD2 B TRP   B 2 41  ? -17.025 4.226   -3.615  0.23 36.47  ? 50  TRP   B CD2 1 
ATOM   685  C CD2 C TRP   B 2 41  ? -15.333 4.724   -4.050  0.25 36.41  ? 50  TRP   B CD2 1 
ATOM   686  C CD2 D TRP   B 2 41  ? -17.025 4.223   -3.615  0.25 36.52  ? 50  TRP   B CD2 1 
ATOM   687  N NE1 A TRP   B 2 41  ? -16.976 4.388   -2.561  0.19 37.39  ? 50  TRP   B NE1 1 
ATOM   688  N NE1 B TRP   B 2 41  ? -15.125 5.312   -3.130  0.23 34.87  ? 50  TRP   B NE1 1 
ATOM   689  N NE1 C TRP   B 2 41  ? -16.974 4.384   -2.563  0.25 37.42  ? 50  TRP   B NE1 1 
ATOM   690  N NE1 D TRP   B 2 41  ? -15.127 5.312   -3.131  0.25 34.82  ? 50  TRP   B NE1 1 
ATOM   691  C CE2 A TRP   B 2 41  ? -15.827 5.100   -2.781  0.19 36.89  ? 50  TRP   B CE2 1 
ATOM   692  C CE2 B TRP   B 2 41  ? -16.394 5.073   -2.678  0.23 35.35  ? 50  TRP   B CE2 1 
ATOM   693  C CE2 C TRP   B 2 41  ? -15.827 5.098   -2.784  0.25 36.77  ? 50  TRP   B CE2 1 
ATOM   694  C CE2 D TRP   B 2 41  ? -16.396 5.071   -2.679  0.25 35.33  ? 50  TRP   B CE2 1 
ATOM   695  C CE3 A TRP   B 2 41  ? -14.147 5.314   -4.506  0.19 37.92  ? 50  TRP   B CE3 1 
ATOM   696  C CE3 B TRP   B 2 41  ? -18.348 3.836   -3.383  0.23 36.62  ? 50  TRP   B CE3 1 
ATOM   697  C CE3 C TRP   B 2 41  ? -14.150 5.313   -4.510  0.25 38.06  ? 50  TRP   B CE3 1 
ATOM   698  C CE3 D TRP   B 2 41  ? -18.347 3.832   -3.382  0.25 36.68  ? 50  TRP   B CE3 1 
ATOM   699  C CZ2 A TRP   B 2 41  ? -15.177 6.033   -1.973  0.19 37.85  ? 50  TRP   B CZ2 1 
ATOM   700  C CZ2 B TRP   B 2 41  ? -17.039 5.526   -1.527  0.23 35.47  ? 50  TRP   B CZ2 1 
ATOM   701  C CZ2 C TRP   B 2 41  ? -15.177 6.032   -1.977  0.25 37.94  ? 50  TRP   B CZ2 1 
ATOM   702  C CZ2 D TRP   B 2 41  ? -17.040 5.522   -1.527  0.25 35.46  ? 50  TRP   B CZ2 1 
ATOM   703  C CZ3 A TRP   B 2 41  ? -13.503 6.233   -3.705  0.19 37.26  ? 50  TRP   B CZ3 1 
ATOM   704  C CZ3 B TRP   B 2 41  ? -18.982 4.280   -2.242  0.23 36.72  ? 50  TRP   B CZ3 1 
ATOM   705  C CZ3 C TRP   B 2 41  ? -13.506 6.231   -3.708  0.25 37.20  ? 50  TRP   B CZ3 1 
ATOM   706  C CZ3 D TRP   B 2 41  ? -18.981 4.273   -2.240  0.25 36.82  ? 50  TRP   B CZ3 1 
ATOM   707  C CH2 A TRP   B 2 41  ? -14.014 6.590   -2.457  0.19 38.28  ? 50  TRP   B CH2 1 
ATOM   708  C CH2 B TRP   B 2 41  ? -18.335 5.115   -1.328  0.23 35.53  ? 50  TRP   B CH2 1 
ATOM   709  C CH2 C TRP   B 2 41  ? -14.016 6.589   -2.461  0.25 38.46  ? 50  TRP   B CH2 1 
ATOM   710  C CH2 D TRP   B 2 41  ? -18.336 5.108   -1.326  0.25 35.54  ? 50  TRP   B CH2 1 
ATOM   711  N N   . HIS   B 2 42  ? -14.720 5.008   -8.035  1.00 39.31  ? 51  HIS   B N   1 
ATOM   712  C CA  . HIS   B 2 42  ? -13.709 6.096   -8.218  1.00 39.35  ? 51  HIS   B CA  1 
ATOM   713  C C   . HIS   B 2 42  ? -14.304 7.290   -9.008  1.00 41.30  ? 51  HIS   B C   1 
ATOM   714  O O   . HIS   B 2 42  ? -13.679 8.349   -9.001  1.00 38.27  ? 51  HIS   B O   1 
ATOM   715  C CB  . HIS   B 2 42  ? -12.380 5.589   -8.805  1.00 39.19  ? 51  HIS   B CB  1 
ATOM   716  C CG  . HIS   B 2 42  ? -12.398 5.346   -10.273 1.00 38.42  ? 51  HIS   B CG  1 
ATOM   717  N ND1 . HIS   B 2 42  ? -12.571 4.074   -10.803 1.00 36.54  ? 51  HIS   B ND1 1 
ATOM   718  C CD2 . HIS   B 2 42  ? -12.266 6.183   -11.326 1.00 42.67  ? 51  HIS   B CD2 1 
ATOM   719  C CE1 . HIS   B 2 42  ? -12.578 4.143   -12.115 1.00 35.63  ? 51  HIS   B CE1 1 
ATOM   720  N NE2 . HIS   B 2 42  ? -12.401 5.427   -12.469 1.00 40.15  ? 51  HIS   B NE2 1 
ATOM   721  N N   . VAL   B 2 43  ? -15.459 7.132   -9.657  1.00 41.19  ? 52  VAL   B N   1 
ATOM   722  C CA  . VAL   B 2 43  ? -16.145 8.213   -10.427 1.00 40.86  ? 52  VAL   B CA  1 
ATOM   723  C C   . VAL   B 2 43  ? -16.874 9.183   -9.483  1.00 40.68  ? 52  VAL   B C   1 
ATOM   724  O O   . VAL   B 2 43  ? -16.705 10.397  -9.642  1.00 41.74  ? 52  VAL   B O   1 
ATOM   725  C CB  . VAL   B 2 43  ? -17.140 7.591   -11.419 1.00 44.12  ? 52  VAL   B CB  1 
ATOM   726  C CG1 . VAL   B 2 43  ? -18.064 8.621   -12.049 1.00 43.98  ? 52  VAL   B CG1 1 
ATOM   727  C CG2 . VAL   B 2 43  ? -16.439 6.773   -12.490 1.00 43.19  ? 52  VAL   B CG2 1 
ATOM   728  N N   . THR   B 2 44  ? -17.740 8.672   -8.607  1.00 38.66  ? 53  THR   B N   1 
ATOM   729  C CA  . THR   B 2 44  ? -18.647 9.486   -7.746  1.00 35.29  ? 53  THR   B CA  1 
ATOM   730  C C   . THR   B 2 44  ? -18.001 9.702   -6.377  1.00 39.86  ? 53  THR   B C   1 
ATOM   731  O O   . THR   B 2 44  ? -18.343 10.706  -5.733  1.00 41.62  ? 53  THR   B O   1 
ATOM   732  C CB  . THR   B 2 44  ? -20.020 8.819   -7.669  1.00 33.85  ? 53  THR   B CB  1 
ATOM   733  O OG1 . THR   B 2 44  ? -19.876 7.556   -7.037  1.00 28.57  ? 53  THR   B OG1 1 
ATOM   734  C CG2 . THR   B 2 44  ? -20.607 8.534   -9.033  1.00 32.92  ? 53  THR   B CG2 1 
ATOM   735  N N   . LYS   B 2 45  ? -17.082 8.810   -5.988  1.00 44.40  ? 54  LYS   B N   1 
ATOM   736  C CA  . LYS   B 2 45  ? -16.564 8.679   -4.608  1.00 48.24  ? 54  LYS   B CA  1 
ATOM   737  C C   . LYS   B 2 45  ? -17.734 8.431   -3.651  1.00 44.90  ? 54  LYS   B C   1 
ATOM   738  O O   . LYS   B 2 45  ? -17.612 8.788   -2.468  1.00 53.06  ? 54  LYS   B O   1 
ATOM   739  C CB  . LYS   B 2 45  ? -15.797 9.936   -4.193  1.00 53.54  ? 54  LYS   B CB  1 
ATOM   740  C CG  . LYS   B 2 45  ? -14.613 10.274  -5.072  1.00 61.43  ? 54  LYS   B CG  1 
ATOM   741  C CD  . LYS   B 2 45  ? -13.477 9.299   -4.927  1.00 63.72  ? 54  LYS   B CD  1 
ATOM   742  C CE  . LYS   B 2 45  ? -12.169 9.880   -5.425  1.00 71.56  ? 54  LYS   B CE  1 
ATOM   743  N NZ  . LYS   B 2 45  ? -11.980 9.612   -6.872  1.00 68.81  ? 54  LYS   B NZ  1 
ATOM   744  N N   . GLY   B 2 46  ? -18.816 7.824   -4.129  1.00 46.23  ? 55  GLY   B N   1 
ATOM   745  C CA  . GLY   B 2 46  ? -20.026 7.577   -3.324  1.00 41.41  ? 55  GLY   B CA  1 
ATOM   746  C C   . GLY   B 2 46  ? -20.880 8.819   -3.103  1.00 44.48  ? 55  GLY   B C   1 
ATOM   747  O O   . GLY   B 2 46  ? -21.797 8.734   -2.327  1.00 44.72  ? 55  GLY   B O   1 
ATOM   748  N N   . ALA   B 2 47  ? -20.644 9.916   -3.813  1.00 45.71  ? 56  ALA   B N   1 
ATOM   749  C CA  . ALA   B 2 47  ? -21.428 11.166  -3.687  1.00 42.33  ? 56  ALA   B CA  1 
ATOM   750  C C   . ALA   B 2 47  ? -22.778 10.992  -4.399  1.00 44.29  ? 56  ALA   B C   1 
ATOM   751  O O   . ALA   B 2 47  ? -22.875 10.182  -5.335  1.00 50.81  ? 56  ALA   B O   1 
ATOM   752  C CB  . ALA   B 2 47  ? -20.630 12.327  -4.238  1.00 39.90  ? 56  ALA   B CB  1 
ATOM   753  N N   . ALA   B 2 48  ? -23.801 11.726  -3.965  1.00 44.28  ? 57  ALA   B N   1 
ATOM   754  C CA  . ALA   B 2 48  ? -25.138 11.740  -4.590  1.00 43.04  ? 57  ALA   B CA  1 
ATOM   755  C C   . ALA   B 2 48  ? -25.044 12.388  -5.975  1.00 39.11  ? 57  ALA   B C   1 
ATOM   756  O O   . ALA   B 2 48  ? -24.024 13.057  -6.245  1.00 50.10  ? 57  ALA   B O   1 
ATOM   757  C CB  . ALA   B 2 48  ? -26.124 12.467  -3.715  1.00 45.16  ? 57  ALA   B CB  1 
ATOM   758  N N   . LEU   B 2 49  ? -26.099 12.209  -6.773  1.00 39.60  ? 58  LEU   B N   1 
ATOM   759  C CA  . LEU   B 2 49  ? -26.212 12.554  -8.218  1.00 44.97  ? 58  LEU   B CA  1 
ATOM   760  C C   . LEU   B 2 49  ? -27.544 13.263  -8.504  1.00 47.69  ? 58  LEU   B C   1 
ATOM   761  O O   . LEU   B 2 49  ? -28.582 12.934  -7.902  1.00 46.06  ? 58  LEU   B O   1 
ATOM   762  C CB  . LEU   B 2 49  ? -26.140 11.274  -9.064  1.00 44.09  ? 58  LEU   B CB  1 
ATOM   763  C CG  . LEU   B 2 49  ? -24.880 10.423  -8.894  1.00 43.04  ? 58  LEU   B CG  1 
ATOM   764  C CD1 . LEU   B 2 49  ? -24.986 9.143   -9.692  1.00 42.07  ? 58  LEU   B CD1 1 
ATOM   765  C CD2 . LEU   B 2 49  ? -23.624 11.193  -9.271  1.00 43.43  ? 58  LEU   B CD2 1 
ATOM   766  N N   . ARG   B 2 50  ? -27.532 14.179  -9.455  1.00 48.02  ? 59  ARG   B N   1 
ATOM   767  C CA  . ARG   B 2 50  ? -28.762 14.858  -9.901  1.00 51.02  ? 59  ARG   B CA  1 
ATOM   768  C C   . ARG   B 2 50  ? -29.190 14.186  -11.212 1.00 49.81  ? 59  ARG   B C   1 
ATOM   769  O O   . ARG   B 2 50  ? -28.333 13.764  -11.994 1.00 47.02  ? 59  ARG   B O   1 
ATOM   770  C CB  . ARG   B 2 50  ? -28.469 16.360  -9.955  1.00 64.28  ? 59  ARG   B CB  1 
ATOM   771  C CG  . ARG   B 2 50  ? -29.627 17.218  -10.443 1.00 74.91  ? 59  ARG   B CG  1 
ATOM   772  C CD  . ARG   B 2 50  ? -29.415 18.691  -10.148 1.00 77.22  ? 59  ARG   B CD  1 
ATOM   773  N NE  . ARG   B 2 50  ? -28.069 19.177  -10.460 1.00 81.19  ? 59  ARG   B NE  1 
ATOM   774  C CZ  . ARG   B 2 50  ? -27.620 19.508  -11.675 1.00 79.56  ? 59  ARG   B CZ  1 
ATOM   775  N NH1 . ARG   B 2 50  ? -28.382 19.363  -12.749 1.00 73.76  ? 59  ARG   B NH1 1 
ATOM   776  N NH2 . ARG   B 2 50  ? -26.388 19.971  -11.809 1.00 84.25  ? 59  ARG   B NH2 1 
ATOM   777  N N   . SER   B 2 51  ? -30.485 13.999  -11.388 1.00 56.13  ? 60  SER   B N   1 
ATOM   778  C CA  . SER   B 2 51  ? -31.100 13.572  -12.668 1.00 63.67  ? 60  SER   B CA  1 
ATOM   779  C C   . SER   B 2 51  ? -32.223 14.555  -13.030 1.00 68.76  ? 60  SER   B C   1 
ATOM   780  O O   . SER   B 2 51  ? -33.394 14.282  -12.711 1.00 70.96  ? 60  SER   B O   1 
ATOM   781  C CB  . SER   B 2 51  ? -31.589 12.167  -12.583 1.00 54.25  ? 60  SER   B CB  1 
ATOM   782  O OG  . SER   B 2 51  ? -32.145 11.808  -13.828 1.00 56.67  ? 60  SER   B OG  1 
ATOM   783  N N   . GLY   B 2 52  ? -31.861 15.671  -13.661 1.00 78.76  ? 61  GLY   B N   1 
ATOM   784  C CA  . GLY   B 2 52  ? -32.747 16.837  -13.817 1.00 92.84  ? 61  GLY   B CA  1 
ATOM   785  C C   . GLY   B 2 52  ? -32.876 17.579  -12.500 1.00 96.72  ? 61  GLY   B C   1 
ATOM   786  O O   . GLY   B 2 52  ? -31.939 18.324  -12.149 1.00 105.84 ? 61  GLY   B O   1 
ATOM   787  N N   . GLU   B 2 53  ? -33.991 17.379  -11.793 1.00 95.52  ? 62  GLU   B N   1 
ATOM   788  C CA  . GLU   B 2 53  ? -34.177 17.854  -10.399 1.00 98.85  ? 62  GLU   B CA  1 
ATOM   789  C C   . GLU   B 2 53  ? -34.604 16.683  -9.507  1.00 88.37  ? 62  GLU   B C   1 
ATOM   790  O O   . GLU   B 2 53  ? -35.095 16.957  -8.408  1.00 86.78  ? 62  GLU   B O   1 
ATOM   791  C CB  . GLU   B 2 53  ? -35.148 19.035  -10.384 1.00 105.24 ? 62  GLU   B CB  1 
ATOM   792  C CG  . GLU   B 2 53  ? -34.477 20.331  -10.795 1.00 118.50 ? 62  GLU   B CG  1 
ATOM   793  C CD  . GLU   B 2 53  ? -35.295 21.581  -10.538 1.00 125.47 ? 62  GLU   B CD  1 
ATOM   794  O OE1 . GLU   B 2 53  ? -36.496 21.564  -10.852 1.00 134.78 ? 62  GLU   B OE1 1 
ATOM   795  O OE2 . GLU   B 2 53  ? -34.729 22.562  -10.012 1.00 130.30 ? 62  GLU   B OE2 1 
ATOM   796  N N   . GLY   B 2 54  ? -34.391 15.440  -9.965  1.00 84.82  ? 63  GLY   B N   1 
ATOM   797  C CA  . GLY   B 2 54  ? -34.464 14.205  -9.158  1.00 75.83  ? 63  GLY   B CA  1 
ATOM   798  C C   . GLY   B 2 54  ? -33.115 13.921  -8.522  1.00 69.94  ? 63  GLY   B C   1 
ATOM   799  O O   . GLY   B 2 54  ? -32.111 14.306  -9.134  1.00 67.62  ? 63  GLY   B O   1 
ATOM   800  N N   . ARG   B 2 55  ? -33.095 13.312  -7.330  1.00 61.17  ? 64  ARG   B N   1 
ATOM   801  C CA  . ARG   B 2 55  ? -31.861 12.975  -6.563  1.00 57.67  ? 64  ARG   B CA  1 
ATOM   802  C C   . ARG   B 2 55  ? -31.628 11.455  -6.594  1.00 54.36  ? 64  ARG   B C   1 
ATOM   803  O O   . ARG   B 2 55  ? -32.583 10.684  -6.382  1.00 54.48  ? 64  ARG   B O   1 
ATOM   804  C CB  . ARG   B 2 55  ? -31.966 13.469  -5.114  1.00 62.01  ? 64  ARG   B CB  1 
ATOM   805  C CG  . ARG   B 2 55  ? -30.648 13.554  -4.353  1.00 65.82  ? 64  ARG   B CG  1 
ATOM   806  C CD  . ARG   B 2 55  ? -30.864 13.943  -2.890  1.00 73.09  ? 64  ARG   B CD  1 
ATOM   807  N NE  . ARG   B 2 55  ? -29.730 13.630  -2.017  1.00 74.80  ? 64  ARG   B NE  1 
ATOM   808  C CZ  . ARG   B 2 55  ? -28.917 14.512  -1.416  1.00 75.26  ? 64  ARG   B CZ  1 
ATOM   809  N NH1 . ARG   B 2 55  ? -29.088 15.812  -1.569  1.00 77.30  ? 64  ARG   B NH1 1 
ATOM   810  N NH2 . ARG   B 2 55  ? -27.934 14.088  -0.638  1.00 72.06  ? 64  ARG   B NH2 1 
ATOM   811  N N   . LEU   B 2 56  ? -30.391 11.032  -6.854  1.00 48.22  ? 65  LEU   B N   1 
ATOM   812  C CA  . LEU   B 2 56  ? -29.977 9.614   -6.742  1.00 48.44  ? 65  LEU   B CA  1 
ATOM   813  C C   . LEU   B 2 56  ? -29.098 9.496   -5.499  1.00 42.79  ? 65  LEU   B C   1 
ATOM   814  O O   . LEU   B 2 56  ? -28.050 10.177  -5.436  1.00 42.63  ? 65  LEU   B O   1 
ATOM   815  C CB  . LEU   B 2 56  ? -29.222 9.186   -8.014  1.00 48.33  ? 65  LEU   B CB  1 
ATOM   816  C CG  . LEU   B 2 56  ? -29.986 9.218   -9.334  1.00 51.96  ? 65  LEU   B CG  1 
ATOM   817  C CD1 . LEU   B 2 56  ? -29.334 8.292   -10.342 1.00 53.85  ? 65  LEU   B CD1 1 
ATOM   818  C CD2 . LEU   B 2 56  ? -31.439 8.818   -9.150  1.00 54.98  ? 65  LEU   B CD2 1 
ATOM   819  N N   . ASP   B 2 57  ? -29.494 8.669   -4.541  1.00 39.44  ? 66  ASP   B N   1 
ATOM   820  C CA  . ASP   B 2 57  ? -28.657 8.425   -3.341  1.00 41.38  ? 66  ASP   B CA  1 
ATOM   821  C C   . ASP   B 2 57  ? -27.996 7.059   -3.450  1.00 38.55  ? 66  ASP   B C   1 
ATOM   822  O O   . ASP   B 2 57  ? -28.611 6.086   -3.931  1.00 32.28  ? 66  ASP   B O   1 
ATOM   823  C CB  . ASP   B 2 57  ? -29.487 8.546   -2.069  1.00 51.19  ? 66  ASP   B CB  1 
ATOM   824  C CG  . ASP   B 2 57  ? -30.018 9.956   -1.897  1.00 54.44  ? 66  ASP   B CG  1 
ATOM   825  O OD1 . ASP   B 2 57  ? -29.233 10.901  -2.071  1.00 59.24  ? 66  ASP   B OD1 1 
ATOM   826  O OD2 . ASP   B 2 57  ? -31.211 10.091  -1.661  1.00 64.39  ? 66  ASP   B OD2 1 
ATOM   827  N N   . PRO   B 2 58  ? -26.728 6.951   -2.994  1.00 35.85  ? 67  PRO   B N   1 
ATOM   828  C CA  . PRO   B 2 58  ? -26.007 5.684   -3.038  1.00 35.99  ? 67  PRO   B CA  1 
ATOM   829  C C   . PRO   B 2 58  ? -26.753 4.709   -2.129  1.00 42.60  ? 67  PRO   B C   1 
ATOM   830  O O   . PRO   B 2 58  ? -27.393 5.139   -1.169  1.00 41.77  ? 67  PRO   B O   1 
ATOM   831  C CB  . PRO   B 2 58  ? -24.617 6.005   -2.504  1.00 38.52  ? 67  PRO   B CB  1 
ATOM   832  C CG  . PRO   B 2 58  ? -24.828 7.255   -1.677  1.00 38.04  ? 67  PRO   B CG  1 
ATOM   833  C CD  . PRO   B 2 58  ? -25.922 8.021   -2.387  1.00 35.91  ? 67  PRO   B CD  1 
ATOM   834  N N   . TYR   B 2 59  ? -26.691 3.437   -2.494  1.00 34.06  ? 68  TYR   B N   1 
ATOM   835  C CA  . TYR   B 2 59  ? -27.374 2.328   -1.800  1.00 34.71  ? 68  TYR   B CA  1 
ATOM   836  C C   . TYR   B 2 59  ? -26.343 1.278   -1.408  1.00 33.34  ? 68  TYR   B C   1 
ATOM   837  O O   . TYR   B 2 59  ? -26.419 0.815   -0.287  1.00 34.36  ? 68  TYR   B O   1 
ATOM   838  C CB  . TYR   B 2 59  ? -28.448 1.761   -2.714  1.00 35.60  ? 68  TYR   B CB  1 
ATOM   839  C CG  . TYR   B 2 59  ? -29.269 0.659   -2.110  1.00 34.46  ? 68  TYR   B CG  1 
ATOM   840  C CD1 . TYR   B 2 59  ? -28.797 -0.636  -2.134  1.00 36.35  ? 68  TYR   B CD1 1 
ATOM   841  C CD2 . TYR   B 2 59  ? -30.531 0.899   -1.595  1.00 37.29  ? 68  TYR   B CD2 1 
ATOM   842  C CE1 . TYR   B 2 59  ? -29.556 -1.681  -1.628  1.00 41.98  ? 68  TYR   B CE1 1 
ATOM   843  C CE2 . TYR   B 2 59  ? -31.313 -0.142  -1.106  1.00 41.88  ? 68  TYR   B CE2 1 
ATOM   844  C CZ  . TYR   B 2 59  ? -30.818 -1.438  -1.113  1.00 40.90  ? 68  TYR   B CZ  1 
ATOM   845  O OH  . TYR   B 2 59  ? -31.518 -2.498  -0.602  1.00 40.47  ? 68  TYR   B OH  1 
ATOM   846  N N   . TRP   B 2 60  ? -25.464 0.887   -2.330  1.00 32.87  ? 69  TRP   B N   1 
ATOM   847  C CA  . TRP   B 2 60  ? -24.393 -0.125  -2.073  1.00 32.58  ? 69  TRP   B CA  1 
ATOM   848  C C   . TRP   B 2 60  ? -23.091 0.357   -2.706  1.00 32.10  ? 69  TRP   B C   1 
ATOM   849  O O   . TRP   B 2 60  ? -23.144 1.030   -3.745  1.00 37.52  ? 69  TRP   B O   1 
ATOM   850  C CB  . TRP   B 2 60  ? -24.787 -1.531  -2.543  1.00 29.52  ? 69  TRP   B CB  1 
ATOM   851  C CG  . TRP   B 2 60  ? -23.633 -2.484  -2.536  1.00 32.97  ? 69  TRP   B CG  1 
ATOM   852  C CD1 . TRP   B 2 60  ? -23.199 -3.247  -1.492  1.00 32.41  ? 69  TRP   B CD1 1 
ATOM   853  C CD2 . TRP   B 2 60  ? -22.727 -2.750  -3.626  1.00 33.30  ? 69  TRP   B CD2 1 
ATOM   854  N NE1 . TRP   B 2 60  ? -22.064 -3.933  -1.846  1.00 32.45  ? 69  TRP   B NE1 1 
ATOM   855  C CE2 . TRP   B 2 60  ? -21.763 -3.671  -3.152  1.00 28.81  ? 69  TRP   B CE2 1 
ATOM   856  C CE3 . TRP   B 2 60  ? -22.625 -2.291  -4.943  1.00 31.87  ? 69  TRP   B CE3 1 
ATOM   857  C CZ2 . TRP   B 2 60  ? -20.716 -4.130  -3.940  1.00 27.32  ? 69  TRP   B CZ2 1 
ATOM   858  C CZ3 . TRP   B 2 60  ? -21.603 -2.780  -5.741  1.00 32.82  ? 69  TRP   B CZ3 1 
ATOM   859  C CH2 . TRP   B 2 60  ? -20.671 -3.698  -5.247  1.00 32.72  ? 69  TRP   B CH2 1 
ATOM   860  N N   . GLY   B 2 61  ? -21.964 0.029   -2.088  1.00 31.87  ? 70  GLY   B N   1 
ATOM   861  C CA  . GLY   B 2 61  ? -20.646 0.344   -2.666  1.00 34.73  ? 70  GLY   B CA  1 
ATOM   862  C C   . GLY   B 2 61  ? -19.540 -0.387  -1.964  1.00 29.75  ? 70  GLY   B C   1 
ATOM   863  O O   . GLY   B 2 61  ? -19.722 -0.747  -0.795  1.00 33.80  ? 70  GLY   B O   1 
ATOM   864  N N   . ASP   B 2 62  ? -18.429 -0.547  -2.647  1.00 30.58  ? 71  ASP   B N   1 
ATOM   865  C CA  . ASP   B 2 62  ? -17.247 -1.301  -2.172  1.00 30.12  ? 71  ASP   B CA  1 
ATOM   866  C C   . ASP   B 2 62  ? -16.051 -0.796  -2.974  1.00 30.86  ? 71  ASP   B C   1 
ATOM   867  O O   . ASP   B 2 62  ? -15.980 -1.100  -4.205  1.00 37.65  ? 71  ASP   B O   1 
ATOM   868  C CB  . ASP   B 2 62  ? -17.434 -2.796  -2.363  1.00 31.28  ? 71  ASP   B CB  1 
ATOM   869  C CG  . ASP   B 2 62  ? -16.349 -3.701  -1.788  1.00 35.64  ? 71  ASP   B CG  1 
ATOM   870  O OD1 . ASP   B 2 62  ? -15.177 -3.328  -1.757  1.00 47.85  ? 71  ASP   B OD1 1 
ATOM   871  O OD2 . ASP   B 2 62  ? -16.704 -4.792  -1.368  1.00 52.71  ? 71  ASP   B OD2 1 
ATOM   872  N N   . VAL   B 2 63  ? -15.154 -0.094  -2.295  1.00 33.82  ? 72  VAL   B N   1 
ATOM   873  C CA  . VAL   B 2 63  ? -13.923 0.501   -2.874  1.00 31.93  ? 72  VAL   B CA  1 
ATOM   874  C C   . VAL   B 2 63  ? -13.057 -0.614  -3.456  1.00 34.95  ? 72  VAL   B C   1 
ATOM   875  O O   . VAL   B 2 63  ? -12.310 -0.304  -4.378  1.00 36.64  ? 72  VAL   B O   1 
ATOM   876  C CB  . VAL   B 2 63  ? -13.129 1.315   -1.843  1.00 32.43  ? 72  VAL   B CB  1 
ATOM   877  C CG1 . VAL   B 2 63  ? -11.664 1.439   -2.209  1.00 32.24  ? 72  VAL   B CG1 1 
ATOM   878  C CG2 . VAL   B 2 63  ? -13.737 2.685   -1.647  1.00 34.14  ? 72  VAL   B CG2 1 
ATOM   879  N N   . LYS   B 2 64  ? -13.095 -1.833  -2.912  1.00 39.83  ? 73  LYS   B N   1 
ATOM   880  C CA  . LYS   B 2 64  ? -12.157 -2.883  -3.392  1.00 38.10  ? 73  LYS   B CA  1 
ATOM   881  C C   . LYS   B 2 64  ? -12.628 -3.395  -4.760  1.00 39.33  ? 73  LYS   B C   1 
ATOM   882  O O   . LYS   B 2 64  ? -11.760 -3.678  -5.590  1.00 44.98  ? 73  LYS   B O   1 
ATOM   883  C CB  . LYS   B 2 64  ? -12.005 -4.063  -2.437  1.00 35.50  ? 73  LYS   B CB  1 
ATOM   884  C CG  . LYS   B 2 64  ? -10.962 -5.058  -2.944  1.00 39.04  ? 73  LYS   B CG  1 
ATOM   885  C CD  . LYS   B 2 64  ? -10.371 -5.917  -1.871  1.00 40.17  ? 73  LYS   B CD  1 
ATOM   886  C CE  . LYS   B 2 64  ? -9.558  -7.064  -2.432  1.00 48.08  ? 73  LYS   B CE  1 
ATOM   887  N NZ  . LYS   B 2 64  ? -8.770  -7.707  -1.359  1.00 48.22  ? 73  LYS   B NZ  1 
ATOM   888  N N   . GLN   B 2 65  ? -13.940 -3.570  -4.955  1.00 39.85  ? 74  GLN   B N   1 
ATOM   889  C CA  . GLN   B 2 65  ? -14.560 -3.971  -6.237  1.00 41.88  ? 74  GLN   B CA  1 
ATOM   890  C C   . GLN   B 2 65  ? -14.589 -2.775  -7.190  1.00 39.59  ? 74  GLN   B C   1 
ATOM   891  O O   . GLN   B 2 65  ? -14.771 -2.989  -8.419  1.00 42.07  ? 74  GLN   B O   1 
ATOM   892  C CB  . GLN   B 2 65  ? -15.974 -4.491  -6.008  1.00 41.48  ? 74  GLN   B CB  1 
ATOM   893  C CG  . GLN   B 2 65  ? -16.002 -5.845  -5.318  1.00 44.79  ? 74  GLN   B CG  1 
ATOM   894  C CD  . GLN   B 2 65  ? -17.434 -6.302  -5.145  1.00 46.75  ? 74  GLN   B CD  1 
ATOM   895  O OE1 . GLN   B 2 65  ? -18.172 -6.516  -6.115  1.00 48.87  ? 74  GLN   B OE1 1 
ATOM   896  N NE2 . GLN   B 2 65  ? -17.861 -6.374  -3.900  1.00 44.56  ? 74  GLN   B NE2 1 
ATOM   897  N N   . ASP   B 2 66  ? -14.436 -1.578  -6.627  1.00 38.93  ? 75  ASP   B N   1 
ATOM   898  C CA  . ASP   B 2 66  ? -14.548 -0.251  -7.292  1.00 37.98  ? 75  ASP   B CA  1 
ATOM   899  C C   . ASP   B 2 66  ? -15.911 -0.106  -7.936  1.00 36.31  ? 75  ASP   B C   1 
ATOM   900  O O   . ASP   B 2 66  ? -15.933 0.431   -9.072  1.00 35.69  ? 75  ASP   B O   1 
ATOM   901  C CB  . ASP   B 2 66  ? -13.499 -0.063  -8.384  1.00 39.55  ? 75  ASP   B CB  1 
ATOM   902  C CG  . ASP   B 2 66  ? -13.348 1.379   -8.826  1.00 41.33  ? 75  ASP   B CG  1 
ATOM   903  O OD1 . ASP   B 2 66  ? -13.725 2.293   -8.046  1.00 41.49  ? 75  ASP   B OD1 1 
ATOM   904  O OD2 . ASP   B 2 66  ? -12.844 1.573   -9.963  1.00 40.79  ? 75  ASP   B OD2 1 
ATOM   905  N N   . LEU   B 2 67  ? -16.980 -0.566  -7.266  1.00 32.52  ? 76  LEU   B N   1 
ATOM   906  C CA  . LEU   B 2 67  ? -18.373 -0.510  -7.787  1.00 30.20  ? 76  LEU   B CA  1 
ATOM   907  C C   . LEU   B 2 67  ? -19.278 0.288   -6.834  1.00 34.82  ? 76  LEU   B C   1 
ATOM   908  O O   . LEU   B 2 67  ? -18.974 0.382   -5.605  1.00 32.45  ? 76  LEU   B O   1 
ATOM   909  C CB  . LEU   B 2 67  ? -18.881 -1.936  -7.996  1.00 31.10  ? 76  LEU   B CB  1 
ATOM   910  C CG  . LEU   B 2 67  ? -18.228 -2.703  -9.167  1.00 34.32  ? 76  LEU   B CG  1 
ATOM   911  C CD1 . LEU   B 2 67  ? -18.853 -4.087  -9.298  1.00 32.99  ? 76  LEU   B CD1 1 
ATOM   912  C CD2 . LEU   B 2 67  ? -18.366 -1.936  -10.490 1.00 37.28  ? 76  LEU   B CD2 1 
ATOM   913  N N   . VAL   B 2 68  ? -20.348 0.874   -7.369  1.00 34.68  ? 77  VAL   B N   1 
ATOM   914  C CA  . VAL   B 2 68  ? -21.376 1.614   -6.573  1.00 36.25  ? 77  VAL   B CA  1 
ATOM   915  C C   . VAL   B 2 68  ? -22.716 1.559   -7.305  1.00 32.41  ? 77  VAL   B C   1 
ATOM   916  O O   . VAL   B 2 68  ? -22.725 1.626   -8.547  1.00 35.65  ? 77  VAL   B O   1 
ATOM   917  C CB  . VAL   B 2 68  ? -20.926 3.054   -6.247  1.00 36.54  ? 77  VAL   B CB  1 
ATOM   918  C CG1 . VAL   B 2 68  ? -20.642 3.874   -7.488  1.00 36.40  ? 77  VAL   B CG1 1 
ATOM   919  C CG2 . VAL   B 2 68  ? -21.917 3.774   -5.343  1.00 41.90  ? 77  VAL   B CG2 1 
ATOM   920  N N   . SER   B 2 69  ? -23.797 1.363   -6.559  1.00 30.27  ? 78  SER   B N   1 
ATOM   921  C CA  . SER   B 2 69  ? -25.203 1.376   -7.044  1.00 31.85  ? 78  SER   B CA  1 
ATOM   922  C C   . SER   B 2 69  ? -25.997 2.494   -6.342  1.00 34.84  ? 78  SER   B C   1 
ATOM   923  O O   . SER   B 2 69  ? -25.708 2.807   -5.142  1.00 32.75  ? 78  SER   B O   1 
ATOM   924  C CB  . SER   B 2 69  ? -25.861 0.016   -6.886  1.00 30.98  ? 78  SER   B CB  1 
ATOM   925  O OG  . SER   B 2 69  ? -26.215 -0.258  -5.534  1.00 29.54  ? 78  SER   B OG  1 
ATOM   926  N N   . TYR   B 2 70  ? -26.969 3.049   -7.068  1.00 34.55  ? 79  TYR   B N   1 
ATOM   927  C CA  . TYR   B 2 70  ? -27.835 4.188   -6.665  1.00 34.44  ? 79  TYR   B CA  1 
ATOM   928  C C   . TYR   B 2 70  ? -29.292 3.725   -6.791  1.00 32.98  ? 79  TYR   B C   1 
ATOM   929  O O   . TYR   B 2 70  ? -29.647 3.099   -7.813  1.00 31.87  ? 79  TYR   B O   1 
ATOM   930  C CB  . TYR   B 2 70  ? -27.548 5.445   -7.490  1.00 34.17  ? 79  TYR   B CB  1 
ATOM   931  C CG  . TYR   B 2 70  ? -26.218 6.096   -7.194  1.00 31.59  ? 79  TYR   B CG  1 
ATOM   932  C CD1 . TYR   B 2 70  ? -25.037 5.518   -7.633  1.00 38.09  ? 79  TYR   B CD1 1 
ATOM   933  C CD2 . TYR   B 2 70  ? -26.115 7.266   -6.454  1.00 34.33  ? 79  TYR   B CD2 1 
ATOM   934  C CE1 . TYR   B 2 70  ? -23.796 6.081   -7.357  1.00 36.05  ? 79  TYR   B CE1 1 
ATOM   935  C CE2 . TYR   B 2 70  ? -24.883 7.853   -6.171  1.00 35.23  ? 79  TYR   B CE2 1 
ATOM   936  C CZ  . TYR   B 2 70  ? -23.715 7.247   -6.611  1.00 35.43  ? 79  TYR   B CZ  1 
ATOM   937  O OH  . TYR   B 2 70  ? -22.490 7.786   -6.344  1.00 39.06  ? 79  TYR   B OH  1 
ATOM   938  N N   . CYS   B 2 71  ? -30.069 3.956   -5.728  1.00 34.01  ? 80  CYS   B N   1 
ATOM   939  C CA  . CYS   B 2 71  ? -31.540 3.775   -5.637  1.00 35.63  ? 80  CYS   B CA  1 
ATOM   940  C C   . CYS   B 2 71  ? -31.901 2.325   -5.344  1.00 39.81  ? 80  CYS   B C   1 
ATOM   941  O O   . CYS   B 2 71  ? -33.090 2.049   -5.093  1.00 40.41  ? 80  CYS   B O   1 
ATOM   942  C CB  . CYS   B 2 71  ? -32.259 4.205   -6.907  1.00 39.53  ? 80  CYS   B CB  1 
ATOM   943  S SG  . CYS   B 2 71  ? -31.852 5.910   -7.382  1.00 46.64  ? 80  CYS   B SG  1 
ATOM   944  N N   . GLY   B 2 72  ? -30.934 1.413   -5.325  1.00 30.76  ? 81  GLY   B N   1 
ATOM   945  C CA  . GLY   B 2 72  ? -31.326 0.001   -5.159  1.00 32.22  ? 81  GLY   B CA  1 
ATOM   946  C C   . GLY   B 2 72  ? -30.090 -0.875  -5.222  1.00 31.06  ? 81  GLY   B C   1 
ATOM   947  O O   . GLY   B 2 72  ? -28.982 -0.372  -5.482  1.00 27.65  ? 81  GLY   B O   1 
ATOM   948  N N   . PRO   B 2 73  ? -30.241 -2.169  -4.905  1.00 30.39  ? 82  PRO   B N   1 
ATOM   949  C CA  . PRO   B 2 73  ? -29.118 -3.104  -4.986  1.00 35.07  ? 82  PRO   B CA  1 
ATOM   950  C C   . PRO   B 2 73  ? -28.585 -3.328  -6.419  1.00 37.51  ? 82  PRO   B C   1 
ATOM   951  O O   . PRO   B 2 73  ? -29.337 -3.166  -7.369  1.00 38.32  ? 82  PRO   B O   1 
ATOM   952  C CB  . PRO   B 2 73  ? -29.711 -4.398  -4.398  1.00 32.54  ? 82  PRO   B CB  1 
ATOM   953  C CG  . PRO   B 2 73  ? -31.220 -4.272  -4.595  1.00 33.18  ? 82  PRO   B CG  1 
ATOM   954  C CD  . PRO   B 2 73  ? -31.485 -2.788  -4.421  1.00 34.36  ? 82  PRO   B CD  1 
ATOM   955  N N   . TRP   B 2 74  ? -27.303 -3.701  -6.540  1.00 39.01  ? 83  TRP   B N   1 
ATOM   956  C CA  . TRP   B 2 74  ? -26.645 -4.095  -7.815  1.00 40.77  ? 83  TRP   B CA  1 
ATOM   957  C C   . TRP   B 2 74  ? -27.526 -5.110  -8.578  1.00 38.67  ? 83  TRP   B C   1 
ATOM   958  O O   . TRP   B 2 74  ? -27.883 -6.124  -7.995  1.00 45.12  ? 83  TRP   B O   1 
ATOM   959  C CB  . TRP   B 2 74  ? -25.230 -4.627  -7.535  1.00 34.71  ? 83  TRP   B CB  1 
ATOM   960  C CG  . TRP   B 2 74  ? -24.413 -4.812  -8.777  1.00 30.78  ? 83  TRP   B CG  1 
ATOM   961  C CD1 . TRP   B 2 74  ? -24.399 -5.919  -9.577  1.00 28.55  ? 83  TRP   B CD1 1 
ATOM   962  C CD2 . TRP   B 2 74  ? -23.570 -3.830  -9.416  1.00 28.65  ? 83  TRP   B CD2 1 
ATOM   963  N NE1 . TRP   B 2 74  ? -23.603 -5.692  -10.665 1.00 28.79  ? 83  TRP   B NE1 1 
ATOM   964  C CE2 . TRP   B 2 74  ? -23.081 -4.424  -10.600 1.00 28.18  ? 83  TRP   B CE2 1 
ATOM   965  C CE3 . TRP   B 2 74  ? -23.239 -2.491  -9.153  1.00 33.95  ? 83  TRP   B CE3 1 
ATOM   966  C CZ2 . TRP   B 2 74  ? -22.250 -3.743  -11.483 1.00 28.08  ? 83  TRP   B CZ2 1 
ATOM   967  C CZ3 . TRP   B 2 74  ? -22.419 -1.816  -10.027 1.00 34.72  ? 83  TRP   B CZ3 1 
ATOM   968  C CH2 . TRP   B 2 74  ? -21.934 -2.439  -11.187 1.00 30.35  ? 83  TRP   B CH2 1 
ATOM   969  N N   . LYS   B 2 75  ? -27.823 -4.855  -9.857  1.00 42.06  ? 84  LYS   B N   1 
ATOM   970  C CA  . LYS   B 2 75  ? -28.790 -5.644  -10.670 1.00 42.83  ? 84  LYS   B CA  1 
ATOM   971  C C   . LYS   B 2 75  ? -28.096 -6.474  -11.759 1.00 43.46  ? 84  LYS   B C   1 
ATOM   972  O O   . LYS   B 2 75  ? -28.758 -7.334  -12.302 1.00 44.31  ? 84  LYS   B O   1 
ATOM   973  C CB  . LYS   B 2 75  ? -29.762 -4.696  -11.373 1.00 46.06  ? 84  LYS   B CB  1 
ATOM   974  C CG  . LYS   B 2 75  ? -30.614 -3.851  -10.444 1.00 46.97  ? 84  LYS   B CG  1 
ATOM   975  C CD  . LYS   B 2 75  ? -31.667 -4.642  -9.746  1.00 46.38  ? 84  LYS   B CD  1 
ATOM   976  C CE  . LYS   B 2 75  ? -32.422 -3.807  -8.739  1.00 49.54  ? 84  LYS   B CE  1 
ATOM   977  N NZ  . LYS   B 2 75  ? -33.809 -4.305  -8.590  1.00 57.57  ? 84  LYS   B NZ  1 
ATOM   978  N N   . LEU   B 2 76  ? -26.828 -6.215  -12.083 1.00 43.07  ? 85  LEU   B N   1 
ATOM   979  C CA  . LEU   B 2 76  ? -26.168 -6.713  -13.315 1.00 41.34  ? 85  LEU   B CA  1 
ATOM   980  C C   . LEU   B 2 76  ? -25.409 -8.004  -12.983 1.00 47.20  ? 85  LEU   B C   1 
ATOM   981  O O   . LEU   B 2 76  ? -24.365 -7.909  -12.292 1.00 44.31  ? 85  LEU   B O   1 
ATOM   982  C CB  . LEU   B 2 76  ? -25.233 -5.613  -13.832 1.00 40.92  ? 85  LEU   B CB  1 
ATOM   983  C CG  . LEU   B 2 76  ? -25.886 -4.248  -14.101 1.00 37.40  ? 85  LEU   B CG  1 
ATOM   984  C CD1 . LEU   B 2 76  ? -24.871 -3.288  -14.681 1.00 35.75  ? 85  LEU   B CD1 1 
ATOM   985  C CD2 . LEU   B 2 76  ? -27.074 -4.349  -15.043 1.00 39.38  ? 85  LEU   B CD2 1 
ATOM   986  N N   . ASP   B 2 77  ? -25.918 -9.149  -13.462 1.00 47.46  ? 86  ASP   B N   1 
ATOM   987  C CA  . ASP   B 2 77  ? -25.456 -10.503 -13.061 1.00 57.68  ? 86  ASP   B CA  1 
ATOM   988  C C   . ASP   B 2 77  ? -24.883 -11.272 -14.260 1.00 56.91  ? 86  ASP   B C   1 
ATOM   989  O O   . ASP   B 2 77  ? -24.364 -12.354 -14.036 1.00 52.69  ? 86  ASP   B O   1 
ATOM   990  C CB  . ASP   B 2 77  ? -26.570 -11.299 -12.377 1.00 64.75  ? 86  ASP   B CB  1 
ATOM   991  C CG  . ASP   B 2 77  ? -27.832 -11.390 -13.207 1.00 75.90  ? 86  ASP   B CG  1 
ATOM   992  O OD1 . ASP   B 2 77  ? -27.843 -10.785 -14.296 1.00 79.00  ? 86  ASP   B OD1 1 
ATOM   993  O OD2 . ASP   B 2 77  ? -28.797 -12.054 -12.755 1.00 83.22  ? 86  ASP   B OD2 1 
ATOM   994  N N   . ALA   B 2 78  ? -24.916 -10.741 -15.482 1.00 53.06  ? 87  ALA   B N   1 
ATOM   995  C CA  . ALA   B 2 78  ? -24.357 -11.445 -16.654 1.00 47.11  ? 87  ALA   B CA  1 
ATOM   996  C C   . ALA   B 2 78  ? -22.832 -11.541 -16.495 1.00 47.25  ? 87  ALA   B C   1 
ATOM   997  O O   . ALA   B 2 78  ? -22.215 -10.632 -15.858 1.00 45.21  ? 87  ALA   B O   1 
ATOM   998  C CB  . ALA   B 2 78  ? -24.775 -10.783 -17.946 1.00 46.11  ? 87  ALA   B CB  1 
ATOM   999  N N   . ALA   B 2 79  ? -22.242 -12.600 -17.063 1.00 42.13  ? 88  ALA   B N   1 
ATOM   1000 C CA  . ALA   B 2 79  ? -20.807 -12.950 -16.942 1.00 45.37  ? 88  ALA   B CA  1 
ATOM   1001 C C   . ALA   B 2 79  ? -20.197 -13.209 -18.323 1.00 41.11  ? 88  ALA   B C   1 
ATOM   1002 O O   . ALA   B 2 79  ? -20.879 -13.849 -19.140 1.00 37.51  ? 88  ALA   B O   1 
ATOM   1003 C CB  . ALA   B 2 79  ? -20.716 -14.183 -16.075 1.00 48.97  ? 88  ALA   B CB  1 
ATOM   1004 N N   . TRP   B 2 80  ? -18.964 -12.753 -18.583 1.00 42.69  ? 89  TRP   B N   1 
ATOM   1005 C CA  . TRP   B 2 80  ? -18.168 -13.212 -19.762 1.00 47.30  ? 89  TRP   B CA  1 
ATOM   1006 C C   . TRP   B 2 80  ? -18.089 -14.739 -19.751 1.00 52.26  ? 89  TRP   B C   1 
ATOM   1007 O O   . TRP   B 2 80  ? -17.850 -15.303 -18.653 1.00 47.07  ? 89  TRP   B O   1 
ATOM   1008 C CB  . TRP   B 2 80  ? -16.770 -12.598 -19.808 1.00 51.64  ? 89  TRP   B CB  1 
ATOM   1009 C CG  . TRP   B 2 80  ? -15.970 -13.016 -21.003 1.00 55.05  ? 89  TRP   B CG  1 
ATOM   1010 C CD1 . TRP   B 2 80  ? -16.413 -13.164 -22.285 1.00 55.26  ? 89  TRP   B CD1 1 
ATOM   1011 C CD2 . TRP   B 2 80  ? -14.562 -13.313 -21.031 1.00 58.65  ? 89  TRP   B CD2 1 
ATOM   1012 N NE1 . TRP   B 2 80  ? -15.385 -13.535 -23.106 1.00 58.24  ? 89  TRP   B NE1 1 
ATOM   1013 C CE2 . TRP   B 2 80  ? -14.235 -13.633 -22.372 1.00 55.18  ? 89  TRP   B CE2 1 
ATOM   1014 C CE3 . TRP   B 2 80  ? -13.559 -13.375 -20.057 1.00 53.42  ? 89  TRP   B CE3 1 
ATOM   1015 C CZ2 . TRP   B 2 80  ? -12.950 -14.004 -22.761 1.00 49.52  ? 89  TRP   B CZ2 1 
ATOM   1016 C CZ3 . TRP   B 2 80  ? -12.281 -13.720 -20.453 1.00 59.72  ? 89  TRP   B CZ3 1 
ATOM   1017 C CH2 . TRP   B 2 80  ? -11.985 -14.040 -21.785 1.00 51.02  ? 89  TRP   B CH2 1 
ATOM   1018 N N   . ASP   B 2 81  ? -18.321 -15.366 -20.915 1.00 55.04  ? 90  ASP   B N   1 
ATOM   1019 C CA  . ASP   B 2 81  ? -18.421 -16.844 -21.061 1.00 53.95  ? 90  ASP   B CA  1 
ATOM   1020 C C   . ASP   B 2 81  ? -17.007 -17.450 -21.119 1.00 53.19  ? 90  ASP   B C   1 
ATOM   1021 O O   . ASP   B 2 81  ? -16.904 -18.663 -20.912 1.00 63.42  ? 90  ASP   B O   1 
ATOM   1022 C CB  . ASP   B 2 81  ? -19.320 -17.242 -22.238 1.00 46.87  ? 90  ASP   B CB  1 
ATOM   1023 C CG  . ASP   B 2 81  ? -18.726 -17.028 -23.611 1.00 44.26  ? 90  ASP   B CG  1 
ATOM   1024 O OD1 . ASP   B 2 81  ? -17.674 -16.334 -23.725 1.00 55.63  ? 90  ASP   B OD1 1 
ATOM   1025 O OD2 . ASP   B 2 81  ? -19.340 -17.519 -24.577 1.00 55.62  ? 90  ASP   B OD2 1 
ATOM   1026 N N   . GLY   B 2 82  ? -15.971 -16.633 -21.339 1.00 52.69  ? 91  GLY   B N   1 
ATOM   1027 C CA  . GLY   B 2 82  ? -14.558 -17.055 -21.398 1.00 52.66  ? 91  GLY   B CA  1 
ATOM   1028 C C   . GLY   B 2 82  ? -14.075 -17.311 -22.823 1.00 56.05  ? 91  GLY   B C   1 
ATOM   1029 O O   . GLY   B 2 82  ? -12.873 -17.558 -22.974 1.00 51.31  ? 91  GLY   B O   1 
ATOM   1030 N N   . LEU   B 2 83  ? -14.966 -17.255 -23.829 1.00 55.79  ? 92  LEU   B N   1 
ATOM   1031 C CA  . LEU   B 2 83  ? -14.698 -17.655 -25.240 1.00 53.75  ? 92  LEU   B CA  1 
ATOM   1032 C C   . LEU   B 2 83  ? -15.056 -16.532 -26.223 1.00 59.40  ? 92  LEU   B C   1 
ATOM   1033 O O   . LEU   B 2 83  ? -14.200 -16.170 -27.064 1.00 52.03  ? 92  LEU   B O   1 
ATOM   1034 C CB  . LEU   B 2 83  ? -15.539 -18.891 -25.554 1.00 57.19  ? 92  LEU   B CB  1 
ATOM   1035 C CG  . LEU   B 2 83  ? -14.993 -20.212 -25.023 1.00 65.20  ? 92  LEU   B CG  1 
ATOM   1036 C CD1 . LEU   B 2 83  ? -15.971 -21.347 -25.295 1.00 65.44  ? 92  LEU   B CD1 1 
ATOM   1037 C CD2 . LEU   B 2 83  ? -13.626 -20.510 -25.622 1.00 58.95  ? 92  LEU   B CD2 1 
ATOM   1038 N N   . SER   B 2 84  ? -16.296 -16.034 -26.167 1.00 60.19  ? 93  SER   B N   1 
ATOM   1039 C CA  . SER   B 2 84  ? -16.888 -15.165 -27.221 1.00 52.43  ? 93  SER   B CA  1 
ATOM   1040 C C   . SER   B 2 84  ? -16.288 -13.754 -27.147 1.00 50.34  ? 93  SER   B C   1 
ATOM   1041 O O   . SER   B 2 84  ? -15.762 -13.379 -26.080 1.00 53.03  ? 93  SER   B O   1 
ATOM   1042 C CB  . SER   B 2 84  ? -18.369 -15.166 -27.101 1.00 52.08  ? 93  SER   B CB  1 
ATOM   1043 O OG  . SER   B 2 84  ? -18.796 -16.242 -26.268 1.00 50.70  ? 93  SER   B OG  1 
ATOM   1044 N N   . GLU   B 2 85  ? -16.301 -13.007 -28.252 1.00 52.89  ? 94  GLU   B N   1 
ATOM   1045 C CA  . GLU   B 2 85  ? -15.921 -11.570 -28.241 1.00 58.93  ? 94  GLU   B CA  1 
ATOM   1046 C C   . GLU   B 2 85  ? -17.029 -10.785 -27.513 1.00 48.15  ? 94  GLU   B C   1 
ATOM   1047 O O   . GLU   B 2 85  ? -18.132 -11.305 -27.266 1.00 33.55  ? 94  GLU   B O   1 
ATOM   1048 C CB  . GLU   B 2 85  ? -15.660 -11.026 -29.652 1.00 73.39  ? 94  GLU   B CB  1 
ATOM   1049 C CG  . GLU   B 2 85  ? -14.290 -11.398 -30.227 1.00 83.82  ? 94  GLU   B CG  1 
ATOM   1050 C CD  . GLU   B 2 85  ? -14.054 -11.091 -31.708 1.00 91.25  ? 94  GLU   B CD  1 
ATOM   1051 O OE1 . GLU   B 2 85  ? -15.046 -10.869 -32.425 1.00 81.92  ? 94  GLU   B OE1 1 
ATOM   1052 O OE2 . GLU   B 2 85  ? -12.872 -11.071 -32.153 1.00 88.77  ? 94  GLU   B OE2 1 
ATOM   1053 N N   . VAL   B 2 86  ? -16.718 -9.557  -27.162 1.00 40.71  ? 95  VAL   B N   1 
ATOM   1054 C CA  . VAL   B 2 86  ? -17.633 -8.668  -26.399 1.00 43.13  ? 95  VAL   B CA  1 
ATOM   1055 C C   . VAL   B 2 86  ? -17.585 -7.302  -27.065 1.00 39.60  ? 95  VAL   B C   1 
ATOM   1056 O O   . VAL   B 2 86  ? -16.617 -7.061  -27.846 1.00 42.70  ? 95  VAL   B O   1 
ATOM   1057 C CB  . VAL   B 2 86  ? -17.182 -8.562  -24.924 1.00 34.36  ? 95  VAL   B CB  1 
ATOM   1058 C CG1 . VAL   B 2 86  ? -17.028 -9.920  -24.308 1.00 35.52  ? 95  VAL   B CG1 1 
ATOM   1059 C CG2 . VAL   B 2 86  ? -15.897 -7.767  -24.798 1.00 35.10  ? 95  VAL   B CG2 1 
ATOM   1060 N N   . GLN   B 2 87  ? -18.516 -6.421  -26.694 1.00 42.89  ? 96  GLN   B N   1 
ATOM   1061 C CA  . GLN   B 2 87  ? -18.471 -5.003  -27.129 1.00 43.26  ? 96  GLN   B CA  1 
ATOM   1062 C C   . GLN   B 2 87  ? -18.317 -4.105  -25.905 1.00 37.79  ? 96  GLN   B C   1 
ATOM   1063 O O   . GLN   B 2 87  ? -19.154 -4.182  -24.997 1.00 43.63  ? 96  GLN   B O   1 
ATOM   1064 C CB  . GLN   B 2 87  ? -19.688 -4.695  -28.007 1.00 44.81  ? 96  GLN   B CB  1 
ATOM   1065 C CG  . GLN   B 2 87  ? -19.561 -5.362  -29.378 1.00 53.57  ? 96  GLN   B CG  1 
ATOM   1066 C CD  . GLN   B 2 87  ? -20.630 -5.014  -30.393 1.00 54.47  ? 96  GLN   B CD  1 
ATOM   1067 O OE1 . GLN   B 2 87  ? -21.216 -3.934  -30.374 1.00 48.03  ? 96  GLN   B OE1 1 
ATOM   1068 N NE2 . GLN   B 2 87  ? -20.882 -5.934  -31.312 1.00 53.55  ? 96  GLN   B NE2 1 
ATOM   1069 N N   . LEU   B 2 88  ? -17.251 -3.316  -25.885 1.00 33.90  ? 97  LEU   B N   1 
ATOM   1070 C CA  . LEU   B 2 88  ? -17.201 -2.097  -25.061 1.00 38.01  ? 97  LEU   B CA  1 
ATOM   1071 C C   . LEU   B 2 88  ? -18.091 -1.031  -25.708 1.00 41.90  ? 97  LEU   B C   1 
ATOM   1072 O O   . LEU   B 2 88  ? -17.693 -0.524  -26.778 1.00 41.39  ? 97  LEU   B O   1 
ATOM   1073 C CB  . LEU   B 2 88  ? -15.766 -1.566  -24.958 1.00 40.25  ? 97  LEU   B CB  1 
ATOM   1074 C CG  . LEU   B 2 88  ? -15.660 -0.235  -24.224 1.00 39.65  ? 97  LEU   B CG  1 
ATOM   1075 C CD1 . LEU   B 2 88  ? -16.020 -0.415  -22.765 1.00 46.83  ? 97  LEU   B CD1 1 
ATOM   1076 C CD2 . LEU   B 2 88  ? -14.274 0.363   -24.336 1.00 40.59  ? 97  LEU   B CD2 1 
ATOM   1077 N N   . LEU   B 2 89  ? -19.193 -0.656  -25.052 1.00 37.83  ? 98  LEU   B N   1 
ATOM   1078 C CA  . LEU   B 2 89  ? -20.019 0.526   -25.414 1.00 35.15  ? 98  LEU   B CA  1 
ATOM   1079 C C   . LEU   B 2 89  ? -19.374 1.728   -24.760 1.00 39.01  ? 98  LEU   B C   1 
ATOM   1080 O O   . LEU   B 2 89  ? -19.863 2.187   -23.679 1.00 41.68  ? 98  LEU   B O   1 
ATOM   1081 C CB  . LEU   B 2 89  ? -21.454 0.246   -24.976 1.00 38.77  ? 98  LEU   B CB  1 
ATOM   1082 C CG  . LEU   B 2 89  ? -22.523 1.342   -25.156 1.00 39.64  ? 98  LEU   B CG  1 
ATOM   1083 C CD1 . LEU   B 2 89  ? -22.219 2.308   -26.271 1.00 45.36  ? 98  LEU   B CD1 1 
ATOM   1084 C CD2 . LEU   B 2 89  ? -23.884 0.706   -25.375 1.00 38.15  ? 98  LEU   B CD2 1 
ATOM   1085 N N   . ALA   B 2 90  ? -18.251 2.165   -25.349 1.00 38.58  ? 99  ALA   B N   1 
ATOM   1086 C CA  . ALA   B 2 90  ? -17.510 3.355   -24.890 1.00 40.85  ? 99  ALA   B CA  1 
ATOM   1087 C C   . ALA   B 2 90  ? -18.400 4.590   -25.024 1.00 47.10  ? 99  ALA   B C   1 
ATOM   1088 O O   . ALA   B 2 90  ? -19.075 4.726   -26.070 1.00 49.70  ? 99  ALA   B O   1 
ATOM   1089 C CB  . ALA   B 2 90  ? -16.250 3.573   -25.671 1.00 41.38  ? 99  ALA   B CB  1 
ATOM   1090 N N   . VAL   B 2 91  ? -18.330 5.475   -24.025 1.00 45.46  ? 100 VAL   B N   1 
ATOM   1091 C CA  . VAL   B 2 91  ? -18.945 6.825   -24.041 1.00 40.63  ? 100 VAL   B CA  1 
ATOM   1092 C C   . VAL   B 2 91  ? -17.879 7.828   -23.636 1.00 40.03  ? 100 VAL   B C   1 
ATOM   1093 O O   . VAL   B 2 91  ? -17.862 8.319   -22.524 1.00 40.90  ? 100 VAL   B O   1 
ATOM   1094 C CB  . VAL   B 2 91  ? -20.198 6.870   -23.154 1.00 44.68  ? 100 VAL   B CB  1 
ATOM   1095 C CG1 . VAL   B 2 91  ? -20.850 8.248   -23.136 1.00 51.88  ? 100 VAL   B CG1 1 
ATOM   1096 C CG2 . VAL   B 2 91  ? -21.199 5.807   -23.590 1.00 39.59  ? 100 VAL   B CG2 1 
ATOM   1097 N N   . PRO   B 2 92  ? -17.002 8.246   -24.566 1.00 44.74  ? 101 PRO   B N   1 
ATOM   1098 C CA  . PRO   B 2 92  ? -15.924 9.167   -24.220 1.00 43.04  ? 101 PRO   B CA  1 
ATOM   1099 C C   . PRO   B 2 92  ? -16.410 10.598  -24.013 1.00 44.45  ? 101 PRO   B C   1 
ATOM   1100 O O   . PRO   B 2 92  ? -17.472 10.980  -24.503 1.00 48.65  ? 101 PRO   B O   1 
ATOM   1101 C CB  . PRO   B 2 92  ? -14.985 9.084   -25.440 1.00 45.43  ? 101 PRO   B CB  1 
ATOM   1102 C CG  . PRO   B 2 92  ? -15.524 7.952   -26.299 1.00 45.46  ? 101 PRO   B CG  1 
ATOM   1103 C CD  . PRO   B 2 92  ? -17.003 7.878   -25.992 1.00 48.09  ? 101 PRO   B CD  1 
ATOM   1104 N N   . PRO   B 2 93  ? -15.629 11.443  -23.309 1.00 43.71  ? 102 PRO   B N   1 
ATOM   1105 C CA  . PRO   B 2 93  ? -15.978 12.849  -23.132 1.00 47.76  ? 102 PRO   B CA  1 
ATOM   1106 C C   . PRO   B 2 93  ? -16.131 13.617  -24.460 1.00 51.74  ? 102 PRO   B C   1 
ATOM   1107 O O   . PRO   B 2 93  ? -15.255 13.544  -25.300 1.00 55.17  ? 102 PRO   B O   1 
ATOM   1108 C CB  . PRO   B 2 93  ? -14.824 13.383  -22.256 1.00 44.36  ? 102 PRO   B CB  1 
ATOM   1109 C CG  . PRO   B 2 93  ? -14.313 12.171  -21.525 1.00 46.00  ? 102 PRO   B CG  1 
ATOM   1110 C CD  . PRO   B 2 93  ? -14.427 11.065  -22.550 1.00 47.40  ? 102 PRO   B CD  1 
ATOM   1111 N N   . GLY   B 2 94  ? -17.258 14.326  -24.606 1.00 51.96  ? 103 GLY   B N   1 
ATOM   1112 C CA  . GLY   B 2 94  ? -17.602 15.172  -25.765 1.00 55.08  ? 103 GLY   B CA  1 
ATOM   1113 C C   . GLY   B 2 94  ? -17.921 14.383  -27.029 1.00 48.11  ? 103 GLY   B C   1 
ATOM   1114 O O   . GLY   B 2 94  ? -18.080 14.994  -28.076 1.00 52.48  ? 103 GLY   B O   1 
ATOM   1115 N N   . GLU   B 2 95  ? -18.049 13.068  -26.953 1.00 47.43  ? 104 GLU   B N   1 
ATOM   1116 C CA  . GLU   B 2 95  ? -18.098 12.209  -28.156 1.00 46.63  ? 104 GLU   B CA  1 
ATOM   1117 C C   . GLU   B 2 95  ? -19.281 11.263  -28.008 1.00 47.35  ? 104 GLU   B C   1 
ATOM   1118 O O   . GLU   B 2 95  ? -19.596 10.849  -26.867 1.00 50.76  ? 104 GLU   B O   1 
ATOM   1119 C CB  . GLU   B 2 95  ? -16.761 11.480  -28.321 1.00 48.92  ? 104 GLU   B CB  1 
ATOM   1120 C CG  . GLU   B 2 95  ? -15.587 12.431  -28.550 1.00 58.46  ? 104 GLU   B CG  1 
ATOM   1121 C CD  . GLU   B 2 95  ? -14.233 11.755  -28.735 1.00 68.75  ? 104 GLU   B CD  1 
ATOM   1122 O OE1 . GLU   B 2 95  ? -14.215 10.510  -28.810 1.00 76.69  ? 104 GLU   B OE1 1 
ATOM   1123 O OE2 . GLU   B 2 95  ? -13.192 12.469  -28.799 1.00 68.02  ? 104 GLU   B OE2 1 
ATOM   1124 N N   . ARG   B 2 96  ? -19.932 10.946  -29.114 1.00 46.82  ? 105 ARG   B N   1 
ATOM   1125 C CA  . ARG   B 2 96  ? -21.142 10.098  -29.104 1.00 49.51  ? 105 ARG   B CA  1 
ATOM   1126 C C   . ARG   B 2 96  ? -20.730 8.701   -28.650 1.00 53.17  ? 105 ARG   B C   1 
ATOM   1127 O O   . ARG   B 2 96  ? -19.530 8.348   -28.795 1.00 51.41  ? 105 ARG   B O   1 
ATOM   1128 C CB  . ARG   B 2 96  ? -21.780 10.126  -30.497 1.00 57.78  ? 105 ARG   B CB  1 
ATOM   1129 C CG  . ARG   B 2 96  ? -23.073 9.337   -30.625 1.00 64.16  ? 105 ARG   B CG  1 
ATOM   1130 C CD  . ARG   B 2 96  ? -23.900 9.679   -31.862 1.00 73.60  ? 105 ARG   B CD  1 
ATOM   1131 N NE  . ARG   B 2 96  ? -23.193 9.599   -33.139 1.00 70.91  ? 105 ARG   B NE  1 
ATOM   1132 C CZ  . ARG   B 2 96  ? -22.587 10.612  -33.755 1.00 78.46  ? 105 ARG   B CZ  1 
ATOM   1133 N NH1 . ARG   B 2 96  ? -22.587 11.826  -33.232 1.00 80.11  ? 105 ARG   B NH1 1 
ATOM   1134 N NH2 . ARG   B 2 96  ? -21.980 10.410  -34.913 1.00 82.91  ? 105 ARG   B NH2 1 
ATOM   1135 N N   . ALA   B 2 97  ? -21.698 7.954   -28.120 1.00 52.92  ? 106 ALA   B N   1 
ATOM   1136 C CA  . ALA   B 2 97  ? -21.590 6.528   -27.748 1.00 52.63  ? 106 ALA   B CA  1 
ATOM   1137 C C   . ALA   B 2 97  ? -21.087 5.727   -28.958 1.00 53.51  ? 106 ALA   B C   1 
ATOM   1138 O O   . ALA   B 2 97  ? -21.605 5.953   -30.048 1.00 58.86  ? 106 ALA   B O   1 
ATOM   1139 C CB  . ALA   B 2 97  ? -22.943 6.060   -27.283 1.00 52.89  ? 106 ALA   B CB  1 
ATOM   1140 N N   . LYS   B 2 98  ? -20.119 4.830   -28.765 1.00 58.31  ? 107 LYS   B N   1 
ATOM   1141 C CA  . LYS   B 2 98  ? -19.489 4.002   -29.836 1.00 63.00  ? 107 LYS   B CA  1 
ATOM   1142 C C   . LYS   B 2 98  ? -19.166 2.586   -29.325 1.00 56.15  ? 107 LYS   B C   1 
ATOM   1143 O O   . LYS   B 2 98  ? -18.305 2.500   -28.440 1.00 56.20  ? 107 LYS   B O   1 
ATOM   1144 C CB  . LYS   B 2 98  ? -18.188 4.669   -30.292 1.00 72.46  ? 107 LYS   B CB  1 
ATOM   1145 C CG  . LYS   B 2 98  ? -17.390 3.880   -31.327 1.00 86.58  ? 107 LYS   B CG  1 
ATOM   1146 C CD  . LYS   B 2 98  ? -16.150 4.590   -31.849 1.00 91.28  ? 107 LYS   B CD  1 
ATOM   1147 C CE  . LYS   B 2 98  ? -15.241 5.070   -30.736 1.00 93.20  ? 107 LYS   B CE  1 
ATOM   1148 N NZ  . LYS   B 2 98  ? -13.840 5.188   -31.198 1.00 97.42  ? 107 LYS   B NZ  1 
ATOM   1149 N N   . ASN   B 2 99  ? -19.829 1.545   -29.859 1.00 44.48  ? 108 ASN   B N   1 
ATOM   1150 C CA  . ASN   B 2 99  ? -19.482 0.109   -29.668 1.00 51.69  ? 108 ASN   B CA  1 
ATOM   1151 C C   . ASN   B 2 99  ? -18.112 -0.188  -30.285 1.00 56.84  ? 108 ASN   B C   1 
ATOM   1152 O O   . ASN   B 2 99  ? -17.857 0.266   -31.405 1.00 64.04  ? 108 ASN   B O   1 
ATOM   1153 C CB  . ASN   B 2 99  ? -20.488 -0.884  -30.263 1.00 44.71  ? 108 ASN   B CB  1 
ATOM   1154 C CG  . ASN   B 2 99  ? -21.891 -0.701  -29.725 1.00 49.62  ? 108 ASN   B CG  1 
ATOM   1155 O OD1 . ASN   B 2 99  ? -22.493 0.347   -29.941 1.00 55.97  ? 108 ASN   B OD1 1 
ATOM   1156 N ND2 . ASN   B 2 99  ? -22.453 -1.704  -29.066 1.00 45.33  ? 108 ASN   B ND2 1 
ATOM   1157 N N   . ILE   B 2 100 ? -17.264 -0.915  -29.554 1.00 55.04  ? 109 ILE   B N   1 
ATOM   1158 C CA  . ILE   B 2 100 ? -15.917 -1.372  -29.994 1.00 52.93  ? 109 ILE   B CA  1 
ATOM   1159 C C   . ILE   B 2 100 ? -15.800 -2.842  -29.614 1.00 51.06  ? 109 ILE   B C   1 
ATOM   1160 O O   . ILE   B 2 100 ? -15.710 -3.118  -28.419 1.00 53.25  ? 109 ILE   B O   1 
ATOM   1161 C CB  . ILE   B 2 100 ? -14.801 -0.555  -29.344 1.00 53.40  ? 109 ILE   B CB  1 
ATOM   1162 C CG1 . ILE   B 2 100 ? -15.033 0.945   -29.470 1.00 54.38  ? 109 ILE   B CG1 1 
ATOM   1163 C CG2 . ILE   B 2 100 ? -13.464 -0.975  -29.920 1.00 56.15  ? 109 ILE   B CG2 1 
ATOM   1164 C CD1 . ILE   B 2 100 ? -14.638 1.502   -30.807 1.00 61.32  ? 109 ILE   B CD1 1 
ATOM   1165 N N   . GLN   B 2 101 ? -15.872 -3.728  -30.600 1.00 47.15  ? 110 GLN   B N   1 
ATOM   1166 C CA  . GLN   B 2 101 ? -15.910 -5.197  -30.428 1.00 47.97  ? 110 GLN   B CA  1 
ATOM   1167 C C   . GLN   B 2 101 ? -14.481 -5.696  -30.202 1.00 53.48  ? 110 GLN   B C   1 
ATOM   1168 O O   . GLN   B 2 101 ? -13.553 -5.131  -30.818 1.00 51.24  ? 110 GLN   B O   1 
ATOM   1169 C CB  . GLN   B 2 101 ? -16.524 -5.861  -31.649 1.00 51.40  ? 110 GLN   B CB  1 
ATOM   1170 C CG  . GLN   B 2 101 ? -16.372 -7.363  -31.650 1.00 49.81  ? 110 GLN   B CG  1 
ATOM   1171 C CD  . GLN   B 2 101 ? -17.541 -8.038  -32.309 1.00 49.66  ? 110 GLN   B CD  1 
ATOM   1172 O OE1 . GLN   B 2 101 ? -18.645 -7.514  -32.360 1.00 54.83  ? 110 GLN   B OE1 1 
ATOM   1173 N NE2 . GLN   B 2 101 ? -17.315 -9.233  -32.804 1.00 52.59  ? 110 GLN   B NE2 1 
ATOM   1174 N N   . THR   B 2 102 ? -14.308 -6.649  -29.273 1.00 55.40  ? 111 THR   B N   1 
ATOM   1175 C CA  . THR   B 2 102 ? -12.976 -7.150  -28.856 1.00 46.87  ? 111 THR   B CA  1 
ATOM   1176 C C   . THR   B 2 102 ? -13.133 -8.513  -28.203 1.00 49.53  ? 111 THR   B C   1 
ATOM   1177 O O   . THR   B 2 102 ? -14.262 -8.841  -27.784 1.00 56.06  ? 111 THR   B O   1 
ATOM   1178 C CB  . THR   B 2 102 ? -12.236 -6.128  -27.989 1.00 50.63  ? 111 THR   B CB  1 
ATOM   1179 O OG1 . THR   B 2 102 ? -10.863 -6.511  -28.022 1.00 47.23  ? 111 THR   B OG1 1 
ATOM   1180 C CG2 . THR   B 2 102 ? -12.742 -6.051  -26.562 1.00 56.72  ? 111 THR   B CG2 1 
ATOM   1181 N N   . LEU   B 2 103 ? -12.063 -9.312  -28.240 1.00 44.22  ? 112 LEU   B N   1 
ATOM   1182 C CA  . LEU   B 2 103 ? -11.958 -10.577 -27.466 1.00 47.44  ? 112 LEU   B CA  1 
ATOM   1183 C C   . LEU   B 2 103 ? -11.170 -10.249 -26.206 1.00 47.50  ? 112 LEU   B C   1 
ATOM   1184 O O   . LEU   B 2 103 ? -10.043 -9.749  -26.264 1.00 50.44  ? 112 LEU   B O   1 
ATOM   1185 C CB  . LEU   B 2 103 ? -11.259 -11.701 -28.233 1.00 48.72  ? 112 LEU   B CB  1 
ATOM   1186 C CG  . LEU   B 2 103 ? -11.090 -12.981 -27.420 1.00 49.04  ? 112 LEU   B CG  1 
ATOM   1187 C CD1 . LEU   B 2 103 ? -12.355 -13.815 -27.502 1.00 48.28  ? 112 LEU   B CD1 1 
ATOM   1188 C CD2 . LEU   B 2 103 ? -9.867  -13.778 -27.862 1.00 51.38  ? 112 LEU   B CD2 1 
ATOM   1189 N N   . PRO   B 2 104 ? -11.753 -10.475 -25.016 1.00 44.26  ? 113 PRO   B N   1 
ATOM   1190 C CA  . PRO   B 2 104 ? -11.060 -10.090 -23.797 1.00 46.96  ? 113 PRO   B CA  1 
ATOM   1191 C C   . PRO   B 2 104 ? -9.826  -10.985 -23.582 1.00 51.72  ? 113 PRO   B C   1 
ATOM   1192 O O   . PRO   B 2 104 ? -9.831  -12.170 -23.974 1.00 51.32  ? 113 PRO   B O   1 
ATOM   1193 C CB  . PRO   B 2 104 ? -12.106 -10.271 -22.698 1.00 47.59  ? 113 PRO   B CB  1 
ATOM   1194 C CG  . PRO   B 2 104 ? -13.427 -10.453 -23.432 1.00 48.22  ? 113 PRO   B CG  1 
ATOM   1195 C CD  . PRO   B 2 104 ? -13.086 -11.045 -24.784 1.00 47.38  ? 113 PRO   B CD  1 
ATOM   1196 N N   . GLY   B 2 105 ? -8.781  -10.370 -23.029 1.00 48.42  ? 114 GLY   B N   1 
ATOM   1197 C CA  . GLY   B 2 105 ? -7.712  -11.055 -22.286 1.00 52.92  ? 114 GLY   B CA  1 
ATOM   1198 C C   . GLY   B 2 105 ? -8.176  -11.459 -20.893 1.00 49.22  ? 114 GLY   B C   1 
ATOM   1199 O O   . GLY   B 2 105 ? -9.380  -11.751 -20.709 1.00 49.47  ? 114 GLY   B O   1 
ATOM   1200 N N   . ILE   B 2 106 ? -7.231  -11.505 -19.955 1.00 51.53  ? 115 ILE   B N   1 
ATOM   1201 C CA  . ILE   B 2 106 ? -7.298  -12.270 -18.671 1.00 51.08  ? 115 ILE   B CA  1 
ATOM   1202 C C   . ILE   B 2 106 ? -6.446  -11.551 -17.618 1.00 44.10  ? 115 ILE   B C   1 
ATOM   1203 O O   . ILE   B 2 106 ? -5.281  -11.276 -17.879 1.00 46.69  ? 115 ILE   B O   1 
ATOM   1204 C CB  . ILE   B 2 106 ? -6.772  -13.693 -18.902 1.00 53.52  ? 115 ILE   B CB  1 
ATOM   1205 C CG1 . ILE   B 2 106 ? -7.698  -14.507 -19.802 1.00 58.03  ? 115 ILE   B CG1 1 
ATOM   1206 C CG2 . ILE   B 2 106 ? -6.513  -14.396 -17.590 1.00 63.31  ? 115 ILE   B CG2 1 
ATOM   1207 C CD1 . ILE   B 2 106 ? -8.882  -15.077 -19.108 1.00 59.93  ? 115 ILE   B CD1 1 
ATOM   1208 N N   . PHE   B 2 107 ? -7.029  -11.194 -16.490 1.00 46.19  ? 116 PHE   B N   1 
ATOM   1209 C CA  . PHE   B 2 107 ? -6.276  -10.844 -15.266 1.00 46.98  ? 116 PHE   B CA  1 
ATOM   1210 C C   . PHE   B 2 107 ? -6.202  -12.116 -14.435 1.00 49.65  ? 116 PHE   B C   1 
ATOM   1211 O O   . PHE   B 2 107 ? -7.289  -12.567 -14.021 1.00 48.91  ? 116 PHE   B O   1 
ATOM   1212 C CB  . PHE   B 2 107 ? -6.969  -9.716  -14.506 1.00 46.89  ? 116 PHE   B CB  1 
ATOM   1213 C CG  . PHE   B 2 107 ? -6.697  -8.335  -15.032 1.00 46.62  ? 116 PHE   B CG  1 
ATOM   1214 C CD1 . PHE   B 2 107 ? -5.973  -8.141  -16.196 1.00 46.34  ? 116 PHE   B CD1 1 
ATOM   1215 C CD2 . PHE   B 2 107 ? -7.206  -7.229  -14.369 1.00 47.10  ? 116 PHE   B CD2 1 
ATOM   1216 C CE1 . PHE   B 2 107 ? -5.754  -6.863  -16.679 1.00 48.81  ? 116 PHE   B CE1 1 
ATOM   1217 C CE2 . PHE   B 2 107 ? -6.982  -5.951  -14.851 1.00 47.86  ? 116 PHE   B CE2 1 
ATOM   1218 C CZ  . PHE   B 2 107 ? -6.252  -5.770  -16.004 1.00 50.57  ? 116 PHE   B CZ  1 
ATOM   1219 N N   . LYS   B 2 108 ? -5.000  -12.687 -14.287 1.00 51.78  ? 117 LYS   B N   1 
ATOM   1220 C CA  . LYS   B 2 108 ? -4.706  -13.831 -13.373 1.00 56.69  ? 117 LYS   B CA  1 
ATOM   1221 C C   . LYS   B 2 108 ? -4.322  -13.292 -11.983 1.00 46.53  ? 117 LYS   B C   1 
ATOM   1222 O O   . LYS   B 2 108 ? -3.326  -12.559 -11.879 1.00 43.09  ? 117 LYS   B O   1 
ATOM   1223 C CB  . LYS   B 2 108 ? -3.593  -14.725 -13.940 1.00 65.71  ? 117 LYS   B CB  1 
ATOM   1224 C CG  . LYS   B 2 108 ? -3.901  -15.407 -15.268 1.00 74.51  ? 117 LYS   B CG  1 
ATOM   1225 C CD  . LYS   B 2 108 ? -2.852  -16.411 -15.742 1.00 78.09  ? 117 LYS   B CD  1 
ATOM   1226 C CE  . LYS   B 2 108 ? -3.420  -17.447 -16.701 1.00 93.12  ? 117 LYS   B CE  1 
ATOM   1227 N NZ  . LYS   B 2 108 ? -2.593  -17.642 -17.924 1.00 92.68  ? 117 LYS   B NZ  1 
ATOM   1228 N N   . THR   B 2 109 ? -5.117  -13.624 -10.963 1.00 50.83  ? 118 THR   B N   1 
ATOM   1229 C CA  . THR   B 2 109 ? -4.930  -13.227 -9.542  1.00 49.51  ? 118 THR   B CA  1 
ATOM   1230 C C   . THR   B 2 109 ? -4.999  -14.471 -8.648  1.00 53.70  ? 118 THR   B C   1 
ATOM   1231 O O   . THR   B 2 109 ? -5.677  -15.449 -9.029  1.00 47.20  ? 118 THR   B O   1 
ATOM   1232 C CB  . THR   B 2 109 ? -6.021  -12.249 -9.071  1.00 50.85  ? 118 THR   B CB  1 
ATOM   1233 O OG1 . THR   B 2 109 ? -7.220  -12.974 -8.757  1.00 44.47  ? 118 THR   B OG1 1 
ATOM   1234 C CG2 . THR   B 2 109 ? -6.309  -11.168 -10.088 1.00 51.53  ? 118 THR   B CG2 1 
ATOM   1235 N N   . LYS   B 2 110 ? -4.421  -14.374 -7.449  1.00 58.51  ? 119 LYS   B N   1 
ATOM   1236 C CA  . LYS   B 2 110 ? -4.446  -15.422 -6.395  1.00 58.66  ? 119 LYS   B CA  1 
ATOM   1237 C C   . LYS   B 2 110 ? -5.892  -15.849 -6.083  1.00 64.09  ? 119 LYS   B C   1 
ATOM   1238 O O   . LYS   B 2 110 ? -6.057  -17.011 -5.673  1.00 75.84  ? 119 LYS   B O   1 
ATOM   1239 C CB  . LYS   B 2 110 ? -3.706  -14.927 -5.142  1.00 65.89  ? 119 LYS   B CB  1 
ATOM   1240 C CG  . LYS   B 2 110 ? -4.318  -13.727 -4.433  1.00 71.10  ? 119 LYS   B CG  1 
ATOM   1241 C CD  . LYS   B 2 110 ? -3.475  -13.186 -3.290  1.00 76.71  ? 119 LYS   B CD  1 
ATOM   1242 C CE  . LYS   B 2 110 ? -3.988  -13.574 -1.916  1.00 83.40  ? 119 LYS   B CE  1 
ATOM   1243 N NZ  . LYS   B 2 110 ? -5.267  -12.900 -1.584  1.00 81.07  ? 119 LYS   B NZ  1 
ATOM   1244 N N   . ASP   B 2 111 ? -6.901  -14.985 -6.256  1.00 58.41  ? 120 ASP   B N   1 
ATOM   1245 C CA  . ASP   B 2 111 ? -8.308  -15.307 -5.890  1.00 58.62  ? 120 ASP   B CA  1 
ATOM   1246 C C   . ASP   B 2 111 ? -9.103  -15.784 -7.104  1.00 60.29  ? 120 ASP   B C   1 
ATOM   1247 O O   . ASP   B 2 111 ? -10.267 -16.210 -6.907  1.00 61.26  ? 120 ASP   B O   1 
ATOM   1248 C CB  . ASP   B 2 111 ? -8.997  -14.114 -5.233  1.00 65.63  ? 120 ASP   B CB  1 
ATOM   1249 C CG  . ASP   B 2 111 ? -8.453  -13.835 -3.847  1.00 67.43  ? 120 ASP   B CG  1 
ATOM   1250 O OD1 . ASP   B 2 111 ? -8.051  -14.804 -3.186  1.00 67.61  ? 120 ASP   B OD1 1 
ATOM   1251 O OD2 . ASP   B 2 111 ? -8.419  -12.655 -3.451  1.00 76.93  ? 120 ASP   B OD2 1 
ATOM   1252 N N   . GLY   B 2 112 ? -8.503  -15.739 -8.297  1.00 58.58  ? 121 GLY   B N   1 
ATOM   1253 C CA  . GLY   B 2 112 ? -9.122  -16.245 -9.534  1.00 57.01  ? 121 GLY   B CA  1 
ATOM   1254 C C   . GLY   B 2 112 ? -8.747  -15.432 -10.761 1.00 57.02  ? 121 GLY   B C   1 
ATOM   1255 O O   . GLY   B 2 112 ? -7.852  -14.551 -10.675 1.00 51.35  ? 121 GLY   B O   1 
ATOM   1256 N N   . ASP   B 2 113 ? -9.389  -15.760 -11.882 1.00 60.54  ? 122 ASP   B N   1 
ATOM   1257 C CA  . ASP   B 2 113 ? -9.139  -15.173 -13.228 1.00 63.29  ? 122 ASP   B CA  1 
ATOM   1258 C C   . ASP   B 2 113 ? -10.304 -14.242 -13.569 1.00 58.78  ? 122 ASP   B C   1 
ATOM   1259 O O   . ASP   B 2 113 ? -11.454 -14.585 -13.204 1.00 49.04  ? 122 ASP   B O   1 
ATOM   1260 C CB  . ASP   B 2 113 ? -8.989  -16.265 -14.293 1.00 65.89  ? 122 ASP   B CB  1 
ATOM   1261 C CG  . ASP   B 2 113 ? -7.608  -16.889 -14.394 1.00 70.11  ? 122 ASP   B CG  1 
ATOM   1262 O OD1 . ASP   B 2 113 ? -6.649  -16.313 -13.831 1.00 74.46  ? 122 ASP   B OD1 1 
ATOM   1263 O OD2 . ASP   B 2 113 ? -7.496  -17.935 -15.073 1.00 82.28  ? 122 ASP   B OD2 1 
ATOM   1264 N N   . ILE   B 2 114 ? -10.008 -13.102 -14.198 1.00 48.34  ? 123 ILE   B N   1 
ATOM   1265 C CA  . ILE   B 2 114 ? -11.021 -12.070 -14.567 1.00 52.65  ? 123 ILE   B CA  1 
ATOM   1266 C C   . ILE   B 2 114 ? -10.802 -11.713 -16.040 1.00 48.53  ? 123 ILE   B C   1 
ATOM   1267 O O   . ILE   B 2 114 ? -9.632  -11.613 -16.436 1.00 39.00  ? 123 ILE   B O   1 
ATOM   1268 C CB  . ILE   B 2 114 ? -10.908 -10.811 -13.673 1.00 52.86  ? 123 ILE   B CB  1 
ATOM   1269 C CG1 . ILE   B 2 114 ? -10.697 -11.137 -12.194 1.00 62.40  ? 123 ILE   B CG1 1 
ATOM   1270 C CG2 . ILE   B 2 114 ? -12.099 -9.887  -13.853 1.00 52.28  ? 123 ILE   B CG2 1 
ATOM   1271 C CD1 . ILE   B 2 114 ? -10.008 -10.026 -11.419 1.00 66.50  ? 123 ILE   B CD1 1 
ATOM   1272 N N   . GLY   B 2 115 ? -11.887 -11.469 -16.785 1.00 47.52  ? 124 GLY   B N   1 
ATOM   1273 C CA  . GLY   B 2 115 ? -11.838 -10.837 -18.116 1.00 43.54  ? 124 GLY   B CA  1 
ATOM   1274 C C   . GLY   B 2 115 ? -11.088 -9.529  -18.039 1.00 44.77  ? 124 GLY   B C   1 
ATOM   1275 O O   . GLY   B 2 115 ? -11.094 -8.844  -16.982 1.00 39.51  ? 124 GLY   B O   1 
ATOM   1276 N N   . ALA   B 2 116 ? -10.365 -9.218  -19.084 1.00 42.08  ? 125 ALA   B N   1 
ATOM   1277 C CA  . ALA   B 2 116 ? -9.782  -7.884  -19.261 1.00 44.37  ? 125 ALA   B CA  1 
ATOM   1278 C C   . ALA   B 2 116 ? -9.969  -7.500  -20.731 1.00 46.23  ? 125 ALA   B C   1 
ATOM   1279 O O   . ALA   B 2 116 ? -9.951  -8.382  -21.607 1.00 52.42  ? 125 ALA   B O   1 
ATOM   1280 C CB  . ALA   B 2 116 ? -8.346  -7.876  -18.825 1.00 45.07  ? 125 ALA   B CB  1 
ATOM   1281 N N   A VAL   B 2 117 ? -10.192 -6.209  -20.991 0.25 45.45  ? 126 VAL   B N   1 
ATOM   1282 N N   B VAL   B 2 117 ? -10.125 -6.196  -20.965 0.25 45.24  ? 126 VAL   B N   1 
ATOM   1283 N N   C VAL   B 2 117 ? -10.192 -6.209  -20.991 0.25 45.45  ? 126 VAL   B N   1 
ATOM   1284 N N   D VAL   B 2 117 ? -10.125 -6.196  -20.965 0.25 45.24  ? 126 VAL   B N   1 
ATOM   1285 C CA  A VAL   B 2 117 ? -10.294 -5.637  -22.366 0.25 46.37  ? 126 VAL   B CA  1 
ATOM   1286 C CA  B VAL   B 2 117 ? -10.303 -5.564  -22.302 0.25 45.74  ? 126 VAL   B CA  1 
ATOM   1287 C CA  C VAL   B 2 117 ? -10.294 -5.637  -22.366 0.25 46.37  ? 126 VAL   B CA  1 
ATOM   1288 C CA  D VAL   B 2 117 ? -10.303 -5.564  -22.302 0.25 45.74  ? 126 VAL   B CA  1 
ATOM   1289 C C   A VAL   B 2 117 ? -9.151  -4.634  -22.560 0.25 48.31  ? 126 VAL   B C   1 
ATOM   1290 C C   B VAL   B 2 117 ? -9.125  -4.614  -22.543 0.25 47.92  ? 126 VAL   B C   1 
ATOM   1291 C C   C VAL   B 2 117 ? -9.151  -4.634  -22.560 0.25 48.31  ? 126 VAL   B C   1 
ATOM   1292 C C   D VAL   B 2 117 ? -9.125  -4.614  -22.543 0.25 47.92  ? 126 VAL   B C   1 
ATOM   1293 O O   A VAL   B 2 117 ? -8.986  -3.745  -21.699 0.25 44.88  ? 126 VAL   B O   1 
ATOM   1294 O O   B VAL   B 2 117 ? -8.911  -3.724  -21.693 0.25 44.37  ? 126 VAL   B O   1 
ATOM   1295 O O   C VAL   B 2 117 ? -8.986  -3.745  -21.699 0.25 44.88  ? 126 VAL   B O   1 
ATOM   1296 O O   D VAL   B 2 117 ? -8.911  -3.724  -21.693 0.25 44.37  ? 126 VAL   B O   1 
ATOM   1297 C CB  A VAL   B 2 117 ? -11.674 -5.004  -22.618 0.25 46.19  ? 126 VAL   B CB  1 
ATOM   1298 C CB  B VAL   B 2 117 ? -11.650 -4.825  -22.357 0.25 45.27  ? 126 VAL   B CB  1 
ATOM   1299 C CB  C VAL   B 2 117 ? -11.674 -5.004  -22.618 0.25 46.19  ? 126 VAL   B CB  1 
ATOM   1300 C CB  D VAL   B 2 117 ? -11.650 -4.825  -22.357 0.25 45.27  ? 126 VAL   B CB  1 
ATOM   1301 C CG1 A VAL   B 2 117 ? -12.765 -6.062  -22.608 0.25 47.21  ? 126 VAL   B CG1 1 
ATOM   1302 C CG1 B VAL   B 2 117 ? -11.612 -3.661  -23.326 0.25 44.52  ? 126 VAL   B CG1 1 
ATOM   1303 C CG1 C VAL   B 2 117 ? -12.765 -6.062  -22.608 0.25 47.21  ? 126 VAL   B CG1 1 
ATOM   1304 C CG1 D VAL   B 2 117 ? -11.612 -3.661  -23.326 0.25 44.52  ? 126 VAL   B CG1 1 
ATOM   1305 C CG2 A VAL   B 2 117 ? -11.993 -3.894  -21.629 0.25 46.40  ? 126 VAL   B CG2 1 
ATOM   1306 C CG2 B VAL   B 2 117 ? -12.791 -5.775  -22.678 0.25 46.33  ? 126 VAL   B CG2 1 
ATOM   1307 C CG2 C VAL   B 2 117 ? -11.993 -3.894  -21.629 0.25 46.40  ? 126 VAL   B CG2 1 
ATOM   1308 C CG2 D VAL   B 2 117 ? -12.791 -5.775  -22.678 0.25 46.33  ? 126 VAL   B CG2 1 
ATOM   1309 N N   . ALA   B 2 118 ? -8.376  -4.807  -23.637 1.00 46.49  ? 127 ALA   B N   1 
ATOM   1310 C CA  . ALA   B 2 118 ? -7.227  -3.934  -23.981 1.00 53.98  ? 127 ALA   B CA  1 
ATOM   1311 C C   . ALA   B 2 118 ? -7.723  -2.897  -24.994 1.00 64.48  ? 127 ALA   B C   1 
ATOM   1312 O O   . ALA   B 2 118 ? -7.625  -3.146  -26.221 1.00 62.32  ? 127 ALA   B O   1 
ATOM   1313 C CB  . ALA   B 2 118 ? -6.057  -4.743  -24.504 1.00 55.93  ? 127 ALA   B CB  1 
ATOM   1314 N N   . LEU   B 2 119 ? -8.348  -1.837  -24.486 1.00 58.64  ? 128 LEU   B N   1 
ATOM   1315 C CA  . LEU   B 2 119 ? -8.813  -0.678  -25.275 1.00 49.35  ? 128 LEU   B CA  1 
ATOM   1316 C C   . LEU   B 2 119 ? -8.475  0.542   -24.427 1.00 48.69  ? 128 LEU   B C   1 
ATOM   1317 O O   . LEU   B 2 119 ? -8.886  0.582   -23.273 1.00 58.13  ? 128 LEU   B O   1 
ATOM   1318 C CB  . LEU   B 2 119 ? -10.313 -0.804  -25.576 1.00 51.26  ? 128 LEU   B CB  1 
ATOM   1319 C CG  . LEU   B 2 119 ? -10.790 -2.110  -26.219 1.00 48.15  ? 128 LEU   B CG  1 
ATOM   1320 C CD1 . LEU   B 2 119 ? -12.296 -2.272  -26.100 1.00 45.94  ? 128 LEU   B CD1 1 
ATOM   1321 C CD2 . LEU   B 2 119 ? -10.403 -2.195  -27.690 1.00 56.79  ? 128 LEU   B CD2 1 
ATOM   1322 N N   . ASP   B 2 120 ? -7.663  1.442   -24.959 1.00 48.22  ? 129 ASP   B N   1 
ATOM   1323 C CA  . ASP   B 2 120 ? -7.254  2.691   -24.289 1.00 51.17  ? 129 ASP   B CA  1 
ATOM   1324 C C   . ASP   B 2 120 ? -8.321  3.723   -24.635 1.00 53.13  ? 129 ASP   B C   1 
ATOM   1325 O O   . ASP   B 2 120 ? -8.724  3.728   -25.785 1.00 61.43  ? 129 ASP   B O   1 
ATOM   1326 C CB  . ASP   B 2 120 ? -5.849  3.059   -24.753 1.00 57.95  ? 129 ASP   B CB  1 
ATOM   1327 C CG  . ASP   B 2 120 ? -5.072  3.920   -23.774 1.00 68.24  ? 129 ASP   B CG  1 
ATOM   1328 O OD1 . ASP   B 2 120 ? -5.670  4.884   -23.212 1.00 67.98  ? 129 ASP   B OD1 1 
ATOM   1329 O OD2 . ASP   B 2 120 ? -3.874  3.620   -23.581 1.00 74.00  ? 129 ASP   B OD2 1 
ATOM   1330 N N   . TYR   B 2 121 ? -8.844  4.464   -23.655 1.00 54.94  ? 130 TYR   B N   1 
ATOM   1331 C CA  . TYR   B 2 121 ? -9.777  5.612   -23.833 1.00 49.84  ? 130 TYR   B CA  1 
ATOM   1332 C C   . TYR   B 2 121 ? -9.562  6.547   -22.655 1.00 51.72  ? 130 TYR   B C   1 
ATOM   1333 O O   . TYR   B 2 121 ? -8.887  6.182   -21.705 1.00 54.49  ? 130 TYR   B O   1 
ATOM   1334 C CB  . TYR   B 2 121 ? -11.236 5.172   -23.883 1.00 49.09  ? 130 TYR   B CB  1 
ATOM   1335 C CG  . TYR   B 2 121 ? -11.707 4.571   -25.187 1.00 56.21  ? 130 TYR   B CG  1 
ATOM   1336 C CD1 . TYR   B 2 121 ? -12.047 5.368   -26.268 1.00 57.77  ? 130 TYR   B CD1 1 
ATOM   1337 C CD2 . TYR   B 2 121 ? -11.847 3.198   -25.338 1.00 64.23  ? 130 TYR   B CD2 1 
ATOM   1338 C CE1 . TYR   B 2 121 ? -12.487 4.815   -27.465 1.00 59.56  ? 130 TYR   B CE1 1 
ATOM   1339 C CE2 . TYR   B 2 121 ? -12.288 2.629   -26.525 1.00 60.77  ? 130 TYR   B CE2 1 
ATOM   1340 C CZ  . TYR   B 2 121 ? -12.604 3.443   -27.596 1.00 60.21  ? 130 TYR   B CZ  1 
ATOM   1341 O OH  . TYR   B 2 121 ? -13.031 2.897   -28.773 1.00 72.73  ? 130 TYR   B OH  1 
ATOM   1342 N N   . PRO   B 2 122 ? -10.079 7.791   -22.655 1.00 52.27  ? 131 PRO   B N   1 
ATOM   1343 C CA  . PRO   B 2 122 ? -9.771  8.685   -21.547 1.00 50.30  ? 131 PRO   B CA  1 
ATOM   1344 C C   . PRO   B 2 122 ? -10.412 8.177   -20.235 1.00 49.13  ? 131 PRO   B C   1 
ATOM   1345 O O   . PRO   B 2 122 ? -11.330 7.357   -20.278 1.00 45.11  ? 131 PRO   B O   1 
ATOM   1346 C CB  . PRO   B 2 122 ? -10.271 10.058  -22.039 1.00 56.13  ? 131 PRO   B CB  1 
ATOM   1347 C CG  . PRO   B 2 122 ? -10.499 9.898   -23.543 1.00 54.19  ? 131 PRO   B CG  1 
ATOM   1348 C CD  . PRO   B 2 122 ? -10.852 8.439   -23.731 1.00 55.56  ? 131 PRO   B CD  1 
ATOM   1349 N N   . ALA   B 2 123 ? -9.891  8.653   -19.102 1.00 42.66  ? 132 ALA   B N   1 
ATOM   1350 C CA  . ALA   B 2 123 ? -10.301 8.269   -17.732 1.00 46.87  ? 132 ALA   B CA  1 
ATOM   1351 C C   . ALA   B 2 123 ? -11.794 8.555   -17.548 1.00 49.10  ? 132 ALA   B C   1 
ATOM   1352 O O   . ALA   B 2 123 ? -12.506 7.740   -16.884 1.00 40.02  ? 132 ALA   B O   1 
ATOM   1353 C CB  . ALA   B 2 123 ? -9.465  9.014   -16.734 1.00 49.86  ? 132 ALA   B CB  1 
ATOM   1354 N N   . GLY   B 2 124 ? -12.276 9.621   -18.195 1.00 45.26  ? 133 GLY   B N   1 
ATOM   1355 C CA  . GLY   B 2 124 ? -13.691 10.039  -18.118 1.00 40.53  ? 133 GLY   B CA  1 
ATOM   1356 C C   . GLY   B 2 124 ? -14.629 9.016   -18.732 1.00 39.75  ? 133 GLY   B C   1 
ATOM   1357 O O   . GLY   B 2 124 ? -15.892 9.211   -18.611 1.00 38.67  ? 133 GLY   B O   1 
ATOM   1358 N N   . THR   B 2 125 ? -14.076 8.005   -19.418 1.00 35.40  ? 134 THR   B N   1 
ATOM   1359 C CA  . THR   B 2 125 ? -14.850 6.877   -20.013 1.00 36.10  ? 134 THR   B CA  1 
ATOM   1360 C C   . THR   B 2 125 ? -15.169 5.815   -18.939 1.00 36.30  ? 134 THR   B C   1 
ATOM   1361 O O   . THR   B 2 125 ? -16.022 4.958   -19.203 1.00 36.02  ? 134 THR   B O   1 
ATOM   1362 C CB  . THR   B 2 125 ? -14.117 6.303   -21.242 1.00 42.59  ? 134 THR   B CB  1 
ATOM   1363 O OG1 . THR   B 2 125 ? -13.735 7.374   -22.103 1.00 45.70  ? 134 THR   B OG1 1 
ATOM   1364 C CG2 . THR   B 2 125 ? -14.947 5.341   -22.068 1.00 36.12  ? 134 THR   B CG2 1 
ATOM   1365 N N   . SER   B 2 126 ? -14.517 5.865   -17.768 1.00 38.23  ? 135 SER   B N   1 
ATOM   1366 C CA  . SER   B 2 126 ? -14.745 4.928   -16.626 1.00 40.02  ? 135 SER   B CA  1 
ATOM   1367 C C   . SER   B 2 126 ? -16.243 4.732   -16.358 1.00 36.19  ? 135 SER   B C   1 
ATOM   1368 O O   . SER   B 2 126 ? -16.907 5.728   -16.152 1.00 37.87  ? 135 SER   B O   1 
ATOM   1369 C CB  . SER   B 2 126 ? -14.072 5.433   -15.409 1.00 39.18  ? 135 SER   B CB  1 
ATOM   1370 O OG  . SER   B 2 126 ? -12.679 5.240   -15.489 1.00 43.00  ? 135 SER   B OG  1 
ATOM   1371 N N   . GLY   B 2 127 ? -16.739 3.494   -16.378 1.00 36.72  ? 136 GLY   B N   1 
ATOM   1372 C CA  . GLY   B 2 127 ? -18.145 3.161   -16.101 1.00 33.43  ? 136 GLY   B CA  1 
ATOM   1373 C C   . GLY   B 2 127 ? -18.863 2.633   -17.308 1.00 33.74  ? 136 GLY   B C   1 
ATOM   1374 O O   . GLY   B 2 127 ? -19.967 2.059   -17.139 1.00 39.29  ? 136 GLY   B O   1 
ATOM   1375 N N   . SER   B 2 128 ? -18.285 2.794   -18.493 1.00 37.74  ? 137 SER   B N   1 
ATOM   1376 C CA  . SER   B 2 128 ? -18.895 2.322   -19.763 1.00 35.13  ? 137 SER   B CA  1 
ATOM   1377 C C   . SER   B 2 128 ? -19.069 0.823   -19.657 1.00 33.49  ? 137 SER   B C   1 
ATOM   1378 O O   . SER   B 2 128 ? -18.133 0.106   -19.327 1.00 34.25  ? 137 SER   B O   1 
ATOM   1379 C CB  . SER   B 2 128 ? -18.070 2.675   -20.997 1.00 36.42  ? 137 SER   B CB  1 
ATOM   1380 O OG  . SER   B 2 128 ? -17.785 4.074   -21.078 1.00 40.75  ? 137 SER   B OG  1 
ATOM   1381 N N   . PRO   B 2 129 ? -20.243 0.311   -20.036 1.00 29.71  ? 138 PRO   B N   1 
ATOM   1382 C CA  . PRO   B 2 129 ? -20.521 -1.110  -19.989 1.00 31.99  ? 138 PRO   B CA  1 
ATOM   1383 C C   . PRO   B 2 129 ? -19.886 -1.934  -21.109 1.00 38.54  ? 138 PRO   B C   1 
ATOM   1384 O O   . PRO   B 2 129 ? -19.677 -1.434  -22.206 1.00 37.71  ? 138 PRO   B O   1 
ATOM   1385 C CB  . PRO   B 2 129 ? -22.036 -1.168  -20.225 1.00 33.37  ? 138 PRO   B CB  1 
ATOM   1386 C CG  . PRO   B 2 129 ? -22.281 0.012   -21.120 1.00 32.86  ? 138 PRO   B CG  1 
ATOM   1387 C CD  . PRO   B 2 129 ? -21.376 1.078   -20.555 1.00 31.69  ? 138 PRO   B CD  1 
ATOM   1388 N N   . ILE   B 2 130 ? -19.669 -3.214  -20.812 1.00 41.54  ? 139 ILE   B N   1 
ATOM   1389 C CA  . ILE   B 2 130 ? -19.114 -4.228  -21.744 1.00 36.59  ? 139 ILE   B CA  1 
ATOM   1390 C C   . ILE   B 2 130 ? -20.250 -5.212  -21.916 1.00 37.38  ? 139 ILE   B C   1 
ATOM   1391 O O   . ILE   B 2 130 ? -20.840 -5.460  -20.873 1.00 31.81  ? 139 ILE   B O   1 
ATOM   1392 C CB  . ILE   B 2 130 ? -17.853 -4.861  -21.139 1.00 42.08  ? 139 ILE   B CB  1 
ATOM   1393 C CG1 . ILE   B 2 130 ? -16.737 -3.834  -20.964 1.00 44.45  ? 139 ILE   B CG1 1 
ATOM   1394 C CG2 . ILE   B 2 130 ? -17.377 -6.061  -21.938 1.00 45.49  ? 139 ILE   B CG2 1 
ATOM   1395 C CD1 . ILE   B 2 130 ? -15.709 -4.287  -19.967 1.00 46.06  ? 139 ILE   B CD1 1 
ATOM   1396 N N   . LEU   B 2 131 ? -20.588 -5.625  -23.155 1.00 39.96  ? 140 LEU   B N   1 
ATOM   1397 C CA  . LEU   B 2 131 ? -21.822 -6.406  -23.472 1.00 45.61  ? 140 LEU   B CA  1 
ATOM   1398 C C   . LEU   B 2 131 ? -21.518 -7.771  -24.091 1.00 43.90  ? 140 LEU   B C   1 
ATOM   1399 O O   . LEU   B 2 131 ? -20.550 -7.884  -24.836 1.00 50.85  ? 140 LEU   B O   1 
ATOM   1400 C CB  . LEU   B 2 131 ? -22.682 -5.646  -24.488 1.00 54.50  ? 140 LEU   B CB  1 
ATOM   1401 C CG  . LEU   B 2 131 ? -22.973 -4.179  -24.194 1.00 55.44  ? 140 LEU   B CG  1 
ATOM   1402 C CD1 . LEU   B 2 131 ? -23.771 -3.560  -25.350 1.00 52.37  ? 140 LEU   B CD1 1 
ATOM   1403 C CD2 . LEU   B 2 131 ? -23.705 -4.054  -22.866 1.00 54.33  ? 140 LEU   B CD2 1 
ATOM   1404 N N   . ASP   B 2 132 ? -22.418 -8.721  -23.869 1.00 46.72  ? 141 ASP   B N   1 
ATOM   1405 C CA  . ASP   B 2 132 ? -22.464 -10.039 -24.548 1.00 56.58  ? 141 ASP   B CA  1 
ATOM   1406 C C   . ASP   B 2 132 ? -23.333 -9.913  -25.814 1.00 64.88  ? 141 ASP   B C   1 
ATOM   1407 O O   . ASP   B 2 132 ? -23.842 -8.798  -26.083 1.00 65.20  ? 141 ASP   B O   1 
ATOM   1408 C CB  . ASP   B 2 132 ? -22.927 -11.125 -23.566 1.00 50.29  ? 141 ASP   B CB  1 
ATOM   1409 C CG  . ASP   B 2 132 ? -24.412 -11.173 -23.261 1.00 50.83  ? 141 ASP   B CG  1 
ATOM   1410 O OD1 . ASP   B 2 132 ? -25.171 -10.488 -23.925 1.00 56.48  ? 141 ASP   B OD1 1 
ATOM   1411 O OD2 . ASP   B 2 132 ? -24.793 -11.917 -22.346 1.00 60.62  ? 141 ASP   B OD2 1 
ATOM   1412 N N   . LYS   B 2 133 ? -23.516 -11.012 -26.554 1.00 69.52  ? 142 LYS   B N   1 
ATOM   1413 C CA  . LYS   B 2 133 ? -24.104 -10.994 -27.925 1.00 73.07  ? 142 LYS   B CA  1 
ATOM   1414 C C   . LYS   B 2 133 ? -25.604 -10.710 -27.810 1.00 65.24  ? 142 LYS   B C   1 
ATOM   1415 O O   . LYS   B 2 133 ? -26.148 -10.070 -28.715 1.00 69.38  ? 142 LYS   B O   1 
ATOM   1416 C CB  . LYS   B 2 133 ? -23.783 -12.292 -28.681 1.00 77.48  ? 142 LYS   B CB  1 
ATOM   1417 C CG  . LYS   B 2 133 ? -22.397 -12.325 -29.323 1.00 85.61  ? 142 LYS   B CG  1 
ATOM   1418 C CD  . LYS   B 2 133 ? -21.748 -13.701 -29.385 1.00 91.85  ? 142 LYS   B CD  1 
ATOM   1419 C CE  . LYS   B 2 133 ? -20.281 -13.629 -29.763 1.00 99.85  ? 142 LYS   B CE  1 
ATOM   1420 N NZ  . LYS   B 2 133 ? -19.750 -14.924 -30.257 1.00 101.95 ? 142 LYS   B NZ  1 
ATOM   1421 N N   . CYS   B 2 134 ? -26.215 -11.107 -26.695 1.00 60.33  ? 143 CYS   B N   1 
ATOM   1422 C CA  . CYS   B 2 134 ? -27.634 -10.840 -26.355 1.00 56.75  ? 143 CYS   B CA  1 
ATOM   1423 C C   . CYS   B 2 134 ? -27.831 -9.422  -25.788 1.00 47.45  ? 143 CYS   B C   1 
ATOM   1424 O O   . CYS   B 2 134 ? -28.968 -9.105  -25.409 1.00 51.91  ? 143 CYS   B O   1 
ATOM   1425 C CB  . CYS   B 2 134 ? -28.121 -11.847 -25.331 1.00 65.19  ? 143 CYS   B CB  1 
ATOM   1426 S SG  . CYS   B 2 134 ? -28.401 -13.492 -26.019 1.00 73.97  ? 143 CYS   B SG  1 
ATOM   1427 N N   . GLY   B 2 135 ? -26.791 -8.586  -25.757 1.00 41.67  ? 144 GLY   B N   1 
ATOM   1428 C CA  . GLY   B 2 135 ? -26.859 -7.198  -25.231 1.00 53.88  ? 144 GLY   B CA  1 
ATOM   1429 C C   . GLY   B 2 135 ? -26.929 -7.054  -23.699 1.00 45.20  ? 144 GLY   B C   1 
ATOM   1430 O O   . GLY   B 2 135 ? -27.224 -5.955  -23.237 1.00 46.48  ? 144 GLY   B O   1 
ATOM   1431 N N   . ARG   B 2 136 ? -26.605 -8.090  -22.928 1.00 49.90  ? 145 ARG   B N   1 
ATOM   1432 C CA  . ARG   B 2 136 ? -26.555 -8.061  -21.441 1.00 50.09  ? 145 ARG   B CA  1 
ATOM   1433 C C   . ARG   B 2 136 ? -25.220 -7.487  -20.944 1.00 46.07  ? 145 ARG   B C   1 
ATOM   1434 O O   . ARG   B 2 136 ? -24.177 -7.776  -21.562 1.00 43.98  ? 145 ARG   B O   1 
ATOM   1435 C CB  . ARG   B 2 136 ? -26.818 -9.469  -20.937 1.00 50.02  ? 145 ARG   B CB  1 
ATOM   1436 C CG  . ARG   B 2 136 ? -28.296 -9.814  -20.964 1.00 59.82  ? 145 ARG   B CG  1 
ATOM   1437 C CD  . ARG   B 2 136 ? -28.508 -11.250 -20.572 1.00 63.92  ? 145 ARG   B CD  1 
ATOM   1438 N NE  . ARG   B 2 136 ? -27.739 -12.091 -21.476 1.00 77.32  ? 145 ARG   B NE  1 
ATOM   1439 C CZ  . ARG   B 2 136 ? -27.228 -13.285 -21.186 1.00 80.08  ? 145 ARG   B CZ  1 
ATOM   1440 N NH1 . ARG   B 2 136 ? -27.368 -13.825 -19.980 1.00 81.01  ? 145 ARG   B NH1 1 
ATOM   1441 N NH2 . ARG   B 2 136 ? -26.556 -13.925 -22.125 1.00 82.00  ? 145 ARG   B NH2 1 
ATOM   1442 N N   . VAL   B 2 137 ? -25.248 -6.676  -19.881 1.00 43.13  ? 146 VAL   B N   1 
ATOM   1443 C CA  . VAL   B 2 137 ? -24.018 -6.020  -19.339 1.00 40.89  ? 146 VAL   B CA  1 
ATOM   1444 C C   . VAL   B 2 137 ? -23.291 -7.073  -18.507 1.00 44.08  ? 146 VAL   B C   1 
ATOM   1445 O O   . VAL   B 2 137 ? -23.903 -7.631  -17.561 1.00 44.61  ? 146 VAL   B O   1 
ATOM   1446 C CB  . VAL   B 2 137 ? -24.297 -4.758  -18.502 1.00 41.12  ? 146 VAL   B CB  1 
ATOM   1447 C CG1 . VAL   B 2 137 ? -23.019 -3.967  -18.264 1.00 43.15  ? 146 VAL   B CG1 1 
ATOM   1448 C CG2 . VAL   B 2 137 ? -25.351 -3.876  -19.156 1.00 48.29  ? 146 VAL   B CG2 1 
ATOM   1449 N N   . ILE   B 2 138 ? -22.044 -7.343  -18.858 1.00 42.25  ? 147 ILE   B N   1 
ATOM   1450 C CA  . ILE   B 2 138 ? -21.223 -8.395  -18.195 1.00 43.18  ? 147 ILE   B CA  1 
ATOM   1451 C C   . ILE   B 2 138 ? -20.201 -7.693  -17.300 1.00 40.40  ? 147 ILE   B C   1 
ATOM   1452 O O   . ILE   B 2 138 ? -19.478 -8.391  -16.584 1.00 43.46  ? 147 ILE   B O   1 
ATOM   1453 C CB  . ILE   B 2 138 ? -20.550 -9.337  -19.225 1.00 42.26  ? 147 ILE   B CB  1 
ATOM   1454 C CG1 . ILE   B 2 138 ? -19.791 -8.561  -20.293 1.00 43.60  ? 147 ILE   B CG1 1 
ATOM   1455 C CG2 . ILE   B 2 138 ? -21.542 -10.302 -19.829 1.00 37.41  ? 147 ILE   B CG2 1 
ATOM   1456 C CD1 . ILE   B 2 138 ? -18.776 -9.384  -21.019 1.00 52.41  ? 147 ILE   B CD1 1 
ATOM   1457 N N   . GLY   B 2 139 ? -20.119 -6.363  -17.354 1.00 33.65  ? 148 GLY   B N   1 
ATOM   1458 C CA  . GLY   B 2 139 ? -19.240 -5.627  -16.439 1.00 31.56  ? 148 GLY   B CA  1 
ATOM   1459 C C   . GLY   B 2 139 ? -19.005 -4.227  -16.913 1.00 32.76  ? 148 GLY   B C   1 
ATOM   1460 O O   . GLY   B 2 139 ? -19.536 -3.890  -17.987 1.00 31.13  ? 148 GLY   B O   1 
ATOM   1461 N N   . LEU   B 2 140 ? -18.218 -3.461  -16.155 1.00 32.14  ? 149 LEU   B N   1 
ATOM   1462 C CA  . LEU   B 2 140 ? -17.941 -2.043  -16.455 1.00 35.68  ? 149 LEU   B CA  1 
ATOM   1463 C C   . LEU   B 2 140 ? -16.442 -1.905  -16.672 1.00 36.98  ? 149 LEU   B C   1 
ATOM   1464 O O   . LEU   B 2 140 ? -15.675 -2.658  -16.023 1.00 36.05  ? 149 LEU   B O   1 
ATOM   1465 C CB  . LEU   B 2 140 ? -18.383 -1.137  -15.300 1.00 36.38  ? 149 LEU   B CB  1 
ATOM   1466 C CG  . LEU   B 2 140 ? -19.841 -1.194  -14.838 1.00 37.27  ? 149 LEU   B CG  1 
ATOM   1467 C CD1 . LEU   B 2 140 ? -20.153 0.028   -13.966 1.00 42.23  ? 149 LEU   B CD1 1 
ATOM   1468 C CD2 . LEU   B 2 140 ? -20.818 -1.274  -15.989 1.00 37.90  ? 149 LEU   B CD2 1 
ATOM   1469 N N   . TYR   B 2 141 ? -16.089 -0.937  -17.516 1.00 34.66  ? 150 TYR   B N   1 
ATOM   1470 C CA  . TYR   B 2 141 ? -14.735 -0.582  -17.981 1.00 37.87  ? 150 TYR   B CA  1 
ATOM   1471 C C   . TYR   B 2 141 ? -14.231 0.537   -17.092 1.00 37.18  ? 150 TYR   B C   1 
ATOM   1472 O O   . TYR   B 2 141 ? -15.059 1.392   -16.763 1.00 40.99  ? 150 TYR   B O   1 
ATOM   1473 C CB  . TYR   B 2 141 ? -14.824 -0.133  -19.455 1.00 41.59  ? 150 TYR   B CB  1 
ATOM   1474 C CG  . TYR   B 2 141 ? -13.579 0.513   -20.023 1.00 43.97  ? 150 TYR   B CG  1 
ATOM   1475 C CD1 . TYR   B 2 141 ? -13.411 1.886   -19.994 1.00 39.79  ? 150 TYR   B CD1 1 
ATOM   1476 C CD2 . TYR   B 2 141 ? -12.561 -0.250  -20.585 1.00 46.58  ? 150 TYR   B CD2 1 
ATOM   1477 C CE1 . TYR   B 2 141 ? -12.259 2.479   -20.482 1.00 46.66  ? 150 TYR   B CE1 1 
ATOM   1478 C CE2 . TYR   B 2 141 ? -11.412 0.330   -21.097 1.00 39.78  ? 150 TYR   B CE2 1 
ATOM   1479 C CZ  . TYR   B 2 141 ? -11.258 1.706   -21.067 1.00 51.37  ? 150 TYR   B CZ  1 
ATOM   1480 O OH  . TYR   B 2 141 ? -10.120 2.309   -21.583 1.00 44.50  ? 150 TYR   B OH  1 
ATOM   1481 N N   . GLY   B 2 142 ? -12.948 0.557   -16.727 1.00 40.28  ? 151 GLY   B N   1 
ATOM   1482 C CA  . GLY   B 2 142 ? -12.342 1.737   -16.073 1.00 43.36  ? 151 GLY   B CA  1 
ATOM   1483 C C   . GLY   B 2 142 ? -11.539 1.444   -14.810 1.00 44.62  ? 151 GLY   B C   1 
ATOM   1484 O O   . GLY   B 2 142 ? -10.988 2.434   -14.261 1.00 45.01  ? 151 GLY   B O   1 
ATOM   1485 N N   . ASN   B 2 143 ? -11.422 0.169   -14.377 1.00 40.79  ? 152 ASN   B N   1 
ATOM   1486 C CA  . ASN   B 2 143 ? -10.420 -0.263  -13.361 1.00 42.32  ? 152 ASN   B CA  1 
ATOM   1487 C C   . ASN   B 2 143 ? -9.442  -1.284  -13.972 1.00 40.49  ? 152 ASN   B C   1 
ATOM   1488 O O   . ASN   B 2 143 ? -9.837  -2.422  -14.268 1.00 40.87  ? 152 ASN   B O   1 
ATOM   1489 C CB  . ASN   B 2 143 ? -11.093 -0.845  -12.114 1.00 39.65  ? 152 ASN   B CB  1 
ATOM   1490 C CG  . ASN   B 2 143 ? -10.185 -1.009  -10.914 1.00 40.77  ? 152 ASN   B CG  1 
ATOM   1491 O OD1 . ASN   B 2 143 ? -9.293  -0.188  -10.645 1.00 39.24  ? 152 ASN   B OD1 1 
ATOM   1492 N ND2 . ASN   B 2 143 ? -10.467 -2.038  -10.131 1.00 41.46  ? 152 ASN   B ND2 1 
ATOM   1493 N N   . GLY   B 2 144 ? -8.184  -0.896  -14.091 1.00 41.58  ? 153 GLY   B N   1 
ATOM   1494 C CA  . GLY   B 2 144 ? -7.150  -1.729  -14.713 1.00 46.88  ? 153 GLY   B CA  1 
ATOM   1495 C C   . GLY   B 2 144 ? -5.774  -1.147  -14.488 1.00 50.51  ? 153 GLY   B C   1 
ATOM   1496 O O   . GLY   B 2 144 ? -5.563  -0.500  -13.434 1.00 50.55  ? 153 GLY   B O   1 
ATOM   1497 N N   . VAL   B 2 145 ? -4.881  -1.347  -15.455 1.00 48.74  ? 154 VAL   B N   1 
ATOM   1498 C CA  . VAL   B 2 145 ? -3.413  -1.342  -15.228 1.00 49.18  ? 154 VAL   B CA  1 
ATOM   1499 C C   . VAL   B 2 145 ? -2.724  -0.879  -16.521 1.00 55.34  ? 154 VAL   B C   1 
ATOM   1500 O O   . VAL   B 2 145 ? -3.303  -1.078  -17.630 1.00 48.21  ? 154 VAL   B O   1 
ATOM   1501 C CB  . VAL   B 2 145 ? -2.983  -2.740  -14.722 1.00 53.29  ? 154 VAL   B CB  1 
ATOM   1502 C CG1 . VAL   B 2 145 ? -2.832  -3.779  -15.826 1.00 49.25  ? 154 VAL   B CG1 1 
ATOM   1503 C CG2 . VAL   B 2 145 ? -1.729  -2.663  -13.875 1.00 54.64  ? 154 VAL   B CG2 1 
ATOM   1504 N N   . VAL   B 2 146 ? -1.575  -0.215  -16.378 1.00 57.12  ? 155 VAL   B N   1 
ATOM   1505 C CA  . VAL   B 2 146 ? -0.727  0.235   -17.517 1.00 65.97  ? 155 VAL   B CA  1 
ATOM   1506 C C   . VAL   B 2 146 ? 0.390   -0.799  -17.699 1.00 63.90  ? 155 VAL   B C   1 
ATOM   1507 O O   . VAL   B 2 146 ? 1.025   -1.111  -16.689 1.00 63.17  ? 155 VAL   B O   1 
ATOM   1508 C CB  . VAL   B 2 146 ? -0.203  1.663   -17.289 1.00 65.36  ? 155 VAL   B CB  1 
ATOM   1509 C CG1 . VAL   B 2 146 ? 0.387   2.224   -18.565 1.00 71.26  ? 155 VAL   B CG1 1 
ATOM   1510 C CG2 . VAL   B 2 146 ? -1.304  2.584   -16.792 1.00 66.51  ? 155 VAL   B CG2 1 
ATOM   1511 N N   . ILE   B 2 147 ? 0.572   -1.348  -18.912 1.00 66.06  ? 156 ILE   B N   1 
ATOM   1512 C CA  . ILE   B 2 147 ? 1.377   -2.593  -19.136 1.00 70.23  ? 156 ILE   B CA  1 
ATOM   1513 C C   . ILE   B 2 147 ? 2.743   -2.196  -19.688 1.00 71.74  ? 156 ILE   B C   1 
ATOM   1514 O O   . ILE   B 2 147 ? 2.933   -1.016  -19.984 1.00 65.66  ? 156 ILE   B O   1 
ATOM   1515 C CB  . ILE   B 2 147 ? 0.649   -3.632  -20.022 1.00 73.05  ? 156 ILE   B CB  1 
ATOM   1516 C CG1 . ILE   B 2 147 ? 0.039   -3.036  -21.296 1.00 77.84  ? 156 ILE   B CG1 1 
ATOM   1517 C CG2 . ILE   B 2 147 ? -0.387  -4.380  -19.199 1.00 74.76  ? 156 ILE   B CG2 1 
ATOM   1518 C CD1 . ILE   B 2 147 ? -0.225  -4.055  -22.392 1.00 73.12  ? 156 ILE   B CD1 1 
ATOM   1519 N N   A LYS   B 2 148 ? 3.660   -3.172  -19.784 0.25 76.69  ? 157 LYS   B N   1 
ATOM   1520 N N   B LYS   B 2 148 ? 3.660   -3.172  -19.784 0.25 76.69  ? 157 LYS   B N   1 
ATOM   1521 N N   C LYS   B 2 148 ? 3.656   -3.166  -19.814 0.25 75.96  ? 157 LYS   B N   1 
ATOM   1522 N N   D LYS   B 2 148 ? 3.656   -3.166  -19.814 0.25 75.96  ? 157 LYS   B N   1 
ATOM   1523 C CA  A LYS   B 2 148 ? 5.028   -3.040  -20.367 0.25 79.28  ? 157 LYS   B CA  1 
ATOM   1524 C CA  B LYS   B 2 148 ? 5.028   -3.040  -20.367 0.25 79.28  ? 157 LYS   B CA  1 
ATOM   1525 C CA  C LYS   B 2 148 ? 5.048   -2.976  -20.312 0.25 77.87  ? 157 LYS   B CA  1 
ATOM   1526 C CA  D LYS   B 2 148 ? 5.048   -2.976  -20.312 0.25 77.87  ? 157 LYS   B CA  1 
ATOM   1527 C C   A LYS   B 2 148 ? 5.043   -1.919  -21.410 0.25 78.54  ? 157 LYS   B C   1 
ATOM   1528 C C   B LYS   B 2 148 ? 5.043   -1.919  -21.410 0.25 78.54  ? 157 LYS   B C   1 
ATOM   1529 C C   C LYS   B 2 148 ? 5.072   -1.930  -21.436 0.25 77.96  ? 157 LYS   B C   1 
ATOM   1530 C C   D LYS   B 2 148 ? 5.072   -1.930  -21.436 0.25 77.96  ? 157 LYS   B C   1 
ATOM   1531 O O   A LYS   B 2 148 ? 5.920   -1.038  -21.325 0.25 82.57  ? 157 LYS   B O   1 
ATOM   1532 O O   B LYS   B 2 148 ? 5.920   -1.038  -21.325 0.25 82.57  ? 157 LYS   B O   1 
ATOM   1533 O O   C LYS   B 2 148 ? 6.002   -1.100  -21.438 0.25 83.03  ? 157 LYS   B O   1 
ATOM   1534 O O   D LYS   B 2 148 ? 6.002   -1.100  -21.438 0.25 83.03  ? 157 LYS   B O   1 
ATOM   1535 C CB  A LYS   B 2 148 ? 5.461   -4.341  -21.055 0.25 81.90  ? 157 LYS   B CB  1 
ATOM   1536 C CB  B LYS   B 2 148 ? 5.461   -4.341  -21.055 0.25 81.90  ? 157 LYS   B CB  1 
ATOM   1537 C CB  C LYS   B 2 148 ? 5.622   -4.311  -20.800 0.25 79.10  ? 157 LYS   B CB  1 
ATOM   1538 C CB  D LYS   B 2 148 ? 5.622   -4.311  -20.800 0.25 79.10  ? 157 LYS   B CB  1 
ATOM   1539 C CG  A LYS   B 2 148 ? 5.988   -5.443  -20.144 0.25 82.53  ? 157 LYS   B CG  1 
ATOM   1540 C CG  B LYS   B 2 148 ? 5.988   -5.443  -20.144 0.25 82.53  ? 157 LYS   B CG  1 
ATOM   1541 C CG  C LYS   B 2 148 ? 5.430   -5.488  -19.850 0.25 78.91  ? 157 LYS   B CG  1 
ATOM   1542 C CG  D LYS   B 2 148 ? 5.430   -5.488  -19.850 0.25 78.91  ? 157 LYS   B CG  1 
ATOM   1543 C CD  A LYS   B 2 148 ? 6.281   -6.744  -20.878 0.25 82.63  ? 157 LYS   B CD  1 
ATOM   1544 C CD  B LYS   B 2 148 ? 6.281   -6.744  -20.878 0.25 82.63  ? 157 LYS   B CD  1 
ATOM   1545 C CD  C LYS   B 2 148 ? 4.126   -6.243  -20.051 0.25 76.92  ? 157 LYS   B CD  1 
ATOM   1546 C CD  D LYS   B 2 148 ? 4.126   -6.243  -20.051 0.25 76.92  ? 157 LYS   B CD  1 
ATOM   1547 C CE  A LYS   B 2 148 ? 7.381   -6.620  -21.913 0.25 82.79  ? 157 LYS   B CE  1 
ATOM   1548 C CE  B LYS   B 2 148 ? 7.381   -6.620  -21.913 0.25 82.79  ? 157 LYS   B CE  1 
ATOM   1549 C CE  C LYS   B 2 148 ? 3.904   -6.666  -21.488 0.25 76.44  ? 157 LYS   B CE  1 
ATOM   1550 C CE  D LYS   B 2 148 ? 3.904   -6.666  -21.488 0.25 76.44  ? 157 LYS   B CE  1 
ATOM   1551 N NZ  A LYS   B 2 148 ? 8.727   -6.630  -21.292 0.25 82.16  ? 157 LYS   B NZ  1 
ATOM   1552 N NZ  B LYS   B 2 148 ? 8.727   -6.630  -21.292 0.25 82.16  ? 157 LYS   B NZ  1 
ATOM   1553 N NZ  C LYS   B 2 148 ? 3.289   -5.580  -22.286 0.25 74.51  ? 157 LYS   B NZ  1 
ATOM   1554 N NZ  D LYS   B 2 148 ? 3.289   -5.580  -22.286 0.25 74.51  ? 157 LYS   B NZ  1 
ATOM   1555 N N   . ASN   B 2 149 ? 4.081   -1.963  -22.337 1.00 77.10  ? 158 ASN   B N   1 
ATOM   1556 C CA  . ASN   B 2 149 ? 3.994   -1.062  -23.520 1.00 77.10  ? 158 ASN   B CA  1 
ATOM   1557 C C   . ASN   B 2 149 ? 3.673   0.385   -23.148 1.00 74.67  ? 158 ASN   B C   1 
ATOM   1558 O O   . ASN   B 2 149 ? 3.869   1.237   -24.015 1.00 69.97  ? 158 ASN   B O   1 
ATOM   1559 C CB  . ASN   B 2 149 ? 2.883   -1.494  -24.486 1.00 79.24  ? 158 ASN   B CB  1 
ATOM   1560 C CG  . ASN   B 2 149 ? 2.781   -2.994  -24.685 1.00 84.93  ? 158 ASN   B CG  1 
ATOM   1561 O OD1 . ASN   B 2 149 ? 3.600   -3.765  -24.184 1.00 95.89  ? 158 ASN   B OD1 1 
ATOM   1562 N ND2 . ASN   B 2 149 ? 1.772   -3.422  -25.422 1.00 89.26  ? 158 ASN   B ND2 1 
ATOM   1563 N N   . GLY   B 2 150 ? 3.100   0.637   -21.966 1.00 79.39  ? 159 GLY   B N   1 
ATOM   1564 C CA  . GLY   B 2 150 ? 2.530   1.947   -21.576 1.00 68.30  ? 159 GLY   B CA  1 
ATOM   1565 C C   . GLY   B 2 150 ? 1.050   2.089   -21.924 1.00 67.33  ? 159 GLY   B C   1 
ATOM   1566 O O   . GLY   B 2 150 ? 0.464   3.160   -21.645 1.00 64.92  ? 159 GLY   B O   1 
ATOM   1567 N N   A SER   B 2 151 ? 0.458   1.042   -22.514 0.25 68.19  ? 160 SER   B N   1 
ATOM   1568 N N   B SER   B 2 151 ? 0.465   1.037   -22.510 0.25 66.75  ? 160 SER   B N   1 
ATOM   1569 N N   C SER   B 2 151 ? 0.458   1.042   -22.514 0.25 68.19  ? 160 SER   B N   1 
ATOM   1570 N N   D SER   B 2 151 ? 0.465   1.037   -22.510 0.25 66.75  ? 160 SER   B N   1 
ATOM   1571 C CA  A SER   B 2 151 ? -0.971  0.976   -22.924 0.25 66.24  ? 160 SER   B CA  1 
ATOM   1572 C CA  B SER   B 2 151 ? -0.963  0.948   -22.916 0.25 64.03  ? 160 SER   B CA  1 
ATOM   1573 C CA  C SER   B 2 151 ? -0.971  0.976   -22.924 0.25 66.24  ? 160 SER   B CA  1 
ATOM   1574 C CA  D SER   B 2 151 ? -0.963  0.948   -22.916 0.25 64.03  ? 160 SER   B CA  1 
ATOM   1575 C C   A SER   B 2 151 ? -1.826  0.532   -21.730 0.25 62.98  ? 160 SER   B C   1 
ATOM   1576 C C   B SER   B 2 151 ? -1.819  0.559   -21.705 0.25 61.71  ? 160 SER   B C   1 
ATOM   1577 C C   C SER   B 2 151 ? -1.826  0.532   -21.730 0.25 62.98  ? 160 SER   B C   1 
ATOM   1578 C C   D SER   B 2 151 ? -1.819  0.559   -21.705 0.25 61.71  ? 160 SER   B C   1 
ATOM   1579 O O   A SER   B 2 151 ? -1.278  -0.131  -20.822 0.25 59.90  ? 160 SER   B O   1 
ATOM   1580 O O   B SER   B 2 151 ? -1.263  -0.044  -20.760 0.25 58.62  ? 160 SER   B O   1 
ATOM   1581 O O   C SER   B 2 151 ? -1.278  -0.131  -20.822 0.25 59.90  ? 160 SER   B O   1 
ATOM   1582 O O   D SER   B 2 151 ? -1.263  -0.044  -20.760 0.25 58.62  ? 160 SER   B O   1 
ATOM   1583 C CB  A SER   B 2 151 ? -1.153  0.059   -24.109 0.25 66.57  ? 160 SER   B CB  1 
ATOM   1584 C CB  B SER   B 2 151 ? -1.135  -0.041  -24.036 0.25 62.96  ? 160 SER   B CB  1 
ATOM   1585 C CB  C SER   B 2 151 ? -1.153  0.059   -24.109 0.25 66.57  ? 160 SER   B CB  1 
ATOM   1586 C CB  D SER   B 2 151 ? -1.135  -0.041  -24.036 0.25 62.96  ? 160 SER   B CB  1 
ATOM   1587 O OG  A SER   B 2 151 ? -2.445  0.214   -24.681 0.25 67.77  ? 160 SER   B OG  1 
ATOM   1588 O OG  B SER   B 2 151 ? -0.613  -1.307  -23.662 0.25 60.92  ? 160 SER   B OG  1 
ATOM   1589 O OG  C SER   B 2 151 ? -2.445  0.214   -24.681 0.25 67.77  ? 160 SER   B OG  1 
ATOM   1590 O OG  D SER   B 2 151 ? -0.613  -1.307  -23.662 0.25 60.92  ? 160 SER   B OG  1 
ATOM   1591 N N   . TYR   B 2 152 ? -3.116  0.885   -21.748 1.00 58.83  ? 161 TYR   B N   1 
ATOM   1592 C CA  . TYR   B 2 152 ? -4.076  0.617   -20.645 1.00 57.45  ? 161 TYR   B CA  1 
ATOM   1593 C C   . TYR   B 2 152 ? -4.864  -0.670  -20.906 1.00 51.52  ? 161 TYR   B C   1 
ATOM   1594 O O   . TYR   B 2 152 ? -5.388  -0.836  -21.985 1.00 51.57  ? 161 TYR   B O   1 
ATOM   1595 C CB  . TYR   B 2 152 ? -5.024  1.811   -20.512 1.00 59.97  ? 161 TYR   B CB  1 
ATOM   1596 C CG  . TYR   B 2 152 ? -6.036  1.676   -19.406 1.00 56.98  ? 161 TYR   B CG  1 
ATOM   1597 C CD1 . TYR   B 2 152 ? -5.681  1.926   -18.090 1.00 56.89  ? 161 TYR   B CD1 1 
ATOM   1598 C CD2 . TYR   B 2 152 ? -7.334  1.273   -19.676 1.00 58.40  ? 161 TYR   B CD2 1 
ATOM   1599 C CE1 . TYR   B 2 152 ? -6.591  1.780   -17.060 1.00 54.90  ? 161 TYR   B CE1 1 
ATOM   1600 C CE2 . TYR   B 2 152 ? -8.263  1.133   -18.660 1.00 58.47  ? 161 TYR   B CE2 1 
ATOM   1601 C CZ  . TYR   B 2 152 ? -7.885  1.381   -17.346 1.00 60.75  ? 161 TYR   B CZ  1 
ATOM   1602 O OH  . TYR   B 2 152 ? -8.790  1.256   -16.328 1.00 61.96  ? 161 TYR   B OH  1 
ATOM   1603 N N   . VAL   B 2 153 ? -4.993  -1.529  -19.898 1.00 53.28  ? 162 VAL   B N   1 
ATOM   1604 C CA  . VAL   B 2 153 ? -5.878  -2.732  -19.922 1.00 52.02  ? 162 VAL   B CA  1 
ATOM   1605 C C   . VAL   B 2 153 ? -6.853  -2.652  -18.734 1.00 47.32  ? 162 VAL   B C   1 
ATOM   1606 O O   . VAL   B 2 153 ? -6.382  -2.503  -17.618 1.00 45.01  ? 162 VAL   B O   1 
ATOM   1607 C CB  . VAL   B 2 153 ? -5.032  -4.022  -19.886 1.00 47.45  ? 162 VAL   B CB  1 
ATOM   1608 C CG1 . VAL   B 2 153 ? -5.886  -5.282  -20.007 1.00 44.73  ? 162 VAL   B CG1 1 
ATOM   1609 C CG2 . VAL   B 2 153 ? -3.949  -3.993  -20.953 1.00 55.07  ? 162 VAL   B CG2 1 
ATOM   1610 N N   . SER   B 2 154 ? -8.157  -2.793  -18.981 1.00 49.72  ? 163 SER   B N   1 
ATOM   1611 C CA  . SER   B 2 154 ? -9.242  -2.708  -17.974 1.00 46.07  ? 163 SER   B CA  1 
ATOM   1612 C C   . SER   B 2 154 ? -9.738  -4.115  -17.662 1.00 43.74  ? 163 SER   B C   1 
ATOM   1613 O O   . SER   B 2 154 ? -9.939  -4.888  -18.582 1.00 40.58  ? 163 SER   B O   1 
ATOM   1614 C CB  . SER   B 2 154 ? -10.404 -1.830  -18.424 1.00 47.21  ? 163 SER   B CB  1 
ATOM   1615 O OG  . SER   B 2 154 ? -11.561 -1.979  -17.575 1.00 40.15  ? 163 SER   B OG  1 
ATOM   1616 N N   . ALA   B 2 155 ? -9.988  -4.383  -16.388 1.00 39.03  ? 164 ALA   B N   1 
ATOM   1617 C CA  . ALA   B 2 155 ? -10.820 -5.508  -15.950 1.00 35.88  ? 164 ALA   B CA  1 
ATOM   1618 C C   . ALA   B 2 155 ? -12.206 -5.373  -16.579 1.00 38.79  ? 164 ALA   B C   1 
ATOM   1619 O O   . ALA   B 2 155 ? -12.725 -4.228  -16.745 1.00 39.08  ? 164 ALA   B O   1 
ATOM   1620 C CB  . ALA   B 2 155 ? -10.904 -5.502  -14.439 1.00 40.94  ? 164 ALA   B CB  1 
ATOM   1621 N N   . ILE   B 2 156 ? -12.820 -6.513  -16.846 1.00 37.27  ? 165 ILE   B N   1 
ATOM   1622 C CA  . ILE   B 2 156 ? -14.299 -6.633  -16.877 1.00 37.17  ? 165 ILE   B CA  1 
ATOM   1623 C C   . ILE   B 2 156 ? -14.815 -6.726  -15.429 1.00 40.08  ? 165 ILE   B C   1 
ATOM   1624 O O   . ILE   B 2 156 ? -15.050 -7.855  -14.942 1.00 33.70  ? 165 ILE   B O   1 
ATOM   1625 C CB  . ILE   B 2 156 ? -14.721 -7.826  -17.744 1.00 37.14  ? 165 ILE   B CB  1 
ATOM   1626 C CG1 . ILE   B 2 156 ? -14.043 -7.766  -19.118 1.00 43.94  ? 165 ILE   B CG1 1 
ATOM   1627 C CG2 . ILE   B 2 156 ? -16.241 -7.853  -17.861 1.00 37.07  ? 165 ILE   B CG2 1 
ATOM   1628 C CD1 . ILE   B 2 156 ? -14.521 -8.827  -20.087 1.00 47.46  ? 165 ILE   B CD1 1 
ATOM   1629 N N   . THR   B 2 157 ? -15.026 -5.580  -14.760 1.00 43.12  ? 166 THR   B N   1 
ATOM   1630 C CA  . THR   B 2 157 ? -15.543 -5.501  -13.360 1.00 37.50  ? 166 THR   B CA  1 
ATOM   1631 C C   . THR   B 2 157 ? -17.056 -5.715  -13.320 1.00 37.37  ? 166 THR   B C   1 
ATOM   1632 O O   . THR   B 2 157 ? -17.777 -4.840  -13.808 1.00 41.44  ? 166 THR   B O   1 
ATOM   1633 C CB  . THR   B 2 157 ? -15.192 -4.170  -12.721 1.00 40.18  ? 166 THR   B CB  1 
ATOM   1634 O OG1 . THR   B 2 157 ? -13.784 -4.012  -12.883 1.00 39.89  ? 166 THR   B OG1 1 
ATOM   1635 C CG2 . THR   B 2 157 ? -15.588 -4.111  -11.265 1.00 41.06  ? 166 THR   B CG2 1 
ATOM   1636 N N   . GLN   B 2 158 ? -17.502 -6.851  -12.763 1.00 39.57  ? 167 GLN   B N   1 
ATOM   1637 C CA  . GLN   B 2 158 ? -18.924 -7.183  -12.498 1.00 37.50  ? 167 GLN   B CA  1 
ATOM   1638 C C   . GLN   B 2 158 ? -19.158 -7.283  -10.986 1.00 41.91  ? 167 GLN   B C   1 
ATOM   1639 O O   . GLN   B 2 158 ? -18.203 -7.557  -10.220 1.00 36.40  ? 167 GLN   B O   1 
ATOM   1640 C CB  . GLN   B 2 158 ? -19.310 -8.482  -13.195 1.00 36.40  ? 167 GLN   B CB  1 
ATOM   1641 C CG  . GLN   B 2 158 ? -20.797 -8.826  -13.102 1.00 39.44  ? 167 GLN   B CG  1 
ATOM   1642 C CD  . GLN   B 2 158 ? -21.713 -7.767  -13.689 1.00 43.45  ? 167 GLN   B CD  1 
ATOM   1643 O OE1 . GLN   B 2 158 ? -21.841 -6.646  -13.188 1.00 42.77  ? 167 GLN   B OE1 1 
ATOM   1644 N NE2 . GLN   B 2 158 ? -22.418 -8.125  -14.746 1.00 44.46  ? 167 GLN   B NE2 1 
ATOM   1645 N N   . GLY   B 2 159 ? -20.382 -6.986  -10.569 1.00 45.56  ? 168 GLY   B N   1 
ATOM   1646 C CA  . GLY   B 2 159 ? -20.808 -7.085  -9.171  1.00 52.25  ? 168 GLY   B CA  1 
ATOM   1647 C C   . GLY   B 2 159 ? -21.571 -8.361  -8.951  1.00 59.07  ? 168 GLY   B C   1 
ATOM   1648 O O   . GLY   B 2 159 ? -21.910 -9.046  -9.911  1.00 65.70  ? 168 GLY   B O   1 
ATOM   1649 N N   A LYS   B 2 160 ? -21.758 -8.723  -7.680  0.25 66.45  ? 169 LYS   B N   1 
ATOM   1650 N N   B LYS   B 2 160 ? -21.758 -8.723  -7.680  0.25 66.45  ? 169 LYS   B N   1 
ATOM   1651 N N   C LYS   B 2 160 ? -21.940 -8.598  -7.691  0.25 64.94  ? 169 LYS   B N   1 
ATOM   1652 N N   D LYS   B 2 160 ? -21.940 -8.598  -7.691  0.25 64.94  ? 169 LYS   B N   1 
ATOM   1653 C CA  A LYS   B 2 160 ? -22.598 -9.873  -7.256  0.25 69.49  ? 169 LYS   B CA  1 
ATOM   1654 C CA  B LYS   B 2 160 ? -22.598 -9.873  -7.256  0.25 69.49  ? 169 LYS   B CA  1 
ATOM   1655 C CA  C LYS   B 2 160 ? -22.563 -9.847  -7.176  0.25 68.23  ? 169 LYS   B CA  1 
ATOM   1656 C CA  D LYS   B 2 160 ? -22.563 -9.847  -7.176  0.25 68.23  ? 169 LYS   B CA  1 
ATOM   1657 C C   A LYS   B 2 160 ? -24.034 -9.373  -7.093  0.25 73.72  ? 169 LYS   B C   1 
ATOM   1658 C C   B LYS   B 2 160 ? -24.034 -9.373  -7.093  0.25 73.72  ? 169 LYS   B C   1 
ATOM   1659 C C   C LYS   B 2 160 ? -24.035 -9.556  -6.835  0.25 75.36  ? 169 LYS   B C   1 
ATOM   1660 C C   D LYS   B 2 160 ? -24.035 -9.556  -6.835  0.25 75.36  ? 169 LYS   B C   1 
ATOM   1661 O O   A LYS   B 2 160 ? -24.215 -8.235  -6.619  0.25 72.58  ? 169 LYS   B O   1 
ATOM   1662 O O   B LYS   B 2 160 ? -24.215 -8.235  -6.619  0.25 72.58  ? 169 LYS   B O   1 
ATOM   1663 O O   C LYS   B 2 160 ? -24.257 -8.757  -5.905  0.25 82.99  ? 169 LYS   B O   1 
ATOM   1664 O O   D LYS   B 2 160 ? -24.257 -8.757  -5.905  0.25 82.99  ? 169 LYS   B O   1 
ATOM   1665 C CB  A LYS   B 2 160 ? -22.096 -10.497 -5.950  0.25 70.18  ? 169 LYS   B CB  1 
ATOM   1666 C CB  B LYS   B 2 160 ? -22.096 -10.497 -5.950  0.25 70.18  ? 169 LYS   B CB  1 
ATOM   1667 C CB  C LYS   B 2 160 ? -21.749 -10.307 -5.956  0.25 66.21  ? 169 LYS   B CB  1 
ATOM   1668 C CB  D LYS   B 2 160 ? -21.749 -10.307 -5.956  0.25 66.21  ? 169 LYS   B CB  1 
ATOM   1669 C CG  A LYS   B 2 160 ? -22.774 -11.811 -5.587  0.25 68.78  ? 169 LYS   B CG  1 
ATOM   1670 C CG  B LYS   B 2 160 ? -22.774 -11.811 -5.587  0.25 68.78  ? 169 LYS   B CG  1 
ATOM   1671 C CG  C LYS   B 2 160 ? -20.254 -9.984  -6.005  0.25 61.02  ? 169 LYS   B CG  1 
ATOM   1672 C CG  D LYS   B 2 160 ? -20.254 -9.984  -6.005  0.25 61.02  ? 169 LYS   B CG  1 
ATOM   1673 C CD  A LYS   B 2 160 ? -22.761 -12.136 -4.113  0.25 67.33  ? 169 LYS   B CD  1 
ATOM   1674 C CD  B LYS   B 2 160 ? -22.761 -12.136 -4.113  0.25 67.33  ? 169 LYS   B CD  1 
ATOM   1675 C CD  C LYS   B 2 160 ? -19.401 -11.114 -6.539  0.25 57.03  ? 169 LYS   B CD  1 
ATOM   1676 C CD  D LYS   B 2 160 ? -19.401 -11.114 -6.539  0.25 57.03  ? 169 LYS   B CD  1 
ATOM   1677 C CE  A LYS   B 2 160 ? -23.621 -13.337 -3.789  0.25 64.49  ? 169 LYS   B CE  1 
ATOM   1678 C CE  B LYS   B 2 160 ? -23.621 -13.337 -3.789  0.25 64.49  ? 169 LYS   B CE  1 
ATOM   1679 C CE  C LYS   B 2 160 ? -17.915 -10.822 -6.498  0.25 54.22  ? 169 LYS   B CE  1 
ATOM   1680 C CE  D LYS   B 2 160 ? -17.915 -10.822 -6.498  0.25 54.22  ? 169 LYS   B CE  1 
ATOM   1681 N NZ  A LYS   B 2 160 ? -23.749 -13.538 -2.328  0.25 65.24  ? 169 LYS   B NZ  1 
ATOM   1682 N NZ  B LYS   B 2 160 ? -23.749 -13.538 -2.328  0.25 65.24  ? 169 LYS   B NZ  1 
ATOM   1683 N NZ  C LYS   B 2 160 ? -17.448 -10.130 -7.721  0.25 53.42  ? 169 LYS   B NZ  1 
ATOM   1684 N NZ  D LYS   B 2 160 ? -17.448 -10.130 -7.721  0.25 53.42  ? 169 LYS   B NZ  1 
ATOM   1685 N N   . ARG   B 2 161 ? -25.002 -10.174 -7.535  1.00 81.36  ? 170 ARG   B N   1 
ATOM   1686 C CA  . ARG   B 2 161 ? -26.461 -9.918  -7.304  1.00 87.54  ? 170 ARG   B CA  1 
ATOM   1687 C C   . ARG   B 2 161 ? -26.937 -10.796 -6.125  1.00 100.09 ? 170 ARG   B C   1 
ATOM   1688 O O   . ARG   B 2 161 ? -26.387 -11.910 -5.957  1.00 117.89 ? 170 ARG   B O   1 
ATOM   1689 C CB  . ARG   B 2 161 ? -27.247 -10.144 -8.606  1.00 89.81  ? 170 ARG   B CB  1 
ATOM   1690 C CG  . ARG   B 2 161 ? -28.702 -9.682  -8.569  1.00 85.44  ? 170 ARG   B CG  1 
ATOM   1691 C CD  . ARG   B 2 161 ? -29.488 -9.958  -9.851  1.00 81.31  ? 170 ARG   B CD  1 
ATOM   1692 N NE  . ARG   B 2 161 ? -30.919 -9.640  -9.758  1.00 77.56  ? 170 ARG   B NE  1 
ATOM   1693 C CZ  . ARG   B 2 161 ? -31.636 -8.903  -10.624 1.00 76.28  ? 170 ARG   B CZ  1 
ATOM   1694 N NH1 . ARG   B 2 161 ? -31.086 -8.360  -11.697 1.00 64.45  ? 170 ARG   B NH1 1 
ATOM   1695 N NH2 . ARG   B 2 161 ? -32.929 -8.704  -10.409 1.00 82.33  ? 170 ARG   B NH2 1 
ATOM   1696 N N   . GLU   B 2 162 ? -27.882 -10.307 -5.305  1.00 104.35 ? 171 GLU   B N   1 
ATOM   1697 C CA  . GLU   B 2 162 ? -28.456 -11.030 -4.126  1.00 105.76 ? 171 GLU   B CA  1 
ATOM   1698 C C   . GLU   B 2 162 ? -29.947 -11.299 -4.384  1.00 92.85  ? 171 GLU   B C   1 
ATOM   1699 O O   . GLU   B 2 162 ? -30.462 -12.418 -4.450  1.00 90.72  ? 171 GLU   B O   1 
ATOM   1700 C CB  . GLU   B 2 162 ? -28.268 -10.229 -2.827  1.00 107.77 ? 171 GLU   B CB  1 
ATOM   1701 C CG  . GLU   B 2 162 ? -26.814 -10.025 -2.395  1.00 106.57 ? 171 GLU   B CG  1 
ATOM   1702 C CD  . GLU   B 2 162 ? -26.239 -11.008 -1.376  1.00 109.46 ? 171 GLU   B CD  1 
ATOM   1703 O OE1 . GLU   B 2 162 ? -26.678 -10.971 -0.198  1.00 97.40  ? 171 GLU   B OE1 1 
ATOM   1704 O OE2 . GLU   B 2 162 ? -25.334 -11.797 -1.752  1.00 90.69  ? 171 GLU   B OE2 1 
HETATM 1705 S S   A DMS   C 3 .   ? -7.743  5.715   -17.693 0.19 111.67 ? 201 DMS   B S   1 
HETATM 1706 S S   B DMS   C 3 .   ? -7.743  5.718   -17.693 0.23 111.71 ? 201 DMS   B S   1 
HETATM 1707 O O   A DMS   C 3 .   ? -6.422  4.996   -17.656 0.19 114.46 ? 201 DMS   B O   1 
HETATM 1708 O O   B DMS   C 3 .   ? -6.420  5.002   -17.656 0.23 114.76 ? 201 DMS   B O   1 
HETATM 1709 C C1  A DMS   C 3 .   ? -8.512  5.411   -16.123 0.19 110.69 ? 201 DMS   B C1  1 
HETATM 1710 C C1  B DMS   C 3 .   ? -8.512  5.412   -16.123 0.23 110.58 ? 201 DMS   B C1  1 
HETATM 1711 C C2  A DMS   C 3 .   ? -8.826  4.717   -18.685 0.19 111.06 ? 201 DMS   B C2  1 
HETATM 1712 C C2  B DMS   C 3 .   ? -8.825  4.717   -18.685 0.23 111.01 ? 201 DMS   B C2  1 
HETATM 1713 S S   A DMS   D 3 .   ? -18.290 11.878  -0.485  0.19 375.75 ? 202 DMS   B S   1 
HETATM 1714 S S   B DMS   D 3 .   ? -18.291 11.875  -0.489  0.23 377.12 ? 202 DMS   B S   1 
HETATM 1715 O O   A DMS   D 3 .   ? -19.026 10.620  -0.851  0.19 378.54 ? 202 DMS   B O   1 
HETATM 1716 O O   B DMS   D 3 .   ? -19.028 10.619  -0.859  0.23 379.79 ? 202 DMS   B O   1 
HETATM 1717 C C1  A DMS   D 3 .   ? -19.451 13.201  -0.701  0.19 373.12 ? 202 DMS   B C1  1 
HETATM 1718 C C1  B DMS   D 3 .   ? -19.451 13.200  -0.702  0.23 374.04 ? 202 DMS   B C1  1 
HETATM 1719 C C2  A DMS   D 3 .   ? -17.237 12.254  -1.863  0.19 369.79 ? 202 DMS   B C2  1 
HETATM 1720 C C2  B DMS   D 3 .   ? -17.237 12.254  -1.864  0.23 370.41 ? 202 DMS   B C2  1 
HETATM 1721 S S   A DMS   E 3 .   ? -7.752  3.264   -13.552 0.19 150.21 ? 203 DMS   B S   1 
HETATM 1722 S S   B DMS   E 3 .   ? -7.751  3.268   -13.553 0.23 150.51 ? 203 DMS   B S   1 
HETATM 1723 O O   A DMS   E 3 .   ? -7.386  1.839   -13.851 0.19 149.75 ? 203 DMS   B O   1 
HETATM 1724 O O   B DMS   E 3 .   ? -7.386  1.843   -13.856 0.23 149.93 ? 203 DMS   B O   1 
HETATM 1725 C C1  A DMS   E 3 .   ? -8.672  3.223   -12.036 0.19 148.46 ? 203 DMS   B C1  1 
HETATM 1726 C C1  B DMS   E 3 .   ? -8.671  3.224   -12.038 0.23 148.53 ? 203 DMS   B C1  1 
HETATM 1727 C C2  A DMS   E 3 .   ? -6.279  4.028   -12.927 0.19 148.96 ? 203 DMS   B C2  1 
HETATM 1728 C C2  B DMS   E 3 .   ? -6.277  4.029   -12.926 0.23 149.01 ? 203 DMS   B C2  1 
HETATM 1729 N N1  C A1BXS F 4 .   ? -8.263  3.790   -12.225 0.29 39.59  ? 204 A1BXS B N1  1 
HETATM 1730 N N1  D A1BXS F 4 .   ? -8.263  3.790   -12.225 0.29 39.59  ? 204 A1BXS B N1  1 
HETATM 1731 N N3  C A1BXS F 4 .   ? -6.345  5.408   -15.942 0.29 44.41  ? 204 A1BXS B N3  1 
HETATM 1732 N N3  D A1BXS F 4 .   ? -6.345  5.408   -15.942 0.29 44.41  ? 204 A1BXS B N3  1 
HETATM 1733 C C4  C A1BXS F 4 .   ? -6.302  5.196   -18.747 0.29 45.56  ? 204 A1BXS B C4  1 
HETATM 1734 C C4  D A1BXS F 4 .   ? -6.302  5.196   -18.747 0.29 45.56  ? 204 A1BXS B C4  1 
HETATM 1735 C C5  C A1BXS F 4 .   ? -6.255  5.088   -20.252 0.29 46.44  ? 204 A1BXS B C5  1 
HETATM 1736 C C5  D A1BXS F 4 .   ? -6.255  5.088   -20.252 0.29 46.44  ? 204 A1BXS B C5  1 
HETATM 1737 C C6  C A1BXS F 4 .   ? -7.508  4.919   -18.032 0.29 44.10  ? 204 A1BXS B C6  1 
HETATM 1738 C C6  D A1BXS F 4 .   ? -7.508  4.919   -18.032 0.29 44.10  ? 204 A1BXS B C6  1 
HETATM 1739 C C7  C A1BXS F 4 .   ? -8.712  4.524   -18.669 0.29 42.61  ? 204 A1BXS B C7  1 
HETATM 1740 C C7  D A1BXS F 4 .   ? -8.712  4.524   -18.669 0.29 42.61  ? 204 A1BXS B C7  1 
HETATM 1741 C C8  C A1BXS F 4 .   ? -9.832  4.269   -17.941 0.29 41.40  ? 204 A1BXS B C8  1 
HETATM 1742 C C8  D A1BXS F 4 .   ? -9.832  4.269   -17.941 0.29 41.40  ? 204 A1BXS B C8  1 
HETATM 1743 C C10 C A1BXS F 4 .   ? -8.666  4.766   -15.868 0.29 40.54  ? 204 A1BXS B C10 1 
HETATM 1744 C C10 D A1BXS F 4 .   ? -8.666  4.766   -15.868 0.29 40.54  ? 204 A1BXS B C10 1 
HETATM 1745 C C13 C A1BXS F 4 .   ? -8.242  5.045   -11.452 0.29 37.04  ? 204 A1BXS B C13 1 
HETATM 1746 C C13 D A1BXS F 4 .   ? -8.242  5.045   -11.452 0.29 37.04  ? 204 A1BXS B C13 1 
HETATM 1747 C C15 C A1BXS F 4 .   ? -8.067  3.196   -9.932  0.29 38.05  ? 204 A1BXS B C15 1 
HETATM 1748 C C15 D A1BXS F 4 .   ? -8.067  3.196   -9.932  0.29 38.05  ? 204 A1BXS B C15 1 
HETATM 1749 C C17 C A1BXS F 4 .   ? -8.209  2.614   -11.341 0.29 39.02  ? 204 A1BXS B C17 1 
HETATM 1750 C C17 D A1BXS F 4 .   ? -8.209  2.614   -11.341 0.29 39.02  ? 204 A1BXS B C17 1 
HETATM 1751 C C1  C A1BXS F 4 .   ? -4.022  6.072   -15.866 0.29 45.96  ? 204 A1BXS B C1  1 
HETATM 1752 C C1  D A1BXS F 4 .   ? -4.022  6.072   -15.866 0.29 45.96  ? 204 A1BXS B C1  1 
HETATM 1753 C C2  C A1BXS F 4 .   ? -5.243  5.660   -16.633 0.29 45.29  ? 204 A1BXS B C2  1 
HETATM 1754 C C2  D A1BXS F 4 .   ? -5.243  5.660   -16.633 0.29 45.29  ? 204 A1BXS B C2  1 
HETATM 1755 C C3  C A1BXS F 4 .   ? -5.190  5.562   -18.036 0.29 45.40  ? 204 A1BXS B C3  1 
HETATM 1756 C C3  D A1BXS F 4 .   ? -5.190  5.562   -18.036 0.29 45.40  ? 204 A1BXS B C3  1 
HETATM 1757 O O1  C A1BXS F 4 .   ? -5.119  5.731   -20.825 0.29 47.66  ? 204 A1BXS B O1  1 
HETATM 1758 O O1  D A1BXS F 4 .   ? -5.119  5.731   -20.825 0.29 47.66  ? 204 A1BXS B O1  1 
HETATM 1759 C C9  C A1BXS F 4 .   ? -9.801  4.389   -16.536 0.29 40.43  ? 204 A1BXS B C9  1 
HETATM 1760 C C9  D A1BXS F 4 .   ? -9.801  4.389   -16.536 0.29 40.43  ? 204 A1BXS B C9  1 
HETATM 1761 C C11 C A1BXS F 4 .   ? -8.696  4.916   -14.362 0.29 39.21  ? 204 A1BXS B C11 1 
HETATM 1762 C C11 D A1BXS F 4 .   ? -8.696  4.916   -14.362 0.29 39.21  ? 204 A1BXS B C11 1 
HETATM 1763 C C12 C A1BXS F 4 .   ? -8.327  3.680   -13.568 0.29 37.59  ? 204 A1BXS B C12 1 
HETATM 1764 C C12 D A1BXS F 4 .   ? -8.327  3.680   -13.568 0.29 37.59  ? 204 A1BXS B C12 1 
HETATM 1765 O O2  C A1BXS F 4 .   ? -8.079  2.620   -14.109 0.29 38.31  ? 204 A1BXS B O2  1 
HETATM 1766 O O2  D A1BXS F 4 .   ? -8.079  2.620   -14.109 0.29 38.31  ? 204 A1BXS B O2  1 
HETATM 1767 C C14 C A1BXS F 4 .   ? -8.634  4.611   -10.065 0.29 37.88  ? 204 A1BXS B C14 1 
HETATM 1768 C C14 D A1BXS F 4 .   ? -8.634  4.611   -10.065 0.29 37.88  ? 204 A1BXS B C14 1 
HETATM 1769 C C16 C A1BXS F 4 .   ? -8.748  2.361   -8.851  0.29 39.58  ? 204 A1BXS B C16 1 
HETATM 1770 C C16 D A1BXS F 4 .   ? -8.748  2.361   -8.851  0.29 39.58  ? 204 A1BXS B C16 1 
HETATM 1771 N N2  C A1BXS F 4 .   ? -10.082 1.876   -9.197  0.29 41.22  ? 204 A1BXS B N2  1 
HETATM 1772 N N2  D A1BXS F 4 .   ? -10.082 1.876   -9.197  0.29 41.22  ? 204 A1BXS B N2  1 
HETATM 1773 C C18 C A1BXS F 4 .   ? -7.483  5.041   -16.612 0.29 43.06  ? 204 A1BXS B C18 1 
HETATM 1774 C C18 D A1BXS F 4 .   ? -7.483  5.041   -16.612 0.29 43.06  ? 204 A1BXS B C18 1 
HETATM 1775 S S   C SO4   G 5 .   ? -18.729 11.824  -0.440  0.50 101.19 ? 205 SO4   B S   1 
HETATM 1776 S S   D SO4   G 5 .   ? -18.729 11.824  -0.440  0.50 101.19 ? 205 SO4   B S   1 
HETATM 1777 O O1  C SO4   G 5 .   ? -17.590 12.065  -1.294  0.50 96.18  ? 205 SO4   B O1  1 
HETATM 1778 O O1  D SO4   G 5 .   ? -17.590 12.065  -1.294  0.50 96.18  ? 205 SO4   B O1  1 
HETATM 1779 O O2  C SO4   G 5 .   ? -18.367 12.065  0.928   0.50 105.47 ? 205 SO4   B O2  1 
HETATM 1780 O O2  D SO4   G 5 .   ? -18.367 12.065  0.928   0.50 105.47 ? 205 SO4   B O2  1 
HETATM 1781 O O3  C SO4   G 5 .   ? -19.799 12.710  -0.809  0.50 106.56 ? 205 SO4   B O3  1 
HETATM 1782 O O3  D SO4   G 5 .   ? -19.799 12.710  -0.809  0.50 106.56 ? 205 SO4   B O3  1 
HETATM 1783 O O4  C SO4   G 5 .   ? -19.167 10.458  -0.579  0.50 103.44 ? 205 SO4   B O4  1 
HETATM 1784 O O4  D SO4   G 5 .   ? -19.167 10.458  -0.579  0.50 103.44 ? 205 SO4   B O4  1 
HETATM 1785 S S   C DMS   H 3 .   ? -23.423 -7.589  -4.349  0.50 120.06 ? 206 DMS   B S   1 
HETATM 1786 S S   D DMS   H 3 .   ? -23.423 -7.589  -4.349  0.50 120.06 ? 206 DMS   B S   1 
HETATM 1787 O O   C DMS   H 3 .   ? -22.283 -6.929  -5.092  0.50 110.07 ? 206 DMS   B O   1 
HETATM 1788 O O   D DMS   H 3 .   ? -22.283 -6.929  -5.092  0.50 110.07 ? 206 DMS   B O   1 
HETATM 1789 C C1  C DMS   H 3 .   ? -24.697 -6.361  -4.183  0.50 115.95 ? 206 DMS   B C1  1 
HETATM 1790 C C1  D DMS   H 3 .   ? -24.697 -6.361  -4.183  0.50 115.95 ? 206 DMS   B C1  1 
HETATM 1791 C C2  C DMS   H 3 .   ? -22.946 -7.658  -2.640  0.50 118.16 ? 206 DMS   B C2  1 
HETATM 1792 C C2  D DMS   H 3 .   ? -22.946 -7.658  -2.640  0.50 118.16 ? 206 DMS   B C2  1 
HETATM 1793 S S   C SO4   I 5 .   ? -7.363  11.431  -19.161 0.29 81.30  ? 207 SO4   B S   1 
HETATM 1794 S S   D SO4   I 5 .   ? -7.363  11.431  -19.161 0.29 81.30  ? 207 SO4   B S   1 
HETATM 1795 O O1  C SO4   I 5 .   ? -8.097  12.353  -19.985 0.29 77.49  ? 207 SO4   B O1  1 
HETATM 1796 O O1  D SO4   I 5 .   ? -8.097  12.353  -19.985 0.29 77.49  ? 207 SO4   B O1  1 
HETATM 1797 O O2  C SO4   I 5 .   ? -5.951  11.619  -19.371 0.29 83.43  ? 207 SO4   B O2  1 
HETATM 1798 O O2  D SO4   I 5 .   ? -5.951  11.619  -19.371 0.29 83.43  ? 207 SO4   B O2  1 
HETATM 1799 O O3  C SO4   I 5 .   ? -7.676  11.675  -17.776 0.29 81.09  ? 207 SO4   B O3  1 
HETATM 1800 O O3  D SO4   I 5 .   ? -7.676  11.675  -17.776 0.29 81.09  ? 207 SO4   B O3  1 
HETATM 1801 O O4  C SO4   I 5 .   ? -7.720  10.084  -19.513 0.29 74.22  ? 207 SO4   B O4  1 
HETATM 1802 O O4  D SO4   I 5 .   ? -7.720  10.084  -19.513 0.29 74.22  ? 207 SO4   B O4  1 
HETATM 1803 O O   A HOH   J 6 .   ? -8.171  0.398   3.720   0.50 62.24  ? 101 HOH   A O   1 
HETATM 1804 O O   B HOH   J 6 .   ? -8.171  0.398   3.720   0.50 62.24  ? 101 HOH   A O   1 
HETATM 1805 O O   . HOH   J 6 .   ? -24.240 9.276   -27.371 1.00 49.44  ? 102 HOH   A O   1 
HETATM 1806 O O   . HOH   J 6 .   ? -28.302 -5.973  -28.039 1.00 66.53  ? 103 HOH   A O   1 
HETATM 1807 O O   C HOH   J 6 .   ? -25.416 12.464  -23.644 0.50 45.00  ? 104 HOH   A O   1 
HETATM 1808 O O   D HOH   J 6 .   ? -25.416 12.464  -23.644 0.50 45.00  ? 104 HOH   A O   1 
HETATM 1809 O O   A HOH   J 6 .   ? -23.828 18.870  -19.542 0.50 68.15  ? 105 HOH   A O   1 
HETATM 1810 O O   B HOH   J 6 .   ? -23.828 18.870  -19.542 0.50 68.15  ? 105 HOH   A O   1 
HETATM 1811 O O   . HOH   J 6 .   ? -9.439  -6.822  -25.529 1.00 55.63  ? 106 HOH   A O   1 
HETATM 1812 O O   . HOH   J 6 .   ? -3.827  -3.675  0.088   1.00 67.06  ? 107 HOH   A O   1 
HETATM 1813 O O   . HOH   J 6 .   ? -4.060  -0.707  -0.459  1.00 53.81  ? 108 HOH   A O   1 
HETATM 1814 O O   . HOH   J 6 .   ? -2.188  -3.588  -6.442  1.00 57.08  ? 109 HOH   A O   1 
HETATM 1815 O O   A HOH   J 6 .   ? -29.488 15.453  -15.009 0.50 97.72  ? 110 HOH   A O   1 
HETATM 1816 O O   B HOH   J 6 .   ? -29.488 15.453  -15.009 0.50 97.72  ? 110 HOH   A O   1 
HETATM 1817 O O   . HOH   J 6 .   ? -30.796 12.655  -16.266 1.00 52.75  ? 111 HOH   A O   1 
HETATM 1818 O O   . HOH   J 6 .   ? -6.974  -9.079  -3.126  1.00 41.94  ? 112 HOH   A O   1 
HETATM 1819 O O   A HOH   J 6 .   ? -8.933  2.225   -8.656  0.19 31.94  ? 113 HOH   A O   1 
HETATM 1820 O O   B HOH   J 6 .   ? -8.937  2.223   -8.654  0.23 31.91  ? 113 HOH   A O   1 
HETATM 1821 O O   . HOH   J 6 .   ? -4.396  -14.722 -25.392 1.00 43.42  ? 114 HOH   A O   1 
HETATM 1822 O O   . HOH   J 6 .   ? -22.741 -9.594  -34.505 1.00 52.45  ? 115 HOH   A O   1 
HETATM 1823 O O   . HOH   J 6 .   ? -30.780 0.430   -22.943 1.00 44.98  ? 116 HOH   A O   1 
HETATM 1824 O O   C HOH   J 6 .   ? -26.685 6.794   -28.586 0.50 47.45  ? 117 HOH   A O   1 
HETATM 1825 O O   D HOH   J 6 .   ? -26.685 6.794   -28.586 0.50 47.45  ? 117 HOH   A O   1 
HETATM 1826 O O   . HOH   J 6 .   ? -4.834  -10.153 -5.761  1.00 54.34  ? 118 HOH   A O   1 
HETATM 1827 O O   A HOH   J 6 .   ? -26.794 -3.625  -35.203 0.50 71.24  ? 119 HOH   A O   1 
HETATM 1828 O O   B HOH   J 6 .   ? -26.794 -3.625  -35.203 0.50 71.24  ? 119 HOH   A O   1 
HETATM 1829 O O   A HOH   J 6 .   ? -31.835 -0.758  -29.376 0.50 61.38  ? 120 HOH   A O   1 
HETATM 1830 O O   B HOH   J 6 .   ? -31.835 -0.758  -29.376 0.50 61.38  ? 120 HOH   A O   1 
HETATM 1831 O O   . HOH   J 6 .   ? -4.601  2.385   -10.208 1.00 55.56  ? 121 HOH   A O   1 
HETATM 1832 O O   . HOH   J 6 .   ? -2.657  -9.350  -3.276  1.00 60.45  ? 122 HOH   A O   1 
HETATM 1833 O O   A HOH   J 6 .   ? -7.907  4.654   -9.432  0.19 83.79  ? 123 HOH   A O   1 
HETATM 1834 O O   B HOH   J 6 .   ? -7.924  4.651   -9.441  0.23 83.70  ? 123 HOH   A O   1 
HETATM 1835 O O   . HOH   K 6 .   ? -25.814 -8.111  -16.793 1.00 40.30  ? 301 HOH   B O   1 
HETATM 1836 O O   . HOH   K 6 .   ? -31.078 12.778  -19.404 1.00 40.94  ? 302 HOH   B O   1 
HETATM 1837 O O   . HOH   K 6 .   ? -17.563 12.812  -5.734  1.00 47.63  ? 303 HOH   B O   1 
HETATM 1838 O O   . HOH   K 6 .   ? -33.843 1.540   -15.180 1.00 57.42  ? 304 HOH   B O   1 
HETATM 1839 O O   A HOH   K 6 .   ? -19.649 -12.405 -25.876 0.50 55.40  ? 305 HOH   B O   1 
HETATM 1840 O O   B HOH   K 6 .   ? -19.649 -12.405 -25.876 0.50 55.40  ? 305 HOH   B O   1 
HETATM 1841 O O   A HOH   K 6 .   ? -15.768 -10.087 -15.411 0.50 57.26  ? 306 HOH   B O   1 
HETATM 1842 O O   B HOH   K 6 .   ? -15.768 -10.087 -15.411 0.50 57.26  ? 306 HOH   B O   1 
HETATM 1843 O O   . HOH   K 6 .   ? -16.494 -14.572 -16.764 1.00 47.79  ? 307 HOH   B O   1 
HETATM 1844 O O   A HOH   K 6 .   ? -35.744 -1.723  -16.687 0.50 66.87  ? 308 HOH   B O   1 
HETATM 1845 O O   B HOH   K 6 .   ? -35.744 -1.723  -16.687 0.50 66.87  ? 308 HOH   B O   1 
HETATM 1846 O O   . HOH   K 6 .   ? -15.198 -6.792  -1.811  1.00 54.85  ? 309 HOH   B O   1 
HETATM 1847 O O   . HOH   K 6 .   ? -12.535 -3.536  -9.992  1.00 45.04  ? 310 HOH   B O   1 
HETATM 1848 O O   A HOH   K 6 .   ? -27.689 -7.179  -5.661  0.50 78.26  ? 311 HOH   B O   1 
HETATM 1849 O O   B HOH   K 6 .   ? -27.689 -7.179  -5.661  0.50 78.26  ? 311 HOH   B O   1 
HETATM 1850 O O   C HOH   K 6 .   ? -16.241 26.175  -12.527 0.50 64.57  ? 312 HOH   B O   1 
HETATM 1851 O O   D HOH   K 6 .   ? -16.241 26.175  -12.527 0.50 64.57  ? 312 HOH   B O   1 
HETATM 1852 O O   A HOH   K 6 .   ? -0.950  0.304   -13.920 0.50 66.67  ? 313 HOH   B O   1 
HETATM 1853 O O   B HOH   K 6 .   ? -0.950  0.304   -13.920 0.50 66.67  ? 313 HOH   B O   1 
HETATM 1854 O O   . HOH   K 6 .   ? -18.261 -20.754 -21.674 1.00 61.11  ? 314 HOH   B O   1 
HETATM 1855 O O   A HOH   K 6 .   ? -28.923 -4.611  -21.754 0.50 71.27  ? 315 HOH   B O   1 
HETATM 1856 O O   B HOH   K 6 .   ? -28.923 -4.611  -21.754 0.50 71.27  ? 315 HOH   B O   1 
HETATM 1857 O O   A HOH   K 6 .   ? -11.811 1.719   -6.002  0.19 35.31  ? 316 HOH   B O   1 
HETATM 1858 O O   B HOH   K 6 .   ? -11.811 1.744   -5.979  0.23 35.50  ? 316 HOH   B O   1 
HETATM 1859 O O   A HOH   K 6 .   ? -21.905 -13.610 -21.587 0.50 57.14  ? 317 HOH   B O   1 
HETATM 1860 O O   B HOH   K 6 .   ? -21.905 -13.610 -21.587 0.50 57.14  ? 317 HOH   B O   1 
HETATM 1861 O O   A HOH   K 6 .   ? -21.176 6.340   -32.653 0.50 82.29  ? 318 HOH   B O   1 
HETATM 1862 O O   B HOH   K 6 .   ? -21.176 6.340   -32.653 0.50 82.29  ? 318 HOH   B O   1 
HETATM 1863 O O   A HOH   K 6 .   ? -22.245 7.505   -34.501 0.50 87.41  ? 319 HOH   B O   1 
HETATM 1864 O O   B HOH   K 6 .   ? -22.245 7.505   -34.501 0.50 87.41  ? 319 HOH   B O   1 
HETATM 1865 O O   . HOH   K 6 .   ? -6.594  -0.525  -10.965 1.00 40.22  ? 320 HOH   B O   1 
HETATM 1866 O O   . HOH   K 6 .   ? -15.566 9.447   -0.851  1.00 57.58  ? 321 HOH   B O   1 
HETATM 1867 O O   A HOH   K 6 .   ? -23.831 -14.636 -17.832 0.50 68.94  ? 322 HOH   B O   1 
HETATM 1868 O O   B HOH   K 6 .   ? -23.831 -14.636 -17.832 0.50 68.94  ? 322 HOH   B O   1 
HETATM 1869 O O   . HOH   K 6 .   ? -16.331 -7.329  -8.293  1.00 51.68  ? 323 HOH   B O   1 
HETATM 1870 O O   . HOH   K 6 .   ? -35.562 4.069   -9.114  1.00 53.93  ? 324 HOH   B O   1 
HETATM 1871 O O   A HOH   K 6 .   ? -11.068 11.723  -19.385 0.50 64.37  ? 325 HOH   B O   1 
HETATM 1872 O O   B HOH   K 6 .   ? -11.068 11.723  -19.385 0.50 64.37  ? 325 HOH   B O   1 
HETATM 1873 O O   . HOH   K 6 .   ? -6.966  -11.040 -5.071  1.00 46.01  ? 326 HOH   B O   1 
HETATM 1874 O O   . HOH   K 6 .   ? -13.322 -2.115  -14.770 1.00 41.14  ? 327 HOH   B O   1 
HETATM 1875 O O   A HOH   K 6 .   ? -21.745 -12.228 -13.322 0.50 53.24  ? 328 HOH   B O   1 
HETATM 1876 O O   B HOH   K 6 .   ? -21.745 -12.228 -13.322 0.50 53.24  ? 328 HOH   B O   1 
HETATM 1877 O O   C HOH   K 6 .   ? -20.305 13.816  1.719   0.50 53.61  ? 329 HOH   B O   1 
HETATM 1878 O O   D HOH   K 6 .   ? -20.305 13.816  1.719   0.50 53.61  ? 329 HOH   B O   1 
HETATM 1879 O O   A HOH   K 6 .   ? -19.978 -7.804  -2.893  0.50 69.74  ? 330 HOH   B O   1 
HETATM 1880 O O   B HOH   K 6 .   ? -19.978 -7.804  -2.893  0.50 69.74  ? 330 HOH   B O   1 
HETATM 1881 O O   . HOH   K 6 .   ? -16.637 20.787  -14.168 1.00 55.84  ? 331 HOH   B O   1 
HETATM 1882 O O   . HOH   K 6 .   ? -18.153 -10.798 -16.517 1.00 39.20  ? 332 HOH   B O   1 
HETATM 1883 O O   A HOH   K 6 .   ? -17.200 15.108  -30.682 0.50 59.44  ? 333 HOH   B O   1 
HETATM 1884 O O   B HOH   K 6 .   ? -17.200 15.108  -30.682 0.50 59.44  ? 333 HOH   B O   1 
HETATM 1885 O O   . HOH   K 6 .   ? -28.018 -6.094  -18.869 1.00 50.75  ? 334 HOH   B O   1 
HETATM 1886 O O   . HOH   K 6 .   ? -35.662 -5.442  -10.294 1.00 51.83  ? 335 HOH   B O   1 
HETATM 1887 O O   A HOH   K 6 .   ? -15.125 16.412  -19.932 0.50 83.78  ? 336 HOH   B O   1 
HETATM 1888 O O   B HOH   K 6 .   ? -15.125 16.412  -19.932 0.50 83.78  ? 336 HOH   B O   1 
HETATM 1889 O O   . HOH   K 6 .   ? -16.344 -13.838 -30.929 1.00 58.38  ? 337 HOH   B O   1 
HETATM 1890 O O   C HOH   K 6 .   ? -22.035 15.070  -6.157  0.50 53.96  ? 338 HOH   B O   1 
HETATM 1891 O O   D HOH   K 6 .   ? -22.035 15.070  -6.157  0.50 53.96  ? 338 HOH   B O   1 
HETATM 1892 O O   . HOH   K 6 .   ? -31.842 7.075   -4.503  1.00 64.98  ? 339 HOH   B O   1 
HETATM 1893 O O   A HOH   K 6 .   ? -7.558  -6.191  0.712   0.50 67.13  ? 340 HOH   B O   1 
HETATM 1894 O O   B HOH   K 6 .   ? -7.558  -6.191  0.712   0.50 67.13  ? 340 HOH   B O   1 
HETATM 1895 O O   . HOH   K 6 .   ? -2.942  -12.003 -6.895  1.00 51.92  ? 341 HOH   B O   1 
HETATM 1896 O O   . HOH   K 6 .   ? -14.620 -12.211 -16.471 1.00 47.11  ? 342 HOH   B O   1 
HETATM 1897 O O   . HOH   K 6 .   ? -19.359 -5.710  -0.888  1.00 37.69  ? 343 HOH   B O   1 
HETATM 1898 O O   A HOH   K 6 .   ? -8.551  -11.107 -7.056  0.50 63.85  ? 344 HOH   B O   1 
HETATM 1899 O O   B HOH   K 6 .   ? -8.551  -11.107 -7.056  0.50 63.85  ? 344 HOH   B O   1 
HETATM 1900 O O   A HOH   K 6 .   ? -11.760 -17.486 -27.800 0.50 82.88  ? 345 HOH   B O   1 
HETATM 1901 O O   B HOH   K 6 .   ? -11.760 -17.486 -27.800 0.50 82.88  ? 345 HOH   B O   1 
HETATM 1902 O O   A HOH   K 6 .   ? -21.290 7.109   0.000   0.19 50.46  ? 346 HOH   B O   1 
HETATM 1903 O O   B HOH   K 6 .   ? -21.290 7.111   0.000   0.23 50.45  ? 346 HOH   B O   1 
HETATM 1904 O O   A HOH   K 6 .   ? -29.303 -1.854  -18.994 0.50 66.64  ? 347 HOH   B O   1 
HETATM 1905 O O   B HOH   K 6 .   ? -29.303 -1.854  -18.994 0.50 66.64  ? 347 HOH   B O   1 
HETATM 1906 O O   A HOH   K 6 .   ? -20.394 24.530  -16.832 0.50 85.50  ? 348 HOH   B O   1 
HETATM 1907 O O   B HOH   K 6 .   ? -20.394 24.530  -16.832 0.50 85.50  ? 348 HOH   B O   1 
HETATM 1908 O O   . HOH   K 6 .   ? -15.238 -4.725  1.223   1.00 50.67  ? 349 HOH   B O   1 
HETATM 1909 O O   A HOH   K 6 .   ? -19.379 24.983  -14.704 0.50 80.21  ? 350 HOH   B O   1 
HETATM 1910 O O   B HOH   K 6 .   ? -19.379 24.983  -14.704 0.50 80.21  ? 350 HOH   B O   1 
HETATM 1911 O O   C HOH   K 6 .   ? -5.293  4.796   -13.193 0.29 44.90  ? 351 HOH   B O   1 
HETATM 1912 O O   D HOH   K 6 .   ? -5.293  4.796   -13.193 0.29 44.90  ? 351 HOH   B O   1 
HETATM 1913 O O   . HOH   K 6 .   ? -30.816 4.562   -2.507  1.00 60.09  ? 352 HOH   B O   1 
HETATM 1914 O O   . HOH   K 6 .   ? -19.075 15.035  -22.280 1.00 55.86  ? 353 HOH   B O   1 
HETATM 1915 O O   . HOH   K 6 .   ? -11.694 -5.242  -8.193  1.00 47.25  ? 354 HOH   B O   1 
HETATM 1916 O O   A HOH   K 6 .   ? -16.813 15.931  -21.822 0.50 67.56  ? 355 HOH   B O   1 
HETATM 1917 O O   B HOH   K 6 .   ? -16.813 15.931  -21.822 0.50 67.56  ? 355 HOH   B O   1 
HETATM 1918 O O   A HOH   K 6 .   ? -19.779 -13.371 -23.044 0.50 49.82  ? 356 HOH   B O   1 
HETATM 1919 O O   B HOH   K 6 .   ? -19.779 -13.371 -23.044 0.50 49.82  ? 356 HOH   B O   1 
HETATM 1920 O O   . HOH   K 6 .   ? -34.970 0.308   -7.146  1.00 56.32  ? 357 HOH   B O   1 
HETATM 1921 O O   . HOH   K 6 .   ? -10.551 7.868   -13.711 1.00 43.11  ? 358 HOH   B O   1 
HETATM 1922 O O   A HOH   K 6 .   ? -26.000 -5.297  -3.863  0.50 44.41  ? 359 HOH   B O   1 
HETATM 1923 O O   B HOH   K 6 .   ? -26.000 -5.297  -3.863  0.50 44.41  ? 359 HOH   B O   1 
HETATM 1924 O O   A HOH   K 6 .   ? -17.293 26.823  -14.512 0.50 75.79  ? 360 HOH   B O   1 
HETATM 1925 O O   B HOH   K 6 .   ? -17.293 26.823  -14.512 0.50 75.79  ? 360 HOH   B O   1 
HETATM 1926 O O   C HOH   K 6 .   ? -10.042 -16.164 -24.288 0.50 58.68  ? 361 HOH   B O   1 
HETATM 1927 O O   D HOH   K 6 .   ? -10.042 -16.164 -24.288 0.50 58.68  ? 361 HOH   B O   1 
HETATM 1928 O O   A HOH   K 6 .   ? -24.195 -8.536  -1.658  0.50 90.17  ? 362 HOH   B O   1 
HETATM 1929 O O   B HOH   K 6 .   ? -24.195 -8.536  -1.658  0.50 90.17  ? 362 HOH   B O   1 
HETATM 1930 O O   C HOH   K 6 .   ? -5.490  8.982   -16.778 0.29 39.53  ? 363 HOH   B O   1 
HETATM 1931 O O   D HOH   K 6 .   ? -5.490  8.982   -16.778 0.29 39.53  ? 363 HOH   B O   1 
HETATM 1932 O O   . HOH   K 6 .   ? -1.206  -14.882 -10.099 1.00 55.89  ? 364 HOH   B O   1 
HETATM 1933 O O   A HOH   K 6 .   ? -31.601 -10.980 -27.046 0.25 64.76  ? 365 HOH   B O   1 
HETATM 1934 O O   B HOH   K 6 .   ? -31.601 -10.980 -27.046 0.25 64.76  ? 365 HOH   B O   1 
HETATM 1935 O O   A HOH   K 6 .   ? -11.332 4.079   -5.949  0.19 12.32  ? 366 HOH   B O   1 
HETATM 1936 O O   B HOH   K 6 .   ? -11.954 4.803   -5.222  0.23 26.35  ? 366 HOH   B O   1 
HETATM 1937 O O   A HOH   K 6 .   ? -30.867 -7.642  -6.251  0.50 65.81  ? 367 HOH   B O   1 
HETATM 1938 O O   B HOH   K 6 .   ? -30.867 -7.642  -6.251  0.50 65.81  ? 367 HOH   B O   1 
HETATM 1939 O O   A HOH   K 6 .   ? -20.195 4.700   -0.558  0.19 25.27  ? 368 HOH   B O   1 
HETATM 1940 O O   B HOH   K 6 .   ? -20.168 3.479   0.401   0.23 17.99  ? 368 HOH   B O   1 
HETATM 1941 O O   . HOH   K 6 .   ? -29.560 -5.763  -0.719  1.00 56.30  ? 369 HOH   B O   1 
HETATM 1942 O O   A HOH   K 6 .   ? -31.219 -8.683  -3.954  0.50 90.17  ? 370 HOH   B O   1 
HETATM 1943 O O   B HOH   K 6 .   ? -31.219 -8.683  -3.954  0.50 90.17  ? 370 HOH   B O   1 
HETATM 1944 O O   A HOH   K 6 .   ? -10.297 21.970  -13.890 0.50 63.28  ? 371 HOH   B O   1 
HETATM 1945 O O   B HOH   K 6 .   ? -10.297 21.970  -13.890 0.50 63.28  ? 371 HOH   B O   1 
HETATM 1946 O O   C HOH   K 6 .   ? -21.350 15.945  -24.215 0.50 66.22  ? 372 HOH   B O   1 
HETATM 1947 O O   D HOH   K 6 .   ? -21.350 15.945  -24.215 0.50 66.22  ? 372 HOH   B O   1 
HETATM 1948 O O   A HOH   K 6 .   ? -19.040 -11.780 -13.639 0.50 67.51  ? 373 HOH   B O   1 
HETATM 1949 O O   B HOH   K 6 .   ? -19.040 -11.780 -13.639 0.50 67.51  ? 373 HOH   B O   1 
HETATM 1950 O O   . HOH   K 6 .   ? -11.939 12.571  -15.108 1.00 63.17  ? 374 HOH   B O   1 
HETATM 1951 O O   A HOH   K 6 .   ? -11.646 -7.497  1.744   0.50 79.10  ? 375 HOH   B O   1 
HETATM 1952 O O   B HOH   K 6 .   ? -11.646 -7.497  1.744   0.50 79.10  ? 375 HOH   B O   1 
HETATM 1953 O O   C HOH   K 6 .   ? -17.876 -19.878 -28.475 0.50 54.49  ? 376 HOH   B O   1 
HETATM 1954 O O   D HOH   K 6 .   ? -17.876 -19.878 -28.475 0.50 54.49  ? 376 HOH   B O   1 
# 
