data_9HQ9
# 
_entry.id   9HQ9 
# 
_audit_conform.dict_name       mmcif_pdbx.dic 
_audit_conform.dict_version    5.403 
_audit_conform.dict_location   http://mmcif.pdb.org/dictionaries/ascii/mmcif_pdbx.dic 
# 
loop_
_database_2.database_id 
_database_2.database_code 
_database_2.pdbx_database_accession 
_database_2.pdbx_DOI 
PDB   9HQ9         pdb_00009hq9 10.2210/pdb9hq9/pdb 
WWPDB D_1292144006 ?            ?                   
# 
loop_
_pdbx_audit_revision_history.ordinal 
_pdbx_audit_revision_history.data_content_type 
_pdbx_audit_revision_history.major_revision 
_pdbx_audit_revision_history.minor_revision 
_pdbx_audit_revision_history.revision_date 
_pdbx_audit_revision_history.part_number 
1 'Structure model' 1 0 2025-01-22 ? 
2 'Structure model' 1 1 2025-03-26 ? 
3 'Structure model' 1 2 2025-04-02 ? 
# 
_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             ? 
# 
loop_
_pdbx_audit_revision_group.ordinal 
_pdbx_audit_revision_group.revision_ordinal 
_pdbx_audit_revision_group.data_content_type 
_pdbx_audit_revision_group.group 
1 2 'Structure model' 'Database references' 
2 3 'Structure model' '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 
3 3 'Structure model' citation        
# 
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 3 'Structure model' '_citation.journal_volume' 
2 3 'Structure model' '_citation.title'          
# 
_pdbx_database_PDB_obs_spr.id               SPRSDE 
_pdbx_database_PDB_obs_spr.date             2025-01-22 
_pdbx_database_PDB_obs_spr.pdb_id           9HQ9 
_pdbx_database_PDB_obs_spr.replace_pdb_id   9F4M 
_pdbx_database_PDB_obs_spr.details          ? 
# 
_pdbx_database_status.status_code                     REL 
_pdbx_database_status.status_code_sf                  REL 
_pdbx_database_status.status_code_mr                  ? 
_pdbx_database_status.entry_id                        9HQ9 
_pdbx_database_status.recvd_initial_deposition_date   2024-12-16 
_pdbx_database_status.SG_entry                        N 
_pdbx_database_status.deposit_site                    PDBE 
_pdbx_database_status.process_site                    PDBE 
_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           N 
# 
_pdbx_contact_author.id                 2 
_pdbx_contact_author.email              filippo.prischi@kcl.ac.uk 
_pdbx_contact_author.name_first         Filippo 
_pdbx_contact_author.name_last          Prischi 
_pdbx_contact_author.name_mi            ? 
_pdbx_contact_author.role               'principal investigator/group leader' 
_pdbx_contact_author.identifier_ORCID   0000-0003-2107-938X 
# 
loop_
_audit_author.name 
_audit_author.pdbx_ordinal 
_audit_author.identifier_ORCID 
'Dunnett, L.' 1 0000-0001-6710-6959 
'Prischi, F.' 2 0000-0003-2107-938X 
# 
loop_
_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 
_citation.database_id_Medline 
_citation.details 
_citation.id 
_citation.journal_abbrev 
_citation.journal_id_ASTM 
_citation.journal_id_CSD 
_citation.journal_id_ISSN 
_citation.journal_full 
_citation.journal_issue 
_citation.journal_volume 
_citation.language 
_citation.page_first 
_citation.page_last 
_citation.title 
_citation.year 
_citation.database_id_CSD 
_citation.pdbx_database_id_DOI 
_citation.pdbx_database_id_PubMed 
_citation.pdbx_database_id_patent 
_citation.unpublished_flag 
? ? ? ? ? ? ? US ? ? primary J.Biol.Chem. JBCHA3 0071 1083-351X ? ? 301 ? 108335 108335 
'Enhanced identification of small molecules binding to hnRNPA1 via cryptic pockets mapping coupled with X-ray fragment screening.' 
2025 ? 10.1016/j.jbc.2025.108335 39984046 ? ? 
? ? ? ? ? ? ? US ? ? 1       Biorxiv      ?      ?    2692-8205 ? ? ?   ? ?      ?      
'Enhanced identification of small molecules binding to hnRNPA1 via cryptic pockets mapping coupled with X-Ray fragment screening.' 
2024 ? 10.1101/2024.12.17.628909 39763864 ? ? 
# 
loop_
_citation_author.citation_id 
_citation_author.name 
_citation_author.ordinal 
_citation_author.identifier_ORCID 
primary 'Dunnett, L.'  1 ?                   
primary 'Das, S.'      2 ?                   
primary 'Venditti, V.' 3 ?                   
primary 'Prischi, F.'  4 ?                   
1       'Dunnett, L.'  5 0000-0001-6710-6959 
1       'Das, S.'      6 ?                   
1       'Venditti, V.' 7 0000-0001-8734-0400 
1       'Prischi, F.'  8 0000-0003-2107-938X 
# 
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 'Heterogeneous nuclear ribonucleoprotein A1, N-terminally processed' 22357.109 1   ? ? ? ? 
2 non-polymer syn '(5~{R})-7-pyrazin-2-yl-2-oxa-7-azaspiro[4.4]nonane'                 205.256   1   ? ? ? ? 
3 water       nat water                                                                18.015    218 ? ? ? ? 
# 
_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       
;GPMGSKSESPKEPEQLRKLFIGGLSFETTDESLRSHFEQWGTLTDCVVMRDPNTKRSRGFGFVTYATVEEVDAAMNARPH
KVDGRVVEPKRAVSREDSQRPGAHLTVKKIFVGGIKEDTEEHHLRDYFEQYGKIEVIEIMTDRGSGKKRGFAFVTFDDHD
SVDKIVIQKYHTVNGHNCEVRKALSKQEMASASSSQRG
;
_entity_poly.pdbx_seq_one_letter_code_can   
;GPMGSKSESPKEPEQLRKLFIGGLSFETTDESLRSHFEQWGTLTDCVVMRDPNTKRSRGFGFVTYATVEEVDAAMNARPH
KVDGRVVEPKRAVSREDSQRPGAHLTVKKIFVGGIKEDTEEHHLRDYFEQYGKIEVIEIMTDRGSGKKRGFAFVTFDDHD
SVDKIVIQKYHTVNGHNCEVRKALSKQEMASASSSQRG
;
_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 '(5~{R})-7-pyrazin-2-yl-2-oxa-7-azaspiro[4.4]nonane' A1H97 
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   MET n 
1 4   GLY n 
1 5   SER n 
1 6   LYS n 
1 7   SER n 
1 8   GLU n 
1 9   SER n 
1 10  PRO n 
1 11  LYS n 
1 12  GLU n 
1 13  PRO n 
1 14  GLU n 
1 15  GLN n 
1 16  LEU n 
1 17  ARG n 
1 18  LYS n 
1 19  LEU n 
1 20  PHE n 
1 21  ILE n 
1 22  GLY n 
1 23  GLY n 
1 24  LEU n 
1 25  SER n 
1 26  PHE n 
1 27  GLU n 
1 28  THR n 
1 29  THR n 
1 30  ASP n 
1 31  GLU n 
1 32  SER n 
1 33  LEU n 
1 34  ARG n 
1 35  SER n 
1 36  HIS n 
1 37  PHE n 
1 38  GLU n 
1 39  GLN n 
1 40  TRP n 
1 41  GLY n 
1 42  THR n 
1 43  LEU n 
1 44  THR n 
1 45  ASP n 
1 46  CYS n 
1 47  VAL n 
1 48  VAL n 
1 49  MET n 
1 50  ARG n 
1 51  ASP n 
1 52  PRO n 
1 53  ASN n 
1 54  THR n 
1 55  LYS n 
1 56  ARG n 
1 57  SER n 
1 58  ARG n 
1 59  GLY n 
1 60  PHE n 
1 61  GLY n 
1 62  PHE n 
1 63  VAL n 
1 64  THR n 
1 65  TYR n 
1 66  ALA n 
1 67  THR n 
1 68  VAL n 
1 69  GLU n 
1 70  GLU n 
1 71  VAL n 
1 72  ASP n 
1 73  ALA n 
1 74  ALA n 
1 75  MET n 
1 76  ASN n 
1 77  ALA n 
1 78  ARG n 
1 79  PRO n 
1 80  HIS n 
1 81  LYS n 
1 82  VAL n 
1 83  ASP n 
1 84  GLY n 
1 85  ARG n 
1 86  VAL n 
1 87  VAL n 
1 88  GLU n 
1 89  PRO n 
1 90  LYS n 
1 91  ARG n 
1 92  ALA n 
1 93  VAL n 
1 94  SER n 
1 95  ARG n 
1 96  GLU n 
1 97  ASP n 
1 98  SER n 
1 99  GLN n 
1 100 ARG n 
1 101 PRO n 
1 102 GLY n 
1 103 ALA n 
1 104 HIS n 
1 105 LEU n 
1 106 THR n 
1 107 VAL n 
1 108 LYS n 
1 109 LYS n 
1 110 ILE n 
1 111 PHE n 
1 112 VAL n 
1 113 GLY n 
1 114 GLY n 
1 115 ILE n 
1 116 LYS n 
1 117 GLU n 
1 118 ASP n 
1 119 THR n 
1 120 GLU n 
1 121 GLU n 
1 122 HIS n 
1 123 HIS n 
1 124 LEU n 
1 125 ARG n 
1 126 ASP n 
1 127 TYR n 
1 128 PHE n 
1 129 GLU n 
1 130 GLN n 
1 131 TYR n 
1 132 GLY n 
1 133 LYS n 
1 134 ILE n 
1 135 GLU n 
1 136 VAL n 
1 137 ILE n 
1 138 GLU n 
1 139 ILE n 
1 140 MET n 
1 141 THR n 
1 142 ASP n 
1 143 ARG n 
1 144 GLY n 
1 145 SER n 
1 146 GLY n 
1 147 LYS n 
1 148 LYS n 
1 149 ARG n 
1 150 GLY n 
1 151 PHE n 
1 152 ALA n 
1 153 PHE n 
1 154 VAL n 
1 155 THR n 
1 156 PHE n 
1 157 ASP n 
1 158 ASP n 
1 159 HIS n 
1 160 ASP n 
1 161 SER n 
1 162 VAL n 
1 163 ASP n 
1 164 LYS n 
1 165 ILE n 
1 166 VAL n 
1 167 ILE n 
1 168 GLN n 
1 169 LYS n 
1 170 TYR n 
1 171 HIS n 
1 172 THR n 
1 173 VAL n 
1 174 ASN n 
1 175 GLY n 
1 176 HIS n 
1 177 ASN n 
1 178 CYS n 
1 179 GLU n 
1 180 VAL n 
1 181 ARG n 
1 182 LYS n 
1 183 ALA n 
1 184 LEU n 
1 185 SER n 
1 186 LYS n 
1 187 GLN n 
1 188 GLU n 
1 189 MET n 
1 190 ALA n 
1 191 SER n 
1 192 ALA n 
1 193 SER n 
1 194 SER n 
1 195 SER n 
1 196 GLN n 
1 197 ARG n 
1 198 GLY 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                   198 
_entity_src_gen.gene_src_common_name               human 
_entity_src_gen.gene_src_genus                     ? 
_entity_src_gen.pdbx_gene_src_gene                 'HNRNPA1, HNRPA1' 
_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      'Homo sapiens' 
_entity_src_gen.pdbx_gene_src_ncbi_taxonomy_id     9606 
_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(DE3)' 
_entity_src_gen.pdbx_host_org_ncbi_taxonomy_id     469008 
_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          pETM-14 
_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 
A1H97 non-polymer         . '(5~{R})-7-pyrazin-2-yl-2-oxa-7-azaspiro[4.4]nonane' ? 'C11 H15 N3 O'   205.256 
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 
TRP   'L-peptide linking' y TRYPTOPHAN                                           ? 'C11 H12 N2 O2'  204.225 
TYR   'L-peptide linking' y TYROSINE                                             ? 'C9 H11 N O3'    181.189 
VAL   'L-peptide linking' y VALINE                                               ? 'C5 H11 N O2'    117.146 
# 
loop_
_pdbx_poly_seq_scheme.asym_id 
_pdbx_poly_seq_scheme.entity_id 
_pdbx_poly_seq_scheme.seq_id 
_pdbx_poly_seq_scheme.mon_id 
_pdbx_poly_seq_scheme.ndb_seq_num 
_pdbx_poly_seq_scheme.pdb_seq_num 
_pdbx_poly_seq_scheme.auth_seq_num 
_pdbx_poly_seq_scheme.pdb_mon_id 
_pdbx_poly_seq_scheme.auth_mon_id 
_pdbx_poly_seq_scheme.pdb_strand_id 
_pdbx_poly_seq_scheme.pdb_ins_code 
_pdbx_poly_seq_scheme.hetero 
A 1 1   GLY 1   -2  ?   ?   ?   A . n 
A 1 2   PRO 2   -1  ?   ?   ?   A . n 
A 1 3   MET 3   0   ?   ?   ?   A . n 
A 1 4   GLY 4   1   ?   ?   ?   A . n 
A 1 5   SER 5   2   ?   ?   ?   A . n 
A 1 6   LYS 6   3   ?   ?   ?   A . n 
A 1 7   SER 7   4   ?   ?   ?   A . n 
A 1 8   GLU 8   5   ?   ?   ?   A . n 
A 1 9   SER 9   6   ?   ?   ?   A . n 
A 1 10  PRO 10  7   7   PRO PRO A . n 
A 1 11  LYS 11  8   8   LYS LYS A . n 
A 1 12  GLU 12  9   9   GLU GLU A . n 
A 1 13  PRO 13  10  10  PRO PRO A . n 
A 1 14  GLU 14  11  11  GLU GLU A . n 
A 1 15  GLN 15  12  12  GLN GLN A . n 
A 1 16  LEU 16  13  13  LEU LEU A . n 
A 1 17  ARG 17  14  14  ARG ARG A . n 
A 1 18  LYS 18  15  15  LYS LYS A . n 
A 1 19  LEU 19  16  16  LEU LEU A . n 
A 1 20  PHE 20  17  17  PHE PHE A . n 
A 1 21  ILE 21  18  18  ILE ILE A . n 
A 1 22  GLY 22  19  19  GLY GLY A . n 
A 1 23  GLY 23  20  20  GLY GLY A . n 
A 1 24  LEU 24  21  21  LEU LEU A . n 
A 1 25  SER 25  22  22  SER SER A . n 
A 1 26  PHE 26  23  23  PHE PHE A . n 
A 1 27  GLU 27  24  24  GLU GLU A . n 
A 1 28  THR 28  25  25  THR THR A . n 
A 1 29  THR 29  26  26  THR THR A . n 
A 1 30  ASP 30  27  27  ASP ASP A . n 
A 1 31  GLU 31  28  28  GLU GLU A . n 
A 1 32  SER 32  29  29  SER SER A . n 
A 1 33  LEU 33  30  30  LEU LEU A . n 
A 1 34  ARG 34  31  31  ARG ARG A . n 
A 1 35  SER 35  32  32  SER SER A . n 
A 1 36  HIS 36  33  33  HIS HIS A . n 
A 1 37  PHE 37  34  34  PHE PHE A . n 
A 1 38  GLU 38  35  35  GLU GLU A . n 
A 1 39  GLN 39  36  36  GLN GLN A . n 
A 1 40  TRP 40  37  37  TRP TRP A . n 
A 1 41  GLY 41  38  38  GLY GLY A . n 
A 1 42  THR 42  39  39  THR THR A . n 
A 1 43  LEU 43  40  40  LEU LEU A . n 
A 1 44  THR 44  41  41  THR THR A . n 
A 1 45  ASP 45  42  42  ASP ASP A . n 
A 1 46  CYS 46  43  43  CYS CYS A . n 
A 1 47  VAL 47  44  44  VAL VAL A . n 
A 1 48  VAL 48  45  45  VAL VAL A . n 
A 1 49  MET 49  46  46  MET MET A . n 
A 1 50  ARG 50  47  47  ARG ARG A . n 
A 1 51  ASP 51  48  48  ASP ASP A . n 
A 1 52  PRO 52  49  49  PRO PRO A . n 
A 1 53  ASN 53  50  50  ASN ASN A . n 
A 1 54  THR 54  51  51  THR THR A . n 
A 1 55  LYS 55  52  52  LYS LYS A . n 
A 1 56  ARG 56  53  53  ARG ARG A . n 
A 1 57  SER 57  54  54  SER SER A . n 
A 1 58  ARG 58  55  55  ARG ARG A . n 
A 1 59  GLY 59  56  56  GLY GLY A . n 
A 1 60  PHE 60  57  57  PHE PHE A . n 
A 1 61  GLY 61  58  58  GLY GLY A . n 
A 1 62  PHE 62  59  59  PHE PHE A . n 
A 1 63  VAL 63  60  60  VAL VAL A . n 
A 1 64  THR 64  61  61  THR THR A . n 
A 1 65  TYR 65  62  62  TYR TYR A . n 
A 1 66  ALA 66  63  63  ALA ALA A . n 
A 1 67  THR 67  64  64  THR THR A . n 
A 1 68  VAL 68  65  65  VAL VAL A . n 
A 1 69  GLU 69  66  66  GLU GLU A . n 
A 1 70  GLU 70  67  67  GLU GLU A . n 
A 1 71  VAL 71  68  68  VAL VAL A . n 
A 1 72  ASP 72  69  69  ASP ASP A . n 
A 1 73  ALA 73  70  70  ALA ALA A . n 
A 1 74  ALA 74  71  71  ALA ALA A . n 
A 1 75  MET 75  72  72  MET MET A . n 
A 1 76  ASN 76  73  73  ASN ASN A . n 
A 1 77  ALA 77  74  74  ALA ALA A . n 
A 1 78  ARG 78  75  75  ARG ARG A . n 
A 1 79  PRO 79  76  76  PRO PRO A . n 
A 1 80  HIS 80  77  77  HIS HIS A . n 
A 1 81  LYS 81  78  78  LYS LYS A . n 
A 1 82  VAL 82  79  79  VAL VAL A . n 
A 1 83  ASP 83  80  80  ASP ASP A . n 
A 1 84  GLY 84  81  81  GLY GLY A . n 
A 1 85  ARG 85  82  82  ARG ARG A . n 
A 1 86  VAL 86  83  83  VAL VAL A . n 
A 1 87  VAL 87  84  84  VAL VAL A . n 
A 1 88  GLU 88  85  85  GLU GLU A . n 
A 1 89  PRO 89  86  86  PRO PRO A . n 
A 1 90  LYS 90  87  87  LYS LYS A . n 
A 1 91  ARG 91  88  88  ARG ARG A . n 
A 1 92  ALA 92  89  89  ALA ALA A . n 
A 1 93  VAL 93  90  90  VAL VAL A . n 
A 1 94  SER 94  91  91  SER SER A . n 
A 1 95  ARG 95  92  ?   ?   ?   A . n 
A 1 96  GLU 96  93  ?   ?   ?   A . n 
A 1 97  ASP 97  94  ?   ?   ?   A . n 
A 1 98  SER 98  95  ?   ?   ?   A . n 
A 1 99  GLN 99  96  ?   ?   ?   A . n 
A 1 100 ARG 100 97  ?   ?   ?   A . n 
A 1 101 PRO 101 98  ?   ?   ?   A . n 
A 1 102 GLY 102 99  ?   ?   ?   A . n 
A 1 103 ALA 103 100 ?   ?   ?   A . n 
A 1 104 HIS 104 101 101 HIS HIS A . n 
A 1 105 LEU 105 102 102 LEU LEU A . n 
A 1 106 THR 106 103 103 THR THR A . n 
A 1 107 VAL 107 104 104 VAL VAL A . n 
A 1 108 LYS 108 105 105 LYS LYS A . n 
A 1 109 LYS 109 106 106 LYS LYS A . n 
A 1 110 ILE 110 107 107 ILE ILE A . n 
A 1 111 PHE 111 108 108 PHE PHE A . n 
A 1 112 VAL 112 109 109 VAL VAL A . n 
A 1 113 GLY 113 110 110 GLY GLY A . n 
A 1 114 GLY 114 111 111 GLY GLY A . n 
A 1 115 ILE 115 112 112 ILE ILE A . n 
A 1 116 LYS 116 113 113 LYS LYS A . n 
A 1 117 GLU 117 114 114 GLU GLU A . n 
A 1 118 ASP 118 115 115 ASP ASP A . n 
A 1 119 THR 119 116 116 THR THR A . n 
A 1 120 GLU 120 117 117 GLU GLU A . n 
A 1 121 GLU 121 118 118 GLU GLU A . n 
A 1 122 HIS 122 119 119 HIS HIS A . n 
A 1 123 HIS 123 120 120 HIS HIS A . n 
A 1 124 LEU 124 121 121 LEU LEU A . n 
A 1 125 ARG 125 122 122 ARG ARG A . n 
A 1 126 ASP 126 123 123 ASP ASP A . n 
A 1 127 TYR 127 124 124 TYR TYR A . n 
A 1 128 PHE 128 125 125 PHE PHE A . n 
A 1 129 GLU 129 126 126 GLU GLU A . n 
A 1 130 GLN 130 127 127 GLN GLN A . n 
A 1 131 TYR 131 128 128 TYR TYR A . n 
A 1 132 GLY 132 129 129 GLY GLY A . n 
A 1 133 LYS 133 130 130 LYS LYS A . n 
A 1 134 ILE 134 131 131 ILE ILE A . n 
A 1 135 GLU 135 132 132 GLU GLU A . n 
A 1 136 VAL 136 133 133 VAL VAL A . n 
A 1 137 ILE 137 134 134 ILE ILE A . n 
A 1 138 GLU 138 135 135 GLU GLU A . n 
A 1 139 ILE 139 136 136 ILE ILE A . n 
A 1 140 MET 140 137 137 MET MET A . n 
A 1 141 THR 141 138 138 THR THR A . n 
A 1 142 ASP 142 139 139 ASP ASP A . n 
A 1 143 ARG 143 140 140 ARG ARG A . n 
A 1 144 GLY 144 141 141 GLY GLY A . n 
A 1 145 SER 145 142 142 SER SER A . n 
A 1 146 GLY 146 143 143 GLY GLY A . n 
A 1 147 LYS 147 144 144 LYS LYS A . n 
A 1 148 LYS 148 145 145 LYS LYS A . n 
A 1 149 ARG 149 146 146 ARG ARG A . n 
A 1 150 GLY 150 147 147 GLY GLY A . n 
A 1 151 PHE 151 148 148 PHE PHE A . n 
A 1 152 ALA 152 149 149 ALA ALA A . n 
A 1 153 PHE 153 150 150 PHE PHE A . n 
A 1 154 VAL 154 151 151 VAL VAL A . n 
A 1 155 THR 155 152 152 THR THR A . n 
A 1 156 PHE 156 153 153 PHE PHE A . n 
A 1 157 ASP 157 154 154 ASP ASP A . n 
A 1 158 ASP 158 155 155 ASP ASP A . n 
A 1 159 HIS 159 156 156 HIS HIS A . n 
A 1 160 ASP 160 157 157 ASP ASP A . n 
A 1 161 SER 161 158 158 SER SER A . n 
A 1 162 VAL 162 159 159 VAL VAL A . n 
A 1 163 ASP 163 160 160 ASP ASP A . n 
A 1 164 LYS 164 161 161 LYS LYS A . n 
A 1 165 ILE 165 162 162 ILE ILE A . n 
A 1 166 VAL 166 163 163 VAL VAL A . n 
A 1 167 ILE 167 164 164 ILE ILE A . n 
A 1 168 GLN 168 165 165 GLN GLN A . n 
A 1 169 LYS 169 166 166 LYS LYS A . n 
A 1 170 TYR 170 167 167 TYR TYR A . n 
A 1 171 HIS 171 168 168 HIS HIS A . n 
A 1 172 THR 172 169 169 THR THR A . n 
A 1 173 VAL 173 170 170 VAL VAL A . n 
A 1 174 ASN 174 171 171 ASN ASN A . n 
A 1 175 GLY 175 172 172 GLY GLY A . n 
A 1 176 HIS 176 173 173 HIS HIS A . n 
A 1 177 ASN 177 174 174 ASN ASN A . n 
A 1 178 CYS 178 175 175 CYS CYS A . n 
A 1 179 GLU 179 176 176 GLU GLU A . n 
A 1 180 VAL 180 177 177 VAL VAL A . n 
A 1 181 ARG 181 178 178 ARG ARG A . n 
A 1 182 LYS 182 179 179 LYS LYS A . n 
A 1 183 ALA 183 180 180 ALA ALA A . n 
A 1 184 LEU 184 181 181 LEU LEU A . n 
A 1 185 SER 185 182 182 SER SER A . n 
A 1 186 LYS 186 183 ?   ?   ?   A . n 
A 1 187 GLN 187 184 ?   ?   ?   A . n 
A 1 188 GLU 188 185 ?   ?   ?   A . n 
A 1 189 MET 189 186 ?   ?   ?   A . n 
A 1 190 ALA 190 187 ?   ?   ?   A . n 
A 1 191 SER 191 188 ?   ?   ?   A . n 
A 1 192 ALA 192 189 ?   ?   ?   A . n 
A 1 193 SER 193 190 ?   ?   ?   A . n 
A 1 194 SER 194 191 ?   ?   ?   A . n 
A 1 195 SER 195 192 ?   ?   ?   A . n 
A 1 196 GLN 196 193 ?   ?   ?   A . n 
A 1 197 ARG 197 194 ?   ?   ?   A . n 
A 1 198 GLY 198 195 ?   ?   ?   A . n 
# 
_pdbx_entity_instance_feature.ordinal        1 
_pdbx_entity_instance_feature.comp_id        A1H97 
_pdbx_entity_instance_feature.asym_id        ? 
_pdbx_entity_instance_feature.seq_num        ? 
_pdbx_entity_instance_feature.auth_comp_id   A1H97 
_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 A1H97 1   201 201 A1H97 LIG A . 
C 3 HOH   1   301 171 HOH   HOH A . 
C 3 HOH   2   302 93  HOH   HOH A . 
C 3 HOH   3   303 92  HOH   HOH A . 
C 3 HOH   4   304 68  HOH   HOH A . 
C 3 HOH   5   305 91  HOH   HOH A . 
C 3 HOH   6   306 69  HOH   HOH A . 
C 3 HOH   7   307 184 HOH   HOH A . 
C 3 HOH   8   308 165 HOH   HOH A . 
C 3 HOH   9   309 108 HOH   HOH A . 
C 3 HOH   10  310 194 HOH   HOH A . 
C 3 HOH   11  311 187 HOH   HOH A . 
C 3 HOH   12  312 34  HOH   HOH A . 
C 3 HOH   13  313 13  HOH   HOH A . 
C 3 HOH   14  314 74  HOH   HOH A . 
C 3 HOH   15  315 131 HOH   HOH A . 
C 3 HOH   16  316 183 HOH   HOH A . 
C 3 HOH   17  317 48  HOH   HOH A . 
C 3 HOH   18  318 106 HOH   HOH A . 
C 3 HOH   19  319 120 HOH   HOH A . 
C 3 HOH   20  320 205 HOH   HOH A . 
C 3 HOH   21  321 25  HOH   HOH A . 
C 3 HOH   22  322 118 HOH   HOH A . 
C 3 HOH   23  323 22  HOH   HOH A . 
C 3 HOH   24  324 99  HOH   HOH A . 
C 3 HOH   25  325 98  HOH   HOH A . 
C 3 HOH   26  326 31  HOH   HOH A . 
C 3 HOH   27  327 163 HOH   HOH A . 
C 3 HOH   28  328 148 HOH   HOH A . 
C 3 HOH   29  329 77  HOH   HOH A . 
C 3 HOH   30  330 4   HOH   HOH A . 
C 3 HOH   31  331 138 HOH   HOH A . 
C 3 HOH   32  332 2   HOH   HOH A . 
C 3 HOH   33  333 6   HOH   HOH A . 
C 3 HOH   34  334 5   HOH   HOH A . 
C 3 HOH   35  335 115 HOH   HOH A . 
C 3 HOH   36  336 162 HOH   HOH A . 
C 3 HOH   37  337 53  HOH   HOH A . 
C 3 HOH   38  338 3   HOH   HOH A . 
C 3 HOH   39  339 122 HOH   HOH A . 
C 3 HOH   40  340 112 HOH   HOH A . 
C 3 HOH   41  341 47  HOH   HOH A . 
C 3 HOH   42  342 70  HOH   HOH A . 
C 3 HOH   43  343 9   HOH   HOH A . 
C 3 HOH   44  344 37  HOH   HOH A . 
C 3 HOH   45  345 102 HOH   HOH A . 
C 3 HOH   46  346 42  HOH   HOH A . 
C 3 HOH   47  347 19  HOH   HOH A . 
C 3 HOH   48  348 11  HOH   HOH A . 
C 3 HOH   49  349 204 HOH   HOH A . 
C 3 HOH   50  350 46  HOH   HOH A . 
C 3 HOH   51  351 7   HOH   HOH A . 
C 3 HOH   52  352 27  HOH   HOH A . 
C 3 HOH   53  353 95  HOH   HOH A . 
C 3 HOH   54  354 193 HOH   HOH A . 
C 3 HOH   55  355 60  HOH   HOH A . 
C 3 HOH   56  356 192 HOH   HOH A . 
C 3 HOH   57  357 189 HOH   HOH A . 
C 3 HOH   58  358 49  HOH   HOH A . 
C 3 HOH   59  359 44  HOH   HOH A . 
C 3 HOH   60  360 158 HOH   HOH A . 
C 3 HOH   61  361 35  HOH   HOH A . 
C 3 HOH   62  362 16  HOH   HOH A . 
C 3 HOH   63  363 43  HOH   HOH A . 
C 3 HOH   64  364 36  HOH   HOH A . 
C 3 HOH   65  365 1   HOH   HOH A . 
C 3 HOH   66  366 103 HOH   HOH A . 
C 3 HOH   67  367 72  HOH   HOH A . 
C 3 HOH   68  368 17  HOH   HOH A . 
C 3 HOH   69  369 30  HOH   HOH A . 
C 3 HOH   70  370 197 HOH   HOH A . 
C 3 HOH   71  371 38  HOH   HOH A . 
C 3 HOH   72  372 8   HOH   HOH A . 
C 3 HOH   73  373 20  HOH   HOH A . 
C 3 HOH   74  374 55  HOH   HOH A . 
C 3 HOH   75  375 164 HOH   HOH A . 
C 3 HOH   76  376 39  HOH   HOH A . 
C 3 HOH   77  377 12  HOH   HOH A . 
C 3 HOH   78  378 201 HOH   HOH A . 
C 3 HOH   79  379 157 HOH   HOH A . 
C 3 HOH   80  380 81  HOH   HOH A . 
C 3 HOH   81  381 32  HOH   HOH A . 
C 3 HOH   82  382 167 HOH   HOH A . 
C 3 HOH   83  383 172 HOH   HOH A . 
C 3 HOH   84  384 75  HOH   HOH A . 
C 3 HOH   85  385 14  HOH   HOH A . 
C 3 HOH   86  386 57  HOH   HOH A . 
C 3 HOH   87  387 156 HOH   HOH A . 
C 3 HOH   88  388 78  HOH   HOH A . 
C 3 HOH   89  389 130 HOH   HOH A . 
C 3 HOH   90  390 24  HOH   HOH A . 
C 3 HOH   91  391 196 HOH   HOH A . 
C 3 HOH   92  392 56  HOH   HOH A . 
C 3 HOH   93  393 97  HOH   HOH A . 
C 3 HOH   94  394 88  HOH   HOH A . 
C 3 HOH   95  395 116 HOH   HOH A . 
C 3 HOH   96  396 127 HOH   HOH A . 
C 3 HOH   97  397 149 HOH   HOH A . 
C 3 HOH   98  398 85  HOH   HOH A . 
C 3 HOH   99  399 66  HOH   HOH A . 
C 3 HOH   100 400 64  HOH   HOH A . 
C 3 HOH   101 401 58  HOH   HOH A . 
C 3 HOH   102 402 40  HOH   HOH A . 
C 3 HOH   103 403 207 HOH   HOH A . 
C 3 HOH   104 404 26  HOH   HOH A . 
C 3 HOH   105 405 89  HOH   HOH A . 
C 3 HOH   106 406 10  HOH   HOH A . 
C 3 HOH   107 407 166 HOH   HOH A . 
C 3 HOH   108 408 76  HOH   HOH A . 
C 3 HOH   109 409 33  HOH   HOH A . 
C 3 HOH   110 410 80  HOH   HOH A . 
C 3 HOH   111 411 41  HOH   HOH A . 
C 3 HOH   112 412 161 HOH   HOH A . 
C 3 HOH   113 413 28  HOH   HOH A . 
C 3 HOH   114 414 45  HOH   HOH A . 
C 3 HOH   115 415 73  HOH   HOH A . 
C 3 HOH   116 416 51  HOH   HOH A . 
C 3 HOH   117 417 155 HOH   HOH A . 
C 3 HOH   118 418 54  HOH   HOH A . 
C 3 HOH   119 419 126 HOH   HOH A . 
C 3 HOH   120 420 84  HOH   HOH A . 
C 3 HOH   121 421 206 HOH   HOH A . 
C 3 HOH   122 422 15  HOH   HOH A . 
C 3 HOH   123 423 83  HOH   HOH A . 
C 3 HOH   124 424 59  HOH   HOH A . 
C 3 HOH   125 425 177 HOH   HOH A . 
C 3 HOH   126 426 96  HOH   HOH A . 
C 3 HOH   127 427 159 HOH   HOH A . 
C 3 HOH   128 428 170 HOH   HOH A . 
C 3 HOH   129 429 216 HOH   HOH A . 
C 3 HOH   130 430 119 HOH   HOH A . 
C 3 HOH   131 431 198 HOH   HOH A . 
C 3 HOH   132 432 109 HOH   HOH A . 
C 3 HOH   133 433 63  HOH   HOH A . 
C 3 HOH   134 434 62  HOH   HOH A . 
C 3 HOH   135 435 52  HOH   HOH A . 
C 3 HOH   136 436 123 HOH   HOH A . 
C 3 HOH   137 437 87  HOH   HOH A . 
C 3 HOH   138 438 134 HOH   HOH A . 
C 3 HOH   139 439 61  HOH   HOH A . 
C 3 HOH   140 440 82  HOH   HOH A . 
C 3 HOH   141 441 147 HOH   HOH A . 
C 3 HOH   142 442 21  HOH   HOH A . 
C 3 HOH   143 443 133 HOH   HOH A . 
C 3 HOH   144 444 129 HOH   HOH A . 
C 3 HOH   145 445 113 HOH   HOH A . 
C 3 HOH   146 446 29  HOH   HOH A . 
C 3 HOH   147 447 175 HOH   HOH A . 
C 3 HOH   148 448 50  HOH   HOH A . 
C 3 HOH   149 449 18  HOH   HOH A . 
C 3 HOH   150 450 124 HOH   HOH A . 
C 3 HOH   151 451 140 HOH   HOH A . 
C 3 HOH   152 452 180 HOH   HOH A . 
C 3 HOH   153 453 86  HOH   HOH A . 
C 3 HOH   154 454 101 HOH   HOH A . 
C 3 HOH   155 455 114 HOH   HOH A . 
C 3 HOH   156 456 117 HOH   HOH A . 
C 3 HOH   157 457 212 HOH   HOH A . 
C 3 HOH   158 458 152 HOH   HOH A . 
C 3 HOH   159 459 208 HOH   HOH A . 
C 3 HOH   160 460 107 HOH   HOH A . 
C 3 HOH   161 461 173 HOH   HOH A . 
C 3 HOH   162 462 132 HOH   HOH A . 
C 3 HOH   163 463 142 HOH   HOH A . 
C 3 HOH   164 464 136 HOH   HOH A . 
C 3 HOH   165 465 65  HOH   HOH A . 
C 3 HOH   166 466 200 HOH   HOH A . 
C 3 HOH   167 467 128 HOH   HOH A . 
C 3 HOH   168 468 176 HOH   HOH A . 
C 3 HOH   169 469 168 HOH   HOH A . 
C 3 HOH   170 470 181 HOH   HOH A . 
C 3 HOH   171 471 186 HOH   HOH A . 
C 3 HOH   172 472 190 HOH   HOH A . 
C 3 HOH   173 473 67  HOH   HOH A . 
C 3 HOH   174 474 151 HOH   HOH A . 
C 3 HOH   175 475 94  HOH   HOH A . 
C 3 HOH   176 476 135 HOH   HOH A . 
C 3 HOH   177 477 211 HOH   HOH A . 
C 3 HOH   178 478 217 HOH   HOH A . 
C 3 HOH   179 479 191 HOH   HOH A . 
C 3 HOH   180 480 185 HOH   HOH A . 
C 3 HOH   181 481 195 HOH   HOH A . 
C 3 HOH   182 482 160 HOH   HOH A . 
C 3 HOH   183 483 150 HOH   HOH A . 
C 3 HOH   184 484 182 HOH   HOH A . 
C 3 HOH   185 485 23  HOH   HOH A . 
C 3 HOH   186 486 146 HOH   HOH A . 
C 3 HOH   187 487 139 HOH   HOH A . 
C 3 HOH   188 488 90  HOH   HOH A . 
C 3 HOH   189 489 143 HOH   HOH A . 
C 3 HOH   190 490 178 HOH   HOH A . 
C 3 HOH   191 491 71  HOH   HOH A . 
C 3 HOH   192 492 199 HOH   HOH A . 
C 3 HOH   193 493 110 HOH   HOH A . 
C 3 HOH   194 494 203 HOH   HOH A . 
C 3 HOH   195 495 137 HOH   HOH A . 
C 3 HOH   196 496 169 HOH   HOH A . 
C 3 HOH   197 497 174 HOH   HOH A . 
C 3 HOH   198 498 179 HOH   HOH A . 
C 3 HOH   199 499 144 HOH   HOH A . 
C 3 HOH   200 500 121 HOH   HOH A . 
C 3 HOH   201 501 153 HOH   HOH A . 
C 3 HOH   202 502 79  HOH   HOH A . 
C 3 HOH   203 503 105 HOH   HOH A . 
C 3 HOH   204 504 100 HOH   HOH A . 
C 3 HOH   205 505 214 HOH   HOH A . 
C 3 HOH   206 506 125 HOH   HOH A . 
C 3 HOH   207 507 218 HOH   HOH A . 
C 3 HOH   208 508 141 HOH   HOH A . 
C 3 HOH   209 509 111 HOH   HOH A . 
C 3 HOH   210 510 188 HOH   HOH A . 
C 3 HOH   211 511 154 HOH   HOH A . 
C 3 HOH   212 512 104 HOH   HOH A . 
C 3 HOH   213 513 202 HOH   HOH A . 
C 3 HOH   214 514 213 HOH   HOH A . 
C 3 HOH   215 515 209 HOH   HOH A . 
C 3 HOH   216 516 145 HOH   HOH A . 
C 3 HOH   217 517 215 HOH   HOH A . 
C 3 HOH   218 518 210 HOH   HOH A . 
# 
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 
? 'data reduction' ? ? ? ? ? ? ? ? ? ? ? xia2    ? ? ? .           2 
? 'data scaling'   ? ? ? ? ? ? ? ? ? ? ? Aimless ? ? ? .           3 
? phasing          ? ? ? ? ? ? ? ? ? ? ? PHASER  ? ? ? .           4 
# 
_cell.angle_alpha                  90.000 
_cell.angle_alpha_esd              ? 
_cell.angle_beta                   94.170 
_cell.angle_beta_esd               ? 
_cell.angle_gamma                  90.000 
_cell.angle_gamma_esd              ? 
_cell.entry_id                     9HQ9 
_cell.details                      ? 
_cell.formula_units_Z              ? 
_cell.length_a                     37.994 
_cell.length_a_esd                 ? 
_cell.length_b                     44.090 
_cell.length_b_esd                 ? 
_cell.length_c                     55.983 
_cell.length_c_esd                 ? 
_cell.volume                       93531.963 
_cell.volume_esd                   ? 
_cell.Z_PDB                        2 
_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                         9HQ9 
_symmetry.cell_setting                     ? 
_symmetry.Int_Tables_number                4 
_symmetry.space_group_name_Hall            'P 2yb' 
_symmetry.space_group_name_H-M             'P 1 21 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                   9HQ9 
_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             2.08 
_exptl_crystal.density_method               ? 
_exptl_crystal.density_percent_sol          40.98 
_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, SITTING DROP' 
_exptl_crystal_grow.method_ref      ? 
_exptl_crystal_grow.pH              8.5 
_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    '0.1 M Tris-HCl, pH 8.50, 25% PEG-4000, 8% 2-Methyl-2,4-pentanediol' 
_exptl_crystal_grow.pdbx_pH_range   ? 
_exptl_crystal_grow.temp            289 
# 
_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 PILATUS 6M-F' 
_diffrn_detector.area_resol_mean              ? 
_diffrn_detector.dtime                        ? 
_diffrn_detector.pdbx_frames_total            ? 
_diffrn_detector.pdbx_collection_time_total   ? 
_diffrn_detector.pdbx_collection_date         2018-06-29 
_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   0.91587 
_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                        'DIAMOND BEAMLINE I04-1' 
_diffrn_source.voltage                     ? 
_diffrn_source.take-off_angle              ? 
_diffrn_source.pdbx_wavelength_list        0.91587 
_diffrn_source.pdbx_wavelength             ? 
_diffrn_source.pdbx_synchrotron_beamline   I04-1 
_diffrn_source.pdbx_synchrotron_site       Diamond 
# 
_reflns.B_iso_Wilson_estimate                          12.30 
_reflns.entry_id                                       9HQ9 
_reflns.data_reduction_details                         ? 
_reflns.data_reduction_method                          ? 
_reflns.d_resolution_high                              1.60 
_reflns.d_resolution_low                               55.84 
_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                                     24516 
_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                           99.8 
_reflns.R_free_details                                 ? 
_reflns.Rmerge_F_all                                   ? 
_reflns.Rmerge_F_obs                                   ? 
_reflns.Friedel_coverage                               ? 
_reflns.number_gt                                      ? 
_reflns.threshold_expression                           ? 
_reflns.pdbx_redundancy                                1.83 
_reflns.pdbx_netI_over_av_sigmaI                       ? 
_reflns.pdbx_netI_over_sigmaI                          11.3 
_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                                   0.998 
_reflns.pdbx_CC_star                                   ? 
_reflns.pdbx_R_split                                   ? 
_reflns.pdbx_Rmerge_I_obs                              0.05 
_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                                    1.60 
_reflns_shell.d_res_low                                     1.63 
_reflns_shell.meanI_over_sigI_all                           ? 
_reflns_shell.meanI_over_sigI_obs                           3.1 
_reflns_shell.number_measured_all                           ? 
_reflns_shell.number_measured_obs                           ? 
_reflns_shell.number_possible                               ? 
_reflns_shell.number_unique_all                             ? 
_reflns_shell.number_unique_obs                             1218 
_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                               ? 
_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                                  0.741 
_reflns_shell.pdbx_CC_star                                  ? 
_reflns_shell.pdbx_R_split                                  ? 
_reflns_shell.percent_possible_all                          ? 
_reflns_shell.Rmerge_I_all                                  ? 
_reflns_shell.Rmerge_I_obs                                  ? 
_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                               16.92 
_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                                 9HQ9 
_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                            1.60 
_refine.ls_d_res_low                             55.84 
_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                     24407 
_refine.ls_number_reflns_R_free                  1266 
_refine.ls_number_reflns_R_work                  23141 
_refine.ls_number_restraints                     ? 
_refine.ls_percent_reflns_obs                    99.37 
_refine.ls_percent_reflns_R_free                 5.19 
_refine.ls_R_factor_all                          ? 
_refine.ls_R_factor_obs                          0.1807 
_refine.ls_R_factor_R_free                       0.2107 
_refine.ls_R_factor_R_free_error                 ? 
_refine.ls_R_factor_R_free_error_details         ? 
_refine.ls_R_factor_R_work                       0.1791 
_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                          1.34 
_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                 21.3945 
_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                            0.1919 
_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                       1.60 
_refine_hist.d_res_low                        55.84 
_refine_hist.number_atoms_solvent             218 
_refine_hist.number_atoms_total               1579 
_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        1346 
_refine_hist.pdbx_number_atoms_nucleic_acid   0 
_refine_hist.pdbx_number_atoms_ligand         15 
_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' ? 0.0079  ? 1420 ? f_bond_d           ? ? 
'X-RAY DIFFRACTION' ? 0.9187  ? 1914 ? f_angle_d          ? ? 
'X-RAY DIFFRACTION' ? 0.0616  ? 203  ? f_chiral_restr     ? ? 
'X-RAY DIFFRACTION' ? 0.0099  ? 248  ? f_plane_restr      ? ? 
'X-RAY DIFFRACTION' ? 15.4908 ? 532  ? 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' 1.60 1.66  . . 144 2516 98.45 . . . . 0.2482 . . . . . . . . . . . 0.3223 
'X-RAY DIFFRACTION' 1.66 1.74  . . 145 2539 98.86 . . . . 0.2227 . . . . . . . . . . . 0.2552 
'X-RAY DIFFRACTION' 1.74 1.83  . . 168 2509 99.07 . . . . 0.2049 . . . . . . . . . . . 0.2385 
'X-RAY DIFFRACTION' 1.83 1.95  . . 147 2541 99.08 . . . . 0.1875 . . . . . . . . . . . 0.2802 
'X-RAY DIFFRACTION' 1.95 2.10  . . 104 2615 99.85 . . . . 0.1617 . . . . . . . . . . . 0.2064 
'X-RAY DIFFRACTION' 2.10 2.31  . . 142 2564 99.52 . . . . 0.1732 . . . . . . . . . . . 0.1975 
'X-RAY DIFFRACTION' 2.31 2.64  . . 110 2617 99.85 . . . . 0.1742 . . . . . . . . . . . 0.1759 
'X-RAY DIFFRACTION' 2.64 3.33  . . 173 2563 99.85 . . . . 0.1726 . . . . . . . . . . . 0.1977 
'X-RAY DIFFRACTION' 3.33 55.84 . . 133 2677 99.79 . . . . 0.1668 . . . . . . . . . . . 0.1892 
# 
_struct.entry_id                     9HQ9 
_struct.title                        'UP1 in complex with Z1401276297' 
_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        9HQ9 
_struct_keywords.text            
'fragment screening, hnRNP A1, UP1, RNA/DNA BINDING PROTEIN, UP1-fragment complex, RNA BINDING PROTEIN' 
_struct_keywords.pdbx_keywords   'RNA BINDING PROTEIN' 
# 
loop_
_struct_asym.id 
_struct_asym.pdbx_blank_PDB_chainid_flag 
_struct_asym.pdbx_modified 
_struct_asym.entity_id 
_struct_asym.details 
A N N 1 ? 
B N N 2 ? 
C N N 3 ? 
# 
_struct_ref.id                         1 
_struct_ref.db_name                    UNP 
_struct_ref.db_code                    ROA1_HUMAN 
_struct_ref.pdbx_db_accession          P09651 
_struct_ref.pdbx_db_isoform            ? 
_struct_ref.entity_id                  1 
_struct_ref.pdbx_seq_one_letter_code   
;SKSESPKEPEQLRKLFIGGLSFETTDESLRSHFEQWGTLTDCVVMRDPNTKRSRGFGFVTYATVEEVDAAMNARPHKVDG
RVVEPKRAVSREDSQRPGAHLTVKKIFVGGIKEDTEEHHLRDYFEQYGKIEVIEIMTDRGSGKKRGFAFVTFDDHDSVDK
IVIQKYHTVNGHNCEVRKALSKQEMASASSSQRG
;
_struct_ref.pdbx_align_begin           2 
# 
_struct_ref_seq.align_id                      1 
_struct_ref_seq.ref_id                        1 
_struct_ref_seq.pdbx_PDB_id_code              9HQ9 
_struct_ref_seq.pdbx_strand_id                A 
_struct_ref_seq.seq_align_beg                 5 
_struct_ref_seq.pdbx_seq_align_beg_ins_code   ? 
_struct_ref_seq.seq_align_end                 198 
_struct_ref_seq.pdbx_seq_align_end_ins_code   ? 
_struct_ref_seq.pdbx_db_accession             P09651 
_struct_ref_seq.db_align_beg                  2 
_struct_ref_seq.pdbx_db_align_beg_ins_code    ? 
_struct_ref_seq.db_align_end                  195 
_struct_ref_seq.pdbx_db_align_end_ins_code    ? 
_struct_ref_seq.pdbx_auth_seq_align_beg       2 
_struct_ref_seq.pdbx_auth_seq_align_end       195 
# 
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 9HQ9 GLY A 1 ? UNP P09651 ? ? 'expression tag' -2 1 
1 9HQ9 PRO A 2 ? UNP P09651 ? ? 'expression tag' -1 2 
1 9HQ9 MET A 3 ? UNP P09651 ? ? 'expression tag' 0  3 
1 9HQ9 GLY A 4 ? UNP P09651 ? ? 'expression tag' 1  4 
# 
_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 
# 
loop_
_pdbx_struct_assembly_prop.biol_id 
_pdbx_struct_assembly_prop.type 
_pdbx_struct_assembly_prop.value 
_pdbx_struct_assembly_prop.details 
1 'ABSA (A^2)' 0    ? 
1 MORE         0    ? 
1 'SSA (A^2)'  9670 ? 
# 
_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_assembly_auth_evidence.id                     1 
_pdbx_struct_assembly_auth_evidence.assembly_id            1 
_pdbx_struct_assembly_auth_evidence.experimental_support   none 
_pdbx_struct_assembly_auth_evidence.details                ? 
# 
_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 PRO A 13  ? LEU A 16  ? PRO A 10  LEU A 13  5 ? 4  
HELX_P HELX_P2 AA2 THR A 29  ? GLU A 38  ? THR A 26  GLU A 35  1 ? 10 
HELX_P HELX_P3 AA3 GLN A 39  ? GLY A 41  ? GLN A 36  GLY A 38  5 ? 3  
HELX_P HELX_P4 AA4 THR A 67  ? ALA A 77  ? THR A 64  ALA A 74  1 ? 11 
HELX_P HELX_P5 AA5 GLU A 120 ? GLU A 129 ? GLU A 117 GLU A 126 1 ? 10 
HELX_P HELX_P6 AA6 ASP A 158 ? GLN A 168 ? ASP A 155 GLN A 165 1 ? 11 
# 
_struct_conf_type.id          HELX_P 
_struct_conf_type.criteria    ? 
_struct_conf_type.reference   ? 
# 
_struct_mon_prot_cis.pdbx_id                1 
_struct_mon_prot_cis.label_comp_id          ARG 
_struct_mon_prot_cis.label_seq_id           78 
_struct_mon_prot_cis.label_asym_id          A 
_struct_mon_prot_cis.label_alt_id           . 
_struct_mon_prot_cis.pdbx_PDB_ins_code      ? 
_struct_mon_prot_cis.auth_comp_id           ARG 
_struct_mon_prot_cis.auth_seq_id            75 
_struct_mon_prot_cis.auth_asym_id           A 
_struct_mon_prot_cis.pdbx_label_comp_id_2   PRO 
_struct_mon_prot_cis.pdbx_label_seq_id_2    79 
_struct_mon_prot_cis.pdbx_label_asym_id_2   A 
_struct_mon_prot_cis.pdbx_PDB_ins_code_2    ? 
_struct_mon_prot_cis.pdbx_auth_comp_id_2    PRO 
_struct_mon_prot_cis.pdbx_auth_seq_id_2     76 
_struct_mon_prot_cis.pdbx_auth_asym_id_2    A 
_struct_mon_prot_cis.pdbx_PDB_model_num     1 
_struct_mon_prot_cis.pdbx_omega_angle       -1.12 
# 
loop_
_struct_sheet.id 
_struct_sheet.type 
_struct_sheet.number_strands 
_struct_sheet.details 
AA1 ? 4 ? 
AA2 ? 2 ? 
AA3 ? 4 ? 
AA4 ? 2 ? 
# 
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 
AA2 1 2 ? anti-parallel 
AA3 1 2 ? anti-parallel 
AA3 2 3 ? anti-parallel 
AA3 3 4 ? anti-parallel 
AA4 1 2 ? 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 LEU A 43  ? ARG A 50  ? LEU A 40  ARG A 47  
AA1 2 SER A 57  ? TYR A 65  ? SER A 54  TYR A 62  
AA1 3 LYS A 18  ? GLY A 22  ? LYS A 15  GLY A 19  
AA1 4 GLU A 88  ? ARG A 91  ? GLU A 85  ARG A 88  
AA2 1 LYS A 81  ? VAL A 82  ? LYS A 78  VAL A 79  
AA2 2 ARG A 85  ? VAL A 86  ? ARG A 82  VAL A 83  
AA3 1 ILE A 134 ? THR A 141 ? ILE A 131 THR A 138 
AA3 2 LYS A 148 ? PHE A 156 ? LYS A 145 PHE A 153 
AA3 3 LYS A 109 ? GLY A 113 ? LYS A 106 GLY A 110 
AA3 4 GLU A 179 ? LYS A 182 ? GLU A 176 LYS A 179 
AA4 1 THR A 172 ? VAL A 173 ? THR A 169 VAL A 170 
AA4 2 HIS A 176 ? ASN A 177 ? HIS A 173 ASN A 174 
# 
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 MET A 49  ? N MET A 46  O ARG A 58  ? O ARG A 55  
AA1 2 3 O VAL A 63  ? O VAL A 60  N LEU A 19  ? N LEU A 16  
AA1 3 4 N PHE A 20  ? N PHE A 17  O LYS A 90  ? O LYS A 87  
AA2 1 2 N VAL A 82  ? N VAL A 79  O ARG A 85  ? O ARG A 82  
AA3 1 2 N GLU A 135 ? N GLU A 132 O THR A 155 ? O THR A 152 
AA3 2 3 O ALA A 152 ? O ALA A 149 N VAL A 112 ? N VAL A 109 
AA3 3 4 N GLY A 113 ? N GLY A 110 O GLU A 179 ? O GLU A 176 
AA4 1 2 N VAL A 173 ? N VAL A 170 O HIS A 176 ? O HIS A 173 
# 
_pdbx_entry_details.entry_id                   9HQ9 
_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   N 
# 
_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    336 
_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    375 
_pdbx_validate_close_contact.PDB_ins_code_2   ? 
_pdbx_validate_close_contact.label_alt_id_2   ? 
_pdbx_validate_close_contact.dist             1.87 
# 
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 CYS A 43  ? ? -163.39 117.00  
2 1 CYS A 43  ? ? -163.71 116.97  
3 1 LYS A 113 ? ? 56.93   -156.81 
# 
loop_
_space_group_symop.id 
_space_group_symop.operation_xyz 
1 x,y,z       
2 -x,y+1/2,-z 
# 
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 GLY -2  ? A GLY 1   
2  1 Y 1 A PRO -1  ? A PRO 2   
3  1 Y 1 A MET 0   ? A MET 3   
4  1 Y 1 A GLY 1   ? A GLY 4   
5  1 Y 1 A SER 2   ? A SER 5   
6  1 Y 1 A LYS 3   ? A LYS 6   
7  1 Y 1 A SER 4   ? A SER 7   
8  1 Y 1 A GLU 5   ? A GLU 8   
9  1 Y 1 A SER 6   ? A SER 9   
10 1 Y 1 A ARG 92  ? A ARG 95  
11 1 Y 1 A GLU 93  ? A GLU 96  
12 1 Y 1 A ASP 94  ? A ASP 97  
13 1 Y 1 A SER 95  ? A SER 98  
14 1 Y 1 A GLN 96  ? A GLN 99  
15 1 Y 1 A ARG 97  ? A ARG 100 
16 1 Y 1 A PRO 98  ? A PRO 101 
17 1 Y 1 A GLY 99  ? A GLY 102 
18 1 Y 1 A ALA 100 ? A ALA 103 
19 1 Y 1 A LYS 183 ? A LYS 186 
20 1 Y 1 A GLN 184 ? A GLN 187 
21 1 Y 1 A GLU 185 ? A GLU 188 
22 1 Y 1 A MET 186 ? A MET 189 
23 1 Y 1 A ALA 187 ? A ALA 190 
24 1 Y 1 A SER 188 ? A SER 191 
25 1 Y 1 A ALA 189 ? A ALA 192 
26 1 Y 1 A SER 190 ? A SER 193 
27 1 Y 1 A SER 191 ? A SER 194 
28 1 Y 1 A SER 192 ? A SER 195 
29 1 Y 1 A GLN 193 ? A GLN 196 
30 1 Y 1 A ARG 194 ? A ARG 197 
31 1 Y 1 A GLY 195 ? A GLY 198 
# 
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 
A1H97 C10  C N N 1   
A1H97 C13  C Y N 2   
A1H97 C15  C Y N 3   
A1H97 C05  C N R 4   
A1H97 C06  C N N 5   
A1H97 C07  C N N 6   
A1H97 C08  C N N 7   
A1H97 C09  C N N 8   
A1H97 C11  C N N 9   
A1H97 C12  C Y N 10  
A1H97 C14  C Y N 11  
A1H97 N02  N N N 12  
A1H97 N03  N Y N 13  
A1H97 N04  N Y N 14  
A1H97 O01  O N N 15  
A1H97 H102 H N N 16  
A1H97 H101 H N N 17  
A1H97 H131 H N N 18  
A1H97 H151 H N N 19  
A1H97 H061 H N N 20  
A1H97 H062 H N N 21  
A1H97 H072 H N N 22  
A1H97 H071 H N N 23  
A1H97 H082 H N N 24  
A1H97 H081 H N N 25  
A1H97 H092 H N N 26  
A1H97 H091 H N N 27  
A1H97 H112 H N N 28  
A1H97 H111 H N N 29  
A1H97 H141 H N N 30  
ALA   N    N N N 31  
ALA   CA   C N S 32  
ALA   C    C N N 33  
ALA   O    O N N 34  
ALA   CB   C N N 35  
ALA   OXT  O N N 36  
ALA   H    H N N 37  
ALA   H2   H N N 38  
ALA   HA   H N N 39  
ALA   HB1  H N N 40  
ALA   HB2  H N N 41  
ALA   HB3  H N N 42  
ALA   HXT  H N N 43  
ARG   N    N N N 44  
ARG   CA   C N S 45  
ARG   C    C N N 46  
ARG   O    O N N 47  
ARG   CB   C N N 48  
ARG   CG   C N N 49  
ARG   CD   C N N 50  
ARG   NE   N N N 51  
ARG   CZ   C N N 52  
ARG   NH1  N N N 53  
ARG   NH2  N N N 54  
ARG   OXT  O N N 55  
ARG   H    H N N 56  
ARG   H2   H N N 57  
ARG   HA   H N N 58  
ARG   HB2  H N N 59  
ARG   HB3  H N N 60  
ARG   HG2  H N N 61  
ARG   HG3  H N N 62  
ARG   HD2  H N N 63  
ARG   HD3  H N N 64  
ARG   HE   H N N 65  
ARG   HH11 H N N 66  
ARG   HH12 H N N 67  
ARG   HH21 H N N 68  
ARG   HH22 H N N 69  
ARG   HXT  H N N 70  
ASN   N    N N N 71  
ASN   CA   C N S 72  
ASN   C    C N N 73  
ASN   O    O N N 74  
ASN   CB   C N N 75  
ASN   CG   C N N 76  
ASN   OD1  O N N 77  
ASN   ND2  N N N 78  
ASN   OXT  O N N 79  
ASN   H    H N N 80  
ASN   H2   H N N 81  
ASN   HA   H N N 82  
ASN   HB2  H N N 83  
ASN   HB3  H N N 84  
ASN   HD21 H N N 85  
ASN   HD22 H N N 86  
ASN   HXT  H N N 87  
ASP   N    N N N 88  
ASP   CA   C N S 89  
ASP   C    C N N 90  
ASP   O    O N N 91  
ASP   CB   C N N 92  
ASP   CG   C N N 93  
ASP   OD1  O N N 94  
ASP   OD2  O N N 95  
ASP   OXT  O N N 96  
ASP   H    H N N 97  
ASP   H2   H N N 98  
ASP   HA   H N N 99  
ASP   HB2  H N N 100 
ASP   HB3  H N N 101 
ASP   HD2  H N N 102 
ASP   HXT  H N N 103 
CYS   N    N N N 104 
CYS   CA   C N R 105 
CYS   C    C N N 106 
CYS   O    O N N 107 
CYS   CB   C N N 108 
CYS   SG   S N N 109 
CYS   OXT  O N N 110 
CYS   H    H N N 111 
CYS   H2   H N N 112 
CYS   HA   H N N 113 
CYS   HB2  H N N 114 
CYS   HB3  H N N 115 
CYS   HG   H N N 116 
CYS   HXT  H N N 117 
GLN   N    N N N 118 
GLN   CA   C N S 119 
GLN   C    C N N 120 
GLN   O    O N N 121 
GLN   CB   C N N 122 
GLN   CG   C N N 123 
GLN   CD   C N N 124 
GLN   OE1  O N N 125 
GLN   NE2  N N N 126 
GLN   OXT  O N N 127 
GLN   H    H N N 128 
GLN   H2   H N N 129 
GLN   HA   H N N 130 
GLN   HB2  H N N 131 
GLN   HB3  H N N 132 
GLN   HG2  H N N 133 
GLN   HG3  H N N 134 
GLN   HE21 H N N 135 
GLN   HE22 H N N 136 
GLN   HXT  H N N 137 
GLU   N    N N N 138 
GLU   CA   C N S 139 
GLU   C    C N N 140 
GLU   O    O N N 141 
GLU   CB   C N N 142 
GLU   CG   C N N 143 
GLU   CD   C N N 144 
GLU   OE1  O N N 145 
GLU   OE2  O N N 146 
GLU   OXT  O N N 147 
GLU   H    H N N 148 
GLU   H2   H N N 149 
GLU   HA   H N N 150 
GLU   HB2  H N N 151 
GLU   HB3  H N N 152 
GLU   HG2  H N N 153 
GLU   HG3  H N N 154 
GLU   HE2  H N N 155 
GLU   HXT  H N N 156 
GLY   N    N N N 157 
GLY   CA   C N N 158 
GLY   C    C N N 159 
GLY   O    O N N 160 
GLY   OXT  O N N 161 
GLY   H    H N N 162 
GLY   H2   H N N 163 
GLY   HA2  H N N 164 
GLY   HA3  H N N 165 
GLY   HXT  H N N 166 
HIS   N    N N N 167 
HIS   CA   C N S 168 
HIS   C    C N N 169 
HIS   O    O N N 170 
HIS   CB   C N N 171 
HIS   CG   C Y N 172 
HIS   ND1  N Y N 173 
HIS   CD2  C Y N 174 
HIS   CE1  C Y N 175 
HIS   NE2  N Y N 176 
HIS   OXT  O N N 177 
HIS   H    H N N 178 
HIS   H2   H N N 179 
HIS   HA   H N N 180 
HIS   HB2  H N N 181 
HIS   HB3  H N N 182 
HIS   HD1  H N N 183 
HIS   HD2  H N N 184 
HIS   HE1  H N N 185 
HIS   HE2  H N N 186 
HIS   HXT  H N N 187 
HOH   O    O N N 188 
HOH   H1   H N N 189 
HOH   H2   H N N 190 
ILE   N    N N N 191 
ILE   CA   C N S 192 
ILE   C    C N N 193 
ILE   O    O N N 194 
ILE   CB   C N S 195 
ILE   CG1  C N N 196 
ILE   CG2  C N N 197 
ILE   CD1  C N N 198 
ILE   OXT  O N N 199 
ILE   H    H N N 200 
ILE   H2   H N N 201 
ILE   HA   H N N 202 
ILE   HB   H N N 203 
ILE   HG12 H N N 204 
ILE   HG13 H N N 205 
ILE   HG21 H N N 206 
ILE   HG22 H N N 207 
ILE   HG23 H N N 208 
ILE   HD11 H N N 209 
ILE   HD12 H N N 210 
ILE   HD13 H N N 211 
ILE   HXT  H N N 212 
LEU   N    N N N 213 
LEU   CA   C N S 214 
LEU   C    C N N 215 
LEU   O    O N N 216 
LEU   CB   C N N 217 
LEU   CG   C N N 218 
LEU   CD1  C N N 219 
LEU   CD2  C N N 220 
LEU   OXT  O N N 221 
LEU   H    H N N 222 
LEU   H2   H N N 223 
LEU   HA   H N N 224 
LEU   HB2  H N N 225 
LEU   HB3  H N N 226 
LEU   HG   H N N 227 
LEU   HD11 H N N 228 
LEU   HD12 H N N 229 
LEU   HD13 H N N 230 
LEU   HD21 H N N 231 
LEU   HD22 H N N 232 
LEU   HD23 H N N 233 
LEU   HXT  H N N 234 
LYS   N    N N N 235 
LYS   CA   C N S 236 
LYS   C    C N N 237 
LYS   O    O N N 238 
LYS   CB   C N N 239 
LYS   CG   C N N 240 
LYS   CD   C N N 241 
LYS   CE   C N N 242 
LYS   NZ   N N N 243 
LYS   OXT  O N N 244 
LYS   H    H N N 245 
LYS   H2   H N N 246 
LYS   HA   H N N 247 
LYS   HB2  H N N 248 
LYS   HB3  H N N 249 
LYS   HG2  H N N 250 
LYS   HG3  H N N 251 
LYS   HD2  H N N 252 
LYS   HD3  H N N 253 
LYS   HE2  H N N 254 
LYS   HE3  H N N 255 
LYS   HZ1  H N N 256 
LYS   HZ2  H N N 257 
LYS   HZ3  H N N 258 
LYS   HXT  H N N 259 
MET   N    N N N 260 
MET   CA   C N S 261 
MET   C    C N N 262 
MET   O    O N N 263 
MET   CB   C N N 264 
MET   CG   C N N 265 
MET   SD   S N N 266 
MET   CE   C N N 267 
MET   OXT  O N N 268 
MET   H    H N N 269 
MET   H2   H N N 270 
MET   HA   H N N 271 
MET   HB2  H N N 272 
MET   HB3  H N N 273 
MET   HG2  H N N 274 
MET   HG3  H N N 275 
MET   HE1  H N N 276 
MET   HE2  H N N 277 
MET   HE3  H N N 278 
MET   HXT  H N N 279 
PHE   N    N N N 280 
PHE   CA   C N S 281 
PHE   C    C N N 282 
PHE   O    O N N 283 
PHE   CB   C N N 284 
PHE   CG   C Y N 285 
PHE   CD1  C Y N 286 
PHE   CD2  C Y N 287 
PHE   CE1  C Y N 288 
PHE   CE2  C Y N 289 
PHE   CZ   C Y N 290 
PHE   OXT  O N N 291 
PHE   H    H N N 292 
PHE   H2   H N N 293 
PHE   HA   H N N 294 
PHE   HB2  H N N 295 
PHE   HB3  H N N 296 
PHE   HD1  H N N 297 
PHE   HD2  H N N 298 
PHE   HE1  H N N 299 
PHE   HE2  H N N 300 
PHE   HZ   H N N 301 
PHE   HXT  H N N 302 
PRO   N    N N N 303 
PRO   CA   C N S 304 
PRO   C    C N N 305 
PRO   O    O N N 306 
PRO   CB   C N N 307 
PRO   CG   C N N 308 
PRO   CD   C N N 309 
PRO   OXT  O N N 310 
PRO   H    H N N 311 
PRO   HA   H N N 312 
PRO   HB2  H N N 313 
PRO   HB3  H N N 314 
PRO   HG2  H N N 315 
PRO   HG3  H N N 316 
PRO   HD2  H N N 317 
PRO   HD3  H N N 318 
PRO   HXT  H N N 319 
SER   N    N N N 320 
SER   CA   C N S 321 
SER   C    C N N 322 
SER   O    O N N 323 
SER   CB   C N N 324 
SER   OG   O N N 325 
SER   OXT  O N N 326 
SER   H    H N N 327 
SER   H2   H N N 328 
SER   HA   H N N 329 
SER   HB2  H N N 330 
SER   HB3  H N N 331 
SER   HG   H N N 332 
SER   HXT  H N N 333 
THR   N    N N N 334 
THR   CA   C N S 335 
THR   C    C N N 336 
THR   O    O N N 337 
THR   CB   C N R 338 
THR   OG1  O N N 339 
THR   CG2  C N N 340 
THR   OXT  O N N 341 
THR   H    H N N 342 
THR   H2   H N N 343 
THR   HA   H N N 344 
THR   HB   H N N 345 
THR   HG1  H N N 346 
THR   HG21 H N N 347 
THR   HG22 H N N 348 
THR   HG23 H N N 349 
THR   HXT  H N N 350 
TRP   N    N N N 351 
TRP   CA   C N S 352 
TRP   C    C N N 353 
TRP   O    O N N 354 
TRP   CB   C N N 355 
TRP   CG   C Y N 356 
TRP   CD1  C Y N 357 
TRP   CD2  C Y N 358 
TRP   NE1  N Y N 359 
TRP   CE2  C Y N 360 
TRP   CE3  C Y N 361 
TRP   CZ2  C Y N 362 
TRP   CZ3  C Y N 363 
TRP   CH2  C Y N 364 
TRP   OXT  O N N 365 
TRP   H    H N N 366 
TRP   H2   H N N 367 
TRP   HA   H N N 368 
TRP   HB2  H N N 369 
TRP   HB3  H N N 370 
TRP   HD1  H N N 371 
TRP   HE1  H N N 372 
TRP   HE3  H N N 373 
TRP   HZ2  H N N 374 
TRP   HZ3  H N N 375 
TRP   HH2  H N N 376 
TRP   HXT  H N N 377 
TYR   N    N N N 378 
TYR   CA   C N S 379 
TYR   C    C N N 380 
TYR   O    O N N 381 
TYR   CB   C N N 382 
TYR   CG   C Y N 383 
TYR   CD1  C Y N 384 
TYR   CD2  C Y N 385 
TYR   CE1  C Y N 386 
TYR   CE2  C Y N 387 
TYR   CZ   C Y N 388 
TYR   OH   O N N 389 
TYR   OXT  O N N 390 
TYR   H    H N N 391 
TYR   H2   H N N 392 
TYR   HA   H N N 393 
TYR   HB2  H N N 394 
TYR   HB3  H N N 395 
TYR   HD1  H N N 396 
TYR   HD2  H N N 397 
TYR   HE1  H N N 398 
TYR   HE2  H N N 399 
TYR   HH   H N N 400 
TYR   HXT  H N N 401 
VAL   N    N N N 402 
VAL   CA   C N S 403 
VAL   C    C N N 404 
VAL   O    O N N 405 
VAL   CB   C N N 406 
VAL   CG1  C N N 407 
VAL   CG2  C N N 408 
VAL   OXT  O N N 409 
VAL   H    H N N 410 
VAL   H2   H N N 411 
VAL   HA   H N N 412 
VAL   HB   H N N 413 
VAL   HG11 H N N 414 
VAL   HG12 H N N 415 
VAL   HG13 H N N 416 
VAL   HG21 H N N 417 
VAL   HG22 H N N 418 
VAL   HG23 H N N 419 
VAL   HXT  H N N 420 
# 
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 
A1H97 O01 C09  sing N N 1   
A1H97 O01 C11  sing N N 2   
A1H97 N02 C07  sing N N 3   
A1H97 N02 C10  sing N N 4   
A1H97 N02 C12  sing N N 5   
A1H97 N03 C12  doub Y N 6   
A1H97 N03 C14  sing Y N 7   
A1H97 N04 C13  doub Y N 8   
A1H97 N04 C15  sing Y N 9   
A1H97 C05 C06  sing N N 10  
A1H97 C05 C07  sing N N 11  
A1H97 C05 C08  sing N N 12  
A1H97 C05 C09  sing N N 13  
A1H97 C06 C10  sing N N 14  
A1H97 C08 C11  sing N N 15  
A1H97 C12 C13  sing Y N 16  
A1H97 C14 C15  doub Y N 17  
A1H97 C10 H102 sing N N 18  
A1H97 C10 H101 sing N N 19  
A1H97 C13 H131 sing N N 20  
A1H97 C15 H151 sing N N 21  
A1H97 C06 H061 sing N N 22  
A1H97 C06 H062 sing N N 23  
A1H97 C07 H072 sing N N 24  
A1H97 C07 H071 sing N N 25  
A1H97 C08 H082 sing N N 26  
A1H97 C08 H081 sing N N 27  
A1H97 C09 H092 sing N N 28  
A1H97 C09 H091 sing N N 29  
A1H97 C11 H112 sing N N 30  
A1H97 C11 H111 sing N N 31  
A1H97 C14 H141 sing N N 32  
ALA   N   CA   sing N N 33  
ALA   N   H    sing N N 34  
ALA   N   H2   sing N N 35  
ALA   CA  C    sing N N 36  
ALA   CA  CB   sing N N 37  
ALA   CA  HA   sing N N 38  
ALA   C   O    doub N N 39  
ALA   C   OXT  sing N N 40  
ALA   CB  HB1  sing N N 41  
ALA   CB  HB2  sing N N 42  
ALA   CB  HB3  sing N N 43  
ALA   OXT HXT  sing N N 44  
ARG   N   CA   sing N N 45  
ARG   N   H    sing N N 46  
ARG   N   H2   sing N N 47  
ARG   CA  C    sing N N 48  
ARG   CA  CB   sing N N 49  
ARG   CA  HA   sing N N 50  
ARG   C   O    doub N N 51  
ARG   C   OXT  sing N N 52  
ARG   CB  CG   sing N N 53  
ARG   CB  HB2  sing N N 54  
ARG   CB  HB3  sing N N 55  
ARG   CG  CD   sing N N 56  
ARG   CG  HG2  sing N N 57  
ARG   CG  HG3  sing N N 58  
ARG   CD  NE   sing N N 59  
ARG   CD  HD2  sing N N 60  
ARG   CD  HD3  sing N N 61  
ARG   NE  CZ   sing N N 62  
ARG   NE  HE   sing N N 63  
ARG   CZ  NH1  sing N N 64  
ARG   CZ  NH2  doub N N 65  
ARG   NH1 HH11 sing N N 66  
ARG   NH1 HH12 sing N N 67  
ARG   NH2 HH21 sing N N 68  
ARG   NH2 HH22 sing N N 69  
ARG   OXT HXT  sing N N 70  
ASN   N   CA   sing N N 71  
ASN   N   H    sing N N 72  
ASN   N   H2   sing N N 73  
ASN   CA  C    sing N N 74  
ASN   CA  CB   sing N N 75  
ASN   CA  HA   sing N N 76  
ASN   C   O    doub N N 77  
ASN   C   OXT  sing N N 78  
ASN   CB  CG   sing N N 79  
ASN   CB  HB2  sing N N 80  
ASN   CB  HB3  sing N N 81  
ASN   CG  OD1  doub N N 82  
ASN   CG  ND2  sing N N 83  
ASN   ND2 HD21 sing N N 84  
ASN   ND2 HD22 sing N N 85  
ASN   OXT HXT  sing N N 86  
ASP   N   CA   sing N N 87  
ASP   N   H    sing N N 88  
ASP   N   H2   sing N N 89  
ASP   CA  C    sing N N 90  
ASP   CA  CB   sing N N 91  
ASP   CA  HA   sing N N 92  
ASP   C   O    doub N N 93  
ASP   C   OXT  sing N N 94  
ASP   CB  CG   sing N N 95  
ASP   CB  HB2  sing N N 96  
ASP   CB  HB3  sing N N 97  
ASP   CG  OD1  doub N N 98  
ASP   CG  OD2  sing N N 99  
ASP   OD2 HD2  sing N N 100 
ASP   OXT HXT  sing N N 101 
CYS   N   CA   sing N N 102 
CYS   N   H    sing N N 103 
CYS   N   H2   sing N N 104 
CYS   CA  C    sing N N 105 
CYS   CA  CB   sing N N 106 
CYS   CA  HA   sing N N 107 
CYS   C   O    doub N N 108 
CYS   C   OXT  sing N N 109 
CYS   CB  SG   sing N N 110 
CYS   CB  HB2  sing N N 111 
CYS   CB  HB3  sing N N 112 
CYS   SG  HG   sing N N 113 
CYS   OXT HXT  sing N N 114 
GLN   N   CA   sing N N 115 
GLN   N   H    sing N N 116 
GLN   N   H2   sing N N 117 
GLN   CA  C    sing N N 118 
GLN   CA  CB   sing N N 119 
GLN   CA  HA   sing N N 120 
GLN   C   O    doub N N 121 
GLN   C   OXT  sing N N 122 
GLN   CB  CG   sing N N 123 
GLN   CB  HB2  sing N N 124 
GLN   CB  HB3  sing N N 125 
GLN   CG  CD   sing N N 126 
GLN   CG  HG2  sing N N 127 
GLN   CG  HG3  sing N N 128 
GLN   CD  OE1  doub N N 129 
GLN   CD  NE2  sing N N 130 
GLN   NE2 HE21 sing N N 131 
GLN   NE2 HE22 sing N N 132 
GLN   OXT HXT  sing N N 133 
GLU   N   CA   sing N N 134 
GLU   N   H    sing N N 135 
GLU   N   H2   sing N N 136 
GLU   CA  C    sing N N 137 
GLU   CA  CB   sing N N 138 
GLU   CA  HA   sing N N 139 
GLU   C   O    doub N N 140 
GLU   C   OXT  sing N N 141 
GLU   CB  CG   sing N N 142 
GLU   CB  HB2  sing N N 143 
GLU   CB  HB3  sing N N 144 
GLU   CG  CD   sing N N 145 
GLU   CG  HG2  sing N N 146 
GLU   CG  HG3  sing N N 147 
GLU   CD  OE1  doub N N 148 
GLU   CD  OE2  sing N N 149 
GLU   OE2 HE2  sing N N 150 
GLU   OXT HXT  sing N N 151 
GLY   N   CA   sing N N 152 
GLY   N   H    sing N N 153 
GLY   N   H2   sing N N 154 
GLY   CA  C    sing N N 155 
GLY   CA  HA2  sing N N 156 
GLY   CA  HA3  sing N N 157 
GLY   C   O    doub N N 158 
GLY   C   OXT  sing N N 159 
GLY   OXT HXT  sing N N 160 
HIS   N   CA   sing N N 161 
HIS   N   H    sing N N 162 
HIS   N   H2   sing N N 163 
HIS   CA  C    sing N N 164 
HIS   CA  CB   sing N N 165 
HIS   CA  HA   sing N N 166 
HIS   C   O    doub N N 167 
HIS   C   OXT  sing N N 168 
HIS   CB  CG   sing N N 169 
HIS   CB  HB2  sing N N 170 
HIS   CB  HB3  sing N N 171 
HIS   CG  ND1  sing Y N 172 
HIS   CG  CD2  doub Y N 173 
HIS   ND1 CE1  doub Y N 174 
HIS   ND1 HD1  sing N N 175 
HIS   CD2 NE2  sing Y N 176 
HIS   CD2 HD2  sing N N 177 
HIS   CE1 NE2  sing Y N 178 
HIS   CE1 HE1  sing N N 179 
HIS   NE2 HE2  sing N N 180 
HIS   OXT HXT  sing N N 181 
HOH   O   H1   sing N N 182 
HOH   O   H2   sing N N 183 
ILE   N   CA   sing N N 184 
ILE   N   H    sing N N 185 
ILE   N   H2   sing N N 186 
ILE   CA  C    sing N N 187 
ILE   CA  CB   sing N N 188 
ILE   CA  HA   sing N N 189 
ILE   C   O    doub N N 190 
ILE   C   OXT  sing N N 191 
ILE   CB  CG1  sing N N 192 
ILE   CB  CG2  sing N N 193 
ILE   CB  HB   sing N N 194 
ILE   CG1 CD1  sing N N 195 
ILE   CG1 HG12 sing N N 196 
ILE   CG1 HG13 sing N N 197 
ILE   CG2 HG21 sing N N 198 
ILE   CG2 HG22 sing N N 199 
ILE   CG2 HG23 sing N N 200 
ILE   CD1 HD11 sing N N 201 
ILE   CD1 HD12 sing N N 202 
ILE   CD1 HD13 sing N N 203 
ILE   OXT HXT  sing N N 204 
LEU   N   CA   sing N N 205 
LEU   N   H    sing N N 206 
LEU   N   H2   sing N N 207 
LEU   CA  C    sing N N 208 
LEU   CA  CB   sing N N 209 
LEU   CA  HA   sing N N 210 
LEU   C   O    doub N N 211 
LEU   C   OXT  sing N N 212 
LEU   CB  CG   sing N N 213 
LEU   CB  HB2  sing N N 214 
LEU   CB  HB3  sing N N 215 
LEU   CG  CD1  sing N N 216 
LEU   CG  CD2  sing N N 217 
LEU   CG  HG   sing N N 218 
LEU   CD1 HD11 sing N N 219 
LEU   CD1 HD12 sing N N 220 
LEU   CD1 HD13 sing N N 221 
LEU   CD2 HD21 sing N N 222 
LEU   CD2 HD22 sing N N 223 
LEU   CD2 HD23 sing N N 224 
LEU   OXT HXT  sing N N 225 
LYS   N   CA   sing N N 226 
LYS   N   H    sing N N 227 
LYS   N   H2   sing N N 228 
LYS   CA  C    sing N N 229 
LYS   CA  CB   sing N N 230 
LYS   CA  HA   sing N N 231 
LYS   C   O    doub N N 232 
LYS   C   OXT  sing N N 233 
LYS   CB  CG   sing N N 234 
LYS   CB  HB2  sing N N 235 
LYS   CB  HB3  sing N N 236 
LYS   CG  CD   sing N N 237 
LYS   CG  HG2  sing N N 238 
LYS   CG  HG3  sing N N 239 
LYS   CD  CE   sing N N 240 
LYS   CD  HD2  sing N N 241 
LYS   CD  HD3  sing N N 242 
LYS   CE  NZ   sing N N 243 
LYS   CE  HE2  sing N N 244 
LYS   CE  HE3  sing N N 245 
LYS   NZ  HZ1  sing N N 246 
LYS   NZ  HZ2  sing N N 247 
LYS   NZ  HZ3  sing N N 248 
LYS   OXT HXT  sing N N 249 
MET   N   CA   sing N N 250 
MET   N   H    sing N N 251 
MET   N   H2   sing N N 252 
MET   CA  C    sing N N 253 
MET   CA  CB   sing N N 254 
MET   CA  HA   sing N N 255 
MET   C   O    doub N N 256 
MET   C   OXT  sing N N 257 
MET   CB  CG   sing N N 258 
MET   CB  HB2  sing N N 259 
MET   CB  HB3  sing N N 260 
MET   CG  SD   sing N N 261 
MET   CG  HG2  sing N N 262 
MET   CG  HG3  sing N N 263 
MET   SD  CE   sing N N 264 
MET   CE  HE1  sing N N 265 
MET   CE  HE2  sing N N 266 
MET   CE  HE3  sing N N 267 
MET   OXT HXT  sing N N 268 
PHE   N   CA   sing N N 269 
PHE   N   H    sing N N 270 
PHE   N   H2   sing N N 271 
PHE   CA  C    sing N N 272 
PHE   CA  CB   sing N N 273 
PHE   CA  HA   sing N N 274 
PHE   C   O    doub N N 275 
PHE   C   OXT  sing N N 276 
PHE   CB  CG   sing N N 277 
PHE   CB  HB2  sing N N 278 
PHE   CB  HB3  sing N N 279 
PHE   CG  CD1  doub Y N 280 
PHE   CG  CD2  sing Y N 281 
PHE   CD1 CE1  sing Y N 282 
PHE   CD1 HD1  sing N N 283 
PHE   CD2 CE2  doub Y N 284 
PHE   CD2 HD2  sing N N 285 
PHE   CE1 CZ   doub Y N 286 
PHE   CE1 HE1  sing N N 287 
PHE   CE2 CZ   sing Y N 288 
PHE   CE2 HE2  sing N N 289 
PHE   CZ  HZ   sing N N 290 
PHE   OXT HXT  sing N N 291 
PRO   N   CA   sing N N 292 
PRO   N   CD   sing N N 293 
PRO   N   H    sing N N 294 
PRO   CA  C    sing N N 295 
PRO   CA  CB   sing N N 296 
PRO   CA  HA   sing N N 297 
PRO   C   O    doub N N 298 
PRO   C   OXT  sing N N 299 
PRO   CB  CG   sing N N 300 
PRO   CB  HB2  sing N N 301 
PRO   CB  HB3  sing N N 302 
PRO   CG  CD   sing N N 303 
PRO   CG  HG2  sing N N 304 
PRO   CG  HG3  sing N N 305 
PRO   CD  HD2  sing N N 306 
PRO   CD  HD3  sing N N 307 
PRO   OXT HXT  sing N N 308 
SER   N   CA   sing N N 309 
SER   N   H    sing N N 310 
SER   N   H2   sing N N 311 
SER   CA  C    sing N N 312 
SER   CA  CB   sing N N 313 
SER   CA  HA   sing N N 314 
SER   C   O    doub N N 315 
SER   C   OXT  sing N N 316 
SER   CB  OG   sing N N 317 
SER   CB  HB2  sing N N 318 
SER   CB  HB3  sing N N 319 
SER   OG  HG   sing N N 320 
SER   OXT HXT  sing N N 321 
THR   N   CA   sing N N 322 
THR   N   H    sing N N 323 
THR   N   H2   sing N N 324 
THR   CA  C    sing N N 325 
THR   CA  CB   sing N N 326 
THR   CA  HA   sing N N 327 
THR   C   O    doub N N 328 
THR   C   OXT  sing N N 329 
THR   CB  OG1  sing N N 330 
THR   CB  CG2  sing N N 331 
THR   CB  HB   sing N N 332 
THR   OG1 HG1  sing N N 333 
THR   CG2 HG21 sing N N 334 
THR   CG2 HG22 sing N N 335 
THR   CG2 HG23 sing N N 336 
THR   OXT HXT  sing N N 337 
TRP   N   CA   sing N N 338 
TRP   N   H    sing N N 339 
TRP   N   H2   sing N N 340 
TRP   CA  C    sing N N 341 
TRP   CA  CB   sing N N 342 
TRP   CA  HA   sing N N 343 
TRP   C   O    doub N N 344 
TRP   C   OXT  sing N N 345 
TRP   CB  CG   sing N N 346 
TRP   CB  HB2  sing N N 347 
TRP   CB  HB3  sing N N 348 
TRP   CG  CD1  doub Y N 349 
TRP   CG  CD2  sing Y N 350 
TRP   CD1 NE1  sing Y N 351 
TRP   CD1 HD1  sing N N 352 
TRP   CD2 CE2  doub Y N 353 
TRP   CD2 CE3  sing Y N 354 
TRP   NE1 CE2  sing Y N 355 
TRP   NE1 HE1  sing N N 356 
TRP   CE2 CZ2  sing Y N 357 
TRP   CE3 CZ3  doub Y N 358 
TRP   CE3 HE3  sing N N 359 
TRP   CZ2 CH2  doub Y N 360 
TRP   CZ2 HZ2  sing N N 361 
TRP   CZ3 CH2  sing Y N 362 
TRP   CZ3 HZ3  sing N N 363 
TRP   CH2 HH2  sing N N 364 
TRP   OXT HXT  sing N N 365 
TYR   N   CA   sing N N 366 
TYR   N   H    sing N N 367 
TYR   N   H2   sing N N 368 
TYR   CA  C    sing N N 369 
TYR   CA  CB   sing N N 370 
TYR   CA  HA   sing N N 371 
TYR   C   O    doub N N 372 
TYR   C   OXT  sing N N 373 
TYR   CB  CG   sing N N 374 
TYR   CB  HB2  sing N N 375 
TYR   CB  HB3  sing N N 376 
TYR   CG  CD1  doub Y N 377 
TYR   CG  CD2  sing Y N 378 
TYR   CD1 CE1  sing Y N 379 
TYR   CD1 HD1  sing N N 380 
TYR   CD2 CE2  doub Y N 381 
TYR   CD2 HD2  sing N N 382 
TYR   CE1 CZ   doub Y N 383 
TYR   CE1 HE1  sing N N 384 
TYR   CE2 CZ   sing Y N 385 
TYR   CE2 HE2  sing N N 386 
TYR   CZ  OH   sing N N 387 
TYR   OH  HH   sing N N 388 
TYR   OXT HXT  sing N N 389 
VAL   N   CA   sing N N 390 
VAL   N   H    sing N N 391 
VAL   N   H2   sing N N 392 
VAL   CA  C    sing N N 393 
VAL   CA  CB   sing N N 394 
VAL   CA  HA   sing N N 395 
VAL   C   O    doub N N 396 
VAL   C   OXT  sing N N 397 
VAL   CB  CG1  sing N N 398 
VAL   CB  CG2  sing N N 399 
VAL   CB  HB   sing N N 400 
VAL   CG1 HG11 sing N N 401 
VAL   CG1 HG12 sing N N 402 
VAL   CG1 HG13 sing N N 403 
VAL   CG2 HG21 sing N N 404 
VAL   CG2 HG22 sing N N 405 
VAL   CG2 HG23 sing N N 406 
VAL   OXT HXT  sing N N 407 
# 
_pdbx_audit_support.funding_organization   'Not funded' 
_pdbx_audit_support.country                ? 
_pdbx_audit_support.grant_number           ? 
_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   1L3K 
_pdbx_initial_refinement_model.details          ? 
# 
_space_group.name_H-M_alt     'P 1 21 1' 
_space_group.name_Hall        'P 2yb' 
_space_group.IT_number        4 
_space_group.crystal_system   monoclinic 
_space_group.id               1 
# 
_atom_sites.entry_id                    9HQ9 
_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]   0.026320 
_atom_sites.fract_transf_matrix[1][2]   0.000000 
_atom_sites.fract_transf_matrix[1][3]   0.001919 
_atom_sites.fract_transf_matrix[2][1]   0.000000 
_atom_sites.fract_transf_matrix[2][2]   0.022681 
_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]   0.017910 
_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.
;
? 
H   ? ? 0.51345 0.48472 ? ? 24.73122 6.32584  ? ? 0.0 
;2-Gaussian fit: Grosse-Kunstleve RW, Sauter NK, Adams PD: Newsletter of the IUCr Commission on Crystallographic Computing 2004, 3, 22-31.
;
? 
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.
;
? 
O1- ? ? 5.12366 3.84317 ? ? 3.49406  27.47979 ? ? 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    . PRO   A 1 10  ? 0.21600   -3.39700  -9.95200  1.000 43.39562 ?  7   PRO   A N    1 
ATOM   2    C CA   . PRO   A 1 10  ? 0.00800   -4.26800  -8.79000  1.000 47.76794 ?  7   PRO   A CA   1 
ATOM   3    C C    . PRO   A 1 10  ? -1.04000  -3.69400  -7.84300  1.000 42.20849 ?  7   PRO   A C    1 
ATOM   4    O O    . PRO   A 1 10  ? -0.70100  -2.87500  -6.99100  1.000 46.51933 ?  7   PRO   A O    1 
ATOM   5    C CB   . PRO   A 1 10  ? 1.38100   -4.30600  -8.11100  1.000 51.02352 ?  7   PRO   A CB   1 
ATOM   6    C CG   . PRO   A 1 10  ? 2.35500   -3.87400  -9.13500  1.000 49.21334 ?  7   PRO   A CG   1 
ATOM   7    C CD   . PRO   A 1 10  ? 1.63700   -3.10000  -10.19800 1.000 51.12671 ?  7   PRO   A CD   1 
ATOM   8    N N    . LYS   A 1 11  ? -2.29400  -4.10500  -8.00400  1.000 32.27265 ?  8   LYS   A N    1 
ATOM   9    C CA   . LYS   A 1 11  ? -3.35800  -3.65700  -7.11800  1.000 27.43817 ?  8   LYS   A CA   1 
ATOM   10   C C    . LYS   A 1 11  ? -3.32800  -4.45300  -5.81900  1.000 26.47891 ?  8   LYS   A C    1 
ATOM   11   O O    . LYS   A 1 11  ? -3.14700  -5.67500  -5.82600  1.000 27.10670 ?  8   LYS   A O    1 
ATOM   12   C CB   . LYS   A 1 11  ? -4.71400  -3.82400  -7.79800  1.000 31.47340 ?  8   LYS   A CB   1 
ATOM   13   C CG   . LYS   A 1 11  ? -5.37100  -2.54100  -8.26300  1.000 41.31259 ?  8   LYS   A CG   1 
ATOM   14   C CD   . LYS   A 1 11  ? -6.24600  -1.95200  -7.16800  1.000 40.80280 ?  8   LYS   A CD   1 
ATOM   15   C CE   . LYS   A 1 11  ? -7.26800  -0.95900  -7.74200  1.000 36.91093 ?  8   LYS   A CE   1 
ATOM   16   N NZ   . LYS   A 1 11  ? -6.69900  0.36900   -8.08700  1.000 38.63088 ?  8   LYS   A NZ   1 
ATOM   17   N N    . GLU   A 1 12  ? -3.49700  -3.75700  -4.69600  1.000 19.08526 ?  9   GLU   A N    1 
ATOM   18   C CA   . GLU   A 1 12  ? -3.63400  -4.45000  -3.42400  1.000 14.20889 ?  9   GLU   A CA   1 
ATOM   19   C C    . GLU   A 1 12  ? -4.89900  -5.30000  -3.46500  1.000 10.62742 ?  9   GLU   A C    1 
ATOM   20   O O    . GLU   A 1 12  ? -5.87900  -4.91000  -4.09700  1.000 13.27917 ?  9   GLU   A O    1 
ATOM   21   C CB   . GLU   A 1 12  ? -3.74100  -3.44600  -2.28500  1.000 12.67508 ?  9   GLU   A CB   1 
ATOM   22   C CG   . GLU   A 1 12  ? -2.58800  -2.47800  -2.26200  1.000 15.11257 ?  9   GLU   A CG   1 
ATOM   23   C CD   . GLU   A 1 12  ? -3.01000  -1.14600  -2.84400  1.000 17.24985 ?  9   GLU   A CD   1 
ATOM   24   O OE1  . GLU   A 1 12  ? -3.40200  -1.12400  -4.03700  1.000 40.47895 ?  9   GLU   A OE1  1 
ATOM   25   O OE2  . GLU   A 1 12  ? -2.94100  -0.14100  -2.13500  1.000 18.93381 -1 9   GLU   A OE2  1 
ATOM   26   N N    . PRO   A 1 13  ? -4.91600  -6.44000  -2.78500  1.000 11.52018 ?  10  PRO   A N    1 
ATOM   27   C CA   . PRO   A 1 13  ? -6.13600  -7.25800  -2.73000  1.000 10.82979 ?  10  PRO   A CA   1 
ATOM   28   C C    . PRO   A 1 13  ? -7.34600  -6.42200  -2.34400  1.000 14.68913 ?  10  PRO   A C    1 
ATOM   29   O O    . PRO   A 1 13  ? -7.30700  -5.62500  -1.40800  1.000 8.76071  ?  10  PRO   A O    1 
ATOM   30   C CB   . PRO   A 1 13  ? -5.82100  -8.29900  -1.65100  1.000 15.42446 ?  10  PRO   A CB   1 
ATOM   31   C CG   . PRO   A 1 13  ? -4.33000  -8.35400  -1.57300  1.000 19.78078 ?  10  PRO   A CG   1 
ATOM   32   C CD   . PRO   A 1 13  ? -3.81000  -7.00900  -1.99500  1.000 11.67085 ?  10  PRO   A CD   1 
ATOM   33   N N    . GLU   A 1 14  ? -8.44600  -6.63800  -3.06200  1.000 12.83235 ?  11  GLU   A N    1 
ATOM   34   C CA   . GLU   A 1 14  ? -9.65600  -5.85600  -2.82700  1.000 10.66530 ?  11  GLU   A CA   1 
ATOM   35   C C    . GLU   A 1 14  ? -10.12400 -5.93900  -1.38200  1.000 13.72570 ?  11  GLU   A C    1 
ATOM   36   O O    . GLU   A 1 14  ? -10.63200 -4.95500  -0.83200  1.000 8.52679  ?  11  GLU   A O    1 
ATOM   37   C CB   . GLU   A 1 14  ? -10.75600 -6.34900  -3.76200  1.000 15.00406 ?  11  GLU   A CB   1 
ATOM   38   C CG   . GLU   A 1 14  ? -11.96100 -5.46100  -3.78900  1.000 20.07251 ?  11  GLU   A CG   1 
ATOM   39   C CD   . GLU   A 1 14  ? -13.04900 -6.05800  -4.64500  1.000 27.95219 ?  11  GLU   A CD   1 
ATOM   40   O OE1  . GLU   A 1 14  ? -12.73600 -6.41300  -5.80300  1.000 21.32545 ?  11  GLU   A OE1  1 
ATOM   41   O OE2  . GLU   A 1 14  ? -14.19700 -6.16200  -4.16500  1.000 27.67537 -1 11  GLU   A OE2  1 
ATOM   42   N N    . GLN   A 1 15  ? -9.97600  -7.10600  -0.74200  1.000 10.58835 ?  12  GLN   A N    1 
ATOM   43   C CA   . GLN   A 1 15  ? -10.42700 -7.23000  0.64000   1.000 10.73813 ?  12  GLN   A CA   1 
ATOM   44   C C    . GLN   A 1 15  ? -9.76200  -6.21200  1.55000   1.000 10.07885 ?  12  GLN   A C    1 
ATOM   45   O O    . GLN   A 1 15  ? -10.35800 -5.79500  2.54900   1.000 12.83424 ?  12  GLN   A O    1 
ATOM   46   C CB   . GLN   A 1 15  ? -10.15700 -8.63900  1.16800   1.000 14.80026 ?  12  GLN   A CB   1 
ATOM   47   C CG   . GLN   A 1 15  ? -10.75000 -8.92800  2.54400   1.000 13.60692 ?  12  GLN   A CG   1 
ATOM   48   C CD   . GLN   A 1 15  ? -12.27900 -9.08700  2.53100   1.000 11.70336 ?  12  GLN   A CD   1 
ATOM   49   O OE1  . GLN   A 1 15  ? -12.92800 -8.95500  1.48400   1.000 16.68646 ?  12  GLN   A OE1  1 
ATOM   50   N NE2  . GLN   A 1 15  ? -12.84300 -9.41600  3.69100   1.000 20.35861 ?  12  GLN   A NE2  1 
ATOM   51   N N    . LEU   A 1 16  ? -8.53200  -5.79500  1.22400   1.000 9.94245  ?  13  LEU   A N    1 
ATOM   52   C CA   . LEU   A 1 16  ? -7.78500  -4.87300  2.07200   1.000 7.04911  ?  13  LEU   A CA   1 
ATOM   53   C C    . LEU   A 1 16  ? -8.08900  -3.42100  1.73200   1.000 6.83107  ?  13  LEU   A C    1 
ATOM   54   O O    . LEU   A 1 16  ? -7.57300  -2.50800  2.38400   1.000 8.24757  ?  13  LEU   A O    1 
ATOM   55   C CB   . LEU   A 1 16  ? -6.27800  -5.14800  1.93300   1.000 6.88702  ?  13  LEU   A CB   1 
ATOM   56   C CG   . LEU   A 1 16  ? -5.87000  -6.58900  2.25300   1.000 11.49297 ?  13  LEU   A CG   1 
ATOM   57   C CD1  . LEU   A 1 16  ? -4.35300  -6.74500  2.09000   1.000 15.24410 ?  13  LEU   A CD1  1 
ATOM   58   C CD2  . LEU   A 1 16  ? -6.33600  -7.02800  3.64900   1.000 15.49304 ?  13  LEU   A CD2  1 
ATOM   59   N N    . ARG   A 1 17  ? -8.94900  -3.19100  0.74500   1.000 6.89309  ?  14  ARG   A N    1 
ATOM   60   C CA   . ARG   A 1 17  ? -9.31800  -1.85200  0.31300   1.000 7.17309  ?  14  ARG   A CA   1 
ATOM   61   C C    . ARG   A 1 17  ? -10.75600 -1.51500  0.68400   1.000 5.56667  ?  14  ARG   A C    1 
ATOM   62   O O    . ARG   A 1 17  ? -11.25600 -0.45200  0.28500   1.000 6.72089  ?  14  ARG   A O    1 
ATOM   63   C CB   . ARG   A 1 17  ? -9.11000  -1.73700  -1.20700  1.000 5.67271  ?  14  ARG   A CB   1 
ATOM   64   C CG   . ARG   A 1 17  ? -7.63000  -1.72600  -1.54400  1.000 9.87740  ?  14  ARG   A CG   1 
ATOM   65   C CD   . ARG   A 1 17  ? -7.33800  -1.54400  -2.99900  1.000 9.97481  ?  14  ARG   A CD   1 
ATOM   66   N NE   . ARG   A 1 17  ? -7.57300  -2.75400  -3.77900  1.000 11.66065 ?  14  ARG   A NE   1 
ATOM   67   C CZ   . ARG   A 1 17  ? -8.54700  -2.88100  -4.67000  1.000 19.00178 ?  14  ARG   A CZ   1 
ATOM   68   N NH1  . ARG   A 1 17  ? -9.46300  -1.93900  -4.82500  1.000 15.16902 ?  14  ARG   A NH1  1 
ATOM   69   N NH2  . ARG   A 1 17  ? -8.61100  -3.99100  -5.41100  1.000 17.71570 ?  14  ARG   A NH2  1 
ATOM   70   N N    . LYS   A 1 18  ? -11.42700 -2.39300  1.43100   1.000 7.30729  ?  15  LYS   A N    1 
ATOM   71   C CA   . LYS   A 1 18  ? -12.84800 -2.26100  1.75900   1.000 7.57513  ?  15  LYS   A CA   1 
ATOM   72   C C    . LYS   A 1 18  ? -13.03700 -1.70600  3.16100   1.000 12.20872 ?  15  LYS   A C    1 
ATOM   73   O O    . LYS   A 1 18  ? -12.32700 -2.09300  4.09800   1.000 14.60831 ?  15  LYS   A O    1 
ATOM   74   C CB   . LYS   A 1 18  ? -13.54500 -3.61600  1.70800   1.000 12.47188 ?  15  LYS   A CB   1 
ATOM   75   C CG   . LYS   A 1 18  ? -13.84400 -4.18000  0.36400   1.000 20.76594 ?  15  LYS   A CG   1 
ATOM   76   C CD   . LYS   A 1 18  ? -14.50400 -5.54600  0.57900   1.000 22.96361 ?  15  LYS   A CD   1 
ATOM   77   C CE   . LYS   A 1 18  ? -14.40800 -6.41700  -0.67500  1.000 31.48088 ?  15  LYS   A CE   1 
ATOM   78   N NZ   . LYS   A 1 18  ? -14.93700 -7.80000  -0.42700  1.000 30.00016 ?  15  LYS   A NZ   1 
ATOM   79   N N    . LEU   A 1 19  ? -14.04500 -0.85800  3.32800   1.000 6.70653  ?  16  LEU   A N    1 
ATOM   80   C CA   . LEU   A 1 19  ? -14.47500 -0.46400  4.66000   1.000 6.95777  ?  16  LEU   A CA   1 
ATOM   81   C C    . LEU   A 1 19  ? -15.92700 -0.86800  4.83800   1.000 9.34656  ?  16  LEU   A C    1 
ATOM   82   O O    . LEU   A 1 19  ? -16.76400 -0.55800  3.97300   1.000 7.47124  ?  16  LEU   A O    1 
ATOM   83   C CB   . LEU   A 1 19  ? -14.33900 1.04200   4.85400   1.000 11.33865 ?  16  LEU   A CB   1 
ATOM   84   C CG   . LEU   A 1 19  ? -12.92100 1.54400   5.07900   1.000 9.09296  ?  16  LEU   A CG   1 
ATOM   85   C CD1  . LEU   A 1 19  ? -12.98300 3.05300   5.28200   1.000 12.05817 ?  16  LEU   A CD1  1 
ATOM   86   C CD2  . LEU   A 1 19  ? -12.25900 0.87800   6.27200   1.000 7.65275  ?  16  LEU   A CD2  1 
ATOM   87   N N    . PHE   A 1 20  ? -16.20100 -1.60900  5.91300   1.000 7.83213  ?  17  PHE   A N    1 
ATOM   88   C CA   . PHE   A 1 20  ? -17.56400 -1.79100  6.39600   1.000 8.11885  ?  17  PHE   A CA   1 
ATOM   89   C C    . PHE   A 1 20  ? -17.96800 -0.51900  7.12900   1.000 9.04555  ?  17  PHE   A C    1 
ATOM   90   O O    . PHE   A 1 20  ? -17.22600 -0.02400  7.98500   1.000 10.58083 ?  17  PHE   A O    1 
ATOM   91   C CB   . PHE   A 1 20  ? -17.64900 -3.00600  7.32300   1.000 13.86259 ?  17  PHE   A CB   1 
ATOM   92   C CG   . PHE   A 1 20  ? -18.80100 -2.96000  8.30400   1.000 19.77642 ?  17  PHE   A CG   1 
ATOM   93   C CD1  . PHE   A 1 20  ? -18.69200 -2.29200  9.51900   1.000 20.73188 ?  17  PHE   A CD1  1 
ATOM   94   C CD2  . PHE   A 1 20  ? -20.00000 -3.57800  7.99400   1.000 16.65395 ?  17  PHE   A CD2  1 
ATOM   95   C CE1  . PHE   A 1 20  ? -19.75300 -2.25400  10.40700  1.000 19.26506 ?  17  PHE   A CE1  1 
ATOM   96   C CE2  . PHE   A 1 20  ? -21.07300 -3.53200  8.88500   1.000 11.81918 ?  17  PHE   A CE2  1 
ATOM   97   C CZ   . PHE   A 1 20  ? -20.94500 -2.87000  10.08100  1.000 16.58723 ?  17  PHE   A CZ   1 
ATOM   98   H HA   . PHE   A 1 20  ? -18.17700 -1.95200  5.66200   1.000 9.74262  ?  17  PHE   A HA   1 
ATOM   99   H HB2  . PHE   A 1 20  ? -17.75600 -3.80200  6.78000   1.000 16.63511 ?  17  PHE   A HB2  1 
ATOM   100  H HB3  . PHE   A 1 20  ? -16.82800 -3.06200  7.83600   1.000 16.63511 ?  17  PHE   A HB3  1 
ATOM   101  H HD1  . PHE   A 1 20  ? -17.89500 -1.86500  9.73900   1.000 24.87826 ?  17  PHE   A HD1  1 
ATOM   102  H HD2  . PHE   A 1 20  ? -20.09100 -4.02800  7.18500   1.000 19.98474 ?  17  PHE   A HD2  1 
ATOM   103  H HE1  . PHE   A 1 20  ? -19.66400 -1.81400  11.22100  1.000 23.11808 ?  17  PHE   A HE1  1 
ATOM   104  H HE2  . PHE   A 1 20  ? -21.87500 -3.94900  8.66800   1.000 14.18302 ?  17  PHE   A HE2  1 
ATOM   105  H HZ   . PHE   A 1 20  ? -21.66100 -2.83700  10.67300  1.000 19.90468 ?  17  PHE   A HZ   1 
ATOM   106  N N    . ILE   A 1 21  ? -19.13300 0.02500   6.80100   1.000 7.49715  ?  18  ILE   A N    1 
ATOM   107  C CA   . ILE   A 1 21  ? -19.60900 1.25200   7.44400   1.000 6.19679  ?  18  ILE   A CA   1 
ATOM   108  C C    . ILE   A 1 21  ? -20.87800 0.90400   8.20000   1.000 9.28485  ?  18  ILE   A C    1 
ATOM   109  O O    . ILE   A 1 21  ? -21.92300 0.67300   7.58600   1.000 9.11511  ?  18  ILE   A O    1 
ATOM   110  C CB   . ILE   A 1 21  ? -19.87800 2.39000   6.44900   1.000 9.73437  ?  18  ILE   A CB   1 
ATOM   111  C CG1  . ILE   A 1 21  ? -18.77500 2.52400   5.38700   1.000 11.71051 ?  18  ILE   A CG1  1 
ATOM   112  C CG2  . ILE   A 1 21  ? -20.15600 3.70000   7.21900   1.000 10.08719 ?  18  ILE   A CG2  1 
ATOM   113  C CD1  . ILE   A 1 21  ? -17.47200 3.07300   5.90000   1.000 13.21185 ?  18  ILE   A CD1  1 
ATOM   114  N N    . GLY   A 1 22  ? -20.79300 0.88300   9.52300   1.000 9.26593  ?  19  GLY   A N    1 
ATOM   115  C CA   . GLY   A 1 22  ? -21.93200 0.59100   10.37000  1.000 7.96606  ?  19  GLY   A CA   1 
ATOM   116  C C    . GLY   A 1 22  ? -22.60000 1.86400   10.86300  1.000 6.97537  ?  19  GLY   A C    1 
ATOM   117  O O    . GLY   A 1 22  ? -22.03400 2.95400   10.81800  1.000 9.51486  ?  19  GLY   A O    1 
ATOM   118  N N    . GLY   A 1 23  ? -23.82600 1.70600   11.36400  1.000 7.80409  ?  20  GLY   A N    1 
ATOM   119  C CA   . GLY   A 1 23  ? -24.51300 2.81900   11.98300  1.000 8.75629  ?  20  GLY   A CA   1 
ATOM   120  C C    . GLY   A 1 23  ? -25.04900 3.85300   11.01600  1.000 8.01412  ?  20  GLY   A C    1 
ATOM   121  O O    . GLY   A 1 23  ? -25.20100 5.02100   11.38200  1.000 12.29565 ?  20  GLY   A O    1 
ATOM   122  N N    . LEU   A 1 24  ? -25.35000 3.45500   9.78500   1.000 7.34796  ?  21  LEU   A N    1 
ATOM   123  C CA   . LEU   A 1 24  ? -25.82900 4.39500   8.78900   1.000 7.18892  ?  21  LEU   A CA   1 
ATOM   124  C C    . LEU   A 1 24  ? -27.19000 4.93300   9.18900   1.000 8.55742  ?  21  LEU   A C    1 
ATOM   125  O O    . LEU   A 1 24  ? -28.01500 4.23000   9.78700   1.000 11.09495 ?  21  LEU   A O    1 
ATOM   126  C CB   . LEU   A 1 24  ? -25.98000 3.69500   7.44600   1.000 7.57487  ?  21  LEU   A CB   1 
ATOM   127  C CG   . LEU   A 1 24  ? -24.69000 3.31900   6.73400   1.000 6.32172  ?  21  LEU   A CG   1 
ATOM   128  C CD1  . LEU   A 1 24  ? -25.06000 2.72100   5.35500   1.000 7.13872  ?  21  LEU   A CD1  1 
ATOM   129  C CD2  . LEU   A 1 24  ? -23.70800 4.49600   6.58700   1.000 10.58260 ?  21  LEU   A CD2  1 
ATOM   130  N N    . SER   A 1 25  ? -27.43800 6.17300   8.81800   1.000 7.23044  ?  22  SER   A N    1 
ATOM   131  C CA   . SER   A 1 25  ? -28.81400 6.64300   8.77200   1.000 8.66615  ?  22  SER   A CA   1 
ATOM   132  C C    . SER   A 1 25  ? -29.57900 5.82500   7.73700   1.000 11.51423 ?  22  SER   A C    1 
ATOM   133  O O    . SER   A 1 25  ? -29.07200 5.53100   6.65300   1.000 8.67063  ?  22  SER   A O    1 
ATOM   134  C CB   . SER   A 1 25  ? -28.86200 8.12200   8.39800   1.000 11.79452 ?  22  SER   A CB   1 
ATOM   135  O OG   . SER   A 1 25  ? -30.16100 8.47400   7.90900   1.000 12.67454 ?  22  SER   A OG   1 
ATOM   136  N N    . PHE   A 1 26  ? -30.81400 5.46600   8.06400   1.000 10.56442 ?  23  PHE   A N    1 
ATOM   137  C CA   . PHE   A 1 26  ? -31.59700 4.69500   7.11000   1.000 8.90361  ?  23  PHE   A CA   1 
ATOM   138  C C    . PHE   A 1 26  ? -31.86800 5.47000   5.83000   1.000 10.78920 ?  23  PHE   A C    1 
ATOM   139  O O    . PHE   A 1 26  ? -32.26200 4.86100   4.82200   1.000 12.50170 ?  23  PHE   A O    1 
ATOM   140  C CB   . PHE   A 1 26  ? -32.92900 4.27100   7.74500   1.000 11.12849 ?  23  PHE   A CB   1 
ATOM   141  C CG   . PHE   A 1 26  ? -32.80600 3.20000   8.80300   1.000 11.25103 ?  23  PHE   A CG   1 
ATOM   142  C CD1  . PHE   A 1 26  ? -31.57500 2.69900   9.20900   1.000 11.97111 ?  23  PHE   A CD1  1 
ATOM   143  C CD2  . PHE   A 1 26  ? -33.95300 2.68200   9.39700   1.000 12.52526 ?  23  PHE   A CD2  1 
ATOM   144  C CE1  . PHE   A 1 26  ? -31.49600 1.72500   10.19400  1.000 12.17612 ?  23  PHE   A CE1  1 
ATOM   145  C CE2  . PHE   A 1 26  ? -33.87300 1.70400   10.36600  1.000 13.07856 ?  23  PHE   A CE2  1 
ATOM   146  C CZ   . PHE   A 1 26  ? -32.64300 1.23700   10.78100  1.000 14.04713 ?  23  PHE   A CZ   1 
ATOM   147  N N    . GLU   A 1 27  ? -31.64700 6.78700   5.82800   1.000 13.07549 ?  24  GLU   A N    1 
ATOM   148  C CA   . GLU   A 1 27  ? -31.84400 7.58500   4.62700   1.000 11.75828 ?  24  GLU   A CA   1 
ATOM   149  C C    . GLU   A 1 27  ? -30.59800 7.67100   3.75400   1.000 9.51861  ?  24  GLU   A C    1 
ATOM   150  O O    . GLU   A 1 27  ? -30.67400 8.19800   2.64200   1.000 10.77156 ?  24  GLU   A O    1 
ATOM   151  C CB   . GLU   A 1 27  ? -32.32700 8.98300   5.00800   1.000 14.93745 ?  24  GLU   A CB   1 
ATOM   152  C CG   . GLU   A 1 27  ? -33.82400 9.02500   5.40000   1.000 28.92014 ?  24  GLU   A CG   1 
ATOM   153  C CD   . GLU   A 1 27  ? -34.14100 8.22200   6.66600   1.000 37.52617 ?  24  GLU   A CD   1 
ATOM   154  O OE1  . GLU   A 1 27  ? -33.47400 8.44500   7.70500   1.000 29.59909 ?  24  GLU   A OE1  1 
ATOM   155  O OE2  . GLU   A 1 27  ? -35.06100 7.36400   6.62300   1.000 33.62925 ?  24  GLU   A OE2  1 
ATOM   156  N N    . THR   A 1 28  ? -29.47100 7.12900   4.20200   1.000 6.79054  ?  25  THR   A N    1 
ATOM   157  C CA   . THR   A 1 28  ? -28.28200 7.12400   3.36600   1.000 7.54280  ?  25  THR   A CA   1 
ATOM   158  C C    . THR   A 1 28  ? -28.46400 6.17100   2.19000   1.000 9.59402  ?  25  THR   A C    1 
ATOM   159  O O    . THR   A 1 28  ? -28.99100 5.06400   2.33600   1.000 9.26123  ?  25  THR   A O    1 
ATOM   160  C CB   . THR   A 1 28  ? -27.05900 6.72800   4.19900   1.000 6.59972  ?  25  THR   A CB   1 
ATOM   161  O OG1  . THR   A 1 28  ? -26.80500 7.75900   5.17400   1.000 8.32132  ?  25  THR   A OG1  1 
ATOM   162  C CG2  . THR   A 1 28  ? -25.79800 6.50700   3.31900   1.000 9.09609  ?  25  THR   A CG2  1 
ATOM   163  N N    . THR   A 1 29  ? -28.01800 6.61200   1.02100   1.000 8.52727  ?  26  THR   A N    1 
ATOM   164  C CA   . THR   A 1 29  ? -28.15100 5.87600   -0.23000  1.000 5.75699  ?  26  THR   A CA   1 
ATOM   165  C C    . THR   A 1 29  ? -26.77300 5.53700   -0.77200  1.000 10.83297 ?  26  THR   A C    1 
ATOM   166  O O    . THR   A 1 29  ? -25.75700 6.06800   -0.31300  1.000 9.41385  ?  26  THR   A O    1 
ATOM   167  C CB   . THR   A 1 29  ? -28.91900 6.70200   -1.26500  1.000 10.49748 ?  26  THR   A CB   1 
ATOM   168  O OG1  . THR   A 1 29  ? -28.17600 7.90200   -1.53400  1.000 11.83078 ?  26  THR   A OG1  1 
ATOM   169  C CG2  . THR   A 1 29  ? -30.33500 7.04500   -0.76600  1.000 9.75926  ?  26  THR   A CG2  1 
ATOM   170  N N    . ASP   A 1 30  ? -26.74800 4.63500   -1.75600  1.000 8.38138  ?  27  ASP   A N    1 
ATOM   171  C CA   . ASP   A 1 30  ? -25.50800 4.38600   -2.49000  1.000 8.62588  ?  27  ASP   A CA   1 
ATOM   172  C C    . ASP   A 1 30  ? -24.86600 5.70200   -2.88900  1.000 8.37836  ?  27  ASP   A C    1 
ATOM   173  O O    . ASP   A 1 30  ? -23.65300 5.89200   -2.74900  1.000 8.09658  ?  27  ASP   A O    1 
ATOM   174  C CB   . ASP   A 1 30  ? -25.76300 3.56500   -3.76100  1.000 9.71494  ?  27  ASP   A CB   1 
ATOM   175  C CG   . ASP   A 1 30  ? -26.09400 2.10500   -3.49900  1.000 16.14318 ?  27  ASP   A CG   1 
ATOM   176  O OD1  . ASP   A 1 30  ? -26.19000 1.68200   -2.33500  1.000 14.56259 ?  27  ASP   A OD1  1 
ATOM   177  O OD2  . ASP   A 1 30  ? -26.27600 1.36800   -4.50000  1.000 19.40489 -1 27  ASP   A OD2  1 
ATOM   178  N N    . GLU   A 1 31  ? -25.67900 6.62600   -3.38100  1.000 10.65342 ?  28  GLU   A N    1 
ATOM   179  C CA   . GLU   A 1 31  ? -25.14800 7.86600   -3.91600  1.000 9.06664  ?  28  GLU   A CA   1 
ATOM   180  C C    . GLU   A 1 31  ? -24.64000 8.78100   -2.80900  1.000 7.29934  ?  28  GLU   A C    1 
ATOM   181  O O    . GLU   A 1 31  ? -23.58500 9.40600   -2.95800  1.000 9.03527  ?  28  GLU   A O    1 
ATOM   182  C CB   . GLU   A 1 31  ? -26.22200 8.57100   -4.74100  1.000 14.41132 ?  28  GLU   A CB   1 
ATOM   183  C CG   . GLU   A 1 31  ? -26.60100 7.83100   -6.01800  1.000 16.44714 ?  28  GLU   A CG   1 
ATOM   184  C CD   . GLU   A 1 31  ? -27.39500 6.54300   -5.75900  1.000 31.80648 ?  28  GLU   A CD   1 
ATOM   185  O OE1  . GLU   A 1 31  ? -28.16500 6.48000   -4.76200  1.000 21.08738 ?  28  GLU   A OE1  1 
ATOM   186  O OE2  . GLU   A 1 31  ? -27.25200 5.59600   -6.56500  1.000 36.12682 -1 28  GLU   A OE2  1 
ATOM   187  N N    . SER   A 1 32  ? -25.37100 8.89800   -1.69700  1.000 6.73729  ?  29  SER   A N    1 
ATOM   188  C CA   . SER   A 1 32  ? -24.91000 9.81100   -0.65400  1.000 7.44417  ?  29  SER   A CA   1 
ATOM   189  C C    . SER   A 1 32  ? -23.73700 9.22600   0.12800   1.000 9.36241  ?  29  SER   A C    1 
ATOM   190  O O    . SER   A 1 32  ? -22.83600 9.96500   0.56300   1.000 7.54664  ?  29  SER   A O    1 
ATOM   191  C CB   . SER   A 1 32  ? -26.06900 10.19600  0.27300   1.000 8.08952  ?  29  SER   A CB   1 
ATOM   192  O OG   . SER   A 1 32  ? -26.43200 9.14900   1.14600   1.000 9.32264  ?  29  SER   A OG   1 
ATOM   193  N N    . LEU   A 1 33  ? -23.70000 7.90500   0.27800   1.000 6.71972  ?  30  LEU   A N    1 
ATOM   194  C CA   . LEU   A 1 33  ? -22.52200 7.29200   0.88700   1.000 5.29351  ?  30  LEU   A CA   1 
ATOM   195  C C    . LEU   A 1 33  ? -21.29600 7.51700   0.01700   1.000 5.23356  ?  30  LEU   A C    1 
ATOM   196  O O    . LEU   A 1 33  ? -20.19900 7.78400   0.52700   1.000 6.79280  ?  30  LEU   A O    1 
ATOM   197  C CB   . LEU   A 1 33  ? -22.77300 5.79400   1.08400   1.000 6.46876  ?  30  LEU   A CB   1 
ATOM   198  C CG   . LEU   A 1 33  ? -21.73800 4.99500   1.88900   1.000 6.62007  ?  30  LEU   A CG   1 
ATOM   199  C CD1  . LEU   A 1 33  ? -21.65800 5.53100   3.28900   1.000 6.67824  ?  30  LEU   A CD1  1 
ATOM   200  C CD2  . LEU   A 1 33  ? -22.14200 3.52000   1.90100   1.000 8.19551  ?  30  LEU   A CD2  1 
ATOM   201  N N    . ARG   A 1 34  ? -21.45600 7.37200   -1.30100  1.000 4.10682  ?  31  ARG   A N    1 
ATOM   202  C CA   . ARG   A 1 34  ? -20.34800 7.58100   -2.22800  1.000 4.90390  ?  31  ARG   A CA   1 
ATOM   203  C C    . ARG   A 1 34  ? -19.88100 9.02900   -2.21400  1.000 6.13233  ?  31  ARG   A C    1 
ATOM   204  O O    . ARG   A 1 34  ? -18.67800 9.30200   -2.14500  1.000 7.93121  ?  31  ARG   A O    1 
ATOM   205  C CB   . ARG   A 1 34  ? -20.76900 7.17800   -3.65300  1.000 8.46197  ?  31  ARG   A CB   1 
ATOM   206  C CG   . ARG   A 1 34  ? -19.74800 7.58800   -4.74000  1.000 9.91352  ?  31  ARG   A CG   1 
ATOM   207  C CD   . ARG   A 1 34  ? -20.14500 7.03600   -6.12900  1.000 10.05417 ?  31  ARG   A CD   1 
ATOM   208  N NE   . ARG   A 1 34  ? -19.90000 5.60100   -6.26100  1.000 10.65100 ?  31  ARG   A NE   1 
ATOM   209  C CZ   . ARG   A 1 34  ? -18.73100 5.06300   -6.59600  1.000 12.83525 ?  31  ARG   A CZ   1 
ATOM   210  N NH1  . ARG   A 1 34  ? -17.66800 5.81200   -6.84900  1.000 13.57857 ?  31  ARG   A NH1  1 
ATOM   211  N NH2  . ARG   A 1 34  ? -18.61900 3.73800   -6.65900  1.000 14.45666 ?  31  ARG   A NH2  1 
ATOM   212  N N    . SER   A 1 35  ? -20.81900 9.98100   -2.31000  1.000 6.83432  ?  32  SER   A N    1 
ATOM   213  C CA   . SER   A 1 35  ? -20.42400 11.38700  -2.28500  1.000 10.28238 ?  32  SER   A CA   1 
ATOM   214  C C    . SER   A 1 35  ? -19.61100 11.70900  -1.04500  1.000 12.91358 ?  32  SER   A C    1 
ATOM   215  O O    . SER   A 1 35  ? -18.60300 12.43000  -1.12200  1.000 12.79306 ?  32  SER   A O    1 
ATOM   216  C CB   . SER   A 1 35  ? -21.65500 12.28200  -2.35700  1.000 10.40514 ?  32  SER   A CB   1 
ATOM   217  O OG   . SER   A 1 35  ? -22.16300 12.24800  -3.67200  1.000 16.84323 ?  32  SER   A OG   1 
ATOM   218  N N    . HIS   A 1 36  ? -20.00400 11.15600  0.10200   1.000 8.21452  ?  33  HIS   A N    1 
ATOM   219  C CA   . HIS   A 1 36  ? -19.25100 11.39100  1.32300   1.000 7.63147  ?  33  HIS   A CA   1 
ATOM   220  C C    . HIS   A 1 36  ? -17.84400 10.80400  1.23100   1.000 9.10749  ?  33  HIS   A C    1 
ATOM   221  O O    . HIS   A 1 36  ? -16.84900 11.52100  1.35800   1.000 8.26957  ?  33  HIS   A O    1 
ATOM   222  C CB   . HIS   A 1 36  ? -19.96700 10.80300  2.53500   1.000 6.72905  ?  33  HIS   A CB   1 
ATOM   223  C CG   . HIS   A 1 36  ? -19.22100 11.05400  3.79700   1.000 6.79927  ?  33  HIS   A CG   1 
ATOM   224  N ND1  . HIS   A 1 36  ? -19.41300 12.18900  4.55400   1.000 13.34056 ?  33  HIS   A ND1  1 
ATOM   225  C CD2  . HIS   A 1 36  ? -18.22000 10.36300  4.39500   1.000 5.76154  ?  33  HIS   A CD2  1 
ATOM   226  C CE1  . HIS   A 1 36  ? -18.59100 12.16500  5.58800   1.000 15.08152 ?  33  HIS   A CE1  1 
ATOM   227  N NE2  . HIS   A 1 36  ? -17.85700 11.06800  5.51500   1.000 11.26154 ?  33  HIS   A NE2  1 
ATOM   228  N N    . PHE   A 1 37  ? -17.73700 9.49700   1.00400   1.000 7.02774  ?  34  PHE   A N    1 
ATOM   229  C CA   . PHE   A 1 37  ? -16.43200 8.86500   1.13800   1.000 7.69729  ?  34  PHE   A CA   1 
ATOM   230  C C    . PHE   A 1 37  ? -15.50400 9.11800   -0.04900  1.000 7.19311  ?  34  PHE   A C    1 
ATOM   231  O O    . PHE   A 1 37  ? -14.29500 8.91400   0.08500   1.000 7.94131  ?  34  PHE   A O    1 
ATOM   232  C CB   . PHE   A 1 37  ? -16.63300 7.36200   1.43900   1.000 5.78682  ?  34  PHE   A CB   1 
ATOM   233  C CG   . PHE   A 1 37  ? -16.92300 7.12200   2.90900   1.000 5.96196  ?  34  PHE   A CG   1 
ATOM   234  C CD1  . PHE   A 1 37  ? -15.92000 7.27500   3.83500   1.000 5.65377  ?  34  PHE   A CD1  1 
ATOM   235  C CD2  . PHE   A 1 37  ? -18.21500 6.88600   3.35900   1.000 6.97324  ?  34  PHE   A CD2  1 
ATOM   236  C CE1  . PHE   A 1 37  ? -16.16400 7.13400   5.20000   1.000 8.01862  ?  34  PHE   A CE1  1 
ATOM   237  C CE2  . PHE   A 1 37  ? -18.49400 6.74000   4.72000   1.000 7.26863  ?  34  PHE   A CE2  1 
ATOM   238  C CZ   . PHE   A 1 37  ? -17.46100 6.86400   5.65300   1.000 6.00162  ?  34  PHE   A CZ   1 
ATOM   239  N N    . GLU   A 1 38  ? -16.01700 9.60800   -1.18100  1.000 8.26599  ?  35  GLU   A N    1 
ATOM   240  C CA   . GLU   A 1 38  ? -15.11900 10.01700  -2.26100  1.000 9.19024  ?  35  GLU   A CA   1 
ATOM   241  C C    . GLU   A 1 38  ? -14.21900 11.17900  -1.87000  1.000 8.20796  ?  35  GLU   A C    1 
ATOM   242  O O    . GLU   A 1 38  ? -13.26400 11.47300  -2.60300  1.000 9.62820  ?  35  GLU   A O    1 
ATOM   243  C CB   . GLU   A 1 38  ? -15.92700 10.40000  -3.50200  1.000 11.53492 ?  35  GLU   A CB   1 
ATOM   244  C CG   . GLU   A 1 38  ? -16.26100 9.21000   -4.36600  1.000 14.43248 ?  35  GLU   A CG   1 
ATOM   245  C CD   . GLU   A 1 38  ? -17.15900 9.59300   -5.54400  1.000 11.39847 ?  35  GLU   A CD   1 
ATOM   246  O OE1  . GLU   A 1 38  ? -17.82000 10.67600  -5.49600  1.000 16.52223 ?  35  GLU   A OE1  1 
ATOM   247  O OE2  . GLU   A 1 38  ? -17.18500 8.80400   -6.50700  1.000 12.02203 -1 35  GLU   A OE2  1 
ATOM   248  N N    . GLN   A 1 39  ? -14.48600 11.84800  -0.74900  1.000 7.68103  ?  36  GLN   A N    1 
ATOM   249  C CA   . GLN   A 1 39  ? -13.58600 12.92200  -0.33600  1.000 8.50483  ?  36  GLN   A CA   1 
ATOM   250  C C    . GLN   A 1 39  ? -12.20200 12.39900  0.00900   1.000 11.23801 ?  36  GLN   A C    1 
ATOM   251  O O    . GLN   A 1 39  ? -11.24600 13.18200  0.01700   1.000 12.08672 ?  36  GLN   A O    1 
ATOM   252  C CB   . GLN   A 1 39  ? -14.14000 13.67100  0.86700   1.000 9.47110  ?  36  GLN   A CB   1 
ATOM   253  C CG   . GLN   A 1 39  ? -15.41200 14.41700  0.60300   1.000 11.84013 ?  36  GLN   A CG   1 
ATOM   254  C CD   . GLN   A 1 39  ? -15.92200 15.03300  1.86600   1.000 20.81276 ?  36  GLN   A CD   1 
ATOM   255  O OE1  . GLN   A 1 39  ? -15.38400 16.03300  2.34400   1.000 19.05050 ?  36  GLN   A OE1  1 
ATOM   256  N NE2  . GLN   A 1 39  ? -16.94100 14.41000  2.45500   1.000 21.49082 ?  36  GLN   A NE2  1 
ATOM   257  N N    . TRP   A 1 40  ? -12.06100 11.10600  0.31900   1.000 8.23028  ?  37  TRP   A N    1 
ATOM   258  C CA   . TRP   A 1 40  ? -10.75700 10.57700  0.71900   1.000 8.52107  ?  37  TRP   A CA   1 
ATOM   259  C C    . TRP   A 1 40  ? -10.15400 9.59800   -0.28000  1.000 7.91702  ?  37  TRP   A C    1 
ATOM   260  O O    . TRP   A 1 40  ? -9.09100  9.03100   -0.00900  1.000 9.12972  ?  37  TRP   A O    1 
ATOM   261  C CB   . TRP   A 1 40  ? -10.84100 9.94900   2.11400   1.000 8.25814  ?  37  TRP   A CB   1 
ATOM   262  C CG   . TRP   A 1 40  ? -11.16700 11.04400  3.07500   1.000 8.81944  ?  37  TRP   A CG   1 
ATOM   263  C CD1  . TRP   A 1 40  ? -10.29300 11.93700  3.62500   1.000 5.69582  ?  37  TRP   A CD1  1 
ATOM   264  C CD2  . TRP   A 1 40  ? -12.47000 11.43800  3.50300   1.000 10.43896 ?  37  TRP   A CD2  1 
ATOM   265  N NE1  . TRP   A 1 40  ? -10.96700 12.84400  4.40200   1.000 10.54574 ?  37  TRP   A NE1  1 
ATOM   266  C CE2  . TRP   A 1 40  ? -12.30800 12.55800  4.34800   1.000 9.65581  ?  37  TRP   A CE2  1 
ATOM   267  C CE3  . TRP   A 1 40  ? -13.75700 10.94300  3.27200   1.000 9.67285  ?  37  TRP   A CE3  1 
ATOM   268  C CZ2  . TRP   A 1 40  ? -13.38400 13.19600  4.95700   1.000 11.96067 ?  37  TRP   A CZ2  1 
ATOM   269  C CZ3  . TRP   A 1 40  ? -14.83700 11.58000  3.88500   1.000 11.26068 ?  37  TRP   A CZ3  1 
ATOM   270  C CH2  . TRP   A 1 40  ? -14.63900 12.69700  4.72200   1.000 9.88514  ?  37  TRP   A CH2  1 
ATOM   271  N N    . GLY   A 1 41  ? -10.76400 9.41100   -1.44000  1.000 8.73302  ?  38  GLY   A N    1 
ATOM   272  C CA   . GLY   A 1 41  ? -10.12200 8.60700   -2.45600  1.000 8.05364  ?  38  GLY   A CA   1 
ATOM   273  C C    . GLY   A 1 41  ? -11.11200 8.17600   -3.50900  1.000 6.60027  ?  38  GLY   A C    1 
ATOM   274  O O    . GLY   A 1 41  ? -12.31800 8.45000   -3.42400  1.000 10.04902 ?  38  GLY   A O    1 
ATOM   275  N N    . THR   A 1 42  ? -10.57000 7.50200   -4.51800  1.000 7.31793  ?  39  THR   A N    1 
ATOM   276  C CA   . THR   A 1 42  ? -11.38800 6.94300   -5.59000  1.000 8.50488  ?  39  THR   A CA   1 
ATOM   277  C C    . THR   A 1 42  ? -12.12800 5.71100   -5.08500  1.000 8.68060  ?  39  THR   A C    1 
ATOM   278  O O    . THR   A 1 42  ? -11.51600 4.80900   -4.51600  1.000 9.08935  ?  39  THR   A O    1 
ATOM   279  C CB   . THR   A 1 42  ? -10.49100 6.57400   -6.76900  1.000 13.49046 ?  39  THR   A CB   1 
ATOM   280  O OG1  . THR   A 1 42  ? -9.86800  7.76500   -7.27200  1.000 12.85344 ?  39  THR   A OG1  1 
ATOM   281  C CG2  . THR   A 1 42  ? -11.29600 5.92800   -7.88700  1.000 15.77805 ?  39  THR   A CG2  1 
ATOM   282  N N    . LEU   A 1 43  ? -13.44600 5.67100   -5.27000  1.000 6.96978  ?  40  LEU   A N    1 
ATOM   283  C CA   . LEU   A 1 43  ? -14.24900 4.53200   -4.82600  1.000 8.95904  ?  40  LEU   A CA   1 
ATOM   284  C C    . LEU   A 1 43  ? -14.57100 3.64100   -6.01500  1.000 11.41684 ?  40  LEU   A C    1 
ATOM   285  O O    . LEU   A 1 43  ? -15.28000 4.06100   -6.93600  1.000 12.66537 ?  40  LEU   A O    1 
ATOM   286  C CB   . LEU   A 1 43  ? -15.55100 4.98500   -4.16300  1.000 11.68510 ?  40  LEU   A CB   1 
ATOM   287  C CG   . LEU   A 1 43  ? -15.41800 5.51700   -2.73800  1.000 9.27524  ?  40  LEU   A CG   1 
ATOM   288  C CD1  . LEU   A 1 43  ? -16.81300 5.87400   -2.18000  1.000 9.08861  ?  40  LEU   A CD1  1 
ATOM   289  C CD2  . LEU   A 1 43  ? -14.70500 4.51300   -1.84500  1.000 8.57679  ?  40  LEU   A CD2  1 
ATOM   290  N N    . THR   A 1 44  ? -14.06800 2.40700   -5.98500  1.000 10.83140 ?  41  THR   A N    1 
ATOM   291  C CA   . THR   A 1 44  ? -14.42200 1.44000   -7.01100  1.000 11.39725 ?  41  THR   A CA   1 
ATOM   292  C C    . THR   A 1 44  ? -15.75700 0.76700   -6.74500  1.000 14.63772 ?  41  THR   A C    1 
ATOM   293  O O    . THR   A 1 44  ? -16.33600 0.18100   -7.67200  1.000 15.21316 ?  41  THR   A O    1 
ATOM   294  C CB   . THR   A 1 44  ? -13.32400 0.38300   -7.13100  1.000 13.60082 ?  41  THR   A CB   1 
ATOM   295  O OG1  . THR   A 1 44  ? -13.28800 -0.41600  -5.93600  1.000 13.84182 ?  41  THR   A OG1  1 
ATOM   296  C CG2  . THR   A 1 44  ? -11.97400 1.02700   -7.34600  1.000 15.55514 ?  41  THR   A CG2  1 
ATOM   297  N N    A ASP   A 1 45  ? -16.26700 0.84900   -5.51600  0.571 10.21460 ?  42  ASP   A N    1 
ATOM   298  N N    B ASP   A 1 45  ? -16.25800 0.83000   -5.51400  0.429 10.24296 ?  42  ASP   A N    1 
ATOM   299  C CA   A ASP   A 1 45  ? -17.54100 0.22200   -5.20300  0.571 11.20089 ?  42  ASP   A CA   1 
ATOM   300  C CA   B ASP   A 1 45  ? -17.53600 0.21800   -5.18100  0.429 11.21012 ?  42  ASP   A CA   1 
ATOM   301  C C    A ASP   A 1 45  ? -18.10100 0.93200   -3.97300  0.571 8.08903  ?  42  ASP   A C    1 
ATOM   302  C C    B ASP   A 1 45  ? -18.10100 0.94300   -3.96700  0.429 8.12928  ?  42  ASP   A C    1 
ATOM   303  O O    A ASP   A 1 45  ? -17.34200 1.42100   -3.13200  0.571 7.40597  ?  42  ASP   A O    1 
ATOM   304  O O    B ASP   A 1 45  ? -17.35000 1.44600   -3.12800  0.429 7.45143  ?  42  ASP   A O    1 
ATOM   305  C CB   A ASP   A 1 45  ? -17.35700 -1.27500  -4.93400  0.571 12.12316 ?  42  ASP   A CB   1 
ATOM   306  C CB   B ASP   A 1 45  ? -17.37900 -1.28000  -4.89200  0.429 12.12992 ?  42  ASP   A CB   1 
ATOM   307  C CG   A ASP   A 1 45  ? -18.66500 -2.03400  -4.91200  0.571 19.55441 ?  42  ASP   A CG   1 
ATOM   308  C CG   B ASP   A 1 45  ? -17.65500 -2.14500  -6.11600  0.429 18.59565 ?  42  ASP   A CG   1 
ATOM   309  O OD1  A ASP   A 1 45  ? -19.71700 -1.42900  -5.21600  0.571 22.04762 ?  42  ASP   A OD1  1 
ATOM   310  O OD1  B ASP   A 1 45  ? -18.21000 -1.63200  -7.11200  0.429 22.75139 ?  42  ASP   A OD1  1 
ATOM   311  O OD2  A ASP   A 1 45  ? -18.63000 -3.24100  -4.59300  0.571 26.35086 -1 42  ASP   A OD2  1 
ATOM   312  O OD2  B ASP   A 1 45  ? -17.30900 -3.34200  -6.08400  0.429 25.22700 -1 42  ASP   A OD2  1 
ATOM   313  N N    . CYS   A 1 46  ? -19.43000 0.99700   -3.88300  1.000 10.49995 ?  43  CYS   A N    1 
ATOM   314  C CA   . CYS   A 1 46  ? -20.09200 1.67000   -2.75900  1.000 7.07892  ?  43  CYS   A CA   1 
ATOM   315  C C    . CYS   A 1 46  ? -21.54400 1.22300   -2.72500  1.000 11.16805 ?  43  CYS   A C    1 
ATOM   316  O O    . CYS   A 1 46  ? -22.29400 1.50500   -3.67000  1.000 13.54355 ?  43  CYS   A O    1 
ATOM   317  C CB   . CYS   A 1 46  ? -20.00300 3.19000   -2.91000  1.000 11.68821 ?  43  CYS   A CB   1 
ATOM   318  S SG   . CYS   A 1 46  ? -20.78800 4.11600   -1.57000  1.000 13.12484 ?  43  CYS   A SG   1 
ATOM   319  N N    A VAL   A 1 47  ? -21.94800 0.55200   -1.64300  0.437 8.66899  ?  44  VAL   A N    1 
ATOM   320  N N    B VAL   A 1 47  ? -21.95600 0.55400   -1.65300  0.563 8.66385  ?  44  VAL   A N    1 
ATOM   321  C CA   A VAL   A 1 47  ? -23.25800 -0.09300  -1.55100  0.437 9.34794  ?  44  VAL   A CA   1 
ATOM   322  C CA   B VAL   A 1 47  ? -23.31500 0.02600   -1.60200  0.563 9.32039  ?  44  VAL   A CA   1 
ATOM   323  C C    A VAL   A 1 47  ? -23.84300 0.10900   -0.15900  0.437 7.45776  ?  44  VAL   A C    1 
ATOM   324  C C    B VAL   A 1 47  ? -23.85500 0.11600   -0.18700  0.563 7.42893  ?  44  VAL   A C    1 
ATOM   325  O O    A VAL   A 1 47  ? -23.13700 -0.04200  0.84500   0.437 7.22977  ?  44  VAL   A O    1 
ATOM   326  O O    B VAL   A 1 47  ? -23.13500 -0.12300  0.79100   0.563 7.20921  ?  44  VAL   A O    1 
ATOM   327  C CB   A VAL   A 1 47  ? -23.16100 -1.60200  -1.86200  0.437 13.61318 ?  44  VAL   A CB   1 
ATOM   328  C CB   B VAL   A 1 47  ? -23.37800 -1.43200  -2.08100  0.563 14.15115 ?  44  VAL   A CB   1 
ATOM   329  C CG1  A VAL   A 1 47  ? -24.54500 -2.21300  -2.01500  0.437 15.83761 ?  44  VAL   A CG1  1 
ATOM   330  C CG1  B VAL   A 1 47  ? -22.43000 -2.24500  -1.28000  0.563 8.78577  ?  44  VAL   A CG1  1 
ATOM   331  C CG2  A VAL   A 1 47  ? -22.34100 -1.84200  -3.11600  0.437 11.01700 ?  44  VAL   A CG2  1 
ATOM   332  C CG2  B VAL   A 1 47  ? -24.78300 -1.97900  -1.92400  0.563 17.23463 ?  44  VAL   A CG2  1 
ATOM   333  N N    . VAL   A 1 48  ? -25.14800 0.41300   -0.09600  1.000 8.09752  ?  45  VAL   A N    1 
ATOM   334  C CA   . VAL   A 1 48  ? -25.89400 0.39100   1.15400   1.000 6.86203  ?  45  VAL   A CA   1 
ATOM   335  C C    . VAL   A 1 48  ? -26.65200 -0.93100  1.16900   1.000 7.11141  ?  45  VAL   A C    1 
ATOM   336  O O    . VAL   A 1 48  ? -27.32400 -1.27300  0.19200   1.000 7.23978  ?  45  VAL   A O    1 
ATOM   337  C CB   . VAL   A 1 48  ? -26.85900 1.58800   1.25300   1.000 7.28272  ?  45  VAL   A CB   1 
ATOM   338  C CG1  . VAL   A 1 48  ? -27.88400 1.36700   2.34800   1.000 9.70571  ?  45  VAL   A CG1  1 
ATOM   339  C CG2  . VAL   A 1 48  ? -26.10500 2.90700   1.43000   1.000 10.88624 ?  45  VAL   A CG2  1 
ATOM   340  N N    . MET   A 1 49  ? -26.49700 -1.72000  2.22700   1.000 7.75162  ?  46  MET   A N    1 
ATOM   341  C CA   . MET   A 1 49  ? -27.26500 -2.96300  2.32400   1.000 5.36361  ?  46  MET   A CA   1 
ATOM   342  C C    . MET   A 1 49  ? -28.71100 -2.68600  2.63300   1.000 6.99856  ?  46  MET   A C    1 
ATOM   343  O O    . MET   A 1 49  ? -29.00500 -1.86800  3.49700   1.000 7.25580  ?  46  MET   A O    1 
ATOM   344  C CB   . MET   A 1 49  ? -26.65400 -3.89800  3.37300   1.000 9.93790  ?  46  MET   A CB   1 
ATOM   345  C CG   . MET   A 1 49  ? -25.21300 -4.34000  3.19000   1.000 11.49829 ?  46  MET   A CG   1 
ATOM   346  S SD   . MET   A 1 49  ? -25.14600 -5.30300  1.66200   1.000 15.26567 ?  46  MET   A SD   1 
ATOM   347  C CE   . MET   A 1 49  ? -26.28100 -6.56700  1.95900   1.000 28.71966 ?  46  MET   A CE   1 
ATOM   348  N N    . ARG   A 1 50  ? -29.61100 -3.34400  1.89300   1.000 7.35642  ?  47  ARG   A N    1 
ATOM   349  C CA   . ARG   A 1 50  ? -31.04500 -3.13200  2.04700   1.000 5.94323  ?  47  ARG   A CA   1 
ATOM   350  C C    . ARG   A 1 50  ? -31.75300 -4.46400  2.18300   1.000 6.28610  ?  47  ARG   A C    1 
ATOM   351  O O    . ARG   A 1 50  ? -31.25900 -5.50300  1.73700   1.000 11.14744 ?  47  ARG   A O    1 
ATOM   352  C CB   . ARG   A 1 50  ? -31.63300 -2.38600  0.85700   1.000 9.42279  ?  47  ARG   A CB   1 
ATOM   353  C CG   . ARG   A 1 50  ? -31.10100 -0.99100  0.76000   1.000 10.87005 ?  47  ARG   A CG   1 
ATOM   354  C CD   . ARG   A 1 50  ? -31.70100 -0.29600  -0.44500  1.000 10.64857 ?  47  ARG   A CD   1 
ATOM   355  N NE   . ARG   A 1 50  ? -31.16400 1.05400   -0.48900  1.000 12.05467 ?  47  ARG   A NE   1 
ATOM   356  C CZ   . ARG   A 1 50  ? -31.53700 2.03400   0.31800   1.000 10.78871 ?  47  ARG   A CZ   1 
ATOM   357  N NH1  . ARG   A 1 50  ? -32.53200 1.88200   1.18500   1.000 13.26999 ?  47  ARG   A NH1  1 
ATOM   358  N NH2  . ARG   A 1 50  ? -30.91500 3.20800   0.23600   1.000 14.30176 ?  47  ARG   A NH2  1 
ATOM   359  N N    . ASP   A 1 51  ? -32.94900 -4.40400  2.77100   1.000 6.97954  ?  48  ASP   A N    1 
ATOM   360  C CA   . ASP   A 1 51  ? -33.79700 -5.58400  2.80000   1.000 8.40956  ?  48  ASP   A CA   1 
ATOM   361  C C    . ASP   A 1 51  ? -34.19400 -5.96700  1.37200   1.000 6.96714  ?  48  ASP   A C    1 
ATOM   362  O O    . ASP   A 1 51  ? -34.52000 -5.09100  0.55600   1.000 9.37775  ?  48  ASP   A O    1 
ATOM   363  C CB   . ASP   A 1 51  ? -35.05600 -5.30700  3.61900   1.000 8.26778  ?  48  ASP   A CB   1 
ATOM   364  C CG   . ASP   A 1 51  ? -35.87600 -6.54900  3.84800   1.000 9.83292  ?  48  ASP   A CG   1 
ATOM   365  O OD1  . ASP   A 1 51  ? -35.58400 -7.25900  4.83400   1.000 9.56498  ?  48  ASP   A OD1  1 
ATOM   366  O OD2  . ASP   A 1 51  ? -36.81100 -6.80800  3.06500   1.000 8.64771  -1 48  ASP   A OD2  1 
ATOM   367  N N    . PRO   A 1 52  ? -34.19300 -7.26000  1.03400   1.000 6.95994  ?  49  PRO   A N    1 
ATOM   368  C CA   . PRO   A 1 52  ? -34.55500 -7.65100  -0.34300  1.000 9.58417  ?  49  PRO   A CA   1 
ATOM   369  C C    . PRO   A 1 52  ? -36.01200 -7.42300  -0.71700  1.000 10.90332 ?  49  PRO   A C    1 
ATOM   370  O O    . PRO   A 1 52  ? -36.31100 -7.29200  -1.91400  1.000 10.59527 ?  49  PRO   A O    1 
ATOM   371  C CB   . PRO   A 1 52  ? -34.18300 -9.13900  -0.38600  1.000 11.78837 ?  49  PRO   A CB   1 
ATOM   372  C CG   . PRO   A 1 52  ? -34.29100 -9.60400  1.02700   1.000 11.45541 ?  49  PRO   A CG   1 
ATOM   373  C CD   . PRO   A 1 52  ? -33.74000 -8.41200  1.83800   1.000 9.02661  ?  49  PRO   A CD   1 
ATOM   374  N N    . ASN   A 1 53  ? -36.93000 -7.38000  0.24400   1.000 9.96077  ?  50  ASN   A N    1 
ATOM   375  C CA   . ASN   A 1 53  ? -38.34100 -7.18300  -0.06200  1.000 8.83170  ?  50  ASN   A CA   1 
ATOM   376  C C    . ASN   A 1 53  ? -38.81400 -5.75600  0.16300   1.000 9.08459  ?  50  ASN   A C    1 
ATOM   377  O O    . ASN   A 1 53  ? -39.53600 -5.21300  -0.67700  1.000 9.30024  ?  50  ASN   A O    1 
ATOM   378  C CB   . ASN   A 1 53  ? -39.18800 -8.12000  0.79200   1.000 7.29217  ?  50  ASN   A CB   1 
ATOM   379  C CG   . ASN   A 1 53  ? -38.92000 -9.57400  0.49700   1.000 15.97715 ?  50  ASN   A CG   1 
ATOM   380  O OD1  . ASN   A 1 53  ? -38.82200 -9.96800  -0.66300  1.000 15.24353 ?  50  ASN   A OD1  1 
ATOM   381  N ND2  . ASN   A 1 53  ? -38.76700 -10.37600 1.54700   1.000 19.20624 ?  50  ASN   A ND2  1 
ATOM   382  N N    . THR   A 1 54  ? -38.43300 -5.13000  1.28300   1.000 5.92076  ?  51  THR   A N    1 
ATOM   383  C CA   . THR   A 1 54  ? -38.90400 -3.78400  1.59600   1.000 7.11004  ?  51  THR   A CA   1 
ATOM   384  C C    . THR   A 1 54  ? -38.04100 -2.68500  1.00400   1.000 8.50528  ?  51  THR   A C    1 
ATOM   385  O O    . THR   A 1 54  ? -38.49100 -1.53600  0.94500   1.000 10.79164 ?  51  THR   A O    1 
ATOM   386  C CB   . THR   A 1 54  ? -38.93900 -3.55500  3.11200   1.000 7.66553  ?  51  THR   A CB   1 
ATOM   387  O OG1  . THR   A 1 54  ? -37.58500 -3.59500  3.57700   1.000 6.66639  ?  51  THR   A OG1  1 
ATOM   388  C CG2  . THR   A 1 54  ? -39.78400 -4.61700  3.83500   1.000 11.73368 ?  51  THR   A CG2  1 
ATOM   389  N N    . LYS   A 1 55  ? -36.80900 -3.00600  0.62500   1.000 7.60623  ?  52  LYS   A N    1 
ATOM   390  C CA   . LYS   A 1 55  ? -35.76400 -2.05600  0.26000   1.000 6.94725  ?  52  LYS   A CA   1 
ATOM   391  C C    . LYS   A 1 55  ? -35.39500 -1.11400  1.39300   1.000 8.38796  ?  52  LYS   A C    1 
ATOM   392  O O    . LYS   A 1 55  ? -34.63300 -0.16900  1.17800   1.000 9.66675  ?  52  LYS   A O    1 
ATOM   393  C CB   . LYS   A 1 55  ? -36.13000 -1.23400  -0.97500  1.000 10.84913 ?  52  LYS   A CB   1 
ATOM   394  C CG   . LYS   A 1 55  ? -36.58900 -2.05900  -2.17800  1.000 16.10271 ?  52  LYS   A CG   1 
ATOM   395  C CD   . LYS   A 1 55  ? -37.04200 -1.12300  -3.28900  1.000 32.01582 ?  52  LYS   A CD   1 
ATOM   396  C CE   . LYS   A 1 55  ? -36.90200 -1.77200  -4.66000  1.000 34.37053 ?  52  LYS   A CE   1 
ATOM   397  N NZ   . LYS   A 1 55  ? -37.93900 -2.80500  -4.86300  1.000 31.38759 ?  52  LYS   A NZ   1 
ATOM   398  N N    . ARG   A 1 56  ? -35.89400 -1.34400  2.60000   1.000 5.34186  ?  53  ARG   A N    1 
ATOM   399  C CA   . ARG   A 1 56  ? -35.47600 -0.50800  3.71400   1.000 8.04726  ?  53  ARG   A CA   1 
ATOM   400  C C    . ARG   A 1 56  ? -34.02500 -0.80900  4.06500   1.000 9.20798  ?  53  ARG   A C    1 
ATOM   401  O O    . ARG   A 1 56  ? -33.60300 -1.96600  4.10200   1.000 8.63206  ?  53  ARG   A O    1 
ATOM   402  C CB   . ARG   A 1 56  ? -36.38300 -0.73800  4.93500   1.000 9.58385  ?  53  ARG   A CB   1 
ATOM   403  C CG   . ARG   A 1 56  ? -36.14300 0.26900   6.09400   1.000 8.81568  ?  53  ARG   A CG   1 
ATOM   404  C CD   . ARG   A 1 56  ? -36.99000 -0.10700  7.33200   1.000 7.10708  ?  53  ARG   A CD   1 
ATOM   405  N NE   . ARG   A 1 56  ? -38.40700 -0.27800  7.01200   1.000 8.69112  ?  53  ARG   A NE   1 
ATOM   406  C CZ   . ARG   A 1 56  ? -39.24000 0.71400   6.73300   1.000 9.97158  ?  53  ARG   A CZ   1 
ATOM   407  N NH1  . ARG   A 1 56  ? -38.87500 1.98200   6.85900   1.000 9.70974  ?  53  ARG   A NH1  1 
ATOM   408  N NH2  . ARG   A 1 56  ? -40.47500 0.42900   6.32100   1.000 7.60960  ?  53  ARG   A NH2  1 
ATOM   409  N N    . SER   A 1 57  ? -33.27400 0.24700   4.35600   1.000 6.35918  ?  54  SER   A N    1 
ATOM   410  C CA   . SER   A 1 57  ? -31.86900 0.11300   4.73100   1.000 6.06478  ?  54  SER   A CA   1 
ATOM   411  C C    . SER   A 1 57  ? -31.69400 -0.81600  5.92200   1.000 7.53734  ?  54  SER   A C    1 
ATOM   412  O O    . SER   A 1 57  ? -32.47100 -0.78400  6.88200   1.000 9.58510  ?  54  SER   A O    1 
ATOM   413  C CB   . SER   A 1 57  ? -31.28500 1.47800   5.08200   1.000 7.22124  ?  54  SER   A CB   1 
ATOM   414  O OG   . SER   A 1 57  ? -29.91100 1.33100   5.50700   1.000 6.37014  ?  54  SER   A OG   1 
ATOM   415  N N    . ARG   A 1 58  ? -30.62100 -1.60600  5.86600   1.000 7.79864  ?  55  ARG   A N    1 
ATOM   416  C CA   . ARG   A 1 58  ? -30.17300 -2.42100  6.98000   1.000 6.40087  ?  55  ARG   A CA   1 
ATOM   417  C C    . ARG   A 1 58  ? -29.23900 -1.64200  7.89900   1.000 8.64363  ?  55  ARG   A C    1 
ATOM   418  O O    . ARG   A 1 58  ? -28.81400 -2.17200  8.93500   1.000 7.00029  ?  55  ARG   A O    1 
ATOM   419  C CB   . ARG   A 1 58  ? -29.51200 -3.67900  6.42800   1.000 6.17236  ?  55  ARG   A CB   1 
ATOM   420  C CG   . ARG   A 1 58  ? -30.55500 -4.70300  5.87800   1.000 12.61660 ?  55  ARG   A CG   1 
ATOM   421  C CD   . ARG   A 1 58  ? -29.90500 -5.89200  5.17300   1.000 15.10593 ?  55  ARG   A CD   1 
ATOM   422  N NE   . ARG   A 1 58  ? -29.19000 -6.73200  6.12100   1.000 20.62294 ?  55  ARG   A NE   1 
ATOM   423  C CZ   . ARG   A 1 58  ? -28.45500 -7.79300  5.81000   1.000 21.16574 ?  55  ARG   A CZ   1 
ATOM   424  N NH1  . ARG   A 1 58  ? -28.34100 -8.21500  4.56900   1.000 22.40578 ?  55  ARG   A NH1  1 
ATOM   425  N NH2  . ARG   A 1 58  ? -27.80600 -8.43700  6.77900   1.000 30.38806 ?  55  ARG   A NH2  1 
ATOM   426  H HA   . ARG   A 1 58  ? -30.91800 -2.71600  7.52500   1.000 7.68104  ?  55  ARG   A HA   1 
ATOM   427  H HB2  . ARG   A 1 58  ? -28.91800 -3.43300  5.70200   1.000 7.40684  ?  55  ARG   A HB2  1 
ATOM   428  H HB3  . ARG   A 1 58  ? -29.00900 -4.11000  7.13600   1.000 7.40684  ?  55  ARG   A HB3  1 
ATOM   429  H HG2  . ARG   A 1 58  ? -31.08200 -5.04500  6.61700   1.000 15.13992 ?  55  ARG   A HG2  1 
ATOM   430  H HG3  . ARG   A 1 58  ? -31.13100 -4.25500  5.23900   1.000 15.13992 ?  55  ARG   A HG3  1 
ATOM   431  H HD2  . ARG   A 1 58  ? -30.59100 -6.42700  4.74400   1.000 18.12712 ?  55  ARG   A HD2  1 
ATOM   432  H HD3  . ARG   A 1 58  ? -29.27400 -5.56900  4.51100   1.000 18.12712 ?  55  ARG   A HD3  1 
ATOM   433  H HE   . ARG   A 1 58  ? -29.24800 -6.52400  6.95300   1.000 24.74752 ?  55  ARG   A HE   1 
ATOM   434  H HH11 . ARG   A 1 58  ? -28.74800 -7.80200  3.93500   1.000 26.88694 ?  55  ARG   A HH11 1 
ATOM   435  H HH12 . ARG   A 1 58  ? -27.85900 -8.90500  4.39200   1.000 26.88694 ?  55  ARG   A HH12 1 
ATOM   436  H HH21 . ARG   A 1 58  ? -27.86700 -8.16500  7.59300   1.000 36.46568 ?  55  ARG   A HH21 1 
ATOM   437  H HH22 . ARG   A 1 58  ? -27.32600 -9.12600  6.59200   1.000 36.46568 ?  55  ARG   A HH22 1 
ATOM   438  N N    . GLY   A 1 59  ? -28.97800 -0.37200  7.59700   1.000 5.97259  ?  56  GLY   A N    1 
ATOM   439  C CA   . GLY   A 1 59  ? -28.17900 0.43300   8.50200   1.000 4.96722  ?  56  GLY   A CA   1 
ATOM   440  C C    . GLY   A 1 59  ? -26.68700 0.25200   8.36300   1.000 7.59210  ?  56  GLY   A C    1 
ATOM   441  O O    . GLY   A 1 59  ? -25.94600 0.71700   9.23800   1.000 8.91388  ?  56  GLY   A O    1 
ATOM   442  N N    . PHE   A 1 60  ? -26.22300 -0.46500  7.34100   1.000 6.54234  ?  57  PHE   A N    1 
ATOM   443  C CA   . PHE   A 1 60  ? -24.79100 -0.55700  7.10600   1.000 7.28922  ?  57  PHE   A CA   1 
ATOM   444  C C    . PHE   A 1 60  ? -24.54300 -0.70800  5.61600   1.000 7.04725  ?  57  PHE   A C    1 
ATOM   445  O O    . PHE   A 1 60  ? -25.45400 -1.00400  4.83000   1.000 6.79079  ?  57  PHE   A O    1 
ATOM   446  C CB   . PHE   A 1 60  ? -24.15800 -1.71200  7.91800   1.000 5.69935  ?  57  PHE   A CB   1 
ATOM   447  C CG   . PHE   A 1 60  ? -24.55300 -3.09700  7.45400   1.000 5.32263  ?  57  PHE   A CG   1 
ATOM   448  C CD1  . PHE   A 1 60  ? -25.72700 -3.67500  7.90300   1.000 7.88496  ?  57  PHE   A CD1  1 
ATOM   449  C CD2  . PHE   A 1 60  ? -23.74300 -3.82500  6.59800   1.000 7.37332  ?  57  PHE   A CD2  1 
ATOM   450  C CE1  . PHE   A 1 60  ? -26.09100 -4.94100  7.49100   1.000 11.06760 ?  57  PHE   A CE1  1 
ATOM   451  C CE2  . PHE   A 1 60  ? -24.11000 -5.09800  6.18000   1.000 8.83555  ?  57  PHE   A CE2  1 
ATOM   452  C CZ   . PHE   A 1 60  ? -25.28800 -5.64900  6.63300   1.000 8.84051  ?  57  PHE   A CZ   1 
ATOM   453  H HA   . PHE   A 1 60  ? -24.35800 0.26400   7.38600   1.000 8.74706  ?  57  PHE   A HA   1 
ATOM   454  H HB2  . PHE   A 1 60  ? -23.19300 -1.64500  7.84900   1.000 6.83921  ?  57  PHE   A HB2  1 
ATOM   455  H HB3  . PHE   A 1 60  ? -24.43100 -1.62500  8.84500   1.000 6.83921  ?  57  PHE   A HB3  1 
ATOM   456  H HD1  . PHE   A 1 60  ? -26.27600 -3.20600  8.48900   1.000 9.46195  ?  57  PHE   A HD1  1 
ATOM   457  H HD2  . PHE   A 1 60  ? -22.94400 -3.45600  6.29900   1.000 8.84799  ?  57  PHE   A HD2  1 
ATOM   458  H HE1  . PHE   A 1 60  ? -26.88600 -5.31500  7.79600   1.000 13.28112 ?  57  PHE   A HE1  1 
ATOM   459  H HE2  . PHE   A 1 60  ? -23.56300 -5.57400  5.59700   1.000 10.60266 ?  57  PHE   A HE2  1 
ATOM   460  H HZ   . PHE   A 1 60  ? -25.53900 -6.50100  6.35800   1.000 10.60861 ?  57  PHE   A HZ   1 
ATOM   461  N N    . GLY   A 1 61  ? -23.28800 -0.48300  5.23500   1.000 6.50643  ?  58  GLY   A N    1 
ATOM   462  C CA   . GLY   A 1 61  ? -22.89200 -0.58700  3.85400   1.000 8.20373  ?  58  GLY   A CA   1 
ATOM   463  C C    . GLY   A 1 61  ? -21.40600 -0.83300  3.77500   1.000 6.06056  ?  58  GLY   A C    1 
ATOM   464  O O    . GLY   A 1 61  ? -20.74400 -1.07500  4.78500   1.000 7.23441  ?  58  GLY   A O    1 
ATOM   465  N N    A PHE   A 1 62  ? -20.89800 -0.76100  2.54900   0.646 7.07485  ?  59  PHE   A N    1 
ATOM   466  N N    B PHE   A 1 62  ? -20.88000 -0.81200  2.55000   0.354 7.14126  ?  59  PHE   A N    1 
ATOM   467  C CA   A PHE   A 1 62  ? -19.48700 -0.97100  2.27800   0.646 8.95650  ?  59  PHE   A CA   1 
ATOM   468  C CA   B PHE   A 1 62  ? -19.44000 -0.95500  2.38400   0.354 8.89987  ?  59  PHE   A CA   1 
ATOM   469  C C    A PHE   A 1 62  ? -19.02000 0.06200   1.26700   0.646 7.08789  ?  59  PHE   A C    1 
ATOM   470  C C    B PHE   A 1 62  ? -18.95300 -0.11800  1.21400   0.354 7.42715  ?  59  PHE   A C    1 
ATOM   471  O O    A PHE   A 1 62  ? -19.77900 0.50300   0.40100   0.646 7.50028  ?  59  PHE   A O    1 
ATOM   472  O O    B PHE   A 1 62  ? -19.63900 0.01800   0.19700   0.354 7.82289  ?  59  PHE   A O    1 
ATOM   473  C CB   A PHE   A 1 62  ? -19.22400 -2.39500  1.74400   0.646 12.71461 ?  59  PHE   A CB   1 
ATOM   474  C CB   B PHE   A 1 62  ? -19.01400 -2.43100  2.21500   0.354 12.61771 ?  59  PHE   A CB   1 
ATOM   475  C CG   A PHE   A 1 62  ? -19.63100 -3.49000  2.69600   0.646 13.81903 ?  59  PHE   A CG   1 
ATOM   476  C CG   B PHE   A 1 62  ? -19.05700 -2.95300  0.79200   0.354 11.60451 ?  59  PHE   A CG   1 
ATOM   477  C CD1  A PHE   A 1 62  ? -18.74900 -3.95100  3.66200   0.646 15.71648 ?  59  PHE   A CD1  1 
ATOM   478  C CD1  B PHE   A 1 62  ? -17.97200 -2.80700  -0.05100  0.354 8.27312  ?  59  PHE   A CD1  1 
ATOM   479  C CD2  A PHE   A 1 62  ? -20.88900 -4.06100  2.61700   0.646 14.02460 ?  59  PHE   A CD2  1 
ATOM   480  C CD2  B PHE   A 1 62  ? -20.17800 -3.60700  0.31000   0.354 14.72817 ?  59  PHE   A CD2  1 
ATOM   481  C CE1  A PHE   A 1 62  ? -19.12800 -4.96300  4.53900   0.646 10.91239 ?  59  PHE   A CE1  1 
ATOM   482  C CE1  B PHE   A 1 62  ? -18.00400 -3.28600  -1.35400  0.354 15.01995 ?  59  PHE   A CE1  1 
ATOM   483  C CE2  A PHE   A 1 62  ? -21.26400 -5.07100  3.48700   0.646 14.44933 ?  59  PHE   A CE2  1 
ATOM   484  C CE2  B PHE   A 1 62  ? -20.20500 -4.10300  -0.99000  0.354 11.18111 ?  59  PHE   A CE2  1 
ATOM   485  C CZ   A PHE   A 1 62  ? -20.38300 -5.51500  4.44400   0.646 12.37392 ?  59  PHE   A CZ   1 
ATOM   486  C CZ   B PHE   A 1 62  ? -19.12400 -3.92800  -1.82000  0.354 12.40620 ?  59  PHE   A CZ   1 
ATOM   487  H HA   A PHE   A 1 62  ? -18.97200 -0.85400  3.09100   0.646 10.74780 ?  59  PHE   A HA   1 
ATOM   488  H HA   B PHE   A 1 62  ? -19.00900 -0.61000  3.18100   0.354 10.67985 ?  59  PHE   A HA   1 
ATOM   489  H HB2  A PHE   A 1 62  ? -19.72400 -2.51700  0.92200   0.646 15.25753 ?  59  PHE   A HB2  1 
ATOM   490  H HB2  B PHE   A 1 62  ? -18.10200 -2.52500  2.53100   0.354 15.14125 ?  59  PHE   A HB2  1 
ATOM   491  H HB3  A PHE   A 1 62  ? -18.27400 -2.49200  1.57200   0.646 15.25753 ?  59  PHE   A HB3  1 
ATOM   492  H HB3  B PHE   A 1 62  ? -19.60800 -2.98500  2.74500   0.354 15.14125 ?  59  PHE   A HB3  1 
ATOM   493  H HD1  A PHE   A 1 62  ? -17.89900 -3.58000  3.72500   0.646 18.85978 ?  59  PHE   A HD1  1 
ATOM   494  H HD1  B PHE   A 1 62  ? -17.20600 -2.38100  0.26000   0.354 9.92774  ?  59  PHE   A HD1  1 
ATOM   495  H HD2  A PHE   A 1 62  ? -21.48900 -3.76300  1.97200   0.646 16.82951 ?  59  PHE   A HD2  1 
ATOM   496  H HD2  B PHE   A 1 62  ? -20.92000 -3.71600  0.86000   0.354 17.67381 ?  59  PHE   A HD2  1 
ATOM   497  H HE1  A PHE   A 1 62  ? -18.53300 -5.26500  5.18800   0.646 13.09487 ?  59  PHE   A HE1  1 
ATOM   498  H HE1  B PHE   A 1 62  ? -17.26700 -3.17200  -1.91000  0.354 18.02394 ?  59  PHE   A HE1  1 
ATOM   499  H HE2  A PHE   A 1 62  ? -22.11100 -5.44900  3.42300   0.646 17.33920 ?  59  PHE   A HE2  1 
ATOM   500  H HE2  B PHE   A 1 62  ? -20.95700 -4.55600  -1.29700  0.354 13.41733 ?  59  PHE   A HE2  1 
ATOM   501  H HZ   A PHE   A 1 62  ? -20.63700 -6.19100  5.02900   0.646 14.84870 ?  59  PHE   A HZ   1 
ATOM   502  H HZ   B PHE   A 1 62  ? -19.15200 -4.24200  -2.69500  0.354 14.88744 ?  59  PHE   A HZ   1 
ATOM   503  N N    . VAL   A 1 63  ? -17.75300 0.43300   1.36600   1.000 6.53504  ?  60  VAL   A N    1 
ATOM   504  C CA   . VAL   A 1 63  ? -17.12400 1.21000   0.31300   1.000 5.47305  ?  60  VAL   A CA   1 
ATOM   505  C C    . VAL   A 1 63  ? -15.79700 0.54100   0.03100   1.000 9.00338  ?  60  VAL   A C    1 
ATOM   506  O O    . VAL   A 1 63  ? -15.16200 -0.00700  0.94100   1.000 7.18629  ?  60  VAL   A O    1 
ATOM   507  C CB   . VAL   A 1 63  ? -16.91400 2.69200   0.69400   1.000 7.72948  ?  60  VAL   A CB   1 
ATOM   508  C CG1  . VAL   A 1 63  ? -18.25100 3.37000   0.96200   1.000 8.77104  ?  60  VAL   A CG1  1 
ATOM   509  C CG2  . VAL   A 1 63  ? -15.98200 2.81400   1.87200   1.000 10.66042 ?  60  VAL   A CG2  1 
ATOM   510  N N    . THR   A 1 64  ? -15.38500 0.57000   -1.23200  1.000 5.42798  ?  61  THR   A N    1 
ATOM   511  C CA   . THR   A 1 64  ? -14.09600 0.00900   -1.63200  1.000 5.93001  ?  61  THR   A CA   1 
ATOM   512  C C    . THR   A 1 64  ? -13.28300 1.09500   -2.31400  1.000 8.36908  ?  61  THR   A C    1 
ATOM   513  O O    . THR   A 1 64  ? -13.73100 1.66300   -3.31100  1.000 8.60844  ?  61  THR   A O    1 
ATOM   514  C CB   . THR   A 1 64  ? -14.28300 -1.16800  -2.57400  1.000 10.09747 ?  61  THR   A CB   1 
ATOM   515  O OG1  . THR   A 1 64  ? -15.11100 -2.13600  -1.92100  1.000 10.68520 ?  61  THR   A OG1  1 
ATOM   516  C CG2  . THR   A 1 64  ? -12.91700 -1.83500  -2.87100  1.000 9.04107  ?  61  THR   A CG2  1 
ATOM   517  N N    . TYR   A 1 65  ? -12.10000 1.37700   -1.77800  1.000 6.99816  ?  62  TYR   A N    1 
ATOM   518  C CA   . TYR   A 1 65  ? -11.20900 2.36400   -2.36900  1.000 8.53191  ?  62  TYR   A CA   1 
ATOM   519  C C    . TYR   A 1 65  ? -10.27000 1.72200   -3.38200  1.000 10.17584 ?  62  TYR   A C    1 
ATOM   520  O O    . TYR   A 1 65  ? -10.10600 0.50900   -3.42900  1.000 8.56819  ?  62  TYR   A O    1 
ATOM   521  C CB   . TYR   A 1 65  ? -10.38100 3.05100   -1.28700  1.000 5.25881  ?  62  TYR   A CB   1 
ATOM   522  C CG   . TYR   A 1 65  ? -11.14800 4.07700   -0.50400  1.000 4.93550  ?  62  TYR   A CG   1 
ATOM   523  C CD1  . TYR   A 1 65  ? -11.38100 5.34000   -1.04300  1.000 8.02806  ?  62  TYR   A CD1  1 
ATOM   524  C CD2  . TYR   A 1 65  ? -11.64400 3.80200   0.76800   1.000 4.56712  ?  62  TYR   A CD2  1 
ATOM   525  C CE1  . TYR   A 1 65  ? -12.10400 6.29400   -0.33800  1.000 7.29078  ?  62  TYR   A CE1  1 
ATOM   526  C CE2  . TYR   A 1 65  ? -12.35700 4.75400   1.47500   1.000 5.94175  ?  62  TYR   A CE2  1 
ATOM   527  C CZ   . TYR   A 1 65  ? -12.58000 6.00000   0.92100   1.000 6.14731  ?  62  TYR   A CZ   1 
ATOM   528  O OH   . TYR   A 1 65  ? -13.27100 6.95600   1.63200   1.000 7.30732  ?  62  TYR   A OH   1 
ATOM   529  N N    . ALA   A 1 66  ? -9.63500  2.56900   -4.19800  1.000 7.78882  ?  63  ALA   A N    1 
ATOM   530  C CA   . ALA   A 1 66  ? -8.68600  2.05800   -5.18500  1.000 6.82205  ?  63  ALA   A CA   1 
ATOM   531  C C    . ALA   A 1 66  ? -7.36700  1.62200   -4.55800  1.000 7.88443  ?  63  ALA   A C    1 
ATOM   532  O O    . ALA   A 1 66  ? -6.66800  0.76600   -5.12900  1.000 9.74594  ?  63  ALA   A O    1 
ATOM   533  C CB   . ALA   A 1 66  ? -8.42900  3.12500   -6.25200  1.000 10.25787 ?  63  ALA   A CB   1 
ATOM   534  N N    . THR   A 1 67  ? -6.99000  2.20800   -3.41700  1.000 5.85579  ?  64  THR   A N    1 
ATOM   535  C CA   . THR   A 1 67  ? -5.72300  1.87000   -2.77900  1.000 8.13997  ?  64  THR   A CA   1 
ATOM   536  C C    . THR   A 1 67  ? -5.88200  1.82300   -1.26400  1.000 7.43026  ?  64  THR   A C    1 
ATOM   537  O O    . THR   A 1 67  ? -6.81900  2.38700   -0.69100  1.000 7.24717  ?  64  THR   A O    1 
ATOM   538  C CB   . THR   A 1 67  ? -4.61400  2.87700   -3.10500  1.000 11.35970 ?  64  THR   A CB   1 
ATOM   539  O OG1  . THR   A 1 67  ? -4.85400  4.08800   -2.37600  1.000 10.59124 ?  64  THR   A OG1  1 
ATOM   540  C CG2  . THR   A 1 67  ? -4.57600  3.19100   -4.61200  1.000 13.31202 ?  64  THR   A CG2  1 
ATOM   541  N N    . VAL   A 1 68  ? -4.93700  1.12700   -0.62200  1.000 6.14134  ?  65  VAL   A N    1 
ATOM   542  C CA   . VAL   A 1 68  ? -4.91400  1.04200   0.84000   1.000 6.53850  ?  65  VAL   A CA   1 
ATOM   543  C C    . VAL   A 1 68  ? -4.61400  2.39500   1.46000   1.000 9.28737  ?  65  VAL   A C    1 
ATOM   544  O O    . VAL   A 1 68  ? -5.15800  2.73100   2.52200   1.000 6.76516  ?  65  VAL   A O    1 
ATOM   545  C CB   . VAL   A 1 68  ? -3.89800  -0.02500  1.30600   1.000 7.34345  ?  65  VAL   A CB   1 
ATOM   546  C CG1  . VAL   A 1 68  ? -3.66200  0.08800   2.82400   1.000 6.49405  ?  65  VAL   A CG1  1 
ATOM   547  C CG2  . VAL   A 1 68  ? -4.42100  -1.41700  0.92800   1.000 7.33871  ?  65  VAL   A CG2  1 
ATOM   548  N N    . GLU   A 1 69  ? -3.77500  3.21100   0.81000   1.000 8.06812  ?  66  GLU   A N    1 
ATOM   549  C CA   . GLU   A 1 69  ? -3.51400  4.54600   1.34100   1.000 9.04922  ?  66  GLU   A CA   1 
ATOM   550  C C    . GLU   A 1 69  ? -4.79200  5.35500   1.44200   1.000 10.17307 ?  66  GLU   A C    1 
ATOM   551  O O    . GLU   A 1 69  ? -4.94000  6.14600   2.37300   1.000 7.96719  ?  66  GLU   A O    1 
ATOM   552  C CB   . GLU   A 1 69  ? -2.48200  5.27000   0.47000   1.000 10.37796 ?  66  GLU   A CB   1 
ATOM   553  C CG   . GLU   A 1 69  ? -1.07800  4.73200   0.65900   1.000 17.05795 ?  66  GLU   A CG   1 
ATOM   554  C CD   . GLU   A 1 69  ? 0.01500   5.71800   0.27800   1.000 24.40448 ?  66  GLU   A CD   1 
ATOM   555  O OE1  . GLU   A 1 69  ? -0.29800  6.77900   -0.31900  1.000 23.10628 ?  66  GLU   A OE1  1 
ATOM   556  O OE2  . GLU   A 1 69  ? 1.19600   5.39300   0.54200   1.000 23.89327 -1 66  GLU   A OE2  1 
ATOM   557  N N    . GLU   A 1 70  ? -5.73200  5.15600   0.50400   1.000 7.35762  ?  67  GLU   A N    1 
ATOM   558  C CA   . GLU   A 1 70  ? -7.01400  5.85000   0.57500   1.000 5.28814  ?  67  GLU   A CA   1 
ATOM   559  C C    . GLU   A 1 70  ? -7.86200  5.33900   1.74100   1.000 5.50285  ?  67  GLU   A C    1 
ATOM   560  O O    . GLU   A 1 70  ? -8.56300  6.12300   2.39300   1.000 7.43468  ?  67  GLU   A O    1 
ATOM   561  C CB   . GLU   A 1 70  ? -7.75500  5.69400   -0.75600  1.000 7.40223  ?  67  GLU   A CB   1 
ATOM   562  C CG   . GLU   A 1 70  ? -7.10900  6.48200   -1.88900  1.000 9.45104  ?  67  GLU   A CG   1 
ATOM   563  C CD   . GLU   A 1 70  ? -7.68300  6.11000   -3.23600  1.000 13.70472 ?  67  GLU   A CD   1 
ATOM   564  O OE1  . GLU   A 1 70  ? -8.18500  4.98200   -3.38200  1.000 13.25874 ?  67  GLU   A OE1  1 
ATOM   565  O OE2  . GLU   A 1 70  ? -7.62800  6.95100   -4.14900  1.000 14.68395 -1 67  GLU   A OE2  1 
ATOM   566  N N    . VAL   A 1 71  ? -7.82200  4.02500   2.01600   1.000 6.94774  ?  68  VAL   A N    1 
ATOM   567  C CA   . VAL   A 1 71  ? -8.49900  3.51200   3.20900   1.000 5.60017  ?  68  VAL   A CA   1 
ATOM   568  C C    . VAL   A 1 71  ? -7.94200  4.19300   4.45400   1.000 5.70953  ?  68  VAL   A C    1 
ATOM   569  O O    . VAL   A 1 71  ? -8.69500  4.63500   5.33900   1.000 7.45285  ?  68  VAL   A O    1 
ATOM   570  C CB   . VAL   A 1 71  ? -8.35200  1.98300   3.31500   1.000 7.31714  ?  68  VAL   A CB   1 
ATOM   571  C CG1  . VAL   A 1 71  ? -9.06100  1.49200   4.58900   1.000 6.43763  ?  68  VAL   A CG1  1 
ATOM   572  C CG2  . VAL   A 1 71  ? -8.88700  1.27000   2.08000   1.000 5.71598  ?  68  VAL   A CG2  1 
ATOM   573  N N    . ASP   A 1 72  ? -6.60600  4.26400   4.54900   1.000 7.34252  ?  69  ASP   A N    1 
ATOM   574  C CA   . ASP   A 1 72  ? -5.95200  4.96900   5.65100   1.000 6.69576  ?  69  ASP   A CA   1 
ATOM   575  C C    . ASP   A 1 72  ? -6.45600  6.40200   5.77400   1.000 6.04487  ?  69  ASP   A C    1 
ATOM   576  O O    . ASP   A 1 72  ? -6.73900  6.88600   6.88000   1.000 8.04825  ?  69  ASP   A O    1 
ATOM   577  C CB   . ASP   A 1 72  ? -4.42700  4.98700   5.44400   1.000 4.22725  ?  69  ASP   A CB   1 
ATOM   578  C CG   . ASP   A 1 72  ? -3.76700  3.63100   5.59500   1.000 9.98644  ?  69  ASP   A CG   1 
ATOM   579  O OD1  . ASP   A 1 72  ? -4.39800  2.64600   6.02600   1.000 7.40421  ?  69  ASP   A OD1  1 
ATOM   580  O OD2  . ASP   A 1 72  ? -2.56000  3.57300   5.25700   1.000 10.38760 -1 69  ASP   A OD2  1 
ATOM   581  N N    . ALA   A 1 73  ? -6.55400  7.10800   4.64100   1.000 5.97095  ?  70  ALA   A N    1 
ATOM   582  C CA   . ALA   A 1 73  ? -7.01200  8.49300   4.67200   1.000 6.11225  ?  70  ALA   A CA   1 
ATOM   583  C C    . ALA   A 1 73  ? -8.42500  8.57200   5.22200   1.000 4.95451  ?  70  ALA   A C    1 
ATOM   584  O O    . ALA   A 1 73  ? -8.74600  9.44800   6.03800   1.000 9.29127  ?  70  ALA   A O    1 
ATOM   585  C CB   . ALA   A 1 73  ? -6.96500  9.09400   3.26400   1.000 8.50762  ?  70  ALA   A CB   1 
ATOM   586  N N    . ALA   A 1 74  ? -9.27900  7.64700   4.79900   1.000 4.96541  ?  71  ALA   A N    1 
ATOM   587  C CA   . ALA   A 1 74  ? -10.64700 7.67800   5.29200   1.000 6.35568  ?  71  ALA   A CA   1 
ATOM   588  C C    . ALA   A 1 74  ? -10.69000 7.39600   6.79200   1.000 6.11811  ?  71  ALA   A C    1 
ATOM   589  O O    . ALA   A 1 74  ? -11.37800 8.09900   7.53300   1.000 7.51786  ?  71  ALA   A O    1 
ATOM   590  C CB   . ALA   A 1 74  ? -11.49800 6.67600   4.51000   1.000 7.33892  ?  71  ALA   A CB   1 
ATOM   591  N N    . MET   A 1 75  ? -9.97400  6.36300   7.26700   1.000 6.24558  ?  72  MET   A N    1 
ATOM   592  C CA   . MET   A 1 75  ? -9.92500  6.11800   8.71300   1.000 5.65427  ?  72  MET   A CA   1 
ATOM   593  C C    . MET   A 1 75  ? -9.34000  7.28800   9.46800   1.000 9.15310  ?  72  MET   A C    1 
ATOM   594  O O    . MET   A 1 75  ? -9.77800  7.57800   10.58800  1.000 9.43396  ?  72  MET   A O    1 
ATOM   595  C CB   . MET   A 1 75  ? -9.17900  4.79500   8.99200   1.000 5.37307  ?  72  MET   A CB   1 
ATOM   596  C CG   . MET   A 1 75  ? -9.94200  3.64900   8.35600   1.000 6.37080  ?  72  MET   A CG   1 
ATOM   597  S SD   . MET   A 1 75  ? -11.59300 3.40100   9.08000   1.000 7.64863  ?  72  MET   A SD   1 
ATOM   598  C CE   . MET   A 1 75  ? -11.17800 2.92500   10.80900  1.000 4.56174  ?  72  MET   A CE   1 
ATOM   599  N N    . ASN   A 1 76  ? -8.33500  7.95500   8.90500   1.000 7.52717  ?  73  ASN   A N    1 
ATOM   600  C CA   . ASN   A 1 76  ? -7.74200  9.06000   9.64400   1.000 9.47666  ?  73  ASN   A CA   1 
ATOM   601  C C    . ASN   A 1 76  ? -8.67000  10.26300  9.70600   1.000 10.28474 ?  73  ASN   A C    1 
ATOM   602  O O    . ASN   A 1 76  ? -8.47800  11.13700  10.56100  1.000 12.89238 ?  73  ASN   A O    1 
ATOM   603  C CB   . ASN   A 1 76  ? -6.39700  9.45900   9.03000   1.000 11.83504 ?  73  ASN   A CB   1 
ATOM   604  C CG   . ASN   A 1 76  ? -5.34100  8.38100   9.20700   1.000 13.73715 ?  73  ASN   A CG   1 
ATOM   605  O OD1  . ASN   A 1 76  ? -5.48800  7.49300   10.04100  1.000 16.21094 ?  73  ASN   A OD1  1 
ATOM   606  N ND2  . ASN   A 1 76  ? -4.26400  8.45900   8.42100   1.000 16.86962 ?  73  ASN   A ND2  1 
ATOM   607  N N    . ALA   A 1 77  ? -9.70100  10.30400  8.86000   1.000 8.44694  ?  74  ALA   A N    1 
ATOM   608  C CA   . ALA   A 1 77  ? -10.66400 11.39600  8.86900   1.000 10.10620 ?  74  ALA   A CA   1 
ATOM   609  C C    . ALA   A 1 77  ? -11.88200 11.14000  9.76400   1.000 8.60391  ?  74  ALA   A C    1 
ATOM   610  O O    . ALA   A 1 77  ? -12.80900 11.96400  9.76500   1.000 10.40689 ?  74  ALA   A O    1 
ATOM   611  C CB   . ALA   A 1 77  ? -11.11300 11.69100  7.43400   1.000 9.82194  ?  74  ALA   A CB   1 
ATOM   612  N N    . ARG   A 1 78  ? -11.90100 10.04500  10.52900  1.000 7.10361  ?  75  ARG   A N    1 
ATOM   613  C CA   . ARG   A 1 78  ? -12.95700 9.84300   11.51100  1.000 8.87818  ?  75  ARG   A CA   1 
ATOM   614  C C    . ARG   A 1 78  ? -12.87600 10.95200  12.55400  1.000 9.40174  ?  75  ARG   A C    1 
ATOM   615  O O    . ARG   A 1 78  ? -11.79000 11.48900  12.80900  1.000 9.17651  ?  75  ARG   A O    1 
ATOM   616  C CB   . ARG   A 1 78  ? -12.81600 8.47700   12.19300  1.000 7.37792  ?  75  ARG   A CB   1 
ATOM   617  C CG   . ARG   A 1 78  ? -13.14600 7.28400   11.27800  1.000 5.63588  ?  75  ARG   A CG   1 
ATOM   618  C CD   . ARG   A 1 78  ? -12.76000 5.95600   11.93800  1.000 6.27587  ?  75  ARG   A CD   1 
ATOM   619  N NE   . ARG   A 1 78  ? -11.32900 5.90600   12.22500  1.000 6.47080  ?  75  ARG   A NE   1 
ATOM   620  C CZ   . ARG   A 1 78  ? -10.79600 5.23200   13.24300  1.000 8.66035  ?  75  ARG   A CZ   1 
ATOM   621  N NH1  . ARG   A 1 78  ? -11.53400 4.48000   14.04400  1.000 10.42354 ?  75  ARG   A NH1  1 
ATOM   622  N NH2  . ARG   A 1 78  ? -9.48600  5.31900   13.46500  1.000 9.57968  ?  75  ARG   A NH2  1 
ATOM   623  N N    . PRO   A 1 79  ? -13.99200 11.27400  13.20900  1.000 8.70152  ?  76  PRO   A N    1 
ATOM   624  C CA   . PRO   A 1 79  ? -15.32800 10.68500  13.02200  1.000 8.05954  ?  76  PRO   A CA   1 
ATOM   625  C C    . PRO   A 1 79  ? -15.97700 11.16000  11.75100  1.000 8.60887  ?  76  PRO   A C    1 
ATOM   626  O O    . PRO   A 1 79  ? -15.83700 12.32500  11.37500  1.000 11.38201 ?  76  PRO   A O    1 
ATOM   627  C CB   . PRO   A 1 79  ? -16.11100 11.16000  14.26200  1.000 10.90097 ?  76  PRO   A CB   1 
ATOM   628  C CG   . PRO   A 1 79  ? -15.04700 11.64000  15.23900  1.000 15.56114 ?  76  PRO   A CG   1 
ATOM   629  C CD   . PRO   A 1 79  ? -13.96400 12.18100  14.36500  1.000 10.77323 ?  76  PRO   A CD   1 
ATOM   630  N N    . HIS   A 1 80  ? -16.69700 10.25900  11.08600  1.000 5.33576  ?  77  HIS   A N    1 
ATOM   631  C CA   . HIS   A 1 80  ? -17.44600 10.56300  9.87500   1.000 5.74447  ?  77  HIS   A CA   1 
ATOM   632  C C    . HIS   A 1 80  ? -18.91300 10.74100  10.22700  1.000 9.36654  ?  77  HIS   A C    1 
ATOM   633  O O    . HIS   A 1 80  ? -19.53500 9.83400   10.78200  1.000 10.72820 ?  77  HIS   A O    1 
ATOM   634  C CB   . HIS   A 1 80  ? -17.27700 9.43100   8.86800   1.000 6.05552  ?  77  HIS   A CB   1 
ATOM   635  C CG   . HIS   A 1 80  ? -15.94700 9.43300   8.20200   1.000 8.46113  ?  77  HIS   A CG   1 
ATOM   636  N ND1  . HIS   A 1 80  ? -15.62900 10.30700  7.18800   1.000 10.90620 ?  77  HIS   A ND1  1 
ATOM   637  C CD2  . HIS   A 1 80  ? -14.82800 8.71300   8.45100   1.000 5.41076  ?  77  HIS   A CD2  1 
ATOM   638  C CE1  . HIS   A 1 80  ? -14.37700 10.09500  6.80700   1.000 9.52078  ?  77  HIS   A CE1  1 
ATOM   639  N NE2  . HIS   A 1 80  ? -13.86700 9.13700   7.56600   1.000 5.96563  ?  77  HIS   A NE2  1 
ATOM   640  N N    . LYS   A 1 81  ? -19.44800 11.91100  9.93200   1.000 7.09052  ?  78  LYS   A N    1 
ATOM   641  C CA   . LYS   A 1 81  ? -20.87300 12.17800  10.04000  1.000 9.00808  ?  78  LYS   A CA   1 
ATOM   642  C C    . LYS   A 1 81  ? -21.43000 12.12700  8.63300   1.000 8.77598  ?  78  LYS   A C    1 
ATOM   643  O O    . LYS   A 1 81  ? -21.06800 12.95900  7.79400   1.000 11.64272 ?  78  LYS   A O    1 
ATOM   644  C CB   . LYS   A 1 81  ? -21.13200 13.53700  10.67700  1.000 9.70798  ?  78  LYS   A CB   1 
ATOM   645  C CG   . LYS   A 1 81  ? -22.56600 13.73900  11.14300  1.000 14.65809 ?  78  LYS   A CG   1 
ATOM   646  C CD   . LYS   A 1 81  ? -22.67200 15.05900  11.91600  1.000 17.18925 ?  78  LYS   A CD   1 
ATOM   647  C CE   . LYS   A 1 81  ? -22.33500 16.25400  11.03300  1.000 28.27683 ?  78  LYS   A CE   1 
ATOM   648  N NZ   . LYS   A 1 81  ? -23.27100 16.44100  9.88400   1.000 31.02821 ?  78  LYS   A NZ   1 
ATOM   649  N N    . VAL   A 1 82  ? -22.29500 11.14600  8.37400   1.000 7.62609  ?  79  VAL   A N    1 
ATOM   650  C CA   . VAL   A 1 82  ? -22.82400 10.87800  7.04300   1.000 7.38542  ?  79  VAL   A CA   1 
ATOM   651  C C    . VAL   A 1 82  ? -24.32200 11.07000  7.11600   1.000 7.40284  ?  79  VAL   A C    1 
ATOM   652  O O    . VAL   A 1 82  ? -25.00100 10.36600  7.87300   1.000 9.15042  ?  79  VAL   A O    1 
ATOM   653  C CB   . VAL   A 1 82  ? -22.48400 9.45200   6.57100   1.000 7.79002  ?  79  VAL   A CB   1 
ATOM   654  C CG1  . VAL   A 1 82  ? -23.02000 9.19100   5.16200   1.000 8.35125  ?  79  VAL   A CG1  1 
ATOM   655  C CG2  . VAL   A 1 82  ? -20.98000 9.25500   6.60800   1.000 10.74550 ?  79  VAL   A CG2  1 
ATOM   656  N N    . ASP   A 1 83  ? -24.83400 12.02300  6.34100   1.000 10.79444 ?  80  ASP   A N    1 
ATOM   657  C CA   . ASP   A 1 83  ? -26.26100 12.33100  6.36100   1.000 8.90819  ?  80  ASP   A CA   1 
ATOM   658  C C    . ASP   A 1 83  ? -26.76500 12.54000  7.78400   1.000 10.92189 ?  80  ASP   A C    1 
ATOM   659  O O    . ASP   A 1 83  ? -27.84900 12.07900  8.15400   1.000 13.70149 ?  80  ASP   A O    1 
ATOM   660  C CB   . ASP   A 1 83  ? -27.06400 11.23700  5.65200   1.000 8.94377  ?  80  ASP   A CB   1 
ATOM   661  C CG   . ASP   A 1 83  ? -26.61100 11.02300  4.22000   1.000 13.92992 ?  80  ASP   A CG   1 
ATOM   662  O OD1  . ASP   A 1 83  ? -26.39400 12.02800  3.50100   1.000 14.68351 ?  80  ASP   A OD1  1 
ATOM   663  O OD2  . ASP   A 1 83  ? -26.45400 9.85400   3.80500   1.000 10.35006 -1 80  ASP   A OD2  1 
ATOM   664  N N    . GLY   A 1 84  ? -25.95300 13.22100  8.60900   1.000 10.78448 ?  81  GLY   A N    1 
ATOM   665  C CA   . GLY   A 1 84  ? -26.37100 13.64900  9.92700   1.000 13.16410 ?  81  GLY   A CA   1 
ATOM   666  C C    . GLY   A 1 84  ? -26.09600 12.68100  11.06200  1.000 18.56251 ?  81  GLY   A C    1 
ATOM   667  O O    . GLY   A 1 84  ? -26.40400 13.00600  12.21900  1.000 17.74260 ?  81  GLY   A O    1 
ATOM   668  N N    . ARG   A 1 85  ? -25.51800 11.51200  10.78200  1.000 9.43387  ?  82  ARG   A N    1 
ATOM   669  C CA   . ARG   A 1 85  ? -25.29800 10.49000  11.79800  1.000 10.77901 ?  82  ARG   A CA   1 
ATOM   670  C C    . ARG   A 1 85  ? -23.82600 10.09600  11.81200  1.000 9.10687  ?  82  ARG   A C    1 
ATOM   671  O O    . ARG   A 1 85  ? -23.23500 9.88800   10.74900  1.000 10.42587 ?  82  ARG   A O    1 
ATOM   672  C CB   . ARG   A 1 85  ? -26.17000 9.26200   11.49900  1.000 11.18079 ?  82  ARG   A CB   1 
ATOM   673  C CG   . ARG   A 1 85  ? -26.16300 8.22700   12.57600  1.000 16.84139 ?  82  ARG   A CG   1 
ATOM   674  C CD   . ARG   A 1 85  ? -27.20500 7.16600   12.27000  1.000 20.52859 ?  82  ARG   A CD   1 
ATOM   675  N NE   . ARG   A 1 85  ? -28.49300 7.64900   12.72900  1.000 33.06174 ?  82  ARG   A NE   1 
ATOM   676  C CZ   . ARG   A 1 85  ? -29.05800 7.31700   13.87800  1.000 18.10261 ?  82  ARG   A CZ   1 
ATOM   677  N NH1  . ARG   A 1 85  ? -28.57800 6.34200   14.63000  1.000 25.20609 ?  82  ARG   A NH1  1 
ATOM   678  N NH2  . ARG   A 1 85  ? -30.15000 7.96500   14.26500  1.000 21.27086 ?  82  ARG   A NH2  1 
ATOM   679  N N    . VAL   A 1 86  ? -23.23100 9.99900   13.00400  1.000 8.08464  ?  83  VAL   A N    1 
ATOM   680  C CA   . VAL   A 1 86  ? -21.85300 9.51300   13.08300  1.000 9.78778  ?  83  VAL   A CA   1 
ATOM   681  C C    . VAL   A 1 86  ? -21.86300 8.00900   12.82900  1.000 9.52748  ?  83  VAL   A C    1 
ATOM   682  O O    . VAL   A 1 86  ? -22.55500 7.25200   13.52100  1.000 13.04403 ?  83  VAL   A O    1 
ATOM   683  C CB   . VAL   A 1 86  ? -21.21300 9.84700   14.43500  1.000 11.80881 ?  83  VAL   A CB   1 
ATOM   684  C CG1  . VAL   A 1 86  ? -19.81600 9.21900   14.52000  1.000 13.06139 ?  83  VAL   A CG1  1 
ATOM   685  C CG2  . VAL   A 1 86  ? -21.15000 11.33900  14.62700  1.000 15.45286 ?  83  VAL   A CG2  1 
ATOM   686  N N    . VAL   A 1 87  ? -21.11100 7.57300   11.81900  1.000 8.07472  ?  84  VAL   A N    1 
ATOM   687  C CA   . VAL   A 1 87  ? -21.10800 6.17200   11.41500  1.000 7.26385  ?  84  VAL   A CA   1 
ATOM   688  C C    . VAL   A 1 87  ? -19.85800 5.49400   11.97100  1.000 9.33449  ?  84  VAL   A C    1 
ATOM   689  O O    . VAL   A 1 87  ? -19.01600 6.14100   12.61700  1.000 10.35063 ?  84  VAL   A O    1 
ATOM   690  C CB   . VAL   A 1 87  ? -21.18600 6.05600   9.88700   1.000 6.18943  ?  84  VAL   A CB   1 
ATOM   691  C CG1  . VAL   A 1 87  ? -22.46800 6.70500   9.38100   1.000 7.74115  ?  84  VAL   A CG1  1 
ATOM   692  C CG2  . VAL   A 1 87  ? -19.94500 6.67700   9.23500   1.000 7.66823  ?  84  VAL   A CG2  1 
ATOM   693  N N    . GLU   A 1 88  ? -19.72300 4.18900   11.73200  1.000 7.24102  ?  85  GLU   A N    1 
ATOM   694  C CA   . GLU   A 1 88  ? -18.65400 3.39900   12.34700  1.000 8.80632  ?  85  GLU   A CA   1 
ATOM   695  C C    . GLU   A 1 88  ? -17.91600 2.62300   11.26400  1.000 6.98907  ?  85  GLU   A C    1 
ATOM   696  O O    . GLU   A 1 88  ? -18.28900 1.49400   10.93000  1.000 8.50909  ?  85  GLU   A O    1 
ATOM   697  C CB   . GLU   A 1 88  ? -19.21400 2.45100   13.41000  1.000 12.10017 ?  85  GLU   A CB   1 
ATOM   698  C CG   . GLU   A 1 88  ? -18.11500 1.69500   14.14900  1.000 18.09577 ?  85  GLU   A CG   1 
ATOM   699  C CD   . GLU   A 1 88  ? -18.65200 0.75900   15.22300  1.000 33.20854 ?  85  GLU   A CD   1 
ATOM   700  O OE1  . GLU   A 1 88  ? -19.88500 0.64800   15.36100  1.000 35.05012 ?  85  GLU   A OE1  1 
ATOM   701  O OE2  . GLU   A 1 88  ? -17.83900 0.14400   15.94100  1.000 33.53993 -1 85  GLU   A OE2  1 
ATOM   702  N N    . PRO   A 1 89  ? -16.85600 3.19100   10.69100  1.000 8.32204  ?  86  PRO   A N    1 
ATOM   703  C CA   . PRO   A 1 89  ? -16.11900 2.46700   9.65100   1.000 10.50068 ?  86  PRO   A CA   1 
ATOM   704  C C    . PRO   A 1 89  ? -15.13400 1.50100   10.27800  1.000 9.93708  ?  86  PRO   A C    1 
ATOM   705  O O    . PRO   A 1 89  ? -14.50300 1.80300   11.29900  1.000 10.32594 ?  86  PRO   A O    1 
ATOM   706  C CB   . PRO   A 1 89  ? -15.38900 3.58000   8.88300   1.000 10.76344 ?  86  PRO   A CB   1 
ATOM   707  C CG   . PRO   A 1 89  ? -15.92600 4.89700   9.45700   1.000 11.81418 ?  86  PRO   A CG   1 
ATOM   708  C CD   . PRO   A 1 89  ? -16.36100 4.56600   10.84700  1.000 8.00175  ?  86  PRO   A CD   1 
ATOM   709  N N    . LYS   A 1 90  ? -15.00400 0.33000   9.65800   1.000 7.17415  ?  87  LYS   A N    1 
ATOM   710  C CA   . LYS   A 1 90  ? -14.01100 -0.65300  10.08900  1.000 4.41275  ?  87  LYS   A CA   1 
ATOM   711  C C    . LYS   A 1 90  ? -13.47100 -1.37300  8.86200   1.000 7.24702  ?  87  LYS   A C    1 
ATOM   712  O O    . LYS   A 1 90  ? -14.21100 -1.63900  7.91900   1.000 7.71523  ?  87  LYS   A O    1 
ATOM   713  C CB   . LYS   A 1 90  ? -14.60600 -1.69300  11.02800  1.000 11.12453 ?  87  LYS   A CB   1 
ATOM   714  C CG   . LYS   A 1 90  ? -15.19000 -1.16000  12.31600  1.000 15.99394 ?  87  LYS   A CG   1 
ATOM   715  C CD   . LYS   A 1 90  ? -15.84200 -2.32800  13.04600  1.000 26.20038 ?  87  LYS   A CD   1 
ATOM   716  C CE   . LYS   A 1 90  ? -16.25600 -1.97200  14.45700  1.000 36.07812 ?  87  LYS   A CE   1 
ATOM   717  N NZ   . LYS   A 1 90  ? -16.83700 -3.17000  15.13000  1.000 32.68494 ?  87  LYS   A NZ   1 
ATOM   718  H HA   . LYS   A 1 90  ? -13.29000 -0.19300  10.54600  1.000 5.29530  ?  87  LYS   A HA   1 
ATOM   719  H HB2  . LYS   A 1 90  ? -15.32000 -2.15300  10.55800  1.000 13.34944 ?  87  LYS   A HB2  1 
ATOM   720  H HB3  . LYS   A 1 90  ? -13.90700 -2.32100  11.26700  1.000 13.34944 ?  87  LYS   A HB3  1 
ATOM   721  H HG2  . LYS   A 1 90  ? -14.48900 -0.78500  12.87200  1.000 19.19273 ?  87  LYS   A HG2  1 
ATOM   722  H HG3  . LYS   A 1 90  ? -15.86100 -0.48500  12.12700  1.000 19.19273 ?  87  LYS   A HG3  1 
ATOM   723  H HD2  . LYS   A 1 90  ? -16.63500 -2.60300  12.56000  1.000 31.44045 ?  87  LYS   A HD2  1 
ATOM   724  H HD3  . LYS   A 1 90  ? -15.21100 -3.06400  13.09400  1.000 31.44045 ?  87  LYS   A HD3  1 
ATOM   725  H HE2  . LYS   A 1 90  ? -15.48100 -1.67600  14.96000  1.000 43.29374 ?  87  LYS   A HE2  1 
ATOM   726  H HE3  . LYS   A 1 90  ? -16.92500 -1.27100  14.43500  1.000 43.29374 ?  87  LYS   A HE3  1 
ATOM   727  H HZ1  . LYS   A 1 90  ? -16.63400 -3.16100  15.99700  1.000 39.22193 ?  87  LYS   A HZ1  1 
ATOM   728  H HZ2  . LYS   A 1 90  ? -17.72300 -3.17000  15.04100  1.000 39.22193 ?  87  LYS   A HZ2  1 
ATOM   729  H HZ3  . LYS   A 1 90  ? -16.51000 -3.91300  14.76500  1.000 39.22193 ?  87  LYS   A HZ3  1 
ATOM   730  N N    . ARG   A 1 91  ? -12.19500 -1.73400  8.88200   1.000 6.10570  ?  88  ARG   A N    1 
ATOM   731  C CA   . ARG   A 1 91  ? -11.67600 -2.53600  7.78600   1.000 8.46389  ?  88  ARG   A CA   1 
ATOM   732  C C    . ARG   A 1 91  ? -12.32500 -3.91900  7.78800   1.000 12.19834 ?  88  ARG   A C    1 
ATOM   733  O O    . ARG   A 1 91  ? -12.67900 -4.46600  8.83400   1.000 14.75834 ?  88  ARG   A O    1 
ATOM   734  C CB   . ARG   A 1 91  ? -10.15800 -2.66000  7.87700   1.000 10.36756 ?  88  ARG   A CB   1 
ATOM   735  C CG   . ARG   A 1 91  ? -9.47400  -1.33300  7.70600   1.000 7.79050  ?  88  ARG   A CG   1 
ATOM   736  C CD   . ARG   A 1 91  ? -7.95900  -1.40900  7.96700   1.000 7.88196  ?  88  ARG   A CD   1 
ATOM   737  N NE   . ARG   A 1 91  ? -7.45600  -0.08000  8.26200   1.000 7.44100  ?  88  ARG   A NE   1 
ATOM   738  C CZ   . ARG   A 1 91  ? -6.73800  0.68300   7.45700   1.000 6.76369  ?  88  ARG   A CZ   1 
ATOM   739  N NH1  . ARG   A 1 91  ? -6.29000  0.23400   6.29400   1.000 9.02183  ?  88  ARG   A NH1  1 
ATOM   740  N NH2  . ARG   A 1 91  ? -6.44500  1.92700   7.84400   1.000 7.27014  ?  88  ARG   A NH2  1 
ATOM   741  H H    . ARG   A 1 91  ? -11.62900 -1.53400  9.49800   1.000 7.32684  ?  88  ARG   A H    1 
ATOM   742  H HA   . ARG   A 1 91  ? -11.88200 -2.10500  6.94200   1.000 10.15667 ?  88  ARG   A HA   1 
ATOM   743  H HB2  . ARG   A 1 91  ? -9.91900  -3.01500  8.74800   1.000 12.44107 ?  88  ARG   A HB2  1 
ATOM   744  H HB3  . ARG   A 1 91  ? -9.84400  -3.25600  7.17900   1.000 12.44107 ?  88  ARG   A HB3  1 
ATOM   745  H HG2  . ARG   A 1 91  ? -9.60700  -1.02300  6.79700   1.000 9.34860  ?  88  ARG   A HG2  1 
ATOM   746  H HG3  . ARG   A 1 91  ? -9.85500  -0.69800  8.33200   1.000 9.34860  ?  88  ARG   A HG3  1 
ATOM   747  H HD2  . ARG   A 1 91  ? -7.78400  -1.98700  8.72700   1.000 9.45835  ?  88  ARG   A HD2  1 
ATOM   748  H HD3  . ARG   A 1 91  ? -7.50600  -1.75000  7.18000   1.000 9.45835  ?  88  ARG   A HD3  1 
ATOM   749  H HE   . ARG   A 1 91  ? -7.64500  0.24300   9.03600   1.000 8.92920  ?  88  ARG   A HE   1 
ATOM   750  H HH11 . ARG   A 1 91  ? -6.46600  -0.57100  6.04700   1.000 10.82619 ?  88  ARG   A HH11 1 
ATOM   751  H HH12 . ARG   A 1 91  ? -5.82400  0.74700   5.78500   1.000 10.82619 ?  88  ARG   A HH12 1 
ATOM   752  H HH21 . ARG   A 1 91  ? -6.72400  2.21900   8.60300   1.000 8.72417  ?  88  ARG   A HH21 1 
ATOM   753  H HH22 . ARG   A 1 91  ? -5.97800  2.43800   7.33200   1.000 8.72417  ?  88  ARG   A HH22 1 
ATOM   754  N N    . ALA   A 1 92  ? -12.50000 -4.47000  6.59300   1.000 16.05725 ?  89  ALA   A N    1 
ATOM   755  C CA   . ALA   A 1 92  ? -13.08100 -5.79700  6.44200   1.000 21.64637 ?  89  ALA   A CA   1 
ATOM   756  C C    . ALA   A 1 92  ? -12.29600 -6.83000  7.24200   1.000 32.48184 ?  89  ALA   A C    1 
ATOM   757  O O    . ALA   A 1 92  ? -11.10700 -6.66600  7.53000   1.000 29.78208 ?  89  ALA   A O    1 
ATOM   758  C CB   . ALA   A 1 92  ? -13.10700 -6.20200  4.96900   1.000 22.17568 ?  89  ALA   A CB   1 
ATOM   759  H H    . ALA   A 1 92  ? -12.29000 -4.09500  5.84900   1.000 19.26870 ?  89  ALA   A H    1 
ATOM   760  H HA   . ALA   A 1 92  ? -13.99100 -5.78300  6.77600   1.000 25.97564 ?  89  ALA   A HA   1 
ATOM   761  H HB1  . ALA   A 1 92  ? -13.50100 -7.08400  4.89100   1.000 26.61081 ?  89  ALA   A HB1  1 
ATOM   762  H HB2  . ALA   A 1 92  ? -13.63700 -5.55800  4.47400   1.000 26.61081 ?  89  ALA   A HB2  1 
ATOM   763  H HB3  . ALA   A 1 92  ? -12.19900 -6.21400  4.62800   1.000 26.61081 ?  89  ALA   A HB3  1 
ATOM   764  N N    . VAL   A 1 93  ? -12.97700 -7.92600  7.58600   1.000 37.00333 ?  90  VAL   A N    1 
ATOM   765  C CA   . VAL   A 1 93  ? -12.38400 -8.91900  8.48500   1.000 37.35891 ?  90  VAL   A CA   1 
ATOM   766  C C    . VAL   A 1 93  ? -11.25900 -9.67900  7.78200   1.000 41.02145 ?  90  VAL   A C    1 
ATOM   767  O O    . VAL   A 1 93  ? -11.21600 -9.80600  6.54900   1.000 29.17908 ?  90  VAL   A O    1 
ATOM   768  C CB   . VAL   A 1 93  ? -13.46100 -9.88800  9.00300   1.000 43.65225 ?  90  VAL   A CB   1 
ATOM   769  C CG1  . VAL   A 1 93  ? -14.55700 -9.13300  9.74600   1.000 30.34684 ?  90  VAL   A CG1  1 
ATOM   770  C CG2  . VAL   A 1 93  ? -14.03600 -10.70100 7.84500   1.000 33.86737 ?  90  VAL   A CG2  1 
ATOM   771  H H    . VAL   A 1 93  ? -13.77200 -8.11600  7.31800   1.000 44.40400 ?  90  VAL   A H    1 
ATOM   772  H HA   . VAL   A 1 93  ? -11.99400 -8.45600  9.24300   1.000 44.83069 ?  90  VAL   A HA   1 
ATOM   773  H HB   . VAL   A 1 93  ? -13.05700 -10.50500 9.63300   1.000 52.38270 ?  90  VAL   A HB   1 
ATOM   774  H HG11 . VAL   A 1 93  ? -15.20900 -9.77000  10.07800  1.000 36.41621 ?  90  VAL   A HG11 1 
ATOM   775  H HG12 . VAL   A 1 93  ? -14.16000 -8.65000  10.48800  1.000 36.41621 ?  90  VAL   A HG12 1 
ATOM   776  H HG13 . VAL   A 1 93  ? -14.98200 -8.51100  9.13500   1.000 36.41621 ?  90  VAL   A HG13 1 
ATOM   777  H HG21 . VAL   A 1 93  ? -14.73600 -11.28100 8.18400   1.000 40.64085 ?  90  VAL   A HG21 1 
ATOM   778  H HG22 . VAL   A 1 93  ? -14.40200 -10.09300 7.18300   1.000 40.64085 ?  90  VAL   A HG22 1 
ATOM   779  H HG23 . VAL   A 1 93  ? -13.32800 -11.23300 7.45000   1.000 40.64085 ?  90  VAL   A HG23 1 
ATOM   780  N N    . SER   A 1 94  ? -10.34600 -10.21600 8.59500   1.000 39.94494 ?  91  SER   A N    1 
ATOM   781  C CA   . SER   A 1 94  ? -9.19400  -10.97200 8.10000   1.000 42.73772 ?  91  SER   A CA   1 
ATOM   782  C C    . SER   A 1 94  ? -9.08400  -12.34500 8.76300   1.000 38.14855 ?  91  SER   A C    1 
ATOM   783  O O    . SER   A 1 94  ? -9.82000  -12.65300 9.70600   1.000 45.93525 ?  91  SER   A O    1 
ATOM   784  C CB   . SER   A 1 94  ? -7.90400  -10.18000 8.32700   1.000 42.26608 ?  91  SER   A CB   1 
ATOM   785  O OG   . SER   A 1 94  ? -7.64600  -10.00900 9.71200   1.000 46.97605 ?  91  SER   A OG   1 
ATOM   786  N N    . HIS   A 1 104 ? -16.02700 -9.12400  12.92600  1.000 37.55394 ?  101 HIS   A N    1 
ATOM   787  C CA   . HIS   A 1 104 ? -14.87600 -8.29900  13.28300  1.000 38.78990 ?  101 HIS   A CA   1 
ATOM   788  C C    . HIS   A 1 104 ? -14.64900 -8.37200  14.78700  1.000 40.20126 ?  101 HIS   A C    1 
ATOM   789  O O    . HIS   A 1 104 ? -15.52900 -8.03600  15.58600  1.000 38.76371 ?  101 HIS   A O    1 
ATOM   790  C CB   . HIS   A 1 104 ? -15.09700 -6.85900  12.81300  1.000 40.34417 ?  101 HIS   A CB   1 
ATOM   791  C CG   . HIS   A 1 104 ? -13.85700 -6.00900  12.79700  1.000 33.91717 ?  101 HIS   A CG   1 
ATOM   792  N ND1  . HIS   A 1 104 ? -13.25900 -5.52100  13.94100  1.000 34.32744 ?  101 HIS   A ND1  1 
ATOM   793  C CD2  . HIS   A 1 104 ? -13.09600 -5.57300  11.76400  1.000 38.15877 ?  101 HIS   A CD2  1 
ATOM   794  C CE1  . HIS   A 1 104 ? -12.20100 -4.79800  13.61100  1.000 21.92947 ?  101 HIS   A CE1  1 
ATOM   795  N NE2  . HIS   A 1 104 ? -12.07800 -4.81700  12.29500  1.000 34.15119 ?  101 HIS   A NE2  1 
ATOM   796  H HA   . HIS   A 1 104 ? -14.07200 -8.61700  12.84400  1.000 46.54788 ?  101 HIS   A HA   1 
ATOM   797  H HB2  . HIS   A 1 104 ? -15.44900 -6.88000  11.91000  1.000 48.41301 ?  101 HIS   A HB2  1 
ATOM   798  H HB3  . HIS   A 1 104 ? -15.73400 -6.43500  13.40800  1.000 48.41301 ?  101 HIS   A HB3  1 
ATOM   799  H HD2  . HIS   A 1 104 ? -13.23600 -5.75300  10.86200  1.000 45.79052 ?  101 HIS   A HD2  1 
ATOM   800  H HE1  . HIS   A 1 104 ? -11.64000 -4.35200  14.20300  1.000 26.31536 ?  101 HIS   A HE1  1 
ATOM   801  H HE2  . HIS   A 1 104 ? -11.46200 -4.42100  11.84500  1.000 40.98143 ?  101 HIS   A HE2  1 
ATOM   802  N N    . LEU   A 1 105 ? -13.46900 -8.85700  15.16300  1.000 30.59818 ?  102 LEU   A N    1 
ATOM   803  C CA   . LEU   A 1 105 ? -13.01200 -8.82600  16.54900  1.000 34.36075 ?  102 LEU   A CA   1 
ATOM   804  C C    . LEU   A 1 105 ? -12.33100 -7.48000  16.76400  1.000 25.04109 ?  102 LEU   A C    1 
ATOM   805  O O    . LEU   A 1 105 ? -11.18100 -7.28300  16.36500  1.000 30.06395 ?  102 LEU   A O    1 
ATOM   806  C CB   . LEU   A 1 105 ? -12.08000 -9.99800  16.82700  1.000 29.41677 ?  102 LEU   A CB   1 
ATOM   807  C CG   . LEU   A 1 105 ? -11.23100 -9.91800  18.09400  1.000 35.81021 ?  102 LEU   A CG   1 
ATOM   808  C CD1  . LEU   A 1 105 ? -12.08400 -10.28900 19.29300  1.000 39.43971 ?  102 LEU   A CD1  1 
ATOM   809  C CD2  . LEU   A 1 105 ? -10.02000 -10.84200 17.98100  1.000 38.06621 ?  102 LEU   A CD2  1 
ATOM   810  N N    . THR   A 1 106 ? -13.04600 -6.54100  17.37800  1.000 19.29727 ?  103 THR   A N    1 
ATOM   811  C CA   . THR   A 1 106 ? -12.60200 -5.14700  17.44200  1.000 19.57462 ?  103 THR   A CA   1 
ATOM   812  C C    . THR   A 1 106 ? -11.94600 -4.86800  18.78900  1.000 20.31395 ?  103 THR   A C    1 
ATOM   813  O O    . THR   A 1 106 ? -12.63200 -4.61500  19.78000  1.000 23.05343 ?  103 THR   A O    1 
ATOM   814  C CB   . THR   A 1 106 ? -13.76800 -4.19100  17.21300  1.000 27.68416 ?  103 THR   A CB   1 
ATOM   815  O OG1  . THR   A 1 106 ? -14.48100 -4.58000  16.03400  1.000 29.85298 ?  103 THR   A OG1  1 
ATOM   816  C CG2  . THR   A 1 106 ? -13.27500 -2.75800  17.06300  1.000 26.19246 ?  103 THR   A CG2  1 
ATOM   817  H HA   . THR   A 1 106 ? -11.93300 -5.02300  16.75100  1.000 23.48955 ?  103 THR   A HA   1 
ATOM   818  H HB   . THR   A 1 106 ? -14.36500 -4.22200  17.97700  1.000 33.22099 ?  103 THR   A HB   1 
ATOM   819  H HG1  . THR   A 1 106 ? -14.39400 -5.40600  15.90500  1.000 35.82358 ?  103 THR   A HG1  1 
ATOM   820  H HG21 . THR   A 1 106 ? -14.02500 -2.16300  16.90500  1.000 31.43096 ?  103 THR   A HG21 1 
ATOM   821  H HG22 . THR   A 1 106 ? -12.81600 -2.47800  17.87100  1.000 31.43096 ?  103 THR   A HG22 1 
ATOM   822  H HG23 . THR   A 1 106 ? -12.66000 -2.69500  16.31500  1.000 31.43096 ?  103 THR   A HG23 1 
ATOM   823  N N    . VAL   A 1 107 ? -10.61600 -4.85300  18.81400  1.000 11.07311 ?  104 VAL   A N    1 
ATOM   824  C CA   . VAL   A 1 107 ? -9.87000  -4.66100  20.05000  1.000 13.93918 ?  104 VAL   A CA   1 
ATOM   825  C C    . VAL   A 1 107 ? -8.82000  -3.58800  19.81600  1.000 11.17678 ?  104 VAL   A C    1 
ATOM   826  O O    . VAL   A 1 107 ? -8.49000  -3.24400  18.67800  1.000 11.21598 ?  104 VAL   A O    1 
ATOM   827  C CB   . VAL   A 1 107 ? -9.20400  -5.95900  20.55800  1.000 18.06869 ?  104 VAL   A CB   1 
ATOM   828  C CG1  . VAL   A 1 107 ? -10.25300 -7.01100  20.89300  1.000 17.84725 ?  104 VAL   A CG1  1 
ATOM   829  C CG2  . VAL   A 1 107 ? -8.18900  -6.49500  19.56200  1.000 17.69263 ?  104 VAL   A CG2  1 
ATOM   830  N N    . LYS   A 1 108 ? -8.26700  -3.08700  20.92300  1.000 10.37061 ?  105 LYS   A N    1 
ATOM   831  C CA   . LYS   A 1 108 ? -7.26600  -2.03300  20.91000  1.000 10.23266 ?  105 LYS   A CA   1 
ATOM   832  C C    . LYS   A 1 108 ? -5.89500  -2.51700  21.36000  1.000 6.59565  ?  105 LYS   A C    1 
ATOM   833  O O    . LYS   A 1 108 ? -4.97500  -1.70700  21.47200  1.000 8.45635  ?  105 LYS   A O    1 
ATOM   834  C CB   . LYS   A 1 108 ? -7.73000  -0.87300  21.80100  1.000 12.67942 ?  105 LYS   A CB   1 
ATOM   835  C CG   . LYS   A 1 108 ? -8.93900  -0.14600  21.21900  1.000 10.38720 ?  105 LYS   A CG   1 
ATOM   836  C CD   . LYS   A 1 108 ? -9.28300  1.11200   21.99400  1.000 13.41660 ?  105 LYS   A CD   1 
ATOM   837  C CE   . LYS   A 1 108 ? -10.10000 0.78100   23.21600  1.000 28.00179 ?  105 LYS   A CE   1 
ATOM   838  N NZ   . LYS   A 1 108 ? -10.33500 1.99300   24.06200  1.000 34.89526 ?  105 LYS   A NZ   1 
ATOM   839  N N    . LYS   A 1 109 ? -5.73100  -3.81700  21.59000  1.000 8.27754  ?  106 LYS   A N    1 
ATOM   840  C CA   . LYS   A 1 109 ? -4.53500  -4.36400  22.22500  1.000 11.06311 ?  106 LYS   A CA   1 
ATOM   841  C C    . LYS   A 1 109 ? -3.98300  -5.49400  21.37200  1.000 9.97814  ?  106 LYS   A C    1 
ATOM   842  O O    . LYS   A 1 109 ? -4.75200  -6.30600  20.83400  1.000 9.48035  ?  106 LYS   A O    1 
ATOM   843  C CB   . LYS   A 1 109 ? -4.87300  -4.89600  23.62900  1.000 12.57329 ?  106 LYS   A CB   1 
ATOM   844  C CG   . LYS   A 1 109 ? -3.69800  -5.22800  24.52800  1.000 15.54698 ?  106 LYS   A CG   1 
ATOM   845  C CD   . LYS   A 1 109 ? -4.23500  -5.58200  25.93100  1.000 20.47983 ?  106 LYS   A CD   1 
ATOM   846  C CE   . LYS   A 1 109 ? -3.21200  -6.31000  26.76400  1.000 26.38175 ?  106 LYS   A CE   1 
ATOM   847  N NZ   . LYS   A 1 109 ? -3.73000  -6.57900  28.14800  1.000 33.76039 ?  106 LYS   A NZ   1 
ATOM   848  N N    . ILE   A 1 110 ? -2.64900  -5.55400  21.25500  1.000 8.95389  ?  107 ILE   A N    1 
ATOM   849  C CA   . ILE   A 1 110 ? -1.97600  -6.63300  20.54000  1.000 8.22481  ?  107 ILE   A CA   1 
ATOM   850  C C    . ILE   A 1 110 ? -1.02300  -7.35300  21.47200  1.000 10.47555 ?  107 ILE   A C    1 
ATOM   851  O O    . ILE   A 1 110 ? -0.46800  -6.76500  22.40300  1.000 9.81264  ?  107 ILE   A O    1 
ATOM   852  C CB   . ILE   A 1 110 ? -1.18400  -6.13500  19.31400  1.000 11.41663 ?  107 ILE   A CB   1 
ATOM   853  C CG1  . ILE   A 1 110 ? -0.22300  -5.01800  19.73600  1.000 9.69168  ?  107 ILE   A CG1  1 
ATOM   854  C CG2  . ILE   A 1 110 ? -2.15300  -5.72400  18.19500  1.000 10.68739 ?  107 ILE   A CG2  1 
ATOM   855  C CD1  . ILE   A 1 110 ? 0.71500   -4.54500  18.59600  1.000 10.56552 ?  107 ILE   A CD1  1 
ATOM   856  N N    . PHE   A 1 111 ? -0.84400  -8.63800  21.19100  1.000 11.89053 ?  108 PHE   A N    1 
ATOM   857  C CA   . PHE   A 1 111 ? 0.26100   -9.44300  21.69600  1.000 12.13427 ?  108 PHE   A CA   1 
ATOM   858  C C    . PHE   A 1 111 ? 1.41400   -9.34500  20.70400  1.000 10.15181 ?  108 PHE   A C    1 
ATOM   859  O O    . PHE   A 1 111 ? 1.20500   -9.46700  19.49400  1.000 12.25907 ?  108 PHE   A O    1 
ATOM   860  C CB   . PHE   A 1 111 ? -0.21100  -10.89000 21.85400  1.000 13.99398 ?  108 PHE   A CB   1 
ATOM   861  C CG   . PHE   A 1 111 ? 0.89200   -11.90600 21.92100  1.000 14.34328 ?  108 PHE   A CG   1 
ATOM   862  C CD1  . PHE   A 1 111 ? 1.38700   -12.49000 20.76200  1.000 18.05374 ?  108 PHE   A CD1  1 
ATOM   863  C CD2  . PHE   A 1 111 ? 1.41200   -12.30400 23.14400  1.000 18.67390 ?  108 PHE   A CD2  1 
ATOM   864  C CE1  . PHE   A 1 111 ? 2.39900   -13.44100 20.82000  1.000 20.52023 ?  108 PHE   A CE1  1 
ATOM   865  C CE2  . PHE   A 1 111 ? 2.41600   -13.25200 23.21200  1.000 16.33466 ?  108 PHE   A CE2  1 
ATOM   866  C CZ   . PHE   A 1 111 ? 2.91600   -13.82000 22.05100  1.000 18.17989 ?  108 PHE   A CZ   1 
ATOM   867  N N    . VAL   A 1 112 ? 2.61300   -9.09700  21.21400  1.000 7.54818  ?  109 VAL   A N    1 
ATOM   868  C CA   . VAL   A 1 112 ? 3.84900   -9.05900  20.42300  1.000 7.55878  ?  109 VAL   A CA   1 
ATOM   869  C C    . VAL   A 1 112 ? 4.76700   -10.14200 20.96100  1.000 9.53197  ?  109 VAL   A C    1 
ATOM   870  O O    . VAL   A 1 112 ? 5.21700   -10.06500 22.11000  1.000 14.32197 ?  109 VAL   A O    1 
ATOM   871  C CB   . VAL   A 1 112 ? 4.52200   -7.68500  20.47300  1.000 6.43126  ?  109 VAL   A CB   1 
ATOM   872  C CG1  . VAL   A 1 112 ? 5.69400   -7.63400  19.48800  1.000 11.38021 ?  109 VAL   A CG1  1 
ATOM   873  C CG2  . VAL   A 1 112 ? 3.50500   -6.58800  20.12400  1.000 10.30672 ?  109 VAL   A CG2  1 
ATOM   874  N N    . GLY   A 1 113 ? 5.04000   -11.15800 20.14000  1.000 11.55858 ?  110 GLY   A N    1 
ATOM   875  C CA   . GLY   A 1 113 ? 5.87600   -12.25000 20.60400  1.000 12.02870 ?  110 GLY   A CA   1 
ATOM   876  C C    . GLY   A 1 113 ? 7.16200   -12.33900 19.81600  1.000 20.59578 ?  110 GLY   A C    1 
ATOM   877  O O    . GLY   A 1 113 ? 7.25800   -11.79500 18.70800  1.000 17.23405 ?  110 GLY   A O    1 
ATOM   878  N N    . GLY   A 1 114 ? 8.14900   -13.02400 20.38200  1.000 15.34828 ?  111 GLY   A N    1 
ATOM   879  C CA   . GLY   A 1 114 ? 9.41500   -13.21900 19.71200  1.000 14.67316 ?  111 GLY   A CA   1 
ATOM   880  C C    . GLY   A 1 114 ? 10.38700  -12.08100 19.87800  1.000 18.11372 ?  111 GLY   A C    1 
ATOM   881  O O    . GLY   A 1 114 ? 11.33300  -11.96800 19.09400  1.000 19.38405 ?  111 GLY   A O    1 
ATOM   882  N N    . ILE   A 1 115 ? 10.17900  -11.21900 20.87800  1.000 16.30202 ?  112 ILE   A N    1 
ATOM   883  C CA   . ILE   A 1 115 ? 11.05400  -10.07500 21.08700  1.000 15.14025 ?  112 ILE   A CA   1 
ATOM   884  C C    . ILE   A 1 115 ? 12.25000  -10.43900 21.94200  1.000 19.68132 ?  112 ILE   A C    1 
ATOM   885  O O    . ILE   A 1 115 ? 13.15800  -9.61200  22.09600  1.000 22.11812 ?  112 ILE   A O    1 
ATOM   886  C CB   . ILE   A 1 115 ? 10.29600  -8.88300  21.70600  1.000 22.29598 ?  112 ILE   A CB   1 
ATOM   887  C CG1  . ILE   A 1 115 ? 9.81200   -9.19600  23.12700  1.000 15.11394 ?  112 ILE   A CG1  1 
ATOM   888  C CG2  . ILE   A 1 115 ? 9.12500   -8.49200  20.81800  1.000 19.32440 ?  112 ILE   A CG2  1 
ATOM   889  C CD1  . ILE   A 1 115 ? 9.02900   -8.05500  23.77100  1.000 22.01200 ?  112 ILE   A CD1  1 
ATOM   890  N N    . LYS   A 1 116 ? 12.27200  -11.64600 22.50100  1.000 18.11731 ?  113 LYS   A N    1 
ATOM   891  C CA   . LYS   A 1 116 ? 13.39500  -12.15200 23.27900  1.000 29.05433 ?  113 LYS   A CA   1 
ATOM   892  C C    . LYS   A 1 116 ? 13.70100  -11.21800 24.43900  1.000 30.72227 ?  113 LYS   A C    1 
ATOM   893  O O    . LYS   A 1 116 ? 12.82100  -10.47600 24.89000  1.000 29.62209 ?  113 LYS   A O    1 
ATOM   894  C CB   . LYS   A 1 116 ? 14.59500  -12.37400 22.35800  1.000 31.62018 ?  113 LYS   A CB   1 
ATOM   895  C CG   . LYS   A 1 116 ? 14.32200  -13.53600 21.40000  1.000 33.86948 ?  113 LYS   A CG   1 
ATOM   896  C CD   . LYS   A 1 116 ? 15.58500  -14.12200 20.80700  1.000 43.21898 ?  113 LYS   A CD   1 
ATOM   897  C CE   . LYS   A 1 116 ? 15.34400  -14.51900 19.36400  1.000 47.42771 ?  113 LYS   A CE   1 
ATOM   898  N NZ   . LYS   A 1 116 ? 13.88400  -14.46200 19.03600  1.000 52.38050 ?  113 LYS   A NZ   1 
ATOM   899  N N    . GLU   A 1 117 ? 14.92700  -11.24800 24.95200  1.000 30.35328 ?  114 GLU   A N    1 
ATOM   900  C CA   . GLU   A 1 117 ? 15.19800  -10.61300 26.23000  1.000 29.67430 ?  114 GLU   A CA   1 
ATOM   901  C C    . GLU   A 1 117 ? 15.96300  -9.30000  26.09200  1.000 38.70390 ?  114 GLU   A C    1 
ATOM   902  O O    . GLU   A 1 117 ? 16.31000  -8.69200  27.10800  1.000 39.00747 ?  114 GLU   A O    1 
ATOM   903  C CB   . GLU   A 1 117 ? 15.92600  -11.60900 27.14200  1.000 34.46592 ?  114 GLU   A CB   1 
ATOM   904  C CG   . GLU   A 1 117 ? 16.19100  -11.13000 28.55700  1.000 40.85575 ?  114 GLU   A CG   1 
ATOM   905  C CD   . GLU   A 1 117 ? 16.83500  -12.21000 29.42900  1.000 55.41647 ?  114 GLU   A CD   1 
ATOM   906  O OE1  . GLU   A 1 117 ? 17.11800  -13.31200 28.91200  1.000 58.92935 ?  114 GLU   A OE1  1 
ATOM   907  O OE2  . GLU   A 1 117 ? 17.03800  -11.96400 30.64000  1.000 54.27333 ?  114 GLU   A OE2  1 
ATOM   908  N N    . ASP   A 1 118 ? 16.19500  -8.81900  24.86600  1.000 24.41168 ?  115 ASP   A N    1 
ATOM   909  C CA   . ASP   A 1 118 ? 16.90300  -7.56000  24.65700  1.000 22.80657 ?  115 ASP   A CA   1 
ATOM   910  C C    . ASP   A 1 118 ? 16.02000  -6.44400  24.10400  1.000 34.02315 ?  115 ASP   A C    1 
ATOM   911  O O    . ASP   A 1 118 ? 16.52300  -5.34700  23.83200  1.000 31.44164 ?  115 ASP   A O    1 
ATOM   912  C CB   . ASP   A 1 118 ? 18.09100  -7.76500  23.70700  1.000 23.27022 ?  115 ASP   A CB   1 
ATOM   913  C CG   . ASP   A 1 118 ? 17.66000  -8.19800  22.30900  1.000 42.28601 ?  115 ASP   A CG   1 
ATOM   914  O OD1  . ASP   A 1 118 ? 16.56700  -8.79900  22.17200  1.000 34.24203 ?  115 ASP   A OD1  1 
ATOM   915  O OD2  . ASP   A 1 118 ? 18.41200  -7.91200  21.34500  1.000 35.96592 -1 115 ASP   A OD2  1 
ATOM   916  N N    . THR   A 1 119 ? 14.73000  -6.68700  23.90700  1.000 28.20894 ?  116 THR   A N    1 
ATOM   917  C CA   . THR   A 1 119 ? 13.84900  -5.66700  23.36000  1.000 26.44447 ?  116 THR   A CA   1 
ATOM   918  C C    . THR   A 1 119 ? 13.28200  -4.83800  24.50400  1.000 20.94199 ?  116 THR   A C    1 
ATOM   919  O O    . THR   A 1 119 ? 12.79300  -5.39500  25.49500  1.000 26.35751 ?  116 THR   A O    1 
ATOM   920  C CB   . THR   A 1 119 ? 12.72400  -6.30600  22.54400  1.000 24.52800 ?  116 THR   A CB   1 
ATOM   921  O OG1  . THR   A 1 119 ? 13.30100  -7.06800  21.47500  1.000 22.20697 ?  116 THR   A OG1  1 
ATOM   922  C CG2  . THR   A 1 119 ? 11.82100  -5.22000  21.94000  1.000 19.70680 ?  116 THR   A CG2  1 
ATOM   923  N N    . GLU   A 1 120 ? 13.33700  -3.51500  24.35700  1.000 23.69226 ?  117 GLU   A N    1 
ATOM   924  C CA   . GLU   A 1 120 ? 12.92300  -2.58200  25.39600  1.000 27.99582 ?  117 GLU   A CA   1 
ATOM   925  C C    . GLU   A 1 120 ? 11.70100  -1.78700  24.94100  1.000 28.18700 ?  117 GLU   A C    1 
ATOM   926  O O    . GLU   A 1 120 ? 11.23300  -1.89100  23.80100  1.000 25.29385 ?  117 GLU   A O    1 
ATOM   927  C CB   . GLU   A 1 120 ? 14.07600  -1.64400  25.76700  1.000 31.69996 ?  117 GLU   A CB   1 
ATOM   928  C CG   . GLU   A 1 120 ? 15.27800  -2.34700  26.38200  1.000 31.52453 ?  117 GLU   A CG   1 
ATOM   929  C CD   . GLU   A 1 120 ? 14.91600  -3.18900  27.59700  1.000 43.21231 ?  117 GLU   A CD   1 
ATOM   930  O OE1  . GLU   A 1 120 ? 13.92700  -2.86100  28.29000  1.000 48.31583 ?  117 GLU   A OE1  1 
ATOM   931  O OE2  . GLU   A 1 120 ? 15.63300  -4.17600  27.86900  1.000 50.14930 -1 117 GLU   A OE2  1 
ATOM   932  N N    . GLU   A 1 121 ? 11.19500  -0.96400  25.86000  1.000 28.04806 ?  118 GLU   A N    1 
ATOM   933  C CA   . GLU   A 1 121 ? 9.97000   -0.21900  25.59800  1.000 26.48445 ?  118 GLU   A CA   1 
ATOM   934  C C    . GLU   A 1 121 ? 10.11200  0.69600   24.38800  1.000 28.49907 ?  118 GLU   A C    1 
ATOM   935  O O    . GLU   A 1 121 ? 9.20400   0.77600   23.55200  1.000 20.90368 ?  118 GLU   A O    1 
ATOM   936  C CB   . GLU   A 1 121 ? 9.58900   0.59300   26.82800  1.000 27.99779 ?  118 GLU   A CB   1 
ATOM   937  C CG   . GLU   A 1 121 ? 8.22100   1.19600   26.74800  1.000 38.23045 ?  118 GLU   A CG   1 
ATOM   938  C CD   . GLU   A 1 121 ? 7.86500   1.97700   27.99800  1.000 48.17170 ?  118 GLU   A CD   1 
ATOM   939  O OE1  . GLU   A 1 121 ? 7.82800   1.36900   29.08900  1.000 42.06606 ?  118 GLU   A OE1  1 
ATOM   940  O OE2  . GLU   A 1 121 ? 7.61200   3.19700   27.87700  1.000 54.79890 -1 118 GLU   A OE2  1 
ATOM   941  N N    . HIS   A 1 122 ? 11.23900  1.40800   24.28000  1.000 18.32822 ?  119 HIS   A N    1 
ATOM   942  C CA   . HIS   A 1 122 ? 11.38800  2.37000   23.19600  1.000 21.11685 ?  119 HIS   A CA   1 
ATOM   943  C C    . HIS   A 1 122 ? 11.45300  1.69000   21.83200  1.000 16.87134 ?  119 HIS   A C    1 
ATOM   944  O O    . HIS   A 1 122 ? 11.04600  2.29000   20.83400  1.000 17.51763 ?  119 HIS   A O    1 
ATOM   945  C CB   . HIS   A 1 122 ? 12.62500  3.24000   23.43400  1.000 23.95462 ?  119 HIS   A CB   1 
ATOM   946  C CG   . HIS   A 1 122 ? 13.92000  2.49600   23.33600  1.000 27.20301 ?  119 HIS   A CG   1 
ATOM   947  N ND1  . HIS   A 1 122 ? 14.74000  2.57400   22.23100  1.000 32.37621 ?  119 HIS   A ND1  1 
ATOM   948  C CD2  . HIS   A 1 122 ? 14.53100  1.65000   24.19900  1.000 29.60742 ?  119 HIS   A CD2  1 
ATOM   949  C CE1  . HIS   A 1 122 ? 15.80400  1.81500   22.42000  1.000 28.26721 ?  119 HIS   A CE1  1 
ATOM   950  N NE2  . HIS   A 1 122 ? 15.70200  1.24200   23.60700  1.000 28.27896 ?  119 HIS   A NE2  1 
ATOM   951  N N    . HIS   A 1 123 ? 11.94400  0.44900   21.76500  1.000 15.04247 ?  120 HIS   A N    1 
ATOM   952  C CA   . HIS   A 1 123 ? 11.91200  -0.29100  20.50200  1.000 19.18139 ?  120 HIS   A CA   1 
ATOM   953  C C    . HIS   A 1 123 ? 10.47800  -0.47600  20.03600  1.000 16.57559 ?  120 HIS   A C    1 
ATOM   954  O O    . HIS   A 1 123 ? 10.14100  -0.22000  18.87000  1.000 15.19956 ?  120 HIS   A O    1 
ATOM   955  C CB   . HIS   A 1 123 ? 12.55800  -1.67000  20.65800  1.000 19.06961 ?  120 HIS   A CB   1 
ATOM   956  C CG   . HIS   A 1 123 ? 14.02400  -1.64000  20.95700  1.000 20.25817 ?  120 HIS   A CG   1 
ATOM   957  N ND1  . HIS   A 1 123 ? 14.56600  -2.23600  22.07600  1.000 29.83291 ?  120 HIS   A ND1  1 
ATOM   958  C CD2  . HIS   A 1 123 ? 15.06100  -1.10700  20.27200  1.000 20.33678 ?  120 HIS   A CD2  1 
ATOM   959  C CE1  . HIS   A 1 123 ? 15.87700  -2.06200  22.07100  1.000 32.43835 ?  120 HIS   A CE1  1 
ATOM   960  N NE2  . HIS   A 1 123 ? 16.20200  -1.37500  20.99100  1.000 21.04049 ?  120 HIS   A NE2  1 
ATOM   961  N N    . LEU   A 1 124 ? 9.63200   -0.96900  20.94000  1.000 21.55543 ?  121 LEU   A N    1 
ATOM   962  C CA   . LEU   A 1 124 ? 8.23300   -1.19700  20.61100  1.000 12.77977 ?  121 LEU   A CA   1 
ATOM   963  C C    . LEU   A 1 124 ? 7.53300   0.10700   20.30400  1.000 11.58965 ?  121 LEU   A C    1 
ATOM   964  O O    . LEU   A 1 124 ? 6.73800   0.17600   19.35800  1.000 11.35898 ?  121 LEU   A O    1 
ATOM   965  C CB   . LEU   A 1 124 ? 7.53700   -1.91600  21.75800  1.000 13.45327 ?  121 LEU   A CB   1 
ATOM   966  C CG   . LEU   A 1 124 ? 8.06600   -3.32000  22.01900  1.000 19.46789 ?  121 LEU   A CG   1 
ATOM   967  C CD1  . LEU   A 1 124 ? 7.56800   -3.84000  23.34100  1.000 20.49688 ?  121 LEU   A CD1  1 
ATOM   968  C CD2  . LEU   A 1 124 ? 7.59500   -4.19900  20.89800  1.000 19.54829 ?  121 LEU   A CD2  1 
ATOM   969  N N    . ARG   A 1 125 ? 7.79600   1.15000   21.10800  1.000 10.03340 ?  122 ARG   A N    1 
ATOM   970  C CA   . ARG   A 1 125 ? 7.12500   2.42700   20.89600  1.000 15.58355 ?  122 ARG   A CA   1 
ATOM   971  C C    . ARG   A 1 125 ? 7.51900   3.05700   19.56200  1.000 11.79764 ?  122 ARG   A C    1 
ATOM   972  O O    . ARG   A 1 125 ? 6.66100   3.52200   18.80400  1.000 11.49549 ?  122 ARG   A O    1 
ATOM   973  C CB   . ARG   A 1 125 ? 7.41900   3.36900   22.06400  1.000 14.29270 ?  122 ARG   A CB   1 
ATOM   974  C CG   . ARG   A 1 125 ? 6.80300   4.73600   21.91100  1.000 13.31320 ?  122 ARG   A CG   1 
ATOM   975  C CD   . ARG   A 1 125 ? 7.03500   5.58800   23.15500  1.000 24.09868 ?  122 ARG   A CD   1 
ATOM   976  N NE   . ARG   A 1 125 ? 6.52400   4.93200   24.36000  1.000 35.18468 ?  122 ARG   A NE   1 
ATOM   977  C CZ   . ARG   A 1 125 ? 5.29400   5.07400   24.84800  1.000 40.16024 ?  122 ARG   A CZ   1 
ATOM   978  N NH1  . ARG   A 1 125 ? 4.38600   5.82600   24.24300  1.000 34.05232 ?  122 ARG   A NH1  1 
ATOM   979  N NH2  . ARG   A 1 125 ? 4.96600   4.44300   25.97300  1.000 36.30135 ?  122 ARG   A NH2  1 
ATOM   980  N N    . ASP   A 1 126 ? 8.82100   3.12000   19.26700  1.000 13.04242 ?  123 ASP   A N    1 
ATOM   981  C CA   . ASP   A 1 126 ? 9.23600   3.76900   18.03000  1.000 14.23455 ?  123 ASP   A CA   1 
ATOM   982  C C    . ASP   A 1 126 ? 8.64400   3.08800   16.80900  1.000 16.25421 ?  123 ASP   A C    1 
ATOM   983  O O    . ASP   A 1 126 ? 8.34200   3.75700   15.81700  1.000 16.75344 ?  123 ASP   A O    1 
ATOM   984  C CB   . ASP   A 1 126 ? 10.75600  3.79600   17.92000  1.000 17.10436 ?  123 ASP   A CB   1 
ATOM   985  C CG   . ASP   A 1 126 ? 11.40400  4.76600   18.89800  1.000 21.87220 ?  123 ASP   A CG   1 
ATOM   986  O OD1  . ASP   A 1 126 ? 10.69000  5.50900   19.60700  1.000 22.43431 ?  123 ASP   A OD1  1 
ATOM   987  O OD2  . ASP   A 1 126 ? 12.64400  4.76000   18.96600  1.000 28.68819 -1 123 ASP   A OD2  1 
ATOM   988  N N    . TYR   A 1 127 ? 8.47300   1.76700   16.86400  1.000 13.85251 ?  124 TYR   A N    1 
ATOM   989  C CA   . TYR   A 1 127 ? 7.88800   1.04200   15.74000  1.000 12.91786 ?  124 TYR   A CA   1 
ATOM   990  C C    . TYR   A 1 127 ? 6.37300   1.19400   15.70700  1.000 12.13567 ?  124 TYR   A C    1 
ATOM   991  O O    . TYR   A 1 127 ? 5.79600   1.62600   14.70000  1.000 13.37869 ?  124 TYR   A O    1 
ATOM   992  C CB   . TYR   A 1 127 ? 8.26900   -0.43000  15.82100  1.000 14.61417 ?  124 TYR   A CB   1 
ATOM   993  C CG   . TYR   A 1 127 ? 7.63600   -1.25100  14.71800  1.000 16.04120 ?  124 TYR   A CG   1 
ATOM   994  C CD1  . TYR   A 1 127 ? 8.10400   -1.15800  13.40900  1.000 15.17738 ?  124 TYR   A CD1  1 
ATOM   995  C CD2  . TYR   A 1 127 ? 6.57500   -2.11400  14.98100  1.000 9.98220  ?  124 TYR   A CD2  1 
ATOM   996  C CE1  . TYR   A 1 127 ? 7.53600   -1.89800  12.38400  1.000 16.68909 ?  124 TYR   A CE1  1 
ATOM   997  C CE2  . TYR   A 1 127 ? 6.00300   -2.87300  13.95900  1.000 11.66846 ?  124 TYR   A CE2  1 
ATOM   998  C CZ   . TYR   A 1 127 ? 6.49300   -2.75500  12.66000  1.000 17.05360 ?  124 TYR   A CZ   1 
ATOM   999  O OH   . TYR   A 1 127 ? 5.93600   -3.49300  11.63300  1.000 13.24941 ?  124 TYR   A OH   1 
ATOM   1000 N N    . PHE   A 1 128 ? 5.70900   0.88100   16.81200  1.000 11.10803 ?  125 PHE   A N    1 
ATOM   1001 C CA   . PHE   A 1 128 ? 4.25100   0.82300   16.76800  1.000 8.31070  ?  125 PHE   A CA   1 
ATOM   1002 C C    . PHE   A 1 128 ? 3.56400   2.18500   16.78100  1.000 9.62562  ?  125 PHE   A C    1 
ATOM   1003 O O    . PHE   A 1 128 ? 2.38200   2.26300   16.41700  1.000 10.87000 ?  125 PHE   A O    1 
ATOM   1004 C CB   . PHE   A 1 128 ? 3.75400   -0.04500  17.92200  1.000 9.33319  ?  125 PHE   A CB   1 
ATOM   1005 C CG   . PHE   A 1 128 ? 3.91900   -1.51500  17.66000  1.000 7.66396  ?  125 PHE   A CG   1 
ATOM   1006 C CD1  . PHE   A 1 128 ? 3.21300   -2.11600  16.62000  1.000 8.07154  ?  125 PHE   A CD1  1 
ATOM   1007 C CD2  . PHE   A 1 128 ? 4.79400   -2.28600  18.40700  1.000 9.26287  ?  125 PHE   A CD2  1 
ATOM   1008 C CE1  . PHE   A 1 128 ? 3.36800   -3.47600  16.34600  1.000 11.83240 ?  125 PHE   A CE1  1 
ATOM   1009 C CE2  . PHE   A 1 128 ? 4.95700   -3.65200  18.13300  1.000 8.28851  ?  125 PHE   A CE2  1 
ATOM   1010 C CZ   . PHE   A 1 128 ? 4.23200   -4.24100  17.09300  1.000 10.17175 ?  125 PHE   A CZ   1 
ATOM   1011 N N    . GLU   A 1 129 ? 4.25500   3.25500   17.17500  1.000 10.65385 ?  126 GLU   A N    1 
ATOM   1012 C CA   . GLU   A 1 129 ? 3.60000   4.55800   17.22200  1.000 7.86919  ?  126 GLU   A CA   1 
ATOM   1013 C C    . GLU   A 1 129 ? 3.17700   5.02900   15.84100  1.000 9.00791  ?  126 GLU   A C    1 
ATOM   1014 O O    . GLU   A 1 129 ? 2.33100   5.92700   15.72300  1.000 9.37346  ?  126 GLU   A O    1 
ATOM   1015 C CB   . GLU   A 1 129 ? 4.51500   5.60800   17.86700  1.000 10.74508 ?  126 GLU   A CB   1 
ATOM   1016 C CG   . GLU   A 1 129 ? 5.71200   6.01200   17.01000  1.000 11.04855 ?  126 GLU   A CG   1 
ATOM   1017 C CD   . GLU   A 1 129 ? 6.71800   6.84100   17.77800  1.000 25.43597 ?  126 GLU   A CD   1 
ATOM   1018 O OE1  . GLU   A 1 129 ? 6.45700   7.12900   18.97000  1.000 23.54501 ?  126 GLU   A OE1  1 
ATOM   1019 O OE2  . GLU   A 1 129 ? 7.75500   7.21700   17.18100  1.000 25.03893 -1 126 GLU   A OE2  1 
ATOM   1020 N N    . GLN   A 1 130 ? 3.75500   4.45200   14.79500  1.000 9.81597  ?  127 GLN   A N    1 
ATOM   1021 C CA   . GLN   A 1 130 ? 3.39200   4.82000   13.43700  1.000 7.12343  ?  127 GLN   A CA   1 
ATOM   1022 C C    . GLN   A 1 130 ? 2.13500   4.12100   12.97100  1.000 8.39201  ?  127 GLN   A C    1 
ATOM   1023 O O    . GLN   A 1 130 ? 1.65800   4.42300   11.87000  1.000 9.21360  ?  127 GLN   A O    1 
ATOM   1024 C CB   . GLN   A 1 130 ? 4.53700   4.48900   12.48400  1.000 9.98901  ?  127 GLN   A CB   1 
ATOM   1025 C CG   . GLN   A 1 130 ? 5.84900   5.11400   12.91300  1.000 12.72524 ?  127 GLN   A CG   1 
ATOM   1026 C CD   . GLN   A 1 130 ? 6.84500   5.22300   11.76100  1.000 10.75278 ?  127 GLN   A CD   1 
ATOM   1027 O OE1  . GLN   A 1 130 ? 7.91600   4.60600   11.81400  1.000 18.17031 ?  127 GLN   A OE1  1 
ATOM   1028 N NE2  . GLN   A 1 130 ? 6.52900   6.02400   10.76300  1.000 12.48054 ?  127 GLN   A NE2  1 
ATOM   1029 N N    . TYR   A 1 131 ? 1.58900   3.20100   13.77500  1.000 8.79045  ?  128 TYR   A N    1 
ATOM   1030 C CA   . TYR   A 1 131 ? 0.29100   2.60700   13.49800  1.000 7.91720  ?  128 TYR   A CA   1 
ATOM   1031 C C    . TYR   A 1 131 ? -0.84600  3.29700   14.24100  1.000 10.47173 ?  128 TYR   A C    1 
ATOM   1032 O O    . TYR   A 1 131 ? -1.99600  3.22300   13.80000  1.000 8.62696  ?  128 TYR   A O    1 
ATOM   1033 C CB   . TYR   A 1 131 ? 0.30400   1.12600   13.88800  1.000 8.46085  ?  128 TYR   A CB   1 
ATOM   1034 C CG   . TYR   A 1 131 ? 0.96000   0.22700   12.86500  1.000 8.11433  ?  128 TYR   A CG   1 
ATOM   1035 C CD1  . TYR   A 1 131 ? 0.28000   -0.16700  11.72300  1.000 9.04899  ?  128 TYR   A CD1  1 
ATOM   1036 C CD2  . TYR   A 1 131 ? 2.27200   -0.21900  13.05200  1.000 8.72308  ?  128 TYR   A CD2  1 
ATOM   1037 C CE1  . TYR   A 1 131 ? 0.88900   -0.99600  10.79200  1.000 7.37817  ?  128 TYR   A CE1  1 
ATOM   1038 C CE2  . TYR   A 1 131 ? 2.88400   -1.04700  12.13000  1.000 9.96564  ?  128 TYR   A CE2  1 
ATOM   1039 C CZ   . TYR   A 1 131 ? 2.17700   -1.43200  11.01000  1.000 9.12487  ?  128 TYR   A CZ   1 
ATOM   1040 O OH   . TYR   A 1 131 ? 2.74100   -2.25100  10.05000  1.000 13.12361 ?  128 TYR   A OH   1 
ATOM   1041 N N    . GLY   A 1 132 ? -0.55600  3.95000   15.35700  1.000 9.44222  ?  129 GLY   A N    1 
ATOM   1042 C CA   . GLY   A 1 132 ? -1.60800  4.57800   16.13200  1.000 10.55490 ?  129 GLY   A CA   1 
ATOM   1043 C C    . GLY   A 1 132 ? -1.03800  5.10400   17.42300  1.000 11.12987 ?  129 GLY   A C    1 
ATOM   1044 O O    . GLY   A 1 132 ? 0.12900   4.89200   17.74600  1.000 9.59179  ?  129 GLY   A O    1 
ATOM   1045 N N    . LYS   A 1 133 ? -1.89900  5.77200   18.17100  1.000 12.07999 ?  130 LYS   A N    1 
ATOM   1046 C CA   . LYS   A 1 133 ? -1.49500  6.38900   19.42600  1.000 9.62351  ?  130 LYS   A CA   1 
ATOM   1047 C C    . LYS   A 1 133 ? -1.43900  5.33100   20.52200  1.000 10.53040 ?  130 LYS   A C    1 
ATOM   1048 O O    . LYS   A 1 133 ? -2.44600  4.68700   20.82200  1.000 11.50183 ?  130 LYS   A O    1 
ATOM   1049 C CB   . LYS   A 1 133 ? -2.46400  7.50600   19.80500  1.000 11.85254 ?  130 LYS   A CB   1 
ATOM   1050 C CG   . LYS   A 1 133 ? -2.13700  8.07700   21.16600  1.000 17.20081 ?  130 LYS   A CG   1 
ATOM   1051 C CD   . LYS   A 1 133 ? -2.65300  9.49700   21.34400  1.000 30.49729 ?  130 LYS   A CD   1 
ATOM   1052 C CE   . LYS   A 1 133 ? -1.91800  10.16100  22.49600  1.000 31.23733 ?  130 LYS   A CE   1 
ATOM   1053 N NZ   . LYS   A 1 133 ? -1.27900  9.12600   23.36200  1.000 39.96801 ?  130 LYS   A NZ   1 
ATOM   1054 N N    . ILE   A 1 134 ? -0.27200  5.17400   21.13200  1.000 10.06372 ?  131 ILE   A N    1 
ATOM   1055 C CA   . ILE   A 1 134 ? -0.04700  4.16000   22.15600  1.000 9.71072  ?  131 ILE   A CA   1 
ATOM   1056 C C    . ILE   A 1 134 ? -0.44700  4.69900   23.51900  1.000 11.96582 ?  131 ILE   A C    1 
ATOM   1057 O O    . ILE   A 1 134 ? -0.06500  5.81200   23.90100  1.000 13.90329 ?  131 ILE   A O    1 
ATOM   1058 C CB   . ILE   A 1 134 ? 1.41900   3.69300   22.15300  1.000 10.75586 ?  131 ILE   A CB   1 
ATOM   1059 C CG1  . ILE   A 1 134 ? 1.76100   3.03000   20.80800  1.000 8.70092  ?  131 ILE   A CG1  1 
ATOM   1060 C CG2  . ILE   A 1 134 ? 1.67100   2.74200   23.29700  1.000 11.43477 ?  131 ILE   A CG2  1 
ATOM   1061 C CD1  . ILE   A 1 134 ? 3.28700   2.72100   20.61700  1.000 9.29709  ?  131 ILE   A CD1  1 
ATOM   1062 N N    . GLU   A 1 135 ? -1.21800  3.90300   24.25900  1.000 9.10694  ?  132 GLU   A N    1 
ATOM   1063 C CA   . GLU   A 1 135 ? -1.52800  4.24400   25.64200  1.000 10.45344 ?  132 GLU   A CA   1 
ATOM   1064 C C    . GLU   A 1 135 ? -0.79800  3.38700   26.66300  1.000 12.27128 ?  132 GLU   A C    1 
ATOM   1065 O O    . GLU   A 1 135 ? -0.46500  3.89900   27.73200  1.000 16.61501 ?  132 GLU   A O    1 
ATOM   1066 C CB   . GLU   A 1 135 ? -3.04200  4.14700   25.87600  1.000 13.17561 ?  132 GLU   A CB   1 
ATOM   1067 C CG   . GLU   A 1 135 ? -3.81800  5.00500   24.90200  1.000 13.80841 ?  132 GLU   A CG   1 
ATOM   1068 C CD   . GLU   A 1 135 ? -5.25500  5.27600   25.34500  1.000 15.90918 ?  132 GLU   A CD   1 
ATOM   1069 O OE1  . GLU   A 1 135 ? -5.93300  4.31400   25.73400  1.000 23.34891 ?  132 GLU   A OE1  1 
ATOM   1070 O OE2  . GLU   A 1 135 ? -5.71000  6.43300   25.24200  1.000 25.48067 -1 132 GLU   A OE2  1 
ATOM   1071 N N    . VAL   A 1 136 ? -0.52900  2.11400   26.37600  1.000 10.77986 ?  133 VAL   A N    1 
ATOM   1072 C CA   . VAL   A 1 136 ? 0.14100   1.22400   27.32900  1.000 11.04474 ?  133 VAL   A CA   1 
ATOM   1073 C C    . VAL   A 1 136 ? 1.12800   0.34400   26.59100  1.000 13.88022 ?  133 VAL   A C    1 
ATOM   1074 O O    . VAL   A 1 136 ? 0.78700   -0.25500  25.56900  1.000 11.81714 ?  133 VAL   A O    1 
ATOM   1075 C CB   . VAL   A 1 136 ? -0.84200  0.32500   28.10300  1.000 14.67555 ?  133 VAL   A CB   1 
ATOM   1076 C CG1  . VAL   A 1 136 ? -0.07900  -0.54100  29.13200  1.000 16.88175 ?  133 VAL   A CG1  1 
ATOM   1077 C CG2  . VAL   A 1 136 ? -1.88700  1.16800   28.78900  1.000 17.79050 ?  133 VAL   A CG2  1 
ATOM   1078 N N    . ILE   A 1 137 ? 2.33500   0.20500   27.13500  1.000 10.85943 ?  134 ILE   A N    1 
ATOM   1079 C CA   . ILE   A 1 137 ? 3.25600   -0.82800  26.68000  1.000 11.10229 ?  134 ILE   A CA   1 
ATOM   1080 C C    . ILE   A 1 137 ? 3.61100   -1.67600  27.88900  1.000 12.42006 ?  134 ILE   A C    1 
ATOM   1081 O O    . ILE   A 1 137 ? 3.99300   -1.13800  28.93100  1.000 17.54926 ?  134 ILE   A O    1 
ATOM   1082 C CB   . ILE   A 1 137 ? 4.52000   -0.23700  26.04300  1.000 12.74098 ?  134 ILE   A CB   1 
ATOM   1083 C CG1  . ILE   A 1 137 ? 4.14800   0.56200   24.79400  1.000 12.44873 ?  134 ILE   A CG1  1 
ATOM   1084 C CG2  . ILE   A 1 137 ? 5.47200   -1.37800  25.66800  1.000 12.74380 ?  134 ILE   A CG2  1 
ATOM   1085 C CD1  . ILE   A 1 137 ? 5.32800   1.24700   24.12500  1.000 13.90443 ?  134 ILE   A CD1  1 
ATOM   1086 N N    . GLU   A 1 138 ? 3.45100   -2.98300  27.76300  1.000 9.09468  ?  135 GLU   A N    1 
ATOM   1087 C CA   . GLU   A 1 138 ? 3.69400   -3.89200  28.87900  1.000 14.99932 ?  135 GLU   A CA   1 
ATOM   1088 C C    . GLU   A 1 138 ? 4.63700   -4.99600  28.40300  1.000 13.95038 ?  135 GLU   A C    1 
ATOM   1089 O O    . GLU   A 1 138 ? 4.22400   -5.93800  27.72300  1.000 13.79701 ?  135 GLU   A O    1 
ATOM   1090 C CB   . GLU   A 1 138 ? 2.38100   -4.44300  29.41700  1.000 17.38475 ?  135 GLU   A CB   1 
ATOM   1091 C CG   . GLU   A 1 138 ? 2.53100   -5.17500  30.74700  1.000 24.79117 ?  135 GLU   A CG   1 
ATOM   1092 C CD   . GLU   A 1 138 ? 1.31800   -6.02600  31.09000  1.000 28.52274 ?  135 GLU   A CD   1 
ATOM   1093 O OE1  . GLU   A 1 138 ? 0.32000   -5.99200  30.33500  1.000 34.89702 ?  135 GLU   A OE1  1 
ATOM   1094 O OE2  . GLU   A 1 138 ? 1.36800   -6.72900  32.12400  1.000 33.60953 -1 135 GLU   A OE2  1 
ATOM   1095 N N    . ILE   A 1 139 ? 5.90800   -4.88000  28.77200  1.000 14.88764 ?  136 ILE   A N    1 
ATOM   1096 C CA   . ILE   A 1 139 ? 6.91300   -5.88900  28.46400  1.000 13.42164 ?  136 ILE   A CA   1 
ATOM   1097 C C    . ILE   A 1 139 ? 6.84900   -6.93700  29.56600  1.000 16.85564 ?  136 ILE   A C    1 
ATOM   1098 O O    . ILE   A 1 139 ? 6.97600   -6.60700  30.75000  1.000 20.00068 ?  136 ILE   A O    1 
ATOM   1099 C CB   . ILE   A 1 139 ? 8.31000   -5.25400  28.36700  1.000 19.83315 ?  136 ILE   A CB   1 
ATOM   1100 C CG1  . ILE   A 1 139 ? 8.38300   -4.32200  27.14700  1.000 21.63185 ?  136 ILE   A CG1  1 
ATOM   1101 C CG2  . ILE   A 1 139 ? 9.39300   -6.30600  28.31100  1.000 16.16056 ?  136 ILE   A CG2  1 
ATOM   1102 C CD1  . ILE   A 1 139 ? 9.72200   -3.65900  26.96700  1.000 29.28013 ?  136 ILE   A CD1  1 
ATOM   1103 N N    . MET   A 1 140 ? 6.62900   -8.18900  29.19000  1.000 14.98679 ?  137 MET   A N    1 
ATOM   1104 C CA   . MET   A 1 140 ? 6.30300   -9.18800  30.19600  1.000 16.54353 ?  137 MET   A CA   1 
ATOM   1105 C C    . MET   A 1 140 ? 7.55700   -9.76700  30.84400  1.000 17.87449 ?  137 MET   A C    1 
ATOM   1106 O O    . MET   A 1 140 ? 8.53500   -10.10000 30.16700  1.000 11.85188 ?  137 MET   A O    1 
ATOM   1107 C CB   . MET   A 1 140 ? 5.46700   -10.30600 29.59200  1.000 16.99125 ?  137 MET   A CB   1 
ATOM   1108 C CG   . MET   A 1 140 ? 4.07500   -9.91000  29.04900  1.000 18.93579 ?  137 MET   A CG   1 
ATOM   1109 S SD   . MET   A 1 140 ? 3.11300   -8.88900  30.17000  1.000 19.52815 ?  137 MET   A SD   1 
ATOM   1110 C CE   . MET   A 1 140 ? 2.30900   -10.12100 31.16400  1.000 24.72942 ?  137 MET   A CE   1 
ATOM   1111 N N    . THR   A 1 141 ? 7.51600   -9.89400  32.16700  1.000 15.27662 ?  138 THR   A N    1 
ATOM   1112 C CA   . THR   A 1 141 ? 8.62500   -10.42800 32.93900  1.000 12.88048 ?  138 THR   A CA   1 
ATOM   1113 C C    . THR   A 1 141 ? 8.13600   -11.59300 33.78400  1.000 12.35143 ?  138 THR   A C    1 
ATOM   1114 O O    . THR   A 1 141 ? 6.94500   -11.71600 34.09300  1.000 12.19144 ?  138 THR   A O    1 
ATOM   1115 C CB   . THR   A 1 141 ? 9.24900   -9.36300  33.84100  1.000 17.04920 ?  138 THR   A CB   1 
ATOM   1116 O OG1  . THR   A 1 141 ? 8.24700   -8.82300  34.71700  1.000 16.89455 ?  138 THR   A OG1  1 
ATOM   1117 C CG2  . THR   A 1 141 ? 9.82600   -8.23600  32.98500  1.000 16.34996 ?  138 THR   A CG2  1 
ATOM   1118 N N    . ASP   A 1 142 ? 9.08300   -12.44800 34.15500  1.000 10.66261 ?  139 ASP   A N    1 
ATOM   1119 C CA   . ASP   A 1 142 ? 8.76900   -13.62200 34.95200  1.000 12.42627 ?  139 ASP   A CA   1 
ATOM   1120 C C    . ASP   A 1 142 ? 8.39000   -13.23000 36.37400  1.000 13.97682 ?  139 ASP   A C    1 
ATOM   1121 O O    . ASP   A 1 142 ? 9.08600   -12.44000 37.02400  1.000 12.78448 ?  139 ASP   A O    1 
ATOM   1122 C CB   . ASP   A 1 142 ? 9.96600   -14.56900 34.95600  1.000 13.27781 ?  139 ASP   A CB   1 
ATOM   1123 C CG   . ASP   A 1 142 ? 9.64100   -15.90000 35.58000  1.000 20.58155 ?  139 ASP   A CG   1 
ATOM   1124 O OD1  . ASP   A 1 142 ? 9.80400   -16.00500 36.81500  1.000 15.65570 ?  139 ASP   A OD1  1 
ATOM   1125 O OD2  . ASP   A 1 142 ? 9.22600   -16.82500 34.84800  1.000 24.23528 -1 139 ASP   A OD2  1 
ATOM   1126 N N    . ARG   A 1 143 ? 7.27500   -13.79800 36.84800  1.000 11.26886 ?  140 ARG   A N    1 
ATOM   1127 C CA   . ARG   A 1 143 ? 6.72600   -13.48300 38.16100  1.000 10.00291 ?  140 ARG   A CA   1 
ATOM   1128 C C    . ARG   A 1 143 ? 7.72000   -13.79300 39.27500  1.000 10.59539 ?  140 ARG   A C    1 
ATOM   1129 O O    . ARG   A 1 143 ? 7.70700   -13.12200 40.31100  1.000 14.31222 ?  140 ARG   A O    1 
ATOM   1130 C CB   . ARG   A 1 143 ? 5.42400   -14.27400 38.36100  1.000 13.06310 ?  140 ARG   A CB   1 
ATOM   1131 C CG   . ARG   A 1 143 ? 4.71700   -14.07400 39.71500  1.000 13.70253 ?  140 ARG   A CG   1 
ATOM   1132 C CD   . ARG   A 1 143 ? 3.31400   -14.69200 39.70100  1.000 15.99164 ?  140 ARG   A CD   1 
ATOM   1133 N NE   . ARG   A 1 143 ? 2.48800   -14.18400 38.60900  1.000 15.02440 ?  140 ARG   A NE   1 
ATOM   1134 C CZ   . ARG   A 1 143 ? 1.83400   -13.03000 38.63300  1.000 22.36992 ?  140 ARG   A CZ   1 
ATOM   1135 N NH1  . ARG   A 1 143 ? 1.85800   -12.24100 39.70200  1.000 21.16176 ?  140 ARG   A NH1  1 
ATOM   1136 N NH2  . ARG   A 1 143 ? 1.12300   -12.66700 37.56300  1.000 16.67457 ?  140 ARG   A NH2  1 
ATOM   1137 N N    . GLY   A 1 144 ? 8.57000   -14.80000 39.08500  1.000 12.60794 ?  141 GLY   A N    1 
ATOM   1138 C CA   . GLY   A 1 144 ? 9.52100   -15.21500 40.10900  1.000 10.89895 ?  141 GLY   A CA   1 
ATOM   1139 C C    . GLY   A 1 144 ? 10.88400  -14.55300 40.03800  1.000 11.20295 ?  141 GLY   A C    1 
ATOM   1140 O O    . GLY   A 1 144 ? 11.40800  -14.10800 41.06700  1.000 10.97543 ?  141 GLY   A O    1 
ATOM   1141 N N    . SER   A 1 145 ? 11.46400  -14.47200 38.83200  1.000 10.70750 ?  142 SER   A N    1 
ATOM   1142 C CA   . SER   A 1 145 ? 12.83000  -13.99400 38.64600  1.000 8.25143  ?  142 SER   A CA   1 
ATOM   1143 C C    . SER   A 1 145 ? 12.91400  -12.56900 38.13800  1.000 12.74872 ?  142 SER   A C    1 
ATOM   1144 O O    . SER   A 1 145 ? 13.98400  -11.95700 38.24400  1.000 15.30978 ?  142 SER   A O    1 
ATOM   1145 C CB   . SER   A 1 145 ? 13.58000  -14.87600 37.64500  1.000 14.19887 ?  142 SER   A CB   1 
ATOM   1146 O OG   . SER   A 1 145 ? 13.00000  -14.75500 36.34400  1.000 12.63623 ?  142 SER   A OG   1 
ATOM   1147 N N    . GLY   A 1 146 ? 11.83800  -12.03800 37.56300  1.000 12.67272 ?  143 GLY   A N    1 
ATOM   1148 C CA   . GLY   A 1 146 ? 11.90900  -10.74300 36.91600  1.000 13.93611 ?  143 GLY   A CA   1 
ATOM   1149 C C    . GLY   A 1 146 ? 12.54700  -10.74400 35.54100  1.000 12.87303 ?  143 GLY   A C    1 
ATOM   1150 O O    . GLY   A 1 146 ? 12.64200  -9.67600  34.92000  1.000 15.42000 ?  143 GLY   A O    1 
ATOM   1151 N N    . LYS   A 1 147 ? 12.97700  -11.89600 35.04400  1.000 11.92709 ?  144 LYS   A N    1 
ATOM   1152 C CA   . LYS   A 1 147 ? 13.59200  -11.95900 33.72800  1.000 13.36761 ?  144 LYS   A CA   1 
ATOM   1153 C C    . LYS   A 1 147 ? 12.54800  -11.71300 32.65200  1.000 16.09068 ?  144 LYS   A C    1 
ATOM   1154 O O    . LYS   A 1 147 ? 11.38300  -12.07500 32.79700  1.000 14.47955 ?  144 LYS   A O    1 
ATOM   1155 C CB   . LYS   A 1 147 ? 14.25900  -13.31000 33.50500  1.000 14.77329 ?  144 LYS   A CB   1 
ATOM   1156 C CG   . LYS   A 1 147 ? 15.59200  -13.46000 34.22500  1.000 21.72869 ?  144 LYS   A CG   1 
ATOM   1157 C CD   . LYS   A 1 147 ? 16.20600  -14.81700 33.91000  1.000 22.45661 ?  144 LYS   A CD   1 
ATOM   1158 C CE   . LYS   A 1 147 ? 17.21100  -15.23100 34.96600  1.000 41.07359 ?  144 LYS   A CE   1 
ATOM   1159 N NZ   . LYS   A 1 147 ? 18.15600  -16.24000 34.40600  1.000 49.29742 ?  144 LYS   A NZ   1 
ATOM   1160 N N    . LYS   A 1 148 ? 12.97400  -11.08200 31.56500  1.000 13.95707 ?  145 LYS   A N    1 
ATOM   1161 C CA   . LYS   A 1 148 ? 12.04700  -10.83100 30.47400  1.000 14.47148 ?  145 LYS   A CA   1 
ATOM   1162 C C    . LYS   A 1 148 ? 11.62500  -12.15000 29.84200  1.000 13.42463 ?  145 LYS   A C    1 
ATOM   1163 O O    . LYS   A 1 148 ? 12.42800  -13.08200 29.70500  1.000 16.04804 ?  145 LYS   A O    1 
ATOM   1164 C CB   . LYS   A 1 148 ? 12.69900  -9.87700  29.46500  1.000 18.60335 ?  145 LYS   A CB   1 
ATOM   1165 C CG   . LYS   A 1 148 ? 12.86900  -8.47700  30.08500  1.000 22.65292 ?  145 LYS   A CG   1 
ATOM   1166 C CD   . LYS   A 1 148 ? 12.80900  -7.33000  29.09500  1.000 31.79372 ?  145 LYS   A CD   1 
ATOM   1167 C CE   . LYS   A 1 148 ? 14.17400  -6.69300  28.91800  1.000 39.17331 ?  145 LYS   A CE   1 
ATOM   1168 N NZ   . LYS   A 1 148 ? 14.45200  -6.29300  27.51100  1.000 44.65421 ?  145 LYS   A NZ   1 
ATOM   1169 N N    . ARG   A 1 149 ? 10.34100  -12.25700 29.50900  1.000 11.59293 ?  146 ARG   A N    1 
ATOM   1170 C CA   . ARG   A 1 149 ? 9.80800   -13.49700 28.96300  1.000 9.63173  ?  146 ARG   A CA   1 
ATOM   1171 C C    . ARG   A 1 149 ? 9.79400   -13.52500 27.44300  1.000 10.16151 ?  146 ARG   A C    1 
ATOM   1172 O O    . ARG   A 1 149 ? 9.56600   -14.58700 26.86100  1.000 17.85123 ?  146 ARG   A O    1 
ATOM   1173 C CB   . ARG   A 1 149 ? 8.40300   -13.74300 29.49800  1.000 14.92683 ?  146 ARG   A CB   1 
ATOM   1174 C CG   . ARG   A 1 149 ? 8.42900   -14.06400 30.98700  1.000 14.14689 ?  146 ARG   A CG   1 
ATOM   1175 C CD   . ARG   A 1 149 ? 7.05100   -14.41200 31.49000  1.000 18.57510 ?  146 ARG   A CD   1 
ATOM   1176 N NE   . ARG   A 1 149 ? 6.54400   -15.62400 30.85600  1.000 15.56413 ?  146 ARG   A NE   1 
ATOM   1177 C CZ   . ARG   A 1 149 ? 5.25600   -15.92700 30.78100  1.000 14.21336 ?  146 ARG   A CZ   1 
ATOM   1178 N NH1  . ARG   A 1 149 ? 4.33600   -15.15700 31.33000  1.000 13.90280 ?  146 ARG   A NH1  1 
ATOM   1179 N NH2  . ARG   A 1 149 ? 4.88500   -17.03300 30.14300  1.000 19.20943 ?  146 ARG   A NH2  1 
ATOM   1180 N N    . GLY   A 1 150 ? 10.04900  -12.39800 26.79600  1.000 12.60273 ?  147 GLY   A N    1 
ATOM   1181 C CA   . GLY   A 1 150 ? 10.14100  -12.39000 25.35400  1.000 15.07292 ?  147 GLY   A CA   1 
ATOM   1182 C C    . GLY   A 1 150 ? 8.84900   -12.08700 24.63600  1.000 16.98917 ?  147 GLY   A C    1 
ATOM   1183 O O    . GLY   A 1 150 ? 8.73300   -12.39900 23.44500  1.000 15.50014 ?  147 GLY   A O    1 
ATOM   1184 N N    . PHE   A 1 151 ? 7.86700   -11.50800 25.32000  1.000 14.44495 ?  148 PHE   A N    1 
ATOM   1185 C CA   . PHE   A 1 151 ? 6.68100   -10.99900 24.64600  1.000 11.24163 ?  148 PHE   A CA   1 
ATOM   1186 C C    . PHE   A 1 151 ? 6.16600   -9.78900  25.40500  1.000 13.22744 ?  148 PHE   A C    1 
ATOM   1187 O O    . PHE   A 1 151 ? 6.60300   -9.49200  26.52100  1.000 12.13072 ?  148 PHE   A O    1 
ATOM   1188 C CB   . PHE   A 1 151 ? 5.59500   -12.07700 24.47000  1.000 12.30393 ?  148 PHE   A CB   1 
ATOM   1189 C CG   . PHE   A 1 151 ? 4.99200   -12.58500 25.75900  1.000 18.31760 ?  148 PHE   A CG   1 
ATOM   1190 C CD1  . PHE   A 1 151 ? 5.66500   -13.51600 26.53400  1.000 20.89090 ?  148 PHE   A CD1  1 
ATOM   1191 C CD2  . PHE   A 1 151 ? 3.73500   -12.16100 26.17100  1.000 16.87318 ?  148 PHE   A CD2  1 
ATOM   1192 C CE1  . PHE   A 1 151 ? 5.10200   -14.01100 27.70600  1.000 14.63301 ?  148 PHE   A CE1  1 
ATOM   1193 C CE2  . PHE   A 1 151 ? 3.16700   -12.64600 27.34300  1.000 19.57982 ?  148 PHE   A CE2  1 
ATOM   1194 C CZ   . PHE   A 1 151 ? 3.86200   -13.56900 28.11600  1.000 17.98836 ?  148 PHE   A CZ   1 
ATOM   1195 N N    . ALA   A 1 152 ? 5.24100   -9.07400  24.76500  1.000 10.67465 ?  149 ALA   A N    1 
ATOM   1196 C CA   . ALA   A 1 152 ? 4.76200   -7.80300  25.27900  1.000 12.30963 ?  149 ALA   A CA   1 
ATOM   1197 C C    . ALA   A 1 152 ? 3.33800   -7.57700  24.79600  1.000 10.55613 ?  149 ALA   A C    1 
ATOM   1198 O O    . ALA   A 1 152 ? 2.85300   -8.24800  23.87900  1.000 11.55744 ?  149 ALA   A O    1 
ATOM   1199 C CB   . ALA   A 1 152 ? 5.66300   -6.63900  24.83200  1.000 11.89462 ?  149 ALA   A CB   1 
ATOM   1200 N N    . PHE   A 1 153 ? 2.67100   -6.62000  25.43100  1.000 11.77014 ?  150 PHE   A N    1 
ATOM   1201 C CA   . PHE   A 1 153 ? 1.35100   -6.17600  24.99900  1.000 11.26208 ?  150 PHE   A CA   1 
ATOM   1202 C C    . PHE   A 1 153 ? 1.40300   -4.67600  24.75300  1.000 12.18079 ?  150 PHE   A C    1 
ATOM   1203 O O    . PHE   A 1 153 ? 1.99500   -3.92400  25.53600  1.000 11.85620 ?  150 PHE   A O    1 
ATOM   1204 C CB   . PHE   A 1 153 ? 0.28000   -6.49900  26.04500  1.000 12.13317 ?  150 PHE   A CB   1 
ATOM   1205 C CG   . PHE   A 1 153 ? 0.02300   -7.96400  26.21400  1.000 11.39046 ?  150 PHE   A CG   1 
ATOM   1206 C CD1  . PHE   A 1 153 ? -0.79900  -8.65400  25.33700  1.000 11.78641 ?  150 PHE   A CD1  1 
ATOM   1207 C CD2  . PHE   A 1 153 ? 0.64400   -8.66400  27.23200  1.000 15.87346 ?  150 PHE   A CD2  1 
ATOM   1208 C CE1  . PHE   A 1 153 ? -1.01400  -10.00400 25.48700  1.000 17.50735 ?  150 PHE   A CE1  1 
ATOM   1209 C CE2  . PHE   A 1 153 ? 0.43600   -10.02500 27.38300  1.000 13.83933 ?  150 PHE   A CE2  1 
ATOM   1210 C CZ   . PHE   A 1 153 ? -0.39300  -10.69300 26.51400  1.000 17.84006 ?  150 PHE   A CZ   1 
ATOM   1211 N N    . VAL   A 1 154 ? 0.81700   -4.23700  23.64900  1.000 10.12091 ?  151 VAL   A N    1 
ATOM   1212 C CA   . VAL   A 1 154 ? 0.72800   -2.82200  23.32200  1.000 8.27131  ?  151 VAL   A CA   1 
ATOM   1213 C C    . VAL   A 1 154 ? -0.74600  -2.47900  23.20200  1.000 8.77829  ?  151 VAL   A C    1 
ATOM   1214 O O    . VAL   A 1 154 ? -1.47900  -3.15600  22.46900  1.000 10.65593 ?  151 VAL   A O    1 
ATOM   1215 C CB   . VAL   A 1 154 ? 1.47200   -2.48300  22.01500  1.000 9.15554  ?  151 VAL   A CB   1 
ATOM   1216 C CG1  . VAL   A 1 154 ? 1.37700   -0.99100  21.71900  1.000 10.48886 ?  151 VAL   A CG1  1 
ATOM   1217 C CG2  . VAL   A 1 154 ? 2.94500   -2.94200  22.08900  1.000 10.49482 ?  151 VAL   A CG2  1 
ATOM   1218 N N    . THR   A 1 155 ? -1.18500  -1.45800  23.93700  1.000 9.18719  ?  152 THR   A N    1 
ATOM   1219 C CA   . THR   A 1 155 ? -2.57000  -0.99600  23.88700  1.000 8.82175  ?  152 THR   A CA   1 
ATOM   1220 C C    . THR   A 1 155 ? -2.60800  0.36100   23.21300  1.000 9.34265  ?  152 THR   A C    1 
ATOM   1221 O O    . THR   A 1 155 ? -1.84200  1.26600   23.57400  1.000 9.61262  ?  152 THR   A O    1 
ATOM   1222 C CB   . THR   A 1 155 ? -3.18300  -0.88800  25.28900  1.000 10.84296 ?  152 THR   A CB   1 
ATOM   1223 O OG1  . THR   A 1 155 ? -3.12400  -2.16600  25.92500  1.000 11.60054 ?  152 THR   A OG1  1 
ATOM   1224 C CG2  . THR   A 1 155 ? -4.66700  -0.44700  25.19200  1.000 12.69108 ?  152 THR   A CG2  1 
ATOM   1225 N N    . PHE   A 1 156 ? -3.50000  0.49900   22.23400  1.000 7.19415  ?  153 PHE   A N    1 
ATOM   1226 C CA   . PHE   A 1 156 ? -3.67800  1.72700   21.48400  1.000 6.90093  ?  153 PHE   A CA   1 
ATOM   1227 C C    . PHE   A 1 156 ? -4.95900  2.42300   21.90700  1.000 8.48245  ?  153 PHE   A C    1 
ATOM   1228 O O    . PHE   A 1 156 ? -5.79200  1.85200   22.61200  1.000 10.17135 ?  153 PHE   A O    1 
ATOM   1229 C CB   . PHE   A 1 156 ? -3.72700  1.42200   19.98400  1.000 6.74037  ?  153 PHE   A CB   1 
ATOM   1230 C CG   . PHE   A 1 156 ? -2.46200  0.82300   19.45100  1.000 7.00784  ?  153 PHE   A CG   1 
ATOM   1231 C CD1  . PHE   A 1 156 ? -1.46600  1.63600   18.93900  1.000 7.38685  ?  153 PHE   A CD1  1 
ATOM   1232 C CD2  . PHE   A 1 156 ? -2.27900  -0.55200  19.43300  1.000 9.00288  ?  153 PHE   A CD2  1 
ATOM   1233 C CE1  . PHE   A 1 156 ? -0.30100  1.09300   18.41700  1.000 6.12484  ?  153 PHE   A CE1  1 
ATOM   1234 C CE2  . PHE   A 1 156 ? -1.11600  -1.10800  18.91800  1.000 10.14792 ?  153 PHE   A CE2  1 
ATOM   1235 C CZ   . PHE   A 1 156 ? -0.13000  -0.27800  18.40500  1.000 9.75718  ?  153 PHE   A CZ   1 
ATOM   1236 N N    . ASP   A 1 157 ? -5.11900  3.66100   21.44400  1.000 8.85971  ?  154 ASP   A N    1 
ATOM   1237 C CA   . ASP   A 1 157 ? -6.34400  4.37900   21.77300  1.000 10.03011 ?  154 ASP   A CA   1 
ATOM   1238 C C    . ASP   A 1 157 ? -7.48200  4.05700   20.82400  1.000 12.83332 ?  154 ASP   A C    1 
ATOM   1239 O O    . ASP   A 1 157 ? -8.58300  4.57300   21.02300  1.000 13.85314 ?  154 ASP   A O    1 
ATOM   1240 C CB   . ASP   A 1 157 ? -6.08400  5.89500   21.83900  1.000 11.23197 ?  154 ASP   A CB   1 
ATOM   1241 C CG   . ASP   A 1 157 ? -5.99300  6.57700   20.47400  1.000 16.47547 ?  154 ASP   A CG   1 
ATOM   1242 O OD1  . ASP   A 1 157 ? -6.04200  5.92100   19.41100  1.000 13.21091 ?  154 ASP   A OD1  1 
ATOM   1243 O OD2  . ASP   A 1 157 ? -5.85600  7.82300   20.47300  1.000 18.28312 -1 154 ASP   A OD2  1 
ATOM   1244 N N    . ASP   A 1 158 ? -7.26800  3.18100   19.84200  1.000 10.18149 ?  155 ASP   A N    1 
ATOM   1245 C CA   . ASP   A 1 158 ? -8.29100  2.95400   18.83000  1.000 10.46767 ?  155 ASP   A CA   1 
ATOM   1246 C C    . ASP   A 1 158 ? -7.99500  1.66000   18.08600  1.000 9.49289  ?  155 ASP   A C    1 
ATOM   1247 O O    . ASP   A 1 158 ? -6.83500  1.27500   17.91300  1.000 10.55985 ?  155 ASP   A O    1 
ATOM   1248 C CB   . ASP   A 1 158 ? -8.34500  4.15900   17.88200  1.000 16.70776 ?  155 ASP   A CB   1 
ATOM   1249 C CG   . ASP   A 1 158 ? -9.19500  3.91800   16.64500  1.000 12.20806 ?  155 ASP   A CG   1 
ATOM   1250 O OD1  . ASP   A 1 158 ? -10.43700 3.99000   16.73000  1.000 13.24959 ?  155 ASP   A OD1  1 
ATOM   1251 O OD2  . ASP   A 1 158 ? -8.58400  3.68700   15.59400  1.000 11.27230 -1 155 ASP   A OD2  1 
ATOM   1252 N N    . HIS   A 1 159 ? -9.06300  1.02300   17.59800  1.000 7.32729  ?  156 HIS   A N    1 
ATOM   1253 C CA   . HIS   A 1 159 ? -8.94700  -0.30000  17.00300  1.000 9.90489  ?  156 HIS   A CA   1 
ATOM   1254 C C    . HIS   A 1 159 ? -8.28100  -0.30000  15.63700  1.000 8.56048  ?  156 HIS   A C    1 
ATOM   1255 O O    . HIS   A 1 159 ? -7.78600  -1.35100  15.22300  1.000 6.82666  ?  156 HIS   A O    1 
ATOM   1256 C CB   . HIS   A 1 159 ? -10.33200 -0.93800  16.88200  1.000 9.46412  ?  156 HIS   A CB   1 
ATOM   1257 C CG   . HIS   A 1 159 ? -11.17900 -0.28700  15.83400  1.000 7.58345  ?  156 HIS   A CG   1 
ATOM   1258 N ND1  . HIS   A 1 159 ? -11.16700 -0.68400  14.51500  1.000 9.84053  ?  156 HIS   A ND1  1 
ATOM   1259 C CD2  . HIS   A 1 159 ? -12.06500 0.73400   15.91500  1.000 11.20199 ?  156 HIS   A CD2  1 
ATOM   1260 C CE1  . HIS   A 1 159 ? -11.99100 0.08000   13.82000  1.000 10.29952 ?  156 HIS   A CE1  1 
ATOM   1261 N NE2  . HIS   A 1 159 ? -12.56300 0.93700   14.64800  1.000 11.86501 ?  156 HIS   A NE2  1 
ATOM   1262 N N    . ASP   A 1 160 ? -8.28700  0.82000   14.89900  1.000 7.20207  ?  157 ASP   A N    1 
ATOM   1263 C CA   . ASP   A 1 160 ? -7.78200  0.73600   13.52700  1.000 7.10159  ?  157 ASP   A CA   1 
ATOM   1264 C C    . ASP   A 1 160 ? -6.29200  0.47200   13.49800  1.000 7.07772  ?  157 ASP   A C    1 
ATOM   1265 O O    . ASP   A 1 160 ? -5.80700  -0.19500  12.58300  1.000 7.91642  ?  157 ASP   A O    1 
ATOM   1266 C CB   . ASP   A 1 160 ? -8.08700  1.99400   12.72700  1.000 7.69857  ?  157 ASP   A CB   1 
ATOM   1267 C CG   . ASP   A 1 160 ? -7.89100  1.76700   11.23100  1.000 6.73678  ?  157 ASP   A CG   1 
ATOM   1268 O OD1  . ASP   A 1 160 ? -8.45500  0.77700   10.69300  1.000 9.16317  ?  157 ASP   A OD1  1 
ATOM   1269 O OD2  . ASP   A 1 160 ? -7.16800  2.57800   10.60600  1.000 8.87260  -1 157 ASP   A OD2  1 
ATOM   1270 N N    . SER   A 1 161 ? -5.56600  0.98300   14.48800  1.000 8.60560  ?  158 SER   A N    1 
ATOM   1271 C CA   . SER   A 1 161 ? -4.16100  0.63100   14.64400  1.000 6.15082  ?  158 SER   A CA   1 
ATOM   1272 C C    . SER   A 1 161 ? -3.96300  -0.87900  14.62200  1.000 8.53476  ?  158 SER   A C    1 
ATOM   1273 O O    . SER   A 1 161 ? -3.15200  -1.40100  13.85400  1.000 8.77867  ?  158 SER   A O    1 
ATOM   1274 C CB   . SER   A 1 161 ? -3.66900  1.23500   15.95100  1.000 8.83779  ?  158 SER   A CB   1 
ATOM   1275 O OG   . SER   A 1 161 ? -4.43100  0.65100   16.99700  1.000 12.83021 ?  158 SER   A OG   1 
ATOM   1276 N N    . VAL   A 1 162 ? -4.69300  -1.59400  15.47500  1.000 7.33148  ?  159 VAL   A N    1 
ATOM   1277 C CA   . VAL   A 1 162 ? -4.58900  -3.04900  15.53900  1.000 6.91009  ?  159 VAL   A CA   1 
ATOM   1278 C C    . VAL   A 1 162 ? -4.97800  -3.68600  14.21000  1.000 6.44134  ?  159 VAL   A C    1 
ATOM   1279 O O    . VAL   A 1 162 ? -4.32000  -4.61800  13.73200  1.000 8.42569  ?  159 VAL   A O    1 
ATOM   1280 C CB   . VAL   A 1 162 ? -5.47600  -3.58500  16.68200  1.000 6.20605  ?  159 VAL   A CB   1 
ATOM   1281 C CG1  . VAL   A 1 162 ? -5.47900  -5.13100  16.66900  1.000 7.81525  ?  159 VAL   A CG1  1 
ATOM   1282 C CG2  . VAL   A 1 162 ? -5.02800  -2.99400  18.00900  1.000 12.56949 ?  159 VAL   A CG2  1 
ATOM   1283 N N    . ASP   A 1 163 ? -6.05000  -3.19300  13.59000  1.000 7.06509  ?  160 ASP   A N    1 
ATOM   1284 C CA   . ASP   A 1 163 ? -6.49400  -3.78600  12.33800  1.000 7.24132  ?  160 ASP   A CA   1 
ATOM   1285 C C    . ASP   A 1 163 ? -5.44000  -3.62400  11.25000  1.000 10.66765 ?  160 ASP   A C    1 
ATOM   1286 O O    . ASP   A 1 163 ? -5.24100  -4.53900  10.44500  1.000 12.35691 ?  160 ASP   A O    1 
ATOM   1287 C CB   . ASP   A 1 163 ? -7.81500  -3.15500  11.91200  1.000 8.00112  ?  160 ASP   A CB   1 
ATOM   1288 C CG   . ASP   A 1 163 ? -8.93800  -3.49100  12.84900  1.000 12.98701 ?  160 ASP   A CG   1 
ATOM   1289 O OD1  . ASP   A 1 163 ? -8.84500  -4.50700  13.57300  1.000 12.46569 ?  160 ASP   A OD1  1 
ATOM   1290 O OD2  . ASP   A 1 163 ? -9.92100  -2.71800  12.88000  1.000 14.35807 -1 160 ASP   A OD2  1 
ATOM   1291 N N    . LYS   A 1 164 ? -4.74700  -2.47600  11.20900  1.000 5.40488  ?  161 LYS   A N    1 
ATOM   1292 C CA   . LYS   A 1 164 ? -3.63900  -2.32400  10.26200  1.000 4.99515  ?  161 LYS   A CA   1 
ATOM   1293 C C    . LYS   A 1 164 ? -2.50100  -3.27600  10.58300  1.000 9.05900  ?  161 LYS   A C    1 
ATOM   1294 O O    . LYS   A 1 164 ? -1.88700  -3.86000  9.67700   1.000 8.03519  ?  161 LYS   A O    1 
ATOM   1295 C CB   . LYS   A 1 164 ? -3.12900  -0.88200  10.28200  1.000 4.62894  ?  161 LYS   A CB   1 
ATOM   1296 C CG   . LYS   A 1 164 ? -4.06200  0.10600   9.57500   1.000 7.56266  ?  161 LYS   A CG   1 
ATOM   1297 C CD   . LYS   A 1 164 ? -3.45900  1.50400   9.58000   1.000 6.68528  ?  161 LYS   A CD   1 
ATOM   1298 C CE   . LYS   A 1 164 ? -3.38100  2.06400   10.99300  1.000 12.17678 ?  161 LYS   A CE   1 
ATOM   1299 N NZ   . LYS   A 1 164 ? -2.77700  3.43900   10.95200  1.000 12.61644 ?  161 LYS   A NZ   1 
ATOM   1300 N N    . ILE   A 1 165 ? -2.19400  -3.42500  11.86700  1.000 7.28081  ?  162 ILE   A N    1 
ATOM   1301 C CA   . ILE   A 1 165 ? -1.04100  -4.21200  12.28200  1.000 8.08485  ?  162 ILE   A CA   1 
ATOM   1302 C C    . ILE   A 1 165 ? -1.22200  -5.67800  11.91900  1.000 9.19593  ?  162 ILE   A C    1 
ATOM   1303 O O    . ILE   A 1 165 ? -0.30500  -6.32400  11.39300  1.000 8.25429  ?  162 ILE   A O    1 
ATOM   1304 C CB   . ILE   A 1 165 ? -0.81500  -4.03300  13.79000  1.000 6.35824  ?  162 ILE   A CB   1 
ATOM   1305 C CG1  . ILE   A 1 165 ? -0.24900  -2.64000  14.06800  1.000 7.24043  ?  162 ILE   A CG1  1 
ATOM   1306 C CG2  . ILE   A 1 165 ? 0.12700   -5.11900  14.32000  1.000 7.77637  ?  162 ILE   A CG2  1 
ATOM   1307 C CD1  . ILE   A 1 165 ? -0.34700  -2.20800  15.53300  1.000 10.04595 ?  162 ILE   A CD1  1 
ATOM   1308 N N    . VAL   A 1 166 ? -2.39700  -6.24100  12.20800  1.000 7.11022  ?  163 VAL   A N    1 
ATOM   1309 C CA   . VAL   A 1 166 ? -2.48900  -7.69800  12.13500  1.000 9.04921  ?  163 VAL   A CA   1 
ATOM   1310 C C    . VAL   A 1 166 ? -2.67700  -8.20400  10.72200  1.000 10.97901 ?  163 VAL   A C    1 
ATOM   1311 O O    . VAL   A 1 166 ? -2.56100  -9.41800  10.49400  1.000 15.52713 ?  163 VAL   A O    1 
ATOM   1312 C CB   . VAL   A 1 166 ? -3.59800  -8.25900  13.04900  1.000 9.57587  ?  163 VAL   A CB   1 
ATOM   1313 C CG1  . VAL   A 1 166 ? -3.28600  -7.93800  14.52800  1.000 10.56930 ?  163 VAL   A CG1  1 
ATOM   1314 C CG2  . VAL   A 1 166 ? -4.97200  -7.74800  12.62700  1.000 12.93291 ?  163 VAL   A CG2  1 
ATOM   1315 N N    . ILE   A 1 167 ? -2.90700  -7.32000  9.75000   1.000 8.99790  ?  164 ILE   A N    1 
ATOM   1316 C CA   . ILE   A 1 167 ? -2.96700  -7.79500  8.37600   1.000 7.86670  ?  164 ILE   A CA   1 
ATOM   1317 C C    . ILE   A 1 167 ? -1.60600  -7.78300  7.70000   1.000 12.26220 ?  164 ILE   A C    1 
ATOM   1318 O O    . ILE   A 1 167 ? -1.47100  -8.35700  6.61000   1.000 14.92290 ?  164 ILE   A O    1 
ATOM   1319 C CB   . ILE   A 1 167 ? -3.93300  -6.97900  7.50100   1.000 14.49314 ?  164 ILE   A CB   1 
ATOM   1320 C CG1  . ILE   A 1 167 ? -3.72800  -5.49200  7.68100   1.000 20.55203 ?  164 ILE   A CG1  1 
ATOM   1321 C CG2  . ILE   A 1 167 ? -5.38900  -7.33400  7.84900   1.000 24.47808 ?  164 ILE   A CG2  1 
ATOM   1322 C CD1  . ILE   A 1 167 ? -4.82300  -4.69000  6.96400   1.000 18.45631 ?  164 ILE   A CD1  1 
ATOM   1323 N N    . GLN   A 1 168 ? -0.59300  -7.16700  8.30800   1.000 10.11338 ?  165 GLN   A N    1 
ATOM   1324 C CA   . GLN   A 1 168 ? 0.75500   -7.23800  7.75200   1.000 9.43565  ?  165 GLN   A CA   1 
ATOM   1325 C C    . GLN   A 1 168 ? 1.29300   -8.65900  7.84700   1.000 9.93759  ?  165 GLN   A C    1 
ATOM   1326 O O    . GLN   A 1 168 ? 1.10400   -9.34200  8.85700   1.000 13.48438 ?  165 GLN   A O    1 
ATOM   1327 C CB   . GLN   A 1 168 ? 1.71800   -6.30200  8.50000   1.000 7.63490  ?  165 GLN   A CB   1 
ATOM   1328 C CG   . GLN   A 1 168 ? 1.37900   -4.81200  8.40200   1.000 7.72054  ?  165 GLN   A CG   1 
ATOM   1329 C CD   . GLN   A 1 168 ? 1.66400   -4.23700  7.01800   1.000 8.73009  ?  165 GLN   A CD   1 
ATOM   1330 O OE1  . GLN   A 1 168 ? 0.76100   -4.17500  6.18800   1.000 9.48243  ?  165 GLN   A OE1  1 
ATOM   1331 N NE2  . GLN   A 1 168 ? 2.89700   -3.78700  6.77800   1.000 9.15731  ?  165 GLN   A NE2  1 
ATOM   1332 N N    . LYS   A 1 169 ? 2.01500   -9.08800  6.80500   1.000 7.96397  ?  166 LYS   A N    1 
ATOM   1333 C CA   . LYS   A 1 169 ? 2.64500   -10.40200 6.84700   1.000 10.32681 ?  166 LYS   A CA   1 
ATOM   1334 C C    . LYS   A 1 169 ? 3.79000   -10.45600 7.84700   1.000 10.49206 ?  166 LYS   A C    1 
ATOM   1335 O O    . LYS   A 1 169 ? 4.01400   -11.50900 8.46200   1.000 10.65602 ?  166 LYS   A O    1 
ATOM   1336 C CB   . LYS   A 1 169 ? 3.17000   -10.78400 5.46200   1.000 11.09758 ?  166 LYS   A CB   1 
ATOM   1337 C CG   . LYS   A 1 169 ? 2.14000   -11.44900 4.56500   1.000 20.47766 ?  166 LYS   A CG   1 
ATOM   1338 C CD   . LYS   A 1 169 ? 2.86000   -12.19200 3.45000   1.000 20.92077 ?  166 LYS   A CD   1 
ATOM   1339 C CE   . LYS   A 1 169 ? 1.89400   -12.68400 2.37900   1.000 27.10864 ?  166 LYS   A CE   1 
ATOM   1340 N NZ   . LYS   A 1 169 ? 2.39800   -13.96300 1.78500   1.000 26.16760 ?  166 LYS   A NZ   1 
ATOM   1341 N N    . TYR   A 1 170 ? 4.53800   -9.35100  8.01300   1.000 10.07948 ?  167 TYR   A N    1 
ATOM   1342 C CA   . TYR   A 1 170 ? 5.78300   -9.34600  8.76900   1.000 9.56519  ?  167 TYR   A CA   1 
ATOM   1343 C C    . TYR   A 1 170 ? 5.81700   -8.16600  9.72000   1.000 10.53043 ?  167 TYR   A C    1 
ATOM   1344 O O    . TYR   A 1 170 ? 5.29000   -7.09900  9.40700   1.000 9.10873  ?  167 TYR   A O    1 
ATOM   1345 C CB   . TYR   A 1 170 ? 7.00900   -9.22100  7.83800   1.000 8.35750  ?  167 TYR   A CB   1 
ATOM   1346 C CG   . TYR   A 1 170 ? 6.98600   -10.16400 6.66100   1.000 6.57772  ?  167 TYR   A CG   1 
ATOM   1347 C CD1  . TYR   A 1 170 ? 7.25900   -11.50800 6.83700   1.000 8.69421  ?  167 TYR   A CD1  1 
ATOM   1348 C CD2  . TYR   A 1 170 ? 6.66200   -9.72400  5.39400   1.000 13.37846 ?  167 TYR   A CD2  1 
ATOM   1349 C CE1  . TYR   A 1 170 ? 7.24000   -12.39500 5.78000   1.000 11.98908 ?  167 TYR   A CE1  1 
ATOM   1350 C CE2  . TYR   A 1 170 ? 6.63600   -10.60300 4.31900   1.000 9.38446  ?  167 TYR   A CE2  1 
ATOM   1351 C CZ   . TYR   A 1 170 ? 6.92200   -11.92500 4.52000   1.000 12.80557 ?  167 TYR   A CZ   1 
ATOM   1352 O OH   . TYR   A 1 170 ? 6.89100   -12.79200 3.45700   1.000 11.30852 ?  167 TYR   A OH   1 
ATOM   1353 N N    . HIS   A 1 171 ? 6.47200   -8.35700  10.86900  1.000 8.55620  ?  168 HIS   A N    1 
ATOM   1354 C CA   . HIS   A 1 171 ? 6.81000   -7.24900  11.75700  1.000 8.08752  ?  168 HIS   A CA   1 
ATOM   1355 C C    . HIS   A 1 171 ? 8.23100   -7.44300  12.24800  1.000 11.00492 ?  168 HIS   A C    1 
ATOM   1356 O O    . HIS   A 1 171 ? 8.54200   -8.48700  12.81400  1.000 12.84531 ?  168 HIS   A O    1 
ATOM   1357 C CB   . HIS   A 1 171 ? 5.84900   -7.18500  12.94100  1.000 10.25605 ?  168 HIS   A CB   1 
ATOM   1358 C CG   . HIS   A 1 171 ? 4.49100   -6.70300  12.56300  1.000 8.81124  ?  168 HIS   A CG   1 
ATOM   1359 N ND1  . HIS   A 1 171 ? 4.23800   -5.40300  12.19200  1.000 9.67569  ?  168 HIS   A ND1  1 
ATOM   1360 C CD2  . HIS   A 1 171 ? 3.31600   -7.36600  12.45000  1.000 12.10979 ?  168 HIS   A CD2  1 
ATOM   1361 C CE1  . HIS   A 1 171 ? 2.95800   -5.27900  11.88100  1.000 8.95476  ?  168 HIS   A CE1  1 
ATOM   1362 N NE2  . HIS   A 1 171 ? 2.37900   -6.45700  12.03100  1.000 10.93356 ?  168 HIS   A NE2  1 
ATOM   1363 N N    . THR   A 1 172 ? 9.08700   -6.44900  12.00100  1.000 11.37833 ?  169 THR   A N    1 
ATOM   1364 C CA   . THR   A 1 172 ? 10.49000  -6.47500  12.38500  1.000 13.68882 ?  169 THR   A CA   1 
ATOM   1365 C C    . THR   A 1 172 ? 10.67800  -5.38500  13.43000  1.000 12.22456 ?  169 THR   A C    1 
ATOM   1366 O O    . THR   A 1 172 ? 10.47400  -4.19900  13.14400  1.000 15.14472 ?  169 THR   A O    1 
ATOM   1367 C CB   . THR   A 1 172 ? 11.38600  -6.25600  11.16600  1.000 14.38260 ?  169 THR   A CB   1 
ATOM   1368 O OG1  . THR   A 1 172 ? 11.07100  -7.23900  10.16900  1.000 16.46222 ?  169 THR   A OG1  1 
ATOM   1369 C CG2  . THR   A 1 172 ? 12.84700  -6.37700  11.55600  1.000 18.77000 ?  169 THR   A CG2  1 
ATOM   1370 N N    . VAL   A 1 173 ? 11.01500  -5.79300  14.64800  1.000 13.63964 ?  170 VAL   A N    1 
ATOM   1371 C CA   . VAL   A 1 173 ? 11.28000  -4.87400  15.74800  1.000 16.46222 ?  170 VAL   A CA   1 
ATOM   1372 C C    . VAL   A 1 173 ? 12.59200  -5.28300  16.39400  1.000 18.71320 ?  170 VAL   A C    1 
ATOM   1373 O O    . VAL   A 1 173 ? 12.73100  -6.42700  16.84000  1.000 19.08203 ?  170 VAL   A O    1 
ATOM   1374 C CB   . VAL   A 1 173 ? 10.15600  -4.88700  16.79200  1.000 18.18401 ?  170 VAL   A CB   1 
ATOM   1375 C CG1  . VAL   A 1 173 ? 10.39700  -3.79500  17.83400  1.000 25.67278 ?  170 VAL   A CG1  1 
ATOM   1376 C CG2  . VAL   A 1 173 ? 8.80800   -4.68400  16.11200  1.000 18.01988 ?  170 VAL   A CG2  1 
ATOM   1377 N N    . ASN   A 1 174 ? 13.53500  -4.35100  16.47400  1.000 22.55227 ?  171 ASN   A N    1 
ATOM   1378 C CA   . ASN   A 1 174 ? 14.80800  -4.62200  17.14600  1.000 21.71362 ?  171 ASN   A CA   1 
ATOM   1379 C C    . ASN   A 1 174 ? 15.51400  -5.80800  16.49400  1.000 28.23041 ?  171 ASN   A C    1 
ATOM   1380 O O    . ASN   A 1 174 ? 16.08100  -6.67000  17.17100  1.000 27.82870 ?  171 ASN   A O    1 
ATOM   1381 C CB   . ASN   A 1 174 ? 14.59900  -4.87600  18.64300  1.000 16.52214 ?  171 ASN   A CB   1 
ATOM   1382 C CG   . ASN   A 1 174 ? 15.90500  -4.89500  19.42600  1.000 32.13564 ?  171 ASN   A CG   1 
ATOM   1383 O OD1  . ASN   A 1 174 ? 16.85800  -4.18800  19.09300  1.000 19.99771 ?  171 ASN   A OD1  1 
ATOM   1384 N ND2  . ASN   A 1 174 ? 15.96000  -5.73100  20.45800  1.000 27.17555 ?  171 ASN   A ND2  1 
ATOM   1385 N N    . GLY   A 1 175 ? 15.44600  -5.87100  15.16300  1.000 36.36502 ?  172 GLY   A N    1 
ATOM   1386 C CA   . GLY   A 1 175 ? 16.02000  -6.96500  14.40400  1.000 34.67050 ?  172 GLY   A CA   1 
ATOM   1387 C C    . GLY   A 1 175 ? 15.29400  -8.28800  14.50800  1.000 32.55642 ?  172 GLY   A C    1 
ATOM   1388 O O    . GLY   A 1 175 ? 15.65900  -9.23000  13.79200  1.000 40.69695 ?  172 GLY   A O    1 
ATOM   1389 N N    . HIS   A 1 176 ? 14.28600  -8.40100  15.36900  1.000 27.49529 ?  173 HIS   A N    1 
ATOM   1390 C CA   . HIS   A 1 176 ? 13.55300  -9.64300  15.55600  1.000 20.36099 ?  173 HIS   A CA   1 
ATOM   1391 C C    . HIS   A 1 176 ? 12.37600  -9.68400  14.58600  1.000 24.15629 ?  173 HIS   A C    1 
ATOM   1392 O O    . HIS   A 1 176 ? 11.72100  -8.66500  14.36100  1.000 18.55291 ?  173 HIS   A O    1 
ATOM   1393 C CB   . HIS   A 1 176 ? 13.02400  -9.73200  16.98900  1.000 23.76625 ?  173 HIS   A CB   1 
ATOM   1394 C CG   . HIS   A 1 176 ? 14.09100  -9.91400  18.02500  1.000 23.43434 ?  173 HIS   A CG   1 
ATOM   1395 N ND1  . HIS   A 1 176 ? 14.83600  -11.06900 18.14000  1.000 28.25811 ?  173 HIS   A ND1  1 
ATOM   1396 C CD2  . HIS   A 1 176 ? 14.54500  -9.07600  18.99000  1.000 29.28229 ?  173 HIS   A CD2  1 
ATOM   1397 C CE1  . HIS   A 1 176 ? 15.69200  -10.94000 19.14000  1.000 26.32035 ?  173 HIS   A CE1  1 
ATOM   1398 N NE2  . HIS   A 1 176 ? 15.54100  -9.73900  19.66800  1.000 25.11830 ?  173 HIS   A NE2  1 
ATOM   1399 N N    . ASN   A 1 177 ? 12.10200  -10.86300 14.02700  1.000 25.09158 ?  174 ASN   A N    1 
ATOM   1400 C CA   . ASN   A 1 177 ? 10.83200  -11.10800 13.34500  1.000 21.40928 ?  174 ASN   A CA   1 
ATOM   1401 C C    . ASN   A 1 177 ? 9.79300   -11.50100 14.38800  1.000 22.17476 ?  174 ASN   A C    1 
ATOM   1402 O O    . ASN   A 1 177 ? 9.90000   -12.56300 15.01100  1.000 23.58057 ?  174 ASN   A O    1 
ATOM   1403 C CB   . ASN   A 1 177 ? 10.97500  -12.19200 12.28300  1.000 26.38501 ?  174 ASN   A CB   1 
ATOM   1404 C CG   . ASN   A 1 177 ? 11.39600  -11.63400 10.92900  1.000 42.66002 ?  174 ASN   A CG   1 
ATOM   1405 O OD1  . ASN   A 1 177 ? 11.92700  -12.36000 10.08500  1.000 47.83300 ?  174 ASN   A OD1  1 
ATOM   1406 N ND2  . ASN   A 1 177 ? 11.14600  -10.33900 10.71100  1.000 36.21237 ?  174 ASN   A ND2  1 
ATOM   1407 N N    . CYS   A 1 178 ? 8.79200   -10.64900 14.57800  1.000 15.11298 ?  175 CYS   A N    1 
ATOM   1408 C CA   . CYS   A 1 178 ? 7.83800   -10.78800 15.66800  1.000 14.47141 ?  175 CYS   A CA   1 
ATOM   1409 C C    . CYS   A 1 178 ? 6.52800   -11.39300 15.18200  1.000 16.35372 ?  175 CYS   A C    1 
ATOM   1410 O O    . CYS   A 1 178 ? 6.12000   -11.20300 14.03600  1.000 16.50871 ?  175 CYS   A O    1 
ATOM   1411 C CB   . CYS   A 1 178 ? 7.55900   -9.42900  16.30700  1.000 13.27793 ?  175 CYS   A CB   1 
ATOM   1412 S SG   . CYS   A 1 178 ? 9.02100   -8.71500  17.05600  1.000 23.26017 ?  175 CYS   A SG   1 
ATOM   1413 N N    . GLU   A 1 179 ? 5.87600   -12.12700 16.07200  1.000 16.10802 ?  176 GLU   A N    1 
ATOM   1414 C CA   . GLU   A 1 179 ? 4.52200   -12.61500 15.86800  1.000 16.57541 ?  176 GLU   A CA   1 
ATOM   1415 C C    . GLU   A 1 179 ? 3.58200   -11.64600 16.56900  1.000 15.67612 ?  176 GLU   A C    1 
ATOM   1416 O O    . GLU   A 1 179 ? 3.75300   -11.37700 17.75500  1.000 16.66873 ?  176 GLU   A O    1 
ATOM   1417 C CB   . GLU   A 1 179 ? 4.36900   -14.03000 16.43400  1.000 26.46359 ?  176 GLU   A CB   1 
ATOM   1418 C CG   . GLU   A 1 179 ? 2.93700   -14.46200 16.66300  1.000 36.84633 ?  176 GLU   A CG   1 
ATOM   1419 C CD   . GLU   A 1 179 ? 2.83300   -15.92300 17.05400  1.000 47.81801 ?  176 GLU   A CD   1 
ATOM   1420 O OE1  . GLU   A 1 179 ? 3.88700   -16.53100 17.34800  1.000 54.54125 ?  176 GLU   A OE1  1 
ATOM   1421 O OE2  . GLU   A 1 179 ? 1.70400   -16.46300 17.05900  1.000 62.53276 -1 176 GLU   A OE2  1 
ATOM   1422 N N    . VAL   A 1 180 ? 2.60800   -11.10800 15.84300  1.000 11.00490 ?  177 VAL   A N    1 
ATOM   1423 C CA   . VAL   A 1 180 ? 1.70500   -10.11800 16.41400  1.000 11.28951 ?  177 VAL   A CA   1 
ATOM   1424 C C    . VAL   A 1 180 ? 0.27800   -10.59900 16.20100  1.000 17.90808 ?  177 VAL   A C    1 
ATOM   1425 O O    . VAL   A 1 180 ? -0.10300  -10.97400 15.08400  1.000 17.12259 ?  177 VAL   A O    1 
ATOM   1426 C CB   . VAL   A 1 180 ? 1.91900   -8.71800  15.80200  1.000 11.04878 ?  177 VAL   A CB   1 
ATOM   1427 C CG1  . VAL   A 1 180 ? 0.96900   -7.70300  16.43500  1.000 15.11383 ?  177 VAL   A CG1  1 
ATOM   1428 C CG2  . VAL   A 1 180 ? 3.36500   -8.28200  15.97100  1.000 12.97018 ?  177 VAL   A CG2  1 
ATOM   1429 N N    . ARG   A 1 181 ? -0.50500  -10.58900 17.27600  1.000 15.03395 ?  178 ARG   A N    1 
ATOM   1430 C CA   . ARG   A 1 181 ? -1.87800  -11.05500 17.23300  1.000 13.70500 ?  178 ARG   A CA   1 
ATOM   1431 C C    . ARG   A 1 181 ? -2.74200  -10.10500 18.05200  1.000 14.56314 ?  178 ARG   A C    1 
ATOM   1432 O O    . ARG   A 1 181 ? -2.25800  -9.41300  18.95200  1.000 14.19130 ?  178 ARG   A O    1 
ATOM   1433 C CB   . ARG   A 1 181 ? -1.98900  -12.49100 17.77100  1.000 21.68794 ?  178 ARG   A CB   1 
ATOM   1434 C CG   . ARG   A 1 181 ? -1.78500  -12.58800 19.27500  1.000 30.46865 ?  178 ARG   A CG   1 
ATOM   1435 C CD   . ARG   A 1 181 ? -1.96600  -14.01600 19.80400  1.000 45.59009 ?  178 ARG   A CD   1 
ATOM   1436 N NE   . ARG   A 1 181 ? -2.23000  -14.03000 21.24100  1.000 43.41572 ?  178 ARG   A NE   1 
ATOM   1437 C CZ   . ARG   A 1 181 ? -1.57000  -14.77700 22.11700  1.000 41.06413 ?  178 ARG   A CZ   1 
ATOM   1438 N NH1  . ARG   A 1 181 ? -0.59900  -15.59300 21.73700  1.000 41.36243 ?  178 ARG   A NH1  1 
ATOM   1439 N NH2  . ARG   A 1 181 ? -1.88500  -14.69900 23.40800  1.000 46.32421 ?  178 ARG   A NH2  1 
ATOM   1440 N N    . LYS   A 1 182 ? -4.03500  -10.07800 17.72800  1.000 14.77278 ?  179 LYS   A N    1 
ATOM   1441 C CA   . LYS   A 1 182 ? -4.99200  -9.37600  18.56600  1.000 12.94163 ?  179 LYS   A CA   1 
ATOM   1442 C C    . LYS   A 1 182 ? -4.99500  -10.01800 19.94600  1.000 18.00322 ?  179 LYS   A C    1 
ATOM   1443 O O    . LYS   A 1 182 ? -4.87700  -11.24200 20.07100  1.000 19.73841 ?  179 LYS   A O    1 
ATOM   1444 C CB   . LYS   A 1 182 ? -6.39900  -9.43300  17.94400  1.000 14.93950 ?  179 LYS   A CB   1 
ATOM   1445 C CG   . LYS   A 1 182 ? -6.57900  -8.60000  16.68900  1.000 14.04773 ?  179 LYS   A CG   1 
ATOM   1446 C CD   . LYS   A 1 182 ? -8.03400  -8.58800  16.15900  1.000 14.42160 ?  179 LYS   A CD   1 
ATOM   1447 C CE   . LYS   A 1 182 ? -8.16300  -7.60300  14.99700  1.000 21.82020 ?  179 LYS   A CE   1 
ATOM   1448 N NZ   . LYS   A 1 182 ? -9.57600  -7.44100  14.52600  1.000 20.39325 ?  179 LYS   A NZ   1 
ATOM   1449 N N    . ALA   A 1 183 ? -5.09400  -9.18700  20.98700  1.000 15.01626 ?  180 ALA   A N    1 
ATOM   1450 C CA   . ALA   A 1 183 ? -5.19100  -9.65900  22.36400  1.000 21.96383 ?  180 ALA   A CA   1 
ATOM   1451 C C    . ALA   A 1 183 ? -6.49000  -9.16300  22.98400  1.000 25.74530 ?  180 ALA   A C    1 
ATOM   1452 O O    . ALA   A 1 183 ? -6.82000  -7.97400  22.88400  1.000 25.64776 ?  180 ALA   A O    1 
ATOM   1453 C CB   . ALA   A 1 183 ? -4.00000  -9.19600  23.20200  1.000 19.80468 ?  180 ALA   A CB   1 
ATOM   1454 N N    . LEU   A 1 184 ? -7.21500  -10.06800 23.63400  1.000 34.96734 ?  181 LEU   A N    1 
ATOM   1455 C CA   . LEU   A 1 184 ? -8.50000  -9.75100  24.24400  1.000 37.89778 ?  181 LEU   A CA   1 
ATOM   1456 C C    . LEU   A 1 184 ? -8.42400  -9.86800  25.76100  1.000 43.02854 ?  181 LEU   A C    1 
ATOM   1457 O O    . LEU   A 1 184 ? -7.47300  -10.41200 26.32700  1.000 47.18210 ?  181 LEU   A O    1 
ATOM   1458 C CB   . LEU   A 1 184 ? -9.60500  -10.66300 23.69800  1.000 47.52545 ?  181 LEU   A CB   1 
ATOM   1459 C CG   . LEU   A 1 184 ? -11.04300 -10.24600 24.02800  1.000 59.32069 ?  181 LEU   A CG   1 
ATOM   1460 C CD1  . LEU   A 1 184 ? -11.29500 -8.77700  23.69500  1.000 47.71028 ?  181 LEU   A CD1  1 
ATOM   1461 C CD2  . LEU   A 1 184 ? -12.05100 -11.14700 23.31700  1.000 64.33036 ?  181 LEU   A CD2  1 
ATOM   1462 N N    . SER   A 1 185 ? -9.45000  -9.33400  26.41300  1.000 50.65361 ?  182 SER   A N    1 
ATOM   1463 C CA   . SER   A 1 185 ? -9.60300  -9.44000  27.85700  1.000 47.51727 ?  182 SER   A CA   1 
ATOM   1464 C C    . SER   A 1 185 ? -10.38400 -10.70200 28.20600  1.000 53.68292 ?  182 SER   A C    1 
ATOM   1465 O O    . SER   A 1 185 ? -11.19000 -11.18200 27.40400  1.000 59.27038 ?  182 SER   A O    1 
ATOM   1466 C CB   . SER   A 1 185 ? -10.31200 -8.20500  28.41100  1.000 51.12710 ?  182 SER   A CB   1 
ATOM   1467 O OG   . SER   A 1 185 ? -11.34500 -7.78500  27.53300  1.000 46.37741 ?  182 SER   A OG   1 
HETATM 1468 C C10  . A1H97 B 2 .   ? -19.66400 -7.44600  7.56200   0.713 28.68630 ?  201 A1H97 A C10  1 
HETATM 1469 C C13  . A1H97 B 2 .   ? -17.11300 -6.34400  8.88100   0.713 29.02481 ?  201 A1H97 A C13  1 
HETATM 1470 C C15  . A1H97 B 2 .   ? -16.19300 -4.88700  10.46900  0.713 35.01113 ?  201 A1H97 A C15  1 
HETATM 1471 C C05  . A1H97 B 2 .   ? -21.69900 -8.07300  8.54800   0.713 37.83358 ?  201 A1H97 A C05  1 
HETATM 1472 C C06  . A1H97 B 2 .   ? -21.16400 -7.58400  7.25200   0.713 29.10026 ?  201 A1H97 A C06  1 
HETATM 1473 C C07  . A1H97 B 2 .   ? -20.88800 -7.30200  9.59000   0.713 37.23878 ?  201 A1H97 A C07  1 
HETATM 1474 C C08  . A1H97 B 2 .   ? -21.63500 -9.58200  8.58900   0.713 37.17880 ?  201 A1H97 A C08  1 
HETATM 1475 C C09  . A1H97 B 2 .   ? -23.17900 -7.82500  8.77100   0.713 38.17603 ?  201 A1H97 A C09  1 
HETATM 1476 C C11  . A1H97 B 2 .   ? -22.97000 -10.02700 8.01100   0.713 37.42283 ?  201 A1H97 A C11  1 
HETATM 1477 C C12  . A1H97 B 2 .   ? -18.37800 -6.44300  9.58900   0.713 26.06763 ?  201 A1H97 A C12  1 
HETATM 1478 C C14  . A1H97 B 2 .   ? -17.39800 -4.96300  11.18500  0.713 34.25330 ?  201 A1H97 A C14  1 
HETATM 1479 N N02  . A1H97 B 2 .   ? -19.47000 -7.27100  9.04700   0.713 27.42888 ?  201 A1H97 A N02  1 
HETATM 1480 N N03  . A1H97 B 2 .   ? -18.43700 -5.71800  10.74400  0.713 37.14865 ?  201 A1H97 A N03  1 
HETATM 1481 N N04  . A1H97 B 2 .   ? -16.07700 -5.59800  9.32400   0.713 30.36161 ?  201 A1H97 A N04  1 
HETATM 1482 O O01  . A1H97 B 2 .   ? -23.84700 -8.91200  8.19700   0.713 45.24228 ?  201 A1H97 A O01  1 
HETATM 1483 H H102 . A1H97 B 2 .   ? -19.21200 -8.29900  7.03600   0.713 34.42356 ?  201 A1H97 A H102 1 
HETATM 1484 H H101 . A1H97 B 2 .   ? -19.38600 -6.54600  6.95700   0.713 34.42356 ?  201 A1H97 A H101 1 
HETATM 1485 H H131 . A1H97 B 2 .   ? -16.91900 -6.87700  7.92900   0.713 34.82977 ?  201 A1H97 A H131 1 
HETATM 1486 H H151 . A1H97 B 2 .   ? -15.31700 -4.28700  10.81300  0.713 42.01336 ?  201 A1H97 A H151 1 
HETATM 1487 H H061 . A1H97 B 2 .   ? -21.63100 -6.63600  6.90100   0.713 34.92031 ?  201 A1H97 A H061 1 
HETATM 1488 H H062 . A1H97 B 2 .   ? -21.32700 -8.33400  6.46000   0.713 34.92031 ?  201 A1H97 A H062 1 
HETATM 1489 H H072 . A1H97 B 2 .   ? -21.35500 -6.29000  9.66900   0.713 44.68653 ?  201 A1H97 A H072 1 
HETATM 1490 H H071 . A1H97 B 2 .   ? -21.16200 -7.82700  10.51600  0.713 44.68653 ?  201 A1H97 A H071 1 
HETATM 1491 H H082 . A1H97 B 2 .   ? -21.50500 -10.00700 9.58600   0.713 44.61456 ?  201 A1H97 A H082 1 
HETATM 1492 H H081 . A1H97 B 2 .   ? -20.86100 -9.97500  7.90400   0.713 44.61456 ?  201 A1H97 A H081 1 
HETATM 1493 H H092 . A1H97 B 2 .   ? -23.41300 -7.69300  9.84200   0.713 45.81123 ?  201 A1H97 A H092 1 
HETATM 1494 H H091 . A1H97 B 2 .   ? -23.40300 -6.85200  8.30900   0.713 45.81123 ?  201 A1H97 A H091 1 
HETATM 1495 H H112 . A1H97 B 2 .   ? -22.80800 -10.34300 6.96300   0.713 44.90740 ?  201 A1H97 A H112 1 
HETATM 1496 H H111 . A1H97 B 2 .   ? -23.27700 -10.95400 8.53200   0.713 44.90740 ?  201 A1H97 A H111 1 
HETATM 1497 H H141 . A1H97 B 2 .   ? -17.52500 -4.40200  12.13900  0.713 41.10396 ?  201 A1H97 A H141 1 
HETATM 1498 O O    . HOH   C 3 .   ? 7.18600   -18.00700 34.64200  1.000 33.80349 ?  301 HOH   A O    1 
HETATM 1499 O O    . HOH   C 3 .   ? -8.74200  -6.70100  7.11800   1.000 25.34213 ?  302 HOH   A O    1 
HETATM 1500 O O    . HOH   C 3 .   ? 7.94400   2.75000   13.36500  1.000 34.83303 ?  303 HOH   A O    1 
HETATM 1501 O O    . HOH   C 3 .   ? -15.51800 -4.33200  -3.26800  1.000 24.36586 ?  304 HOH   A O    1 
HETATM 1502 O O    . HOH   C 3 .   ? 13.22500  -16.82900 35.04500  1.000 26.96279 ?  305 HOH   A O    1 
HETATM 1503 O O    . HOH   C 3 .   ? -7.20800  2.35100   24.81100  1.000 21.07337 ?  306 HOH   A O    1 
HETATM 1504 O O    . HOH   C 3 .   ? -17.34100 -7.05800  -0.48300  1.000 32.28304 ?  307 HOH   A O    1 
HETATM 1505 O O    . HOH   C 3 .   ? -18.10700 -1.88200  17.41700  1.000 33.24420 ?  308 HOH   A O    1 
HETATM 1506 O O    . HOH   C 3 .   ? 11.62000  -8.53400  25.96900  1.000 27.43758 ?  309 HOH   A O    1 
HETATM 1507 O O    . HOH   C 3 .   ? -8.71200  0.76000   -9.57000  1.000 41.18306 ?  310 HOH   A O    1 
HETATM 1508 O O    . HOH   C 3 .   ? -3.54600  9.03100   6.06100   1.000 31.28271 ?  311 HOH   A O    1 
HETATM 1509 O O    . HOH   C 3 .   ? 3.16800   -15.96500 3.14500   1.000 18.35446 ?  312 HOH   A O    1 
HETATM 1510 O O    . HOH   C 3 .   ? -29.16300 -6.59800  8.66900   1.000 13.00711 ?  313 HOH   A O    1 
HETATM 1511 O O    . HOH   C 3 .   ? -1.12800  -4.29500  29.08800  1.000 23.89093 ?  314 HOH   A O    1 
HETATM 1512 O O    . HOH   C 3 .   ? 11.76800  -1.57900  28.83600  1.000 37.72360 ?  315 HOH   A O    1 
HETATM 1513 O O    . HOH   C 3 .   ? 8.84200   -18.12400 37.91400  1.000 28.80290 ?  316 HOH   A O    1 
HETATM 1514 O O    . HOH   C 3 .   ? -4.56500  4.24800   18.11400  1.000 17.30280 ?  317 HOH   A O    1 
HETATM 1515 O O    . HOH   C 3 .   ? -10.66600 -5.70800  -7.17500  1.000 29.39104 ?  318 HOH   A O    1 
HETATM 1516 O O    . HOH   C 3 .   ? -14.33800 -2.73000  -6.42800  1.000 26.95123 ?  319 HOH   A O    1 
HETATM 1517 O O    . HOH   C 3 .   ? -14.96000 17.03400  4.69400   1.000 34.11272 ?  320 HOH   A O    1 
HETATM 1518 O O    . HOH   C 3 .   ? -14.31200 -7.33700  -7.64800  1.000 14.84721 ?  321 HOH   A O    1 
HETATM 1519 O O    . HOH   C 3 .   ? -17.92600 8.93100   -8.99500  1.000 28.51000 ?  322 HOH   A O    1 
HETATM 1520 O O    . HOH   C 3 .   ? -32.791   -1.656    9.311     1.000 13.98275 ?  323 HOH   A O    1 
HETATM 1521 O O    . HOH   C 3 .   ? -8.46000  -6.46200  24.22200  1.000 24.84919 ?  324 HOH   A O    1 
HETATM 1522 O O    . HOH   C 3 .   ? -30.38600 11.03800  7.51400   1.000 23.35653 ?  325 HOH   A O    1 
HETATM 1523 O O    . HOH   C 3 .   ? -6.77600  10.00300  -0.70300  1.000 14.43770 ?  326 HOH   A O    1 
HETATM 1524 O O    . HOH   C 3 .   ? 13.50200  -1.85600  15.71900  1.000 34.46697 ?  327 HOH   A O    1 
HETATM 1525 O O    . HOH   C 3 .   ? -2.09800  -7.69000  29.85400  1.000 35.25592 ?  328 HOH   A O    1 
HETATM 1526 O O    . HOH   C 3 .   ? -5.76900  4.65500   11.37000  1.000 20.06444 ?  329 HOH   A O    1 
HETATM 1527 O O    . HOH   C 3 .   ? -25.44100 7.64400   7.41600   1.000 9.74303  ?  330 HOH   A O    1 
HETATM 1528 O O    . HOH   C 3 .   ? -10.56900 -5.47900  10.24700  1.000 32.68970 ?  331 HOH   A O    1 
HETATM 1529 O O    . HOH   C 3 .   ? -28.81800 3.59500   4.73700   1.000 7.39654  ?  332 HOH   A O    1 
HETATM 1530 O O    . HOH   C 3 .   ? -1.79300  1.97500   -1.06800  1.000 10.73104 ?  333 HOH   A O    1 
HETATM 1531 O O    . HOH   C 3 .   ? -10.53700 -0.85900  11.11700  1.000 8.46907  ?  334 HOH   A O    1 
HETATM 1532 O O    . HOH   C 3 .   ? 7.27600   -6.42900  35.23700  1.000 38.35882 ?  335 HOH   A O    1 
HETATM 1533 O O    . HOH   C 3 .   ? -24.77700 5.86300   13.85200  1.000 30.03046 ?  336 HOH   A O    1 
HETATM 1534 O O    . HOH   C 3 .   ? -9.83800  10.20500  14.04700  1.000 23.81237 ?  337 HOH   A O    1 
HETATM 1535 O O    . HOH   C 3 .   ? -1.40700  -3.02000  7.17400   1.000 9.37352  ?  338 HOH   A O    1 
HETATM 1536 O O    . HOH   C 3 .   ? 4.35600   7.45700   10.22400  1.000 26.80426 ?  339 HOH   A O    1 
HETATM 1537 O O    . HOH   C 3 .   ? 9.47700   -17.14000 32.21400  1.000 33.55369 ?  340 HOH   A O    1 
HETATM 1538 O O    . HOH   C 3 .   ? 8.36300   -9.90700  37.42700  1.000 22.03014 ?  341 HOH   A O    1 
HETATM 1539 O O    . HOH   C 3 .   ? -4.47800  -2.50100  28.20800  1.000 29.90910 ?  342 HOH   A O    1 
HETATM 1540 O O    . HOH   C 3 .   ? -14.08200 3.20100   13.54200  1.000 8.42221  ?  343 HOH   A O    1 
HETATM 1541 O O    . HOH   C 3 .   ? -10.31800 -3.81600  4.51100   1.000 19.21326 ?  344 HOH   A O    1 
HETATM 1542 O O    . HOH   C 3 .   ? -6.04900  9.57700   22.49000  1.000 24.47564 ?  345 HOH   A O    1 
HETATM 1543 O O    . HOH   C 3 .   ? -5.90600  3.69200   15.76900  1.000 15.77823 ?  346 HOH   A O    1 
HETATM 1544 O O    . HOH   C 3 .   ? 4.97800   -4.52600  8.68700   1.000 12.56342 ?  347 HOH   A O    1 
HETATM 1545 O O    . HOH   C 3 .   ? -0.46300  -8.76900  4.15000   1.000 11.42803 ?  348 HOH   A O    1 
HETATM 1546 O O    . HOH   C 3 .   ? -29.35800 10.32400  -1.58600  1.000 30.01928 ?  349 HOH   A O    1 
HETATM 1547 O O    . HOH   C 3 .   ? -1.40500  6.00400   5.09900   1.000 15.36615 ?  350 HOH   A O    1 
HETATM 1548 O O    . HOH   C 3 .   ? -33.30900 -6.99000  6.25600   1.000 10.21793 ?  351 HOH   A O    1 
HETATM 1549 O O    . HOH   C 3 .   ? -9.29400  -4.47300  16.24000  1.000 11.65356 ?  352 HOH   A O    1 
HETATM 1550 O O    . HOH   C 3 .   ? -33.46400 -4.37500  -1.83100  1.000 29.36928 ?  353 HOH   A O    1 
HETATM 1551 O O    . HOH   C 3 .   ? -11.31500 -9.03500  13.19600  1.000 35.79055 ?  354 HOH   A O    1 
HETATM 1552 O O    . HOH   C 3 .   ? 2.04300   2.91600   1.24200   1.000 24.85715 ?  355 HOH   A O    1 
HETATM 1553 O O    . HOH   C 3 .   ? -29.34500 11.73900  10.39600  1.000 35.72650 ?  356 HOH   A O    1 
HETATM 1554 O O    . HOH   C 3 .   ? 5.59000   -15.55000 19.22700  1.000 38.53739 ?  357 HOH   A O    1 
HETATM 1555 O O    . HOH   C 3 .   ? -7.61100  7.26600   -8.70500  1.000 19.55042 ?  358 HOH   A O    1 
HETATM 1556 O O    . HOH   C 3 .   ? -27.175   -10.549   3.799     1.000 17.31108 ?  359 HOH   A O    1 
HETATM 1557 O O    . HOH   C 3 .   ? -21.67800 -3.09000  -6.12200  1.000 34.78811 ?  360 HOH   A O    1 
HETATM 1558 O O    . HOH   C 3 .   ? 4.59800   -12.80100 33.21900  1.000 19.43185 ?  361 HOH   A O    1 
HETATM 1559 O O    . HOH   C 3 .   ? 7.01900   -11.17400 11.45000  1.000 13.54989 ?  362 HOH   A O    1 
HETATM 1560 O O    . HOH   C 3 .   ? -28.57400 12.36300  1.87500   1.000 15.95870 ?  363 HOH   A O    1 
HETATM 1561 O O    . HOH   C 3 .   ? 1.67500   7.69000   17.72400  1.000 17.08599 ?  364 HOH   A O    1 
HETATM 1562 O O    . HOH   C 3 .   ? 12.58600  -14.45200 43.52400  1.000 8.76653  ?  365 HOH   A O    1 
HETATM 1563 O O    . HOH   C 3 .   ? -11.46700 -2.53100  -6.61000  1.000 26.34444 ?  366 HOH   A O    1 
HETATM 1564 O O    . HOH   C 3 .   ? -9.27500  12.58200  -1.80600  1.000 20.53902 ?  367 HOH   A O    1 
HETATM 1565 O O    . HOH   C 3 .   ? -6.32000  -2.38300  4.83500   1.000 12.14149 ?  368 HOH   A O    1 
HETATM 1566 O O    . HOH   C 3 .   ? -34.12700 3.00800   3.97900   1.000 14.24182 ?  369 HOH   A O    1 
HETATM 1567 O O    . HOH   C 3 .   ? -32.947   8.859     1.221     1.000 39.65483 ?  370 HOH   A O    1 
HETATM 1568 O O    . HOH   C 3 .   ? -0.67900  -3.12100  26.80200  1.000 16.38029 ?  371 HOH   A O    1 
HETATM 1569 O O    . HOH   C 3 .   ? -29.94500 -4.45000  10.04000  1.000 10.42650 ?  372 HOH   A O    1 
HETATM 1570 O O    . HOH   C 3 .   ? -14.68000 7.71400   -6.98400  1.000 12.94191 ?  373 HOH   A O    1 
HETATM 1571 O O    . HOH   C 3 .   ? -36.76600 3.67500   7.48400   1.000 19.20458 ?  374 HOH   A O    1 
HETATM 1572 O O    . HOH   C 3 .   ? -26.324   4.830     14.043    1.000 35.75031 ?  375 HOH   A O    1 
HETATM 1573 O O    . HOH   C 3 .   ? -32.43200 4.75900   1.97100   1.000 15.81417 ?  376 HOH   A O    1 
HETATM 1574 O O    . HOH   C 3 .   ? -38.12400 1.20700   1.19400   1.000 11.38311 ?  377 HOH   A O    1 
HETATM 1575 O O    . HOH   C 3 .   ? 12.01500  -7.22000  36.05900  1.000 38.71111 ?  378 HOH   A O    1 
HETATM 1576 O O    . HOH   C 3 .   ? 2.00300   6.46700   25.63900  1.000 33.33924 ?  379 HOH   A O    1 
HETATM 1577 O O    . HOH   C 3 .   ? -4.67900  5.02000   9.05200   1.000 24.63964 ?  380 HOH   A O    1 
HETATM 1578 O O    . HOH   C 3 .   ? -6.33600  6.14700   -6.48500  1.000 17.91740 ?  381 HOH   A O    1 
HETATM 1579 O O    . HOH   C 3 .   ? -27.89500 2.29700   -6.57200  1.000 40.54723 ?  382 HOH   A O    1 
HETATM 1580 O O    . HOH   C 3 .   ? -15.38000 -6.90700  18.86900  1.000 36.77646 ?  383 HOH   A O    1 
HETATM 1581 O O    . HOH   C 3 .   ? -20.35000 10.94200  -6.65100  1.000 19.23373 ?  384 HOH   A O    1 
HETATM 1582 O O    . HOH   C 3 .   ? -28.64500 0.10100   -1.85100  1.000 13.33359 ?  385 HOH   A O    1 
HETATM 1583 O O    . HOH   C 3 .   ? -18.29300 5.61200   15.26600  1.000 14.10114 ?  386 HOH   A O    1 
HETATM 1584 O O    . HOH   C 3 .   ? -27.81600 15.40200  12.53600  1.000 40.82347 ?  387 HOH   A O    1 
HETATM 1585 O O    . HOH   C 3 .   ? -3.50600  7.30600   12.01100  1.000 30.02482 ?  388 HOH   A O    1 
HETATM 1586 O O    . HOH   C 3 .   ? 3.03100   1.97800   29.18900  1.000 27.72860 ?  389 HOH   A O    1 
HETATM 1587 O O    . HOH   C 3 .   ? -3.05600  7.72200   3.72400   1.000 13.16963 ?  390 HOH   A O    1 
HETATM 1588 O O    . HOH   C 3 .   ? 3.62700   -6.92800  33.77300  1.000 37.16803 ?  391 HOH   A O    1 
HETATM 1589 O O    . HOH   C 3 .   ? -7.31900  11.85600  6.25600   1.000 15.21278 ?  392 HOH   A O    1 
HETATM 1590 O O    . HOH   C 3 .   ? -37.38700 -12.29700 -1.30700  1.000 31.40663 ?  393 HOH   A O    1 
HETATM 1591 O O    . HOH   C 3 .   ? -38.03800 -5.28300  -3.53700  1.000 26.62620 ?  394 HOH   A O    1 
HETATM 1592 O O    . HOH   C 3 .   ? 11.60600  -13.85900 17.03000  1.000 27.53841 ?  395 HOH   A O    1 
HETATM 1593 O O    . HOH   C 3 .   ? 6.56800   -2.94400  30.70800  1.000 28.96031 ?  396 HOH   A O    1 
HETATM 1594 O O    . HOH   C 3 .   ? -29.77800 8.69500   -4.10300  1.000 36.13406 ?  397 HOH   A O    1 
HETATM 1595 O O    . HOH   C 3 .   ? -22.10200 3.99100   -5.55100  1.000 21.85510 ?  398 HOH   A O    1 
HETATM 1596 O O    . HOH   C 3 .   ? 5.98200   -12.95700 9.86800   1.000 17.35722 ?  399 HOH   A O    1 
HETATM 1597 O O    . HOH   C 3 .   ? 4.55100   7.06900   21.04800  1.000 20.72356 ?  400 HOH   A O    1 
HETATM 1598 O O    . HOH   C 3 .   ? -24.70900 10.43500  15.36800  1.000 16.30144 ?  401 HOH   A O    1 
HETATM 1599 O O    . HOH   C 3 .   ? -27.04700 -2.15300  11.13900  1.000 14.73824 ?  402 HOH   A O    1 
HETATM 1600 O O    . HOH   C 3 .   ? 14.78800  -10.75800 11.57400  1.000 39.18973 ?  403 HOH   A O    1 
HETATM 1601 O O    . HOH   C 3 .   ? -9.57800  7.22500   20.96700  1.000 14.32541 ?  404 HOH   A O    1 
HETATM 1602 O O    . HOH   C 3 .   ? -20.29300 13.43100  -5.44200  1.000 22.55437 ?  405 HOH   A O    1 
HETATM 1603 O O    . HOH   C 3 .   ? -27.89300 2.00900   11.54900  1.000 11.24498 ?  406 HOH   A O    1 
HETATM 1604 O O    . HOH   C 3 .   ? -34.60700 -7.70000  -4.15100  1.000 29.23033 ?  407 HOH   A O    1 
HETATM 1605 O O    . HOH   C 3 .   ? 11.94600  0.44600   16.77800  1.000 25.05420 ?  408 HOH   A O    1 
HETATM 1606 O O    . HOH   C 3 .   ? -29.20700 3.26900   -2.17100  1.000 17.89350 ?  409 HOH   A O    1 
HETATM 1607 O O    . HOH   C 3 .   ? 1.58400   8.55000   -1.51900  1.000 26.80718 ?  410 HOH   A O    1 
HETATM 1608 O O    . HOH   C 3 .   ? -41.50300 -2.09000  5.46700   1.000 13.07576 ?  411 HOH   A O    1 
HETATM 1609 O O    . HOH   C 3 .   ? -9.00900  -3.82900  23.58300  1.000 21.24680 ?  412 HOH   A O    1 
HETATM 1610 O O    . HOH   C 3 .   ? 4.28200   -13.09100 -0.18800  1.000 18.56834 ?  413 HOH   A O    1 
HETATM 1611 O O    . HOH   C 3 .   ? 9.76800   -9.66100  27.59800  1.000 16.23765 ?  414 HOH   A O    1 
HETATM 1612 O O    . HOH   C 3 .   ? 0.72000   -9.36200  11.70400  1.000 17.36473 ?  415 HOH   A O    1 
HETATM 1613 O O    . HOH   C 3 .   ? -0.05900  3.21000   9.91100   1.000 16.34776 ?  416 HOH   A O    1 
HETATM 1614 O O    . HOH   C 3 .   ? -22.12600 4.56900   14.45900  1.000 34.67847 ?  417 HOH   A O    1 
HETATM 1615 O O    . HOH   C 3 .   ? 1.92000   6.90400   20.44700  1.000 18.97891 ?  418 HOH   A O    1 
HETATM 1616 O O    . HOH   C 3 .   ? 0.05300   -10.05200 40.21400  1.000 38.79960 ?  419 HOH   A O    1 
HETATM 1617 O O    . HOH   C 3 .   ? 3.87100   6.45600   0.72400   1.000 37.89609 ?  420 HOH   A O    1 
HETATM 1618 O O    . HOH   C 3 .   ? 12.78300  2.32300   26.53800  1.000 34.62452 ?  421 HOH   A O    1 
HETATM 1619 O O    . HOH   C 3 .   ? -0.58300  2.34300   3.55000   1.000 14.50335 ?  422 HOH   A O    1 
HETATM 1620 O O    . HOH   C 3 .   ? 10.89400  -14.18600 22.47600  1.000 29.78219 ?  423 HOH   A O    1 
HETATM 1621 O O    . HOH   C 3 .   ? -17.73100 13.97700  8.84100   1.000 23.25821 ?  424 HOH   A O    1 
HETATM 1622 O O    . HOH   C 3 .   ? -22.50300 1.78300   14.84200  1.000 31.87213 ?  425 HOH   A O    1 
HETATM 1623 O O    . HOH   C 3 .   ? 14.43400  -9.19500  39.02500  1.000 32.11191 ?  426 HOH   A O    1 
HETATM 1624 O O    . HOH   C 3 .   ? 19.26100  -4.34000  20.72300  1.000 32.94092 ?  427 HOH   A O    1 
HETATM 1625 O O    . HOH   C 3 .   ? 11.20800  -18.85200 35.49500  1.000 38.77573 ?  428 HOH   A O    1 
HETATM 1626 O O    . HOH   C 3 .   ? -14.52600 4.39200   -9.72800  1.000 38.25499 ?  429 HOH   A O    1 
HETATM 1627 O O    . HOH   C 3 .   ? 2.79100   -14.10300 7.95800   1.000 27.40712 ?  430 HOH   A O    1 
HETATM 1628 O O    . HOH   C 3 .   ? -11.06500 14.22800  12.11300  1.000 38.78339 ?  431 HOH   A O    1 
HETATM 1629 O O    . HOH   C 3 .   ? 0.22000   7.10400   14.07700  1.000 27.55569 ?  432 HOH   A O    1 
HETATM 1630 O O    . HOH   C 3 .   ? -7.11200  6.72100   12.35000  1.000 20.54531 ?  433 HOH   A O    1 
HETATM 1631 O O    . HOH   C 3 .   ? -15.30000 -8.83700  -4.60600  1.000 17.56319 ?  434 HOH   A O    1 
HETATM 1632 O O    . HOH   C 3 .   ? -4.88200  -11.76300 15.48700  1.000 19.21539 ?  435 HOH   A O    1 
HETATM 1633 O O    . HOH   C 3 .   ? -14.41600 14.87200  11.70500  1.000 31.57498 ?  436 HOH   A O    1 
HETATM 1634 O O    . HOH   C 3 .   ? -9.81400  15.09900  5.90100   1.000 26.64436 ?  437 HOH   A O    1 
HETATM 1635 O O    . HOH   C 3 .   ? 14.09000  -13.02800 14.31200  1.000 28.34144 ?  438 HOH   A O    1 
HETATM 1636 O O    . HOH   C 3 .   ? -10.87000 10.44200  -6.52000  1.000 17.42564 ?  439 HOH   A O    1 
HETATM 1637 O O    . HOH   C 3 .   ? -36.704   6.356     4.377     1.000 30.24360 ?  440 HOH   A O    1 
HETATM 1638 O O    . HOH   C 3 .   ? -13.16300 -11.85700 29.51400  1.000 45.71710 ?  441 HOH   A O    1 
HETATM 1639 O O    . HOH   C 3 .   ? -22.52200 9.68200   -5.71700  1.000 16.48021 ?  442 HOH   A O    1 
HETATM 1640 O O    . HOH   C 3 .   ? 8.44400   -17.76300 30.04800  1.000 34.98509 ?  443 HOH   A O    1 
HETATM 1641 O O    . HOH   C 3 .   ? -7.63500  -6.22300  9.86600   1.000 29.94467 ?  444 HOH   A O    1 
HETATM 1642 O O    . HOH   C 3 .   ? -4.59200  4.69300   13.67300  1.000 23.85680 ?  445 HOH   A O    1 
HETATM 1643 O O    . HOH   C 3 .   ? -11.61500 1.49400   19.14600  1.000 16.72827 ?  446 HOH   A O    1 
HETATM 1644 O O    . HOH   C 3 .   ? -6.28800  -12.95500 23.67000  1.000 39.93761 ?  447 HOH   A O    1 
HETATM 1645 O O    . HOH   C 3 .   ? 3.25700   -12.43300 42.38700  1.000 20.26212 ?  448 HOH   A O    1 
HETATM 1646 O O    . HOH   C 3 .   ? -28.67700 -5.09800  -0.40600  1.000 20.69529 ?  449 HOH   A O    1 
HETATM 1647 O O    . HOH   C 3 .   ? -29.81300 10.43800  0.76300   1.000 26.26310 ?  450 HOH   A O    1 
HETATM 1648 O O    . HOH   C 3 .   ? 2.03500   5.96900   9.27000   1.000 33.65195 ?  451 HOH   A O    1 
HETATM 1649 O O    . HOH   C 3 .   ? 16.85400  -12.85200 37.66400  1.000 28.34678 ?  452 HOH   A O    1 
HETATM 1650 O O    . HOH   C 3 .   ? -1.97100  6.48300   7.83500   1.000 27.54335 ?  453 HOH   A O    1 
HETATM 1651 O O    . HOH   C 3 .   ? 10.63000  2.39500   14.25300  1.000 26.42817 ?  454 HOH   A O    1 
HETATM 1652 O O    . HOH   C 3 .   ? -1.38200  6.00900   12.01900  1.000 23.56783 ?  455 HOH   A O    1 
HETATM 1653 O O    . HOH   C 3 .   ? -8.41600  -8.79000  5.62300   1.000 27.63127 ?  456 HOH   A O    1 
HETATM 1654 O O    . HOH   C 3 .   ? -4.60700  -9.56400  27.22600  1.000 42.24900 ?  457 HOH   A O    1 
HETATM 1655 O O    . HOH   C 3 .   ? -5.941    11.175    12.383    1.000 28.67167 ?  458 HOH   A O    1 
HETATM 1656 O O    . HOH   C 3 .   ? -3.55700  -10.21200 5.19000   1.000 38.22135 ?  459 HOH   A O    1 
HETATM 1657 O O    . HOH   C 3 .   ? -31.14100 -5.97200  -1.37500  1.000 26.06271 ?  460 HOH   A O    1 
HETATM 1658 O O    . HOH   C 3 .   ? 12.614    -15.246   11.198    1.000 39.74220 ?  461 HOH   A O    1 
HETATM 1659 O O    . HOH   C 3 .   ? 4.77300   -9.28500  33.63200  1.000 26.22334 ?  462 HOH   A O    1 
HETATM 1660 O O    . HOH   C 3 .   ? 1.64700   7.90000   2.45700   1.000 40.74974 ?  463 HOH   A O    1 
HETATM 1661 O O    . HOH   C 3 .   ? -35.14600 -5.16300  -4.02600  1.000 34.57161 ?  464 HOH   A O    1 
HETATM 1662 O O    . HOH   C 3 .   ? -15.29600 13.35300  8.20800   1.000 24.03481 ?  465 HOH   A O    1 
HETATM 1663 O O    . HOH   C 3 .   ? -40.902   -11.414   -2.739    1.000 36.23190 ?  466 HOH   A O    1 
HETATM 1664 O O    . HOH   C 3 .   ? -23.97100 5.38300   -6.59200  1.000 31.82229 ?  467 HOH   A O    1 
HETATM 1665 O O    . HOH   C 3 .   ? -3.95300  8.82900   26.71200  1.000 32.28295 ?  468 HOH   A O    1 
HETATM 1666 O O    . HOH   C 3 .   ? -26.024   16.832    11.775    1.000 40.93049 ?  469 HOH   A O    1 
HETATM 1667 O O    . HOH   C 3 .   ? -4.70700  11.18200  6.49500   1.000 21.78559 ?  470 HOH   A O    1 
HETATM 1668 O O    . HOH   C 3 .   ? 13.80300  1.85400   17.62100  1.000 30.27152 ?  471 HOH   A O    1 
HETATM 1669 O O    . HOH   C 3 .   ? 10.872    -18.898   38.311    1.000 33.04140 ?  472 HOH   A O    1 
HETATM 1670 O O    . HOH   C 3 .   ? -36.54600 3.77800   5.01800   1.000 19.01389 ?  473 HOH   A O    1 
HETATM 1671 O O    . HOH   C 3 .   ? -7.81200  -6.28700  26.74500  1.000 42.32601 ?  474 HOH   A O    1 
HETATM 1672 O O    . HOH   C 3 .   ? -7.69300  13.74100  8.37200   1.000 28.76986 ?  475 HOH   A O    1 
HETATM 1673 O O    . HOH   C 3 .   ? -7.66100  14.00900  4.90500   1.000 29.91221 ?  476 HOH   A O    1 
HETATM 1674 O O    . HOH   C 3 .   ? -2.59900  8.10800   15.56800  1.000 37.81581 ?  477 HOH   A O    1 
HETATM 1675 O O    . HOH   C 3 .   ? -3.20300  -12.14100 13.58700  1.000 37.86601 ?  478 HOH   A O    1 
HETATM 1676 O O    . HOH   C 3 .   ? 17.37800  -2.92900  14.24800  1.000 35.13944 ?  479 HOH   A O    1 
HETATM 1677 O O    . HOH   C 3 .   ? 0.174     -14.839   41.626    1.000 32.89964 ?  480 HOH   A O    1 
HETATM 1678 O O    . HOH   C 3 .   ? -2.580    11.655    25.650    1.000 37.19625 ?  481 HOH   A O    1 
HETATM 1679 O O    . HOH   C 3 .   ? 11.840    -17.756   40.472    1.000 17.46622 ?  482 HOH   A O    1 
HETATM 1680 O O    . HOH   C 3 .   ? -0.49400  6.74100   9.88900   1.000 32.38376 ?  483 HOH   A O    1 
HETATM 1681 O O    . HOH   C 3 .   ? 7.50300   -15.57400 17.71600  1.000 36.43564 ?  484 HOH   A O    1 
HETATM 1682 O O    . HOH   C 3 .   ? -8.09500  -4.34000  5.61900   1.000 14.93666 ?  485 HOH   A O    1 
HETATM 1683 O O    . HOH   C 3 .   ? -14.69400 6.70800   -9.54800  1.000 32.03835 ?  486 HOH   A O    1 
HETATM 1684 O O    . HOH   C 3 .   ? -8.06600  0.22500   26.52800  1.000 32.62278 ?  487 HOH   A O    1 
HETATM 1685 O O    . HOH   C 3 .   ? -7.231    12.414    0.023     1.000 27.60635 ?  488 HOH   A O    1 
HETATM 1686 O O    . HOH   C 3 .   ? 3.74400   9.27900   17.06000  1.000 28.50964 ?  489 HOH   A O    1 
HETATM 1687 O O    . HOH   C 3 .   ? -7.336    -9.772    -5.084    1.000 26.09532 ?  490 HOH   A O    1 
HETATM 1688 O O    . HOH   C 3 .   ? -0.93800  3.85100   -2.98600  1.000 24.18564 ?  491 HOH   A O    1 
HETATM 1689 O O    . HOH   C 3 .   ? -21.91100 7.33400   17.46100  1.000 35.99209 ?  492 HOH   A O    1 
HETATM 1690 O O    . HOH   C 3 .   ? -5.42800  4.17400   -8.26200  1.000 25.44418 ?  493 HOH   A O    1 
HETATM 1691 O O    . HOH   C 3 .   ? -12.46600 17.26900  4.83700   1.000 33.90999 ?  494 HOH   A O    1 
HETATM 1692 O O    . HOH   C 3 .   ? -20.61600 5.50500   16.60200  1.000 34.35804 ?  495 HOH   A O    1 
HETATM 1693 O O    . HOH   C 3 .   ? 0.709     -10.099   34.269    1.000 38.03745 ?  496 HOH   A O    1 
HETATM 1694 O O    . HOH   C 3 .   ? 5.149     -9.836    39.762    1.000 40.32396 ?  497 HOH   A O    1 
HETATM 1695 O O    . HOH   C 3 .   ? -4.581    -9.751    -5.145    1.000 34.56963 ?  498 HOH   A O    1 
HETATM 1696 O O    . HOH   C 3 .   ? 9.60800   -7.73600  38.43000  1.000 29.70109 ?  499 HOH   A O    1 
HETATM 1697 O O    . HOH   C 3 .   ? -0.13600  9.46400   17.22700  1.000 38.72104 ?  500 HOH   A O    1 
HETATM 1698 O O    . HOH   C 3 .   ? -7.55900  -2.83000  25.25800  1.000 34.26067 ?  501 HOH   A O    1 
HETATM 1699 O O    . HOH   C 3 .   ? -3.091    9.960     2.228     1.000 17.18264 ?  502 HOH   A O    1 
HETATM 1700 O O    . HOH   C 3 .   ? -23.31300 7.86100   -7.44900  1.000 22.64755 ?  503 HOH   A O    1 
HETATM 1701 O O    . HOH   C 3 .   ? -33.74300 -10.15800 -3.77300  1.000 27.93759 ?  504 HOH   A O    1 
HETATM 1702 O O    . HOH   C 3 .   ? -3.03400  -3.09000  30.53800  1.000 39.72803 ?  505 HOH   A O    1 
HETATM 1703 O O    . HOH   C 3 .   ? -6.82200  -10.83900 13.87300  1.000 32.91690 ?  506 HOH   A O    1 
HETATM 1704 O O    . HOH   C 3 .   ? -13.06300 -0.30500  20.00500  1.000 40.03719 ?  507 HOH   A O    1 
HETATM 1705 O O    . HOH   C 3 .   ? -28.056   16.806    9.939     1.000 35.76986 ?  508 HOH   A O    1 
HETATM 1706 O O    . HOH   C 3 .   ? -3.54100  6.47000   -5.88300  1.000 28.51950 ?  509 HOH   A O    1 
HETATM 1707 O O    . HOH   C 3 .   ? -9.78600  3.07200   -9.78300  1.000 34.34223 ?  510 HOH   A O    1 
HETATM 1708 O O    . HOH   C 3 .   ? 4.19000   8.17600   -1.31400  1.000 35.32548 ?  511 HOH   A O    1 
HETATM 1709 O O    . HOH   C 3 .   ? -6.846    12.729    2.474     1.000 25.02776 ?  512 HOH   A O    1 
HETATM 1710 O O    . HOH   C 3 .   ? 6.47200   -5.81600  37.72200  1.000 35.72002 ?  513 HOH   A O    1 
HETATM 1711 O O    . HOH   C 3 .   ? 2.73200   11.28000  22.40200  1.000 47.00457 ?  514 HOH   A O    1 
HETATM 1712 O O    . HOH   C 3 .   ? 18.56200  -10.89700 37.90000  1.000 43.06554 ?  515 HOH   A O    1 
HETATM 1713 O O    . HOH   C 3 .   ? -15.05800 15.73400  7.18900   1.000 39.29237 ?  516 HOH   A O    1 
HETATM 1714 O O    . HOH   C 3 .   ? -19.167   14.405    14.379    1.000 42.65121 ?  517 HOH   A O    1 
HETATM 1715 O O    . HOH   C 3 .   ? -6.60700  0.09400   28.71200  1.000 34.61433 ?  518 HOH   A O    1 
# 
