data_8PQ8
# 
_entry.id   8PQ8 
# 
_audit_conform.dict_name       mmcif_pdbx.dic 
_audit_conform.dict_version    5.402 
_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   8PQ8         pdb_00008pq8 10.2210/pdb8pq8/pdb 
WWPDB D_1292131753 ?            ?                   
EMDB  EMD-17821    ?            ?                   
# 
loop_
_pdbx_audit_revision_history.ordinal 
_pdbx_audit_revision_history.data_content_type 
_pdbx_audit_revision_history.major_revision 
_pdbx_audit_revision_history.minor_revision 
_pdbx_audit_revision_history.revision_date 
_pdbx_audit_revision_history.part_number 
1  'Structure model' 1 0 2025-02-12 ? 
2  'EM metadata'     1 0 2025-02-12 ? 
3  FSC               1 0 2025-02-12 ? 
4  'Half map'        1 0 2025-02-12 1 
5  'Half map'        1 0 2025-02-12 2 
6  Image             1 0 2025-02-12 ? 
7  Mask              1 0 2025-02-12 ? 
8  'Primary map'     1 0 2025-02-12 ? 
9  'Structure model' 1 1 2025-03-05 ? 
10 'EM metadata'     1 1 2025-03-05 ? 
# 
loop_
_pdbx_audit_revision_details.ordinal 
_pdbx_audit_revision_details.revision_ordinal 
_pdbx_audit_revision_details.data_content_type 
_pdbx_audit_revision_details.provider 
_pdbx_audit_revision_details.type 
_pdbx_audit_revision_details.description 
_pdbx_audit_revision_details.details 
1 1 'Structure model' repository 'Initial release' ? ? 
2 2 'EM metadata'     repository 'Initial release' ? ? 
3 3 FSC               repository 'Initial release' ? ? 
4 4 'Half map'        repository 'Initial release' ? ? 
5 5 'Half map'        repository 'Initial release' ? ? 
6 6 Image             repository 'Initial release' ? ? 
7 7 Mask              repository 'Initial release' ? ? 
8 8 'Primary map'     repository 'Initial release' ? ? 
# 
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 9  'Structure model' 'Data collection'      
2 9  'Structure model' 'Database references'  
3 10 'EM metadata'     'Database references'  
4 10 'EM metadata'     'Experimental summary' 
# 
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 9  'Structure model' citation        
2 9  'Structure model' citation_author 
3 9  'Structure model' em_admin        
4 10 'EM metadata'     citation        
5 10 'EM metadata'     citation_author 
6 10 'EM metadata'     em_admin        
# 
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  9  'Structure model' '_citation.country'                 
2  9  'Structure model' '_citation.journal_abbrev'          
3  9  'Structure model' '_citation.journal_id_CSD'          
4  9  'Structure model' '_citation.journal_id_ISSN'         
5  9  'Structure model' '_citation.journal_volume'          
6  9  'Structure model' '_citation.page_first'              
7  9  'Structure model' '_citation.page_last'               
8  9  'Structure model' '_citation.pdbx_database_id_DOI'    
9  9  'Structure model' '_citation.pdbx_database_id_PubMed' 
10 9  'Structure model' '_citation.title'                   
11 9  'Structure model' '_citation.year'                    
12 9  'Structure model' '_em_admin.last_update'             
13 10 'EM metadata'     '_citation.country'                 
14 10 'EM metadata'     '_citation.journal_abbrev'          
15 10 'EM metadata'     '_citation.journal_id_CSD'          
16 10 'EM metadata'     '_citation.journal_id_ISSN'         
17 10 'EM metadata'     '_citation.journal_volume'          
18 10 'EM metadata'     '_citation.page_first'              
19 10 'EM metadata'     '_citation.page_last'               
20 10 'EM metadata'     '_citation.pdbx_database_id_DOI'    
21 10 'EM metadata'     '_citation.pdbx_database_id_PubMed' 
22 10 'EM metadata'     '_citation.title'                   
23 10 'EM metadata'     '_citation.year'                    
24 10 'EM metadata'     '_em_admin.last_update'             
# 
_pdbx_database_status.status_code                     REL 
_pdbx_database_status.status_code_sf                  ? 
_pdbx_database_status.status_code_mr                  ? 
_pdbx_database_status.entry_id                        8PQ8 
_pdbx_database_status.recvd_initial_deposition_date   2023-07-10 
_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           Y 
# 
_pdbx_database_related.db_name        EMDB 
_pdbx_database_related.details        'Sak Single Strand Annealing Protein from Staphylococcal Bacteriophage 80a - dCTD' 
_pdbx_database_related.db_id          EMD-17821 
_pdbx_database_related.content_type   'associated EM volume' 
# 
_pdbx_contact_author.id                 2 
_pdbx_contact_author.email              ignacio.mir-sanchis@umu.se 
_pdbx_contact_author.name_first         Ignacio 
_pdbx_contact_author.name_last          Mir-Sanchis 
_pdbx_contact_author.name_mi            ? 
_pdbx_contact_author.role               'principal investigator/group leader' 
_pdbx_contact_author.identifier_ORCID   0000-0002-6536-0045 
# 
loop_
_audit_author.name 
_audit_author.pdbx_ordinal 
_audit_author.identifier_ORCID 
'Debiasi-Anders, G.' 1 0000-0003-0545-6579 
'Mir-Sanchis, I.'    2 0000-0002-6536-0045 
# 
_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                   UK 
_citation.database_id_Medline       ? 
_citation.details                   ? 
_citation.id                        primary 
_citation.journal_abbrev            'Nat Commun' 
_citation.journal_id_ASTM           ? 
_citation.journal_id_CSD            ? 
_citation.journal_id_ISSN           2041-1723 
_citation.journal_full              ? 
_citation.journal_issue             ? 
_citation.journal_volume            16 
_citation.language                  ? 
_citation.page_first                1889 
_citation.page_last                 1889 
_citation.title                     'Phage parasites targeting phage homologous recombinases provide antiviral immunity.' 
_citation.year                      2025 
_citation.database_id_CSD           ? 
_citation.pdbx_database_id_DOI      10.1038/s41467-025-57156-3 
_citation.pdbx_database_id_PubMed   39987160 
_citation.pdbx_database_id_patent   ? 
_citation.unpublished_flag          ? 
# 
loop_
_citation_author.citation_id 
_citation_author.name 
_citation_author.ordinal 
_citation_author.identifier_ORCID 
primary 'Debiasi-Anders, G.' 1 0000-0003-0545-6579 
primary 'Qiao, C.'           2 0000-0002-2642-3672 
primary 'Salim, A.'          3 ?                   
primary 'Li, N.'             4 ?                   
primary 'Mir-Sanchis, I.'    5 0000-0002-6536-0045 
# 
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 Topoisomerase 19417.621 1 ? 'Truncation of CTD at N142' ? ? 
2 water   nat water         18.015    9 ? ?                           ? ? 
# 
_entity_name_com.entity_id   1 
_entity_name_com.name        'Sak Single-Strand Annealing Protein' 
# 
_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       
;MKHHHHHHPMSDYDIPTTENLYFQGAMGMTEQTLFEQLNSKNVNDHTEQKNGLTYLAWSYAHQELKKIDPNYTVKVHEFP
HPDINTENYFVPYLATPEGYFVQVSVTVKDSTETEWLPVLDFRNKSLAKGSATTFDINKAQKRCFVKASALHGLGLYIYN
GEELPSASD
;
_entity_poly.pdbx_seq_one_letter_code_can   
;MKHHHHHHPMSDYDIPTTENLYFQGAMGMTEQTLFEQLNSKNVNDHTEQKNGLTYLAWSYAHQELKKIDPNYTVKVHEFP
HPDINTENYFVPYLATPEGYFVQVSVTVKDSTETEWLPVLDFRNKSLAKGSATTFDINKAQKRCFVKASALHGLGLYIYN
GEELPSASD
;
_entity_poly.pdbx_strand_id                 A 
_entity_poly.pdbx_target_identifier         ? 
# 
_pdbx_entity_nonpoly.entity_id   2 
_pdbx_entity_nonpoly.name        water 
_pdbx_entity_nonpoly.comp_id     HOH 
# 
loop_
_entity_poly_seq.entity_id 
_entity_poly_seq.num 
_entity_poly_seq.mon_id 
_entity_poly_seq.hetero 
1 1   MET n 
1 2   LYS n 
1 3   HIS n 
1 4   HIS n 
1 5   HIS n 
1 6   HIS n 
1 7   HIS n 
1 8   HIS n 
1 9   PRO n 
1 10  MET n 
1 11  SER n 
1 12  ASP n 
1 13  TYR n 
1 14  ASP n 
1 15  ILE n 
1 16  PRO n 
1 17  THR n 
1 18  THR n 
1 19  GLU n 
1 20  ASN n 
1 21  LEU n 
1 22  TYR n 
1 23  PHE n 
1 24  GLN n 
1 25  GLY n 
1 26  ALA n 
1 27  MET n 
1 28  GLY n 
1 29  MET n 
1 30  THR n 
1 31  GLU n 
1 32  GLN n 
1 33  THR n 
1 34  LEU n 
1 35  PHE n 
1 36  GLU n 
1 37  GLN n 
1 38  LEU n 
1 39  ASN n 
1 40  SER n 
1 41  LYS n 
1 42  ASN n 
1 43  VAL n 
1 44  ASN n 
1 45  ASP n 
1 46  HIS n 
1 47  THR n 
1 48  GLU n 
1 49  GLN n 
1 50  LYS n 
1 51  ASN n 
1 52  GLY n 
1 53  LEU n 
1 54  THR n 
1 55  TYR n 
1 56  LEU n 
1 57  ALA n 
1 58  TRP n 
1 59  SER n 
1 60  TYR n 
1 61  ALA n 
1 62  HIS n 
1 63  GLN n 
1 64  GLU n 
1 65  LEU n 
1 66  LYS n 
1 67  LYS n 
1 68  ILE n 
1 69  ASP n 
1 70  PRO n 
1 71  ASN n 
1 72  TYR n 
1 73  THR n 
1 74  VAL n 
1 75  LYS n 
1 76  VAL n 
1 77  HIS n 
1 78  GLU n 
1 79  PHE n 
1 80  PRO n 
1 81  HIS n 
1 82  PRO n 
1 83  ASP n 
1 84  ILE n 
1 85  ASN n 
1 86  THR n 
1 87  GLU n 
1 88  ASN n 
1 89  TYR n 
1 90  PHE n 
1 91  VAL n 
1 92  PRO n 
1 93  TYR n 
1 94  LEU n 
1 95  ALA n 
1 96  THR n 
1 97  PRO n 
1 98  GLU n 
1 99  GLY n 
1 100 TYR n 
1 101 PHE n 
1 102 VAL n 
1 103 GLN n 
1 104 VAL n 
1 105 SER n 
1 106 VAL n 
1 107 THR n 
1 108 VAL n 
1 109 LYS n 
1 110 ASP n 
1 111 SER n 
1 112 THR n 
1 113 GLU n 
1 114 THR n 
1 115 GLU n 
1 116 TRP n 
1 117 LEU n 
1 118 PRO n 
1 119 VAL n 
1 120 LEU n 
1 121 ASP n 
1 122 PHE n 
1 123 ARG n 
1 124 ASN n 
1 125 LYS n 
1 126 SER n 
1 127 LEU n 
1 128 ALA n 
1 129 LYS n 
1 130 GLY n 
1 131 SER n 
1 132 ALA n 
1 133 THR n 
1 134 THR n 
1 135 PHE n 
1 136 ASP n 
1 137 ILE n 
1 138 ASN n 
1 139 LYS n 
1 140 ALA n 
1 141 GLN n 
1 142 LYS n 
1 143 ARG n 
1 144 CYS n 
1 145 PHE n 
1 146 VAL n 
1 147 LYS n 
1 148 ALA n 
1 149 SER n 
1 150 ALA n 
1 151 LEU n 
1 152 HIS n 
1 153 GLY n 
1 154 LEU n 
1 155 GLY n 
1 156 LEU n 
1 157 TYR n 
1 158 ILE n 
1 159 TYR n 
1 160 ASN n 
1 161 GLY n 
1 162 GLU n 
1 163 GLU n 
1 164 LEU n 
1 165 PRO n 
1 166 SER n 
1 167 ALA n 
1 168 SER n 
1 169 ASP 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                   169 
_entity_src_gen.gene_src_common_name               ? 
_entity_src_gen.gene_src_genus                     ? 
_entity_src_gen.pdbx_gene_src_gene                 ? 
_entity_src_gen.gene_src_species                   ? 
_entity_src_gen.gene_src_strain                    ? 
_entity_src_gen.gene_src_tissue                    ? 
_entity_src_gen.gene_src_tissue_fraction           ? 
_entity_src_gen.gene_src_details                   ? 
_entity_src_gen.pdbx_gene_src_fragment             ? 
_entity_src_gen.pdbx_gene_src_scientific_name      'Staphylococcus phage 80alpha' 
_entity_src_gen.pdbx_gene_src_ncbi_taxonomy_id     2911440 
_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                NA 
_entity_src_gen.host_org_species                   ? 
_entity_src_gen.pdbx_host_org_tissue               NA 
_entity_src_gen.pdbx_host_org_tissue_fraction      ? 
_entity_src_gen.pdbx_host_org_strain               'BL21(DE3)' 
_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                 NA 
_entity_src_gen.pdbx_host_org_organelle            ? 
_entity_src_gen.pdbx_host_org_cellular_location    ? 
_entity_src_gen.pdbx_host_org_vector_type          Plasmid 
_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 
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   MET 1   -27 ?   ?   ?   A . n 
A 1 2   LYS 2   -26 ?   ?   ?   A . n 
A 1 3   HIS 3   -25 ?   ?   ?   A . n 
A 1 4   HIS 4   -24 ?   ?   ?   A . n 
A 1 5   HIS 5   -23 ?   ?   ?   A . n 
A 1 6   HIS 6   -22 ?   ?   ?   A . n 
A 1 7   HIS 7   -21 ?   ?   ?   A . n 
A 1 8   HIS 8   -20 ?   ?   ?   A . n 
A 1 9   PRO 9   -19 ?   ?   ?   A . n 
A 1 10  MET 10  -18 ?   ?   ?   A . n 
A 1 11  SER 11  -17 ?   ?   ?   A . n 
A 1 12  ASP 12  -16 ?   ?   ?   A . n 
A 1 13  TYR 13  -15 ?   ?   ?   A . n 
A 1 14  ASP 14  -14 ?   ?   ?   A . n 
A 1 15  ILE 15  -13 ?   ?   ?   A . n 
A 1 16  PRO 16  -12 ?   ?   ?   A . n 
A 1 17  THR 17  -11 ?   ?   ?   A . n 
A 1 18  THR 18  -10 ?   ?   ?   A . n 
A 1 19  GLU 19  -9  ?   ?   ?   A . n 
A 1 20  ASN 20  -8  ?   ?   ?   A . n 
A 1 21  LEU 21  -7  ?   ?   ?   A . n 
A 1 22  TYR 22  -6  ?   ?   ?   A . n 
A 1 23  PHE 23  -5  ?   ?   ?   A . n 
A 1 24  GLN 24  -4  ?   ?   ?   A . n 
A 1 25  GLY 25  -3  ?   ?   ?   A . n 
A 1 26  ALA 26  -2  ?   ?   ?   A . n 
A 1 27  MET 27  -1  ?   ?   ?   A . n 
A 1 28  GLY 28  0   ?   ?   ?   A . n 
A 1 29  MET 29  1   ?   ?   ?   A . n 
A 1 30  THR 30  2   ?   ?   ?   A . n 
A 1 31  GLU 31  3   ?   ?   ?   A . n 
A 1 32  GLN 32  4   4   GLN GLN A . n 
A 1 33  THR 33  5   5   THR THR A . n 
A 1 34  LEU 34  6   6   LEU LEU A . n 
A 1 35  PHE 35  7   7   PHE PHE A . n 
A 1 36  GLU 36  8   8   GLU GLU A . n 
A 1 37  GLN 37  9   9   GLN GLN A . n 
A 1 38  LEU 38  10  10  LEU LEU A . n 
A 1 39  ASN 39  11  11  ASN ASN A . n 
A 1 40  SER 40  12  12  SER SER A . n 
A 1 41  LYS 41  13  13  LYS LYS A . n 
A 1 42  ASN 42  14  14  ASN ASN A . n 
A 1 43  VAL 43  15  15  VAL VAL A . n 
A 1 44  ASN 44  16  16  ASN ASN A . n 
A 1 45  ASP 45  17  17  ASP ASP A . n 
A 1 46  HIS 46  18  18  HIS HIS A . n 
A 1 47  THR 47  19  19  THR THR A . n 
A 1 48  GLU 48  20  20  GLU GLU A . n 
A 1 49  GLN 49  21  21  GLN GLN A . n 
A 1 50  LYS 50  22  22  LYS LYS A . n 
A 1 51  ASN 51  23  23  ASN ASN A . n 
A 1 52  GLY 52  24  24  GLY GLY A . n 
A 1 53  LEU 53  25  25  LEU LEU A . n 
A 1 54  THR 54  26  26  THR THR A . n 
A 1 55  TYR 55  27  27  TYR TYR A . n 
A 1 56  LEU 56  28  28  LEU LEU A . n 
A 1 57  ALA 57  29  29  ALA ALA A . n 
A 1 58  TRP 58  30  30  TRP TRP A . n 
A 1 59  SER 59  31  31  SER SER A . n 
A 1 60  TYR 60  32  32  TYR TYR A . n 
A 1 61  ALA 61  33  33  ALA ALA A . n 
A 1 62  HIS 62  34  34  HIS HIS A . n 
A 1 63  GLN 63  35  35  GLN GLN A . n 
A 1 64  GLU 64  36  36  GLU GLU A . n 
A 1 65  LEU 65  37  37  LEU LEU A . n 
A 1 66  LYS 66  38  38  LYS LYS A . n 
A 1 67  LYS 67  39  39  LYS LYS A . n 
A 1 68  ILE 68  40  40  ILE ILE A . n 
A 1 69  ASP 69  41  41  ASP ASP A . n 
A 1 70  PRO 70  42  42  PRO PRO A . n 
A 1 71  ASN 71  43  43  ASN ASN A . n 
A 1 72  TYR 72  44  44  TYR TYR A . n 
A 1 73  THR 73  45  45  THR THR A . n 
A 1 74  VAL 74  46  46  VAL VAL A . n 
A 1 75  LYS 75  47  47  LYS LYS A . n 
A 1 76  VAL 76  48  48  VAL VAL A . n 
A 1 77  HIS 77  49  49  HIS HIS A . n 
A 1 78  GLU 78  50  50  GLU GLU A . n 
A 1 79  PHE 79  51  51  PHE PHE A . n 
A 1 80  PRO 80  52  52  PRO PRO A . n 
A 1 81  HIS 81  53  53  HIS HIS A . n 
A 1 82  PRO 82  54  54  PRO PRO A . n 
A 1 83  ASP 83  55  55  ASP ASP A . n 
A 1 84  ILE 84  56  56  ILE ILE A . n 
A 1 85  ASN 85  57  57  ASN ASN A . n 
A 1 86  THR 86  58  58  THR THR A . n 
A 1 87  GLU 87  59  59  GLU GLU A . n 
A 1 88  ASN 88  60  60  ASN ASN A . n 
A 1 89  TYR 89  61  61  TYR TYR A . n 
A 1 90  PHE 90  62  62  PHE PHE A . n 
A 1 91  VAL 91  63  63  VAL VAL A . n 
A 1 92  PRO 92  64  64  PRO PRO A . n 
A 1 93  TYR 93  65  65  TYR TYR A . n 
A 1 94  LEU 94  66  66  LEU LEU A . n 
A 1 95  ALA 95  67  67  ALA ALA A . n 
A 1 96  THR 96  68  68  THR THR A . n 
A 1 97  PRO 97  69  69  PRO PRO A . n 
A 1 98  GLU 98  70  70  GLU GLU A . n 
A 1 99  GLY 99  71  71  GLY GLY A . n 
A 1 100 TYR 100 72  72  TYR TYR A . n 
A 1 101 PHE 101 73  73  PHE PHE A . n 
A 1 102 VAL 102 74  74  VAL VAL A . n 
A 1 103 GLN 103 75  75  GLN GLN A . n 
A 1 104 VAL 104 76  76  VAL VAL A . n 
A 1 105 SER 105 77  77  SER SER A . n 
A 1 106 VAL 106 78  78  VAL VAL A . n 
A 1 107 THR 107 79  79  THR THR A . n 
A 1 108 VAL 108 80  80  VAL VAL A . n 
A 1 109 LYS 109 81  81  LYS LYS A . n 
A 1 110 ASP 110 82  82  ASP ASP A . n 
A 1 111 SER 111 83  83  SER SER A . n 
A 1 112 THR 112 84  84  THR THR A . n 
A 1 113 GLU 113 85  85  GLU GLU A . n 
A 1 114 THR 114 86  86  THR THR A . n 
A 1 115 GLU 115 87  87  GLU GLU A . n 
A 1 116 TRP 116 88  88  TRP TRP A . n 
A 1 117 LEU 117 89  89  LEU LEU A . n 
A 1 118 PRO 118 90  90  PRO PRO A . n 
A 1 119 VAL 119 91  91  VAL VAL A . n 
A 1 120 LEU 120 92  92  LEU LEU A . n 
A 1 121 ASP 121 93  93  ASP ASP A . n 
A 1 122 PHE 122 94  94  PHE PHE A . n 
A 1 123 ARG 123 95  95  ARG ARG A . n 
A 1 124 ASN 124 96  96  ASN ASN A . n 
A 1 125 LYS 125 97  97  LYS LYS A . n 
A 1 126 SER 126 98  98  SER SER A . n 
A 1 127 LEU 127 99  99  LEU LEU A . n 
A 1 128 ALA 128 100 100 ALA ALA A . n 
A 1 129 LYS 129 101 101 LYS LYS A . n 
A 1 130 GLY 130 102 102 GLY GLY A . n 
A 1 131 SER 131 103 103 SER SER A . n 
A 1 132 ALA 132 104 104 ALA ALA A . n 
A 1 133 THR 133 105 105 THR THR A . n 
A 1 134 THR 134 106 106 THR THR A . n 
A 1 135 PHE 135 107 107 PHE PHE A . n 
A 1 136 ASP 136 108 108 ASP ASP A . n 
A 1 137 ILE 137 109 109 ILE ILE A . n 
A 1 138 ASN 138 110 110 ASN ASN A . n 
A 1 139 LYS 139 111 111 LYS LYS A . n 
A 1 140 ALA 140 112 112 ALA ALA A . n 
A 1 141 GLN 141 113 113 GLN GLN A . n 
A 1 142 LYS 142 114 114 LYS LYS A . n 
A 1 143 ARG 143 115 115 ARG ARG A . n 
A 1 144 CYS 144 116 116 CYS CYS A . n 
A 1 145 PHE 145 117 117 PHE PHE A . n 
A 1 146 VAL 146 118 118 VAL VAL A . n 
A 1 147 LYS 147 119 119 LYS LYS A . n 
A 1 148 ALA 148 120 120 ALA ALA A . n 
A 1 149 SER 149 121 121 SER SER A . n 
A 1 150 ALA 150 122 122 ALA ALA A . n 
A 1 151 LEU 151 123 123 LEU LEU A . n 
A 1 152 HIS 152 124 124 HIS HIS A . n 
A 1 153 GLY 153 125 125 GLY GLY A . n 
A 1 154 LEU 154 126 126 LEU LEU A . n 
A 1 155 GLY 155 127 127 GLY GLY A . n 
A 1 156 LEU 156 128 128 LEU LEU A . n 
A 1 157 TYR 157 129 129 TYR TYR A . n 
A 1 158 ILE 158 130 130 ILE ILE A . n 
A 1 159 TYR 159 131 131 TYR TYR A . n 
A 1 160 ASN 160 132 ?   ?   ?   A . n 
A 1 161 GLY 161 133 ?   ?   ?   A . n 
A 1 162 GLU 162 134 ?   ?   ?   A . n 
A 1 163 GLU 163 135 ?   ?   ?   A . n 
A 1 164 LEU 164 136 ?   ?   ?   A . n 
A 1 165 PRO 165 137 ?   ?   ?   A . n 
A 1 166 SER 166 138 ?   ?   ?   A . n 
A 1 167 ALA 167 139 ?   ?   ?   A . n 
A 1 168 SER 168 140 ?   ?   ?   A . n 
A 1 169 ASP 169 141 ?   ?   ?   A . n 
# 
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 HOH 1 201 134 HOH HOH A . 
B 2 HOH 2 202 133 HOH HOH A . 
B 2 HOH 3 203 132 HOH HOH A . 
B 2 HOH 4 204 136 HOH HOH A . 
B 2 HOH 5 205 135 HOH HOH A . 
B 2 HOH 6 206 140 HOH HOH A . 
B 2 HOH 7 207 139 HOH HOH A . 
B 2 HOH 8 208 137 HOH HOH A . 
B 2 HOH 9 209 138 HOH HOH A . 
# 
_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                   8PQ8 
_exptl.crystals_number            ? 
_exptl.details                    ? 
_exptl.method                     'ELECTRON MICROSCOPY' 
_exptl.method_details             ? 
# 
_struct.entry_id                     8PQ8 
_struct.title                        'Sak Single Strand Annealing Protein from Staphylococcal Bacteriophage 80a - dCTD' 
_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        8PQ8 
_struct_keywords.text            
;Annealase, SSAP, Single Strand Annealing, Single Strand Binding, Recombineering, Recombination, SaPI, Bacteriophage, Staphylococcal, Complex, SaPI induction, SaPI2, Mobile Genetic Element, MGE, PICI, Phage-Inducible Chromosomal Island, C18, Ring
;
_struct_keywords.pdbx_keywords   RECOMBINATION 
# 
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 ? 
# 
_struct_ref.id                         1 
_struct_ref.db_name                    UNP 
_struct_ref.db_code                    C8CGY8_9CAUD 
_struct_ref.pdbx_db_accession          C8CGY8 
_struct_ref.pdbx_db_isoform            ? 
_struct_ref.entity_id                  1 
_struct_ref.pdbx_seq_one_letter_code   
;MTEQTLFEQLNSKNVNDHTEQKNGLTYLAWSYAHQELKKIDPNYTVKVHEFPHPDINTENYFVPYLATPEGYFVQVSVTV
KDSTETEWLPVLDFRNKSLAKGSATTFDINKAQKRCFVKASALHGLGLYIYNGEELPSASD
;
_struct_ref.pdbx_align_begin           1 
# 
_struct_ref_seq.align_id                      1 
_struct_ref_seq.ref_id                        1 
_struct_ref_seq.pdbx_PDB_id_code              8PQ8 
_struct_ref_seq.pdbx_strand_id                A 
_struct_ref_seq.seq_align_beg                 29 
_struct_ref_seq.pdbx_seq_align_beg_ins_code   ? 
_struct_ref_seq.seq_align_end                 169 
_struct_ref_seq.pdbx_seq_align_end_ins_code   ? 
_struct_ref_seq.pdbx_db_accession             C8CGY8 
_struct_ref_seq.db_align_beg                  1 
_struct_ref_seq.pdbx_db_align_beg_ins_code    ? 
_struct_ref_seq.db_align_end                  141 
_struct_ref_seq.pdbx_db_align_end_ins_code    ? 
_struct_ref_seq.pdbx_auth_seq_align_beg       1 
_struct_ref_seq.pdbx_auth_seq_align_end       141 
# 
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 8PQ8 MET A 1  ? UNP C8CGY8 ? ? 'initiating methionine' -27 1  
1 8PQ8 LYS A 2  ? UNP C8CGY8 ? ? 'expression tag'        -26 2  
1 8PQ8 HIS A 3  ? UNP C8CGY8 ? ? 'expression tag'        -25 3  
1 8PQ8 HIS A 4  ? UNP C8CGY8 ? ? 'expression tag'        -24 4  
1 8PQ8 HIS A 5  ? UNP C8CGY8 ? ? 'expression tag'        -23 5  
1 8PQ8 HIS A 6  ? UNP C8CGY8 ? ? 'expression tag'        -22 6  
1 8PQ8 HIS A 7  ? UNP C8CGY8 ? ? 'expression tag'        -21 7  
1 8PQ8 HIS A 8  ? UNP C8CGY8 ? ? 'expression tag'        -20 8  
1 8PQ8 PRO A 9  ? UNP C8CGY8 ? ? 'expression tag'        -19 9  
1 8PQ8 MET A 10 ? UNP C8CGY8 ? ? 'expression tag'        -18 10 
1 8PQ8 SER A 11 ? UNP C8CGY8 ? ? 'expression tag'        -17 11 
1 8PQ8 ASP A 12 ? UNP C8CGY8 ? ? 'expression tag'        -16 12 
1 8PQ8 TYR A 13 ? UNP C8CGY8 ? ? 'expression tag'        -15 13 
1 8PQ8 ASP A 14 ? UNP C8CGY8 ? ? 'expression tag'        -14 14 
1 8PQ8 ILE A 15 ? UNP C8CGY8 ? ? 'expression tag'        -13 15 
1 8PQ8 PRO A 16 ? UNP C8CGY8 ? ? 'expression tag'        -12 16 
1 8PQ8 THR A 17 ? UNP C8CGY8 ? ? 'expression tag'        -11 17 
1 8PQ8 THR A 18 ? UNP C8CGY8 ? ? 'expression tag'        -10 18 
1 8PQ8 GLU A 19 ? UNP C8CGY8 ? ? 'expression tag'        -9  19 
1 8PQ8 ASN A 20 ? UNP C8CGY8 ? ? 'expression tag'        -8  20 
1 8PQ8 LEU A 21 ? UNP C8CGY8 ? ? 'expression tag'        -7  21 
1 8PQ8 TYR A 22 ? UNP C8CGY8 ? ? 'expression tag'        -6  22 
1 8PQ8 PHE A 23 ? UNP C8CGY8 ? ? 'expression tag'        -5  23 
1 8PQ8 GLN A 24 ? UNP C8CGY8 ? ? 'expression tag'        -4  24 
1 8PQ8 GLY A 25 ? UNP C8CGY8 ? ? 'expression tag'        -3  25 
1 8PQ8 ALA A 26 ? UNP C8CGY8 ? ? 'expression tag'        -2  26 
1 8PQ8 MET A 27 ? UNP C8CGY8 ? ? 'expression tag'        -1  27 
1 8PQ8 GLY A 28 ? UNP C8CGY8 ? ? 'expression tag'        0   28 
# 
_pdbx_struct_assembly.id                   1 
_pdbx_struct_assembly.details              author_and_software_defined_assembly 
_pdbx_struct_assembly.method_details       ? 
_pdbx_struct_assembly.oligomeric_details   18-meric 
_pdbx_struct_assembly.oligomeric_count     18 
# 
_pdbx_struct_assembly_gen.assembly_id       1 
_pdbx_struct_assembly_gen.oper_expression   1,2,3,4,5,6,7,8,9,10,11,12,13,14,15,16,17,18 
_pdbx_struct_assembly_gen.asym_id_list      A,B 
# 
_pdbx_struct_assembly_auth_evidence.id                     1 
_pdbx_struct_assembly_auth_evidence.assembly_id            1 
_pdbx_struct_assembly_auth_evidence.experimental_support   microscopy 
_pdbx_struct_assembly_auth_evidence.details                'not applicable' 
# 
loop_
_pdbx_struct_oper_list.id 
_pdbx_struct_oper_list.type 
_pdbx_struct_oper_list.name 
_pdbx_struct_oper_list.symmetry_operation 
_pdbx_struct_oper_list.matrix[1][1] 
_pdbx_struct_oper_list.matrix[1][2] 
_pdbx_struct_oper_list.matrix[1][3] 
_pdbx_struct_oper_list.vector[1] 
_pdbx_struct_oper_list.matrix[2][1] 
_pdbx_struct_oper_list.matrix[2][2] 
_pdbx_struct_oper_list.matrix[2][3] 
_pdbx_struct_oper_list.vector[2] 
_pdbx_struct_oper_list.matrix[3][1] 
_pdbx_struct_oper_list.matrix[3][2] 
_pdbx_struct_oper_list.matrix[3][3] 
_pdbx_struct_oper_list.vector[3] 
1  'identity operation'       1_555 x,y,z 1.00000000  0.00000000  -0.00000000 0.00000000   -0.00000000 1.00000000  -0.00000000 
0.00000000   0.00000000  0.00000000  1.00000000 0.00000000  
2  'point symmetry operation' ?     ?     0.93970040  -0.34199876 0.00000015  60.02603997  0.34199876  0.93970040  0.00000072  
-42.03272609 -0.00000038 -0.00000063 1.00000000 0.00015331  
3  'point symmetry operation' ?     ?     0.76601950  -0.64281733 -0.00000497 130.81855339 0.64281733  0.76601950  -0.00000064 
-60.98850151 0.00000422  -0.00000271 1.00000000 -0.00050728 
4  'point symmetry operation' ?     ?     0.50001129  -0.86601889 -0.00000377 203.81497712 0.86601889  0.50001129  -0.00000212 
-54.60921227 0.00000372  -0.00000220 1.00000000 -0.00046975 
5  'point symmetry operation' ?     ?     0.17360316  -0.98481569 -0.00000183 270.22907056 0.98481569  0.17360316  -0.00000213 
-23.62559899 0.00000241  -0.00000143 1.00000000 -0.00030449 
6  'point symmetry operation' ?     ?     -0.17360390 -0.98481556 -0.00000072 322.04564502 0.98481556  -0.17360390 -0.00000284 
28.16424344  0.00000267  -0.00000120 1.00000000 -0.00038353 
7  'point symmetry operation' ?     ?     -0.50001107 -0.86601901 -0.00000059 353.01286626 0.86601901  -0.50001107 -0.00000367 
94.59889917  0.00000288  -0.00000234 1.00000000 -0.00028708 
8  'point symmetry operation' ?     ?     -0.76601925 -0.64281763 0.00000229  359.40679693 0.64281763  -0.76601925 -0.00000436 
167.58221344 0.00000455  -0.00000187 1.00000000 -0.00067645 
9  'point symmetry operation' ?     ?     -0.93969975 -0.34200057 0.00000013  340.42608357 0.34200057  -0.93969975 0.00000001  
238.38016941 0.00000011  0.00000006  1.00000000 -0.00002982 
10 'point symmetry operation' ?     ?     -1.00000000 0.00000000  -0.00000000 298.40000000 -0.00000000 -1.00000000 -0.00000000 
298.40000000 -0.00000000 -0.00000000 1.00000000 0.00000000  
11 'point symmetry operation' ?     ?     -0.93970001 0.34199985  -0.00000008 238.37963848 -0.34199985 -0.93970001 -0.00000065 
340.42696941 -0.00000030 -0.00000058 1.00000000 0.00013036  
12 'point symmetry operation' ?     ?     -0.76602036 0.64281631  0.00000511  167.57760229 -0.64281631 -0.76602036 -0.00000011 
359.40818538 0.00000384  -0.00000337 1.00000000 -0.00035148 
13 'point symmetry operation' ?     ?     -0.50001065 0.86601926  0.00000314  94.59463543  -0.86601926 -0.50001065 0.00000244  
353.01258118 0.00000369  -0.00000150 1.00000000 -0.00054969 
14 'point symmetry operation' ?     ?     -0.17369974 0.98479866  -0.00000056 28.19118314  -0.98479866 -0.17369974 -0.00000010 
322.04061055 -0.00000020 0.00000053  1.00000000 -0.00002554 
15 'point symmetry operation' ?     ?     0.17360249  0.98481581  0.00000121  -23.62780900 -0.98481581 0.17360249  0.00000332  
270.22776057 0.00000306  -0.00000177 1.00000000 -0.00039281 
16 'point symmetry operation' ?     ?     0.50001047  0.86601936  0.00000044  -54.61098611 -0.86601936 0.50001047  0.00000344  
203.81259959 0.00000276  -0.00000210 1.00000000 -0.00029142 
17 'point symmetry operation' ?     ?     0.76602046  0.64281620  -0.00000154 -60.98885743 -0.64281620 0.76602046  0.00000442  
130.81478708 0.00000402  -0.00000240 1.00000000 -0.00050600 
18 'point symmetry operation' ?     ?     0.93970040  0.34199877  0.00000003  -42.03351262 -0.34199877 0.93970040  0.00000011  
60.02679466  0.00000001  -0.00000012 1.00000000 0.00001279  
# 
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 THR A 33  ? SER A 40  ? THR A 5   SER A 12  1 ? 8  
HELX_P HELX_P2 AA2 ALA A 57  ? ASP A 69  ? ALA A 29  ASP A 41  1 ? 13 
HELX_P HELX_P3 AA3 THR A 133 ? ALA A 150 ? THR A 105 ALA A 122 1 ? 18 
HELX_P HELX_P4 AA4 GLY A 155 ? TYR A 159 ? GLY A 127 TYR A 131 5 ? 5  
# 
_struct_conf_type.id          HELX_P 
_struct_conf_type.criteria    ? 
_struct_conf_type.reference   ? 
# 
loop_
_struct_sheet.id 
_struct_sheet.type 
_struct_sheet.number_strands 
_struct_sheet.details 
AA1 ? 2 ? 
AA2 ? 3 ? 
AA3 ? 3 ? 
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 
AA2 1 2 ? anti-parallel 
AA2 2 3 ? anti-parallel 
AA3 1 2 ? anti-parallel 
AA3 2 3 ? 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 THR A 47  ? LYS A 50  ? THR A 19 LYS A 22 
AA1 2 LEU A 53  ? LEU A 56  ? LEU A 25 LEU A 28 
AA2 1 THR A 73  ? VAL A 76  ? THR A 45 VAL A 48 
AA2 2 GLY A 99  ? VAL A 108 ? GLY A 71 VAL A 80 
AA2 3 LEU A 94  ? THR A 96  ? LEU A 66 THR A 68 
AA3 1 THR A 73  ? VAL A 76  ? THR A 45 VAL A 48 
AA3 2 GLY A 99  ? VAL A 108 ? GLY A 71 VAL A 80 
AA3 3 SER A 111 ? PRO A 118 ? SER A 83 PRO A 90 
AA4 1 PHE A 79  ? PRO A 80  ? PHE A 51 PRO A 52 
AA4 2 PHE A 90  ? VAL A 91  ? PHE A 62 VAL A 63 
# 
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 GLU A 48  ? N GLU A 20 O TYR A 55  ? O TYR A 27 
AA2 1 2 N LYS A 75  ? N LYS A 47 O SER A 105 ? O SER A 77 
AA2 2 3 O PHE A 101 ? O PHE A 73 N LEU A 94  ? N LEU A 66 
AA3 1 2 N LYS A 75  ? N LYS A 47 O SER A 105 ? O SER A 77 
AA3 2 3 N VAL A 106 ? N VAL A 78 O GLU A 113 ? O GLU A 85 
AA4 1 2 N PHE A 79  ? N PHE A 51 O VAL A 91  ? O VAL A 63 
# 
_pdbx_entry_details.entry_id                   8PQ8 
_pdbx_entry_details.compound_details           ? 
_pdbx_entry_details.source_details             ? 
_pdbx_entry_details.nonpolymer_details         ? 
_pdbx_entry_details.sequence_details           ? 
_pdbx_entry_details.has_ligand_of_interest     ? 
_pdbx_entry_details.has_protein_modification   N 
# 
_em_3d_fitting.id                1 
_em_3d_fitting.entry_id          8PQ8 
_em_3d_fitting.method            ? 
_em_3d_fitting.target_criteria   ? 
_em_3d_fitting.details           
;Fitting of the truncated AlphaFold prediction was done with ChimeraX and then subjected to real space refinement in PHENIX. The output was then repeatedly adjusted with Coot and verified in PHENIX.
;
_em_3d_fitting.overall_b_value   ? 
_em_3d_fitting.ref_space         REAL 
_em_3d_fitting.ref_protocol      'RIGID BODY FIT' 
# 
_em_3d_fitting_list.id                            1 
_em_3d_fitting_list.3d_fitting_id                 1 
_em_3d_fitting_list.pdb_entry_id                  . 
_em_3d_fitting_list.pdb_chain_id                  . 
_em_3d_fitting_list.pdb_chain_residue_range       . 
_em_3d_fitting_list.details                       
;AlphaFold prediction was done locally. CTD residues of the full-length AlphaFold prediction were deleted before fiting with ChimeraX.
;
_em_3d_fitting_list.chain_id                      A 
_em_3d_fitting_list.chain_residue_range           1-141 
_em_3d_fitting_list.source_name                   AlphaFold 
_em_3d_fitting_list.type                          'in silico model' 
_em_3d_fitting_list.accession_code                ? 
_em_3d_fitting_list.initial_refinement_model_id   ? 
# 
_em_3d_reconstruction.entry_id                    8PQ8 
_em_3d_reconstruction.id                          1 
_em_3d_reconstruction.method                      ? 
_em_3d_reconstruction.algorithm                   ? 
_em_3d_reconstruction.citation_id                 ? 
_em_3d_reconstruction.details                     
'Symmetry expanded to C18, multiplying the stack by 18, from 75703 to 1365300 particles.' 
_em_3d_reconstruction.resolution                  3.21 
_em_3d_reconstruction.resolution_method           'FSC 0.143 CUT-OFF' 
_em_3d_reconstruction.magnification_calibration   ? 
_em_3d_reconstruction.nominal_pixel_size          ? 
_em_3d_reconstruction.actual_pixel_size           ? 
_em_3d_reconstruction.num_particles               75703 
_em_3d_reconstruction.euler_angles_details        ? 
_em_3d_reconstruction.num_class_averages          ? 
_em_3d_reconstruction.refinement_type             ? 
_em_3d_reconstruction.image_processing_id         1 
_em_3d_reconstruction.symmetry_type               POINT 
# 
_em_buffer.id            1 
_em_buffer.specimen_id   1 
_em_buffer.name          ? 
_em_buffer.details       '20mM Tris-HCl pH 7.6, 100mM NaCl, 1mM DTT' 
_em_buffer.pH            8.1 
# 
_em_entity_assembly.id                   1 
_em_entity_assembly.parent_id            0 
_em_entity_assembly.source               RECOMBINANT 
_em_entity_assembly.type                 COMPLEX 
_em_entity_assembly.name                 '18-mer ring cryoEM structure of the 80a-Sak NTD in apo state' 
_em_entity_assembly.details              ? 
_em_entity_assembly.synonym              ? 
_em_entity_assembly.oligomeric_details   ? 
_em_entity_assembly.entity_id_list       1 
# 
_em_imaging.entry_id                        8PQ8 
_em_imaging.id                              1 
_em_imaging.astigmatism                     ? 
_em_imaging.electron_beam_tilt_params       ? 
_em_imaging.residual_tilt                   ? 
_em_imaging.microscope_model                'TFS GLACIOS' 
_em_imaging.specimen_holder_type            ? 
_em_imaging.specimen_holder_model           ? 
_em_imaging.details                         ? 
_em_imaging.date                            ? 
_em_imaging.accelerating_voltage            200 
_em_imaging.illumination_mode               'FLOOD BEAM' 
_em_imaging.mode                            'BRIGHT FIELD' 
_em_imaging.nominal_cs                      2.7 
_em_imaging.nominal_defocus_min             1600 
_em_imaging.nominal_defocus_max             2900 
_em_imaging.calibrated_defocus_min          ? 
_em_imaging.calibrated_defocus_max          ? 
_em_imaging.tilt_angle_min                  ? 
_em_imaging.tilt_angle_max                  ? 
_em_imaging.nominal_magnification           190000 
_em_imaging.calibrated_magnification        ? 
_em_imaging.electron_source                 'FIELD EMISSION GUN' 
_em_imaging.citation_id                     ? 
_em_imaging.temperature                     ? 
_em_imaging.detector_distance               ? 
_em_imaging.recording_temperature_minimum   ? 
_em_imaging.recording_temperature_maximum   ? 
_em_imaging.alignment_procedure             ? 
_em_imaging.c2_aperture_diameter            ? 
_em_imaging.specimen_id                     1 
_em_imaging.cryogen                         NITROGEN 
# 
_em_sample_support.id               1 
_em_sample_support.film_material    ? 
_em_sample_support.method           ? 
_em_sample_support.grid_material    COPPER 
_em_sample_support.grid_mesh_size   300 
_em_sample_support.grid_type        'Quantifoil R2/1' 
_em_sample_support.details          ? 
_em_sample_support.specimen_id      1 
_em_sample_support.citation_id      ? 
# 
_em_vitrification.entry_id              8PQ8 
_em_vitrification.id                    1 
_em_vitrification.specimen_id           1 
_em_vitrification.cryogen_name          ETHANE 
_em_vitrification.humidity              100 
_em_vitrification.temp                  ? 
_em_vitrification.chamber_temperature   277 
_em_vitrification.instrument            'FEI VITROBOT MARK IV' 
_em_vitrification.method                ? 
_em_vitrification.time_resolved_state   ? 
_em_vitrification.citation_id           ? 
_em_vitrification.details               ? 
# 
_em_experiment.entry_id                8PQ8 
_em_experiment.id                      1 
_em_experiment.reconstruction_method   'SINGLE PARTICLE' 
_em_experiment.aggregation_state       PARTICLE 
_em_experiment.entity_assembly_id      1 
# 
_em_single_particle_entity.entry_id              8PQ8 
_em_single_particle_entity.id                    1 
_em_single_particle_entity.image_processing_id   1 
_em_single_particle_entity.point_symmetry        C18 
# 
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 MET -27 ? A MET 1   
2  1 Y 1 A LYS -26 ? A LYS 2   
3  1 Y 1 A HIS -25 ? A HIS 3   
4  1 Y 1 A HIS -24 ? A HIS 4   
5  1 Y 1 A HIS -23 ? A HIS 5   
6  1 Y 1 A HIS -22 ? A HIS 6   
7  1 Y 1 A HIS -21 ? A HIS 7   
8  1 Y 1 A HIS -20 ? A HIS 8   
9  1 Y 1 A PRO -19 ? A PRO 9   
10 1 Y 1 A MET -18 ? A MET 10  
11 1 Y 1 A SER -17 ? A SER 11  
12 1 Y 1 A ASP -16 ? A ASP 12  
13 1 Y 1 A TYR -15 ? A TYR 13  
14 1 Y 1 A ASP -14 ? A ASP 14  
15 1 Y 1 A ILE -13 ? A ILE 15  
16 1 Y 1 A PRO -12 ? A PRO 16  
17 1 Y 1 A THR -11 ? A THR 17  
18 1 Y 1 A THR -10 ? A THR 18  
19 1 Y 1 A GLU -9  ? A GLU 19  
20 1 Y 1 A ASN -8  ? A ASN 20  
21 1 Y 1 A LEU -7  ? A LEU 21  
22 1 Y 1 A TYR -6  ? A TYR 22  
23 1 Y 1 A PHE -5  ? A PHE 23  
24 1 Y 1 A GLN -4  ? A GLN 24  
25 1 Y 1 A GLY -3  ? A GLY 25  
26 1 Y 1 A ALA -2  ? A ALA 26  
27 1 Y 1 A MET -1  ? A MET 27  
28 1 Y 1 A GLY 0   ? A GLY 28  
29 1 Y 1 A MET 1   ? A MET 29  
30 1 Y 1 A THR 2   ? A THR 30  
31 1 Y 1 A GLU 3   ? A GLU 31  
32 1 Y 1 A ASN 132 ? A ASN 160 
33 1 Y 1 A GLY 133 ? A GLY 161 
34 1 Y 1 A GLU 134 ? A GLU 162 
35 1 Y 1 A GLU 135 ? A GLU 163 
36 1 Y 1 A LEU 136 ? A LEU 164 
37 1 Y 1 A PRO 137 ? A PRO 165 
38 1 Y 1 A SER 138 ? A SER 166 
39 1 Y 1 A ALA 139 ? A ALA 167 
40 1 Y 1 A SER 140 ? A SER 168 
41 1 Y 1 A ASP 141 ? A ASP 169 
# 
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 
ALA N    N N N 1   
ALA CA   C N S 2   
ALA C    C N N 3   
ALA O    O N N 4   
ALA CB   C N N 5   
ALA OXT  O N N 6   
ALA H    H N N 7   
ALA H2   H N N 8   
ALA HA   H N N 9   
ALA HB1  H N N 10  
ALA HB2  H N N 11  
ALA HB3  H N N 12  
ALA HXT  H N N 13  
ARG N    N N N 14  
ARG CA   C N S 15  
ARG C    C N N 16  
ARG O    O N N 17  
ARG CB   C N N 18  
ARG CG   C N N 19  
ARG CD   C N N 20  
ARG NE   N N N 21  
ARG CZ   C N N 22  
ARG NH1  N N N 23  
ARG NH2  N N N 24  
ARG OXT  O N N 25  
ARG H    H N N 26  
ARG H2   H N N 27  
ARG HA   H N N 28  
ARG HB2  H N N 29  
ARG HB3  H N N 30  
ARG HG2  H N N 31  
ARG HG3  H N N 32  
ARG HD2  H N N 33  
ARG HD3  H N N 34  
ARG HE   H N N 35  
ARG HH11 H N N 36  
ARG HH12 H N N 37  
ARG HH21 H N N 38  
ARG HH22 H N N 39  
ARG HXT  H N N 40  
ASN N    N N N 41  
ASN CA   C N S 42  
ASN C    C N N 43  
ASN O    O N N 44  
ASN CB   C N N 45  
ASN CG   C N N 46  
ASN OD1  O N N 47  
ASN ND2  N N N 48  
ASN OXT  O N N 49  
ASN H    H N N 50  
ASN H2   H N N 51  
ASN HA   H N N 52  
ASN HB2  H N N 53  
ASN HB3  H N N 54  
ASN HD21 H N N 55  
ASN HD22 H N N 56  
ASN HXT  H N N 57  
ASP N    N N N 58  
ASP CA   C N S 59  
ASP C    C N N 60  
ASP O    O N N 61  
ASP CB   C N N 62  
ASP CG   C N N 63  
ASP OD1  O N N 64  
ASP OD2  O N N 65  
ASP OXT  O N N 66  
ASP H    H N N 67  
ASP H2   H N N 68  
ASP HA   H N N 69  
ASP HB2  H N N 70  
ASP HB3  H N N 71  
ASP HD2  H N N 72  
ASP HXT  H N N 73  
CYS N    N N N 74  
CYS CA   C N R 75  
CYS C    C N N 76  
CYS O    O N N 77  
CYS CB   C N N 78  
CYS SG   S N N 79  
CYS OXT  O N N 80  
CYS H    H N N 81  
CYS H2   H N N 82  
CYS HA   H N N 83  
CYS HB2  H N N 84  
CYS HB3  H N N 85  
CYS HG   H N N 86  
CYS HXT  H N N 87  
GLN N    N N N 88  
GLN CA   C N S 89  
GLN C    C N N 90  
GLN O    O N N 91  
GLN CB   C N N 92  
GLN CG   C N N 93  
GLN CD   C N N 94  
GLN OE1  O N N 95  
GLN NE2  N N N 96  
GLN OXT  O N N 97  
GLN H    H N N 98  
GLN H2   H N N 99  
GLN HA   H N N 100 
GLN HB2  H N N 101 
GLN HB3  H N N 102 
GLN HG2  H N N 103 
GLN HG3  H N N 104 
GLN HE21 H N N 105 
GLN HE22 H N N 106 
GLN HXT  H N N 107 
GLU N    N N N 108 
GLU CA   C N S 109 
GLU C    C N N 110 
GLU O    O N N 111 
GLU CB   C N N 112 
GLU CG   C N N 113 
GLU CD   C N N 114 
GLU OE1  O N N 115 
GLU OE2  O N N 116 
GLU OXT  O N N 117 
GLU H    H N N 118 
GLU H2   H N N 119 
GLU HA   H N N 120 
GLU HB2  H N N 121 
GLU HB3  H N N 122 
GLU HG2  H N N 123 
GLU HG3  H N N 124 
GLU HE2  H N N 125 
GLU HXT  H N N 126 
GLY N    N N N 127 
GLY CA   C N N 128 
GLY C    C N N 129 
GLY O    O N N 130 
GLY OXT  O N N 131 
GLY H    H N N 132 
GLY H2   H N N 133 
GLY HA2  H N N 134 
GLY HA3  H N N 135 
GLY HXT  H N N 136 
HIS N    N N N 137 
HIS CA   C N S 138 
HIS C    C N N 139 
HIS O    O N N 140 
HIS CB   C N N 141 
HIS CG   C Y N 142 
HIS ND1  N Y N 143 
HIS CD2  C Y N 144 
HIS CE1  C Y N 145 
HIS NE2  N Y N 146 
HIS OXT  O N N 147 
HIS H    H N N 148 
HIS H2   H N N 149 
HIS HA   H N N 150 
HIS HB2  H N N 151 
HIS HB3  H N N 152 
HIS HD1  H N N 153 
HIS HD2  H N N 154 
HIS HE1  H N N 155 
HIS HE2  H N N 156 
HIS HXT  H N N 157 
HOH O    O N N 158 
HOH H1   H N N 159 
HOH H2   H N N 160 
ILE N    N N N 161 
ILE CA   C N S 162 
ILE C    C N N 163 
ILE O    O N N 164 
ILE CB   C N S 165 
ILE CG1  C N N 166 
ILE CG2  C N N 167 
ILE CD1  C N N 168 
ILE OXT  O N N 169 
ILE H    H N N 170 
ILE H2   H N N 171 
ILE HA   H N N 172 
ILE HB   H N N 173 
ILE HG12 H N N 174 
ILE HG13 H N N 175 
ILE HG21 H N N 176 
ILE HG22 H N N 177 
ILE HG23 H N N 178 
ILE HD11 H N N 179 
ILE HD12 H N N 180 
ILE HD13 H N N 181 
ILE HXT  H N N 182 
LEU N    N N N 183 
LEU CA   C N S 184 
LEU C    C N N 185 
LEU O    O N N 186 
LEU CB   C N N 187 
LEU CG   C N N 188 
LEU CD1  C N N 189 
LEU CD2  C N N 190 
LEU OXT  O N N 191 
LEU H    H N N 192 
LEU H2   H N N 193 
LEU HA   H N N 194 
LEU HB2  H N N 195 
LEU HB3  H N N 196 
LEU HG   H N N 197 
LEU HD11 H N N 198 
LEU HD12 H N N 199 
LEU HD13 H N N 200 
LEU HD21 H N N 201 
LEU HD22 H N N 202 
LEU HD23 H N N 203 
LEU HXT  H N N 204 
LYS N    N N N 205 
LYS CA   C N S 206 
LYS C    C N N 207 
LYS O    O N N 208 
LYS CB   C N N 209 
LYS CG   C N N 210 
LYS CD   C N N 211 
LYS CE   C N N 212 
LYS NZ   N N N 213 
LYS OXT  O N N 214 
LYS H    H N N 215 
LYS H2   H N N 216 
LYS HA   H N N 217 
LYS HB2  H N N 218 
LYS HB3  H N N 219 
LYS HG2  H N N 220 
LYS HG3  H N N 221 
LYS HD2  H N N 222 
LYS HD3  H N N 223 
LYS HE2  H N N 224 
LYS HE3  H N N 225 
LYS HZ1  H N N 226 
LYS HZ2  H N N 227 
LYS HZ3  H N N 228 
LYS HXT  H N N 229 
MET N    N N N 230 
MET CA   C N S 231 
MET C    C N N 232 
MET O    O N N 233 
MET CB   C N N 234 
MET CG   C N N 235 
MET SD   S N N 236 
MET CE   C N N 237 
MET OXT  O N N 238 
MET H    H N N 239 
MET H2   H N N 240 
MET HA   H N N 241 
MET HB2  H N N 242 
MET HB3  H N N 243 
MET HG2  H N N 244 
MET HG3  H N N 245 
MET HE1  H N N 246 
MET HE2  H N N 247 
MET HE3  H N N 248 
MET HXT  H N N 249 
PHE N    N N N 250 
PHE CA   C N S 251 
PHE C    C N N 252 
PHE O    O N N 253 
PHE CB   C N N 254 
PHE CG   C Y N 255 
PHE CD1  C Y N 256 
PHE CD2  C Y N 257 
PHE CE1  C Y N 258 
PHE CE2  C Y N 259 
PHE CZ   C Y N 260 
PHE OXT  O N N 261 
PHE H    H N N 262 
PHE H2   H N N 263 
PHE HA   H N N 264 
PHE HB2  H N N 265 
PHE HB3  H N N 266 
PHE HD1  H N N 267 
PHE HD2  H N N 268 
PHE HE1  H N N 269 
PHE HE2  H N N 270 
PHE HZ   H N N 271 
PHE HXT  H N N 272 
PRO N    N N N 273 
PRO CA   C N S 274 
PRO C    C N N 275 
PRO O    O N N 276 
PRO CB   C N N 277 
PRO CG   C N N 278 
PRO CD   C N N 279 
PRO OXT  O N N 280 
PRO H    H N N 281 
PRO HA   H N N 282 
PRO HB2  H N N 283 
PRO HB3  H N N 284 
PRO HG2  H N N 285 
PRO HG3  H N N 286 
PRO HD2  H N N 287 
PRO HD3  H N N 288 
PRO HXT  H N N 289 
SER N    N N N 290 
SER CA   C N S 291 
SER C    C N N 292 
SER O    O N N 293 
SER CB   C N N 294 
SER OG   O N N 295 
SER OXT  O N N 296 
SER H    H N N 297 
SER H2   H N N 298 
SER HA   H N N 299 
SER HB2  H N N 300 
SER HB3  H N N 301 
SER HG   H N N 302 
SER HXT  H N N 303 
THR N    N N N 304 
THR CA   C N S 305 
THR C    C N N 306 
THR O    O N N 307 
THR CB   C N R 308 
THR OG1  O N N 309 
THR CG2  C N N 310 
THR OXT  O N N 311 
THR H    H N N 312 
THR H2   H N N 313 
THR HA   H N N 314 
THR HB   H N N 315 
THR HG1  H N N 316 
THR HG21 H N N 317 
THR HG22 H N N 318 
THR HG23 H N N 319 
THR HXT  H N N 320 
TRP N    N N N 321 
TRP CA   C N S 322 
TRP C    C N N 323 
TRP O    O N N 324 
TRP CB   C N N 325 
TRP CG   C Y N 326 
TRP CD1  C Y N 327 
TRP CD2  C Y N 328 
TRP NE1  N Y N 329 
TRP CE2  C Y N 330 
TRP CE3  C Y N 331 
TRP CZ2  C Y N 332 
TRP CZ3  C Y N 333 
TRP CH2  C Y N 334 
TRP OXT  O N N 335 
TRP H    H N N 336 
TRP H2   H N N 337 
TRP HA   H N N 338 
TRP HB2  H N N 339 
TRP HB3  H N N 340 
TRP HD1  H N N 341 
TRP HE1  H N N 342 
TRP HE3  H N N 343 
TRP HZ2  H N N 344 
TRP HZ3  H N N 345 
TRP HH2  H N N 346 
TRP HXT  H N N 347 
TYR N    N N N 348 
TYR CA   C N S 349 
TYR C    C N N 350 
TYR O    O N N 351 
TYR CB   C N N 352 
TYR CG   C Y N 353 
TYR CD1  C Y N 354 
TYR CD2  C Y N 355 
TYR CE1  C Y N 356 
TYR CE2  C Y N 357 
TYR CZ   C Y N 358 
TYR OH   O N N 359 
TYR OXT  O N N 360 
TYR H    H N N 361 
TYR H2   H N N 362 
TYR HA   H N N 363 
TYR HB2  H N N 364 
TYR HB3  H N N 365 
TYR HD1  H N N 366 
TYR HD2  H N N 367 
TYR HE1  H N N 368 
TYR HE2  H N N 369 
TYR HH   H N N 370 
TYR HXT  H N N 371 
VAL N    N N N 372 
VAL CA   C N S 373 
VAL C    C N N 374 
VAL O    O N N 375 
VAL CB   C N N 376 
VAL CG1  C N N 377 
VAL CG2  C N N 378 
VAL OXT  O N N 379 
VAL H    H N N 380 
VAL H2   H N N 381 
VAL HA   H N N 382 
VAL HB   H N N 383 
VAL HG11 H N N 384 
VAL HG12 H N N 385 
VAL HG13 H N N 386 
VAL HG21 H N N 387 
VAL HG22 H N N 388 
VAL HG23 H N N 389 
VAL HXT  H N N 390 
# 
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 
ALA N   CA   sing N N 1   
ALA N   H    sing N N 2   
ALA N   H2   sing N N 3   
ALA CA  C    sing N N 4   
ALA CA  CB   sing N N 5   
ALA CA  HA   sing N N 6   
ALA C   O    doub N N 7   
ALA C   OXT  sing N N 8   
ALA CB  HB1  sing N N 9   
ALA CB  HB2  sing N N 10  
ALA CB  HB3  sing N N 11  
ALA OXT HXT  sing N N 12  
ARG N   CA   sing N N 13  
ARG N   H    sing N N 14  
ARG N   H2   sing N N 15  
ARG CA  C    sing N N 16  
ARG CA  CB   sing N N 17  
ARG CA  HA   sing N N 18  
ARG C   O    doub N N 19  
ARG C   OXT  sing N N 20  
ARG CB  CG   sing N N 21  
ARG CB  HB2  sing N N 22  
ARG CB  HB3  sing N N 23  
ARG CG  CD   sing N N 24  
ARG CG  HG2  sing N N 25  
ARG CG  HG3  sing N N 26  
ARG CD  NE   sing N N 27  
ARG CD  HD2  sing N N 28  
ARG CD  HD3  sing N N 29  
ARG NE  CZ   sing N N 30  
ARG NE  HE   sing N N 31  
ARG CZ  NH1  sing N N 32  
ARG CZ  NH2  doub N N 33  
ARG NH1 HH11 sing N N 34  
ARG NH1 HH12 sing N N 35  
ARG NH2 HH21 sing N N 36  
ARG NH2 HH22 sing N N 37  
ARG OXT HXT  sing N N 38  
ASN N   CA   sing N N 39  
ASN N   H    sing N N 40  
ASN N   H2   sing N N 41  
ASN CA  C    sing N N 42  
ASN CA  CB   sing N N 43  
ASN CA  HA   sing N N 44  
ASN C   O    doub N N 45  
ASN C   OXT  sing N N 46  
ASN CB  CG   sing N N 47  
ASN CB  HB2  sing N N 48  
ASN CB  HB3  sing N N 49  
ASN CG  OD1  doub N N 50  
ASN CG  ND2  sing N N 51  
ASN ND2 HD21 sing N N 52  
ASN ND2 HD22 sing N N 53  
ASN OXT HXT  sing N N 54  
ASP N   CA   sing N N 55  
ASP N   H    sing N N 56  
ASP N   H2   sing N N 57  
ASP CA  C    sing N N 58  
ASP CA  CB   sing N N 59  
ASP CA  HA   sing N N 60  
ASP C   O    doub N N 61  
ASP C   OXT  sing N N 62  
ASP CB  CG   sing N N 63  
ASP CB  HB2  sing N N 64  
ASP CB  HB3  sing N N 65  
ASP CG  OD1  doub N N 66  
ASP CG  OD2  sing N N 67  
ASP OD2 HD2  sing N N 68  
ASP OXT HXT  sing N N 69  
CYS N   CA   sing N N 70  
CYS N   H    sing N N 71  
CYS N   H2   sing N N 72  
CYS CA  C    sing N N 73  
CYS CA  CB   sing N N 74  
CYS CA  HA   sing N N 75  
CYS C   O    doub N N 76  
CYS C   OXT  sing N N 77  
CYS CB  SG   sing N N 78  
CYS CB  HB2  sing N N 79  
CYS CB  HB3  sing N N 80  
CYS SG  HG   sing N N 81  
CYS OXT HXT  sing N N 82  
GLN N   CA   sing N N 83  
GLN N   H    sing N N 84  
GLN N   H2   sing N N 85  
GLN CA  C    sing N N 86  
GLN CA  CB   sing N N 87  
GLN CA  HA   sing N N 88  
GLN C   O    doub N N 89  
GLN C   OXT  sing N N 90  
GLN CB  CG   sing N N 91  
GLN CB  HB2  sing N N 92  
GLN CB  HB3  sing N N 93  
GLN CG  CD   sing N N 94  
GLN CG  HG2  sing N N 95  
GLN CG  HG3  sing N N 96  
GLN CD  OE1  doub N N 97  
GLN CD  NE2  sing N N 98  
GLN NE2 HE21 sing N N 99  
GLN NE2 HE22 sing N N 100 
GLN OXT HXT  sing N N 101 
GLU N   CA   sing N N 102 
GLU N   H    sing N N 103 
GLU N   H2   sing N N 104 
GLU CA  C    sing N N 105 
GLU CA  CB   sing N N 106 
GLU CA  HA   sing N N 107 
GLU C   O    doub N N 108 
GLU C   OXT  sing N N 109 
GLU CB  CG   sing N N 110 
GLU CB  HB2  sing N N 111 
GLU CB  HB3  sing N N 112 
GLU CG  CD   sing N N 113 
GLU CG  HG2  sing N N 114 
GLU CG  HG3  sing N N 115 
GLU CD  OE1  doub N N 116 
GLU CD  OE2  sing N N 117 
GLU OE2 HE2  sing N N 118 
GLU OXT HXT  sing N N 119 
GLY N   CA   sing N N 120 
GLY N   H    sing N N 121 
GLY N   H2   sing N N 122 
GLY CA  C    sing N N 123 
GLY CA  HA2  sing N N 124 
GLY CA  HA3  sing N N 125 
GLY C   O    doub N N 126 
GLY C   OXT  sing N N 127 
GLY OXT HXT  sing N N 128 
HIS N   CA   sing N N 129 
HIS N   H    sing N N 130 
HIS N   H2   sing N N 131 
HIS CA  C    sing N N 132 
HIS CA  CB   sing N N 133 
HIS CA  HA   sing N N 134 
HIS C   O    doub N N 135 
HIS C   OXT  sing N N 136 
HIS CB  CG   sing N N 137 
HIS CB  HB2  sing N N 138 
HIS CB  HB3  sing N N 139 
HIS CG  ND1  sing Y N 140 
HIS CG  CD2  doub Y N 141 
HIS ND1 CE1  doub Y N 142 
HIS ND1 HD1  sing N N 143 
HIS CD2 NE2  sing Y N 144 
HIS CD2 HD2  sing N N 145 
HIS CE1 NE2  sing Y N 146 
HIS CE1 HE1  sing N N 147 
HIS NE2 HE2  sing N N 148 
HIS OXT HXT  sing N N 149 
HOH O   H1   sing N N 150 
HOH O   H2   sing N N 151 
ILE N   CA   sing N N 152 
ILE N   H    sing N N 153 
ILE N   H2   sing N N 154 
ILE CA  C    sing N N 155 
ILE CA  CB   sing N N 156 
ILE CA  HA   sing N N 157 
ILE C   O    doub N N 158 
ILE C   OXT  sing N N 159 
ILE CB  CG1  sing N N 160 
ILE CB  CG2  sing N N 161 
ILE CB  HB   sing N N 162 
ILE CG1 CD1  sing N N 163 
ILE CG1 HG12 sing N N 164 
ILE CG1 HG13 sing N N 165 
ILE CG2 HG21 sing N N 166 
ILE CG2 HG22 sing N N 167 
ILE CG2 HG23 sing N N 168 
ILE CD1 HD11 sing N N 169 
ILE CD1 HD12 sing N N 170 
ILE CD1 HD13 sing N N 171 
ILE OXT HXT  sing N N 172 
LEU N   CA   sing N N 173 
LEU N   H    sing N N 174 
LEU N   H2   sing N N 175 
LEU CA  C    sing N N 176 
LEU CA  CB   sing N N 177 
LEU CA  HA   sing N N 178 
LEU C   O    doub N N 179 
LEU C   OXT  sing N N 180 
LEU CB  CG   sing N N 181 
LEU CB  HB2  sing N N 182 
LEU CB  HB3  sing N N 183 
LEU CG  CD1  sing N N 184 
LEU CG  CD2  sing N N 185 
LEU CG  HG   sing N N 186 
LEU CD1 HD11 sing N N 187 
LEU CD1 HD12 sing N N 188 
LEU CD1 HD13 sing N N 189 
LEU CD2 HD21 sing N N 190 
LEU CD2 HD22 sing N N 191 
LEU CD2 HD23 sing N N 192 
LEU OXT HXT  sing N N 193 
LYS N   CA   sing N N 194 
LYS N   H    sing N N 195 
LYS N   H2   sing N N 196 
LYS CA  C    sing N N 197 
LYS CA  CB   sing N N 198 
LYS CA  HA   sing N N 199 
LYS C   O    doub N N 200 
LYS C   OXT  sing N N 201 
LYS CB  CG   sing N N 202 
LYS CB  HB2  sing N N 203 
LYS CB  HB3  sing N N 204 
LYS CG  CD   sing N N 205 
LYS CG  HG2  sing N N 206 
LYS CG  HG3  sing N N 207 
LYS CD  CE   sing N N 208 
LYS CD  HD2  sing N N 209 
LYS CD  HD3  sing N N 210 
LYS CE  NZ   sing N N 211 
LYS CE  HE2  sing N N 212 
LYS CE  HE3  sing N N 213 
LYS NZ  HZ1  sing N N 214 
LYS NZ  HZ2  sing N N 215 
LYS NZ  HZ3  sing N N 216 
LYS OXT HXT  sing N N 217 
MET N   CA   sing N N 218 
MET N   H    sing N N 219 
MET N   H2   sing N N 220 
MET CA  C    sing N N 221 
MET CA  CB   sing N N 222 
MET CA  HA   sing N N 223 
MET C   O    doub N N 224 
MET C   OXT  sing N N 225 
MET CB  CG   sing N N 226 
MET CB  HB2  sing N N 227 
MET CB  HB3  sing N N 228 
MET CG  SD   sing N N 229 
MET CG  HG2  sing N N 230 
MET CG  HG3  sing N N 231 
MET SD  CE   sing N N 232 
MET CE  HE1  sing N N 233 
MET CE  HE2  sing N N 234 
MET CE  HE3  sing N N 235 
MET OXT HXT  sing N N 236 
PHE N   CA   sing N N 237 
PHE N   H    sing N N 238 
PHE N   H2   sing N N 239 
PHE CA  C    sing N N 240 
PHE CA  CB   sing N N 241 
PHE CA  HA   sing N N 242 
PHE C   O    doub N N 243 
PHE C   OXT  sing N N 244 
PHE CB  CG   sing N N 245 
PHE CB  HB2  sing N N 246 
PHE CB  HB3  sing N N 247 
PHE CG  CD1  doub Y N 248 
PHE CG  CD2  sing Y N 249 
PHE CD1 CE1  sing Y N 250 
PHE CD1 HD1  sing N N 251 
PHE CD2 CE2  doub Y N 252 
PHE CD2 HD2  sing N N 253 
PHE CE1 CZ   doub Y N 254 
PHE CE1 HE1  sing N N 255 
PHE CE2 CZ   sing Y N 256 
PHE CE2 HE2  sing N N 257 
PHE CZ  HZ   sing N N 258 
PHE OXT HXT  sing N N 259 
PRO N   CA   sing N N 260 
PRO N   CD   sing N N 261 
PRO N   H    sing N N 262 
PRO CA  C    sing N N 263 
PRO CA  CB   sing N N 264 
PRO CA  HA   sing N N 265 
PRO C   O    doub N N 266 
PRO C   OXT  sing N N 267 
PRO CB  CG   sing N N 268 
PRO CB  HB2  sing N N 269 
PRO CB  HB3  sing N N 270 
PRO CG  CD   sing N N 271 
PRO CG  HG2  sing N N 272 
PRO CG  HG3  sing N N 273 
PRO CD  HD2  sing N N 274 
PRO CD  HD3  sing N N 275 
PRO OXT HXT  sing N N 276 
SER N   CA   sing N N 277 
SER N   H    sing N N 278 
SER N   H2   sing N N 279 
SER CA  C    sing N N 280 
SER CA  CB   sing N N 281 
SER CA  HA   sing N N 282 
SER C   O    doub N N 283 
SER C   OXT  sing N N 284 
SER CB  OG   sing N N 285 
SER CB  HB2  sing N N 286 
SER CB  HB3  sing N N 287 
SER OG  HG   sing N N 288 
SER OXT HXT  sing N N 289 
THR N   CA   sing N N 290 
THR N   H    sing N N 291 
THR N   H2   sing N N 292 
THR CA  C    sing N N 293 
THR CA  CB   sing N N 294 
THR CA  HA   sing N N 295 
THR C   O    doub N N 296 
THR C   OXT  sing N N 297 
THR CB  OG1  sing N N 298 
THR CB  CG2  sing N N 299 
THR CB  HB   sing N N 300 
THR OG1 HG1  sing N N 301 
THR CG2 HG21 sing N N 302 
THR CG2 HG22 sing N N 303 
THR CG2 HG23 sing N N 304 
THR OXT HXT  sing N N 305 
TRP N   CA   sing N N 306 
TRP N   H    sing N N 307 
TRP N   H2   sing N N 308 
TRP CA  C    sing N N 309 
TRP CA  CB   sing N N 310 
TRP CA  HA   sing N N 311 
TRP C   O    doub N N 312 
TRP C   OXT  sing N N 313 
TRP CB  CG   sing N N 314 
TRP CB  HB2  sing N N 315 
TRP CB  HB3  sing N N 316 
TRP CG  CD1  doub Y N 317 
TRP CG  CD2  sing Y N 318 
TRP CD1 NE1  sing Y N 319 
TRP CD1 HD1  sing N N 320 
TRP CD2 CE2  doub Y N 321 
TRP CD2 CE3  sing Y N 322 
TRP NE1 CE2  sing Y N 323 
TRP NE1 HE1  sing N N 324 
TRP CE2 CZ2  sing Y N 325 
TRP CE3 CZ3  doub Y N 326 
TRP CE3 HE3  sing N N 327 
TRP CZ2 CH2  doub Y N 328 
TRP CZ2 HZ2  sing N N 329 
TRP CZ3 CH2  sing Y N 330 
TRP CZ3 HZ3  sing N N 331 
TRP CH2 HH2  sing N N 332 
TRP OXT HXT  sing N N 333 
TYR N   CA   sing N N 334 
TYR N   H    sing N N 335 
TYR N   H2   sing N N 336 
TYR CA  C    sing N N 337 
TYR CA  CB   sing N N 338 
TYR CA  HA   sing N N 339 
TYR C   O    doub N N 340 
TYR C   OXT  sing N N 341 
TYR CB  CG   sing N N 342 
TYR CB  HB2  sing N N 343 
TYR CB  HB3  sing N N 344 
TYR CG  CD1  doub Y N 345 
TYR CG  CD2  sing Y N 346 
TYR CD1 CE1  sing Y N 347 
TYR CD1 HD1  sing N N 348 
TYR CD2 CE2  doub Y N 349 
TYR CD2 HD2  sing N N 350 
TYR CE1 CZ   doub Y N 351 
TYR CE1 HE1  sing N N 352 
TYR CE2 CZ   sing Y N 353 
TYR CE2 HE2  sing N N 354 
TYR CZ  OH   sing N N 355 
TYR OH  HH   sing N N 356 
TYR OXT HXT  sing N N 357 
VAL N   CA   sing N N 358 
VAL N   H    sing N N 359 
VAL N   H2   sing N N 360 
VAL CA  C    sing N N 361 
VAL CA  CB   sing N N 362 
VAL CA  HA   sing N N 363 
VAL C   O    doub N N 364 
VAL C   OXT  sing N N 365 
VAL CB  CG1  sing N N 366 
VAL CB  CG2  sing N N 367 
VAL CB  HB   sing N N 368 
VAL CG1 HG11 sing N N 369 
VAL CG1 HG12 sing N N 370 
VAL CG1 HG13 sing N N 371 
VAL CG2 HG21 sing N N 372 
VAL CG2 HG22 sing N N 373 
VAL CG2 HG23 sing N N 374 
VAL OXT HXT  sing N N 375 
# 
_em_admin.current_status     REL 
_em_admin.deposition_date    2023-07-10 
_em_admin.deposition_site    PDBE 
_em_admin.entry_id           8PQ8 
_em_admin.last_update        2025-03-05 
_em_admin.map_release_date   2025-02-12 
_em_admin.title              'Sak Single Strand Annealing Protein from Staphylococcal Bacteriophage 80a - dCTD' 
# 
loop_
_em_buffer_component.buffer_id 
_em_buffer_component.concentration 
_em_buffer_component.concentration_units 
_em_buffer_component.formula 
_em_buffer_component.id 
_em_buffer_component.name 
1 20  mM Tris-HCl 1 'Tris-HCl pH 7.6' 
1 100 mM NaCl     2 'Sodium Chloride' 
1 1   mM DTT      3 Dithiothreitol    
# 
_em_ctf_correction.details                  'CTF correction was applied on-the-fly during data collection with CryoSPARC Live.' 
_em_ctf_correction.em_image_processing_id   1 
_em_ctf_correction.id                       1 
_em_ctf_correction.type                     'PHASE FLIPPING AND AMPLITUDE CORRECTION' 
# 
_em_entity_assembly_molwt.entity_assembly_id   1 
_em_entity_assembly_molwt.experimental_flag    YES 
_em_entity_assembly_molwt.id                   1 
_em_entity_assembly_molwt.units                MEGADALTONS 
_em_entity_assembly_molwt.value                0.46 
# 
_em_entity_assembly_naturalsource.cell                 ? 
_em_entity_assembly_naturalsource.cellular_location    NA 
_em_entity_assembly_naturalsource.entity_assembly_id   1 
_em_entity_assembly_naturalsource.id                   2 
_em_entity_assembly_naturalsource.ncbi_tax_id          2911440 
_em_entity_assembly_naturalsource.organism             'Staphylococcus phage 80alpha' 
_em_entity_assembly_naturalsource.organelle            NA 
_em_entity_assembly_naturalsource.organ                NA 
_em_entity_assembly_naturalsource.strain               ? 
_em_entity_assembly_naturalsource.tissue               NA 
_em_entity_assembly_naturalsource.details              ? 
# 
_em_entity_assembly_recombinant.cell                 ? 
_em_entity_assembly_recombinant.entity_assembly_id   1 
_em_entity_assembly_recombinant.id                   2 
_em_entity_assembly_recombinant.ncbi_tax_id          469008 
_em_entity_assembly_recombinant.organism             'Escherichia coli BL21(DE3)' 
_em_entity_assembly_recombinant.plasmid              ? 
_em_entity_assembly_recombinant.strain               ? 
# 
_em_image_processing.details              ? 
_em_image_processing.id                   1 
_em_image_processing.image_recording_id   1 
# 
_em_image_recording.average_exposure_time               2.99 
_em_image_recording.avg_electron_dose_per_subtomogram   ? 
_em_image_recording.avg_electron_dose_per_image         50 
_em_image_recording.details                             ? 
_em_image_recording.detector_mode                       ? 
_em_image_recording.film_or_detector_model              'TFS FALCON 4i (4k x 4k)' 
_em_image_recording.id                                  1 
_em_image_recording.imaging_id                          1 
_em_image_recording.num_diffraction_images              ? 
_em_image_recording.num_grids_imaged                    1 
_em_image_recording.num_real_images                     4344 
# 
loop_
_em_software.category 
_em_software.details 
_em_software.id 
_em_software.image_processing_id 
_em_software.fitting_id 
_em_software.imaging_id 
_em_software.name 
_em_software.version 
'PARTICLE SELECTION'            ?                                               1  1 ? ? cryoSPARC       4.2.1        
'IMAGE ACQUISITION'             ?                                               2  ? ? 1 EPU             2.13.0       
MASKING                         ?                                               3  ? ? ? ?               ?            
'CTF CORRECTION'                'CTF correct on-the-fly with cryoSPARC Live'    4  1 ? ? cryoSPARC       4.2.1        
'LAYERLINE INDEXING'            ?                                               5  ? ? ? ?               ?            
'DIFFRACTION INDEXING'          ?                                               6  ? ? ? ?               ?            
'MODEL FITTING'                 ?                                               7  ? 1 ? 'UCSF ChimeraX' 1.4          
OTHER                           ?                                               8  ? ? ? ?               ?            
'MODEL REFINEMENT'              ?                                               9  ? 1 ? PHENIX          1.20.1       
'MODEL REFINEMENT'              ?                                               10 ? 1 ? Coot            '0.9.8.4 EL' 
'INITIAL EULER ASSIGNMENT'      ?                                               11 1 ? ? cryoSPARC       4.2.1        
'FINAL EULER ASSIGNMENT'        ?                                               12 1 ? ? cryoSPARC       4.2.1        
CLASSIFICATION                  ?                                               13 1 ? ? ?               ?            
RECONSTRUCTION                  'Local refinement job after symmetry expansion' 14 1 ? ? cryoSPARC       4.2.1        
'VOLUME SELECTION'              ?                                               15 1 1 1 ?               ?            
'SERIES ALIGNMENT'              ?                                               16 1 1 1 ?               ?            
'MOLECULAR REPLACEMENT'         ?                                               17 1 1 1 ?               ?            
'LATTICE DISTORTION CORRECTION' ?                                               18 1 1 1 ?               ?            
'SYMMETRY DETERMINATION'        ?                                               19 1 1 1 ?               ?            
'CRYSTALLOGRAPHY MERGING'       ?                                               20 1 1 1 ?               ?            
# 
_em_specimen.concentration           1 
_em_specimen.details                 'Monodisperse sample' 
_em_specimen.embedding_applied       NO 
_em_specimen.experiment_id           1 
_em_specimen.id                      1 
_em_specimen.shadowing_applied       NO 
_em_specimen.staining_applied        NO 
_em_specimen.vitrification_applied   YES 
# 
_pdbx_audit_support.funding_organization   'Knut and Alice Wallenberg Foundation' 
_pdbx_audit_support.country                Sweden 
_pdbx_audit_support.grant_number           ? 
_pdbx_audit_support.ordinal                1 
# 
_pdbx_initial_refinement_model.id               1 
_pdbx_initial_refinement_model.type             'in silico model' 
_pdbx_initial_refinement_model.source_name      AlphaFold 
_pdbx_initial_refinement_model.accession_code   ? 
# 
_atom_sites.entry_id                    8PQ8 
_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]   1.000000 
_atom_sites.fract_transf_matrix[1][2]   0.000000 
_atom_sites.fract_transf_matrix[1][3]   0.000000 
_atom_sites.fract_transf_matrix[2][1]   0.000000 
_atom_sites.fract_transf_matrix[2][2]   1.000000 
_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]   1.000000 
_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 
C 
N 
O 
S 
# 
loop_
_atom_site.group_PDB 
_atom_site.id 
_atom_site.type_symbol 
_atom_site.label_atom_id 
_atom_site.label_alt_id 
_atom_site.label_comp_id 
_atom_site.label_asym_id 
_atom_site.label_entity_id 
_atom_site.label_seq_id 
_atom_site.pdbx_PDB_ins_code 
_atom_site.Cartn_x 
_atom_site.Cartn_y 
_atom_site.Cartn_z 
_atom_site.occupancy 
_atom_site.B_iso_or_equiv 
_atom_site.pdbx_formal_charge 
_atom_site.auth_seq_id 
_atom_site.auth_comp_id 
_atom_site.auth_asym_id 
_atom_site.auth_atom_id 
_atom_site.pdbx_PDB_model_num 
ATOM   1    N N   . GLN A 1 32  ? 207.340 109.231 128.788 1.00 161.12 ? 4   GLN A N   1 
ATOM   2    C CA  . GLN A 1 32  ? 206.526 108.446 129.753 1.00 161.61 ? 4   GLN A CA  1 
ATOM   3    C C   . GLN A 1 32  ? 205.258 109.226 130.102 1.00 161.58 ? 4   GLN A C   1 
ATOM   4    O O   . GLN A 1 32  ? 204.455 109.487 129.185 1.00 160.94 ? 4   GLN A O   1 
ATOM   5    C CB  . GLN A 1 32  ? 207.314 108.187 131.037 1.00 161.30 ? 4   GLN A CB  1 
ATOM   6    C CG  . GLN A 1 32  ? 208.710 107.627 130.810 1.00 161.89 ? 4   GLN A CG  1 
ATOM   7    C CD  . GLN A 1 32  ? 209.518 107.623 132.084 1.00 162.02 ? 4   GLN A CD  1 
ATOM   8    O OE1 . GLN A 1 32  ? 210.663 107.181 132.116 1.00 161.00 ? 4   GLN A OE1 1 
ATOM   9    N NE2 . GLN A 1 32  ? 208.921 108.124 133.153 1.00 162.46 ? 4   GLN A NE2 1 
ATOM   10   N N   . THR A 1 33  ? 205.094 109.583 131.378 1.00 157.28 ? 5   THR A N   1 
ATOM   11   C CA  . THR A 1 33  ? 203.890 110.322 131.841 1.00 156.89 ? 5   THR A CA  1 
ATOM   12   C C   . THR A 1 33  ? 204.261 111.154 133.071 1.00 156.25 ? 5   THR A C   1 
ATOM   13   O O   . THR A 1 33  ? 205.302 110.858 133.687 1.00 157.23 ? 5   THR A O   1 
ATOM   14   C CB  . THR A 1 33  ? 202.721 109.365 132.111 1.00 156.37 ? 5   THR A CB  1 
ATOM   15   O OG1 . THR A 1 33  ? 201.620 110.134 132.595 1.00 155.94 ? 5   THR A OG1 1 
ATOM   16   C CG2 . THR A 1 33  ? 203.066 108.282 133.109 1.00 155.62 ? 5   THR A CG2 1 
ATOM   17   N N   . LEU A 1 34  ? 203.435 112.144 133.419 1.00 150.42 ? 6   LEU A N   1 
ATOM   18   C CA  . LEU A 1 34  ? 203.771 113.051 134.549 1.00 150.95 ? 6   LEU A CA  1 
ATOM   19   C C   . LEU A 1 34  ? 203.825 112.255 135.856 1.00 150.61 ? 6   LEU A C   1 
ATOM   20   O O   . LEU A 1 34  ? 204.813 112.411 136.592 1.00 151.53 ? 6   LEU A O   1 
ATOM   21   C CB  . LEU A 1 34  ? 202.728 114.171 134.622 1.00 150.32 ? 6   LEU A CB  1 
ATOM   22   C CG  . LEU A 1 34  ? 201.290 113.730 134.891 1.00 149.61 ? 6   LEU A CG  1 
ATOM   23   C CD1 . LEU A 1 34  ? 200.945 113.878 136.366 1.00 148.36 ? 6   LEU A CD1 1 
ATOM   24   C CD2 . LEU A 1 34  ? 200.315 114.530 134.042 1.00 149.15 ? 6   LEU A CD2 1 
ATOM   25   N N   . PHE A 1 35  ? 202.835 111.397 136.112 1.00 144.82 ? 7   PHE A N   1 
ATOM   26   C CA  . PHE A 1 35  ? 202.797 110.687 137.414 1.00 144.25 ? 7   PHE A CA  1 
ATOM   27   C C   . PHE A 1 35  ? 204.084 109.877 137.577 1.00 144.49 ? 7   PHE A C   1 
ATOM   28   O O   . PHE A 1 35  ? 204.765 110.048 138.598 1.00 143.95 ? 7   PHE A O   1 
ATOM   29   C CB  . PHE A 1 35  ? 201.573 109.776 137.522 1.00 143.13 ? 7   PHE A CB  1 
ATOM   30   C CG  . PHE A 1 35  ? 201.425 109.110 138.865 1.00 142.96 ? 7   PHE A CG  1 
ATOM   31   C CD1 . PHE A 1 35  ? 201.269 109.866 140.014 1.00 141.84 ? 7   PHE A CD1 1 
ATOM   32   C CD2 . PHE A 1 35  ? 201.474 107.731 138.987 1.00 143.73 ? 7   PHE A CD2 1 
ATOM   33   C CE1 . PHE A 1 35  ? 201.142 109.260 141.253 1.00 142.03 ? 7   PHE A CE1 1 
ATOM   34   C CE2 . PHE A 1 35  ? 201.352 107.125 140.227 1.00 143.29 ? 7   PHE A CE2 1 
ATOM   35   C CZ  . PHE A 1 35  ? 201.185 107.890 141.357 1.00 142.43 ? 7   PHE A CZ  1 
ATOM   36   N N   . GLU A 1 36  ? 204.412 109.035 136.595 1.00 151.48 ? 8   GLU A N   1 
ATOM   37   C CA  . GLU A 1 36  ? 205.598 108.151 136.752 1.00 151.79 ? 8   GLU A CA  1 
ATOM   38   C C   . GLU A 1 36  ? 206.878 108.986 136.888 1.00 152.72 ? 8   GLU A C   1 
ATOM   39   O O   . GLU A 1 36  ? 207.683 108.669 137.783 1.00 152.52 ? 8   GLU A O   1 
ATOM   40   C CB  . GLU A 1 36  ? 205.704 107.189 135.569 1.00 152.21 ? 8   GLU A CB  1 
ATOM   41   C CG  . GLU A 1 36  ? 206.904 106.261 135.644 1.00 153.35 ? 8   GLU A CG  1 
ATOM   42   C CD  . GLU A 1 36  ? 206.946 105.295 136.817 1.00 152.82 ? 8   GLU A CD  1 
ATOM   43   O OE1 . GLU A 1 36  ? 206.006 105.307 137.637 1.00 151.77 ? 8   GLU A OE1 1 
ATOM   44   O OE2 . GLU A 1 36  ? 207.929 104.535 136.913 1.00 152.64 ? 8   GLU A OE2 1 
ATOM   45   N N   . GLN A 1 37  ? 207.107 109.948 135.992 1.00 154.24 ? 9   GLN A N   1 
ATOM   46   C CA  . GLN A 1 37  ? 208.315 110.809 136.091 1.00 153.51 ? 9   GLN A CA  1 
ATOM   47   C C   . GLN A 1 37  ? 208.402 111.402 137.500 1.00 153.48 ? 9   GLN A C   1 
ATOM   48   O O   . GLN A 1 37  ? 209.432 111.191 138.166 1.00 153.76 ? 9   GLN A O   1 
ATOM   49   C CB  . GLN A 1 37  ? 208.271 111.920 135.042 1.00 153.52 ? 9   GLN A CB  1 
ATOM   50   C CG  . GLN A 1 37  ? 208.281 111.404 133.611 1.00 154.82 ? 9   GLN A CG  1 
ATOM   51   C CD  . GLN A 1 37  ? 208.238 112.521 132.598 1.00 155.62 ? 9   GLN A CD  1 
ATOM   52   O OE1 . GLN A 1 37  ? 208.202 113.700 132.944 1.00 154.92 ? 9   GLN A OE1 1 
ATOM   53   N NE2 . GLN A 1 37  ? 208.242 112.154 131.327 1.00 154.56 ? 9   GLN A NE2 1 
ATOM   54   N N   . LEU A 1 38  ? 207.357 112.104 137.936 1.00 143.43 ? 10  LEU A N   1 
ATOM   55   C CA  . LEU A 1 38  ? 207.346 112.774 139.263 1.00 142.68 ? 10  LEU A CA  1 
ATOM   56   C C   . LEU A 1 38  ? 207.464 111.723 140.370 1.00 144.54 ? 10  LEU A C   1 
ATOM   57   O O   . LEU A 1 38  ? 208.181 111.984 141.353 1.00 144.14 ? 10  LEU A O   1 
ATOM   58   C CB  . LEU A 1 38  ? 206.058 113.591 139.403 1.00 141.90 ? 10  LEU A CB  1 
ATOM   59   C CG  . LEU A 1 38  ? 205.878 114.727 138.399 1.00 142.99 ? 10  LEU A CG  1 
ATOM   60   C CD1 . LEU A 1 38  ? 204.766 115.664 138.842 1.00 143.12 ? 10  LEU A CD1 1 
ATOM   61   C CD2 . LEU A 1 38  ? 207.177 115.496 138.216 1.00 142.66 ? 10  LEU A CD2 1 
ATOM   62   N N   . ASN A 1 39  ? 206.782 110.584 140.219 1.00 148.46 ? 11  ASN A N   1 
ATOM   63   C CA  . ASN A 1 39  ? 206.773 109.558 141.297 1.00 148.66 ? 11  ASN A CA  1 
ATOM   64   C C   . ASN A 1 39  ? 208.201 109.046 141.500 1.00 148.36 ? 11  ASN A C   1 
ATOM   65   O O   . ASN A 1 39  ? 208.596 108.846 142.664 1.00 147.70 ? 11  ASN A O   1 
ATOM   66   C CB  . ASN A 1 39  ? 205.769 108.438 141.007 1.00 146.65 ? 11  ASN A CB  1 
ATOM   67   C CG  . ASN A 1 39  ? 205.655 107.422 142.124 1.00 147.55 ? 11  ASN A CG  1 
ATOM   68   O OD1 . ASN A 1 39  ? 206.623 106.747 142.465 1.00 148.20 ? 11  ASN A OD1 1 
ATOM   69   N ND2 . ASN A 1 39  ? 204.465 107.291 142.686 1.00 148.22 ? 11  ASN A ND2 1 
ATOM   70   N N   . SER A 1 40  ? 208.945 108.860 140.408 1.00 151.71 ? 12  SER A N   1 
ATOM   71   C CA  . SER A 1 40  ? 210.318 108.305 140.508 1.00 152.00 ? 12  SER A CA  1 
ATOM   72   C C   . SER A 1 40  ? 211.322 109.420 140.822 1.00 153.01 ? 12  SER A C   1 
ATOM   73   O O   . SER A 1 40  ? 212.118 109.760 139.926 1.00 152.09 ? 12  SER A O   1 
ATOM   74   C CB  . SER A 1 40  ? 210.681 107.572 139.245 1.00 151.35 ? 12  SER A CB  1 
ATOM   75   O OG  . SER A 1 40  ? 211.987 107.024 139.338 1.00 152.42 ? 12  SER A OG  1 
ATOM   76   N N   . LYS A 1 41  ? 211.275 109.970 142.039 1.00 151.33 ? 13  LYS A N   1 
ATOM   77   C CA  . LYS A 1 41  ? 212.258 110.997 142.480 1.00 150.20 ? 13  LYS A CA  1 
ATOM   78   C C   . LYS A 1 41  ? 212.577 110.719 143.951 1.00 151.01 ? 13  LYS A C   1 
ATOM   79   O O   . LYS A 1 41  ? 211.731 110.093 144.616 1.00 150.62 ? 13  LYS A O   1 
ATOM   80   C CB  . LYS A 1 41  ? 211.696 112.411 142.317 1.00 149.54 ? 13  LYS A CB  1 
ATOM   81   C CG  . LYS A 1 41  ? 211.349 112.820 140.892 1.00 150.39 ? 13  LYS A CG  1 
ATOM   82   C CD  . LYS A 1 41  ? 210.789 114.221 140.800 1.00 149.66 ? 13  LYS A CD  1 
ATOM   83   C CE  . LYS A 1 41  ? 211.744 115.266 141.334 1.00 148.89 ? 13  LYS A CE  1 
ATOM   84   N NZ  . LYS A 1 41  ? 213.026 115.267 140.592 1.00 149.31 ? 13  LYS A NZ  1 
ATOM   85   N N   . ASN A 1 42  ? 213.738 111.157 144.448 1.00 153.53 ? 14  ASN A N   1 
ATOM   86   C CA  . ASN A 1 42  ? 214.020 110.966 145.897 1.00 152.69 ? 14  ASN A CA  1 
ATOM   87   C C   . ASN A 1 42  ? 213.920 112.320 146.601 1.00 151.95 ? 14  ASN A C   1 
ATOM   88   O O   . ASN A 1 42  ? 214.807 113.165 146.385 1.00 152.61 ? 14  ASN A O   1 
ATOM   89   C CB  . ASN A 1 42  ? 215.379 110.311 146.148 1.00 152.66 ? 14  ASN A CB  1 
ATOM   90   C CG  . ASN A 1 42  ? 215.488 108.927 145.546 1.00 154.05 ? 14  ASN A CG  1 
ATOM   91   O OD1 . ASN A 1 42  ? 214.542 108.434 144.937 1.00 155.04 ? 14  ASN A OD1 1 
ATOM   92   N ND2 . ASN A 1 42  ? 216.635 108.290 145.718 1.00 153.25 ? 14  ASN A ND2 1 
ATOM   93   N N   . VAL A 1 43  ? 212.850 112.530 147.368 1.00 147.50 ? 15  VAL A N   1 
ATOM   94   C CA  . VAL A 1 43  ? 212.675 113.803 148.123 1.00 148.48 ? 15  VAL A CA  1 
ATOM   95   C C   . VAL A 1 43  ? 213.087 113.537 149.572 1.00 147.50 ? 15  VAL A C   1 
ATOM   96   O O   . VAL A 1 43  ? 212.810 114.394 150.427 1.00 147.09 ? 15  VAL A O   1 
ATOM   97   C CB  . VAL A 1 43  ? 211.226 114.313 148.023 1.00 147.67 ? 15  VAL A CB  1 
ATOM   98   C CG1 . VAL A 1 43  ? 210.851 114.644 146.588 1.00 145.94 ? 15  VAL A CG1 1 
ATOM   99   C CG2 . VAL A 1 43  ? 210.236 113.323 148.615 1.00 146.38 ? 15  VAL A CG2 1 
ATOM   100  N N   . ASN A 1 44  ? 213.743 112.401 149.819 1.00 147.34 ? 16  ASN A N   1 
ATOM   101  C CA  . ASN A 1 44  ? 214.155 112.019 151.197 1.00 146.86 ? 16  ASN A CA  1 
ATOM   102  C C   . ASN A 1 44  ? 215.149 113.036 151.761 1.00 147.59 ? 16  ASN A C   1 
ATOM   103  O O   . ASN A 1 44  ? 215.050 113.348 152.961 1.00 147.75 ? 16  ASN A O   1 
ATOM   104  C CB  . ASN A 1 44  ? 214.767 110.617 151.235 1.00 145.87 ? 16  ASN A CB  1 
ATOM   105  C CG  . ASN A 1 44  ? 213.805 109.537 150.790 1.00 146.79 ? 16  ASN A CG  1 
ATOM   106  O OD1 . ASN A 1 44  ? 212.654 109.821 150.472 1.00 147.57 ? 16  ASN A OD1 1 
ATOM   107  N ND2 . ASN A 1 44  ? 214.262 108.296 150.785 1.00 147.78 ? 16  ASN A ND2 1 
ATOM   108  N N   . ASP A 1 45  ? 216.081 113.520 150.940 1.00 152.01 ? 17  ASP A N   1 
ATOM   109  C CA  . ASP A 1 45  ? 217.136 114.424 151.471 1.00 151.91 ? 17  ASP A CA  1 
ATOM   110  C C   . ASP A 1 45  ? 216.495 115.698 152.027 1.00 152.14 ? 17  ASP A C   1 
ATOM   111  O O   . ASP A 1 45  ? 216.906 116.129 153.119 1.00 151.84 ? 17  ASP A O   1 
ATOM   112  C CB  . ASP A 1 45  ? 218.177 114.738 150.395 1.00 151.84 ? 17  ASP A CB  1 
ATOM   113  C CG  . ASP A 1 45  ? 218.885 113.500 149.872 1.00 152.77 ? 17  ASP A CG  1 
ATOM   114  O OD1 . ASP A 1 45  ? 218.192 112.613 149.334 1.00 153.24 ? 17  ASP A OD1 1 
ATOM   115  O OD2 . ASP A 1 45  ? 220.120 113.429 150.017 1.00 152.77 ? 17  ASP A OD2 1 
ATOM   116  N N   . HIS A 1 46  ? 215.529 116.270 151.302 1.00 149.81 ? 18  HIS A N   1 
ATOM   117  C CA  . HIS A 1 46  ? 214.841 117.507 151.762 1.00 148.74 ? 18  HIS A CA  1 
ATOM   118  C C   . HIS A 1 46  ? 213.616 117.142 152.607 1.00 148.05 ? 18  HIS A C   1 
ATOM   119  O O   . HIS A 1 46  ? 212.481 117.370 152.141 1.00 147.74 ? 18  HIS A O   1 
ATOM   120  C CB  . HIS A 1 46  ? 214.466 118.382 150.563 1.00 148.36 ? 18  HIS A CB  1 
ATOM   121  C CG  . HIS A 1 46  ? 215.642 118.773 149.731 1.00 149.32 ? 18  HIS A CG  1 
ATOM   122  N ND1 . HIS A 1 46  ? 216.428 117.854 149.069 1.00 147.83 ? 18  HIS A ND1 1 
ATOM   123  C CD2 . HIS A 1 46  ? 216.148 119.976 149.431 1.00 148.37 ? 18  HIS A CD2 1 
ATOM   124  C CE1 . HIS A 1 46  ? 217.382 118.492 148.406 1.00 148.04 ? 18  HIS A CE1 1 
ATOM   125  N NE2 . HIS A 1 46  ? 217.230 119.782 148.611 1.00 149.60 ? 18  HIS A NE2 1 
ATOM   126  N N   . THR A 1 47  ? 213.836 116.605 153.810 1.00 152.79 ? 19  THR A N   1 
ATOM   127  C CA  . THR A 1 47  ? 212.710 116.267 154.720 1.00 153.42 ? 19  THR A CA  1 
ATOM   128  C C   . THR A 1 47  ? 213.055 116.662 156.157 1.00 152.84 ? 19  THR A C   1 
ATOM   129  O O   . THR A 1 47  ? 214.256 116.714 156.479 1.00 151.92 ? 19  THR A O   1 
ATOM   130  C CB  . THR A 1 47  ? 212.346 114.778 154.669 1.00 151.83 ? 19  THR A CB  1 
ATOM   131  O OG1 . THR A 1 47  ? 213.499 114.029 155.054 1.00 152.55 ? 19  THR A OG1 1 
ATOM   132  C CG2 . THR A 1 47  ? 211.863 114.324 153.310 1.00 150.31 ? 19  THR A CG2 1 
ATOM   133  N N   . GLU A 1 48  ? 212.039 116.928 156.980 1.00 155.98 ? 20  GLU A N   1 
ATOM   134  C CA  . GLU A 1 48  ? 212.265 117.253 158.411 1.00 154.93 ? 20  GLU A CA  1 
ATOM   135  C C   . GLU A 1 48  ? 211.537 116.216 159.269 1.00 156.09 ? 20  GLU A C   1 
ATOM   136  O O   . GLU A 1 48  ? 210.340 115.983 159.012 1.00 154.55 ? 20  GLU A O   1 
ATOM   137  C CB  . GLU A 1 48  ? 211.741 118.654 158.718 1.00 154.14 ? 20  GLU A CB  1 
ATOM   138  C CG  . GLU A 1 48  ? 211.883 119.046 160.178 1.00 154.81 ? 20  GLU A CG  1 
ATOM   139  C CD  . GLU A 1 48  ? 211.328 120.417 160.523 1.00 154.81 ? 20  GLU A CD  1 
ATOM   140  O OE1 . GLU A 1 48  ? 210.818 121.094 159.608 1.00 153.60 ? 20  GLU A OE1 1 
ATOM   141  O OE2 . GLU A 1 48  ? 211.394 120.799 161.708 1.00 154.21 ? 20  GLU A OE2 1 
ATOM   142  N N   . GLN A 1 49  ? 212.227 115.627 160.250 1.00 160.64 ? 21  GLN A N   1 
ATOM   143  C CA  . GLN A 1 49  ? 211.587 114.642 161.163 1.00 160.81 ? 21  GLN A CA  1 
ATOM   144  C C   . GLN A 1 49  ? 211.068 115.375 162.405 1.00 160.83 ? 21  GLN A C   1 
ATOM   145  O O   . GLN A 1 49  ? 211.860 115.569 163.345 1.00 161.64 ? 21  GLN A O   1 
ATOM   146  C CB  . GLN A 1 49  ? 212.578 113.543 161.547 1.00 159.78 ? 21  GLN A CB  1 
ATOM   147  C CG  . GLN A 1 49  ? 213.113 112.750 160.361 1.00 159.83 ? 21  GLN A CG  1 
ATOM   148  C CD  . GLN A 1 49  ? 212.061 111.949 159.633 1.00 161.19 ? 21  GLN A CD  1 
ATOM   149  O OE1 . GLN A 1 49  ? 210.894 111.917 160.014 1.00 161.80 ? 21  GLN A OE1 1 
ATOM   150  N NE2 . GLN A 1 49  ? 212.482 111.255 158.588 1.00 161.47 ? 21  GLN A NE2 1 
ATOM   151  N N   . LYS A 1 50  ? 209.792 115.771 162.397 1.00 158.87 ? 22  LYS A N   1 
ATOM   152  C CA  . LYS A 1 50  ? 209.189 116.451 163.574 1.00 159.12 ? 22  LYS A CA  1 
ATOM   153  C C   . LYS A 1 50  ? 208.030 115.596 164.094 1.00 158.99 ? 22  LYS A C   1 
ATOM   154  O O   . LYS A 1 50  ? 207.148 115.261 163.278 1.00 158.92 ? 22  LYS A O   1 
ATOM   155  C CB  . LYS A 1 50  ? 208.703 117.852 163.195 1.00 158.23 ? 22  LYS A CB  1 
ATOM   156  C CG  . LYS A 1 50  ? 208.019 118.623 164.315 1.00 158.58 ? 22  LYS A CG  1 
ATOM   157  C CD  . LYS A 1 50  ? 208.899 118.826 165.529 1.00 158.92 ? 22  LYS A CD  1 
ATOM   158  C CE  . LYS A 1 50  ? 208.208 119.591 166.637 1.00 159.14 ? 22  LYS A CE  1 
ATOM   159  N NZ  . LYS A 1 50  ? 209.090 119.767 167.814 1.00 159.21 ? 22  LYS A NZ  1 
ATOM   160  N N   . ASN A 1 51  ? 208.064 115.222 165.378 1.00 157.15 ? 23  ASN A N   1 
ATOM   161  C CA  . ASN A 1 51  ? 206.983 114.401 165.992 1.00 156.67 ? 23  ASN A CA  1 
ATOM   162  C C   . ASN A 1 51  ? 207.061 112.969 165.450 1.00 156.11 ? 23  ASN A C   1 
ATOM   163  O O   . ASN A 1 51  ? 206.097 112.210 165.657 1.00 157.09 ? 23  ASN A O   1 
ATOM   164  C CB  . ASN A 1 51  ? 205.590 115.003 165.780 1.00 156.60 ? 23  ASN A CB  1 
ATOM   165  C CG  . ASN A 1 51  ? 205.422 116.370 166.404 1.00 156.34 ? 23  ASN A CG  1 
ATOM   166  O OD1 . ASN A 1 51  ? 206.344 116.894 167.025 1.00 156.25 ? 23  ASN A OD1 1 
ATOM   167  N ND2 . ASN A 1 51  ? 204.242 116.949 166.255 1.00 156.29 ? 23  ASN A ND2 1 
ATOM   168  N N   . GLY A 1 52  ? 208.179 112.605 164.817 1.00 158.76 ? 24  GLY A N   1 
ATOM   169  C CA  . GLY A 1 52  ? 208.307 111.262 164.222 1.00 159.47 ? 24  GLY A CA  1 
ATOM   170  C C   . GLY A 1 52  ? 207.618 111.149 162.873 1.00 158.72 ? 24  GLY A C   1 
ATOM   171  O O   . GLY A 1 52  ? 207.421 110.007 162.416 1.00 158.52 ? 24  GLY A O   1 
ATOM   172  N N   . LEU A 1 53  ? 207.247 112.275 162.256 1.00 155.05 ? 25  LEU A N   1 
ATOM   173  C CA  . LEU A 1 53  ? 206.660 112.213 160.889 1.00 154.53 ? 25  LEU A CA  1 
ATOM   174  C C   . LEU A 1 53  ? 207.640 112.825 159.886 1.00 154.99 ? 25  LEU A C   1 
ATOM   175  O O   . LEU A 1 53  ? 208.510 113.601 160.314 1.00 156.15 ? 25  LEU A O   1 
ATOM   176  C CB  . LEU A 1 53  ? 205.307 112.934 160.841 1.00 154.47 ? 25  LEU A CB  1 
ATOM   177  C CG  . LEU A 1 53  ? 204.179 112.329 161.676 1.00 154.01 ? 25  LEU A CG  1 
ATOM   178  C CD1 . LEU A 1 53  ? 204.299 112.707 163.143 1.00 153.37 ? 25  LEU A CD1 1 
ATOM   179  C CD2 . LEU A 1 53  ? 202.820 112.735 161.129 1.00 153.84 ? 25  LEU A CD2 1 
ATOM   180  N N   . THR A 1 54  ? 207.482 112.496 158.604 1.00 153.02 ? 26  THR A N   1 
ATOM   181  C CA  . THR A 1 54  ? 208.408 113.003 157.560 1.00 152.31 ? 26  THR A CA  1 
ATOM   182  C C   . THR A 1 54  ? 207.674 114.045 156.712 1.00 150.20 ? 26  THR A C   1 
ATOM   183  O O   . THR A 1 54  ? 206.560 113.742 156.247 1.00 151.83 ? 26  THR A O   1 
ATOM   184  C CB  . THR A 1 54  ? 208.950 111.845 156.715 1.00 153.01 ? 26  THR A CB  1 
ATOM   185  O OG1 . THR A 1 54  ? 209.605 110.929 157.593 1.00 153.14 ? 26  THR A OG1 1 
ATOM   186  C CG2 . THR A 1 54  ? 209.911 112.296 155.638 1.00 152.35 ? 26  THR A CG2 1 
ATOM   187  N N   . TYR A 1 55  ? 208.265 115.231 156.547 1.00 146.19 ? 27  TYR A N   1 
ATOM   188  C CA  . TYR A 1 55  ? 207.613 116.322 155.783 1.00 145.18 ? 27  TYR A CA  1 
ATOM   189  C C   . TYR A 1 55  ? 208.584 116.846 154.724 1.00 144.92 ? 27  TYR A C   1 
ATOM   190  O O   . TYR A 1 55  ? 209.742 117.095 155.083 1.00 147.34 ? 27  TYR A O   1 
ATOM   191  C CB  . TYR A 1 55  ? 207.272 117.460 156.741 1.00 145.99 ? 27  TYR A CB  1 
ATOM   192  C CG  . TYR A 1 55  ? 206.442 117.065 157.936 1.00 147.25 ? 27  TYR A CG  1 
ATOM   193  C CD1 . TYR A 1 55  ? 205.180 116.516 157.788 1.00 146.95 ? 27  TYR A CD1 1 
ATOM   194  C CD2 . TYR A 1 55  ? 206.930 117.230 159.221 1.00 147.38 ? 27  TYR A CD2 1 
ATOM   195  C CE1 . TYR A 1 55  ? 204.418 116.152 158.886 1.00 147.51 ? 27  TYR A CE1 1 
ATOM   196  C CE2 . TYR A 1 55  ? 206.184 116.870 160.330 1.00 147.38 ? 27  TYR A CE2 1 
ATOM   197  C CZ  . TYR A 1 55  ? 204.922 116.330 160.162 1.00 148.41 ? 27  TYR A CZ  1 
ATOM   198  O OH  . TYR A 1 55  ? 204.178 115.973 161.259 1.00 148.09 ? 27  TYR A OH  1 
ATOM   199  N N   . LEU A 1 56  ? 208.138 117.033 153.479 1.00 126.58 ? 28  LEU A N   1 
ATOM   200  C CA  . LEU A 1 56  ? 209.035 117.655 152.467 1.00 127.49 ? 28  LEU A CA  1 
ATOM   201  C C   . LEU A 1 56  ? 208.749 119.161 152.450 1.00 129.30 ? 28  LEU A C   1 
ATOM   202  O O   . LEU A 1 56  ? 207.564 119.531 152.492 1.00 131.14 ? 28  LEU A O   1 
ATOM   203  C CB  . LEU A 1 56  ? 208.859 116.978 151.099 1.00 124.67 ? 28  LEU A CB  1 
ATOM   204  C CG  . LEU A 1 56  ? 207.490 117.062 150.425 1.00 126.86 ? 28  LEU A CG  1 
ATOM   205  C CD1 . LEU A 1 56  ? 207.325 118.368 149.665 1.00 128.15 ? 28  LEU A CD1 1 
ATOM   206  C CD2 . LEU A 1 56  ? 207.275 115.879 149.494 1.00 129.21 ? 28  LEU A CD2 1 
ATOM   207  N N   . ALA A 1 57  ? 209.788 119.997 152.459 1.00 109.72 ? 29  ALA A N   1 
ATOM   208  C CA  . ALA A 1 57  ? 209.589 121.462 152.549 1.00 108.16 ? 29  ALA A CA  1 
ATOM   209  C C   . ALA A 1 57  ? 208.889 121.985 151.292 1.00 109.56 ? 29  ALA A C   1 
ATOM   210  O O   . ALA A 1 57  ? 209.144 121.442 150.205 1.00 108.25 ? 29  ALA A O   1 
ATOM   211  C CB  . ALA A 1 57  ? 210.919 122.133 152.761 1.00 110.49 ? 29  ALA A CB  1 
ATOM   212  N N   . TRP A 1 58  ? 208.044 123.008 151.446 1.00 102.42 ? 30  TRP A N   1 
ATOM   213  C CA  . TRP A 1 58  ? 207.305 123.578 150.288 1.00 101.17 ? 30  TRP A CA  1 
ATOM   214  C C   . TRP A 1 58  ? 208.289 124.167 149.276 1.00 103.64 ? 30  TRP A C   1 
ATOM   215  O O   . TRP A 1 58  ? 208.046 124.014 148.070 1.00 106.18 ? 30  TRP A O   1 
ATOM   216  C CB  . TRP A 1 58  ? 206.294 124.639 150.731 1.00 100.75 ? 30  TRP A CB  1 
ATOM   217  C CG  . TRP A 1 58  ? 206.897 125.815 151.432 1.00 98.69  ? 30  TRP A CG  1 
ATOM   218  C CD1 . TRP A 1 58  ? 207.587 125.817 152.608 1.00 99.89  ? 30  TRP A CD1 1 
ATOM   219  C CD2 . TRP A 1 58  ? 206.930 127.166 150.945 1.00 97.00  ? 30  TRP A CD2 1 
ATOM   220  N NE1 . TRP A 1 58  ? 208.006 127.084 152.909 1.00 102.07 ? 30  TRP A NE1 1 
ATOM   221  C CE2 . TRP A 1 58  ? 207.622 127.932 151.905 1.00 100.88 ? 30  TRP A CE2 1 
ATOM   222  C CE3 . TRP A 1 58  ? 206.431 127.803 149.804 1.00 96.33  ? 30  TRP A CE3 1 
ATOM   223  C CZ2 . TRP A 1 58  ? 207.824 129.303 151.755 1.00 101.20 ? 30  TRP A CZ2 1 
ATOM   224  C CZ3 . TRP A 1 58  ? 206.630 129.157 149.658 1.00 100.36 ? 30  TRP A CZ3 1 
ATOM   225  C CH2 . TRP A 1 58  ? 207.317 129.894 150.621 1.00 101.08 ? 30  TRP A CH2 1 
ATOM   226  N N   . SER A 1 59  ? 209.338 124.840 149.752 1.00 105.10 ? 31  SER A N   1 
ATOM   227  C CA  . SER A 1 59  ? 210.315 125.484 148.841 1.00 104.98 ? 31  SER A CA  1 
ATOM   228  C C   . SER A 1 59  ? 210.749 124.487 147.763 1.00 104.93 ? 31  SER A C   1 
ATOM   229  O O   . SER A 1 59  ? 210.760 124.869 146.579 1.00 101.93 ? 31  SER A O   1 
ATOM   230  C CB  . SER A 1 59  ? 211.485 125.998 149.617 1.00 103.84 ? 31  SER A CB  1 
ATOM   231  O OG  . SER A 1 59  ? 212.121 124.941 150.318 1.00 103.27 ? 31  SER A OG  1 
ATOM   232  N N   . TYR A 1 60  ? 211.077 123.255 148.162 1.00 116.90 ? 32  TYR A N   1 
ATOM   233  C CA  . TYR A 1 60  ? 211.527 122.214 147.199 1.00 117.15 ? 32  TYR A CA  1 
ATOM   234  C C   . TYR A 1 60  ? 210.383 121.872 146.236 1.00 117.49 ? 32  TYR A C   1 
ATOM   235  O O   . TYR A 1 60  ? 210.625 121.790 145.022 1.00 118.56 ? 32  TYR A O   1 
ATOM   236  C CB  . TYR A 1 60  ? 212.086 121.015 147.972 1.00 114.98 ? 32  TYR A CB  1 
ATOM   237  C CG  . TYR A 1 60  ? 212.555 119.843 147.146 1.00 117.69 ? 32  TYR A CG  1 
ATOM   238  C CD1 . TYR A 1 60  ? 211.669 119.079 146.405 1.00 119.58 ? 32  TYR A CD1 1 
ATOM   239  C CD2 . TYR A 1 60  ? 213.879 119.445 147.172 1.00 118.97 ? 32  TYR A CD2 1 
ATOM   240  C CE1 . TYR A 1 60  ? 212.093 117.984 145.673 1.00 120.69 ? 32  TYR A CE1 1 
ATOM   241  C CE2 . TYR A 1 60  ? 214.323 118.361 146.434 1.00 119.68 ? 32  TYR A CE2 1 
ATOM   242  C CZ  . TYR A 1 60  ? 213.429 117.625 145.682 1.00 120.36 ? 32  TYR A CZ  1 
ATOM   243  O OH  . TYR A 1 60  ? 213.858 116.542 144.955 1.00 117.44 ? 32  TYR A OH  1 
ATOM   244  N N   . ALA A 1 61  ? 209.167 121.727 146.761 1.00 108.94 ? 33  ALA A N   1 
ATOM   245  C CA  . ALA A 1 61  ? 208.001 121.403 145.911 1.00 109.12 ? 33  ALA A CA  1 
ATOM   246  C C   . ALA A 1 61  ? 207.761 122.534 144.908 1.00 109.68 ? 33  ALA A C   1 
ATOM   247  O O   . ALA A 1 61  ? 207.457 122.231 143.742 1.00 110.28 ? 33  ALA A O   1 
ATOM   248  C CB  . ALA A 1 61  ? 206.792 121.192 146.778 1.00 108.42 ? 33  ALA A CB  1 
ATOM   249  N N   . HIS A 1 62  ? 207.895 123.785 145.355 1.00 107.41 ? 34  HIS A N   1 
ATOM   250  C CA  . HIS A 1 62  ? 207.608 124.940 144.465 1.00 107.31 ? 34  HIS A CA  1 
ATOM   251  C C   . HIS A 1 62  ? 208.576 124.928 143.281 1.00 107.49 ? 34  HIS A C   1 
ATOM   252  O O   . HIS A 1 62  ? 208.132 125.242 142.165 1.00 108.96 ? 34  HIS A O   1 
ATOM   253  C CB  . HIS A 1 62  ? 207.661 126.262 145.236 1.00 105.31 ? 34  HIS A CB  1 
ATOM   254  C CG  . HIS A 1 62  ? 207.332 127.446 144.394 1.00 103.85 ? 34  HIS A CG  1 
ATOM   255  N ND1 . HIS A 1 62  ? 207.647 128.733 144.779 1.00 107.44 ? 34  HIS A ND1 1 
ATOM   256  C CD2 . HIS A 1 62  ? 206.717 127.547 143.197 1.00 102.75 ? 34  HIS A CD2 1 
ATOM   257  C CE1 . HIS A 1 62  ? 207.239 129.578 143.855 1.00 106.27 ? 34  HIS A CE1 1 
ATOM   258  N NE2 . HIS A 1 62  ? 206.666 128.875 142.874 1.00 107.10 ? 34  HIS A NE2 1 
ATOM   259  N N   . GLN A 1 63  ? 209.844 124.583 143.517 1.00 106.48 ? 35  GLN A N   1 
ATOM   260  C CA  . GLN A 1 63  ? 210.832 124.638 142.406 1.00 107.42 ? 35  GLN A CA  1 
ATOM   261  C C   . GLN A 1 63  ? 210.633 123.434 141.473 1.00 108.31 ? 35  GLN A C   1 
ATOM   262  O O   . GLN A 1 63  ? 210.670 123.648 140.250 1.00 108.21 ? 35  GLN A O   1 
ATOM   263  C CB  . GLN A 1 63  ? 212.263 124.758 142.936 1.00 108.89 ? 35  GLN A CB  1 
ATOM   264  C CG  . GLN A 1 63  ? 212.728 123.588 143.786 1.00 111.51 ? 35  GLN A CG  1 
ATOM   265  C CD  . GLN A 1 63  ? 214.143 123.779 144.273 1.00 110.05 ? 35  GLN A CD  1 
ATOM   266  O OE1 . GLN A 1 63  ? 214.784 124.789 143.993 1.00 107.36 ? 35  GLN A OE1 1 
ATOM   267  N NE2 . GLN A 1 63  ? 214.640 122.806 145.019 1.00 108.62 ? 35  GLN A NE2 1 
ATOM   268  N N   . GLU A 1 64  ? 210.410 122.225 142.006 1.00 113.94 ? 36  GLU A N   1 
ATOM   269  C CA  . GLU A 1 64  ? 210.316 121.037 141.113 1.00 113.39 ? 36  GLU A CA  1 
ATOM   270  C C   . GLU A 1 64  ? 209.158 121.178 140.121 1.00 114.02 ? 36  GLU A C   1 
ATOM   271  O O   . GLU A 1 64  ? 209.384 120.942 138.924 1.00 114.62 ? 36  GLU A O   1 
ATOM   272  C CB  . GLU A 1 64  ? 210.110 119.769 141.940 1.00 112.48 ? 36  GLU A CB  1 
ATOM   273  C CG  . GLU A 1 64  ? 211.228 119.500 142.926 1.00 113.37 ? 36  GLU A CG  1 
ATOM   274  C CD  . GLU A 1 64  ? 212.596 119.285 142.305 1.00 116.87 ? 36  GLU A CD  1 
ATOM   275  O OE1 . GLU A 1 64  ? 212.738 118.340 141.506 1.00 118.21 ? 36  GLU A OE1 1 
ATOM   276  O OE2 . GLU A 1 64  ? 213.515 120.062 142.623 1.00 118.12 ? 36  GLU A OE2 1 
ATOM   277  N N   . LEU A 1 65  ? 207.967 121.538 140.595 1.00 110.33 ? 37  LEU A N   1 
ATOM   278  C CA  . LEU A 1 65  ? 206.822 121.757 139.673 1.00 108.53 ? 37  LEU A CA  1 
ATOM   279  C C   . LEU A 1 65  ? 207.147 122.925 138.741 1.00 109.64 ? 37  LEU A C   1 
ATOM   280  O O   . LEU A 1 65  ? 206.779 122.849 137.558 1.00 110.32 ? 37  LEU A O   1 
ATOM   281  C CB  . LEU A 1 65  ? 205.558 122.037 140.489 1.00 109.14 ? 37  LEU A CB  1 
ATOM   282  C CG  . LEU A 1 65  ? 205.103 120.911 141.415 1.00 109.31 ? 37  LEU A CG  1 
ATOM   283  C CD1 . LEU A 1 65  ? 203.682 121.152 141.895 1.00 110.44 ? 37  LEU A CD1 1 
ATOM   284  C CD2 . LEU A 1 65  ? 205.199 119.564 140.715 1.00 108.83 ? 37  LEU A CD2 1 
ATOM   285  N N   . LYS A 1 66  ? 207.739 124.004 139.268 1.00 114.41 ? 38  LYS A N   1 
ATOM   286  C CA  . LYS A 1 66  ? 208.122 125.164 138.413 1.00 115.38 ? 38  LYS A CA  1 
ATOM   287  C C   . LYS A 1 66  ? 209.003 124.700 137.252 1.00 115.74 ? 38  LYS A C   1 
ATOM   288  O O   . LYS A 1 66  ? 208.805 125.184 136.124 1.00 113.82 ? 38  LYS A O   1 
ATOM   289  C CB  . LYS A 1 66  ? 208.839 126.269 139.192 1.00 112.87 ? 38  LYS A CB  1 
ATOM   290  C CG  . LYS A 1 66  ? 207.941 127.260 139.917 1.00 113.49 ? 38  LYS A CG  1 
ATOM   291  C CD  . LYS A 1 66  ? 207.104 128.057 138.940 1.00 115.40 ? 38  LYS A CD  1 
ATOM   292  C CE  . LYS A 1 66  ? 206.236 129.109 139.594 1.00 113.59 ? 38  LYS A CE  1 
ATOM   293  N NZ  . LYS A 1 66  ? 205.443 129.859 138.592 1.00 111.13 ? 38  LYS A NZ  1 
ATOM   294  N N   . LYS A 1 67  ? 209.948 123.809 137.531 1.00 118.30 ? 39  LYS A N   1 
ATOM   295  C CA  . LYS A 1 67  ? 210.819 123.283 136.447 1.00 117.78 ? 39  LYS A CA  1 
ATOM   296  C C   . LYS A 1 67  ? 209.946 122.558 135.420 1.00 117.99 ? 39  LYS A C   1 
ATOM   297  O O   . LYS A 1 67  ? 209.914 123.002 134.260 1.00 119.14 ? 39  LYS A O   1 
ATOM   298  C CB  . LYS A 1 67  ? 211.883 122.347 137.024 1.00 118.54 ? 39  LYS A CB  1 
ATOM   299  C CG  . LYS A 1 67  ? 212.902 123.015 137.936 1.00 118.06 ? 39  LYS A CG  1 
ATOM   300  C CD  . LYS A 1 67  ? 213.587 122.048 138.877 1.00 119.77 ? 39  LYS A CD  1 
ATOM   301  C CE  . LYS A 1 67  ? 214.234 120.880 138.164 1.00 118.01 ? 39  LYS A CE  1 
ATOM   302  N NZ  . LYS A 1 67  ? 214.874 119.945 139.120 1.00 116.81 ? 39  LYS A NZ  1 
ATOM   303  N N   . ILE A 1 68  ? 209.257 121.495 135.840 1.00 117.63 ? 40  ILE A N   1 
ATOM   304  C CA  . ILE A 1 68  ? 208.389 120.706 134.913 1.00 117.62 ? 40  ILE A CA  1 
ATOM   305  C C   . ILE A 1 68  ? 207.520 121.672 134.103 1.00 117.13 ? 40  ILE A C   1 
ATOM   306  O O   . ILE A 1 68  ? 207.527 121.570 132.864 1.00 117.35 ? 40  ILE A O   1 
ATOM   307  C CB  . ILE A 1 68  ? 207.521 119.702 135.696 1.00 117.08 ? 40  ILE A CB  1 
ATOM   308  C CG1 . ILE A 1 68  ? 208.368 118.779 136.576 1.00 115.92 ? 40  ILE A CG1 1 
ATOM   309  C CG2 . ILE A 1 68  ? 206.628 118.913 134.753 1.00 116.61 ? 40  ILE A CG2 1 
ATOM   310  C CD1 . ILE A 1 68  ? 209.364 117.944 135.809 1.00 114.92 ? 40  ILE A CD1 1 
ATOM   311  N N   . ASP A 1 69  ? 206.750 122.515 134.795 1.00 121.48 ? 41  ASP A N   1 
ATOM   312  C CA  . ASP A 1 69  ? 205.841 123.474 134.116 1.00 122.24 ? 41  ASP A CA  1 
ATOM   313  C C   . ASP A 1 69  ? 206.172 124.887 134.600 1.00 123.46 ? 41  ASP A C   1 
ATOM   314  O O   . ASP A 1 69  ? 206.025 125.150 135.806 1.00 126.80 ? 41  ASP A O   1 
ATOM   315  C CB  . ASP A 1 69  ? 204.376 123.123 134.379 1.00 122.78 ? 41  ASP A CB  1 
ATOM   316  C CG  . ASP A 1 69  ? 203.380 124.077 133.741 1.00 123.52 ? 41  ASP A CG  1 
ATOM   317  O OD1 . ASP A 1 69  ? 203.816 125.105 133.193 1.00 121.07 ? 41  ASP A OD1 1 
ATOM   318  O OD2 . ASP A 1 69  ? 202.171 123.781 133.799 1.00 125.34 ? 41  ASP A OD2 1 
ATOM   319  N N   . PRO A 1 70  ? 206.595 125.804 133.706 1.00 120.44 ? 42  PRO A N   1 
ATOM   320  C CA  . PRO A 1 70  ? 206.946 127.165 134.100 1.00 120.75 ? 42  PRO A CA  1 
ATOM   321  C C   . PRO A 1 70  ? 205.734 127.921 134.658 1.00 121.42 ? 42  PRO A C   1 
ATOM   322  O O   . PRO A 1 70  ? 205.909 128.692 135.579 1.00 119.74 ? 42  PRO A O   1 
ATOM   323  C CB  . PRO A 1 70  ? 207.387 127.811 132.781 1.00 121.85 ? 42  PRO A CB  1 
ATOM   324  C CG  . PRO A 1 70  ? 206.701 126.989 131.717 1.00 121.78 ? 42  PRO A CG  1 
ATOM   325  C CD  . PRO A 1 70  ? 206.733 125.580 132.268 1.00 120.56 ? 42  PRO A CD  1 
ATOM   326  N N   . ASN A 1 71  ? 204.550 127.689 134.088 1.00 124.86 ? 43  ASN A N   1 
ATOM   327  C CA  . ASN A 1 71  ? 203.336 128.428 134.528 1.00 123.63 ? 43  ASN A CA  1 
ATOM   328  C C   . ASN A 1 71  ? 202.340 127.466 135.181 1.00 123.49 ? 43  ASN A C   1 
ATOM   329  O O   . ASN A 1 71  ? 201.610 126.786 134.439 1.00 124.07 ? 43  ASN A O   1 
ATOM   330  C CB  . ASN A 1 71  ? 202.696 129.209 133.378 1.00 123.31 ? 43  ASN A CB  1 
ATOM   331  C CG  . ASN A 1 71  ? 202.469 128.370 132.138 1.00 124.83 ? 43  ASN A CG  1 
ATOM   332  O OD1 . ASN A 1 71  ? 203.105 127.335 131.956 1.00 124.33 ? 43  ASN A OD1 1 
ATOM   333  N ND2 . ASN A 1 71  ? 201.570 128.813 131.275 1.00 125.08 ? 43  ASN A ND2 1 
ATOM   334  N N   . TYR A 1 72  ? 202.323 127.406 136.515 1.00 111.42 ? 44  TYR A N   1 
ATOM   335  C CA  . TYR A 1 72  ? 201.366 126.579 137.231 1.00 111.01 ? 44  TYR A CA  1 
ATOM   336  C C   . TYR A 1 72  ? 200.740 127.406 138.343 1.00 110.47 ? 44  TYR A C   1 
ATOM   337  O O   . TYR A 1 72  ? 201.340 128.362 138.837 1.00 112.05 ? 44  TYR A O   1 
ATOM   338  C CB  . TYR A 1 72  ? 202.023 125.309 137.789 1.00 109.09 ? 44  TYR A CB  1 
ATOM   339  C CG  . TYR A 1 72  ? 202.660 125.479 139.145 1.00 109.34 ? 44  TYR A CG  1 
ATOM   340  C CD1 . TYR A 1 72  ? 203.838 126.197 139.295 1.00 109.49 ? 44  TYR A CD1 1 
ATOM   341  C CD2 . TYR A 1 72  ? 202.092 124.911 140.275 1.00 109.65 ? 44  TYR A CD2 1 
ATOM   342  C CE1 . TYR A 1 72  ? 204.426 126.350 140.531 1.00 111.35 ? 44  TYR A CE1 1 
ATOM   343  C CE2 . TYR A 1 72  ? 202.675 125.057 141.515 1.00 109.05 ? 44  TYR A CE2 1 
ATOM   344  C CZ  . TYR A 1 72  ? 203.841 125.779 141.638 1.00 112.73 ? 44  TYR A CZ  1 
ATOM   345  O OH  . TYR A 1 72  ? 204.424 125.928 142.874 1.00 116.65 ? 44  TYR A OH  1 
ATOM   346  N N   . THR A 1 73  ? 199.526 127.026 138.734 1.00 95.49  ? 45  THR A N   1 
ATOM   347  C CA  . THR A 1 73  ? 198.697 127.834 139.617 1.00 94.97  ? 45  THR A CA  1 
ATOM   348  C C   . THR A 1 73  ? 198.473 127.127 140.946 1.00 96.31  ? 45  THR A C   1 
ATOM   349  O O   . THR A 1 73  ? 198.209 125.923 140.984 1.00 99.49  ? 45  THR A O   1 
ATOM   350  C CB  . THR A 1 73  ? 197.344 128.139 138.965 1.00 95.26  ? 45  THR A CB  1 
ATOM   351  O OG1 . THR A 1 73  ? 197.550 128.605 137.626 1.00 97.00  ? 45  THR A OG1 1 
ATOM   352  C CG2 . THR A 1 73  ? 196.595 129.202 139.754 1.00 92.48  ? 45  THR A CG2 1 
ATOM   353  N N   . VAL A 1 74  ? 198.583 127.888 142.033 1.00 82.87  ? 46  VAL A N   1 
ATOM   354  C CA  . VAL A 1 74  ? 198.213 127.440 143.369 1.00 78.09  ? 46  VAL A CA  1 
ATOM   355  C C   . VAL A 1 74  ? 197.134 128.375 143.889 1.00 75.12  ? 46  VAL A C   1 
ATOM   356  O O   . VAL A 1 74  ? 197.332 129.594 143.930 1.00 83.63  ? 46  VAL A O   1 
ATOM   357  C CB  . VAL A 1 74  ? 199.419 127.420 144.324 1.00 80.04  ? 46  VAL A CB  1 
ATOM   358  C CG1 . VAL A 1 74  ? 198.970 127.090 145.736 1.00 74.82  ? 46  VAL A CG1 1 
ATOM   359  C CG2 . VAL A 1 74  ? 200.454 126.425 143.846 1.00 80.05  ? 46  VAL A CG2 1 
ATOM   360  N N   . LYS A 1 75  ? 195.997 127.809 144.284 1.00 63.08  ? 47  LYS A N   1 
ATOM   361  C CA  . LYS A 1 75  ? 194.851 128.590 144.732 1.00 64.59  ? 47  LYS A CA  1 
ATOM   362  C C   . LYS A 1 75  ? 194.415 128.088 146.098 1.00 76.49  ? 47  LYS A C   1 
ATOM   363  O O   . LYS A 1 75  ? 194.168 126.891 146.270 1.00 86.35  ? 47  LYS A O   1 
ATOM   364  C CB  . LYS A 1 75  ? 193.697 128.496 143.731 1.00 68.38  ? 47  LYS A CB  1 
ATOM   365  C CG  . LYS A 1 75  ? 192.369 129.006 144.258 1.00 72.34  ? 47  LYS A CG  1 
ATOM   366  C CD  . LYS A 1 75  ? 191.280 128.889 143.208 1.00 73.53  ? 47  LYS A CD  1 
ATOM   367  C CE  . LYS A 1 75  ? 189.912 129.190 143.793 1.00 72.69  ? 47  LYS A CE  1 
ATOM   368  N NZ  . LYS A 1 75  ? 189.900 130.486 144.524 1.00 71.84  ? 47  LYS A NZ  1 
ATOM   369  N N   . VAL A 1 76  ? 194.322 128.997 147.062 1.00 55.25  ? 48  VAL A N   1 
ATOM   370  C CA  . VAL A 1 76  ? 193.833 128.671 148.395 1.00 51.03  ? 48  VAL A CA  1 
ATOM   371  C C   . VAL A 1 76  ? 192.376 129.103 148.480 1.00 55.33  ? 48  VAL A C   1 
ATOM   372  O O   . VAL A 1 76  ? 192.068 130.296 148.407 1.00 64.28  ? 48  VAL A O   1 
ATOM   373  C CB  . VAL A 1 76  ? 194.677 129.352 149.482 1.00 52.26  ? 48  VAL A CB  1 
ATOM   374  C CG1 . VAL A 1 76  ? 194.143 129.005 150.857 1.00 48.58  ? 48  VAL A CG1 1 
ATOM   375  C CG2 . VAL A 1 76  ? 196.132 128.938 149.355 1.00 54.21  ? 48  VAL A CG2 1 
ATOM   376  N N   . HIS A 1 77  ? 191.480 128.138 148.662 1.00 58.14  ? 49  HIS A N   1 
ATOM   377  C CA  . HIS A 1 77  ? 190.032 128.466 148.633 1.00 59.61  ? 49  HIS A CA  1 
ATOM   378  C C   . HIS A 1 77  ? 189.640 129.336 149.819 1.00 66.43  ? 49  HIS A C   1 
ATOM   379  O O   . HIS A 1 77  ? 190.212 129.167 150.903 1.00 73.12  ? 49  HIS A O   1 
ATOM   380  C CB  . HIS A 1 77  ? 189.189 127.196 148.540 1.00 62.85  ? 49  HIS A CB  1 
ATOM   381  C CG  . HIS A 1 77  ? 189.336 126.465 147.251 1.00 74.15  ? 49  HIS A CG  1 
ATOM   382  N ND1 . HIS A 1 77  ? 188.260 126.284 146.410 1.00 76.03  ? 49  HIS A ND1 1 
ATOM   383  C CD2 . HIS A 1 77  ? 190.384 125.904 146.643 1.00 74.15  ? 49  HIS A CD2 1 
ATOM   384  C CE1 . HIS A 1 77  ? 188.655 125.623 145.335 1.00 73.86  ? 49  HIS A CE1 1 
ATOM   385  N NE2 . HIS A 1 77  ? 189.941 125.385 145.457 1.00 73.13  ? 49  HIS A NE2 1 
ATOM   386  N N   . GLU A 1 78  ? 188.667 130.217 149.605 1.00 64.22  ? 50  GLU A N   1 
ATOM   387  C CA  . GLU A 1 78  ? 188.205 131.154 150.656 1.00 57.71  ? 50  GLU A CA  1 
ATOM   388  C C   . GLU A 1 78  ? 186.735 130.857 150.943 1.00 62.60  ? 50  GLU A C   1 
ATOM   389  O O   . GLU A 1 78  ? 185.982 130.706 149.975 1.00 71.57  ? 50  GLU A O   1 
ATOM   390  C CB  . GLU A 1 78  ? 188.400 132.579 150.148 1.00 56.00  ? 50  GLU A CB  1 
ATOM   391  C CG  . GLU A 1 78  ? 189.849 132.906 149.843 1.00 60.98  ? 50  GLU A CG  1 
ATOM   392  C CD  . GLU A 1 78  ? 190.080 134.305 149.302 1.00 73.20  ? 50  GLU A CD  1 
ATOM   393  O OE1 . GLU A 1 78  ? 189.744 135.273 150.009 1.00 68.78  ? 50  GLU A OE1 1 
ATOM   394  O OE2 . GLU A 1 78  ? 190.603 134.419 148.179 1.00 75.20  ? 50  GLU A OE2 1 
ATOM   395  N N   . PHE A 1 79  ? 186.336 130.793 152.212 1.00 58.11  ? 51  PHE A N   1 
ATOM   396  C CA  . PHE A 1 79  ? 184.958 130.369 152.551 1.00 59.91  ? 51  PHE A CA  1 
ATOM   397  C C   . PHE A 1 79  ? 184.285 131.422 153.429 1.00 67.65  ? 51  PHE A C   1 
ATOM   398  O O   . PHE A 1 79  ? 184.990 132.098 154.173 1.00 74.40  ? 51  PHE A O   1 
ATOM   399  C CB  . PHE A 1 79  ? 185.042 129.046 153.309 1.00 61.58  ? 51  PHE A CB  1 
ATOM   400  C CG  . PHE A 1 79  ? 185.738 127.923 152.585 1.00 60.38  ? 51  PHE A CG  1 
ATOM   401  C CD1 . PHE A 1 79  ? 185.258 127.439 151.382 1.00 58.44  ? 51  PHE A CD1 1 
ATOM   402  C CD2 . PHE A 1 79  ? 186.895 127.365 153.102 1.00 62.31  ? 51  PHE A CD2 1 
ATOM   403  C CE1 . PHE A 1 79  ? 185.908 126.407 150.724 1.00 61.50  ? 51  PHE A CE1 1 
ATOM   404  C CE2 . PHE A 1 79  ? 187.548 126.338 152.440 1.00 60.93  ? 51  PHE A CE2 1 
ATOM   405  C CZ  . PHE A 1 79  ? 187.051 125.860 151.254 1.00 61.76  ? 51  PHE A CZ  1 
ATOM   406  N N   . PRO A 1 80  ? 182.943 131.564 153.404 1.00 63.38  ? 52  PRO A N   1 
ATOM   407  C CA  . PRO A 1 80  ? 182.250 132.516 154.265 1.00 56.28  ? 52  PRO A CA  1 
ATOM   408  C C   . PRO A 1 80  ? 182.469 132.159 155.736 1.00 57.37  ? 52  PRO A C   1 
ATOM   409  O O   . PRO A 1 80  ? 182.658 131.007 156.006 1.00 67.24  ? 52  PRO A O   1 
ATOM   410  C CB  . PRO A 1 80  ? 180.781 132.279 153.926 1.00 51.10  ? 52  PRO A CB  1 
ATOM   411  C CG  . PRO A 1 80  ? 180.814 131.747 152.519 1.00 57.08  ? 52  PRO A CG  1 
ATOM   412  C CD  . PRO A 1 80  ? 182.034 130.854 152.508 1.00 59.11  ? 52  PRO A CD  1 
ATOM   413  N N   . HIS A 1 81  ? 182.486 133.144 156.635 1.00 50.14  ? 53  HIS A N   1 
ATOM   414  C CA  . HIS A 1 81  ? 182.794 132.849 158.061 1.00 52.89  ? 53  HIS A CA  1 
ATOM   415  C C   . HIS A 1 81  ? 181.480 132.691 158.829 1.00 59.85  ? 53  HIS A C   1 
ATOM   416  O O   . HIS A 1 81  ? 180.564 133.509 158.654 1.00 66.63  ? 53  HIS A O   1 
ATOM   417  C CB  . HIS A 1 81  ? 183.713 133.914 158.670 1.00 55.66  ? 53  HIS A CB  1 
ATOM   418  C CG  . HIS A 1 81  ? 184.212 133.587 160.038 1.00 59.12  ? 53  HIS A CG  1 
ATOM   419  N ND1 . HIS A 1 81  ? 183.407 133.415 161.142 1.00 56.09  ? 53  HIS A ND1 1 
ATOM   420  C CD2 . HIS A 1 81  ? 185.466 133.420 160.469 1.00 59.49  ? 53  HIS A CD2 1 
ATOM   421  C CE1 . HIS A 1 81  ? 184.162 133.139 162.195 1.00 56.24  ? 53  HIS A CE1 1 
ATOM   422  N NE2 . HIS A 1 81  ? 185.416 133.136 161.807 1.00 55.46  ? 53  HIS A NE2 1 
ATOM   423  N N   . PRO A 1 82  ? 181.343 131.649 159.673 1.00 58.52  ? 54  PRO A N   1 
ATOM   424  C CA  . PRO A 1 82  ? 180.104 131.397 160.406 1.00 55.77  ? 54  PRO A CA  1 
ATOM   425  C C   . PRO A 1 82  ? 179.674 132.506 161.379 1.00 59.21  ? 54  PRO A C   1 
ATOM   426  O O   . PRO A 1 82  ? 178.489 132.744 161.461 1.00 64.42  ? 54  PRO A O   1 
ATOM   427  C CB  . PRO A 1 82  ? 180.446 130.136 161.215 1.00 58.14  ? 54  PRO A CB  1 
ATOM   428  C CG  . PRO A 1 82  ? 181.947 130.105 161.279 1.00 54.81  ? 54  PRO A CG  1 
ATOM   429  C CD  . PRO A 1 82  ? 182.364 130.633 159.926 1.00 60.91  ? 54  PRO A CD  1 
ATOM   430  N N   . ASP A 1 83  ? 180.610 133.143 162.090 1.00 65.55  ? 55  ASP A N   1 
ATOM   431  C CA  . ASP A 1 83  ? 180.259 134.144 163.137 1.00 73.44  ? 55  ASP A CA  1 
ATOM   432  C C   . ASP A 1 83  ? 180.030 135.552 162.564 1.00 75.76  ? 55  ASP A C   1 
ATOM   433  O O   . ASP A 1 83  ? 179.098 136.213 163.038 1.00 76.41  ? 55  ASP A O   1 
ATOM   434  C CB  . ASP A 1 83  ? 181.339 134.181 164.218 1.00 72.97  ? 55  ASP A CB  1 
ATOM   435  C CG  . ASP A 1 83  ? 181.541 132.856 164.928 1.00 72.01  ? 55  ASP A CG  1 
ATOM   436  O OD1 . ASP A 1 83  ? 180.832 131.894 164.583 1.00 73.25  ? 55  ASP A OD1 1 
ATOM   437  O OD2 . ASP A 1 83  ? 182.414 132.796 165.813 1.00 74.97  ? 55  ASP A OD2 1 
ATOM   438  N N   . ILE A 1 84  ? 180.852 136.013 161.616 1.00 69.12  ? 56  ILE A N   1 
ATOM   439  C CA  . ILE A 1 84  ? 180.745 137.409 161.080 1.00 64.99  ? 56  ILE A CA  1 
ATOM   440  C C   . ILE A 1 84  ? 179.689 137.465 159.973 1.00 68.44  ? 56  ILE A C   1 
ATOM   441  O O   . ILE A 1 84  ? 179.791 136.669 159.026 1.00 65.01  ? 56  ILE A O   1 
ATOM   442  C CB  . ILE A 1 84  ? 182.111 137.904 160.571 1.00 65.31  ? 56  ILE A CB  1 
ATOM   443  C CG1 . ILE A 1 84  ? 183.204 137.771 161.634 1.00 61.06  ? 56  ILE A CG1 1 
ATOM   444  C CG2 . ILE A 1 84  ? 182.008 139.327 160.046 1.00 67.21  ? 56  ILE A CG2 1 
ATOM   445  C CD1 . ILE A 1 84  ? 182.934 138.557 162.893 1.00 64.86  ? 56  ILE A CD1 1 
ATOM   446  N N   . ASN A 1 85  ? 178.728 138.388 160.083 1.00 85.12  ? 57  ASN A N   1 
ATOM   447  C CA  . ASN A 1 85  ? 177.616 138.487 159.097 1.00 85.33  ? 57  ASN A CA  1 
ATOM   448  C C   . ASN A 1 85  ? 177.830 139.624 158.088 1.00 85.01  ? 57  ASN A C   1 
ATOM   449  O O   . ASN A 1 85  ? 176.941 139.815 157.242 1.00 85.09  ? 57  ASN A O   1 
ATOM   450  C CB  . ASN A 1 85  ? 176.270 138.649 159.805 1.00 85.15  ? 57  ASN A CB  1 
ATOM   451  C CG  . ASN A 1 85  ? 176.218 139.854 160.719 1.00 87.79  ? 57  ASN A CG  1 
ATOM   452  O OD1 . ASN A 1 85  ? 177.196 140.586 160.855 1.00 84.37  ? 57  ASN A OD1 1 
ATOM   453  N ND2 . ASN A 1 85  ? 175.082 140.061 161.364 1.00 88.04  ? 57  ASN A ND2 1 
ATOM   454  N N   . THR A 1 86  ? 178.945 140.349 158.168 1.00 85.45  ? 58  THR A N   1 
ATOM   455  C CA  . THR A 1 86  ? 179.240 141.411 157.170 1.00 82.58  ? 58  THR A CA  1 
ATOM   456  C C   . THR A 1 86  ? 179.208 140.803 155.769 1.00 84.56  ? 58  THR A C   1 
ATOM   457  O O   . THR A 1 86  ? 179.626 139.647 155.628 1.00 90.81  ? 58  THR A O   1 
ATOM   458  C CB  . THR A 1 86  ? 180.585 142.093 157.445 1.00 78.85  ? 58  THR A CB  1 
ATOM   459  O OG1 . THR A 1 86  ? 180.536 142.656 158.755 1.00 86.51  ? 58  THR A OG1 1 
ATOM   460  C CG2 . THR A 1 86  ? 180.918 143.178 156.444 1.00 79.98  ? 58  THR A CG2 1 
ATOM   461  N N   . GLU A 1 87  ? 178.731 141.551 154.779 1.00 88.13  ? 59  GLU A N   1 
ATOM   462  C CA  . GLU A 1 87  ? 178.667 141.082 153.403 1.00 89.46  ? 59  GLU A CA  1 
ATOM   463  C C   . GLU A 1 87  ? 180.038 141.147 152.741 1.00 91.63  ? 59  GLU A C   1 
ATOM   464  O O   . GLU A 1 87  ? 180.863 142.013 153.048 1.00 91.83  ? 59  GLU A O   1 
ATOM   465  C CB  . GLU A 1 87  ? 177.660 141.908 152.604 1.00 90.70  ? 59  GLU A CB  1 
ATOM   466  C CG  . GLU A 1 87  ? 176.990 141.142 151.478 1.00 90.19  ? 59  GLU A CG  1 
ATOM   467  C CD  . GLU A 1 87  ? 176.605 139.733 151.881 1.00 91.85  ? 59  GLU A CD  1 
ATOM   468  O OE1 . GLU A 1 87  ? 175.802 139.579 152.823 1.00 91.63  ? 59  GLU A OE1 1 
ATOM   469  O OE2 . GLU A 1 87  ? 177.110 138.777 151.254 1.00 92.76  ? 59  GLU A OE2 1 
ATOM   470  N N   . ASN A 1 88  ? 180.273 140.210 151.820 1.00 85.81  ? 60  ASN A N   1 
ATOM   471  C CA  . ASN A 1 88  ? 181.529 140.117 151.070 1.00 85.97  ? 60  ASN A CA  1 
ATOM   472  C C   . ASN A 1 88  ? 182.731 139.952 151.997 1.00 84.93  ? 60  ASN A C   1 
ATOM   473  O O   . ASN A 1 88  ? 183.799 140.520 151.764 1.00 86.46  ? 60  ASN A O   1 
ATOM   474  C CB  . ASN A 1 88  ? 181.716 141.327 150.151 1.00 83.22  ? 60  ASN A CB  1 
ATOM   475  C CG  . ASN A 1 88  ? 180.461 141.673 149.380 1.00 84.33  ? 60  ASN A CG  1 
ATOM   476  O OD1 . ASN A 1 88  ? 179.565 142.335 149.898 1.00 84.95  ? 60  ASN A OD1 1 
ATOM   477  N ND2 . ASN A 1 88  ? 180.392 141.227 148.131 1.00 85.22  ? 60  ASN A ND2 1 
ATOM   478  N N   . TYR A 1 89  ? 182.540 139.184 153.073 1.00 62.68  ? 61  TYR A N   1 
ATOM   479  C CA  . TYR A 1 89  ? 183.651 138.901 154.015 1.00 58.29  ? 61  TYR A CA  1 
ATOM   480  C C   . TYR A 1 89  ? 184.040 137.430 153.855 1.00 64.66  ? 61  TYR A C   1 
ATOM   481  O O   . TYR A 1 89  ? 183.241 136.577 154.256 1.00 72.28  ? 61  TYR A O   1 
ATOM   482  C CB  . TYR A 1 89  ? 183.235 139.221 155.451 1.00 56.93  ? 61  TYR A CB  1 
ATOM   483  C CG  . TYR A 1 89  ? 184.318 139.009 156.474 1.00 56.75  ? 61  TYR A CG  1 
ATOM   484  C CD1 . TYR A 1 89  ? 185.507 139.714 156.413 1.00 59.27  ? 61  TYR A CD1 1 
ATOM   485  C CD2 . TYR A 1 89  ? 184.164 138.083 157.488 1.00 59.43  ? 61  TYR A CD2 1 
ATOM   486  C CE1 . TYR A 1 89  ? 186.510 139.517 157.345 1.00 59.53  ? 61  TYR A CE1 1 
ATOM   487  C CE2 . TYR A 1 89  ? 185.158 137.869 158.426 1.00 61.88  ? 61  TYR A CE2 1 
ATOM   488  C CZ  . TYR A 1 89  ? 186.333 138.590 158.354 1.00 61.93  ? 61  TYR A CZ  1 
ATOM   489  O OH  . TYR A 1 89  ? 187.312 138.373 159.286 1.00 62.14  ? 61  TYR A OH  1 
ATOM   490  N N   . PHE A 1 90  ? 185.217 137.149 153.290 1.00 64.95  ? 62  PHE A N   1 
ATOM   491  C CA  . PHE A 1 90  ? 185.635 135.755 153.007 1.00 60.67  ? 62  PHE A CA  1 
ATOM   492  C C   . PHE A 1 90  ? 187.016 135.474 153.594 1.00 59.41  ? 62  PHE A C   1 
ATOM   493  O O   . PHE A 1 90  ? 187.997 136.002 153.061 1.00 67.91  ? 62  PHE A O   1 
ATOM   494  C CB  . PHE A 1 90  ? 185.651 135.488 151.503 1.00 67.69  ? 62  PHE A CB  1 
ATOM   495  C CG  . PHE A 1 90  ? 184.320 135.524 150.799 1.00 69.77  ? 62  PHE A CG  1 
ATOM   496  C CD1 . PHE A 1 90  ? 183.540 136.668 150.786 1.00 66.41  ? 62  PHE A CD1 1 
ATOM   497  C CD2 . PHE A 1 90  ? 183.844 134.401 150.144 1.00 69.53  ? 62  PHE A CD2 1 
ATOM   498  C CE1 . PHE A 1 90  ? 182.318 136.688 150.137 1.00 68.18  ? 62  PHE A CE1 1 
ATOM   499  C CE2 . PHE A 1 90  ? 182.621 134.421 149.495 1.00 69.45  ? 62  PHE A CE2 1 
ATOM   500  C CZ  . PHE A 1 90  ? 181.859 135.565 149.493 1.00 73.68  ? 62  PHE A CZ  1 
ATOM   501  N N   . VAL A 1 91  ? 187.081 134.655 154.639 1.00 47.36  ? 63  VAL A N   1 
ATOM   502  C CA  . VAL A 1 91  ? 188.376 134.258 155.257 1.00 51.65  ? 63  VAL A CA  1 
ATOM   503  C C   . VAL A 1 91  ? 189.029 133.167 154.399 1.00 55.38  ? 63  VAL A C   1 
ATOM   504  O O   . VAL A 1 91  ? 188.328 132.589 153.568 1.00 64.86  ? 63  VAL A O   1 
ATOM   505  C CB  . VAL A 1 91  ? 188.152 133.798 156.706 1.00 53.63  ? 63  VAL A CB  1 
ATOM   506  C CG1 . VAL A 1 91  ? 187.656 134.938 157.580 1.00 53.79  ? 63  VAL A CG1 1 
ATOM   507  C CG2 . VAL A 1 91  ? 187.198 132.619 156.779 1.00 53.49  ? 63  VAL A CG2 1 
ATOM   508  N N   . PRO A 1 92  ? 190.335 132.867 154.555 1.00 42.75  ? 64  PRO A N   1 
ATOM   509  C CA  . PRO A 1 92  ? 191.019 131.873 153.731 1.00 41.42  ? 64  PRO A CA  1 
ATOM   510  C C   . PRO A 1 92  ? 190.950 130.431 154.266 1.00 55.42  ? 64  PRO A C   1 
ATOM   511  O O   . PRO A 1 92  ? 191.689 129.610 153.765 1.00 60.92  ? 64  PRO A O   1 
ATOM   512  C CB  . PRO A 1 92  ? 192.460 132.369 153.815 1.00 37.32  ? 64  PRO A CB  1 
ATOM   513  C CG  . PRO A 1 92  ? 192.582 132.864 155.227 1.00 47.83  ? 64  PRO A CG  1 
ATOM   514  C CD  . PRO A 1 92  ? 191.248 133.521 155.494 1.00 50.46  ? 64  PRO A CD  1 
ATOM   515  N N   . TYR A 1 93  ? 190.127 130.162 155.283 1.00 57.42  ? 65  TYR A N   1 
ATOM   516  C CA  . TYR A 1 93  ? 190.013 128.821 155.912 1.00 44.13  ? 65  TYR A CA  1 
ATOM   517  C C   . TYR A 1 93  ? 188.546 128.542 156.221 1.00 54.79  ? 65  TYR A C   1 
ATOM   518  O O   . TYR A 1 93  ? 187.757 129.489 156.167 1.00 59.48  ? 65  TYR A O   1 
ATOM   519  C CB  . TYR A 1 93  ? 190.808 128.761 157.215 1.00 44.38  ? 65  TYR A CB  1 
ATOM   520  C CG  . TYR A 1 93  ? 190.392 129.739 158.285 1.00 49.46  ? 65  TYR A CG  1 
ATOM   521  C CD1 . TYR A 1 93  ? 190.463 131.105 158.081 1.00 52.22  ? 65  TYR A CD1 1 
ATOM   522  C CD2 . TYR A 1 93  ? 189.902 129.295 159.498 1.00 50.84  ? 65  TYR A CD2 1 
ATOM   523  C CE1 . TYR A 1 93  ? 190.074 132.006 159.057 1.00 47.47  ? 65  TYR A CE1 1 
ATOM   524  C CE2 . TYR A 1 93  ? 189.504 130.181 160.484 1.00 55.72  ? 65  TYR A CE2 1 
ATOM   525  C CZ  . TYR A 1 93  ? 189.591 131.541 160.264 1.00 52.97  ? 65  TYR A CZ  1 
ATOM   526  O OH  . TYR A 1 93  ? 189.198 132.425 161.237 1.00 56.80  ? 65  TYR A OH  1 
ATOM   527  N N   . LEU A 1 94  ? 188.198 127.303 156.578 1.00 54.14  ? 66  LEU A N   1 
ATOM   528  C CA  . LEU A 1 94  ? 186.795 126.963 156.945 1.00 48.85  ? 66  LEU A CA  1 
ATOM   529  C C   . LEU A 1 94  ? 186.696 126.747 158.452 1.00 52.90  ? 66  LEU A C   1 
ATOM   530  O O   . LEU A 1 94  ? 187.337 125.816 158.951 1.00 57.06  ? 66  LEU A O   1 
ATOM   531  C CB  . LEU A 1 94  ? 186.352 125.701 156.206 1.00 47.68  ? 66  LEU A CB  1 
ATOM   532  C CG  . LEU A 1 94  ? 184.913 125.256 156.445 1.00 48.88  ? 66  LEU A CG  1 
ATOM   533  C CD1 . LEU A 1 94  ? 183.944 126.180 155.727 1.00 49.45  ? 66  LEU A CD1 1 
ATOM   534  C CD2 . LEU A 1 94  ? 184.718 123.827 155.972 1.00 44.26  ? 66  LEU A CD2 1 
ATOM   535  N N   . ALA A 1 95  ? 185.915 127.579 159.137 1.00 50.20  ? 67  ALA A N   1 
ATOM   536  C CA  . ALA A 1 95  ? 185.707 127.373 160.579 1.00 47.52  ? 67  ALA A CA  1 
ATOM   537  C C   . ALA A 1 95  ? 184.381 126.645 160.742 1.00 55.00  ? 67  ALA A C   1 
ATOM   538  O O   . ALA A 1 95  ? 183.355 127.192 160.307 1.00 57.85  ? 67  ALA A O   1 
ATOM   539  C CB  . ALA A 1 95  ? 185.680 128.692 161.281 1.00 50.96  ? 67  ALA A CB  1 
ATOM   540  N N   . THR A 1 96  ? 184.409 125.467 161.353 1.00 56.11  ? 68  THR A N   1 
ATOM   541  C CA  . THR A 1 96  ? 183.185 124.644 161.501 1.00 56.14  ? 68  THR A CA  1 
ATOM   542  C C   . THR A 1 96  ? 182.975 124.419 162.994 1.00 65.62  ? 68  THR A C   1 
ATOM   543  O O   . THR A 1 96  ? 183.966 124.512 163.733 1.00 64.25  ? 68  THR A O   1 
ATOM   544  C CB  . THR A 1 96  ? 183.348 123.317 160.762 1.00 52.73  ? 68  THR A CB  1 
ATOM   545  O OG1 . THR A 1 96  ? 184.470 122.642 161.327 1.00 57.56  ? 68  THR A OG1 1 
ATOM   546  C CG2 . THR A 1 96  ? 183.563 123.485 159.276 1.00 57.91  ? 68  THR A CG2 1 
ATOM   547  N N   . PRO A 1 97  ? 181.755 124.124 163.478 1.00 68.20  ? 69  PRO A N   1 
ATOM   548  C CA  . PRO A 1 97  ? 181.542 123.989 164.908 1.00 64.10  ? 69  PRO A CA  1 
ATOM   549  C C   . PRO A 1 97  ? 182.447 122.885 165.471 1.00 66.48  ? 69  PRO A C   1 
ATOM   550  O O   . PRO A 1 97  ? 182.716 122.921 166.648 1.00 70.47  ? 69  PRO A O   1 
ATOM   551  C CB  . PRO A 1 97  ? 180.067 123.611 164.988 1.00 58.39  ? 69  PRO A CB  1 
ATOM   552  C CG  . PRO A 1 97  ? 179.467 124.228 163.753 1.00 61.09  ? 69  PRO A CG  1 
ATOM   553  C CD  . PRO A 1 97  ? 180.526 124.010 162.697 1.00 62.02  ? 69  PRO A CD  1 
ATOM   554  N N   . GLU A 1 98  ? 182.928 121.980 164.615 1.00 66.41  ? 70  GLU A N   1 
ATOM   555  C CA  . GLU A 1 98  ? 183.754 120.829 165.076 1.00 68.22  ? 70  GLU A CA  1 
ATOM   556  C C   . GLU A 1 98  ? 185.260 121.109 164.939 1.00 70.36  ? 70  GLU A C   1 
ATOM   557  O O   . GLU A 1 98  ? 186.047 120.248 165.358 1.00 72.40  ? 70  GLU A O   1 
ATOM   558  C CB  . GLU A 1 98  ? 183.382 119.544 164.329 1.00 66.65  ? 70  GLU A CB  1 
ATOM   559  C CG  . GLU A 1 98  ? 182.001 118.991 164.644 1.00 68.04  ? 70  GLU A CG  1 
ATOM   560  C CD  . GLU A 1 98  ? 180.775 119.778 164.215 1.00 75.59  ? 70  GLU A CD  1 
ATOM   561  O OE1 . GLU A 1 98  ? 179.655 119.316 164.500 1.00 79.74  ? 70  GLU A OE1 1 
ATOM   562  O OE2 . GLU A 1 98  ? 180.935 120.815 163.553 1.00 71.53  ? 70  GLU A OE2 1 
ATOM   563  N N   . GLY A 1 99  ? 185.657 122.245 164.359 1.00 54.61  ? 71  GLY A N   1 
ATOM   564  C CA  . GLY A 1 99  ? 187.099 122.509 164.173 1.00 60.54  ? 71  GLY A CA  1 
ATOM   565  C C   . GLY A 1 99  ? 187.429 123.386 162.975 1.00 66.97  ? 71  GLY A C   1 
ATOM   566  O O   . GLY A 1 99  ? 186.555 124.166 162.580 1.00 70.28  ? 71  GLY A O   1 
ATOM   567  N N   . TYR A 1 100 ? 188.641 123.262 162.411 1.00 55.29  ? 72  TYR A N   1 
ATOM   568  C CA  . TYR A 1 100 ? 189.082 124.122 161.279 1.00 52.40  ? 72  TYR A CA  1 
ATOM   569  C C   . TYR A 1 100 ? 189.540 123.299 160.074 1.00 53.97  ? 72  TYR A C   1 
ATOM   570  O O   . TYR A 1 100 ? 190.191 122.275 160.294 1.00 66.99  ? 72  TYR A O   1 
ATOM   571  C CB  . TYR A 1 100 ? 190.215 125.033 161.743 1.00 57.29  ? 72  TYR A CB  1 
ATOM   572  C CG  . TYR A 1 100 ? 189.807 126.102 162.722 1.00 58.60  ? 72  TYR A CG  1 
ATOM   573  C CD1 . TYR A 1 100 ? 188.887 127.073 162.368 1.00 49.29  ? 72  TYR A CD1 1 
ATOM   574  C CD2 . TYR A 1 100 ? 190.307 126.125 164.012 1.00 64.96  ? 72  TYR A CD2 1 
ATOM   575  C CE1 . TYR A 1 100 ? 188.498 128.059 163.257 1.00 56.67  ? 72  TYR A CE1 1 
ATOM   576  C CE2 . TYR A 1 100 ? 189.919 127.096 164.917 1.00 63.12  ? 72  TYR A CE2 1 
ATOM   577  C CZ  . TYR A 1 100 ? 189.016 128.070 164.536 1.00 59.93  ? 72  TYR A CZ  1 
ATOM   578  O OH  . TYR A 1 100 ? 188.631 129.039 165.425 1.00 61.62  ? 72  TYR A OH  1 
ATOM   579  N N   . PHE A 1 101 ? 189.247 123.757 158.852 1.00 39.34  ? 73  PHE A N   1 
ATOM   580  C CA  . PHE A 1 101 ? 189.613 123.066 157.625 1.00 33.96  ? 73  PHE A CA  1 
ATOM   581  C C   . PHE A 1 101 ? 190.253 124.048 156.656 1.00 42.95  ? 73  PHE A C   1 
ATOM   582  O O   . PHE A 1 101 ? 189.913 125.232 156.634 1.00 58.72  ? 73  PHE A O   1 
ATOM   583  C CB  . PHE A 1 101 ? 188.392 122.415 156.956 1.00 42.47  ? 73  PHE A CB  1 
ATOM   584  C CG  . PHE A 1 101 ? 188.130 121.002 157.396 1.00 50.00  ? 73  PHE A CG  1 
ATOM   585  C CD1 . PHE A 1 101 ? 188.703 119.935 156.725 1.00 47.05  ? 73  PHE A CD1 1 
ATOM   586  C CD2 . PHE A 1 101 ? 187.300 120.739 158.471 1.00 43.47  ? 73  PHE A CD2 1 
ATOM   587  C CE1 . PHE A 1 101 ? 188.460 118.638 157.121 1.00 38.72  ? 73  PHE A CE1 1 
ATOM   588  C CE2 . PHE A 1 101 ? 187.055 119.442 158.871 1.00 40.96  ? 73  PHE A CE2 1 
ATOM   589  C CZ  . PHE A 1 101 ? 187.636 118.391 158.195 1.00 42.42  ? 73  PHE A CZ  1 
ATOM   590  N N   . VAL A 1 102 ? 191.190 123.543 155.850 1.00 48.02  ? 74  VAL A N   1 
ATOM   591  C CA  . VAL A 1 102 ? 191.834 124.322 154.802 1.00 48.42  ? 74  VAL A CA  1 
ATOM   592  C C   . VAL A 1 102 ? 191.746 123.540 153.498 1.00 53.20  ? 74  VAL A C   1 
ATOM   593  O O   . VAL A 1 102 ? 191.589 122.317 153.489 1.00 72.01  ? 74  VAL A O   1 
ATOM   594  C CB  . VAL A 1 102 ? 193.308 124.660 155.128 1.00 36.36  ? 74  VAL A CB  1 
ATOM   595  C CG1 . VAL A 1 102 ? 193.424 125.278 156.510 1.00 46.89  ? 74  VAL A CG1 1 
ATOM   596  C CG2 . VAL A 1 102 ? 194.179 123.424 155.016 1.00 38.76  ? 74  VAL A CG2 1 
ATOM   597  N N   . GLN A 1 103 ? 191.845 124.263 152.386 1.00 53.01  ? 75  GLN A N   1 
ATOM   598  C CA  . GLN A 1 103 ? 191.774 123.657 151.065 1.00 54.68  ? 75  GLN A CA  1 
ATOM   599  C C   . GLN A 1 103 ? 192.775 124.330 150.138 1.00 58.26  ? 75  GLN A C   1 
ATOM   600  O O   . GLN A 1 103 ? 192.910 125.555 150.146 1.00 75.44  ? 75  GLN A O   1 
ATOM   601  C CB  . GLN A 1 103 ? 190.363 123.763 150.478 1.00 57.45  ? 75  GLN A CB  1 
ATOM   602  C CG  . GLN A 1 103 ? 190.058 122.729 149.413 1.00 59.45  ? 75  GLN A CG  1 
ATOM   603  C CD  . GLN A 1 103 ? 188.654 122.858 148.861 1.00 68.58  ? 75  GLN A CD  1 
ATOM   604  O OE1 . GLN A 1 103 ? 188.179 123.960 148.595 1.00 72.22  ? 75  GLN A OE1 1 
ATOM   605  N NE2 . GLN A 1 103 ? 187.980 121.730 148.690 1.00 66.13  ? 75  GLN A NE2 1 
ATOM   606  N N   . VAL A 1 104 ? 193.473 123.523 149.343 1.00 59.78  ? 76  VAL A N   1 
ATOM   607  C CA  . VAL A 1 104 ? 194.464 124.016 148.392 1.00 58.95  ? 76  VAL A CA  1 
ATOM   608  C C   . VAL A 1 104 ? 194.277 123.275 147.077 1.00 68.79  ? 76  VAL A C   1 
ATOM   609  O O   . VAL A 1 104 ? 194.175 122.043 147.064 1.00 84.89  ? 76  VAL A O   1 
ATOM   610  C CB  . VAL A 1 104 ? 195.902 123.832 148.916 1.00 62.04  ? 76  VAL A CB  1 
ATOM   611  C CG1 . VAL A 1 104 ? 196.910 124.124 147.820 1.00 66.80  ? 76  VAL A CG1 1 
ATOM   612  C CG2 . VAL A 1 104 ? 196.149 124.728 150.116 1.00 65.59  ? 76  VAL A CG2 1 
ATOM   613  N N   . SER A 1 105 ? 194.212 124.025 145.973 1.00 58.81  ? 77  SER A N   1 
ATOM   614  C CA  . SER A 1 105 ? 194.050 123.424 144.623 1.00 65.46  ? 77  SER A CA  1 
ATOM   615  C C   . SER A 1 105 ? 195.269 123.724 143.752 1.00 68.02  ? 77  SER A C   1 
ATOM   616  O O   . SER A 1 105 ? 195.447 124.887 143.385 1.00 72.85  ? 77  SER A O   1 
ATOM   617  C CB  . SER A 1 105 ? 192.793 123.903 143.970 1.00 66.15  ? 77  SER A CB  1 
ATOM   618  O OG  . SER A 1 105 ? 191.663 123.498 144.724 1.00 67.72  ? 77  SER A OG  1 
ATOM   619  N N   . VAL A 1 106 ? 196.042 122.706 143.394 1.00 80.58  ? 78  VAL A N   1 
ATOM   620  C CA  . VAL A 1 106 ? 197.271 122.846 142.623 1.00 83.09  ? 78  VAL A CA  1 
ATOM   621  C C   . VAL A 1 106 ? 196.998 122.386 141.197 1.00 86.08  ? 78  VAL A C   1 
ATOM   622  O O   . VAL A 1 106 ? 196.609 121.235 140.971 1.00 88.85  ? 78  VAL A O   1 
ATOM   623  C CB  . VAL A 1 106 ? 198.421 122.043 143.250 1.00 82.33  ? 78  VAL A CB  1 
ATOM   624  C CG1 . VAL A 1 106 ? 199.655 122.109 142.370 1.00 81.88  ? 78  VAL A CG1 1 
ATOM   625  C CG2 . VAL A 1 106 ? 198.729 122.565 144.639 1.00 84.28  ? 78  VAL A CG2 1 
ATOM   626  N N   . THR A 1 107 ? 197.199 123.283 140.228 1.00 99.09  ? 79  THR A N   1 
ATOM   627  C CA  . THR A 1 107 ? 196.949 122.945 138.805 1.00 98.13  ? 79  THR A CA  1 
ATOM   628  C C   . THR A 1 107 ? 198.267 122.920 138.037 1.00 98.19  ? 79  THR A C   1 
ATOM   629  O O   . THR A 1 107 ? 198.872 123.990 137.893 1.00 99.36  ? 79  THR A O   1 
ATOM   630  C CB  . THR A 1 107 ? 196.039 123.979 138.139 1.00 98.37  ? 79  THR A CB  1 
ATOM   631  O OG1 . THR A 1 107 ? 194.839 124.074 138.906 1.00 100.17 ? 79  THR A OG1 1 
ATOM   632  C CG2 . THR A 1 107 ? 195.719 123.640 136.699 1.00 96.59  ? 79  THR A CG2 1 
ATOM   633  N N   . VAL A 1 108 ? 198.698 121.750 137.570 1.00 106.38 ? 80  VAL A N   1 
ATOM   634  C CA  . VAL A 1 108 ? 199.921 121.686 136.720 1.00 109.02 ? 80  VAL A CA  1 
ATOM   635  C C   . VAL A 1 108 ? 199.526 121.150 135.342 1.00 110.87 ? 80  VAL A C   1 
ATOM   636  O O   . VAL A 1 108 ? 198.974 120.038 135.286 1.00 113.61 ? 80  VAL A O   1 
ATOM   637  C CB  . VAL A 1 108 ? 201.017 120.819 137.367 1.00 108.71 ? 80  VAL A CB  1 
ATOM   638  C CG1 . VAL A 1 108 ? 202.210 120.630 136.444 1.00 107.90 ? 80  VAL A CG1 1 
ATOM   639  C CG2 . VAL A 1 108 ? 201.459 121.373 138.712 1.00 110.14 ? 80  VAL A CG2 1 
ATOM   640  N N   . LYS A 1 109 ? 199.817 121.896 134.275 1.00 117.09 ? 81  LYS A N   1 
ATOM   641  C CA  . LYS A 1 109 ? 199.537 121.431 132.888 1.00 117.33 ? 81  LYS A CA  1 
ATOM   642  C C   . LYS A 1 109 ? 198.052 121.075 132.722 1.00 120.08 ? 81  LYS A C   1 
ATOM   643  O O   . LYS A 1 109 ? 197.769 119.989 132.187 1.00 121.59 ? 81  LYS A O   1 
ATOM   644  C CB  . LYS A 1 109 ? 200.495 120.284 132.540 1.00 119.05 ? 81  LYS A CB  1 
ATOM   645  C CG  . LYS A 1 109 ? 200.494 119.813 131.092 1.00 118.83 ? 81  LYS A CG  1 
ATOM   646  C CD  . LYS A 1 109 ? 201.485 118.697 130.859 1.00 119.13 ? 81  LYS A CD  1 
ATOM   647  C CE  . LYS A 1 109 ? 202.897 119.086 131.242 1.00 118.66 ? 81  LYS A CE  1 
ATOM   648  N NZ  . LYS A 1 109 ? 203.371 120.267 130.480 1.00 118.56 ? 81  LYS A NZ  1 
ATOM   649  N N   . ASP A 1 110 ? 197.144 121.957 133.146 1.00 130.43 ? 82  ASP A N   1 
ATOM   650  C CA  . ASP A 1 110 ? 195.678 121.770 132.922 1.00 133.07 ? 82  ASP A CA  1 
ATOM   651  C C   . ASP A 1 110 ? 195.079 120.615 133.738 1.00 132.74 ? 82  ASP A C   1 
ATOM   652  O O   . ASP A 1 110 ? 193.970 120.183 133.381 1.00 130.23 ? 82  ASP A O   1 
ATOM   653  C CB  . ASP A 1 110 ? 195.359 121.619 131.432 1.00 133.80 ? 82  ASP A CB  1 
ATOM   654  C CG  . ASP A 1 110 ? 195.786 122.820 130.605 1.00 134.23 ? 82  ASP A CG  1 
ATOM   655  O OD1 . ASP A 1 110 ? 196.335 123.773 131.195 1.00 133.37 ? 82  ASP A OD1 1 
ATOM   656  O OD2 . ASP A 1 110 ? 195.565 122.794 129.379 1.00 133.30 ? 82  ASP A OD2 1 
ATOM   657  N N   . SER A 1 111 ? 195.751 120.145 134.791 1.00 124.96 ? 83  SER A N   1 
ATOM   658  C CA  . SER A 1 111 ? 195.157 119.102 135.669 1.00 121.02 ? 83  SER A CA  1 
ATOM   659  C C   . SER A 1 111 ? 195.066 119.649 137.095 1.00 122.68 ? 83  SER A C   1 
ATOM   660  O O   . SER A 1 111 ? 196.102 120.108 137.599 1.00 122.64 ? 83  SER A O   1 
ATOM   661  C CB  . SER A 1 111 ? 195.968 117.841 135.635 1.00 119.92 ? 83  SER A CB  1 
ATOM   662  O OG  . SER A 1 111 ? 197.283 118.070 136.117 1.00 123.24 ? 83  SER A OG  1 
ATOM   663  N N   . THR A 1 112 ? 193.895 119.567 137.736 1.00 101.09 ? 84  THR A N   1 
ATOM   664  C CA  . THR A 1 112 ? 193.740 120.188 139.081 1.00 98.28  ? 84  THR A CA  1 
ATOM   665  C C   . THR A 1 112 ? 193.592 119.120 140.168 1.00 95.28  ? 84  THR A C   1 
ATOM   666  O O   . THR A 1 112 ? 192.722 118.254 140.018 1.00 99.58  ? 84  THR A O   1 
ATOM   667  C CB  . THR A 1 112 ? 192.574 121.179 139.076 1.00 99.67  ? 84  THR A CB  1 
ATOM   668  O OG1 . THR A 1 112 ? 192.450 121.685 140.405 1.00 100.58 ? 84  THR A OG1 1 
ATOM   669  C CG2 . THR A 1 112 ? 191.263 120.560 138.647 1.00 99.92  ? 84  THR A CG2 1 
ATOM   670  N N   . GLU A 1 113 ? 194.422 119.176 141.211 1.00 89.57  ? 85  GLU A N   1 
ATOM   671  C CA  . GLU A 1 113 ? 194.282 118.232 142.352 1.00 89.91  ? 85  GLU A CA  1 
ATOM   672  C C   . GLU A 1 113 ? 193.939 119.015 143.621 1.00 88.95  ? 85  GLU A C   1 
ATOM   673  O O   . GLU A 1 113 ? 194.830 119.697 144.141 1.00 95.15  ? 85  GLU A O   1 
ATOM   674  C CB  . GLU A 1 113 ? 195.584 117.470 142.567 1.00 92.64  ? 85  GLU A CB  1 
ATOM   675  C CG  . GLU A 1 113 ? 196.012 116.643 141.373 1.00 93.00  ? 85  GLU A CG  1 
ATOM   676  C CD  . GLU A 1 113 ? 195.035 115.549 140.982 1.00 95.19  ? 85  GLU A CD  1 
ATOM   677  O OE1 . GLU A 1 113 ? 194.540 115.583 139.839 1.00 92.47  ? 85  GLU A OE1 1 
ATOM   678  O OE2 . GLU A 1 113 ? 194.777 114.666 141.821 1.00 97.51  ? 85  GLU A OE2 1 
ATOM   679  N N   . THR A 1 114 ? 192.710 118.883 144.120 1.00 70.51  ? 86  THR A N   1 
ATOM   680  C CA  . THR A 1 114 ? 192.277 119.598 145.345 1.00 70.69  ? 86  THR A CA  1 
ATOM   681  C C   . THR A 1 114 ? 192.676 118.771 146.563 1.00 70.28  ? 86  THR A C   1 
ATOM   682  O O   . THR A 1 114 ? 192.887 117.566 146.393 1.00 84.18  ? 86  THR A O   1 
ATOM   683  C CB  . THR A 1 114 ? 190.772 119.872 145.295 1.00 79.55  ? 86  THR A CB  1 
ATOM   684  O OG1 . THR A 1 114 ? 190.509 120.614 144.105 1.00 83.52  ? 86  THR A OG1 1 
ATOM   685  C CG2 . THR A 1 114 ? 190.258 120.631 146.498 1.00 78.51  ? 86  THR A CG2 1 
ATOM   686  N N   . GLU A 1 115 ? 192.798 119.395 147.730 1.00 51.23  ? 87  GLU A N   1 
ATOM   687  C CA  . GLU A 1 115 ? 193.110 118.627 148.956 1.00 53.06  ? 87  GLU A CA  1 
ATOM   688  C C   . GLU A 1 115 ? 192.502 119.342 150.160 1.00 54.39  ? 87  GLU A C   1 
ATOM   689  O O   . GLU A 1 115 ? 192.351 120.558 150.084 1.00 65.37  ? 87  GLU A O   1 
ATOM   690  C CB  . GLU A 1 115 ? 194.622 118.498 149.095 1.00 56.28  ? 87  GLU A CB  1 
ATOM   691  C CG  . GLU A 1 115 ? 195.082 117.610 150.235 1.00 62.84  ? 87  GLU A CG  1 
ATOM   692  C CD  . GLU A 1 115 ? 194.774 116.131 150.074 1.00 69.95  ? 87  GLU A CD  1 
ATOM   693  O OE1 . GLU A 1 115 ? 194.191 115.753 149.039 1.00 73.25  ? 87  GLU A OE1 1 
ATOM   694  O OE2 . GLU A 1 115 ? 195.118 115.359 150.988 1.00 70.79  ? 87  GLU A OE2 1 
ATOM   695  N N   . TRP A 1 116 ? 192.171 118.611 151.218 1.00 42.89  ? 88  TRP A N   1 
ATOM   696  C CA  . TRP A 1 116 ? 191.606 119.179 152.463 1.00 44.60  ? 88  TRP A CA  1 
ATOM   697  C C   . TRP A 1 116 ? 192.575 118.819 153.575 1.00 43.92  ? 88  TRP A C   1 
ATOM   698  O O   . TRP A 1 116 ? 193.322 117.859 153.384 1.00 59.94  ? 88  TRP A O   1 
ATOM   699  C CB  . TRP A 1 116 ? 190.247 118.541 152.765 1.00 47.00  ? 88  TRP A CB  1 
ATOM   700  C CG  . TRP A 1 116 ? 189.034 119.006 152.024 1.00 42.30  ? 88  TRP A CG  1 
ATOM   701  C CD1 . TRP A 1 116 ? 188.275 118.274 151.160 1.00 45.26  ? 88  TRP A CD1 1 
ATOM   702  C CD2 . TRP A 1 116 ? 188.299 120.217 152.266 1.00 46.34  ? 88  TRP A CD2 1 
ATOM   703  N NE1 . TRP A 1 116 ? 187.188 118.997 150.753 1.00 49.37  ? 88  TRP A NE1 1 
ATOM   704  C CE2 . TRP A 1 116 ? 187.168 120.188 151.424 1.00 52.18  ? 88  TRP A CE2 1 
ATOM   705  C CE3 . TRP A 1 116 ? 188.507 121.341 153.070 1.00 51.90  ? 88  TRP A CE3 1 
ATOM   706  C CZ2 . TRP A 1 116 ? 186.260 121.243 151.363 1.00 52.17  ? 88  TRP A CZ2 1 
ATOM   707  C CZ3 . TRP A 1 116 ? 187.609 122.381 153.010 1.00 51.84  ? 88  TRP A CZ3 1 
ATOM   708  C CH2 . TRP A 1 116 ? 186.501 122.332 152.167 1.00 48.25  ? 88  TRP A CH2 1 
ATOM   709  N N   . LEU A 1 117 ? 192.571 119.551 154.680 1.00 37.00  ? 89  LEU A N   1 
ATOM   710  C CA  . LEU A 1 117 ? 193.403 119.100 155.818 1.00 39.95  ? 89  LEU A CA  1 
ATOM   711  C C   . LEU A 1 117 ? 192.858 119.711 157.102 1.00 45.39  ? 89  LEU A C   1 
ATOM   712  O O   . LEU A 1 117 ? 192.320 120.814 157.032 1.00 59.69  ? 89  LEU A O   1 
ATOM   713  C CB  . LEU A 1 117 ? 194.851 119.524 155.551 1.00 46.85  ? 89  LEU A CB  1 
ATOM   714  C CG  . LEU A 1 117 ? 195.901 119.062 156.557 1.00 53.68  ? 89  LEU A CG  1 
ATOM   715  C CD1 . LEU A 1 117 ? 196.239 117.598 156.334 1.00 54.67  ? 89  LEU A CD1 1 
ATOM   716  C CD2 . LEU A 1 117 ? 197.154 119.916 156.455 1.00 53.74  ? 89  LEU A CD2 1 
ATOM   717  N N   . PRO A 1 118 ? 192.951 119.065 158.283 1.00 37.38  ? 90  PRO A N   1 
ATOM   718  C CA  . PRO A 1 118 ? 192.543 119.720 159.515 1.00 47.09  ? 90  PRO A CA  1 
ATOM   719  C C   . PRO A 1 118 ? 193.672 120.600 160.065 1.00 57.92  ? 90  PRO A C   1 
ATOM   720  O O   . PRO A 1 118 ? 194.802 120.177 159.992 1.00 64.66  ? 90  PRO A O   1 
ATOM   721  C CB  . PRO A 1 118 ? 192.349 118.547 160.470 1.00 47.88  ? 90  PRO A CB  1 
ATOM   722  C CG  . PRO A 1 118 ? 193.349 117.522 160.013 1.00 51.28  ? 90  PRO A CG  1 
ATOM   723  C CD  . PRO A 1 118 ? 193.364 117.671 158.509 1.00 49.43  ? 90  PRO A CD  1 
ATOM   724  N N   . VAL A 1 119 ? 193.366 121.799 160.573 1.00 59.89  ? 91  VAL A N   1 
ATOM   725  C CA  . VAL A 1 119 ? 194.421 122.626 161.228 1.00 56.66  ? 91  VAL A CA  1 
ATOM   726  C C   . VAL A 1 119 ? 194.780 121.913 162.533 1.00 65.84  ? 91  VAL A C   1 
ATOM   727  O O   . VAL A 1 119 ? 193.843 121.540 163.249 1.00 70.77  ? 91  VAL A O   1 
ATOM   728  C CB  . VAL A 1 119 ? 193.932 124.064 161.463 1.00 49.39  ? 91  VAL A CB  1 
ATOM   729  C CG1 . VAL A 1 119 ? 194.938 124.887 162.247 1.00 57.80  ? 91  VAL A CG1 1 
ATOM   730  C CG2 . VAL A 1 119 ? 193.572 124.749 160.156 1.00 54.03  ? 91  VAL A CG2 1 
ATOM   731  N N   . LEU A 1 120 ? 196.067 121.749 162.845 1.00 85.14  ? 92  LEU A N   1 
ATOM   732  C CA  . LEU A 1 120 ? 196.475 120.955 164.039 1.00 84.26  ? 92  LEU A CA  1 
ATOM   733  C C   . LEU A 1 120 ? 197.510 121.704 164.889 1.00 88.64  ? 92  LEU A C   1 
ATOM   734  O O   . LEU A 1 120 ? 198.161 122.613 164.348 1.00 87.28  ? 92  LEU A O   1 
ATOM   735  C CB  . LEU A 1 120 ? 197.054 119.618 163.566 1.00 79.69  ? 92  LEU A CB  1 
ATOM   736  C CG  . LEU A 1 120 ? 196.099 118.667 162.850 1.00 78.36  ? 92  LEU A CG  1 
ATOM   737  C CD1 . LEU A 1 120 ? 196.739 117.296 162.703 1.00 83.12  ? 92  LEU A CD1 1 
ATOM   738  C CD2 . LEU A 1 120 ? 194.793 118.544 163.617 1.00 83.16  ? 92  LEU A CD2 1 
ATOM   739  N N   . ASP A 1 121 ? 197.674 121.292 166.156 1.00 112.89 ? 93  ASP A N   1 
ATOM   740  C CA  . ASP A 1 121 ? 198.671 121.922 167.064 1.00 111.97 ? 93  ASP A CA  1 
ATOM   741  C C   . ASP A 1 121 ? 200.093 121.525 166.673 1.00 115.85 ? 93  ASP A C   1 
ATOM   742  O O   . ASP A 1 121 ? 200.255 120.772 165.691 1.00 115.44 ? 93  ASP A O   1 
ATOM   743  C CB  . ASP A 1 121 ? 198.563 121.442 168.512 1.00 110.49 ? 93  ASP A CB  1 
ATOM   744  C CG  . ASP A 1 121 ? 197.254 121.725 169.224 1.00 114.89 ? 93  ASP A CG  1 
ATOM   745  O OD1 . ASP A 1 121 ? 196.216 121.235 168.758 1.00 115.48 ? 93  ASP A OD1 1 
ATOM   746  O OD2 . ASP A 1 121 ? 197.291 122.427 170.253 1.00 116.76 ? 93  ASP A OD2 1 
ATOM   747  N N   . PHE A 1 122 ? 201.080 121.994 167.439 1.00 130.62 ? 94  PHE A N   1 
ATOM   748  C CA  . PHE A 1 122 ? 202.488 121.576 167.204 1.00 130.37 ? 94  PHE A CA  1 
ATOM   749  C C   . PHE A 1 122 ? 202.643 120.097 167.584 1.00 128.88 ? 94  PHE A C   1 
ATOM   750  O O   . PHE A 1 122 ? 203.594 119.451 167.114 1.00 128.72 ? 94  PHE A O   1 
ATOM   751  C CB  . PHE A 1 122 ? 203.460 122.478 167.968 1.00 130.23 ? 94  PHE A CB  1 
ATOM   752  C CG  . PHE A 1 122 ? 203.316 122.485 169.470 1.00 132.54 ? 94  PHE A CG  1 
ATOM   753  C CD1 . PHE A 1 122 ? 202.135 122.881 170.079 1.00 131.78 ? 94  PHE A CD1 1 
ATOM   754  C CD2 . PHE A 1 122 ? 204.372 122.106 170.279 1.00 132.13 ? 94  PHE A CD2 1 
ATOM   755  C CE1 . PHE A 1 122 ? 202.015 122.889 171.459 1.00 130.77 ? 94  PHE A CE1 1 
ATOM   756  C CE2 . PHE A 1 122 ? 204.251 122.114 171.660 1.00 131.91 ? 94  PHE A CE2 1 
ATOM   757  C CZ  . PHE A 1 122 ? 203.072 122.505 172.248 1.00 131.13 ? 94  PHE A CZ  1 
ATOM   758  N N   . ARG A 1 123 ? 201.747 119.590 168.432 1.00 122.35 ? 95  ARG A N   1 
ATOM   759  C CA  . ARG A 1 123 ? 201.823 118.180 168.892 1.00 122.84 ? 95  ARG A CA  1 
ATOM   760  C C   . ARG A 1 123 ? 200.920 117.311 168.013 1.00 122.84 ? 95  ARG A C   1 
ATOM   761  O O   . ARG A 1 123 ? 200.653 116.166 168.413 1.00 123.50 ? 95  ARG A O   1 
ATOM   762  C CB  . ARG A 1 123 ? 201.380 118.052 170.352 1.00 124.19 ? 95  ARG A CB  1 
ATOM   763  C CG  . ARG A 1 123 ? 202.155 118.915 171.334 1.00 123.12 ? 95  ARG A CG  1 
ATOM   764  C CD  . ARG A 1 123 ? 201.678 118.605 172.739 1.00 124.55 ? 95  ARG A CD  1 
ATOM   765  N NE  . ARG A 1 123 ? 200.242 118.790 172.892 1.00 128.00 ? 95  ARG A NE  1 
ATOM   766  C CZ  . ARG A 1 123 ? 199.572 118.576 174.019 1.00 126.43 ? 95  ARG A CZ  1 
ATOM   767  N NH1 . ARG A 1 123 ? 200.216 118.200 175.110 1.00 125.22 ? 95  ARG A NH1 1 
ATOM   768  N NH2 . ARG A 1 123 ? 198.260 118.736 174.051 1.00 122.99 ? 95  ARG A NH2 1 
ATOM   769  N N   . ASN A 1 124 ? 200.459 117.838 166.876 1.00 117.23 ? 96  ASN A N   1 
ATOM   770  C CA  . ASN A 1 124 ? 199.514 117.090 166.003 1.00 118.40 ? 96  ASN A CA  1 
ATOM   771  C C   . ASN A 1 124 ? 198.241 116.729 166.778 1.00 120.09 ? 96  ASN A C   1 
ATOM   772  O O   . ASN A 1 124 ? 197.849 115.550 166.752 1.00 119.44 ? 96  ASN A O   1 
ATOM   773  C CB  . ASN A 1 124 ? 200.184 115.896 165.317 1.00 119.72 ? 96  ASN A CB  1 
ATOM   774  C CG  . ASN A 1 124 ? 201.265 116.326 164.350 1.00 119.60 ? 96  ASN A CG  1 
ATOM   775  O OD1 . ASN A 1 124 ? 201.504 117.518 164.171 1.00 116.25 ? 96  ASN A OD1 1 
ATOM   776  N ND2 . ASN A 1 124 ? 201.910 115.365 163.707 1.00 121.09 ? 96  ASN A ND2 1 
ATOM   777  N N   . LYS A 1 125 ? 197.639 117.705 167.461 1.00 106.83 ? 97  LYS A N   1 
ATOM   778  C CA  . LYS A 1 125 ? 196.341 117.486 168.149 1.00 105.31 ? 97  LYS A CA  1 
ATOM   779  C C   . LYS A 1 125 ? 195.341 118.468 167.528 1.00 105.66 ? 97  LYS A C   1 
ATOM   780  O O   . LYS A 1 125 ? 195.803 119.441 166.923 1.00 108.10 ? 97  LYS A O   1 
ATOM   781  C CB  . LYS A 1 125 ? 196.498 117.723 169.649 1.00 106.40 ? 97  LYS A CB  1 
ATOM   782  C CG  . LYS A 1 125 ? 197.512 116.824 170.343 1.00 107.65 ? 97  LYS A CG  1 
ATOM   783  C CD  . LYS A 1 125 ? 197.173 115.355 170.231 1.00 106.87 ? 97  LYS A CD  1 
ATOM   784  C CE  . LYS A 1 125 ? 195.832 115.014 170.844 1.00 106.82 ? 97  LYS A CE  1 
ATOM   785  N NZ  . LYS A 1 125 ? 195.524 113.570 170.722 1.00 107.23 ? 97  LYS A NZ  1 
ATOM   786  N N   . SER A 1 126 ? 194.039 118.194 167.593 1.00 83.99  ? 98  SER A N   1 
ATOM   787  C CA  . SER A 1 126 ? 193.051 119.074 166.917 1.00 79.84  ? 98  SER A CA  1 
ATOM   788  C C   . SER A 1 126 ? 192.848 120.376 167.691 1.00 80.74  ? 98  SER A C   1 
ATOM   789  O O   . SER A 1 126 ? 193.055 120.364 168.912 1.00 82.46  ? 98  SER A O   1 
ATOM   790  C CB  . SER A 1 126 ? 191.755 118.372 166.714 1.00 84.25  ? 98  SER A CB  1 
ATOM   791  O OG  . SER A 1 126 ? 190.826 119.228 166.066 1.00 87.45  ? 98  SER A OG  1 
ATOM   792  N N   . LEU A 1 127 ? 192.447 121.446 166.997 1.00 76.82  ? 99  LEU A N   1 
ATOM   793  C CA  . LEU A 1 127 ? 192.201 122.770 167.633 1.00 78.76  ? 99  LEU A CA  1 
ATOM   794  C C   . LEU A 1 127 ? 190.704 123.079 167.584 1.00 77.86  ? 99  LEU A C   1 
ATOM   795  O O   . LEU A 1 127 ? 190.156 123.105 166.472 1.00 77.42  ? 99  LEU A O   1 
ATOM   796  C CB  . LEU A 1 127 ? 193.011 123.826 166.874 1.00 77.51  ? 99  LEU A CB  1 
ATOM   797  C CG  . LEU A 1 127 ? 194.524 123.767 167.054 1.00 76.82  ? 99  LEU A CG  1 
ATOM   798  C CD1 . LEU A 1 127 ? 195.181 124.946 166.357 1.00 74.30  ? 99  LEU A CD1 1 
ATOM   799  C CD2 . LEU A 1 127 ? 194.850 123.830 168.534 1.00 81.45  ? 99  LEU A CD2 1 
ATOM   800  N N   . ALA A 1 128 ? 190.081 123.326 168.738 1.00 69.82  ? 100 ALA A N   1 
ATOM   801  C CA  . ALA A 1 128 ? 188.621 123.547 168.799 1.00 69.19  ? 100 ALA A CA  1 
ATOM   802  C C   . ALA A 1 128 ? 188.290 124.973 168.373 1.00 72.53  ? 100 ALA A C   1 
ATOM   803  O O   . ALA A 1 128 ? 189.212 125.792 168.315 1.00 77.86  ? 100 ALA A O   1 
ATOM   804  C CB  . ALA A 1 128 ? 188.130 123.282 170.192 1.00 71.37  ? 100 ALA A CB  1 
ATOM   805  N N   . LYS A 1 129 ? 187.008 125.260 168.137 1.00 67.87  ? 101 LYS A N   1 
ATOM   806  C CA  . LYS A 1 129 ? 186.622 126.605 167.644 1.00 66.39  ? 101 LYS A CA  1 
ATOM   807  C C   . LYS A 1 129 ? 187.102 127.641 168.660 1.00 72.43  ? 101 LYS A C   1 
ATOM   808  O O   . LYS A 1 129 ? 186.826 127.459 169.854 1.00 78.91  ? 101 LYS A O   1 
ATOM   809  C CB  . LYS A 1 129 ? 185.112 126.702 167.413 1.00 65.97  ? 101 LYS A CB  1 
ATOM   810  C CG  . LYS A 1 129 ? 184.663 127.938 166.648 1.00 69.92  ? 101 LYS A CG  1 
ATOM   811  C CD  . LYS A 1 129 ? 183.190 127.939 166.318 1.00 74.69  ? 101 LYS A CD  1 
ATOM   812  C CE  . LYS A 1 129 ? 182.772 129.135 165.491 1.00 75.39  ? 101 LYS A CE  1 
ATOM   813  N NZ  . LYS A 1 129 ? 181.327 129.099 165.168 1.00 74.11  ? 101 LYS A NZ  1 
ATOM   814  N N   . GLY A 1 130 ? 187.807 128.675 168.196 1.00 79.19  ? 102 GLY A N   1 
ATOM   815  C CA  . GLY A 1 130 ? 188.266 129.739 169.108 1.00 74.68  ? 102 GLY A CA  1 
ATOM   816  C C   . GLY A 1 130 ? 189.586 129.431 169.789 1.00 75.66  ? 102 GLY A C   1 
ATOM   817  O O   . GLY A 1 130 ? 189.975 130.218 170.662 1.00 85.30  ? 102 GLY A O   1 
ATOM   818  N N   . SER A 1 131 ? 190.261 128.344 169.429 1.00 74.06  ? 103 SER A N   1 
ATOM   819  C CA  . SER A 1 131 ? 191.597 128.086 170.028 1.00 78.37  ? 103 SER A CA  1 
ATOM   820  C C   . SER A 1 131 ? 192.727 128.140 168.994 1.00 80.34  ? 103 SER A C   1 
ATOM   821  O O   . SER A 1 131 ? 193.845 127.747 169.360 1.00 83.12  ? 103 SER A O   1 
ATOM   822  C CB  . SER A 1 131 ? 191.603 126.775 170.750 1.00 81.06  ? 103 SER A CB  1 
ATOM   823  O OG  . SER A 1 131 ? 190.637 126.772 171.791 1.00 86.30  ? 103 SER A OG  1 
ATOM   824  N N   . ALA A 1 132 ? 192.474 128.598 167.767 1.00 74.67  ? 104 ALA A N   1 
ATOM   825  C CA  . ALA A 1 132 ? 193.532 128.542 166.730 1.00 73.19  ? 104 ALA A CA  1 
ATOM   826  C C   . ALA A 1 132 ? 194.025 129.942 166.358 1.00 72.88  ? 104 ALA A C   1 
ATOM   827  O O   . ALA A 1 132 ? 193.178 130.829 166.178 1.00 79.68  ? 104 ALA A O   1 
ATOM   828  C CB  . ALA A 1 132 ? 193.014 127.824 165.522 1.00 68.64  ? 104 ALA A CB  1 
ATOM   829  N N   . THR A 1 133 ? 195.346 130.121 166.236 1.00 66.93  ? 105 THR A N   1 
ATOM   830  C CA  . THR A 1 133 ? 195.928 131.431 165.842 1.00 71.02  ? 105 THR A CA  1 
ATOM   831  C C   . THR A 1 133 ? 196.167 131.454 164.331 1.00 75.88  ? 105 THR A C   1 
ATOM   832  O O   . THR A 1 133 ? 196.136 130.373 163.729 1.00 77.38  ? 105 THR A O   1 
ATOM   833  C CB  . THR A 1 133 ? 197.210 131.712 166.632 1.00 71.70  ? 105 THR A CB  1 
ATOM   834  O OG1 . THR A 1 133 ? 198.148 130.683 166.329 1.00 72.12  ? 105 THR A OG1 1 
ATOM   835  C CG2 . THR A 1 133 ? 196.975 131.766 168.125 1.00 75.01  ? 105 THR A CG2 1 
ATOM   836  N N   . THR A 1 134 ? 196.420 132.637 163.767 1.00 67.29  ? 106 THR A N   1 
ATOM   837  C CA  . THR A 1 134 ? 196.660 132.797 162.310 1.00 64.20  ? 106 THR A CA  1 
ATOM   838  C C   . THR A 1 134 ? 197.950 132.095 161.882 1.00 68.37  ? 106 THR A C   1 
ATOM   839  O O   . THR A 1 134 ? 198.032 131.699 160.716 1.00 76.16  ? 106 THR A O   1 
ATOM   840  C CB  . THR A 1 134 ? 196.678 134.284 161.960 1.00 57.22  ? 106 THR A CB  1 
ATOM   841  O OG1 . THR A 1 134 ? 197.166 134.384 160.628 1.00 66.93  ? 106 THR A OG1 1 
ATOM   842  C CG2 . THR A 1 134 ? 197.602 135.082 162.848 1.00 63.38  ? 106 THR A CG2 1 
ATOM   843  N N   . PHE A 1 135 ? 198.918 131.948 162.783 1.00 66.92  ? 107 PHE A N   1 
ATOM   844  C CA  . PHE A 1 135 ? 200.187 131.241 162.476 1.00 63.10  ? 107 PHE A CA  1 
ATOM   845  C C   . PHE A 1 135 ? 199.889 129.762 162.240 1.00 67.32  ? 107 PHE A C   1 
ATOM   846  O O   . PHE A 1 135 ? 200.531 129.178 161.363 1.00 75.53  ? 107 PHE A O   1 
ATOM   847  C CB  . PHE A 1 135 ? 201.191 131.412 163.612 1.00 65.74  ? 107 PHE A CB  1 
ATOM   848  C CG  . PHE A 1 135 ? 202.538 130.788 163.356 1.00 71.02  ? 107 PHE A CG  1 
ATOM   849  C CD1 . PHE A 1 135 ? 203.310 131.189 162.278 1.00 75.18  ? 107 PHE A CD1 1 
ATOM   850  C CD2 . PHE A 1 135 ? 203.039 129.803 164.192 1.00 73.62  ? 107 PHE A CD2 1 
ATOM   851  C CE1 . PHE A 1 135 ? 204.547 130.618 162.038 1.00 75.73  ? 107 PHE A CE1 1 
ATOM   852  C CE2 . PHE A 1 135 ? 204.278 129.233 163.953 1.00 76.77  ? 107 PHE A CE2 1 
ATOM   853  C CZ  . PHE A 1 135 ? 205.029 129.640 162.876 1.00 78.18  ? 107 PHE A CZ  1 
ATOM   854  N N   . ASP A 1 136 ? 198.953 129.182 162.993 1.00 66.25  ? 108 ASP A N   1 
ATOM   855  C CA  . ASP A 1 136 ? 198.565 127.760 162.799 1.00 63.38  ? 108 ASP A CA  1 
ATOM   856  C C   . ASP A 1 136 ? 197.935 127.589 161.419 1.00 64.85  ? 108 ASP A C   1 
ATOM   857  O O   . ASP A 1 136 ? 198.295 126.632 160.728 1.00 67.13  ? 108 ASP A O   1 
ATOM   858  C CB  . ASP A 1 136 ? 197.585 127.292 163.869 1.00 65.36  ? 108 ASP A CB  1 
ATOM   859  C CG  . ASP A 1 136 ? 198.131 127.404 165.280 1.00 74.77  ? 108 ASP A CG  1 
ATOM   860  O OD1 . ASP A 1 136 ? 199.165 126.771 165.558 1.00 78.43  ? 108 ASP A OD1 1 
ATOM   861  O OD2 . ASP A 1 136 ? 197.504 128.110 166.093 1.00 72.41  ? 108 ASP A OD2 1 
ATOM   862  N N   . ILE A 1 137 ? 197.039 128.494 161.034 1.00 52.99  ? 109 ILE A N   1 
ATOM   863  C CA  . ILE A 1 137 ? 196.330 128.346 159.735 1.00 47.85  ? 109 ILE A CA  1 
ATOM   864  C C   . ILE A 1 137 ? 197.390 128.385 158.631 1.00 47.61  ? 109 ILE A C   1 
ATOM   865  O O   . ILE A 1 137 ? 197.338 127.523 157.752 1.00 59.69  ? 109 ILE A O   1 
ATOM   866  C CB  . ILE A 1 137 ? 195.240 129.419 159.552 1.00 49.16  ? 109 ILE A CB  1 
ATOM   867  C CG1 . ILE A 1 137 ? 194.323 129.536 160.771 1.00 48.22  ? 109 ILE A CG1 1 
ATOM   868  C CG2 . ILE A 1 137 ? 194.455 129.184 158.270 1.00 47.29  ? 109 ILE A CG2 1 
ATOM   869  C CD1 . ILE A 1 137 ? 193.564 128.280 161.096 1.00 48.12  ? 109 ILE A CD1 1 
ATOM   870  N N   . ASN A 1 138 ? 198.339 129.323 158.683 1.00 58.60  ? 110 ASN A N   1 
ATOM   871  C CA  . ASN A 1 138 ? 199.334 129.439 157.621 1.00 58.30  ? 110 ASN A CA  1 
ATOM   872  C C   . ASN A 1 138 ? 200.170 128.168 157.497 1.00 66.13  ? 110 ASN A C   1 
ATOM   873  O O   . ASN A 1 138 ? 200.459 127.712 156.380 1.00 77.43  ? 110 ASN A O   1 
ATOM   874  C CB  . ASN A 1 138 ? 200.227 130.652 157.869 1.00 52.42  ? 110 ASN A CB  1 
ATOM   875  C CG  . ASN A 1 138 ? 200.974 131.085 156.629 1.00 57.93  ? 110 ASN A CG  1 
ATOM   876  O OD1 . ASN A 1 138 ? 202.200 131.181 156.628 1.00 64.94  ? 110 ASN A OD1 1 
ATOM   877  N ND2 . ASN A 1 138 ? 200.236 131.345 155.557 1.00 64.36  ? 110 ASN A ND2 1 
ATOM   878  N N   . LYS A 1 139 ? 200.570 127.582 158.628 1.00 69.64  ? 111 LYS A N   1 
ATOM   879  C CA  . LYS A 1 139 ? 201.319 126.331 158.578 1.00 63.98  ? 111 LYS A CA  1 
ATOM   880  C C   . LYS A 1 139 ? 200.492 125.226 157.933 1.00 66.33  ? 111 LYS A C   1 
ATOM   881  O O   . LYS A 1 139 ? 201.006 124.452 157.112 1.00 72.83  ? 111 LYS A O   1 
ATOM   882  C CB  . LYS A 1 139 ? 201.758 125.922 159.982 1.00 69.16  ? 111 LYS A CB  1 
ATOM   883  C CG  . LYS A 1 139 ? 202.852 126.796 160.572 1.00 71.90  ? 111 LYS A CG  1 
ATOM   884  C CD  . LYS A 1 139 ? 203.253 126.360 161.980 1.00 71.51  ? 111 LYS A CD  1 
ATOM   885  C CE  . LYS A 1 139 ? 202.642 125.022 162.373 1.00 72.00  ? 111 LYS A CE  1 
ATOM   886  N NZ  . LYS A 1 139 ? 202.677 124.804 163.844 1.00 72.46  ? 111 LYS A NZ  1 
ATOM   887  N N   . ALA A 1 140 ? 199.208 125.144 158.283 1.00 65.79  ? 112 ALA A N   1 
ATOM   888  C CA  . ALA A 1 140 ? 198.335 124.144 157.680 1.00 69.97  ? 112 ALA A CA  1 
ATOM   889  C C   . ALA A 1 140 ? 198.168 124.389 156.188 1.00 70.34  ? 112 ALA A C   1 
ATOM   890  O O   . ALA A 1 140 ? 198.097 123.437 155.404 1.00 78.35  ? 112 ALA A O   1 
ATOM   891  C CB  . ALA A 1 140 ? 196.975 124.140 158.379 1.00 65.37  ? 112 ALA A CB  1 
ATOM   892  N N   . GLN A 1 141 ? 198.092 125.655 155.775 1.00 56.08  ? 113 GLN A N   1 
ATOM   893  C CA  . GLN A 1 141 ? 197.982 125.963 154.353 1.00 51.56  ? 113 GLN A CA  1 
ATOM   894  C C   . GLN A 1 141 ? 199.215 125.499 153.590 1.00 58.41  ? 113 GLN A C   1 
ATOM   895  O O   . GLN A 1 141 ? 199.102 124.886 152.521 1.00 70.14  ? 113 GLN A O   1 
ATOM   896  C CB  . GLN A 1 141 ? 197.758 127.461 154.156 1.00 49.79  ? 113 GLN A CB  1 
ATOM   897  C CG  . GLN A 1 141 ? 196.326 127.906 154.398 1.00 58.61  ? 113 GLN A CG  1 
ATOM   898  C CD  . GLN A 1 141 ? 196.150 129.404 154.284 1.00 61.99  ? 113 GLN A CD  1 
ATOM   899  O OE1 . GLN A 1 141 ? 197.118 130.143 154.119 1.00 68.48  ? 113 GLN A OE1 1 
ATOM   900  N NE2 . GLN A 1 141 ? 194.907 129.861 154.366 1.00 52.16  ? 113 GLN A NE2 1 
ATOM   901  N N   . LYS A 1 142 ? 200.407 125.770 154.131 1.00 71.05  ? 114 LYS A N   1 
ATOM   902  C CA  . LYS A 1 142 ? 201.627 125.313 153.471 1.00 71.89  ? 114 LYS A CA  1 
ATOM   903  C C   . LYS A 1 142 ? 201.684 123.789 153.409 1.00 83.37  ? 114 LYS A C   1 
ATOM   904  O O   . LYS A 1 142 ? 202.033 123.212 152.369 1.00 88.21  ? 114 LYS A O   1 
ATOM   905  C CB  . LYS A 1 142 ? 202.861 125.866 154.185 1.00 71.97  ? 114 LYS A CB  1 
ATOM   906  C CG  . LYS A 1 142 ? 202.870 127.379 154.354 1.00 78.19  ? 114 LYS A CG  1 
ATOM   907  C CD  . LYS A 1 142 ? 202.577 128.099 153.046 1.00 79.99  ? 114 LYS A CD  1 
ATOM   908  C CE  . LYS A 1 142 ? 203.750 128.020 152.084 1.00 82.58  ? 114 LYS A CE  1 
ATOM   909  N NZ  . LYS A 1 142 ? 203.426 128.641 150.769 1.00 81.53  ? 114 LYS A NZ  1 
ATOM   910  N N   . ARG A 1 143 ? 201.327 123.119 154.508 1.00 82.51  ? 115 ARG A N   1 
ATOM   911  C CA  . ARG A 1 143 ? 201.352 121.658 154.515 1.00 71.50  ? 115 ARG A CA  1 
ATOM   912  C C   . ARG A 1 143 ? 200.362 121.080 153.512 1.00 69.12  ? 115 ARG A C   1 
ATOM   913  O O   . ARG A 1 143 ? 200.685 120.126 152.794 1.00 77.76  ? 115 ARG A O   1 
ATOM   914  C CB  . ARG A 1 143 ? 201.070 121.132 155.921 1.00 73.66  ? 115 ARG A CB  1 
ATOM   915  C CG  . ARG A 1 143 ? 202.303 121.073 156.803 1.00 80.12  ? 115 ARG A CG  1 
ATOM   916  C CD  . ARG A 1 143 ? 202.062 120.260 158.061 1.00 79.86  ? 115 ARG A CD  1 
ATOM   917  N NE  . ARG A 1 143 ? 201.219 120.967 159.018 1.00 80.86  ? 115 ARG A NE  1 
ATOM   918  C CZ  . ARG A 1 143 ? 200.992 120.561 160.259 1.00 83.45  ? 115 ARG A CZ  1 
ATOM   919  N NH1 . ARG A 1 143 ? 201.541 119.454 160.735 1.00 82.73  ? 115 ARG A NH1 1 
ATOM   920  N NH2 . ARG A 1 143 ? 200.197 121.282 161.043 1.00 82.99  ? 115 ARG A NH2 1 
ATOM   921  N N   . CYS A 1 144 ? 199.175 121.673 153.402 1.00 69.56  ? 116 CYS A N   1 
ATOM   922  C CA  . CYS A 1 144 ? 198.169 121.176 152.422 1.00 73.61  ? 116 CYS A CA  1 
ATOM   923  C C   . CYS A 1 144 ? 198.696 121.320 150.989 1.00 74.42  ? 116 CYS A C   1 
ATOM   924  O O   . CYS A 1 144 ? 198.311 120.503 150.146 1.00 77.68  ? 116 CYS A O   1 
ATOM   925  C CB  . CYS A 1 144 ? 196.842 121.904 152.559 1.00 75.14  ? 116 CYS A CB  1 
ATOM   926  S SG  . CYS A 1 144 ? 195.595 121.324 151.386 1.00 92.68  ? 116 CYS A SG  1 
ATOM   927  N N   . PHE A 1 145 ? 199.525 122.324 150.716 1.00 77.63  ? 117 PHE A N   1 
ATOM   928  C CA  . PHE A 1 145 ? 200.121 122.506 149.366 1.00 77.85  ? 117 PHE A CA  1 
ATOM   929  C C   . PHE A 1 145 ? 201.043 121.344 149.015 1.00 74.34  ? 117 PHE A C   1 
ATOM   930  O O   . PHE A 1 145 ? 200.948 120.819 147.900 1.00 73.23  ? 117 PHE A O   1 
ATOM   931  C CB  . PHE A 1 145 ? 200.928 123.806 149.327 1.00 80.38  ? 117 PHE A CB  1 
ATOM   932  C CG  . PHE A 1 145 ? 201.789 124.016 148.109 1.00 81.61  ? 117 PHE A CG  1 
ATOM   933  C CD1 . PHE A 1 145 ? 201.243 124.063 146.839 1.00 84.36  ? 117 PHE A CD1 1 
ATOM   934  C CD2 . PHE A 1 145 ? 203.158 124.184 148.242 1.00 81.26  ? 117 PHE A CD2 1 
ATOM   935  C CE1 . PHE A 1 145 ? 202.051 124.259 145.729 1.00 81.97  ? 117 PHE A CE1 1 
ATOM   936  C CE2 . PHE A 1 145 ? 203.963 124.383 147.133 1.00 80.91  ? 117 PHE A CE2 1 
ATOM   937  C CZ  . PHE A 1 145 ? 203.407 124.422 145.878 1.00 78.35  ? 117 PHE A CZ  1 
ATOM   938  N N   . VAL A 1 146 ? 201.923 120.938 149.929 1.00 81.49  ? 118 VAL A N   1 
ATOM   939  C CA  . VAL A 1 146 ? 202.915 119.880 149.569 1.00 81.19  ? 118 VAL A CA  1 
ATOM   940  C C   . VAL A 1 146 ? 202.195 118.535 149.443 1.00 83.24  ? 118 VAL A C   1 
ATOM   941  O O   . VAL A 1 146 ? 202.678 117.698 148.666 1.00 86.42  ? 118 VAL A O   1 
ATOM   942  C CB  . VAL A 1 146 ? 204.086 119.808 150.567 1.00 86.65  ? 118 VAL A CB  1 
ATOM   943  C CG1 . VAL A 1 146 ? 204.916 121.078 150.547 1.00 90.29  ? 118 VAL A CG1 1 
ATOM   944  C CG2 . VAL A 1 146 ? 203.624 119.495 151.979 1.00 87.33  ? 118 VAL A CG2 1 
ATOM   945  N N   . LYS A 1 147 ? 201.064 118.360 150.133 1.00 87.71  ? 119 LYS A N   1 
ATOM   946  C CA  . LYS A 1 147 ? 200.289 117.092 150.062 1.00 83.55  ? 119 LYS A CA  1 
ATOM   947  C C   . LYS A 1 147 ? 199.523 117.037 148.740 1.00 85.15  ? 119 LYS A C   1 
ATOM   948  O O   . LYS A 1 147 ? 199.500 115.963 148.127 1.00 86.48  ? 119 LYS A O   1 
ATOM   949  C CB  . LYS A 1 147 ? 199.340 116.981 151.256 1.00 82.39  ? 119 LYS A CB  1 
ATOM   950  C CG  . LYS A 1 147 ? 200.022 117.067 152.614 1.00 86.81  ? 119 LYS A CG  1 
ATOM   951  C CD  . LYS A 1 147 ? 199.078 116.900 153.781 1.00 89.39  ? 119 LYS A CD  1 
ATOM   952  C CE  . LYS A 1 147 ? 199.742 117.172 155.114 1.00 91.10  ? 119 LYS A CE  1 
ATOM   953  N NZ  . LYS A 1 147 ? 200.933 116.315 155.322 1.00 88.95  ? 119 LYS A NZ  1 
ATOM   954  N N   . ALA A 1 148 ? 198.928 118.151 148.319 1.00 93.03  ? 120 ALA A N   1 
ATOM   955  C CA  . ALA A 1 148 ? 198.222 118.202 147.016 1.00 89.48  ? 120 ALA A CA  1 
ATOM   956  C C   . ALA A 1 148 ? 199.224 117.956 145.889 1.00 90.83  ? 120 ALA A C   1 
ATOM   957  O O   . ALA A 1 148 ? 198.838 117.323 144.898 1.00 89.99  ? 120 ALA A O   1 
ATOM   958  C CB  . ALA A 1 148 ? 197.523 119.522 146.844 1.00 92.79  ? 120 ALA A CB  1 
ATOM   959  N N   . SER A 1 149 ? 200.440 118.488 146.010 1.00 102.47 ? 121 SER A N   1 
ATOM   960  C CA  . SER A 1 149 ? 201.505 118.226 145.007 1.00 98.50  ? 121 SER A CA  1 
ATOM   961  C C   . SER A 1 149 ? 201.840 116.732 145.015 1.00 99.26  ? 121 SER A C   1 
ATOM   962  O O   . SER A 1 149 ? 202.136 116.204 143.940 1.00 100.18 ? 121 SER A O   1 
ATOM   963  C CB  . SER A 1 149 ? 202.716 119.065 145.261 1.00 98.98  ? 121 SER A CB  1 
ATOM   964  O OG  . SER A 1 149 ? 202.386 120.443 145.187 1.00 104.31 ? 121 SER A OG  1 
ATOM   965  N N   . ALA A 1 150 ? 201.769 116.081 146.181 1.00 103.80 ? 122 ALA A N   1 
ATOM   966  C CA  . ALA A 1 150 ? 202.026 114.624 146.281 1.00 102.75 ? 122 ALA A CA  1 
ATOM   967  C C   . ALA A 1 150 ? 200.905 113.847 145.595 1.00 101.37 ? 122 ALA A C   1 
ATOM   968  O O   . ALA A 1 150 ? 201.104 112.651 145.360 1.00 101.64 ? 122 ALA A O   1 
ATOM   969  C CB  . ALA A 1 150 ? 202.172 114.208 147.718 1.00 103.01 ? 122 ALA A CB  1 
ATOM   970  N N   . LEU A 1 151 ? 199.753 114.474 145.338 1.00 103.83 ? 123 LEU A N   1 
ATOM   971  C CA  . LEU A 1 151 ? 198.715 113.759 144.548 1.00 103.64 ? 123 LEU A CA  1 
ATOM   972  C C   . LEU A 1 151 ? 199.333 113.582 143.165 1.00 105.97 ? 123 LEU A C   1 
ATOM   973  O O   . LEU A 1 151 ? 199.035 112.567 142.514 1.00 109.12 ? 123 LEU A O   1 
ATOM   974  C CB  . LEU A 1 151 ? 197.398 114.536 144.514 1.00 103.82 ? 123 LEU A CB  1 
ATOM   975  C CG  . LEU A 1 151 ? 196.730 114.753 145.870 1.00 104.20 ? 123 LEU A CG  1 
ATOM   976  C CD1 . LEU A 1 151 ? 195.281 115.175 145.697 1.00 104.64 ? 123 LEU A CD1 1 
ATOM   977  C CD2 . LEU A 1 151 ? 196.820 113.497 146.723 1.00 102.83 ? 123 LEU A CD2 1 
ATOM   978  N N   . HIS A 1 152 ? 200.151 114.542 142.729 1.00 111.65 ? 124 HIS A N   1 
ATOM   979  C CA  . HIS A 1 152 ? 200.929 114.336 141.481 1.00 111.73 ? 124 HIS A CA  1 
ATOM   980  C C   . HIS A 1 152 ? 202.051 113.404 141.938 1.00 113.94 ? 124 HIS A C   1 
ATOM   981  O O   . HIS A 1 152 ? 202.249 113.275 143.150 1.00 115.58 ? 124 HIS A O   1 
ATOM   982  C CB  . HIS A 1 152 ? 201.400 115.662 140.874 1.00 112.06 ? 124 HIS A CB  1 
ATOM   983  C CG  . HIS A 1 152 ? 200.311 116.588 140.441 1.00 113.12 ? 124 HIS A CG  1 
ATOM   984  N ND1 . HIS A 1 152 ? 200.155 117.850 140.968 1.00 113.01 ? 124 HIS A ND1 1 
ATOM   985  C CD2 . HIS A 1 152 ? 199.335 116.441 139.540 1.00 112.70 ? 124 HIS A CD2 1 
ATOM   986  C CE1 . HIS A 1 152 ? 199.117 118.439 140.394 1.00 110.86 ? 124 HIS A CE1 1 
ATOM   987  N NE2 . HIS A 1 152 ? 198.605 117.602 139.521 1.00 110.26 ? 124 HIS A NE2 1 
ATOM   988  N N   . GLY A 1 153 ? 202.831 112.833 141.036 1.00 129.82 ? 125 GLY A N   1 
ATOM   989  C CA  . GLY A 1 153 ? 203.798 111.809 141.479 1.00 130.92 ? 125 GLY A CA  1 
ATOM   990  C C   . GLY A 1 153 ? 204.774 112.263 142.550 1.00 130.63 ? 125 GLY A C   1 
ATOM   991  O O   . GLY A 1 153 ? 205.142 111.416 143.382 1.00 128.84 ? 125 GLY A O   1 
ATOM   992  N N   . LEU A 1 154 ? 205.162 113.540 142.582 1.00 130.92 ? 126 LEU A N   1 
ATOM   993  C CA  . LEU A 1 154 ? 206.258 113.971 143.495 1.00 131.04 ? 126 LEU A CA  1 
ATOM   994  C C   . LEU A 1 154 ? 206.016 113.605 144.964 1.00 129.67 ? 126 LEU A C   1 
ATOM   995  O O   . LEU A 1 154 ? 204.961 113.995 145.490 1.00 127.97 ? 126 LEU A O   1 
ATOM   996  C CB  . LEU A 1 154 ? 206.401 115.491 143.354 1.00 128.35 ? 126 LEU A CB  1 
ATOM   997  C CG  . LEU A 1 154 ? 207.498 116.132 144.202 1.00 126.11 ? 126 LEU A CG  1 
ATOM   998  C CD1 . LEU A 1 154 ? 208.871 115.869 143.602 1.00 127.75 ? 126 LEU A CD1 1 
ATOM   999  C CD2 . LEU A 1 154 ? 207.261 117.626 144.356 1.00 126.27 ? 126 LEU A CD2 1 
ATOM   1000 N N   . GLY A 1 155 ? 206.941 112.864 145.590 1.00 129.44 ? 127 GLY A N   1 
ATOM   1001 C CA  . GLY A 1 155 ? 206.876 112.563 147.038 1.00 128.80 ? 127 GLY A CA  1 
ATOM   1002 C C   . GLY A 1 155 ? 205.598 111.899 147.522 1.00 131.23 ? 127 GLY A C   1 
ATOM   1003 O O   . GLY A 1 155 ? 205.247 112.108 148.699 1.00 130.23 ? 127 GLY A O   1 
ATOM   1004 N N   . LEU A 1 156 ? 204.942 111.103 146.675 1.00 128.74 ? 128 LEU A N   1 
ATOM   1005 C CA  . LEU A 1 156 ? 203.712 110.371 147.086 1.00 125.05 ? 128 LEU A CA  1 
ATOM   1006 C C   . LEU A 1 156 ? 204.050 109.384 148.206 1.00 124.97 ? 128 LEU A C   1 
ATOM   1007 O O   . LEU A 1 156 ? 203.224 109.241 149.126 1.00 126.44 ? 128 LEU A O   1 
ATOM   1008 C CB  . LEU A 1 156 ? 203.123 109.649 145.870 1.00 125.15 ? 128 LEU A CB  1 
ATOM   1009 C CG  . LEU A 1 156 ? 201.871 108.816 146.137 1.00 124.77 ? 128 LEU A CG  1 
ATOM   1010 C CD1 . LEU A 1 156 ? 200.659 109.706 146.355 1.00 122.75 ? 128 LEU A CD1 1 
ATOM   1011 C CD2 . LEU A 1 156 ? 201.616 107.852 144.991 1.00 126.39 ? 128 LEU A CD2 1 
ATOM   1012 N N   . TYR A 1 157 ? 205.233 108.769 148.158 1.00 132.20 ? 129 TYR A N   1 
ATOM   1013 C CA  . TYR A 1 157 ? 205.584 107.699 149.134 1.00 133.43 ? 129 TYR A CA  1 
ATOM   1014 C C   . TYR A 1 157 ? 205.516 108.218 150.579 1.00 133.72 ? 129 TYR A C   1 
ATOM   1015 O O   . TYR A 1 157 ? 205.140 107.433 151.464 1.00 134.16 ? 129 TYR A O   1 
ATOM   1016 C CB  . TYR A 1 157 ? 206.916 107.051 148.738 1.00 133.31 ? 129 TYR A CB  1 
ATOM   1017 C CG  . TYR A 1 157 ? 208.117 107.954 148.593 1.00 134.05 ? 129 TYR A CG  1 
ATOM   1018 C CD1 . TYR A 1 157 ? 208.606 108.695 149.656 1.00 132.89 ? 129 TYR A CD1 1 
ATOM   1019 C CD2 . TYR A 1 157 ? 208.775 108.058 147.379 1.00 133.02 ? 129 TYR A CD2 1 
ATOM   1020 C CE1 . TYR A 1 157 ? 209.715 109.513 149.518 1.00 132.57 ? 129 TYR A CE1 1 
ATOM   1021 C CE2 . TYR A 1 157 ? 209.883 108.873 147.222 1.00 132.95 ? 129 TYR A CE2 1 
ATOM   1022 C CZ  . TYR A 1 157 ? 210.355 109.603 148.296 1.00 134.06 ? 129 TYR A CZ  1 
ATOM   1023 O OH  . TYR A 1 157 ? 211.456 110.412 148.146 1.00 135.20 ? 129 TYR A OH  1 
ATOM   1024 N N   . ILE A 1 158 ? 205.823 109.490 150.825 1.00 128.32 ? 130 ILE A N   1 
ATOM   1025 C CA  . ILE A 1 158 ? 205.853 109.971 152.240 1.00 129.42 ? 130 ILE A CA  1 
ATOM   1026 C C   . ILE A 1 158 ? 204.450 109.873 152.848 1.00 130.09 ? 130 ILE A C   1 
ATOM   1027 O O   . ILE A 1 158 ? 204.356 109.529 154.041 1.00 129.02 ? 130 ILE A O   1 
ATOM   1028 C CB  . ILE A 1 158 ? 206.419 111.401 152.318 1.00 129.17 ? 130 ILE A CB  1 
ATOM   1029 C CG1 . ILE A 1 158 ? 207.849 111.451 151.780 1.00 129.56 ? 130 ILE A CG1 1 
ATOM   1030 C CG2 . ILE A 1 158 ? 206.339 111.941 153.734 1.00 128.25 ? 130 ILE A CG2 1 
ATOM   1031 C CD1 . ILE A 1 158 ? 208.486 112.807 151.872 1.00 129.71 ? 130 ILE A CD1 1 
ATOM   1032 N N   . TYR A 1 159 ? 203.405 110.141 152.060 1.00 124.65 ? 131 TYR A N   1 
ATOM   1033 C CA  . TYR A 1 159 ? 202.027 110.171 152.618 1.00 121.80 ? 131 TYR A CA  1 
ATOM   1034 C C   . TYR A 1 159 ? 201.290 108.893 152.215 1.00 121.65 ? 131 TYR A C   1 
ATOM   1035 O O   . TYR A 1 159 ? 201.431 107.912 152.967 1.00 122.66 ? 131 TYR A O   1 
ATOM   1036 C CB  . TYR A 1 159 ? 201.299 111.425 152.129 1.00 121.26 ? 131 TYR A CB  1 
ATOM   1037 C CG  . TYR A 1 159 ? 202.029 112.709 152.431 1.00 121.61 ? 131 TYR A CG  1 
ATOM   1038 C CD1 . TYR A 1 159 ? 202.320 113.076 153.734 1.00 121.36 ? 131 TYR A CD1 1 
ATOM   1039 C CD2 . TYR A 1 159 ? 202.457 113.543 151.412 1.00 121.87 ? 131 TYR A CD2 1 
ATOM   1040 C CE1 . TYR A 1 159 ? 203.006 114.245 154.018 1.00 123.37 ? 131 TYR A CE1 1 
ATOM   1041 C CE2 . TYR A 1 159 ? 203.144 114.715 151.678 1.00 122.70 ? 131 TYR A CE2 1 
ATOM   1042 C CZ  . TYR A 1 159 ? 203.419 115.068 152.987 1.00 125.71 ? 131 TYR A CZ  1 
ATOM   1043 O OH  . TYR A 1 159 ? 204.098 116.230 153.263 1.00 127.64 ? 131 TYR A OH  1 
HETATM 1044 O O   . HOH B 2 .   ? 203.950 131.590 158.211 1.00 56.02  ? 201 HOH A O   1 
HETATM 1045 O O   . HOH B 2 .   ? 207.497 128.942 155.200 1.00 82.18  ? 202 HOH A O   1 
HETATM 1046 O O   . HOH B 2 .   ? 185.421 126.993 147.435 1.00 62.38  ? 203 HOH A O   1 
HETATM 1047 O O   . HOH B 2 .   ? 200.444 131.368 143.122 1.00 74.23  ? 204 HOH A O   1 
HETATM 1048 O O   . HOH B 2 .   ? 200.068 130.462 150.992 1.00 50.09  ? 205 HOH A O   1 
HETATM 1049 O O   . HOH B 2 .   ? 215.412 125.855 148.145 1.00 72.36  ? 206 HOH A O   1 
HETATM 1050 O O   . HOH B 2 .   ? 214.759 125.733 153.478 1.00 57.85  ? 207 HOH A O   1 
HETATM 1051 O O   . HOH B 2 .   ? 198.804 131.571 147.501 1.00 67.13  ? 208 HOH A O   1 
HETATM 1052 O O   . HOH B 2 .   ? 210.061 124.936 157.585 1.00 71.03  ? 209 HOH A O   1 
# 
