data_9CI7
# 
_entry.id   9CI7 
# 
_audit_conform.dict_name       mmcif_pdbx.dic 
_audit_conform.dict_version    5.403 
_audit_conform.dict_location   http://mmcif.pdb.org/dictionaries/ascii/mmcif_pdbx.dic 
# 
loop_
_database_2.database_id 
_database_2.database_code 
_database_2.pdbx_database_accession 
_database_2.pdbx_DOI 
PDB   9CI7         pdb_00009ci7 10.2210/pdb9ci7/pdb 
WWPDB D_1000285270 ?            ?                   
# 
_pdbx_audit_revision_history.ordinal             1 
_pdbx_audit_revision_history.data_content_type   'Structure model' 
_pdbx_audit_revision_history.major_revision      1 
_pdbx_audit_revision_history.minor_revision      0 
_pdbx_audit_revision_history.revision_date       2025-05-21 
_pdbx_audit_revision_history.part_number         ? 
# 
_pdbx_audit_revision_details.ordinal             1 
_pdbx_audit_revision_details.revision_ordinal    1 
_pdbx_audit_revision_details.data_content_type   'Structure model' 
_pdbx_audit_revision_details.provider            repository 
_pdbx_audit_revision_details.type                'Initial release' 
_pdbx_audit_revision_details.description         ? 
_pdbx_audit_revision_details.details             ? 
# 
_pdbx_database_status.status_code                     REL 
_pdbx_database_status.status_code_sf                  REL 
_pdbx_database_status.status_code_mr                  ? 
_pdbx_database_status.entry_id                        9CI7 
_pdbx_database_status.recvd_initial_deposition_date   2024-07-02 
_pdbx_database_status.SG_entry                        N 
_pdbx_database_status.deposit_site                    RCSB 
_pdbx_database_status.process_site                    RCSB 
_pdbx_database_status.status_code_cs                  ? 
_pdbx_database_status.status_code_nmr_data            ? 
_pdbx_database_status.methods_development_category    ? 
_pdbx_database_status.pdb_format_compatible           Y 
# 
loop_
_pdbx_contact_author.id 
_pdbx_contact_author.email 
_pdbx_contact_author.name_first 
_pdbx_contact_author.name_last 
_pdbx_contact_author.name_mi 
_pdbx_contact_author.role 
_pdbx_contact_author.identifier_ORCID 
2 rpage@uchc.edu Rebecca  Page ? 'principal investigator/group leader' 0000-0002-4645-1232 
3 peti@uchc.edu  Wolfgang Peti ? 'principal investigator/group leader' 0000-0002-8830-6594 
# 
loop_
_audit_author.name 
_audit_author.pdbx_ordinal 
_audit_author.identifier_ORCID 
'Page, R.' 1 ? 
'Peti, W.' 2 ? 
'Wang, X.' 3 ? 
# 
_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                   US 
_citation.database_id_Medline       ? 
_citation.details                   ? 
_citation.id                        primary 
_citation.journal_abbrev            'Cell Rep' 
_citation.journal_id_ASTM           ? 
_citation.journal_id_CSD            ? 
_citation.journal_id_ISSN           2211-1247 
_citation.journal_full              ? 
_citation.journal_issue             ? 
_citation.journal_volume            44 
_citation.language                  ? 
_citation.page_first                115693 
_citation.page_last                 115693 
_citation.title                     
'PNUTS:PP1 recruitment to Tox4 regulates chromosomal dispersal in Drosophila germline development.' 
_citation.year                      2025 
_citation.database_id_CSD           ? 
_citation.pdbx_database_id_DOI      10.1016/j.celrep.2025.115693 
_citation.pdbx_database_id_PubMed   40347473 
_citation.pdbx_database_id_patent   ? 
_citation.unpublished_flag          ? 
# 
loop_
_citation_author.citation_id 
_citation_author.name 
_citation_author.ordinal 
_citation_author.identifier_ORCID 
primary 'Duncalf, L.'    1  ? 
primary 'Wang, X.'       2  ? 
primary 'Aljabri, A.A.'  3  ? 
primary 'Campbell, A.E.' 4  ? 
primary 'Alharbi, R.Q.'  5  ? 
primary 'Donaldson, I.'  6  ? 
primary 'Hayes, A.'      7  ? 
primary 'Peti, W.'       8  ? 
primary 'Page, R.'       9  ? 
primary 'Bennett, D.'    10 ? 
# 
loop_
_entity.id 
_entity.type 
_entity.src_method 
_entity.pdbx_description 
_entity.formula_weight 
_entity.pdbx_number_of_molecules 
_entity.pdbx_ec 
_entity.pdbx_mutation 
_entity.pdbx_fragment 
_entity.details 
1 polymer     man 'Serine/threonine-protein phosphatase 1 regulatory subunit 10' 18029.049 1   ? C48S  ? ? 
2 polymer     man 'TOX high mobility group box family member 4'                  6180.001  1   ? C601S ? ? 
3 non-polymer syn 'CHLORIDE ION'                                                 35.453    4   ? ?     ? ? 
4 non-polymer syn 'ZINC ION'                                                     65.409    2   ? ?     ? ? 
5 non-polymer nat 'SODIUM ION'                                                   22.990    1   ? ?     ? ? 
6 water       nat water                                                          18.015    128 ? ?     ? ? 
# 
loop_
_entity_name_com.entity_id 
_entity_name_com.name 
1 'MHC class I region proline-rich protein CAT53,Phosphatase 1 nuclear targeting subunit,Protein PNUTS' 
2 'Epidermal Langerhans cell protein LCP1'                                                              
# 
loop_
_entity_poly.entity_id 
_entity_poly.type 
_entity_poly.nstd_linkage 
_entity_poly.nstd_monomer 
_entity_poly.pdbx_seq_one_letter_code 
_entity_poly.pdbx_seq_one_letter_code_can 
_entity_poly.pdbx_strand_id 
_entity_poly.pdbx_target_identifier 
1 'polypeptide(L)' no no 
;GHMPIDPKELLKGLDSFLTRDGEVKSVDGIAKIFSLMKEARKMVSRSTYLNIILQTRAPEVLVKFIDVGGYKLLNSWLTY
SKTTNNIPLLQQILLTLQHLPLTVDHLKQNNTAKLVKQLSKSSEDEELRKLASVLVSDWMAVIRSQSSTQPAEKDKKKR
;
;GHMPIDPKELLKGLDSFLTRDGEVKSVDGIAKIFSLMKEARKMVSRSTYLNIILQTRAPEVLVKFIDVGGYKLLNSWLTY
SKTTNNIPLLQQILLTLQHLPLTVDHLKQNNTAKLVKQLSKSSEDEELRKLASVLVSDWMAVIRSQSSTQPAEKDKKKR
;
A ? 
2 'polypeptide(L)' no no GHMRCVRSGCENPPIVSKDWDNEYCSNECVVKHSRDVFLAWVASRNSNTVVFVK 
GHMRCVRSGCENPPIVSKDWDNEYCSNECVVKHSRDVFLAWVASRNSNTVVFVK B ? 
# 
loop_
_pdbx_entity_nonpoly.entity_id 
_pdbx_entity_nonpoly.name 
_pdbx_entity_nonpoly.comp_id 
3 'CHLORIDE ION' CL  
4 'ZINC ION'     ZN  
5 'SODIUM ION'   NA  
6 water          HOH 
# 
loop_
_entity_poly_seq.entity_id 
_entity_poly_seq.num 
_entity_poly_seq.mon_id 
_entity_poly_seq.hetero 
1 1   GLY n 
1 2   HIS n 
1 3   MET n 
1 4   PRO n 
1 5   ILE n 
1 6   ASP n 
1 7   PRO n 
1 8   LYS n 
1 9   GLU n 
1 10  LEU n 
1 11  LEU n 
1 12  LYS n 
1 13  GLY n 
1 14  LEU n 
1 15  ASP n 
1 16  SER n 
1 17  PHE n 
1 18  LEU n 
1 19  THR n 
1 20  ARG n 
1 21  ASP n 
1 22  GLY n 
1 23  GLU n 
1 24  VAL n 
1 25  LYS n 
1 26  SER n 
1 27  VAL n 
1 28  ASP n 
1 29  GLY n 
1 30  ILE n 
1 31  ALA n 
1 32  LYS n 
1 33  ILE n 
1 34  PHE n 
1 35  SER n 
1 36  LEU n 
1 37  MET n 
1 38  LYS n 
1 39  GLU n 
1 40  ALA n 
1 41  ARG n 
1 42  LYS n 
1 43  MET n 
1 44  VAL n 
1 45  SER n 
1 46  ARG n 
1 47  SER n 
1 48  THR n 
1 49  TYR n 
1 50  LEU n 
1 51  ASN n 
1 52  ILE n 
1 53  ILE n 
1 54  LEU n 
1 55  GLN n 
1 56  THR n 
1 57  ARG n 
1 58  ALA n 
1 59  PRO n 
1 60  GLU n 
1 61  VAL n 
1 62  LEU n 
1 63  VAL n 
1 64  LYS n 
1 65  PHE n 
1 66  ILE n 
1 67  ASP n 
1 68  VAL n 
1 69  GLY n 
1 70  GLY n 
1 71  TYR n 
1 72  LYS n 
1 73  LEU n 
1 74  LEU n 
1 75  ASN n 
1 76  SER n 
1 77  TRP n 
1 78  LEU n 
1 79  THR n 
1 80  TYR n 
1 81  SER n 
1 82  LYS n 
1 83  THR n 
1 84  THR n 
1 85  ASN n 
1 86  ASN n 
1 87  ILE n 
1 88  PRO n 
1 89  LEU n 
1 90  LEU n 
1 91  GLN n 
1 92  GLN n 
1 93  ILE n 
1 94  LEU n 
1 95  LEU n 
1 96  THR n 
1 97  LEU n 
1 98  GLN n 
1 99  HIS n 
1 100 LEU n 
1 101 PRO n 
1 102 LEU n 
1 103 THR n 
1 104 VAL n 
1 105 ASP n 
1 106 HIS n 
1 107 LEU n 
1 108 LYS n 
1 109 GLN n 
1 110 ASN n 
1 111 ASN n 
1 112 THR n 
1 113 ALA n 
1 114 LYS n 
1 115 LEU n 
1 116 VAL n 
1 117 LYS n 
1 118 GLN n 
1 119 LEU n 
1 120 SER n 
1 121 LYS n 
1 122 SER n 
1 123 SER n 
1 124 GLU n 
1 125 ASP n 
1 126 GLU n 
1 127 GLU n 
1 128 LEU n 
1 129 ARG n 
1 130 LYS n 
1 131 LEU n 
1 132 ALA n 
1 133 SER n 
1 134 VAL n 
1 135 LEU n 
1 136 VAL n 
1 137 SER n 
1 138 ASP n 
1 139 TRP n 
1 140 MET n 
1 141 ALA n 
1 142 VAL n 
1 143 ILE n 
1 144 ARG n 
1 145 SER n 
1 146 GLN n 
1 147 SER n 
1 148 SER n 
1 149 THR n 
1 150 GLN n 
1 151 PRO n 
1 152 ALA n 
1 153 GLU n 
1 154 LYS n 
1 155 ASP n 
1 156 LYS n 
1 157 LYS n 
1 158 LYS n 
1 159 ARG n 
2 1   GLY n 
2 2   HIS n 
2 3   MET n 
2 4   ARG n 
2 5   CYS n 
2 6   VAL n 
2 7   ARG n 
2 8   SER n 
2 9   GLY n 
2 10  CYS n 
2 11  GLU n 
2 12  ASN n 
2 13  PRO n 
2 14  PRO n 
2 15  ILE n 
2 16  VAL n 
2 17  SER n 
2 18  LYS n 
2 19  ASP n 
2 20  TRP n 
2 21  ASP n 
2 22  ASN n 
2 23  GLU n 
2 24  TYR n 
2 25  CYS n 
2 26  SER n 
2 27  ASN n 
2 28  GLU n 
2 29  CYS n 
2 30  VAL n 
2 31  VAL n 
2 32  LYS n 
2 33  HIS n 
2 34  SER n 
2 35  ARG n 
2 36  ASP n 
2 37  VAL n 
2 38  PHE n 
2 39  LEU n 
2 40  ALA n 
2 41  TRP n 
2 42  VAL n 
2 43  ALA n 
2 44  SER n 
2 45  ARG n 
2 46  ASN n 
2 47  SER n 
2 48  ASN n 
2 49  THR n 
2 50  VAL n 
2 51  VAL n 
2 52  PHE n 
2 53  VAL n 
2 54  LYS n 
# 
loop_
_entity_src_gen.entity_id 
_entity_src_gen.pdbx_src_id 
_entity_src_gen.pdbx_alt_source_flag 
_entity_src_gen.pdbx_seq_type 
_entity_src_gen.pdbx_beg_seq_num 
_entity_src_gen.pdbx_end_seq_num 
_entity_src_gen.gene_src_common_name 
_entity_src_gen.gene_src_genus 
_entity_src_gen.pdbx_gene_src_gene 
_entity_src_gen.gene_src_species 
_entity_src_gen.gene_src_strain 
_entity_src_gen.gene_src_tissue 
_entity_src_gen.gene_src_tissue_fraction 
_entity_src_gen.gene_src_details 
_entity_src_gen.pdbx_gene_src_fragment 
_entity_src_gen.pdbx_gene_src_scientific_name 
_entity_src_gen.pdbx_gene_src_ncbi_taxonomy_id 
_entity_src_gen.pdbx_gene_src_variant 
_entity_src_gen.pdbx_gene_src_cell_line 
_entity_src_gen.pdbx_gene_src_atcc 
_entity_src_gen.pdbx_gene_src_organ 
_entity_src_gen.pdbx_gene_src_organelle 
_entity_src_gen.pdbx_gene_src_cell 
_entity_src_gen.pdbx_gene_src_cellular_location 
_entity_src_gen.host_org_common_name 
_entity_src_gen.pdbx_host_org_scientific_name 
_entity_src_gen.pdbx_host_org_ncbi_taxonomy_id 
_entity_src_gen.host_org_genus 
_entity_src_gen.pdbx_host_org_gene 
_entity_src_gen.pdbx_host_org_organ 
_entity_src_gen.host_org_species 
_entity_src_gen.pdbx_host_org_tissue 
_entity_src_gen.pdbx_host_org_tissue_fraction 
_entity_src_gen.pdbx_host_org_strain 
_entity_src_gen.pdbx_host_org_variant 
_entity_src_gen.pdbx_host_org_cell_line 
_entity_src_gen.pdbx_host_org_atcc 
_entity_src_gen.pdbx_host_org_culture_collection 
_entity_src_gen.pdbx_host_org_cell 
_entity_src_gen.pdbx_host_org_organelle 
_entity_src_gen.pdbx_host_org_cellular_location 
_entity_src_gen.pdbx_host_org_vector_type 
_entity_src_gen.pdbx_host_org_vector 
_entity_src_gen.host_org_details 
_entity_src_gen.expression_system_id 
_entity_src_gen.plasmid_name 
_entity_src_gen.plasmid_details 
_entity_src_gen.pdbx_description 
1 1 sample 'Biological sequence' 1 159 'Norway rat' ? 'Ppp1r10, Cat53, Pnuts'    ? ? ? ? ? ? 'Rattus norvegicus' 10116 ? ? ? ? ? ? 
? ? 'Escherichia coli' 562 ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? 
2 1 sample 'Biological sequence' 1 54  human        ? 'TOX4, C14orf92, KIAA0737' ? ? ? ? ? ? 'Homo sapiens'      9606  ? ? ? ? ? ? 
? ? 'Escherichia coli' 562 ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? 
# 
loop_
_chem_comp.id 
_chem_comp.type 
_chem_comp.mon_nstd_flag 
_chem_comp.name 
_chem_comp.pdbx_synonyms 
_chem_comp.formula 
_chem_comp.formula_weight 
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 
CL  non-polymer         . 'CHLORIDE ION'  ? 'Cl -1'          35.453  
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 
NA  non-polymer         . 'SODIUM ION'    ? 'Na 1'           22.990  
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 
ZN  non-polymer         . 'ZINC ION'      ? 'Zn 2'           65.409  
# 
loop_
_pdbx_poly_seq_scheme.asym_id 
_pdbx_poly_seq_scheme.entity_id 
_pdbx_poly_seq_scheme.seq_id 
_pdbx_poly_seq_scheme.mon_id 
_pdbx_poly_seq_scheme.ndb_seq_num 
_pdbx_poly_seq_scheme.pdb_seq_num 
_pdbx_poly_seq_scheme.auth_seq_num 
_pdbx_poly_seq_scheme.pdb_mon_id 
_pdbx_poly_seq_scheme.auth_mon_id 
_pdbx_poly_seq_scheme.pdb_strand_id 
_pdbx_poly_seq_scheme.pdb_ins_code 
_pdbx_poly_seq_scheme.hetero 
A 1 1   GLY 1   2   2   GLY GLY A . n 
A 1 2   HIS 2   3   3   HIS HIS A . n 
A 1 3   MET 3   4   4   MET MET A . n 
A 1 4   PRO 4   5   5   PRO PRO A . n 
A 1 5   ILE 5   6   6   ILE ILE A . n 
A 1 6   ASP 6   7   7   ASP ASP A . n 
A 1 7   PRO 7   8   8   PRO PRO A . n 
A 1 8   LYS 8   9   9   LYS LYS A . n 
A 1 9   GLU 9   10  10  GLU GLU A . n 
A 1 10  LEU 10  11  11  LEU LEU A . n 
A 1 11  LEU 11  12  12  LEU LEU A . n 
A 1 12  LYS 12  13  13  LYS LYS A . n 
A 1 13  GLY 13  14  14  GLY GLY A . n 
A 1 14  LEU 14  15  15  LEU LEU A . n 
A 1 15  ASP 15  16  16  ASP ASP A . n 
A 1 16  SER 16  17  17  SER SER A . n 
A 1 17  PHE 17  18  18  PHE PHE A . n 
A 1 18  LEU 18  19  19  LEU LEU A . n 
A 1 19  THR 19  20  20  THR THR A . n 
A 1 20  ARG 20  21  21  ARG ARG A . n 
A 1 21  ASP 21  22  22  ASP ASP A . n 
A 1 22  GLY 22  23  23  GLY GLY A . n 
A 1 23  GLU 23  24  24  GLU GLU A . n 
A 1 24  VAL 24  25  25  VAL VAL A . n 
A 1 25  LYS 25  26  26  LYS LYS A . n 
A 1 26  SER 26  27  27  SER SER A . n 
A 1 27  VAL 27  28  28  VAL VAL A . n 
A 1 28  ASP 28  29  29  ASP ASP A . n 
A 1 29  GLY 29  30  30  GLY GLY A . n 
A 1 30  ILE 30  31  31  ILE ILE A . n 
A 1 31  ALA 31  32  32  ALA ALA A . n 
A 1 32  LYS 32  33  33  LYS LYS A . n 
A 1 33  ILE 33  34  34  ILE ILE A . n 
A 1 34  PHE 34  35  35  PHE PHE A . n 
A 1 35  SER 35  36  36  SER SER A . n 
A 1 36  LEU 36  37  37  LEU LEU A . n 
A 1 37  MET 37  38  38  MET MET A . n 
A 1 38  LYS 38  39  39  LYS LYS A . n 
A 1 39  GLU 39  40  40  GLU GLU A . n 
A 1 40  ALA 40  41  41  ALA ALA A . n 
A 1 41  ARG 41  42  42  ARG ARG A . n 
A 1 42  LYS 42  43  43  LYS LYS A . n 
A 1 43  MET 43  44  44  MET MET A . n 
A 1 44  VAL 44  45  45  VAL VAL A . n 
A 1 45  SER 45  46  46  SER SER A . n 
A 1 46  ARG 46  47  47  ARG ARG A . n 
A 1 47  SER 47  48  48  SER SER A . n 
A 1 48  THR 48  49  49  THR THR A . n 
A 1 49  TYR 49  50  50  TYR TYR A . n 
A 1 50  LEU 50  51  51  LEU LEU A . n 
A 1 51  ASN 51  52  52  ASN ASN A . n 
A 1 52  ILE 52  53  53  ILE ILE A . n 
A 1 53  ILE 53  54  54  ILE ILE A . n 
A 1 54  LEU 54  55  55  LEU LEU A . n 
A 1 55  GLN 55  56  56  GLN GLN A . n 
A 1 56  THR 56  57  57  THR THR A . n 
A 1 57  ARG 57  58  58  ARG ARG A . n 
A 1 58  ALA 58  59  59  ALA ALA A . n 
A 1 59  PRO 59  60  60  PRO PRO A . n 
A 1 60  GLU 60  61  61  GLU GLU A . n 
A 1 61  VAL 61  62  62  VAL VAL A . n 
A 1 62  LEU 62  63  63  LEU LEU A . n 
A 1 63  VAL 63  64  64  VAL VAL A . n 
A 1 64  LYS 64  65  65  LYS LYS A . n 
A 1 65  PHE 65  66  66  PHE PHE A . n 
A 1 66  ILE 66  67  67  ILE ILE A . n 
A 1 67  ASP 67  68  68  ASP ASP A . n 
A 1 68  VAL 68  69  69  VAL VAL A . n 
A 1 69  GLY 69  70  70  GLY GLY A . n 
A 1 70  GLY 70  71  71  GLY GLY A . n 
A 1 71  TYR 71  72  72  TYR TYR A . n 
A 1 72  LYS 72  73  73  LYS LYS A . n 
A 1 73  LEU 73  74  74  LEU LEU A . n 
A 1 74  LEU 74  75  75  LEU LEU A . n 
A 1 75  ASN 75  76  76  ASN ASN A . n 
A 1 76  SER 76  77  77  SER SER A . n 
A 1 77  TRP 77  78  78  TRP TRP A . n 
A 1 78  LEU 78  79  79  LEU LEU A . n 
A 1 79  THR 79  80  80  THR THR A . n 
A 1 80  TYR 80  81  81  TYR TYR A . n 
A 1 81  SER 81  82  82  SER SER A . n 
A 1 82  LYS 82  83  83  LYS LYS A . n 
A 1 83  THR 83  84  84  THR THR A . n 
A 1 84  THR 84  85  85  THR THR A . n 
A 1 85  ASN 85  86  86  ASN ASN A . n 
A 1 86  ASN 86  87  87  ASN ASN A . n 
A 1 87  ILE 87  88  88  ILE ILE A . n 
A 1 88  PRO 88  89  89  PRO PRO A . n 
A 1 89  LEU 89  90  90  LEU LEU A . n 
A 1 90  LEU 90  91  91  LEU LEU A . n 
A 1 91  GLN 91  92  92  GLN GLN A . n 
A 1 92  GLN 92  93  93  GLN GLN A . n 
A 1 93  ILE 93  94  94  ILE ILE A . n 
A 1 94  LEU 94  95  95  LEU LEU A . n 
A 1 95  LEU 95  96  96  LEU LEU A . n 
A 1 96  THR 96  97  97  THR THR A . n 
A 1 97  LEU 97  98  98  LEU LEU A . n 
A 1 98  GLN 98  99  99  GLN GLN A . n 
A 1 99  HIS 99  100 100 HIS HIS A . n 
A 1 100 LEU 100 101 101 LEU LEU A . n 
A 1 101 PRO 101 102 102 PRO PRO A . n 
A 1 102 LEU 102 103 103 LEU LEU A . n 
A 1 103 THR 103 104 104 THR THR A . n 
A 1 104 VAL 104 105 105 VAL VAL A . n 
A 1 105 ASP 105 106 106 ASP ASP A . n 
A 1 106 HIS 106 107 107 HIS HIS A . n 
A 1 107 LEU 107 108 108 LEU LEU A . n 
A 1 108 LYS 108 109 109 LYS LYS A . n 
A 1 109 GLN 109 110 110 GLN GLN A . n 
A 1 110 ASN 110 111 111 ASN ASN A . n 
A 1 111 ASN 111 112 112 ASN ASN A . n 
A 1 112 THR 112 113 113 THR THR A . n 
A 1 113 ALA 113 114 114 ALA ALA A . n 
A 1 114 LYS 114 115 115 LYS LYS A . n 
A 1 115 LEU 115 116 116 LEU LEU A . n 
A 1 116 VAL 116 117 117 VAL VAL A . n 
A 1 117 LYS 117 118 118 LYS LYS A . n 
A 1 118 GLN 118 119 119 GLN GLN A . n 
A 1 119 LEU 119 120 120 LEU LEU A . n 
A 1 120 SER 120 121 121 SER SER A . n 
A 1 121 LYS 121 122 122 LYS LYS A . n 
A 1 122 SER 122 123 123 SER SER A . n 
A 1 123 SER 123 124 124 SER SER A . n 
A 1 124 GLU 124 125 125 GLU GLU A . n 
A 1 125 ASP 125 126 126 ASP ASP A . n 
A 1 126 GLU 126 127 127 GLU GLU A . n 
A 1 127 GLU 127 128 128 GLU GLU A . n 
A 1 128 LEU 128 129 129 LEU LEU A . n 
A 1 129 ARG 129 130 130 ARG ARG A . n 
A 1 130 LYS 130 131 131 LYS LYS A . n 
A 1 131 LEU 131 132 132 LEU LEU A . n 
A 1 132 ALA 132 133 133 ALA ALA A . n 
A 1 133 SER 133 134 134 SER SER A . n 
A 1 134 VAL 134 135 135 VAL VAL A . n 
A 1 135 LEU 135 136 136 LEU LEU A . n 
A 1 136 VAL 136 137 137 VAL VAL A . n 
A 1 137 SER 137 138 138 SER SER A . n 
A 1 138 ASP 138 139 139 ASP ASP A . n 
A 1 139 TRP 139 140 140 TRP TRP A . n 
A 1 140 MET 140 141 141 MET MET A . n 
A 1 141 ALA 141 142 142 ALA ALA A . n 
A 1 142 VAL 142 143 143 VAL VAL A . n 
A 1 143 ILE 143 144 144 ILE ILE A . n 
A 1 144 ARG 144 145 145 ARG ARG A . n 
A 1 145 SER 145 146 146 SER SER A . n 
A 1 146 GLN 146 147 147 GLN GLN A . n 
A 1 147 SER 147 148 ?   ?   ?   A . n 
A 1 148 SER 148 149 ?   ?   ?   A . n 
A 1 149 THR 149 150 ?   ?   ?   A . n 
A 1 150 GLN 150 151 ?   ?   ?   A . n 
A 1 151 PRO 151 152 ?   ?   ?   A . n 
A 1 152 ALA 152 153 ?   ?   ?   A . n 
A 1 153 GLU 153 154 ?   ?   ?   A . n 
A 1 154 LYS 154 155 ?   ?   ?   A . n 
A 1 155 ASP 155 156 ?   ?   ?   A . n 
A 1 156 LYS 156 157 ?   ?   ?   A . n 
A 1 157 LYS 157 158 ?   ?   ?   A . n 
A 1 158 LYS 158 159 ?   ?   ?   A . n 
A 1 159 ARG 159 160 ?   ?   ?   A . n 
B 2 1   GLY 1   568 568 GLY GLY B . n 
B 2 2   HIS 2   569 569 HIS HIS B . n 
B 2 3   MET 3   570 570 MET MET B . n 
B 2 4   ARG 4   571 571 ARG ARG B . n 
B 2 5   CYS 5   572 572 CYS CYS B . n 
B 2 6   VAL 6   573 573 VAL VAL B . n 
B 2 7   ARG 7   574 574 ARG ARG B . n 
B 2 8   SER 8   575 575 SER SER B . n 
B 2 9   GLY 9   576 576 GLY GLY B . n 
B 2 10  CYS 10  577 577 CYS CYS B . n 
B 2 11  GLU 11  578 578 GLU GLU B . n 
B 2 12  ASN 12  579 579 ASN ASN B . n 
B 2 13  PRO 13  580 580 PRO PRO B . n 
B 2 14  PRO 14  581 581 PRO PRO B . n 
B 2 15  ILE 15  582 582 ILE ILE B . n 
B 2 16  VAL 16  583 583 VAL VAL B . n 
B 2 17  SER 17  584 584 SER SER B . n 
B 2 18  LYS 18  585 585 LYS LYS B . n 
B 2 19  ASP 19  586 586 ASP ASP B . n 
B 2 20  TRP 20  587 587 TRP TRP B . n 
B 2 21  ASP 21  588 588 ASP ASP B . n 
B 2 22  ASN 22  589 589 ASN ASN B . n 
B 2 23  GLU 23  590 590 GLU GLU B . n 
B 2 24  TYR 24  591 591 TYR TYR B . n 
B 2 25  CYS 25  592 592 CYS CYS B . n 
B 2 26  SER 26  593 593 SER SER B . n 
B 2 27  ASN 27  594 594 ASN ASN B . n 
B 2 28  GLU 28  595 595 GLU GLU B . n 
B 2 29  CYS 29  596 596 CYS CYS B . n 
B 2 30  VAL 30  597 597 VAL VAL B . n 
B 2 31  VAL 31  598 598 VAL VAL B . n 
B 2 32  LYS 32  599 599 LYS LYS B . n 
B 2 33  HIS 33  600 600 HIS HIS B . n 
B 2 34  SER 34  601 601 SER SER B . n 
B 2 35  ARG 35  602 602 ARG ARG B . n 
B 2 36  ASP 36  603 603 ASP ASP B . n 
B 2 37  VAL 37  604 604 VAL VAL B . n 
B 2 38  PHE 38  605 605 PHE PHE B . n 
B 2 39  LEU 39  606 606 LEU LEU B . n 
B 2 40  ALA 40  607 607 ALA ALA B . n 
B 2 41  TRP 41  608 608 TRP TRP B . n 
B 2 42  VAL 42  609 609 VAL VAL B . n 
B 2 43  ALA 43  610 610 ALA ALA B . n 
B 2 44  SER 44  611 611 SER SER B . n 
B 2 45  ARG 45  612 612 ARG ARG B . n 
B 2 46  ASN 46  613 613 ASN ASN B . n 
B 2 47  SER 47  614 614 SER SER B . n 
B 2 48  ASN 48  615 615 ASN ASN B . n 
B 2 49  THR 49  616 616 THR THR B . n 
B 2 50  VAL 50  617 617 VAL VAL B . n 
B 2 51  VAL 51  618 618 VAL VAL B . n 
B 2 52  PHE 52  619 619 PHE PHE B . n 
B 2 53  VAL 53  620 620 VAL VAL B . n 
B 2 54  LYS 54  621 ?   ?   ?   B . 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 
C 3 CL  1  201 1   CL  CL  A . 
D 3 CL  1  202 2   CL  CL  A . 
E 3 CL  1  203 4   CL  CL  A . 
F 4 ZN  1  204 2   ZN  ZN  A . 
G 5 NA  1  205 1   NA  NA  A . 
H 4 ZN  1  701 701 ZN  ZN  B . 
I 3 CL  1  702 3   CL  CL  B . 
J 6 HOH 1  301 29  HOH HOH A . 
J 6 HOH 2  302 143 HOH HOH A . 
J 6 HOH 3  303 61  HOH HOH A . 
J 6 HOH 4  304 130 HOH HOH A . 
J 6 HOH 5  305 52  HOH HOH A . 
J 6 HOH 6  306 65  HOH HOH A . 
J 6 HOH 7  307 35  HOH HOH A . 
J 6 HOH 8  308 39  HOH HOH A . 
J 6 HOH 9  309 3   HOH HOH A . 
J 6 HOH 10 310 36  HOH HOH A . 
J 6 HOH 11 311 21  HOH HOH A . 
J 6 HOH 12 312 107 HOH HOH A . 
J 6 HOH 13 313 11  HOH HOH A . 
J 6 HOH 14 314 51  HOH HOH A . 
J 6 HOH 15 315 122 HOH HOH A . 
J 6 HOH 16 316 46  HOH HOH A . 
J 6 HOH 17 317 82  HOH HOH A . 
J 6 HOH 18 318 63  HOH HOH A . 
J 6 HOH 19 319 17  HOH HOH A . 
J 6 HOH 20 320 88  HOH HOH A . 
J 6 HOH 21 321 113 HOH HOH A . 
J 6 HOH 22 322 74  HOH HOH A . 
J 6 HOH 23 323 58  HOH HOH A . 
J 6 HOH 24 324 34  HOH HOH A . 
J 6 HOH 25 325 96  HOH HOH A . 
J 6 HOH 26 326 114 HOH HOH A . 
J 6 HOH 27 327 12  HOH HOH A . 
J 6 HOH 28 328 38  HOH HOH A . 
J 6 HOH 29 329 24  HOH HOH A . 
J 6 HOH 30 330 26  HOH HOH A . 
J 6 HOH 31 331 37  HOH HOH A . 
J 6 HOH 32 332 97  HOH HOH A . 
J 6 HOH 33 333 76  HOH HOH A . 
J 6 HOH 34 334 144 HOH HOH A . 
J 6 HOH 35 335 13  HOH HOH A . 
J 6 HOH 36 336 42  HOH HOH A . 
J 6 HOH 37 337 54  HOH HOH A . 
J 6 HOH 38 338 87  HOH HOH A . 
J 6 HOH 39 339 109 HOH HOH A . 
J 6 HOH 40 340 119 HOH HOH A . 
J 6 HOH 41 341 139 HOH HOH A . 
J 6 HOH 42 342 140 HOH HOH A . 
J 6 HOH 43 343 129 HOH HOH A . 
J 6 HOH 44 344 30  HOH HOH A . 
J 6 HOH 45 345 27  HOH HOH A . 
J 6 HOH 46 346 6   HOH HOH A . 
J 6 HOH 47 347 108 HOH HOH A . 
J 6 HOH 48 348 95  HOH HOH A . 
J 6 HOH 49 349 49  HOH HOH A . 
J 6 HOH 50 350 22  HOH HOH A . 
J 6 HOH 51 351 92  HOH HOH A . 
J 6 HOH 52 352 85  HOH HOH A . 
J 6 HOH 53 353 137 HOH HOH A . 
J 6 HOH 54 354 4   HOH HOH A . 
J 6 HOH 55 355 23  HOH HOH A . 
J 6 HOH 56 356 103 HOH HOH A . 
J 6 HOH 57 357 57  HOH HOH A . 
J 6 HOH 58 358 73  HOH HOH A . 
J 6 HOH 59 359 141 HOH HOH A . 
J 6 HOH 60 360 134 HOH HOH A . 
J 6 HOH 61 361 120 HOH HOH A . 
J 6 HOH 62 362 71  HOH HOH A . 
J 6 HOH 63 363 125 HOH HOH A . 
J 6 HOH 64 364 86  HOH HOH A . 
J 6 HOH 65 365 75  HOH HOH A . 
J 6 HOH 66 366 136 HOH HOH A . 
J 6 HOH 67 367 98  HOH HOH A . 
J 6 HOH 68 368 48  HOH HOH A . 
J 6 HOH 69 369 126 HOH HOH A . 
J 6 HOH 70 370 99  HOH HOH A . 
J 6 HOH 71 371 68  HOH HOH A . 
J 6 HOH 72 372 111 HOH HOH A . 
J 6 HOH 73 373 127 HOH HOH A . 
K 6 HOH 1  801 142 HOH HOH B . 
K 6 HOH 2  802 66  HOH HOH B . 
K 6 HOH 3  803 19  HOH HOH B . 
K 6 HOH 4  804 69  HOH HOH B . 
K 6 HOH 5  805 50  HOH HOH B . 
K 6 HOH 6  806 43  HOH HOH B . 
K 6 HOH 7  807 128 HOH HOH B . 
K 6 HOH 8  808 131 HOH HOH B . 
K 6 HOH 9  809 83  HOH HOH B . 
K 6 HOH 10 810 32  HOH HOH B . 
K 6 HOH 11 811 8   HOH HOH B . 
K 6 HOH 12 812 14  HOH HOH B . 
K 6 HOH 13 813 9   HOH HOH B . 
K 6 HOH 14 814 93  HOH HOH B . 
K 6 HOH 15 815 64  HOH HOH B . 
K 6 HOH 16 816 115 HOH HOH B . 
K 6 HOH 17 817 45  HOH HOH B . 
K 6 HOH 18 818 7   HOH HOH B . 
K 6 HOH 19 819 5   HOH HOH B . 
K 6 HOH 20 820 10  HOH HOH B . 
K 6 HOH 21 821 40  HOH HOH B . 
K 6 HOH 22 822 62  HOH HOH B . 
K 6 HOH 23 823 118 HOH HOH B . 
K 6 HOH 24 824 72  HOH HOH B . 
K 6 HOH 25 825 33  HOH HOH B . 
K 6 HOH 26 826 18  HOH HOH B . 
K 6 HOH 27 827 67  HOH HOH B . 
K 6 HOH 28 828 25  HOH HOH B . 
K 6 HOH 29 829 116 HOH HOH B . 
K 6 HOH 30 830 28  HOH HOH B . 
K 6 HOH 31 831 77  HOH HOH B . 
K 6 HOH 32 832 16  HOH HOH B . 
K 6 HOH 33 833 47  HOH HOH B . 
K 6 HOH 34 834 100 HOH HOH B . 
K 6 HOH 35 835 84  HOH HOH B . 
K 6 HOH 36 836 44  HOH HOH B . 
K 6 HOH 37 837 20  HOH HOH B . 
K 6 HOH 38 838 102 HOH HOH B . 
K 6 HOH 39 839 106 HOH HOH B . 
K 6 HOH 40 840 104 HOH HOH B . 
K 6 HOH 41 841 53  HOH HOH B . 
K 6 HOH 42 842 2   HOH HOH B . 
K 6 HOH 43 843 60  HOH HOH B . 
K 6 HOH 44 844 15  HOH HOH B . 
K 6 HOH 45 845 81  HOH HOH B . 
K 6 HOH 46 846 70  HOH HOH B . 
K 6 HOH 47 847 41  HOH HOH B . 
K 6 HOH 48 848 101 HOH HOH B . 
K 6 HOH 49 849 78  HOH HOH B . 
K 6 HOH 50 850 133 HOH HOH B . 
K 6 HOH 51 851 91  HOH HOH B . 
K 6 HOH 52 852 94  HOH HOH B . 
K 6 HOH 53 853 132 HOH HOH B . 
K 6 HOH 54 854 117 HOH HOH B . 
K 6 HOH 55 855 59  HOH HOH B . 
# 
loop_
_software.citation_id 
_software.classification 
_software.compiler_name 
_software.compiler_version 
_software.contact_author 
_software.contact_author_email 
_software.date 
_software.description 
_software.dependencies 
_software.hardware 
_software.language 
_software.location 
_software.mods 
_software.name 
_software.os 
_software.os_version 
_software.type 
_software.version 
_software.pdbx_ordinal 
? 'model building' ? ? ? ? ? ? ? ? ? ? ? RESOLVE ? ? ? .           1 
? refinement       ? ? ? ? ? ? ? ? ? ? ? PHENIX  ? ? ? 1.19.1_4122 2 
? 'data reduction' ? ? ? ? ? ? ? ? ? ? ? XDS     ? ? ? .           3 
? phasing          ? ? ? ? ? ? ? ? ? ? ? SOLVE   ? ? ? .           4 
? 'model building' ? ? ? ? ? ? ? ? ? ? ? Coot    ? ? ? .           5 
? 'data reduction' ? ? ? ? ? ? ? ? ? ? ? Aimless ? ? ? .           6 
# 
_cell.angle_alpha                  90.000 
_cell.angle_alpha_esd              ? 
_cell.angle_beta                   90.000 
_cell.angle_beta_esd               ? 
_cell.angle_gamma                  120.000 
_cell.angle_gamma_esd              ? 
_cell.entry_id                     9CI7 
_cell.details                      ? 
_cell.formula_units_Z              ? 
_cell.length_a                     70.630 
_cell.length_a_esd                 ? 
_cell.length_b                     70.630 
_cell.length_b_esd                 ? 
_cell.length_c                     97.165 
_cell.length_c_esd                 ? 
_cell.volume                       419780.817 
_cell.volume_esd                   ? 
_cell.Z_PDB                        6 
_cell.reciprocal_angle_alpha       ? 
_cell.reciprocal_angle_beta        ? 
_cell.reciprocal_angle_gamma       ? 
_cell.reciprocal_angle_alpha_esd   ? 
_cell.reciprocal_angle_beta_esd    ? 
_cell.reciprocal_angle_gamma_esd   ? 
_cell.reciprocal_length_a          ? 
_cell.reciprocal_length_b          ? 
_cell.reciprocal_length_c          ? 
_cell.reciprocal_length_a_esd      ? 
_cell.reciprocal_length_b_esd      ? 
_cell.reciprocal_length_c_esd      ? 
_cell.pdbx_unique_axis             ? 
_cell.pdbx_esd_method              ? 
# 
_symmetry.entry_id                         9CI7 
_symmetry.cell_setting                     ? 
_symmetry.Int_Tables_number                169 
_symmetry.space_group_name_Hall            'P 61' 
_symmetry.space_group_name_H-M             'P 61' 
_symmetry.pdbx_full_space_group_name_H-M   ? 
# 
_exptl.absorpt_coefficient_mu     ? 
_exptl.absorpt_correction_T_max   ? 
_exptl.absorpt_correction_T_min   ? 
_exptl.absorpt_correction_type    ? 
_exptl.absorpt_process_details    ? 
_exptl.entry_id                   9CI7 
_exptl.crystals_number            1 
_exptl.details                    ? 
_exptl.method                     'X-RAY DIFFRACTION' 
_exptl.method_details             ? 
# 
_exptl_crystal.colour                       ? 
_exptl_crystal.density_diffrn               ? 
_exptl_crystal.density_Matthews             3.10 
_exptl_crystal.density_method               ? 
_exptl_crystal.density_percent_sol          60.28 
_exptl_crystal.description                  ? 
_exptl_crystal.F_000                        ? 
_exptl_crystal.id                           1 
_exptl_crystal.preparation                  ? 
_exptl_crystal.size_max                     ? 
_exptl_crystal.size_mid                     ? 
_exptl_crystal.size_min                     ? 
_exptl_crystal.size_rad                     ? 
_exptl_crystal.colour_lustre                ? 
_exptl_crystal.colour_modifier              ? 
_exptl_crystal.colour_primary               ? 
_exptl_crystal.density_meas                 ? 
_exptl_crystal.density_meas_esd             ? 
_exptl_crystal.density_meas_gt              ? 
_exptl_crystal.density_meas_lt              ? 
_exptl_crystal.density_meas_temp            ? 
_exptl_crystal.density_meas_temp_esd        ? 
_exptl_crystal.density_meas_temp_gt         ? 
_exptl_crystal.density_meas_temp_lt         ? 
_exptl_crystal.pdbx_crystal_image_url       ? 
_exptl_crystal.pdbx_crystal_image_format    ? 
_exptl_crystal.pdbx_mosaicity               ? 
_exptl_crystal.pdbx_mosaicity_esd           ? 
_exptl_crystal.pdbx_mosaic_method           ? 
_exptl_crystal.pdbx_mosaic_block_size       ? 
_exptl_crystal.pdbx_mosaic_block_size_esd   ? 
# 
_exptl_crystal_grow.apparatus       ? 
_exptl_crystal_grow.atmosphere      ? 
_exptl_crystal_grow.crystal_id      1 
_exptl_crystal_grow.details         ? 
_exptl_crystal_grow.method          'VAPOR DIFFUSION' 
_exptl_crystal_grow.method_ref      ? 
_exptl_crystal_grow.pH              ? 
_exptl_crystal_grow.pressure        ? 
_exptl_crystal_grow.pressure_esd    ? 
_exptl_crystal_grow.seeding         ? 
_exptl_crystal_grow.seeding_ref     ? 
_exptl_crystal_grow.temp_details    ? 
_exptl_crystal_grow.temp_esd        ? 
_exptl_crystal_grow.time            ? 
_exptl_crystal_grow.pdbx_details    '100 mM MES pH 6.5, 1 M LiCl, 15% PEG6K' 
_exptl_crystal_grow.pdbx_pH_range   ? 
_exptl_crystal_grow.temp            298 
# 
_diffrn.ambient_environment              ? 
_diffrn.ambient_temp                     100 
_diffrn.ambient_temp_details             ? 
_diffrn.ambient_temp_esd                 ? 
_diffrn.crystal_id                       1 
_diffrn.crystal_support                  ? 
_diffrn.crystal_treatment                ? 
_diffrn.details                          ? 
_diffrn.id                               1 
_diffrn.ambient_pressure                 ? 
_diffrn.ambient_pressure_esd             ? 
_diffrn.ambient_pressure_gt              ? 
_diffrn.ambient_pressure_lt              ? 
_diffrn.ambient_temp_gt                  ? 
_diffrn.ambient_temp_lt                  ? 
_diffrn.pdbx_serial_crystal_experiment   N 
# 
_diffrn_detector.details                      ? 
_diffrn_detector.detector                     PIXEL 
_diffrn_detector.diffrn_id                    1 
_diffrn_detector.type                         'DECTRIS PILATUS 6M' 
_diffrn_detector.area_resol_mean              ? 
_diffrn_detector.dtime                        ? 
_diffrn_detector.pdbx_frames_total            ? 
_diffrn_detector.pdbx_collection_time_total   ? 
_diffrn_detector.pdbx_collection_date         2017-05-16 
_diffrn_detector.pdbx_frequency               ? 
_diffrn_detector.id                           ? 
_diffrn_detector.number_of_axes               ? 
# 
_diffrn_radiation.collimation                      ? 
_diffrn_radiation.diffrn_id                        1 
_diffrn_radiation.filter_edge                      ? 
_diffrn_radiation.inhomogeneity                    ? 
_diffrn_radiation.monochromator                    ? 
_diffrn_radiation.polarisn_norm                    ? 
_diffrn_radiation.polarisn_ratio                   ? 
_diffrn_radiation.probe                            ? 
_diffrn_radiation.type                             ? 
_diffrn_radiation.xray_symbol                      ? 
_diffrn_radiation.wavelength_id                    1 
_diffrn_radiation.pdbx_monochromatic_or_laue_m_l   M 
_diffrn_radiation.pdbx_wavelength_list             ? 
_diffrn_radiation.pdbx_wavelength                  ? 
_diffrn_radiation.pdbx_diffrn_protocol             'SINGLE WAVELENGTH' 
_diffrn_radiation.pdbx_analyzer                    ? 
_diffrn_radiation.pdbx_scattering_type             x-ray 
# 
_diffrn_radiation_wavelength.id           1 
_diffrn_radiation_wavelength.wavelength   1.192 
_diffrn_radiation_wavelength.wt           1.0 
# 
_diffrn_source.current                     ? 
_diffrn_source.details                     ? 
_diffrn_source.diffrn_id                   1 
_diffrn_source.power                       ? 
_diffrn_source.size                        ? 
_diffrn_source.source                      SYNCHROTRON 
_diffrn_source.target                      ? 
_diffrn_source.type                        'SSRL BEAMLINE BL12-2' 
_diffrn_source.voltage                     ? 
_diffrn_source.take-off_angle              ? 
_diffrn_source.pdbx_wavelength_list        1.192 
_diffrn_source.pdbx_wavelength             ? 
_diffrn_source.pdbx_synchrotron_beamline   BL12-2 
_diffrn_source.pdbx_synchrotron_site       SSRL 
# 
_reflns.B_iso_Wilson_estimate                          38.74 
_reflns.entry_id                                       9CI7 
_reflns.data_reduction_details                         ? 
_reflns.data_reduction_method                          ? 
_reflns.d_resolution_high                              2.10 
_reflns.d_resolution_low                               38.04 
_reflns.details                                        ? 
_reflns.limit_h_max                                    ? 
_reflns.limit_h_min                                    ? 
_reflns.limit_k_max                                    ? 
_reflns.limit_k_min                                    ? 
_reflns.limit_l_max                                    ? 
_reflns.limit_l_min                                    ? 
_reflns.number_all                                     ? 
_reflns.number_obs                                     15943 
_reflns.observed_criterion                             ? 
_reflns.observed_criterion_F_max                       ? 
_reflns.observed_criterion_F_min                       ? 
_reflns.observed_criterion_I_max                       ? 
_reflns.observed_criterion_I_min                       ? 
_reflns.observed_criterion_sigma_F                     ? 
_reflns.observed_criterion_sigma_I                     ? 
_reflns.percent_possible_obs                           98.8 
_reflns.R_free_details                                 ? 
_reflns.Rmerge_F_all                                   ? 
_reflns.Rmerge_F_obs                                   ? 
_reflns.Friedel_coverage                               ? 
_reflns.number_gt                                      ? 
_reflns.threshold_expression                           ? 
_reflns.pdbx_redundancy                                2.8 
_reflns.pdbx_netI_over_av_sigmaI                       ? 
_reflns.pdbx_netI_over_sigmaI                          9.0 
_reflns.pdbx_res_netI_over_av_sigmaI_2                 ? 
_reflns.pdbx_res_netI_over_sigmaI_2                    ? 
_reflns.pdbx_chi_squared                               ? 
_reflns.pdbx_scaling_rejects                           ? 
_reflns.pdbx_d_res_high_opt                            ? 
_reflns.pdbx_d_res_low_opt                             ? 
_reflns.pdbx_d_res_opt_method                          ? 
_reflns.phase_calculation_details                      ? 
_reflns.pdbx_Rrim_I_all                                ? 
_reflns.pdbx_Rpim_I_all                                ? 
_reflns.pdbx_d_opt                                     ? 
_reflns.pdbx_number_measured_all                       ? 
_reflns.pdbx_diffrn_id                                 1 
_reflns.pdbx_ordinal                                   1 
_reflns.pdbx_CC_half                                   0.973 
_reflns.pdbx_CC_star                                   ? 
_reflns.pdbx_R_split                                   ? 
_reflns.pdbx_Rmerge_I_obs                              0.067 
_reflns.pdbx_Rmerge_I_all                              ? 
_reflns.pdbx_Rsym_value                                ? 
_reflns.pdbx_CC_split_method                           ? 
_reflns.pdbx_aniso_diffraction_limit_axis_1_ortho[1]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_1_ortho[2]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_1_ortho[3]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_2_ortho[1]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_2_ortho[2]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_2_ortho[3]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_3_ortho[1]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_3_ortho[2]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_3_ortho[3]   ? 
_reflns.pdbx_aniso_diffraction_limit_1                 ? 
_reflns.pdbx_aniso_diffraction_limit_2                 ? 
_reflns.pdbx_aniso_diffraction_limit_3                 ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_1_ortho[1]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_1_ortho[2]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_1_ortho[3]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_2_ortho[1]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_2_ortho[2]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_2_ortho[3]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_3_ortho[1]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_3_ortho[2]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_3_ortho[3]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvalue_1               ? 
_reflns.pdbx_aniso_B_tensor_eigenvalue_2               ? 
_reflns.pdbx_aniso_B_tensor_eigenvalue_3               ? 
_reflns.pdbx_orthogonalization_convention              ? 
_reflns.pdbx_percent_possible_ellipsoidal              ? 
_reflns.pdbx_percent_possible_spherical                ? 
_reflns.pdbx_percent_possible_ellipsoidal_anomalous    ? 
_reflns.pdbx_percent_possible_spherical_anomalous      ? 
_reflns.pdbx_redundancy_anomalous                      ? 
_reflns.pdbx_CC_half_anomalous                         ? 
_reflns.pdbx_absDiff_over_sigma_anomalous              ? 
_reflns.pdbx_percent_possible_anomalous                ? 
_reflns.pdbx_observed_signal_threshold                 ? 
_reflns.pdbx_signal_type                               ? 
_reflns.pdbx_signal_details                            ? 
_reflns.pdbx_signal_software_id                        ? 
# 
_reflns_shell.d_res_high                                    2.10 
_reflns_shell.d_res_low                                     2.16 
_reflns_shell.meanI_over_sigI_all                           ? 
_reflns_shell.meanI_over_sigI_obs                           ? 
_reflns_shell.number_measured_all                           ? 
_reflns_shell.number_measured_obs                           ? 
_reflns_shell.number_possible                               ? 
_reflns_shell.number_unique_all                             ? 
_reflns_shell.number_unique_obs                             1260 
_reflns_shell.percent_possible_obs                          ? 
_reflns_shell.Rmerge_F_all                                  ? 
_reflns_shell.Rmerge_F_obs                                  ? 
_reflns_shell.meanI_over_sigI_gt                            ? 
_reflns_shell.meanI_over_uI_all                             ? 
_reflns_shell.meanI_over_uI_gt                              ? 
_reflns_shell.number_measured_gt                            ? 
_reflns_shell.number_unique_gt                              ? 
_reflns_shell.percent_possible_gt                           ? 
_reflns_shell.Rmerge_F_gt                                   ? 
_reflns_shell.Rmerge_I_gt                                   ? 
_reflns_shell.pdbx_redundancy                               ? 
_reflns_shell.pdbx_chi_squared                              ? 
_reflns_shell.pdbx_netI_over_sigmaI_all                     ? 
_reflns_shell.pdbx_netI_over_sigmaI_obs                     ? 
_reflns_shell.pdbx_Rrim_I_all                               ? 
_reflns_shell.pdbx_Rpim_I_all                               ? 
_reflns_shell.pdbx_rejects                                  ? 
_reflns_shell.pdbx_ordinal                                  1 
_reflns_shell.pdbx_diffrn_id                                1 
_reflns_shell.pdbx_CC_half                                  0.735 
_reflns_shell.pdbx_CC_star                                  ? 
_reflns_shell.pdbx_R_split                                  ? 
_reflns_shell.percent_possible_all                          ? 
_reflns_shell.Rmerge_I_all                                  ? 
_reflns_shell.Rmerge_I_obs                                  0.498 
_reflns_shell.pdbx_Rsym_value                               ? 
_reflns_shell.pdbx_percent_possible_ellipsoidal             ? 
_reflns_shell.pdbx_percent_possible_spherical               ? 
_reflns_shell.pdbx_percent_possible_ellipsoidal_anomalous   ? 
_reflns_shell.pdbx_percent_possible_spherical_anomalous     ? 
_reflns_shell.pdbx_redundancy_anomalous                     ? 
_reflns_shell.pdbx_CC_half_anomalous                        ? 
_reflns_shell.pdbx_absDiff_over_sigma_anomalous             ? 
_reflns_shell.pdbx_percent_possible_anomalous               ? 
# 
_refine.aniso_B[1][1]                            ? 
_refine.aniso_B[1][2]                            ? 
_refine.aniso_B[1][3]                            ? 
_refine.aniso_B[2][2]                            ? 
_refine.aniso_B[2][3]                            ? 
_refine.aniso_B[3][3]                            ? 
_refine.B_iso_max                                ? 
_refine.B_iso_mean                               46.32 
_refine.B_iso_min                                ? 
_refine.correlation_coeff_Fo_to_Fc               ? 
_refine.correlation_coeff_Fo_to_Fc_free          ? 
_refine.details                                  ? 
_refine.diff_density_max                         ? 
_refine.diff_density_max_esd                     ? 
_refine.diff_density_min                         ? 
_refine.diff_density_min_esd                     ? 
_refine.diff_density_rms                         ? 
_refine.diff_density_rms_esd                     ? 
_refine.entry_id                                 9CI7 
_refine.pdbx_refine_id                           'X-RAY DIFFRACTION' 
_refine.ls_abs_structure_details                 ? 
_refine.ls_abs_structure_Flack                   ? 
_refine.ls_abs_structure_Flack_esd               ? 
_refine.ls_abs_structure_Rogers                  ? 
_refine.ls_abs_structure_Rogers_esd              ? 
_refine.ls_d_res_high                            2.10 
_refine.ls_d_res_low                             35.32 
_refine.ls_extinction_coef                       ? 
_refine.ls_extinction_coef_esd                   ? 
_refine.ls_extinction_expression                 ? 
_refine.ls_extinction_method                     ? 
_refine.ls_goodness_of_fit_all                   ? 
_refine.ls_goodness_of_fit_all_esd               ? 
_refine.ls_goodness_of_fit_obs                   ? 
_refine.ls_goodness_of_fit_obs_esd               ? 
_refine.ls_hydrogen_treatment                    ? 
_refine.ls_matrix_type                           ? 
_refine.ls_number_constraints                    ? 
_refine.ls_number_parameters                     ? 
_refine.ls_number_reflns_all                     ? 
_refine.ls_number_reflns_obs                     15916 
_refine.ls_number_reflns_R_free                  783 
_refine.ls_number_reflns_R_work                  15133 
_refine.ls_number_restraints                     ? 
_refine.ls_percent_reflns_obs                    98.73 
_refine.ls_percent_reflns_R_free                 4.92 
_refine.ls_R_factor_all                          ? 
_refine.ls_R_factor_obs                          0.1896 
_refine.ls_R_factor_R_free                       0.2167 
_refine.ls_R_factor_R_free_error                 ? 
_refine.ls_R_factor_R_free_error_details         ? 
_refine.ls_R_factor_R_work                       0.1882 
_refine.ls_R_Fsqd_factor_obs                     ? 
_refine.ls_R_I_factor_obs                        ? 
_refine.ls_redundancy_reflns_all                 ? 
_refine.ls_redundancy_reflns_obs                 ? 
_refine.ls_restrained_S_all                      ? 
_refine.ls_restrained_S_obs                      ? 
_refine.ls_shift_over_esd_max                    ? 
_refine.ls_shift_over_esd_mean                   ? 
_refine.ls_structure_factor_coef                 ? 
_refine.ls_weighting_details                     ? 
_refine.ls_weighting_scheme                      ? 
_refine.ls_wR_factor_all                         ? 
_refine.ls_wR_factor_obs                         ? 
_refine.ls_wR_factor_R_free                      ? 
_refine.ls_wR_factor_R_work                      ? 
_refine.occupancy_max                            ? 
_refine.occupancy_min                            ? 
_refine.solvent_model_details                    'FLAT BULK SOLVENT MODEL' 
_refine.solvent_model_param_bsol                 ? 
_refine.solvent_model_param_ksol                 ? 
_refine.pdbx_R_complete                          ? 
_refine.ls_R_factor_gt                           ? 
_refine.ls_goodness_of_fit_gt                    ? 
_refine.ls_goodness_of_fit_ref                   ? 
_refine.ls_shift_over_su_max                     ? 
_refine.ls_shift_over_su_max_lt                  ? 
_refine.ls_shift_over_su_mean                    ? 
_refine.ls_shift_over_su_mean_lt                 ? 
_refine.pdbx_ls_sigma_I                          ? 
_refine.pdbx_ls_sigma_F                          1.35 
_refine.pdbx_ls_sigma_Fsqd                       ? 
_refine.pdbx_data_cutoff_high_absF               ? 
_refine.pdbx_data_cutoff_high_rms_absF           ? 
_refine.pdbx_data_cutoff_low_absF                ? 
_refine.pdbx_isotropic_thermal_model             ? 
_refine.pdbx_ls_cross_valid_method               'FREE R-VALUE' 
_refine.pdbx_method_to_determine_struct          MAD 
_refine.pdbx_starting_model                      ? 
_refine.pdbx_stereochemistry_target_values       'GeoStd + Monomer Library + CDL v1.2' 
_refine.pdbx_R_Free_selection_details            ? 
_refine.pdbx_stereochem_target_val_spec_case     ? 
_refine.pdbx_overall_ESU_R                       ? 
_refine.pdbx_overall_ESU_R_Free                  ? 
_refine.pdbx_solvent_vdw_probe_radii             1.1100 
_refine.pdbx_solvent_ion_probe_radii             ? 
_refine.pdbx_solvent_shrinkage_radii             0.9000 
_refine.pdbx_real_space_R                        ? 
_refine.pdbx_density_correlation                 ? 
_refine.pdbx_pd_number_of_powder_patterns        ? 
_refine.pdbx_pd_number_of_points                 ? 
_refine.pdbx_pd_meas_number_of_points            ? 
_refine.pdbx_pd_proc_ls_prof_R_factor            ? 
_refine.pdbx_pd_proc_ls_prof_wR_factor           ? 
_refine.pdbx_pd_Marquardt_correlation_coeff      ? 
_refine.pdbx_pd_Fsqrd_R_factor                   ? 
_refine.pdbx_pd_ls_matrix_band_width             ? 
_refine.pdbx_overall_phase_error                 23.8137 
_refine.pdbx_overall_SU_R_free_Cruickshank_DPI   ? 
_refine.pdbx_overall_SU_R_free_Blow_DPI          ? 
_refine.pdbx_overall_SU_R_Blow_DPI               ? 
_refine.pdbx_TLS_residual_ADP_flag               ? 
_refine.pdbx_diffrn_id                           1 
_refine.overall_SU_B                             ? 
_refine.overall_SU_ML                            0.2166 
_refine.overall_SU_R_Cruickshank_DPI             ? 
_refine.overall_SU_R_free                        ? 
_refine.overall_FOM_free_R_set                   ? 
_refine.overall_FOM_work_R_set                   ? 
_refine.pdbx_average_fsc_overall                 ? 
_refine.pdbx_average_fsc_work                    ? 
_refine.pdbx_average_fsc_free                    ? 
# 
_refine_hist.pdbx_refine_id                   'X-RAY DIFFRACTION' 
_refine_hist.cycle_id                         LAST 
_refine_hist.details                          ? 
_refine_hist.d_res_high                       2.10 
_refine_hist.d_res_low                        35.32 
_refine_hist.number_atoms_solvent             128 
_refine_hist.number_atoms_total               1716 
_refine_hist.number_reflns_all                ? 
_refine_hist.number_reflns_obs                ? 
_refine_hist.number_reflns_R_free             ? 
_refine_hist.number_reflns_R_work             ? 
_refine_hist.R_factor_all                     ? 
_refine_hist.R_factor_obs                     ? 
_refine_hist.R_factor_R_free                  ? 
_refine_hist.R_factor_R_work                  ? 
_refine_hist.pdbx_number_residues_total       ? 
_refine_hist.pdbx_B_iso_mean_ligand           ? 
_refine_hist.pdbx_B_iso_mean_solvent          ? 
_refine_hist.pdbx_number_atoms_protein        1581 
_refine_hist.pdbx_number_atoms_nucleic_acid   0 
_refine_hist.pdbx_number_atoms_ligand         7 
_refine_hist.pdbx_number_atoms_lipid          ? 
_refine_hist.pdbx_number_atoms_carb           ? 
_refine_hist.pdbx_pseudo_atom_details         ? 
# 
loop_
_refine_ls_restr.pdbx_refine_id 
_refine_ls_restr.criterion 
_refine_ls_restr.dev_ideal 
_refine_ls_restr.dev_ideal_target 
_refine_ls_restr.number 
_refine_ls_restr.rejects 
_refine_ls_restr.type 
_refine_ls_restr.weight 
_refine_ls_restr.pdbx_restraint_function 
'X-RAY DIFFRACTION' ? 0.0012  ? 1629 ? f_bond_d           ? ? 
'X-RAY DIFFRACTION' ? 0.3360  ? 2204 ? f_angle_d          ? ? 
'X-RAY DIFFRACTION' ? 0.0326  ? 258  ? f_chiral_restr     ? ? 
'X-RAY DIFFRACTION' ? 0.0025  ? 276  ? f_plane_restr      ? ? 
'X-RAY DIFFRACTION' ? 10.0886 ? 619  ? f_dihedral_angle_d ? ? 
# 
loop_
_refine_ls_shell.pdbx_refine_id 
_refine_ls_shell.d_res_high 
_refine_ls_shell.d_res_low 
_refine_ls_shell.number_reflns_all 
_refine_ls_shell.number_reflns_obs 
_refine_ls_shell.number_reflns_R_free 
_refine_ls_shell.number_reflns_R_work 
_refine_ls_shell.percent_reflns_obs 
_refine_ls_shell.percent_reflns_R_free 
_refine_ls_shell.R_factor_all 
_refine_ls_shell.R_factor_obs 
_refine_ls_shell.R_factor_R_free_error 
_refine_ls_shell.R_factor_R_work 
_refine_ls_shell.redundancy_reflns_all 
_refine_ls_shell.redundancy_reflns_obs 
_refine_ls_shell.wR_factor_all 
_refine_ls_shell.wR_factor_obs 
_refine_ls_shell.wR_factor_R_free 
_refine_ls_shell.wR_factor_R_work 
_refine_ls_shell.pdbx_R_complete 
_refine_ls_shell.pdbx_total_number_of_bins_used 
_refine_ls_shell.pdbx_phase_error 
_refine_ls_shell.pdbx_fsc_work 
_refine_ls_shell.pdbx_fsc_free 
_refine_ls_shell.R_factor_R_free 
'X-RAY DIFFRACTION' 2.10 2.23  . . 140 2459 97.12 . . . . 0.2476 . . . . . . . . . . . 0.2888 
'X-RAY DIFFRACTION' 2.23 2.40  . . 121 2539 99.25 . . . . 0.2041 . . . . . . . . . . . 0.2261 
'X-RAY DIFFRACTION' 2.40 2.64  . . 142 2517 99.55 . . . . 0.2413 . . . . . . . . . . . 0.2749 
'X-RAY DIFFRACTION' 2.64 3.03  . . 140 2512 98.66 . . . . 0.2216 . . . . . . . . . . . 0.2703 
'X-RAY DIFFRACTION' 3.03 3.81  . . 107 2569 99.78 . . . . 0.1987 . . . . . . . . . . . 0.2269 
'X-RAY DIFFRACTION' 3.81 35.32 . . 133 2537 98.13 . . . . 0.1455 . . . . . . . . . . . 0.1555 
# 
_struct.entry_id                     9CI7 
_struct.title                        'Structure of PNUTS:Tox4 complex' 
_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        9CI7 
_struct_keywords.text            
;PNUTS, PPP1R10, Transcriptional elongation factor S-II homology N-terminal domain. Tox4, zinc binding protein, complex, SIGNALING PROTEIN
;
_struct_keywords.pdbx_keywords   'SIGNALING PROTEIN' 
# 
loop_
_struct_asym.id 
_struct_asym.pdbx_blank_PDB_chainid_flag 
_struct_asym.pdbx_modified 
_struct_asym.entity_id 
_struct_asym.details 
A N N 1 ? 
B N N 2 ? 
C N N 3 ? 
D N N 3 ? 
E N N 3 ? 
F N N 4 ? 
G N N 5 ? 
H N N 4 ? 
I N N 3 ? 
J N N 6 ? 
K N N 6 ? 
# 
loop_
_struct_ref.id 
_struct_ref.db_name 
_struct_ref.db_code 
_struct_ref.pdbx_db_accession 
_struct_ref.pdbx_db_isoform 
_struct_ref.entity_id 
_struct_ref.pdbx_seq_one_letter_code 
_struct_ref.pdbx_align_begin 
1 UNP PP1RA_RAT  O55000 ? 1 
;PIDPKELLKGLDSFLTRDGEVKSVDGIAKIFSLMKEARKMVSRCTYLNIILQTRAPEVLVKFIDVGGYKLLNSWLTYSKT
TNNIPLLQQILLTLQHLPLTVDHLKQNNTAKLVKQLSKSSEDEELRKLASVLVSDWMAVIRSQSSTQPAEKDKKKR
;
5   
2 UNP TOX4_HUMAN O94842 ? 2 RCVRSGCENPPIVSKDWDNEYCSNECVVKHCRDVFLAWVASRNSNTVVFVK 571 
# 
loop_
_struct_ref_seq.align_id 
_struct_ref_seq.ref_id 
_struct_ref_seq.pdbx_PDB_id_code 
_struct_ref_seq.pdbx_strand_id 
_struct_ref_seq.seq_align_beg 
_struct_ref_seq.pdbx_seq_align_beg_ins_code 
_struct_ref_seq.seq_align_end 
_struct_ref_seq.pdbx_seq_align_end_ins_code 
_struct_ref_seq.pdbx_db_accession 
_struct_ref_seq.db_align_beg 
_struct_ref_seq.pdbx_db_align_beg_ins_code 
_struct_ref_seq.db_align_end 
_struct_ref_seq.pdbx_db_align_end_ins_code 
_struct_ref_seq.pdbx_auth_seq_align_beg 
_struct_ref_seq.pdbx_auth_seq_align_end 
1 1 9CI7 A 4 ? 159 ? O55000 5   ? 160 ? 5   160 
2 2 9CI7 B 4 ? 54  ? O94842 571 ? 621 ? 571 621 
# 
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 9CI7 GLY A 1  ? UNP O55000 ?   ?   'expression tag'      2   1 
1 9CI7 HIS A 2  ? UNP O55000 ?   ?   'expression tag'      3   2 
1 9CI7 MET A 3  ? UNP O55000 ?   ?   'expression tag'      4   3 
1 9CI7 SER A 47 ? UNP O55000 CYS 48  'engineered mutation' 48  4 
2 9CI7 GLY B 1  ? UNP O94842 ?   ?   'expression tag'      568 5 
2 9CI7 HIS B 2  ? UNP O94842 ?   ?   'expression tag'      569 6 
2 9CI7 MET B 3  ? UNP O94842 ?   ?   'expression tag'      570 7 
2 9CI7 SER B 34 ? UNP O94842 CYS 601 'engineered mutation' 601 8 
# 
_pdbx_struct_assembly.id                   1 
_pdbx_struct_assembly.details              author_and_software_defined_assembly 
_pdbx_struct_assembly.method_details       PISA 
_pdbx_struct_assembly.oligomeric_details   dimeric 
_pdbx_struct_assembly.oligomeric_count     2 
# 
loop_
_pdbx_struct_assembly_prop.biol_id 
_pdbx_struct_assembly_prop.type 
_pdbx_struct_assembly_prop.value 
_pdbx_struct_assembly_prop.details 
1 'ABSA (A^2)' 2970  ? 
1 MORE         -90   ? 
1 'SSA (A^2)'  10930 ? 
# 
_pdbx_struct_assembly_gen.assembly_id       1 
_pdbx_struct_assembly_gen.oper_expression   1 
_pdbx_struct_assembly_gen.asym_id_list      A,B,C,D,E,F,G,H,I,J,K 
# 
_pdbx_struct_oper_list.id                   1 
_pdbx_struct_oper_list.type                 'identity operation' 
_pdbx_struct_oper_list.name                 1_555 
_pdbx_struct_oper_list.symmetry_operation   x,y,z 
_pdbx_struct_oper_list.matrix[1][1]         1.0000000000 
_pdbx_struct_oper_list.matrix[1][2]         0.0000000000 
_pdbx_struct_oper_list.matrix[1][3]         0.0000000000 
_pdbx_struct_oper_list.vector[1]            0.0000000000 
_pdbx_struct_oper_list.matrix[2][1]         0.0000000000 
_pdbx_struct_oper_list.matrix[2][2]         1.0000000000 
_pdbx_struct_oper_list.matrix[2][3]         0.0000000000 
_pdbx_struct_oper_list.vector[2]            0.0000000000 
_pdbx_struct_oper_list.matrix[3][1]         0.0000000000 
_pdbx_struct_oper_list.matrix[3][2]         0.0000000000 
_pdbx_struct_oper_list.matrix[3][3]         1.0000000000 
_pdbx_struct_oper_list.vector[3]            0.0000000000 
# 
loop_
_struct_conf.conf_type_id 
_struct_conf.id 
_struct_conf.pdbx_PDB_helix_id 
_struct_conf.beg_label_comp_id 
_struct_conf.beg_label_asym_id 
_struct_conf.beg_label_seq_id 
_struct_conf.pdbx_beg_PDB_ins_code 
_struct_conf.end_label_comp_id 
_struct_conf.end_label_asym_id 
_struct_conf.end_label_seq_id 
_struct_conf.pdbx_end_PDB_ins_code 
_struct_conf.beg_auth_comp_id 
_struct_conf.beg_auth_asym_id 
_struct_conf.beg_auth_seq_id 
_struct_conf.end_auth_comp_id 
_struct_conf.end_auth_asym_id 
_struct_conf.end_auth_seq_id 
_struct_conf.pdbx_PDB_helix_class 
_struct_conf.details 
_struct_conf.pdbx_PDB_helix_length 
HELX_P HELX_P1  AA1 ASP A 6   ? LEU A 14  ? ASP A 7   LEU A 15  1 ? 9  
HELX_P HELX_P2  AA2 SER A 26  ? GLU A 39  ? SER A 27  GLU A 40  1 ? 14 
HELX_P HELX_P3  AA3 LYS A 42  ? THR A 56  ? LYS A 43  THR A 57  1 ? 15 
HELX_P HELX_P4  AA4 ALA A 58  ? VAL A 68  ? ALA A 59  VAL A 69  1 ? 11 
HELX_P HELX_P5  AA5 GLY A 69  ? THR A 84  ? GLY A 70  THR A 85  1 ? 16 
HELX_P HELX_P6  AA6 ASN A 86  ? LEU A 100 ? ASN A 87  LEU A 101 1 ? 15 
HELX_P HELX_P7  AA7 THR A 103 ? LYS A 108 ? THR A 104 LYS A 109 1 ? 6  
HELX_P HELX_P8  AA8 ASN A 111 ? SER A 123 ? ASN A 112 SER A 124 1 ? 13 
HELX_P HELX_P9  AA9 ASP A 125 ? SER A 145 ? ASP A 126 SER A 146 1 ? 21 
HELX_P HELX_P10 AB1 SER B 26  ? ARG B 45  ? SER B 593 ARG B 612 1 ? 20 
# 
_struct_conf_type.id          HELX_P 
_struct_conf_type.criteria    ? 
_struct_conf_type.reference   ? 
# 
loop_
_struct_conn.id 
_struct_conn.conn_type_id 
_struct_conn.pdbx_leaving_atom_flag 
_struct_conn.pdbx_PDB_id 
_struct_conn.ptnr1_label_asym_id 
_struct_conn.ptnr1_label_comp_id 
_struct_conn.ptnr1_label_seq_id 
_struct_conn.ptnr1_label_atom_id 
_struct_conn.pdbx_ptnr1_label_alt_id 
_struct_conn.pdbx_ptnr1_PDB_ins_code 
_struct_conn.pdbx_ptnr1_standard_comp_id 
_struct_conn.ptnr1_symmetry 
_struct_conn.ptnr2_label_asym_id 
_struct_conn.ptnr2_label_comp_id 
_struct_conn.ptnr2_label_seq_id 
_struct_conn.ptnr2_label_atom_id 
_struct_conn.pdbx_ptnr2_label_alt_id 
_struct_conn.pdbx_ptnr2_PDB_ins_code 
_struct_conn.ptnr1_auth_asym_id 
_struct_conn.ptnr1_auth_comp_id 
_struct_conn.ptnr1_auth_seq_id 
_struct_conn.ptnr2_auth_asym_id 
_struct_conn.ptnr2_auth_comp_id 
_struct_conn.ptnr2_auth_seq_id 
_struct_conn.ptnr2_symmetry 
_struct_conn.pdbx_ptnr3_label_atom_id 
_struct_conn.pdbx_ptnr3_label_seq_id 
_struct_conn.pdbx_ptnr3_label_comp_id 
_struct_conn.pdbx_ptnr3_label_asym_id 
_struct_conn.pdbx_ptnr3_label_alt_id 
_struct_conn.pdbx_ptnr3_PDB_ins_code 
_struct_conn.details 
_struct_conn.pdbx_dist_value 
_struct_conn.pdbx_value_order 
_struct_conn.pdbx_role 
metalc1 metalc ? ? A HIS 2  NE2 ? ? ? 1_555 F ZN  . ZN  ? ? A HIS 3   A ZN  204 1_555 ? ? ? ? ? ? ? 2.034 ? ? 
metalc2 metalc ? ? A HIS 99 ND1 ? ? ? 1_555 F ZN  . ZN  ? ? A HIS 100 A ZN  204 6_655 ? ? ? ? ? ? ? 2.284 ? ? 
metalc3 metalc ? ? F ZN  .  ZN  ? ? ? 1_555 B HIS 2 NE2 ? ? A ZN  204 B HIS 569 1_555 ? ? ? ? ? ? ? 2.022 ? ? 
metalc4 metalc ? ? B CYS 5  SG  ? ? ? 1_555 H ZN  . ZN  ? ? B CYS 572 B ZN  701 1_555 ? ? ? ? ? ? ? 2.345 ? ? 
metalc5 metalc ? ? B CYS 10 SG  ? ? ? 1_555 H ZN  . ZN  ? ? B CYS 577 B ZN  701 1_555 ? ? ? ? ? ? ? 2.304 ? ? 
metalc6 metalc ? ? B CYS 25 SG  ? ? ? 1_555 H ZN  . ZN  ? ? B CYS 592 B ZN  701 1_555 ? ? ? ? ? ? ? 2.318 ? ? 
metalc7 metalc ? ? B CYS 29 SG  ? ? ? 1_555 H ZN  . ZN  ? ? B CYS 596 B ZN  701 1_555 ? ? ? ? ? ? ? 2.328 ? ? 
# 
_struct_conn_type.id          metalc 
_struct_conn_type.criteria    ? 
_struct_conn_type.reference   ? 
# 
loop_
_pdbx_struct_conn_angle.id 
_pdbx_struct_conn_angle.ptnr1_label_atom_id 
_pdbx_struct_conn_angle.ptnr1_label_alt_id 
_pdbx_struct_conn_angle.ptnr1_label_asym_id 
_pdbx_struct_conn_angle.ptnr1_label_comp_id 
_pdbx_struct_conn_angle.ptnr1_label_seq_id 
_pdbx_struct_conn_angle.ptnr1_auth_atom_id 
_pdbx_struct_conn_angle.ptnr1_auth_asym_id 
_pdbx_struct_conn_angle.ptnr1_auth_comp_id 
_pdbx_struct_conn_angle.ptnr1_auth_seq_id 
_pdbx_struct_conn_angle.ptnr1_PDB_ins_code 
_pdbx_struct_conn_angle.ptnr1_symmetry 
_pdbx_struct_conn_angle.ptnr2_label_atom_id 
_pdbx_struct_conn_angle.ptnr2_label_alt_id 
_pdbx_struct_conn_angle.ptnr2_label_asym_id 
_pdbx_struct_conn_angle.ptnr2_label_comp_id 
_pdbx_struct_conn_angle.ptnr2_label_seq_id 
_pdbx_struct_conn_angle.ptnr2_auth_atom_id 
_pdbx_struct_conn_angle.ptnr2_auth_asym_id 
_pdbx_struct_conn_angle.ptnr2_auth_comp_id 
_pdbx_struct_conn_angle.ptnr2_auth_seq_id 
_pdbx_struct_conn_angle.ptnr2_PDB_ins_code 
_pdbx_struct_conn_angle.ptnr2_symmetry 
_pdbx_struct_conn_angle.ptnr3_label_atom_id 
_pdbx_struct_conn_angle.ptnr3_label_alt_id 
_pdbx_struct_conn_angle.ptnr3_label_asym_id 
_pdbx_struct_conn_angle.ptnr3_label_comp_id 
_pdbx_struct_conn_angle.ptnr3_label_seq_id 
_pdbx_struct_conn_angle.ptnr3_auth_atom_id 
_pdbx_struct_conn_angle.ptnr3_auth_asym_id 
_pdbx_struct_conn_angle.ptnr3_auth_comp_id 
_pdbx_struct_conn_angle.ptnr3_auth_seq_id 
_pdbx_struct_conn_angle.ptnr3_PDB_ins_code 
_pdbx_struct_conn_angle.ptnr3_symmetry 
_pdbx_struct_conn_angle.value 
_pdbx_struct_conn_angle.value_esd 
1 NE2 ? A HIS 2  ? A HIS 3   ? 1_555 ZN ? F ZN . ? A ZN 204 ? 1_555 ND1 ? A HIS 99 ? A HIS 100 ? 1_555 76.7  ? 
2 NE2 ? A HIS 2  ? A HIS 3   ? 1_555 ZN ? F ZN . ? A ZN 204 ? 1_555 NE2 ? B HIS 2  ? B HIS 569 ? 1_555 115.7 ? 
3 ND1 ? A HIS 99 ? A HIS 100 ? 1_555 ZN ? F ZN . ? A ZN 204 ? 1_555 NE2 ? B HIS 2  ? B HIS 569 ? 1_555 81.0  ? 
4 SG  ? B CYS 5  ? B CYS 572 ? 1_555 ZN ? H ZN . ? B ZN 701 ? 1_555 SG  ? B CYS 10 ? B CYS 577 ? 1_555 111.1 ? 
5 SG  ? B CYS 5  ? B CYS 572 ? 1_555 ZN ? H ZN . ? B ZN 701 ? 1_555 SG  ? B CYS 25 ? B CYS 592 ? 1_555 116.9 ? 
6 SG  ? B CYS 10 ? B CYS 577 ? 1_555 ZN ? H ZN . ? B ZN 701 ? 1_555 SG  ? B CYS 25 ? B CYS 592 ? 1_555 104.4 ? 
7 SG  ? B CYS 5  ? B CYS 572 ? 1_555 ZN ? H ZN . ? B ZN 701 ? 1_555 SG  ? B CYS 29 ? B CYS 596 ? 1_555 108.6 ? 
8 SG  ? B CYS 10 ? B CYS 577 ? 1_555 ZN ? H ZN . ? B ZN 701 ? 1_555 SG  ? B CYS 29 ? B CYS 596 ? 1_555 115.0 ? 
9 SG  ? B CYS 25 ? B CYS 592 ? 1_555 ZN ? H ZN . ? B ZN 701 ? 1_555 SG  ? B CYS 29 ? B CYS 596 ? 1_555 100.7 ? 
# 
_pdbx_entry_details.entry_id                   9CI7 
_pdbx_entry_details.has_ligand_of_interest     N 
_pdbx_entry_details.compound_details           ? 
_pdbx_entry_details.source_details             ? 
_pdbx_entry_details.nonpolymer_details         ? 
_pdbx_entry_details.sequence_details           ? 
_pdbx_entry_details.has_protein_modification   N 
# 
_pdbx_validate_torsion.id              1 
_pdbx_validate_torsion.PDB_model_num   1 
_pdbx_validate_torsion.auth_comp_id    ASN 
_pdbx_validate_torsion.auth_asym_id    B 
_pdbx_validate_torsion.auth_seq_id     613 
_pdbx_validate_torsion.PDB_ins_code    ? 
_pdbx_validate_torsion.label_alt_id    ? 
_pdbx_validate_torsion.phi             -103.82 
_pdbx_validate_torsion.psi             -169.11 
# 
loop_
_space_group_symop.id 
_space_group_symop.operation_xyz 
1 x,y,z         
2 x-y,x,z+1/6   
3 y,-x+y,z+5/6  
4 -y,x-y,z+1/3  
5 -x+y,-x,z+2/3 
6 -x,-y,z+1/2   
# 
loop_
_pdbx_unobs_or_zero_occ_residues.id 
_pdbx_unobs_or_zero_occ_residues.PDB_model_num 
_pdbx_unobs_or_zero_occ_residues.polymer_flag 
_pdbx_unobs_or_zero_occ_residues.occupancy_flag 
_pdbx_unobs_or_zero_occ_residues.auth_asym_id 
_pdbx_unobs_or_zero_occ_residues.auth_comp_id 
_pdbx_unobs_or_zero_occ_residues.auth_seq_id 
_pdbx_unobs_or_zero_occ_residues.PDB_ins_code 
_pdbx_unobs_or_zero_occ_residues.label_asym_id 
_pdbx_unobs_or_zero_occ_residues.label_comp_id 
_pdbx_unobs_or_zero_occ_residues.label_seq_id 
1  1 Y 1 A SER 148 ? A SER 147 
2  1 Y 1 A SER 149 ? A SER 148 
3  1 Y 1 A THR 150 ? A THR 149 
4  1 Y 1 A GLN 151 ? A GLN 150 
5  1 Y 1 A PRO 152 ? A PRO 151 
6  1 Y 1 A ALA 153 ? A ALA 152 
7  1 Y 1 A GLU 154 ? A GLU 153 
8  1 Y 1 A LYS 155 ? A LYS 154 
9  1 Y 1 A ASP 156 ? A ASP 155 
10 1 Y 1 A LYS 157 ? A LYS 156 
11 1 Y 1 A LYS 158 ? A LYS 157 
12 1 Y 1 A LYS 159 ? A LYS 158 
13 1 Y 1 A ARG 160 ? A ARG 159 
14 1 Y 1 B LYS 621 ? B LYS 54  
# 
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  
CL  CL   CL N N 74  
CYS N    N  N N 75  
CYS CA   C  N R 76  
CYS C    C  N N 77  
CYS O    O  N N 78  
CYS CB   C  N N 79  
CYS SG   S  N N 80  
CYS OXT  O  N N 81  
CYS H    H  N N 82  
CYS H2   H  N N 83  
CYS HA   H  N N 84  
CYS HB2  H  N N 85  
CYS HB3  H  N N 86  
CYS HG   H  N N 87  
CYS HXT  H  N N 88  
GLN N    N  N N 89  
GLN CA   C  N S 90  
GLN C    C  N N 91  
GLN O    O  N N 92  
GLN CB   C  N N 93  
GLN CG   C  N N 94  
GLN CD   C  N N 95  
GLN OE1  O  N N 96  
GLN NE2  N  N N 97  
GLN OXT  O  N N 98  
GLN H    H  N N 99  
GLN H2   H  N N 100 
GLN HA   H  N N 101 
GLN HB2  H  N N 102 
GLN HB3  H  N N 103 
GLN HG2  H  N N 104 
GLN HG3  H  N N 105 
GLN HE21 H  N N 106 
GLN HE22 H  N N 107 
GLN HXT  H  N N 108 
GLU N    N  N N 109 
GLU CA   C  N S 110 
GLU C    C  N N 111 
GLU O    O  N N 112 
GLU CB   C  N N 113 
GLU CG   C  N N 114 
GLU CD   C  N N 115 
GLU OE1  O  N N 116 
GLU OE2  O  N N 117 
GLU OXT  O  N N 118 
GLU H    H  N N 119 
GLU H2   H  N N 120 
GLU HA   H  N N 121 
GLU HB2  H  N N 122 
GLU HB3  H  N N 123 
GLU HG2  H  N N 124 
GLU HG3  H  N N 125 
GLU HE2  H  N N 126 
GLU HXT  H  N N 127 
GLY N    N  N N 128 
GLY CA   C  N N 129 
GLY C    C  N N 130 
GLY O    O  N N 131 
GLY OXT  O  N N 132 
GLY H    H  N N 133 
GLY H2   H  N N 134 
GLY HA2  H  N N 135 
GLY HA3  H  N N 136 
GLY HXT  H  N N 137 
HIS N    N  N N 138 
HIS CA   C  N S 139 
HIS C    C  N N 140 
HIS O    O  N N 141 
HIS CB   C  N N 142 
HIS CG   C  Y N 143 
HIS ND1  N  Y N 144 
HIS CD2  C  Y N 145 
HIS CE1  C  Y N 146 
HIS NE2  N  Y N 147 
HIS OXT  O  N N 148 
HIS H    H  N N 149 
HIS H2   H  N N 150 
HIS HA   H  N N 151 
HIS HB2  H  N N 152 
HIS HB3  H  N N 153 
HIS HD1  H  N N 154 
HIS HD2  H  N N 155 
HIS HE1  H  N N 156 
HIS HE2  H  N N 157 
HIS HXT  H  N N 158 
HOH O    O  N N 159 
HOH H1   H  N N 160 
HOH H2   H  N N 161 
ILE N    N  N N 162 
ILE CA   C  N S 163 
ILE C    C  N N 164 
ILE O    O  N N 165 
ILE CB   C  N S 166 
ILE CG1  C  N N 167 
ILE CG2  C  N N 168 
ILE CD1  C  N N 169 
ILE OXT  O  N N 170 
ILE H    H  N N 171 
ILE H2   H  N N 172 
ILE HA   H  N N 173 
ILE HB   H  N N 174 
ILE HG12 H  N N 175 
ILE HG13 H  N N 176 
ILE HG21 H  N N 177 
ILE HG22 H  N N 178 
ILE HG23 H  N N 179 
ILE HD11 H  N N 180 
ILE HD12 H  N N 181 
ILE HD13 H  N N 182 
ILE HXT  H  N N 183 
LEU N    N  N N 184 
LEU CA   C  N S 185 
LEU C    C  N N 186 
LEU O    O  N N 187 
LEU CB   C  N N 188 
LEU CG   C  N N 189 
LEU CD1  C  N N 190 
LEU CD2  C  N N 191 
LEU OXT  O  N N 192 
LEU H    H  N N 193 
LEU H2   H  N N 194 
LEU HA   H  N N 195 
LEU HB2  H  N N 196 
LEU HB3  H  N N 197 
LEU HG   H  N N 198 
LEU HD11 H  N N 199 
LEU HD12 H  N N 200 
LEU HD13 H  N N 201 
LEU HD21 H  N N 202 
LEU HD22 H  N N 203 
LEU HD23 H  N N 204 
LEU HXT  H  N N 205 
LYS N    N  N N 206 
LYS CA   C  N S 207 
LYS C    C  N N 208 
LYS O    O  N N 209 
LYS CB   C  N N 210 
LYS CG   C  N N 211 
LYS CD   C  N N 212 
LYS CE   C  N N 213 
LYS NZ   N  N N 214 
LYS OXT  O  N N 215 
LYS H    H  N N 216 
LYS H2   H  N N 217 
LYS HA   H  N N 218 
LYS HB2  H  N N 219 
LYS HB3  H  N N 220 
LYS HG2  H  N N 221 
LYS HG3  H  N N 222 
LYS HD2  H  N N 223 
LYS HD3  H  N N 224 
LYS HE2  H  N N 225 
LYS HE3  H  N N 226 
LYS HZ1  H  N N 227 
LYS HZ2  H  N N 228 
LYS HZ3  H  N N 229 
LYS HXT  H  N N 230 
MET N    N  N N 231 
MET CA   C  N S 232 
MET C    C  N N 233 
MET O    O  N N 234 
MET CB   C  N N 235 
MET CG   C  N N 236 
MET SD   S  N N 237 
MET CE   C  N N 238 
MET OXT  O  N N 239 
MET H    H  N N 240 
MET H2   H  N N 241 
MET HA   H  N N 242 
MET HB2  H  N N 243 
MET HB3  H  N N 244 
MET HG2  H  N N 245 
MET HG3  H  N N 246 
MET HE1  H  N N 247 
MET HE2  H  N N 248 
MET HE3  H  N N 249 
MET HXT  H  N N 250 
NA  NA   NA N N 251 
PHE N    N  N N 252 
PHE CA   C  N S 253 
PHE C    C  N N 254 
PHE O    O  N N 255 
PHE CB   C  N N 256 
PHE CG   C  Y N 257 
PHE CD1  C  Y N 258 
PHE CD2  C  Y N 259 
PHE CE1  C  Y N 260 
PHE CE2  C  Y N 261 
PHE CZ   C  Y N 262 
PHE OXT  O  N N 263 
PHE H    H  N N 264 
PHE H2   H  N N 265 
PHE HA   H  N N 266 
PHE HB2  H  N N 267 
PHE HB3  H  N N 268 
PHE HD1  H  N N 269 
PHE HD2  H  N N 270 
PHE HE1  H  N N 271 
PHE HE2  H  N N 272 
PHE HZ   H  N N 273 
PHE HXT  H  N N 274 
PRO N    N  N N 275 
PRO CA   C  N S 276 
PRO C    C  N N 277 
PRO O    O  N N 278 
PRO CB   C  N N 279 
PRO CG   C  N N 280 
PRO CD   C  N N 281 
PRO OXT  O  N N 282 
PRO H    H  N N 283 
PRO HA   H  N N 284 
PRO HB2  H  N N 285 
PRO HB3  H  N N 286 
PRO HG2  H  N N 287 
PRO HG3  H  N N 288 
PRO HD2  H  N N 289 
PRO HD3  H  N N 290 
PRO HXT  H  N N 291 
SER N    N  N N 292 
SER CA   C  N S 293 
SER C    C  N N 294 
SER O    O  N N 295 
SER CB   C  N N 296 
SER OG   O  N N 297 
SER OXT  O  N N 298 
SER H    H  N N 299 
SER H2   H  N N 300 
SER HA   H  N N 301 
SER HB2  H  N N 302 
SER HB3  H  N N 303 
SER HG   H  N N 304 
SER HXT  H  N N 305 
THR N    N  N N 306 
THR CA   C  N S 307 
THR C    C  N N 308 
THR O    O  N N 309 
THR CB   C  N R 310 
THR OG1  O  N N 311 
THR CG2  C  N N 312 
THR OXT  O  N N 313 
THR H    H  N N 314 
THR H2   H  N N 315 
THR HA   H  N N 316 
THR HB   H  N N 317 
THR HG1  H  N N 318 
THR HG21 H  N N 319 
THR HG22 H  N N 320 
THR HG23 H  N N 321 
THR HXT  H  N N 322 
TRP N    N  N N 323 
TRP CA   C  N S 324 
TRP C    C  N N 325 
TRP O    O  N N 326 
TRP CB   C  N N 327 
TRP CG   C  Y N 328 
TRP CD1  C  Y N 329 
TRP CD2  C  Y N 330 
TRP NE1  N  Y N 331 
TRP CE2  C  Y N 332 
TRP CE3  C  Y N 333 
TRP CZ2  C  Y N 334 
TRP CZ3  C  Y N 335 
TRP CH2  C  Y N 336 
TRP OXT  O  N N 337 
TRP H    H  N N 338 
TRP H2   H  N N 339 
TRP HA   H  N N 340 
TRP HB2  H  N N 341 
TRP HB3  H  N N 342 
TRP HD1  H  N N 343 
TRP HE1  H  N N 344 
TRP HE3  H  N N 345 
TRP HZ2  H  N N 346 
TRP HZ3  H  N N 347 
TRP HH2  H  N N 348 
TRP HXT  H  N N 349 
TYR N    N  N N 350 
TYR CA   C  N S 351 
TYR C    C  N N 352 
TYR O    O  N N 353 
TYR CB   C  N N 354 
TYR CG   C  Y N 355 
TYR CD1  C  Y N 356 
TYR CD2  C  Y N 357 
TYR CE1  C  Y N 358 
TYR CE2  C  Y N 359 
TYR CZ   C  Y N 360 
TYR OH   O  N N 361 
TYR OXT  O  N N 362 
TYR H    H  N N 363 
TYR H2   H  N N 364 
TYR HA   H  N N 365 
TYR HB2  H  N N 366 
TYR HB3  H  N N 367 
TYR HD1  H  N N 368 
TYR HD2  H  N N 369 
TYR HE1  H  N N 370 
TYR HE2  H  N N 371 
TYR HH   H  N N 372 
TYR HXT  H  N N 373 
VAL N    N  N N 374 
VAL CA   C  N S 375 
VAL C    C  N N 376 
VAL O    O  N N 377 
VAL CB   C  N N 378 
VAL CG1  C  N N 379 
VAL CG2  C  N N 380 
VAL OXT  O  N N 381 
VAL H    H  N N 382 
VAL H2   H  N N 383 
VAL HA   H  N N 384 
VAL HB   H  N N 385 
VAL HG11 H  N N 386 
VAL HG12 H  N N 387 
VAL HG13 H  N N 388 
VAL HG21 H  N N 389 
VAL HG22 H  N N 390 
VAL HG23 H  N N 391 
VAL HXT  H  N N 392 
ZN  ZN   ZN N N 393 
# 
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 
# 
loop_
_pdbx_audit_support.funding_organization 
_pdbx_audit_support.country 
_pdbx_audit_support.grant_number 
_pdbx_audit_support.ordinal 
'National Institutes of Health/National Institute of General Medical Sciences (NIH/NIGMS)' 'United States' 144379 1 
'National Institutes of Health/National Institute of General Medical Sciences (NIH/NIGMS)' 'United States' 144483 2 
# 
_space_group.name_H-M_alt     'P 61' 
_space_group.name_Hall        'P 61' 
_space_group.IT_number        169 
_space_group.crystal_system   hexagonal 
_space_group.id               1 
# 
_atom_sites.entry_id                    9CI7 
_atom_sites.Cartn_transf_matrix[1][1]   ? 
_atom_sites.Cartn_transf_matrix[1][2]   ? 
_atom_sites.Cartn_transf_matrix[1][3]   ? 
_atom_sites.Cartn_transf_matrix[2][1]   ? 
_atom_sites.Cartn_transf_matrix[2][2]   ? 
_atom_sites.Cartn_transf_matrix[2][3]   ? 
_atom_sites.Cartn_transf_matrix[3][1]   ? 
_atom_sites.Cartn_transf_matrix[3][2]   ? 
_atom_sites.Cartn_transf_matrix[3][3]   ? 
_atom_sites.Cartn_transf_vector[1]      ? 
_atom_sites.Cartn_transf_vector[2]      ? 
_atom_sites.Cartn_transf_vector[3]      ? 
_atom_sites.Cartn_transform_axes        ? 
_atom_sites.fract_transf_matrix[1][1]   0.014158 
_atom_sites.fract_transf_matrix[1][2]   0.008174 
_atom_sites.fract_transf_matrix[1][3]   0.000000 
_atom_sites.fract_transf_matrix[2][1]   0.000000 
_atom_sites.fract_transf_matrix[2][2]   0.016349 
_atom_sites.fract_transf_matrix[2][3]   0.000000 
_atom_sites.fract_transf_matrix[3][1]   0.000000 
_atom_sites.fract_transf_matrix[3][2]   0.000000 
_atom_sites.fract_transf_matrix[3][3]   0.010292 
_atom_sites.fract_transf_vector[1]      0.00000 
_atom_sites.fract_transf_vector[2]      0.00000 
_atom_sites.fract_transf_vector[3]      0.00000 
_atom_sites.solution_primary            ? 
_atom_sites.solution_secondary          ? 
_atom_sites.solution_hydrogens          ? 
_atom_sites.special_details             ? 
# 
loop_
_atom_type.symbol 
_atom_type.scat_dispersion_real 
_atom_type.scat_dispersion_imag 
_atom_type.scat_Cromer_Mann_a1 
_atom_type.scat_Cromer_Mann_a2 
_atom_type.scat_Cromer_Mann_a3 
_atom_type.scat_Cromer_Mann_a4 
_atom_type.scat_Cromer_Mann_b1 
_atom_type.scat_Cromer_Mann_b2 
_atom_type.scat_Cromer_Mann_b3 
_atom_type.scat_Cromer_Mann_b4 
_atom_type.scat_Cromer_Mann_c 
_atom_type.scat_source 
_atom_type.scat_dispersion_source 
C  ? ? 3.54356  2.42580 ? ? 25.62398 1.50364  ? ? 0.0 
;2-Gaussian fit: Grosse-Kunstleve RW, Sauter NK, Adams PD: Newsletter of the IUCr Commission on Crystallographic Computing 2004, 3, 22-31.
;
? 
CL ? ? 9.50761  7.44341 ? ? 1.04373  23.83732 ? ? 0.0 
;2-Gaussian fit: Grosse-Kunstleve RW, Sauter NK, Adams PD: Newsletter of the IUCr Commission on Crystallographic Computing 2004, 3, 22-31.
;
? 
N  ? ? 4.01032  2.96436 ? ? 19.97189 1.75589  ? ? 0.0 
;2-Gaussian fit: Grosse-Kunstleve RW, Sauter NK, Adams PD: Newsletter of the IUCr Commission on Crystallographic Computing 2004, 3, 22-31.
;
? 
NA ? ? ?        ?       ? ? ?        ?        ? ? ?   ? ? 
O  ? ? 4.49882  3.47563 ? ? 15.80542 1.70748  ? ? 0.0 
;2-Gaussian fit: Grosse-Kunstleve RW, Sauter NK, Adams PD: Newsletter of the IUCr Commission on Crystallographic Computing 2004, 3, 22-31.
;
? 
S  ? ? 9.55732  6.39887 ? ? 1.23737  29.19336 ? ? 0.0 
;2-Gaussian fit: Grosse-Kunstleve RW, Sauter NK, Adams PD: Newsletter of the IUCr Commission on Crystallographic Computing 2004, 3, 22-31.
;
? 
ZN ? ? 24.64596 5.25405 ? ? 2.14387  29.76375 ? ? 0.0 
;2-Gaussian fit: Grosse-Kunstleve RW, Sauter NK, Adams PD: Newsletter of the IUCr Commission on Crystallographic Computing 2004, 3, 22-31.
;
? 
# 
loop_
_atom_site.group_PDB 
_atom_site.id 
_atom_site.type_symbol 
_atom_site.label_atom_id 
_atom_site.label_alt_id 
_atom_site.label_comp_id 
_atom_site.label_asym_id 
_atom_site.label_entity_id 
_atom_site.label_seq_id 
_atom_site.pdbx_PDB_ins_code 
_atom_site.Cartn_x 
_atom_site.Cartn_y 
_atom_site.Cartn_z 
_atom_site.occupancy 
_atom_site.B_iso_or_equiv 
_atom_site.pdbx_formal_charge 
_atom_site.auth_seq_id 
_atom_site.auth_comp_id 
_atom_site.auth_asym_id 
_atom_site.auth_atom_id 
_atom_site.pdbx_PDB_model_num 
ATOM   1    N  N   . GLY A 1 1   ? -2.94532 61.97353 -3.29187  1.000 63.59575  ? 2   GLY A N   1 
ATOM   2    C  CA  . GLY A 1 1   ? -3.13181 60.78805 -4.10606  1.000 47.50865  ? 2   GLY A CA  1 
ATOM   3    C  C   . GLY A 1 1   ? -2.36103 59.59679 -3.57708  1.000 73.90971  ? 2   GLY A C   1 
ATOM   4    O  O   . GLY A 1 1   ? -2.52423 58.47409 -4.05615  1.000 87.14928  ? 2   GLY A O   1 
ATOM   5    N  N   . HIS A 1 2   ? -1.51528 59.84457 -2.58010  1.000 60.14157  ? 3   HIS A N   1 
ATOM   6    C  CA  . HIS A 1 2   ? -0.71467 58.79092 -1.97709  1.000 64.81849  ? 3   HIS A CA  1 
ATOM   7    C  C   . HIS A 1 2   ? -0.49292 59.11662 -0.50737  1.000 56.69651  ? 3   HIS A C   1 
ATOM   8    O  O   . HIS A 1 2   ? -0.87694 60.18200 -0.01840  1.000 59.24728  ? 3   HIS A O   1 
ATOM   9    C  CB  . HIS A 1 2   ? 0.62084  58.61019 -2.71380  1.000 63.93854  ? 3   HIS A CB  1 
ATOM   10   C  CG  . HIS A 1 2   ? 1.47977  59.83911 -2.74128  1.000 45.50313  ? 3   HIS A CG  1 
ATOM   11   N  ND1 . HIS A 1 2   ? 2.58379  59.95149 -3.55857  1.000 40.48174  ? 3   HIS A ND1 1 
ATOM   12   C  CD2 . HIS A 1 2   ? 1.40461  61.00255 -2.05145  1.000 43.15150  ? 3   HIS A CD2 1 
ATOM   13   C  CE1 . HIS A 1 2   ? 3.14917  61.13109 -3.37370  1.000 42.85207  ? 3   HIS A CE1 1 
ATOM   14   N  NE2 . HIS A 1 2   ? 2.45419  61.78771 -2.46276  1.000 34.44167  ? 3   HIS A NE2 1 
ATOM   15   N  N   . MET A 1 3   ? 0.13644  58.18070 0.19469   1.000 56.85570  ? 4   MET A N   1 
ATOM   16   C  CA  . MET A 1 3   ? 0.49777  58.38775 1.58989   1.000 64.40297  ? 4   MET A CA  1 
ATOM   17   C  C   . MET A 1 3   ? 1.73748  57.56512 1.92241   1.000 49.94157  ? 4   MET A C   1 
ATOM   18   O  O   . MET A 1 3   ? 1.66882  56.33098 1.99293   1.000 43.50618  ? 4   MET A O   1 
ATOM   19   C  CB  . MET A 1 3   ? -0.67132 58.03156 2.51357   1.000 60.26970  ? 4   MET A CB  1 
ATOM   20   C  CG  . MET A 1 3   ? -1.34544 56.70072 2.20918   1.000 85.05372  ? 4   MET A CG  1 
ATOM   21   S  SD  . MET A 1 3   ? -2.79498 56.39599 3.23698   1.000 154.22683 ? 4   MET A SD  1 
ATOM   22   C  CE  . MET A 1 3   ? -3.96132 57.55610 2.52907   1.000 102.79289 ? 4   MET A CE  1 
ATOM   23   N  N   . PRO A 1 4   ? 2.89020  58.20711 2.10635   1.000 46.76641  ? 5   PRO A N   1 
ATOM   24   C  CA  . PRO A 1 4   ? 4.10486  57.45379 2.43847   1.000 41.78634  ? 5   PRO A CA  1 
ATOM   25   C  C   . PRO A 1 4   ? 3.94740  56.71003 3.75583   1.000 46.79116  ? 5   PRO A C   1 
ATOM   26   O  O   . PRO A 1 4   ? 3.41016  57.23964 4.73098   1.000 44.12697  ? 5   PRO A O   1 
ATOM   27   C  CB  . PRO A 1 4   ? 5.18324  58.53972 2.52735   1.000 37.70232  ? 5   PRO A CB  1 
ATOM   28   C  CG  . PRO A 1 4   ? 4.64687  59.67493 1.71076   1.000 41.28284  ? 5   PRO A CG  1 
ATOM   29   C  CD  . PRO A 1 4   ? 3.16200  59.64159 1.91456   1.000 42.53766  ? 5   PRO A CD  1 
ATOM   30   N  N   . ILE A 1 5   ? 4.41552  55.46242 3.77017   1.000 44.20756  ? 6   ILE A N   1 
ATOM   31   C  CA  . ILE A 1 5   ? 4.30499  54.63172 4.96205   1.000 34.64332  ? 6   ILE A CA  1 
ATOM   32   C  C   . ILE A 1 5   ? 5.18926  55.20222 6.06114   1.000 36.55965  ? 6   ILE A C   1 
ATOM   33   O  O   . ILE A 1 5   ? 6.38606  55.44311 5.85640   1.000 36.61478  ? 6   ILE A O   1 
ATOM   34   C  CB  . ILE A 1 5   ? 4.68565  53.17839 4.64446   1.000 37.39170  ? 6   ILE A CB  1 
ATOM   35   C  CG1 . ILE A 1 5   ? 3.82928  52.63700 3.49805   1.000 37.86151  ? 6   ILE A CG1 1 
ATOM   36   C  CG2 . ILE A 1 5   ? 4.53496  52.30819 5.88454   1.000 40.80148  ? 6   ILE A CG2 1 
ATOM   37   C  CD1 . ILE A 1 5   ? 2.34877  52.59549 3.80733   1.000 44.07283  ? 6   ILE A CD1 1 
ATOM   38   N  N   . ASP A 1 6   ? 4.59937  55.42619 7.23655   1.000 36.67793  ? 7   ASP A N   1 
ATOM   39   C  CA  . ASP A 1 6   ? 5.33438  55.89338 8.40226   1.000 47.19539  ? 7   ASP A CA  1 
ATOM   40   C  C   . ASP A 1 6   ? 5.69742  54.68497 9.25464   1.000 43.14989  ? 7   ASP A C   1 
ATOM   41   O  O   . ASP A 1 6   ? 4.83256  54.15575 9.96955   1.000 46.68838  ? 7   ASP A O   1 
ATOM   42   C  CB  . ASP A 1 6   ? 4.49620  56.89257 9.20624   1.000 49.63248  ? 7   ASP A CB  1 
ATOM   43   C  CG  . ASP A 1 6   ? 5.32084  57.67909 10.21326  1.000 52.72300  ? 7   ASP A CG  1 
ATOM   44   O  OD1 . ASP A 1 6   ? 6.36084  57.16619 10.67765  1.000 52.18440  ? 7   ASP A OD1 1 
ATOM   45   O  OD2 . ASP A 1 6   ? 4.92374  58.81697 10.54335  1.000 58.76991  ? 7   ASP A OD2 1 
ATOM   46   N  N   . PRO A 1 7   ? 6.94508  54.20687 9.21816   1.000 39.19596  ? 8   PRO A N   1 
ATOM   47   C  CA  . PRO A 1 7   ? 7.28637  53.01240 10.00668  1.000 41.07303  ? 8   PRO A CA  1 
ATOM   48   C  C   . PRO A 1 7   ? 7.18617  53.23362 11.50417  1.000 32.94338  ? 8   PRO A C   1 
ATOM   49   O  O   . PRO A 1 7   ? 6.94013  52.27287 12.24377  1.000 40.59782  ? 8   PRO A O   1 
ATOM   50   C  CB  . PRO A 1 7   ? 8.72663  52.70570 9.57282   1.000 36.20653  ? 8   PRO A CB  1 
ATOM   51   C  CG  . PRO A 1 7   ? 9.26501  54.02001 9.11095   1.000 40.05494  ? 8   PRO A CG  1 
ATOM   52   C  CD  . PRO A 1 7   ? 8.10536  54.73975 8.48373   1.000 36.99892  ? 8   PRO A CD  1 
ATOM   53   N  N   . LYS A 1 8   ? 7.36845  54.46965 11.97413  1.000 33.81466  ? 9   LYS A N   1 
ATOM   54   C  CA  . LYS A 1 8   ? 7.20530  54.75101 13.39629  1.000 37.58624  ? 9   LYS A CA  1 
ATOM   55   C  C   . LYS A 1 8   ? 5.75391  54.58001 13.82769  1.000 44.41548  ? 9   LYS A C   1 
ATOM   56   O  O   . LYS A 1 8   ? 5.47947  54.02452 14.89813  1.000 35.68279  ? 9   LYS A O   1 
ATOM   57   C  CB  . LYS A 1 8   ? 7.70097  56.16284 13.70781  1.000 42.21956  ? 9   LYS A CB  1 
ATOM   58   C  CG  . LYS A 1 8   ? 7.58588  56.56223 15.16867  1.000 42.30817  ? 9   LYS A CG  1 
ATOM   59   C  CD  . LYS A 1 8   ? 8.11546  57.97053 15.39010  1.000 51.95296  ? 9   LYS A CD  1 
ATOM   60   C  CE  . LYS A 1 8   ? 7.92364  58.41966 16.82970  1.000 55.10323  ? 9   LYS A CE  1 
ATOM   61   N  NZ  . LYS A 1 8   ? 8.42643  59.80560 17.04414  1.000 58.38213  ? 9   LYS A NZ  1 
ATOM   62   N  N   . GLU A 1 9   ? 4.80998  55.04478 13.00466  1.000 41.45917  ? 10  GLU A N   1 
ATOM   63   C  CA  . GLU A 1 9   ? 3.39869  54.87876 13.33470  1.000 45.86190  ? 10  GLU A CA  1 
ATOM   64   C  C   . GLU A 1 9   ? 2.95187  53.43141 13.17947  1.000 40.75019  ? 10  GLU A C   1 
ATOM   65   O  O   . GLU A 1 9   ? 1.99467  53.00682 13.83669  1.000 41.20323  ? 10  GLU A O   1 
ATOM   66   C  CB  . GLU A 1 9   ? 2.54256  55.79976 12.46602  1.000 41.30927  ? 10  GLU A CB  1 
ATOM   67   C  CG  . GLU A 1 9   ? 2.75258  57.27755 12.75051  1.000 72.31077  ? 10  GLU A CG  1 
ATOM   68   C  CD  . GLU A 1 9   ? 2.40449  57.64937 14.17980  1.000 82.04406  ? 10  GLU A CD  1 
ATOM   69   O  OE1 . GLU A 1 9   ? 1.37760  57.15420 14.69184  1.000 70.52624  ? 10  GLU A OE1 1 
ATOM   70   O  OE2 . GLU A 1 9   ? 3.16269  58.43014 14.79385  1.000 62.20386  ? 10  GLU A OE2 1 
ATOM   71   N  N   . LEU A 1 10  ? 3.62277  52.66342 12.31779  1.000 39.78082  ? 11  LEU A N   1 
ATOM   72   C  CA  . LEU A 1 10  ? 3.31609  51.24125 12.20726  1.000 40.74053  ? 11  LEU A CA  1 
ATOM   73   C  C   . LEU A 1 10  ? 3.68268  50.50213 13.48807  1.000 36.59023  ? 11  LEU A C   1 
ATOM   74   O  O   . LEU A 1 10  ? 2.90211  49.68169 13.98449  1.000 37.55653  ? 11  LEU A O   1 
ATOM   75   C  CB  . LEU A 1 10  ? 4.04953  50.63906 11.00934  1.000 44.73240  ? 11  LEU A CB  1 
ATOM   76   C  CG  . LEU A 1 10  ? 3.20024  49.82898 10.03018  1.000 62.34486  ? 11  LEU A CG  1 
ATOM   77   C  CD1 . LEU A 1 10  ? 2.09934  50.69771 9.44089   1.000 61.04376  ? 11  LEU A CD1 1 
ATOM   78   C  CD2 . LEU A 1 10  ? 4.06956  49.23720 8.93137   1.000 44.29956  ? 11  LEU A CD2 1 
ATOM   79   N  N   . LEU A 1 11  ? 4.86713  50.78252 14.03775  1.000 35.43227  ? 12  LEU A N   1 
ATOM   80   C  CA  . LEU A 1 11  ? 5.26395  50.17180 15.30164  1.000 46.35867  ? 12  LEU A CA  1 
ATOM   81   C  C   . LEU A 1 11  ? 4.43218  50.70183 16.46186  1.000 45.93960  ? 12  LEU A C   1 
ATOM   82   O  O   . LEU A 1 11  ? 4.13594  49.95704 17.40372  1.000 45.07056  ? 12  LEU A O   1 
ATOM   83   C  CB  . LEU A 1 11  ? 6.75103  50.41689 15.55730  1.000 46.70350  ? 12  LEU A CB  1 
ATOM   84   C  CG  . LEU A 1 11  ? 7.72423  49.84291 14.52482  1.000 37.66997  ? 12  LEU A CG  1 
ATOM   85   C  CD1 . LEU A 1 11  ? 9.12239  50.39877 14.73959  1.000 38.96732  ? 12  LEU A CD1 1 
ATOM   86   C  CD2 . LEU A 1 11  ? 7.73554  48.32245 14.58652  1.000 34.36220  ? 12  LEU A CD2 1 
ATOM   87   N  N   . LYS A 1 12  ? 4.05178  51.98075 16.41230  1.000 48.37780  ? 13  LYS A N   1 
ATOM   88   C  CA  . LYS A 1 12  ? 3.21277  52.55066 17.46103  1.000 40.36369  ? 13  LYS A CA  1 
ATOM   89   C  C   . LYS A 1 12  ? 1.85798  51.85740 17.51769  1.000 46.49999  ? 13  LYS A C   1 
ATOM   90   O  O   . LYS A 1 12  ? 1.32199  51.61318 18.60469  1.000 39.94969  ? 13  LYS A O   1 
ATOM   91   C  CB  . LYS A 1 12  ? 3.04388  54.05297 17.23074  1.000 52.55781  ? 13  LYS A CB  1 
ATOM   92   C  CG  . LYS A 1 12  ? 2.09041  54.74040 18.19379  1.000 63.57416  ? 13  LYS A CG  1 
ATOM   93   C  CD  . LYS A 1 12  ? 1.93410  56.21170 17.84140  1.000 76.47116  ? 13  LYS A CD  1 
ATOM   94   C  CE  . LYS A 1 12  ? 0.89182  56.88951 18.71478  1.000 82.84062  ? 13  LYS A CE  1 
ATOM   95   N  NZ  . LYS A 1 12  ? 0.70080  58.31675 18.33357  1.000 82.21216  ? 13  LYS A NZ  1 
ATOM   96   N  N   . GLY A 1 13  ? 1.29181  51.52443 16.35540  1.000 40.48783  ? 14  GLY A N   1 
ATOM   97   C  CA  . GLY A 1 13  ? 0.03187  50.80353 16.32038  1.000 48.13757  ? 14  GLY A CA  1 
ATOM   98   C  C   . GLY A 1 13  ? 0.11516  49.39234 16.86180  1.000 48.93966  ? 14  GLY A C   1 
ATOM   99   O  O   . GLY A 1 13  ? -0.92104 48.79826 17.17711  1.000 50.77807  ? 14  GLY A O   1 
ATOM   100  N  N   . LEU A 1 14  ? 1.32378  48.84195 16.97374  1.000 47.50412  ? 15  LEU A N   1 
ATOM   101  C  CA  . LEU A 1 14  ? 1.54590  47.51360 17.53033  1.000 43.09973  ? 15  LEU A CA  1 
ATOM   102  C  C   . LEU A 1 14  ? 2.18109  47.58666 18.91566  1.000 41.32199  ? 15  LEU A C   1 
ATOM   103  O  O   . LEU A 1 14  ? 2.89543  46.67034 19.32875  1.000 47.09387  ? 15  LEU A O   1 
ATOM   104  C  CB  . LEU A 1 14  ? 2.41409  46.68064 16.58889  1.000 43.50776  ? 15  LEU A CB  1 
ATOM   105  C  CG  . LEU A 1 14  ? 1.91717  46.56098 15.14756  1.000 43.09880  ? 15  LEU A CG  1 
ATOM   106  C  CD1 . LEU A 1 14  ? 2.91626  45.79385 14.29707  1.000 55.19020  ? 15  LEU A CD1 1 
ATOM   107  C  CD2 . LEU A 1 14  ? 0.55280  45.89443 15.10896  1.000 61.00060  ? 15  LEU A CD2 1 
ATOM   108  N  N   . ASP A 1 15  ? 1.92178  48.67719 19.64116  1.000 43.97585  ? 16  ASP A N   1 
ATOM   109  C  CA  . ASP A 1 15  ? 2.57945  48.89798 20.92509  1.000 43.37018  ? 16  ASP A CA  1 
ATOM   110  C  C   . ASP A 1 15  ? 2.18693  47.83572 21.94510  1.000 41.50051  ? 16  ASP A C   1 
ATOM   111  O  O   . ASP A 1 15  ? 3.02098  47.39286 22.74397  1.000 44.66587  ? 16  ASP A O   1 
ATOM   112  C  CB  . ASP A 1 15  ? 2.23542  50.29314 21.44723  1.000 49.48676  ? 16  ASP A CB  1 
ATOM   113  C  CG  . ASP A 1 15  ? 3.45280  51.05241 21.93254  1.000 72.71509  ? 16  ASP A CG  1 
ATOM   114  O  OD1 . ASP A 1 15  ? 4.58252  50.57227 21.70541  1.000 78.13153  ? 16  ASP A OD1 1 
ATOM   115  O  OD2 . ASP A 1 15  ? 3.27927  52.13025 22.54077  1.000 65.75155  ? 16  ASP A OD2 1 
ATOM   116  N  N   . SER A 1 16  ? 0.92198  47.41244 21.93337  1.000 35.21007  ? 17  SER A N   1 
ATOM   117  C  CA  . SER A 1 16  ? 0.43717  46.45944 22.92398  1.000 44.01001  ? 17  SER A CA  1 
ATOM   118  C  C   . SER A 1 16  ? 0.83024  45.02186 22.61075  1.000 43.11242  ? 17  SER A C   1 
ATOM   119  O  O   . SER A 1 16  ? 0.81381  44.18053 23.51555  1.000 43.95184  ? 17  SER A O   1 
ATOM   120  C  CB  . SER A 1 16  ? -1.08500 46.55824 23.04467  1.000 39.69127  ? 17  SER A CB  1 
ATOM   121  O  OG  . SER A 1 16  ? -1.71205 46.25258 21.81135  1.000 51.32741  ? 17  SER A OG  1 
ATOM   122  N  N   . PHE A 1 17  ? 1.18035  44.71975 21.36194  1.000 47.71016  ? 18  PHE A N   1 
ATOM   123  C  CA  . PHE A 1 17  ? 1.53340  43.36180 20.97113  1.000 39.14381  ? 18  PHE A CA  1 
ATOM   124  C  C   . PHE A 1 17  ? 3.02433  43.07272 21.07777  1.000 40.36625  ? 18  PHE A C   1 
ATOM   125  O  O   . PHE A 1 17  ? 3.41445  41.90089 21.03749  1.000 41.18447  ? 18  PHE A O   1 
ATOM   126  C  CB  . PHE A 1 17  ? 1.07473  43.08457 19.53473  1.000 41.54781  ? 18  PHE A CB  1 
ATOM   127  C  CG  . PHE A 1 17  ? -0.39542 43.29446 19.31362  1.000 55.30972  ? 18  PHE A CG  1 
ATOM   128  C  CD1 . PHE A 1 17  ? -1.31825 42.37197 19.77803  1.000 49.12111  ? 18  PHE A CD1 1 
ATOM   129  C  CD2 . PHE A 1 17  ? -0.85397 44.40836 18.62985  1.000 55.86327  ? 18  PHE A CD2 1 
ATOM   130  C  CE1 . PHE A 1 17  ? -2.67209 42.56075 19.57237  1.000 57.49079  ? 18  PHE A CE1 1 
ATOM   131  C  CE2 . PHE A 1 17  ? -2.20655 44.60248 18.42040  1.000 71.75750  ? 18  PHE A CE2 1 
ATOM   132  C  CZ  . PHE A 1 17  ? -3.11654 43.67731 18.89241  1.000 55.61203  ? 18  PHE A CZ  1 
ATOM   133  N  N   . LEU A 1 18  ? 3.86042  44.09636 21.21255  1.000 39.28230  ? 19  LEU A N   1 
ATOM   134  C  CA  . LEU A 1 18  ? 5.30501  43.93293 21.20946  1.000 38.48244  ? 19  LEU A CA  1 
ATOM   135  C  C   . LEU A 1 18  ? 5.88982  44.29218 22.56890  1.000 43.08553  ? 19  LEU A C   1 
ATOM   136  O  O   . LEU A 1 18  ? 5.30563  45.05593 23.34223  1.000 41.87932  ? 19  LEU A O   1 
ATOM   137  C  CB  . LEU A 1 18  ? 5.95048  44.79942 20.12132  1.000 32.82245  ? 19  LEU A CB  1 
ATOM   138  C  CG  . LEU A 1 18  ? 5.40536  44.62635 18.70259  1.000 30.90390  ? 19  LEU A CG  1 
ATOM   139  C  CD1 . LEU A 1 18  ? 6.14094  45.53606 17.73040  1.000 37.76803  ? 19  LEU A CD1 1 
ATOM   140  C  CD2 . LEU A 1 18  ? 5.50020  43.17434 18.26268  1.000 38.39414  ? 19  LEU A CD2 1 
ATOM   141  N  N   . THR A 1 19  ? 7.06216  43.72786 22.84897  1.000 39.35516  ? 20  THR A N   1 
ATOM   142  C  CA  . THR A 1 19  ? 7.80811  44.05613 24.05601  1.000 43.93499  ? 20  THR A CA  1 
ATOM   143  C  C   . THR A 1 19  ? 8.53318  45.38499 23.85043  1.000 49.02864  ? 20  THR A C   1 
ATOM   144  O  O   . THR A 1 19  ? 8.34296  46.07748 22.84679  1.000 49.44026  ? 20  THR A O   1 
ATOM   145  C  CB  . THR A 1 19  ? 8.78634  42.93703 24.40416  1.000 42.16180  ? 20  THR A CB  1 
ATOM   146  O  OG1 . THR A 1 19  ? 9.84202  42.90778 23.43559  1.000 48.57436  ? 20  THR A OG1 1 
ATOM   147  C  CG2 . THR A 1 19  ? 8.08225  41.59119 24.41048  1.000 56.11600  ? 20  THR A CG2 1 
ATOM   148  N  N   . ARG A 1 20  ? 9.38716  45.75488 24.80733  1.000 44.18670  ? 21  ARG A N   1 
ATOM   149  C  CA  . ARG A 1 20  ? 10.19974 46.95469 24.64935  1.000 54.19080  ? 21  ARG A CA  1 
ATOM   150  C  C   . ARG A 1 20  ? 11.25884 46.79172 23.56816  1.000 43.39590  ? 21  ARG A C   1 
ATOM   151  O  O   . ARG A 1 20  ? 11.73836 47.79609 23.03147  1.000 50.87256  ? 21  ARG A O   1 
ATOM   152  C  CB  . ARG A 1 20  ? 10.86527 47.32396 25.97640  1.000 39.77798  ? 21  ARG A CB  1 
ATOM   153  C  CG  . ARG A 1 20  ? 11.72909 46.22100 26.56669  1.000 58.85396  ? 21  ARG A CG  1 
ATOM   154  C  CD  . ARG A 1 20  ? 12.43992 46.69011 27.82635  1.000 72.44800  ? 21  ARG A CD  1 
ATOM   155  N  NE  . ARG A 1 20  ? 13.16829 45.60864 28.47884  1.000 91.33551  ? 21  ARG A NE  1 
ATOM   156  C  CZ  . ARG A 1 20  ? 14.41737 45.26552 28.19421  1.000 99.34322  ? 21  ARG A CZ  1 
ATOM   157  N  NH1 . ARG A 1 20  ? 15.11386 45.89879 27.26443  1.000 71.88414  ? 21  ARG A NH1 1 
ATOM   158  N  NH2 . ARG A 1 20  ? 14.98175 44.26067 28.85864  1.000 93.25638  ? 21  ARG A NH2 1 
ATOM   159  N  N   . ASP A 1 21  ? 11.62829 45.55609 23.23510  1.000 42.29071  ? 22  ASP A N   1 
ATOM   160  C  CA  . ASP A 1 21  ? 12.62592 45.28001 22.21180  1.000 50.45641  ? 22  ASP A CA  1 
ATOM   161  C  C   . ASP A 1 21  ? 12.00544 44.87916 20.87858  1.000 43.64920  ? 22  ASP A C   1 
ATOM   162  O  O   . ASP A 1 21  ? 12.73311 44.48275 19.96279  1.000 43.18574  ? 22  ASP A O   1 
ATOM   163  C  CB  . ASP A 1 21  ? 13.58484 44.19069 22.69477  1.000 48.08261  ? 22  ASP A CB  1 
ATOM   164  C  CG  . ASP A 1 21  ? 14.32822 44.58797 23.95490  1.000 68.80893  ? 22  ASP A CG  1 
ATOM   165  O  OD1 . ASP A 1 21  ? 14.65761 45.78434 24.10096  1.000 66.15180  ? 22  ASP A OD1 1 
ATOM   166  O  OD2 . ASP A 1 21  ? 14.57950 43.70529 24.80165  1.000 92.46134  ? 22  ASP A OD2 1 
ATOM   167  N  N   . GLY A 1 22  ? 10.68303 44.96738 20.75038  1.000 39.71461  ? 23  GLY A N   1 
ATOM   168  C  CA  . GLY A 1 22  ? 10.03320 44.70251 19.48233  1.000 42.48349  ? 23  GLY A CA  1 
ATOM   169  C  C   . GLY A 1 22  ? 9.71663  43.25368 19.19758  1.000 43.55073  ? 23  GLY A C   1 
ATOM   170  O  O   . GLY A 1 22  ? 9.54523  42.88944 18.03002  1.000 40.02687  ? 23  GLY A O   1 
ATOM   171  N  N   . GLU A 1 23  ? 9.62544  42.41358 20.22360  1.000 43.18024  ? 24  GLU A N   1 
ATOM   172  C  CA  . GLU A 1 23  ? 9.33100  40.99791 20.05202  1.000 43.05252  ? 24  GLU A CA  1 
ATOM   173  C  C   . GLU A 1 23  ? 7.84131  40.74579 20.24146  1.000 36.50615  ? 24  GLU A C   1 
ATOM   174  O  O   . GLU A 1 23  ? 7.20550  41.34750 21.11172  1.000 43.72287  ? 24  GLU A O   1 
ATOM   175  C  CB  . GLU A 1 23  ? 10.12858 40.14876 21.04464  1.000 40.82147  ? 24  GLU A CB  1 
ATOM   176  C  CG  . GLU A 1 23  ? 11.60602 40.49423 21.11629  1.000 53.31820  ? 24  GLU A CG  1 
ATOM   177  C  CD  . GLU A 1 23  ? 12.38394 39.53402 21.99423  1.000 75.81913  ? 24  GLU A CD  1 
ATOM   178  O  OE1 . GLU A 1 23  ? 11.93911 38.37686 22.14712  1.000 79.94917  ? 24  GLU A OE1 1 
ATOM   179  O  OE2 . GLU A 1 23  ? 13.43627 39.93638 22.53432  1.000 76.91463  ? 24  GLU A OE2 1 
ATOM   180  N  N   . VAL A 1 24  ? 7.28821  39.85179 19.42098  1.000 36.36438  ? 25  VAL A N   1 
ATOM   181  C  CA  . VAL A 1 24  ? 5.88470  39.48111 19.55693  1.000 38.26439  ? 25  VAL A CA  1 
ATOM   182  C  C   . VAL A 1 24  ? 5.69594  38.70796 20.85453  1.000 43.26331  ? 25  VAL A C   1 
ATOM   183  O  O   . VAL A 1 24  ? 6.40426  37.72871 21.12275  1.000 41.48650  ? 25  VAL A O   1 
ATOM   184  C  CB  . VAL A 1 24  ? 5.42002  38.66242 18.34424  1.000 33.78415  ? 25  VAL A CB  1 
ATOM   185  C  CG1 . VAL A 1 24  ? 3.94397  38.31796 18.47294  1.000 41.77343  ? 25  VAL A CG1 1 
ATOM   186  C  CG2 . VAL A 1 24  ? 5.68334  39.42819 17.05831  1.000 31.23562  ? 25  VAL A CG2 1 
ATOM   187  N  N   . LYS A 1 25  ? 4.72938  39.14237 21.66470  1.000 39.30075  ? 26  LYS A N   1 
ATOM   188  C  CA  . LYS A 1 25  ? 4.57522  38.60260 23.01161  1.000 36.09354  ? 26  LYS A CA  1 
ATOM   189  C  C   . LYS A 1 25  ? 3.88975  37.23993 23.00847  1.000 47.53902  ? 26  LYS A C   1 
ATOM   190  O  O   . LYS A 1 25  ? 4.40755  36.27846 23.58702  1.000 48.71715  ? 26  LYS A O   1 
ATOM   191  C  CB  . LYS A 1 25  ? 3.79884  39.59482 23.87932  1.000 37.78192  ? 26  LYS A CB  1 
ATOM   192  C  CG  . LYS A 1 25  ? 4.58168  40.85449 24.21118  1.000 44.32786  ? 26  LYS A CG  1 
ATOM   193  C  CD  . LYS A 1 25  ? 3.66631  42.03975 24.47572  1.000 57.78003  ? 26  LYS A CD  1 
ATOM   194  C  CE  . LYS A 1 25  ? 2.74567  41.79087 25.65589  1.000 50.53964  ? 26  LYS A CE  1 
ATOM   195  N  NZ  . LYS A 1 25  ? 1.83850  42.94963 25.88754  1.000 58.79885  ? 26  LYS A NZ  1 
ATOM   196  N  N   . SER A 1 26  ? 2.72684  37.13542 22.36924  1.000 40.00619  ? 27  SER A N   1 
ATOM   197  C  CA  . SER A 1 26  ? 1.90864  35.93385 22.44316  1.000 54.06497  ? 27  SER A CA  1 
ATOM   198  C  C   . SER A 1 26  ? 1.56543  35.44172 21.04406  1.000 51.38915  ? 27  SER A C   1 
ATOM   199  O  O   . SER A 1 26  ? 1.82236  36.11020 20.03897  1.000 46.81771  ? 27  SER A O   1 
ATOM   200  C  CB  . SER A 1 26  ? 0.61951  36.18560 23.23808  1.000 51.41113  ? 27  SER A CB  1 
ATOM   201  O  OG  . SER A 1 26  ? -0.21059 37.12278 22.57239  1.000 49.62464  ? 27  SER A OG  1 
ATOM   202  N  N   . VAL A 1 27  ? 0.96808  34.24780 20.99506  1.000 45.28924  ? 28  VAL A N   1 
ATOM   203  C  CA  . VAL A 1 27  ? 0.51008  33.68856 19.73041  1.000 42.73510  ? 28  VAL A CA  1 
ATOM   204  C  C   . VAL A 1 27  ? -0.71885 34.41915 19.20888  1.000 46.90037  ? 28  VAL A C   1 
ATOM   205  O  O   . VAL A 1 27  ? -1.00755 34.36069 18.00838  1.000 50.96996  ? 28  VAL A O   1 
ATOM   206  C  CB  . VAL A 1 27  ? 0.22469  32.18300 19.88146  1.000 47.61653  ? 28  VAL A CB  1 
ATOM   207  C  CG1 . VAL A 1 27  ? 1.50242  31.43383 20.22506  1.000 46.46349  ? 28  VAL A CG1 1 
ATOM   208  C  CG2 . VAL A 1 27  ? -0.83350 31.94994 20.94693  1.000 55.11001  ? 28  VAL A CG2 1 
ATOM   209  N  N   . ASP A 1 28  ? -1.45905 35.10571 20.08246  1.000 49.24441  ? 29  ASP A N   1 
ATOM   210  C  CA  . ASP A 1 28  ? -2.57775 35.91806 19.61793  1.000 52.14506  ? 29  ASP A CA  1 
ATOM   211  C  C   . ASP A 1 28  ? -2.09722 37.17501 18.90630  1.000 55.74776  ? 29  ASP A C   1 
ATOM   212  O  O   . ASP A 1 28  ? -2.76478 37.65734 17.98453  1.000 55.16101  ? 29  ASP A O   1 
ATOM   213  C  CB  . ASP A 1 28  ? -3.48671 36.28606 20.79089  1.000 70.67256  ? 29  ASP A CB  1 
ATOM   214  C  CG  . ASP A 1 28  ? -4.64618 35.32287 20.95465  1.000 89.11477  ? 29  ASP A CG  1 
ATOM   215  O  OD1 . ASP A 1 28  ? -5.30835 35.01129 19.94199  1.000 76.85315  ? 29  ASP A OD1 1 
ATOM   216  O  OD2 . ASP A 1 28  ? -4.89382 34.87516 22.09406  1.000 89.21667  ? 29  ASP A OD2 1 
ATOM   217  N  N   . GLY A 1 29  ? -0.94777 37.71534 19.31370  1.000 46.60993  ? 30  GLY A N   1 
ATOM   218  C  CA  . GLY A 1 29  ? -0.42792 38.90113 18.65453  1.000 45.06072  ? 30  GLY A CA  1 
ATOM   219  C  C   . GLY A 1 29  ? 0.13318  38.60740 17.27659  1.000 39.76556  ? 30  GLY A C   1 
ATOM   220  O  O   . GLY A 1 29  ? -0.01467 39.41261 16.35310  1.000 46.53800  ? 30  GLY A O   1 
ATOM   221  N  N   . ILE A 1 30  ? 0.78393  37.45138 17.11570  1.000 43.50816  ? 31  ILE A N   1 
ATOM   222  C  CA  . ILE A 1 30  ? 1.35696  37.10004 15.82141  1.000 42.61420  ? 31  ILE A CA  1 
ATOM   223  C  C   . ILE A 1 30  ? 0.26995  36.80439 14.79629  1.000 42.34176  ? 31  ILE A C   1 
ATOM   224  O  O   . ILE A 1 30  ? 0.51897  36.89454 13.58828  1.000 55.42669  ? 31  ILE A O   1 
ATOM   225  C  CB  . ILE A 1 30  ? 2.32772  35.91042 15.96661  1.000 47.00369  ? 31  ILE A CB  1 
ATOM   226  C  CG1 . ILE A 1 30  ? 3.27203  35.83014 14.76491  1.000 46.91636  ? 31  ILE A CG1 1 
ATOM   227  C  CG2 . ILE A 1 30  ? 1.56939  34.60760 16.11965  1.000 52.58096  ? 31  ILE A CG2 1 
ATOM   228  C  CD1 . ILE A 1 30  ? 4.22528  36.99441 14.66264  1.000 46.32499  ? 31  ILE A CD1 1 
ATOM   229  N  N   . ALA A 1 31  ? -0.93942 36.46461 15.24809  1.000 46.43639  ? 32  ALA A N   1 
ATOM   230  C  CA  . ALA A 1 31  ? -2.05459 36.27127 14.32936  1.000 51.24753  ? 32  ALA A CA  1 
ATOM   231  C  C   . ALA A 1 31  ? -2.57069 37.60144 13.79647  1.000 49.41785  ? 32  ALA A C   1 
ATOM   232  O  O   . ALA A 1 31  ? -2.89187 37.71449 12.60823  1.000 52.46589  ? 32  ALA A O   1 
ATOM   233  C  CB  . ALA A 1 31  ? -3.17793 35.49882 15.02093  1.000 52.97877  ? 32  ALA A CB  1 
ATOM   234  N  N   . LYS A 1 32  ? -2.65422 38.61829 14.65802  1.000 52.18805  ? 33  LYS A N   1 
ATOM   235  C  CA  . LYS A 1 32  ? -3.07590 39.93628 14.19783  1.000 57.03082  ? 33  LYS A CA  1 
ATOM   236  C  C   . LYS A 1 32  ? -2.00171 40.59403 13.34282  1.000 42.50072  ? 33  LYS A C   1 
ATOM   237  O  O   . LYS A 1 32  ? -2.32148 41.33142 12.40301  1.000 55.35755  ? 33  LYS A O   1 
ATOM   238  C  CB  . LYS A 1 32  ? -3.42591 40.82771 15.38895  1.000 57.10422  ? 33  LYS A CB  1 
ATOM   239  C  CG  . LYS A 1 32  ? -4.21741 40.12411 16.47952  1.000 86.98075  ? 33  LYS A CG  1 
ATOM   240  C  CD  . LYS A 1 32  ? -5.29144 41.02830 17.06237  1.000 87.82707  ? 33  LYS A CD  1 
ATOM   241  C  CE  . LYS A 1 32  ? -5.85474 40.44923 18.35131  1.000 73.58069  ? 33  LYS A CE  1 
ATOM   242  N  NZ  . LYS A 1 32  ? -6.22851 39.01512 18.20828  1.000 83.64824  ? 33  LYS A NZ  1 
ATOM   243  N  N   . ILE A 1 33  ? -0.72856 40.33756 13.64809  1.000 46.44052  ? 34  ILE A N   1 
ATOM   244  C  CA  . ILE A 1 33  ? 0.35250  40.89358 12.84205  1.000 38.88762  ? 34  ILE A CA  1 
ATOM   245  C  C   . ILE A 1 33  ? 0.36909  40.25503 11.45856  1.000 37.85877  ? 34  ILE A C   1 
ATOM   246  O  O   . ILE A 1 33  ? 0.58311  40.93728 10.44917  1.000 44.86506  ? 34  ILE A O   1 
ATOM   247  C  CB  . ILE A 1 33  ? 1.69881  40.72693 13.57073  1.000 48.15309  ? 34  ILE A CB  1 
ATOM   248  C  CG1 . ILE A 1 33  ? 1.73969  41.62480 14.80996  1.000 43.85732  ? 34  ILE A CG1 1 
ATOM   249  C  CG2 . ILE A 1 33  ? 2.86186  41.04286 12.64010  1.000 37.87208  ? 34  ILE A CG2 1 
ATOM   250  C  CD1 . ILE A 1 33  ? 2.98862  41.46672 15.64226  1.000 57.38229  ? 34  ILE A CD1 1 
ATOM   251  N  N   . PHE A 1 34  ? 0.13072  38.94190 11.38434  1.000 31.77201  ? 35  PHE A N   1 
ATOM   252  C  CA  . PHE A 1 34  ? 0.07695  38.27861 10.08529  1.000 38.87100  ? 35  PHE A CA  1 
ATOM   253  C  C   . PHE A 1 34  ? -1.06833 38.80775 9.23400   1.000 34.53910  ? 35  PHE A C   1 
ATOM   254  O  O   . PHE A 1 34  ? -0.94099 38.89505 8.00694   1.000 40.29930  ? 35  PHE A O   1 
ATOM   255  C  CB  . PHE A 1 34  ? -0.05412 36.76548 10.26263  1.000 37.93312  ? 35  PHE A CB  1 
ATOM   256  C  CG  . PHE A 1 34  ? -0.33961 36.03266 8.98227   1.000 49.47875  ? 35  PHE A CG  1 
ATOM   257  C  CD1 . PHE A 1 34  ? 0.65411  35.85925 8.03354   1.000 41.27996  ? 35  PHE A CD1 1 
ATOM   258  C  CD2 . PHE A 1 34  ? -1.60287 35.52487 8.72384   1.000 48.59276  ? 35  PHE A CD2 1 
ATOM   259  C  CE1 . PHE A 1 34  ? 0.39587  35.19191 6.85133   1.000 42.52985  ? 35  PHE A CE1 1 
ATOM   260  C  CE2 . PHE A 1 34  ? -1.86750 34.85478 7.54328   1.000 63.28602  ? 35  PHE A CE2 1 
ATOM   261  C  CZ  . PHE A 1 34  ? -0.86588 34.68778 6.60600   1.000 46.80653  ? 35  PHE A CZ  1 
ATOM   262  N  N   . SER A 1 35  ? -2.19180 39.16148 9.86231   1.000 49.65199  ? 36  SER A N   1 
ATOM   263  C  CA  . SER A 1 35  ? -3.30032 39.74729 9.11657   1.000 42.20018  ? 36  SER A CA  1 
ATOM   264  C  C   . SER A 1 35  ? -2.90550 41.08838 8.51368   1.000 43.93770  ? 36  SER A C   1 
ATOM   265  O  O   . SER A 1 35  ? -3.34519 41.43693 7.41140   1.000 44.31658  ? 36  SER A O   1 
ATOM   266  C  CB  . SER A 1 35  ? -4.51905 39.90301 10.02557  1.000 58.79448  ? 36  SER A CB  1 
ATOM   267  O  OG  . SER A 1 35  ? -4.91642 38.65243 10.55968  1.000 66.87041  ? 36  SER A OG  1 
ATOM   268  N  N   . LEU A 1 36  ? -2.07467 41.85533 9.22308   1.000 38.35464  ? 37  LEU A N   1 
ATOM   269  C  CA  . LEU A 1 36  ? -1.58875 43.11608 8.67445   1.000 42.51897  ? 37  LEU A CA  1 
ATOM   270  C  C   . LEU A 1 36  ? -0.52890 42.87793 7.60657   1.000 40.82885  ? 37  LEU A C   1 
ATOM   271  O  O   . LEU A 1 36  ? -0.47673 43.60042 6.60444   1.000 42.23701  ? 37  LEU A O   1 
ATOM   272  C  CB  . LEU A 1 36  ? -1.03630 43.99592 9.79504   1.000 44.96985  ? 37  LEU A CB  1 
ATOM   273  C  CG  . LEU A 1 36  ? -2.02424 44.36852 10.90172  1.000 49.16133  ? 37  LEU A CG  1 
ATOM   274  C  CD1 . LEU A 1 36  ? -1.32314 45.12955 12.01527  1.000 39.35007  ? 37  LEU A CD1 1 
ATOM   275  C  CD2 . LEU A 1 36  ? -3.17920 45.18024 10.33490  1.000 43.11085  ? 37  LEU A CD2 1 
ATOM   276  N  N   . MET A 1 37  ? 0.32531  41.86911 7.80490   1.000 38.38311  ? 38  MET A N   1 
ATOM   277  C  CA  . MET A 1 37  ? 1.36174  41.56537 6.82344   1.000 38.76498  ? 38  MET A CA  1 
ATOM   278  C  C   . MET A 1 37  ? 0.76876  41.08319 5.50687   1.000 36.95531  ? 38  MET A C   1 
ATOM   279  O  O   . MET A 1 37  ? 1.32044  41.37153 4.43869   1.000 46.32161  ? 38  MET A O   1 
ATOM   280  C  CB  . MET A 1 37  ? 2.32446  40.51471 7.37900   1.000 42.53548  ? 38  MET A CB  1 
ATOM   281  C  CG  . MET A 1 37  ? 3.16359  40.98705 8.55082   1.000 36.50823  ? 38  MET A CG  1 
ATOM   282  S  SD  . MET A 1 37  ? 4.23468  39.69144 9.20149   1.000 38.77425  ? 38  MET A SD  1 
ATOM   283  C  CE  . MET A 1 37  ? 5.26670  39.34192 7.78047   1.000 31.25435  ? 38  MET A CE  1 
ATOM   284  N  N   . LYS A 1 38  ? -0.34740 40.35248 5.56069   1.000 37.98289  ? 39  LYS A N   1 
ATOM   285  C  CA  . LYS A 1 38  ? -0.95662 39.84056 4.33849   1.000 50.45874  ? 39  LYS A CA  1 
ATOM   286  C  C   . LYS A 1 38  ? -1.49458 40.96488 3.46288   1.000 41.52914  ? 39  LYS A C   1 
ATOM   287  O  O   . LYS A 1 38  ? -1.60300 40.79900 2.24334   1.000 47.25011  ? 39  LYS A O   1 
ATOM   288  C  CB  . LYS A 1 38  ? -2.07066 38.85105 4.68502   1.000 40.89184  ? 39  LYS A CB  1 
ATOM   289  C  CG  . LYS A 1 38  ? -2.53869 38.00349 3.51212   1.000 67.84950  ? 39  LYS A CG  1 
ATOM   290  C  CD  . LYS A 1 38  ? -3.58966 36.99296 3.94437   1.000 81.16360  ? 39  LYS A CD  1 
ATOM   291  C  CE  . LYS A 1 38  ? -4.03069 36.12732 2.77542   1.000 82.66090  ? 39  LYS A CE  1 
ATOM   292  N  NZ  . LYS A 1 38  ? -5.06608 35.13834 3.18187   1.000 92.27180  ? 39  LYS A NZ  1 
ATOM   293  N  N   . GLU A 1 39  ? -1.82752 42.10851 4.05652   1.000 41.27158  ? 40  GLU A N   1 
ATOM   294  C  CA  . GLU A 1 39  ? -2.30939 43.26337 3.31295   1.000 44.68941  ? 40  GLU A CA  1 
ATOM   295  C  C   . GLU A 1 39  ? -1.21579 44.28723 3.04296   1.000 46.69340  ? 40  GLU A C   1 
ATOM   296  O  O   . GLU A 1 39  ? -1.48848 45.31536 2.41556   1.000 48.07502  ? 40  GLU A O   1 
ATOM   297  C  CB  . GLU A 1 39  ? -3.46543 43.93185 4.06537   1.000 44.35071  ? 40  GLU A CB  1 
ATOM   298  C  CG  . GLU A 1 39  ? -4.48780 42.95564 4.62779   1.000 53.42274  ? 40  GLU A CG  1 
ATOM   299  C  CD  . GLU A 1 39  ? -5.17928 42.13718 3.55304   1.000 88.72926  ? 40  GLU A CD  1 
ATOM   300  O  OE1 . GLU A 1 39  ? -5.33912 42.64315 2.42204   1.000 88.63541  ? 40  GLU A OE1 1 
ATOM   301  O  OE2 . GLU A 1 39  ? -5.56254 40.98361 3.84096   1.000 90.23953  ? 40  GLU A OE2 1 
ATOM   302  N  N   . ALA A 1 40  ? 0.00873  44.03216 3.49711   1.000 36.83084  ? 41  ALA A N   1 
ATOM   303  C  CA  . ALA A 1 40  ? 1.10982  44.96728 3.30897   1.000 38.95928  ? 41  ALA A CA  1 
ATOM   304  C  C   . ALA A 1 40  ? 1.71705  44.77208 1.92552   1.000 40.84138  ? 41  ALA A C   1 
ATOM   305  O  O   . ALA A 1 40  ? 2.25903  43.70321 1.62318   1.000 43.05105  ? 41  ALA A O   1 
ATOM   306  C  CB  . ALA A 1 40  ? 2.16576  44.77291 4.39394   1.000 30.35336  ? 41  ALA A CB  1 
ATOM   307  N  N   . ARG A 1 41  ? 1.62527  45.80224 1.08616   1.000 38.69656  ? 42  ARG A N   1 
ATOM   308  C  CA  . ARG A 1 41  ? 2.18393  45.75929 -0.25804  1.000 44.72119  ? 42  ARG A CA  1 
ATOM   309  C  C   . ARG A 1 41  ? 3.35402  46.70688 -0.46045  1.000 44.36115  ? 42  ARG A C   1 
ATOM   310  O  O   . ARG A 1 41  ? 4.20235  46.44356 -1.31485  1.000 48.00056  ? 42  ARG A O   1 
ATOM   311  C  CB  . ARG A 1 41  ? 1.10051  46.07686 -1.29697  1.000 43.49083  ? 42  ARG A CB  1 
ATOM   312  C  CG  . ARG A 1 41  ? -0.03412 45.06570 -1.33302  1.000 64.41638  ? 42  ARG A CG  1 
ATOM   313  C  CD  . ARG A 1 41  ? 0.49658  43.65546 -1.54466  1.000 81.32422  ? 42  ARG A CD  1 
ATOM   314  N  NE  . ARG A 1 41  ? -0.56832 42.65936 -1.56380  1.000 93.21799  ? 42  ARG A NE  1 
ATOM   315  C  CZ  . ARG A 1 41  ? -1.17104 42.22764 -2.66326  1.000 103.50683 ? 42  ARG A CZ  1 
ATOM   316  N  NH1 . ARG A 1 41  ? -0.83986 42.68716 -3.85899  1.000 88.70435  ? 42  ARG A NH1 1 
ATOM   317  N  NH2 . ARG A 1 41  ? -2.12949 41.31111 -2.56056  1.000 105.17619 ? 42  ARG A NH2 1 
ATOM   318  N  N   . LYS A 1 42  ? 3.42174  47.79510 0.29997   1.000 37.04264  ? 43  LYS A N   1 
ATOM   319  C  CA  . LYS A 1 42  ? 4.53794  48.72130 0.19847   1.000 42.64162  ? 43  LYS A CA  1 
ATOM   320  C  C   . LYS A 1 42  ? 5.77809  48.13586 0.86380   1.000 40.92788  ? 43  LYS A C   1 
ATOM   321  O  O   . LYS A 1 42  ? 5.69084  47.37714 1.83353   1.000 36.20364  ? 43  LYS A O   1 
ATOM   322  C  CB  . LYS A 1 42  ? 4.18285  50.06325 0.83897   1.000 43.65200  ? 43  LYS A CB  1 
ATOM   323  C  CG  . LYS A 1 42  ? 3.08486  50.83027 0.11689   1.000 44.64775  ? 43  LYS A CG  1 
ATOM   324  C  CD  . LYS A 1 42  ? 3.51916  51.23321 -1.28256  1.000 44.94853  ? 43  LYS A CD  1 
ATOM   325  C  CE  . LYS A 1 42  ? 2.45410  52.07395 -1.96862  1.000 52.01473  ? 43  LYS A CE  1 
ATOM   326  N  NZ  . LYS A 1 42  ? 2.87618  52.51743 -3.32670  1.000 56.87536  ? 43  LYS A NZ  1 
ATOM   327  N  N   . MET A 1 43  ? 6.94585  48.50780 0.33339   1.000 36.84762  ? 44  MET A N   1 
ATOM   328  C  CA  . MET A 1 43  ? 8.19532  47.92082 0.80668   1.000 33.36095  ? 44  MET A CA  1 
ATOM   329  C  C   . MET A 1 43  ? 8.51478  48.33020 2.23960   1.000 32.30945  ? 44  MET A C   1 
ATOM   330  O  O   . MET A 1 43  ? 9.07989  47.53197 2.99614   1.000 38.78796  ? 44  MET A O   1 
ATOM   331  C  CB  . MET A 1 43  ? 9.34142  48.31170 -0.12440  1.000 36.11100  ? 44  MET A CB  1 
ATOM   332  C  CG  . MET A 1 43  ? 10.66516 47.65002 0.21375   1.000 39.04121  ? 44  MET A CG  1 
ATOM   333  S  SD  . MET A 1 43  ? 12.00927 48.22743 -0.83494  1.000 37.11935  ? 44  MET A SD  1 
ATOM   334  C  CE  . MET A 1 43  ? 13.40103 47.36544 -0.10539  1.000 43.38088  ? 44  MET A CE  1 
ATOM   335  N  N   . VAL A 1 44  ? 8.16892  49.55934 2.62985   1.000 32.99145  ? 45  VAL A N   1 
ATOM   336  C  CA  . VAL A 1 44  ? 8.44328  50.01023 3.99238   1.000 32.27006  ? 45  VAL A CA  1 
ATOM   337  C  C   . VAL A 1 44  ? 7.68434  49.15819 5.00054   1.000 35.24855  ? 45  VAL A C   1 
ATOM   338  O  O   . VAL A 1 44  ? 8.22841  48.76974 6.04190   1.000 33.53360  ? 45  VAL A O   1 
ATOM   339  C  CB  . VAL A 1 44  ? 8.09815  51.50315 4.14249   1.000 35.58587  ? 45  VAL A CB  1 
ATOM   340  C  CG1 . VAL A 1 44  ? 8.26835  51.94601 5.58601   1.000 35.99166  ? 45  VAL A CG1 1 
ATOM   341  C  CG2 . VAL A 1 44  ? 8.96767  52.33728 3.22514   1.000 36.82417  ? 45  VAL A CG2 1 
ATOM   342  N  N   . SER A 1 45  ? 6.41665  48.85402 4.70964   1.000 30.52331  ? 46  SER A N   1 
ATOM   343  C  CA  . SER A 1 45  ? 5.63130  48.02374 5.61706   1.000 34.47349  ? 46  SER A CA  1 
ATOM   344  C  C   . SER A 1 45  ? 6.20959  46.61861 5.71527   1.000 29.37869  ? 46  SER A C   1 
ATOM   345  O  O   . SER A 1 45  ? 6.29216  46.04822 6.80886   1.000 30.38529  ? 46  SER A O   1 
ATOM   346  C  CB  . SER A 1 45  ? 4.17479  47.97013 5.15555   1.000 32.38785  ? 46  SER A CB  1 
ATOM   347  O  OG  . SER A 1 45  ? 3.61229  49.26751 5.08467   1.000 43.53038  ? 46  SER A OG  1 
ATOM   348  N  N   . ARG A 1 46  ? 6.62224  46.04708 4.58131   1.000 28.93531  ? 47  ARG A N   1 
ATOM   349  C  CA  . ARG A 1 46  ? 7.16610  44.69318 4.59122   1.000 33.91692  ? 47  ARG A CA  1 
ATOM   350  C  C   . ARG A 1 46  ? 8.48584  44.63046 5.34931   1.000 31.93870  ? 47  ARG A C   1 
ATOM   351  O  O   . ARG A 1 46  ? 8.69923  43.72015 6.15805   1.000 34.09402  ? 47  ARG A O   1 
ATOM   352  C  CB  . ARG A 1 46  ? 7.34016  44.18964 3.15869   1.000 26.13186  ? 47  ARG A CB  1 
ATOM   353  C  CG  . ARG A 1 46  ? 6.03322  44.06458 2.39718   1.000 37.23660  ? 47  ARG A CG  1 
ATOM   354  C  CD  . ARG A 1 46  ? 6.25055  43.57618 0.97595   1.000 31.59482  ? 47  ARG A CD  1 
ATOM   355  N  NE  . ARG A 1 46  ? 4.98573  43.24896 0.32942   1.000 40.94309  ? 47  ARG A NE  1 
ATOM   356  C  CZ  . ARG A 1 46  ? 4.86886  42.81260 -0.91698  1.000 42.75267  ? 47  ARG A CZ  1 
ATOM   357  N  NH1 . ARG A 1 46  ? 5.92640  42.65059 -1.69507  1.000 35.28741  ? 47  ARG A NH1 1 
ATOM   358  N  NH2 . ARG A 1 46  ? 3.65997  42.53084 -1.39426  1.000 42.18630  ? 47  ARG A NH2 1 
ATOM   359  N  N   . SER A 1 47  ? 9.38044  45.59185 5.10856   1.000 30.71186  ? 48  SER A N   1 
ATOM   360  C  CA  . SER A 1 47  ? 10.66422 45.59334 5.80253   1.000 29.97939  ? 48  SER A CA  1 
ATOM   361  C  C   . SER A 1 47  ? 10.49555 45.81187 7.30142   1.000 26.73809  ? 48  SER A C   1 
ATOM   362  O  O   . SER A 1 47  ? 11.28330 45.28491 8.09513   1.000 37.81186  ? 48  SER A O   1 
ATOM   363  C  CB  . SER A 1 47  ? 11.58004 46.66290 5.20683   1.000 27.45602  ? 48  SER A CB  1 
ATOM   364  O  OG  . SER A 1 47  ? 12.88024 46.59245 5.76525   1.000 31.55903  ? 48  SER A OG  1 
ATOM   365  N  N   . THR A 1 48  ? 9.48012  46.57761 7.70792   1.000 30.51594  ? 49  THR A N   1 
ATOM   366  C  CA  . THR A 1 48  ? 9.24535  46.79747 9.13189   1.000 26.85606  ? 49  THR A CA  1 
ATOM   367  C  C   . THR A 1 48  ? 8.70452  45.54062 9.80335   1.000 25.43034  ? 49  THR A C   1 
ATOM   368  O  O   . THR A 1 48  ? 9.14235  45.17929 10.90224  1.000 30.72041  ? 49  THR A O   1 
ATOM   369  C  CB  . THR A 1 48  ? 8.28552  47.97129 9.33011   1.000 33.26717  ? 49  THR A CB  1 
ATOM   370  O  OG1 . THR A 1 48  ? 8.89828  49.17513 8.85113   1.000 31.58357  ? 49  THR A OG1 1 
ATOM   371  C  CG2 . THR A 1 48  ? 7.93557  48.13922 10.80199  1.000 33.74848  ? 49  THR A CG2 1 
ATOM   372  N  N   . TYR A 1 49  ? 7.75542  44.85851 9.15768   1.000 30.09653  ? 50  TYR A N   1 
ATOM   373  C  CA  . TYR A 1 49  ? 7.21872  43.62687 9.72665   1.000 28.51515  ? 50  TYR A CA  1 
ATOM   374  C  C   . TYR A 1 49  ? 8.26323  42.51873 9.76027   1.000 33.82742  ? 50  TYR A C   1 
ATOM   375  O  O   . TYR A 1 49  ? 8.23125  41.66800 10.65683  1.000 38.57259  ? 50  TYR A O   1 
ATOM   376  C  CB  . TYR A 1 49  ? 5.98851  43.17739 8.93984   1.000 25.33609  ? 50  TYR A CB  1 
ATOM   377  C  CG  . TYR A 1 49  ? 4.76494  44.02836 9.19176   1.000 37.00066  ? 50  TYR A CG  1 
ATOM   378  C  CD1 . TYR A 1 49  ? 4.41805  44.41377 10.48004  1.000 44.47202  ? 50  TYR A CD1 1 
ATOM   379  C  CD2 . TYR A 1 49  ? 3.96289  44.45532 8.14168   1.000 26.24298  ? 50  TYR A CD2 1 
ATOM   380  C  CE1 . TYR A 1 49  ? 3.30157  45.19511 10.71669  1.000 45.16668  ? 50  TYR A CE1 1 
ATOM   381  C  CE2 . TYR A 1 49  ? 2.84470  45.23780 8.36806   1.000 35.83676  ? 50  TYR A CE2 1 
ATOM   382  C  CZ  . TYR A 1 49  ? 2.51941  45.60441 9.65718   1.000 45.07722  ? 50  TYR A CZ  1 
ATOM   383  O  OH  . TYR A 1 49  ? 1.40838  46.38243 9.88825   1.000 48.02377  ? 50  TYR A OH  1 
ATOM   384  N  N   . LEU A 1 50  ? 9.19082  42.50700 8.79950   1.000 34.70023  ? 51  LEU A N   1 
ATOM   385  C  CA  . LEU A 1 50  ? 10.26098 41.51698 8.83103   1.000 34.23633  ? 51  LEU A CA  1 
ATOM   386  C  C   . LEU A 1 50  ? 11.19422 41.74141 10.01258  1.000 33.55304  ? 51  LEU A C   1 
ATOM   387  O  O   . LEU A 1 50  ? 11.72065 40.77448 10.57474  1.000 31.15240  ? 51  LEU A O   1 
ATOM   388  C  CB  . LEU A 1 50  ? 11.04613 41.54272 7.51981   1.000 31.44899  ? 51  LEU A CB  1 
ATOM   389  C  CG  . LEU A 1 50  ? 10.32780 40.97297 6.29441   1.000 34.93236  ? 51  LEU A CG  1 
ATOM   390  C  CD1 . LEU A 1 50  ? 11.17736 41.13438 5.04339   1.000 34.47794  ? 51  LEU A CD1 1 
ATOM   391  C  CD2 . LEU A 1 50  ? 9.96612  39.51306 6.51616   1.000 31.38886  ? 51  LEU A CD2 1 
ATOM   392  N  N   . ASN A 1 51  ? 11.41357 43.00084 10.40138  1.000 30.81849  ? 52  ASN A N   1 
ATOM   393  C  CA  . ASN A 1 51  ? 12.22871 43.27452 11.58078  1.000 35.01946  ? 52  ASN A CA  1 
ATOM   394  C  C   . ASN A 1 51  ? 11.55743 42.75296 12.84554  1.000 32.80076  ? 52  ASN A C   1 
ATOM   395  O  O   . ASN A 1 51  ? 12.23446 42.27834 13.76430  1.000 31.92484  ? 52  ASN A O   1 
ATOM   396  C  CB  . ASN A 1 51  ? 12.50167 44.77492 11.69945  1.000 33.77646  ? 52  ASN A CB  1 
ATOM   397  C  CG  . ASN A 1 51  ? 13.38948 45.29924 10.58671  1.000 34.36813  ? 52  ASN A CG  1 
ATOM   398  O  OD1 . ASN A 1 51  ? 14.18098 44.55724 10.00670  1.000 36.08049  ? 52  ASN A OD1 1 
ATOM   399  N  ND2 . ASN A 1 51  ? 13.26229 46.58580 10.28523  1.000 31.74864  ? 52  ASN A ND2 1 
ATOM   400  N  N   . ILE A 1 52  ? 10.22673 42.83019 12.90805  1.000 32.34320  ? 53  ILE A N   1 
ATOM   401  C  CA  . ILE A 1 52  ? 9.50135  42.31575 14.06539  1.000 33.46103  ? 53  ILE A CA  1 
ATOM   402  C  C   . ILE A 1 52  ? 9.65835  40.80372 14.16628  1.000 32.77432  ? 53  ILE A C   1 
ATOM   403  O  O   . ILE A 1 52  ? 9.85665  40.25742 15.25812  1.000 33.48155  ? 53  ILE A O   1 
ATOM   404  C  CB  . ILE A 1 52  ? 8.02015  42.72807 13.98848  1.000 35.80002  ? 53  ILE A CB  1 
ATOM   405  C  CG1 . ILE A 1 52  ? 7.88685  44.25218 14.01604  1.000 31.88679  ? 53  ILE A CG1 1 
ATOM   406  C  CG2 . ILE A 1 52  ? 7.23098  42.10402 15.12553  1.000 32.96312  ? 53  ILE A CG2 1 
ATOM   407  C  CD1 . ILE A 1 52  ? 6.46423  44.73865 13.87161  1.000 37.05488  ? 53  ILE A CD1 1 
ATOM   408  N  N   . ILE A 1 53  ? 9.57147  40.10409 13.03297  1.000 31.07792  ? 54  ILE A N   1 
ATOM   409  C  CA  . ILE A 1 53  ? 9.75424  38.65630 13.03830  1.000 37.52928  ? 54  ILE A CA  1 
ATOM   410  C  C   . ILE A 1 53  ? 11.18707 38.30045 13.41504  1.000 35.57235  ? 54  ILE A C   1 
ATOM   411  O  O   . ILE A 1 53  ? 11.42651 37.35434 14.17504  1.000 36.03251  ? 54  ILE A O   1 
ATOM   412  C  CB  . ILE A 1 53  ? 9.36404  38.06409 11.67115  1.000 29.87057  ? 54  ILE A CB  1 
ATOM   413  C  CG1 . ILE A 1 53  ? 7.93054  38.45623 11.30582  1.000 32.57434  ? 54  ILE A CG1 1 
ATOM   414  C  CG2 . ILE A 1 53  ? 9.51694  36.55063 11.67818  1.000 33.43132  ? 54  ILE A CG2 1 
ATOM   415  C  CD1 . ILE A 1 53  ? 6.89320  37.97231 12.29255  1.000 33.46201  ? 54  ILE A CD1 1 
ATOM   416  N  N   . LEU A 1 54  ? 12.16101 39.05519 12.89727  1.000 31.89998  ? 55  LEU A N   1 
ATOM   417  C  CA  . LEU A 1 54  ? 13.56154 38.76748 13.19163  1.000 35.86207  ? 55  LEU A CA  1 
ATOM   418  C  C   . LEU A 1 54  ? 13.88118 38.95570 14.66884  1.000 34.32066  ? 55  LEU A C   1 
ATOM   419  O  O   . LEU A 1 54  ? 14.71724 38.22960 15.21913  1.000 31.77201  ? 55  LEU A O   1 
ATOM   420  C  CB  . LEU A 1 54  ? 14.46982 39.65196 12.33649  1.000 29.42742  ? 55  LEU A CB  1 
ATOM   421  C  CG  . LEU A 1 54  ? 14.59344 39.26820 10.86118  1.000 30.58726  ? 55  LEU A CG  1 
ATOM   422  C  CD1 . LEU A 1 54  ? 15.26044 40.38086 10.06910  1.000 30.20254  ? 55  LEU A CD1 1 
ATOM   423  C  CD2 . LEU A 1 54  ? 15.37169 37.97147 10.72213  1.000 28.97351  ? 55  LEU A CD2 1 
ATOM   424  N  N   . GLN A 1 55  ? 13.23257 39.91748 15.32719  1.000 33.65217  ? 56  GLN A N   1 
ATOM   425  C  CA  . GLN A 1 55  ? 13.48497 40.15437 16.74281  1.000 39.07886  ? 56  GLN A CA  1 
ATOM   426  C  C   . GLN A 1 55  ? 12.76446 39.16147 17.64459  1.000 32.11708  ? 56  GLN A C   1 
ATOM   427  O  O   . GLN A 1 55  ? 13.21198 38.93600 18.77442  1.000 36.93814  ? 56  GLN A O   1 
ATOM   428  C  CB  . GLN A 1 55  ? 13.08269 41.58247 17.11793  1.000 32.17643  ? 56  GLN A CB  1 
ATOM   429  C  CG  . GLN A 1 55  ? 13.93398 42.65628 16.45684  1.000 43.24493  ? 56  GLN A CG  1 
ATOM   430  C  CD  . GLN A 1 55  ? 15.41135 42.50402 16.76775  1.000 43.18601  ? 56  GLN A CD  1 
ATOM   431  O  OE1 . GLN A 1 55  ? 15.87914 42.91136 17.83080  1.000 56.64107  ? 56  GLN A OE1 1 
ATOM   432  N  NE2 . GLN A 1 55  ? 16.15455 41.91422 15.83792  1.000 34.04004  ? 56  GLN A NE2 1 
ATOM   433  N  N   . THR A 1 56  ? 11.67044 38.56548 17.17589  1.000 33.14696  ? 57  THR A N   1 
ATOM   434  C  CA  . THR A 1 56  ? 10.94217 37.59011 17.97713  1.000 32.63847  ? 57  THR A CA  1 
ATOM   435  C  C   . THR A 1 56  ? 11.72798 36.28695 18.05657  1.000 38.59127  ? 57  THR A C   1 
ATOM   436  O  O   . THR A 1 56  ? 12.12012 35.72384 17.03046  1.000 39.76839  ? 57  THR A O   1 
ATOM   437  C  CB  . THR A 1 56  ? 9.55942  37.33897 17.37660  1.000 31.53916  ? 57  THR A CB  1 
ATOM   438  O  OG1 . THR A 1 56  ? 8.85899  38.58322 17.25298  1.000 38.08551  ? 57  THR A OG1 1 
ATOM   439  C  CG2 . THR A 1 56  ? 8.75610  36.39600 18.26327  1.000 32.09886  ? 57  THR A CG2 1 
ATOM   440  N  N   . ARG A 1 57  ? 11.95433 35.80217 19.27988  1.000 43.11428  ? 58  ARG A N   1 
ATOM   441  C  CA  . ARG A 1 57  ? 12.77995 34.62209 19.49466  1.000 41.72108  ? 58  ARG A CA  1 
ATOM   442  C  C   . ARG A 1 57  ? 12.03015 33.43133 20.07289  1.000 34.27964  ? 58  ARG A C   1 
ATOM   443  O  O   . ARG A 1 57  ? 12.55768 32.31546 20.02703  1.000 50.48378  ? 58  ARG A O   1 
ATOM   444  C  CB  . ARG A 1 57  ? 13.95353 34.95692 20.42569  1.000 48.11776  ? 58  ARG A CB  1 
ATOM   445  C  CG  . ARG A 1 57  ? 14.85328 36.07017 19.92357  1.000 50.25231  ? 58  ARG A CG  1 
ATOM   446  C  CD  . ARG A 1 57  ? 15.84368 36.47904 20.99833  1.000 74.65174  ? 58  ARG A CD  1 
ATOM   447  N  NE  . ARG A 1 57  ? 15.16489 36.80721 22.24615  1.000 87.64773  ? 58  ARG A NE  1 
ATOM   448  C  CZ  . ARG A 1 57  ? 15.78047 37.12261 23.37729  1.000 97.58125  ? 58  ARG A CZ  1 
ATOM   449  N  NH1 . ARG A 1 57  ? 17.10030 37.16674 23.45739  1.000 98.97680  ? 58  ARG A NH1 1 
ATOM   450  N  NH2 . ARG A 1 57  ? 15.05310 37.39919 24.45608  1.000 91.11788  ? 58  ARG A NH2 1 
ATOM   451  N  N   . ALA A 1 58  ? 10.83687 33.63394 20.61798  1.000 44.06425  ? 59  ALA A N   1 
ATOM   452  C  CA  . ALA A 1 58  ? 10.07307 32.53787 21.19892  1.000 45.11214  ? 59  ALA A CA  1 
ATOM   453  C  C   . ALA A 1 58  ? 9.70406  31.52755 20.11809  1.000 53.63097  ? 59  ALA A C   1 
ATOM   454  O  O   . ALA A 1 58  ? 9.02407  31.89230 19.14616  1.000 49.22711  ? 59  ALA A O   1 
ATOM   455  C  CB  . ALA A 1 58  ? 8.81568  33.06509 21.88429  1.000 44.63174  ? 59  ALA A CB  1 
ATOM   456  N  N   . PRO A 1 59  ? 10.12375 30.26511 20.23969  1.000 44.66060  ? 60  PRO A N   1 
ATOM   457  C  CA  . PRO A 1 59  ? 9.85035  29.30166 19.15928  1.000 37.67587  ? 60  PRO A CA  1 
ATOM   458  C  C   . PRO A 1 59  ? 8.37202  29.02478 18.95609  1.000 53.11554  ? 60  PRO A C   1 
ATOM   459  O  O   . PRO A 1 59  ? 7.93150  28.85893 17.81200  1.000 50.95500  ? 60  PRO A O   1 
ATOM   460  C  CB  . PRO A 1 59  ? 10.61210 28.04875 19.61377  1.000 50.19921  ? 60  PRO A CB  1 
ATOM   461  C  CG  . PRO A 1 59  ? 10.70399 28.18301 21.09930  1.000 49.88967  ? 60  PRO A CG  1 
ATOM   462  C  CD  . PRO A 1 59  ? 10.84628 29.65227 21.36690  1.000 61.25149  ? 60  PRO A CD  1 
ATOM   463  N  N   . GLU A 1 60  ? 7.58819  28.97276 20.03620  1.000 47.15546  ? 61  GLU A N   1 
ATOM   464  C  CA  . GLU A 1 60  ? 6.15564  28.73538 19.89327  1.000 45.94755  ? 61  GLU A CA  1 
ATOM   465  C  C   . GLU A 1 60  ? 5.46682  29.88091 19.16168  1.000 44.41124  ? 61  GLU A C   1 
ATOM   466  O  O   . GLU A 1 60  ? 4.44762  29.66448 18.49646  1.000 44.88085  ? 61  GLU A O   1 
ATOM   467  C  CB  . GLU A 1 60  ? 5.51359  28.51187 21.26528  1.000 65.43573  ? 61  GLU A CB  1 
ATOM   468  C  CG  . GLU A 1 60  ? 5.63583  29.68475 22.23437  1.000 74.25461  ? 61  GLU A CG  1 
ATOM   469  C  CD  . GLU A 1 60  ? 6.98299  29.74255 22.93702  1.000 70.88677  ? 61  GLU A CD  1 
ATOM   470  O  OE1 . GLU A 1 60  ? 7.83172  28.86052 22.68564  1.000 64.99515  ? 61  GLU A OE1 1 
ATOM   471  O  OE2 . GLU A 1 60  ? 7.19158  30.67222 23.74454  1.000 68.22105  ? 61  GLU A OE2 1 
ATOM   472  N  N   . VAL A 1 61  ? 6.00516  31.09694 19.26487  1.000 42.25916  ? 62  VAL A N   1 
ATOM   473  C  CA  . VAL A 1 61  ? 5.44518  32.22275 18.52481  1.000 37.60617  ? 62  VAL A CA  1 
ATOM   474  C  C   . VAL A 1 61  ? 5.86685  32.16696 17.06131  1.000 31.27402  ? 62  VAL A C   1 
ATOM   475  O  O   . VAL A 1 61  ? 5.07474  32.47267 16.16262  1.000 35.26249  ? 62  VAL A O   1 
ATOM   476  C  CB  . VAL A 1 61  ? 5.85889  33.54970 19.18740  1.000 43.05031  ? 62  VAL A CB  1 
ATOM   477  C  CG1 . VAL A 1 61  ? 5.33968  34.73317 18.38556  1.000 37.04832  ? 62  VAL A CG1 1 
ATOM   478  C  CG2 . VAL A 1 61  ? 5.34821  33.60848 20.61967  1.000 43.93749  ? 62  VAL A CG2 1 
ATOM   479  N  N   . LEU A 1 62  ? 7.11375  31.76939 16.79734  1.000 36.48938  ? 63  LEU A N   1 
ATOM   480  C  CA  . LEU A 1 62  ? 7.58572  31.68276 15.41910  1.000 40.84887  ? 63  LEU A CA  1 
ATOM   481  C  C   . LEU A 1 62  ? 6.89169  30.55484 14.66441  1.000 40.74104  ? 63  LEU A C   1 
ATOM   482  O  O   . LEU A 1 62  ? 6.57724  30.69854 13.47708  1.000 37.94465  ? 63  LEU A O   1 
ATOM   483  C  CB  . LEU A 1 62  ? 9.10234  31.49384 15.39568  1.000 31.88202  ? 63  LEU A CB  1 
ATOM   484  C  CG  . LEU A 1 62  ? 9.93440  32.61109 16.03069  1.000 36.30720  ? 63  LEU A CG  1 
ATOM   485  C  CD1 . LEU A 1 62  ? 11.41821 32.28453 15.96173  1.000 38.70124  ? 63  LEU A CD1 1 
ATOM   486  C  CD2 . LEU A 1 62  ? 9.64480  33.94413 15.36042  1.000 37.17481  ? 63  LEU A CD2 1 
ATOM   487  N  N   . VAL A 1 63  ? 6.64730  29.42458 15.33323  1.000 36.83356  ? 64  VAL A N   1 
ATOM   488  C  CA  . VAL A 1 63  ? 5.94093  28.31884 14.68981  1.000 38.61821  ? 64  VAL A CA  1 
ATOM   489  C  C   . VAL A 1 63  ? 4.51496  28.72874 14.34494  1.000 37.87405  ? 64  VAL A C   1 
ATOM   490  O  O   . VAL A 1 63  ? 3.98235  28.35630 13.29150  1.000 43.67156  ? 64  VAL A O   1 
ATOM   491  C  CB  . VAL A 1 63  ? 5.97379  27.06696 15.58759  1.000 36.64079  ? 64  VAL A CB  1 
ATOM   492  C  CG1 . VAL A 1 63  ? 5.05017  25.98730 15.04062  1.000 39.42459  ? 64  VAL A CG1 1 
ATOM   493  C  CG2 . VAL A 1 63  ? 7.39354  26.53532 15.70160  1.000 49.75449  ? 64  VAL A CG2 1 
ATOM   494  N  N   . LYS A 1 64  ? 3.87791  29.51065 15.22027  1.000 36.63590  ? 65  LYS A N   1 
ATOM   495  C  CA  . LYS A 1 64  ? 2.52595  29.98281 14.93949  1.000 31.75103  ? 65  LYS A CA  1 
ATOM   496  C  C   . LYS A 1 64  ? 2.50139  30.87526 13.70474  1.000 43.30242  ? 65  LYS A C   1 
ATOM   497  O  O   . LYS A 1 64  ? 1.55386  30.82426 12.91174  1.000 43.93748  ? 65  LYS A O   1 
ATOM   498  C  CB  . LYS A 1 64  ? 1.96755  30.72421 16.15383  1.000 39.48109  ? 65  LYS A CB  1 
ATOM   499  C  CG  . LYS A 1 64  ? 0.52123  31.17108 16.00385  1.000 45.98404  ? 65  LYS A CG  1 
ATOM   500  C  CD  . LYS A 1 64  ? -0.41029 29.98840 15.79911  1.000 52.17430  ? 65  LYS A CD  1 
ATOM   501  C  CE  . LYS A 1 64  ? -1.86427 30.43396 15.74853  1.000 64.24112  ? 65  LYS A CE  1 
ATOM   502  N  NZ  . LYS A 1 64  ? -2.78982 29.29438 15.49261  1.000 74.11073  ? 65  LYS A NZ  1 
ATOM   503  N  N   . PHE A 1 65  ? 3.53805  31.69860 13.52281  1.000 36.40222  ? 66  PHE A N   1 
ATOM   504  C  CA  . PHE A 1 65  ? 3.62369  32.52248 12.32075  1.000 45.04982  ? 66  PHE A CA  1 
ATOM   505  C  C   . PHE A 1 65  ? 3.70686  31.65933 11.06842  1.000 36.16306  ? 66  PHE A C   1 
ATOM   506  O  O   . PHE A 1 65  ? 3.13135  32.00151 10.02901  1.000 34.24799  ? 66  PHE A O   1 
ATOM   507  C  CB  . PHE A 1 65  ? 4.82919  33.45985 12.40829  1.000 38.47834  ? 66  PHE A CB  1 
ATOM   508  C  CG  . PHE A 1 65  ? 5.10163  34.21769 11.13865  1.000 36.50682  ? 66  PHE A CG  1 
ATOM   509  C  CD1 . PHE A 1 65  ? 4.32869  35.31344 10.79038  1.000 40.68847  ? 66  PHE A CD1 1 
ATOM   510  C  CD2 . PHE A 1 65  ? 6.13357  33.83702 10.29503  1.000 36.40876  ? 66  PHE A CD2 1 
ATOM   511  C  CE1 . PHE A 1 65  ? 4.57634  36.01307 9.62229   1.000 38.14997  ? 66  PHE A CE1 1 
ATOM   512  C  CE2 . PHE A 1 65  ? 6.38652  34.53215 9.12683   1.000 38.79365  ? 66  PHE A CE2 1 
ATOM   513  C  CZ  . PHE A 1 65  ? 5.60719  35.62147 8.79044   1.000 39.10414  ? 66  PHE A CZ  1 
ATOM   514  N  N   . ILE A 1 66  ? 4.41454  30.53170 11.15036  1.000 35.65314  ? 67  ILE A N   1 
ATOM   515  C  CA  . ILE A 1 66  ? 4.51017  29.62991 10.00763  1.000 34.90258  ? 67  ILE A CA  1 
ATOM   516  C  C   . ILE A 1 66  ? 3.17320  28.94418 9.75237   1.000 44.75597  ? 67  ILE A C   1 
ATOM   517  O  O   . ILE A 1 66  ? 2.76337  28.76165 8.59938   1.000 43.50074  ? 67  ILE A O   1 
ATOM   518  C  CB  . ILE A 1 66  ? 5.63825  28.60720 10.23537  1.000 37.45474  ? 67  ILE A CB  1 
ATOM   519  C  CG1 . ILE A 1 66  ? 6.97362  29.32412 10.44361  1.000 31.31485  ? 67  ILE A CG1 1 
ATOM   520  C  CG2 . ILE A 1 66  ? 5.72831  27.63591 9.06834   1.000 48.28621  ? 67  ILE A CG2 1 
ATOM   521  C  CD1 . ILE A 1 66  ? 8.10082  28.40398 10.86181  1.000 33.35662  ? 67  ILE A CD1 1 
ATOM   522  N  N   . ASP A 1 67  ? 2.46491  28.56792 10.82024  1.000 41.27048  ? 68  ASP A N   1 
ATOM   523  C  CA  . ASP A 1 67  ? 1.24185  27.78638 10.66030  1.000 54.43812  ? 68  ASP A CA  1 
ATOM   524  C  C   . ASP A 1 67  ? 0.10780  28.62329 10.07878  1.000 42.13064  ? 68  ASP A C   1 
ATOM   525  O  O   . ASP A 1 67  ? -0.67077 28.13025 9.25434   1.000 49.07263  ? 68  ASP A O   1 
ATOM   526  C  CB  . ASP A 1 67  ? 0.82668  27.18007 12.00095  1.000 47.98833  ? 68  ASP A CB  1 
ATOM   527  C  CG  . ASP A 1 67  ? 1.80432  26.12919 12.49470  1.000 66.80510  ? 68  ASP A CG  1 
ATOM   528  O  OD1 . ASP A 1 67  ? 2.50077  25.51941 11.65578  1.000 53.72446  ? 68  ASP A OD1 1 
ATOM   529  O  OD2 . ASP A 1 67  ? 1.87280  25.90928 13.72264  1.000 57.72631  ? 68  ASP A OD2 1 
ATOM   530  N  N   . VAL A 1 68  ? -0.00696 29.88857 10.49274  1.000 41.86122  ? 69  VAL A N   1 
ATOM   531  C  CA  . VAL A 1 68  ? -1.10477 30.73016 10.02548  1.000 39.89992  ? 69  VAL A CA  1 
ATOM   532  C  C   . VAL A 1 68  ? -0.98116 31.10871 8.55902   1.000 49.69562  ? 69  VAL A C   1 
ATOM   533  O  O   . VAL A 1 68  ? -1.94123 31.63424 7.98419   1.000 40.38957  ? 69  VAL A O   1 
ATOM   534  C  CB  . VAL A 1 68  ? -1.22068 32.01656 10.86961  1.000 46.60066  ? 69  VAL A CB  1 
ATOM   535  C  CG1 . VAL A 1 68  ? -1.53395 31.67646 12.31741  1.000 49.43729  ? 69  VAL A CG1 1 
ATOM   536  C  CG2 . VAL A 1 68  ? 0.05301  32.84460 10.76666  1.000 36.46566  ? 69  VAL A CG2 1 
ATOM   537  N  N   . GLY A 1 69  ? 0.16891  30.85808 7.93810   1.000 39.60338  ? 70  GLY A N   1 
ATOM   538  C  CA  . GLY A 1 69  ? 0.35138  31.17540 6.53594   1.000 45.25403  ? 70  GLY A CA  1 
ATOM   539  C  C   . GLY A 1 69  ? 1.52174  32.10126 6.27853   1.000 46.25536  ? 70  GLY A C   1 
ATOM   540  O  O   . GLY A 1 69  ? 1.66879  32.63459 5.17451   1.000 36.04643  ? 70  GLY A O   1 
ATOM   541  N  N   . GLY A 1 70  ? 2.36342  32.30214 7.29497   1.000 35.47632  ? 71  GLY A N   1 
ATOM   542  C  CA  . GLY A 1 70  ? 3.50757  33.18207 7.13483   1.000 34.08504  ? 71  GLY A CA  1 
ATOM   543  C  C   . GLY A 1 70  ? 4.54344  32.64959 6.16704   1.000 33.56486  ? 71  GLY A C   1 
ATOM   544  O  O   . GLY A 1 70  ? 5.24203  33.42855 5.51279   1.000 34.60741  ? 71  GLY A O   1 
ATOM   545  N  N   . TYR A 1 71  ? 4.66293  31.32385 6.06118   1.000 36.76972  ? 72  TYR A N   1 
ATOM   546  C  CA  . TYR A 1 71  ? 5.60151  30.75007 5.10392   1.000 35.03787  ? 72  TYR A CA  1 
ATOM   547  C  C   . TYR A 1 71  ? 5.10364  30.90949 3.67382   1.000 38.14060  ? 72  TYR A C   1 
ATOM   548  O  O   . TYR A 1 71  ? 5.90829  31.10965 2.75661   1.000 32.21481  ? 72  TYR A O   1 
ATOM   549  C  CB  . TYR A 1 71  ? 5.84957  29.27622 5.42557   1.000 40.34572  ? 72  TYR A CB  1 
ATOM   550  C  CG  . TYR A 1 71  ? 6.99865  28.67095 4.65191   1.000 37.87852  ? 72  TYR A CG  1 
ATOM   551  C  CD1 . TYR A 1 71  ? 8.31451  28.98098 4.97198   1.000 34.60656  ? 72  TYR A CD1 1 
ATOM   552  C  CD2 . TYR A 1 71  ? 6.76979  27.78911 3.60453   1.000 43.53906  ? 72  TYR A CD2 1 
ATOM   553  C  CE1 . TYR A 1 71  ? 9.36978  28.43289 4.26880   1.000 42.32552  ? 72  TYR A CE1 1 
ATOM   554  C  CE2 . TYR A 1 71  ? 7.81950  27.23561 2.89573   1.000 38.44779  ? 72  TYR A CE2 1 
ATOM   555  C  CZ  . TYR A 1 71  ? 9.11722  27.56031 3.23251   1.000 41.50426  ? 72  TYR A CZ  1 
ATOM   556  O  OH  . TYR A 1 71  ? 10.16641 27.01215 2.53023   1.000 39.56769  ? 72  TYR A OH  1 
ATOM   557  N  N   . LYS A 1 72  ? 3.78852  30.82591 3.46300   1.000 37.78085  ? 73  LYS A N   1 
ATOM   558  C  CA  . LYS A 1 72  ? 3.24031  31.09558 2.13874   1.000 37.39739  ? 73  LYS A CA  1 
ATOM   559  C  C   . LYS A 1 72  ? 3.37591  32.57046 1.78227   1.000 39.60077  ? 73  LYS A C   1 
ATOM   560  O  O   . LYS A 1 72  ? 3.63699  32.91485 0.62356   1.000 37.91921  ? 73  LYS A O   1 
ATOM   561  C  CB  . LYS A 1 72  ? 1.77711  30.65705 2.07614   1.000 35.73556  ? 73  LYS A CB  1 
ATOM   562  C  CG  . LYS A 1 72  ? 1.10799  30.91711 0.73510   1.000 43.58164  ? 73  LYS A CG  1 
ATOM   563  C  CD  . LYS A 1 72  ? -0.33030 30.42537 0.72699   1.000 58.48961  ? 73  LYS A CD  1 
ATOM   564  C  CE  . LYS A 1 72  ? -0.99423 30.69187 -0.61526  1.000 67.82313  ? 73  LYS A CE  1 
ATOM   565  N  NZ  . LYS A 1 72  ? -2.39491 30.18699 -0.65648  1.000 70.07398  ? 73  LYS A NZ  1 
ATOM   566  N  N   . LEU A 1 73  ? 3.21243  33.45496 2.76889   1.000 35.58203  ? 74  LEU A N   1 
ATOM   567  C  CA  . LEU A 1 73  ? 3.33704  34.88534 2.51002   1.000 28.85337  ? 74  LEU A CA  1 
ATOM   568  C  C   . LEU A 1 73  ? 4.76658  35.25786 2.13708   1.000 31.14965  ? 74  LEU A C   1 
ATOM   569  O  O   . LEU A 1 73  ? 4.98635  36.02859 1.19556   1.000 34.24125  ? 74  LEU A O   1 
ATOM   570  C  CB  . LEU A 1 73  ? 2.87380  35.67972 3.73099   1.000 34.44249  ? 74  LEU A CB  1 
ATOM   571  C  CG  . LEU A 1 73  ? 2.89715  37.20364 3.59824   1.000 37.45263  ? 74  LEU A CG  1 
ATOM   572  C  CD1 . LEU A 1 73  ? 1.99232  37.65690 2.46304   1.000 43.41774  ? 74  LEU A CD1 1 
ATOM   573  C  CD2 . LEU A 1 73  ? 2.48924  37.86027 4.90612   1.000 47.34471  ? 74  LEU A CD2 1 
ATOM   574  N  N   . LEU A 1 74  ? 5.75227  34.72126 2.86255   1.000 34.16878  ? 75  LEU A N   1 
ATOM   575  C  CA  . LEU A 1 74  ? 7.14552  35.00661 2.53524   1.000 30.74838  ? 75  LEU A CA  1 
ATOM   576  C  C   . LEU A 1 74  ? 7.51869  34.46981 1.16065   1.000 32.02993  ? 75  LEU A C   1 
ATOM   577  O  O   . LEU A 1 74  ? 8.39174  35.03377 0.49165   1.000 31.01218  ? 75  LEU A O   1 
ATOM   578  C  CB  . LEU A 1 74  ? 8.07118  34.42487 3.60398   1.000 32.83265  ? 75  LEU A CB  1 
ATOM   579  C  CG  . LEU A 1 74  ? 8.02160  35.10026 4.97647   1.000 47.22879  ? 75  LEU A CG  1 
ATOM   580  C  CD1 . LEU A 1 74  ? 9.00917  34.45123 5.93312   1.000 37.70947  ? 75  LEU A CD1 1 
ATOM   581  C  CD2 . LEU A 1 74  ? 8.29562  36.59060 4.84827   1.000 35.74777  ? 75  LEU A CD2 1 
ATOM   582  N  N   . ASN A 1 75  ? 6.87373  33.38647 0.72228   1.000 31.45173  ? 76  ASN A N   1 
ATOM   583  C  CA  . ASN A 1 75  ? 7.10345  32.89363 -0.63129  1.000 31.39951  ? 76  ASN A CA  1 
ATOM   584  C  C   . ASN A 1 75  ? 6.61505  33.89574 -1.66921  1.000 37.46535  ? 76  ASN A C   1 
ATOM   585  O  O   . ASN A 1 75  ? 7.26023  34.08884 -2.70672  1.000 34.33368  ? 76  ASN A O   1 
ATOM   586  C  CB  . ASN A 1 75  ? 6.41462  31.54354 -0.82291  1.000 36.08741  ? 76  ASN A CB  1 
ATOM   587  C  CG  . ASN A 1 75  ? 6.55704  31.01342 -2.23570  1.000 42.46250  ? 76  ASN A CG  1 
ATOM   588  O  OD1 . ASN A 1 75  ? 5.70415  31.25319 -3.08978  1.000 39.36547  ? 76  ASN A OD1 1 
ATOM   589  N  ND2 . ASN A 1 75  ? 7.63992  30.28854 -2.48912  1.000 36.96656  ? 76  ASN A ND2 1 
ATOM   590  N  N   . SER A 1 76  ? 5.47752  34.54384 -1.40517  1.000 32.14384  ? 77  SER A N   1 
ATOM   591  C  CA  . SER A 1 76  ? 4.96874  35.55361 -2.32728  1.000 40.53527  ? 77  SER A CA  1 
ATOM   592  C  C   . SER A 1 76  ? 5.86609  36.78462 -2.34651  1.000 36.21284  ? 77  SER A C   1 
ATOM   593  O  O   . SER A 1 76  ? 6.11153  37.36292 -3.41155  1.000 33.31910  ? 77  SER A O   1 
ATOM   594  C  CB  . SER A 1 76  ? 3.53747  35.93605 -1.94995  1.000 33.52742  ? 77  SER A CB  1 
ATOM   595  O  OG  . SER A 1 76  ? 3.01999  36.91042 -2.83990  1.000 60.08868  ? 77  SER A OG  1 
ATOM   596  N  N   . TRP A 1 77  ? 6.36296  37.20231 -1.17889  1.000 31.46755  ? 78  TRP A N   1 
ATOM   597  C  CA  . TRP A 1 77  ? 7.29377  38.32577 -1.13544  1.000 36.72376  ? 78  TRP A CA  1 
ATOM   598  C  C   . TRP A 1 77  ? 8.62626  37.96021 -1.77632  1.000 33.13798  ? 78  TRP A C   1 
ATOM   599  O  O   . TRP A 1 77  ? 9.24160  38.78860 -2.45738  1.000 34.63000  ? 78  TRP A O   1 
ATOM   600  C  CB  . TRP A 1 77  ? 7.50848  38.78373 0.30676   1.000 30.19035  ? 78  TRP A CB  1 
ATOM   601  C  CG  . TRP A 1 77  ? 6.29716  39.38021 0.95720   1.000 42.41539  ? 78  TRP A CG  1 
ATOM   602  C  CD1 . TRP A 1 77  ? 5.04665  39.49749 0.42179   1.000 37.15551  ? 78  TRP A CD1 1 
ATOM   603  C  CD2 . TRP A 1 77  ? 6.22567  39.94557 2.27103   1.000 35.81931  ? 78  TRP A CD2 1 
ATOM   604  N  NE1 . TRP A 1 77  ? 4.20106  40.09909 1.32297   1.000 33.23448  ? 78  TRP A NE1 1 
ATOM   605  C  CE2 . TRP A 1 77  ? 4.90105  40.38434 2.46592   1.000 34.54412  ? 78  TRP A CE2 1 
ATOM   606  C  CE3 . TRP A 1 77  ? 7.15407  40.12261 3.30208   1.000 27.65511  ? 78  TRP A CE3 1 
ATOM   607  C  CZ2 . TRP A 1 77  ? 4.48161  40.98761 3.64971   1.000 27.28846  ? 78  TRP A CZ2 1 
ATOM   608  C  CZ3 . TRP A 1 77  ? 6.73574  40.72263 4.47602   1.000 31.29731  ? 78  TRP A CZ3 1 
ATOM   609  C  CH2 . TRP A 1 77  ? 5.41176  41.14805 4.63970   1.000 33.92217  ? 78  TRP A CH2 1 
ATOM   610  N  N   . LEU A 1 78  ? 9.09111  36.72708 -1.55876  1.000 30.49687  ? 79  LEU A N   1 
ATOM   611  C  CA  . LEU A 1 78  ? 10.32710 36.27384 -2.18888  1.000 32.07815  ? 79  LEU A CA  1 
ATOM   612  C  C   . LEU A 1 78  ? 10.19488 36.25472 -3.70536  1.000 31.39458  ? 79  LEU A C   1 
ATOM   613  O  O   . LEU A 1 78  ? 11.11983 36.65281 -4.42336  1.000 35.11651  ? 79  LEU A O   1 
ATOM   614  C  CB  . LEU A 1 78  ? 10.69877 34.88555 -1.66685  1.000 29.78965  ? 79  LEU A CB  1 
ATOM   615  C  CG  . LEU A 1 78  ? 11.86316 34.15578 -2.33944  1.000 35.60569  ? 79  LEU A CG  1 
ATOM   616  C  CD1 . LEU A 1 78  ? 13.17930 34.85335 -2.04730  1.000 33.84807  ? 79  LEU A CD1 1 
ATOM   617  C  CD2 . LEU A 1 78  ? 11.91023 32.70464 -1.88892  1.000 34.20306  ? 79  LEU A CD2 1 
ATOM   618  N  N   . THR A 1 79  ? 9.04767  35.79540 -4.20969  1.000 39.17765  ? 80  THR A N   1 
ATOM   619  C  CA  . THR A 1 79  ? 8.83389  35.75380 -5.65195  1.000 33.60061  ? 80  THR A CA  1 
ATOM   620  C  C   . THR A 1 79  ? 8.82299  37.15513 -6.24988  1.000 35.85555  ? 80  THR A C   1 
ATOM   621  O  O   . THR A 1 79  ? 9.44347  37.39867 -7.29132  1.000 35.66472  ? 80  THR A O   1 
ATOM   622  C  CB  . THR A 1 79  ? 7.52622  35.02603 -5.96452  1.000 47.00033  ? 80  THR A CB  1 
ATOM   623  O  OG1 . THR A 1 79  ? 7.59258  33.68443 -5.46446  1.000 36.70442  ? 80  THR A OG1 1 
ATOM   624  C  CG2 . THR A 1 79  ? 7.28039  34.99111 -7.46429  1.000 51.19895  ? 80  THR A CG2 1 
ATOM   625  N  N   . TYR A 1 80  ? 8.12864  38.09261 -5.60094  1.000 33.93438  ? 81  TYR A N   1 
ATOM   626  C  CA  . TYR A 1 80  ? 8.06371  39.45436 -6.12075  1.000 31.72062  ? 81  TYR A CA  1 
ATOM   627  C  C   . TYR A 1 80  ? 9.42057  40.14282 -6.04475  1.000 36.42242  ? 81  TYR A C   1 
ATOM   628  O  O   . TYR A 1 80  ? 9.80565  40.87123 -6.96685  1.000 34.44333  ? 81  TYR A O   1 
ATOM   629  C  CB  . TYR A 1 80  ? 7.00879  40.25697 -5.35860  1.000 34.63565  ? 81  TYR A CB  1 
ATOM   630  C  CG  . TYR A 1 80  ? 6.97665  41.72262 -5.72741  1.000 41.56424  ? 81  TYR A CG  1 
ATOM   631  C  CD1 . TYR A 1 80  ? 6.39478  42.14758 -6.91533  1.000 36.08649  ? 81  TYR A CD1 1 
ATOM   632  C  CD2 . TYR A 1 80  ? 7.52670  42.68214 -4.88714  1.000 38.67881  ? 81  TYR A CD2 1 
ATOM   633  C  CE1 . TYR A 1 80  ? 6.36462  43.48664 -7.25698  1.000 42.13426  ? 81  TYR A CE1 1 
ATOM   634  C  CE2 . TYR A 1 80  ? 7.50082  44.02289 -5.21992  1.000 46.54352  ? 81  TYR A CE2 1 
ATOM   635  C  CZ  . TYR A 1 80  ? 6.91885  44.41951 -6.40525  1.000 46.86530  ? 81  TYR A CZ  1 
ATOM   636  O  OH  . TYR A 1 80  ? 6.89174  45.75419 -6.73862  1.000 45.12302  ? 81  TYR A OH  1 
ATOM   637  N  N   . SER A 1 81  ? 10.15970 39.92589 -4.95485  1.000 36.77012  ? 82  SER A N   1 
ATOM   638  C  CA  . SER A 1 81  ? 11.46863 40.55516 -4.81771  1.000 37.80535  ? 82  SER A CA  1 
ATOM   639  C  C   . SER A 1 81  ? 12.47506 39.97973 -5.80546  1.000 41.15050  ? 82  SER A C   1 
ATOM   640  O  O   . SER A 1 81  ? 13.39016 40.68857 -6.23999  1.000 34.00891  ? 82  SER A O   1 
ATOM   641  C  CB  . SER A 1 81  ? 11.97676 40.39882 -3.38520  1.000 35.28562  ? 82  SER A CB  1 
ATOM   642  O  OG  . SER A 1 81  ? 11.07229 40.97834 -2.46149  1.000 42.48823  ? 82  SER A OG  1 
ATOM   643  N  N   . LYS A 1 82  ? 12.32268 38.70537 -6.17169  1.000 36.03349  ? 83  LYS A N   1 
ATOM   644  C  CA  . LYS A 1 82  ? 13.21761 38.10377 -7.15465  1.000 39.36812  ? 83  LYS A CA  1 
ATOM   645  C  C   . LYS A 1 82  ? 12.90597 38.60030 -8.56175  1.000 46.59830  ? 83  LYS A C   1 
ATOM   646  O  O   . LYS A 1 82  ? 13.81747 38.78849 -9.37619  1.000 38.96534  ? 83  LYS A O   1 
ATOM   647  C  CB  . LYS A 1 82  ? 13.11842 36.57959 -7.08166  1.000 53.25166  ? 83  LYS A CB  1 
ATOM   648  C  CG  . LYS A 1 82  ? 14.05051 35.83705 -8.02390  1.000 51.65658  ? 83  LYS A CG  1 
ATOM   649  C  CD  . LYS A 1 82  ? 14.03865 34.34207 -7.73602  1.000 66.63222  ? 83  LYS A CD  1 
ATOM   650  C  CE  . LYS A 1 82  ? 14.88778 33.57587 -8.73746  1.000 70.82558  ? 83  LYS A CE  1 
ATOM   651  N  NZ  . LYS A 1 82  ? 14.33269 33.66478 -10.11634 1.000 78.70879  ? 83  LYS A NZ  1 
ATOM   652  N  N   . THR A 1 83  ? 11.62478 38.82155 -8.86403  1.000 42.42861  ? 84  THR A N   1 
ATOM   653  C  CA  . THR A 1 83  ? 11.24614 39.32522 -10.18060 1.000 44.57216  ? 84  THR A CA  1 
ATOM   654  C  C   . THR A 1 83  ? 11.72287 40.75932 -10.37779 1.000 51.20296  ? 84  THR A C   1 
ATOM   655  O  O   . THR A 1 83  ? 12.29899 41.09624 -11.41881 1.000 42.63708  ? 84  THR A O   1 
ATOM   656  C  CB  . THR A 1 83  ? 9.72989  39.23371 -10.36038 1.000 44.24125  ? 84  THR A CB  1 
ATOM   657  O  OG1 . THR A 1 83  ? 9.32387  37.85912 -10.33324 1.000 59.66448  ? 84  THR A OG1 1 
ATOM   658  C  CG2 . THR A 1 83  ? 9.30916  39.85726 -11.68178 1.000 45.29013  ? 84  THR A CG2 1 
ATOM   659  N  N   . THR A 1 84  ? 11.49324 41.61813 -9.38586  1.000 46.09575  ? 85  THR A N   1 
ATOM   660  C  CA  . THR A 1 84  ? 11.89407 43.01705 -9.46467  1.000 45.87589  ? 85  THR A CA  1 
ATOM   661  C  C   . THR A 1 84  ? 13.35383 43.24293 -9.09145  1.000 51.04790  ? 85  THR A C   1 
ATOM   662  O  O   . THR A 1 84  ? 13.80365 44.39447 -9.10533  1.000 43.36487  ? 85  THR A O   1 
ATOM   663  C  CB  . THR A 1 84  ? 10.99844 43.87236 -8.56425  1.000 43.38936  ? 85  THR A CB  1 
ATOM   664  O  OG1 . THR A 1 84  ? 11.06371 43.38301 -7.21870  1.000 39.08366  ? 85  THR A OG1 1 
ATOM   665  C  CG2 . THR A 1 84  ? 9.55671  43.82310 -9.04773  1.000 43.30456  ? 85  THR A CG2 1 
ATOM   666  N  N   . ASN A 1 85  ? 14.09286 42.18238 -8.75851  1.000 48.76224  ? 86  ASN A N   1 
ATOM   667  C  CA  . ASN A 1 85  ? 15.51282 42.26252 -8.41091  1.000 43.07573  ? 86  ASN A CA  1 
ATOM   668  C  C   . ASN A 1 85  ? 15.74350 43.24664 -7.26037  1.000 43.64997  ? 86  ASN A C   1 
ATOM   669  O  O   . ASN A 1 85  ? 16.51413 44.20382 -7.36060  1.000 43.70911  ? 86  ASN A O   1 
ATOM   670  C  CB  . ASN A 1 85  ? 16.35616 42.62839 -9.63911  1.000 51.38771  ? 86  ASN A CB  1 
ATOM   671  C  CG  . ASN A 1 85  ? 17.84626 42.46762 -9.39428  1.000 73.02868  ? 86  ASN A CG  1 
ATOM   672  O  OD1 . ASN A 1 85  ? 18.56373 43.44743 -9.18950  1.000 78.57863  ? 86  ASN A OD1 1 
ATOM   673  N  ND2 . ASN A 1 85  ? 18.31737 41.22608 -9.40846  1.000 74.23791  ? 86  ASN A ND2 1 
ATOM   674  N  N   . ASN A 1 86  ? 15.05121 42.99076 -6.15246  1.000 42.56081  ? 87  ASN A N   1 
ATOM   675  C  CA  . ASN A 1 86  ? 15.15947 43.81374 -4.94837  1.000 36.19742  ? 87  ASN A CA  1 
ATOM   676  C  C   . ASN A 1 86  ? 16.13243 43.11397 -4.00411  1.000 41.95544  ? 87  ASN A C   1 
ATOM   677  O  O   . ASN A 1 86  ? 15.73532 42.33405 -3.13845  1.000 41.45572  ? 87  ASN A O   1 
ATOM   678  C  CB  . ASN A 1 86  ? 13.79116 44.02598 -4.30905  1.000 36.20123  ? 87  ASN A CB  1 
ATOM   679  C  CG  . ASN A 1 86  ? 13.78751 45.15611 -3.29572  1.000 42.58947  ? 87  ASN A CG  1 
ATOM   680  O  OD1 . ASN A 1 86  ? 14.77101 45.37876 -2.59023  1.000 33.15578  ? 87  ASN A OD1 1 
ATOM   681  N  ND2 . ASN A 1 86  ? 12.67600 45.88042 -3.22321  1.000 29.36936  ? 87  ASN A ND2 1 
ATOM   682  N  N   . ILE A 1 87  ? 17.42418 43.40631 -4.17829  1.000 36.62261  ? 88  ILE A N   1 
ATOM   683  C  CA  . ILE A 1 87  ? 18.45390 42.74358 -3.37230  1.000 37.88674  ? 88  ILE A CA  1 
ATOM   684  C  C   . ILE A 1 87  ? 18.29505 43.02585 -1.88126  1.000 35.69371  ? 88  ILE A C   1 
ATOM   685  O  O   . ILE A 1 87  ? 18.36645 42.07141 -1.08664  1.000 43.12127  ? 88  ILE A O   1 
ATOM   686  C  CB  . ILE A 1 87  ? 19.85141 43.11046 -3.89661  1.000 35.04416  ? 88  ILE A CB  1 
ATOM   687  C  CG1 . ILE A 1 87  ? 20.00160 42.69301 -5.36117  1.000 45.95476  ? 88  ILE A CG1 1 
ATOM   688  C  CG2 . ILE A 1 87  ? 20.93158 42.46198 -3.04396  1.000 40.06748  ? 88  ILE A CG2 1 
ATOM   689  C  CD1 . ILE A 1 87  ? 19.86662 41.20374 -5.58864  1.000 57.75343  ? 88  ILE A CD1 1 
ATOM   690  N  N   . PRO A 1 88  ? 18.09535 44.27189 -1.42684  1.000 38.93454  ? 89  PRO A N   1 
ATOM   691  C  CA  . PRO A 1 88  ? 17.96445 44.48812 0.02590   1.000 33.89557  ? 89  PRO A CA  1 
ATOM   692  C  C   . PRO A 1 88  ? 16.80817 43.72933 0.65517   1.000 36.95192  ? 89  PRO A C   1 
ATOM   693  O  O   . PRO A 1 88  ? 16.95572 43.19699 1.76231   1.000 34.05475  ? 89  PRO A O   1 
ATOM   694  C  CB  . PRO A 1 88  ? 17.77593 46.00715 0.13605   1.000 31.43799  ? 89  PRO A CB  1 
ATOM   695  C  CG  . PRO A 1 88  ? 18.40170 46.54997 -1.08768  1.000 35.32763  ? 89  PRO A CG  1 
ATOM   696  C  CD  . PRO A 1 88  ? 18.10832 45.55294 -2.15845  1.000 34.42685  ? 89  PRO A CD  1 
ATOM   697  N  N   . LEU A 1 89  ? 15.65723 43.65849 -0.01598  1.000 34.32254  ? 90  LEU A N   1 
ATOM   698  C  CA  . LEU A 1 89  ? 14.53907 42.91486 0.55289   1.000 36.87590  ? 90  LEU A CA  1 
ATOM   699  C  C   . LEU A 1 89  ? 14.75542 41.41050 0.43864   1.000 34.92646  ? 90  LEU A C   1 
ATOM   700  O  O   . LEU A 1 89  ? 14.35184 40.65694 1.33120   1.000 32.51258  ? 90  LEU A O   1 
ATOM   701  C  CB  . LEU A 1 89  ? 13.22808 43.32115 -0.11759  1.000 38.46571  ? 90  LEU A CB  1 
ATOM   702  C  CG  . LEU A 1 89  ? 11.97927 42.92659 0.67480   1.000 33.17750  ? 90  LEU A CG  1 
ATOM   703  C  CD1 . LEU A 1 89  ? 12.00360 43.56801 2.05337   1.000 36.19594  ? 90  LEU A CD1 1 
ATOM   704  C  CD2 . LEU A 1 89  ? 10.71162 43.30658 -0.07045  1.000 37.38294  ? 90  LEU A CD2 1 
ATOM   705  N  N   . LEU A 1 90  ? 15.38840 40.95510 -0.64696  1.000 34.46120  ? 91  LEU A N   1 
ATOM   706  C  CA  . LEU A 1 90  ? 15.74685 39.54318 -0.74955  1.000 39.13703  ? 91  LEU A CA  1 
ATOM   707  C  C   . LEU A 1 90  ? 16.66419 39.12831 0.39269   1.000 31.04850  ? 91  LEU A C   1 
ATOM   708  O  O   . LEU A 1 90  ? 16.50367 38.04504 0.96759   1.000 33.20342  ? 91  LEU A O   1 
ATOM   709  C  CB  . LEU A 1 90  ? 16.41528 39.26093 -2.09528  1.000 37.09455  ? 91  LEU A CB  1 
ATOM   710  C  CG  . LEU A 1 90  ? 15.52717 39.17096 -3.33667  1.000 29.85824  ? 91  LEU A CG  1 
ATOM   711  C  CD1 . LEU A 1 90  ? 16.38000 39.15203 -4.59647  1.000 38.99197  ? 91  LEU A CD1 1 
ATOM   712  C  CD2 . LEU A 1 90  ? 14.64275 37.93925 -3.27492  1.000 32.99785  ? 91  LEU A CD2 1 
ATOM   713  N  N   . GLN A 1 91  ? 17.63200 39.98146 0.73478   1.000 37.31878  ? 92  GLN A N   1 
ATOM   714  C  CA  . GLN A 1 91  ? 18.52457 39.69359 1.85260   1.000 28.97982  ? 92  GLN A CA  1 
ATOM   715  C  C   . GLN A 1 91  ? 17.74447 39.58139 3.15664   1.000 38.69531  ? 92  GLN A C   1 
ATOM   716  O  O   . GLN A 1 91  ? 17.93293 38.63505 3.92969   1.000 33.42753  ? 92  GLN A O   1 
ATOM   717  C  CB  . GLN A 1 91  ? 19.59429 40.78314 1.95343   1.000 34.78445  ? 92  GLN A CB  1 
ATOM   718  C  CG  . GLN A 1 91  ? 20.64509 40.54665 3.02871   1.000 42.22526  ? 92  GLN A CG  1 
ATOM   719  C  CD  . GLN A 1 91  ? 21.71146 39.55853 2.59756   1.000 50.84656  ? 92  GLN A CD  1 
ATOM   720  O  OE1 . GLN A 1 91  ? 21.76362 39.15080 1.43732   1.000 48.27165  ? 92  GLN A OE1 1 
ATOM   721  N  NE2 . GLN A 1 91  ? 22.57165 39.16992 3.53280   1.000 40.55351  ? 92  GLN A NE2 1 
ATOM   722  N  N   . GLN A 1 92  ? 16.84980 40.53924 3.41086   1.000 37.12422  ? 93  GLN A N   1 
ATOM   723  C  CA  . GLN A 1 92  ? 16.08228 40.52845 4.65095   1.000 35.98462  ? 93  GLN A CA  1 
ATOM   724  C  C   . GLN A 1 92  ? 15.10516 39.35995 4.69948   1.000 31.91829  ? 93  GLN A C   1 
ATOM   725  O  O   . GLN A 1 92  ? 14.83752 38.82269 5.78061   1.000 34.16063  ? 93  GLN A O   1 
ATOM   726  C  CB  . GLN A 1 92  ? 15.34197 41.85649 4.81382   1.000 28.84749  ? 93  GLN A CB  1 
ATOM   727  C  CG  . GLN A 1 92  ? 14.76732 42.08824 6.20136   1.000 35.63882  ? 93  GLN A CG  1 
ATOM   728  C  CD  . GLN A 1 92  ? 14.08734 43.43760 6.32709   1.000 41.64896  ? 93  GLN A CD  1 
ATOM   729  O  OE1 . GLN A 1 92  ? 13.80385 44.09690 5.32676   1.000 33.56624  ? 93  GLN A OE1 1 
ATOM   730  N  NE2 . GLN A 1 92  ? 13.82520 43.85770 7.56021   1.000 30.24905  ? 93  GLN A NE2 1 
ATOM   731  N  N   . ILE A 1 93  ? 14.56917 38.94966 3.54813   1.000 30.13634  ? 94  ILE A N   1 
ATOM   732  C  CA  . ILE A 1 93  ? 13.65113 37.81511 3.52248   1.000 34.65775  ? 94  ILE A CA  1 
ATOM   733  C  C   . ILE A 1 93  ? 14.39022 36.52035 3.83783   1.000 35.94774  ? 94  ILE A C   1 
ATOM   734  O  O   . ILE A 1 93  ? 13.91063 35.69306 4.62295   1.000 36.04046  ? 94  ILE A O   1 
ATOM   735  C  CB  . ILE A 1 93  ? 12.92652 37.74337 2.16542   1.000 30.18250  ? 94  ILE A CB  1 
ATOM   736  C  CG1 . ILE A 1 93  ? 11.88312 38.85831 2.05865   1.000 32.45474  ? 94  ILE A CG1 1 
ATOM   737  C  CG2 . ILE A 1 93  ? 12.27424 36.38269 1.97384   1.000 28.64578  ? 94  ILE A CG2 1 
ATOM   738  C  CD1 . ILE A 1 93  ? 11.23545 38.96135 0.69120   1.000 30.57045  ? 94  ILE A CD1 1 
ATOM   739  N  N   . LEU A 1 94  ? 15.56988 36.32379 3.24021   1.000 32.48885  ? 95  LEU A N   1 
ATOM   740  C  CA  . LEU A 1 94  ? 16.33764 35.11323 3.51580   1.000 33.85407  ? 95  LEU A CA  1 
ATOM   741  C  C   . LEU A 1 94  ? 16.83982 35.08065 4.95330   1.000 32.60159  ? 95  LEU A C   1 
ATOM   742  O  O   . LEU A 1 94  ? 16.92290 34.00272 5.55243   1.000 31.24717  ? 95  LEU A O   1 
ATOM   743  C  CB  . LEU A 1 94  ? 17.51121 34.98902 2.54312   1.000 29.47759  ? 95  LEU A CB  1 
ATOM   744  C  CG  . LEU A 1 94  ? 17.18778 34.80439 1.05883   1.000 47.82663  ? 95  LEU A CG  1 
ATOM   745  C  CD1 . LEU A 1 94  ? 18.40255 34.27302 0.31349   1.000 45.13547  ? 95  LEU A CD1 1 
ATOM   746  C  CD2 . LEU A 1 94  ? 15.99347 33.88805 0.86658   1.000 46.94996  ? 95  LEU A CD2 1 
ATOM   747  N  N   . LEU A 1 95  ? 17.18495 36.24061 5.51953   1.000 29.05261  ? 96  LEU A N   1 
ATOM   748  C  CA  . LEU A 1 95  ? 17.53167 36.28940 6.93599   1.000 35.30207  ? 96  LEU A CA  1 
ATOM   749  C  C   . LEU A 1 95  ? 16.35388 35.87714 7.80777   1.000 34.87008  ? 96  LEU A C   1 
ATOM   750  O  O   . LEU A 1 95  ? 16.54549 35.24793 8.85523   1.000 30.64224  ? 96  LEU A O   1 
ATOM   751  C  CB  . LEU A 1 95  ? 18.01002 37.69153 7.31733   1.000 36.15951  ? 96  LEU A CB  1 
ATOM   752  C  CG  . LEU A 1 95  ? 19.37935 38.12132 6.78618   1.000 45.68953  ? 96  LEU A CG  1 
ATOM   753  C  CD1 . LEU A 1 95  ? 19.67378 39.56869 7.15288   1.000 39.80064  ? 96  LEU A CD1 1 
ATOM   754  C  CD2 . LEU A 1 95  ? 20.46802 37.20121 7.31478   1.000 46.45783  ? 96  LEU A CD2 1 
ATOM   755  N  N   . THR A 1 96  ? 15.13170 36.21741 7.39186   1.000 28.42371  ? 97  THR A N   1 
ATOM   756  C  CA  . THR A 1 96  ? 13.95171 35.79359 8.13738   1.000 33.27602  ? 97  THR A CA  1 
ATOM   757  C  C   . THR A 1 96  ? 13.73723 34.28971 8.01673   1.000 28.74416  ? 97  THR A C   1 
ATOM   758  O  O   . THR A 1 96  ? 13.40206 33.62491 9.00359   1.000 33.90519  ? 97  THR A O   1 
ATOM   759  C  CB  . THR A 1 96  ? 12.71963 36.55591 7.64789   1.000 30.89699  ? 97  THR A CB  1 
ATOM   760  O  OG1 . THR A 1 96  ? 12.96269 37.96533 7.73537   1.000 32.78888  ? 97  THR A OG1 1 
ATOM   761  C  CG2 . THR A 1 96  ? 11.50550 36.20861 8.49313   1.000 30.63938  ? 97  THR A CG2 1 
ATOM   762  N  N   . LEU A 1 97  ? 13.93246 33.73664 6.81565   1.000 33.74823  ? 98  LEU A N   1 
ATOM   763  C  CA  . LEU A 1 97  ? 13.79010 32.29584 6.62562   1.000 32.10313  ? 98  LEU A CA  1 
ATOM   764  C  C   . LEU A 1 97  ? 14.79829 31.52478 7.46737   1.000 35.84213  ? 98  LEU A C   1 
ATOM   765  O  O   . LEU A 1 97  ? 14.46668 30.48561 8.05036   1.000 35.65366  ? 98  LEU A O   1 
ATOM   766  C  CB  . LEU A 1 97  ? 13.95087 31.94238 5.14716   1.000 30.29851  ? 98  LEU A CB  1 
ATOM   767  C  CG  . LEU A 1 97  ? 12.91582 32.52024 4.18134   1.000 36.49114  ? 98  LEU A CG  1 
ATOM   768  C  CD1 . LEU A 1 97  ? 13.27701 32.16447 2.75193   1.000 42.52958  ? 98  LEU A CD1 1 
ATOM   769  C  CD2 . LEU A 1 97  ? 11.52217 32.01817 4.52442   1.000 36.32451  ? 98  LEU A CD2 1 
ATOM   770  N  N   . GLN A 1 98  ? 16.03891 32.01420 7.53476   1.000 31.95929  ? 99  GLN A N   1 
ATOM   771  C  CA  . GLN A 1 98  ? 17.03870 31.38840 8.39328   1.000 38.85253  ? 99  GLN A CA  1 
ATOM   772  C  C   . GLN A 1 98  ? 16.67871 31.53650 9.86466   1.000 42.04451  ? 99  GLN A C   1 
ATOM   773  O  O   . GLN A 1 98  ? 17.03573 30.67933 10.68061  1.000 38.84872  ? 99  GLN A O   1 
ATOM   774  C  CB  . GLN A 1 98  ? 18.41468 31.99788 8.12307   1.000 37.74035  ? 99  GLN A CB  1 
ATOM   775  C  CG  . GLN A 1 98  ? 19.57367 31.26372 8.77726   1.000 38.14659  ? 99  GLN A CG  1 
ATOM   776  C  CD  . GLN A 1 98  ? 20.88597 32.00944 8.62706   1.000 44.64534  ? 99  GLN A CD  1 
ATOM   777  O  OE1 . GLN A 1 98  ? 20.93913 33.22984 8.78051   1.000 43.95756  ? 99  GLN A OE1 1 
ATOM   778  N  NE2 . GLN A 1 98  ? 21.95195 31.27911 8.32043   1.000 53.97465  ? 99  GLN A NE2 1 
ATOM   779  N  N   . HIS A 1 99  ? 15.97277 32.61086 10.21936  1.000 36.13404  ? 100 HIS A N   1 
ATOM   780  C  CA  . HIS A 1 99  ? 15.60653 32.83586 11.61183  1.000 28.73760  ? 100 HIS A CA  1 
ATOM   781  C  C   . HIS A 1 99  ? 14.44678 31.94367 12.03825  1.000 39.01633  ? 100 HIS A C   1 
ATOM   782  O  O   . HIS A 1 99  ? 14.33823 31.59077 13.21789  1.000 36.98245  ? 100 HIS A O   1 
ATOM   783  C  CB  . HIS A 1 99  ? 15.27253 34.31710 11.80508  1.000 35.90265  ? 100 HIS A CB  1 
ATOM   784  C  CG  . HIS A 1 99  ? 14.60580 34.63585 13.10638  1.000 29.06275  ? 100 HIS A CG  1 
ATOM   785  N  ND1 . HIS A 1 99  ? 15.25173 34.54219 14.31897  1.000 31.63082  ? 100 HIS A ND1 1 
ATOM   786  C  CD2 . HIS A 1 99  ? 13.35062 35.06241 13.38214  1.000 35.60611  ? 100 HIS A CD2 1 
ATOM   787  C  CE1 . HIS A 1 99  ? 14.42387 34.89255 15.28660  1.000 38.70433  ? 100 HIS A CE1 1 
ATOM   788  N  NE2 . HIS A 1 99  ? 13.26264 35.21202 14.74487  1.000 33.26029  ? 100 HIS A NE2 1 
ATOM   789  N  N   . LEU A 1 100 ? 13.59241 31.54936 11.09834  1.000 39.89218  ? 101 LEU A N   1 
ATOM   790  C  CA  . LEU A 1 100 ? 12.40894 30.76890 11.43447  1.000 38.97447  ? 101 LEU A CA  1 
ATOM   791  C  C   . LEU A 1 100 ? 12.76631 29.29105 11.59042  1.000 38.17651  ? 101 LEU A C   1 
ATOM   792  O  O   . LEU A 1 100 ? 13.59445 28.76829 10.84037  1.000 34.84436  ? 101 LEU A O   1 
ATOM   793  C  CB  . LEU A 1 100 ? 11.33760 30.93250 10.35728  1.000 35.05233  ? 101 LEU A CB  1 
ATOM   794  C  CG  . LEU A 1 100 ? 10.70959 32.32069 10.21217  1.000 40.70886  ? 101 LEU A CG  1 
ATOM   795  C  CD1 . LEU A 1 100 ? 9.76646  32.35096 9.02151   1.000 36.66574  ? 101 LEU A CD1 1 
ATOM   796  C  CD2 . LEU A 1 100 ? 9.98120  32.72946 11.48528  1.000 34.48127  ? 101 LEU A CD2 1 
ATOM   797  N  N   . PRO A 1 101 ? 12.16083 28.59828 12.55431  1.000 38.53574  ? 102 PRO A N   1 
ATOM   798  C  CA  . PRO A 1 101 ? 12.41573 27.15256 12.72817  1.000 39.56824  ? 102 PRO A CA  1 
ATOM   799  C  C   . PRO A 1 101 ? 11.63854 26.31223 11.72180  1.000 44.09554  ? 102 PRO A C   1 
ATOM   800  O  O   . PRO A 1 101 ? 10.63353 25.66022 12.02541  1.000 40.04147  ? 102 PRO A O   1 
ATOM   801  C  CB  . PRO A 1 101 ? 11.96879 26.91520 14.17304  1.000 43.61885  ? 102 PRO A CB  1 
ATOM   802  C  CG  . PRO A 1 101 ? 10.87357 27.91081 14.37907  1.000 52.39470  ? 102 PRO A CG  1 
ATOM   803  C  CD  . PRO A 1 101 ? 11.26976 29.13419 13.59646  1.000 42.64515  ? 102 PRO A CD  1 
ATOM   804  N  N   . LEU A 1 102 ? 12.11535 26.31769 10.48081  1.000 39.71932  ? 103 LEU A N   1 
ATOM   805  C  CA  . LEU A 1 102 ? 11.44852 25.59427 9.40815   1.000 35.60076  ? 103 LEU A CA  1 
ATOM   806  C  C   . LEU A 1 102 ? 11.74379 24.10348 9.50267   1.000 53.56709  ? 103 LEU A C   1 
ATOM   807  O  O   . LEU A 1 102 ? 12.88571 23.69374 9.73023   1.000 41.35797  ? 103 LEU A O   1 
ATOM   808  C  CB  . LEU A 1 102 ? 11.89247 26.12845 8.04692   1.000 36.94326  ? 103 LEU A CB  1 
ATOM   809  C  CG  . LEU A 1 102 ? 11.67658 27.62374 7.80226   1.000 36.12181  ? 103 LEU A CG  1 
ATOM   810  C  CD1 . LEU A 1 102 ? 12.25429 28.03809 6.45632   1.000 38.60079  ? 103 LEU A CD1 1 
ATOM   811  C  CD2 . LEU A 1 102 ? 10.19984 27.96817 7.88168   1.000 34.19383  ? 103 LEU A CD2 1 
ATOM   812  N  N   . THR A 1 103 ? 10.70421 23.29323 9.32386   1.000 38.64675  ? 104 THR A N   1 
ATOM   813  C  CA  . THR A 1 103 ? 10.82870 21.84615 9.31274   1.000 45.11750  ? 104 THR A CA  1 
ATOM   814  C  C   . THR A 1 103 ? 10.83076 21.34212 7.87148   1.000 50.42106  ? 104 THR A C   1 
ATOM   815  O  O   . THR A 1 103 ? 10.68822 22.10837 6.91572   1.000 37.23898  ? 104 THR A O   1 
ATOM   816  C  CB  . THR A 1 103 ? 9.69784  21.19993 10.11639  1.000 39.81197  ? 104 THR A CB  1 
ATOM   817  O  OG1 . THR A 1 103 ? 8.44507  21.44946 9.46610   1.000 42.08738  ? 104 THR A OG1 1 
ATOM   818  C  CG2 . THR A 1 103 ? 9.65290  21.76938 11.52726  1.000 41.31443  ? 104 THR A CG2 1 
ATOM   819  N  N   . VAL A 1 104 ? 10.99282 20.02631 7.71783   1.000 39.28053  ? 105 VAL A N   1 
ATOM   820  C  CA  . VAL A 1 104 ? 10.98327 19.43019 6.38560   1.000 47.25564  ? 105 VAL A CA  1 
ATOM   821  C  C   . VAL A 1 104 ? 9.60801  19.57555 5.74487   1.000 39.48681  ? 105 VAL A C   1 
ATOM   822  O  O   . VAL A 1 104 ? 9.49349  19.84254 4.54230   1.000 44.37982  ? 105 VAL A O   1 
ATOM   823  C  CB  . VAL A 1 104 ? 11.42763 17.95750 6.45801   1.000 44.04651  ? 105 VAL A CB  1 
ATOM   824  C  CG1 . VAL A 1 104 ? 11.38126 17.31581 5.08096   1.000 50.02810  ? 105 VAL A CG1 1 
ATOM   825  C  CG2 . VAL A 1 104 ? 12.82658 17.85706 7.04286   1.000 44.75249  ? 105 VAL A CG2 1 
ATOM   826  N  N   . ASP A 1 105 ? 8.54372  19.41243 6.53567   1.000 48.80268  ? 106 ASP A N   1 
ATOM   827  C  CA  . ASP A 1 105 ? 7.19489  19.57197 6.00183   1.000 53.39500  ? 106 ASP A CA  1 
ATOM   828  C  C   . ASP A 1 105 ? 6.94114  20.99896 5.53408   1.000 44.98699  ? 106 ASP A C   1 
ATOM   829  O  O   . ASP A 1 105 ? 6.20113  21.21223 4.56667   1.000 51.71451  ? 106 ASP A O   1 
ATOM   830  C  CB  . ASP A 1 105 ? 6.16193  19.16424 7.05238   1.000 56.82893  ? 106 ASP A CB  1 
ATOM   831  C  CG  . ASP A 1 105 ? 6.19921  17.68008 7.36072   1.000 74.46782  ? 106 ASP A CG  1 
ATOM   832  O  OD1 . ASP A 1 105 ? 6.45759  16.88488 6.43218   1.000 71.32626  ? 106 ASP A OD1 1 
ATOM   833  O  OD2 . ASP A 1 105 ? 5.97041  17.30871 8.53143   1.000 69.88685  ? 106 ASP A OD2 1 
ATOM   834  N  N   . HIS A 1 106 ? 7.54214  21.98581 6.20289   1.000 43.02671  ? 107 HIS A N   1 
ATOM   835  C  CA  . HIS A 1 106 ? 7.39987  23.36884 5.76059   1.000 38.49887  ? 107 HIS A CA  1 
ATOM   836  C  C   . HIS A 1 106 ? 8.09905  23.59423 4.42630   1.000 40.30108  ? 107 HIS A C   1 
ATOM   837  O  O   . HIS A 1 106 ? 7.54686  24.24472 3.53164   1.000 39.67765  ? 107 HIS A O   1 
ATOM   838  C  CB  . HIS A 1 106 ? 7.95413  24.31986 6.82170   1.000 35.50890  ? 107 HIS A CB  1 
ATOM   839  C  CG  . HIS A 1 106 ? 7.23646  24.24856 8.13373   1.000 40.01448  ? 107 HIS A CG  1 
ATOM   840  N  ND1 . HIS A 1 106 ? 7.85387  24.52331 9.33506   1.000 38.10273  ? 107 HIS A ND1 1 
ATOM   841  C  CD2 . HIS A 1 106 ? 5.95242  23.93990 8.43289   1.000 49.16235  ? 107 HIS A CD2 1 
ATOM   842  C  CE1 . HIS A 1 106 ? 6.98239  24.38295 10.31799  1.000 38.03585  ? 107 HIS A CE1 1 
ATOM   843  N  NE2 . HIS A 1 106 ? 5.82091  24.02996 9.79746   1.000 43.35010  ? 107 HIS A NE2 1 
ATOM   844  N  N   . LEU A 1 107 ? 9.31154  23.05610 4.27236   1.000 41.33053  ? 108 LEU A N   1 
ATOM   845  C  CA  . LEU A 1 107 ? 10.07836 23.25515 3.04859   1.000 47.13778  ? 108 LEU A CA  1 
ATOM   846  C  C   . LEU A 1 107 ? 9.42788  22.59995 1.83708   1.000 36.92670  ? 108 LEU A C   1 
ATOM   847  O  O   . LEU A 1 107 ? 9.72892  22.98935 0.70401   1.000 42.68492  ? 108 LEU A O   1 
ATOM   848  C  CB  . LEU A 1 107 ? 11.49987 22.71944 3.23131   1.000 47.16481  ? 108 LEU A CB  1 
ATOM   849  C  CG  . LEU A 1 107 ? 12.33333 23.36194 4.34342   1.000 36.92033  ? 108 LEU A CG  1 
ATOM   850  C  CD1 . LEU A 1 107 ? 13.67006 22.65235 4.49586   1.000 48.79453  ? 108 LEU A CD1 1 
ATOM   851  C  CD2 . LEU A 1 107 ? 12.54150 24.84317 4.07342   1.000 35.69408  ? 108 LEU A CD2 1 
ATOM   852  N  N   . LYS A 1 108 ? 8.54800  21.62339 2.04606   1.000 47.46571  ? 109 LYS A N   1 
ATOM   853  C  CA  . LYS A 1 108 ? 7.85985  20.94226 0.95723   1.000 36.67347  ? 109 LYS A CA  1 
ATOM   854  C  C   . LYS A 1 108 ? 6.57229  21.63756 0.53291   1.000 44.51167  ? 109 LYS A C   1 
ATOM   855  O  O   . LYS A 1 108 ? 5.90866  21.16213 -0.39383  1.000 45.18615  ? 109 LYS A O   1 
ATOM   856  C  CB  . LYS A 1 108 ? 7.54250  19.49718 1.35446   1.000 38.59242  ? 109 LYS A CB  1 
ATOM   857  C  CG  . LYS A 1 108 ? 8.75911  18.61274 1.55658   1.000 45.33245  ? 109 LYS A CG  1 
ATOM   858  C  CD  . LYS A 1 108 ? 8.34092  17.20801 1.96192   1.000 48.15204  ? 109 LYS A CD  1 
ATOM   859  C  CE  . LYS A 1 108 ? 9.54261  16.29066 2.11017   1.000 58.02135  ? 109 LYS A CE  1 
ATOM   860  N  NZ  . LYS A 1 108 ? 9.14953  14.93718 2.59031   1.000 55.18891  ? 109 LYS A NZ  1 
ATOM   861  N  N   . GLN A 1 109 ? 6.20461  22.74497 1.18167   1.000 35.60355  ? 110 GLN A N   1 
ATOM   862  C  CA  . GLN A 1 109 ? 4.93090  23.39522 0.88954   1.000 32.21564  ? 110 GLN A CA  1 
ATOM   863  C  C   . GLN A 1 109 ? 4.95787  24.14838 -0.43591  1.000 38.42198  ? 110 GLN A C   1 
ATOM   864  O  O   . GLN A 1 109 ? 3.98282  24.10157 -1.19406  1.000 45.67032  ? 110 GLN A O   1 
ATOM   865  C  CB  . GLN A 1 109 ? 4.55159  24.34395 2.02651   1.000 45.65290  ? 110 GLN A CB  1 
ATOM   866  C  CG  . GLN A 1 109 ? 4.29392  23.65003 3.35130   1.000 42.24464  ? 110 GLN A CG  1 
ATOM   867  C  CD  . GLN A 1 109 ? 3.86561  24.61444 4.44166   1.000 45.76809  ? 110 GLN A CD  1 
ATOM   868  O  OE1 . GLN A 1 109 ? 3.65173  25.80048 4.19038   1.000 52.75560  ? 110 GLN A OE1 1 
ATOM   869  N  NE2 . GLN A 1 109 ? 3.73900  24.10767 5.66197   1.000 49.83623  ? 110 GLN A NE2 1 
ATOM   870  N  N   . ASN A 1 110 ? 6.05011  24.84812 -0.73432  1.000 36.44212  ? 111 ASN A N   1 
ATOM   871  C  CA  . ASN A 1 110 ? 6.11958  25.68866 -1.92381  1.000 38.82268  ? 111 ASN A CA  1 
ATOM   872  C  C   . ASN A 1 110 ? 7.52391  25.58902 -2.51309  1.000 39.65354  ? 111 ASN A C   1 
ATOM   873  O  O   . ASN A 1 110 ? 8.31974  24.72302 -2.13557  1.000 39.10869  ? 111 ASN A O   1 
ATOM   874  C  CB  . ASN A 1 110 ? 5.72095  27.13153 -1.58243  1.000 41.06178  ? 111 ASN A CB  1 
ATOM   875  C  CG  . ASN A 1 110 ? 6.49271  27.68774 -0.40068  1.000 35.25049  ? 111 ASN A CG  1 
ATOM   876  O  OD1 . ASN A 1 110 ? 7.68264  27.42158 -0.23890  1.000 38.54754  ? 111 ASN A OD1 1 
ATOM   877  N  ND2 . ASN A 1 110 ? 5.81294  28.46247 0.43626   1.000 33.20105  ? 111 ASN A ND2 1 
ATOM   878  N  N   . ASN A 1 111 ? 7.83097  26.49142 -3.44681  1.000 34.39153  ? 112 ASN A N   1 
ATOM   879  C  CA  . ASN A 1 111 ? 9.10038  26.48648 -4.16079  1.000 34.56724  ? 112 ASN A CA  1 
ATOM   880  C  C   . ASN A 1 111 ? 10.11812 27.45099 -3.56128  1.000 32.13915  ? 112 ASN A C   1 
ATOM   881  O  O   . ASN A 1 111 ? 11.05466 27.85956 -4.25609  1.000 41.11799  ? 112 ASN A O   1 
ATOM   882  C  CB  . ASN A 1 111 ? 8.87528  26.81301 -5.63874  1.000 35.14505  ? 112 ASN A CB  1 
ATOM   883  C  CG  . ASN A 1 111 ? 8.38018  28.23164 -5.85609  1.000 49.18327  ? 112 ASN A CG  1 
ATOM   884  O  OD1 . ASN A 1 111 ? 7.78773  28.83872 -4.96420  1.000 48.57109  ? 112 ASN A OD1 1 
ATOM   885  N  ND2 . ASN A 1 111 ? 8.61939  28.76617 -7.04917  1.000 37.87166  ? 112 ASN A ND2 1 
ATOM   886  N  N   . THR A 1 112 ? 9.95538  27.82258 -2.28906  1.000 39.55650  ? 113 THR A N   1 
ATOM   887  C  CA  . THR A 1 112 ? 10.90735 28.73013 -1.65384  1.000 39.10080  ? 113 THR A CA  1 
ATOM   888  C  C   . THR A 1 112 ? 12.30369 28.12207 -1.61802  1.000 40.76240  ? 113 THR A C   1 
ATOM   889  O  O   . THR A 1 112 ? 13.29465 28.79349 -1.93015  1.000 38.19321  ? 113 THR A O   1 
ATOM   890  C  CB  . THR A 1 112 ? 10.43825 29.08244 -0.24148  1.000 39.56748  ? 113 THR A CB  1 
ATOM   891  O  OG1 . THR A 1 112 ? 9.25826  29.89221 -0.31526  1.000 40.48978  ? 113 THR A OG1 1 
ATOM   892  C  CG2 . THR A 1 112 ? 11.52007 29.83735 0.51304   1.000 32.28876  ? 113 THR A CG2 1 
ATOM   893  N  N   . ALA A 1 113 ? 12.39946 26.84350 -1.24311  1.000 38.35363  ? 114 ALA A N   1 
ATOM   894  C  CA  . ALA A 1 113 ? 13.69724 26.17696 -1.21261  1.000 36.58261  ? 114 ALA A CA  1 
ATOM   895  C  C   . ALA A 1 113 ? 14.32699 26.13682 -2.59848  1.000 32.42643  ? 114 ALA A C   1 
ATOM   896  O  O   . ALA A 1 113 ? 15.54877 26.26610 -2.73801  1.000 38.44080  ? 114 ALA A O   1 
ATOM   897  C  CB  . ALA A 1 113 ? 13.54907 24.76497 -0.64568  1.000 34.29640  ? 114 ALA A CB  1 
ATOM   898  N  N   . LYS A 1 114 ? 13.50641 25.96190 -3.63670  1.000 41.53342  ? 115 LYS A N   1 
ATOM   899  C  CA  . LYS A 1 114 ? 14.02307 25.97557 -5.00082  1.000 41.09938  ? 115 LYS A CA  1 
ATOM   900  C  C   . LYS A 1 114 ? 14.56472 27.35021 -5.37253  1.000 42.20866  ? 115 LYS A C   1 
ATOM   901  O  O   . LYS A 1 114 ? 15.64630 27.45775 -5.96197  1.000 43.53420  ? 115 LYS A O   1 
ATOM   902  C  CB  . LYS A 1 114 ? 12.92876 25.54555 -5.97749  1.000 42.44536  ? 115 LYS A CB  1 
ATOM   903  C  CG  . LYS A 1 114 ? 13.33553 25.62007 -7.44101  1.000 64.38165  ? 115 LYS A CG  1 
ATOM   904  C  CD  . LYS A 1 114 ? 12.18426 25.22693 -8.35091  1.000 49.40965  ? 115 LYS A CD  1 
ATOM   905  C  CE  . LYS A 1 114 ? 12.56704 25.35641 -9.81609  1.000 71.34006  ? 115 LYS A CE  1 
ATOM   906  N  NZ  . LYS A 1 114 ? 11.43456 25.00642 -10.71764 1.000 68.29135  ? 115 LYS A NZ  1 
ATOM   907  N  N   . LEU A 1 115 ? 13.83055 28.41305 -5.03278  1.000 45.28299  ? 116 LEU A N   1 
ATOM   908  C  CA  . LEU A 1 115 ? 14.28604 29.75973 -5.36324  1.000 38.29731  ? 116 LEU A CA  1 
ATOM   909  C  C   . LEU A 1 115 ? 15.54181 30.12777 -4.58181  1.000 44.30252  ? 116 LEU A C   1 
ATOM   910  O  O   . LEU A 1 115 ? 16.42494 30.81659 -5.10586  1.000 43.56413  ? 116 LEU A O   1 
ATOM   911  C  CB  . LEU A 1 115 ? 13.17064 30.77133 -5.09959  1.000 33.93975  ? 116 LEU A CB  1 
ATOM   912  C  CG  . LEU A 1 115 ? 11.86932 30.57158 -5.88071  1.000 38.53596  ? 116 LEU A CG  1 
ATOM   913  C  CD1 . LEU A 1 115 ? 10.86301 31.66022 -5.54025  1.000 44.40689  ? 116 LEU A CD1 1 
ATOM   914  C  CD2 . LEU A 1 115 ? 12.13642 30.53138 -7.37784  1.000 47.44148  ? 116 LEU A CD2 1 
ATOM   915  N  N   . VAL A 1 116 ? 15.64057 29.67920 -3.32826  1.000 39.30843  ? 117 VAL A N   1 
ATOM   916  C  CA  . VAL A 1 116 ? 16.83975 29.94616 -2.53976  1.000 39.88303  ? 117 VAL A CA  1 
ATOM   917  C  C   . VAL A 1 116 ? 18.02981 29.17882 -3.10316  1.000 51.48398  ? 117 VAL A C   1 
ATOM   918  O  O   . VAL A 1 116 ? 19.15464 29.69288 -3.14529  1.000 48.22244  ? 117 VAL A O   1 
ATOM   919  C  CB  . VAL A 1 116 ? 16.59122 29.60652 -1.05850  1.000 43.90556  ? 117 VAL A CB  1 
ATOM   920  C  CG1 . VAL A 1 116 ? 17.88485 29.69851 -0.26271  1.000 35.03954  ? 117 VAL A CG1 1 
ATOM   921  C  CG2 . VAL A 1 116 ? 15.54009 30.53607 -0.47329  1.000 35.06986  ? 117 VAL A CG2 1 
ATOM   922  N  N   . LYS A 1 117 ? 17.80227 27.94142 -3.55086  1.000 45.20849  ? 118 LYS A N   1 
ATOM   923  C  CA  . LYS A 1 117 ? 18.88125 27.16069 -4.14783  1.000 48.20206  ? 118 LYS A CA  1 
ATOM   924  C  C   . LYS A 1 117 ? 19.39715 27.82039 -5.42070  1.000 47.73740  ? 118 LYS A C   1 
ATOM   925  O  O   . LYS A 1 117 ? 20.60527 27.81723 -5.68544  1.000 49.71958  ? 118 LYS A O   1 
ATOM   926  C  CB  . LYS A 1 117 ? 18.40035 25.73793 -4.43400  1.000 49.13764  ? 118 LYS A CB  1 
ATOM   927  C  CG  . LYS A 1 117 ? 19.47655 24.80508 -4.97012  1.000 62.99266  ? 118 LYS A CG  1 
ATOM   928  C  CD  . LYS A 1 117 ? 18.90493 23.42760 -5.27023  1.000 55.44734  ? 118 LYS A CD  1 
ATOM   929  C  CE  . LYS A 1 117 ? 19.97176 22.48051 -5.79504  1.000 60.52972  ? 118 LYS A CE  1 
ATOM   930  N  NZ  . LYS A 1 117 ? 21.05465 22.25304 -4.79953  1.000 73.85270  ? 118 LYS A NZ  1 
ATOM   931  N  N   . GLN A 1 118 ? 18.49532 28.39689 -6.21935  1.000 43.37569  ? 119 GLN A N   1 
ATOM   932  C  CA  . GLN A 1 118 ? 18.91822 29.09812 -7.42751  1.000 54.14558  ? 119 GLN A CA  1 
ATOM   933  C  C   . GLN A 1 118 ? 19.71137 30.35412 -7.08879  1.000 61.93608  ? 119 GLN A C   1 
ATOM   934  O  O   . GLN A 1 118 ? 20.66298 30.70338 -7.79723  1.000 55.81182  ? 119 GLN A O   1 
ATOM   935  C  CB  . GLN A 1 118 ? 17.70245 29.44710 -8.28559  1.000 48.66718  ? 119 GLN A CB  1 
ATOM   936  C  CG  . GLN A 1 118 ? 16.95329 28.23937 -8.82287  1.000 66.26779  ? 119 GLN A CG  1 
ATOM   937  C  CD  . GLN A 1 118 ? 15.69778 28.62272 -9.58103  1.000 81.70490  ? 119 GLN A CD  1 
ATOM   938  O  OE1 . GLN A 1 118 ? 15.33458 29.79719 -9.65060  1.000 79.69462  ? 119 GLN A OE1 1 
ATOM   939  N  NE2 . GLN A 1 118 ? 15.02668 27.63037 -10.15447 1.000 78.12090  ? 119 GLN A NE2 1 
ATOM   940  N  N   . LEU A 1 119 ? 19.33344 31.04801 -6.01144  1.000 52.17758  ? 120 LEU A N   1 
ATOM   941  C  CA  . LEU A 1 119 ? 20.07420 32.23663 -5.60266  1.000 47.55879  ? 120 LEU A CA  1 
ATOM   942  C  C   . LEU A 1 119 ? 21.48104 31.88909 -5.13425  1.000 44.47527  ? 120 LEU A C   1 
ATOM   943  O  O   . LEU A 1 119 ? 22.40891 32.68222 -5.32417  1.000 48.92461  ? 120 LEU A O   1 
ATOM   944  C  CB  . LEU A 1 119 ? 19.31698 32.97911 -4.50100  1.000 49.51987  ? 120 LEU A CB  1 
ATOM   945  C  CG  . LEU A 1 119 ? 18.04291 33.71932 -4.91231  1.000 49.69514  ? 120 LEU A CG  1 
ATOM   946  C  CD1 . LEU A 1 119 ? 17.36299 34.33036 -3.69677  1.000 47.60002  ? 120 LEU A CD1 1 
ATOM   947  C  CD2 . LEU A 1 119 ? 18.35691 34.78972 -5.94684  1.000 46.82579  ? 120 LEU A CD2 1 
ATOM   948  N  N   . SER A 1 120 ? 21.66346 30.71363 -4.53068  1.000 52.66027  ? 121 SER A N   1 
ATOM   949  C  CA  . SER A 1 120 ? 22.98371 30.30767 -4.06578  1.000 59.61623  ? 121 SER A CA  1 
ATOM   950  C  C   . SER A 1 120 ? 23.94301 29.99724 -5.20654  1.000 69.23199  ? 121 SER A C   1 
ATOM   951  O  O   . SER A 1 120 ? 25.14094 29.82874 -4.95380  1.000 63.52690  ? 121 SER A O   1 
ATOM   952  C  CB  . SER A 1 120 ? 22.86587 29.08803 -3.14991  1.000 43.87264  ? 121 SER A CB  1 
ATOM   953  O  OG  . SER A 1 120 ? 22.34002 27.97381 -3.85099  1.000 51.03551  ? 121 SER A OG  1 
ATOM   954  N  N   . LYS A 1 121 ? 23.45624 29.92408 -6.44188  1.000 64.30253  ? 122 LYS A N   1 
ATOM   955  C  CA  . LYS A 1 121 ? 24.27908 29.55601 -7.58743  1.000 73.98542  ? 122 LYS A CA  1 
ATOM   956  C  C   . LYS A 1 121 ? 24.43268 30.66697 -8.61279  1.000 65.01304  ? 122 LYS A C   1 
ATOM   957  O  O   . LYS A 1 121 ? 25.50228 30.79548 -9.21357  1.000 77.70089  ? 122 LYS A O   1 
ATOM   958  C  CB  . LYS A 1 121 ? 23.69392 28.31530 -8.27970  1.000 61.47172  ? 122 LYS A CB  1 
ATOM   959  C  CG  . LYS A 1 121 ? 23.59209 27.08637 -7.39126  1.000 61.11617  ? 122 LYS A CG  1 
ATOM   960  C  CD  . LYS A 1 121 ? 22.97905 25.91752 -8.14806  1.000 61.12520  ? 122 LYS A CD  1 
ATOM   961  C  CE  . LYS A 1 121 ? 22.87115 24.68078 -7.27138  1.000 60.33897  ? 122 LYS A CE  1 
ATOM   962  N  NZ  . LYS A 1 121 ? 22.26560 23.53533 -8.00713  1.000 76.06530  ? 122 LYS A NZ  1 
ATOM   963  N  N   . SER A 1 122 ? 23.39746 31.47870 -8.83332  1.000 58.77015  ? 123 SER A N   1 
ATOM   964  C  CA  . SER A 1 122 ? 23.39482 32.43209 -9.93397  1.000 64.28922  ? 123 SER A CA  1 
ATOM   965  C  C   . SER A 1 122 ? 23.22465 33.88438 -9.50883  1.000 64.41907  ? 123 SER A C   1 
ATOM   966  O  O   . SER A 1 122 ? 23.18399 34.76141 -10.37976 1.000 69.27895  ? 123 SER A O   1 
ATOM   967  C  CB  . SER A 1 122 ? 22.29180 32.07173 -10.93924 1.000 65.84170  ? 123 SER A CB  1 
ATOM   968  O  OG  . SER A 1 122 ? 21.01307 32.11855 -10.33090 1.000 68.80513  ? 123 SER A OG  1 
ATOM   969  N  N   . SER A 1 123 ? 23.12282 34.17254 -8.21382  1.000 71.02348  ? 124 SER A N   1 
ATOM   970  C  CA  . SER A 1 123 ? 22.96767 35.55454 -7.77804  1.000 64.37058  ? 124 SER A CA  1 
ATOM   971  C  C   . SER A 1 123 ? 24.28457 36.30529 -7.92847  1.000 68.05248  ? 124 SER A C   1 
ATOM   972  O  O   . SER A 1 123 ? 25.33817 35.82779 -7.49639  1.000 65.04120  ? 124 SER A O   1 
ATOM   973  C  CB  . SER A 1 123 ? 22.48949 35.61187 -6.32876  1.000 55.10874  ? 124 SER A CB  1 
ATOM   974  O  OG  . SER A 1 123 ? 22.35128 36.95269 -5.89281  1.000 52.43240  ? 124 SER A OG  1 
ATOM   975  N  N   . GLU A 1 124 ? 24.22224 37.48505 -8.54273  1.000 65.99456  ? 125 GLU A N   1 
ATOM   976  C  CA  . GLU A 1 124 ? 25.41017 38.29844 -8.76431  1.000 63.35483  ? 125 GLU A CA  1 
ATOM   977  C  C   . GLU A 1 124 ? 25.78320 39.14917 -7.55759  1.000 60.72434  ? 125 GLU A C   1 
ATOM   978  O  O   . GLU A 1 124 ? 26.81138 39.83359 -7.59850  1.000 59.85101  ? 125 GLU A O   1 
ATOM   979  C  CB  . GLU A 1 124 ? 25.21090 39.19382 -9.99028  1.000 71.37726  ? 125 GLU A CB  1 
ATOM   980  C  CG  . GLU A 1 124 ? 24.87986 38.42940 -11.26460 1.000 88.80472  ? 125 GLU A CG  1 
ATOM   981  C  CD  . GLU A 1 124 ? 25.96785 37.44680 -11.66151 1.000 99.38071  ? 125 GLU A CD  1 
ATOM   982  O  OE1 . GLU A 1 124 ? 27.15694 37.73154 -11.40334 1.000 92.88096  ? 125 GLU A OE1 1 
ATOM   983  O  OE2 . GLU A 1 124 ? 25.63230 36.38587 -12.22978 1.000 96.76774  ? 125 GLU A OE2 1 
ATOM   984  N  N   . ASP A 1 125 ? 24.98211 39.12875 -6.49549  1.000 62.06733  ? 126 ASP A N   1 
ATOM   985  C  CA  . ASP A 1 125 ? 25.31095 39.83220 -5.26387  1.000 44.78966  ? 126 ASP A CA  1 
ATOM   986  C  C   . ASP A 1 125 ? 26.08529 38.89673 -4.34487  1.000 54.48846  ? 126 ASP A C   1 
ATOM   987  O  O   . ASP A 1 125 ? 25.64010 37.77738 -4.07188  1.000 63.25231  ? 126 ASP A O   1 
ATOM   988  C  CB  . ASP A 1 125 ? 24.04531 40.33719 -4.56992  1.000 53.27030  ? 126 ASP A CB  1 
ATOM   989  C  CG  . ASP A 1 125 ? 24.34866 41.16412 -3.33486  1.000 53.30810  ? 126 ASP A CG  1 
ATOM   990  O  OD1 . ASP A 1 125 ? 24.81733 42.31207 -3.48586  1.000 59.45616  ? 126 ASP A OD1 1 
ATOM   991  O  OD2 . ASP A 1 125 ? 24.12130 40.66592 -2.21245  1.000 57.88668  ? 126 ASP A OD2 1 
ATOM   992  N  N   . GLU A 1 126 ? 27.24475 39.35978 -3.87125  1.000 57.96698  ? 127 GLU A N   1 
ATOM   993  C  CA  . GLU A 1 126 ? 28.11850 38.49755 -3.08057  1.000 61.85342  ? 127 GLU A CA  1 
ATOM   994  C  C   . GLU A 1 126 ? 27.47811 38.11821 -1.75053  1.000 55.44878  ? 127 GLU A C   1 
ATOM   995  O  O   . GLU A 1 126 ? 27.54662 36.95642 -1.33239  1.000 48.83378  ? 127 GLU A O   1 
ATOM   996  C  CB  . GLU A 1 126 ? 29.46467 39.18405 -2.84994  1.000 59.88904  ? 127 GLU A CB  1 
ATOM   997  C  CG  . GLU A 1 126 ? 30.47126 38.33188 -2.09247  1.000 87.36619  ? 127 GLU A CG  1 
ATOM   998  C  CD  . GLU A 1 126 ? 31.77179 39.06336 -1.82255  1.000 86.68033  ? 127 GLU A CD  1 
ATOM   999  O  OE1 . GLU A 1 126 ? 31.83558 40.28337 -2.08314  1.000 89.39537  ? 127 GLU A OE1 1 
ATOM   1000 O  OE2 . GLU A 1 126 ? 32.73080 38.41737 -1.34987  1.000 89.59723  ? 127 GLU A OE2 1 
ATOM   1001 N  N   . GLU A 1 127 ? 26.85186 39.08063 -1.07003  1.000 47.06907  ? 128 GLU A N   1 
ATOM   1002 C  CA  . GLU A 1 127 ? 26.25609 38.78499 0.22825   1.000 50.37460  ? 128 GLU A CA  1 
ATOM   1003 C  C   . GLU A 1 127 ? 24.98510 37.95662 0.09286   1.000 43.58029  ? 128 GLU A C   1 
ATOM   1004 O  O   . GLU A 1 127 ? 24.70610 37.11219 0.95161   1.000 54.79879  ? 128 GLU A O   1 
ATOM   1005 C  CB  . GLU A 1 127 ? 25.97294 40.08138 0.98705   1.000 46.83709  ? 128 GLU A CB  1 
ATOM   1006 C  CG  . GLU A 1 127 ? 27.22676 40.82805 1.41160   1.000 51.33879  ? 128 GLU A CG  1 
ATOM   1007 C  CD  . GLU A 1 127 ? 28.12015 39.99923 2.31644   1.000 81.80130  ? 128 GLU A CD  1 
ATOM   1008 O  OE1 . GLU A 1 127 ? 27.58664 39.27911 3.18747   1.000 68.97434  ? 128 GLU A OE1 1 
ATOM   1009 O  OE2 . GLU A 1 127 ? 29.35691 40.06257 2.15166   1.000 81.51400  ? 128 GLU A OE2 1 
ATOM   1010 N  N   . LEU A 1 128 ? 24.20647 38.17596 -0.96894  1.000 42.26899  ? 129 LEU A N   1 
ATOM   1011 C  CA  . LEU A 1 128 ? 22.99291 37.38810 -1.16035  1.000 43.46083  ? 129 LEU A CA  1 
ATOM   1012 C  C   . LEU A 1 128 ? 23.32404 35.95656 -1.56328  1.000 48.05465  ? 129 LEU A C   1 
ATOM   1013 O  O   . LEU A 1 128 ? 22.66112 35.01182 -1.11940  1.000 44.92419  ? 129 LEU A O   1 
ATOM   1014 C  CB  . LEU A 1 128 ? 22.09391 38.04855 -2.20528  1.000 47.11964  ? 129 LEU A CB  1 
ATOM   1015 C  CG  . LEU A 1 128 ? 20.72950 37.39124 -2.42630  1.000 52.90774  ? 129 LEU A CG  1 
ATOM   1016 C  CD1 . LEU A 1 128 ? 19.93141 37.36685 -1.13198  1.000 40.87564  ? 129 LEU A CD1 1 
ATOM   1017 C  CD2 . LEU A 1 128 ? 19.95656 38.10771 -3.52159  1.000 48.36039  ? 129 LEU A CD2 1 
ATOM   1018 N  N   . ARG A 1 129 ? 24.34552 35.77637 -2.40415  1.000 46.59832  ? 130 ARG A N   1 
ATOM   1019 C  CA  . ARG A 1 129 ? 24.76652 34.43020 -2.77885  1.000 45.05323  ? 130 ARG A CA  1 
ATOM   1020 C  C   . ARG A 1 129 ? 25.32099 33.67194 -1.57883  1.000 49.26861  ? 130 ARG A C   1 
ATOM   1021 O  O   . ARG A 1 129 ? 25.05121 32.47628 -1.41344  1.000 49.25860  ? 130 ARG A O   1 
ATOM   1022 C  CB  . ARG A 1 129 ? 25.80632 34.49907 -3.89766  1.000 51.14212  ? 130 ARG A CB  1 
ATOM   1023 C  CG  . ARG A 1 129 ? 26.40353 33.15335 -4.28019  1.000 60.72410  ? 130 ARG A CG  1 
ATOM   1024 C  CD  . ARG A 1 129 ? 27.63511 33.32424 -5.15797  1.000 80.29618  ? 130 ARG A CD  1 
ATOM   1025 N  NE  . ARG A 1 129 ? 27.30763 33.84780 -6.47876  1.000 73.34909  ? 130 ARG A NE  1 
ATOM   1026 C  CZ  . ARG A 1 129 ? 27.17835 33.10262 -7.56805  1.000 86.74999  ? 130 ARG A CZ  1 
ATOM   1027 N  NH1 . ARG A 1 129 ? 27.34773 31.79089 -7.53237  1.000 85.50935  ? 130 ARG A NH1 1 
ATOM   1028 N  NH2 . ARG A 1 129 ? 26.87491 33.68845 -8.72290  1.000 91.43952  ? 130 ARG A NH2 1 
ATOM   1029 N  N   . LYS A 1 130 ? 26.09503 34.35133 -0.72878  1.000 49.34707  ? 131 LYS A N   1 
ATOM   1030 C  CA  . LYS A 1 130 ? 26.65708 33.69402 0.44661   1.000 51.29363  ? 131 LYS A CA  1 
ATOM   1031 C  C   . LYS A 1 130 ? 25.57127 33.33825 1.45439   1.000 58.42973  ? 131 LYS A C   1 
ATOM   1032 O  O   . LYS A 1 130 ? 25.59199 32.24751 2.03699   1.000 43.69817  ? 131 LYS A O   1 
ATOM   1033 C  CB  . LYS A 1 130 ? 27.71692 34.58756 1.09034   1.000 44.40323  ? 131 LYS A CB  1 
ATOM   1034 C  CG  . LYS A 1 130 ? 28.40970 33.96493 2.29230   1.000 52.22375  ? 131 LYS A CG  1 
ATOM   1035 C  CD  . LYS A 1 130 ? 29.51748 34.86399 2.81946   1.000 55.49489  ? 131 LYS A CD  1 
ATOM   1036 C  CE  . LYS A 1 130 ? 28.97593 36.21919 3.24542   1.000 76.45919  ? 131 LYS A CE  1 
ATOM   1037 N  NZ  . LYS A 1 130 ? 30.04979 37.10580 3.77373   1.000 81.73845  ? 131 LYS A NZ  1 
ATOM   1038 N  N   . LEU A 1 131 ? 24.61553 34.24513 1.67425   1.000 41.36696  ? 132 LEU A N   1 
ATOM   1039 C  CA  . LEU A 1 131 ? 23.52535 33.95729 2.60107   1.000 44.88559  ? 132 LEU A CA  1 
ATOM   1040 C  C   . LEU A 1 131 ? 22.66506 32.80589 2.09825   1.000 36.55089  ? 132 LEU A C   1 
ATOM   1041 O  O   . LEU A 1 131 ? 22.24236 31.94760 2.88207   1.000 38.58383  ? 132 LEU A O   1 
ATOM   1042 C  CB  . LEU A 1 131 ? 22.67356 35.20769 2.81710   1.000 44.70565  ? 132 LEU A CB  1 
ATOM   1043 C  CG  . LEU A 1 131 ? 21.40468 35.02709 3.65324   1.000 39.18987  ? 132 LEU A CG  1 
ATOM   1044 C  CD1 . LEU A 1 131 ? 21.74277 34.51090 5.04415   1.000 58.49748  ? 132 LEU A CD1 1 
ATOM   1045 C  CD2 . LEU A 1 131 ? 20.63397 36.33335 3.73486   1.000 40.88718  ? 132 LEU A CD2 1 
ATOM   1046 N  N   . ALA A 1 132 ? 22.39510 32.77001 0.79186   1.000 40.20526  ? 133 ALA A N   1 
ATOM   1047 C  CA  . ALA A 1 132 ? 21.62290 31.66739 0.23049   1.000 50.79861  ? 133 ALA A CA  1 
ATOM   1048 C  C   . ALA A 1 132 ? 22.37650 30.34820 0.34923   1.000 54.62987  ? 133 ALA A C   1 
ATOM   1049 O  O   . ALA A 1 132 ? 21.76657 29.29946 0.58736   1.000 38.59852  ? 133 ALA A O   1 
ATOM   1050 C  CB  . ALA A 1 132 ? 21.27332 31.96063 -1.22806  1.000 37.89963  ? 133 ALA A CB  1 
ATOM   1051 N  N   . SER A 1 133 ? 23.70286 30.38017 0.19065   1.000 49.34914  ? 134 SER A N   1 
ATOM   1052 C  CA  . SER A 1 133 ? 24.49154 29.15749 0.31355   1.000 51.10033  ? 134 SER A CA  1 
ATOM   1053 C  C   . SER A 1 133 ? 24.44827 28.61306 1.73582   1.000 41.28995  ? 134 SER A C   1 
ATOM   1054 O  O   . SER A 1 133 ? 24.27811 27.40516 1.93915   1.000 46.35905  ? 134 SER A O   1 
ATOM   1055 C  CB  . SER A 1 133 ? 25.93473 29.41655 -0.11873  1.000 41.50239  ? 134 SER A CB  1 
ATOM   1056 O  OG  . SER A 1 133 ? 25.99054 29.88633 -1.45456  1.000 51.08970  ? 134 SER A OG  1 
ATOM   1057 N  N   . VAL A 1 134 ? 24.60013 29.48807 2.73283   1.000 47.22323  ? 135 VAL A N   1 
ATOM   1058 C  CA  . VAL A 1 134 ? 24.50287 29.04948 4.12097   1.000 39.34896  ? 135 VAL A CA  1 
ATOM   1059 C  C   . VAL A 1 134 ? 23.09432 28.56041 4.42983   1.000 41.45730  ? 135 VAL A C   1 
ATOM   1060 O  O   . VAL A 1 134 ? 22.91208 27.61863 5.21165   1.000 45.76947  ? 135 VAL A O   1 
ATOM   1061 C  CB  . VAL A 1 134 ? 24.93065 30.18585 5.06973   1.000 57.51566  ? 135 VAL A CB  1 
ATOM   1062 C  CG1 . VAL A 1 134 ? 24.82586 29.74354 6.52292   1.000 65.35443  ? 135 VAL A CG1 1 
ATOM   1063 C  CG2 . VAL A 1 134 ? 26.34762 30.63796 4.75095   1.000 56.93948  ? 135 VAL A CG2 1 
ATOM   1064 N  N   . LEU A 1 135 ? 22.07981 29.17208 3.81552   1.000 46.41938  ? 136 LEU A N   1 
ATOM   1065 C  CA  . LEU A 1 135 ? 20.70425 28.76259 4.07574   1.000 42.64312  ? 136 LEU A CA  1 
ATOM   1066 C  C   . LEU A 1 135 ? 20.41509 27.38612 3.48816   1.000 38.10232  ? 136 LEU A C   1 
ATOM   1067 O  O   . LEU A 1 135 ? 19.68569 26.58955 4.09025   1.000 42.84727  ? 136 LEU A O   1 
ATOM   1068 C  CB  . LEU A 1 135 ? 19.73676 29.80637 3.51806   1.000 41.51174  ? 136 LEU A CB  1 
ATOM   1069 C  CG  . LEU A 1 135 ? 18.25486 29.62107 3.84565   1.000 37.52888  ? 136 LEU A CG  1 
ATOM   1070 C  CD1 . LEU A 1 135 ? 18.05446 29.47159 5.34396   1.000 38.64945  ? 136 LEU A CD1 1 
ATOM   1071 C  CD2 . LEU A 1 135 ? 17.44334 30.79018 3.30912   1.000 40.55980  ? 136 LEU A CD2 1 
ATOM   1072 N  N   . VAL A 1 136 ? 20.98078 27.08546 2.31700   1.000 47.41735  ? 137 VAL A N   1 
ATOM   1073 C  CA  . VAL A 1 136 ? 20.76904 25.77615 1.70652   1.000 41.52777  ? 137 VAL A CA  1 
ATOM   1074 C  C   . VAL A 1 136 ? 21.47048 24.68911 2.51242   1.000 49.12086  ? 137 VAL A C   1 
ATOM   1075 O  O   . VAL A 1 136 ? 20.92768 23.59442 2.70736   1.000 45.78020  ? 137 VAL A O   1 
ATOM   1076 C  CB  . VAL A 1 136 ? 21.23604 25.79007 0.23898   1.000 54.08825  ? 137 VAL A CB  1 
ATOM   1077 C  CG1 . VAL A 1 136 ? 21.24724 24.38134 -0.33423  1.000 52.62025  ? 137 VAL A CG1 1 
ATOM   1078 C  CG2 . VAL A 1 136 ? 20.33687 26.69094 -0.59153  1.000 39.71223  ? 137 VAL A CG2 1 
ATOM   1079 N  N   . SER A 1 137 ? 22.68116 24.97268 3.00061   1.000 52.80453  ? 138 SER A N   1 
ATOM   1080 C  CA  . SER A 1 137 ? 23.40810 23.98440 3.79185   1.000 56.37892  ? 138 SER A CA  1 
ATOM   1081 C  C   . SER A 1 137 ? 22.69379 23.69444 5.10631   1.000 55.45660  ? 138 SER A C   1 
ATOM   1082 O  O   . SER A 1 137 ? 22.69984 22.55340 5.58290   1.000 58.81889  ? 138 SER A O   1 
ATOM   1083 C  CB  . SER A 1 137 ? 24.83622 24.46359 4.05001   1.000 43.65122  ? 138 SER A CB  1 
ATOM   1084 O  OG  . SER A 1 137 ? 24.84275 25.65608 4.81414   1.000 71.06290  ? 138 SER A OG  1 
ATOM   1085 N  N   . ASP A 1 138 ? 22.07516 24.71379 5.70821   1.000 55.43272  ? 139 ASP A N   1 
ATOM   1086 C  CA  . ASP A 1 138 ? 21.29077 24.48750 6.91776   1.000 50.01530  ? 139 ASP A CA  1 
ATOM   1087 C  C   . ASP A 1 138 ? 20.08325 23.60414 6.63199   1.000 44.67421  ? 139 ASP A C   1 
ATOM   1088 O  O   . ASP A 1 138 ? 19.77033 22.69950 7.41437   1.000 52.67442  ? 139 ASP A O   1 
ATOM   1089 C  CB  . ASP A 1 138 ? 20.84824 25.82212 7.51865   1.000 63.24767  ? 139 ASP A CB  1 
ATOM   1090 C  CG  . ASP A 1 138 ? 22.00846 26.62852 8.07056   1.000 79.97936  ? 139 ASP A CG  1 
ATOM   1091 O  OD1 . ASP A 1 138 ? 23.14815 26.11642 8.06489   1.000 73.99266  ? 139 ASP A OD1 1 
ATOM   1092 O  OD2 . ASP A 1 138 ? 21.77976 27.77584 8.51033   1.000 80.64943  ? 139 ASP A OD2 1 
ATOM   1093 N  N   . TRP A 1 139 ? 19.39485 23.84880 5.51363   1.000 46.66046  ? 140 TRP A N   1 
ATOM   1094 C  CA  . TRP A 1 139 ? 18.24699 23.02241 5.15613   1.000 42.65315  ? 140 TRP A CA  1 
ATOM   1095 C  C   . TRP A 1 139 ? 18.66887 21.61496 4.75533   1.000 51.98019  ? 140 TRP A C   1 
ATOM   1096 O  O   . TRP A 1 139 ? 17.90583 20.66267 4.95283   1.000 43.90250  ? 140 TRP A O   1 
ATOM   1097 C  CB  . TRP A 1 139 ? 17.45379 23.68441 4.03023   1.000 45.21633  ? 140 TRP A CB  1 
ATOM   1098 C  CG  . TRP A 1 139 ? 16.72160 24.91604 4.46626   1.000 51.45962  ? 140 TRP A CG  1 
ATOM   1099 C  CD1 . TRP A 1 139 ? 16.44839 25.29545 5.74851   1.000 38.96043  ? 140 TRP A CD1 1 
ATOM   1100 C  CD2 . TRP A 1 139 ? 16.17474 25.93561 3.62086   1.000 40.18164  ? 140 TRP A CD2 1 
ATOM   1101 N  NE1 . TRP A 1 139 ? 15.76116 26.48558 5.75408   1.000 38.52958  ? 140 TRP A NE1 1 
ATOM   1102 C  CE2 . TRP A 1 139 ? 15.58114 26.89978 4.46032   1.000 44.71453  ? 140 TRP A CE2 1 
ATOM   1103 C  CE3 . TRP A 1 139 ? 16.12784 26.12595 2.23639   1.000 34.72803  ? 140 TRP A CE3 1 
ATOM   1104 C  CZ2 . TRP A 1 139 ? 14.94885 28.03664 3.96096   1.000 42.32737  ? 140 TRP A CZ2 1 
ATOM   1105 C  CZ3 . TRP A 1 139 ? 15.49944 27.25570 1.74292   1.000 46.36321  ? 140 TRP A CZ3 1 
ATOM   1106 C  CH2 . TRP A 1 139 ? 14.91869 28.19598 2.60261   1.000 45.30355  ? 140 TRP A CH2 1 
ATOM   1107 N  N   . MET A 1 140 ? 19.86928 21.46203 4.19086   1.000 54.93553  ? 141 MET A N   1 
ATOM   1108 C  CA  . MET A 1 140 ? 20.37797 20.12597 3.89736   1.000 54.29179  ? 141 MET A CA  1 
ATOM   1109 C  C   . MET A 1 140 ? 20.59153 19.32799 5.17750   1.000 53.58720  ? 141 MET A C   1 
ATOM   1110 O  O   . MET A 1 140 ? 20.37613 18.11063 5.20346   1.000 49.18655  ? 141 MET A O   1 
ATOM   1111 C  CB  . MET A 1 140 ? 21.67936 20.21978 3.10070   1.000 55.19212  ? 141 MET A CB  1 
ATOM   1112 C  CG  . MET A 1 140 ? 21.49735 20.57489 1.63294   1.000 54.67500  ? 141 MET A CG  1 
ATOM   1113 S  SD  . MET A 1 140 ? 20.64274 19.28712 0.70300   1.000 68.79603  ? 141 MET A SD  1 
ATOM   1114 C  CE  . MET A 1 140 ? 20.83898 19.89142 -0.97132  1.000 76.30550  ? 141 MET A CE  1 
ATOM   1115 N  N   . ALA A 1 141 ? 21.01350 19.99860 6.25264   1.000 56.32972  ? 142 ALA A N   1 
ATOM   1116 C  CA  . ALA A 1 141 ? 21.20039 19.31207 7.52579   1.000 47.45738  ? 142 ALA A CA  1 
ATOM   1117 C  C   . ALA A 1 141 ? 19.86910 18.94599 8.16845   1.000 56.17829  ? 142 ALA A C   1 
ATOM   1118 O  O   . ALA A 1 141 ? 19.77765 17.92587 8.86100   1.000 55.59486  ? 142 ALA A O   1 
ATOM   1119 C  CB  . ALA A 1 141 ? 22.02816 20.17902 8.47410   1.000 65.23257  ? 142 ALA A CB  1 
ATOM   1120 N  N   . VAL A 1 142 ? 18.83299 19.76080 7.95577   1.000 70.79579  ? 143 VAL A N   1 
ATOM   1121 C  CA  . VAL A 1 142 ? 17.51618 19.44792 8.50247   1.000 47.19783  ? 143 VAL A CA  1 
ATOM   1122 C  C   . VAL A 1 142 ? 16.94869 18.19699 7.84329   1.000 51.50052  ? 143 VAL A C   1 
ATOM   1123 O  O   . VAL A 1 142 ? 16.36257 17.33688 8.51221   1.000 62.99059  ? 143 VAL A O   1 
ATOM   1124 C  CB  . VAL A 1 142 ? 16.57266 20.65421 8.34244   1.000 50.50792  ? 143 VAL A CB  1 
ATOM   1125 C  CG1 . VAL A 1 142 ? 15.16733 20.29797 8.80097   1.000 55.13344  ? 143 VAL A CG1 1 
ATOM   1126 C  CG2 . VAL A 1 142 ? 17.10304 21.84912 9.12101   1.000 39.84549  ? 143 VAL A CG2 1 
ATOM   1127 N  N   . ILE A 1 143 ? 17.11472 18.07291 6.52476   1.000 59.14312  ? 144 ILE A N   1 
ATOM   1128 C  CA  . ILE A 1 143 ? 16.66653 16.87108 5.82827   1.000 60.80449  ? 144 ILE A CA  1 
ATOM   1129 C  C   . ILE A 1 143 ? 17.48234 15.66357 6.27268   1.000 61.44425  ? 144 ILE A C   1 
ATOM   1130 O  O   . ILE A 1 143 ? 16.95352 14.55402 6.41019   1.000 63.85281  ? 144 ILE A O   1 
ATOM   1131 C  CB  . ILE A 1 143 ? 16.74978 17.07835 4.30535   1.000 58.22444  ? 144 ILE A CB  1 
ATOM   1132 C  CG1 . ILE A 1 143 ? 15.97939 18.33258 3.89213   1.000 55.62186  ? 144 ILE A CG1 1 
ATOM   1133 C  CG2 . ILE A 1 143 ? 16.21579 15.85989 3.56809   1.000 49.78095  ? 144 ILE A CG2 1 
ATOM   1134 C  CD1 . ILE A 1 143 ? 16.22078 18.74122 2.45757   1.000 52.03215  ? 144 ILE A CD1 1 
ATOM   1135 N  N   A ARG A 1 144 ? 18.77965 15.86055 6.50709   0.546 64.56255  ? 145 ARG A N   1 
ATOM   1136 N  N   B ARG A 1 144 ? 18.78240 15.85709 6.50882   0.454 64.54968  ? 145 ARG A N   1 
ATOM   1137 C  CA  A ARG A 1 144 ? 19.65910 14.77922 6.92908   0.546 62.48452  ? 145 ARG A CA  1 
ATOM   1138 C  CA  B ARG A 1 144 ? 19.64844 14.76115 6.92795   0.454 62.49151  ? 145 ARG A CA  1 
ATOM   1139 C  C   A ARG A 1 144 ? 19.39187 14.32416 8.35786   0.546 64.71984  ? 145 ARG A C   1 
ATOM   1140 C  C   B ARG A 1 144 ? 19.41817 14.33929 8.37298   0.454 64.75035  ? 145 ARG A C   1 
ATOM   1141 O  O   A ARG A 1 144 ? 19.86888 13.25189 8.74548   0.546 74.96519  ? 145 ARG A O   1 
ATOM   1142 O  O   B ARG A 1 144 ? 19.95769 13.30916 8.79066   0.454 74.96500  ? 145 ARG A O   1 
ATOM   1143 C  CB  A ARG A 1 144 ? 21.11546 15.22237 6.78052   0.546 64.20190  ? 145 ARG A CB  1 
ATOM   1144 C  CB  B ARG A 1 144 ? 21.11716 15.14557 6.72841   0.454 64.22655  ? 145 ARG A CB  1 
ATOM   1145 C  CG  A ARG A 1 144 ? 22.06648 14.14192 6.29108   0.546 69.17584  ? 145 ARG A CG  1 
ATOM   1146 C  CG  B ARG A 1 144 ? 21.58712 15.04570 5.28424   0.454 69.00713  ? 145 ARG A CG  1 
ATOM   1147 C  CD  A ARG A 1 144 ? 23.11764 14.73465 5.36159   0.546 71.48326  ? 145 ARG A CD  1 
ATOM   1148 C  CD  B ARG A 1 144 ? 23.08819 15.27582 5.15276   0.454 71.81357  ? 145 ARG A CD  1 
ATOM   1149 N  NE  A ARG A 1 144 ? 22.59989 14.93585 4.01254   0.546 76.21917  ? 145 ARG A NE  1 
ATOM   1150 N  NE  B ARG A 1 144 ? 23.42094 16.67308 4.89933   0.454 57.94856  ? 145 ARG A NE  1 
ATOM   1151 C  CZ  A ARG A 1 144 ? 23.15529 15.72724 3.10471   0.546 50.77029  ? 145 ARG A CZ  1 
ATOM   1152 C  CZ  B ARG A 1 144 ? 23.87426 17.51743 5.81575   0.454 51.57010  ? 145 ARG A CZ  1 
ATOM   1153 N  NH1 A ARG A 1 144 ? 24.23155 16.44535 3.37911   0.546 51.54499  ? 145 ARG A NH1 1 
ATOM   1154 N  NH1 B ARG A 1 144 ? 24.06587 17.14026 7.06918   0.454 49.95523  ? 145 ARG A NH1 1 
ATOM   1155 N  NH2 A ARG A 1 144 ? 22.61352 15.80451 1.89261   0.546 51.05395  ? 145 ARG A NH2 1 
ATOM   1156 N  NH2 B ARG A 1 144 ? 24.14622 18.77118 5.46445   0.454 54.52489  ? 145 ARG A NH2 1 
ATOM   1157 N  N   . SER A 1 145 ? 18.63790 15.09732 9.13994   1.000 67.25266  ? 146 SER A N   1 
ATOM   1158 C  CA  . SER A 1 145 ? 18.34295 14.74372 10.52271  1.000 67.38767  ? 146 SER A CA  1 
ATOM   1159 C  C   . SER A 1 145 ? 17.27575 13.66484 10.64890  1.000 73.96588  ? 146 SER A C   1 
ATOM   1160 O  O   . SER A 1 145 ? 16.97185 13.25026 11.77247  1.000 94.71661  ? 146 SER A O   1 
ATOM   1161 C  CB  . SER A 1 145 ? 17.90509 15.98558 11.30406  1.000 65.80829  ? 146 SER A CB  1 
ATOM   1162 O  OG  . SER A 1 145 ? 18.93563 16.95681 11.34478  1.000 58.06022  ? 146 SER A OG  1 
ATOM   1163 N  N   . GLN A 1 146 ? 16.70239 13.20502 9.54121   1.000 86.67970  ? 147 GLN A N   1 
ATOM   1164 C  CA  . GLN A 1 146 ? 15.67317 12.17315 9.58532   1.000 84.87811  ? 147 GLN A CA  1 
ATOM   1165 C  C   . GLN A 1 146 ? 15.75866 11.25736 8.36796   1.000 83.88468  ? 147 GLN A C   1 
ATOM   1166 O  O   . GLN A 1 146 ? 16.78702 11.19896 7.69316   1.000 75.85247  ? 147 GLN A O   1 
ATOM   1167 C  CB  . GLN A 1 146 ? 14.28442 12.80807 9.67020   1.000 86.00761  ? 147 GLN A CB  1 
ATOM   1168 C  CG  . GLN A 1 146 ? 13.90081 13.62156 8.44561   1.000 80.24813  ? 147 GLN A CG  1 
ATOM   1169 C  CD  . GLN A 1 146 ? 12.59709 14.37083 8.63134   1.000 74.47826  ? 147 GLN A CD  1 
ATOM   1170 O  OE1 . GLN A 1 146 ? 12.30772 14.87556 9.71629   1.000 83.56761  ? 147 GLN A OE1 1 
ATOM   1171 N  NE2 . GLN A 1 146 ? 11.79902 14.44269 7.57208   1.000 85.83917  ? 147 GLN A NE2 1 
ATOM   1172 N  N   . GLY B 2 1   ? 8.98731  63.94074 3.00636   1.000 75.19836  ? 568 GLY B N   1 
ATOM   1173 C  CA  . GLY B 2 1   ? 8.98140  64.90411 1.92168   1.000 51.92788  ? 568 GLY B CA  1 
ATOM   1174 C  C   . GLY B 2 1   ? 9.38539  64.29808 0.59082   1.000 52.60698  ? 568 GLY B C   1 
ATOM   1175 O  O   . GLY B 2 1   ? 9.65572  63.09943 0.49875   1.000 56.32687  ? 568 GLY B O   1 
ATOM   1176 N  N   . HIS B 2 2   ? 9.43279  65.13415 -0.44668  1.000 42.50050  ? 569 HIS B N   1 
ATOM   1177 C  CA  . HIS B 2 2   ? 9.76390  64.68930 -1.79492  1.000 36.46335  ? 569 HIS B CA  1 
ATOM   1178 C  C   . HIS B 2 2   ? 11.00944 65.36798 -2.35212  1.000 34.60752  ? 569 HIS B C   1 
ATOM   1179 O  O   . HIS B 2 2   ? 11.35620 65.13807 -3.51705  1.000 43.98736  ? 569 HIS B O   1 
ATOM   1180 C  CB  . HIS B 2 2   ? 8.58228  64.92798 -2.74104  1.000 37.99080  ? 569 HIS B CB  1 
ATOM   1181 C  CG  . HIS B 2 2   ? 7.33611  64.19049 -2.35847  1.000 36.01327  ? 569 HIS B CG  1 
ATOM   1182 N  ND1 . HIS B 2 2   ? 7.26124  62.81395 -2.32762  1.000 40.42562  ? 569 HIS B ND1 1 
ATOM   1183 C  CD2 . HIS B 2 2   ? 6.10850  64.64107 -2.00842  1.000 38.31774  ? 569 HIS B CD2 1 
ATOM   1184 C  CE1 . HIS B 2 2   ? 6.04400  62.44904 -1.96603  1.000 40.60761  ? 569 HIS B CE1 1 
ATOM   1185 N  NE2 . HIS B 2 2   ? 5.32516  63.53897 -1.76673  1.000 42.48444  ? 569 HIS B NE2 1 
ATOM   1186 N  N   . MET B 2 3   ? 11.68528 66.20140 -1.55974  1.000 33.68233  ? 570 MET B N   1 
ATOM   1187 C  CA  . MET B 2 3   ? 12.89508 66.87779 -2.01196  1.000 35.68582  ? 570 MET B CA  1 
ATOM   1188 C  C   . MET B 2 3   ? 14.14828 66.02644 -1.85683  1.000 47.03743  ? 570 MET B C   1 
ATOM   1189 O  O   . MET B 2 3   ? 15.07096 66.14795 -2.67087  1.000 38.63165  ? 570 MET B O   1 
ATOM   1190 C  CB  . MET B 2 3   ? 13.07883 68.19787 -1.25599  1.000 41.48797  ? 570 MET B CB  1 
ATOM   1191 C  CG  . MET B 2 3   ? 11.97129 69.22383 -1.48265  1.000 52.12327  ? 570 MET B CG  1 
ATOM   1192 S  SD  . MET B 2 3   ? 11.82734 69.78911 -3.19348  1.000 51.60806  ? 570 MET B SD  1 
ATOM   1193 C  CE  . MET B 2 3   ? 10.42964 68.82593 -3.77214  1.000 40.48717  ? 570 MET B CE  1 
ATOM   1194 N  N   . ARG B 2 4   ? 14.20662 65.16674 -0.84148  1.000 35.47242  ? 571 ARG B N   1 
ATOM   1195 C  CA  . ARG B 2 4   ? 15.37365 64.32303 -0.63162  1.000 36.86845  ? 571 ARG B CA  1 
ATOM   1196 C  C   . ARG B 2 4   ? 14.94416 63.00227 -0.00927  1.000 44.99962  ? 571 ARG B C   1 
ATOM   1197 O  O   . ARG B 2 4   ? 13.84586 62.87736 0.54032   1.000 37.32344  ? 571 ARG B O   1 
ATOM   1198 C  CB  . ARG B 2 4   ? 16.41527 65.01514 0.25461   1.000 39.65278  ? 571 ARG B CB  1 
ATOM   1199 C  CG  . ARG B 2 4   ? 15.87484 65.49012 1.59002   1.000 48.22834  ? 571 ARG B CG  1 
ATOM   1200 C  CD  . ARG B 2 4   ? 16.96708 66.13801 2.42624   1.000 50.73201  ? 571 ARG B CD  1 
ATOM   1201 N  NE  . ARG B 2 4   ? 16.43976 66.70515 3.66093   1.000 53.80198  ? 571 ARG B NE  1 
ATOM   1202 C  CZ  . ARG B 2 4   ? 17.18660 67.24503 4.61388   1.000 69.17316  ? 571 ARG B CZ  1 
ATOM   1203 N  NH1 . ARG B 2 4   ? 18.50432 67.30071 4.51025   1.000 52.44726  ? 571 ARG B NH1 1 
ATOM   1204 N  NH2 . ARG B 2 4   ? 16.59691 67.73976 5.69868   1.000 71.45680  ? 571 ARG B NH2 1 
ATOM   1205 N  N   . CYS B 2 5   ? 15.83589 62.01554 -0.10248  1.000 36.98683  ? 572 CYS B N   1 
ATOM   1206 C  CA  . CYS B 2 5   ? 15.58307 60.70481 0.48238   1.000 39.53024  ? 572 CYS B CA  1 
ATOM   1207 C  C   . CYS B 2 5   ? 15.35591 60.83116 1.98320   1.000 38.79643  ? 572 CYS B C   1 
ATOM   1208 O  O   . CYS B 2 5   ? 16.14888 61.45564 2.69401   1.000 39.52455  ? 572 CYS B O   1 
ATOM   1209 C  CB  . CYS B 2 5   ? 16.75828 59.76880 0.19777   1.000 40.48329  ? 572 CYS B CB  1 
ATOM   1210 S  SG  . CYS B 2 5   ? 16.53512 58.07307 0.78570   1.000 34.97134  ? 572 CYS B SG  1 
ATOM   1211 N  N   . VAL B 2 6   ? 14.26616 60.22772 2.46550   1.000 41.67651  ? 573 VAL B N   1 
ATOM   1212 C  CA  . VAL B 2 6   ? 13.86099 60.39631 3.85707   1.000 38.71852  ? 573 VAL B CA  1 
ATOM   1213 C  C   . VAL B 2 6   ? 14.81630 59.73626 4.84070   1.000 38.81101  ? 573 VAL B C   1 
ATOM   1214 O  O   . VAL B 2 6   ? 14.73618 60.00944 6.04437   1.000 37.06381  ? 573 VAL B O   1 
ATOM   1215 C  CB  . VAL B 2 6   ? 12.42841 59.85806 4.06029   1.000 35.98499  ? 573 VAL B CB  1 
ATOM   1216 C  CG1 . VAL B 2 6   ? 12.43961 58.34923 4.22930   1.000 38.41369  ? 573 VAL B CG1 1 
ATOM   1217 C  CG2 . VAL B 2 6   ? 11.75398 60.54061 5.24550   1.000 46.67815  ? 573 VAL B CG2 1 
ATOM   1218 N  N   . ARG B 2 7   ? 15.72241 58.88273 4.36871   1.000 35.00609  ? 574 ARG B N   1 
ATOM   1219 C  CA  . ARG B 2 7   ? 16.69831 58.27003 5.26030   1.000 35.95264  ? 574 ARG B CA  1 
ATOM   1220 C  C   . ARG B 2 7   ? 17.66244 59.32710 5.78386   1.000 40.92850  ? 574 ARG B C   1 
ATOM   1221 O  O   . ARG B 2 7   ? 18.19923 60.12930 5.01319   1.000 38.61209  ? 574 ARG B O   1 
ATOM   1222 C  CB  . ARG B 2 7   ? 17.46807 57.16582 4.53794   1.000 27.32355  ? 574 ARG B CB  1 
ATOM   1223 C  CG  . ARG B 2 7   ? 18.37881 56.35675 5.45208   1.000 40.87481  ? 574 ARG B CG  1 
ATOM   1224 C  CD  . ARG B 2 7   ? 19.14885 55.29520 4.68336   1.000 48.18630  ? 574 ARG B CD  1 
ATOM   1225 N  NE  . ARG B 2 7   ? 20.21370 55.86625 3.86726   1.000 56.21885  ? 574 ARG B NE  1 
ATOM   1226 C  CZ  . ARG B 2 7   ? 21.47904 55.96545 4.25135   1.000 63.93118  ? 574 ARG B CZ  1 
ATOM   1227 N  NH1 . ARG B 2 7   ? 21.87633 55.53816 5.43879   1.000 73.19506  ? 574 ARG B NH1 1 
ATOM   1228 N  NH2 . ARG B 2 7   ? 22.36836 56.50561 3.42287   1.000 59.21895  ? 574 ARG B NH2 1 
ATOM   1229 N  N   . SER B 2 8   ? 17.87503 59.33109 7.09772   1.000 40.21057  ? 575 SER B N   1 
ATOM   1230 C  CA  . SER B 2 8   ? 18.78181 60.29452 7.70702   1.000 39.09917  ? 575 SER B CA  1 
ATOM   1231 C  C   . SER B 2 8   ? 20.21109 60.02876 7.25121   1.000 40.12756  ? 575 SER B C   1 
ATOM   1232 O  O   . SER B 2 8   ? 20.71811 58.90990 7.37737   1.000 54.80075  ? 575 SER B O   1 
ATOM   1233 C  CB  . SER B 2 8   ? 18.68588 60.22488 9.22998   1.000 41.44774  ? 575 SER B CB  1 
ATOM   1234 O  OG  . SER B 2 8   ? 19.49170 61.21987 9.83653   1.000 65.03231  ? 575 SER B OG  1 
ATOM   1235 N  N   . GLY B 2 9   ? 20.85975 61.06113 6.71703   1.000 53.71574  ? 576 GLY B N   1 
ATOM   1236 C  CA  . GLY B 2 9   ? 22.19603 60.94247 6.17714   1.000 43.90916  ? 576 GLY B CA  1 
ATOM   1237 C  C   . GLY B 2 9   ? 22.25888 60.82224 4.66997   1.000 59.55970  ? 576 GLY B C   1 
ATOM   1238 O  O   . GLY B 2 9   ? 23.35711 60.89825 4.10483   1.000 56.42120  ? 576 GLY B O   1 
ATOM   1239 N  N   . CYS B 2 10  ? 21.12151 60.63493 4.00599   1.000 46.10096  ? 577 CYS B N   1 
ATOM   1240 C  CA  . CYS B 2 10  ? 21.05372 60.55229 2.55287   1.000 44.97591  ? 577 CYS B CA  1 
ATOM   1241 C  C   . CYS B 2 10  ? 20.40737 61.82388 2.02177   1.000 49.20756  ? 577 CYS B C   1 
ATOM   1242 O  O   . CYS B 2 10  ? 19.29345 62.17460 2.42734   1.000 37.70618  ? 577 CYS B O   1 
ATOM   1243 C  CB  . CYS B 2 10  ? 20.26614 59.32066 2.10626   1.000 38.33216  ? 577 CYS B CB  1 
ATOM   1244 S  SG  . CYS B 2 10  ? 20.19922 59.09709 0.31306   1.000 37.71126  ? 577 CYS B SG  1 
ATOM   1245 N  N   . GLU B 2 11  ? 21.10667 62.51035 1.11974   1.000 41.49735  ? 578 GLU B N   1 
ATOM   1246 C  CA  . GLU B 2 11  ? 20.61613 63.74317 0.51964   1.000 36.43674  ? 578 GLU B CA  1 
ATOM   1247 C  C   . GLU B 2 11  ? 20.19223 63.55376 -0.93093  1.000 47.95959  ? 578 GLU B C   1 
ATOM   1248 O  O   . GLU B 2 11  ? 19.91022 64.54070 -1.61861  1.000 41.53488  ? 578 GLU B O   1 
ATOM   1249 C  CB  . GLU B 2 11  ? 21.68334 64.83649 0.61442   1.000 52.34527  ? 578 GLU B CB  1 
ATOM   1250 C  CG  . GLU B 2 11  ? 22.34541 64.94874 1.98000   1.000 57.22518  ? 578 GLU B CG  1 
ATOM   1251 C  CD  . GLU B 2 11  ? 21.39620 65.43208 3.05977   1.000 55.60605  ? 578 GLU B CD  1 
ATOM   1252 O  OE1 . GLU B 2 11  ? 20.39739 66.10385 2.72430   1.000 58.35251  ? 578 GLU B OE1 1 
ATOM   1253 O  OE2 . GLU B 2 11  ? 21.65091 65.13935 4.24712   1.000 61.74549  ? 578 GLU B OE2 1 
ATOM   1254 N  N   . ASN B 2 12  ? 20.13936 62.31393 -1.41006  1.000 39.23591  ? 579 ASN B N   1 
ATOM   1255 C  CA  . ASN B 2 12  ? 19.80847 62.06555 -2.80199  1.000 37.55654  ? 579 ASN B CA  1 
ATOM   1256 C  C   . ASN B 2 12  ? 18.33794 62.37932 -3.07201  1.000 41.30367  ? 579 ASN B C   1 
ATOM   1257 O  O   . ASN B 2 12  ? 17.48617 62.21063 -2.19587  1.000 36.85534  ? 579 ASN B O   1 
ATOM   1258 C  CB  . ASN B 2 12  ? 20.09745 60.61313 -3.16981  1.000 35.57610  ? 579 ASN B CB  1 
ATOM   1259 C  CG  . ASN B 2 12  ? 21.56138 60.25755 -3.03026  1.000 40.70829  ? 579 ASN B CG  1 
ATOM   1260 O  OD1 . ASN B 2 12  ? 22.43506 61.11377 -3.16342  1.000 49.94365  ? 579 ASN B OD1 1 
ATOM   1261 N  ND2 . ASN B 2 12  ? 21.83819 58.98682 -2.76167  1.000 48.91552  ? 579 ASN B ND2 1 
ATOM   1262 N  N   . PRO B 2 13  ? 18.01614 62.84278 -4.27568  1.000 45.59246  ? 580 PRO B N   1 
ATOM   1263 C  CA  . PRO B 2 13  ? 16.61266 63.04244 -4.64306  1.000 36.09605  ? 580 PRO B CA  1 
ATOM   1264 C  C   . PRO B 2 13  ? 15.88387 61.71360 -4.70947  1.000 39.96666  ? 580 PRO B C   1 
ATOM   1265 O  O   . PRO B 2 13  ? 16.46057 60.70182 -5.13648  1.000 40.89946  ? 580 PRO B O   1 
ATOM   1266 C  CB  . PRO B 2 13  ? 16.69585 63.70070 -6.03007  1.000 36.22999  ? 580 PRO B CB  1 
ATOM   1267 C  CG  . PRO B 2 13  ? 18.09434 64.22143 -6.13628  1.000 51.04352  ? 580 PRO B CG  1 
ATOM   1268 C  CD  . PRO B 2 13  ? 18.93482 63.27663 -5.34083  1.000 37.88669  ? 580 PRO B CD  1 
ATOM   1269 N  N   . PRO B 2 14  ? 14.62172 61.67092 -4.29057  1.000 40.21442  ? 581 PRO B N   1 
ATOM   1270 C  CA  . PRO B 2 14  ? 13.85996 60.42151 -4.38109  1.000 35.18379  ? 581 PRO B CA  1 
ATOM   1271 C  C   . PRO B 2 14  ? 13.60703 60.02924 -5.82721  1.000 41.06246  ? 581 PRO B C   1 
ATOM   1272 O  O   . PRO B 2 14  ? 13.58731 60.86770 -6.73202  1.000 39.06484  ? 581 PRO B O   1 
ATOM   1273 C  CB  . PRO B 2 14  ? 12.54577 60.74829 -3.65965  1.000 38.69682  ? 581 PRO B CB  1 
ATOM   1274 C  CG  . PRO B 2 14  ? 12.83308 61.98412 -2.85628  1.000 48.66456  ? 581 PRO B CG  1 
ATOM   1275 C  CD  . PRO B 2 14  ? 13.85236 62.74368 -3.64224  1.000 40.33404  ? 581 PRO B CD  1 
ATOM   1276 N  N   . ILE B 2 15  ? 13.41546 58.73127 -6.03756  1.000 30.03646  ? 582 ILE B N   1 
ATOM   1277 C  CA  . ILE B 2 15  ? 13.10047 58.19671 -7.35156  1.000 35.13703  ? 582 ILE B CA  1 
ATOM   1278 C  C   . ILE B 2 15  ? 11.68655 57.62131 -7.32015  1.000 40.66613  ? 582 ILE B C   1 
ATOM   1279 O  O   . ILE B 2 15  ? 11.09670 57.40858 -6.25993  1.000 36.38738  ? 582 ILE B O   1 
ATOM   1280 C  CB  . ILE B 2 15  ? 14.12039 57.13750 -7.81311  1.000 37.18226  ? 582 ILE B CB  1 
ATOM   1281 C  CG1 . ILE B 2 15  ? 14.03051 55.88580 -6.93867  1.000 31.08079  ? 582 ILE B CG1 1 
ATOM   1282 C  CG2 . ILE B 2 15  ? 15.53005 57.71039 -7.79683  1.000 37.95109  ? 582 ILE B CG2 1 
ATOM   1283 C  CD1 . ILE B 2 15  ? 14.86366 54.72285 -7.44755  1.000 38.11123  ? 582 ILE B CD1 1 
ATOM   1284 N  N   . VAL B 2 16  ? 11.14370 57.36866 -8.50635  1.000 35.97078  ? 583 VAL B N   1 
ATOM   1285 C  CA  . VAL B 2 16  ? 9.79955  56.82220 -8.65126  1.000 41.39816  ? 583 VAL B CA  1 
ATOM   1286 C  C   . VAL B 2 16  ? 9.87817  55.30373 -8.58522  1.000 38.07143  ? 583 VAL B C   1 
ATOM   1287 O  O   . VAL B 2 16  ? 10.71742 54.68449 -9.25021  1.000 40.30957  ? 583 VAL B O   1 
ATOM   1288 C  CB  . VAL B 2 16  ? 9.15624  57.28662 -9.96915  1.000 48.86172  ? 583 VAL B CB  1 
ATOM   1289 C  CG1 . VAL B 2 16  ? 7.80819  56.60971 -10.17982 1.000 39.32908  ? 583 VAL B CG1 1 
ATOM   1290 C  CG2 . VAL B 2 16  ? 9.00438  58.80085 -9.97689  1.000 59.11253  ? 583 VAL B CG2 1 
ATOM   1291 N  N   . SER B 2 17  ? 9.00870  54.70379 -7.77652  1.000 36.12459  ? 584 SER B N   1 
ATOM   1292 C  CA  . SER B 2 17  ? 8.93129  53.25499 -7.67134  1.000 39.36168  ? 584 SER B CA  1 
ATOM   1293 C  C   . SER B 2 17  ? 7.54745  52.87505 -7.17071  1.000 33.93900  ? 584 SER B C   1 
ATOM   1294 O  O   . SER B 2 17  ? 6.97978  53.56318 -6.31865  1.000 37.42732  ? 584 SER B O   1 
ATOM   1295 C  CB  . SER B 2 17  ? 10.00666 52.69796 -6.73147  1.000 39.93997  ? 584 SER B CB  1 
ATOM   1296 O  OG  . SER B 2 17  ? 9.80605  51.31572 -6.48691  1.000 42.59565  ? 584 SER B OG  1 
ATOM   1297 N  N   . LYS B 2 18  ? 7.01511  51.77339 -7.70248  1.000 33.09662  ? 585 LYS B N   1 
ATOM   1298 C  CA  . LYS B 2 18  ? 5.72955  51.26163 -7.24543  1.000 41.35786  ? 585 LYS B CA  1 
ATOM   1299 C  C   . LYS B 2 18  ? 5.78977  50.69974 -5.83117  1.000 46.83564  ? 585 LYS B C   1 
ATOM   1300 O  O   . LYS B 2 18  ? 4.74094  50.35343 -5.27710  1.000 43.25316  ? 585 LYS B O   1 
ATOM   1301 C  CB  . LYS B 2 18  ? 5.22537  50.18531 -8.20872  1.000 48.59616  ? 585 LYS B CB  1 
ATOM   1302 C  CG  . LYS B 2 18  ? 6.22303  49.06274 -8.45070  1.000 54.54426  ? 585 LYS B CG  1 
ATOM   1303 C  CD  . LYS B 2 18  ? 5.69615  48.04697 -9.45291  1.000 73.35656  ? 585 LYS B CD  1 
ATOM   1304 C  CE  . LYS B 2 18  ? 6.73622  46.97427 -9.74615  1.000 64.30660  ? 585 LYS B CE  1 
ATOM   1305 N  NZ  . LYS B 2 18  ? 6.22618  45.93433 -10.68264 1.000 82.54784  ? 585 LYS B NZ  1 
ATOM   1306 N  N   . ASP B 2 19  ? 6.97975  50.60651 -5.23776  1.000 40.32086  ? 586 ASP B N   1 
ATOM   1307 C  CA  . ASP B 2 19  ? 7.14983  50.04270 -3.90667  1.000 35.84270  ? 586 ASP B CA  1 
ATOM   1308 C  C   . ASP B 2 19  ? 7.13895  51.09090 -2.80084  1.000 33.91901  ? 586 ASP B C   1 
ATOM   1309 O  O   . ASP B 2 19  ? 7.11023  50.71942 -1.62237  1.000 33.42425  ? 586 ASP B O   1 
ATOM   1310 C  CB  . ASP B 2 19  ? 8.45477  49.24003 -3.84219  1.000 28.62778  ? 586 ASP B CB  1 
ATOM   1311 C  CG  . ASP B 2 19  ? 8.46882  48.07529 -4.81458  1.000 43.61853  ? 586 ASP B CG  1 
ATOM   1312 O  OD1 . ASP B 2 19  ? 7.40468  47.45075 -5.00811  1.000 43.82175  ? 586 ASP B OD1 1 
ATOM   1313 O  OD2 . ASP B 2 19  ? 9.53987  47.78591 -5.38880  1.000 42.83586  ? 586 ASP B OD2 1 
ATOM   1314 N  N   . TRP B 2 20  ? 7.16728  52.37459 -3.13999  1.000 30.05764  ? 587 TRP B N   1 
ATOM   1315 C  CA  . TRP B 2 20  ? 7.01975  53.43358 -2.14436  1.000 37.76583  ? 587 TRP B CA  1 
ATOM   1316 C  C   . TRP B 2 20  ? 6.31981  54.61560 -2.81057  1.000 37.11008  ? 587 TRP B C   1 
ATOM   1317 O  O   . TRP B 2 20  ? 5.68680  54.46311 -3.86011  1.000 39.69557  ? 587 TRP B O   1 
ATOM   1318 C  CB  . TRP B 2 20  ? 8.38044  53.79176 -1.51880  1.000 31.26727  ? 587 TRP B CB  1 
ATOM   1319 C  CG  . TRP B 2 20  ? 9.46065  54.15852 -2.48988  1.000 31.84163  ? 587 TRP B CG  1 
ATOM   1320 C  CD1 . TRP B 2 20  ? 9.62455  55.35737 -3.12219  1.000 36.85122  ? 587 TRP B CD1 1 
ATOM   1321 C  CD2 . TRP B 2 20  ? 10.55281 53.33126 -2.90963  1.000 28.70179  ? 587 TRP B CD2 1 
ATOM   1322 N  NE1 . TRP B 2 20  ? 10.74163 55.32149 -3.92204  1.000 35.36635  ? 587 TRP B NE1 1 
ATOM   1323 C  CE2 . TRP B 2 20  ? 11.32992 54.08930 -3.80822  1.000 29.84000  ? 587 TRP B CE2 1 
ATOM   1324 C  CE3 . TRP B 2 20  ? 10.94386 52.02036 -2.61935  1.000 28.54876  ? 587 TRP B CE3 1 
ATOM   1325 C  CZ2 . TRP B 2 20  ? 12.47503 53.58002 -4.41842  1.000 27.88014  ? 587 TRP B CZ2 1 
ATOM   1326 C  CZ3 . TRP B 2 20  ? 12.08040 51.51677 -3.22549  1.000 34.71866  ? 587 TRP B CZ3 1 
ATOM   1327 C  CH2 . TRP B 2 20  ? 12.83226 52.29470 -4.11516  1.000 32.62188  ? 587 TRP B CH2 1 
ATOM   1328 N  N   . ASP B 2 21  ? 6.42209  55.79840 -2.19947  1.000 32.66810  ? 588 ASP B N   1 
ATOM   1329 C  CA  . ASP B 2 21  ? 5.65284  56.96747 -2.62689  1.000 47.28869  ? 588 ASP B CA  1 
ATOM   1330 C  C   . ASP B 2 21  ? 6.57572  58.17652 -2.80545  1.000 40.96058  ? 588 ASP B C   1 
ATOM   1331 O  O   . ASP B 2 21  ? 6.37993  59.23205 -2.20344  1.000 29.13349  ? 588 ASP B O   1 
ATOM   1332 C  CB  . ASP B 2 21  ? 4.53416  57.27360 -1.63226  1.000 32.34363  ? 588 ASP B CB  1 
ATOM   1333 C  CG  . ASP B 2 21  ? 3.61801  56.08629 -1.40382  1.000 45.03425  ? 588 ASP B CG  1 
ATOM   1334 O  OD1 . ASP B 2 21  ? 4.00611  55.17005 -0.64780  1.000 38.57055  ? 588 ASP B OD1 1 
ATOM   1335 O  OD2 . ASP B 2 21  ? 2.51356  56.06457 -1.98597  1.000 41.72995  ? 588 ASP B OD2 1 
ATOM   1336 N  N   . ASN B 2 22  ? 7.59610  58.00832 -3.65017  1.000 31.15160  ? 589 ASN B N   1 
ATOM   1337 C  CA  . ASN B 2 22  ? 8.47476  59.10223 -4.07533  1.000 44.05127  ? 589 ASN B CA  1 
ATOM   1338 C  C   . ASN B 2 22  ? 9.16171  59.77334 -2.88392  1.000 40.09000  ? 589 ASN B C   1 
ATOM   1339 O  O   . ASN B 2 22  ? 9.23989  61.00024 -2.78953  1.000 31.19642  ? 589 ASN B O   1 
ATOM   1340 C  CB  . ASN B 2 22  ? 7.70071  60.12709 -4.91272  1.000 40.25274  ? 589 ASN B CB  1 
ATOM   1341 C  CG  . ASN B 2 22  ? 8.61104  61.12597 -5.60741  1.000 46.47631  ? 589 ASN B CG  1 
ATOM   1342 O  OD1 . ASN B 2 22  ? 9.71348  60.78644 -6.03753  1.000 50.61001  ? 589 ASN B OD1 1 
ATOM   1343 N  ND2 . ASN B 2 22  ? 8.15635  62.36979 -5.70607  1.000 41.47953  ? 589 ASN B ND2 1 
ATOM   1344 N  N   . GLU B 2 23  ? 9.66885  58.95305 -1.96068  1.000 29.80929  ? 590 GLU B N   1 
ATOM   1345 C  CA  . GLU B 2 23  ? 10.39489 59.49387 -0.81855  1.000 30.09646  ? 590 GLU B CA  1 
ATOM   1346 C  C   . GLU B 2 23  ? 11.66917 58.71392 -0.51069  1.000 36.37186  ? 590 GLU B C   1 
ATOM   1347 O  O   . GLU B 2 23  ? 12.31530 58.99219 0.50773   1.000 36.89852  ? 590 GLU B O   1 
ATOM   1348 C  CB  . GLU B 2 23  ? 9.48891  59.54820 0.42490   1.000 32.26156  ? 590 GLU B CB  1 
ATOM   1349 C  CG  . GLU B 2 23  ? 9.33110  58.23931 1.19171   1.000 37.97198  ? 590 GLU B CG  1 
ATOM   1350 C  CD  . GLU B 2 23  ? 8.35719  57.26670 0.54789   1.000 42.69301  ? 590 GLU B CD  1 
ATOM   1351 O  OE1 . GLU B 2 23  ? 8.39139  57.10191 -0.68864  1.000 33.19837  ? 590 GLU B OE1 1 
ATOM   1352 O  OE2 . GLU B 2 23  ? 7.55482  56.65899 1.28846   1.000 34.23580  ? 590 GLU B OE2 1 
ATOM   1353 N  N   . TYR B 2 24  ? 12.05566 57.75976 -1.35562  1.000 32.11963  ? 591 TYR B N   1 
ATOM   1354 C  CA  . TYR B 2 24  ? 13.30591 57.03011 -1.20733  1.000 35.83550  ? 591 TYR B CA  1 
ATOM   1355 C  C   . TYR B 2 24  ? 14.08091 57.08118 -2.51481  1.000 30.93001  ? 591 TYR B C   1 
ATOM   1356 O  O   . TYR B 2 24  ? 13.49573 57.15678 -3.59853  1.000 33.31220  ? 591 TYR B O   1 
ATOM   1357 C  CB  . TYR B 2 24  ? 13.07295 55.56628 -0.80946  1.000 34.04353  ? 591 TYR B CB  1 
ATOM   1358 C  CG  . TYR B 2 24  ? 12.50723 55.38732 0.57795   1.000 36.42694  ? 591 TYR B CG  1 
ATOM   1359 C  CD1 . TYR B 2 24  ? 13.34194 55.30664 1.68482   1.000 34.78898  ? 591 TYR B CD1 1 
ATOM   1360 C  CD2 . TYR B 2 24  ? 11.13907 55.29091 0.78082   1.000 36.41863  ? 591 TYR B CD2 1 
ATOM   1361 C  CE1 . TYR B 2 24  ? 12.82789 55.13860 2.95544   1.000 35.62992  ? 591 TYR B CE1 1 
ATOM   1362 C  CE2 . TYR B 2 24  ? 10.61571 55.12661 2.04590   1.000 33.20180  ? 591 TYR B CE2 1 
ATOM   1363 C  CZ  . TYR B 2 24  ? 11.46254 55.05056 3.12965   1.000 39.14099  ? 591 TYR B CZ  1 
ATOM   1364 O  OH  . TYR B 2 24  ? 10.93904 54.88560 4.39026   1.000 37.55076  ? 591 TYR B OH  1 
ATOM   1365 N  N   . CYS B 2 25  ? 15.40829 57.03299 -2.40303  1.000 35.77306  ? 592 CYS B N   1 
ATOM   1366 C  CA  . CYS B 2 25  ? 16.26811 57.05037 -3.57795  1.000 35.49108  ? 592 CYS B CA  1 
ATOM   1367 C  C   . CYS B 2 25  ? 16.65378 55.65836 -4.05594  1.000 46.24820  ? 592 CYS B C   1 
ATOM   1368 O  O   . CYS B 2 25  ? 17.10135 55.51621 -5.19946  1.000 40.00783  ? 592 CYS B O   1 
ATOM   1369 C  CB  . CYS B 2 25  ? 17.54618 57.84920 -3.29467  1.000 38.63922  ? 592 CYS B CB  1 
ATOM   1370 S  SG  . CYS B 2 25  ? 18.78511 56.97404 -2.29879  1.000 38.46722  ? 592 CYS B SG  1 
ATOM   1371 N  N   . SER B 2 26  ? 16.49193 54.63479 -3.22019  1.000 37.48291  ? 593 SER B N   1 
ATOM   1372 C  CA  . SER B 2 26  ? 16.94692 53.29452 -3.56518  1.000 32.20516  ? 593 SER B CA  1 
ATOM   1373 C  C   . SER B 2 26  ? 16.28334 52.28795 -2.63696  1.000 45.28882  ? 593 SER B C   1 
ATOM   1374 O  O   . SER B 2 26  ? 15.67227 52.64811 -1.62758  1.000 34.08066  ? 593 SER B O   1 
ATOM   1375 C  CB  . SER B 2 26  ? 18.47172 53.18680 -3.47422  1.000 32.21012  ? 593 SER B CB  1 
ATOM   1376 O  OG  . SER B 2 26  ? 18.91389 53.46641 -2.15688  1.000 35.02758  ? 593 SER B OG  1 
ATOM   1377 N  N   . ASN B 2 27  ? 16.41855 51.00847 -2.99714  1.000 35.91689  ? 594 ASN B N   1 
ATOM   1378 C  CA  . ASN B 2 27  ? 15.90833 49.93849 -2.14624  1.000 31.00529  ? 594 ASN B CA  1 
ATOM   1379 C  C   . ASN B 2 27  ? 16.68395 49.84140 -0.83857  1.000 34.90230  ? 594 ASN B C   1 
ATOM   1380 O  O   . ASN B 2 27  ? 16.09696 49.53904 0.20705   1.000 34.59427  ? 594 ASN B O   1 
ATOM   1381 C  CB  . ASN B 2 27  ? 15.96332 48.60206 -2.88641  1.000 38.64190  ? 594 ASN B CB  1 
ATOM   1382 C  CG  . ASN B 2 27  ? 14.99778 48.53807 -4.05208  1.000 31.12800  ? 594 ASN B CG  1 
ATOM   1383 O  OD1 . ASN B 2 27  ? 13.88029 49.04638 -3.97804  1.000 38.09113  ? 594 ASN B OD1 1 
ATOM   1384 N  ND2 . ASN B 2 27  ? 15.42517 47.90476 -5.13846  1.000 35.48818  ? 594 ASN B ND2 1 
ATOM   1385 N  N   . GLU B 2 28  ? 17.99685 50.08811 -0.87560  1.000 35.87669  ? 595 GLU B N   1 
ATOM   1386 C  CA  . GLU B 2 28  ? 18.80133 49.99645 0.33907   1.000 34.20246  ? 595 GLU B CA  1 
ATOM   1387 C  C   . GLU B 2 28  ? 18.37591 51.03331 1.36882   1.000 31.97673  ? 595 GLU B C   1 
ATOM   1388 O  O   . GLU B 2 28  ? 18.37600 50.75248 2.57326   1.000 32.52138  ? 595 GLU B O   1 
ATOM   1389 C  CB  . GLU B 2 28  ? 20.28606 50.15704 0.01052   1.000 36.89042  ? 595 GLU B CB  1 
ATOM   1390 C  CG  . GLU B 2 28  ? 20.98122 48.87136 -0.39853  1.000 60.77158  ? 595 GLU B CG  1 
ATOM   1391 C  CD  . GLU B 2 28  ? 22.49397 48.98429 -0.35835  1.000 93.56134  ? 595 GLU B CD  1 
ATOM   1392 O  OE1 . GLU B 2 28  ? 23.00441 50.10542 -0.15073  1.000 81.90858  ? 595 GLU B OE1 1 
ATOM   1393 O  OE2 . GLU B 2 28  ? 23.17284 47.94939 -0.52973  1.000 95.86949  ? 595 GLU B OE2 1 
ATOM   1394 N  N   . CYS B 2 29  ? 18.01593 52.23913 0.92031   1.000 29.67893  ? 596 CYS B N   1 
ATOM   1395 C  CA  . CYS B 2 29  ? 17.62124 53.27247 1.87136   1.000 29.94566  ? 596 CYS B CA  1 
ATOM   1396 C  C   . CYS B 2 29  ? 16.29080 52.94546 2.53703   1.000 29.94613  ? 596 CYS B C   1 
ATOM   1397 O  O   . CYS B 2 29  ? 16.03074 53.40610 3.65302   1.000 40.88293  ? 596 CYS B O   1 
ATOM   1398 C  CB  . CYS B 2 29  ? 17.56331 54.63563 1.18073   1.000 34.60819  ? 596 CYS B CB  1 
ATOM   1399 S  SG  . CYS B 2 29  ? 19.19186 55.36416 0.86877   1.000 45.03223  ? 596 CYS B SG  1 
ATOM   1400 N  N   . VAL B 2 30  ? 15.44287 52.15399 1.87953   1.000 30.09873  ? 597 VAL B N   1 
ATOM   1401 C  CA  . VAL B 2 30  ? 14.20572 51.70763 2.51261   1.000 40.46439  ? 597 VAL B CA  1 
ATOM   1402 C  C   . VAL B 2 30  ? 14.51501 50.80070 3.69760   1.000 34.82592  ? 597 VAL B C   1 
ATOM   1403 O  O   . VAL B 2 30  ? 13.98876 50.98920 4.80077   1.000 37.59158  ? 597 VAL B O   1 
ATOM   1404 C  CB  . VAL B 2 30  ? 13.30022 51.00256 1.48698   1.000 40.47893  ? 597 VAL B CB  1 
ATOM   1405 C  CG1 . VAL B 2 30  ? 12.04544 50.47790 2.16667   1.000 33.62648  ? 597 VAL B CG1 1 
ATOM   1406 C  CG2 . VAL B 2 30  ? 12.94347 51.94951 0.35592   1.000 39.72344  ? 597 VAL B CG2 1 
ATOM   1407 N  N   . VAL B 2 31  ? 15.37887 49.80544 3.48768   1.000 33.87789  ? 598 VAL B N   1 
ATOM   1408 C  CA  . VAL B 2 31  ? 15.69663 48.85766 4.55130   1.000 42.13974  ? 598 VAL B CA  1 
ATOM   1409 C  C   . VAL B 2 31  ? 16.47144 49.54284 5.67013   1.000 33.56463  ? 598 VAL B C   1 
ATOM   1410 O  O   . VAL B 2 31  ? 16.21534 49.30368 6.85647   1.000 31.28612  ? 598 VAL B O   1 
ATOM   1411 C  CB  . VAL B 2 31  ? 16.46856 47.65588 3.97726   1.000 28.10850  ? 598 VAL B CB  1 
ATOM   1412 C  CG1 . VAL B 2 31  ? 16.88824 46.70760 5.09194   1.000 35.88408  ? 598 VAL B CG1 1 
ATOM   1413 C  CG2 . VAL B 2 31  ? 15.61845 46.92973 2.95057   1.000 30.46200  ? 598 VAL B CG2 1 
ATOM   1414 N  N   . LYS B 2 32  ? 17.42311 50.40992 5.31605   1.000 33.05686  ? 599 LYS B N   1 
ATOM   1415 C  CA  . LYS B 2 32  ? 18.22524 51.07728 6.33652   1.000 38.18881  ? 599 LYS B CA  1 
ATOM   1416 C  C   . LYS B 2 32  ? 17.38692 52.04765 7.15967   1.000 38.76272  ? 599 LYS B C   1 
ATOM   1417 O  O   . LYS B 2 32  ? 17.56113 52.14248 8.38026   1.000 38.99482  ? 599 LYS B O   1 
ATOM   1418 C  CB  . LYS B 2 32  ? 19.40466 51.80272 5.69038   1.000 33.72679  ? 599 LYS B CB  1 
ATOM   1419 C  CG  . LYS B 2 32  ? 20.44807 50.87866 5.08624   1.000 38.04673  ? 599 LYS B CG  1 
ATOM   1420 C  CD  . LYS B 2 32  ? 21.61057 51.66951 4.50791   1.000 67.70740  ? 599 LYS B CD  1 
ATOM   1421 C  CE  . LYS B 2 32  ? 22.67092 50.74858 3.92729   1.000 58.84133  ? 599 LYS B CE  1 
ATOM   1422 N  NZ  . LYS B 2 32  ? 23.82291 51.51227 3.37405   1.000 78.56762  ? 599 LYS B NZ  1 
ATOM   1423 N  N   . HIS B 2 33  ? 16.47492 52.77857 6.51344   1.000 33.28650  ? 600 HIS B N   1 
ATOM   1424 C  CA  . HIS B 2 33  ? 15.64320 53.72782 7.24747   1.000 39.22903  ? 600 HIS B CA  1 
ATOM   1425 C  C   . HIS B 2 33  ? 14.67711 53.01048 8.18104   1.000 32.25275  ? 600 HIS B C   1 
ATOM   1426 O  O   . HIS B 2 33  ? 14.46880 53.44616 9.31903   1.000 34.91480  ? 600 HIS B O   1 
ATOM   1427 C  CB  . HIS B 2 33  ? 14.87929 54.62693 6.27678   1.000 33.12307  ? 600 HIS B CB  1 
ATOM   1428 C  CG  . HIS B 2 33  ? 13.97662 55.61240 6.95083   1.000 34.75495  ? 600 HIS B CG  1 
ATOM   1429 N  ND1 . HIS B 2 33  ? 14.42631 56.50680 7.89810   1.000 34.22218  ? 600 HIS B ND1 1 
ATOM   1430 C  CD2 . HIS B 2 33  ? 12.64972 55.84468 6.81425   1.000 33.07274  ? 600 HIS B CD2 1 
ATOM   1431 C  CE1 . HIS B 2 33  ? 13.41524 57.24719 8.31637   1.000 40.32534  ? 600 HIS B CE1 1 
ATOM   1432 N  NE2 . HIS B 2 33  ? 12.32584 56.86547 7.67446   1.000 44.32326  ? 600 HIS B NE2 1 
ATOM   1433 N  N   . SER B 2 34  ? 14.07405 51.91258 7.71778   1.000 29.06406  ? 601 SER B N   1 
ATOM   1434 C  CA  . SER B 2 34  ? 13.19601 51.13535 8.58581   1.000 36.12792  ? 601 SER B CA  1 
ATOM   1435 C  C   . SER B 2 34  ? 13.95610 50.56012 9.77210   1.000 35.70037  ? 601 SER B C   1 
ATOM   1436 O  O   . SER B 2 34  ? 13.39412 50.42890 10.86553  1.000 39.73825  ? 601 SER B O   1 
ATOM   1437 C  CB  . SER B 2 34  ? 12.52345 50.01594 7.79059   1.000 30.92745  ? 601 SER B CB  1 
ATOM   1438 O  OG  . SER B 2 34  ? 11.66660 50.54280 6.79214   1.000 44.00984  ? 601 SER B OG  1 
ATOM   1439 N  N   . ARG B 2 35  ? 15.23118 50.21596 9.57760   1.000 37.20063  ? 602 ARG B N   1 
ATOM   1440 C  CA  . ARG B 2 35  ? 16.04951 49.74222 10.68807  1.000 34.49045  ? 602 ARG B CA  1 
ATOM   1441 C  C   . ARG B 2 35  ? 16.36810 50.87344 11.65838  1.000 41.14728  ? 602 ARG B C   1 
ATOM   1442 O  O   . ARG B 2 35  ? 16.36991 50.66986 12.87847  1.000 41.14509  ? 602 ARG B O   1 
ATOM   1443 C  CB  . ARG B 2 35  ? 17.33450 49.10845 10.15501  1.000 37.06186  ? 602 ARG B CB  1 
ATOM   1444 C  CG  . ARG B 2 35  ? 18.29558 48.64546 11.23504  1.000 45.98635  ? 602 ARG B CG  1 
ATOM   1445 C  CD  . ARG B 2 35  ? 19.58916 48.12255 10.63281  1.000 44.61737  ? 602 ARG B CD  1 
ATOM   1446 N  NE  . ARG B 2 35  ? 20.60192 47.87875 11.65265  1.000 57.73400  ? 602 ARG B NE  1 
ATOM   1447 C  CZ  . ARG B 2 35  ? 21.43967 48.79931 12.11074  1.000 54.19015  ? 602 ARG B CZ  1 
ATOM   1448 N  NH1 . ARG B 2 35  ? 21.41379 50.04317 11.66016  1.000 41.96275  ? 602 ARG B NH1 1 
ATOM   1449 N  NH2 . ARG B 2 35  ? 22.32520 48.46368 13.04515  1.000 35.26886  ? 602 ARG B NH2 1 
ATOM   1450 N  N   . ASP B 2 36  ? 16.64073 52.07271 11.13509  1.000 32.14857  ? 603 ASP B N   1 
ATOM   1451 C  CA  . ASP B 2 36  ? 16.89500 53.21937 12.00245  1.000 32.40992  ? 603 ASP B CA  1 
ATOM   1452 C  C   . ASP B 2 36  ? 15.66926 53.55863 12.84100  1.000 39.32100  ? 603 ASP B C   1 
ATOM   1453 O  O   . ASP B 2 36  ? 15.78618 53.84384 14.03886  1.000 38.63657  ? 603 ASP B O   1 
ATOM   1454 C  CB  . ASP B 2 36  ? 17.31881 54.42876 11.16839  1.000 39.60565  ? 603 ASP B CB  1 
ATOM   1455 C  CG  . ASP B 2 36  ? 18.65997 54.23198 10.49050  1.000 51.32085  ? 603 ASP B CG  1 
ATOM   1456 O  OD1 . ASP B 2 36  ? 19.34439 53.23257 10.79593  1.000 57.03123  ? 603 ASP B OD1 1 
ATOM   1457 O  OD2 . ASP B 2 36  ? 19.02807 55.07900 9.64890   1.000 50.61479  ? 603 ASP B OD2 1 
ATOM   1458 N  N   . VAL B 2 37  ? 14.48388 53.53351 12.22804  1.000 34.71550  ? 604 VAL B N   1 
ATOM   1459 C  CA  . VAL B 2 37  ? 13.26025 53.83880 12.96254  1.000 33.32885  ? 604 VAL B CA  1 
ATOM   1460 C  C   . VAL B 2 37  ? 12.98257 52.76692 14.00913  1.000 30.18693  ? 604 VAL B C   1 
ATOM   1461 O  O   . VAL B 2 37  ? 12.53240 53.06883 15.12108  1.000 37.61273  ? 604 VAL B O   1 
ATOM   1462 C  CB  . VAL B 2 37  ? 12.08027 54.00140 11.98656  1.000 40.60895  ? 604 VAL B CB  1 
ATOM   1463 C  CG1 . VAL B 2 37  ? 10.78429 54.23325 12.74703  1.000 40.30365  ? 604 VAL B CG1 1 
ATOM   1464 C  CG2 . VAL B 2 37  ? 12.34332 55.14690 11.02489  1.000 42.32542  ? 604 VAL B CG2 1 
ATOM   1465 N  N   . PHE B 2 38  ? 13.25098 51.50202 13.67606  1.000 31.22866  ? 605 PHE B N   1 
ATOM   1466 C  CA  . PHE B 2 38  ? 13.01688 50.41767 14.62562  1.000 39.90256  ? 605 PHE B CA  1 
ATOM   1467 C  C   . PHE B 2 38  ? 13.89776 50.57217 15.85979  1.000 42.42420  ? 605 PHE B C   1 
ATOM   1468 O  O   . PHE B 2 38  ? 13.42803 50.42896 16.99458  1.000 40.56281  ? 605 PHE B O   1 
ATOM   1469 C  CB  . PHE B 2 38  ? 13.26426 49.06816 13.94850  1.000 37.97526  ? 605 PHE B CB  1 
ATOM   1470 C  CG  . PHE B 2 38  ? 12.73895 47.88867 14.72466  1.000 34.46042  ? 605 PHE B CG  1 
ATOM   1471 C  CD1 . PHE B 2 38  ? 13.47870 47.32992 15.75500  1.000 42.00192  ? 605 PHE B CD1 1 
ATOM   1472 C  CD2 . PHE B 2 38  ? 11.50796 47.33424 14.41570  1.000 45.67014  ? 605 PHE B CD2 1 
ATOM   1473 C  CE1 . PHE B 2 38  ? 12.99682 46.24636 16.46629  1.000 38.83794  ? 605 PHE B CE1 1 
ATOM   1474 C  CE2 . PHE B 2 38  ? 11.02162 46.25027 15.12195  1.000 43.37902  ? 605 PHE B CE2 1 
ATOM   1475 C  CZ  . PHE B 2 38  ? 11.76699 45.70609 16.14862  1.000 49.27343  ? 605 PHE B CZ  1 
ATOM   1476 N  N   . LEU B 2 39  ? 15.18407 50.86722 15.65448  1.000 38.98418  ? 606 LEU B N   1 
ATOM   1477 C  CA  . LEU B 2 39  ? 16.09987 51.02691 16.78007  1.000 35.56354  ? 606 LEU B CA  1 
ATOM   1478 C  C   . LEU B 2 39  ? 15.72182 52.22710 17.64009  1.000 37.42989  ? 606 LEU B C   1 
ATOM   1479 O  O   . LEU B 2 39  ? 15.79235 52.15987 18.87281  1.000 40.76193  ? 606 LEU B O   1 
ATOM   1480 C  CB  . LEU B 2 39  ? 17.53505 51.15771 16.27046  1.000 30.03892  ? 606 LEU B CB  1 
ATOM   1481 C  CG  . LEU B 2 39  ? 18.14104 49.89677 15.65116  1.000 43.31303  ? 606 LEU B CG  1 
ATOM   1482 C  CD1 . LEU B 2 39  ? 19.47795 50.20802 15.00198  1.000 42.22569  ? 606 LEU B CD1 1 
ATOM   1483 C  CD2 . LEU B 2 39  ? 18.29532 48.81045 16.70439  1.000 47.91811  ? 606 LEU B CD2 1 
ATOM   1484 N  N   . ALA B 2 40  ? 15.32053 53.33471 17.01096  1.000 37.67412  ? 607 ALA B N   1 
ATOM   1485 C  CA  . ALA B 2 40  ? 14.88467 54.49678 17.77738  1.000 37.08776  ? 607 ALA B CA  1 
ATOM   1486 C  C   . ALA B 2 40  ? 13.58335 54.22120 18.51782  1.000 36.34752  ? 607 ALA B C   1 
ATOM   1487 O  O   . ALA B 2 40  ? 13.37219 54.74865 19.61587  1.000 43.67328  ? 607 ALA B O   1 
ATOM   1488 C  CB  . ALA B 2 40  ? 14.72712 55.70663 16.85741  1.000 39.86781  ? 607 ALA B CB  1 
ATOM   1489 N  N   . TRP B 2 41  ? 12.70394 53.40332 17.93520  1.000 33.27327  ? 608 TRP B N   1 
ATOM   1490 C  CA  . TRP B 2 41  ? 11.46640 53.03563 18.61447  1.000 40.11142  ? 608 TRP B CA  1 
ATOM   1491 C  C   . TRP B 2 41  ? 11.74869 52.17057 19.83619  1.000 39.03429  ? 608 TRP B C   1 
ATOM   1492 O  O   . TRP B 2 41  ? 11.10419 52.32973 20.87949  1.000 41.28898  ? 608 TRP B O   1 
ATOM   1493 C  CB  . TRP B 2 41  ? 10.53543 52.31659 17.63813  1.000 43.31844  ? 608 TRP B CB  1 
ATOM   1494 C  CG  . TRP B 2 41  ? 9.23471  51.87576 18.23140  1.000 43.65045  ? 608 TRP B CG  1 
ATOM   1495 C  CD1 . TRP B 2 41  ? 8.13123  52.64653 18.45333  1.000 42.09672  ? 608 TRP B CD1 1 
ATOM   1496 C  CD2 . TRP B 2 41  ? 8.89369  50.55335 18.66227  1.000 40.04546  ? 608 TRP B CD2 1 
ATOM   1497 N  NE1 . TRP B 2 41  ? 7.12659  51.88765 19.00277  1.000 41.06448  ? 608 TRP B NE1 1 
ATOM   1498 C  CE2 . TRP B 2 41  ? 7.56961  50.59871 19.14126  1.000 43.31452  ? 608 TRP B CE2 1 
ATOM   1499 C  CE3 . TRP B 2 41  ? 9.58085  49.33638 18.69317  1.000 43.18257  ? 608 TRP B CE3 1 
ATOM   1500 C  CZ2 . TRP B 2 41  ? 6.91929  49.47455 19.64436  1.000 44.46069  ? 608 TRP B CZ2 1 
ATOM   1501 C  CZ3 . TRP B 2 41  ? 8.93374  48.22164 19.19353  1.000 52.41244  ? 608 TRP B CZ3 1 
ATOM   1502 C  CH2 . TRP B 2 41  ? 7.61698  48.29867 19.66227  1.000 49.54250  ? 608 TRP B CH2 1 
ATOM   1503 N  N   . VAL B 2 42  ? 12.71259 51.25379 19.72661  1.000 40.86360  ? 609 VAL B N   1 
ATOM   1504 C  CA  . VAL B 2 42  ? 13.11622 50.45520 20.87974  1.000 43.75101  ? 609 VAL B CA  1 
ATOM   1505 C  C   . VAL B 2 42  ? 13.76563 51.33810 21.93820  1.000 47.19539  ? 609 VAL B C   1 
ATOM   1506 O  O   . VAL B 2 42  ? 13.52323 51.17175 23.13987  1.000 42.56407  ? 609 VAL B O   1 
ATOM   1507 C  CB  . VAL B 2 42  ? 14.05319 49.31660 20.43602  1.000 35.25628  ? 609 VAL B CB  1 
ATOM   1508 C  CG1 . VAL B 2 42  ? 14.61596 48.58388 21.64476  1.000 36.78426  ? 609 VAL B CG1 1 
ATOM   1509 C  CG2 . VAL B 2 42  ? 13.31612 48.35186 19.51993  1.000 39.42242  ? 609 VAL B CG2 1 
ATOM   1510 N  N   . ALA B 2 43  ? 14.59491 52.29428 21.51090  1.000 39.99293  ? 610 ALA B N   1 
ATOM   1511 C  CA  . ALA B 2 43  ? 15.23542 53.19881 22.45904  1.000 39.87021  ? 610 ALA B CA  1 
ATOM   1512 C  C   . ALA B 2 43  ? 14.21562 54.06685 23.18397  1.000 38.70204  ? 610 ALA B C   1 
ATOM   1513 O  O   . ALA B 2 43  ? 14.40305 54.38755 24.36326  1.000 43.08742  ? 610 ALA B O   1 
ATOM   1514 C  CB  . ALA B 2 43  ? 16.26291 54.07289 21.74105  1.000 42.18759  ? 610 ALA B CB  1 
ATOM   1515 N  N   . SER B 2 44  ? 13.13200 54.44964 22.50398  1.000 38.48603  ? 611 SER B N   1 
ATOM   1516 C  CA  . SER B 2 44  ? 12.11815 55.28970 23.12994  1.000 37.12042  ? 611 SER B CA  1 
ATOM   1517 C  C   . SER B 2 44  ? 11.32066 54.54368 24.19035  1.000 39.57148  ? 611 SER B C   1 
ATOM   1518 O  O   . SER B 2 44  ? 10.71072 55.18527 25.05176  1.000 55.75012  ? 611 SER B O   1 
ATOM   1519 C  CB  . SER B 2 44  ? 11.17047 55.85371 22.07177  1.000 41.49080  ? 611 SER B CB  1 
ATOM   1520 O  OG  . SER B 2 44  ? 10.39843 54.82437 21.47758  1.000 53.27349  ? 611 SER B OG  1 
ATOM   1521 N  N   . ARG B 2 45  ? 11.30321 53.21290 24.14530  1.000 42.52312  ? 612 ARG B N   1 
ATOM   1522 C  CA  A ARG B 2 45  ? 10.59555 52.40129 25.12522  0.647 37.90426  ? 612 ARG B CA  1 
ATOM   1523 C  CA  B ARG B 2 45  ? 10.59394 52.41509 25.13501  0.353 37.93818  ? 612 ARG B CA  1 
ATOM   1524 C  C   . ARG B 2 45  ? 11.51294 51.83925 26.20328  1.000 50.13996  ? 612 ARG B C   1 
ATOM   1525 O  O   . ARG B 2 45  ? 11.03400 51.13982 27.10117  1.000 46.31973  ? 612 ARG B O   1 
ATOM   1526 C  CB  A ARG B 2 45  ? 9.85948  51.25010 24.42987  0.647 44.77231  ? 612 ARG B CB  1 
ATOM   1527 C  CB  B ARG B 2 45  ? 9.82010  51.28370 24.44963  0.353 44.71504  ? 612 ARG B CB  1 
ATOM   1528 C  CG  A ARG B 2 45  ? 8.91834  51.68127 23.31622  0.647 40.28025  ? 612 ARG B CG  1 
ATOM   1529 C  CG  B ARG B 2 45  ? 8.41563  51.67562 24.01519  0.353 39.81042  ? 612 ARG B CG  1 
ATOM   1530 C  CD  A ARG B 2 45  ? 8.10472  50.50278 22.80369  0.647 42.03765  ? 612 ARG B CD  1 
ATOM   1531 C  CD  B ARG B 2 45  ? 8.27044  51.68461 22.50389  0.353 46.01339  ? 612 ARG B CD  1 
ATOM   1532 N  NE  A ARG B 2 45  ? 7.04159  50.12834 23.72875  0.647 61.21526  ? 612 ARG B NE  1 
ATOM   1533 N  NE  B ARG B 2 45  ? 6.94041  52.11876 22.09289  0.353 41.62385  ? 612 ARG B NE  1 
ATOM   1534 C  CZ  A ARG B 2 45  ? 6.32085  49.01920 23.63427  0.647 51.72961  ? 612 ARG B CZ  1 
ATOM   1535 C  CZ  B ARG B 2 45  ? 6.63288  53.36018 21.74281  0.353 46.33806  ? 612 ARG B CZ  1 
ATOM   1536 N  NH1 A ARG B 2 45  ? 6.54381  48.12883 22.68181  0.647 37.74102  ? 612 ARG B NH1 1 
ATOM   1537 N  NH1 B ARG B 2 45  ? 7.54376  54.31933 21.72681  0.353 53.19420  ? 612 ARG B NH1 1 
ATOM   1538 N  NH2 A ARG B 2 45  ? 5.35181  48.79795 24.51773  0.647 57.36710  ? 612 ARG B NH2 1 
ATOM   1539 N  NH2 B ARG B 2 45  ? 5.38114  53.64542 21.39552  0.353 36.38176  ? 612 ARG B NH2 1 
ATOM   1540 N  N   . ASN B 2 46  ? 12.81101 52.11658 26.13493  1.000 41.15494  ? 613 ASN B N   1 
ATOM   1541 C  CA  . ASN B 2 46  ? 13.76048 51.64446 27.12726  1.000 55.82127  ? 613 ASN B CA  1 
ATOM   1542 C  C   . ASN B 2 46  ? 14.14421 52.79185 28.06026  1.000 50.26490  ? 613 ASN B C   1 
ATOM   1543 O  O   . ASN B 2 46  ? 13.52912 53.86326 28.05186  1.000 47.53484  ? 613 ASN B O   1 
ATOM   1544 C  CB  . ASN B 2 46  ? 14.98089 51.02769 26.44076  1.000 45.23029  ? 613 ASN B CB  1 
ATOM   1545 C  CG  . ASN B 2 46  ? 14.76254 49.57508 26.06191  1.000 64.90455  ? 613 ASN B CG  1 
ATOM   1546 O  OD1 . ASN B 2 46  ? 15.12788 48.66584 26.80763  1.000 65.54473  ? 613 ASN B OD1 1 
ATOM   1547 N  ND2 . ASN B 2 46  ? 14.15791 49.34964 24.90158  1.000 52.28230  ? 613 ASN B ND2 1 
ATOM   1548 N  N   . SER B 2 47  ? 15.17117 52.56809 28.87681  1.000 50.51900  ? 614 SER B N   1 
ATOM   1549 C  CA  . SER B 2 47  ? 15.57733 53.55974 29.86280  1.000 56.05222  ? 614 SER B CA  1 
ATOM   1550 C  C   . SER B 2 47  ? 16.14291 54.79840 29.17967  1.000 47.52886  ? 614 SER B C   1 
ATOM   1551 O  O   . SER B 2 47  ? 16.88695 54.70421 28.19951  1.000 51.73949  ? 614 SER B O   1 
ATOM   1552 C  CB  . SER B 2 47  ? 16.61279 52.96646 30.81765  1.000 42.96506  ? 614 SER B CB  1 
ATOM   1553 O  OG  . SER B 2 47  ? 16.95115 53.89016 31.83742  1.000 81.13316  ? 614 SER B OG  1 
ATOM   1554 N  N   . ASN B 2 48  ? 15.78066 55.96597 29.70328  1.000 47.34103  ? 615 ASN B N   1 
ATOM   1555 C  CA  . ASN B 2 48  ? 16.20696 57.24235 29.15411  1.000 63.61764  ? 615 ASN B CA  1 
ATOM   1556 C  C   . ASN B 2 48  ? 17.02123 58.00847 30.18830  1.000 61.71752  ? 615 ASN B C   1 
ATOM   1557 O  O   . ASN B 2 48  ? 16.91912 57.76851 31.39454  1.000 65.78853  ? 615 ASN B O   1 
ATOM   1558 C  CB  . ASN B 2 48  ? 15.00488 58.09018 28.71492  1.000 52.24212  ? 615 ASN B CB  1 
ATOM   1559 C  CG  . ASN B 2 48  ? 13.89964 57.25947 28.09448  1.000 70.93780  ? 615 ASN B CG  1 
ATOM   1560 O  OD1 . ASN B 2 48  ? 13.95451 56.91218 26.91480  1.000 61.19320  ? 615 ASN B OD1 1 
ATOM   1561 N  ND2 . ASN B 2 48  ? 12.88282 56.94166 28.88840  1.000 56.76028  ? 615 ASN B ND2 1 
ATOM   1562 N  N   . THR B 2 49  ? 17.83889 58.93928 29.69929  1.000 68.09836  ? 616 THR B N   1 
ATOM   1563 C  CA  . THR B 2 49  ? 18.57703 59.84378 30.56996  1.000 63.52592  ? 616 THR B CA  1 
ATOM   1564 C  C   . THR B 2 49  ? 17.78547 61.09549 30.92299  1.000 58.05896  ? 616 THR B C   1 
ATOM   1565 O  O   . THR B 2 49  ? 18.22561 61.86761 31.78153  1.000 63.60741  ? 616 THR B O   1 
ATOM   1566 C  CB  . THR B 2 49  ? 19.90587 60.24874 29.92030  1.000 65.58940  ? 616 THR B CB  1 
ATOM   1567 O  OG1 . THR B 2 49  ? 19.65734 60.81863 28.62916  1.000 69.51035  ? 616 THR B OG1 1 
ATOM   1568 C  CG2 . THR B 2 49  ? 20.81702 59.03914 29.77162  1.000 65.81704  ? 616 THR B CG2 1 
ATOM   1569 N  N   . VAL B 2 50  ? 16.63739 61.31179 30.28369  1.000 64.44056  ? 617 VAL B N   1 
ATOM   1570 C  CA  . VAL B 2 50  ? 15.75786 62.43442 30.57699  1.000 63.01086  ? 617 VAL B CA  1 
ATOM   1571 C  C   . VAL B 2 50  ? 14.32770 61.92063 30.64978  1.000 56.87780  ? 617 VAL B C   1 
ATOM   1572 O  O   . VAL B 2 50  ? 13.96573 60.93915 29.99339  1.000 69.50825  ? 617 VAL B O   1 
ATOM   1573 C  CB  . VAL B 2 50  ? 15.88008 63.55957 29.52534  1.000 56.16910  ? 617 VAL B CB  1 
ATOM   1574 C  CG1 . VAL B 2 50  ? 17.19598 64.30385 29.69157  1.000 51.36940  ? 617 VAL B CG1 1 
ATOM   1575 C  CG2 . VAL B 2 50  ? 15.76253 62.98649 28.12124  1.000 51.05595  ? 617 VAL B CG2 1 
ATOM   1576 N  N   . VAL B 2 51  ? 13.50990 62.59339 31.45965  1.000 61.10693  ? 618 VAL B N   1 
ATOM   1577 C  CA  . VAL B 2 51  ? 12.12047 62.17536 31.63018  1.000 49.81308  ? 618 VAL B CA  1 
ATOM   1578 C  C   . VAL B 2 51  ? 11.31026 62.50338 30.38160  1.000 59.84433  ? 618 VAL B C   1 
ATOM   1579 O  O   . VAL B 2 51  ? 10.71785 61.61931 29.75230  1.000 63.89979  ? 618 VAL B O   1 
ATOM   1580 C  CB  . VAL B 2 51  ? 11.51088 62.82676 32.88325  1.000 59.66768  ? 618 VAL B CB  1 
ATOM   1581 C  CG1 . VAL B 2 51  ? 10.04832 62.43582 33.02531  1.000 47.03822  ? 618 VAL B CG1 1 
ATOM   1582 C  CG2 . VAL B 2 51  ? 12.29850 62.43013 34.12265  1.000 46.41617  ? 618 VAL B CG2 1 
ATOM   1583 N  N   . PHE B 2 52  ? 11.27079 63.77831 30.00861  1.000 55.00988  ? 619 PHE B N   1 
ATOM   1584 C  CA  . PHE B 2 52  ? 10.55440 64.23199 28.82757  1.000 63.78895  ? 619 PHE B CA  1 
ATOM   1585 C  C   . PHE B 2 52  ? 11.53993 64.58050 27.71956  1.000 76.56116  ? 619 PHE B C   1 
ATOM   1586 O  O   . PHE B 2 52  ? 12.67661 64.98567 27.98010  1.000 71.06656  ? 619 PHE B O   1 
ATOM   1587 C  CB  . PHE B 2 52  ? 9.67927  65.44828 29.14516  1.000 62.93082  ? 619 PHE B CB  1 
ATOM   1588 C  CG  . PHE B 2 52  ? 8.64595  65.19303 30.20521  1.000 61.10867  ? 619 PHE B CG  1 
ATOM   1589 C  CD1 . PHE B 2 52  ? 7.45211  64.56579 29.89005  1.000 59.86130  ? 619 PHE B CD1 1 
ATOM   1590 C  CD2 . PHE B 2 52  ? 8.86584  65.58654 31.51482  1.000 62.00301  ? 619 PHE B CD2 1 
ATOM   1591 C  CE1 . PHE B 2 52  ? 6.49745  64.33153 30.86199  1.000 47.38302  ? 619 PHE B CE1 1 
ATOM   1592 C  CE2 . PHE B 2 52  ? 7.91500  65.35584 32.49149  1.000 62.39422  ? 619 PHE B CE2 1 
ATOM   1593 C  CZ  . PHE B 2 52  ? 6.72925  64.72713 32.16424  1.000 51.25884  ? 619 PHE B CZ  1 
ATOM   1594 N  N   . VAL B 2 53  ? 11.09213 64.42010 26.47836  1.000 70.21104  ? 620 VAL B N   1 
ATOM   1595 C  CA  . VAL B 2 53  ? 11.92809 64.71490 25.32091  1.000 88.37166  ? 620 VAL B CA  1 
ATOM   1596 C  C   . VAL B 2 53  ? 11.88412 66.20526 25.00265  1.000 63.94787  ? 620 VAL B C   1 
ATOM   1597 O  O   . VAL B 2 53  ? 12.90512 66.89165 25.05407  1.000 69.70403  ? 620 VAL B O   1 
ATOM   1598 C  CB  . VAL B 2 53  ? 11.49952 63.88503 24.09770  1.000 74.88096  ? 620 VAL B CB  1 
ATOM   1599 C  CG1 . VAL B 2 53  ? 12.42190 64.16105 22.91969  1.000 70.86687  ? 620 VAL B CG1 1 
ATOM   1600 C  CG2 . VAL B 2 53  ? 11.48907 62.40287 24.43919  1.000 71.65042  ? 620 VAL B CG2 1 
HETATM 1601 CL CL  . CL  C 3 .   ? 2.92559  63.18268 0.59915   1.000 47.09062  ? 201 CL  A CL  1 
HETATM 1602 CL CL  . CL  D 3 .   ? 1.30093  48.67696 2.70441   1.000 50.35651  ? 202 CL  A CL  1 
HETATM 1603 CL CL  . CL  E 3 .   ? 3.35345  40.82493 -4.19868  1.000 74.32845  ? 203 CL  A CL  1 
HETATM 1604 ZN ZN  . ZN  F 4 .   ? 3.34713  63.29195 -1.42569  1.000 42.01804  ? 204 ZN  A ZN  1 
HETATM 1605 NA NA  . NA  G 5 .   ? 2.75012  27.60552 0.93490   1.000 35.67022  ? 205 NA  A NA  1 
HETATM 1606 ZN ZN  . ZN  H 4 .   ? 18.63834 57.43763 -0.03268  1.000 40.41857  ? 701 ZN  B ZN  1 
HETATM 1607 CL CL  . CL  I 3 .   ? 19.52953 49.49954 -3.71050  1.000 56.67557  ? 702 CL  B CL  1 
HETATM 1608 O  O   . HOH J 6 .   ? 10.54689 36.54870 21.92729  1.000 32.46298  ? 301 HOH A O   1 
HETATM 1609 O  O   . HOH J 6 .   ? 25.18369 37.71741 3.16227   1.000 60.52931  ? 302 HOH A O   1 
HETATM 1610 O  O   . HOH J 6 .   ? 3.49705  21.84209 6.29744   1.000 48.31490  ? 303 HOH A O   1 
HETATM 1611 O  O   . HOH J 6 .   ? 27.96004 39.95372 -11.69241 1.000 63.27063  ? 304 HOH A O   1 
HETATM 1612 O  O   . HOH J 6 .   ? 6.28266  21.05949 10.52367  1.000 55.49773  ? 305 HOH A O   1 
HETATM 1613 O  O   . HOH J 6 .   ? 0.98813  26.99103 15.75237  1.000 57.72312  ? 306 HOH A O   1 
HETATM 1614 O  O   . HOH J 6 .   ? 6.54109  46.81438 -2.30601  1.000 36.98401  ? 307 HOH A O   1 
HETATM 1615 O  O   . HOH J 6 .   ? -1.39084 45.99926 6.47348   1.000 40.86938  ? 308 HOH A O   1 
HETATM 1616 O  O   . HOH J 6 .   ? 8.36241  30.74746 2.01816   1.000 32.39681  ? 309 HOH A O   1 
HETATM 1617 O  O   . HOH J 6 .   ? 5.37464  27.92397 -4.72446  1.000 44.33085  ? 310 HOH A O   1 
HETATM 1618 O  O   . HOH J 6 .   ? 4.174    51.820   24.972    1.000 37.87135  ? 311 HOH A O   1 
HETATM 1619 O  O   . HOH J 6 .   ? -0.97572 47.71821 19.77725  1.000 50.51565  ? 312 HOH A O   1 
HETATM 1620 O  O   . HOH J 6 .   ? 18.94160 43.78324 3.37703   1.000 35.33025  ? 313 HOH A O   1 
HETATM 1621 O  O   . HOH J 6 .   ? -2.53546 28.19465 13.11644  1.000 51.83450  ? 314 HOH A O   1 
HETATM 1622 O  O   . HOH J 6 .   ? 7.47399  36.19664 23.01655  1.000 45.41732  ? 315 HOH A O   1 
HETATM 1623 O  O   . HOH J 6 .   ? 9.02245  57.36982 10.69669  1.000 46.44816  ? 316 HOH A O   1 
HETATM 1624 O  O   . HOH J 6 .   ? -0.00123 47.74153 8.05246   1.000 44.00598  ? 317 HOH A O   1 
HETATM 1625 O  O   . HOH J 6 .   ? 10.70118 45.21093 -5.27905  1.000 43.35801  ? 318 HOH A O   1 
HETATM 1626 O  O   . HOH J 6 .   ? 9.97557  25.68740 0.19382   1.000 41.90123  ? 319 HOH A O   1 
HETATM 1627 O  O   . HOH J 6 .   ? 3.36664  46.61114 25.30523  1.000 51.68324  ? 320 HOH A O   1 
HETATM 1628 O  O   . HOH J 6 .   ? 15.04232 25.31792 9.83746   1.000 42.50094  ? 321 HOH A O   1 
HETATM 1629 O  O   . HOH J 6 .   ? 13.67352 22.22776 11.86586  1.000 47.08795  ? 322 HOH A O   1 
HETATM 1630 O  O   . HOH J 6 .   ? 11.84079 41.36115 24.49862  1.000 52.80412  ? 323 HOH A O   1 
HETATM 1631 O  O   . HOH J 6 .   ? 1.60948  39.82548 21.07405  1.000 44.34925  ? 324 HOH A O   1 
HETATM 1632 O  O   . HOH J 6 .   ? 20.20967 23.21313 10.08672  1.000 63.96156  ? 325 HOH A O   1 
HETATM 1633 O  O   . HOH J 6 .   ? 15.35774 30.43853 15.50607  1.000 46.07825  ? 326 HOH A O   1 
HETATM 1634 O  O   . HOH J 6 .   ? 1.37056  41.12699 1.17367   1.000 41.35513  ? 327 HOH A O   1 
HETATM 1635 O  O   . HOH J 6 .   ? 16.60014 45.28611 8.87664   1.000 45.69326  ? 328 HOH A O   1 
HETATM 1636 O  O   . HOH J 6 .   ? 15.46468 27.90649 8.40264   1.000 34.98720  ? 329 HOH A O   1 
HETATM 1637 O  O   . HOH J 6 .   ? 1.86307  55.30050 7.77889   1.000 52.10429  ? 330 HOH A O   1 
HETATM 1638 O  O   . HOH J 6 .   ? 5.71230  30.45263 -5.94172  1.000 50.21693  ? 331 HOH A O   1 
HETATM 1639 O  O   . HOH J 6 .   ? -4.252   58.428   -6.273    1.000 66.21498  ? 332 HOH A O   1 
HETATM 1640 O  O   . HOH J 6 .   ? 2.82334  57.47402 -4.87204  1.000 51.33794  ? 333 HOH A O   1 
HETATM 1641 O  O   . HOH J 6 .   ? -0.14978 54.51621 14.88438  1.000 50.74762  ? 334 HOH A O   1 
HETATM 1642 O  O   . HOH J 6 .   ? 4.73247  37.54778 -5.87519  1.000 37.02470  ? 335 HOH A O   1 
HETATM 1643 O  O   . HOH J 6 .   ? 1.10480  49.28506 6.40182   1.000 49.05904  ? 336 HOH A O   1 
HETATM 1644 O  O   . HOH J 6 .   ? 16.55368 38.02732 17.38651  1.000 51.80612  ? 337 HOH A O   1 
HETATM 1645 O  O   . HOH J 6 .   ? 9.95397  24.19509 14.40590  1.000 50.04019  ? 338 HOH A O   1 
HETATM 1646 O  O   . HOH J 6 .   ? 27.02226 42.06154 -1.65362  1.000 49.83668  ? 339 HOH A O   1 
HETATM 1647 O  O   . HOH J 6 .   ? 29.57807 35.01245 -1.96833  1.000 50.80856  ? 340 HOH A O   1 
HETATM 1648 O  O   . HOH J 6 .   ? 20.12894 38.16823 -7.28758  1.000 45.73243  ? 341 HOH A O   1 
HETATM 1649 O  O   . HOH J 6 .   ? 25.981   40.235   5.396     1.000 53.63247  ? 342 HOH A O   1 
HETATM 1650 O  O   . HOH J 6 .   ? 1.83885  39.42367 -1.94209  1.000 64.31656  ? 343 HOH A O   1 
HETATM 1651 O  O   . HOH J 6 .   ? 2.90133  27.23681 17.97084  1.000 43.11776  ? 344 HOH A O   1 
HETATM 1652 O  O   . HOH J 6 .   ? 1.43894  35.50426 -4.87874  1.000 47.80387  ? 345 HOH A O   1 
HETATM 1653 O  O   . HOH J 6 .   ? 19.03748 35.55429 10.39844  1.000 38.27361  ? 346 HOH A O   1 
HETATM 1654 O  O   . HOH J 6 .   ? 22.90198 41.74570 0.25740   1.000 50.37712  ? 347 HOH A O   1 
HETATM 1655 O  O   . HOH J 6 .   ? 11.25705 24.03688 -3.41585  1.000 53.07961  ? 348 HOH A O   1 
HETATM 1656 O  O   . HOH J 6 .   ? 8.04143  44.77167 -1.75201  1.000 46.27041  ? 349 HOH A O   1 
HETATM 1657 O  O   . HOH J 6 .   ? 8.59711  44.73931 27.51931  1.000 38.94046  ? 350 HOH A O   1 
HETATM 1658 O  O   . HOH J 6 .   ? 16.78745 38.68790 -8.83390  1.000 54.98801  ? 351 HOH A O   1 
HETATM 1659 O  O   . HOH J 6 .   ? 18.51531 33.34210 -9.05601  1.000 57.28472  ? 352 HOH A O   1 
HETATM 1660 O  O   . HOH J 6 .   ? 1.50140  32.80402 23.64949  1.000 48.37092  ? 353 HOH A O   1 
HETATM 1661 O  O   . HOH J 6 .   ? 2.42937  28.88249 5.41872   1.000 38.42110  ? 354 HOH A O   1 
HETATM 1662 O  O   . HOH J 6 .   ? 10.18048 43.97653 -3.20694  1.000 48.49529  ? 355 HOH A O   1 
HETATM 1663 O  O   . HOH J 6 .   ? 12.00048 18.43955 10.24020  1.000 38.90391  ? 356 HOH A O   1 
HETATM 1664 O  O   . HOH J 6 .   ? -1.877   59.466   -7.027    1.000 44.11821  ? 357 HOH A O   1 
HETATM 1665 O  O   . HOH J 6 .   ? 10.55804 43.60618 28.44655  1.000 52.81817  ? 358 HOH A O   1 
HETATM 1666 O  O   . HOH J 6 .   ? 18.41264 46.29971 -5.50200  1.000 43.49125  ? 359 HOH A O   1 
HETATM 1667 O  O   . HOH J 6 .   ? -0.30333 40.40626 23.27243  1.000 34.34512  ? 360 HOH A O   1 
HETATM 1668 O  O   . HOH J 6 .   ? 28.70905 32.50760 -1.98926  1.000 57.97173  ? 361 HOH A O   1 
HETATM 1669 O  O   . HOH J 6 .   ? 8.45426  58.54202 5.54406   1.000 45.84387  ? 362 HOH A O   1 
HETATM 1670 O  O   . HOH J 6 .   ? -1.62765 48.95114 9.67595   1.000 55.29139  ? 363 HOH A O   1 
HETATM 1671 O  O   . HOH J 6 .   ? 10.577   48.073   30.270    1.000 58.87111  ? 364 HOH A O   1 
HETATM 1672 O  O   . HOH J 6 .   ? 17.72480 42.91561 8.16102   1.000 47.87621  ? 365 HOH A O   1 
HETATM 1673 O  O   . HOH J 6 .   ? 0.08315  35.08225 0.50396   1.000 47.72768  ? 366 HOH A O   1 
HETATM 1674 O  O   . HOH J 6 .   ? 12.06099 22.31896 14.06313  1.000 59.51962  ? 367 HOH A O   1 
HETATM 1675 O  O   . HOH J 6 .   ? 18.92388 43.21601 5.90393   1.000 44.56383  ? 368 HOH A O   1 
HETATM 1676 O  O   . HOH J 6 .   ? 0.78735  57.35242 9.56555   1.000 55.71494  ? 369 HOH A O   1 
HETATM 1677 O  O   . HOH J 6 .   ? -4.02552 46.53085 6.73408   1.000 50.27920  ? 370 HOH A O   1 
HETATM 1678 O  O   . HOH J 6 .   ? 6.24547  43.14615 27.47794  1.000 54.33707  ? 371 HOH A O   1 
HETATM 1679 O  O   . HOH J 6 .   ? 10.07351 24.81786 16.86530  1.000 52.90320  ? 372 HOH A O   1 
HETATM 1680 O  O   . HOH J 6 .   ? 12.23813 25.88004 17.49295  1.000 57.90709  ? 373 HOH A O   1 
HETATM 1681 O  O   . HOH K 6 .   ? 15.46915 55.27439 26.17825  1.000 45.13141  ? 801 HOH B O   1 
HETATM 1682 O  O   . HOH K 6 .   ? 7.517    55.886   23.395    1.000 50.71728  ? 802 HOH B O   1 
HETATM 1683 O  O   . HOH K 6 .   ? 11.24718 55.18802 27.36699  1.000 50.23222  ? 803 HOH B O   1 
HETATM 1684 O  O   . HOH K 6 .   ? 20.16718 51.48558 9.37075   1.000 44.32766  ? 804 HOH B O   1 
HETATM 1685 O  O   . HOH K 6 .   ? 17.63062 62.55929 4.33746   1.000 47.52827  ? 805 HOH B O   1 
HETATM 1686 O  O   . HOH K 6 .   ? 18.39676 59.81805 -6.42680  1.000 38.34566  ? 806 HOH B O   1 
HETATM 1687 O  O   . HOH K 6 .   ? 17.81810 56.23004 33.17535  1.000 52.89829  ? 807 HOH B O   1 
HETATM 1688 O  O   . HOH K 6 .   ? 10.664   64.811   -5.940    1.000 57.19219  ? 808 HOH B O   1 
HETATM 1689 O  O   . HOH K 6 .   ? 11.72324 62.42668 -7.55209  1.000 45.35477  ? 809 HOH B O   1 
HETATM 1690 O  O   . HOH K 6 .   ? 20.61085 68.31984 1.39111   1.000 45.34382  ? 810 HOH B O   1 
HETATM 1691 O  O   . HOH K 6 .   ? 14.71415 47.37035 7.78794   1.000 32.15346  ? 811 HOH B O   1 
HETATM 1692 O  O   . HOH K 6 .   ? 7.20099  56.47741 -5.74479  1.000 42.83789  ? 812 HOH B O   1 
HETATM 1693 O  O   . HOH K 6 .   ? 16.81692 57.24025 8.72002   1.000 32.56401  ? 813 HOH B O   1 
HETATM 1694 O  O   . HOH K 6 .   ? 21.31359 66.51023 -2.68804  1.000 57.04525  ? 814 HOH B O   1 
HETATM 1695 O  O   . HOH K 6 .   ? 12.91464 63.88965 2.80879   1.000 48.23725  ? 815 HOH B O   1 
HETATM 1696 O  O   . HOH K 6 .   ? 23.98912 64.01501 4.90296   1.000 72.86008  ? 816 HOH B O   1 
HETATM 1697 O  O   . HOH K 6 .   ? 18.18244 53.59405 -6.73305  1.000 44.07447  ? 817 HOH B O   1 
HETATM 1698 O  O   . HOH K 6 .   ? 8.12260  56.31351 3.89832   1.000 36.31323  ? 818 HOH B O   1 
HETATM 1699 O  O   . HOH K 6 .   ? 11.27335 48.76411 11.00532  1.000 42.48562  ? 819 HOH B O   1 
HETATM 1700 O  O   . HOH K 6 .   ? 6.85553  51.87377 0.81287   1.000 35.24113  ? 820 HOH B O   1 
HETATM 1701 O  O   . HOH K 6 .   ? 17.65931 50.61548 20.08338  1.000 46.83502  ? 821 HOH B O   1 
HETATM 1702 O  O   . HOH K 6 .   ? 11.74651 49.27836 -5.91881  1.000 47.59996  ? 822 HOH B O   1 
HETATM 1703 O  O   . HOH K 6 .   ? 21.20403 66.82844 6.35928   1.000 58.04817  ? 823 HOH B O   1 
HETATM 1704 O  O   . HOH K 6 .   ? 15.07257 61.30955 -9.00394  1.000 46.13910  ? 824 HOH B O   1 
HETATM 1705 O  O   . HOH K 6 .   ? 5.92997  54.32942 1.13532   1.000 34.55111  ? 825 HOH B O   1 
HETATM 1706 O  O   . HOH K 6 .   ? 18.73453 57.10469 -6.82573  1.000 52.18610  ? 826 HOH B O   1 
HETATM 1707 O  O   . HOH K 6 .   ? 4.03404  55.07743 -6.03617  1.000 50.63634  ? 827 HOH B O   1 
HETATM 1708 O  O   . HOH K 6 .   ? 18.10507 54.85087 15.24483  1.000 40.71117  ? 828 HOH B O   1 
HETATM 1709 O  O   . HOH K 6 .   ? 14.79230 57.06821 20.35353  1.000 51.30751  ? 829 HOH B O   1 
HETATM 1710 O  O   . HOH K 6 .   ? 11.114   58.899   30.434    1.000 49.67694  ? 830 HOH B O   1 
HETATM 1711 O  O   . HOH K 6 .   ? 11.735   49.981   29.619    1.000 45.07398  ? 831 HOH B O   1 
HETATM 1712 O  O   . HOH K 6 .   ? 9.71410  58.07742 7.97643   1.000 37.19196  ? 832 HOH B O   1 
HETATM 1713 O  O   . HOH K 6 .   ? 13.67751 46.69778 -7.11420  1.000 38.53366  ? 833 HOH B O   1 
HETATM 1714 O  O   . HOH K 6 .   ? 18.34913 52.25190 27.56442  1.000 59.09071  ? 834 HOH B O   1 
HETATM 1715 O  O   . HOH K 6 .   ? 19.39563 63.67678 5.58641   1.000 58.87660  ? 835 HOH B O   1 
HETATM 1716 O  O   . HOH K 6 .   ? 11.15536 55.70868 15.73235  1.000 44.70344  ? 836 HOH B O   1 
HETATM 1717 O  O   . HOH K 6 .   ? 16.73319 50.99092 -6.07648  1.000 42.15298  ? 837 HOH B O   1 
HETATM 1718 O  O   . HOH K 6 .   ? 17.16134 59.63286 26.64309  1.000 58.55166  ? 838 HOH B O   1 
HETATM 1719 O  O   . HOH K 6 .   ? 8.52225  50.78220 -10.39006 1.000 43.86901  ? 839 HOH B O   1 
HETATM 1720 O  O   . HOH K 6 .   ? 14.90832 64.86279 33.37761  1.000 39.24062  ? 840 HOH B O   1 
HETATM 1721 O  O   . HOH K 6 .   ? 10.38649 56.43143 18.61337  1.000 50.35105  ? 841 HOH B O   1 
HETATM 1722 O  O   . HOH K 6 .   ? 12.15150 66.39504 1.71643   1.000 29.05596  ? 842 HOH B O   1 
HETATM 1723 O  O   . HOH K 6 .   ? 22.55496 57.15200 0.15843   1.000 55.74483  ? 843 HOH B O   1 
HETATM 1724 O  O   . HOH K 6 .   ? 18.41169 54.70900 18.01287  1.000 45.68758  ? 844 HOH B O   1 
HETATM 1725 O  O   . HOH K 6 .   ? 19.85202 70.24289 3.00431   1.000 50.07844  ? 845 HOH B O   1 
HETATM 1726 O  O   . HOH K 6 .   ? 14.69626 57.27738 13.37165  1.000 48.30185  ? 846 HOH B O   1 
HETATM 1727 O  O   . HOH K 6 .   ? 17.645   71.070   6.874     1.000 43.16937  ? 847 HOH B O   1 
HETATM 1728 O  O   . HOH K 6 .   ? 15.20841 57.68060 22.87468  1.000 50.28171  ? 848 HOH B O   1 
HETATM 1729 O  O   . HOH K 6 .   ? 14.10865 63.84813 5.01502   1.000 54.46793  ? 849 HOH B O   1 
HETATM 1730 O  O   . HOH K 6 .   ? 21.04638 56.00514 -5.37486  1.000 49.48015  ? 850 HOH B O   1 
HETATM 1731 O  O   . HOH K 6 .   ? 17.32118 57.64703 14.52133  1.000 55.40276  ? 851 HOH B O   1 
HETATM 1732 O  O   . HOH K 6 .   ? 16.08629 58.17661 11.33176  1.000 48.41699  ? 852 HOH B O   1 
HETATM 1733 O  O   . HOH K 6 .   ? 21.568   68.352   -0.921    1.000 50.62087  ? 853 HOH B O   1 
HETATM 1734 O  O   . HOH K 6 .   ? 17.27987 56.92411 19.33249  1.000 51.71292  ? 854 HOH B O   1 
HETATM 1735 O  O   . HOH K 6 .   ? 12.25780 57.46709 14.22462  1.000 41.13360  ? 855 HOH B O   1 
# 
