data_8W3C
# 
_entry.id   8W3C 
# 
_audit_conform.dict_name       mmcif_pdbx.dic 
_audit_conform.dict_version    5.401 
_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   8W3C         pdb_00008w3c 10.2210/pdb8w3c/pdb 
WWPDB D_1000281795 ?            ?                   
# 
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 
1 'Structure model' 1 0 2025-01-15 
2 'Structure model' 1 1 2025-02-05 
# 
_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               'Database references' 
# 
loop_
_pdbx_audit_revision_category.ordinal 
_pdbx_audit_revision_category.revision_ordinal 
_pdbx_audit_revision_category.data_content_type 
_pdbx_audit_revision_category.category 
1 2 'Structure model' citation        
2 2 'Structure model' citation_author 
# 
loop_
_pdbx_audit_revision_item.ordinal 
_pdbx_audit_revision_item.revision_ordinal 
_pdbx_audit_revision_item.data_content_type 
_pdbx_audit_revision_item.item 
1 2 'Structure model' '_citation.journal_volume'          
2 2 'Structure model' '_citation.pdbx_database_id_PubMed' 
3 2 'Structure model' '_citation.title'                   
4 2 'Structure model' '_citation_author.identifier_ORCID' 
5 2 'Structure model' '_citation_author.name'             
# 
_pdbx_database_status.status_code                     REL 
_pdbx_database_status.status_code_sf                  REL 
_pdbx_database_status.status_code_mr                  ? 
_pdbx_database_status.entry_id                        8W3C 
_pdbx_database_status.recvd_initial_deposition_date   2024-02-22 
_pdbx_database_status.SG_entry                        N 
_pdbx_database_status.deposit_site                    RCSB 
_pdbx_database_status.process_site                    RCSB 
_pdbx_database_status.status_code_cs                  ? 
_pdbx_database_status.status_code_nmr_data            ? 
_pdbx_database_status.methods_development_category    ? 
_pdbx_database_status.pdb_format_compatible           Y 
# 
_pdbx_contact_author.id                 4 
_pdbx_contact_author.email              celia.schiffer@umassmed.edu 
_pdbx_contact_author.name_first         Celia 
_pdbx_contact_author.name_last          Schiffer 
_pdbx_contact_author.name_mi            A. 
_pdbx_contact_author.role               'principal investigator/group leader' 
_pdbx_contact_author.identifier_ORCID   0000-0003-2270-6613 
# 
loop_
_audit_author.name 
_audit_author.pdbx_ordinal 
_audit_author.identifier_ORCID 
'Azzolino, V.N.' 1 0000-0003-3186-4760 
'Shaqra, A.M.'   2 0000-0001-6994-2416 
'Schiffer, C.A.' 3 0000-0003-2270-6613 
# 
_citation.abstract                  ? 
_citation.abstract_id_CAS           ? 
_citation.book_id_ISBN              ? 
_citation.book_publisher            ? 
_citation.book_publisher_city       ? 
_citation.book_title                ? 
_citation.coordinate_linkage        ? 
_citation.country                   CH 
_citation.database_id_Medline       ? 
_citation.details                   ? 
_citation.id                        primary 
_citation.journal_abbrev            Viruses 
_citation.journal_id_ASTM           ? 
_citation.journal_id_CSD            ? 
_citation.journal_id_ISSN           1999-4915 
_citation.journal_full              ? 
_citation.journal_issue             ? 
_citation.journal_volume            17 
_citation.language                  ? 
_citation.page_first                ? 
_citation.page_last                 ? 
_citation.title                     'Structural Analysis of Inhibitor Binding to Enterovirus-D68 3C Protease.' 
_citation.year                      2025 
_citation.database_id_CSD           ? 
_citation.pdbx_database_id_DOI      10.3390/v17010075 
_citation.pdbx_database_id_PubMed   39861864 
_citation.pdbx_database_id_patent   ? 
_citation.unpublished_flag          ? 
# 
loop_
_citation_author.citation_id 
_citation_author.name 
_citation_author.ordinal 
_citation_author.identifier_ORCID 
primary 'Azzolino, V.N.'  1 0000-0003-3186-4760 
primary 'Shaqra, A.M.'    2 ?                   
primary 'Ali, A.'         3 0000-0003-3491-791X 
primary 'Kurt Yilmaz, N.' 4 0000-0002-5036-676X 
primary 'Schiffer, C.A.'  5 0000-0003-2270-6613 
# 
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 'Peptidase C3' 21163.020 1   3.4.22.29,3.6.1.15,3.4.22.28,2.7.7.48 ? ? ? 
2 non-polymer syn 
;4-{2-(4-FLUORO-BENZYL)-6-METHYL-5-[(5-METHYL-ISOXAZOLE-3-CARBONYL)-AMINO]-4-OXO-HEPTANOYLAMINO}-5-(2-OXO-PYRROLIDIN-3-YL)-PENTANOIC ACID ETHYL ESTER
;
600.678   1   ?                                     ? ? ? 
3 water       nat water 18.015    130 ?                                     ? ? ? 
# 
_entity_poly.entity_id                      1 
_entity_poly.type                           'polypeptide(L)' 
_entity_poly.nstd_linkage                   no 
_entity_poly.nstd_monomer                   no 
_entity_poly.pdbx_seq_one_letter_code       
;GPGFDFAQAIMKKNTVVARTEKGEFTMLGVHDRVAVIPTHASVGETIYINDVETKVLDACALRDLTDTNLEITIVKLDRN
QKFRDIRHFLPRYEDDYNDAVLSVHTSKFPNMYIPVGQVTNYGFLNLGGTPTHRILMYNFPTRAGQCGGVVTTTGKVIGI
HVGGNGAQGFAAMLLHSYFTDTQKHHHHHH
;
_entity_poly.pdbx_seq_one_letter_code_can   
;GPGFDFAQAIMKKNTVVARTEKGEFTMLGVHDRVAVIPTHASVGETIYINDVETKVLDACALRDLTDTNLEITIVKLDRN
QKFRDIRHFLPRYEDDYNDAVLSVHTSKFPNMYIPVGQVTNYGFLNLGGTPTHRILMYNFPTRAGQCGGVVTTTGKVIGI
HVGGNGAQGFAAMLLHSYFTDTQKHHHHHH
;
_entity_poly.pdbx_strand_id                 A 
_entity_poly.pdbx_target_identifier         ? 
# 
loop_
_pdbx_entity_nonpoly.entity_id 
_pdbx_entity_nonpoly.name 
_pdbx_entity_nonpoly.comp_id 
2 
;4-{2-(4-FLUORO-BENZYL)-6-METHYL-5-[(5-METHYL-ISOXAZOLE-3-CARBONYL)-AMINO]-4-OXO-HEPTANOYLAMINO}-5-(2-OXO-PYRROLIDIN-3-YL)-PENTANOIC ACID ETHYL ESTER
;
AG7 
3 water HOH 
# 
loop_
_entity_poly_seq.entity_id 
_entity_poly_seq.num 
_entity_poly_seq.mon_id 
_entity_poly_seq.hetero 
1 1   GLY n 
1 2   PRO n 
1 3   GLY n 
1 4   PHE n 
1 5   ASP n 
1 6   PHE n 
1 7   ALA n 
1 8   GLN n 
1 9   ALA n 
1 10  ILE n 
1 11  MET n 
1 12  LYS n 
1 13  LYS n 
1 14  ASN n 
1 15  THR n 
1 16  VAL n 
1 17  VAL n 
1 18  ALA n 
1 19  ARG n 
1 20  THR n 
1 21  GLU n 
1 22  LYS n 
1 23  GLY n 
1 24  GLU n 
1 25  PHE n 
1 26  THR n 
1 27  MET n 
1 28  LEU n 
1 29  GLY n 
1 30  VAL n 
1 31  HIS n 
1 32  ASP n 
1 33  ARG n 
1 34  VAL n 
1 35  ALA n 
1 36  VAL n 
1 37  ILE n 
1 38  PRO n 
1 39  THR n 
1 40  HIS n 
1 41  ALA n 
1 42  SER n 
1 43  VAL n 
1 44  GLY n 
1 45  GLU n 
1 46  THR n 
1 47  ILE n 
1 48  TYR n 
1 49  ILE n 
1 50  ASN n 
1 51  ASP n 
1 52  VAL n 
1 53  GLU n 
1 54  THR n 
1 55  LYS n 
1 56  VAL n 
1 57  LEU n 
1 58  ASP n 
1 59  ALA n 
1 60  CYS n 
1 61  ALA n 
1 62  LEU n 
1 63  ARG n 
1 64  ASP n 
1 65  LEU n 
1 66  THR n 
1 67  ASP n 
1 68  THR n 
1 69  ASN n 
1 70  LEU n 
1 71  GLU n 
1 72  ILE n 
1 73  THR n 
1 74  ILE n 
1 75  VAL n 
1 76  LYS n 
1 77  LEU n 
1 78  ASP n 
1 79  ARG n 
1 80  ASN n 
1 81  GLN n 
1 82  LYS n 
1 83  PHE n 
1 84  ARG n 
1 85  ASP n 
1 86  ILE n 
1 87  ARG n 
1 88  HIS n 
1 89  PHE n 
1 90  LEU n 
1 91  PRO n 
1 92  ARG n 
1 93  TYR n 
1 94  GLU n 
1 95  ASP n 
1 96  ASP n 
1 97  TYR n 
1 98  ASN n 
1 99  ASP n 
1 100 ALA n 
1 101 VAL n 
1 102 LEU n 
1 103 SER n 
1 104 VAL n 
1 105 HIS n 
1 106 THR n 
1 107 SER n 
1 108 LYS n 
1 109 PHE n 
1 110 PRO n 
1 111 ASN n 
1 112 MET n 
1 113 TYR n 
1 114 ILE n 
1 115 PRO n 
1 116 VAL n 
1 117 GLY n 
1 118 GLN n 
1 119 VAL n 
1 120 THR n 
1 121 ASN n 
1 122 TYR n 
1 123 GLY n 
1 124 PHE n 
1 125 LEU n 
1 126 ASN n 
1 127 LEU n 
1 128 GLY n 
1 129 GLY n 
1 130 THR n 
1 131 PRO n 
1 132 THR n 
1 133 HIS n 
1 134 ARG n 
1 135 ILE n 
1 136 LEU n 
1 137 MET n 
1 138 TYR n 
1 139 ASN n 
1 140 PHE n 
1 141 PRO n 
1 142 THR n 
1 143 ARG n 
1 144 ALA n 
1 145 GLY n 
1 146 GLN n 
1 147 CYS n 
1 148 GLY n 
1 149 GLY n 
1 150 VAL n 
1 151 VAL n 
1 152 THR n 
1 153 THR n 
1 154 THR n 
1 155 GLY n 
1 156 LYS n 
1 157 VAL n 
1 158 ILE n 
1 159 GLY n 
1 160 ILE n 
1 161 HIS n 
1 162 VAL n 
1 163 GLY n 
1 164 GLY n 
1 165 ASN n 
1 166 GLY n 
1 167 ALA n 
1 168 GLN n 
1 169 GLY n 
1 170 PHE n 
1 171 ALA n 
1 172 ALA n 
1 173 MET n 
1 174 LEU n 
1 175 LEU n 
1 176 HIS n 
1 177 SER n 
1 178 TYR n 
1 179 PHE n 
1 180 THR n 
1 181 ASP n 
1 182 THR n 
1 183 GLN n 
1 184 LYS n 
1 185 HIS n 
1 186 HIS n 
1 187 HIS n 
1 188 HIS n 
1 189 HIS n 
1 190 HIS n 
# 
_entity_src_gen.entity_id                          1 
_entity_src_gen.pdbx_src_id                        1 
_entity_src_gen.pdbx_alt_source_flag               sample 
_entity_src_gen.pdbx_seq_type                      'Biological sequence' 
_entity_src_gen.pdbx_beg_seq_num                   1 
_entity_src_gen.pdbx_end_seq_num                   190 
_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      'enterovirus D68' 
_entity_src_gen.pdbx_gene_src_ncbi_taxonomy_id     42789 
_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      
;Escherichia coli 'BL21-Gold(DE3)pLysS AG'
;
_entity_src_gen.pdbx_host_org_ncbi_taxonomy_id     866768 
_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                   ? 
# 
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 
AG7 non-polymer         . 
;4-{2-(4-FLUORO-BENZYL)-6-METHYL-5-[(5-METHYL-ISOXAZOLE-3-CARBONYL)-AMINO]-4-OXO-HEPTANOYLAMINO}-5-(2-OXO-PYRROLIDIN-3-YL)-PENTANOIC ACID ETHYL ESTER
;
'RUPINTRIVIR, bound form' 'C31 H41 F N4 O7' 600.678 
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 
GLN 'L-peptide linking' y GLUTAMINE ?                         'C5 H10 N2 O3'    146.144 
GLU 'L-peptide linking' y 'GLUTAMIC ACID' ?                         'C5 H9 N O4'      147.129 
GLY 'peptide linking'   y GLYCINE ?                         'C2 H5 N O2'      75.067  
HIS 'L-peptide linking' y HISTIDINE ?                         'C6 H10 N3 O2 1'  156.162 
HOH non-polymer         . WATER ?                         'H2 O'            18.015  
ILE 'L-peptide linking' y ISOLEUCINE ?                         'C6 H13 N O2'     131.173 
LEU 'L-peptide linking' y LEUCINE ?                         'C6 H13 N O2'     131.173 
LYS 'L-peptide linking' y LYSINE ?                         'C6 H15 N2 O2 1'  147.195 
MET 'L-peptide linking' y METHIONINE ?                         'C5 H11 N O2 S'   149.211 
PHE 'L-peptide linking' y PHENYLALANINE ?                         'C9 H11 N O2'     165.189 
PRO 'L-peptide linking' y PROLINE ?                         'C5 H9 N O2'      115.130 
SER 'L-peptide linking' y SERINE ?                         'C3 H7 N O3'      105.093 
THR 'L-peptide linking' y THREONINE ?                         'C4 H9 N O3'      119.119 
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   GLY 1   1   1   GLY GLY A . n 
A 1 2   PRO 2   2   2   PRO PRO A . n 
A 1 3   GLY 3   3   3   GLY GLY A . n 
A 1 4   PHE 4   4   4   PHE PHE A . n 
A 1 5   ASP 5   5   5   ASP ASP A . n 
A 1 6   PHE 6   6   6   PHE PHE A . n 
A 1 7   ALA 7   7   7   ALA ALA A . n 
A 1 8   GLN 8   8   8   GLN GLN A . n 
A 1 9   ALA 9   9   9   ALA ALA A . n 
A 1 10  ILE 10  10  10  ILE ILE A . n 
A 1 11  MET 11  11  11  MET MET A . n 
A 1 12  LYS 12  12  12  LYS LYS A . n 
A 1 13  LYS 13  13  13  LYS LYS A . n 
A 1 14  ASN 14  14  14  ASN ASN A . n 
A 1 15  THR 15  15  15  THR THR A . n 
A 1 16  VAL 16  16  16  VAL VAL A . n 
A 1 17  VAL 17  17  17  VAL VAL A . n 
A 1 18  ALA 18  18  18  ALA ALA A . n 
A 1 19  ARG 19  19  19  ARG ARG A . n 
A 1 20  THR 20  20  20  THR THR A . n 
A 1 21  GLU 21  21  21  GLU GLU A . n 
A 1 22  LYS 22  22  22  LYS LYS A . n 
A 1 23  GLY 23  23  23  GLY GLY A . n 
A 1 24  GLU 24  24  24  GLU GLU A . n 
A 1 25  PHE 25  25  25  PHE PHE A . n 
A 1 26  THR 26  26  26  THR THR A . n 
A 1 27  MET 27  27  27  MET MET A . n 
A 1 28  LEU 28  28  28  LEU LEU A . n 
A 1 29  GLY 29  29  29  GLY GLY A . n 
A 1 30  VAL 30  30  30  VAL VAL A . n 
A 1 31  HIS 31  31  31  HIS HIS A . n 
A 1 32  ASP 32  32  32  ASP ASP A . n 
A 1 33  ARG 33  33  33  ARG ARG A . n 
A 1 34  VAL 34  34  34  VAL VAL A . n 
A 1 35  ALA 35  35  35  ALA ALA A . n 
A 1 36  VAL 36  36  36  VAL VAL A . n 
A 1 37  ILE 37  37  37  ILE ILE A . n 
A 1 38  PRO 38  38  38  PRO PRO A . n 
A 1 39  THR 39  39  39  THR THR A . n 
A 1 40  HIS 40  40  40  HIS HIS A . n 
A 1 41  ALA 41  41  41  ALA ALA A . n 
A 1 42  SER 42  42  42  SER SER A . n 
A 1 43  VAL 43  43  43  VAL VAL A . n 
A 1 44  GLY 44  44  44  GLY GLY A . n 
A 1 45  GLU 45  45  45  GLU GLU A . n 
A 1 46  THR 46  46  46  THR THR A . n 
A 1 47  ILE 47  47  47  ILE ILE A . n 
A 1 48  TYR 48  48  48  TYR TYR A . n 
A 1 49  ILE 49  49  49  ILE ILE A . n 
A 1 50  ASN 50  50  50  ASN ASN A . n 
A 1 51  ASP 51  51  51  ASP ASP A . n 
A 1 52  VAL 52  52  52  VAL VAL A . n 
A 1 53  GLU 53  53  53  GLU GLU A . n 
A 1 54  THR 54  54  54  THR THR A . n 
A 1 55  LYS 55  55  55  LYS LYS A . n 
A 1 56  VAL 56  56  56  VAL VAL A . n 
A 1 57  LEU 57  57  57  LEU LEU A . n 
A 1 58  ASP 58  58  58  ASP ASP A . n 
A 1 59  ALA 59  59  59  ALA ALA A . n 
A 1 60  CYS 60  60  60  CYS CYS A . n 
A 1 61  ALA 61  61  61  ALA ALA A . n 
A 1 62  LEU 62  62  62  LEU LEU A . n 
A 1 63  ARG 63  63  63  ARG ARG A . n 
A 1 64  ASP 64  64  64  ASP ASP A . n 
A 1 65  LEU 65  65  65  LEU LEU A . n 
A 1 66  THR 66  66  66  THR THR A . n 
A 1 67  ASP 67  67  67  ASP ASP A . n 
A 1 68  THR 68  68  68  THR THR A . n 
A 1 69  ASN 69  69  69  ASN ASN A . n 
A 1 70  LEU 70  70  70  LEU LEU A . n 
A 1 71  GLU 71  71  71  GLU GLU A . n 
A 1 72  ILE 72  72  72  ILE ILE A . n 
A 1 73  THR 73  73  73  THR THR A . n 
A 1 74  ILE 74  74  74  ILE ILE A . n 
A 1 75  VAL 75  75  75  VAL VAL A . n 
A 1 76  LYS 76  76  76  LYS LYS A . n 
A 1 77  LEU 77  77  77  LEU LEU A . n 
A 1 78  ASP 78  78  78  ASP ASP A . n 
A 1 79  ARG 79  79  79  ARG ARG A . n 
A 1 80  ASN 80  80  80  ASN ASN A . n 
A 1 81  GLN 81  81  81  GLN GLN A . n 
A 1 82  LYS 82  82  82  LYS LYS A . n 
A 1 83  PHE 83  83  83  PHE PHE A . n 
A 1 84  ARG 84  84  84  ARG ARG A . n 
A 1 85  ASP 85  85  85  ASP ASP A . n 
A 1 86  ILE 86  86  86  ILE ILE A . n 
A 1 87  ARG 87  87  87  ARG ARG A . n 
A 1 88  HIS 88  88  88  HIS HIS A . n 
A 1 89  PHE 89  89  89  PHE PHE A . n 
A 1 90  LEU 90  90  90  LEU LEU A . n 
A 1 91  PRO 91  91  91  PRO PRO A . n 
A 1 92  ARG 92  92  92  ARG ARG A . n 
A 1 93  TYR 93  93  93  TYR TYR A . n 
A 1 94  GLU 94  94  94  GLU GLU A . n 
A 1 95  ASP 95  95  95  ASP ASP A . n 
A 1 96  ASP 96  96  96  ASP ASP A . n 
A 1 97  TYR 97  97  97  TYR TYR A . n 
A 1 98  ASN 98  98  98  ASN ASN A . n 
A 1 99  ASP 99  99  99  ASP ASP A . n 
A 1 100 ALA 100 100 100 ALA ALA A . n 
A 1 101 VAL 101 101 101 VAL VAL A . n 
A 1 102 LEU 102 102 102 LEU LEU A . n 
A 1 103 SER 103 103 103 SER SER A . n 
A 1 104 VAL 104 104 104 VAL VAL A . n 
A 1 105 HIS 105 105 105 HIS HIS A . n 
A 1 106 THR 106 106 106 THR THR A . n 
A 1 107 SER 107 107 107 SER SER A . n 
A 1 108 LYS 108 108 108 LYS LYS A . n 
A 1 109 PHE 109 109 109 PHE PHE A . n 
A 1 110 PRO 110 110 110 PRO PRO A . n 
A 1 111 ASN 111 111 111 ASN ASN A . n 
A 1 112 MET 112 112 112 MET MET A . n 
A 1 113 TYR 113 113 113 TYR TYR A . n 
A 1 114 ILE 114 114 114 ILE ILE A . n 
A 1 115 PRO 115 115 115 PRO PRO A . n 
A 1 116 VAL 116 116 116 VAL VAL A . n 
A 1 117 GLY 117 117 117 GLY GLY A . n 
A 1 118 GLN 118 118 118 GLN GLN A . n 
A 1 119 VAL 119 119 119 VAL VAL A . n 
A 1 120 THR 120 120 120 THR THR A . n 
A 1 121 ASN 121 121 121 ASN ASN A . n 
A 1 122 TYR 122 122 122 TYR TYR A . n 
A 1 123 GLY 123 123 123 GLY GLY A . n 
A 1 124 PHE 124 124 124 PHE PHE A . n 
A 1 125 LEU 125 125 125 LEU LEU A . n 
A 1 126 ASN 126 126 126 ASN ASN A . n 
A 1 127 LEU 127 127 127 LEU LEU A . n 
A 1 128 GLY 128 128 128 GLY GLY A . n 
A 1 129 GLY 129 129 129 GLY GLY A . n 
A 1 130 THR 130 130 130 THR THR A . n 
A 1 131 PRO 131 131 131 PRO PRO A . n 
A 1 132 THR 132 132 132 THR THR A . n 
A 1 133 HIS 133 133 133 HIS HIS A . n 
A 1 134 ARG 134 134 134 ARG ARG A . n 
A 1 135 ILE 135 135 135 ILE ILE A . n 
A 1 136 LEU 136 136 136 LEU LEU A . n 
A 1 137 MET 137 137 137 MET MET A . n 
A 1 138 TYR 138 138 138 TYR TYR A . n 
A 1 139 ASN 139 139 139 ASN ASN A . n 
A 1 140 PHE 140 140 140 PHE PHE A . n 
A 1 141 PRO 141 141 141 PRO PRO A . n 
A 1 142 THR 142 142 142 THR THR A . n 
A 1 143 ARG 143 143 143 ARG ARG A . n 
A 1 144 ALA 144 144 144 ALA ALA A . n 
A 1 145 GLY 145 145 145 GLY GLY A . n 
A 1 146 GLN 146 146 146 GLN GLN A . n 
A 1 147 CYS 147 147 147 CYS CYS A . n 
A 1 148 GLY 148 148 148 GLY GLY A . n 
A 1 149 GLY 149 149 149 GLY GLY A . n 
A 1 150 VAL 150 150 150 VAL VAL A . n 
A 1 151 VAL 151 151 151 VAL VAL A . n 
A 1 152 THR 152 152 152 THR THR A . n 
A 1 153 THR 153 153 153 THR THR A . n 
A 1 154 THR 154 154 154 THR THR A . n 
A 1 155 GLY 155 155 155 GLY GLY A . n 
A 1 156 LYS 156 156 156 LYS LYS A . n 
A 1 157 VAL 157 157 157 VAL VAL A . n 
A 1 158 ILE 158 158 158 ILE ILE A . n 
A 1 159 GLY 159 159 159 GLY GLY A . n 
A 1 160 ILE 160 160 160 ILE ILE A . n 
A 1 161 HIS 161 161 161 HIS HIS A . n 
A 1 162 VAL 162 162 162 VAL VAL A . n 
A 1 163 GLY 163 163 163 GLY GLY A . n 
A 1 164 GLY 164 164 164 GLY GLY A . n 
A 1 165 ASN 165 165 165 ASN ASN A . n 
A 1 166 GLY 166 166 166 GLY GLY A . n 
A 1 167 ALA 167 167 167 ALA ALA A . n 
A 1 168 GLN 168 168 168 GLN GLN A . n 
A 1 169 GLY 169 169 169 GLY GLY A . n 
A 1 170 PHE 170 170 170 PHE PHE A . n 
A 1 171 ALA 171 171 171 ALA ALA A . n 
A 1 172 ALA 172 172 172 ALA ALA A . n 
A 1 173 MET 173 173 173 MET MET A . n 
A 1 174 LEU 174 174 174 LEU LEU A . n 
A 1 175 LEU 175 175 175 LEU LEU A . n 
A 1 176 HIS 176 176 176 HIS HIS A . n 
A 1 177 SER 177 177 177 SER SER A . n 
A 1 178 TYR 178 178 178 TYR TYR A . n 
A 1 179 PHE 179 179 179 PHE PHE A . n 
A 1 180 THR 180 180 180 THR THR A . n 
A 1 181 ASP 181 181 181 ASP ASP A . n 
A 1 182 THR 182 182 ?   ?   ?   A . n 
A 1 183 GLN 183 183 183 GLN GLN A . n 
A 1 184 LYS 184 184 184 LYS LYS A . n 
A 1 185 HIS 185 185 185 HIS HIS A . n 
A 1 186 HIS 186 186 186 HIS HIS A . n 
A 1 187 HIS 187 187 187 HIS HIS A . n 
A 1 188 HIS 188 188 188 HIS HIS A . n 
A 1 189 HIS 189 189 ?   ?   ?   A . n 
A 1 190 HIS 190 190 ?   ?   ?   A . n 
# 
_pdbx_entity_instance_feature.ordinal        1 
_pdbx_entity_instance_feature.comp_id        AG7 
_pdbx_entity_instance_feature.asym_id        ? 
_pdbx_entity_instance_feature.seq_num        ? 
_pdbx_entity_instance_feature.auth_comp_id   AG7 
_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 
B 2 AG7 1   201 201 AG7 LIG A . 
C 3 HOH 1   301 201 HOH HOH A . 
C 3 HOH 2   302 103 HOH HOH A . 
C 3 HOH 3   303 200 HOH HOH A . 
C 3 HOH 4   304 58  HOH HOH A . 
C 3 HOH 5   305 17  HOH HOH A . 
C 3 HOH 6   306 166 HOH HOH A . 
C 3 HOH 7   307 8   HOH HOH A . 
C 3 HOH 8   308 30  HOH HOH A . 
C 3 HOH 9   309 149 HOH HOH A . 
C 3 HOH 10  310 205 HOH HOH A . 
C 3 HOH 11  311 46  HOH HOH A . 
C 3 HOH 12  312 3   HOH HOH A . 
C 3 HOH 13  313 14  HOH HOH A . 
C 3 HOH 14  314 50  HOH HOH A . 
C 3 HOH 15  315 11  HOH HOH A . 
C 3 HOH 16  316 49  HOH HOH A . 
C 3 HOH 17  317 35  HOH HOH A . 
C 3 HOH 18  318 16  HOH HOH A . 
C 3 HOH 19  319 165 HOH HOH A . 
C 3 HOH 20  320 86  HOH HOH A . 
C 3 HOH 21  321 27  HOH HOH A . 
C 3 HOH 22  322 32  HOH HOH A . 
C 3 HOH 23  323 12  HOH HOH A . 
C 3 HOH 24  324 5   HOH HOH A . 
C 3 HOH 25  325 111 HOH HOH A . 
C 3 HOH 26  326 7   HOH HOH A . 
C 3 HOH 27  327 20  HOH HOH A . 
C 3 HOH 28  328 15  HOH HOH A . 
C 3 HOH 29  329 2   HOH HOH A . 
C 3 HOH 30  330 26  HOH HOH A . 
C 3 HOH 31  331 23  HOH HOH A . 
C 3 HOH 32  332 59  HOH HOH A . 
C 3 HOH 33  333 25  HOH HOH A . 
C 3 HOH 34  334 38  HOH HOH A . 
C 3 HOH 35  335 118 HOH HOH A . 
C 3 HOH 36  336 37  HOH HOH A . 
C 3 HOH 37  337 187 HOH HOH A . 
C 3 HOH 38  338 179 HOH HOH A . 
C 3 HOH 39  339 22  HOH HOH A . 
C 3 HOH 40  340 31  HOH HOH A . 
C 3 HOH 41  341 42  HOH HOH A . 
C 3 HOH 42  342 66  HOH HOH A . 
C 3 HOH 43  343 1   HOH HOH A . 
C 3 HOH 44  344 56  HOH HOH A . 
C 3 HOH 45  345 193 HOH HOH A . 
C 3 HOH 46  346 13  HOH HOH A . 
C 3 HOH 47  347 29  HOH HOH A . 
C 3 HOH 48  348 4   HOH HOH A . 
C 3 HOH 49  349 21  HOH HOH A . 
C 3 HOH 50  350 99  HOH HOH A . 
C 3 HOH 51  351 57  HOH HOH A . 
C 3 HOH 52  352 61  HOH HOH A . 
C 3 HOH 53  353 28  HOH HOH A . 
C 3 HOH 54  354 157 HOH HOH A . 
C 3 HOH 55  355 109 HOH HOH A . 
C 3 HOH 56  356 196 HOH HOH A . 
C 3 HOH 57  357 62  HOH HOH A . 
C 3 HOH 58  358 41  HOH HOH A . 
C 3 HOH 59  359 51  HOH HOH A . 
C 3 HOH 60  360 53  HOH HOH A . 
C 3 HOH 61  361 60  HOH HOH A . 
C 3 HOH 62  362 47  HOH HOH A . 
C 3 HOH 63  363 67  HOH HOH A . 
C 3 HOH 64  364 39  HOH HOH A . 
C 3 HOH 65  365 9   HOH HOH A . 
C 3 HOH 66  366 76  HOH HOH A . 
C 3 HOH 67  367 97  HOH HOH A . 
C 3 HOH 68  368 6   HOH HOH A . 
C 3 HOH 69  369 73  HOH HOH A . 
C 3 HOH 70  370 33  HOH HOH A . 
C 3 HOH 71  371 89  HOH HOH A . 
C 3 HOH 72  372 24  HOH HOH A . 
C 3 HOH 73  373 10  HOH HOH A . 
C 3 HOH 74  374 36  HOH HOH A . 
C 3 HOH 75  375 169 HOH HOH A . 
C 3 HOH 76  376 114 HOH HOH A . 
C 3 HOH 77  377 112 HOH HOH A . 
C 3 HOH 78  378 148 HOH HOH A . 
C 3 HOH 79  379 18  HOH HOH A . 
C 3 HOH 80  380 40  HOH HOH A . 
C 3 HOH 81  381 63  HOH HOH A . 
C 3 HOH 82  382 44  HOH HOH A . 
C 3 HOH 83  383 74  HOH HOH A . 
C 3 HOH 84  384 69  HOH HOH A . 
C 3 HOH 85  385 52  HOH HOH A . 
C 3 HOH 86  386 170 HOH HOH A . 
C 3 HOH 87  387 195 HOH HOH A . 
C 3 HOH 88  388 34  HOH HOH A . 
C 3 HOH 89  389 127 HOH HOH A . 
C 3 HOH 90  390 190 HOH HOH A . 
C 3 HOH 91  391 80  HOH HOH A . 
C 3 HOH 92  392 81  HOH HOH A . 
C 3 HOH 93  393 125 HOH HOH A . 
C 3 HOH 94  394 119 HOH HOH A . 
C 3 HOH 95  395 138 HOH HOH A . 
C 3 HOH 96  396 92  HOH HOH A . 
C 3 HOH 97  397 65  HOH HOH A . 
C 3 HOH 98  398 43  HOH HOH A . 
C 3 HOH 99  399 48  HOH HOH A . 
C 3 HOH 100 400 116 HOH HOH A . 
C 3 HOH 101 401 177 HOH HOH A . 
C 3 HOH 102 402 78  HOH HOH A . 
C 3 HOH 103 403 105 HOH HOH A . 
C 3 HOH 104 404 98  HOH HOH A . 
C 3 HOH 105 405 139 HOH HOH A . 
C 3 HOH 106 406 107 HOH HOH A . 
C 3 HOH 107 407 64  HOH HOH A . 
C 3 HOH 108 408 71  HOH HOH A . 
C 3 HOH 109 409 184 HOH HOH A . 
C 3 HOH 110 410 82  HOH HOH A . 
C 3 HOH 111 411 83  HOH HOH A . 
C 3 HOH 112 412 108 HOH HOH A . 
C 3 HOH 113 413 197 HOH HOH A . 
C 3 HOH 114 414 123 HOH HOH A . 
C 3 HOH 115 415 203 HOH HOH A . 
C 3 HOH 116 416 133 HOH HOH A . 
C 3 HOH 117 417 126 HOH HOH A . 
C 3 HOH 118 418 151 HOH HOH A . 
C 3 HOH 119 419 204 HOH HOH A . 
C 3 HOH 120 420 175 HOH HOH A . 
C 3 HOH 121 421 85  HOH HOH A . 
C 3 HOH 122 422 156 HOH HOH A . 
C 3 HOH 123 423 178 HOH HOH A . 
C 3 HOH 124 424 167 HOH HOH A . 
C 3 HOH 125 425 101 HOH HOH A . 
C 3 HOH 126 426 188 HOH HOH A . 
C 3 HOH 127 427 171 HOH HOH A . 
C 3 HOH 128 428 199 HOH HOH A . 
C 3 HOH 129 429 202 HOH HOH A . 
C 3 HOH 130 430 198 HOH HOH A . 
# 
loop_
_pdbx_unobs_or_zero_occ_atoms.id 
_pdbx_unobs_or_zero_occ_atoms.PDB_model_num 
_pdbx_unobs_or_zero_occ_atoms.polymer_flag 
_pdbx_unobs_or_zero_occ_atoms.occupancy_flag 
_pdbx_unobs_or_zero_occ_atoms.auth_asym_id 
_pdbx_unobs_or_zero_occ_atoms.auth_comp_id 
_pdbx_unobs_or_zero_occ_atoms.auth_seq_id 
_pdbx_unobs_or_zero_occ_atoms.PDB_ins_code 
_pdbx_unobs_or_zero_occ_atoms.auth_atom_id 
_pdbx_unobs_or_zero_occ_atoms.label_alt_id 
_pdbx_unobs_or_zero_occ_atoms.label_asym_id 
_pdbx_unobs_or_zero_occ_atoms.label_comp_id 
_pdbx_unobs_or_zero_occ_atoms.label_seq_id 
_pdbx_unobs_or_zero_occ_atoms.label_atom_id 
1 1 Y 1 A MET 112 ? CE  ? A MET 112 CE  
2 1 Y 1 A GLN 183 ? CG  ? A GLN 183 CG  
3 1 Y 1 A GLN 183 ? CD  ? A GLN 183 CD  
4 1 Y 1 A GLN 183 ? OE1 ? A GLN 183 OE1 
5 1 Y 1 A GLN 183 ? NE2 ? A GLN 183 NE2 
6 1 Y 1 A LYS 184 ? CG  ? A LYS 184 CG  
7 1 Y 1 A LYS 184 ? CD  ? A LYS 184 CD  
8 1 Y 1 A LYS 184 ? CE  ? A LYS 184 CE  
9 1 Y 1 A LYS 184 ? NZ  ? A LYS 184 NZ  
# 
loop_
_software.citation_id 
_software.classification 
_software.compiler_name 
_software.compiler_version 
_software.contact_author 
_software.contact_author_email 
_software.date 
_software.description 
_software.dependencies 
_software.hardware 
_software.language 
_software.location 
_software.mods 
_software.name 
_software.os 
_software.os_version 
_software.type 
_software.version 
_software.pdbx_ordinal 
? refinement       ? ? ? ? ? ? ? ? ? ? ? PHENIX ? ? ? 1.20.1_4487 1 
? phasing          ? ? ? ? ? ? ? ? ? ? ? PHENIX ? ? ? 1.20.1_4487 2 
? 'model building' ? ? ? ? ? ? ? ? ? ? ? Coot   ? ? ? 0.9.8.6     3 
? 'data reduction' ? ? ? ? ? ? ? ? ? ? ? XDS    ? ? ? .           4 
? 'data scaling'   ? ? ? ? ? ? ? ? ? ? ? XDS    ? ? ? .           5 
# 
_cell.angle_alpha                  90.000 
_cell.angle_alpha_esd              ? 
_cell.angle_beta                   90.000 
_cell.angle_beta_esd               ? 
_cell.angle_gamma                  120.000 
_cell.angle_gamma_esd              ? 
_cell.entry_id                     8W3C 
_cell.details                      ? 
_cell.formula_units_Z              ? 
_cell.length_a                     56.431 
_cell.length_a_esd                 ? 
_cell.length_b                     56.431 
_cell.length_b_esd                 ? 
_cell.length_c                     170.482 
_cell.length_c_esd                 ? 
_cell.volume                       470158.894 
_cell.volume_esd                   ? 
_cell.Z_PDB                        6 
_cell.reciprocal_angle_alpha       ? 
_cell.reciprocal_angle_beta        ? 
_cell.reciprocal_angle_gamma       ? 
_cell.reciprocal_angle_alpha_esd   ? 
_cell.reciprocal_angle_beta_esd    ? 
_cell.reciprocal_angle_gamma_esd   ? 
_cell.reciprocal_length_a          ? 
_cell.reciprocal_length_b          ? 
_cell.reciprocal_length_c          ? 
_cell.reciprocal_length_a_esd      ? 
_cell.reciprocal_length_b_esd      ? 
_cell.reciprocal_length_c_esd      ? 
_cell.pdbx_unique_axis             ? 
_cell.pdbx_esd_method              ? 
# 
_symmetry.entry_id                         8W3C 
_symmetry.cell_setting                     ? 
_symmetry.Int_Tables_number                152 
_symmetry.space_group_name_Hall            
;P 31 2"
;
_symmetry.space_group_name_H-M             'P 31 2 1' 
_symmetry.pdbx_full_space_group_name_H-M   ? 
# 
_exptl.absorpt_coefficient_mu     ? 
_exptl.absorpt_correction_T_max   ? 
_exptl.absorpt_correction_T_min   ? 
_exptl.absorpt_correction_type    ? 
_exptl.absorpt_process_details    ? 
_exptl.entry_id                   8W3C 
_exptl.crystals_number            1 
_exptl.details                    ? 
_exptl.method                     'X-RAY DIFFRACTION' 
_exptl.method_details             ? 
# 
_exptl_crystal.colour                       ? 
_exptl_crystal.density_diffrn               ? 
_exptl_crystal.density_Matthews             3.70 
_exptl_crystal.density_method               ? 
_exptl_crystal.density_percent_sol          66.78 
_exptl_crystal.description                  ? 
_exptl_crystal.F_000                        ? 
_exptl_crystal.id                           1 
_exptl_crystal.preparation                  ? 
_exptl_crystal.size_max                     ? 
_exptl_crystal.size_mid                     ? 
_exptl_crystal.size_min                     ? 
_exptl_crystal.size_rad                     ? 
_exptl_crystal.colour_lustre                ? 
_exptl_crystal.colour_modifier              ? 
_exptl_crystal.colour_primary               ? 
_exptl_crystal.density_meas                 ? 
_exptl_crystal.density_meas_esd             ? 
_exptl_crystal.density_meas_gt              ? 
_exptl_crystal.density_meas_lt              ? 
_exptl_crystal.density_meas_temp            ? 
_exptl_crystal.density_meas_temp_esd        ? 
_exptl_crystal.density_meas_temp_gt         ? 
_exptl_crystal.density_meas_temp_lt         ? 
_exptl_crystal.pdbx_crystal_image_url       ? 
_exptl_crystal.pdbx_crystal_image_format    ? 
_exptl_crystal.pdbx_mosaicity               ? 
_exptl_crystal.pdbx_mosaicity_esd           ? 
_exptl_crystal.pdbx_mosaic_method           ? 
_exptl_crystal.pdbx_mosaic_block_size       ? 
_exptl_crystal.pdbx_mosaic_block_size_esd   ? 
# 
_exptl_crystal_grow.apparatus       ? 
_exptl_crystal_grow.atmosphere      ? 
_exptl_crystal_grow.crystal_id      1 
_exptl_crystal_grow.details         ? 
_exptl_crystal_grow.method          'VAPOR DIFFUSION, HANGING DROP' 
_exptl_crystal_grow.method_ref      ? 
_exptl_crystal_grow.pH              4.6 
_exptl_crystal_grow.pressure        ? 
_exptl_crystal_grow.pressure_esd    ? 
_exptl_crystal_grow.seeding         ? 
_exptl_crystal_grow.seeding_ref     ? 
_exptl_crystal_grow.temp_details    ? 
_exptl_crystal_grow.temp_esd        ? 
_exptl_crystal_grow.time            ? 
_exptl_crystal_grow.pdbx_details    '0.07M Sodium Acetate, 6-15% PEG4000, Glycerol 10-35%' 
_exptl_crystal_grow.pdbx_pH_range   ? 
_exptl_crystal_grow.temp            293.15 
# 
_diffrn.ambient_environment              ? 
_diffrn.ambient_temp                     100 
_diffrn.ambient_temp_details             ? 
_diffrn.ambient_temp_esd                 ? 
_diffrn.crystal_id                       1 
_diffrn.crystal_support                  ? 
_diffrn.crystal_treatment                ? 
_diffrn.details                          ? 
_diffrn.id                               1 
_diffrn.ambient_pressure                 ? 
_diffrn.ambient_pressure_esd             ? 
_diffrn.ambient_pressure_gt              ? 
_diffrn.ambient_pressure_lt              ? 
_diffrn.ambient_temp_gt                  ? 
_diffrn.ambient_temp_lt                  ? 
_diffrn.pdbx_serial_crystal_experiment   N 
# 
_diffrn_detector.details                      ? 
_diffrn_detector.detector                     PIXEL 
_diffrn_detector.diffrn_id                    1 
_diffrn_detector.type                         'DECTRIS EIGER X 9M' 
_diffrn_detector.area_resol_mean              ? 
_diffrn_detector.dtime                        ? 
_diffrn_detector.pdbx_frames_total            ? 
_diffrn_detector.pdbx_collection_time_total   ? 
_diffrn_detector.pdbx_collection_date         2024-01-24 
_diffrn_detector.pdbx_frequency               ? 
_diffrn_detector.id                           ? 
_diffrn_detector.number_of_axes               ? 
# 
_diffrn_radiation.collimation                      ? 
_diffrn_radiation.diffrn_id                        1 
_diffrn_radiation.filter_edge                      ? 
_diffrn_radiation.inhomogeneity                    ? 
_diffrn_radiation.monochromator                    ? 
_diffrn_radiation.polarisn_norm                    ? 
_diffrn_radiation.polarisn_ratio                   ? 
_diffrn_radiation.probe                            ? 
_diffrn_radiation.type                             ? 
_diffrn_radiation.xray_symbol                      ? 
_diffrn_radiation.wavelength_id                    1 
_diffrn_radiation.pdbx_monochromatic_or_laue_m_l   M 
_diffrn_radiation.pdbx_wavelength_list             ? 
_diffrn_radiation.pdbx_wavelength                  ? 
_diffrn_radiation.pdbx_diffrn_protocol             'SINGLE WAVELENGTH' 
_diffrn_radiation.pdbx_analyzer                    ? 
_diffrn_radiation.pdbx_scattering_type             x-ray 
# 
_diffrn_radiation_wavelength.id           1 
_diffrn_radiation_wavelength.wavelength   0.9 
_diffrn_radiation_wavelength.wt           1.0 
# 
_diffrn_source.current                     ? 
_diffrn_source.details                     ? 
_diffrn_source.diffrn_id                   1 
_diffrn_source.power                       ? 
_diffrn_source.size                        ? 
_diffrn_source.source                      SYNCHROTRON 
_diffrn_source.target                      ? 
_diffrn_source.type                        'NSLS-II BEAMLINE 17-ID-2' 
_diffrn_source.voltage                     ? 
_diffrn_source.take-off_angle              ? 
_diffrn_source.pdbx_wavelength_list        0.9 
_diffrn_source.pdbx_wavelength             ? 
_diffrn_source.pdbx_synchrotron_beamline   17-ID-2 
_diffrn_source.pdbx_synchrotron_site       NSLS-II 
# 
_reflns.B_iso_Wilson_estimate                          36.98 
_reflns.entry_id                                       8W3C 
_reflns.data_reduction_details                         ? 
_reflns.data_reduction_method                          ? 
_reflns.d_resolution_high                              1.97 
_reflns.d_resolution_low                               32.12 
_reflns.details                                        ? 
_reflns.limit_h_max                                    ? 
_reflns.limit_h_min                                    ? 
_reflns.limit_k_max                                    ? 
_reflns.limit_k_min                                    ? 
_reflns.limit_l_max                                    ? 
_reflns.limit_l_min                                    ? 
_reflns.number_all                                     ? 
_reflns.number_obs                                     22963 
_reflns.observed_criterion                             ? 
_reflns.observed_criterion_F_max                       ? 
_reflns.observed_criterion_F_min                       ? 
_reflns.observed_criterion_I_max                       ? 
_reflns.observed_criterion_I_min                       ? 
_reflns.observed_criterion_sigma_F                     ? 
_reflns.observed_criterion_sigma_I                     ? 
_reflns.percent_possible_obs                           99.29 
_reflns.R_free_details                                 ? 
_reflns.Rmerge_F_all                                   ? 
_reflns.Rmerge_F_obs                                   ? 
_reflns.Friedel_coverage                               ? 
_reflns.number_gt                                      ? 
_reflns.threshold_expression                           ? 
_reflns.pdbx_redundancy                                2.0 
_reflns.pdbx_netI_over_av_sigmaI                       ? 
_reflns.pdbx_netI_over_sigmaI                          11.4 
_reflns.pdbx_res_netI_over_av_sigmaI_2                 ? 
_reflns.pdbx_res_netI_over_sigmaI_2                    ? 
_reflns.pdbx_chi_squared                               ? 
_reflns.pdbx_scaling_rejects                           ? 
_reflns.pdbx_d_res_high_opt                            ? 
_reflns.pdbx_d_res_low_opt                             ? 
_reflns.pdbx_d_res_opt_method                          ? 
_reflns.phase_calculation_details                      ? 
_reflns.pdbx_Rrim_I_all                                ? 
_reflns.pdbx_Rpim_I_all                                ? 
_reflns.pdbx_d_opt                                     ? 
_reflns.pdbx_number_measured_all                       ? 
_reflns.pdbx_diffrn_id                                 1 
_reflns.pdbx_ordinal                                   1 
_reflns.pdbx_CC_half                                   1.000 
_reflns.pdbx_CC_star                                   ? 
_reflns.pdbx_R_split                                   ? 
_reflns.pdbx_Rmerge_I_obs                              0.023 
_reflns.pdbx_Rmerge_I_all                              ? 
_reflns.pdbx_Rsym_value                                ? 
_reflns.pdbx_CC_split_method                           ? 
_reflns.pdbx_aniso_diffraction_limit_axis_1_ortho[1]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_1_ortho[2]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_1_ortho[3]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_2_ortho[1]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_2_ortho[2]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_2_ortho[3]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_3_ortho[1]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_3_ortho[2]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_3_ortho[3]   ? 
_reflns.pdbx_aniso_diffraction_limit_1                 ? 
_reflns.pdbx_aniso_diffraction_limit_2                 ? 
_reflns.pdbx_aniso_diffraction_limit_3                 ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_1_ortho[1]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_1_ortho[2]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_1_ortho[3]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_2_ortho[1]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_2_ortho[2]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_2_ortho[3]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_3_ortho[1]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_3_ortho[2]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_3_ortho[3]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvalue_1               ? 
_reflns.pdbx_aniso_B_tensor_eigenvalue_2               ? 
_reflns.pdbx_aniso_B_tensor_eigenvalue_3               ? 
_reflns.pdbx_orthogonalization_convention              ? 
_reflns.pdbx_percent_possible_ellipsoidal              ? 
_reflns.pdbx_percent_possible_spherical                ? 
_reflns.pdbx_percent_possible_ellipsoidal_anomalous    ? 
_reflns.pdbx_percent_possible_spherical_anomalous      ? 
_reflns.pdbx_redundancy_anomalous                      ? 
_reflns.pdbx_CC_half_anomalous                         ? 
_reflns.pdbx_absDiff_over_sigma_anomalous              ? 
_reflns.pdbx_percent_possible_anomalous                ? 
_reflns.pdbx_observed_signal_threshold                 ? 
_reflns.pdbx_signal_type                               ? 
_reflns.pdbx_signal_details                            ? 
_reflns.pdbx_signal_software_id                        ? 
# 
_reflns_shell.d_res_high                                    1.97 
_reflns_shell.d_res_low                                     2.04 
_reflns_shell.meanI_over_sigI_all                           ? 
_reflns_shell.meanI_over_sigI_obs                           1.4 
_reflns_shell.number_measured_all                           ? 
_reflns_shell.number_measured_obs                           ? 
_reflns_shell.number_possible                               ? 
_reflns_shell.number_unique_all                             ? 
_reflns_shell.number_unique_obs                             2280 
_reflns_shell.percent_possible_obs                          ? 
_reflns_shell.Rmerge_F_all                                  ? 
_reflns_shell.Rmerge_F_obs                                  ? 
_reflns_shell.meanI_over_sigI_gt                            ? 
_reflns_shell.meanI_over_uI_all                             ? 
_reflns_shell.meanI_over_uI_gt                              ? 
_reflns_shell.number_measured_gt                            ? 
_reflns_shell.number_unique_gt                              ? 
_reflns_shell.percent_possible_gt                           ? 
_reflns_shell.Rmerge_F_gt                                   ? 
_reflns_shell.Rmerge_I_gt                                   ? 
_reflns_shell.pdbx_redundancy                               2.0 
_reflns_shell.pdbx_chi_squared                              ? 
_reflns_shell.pdbx_netI_over_sigmaI_all                     ? 
_reflns_shell.pdbx_netI_over_sigmaI_obs                     ? 
_reflns_shell.pdbx_Rrim_I_all                               ? 
_reflns_shell.pdbx_Rpim_I_all                               ? 
_reflns_shell.pdbx_rejects                                  ? 
_reflns_shell.pdbx_ordinal                                  1 
_reflns_shell.pdbx_diffrn_id                                1 
_reflns_shell.pdbx_CC_half                                  0.956 
_reflns_shell.pdbx_CC_star                                  ? 
_reflns_shell.pdbx_R_split                                  ? 
_reflns_shell.percent_possible_all                          99.9 
_reflns_shell.Rmerge_I_all                                  ? 
_reflns_shell.Rmerge_I_obs                                  0.310 
_reflns_shell.pdbx_Rsym_value                               ? 
_reflns_shell.pdbx_percent_possible_ellipsoidal             ? 
_reflns_shell.pdbx_percent_possible_spherical               ? 
_reflns_shell.pdbx_percent_possible_ellipsoidal_anomalous   ? 
_reflns_shell.pdbx_percent_possible_spherical_anomalous     ? 
_reflns_shell.pdbx_redundancy_anomalous                     ? 
_reflns_shell.pdbx_CC_half_anomalous                        ? 
_reflns_shell.pdbx_absDiff_over_sigma_anomalous             ? 
_reflns_shell.pdbx_percent_possible_anomalous               ? 
# 
_refine.aniso_B[1][1]                            ? 
_refine.aniso_B[1][2]                            ? 
_refine.aniso_B[1][3]                            ? 
_refine.aniso_B[2][2]                            ? 
_refine.aniso_B[2][3]                            ? 
_refine.aniso_B[3][3]                            ? 
_refine.B_iso_max                                ? 
_refine.B_iso_mean                               48.63 
_refine.B_iso_min                                ? 
_refine.correlation_coeff_Fo_to_Fc               ? 
_refine.correlation_coeff_Fo_to_Fc_free          ? 
_refine.details                                  ? 
_refine.diff_density_max                         ? 
_refine.diff_density_max_esd                     ? 
_refine.diff_density_min                         ? 
_refine.diff_density_min_esd                     ? 
_refine.diff_density_rms                         ? 
_refine.diff_density_rms_esd                     ? 
_refine.entry_id                                 8W3C 
_refine.pdbx_refine_id                           'X-RAY DIFFRACTION' 
_refine.ls_abs_structure_details                 ? 
_refine.ls_abs_structure_Flack                   ? 
_refine.ls_abs_structure_Flack_esd               ? 
_refine.ls_abs_structure_Rogers                  ? 
_refine.ls_abs_structure_Rogers_esd              ? 
_refine.ls_d_res_high                            1.97 
_refine.ls_d_res_low                             32.12 
_refine.ls_extinction_coef                       ? 
_refine.ls_extinction_coef_esd                   ? 
_refine.ls_extinction_expression                 ? 
_refine.ls_extinction_method                     ? 
_refine.ls_goodness_of_fit_all                   ? 
_refine.ls_goodness_of_fit_all_esd               ? 
_refine.ls_goodness_of_fit_obs                   ? 
_refine.ls_goodness_of_fit_obs_esd               ? 
_refine.ls_hydrogen_treatment                    ? 
_refine.ls_matrix_type                           ? 
_refine.ls_number_constraints                    ? 
_refine.ls_number_parameters                     ? 
_refine.ls_number_reflns_all                     ? 
_refine.ls_number_reflns_obs                     22963 
_refine.ls_number_reflns_R_free                  1155 
_refine.ls_number_reflns_R_work                  21808 
_refine.ls_number_restraints                     ? 
_refine.ls_percent_reflns_obs                    99.29 
_refine.ls_percent_reflns_R_free                 5.03 
_refine.ls_R_factor_all                          ? 
_refine.ls_R_factor_obs                          0.2097 
_refine.ls_R_factor_R_free                       0.2306 
_refine.ls_R_factor_R_free_error                 ? 
_refine.ls_R_factor_R_free_error_details         ? 
_refine.ls_R_factor_R_work                       0.2085 
_refine.ls_R_Fsqd_factor_obs                     ? 
_refine.ls_R_I_factor_obs                        ? 
_refine.ls_redundancy_reflns_all                 ? 
_refine.ls_redundancy_reflns_obs                 ? 
_refine.ls_restrained_S_all                      ? 
_refine.ls_restrained_S_obs                      ? 
_refine.ls_shift_over_esd_max                    ? 
_refine.ls_shift_over_esd_mean                   ? 
_refine.ls_structure_factor_coef                 ? 
_refine.ls_weighting_details                     ? 
_refine.ls_weighting_scheme                      ? 
_refine.ls_wR_factor_all                         ? 
_refine.ls_wR_factor_obs                         ? 
_refine.ls_wR_factor_R_free                      ? 
_refine.ls_wR_factor_R_work                      ? 
_refine.occupancy_max                            ? 
_refine.occupancy_min                            ? 
_refine.solvent_model_details                    'FLAT BULK SOLVENT MODEL' 
_refine.solvent_model_param_bsol                 ? 
_refine.solvent_model_param_ksol                 ? 
_refine.pdbx_R_complete                          ? 
_refine.ls_R_factor_gt                           ? 
_refine.ls_goodness_of_fit_gt                    ? 
_refine.ls_goodness_of_fit_ref                   ? 
_refine.ls_shift_over_su_max                     ? 
_refine.ls_shift_over_su_max_lt                  ? 
_refine.ls_shift_over_su_mean                    ? 
_refine.ls_shift_over_su_mean_lt                 ? 
_refine.pdbx_ls_sigma_I                          ? 
_refine.pdbx_ls_sigma_F                          1.35 
_refine.pdbx_ls_sigma_Fsqd                       ? 
_refine.pdbx_data_cutoff_high_absF               ? 
_refine.pdbx_data_cutoff_high_rms_absF           ? 
_refine.pdbx_data_cutoff_low_absF                ? 
_refine.pdbx_isotropic_thermal_model             ? 
_refine.pdbx_ls_cross_valid_method               'FREE R-VALUE' 
_refine.pdbx_method_to_determine_struct          'MOLECULAR REPLACEMENT' 
_refine.pdbx_starting_model                      ? 
_refine.pdbx_stereochemistry_target_values       'GeoStd + Monomer Library + CDL v1.2' 
_refine.pdbx_R_Free_selection_details            ? 
_refine.pdbx_stereochem_target_val_spec_case     ? 
_refine.pdbx_overall_ESU_R                       ? 
_refine.pdbx_overall_ESU_R_Free                  ? 
_refine.pdbx_solvent_vdw_probe_radii             1.1000 
_refine.pdbx_solvent_ion_probe_radii             ? 
_refine.pdbx_solvent_shrinkage_radii             0.9000 
_refine.pdbx_real_space_R                        ? 
_refine.pdbx_density_correlation                 ? 
_refine.pdbx_pd_number_of_powder_patterns        ? 
_refine.pdbx_pd_number_of_points                 ? 
_refine.pdbx_pd_meas_number_of_points            ? 
_refine.pdbx_pd_proc_ls_prof_R_factor            ? 
_refine.pdbx_pd_proc_ls_prof_wR_factor           ? 
_refine.pdbx_pd_Marquardt_correlation_coeff      ? 
_refine.pdbx_pd_Fsqrd_R_factor                   ? 
_refine.pdbx_pd_ls_matrix_band_width             ? 
_refine.pdbx_overall_phase_error                 35.4774 
_refine.pdbx_overall_SU_R_free_Cruickshank_DPI   ? 
_refine.pdbx_overall_SU_R_free_Blow_DPI          ? 
_refine.pdbx_overall_SU_R_Blow_DPI               ? 
_refine.pdbx_TLS_residual_ADP_flag               ? 
_refine.pdbx_diffrn_id                           1 
_refine.overall_SU_B                             ? 
_refine.overall_SU_ML                            0.1973 
_refine.overall_SU_R_Cruickshank_DPI             ? 
_refine.overall_SU_R_free                        ? 
_refine.overall_FOM_free_R_set                   ? 
_refine.overall_FOM_work_R_set                   ? 
_refine.pdbx_average_fsc_overall                 ? 
_refine.pdbx_average_fsc_work                    ? 
_refine.pdbx_average_fsc_free                    ? 
# 
_refine_hist.pdbx_refine_id                   'X-RAY DIFFRACTION' 
_refine_hist.cycle_id                         LAST 
_refine_hist.details                          ? 
_refine_hist.d_res_high                       1.97 
_refine_hist.d_res_low                        32.12 
_refine_hist.number_atoms_solvent             130 
_refine_hist.number_atoms_total               1626 
_refine_hist.number_reflns_all                ? 
_refine_hist.number_reflns_obs                ? 
_refine_hist.number_reflns_R_free             ? 
_refine_hist.number_reflns_R_work             ? 
_refine_hist.R_factor_all                     ? 
_refine_hist.R_factor_obs                     ? 
_refine_hist.R_factor_R_free                  ? 
_refine_hist.R_factor_R_work                  ? 
_refine_hist.pdbx_number_residues_total       ? 
_refine_hist.pdbx_B_iso_mean_ligand           ? 
_refine_hist.pdbx_B_iso_mean_solvent          ? 
_refine_hist.pdbx_number_atoms_protein        1453 
_refine_hist.pdbx_number_atoms_nucleic_acid   0 
_refine_hist.pdbx_number_atoms_ligand         43 
_refine_hist.pdbx_number_atoms_lipid          ? 
_refine_hist.pdbx_number_atoms_carb           ? 
_refine_hist.pdbx_pseudo_atom_details         ? 
# 
loop_
_refine_ls_restr.pdbx_refine_id 
_refine_ls_restr.criterion 
_refine_ls_restr.dev_ideal 
_refine_ls_restr.dev_ideal_target 
_refine_ls_restr.number 
_refine_ls_restr.rejects 
_refine_ls_restr.type 
_refine_ls_restr.weight 
_refine_ls_restr.pdbx_restraint_function 
'X-RAY DIFFRACTION' ? 0.0133 ? 1535 ? f_bond_d           ? ? 
'X-RAY DIFFRACTION' ? 1.2578 ? 2084 ? f_angle_d          ? ? 
'X-RAY DIFFRACTION' ? 0.0812 ? 233  ? f_chiral_restr     ? ? 
'X-RAY DIFFRACTION' ? 0.0146 ? 270  ? f_plane_restr      ? ? 
'X-RAY DIFFRACTION' ? 7.8328 ? 211  ? f_dihedral_angle_d ? ? 
# 
loop_
_refine_ls_shell.pdbx_refine_id 
_refine_ls_shell.d_res_high 
_refine_ls_shell.d_res_low 
_refine_ls_shell.number_reflns_all 
_refine_ls_shell.number_reflns_obs 
_refine_ls_shell.number_reflns_R_free 
_refine_ls_shell.number_reflns_R_work 
_refine_ls_shell.percent_reflns_obs 
_refine_ls_shell.percent_reflns_R_free 
_refine_ls_shell.R_factor_all 
_refine_ls_shell.R_factor_obs 
_refine_ls_shell.R_factor_R_free_error 
_refine_ls_shell.R_factor_R_work 
_refine_ls_shell.redundancy_reflns_all 
_refine_ls_shell.redundancy_reflns_obs 
_refine_ls_shell.wR_factor_all 
_refine_ls_shell.wR_factor_obs 
_refine_ls_shell.wR_factor_R_free 
_refine_ls_shell.wR_factor_R_work 
_refine_ls_shell.pdbx_R_complete 
_refine_ls_shell.pdbx_total_number_of_bins_used 
_refine_ls_shell.pdbx_phase_error 
_refine_ls_shell.pdbx_fsc_work 
_refine_ls_shell.pdbx_fsc_free 
_refine_ls_shell.R_factor_R_free 
'X-RAY DIFFRACTION' 1.97 2.04 . . 140 2280 99.9 . . . . 0.3581 . . . . . . . . . . . 0.5230 
'X-RAY DIFFRACTION' 2.04 2.12 . . 146 2264 100  . . . . 0.3233 . . . . . . . . . . . 0.3196 
'X-RAY DIFFRACTION' 2.12 2.22 . . 138 2243 99.5 . . . . 0.2810 . . . . . . . . . . . 0.3515 
'X-RAY DIFFRACTION' 2.22 2.34 . . 145 2298 99.9 . . . . 0.2720 . . . . . . . . . . . 0.3303 
'X-RAY DIFFRACTION' 2.34 2.48 . . 145 2254 99.9 . . . . 0.2286 . . . . . . . . . . . 0.2716 
'X-RAY DIFFRACTION' 2.48 2.67 . . 145 2292 100  . . . . 0.2638 . . . . . . . . . . . 0.3450 
'X-RAY DIFFRACTION' 2.67 2.94 . . 139 2309 100  . . . . 0.2403 . . . . . . . . . . . 0.2543 
'X-RAY DIFFRACTION' 2.94 3.37 . . 157 2316 100  . . . . 0.2199 . . . . . . . . . . . 0.2075 
# 
_struct.entry_id                     8W3C 
_struct.title                        'Crystal Structure of Enterovirus 68 3C Protease with AG7088 at 1.97 Angstroms' 
_struct.pdbx_model_details           ? 
_struct.pdbx_formula_weight          ? 
_struct.pdbx_formula_weight_method   ? 
_struct.pdbx_model_type_details      ? 
_struct.pdbx_CASP_flag               N 
# 
_struct_keywords.entry_id        8W3C 
_struct_keywords.text            
'PROTEASE, HYDROLASE, ENTEROVIRUS, 3C PROTEIN, EV68, INHIBITOR, VIRAL PROTEIN, HYDROLASE-INHIBITOR complex' 
_struct_keywords.pdbx_keywords   'VIRAL PROTEIN,HYDROLASE/INHIBITOR' 
# 
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 ? 
# 
_struct_ref.id                         1 
_struct_ref.db_name                    UNP 
_struct_ref.db_code                    A1E4A3_HED68 
_struct_ref.pdbx_db_accession          A1E4A3 
_struct_ref.pdbx_db_isoform            ? 
_struct_ref.entity_id                  1 
_struct_ref.pdbx_seq_one_letter_code   
;GPGFDFAQAIMKKNTVVARTEKGEFTMLGVHDRVAVIPTHASVGETIYINDVETKVLDACALRDLTDTNLEITIVKLDRN
QKFRDIRHFLPRYEDDYNDAVLSVHTSKFPNMYIPVGQVTNYGFLNLGGTPTHRILMYNFPTRAGQCGGVVTTTGKVIGI
HVGGNGAQGFAAMLLHSYFTDTQ
;
_struct_ref.pdbx_align_begin           1549 
# 
_struct_ref_seq.align_id                      1 
_struct_ref_seq.ref_id                        1 
_struct_ref_seq.pdbx_PDB_id_code              8W3C 
_struct_ref_seq.pdbx_strand_id                A 
_struct_ref_seq.seq_align_beg                 1 
_struct_ref_seq.pdbx_seq_align_beg_ins_code   ? 
_struct_ref_seq.seq_align_end                 183 
_struct_ref_seq.pdbx_seq_align_end_ins_code   ? 
_struct_ref_seq.pdbx_db_accession             A1E4A3 
_struct_ref_seq.db_align_beg                  1549 
_struct_ref_seq.pdbx_db_align_beg_ins_code    ? 
_struct_ref_seq.db_align_end                  1731 
_struct_ref_seq.pdbx_db_align_end_ins_code    ? 
_struct_ref_seq.pdbx_auth_seq_align_beg       1 
_struct_ref_seq.pdbx_auth_seq_align_end       183 
# 
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 8W3C LYS A 184 ? UNP A1E4A3 ? ? 'expression tag' 184 1 
1 8W3C HIS A 185 ? UNP A1E4A3 ? ? 'expression tag' 185 2 
1 8W3C HIS A 186 ? UNP A1E4A3 ? ? 'expression tag' 186 3 
1 8W3C HIS A 187 ? UNP A1E4A3 ? ? 'expression tag' 187 4 
1 8W3C HIS A 188 ? UNP A1E4A3 ? ? 'expression tag' 188 5 
1 8W3C HIS A 189 ? UNP A1E4A3 ? ? 'expression tag' 189 6 
1 8W3C HIS A 190 ? UNP A1E4A3 ? ? 'expression tag' 190 7 
# 
_pdbx_struct_assembly.id                   1 
_pdbx_struct_assembly.details              author_defined_assembly 
_pdbx_struct_assembly.method_details       ? 
_pdbx_struct_assembly.oligomeric_details   monomeric 
_pdbx_struct_assembly.oligomeric_count     1 
# 
_pdbx_struct_assembly_gen.assembly_id       1 
_pdbx_struct_assembly_gen.oper_expression   1 
_pdbx_struct_assembly_gen.asym_id_list      A,B,C 
# 
_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 GLY A 3   ? ASN A 14  ? GLY A 3   ASN A 14  1 ? 12 
HELX_P HELX_P2 AA2 HIS A 40  ? SER A 42  ? HIS A 40  SER A 42  5 ? 3  
HELX_P HELX_P3 AA3 ILE A 86  ? LEU A 90  ? ILE A 86  LEU A 90  5 ? 5  
HELX_P HELX_P4 AA4 LEU A 175 ? PHE A 179 ? LEU A 175 PHE A 179 5 ? 5  
# 
_struct_conf_type.id          HELX_P 
_struct_conf_type.criteria    ? 
_struct_conf_type.reference   ? 
# 
_struct_conn.id                            covale1 
_struct_conn.conn_type_id                  covale 
_struct_conn.pdbx_leaving_atom_flag        none 
_struct_conn.pdbx_PDB_id                   ? 
_struct_conn.ptnr1_label_asym_id           A 
_struct_conn.ptnr1_label_comp_id           CYS 
_struct_conn.ptnr1_label_seq_id            147 
_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           AG7 
_struct_conn.ptnr2_label_seq_id            . 
_struct_conn.ptnr2_label_atom_id           C19 
_struct_conn.pdbx_ptnr2_label_alt_id       ? 
_struct_conn.pdbx_ptnr2_PDB_ins_code       ? 
_struct_conn.ptnr1_auth_asym_id            A 
_struct_conn.ptnr1_auth_comp_id            CYS 
_struct_conn.ptnr1_auth_seq_id             147 
_struct_conn.ptnr2_auth_asym_id            A 
_struct_conn.ptnr2_auth_comp_id            AG7 
_struct_conn.ptnr2_auth_seq_id             201 
_struct_conn.ptnr2_symmetry                1_555 
_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               1.769 
_struct_conn.pdbx_value_order              ? 
_struct_conn.pdbx_role                     ? 
# 
_struct_conn_type.id          covale 
_struct_conn_type.criteria    ? 
_struct_conn_type.reference   ? 
# 
_pdbx_modification_feature.ordinal                            1 
_pdbx_modification_feature.label_comp_id                      AG7 
_pdbx_modification_feature.label_asym_id                      B 
_pdbx_modification_feature.label_seq_id                       . 
_pdbx_modification_feature.label_alt_id                       ? 
_pdbx_modification_feature.modified_residue_label_comp_id     CYS 
_pdbx_modification_feature.modified_residue_label_asym_id     A 
_pdbx_modification_feature.modified_residue_label_seq_id      147 
_pdbx_modification_feature.modified_residue_label_alt_id      ? 
_pdbx_modification_feature.auth_comp_id                       AG7 
_pdbx_modification_feature.auth_asym_id                       A 
_pdbx_modification_feature.auth_seq_id                        201 
_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      A 
_pdbx_modification_feature.modified_residue_auth_seq_id       147 
_pdbx_modification_feature.modified_residue_PDB_ins_code      ? 
_pdbx_modification_feature.modified_residue_symmetry          1_555 
_pdbx_modification_feature.comp_id_linking_atom               C19 
_pdbx_modification_feature.modified_residue_id_linking_atom   SG 
_pdbx_modification_feature.modified_residue_id                CYS 
_pdbx_modification_feature.ref_pcm_id                         1 
_pdbx_modification_feature.ref_comp_id                        AG7 
_pdbx_modification_feature.type                               None 
_pdbx_modification_feature.category                           'Covalent chemical modification' 
# 
loop_
_struct_sheet.id 
_struct_sheet.type 
_struct_sheet.number_strands 
_struct_sheet.details 
AA1 ? 7 ? 
AA2 ? 7 ? 
# 
loop_
_struct_sheet_order.sheet_id 
_struct_sheet_order.range_id_1 
_struct_sheet_order.range_id_2 
_struct_sheet_order.offset 
_struct_sheet_order.sense 
AA1 1 2 ? anti-parallel 
AA1 2 3 ? anti-parallel 
AA1 3 4 ? anti-parallel 
AA1 4 5 ? anti-parallel 
AA1 5 6 ? anti-parallel 
AA1 6 7 ? anti-parallel 
AA2 1 2 ? anti-parallel 
AA2 2 3 ? anti-parallel 
AA2 3 4 ? anti-parallel 
AA2 4 5 ? anti-parallel 
AA2 5 6 ? anti-parallel 
AA2 6 7 ? 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 THR A 15  ? THR A 20  ? THR A 15  THR A 20  
AA1 2 GLY A 23  ? HIS A 31  ? GLY A 23  HIS A 31  
AA1 3 VAL A 34  ? PRO A 38  ? VAL A 34  PRO A 38  
AA1 4 ASN A 69  ? LEU A 77  ? ASN A 69  LEU A 77  
AA1 5 VAL A 52  ? ARG A 63  ? VAL A 52  ARG A 63  
AA1 6 THR A 46  ? ILE A 49  ? THR A 46  ILE A 49  
AA1 7 THR A 15  ? THR A 20  ? THR A 15  THR A 20  
AA2 1 TYR A 97  ? VAL A 104 ? TYR A 97  VAL A 104 
AA2 2 MET A 112 ? LEU A 127 ? MET A 112 LEU A 127 
AA2 3 THR A 130 ? TYR A 138 ? THR A 130 TYR A 138 
AA2 4 GLY A 169 ? MET A 173 ? GLY A 169 MET A 173 
AA2 5 LYS A 156 ? GLY A 164 ? LYS A 156 GLY A 164 
AA2 6 VAL A 150 ? THR A 153 ? VAL A 150 THR A 153 
AA2 7 TYR A 97  ? VAL A 104 ? TYR A 97  VAL A 104 
# 
loop_
_pdbx_struct_sheet_hbond.sheet_id 
_pdbx_struct_sheet_hbond.range_id_1 
_pdbx_struct_sheet_hbond.range_id_2 
_pdbx_struct_sheet_hbond.range_1_label_atom_id 
_pdbx_struct_sheet_hbond.range_1_label_comp_id 
_pdbx_struct_sheet_hbond.range_1_label_asym_id 
_pdbx_struct_sheet_hbond.range_1_label_seq_id 
_pdbx_struct_sheet_hbond.range_1_PDB_ins_code 
_pdbx_struct_sheet_hbond.range_1_auth_atom_id 
_pdbx_struct_sheet_hbond.range_1_auth_comp_id 
_pdbx_struct_sheet_hbond.range_1_auth_asym_id 
_pdbx_struct_sheet_hbond.range_1_auth_seq_id 
_pdbx_struct_sheet_hbond.range_2_label_atom_id 
_pdbx_struct_sheet_hbond.range_2_label_comp_id 
_pdbx_struct_sheet_hbond.range_2_label_asym_id 
_pdbx_struct_sheet_hbond.range_2_label_seq_id 
_pdbx_struct_sheet_hbond.range_2_PDB_ins_code 
_pdbx_struct_sheet_hbond.range_2_auth_atom_id 
_pdbx_struct_sheet_hbond.range_2_auth_comp_id 
_pdbx_struct_sheet_hbond.range_2_auth_asym_id 
_pdbx_struct_sheet_hbond.range_2_auth_seq_id 
AA1 1 2 N ALA A 18  ? N ALA A 18  O PHE A 25  ? O PHE A 25  
AA1 2 3 N HIS A 31  ? N HIS A 31  O VAL A 34  ? O VAL A 34  
AA1 3 4 N ALA A 35  ? N ALA A 35  O VAL A 75  ? O VAL A 75  
AA1 4 5 O ILE A 72  ? O ILE A 72  N LEU A 62  ? N LEU A 62  
AA1 5 6 O VAL A 52  ? O VAL A 52  N ILE A 49  ? N ILE A 49  
AA1 6 7 O TYR A 48  ? O TYR A 48  N ARG A 19  ? N ARG A 19  
AA2 1 2 N LEU A 102 ? N LEU A 102 O ILE A 114 ? O ILE A 114 
AA2 2 3 N THR A 120 ? N THR A 120 O MET A 137 ? O MET A 137 
AA2 3 4 N TYR A 138 ? N TYR A 138 O GLY A 169 ? O GLY A 169 
AA2 4 5 O PHE A 170 ? O PHE A 170 N VAL A 162 ? N VAL A 162 
AA2 5 6 O GLY A 159 ? O GLY A 159 N VAL A 151 ? N VAL A 151 
AA2 6 7 O THR A 152 ? O THR A 152 N VAL A 101 ? N VAL A 101 
# 
_pdbx_entry_details.entry_id                   8W3C 
_pdbx_entry_details.nonpolymer_details         ? 
_pdbx_entry_details.sequence_details           ? 
_pdbx_entry_details.compound_details           ? 
_pdbx_entry_details.source_details             ? 
_pdbx_entry_details.has_ligand_of_interest     Y 
_pdbx_entry_details.has_protein_modification   Y 
# 
_pdbx_validate_close_contact.id               1 
_pdbx_validate_close_contact.PDB_model_num    1 
_pdbx_validate_close_contact.auth_atom_id_1   O 
_pdbx_validate_close_contact.auth_asym_id_1   A 
_pdbx_validate_close_contact.auth_comp_id_1   HOH 
_pdbx_validate_close_contact.auth_seq_id_1    356 
_pdbx_validate_close_contact.PDB_ins_code_1   ? 
_pdbx_validate_close_contact.label_alt_id_1   ? 
_pdbx_validate_close_contact.auth_atom_id_2   O 
_pdbx_validate_close_contact.auth_asym_id_2   A 
_pdbx_validate_close_contact.auth_comp_id_2   HOH 
_pdbx_validate_close_contact.auth_seq_id_2    413 
_pdbx_validate_close_contact.PDB_ins_code_2   ? 
_pdbx_validate_close_contact.label_alt_id_2   ? 
_pdbx_validate_close_contact.dist             2.00 
# 
_pdbx_validate_symm_contact.id                1 
_pdbx_validate_symm_contact.PDB_model_num     1 
_pdbx_validate_symm_contact.auth_atom_id_1    O 
_pdbx_validate_symm_contact.auth_asym_id_1    A 
_pdbx_validate_symm_contact.auth_comp_id_1    HOH 
_pdbx_validate_symm_contact.auth_seq_id_1     354 
_pdbx_validate_symm_contact.PDB_ins_code_1    ? 
_pdbx_validate_symm_contact.label_alt_id_1    ? 
_pdbx_validate_symm_contact.site_symmetry_1   1_555 
_pdbx_validate_symm_contact.auth_atom_id_2    O 
_pdbx_validate_symm_contact.auth_asym_id_2    A 
_pdbx_validate_symm_contact.auth_comp_id_2    HOH 
_pdbx_validate_symm_contact.auth_seq_id_2     395 
_pdbx_validate_symm_contact.PDB_ins_code_2    ? 
_pdbx_validate_symm_contact.label_alt_id_2    ? 
_pdbx_validate_symm_contact.site_symmetry_2   6_555 
_pdbx_validate_symm_contact.dist              2.12 
# 
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 32  ? ? 48.70  -115.22 
2 1 ASN A 121 ? ? -62.03 98.52   
3 1 ALA A 144 ? ? -37.88 132.47  
# 
_pdbx_validate_planes.id              1 
_pdbx_validate_planes.PDB_model_num   1 
_pdbx_validate_planes.auth_comp_id    ARG 
_pdbx_validate_planes.auth_asym_id    A 
_pdbx_validate_planes.auth_seq_id     143 
_pdbx_validate_planes.PDB_ins_code    ? 
_pdbx_validate_planes.label_alt_id    ? 
_pdbx_validate_planes.rmsd            0.108 
_pdbx_validate_planes.type            'SIDE CHAIN' 
# 
loop_
_space_group_symop.id 
_space_group_symop.operation_xyz 
1 x,y,z          
2 -y,x-y,z+1/3   
3 -x+y,-x,z+2/3  
4 x-y,-y,-z+2/3  
5 -x,-x+y,-z+1/3 
6 y,x,-z         
# 
loop_
_pdbx_distant_solvent_atoms.id 
_pdbx_distant_solvent_atoms.PDB_model_num 
_pdbx_distant_solvent_atoms.auth_atom_id 
_pdbx_distant_solvent_atoms.label_alt_id 
_pdbx_distant_solvent_atoms.auth_asym_id 
_pdbx_distant_solvent_atoms.auth_comp_id 
_pdbx_distant_solvent_atoms.auth_seq_id 
_pdbx_distant_solvent_atoms.PDB_ins_code 
_pdbx_distant_solvent_atoms.neighbor_macromolecule_distance 
_pdbx_distant_solvent_atoms.neighbor_ligand_distance 
1 1 O ? A HOH 429 ? .    6.22 
2 1 O ? A HOH 430 ? 6.23 .    
# 
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 THR 182 ? A THR 182 
2 1 Y 1 A HIS 189 ? A HIS 189 
3 1 Y 1 A HIS 190 ? A HIS 190 
# 
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 
AG7 C01  C N N 1   
AG7 C02  C N N 2   
AG7 O03  O N N 3   
AG7 C04  C N R 4   
AG7 C05  C N N 5   
AG7 C06  C Y N 6   
AG7 C07  C Y N 7   
AG7 C08  C Y N 8   
AG7 C09  C Y N 9   
AG7 C10  C Y N 10  
AG7 C11  C Y N 11  
AG7 N12  N N N 12  
AG7 C13  C N R 13  
AG7 C14  C N N 14  
AG7 C15  C N S 15  
AG7 C16  C N N 16  
AG7 N17  N N N 17  
AG7 O18  O N N 18  
AG7 C19  C N N 19  
AG7 C20  C N N 20  
AG7 C21  C N N 21  
AG7 O22  O N N 22  
AG7 O23  O N N 23  
AG7 C47  C N N 24  
AG7 O48  O N N 25  
AG7 C50  C N N 26  
AG7 C53  C N N 27  
AG7 C57  C N S 28  
AG7 N58  N N N 29  
AG7 C59  C N N 30  
AG7 O60  O N N 31  
AG7 C78  C N N 32  
AG7 C81  C N N 33  
AG7 F1   F N N 34  
AG7 C82  C N N 35  
AG7 C83  C N N 36  
AG7 C84  C N N 37  
AG7 C1   C Y N 38  
AG7 C2   C Y N 39  
AG7 C3   C Y N 40  
AG7 O4   O Y N 41  
AG7 N5   N Y N 42  
AG7 C4   C N N 43  
AG7 H2   H N N 44  
AG7 H3   H N N 45  
AG7 H27  H N N 46  
AG7 H28  H N N 47  
AG7 H29  H N N 48  
AG7 H30  H N N 49  
AG7 H31  H N N 50  
AG7 H33  H N N 51  
AG7 H34  H N N 52  
AG7 H49  H N N 53  
AG7 H91  H N N 54  
AG7 H35  H N N 55  
AG7 H36  H N N 56  
AG7 H94  H N N 57  
AG7 H39  H N N 58  
AG7 H191 H N N 59  
AG7 H192 H N N 60  
AG7 H41  H N N 61  
AG7 H42  H N N 62  
AG7 H51  H N N 63  
AG7 H52  H N N 64  
AG7 H53  H N N 65  
AG7 H54  H N N 66  
AG7 H56  H N N 67  
AG7 H77  H N N 68  
AG7 H61  H N N 69  
AG7 H79  H N N 70  
AG7 H82  H N N 71  
AG7 H84  H N N 72  
AG7 H85  H N N 73  
AG7 H86  H N N 74  
AG7 H87  H N N 75  
AG7 H88  H N N 76  
AG7 H89  H N N 77  
AG7 H90  H N N 78  
AG7 H92  H N N 79  
AG7 H93  H N N 80  
AG7 H8   H N N 81  
AG7 H5   H N N 82  
AG7 H6   H N N 83  
AG7 H7   H N N 84  
ALA N    N N N 85  
ALA CA   C N S 86  
ALA C    C N N 87  
ALA O    O N N 88  
ALA CB   C N N 89  
ALA OXT  O N N 90  
ALA H    H N N 91  
ALA H2   H N N 92  
ALA HA   H N N 93  
ALA HB1  H N N 94  
ALA HB2  H N N 95  
ALA HB3  H N N 96  
ALA HXT  H N N 97  
ARG N    N N N 98  
ARG CA   C N S 99  
ARG C    C N N 100 
ARG O    O N N 101 
ARG CB   C N N 102 
ARG CG   C N N 103 
ARG CD   C N N 104 
ARG NE   N N N 105 
ARG CZ   C N N 106 
ARG NH1  N N N 107 
ARG NH2  N N N 108 
ARG OXT  O N N 109 
ARG H    H N N 110 
ARG H2   H N N 111 
ARG HA   H N N 112 
ARG HB2  H N N 113 
ARG HB3  H N N 114 
ARG HG2  H N N 115 
ARG HG3  H N N 116 
ARG HD2  H N N 117 
ARG HD3  H N N 118 
ARG HE   H N N 119 
ARG HH11 H N N 120 
ARG HH12 H N N 121 
ARG HH21 H N N 122 
ARG HH22 H N N 123 
ARG HXT  H N N 124 
ASN N    N N N 125 
ASN CA   C N S 126 
ASN C    C N N 127 
ASN O    O N N 128 
ASN CB   C N N 129 
ASN CG   C N N 130 
ASN OD1  O N N 131 
ASN ND2  N N N 132 
ASN OXT  O N N 133 
ASN H    H N N 134 
ASN H2   H N N 135 
ASN HA   H N N 136 
ASN HB2  H N N 137 
ASN HB3  H N N 138 
ASN HD21 H N N 139 
ASN HD22 H N N 140 
ASN HXT  H N N 141 
ASP N    N N N 142 
ASP CA   C N S 143 
ASP C    C N N 144 
ASP O    O N N 145 
ASP CB   C N N 146 
ASP CG   C N N 147 
ASP OD1  O N N 148 
ASP OD2  O N N 149 
ASP OXT  O N N 150 
ASP H    H N N 151 
ASP H2   H N N 152 
ASP HA   H N N 153 
ASP HB2  H N N 154 
ASP HB3  H N N 155 
ASP HD2  H N N 156 
ASP HXT  H N N 157 
CYS N    N N N 158 
CYS CA   C N R 159 
CYS C    C N N 160 
CYS O    O N N 161 
CYS CB   C N N 162 
CYS SG   S N N 163 
CYS OXT  O N N 164 
CYS H    H N N 165 
CYS H2   H N N 166 
CYS HA   H N N 167 
CYS HB2  H N N 168 
CYS HB3  H N N 169 
CYS HG   H N N 170 
CYS HXT  H N N 171 
GLN N    N N N 172 
GLN CA   C N S 173 
GLN C    C N N 174 
GLN O    O N N 175 
GLN CB   C N N 176 
GLN CG   C N N 177 
GLN CD   C N N 178 
GLN OE1  O N N 179 
GLN NE2  N N N 180 
GLN OXT  O N N 181 
GLN H    H N N 182 
GLN H2   H N N 183 
GLN HA   H N N 184 
GLN HB2  H N N 185 
GLN HB3  H N N 186 
GLN HG2  H N N 187 
GLN HG3  H N N 188 
GLN HE21 H N N 189 
GLN HE22 H N N 190 
GLN HXT  H N N 191 
GLU N    N N N 192 
GLU CA   C N S 193 
GLU C    C N N 194 
GLU O    O N N 195 
GLU CB   C N N 196 
GLU CG   C N N 197 
GLU CD   C N N 198 
GLU OE1  O N N 199 
GLU OE2  O N N 200 
GLU OXT  O N N 201 
GLU H    H N N 202 
GLU H2   H N N 203 
GLU HA   H N N 204 
GLU HB2  H N N 205 
GLU HB3  H N N 206 
GLU HG2  H N N 207 
GLU HG3  H N N 208 
GLU HE2  H N N 209 
GLU HXT  H N N 210 
GLY N    N N N 211 
GLY CA   C N N 212 
GLY C    C N N 213 
GLY O    O N N 214 
GLY OXT  O N N 215 
GLY H    H N N 216 
GLY H2   H N N 217 
GLY HA2  H N N 218 
GLY HA3  H N N 219 
GLY HXT  H N N 220 
HIS N    N N N 221 
HIS CA   C N S 222 
HIS C    C N N 223 
HIS O    O N N 224 
HIS CB   C N N 225 
HIS CG   C Y N 226 
HIS ND1  N Y N 227 
HIS CD2  C Y N 228 
HIS CE1  C Y N 229 
HIS NE2  N Y N 230 
HIS OXT  O N N 231 
HIS H    H N N 232 
HIS H2   H N N 233 
HIS HA   H N N 234 
HIS HB2  H N N 235 
HIS HB3  H N N 236 
HIS HD1  H N N 237 
HIS HD2  H N N 238 
HIS HE1  H N N 239 
HIS HE2  H N N 240 
HIS HXT  H N N 241 
HOH O    O N N 242 
HOH H1   H N N 243 
HOH H2   H N N 244 
ILE N    N N N 245 
ILE CA   C N S 246 
ILE C    C N N 247 
ILE O    O N N 248 
ILE CB   C N S 249 
ILE CG1  C N N 250 
ILE CG2  C N N 251 
ILE CD1  C N N 252 
ILE OXT  O N N 253 
ILE H    H N N 254 
ILE H2   H N N 255 
ILE HA   H N N 256 
ILE HB   H N N 257 
ILE HG12 H N N 258 
ILE HG13 H N N 259 
ILE HG21 H N N 260 
ILE HG22 H N N 261 
ILE HG23 H N N 262 
ILE HD11 H N N 263 
ILE HD12 H N N 264 
ILE HD13 H N N 265 
ILE HXT  H N N 266 
LEU N    N N N 267 
LEU CA   C N S 268 
LEU C    C N N 269 
LEU O    O N N 270 
LEU CB   C N N 271 
LEU CG   C N N 272 
LEU CD1  C N N 273 
LEU CD2  C N N 274 
LEU OXT  O N N 275 
LEU H    H N N 276 
LEU H2   H N N 277 
LEU HA   H N N 278 
LEU HB2  H N N 279 
LEU HB3  H N N 280 
LEU HG   H N N 281 
LEU HD11 H N N 282 
LEU HD12 H N N 283 
LEU HD13 H N N 284 
LEU HD21 H N N 285 
LEU HD22 H N N 286 
LEU HD23 H N N 287 
LEU HXT  H N N 288 
LYS N    N N N 289 
LYS CA   C N S 290 
LYS C    C N N 291 
LYS O    O N N 292 
LYS CB   C N N 293 
LYS CG   C N N 294 
LYS CD   C N N 295 
LYS CE   C N N 296 
LYS NZ   N N N 297 
LYS OXT  O N N 298 
LYS H    H N N 299 
LYS H2   H N N 300 
LYS HA   H N N 301 
LYS HB2  H N N 302 
LYS HB3  H N N 303 
LYS HG2  H N N 304 
LYS HG3  H N N 305 
LYS HD2  H N N 306 
LYS HD3  H N N 307 
LYS HE2  H N N 308 
LYS HE3  H N N 309 
LYS HZ1  H N N 310 
LYS HZ2  H N N 311 
LYS HZ3  H N N 312 
LYS HXT  H N N 313 
MET N    N N N 314 
MET CA   C N S 315 
MET C    C N N 316 
MET O    O N N 317 
MET CB   C N N 318 
MET CG   C N N 319 
MET SD   S N N 320 
MET CE   C N N 321 
MET OXT  O N N 322 
MET H    H N N 323 
MET H2   H N N 324 
MET HA   H N N 325 
MET HB2  H N N 326 
MET HB3  H N N 327 
MET HG2  H N N 328 
MET HG3  H N N 329 
MET HE1  H N N 330 
MET HE2  H N N 331 
MET HE3  H N N 332 
MET HXT  H N N 333 
PHE N    N N N 334 
PHE CA   C N S 335 
PHE C    C N N 336 
PHE O    O N N 337 
PHE CB   C N N 338 
PHE CG   C Y N 339 
PHE CD1  C Y N 340 
PHE CD2  C Y N 341 
PHE CE1  C Y N 342 
PHE CE2  C Y N 343 
PHE CZ   C Y N 344 
PHE OXT  O N N 345 
PHE H    H N N 346 
PHE H2   H N N 347 
PHE HA   H N N 348 
PHE HB2  H N N 349 
PHE HB3  H N N 350 
PHE HD1  H N N 351 
PHE HD2  H N N 352 
PHE HE1  H N N 353 
PHE HE2  H N N 354 
PHE HZ   H N N 355 
PHE HXT  H N N 356 
PRO N    N N N 357 
PRO CA   C N S 358 
PRO C    C N N 359 
PRO O    O N N 360 
PRO CB   C N N 361 
PRO CG   C N N 362 
PRO CD   C N N 363 
PRO OXT  O N N 364 
PRO H    H N N 365 
PRO HA   H N N 366 
PRO HB2  H N N 367 
PRO HB3  H N N 368 
PRO HG2  H N N 369 
PRO HG3  H N N 370 
PRO HD2  H N N 371 
PRO HD3  H N N 372 
PRO HXT  H N N 373 
SER N    N N N 374 
SER CA   C N S 375 
SER C    C N N 376 
SER O    O N N 377 
SER CB   C N N 378 
SER OG   O N N 379 
SER OXT  O N N 380 
SER H    H N N 381 
SER H2   H N N 382 
SER HA   H N N 383 
SER HB2  H N N 384 
SER HB3  H N N 385 
SER HG   H N N 386 
SER HXT  H N N 387 
THR N    N N N 388 
THR CA   C N S 389 
THR C    C N N 390 
THR O    O N N 391 
THR CB   C N R 392 
THR OG1  O N N 393 
THR CG2  C N N 394 
THR OXT  O N N 395 
THR H    H N N 396 
THR H2   H N N 397 
THR HA   H N N 398 
THR HB   H N N 399 
THR HG1  H N N 400 
THR HG21 H N N 401 
THR HG22 H N N 402 
THR HG23 H N N 403 
THR HXT  H N N 404 
TYR N    N N N 405 
TYR CA   C N S 406 
TYR C    C N N 407 
TYR O    O N N 408 
TYR CB   C N N 409 
TYR CG   C Y N 410 
TYR CD1  C Y N 411 
TYR CD2  C Y N 412 
TYR CE1  C Y N 413 
TYR CE2  C Y N 414 
TYR CZ   C Y N 415 
TYR OH   O N N 416 
TYR OXT  O N N 417 
TYR H    H N N 418 
TYR H2   H N N 419 
TYR HA   H N N 420 
TYR HB2  H N N 421 
TYR HB3  H N N 422 
TYR HD1  H N N 423 
TYR HD2  H N N 424 
TYR HE1  H N N 425 
TYR HE2  H N N 426 
TYR HH   H N N 427 
TYR HXT  H N N 428 
VAL N    N N N 429 
VAL CA   C N S 430 
VAL C    C N N 431 
VAL O    O N N 432 
VAL CB   C N N 433 
VAL CG1  C N N 434 
VAL CG2  C N N 435 
VAL OXT  O N N 436 
VAL H    H N N 437 
VAL H2   H N N 438 
VAL HA   H N N 439 
VAL HB   H N N 440 
VAL HG11 H N N 441 
VAL HG12 H N N 442 
VAL HG13 H N N 443 
VAL HG21 H N N 444 
VAL HG22 H N N 445 
VAL HG23 H N N 446 
VAL HXT  H N N 447 
# 
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 
AG7 C01 C02  sing N N 1   
AG7 C01 O03  doub N N 2   
AG7 C01 C57  sing N N 3   
AG7 C02 C04  sing N N 4   
AG7 C02 H2   sing N N 5   
AG7 C02 H3   sing N N 6   
AG7 C04 C05  sing N N 7   
AG7 C04 C47  sing N N 8   
AG7 C04 H27  sing N N 9   
AG7 C05 C06  sing N N 10  
AG7 C05 H28  sing N N 11  
AG7 C05 H29  sing N N 12  
AG7 C06 C07  doub Y N 13  
AG7 C06 C11  sing Y N 14  
AG7 C07 C08  sing Y N 15  
AG7 C07 H30  sing N N 16  
AG7 C08 C09  doub Y N 17  
AG7 C08 H31  sing N N 18  
AG7 C09 C10  sing Y N 19  
AG7 C09 F1   sing N N 20  
AG7 C10 C11  doub Y N 21  
AG7 C10 H33  sing N N 22  
AG7 C11 H34  sing N N 23  
AG7 N12 C13  sing N N 24  
AG7 N12 C47  sing N N 25  
AG7 N12 H49  sing N N 26  
AG7 C13 C14  sing N N 27  
AG7 C13 C19  sing N N 28  
AG7 C13 H91  sing N N 29  
AG7 C14 C15  sing N N 30  
AG7 C14 H35  sing N N 31  
AG7 C14 H36  sing N N 32  
AG7 C15 C16  sing N N 33  
AG7 C15 C84  sing N N 34  
AG7 C15 H94  sing N N 35  
AG7 C16 N17  sing N N 36  
AG7 C16 O18  doub N N 37  
AG7 N17 C83  sing N N 38  
AG7 N17 H39  sing N N 39  
AG7 C19 C20  sing N N 40  
AG7 C19 H191 sing N N 41  
AG7 C19 H192 sing N N 42  
AG7 C20 C21  sing N N 43  
AG7 C20 H41  sing N N 44  
AG7 C20 H42  sing N N 45  
AG7 C21 O22  sing N N 46  
AG7 C21 O23  doub N N 47  
AG7 O22 C50  sing N N 48  
AG7 C47 O48  doub N N 49  
AG7 C50 C53  sing N N 50  
AG7 C50 H51  sing N N 51  
AG7 C50 H52  sing N N 52  
AG7 C53 H53  sing N N 53  
AG7 C53 H54  sing N N 54  
AG7 C53 H56  sing N N 55  
AG7 C57 N58  sing N N 56  
AG7 C57 C78  sing N N 57  
AG7 C57 H77  sing N N 58  
AG7 N58 C59  sing N N 59  
AG7 N58 H61  sing N N 60  
AG7 C59 O60  doub N N 61  
AG7 C59 C1   sing N N 62  
AG7 C78 C81  sing N N 63  
AG7 C78 C82  sing N N 64  
AG7 C78 H79  sing N N 65  
AG7 C81 H82  sing N N 66  
AG7 C81 H84  sing N N 67  
AG7 C81 H85  sing N N 68  
AG7 C82 H86  sing N N 69  
AG7 C82 H87  sing N N 70  
AG7 C82 H88  sing N N 71  
AG7 C83 C84  sing N N 72  
AG7 C83 H89  sing N N 73  
AG7 C83 H90  sing N N 74  
AG7 C84 H92  sing N N 75  
AG7 C84 H93  sing N N 76  
AG7 C1  C2   sing Y N 77  
AG7 C1  N5   doub Y N 78  
AG7 C2  C3   doub Y N 79  
AG7 C2  H8   sing N N 80  
AG7 C3  O4   sing Y N 81  
AG7 C3  C4   sing N N 82  
AG7 O4  N5   sing Y N 83  
AG7 C4  H5   sing N N 84  
AG7 C4  H6   sing N N 85  
AG7 C4  H7   sing N N 86  
ALA N   CA   sing N N 87  
ALA N   H    sing N N 88  
ALA N   H2   sing N N 89  
ALA CA  C    sing N N 90  
ALA CA  CB   sing N N 91  
ALA CA  HA   sing N N 92  
ALA C   O    doub N N 93  
ALA C   OXT  sing N N 94  
ALA CB  HB1  sing N N 95  
ALA CB  HB2  sing N N 96  
ALA CB  HB3  sing N N 97  
ALA OXT HXT  sing N N 98  
ARG N   CA   sing N N 99  
ARG N   H    sing N N 100 
ARG N   H2   sing N N 101 
ARG CA  C    sing N N 102 
ARG CA  CB   sing N N 103 
ARG CA  HA   sing N N 104 
ARG C   O    doub N N 105 
ARG C   OXT  sing N N 106 
ARG CB  CG   sing N N 107 
ARG CB  HB2  sing N N 108 
ARG CB  HB3  sing N N 109 
ARG CG  CD   sing N N 110 
ARG CG  HG2  sing N N 111 
ARG CG  HG3  sing N N 112 
ARG CD  NE   sing N N 113 
ARG CD  HD2  sing N N 114 
ARG CD  HD3  sing N N 115 
ARG NE  CZ   sing N N 116 
ARG NE  HE   sing N N 117 
ARG CZ  NH1  sing N N 118 
ARG CZ  NH2  doub N N 119 
ARG NH1 HH11 sing N N 120 
ARG NH1 HH12 sing N N 121 
ARG NH2 HH21 sing N N 122 
ARG NH2 HH22 sing N N 123 
ARG OXT HXT  sing N N 124 
ASN N   CA   sing N N 125 
ASN N   H    sing N N 126 
ASN N   H2   sing N N 127 
ASN CA  C    sing N N 128 
ASN CA  CB   sing N N 129 
ASN CA  HA   sing N N 130 
ASN C   O    doub N N 131 
ASN C   OXT  sing N N 132 
ASN CB  CG   sing N N 133 
ASN CB  HB2  sing N N 134 
ASN CB  HB3  sing N N 135 
ASN CG  OD1  doub N N 136 
ASN CG  ND2  sing N N 137 
ASN ND2 HD21 sing N N 138 
ASN ND2 HD22 sing N N 139 
ASN OXT HXT  sing N N 140 
ASP N   CA   sing N N 141 
ASP N   H    sing N N 142 
ASP N   H2   sing N N 143 
ASP CA  C    sing N N 144 
ASP CA  CB   sing N N 145 
ASP CA  HA   sing N N 146 
ASP C   O    doub N N 147 
ASP C   OXT  sing N N 148 
ASP CB  CG   sing N N 149 
ASP CB  HB2  sing N N 150 
ASP CB  HB3  sing N N 151 
ASP CG  OD1  doub N N 152 
ASP CG  OD2  sing N N 153 
ASP OD2 HD2  sing N N 154 
ASP OXT HXT  sing N N 155 
CYS N   CA   sing N N 156 
CYS N   H    sing N N 157 
CYS N   H2   sing N N 158 
CYS CA  C    sing N N 159 
CYS CA  CB   sing N N 160 
CYS CA  HA   sing N N 161 
CYS C   O    doub N N 162 
CYS C   OXT  sing N N 163 
CYS CB  SG   sing N N 164 
CYS CB  HB2  sing N N 165 
CYS CB  HB3  sing N N 166 
CYS SG  HG   sing N N 167 
CYS OXT HXT  sing N N 168 
GLN N   CA   sing N N 169 
GLN N   H    sing N N 170 
GLN N   H2   sing N N 171 
GLN CA  C    sing N N 172 
GLN CA  CB   sing N N 173 
GLN CA  HA   sing N N 174 
GLN C   O    doub N N 175 
GLN C   OXT  sing N N 176 
GLN CB  CG   sing N N 177 
GLN CB  HB2  sing N N 178 
GLN CB  HB3  sing N N 179 
GLN CG  CD   sing N N 180 
GLN CG  HG2  sing N N 181 
GLN CG  HG3  sing N N 182 
GLN CD  OE1  doub N N 183 
GLN CD  NE2  sing N N 184 
GLN NE2 HE21 sing N N 185 
GLN NE2 HE22 sing N N 186 
GLN OXT HXT  sing N N 187 
GLU N   CA   sing N N 188 
GLU N   H    sing N N 189 
GLU N   H2   sing N N 190 
GLU CA  C    sing N N 191 
GLU CA  CB   sing N N 192 
GLU CA  HA   sing N N 193 
GLU C   O    doub N N 194 
GLU C   OXT  sing N N 195 
GLU CB  CG   sing N N 196 
GLU CB  HB2  sing N N 197 
GLU CB  HB3  sing N N 198 
GLU CG  CD   sing N N 199 
GLU CG  HG2  sing N N 200 
GLU CG  HG3  sing N N 201 
GLU CD  OE1  doub N N 202 
GLU CD  OE2  sing N N 203 
GLU OE2 HE2  sing N N 204 
GLU OXT HXT  sing N N 205 
GLY N   CA   sing N N 206 
GLY N   H    sing N N 207 
GLY N   H2   sing N N 208 
GLY CA  C    sing N N 209 
GLY CA  HA2  sing N N 210 
GLY CA  HA3  sing N N 211 
GLY C   O    doub N N 212 
GLY C   OXT  sing N N 213 
GLY OXT HXT  sing N N 214 
HIS N   CA   sing N N 215 
HIS N   H    sing N N 216 
HIS N   H2   sing N N 217 
HIS CA  C    sing N N 218 
HIS CA  CB   sing N N 219 
HIS CA  HA   sing N N 220 
HIS C   O    doub N N 221 
HIS C   OXT  sing N N 222 
HIS CB  CG   sing N N 223 
HIS CB  HB2  sing N N 224 
HIS CB  HB3  sing N N 225 
HIS CG  ND1  sing Y N 226 
HIS CG  CD2  doub Y N 227 
HIS ND1 CE1  doub Y N 228 
HIS ND1 HD1  sing N N 229 
HIS CD2 NE2  sing Y N 230 
HIS CD2 HD2  sing N N 231 
HIS CE1 NE2  sing Y N 232 
HIS CE1 HE1  sing N N 233 
HIS NE2 HE2  sing N N 234 
HIS OXT HXT  sing N N 235 
HOH O   H1   sing N N 236 
HOH O   H2   sing N N 237 
ILE N   CA   sing N N 238 
ILE N   H    sing N N 239 
ILE N   H2   sing N N 240 
ILE CA  C    sing N N 241 
ILE CA  CB   sing N N 242 
ILE CA  HA   sing N N 243 
ILE C   O    doub N N 244 
ILE C   OXT  sing N N 245 
ILE CB  CG1  sing N N 246 
ILE CB  CG2  sing N N 247 
ILE CB  HB   sing N N 248 
ILE CG1 CD1  sing N N 249 
ILE CG1 HG12 sing N N 250 
ILE CG1 HG13 sing N N 251 
ILE CG2 HG21 sing N N 252 
ILE CG2 HG22 sing N N 253 
ILE CG2 HG23 sing N N 254 
ILE CD1 HD11 sing N N 255 
ILE CD1 HD12 sing N N 256 
ILE CD1 HD13 sing N N 257 
ILE OXT HXT  sing N N 258 
LEU N   CA   sing N N 259 
LEU N   H    sing N N 260 
LEU N   H2   sing N N 261 
LEU CA  C    sing N N 262 
LEU CA  CB   sing N N 263 
LEU CA  HA   sing N N 264 
LEU C   O    doub N N 265 
LEU C   OXT  sing N N 266 
LEU CB  CG   sing N N 267 
LEU CB  HB2  sing N N 268 
LEU CB  HB3  sing N N 269 
LEU CG  CD1  sing N N 270 
LEU CG  CD2  sing N N 271 
LEU CG  HG   sing N N 272 
LEU CD1 HD11 sing N N 273 
LEU CD1 HD12 sing N N 274 
LEU CD1 HD13 sing N N 275 
LEU CD2 HD21 sing N N 276 
LEU CD2 HD22 sing N N 277 
LEU CD2 HD23 sing N N 278 
LEU OXT HXT  sing N N 279 
LYS N   CA   sing N N 280 
LYS N   H    sing N N 281 
LYS N   H2   sing N N 282 
LYS CA  C    sing N N 283 
LYS CA  CB   sing N N 284 
LYS CA  HA   sing N N 285 
LYS C   O    doub N N 286 
LYS C   OXT  sing N N 287 
LYS CB  CG   sing N N 288 
LYS CB  HB2  sing N N 289 
LYS CB  HB3  sing N N 290 
LYS CG  CD   sing N N 291 
LYS CG  HG2  sing N N 292 
LYS CG  HG3  sing N N 293 
LYS CD  CE   sing N N 294 
LYS CD  HD2  sing N N 295 
LYS CD  HD3  sing N N 296 
LYS CE  NZ   sing N N 297 
LYS CE  HE2  sing N N 298 
LYS CE  HE3  sing N N 299 
LYS NZ  HZ1  sing N N 300 
LYS NZ  HZ2  sing N N 301 
LYS NZ  HZ3  sing N N 302 
LYS OXT HXT  sing N N 303 
MET N   CA   sing N N 304 
MET N   H    sing N N 305 
MET N   H2   sing N N 306 
MET CA  C    sing N N 307 
MET CA  CB   sing N N 308 
MET CA  HA   sing N N 309 
MET C   O    doub N N 310 
MET C   OXT  sing N N 311 
MET CB  CG   sing N N 312 
MET CB  HB2  sing N N 313 
MET CB  HB3  sing N N 314 
MET CG  SD   sing N N 315 
MET CG  HG2  sing N N 316 
MET CG  HG3  sing N N 317 
MET SD  CE   sing N N 318 
MET CE  HE1  sing N N 319 
MET CE  HE2  sing N N 320 
MET CE  HE3  sing N N 321 
MET OXT HXT  sing N N 322 
PHE N   CA   sing N N 323 
PHE N   H    sing N N 324 
PHE N   H2   sing N N 325 
PHE CA  C    sing N N 326 
PHE CA  CB   sing N N 327 
PHE CA  HA   sing N N 328 
PHE C   O    doub N N 329 
PHE C   OXT  sing N N 330 
PHE CB  CG   sing N N 331 
PHE CB  HB2  sing N N 332 
PHE CB  HB3  sing N N 333 
PHE CG  CD1  doub Y N 334 
PHE CG  CD2  sing Y N 335 
PHE CD1 CE1  sing Y N 336 
PHE CD1 HD1  sing N N 337 
PHE CD2 CE2  doub Y N 338 
PHE CD2 HD2  sing N N 339 
PHE CE1 CZ   doub Y N 340 
PHE CE1 HE1  sing N N 341 
PHE CE2 CZ   sing Y N 342 
PHE CE2 HE2  sing N N 343 
PHE CZ  HZ   sing N N 344 
PHE OXT HXT  sing N N 345 
PRO N   CA   sing N N 346 
PRO N   CD   sing N N 347 
PRO N   H    sing N N 348 
PRO CA  C    sing N N 349 
PRO CA  CB   sing N N 350 
PRO CA  HA   sing N N 351 
PRO C   O    doub N N 352 
PRO C   OXT  sing N N 353 
PRO CB  CG   sing N N 354 
PRO CB  HB2  sing N N 355 
PRO CB  HB3  sing N N 356 
PRO CG  CD   sing N N 357 
PRO CG  HG2  sing N N 358 
PRO CG  HG3  sing N N 359 
PRO CD  HD2  sing N N 360 
PRO CD  HD3  sing N N 361 
PRO OXT HXT  sing N N 362 
SER N   CA   sing N N 363 
SER N   H    sing N N 364 
SER N   H2   sing N N 365 
SER CA  C    sing N N 366 
SER CA  CB   sing N N 367 
SER CA  HA   sing N N 368 
SER C   O    doub N N 369 
SER C   OXT  sing N N 370 
SER CB  OG   sing N N 371 
SER CB  HB2  sing N N 372 
SER CB  HB3  sing N N 373 
SER OG  HG   sing N N 374 
SER OXT HXT  sing N N 375 
THR N   CA   sing N N 376 
THR N   H    sing N N 377 
THR N   H2   sing N N 378 
THR CA  C    sing N N 379 
THR CA  CB   sing N N 380 
THR CA  HA   sing N N 381 
THR C   O    doub N N 382 
THR C   OXT  sing N N 383 
THR CB  OG1  sing N N 384 
THR CB  CG2  sing N N 385 
THR CB  HB   sing N N 386 
THR OG1 HG1  sing N N 387 
THR CG2 HG21 sing N N 388 
THR CG2 HG22 sing N N 389 
THR CG2 HG23 sing N N 390 
THR OXT HXT  sing N N 391 
TYR N   CA   sing N N 392 
TYR N   H    sing N N 393 
TYR N   H2   sing N N 394 
TYR CA  C    sing N N 395 
TYR CA  CB   sing N N 396 
TYR CA  HA   sing N N 397 
TYR C   O    doub N N 398 
TYR C   OXT  sing N N 399 
TYR CB  CG   sing N N 400 
TYR CB  HB2  sing N N 401 
TYR CB  HB3  sing N N 402 
TYR CG  CD1  doub Y N 403 
TYR CG  CD2  sing Y N 404 
TYR CD1 CE1  sing Y N 405 
TYR CD1 HD1  sing N N 406 
TYR CD2 CE2  doub Y N 407 
TYR CD2 HD2  sing N N 408 
TYR CE1 CZ   doub Y N 409 
TYR CE1 HE1  sing N N 410 
TYR CE2 CZ   sing Y N 411 
TYR CE2 HE2  sing N N 412 
TYR CZ  OH   sing N N 413 
TYR OH  HH   sing N N 414 
TYR OXT HXT  sing N N 415 
VAL N   CA   sing N N 416 
VAL N   H    sing N N 417 
VAL N   H2   sing N N 418 
VAL CA  C    sing N N 419 
VAL CA  CB   sing N N 420 
VAL CA  HA   sing N N 421 
VAL C   O    doub N N 422 
VAL C   OXT  sing N N 423 
VAL CB  CG1  sing N N 424 
VAL CB  CG2  sing N N 425 
VAL CB  HB   sing N N 426 
VAL CG1 HG11 sing N N 427 
VAL CG1 HG12 sing N N 428 
VAL CG1 HG13 sing N N 429 
VAL CG2 HG21 sing N N 430 
VAL CG2 HG22 sing N N 431 
VAL CG2 HG23 sing N N 432 
VAL OXT HXT  sing N N 433 
# 
_pdbx_audit_support.funding_organization   
'National Institutes of Health/National Institute Of Allergy and Infectious Diseases (NIH/NIAID)' 
_pdbx_audit_support.country                'United States' 
_pdbx_audit_support.grant_number           1F30AI181515-01 
_pdbx_audit_support.ordinal                1 
# 
_pdbx_initial_refinement_model.id               1 
_pdbx_initial_refinement_model.entity_id_list   ? 
_pdbx_initial_refinement_model.type             'experimental model' 
_pdbx_initial_refinement_model.source_name      PDB 
_pdbx_initial_refinement_model.accession_code   3ZVE 
_pdbx_initial_refinement_model.details          ? 
# 
_space_group.name_H-M_alt     'P 31 2 1' 
_space_group.name_Hall        
;P 31 2"
;
_space_group.IT_number        152 
_space_group.crystal_system   trigonal 
_space_group.id               1 
# 
_atom_sites.entry_id                    8W3C 
_atom_sites.Cartn_transf_matrix[1][1]   ? 
_atom_sites.Cartn_transf_matrix[1][2]   ? 
_atom_sites.Cartn_transf_matrix[1][3]   ? 
_atom_sites.Cartn_transf_matrix[2][1]   ? 
_atom_sites.Cartn_transf_matrix[2][2]   ? 
_atom_sites.Cartn_transf_matrix[2][3]   ? 
_atom_sites.Cartn_transf_matrix[3][1]   ? 
_atom_sites.Cartn_transf_matrix[3][2]   ? 
_atom_sites.Cartn_transf_matrix[3][3]   ? 
_atom_sites.Cartn_transf_vector[1]      ? 
_atom_sites.Cartn_transf_vector[2]      ? 
_atom_sites.Cartn_transf_vector[3]      ? 
_atom_sites.Cartn_transform_axes        ? 
_atom_sites.fract_transf_matrix[1][1]   0.017721 
_atom_sites.fract_transf_matrix[1][2]   0.010231 
_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]   0.020462 
_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]   0.005866 
_atom_sites.fract_transf_vector[1]      0.00000 
_atom_sites.fract_transf_vector[2]      0.00000 
_atom_sites.fract_transf_vector[3]      0.00000 
_atom_sites.solution_primary            ? 
_atom_sites.solution_secondary          ? 
_atom_sites.solution_hydrogens          ? 
_atom_sites.special_details             ? 
# 
loop_
_atom_type.symbol 
_atom_type.scat_dispersion_real 
_atom_type.scat_dispersion_imag 
_atom_type.scat_Cromer_Mann_a1 
_atom_type.scat_Cromer_Mann_a2 
_atom_type.scat_Cromer_Mann_a3 
_atom_type.scat_Cromer_Mann_a4 
_atom_type.scat_Cromer_Mann_b1 
_atom_type.scat_Cromer_Mann_b2 
_atom_type.scat_Cromer_Mann_b3 
_atom_type.scat_Cromer_Mann_b4 
_atom_type.scat_Cromer_Mann_c 
_atom_type.scat_source 
_atom_type.scat_dispersion_source 
C ? ? 3.54356 2.42580 ? ? 25.62398 1.50364  ? ? 0.0 
;2-Gaussian fit: Grosse-Kunstleve RW, Sauter NK, Adams PD: Newsletter of the IUCr Commission on Crystallographic Computing 2004, 3, 22-31.
;
? 
F ? ? 8.95735 ?       ? ? 7.27484  ?        ? ? 0.0 
;1-Gaussian fit: Grosse-Kunstleve RW, Sauter NK, Adams PD: Newsletter of the IUCr Commission on Crystallographic Computing 2004, 3, 22-31.
;
? 
H ? ? ?       ?       ? ? ?        ?        ? ? ?   ? ? 
N ? ? 4.01032 2.96436 ? ? 19.97189 1.75589  ? ? 0.0 
;2-Gaussian fit: Grosse-Kunstleve RW, Sauter NK, Adams PD: Newsletter of the IUCr Commission on Crystallographic Computing 2004, 3, 22-31.
;
? 
O ? ? 4.49882 3.47563 ? ? 15.80542 1.70748  ? ? 0.0 
;2-Gaussian fit: Grosse-Kunstleve RW, Sauter NK, Adams PD: Newsletter of the IUCr Commission on Crystallographic Computing 2004, 3, 22-31.
;
? 
S ? ? 9.55732 6.39887 ? ? 1.23737  29.19336 ? ? 0.0 
;2-Gaussian fit: Grosse-Kunstleve RW, Sauter NK, Adams PD: Newsletter of the IUCr Commission on Crystallographic Computing 2004, 3, 22-31.
;
? 
# 
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    . GLY A 1 1   ? -14.32551 39.23039 26.82661  1.000 72.70588  ? 1   GLY A N    1 
ATOM   2    C CA   . GLY A 1 1   ? -13.42610 38.08484 26.81173  1.000 71.14728  ? 1   GLY A CA   1 
ATOM   3    C C    . GLY A 1 1   ? -13.59131 37.20039 25.57468  1.000 68.85788  ? 1   GLY A C    1 
ATOM   4    O O    . GLY A 1 1   ? -13.84446 37.71202 24.47429  1.000 69.43594  ? 1   GLY A O    1 
ATOM   5    N N    . PRO A 1 2   ? -13.43651 35.88071 25.73981  1.000 65.86030  ? 2   PRO A N    1 
ATOM   6    C CA   . PRO A 1 2   ? -13.74367 34.94966 24.63984  1.000 62.81751  ? 2   PRO A CA   1 
ATOM   7    C C    . PRO A 1 2   ? -15.24886 34.73090 24.49743  1.000 61.43460  ? 2   PRO A C    1 
ATOM   8    O O    . PRO A 1 2   ? -16.01706 34.83005 25.46825  1.000 58.37848  ? 2   PRO A O    1 
ATOM   9    C CB   . PRO A 1 2   ? -13.03514 33.64710 25.05839  1.000 60.01728  ? 2   PRO A CB   1 
ATOM   10   C CG   . PRO A 1 2   ? -12.13803 34.02293 26.22887  1.000 57.47605  ? 2   PRO A CG   1 
ATOM   11   C CD   . PRO A 1 2   ? -12.78903 35.20774 26.87997  1.000 62.02333  ? 2   PRO A CD   1 
ATOM   12   N N    . GLY A 1 3   ? -15.66122 34.41307 23.26289  1.000 49.48576  ? 3   GLY A N    1 
ATOM   13   C CA   . GLY A 1 3   ? -17.07119 34.20764 22.93487  1.000 48.99494  ? 3   GLY A CA   1 
ATOM   14   C C    . GLY A 1 3   ? -17.61776 32.83123 23.29283  1.000 50.44444  ? 3   GLY A C    1 
ATOM   15   O O    . GLY A 1 3   ? -17.93882 32.02405 22.39881  1.000 39.86321  ? 3   GLY A O    1 
ATOM   16   N N    . PHE A 1 4   ? -17.76399 32.57982 24.60937  1.000 45.36838  ? 4   PHE A N    1 
ATOM   17   C CA   . PHE A 1 4   ? -18.20604 31.28311 25.11003  1.000 43.66573  ? 4   PHE A CA   1 
ATOM   18   C C    . PHE A 1 4   ? -19.65416 31.02551 24.75552  1.000 44.23088  ? 4   PHE A C    1 
ATOM   19   O O    . PHE A 1 4   ? -20.04534 29.88463 24.47406  1.000 44.71609  ? 4   PHE A O    1 
ATOM   20   C CB   . PHE A 1 4   ? -18.02688 31.21917 26.64328  1.000 49.44026  ? 4   PHE A CB   1 
ATOM   21   C CG   . PHE A 1 4   ? -16.59487 31.08295 27.06734  1.000 51.00215  ? 4   PHE A CG   1 
ATOM   22   C CD1  . PHE A 1 4   ? -15.91474 29.87216 26.87531  1.000 48.91602  ? 4   PHE A CD1  1 
ATOM   23   C CD2  . PHE A 1 4   ? -15.91276 32.15418 27.65447  1.000 51.94093  ? 4   PHE A CD2  1 
ATOM   24   C CE1  . PHE A 1 4   ? -14.56338 29.71799 27.24815  1.000 48.23878  ? 4   PHE A CE1  1 
ATOM   25   C CE2  . PHE A 1 4   ? -14.56201 32.01346 28.02725  1.000 55.39299  ? 4   PHE A CE2  1 
ATOM   26   C CZ   . PHE A 1 4   ? -13.88455 30.79186 27.79546  1.000 53.59294  ? 4   PHE A CZ   1 
ATOM   27   N N    . ASP A 1 5   ? -20.47317 32.06912 24.78914  1.000 42.28694  ? 5   ASP A N    1 
ATOM   28   C CA   . ASP A 1 5   ? -21.87447 31.90500 24.46487  1.000 43.51478  ? 5   ASP A CA   1 
ATOM   29   C C    . ASP A 1 5   ? -22.00824 31.45258 23.00661  1.000 46.54221  ? 5   ASP A C    1 
ATOM   30   O O    . ASP A 1 5   ? -22.77292 30.53240 22.68525  1.000 43.60436  ? 5   ASP A O    1 
ATOM   31   C CB   . ASP A 1 5   ? -22.55711 33.24135 24.66212  1.000 49.04545  ? 5   ASP A CB   1 
ATOM   32   C CG   . ASP A 1 5   ? -23.00538 33.44851 26.12411  1.000 57.92287  ? 5   ASP A CG   1 
ATOM   33   O OD1  . ASP A 1 5   ? -22.56544 32.66506 27.01623  1.000 61.27968  ? 5   ASP A OD1  1 
ATOM   34   O OD2  . ASP A 1 5   ? -23.74849 34.41915 26.37282  1.000 63.58507  ? 5   ASP A OD2  1 
ATOM   35   N N    . PHE A 1 6   ? -21.24805 32.07634 22.10829  1.000 43.66353  ? 6   PHE A N    1 
ATOM   36   C CA   . PHE A 1 6   ? -21.34068 31.68363 20.69420  1.000 43.52935  ? 6   PHE A CA   1 
ATOM   37   C C    . PHE A 1 6   ? -20.88568 30.24372 20.50521  1.000 41.85910  ? 6   PHE A C    1 
ATOM   38   O O    . PHE A 1 6   ? -21.54066 29.45324 19.81323  1.000 42.64329  ? 6   PHE A O    1 
ATOM   39   C CB   . PHE A 1 6   ? -20.50993 32.61767 19.81960  1.000 44.04809  ? 6   PHE A CB   1 
ATOM   40   C CG   . PHE A 1 6   ? -20.56707 32.28235 18.36162  1.000 44.44470  ? 6   PHE A CG   1 
ATOM   41   C CD1  . PHE A 1 6   ? -21.70683 32.54353 17.63701  1.000 46.09909  ? 6   PHE A CD1  1 
ATOM   42   C CD2  . PHE A 1 6   ? -19.49763 31.68293 17.73430  1.000 41.10328  ? 6   PHE A CD2  1 
ATOM   43   C CE1  . PHE A 1 6   ? -21.78776 32.24170 16.28866  1.000 44.23762  ? 6   PHE A CE1  1 
ATOM   44   C CE2  . PHE A 1 6   ? -19.57111 31.37144 16.34258  1.000 44.60624  ? 6   PHE A CE2  1 
ATOM   45   C CZ   . PHE A 1 6   ? -20.71919 31.65580 15.64537  1.000 45.91935  ? 6   PHE A CZ   1 
ATOM   46   N N    . ALA A 1 7   ? -19.75104 29.88371 21.11232  1.000 40.91626  ? 7   ALA A N    1 
ATOM   47   C CA   . ALA A 1 7   ? -19.23409 28.53341 20.93687  1.000 38.28978  ? 7   ALA A CA   1 
ATOM   48   C C    . ALA A 1 7   ? -20.22452 27.48447 21.43445  1.000 42.81034  ? 7   ALA A C    1 
ATOM   49   O O    . ALA A 1 7   ? -20.33436 26.39837 20.84950  1.000 39.91499  ? 7   ALA A O    1 
ATOM   50   C CB   . ALA A 1 7   ? -17.88159 28.41083 21.63327  1.000 40.57415  ? 7   ALA A CB   1 
ATOM   51   N N    . GLN A 1 8   ? -20.94823 27.78660 22.51548  1.000 44.94684  ? 8   GLN A N    1 
ATOM   52   C CA   . GLN A 1 8   ? -21.88908 26.83592 23.09097  1.000 44.34143  ? 8   GLN A CA   1 
ATOM   53   C C    . GLN A 1 8   ? -23.07083 26.58569 22.16151  1.000 42.03199  ? 8   GLN A C    1 
ATOM   54   O O    . GLN A 1 8   ? -23.54532 25.44727 22.02081  1.000 36.22161  ? 8   GLN A O    1 
ATOM   55   C CB   . GLN A 1 8   ? -22.39227 27.38998 24.42987  1.000 45.92741  ? 8   GLN A CB   1 
ATOM   56   C CG   . GLN A 1 8   ? -22.68527 26.32575 25.40640  1.000 52.19710  ? 8   GLN A CG   1 
ATOM   57   C CD   . GLN A 1 8   ? -23.01817 26.89080 26.77269  1.000 54.34305  ? 8   GLN A CD   1 
ATOM   58   O OE1  . GLN A 1 8   ? -22.92026 28.11264 27.02099  1.000 56.15968  ? 8   GLN A OE1  1 
ATOM   59   N NE2  . GLN A 1 8   ? -23.39255 26.00462 27.67284  1.000 58.45447  ? 8   GLN A NE2  1 
ATOM   60   N N    . ALA A 1 9   ? -23.63608 27.66354 21.62209  1.000 40.32874  ? 9   ALA A N    1 
ATOM   61   C CA   . ALA A 1 9   ? -24.71971 27.54862 20.65214  1.000 47.05632  ? 9   ALA A CA   1 
ATOM   62   C C    . ALA A 1 9   ? -24.30652 26.73990 19.42966  1.000 45.86504  ? 9   ALA A C    1 
ATOM   63   O O    . ALA A 1 9   ? -25.12250 26.00432 18.86006  1.000 47.18428  ? 9   ALA A O    1 
ATOM   64   C CB   . ALA A 1 9   ? -25.18176 28.94019 20.21936  1.000 48.41709  ? 9   ALA A CB   1 
ATOM   65   N N    . ILE A 1 10  ? -23.05803 26.87582 18.98569  1.000 45.90620  ? 10  ILE A N    1 
ATOM   66   C CA   . ILE A 1 10  ? -22.62662 26.06558 17.83988  1.000 41.37450  ? 10  ILE A CA   1 
ATOM   67   C C    . ILE A 1 10  ? -22.51953 24.60334 18.25208  1.000 45.38578  ? 10  ILE A C    1 
ATOM   68   O O    . ILE A 1 10  ? -22.89351 23.69168 17.50067  1.000 43.43597  ? 10  ILE A O    1 
ATOM   69   C CB   . ILE A 1 10  ? -21.28651 26.57489 17.25950  1.000 41.63137  ? 10  ILE A CB   1 
ATOM   70   C CG1  . ILE A 1 10  ? -21.41721 27.97419 16.61501  1.000 41.82028  ? 10  ILE A CG1  1 
ATOM   71   C CG2  . ILE A 1 10  ? -20.68240 25.51722 16.28786  1.000 41.94660  ? 10  ILE A CG2  1 
ATOM   72   C CD1  . ILE A 1 10  ? -22.29463 27.99198 15.28351  1.000 39.12292  ? 10  ILE A CD1  1 
ATOM   73   N N    . MET A 1 11  ? -22.04065 24.35494 19.46923  1.000 44.17282  ? 11  MET A N    1 
ATOM   74   C CA   . MET A 1 11  ? -21.82503 22.98363 19.91970  1.000 43.60652  ? 11  MET A CA   1 
ATOM   75   C C    . MET A 1 11  ? -23.15971 22.27129 20.07976  1.000 43.32664  ? 11  MET A C    1 
ATOM   76   O O    . MET A 1 11  ? -23.32070 21.11797 19.66350  1.000 44.57950  ? 11  MET A O    1 
ATOM   77   C CB   . MET A 1 11  ? -21.05748 23.02315 21.24820  1.000 43.30930  ? 11  MET A CB   1 
ATOM   78   C CG   . MET A 1 11  ? -19.54161 23.28311 21.10891  1.000 44.58311  ? 11  MET A CG   1 
ATOM   79   S SD   . MET A 1 11  ? -18.69393 22.78048 19.53876  1.000 55.12473  ? 11  MET A SD   1 
ATOM   80   C CE   . MET A 1 11  ? -18.15925 21.21035 20.30711  1.000 46.53174  ? 11  MET A CE   1 
ATOM   81   N N    . LYS A 1 12  ? -24.12168 22.96905 20.68339  1.000 47.11536  ? 12  LYS A N    1 
ATOM   82   C CA   . LYS A 1 12  ? -25.42982 22.41477 20.99280  1.000 48.01835  ? 12  LYS A CA   1 
ATOM   83   C C    . LYS A 1 12  ? -26.13575 21.90074 19.75389  1.000 50.96547  ? 12  LYS A C    1 
ATOM   84   O O    . LYS A 1 12  ? -26.67803 20.79026 19.75364  1.000 52.94781  ? 12  LYS A O    1 
ATOM   85   C CB   . LYS A 1 12  ? -26.27573 23.48790 21.64719  1.000 49.40520  ? 12  LYS A CB   1 
ATOM   86   C CG   . LYS A 1 12  ? -27.58580 22.95431 22.17729  1.000 58.88808  ? 12  LYS A CG   1 
ATOM   87   C CD   . LYS A 1 12  ? -28.66651 24.04083 22.15095  1.000 67.39827  ? 12  LYS A CD   1 
ATOM   88   C CE   . LYS A 1 12  ? -29.44842 24.05260 23.47046  1.000 82.12054  ? 12  LYS A CE   1 
ATOM   89   N NZ   . LYS A 1 12  ? -30.76226 24.75022 23.34045  1.000 86.98536  ? 12  LYS A NZ   1 
ATOM   90   N N    . LYS A 1 13  ? -26.15198 22.69931 18.68527  1.000 50.95294  ? 13  LYS A N    1 
ATOM   91   C CA   . LYS A 1 13  ? -26.99241 22.41061 17.52786  1.000 51.39293  ? 13  LYS A CA   1 
ATOM   92   C C    . LYS A 1 13  ? -26.21516 21.87170 16.34439  1.000 50.53297  ? 13  LYS A C    1 
ATOM   93   O O    . LYS A 1 13  ? -26.82496 21.33511 15.41295  1.000 54.22469  ? 13  LYS A O    1 
ATOM   94   C CB   . LYS A 1 13  ? -27.73226 23.68404 17.11320  1.000 54.27918  ? 13  LYS A CB   1 
ATOM   95   C CG   . LYS A 1 13  ? -28.92055 23.98079 18.00576  1.000 58.80531  ? 13  LYS A CG   1 
ATOM   96   C CD   . LYS A 1 13  ? -29.65298 25.22356 17.52978  1.000 63.49069  ? 13  LYS A CD   1 
ATOM   97   C CE   . LYS A 1 13  ? -30.34164 25.92414 18.69758  1.000 70.83677  ? 13  LYS A CE   1 
ATOM   98   N NZ   . LYS A 1 13  ? -29.84535 27.33949 18.78087  1.000 70.20516  ? 13  LYS A NZ   1 
ATOM   99   N N    . ASN A 1 14  ? -24.88876 21.99634 16.33665  1.000 46.23335  ? 14  ASN A N    1 
ATOM   100  C CA   . ASN A 1 14  ? -24.15960 21.69149 15.11001  1.000 45.53651  ? 14  ASN A CA   1 
ATOM   101  C C    . ASN A 1 14  ? -22.96620 20.77555 15.33106  1.000 45.59821  ? 14  ASN A C    1 
ATOM   102  O O    . ASN A 1 14  ? -22.04091 20.77901 14.51144  1.000 41.62184  ? 14  ASN A O    1 
ATOM   103  C CB   . ASN A 1 14  ? -23.68964 22.97294 14.43467  1.000 44.60051  ? 14  ASN A CB   1 
ATOM   104  C CG   . ASN A 1 14  ? -24.79619 23.67801 13.73215  1.000 47.78857  ? 14  ASN A CG   1 
ATOM   105  O OD1  . ASN A 1 14  ? -25.56242 24.39590 14.35903  1.000 45.47838  ? 14  ASN A OD1  1 
ATOM   106  N ND2  . ASN A 1 14  ? -24.91712 23.45291 12.40127  1.000 42.87508  ? 14  ASN A ND2  1 
ATOM   107  N N    . THR A 1 15  ? -22.91003 20.03096 16.43819  1.000 40.53597  ? 15  THR A N    1 
ATOM   108  C CA   . THR A 1 15  ? -21.84543 19.05890 16.54785  1.000 38.10150  ? 15  THR A CA   1 
ATOM   109  C C    . THR A 1 15  ? -22.39523 17.68836 16.88636  1.000 42.78931  ? 15  THR A C    1 
ATOM   110  O O    . THR A 1 15  ? -23.45309 17.54215 17.52148  1.000 45.51251  ? 15  THR A O    1 
ATOM   111  C CB   . THR A 1 15  ? -20.79415 19.49654 17.56363  1.000 45.33074  ? 15  THR A CB   1 
ATOM   112  O OG1  . THR A 1 15  ? -21.37141 19.59787 18.88679  1.000 41.67809  ? 15  THR A OG1  1 
ATOM   113  C CG2  . THR A 1 15  ? -20.24646 20.87069 17.15413  1.000 42.01512  ? 15  THR A CG2  1 
ATOM   114  N N    . VAL A 1 16  ? -21.62414 16.68439 16.48302  1.000 38.94431  ? 16  VAL A N    1 
ATOM   115  C CA   . VAL A 1 16  ? -21.92853 15.29038 16.74583  1.000 40.31895  ? 16  VAL A CA   1 
ATOM   116  C C    . VAL A 1 16  ? -20.60047 14.59024 16.99359  1.000 43.57420  ? 16  VAL A C    1 
ATOM   117  O O    . VAL A 1 16  ? -19.54057 15.06571 16.57614  1.000 41.34451  ? 16  VAL A O    1 
ATOM   118  C CB   . VAL A 1 16  ? -22.69362 14.62080 15.57169  1.000 43.08741  ? 16  VAL A CB   1 
ATOM   119  C CG1  . VAL A 1 16  ? -24.02341 15.34648 15.30863  1.000 44.84633  ? 16  VAL A CG1  1 
ATOM   120  C CG2  . VAL A 1 16  ? -21.80979 14.53191 14.28799  1.000 42.63885  ? 16  VAL A CG2  1 
ATOM   121  N N    . VAL A 1 17  ? -20.66520 13.45397 17.69525  1.000 41.12676  ? 17  VAL A N    1 
ATOM   122  C CA   . VAL A 1 17  ? -19.52067 12.55369 17.82673  1.000 42.03827  ? 17  VAL A CA   1 
ATOM   123  C C    . VAL A 1 17  ? -19.44403 11.66612 16.59402  1.000 43.76601  ? 17  VAL A C    1 
ATOM   124  O O    . VAL A 1 17  ? -20.37952 10.90753 16.32417  1.000 42.48368  ? 17  VAL A O    1 
ATOM   125  C CB   . VAL A 1 17  ? -19.64291 11.69390 19.09528  1.000 42.83562  ? 17  VAL A CB   1 
ATOM   126  C CG1  . VAL A 1 17  ? -18.40220 10.82855 19.25218  1.000 43.58047  ? 17  VAL A CG1  1 
ATOM   127  C CG2  . VAL A 1 17  ? -19.83364 12.58771 20.32408  1.000 45.03046  ? 17  VAL A CG2  1 
ATOM   128  N N    . ALA A 1 18  ? -18.31637 11.70948 15.87831  1.000 43.01010  ? 18  ALA A N    1 
ATOM   129  C CA   . ALA A 1 18  ? -18.11111 10.87451 14.70056  1.000 44.13007  ? 18  ALA A CA   1 
ATOM   130  C C    . ALA A 1 18  ? -17.01956 9.86913  15.01521  1.000 46.50256  ? 18  ALA A C    1 
ATOM   131  O O    . ALA A 1 18  ? -16.03898 10.20549 15.68112  1.000 46.30165  ? 18  ALA A O    1 
ATOM   132  C CB   . ALA A 1 18  ? -17.71452 11.69518 13.45487  1.000 42.58775  ? 18  ALA A CB   1 
ATOM   133  N N    . ARG A 1 19  ? -17.19328 8.63872  14.53595  1.000 44.15638  ? 19  ARG A N    1 
ATOM   134  C CA   . ARG A 1 19  ? -16.25731 7.56315  14.82681  1.000 47.80465  ? 19  ARG A CA   1 
ATOM   135  C C    . ARG A 1 19  ? -16.02974 6.76861  13.55205  1.000 45.27395  ? 19  ARG A C    1 
ATOM   136  O O    . ARG A 1 19  ? -16.98668 6.27281  12.93499  1.000 45.70706  ? 19  ARG A O    1 
ATOM   137  C CB   . ARG A 1 19  ? -16.76083 6.65709  15.95851  1.000 46.03321  ? 19  ARG A CB   1 
ATOM   138  C CG   . ARG A 1 19  ? -15.92333 5.37373  16.14720  1.000 49.96054  ? 19  ARG A CG   1 
ATOM   139  C CD   . ARG A 1 19  ? -16.12721 4.76139  17.54891  1.000 51.89713  ? 19  ARG A CD   1 
ATOM   140  N NE   . ARG A 1 19  ? -17.54695 4.54355  17.81579  1.000 53.75989  ? 19  ARG A NE   1 
ATOM   141  C CZ   . ARG A 1 19  ? -18.20655 3.42383  17.54327  1.000 54.26721  ? 19  ARG A CZ   1 
ATOM   142  N NH1  . ARG A 1 19  ? -17.59553 2.37482  17.01832  1.000 57.88407  ? 19  ARG A NH1  1 
ATOM   143  N NH2  . ARG A 1 19  ? -19.51409 3.35753  17.80261  1.000 54.52740  ? 19  ARG A NH2  1 
ATOM   144  N N    . THR A 1 20  ? -14.76243 6.70470  13.15074  1.000 44.12716  ? 20  THR A N    1 
ATOM   145  C CA   . THR A 1 20  ? -14.25396 5.93759  12.03091  1.000 50.31532  ? 20  THR A CA   1 
ATOM   146  C C    . THR A 1 20  ? -13.31214 4.90039  12.62132  1.000 52.69743  ? 20  THR A C    1 
ATOM   147  O O    . THR A 1 20  ? -13.19140 4.77560  13.84753  1.000 50.04089  ? 20  THR A O    1 
ATOM   148  C CB   . THR A 1 20  ? -13.52603 6.82953  11.02322  1.000 48.87463  ? 20  THR A CB   1 
ATOM   149  O OG1  . THR A 1 20  ? -12.27811 7.25476  11.59472  1.000 47.62121  ? 20  THR A OG1  1 
ATOM   150  C CG2  . THR A 1 20  ? -14.35892 8.04705  10.67895  1.000 43.84708  ? 20  THR A CG2  1 
ATOM   151  N N    . GLU A 1 21  ? -12.62524 4.17175  11.74690  1.000 51.40212  ? 21  GLU A N    1 
ATOM   152  C CA   . GLU A 1 21  ? -11.65922 3.19760  12.23321  1.000 55.53518  ? 21  GLU A CA   1 
ATOM   153  C C    . GLU A 1 21  ? -10.41965 3.86585  12.79187  1.000 55.79403  ? 21  GLU A C    1 
ATOM   154  O O    . GLU A 1 21  ? -9.61438  3.19327  13.44000  1.000 58.65762  ? 21  GLU A O    1 
ATOM   155  C CB   . GLU A 1 21  ? -11.28267 2.22259  11.11149  1.000 61.16892  ? 21  GLU A CB   1 
ATOM   156  C CG   . GLU A 1 21  ? -10.01101 2.57433  10.30977  1.000 65.45040  ? 21  GLU A CG   1 
ATOM   157  C CD   . GLU A 1 21  ? -10.30118 3.24477  8.95632   1.000 69.25617  ? 21  GLU A CD   1 
ATOM   158  O OE1  . GLU A 1 21  ? -9.65646  2.85758  7.93188   1.000 67.25529  ? 21  GLU A OE1  1 
ATOM   159  O OE2  . GLU A 1 21  ? -11.12234 4.21185  8.94334   1.000 65.88261  ? 21  GLU A OE2  1 
ATOM   160  N N    . LYS A 1 22  ? -10.26991 5.17424  12.59781  1.000 52.78091  ? 22  LYS A N    1 
ATOM   161  C CA   . LYS A 1 22  ? -9.11909  5.87436  13.14026  1.000 52.35924  ? 22  LYS A CA   1 
ATOM   162  C C    . LYS A 1 22  ? -9.37500  6.37895  14.55358  1.000 54.81253  ? 22  LYS A C    1 
ATOM   163  O O    . LYS A 1 22  ? -8.43661  6.82953  15.21668  1.000 54.19907  ? 22  LYS A O    1 
ATOM   164  C CB   . LYS A 1 22  ? -8.76221  7.06089  12.25596  1.000 52.63192  ? 22  LYS A CB   1 
ATOM   165  C CG   . LYS A 1 22  ? -8.13685  6.70913  10.86859  1.000 56.56451  ? 22  LYS A CG   1 
ATOM   166  C CD   . LYS A 1 22  ? -6.76577  6.03566  10.87809  1.000 61.90542  ? 22  LYS A CD   1 
ATOM   167  C CE   . LYS A 1 22  ? -6.69667  4.86380  9.86828   1.000 64.17703  ? 22  LYS A CE   1 
ATOM   168  N NZ   . LYS A 1 22  ? -5.81844  3.71533  10.26948  1.000 71.04530  ? 22  LYS A NZ   1 
ATOM   169  N N    . GLY A 1 23  ? -10.62053 6.34833  15.01663  1.000 50.36690  ? 23  GLY A N    1 
ATOM   170  C CA   . GLY A 1 23  ? -10.94285 6.80094  16.34538  1.000 51.57443  ? 23  GLY A CA   1 
ATOM   171  C C    . GLY A 1 23  ? -12.12904 7.74619  16.33786  1.000 50.26758  ? 23  GLY A C    1 
ATOM   172  O O    . GLY A 1 23  ? -12.92716 7.78893  15.39161  1.000 50.17851  ? 23  GLY A O    1 
ATOM   173  N N    . GLU A 1 24  ? -12.24074 8.51672  17.40244  1.000 49.15337  ? 24  GLU A N    1 
ATOM   174  C CA   . GLU A 1 24  ? -13.35218 9.43269  17.55650  1.000 47.09055  ? 24  GLU A CA   1 
ATOM   175  C C    . GLU A 1 24  ? -12.87877 10.83949 17.24916  1.000 47.08508  ? 24  GLU A C    1 
ATOM   176  O O    . GLU A 1 24  ? -11.72030 11.18645 17.50482  1.000 49.06770  ? 24  GLU A O    1 
ATOM   177  C CB   . GLU A 1 24  ? -13.91173 9.36749  18.96577  1.000 49.40568  ? 24  GLU A CB   1 
ATOM   178  C CG   . GLU A 1 24  ? -15.30618 8.80085  18.98150  1.000 51.74843  ? 24  GLU A CG   1 
ATOM   179  C CD   . GLU A 1 24  ? -15.86763 8.71069  20.38518  1.000 49.55010  ? 24  GLU A CD   1 
ATOM   180  O OE1  . GLU A 1 24  ? -15.50967 9.56385  21.24053  1.000 47.81522  ? 24  GLU A OE1  1 
ATOM   181  O OE2  . GLU A 1 24  ? -16.66241 7.77628  20.62090  1.000 53.38288  ? 24  GLU A OE2  1 
ATOM   182  N N    . PHE A 1 25  ? -13.79170 11.64457 16.69593  1.000 41.38910  ? 25  PHE A N    1 
ATOM   183  C CA   . PHE A 1 25  ? -13.52170 13.01663 16.30536  1.000 40.68843  ? 25  PHE A CA   1 
ATOM   184  C C    . PHE A 1 25  ? -14.76633 13.82436 16.59660  1.000 40.43211  ? 25  PHE A C    1 
ATOM   185  O O    . PHE A 1 25  ? -15.88535 13.33529 16.38099  1.000 42.31782  ? 25  PHE A O    1 
ATOM   186  C CB   . PHE A 1 25  ? -13.18400 13.10762 14.77815  1.000 44.05710  ? 25  PHE A CB   1 
ATOM   187  C CG   . PHE A 1 25  ? -11.98547 12.30485 14.38498  1.000 45.64133  ? 25  PHE A CG   1 
ATOM   188  C CD1  . PHE A 1 25  ? -12.09103 10.92945 14.17784  1.000 44.52934  ? 25  PHE A CD1  1 
ATOM   189  C CD2  . PHE A 1 25  ? -10.74447 12.91705 14.22962  1.000 45.29412  ? 25  PHE A CD2  1 
ATOM   190  C CE1  . PHE A 1 25  ? -10.99406 10.16960 13.85596  1.000 46.94720  ? 25  PHE A CE1  1 
ATOM   191  C CE2  . PHE A 1 25  ? -9.62195  12.16967 13.87992  1.000 47.32199  ? 25  PHE A CE2  1 
ATOM   192  C CZ   . PHE A 1 25  ? -9.74644  10.78368 13.69667  1.000 49.86340  ? 25  PHE A CZ   1 
ATOM   193  N N    . THR A 1 26  ? -14.57848 15.06452 17.05123  1.000 39.61848  ? 26  THR A N    1 
ATOM   194  C CA   . THR A 1 26  ? -15.65431 16.05020 16.96489  1.000 38.88796  ? 26  THR A CA   1 
ATOM   195  C C    . THR A 1 26  ? -16.00224 16.29972 15.49495  1.000 40.74420  ? 26  THR A C    1 
ATOM   196  O O    . THR A 1 26  ? -15.10807 16.47432 14.66402  1.000 39.77557  ? 26  THR A O    1 
ATOM   197  C CB   . THR A 1 26  ? -15.20761 17.35096 17.59736  1.000 39.34274  ? 26  THR A CB   1 
ATOM   198  O OG1  . THR A 1 26  ? -14.88874 17.12102 19.00130  1.000 42.89279  ? 26  THR A OG1  1 
ATOM   199  C CG2  . THR A 1 26  ? -16.33025 18.37228 17.51073  1.000 39.63977  ? 26  THR A CG2  1 
ATOM   200  N N    . MET A 1 27  ? -17.29872 16.35451 15.16266  1.000 39.46635  ? 27  MET A N    1 
ATOM   201  C CA   . MET A 1 27  ? -17.67863 16.59674 13.76789  1.000 40.23664  ? 27  MET A CA   1 
ATOM   202  C C    . MET A 1 27  ? -18.64556 17.77547 13.71206  1.000 41.44996  ? 27  MET A C    1 
ATOM   203  O O    . MET A 1 27  ? -19.64748 17.80414 14.43866  1.000 39.16543  ? 27  MET A O    1 
ATOM   204  C CB   . MET A 1 27  ? -18.30846 15.35680 13.13000  1.000 42.25106  ? 27  MET A CB   1 
ATOM   205  C CG   . MET A 1 27  ? -19.39692 15.65642 12.06628  1.000 41.76626  ? 27  MET A CG   1 
ATOM   206  S SD   . MET A 1 27  ? -19.97012 14.19767 11.17657  1.000 45.08129  ? 27  MET A SD   1 
ATOM   207  C CE   . MET A 1 27  ? -18.48841 13.55537 10.42270  1.000 45.26717  ? 27  MET A CE   1 
ATOM   208  N N    . LEU A 1 28  ? -18.31845 18.77555 12.89073  1.000 36.74078  ? 28  LEU A N    1 
ATOM   209  C CA   . LEU A 1 28  ? -19.15473 19.97054 12.76264  1.000 35.83410  ? 28  LEU A CA   1 
ATOM   210  C C    . LEU A 1 28  ? -20.14495 19.77242 11.62612  1.000 41.68697  ? 28  LEU A C    1 
ATOM   211  O O    . LEU A 1 28  ? -19.73830 19.56199 10.48315  1.000 39.78991  ? 28  LEU A O    1 
ATOM   212  C CB   . LEU A 1 28  ? -18.29058 21.20317 12.48053  1.000 37.90838  ? 28  LEU A CB   1 
ATOM   213  C CG   . LEU A 1 28  ? -19.02376 22.51271 12.22504  1.000 39.15574  ? 28  LEU A CG   1 
ATOM   214  C CD1  . LEU A 1 28  ? -19.52470 23.07818 13.59788  1.000 40.15766  ? 28  LEU A CD1  1 
ATOM   215  C CD2  . LEU A 1 28  ? -18.08001 23.51551 11.56717  1.000 38.79776  ? 28  LEU A CD2  1 
ATOM   216  N N    . GLY A 1 29  ? -21.44078 19.87363 11.91082  1.000 41.52565  ? 29  GLY A N    1 
ATOM   217  C CA   . GLY A 1 29  ? -22.42997 19.86907 10.85314  1.000 41.57989  ? 29  GLY A CA   1 
ATOM   218  C C    . GLY A 1 29  ? -22.60870 21.29074 10.36163  1.000 43.91407  ? 29  GLY A C    1 
ATOM   219  O O    . GLY A 1 29  ? -22.69782 22.22258 11.16224  1.000 40.03243  ? 29  GLY A O    1 
ATOM   220  N N    . VAL A 1 30  ? -22.64774 21.46251 9.03421   1.000 40.39161  ? 30  VAL A N    1 
ATOM   221  C CA   . VAL A 1 30  ? -22.62291 22.77812 8.42045   1.000 40.47727  ? 30  VAL A CA   1 
ATOM   222  C C    . VAL A 1 30  ? -23.99625 23.18179 7.88303   1.000 43.23029  ? 30  VAL A C    1 
ATOM   223  O O    . VAL A 1 30  ? -24.44704 24.31276 8.08906   1.000 39.92281  ? 30  VAL A O    1 
ATOM   224  C CB   . VAL A 1 30  ? -21.53883 22.84190 7.32203   1.000 43.90816  ? 30  VAL A CB   1 
ATOM   225  C CG1  . VAL A 1 30  ? -21.52734 24.21173 6.67135   1.000 42.76939  ? 30  VAL A CG1  1 
ATOM   226  C CG2  . VAL A 1 30  ? -20.18566 22.55220 7.98008   1.000 41.83890  ? 30  VAL A CG2  1 
ATOM   227  N N    . HIS A 1 31  ? -24.67306 22.27685 7.18204   1.000 45.89173  ? 31  HIS A N    1 
ATOM   228  C CA   . HIS A 1 31  ? -26.01715 22.57818 6.70042   1.000 45.60966  ? 31  HIS A CA   1 
ATOM   229  C C    . HIS A 1 31  ? -26.62724 21.29098 6.17709   1.000 45.30892  ? 31  HIS A C    1 
ATOM   230  O O    . HIS A 1 31  ? -25.90963 20.37033 5.80138   1.000 44.48309  ? 31  HIS A O    1 
ATOM   231  C CB   . HIS A 1 31  ? -26.00737 23.64600 5.59447   1.000 45.65197  ? 31  HIS A CB   1 
ATOM   232  C CG   . HIS A 1 31  ? -25.46352 23.14613 4.29731   1.000 46.87003  ? 31  HIS A CG   1 
ATOM   233  N ND1  . HIS A 1 31  ? -26.27386 22.74016 3.25816   1.000 48.93881  ? 31  HIS A ND1  1 
ATOM   234  C CD2  . HIS A 1 31  ? -24.18967 22.97313 3.87313   1.000 44.63788  ? 31  HIS A CD2  1 
ATOM   235  C CE1  . HIS A 1 31  ? -25.52296 22.33245 2.25340   1.000 46.87264  ? 31  HIS A CE1  1 
ATOM   236  N NE2  . HIS A 1 31  ? -24.25479 22.45767 2.60208   1.000 46.66789  ? 31  HIS A NE2  1 
ATOM   237  N N    . ASP A 1 32  ? -27.95327 21.23232 6.17235   1.000 47.70601  ? 32  ASP A N    1 
ATOM   238  C CA   . ASP A 1 32  ? -28.67018 20.06488 5.67620   1.000 50.56382  ? 32  ASP A CA   1 
ATOM   239  C C    . ASP A 1 32  ? -28.10676 18.78676 6.27463   1.000 48.12956  ? 32  ASP A C    1 
ATOM   240  O O    . ASP A 1 32  ? -28.20061 18.59156 7.48584   1.000 50.25234  ? 32  ASP A O    1 
ATOM   241  C CB   . ASP A 1 32  ? -28.64890 20.04220 4.14164   1.000 48.34105  ? 32  ASP A CB   1 
ATOM   242  C CG   . ASP A 1 32  ? -29.48007 21.16701 3.57018   1.000 55.19157  ? 32  ASP A CG   1 
ATOM   243  O OD1  . ASP A 1 32  ? -30.72375 21.03360 3.54690   1.000 62.57131  ? 32  ASP A OD1  1 
ATOM   244  O OD2  . ASP A 1 32  ? -28.90504 22.19867 3.15019   1.000 55.90941  ? 32  ASP A OD2  1 
ATOM   245  N N    . ARG A 1 33  ? -27.52093 17.90061 5.47856   1.000 46.73838  ? 33  ARG A N    1 
ATOM   246  C CA   . ARG A 1 33  ? -26.90432 16.72014 6.07235   1.000 44.21718  ? 33  ARG A CA   1 
ATOM   247  C C    . ARG A 1 33  ? -25.41552 16.67561 5.77159   1.000 41.22482  ? 33  ARG A C    1 
ATOM   248  O O    . ARG A 1 33  ? -24.80782 15.60022 5.71759   1.000 40.97224  ? 33  ARG A O    1 
ATOM   249  C CB   . ARG A 1 33  ? -27.60388 15.43403 5.63362   1.000 45.08128  ? 33  ARG A CB   1 
ATOM   250  C CG   . ARG A 1 33  ? -28.88712 15.13890 6.42418   1.000 49.32816  ? 33  ARG A CG   1 
ATOM   251  C CD   . ARG A 1 33  ? -30.08092 15.17797 5.50740   1.000 51.16994  ? 33  ARG A CD   1 
ATOM   252  N NE   . ARG A 1 33  ? -31.36744 15.06994 6.18523   1.000 52.76589  ? 33  ARG A NE   1 
ATOM   253  C CZ   . ARG A 1 33  ? -32.48660 15.58013 5.68899   1.000 53.95336  ? 33  ARG A CZ   1 
ATOM   254  N NH1  . ARG A 1 33  ? -32.48563 16.26926 4.55999   1.000 55.69826  ? 33  ARG A NH1  1 
ATOM   255  N NH2  . ARG A 1 33  ? -33.63779 15.36412 6.31708   1.000 51.77285  ? 33  ARG A NH2  1 
ATOM   256  N N    . VAL A 1 34  ? -24.81260 17.85048 5.60158   1.000 43.05464  ? 34  VAL A N    1 
ATOM   257  C CA   . VAL A 1 34  ? -23.40407 17.99430 5.22067   1.000 43.33039  ? 34  VAL A CA   1 
ATOM   258  C C    . VAL A 1 34  ? -22.61093 18.43582 6.45247   1.000 40.87438  ? 34  VAL A C    1 
ATOM   259  O O    . VAL A 1 34  ? -22.99154 19.40800 7.11899   1.000 38.09152  ? 34  VAL A O    1 
ATOM   260  C CB   . VAL A 1 34  ? -23.24901 19.01062 4.07904   1.000 41.58012  ? 34  VAL A CB   1 
ATOM   261  C CG1  . VAL A 1 34  ? -21.78292 19.38306 3.85406   1.000 41.80108  ? 34  VAL A CG1  1 
ATOM   262  C CG2  . VAL A 1 34  ? -23.91513 18.45939 2.75428   1.000 43.16278  ? 34  VAL A CG2  1 
ATOM   263  N N    . ALA A 1 35  ? -21.48485 17.75784 6.70575   1.000 39.60090  ? 35  ALA A N    1 
ATOM   264  C CA   . ALA A 1 35  ? -20.63024 17.97507 7.87530   1.000 41.61758  ? 35  ALA A CA   1 
ATOM   265  C C    . ALA A 1 35  ? -19.17379 17.93387 7.41883   1.000 42.00741  ? 35  ALA A C    1 
ATOM   266  O O    . ALA A 1 35  ? -18.87454 17.64464 6.25262   1.000 42.85685  ? 35  ALA A O    1 
ATOM   267  C CB   . ALA A 1 35  ? -20.87586 16.91986 8.95613   1.000 38.01121  ? 35  ALA A CB   1 
ATOM   268  N N    . VAL A 1 36  ? -18.27054 18.27442 8.32430   1.000 39.64756  ? 36  VAL A N    1 
ATOM   269  C CA   . VAL A 1 36  ? -16.83736 18.22784 8.06906   1.000 35.38425  ? 36  VAL A CA   1 
ATOM   270  C C    . VAL A 1 36  ? -16.13163 17.38130 9.11469   1.000 42.45543  ? 36  VAL A C    1 
ATOM   271  O O    . VAL A 1 36  ? -16.54962 17.27158 10.28245  1.000 41.16124  ? 36  VAL A O    1 
ATOM   272  C CB   . VAL A 1 36  ? -16.17115 19.63375 8.01175   1.000 38.36187  ? 36  VAL A CB   1 
ATOM   273  C CG1  . VAL A 1 36  ? -16.59217 20.43656 6.79700   1.000 38.78760  ? 36  VAL A CG1  1 
ATOM   274  C CG2  . VAL A 1 36  ? -16.35580 20.44475 9.35657   1.000 38.96923  ? 36  VAL A CG2  1 
ATOM   275  N N    . ILE A 1 37  ? -15.00151 16.82739 8.69550   1.000 42.12528  ? 37  ILE A N    1 
ATOM   276  C CA   . ILE A 1 37  ? -14.16951 16.04678 9.60770   1.000 43.75844  ? 37  ILE A CA   1 
ATOM   277  C C    . ILE A 1 37  ? -12.73014 16.08457 9.10184   1.000 42.07766  ? 37  ILE A C    1 
ATOM   278  O O    . ILE A 1 37  ? -12.51805 16.16234 7.87701   1.000 45.08224  ? 37  ILE A O    1 
ATOM   279  C CB   . ILE A 1 37  ? -14.68898 14.60504 9.70602   1.000 44.06119  ? 37  ILE A CB   1 
ATOM   280  C CG1  . ILE A 1 37  ? -13.99173 13.86879 10.86545  1.000 45.34093  ? 37  ILE A CG1  1 
ATOM   281  C CG2  . ILE A 1 37  ? -14.53725 13.91744 8.35736   1.000 42.94937  ? 37  ILE A CG2  1 
ATOM   282  C CD1  . ILE A 1 37  ? -14.52429 12.48019 11.16343  1.000 45.13557  ? 37  ILE A CD1  1 
ATOM   283  N N    . PRO A 1 38  ? -11.72407 16.06810 9.97907   1.000 40.77885  ? 38  PRO A N    1 
ATOM   284  C CA   . PRO A 1 38  ? -10.32910 16.00699 9.51008   1.000 40.18999  ? 38  PRO A CA   1 
ATOM   285  C C    . PRO A 1 38  ? -10.11404 14.85062 8.54164   1.000 45.89038  ? 38  PRO A C    1 
ATOM   286  O O    . PRO A 1 38  ? -10.57378 13.72448 8.77606   1.000 43.09338  ? 38  PRO A O    1 
ATOM   287  C CB   . PRO A 1 38  ? -9.52824  15.81557 10.80428  1.000 44.63062  ? 38  PRO A CB   1 
ATOM   288  C CG   . PRO A 1 38  ? -10.39213 16.39818 11.86848  1.000 38.15748  ? 38  PRO A CG   1 
ATOM   289  C CD   . PRO A 1 38  ? -11.81451 16.12492 11.45718  1.000 40.81974  ? 38  PRO A CD   1 
ATOM   290  N N    . THR A 1 39  ? -9.41005  15.13742 7.42604   1.000 45.48648  ? 39  THR A N    1 
ATOM   291  C CA   . THR A 1 39  ? -9.11861  14.08612 6.45468   1.000 45.13343  ? 39  THR A CA   1 
ATOM   292  C C    . THR A 1 39  ? -8.35701  12.91696 7.07301   1.000 47.59193  ? 39  THR A C    1 
ATOM   293  O O    . THR A 1 39  ? -8.47292  11.78841 6.59085   1.000 46.35808  ? 39  THR A O    1 
ATOM   294  C CB   . THR A 1 39  ? -8.32045  14.64685 5.27258   1.000 46.66503  ? 39  THR A CB   1 
ATOM   295  O OG1  . THR A 1 39  ? -9.05089  15.72028 4.67178   1.000 44.33556  ? 39  THR A OG1  1 
ATOM   296  C CG2  . THR A 1 39  ? -8.06145  13.55416 4.23667   1.000 43.77369  ? 39  THR A CG2  1 
ATOM   297  N N    . HIS A 1 40  ? -7.55113  13.16010 8.11203   1.000 49.73987  ? 40  HIS A N    1 
ATOM   298  C CA   . HIS A 1 40  ? -6.87963  12.06155 8.80837   1.000 51.43448  ? 40  HIS A CA   1 
ATOM   299  C C    . HIS A 1 40  ? -7.82941  11.02384 9.40301   1.000 45.48882  ? 40  HIS A C    1 
ATOM   300  O O    . HIS A 1 40  ? -7.39873  9.89905  9.67934   1.000 44.54753  ? 40  HIS A O    1 
ATOM   301  C CB   . HIS A 1 40  ? -5.94342  12.61656 9.88508   1.000 54.75167  ? 40  HIS A CB   1 
ATOM   302  C CG   . HIS A 1 40  ? -4.95873  11.60762 10.42181  1.000 60.62454  ? 40  HIS A CG   1 
ATOM   303  N ND1  . HIS A 1 40  ? -4.98388  11.19005 11.74891  1.000 63.23903  ? 40  HIS A ND1  1 
ATOM   304  C CD2  . HIS A 1 40  ? -3.99524  10.86907 9.81216   1.000 61.54630  ? 40  HIS A CD2  1 
ATOM   305  C CE1  . HIS A 1 40  ? -4.04686  10.27233 11.93449  1.000 63.61236  ? 40  HIS A CE1  1 
ATOM   306  N NE2  . HIS A 1 40  ? -3.43535  10.05756 10.77641  1.000 64.84230  ? 40  HIS A NE2  1 
ATOM   307  N N    . ALA A 1 41  ? -9.10691  11.34017 9.58073   1.000 44.25748  ? 41  ALA A N    1 
ATOM   308  C CA   . ALA A 1 41  ? -10.02101 10.33043 10.10626  1.000 44.93062  ? 41  ALA A CA   1 
ATOM   309  C C    . ALA A 1 41  ? -10.28809 9.18883  9.11767   1.000 49.18331  ? 41  ALA A C    1 
ATOM   310  O O    . ALA A 1 41  ? -10.85584 8.16768  9.51220   1.000 51.95135  ? 41  ALA A O    1 
ATOM   311  C CB   . ALA A 1 41  ? -11.33914 10.98886 10.50577  1.000 45.89537  ? 41  ALA A CB   1 
ATOM   312  N N    . SER A 1 42  ? -9.93702  9.33829  7.83441   1.000 50.45888  ? 42  SER A N    1 
ATOM   313  C CA   . SER A 1 42  ? -10.02516 8.21688  6.89127   1.000 51.08060  ? 42  SER A CA   1 
ATOM   314  C C    . SER A 1 42  ? -11.46390 7.69240  6.76806   1.000 46.66898  ? 42  SER A C    1 
ATOM   315  O O    . SER A 1 42  ? -11.73410 6.50551  6.94267   1.000 49.97093  ? 42  SER A O    1 
ATOM   316  C CB   . SER A 1 42  ? -9.05919  7.10416  7.33178   1.000 54.39780  ? 42  SER A CB   1 
ATOM   317  O OG   . SER A 1 42  ? -8.57574  6.36404  6.21468   1.000 64.41436  ? 42  SER A OG   1 
ATOM   318  N N    . VAL A 1 43  ? -12.40380 8.60502  6.51079   1.000 44.20233  ? 43  VAL A N    1 
ATOM   319  C CA   . VAL A 1 43  ? -13.80869 8.23427  6.34510   1.000 45.51272  ? 43  VAL A CA   1 
ATOM   320  C C    . VAL A 1 43  ? -13.99072 7.20650  5.22574   1.000 48.64333  ? 43  VAL A C    1 
ATOM   321  O O    . VAL A 1 43  ? -13.40502 7.33302  4.15579   1.000 46.68537  ? 43  VAL A O    1 
ATOM   322  C CB   . VAL A 1 43  ? -14.61091 9.50004  6.01720   1.000 46.45220  ? 43  VAL A CB   1 
ATOM   323  C CG1  . VAL A 1 43  ? -16.08757 9.19680  6.07145   1.000 46.10068  ? 43  VAL A CG1  1 
ATOM   324  C CG2  . VAL A 1 43  ? -14.21693 10.60897 6.99158   1.000 49.69879  ? 43  VAL A CG2  1 
ATOM   325  N N    . GLY A 1 44  ? -14.85286 6.21409  5.44586   1.000 49.41188  ? 44  GLY A N    1 
ATOM   326  C CA   . GLY A 1 44  ? -15.15988 5.24819  4.38717   1.000 47.54953  ? 44  GLY A CA   1 
ATOM   327  C C    . GLY A 1 44  ? -16.59444 5.39364  3.89955   1.000 46.82591  ? 44  GLY A C    1 
ATOM   328  O O    . GLY A 1 44  ? -17.06156 6.52334  3.69425   1.000 48.14883  ? 44  GLY A O    1 
ATOM   329  N N    . GLU A 1 45  ? -17.33483 4.29474  3.73804   1.000 45.51672  ? 45  GLU A N    1 
ATOM   330  C CA   . GLU A 1 45  ? -18.68561 4.39699  3.20042   1.000 47.03023  ? 45  GLU A CA   1 
ATOM   331  C C    . GLU A 1 45  ? -19.74658 4.28868  4.28674   1.000 48.58446  ? 45  GLU A C    1 
ATOM   332  O O    . GLU A 1 45  ? -20.94183 4.46156  4.00870   1.000 49.51765  ? 45  GLU A O    1 
ATOM   333  C CB   . GLU A 1 45  ? -18.87660 3.32728  2.10262   1.000 50.98240  ? 45  GLU A CB   1 
ATOM   334  C CG   . GLU A 1 45  ? -18.25230 1.96233  2.45661   1.000 54.83835  ? 45  GLU A CG   1 
ATOM   335  C CD   . GLU A 1 45  ? -18.58579 0.85346  1.42268   1.000 55.98721  ? 45  GLU A CD   1 
ATOM   336  O OE1  . GLU A 1 45  ? -18.94185 1.20263  0.28646   1.000 46.77445  ? 45  GLU A OE1  1 
ATOM   337  O OE2  . GLU A 1 45  ? -18.61422 -0.35019 1.79630   1.000 62.11323  ? 45  GLU A OE2  1 
ATOM   338  N N    . THR A 1 46  ? -19.33591 4.06103  5.52741   1.000 46.87871  ? 46  THR A N    1 
ATOM   339  C CA   . THR A 1 46  ? -20.19733 4.23266  6.68214   1.000 49.04716  ? 46  THR A CA   1 
ATOM   340  C C    . THR A 1 46  ? -19.38730 4.86464  7.80843   1.000 46.73897  ? 46  THR A C    1 
ATOM   341  O O    . THR A 1 46  ? -18.15536 4.74505  7.86727   1.000 46.34470  ? 46  THR A O    1 
ATOM   342  C CB   . THR A 1 46  ? -20.78198 2.90626  7.17914   1.000 52.07498  ? 46  THR A CB   1 
ATOM   343  O OG1  . THR A 1 46  ? -19.70351 2.06798  7.60134   1.000 55.14244  ? 46  THR A OG1  1 
ATOM   344  C CG2  . THR A 1 46  ? -21.54213 2.20347  6.08447   1.000 53.27936  ? 46  THR A CG2  1 
ATOM   345  N N    . ILE A 1 47  ? -20.09461 5.53505  8.70321   1.000 45.58695  ? 47  ILE A N    1 
ATOM   346  C CA   . ILE A 1 47  ? -19.47026 6.19504  9.83915   1.000 47.03241  ? 47  ILE A CA   1 
ATOM   347  C C    . ILE A 1 47  ? -20.45645 6.09591  10.98402  1.000 46.44739  ? 47  ILE A C    1 
ATOM   348  O O    . ILE A 1 47  ? -21.67381 6.03602  10.76360  1.000 44.88533  ? 47  ILE A O    1 
ATOM   349  C CB   . ILE A 1 47  ? -19.12267 7.65985  9.47599   1.000 45.81673  ? 47  ILE A CB   1 
ATOM   350  C CG1  . ILE A 1 47  ? -18.08085 8.23953  10.42243  1.000 45.41335  ? 47  ILE A CG1  1 
ATOM   351  C CG2  . ILE A 1 47  ? -20.39836 8.49944  9.37160   1.000 43.32941  ? 47  ILE A CG2  1 
ATOM   352  C CD1  . ILE A 1 47  ? -17.61096 9.64598  10.05925  1.000 44.36544  ? 47  ILE A CD1  1 
ATOM   353  N N    . TYR A 1 48  ? -19.92950 6.07797  12.22180  1.000 50.15356  ? 48  TYR A N    1 
ATOM   354  C CA   . TYR A 1 48  ? -20.76793 6.12301  13.40927  1.000 48.65437  ? 48  TYR A CA   1 
ATOM   355  C C    . TYR A 1 48  ? -20.99344 7.57621  13.78319  1.000 47.19361  ? 48  TYR A C    1 
ATOM   356  O O    . TYR A 1 48  ? -20.02804 8.32906  13.96781  1.000 46.90832  ? 48  TYR A O    1 
ATOM   357  C CB   . TYR A 1 48  ? -20.13702 5.37231  14.58618  1.000 47.74309  ? 48  TYR A CB   1 
ATOM   358  C CG   . TYR A 1 48  ? -20.23036 3.87972  14.42894  1.000 51.75815  ? 48  TYR A CG   1 
ATOM   359  C CD1  . TYR A 1 48  ? -21.40758 3.19054  14.75318  1.000 53.33051  ? 48  TYR A CD1  1 
ATOM   360  C CD2  . TYR A 1 48  ? -19.15984 3.15025  13.90882  1.000 51.22441  ? 48  TYR A CD2  1 
ATOM   361  C CE1  . TYR A 1 48  ? -21.49408 1.79892  14.56967  1.000 56.62808  ? 48  TYR A CE1  1 
ATOM   362  C CE2  . TYR A 1 48  ? -19.24146 1.76676  13.72493  1.000 51.86505  ? 48  TYR A CE2  1 
ATOM   363  C CZ   . TYR A 1 48  ? -20.40083 1.10857  14.05484  1.000 54.81005  ? 48  TYR A CZ   1 
ATOM   364  O OH   . TYR A 1 48  ? -20.45922 -0.25016 13.87796  1.000 63.30057  ? 48  TYR A OH   1 
ATOM   365  N N    . ILE A 1 49  ? -22.25950 7.96470  13.88646  1.000 45.20504  ? 49  ILE A N    1 
ATOM   366  C CA   . ILE A 1 49  ? -22.65490 9.29247  14.33390  1.000 43.94342  ? 49  ILE A CA   1 
ATOM   367  C C    . ILE A 1 49  ? -23.41123 9.13009  15.66343  1.000 44.34382  ? 49  ILE A C    1 
ATOM   368  O O    . ILE A 1 49  ? -24.53369 8.60118  15.68410  1.000 44.20854  ? 49  ILE A O    1 
ATOM   369  C CB   . ILE A 1 49  ? -23.53553 9.98659  13.29197  1.000 42.46306  ? 49  ILE A CB   1 
ATOM   370  C CG1  . ILE A 1 49  ? -22.85118 10.01711 11.88729  1.000 42.08945  ? 49  ILE A CG1  1 
ATOM   371  C CG2  . ILE A 1 49  ? -23.89267 11.38212 13.72117  1.000 40.51360  ? 49  ILE A CG2  1 
ATOM   372  C CD1  . ILE A 1 49  ? -21.62657 10.93205 11.82007  1.000 37.92031  ? 49  ILE A CD1  1 
ATOM   373  N N    . ASN A 1 50  ? -22.84682 9.64692  16.75728  1.000 45.30137  ? 50  ASN A N    1 
ATOM   374  C CA   . ASN A 1 50  ? -23.46077 9.46491  18.09771  1.000 43.39107  ? 50  ASN A CA   1 
ATOM   375  C C    . ASN A 1 50  ? -23.78164 8.00352  18.32529  1.000 44.23036  ? 50  ASN A C    1 
ATOM   376  O O    . ASN A 1 50  ? -24.88279 7.63009  18.73817  1.000 48.19008  ? 50  ASN A O    1 
ATOM   377  C CB   . ASN A 1 50  ? -24.70368 10.33231 18.26638  1.000 41.41682  ? 50  ASN A CB   1 
ATOM   378  C CG   . ASN A 1 50  ? -24.34613 11.79862 18.27262  1.000 43.66250  ? 50  ASN A CG   1 
ATOM   379  O OD1  . ASN A 1 50  ? -23.16131 12.14330 18.39769  1.000 43.98336  ? 50  ASN A OD1  1 
ATOM   380  N ND2  . ASN A 1 50  ? -25.34182 12.66900 18.20021  1.000 44.17387  ? 50  ASN A ND2  1 
ATOM   381  N N    . ASP A 1 51  ? -22.79687 7.18027  17.98056  1.000 47.38298  ? 51  ASP A N    1 
ATOM   382  C CA   . ASP A 1 51  ? -22.76379 5.73212  18.08288  1.000 50.27340  ? 51  ASP A CA   1 
ATOM   383  C C    . ASP A 1 51  ? -23.75929 5.02471  17.18669  1.000 53.08584  ? 51  ASP A C    1 
ATOM   384  O O    . ASP A 1 51  ? -23.92963 3.80678  17.32104  1.000 55.28897  ? 51  ASP A O    1 
ATOM   385  C CB   . ASP A 1 51  ? -22.95640 5.29755  19.53226  1.000 50.49034  ? 51  ASP A CB   1 
ATOM   386  C CG   . ASP A 1 51  ? -21.82892 5.76026  20.37513  1.000 53.57998  ? 51  ASP A CG   1 
ATOM   387  O OD1  . ASP A 1 51  ? -20.66739 5.49022  19.96935  1.000 53.03844  ? 51  ASP A OD1  1 
ATOM   388  O OD2  . ASP A 1 51  ? -22.08517 6.38174  21.42714  1.000 55.00882  ? 51  ASP A OD2  1 
ATOM   389  N N    . VAL A 1 52  ? -24.39414 5.73728  16.25752  1.000 50.71338  ? 52  VAL A N    1 
ATOM   390  C CA   . VAL A 1 52  ? -25.35566 5.15969  15.33293  1.000 52.62487  ? 52  VAL A CA   1 
ATOM   391  C C    . VAL A 1 52  ? -24.69636 5.05399  13.96728  1.000 52.28143  ? 52  VAL A C    1 
ATOM   392  O O    . VAL A 1 52  ? -24.13188 6.03765  13.46401  1.000 49.35041  ? 52  VAL A O    1 
ATOM   393  C CB   . VAL A 1 52  ? -26.63314 6.00975  15.25407  1.000 52.06097  ? 52  VAL A CB   1 
ATOM   394  C CG1  . VAL A 1 52  ? -27.50850 5.54426  14.06155  1.000 50.57543  ? 52  VAL A CG1  1 
ATOM   395  C CG2  . VAL A 1 52  ? -27.36037 5.94033  16.55213  1.000 48.11267  ? 52  VAL A CG2  1 
ATOM   396  N N    . GLU A 1 53  ? -24.74166 3.86386  13.37920  1.000 52.95291  ? 53  GLU A N    1 
ATOM   397  C CA   . GLU A 1 53  ? -24.03779 3.65368  12.12771  1.000 53.98786  ? 53  GLU A CA   1 
ATOM   398  C C    . GLU A 1 53  ? -24.79088 4.32309  10.97569  1.000 51.84670  ? 53  GLU A C    1 
ATOM   399  O O    . GLU A 1 53  ? -26.01593 4.22611  10.85647  1.000 51.76024  ? 53  GLU A O    1 
ATOM   400  C CB   . GLU A 1 53  ? -23.84558 2.16294  11.86992  1.000 58.03673  ? 53  GLU A CB   1 
ATOM   401  C CG   . GLU A 1 53  ? -23.23119 1.88733  10.52387  1.000 60.30087  ? 53  GLU A CG   1 
ATOM   402  C CD   . GLU A 1 53  ? -22.86295 0.43004  10.33359  1.000 68.96729  ? 53  GLU A CD   1 
ATOM   403  O OE1  . GLU A 1 53  ? -23.76654 -0.43863 10.44295  1.000 72.30830  ? 53  GLU A OE1  1 
ATOM   404  O OE2  . GLU A 1 53  ? -21.67661 0.16473  10.03924  1.000 71.84405  ? 53  GLU A OE2  1 
ATOM   405  N N    . THR A 1 54  ? -24.05494 5.03611  10.13666  1.000 50.90401  ? 54  THR A N    1 
ATOM   406  C CA   . THR A 1 54  ? -24.67239 5.96029  9.19876   1.000 47.23581  ? 54  THR A CA   1 
ATOM   407  C C    . THR A 1 54  ? -23.96985 5.82430  7.86231   1.000 47.42273  ? 54  THR A C    1 
ATOM   408  O O    . THR A 1 54  ? -22.73808 5.72537  7.81106   1.000 47.07957  ? 54  THR A O    1 
ATOM   409  C CB   . THR A 1 54  ? -24.58390 7.40545  9.72813   1.000 46.67940  ? 54  THR A CB   1 
ATOM   410  O OG1  . THR A 1 54  ? -25.10604 7.45636  11.08246  1.000 47.24895  ? 54  THR A OG1  1 
ATOM   411  C CG2  . THR A 1 54  ? -25.35711 8.37332  8.87011   1.000 43.35824  ? 54  THR A CG2  1 
ATOM   412  N N    . LYS A 1 55  ? -24.75900 5.79104  6.79375   1.000 44.08385  ? 55  LYS A N    1 
ATOM   413  C CA   . LYS A 1 55  ? -24.19592 5.74284  5.44147   1.000 45.49778  ? 55  LYS A CA   1 
ATOM   414  C C    . LYS A 1 55  ? -23.54553 7.07885  5.08661   1.000 40.84298  ? 55  LYS A C    1 
ATOM   415  O O    . LYS A 1 55  ? -24.16974 8.14360  5.20868   1.000 42.13325  ? 55  LYS A O    1 
ATOM   416  C CB   . LYS A 1 55  ? -25.29751 5.42982  4.43614   1.000 45.18315  ? 55  LYS A CB   1 
ATOM   417  C CG   . LYS A 1 55  ? -25.29354 4.03552  3.90023   1.000 50.82602  ? 55  LYS A CG   1 
ATOM   418  C CD   . LYS A 1 55  ? -26.38051 3.90320  2.81725   1.000 45.31136  ? 55  LYS A CD   1 
ATOM   419  C CE   . LYS A 1 55  ? -27.10693 2.56433  2.96190   1.000 46.59366  ? 55  LYS A CE   1 
ATOM   420  N NZ   . LYS A 1 55  ? -26.02993 1.49398  2.87459   1.000 44.14832  ? 55  LYS A NZ   1 
ATOM   421  N N    . VAL A 1 56  ? -22.30494 7.02714  4.61101   1.000 41.49037  ? 56  VAL A N    1 
ATOM   422  C CA   . VAL A 1 56  ? -21.63849 8.21025  4.08250   1.000 38.36282  ? 56  VAL A CA   1 
ATOM   423  C C    . VAL A 1 56  ? -21.95571 8.26730  2.58049   1.000 44.74296  ? 56  VAL A C    1 
ATOM   424  O O    . VAL A 1 56  ? -21.42661 7.50474  1.78812   1.000 42.40825  ? 56  VAL A O    1 
ATOM   425  C CB   . VAL A 1 56  ? -20.13891 8.19279  4.39028   1.000 37.92164  ? 56  VAL A CB   1 
ATOM   426  C CG1  . VAL A 1 56  ? -19.45954 9.39804  3.75851   1.000 40.06352  ? 56  VAL A CG1  1 
ATOM   427  C CG2  . VAL A 1 56  ? -19.91009 8.23022  5.98490   1.000 39.28050  ? 56  VAL A CG2  1 
ATOM   428  N N    . LEU A 1 57  ? -22.86089 9.17656  2.19877   1.000 42.15409  ? 57  LEU A N    1 
ATOM   429  C CA   . LEU A 1 57  ? -23.32809 9.26865  0.82244   1.000 41.54999  ? 57  LEU A CA   1 
ATOM   430  C C    . LEU A 1 57  ? -22.30428 9.91912  -0.09772  1.000 46.47273  ? 57  LEU A C    1 
ATOM   431  O O    . LEU A 1 57  ? -22.23454 9.58128  -1.30170  1.000 45.27379  ? 57  LEU A O    1 
ATOM   432  C CB   . LEU A 1 57  ? -24.64745 10.04336 0.76903   1.000 40.61899  ? 57  LEU A CB   1 
ATOM   433  C CG   . LEU A 1 57  ? -25.81071 9.38731  1.52016   1.000 39.45724  ? 57  LEU A CG   1 
ATOM   434  C CD1  . LEU A 1 57  ? -27.11860 10.20505 1.38964   1.000 38.29000  ? 57  LEU A CD1  1 
ATOM   435  C CD2  . LEU A 1 57  ? -26.00359 7.91083  1.14679   1.000 39.54780  ? 57  LEU A CD2  1 
ATOM   436  N N    . ASP A 1 58  ? -21.52184 10.86319 0.42161   1.000 44.20524  ? 58  ASP A N    1 
ATOM   437  C CA   . ASP A 1 58  ? -20.50340 11.48229 -0.40250  1.000 44.71545  ? 58  ASP A CA   1 
ATOM   438  C C    . ASP A 1 58  ? -19.39143 11.88396 0.55161   1.000 47.29237  ? 58  ASP A C    1 
ATOM   439  O O    . ASP A 1 58  ? -19.64647 12.14104 1.72709   1.000 43.24044  ? 58  ASP A O    1 
ATOM   440  C CB   . ASP A 1 58  ? -21.07600 12.70159 -1.15059  1.000 46.91602  ? 58  ASP A CB   1 
ATOM   441  C CG   . ASP A 1 58  ? -20.26528 13.06561 -2.39177  1.000 51.62934  ? 58  ASP A CG   1 
ATOM   442  O OD1  . ASP A 1 58  ? -20.82907 13.74908 -3.26316  1.000 48.84553  ? 58  ASP A OD1  1 
ATOM   443  O OD2  . ASP A 1 58  ? -19.13722 12.54656 -2.56645  1.000 49.98192  ? 58  ASP A OD2  1 
ATOM   444  N N    . ALA A 1 59  ? -18.15772 11.91410 0.07203   1.000 47.49632  ? 59  ALA A N    1 
ATOM   445  C CA   . ALA A 1 59  ? -17.04126 12.34096 0.90880   1.000 43.84382  ? 59  ALA A CA   1 
ATOM   446  C C    . ALA A 1 59  ? -16.02022 12.97950 -0.00607  1.000 50.85229  ? 59  ALA A C    1 
ATOM   447  O O    . ALA A 1 59  ? -15.67636 12.39088 -1.04461  1.000 50.65153  ? 59  ALA A O    1 
ATOM   448  C CB   . ALA A 1 59  ? -16.41655 11.16902 1.66487   1.000 46.69675  ? 59  ALA A CB   1 
ATOM   449  N N    . CYS A 1 60  ? -15.57311 14.18946 0.32716   1.000 44.35646  ? 60  CYS A N    1 
ATOM   450  C CA   A CYS A 1 60  ? -14.67383 14.94000 -0.54163  0.609 48.83976  ? 60  CYS A CA   1 
ATOM   451  C CA   B CYS A 1 60  ? -14.65887 14.93059 -0.53883  0.391 49.62839  ? 60  CYS A CA   1 
ATOM   452  C C    . CYS A 1 60  ? -13.51017 15.45976 0.30131   1.000 47.29386  ? 60  CYS A C    1 
ATOM   453  O O    . CYS A 1 60  ? -13.68907 16.38728 1.08680   1.000 45.19999  ? 60  CYS A O    1 
ATOM   454  C CB   A CYS A 1 60  ? -15.43698 16.07634 -1.24419  0.609 50.65820  ? 60  CYS A CB   1 
ATOM   455  C CB   B CYS A 1 60  ? -15.37078 16.07458 -1.26058  0.391 50.00817  ? 60  CYS A CB   1 
ATOM   456  S SG   A CYS A 1 60  ? -17.07833 15.62246 -2.05039  0.609 57.08712  ? 60  CYS A SG   1 
ATOM   457  S SG   B CYS A 1 60  ? -14.32665 16.96322 -2.45329  0.391 52.60939  ? 60  CYS A SG   1 
ATOM   458  N N    . ALA A 1 61  ? -12.32710 14.86769 0.13342   1.000 43.37638  ? 61  ALA A N    1 
ATOM   459  C CA   . ALA A 1 61  ? -11.11497 15.32173 0.79913   1.000 45.46400  ? 61  ALA A CA   1 
ATOM   460  C C    . ALA A 1 61  ? -10.58648 16.54689 0.07448   1.000 47.98405  ? 61  ALA A C    1 
ATOM   461  O O    . ALA A 1 61  ? -10.10208 16.43658 -1.04716  1.000 45.36155  ? 61  ALA A O    1 
ATOM   462  C CB   . ALA A 1 61  ? -10.06891 14.21291 0.81263   1.000 46.41323  ? 61  ALA A CB   1 
ATOM   463  N N    . LEU A 1 62  ? -10.66301 17.71715 0.70202   1.000 46.03513  ? 62  LEU A N    1 
ATOM   464  C CA   . LEU A 1 62  ? -10.36882 18.94467 -0.02674  1.000 45.94207  ? 62  LEU A CA   1 
ATOM   465  C C    . LEU A 1 62  ? -8.86949  19.07127 -0.25375  1.000 46.19826  ? 62  LEU A C    1 
ATOM   466  O O    . LEU A 1 62  ? -8.06931  18.79203 0.64212   1.000 41.93132  ? 62  LEU A O    1 
ATOM   467  C CB   . LEU A 1 62  ? -10.86266 20.15649 0.74738   1.000 47.65726  ? 62  LEU A CB   1 
ATOM   468  C CG   . LEU A 1 62  ? -12.37902 20.22588 0.90657   1.000 49.32621  ? 62  LEU A CG   1 
ATOM   469  C CD1  . LEU A 1 62  ? -12.85184 21.62483 1.32598   1.000 45.40218  ? 62  LEU A CD1  1 
ATOM   470  C CD2  . LEU A 1 62  ? -13.01392 19.79266 -0.39319  1.000 44.96305  ? 62  LEU A CD2  1 
ATOM   471  N N    . ARG A 1 63  ? -8.49149  19.48247 -1.46498  1.000 43.36926  ? 63  ARG A N    1 
ATOM   472  C CA   . ARG A 1 63  ? -7.10921  19.84613 -1.78084  1.000 43.66966  ? 63  ARG A CA   1 
ATOM   473  C C    . ARG A 1 63  ? -7.13298  21.13119 -2.60584  1.000 43.18088  ? 63  ARG A C    1 
ATOM   474  O O    . ARG A 1 63  ? -8.14234  21.45582 -3.24139  1.000 46.12167  ? 63  ARG A O    1 
ATOM   475  C CB   . ARG A 1 63  ? -6.38619  18.72125 -2.53185  1.000 44.81396  ? 63  ARG A CB   1 
ATOM   476  C CG   . ARG A 1 63  ? -6.41556  17.39714 -1.82157  1.000 44.17599  ? 63  ARG A CG   1 
ATOM   477  C CD   . ARG A 1 63  ? -5.89799  16.26357 -2.68528  1.000 46.92803  ? 63  ARG A CD   1 
ATOM   478  N NE   . ARG A 1 63  ? -4.43677  16.23930 -2.76037  1.000 45.25933  ? 63  ARG A NE   1 
ATOM   479  C CZ   . ARG A 1 63  ? -3.61551  15.81118 -1.81286  1.000 49.20755  ? 63  ARG A CZ   1 
ATOM   480  N NH1  . ARG A 1 63  ? -4.05683  15.44869 -0.61383  1.000 47.87869  ? 63  ARG A NH1  1 
ATOM   481  N NH2  . ARG A 1 63  ? -2.30674  15.77684 -2.05818  1.000 49.21828  ? 63  ARG A NH2  1 
ATOM   482  N N    . ASP A 1 64  ? -6.01961  21.88173 -2.58827  1.000 40.55879  ? 64  ASP A N    1 
ATOM   483  C CA   . ASP A 1 64  ? -5.99614  23.15597 -3.28863  1.000 42.72066  ? 64  ASP A CA   1 
ATOM   484  C C    . ASP A 1 64  ? -5.42274  22.96115 -4.69147  1.000 43.39284  ? 64  ASP A C    1 
ATOM   485  O O    . ASP A 1 64  ? -5.06953  21.84766 -5.10264  1.000 39.03886  ? 64  ASP A O    1 
ATOM   486  C CB   . ASP A 1 64  ? -5.20327  24.20153 -2.52965  1.000 39.36140  ? 64  ASP A CB   1 
ATOM   487  C CG   . ASP A 1 64  ? -3.74321  23.83002 -2.36935  1.000 44.22658  ? 64  ASP A CG   1 
ATOM   488  O OD1  . ASP A 1 64  ? -3.26636  22.92737 -3.09873  1.000 44.95551  ? 64  ASP A OD1  1 
ATOM   489  O OD2  . ASP A 1 64  ? -3.07454  24.43291 -1.48277  1.000 47.25121  ? 64  ASP A OD2  1 
ATOM   490  N N    . LEU A 1 65  ? -5.25614  24.06152 -5.41410  1.000 42.43743  ? 65  LEU A N    1 
ATOM   491  C CA   . LEU A 1 65  ? -4.88704  23.87545 -6.81860  1.000 46.00122  ? 65  LEU A CA   1 
ATOM   492  C C    . LEU A 1 65  ? -3.42452  23.45663 -6.97788  1.000 47.67526  ? 65  LEU A C    1 
ATOM   493  O O    . LEU A 1 65  ? -3.05149  23.06346 -8.08411  1.000 47.85468  ? 65  LEU A O    1 
ATOM   494  C CB   . LEU A 1 65  ? -5.19051  25.13778 -7.62411  1.000 45.72248  ? 65  LEU A CB   1 
ATOM   495  C CG   . LEU A 1 65  ? -6.54616  25.13540 -8.32782  1.000 47.94003  ? 65  LEU A CG   1 
ATOM   496  C CD1  . LEU A 1 65  ? -6.49295  24.25226 -9.58032  1.000 49.21276  ? 65  LEU A CD1  1 
ATOM   497  C CD2  . LEU A 1 65  ? -7.61045  24.64435 -7.39245  1.000 48.50541  ? 65  LEU A CD2  1 
ATOM   498  N N    . THR A 1 66  ? -2.60065  23.48735 -5.90615  1.000 42.20037  ? 66  THR A N    1 
ATOM   499  C CA   . THR A 1 66  ? -1.25517  22.89390 -5.95413  1.000 42.19503  ? 66  THR A CA   1 
ATOM   500  C C    . THR A 1 66  ? -1.29721  21.38738 -5.71881  1.000 42.14089  ? 66  THR A C    1 
ATOM   501  O O    . THR A 1 66  ? -0.24650  20.75173 -5.51796  1.000 46.19851  ? 66  THR A O    1 
ATOM   502  C CB   . THR A 1 66  ? -0.29784  23.52312 -4.92471  1.000 46.95140  ? 66  THR A CB   1 
ATOM   503  O OG1  . THR A 1 66  ? -0.67838  23.13501 -3.57966  1.000 47.28390  ? 66  THR A OG1  1 
ATOM   504  C CG2  . THR A 1 66  ? -0.28838  25.05295 -5.00779  1.000 49.98118  ? 66  THR A CG2  1 
ATOM   505  N N    . ASP A 1 67  ? -2.50031  20.81967 -5.66720  1.000 38.85584  ? 67  ASP A N    1 
ATOM   506  C CA   . ASP A 1 67  ? -2.70555  19.43352 -5.21237  1.000 46.28937  ? 67  ASP A CA   1 
ATOM   507  C C    . ASP A 1 67  ? -2.08690  19.18651 -3.83218  1.000 47.59272  ? 67  ASP A C    1 
ATOM   508  O O    . ASP A 1 67  ? -1.43207  18.16934 -3.56787  1.000 47.77182  ? 67  ASP A O    1 
ATOM   509  C CB   . ASP A 1 67  ? -2.19019  18.43486 -6.25210  1.000 48.20432  ? 67  ASP A CB   1 
ATOM   510  C CG   . ASP A 1 67  ? -2.65384  17.02643 -5.96549  1.000 55.05856  ? 67  ASP A CG   1 
ATOM   511  O OD1  . ASP A 1 67  ? -3.85837  16.86317 -5.61617  1.000 51.64528  ? 67  ASP A OD1  1 
ATOM   512  O OD2  . ASP A 1 67  ? -1.84229  16.08385 -6.12706  1.000 56.81329  ? 67  ASP A OD2  1 
ATOM   513  N N    . THR A 1 68  ? -2.29576  20.12471 -2.92840  1.000 43.46303  ? 68  THR A N    1 
ATOM   514  C CA   . THR A 1 68  ? -1.84371  19.94725 -1.55415  1.000 46.04773  ? 68  THR A CA   1 
ATOM   515  C C    . THR A 1 68  ? -3.04147  19.71295 -0.63779  1.000 42.38393  ? 68  THR A C    1 
ATOM   516  O O    . THR A 1 68  ? -4.06896  20.39129 -0.75194  1.000 40.55392  ? 68  THR A O    1 
ATOM   517  C CB   . THR A 1 68  ? -1.01556  21.15280 -1.09369  1.000 45.42737  ? 68  THR A CB   1 
ATOM   518  O OG1  . THR A 1 68  ? 0.16713   21.27541 -1.91608  1.000 46.19409  ? 68  THR A OG1  1 
ATOM   519  C CG2  . THR A 1 68  ? -0.62642  21.01620 0.39393   1.000 46.87133  ? 68  THR A CG2  1 
ATOM   520  N N    . ASN A 1 69  ? -2.90847  18.73036 0.24671   1.000 47.22259  ? 69  ASN A N    1 
ATOM   521  C CA   . ASN A 1 69  ? -3.89108  18.46297 1.30940   1.000 45.49662  ? 69  ASN A CA   1 
ATOM   522  C C    . ASN A 1 69  ? -4.34297  19.74563 2.00448   1.000 42.58571  ? 69  ASN A C    1 
ATOM   523  O O    . ASN A 1 69  ? -3.51937  20.56426 2.42128   1.000 44.70610  ? 69  ASN A O    1 
ATOM   524  C CB   . ASN A 1 69  ? -3.26747  17.51249 2.32608   1.000 44.57779  ? 69  ASN A CB   1 
ATOM   525  C CG   . ASN A 1 69  ? -4.18458  17.21147 3.48967   1.000 46.19809  ? 69  ASN A CG   1 
ATOM   526  O OD1  . ASN A 1 69  ? -5.37121  16.89853 3.30408   1.000 47.86357  ? 69  ASN A OD1  1 
ATOM   527  N ND2  . ASN A 1 69  ? -3.65729  17.30106 4.67101   1.000 45.90929  ? 69  ASN A ND2  1 
ATOM   528  N N    . LEU A 1 70  ? -5.66325  19.92431 2.13755   1.000 42.81941  ? 70  LEU A N    1 
ATOM   529  C CA   . LEU A 1 70  ? -6.19638  20.95737 3.02928   1.000 42.28056  ? 70  LEU A CA   1 
ATOM   530  C C    . LEU A 1 70  ? -6.66475  20.39938 4.37485   1.000 42.70196  ? 70  LEU A C    1 
ATOM   531  O O    . LEU A 1 70  ? -7.04779  21.18794 5.24284   1.000 42.98508  ? 70  LEU A O    1 
ATOM   532  C CB   . LEU A 1 70  ? -7.35373  21.70706 2.35181   1.000 41.02992  ? 70  LEU A CB   1 
ATOM   533  C CG   . LEU A 1 70  ? -6.87271  22.47351 1.10472   1.000 41.07890  ? 70  LEU A CG   1 
ATOM   534  C CD1  . LEU A 1 70  ? -8.05241  23.03460 0.35683   1.000 40.59040  ? 70  LEU A CD1  1 
ATOM   535  C CD2  . LEU A 1 70  ? -5.89265  23.58204 1.48804   1.000 38.75227  ? 70  LEU A CD2  1 
ATOM   536  N N    . GLU A 1 71  ? -6.65083  19.07032 4.56288   1.000 43.32652  ? 71  GLU A N    1 
ATOM   537  C CA   . GLU A 1 71  ? -7.03126  18.37370 5.79179   1.000 42.65800  ? 71  GLU A CA   1 
ATOM   538  C C    . GLU A 1 71  ? -8.51397  18.42496 6.14540   1.000 43.14685  ? 71  GLU A C    1 
ATOM   539  O O    . GLU A 1 71  ? -8.88628  17.91674 7.21705   1.000 45.44300  ? 71  GLU A O    1 
ATOM   540  C CB   . GLU A 1 71  ? -6.19178  18.88978 6.96634   1.000 42.73135  ? 71  GLU A CB   1 
ATOM   541  C CG   . GLU A 1 71  ? -5.90192  17.95983 8.19639   1.000 46.97293  ? 71  GLU A CG   1 
ATOM   542  C CD   . GLU A 1 71  ? -5.82465  16.46906 7.87037   1.000 51.22976  ? 71  GLU A CD   1 
ATOM   543  O OE1  . GLU A 1 71  ? -5.20402  16.05097 6.83030   1.000 48.29289  ? 71  GLU A OE1  1 
ATOM   544  O OE2  . GLU A 1 71  ? -6.27303  15.71941 8.77705   1.000 44.09556  ? 71  GLU A OE2  1 
ATOM   545  N N    . ILE A 1 72  ? -9.35529  19.05147 5.33564   1.000 41.78217  ? 72  ILE A N    1 
ATOM   546  C CA   . ILE A 1 72  ? -10.80604 19.04390 5.50099   1.000 40.86509  ? 72  ILE A CA   1 
ATOM   547  C C    . ILE A 1 72  ? -11.39157 17.96964 4.59701   1.000 44.46517  ? 72  ILE A C    1 
ATOM   548  O O    . ILE A 1 72  ? -11.11028 17.94826 3.38695   1.000 41.72385  ? 72  ILE A O    1 
ATOM   549  C CB   . ILE A 1 72  ? -11.42566 20.41337 5.15388   1.000 41.62536  ? 72  ILE A CB   1 
ATOM   550  C CG1  . ILE A 1 72  ? -10.89857 21.52744 6.06177   1.000 40.59074  ? 72  ILE A CG1  1 
ATOM   551  C CG2  . ILE A 1 72  ? -12.90969 20.35565 5.24307   1.000 42.51798  ? 72  ILE A CG2  1 
ATOM   552  C CD1  . ILE A 1 72  ? -11.53167 21.49118 7.45642   1.000 44.62306  ? 72  ILE A CD1  1 
ATOM   553  N N    . THR A 1 73  ? -12.24731 17.11341 5.15218   1.000 40.03245  ? 73  THR A N    1 
ATOM   554  C CA   . THR A 1 73  ? -13.11728 16.25962 4.34075   1.000 41.48027  ? 73  THR A CA   1 
ATOM   555  C C    . THR A 1 73  ? -14.56822 16.65884 4.58391   1.000 42.63623  ? 73  THR A C    1 
ATOM   556  O O    . THR A 1 73  ? -15.00649 16.81258 5.73494   1.000 39.18551  ? 73  THR A O    1 
ATOM   557  C CB   . THR A 1 73  ? -12.93504 14.78779 4.68015   1.000 42.79255  ? 73  THR A CB   1 
ATOM   558  O OG1  . THR A 1 73  ? -11.65105 14.34872 4.23622   1.000 41.92361  ? 73  THR A OG1  1 
ATOM   559  C CG2  . THR A 1 73  ? -14.02505 13.98011 4.02818   1.000 42.76720  ? 73  THR A CG2  1 
ATOM   560  N N    . ILE A 1 74  ? -15.30834 16.88093 3.51514   1.000 38.22601  ? 74  ILE A N    1 
ATOM   561  C CA   . ILE A 1 74  ? -16.71790 17.21664 3.63065   1.000 39.33584  ? 74  ILE A CA   1 
ATOM   562  C C    . ILE A 1 74  ? -17.50192 15.93938 3.39387   1.000 44.25990  ? 74  ILE A C    1 
ATOM   563  O O    . ILE A 1 74  ? -17.24801 15.23472 2.40834   1.000 44.76179  ? 74  ILE A O    1 
ATOM   564  C CB   . ILE A 1 74  ? -17.11614 18.29761 2.62316   1.000 40.20864  ? 74  ILE A CB   1 
ATOM   565  C CG1  . ILE A 1 74  ? -16.28492 19.56433 2.80911   1.000 39.71479  ? 74  ILE A CG1  1 
ATOM   566  C CG2  . ILE A 1 74  ? -18.60888 18.56328 2.64852   1.000 39.28865  ? 74  ILE A CG2  1 
ATOM   567  C CD1  . ILE A 1 74  ? -16.56987 20.62633 1.66775   1.000 41.90956  ? 74  ILE A CD1  1 
ATOM   568  N N    . VAL A 1 75  ? -18.45205 15.63039 4.28886   1.000 39.37457  ? 75  VAL A N    1 
ATOM   569  C CA   . VAL A 1 75  ? -19.25916 14.42494 4.13370   1.000 39.95193  ? 75  VAL A CA   1 
ATOM   570  C C    . VAL A 1 75  ? -20.72973 14.80939 3.99859   1.000 44.48772  ? 75  VAL A C    1 
ATOM   571  O O    . VAL A 1 75  ? -21.17513 15.85606 4.48243   1.000 42.79630  ? 75  VAL A O    1 
ATOM   572  C CB   . VAL A 1 75  ? -19.03398 13.44305 5.30041   1.000 41.73739  ? 75  VAL A CB   1 
ATOM   573  C CG1  . VAL A 1 75  ? -17.58626 13.00447 5.31770   1.000 40.18161  ? 75  VAL A CG1  1 
ATOM   574  C CG2  . VAL A 1 75  ? -19.44548 14.06966 6.64373   1.000 43.63559  ? 75  VAL A CG2  1 
ATOM   575  N N    . LYS A 1 76  ? -21.46568 13.97326 3.25854   1.000 41.54955  ? 76  LYS A N    1 
ATOM   576  C CA   . LYS A 1 76  ? -22.92165 14.00480 3.16896   1.000 40.31084  ? 76  LYS A CA   1 
ATOM   577  C C    . LYS A 1 76  ? -23.40293 12.71276 3.79795   1.000 41.95702  ? 76  LYS A C    1 
ATOM   578  O O    . LYS A 1 76  ? -22.91278 11.63103 3.44333   1.000 43.30806  ? 76  LYS A O    1 
ATOM   579  C CB   . LYS A 1 76  ? -23.39277 14.08424 1.69516   1.000 42.97723  ? 76  LYS A CB   1 
ATOM   580  C CG   . LYS A 1 76  ? -24.91518 14.25317 1.46759   1.000 40.60058  ? 76  LYS A CG   1 
ATOM   581  C CD   . LYS A 1 76  ? -25.28264 14.24060 -0.08125  1.000 43.55550  ? 76  LYS A CD   1 
ATOM   582  C CE   . LYS A 1 76  ? -26.74480 14.63713 -0.32280  1.000 45.01457  ? 76  LYS A CE   1 
ATOM   583  N NZ   . LYS A 1 76  ? -26.95805 15.02834 -1.78512  1.000 50.57438  ? 76  LYS A NZ   1 
ATOM   584  N N    . LEU A 1 77  ? -24.33799 12.81119 4.72360   1.000 44.05608  ? 77  LEU A N    1 
ATOM   585  C CA   . LEU A 1 77  ? -24.65132 11.69803 5.60810   1.000 43.34494  ? 77  LEU A CA   1 
ATOM   586  C C    . LEU A 1 77  ? -26.09554 11.27651 5.39803   1.000 43.12787  ? 77  LEU A C    1 
ATOM   587  O O    . LEU A 1 77  ? -26.96536 12.12530 5.17221   1.000 45.23743  ? 77  LEU A O    1 
ATOM   588  C CB   . LEU A 1 77  ? -24.45509 12.07730 7.08264   1.000 39.03216  ? 77  LEU A CB   1 
ATOM   589  C CG   . LEU A 1 77  ? -23.06178 12.38572 7.61185   1.000 42.26426  ? 77  LEU A CG   1 
ATOM   590  C CD1  . LEU A 1 77  ? -23.23065 12.85830 9.07823   1.000 41.63010  ? 77  LEU A CD1  1 
ATOM   591  C CD2  . LEU A 1 77  ? -22.19557 11.14634 7.57823   1.000 44.31810  ? 77  LEU A CD2  1 
ATOM   592  N N    . ASP A 1 78  ? -26.37887 9.97339  5.52152   1.000 42.20059  ? 78  ASP A N    1 
ATOM   593  C CA   . ASP A 1 78  ? -27.77230 9.55166  5.38233   1.000 43.41662  ? 78  ASP A CA   1 
ATOM   594  C C    . ASP A 1 78  ? -28.36963 9.52666  6.79950   1.000 47.92176  ? 78  ASP A C    1 
ATOM   595  O O    . ASP A 1 78  ? -28.22864 8.54708  7.53513   1.000 46.25076  ? 78  ASP A O    1 
ATOM   596  C CB   . ASP A 1 78  ? -27.87753 8.20195  4.68232   1.000 44.71292  ? 78  ASP A CB   1 
ATOM   597  C CG   . ASP A 1 78  ? -29.30098 7.66682  4.65425   1.000 47.01192  ? 78  ASP A CG   1 
ATOM   598  O OD1  . ASP A 1 78  ? -30.26900 8.50013  4.64929   1.000 43.06185  ? 78  ASP A OD1  1 
ATOM   599  O OD2  . ASP A 1 78  ? -29.44775 6.42249  4.56310   1.000 50.74453  ? 78  ASP A OD2  1 
ATOM   600  N N    . ARG A 1 79  ? -29.04027 10.61227 7.18044   1.000 44.53749  ? 79  ARG A N    1 
ATOM   601  C CA   . ARG A 1 79  ? -29.68361 10.68215 8.47040   1.000 49.72088  ? 79  ARG A CA   1 
ATOM   602  C C    . ARG A 1 79  ? -30.85026 11.65150 8.36970   1.000 50.02788  ? 79  ARG A C    1 
ATOM   603  O O    . ARG A 1 79  ? -30.92938 12.47047 7.45239   1.000 49.96059  ? 79  ARG A O    1 
ATOM   604  C CB   . ARG A 1 79  ? -28.64523 11.03246 9.55675   1.000 48.66453  ? 79  ARG A CB   1 
ATOM   605  C CG   . ARG A 1 79  ? -28.09234 12.45054 9.58092   1.000 48.35802  ? 79  ARG A CG   1 
ATOM   606  C CD   . ARG A 1 79  ? -26.79473 12.44269 10.45042  1.000 49.36127  ? 79  ARG A CD   1 
ATOM   607  N NE   . ARG A 1 79  ? -26.97368 12.23430 11.90432  1.000 45.91967  ? 79  ARG A NE   1 
ATOM   608  C CZ   . ARG A 1 79  ? -27.32289 13.15568 12.79834  1.000 51.24973  ? 79  ARG A CZ   1 
ATOM   609  N NH1  . ARG A 1 79  ? -27.56160 14.41711 12.45196  1.000 48.32254  ? 79  ARG A NH1  1 
ATOM   610  N NH2  . ARG A 1 79  ? -27.37582 12.81718 14.08624  1.000 50.70930  ? 79  ARG A NH2  1 
ATOM   611  N N    . ASN A 1 80  ? -31.78928 11.50272 9.29907   1.000 50.35185  ? 80  ASN A N    1 
ATOM   612  C CA   . ASN A 1 80  ? -33.05187 12.22529 9.21222   1.000 50.21756  ? 80  ASN A CA   1 
ATOM   613  C C    . ASN A 1 80  ? -32.92597 13.67122 9.66963   1.000 53.15609  ? 80  ASN A C    1 
ATOM   614  O O    . ASN A 1 80  ? -33.52952 14.55595 9.06323   1.000 57.30567  ? 80  ASN A O    1 
ATOM   615  C CB   . ASN A 1 80  ? -34.11769 11.50172 10.03218  1.000 52.33422  ? 80  ASN A CB   1 
ATOM   616  C CG   . ASN A 1 80  ? -35.49379 12.09585 9.83067   1.000 52.10677  ? 80  ASN A CG   1 
ATOM   617  O OD1  . ASN A 1 80  ? -35.86256 12.52621 8.73348   1.000 54.67840  ? 80  ASN A OD1  1 
ATOM   618  N ND2  . ASN A 1 80  ? -36.24955 12.17318 10.91901  1.000 61.66381  ? 80  ASN A ND2  1 
ATOM   619  N N    . GLN A 1 81  ? -32.19275 13.92436 10.75657  1.000 56.84702  ? 81  GLN A N    1 
ATOM   620  C CA   . GLN A 1 81  ? -31.99737 15.29128 11.23512  1.000 57.96809  ? 81  GLN A CA   1 
ATOM   621  C C    . GLN A 1 81  ? -31.27329 16.14267 10.18877  1.000 53.87554  ? 81  GLN A C    1 
ATOM   622  O O    . GLN A 1 81  ? -30.27344 15.72468 9.60372   1.000 53.21921  ? 81  GLN A O    1 
ATOM   623  C CB   . GLN A 1 81  ? -31.18334 15.28764 12.54067  1.000 58.09486  ? 81  GLN A CB   1 
ATOM   624  C CG   . GLN A 1 81  ? -31.74466 14.42677 13.70547  1.000 60.86155  ? 81  GLN A CG   1 
ATOM   625  C CD   . GLN A 1 81  ? -31.15534 12.99760 13.71251  1.000 62.02306  ? 81  GLN A CD   1 
ATOM   626  O OE1  . GLN A 1 81  ? -30.87940 12.40316 12.63309  1.000 61.00541  ? 81  GLN A OE1  1 
ATOM   627  N NE2  . GLN A 1 81  ? -30.98756 12.43043 14.91689  1.000 62.87602  ? 81  GLN A NE2  1 
ATOM   628  N N    . LYS A 1 82  ? -31.76741 17.35531 9.98672   1.000 52.17030  ? 82  LYS A N    1 
ATOM   629  C CA   . LYS A 1 82  ? -31.06557 18.39804 9.25442   1.000 53.02949  ? 82  LYS A CA   1 
ATOM   630  C C    . LYS A 1 82  ? -30.25963 19.25309 10.23610  1.000 52.40352  ? 82  LYS A C    1 
ATOM   631  O O    . LYS A 1 82  ? -30.72660 19.55616 11.33362  1.000 53.60061  ? 82  LYS A O    1 
ATOM   632  C CB   . LYS A 1 82  ? -32.09116 19.26108 8.52028   1.000 52.80419  ? 82  LYS A CB   1 
ATOM   633  C CG   . LYS A 1 82  ? -32.17265 19.07705 7.03986   1.000 56.91406  ? 82  LYS A CG   1 
ATOM   634  C CD   . LYS A 1 82  ? -32.88279 20.25577 6.36096   1.000 60.57474  ? 82  LYS A CD   1 
ATOM   635  C CE   . LYS A 1 82  ? -34.18481 19.78227 5.70150   1.000 66.99650  ? 82  LYS A CE   1 
ATOM   636  N NZ   . LYS A 1 82  ? -34.74641 20.80832 4.77080   1.000 64.34697  ? 82  LYS A NZ   1 
ATOM   637  N N    . PHE A 1 83  ? -29.05220 19.65065 9.83621   1.000 52.25512  ? 83  PHE A N    1 
ATOM   638  C CA   . PHE A 1 83  ? -28.24936 20.57569 10.63454  1.000 50.03958  ? 83  PHE A CA   1 
ATOM   639  C C    . PHE A 1 83  ? -28.74875 21.99762 10.42419  1.000 48.68603  ? 83  PHE A C    1 
ATOM   640  O O    . PHE A 1 83  ? -29.07308 22.39081 9.30031   1.000 50.02473  ? 83  PHE A O    1 
ATOM   641  C CB   . PHE A 1 83  ? -26.77498 20.53547 10.22115  1.000 49.20329  ? 83  PHE A CB   1 
ATOM   642  C CG   . PHE A 1 83  ? -26.06734 19.24460 10.52338  1.000 47.45805  ? 83  PHE A CG   1 
ATOM   643  C CD1  . PHE A 1 83  ? -25.99760 18.75826 11.80804  1.000 47.11451  ? 83  PHE A CD1  1 
ATOM   644  C CD2  . PHE A 1 83  ? -25.45365 18.53337 9.50900   1.000 45.58812  ? 83  PHE A CD2  1 
ATOM   645  C CE1  . PHE A 1 83  ? -25.33155 17.57435 12.09056  1.000 46.09259  ? 83  PHE A CE1  1 
ATOM   646  C CE2  . PHE A 1 83  ? -24.78540 17.34805 9.77231   1.000 45.16588  ? 83  PHE A CE2  1 
ATOM   647  C CZ   . PHE A 1 83  ? -24.73709 16.86598 11.09721  1.000 44.43610  ? 83  PHE A CZ   1 
ATOM   648  N N    . ARG A 1 84  ? -28.77043 22.78516 11.50279  1.000 49.27485  ? 84  ARG A N    1 
ATOM   649  C CA   . ARG A 1 84  ? -28.94357 24.22601 11.34982  1.000 49.31947  ? 84  ARG A CA   1 
ATOM   650  C C    . ARG A 1 84  ? -27.92032 24.78160 10.35604  1.000 47.49512  ? 84  ARG A C    1 
ATOM   651  O O    . ARG A 1 84  ? -26.74344 24.40477 10.36967  1.000 47.24445  ? 84  ARG A O    1 
ATOM   652  C CB   . ARG A 1 84  ? -28.82960 24.93045 12.71917  1.000 47.06466  ? 84  ARG A CB   1 
ATOM   653  C CG   . ARG A 1 84  ? -28.71874 26.45593 12.59451  1.000 46.39565  ? 84  ARG A CG   1 
ATOM   654  C CD   . ARG A 1 84  ? -28.79981 27.21698 13.88309  1.000 54.76648  ? 84  ARG A CD   1 
ATOM   655  N NE   . ARG A 1 84  ? -27.68396 26.91534 14.76478  1.000 59.24154  ? 84  ARG A NE   1 
ATOM   656  C CZ   . ARG A 1 84  ? -26.96695 27.82595 15.40684  1.000 58.62587  ? 84  ARG A CZ   1 
ATOM   657  N NH1  . ARG A 1 84  ? -27.19183 29.12628 15.24096  1.000 57.04007  ? 84  ARG A NH1  1 
ATOM   658  N NH2  . ARG A 1 84  ? -26.00714 27.42049 16.23885  1.000 53.76200  ? 84  ARG A NH2  1 
ATOM   659  N N    . ASP A 1 85  ? -28.37846 25.65041 9.45741   1.000 46.07221  ? 85  ASP A N    1 
ATOM   660  C CA   . ASP A 1 85  ? -27.50472 26.18496 8.41637   1.000 48.02287  ? 85  ASP A CA   1 
ATOM   661  C C    . ASP A 1 85  ? -26.62537 27.26344 9.01814   1.000 44.63725  ? 85  ASP A C    1 
ATOM   662  O O    . ASP A 1 85  ? -27.10343 28.35223 9.34929   1.000 47.76752  ? 85  ASP A O    1 
ATOM   663  C CB   . ASP A 1 85  ? -28.31685 26.73760 7.24393   1.000 45.71507  ? 85  ASP A CB   1 
ATOM   664  C CG   . ASP A 1 85  ? -27.46461 27.12050 6.04886   1.000 46.67794  ? 85  ASP A CG   1 
ATOM   665  O OD1  . ASP A 1 85  ? -26.20552 27.11739 6.12222   1.000 42.54194  ? 85  ASP A OD1  1 
ATOM   666  O OD2  . ASP A 1 85  ? -28.08256 27.39513 4.98363   1.000 48.63065  ? 85  ASP A OD2  1 
ATOM   667  N N    . ILE A 1 86  ? -25.33466 26.98324 9.14033   1.000 44.15511  ? 86  ILE A N    1 
ATOM   668  C CA   . ILE A 1 86  ? -24.41544 27.93100 9.75548   1.000 44.37943  ? 86  ILE A CA   1 
ATOM   669  C C    . ILE A 1 86  ? -23.44629 28.50652 8.73898   1.000 43.89120  ? 86  ILE A C    1 
ATOM   670  O O    . ILE A 1 86  ? -22.43157 29.11148 9.11338   1.000 40.77853  ? 86  ILE A O    1 
ATOM   671  C CB   . ILE A 1 86  ? -23.66372 27.30548 10.94834  1.000 43.51798  ? 86  ILE A CB   1 
ATOM   672  C CG1  . ILE A 1 86  ? -22.97028 25.99571 10.54872  1.000 42.33945  ? 86  ILE A CG1  1 
ATOM   673  C CG2  . ILE A 1 86  ? -24.58940 27.14407 12.14884  1.000 44.98104  ? 86  ILE A CG2  1 
ATOM   674  C CD1  . ILE A 1 86  ? -21.96168 25.54726 11.58671  1.000 44.90298  ? 86  ILE A CD1  1 
ATOM   675  N N    . ARG A 1 87  ? -23.73369 28.34226 7.44345   1.000 43.59876  ? 87  ARG A N    1 
ATOM   676  C CA   . ARG A 1 87  ? -22.80843 28.84013 6.45334   1.000 40.11750  ? 87  ARG A CA   1 
ATOM   677  C C    . ARG A 1 87  ? -22.60570 30.33906 6.60247   1.000 40.80209  ? 87  ARG A C    1 
ATOM   678  O O    . ARG A 1 87  ? -21.50642 30.84271 6.34245   1.000 42.70765  ? 87  ARG A O    1 
ATOM   679  C CB   . ARG A 1 87  ? -23.32644 28.48070 5.04640   1.000 42.42983  ? 87  ARG A CB   1 
ATOM   680  C CG   . ARG A 1 87  ? -23.04760 27.03427 4.68116   1.000 38.41147  ? 87  ARG A CG   1 
ATOM   681  C CD   . ARG A 1 87  ? -23.66505 26.70393 3.28495   1.000 45.45181  ? 87  ARG A CD   1 
ATOM   682  N NE   . ARG A 1 87  ? -25.12190 26.60852 3.36159   1.000 44.67198  ? 87  ARG A NE   1 
ATOM   683  C CZ   . ARG A 1 87  ? -25.85218 26.15496 2.35073   1.000 49.99247  ? 87  ARG A CZ   1 
ATOM   684  N NH1  . ARG A 1 87  ? -25.28360 25.78233 1.21544   1.000 49.58503  ? 87  ARG A NH1  1 
ATOM   685  N NH2  . ARG A 1 87  ? -27.17657 26.07579 2.47967   1.000 46.44746  ? 87  ARG A NH2  1 
ATOM   686  N N    . HIS A 1 88  ? -23.63860 31.07468 7.01346   1.000 40.92225  ? 88  HIS A N    1 
ATOM   687  C CA   . HIS A 1 88  ? -23.44162 32.51579 7.14183   1.000 44.93818  ? 88  HIS A CA   1 
ATOM   688  C C    . HIS A 1 88  ? -22.48095 32.88000 8.28244   1.000 47.43600  ? 88  HIS A C    1 
ATOM   689  O O    . HIS A 1 88  ? -22.05409 34.04252 8.35764   1.000 45.46313  ? 88  HIS A O    1 
ATOM   690  C CB   . HIS A 1 88  ? -24.77925 33.25504 7.33993   1.000 44.61144  ? 88  HIS A CB   1 
ATOM   691  C CG   . HIS A 1 88  ? -25.46219 32.98344 8.66030   1.000 52.54301  ? 88  HIS A CG   1 
ATOM   692  N ND1  . HIS A 1 88  ? -25.47962 33.91066 9.68272   1.000 53.01528  ? 88  HIS A ND1  1 
ATOM   693  C CD2  . HIS A 1 88  ? -26.19049 31.92648 9.10540   1.000 52.13953  ? 88  HIS A CD2  1 
ATOM   694  C CE1  . HIS A 1 88  ? -26.17280 33.43240 10.70608  1.000 52.00013  ? 88  HIS A CE1  1 
ATOM   695  N NE2  . HIS A 1 88  ? -26.60909 32.22499 10.38716  1.000 50.96645  ? 88  HIS A NE2  1 
ATOM   696  N N    . PHE A 1 89  ? -22.11322 31.93378 9.16258   1.000 43.58318  ? 89  PHE A N    1 
ATOM   697  C CA   . PHE A 1 89  ? -21.07472 32.19913 10.15387  1.000 43.24705  ? 89  PHE A CA   1 
ATOM   698  C C    . PHE A 1 89  ? -19.68547 31.89068 9.64683   1.000 43.15496  ? 89  PHE A C    1 
ATOM   699  O O    . PHE A 1 89  ? -18.72216 32.04266 10.40886  1.000 41.71501  ? 89  PHE A O    1 
ATOM   700  C CB   . PHE A 1 89  ? -21.32167 31.38696 11.44540  1.000 43.46860  ? 89  PHE A CB   1 
ATOM   701  C CG   . PHE A 1 89  ? -22.51952 31.81855 12.17061  1.000 45.81653  ? 89  PHE A CG   1 
ATOM   702  C CD1  . PHE A 1 89  ? -22.69792 33.16383 12.49714  1.000 46.72145  ? 89  PHE A CD1  1 
ATOM   703  C CD2  . PHE A 1 89  ? -23.49505 30.90472 12.53456  1.000 48.52429  ? 89  PHE A CD2  1 
ATOM   704  C CE1  . PHE A 1 89  ? -23.82998 33.58579 13.19539  1.000 49.43465  ? 89  PHE A CE1  1 
ATOM   705  C CE2  . PHE A 1 89  ? -24.62725 31.32167 13.25376  1.000 49.61281  ? 89  PHE A CE2  1 
ATOM   706  C CZ   . PHE A 1 89  ? -24.80342 32.66610 13.55620  1.000 48.20081  ? 89  PHE A CZ   1 
ATOM   707  N N    . LEU A 1 90  ? -19.55554 31.46456 8.36227   1.000 41.06728  ? 90  LEU A N    1 
ATOM   708  C CA   . LEU A 1 90  ? -18.22247 31.09724 7.91121   1.000 40.33344  ? 90  LEU A CA   1 
ATOM   709  C C    . LEU A 1 90  ? -17.49929 32.31006 7.33589   1.000 39.59944  ? 90  LEU A C    1 
ATOM   710  O O    . LEU A 1 90  ? -18.11606 33.13785 6.66713   1.000 44.56640  ? 90  LEU A O    1 
ATOM   711  C CB   . LEU A 1 90  ? -18.29316 30.00925 6.84997   1.000 44.13093  ? 90  LEU A CB   1 
ATOM   712  C CG   . LEU A 1 90  ? -18.91924 28.68775 7.29614   1.000 42.58938  ? 90  LEU A CG   1 
ATOM   713  C CD1  . LEU A 1 90  ? -19.08673 27.83188 6.03690   1.000 41.57809  ? 90  LEU A CD1  1 
ATOM   714  C CD2  . LEU A 1 90  ? -18.06612 27.94481 8.29266   1.000 41.24705  ? 90  LEU A CD2  1 
ATOM   715  N N    . PRO A 1 91  ? -16.20272 32.41501 7.59088   1.000 40.49352  ? 91  PRO A N    1 
ATOM   716  C CA   . PRO A 1 91  ? -15.41920 33.48724 6.98867   1.000 43.45118  ? 91  PRO A CA   1 
ATOM   717  C C    . PRO A 1 91  ? -15.37447 33.40734 5.46495   1.000 42.55010  ? 91  PRO A C    1 
ATOM   718  O O    . PRO A 1 91  ? -15.27067 32.33899 4.84810   1.000 37.82292  ? 91  PRO A O    1 
ATOM   719  C CB   . PRO A 1 91  ? -14.01858 33.28833 7.57651   1.000 42.01281  ? 91  PRO A CB   1 
ATOM   720  C CG   . PRO A 1 91  ? -14.14694 32.25402 8.61011   1.000 44.86030  ? 91  PRO A CG   1 
ATOM   721  C CD   . PRO A 1 91  ? -15.36778 31.49048 8.37519   1.000 43.13820  ? 91  PRO A CD   1 
ATOM   722  N N    . ARG A 1 92  ? -15.38813 34.57923 4.87149   1.000 41.44787  ? 92  ARG A N    1 
ATOM   723  C CA   . ARG A 1 92  ? -15.22447 34.64841 3.43091   1.000 43.82824  ? 92  ARG A CA   1 
ATOM   724  C C    . ARG A 1 92  ? -13.76997 34.45063 3.02208   1.000 44.34489  ? 92  ARG A C    1 
ATOM   725  O O    . ARG A 1 92  ? -13.49017 33.71047 2.08894   1.000 47.85706  ? 92  ARG A O    1 
ATOM   726  C CB   . ARG A 1 92  ? -15.75134 35.96988 2.93958   1.000 44.73670  ? 92  ARG A CB   1 
ATOM   727  C CG   . ARG A 1 92  ? -15.54445 36.09757 1.45847   1.000 52.07353  ? 92  ARG A CG   1 
ATOM   728  C CD   . ARG A 1 92  ? -16.14686 37.36852 0.94325   1.000 56.88491  ? 92  ARG A CD   1 
ATOM   729  N NE   . ARG A 1 92  ? -17.59216 37.22799 0.79217   1.000 65.54414  ? 92  ARG A NE   1 
ATOM   730  C CZ   . ARG A 1 92  ? -18.35239 38.09536 0.13911   1.000 75.11458  ? 92  ARG A CZ   1 
ATOM   731  N NH1  . ARG A 1 92  ? -17.81986 39.12173 -0.51906  1.000 71.69062  ? 92  ARG A NH1  1 
ATOM   732  N NH2  . ARG A 1 92  ? -19.67172 37.90874 0.11162   1.000 81.18121  ? 92  ARG A NH2  1 
ATOM   733  N N    . TYR A 1 93  ? -12.83270 35.04809 3.73589   1.000 46.19539  ? 93  TYR A N    1 
ATOM   734  C CA   . TYR A 1 93  ? -11.42732 35.02020 3.37476   1.000 42.06008  ? 93  TYR A CA   1 
ATOM   735  C C    . TYR A 1 93  ? -10.55820 34.45161 4.48595   1.000 45.52929  ? 93  TYR A C    1 
ATOM   736  O O    . TYR A 1 93  ? -10.99175 34.31816 5.62905   1.000 43.75987  ? 93  TYR A O    1 
ATOM   737  C CB   . TYR A 1 93  ? -10.95606 36.44118 3.02634   1.000 46.72189  ? 93  TYR A CB   1 
ATOM   738  C CG   . TYR A 1 93  ? -11.66081 37.02406 1.81333   1.000 47.06339  ? 93  TYR A CG   1 
ATOM   739  C CD1  . TYR A 1 93  ? -11.61169 36.37580 0.55870   1.000 46.13654  ? 93  TYR A CD1  1 
ATOM   740  C CD2  . TYR A 1 93  ? -12.40535 38.19301 1.92276   1.000 47.94554  ? 93  TYR A CD2  1 
ATOM   741  C CE1  . TYR A 1 93  ? -12.27286 36.92693 -0.57880  1.000 45.56177  ? 93  TYR A CE1  1 
ATOM   742  C CE2  . TYR A 1 93  ? -13.07172 38.72977 0.82275   1.000 50.72914  ? 93  TYR A CE2  1 
ATOM   743  C CZ   . TYR A 1 93  ? -12.99429 38.10711 -0.41302  1.000 48.78931  ? 93  TYR A CZ   1 
ATOM   744  O OH   . TYR A 1 93  ? -13.66362 38.69944 -1.43618  1.000 51.85572  ? 93  TYR A OH   1 
ATOM   745  N N    . GLU A 1 94  ? -9.31102  34.11074 4.14100   1.000 43.88197  ? 94  GLU A N    1 
ATOM   746  C CA   . GLU A 1 94  ? -8.27330  33.91947 5.14878   1.000 46.74586  ? 94  GLU A CA   1 
ATOM   747  C C    . GLU A 1 94  ? -8.11292  35.16358 6.02752   1.000 45.57217  ? 94  GLU A C    1 
ATOM   748  O O    . GLU A 1 94  ? -8.25729  36.30507 5.56827   1.000 44.05348  ? 94  GLU A O    1 
ATOM   749  C CB   . GLU A 1 94  ? -6.94736  33.57469 4.47112   1.000 46.63022  ? 94  GLU A CB   1 
ATOM   750  C CG   . GLU A 1 94  ? -7.03948  32.52492 3.37020   1.000 47.27679  ? 94  GLU A CG   1 
ATOM   751  C CD   . GLU A 1 94  ? -5.66362  32.07870 2.87194   1.000 48.66389  ? 94  GLU A CD   1 
ATOM   752  O OE1  . GLU A 1 94  ? -4.68159  32.81462 3.12482   1.000 49.10570  ? 94  GLU A OE1  1 
ATOM   753  O OE2  . GLU A 1 94  ? -5.53921  30.97314 2.28248   1.000 51.52144  ? 94  GLU A OE2  1 
ATOM   754  N N    . ASP A 1 95  ? -7.80465  34.94163 7.30968   1.000 46.04123  ? 95  ASP A N    1 
ATOM   755  C CA   . ASP A 1 95  ? -7.70794  36.05418 8.26034   1.000 46.58190  ? 95  ASP A CA   1 
ATOM   756  C C    . ASP A 1 95  ? -7.00976  35.57642 9.53867   1.000 47.89799  ? 95  ASP A C    1 
ATOM   757  O O    . ASP A 1 95  ? -6.88137  34.37165 9.77381   1.000 44.33603  ? 95  ASP A O    1 
ATOM   758  C CB   . ASP A 1 95  ? -9.10246  36.61300 8.59101   1.000 47.49446  ? 95  ASP A CB   1 
ATOM   759  C CG   . ASP A 1 95  ? -9.08398  38.10007 8.89375   1.000 52.25835  ? 95  ASP A CG   1 
ATOM   760  O OD1  . ASP A 1 95  ? -7.99290  38.67740 9.03427   1.000 54.16785  ? 95  ASP A OD1  1 
ATOM   761  O OD2  . ASP A 1 95  ? -10.17177 38.68895 9.00122   1.000 54.16791  ? 95  ASP A OD2  1 
ATOM   762  N N    . ASP A 1 96  ? -6.52872  36.52959 10.34699  1.000 47.26356  ? 96  ASP A N    1 
ATOM   763  C CA   . ASP A 1 96  ? -6.17529  36.22932 11.72472  1.000 51.25265  ? 96  ASP A CA   1 
ATOM   764  C C    . ASP A 1 96  ? -7.31289  36.65264 12.62327  1.000 49.88958  ? 96  ASP A C    1 
ATOM   765  O O    . ASP A 1 96  ? -8.18258  37.43269 12.21545  1.000 49.60052  ? 96  ASP A O    1 
ATOM   766  C CB   . ASP A 1 96  ? -4.89704  36.92819 12.18769  1.000 57.06415  ? 96  ASP A CB   1 
ATOM   767  C CG   . ASP A 1 96  ? -3.82235  36.89682 11.15667  1.000 57.88979  ? 96  ASP A CG   1 
ATOM   768  O OD1  . ASP A 1 96  ? -3.55020  37.96923 10.58467  1.000 67.45224  ? 96  ASP A OD1  1 
ATOM   769  O OD2  . ASP A 1 96  ? -3.29723  35.79508 10.87512  1.000 62.68137  ? 96  ASP A OD2  1 
ATOM   770  N N    . TYR A 1 97  ? -7.28109  36.15078 13.87502  1.000 47.18421  ? 97  TYR A N    1 
ATOM   771  C CA   . TYR A 1 97  ? -8.40622  36.30830 14.76892  1.000 47.46545  ? 97  TYR A CA   1 
ATOM   772  C C    . TYR A 1 97  ? -7.90556  36.50659 16.18411  1.000 45.42743  ? 97  TYR A C    1 
ATOM   773  O O    . TYR A 1 97  ? -6.81858  36.03928 16.55473  1.000 42.79723  ? 97  TYR A O    1 
ATOM   774  C CB   . TYR A 1 97  ? -9.33171  35.08410 14.73926  1.000 46.88831  ? 97  TYR A CB   1 
ATOM   775  C CG   . TYR A 1 97  ? -9.97477  34.91774 13.39795  1.000 44.16267  ? 97  TYR A CG   1 
ATOM   776  C CD1  . TYR A 1 97  ? -9.37054  34.16444 12.40723  1.000 45.65456  ? 97  TYR A CD1  1 
ATOM   777  C CD2  . TYR A 1 97  ? -11.18367 35.54278 13.11984  1.000 44.66487  ? 97  TYR A CD2  1 
ATOM   778  C CE1  . TYR A 1 97  ? -9.97555  34.02531 11.11815  1.000 41.93315  ? 97  TYR A CE1  1 
ATOM   779  C CE2  . TYR A 1 97  ? -11.78139 35.42789 11.86136  1.000 47.20522  ? 97  TYR A CE2  1 
ATOM   780  C CZ   . TYR A 1 97  ? -11.17788 34.66757 10.87550  1.000 45.41730  ? 97  TYR A CZ   1 
ATOM   781  O OH   . TYR A 1 97  ? -11.79466 34.56824 9.64555   1.000 47.38328  ? 97  TYR A OH   1 
ATOM   782  N N    . ASN A 1 98  ? -8.73377  37.16494 16.97368  1.000 47.88103  ? 98  ASN A N    1 
ATOM   783  C CA   . ASN A 1 98  ? -8.44150  37.37272 18.39073  1.000 47.22231  ? 98  ASN A CA   1 
ATOM   784  C C    . ASN A 1 98  ? -9.25578  36.43770 19.26905  1.000 50.60379  ? 98  ASN A C    1 
ATOM   785  O O    . ASN A 1 98  ? -10.45754 36.24527 19.05013  1.000 49.94417  ? 98  ASN A O    1 
ATOM   786  C CB   . ASN A 1 98  ? -8.76640  38.80334 18.79182  1.000 48.25029  ? 98  ASN A CB   1 
ATOM   787  C CG   . ASN A 1 98  ? -7.92271  39.80064 18.07062  1.000 55.66537  ? 98  ASN A CG   1 
ATOM   788  O OD1  . ASN A 1 98  ? -8.45000  40.73528 17.43427  1.000 55.66531  ? 98  ASN A OD1  1 
ATOM   789  N ND2  . ASN A 1 98  ? -6.60366  39.58626 18.10142  1.000 54.61412  ? 98  ASN A ND2  1 
ATOM   790  N N    . ASP A 1 99  ? -8.59604  35.89119 20.29338  1.000 51.41508  ? 99  ASP A N    1 
ATOM   791  C CA   . ASP A 1 99  ? -9.25391  35.32934 21.47274  1.000 51.68347  ? 99  ASP A CA   1 
ATOM   792  C C    . ASP A 1 99  ? -10.28165 34.25083 21.09019  1.000 50.53459  ? 99  ASP A C    1 
ATOM   793  O O    . ASP A 1 99  ? -11.46742 34.31211 21.44621  1.000 50.94028  ? 99  ASP A O    1 
ATOM   794  C CB   . ASP A 1 99  ? -9.87554  36.45569 22.30178  1.000 54.49545  ? 99  ASP A CB   1 
ATOM   795  C CG   . ASP A 1 99  ? -10.32738 35.98259 23.66417  1.000 63.44545  ? 99  ASP A CG   1 
ATOM   796  O OD1  . ASP A 1 99  ? -9.55030  35.23683 24.31517  1.000 64.74295  ? 99  ASP A OD1  1 
ATOM   797  O OD2  . ASP A 1 99  ? -11.41797 36.40033 24.12037  1.000 65.81333  ? 99  ASP A OD2  1 
ATOM   798  N N    . ALA A 1 100 ? -9.79433  33.22688 20.38782  1.000 45.25070  ? 100 ALA A N    1 
ATOM   799  C CA   . ALA A 1 100 ? -10.69975 32.20633 19.87474  1.000 47.63596  ? 100 ALA A CA   1 
ATOM   800  C C    . ALA A 1 100 ? -10.98000 31.13242 20.92659  1.000 41.93787  ? 100 ALA A C    1 
ATOM   801  O O    . ALA A 1 100 ? -10.22762 30.95354 21.88674  1.000 44.19672  ? 100 ALA A O    1 
ATOM   802  C CB   . ALA A 1 100 ? -10.13000 31.56452 18.59299  1.000 39.25988  ? 100 ALA A CB   1 
ATOM   803  N N    . VAL A 1 101 ? -12.06937 30.38415 20.71112  1.000 40.93485  ? 101 VAL A N    1 
ATOM   804  C CA   . VAL A 1 101 ? -12.41753 29.23443 21.54378  1.000 43.41680  ? 101 VAL A CA   1 
ATOM   805  C C    . VAL A 1 101 ? -12.36371 27.96750 20.69679  1.000 41.72761  ? 101 VAL A C    1 
ATOM   806  O O    . VAL A 1 101 ? -12.81417 27.95690 19.54062  1.000 42.16418  ? 101 VAL A O    1 
ATOM   807  C CB   . VAL A 1 101 ? -13.80518 29.40306 22.19068  1.000 44.56378  ? 101 VAL A CB   1 
ATOM   808  C CG1  . VAL A 1 101 ? -14.18790 28.13895 22.98695  1.000 39.55544  ? 101 VAL A CG1  1 
ATOM   809  C CG2  . VAL A 1 101 ? -13.81258 30.65533 23.10052  1.000 42.92247  ? 101 VAL A CG2  1 
ATOM   810  N N    . LEU A 1 102 ? -11.77754 26.91214 21.27179  1.000 40.03437  ? 102 LEU A N    1 
ATOM   811  C CA   . LEU A 1 102 ? -11.74816 25.56218 20.72602  1.000 35.40306  ? 102 LEU A CA   1 
ATOM   812  C C    . LEU A 1 102 ? -12.69526 24.68271 21.53509  1.000 41.86048  ? 102 LEU A C    1 
ATOM   813  O O    . LEU A 1 102 ? -12.55790 24.56391 22.76970  1.000 38.82178  ? 102 LEU A O    1 
ATOM   814  C CB   . LEU A 1 102 ? -10.32808 25.00394 20.76651  1.000 31.73164  ? 102 LEU A CB   1 
ATOM   815  C CG   . LEU A 1 102 ? -10.27090 23.51433 20.43138  1.000 37.34598  ? 102 LEU A CG   1 
ATOM   816  C CD1  . LEU A 1 102 ? -10.63274 23.28736 18.93324  1.000 38.79628  ? 102 LEU A CD1  1 
ATOM   817  C CD2  . LEU A 1 102 ? -8.86363  22.96852 20.71009  1.000 41.54665  ? 102 LEU A CD2  1 
ATOM   818  N N    . SER A 1 103 ? -13.64772 24.06482 20.85047  1.000 40.74803  ? 103 SER A N    1 
ATOM   819  C CA   . SER A 1 103 ? -14.78948 23.40832 21.48220  1.000 40.38444  ? 103 SER A CA   1 
ATOM   820  C C    . SER A 1 103 ? -14.84071 21.94706 21.04612  1.000 43.58076  ? 103 SER A C    1 
ATOM   821  O O    . SER A 1 103 ? -14.88818 21.66982 19.84032  1.000 38.84624  ? 103 SER A O    1 
ATOM   822  C CB   . SER A 1 103 ? -16.06737 24.11006 21.03989  1.000 43.60723  ? 103 SER A CB   1 
ATOM   823  O OG   . SER A 1 103 ? -16.21723 25.32634 21.73771  1.000 49.22805  ? 103 SER A OG   1 
ATOM   824  N N    . VAL A 1 104 ? -14.88923 21.01941 22.00856  1.000 38.09767  ? 104 VAL A N    1 
ATOM   825  C CA   . VAL A 1 104 ? -14.79164 19.58401 21.73604  1.000 40.12928  ? 104 VAL A CA   1 
ATOM   826  C C    . VAL A 1 104 ? -16.09000 18.88600 22.12104  1.000 45.71378  ? 104 VAL A C    1 
ATOM   827  O O    . VAL A 1 104 ? -16.71338 19.20683 23.14839  1.000 43.28863  ? 104 VAL A O    1 
ATOM   828  C CB   . VAL A 1 104 ? -13.59993 18.94556 22.47029  1.000 44.01406  ? 104 VAL A CB   1 
ATOM   829  C CG1  . VAL A 1 104 ? -13.57099 17.44483 22.23816  1.000 44.89657  ? 104 VAL A CG1  1 
ATOM   830  C CG2  . VAL A 1 104 ? -12.32200 19.50571 21.91502  1.000 41.28790  ? 104 VAL A CG2  1 
ATOM   831  N N    . HIS A 1 105 ? -16.47718 17.89750 21.30473  1.000 42.69154  ? 105 HIS A N    1 
ATOM   832  C CA   . HIS A 1 105 ? -17.66574 17.05306 21.54557  1.000 45.38715  ? 105 HIS A CA   1 
ATOM   833  C C    . HIS A 1 105 ? -17.29022 15.61520 21.15670  1.000 46.38572  ? 105 HIS A C    1 
ATOM   834  O O    . HIS A 1 105 ? -17.36498 15.23036 19.98840  1.000 39.29201  ? 105 HIS A O    1 
ATOM   835  C CB   . HIS A 1 105 ? -18.86777 17.57686 20.75774  1.000 42.84531  ? 105 HIS A CB   1 
ATOM   836  C CG   . HIS A 1 105 ? -20.14969 16.80134 20.96002  1.000 46.04776  ? 105 HIS A CG   1 
ATOM   837  N ND1  . HIS A 1 105 ? -21.35910 17.23331 20.45561  1.000 47.55101  ? 105 HIS A ND1  1 
ATOM   838  C CD2  . HIS A 1 105 ? -20.42203 15.66344 21.64837  1.000 46.77540  ? 105 HIS A CD2  1 
ATOM   839  C CE1  . HIS A 1 105 ? -22.31321 16.38160 20.78898  1.000 47.88092  ? 105 HIS A CE1  1 
ATOM   840  N NE2  . HIS A 1 105 ? -21.77066 15.42029 21.51499  1.000 47.18204  ? 105 HIS A NE2  1 
ATOM   841  N N    . THR A 1 106 ? -16.81898 14.83610 22.12757  1.000 42.35845  ? 106 THR A N    1 
ATOM   842  C CA   . THR A 1 106 ? -16.48570 13.42670 21.93779  1.000 43.61571  ? 106 THR A CA   1 
ATOM   843  C C    . THR A 1 106 ? -17.19973 12.62592 23.02288  1.000 46.40414  ? 106 THR A C    1 
ATOM   844  O O    . THR A 1 106 ? -17.87784 13.18995 23.88432  1.000 46.31139  ? 106 THR A O    1 
ATOM   845  C CB   . THR A 1 106 ? -14.96862 13.16948 21.99910  1.000 45.62795  ? 106 THR A CB   1 
ATOM   846  O OG1  . THR A 1 106 ? -14.48327 13.43020 23.33567  1.000 43.72819  ? 106 THR A OG1  1 
ATOM   847  C CG2  . THR A 1 106 ? -14.21696 14.02975 21.00491  1.000 45.27517  ? 106 THR A CG2  1 
ATOM   848  N N    . SER A 1 107 ? -17.06024 11.29759 22.99140  1.000 44.78960  ? 107 SER A N    1 
ATOM   849  C CA   . SER A 1 107 ? -17.63552 10.51497 24.08674  1.000 47.71191  ? 107 SER A CA   1 
ATOM   850  C C    . SER A 1 107 ? -16.92988 10.82157 25.40438  1.000 45.23869  ? 107 SER A C    1 
ATOM   851  O O    . SER A 1 107 ? -17.57928 10.94488 26.43956  1.000 48.34716  ? 107 SER A O    1 
ATOM   852  C CB   . SER A 1 107 ? -17.55630 9.02510  23.76657  1.000 48.64107  ? 107 SER A CB   1 
ATOM   853  O OG   . SER A 1 107 ? -18.39413 8.71601  22.65748  1.000 54.36816  ? 107 SER A OG   1 
ATOM   854  N N    . LYS A 1 108 ? -15.59469 10.92557 25.37369  1.000 46.58142  ? 108 LYS A N    1 
ATOM   855  C CA   . LYS A 1 108 ? -14.79523 11.23728 26.55313  1.000 49.02397  ? 108 LYS A CA   1 
ATOM   856  C C    . LYS A 1 108 ? -15.07792 12.64901 27.05607  1.000 50.69018  ? 108 LYS A C    1 
ATOM   857  O O    . LYS A 1 108 ? -15.10790 12.89965 28.27985  1.000 45.19547  ? 108 LYS A O    1 
ATOM   858  C CB   . LYS A 1 108 ? -13.31190 11.08364 26.18857  1.000 49.03892  ? 108 LYS A CB   1 
ATOM   859  C CG   . LYS A 1 108 ? -12.30755 11.43911 27.30987  1.000 54.25142  ? 108 LYS A CG   1 
ATOM   860  C CD   . LYS A 1 108 ? -11.06135 10.51890 27.23351  1.000 57.77513  ? 108 LYS A CD   1 
ATOM   861  C CE   . LYS A 1 108 ? -10.13524 10.63856 28.48092  1.000 61.27151  ? 108 LYS A CE   1 
ATOM   862  N NZ   . LYS A 1 108 ? -10.88674 10.90341 29.73814  1.000 60.07707  ? 108 LYS A NZ   1 
ATOM   863  N N    . PHE A 1 109 ? -15.26680 13.59306 26.12585  1.000 44.76166  ? 109 PHE A N    1 
ATOM   864  C CA   . PHE A 1 109 ? -15.51372 15.00078 26.45586  1.000 46.68127  ? 109 PHE A CA   1 
ATOM   865  C C    . PHE A 1 109 ? -16.76596 15.46165 25.71846  1.000 46.92039  ? 109 PHE A C    1 
ATOM   866  O O    . PHE A 1 109 ? -16.69436 15.97945 24.59052  1.000 48.21787  ? 109 PHE A O    1 
ATOM   867  C CB   . PHE A 1 109 ? -14.30617 15.86929 26.10366  1.000 48.89465  ? 109 PHE A CB   1 
ATOM   868  C CG   . PHE A 1 109 ? -13.09448 15.61943 26.96249  1.000 50.83347  ? 109 PHE A CG   1 
ATOM   869  C CD1  . PHE A 1 109 ? -13.00458 16.14730 28.22839  1.000 54.01650  ? 109 PHE A CD1  1 
ATOM   870  C CD2  . PHE A 1 109 ? -12.03754 14.87849 26.48435  1.000 50.51513  ? 109 PHE A CD2  1 
ATOM   871  C CE1  . PHE A 1 109 ? -11.88470 15.92376 29.01418  1.000 54.76175  ? 109 PHE A CE1  1 
ATOM   872  C CE2  . PHE A 1 109 ? -10.90966 14.65153 27.24959  1.000 55.02503  ? 109 PHE A CE2  1 
ATOM   873  C CZ   . PHE A 1 109 ? -10.83490 15.16793 28.51942  1.000 53.15690  ? 109 PHE A CZ   1 
ATOM   874  N N    . PRO A 1 110 ? -17.93949 15.26074 26.31373  1.000 48.59464  ? 110 PRO A N    1 
ATOM   875  C CA   . PRO A 1 110 ? -19.19352 15.58106 25.60439  1.000 47.69492  ? 110 PRO A CA   1 
ATOM   876  C C    . PRO A 1 110 ? -19.40259 17.06671 25.37453  1.000 47.62010  ? 110 PRO A C    1 
ATOM   877  O O    . PRO A 1 110 ? -20.16359 17.42107 24.46985  1.000 50.01858  ? 110 PRO A O    1 
ATOM   878  C CB   . PRO A 1 110 ? -20.27786 15.02624 26.54804  1.000 47.96143  ? 110 PRO A CB   1 
ATOM   879  C CG   . PRO A 1 110 ? -19.55894 13.97937 27.39166  1.000 47.58915  ? 110 PRO A CG   1 
ATOM   880  C CD   . PRO A 1 110 ? -18.18304 14.56070 27.59222  1.000 46.53818  ? 110 PRO A CD   1 
ATOM   881  N N    . ASN A 1 111 ? -18.88441 17.94784 26.23186  1.000 48.84862  ? 111 ASN A N    1 
ATOM   882  C CA   . ASN A 1 111 ? -18.61831 19.30105 25.76132  1.000 47.32188  ? 111 ASN A CA   1 
ATOM   883  C C    . ASN A 1 111 ? -17.64897 20.01816 26.66731  1.000 48.69058  ? 111 ASN A C    1 
ATOM   884  O O    . ASN A 1 111 ? -17.74999 19.98293 27.89975  1.000 46.42173  ? 111 ASN A O    1 
ATOM   885  C CB   . ASN A 1 111 ? -19.89197 20.13014 25.49839  1.000 50.67569  ? 111 ASN A CB   1 
ATOM   886  C CG   . ASN A 1 111 ? -20.51446 20.70524 26.68294  1.000 53.65257  ? 111 ASN A CG   1 
ATOM   887  O OD1  . ASN A 1 111 ? -20.20710 20.36620 27.83764  1.000 58.24163  ? 111 ASN A OD1  1 
ATOM   888  N ND2  . ASN A 1 111 ? -21.39877 21.67743 26.42759  1.000 55.74447  ? 111 ASN A ND2  1 
ATOM   889  N N    . MET A 1 112 ? -16.66752 20.61560 26.03355  1.000 44.19882  ? 112 MET A N    1 
ATOM   890  C CA   . MET A 1 112 ? -15.53444 21.19534 26.71844  1.000 42.87888  ? 112 MET A CA   1 
ATOM   891  C C    . MET A 1 112 ? -15.06387 22.35364 25.88042  1.000 43.94955  ? 112 MET A C    1 
ATOM   892  O O    . MET A 1 112 ? -15.11699 22.29223 24.64164  1.000 41.46996  ? 112 MET A O    1 
ATOM   893  C CB   . MET A 1 112 ? -14.44065 20.17159 26.88995  1.000 46.04221  ? 112 MET A CB   1 
ATOM   894  C CG   . MET A 1 112 ? -13.05214 20.72471 26.69877  1.000 50.47457  ? 112 MET A CG   1 
ATOM   895  S SD   . MET A 1 112 ? -11.90723 19.34939 26.94655  1.000 70.62297  ? 112 MET A SD   1 
ATOM   896  N N    . TYR A 1 113 ? -14.66226 23.42194 26.54519  1.000 40.03287  ? 113 TYR A N    1 
ATOM   897  C CA   . TYR A 1 113 ? -14.29358 24.64667 25.85827  1.000 38.71363  ? 113 TYR A CA   1 
ATOM   898  C C    . TYR A 1 113 ? -12.91209 25.07145 26.30523  1.000 42.48176  ? 113 TYR A C    1 
ATOM   899  O O    . TYR A 1 113 ? -12.61416 25.06182 27.51030  1.000 39.42406  ? 113 TYR A O    1 
ATOM   900  C CB   . TYR A 1 113 ? -15.31104 25.74611 26.12145  1.000 38.14838  ? 113 TYR A CB   1 
ATOM   901  C CG   . TYR A 1 113 ? -16.70396 25.31833 25.74637  1.000 41.48916  ? 113 TYR A CG   1 
ATOM   902  C CD1  . TYR A 1 113 ? -17.47604 24.51502 26.58194  1.000 41.05024  ? 113 TYR A CD1  1 
ATOM   903  C CD2  . TYR A 1 113 ? -17.20929 25.64084 24.49037  1.000 42.88303  ? 113 TYR A CD2  1 
ATOM   904  C CE1  . TYR A 1 113 ? -18.75805 24.09401 26.21903  1.000 42.62989  ? 113 TYR A CE1  1 
ATOM   905  C CE2  . TYR A 1 113 ? -18.47789 25.22904 24.10271  1.000 40.98669  ? 113 TYR A CE2  1 
ATOM   906  C CZ   . TYR A 1 113 ? -19.23642 24.45181 24.94533  1.000 45.30484  ? 113 TYR A CZ   1 
ATOM   907  O OH   . TYR A 1 113 ? -20.48283 24.05751 24.51359  1.000 45.48754  ? 113 TYR A OH   1 
ATOM   908  N N    . ILE A 1 114 ? -12.07145 25.41967 25.33625  1.000 33.90175  ? 114 ILE A N    1 
ATOM   909  C CA   . ILE A 1 114 ? -10.69012 25.79075 25.60764  1.000 38.20282  ? 114 ILE A CA   1 
ATOM   910  C C    . ILE A 1 114 ? -10.42475 27.13386 24.94991  1.000 39.17501  ? 114 ILE A C    1 
ATOM   911  O O    . ILE A 1 114 ? -10.45525 27.22019 23.71173  1.000 42.59578  ? 114 ILE A O    1 
ATOM   912  C CB   . ILE A 1 114 ? -9.70788  24.73937 25.08380  1.000 35.06534  ? 114 ILE A CB   1 
ATOM   913  C CG1  . ILE A 1 114 ? -9.88612  23.42521 25.80159  1.000 44.06030  ? 114 ILE A CG1  1 
ATOM   914  C CG2  . ILE A 1 114 ? -8.27601  25.25586 25.18099  1.000 38.33251  ? 114 ILE A CG2  1 
ATOM   915  C CD1  . ILE A 1 114 ? -9.19058  22.28711 25.14677  1.000 42.82764  ? 114 ILE A CD1  1 
ATOM   916  N N    . PRO A 1 115 ? -10.17610 28.20313 25.70806  1.000 43.08761  ? 115 PRO A N    1 
ATOM   917  C CA   . PRO A 1 115 ? -9.76471  29.47172 25.07526  1.000 42.86915  ? 115 PRO A CA   1 
ATOM   918  C C    . PRO A 1 115 ? -8.33436  29.31947 24.58343  1.000 45.25317  ? 115 PRO A C    1 
ATOM   919  O O    . PRO A 1 115 ? -7.45176  28.95339 25.35510  1.000 44.14517  ? 115 PRO A O    1 
ATOM   920  C CB   . PRO A 1 115 ? -9.88438  30.50420 26.21029  1.000 46.43357  ? 115 PRO A CB   1 
ATOM   921  C CG   . PRO A 1 115 ? -10.62677 29.78013 27.33428  1.000 44.95814  ? 115 PRO A CG   1 
ATOM   922  C CD   . PRO A 1 115 ? -10.32983 28.32959 27.18332  1.000 40.93533  ? 115 PRO A CD   1 
ATOM   923  N N    . VAL A 1 116 ? -8.12017  29.47986 23.26445  1.000 43.32117  ? 116 VAL A N    1 
ATOM   924  C CA   . VAL A 1 116 ? -6.78545  29.24495 22.72892  1.000 40.94484  ? 116 VAL A CA   1 
ATOM   925  C C    . VAL A 1 116 ? -6.00005  30.52970 22.48271  1.000 41.06132  ? 116 VAL A C    1 
ATOM   926  O O    . VAL A 1 116 ? -4.81196  30.45010 22.11992  1.000 42.43631  ? 116 VAL A O    1 
ATOM   927  C CB   . VAL A 1 116 ? -6.85550  28.39810 21.43613  1.000 42.82542  ? 116 VAL A CB   1 
ATOM   928  C CG1  . VAL A 1 116 ? -7.28990  26.96061 21.77613  1.000 42.13519  ? 116 VAL A CG1  1 
ATOM   929  C CG2  . VAL A 1 116 ? -7.83813  29.04827 20.46987  1.000 38.41433  ? 116 VAL A CG2  1 
ATOM   930  N N    . GLY A 1 117 ? -6.60662  31.70418 22.68169  1.000 42.79796  ? 117 GLY A N    1 
ATOM   931  C CA   . GLY A 1 117 ? -5.90104  32.96524 22.44537  1.000 43.40235  ? 117 GLY A CA   1 
ATOM   932  C C    . GLY A 1 117 ? -5.96245  33.40670 20.98146  1.000 47.77928  ? 117 GLY A C    1 
ATOM   933  O O    . GLY A 1 117 ? -6.95389  33.17825 20.27453  1.000 40.82564  ? 117 GLY A O    1 
ATOM   934  N N    . GLN A 1 118 ? -4.89413  34.07138 20.53231  1.000 44.27361  ? 118 GLN A N    1 
ATOM   935  C CA   . GLN A 1 118 ? -4.88436  34.57073 19.16957  1.000 49.79862  ? 118 GLN A CA   1 
ATOM   936  C C    . GLN A 1 118 ? -4.63852  33.46558 18.17226  1.000 43.13403  ? 118 GLN A C    1 
ATOM   937  O O    . GLN A 1 118 ? -3.92061  32.49723 18.44053  1.000 44.14252  ? 118 GLN A O    1 
ATOM   938  C CB   . GLN A 1 118 ? -3.83232  35.63237 18.95284  1.000 51.42741  ? 118 GLN A CB   1 
ATOM   939  C CG   . GLN A 1 118 ? -3.86102  36.73772 19.92328  1.000 58.80349  ? 118 GLN A CG   1 
ATOM   940  C CD   . GLN A 1 118 ? -3.66192  38.02083 19.18130  1.000 70.19581  ? 118 GLN A CD   1 
ATOM   941  O OE1  . GLN A 1 118 ? -4.63363  38.76038 18.93111  1.000 68.47948  ? 118 GLN A OE1  1 
ATOM   942  N NE2  . GLN A 1 118 ? -2.41697  38.26220 18.72943  1.000 75.97203  ? 118 GLN A NE2  1 
ATOM   943  N N    . VAL A 1 119 ? -5.21561  33.64834 16.99288  1.000 47.37458  ? 119 VAL A N    1 
ATOM   944  C CA   . VAL A 1 119 ? -5.13617  32.67519 15.92300  1.000 45.87114  ? 119 VAL A CA   1 
ATOM   945  C C    . VAL A 1 119 ? -4.52344  33.39284 14.72638  1.000 45.69626  ? 119 VAL A C    1 
ATOM   946  O O    . VAL A 1 119 ? -5.02853  34.44086 14.30059  1.000 47.69264  ? 119 VAL A O    1 
ATOM   947  C CB   . VAL A 1 119 ? -6.52216  32.10131 15.58598  1.000 44.79897  ? 119 VAL A CB   1 
ATOM   948  C CG1  . VAL A 1 119 ? -6.40788  31.19293 14.42241  1.000 48.44921  ? 119 VAL A CG1  1 
ATOM   949  C CG2  . VAL A 1 119 ? -7.05892  31.33571 16.74667  1.000 48.24338  ? 119 VAL A CG2  1 
ATOM   950  N N    . THR A 1 120 ? -3.43604  32.85100 14.19575  1.000 44.96961  ? 120 THR A N    1 
ATOM   951  C CA   . THR A 1 120 ? -2.79158  33.48197 13.05717  1.000 47.68424  ? 120 THR A CA   1 
ATOM   952  C C    . THR A 1 120 ? -2.89892  32.60718 11.81002  1.000 46.54995  ? 120 THR A C    1 
ATOM   953  O O    . THR A 1 120 ? -2.81783  31.37170 11.87453  1.000 43.71885  ? 120 THR A O    1 
ATOM   954  C CB   . THR A 1 120 ? -1.32168  33.75730 13.33085  1.000 48.84657  ? 120 THR A CB   1 
ATOM   955  O OG1  . THR A 1 120 ? -0.68944  32.52015 13.64923  1.000 50.75886  ? 120 THR A OG1  1 
ATOM   956  C CG2  . THR A 1 120 ? -1.18504  34.68410 14.54608  1.000 51.51068  ? 120 THR A CG2  1 
ATOM   957  N N    . ASN A 1 121 ? -3.02429  33.28230 10.66569  1.000 45.99507  ? 121 ASN A N    1 
ATOM   958  C CA   . ASN A 1 121 ? -2.93167  32.64143 9.35665   1.000 45.40626  ? 121 ASN A CA   1 
ATOM   959  C C    . ASN A 1 121 ? -1.53336  32.04995 9.23394   1.000 46.46696  ? 121 ASN A C    1 
ATOM   960  O O    . ASN A 1 121 ? -0.57792  32.78340 8.94872   1.000 48.64616  ? 121 ASN A O    1 
ATOM   961  C CB   . ASN A 1 121 ? -3.15323  33.66979 8.25390   1.000 43.80997  ? 121 ASN A CB   1 
ATOM   962  C CG   . ASN A 1 121 ? -3.27972  33.02923 6.89388   1.000 48.47909  ? 121 ASN A CG   1 
ATOM   963  O OD1  . ASN A 1 121 ? -2.79823  31.90585 6.70719   1.000 46.10137  ? 121 ASN A OD1  1 
ATOM   964  N ND2  . ASN A 1 121 ? -3.74332  33.80215 5.89742   1.000 46.52119  ? 121 ASN A ND2  1 
ATOM   965  N N    . TYR A 1 122 ? -1.37993  30.75449 9.48478   1.000 42.77076  ? 122 TYR A N    1 
ATOM   966  C CA   . TYR A 1 122 ? -0.05273  30.13155 9.52405   1.000 44.37300  ? 122 TYR A CA   1 
ATOM   967  C C    . TYR A 1 122 ? 0.45807   29.74225 8.12093   1.000 46.95218  ? 122 TYR A C    1 
ATOM   968  O O    . TYR A 1 122 ? 1.65998   29.87234 7.82730   1.000 48.12956  ? 122 TYR A O    1 
ATOM   969  C CB   . TYR A 1 122 ? -0.12634  28.88148 10.36540  1.000 41.66229  ? 122 TYR A CB   1 
ATOM   970  C CG   . TYR A 1 122 ? 1.18906   28.29682 10.77908  1.000 46.20767  ? 122 TYR A CG   1 
ATOM   971  C CD1  . TYR A 1 122 ? 1.99117   28.91895 11.72490  1.000 47.33907  ? 122 TYR A CD1  1 
ATOM   972  C CD2  . TYR A 1 122 ? 1.60265   27.09547 10.26829  1.000 45.91877  ? 122 TYR A CD2  1 
ATOM   973  C CE1  . TYR A 1 122 ? 3.18265   28.34842 12.12664  1.000 47.89299  ? 122 TYR A CE1  1 
ATOM   974  C CE2  . TYR A 1 122 ? 2.79573   26.52126 10.65109  1.000 47.55248  ? 122 TYR A CE2  1 
ATOM   975  C CZ   . TYR A 1 122 ? 3.57318   27.14116 11.57983  1.000 48.93921  ? 122 TYR A CZ   1 
ATOM   976  O OH   . TYR A 1 122 ? 4.75439   26.54866 11.96094  1.000 50.26759  ? 122 TYR A OH   1 
ATOM   977  N N    . GLY A 1 123 ? -0.41702  29.20693 7.28335   1.000 45.10858  ? 123 GLY A N    1 
ATOM   978  C CA   . GLY A 1 123 ? -0.06118  28.79167 5.91379   1.000 45.83865  ? 123 GLY A CA   1 
ATOM   979  C C    . GLY A 1 123 ? 0.36573   27.32099 5.85562   1.000 48.46353  ? 123 GLY A C    1 
ATOM   980  O O    . GLY A 1 123 ? -0.43684  26.42094 6.21594   1.000 45.54876  ? 123 GLY A O    1 
ATOM   981  N N    . PHE A 1 124 ? 1.60611   27.07187 5.39587   1.000 50.55537  ? 124 PHE A N    1 
ATOM   982  C CA   . PHE A 1 124 ? 2.12889   25.71026 5.24535   1.000 48.96067  ? 124 PHE A CA   1 
ATOM   983  C C    . PHE A 1 124 ? 2.43347   25.04738 6.59115   1.000 48.49831  ? 124 PHE A C    1 
ATOM   984  O O    . PHE A 1 124 ? 3.03713   25.65439 7.48703   1.000 49.65403  ? 124 PHE A O    1 
ATOM   985  C CB   . PHE A 1 124 ? 3.41724   25.71250 4.41294   1.000 49.60527  ? 124 PHE A CB   1 
ATOM   986  C CG   . PHE A 1 124 ? 4.11912   24.37892 4.38972   1.000 49.93328  ? 124 PHE A CG   1 
ATOM   987  C CD1  . PHE A 1 124 ? 3.76206   23.41137 3.47005   1.000 55.14510  ? 124 PHE A CD1  1 
ATOM   988  C CD2  . PHE A 1 124 ? 5.10598   24.08196 5.32336   1.000 54.56622  ? 124 PHE A CD2  1 
ATOM   989  C CE1  . PHE A 1 124 ? 4.39726   22.17008 3.45476   1.000 55.68589  ? 124 PHE A CE1  1 
ATOM   990  C CE2  . PHE A 1 124 ? 5.73709   22.84275 5.33288   1.000 55.30632  ? 124 PHE A CE2  1 
ATOM   991  C CZ   . PHE A 1 124 ? 5.38433   21.88340 4.39618   1.000 54.94200  ? 124 PHE A CZ   1 
ATOM   992  N N    . LEU A 1 125 ? 2.07481   23.76210 6.69432   1.000 45.98868  ? 125 LEU A N    1 
ATOM   993  C CA   . LEU A 1 125 ? 2.35085   22.92991 7.85617   1.000 52.58378  ? 125 LEU A CA   1 
ATOM   994  C C    . LEU A 1 125 ? 2.65377   21.51921 7.37718   1.000 52.40767  ? 125 LEU A C    1 
ATOM   995  O O    . LEU A 1 125 ? 1.90912   20.97101 6.56225   1.000 52.69028  ? 125 LEU A O    1 
ATOM   996  C CB   . LEU A 1 125 ? 1.16015   22.91513 8.83363   1.000 48.68403  ? 125 LEU A CB   1 
ATOM   997  C CG   . LEU A 1 125 ? 1.29517   21.97381 10.03055  1.000 50.63352  ? 125 LEU A CG   1 
ATOM   998  C CD1  . LEU A 1 125 ? 2.31376   22.50669 10.97801  1.000 52.91709  ? 125 LEU A CD1  1 
ATOM   999  C CD2  . LEU A 1 125 ? -0.04655  21.78488 10.75363  1.000 45.49836  ? 125 LEU A CD2  1 
ATOM   1000 N N    . ASN A 1 126 ? 3.77179   20.95820 7.83038   1.000 51.95476  ? 126 ASN A N    1 
ATOM   1001 C CA   . ASN A 1 126 ? 4.09208   19.54972 7.60947   1.000 52.83492  ? 126 ASN A CA   1 
ATOM   1002 C C    . ASN A 1 126 ? 3.34203   18.77255 8.68152   1.000 53.92433  ? 126 ASN A C    1 
ATOM   1003 O O    . ASN A 1 126 ? 3.80073   18.63351 9.82327   1.000 56.13611  ? 126 ASN A O    1 
ATOM   1004 C CB   . ASN A 1 126 ? 5.59969   19.32817 7.67644   1.000 57.37089  ? 126 ASN A CB   1 
ATOM   1005 C CG   . ASN A 1 126 ? 6.01955   17.88238 7.35699   1.000 61.97058  ? 126 ASN A CG   1 
ATOM   1006 O OD1  . ASN A 1 126 ? 5.18635   17.00546 7.10391   1.000 58.67730  ? 126 ASN A OD1  1 
ATOM   1007 N ND2  . ASN A 1 126 ? 7.33269   17.63556 7.38050   1.000 63.76639  ? 126 ASN A ND2  1 
ATOM   1008 N N    . LEU A 1 127 ? 2.15121   18.29770 8.33106   1.000 49.71612  ? 127 LEU A N    1 
ATOM   1009 C CA   . LEU A 1 127 ? 1.23931   17.72855 9.31506   1.000 53.97707  ? 127 LEU A CA   1 
ATOM   1010 C C    . LEU A 1 127 ? 1.48674   16.23556 9.40094   1.000 56.70244  ? 127 LEU A C    1 
ATOM   1011 O O    . LEU A 1 127 ? 1.06357   15.48430 8.51511   1.000 55.71770  ? 127 LEU A O    1 
ATOM   1012 C CB   . LEU A 1 127 ? -0.20771  18.00008 8.94578   1.000 50.90945  ? 127 LEU A CB   1 
ATOM   1013 C CG   . LEU A 1 127 ? -1.29282  17.68644 9.96123   1.000 51.17462  ? 127 LEU A CG   1 
ATOM   1014 C CD1  . LEU A 1 127 ? -0.88285  18.05133 11.42113  1.000 49.91686  ? 127 LEU A CD1  1 
ATOM   1015 C CD2  . LEU A 1 127 ? -2.58555  18.37886 9.52786   1.000 49.95857  ? 127 LEU A CD2  1 
ATOM   1016 N N    . GLY A 1 128 ? 2.13550   15.80162 10.48719  1.000 56.33645  ? 128 GLY A N    1 
ATOM   1017 C CA   . GLY A 1 128 ? 2.52059   14.40992 10.61148  1.000 56.53267  ? 128 GLY A CA   1 
ATOM   1018 C C    . GLY A 1 128 ? 3.05392   13.85802 9.29972   1.000 56.80514  ? 128 GLY A C    1 
ATOM   1019 O O    . GLY A 1 128 ? 2.65471   12.76960 8.86660   1.000 57.00849  ? 128 GLY A O    1 
ATOM   1020 N N    . GLY A 1 129 ? 3.93770   14.61019 8.64230   1.000 56.97862  ? 129 GLY A N    1 
ATOM   1021 C CA   . GLY A 1 129 ? 4.55780   14.17237 7.39609   1.000 55.53370  ? 129 GLY A CA   1 
ATOM   1022 C C    . GLY A 1 129 ? 3.76922   14.40166 6.11454   1.000 57.63425  ? 129 GLY A C    1 
ATOM   1023 O O    . GLY A 1 129 ? 4.22496   13.97197 5.04307   1.000 57.44100  ? 129 GLY A O    1 
ATOM   1024 N N    . THR A 1 130 ? 2.60172   15.04937 6.17303   1.000 56.06415  ? 130 THR A N    1 
ATOM   1025 C CA   . THR A 1 130 ? 1.85389   15.37822 4.96041   1.000 53.21932  ? 130 THR A CA   1 
ATOM   1026 C C    . THR A 1 130 ? 1.86134   16.88237 4.77241   1.000 52.11497  ? 130 THR A C    1 
ATOM   1027 O O    . THR A 1 130 ? 1.35830   17.60133 5.64720   1.000 52.24043  ? 130 THR A O    1 
ATOM   1028 C CB   . THR A 1 130 ? 0.41614   14.89050 5.04963   1.000 52.96655  ? 130 THR A CB   1 
ATOM   1029 O OG1  . THR A 1 130 ? 0.39607   13.46547 5.02680   1.000 56.34437  ? 130 THR A OG1  1 
ATOM   1030 C CG2  . THR A 1 130 ? -0.40182  15.43375 3.87296   1.000 50.62374  ? 130 THR A CG2  1 
ATOM   1031 N N    . PRO A 1 131 ? 2.39625   17.41705 3.68707   1.000 51.03909  ? 131 PRO A N    1 
ATOM   1032 C CA   . PRO A 1 131 ? 2.27170   18.86323 3.45669   1.000 48.84904  ? 131 PRO A CA   1 
ATOM   1033 C C    . PRO A 1 131 ? 0.80529   19.26554 3.44053   1.000 47.43986  ? 131 PRO A C    1 
ATOM   1034 O O    . PRO A 1 131 ? -0.03965  18.57564 2.86614   1.000 47.26189  ? 131 PRO A O    1 
ATOM   1035 C CB   . PRO A 1 131 ? 2.91089   19.06914 2.07215   1.000 48.29847  ? 131 PRO A CB   1 
ATOM   1036 C CG   . PRO A 1 131 ? 3.76906   17.87171 1.84174   1.000 52.29903  ? 131 PRO A CG   1 
ATOM   1037 C CD   . PRO A 1 131 ? 3.32901   16.75887 2.74484   1.000 52.94867  ? 131 PRO A CD   1 
ATOM   1038 N N    . THR A 1 132 ? 0.50780   20.41048 4.04517   1.000 45.33921  ? 132 THR A N    1 
ATOM   1039 C CA   . THR A 1 132 ? -0.87307  20.84459 4.20617   1.000 44.00879  ? 132 THR A CA   1 
ATOM   1040 C C    . THR A 1 132 ? -0.88182  22.35554 4.07403   1.000 42.33633  ? 132 THR A C    1 
ATOM   1041 O O    . THR A 1 132 ? 0.08315   23.01717 4.45872   1.000 44.83082  ? 132 THR A O    1 
ATOM   1042 C CB   . THR A 1 132 ? -1.42764  20.36193 5.58939   1.000 44.65783  ? 132 THR A CB   1 
ATOM   1043 O OG1  . THR A 1 132 ? -1.28310  18.94409 5.66085   1.000 43.80024  ? 132 THR A OG1  1 
ATOM   1044 C CG2  . THR A 1 132 ? -2.89960  20.69069 5.76208   1.000 40.79181  ? 132 THR A CG2  1 
ATOM   1045 N N    . HIS A 1 133 ? -1.95967  22.90576 3.53203   1.000 38.50848  ? 133 HIS A N    1 
ATOM   1046 C CA   . HIS A 1 133 ? -2.05239  24.34322 3.36382   1.000 42.24176  ? 133 HIS A CA   1 
ATOM   1047 C C    . HIS A 1 133 ? -3.23824  24.91108 4.12106   1.000 43.07402  ? 133 HIS A C    1 
ATOM   1048 O O    . HIS A 1 133 ? -4.13711  24.19354 4.55841   1.000 44.02706  ? 133 HIS A O    1 
ATOM   1049 C CB   . HIS A 1 133 ? -2.20364  24.71890 1.86240   1.000 45.51838  ? 133 HIS A CB   1 
ATOM   1050 C CG   . HIS A 1 133 ? -0.94266  24.57223 1.07892   1.000 45.59077  ? 133 HIS A CG   1 
ATOM   1051 N ND1  . HIS A 1 133 ? -0.92408  24.57599 -0.30438  1.000 47.44887  ? 133 HIS A ND1  1 
ATOM   1052 C CD2  . HIS A 1 133 ? 0.34263   24.40511 1.47725   1.000 46.84657  ? 133 HIS A CD2  1 
ATOM   1053 C CE1  . HIS A 1 133 ? 0.31958   24.41201 -0.72258  1.000 47.46337  ? 133 HIS A CE1  1 
ATOM   1054 N NE2  . HIS A 1 133 ? 1.10888   24.31451 0.33299   1.000 48.61589  ? 133 HIS A NE2  1 
ATOM   1055 N N    . ARG A 1 134 ? -3.26248  26.24300 4.17696   1.000 41.03090  ? 134 ARG A N    1 
ATOM   1056 C CA   . ARG A 1 134 ? -4.38026  26.98723 4.72505   1.000 42.86154  ? 134 ARG A CA   1 
ATOM   1057 C C    . ARG A 1 134 ? -4.57275  26.71262 6.21689   1.000 43.24795  ? 134 ARG A C    1 
ATOM   1058 O O    . ARG A 1 134 ? -5.69568  26.52766 6.68225   1.000 39.52887  ? 134 ARG A O    1 
ATOM   1059 C CB   . ARG A 1 134 ? -5.66084  26.69253 3.97433   1.000 42.60643  ? 134 ARG A CB   1 
ATOM   1060 C CG   . ARG A 1 134 ? -5.96389  27.75856 2.97852   1.000 50.78577  ? 134 ARG A CG   1 
ATOM   1061 C CD   . ARG A 1 134 ? -7.05493  27.34274 2.12022   1.000 47.54469  ? 134 ARG A CD   1 
ATOM   1062 N NE   . ARG A 1 134 ? -6.66800  27.32063 0.71972   1.000 45.52728  ? 134 ARG A NE   1 
ATOM   1063 C CZ   . ARG A 1 134 ? -7.49325  26.95124 -0.23837  1.000 44.15521  ? 134 ARG A CZ   1 
ATOM   1064 N NH1  . ARG A 1 134 ? -8.74372  26.59890 0.03633   1.000 44.76631  ? 134 ARG A NH1  1 
ATOM   1065 N NH2  . ARG A 1 134 ? -7.06337  26.94002 -1.50201  1.000 49.54189  ? 134 ARG A NH2  1 
ATOM   1066 N N    . ILE A 1 135 ? -3.48694  26.68567 6.95290   1.000 42.64254  ? 135 ILE A N    1 
ATOM   1067 C CA   . ILE A 1 135 ? -3.51662  26.27958 8.34922   1.000 42.46963  ? 135 ILE A CA   1 
ATOM   1068 C C    . ILE A 1 135 ? -3.56916  27.51028 9.24444   1.000 43.87275  ? 135 ILE A C    1 
ATOM   1069 O O    . ILE A 1 135 ? -2.94031  28.54652 8.95369   1.000 42.03504  ? 135 ILE A O    1 
ATOM   1070 C CB   . ILE A 1 135 ? -2.30896  25.40167 8.70197   1.000 42.66244  ? 135 ILE A CB   1 
ATOM   1071 C CG1  . ILE A 1 135 ? -2.44354  24.03222 8.05441   1.000 43.08219  ? 135 ILE A CG1  1 
ATOM   1072 C CG2  . ILE A 1 135 ? -2.21416  25.25998 10.22210  1.000 42.17206  ? 135 ILE A CG2  1 
ATOM   1073 C CD1  . ILE A 1 135 ? -3.52029  23.18033 8.64462   1.000 44.91916  ? 135 ILE A CD1  1 
ATOM   1074 N N    . LEU A 1 136 ? -4.35628  27.40986 10.31990  1.000 41.78025  ? 136 LEU A N    1 
ATOM   1075 C CA   . LEU A 1 136 ? -4.41762  28.42253 11.37061  1.000 43.85660  ? 136 LEU A CA   1 
ATOM   1076 C C    . LEU A 1 136 ? -3.66498  27.89911 12.58418  1.000 42.79503  ? 136 LEU A C    1 
ATOM   1077 O O    . LEU A 1 136 ? -3.68203  26.68846 12.85271  1.000 41.63100  ? 136 LEU A O    1 
ATOM   1078 C CB   . LEU A 1 136 ? -5.86440  28.73183 11.78275  1.000 45.23282  ? 136 LEU A CB   1 
ATOM   1079 C CG   . LEU A 1 136 ? -6.69641  29.44453 10.73339  1.000 40.03021  ? 136 LEU A CG   1 
ATOM   1080 C CD1  . LEU A 1 136 ? -8.17344  29.23218 11.00789  1.000 40.36260  ? 136 LEU A CD1  1 
ATOM   1081 C CD2  . LEU A 1 136 ? -6.37658  30.90783 10.68837  1.000 43.40907  ? 136 LEU A CD2  1 
ATOM   1082 N N    . MET A 1 137 ? -2.98458  28.81201 13.29753  1.000 40.92889  ? 137 MET A N    1 
ATOM   1083 C CA   . MET A 1 137 ? -2.11974  28.48143 14.42893  1.000 45.47673  ? 137 MET A CA   1 
ATOM   1084 C C    . MET A 1 137 ? -2.50956  29.25573 15.68614  1.000 43.30453  ? 137 MET A C    1 
ATOM   1085 O O    . MET A 1 137 ? -2.82255  30.45659 15.64043  1.000 43.80145  ? 137 MET A O    1 
ATOM   1086 C CB   . MET A 1 137 ? -0.64039  28.71778 14.02702  1.000 46.31533  ? 137 MET A CB   1 
ATOM   1087 C CG   . MET A 1 137 ? 0.51343   28.42398 14.99381  1.000 47.33085  ? 137 MET A CG   1 
ATOM   1088 S SD   . MET A 1 137 ? 0.53013   29.43720 16.50356  1.000 49.84684  ? 137 MET A SD   1 
ATOM   1089 C CE   . MET A 1 137 ? 1.53994   30.81184 15.90396  1.000 51.95673  ? 137 MET A CE   1 
ATOM   1090 N N    . TYR A 1 138 ? -2.53664  28.53183 16.80092  1.000 45.99894  ? 138 TYR A N    1 
ATOM   1091 C CA   . TYR A 1 138 ? -2.66711  29.12198 18.12489  1.000 43.85042  ? 138 TYR A CA   1 
ATOM   1092 C C    . TYR A 1 138 ? -1.58301  28.56374 19.02319  1.000 46.58886  ? 138 TYR A C    1 
ATOM   1093 O O    . TYR A 1 138 ? -1.11704  27.42459 18.86050  1.000 44.43362  ? 138 TYR A O    1 
ATOM   1094 C CB   . TYR A 1 138 ? -4.12128  28.93948 18.71845  1.000 46.20254  ? 138 TYR A CB   1 
ATOM   1095 C CG   . TYR A 1 138 ? -4.89231  27.72092 18.22141  1.000 44.49492  ? 138 TYR A CG   1 
ATOM   1096 C CD1  . TYR A 1 138 ? -4.81430  26.46477 18.83150  1.000 41.24383  ? 138 TYR A CD1  1 
ATOM   1097 C CD2  . TYR A 1 138 ? -5.56020  27.81438 16.97691  1.000 44.55892  ? 138 TYR A CD2  1 
ATOM   1098 C CE1  . TYR A 1 138 ? -5.53222  25.33921 18.26699  1.000 43.66473  ? 138 TYR A CE1  1 
ATOM   1099 C CE2  . TYR A 1 138 ? -6.22888  26.71900 16.39702  1.000 43.70835  ? 138 TYR A CE2  1 
ATOM   1100 C CZ   . TYR A 1 138 ? -6.21445  25.48860 17.02954  1.000 45.05549  ? 138 TYR A CZ   1 
ATOM   1101 O OH   . TYR A 1 138 ? -6.92354  24.44610 16.41537  1.000 42.76054  ? 138 TYR A OH   1 
ATOM   1102 N N    . ASN A 1 139 ? -1.15381  29.41256 19.95428  1.000 48.52247  ? 139 ASN A N    1 
ATOM   1103 C CA   . ASN A 1 139 ? -0.17023  29.02130 20.95551  1.000 48.53702  ? 139 ASN A CA   1 
ATOM   1104 C C    . ASN A 1 139 ? -0.89289  28.44588 22.16150  1.000 51.40680  ? 139 ASN A C    1 
ATOM   1105 O O    . ASN A 1 139 ? -1.10535  29.09732 23.18300  1.000 51.69228  ? 139 ASN A O    1 
ATOM   1106 C CB   . ASN A 1 139 ? 0.72113   30.20649 21.30268  1.000 51.55696  ? 139 ASN A CB   1 
ATOM   1107 C CG   . ASN A 1 139 ? 1.64027   30.55577 20.16354  1.000 53.93286  ? 139 ASN A CG   1 
ATOM   1108 O OD1  . ASN A 1 139 ? 2.53263   29.76244 19.86137  1.000 57.15639  ? 139 ASN A OD1  1 
ATOM   1109 N ND2  . ASN A 1 139 ? 1.41585   31.69724 19.48913  1.000 52.80737  ? 139 ASN A ND2  1 
ATOM   1110 N N    . PHE A 1 140 ? -1.29030  27.18321 22.02129  1.000 51.00824  ? 140 PHE A N    1 
ATOM   1111 C CA   . PHE A 1 140 ? -1.93781  26.54099 23.11001  1.000 44.63753  ? 140 PHE A CA   1 
ATOM   1112 C C    . PHE A 1 140 ? -1.51576  25.08825 23.01343  1.000 45.65556  ? 140 PHE A C    1 
ATOM   1113 O O    . PHE A 1 140 ? -1.40350  24.56123 21.89457  1.000 47.22833  ? 140 PHE A O    1 
ATOM   1114 C CB   . PHE A 1 140 ? -3.46187  26.65316 23.08277  1.000 44.16123  ? 140 PHE A CB   1 
ATOM   1115 C CG   . PHE A 1 140 ? -4.09644  26.20460 24.37100  1.000 48.51647  ? 140 PHE A CG   1 
ATOM   1116 C CD1  . PHE A 1 140 ? -4.29408  27.12770 25.40061  1.000 47.93261  ? 140 PHE A CD1  1 
ATOM   1117 C CD2  . PHE A 1 140 ? -4.46987  24.87957 24.57723  1.000 45.70458  ? 140 PHE A CD2  1 
ATOM   1118 C CE1  . PHE A 1 140 ? -4.84896  26.72962 26.63543  1.000 51.34661  ? 140 PHE A CE1  1 
ATOM   1119 C CE2  . PHE A 1 140 ? -5.02872  24.47279 25.82095  1.000 47.83141  ? 140 PHE A CE2  1 
ATOM   1120 C CZ   . PHE A 1 140 ? -5.22347  25.39403 26.82958  1.000 47.52665  ? 140 PHE A CZ   1 
ATOM   1121 N N    . PRO A 1 141 ? -1.21396  24.44569 24.13727  1.000 45.59964  ? 141 PRO A N    1 
ATOM   1122 C CA   . PRO A 1 141 ? -0.86471  23.01272 24.12939  1.000 43.76208  ? 141 PRO A CA   1 
ATOM   1123 C C    . PRO A 1 141 ? -2.06983  22.09743 23.94749  1.000 45.65215  ? 141 PRO A C    1 
ATOM   1124 O O    . PRO A 1 141 ? -2.53096  21.45347 24.88827  1.000 46.44822  ? 141 PRO A O    1 
ATOM   1125 C CB   . PRO A 1 141 ? -0.19377  22.82231 25.50108  1.000 47.16450  ? 141 PRO A CB   1 
ATOM   1126 C CG   . PRO A 1 141 ? -0.74592  23.91230 26.30612  1.000 44.00527  ? 141 PRO A CG   1 
ATOM   1127 C CD   . PRO A 1 141 ? -0.94890  25.07518 25.44728  1.000 45.19546  ? 141 PRO A CD   1 
ATOM   1128 N N    . THR A 1 142 ? -2.60743  22.03791 22.72730  1.000 42.22424  ? 142 THR A N    1 
ATOM   1129 C CA   . THR A 1 142 ? -3.71675  21.14448 22.43746  1.000 39.30554  ? 142 THR A CA   1 
ATOM   1130 C C    . THR A 1 142 ? -3.23709  19.70601 22.41587  1.000 39.01062  ? 142 THR A C    1 
ATOM   1131 O O    . THR A 1 142 ? -2.03532  19.42398 22.32248  1.000 42.34463  ? 142 THR A O    1 
ATOM   1132 C CB   . THR A 1 142 ? -4.36948  21.55251 21.10114  1.000 42.69915  ? 142 THR A CB   1 
ATOM   1133 O OG1  . THR A 1 142 ? -3.40736  21.30756 20.08860  1.000 41.12337  ? 142 THR A OG1  1 
ATOM   1134 C CG2  . THR A 1 142 ? -4.85652  23.00865 21.04090  1.000 39.25611  ? 142 THR A CG2  1 
ATOM   1135 N N    . ARG A 1 143 ? -4.18759  18.77480 22.47704  1.000 39.21806  ? 143 ARG A N    1 
ATOM   1136 C CA   . ARG A 1 143 ? -3.79159  17.38876 22.65909  1.000 43.89021  ? 143 ARG A CA   1 
ATOM   1137 C C    . ARG A 1 143 ? -4.59639  16.42974 21.78512  1.000 42.30200  ? 143 ARG A C    1 
ATOM   1138 O O    . ARG A 1 143 ? -5.72802  16.70238 21.37193  1.000 43.92587  ? 143 ARG A O    1 
ATOM   1139 C CB   . ARG A 1 143 ? -3.96738  16.93355 24.13411  1.000 41.69431  ? 143 ARG A CB   1 
ATOM   1140 C CG   . ARG A 1 143 ? -3.55456  17.95920 25.24540  1.000 44.80353  ? 143 ARG A CG   1 
ATOM   1141 C CD   . ARG A 1 143 ? -2.11129  17.78664 25.77829  1.000 50.76399  ? 143 ARG A CD   1 
ATOM   1142 N NE   . ARG A 1 143 ? -1.57269  18.92668 26.54249  1.000 46.18773  ? 143 ARG A NE   1 
ATOM   1143 C CZ   . ARG A 1 143 ? -0.28852  19.29805 26.60450  1.000 49.57873  ? 143 ARG A CZ   1 
ATOM   1144 N NH1  . ARG A 1 143 ? 0.59245   18.97400 25.65304  1.000 51.01890  ? 143 ARG A NH1  1 
ATOM   1145 N NH2  . ARG A 1 143 ? 0.13195   20.02551 27.64228  1.000 48.63242  ? 143 ARG A NH2  1 
ATOM   1146 N N    . ALA A 1 144 ? -4.01243  15.25123 21.57308  1.000 44.77912  ? 144 ALA A N    1 
ATOM   1147 C CA   . ALA A 1 144 ? -4.75980  14.08601 21.12812  1.000 46.92176  ? 144 ALA A CA   1 
ATOM   1148 C C    . ALA A 1 144 ? -6.12760  14.03427 21.78585  1.000 48.61271  ? 144 ALA A C    1 
ATOM   1149 O O    . ALA A 1 144 ? -6.25540  14.17035 23.02229  1.000 49.70179  ? 144 ALA A O    1 
ATOM   1150 C CB   . ALA A 1 144 ? -3.97548  12.81357 21.45603  1.000 50.26127  ? 144 ALA A CB   1 
ATOM   1151 N N    . GLY A 1 145 ? -7.14773  13.80222 20.96546  1.000 45.51267  ? 145 GLY A N    1 
ATOM   1152 C CA   . GLY A 1 145 ? -8.52134  13.77480 21.43181  1.000 41.19589  ? 145 GLY A CA   1 
ATOM   1153 C C    . GLY A 1 145 ? -9.30899  15.00553 21.04527  1.000 42.76224  ? 145 GLY A C    1 
ATOM   1154 O O    . GLY A 1 145 ? -10.54296 14.98842 21.12078  1.000 44.98801  ? 145 GLY A O    1 
ATOM   1155 N N    . GLN A 1 146 ? -8.63598  16.07508 20.63624  1.000 40.57456  ? 146 GLN A N    1 
ATOM   1156 C CA   . GLN A 1 146 ? -9.30919  17.31097 20.25484  1.000 38.56887  ? 146 GLN A CA   1 
ATOM   1157 C C    . GLN A 1 146 ? -9.42893  17.51053 18.72872  1.000 38.59374  ? 146 GLN A C    1 
ATOM   1158 O O    . GLN A 1 146 ? -10.01699 18.51078 18.29702  1.000 37.08725  ? 146 GLN A O    1 
ATOM   1159 C CB   . GLN A 1 146 ? -8.59445  18.47848 20.90931  1.000 36.35355  ? 146 GLN A CB   1 
ATOM   1160 C CG   . GLN A 1 146 ? -8.51255  18.25390 22.48272  1.000 40.62365  ? 146 GLN A CG   1 
ATOM   1161 C CD   . GLN A 1 146 ? -7.57420  19.19347 23.20127  1.000 42.13900  ? 146 GLN A CD   1 
ATOM   1162 O OE1  . GLN A 1 146 ? -6.81607  19.93142 22.58766  1.000 41.62989  ? 146 GLN A OE1  1 
ATOM   1163 N NE2  . GLN A 1 146 ? -7.58180  19.12487 24.53808  1.000 39.73967  ? 146 GLN A NE2  1 
ATOM   1164 N N    . CYS A 1 147 ? -8.95777  16.58106 17.90996  1.000 37.86196  ? 147 CYS A N    1 
ATOM   1165 C CA   . CYS A 1 147 ? -9.16465  16.77598 16.45879  1.000 39.41553  ? 147 CYS A CA   1 
ATOM   1166 C C    . CYS A 1 147 ? -10.64175 16.75977 16.06889  1.000 41.29463  ? 147 CYS A C    1 
ATOM   1167 O O    . CYS A 1 147 ? -11.46069 15.99535 16.60302  1.000 40.78996  ? 147 CYS A O    1 
ATOM   1168 C CB   . CYS A 1 147 ? -8.39128  15.78579 15.60403  1.000 39.90201  ? 147 CYS A CB   1 
ATOM   1169 S SG   . CYS A 1 147 ? -6.62501  16.06369 15.58331  1.000 45.52313  ? 147 CYS A SG   1 
ATOM   1170 N N    . GLY A 1 148 ? -10.97694 17.64804 15.13789  1.000 40.36641  ? 148 GLY A N    1 
ATOM   1171 C CA   . GLY A 1 148 ? -12.34809 17.94774 14.80431  1.000 40.96619  ? 148 GLY A CA   1 
ATOM   1172 C C    . GLY A 1 148 ? -12.92738 19.07784 15.60258  1.000 38.55440  ? 148 GLY A C    1 
ATOM   1173 O O    . GLY A 1 148 ? -13.98387 19.60377 15.23107  1.000 36.49015  ? 148 GLY A O    1 
ATOM   1174 N N    . GLY A 1 149 ? -12.29701 19.42653 16.73095  1.000 44.39930  ? 149 GLY A N    1 
ATOM   1175 C CA   . GLY A 1 149 ? -12.77261 20.48647 17.59532  1.000 36.56008  ? 149 GLY A CA   1 
ATOM   1176 C C    . GLY A 1 149 ? -13.00556 21.79449 16.87150  1.000 37.76443  ? 149 GLY A C    1 
ATOM   1177 O O    . GLY A 1 149 ? -12.22257 22.17772 15.99970  1.000 42.72821  ? 149 GLY A O    1 
ATOM   1178 N N    . VAL A 1 150 ? -14.11453 22.45761 17.17615  1.000 38.08340  ? 150 VAL A N    1 
ATOM   1179 C CA   . VAL A 1 150 ? -14.53042 23.63946 16.42611  1.000 37.08256  ? 150 VAL A CA   1 
ATOM   1180 C C    . VAL A 1 150 ? -13.77607 24.84219 16.96074  1.000 42.47312  ? 150 VAL A C    1 
ATOM   1181 O O    . VAL A 1 150 ? -13.70787 25.03766 18.18205  1.000 37.58640  ? 150 VAL A O    1 
ATOM   1182 C CB   . VAL A 1 150 ? -16.04358 23.86333 16.57250  1.000 37.60421  ? 150 VAL A CB   1 
ATOM   1183 C CG1  . VAL A 1 150 ? -16.48634 24.92643 15.56253  1.000 39.74756  ? 150 VAL A CG1  1 
ATOM   1184 C CG2  . VAL A 1 150 ? -16.78064 22.53844 16.36558  1.000 34.42934  ? 150 VAL A CG2  1 
ATOM   1185 N N    . VAL A 1 151 ? -13.24494 25.67520 16.06892  1.000 37.22053  ? 151 VAL A N    1 
ATOM   1186 C CA   . VAL A 1 151 ? -12.57404 26.90736 16.48581  1.000 38.92804  ? 151 VAL A CA   1 
ATOM   1187 C C    . VAL A 1 151 ? -13.45853 28.07932 16.08105  1.000 40.77396  ? 151 VAL A C    1 
ATOM   1188 O O    . VAL A 1 151 ? -13.77098 28.25866 14.88764  1.000 40.31608  ? 151 VAL A O    1 
ATOM   1189 C CB   . VAL A 1 151 ? -11.17357 27.02674 15.87132  1.000 40.44892  ? 151 VAL A CB   1 
ATOM   1190 C CG1  . VAL A 1 151 ? -10.44627 28.26708 16.41339  1.000 36.08331  ? 151 VAL A CG1  1 
ATOM   1191 C CG2  . VAL A 1 151 ? -10.39771 25.76150 16.13322  1.000 36.70941  ? 151 VAL A CG2  1 
ATOM   1192 N N    . THR A 1 152 ? -13.84478 28.88839 17.06276  1.000 36.50977  ? 152 THR A N    1 
ATOM   1193 C CA   . THR A 1 152 ? -14.72906 30.03568 16.86142  1.000 40.36404  ? 152 THR A CA   1 
ATOM   1194 C C    . THR A 1 152 ? -14.14737 31.30087 17.49152  1.000 43.01079  ? 152 THR A C    1 
ATOM   1195 O O    . THR A 1 152 ? -13.25415 31.26107 18.34927  1.000 41.61692  ? 152 THR A O    1 
ATOM   1196 C CB   . THR A 1 152 ? -16.12969 29.82095 17.43579  1.000 39.15395  ? 152 THR A CB   1 
ATOM   1197 O OG1  . THR A 1 152 ? -16.04801 29.60401 18.88452  1.000 40.48298  ? 152 THR A OG1  1 
ATOM   1198 C CG2  . THR A 1 152 ? -16.78464 28.64818 16.82001  1.000 36.37791  ? 152 THR A CG2  1 
ATOM   1199 N N    . THR A 1 153 ? -14.63769 32.42737 16.98695  1.000 40.54225  ? 153 THR A N    1 
ATOM   1200 C CA   . THR A 1 153 ? -14.75133 33.70959 17.66347  1.000 46.22398  ? 153 THR A CA   1 
ATOM   1201 C C    . THR A 1 153 ? -16.22723 34.06441 17.59955  1.000 50.40201  ? 153 THR A C    1 
ATOM   1202 O O    . THR A 1 153 ? -16.99331 33.43198 16.85718  1.000 51.16531  ? 153 THR A O    1 
ATOM   1203 C CB   . THR A 1 153 ? -13.92710 34.80187 16.98411  1.000 46.81019  ? 153 THR A CB   1 
ATOM   1204 O OG1  . THR A 1 153 ? -14.46710 34.99096 15.66087  1.000 47.01253  ? 153 THR A OG1  1 
ATOM   1205 C CG2  . THR A 1 153 ? -12.43621 34.42580 16.93850  1.000 43.93508  ? 153 THR A CG2  1 
ATOM   1206 N N    . THR A 1 154 ? -16.65726 35.08365 18.33814  1.000 50.21562  ? 154 THR A N    1 
ATOM   1207 C CA   . THR A 1 154 ? -18.06250 35.45798 18.19488  1.000 51.47866  ? 154 THR A CA   1 
ATOM   1208 C C    . THR A 1 154 ? -18.39726 35.75003 16.73357  1.000 48.75595  ? 154 THR A C    1 
ATOM   1209 O O    . THR A 1 154 ? -17.67326 36.46986 16.03618  1.000 52.58177  ? 154 THR A O    1 
ATOM   1210 C CB   . THR A 1 154 ? -18.44600 36.65373 19.06448  1.000 53.22481  ? 154 THR A CB   1 
ATOM   1211 O OG1  . THR A 1 154 ? -17.83170 36.54022 20.36035  1.000 56.81814  ? 154 THR A OG1  1 
ATOM   1212 C CG2  . THR A 1 154 ? -19.98090 36.68043 19.22446  1.000 54.10179  ? 154 THR A CG2  1 
ATOM   1213 N N    . GLY A 1 155 ? -19.51465 35.18031 16.28433  1.000 48.71761  ? 155 GLY A N    1 
ATOM   1214 C CA   . GLY A 1 155 ? -19.99825 35.35711 14.93879  1.000 51.33950  ? 155 GLY A CA   1 
ATOM   1215 C C    . GLY A 1 155 ? -19.29610 34.55636 13.88122  1.000 47.22078  ? 155 GLY A C    1 
ATOM   1216 O O    . GLY A 1 155 ? -19.75487 34.56707 12.73480  1.000 53.83681  ? 155 GLY A O    1 
ATOM   1217 N N    . LYS A 1 156 ? -18.18316 33.87783 14.18293  1.000 42.20986  ? 156 LYS A N    1 
ATOM   1218 C CA   . LYS A 1 156 ? -17.48621 33.21309 13.09137  1.000 47.86277  ? 156 LYS A CA   1 
ATOM   1219 C C    . LYS A 1 156 ? -17.01425 31.82975 13.50315  1.000 45.96020  ? 156 LYS A C    1 
ATOM   1220 O O    . LYS A 1 156 ? -16.43279 31.65624 14.57688  1.000 43.51833  ? 156 LYS A O    1 
ATOM   1221 C CB   . LYS A 1 156 ? -16.29909 34.06109 12.61324  1.000 47.58767  ? 156 LYS A CB   1 
ATOM   1222 C CG   . LYS A 1 156 ? -16.68956 35.38872 11.95708  1.000 46.45741  ? 156 LYS A CG   1 
ATOM   1223 C CD   . LYS A 1 156 ? -16.62064 35.34996 10.42255  1.000 51.57965  ? 156 LYS A CD   1 
ATOM   1224 C CE   . LYS A 1 156 ? -16.82354 36.74625 9.84639   1.000 56.75921  ? 156 LYS A CE   1 
ATOM   1225 N NZ   . LYS A 1 156 ? -18.27504 37.13210 9.79898   1.000 62.61089  ? 156 LYS A NZ   1 
ATOM   1226 N N    . VAL A 1 157 ? -17.27491 30.85438 12.63956  1.000 43.89164  ? 157 VAL A N    1 
ATOM   1227 C CA   . VAL A 1 157 ? -16.70828 29.51596 12.73224  1.000 41.93137  ? 157 VAL A CA   1 
ATOM   1228 C C    . VAL A 1 157 ? -15.54529 29.44531 11.75247  1.000 44.62182  ? 157 VAL A C    1 
ATOM   1229 O O    . VAL A 1 157 ? -15.76187 29.43804 10.53494  1.000 41.54956  ? 157 VAL A O    1 
ATOM   1230 C CB   . VAL A 1 157 ? -17.74851 28.45168 12.38235  1.000 41.44388  ? 157 VAL A CB   1 
ATOM   1231 C CG1  . VAL A 1 157 ? -17.09378 27.06963 12.50112  1.000 41.44978  ? 157 VAL A CG1  1 
ATOM   1232 C CG2  . VAL A 1 157 ? -18.99162 28.60516 13.24598  1.000 43.70436  ? 157 VAL A CG2  1 
ATOM   1233 N N    . ILE A 1 158 ? -14.31583 29.32942 12.24842  1.000 42.95442  ? 158 ILE A N    1 
ATOM   1234 C CA   . ILE A 1 158 ? -13.14781 29.59215 11.41628  1.000 40.05626  ? 158 ILE A CA   1 
ATOM   1235 C C    . ILE A 1 158 ? -12.31895 28.35586 11.09948  1.000 40.81754  ? 158 ILE A C    1 
ATOM   1236 O O    . ILE A 1 158 ? -11.49649 28.41237 10.17057  1.000 44.24253  ? 158 ILE A O    1 
ATOM   1237 C CB   . ILE A 1 158 ? -12.24584 30.67847 12.04662  1.000 44.86098  ? 158 ILE A CB   1 
ATOM   1238 C CG1  . ILE A 1 158 ? -11.58303 30.16816 13.33230  1.000 41.57342  ? 158 ILE A CG1  1 
ATOM   1239 C CG2  . ILE A 1 158 ? -13.04301 31.95555 12.33258  1.000 44.78901  ? 158 ILE A CG2  1 
ATOM   1240 C CD1  . ILE A 1 158 ? -10.61773 31.18437 13.94101  1.000 40.94478  ? 158 ILE A CD1  1 
ATOM   1241 N N    . GLY A 1 159 ? -12.48910 27.25148 11.81148  1.000 40.38142  ? 159 GLY A N    1 
ATOM   1242 C CA   . GLY A 1 159 ? -11.62707 26.10993 11.53714  1.000 37.18559  ? 159 GLY A CA   1 
ATOM   1243 C C    . GLY A 1 159 ? -12.01305 24.91056 12.36157  1.000 40.25247  ? 159 GLY A C    1 
ATOM   1244 O O    . GLY A 1 159 ? -12.81076 25.00170 13.31100  1.000 39.79615  ? 159 GLY A O    1 
ATOM   1245 N N    . ILE A 1 160 ? -11.39090 23.77867 12.01742  1.000 37.61100  ? 160 ILE A N    1 
ATOM   1246 C CA   . ILE A 1 160 ? -11.46582 22.58537 12.85667  1.000 37.85336  ? 160 ILE A CA   1 
ATOM   1247 C C    . ILE A 1 160 ? -10.05190 22.14550 13.19211  1.000 38.52984  ? 160 ILE A C    1 
ATOM   1248 O O    . ILE A 1 160 ? -9.12803  22.30388 12.38761  1.000 37.02026  ? 160 ILE A O    1 
ATOM   1249 C CB   . ILE A 1 160 ? -12.28614 21.45118 12.20010  1.000 36.08799  ? 160 ILE A CB   1 
ATOM   1250 C CG1  . ILE A 1 160 ? -11.66551 21.00035 10.86267  1.000 42.93903  ? 160 ILE A CG1  1 
ATOM   1251 C CG2  . ILE A 1 160 ? -13.74341 21.93718 11.94798  1.000 33.35618  ? 160 ILE A CG2  1 
ATOM   1252 C CD1  . ILE A 1 160 ? -12.30459 19.69619 10.35260  1.000 41.31140  ? 160 ILE A CD1  1 
ATOM   1253 N N    . HIS A 1 161 ? -9.86880  21.71089 14.43823  1.000 38.74279  ? 161 HIS A N    1 
ATOM   1254 C CA   . HIS A 1 161 ? -8.54755  21.39364 14.95051  1.000 37.40774  ? 161 HIS A CA   1 
ATOM   1255 C C    . HIS A 1 161 ? -7.98476  20.13803 14.28131  1.000 40.37499  ? 161 HIS A C    1 
ATOM   1256 O O    . HIS A 1 161 ? -8.68896  19.12681 14.13776  1.000 38.25030  ? 161 HIS A O    1 
ATOM   1257 C CB   . HIS A 1 161 ? -8.63541  21.21504 16.49561  1.000 36.60643  ? 161 HIS A CB   1 
ATOM   1258 C CG   . HIS A 1 161 ? -7.31758  20.94353 17.08664  1.000 37.18599  ? 161 HIS A CG   1 
ATOM   1259 N ND1  . HIS A 1 161 ? -6.40484  21.94747 17.32199  1.000 37.77268  ? 161 HIS A ND1  1 
ATOM   1260 C CD2  . HIS A 1 161 ? -6.70000  19.77523 17.39073  1.000 39.35018  ? 161 HIS A CD2  1 
ATOM   1261 C CE1  . HIS A 1 161 ? -5.28985  21.40865 17.79104  1.000 41.81277  ? 161 HIS A CE1  1 
ATOM   1262 N NE2  . HIS A 1 161 ? -5.43906  20.09289 17.82835  1.000 39.71241  ? 161 HIS A NE2  1 
ATOM   1263 N N    . VAL A 1 162 ? -6.70789  20.17651 13.87625  1.000 39.54891  ? 162 VAL A N    1 
ATOM   1264 C CA   . VAL A 1 162 ? -6.17974  19.00458 13.19727  1.000 40.21736  ? 162 VAL A CA   1 
ATOM   1265 C C    . VAL A 1 162 ? -4.82027  18.57199 13.70026  1.000 44.53154  ? 162 VAL A C    1 
ATOM   1266 O O    . VAL A 1 162 ? -4.37309  17.47666 13.33504  1.000 45.30955  ? 162 VAL A O    1 
ATOM   1267 C CB   . VAL A 1 162 ? -6.10039  19.20007 11.64923  1.000 41.15252  ? 162 VAL A CB   1 
ATOM   1268 C CG1  . VAL A 1 162 ? -7.45950  19.44074 11.10606  1.000 37.69921  ? 162 VAL A CG1  1 
ATOM   1269 C CG2  . VAL A 1 162 ? -5.16709  20.35974 11.24408  1.000 40.15627  ? 162 VAL A CG2  1 
ATOM   1270 N N    . GLY A 1 163 ? -4.12963  19.40807 14.48976  1.000 42.95872  ? 163 GLY A N    1 
ATOM   1271 C CA   . GLY A 1 163 ? -2.76278  19.03139 14.85424  1.000 45.22875  ? 163 GLY A CA   1 
ATOM   1272 C C    . GLY A 1 163 ? -2.15531  19.89573 15.95282  1.000 42.13030  ? 163 GLY A C    1 
ATOM   1273 O O    . GLY A 1 163 ? -2.66955  20.95422 16.30526  1.000 40.30209  ? 163 GLY A O    1 
ATOM   1274 N N    . GLY A 1 164 ? -0.98928  19.48148 16.41728  1.000 42.93698  ? 164 GLY A N    1 
ATOM   1275 C CA   . GLY A 1 164 ? -0.37607  20.14397 17.56418  1.000 48.37546  ? 164 GLY A CA   1 
ATOM   1276 C C    . GLY A 1 164 ? 0.94713   19.50749 17.89205  1.000 47.40049  ? 164 GLY A C    1 
ATOM   1277 O O    . GLY A 1 164 ? 1.14560   18.32433 17.60310  1.000 48.35797  ? 164 GLY A O    1 
ATOM   1278 N N    . ASN A 1 165 ? 1.87403   20.26483 18.47347  1.000 47.79588  ? 165 ASN A N    1 
ATOM   1279 C CA   . ASN A 1 165 ? 3.19815   19.72734 18.76283  1.000 49.95335  ? 165 ASN A CA   1 
ATOM   1280 C C    . ASN A 1 165 ? 3.51735   19.76274 20.25162  1.000 53.47875  ? 165 ASN A C    1 
ATOM   1281 O O    . ASN A 1 165 ? 4.68514   19.64598 20.62105  1.000 55.00195  ? 165 ASN A O    1 
ATOM   1282 C CB   . ASN A 1 165 ? 4.26791   20.49899 17.99972  1.000 53.45211  ? 165 ASN A CB   1 
ATOM   1283 C CG   . ASN A 1 165 ? 4.28056   21.95657 18.37437  1.000 53.51813  ? 165 ASN A CG   1 
ATOM   1284 O OD1  . ASN A 1 165 ? 3.68990   22.34861 19.38289  1.000 52.93361  ? 165 ASN A OD1  1 
ATOM   1285 N ND2  . ASN A 1 165 ? 4.91809   22.77284 17.55811  1.000 57.43333  ? 165 ASN A ND2  1 
ATOM   1286 N N    . GLY A 1 166 ? 2.50691   19.93507 21.10588  1.000 50.33488  ? 166 GLY A N    1 
ATOM   1287 C CA   . GLY A 1 166 ? 2.69576   20.11921 22.53692  1.000 51.92797  ? 166 GLY A CA   1 
ATOM   1288 C C    . GLY A 1 166 ? 2.81173   21.57021 22.95221  1.000 51.69155  ? 166 GLY A C    1 
ATOM   1289 O O    . GLY A 1 166 ? 2.68283   21.87391 24.13694  1.000 52.29793  ? 166 GLY A O    1 
ATOM   1290 N N    . ALA A 1 167 ? 3.05555   22.47307 22.01772  1.000 51.25850  ? 167 ALA A N    1 
ATOM   1291 C CA   . ALA A 1 167 ? 3.16316   23.90083 22.30006  1.000 49.28222  ? 167 ALA A CA   1 
ATOM   1292 C C    . ALA A 1 167 ? 2.19027   24.74213 21.49588  1.000 51.36863  ? 167 ALA A C    1 
ATOM   1293 O O    . ALA A 1 167 ? 1.62571   25.69888 22.03042  1.000 51.22878  ? 167 ALA A O    1 
ATOM   1294 C CB   . ALA A 1 167 ? 4.59365   24.39183 22.01735  1.000 51.29388  ? 167 ALA A CB   1 
ATOM   1295 N N    . GLN A 1 168 ? 1.99856   24.42844 20.20798  1.000 50.14101  ? 168 GLN A N    1 
ATOM   1296 C CA   . GLN A 1 168 ? 1.09405   25.16123 19.33825  1.000 50.21184  ? 168 GLN A CA   1 
ATOM   1297 C C    . GLN A 1 168 ? -0.03371  24.22517 18.93608  1.000 43.58251  ? 168 GLN A C    1 
ATOM   1298 O O    . GLN A 1 168 ? 0.13791   23.00541 18.94124  1.000 41.80907  ? 168 GLN A O    1 
ATOM   1299 C CB   . GLN A 1 168 ? 1.82716   25.66751 18.09819  1.000 48.80850  ? 168 GLN A CB   1 
ATOM   1300 C CG   . GLN A 1 168 ? 3.07674   26.47685 18.47679  1.000 51.29679  ? 168 GLN A CG   1 
ATOM   1301 C CD   . GLN A 1 168 ? 3.75760   27.12338 17.28867  1.000 59.75663  ? 168 GLN A CD   1 
ATOM   1302 O OE1  . GLN A 1 168 ? 4.20985   26.44723 16.33126  1.000 60.32033  ? 168 GLN A OE1  1 
ATOM   1303 N NE2  . GLN A 1 168 ? 3.86419   28.45272 17.34485  1.000 61.15181  ? 168 GLN A NE2  1 
ATOM   1304 N N    . GLY A 1 169 ? -1.20077  24.80015 18.65006  1.000 43.04865  ? 169 GLY A N    1 
ATOM   1305 C CA   . GLY A 1 169 ? -2.29895  24.07720 18.02542  1.000 43.00005  ? 169 GLY A CA   1 
ATOM   1306 C C    . GLY A 1 169 ? -2.51738  24.55597 16.59573  1.000 44.98943  ? 169 GLY A C    1 
ATOM   1307 O O    . GLY A 1 169 ? -2.23564  25.71168 16.26828  1.000 44.49461  ? 169 GLY A O    1 
ATOM   1308 N N    . PHE A 1 170 ? -3.03280  23.66972 15.74203  1.000 43.09465  ? 170 PHE A N    1 
ATOM   1309 C CA   . PHE A 1 170 ? -3.26352  23.99270 14.33004  1.000 42.58100  ? 170 PHE A CA   1 
ATOM   1310 C C    . PHE A 1 170 ? -4.64571  23.54231 13.90140  1.000 41.50156  ? 170 PHE A C    1 
ATOM   1311 O O    . PHE A 1 170 ? -5.05794  22.40775 14.20138  1.000 40.16739  ? 170 PHE A O    1 
ATOM   1312 C CB   . PHE A 1 170 ? -2.21435  23.34489 13.44664  1.000 43.00177  ? 170 PHE A CB   1 
ATOM   1313 C CG   . PHE A 1 170 ? -0.81537  23.74084 13.80979  1.000 43.77503  ? 170 PHE A CG   1 
ATOM   1314 C CD1  . PHE A 1 170 ? -0.29551  24.94325 13.37736  1.000 42.93115  ? 170 PHE A CD1  1 
ATOM   1315 C CD2  . PHE A 1 170 ? -0.03771  22.92498 14.61179  1.000 46.94336  ? 170 PHE A CD2  1 
ATOM   1316 C CE1  . PHE A 1 170 ? 1.00955   25.31113 13.70214  1.000 45.14283  ? 170 PHE A CE1  1 
ATOM   1317 C CE2  . PHE A 1 170 ? 1.24248   23.28367 14.96742  1.000 49.08452  ? 170 PHE A CE2  1 
ATOM   1318 C CZ   . PHE A 1 170 ? 1.77354   24.47575 14.50209  1.000 50.21531  ? 170 PHE A CZ   1 
ATOM   1319 N N    . ALA A 1 171 ? -5.34141  24.43694 13.18256  1.000 41.45561  ? 171 ALA A N    1 
ATOM   1320 C CA   . ALA A 1 171 ? -6.65696  24.17669 12.62462  1.000 40.53001  ? 171 ALA A CA   1 
ATOM   1321 C C    . ALA A 1 171 ? -6.62497  24.33471 11.10201  1.000 38.48349  ? 171 ALA A C    1 
ATOM   1322 O O    . ALA A 1 171 ? -5.85730  25.13230 10.55342  1.000 38.54289  ? 171 ALA A O    1 
ATOM   1323 C CB   . ALA A 1 171 ? -7.71042  25.12566 13.21544  1.000 35.91752  ? 171 ALA A CB   1 
ATOM   1324 N N    . ALA A 1 172 ? -7.45285  23.55046 10.43181  1.000 37.98018  ? 172 ALA A N    1 
ATOM   1325 C CA   . ALA A 1 172 ? -7.69712  23.71914 9.00146   1.000 37.08965  ? 172 ALA A CA   1 
ATOM   1326 C C    . ALA A 1 172 ? -8.78173  24.76500 8.80466   1.000 39.66564  ? 172 ALA A C    1 
ATOM   1327 O O    . ALA A 1 172 ? -9.85532  24.65173 9.38726   1.000 37.22778  ? 172 ALA A O    1 
ATOM   1328 C CB   . ALA A 1 172 ? -8.11999  22.38203 8.41027   1.000 36.59312  ? 172 ALA A CB   1 
ATOM   1329 N N    . MET A 1 173 ? -8.52969  25.76042 7.93956   1.000 42.51494  ? 173 MET A N    1 
ATOM   1330 C CA   . MET A 1 173 ? -9.51364  26.82155 7.70129   1.000 40.67479  ? 173 MET A CA   1 
ATOM   1331 C C    . MET A 1 173 ? -10.83476 26.25652 7.19881   1.000 42.01051  ? 173 MET A C    1 
ATOM   1332 O O    . MET A 1 173 ? -10.87706 25.24686 6.49140   1.000 45.85972  ? 173 MET A O    1 
ATOM   1333 C CB   . MET A 1 173 ? -9.01222  27.78935 6.66006   1.000 45.54123  ? 173 MET A CB   1 
ATOM   1334 C CG   . MET A 1 173 ? -7.70615  28.44794 6.96722   1.000 48.88935  ? 173 MET A CG   1 
ATOM   1335 S SD   . MET A 1 173 ? -7.64126  30.03549 6.11803   1.000 52.00207  ? 173 MET A SD   1 
ATOM   1336 C CE   . MET A 1 173 ? -5.98579  30.50848 6.58885   1.000 48.73546  ? 173 MET A CE   1 
ATOM   1337 N N    . LEU A 1 174 ? -11.92359 26.92483 7.56387   1.000 39.11807  ? 174 LEU A N    1 
ATOM   1338 C CA   . LEU A 1 174 ? -13.19393 26.76219 6.89004   1.000 41.70886  ? 174 LEU A CA   1 
ATOM   1339 C C    . LEU A 1 174 ? -13.48481 28.08441 6.20798   1.000 44.31108  ? 174 LEU A C    1 
ATOM   1340 O O    . LEU A 1 174 ? -13.39409 29.13348 6.85323   1.000 40.95058  ? 174 LEU A O    1 
ATOM   1341 C CB   . LEU A 1 174 ? -14.30022 26.38882 7.84687   1.000 39.52345  ? 174 LEU A CB   1 
ATOM   1342 C CG   . LEU A 1 174 ? -14.15570 25.02278 8.51344   1.000 40.87993  ? 174 LEU A CG   1 
ATOM   1343 C CD1  . LEU A 1 174 ? -14.98272 24.98091 9.84010   1.000 39.29444  ? 174 LEU A CD1  1 
ATOM   1344 C CD2  . LEU A 1 174 ? -14.61135 23.94376 7.57382   1.000 39.77901  ? 174 LEU A CD2  1 
ATOM   1345 N N    . LEU A 1 175 ? -13.78030 28.03031 4.90232   1.000 40.47886  ? 175 LEU A N    1 
ATOM   1346 C CA   . LEU A 1 175 ? -14.14883 29.18590 4.09347   1.000 41.53942  ? 175 LEU A CA   1 
ATOM   1347 C C    . LEU A 1 175 ? -15.57869 29.04163 3.59038   1.000 40.03113  ? 175 LEU A C    1 
ATOM   1348 O O    . LEU A 1 175 ? -16.02928 27.94272 3.24828   1.000 39.74433  ? 175 LEU A O    1 
ATOM   1349 C CB   . LEU A 1 175 ? -13.18821 29.35804 2.89455   1.000 41.99893  ? 175 LEU A CB   1 
ATOM   1350 C CG   . LEU A 1 175 ? -11.75049 29.62410 3.37918   1.000 41.36451  ? 175 LEU A CG   1 
ATOM   1351 C CD1  . LEU A 1 175 ? -10.77973 29.52470 2.18938   1.000 45.31963  ? 175 LEU A CD1  1 
ATOM   1352 C CD2  . LEU A 1 175 ? -11.66406 30.97562 4.06108   1.000 46.39445  ? 175 LEU A CD2  1 
ATOM   1353 N N    . HIS A 1 176 ? -16.29478 30.15791 3.54845   1.000 36.15521  ? 176 HIS A N    1 
ATOM   1354 C CA   . HIS A 1 176 ? -17.67477 30.11354 3.10029   1.000 39.63471  ? 176 HIS A CA   1 
ATOM   1355 C C    . HIS A 1 176 ? -17.80653 29.45958 1.71410   1.000 44.25714  ? 176 HIS A C    1 
ATOM   1356 O O    . HIS A 1 176 ? -18.72035 28.65444 1.48422   1.000 41.60065  ? 176 HIS A O    1 
ATOM   1357 C CB   . HIS A 1 176 ? -18.22402 31.53644 3.10328   1.000 41.46820  ? 176 HIS A CB   1 
ATOM   1358 C CG   . HIS A 1 176 ? -19.60578 31.65780 2.55143   1.000 48.20041  ? 176 HIS A CG   1 
ATOM   1359 N ND1  . HIS A 1 176 ? -20.73463 31.60511 3.33643   1.000 46.74454  ? 176 HIS A ND1  1 
ATOM   1360 C CD2  . HIS A 1 176 ? -20.04206 31.81085 1.27898   1.000 46.34174  ? 176 HIS A CD2  1 
ATOM   1361 C CE1  . HIS A 1 176 ? -21.80842 31.74115 2.58207   1.000 45.22859  ? 176 HIS A CE1  1 
ATOM   1362 N NE2  . HIS A 1 176 ? -21.41489 31.86571 1.32857   1.000 49.63848  ? 176 HIS A NE2  1 
ATOM   1363 N N    . SER A 1 177 ? -16.87995 29.74667 0.79161   1.000 41.32867  ? 177 SER A N    1 
ATOM   1364 C CA   . SER A 1 177 ? -17.06191 29.19099 -0.55552  1.000 45.18687  ? 177 SER A CA   1 
ATOM   1365 C C    . SER A 1 177 ? -16.82921 27.67612 -0.60648  1.000 45.42742  ? 177 SER A C    1 
ATOM   1366 O O    . SER A 1 177 ? -16.97453 27.07985 -1.67479  1.000 43.85532  ? 177 SER A O    1 
ATOM   1367 C CB   . SER A 1 177 ? -16.13597 29.89771 -1.54965  1.000 45.16782  ? 177 SER A CB   1 
ATOM   1368 O OG   . SER A 1 177 ? -14.79512 29.49082 -1.32815  1.000 45.78927  ? 177 SER A OG   1 
ATOM   1369 N N    . TYR A 1 178 ? -16.48605 27.02628 0.50795   1.000 41.48338  ? 178 TYR A N    1 
ATOM   1370 C CA   . TYR A 1 178 ? -16.42790 25.56287 0.50211   1.000 42.18335  ? 178 TYR A CA   1 
ATOM   1371 C C    . TYR A 1 178 ? -17.81562 24.94238 0.42448   1.000 40.83412  ? 178 TYR A C    1 
ATOM   1372 O O    . TYR A 1 178 ? -17.92245 23.76627 0.09007   1.000 42.70480  ? 178 TYR A O    1 
ATOM   1373 C CB   . TYR A 1 178 ? -15.74760 25.00175 1.76689   1.000 41.99898  ? 178 TYR A CB   1 
ATOM   1374 C CG   . TYR A 1 178 ? -14.24861 25.22149 1.90461   1.000 42.70866  ? 178 TYR A CG   1 
ATOM   1375 C CD1  . TYR A 1 178 ? -13.49655 25.78145 0.88973   1.000 43.36323  ? 178 TYR A CD1  1 
ATOM   1376 C CD2  . TYR A 1 178 ? -13.59534 24.88137 3.07762   1.000 38.65460  ? 178 TYR A CD2  1 
ATOM   1377 C CE1  . TYR A 1 178 ? -12.09882 25.98244 1.03591   1.000 41.98582  ? 178 TYR A CE1  1 
ATOM   1378 C CE2  . TYR A 1 178 ? -12.21797 25.07387 3.22956   1.000 36.91300  ? 178 TYR A CE2  1 
ATOM   1379 C CZ   . TYR A 1 178 ? -11.47867 25.63620 2.21457   1.000 44.84114  ? 178 TYR A CZ   1 
ATOM   1380 O OH   . TYR A 1 178 ? -10.10730 25.81947 2.39353   1.000 43.00221  ? 178 TYR A OH   1 
ATOM   1381 N N    . PHE A 1 179 ? -18.88319 25.68928 0.73128   1.000 41.93100  ? 179 PHE A N    1 
ATOM   1382 C CA   . PHE A 1 179 ? -20.20317 25.08135 0.95310   1.000 44.37997  ? 179 PHE A CA   1 
ATOM   1383 C C    . PHE A 1 179 ? -21.31369 25.69799 0.11408   1.000 50.16895  ? 179 PHE A C    1 
ATOM   1384 O O    . PHE A 1 179 ? -22.49565 25.52566 0.43366   1.000 49.59210  ? 179 PHE A O    1 
ATOM   1385 C CB   . PHE A 1 179 ? -20.58870 25.15228 2.44933   1.000 42.74477  ? 179 PHE A CB   1 
ATOM   1386 C CG   . PHE A 1 179 ? -19.58973 24.52017 3.30133   1.000 43.23860  ? 179 PHE A CG   1 
ATOM   1387 C CD1  . PHE A 1 179 ? -19.63920 23.15605 3.51286   1.000 42.00503  ? 179 PHE A CD1  1 
ATOM   1388 C CD2  . PHE A 1 179 ? -18.56954 25.26170 3.87721   1.000 43.77487  ? 179 PHE A CD2  1 
ATOM   1389 C CE1  . PHE A 1 179 ? -18.67795 22.53194 4.26940   1.000 39.47258  ? 179 PHE A CE1  1 
ATOM   1390 C CE2  . PHE A 1 179 ? -17.59943 24.65064 4.64575   1.000 37.77418  ? 179 PHE A CE2  1 
ATOM   1391 C CZ   . PHE A 1 179 ? -17.66267 23.27806 4.84641   1.000 41.27767  ? 179 PHE A CZ   1 
ATOM   1392 N N    . THR A 1 180 ? -20.97330 26.39762 -0.95852  1.000 53.95137  ? 180 THR A N    1 
ATOM   1393 C CA   . THR A 1 180 ? -21.99235 27.01155 -1.79323  1.000 58.99007  ? 180 THR A CA   1 
ATOM   1394 C C    . THR A 1 180 ? -22.46687 26.02950 -2.85731  1.000 64.10320  ? 180 THR A C    1 
ATOM   1395 O O    . THR A 1 180 ? -21.71494 25.16525 -3.32977  1.000 63.53819  ? 180 THR A O    1 
ATOM   1396 C CB   . THR A 1 180 ? -21.45781 28.28634 -2.44685  1.000 59.14110  ? 180 THR A CB   1 
ATOM   1397 O OG1  . THR A 1 180 ? -20.26252 27.97360 -3.17190  1.000 59.24325  ? 180 THR A OG1  1 
ATOM   1398 C CG2  . THR A 1 180 ? -21.17736 29.39615 -1.41048  1.000 52.93191  ? 180 THR A CG2  1 
ATOM   1399 N N    . ASP A 1 181 ? -23.72619 26.18364 -3.24479  1.000 70.83592  ? 181 ASP A N    1 
ATOM   1400 C CA   . ASP A 1 181 ? -24.34564 25.34769 -4.29120  1.000 74.36272  ? 181 ASP A CA   1 
ATOM   1401 C C    . ASP A 1 181 ? -23.98568 25.80636 -5.70823  1.000 68.89368  ? 181 ASP A C    1 
ATOM   1402 O O    . ASP A 1 181 ? -23.17830 25.17807 -6.40598  1.000 76.11690  ? 181 ASP A O    1 
ATOM   1403 C CB   . ASP A 1 181 ? -25.85411 25.37789 -4.08505  1.000 76.45488  ? 181 ASP A CB   1 
ATOM   1404 C CG   . ASP A 1 181 ? -26.22376 25.44603 -2.58628  1.000 77.13986  ? 181 ASP A CG   1 
ATOM   1405 O OD1  . ASP A 1 181 ? -26.97155 26.37546 -2.17986  1.000 75.96613  ? 181 ASP A OD1  1 
ATOM   1406 O OD2  . ASP A 1 181 ? -25.69946 24.60963 -1.80020  1.000 75.15453  ? 181 ASP A OD2  1 
ATOM   1407 N N    . GLN A 1 183 ? -21.21021 23.11029 -9.91957  1.000 88.85460  ? 183 GLN A N    1 
ATOM   1408 C CA   . GLN A 1 183 ? -22.03737 22.65646 -11.04066 1.000 89.59346  ? 183 GLN A CA   1 
ATOM   1409 C C    . GLN A 1 183 ? -21.88109 21.13749 -11.26970 1.000 89.58421  ? 183 GLN A C    1 
ATOM   1410 O O    . GLN A 1 183 ? -21.86160 20.35297 -10.30169 1.000 86.22265  ? 183 GLN A O    1 
ATOM   1411 C CB   . GLN A 1 183 ? -21.68644 23.43740 -12.31587 1.000 78.05001  ? 183 GLN A CB   1 
ATOM   1412 N N    . LYS A 1 184 ? -21.76440 20.73860 -12.54550 1.000 87.80880  ? 184 LYS A N    1 
ATOM   1413 C CA   . LYS A 1 184 ? -21.69885 19.32888 -12.94614 1.000 85.40793  ? 184 LYS A CA   1 
ATOM   1414 C C    . LYS A 1 184 ? -20.23915 18.87238 -13.00310 1.000 83.77769  ? 184 LYS A C    1 
ATOM   1415 O O    . LYS A 1 184 ? -19.49456 19.25505 -13.90969 1.000 85.46758  ? 184 LYS A O    1 
ATOM   1416 C CB   . LYS A 1 184 ? -22.38623 19.11913 -14.29657 1.000 80.81672  ? 184 LYS A CB   1 
ATOM   1417 N N    . HIS A 1 185 ? -19.83839 18.02433 -12.05782 1.000 83.75105  ? 185 HIS A N    1 
ATOM   1418 C CA   . HIS A 1 185 ? -18.43829 17.63480 -11.90483 1.000 84.89610  ? 185 HIS A CA   1 
ATOM   1419 C C    . HIS A 1 185 ? -18.33824 16.17128 -11.50553 1.000 75.83695  ? 185 HIS A C    1 
ATOM   1420 O O    . HIS A 1 185 ? -18.85478 15.78199 -10.45491 1.000 74.84831  ? 185 HIS A O    1 
ATOM   1421 C CB   . HIS A 1 185 ? -17.73957 18.50275 -10.84844 1.000 89.91106  ? 185 HIS A CB   1 
ATOM   1422 C CG   . HIS A 1 185 ? -16.25913 18.62628 -11.04981 1.000 98.82788  ? 185 HIS A CG   1 
ATOM   1423 N ND1  . HIS A 1 185 ? -15.67510 18.64661 -12.30126 1.000 103.39468 ? 185 HIS A ND1  1 
ATOM   1424 C CD2  . HIS A 1 185 ? -15.24100 18.70140 -10.15670 1.000 100.34601 ? 185 HIS A CD2  1 
ATOM   1425 C CE1  . HIS A 1 185 ? -14.36355 18.75382 -12.16969 1.000 111.58686 ? 185 HIS A CE1  1 
ATOM   1426 N NE2  . HIS A 1 185 ? -14.07413 18.78754 -10.87962 1.000 112.07649 ? 185 HIS A NE2  1 
ATOM   1427 N N    . HIS A 1 186 ? -17.64141 15.37115 -12.30980 1.000 72.77880  ? 186 HIS A N    1 
ATOM   1428 C CA   . HIS A 1 186 ? -17.27522 14.01225 -11.90265 1.000 66.59911  ? 186 HIS A CA   1 
ATOM   1429 C C    . HIS A 1 186 ? -16.10653 14.10932 -10.92593 1.000 68.60789  ? 186 HIS A C    1 
ATOM   1430 O O    . HIS A 1 186 ? -14.96350 14.34739 -11.32988 1.000 70.03660  ? 186 HIS A O    1 
ATOM   1431 C CB   . HIS A 1 186 ? -16.91106 13.14967 -13.11036 1.000 62.44677  ? 186 HIS A CB   1 
ATOM   1432 C CG   . HIS A 1 186 ? -16.63132 11.72133 -12.75343 1.000 57.58335  ? 186 HIS A CG   1 
ATOM   1433 N ND1  . HIS A 1 186 ? -17.62237 10.85523 -12.33531 1.000 55.17452  ? 186 HIS A ND1  1 
ATOM   1434 C CD2  . HIS A 1 186 ? -15.47114 11.02060 -12.69958 1.000 57.09817  ? 186 HIS A CD2  1 
ATOM   1435 C CE1  . HIS A 1 186 ? -17.08289 9.68266  -12.03517 1.000 57.30258  ? 186 HIS A CE1  1 
ATOM   1436 N NE2  . HIS A 1 186 ? -15.78007 9.75496  -12.25159 1.000 59.09359  ? 186 HIS A NE2  1 
ATOM   1437 N N    . HIS A 1 187 ? -16.37406 13.92196 -9.62856  1.000 68.04336  ? 187 HIS A N    1 
ATOM   1438 C CA   . HIS A 1 187 ? -15.34778 14.17932 -8.62319  1.000 67.53556  ? 187 HIS A CA   1 
ATOM   1439 C C    . HIS A 1 187 ? -14.84180 12.91974 -7.91903  1.000 64.47075  ? 187 HIS A C    1 
ATOM   1440 O O    . HIS A 1 187 ? -14.09145 13.03965 -6.95108  1.000 66.35745  ? 187 HIS A O    1 
ATOM   1441 C CB   . HIS A 1 187 ? -15.83019 15.21157 -7.58966  1.000 70.16861  ? 187 HIS A CB   1 
ATOM   1442 C CG   . HIS A 1 187 ? -17.24224 15.02518 -7.12374  1.000 68.78089  ? 187 HIS A CG   1 
ATOM   1443 N ND1  . HIS A 1 187 ? -17.57379 14.20850 -6.05823  1.000 68.33879  ? 187 HIS A ND1  1 
ATOM   1444 C CD2  . HIS A 1 187 ? -18.40766 15.56695 -7.55962  1.000 72.98060  ? 187 HIS A CD2  1 
ATOM   1445 C CE1  . HIS A 1 187 ? -18.88251 14.25124 -5.85770  1.000 65.01202  ? 187 HIS A CE1  1 
ATOM   1446 N NE2  . HIS A 1 187 ? -19.41206 15.06721 -6.75685  1.000 71.88505  ? 187 HIS A NE2  1 
ATOM   1447 N N    . HIS A 1 188 ? -15.21568 11.72476 -8.38373  1.000 60.37818  ? 188 HIS A N    1 
ATOM   1448 C CA   . HIS A 1 188 ? -14.60669 10.45534 -7.94356  1.000 57.36698  ? 188 HIS A CA   1 
ATOM   1449 C C    . HIS A 1 188 ? -14.12165 9.58597  -9.13410  1.000 64.14588  ? 188 HIS A C    1 
ATOM   1450 O O    . HIS A 1 188 ? -13.34035 8.62982  -8.95838  1.000 65.60523  ? 188 HIS A O    1 
ATOM   1451 C CB   . HIS A 1 188 ? -15.60269 9.66120  -7.08617  1.000 59.46670  ? 188 HIS A CB   1 
ATOM   1452 C CG   . HIS A 1 188 ? -16.13451 10.41394 -5.89243  1.000 58.68070  ? 188 HIS A CG   1 
ATOM   1453 N ND1  . HIS A 1 188 ? -15.31706 11.12388 -5.03889  1.000 59.92291  ? 188 HIS A ND1  1 
ATOM   1454 C CD2  . HIS A 1 188 ? -17.40521 10.65137 -5.47650  1.000 56.16530  ? 188 HIS A CD2  1 
ATOM   1455 C CE1  . HIS A 1 188 ? -16.05243 11.69698 -4.09873  1.000 58.88513  ? 188 HIS A CE1  1 
ATOM   1456 N NE2  . HIS A 1 188 ? -17.32427 11.44448 -4.35429  1.000 56.98525  ? 188 HIS A NE2  1 
HETATM 1457 C C01  . AG7 B 2 .   ? -0.01118  15.85432 14.62725  1.000 50.18891  ? 201 AG7 A C01  1 
HETATM 1458 C C02  . AG7 B 2 .   ? -0.63837  14.75432 13.79740  1.000 48.86011  ? 201 AG7 A C02  1 
HETATM 1459 O O03  . AG7 B 2 .   ? -0.61568  16.78178 15.13202  1.000 47.83546  ? 201 AG7 A O03  1 
HETATM 1460 C C04  . AG7 B 2 .   ? -2.13506  14.88464 13.63353  1.000 47.05936  ? 201 AG7 A C04  1 
HETATM 1461 C C05  . AG7 B 2 .   ? -2.70589  13.72809 12.80991  1.000 52.85779  ? 201 AG7 A C05  1 
HETATM 1462 C C06  . AG7 B 2 .   ? -2.35132  13.75866 11.32800  1.000 56.48822  ? 201 AG7 A C06  1 
HETATM 1463 C C07  . AG7 B 2 .   ? -3.02457  14.60843 10.42092  1.000 57.07061  ? 201 AG7 A C07  1 
HETATM 1464 C C08  . AG7 B 2 .   ? -2.71979  14.61908 9.04653   1.000 57.08942  ? 201 AG7 A C08  1 
HETATM 1465 C C09  . AG7 B 2 .   ? -1.72536  13.76862 8.58434   1.000 56.67857  ? 201 AG7 A C09  1 
HETATM 1466 C C10  . AG7 B 2 .   ? -1.03392  12.91858 9.42608   1.000 59.24673  ? 201 AG7 A C10  1 
HETATM 1467 C C11  . AG7 B 2 .   ? -1.34828  12.92164 10.79563  1.000 59.32569  ? 201 AG7 A C11  1 
HETATM 1468 N N12  . AG7 B 2 .   ? -3.74038  15.49813 15.43086  1.000 46.48707  ? 201 AG7 A N12  1 
HETATM 1469 C C13  . AG7 B 2 .   ? -4.30170  15.28766 16.74615  1.000 47.16373  ? 201 AG7 A C13  1 
HETATM 1470 C C14  . AG7 B 2 .   ? -4.12398  16.50200 17.62884  1.000 40.96800  ? 201 AG7 A C14  1 
HETATM 1471 C C15  . AG7 B 2 .   ? -2.66921  16.72946 18.05455  1.000 48.23550  ? 201 AG7 A C15  1 
HETATM 1472 C C16  . AG7 B 2 .   ? -2.46296  17.90191 19.03908  1.000 44.65065  ? 201 AG7 A C16  1 
HETATM 1473 N N17  . AG7 B 2 .   ? -1.42528  17.56761 19.85416  1.000 43.63555  ? 201 AG7 A N17  1 
HETATM 1474 O O18  . AG7 B 2 .   ? -3.07121  18.95718 19.04639  1.000 45.06322  ? 201 AG7 A O18  1 
HETATM 1475 C C19  . AG7 B 2 .   ? -5.80472  14.95580 16.69209  1.000 47.37582  ? 201 AG7 A C19  1 
HETATM 1476 C C20  . AG7 B 2 .   ? -6.09269  13.55485 16.19026  1.000 52.56338  ? 201 AG7 A C20  1 
HETATM 1477 C C21  . AG7 B 2 .   ? -5.79773  12.53522 17.27668  1.000 57.95327  ? 201 AG7 A C21  1 
HETATM 1478 O O22  . AG7 B 2 .   ? -5.16030  11.46552 16.76026  1.000 62.04315  ? 201 AG7 A O22  1 
HETATM 1479 O O23  . AG7 B 2 .   ? -6.10253  12.67292 18.46220  1.000 56.32748  ? 201 AG7 A O23  1 
HETATM 1480 C C47  . AG7 B 2 .   ? -2.71519  14.70075 15.03431  1.000 51.97988  ? 201 AG7 A C47  1 
HETATM 1481 O O48  . AG7 B 2 .   ? -2.22719  13.82521 15.74610  1.000 49.76898  ? 201 AG7 A O48  1 
HETATM 1482 C C50  . AG7 B 2 .   ? -5.61473  11.03129 15.44296  1.000 64.24100  ? 201 AG7 A C50  1 
HETATM 1483 C C53  . AG7 B 2 .   ? -5.42104  9.54431  15.25180  1.000 67.34900  ? 201 AG7 A C53  1 
HETATM 1484 C C57  . AG7 B 2 .   ? 1.51739   15.78685 14.75896  1.000 49.76323  ? 201 AG7 A C57  1 
HETATM 1485 N N58  . AG7 B 2 .   ? 2.00298   17.14813 14.89225  1.000 51.22898  ? 201 AG7 A N58  1 
HETATM 1486 C C59  . AG7 B 2 .   ? 2.65301   17.71123 13.83162  1.000 55.33107  ? 201 AG7 A C59  1 
HETATM 1487 O O60  . AG7 B 2 .   ? 2.86734   17.15259 12.78316  1.000 57.53651  ? 201 AG7 A O60  1 
HETATM 1488 C C78  . AG7 B 2 .   ? 1.96171   14.83920 15.86600  1.000 54.11787  ? 201 AG7 A C78  1 
HETATM 1489 C C81  . AG7 B 2 .   ? 3.23510   15.35747 16.51276  1.000 55.42030  ? 201 AG7 A C81  1 
HETATM 1490 F F1   . AG7 B 2 .   ? -1.41107  13.76211 7.26328   1.000 63.49529  ? 201 AG7 A F1   1 
HETATM 1491 C C82  . AG7 B 2 .   ? 0.90700   14.74070 16.92144  1.000 53.78403  ? 201 AG7 A C82  1 
HETATM 1492 C C83  . AG7 B 2 .   ? -0.83496  16.26048 19.62125  1.000 46.36828  ? 201 AG7 A C83  1 
HETATM 1493 C C84  . AG7 B 2 .   ? -1.88783  15.56258 18.72613  1.000 46.48837  ? 201 AG7 A C84  1 
HETATM 1494 C C1   . AG7 B 2 .   ? 3.16366   19.10076 13.97643  1.000 55.63482  ? 201 AG7 A C1   1 
HETATM 1495 C C2   . AG7 B 2 .   ? 4.01088   19.81646 13.06501  1.000 56.88635  ? 201 AG7 A C2   1 
HETATM 1496 C C3   . AG7 B 2 .   ? 4.17690   21.01555 13.69789  1.000 59.11156  ? 201 AG7 A C3   1 
HETATM 1497 O O4   . AG7 B 2 .   ? 3.50636   21.00446 14.88201  1.000 60.64433  ? 201 AG7 A O4   1 
HETATM 1498 N N5   . AG7 B 2 .   ? 2.85845   19.78631 15.03158  1.000 56.92943  ? 201 AG7 A N5   1 
HETATM 1499 C C4   . AG7 B 2 .   ? 4.90058   22.28062 13.40345  1.000 62.03206  ? 201 AG7 A C4   1 
HETATM 1500 H H2   . AG7 B 2 .   ? -0.38772  13.79630 14.26473  1.000 58.63213  ? 201 AG7 A H2   1 
HETATM 1501 H H3   . AG7 B 2 .   ? -0.14646  14.74931 12.81912  1.000 58.63213  ? 201 AG7 A H3   1 
HETATM 1502 H H27  . AG7 B 2 .   ? -2.39394  15.83912 13.16580  1.000 56.47123  ? 201 AG7 A H27  1 
HETATM 1503 H H28  . AG7 B 2 .   ? -3.79543  13.73273 12.91897  1.000 63.42935  ? 201 AG7 A H28  1 
HETATM 1504 H H29  . AG7 B 2 .   ? -2.35140  12.78784 13.24499  1.000 63.42935  ? 201 AG7 A H29  1 
HETATM 1505 H H30  . AG7 B 2 .   ? -3.79920  15.27382 10.78757  1.000 68.48473  ? 201 AG7 A H30  1 
HETATM 1506 H H31  . AG7 B 2 .   ? -3.23917  15.26899 8.35317   1.000 68.50730  ? 201 AG7 A H31  1 
HETATM 1507 H H33  . AG7 B 2 .   ? -0.26744  12.26887 9.02203   1.000 71.09607  ? 201 AG7 A H33  1 
HETATM 1508 H H34  . AG7 B 2 .   ? -0.80134  12.25968 11.45889  1.000 71.19082  ? 201 AG7 A H34  1 
HETATM 1509 H H49  . AG7 B 2 .   ? -4.10946  16.22188 14.83248  1.000 55.78448  ? 201 AG7 A H49  1 
HETATM 1510 H H91  . AG7 B 2 .   ? -3.74826  14.42590 17.12502  1.000 56.59648  ? 201 AG7 A H91  1 
HETATM 1511 H H35  . AG7 B 2 .   ? -4.49397  17.38297 17.09200  1.000 49.16160  ? 201 AG7 A H35  1 
HETATM 1512 H H36  . AG7 B 2 .   ? -4.75504  16.38516 18.51727  1.000 49.16160  ? 201 AG7 A H36  1 
HETATM 1513 H H94  . AG7 B 2 .   ? -2.13662  17.04374 17.14847  1.000 57.88260  ? 201 AG7 A H94  1 
HETATM 1514 H H39  . AG7 B 2 .   ? -1.11080  18.21057 20.56535  1.000 52.36266  ? 201 AG7 A H39  1 
HETATM 1515 H H191 . AG7 B 2 .   ? -6.20356  15.04226 17.70281  1.000 56.85098  ? 201 AG7 A H191 1 
HETATM 1516 H H41  . AG7 B 2 .   ? -7.13675  13.45066 15.88410  1.000 63.07605  ? 201 AG7 A H41  1 
HETATM 1517 H H42  . AG7 B 2 .   ? -5.48830  13.31704 15.31116  1.000 63.07605  ? 201 AG7 A H42  1 
HETATM 1518 H H51  . AG7 B 2 .   ? -5.05168  11.60321 14.70098  1.000 77.08919  ? 201 AG7 A H51  1 
HETATM 1519 H H52  . AG7 B 2 .   ? -6.66841  11.30844 15.35587  1.000 77.08919  ? 201 AG7 A H52  1 
HETATM 1520 H H53  . AG7 B 2 .   ? -6.04690  9.19658  14.42594  1.000 80.81880  ? 201 AG7 A H53  1 
HETATM 1521 H H54  . AG7 B 2 .   ? -4.37227  9.33789  15.02351  1.000 80.81880  ? 201 AG7 A H54  1 
HETATM 1522 H H56  . AG7 B 2 .   ? -5.70316  9.01754  16.16699  1.000 80.81880  ? 201 AG7 A H56  1 
HETATM 1523 H H77  . AG7 B 2 .   ? 1.95906   15.42018 13.83119  1.000 59.71588  ? 201 AG7 A H77  1 
HETATM 1524 H H61  . AG7 B 2 .   ? 1.86373   17.66844 15.75018  1.000 61.47478  ? 201 AG7 A H61  1 
HETATM 1525 H H79  . AG7 B 2 .   ? 2.13362   13.85903 15.40434  1.000 64.94144  ? 201 AG7 A H79  1 
HETATM 1526 H H82  . AG7 B 2 .   ? 3.01139   16.23418 17.12592  1.000 66.50436  ? 201 AG7 A H82  1 
HETATM 1527 H H84  . AG7 B 2 .   ? 3.95742   15.63726 15.74165  1.000 66.50436  ? 201 AG7 A H84  1 
HETATM 1528 H H85  . AG7 B 2 .   ? 3.67327   14.58221 17.14652  1.000 66.50436  ? 201 AG7 A H85  1 
HETATM 1529 H H86  . AG7 B 2 .   ? 1.33020   14.31899 17.83790  1.000 64.54083  ? 201 AG7 A H86  1 
HETATM 1530 H H87  . AG7 B 2 .   ? 0.09196   14.09590 16.57970  1.000 64.54083  ? 201 AG7 A H87  1 
HETATM 1531 H H88  . AG7 B 2 .   ? 0.50294   15.73287 17.14318  1.000 64.54083  ? 201 AG7 A H88  1 
HETATM 1532 H H89  . AG7 B 2 .   ? 0.13233   16.35764 19.12169  1.000 55.64193  ? 201 AG7 A H89  1 
HETATM 1533 H H90  . AG7 B 2 .   ? -0.68141  15.73278 20.56603  1.000 55.64193  ? 201 AG7 A H90  1 
HETATM 1534 H H92  . AG7 B 2 .   ? -1.39992  14.92802 17.98628  1.000 55.78604  ? 201 AG7 A H92  1 
HETATM 1535 H H93  . AG7 B 2 .   ? -2.54421  14.93381 19.32772  1.000 55.78604  ? 201 AG7 A H93  1 
HETATM 1536 H H8   . AG7 B 2 .   ? 4.40603   19.47663 12.12365  1.000 68.26362  ? 201 AG7 A H8   1 
HETATM 1537 H H5   . AG7 B 2 .   ? 5.86093   22.07572 12.92346  1.000 74.43847  ? 201 AG7 A H5   1 
HETATM 1538 H H6   . AG7 B 2 .   ? 4.31495   22.91604 12.73417  1.000 74.43847  ? 201 AG7 A H6   1 
HETATM 1539 H H7   . AG7 B 2 .   ? 5.09257   22.84079 14.32214  1.000 74.43847  ? 201 AG7 A H7   1 
HETATM 1540 O O    . HOH C 3 .   ? -20.62211 19.55254 -8.55468  1.000 81.02306  ? 301 HOH A O    1 
HETATM 1541 O O    . HOH C 3 .   ? -29.36116 4.20034  5.26478   1.000 58.15866  ? 302 HOH A O    1 
HETATM 1542 O O    . HOH C 3 .   ? -13.171   7.258    -10.898   1.000 66.92557  ? 303 HOH A O    1 
HETATM 1543 O O    . HOH C 3 .   ? 4.17705   27.74273 7.64768   1.000 49.38040  ? 304 HOH A O    1 
HETATM 1544 O O    . HOH C 3 .   ? -31.40824 10.61719 4.74169   1.000 50.24965  ? 305 HOH A O    1 
HETATM 1545 O O    . HOH C 3 .   ? -13.466   31.506   -1.743    1.000 48.63701  ? 306 HOH A O    1 
HETATM 1546 O O    . HOH C 3 .   ? -18.68635 6.70767  19.19763  1.000 52.99479  ? 307 HOH A O    1 
HETATM 1547 O O    . HOH C 3 .   ? -12.03142 13.38397 23.21957  1.000 49.62250  ? 308 HOH A O    1 
HETATM 1548 O O    . HOH C 3 .   ? -6.855    1.478    10.853    1.000 68.46888  ? 309 HOH A O    1 
HETATM 1549 O O    . HOH C 3 .   ? -27.74892 15.69475 9.86597   1.000 46.67753  ? 310 HOH A O    1 
HETATM 1550 O O    . HOH C 3 .   ? -29.28293 23.32930 6.72415   1.000 50.89999  ? 311 HOH A O    1 
HETATM 1551 O O    . HOH C 3 .   ? -20.82248 2.54517  -0.79097  1.000 44.70497  ? 312 HOH A O    1 
HETATM 1552 O O    . HOH C 3 .   ? -4.54700  13.67065 6.17600   1.000 55.58372  ? 313 HOH A O    1 
HETATM 1553 O O    . HOH C 3 .   ? -20.08033 10.49889 26.73940  1.000 49.46725  ? 314 HOH A O    1 
HETATM 1554 O O    . HOH C 3 .   ? -12.48260 16.28191 19.24897  1.000 40.99811  ? 315 HOH A O    1 
HETATM 1555 O O    . HOH C 3 .   ? -22.127   6.092    -0.230    1.000 47.91517  ? 316 HOH A O    1 
HETATM 1556 O O    . HOH C 3 .   ? -15.94749 6.05166  8.23785   1.000 45.90059  ? 317 HOH A O    1 
HETATM 1557 O O    . HOH C 3 .   ? -9.00804  32.73369 23.81888  1.000 46.01623  ? 318 HOH A O    1 
HETATM 1558 O O    . HOH C 3 .   ? -25.71000 18.85615 17.81583  1.000 54.12828  ? 319 HOH A O    1 
HETATM 1559 O O    . HOH C 3 .   ? -32.50247 22.93229 3.09395   1.000 66.13760  ? 320 HOH A O    1 
HETATM 1560 O O    . HOH C 3 .   ? -29.10835 21.57179 14.10168  1.000 51.37519  ? 321 HOH A O    1 
HETATM 1561 O O    . HOH C 3 .   ? -12.39073 36.94663 8.62643   1.000 47.77952  ? 322 HOH A O    1 
HETATM 1562 O O    . HOH C 3 .   ? -14.13556 33.87573 21.15136  1.000 47.51425  ? 323 HOH A O    1 
HETATM 1563 O O    . HOH C 3 .   ? -7.97010  16.54336 2.37975   1.000 44.88529  ? 324 HOH A O    1 
HETATM 1564 O O    . HOH C 3 .   ? -19.60303 35.05131 8.00252   1.000 54.23327  ? 325 HOH A O    1 
HETATM 1565 O O    . HOH C 3 .   ? -2.79938  31.66865 20.73310  1.000 47.49574  ? 326 HOH A O    1 
HETATM 1566 O O    . HOH C 3 .   ? -26.86601 9.67021  14.87940  1.000 50.71618  ? 327 HOH A O    1 
HETATM 1567 O O    . HOH C 3 .   ? 0.04804   21.02388 21.01394  1.000 44.24449  ? 328 HOH A O    1 
HETATM 1568 O O    . HOH C 3 .   ? -8.97119  24.72719 4.66094   1.000 39.15833  ? 329 HOH A O    1 
HETATM 1569 O O    . HOH C 3 .   ? -28.15914 5.60477  9.98494   1.000 52.38722  ? 330 HOH A O    1 
HETATM 1570 O O    . HOH C 3 .   ? -16.30991 31.96939 20.14910  1.000 45.38277  ? 331 HOH A O    1 
HETATM 1571 O O    . HOH C 3 .   ? -13.67671 9.94347  23.18168  1.000 49.99650  ? 332 HOH A O    1 
HETATM 1572 O O    . HOH C 3 .   ? -26.98882 9.11593  12.10124  1.000 51.40825  ? 333 HOH A O    1 
HETATM 1573 O O    . HOH C 3 .   ? -14.03131 37.57965 14.98823  1.000 52.35183  ? 334 HOH A O    1 
HETATM 1574 O O    . HOH C 3 .   ? 3.75542   23.86133 -0.05690  1.000 55.28460  ? 335 HOH A O    1 
HETATM 1575 O O    . HOH C 3 .   ? -6.70930  23.85033 5.68070   1.000 39.78483  ? 336 HOH A O    1 
HETATM 1576 O O    . HOH C 3 .   ? -23.34296 14.83108 -3.33868  1.000 54.34606  ? 337 HOH A O    1 
HETATM 1577 O O    . HOH C 3 .   ? -26.20875 30.17021 6.53670   1.000 56.97344  ? 338 HOH A O    1 
HETATM 1578 O O    . HOH C 3 .   ? -0.56381  17.25105 0.27345   1.000 50.13715  ? 339 HOH A O    1 
HETATM 1579 O O    . HOH C 3 .   ? -15.19500 18.86423 12.84546  1.000 39.68650  ? 340 HOH A O    1 
HETATM 1580 O O    . HOH C 3 .   ? -13.89413 4.11637  8.74683   1.000 54.92715  ? 341 HOH A O    1 
HETATM 1581 O O    . HOH C 3 .   ? -27.93160 -0.53863 2.86767   1.000 49.33893  ? 342 HOH A O    1 
HETATM 1582 O O    . HOH C 3 .   ? -15.42137 26.94954 19.54044  1.000 40.56692  ? 343 HOH A O    1 
HETATM 1583 O O    . HOH C 3 .   ? -27.62083 5.81752  7.51029   1.000 49.52907  ? 344 HOH A O    1 
HETATM 1584 O O    . HOH C 3 .   ? -5.33276  8.08983  9.14100   1.000 64.49206  ? 345 HOH A O    1 
HETATM 1585 O O    . HOH C 3 .   ? -11.24909 30.48621 8.12778   1.000 41.11975  ? 346 HOH A O    1 
HETATM 1586 O O    . HOH C 3 .   ? -10.47134 19.08449 -3.47842  1.000 47.19958  ? 347 HOH A O    1 
HETATM 1587 O O    . HOH C 3 .   ? -10.17465 32.91716 7.97614   1.000 40.10765  ? 348 HOH A O    1 
HETATM 1588 O O    . HOH C 3 .   ? -11.06588 38.27119 15.75757  1.000 43.60707  ? 349 HOH A O    1 
HETATM 1589 O O    . HOH C 3 .   ? -9.23201  21.77823 -5.86263  1.000 53.69356  ? 350 HOH A O    1 
HETATM 1590 O O    . HOH C 3 .   ? -3.13720  29.62733 1.47541   1.000 52.98415  ? 351 HOH A O    1 
HETATM 1591 O O    . HOH C 3 .   ? -25.02065 15.53679 18.85332  1.000 52.25653  ? 352 HOH A O    1 
HETATM 1592 O O    . HOH C 3 .   ? -20.18732 7.93011  17.03438  1.000 46.48135  ? 353 HOH A O    1 
HETATM 1593 O O    . HOH C 3 .   ? -20.991   34.060   28.999    1.000 57.58645  ? 354 HOH A O    1 
HETATM 1594 O O    . HOH C 3 .   ? -24.57774 36.65122 9.50079   1.000 66.83972  ? 355 HOH A O    1 
HETATM 1595 O O    . HOH C 3 .   ? -21.57363 9.22271  21.68565  1.000 56.59899  ? 356 HOH A O    1 
HETATM 1596 O O    . HOH C 3 .   ? -11.94581 13.35099 -2.30766  1.000 53.81076  ? 357 HOH A O    1 
HETATM 1597 O O    . HOH C 3 .   ? -31.19206 26.37413 9.34315   1.000 52.09130  ? 358 HOH A O    1 
HETATM 1598 O O    . HOH C 3 .   ? -10.64204 7.95480  19.76791  1.000 54.87230  ? 359 HOH A O    1 
HETATM 1599 O O    . HOH C 3 .   ? -18.62521 -0.36546 16.85398  1.000 62.69386  ? 360 HOH A O    1 
HETATM 1600 O O    . HOH C 3 .   ? -31.10048 9.60689  11.42741  1.000 48.64967  ? 361 HOH A O    1 
HETATM 1601 O O    . HOH C 3 .   ? -13.30643 36.94790 5.93553   1.000 45.40027  ? 362 HOH A O    1 
HETATM 1602 O O    . HOH C 3 .   ? -10.60040 22.92737 -2.52783  1.000 53.14179  ? 363 HOH A O    1 
HETATM 1603 O O    . HOH C 3 .   ? -2.91235  34.82954 22.59874  1.000 50.10858  ? 364 HOH A O    1 
HETATM 1604 O O    . HOH C 3 .   ? -20.17080 34.78807 22.62472  1.000 50.06004  ? 365 HOH A O    1 
HETATM 1605 O O    . HOH C 3 .   ? -14.56572 36.44962 19.93387  1.000 53.77487  ? 366 HOH A O    1 
HETATM 1606 O O    . HOH C 3 .   ? -25.53689 1.28646  14.61730  1.000 62.14411  ? 367 HOH A O    1 
HETATM 1607 O O    . HOH C 3 .   ? -4.13150  27.18779 -1.10442  1.000 49.45051  ? 368 HOH A O    1 
HETATM 1608 O O    . HOH C 3 .   ? -0.00220  29.06798 25.94956  1.000 62.30902  ? 369 HOH A O    1 
HETATM 1609 O O    . HOH C 3 .   ? 6.01912   22.43951 9.16171   1.000 57.38770  ? 370 HOH A O    1 
HETATM 1610 O O    . HOH C 3 .   ? -6.65609  9.61657  5.55955   1.000 57.13953  ? 371 HOH A O    1 
HETATM 1611 O O    . HOH C 3 .   ? -21.96275 21.80483 0.73182   1.000 45.30755  ? 372 HOH A O    1 
HETATM 1612 O O    . HOH C 3 .   ? -27.65027 16.83959 2.64208   1.000 46.21586  ? 373 HOH A O    1 
HETATM 1613 O O    . HOH C 3 .   ? -9.91271  25.25008 -2.41622  1.000 52.47891  ? 374 HOH A O    1 
HETATM 1614 O O    . HOH C 3 .   ? -5.53220  31.21682 25.99473  1.000 52.62725  ? 375 HOH A O    1 
HETATM 1615 O O    . HOH C 3 .   ? -1.12191  32.64441 16.90982  1.000 48.88055  ? 376 HOH A O    1 
HETATM 1616 O O    . HOH C 3 .   ? -21.16368 36.37971 10.72849  1.000 62.08512  ? 377 HOH A O    1 
HETATM 1617 O O    . HOH C 3 .   ? -10.978   10.985   5.027     1.000 54.18862  ? 378 HOH A O    1 
HETATM 1618 O O    . HOH C 3 .   ? -1.14371  28.01981 2.85264   1.000 46.28445  ? 379 HOH A O    1 
HETATM 1619 O O    . HOH C 3 .   ? -8.72550  11.26581 16.85184  1.000 52.67077  ? 380 HOH A O    1 
HETATM 1620 O O    . HOH C 3 .   ? -19.40610 35.05265 2.01730   1.000 55.38680  ? 381 HOH A O    1 
HETATM 1621 O O    . HOH C 3 .   ? -2.76217  31.29626 24.57960  1.000 55.66407  ? 382 HOH A O    1 
HETATM 1622 O O    . HOH C 3 .   ? 3.21643   12.13644 2.77104   1.000 68.64175  ? 383 HOH A O    1 
HETATM 1623 O O    . HOH C 3 .   ? 5.87315   16.63298 10.99789  1.000 57.50741  ? 384 HOH A O    1 
HETATM 1624 O O    . HOH C 3 .   ? -16.54198 37.13897 6.21163   1.000 52.41615  ? 385 HOH A O    1 
HETATM 1625 O O    . HOH C 3 .   ? -28.13185 2.25687  12.07157  1.000 62.28879  ? 386 HOH A O    1 
HETATM 1626 O O    . HOH C 3 .   ? -28.62689 19.21062 17.86821  1.000 64.56755  ? 387 HOH A O    1 
HETATM 1627 O O    . HOH C 3 .   ? 0.39625   17.11169 23.10426  1.000 50.32816  ? 388 HOH A O    1 
HETATM 1628 O O    . HOH C 3 .   ? -16.15685 22.13455 -1.98663  1.000 57.34026  ? 389 HOH A O    1 
HETATM 1629 O O    . HOH C 3 .   ? 9.46538   19.62875 8.71748   1.000 70.56311  ? 390 HOH A O    1 
HETATM 1630 O O    . HOH C 3 .   ? -20.33979 20.12076 22.73343  1.000 53.39281  ? 391 HOH A O    1 
HETATM 1631 O O    . HOH C 3 .   ? -14.44840 2.38586  15.62750  1.000 59.93141  ? 392 HOH A O    1 
HETATM 1632 O O    . HOH C 3 .   ? 3.66484   32.91826 17.50128  1.000 56.93508  ? 393 HOH A O    1 
HETATM 1633 O O    . HOH C 3 .   ? 6.88353   21.24263 15.46070  1.000 63.80927  ? 394 HOH A O    1 
HETATM 1634 O O    . HOH C 3 .   ? -19.79108 35.08383 25.86853  1.000 54.89108  ? 395 HOH A O    1 
HETATM 1635 O O    . HOH C 3 .   ? -11.23544 3.96408  4.93169   1.000 60.47619  ? 396 HOH A O    1 
HETATM 1636 O O    . HOH C 3 .   ? -6.25504  15.05010 12.12045  1.000 55.30003  ? 397 HOH A O    1 
HETATM 1637 O O    . HOH C 3 .   ? -1.16313  14.91905 23.24569  1.000 47.04209  ? 398 HOH A O    1 
HETATM 1638 O O    . HOH C 3 .   ? -35.04922 17.82816 3.00144   1.000 73.59516  ? 399 HOH A O    1 
HETATM 1639 O O    . HOH C 3 .   ? -7.33411  33.29234 26.24161  1.000 55.83264  ? 400 HOH A O    1 
HETATM 1640 O O    . HOH C 3 .   ? -3.60830  37.45440 15.44445  1.000 55.05888  ? 401 HOH A O    1 
HETATM 1641 O O    . HOH C 3 .   ? -25.95628 31.43983 17.62043  1.000 57.62170  ? 402 HOH A O    1 
HETATM 1642 O O    . HOH C 3 .   ? -27.93511 17.13914 14.69355  1.000 57.46724  ? 403 HOH A O    1 
HETATM 1643 O O    . HOH C 3 .   ? -14.23004 15.17400 -4.11820  1.000 56.68262  ? 404 HOH A O    1 
HETATM 1644 O O    . HOH C 3 .   ? -24.35069 33.21456 20.75456  1.000 56.77149  ? 405 HOH A O    1 
HETATM 1645 O O    . HOH C 3 .   ? -24.53159 32.63360 3.89263   1.000 54.01808  ? 406 HOH A O    1 
HETATM 1646 O O    . HOH C 3 .   ? 2.924     24.709   -2.760    1.000 59.35469  ? 407 HOH A O    1 
HETATM 1647 O O    . HOH C 3 .   ? -26.40518 27.55989 23.96532  1.000 55.91088  ? 408 HOH A O    1 
HETATM 1648 O O    . HOH C 3 .   ? -22.61052 35.45156 21.69988  1.000 60.33037  ? 409 HOH A O    1 
HETATM 1649 O O    . HOH C 3 .   ? -21.07402 2.10727  21.45003  1.000 66.59177  ? 410 HOH A O    1 
HETATM 1650 O O    . HOH C 3 .   ? -17.54885 3.74606  21.45335  1.000 63.63212  ? 411 HOH A O    1 
HETATM 1651 O O    . HOH C 3 .   ? -24.59024 29.94209 1.71796   1.000 63.50636  ? 412 HOH A O    1 
HETATM 1652 O O    . HOH C 3 .   ? -23.34774 10.14040 21.55216  1.000 55.13747  ? 413 HOH A O    1 
HETATM 1653 O O    . HOH C 3 .   ? 5.22772   10.25033 9.94264   1.000 70.57310  ? 414 HOH A O    1 
HETATM 1654 O O    . HOH C 3 .   ? -6.20691  3.08438  6.17953   1.000 68.43219  ? 415 HOH A O    1 
HETATM 1655 O O    . HOH C 3 .   ? -1.247    19.932   -9.488    1.000 59.98445  ? 416 HOH A O    1 
HETATM 1656 O O    . HOH C 3 .   ? -26.496   2.309    7.058     1.000 58.28257  ? 417 HOH A O    1 
HETATM 1657 O O    . HOH C 3 .   ? 0.37138   34.16604 5.40226   1.000 63.99128  ? 418 HOH A O    1 
HETATM 1658 O O    . HOH C 3 .   ? -3.86050  11.73555 7.25240   1.000 59.50381  ? 419 HOH A O    1 
HETATM 1659 O O    . HOH C 3 .   ? 6.17830   17.75667 15.58768  1.000 65.72932  ? 420 HOH A O    1 
HETATM 1660 O O    . HOH C 3 .   ? -11.43029 11.01366 22.58858  1.000 60.09988  ? 421 HOH A O    1 
HETATM 1661 O O    . HOH C 3 .   ? -7.35320  12.77515 26.56764  1.000 66.69394  ? 422 HOH A O    1 
HETATM 1662 O O    . HOH C 3 .   ? -1.831    28.203   -1.973    1.000 62.36150  ? 423 HOH A O    1 
HETATM 1663 O O    . HOH C 3 .   ? 6.13042   16.74562 18.25779  1.000 67.36219  ? 424 HOH A O    1 
HETATM 1664 O O    . HOH C 3 .   ? 1.77018   16.91679 -1.15620  1.000 55.34908  ? 425 HOH A O    1 
HETATM 1665 O O    . HOH C 3 .   ? -19.24179 17.53783 -1.27979  1.000 64.09749  ? 426 HOH A O    1 
HETATM 1666 O O    . HOH C 3 .   ? -16.79061 19.78251 -2.34732  1.000 62.45888  ? 427 HOH A O    1 
HETATM 1667 O O    . HOH C 3 .   ? 0.08398   12.58536 20.15605  1.000 65.29170  ? 428 HOH A O    1 
HETATM 1668 O O    . HOH C 3 .   ? 3.02154   10.98871 17.51632  1.000 71.71418  ? 429 HOH A O    1 
HETATM 1669 O O    . HOH C 3 .   ? 4.15372   14.42635 -5.75956  1.000 75.46257  ? 430 HOH A O    1 
# 
