data_9HHB
# 
_entry.id   9HHB 
# 
_audit_conform.dict_name       mmcif_pdbx.dic 
_audit_conform.dict_version    5.404 
_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   9HHB         pdb_00009hhb 10.2210/pdb9hhb/pdb 
WWPDB D_1292143301 ?            ?                   
# 
loop_
_pdbx_audit_revision_history.ordinal 
_pdbx_audit_revision_history.data_content_type 
_pdbx_audit_revision_history.major_revision 
_pdbx_audit_revision_history.minor_revision 
_pdbx_audit_revision_history.revision_date 
_pdbx_audit_revision_history.part_number 
1 'Structure model' 1 0 2025-04-02 ? 
2 'Structure model' 1 1 2025-04-16 ? 
3 'Structure model' 1 2 2025-06-11 ? 
# 
_pdbx_audit_revision_details.ordinal             1 
_pdbx_audit_revision_details.revision_ordinal    1 
_pdbx_audit_revision_details.data_content_type   'Structure model' 
_pdbx_audit_revision_details.provider            repository 
_pdbx_audit_revision_details.type                'Initial release' 
_pdbx_audit_revision_details.description         ? 
_pdbx_audit_revision_details.details             ? 
# 
loop_
_pdbx_audit_revision_group.ordinal 
_pdbx_audit_revision_group.revision_ordinal 
_pdbx_audit_revision_group.data_content_type 
_pdbx_audit_revision_group.group 
1 2 'Structure model' 'Database references' 
2 3 'Structure model' 'Database references' 
# 
loop_
_pdbx_audit_revision_category.ordinal 
_pdbx_audit_revision_category.revision_ordinal 
_pdbx_audit_revision_category.data_content_type 
_pdbx_audit_revision_category.category 
1 2 'Structure model' citation        
2 2 'Structure model' citation_author 
3 3 'Structure model' citation        
# 
loop_
_pdbx_audit_revision_item.ordinal 
_pdbx_audit_revision_item.revision_ordinal 
_pdbx_audit_revision_item.data_content_type 
_pdbx_audit_revision_item.item 
1 2 'Structure model' '_citation.page_first'              
2 2 'Structure model' '_citation.page_last'               
3 2 'Structure model' '_citation.title'                   
4 2 'Structure model' '_citation_author.identifier_ORCID' 
5 3 'Structure model' '_citation.journal_volume'          
6 3 'Structure model' '_citation.page_first'              
7 3 'Structure model' '_citation.page_last'               
# 
_pdbx_database_status.status_code                     REL 
_pdbx_database_status.status_code_sf                  REL 
_pdbx_database_status.status_code_mr                  ? 
_pdbx_database_status.entry_id                        9HHB 
_pdbx_database_status.recvd_initial_deposition_date   2024-11-21 
_pdbx_database_status.SG_entry                        N 
_pdbx_database_status.deposit_site                    PDBE 
_pdbx_database_status.process_site                    PDBE 
_pdbx_database_status.status_code_cs                  ? 
_pdbx_database_status.status_code_nmr_data            ? 
_pdbx_database_status.methods_development_category    ? 
_pdbx_database_status.pdb_format_compatible           N 
# 
_pdbx_database_related.db_name        PDB 
_pdbx_database_related.details        . 
_pdbx_database_related.db_id          9HGF 
_pdbx_database_related.content_type   unspecified 
# 
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 
3 Oliver.Einsle@BIOCHEMIE.uni-freiburg.de   Oliver Einsle   ? 'principal investigator/group leader' 0000-0001-8722-2893 
4 stefan.guenther@pharmazie.uni-freiburg.de Stefan Guenther ? 'principal investigator/group leader' 0000-0003-3744-189X 
# 
loop_
_audit_author.name 
_audit_author.pdbx_ordinal 
_audit_author.identifier_ORCID 
'Amann, M.'    1 0000-0001-7594-3810 
'Huegle, M.'   2 0000-0002-2830-7130 
'Einsle, O.'   3 0000-0001-8722-2893 
'Guenther, S.' 4 0000-0003-3744-189X 
# 
_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                   DE 
_citation.database_id_Medline       ? 
_citation.details                   ? 
_citation.id                        primary 
_citation.journal_abbrev            Chemmedchem 
_citation.journal_id_ASTM           ? 
_citation.journal_id_CSD            ? 
_citation.journal_id_ISSN           1860-7187 
_citation.journal_full              ? 
_citation.journal_issue             ? 
_citation.journal_volume            20 
_citation.language                  ? 
_citation.page_first                e202500024 
_citation.page_last                 e202500024 
_citation.title                     
'A Novel Inhibitor against the Bromodomain Protein 1 of the Malaria Pathogen Plasmodium Falciparum.' 
_citation.year                      2025 
_citation.database_id_CSD           ? 
_citation.pdbx_database_id_DOI      10.1002/cmdc.202500024 
_citation.pdbx_database_id_PubMed   40099623 
_citation.pdbx_database_id_patent   ? 
_citation.unpublished_flag          ? 
# 
loop_
_citation_author.citation_id 
_citation_author.name 
_citation_author.ordinal 
_citation_author.identifier_ORCID 
primary 'Amann, M.'        1  0000-0001-7594-3810 
primary 'Warstat, R.'      2  ?                   
primary 'Rechten, K.K.'    3  ?                   
primary 'Theuer, P.'       4  ?                   
primary 'Schustereder, M.' 5  ?                   
primary 'Clavey, S.'       6  ?                   
primary 'Breit, B.'        7  0000-0002-2514-3898 
primary 'Einsle, O.'       8  0000-0001-8722-2893 
primary 'Hugle, M.'        9  0000-0002-2830-7130 
primary 'Petter, M.'       10 0000-0002-1837-2756 
primary 'Gunther, S.'      11 0000-0003-3744-189X 
# 
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 'Bromo domain-containing protein' 15163.188 1  ? ? ? ? 
2 non-polymer syn 'SULFATE ION' 96.063    1  ? ? ? ? 
3 non-polymer syn 
'~{N}-[2-methyl-3-(3-methyl-4-oxidanylidene-5,6,7,8-tetrahydro-2~{H}-cyclohepta[c]pyrrol-1-yl)phenyl]methanesulfonamide' 346.444   
1  ? ? ? ? 
4 water       nat water 18.015    55 ? ? ? ? 
# 
_entity_poly.entity_id                      1 
_entity_poly.type                           'polypeptide(L)' 
_entity_poly.nstd_linkage                   no 
_entity_poly.nstd_monomer                   no 
_entity_poly.pdbx_seq_one_letter_code       
;SFNKQWYLLANQIIQSLSKYEGGHIFEKLVDAKKQNCPDYYDVIKNPMSFSCVKTKLKKGQYGLPTEFIKDVQLIFDNCS
LYNTSGSLVAITGKNIEAYFNNQLIVTGYNNFVTKANTINERLQKVEDENLE
;
_entity_poly.pdbx_seq_one_letter_code_can   
;SFNKQWYLLANQIIQSLSKYEGGHIFEKLVDAKKQNCPDYYDVIKNPMSFSCVKTKLKKGQYGLPTEFIKDVQLIFDNCS
LYNTSGSLVAITGKNIEAYFNNQLIVTGYNNFVTKANTINERLQKVEDENLE
;
_entity_poly.pdbx_strand_id                 A 
_entity_poly.pdbx_target_identifier         ? 
# 
loop_
_pdbx_entity_nonpoly.entity_id 
_pdbx_entity_nonpoly.name 
_pdbx_entity_nonpoly.comp_id 
2 'SULFATE ION'                                                                                                            SO4   
3 '~{N}-[2-methyl-3-(3-methyl-4-oxidanylidene-5,6,7,8-tetrahydro-2~{H}-cyclohepta[c]pyrrol-1-yl)phenyl]methanesulfonamide' A1IUY 
4 water                                                                                                                    HOH   
# 
loop_
_entity_poly_seq.entity_id 
_entity_poly_seq.num 
_entity_poly_seq.mon_id 
_entity_poly_seq.hetero 
1 1   SER n 
1 2   PHE n 
1 3   ASN n 
1 4   LYS n 
1 5   GLN n 
1 6   TRP n 
1 7   TYR n 
1 8   LEU n 
1 9   LEU n 
1 10  ALA n 
1 11  ASN n 
1 12  GLN n 
1 13  ILE n 
1 14  ILE n 
1 15  GLN n 
1 16  SER n 
1 17  LEU n 
1 18  SER n 
1 19  LYS n 
1 20  TYR n 
1 21  GLU n 
1 22  GLY n 
1 23  GLY n 
1 24  HIS n 
1 25  ILE n 
1 26  PHE n 
1 27  GLU n 
1 28  LYS n 
1 29  LEU n 
1 30  VAL n 
1 31  ASP n 
1 32  ALA n 
1 33  LYS n 
1 34  LYS n 
1 35  GLN n 
1 36  ASN n 
1 37  CYS n 
1 38  PRO n 
1 39  ASP n 
1 40  TYR n 
1 41  TYR n 
1 42  ASP n 
1 43  VAL n 
1 44  ILE n 
1 45  LYS n 
1 46  ASN n 
1 47  PRO n 
1 48  MET n 
1 49  SER n 
1 50  PHE n 
1 51  SER n 
1 52  CYS n 
1 53  VAL n 
1 54  LYS n 
1 55  THR n 
1 56  LYS n 
1 57  LEU n 
1 58  LYS n 
1 59  LYS n 
1 60  GLY n 
1 61  GLN n 
1 62  TYR n 
1 63  GLY n 
1 64  LEU n 
1 65  PRO n 
1 66  THR n 
1 67  GLU n 
1 68  PHE n 
1 69  ILE n 
1 70  LYS n 
1 71  ASP n 
1 72  VAL n 
1 73  GLN n 
1 74  LEU n 
1 75  ILE n 
1 76  PHE n 
1 77  ASP n 
1 78  ASN n 
1 79  CYS n 
1 80  SER n 
1 81  LEU n 
1 82  TYR n 
1 83  ASN n 
1 84  THR n 
1 85  SER n 
1 86  GLY n 
1 87  SER n 
1 88  LEU n 
1 89  VAL n 
1 90  ALA n 
1 91  ILE n 
1 92  THR n 
1 93  GLY n 
1 94  LYS n 
1 95  ASN n 
1 96  ILE n 
1 97  GLU n 
1 98  ALA n 
1 99  TYR n 
1 100 PHE n 
1 101 ASN n 
1 102 ASN n 
1 103 GLN n 
1 104 LEU n 
1 105 ILE n 
1 106 VAL n 
1 107 THR n 
1 108 GLY n 
1 109 TYR n 
1 110 ASN n 
1 111 ASN n 
1 112 PHE n 
1 113 VAL n 
1 114 THR n 
1 115 LYS n 
1 116 ALA n 
1 117 ASN n 
1 118 THR n 
1 119 ILE n 
1 120 ASN n 
1 121 GLU n 
1 122 ARG n 
1 123 LEU n 
1 124 GLN n 
1 125 LYS n 
1 126 VAL n 
1 127 GLU n 
1 128 ASP n 
1 129 GLU n 
1 130 ASN n 
1 131 LEU n 
1 132 GLU n 
# 
_entity_src_gen.entity_id                          1 
_entity_src_gen.pdbx_src_id                        1 
_entity_src_gen.pdbx_alt_source_flag               sample 
_entity_src_gen.pdbx_seq_type                      'Biological sequence' 
_entity_src_gen.pdbx_beg_seq_num                   1 
_entity_src_gen.pdbx_end_seq_num                   132 
_entity_src_gen.gene_src_common_name               'malaria parasite P. vivax' 
_entity_src_gen.gene_src_genus                     ? 
_entity_src_gen.pdbx_gene_src_gene                 PVX_111040 
_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      'Plasmodium vivax' 
_entity_src_gen.pdbx_gene_src_ncbi_taxonomy_id     5855 
_entity_src_gen.pdbx_gene_src_variant              ? 
_entity_src_gen.pdbx_gene_src_cell_line            ? 
_entity_src_gen.pdbx_gene_src_atcc                 ? 
_entity_src_gen.pdbx_gene_src_organ                ? 
_entity_src_gen.pdbx_gene_src_organelle            ? 
_entity_src_gen.pdbx_gene_src_cell                 ? 
_entity_src_gen.pdbx_gene_src_cellular_location    ? 
_entity_src_gen.host_org_common_name               ? 
_entity_src_gen.pdbx_host_org_scientific_name      'Escherichia coli' 
_entity_src_gen.pdbx_host_org_ncbi_taxonomy_id     562 
_entity_src_gen.host_org_genus                     ? 
_entity_src_gen.pdbx_host_org_gene                 ? 
_entity_src_gen.pdbx_host_org_organ                ? 
_entity_src_gen.host_org_species                   ? 
_entity_src_gen.pdbx_host_org_tissue               ? 
_entity_src_gen.pdbx_host_org_tissue_fraction      ? 
_entity_src_gen.pdbx_host_org_strain               ? 
_entity_src_gen.pdbx_host_org_variant              ? 
_entity_src_gen.pdbx_host_org_cell_line            ? 
_entity_src_gen.pdbx_host_org_atcc                 ? 
_entity_src_gen.pdbx_host_org_culture_collection   ? 
_entity_src_gen.pdbx_host_org_cell                 ? 
_entity_src_gen.pdbx_host_org_organelle            ? 
_entity_src_gen.pdbx_host_org_cellular_location    ? 
_entity_src_gen.pdbx_host_org_vector_type          ? 
_entity_src_gen.pdbx_host_org_vector               ? 
_entity_src_gen.host_org_details                   ? 
_entity_src_gen.expression_system_id               ? 
_entity_src_gen.plasmid_name                       ? 
_entity_src_gen.plasmid_details                    ? 
_entity_src_gen.pdbx_description                   ? 
# 
loop_
_chem_comp.id 
_chem_comp.type 
_chem_comp.mon_nstd_flag 
_chem_comp.name 
_chem_comp.pdbx_synonyms 
_chem_comp.formula 
_chem_comp.formula_weight 
A1IUY non-polymer         . 
'~{N}-[2-methyl-3-(3-methyl-4-oxidanylidene-5,6,7,8-tetrahydro-2~{H}-cyclohepta[c]pyrrol-1-yl)phenyl]methanesulfonamide' ? 
'C18 H22 N2 O3 S' 346.444 
ALA   'L-peptide linking' y ALANINE ? 'C3 H7 N O2'      89.093  
ARG   'L-peptide linking' y ARGININE ? 'C6 H15 N4 O2 1'  175.209 
ASN   'L-peptide linking' y ASPARAGINE ? 'C4 H8 N2 O3'     132.118 
ASP   'L-peptide linking' y 'ASPARTIC ACID' ? 'C4 H7 N O4'      133.103 
CYS   'L-peptide linking' y CYSTEINE ? 'C3 H7 N O2 S'    121.158 
GLN   'L-peptide linking' y GLUTAMINE ? 'C5 H10 N2 O3'    146.144 
GLU   'L-peptide linking' y 'GLUTAMIC ACID' ? 'C5 H9 N O4'      147.129 
GLY   'peptide linking'   y GLYCINE ? 'C2 H5 N O2'      75.067  
HIS   'L-peptide linking' y HISTIDINE ? 'C6 H10 N3 O2 1'  156.162 
HOH   non-polymer         . WATER ? 'H2 O'            18.015  
ILE   'L-peptide linking' y ISOLEUCINE ? 'C6 H13 N O2'     131.173 
LEU   'L-peptide linking' y LEUCINE ? 'C6 H13 N O2'     131.173 
LYS   'L-peptide linking' y LYSINE ? 'C6 H15 N2 O2 1'  147.195 
MET   'L-peptide linking' y METHIONINE ? 'C5 H11 N O2 S'   149.211 
PHE   'L-peptide linking' y PHENYLALANINE ? 'C9 H11 N O2'     165.189 
PRO   'L-peptide linking' y PROLINE ? 'C5 H9 N O2'      115.130 
SER   'L-peptide linking' y SERINE ? 'C3 H7 N O3'      105.093 
SO4   non-polymer         . 'SULFATE ION' ? 'O4 S -2'         96.063  
THR   'L-peptide linking' y THREONINE ? 'C4 H9 N O3'      119.119 
TRP   'L-peptide linking' y TRYPTOPHAN ? 'C11 H12 N2 O2'   204.225 
TYR   'L-peptide linking' y TYROSINE ? 'C9 H11 N O3'     181.189 
VAL   'L-peptide linking' y VALINE ? 'C5 H11 N O2'     117.146 
# 
loop_
_pdbx_poly_seq_scheme.asym_id 
_pdbx_poly_seq_scheme.entity_id 
_pdbx_poly_seq_scheme.seq_id 
_pdbx_poly_seq_scheme.mon_id 
_pdbx_poly_seq_scheme.ndb_seq_num 
_pdbx_poly_seq_scheme.pdb_seq_num 
_pdbx_poly_seq_scheme.auth_seq_num 
_pdbx_poly_seq_scheme.pdb_mon_id 
_pdbx_poly_seq_scheme.auth_mon_id 
_pdbx_poly_seq_scheme.pdb_strand_id 
_pdbx_poly_seq_scheme.pdb_ins_code 
_pdbx_poly_seq_scheme.hetero 
A 1 1   SER 1   1   1   SER SER A . n 
A 1 2   PHE 2   2   2   PHE PHE A . n 
A 1 3   ASN 3   3   3   ASN ASN A . n 
A 1 4   LYS 4   4   4   LYS LYS A . n 
A 1 5   GLN 5   5   5   GLN GLN A . n 
A 1 6   TRP 6   6   6   TRP TRP A . n 
A 1 7   TYR 7   7   7   TYR TYR A . n 
A 1 8   LEU 8   8   8   LEU LEU A . n 
A 1 9   LEU 9   9   9   LEU LEU A . n 
A 1 10  ALA 10  10  10  ALA ALA A . n 
A 1 11  ASN 11  11  11  ASN ASN A . n 
A 1 12  GLN 12  12  12  GLN GLN A . n 
A 1 13  ILE 13  13  13  ILE ILE A . n 
A 1 14  ILE 14  14  14  ILE ILE A . n 
A 1 15  GLN 15  15  15  GLN GLN A . n 
A 1 16  SER 16  16  16  SER SER A . n 
A 1 17  LEU 17  17  17  LEU LEU A . n 
A 1 18  SER 18  18  18  SER SER A . n 
A 1 19  LYS 19  19  19  LYS LYS A . n 
A 1 20  TYR 20  20  20  TYR TYR A . n 
A 1 21  GLU 21  21  21  GLU GLU A . n 
A 1 22  GLY 22  22  22  GLY GLY A . n 
A 1 23  GLY 23  23  23  GLY GLY A . n 
A 1 24  HIS 24  24  24  HIS HIS A . n 
A 1 25  ILE 25  25  25  ILE ILE A . n 
A 1 26  PHE 26  26  26  PHE PHE A . n 
A 1 27  GLU 27  27  27  GLU GLU A . n 
A 1 28  LYS 28  28  28  LYS LYS A . n 
A 1 29  LEU 29  29  29  LEU LEU A . n 
A 1 30  VAL 30  30  30  VAL VAL A . n 
A 1 31  ASP 31  31  31  ASP ASP A . n 
A 1 32  ALA 32  32  32  ALA ALA A . n 
A 1 33  LYS 33  33  33  LYS LYS A . n 
A 1 34  LYS 34  34  34  LYS LYS A . n 
A 1 35  GLN 35  35  35  GLN GLN A . n 
A 1 36  ASN 36  36  36  ASN ASN A . n 
A 1 37  CYS 37  37  37  CYS CYS A . n 
A 1 38  PRO 38  38  38  PRO PRO A . n 
A 1 39  ASP 39  39  39  ASP ASP A . n 
A 1 40  TYR 40  40  40  TYR TYR A . n 
A 1 41  TYR 41  41  41  TYR TYR A . n 
A 1 42  ASP 42  42  42  ASP ASP A . n 
A 1 43  VAL 43  43  43  VAL VAL A . n 
A 1 44  ILE 44  44  44  ILE ILE A . n 
A 1 45  LYS 45  45  45  LYS LYS A . n 
A 1 46  ASN 46  46  46  ASN ASN A . n 
A 1 47  PRO 47  47  47  PRO PRO A . n 
A 1 48  MET 48  48  48  MET MET A . n 
A 1 49  SER 49  49  49  SER SER A . n 
A 1 50  PHE 50  50  50  PHE PHE A . n 
A 1 51  SER 51  51  51  SER SER A . n 
A 1 52  CYS 52  52  52  CYS CYS A . n 
A 1 53  VAL 53  53  53  VAL VAL A . n 
A 1 54  LYS 54  54  54  LYS LYS A . n 
A 1 55  THR 55  55  55  THR THR A . n 
A 1 56  LYS 56  56  56  LYS LYS A . n 
A 1 57  LEU 57  57  57  LEU LEU A . n 
A 1 58  LYS 58  58  58  LYS LYS A . n 
A 1 59  LYS 59  59  59  LYS LYS A . n 
A 1 60  GLY 60  60  60  GLY GLY A . n 
A 1 61  GLN 61  61  61  GLN GLN A . n 
A 1 62  TYR 62  62  62  TYR TYR A . n 
A 1 63  GLY 63  63  63  GLY GLY A . n 
A 1 64  LEU 64  64  64  LEU LEU A . n 
A 1 65  PRO 65  65  65  PRO PRO A . n 
A 1 66  THR 66  66  66  THR THR A . n 
A 1 67  GLU 67  67  67  GLU GLU A . n 
A 1 68  PHE 68  68  68  PHE PHE A . n 
A 1 69  ILE 69  69  69  ILE ILE A . n 
A 1 70  LYS 70  70  70  LYS LYS A . n 
A 1 71  ASP 71  71  71  ASP ASP A . n 
A 1 72  VAL 72  72  72  VAL VAL A . n 
A 1 73  GLN 73  73  73  GLN GLN A . n 
A 1 74  LEU 74  74  74  LEU LEU A . n 
A 1 75  ILE 75  75  75  ILE ILE A . n 
A 1 76  PHE 76  76  76  PHE PHE A . n 
A 1 77  ASP 77  77  77  ASP ASP A . n 
A 1 78  ASN 78  78  78  ASN ASN A . n 
A 1 79  CYS 79  79  79  CYS CYS A . n 
A 1 80  SER 80  80  80  SER SER A . n 
A 1 81  LEU 81  81  81  LEU LEU A . n 
A 1 82  TYR 82  82  82  TYR TYR A . n 
A 1 83  ASN 83  83  83  ASN ASN A . n 
A 1 84  THR 84  84  84  THR THR A . n 
A 1 85  SER 85  85  85  SER SER A . n 
A 1 86  GLY 86  86  86  GLY GLY A . n 
A 1 87  SER 87  87  87  SER SER A . n 
A 1 88  LEU 88  88  88  LEU LEU A . n 
A 1 89  VAL 89  89  89  VAL VAL A . n 
A 1 90  ALA 90  90  90  ALA ALA A . n 
A 1 91  ILE 91  91  91  ILE ILE A . n 
A 1 92  THR 92  92  92  THR THR A . n 
A 1 93  GLY 93  93  93  GLY GLY A . n 
A 1 94  LYS 94  94  94  LYS LYS A . n 
A 1 95  ASN 95  95  95  ASN ASN A . n 
A 1 96  ILE 96  96  96  ILE ILE A . n 
A 1 97  GLU 97  97  97  GLU GLU A . n 
A 1 98  ALA 98  98  98  ALA ALA A . n 
A 1 99  TYR 99  99  99  TYR TYR A . n 
A 1 100 PHE 100 100 100 PHE PHE A . n 
A 1 101 ASN 101 101 101 ASN ASN A . n 
A 1 102 ASN 102 102 102 ASN ASN A . n 
A 1 103 GLN 103 103 103 GLN GLN A . n 
A 1 104 LEU 104 104 104 LEU LEU A . n 
A 1 105 ILE 105 105 105 ILE ILE A . n 
A 1 106 VAL 106 106 106 VAL VAL A . n 
A 1 107 THR 107 107 107 THR THR A . n 
A 1 108 GLY 108 108 108 GLY GLY A . n 
A 1 109 TYR 109 109 109 TYR TYR A . n 
A 1 110 ASN 110 110 110 ASN ASN A . n 
A 1 111 ASN 111 111 111 ASN ASN A . n 
A 1 112 PHE 112 112 112 PHE PHE A . n 
A 1 113 VAL 113 113 113 VAL VAL A . n 
A 1 114 THR 114 114 114 THR THR A . n 
A 1 115 LYS 115 115 115 LYS LYS A . n 
A 1 116 ALA 116 116 116 ALA ALA A . n 
A 1 117 ASN 117 117 117 ASN ASN A . n 
A 1 118 THR 118 118 118 THR THR A . n 
A 1 119 ILE 119 119 119 ILE ILE A . n 
A 1 120 ASN 120 120 120 ASN ASN A . n 
A 1 121 GLU 121 121 ?   ?   ?   A . n 
A 1 122 ARG 122 122 ?   ?   ?   A . n 
A 1 123 LEU 123 123 ?   ?   ?   A . n 
A 1 124 GLN 124 124 ?   ?   ?   A . n 
A 1 125 LYS 125 125 ?   ?   ?   A . n 
A 1 126 VAL 126 126 ?   ?   ?   A . n 
A 1 127 GLU 127 127 ?   ?   ?   A . n 
A 1 128 ASP 128 128 ?   ?   ?   A . n 
A 1 129 GLU 129 129 ?   ?   ?   A . n 
A 1 130 ASN 130 130 ?   ?   ?   A . n 
A 1 131 LEU 131 131 ?   ?   ?   A . n 
A 1 132 GLU 132 132 ?   ?   ?   A . n 
# 
_pdbx_entity_instance_feature.ordinal        1 
_pdbx_entity_instance_feature.comp_id        A1IUY 
_pdbx_entity_instance_feature.asym_id        ? 
_pdbx_entity_instance_feature.seq_num        ? 
_pdbx_entity_instance_feature.auth_comp_id   A1IUY 
_pdbx_entity_instance_feature.auth_asym_id   ? 
_pdbx_entity_instance_feature.auth_seq_num   ? 
_pdbx_entity_instance_feature.feature_type   'SUBJECT OF INVESTIGATION' 
_pdbx_entity_instance_feature.details        ? 
# 
loop_
_pdbx_nonpoly_scheme.asym_id 
_pdbx_nonpoly_scheme.entity_id 
_pdbx_nonpoly_scheme.mon_id 
_pdbx_nonpoly_scheme.ndb_seq_num 
_pdbx_nonpoly_scheme.pdb_seq_num 
_pdbx_nonpoly_scheme.auth_seq_num 
_pdbx_nonpoly_scheme.pdb_mon_id 
_pdbx_nonpoly_scheme.auth_mon_id 
_pdbx_nonpoly_scheme.pdb_strand_id 
_pdbx_nonpoly_scheme.pdb_ins_code 
B 2 SO4   1  201 1  SO4   SO4 A . 
C 3 A1IUY 1  202 1  A1IUY 150 A . 
D 4 HOH   1  301 57 HOH   HOH A . 
D 4 HOH   2  302 43 HOH   HOH A . 
D 4 HOH   3  303 15 HOH   HOH A . 
D 4 HOH   4  304 13 HOH   HOH A . 
D 4 HOH   5  305 5  HOH   HOH A . 
D 4 HOH   6  306 6  HOH   HOH A . 
D 4 HOH   7  307 10 HOH   HOH A . 
D 4 HOH   8  308 14 HOH   HOH A . 
D 4 HOH   9  309 2  HOH   HOH A . 
D 4 HOH   10 310 12 HOH   HOH A . 
D 4 HOH   11 311 24 HOH   HOH A . 
D 4 HOH   12 312 32 HOH   HOH A . 
D 4 HOH   13 313 26 HOH   HOH A . 
D 4 HOH   14 314 7  HOH   HOH A . 
D 4 HOH   15 315 21 HOH   HOH A . 
D 4 HOH   16 316 4  HOH   HOH A . 
D 4 HOH   17 317 53 HOH   HOH A . 
D 4 HOH   18 318 17 HOH   HOH A . 
D 4 HOH   19 319 51 HOH   HOH A . 
D 4 HOH   20 320 56 HOH   HOH A . 
D 4 HOH   21 321 22 HOH   HOH A . 
D 4 HOH   22 322 20 HOH   HOH A . 
D 4 HOH   23 323 25 HOH   HOH A . 
D 4 HOH   24 324 11 HOH   HOH A . 
D 4 HOH   25 325 19 HOH   HOH A . 
D 4 HOH   26 326 28 HOH   HOH A . 
D 4 HOH   27 327 50 HOH   HOH A . 
D 4 HOH   28 328 3  HOH   HOH A . 
D 4 HOH   29 329 23 HOH   HOH A . 
D 4 HOH   30 330 18 HOH   HOH A . 
D 4 HOH   31 331 16 HOH   HOH A . 
D 4 HOH   32 332 29 HOH   HOH A . 
D 4 HOH   33 333 27 HOH   HOH A . 
D 4 HOH   34 334 9  HOH   HOH A . 
D 4 HOH   35 335 58 HOH   HOH A . 
D 4 HOH   36 336 1  HOH   HOH A . 
D 4 HOH   37 337 48 HOH   HOH A . 
D 4 HOH   38 338 52 HOH   HOH A . 
D 4 HOH   39 339 31 HOH   HOH A . 
D 4 HOH   40 340 30 HOH   HOH A . 
D 4 HOH   41 341 59 HOH   HOH A . 
D 4 HOH   42 342 46 HOH   HOH A . 
D 4 HOH   43 343 34 HOH   HOH A . 
D 4 HOH   44 344 41 HOH   HOH A . 
D 4 HOH   45 345 49 HOH   HOH A . 
D 4 HOH   46 346 35 HOH   HOH A . 
D 4 HOH   47 347 40 HOH   HOH A . 
D 4 HOH   48 348 47 HOH   HOH A . 
D 4 HOH   49 349 45 HOH   HOH A . 
D 4 HOH   50 350 38 HOH   HOH A . 
D 4 HOH   51 351 37 HOH   HOH A . 
D 4 HOH   52 352 39 HOH   HOH A . 
D 4 HOH   53 353 8  HOH   HOH A . 
D 4 HOH   54 354 55 HOH   HOH A . 
D 4 HOH   55 355 54 HOH   HOH A . 
# 
loop_
_pdbx_unobs_or_zero_occ_atoms.id 
_pdbx_unobs_or_zero_occ_atoms.PDB_model_num 
_pdbx_unobs_or_zero_occ_atoms.polymer_flag 
_pdbx_unobs_or_zero_occ_atoms.occupancy_flag 
_pdbx_unobs_or_zero_occ_atoms.auth_asym_id 
_pdbx_unobs_or_zero_occ_atoms.auth_comp_id 
_pdbx_unobs_or_zero_occ_atoms.auth_seq_id 
_pdbx_unobs_or_zero_occ_atoms.PDB_ins_code 
_pdbx_unobs_or_zero_occ_atoms.auth_atom_id 
_pdbx_unobs_or_zero_occ_atoms.label_alt_id 
_pdbx_unobs_or_zero_occ_atoms.label_asym_id 
_pdbx_unobs_or_zero_occ_atoms.label_comp_id 
_pdbx_unobs_or_zero_occ_atoms.label_seq_id 
_pdbx_unobs_or_zero_occ_atoms.label_atom_id 
1  1 Y 1 A LYS 19 ? NZ ? A LYS 19 NZ 
2  1 Y 1 A LYS 28 ? NZ ? A LYS 28 NZ 
3  1 Y 1 A LYS 33 ? CD ? A LYS 33 CD 
4  1 Y 1 A LYS 33 ? CE ? A LYS 33 CE 
5  1 Y 1 A LYS 33 ? NZ ? A LYS 33 NZ 
6  1 Y 1 A LYS 34 ? CD ? A LYS 34 CD 
7  1 Y 1 A LYS 34 ? CE ? A LYS 34 CE 
8  1 Y 1 A LYS 34 ? NZ ? A LYS 34 NZ 
9  1 Y 1 A LYS 45 ? NZ ? A LYS 45 NZ 
10 1 Y 1 A LYS 70 ? CE ? A LYS 70 CE 
11 1 Y 1 A LYS 70 ? NZ ? A LYS 70 NZ 
# 
loop_
_software.citation_id 
_software.classification 
_software.compiler_name 
_software.compiler_version 
_software.contact_author 
_software.contact_author_email 
_software.date 
_software.description 
_software.dependencies 
_software.hardware 
_software.language 
_software.location 
_software.mods 
_software.name 
_software.os 
_software.os_version 
_software.type 
_software.version 
_software.pdbx_ordinal 
? refinement       ? ? ? ? ? ? ? ? ? ? ? PHENIX  ? ? ? 1.21_5207 1 
? 'data scaling'   ? ? ? ? ? ? ? ? ? ? ? Aimless ? ? ? .         2 
? 'data reduction' ? ? ? ? ? ? ? ? ? ? ? XDS     ? ? ? .         3 
? phasing          ? ? ? ? ? ? ? ? ? ? ? PHASER  ? ? ? .         4 
# 
_cell.angle_alpha                  90.00 
_cell.angle_alpha_esd              ? 
_cell.angle_beta                   90.00 
_cell.angle_beta_esd               ? 
_cell.angle_gamma                  120.00 
_cell.angle_gamma_esd              ? 
_cell.entry_id                     9HHB 
_cell.details                      ? 
_cell.formula_units_Z              ? 
_cell.length_a                     92.382 
_cell.length_a_esd                 ? 
_cell.length_b                     92.382 
_cell.length_b_esd                 ? 
_cell.length_c                     69.811 
_cell.length_c_esd                 ? 
_cell.volume                       ? 
_cell.volume_esd                   ? 
_cell.Z_PDB                        12 
_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                         9HHB 
_symmetry.cell_setting                     ? 
_symmetry.Int_Tables_number                180 
_symmetry.space_group_name_Hall            ? 
_symmetry.space_group_name_H-M             'P 62 2 2' 
_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                   9HHB 
_exptl.crystals_number            1 
_exptl.details                    ? 
_exptl.method                     'X-RAY DIFFRACTION' 
_exptl.method_details             ? 
# 
_exptl_crystal.colour                       ? 
_exptl_crystal.density_diffrn               ? 
_exptl_crystal.density_Matthews             2.84 
_exptl_crystal.density_method               ? 
_exptl_crystal.density_percent_sol          56.62 
_exptl_crystal.description                  ? 
_exptl_crystal.F_000                        ? 
_exptl_crystal.id                           1 
_exptl_crystal.preparation                  ? 
_exptl_crystal.size_max                     ? 
_exptl_crystal.size_mid                     ? 
_exptl_crystal.size_min                     ? 
_exptl_crystal.size_rad                     ? 
_exptl_crystal.colour_lustre                ? 
_exptl_crystal.colour_modifier              ? 
_exptl_crystal.colour_primary               ? 
_exptl_crystal.density_meas                 ? 
_exptl_crystal.density_meas_esd             ? 
_exptl_crystal.density_meas_gt              ? 
_exptl_crystal.density_meas_lt              ? 
_exptl_crystal.density_meas_temp            ? 
_exptl_crystal.density_meas_temp_esd        ? 
_exptl_crystal.density_meas_temp_gt         ? 
_exptl_crystal.density_meas_temp_lt         ? 
_exptl_crystal.pdbx_crystal_image_url       ? 
_exptl_crystal.pdbx_crystal_image_format    ? 
_exptl_crystal.pdbx_mosaicity               ? 
_exptl_crystal.pdbx_mosaicity_esd           ? 
_exptl_crystal.pdbx_mosaic_method           ? 
_exptl_crystal.pdbx_mosaic_block_size       ? 
_exptl_crystal.pdbx_mosaic_block_size_esd   ? 
# 
_exptl_crystal_grow.apparatus       ? 
_exptl_crystal_grow.atmosphere      ? 
_exptl_crystal_grow.crystal_id      1 
_exptl_crystal_grow.details         ? 
_exptl_crystal_grow.method          'VAPOR DIFFUSION, SITTING DROP' 
_exptl_crystal_grow.method_ref      ? 
_exptl_crystal_grow.pH              ? 
_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    '35% PEG3350, 0.4 M LiSO4, Tris pH 8,2' 
_exptl_crystal_grow.pdbx_pH_range   ? 
_exptl_crystal_grow.temp            277 
# 
_diffrn.ambient_environment              ? 
_diffrn.ambient_temp                     100 
_diffrn.ambient_temp_details             ? 
_diffrn.ambient_temp_esd                 ? 
_diffrn.crystal_id                       1 
_diffrn.crystal_support                  ? 
_diffrn.crystal_treatment                ? 
_diffrn.details                          ? 
_diffrn.id                               1 
_diffrn.ambient_pressure                 ? 
_diffrn.ambient_pressure_esd             ? 
_diffrn.ambient_pressure_gt              ? 
_diffrn.ambient_pressure_lt              ? 
_diffrn.ambient_temp_gt                  ? 
_diffrn.ambient_temp_lt                  ? 
_diffrn.pdbx_serial_crystal_experiment   N 
# 
_diffrn_detector.details                      ? 
_diffrn_detector.detector                     PIXEL 
_diffrn_detector.diffrn_id                    1 
_diffrn_detector.type                         'DECTRIS EIGER X 16M' 
_diffrn_detector.area_resol_mean              ? 
_diffrn_detector.dtime                        ? 
_diffrn_detector.pdbx_frames_total            ? 
_diffrn_detector.pdbx_collection_time_total   ? 
_diffrn_detector.pdbx_collection_date         2022-06-24 
_diffrn_detector.pdbx_frequency               ? 
_diffrn_detector.id                           ? 
_diffrn_detector.number_of_axes               ? 
# 
_diffrn_radiation.collimation                      ? 
_diffrn_radiation.diffrn_id                        1 
_diffrn_radiation.filter_edge                      ? 
_diffrn_radiation.inhomogeneity                    ? 
_diffrn_radiation.monochromator                    ? 
_diffrn_radiation.polarisn_norm                    ? 
_diffrn_radiation.polarisn_ratio                   ? 
_diffrn_radiation.probe                            ? 
_diffrn_radiation.type                             ? 
_diffrn_radiation.xray_symbol                      ? 
_diffrn_radiation.wavelength_id                    1 
_diffrn_radiation.pdbx_monochromatic_or_laue_m_l   M 
_diffrn_radiation.pdbx_wavelength_list             ? 
_diffrn_radiation.pdbx_wavelength                  ? 
_diffrn_radiation.pdbx_diffrn_protocol             'SINGLE WAVELENGTH' 
_diffrn_radiation.pdbx_analyzer                    ? 
_diffrn_radiation.pdbx_scattering_type             x-ray 
# 
_diffrn_radiation_wavelength.id           1 
_diffrn_radiation_wavelength.wavelength   0.999987 
_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                        'SLS BEAMLINE X06SA' 
_diffrn_source.voltage                     ? 
_diffrn_source.take-off_angle              ? 
_diffrn_source.pdbx_wavelength_list        0.999987 
_diffrn_source.pdbx_wavelength             ? 
_diffrn_source.pdbx_synchrotron_beamline   X06SA 
_diffrn_source.pdbx_synchrotron_site       SLS 
# 
_reflns.B_iso_Wilson_estimate                          ? 
_reflns.entry_id                                       9HHB 
_reflns.data_reduction_details                         ? 
_reflns.data_reduction_method                          ? 
_reflns.d_resolution_high                              2.26 
_reflns.d_resolution_low                               46.19 
_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                                     8689 
_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                           100.0 
_reflns.R_free_details                                 ? 
_reflns.Rmerge_F_all                                   ? 
_reflns.Rmerge_F_obs                                   ? 
_reflns.Friedel_coverage                               ? 
_reflns.number_gt                                      ? 
_reflns.threshold_expression                           ? 
_reflns.pdbx_redundancy                                38.4 
_reflns.pdbx_netI_over_av_sigmaI                       ? 
_reflns.pdbx_netI_over_sigmaI                          20.0 
_reflns.pdbx_res_netI_over_av_sigmaI_2                 ? 
_reflns.pdbx_res_netI_over_sigmaI_2                    ? 
_reflns.pdbx_chi_squared                               1.00 
_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                                0.139 
_reflns.pdbx_Rpim_I_all                                0.023 
_reflns.pdbx_d_opt                                     ? 
_reflns.pdbx_number_measured_all                       333586 
_reflns.pdbx_diffrn_id                                 1 
_reflns.pdbx_ordinal                                   1 
_reflns.pdbx_CC_half                                   0.999 
_reflns.pdbx_CC_star                                   ? 
_reflns.pdbx_R_split                                   ? 
_reflns.pdbx_Rmerge_I_obs                              0.137 
_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                                    2.26 
_reflns_shell.d_res_low                                     2.33 
_reflns_shell.meanI_over_sigI_all                           ? 
_reflns_shell.meanI_over_sigI_obs                           ? 
_reflns_shell.number_measured_all                           31733 
_reflns_shell.number_measured_obs                           ? 
_reflns_shell.number_possible                               ? 
_reflns_shell.number_unique_all                             ? 
_reflns_shell.number_unique_obs                             778 
_reflns_shell.percent_possible_obs                          100.0 
_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                               40.8 
_reflns_shell.pdbx_chi_squared                              1.02 
_reflns_shell.pdbx_netI_over_sigmaI_all                     ? 
_reflns_shell.pdbx_netI_over_sigmaI_obs                     5.6 
_reflns_shell.pdbx_Rrim_I_all                               0.977 
_reflns_shell.pdbx_Rpim_I_all                               0.153 
_reflns_shell.pdbx_rejects                                  ? 
_reflns_shell.pdbx_ordinal                                  1 
_reflns_shell.pdbx_diffrn_id                                1 
_reflns_shell.pdbx_CC_half                                  0.975 
_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                                  0.965 
_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                               ? 
_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                                 9HHB 
_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                            2.26 
_refine.ls_d_res_low                             46.19 
_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                     8653 
_refine.ls_number_reflns_R_free                  428 
_refine.ls_number_reflns_R_work                  ? 
_refine.ls_number_restraints                     ? 
_refine.ls_percent_reflns_obs                    99.78 
_refine.ls_percent_reflns_R_free                 4.95 
_refine.ls_R_factor_all                          ? 
_refine.ls_R_factor_obs                          0.2187 
_refine.ls_R_factor_R_free                       0.2687 
_refine.ls_R_factor_R_free_error                 ? 
_refine.ls_R_factor_R_free_error_details         ? 
_refine.ls_R_factor_R_work                       0.2163 
_refine.ls_R_Fsqd_factor_obs                     ? 
_refine.ls_R_I_factor_obs                        ? 
_refine.ls_redundancy_reflns_all                 ? 
_refine.ls_redundancy_reflns_obs                 ? 
_refine.ls_restrained_S_all                      ? 
_refine.ls_restrained_S_obs                      ? 
_refine.ls_shift_over_esd_max                    ? 
_refine.ls_shift_over_esd_mean                   ? 
_refine.ls_structure_factor_coef                 ? 
_refine.ls_weighting_details                     ? 
_refine.ls_weighting_scheme                      ? 
_refine.ls_wR_factor_all                         ? 
_refine.ls_wR_factor_obs                         ? 
_refine.ls_wR_factor_R_free                      ? 
_refine.ls_wR_factor_R_work                      ? 
_refine.occupancy_max                            ? 
_refine.occupancy_min                            ? 
_refine.solvent_model_details                    'FLAT BULK SOLVENT MODEL' 
_refine.solvent_model_param_bsol                 ? 
_refine.solvent_model_param_ksol                 ? 
_refine.pdbx_R_complete                          ? 
_refine.ls_R_factor_gt                           ? 
_refine.ls_goodness_of_fit_gt                    ? 
_refine.ls_goodness_of_fit_ref                   ? 
_refine.ls_shift_over_su_max                     ? 
_refine.ls_shift_over_su_max_lt                  ? 
_refine.ls_shift_over_su_mean                    ? 
_refine.ls_shift_over_su_mean_lt                 ? 
_refine.pdbx_ls_sigma_I                          ? 
_refine.pdbx_ls_sigma_F                          1.34 
_refine.pdbx_ls_sigma_Fsqd                       ? 
_refine.pdbx_data_cutoff_high_absF               ? 
_refine.pdbx_data_cutoff_high_rms_absF           ? 
_refine.pdbx_data_cutoff_low_absF                ? 
_refine.pdbx_isotropic_thermal_model             ? 
_refine.pdbx_ls_cross_valid_method               'FREE R-VALUE' 
_refine.pdbx_method_to_determine_struct          'MOLECULAR REPLACEMENT' 
_refine.pdbx_starting_model                      ? 
_refine.pdbx_stereochemistry_target_values       ML 
_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             1.10 
_refine.pdbx_solvent_ion_probe_radii             ? 
_refine.pdbx_solvent_shrinkage_radii             0.90 
_refine.pdbx_real_space_R                        ? 
_refine.pdbx_density_correlation                 ? 
_refine.pdbx_pd_number_of_powder_patterns        ? 
_refine.pdbx_pd_number_of_points                 ? 
_refine.pdbx_pd_meas_number_of_points            ? 
_refine.pdbx_pd_proc_ls_prof_R_factor            ? 
_refine.pdbx_pd_proc_ls_prof_wR_factor           ? 
_refine.pdbx_pd_Marquardt_correlation_coeff      ? 
_refine.pdbx_pd_Fsqrd_R_factor                   ? 
_refine.pdbx_pd_ls_matrix_band_width             ? 
_refine.pdbx_overall_phase_error                 35.55 
_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                            0.35 
_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.pdbx_number_atoms_protein        952 
_refine_hist.pdbx_number_atoms_nucleic_acid   0 
_refine_hist.pdbx_number_atoms_ligand         29 
_refine_hist.number_atoms_solvent             55 
_refine_hist.number_atoms_total               1036 
_refine_hist.d_res_high                       2.26 
_refine_hist.d_res_low                        46.19 
# 
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' ? 0.002  ? 1044 ? f_bond_d           ? ? 
'X-RAY DIFFRACTION' ? 0.376  ? 1427 ? f_angle_d          ? ? 
'X-RAY DIFFRACTION' ? 19.235 ? 371  ? f_dihedral_angle_d ? ? 
'X-RAY DIFFRACTION' ? 0.034  ? 150  ? f_chiral_restr     ? ? 
'X-RAY DIFFRACTION' ? 0.001  ? 179  ? f_plane_restr      ? ? 
# 
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' 2.26 2.59  . . 138 2661 100.00 . . . . 0.2944 . . . . . . . . . . . 0.3395 
'X-RAY DIFFRACTION' 2.59 3.26  . . 160 2672 100.00 . . . . 0.2660 . . . . . . . . . . . 0.2895 
'X-RAY DIFFRACTION' 3.26 46.19 . . 130 2892 100.00 . . . . 0.1814 . . . . . . . . . . . 0.2368 
# 
_struct.entry_id                     9HHB 
_struct.title                        'Crystal Structure of the Plasmodium vivax Bromodomain PvBDP1 in complex with RMM21' 
_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        9HHB 
_struct_keywords.text            'plasmodium, bromodomain, inhibitor, complex, TRANSCRIPTION' 
_struct_keywords.pdbx_keywords   TRANSCRIPTION 
# 
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 4 ? 
# 
_struct_ref.id                         1 
_struct_ref.db_name                    UNP 
_struct_ref.db_code                    A5KDW3_PLAVS 
_struct_ref.pdbx_db_accession          A5KDW3 
_struct_ref.pdbx_db_isoform            ? 
_struct_ref.entity_id                  1 
_struct_ref.pdbx_seq_one_letter_code   
;FNKQWYLLANQIIQSLSKYEGGHIFEKLVDAKKQNCPDYYDVIKNPMSFSCVKTKLKKGQYGLPTEFIKDVQLIFDNCSL
YNTSGSLVAITGKNIEAYFNNQLIVTGYNNFVTKANTINERLQKVEDEN
;
_struct_ref.pdbx_align_begin           318 
# 
_struct_ref_seq.align_id                      1 
_struct_ref_seq.ref_id                        1 
_struct_ref_seq.pdbx_PDB_id_code              9HHB 
_struct_ref_seq.pdbx_strand_id                A 
_struct_ref_seq.seq_align_beg                 2 
_struct_ref_seq.pdbx_seq_align_beg_ins_code   ? 
_struct_ref_seq.seq_align_end                 130 
_struct_ref_seq.pdbx_seq_align_end_ins_code   ? 
_struct_ref_seq.pdbx_db_accession             A5KDW3 
_struct_ref_seq.db_align_beg                  318 
_struct_ref_seq.pdbx_db_align_beg_ins_code    ? 
_struct_ref_seq.db_align_end                  446 
_struct_ref_seq.pdbx_db_align_end_ins_code    ? 
_struct_ref_seq.pdbx_auth_seq_align_beg       2 
_struct_ref_seq.pdbx_auth_seq_align_end       130 
# 
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 9HHB SER A 1   ? UNP A5KDW3 ? ? 'expression tag' 1   1 
1 9HHB LEU A 131 ? UNP A5KDW3 ? ? 'expression tag' 131 2 
1 9HHB GLU A 132 ? UNP A5KDW3 ? ? 'expression tag' 132 3 
# 
_pdbx_struct_assembly.id                   1 
_pdbx_struct_assembly.details              author_defined_assembly 
_pdbx_struct_assembly.method_details       ? 
_pdbx_struct_assembly.oligomeric_details   monomeric 
_pdbx_struct_assembly.oligomeric_count     1 
# 
loop_
_pdbx_struct_assembly_prop.biol_id 
_pdbx_struct_assembly_prop.type 
_pdbx_struct_assembly_prop.value 
_pdbx_struct_assembly_prop.details 
1 'ABSA (A^2)' 90   ? 
1 MORE         -6   ? 
1 'SSA (A^2)'  7030 ? 
# 
_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 
# 
_pdbx_struct_assembly_auth_evidence.id                     1 
_pdbx_struct_assembly_auth_evidence.assembly_id            1 
_pdbx_struct_assembly_auth_evidence.experimental_support   'gel filtration' 
_pdbx_struct_assembly_auth_evidence.details                ? 
# 
_pdbx_struct_oper_list.id                   1 
_pdbx_struct_oper_list.type                 'identity operation' 
_pdbx_struct_oper_list.name                 1_555 
_pdbx_struct_oper_list.symmetry_operation   x,y,z 
_pdbx_struct_oper_list.matrix[1][1]         1.0000000000 
_pdbx_struct_oper_list.matrix[1][2]         0.0000000000 
_pdbx_struct_oper_list.matrix[1][3]         0.0000000000 
_pdbx_struct_oper_list.vector[1]            0.0000000000 
_pdbx_struct_oper_list.matrix[2][1]         0.0000000000 
_pdbx_struct_oper_list.matrix[2][2]         1.0000000000 
_pdbx_struct_oper_list.matrix[2][3]         0.0000000000 
_pdbx_struct_oper_list.vector[2]            0.0000000000 
_pdbx_struct_oper_list.matrix[3][1]         0.0000000000 
_pdbx_struct_oper_list.matrix[3][2]         0.0000000000 
_pdbx_struct_oper_list.matrix[3][3]         1.0000000000 
_pdbx_struct_oper_list.vector[3]            0.0000000000 
# 
loop_
_struct_conf.conf_type_id 
_struct_conf.id 
_struct_conf.pdbx_PDB_helix_id 
_struct_conf.beg_label_comp_id 
_struct_conf.beg_label_asym_id 
_struct_conf.beg_label_seq_id 
_struct_conf.pdbx_beg_PDB_ins_code 
_struct_conf.end_label_comp_id 
_struct_conf.end_label_asym_id 
_struct_conf.end_label_seq_id 
_struct_conf.pdbx_end_PDB_ins_code 
_struct_conf.beg_auth_comp_id 
_struct_conf.beg_auth_asym_id 
_struct_conf.beg_auth_seq_id 
_struct_conf.end_auth_comp_id 
_struct_conf.end_auth_asym_id 
_struct_conf.end_auth_seq_id 
_struct_conf.pdbx_PDB_helix_class 
_struct_conf.details 
_struct_conf.pdbx_PDB_helix_length 
HELX_P HELX_P1 AA1 SER A 1   ? TYR A 20  ? SER A 1   TYR A 20  1 ? 20 
HELX_P HELX_P2 AA2 GLY A 22  ? GLU A 27  ? GLY A 22  GLU A 27  5 ? 6  
HELX_P HELX_P3 AA3 ASP A 39  ? ILE A 44  ? ASP A 39  ILE A 44  1 ? 6  
HELX_P HELX_P4 AA4 SER A 49  ? GLY A 60  ? SER A 49  GLY A 60  1 ? 12 
HELX_P HELX_P5 AA5 LEU A 64  ? ASN A 83  ? LEU A 64  ASN A 83  1 ? 20 
HELX_P HELX_P6 AA6 SER A 87  ? THR A 107 ? SER A 87  THR A 107 1 ? 21 
HELX_P HELX_P7 AA7 GLY A 108 ? ASN A 120 ? GLY A 108 ASN A 120 1 ? 13 
# 
_struct_conf_type.id          HELX_P 
_struct_conf_type.criteria    ? 
_struct_conf_type.reference   ? 
# 
_pdbx_entry_details.entry_id                   9HHB 
_pdbx_entry_details.nonpolymer_details         ? 
_pdbx_entry_details.sequence_details           ? 
_pdbx_entry_details.compound_details           ? 
_pdbx_entry_details.source_details             ? 
_pdbx_entry_details.has_ligand_of_interest     Y 
_pdbx_entry_details.has_protein_modification   N 
# 
loop_
_pdbx_struct_special_symmetry.id 
_pdbx_struct_special_symmetry.PDB_model_num 
_pdbx_struct_special_symmetry.auth_asym_id 
_pdbx_struct_special_symmetry.auth_comp_id 
_pdbx_struct_special_symmetry.auth_seq_id 
_pdbx_struct_special_symmetry.PDB_ins_code 
_pdbx_struct_special_symmetry.label_asym_id 
_pdbx_struct_special_symmetry.label_comp_id 
_pdbx_struct_special_symmetry.label_seq_id 
1 1 A HOH 345 ? D HOH . 
2 1 A HOH 350 ? D HOH . 
3 1 A HOH 355 ? D HOH . 
# 
_pdbx_refine_tls.id               1 
_pdbx_refine_tls.pdbx_refine_id   'X-RAY DIFFRACTION' 
_pdbx_refine_tls.details          ? 
_pdbx_refine_tls.method           refined 
_pdbx_refine_tls.origin_x         25.5415 
_pdbx_refine_tls.origin_y         -22.8954 
_pdbx_refine_tls.origin_z         -0.8998 
_pdbx_refine_tls.T[1][1]          0.3414 
_pdbx_refine_tls.T[1][1]_esd      ? 
_pdbx_refine_tls.T[1][2]          0.0014 
_pdbx_refine_tls.T[1][2]_esd      ? 
_pdbx_refine_tls.T[1][3]          0.0181 
_pdbx_refine_tls.T[1][3]_esd      ? 
_pdbx_refine_tls.T[2][2]          0.2695 
_pdbx_refine_tls.T[2][2]_esd      ? 
_pdbx_refine_tls.T[2][3]          0.0032 
_pdbx_refine_tls.T[2][3]_esd      ? 
_pdbx_refine_tls.T[3][3]          0.6341 
_pdbx_refine_tls.T[3][3]_esd      ? 
_pdbx_refine_tls.L[1][1]          2.4685 
_pdbx_refine_tls.L[1][1]_esd      ? 
_pdbx_refine_tls.L[1][2]          1.2431 
_pdbx_refine_tls.L[1][2]_esd      ? 
_pdbx_refine_tls.L[1][3]          1.0309 
_pdbx_refine_tls.L[1][3]_esd      ? 
_pdbx_refine_tls.L[2][2]          2.0131 
_pdbx_refine_tls.L[2][2]_esd      ? 
_pdbx_refine_tls.L[2][3]          1.2405 
_pdbx_refine_tls.L[2][3]_esd      ? 
_pdbx_refine_tls.L[3][3]          4.0438 
_pdbx_refine_tls.L[3][3]_esd      ? 
_pdbx_refine_tls.S[1][1]          0.0924 
_pdbx_refine_tls.S[1][1]_esd      ? 
_pdbx_refine_tls.S[1][2]          -0.0830 
_pdbx_refine_tls.S[1][2]_esd      ? 
_pdbx_refine_tls.S[1][3]          0.1185 
_pdbx_refine_tls.S[1][3]_esd      ? 
_pdbx_refine_tls.S[2][1]          0.1775 
_pdbx_refine_tls.S[2][1]_esd      ? 
_pdbx_refine_tls.S[2][2]          -0.0217 
_pdbx_refine_tls.S[2][2]_esd      ? 
_pdbx_refine_tls.S[2][3]          0.0519 
_pdbx_refine_tls.S[2][3]_esd      ? 
_pdbx_refine_tls.S[3][1]          -0.0414 
_pdbx_refine_tls.S[3][1]_esd      ? 
_pdbx_refine_tls.S[3][2]          0.0164 
_pdbx_refine_tls.S[3][2]_esd      ? 
_pdbx_refine_tls.S[3][3]          -0.0642 
_pdbx_refine_tls.S[3][3]_esd      ? 
# 
_pdbx_refine_tls_group.id                  1 
_pdbx_refine_tls_group.pdbx_refine_id      'X-RAY DIFFRACTION' 
_pdbx_refine_tls_group.refine_tls_id       1 
_pdbx_refine_tls_group.beg_label_asym_id   ? 
_pdbx_refine_tls_group.beg_label_seq_id    ? 
_pdbx_refine_tls_group.beg_auth_asym_id    ? 
_pdbx_refine_tls_group.beg_auth_seq_id     ? 
_pdbx_refine_tls_group.beg_PDB_ins_code    ? 
_pdbx_refine_tls_group.end_label_asym_id   ? 
_pdbx_refine_tls_group.end_label_seq_id    ? 
_pdbx_refine_tls_group.end_auth_asym_id    ? 
_pdbx_refine_tls_group.end_auth_seq_id     ? 
_pdbx_refine_tls_group.end_PDB_ins_code    ? 
_pdbx_refine_tls_group.selection           ? 
_pdbx_refine_tls_group.selection_details   all 
# 
loop_
_pdbx_distant_solvent_atoms.id 
_pdbx_distant_solvent_atoms.PDB_model_num 
_pdbx_distant_solvent_atoms.auth_atom_id 
_pdbx_distant_solvent_atoms.label_alt_id 
_pdbx_distant_solvent_atoms.auth_asym_id 
_pdbx_distant_solvent_atoms.auth_comp_id 
_pdbx_distant_solvent_atoms.auth_seq_id 
_pdbx_distant_solvent_atoms.PDB_ins_code 
_pdbx_distant_solvent_atoms.neighbor_macromolecule_distance 
_pdbx_distant_solvent_atoms.neighbor_ligand_distance 
1 1 O ? A HOH 354 ? 5.95 . 
2 1 O ? A HOH 355 ? 6.08 . 
# 
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 GLU 121 ? A GLU 121 
2  1 Y 1 A ARG 122 ? A ARG 122 
3  1 Y 1 A LEU 123 ? A LEU 123 
4  1 Y 1 A GLN 124 ? A GLN 124 
5  1 Y 1 A LYS 125 ? A LYS 125 
6  1 Y 1 A VAL 126 ? A VAL 126 
7  1 Y 1 A GLU 127 ? A GLU 127 
8  1 Y 1 A ASP 128 ? A ASP 128 
9  1 Y 1 A GLU 129 ? A GLU 129 
10 1 Y 1 A ASN 130 ? A ASN 130 
11 1 Y 1 A LEU 131 ? A LEU 131 
12 1 Y 1 A GLU 132 ? A GLU 132 
# 
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 
A1IUY C01  C N N 1   
A1IUY C02  C N N 2   
A1IUY C03  C N N 3   
A1IUY C04  C N N 4   
A1IUY C05  C N N 5   
A1IUY C07  C Y N 6   
A1IUY C08  C Y N 7   
A1IUY C09  C Y N 8   
A1IUY C10  C N N 9   
A1IUY C12  C Y N 10  
A1IUY C13  C Y N 11  
A1IUY C14  C Y N 12  
A1IUY C15  C Y N 13  
A1IUY C16  C Y N 14  
A1IUY C17  C Y N 15  
A1IUY C18  C Y N 16  
A1IUY C19  C N N 17  
A1IUY C24  C N N 18  
A1IUY N11  N Y N 19  
A1IUY N20  N N N 20  
A1IUY O06  O N N 21  
A1IUY O22  O N N 22  
A1IUY O23  O N N 23  
A1IUY S21  S N N 24  
A1IUY H1   H N N 25  
A1IUY H2   H N N 26  
A1IUY H3   H N N 27  
A1IUY H4   H N N 28  
A1IUY H5   H N N 29  
A1IUY H6   H N N 30  
A1IUY H7   H N N 31  
A1IUY H8   H N N 32  
A1IUY H9   H N N 33  
A1IUY H10  H N N 34  
A1IUY H11  H N N 35  
A1IUY H12  H N N 36  
A1IUY H13  H N N 37  
A1IUY H14  H N N 38  
A1IUY H15  H N N 39  
A1IUY H16  H N N 40  
A1IUY H17  H N N 41  
A1IUY H18  H N N 42  
A1IUY H19  H N N 43  
A1IUY H20  H N N 44  
A1IUY H21  H N N 45  
A1IUY H22  H N N 46  
ALA   N    N N N 47  
ALA   CA   C N S 48  
ALA   C    C N N 49  
ALA   O    O N N 50  
ALA   CB   C N N 51  
ALA   OXT  O N N 52  
ALA   H    H N N 53  
ALA   H2   H N N 54  
ALA   HA   H N N 55  
ALA   HB1  H N N 56  
ALA   HB2  H N N 57  
ALA   HB3  H N N 58  
ALA   HXT  H N N 59  
ARG   N    N N N 60  
ARG   CA   C N S 61  
ARG   C    C N N 62  
ARG   O    O N N 63  
ARG   CB   C N N 64  
ARG   CG   C N N 65  
ARG   CD   C N N 66  
ARG   NE   N N N 67  
ARG   CZ   C N N 68  
ARG   NH1  N N N 69  
ARG   NH2  N N N 70  
ARG   OXT  O N N 71  
ARG   H    H N N 72  
ARG   H2   H N N 73  
ARG   HA   H N N 74  
ARG   HB2  H N N 75  
ARG   HB3  H N N 76  
ARG   HG2  H N N 77  
ARG   HG3  H N N 78  
ARG   HD2  H N N 79  
ARG   HD3  H N N 80  
ARG   HE   H N N 81  
ARG   HH11 H N N 82  
ARG   HH12 H N N 83  
ARG   HH21 H N N 84  
ARG   HH22 H N N 85  
ARG   HXT  H N N 86  
ASN   N    N N N 87  
ASN   CA   C N S 88  
ASN   C    C N N 89  
ASN   O    O N N 90  
ASN   CB   C N N 91  
ASN   CG   C N N 92  
ASN   OD1  O N N 93  
ASN   ND2  N N N 94  
ASN   OXT  O N N 95  
ASN   H    H N N 96  
ASN   H2   H N N 97  
ASN   HA   H N N 98  
ASN   HB2  H N N 99  
ASN   HB3  H N N 100 
ASN   HD21 H N N 101 
ASN   HD22 H N N 102 
ASN   HXT  H N N 103 
ASP   N    N N N 104 
ASP   CA   C N S 105 
ASP   C    C N N 106 
ASP   O    O N N 107 
ASP   CB   C N N 108 
ASP   CG   C N N 109 
ASP   OD1  O N N 110 
ASP   OD2  O N N 111 
ASP   OXT  O N N 112 
ASP   H    H N N 113 
ASP   H2   H N N 114 
ASP   HA   H N N 115 
ASP   HB2  H N N 116 
ASP   HB3  H N N 117 
ASP   HD2  H N N 118 
ASP   HXT  H N N 119 
CYS   N    N N N 120 
CYS   CA   C N R 121 
CYS   C    C N N 122 
CYS   O    O N N 123 
CYS   CB   C N N 124 
CYS   SG   S N N 125 
CYS   OXT  O N N 126 
CYS   H    H N N 127 
CYS   H2   H N N 128 
CYS   HA   H N N 129 
CYS   HB2  H N N 130 
CYS   HB3  H N N 131 
CYS   HG   H N N 132 
CYS   HXT  H N N 133 
GLN   N    N N N 134 
GLN   CA   C N S 135 
GLN   C    C N N 136 
GLN   O    O N N 137 
GLN   CB   C N N 138 
GLN   CG   C N N 139 
GLN   CD   C N N 140 
GLN   OE1  O N N 141 
GLN   NE2  N N N 142 
GLN   OXT  O N N 143 
GLN   H    H N N 144 
GLN   H2   H N N 145 
GLN   HA   H N N 146 
GLN   HB2  H N N 147 
GLN   HB3  H N N 148 
GLN   HG2  H N N 149 
GLN   HG3  H N N 150 
GLN   HE21 H N N 151 
GLN   HE22 H N N 152 
GLN   HXT  H N N 153 
GLU   N    N N N 154 
GLU   CA   C N S 155 
GLU   C    C N N 156 
GLU   O    O N N 157 
GLU   CB   C N N 158 
GLU   CG   C N N 159 
GLU   CD   C N N 160 
GLU   OE1  O N N 161 
GLU   OE2  O N N 162 
GLU   OXT  O N N 163 
GLU   H    H N N 164 
GLU   H2   H N N 165 
GLU   HA   H N N 166 
GLU   HB2  H N N 167 
GLU   HB3  H N N 168 
GLU   HG2  H N N 169 
GLU   HG3  H N N 170 
GLU   HE2  H N N 171 
GLU   HXT  H N N 172 
GLY   N    N N N 173 
GLY   CA   C N N 174 
GLY   C    C N N 175 
GLY   O    O N N 176 
GLY   OXT  O N N 177 
GLY   H    H N N 178 
GLY   H2   H N N 179 
GLY   HA2  H N N 180 
GLY   HA3  H N N 181 
GLY   HXT  H N N 182 
HIS   N    N N N 183 
HIS   CA   C N S 184 
HIS   C    C N N 185 
HIS   O    O N N 186 
HIS   CB   C N N 187 
HIS   CG   C Y N 188 
HIS   ND1  N Y N 189 
HIS   CD2  C Y N 190 
HIS   CE1  C Y N 191 
HIS   NE2  N Y N 192 
HIS   OXT  O N N 193 
HIS   H    H N N 194 
HIS   H2   H N N 195 
HIS   HA   H N N 196 
HIS   HB2  H N N 197 
HIS   HB3  H N N 198 
HIS   HD1  H N N 199 
HIS   HD2  H N N 200 
HIS   HE1  H N N 201 
HIS   HE2  H N N 202 
HIS   HXT  H N N 203 
HOH   O    O N N 204 
HOH   H1   H N N 205 
HOH   H2   H N N 206 
ILE   N    N N N 207 
ILE   CA   C N S 208 
ILE   C    C N N 209 
ILE   O    O N N 210 
ILE   CB   C N S 211 
ILE   CG1  C N N 212 
ILE   CG2  C N N 213 
ILE   CD1  C N N 214 
ILE   OXT  O N N 215 
ILE   H    H N N 216 
ILE   H2   H N N 217 
ILE   HA   H N N 218 
ILE   HB   H N N 219 
ILE   HG12 H N N 220 
ILE   HG13 H N N 221 
ILE   HG21 H N N 222 
ILE   HG22 H N N 223 
ILE   HG23 H N N 224 
ILE   HD11 H N N 225 
ILE   HD12 H N N 226 
ILE   HD13 H N N 227 
ILE   HXT  H N N 228 
LEU   N    N N N 229 
LEU   CA   C N S 230 
LEU   C    C N N 231 
LEU   O    O N N 232 
LEU   CB   C N N 233 
LEU   CG   C N N 234 
LEU   CD1  C N N 235 
LEU   CD2  C N N 236 
LEU   OXT  O N N 237 
LEU   H    H N N 238 
LEU   H2   H N N 239 
LEU   HA   H N N 240 
LEU   HB2  H N N 241 
LEU   HB3  H N N 242 
LEU   HG   H N N 243 
LEU   HD11 H N N 244 
LEU   HD12 H N N 245 
LEU   HD13 H N N 246 
LEU   HD21 H N N 247 
LEU   HD22 H N N 248 
LEU   HD23 H N N 249 
LEU   HXT  H N N 250 
LYS   N    N N N 251 
LYS   CA   C N S 252 
LYS   C    C N N 253 
LYS   O    O N N 254 
LYS   CB   C N N 255 
LYS   CG   C N N 256 
LYS   CD   C N N 257 
LYS   CE   C N N 258 
LYS   NZ   N N N 259 
LYS   OXT  O N N 260 
LYS   H    H N N 261 
LYS   H2   H N N 262 
LYS   HA   H N N 263 
LYS   HB2  H N N 264 
LYS   HB3  H N N 265 
LYS   HG2  H N N 266 
LYS   HG3  H N N 267 
LYS   HD2  H N N 268 
LYS   HD3  H N N 269 
LYS   HE2  H N N 270 
LYS   HE3  H N N 271 
LYS   HZ1  H N N 272 
LYS   HZ2  H N N 273 
LYS   HZ3  H N N 274 
LYS   HXT  H N N 275 
MET   N    N N N 276 
MET   CA   C N S 277 
MET   C    C N N 278 
MET   O    O N N 279 
MET   CB   C N N 280 
MET   CG   C N N 281 
MET   SD   S N N 282 
MET   CE   C N N 283 
MET   OXT  O N N 284 
MET   H    H N N 285 
MET   H2   H N N 286 
MET   HA   H N N 287 
MET   HB2  H N N 288 
MET   HB3  H N N 289 
MET   HG2  H N N 290 
MET   HG3  H N N 291 
MET   HE1  H N N 292 
MET   HE2  H N N 293 
MET   HE3  H N N 294 
MET   HXT  H N N 295 
PHE   N    N N N 296 
PHE   CA   C N S 297 
PHE   C    C N N 298 
PHE   O    O N N 299 
PHE   CB   C N N 300 
PHE   CG   C Y N 301 
PHE   CD1  C Y N 302 
PHE   CD2  C Y N 303 
PHE   CE1  C Y N 304 
PHE   CE2  C Y N 305 
PHE   CZ   C Y N 306 
PHE   OXT  O N N 307 
PHE   H    H N N 308 
PHE   H2   H N N 309 
PHE   HA   H N N 310 
PHE   HB2  H N N 311 
PHE   HB3  H N N 312 
PHE   HD1  H N N 313 
PHE   HD2  H N N 314 
PHE   HE1  H N N 315 
PHE   HE2  H N N 316 
PHE   HZ   H N N 317 
PHE   HXT  H N N 318 
PRO   N    N N N 319 
PRO   CA   C N S 320 
PRO   C    C N N 321 
PRO   O    O N N 322 
PRO   CB   C N N 323 
PRO   CG   C N N 324 
PRO   CD   C N N 325 
PRO   OXT  O N N 326 
PRO   H    H N N 327 
PRO   HA   H N N 328 
PRO   HB2  H N N 329 
PRO   HB3  H N N 330 
PRO   HG2  H N N 331 
PRO   HG3  H N N 332 
PRO   HD2  H N N 333 
PRO   HD3  H N N 334 
PRO   HXT  H N N 335 
SER   N    N N N 336 
SER   CA   C N S 337 
SER   C    C N N 338 
SER   O    O N N 339 
SER   CB   C N N 340 
SER   OG   O N N 341 
SER   OXT  O N N 342 
SER   H    H N N 343 
SER   H2   H N N 344 
SER   HA   H N N 345 
SER   HB2  H N N 346 
SER   HB3  H N N 347 
SER   HG   H N N 348 
SER   HXT  H N N 349 
SO4   S    S N N 350 
SO4   O1   O N N 351 
SO4   O2   O N N 352 
SO4   O3   O N N 353 
SO4   O4   O N N 354 
THR   N    N N N 355 
THR   CA   C N S 356 
THR   C    C N N 357 
THR   O    O N N 358 
THR   CB   C N R 359 
THR   OG1  O N N 360 
THR   CG2  C N N 361 
THR   OXT  O N N 362 
THR   H    H N N 363 
THR   H2   H N N 364 
THR   HA   H N N 365 
THR   HB   H N N 366 
THR   HG1  H N N 367 
THR   HG21 H N N 368 
THR   HG22 H N N 369 
THR   HG23 H N N 370 
THR   HXT  H N N 371 
TRP   N    N N N 372 
TRP   CA   C N S 373 
TRP   C    C N N 374 
TRP   O    O N N 375 
TRP   CB   C N N 376 
TRP   CG   C Y N 377 
TRP   CD1  C Y N 378 
TRP   CD2  C Y N 379 
TRP   NE1  N Y N 380 
TRP   CE2  C Y N 381 
TRP   CE3  C Y N 382 
TRP   CZ2  C Y N 383 
TRP   CZ3  C Y N 384 
TRP   CH2  C Y N 385 
TRP   OXT  O N N 386 
TRP   H    H N N 387 
TRP   H2   H N N 388 
TRP   HA   H N N 389 
TRP   HB2  H N N 390 
TRP   HB3  H N N 391 
TRP   HD1  H N N 392 
TRP   HE1  H N N 393 
TRP   HE3  H N N 394 
TRP   HZ2  H N N 395 
TRP   HZ3  H N N 396 
TRP   HH2  H N N 397 
TRP   HXT  H N N 398 
TYR   N    N N N 399 
TYR   CA   C N S 400 
TYR   C    C N N 401 
TYR   O    O N N 402 
TYR   CB   C N N 403 
TYR   CG   C Y N 404 
TYR   CD1  C Y N 405 
TYR   CD2  C Y N 406 
TYR   CE1  C Y N 407 
TYR   CE2  C Y N 408 
TYR   CZ   C Y N 409 
TYR   OH   O N N 410 
TYR   OXT  O N N 411 
TYR   H    H N N 412 
TYR   H2   H N N 413 
TYR   HA   H N N 414 
TYR   HB2  H N N 415 
TYR   HB3  H N N 416 
TYR   HD1  H N N 417 
TYR   HD2  H N N 418 
TYR   HE1  H N N 419 
TYR   HE2  H N N 420 
TYR   HH   H N N 421 
TYR   HXT  H N N 422 
VAL   N    N N N 423 
VAL   CA   C N S 424 
VAL   C    C N N 425 
VAL   O    O N N 426 
VAL   CB   C N N 427 
VAL   CG1  C N N 428 
VAL   CG2  C N N 429 
VAL   OXT  O N N 430 
VAL   H    H N N 431 
VAL   H2   H N N 432 
VAL   HA   H N N 433 
VAL   HB   H N N 434 
VAL   HG11 H N N 435 
VAL   HG12 H N N 436 
VAL   HG13 H N N 437 
VAL   HG21 H N N 438 
VAL   HG22 H N N 439 
VAL   HG23 H N N 440 
VAL   HXT  H N N 441 
# 
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 
A1IUY C02 C03  sing N N 1   
A1IUY C02 C01  sing N N 2   
A1IUY C03 C04  sing N N 3   
A1IUY O22 S21  doub N N 4   
A1IUY C01 C08  sing N N 5   
A1IUY C04 C05  sing N N 6   
A1IUY C15 C14  doub Y N 7   
A1IUY C15 C16  sing Y N 8   
A1IUY O23 S21  doub N N 9   
A1IUY C14 C13  sing Y N 10  
A1IUY S21 C24  sing N N 11  
A1IUY S21 N20  sing N N 12  
A1IUY C16 C17  doub Y N 13  
A1IUY C08 C07  sing Y N 14  
A1IUY C08 C12  doub Y N 15  
A1IUY C05 O06  doub N N 16  
A1IUY C05 C07  sing N N 17  
A1IUY C13 C12  sing N N 18  
A1IUY C13 C18  doub Y N 19  
A1IUY C17 C18  sing Y N 20  
A1IUY C17 N20  sing N N 21  
A1IUY C07 C09  doub Y N 22  
A1IUY C12 N11  sing Y N 23  
A1IUY C18 C19  sing N N 24  
A1IUY N11 C09  sing Y N 25  
A1IUY C09 C10  sing N N 26  
A1IUY C01 H1   sing N N 27  
A1IUY C01 H2   sing N N 28  
A1IUY C02 H3   sing N N 29  
A1IUY C02 H4   sing N N 30  
A1IUY C03 H5   sing N N 31  
A1IUY C03 H6   sing N N 32  
A1IUY C04 H7   sing N N 33  
A1IUY C04 H8   sing N N 34  
A1IUY C10 H9   sing N N 35  
A1IUY C10 H10  sing N N 36  
A1IUY C10 H11  sing N N 37  
A1IUY C14 H12  sing N N 38  
A1IUY C15 H13  sing N N 39  
A1IUY C16 H14  sing N N 40  
A1IUY C19 H15  sing N N 41  
A1IUY C19 H16  sing N N 42  
A1IUY C19 H17  sing N N 43  
A1IUY C24 H18  sing N N 44  
A1IUY C24 H19  sing N N 45  
A1IUY C24 H20  sing N N 46  
A1IUY N11 H21  sing N N 47  
A1IUY N20 H22  sing N N 48  
ALA   N   CA   sing N N 49  
ALA   N   H    sing N N 50  
ALA   N   H2   sing N N 51  
ALA   CA  C    sing N N 52  
ALA   CA  CB   sing N N 53  
ALA   CA  HA   sing N N 54  
ALA   C   O    doub N N 55  
ALA   C   OXT  sing N N 56  
ALA   CB  HB1  sing N N 57  
ALA   CB  HB2  sing N N 58  
ALA   CB  HB3  sing N N 59  
ALA   OXT HXT  sing N N 60  
ARG   N   CA   sing N N 61  
ARG   N   H    sing N N 62  
ARG   N   H2   sing N N 63  
ARG   CA  C    sing N N 64  
ARG   CA  CB   sing N N 65  
ARG   CA  HA   sing N N 66  
ARG   C   O    doub N N 67  
ARG   C   OXT  sing N N 68  
ARG   CB  CG   sing N N 69  
ARG   CB  HB2  sing N N 70  
ARG   CB  HB3  sing N N 71  
ARG   CG  CD   sing N N 72  
ARG   CG  HG2  sing N N 73  
ARG   CG  HG3  sing N N 74  
ARG   CD  NE   sing N N 75  
ARG   CD  HD2  sing N N 76  
ARG   CD  HD3  sing N N 77  
ARG   NE  CZ   sing N N 78  
ARG   NE  HE   sing N N 79  
ARG   CZ  NH1  sing N N 80  
ARG   CZ  NH2  doub N N 81  
ARG   NH1 HH11 sing N N 82  
ARG   NH1 HH12 sing N N 83  
ARG   NH2 HH21 sing N N 84  
ARG   NH2 HH22 sing N N 85  
ARG   OXT HXT  sing N N 86  
ASN   N   CA   sing N N 87  
ASN   N   H    sing N N 88  
ASN   N   H2   sing N N 89  
ASN   CA  C    sing N N 90  
ASN   CA  CB   sing N N 91  
ASN   CA  HA   sing N N 92  
ASN   C   O    doub N N 93  
ASN   C   OXT  sing N N 94  
ASN   CB  CG   sing N N 95  
ASN   CB  HB2  sing N N 96  
ASN   CB  HB3  sing N N 97  
ASN   CG  OD1  doub N N 98  
ASN   CG  ND2  sing N N 99  
ASN   ND2 HD21 sing N N 100 
ASN   ND2 HD22 sing N N 101 
ASN   OXT HXT  sing N N 102 
ASP   N   CA   sing N N 103 
ASP   N   H    sing N N 104 
ASP   N   H2   sing N N 105 
ASP   CA  C    sing N N 106 
ASP   CA  CB   sing N N 107 
ASP   CA  HA   sing N N 108 
ASP   C   O    doub N N 109 
ASP   C   OXT  sing N N 110 
ASP   CB  CG   sing N N 111 
ASP   CB  HB2  sing N N 112 
ASP   CB  HB3  sing N N 113 
ASP   CG  OD1  doub N N 114 
ASP   CG  OD2  sing N N 115 
ASP   OD2 HD2  sing N N 116 
ASP   OXT HXT  sing N N 117 
CYS   N   CA   sing N N 118 
CYS   N   H    sing N N 119 
CYS   N   H2   sing N N 120 
CYS   CA  C    sing N N 121 
CYS   CA  CB   sing N N 122 
CYS   CA  HA   sing N N 123 
CYS   C   O    doub N N 124 
CYS   C   OXT  sing N N 125 
CYS   CB  SG   sing N N 126 
CYS   CB  HB2  sing N N 127 
CYS   CB  HB3  sing N N 128 
CYS   SG  HG   sing N N 129 
CYS   OXT HXT  sing N N 130 
GLN   N   CA   sing N N 131 
GLN   N   H    sing N N 132 
GLN   N   H2   sing N N 133 
GLN   CA  C    sing N N 134 
GLN   CA  CB   sing N N 135 
GLN   CA  HA   sing N N 136 
GLN   C   O    doub N N 137 
GLN   C   OXT  sing N N 138 
GLN   CB  CG   sing N N 139 
GLN   CB  HB2  sing N N 140 
GLN   CB  HB3  sing N N 141 
GLN   CG  CD   sing N N 142 
GLN   CG  HG2  sing N N 143 
GLN   CG  HG3  sing N N 144 
GLN   CD  OE1  doub N N 145 
GLN   CD  NE2  sing N N 146 
GLN   NE2 HE21 sing N N 147 
GLN   NE2 HE22 sing N N 148 
GLN   OXT HXT  sing N N 149 
GLU   N   CA   sing N N 150 
GLU   N   H    sing N N 151 
GLU   N   H2   sing N N 152 
GLU   CA  C    sing N N 153 
GLU   CA  CB   sing N N 154 
GLU   CA  HA   sing N N 155 
GLU   C   O    doub N N 156 
GLU   C   OXT  sing N N 157 
GLU   CB  CG   sing N N 158 
GLU   CB  HB2  sing N N 159 
GLU   CB  HB3  sing N N 160 
GLU   CG  CD   sing N N 161 
GLU   CG  HG2  sing N N 162 
GLU   CG  HG3  sing N N 163 
GLU   CD  OE1  doub N N 164 
GLU   CD  OE2  sing N N 165 
GLU   OE2 HE2  sing N N 166 
GLU   OXT HXT  sing N N 167 
GLY   N   CA   sing N N 168 
GLY   N   H    sing N N 169 
GLY   N   H2   sing N N 170 
GLY   CA  C    sing N N 171 
GLY   CA  HA2  sing N N 172 
GLY   CA  HA3  sing N N 173 
GLY   C   O    doub N N 174 
GLY   C   OXT  sing N N 175 
GLY   OXT HXT  sing N N 176 
HIS   N   CA   sing N N 177 
HIS   N   H    sing N N 178 
HIS   N   H2   sing N N 179 
HIS   CA  C    sing N N 180 
HIS   CA  CB   sing N N 181 
HIS   CA  HA   sing N N 182 
HIS   C   O    doub N N 183 
HIS   C   OXT  sing N N 184 
HIS   CB  CG   sing N N 185 
HIS   CB  HB2  sing N N 186 
HIS   CB  HB3  sing N N 187 
HIS   CG  ND1  sing Y N 188 
HIS   CG  CD2  doub Y N 189 
HIS   ND1 CE1  doub Y N 190 
HIS   ND1 HD1  sing N N 191 
HIS   CD2 NE2  sing Y N 192 
HIS   CD2 HD2  sing N N 193 
HIS   CE1 NE2  sing Y N 194 
HIS   CE1 HE1  sing N N 195 
HIS   NE2 HE2  sing N N 196 
HIS   OXT HXT  sing N N 197 
HOH   O   H1   sing N N 198 
HOH   O   H2   sing N N 199 
ILE   N   CA   sing N N 200 
ILE   N   H    sing N N 201 
ILE   N   H2   sing N N 202 
ILE   CA  C    sing N N 203 
ILE   CA  CB   sing N N 204 
ILE   CA  HA   sing N N 205 
ILE   C   O    doub N N 206 
ILE   C   OXT  sing N N 207 
ILE   CB  CG1  sing N N 208 
ILE   CB  CG2  sing N N 209 
ILE   CB  HB   sing N N 210 
ILE   CG1 CD1  sing N N 211 
ILE   CG1 HG12 sing N N 212 
ILE   CG1 HG13 sing N N 213 
ILE   CG2 HG21 sing N N 214 
ILE   CG2 HG22 sing N N 215 
ILE   CG2 HG23 sing N N 216 
ILE   CD1 HD11 sing N N 217 
ILE   CD1 HD12 sing N N 218 
ILE   CD1 HD13 sing N N 219 
ILE   OXT HXT  sing N N 220 
LEU   N   CA   sing N N 221 
LEU   N   H    sing N N 222 
LEU   N   H2   sing N N 223 
LEU   CA  C    sing N N 224 
LEU   CA  CB   sing N N 225 
LEU   CA  HA   sing N N 226 
LEU   C   O    doub N N 227 
LEU   C   OXT  sing N N 228 
LEU   CB  CG   sing N N 229 
LEU   CB  HB2  sing N N 230 
LEU   CB  HB3  sing N N 231 
LEU   CG  CD1  sing N N 232 
LEU   CG  CD2  sing N N 233 
LEU   CG  HG   sing N N 234 
LEU   CD1 HD11 sing N N 235 
LEU   CD1 HD12 sing N N 236 
LEU   CD1 HD13 sing N N 237 
LEU   CD2 HD21 sing N N 238 
LEU   CD2 HD22 sing N N 239 
LEU   CD2 HD23 sing N N 240 
LEU   OXT HXT  sing N N 241 
LYS   N   CA   sing N N 242 
LYS   N   H    sing N N 243 
LYS   N   H2   sing N N 244 
LYS   CA  C    sing N N 245 
LYS   CA  CB   sing N N 246 
LYS   CA  HA   sing N N 247 
LYS   C   O    doub N N 248 
LYS   C   OXT  sing N N 249 
LYS   CB  CG   sing N N 250 
LYS   CB  HB2  sing N N 251 
LYS   CB  HB3  sing N N 252 
LYS   CG  CD   sing N N 253 
LYS   CG  HG2  sing N N 254 
LYS   CG  HG3  sing N N 255 
LYS   CD  CE   sing N N 256 
LYS   CD  HD2  sing N N 257 
LYS   CD  HD3  sing N N 258 
LYS   CE  NZ   sing N N 259 
LYS   CE  HE2  sing N N 260 
LYS   CE  HE3  sing N N 261 
LYS   NZ  HZ1  sing N N 262 
LYS   NZ  HZ2  sing N N 263 
LYS   NZ  HZ3  sing N N 264 
LYS   OXT HXT  sing N N 265 
MET   N   CA   sing N N 266 
MET   N   H    sing N N 267 
MET   N   H2   sing N N 268 
MET   CA  C    sing N N 269 
MET   CA  CB   sing N N 270 
MET   CA  HA   sing N N 271 
MET   C   O    doub N N 272 
MET   C   OXT  sing N N 273 
MET   CB  CG   sing N N 274 
MET   CB  HB2  sing N N 275 
MET   CB  HB3  sing N N 276 
MET   CG  SD   sing N N 277 
MET   CG  HG2  sing N N 278 
MET   CG  HG3  sing N N 279 
MET   SD  CE   sing N N 280 
MET   CE  HE1  sing N N 281 
MET   CE  HE2  sing N N 282 
MET   CE  HE3  sing N N 283 
MET   OXT HXT  sing N N 284 
PHE   N   CA   sing N N 285 
PHE   N   H    sing N N 286 
PHE   N   H2   sing N N 287 
PHE   CA  C    sing N N 288 
PHE   CA  CB   sing N N 289 
PHE   CA  HA   sing N N 290 
PHE   C   O    doub N N 291 
PHE   C   OXT  sing N N 292 
PHE   CB  CG   sing N N 293 
PHE   CB  HB2  sing N N 294 
PHE   CB  HB3  sing N N 295 
PHE   CG  CD1  doub Y N 296 
PHE   CG  CD2  sing Y N 297 
PHE   CD1 CE1  sing Y N 298 
PHE   CD1 HD1  sing N N 299 
PHE   CD2 CE2  doub Y N 300 
PHE   CD2 HD2  sing N N 301 
PHE   CE1 CZ   doub Y N 302 
PHE   CE1 HE1  sing N N 303 
PHE   CE2 CZ   sing Y N 304 
PHE   CE2 HE2  sing N N 305 
PHE   CZ  HZ   sing N N 306 
PHE   OXT HXT  sing N N 307 
PRO   N   CA   sing N N 308 
PRO   N   CD   sing N N 309 
PRO   N   H    sing N N 310 
PRO   CA  C    sing N N 311 
PRO   CA  CB   sing N N 312 
PRO   CA  HA   sing N N 313 
PRO   C   O    doub N N 314 
PRO   C   OXT  sing N N 315 
PRO   CB  CG   sing N N 316 
PRO   CB  HB2  sing N N 317 
PRO   CB  HB3  sing N N 318 
PRO   CG  CD   sing N N 319 
PRO   CG  HG2  sing N N 320 
PRO   CG  HG3  sing N N 321 
PRO   CD  HD2  sing N N 322 
PRO   CD  HD3  sing N N 323 
PRO   OXT HXT  sing N N 324 
SER   N   CA   sing N N 325 
SER   N   H    sing N N 326 
SER   N   H2   sing N N 327 
SER   CA  C    sing N N 328 
SER   CA  CB   sing N N 329 
SER   CA  HA   sing N N 330 
SER   C   O    doub N N 331 
SER   C   OXT  sing N N 332 
SER   CB  OG   sing N N 333 
SER   CB  HB2  sing N N 334 
SER   CB  HB3  sing N N 335 
SER   OG  HG   sing N N 336 
SER   OXT HXT  sing N N 337 
SO4   S   O1   doub N N 338 
SO4   S   O2   doub N N 339 
SO4   S   O3   sing N N 340 
SO4   S   O4   sing N N 341 
THR   N   CA   sing N N 342 
THR   N   H    sing N N 343 
THR   N   H2   sing N N 344 
THR   CA  C    sing N N 345 
THR   CA  CB   sing N N 346 
THR   CA  HA   sing N N 347 
THR   C   O    doub N N 348 
THR   C   OXT  sing N N 349 
THR   CB  OG1  sing N N 350 
THR   CB  CG2  sing N N 351 
THR   CB  HB   sing N N 352 
THR   OG1 HG1  sing N N 353 
THR   CG2 HG21 sing N N 354 
THR   CG2 HG22 sing N N 355 
THR   CG2 HG23 sing N N 356 
THR   OXT HXT  sing N N 357 
TRP   N   CA   sing N N 358 
TRP   N   H    sing N N 359 
TRP   N   H2   sing N N 360 
TRP   CA  C    sing N N 361 
TRP   CA  CB   sing N N 362 
TRP   CA  HA   sing N N 363 
TRP   C   O    doub N N 364 
TRP   C   OXT  sing N N 365 
TRP   CB  CG   sing N N 366 
TRP   CB  HB2  sing N N 367 
TRP   CB  HB3  sing N N 368 
TRP   CG  CD1  doub Y N 369 
TRP   CG  CD2  sing Y N 370 
TRP   CD1 NE1  sing Y N 371 
TRP   CD1 HD1  sing N N 372 
TRP   CD2 CE2  doub Y N 373 
TRP   CD2 CE3  sing Y N 374 
TRP   NE1 CE2  sing Y N 375 
TRP   NE1 HE1  sing N N 376 
TRP   CE2 CZ2  sing Y N 377 
TRP   CE3 CZ3  doub Y N 378 
TRP   CE3 HE3  sing N N 379 
TRP   CZ2 CH2  doub Y N 380 
TRP   CZ2 HZ2  sing N N 381 
TRP   CZ3 CH2  sing Y N 382 
TRP   CZ3 HZ3  sing N N 383 
TRP   CH2 HH2  sing N N 384 
TRP   OXT HXT  sing N N 385 
TYR   N   CA   sing N N 386 
TYR   N   H    sing N N 387 
TYR   N   H2   sing N N 388 
TYR   CA  C    sing N N 389 
TYR   CA  CB   sing N N 390 
TYR   CA  HA   sing N N 391 
TYR   C   O    doub N N 392 
TYR   C   OXT  sing N N 393 
TYR   CB  CG   sing N N 394 
TYR   CB  HB2  sing N N 395 
TYR   CB  HB3  sing N N 396 
TYR   CG  CD1  doub Y N 397 
TYR   CG  CD2  sing Y N 398 
TYR   CD1 CE1  sing Y N 399 
TYR   CD1 HD1  sing N N 400 
TYR   CD2 CE2  doub Y N 401 
TYR   CD2 HD2  sing N N 402 
TYR   CE1 CZ   doub Y N 403 
TYR   CE1 HE1  sing N N 404 
TYR   CE2 CZ   sing Y N 405 
TYR   CE2 HE2  sing N N 406 
TYR   CZ  OH   sing N N 407 
TYR   OH  HH   sing N N 408 
TYR   OXT HXT  sing N N 409 
VAL   N   CA   sing N N 410 
VAL   N   H    sing N N 411 
VAL   N   H2   sing N N 412 
VAL   CA  C    sing N N 413 
VAL   CA  CB   sing N N 414 
VAL   CA  HA   sing N N 415 
VAL   C   O    doub N N 416 
VAL   C   OXT  sing N N 417 
VAL   CB  CG1  sing N N 418 
VAL   CB  CG2  sing N N 419 
VAL   CB  HB   sing N N 420 
VAL   CG1 HG11 sing N N 421 
VAL   CG1 HG12 sing N N 422 
VAL   CG1 HG13 sing N N 423 
VAL   CG2 HG21 sing N N 424 
VAL   CG2 HG22 sing N N 425 
VAL   CG2 HG23 sing N N 426 
VAL   OXT HXT  sing N N 427 
# 
_pdbx_audit_support.funding_organization   'German Research Foundation (DFG)' 
_pdbx_audit_support.country                Germany 
_pdbx_audit_support.grant_number           RTG2202 
_pdbx_audit_support.ordinal                1 
# 
_pdbx_initial_refinement_model.id               1 
_pdbx_initial_refinement_model.entity_id_list   ? 
_pdbx_initial_refinement_model.type             'in silico model' 
_pdbx_initial_refinement_model.source_name      AlphaFold 
_pdbx_initial_refinement_model.accession_code   ? 
_pdbx_initial_refinement_model.details          ? 
# 
_atom_sites.entry_id                    9HHB 
_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]   0.010825 
_atom_sites.fract_transf_matrix[1][2]   0.006250 
_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]   0.012499 
_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]   0.014324 
_atom_sites.fract_transf_vector[1]      0.00000 
_atom_sites.fract_transf_vector[2]      0.00000 
_atom_sites.fract_transf_vector[3]      0.00000 
_atom_sites.solution_primary            ? 
_atom_sites.solution_secondary          ? 
_atom_sites.solution_hydrogens          ? 
_atom_sites.special_details             ? 
# 
loop_
_atom_type.symbol 
C 
N 
O 
S 
# 
loop_
_atom_site.group_PDB 
_atom_site.id 
_atom_site.type_symbol 
_atom_site.label_atom_id 
_atom_site.label_alt_id 
_atom_site.label_comp_id 
_atom_site.label_asym_id 
_atom_site.label_entity_id 
_atom_site.label_seq_id 
_atom_site.pdbx_PDB_ins_code 
_atom_site.Cartn_x 
_atom_site.Cartn_y 
_atom_site.Cartn_z 
_atom_site.occupancy 
_atom_site.B_iso_or_equiv 
_atom_site.pdbx_formal_charge 
_atom_site.auth_seq_id 
_atom_site.auth_comp_id 
_atom_site.auth_asym_id 
_atom_site.auth_atom_id 
_atom_site.pdbx_PDB_model_num 
ATOM   1    N N   . SER   A 1 1   ? 38.036 -6.221  11.918  1.00 58.08  ? 1   SER   A N   1 
ATOM   2    C CA  . SER   A 1 1   ? 36.990 -5.504  11.201  1.00 60.85  ? 1   SER   A CA  1 
ATOM   3    C C   . SER   A 1 1   ? 35.691 -6.301  11.170  1.00 56.26  ? 1   SER   A C   1 
ATOM   4    O O   . SER   A 1 1   ? 35.710 -7.531  11.154  1.00 60.38  ? 1   SER   A O   1 
ATOM   5    C CB  . SER   A 1 1   ? 37.438 -5.184  9.774   1.00 58.07  ? 1   SER   A CB  1 
ATOM   6    O OG  . SER   A 1 1   ? 36.376 -4.625  9.020   1.00 61.81  ? 1   SER   A OG  1 
ATOM   7    N N   . PHE   A 1 2   ? 34.565 -5.583  11.158  1.00 56.91  ? 2   PHE   A N   1 
ATOM   8    C CA  . PHE   A 1 2   ? 33.261 -6.239  11.133  1.00 55.59  ? 2   PHE   A CA  1 
ATOM   9    C C   . PHE   A 1 2   ? 33.107 -7.108  9.891   1.00 53.53  ? 2   PHE   A C   1 
ATOM   10   O O   . PHE   A 1 2   ? 32.769 -8.293  9.986   1.00 51.89  ? 2   PHE   A O   1 
ATOM   11   C CB  . PHE   A 1 2   ? 32.147 -5.192  11.200  1.00 57.13  ? 2   PHE   A CB  1 
ATOM   12   C CG  . PHE   A 1 2   ? 30.761 -5.769  11.089  1.00 56.13  ? 2   PHE   A CG  1 
ATOM   13   C CD1 . PHE   A 1 2   ? 30.119 -6.282  12.204  1.00 56.20  ? 2   PHE   A CD1 1 
ATOM   14   C CD2 . PHE   A 1 2   ? 30.099 -5.794  9.871   1.00 55.38  ? 2   PHE   A CD2 1 
ATOM   15   C CE1 . PHE   A 1 2   ? 28.844 -6.813  12.105  1.00 55.57  ? 2   PHE   A CE1 1 
ATOM   16   C CE2 . PHE   A 1 2   ? 28.826 -6.323  9.766   1.00 55.57  ? 2   PHE   A CE2 1 
ATOM   17   C CZ  . PHE   A 1 2   ? 28.198 -6.833  10.885  1.00 54.78  ? 2   PHE   A CZ  1 
ATOM   18   N N   . ASN   A 1 3   ? 33.353 -6.532  8.711   1.00 53.81  ? 3   ASN   A N   1 
ATOM   19   C CA  . ASN   A 1 3   ? 33.203 -7.294  7.476   1.00 52.10  ? 3   ASN   A CA  1 
ATOM   20   C C   . ASN   A 1 3   ? 34.267 -8.375  7.346   1.00 50.96  ? 3   ASN   A C   1 
ATOM   21   O O   . ASN   A 1 3   ? 34.006 -9.427  6.753   1.00 49.21  ? 3   ASN   A O   1 
ATOM   22   C CB  . ASN   A 1 3   ? 33.245 -6.358  6.269   1.00 53.11  ? 3   ASN   A CB  1 
ATOM   23   C CG  . ASN   A 1 3   ? 32.008 -5.489  6.164   1.00 54.25  ? 3   ASN   A CG  1 
ATOM   24   O OD1 . ASN   A 1 3   ? 30.920 -5.884  6.585   1.00 53.64  ? 3   ASN   A OD1 1 
ATOM   25   N ND2 . ASN   A 1 3   ? 32.168 -4.298  5.599   1.00 56.22  ? 3   ASN   A ND2 1 
ATOM   26   N N   . LYS   A 1 4   ? 35.462 -8.145  7.893   1.00 51.94  ? 4   LYS   A N   1 
ATOM   27   C CA  . LYS   A 1 4   ? 36.514 -9.152  7.805   1.00 53.23  ? 4   LYS   A CA  1 
ATOM   28   C C   . LYS   A 1 4   ? 36.179 -10.395 8.621   1.00 53.93  ? 4   LYS   A C   1 
ATOM   29   O O   . LYS   A 1 4   ? 36.571 -11.505 8.243   1.00 51.63  ? 4   LYS   A O   1 
ATOM   30   C CB  . LYS   A 1 4   ? 37.848 -8.568  8.267   1.00 53.01  ? 4   LYS   A CB  1 
ATOM   31   C CG  . LYS   A 1 4   ? 38.507 -7.645  7.258   1.00 67.44  ? 4   LYS   A CG  1 
ATOM   32   C CD  . LYS   A 1 4   ? 39.853 -7.151  7.765   1.00 72.56  ? 4   LYS   A CD  1 
ATOM   33   C CE  . LYS   A 1 4   ? 40.548 -6.282  6.734   1.00 67.65  ? 4   LYS   A CE  1 
ATOM   34   N NZ  . LYS   A 1 4   ? 41.853 -5.768  7.236   1.00 75.78  ? 4   LYS   A NZ  1 
ATOM   35   N N   . GLN   A 1 5   ? 35.457 -10.236 9.732   1.00 52.64  ? 5   GLN   A N   1 
ATOM   36   C CA  . GLN   A 1 5   ? 35.195 -11.378 10.601  1.00 49.66  ? 5   GLN   A CA  1 
ATOM   37   C C   . GLN   A 1 5   ? 34.164 -12.319 9.989   1.00 51.61  ? 5   GLN   A C   1 
ATOM   38   O O   . GLN   A 1 5   ? 34.389 -13.533 9.915   1.00 51.31  ? 5   GLN   A O   1 
ATOM   39   C CB  . GLN   A 1 5   ? 34.744 -10.906 11.984  1.00 50.91  ? 5   GLN   A CB  1 
ATOM   40   C CG  . GLN   A 1 5   ? 35.840 -10.221 12.787  1.00 69.15  ? 5   GLN   A CG  1 
ATOM   41   C CD  . GLN   A 1 5   ? 37.152 -10.988 12.773  1.00 76.31  ? 5   GLN   A CD  1 
ATOM   42   O OE1 . GLN   A 1 5   ? 38.202 -10.435 12.439  1.00 79.46  ? 5   GLN   A OE1 1 
ATOM   43   N NE2 . GLN   A 1 5   ? 37.101 -12.263 13.147  1.00 59.34  ? 5   GLN   A NE2 1 
ATOM   44   N N   . TRP   A 1 6   ? 33.022 -11.786 9.543   1.00 47.73  ? 6   TRP   A N   1 
ATOM   45   C CA  . TRP   A 1 6   ? 32.019 -12.666 8.955   1.00 49.68  ? 6   TRP   A CA  1 
ATOM   46   C C   . TRP   A 1 6   ? 32.408 -13.122 7.555   1.00 45.42  ? 6   TRP   A C   1 
ATOM   47   O O   . TRP   A 1 6   ? 31.857 -14.114 7.068   1.00 52.80  ? 6   TRP   A O   1 
ATOM   48   C CB  . TRP   A 1 6   ? 30.633 -12.005 8.953   1.00 46.68  ? 6   TRP   A CB  1 
ATOM   49   C CG  . TRP   A 1 6   ? 30.442 -10.811 8.059   1.00 47.39  ? 6   TRP   A CG  1 
ATOM   50   C CD1 . TRP   A 1 6   ? 30.446 -9.500  8.436   1.00 49.17  ? 6   TRP   A CD1 1 
ATOM   51   C CD2 . TRP   A 1 6   ? 30.166 -10.820 6.650   1.00 46.64  ? 6   TRP   A CD2 1 
ATOM   52   N NE1 . TRP   A 1 6   ? 30.209 -8.692  7.350   1.00 49.67  ? 6   TRP   A NE1 1 
ATOM   53   C CE2 . TRP   A 1 6   ? 30.035 -9.477  6.242   1.00 48.13  ? 6   TRP   A CE2 1 
ATOM   54   C CE3 . TRP   A 1 6   ? 30.026 -11.832 5.694   1.00 45.08  ? 6   TRP   A CE3 1 
ATOM   55   C CZ2 . TRP   A 1 6   ? 29.774 -9.120  4.920   1.00 48.13  ? 6   TRP   A CZ2 1 
ATOM   56   C CZ3 . TRP   A 1 6   ? 29.768 -11.475 4.381   1.00 44.97  ? 6   TRP   A CZ3 1 
ATOM   57   C CH2 . TRP   A 1 6   ? 29.642 -10.131 4.008   1.00 46.50  ? 6   TRP   A CH2 1 
ATOM   58   N N   . TYR   A 1 7   ? 33.341 -12.429 6.899   1.00 45.77  ? 7   TYR   A N   1 
ATOM   59   C CA  . TYR   A 1 7   ? 33.970 -12.991 5.708   1.00 45.52  ? 7   TYR   A CA  1 
ATOM   60   C C   . TYR   A 1 7   ? 34.783 -14.225 6.069   1.00 48.78  ? 7   TYR   A C   1 
ATOM   61   O O   . TYR   A 1 7   ? 34.719 -15.253 5.383   1.00 45.07  ? 7   TYR   A O   1 
ATOM   62   C CB  . TYR   A 1 7   ? 34.856 -11.944 5.033   1.00 46.24  ? 7   TYR   A CB  1 
ATOM   63   C CG  . TYR   A 1 7   ? 34.256 -11.319 3.793   1.00 50.11  ? 7   TYR   A CG  1 
ATOM   64   C CD1 . TYR   A 1 7   ? 33.291 -10.326 3.888   1.00 46.99  ? 7   TYR   A CD1 1 
ATOM   65   C CD2 . TYR   A 1 7   ? 34.667 -11.713 2.527   1.00 45.86  ? 7   TYR   A CD2 1 
ATOM   66   C CE1 . TYR   A 1 7   ? 32.747 -9.749  2.758   1.00 47.34  ? 7   TYR   A CE1 1 
ATOM   67   C CE2 . TYR   A 1 7   ? 34.127 -11.141 1.390   1.00 49.31  ? 7   TYR   A CE2 1 
ATOM   68   C CZ  . TYR   A 1 7   ? 33.167 -10.160 1.512   1.00 46.87  ? 7   TYR   A CZ  1 
ATOM   69   O OH  . TYR   A 1 7   ? 32.626 -9.587  0.385   1.00 47.42  ? 7   TYR   A OH  1 
ATOM   70   N N   A LEU   A 1 8   ? 35.565 -14.137 7.148   0.54 45.63  ? 8   LEU   A N   1 
ATOM   71   N N   B LEU   A 1 8   ? 35.563 -14.142 7.151   0.46 45.63  ? 8   LEU   A N   1 
ATOM   72   C CA  A LEU   A 1 8   ? 36.315 -15.293 7.626   0.54 49.37  ? 8   LEU   A CA  1 
ATOM   73   C CA  B LEU   A 1 8   ? 36.315 -15.303 7.616   0.46 49.38  ? 8   LEU   A CA  1 
ATOM   74   C C   A LEU   A 1 8   ? 35.380 -16.415 8.060   0.54 48.73  ? 8   LEU   A C   1 
ATOM   75   C C   B LEU   A 1 8   ? 35.382 -16.420 8.064   0.46 48.72  ? 8   LEU   A C   1 
ATOM   76   O O   A LEU   A 1 8   ? 35.629 -17.590 7.768   0.54 48.61  ? 8   LEU   A O   1 
ATOM   77   O O   B LEU   A 1 8   ? 35.634 -17.599 7.789   0.46 48.62  ? 8   LEU   A O   1 
ATOM   78   C CB  A LEU   A 1 8   ? 37.225 -14.878 8.782   0.54 47.38  ? 8   LEU   A CB  1 
ATOM   79   C CB  B LEU   A 1 8   ? 37.252 -14.903 8.756   0.46 47.41  ? 8   LEU   A CB  1 
ATOM   80   C CG  A LEU   A 1 8   ? 37.762 -15.994 9.681   0.54 54.15  ? 8   LEU   A CG  1 
ATOM   81   C CG  B LEU   A 1 8   ? 38.541 -14.163 8.391   0.46 50.16  ? 8   LEU   A CG  1 
ATOM   82   C CD1 A LEU   A 1 8   ? 38.777 -16.854 8.943   0.54 55.08  ? 8   LEU   A CD1 1 
ATOM   83   C CD1 B LEU   A 1 8   ? 39.287 -13.742 9.647   0.46 52.44  ? 8   LEU   A CD1 1 
ATOM   84   C CD2 A LEU   A 1 8   ? 38.359 -15.417 10.957  0.54 56.03  ? 8   LEU   A CD2 1 
ATOM   85   C CD2 B LEU   A 1 8   ? 39.425 -15.032 7.512   0.46 48.44  ? 8   LEU   A CD2 1 
ATOM   86   N N   . LEU   A 1 9   ? 34.297 -16.069 8.758   1.00 50.62  ? 9   LEU   A N   1 
ATOM   87   C CA  . LEU   A 1 9   ? 33.368 -17.086 9.234   1.00 44.47  ? 9   LEU   A CA  1 
ATOM   88   C C   . LEU   A 1 9   ? 32.619 -17.734 8.075   1.00 48.09  ? 9   LEU   A C   1 
ATOM   89   O O   . LEU   A 1 9   ? 32.373 -18.945 8.090   1.00 44.02  ? 9   LEU   A O   1 
ATOM   90   C CB  . LEU   A 1 9   ? 32.394 -16.471 10.239  1.00 44.73  ? 9   LEU   A CB  1 
ATOM   91   C CG  . LEU   A 1 9   ? 31.739 -17.431 11.231  1.00 62.93  ? 9   LEU   A CG  1 
ATOM   92   C CD1 . LEU   A 1 9   ? 32.800 -18.217 11.987  1.00 63.46  ? 9   LEU   A CD1 1 
ATOM   93   C CD2 . LEU   A 1 9   ? 30.840 -16.673 12.198  1.00 53.54  ? 9   LEU   A CD2 1 
ATOM   94   N N   . ALA   A 1 10  ? 32.261 -16.947 7.056   1.00 45.19  ? 10  ALA   A N   1 
ATOM   95   C CA  . ALA   A 1 10  ? 31.590 -17.515 5.890   1.00 47.43  ? 10  ALA   A CA  1 
ATOM   96   C C   . ALA   A 1 10  ? 32.516 -18.450 5.122   1.00 46.36  ? 10  ALA   A C   1 
ATOM   97   O O   . ALA   A 1 10  ? 32.065 -19.452 4.556   1.00 49.30  ? 10  ALA   A O   1 
ATOM   98   C CB  . ALA   A 1 10  ? 31.077 -16.400 4.979   1.00 41.12  ? 10  ALA   A CB  1 
ATOM   99   N N   . ASN   A 1 11  ? 33.814 -18.135 5.085   1.00 44.79  ? 11  ASN   A N   1 
ATOM   100  C CA  . ASN   A 1 11  ? 34.771 -19.015 4.424   1.00 44.56  ? 11  ASN   A CA  1 
ATOM   101  C C   . ASN   A 1 11  ? 34.885 -20.349 5.151   1.00 46.68  ? 11  ASN   A C   1 
ATOM   102  O O   . ASN   A 1 11  ? 34.944 -21.409 4.516   1.00 47.94  ? 11  ASN   A O   1 
ATOM   103  C CB  . ASN   A 1 11  ? 36.138 -18.334 4.335   1.00 45.03  ? 11  ASN   A CB  1 
ATOM   104  C CG  . ASN   A 1 11  ? 36.356 -17.630 3.010   1.00 54.16  ? 11  ASN   A CG  1 
ATOM   105  O OD1 . ASN   A 1 11  ? 36.171 -18.219 1.944   1.00 51.88  ? 11  ASN   A OD1 1 
ATOM   106  N ND2 . ASN   A 1 11  ? 36.749 -16.362 3.070   1.00 58.71  ? 11  ASN   A ND2 1 
ATOM   107  N N   . GLN   A 1 12  ? 34.918 -20.316 6.485   1.00 42.43  ? 12  GLN   A N   1 
ATOM   108  C CA  . GLN   A 1 12  ? 34.995 -21.555 7.251   1.00 46.51  ? 12  GLN   A CA  1 
ATOM   109  C C   . GLN   A 1 12  ? 33.727 -22.384 7.086   1.00 44.68  ? 12  GLN   A C   1 
ATOM   110  O O   . GLN   A 1 12  ? 33.788 -23.616 6.987   1.00 49.42  ? 12  GLN   A O   1 
ATOM   111  C CB  . GLN   A 1 12  ? 35.242 -21.246 8.729   1.00 44.11  ? 12  GLN   A CB  1 
ATOM   112  C CG  . GLN   A 1 12  ? 36.623 -20.685 9.033   1.00 65.42  ? 12  GLN   A CG  1 
ATOM   113  C CD  . GLN   A 1 12  ? 36.735 -20.158 10.452  1.00 74.76  ? 12  GLN   A CD  1 
ATOM   114  O OE1 . GLN   A 1 12  ? 35.832 -19.481 10.945  1.00 72.70  ? 12  GLN   A OE1 1 
ATOM   115  N NE2 . GLN   A 1 12  ? 37.842 -20.472 11.118  1.00 89.21  ? 12  GLN   A NE2 1 
ATOM   116  N N   . ILE   A 1 13  ? 32.569 -21.725 7.045   1.00 49.11  ? 13  ILE   A N   1 
ATOM   117  C CA  . ILE   A 1 13  ? 31.305 -22.445 6.938   1.00 42.81  ? 13  ILE   A CA  1 
ATOM   118  C C   . ILE   A 1 13  ? 31.173 -23.092 5.564   1.00 44.21  ? 13  ILE   A C   1 
ATOM   119  O O   . ILE   A 1 13  ? 30.800 -24.265 5.447   1.00 43.88  ? 13  ILE   A O   1 
ATOM   120  C CB  . ILE   A 1 13  ? 30.125 -21.502 7.236   1.00 40.55  ? 13  ILE   A CB  1 
ATOM   121  C CG1 . ILE   A 1 13  ? 30.122 -21.100 8.712   1.00 41.70  ? 13  ILE   A CG1 1 
ATOM   122  C CG2 . ILE   A 1 13  ? 28.809 -22.154 6.856   1.00 40.00  ? 13  ILE   A CG2 1 
ATOM   123  C CD1 . ILE   A 1 13  ? 29.066 -20.074 9.060   1.00 41.95  ? 13  ILE   A CD1 1 
ATOM   124  N N   . ILE   A 1 14  ? 31.483 -22.340 4.503   1.00 41.33  ? 14  ILE   A N   1 
ATOM   125  C CA  . ILE   A 1 14  ? 31.368 -22.888 3.154   1.00 39.01  ? 14  ILE   A CA  1 
ATOM   126  C C   . ILE   A 1 14  ? 32.380 -24.005 2.939   1.00 50.37  ? 14  ILE   A C   1 
ATOM   127  O O   . ILE   A 1 14  ? 32.148 -24.921 2.140   1.00 47.70  ? 14  ILE   A O   1 
ATOM   128  C CB  . ILE   A 1 14  ? 31.522 -21.772 2.099   1.00 44.56  ? 14  ILE   A CB  1 
ATOM   129  C CG1 . ILE   A 1 14  ? 31.034 -22.253 0.730   1.00 45.03  ? 14  ILE   A CG1 1 
ATOM   130  C CG2 . ILE   A 1 14  ? 32.965 -21.307 1.999   1.00 43.79  ? 14  ILE   A CG2 1 
ATOM   131  C CD1 . ILE   A 1 14  ? 29.547 -22.507 0.666   1.00 42.20  ? 14  ILE   A CD1 1 
ATOM   132  N N   . GLN   A 1 15  ? 33.506 -23.960 3.655   1.00 47.41  ? 15  GLN   A N   1 
ATOM   133  C CA  . GLN   A 1 15  ? 34.494 -25.026 3.538   1.00 44.42  ? 15  GLN   A CA  1 
ATOM   134  C C   . GLN   A 1 15  ? 34.009 -26.299 4.220   1.00 47.01  ? 15  GLN   A C   1 
ATOM   135  O O   . GLN   A 1 15  ? 34.273 -27.407 3.739   1.00 44.66  ? 15  GLN   A O   1 
ATOM   136  C CB  . GLN   A 1 15  ? 35.827 -24.571 4.129   1.00 48.73  ? 15  GLN   A CB  1 
ATOM   137  C CG  . GLN   A 1 15  ? 37.005 -25.439 3.730   1.00 77.25  ? 15  GLN   A CG  1 
ATOM   138  C CD  . GLN   A 1 15  ? 37.374 -25.281 2.266   1.00 88.60  ? 15  GLN   A CD  1 
ATOM   139  O OE1 . GLN   A 1 15  ? 37.497 -26.265 1.534   1.00 76.64  ? 15  GLN   A OE1 1 
ATOM   140  N NE2 . GLN   A 1 15  ? 37.562 -24.039 1.836   1.00 71.52  ? 15  GLN   A NE2 1 
ATOM   141  N N   . SER   A 1 16  ? 33.291 -26.159 5.338   1.00 41.76  ? 16  SER   A N   1 
ATOM   142  C CA  . SER   A 1 16  ? 32.747 -27.329 6.017   1.00 48.15  ? 16  SER   A CA  1 
ATOM   143  C C   . SER   A 1 16  ? 31.642 -27.985 5.201   1.00 47.13  ? 16  SER   A C   1 
ATOM   144  O O   . SER   A 1 16  ? 31.467 -29.207 5.267   1.00 45.97  ? 16  SER   A O   1 
ATOM   145  C CB  . SER   A 1 16  ? 32.225 -26.943 7.401   1.00 43.52  ? 16  SER   A CB  1 
ATOM   146  O OG  . SER   A 1 16  ? 31.045 -26.164 7.303   1.00 51.68  ? 16  SER   A OG  1 
ATOM   147  N N   . LEU   A 1 17  ? 30.884 -27.194 4.437   1.00 41.84  ? 17  LEU   A N   1 
ATOM   148  C CA  . LEU   A 1 17  ? 29.895 -27.772 3.534   1.00 39.62  ? 17  LEU   A CA  1 
ATOM   149  C C   . LEU   A 1 17  ? 30.559 -28.554 2.409   1.00 44.56  ? 17  LEU   A C   1 
ATOM   150  O O   . LEU   A 1 17  ? 30.010 -29.560 1.947   1.00 46.69  ? 17  LEU   A O   1 
ATOM   151  C CB  . LEU   A 1 17  ? 28.999 -26.677 2.955   1.00 38.46  ? 17  LEU   A CB  1 
ATOM   152  C CG  . LEU   A 1 17  ? 28.261 -25.770 3.942   1.00 39.95  ? 17  LEU   A CG  1 
ATOM   153  C CD1 . LEU   A 1 17  ? 27.332 -24.822 3.201   1.00 37.71  ? 17  LEU   A CD1 1 
ATOM   154  C CD2 . LEU   A 1 17  ? 27.492 -26.589 4.964   1.00 42.17  ? 17  LEU   A CD2 1 
ATOM   155  N N   . SER   A 1 18  ? 31.733 -28.109 1.958   1.00 39.95  ? 18  SER   A N   1 
ATOM   156  C CA  . SER   A 1 18  ? 32.442 -28.832 0.910   1.00 40.45  ? 18  SER   A CA  1 
ATOM   157  C C   . SER   A 1 18  ? 33.002 -30.152 1.424   1.00 49.00  ? 18  SER   A C   1 
ATOM   158  O O   . SER   A 1 18  ? 33.107 -31.119 0.661   1.00 54.15  ? 18  SER   A O   1 
ATOM   159  C CB  . SER   A 1 18  ? 33.563 -27.961 0.341   1.00 43.44  ? 18  SER   A CB  1 
ATOM   160  O OG  . SER   A 1 18  ? 33.054 -26.729 -0.144  1.00 46.96  ? 18  SER   A OG  1 
ATOM   161  N N   . LYS   A 1 19  ? 33.361 -30.212 2.706   1.00 46.88  ? 19  LYS   A N   1 
ATOM   162  C CA  . LYS   A 1 19  ? 33.876 -31.431 3.313   1.00 44.87  ? 19  LYS   A CA  1 
ATOM   163  C C   . LYS   A 1 19  ? 32.776 -32.347 3.834   1.00 45.22  ? 19  LYS   A C   1 
ATOM   164  O O   . LYS   A 1 19  ? 33.070 -33.480 4.231   1.00 51.60  ? 19  LYS   A O   1 
ATOM   165  C CB  . LYS   A 1 19  ? 34.836 -31.081 4.455   1.00 47.17  ? 19  LYS   A CB  1 
ATOM   166  C CG  . LYS   A 1 19  ? 35.994 -30.191 4.029   1.00 58.65  ? 19  LYS   A CG  1 
ATOM   167  C CD  . LYS   A 1 19  ? 36.712 -29.588 5.226   1.00 65.45  ? 19  LYS   A CD  1 
ATOM   168  C CE  . LYS   A 1 19  ? 37.382 -30.658 6.070   1.00 72.32  ? 19  LYS   A CE  1 
ATOM   169  N N   . TYR   A 1 20  ? 31.526 -31.891 3.839   1.00 45.55  ? 20  TYR   A N   1 
ATOM   170  C CA  . TYR   A 1 20  ? 30.429 -32.719 4.314   1.00 47.28  ? 20  TYR   A CA  1 
ATOM   171  C C   . TYR   A 1 20  ? 30.198 -33.891 3.367   1.00 47.26  ? 20  TYR   A C   1 
ATOM   172  O O   . TYR   A 1 20  ? 30.432 -33.799 2.158   1.00 47.92  ? 20  TYR   A O   1 
ATOM   173  C CB  . TYR   A 1 20  ? 29.152 -31.888 4.447   1.00 48.79  ? 20  TYR   A CB  1 
ATOM   174  C CG  . TYR   A 1 20  ? 28.093 -32.519 5.323   1.00 50.47  ? 20  TYR   A CG  1 
ATOM   175  C CD1 . TYR   A 1 20  ? 28.083 -32.306 6.695   1.00 57.51  ? 20  TYR   A CD1 1 
ATOM   176  C CD2 . TYR   A 1 20  ? 27.101 -33.325 4.778   1.00 50.55  ? 20  TYR   A CD2 1 
ATOM   177  C CE1 . TYR   A 1 20  ? 27.116 -32.879 7.502   1.00 59.39  ? 20  TYR   A CE1 1 
ATOM   178  C CE2 . TYR   A 1 20  ? 26.131 -33.902 5.575   1.00 56.92  ? 20  TYR   A CE2 1 
ATOM   179  C CZ  . TYR   A 1 20  ? 26.142 -33.676 6.937   1.00 56.99  ? 20  TYR   A CZ  1 
ATOM   180  O OH  . TYR   A 1 20  ? 25.178 -34.248 7.736   1.00 62.39  ? 20  TYR   A OH  1 
ATOM   181  N N   . GLU   A 1 21  ? 29.739 -35.005 3.935   1.00 46.45  ? 21  GLU   A N   1 
ATOM   182  C CA  . GLU   A 1 21  ? 29.514 -36.224 3.168   1.00 50.58  ? 21  GLU   A CA  1 
ATOM   183  C C   . GLU   A 1 21  ? 28.529 -35.971 2.032   1.00 55.26  ? 21  GLU   A C   1 
ATOM   184  O O   . GLU   A 1 21  ? 27.384 -35.573 2.265   1.00 50.40  ? 21  GLU   A O   1 
ATOM   185  C CB  . GLU   A 1 21  ? 29.001 -37.326 4.095   1.00 49.95  ? 21  GLU   A CB  1 
ATOM   186  C CG  . GLU   A 1 21  ? 28.654 -38.633 3.407   1.00 62.17  ? 21  GLU   A CG  1 
ATOM   187  C CD  . GLU   A 1 21  ? 28.417 -39.758 4.398   1.00 71.88  ? 21  GLU   A CD  1 
ATOM   188  O OE1 . GLU   A 1 21  ? 29.372 -40.137 5.109   1.00 90.39  ? 21  GLU   A OE1 1 
ATOM   189  O OE2 . GLU   A 1 21  ? 27.275 -40.258 4.475   1.00 77.60  ? 21  GLU   A OE2 1 
ATOM   190  N N   . GLY   A 1 22  ? 28.984 -36.195 0.800   1.00 51.27  ? 22  GLY   A N   1 
ATOM   191  C CA  . GLY   A 1 22  ? 28.190 -35.915 -0.377  1.00 45.80  ? 22  GLY   A CA  1 
ATOM   192  C C   . GLY   A 1 22  ? 28.198 -34.472 -0.830  1.00 45.37  ? 22  GLY   A C   1 
ATOM   193  O O   . GLY   A 1 22  ? 27.544 -34.152 -1.831  1.00 42.10  ? 22  GLY   A O   1 
ATOM   194  N N   . GLY   A 1 23  ? 28.922 -33.591 -0.136  1.00 45.80  ? 23  GLY   A N   1 
ATOM   195  C CA  . GLY   A 1 23  ? 28.922 -32.181 -0.485  1.00 40.38  ? 23  GLY   A CA  1 
ATOM   196  C C   . GLY   A 1 23  ? 29.585 -31.866 -1.808  1.00 43.66  ? 23  GLY   A C   1 
ATOM   197  O O   . GLY   A 1 23  ? 29.413 -30.757 -2.325  1.00 39.33  ? 23  GLY   A O   1 
ATOM   198  N N   . HIS   A 1 24  ? 30.339 -32.815 -2.368  1.00 42.73  ? 24  HIS   A N   1 
ATOM   199  C CA  . HIS   A 1 24  ? 31.036 -32.574 -3.626  1.00 41.17  ? 24  HIS   A CA  1 
ATOM   200  C C   . HIS   A 1 24  ? 30.080 -32.319 -4.783  1.00 44.77  ? 24  HIS   A C   1 
ATOM   201  O O   . HIS   A 1 24  ? 30.480 -31.707 -5.778  1.00 46.51  ? 24  HIS   A O   1 
ATOM   202  C CB  . HIS   A 1 24  ? 31.942 -33.762 -3.955  1.00 43.02  ? 24  HIS   A CB  1 
ATOM   203  C CG  . HIS   A 1 24  ? 31.211 -35.063 -4.060  1.00 45.95  ? 24  HIS   A CG  1 
ATOM   204  N ND1 . HIS   A 1 24  ? 31.030 -35.904 -2.983  1.00 45.97  ? 24  HIS   A ND1 1 
ATOM   205  C CD2 . HIS   A 1 24  ? 30.607 -35.664 -5.112  1.00 45.51  ? 24  HIS   A CD2 1 
ATOM   206  C CE1 . HIS   A 1 24  ? 30.349 -36.969 -3.368  1.00 50.93  ? 24  HIS   A CE1 1 
ATOM   207  N NE2 . HIS   A 1 24  ? 30.080 -36.848 -4.656  1.00 50.48  ? 24  HIS   A NE2 1 
ATOM   208  N N   . ILE   A 1 25  ? 28.827 -32.770 -4.677  1.00 40.05  ? 25  ILE   A N   1 
ATOM   209  C CA  . ILE   A 1 25  ? 27.877 -32.563 -5.761  1.00 42.46  ? 25  ILE   A CA  1 
ATOM   210  C C   . ILE   A 1 25  ? 27.454 -31.105 -5.864  1.00 43.08  ? 25  ILE   A C   1 
ATOM   211  O O   . ILE   A 1 25  ? 26.985 -30.672 -6.923  1.00 47.99  ? 25  ILE   A O   1 
ATOM   212  C CB  . ILE   A 1 25  ? 26.649 -33.476 -5.587  1.00 42.62  ? 25  ILE   A CB  1 
ATOM   213  C CG1 . ILE   A 1 25  ? 25.783 -33.000 -4.421  1.00 39.03  ? 25  ILE   A CG1 1 
ATOM   214  C CG2 . ILE   A 1 25  ? 27.087 -34.917 -5.362  1.00 45.77  ? 25  ILE   A CG2 1 
ATOM   215  C CD1 . ILE   A 1 25  ? 24.481 -33.750 -4.293  1.00 39.85  ? 25  ILE   A CD1 1 
ATOM   216  N N   . PHE   A 1 26  ? 27.611 -30.330 -4.791  1.00 40.26  ? 26  PHE   A N   1 
ATOM   217  C CA  . PHE   A 1 26  ? 27.306 -28.906 -4.805  1.00 36.59  ? 26  PHE   A CA  1 
ATOM   218  C C   . PHE   A 1 26  ? 28.546 -28.040 -4.969  1.00 40.29  ? 26  PHE   A C   1 
ATOM   219  O O   . PHE   A 1 26  ? 28.436 -26.811 -4.931  1.00 47.13  ? 26  PHE   A O   1 
ATOM   220  C CB  . PHE   A 1 26  ? 26.574 -28.506 -3.519  1.00 39.49  ? 26  PHE   A CB  1 
ATOM   221  C CG  . PHE   A 1 26  ? 25.313 -29.280 -3.268  1.00 36.51  ? 26  PHE   A CG  1 
ATOM   222  C CD1 . PHE   A 1 26  ? 24.203 -29.104 -4.073  1.00 36.22  ? 26  PHE   A CD1 1 
ATOM   223  C CD2 . PHE   A 1 26  ? 25.234 -30.173 -2.212  1.00 42.37  ? 26  PHE   A CD2 1 
ATOM   224  C CE1 . PHE   A 1 26  ? 23.038 -29.811 -3.840  1.00 41.59  ? 26  PHE   A CE1 1 
ATOM   225  C CE2 . PHE   A 1 26  ? 24.074 -30.883 -1.973  1.00 42.95  ? 26  PHE   A CE2 1 
ATOM   226  C CZ  . PHE   A 1 26  ? 22.974 -30.702 -2.789  1.00 39.74  ? 26  PHE   A CZ  1 
ATOM   227  N N   . GLU   A 1 27  ? 29.721 -28.649 -5.148  1.00 40.35  ? 27  GLU   A N   1 
ATOM   228  C CA  . GLU   A 1 27  ? 30.952 -27.870 -5.239  1.00 42.48  ? 27  GLU   A CA  1 
ATOM   229  C C   . GLU   A 1 27  ? 31.006 -27.074 -6.536  1.00 38.85  ? 27  GLU   A C   1 
ATOM   230  O O   . GLU   A 1 27  ? 31.226 -25.858 -6.520  1.00 44.25  ? 27  GLU   A O   1 
ATOM   231  C CB  . GLU   A 1 27  ? 32.169 -28.790 -5.122  1.00 39.26  ? 27  GLU   A CB  1 
ATOM   232  C CG  . GLU   A 1 27  ? 33.497 -28.053 -5.076  1.00 43.78  ? 27  GLU   A CG  1 
ATOM   233  C CD  . GLU   A 1 27  ? 33.642 -27.195 -3.831  1.00 52.55  ? 27  GLU   A CD  1 
ATOM   234  O OE1 . GLU   A 1 27  ? 33.015 -27.526 -2.802  1.00 49.43  ? 27  GLU   A OE1 1 
ATOM   235  O OE2 . GLU   A 1 27  ? 34.381 -26.188 -3.881  1.00 47.28  ? 27  GLU   A OE2 1 
ATOM   236  N N   . LYS   A 1 28  ? 30.809 -27.739 -7.669  1.00 42.91  ? 28  LYS   A N   1 
ATOM   237  C CA  . LYS   A 1 28  ? 30.858 -27.093 -8.969  1.00 41.13  ? 28  LYS   A CA  1 
ATOM   238  C C   . LYS   A 1 28  ? 29.460 -26.997 -9.565  1.00 44.44  ? 28  LYS   A C   1 
ATOM   239  O O   . LYS   A 1 28  ? 28.523 -27.676 -9.132  1.00 38.88  ? 28  LYS   A O   1 
ATOM   240  C CB  . LYS   A 1 28  ? 31.783 -27.851 -9.930  1.00 40.63  ? 28  LYS   A CB  1 
ATOM   241  C CG  . LYS   A 1 28  ? 33.146 -28.191 -9.349  1.00 45.48  ? 28  LYS   A CG  1 
ATOM   242  C CD  . LYS   A 1 28  ? 33.839 -26.971 -8.759  1.00 52.76  ? 28  LYS   A CD  1 
ATOM   243  C CE  . LYS   A 1 28  ? 34.179 -25.943 -9.825  1.00 63.53  ? 28  LYS   A CE  1 
ATOM   244  N N   . LEU   A 1 29  ? 29.333 -26.134 -10.568 1.00 42.18  ? 29  LEU   A N   1 
ATOM   245  C CA  . LEU   A 1 29  ? 28.077 -26.000 -11.289 1.00 42.81  ? 29  LEU   A CA  1 
ATOM   246  C C   . LEU   A 1 29  ? 27.824 -27.240 -12.139 1.00 42.73  ? 29  LEU   A C   1 
ATOM   247  O O   . LEU   A 1 29  ? 28.754 -27.869 -12.653 1.00 43.20  ? 29  LEU   A O   1 
ATOM   248  C CB  . LEU   A 1 29  ? 28.096 -24.748 -12.166 1.00 39.43  ? 29  LEU   A CB  1 
ATOM   249  C CG  . LEU   A 1 29  ? 28.091 -23.412 -11.419 1.00 47.00  ? 29  LEU   A CG  1 
ATOM   250  C CD1 . LEU   A 1 29  ? 28.564 -22.283 -12.322 1.00 41.81  ? 29  LEU   A CD1 1 
ATOM   251  C CD2 . LEU   A 1 29  ? 26.702 -23.117 -10.874 1.00 39.99  ? 29  LEU   A CD2 1 
ATOM   252  N N   . VAL   A 1 30  ? 26.546 -27.588 -12.282 1.00 39.86  ? 30  VAL   A N   1 
ATOM   253  C CA  . VAL   A 1 30  ? 26.175 -28.805 -12.992 1.00 42.59  ? 30  VAL   A CA  1 
ATOM   254  C C   . VAL   A 1 30  ? 26.519 -28.671 -14.469 1.00 39.07  ? 30  VAL   A C   1 
ATOM   255  O O   . VAL   A 1 30  ? 26.170 -27.676 -15.118 1.00 46.17  ? 30  VAL   A O   1 
ATOM   256  C CB  . VAL   A 1 30  ? 24.682 -29.100 -12.798 1.00 43.89  ? 30  VAL   A CB  1 
ATOM   257  C CG1 . VAL   A 1 30  ? 24.260 -30.276 -13.660 1.00 47.29  ? 30  VAL   A CG1 1 
ATOM   258  C CG2 . VAL   A 1 30  ? 24.380 -29.371 -11.333 1.00 47.70  ? 30  VAL   A CG2 1 
ATOM   259  N N   . ASP   A 1 31  ? 27.216 -29.671 -15.006 1.00 42.23  ? 31  ASP   A N   1 
ATOM   260  C CA  . ASP   A 1 31  ? 27.416 -29.796 -16.444 1.00 45.71  ? 31  ASP   A CA  1 
ATOM   261  C C   . ASP   A 1 31  ? 26.210 -30.526 -17.024 1.00 48.73  ? 31  ASP   A C   1 
ATOM   262  O O   . ASP   A 1 31  ? 25.960 -31.686 -16.681 1.00 48.53  ? 31  ASP   A O   1 
ATOM   263  C CB  . ASP   A 1 31  ? 28.712 -30.546 -16.751 1.00 47.61  ? 31  ASP   A CB  1 
ATOM   264  C CG  . ASP   A 1 31  ? 29.127 -30.440 -18.212 1.00 51.91  ? 31  ASP   A CG  1 
ATOM   265  O OD1 . ASP   A 1 31  ? 28.244 -30.440 -19.099 1.00 52.08  ? 31  ASP   A OD1 1 
ATOM   266  O OD2 . ASP   A 1 31  ? 30.346 -30.356 -18.475 1.00 48.07  ? 31  ASP   A OD2 1 
ATOM   267  N N   . ALA   A 1 32  ? 25.459 -29.840 -17.889 1.00 50.48  ? 32  ALA   A N   1 
ATOM   268  C CA  . ALA   A 1 32  ? 24.198 -30.390 -18.379 1.00 47.81  ? 32  ALA   A CA  1 
ATOM   269  C C   . ALA   A 1 32  ? 24.415 -31.663 -19.188 1.00 51.39  ? 32  ALA   A C   1 
ATOM   270  O O   . ALA   A 1 32  ? 23.643 -32.621 -19.067 1.00 49.85  ? 32  ALA   A O   1 
ATOM   271  C CB  . ALA   A 1 32  ? 23.457 -29.346 -19.214 1.00 51.10  ? 32  ALA   A CB  1 
ATOM   272  N N   . LYS   A 1 33  ? 25.460 -31.696 -20.017 1.00 49.02  ? 33  LYS   A N   1 
ATOM   273  C CA  . LYS   A 1 33  ? 25.715 -32.875 -20.839 1.00 62.30  ? 33  LYS   A CA  1 
ATOM   274  C C   . LYS   A 1 33  ? 26.346 -34.000 -20.027 1.00 57.44  ? 33  LYS   A C   1 
ATOM   275  O O   . LYS   A 1 33  ? 25.926 -35.159 -20.127 1.00 56.60  ? 33  LYS   A O   1 
ATOM   276  C CB  . LYS   A 1 33  ? 26.609 -32.508 -22.025 1.00 62.14  ? 33  LYS   A CB  1 
ATOM   277  C CG  . LYS   A 1 33  ? 25.910 -31.703 -23.107 1.00 72.13  ? 33  LYS   A CG  1 
ATOM   278  N N   . LYS   A 1 34  ? 27.354 -33.678 -19.214 1.00 58.08  ? 34  LYS   A N   1 
ATOM   279  C CA  . LYS   A 1 34  ? 28.071 -34.715 -18.479 1.00 57.21  ? 34  LYS   A CA  1 
ATOM   280  C C   . LYS   A 1 34  ? 27.181 -35.380 -17.435 1.00 51.31  ? 34  LYS   A C   1 
ATOM   281  O O   . LYS   A 1 34  ? 27.197 -36.607 -17.291 1.00 59.93  ? 34  LYS   A O   1 
ATOM   282  C CB  . LYS   A 1 34  ? 29.322 -34.129 -17.825 1.00 54.63  ? 34  LYS   A CB  1 
ATOM   283  C CG  . LYS   A 1 34  ? 30.437 -33.787 -18.805 1.00 64.26  ? 34  LYS   A CG  1 
ATOM   284  N N   . GLN   A 1 35  ? 26.394 -34.593 -16.703 1.00 54.04  ? 35  GLN   A N   1 
ATOM   285  C CA  . GLN   A 1 35  ? 25.535 -35.130 -15.655 1.00 54.61  ? 35  GLN   A CA  1 
ATOM   286  C C   . GLN   A 1 35  ? 24.211 -35.677 -16.182 1.00 53.57  ? 35  GLN   A C   1 
ATOM   287  O O   . GLN   A 1 35  ? 23.346 -36.036 -15.374 1.00 49.00  ? 35  GLN   A O   1 
ATOM   288  C CB  . GLN   A 1 35  ? 25.268 -34.062 -14.591 1.00 52.63  ? 35  GLN   A CB  1 
ATOM   289  C CG  . GLN   A 1 35  ? 26.141 -34.183 -13.345 1.00 52.49  ? 35  GLN   A CG  1 
ATOM   290  C CD  . GLN   A 1 35  ? 27.546 -33.652 -13.551 1.00 61.61  ? 35  GLN   A CD  1 
ATOM   291  O OE1 . GLN   A 1 35  ? 27.747 -32.452 -13.740 1.00 49.96  ? 35  GLN   A OE1 1 
ATOM   292  N NE2 . GLN   A 1 35  ? 28.529 -34.547 -13.510 1.00 63.13  ? 35  GLN   A NE2 1 
ATOM   293  N N   . ASN   A 1 36  ? 24.035 -35.739 -17.505 1.00 50.68  ? 36  ASN   A N   1 
ATOM   294  C CA  . ASN   A 1 36  ? 22.862 -36.356 -18.128 1.00 51.91  ? 36  ASN   A CA  1 
ATOM   295  C C   . ASN   A 1 36  ? 21.565 -35.682 -17.678 1.00 57.70  ? 36  ASN   A C   1 
ATOM   296  O O   . ASN   A 1 36  ? 20.576 -36.338 -17.343 1.00 56.27  ? 36  ASN   A O   1 
ATOM   297  C CB  . ASN   A 1 36  ? 22.828 -37.861 -17.853 1.00 52.54  ? 36  ASN   A CB  1 
ATOM   298  C CG  . ASN   A 1 36  ? 23.999 -38.589 -18.479 1.00 58.32  ? 36  ASN   A CG  1 
ATOM   299  O OD1 . ASN   A 1 36  ? 24.841 -39.151 -17.778 1.00 63.95  ? 36  ASN   A OD1 1 
ATOM   300  N ND2 . ASN   A 1 36  ? 24.057 -38.586 -19.805 1.00 66.91  ? 36  ASN   A ND2 1 
ATOM   301  N N   A CYS   A 1 37  ? 21.578 -34.350 -17.678 0.61 52.13  ? 37  CYS   A N   1 
ATOM   302  N N   B CYS   A 1 37  ? 21.581 -34.351 -17.673 0.39 52.53  ? 37  CYS   A N   1 
ATOM   303  C CA  A CYS   A 1 37  ? 20.412 -33.541 -17.313 0.61 51.11  ? 37  CYS   A CA  1 
ATOM   304  C CA  B CYS   A 1 37  ? 20.416 -33.541 -17.313 0.39 51.09  ? 37  CYS   A CA  1 
ATOM   305  C C   A CYS   A 1 37  ? 20.356 -32.326 -18.230 0.61 48.39  ? 37  CYS   A C   1 
ATOM   306  C C   B CYS   A 1 37  ? 20.370 -32.329 -18.233 0.39 48.31  ? 37  CYS   A C   1 
ATOM   307  O O   A CYS   A 1 37  ? 20.667 -31.199 -17.824 0.61 46.81  ? 37  CYS   A O   1 
ATOM   308  O O   B CYS   A 1 37  ? 20.707 -31.208 -17.834 0.39 45.89  ? 37  CYS   A O   1 
ATOM   309  C CB  A CYS   A 1 37  ? 20.475 -33.132 -15.841 0.61 49.70  ? 37  CYS   A CB  1 
ATOM   310  C CB  B CYS   A 1 37  ? 20.473 -33.124 -15.842 0.39 49.71  ? 37  CYS   A CB  1 
ATOM   311  S SG  A CYS   A 1 37  ? 22.061 -32.431 -15.352 0.61 48.62  ? 37  CYS   A SG  1 
ATOM   312  S SG  B CYS   A 1 37  ? 20.436 -34.502 -14.674 0.39 50.87  ? 37  CYS   A SG  1 
ATOM   313  N N   . PRO   A 1 38  ? 19.948 -32.523 -19.486 1.00 50.48  ? 38  PRO   A N   1 
ATOM   314  C CA  . PRO   A 1 38  ? 19.986 -31.418 -20.458 1.00 52.79  ? 38  PRO   A CA  1 
ATOM   315  C C   . PRO   A 1 38  ? 18.988 -30.309 -20.180 1.00 49.29  ? 38  PRO   A C   1 
ATOM   316  O O   . PRO   A 1 38  ? 19.109 -29.235 -20.782 1.00 49.40  ? 38  PRO   A O   1 
ATOM   317  C CB  . PRO   A 1 38  ? 19.675 -32.112 -21.793 1.00 57.00  ? 38  PRO   A CB  1 
ATOM   318  C CG  . PRO   A 1 38  ? 19.800 -33.597 -21.517 1.00 59.05  ? 38  PRO   A CG  1 
ATOM   319  C CD  . PRO   A 1 38  ? 19.439 -33.767 -20.084 1.00 44.58  ? 38  PRO   A CD  1 
ATOM   320  N N   . ASP   A 1 39  ? 18.016 -30.525 -19.297 1.00 43.38  ? 39  ASP   A N   1 
ATOM   321  C CA  . ASP   A 1 39  ? 17.008 -29.526 -18.976 1.00 47.09  ? 39  ASP   A CA  1 
ATOM   322  C C   . ASP   A 1 39  ? 17.297 -28.801 -17.670 1.00 47.16  ? 39  ASP   A C   1 
ATOM   323  O O   . ASP   A 1 39  ? 16.412 -28.117 -17.148 1.00 55.45  ? 39  ASP   A O   1 
ATOM   324  C CB  . ASP   A 1 39  ? 15.625 -30.177 -18.906 1.00 46.89  ? 39  ASP   A CB  1 
ATOM   325  C CG  . ASP   A 1 39  ? 15.505 -31.167 -17.761 1.00 51.25  ? 39  ASP   A CG  1 
ATOM   326  O OD1 . ASP   A 1 39  ? 16.547 -31.696 -17.318 1.00 54.64  ? 39  ASP   A OD1 1 
ATOM   327  O OD2 . ASP   A 1 39  ? 14.370 -31.420 -17.306 1.00 63.18  ? 39  ASP   A OD2 1 
ATOM   328  N N   . TYR   A 1 40  ? 18.511 -28.936 -17.131 1.00 50.80  ? 40  TYR   A N   1 
ATOM   329  C CA  . TYR   A 1 40  ? 18.801 -28.379 -15.813 1.00 43.23  ? 40  TYR   A CA  1 
ATOM   330  C C   . TYR   A 1 40  ? 18.683 -26.860 -15.816 1.00 44.48  ? 40  TYR   A C   1 
ATOM   331  O O   . TYR   A 1 40  ? 18.061 -26.272 -14.923 1.00 43.43  ? 40  TYR   A O   1 
ATOM   332  C CB  . TYR   A 1 40  ? 20.194 -28.808 -15.351 1.00 38.97  ? 40  TYR   A CB  1 
ATOM   333  C CG  . TYR   A 1 40  ? 20.546 -28.293 -13.974 1.00 41.31  ? 40  TYR   A CG  1 
ATOM   334  C CD1 . TYR   A 1 40  ? 20.085 -28.938 -12.835 1.00 41.14  ? 40  TYR   A CD1 1 
ATOM   335  C CD2 . TYR   A 1 40  ? 21.331 -27.159 -13.813 1.00 37.89  ? 40  TYR   A CD2 1 
ATOM   336  C CE1 . TYR   A 1 40  ? 20.398 -28.472 -11.574 1.00 43.90  ? 40  TYR   A CE1 1 
ATOM   337  C CE2 . TYR   A 1 40  ? 21.650 -26.685 -12.555 1.00 39.93  ? 40  TYR   A CE2 1 
ATOM   338  C CZ  . TYR   A 1 40  ? 21.180 -27.346 -11.439 1.00 37.66  ? 40  TYR   A CZ  1 
ATOM   339  O OH  . TYR   A 1 40  ? 21.492 -26.884 -10.182 1.00 37.04  ? 40  TYR   A OH  1 
ATOM   340  N N   . TYR   A 1 41  ? 19.274 -26.206 -16.811 1.00 40.39  ? 41  TYR   A N   1 
ATOM   341  C CA  . TYR   A 1 41  ? 19.258 -24.753 -16.887 1.00 44.35  ? 41  TYR   A CA  1 
ATOM   342  C C   . TYR   A 1 41  ? 18.013 -24.210 -17.575 1.00 48.66  ? 41  TYR   A C   1 
ATOM   343  O O   . TYR   A 1 41  ? 17.878 -22.989 -17.711 1.00 56.86  ? 41  TYR   A O   1 
ATOM   344  C CB  . TYR   A 1 41  ? 20.527 -24.255 -17.584 1.00 41.66  ? 41  TYR   A CB  1 
ATOM   345  C CG  . TYR   A 1 41  ? 21.770 -24.605 -16.800 1.00 41.01  ? 41  TYR   A CG  1 
ATOM   346  C CD1 . TYR   A 1 41  ? 22.063 -23.953 -15.609 1.00 42.75  ? 41  TYR   A CD1 1 
ATOM   347  C CD2 . TYR   A 1 41  ? 22.634 -25.602 -17.231 1.00 40.36  ? 41  TYR   A CD2 1 
ATOM   348  C CE1 . TYR   A 1 41  ? 23.188 -24.273 -14.878 1.00 38.94  ? 41  TYR   A CE1 1 
ATOM   349  C CE2 . TYR   A 1 41  ? 23.765 -25.928 -16.505 1.00 39.77  ? 41  TYR   A CE2 1 
ATOM   350  C CZ  . TYR   A 1 41  ? 24.036 -25.260 -15.329 1.00 43.81  ? 41  TYR   A CZ  1 
ATOM   351  O OH  . TYR   A 1 41  ? 25.155 -25.577 -14.597 1.00 41.24  ? 41  TYR   A OH  1 
ATOM   352  N N   . ASP   A 1 42  ? 17.104 -25.085 -18.010 1.00 51.25  ? 42  ASP   A N   1 
ATOM   353  C CA  . ASP   A 1 42  ? 15.754 -24.649 -18.342 1.00 52.79  ? 42  ASP   A CA  1 
ATOM   354  C C   . ASP   A 1 42  ? 14.879 -24.578 -17.099 1.00 45.00  ? 42  ASP   A C   1 
ATOM   355  O O   . ASP   A 1 42  ? 13.905 -23.819 -17.070 1.00 53.46  ? 42  ASP   A O   1 
ATOM   356  C CB  . ASP   A 1 42  ? 15.123 -25.591 -19.368 1.00 44.71  ? 42  ASP   A CB  1 
ATOM   357  C CG  . ASP   A 1 42  ? 15.929 -25.681 -20.649 1.00 56.56  ? 42  ASP   A CG  1 
ATOM   358  O OD1 . ASP   A 1 42  ? 16.566 -24.674 -21.028 1.00 61.57  ? 42  ASP   A OD1 1 
ATOM   359  O OD2 . ASP   A 1 42  ? 15.920 -26.760 -21.281 1.00 56.16  ? 42  ASP   A OD2 1 
ATOM   360  N N   . VAL   A 1 43  ? 15.218 -25.352 -16.073 1.00 45.24  ? 43  VAL   A N   1 
ATOM   361  C CA  . VAL   A 1 43  ? 14.488 -25.358 -14.814 1.00 42.12  ? 43  VAL   A CA  1 
ATOM   362  C C   . VAL   A 1 43  ? 15.146 -24.451 -13.781 1.00 48.70  ? 43  VAL   A C   1 
ATOM   363  O O   . VAL   A 1 43  ? 14.457 -23.745 -13.044 1.00 49.29  ? 43  VAL   A O   1 
ATOM   364  C CB  . VAL   A 1 43  ? 14.362 -26.804 -14.287 1.00 41.52  ? 43  VAL   A CB  1 
ATOM   365  C CG1 . VAL   A 1 43  ? 13.659 -26.829 -12.939 1.00 41.58  ? 43  VAL   A CG1 1 
ATOM   366  C CG2 . VAL   A 1 43  ? 13.627 -27.671 -15.298 1.00 43.30  ? 43  VAL   A CG2 1 
ATOM   367  N N   . ILE   A 1 44  ? 16.473 -24.454 -13.721 1.00 42.23  ? 44  ILE   A N   1 
ATOM   368  C CA  . ILE   A 1 44  ? 17.227 -23.636 -12.779 1.00 41.20  ? 44  ILE   A CA  1 
ATOM   369  C C   . ILE   A 1 44  ? 17.748 -22.420 -13.533 1.00 44.27  ? 44  ILE   A C   1 
ATOM   370  O O   . ILE   A 1 44  ? 18.675 -22.528 -14.344 1.00 43.57  ? 44  ILE   A O   1 
ATOM   371  C CB  . ILE   A 1 44  ? 18.372 -24.425 -12.131 1.00 41.07  ? 44  ILE   A CB  1 
ATOM   372  C CG1 . ILE   A 1 44  ? 17.820 -25.630 -11.369 1.00 39.90  ? 44  ILE   A CG1 1 
ATOM   373  C CG2 . ILE   A 1 44  ? 19.180 -23.529 -11.206 1.00 38.17  ? 44  ILE   A CG2 1 
ATOM   374  C CD1 . ILE   A 1 44  ? 16.787 -25.266 -10.325 1.00 43.69  ? 44  ILE   A CD1 1 
ATOM   375  N N   . LYS   A 1 45  ? 17.153 -21.258 -13.267 1.00 41.59  ? 45  LYS   A N   1 
ATOM   376  C CA  . LYS   A 1 45  ? 17.549 -20.019 -13.920 1.00 52.05  ? 45  LYS   A CA  1 
ATOM   377  C C   . LYS   A 1 45  ? 18.575 -19.225 -13.124 1.00 42.28  ? 45  LYS   A C   1 
ATOM   378  O O   . LYS   A 1 45  ? 19.143 -18.268 -13.658 1.00 45.03  ? 45  LYS   A O   1 
ATOM   379  C CB  . LYS   A 1 45  ? 16.318 -19.143 -14.178 1.00 53.62  ? 45  LYS   A CB  1 
ATOM   380  C CG  . LYS   A 1 45  ? 15.116 -19.896 -14.744 1.00 64.02  ? 45  LYS   A CG  1 
ATOM   381  C CD  . LYS   A 1 45  ? 14.931 -19.654 -16.238 1.00 71.30  ? 45  LYS   A CD  1 
ATOM   382  C CE  . LYS   A 1 45  ? 15.970 -20.387 -17.074 1.00 59.31  ? 45  LYS   A CE  1 
ATOM   383  N N   . ASN   A 1 46  ? 18.820 -19.592 -11.868 1.00 41.13  ? 46  ASN   A N   1 
ATOM   384  C CA  . ASN   A 1 46  ? 19.815 -18.935 -11.022 1.00 41.60  ? 46  ASN   A CA  1 
ATOM   385  C C   . ASN   A 1 46  ? 20.706 -19.999 -10.394 1.00 42.54  ? 46  ASN   A C   1 
ATOM   386  O O   . ASN   A 1 46  ? 20.612 -20.279 -9.193  1.00 39.84  ? 46  ASN   A O   1 
ATOM   387  C CB  . ASN   A 1 46  ? 19.146 -18.076 -9.948  1.00 49.94  ? 46  ASN   A CB  1 
ATOM   388  C CG  . ASN   A 1 46  ? 18.437 -16.866 -10.525 1.00 57.79  ? 46  ASN   A CG  1 
ATOM   389  O OD1 . ASN   A 1 46  ? 17.216 -16.743 -10.429 1.00 69.62  ? 46  ASN   A OD1 1 
ATOM   390  N ND2 . ASN   A 1 46  ? 19.204 -15.960 -11.121 1.00 68.24  ? 46  ASN   A ND2 1 
ATOM   391  N N   . PRO   A 1 47  ? 21.587 -20.613 -11.182 1.00 43.89  ? 47  PRO   A N   1 
ATOM   392  C CA  . PRO   A 1 47  ? 22.436 -21.678 -10.642 1.00 41.78  ? 47  PRO   A CA  1 
ATOM   393  C C   . PRO   A 1 47  ? 23.461 -21.132 -9.663  1.00 40.27  ? 47  PRO   A C   1 
ATOM   394  O O   . PRO   A 1 47  ? 23.888 -19.978 -9.748  1.00 38.98  ? 47  PRO   A O   1 
ATOM   395  C CB  . PRO   A 1 47  ? 23.109 -22.259 -11.890 1.00 42.76  ? 47  PRO   A CB  1 
ATOM   396  C CG  . PRO   A 1 47  ? 23.145 -21.115 -12.846 1.00 41.00  ? 47  PRO   A CG  1 
ATOM   397  C CD  . PRO   A 1 47  ? 21.878 -20.343 -12.602 1.00 45.13  ? 47  PRO   A CD  1 
ATOM   398  N N   . MET   A 1 48  ? 23.856 -21.985 -8.720  1.00 40.47  ? 48  MET   A N   1 
ATOM   399  C CA  . MET   A 1 48  ? 24.783 -21.585 -7.673  1.00 38.81  ? 48  MET   A CA  1 
ATOM   400  C C   . MET   A 1 48  ? 25.482 -22.826 -7.139  1.00 45.29  ? 48  MET   A C   1 
ATOM   401  O O   . MET   A 1 48  ? 24.859 -23.880 -6.993  1.00 40.13  ? 48  MET   A O   1 
ATOM   402  C CB  . MET   A 1 48  ? 24.054 -20.849 -6.542  1.00 39.23  ? 48  MET   A CB  1 
ATOM   403  C CG  . MET   A 1 48  ? 24.973 -20.214 -5.512  1.00 42.31  ? 48  MET   A CG  1 
ATOM   404  S SD  . MET   A 1 48  ? 25.965 -18.874 -6.194  1.00 45.55  ? 48  MET   A SD  1 
ATOM   405  C CE  . MET   A 1 48  ? 24.682 -17.731 -6.692  1.00 41.42  ? 48  MET   A CE  1 
ATOM   406  N N   . SER   A 1 49  ? 26.776 -22.693 -6.855  1.00 48.20  ? 49  SER   A N   1 
ATOM   407  C CA  . SER   A 1 49  ? 27.576 -23.793 -6.339  1.00 38.82  ? 49  SER   A CA  1 
ATOM   408  C C   . SER   A 1 49  ? 28.459 -23.279 -5.212  1.00 39.24  ? 49  SER   A C   1 
ATOM   409  O O   . SER   A 1 49  ? 28.583 -22.072 -4.991  1.00 43.88  ? 49  SER   A O   1 
ATOM   410  C CB  . SER   A 1 49  ? 28.431 -24.432 -7.440  1.00 41.00  ? 49  SER   A CB  1 
ATOM   411  O OG  . SER   A 1 49  ? 29.411 -23.526 -7.918  1.00 38.79  ? 49  SER   A OG  1 
ATOM   412  N N   . PHE   A 1 50  ? 29.072 -24.219 -4.487  1.00 39.20  ? 50  PHE   A N   1 
ATOM   413  C CA  . PHE   A 1 50  ? 29.996 -23.842 -3.421  1.00 45.09  ? 50  PHE   A CA  1 
ATOM   414  C C   . PHE   A 1 50  ? 31.168 -23.038 -3.970  1.00 38.57  ? 50  PHE   A C   1 
ATOM   415  O O   . PHE   A 1 50  ? 31.639 -22.093 -3.326  1.00 39.98  ? 50  PHE   A O   1 
ATOM   416  C CB  . PHE   A 1 50  ? 30.502 -25.088 -2.691  1.00 38.50  ? 50  PHE   A CB  1 
ATOM   417  C CG  . PHE   A 1 50  ? 29.456 -25.777 -1.856  1.00 42.39  ? 50  PHE   A CG  1 
ATOM   418  C CD1 . PHE   A 1 50  ? 28.313 -25.106 -1.450  1.00 45.26  ? 50  PHE   A CD1 1 
ATOM   419  C CD2 . PHE   A 1 50  ? 29.622 -27.098 -1.472  1.00 40.22  ? 50  PHE   A CD2 1 
ATOM   420  C CE1 . PHE   A 1 50  ? 27.354 -25.744 -0.681  1.00 44.51  ? 50  PHE   A CE1 1 
ATOM   421  C CE2 . PHE   A 1 50  ? 28.668 -27.739 -0.704  1.00 41.36  ? 50  PHE   A CE2 1 
ATOM   422  C CZ  . PHE   A 1 50  ? 27.533 -27.061 -0.308  1.00 44.02  ? 50  PHE   A CZ  1 
ATOM   423  N N   . SER   A 1 51  ? 31.651 -23.397 -5.164  1.00 41.27  ? 51  SER   A N   1 
ATOM   424  C CA  . SER   A 1 51  ? 32.761 -22.666 -5.767  1.00 43.88  ? 51  SER   A CA  1 
ATOM   425  C C   . SER   A 1 51  ? 32.359 -21.248 -6.154  1.00 44.52  ? 51  SER   A C   1 
ATOM   426  O O   . SER   A 1 51  ? 33.190 -20.334 -6.099  1.00 45.58  ? 51  SER   A O   1 
ATOM   427  C CB  . SER   A 1 51  ? 33.287 -23.417 -6.989  1.00 39.29  ? 51  SER   A CB  1 
ATOM   428  O OG  . SER   A 1 51  ? 32.272 -23.571 -7.966  1.00 53.09  ? 51  SER   A OG  1 
ATOM   429  N N   . CYS   A 1 52  ? 31.102 -21.047 -6.555  1.00 43.95  ? 52  CYS   A N   1 
ATOM   430  C CA  . CYS   A 1 52  ? 30.623 -19.696 -6.830  1.00 40.26  ? 52  CYS   A CA  1 
ATOM   431  C C   . CYS   A 1 52  ? 30.675 -18.841 -5.571  1.00 38.61  ? 52  CYS   A C   1 
ATOM   432  O O   . CYS   A 1 52  ? 31.110 -17.685 -5.605  1.00 42.40  ? 52  CYS   A O   1 
ATOM   433  C CB  . CYS   A 1 52  ? 29.201 -19.747 -7.388  1.00 39.36  ? 52  CYS   A CB  1 
ATOM   434  S SG  . CYS   A 1 52  ? 29.010 -20.724 -8.897  1.00 53.90  ? 52  CYS   A SG  1 
ATOM   435  N N   . VAL   A 1 53  ? 30.245 -19.407 -4.443  1.00 37.88  ? 53  VAL   A N   1 
ATOM   436  C CA  . VAL   A 1 53  ? 30.261 -18.676 -3.180  1.00 43.01  ? 53  VAL   A CA  1 
ATOM   437  C C   . VAL   A 1 53  ? 31.692 -18.414 -2.726  1.00 43.36  ? 53  VAL   A C   1 
ATOM   438  O O   . VAL   A 1 53  ? 32.003 -17.340 -2.195  1.00 46.76  ? 53  VAL   A O   1 
ATOM   439  C CB  . VAL   A 1 53  ? 29.457 -19.448 -2.119  1.00 41.62  ? 53  VAL   A CB  1 
ATOM   440  C CG1 . VAL   A 1 53  ? 29.541 -18.755 -0.774  1.00 40.38  ? 53  VAL   A CG1 1 
ATOM   441  C CG2 . VAL   A 1 53  ? 28.011 -19.595 -2.563  1.00 37.00  ? 53  VAL   A CG2 1 
ATOM   442  N N   . LYS   A 1 54  ? 32.585 -19.388 -2.922  1.00 45.38  ? 54  LYS   A N   1 
ATOM   443  C CA  . LYS   A 1 54  ? 33.981 -19.198 -2.539  1.00 39.89  ? 54  LYS   A CA  1 
ATOM   444  C C   . LYS   A 1 54  ? 34.629 -18.085 -3.351  1.00 41.78  ? 54  LYS   A C   1 
ATOM   445  O O   . LYS   A 1 54  ? 35.435 -17.309 -2.823  1.00 42.00  ? 54  LYS   A O   1 
ATOM   446  C CB  . LYS   A 1 54  ? 34.758 -20.504 -2.709  1.00 40.10  ? 54  LYS   A CB  1 
ATOM   447  C CG  . LYS   A 1 54  ? 34.378 -21.590 -1.718  1.00 48.83  ? 54  LYS   A CG  1 
ATOM   448  C CD  . LYS   A 1 54  ? 35.109 -22.885 -2.022  1.00 43.80  ? 54  LYS   A CD  1 
ATOM   449  C CE  . LYS   A 1 54  ? 34.779 -23.955 -0.999  1.00 50.24  ? 54  LYS   A CE  1 
ATOM   450  N NZ  . LYS   A 1 54  ? 35.473 -25.232 -1.317  1.00 47.39  ? 54  LYS   A NZ  1 
ATOM   451  N N   . THR   A 1 55  ? 34.293 -17.994 -4.640  1.00 41.08  ? 55  THR   A N   1 
ATOM   452  C CA  . THR   A 1 55  ? 34.843 -16.930 -5.472  1.00 45.41  ? 55  THR   A CA  1 
ATOM   453  C C   . THR   A 1 55  ? 34.356 -15.563 -5.008  1.00 42.92  ? 55  THR   A C   1 
ATOM   454  O O   . THR   A 1 55  ? 35.138 -14.607 -4.946  1.00 44.32  ? 55  THR   A O   1 
ATOM   455  C CB  . THR   A 1 55  ? 34.471 -17.163 -6.937  1.00 46.34  ? 55  THR   A CB  1 
ATOM   456  O OG1 . THR   A 1 55  ? 35.008 -18.417 -7.376  1.00 42.67  ? 55  THR   A OG1 1 
ATOM   457  C CG2 . THR   A 1 55  ? 35.021 -16.044 -7.817  1.00 44.32  ? 55  THR   A CG2 1 
ATOM   458  N N   . LYS   A 1 56  ? 33.069 -15.452 -4.668  1.00 42.03  ? 56  LYS   A N   1 
ATOM   459  C CA  . LYS   A 1 56  ? 32.532 -14.173 -4.215  1.00 47.97  ? 56  LYS   A CA  1 
ATOM   460  C C   . LYS   A 1 56  ? 33.156 -13.751 -2.890  1.00 44.25  ? 56  LYS   A C   1 
ATOM   461  O O   . LYS   A 1 56  ? 33.408 -12.560 -2.668  1.00 47.65  ? 56  LYS   A O   1 
ATOM   462  C CB  . LYS   A 1 56  ? 31.008 -14.258 -4.104  1.00 41.96  ? 56  LYS   A CB  1 
ATOM   463  C CG  . LYS   A 1 56  ? 30.328 -14.633 -5.414  1.00 41.71  ? 56  LYS   A CG  1 
ATOM   464  C CD  . LYS   A 1 56  ? 28.834 -14.877 -5.252  1.00 44.61  ? 56  LYS   A CD  1 
ATOM   465  C CE  . LYS   A 1 56  ? 28.045 -13.587 -5.369  1.00 50.65  ? 56  LYS   A CE  1 
ATOM   466  N NZ  . LYS   A 1 56  ? 26.579 -13.848 -5.415  1.00 51.85  ? 56  LYS   A NZ  1 
ATOM   467  N N   . LEU   A 1 57  ? 33.419 -14.710 -1.999  1.00 42.71  ? 57  LEU   A N   1 
ATOM   468  C CA  . LEU   A 1 57  ? 34.137 -14.393 -0.770  1.00 45.30  ? 57  LEU   A CA  1 
ATOM   469  C C   . LEU   A 1 57  ? 35.588 -14.026 -1.052  1.00 45.30  ? 57  LEU   A C   1 
ATOM   470  O O   . LEU   A 1 57  ? 36.172 -13.207 -0.333  1.00 52.14  ? 57  LEU   A O   1 
ATOM   471  C CB  . LEU   A 1 57  ? 34.065 -15.571 0.202   1.00 41.89  ? 57  LEU   A CB  1 
ATOM   472  C CG  . LEU   A 1 57  ? 32.720 -15.811 0.891   1.00 42.34  ? 57  LEU   A CG  1 
ATOM   473  C CD1 . LEU   A 1 57  ? 32.703 -17.160 1.589   1.00 43.79  ? 57  LEU   A CD1 1 
ATOM   474  C CD2 . LEU   A 1 57  ? 32.439 -14.697 1.883   1.00 49.35  ? 57  LEU   A CD2 1 
ATOM   475  N N   . LYS   A 1 58  ? 36.182 -14.613 -2.092  1.00 44.38  ? 58  LYS   A N   1 
ATOM   476  C CA  . LYS   A 1 58  ? 37.563 -14.292 -2.436  1.00 46.00  ? 58  LYS   A CA  1 
ATOM   477  C C   . LYS   A 1 58  ? 37.670 -12.907 -3.062  1.00 47.54  ? 58  LYS   A C   1 
ATOM   478  O O   . LYS   A 1 58  ? 38.561 -12.126 -2.709  1.00 49.13  ? 58  LYS   A O   1 
ATOM   479  C CB  . LYS   A 1 58  ? 38.122 -15.353 -3.382  1.00 46.00  ? 58  LYS   A CB  1 
ATOM   480  C CG  . LYS   A 1 58  ? 39.523 -15.059 -3.892  1.00 47.99  ? 58  LYS   A CG  1 
ATOM   481  C CD  . LYS   A 1 58  ? 39.936 -16.051 -4.967  1.00 49.63  ? 58  LYS   A CD  1 
ATOM   482  C CE  . LYS   A 1 58  ? 41.347 -15.769 -5.459  1.00 61.53  ? 58  LYS   A CE  1 
ATOM   483  N NZ  . LYS   A 1 58  ? 41.754 -16.704 -6.544  1.00 71.47  ? 58  LYS   A NZ  1 
ATOM   484  N N   . LYS   A 1 59  ? 36.767 -12.583 -3.989  1.00 47.34  ? 59  LYS   A N   1 
ATOM   485  C CA  . LYS   A 1 59  ? 36.823 -11.318 -4.710  1.00 49.12  ? 59  LYS   A CA  1 
ATOM   486  C C   . LYS   A 1 59  ? 36.215 -10.157 -3.934  1.00 49.74  ? 59  LYS   A C   1 
ATOM   487  O O   . LYS   A 1 59  ? 36.445 -9.000  -4.305  1.00 51.69  ? 59  LYS   A O   1 
ATOM   488  C CB  . LYS   A 1 59  ? 36.110 -11.449 -6.059  1.00 49.01  ? 59  LYS   A CB  1 
ATOM   489  C CG  . LYS   A 1 59  ? 36.580 -12.609 -6.918  1.00 48.54  ? 59  LYS   A CG  1 
ATOM   490  C CD  . LYS   A 1 59  ? 37.947 -12.355 -7.527  1.00 50.57  ? 59  LYS   A CD  1 
ATOM   491  C CE  . LYS   A 1 59  ? 38.313 -13.468 -8.494  1.00 50.43  ? 59  LYS   A CE  1 
ATOM   492  N NZ  . LYS   A 1 59  ? 39.577 -13.186 -9.225  1.00 52.79  ? 59  LYS   A NZ  1 
ATOM   493  N N   . GLY   A 1 60  ? 35.444 -10.429 -2.884  1.00 49.68  ? 60  GLY   A N   1 
ATOM   494  C CA  . GLY   A 1 60  ? 34.811 -9.367  -2.128  1.00 49.21  ? 60  GLY   A CA  1 
ATOM   495  C C   . GLY   A 1 60  ? 33.563 -8.832  -2.798  1.00 49.48  ? 60  GLY   A C   1 
ATOM   496  O O   . GLY   A 1 60  ? 33.425 -7.621  -2.994  1.00 51.37  ? 60  GLY   A O   1 
ATOM   497  N N   . GLN   A 1 61  ? 32.647 -9.732  -3.159  1.00 47.85  ? 61  GLN   A N   1 
ATOM   498  C CA  . GLN   A 1 61  ? 31.398 -9.362  -3.811  1.00 52.49  ? 61  GLN   A CA  1 
ATOM   499  C C   . GLN   A 1 61  ? 30.233 -9.213  -2.841  1.00 50.26  ? 61  GLN   A C   1 
ATOM   500  O O   . GLN   A 1 61  ? 29.189 -8.681  -3.232  1.00 53.26  ? 61  GLN   A O   1 
ATOM   501  C CB  . GLN   A 1 61  ? 31.031 -10.397 -4.883  1.00 46.90  ? 61  GLN   A CB  1 
ATOM   502  C CG  . GLN   A 1 61  ? 32.034 -10.509 -6.019  1.00 50.92  ? 61  GLN   A CG  1 
ATOM   503  C CD  . GLN   A 1 61  ? 31.495 -11.310 -7.190  1.00 48.27  ? 61  GLN   A CD  1 
ATOM   504  O OE1 . GLN   A 1 61  ? 30.283 -11.410 -7.382  1.00 59.24  ? 61  GLN   A OE1 1 
ATOM   505  N NE2 . GLN   A 1 61  ? 32.393 -11.888 -7.977  1.00 53.30  ? 61  GLN   A NE2 1 
ATOM   506  N N   . TYR   A 1 62  ? 30.380 -9.665  -1.599  1.00 49.48  ? 62  TYR   A N   1 
ATOM   507  C CA  . TYR   A 1 62  ? 29.318 -9.563  -0.608  1.00 46.80  ? 62  TYR   A CA  1 
ATOM   508  C C   . TYR   A 1 62  ? 29.474 -8.279  0.195   1.00 49.33  ? 62  TYR   A C   1 
ATOM   509  O O   . TYR   A 1 62  ? 30.564 -7.978  0.692   1.00 49.26  ? 62  TYR   A O   1 
ATOM   510  C CB  . TYR   A 1 62  ? 29.334 -10.770 0.330   1.00 46.67  ? 62  TYR   A CB  1 
ATOM   511  C CG  . TYR   A 1 62  ? 28.944 -12.071 -0.330  1.00 50.14  ? 62  TYR   A CG  1 
ATOM   512  C CD1 . TYR   A 1 62  ? 27.933 -12.117 -1.281  1.00 50.51  ? 62  TYR   A CD1 1 
ATOM   513  C CD2 . TYR   A 1 62  ? 29.590 -13.256 -0.004  1.00 48.62  ? 62  TYR   A CD2 1 
ATOM   514  C CE1 . TYR   A 1 62  ? 27.574 -13.308 -1.885  1.00 54.72  ? 62  TYR   A CE1 1 
ATOM   515  C CE2 . TYR   A 1 62  ? 29.239 -14.451 -0.603  1.00 53.66  ? 62  TYR   A CE2 1 
ATOM   516  C CZ  . TYR   A 1 62  ? 28.231 -14.472 -1.543  1.00 54.51  ? 62  TYR   A CZ  1 
ATOM   517  O OH  . TYR   A 1 62  ? 27.878 -15.661 -2.142  1.00 49.40  ? 62  TYR   A OH  1 
ATOM   518  N N   . GLY   A 1 63  ? 28.383 -7.528  0.322   1.00 49.95  ? 63  GLY   A N   1 
ATOM   519  C CA  . GLY   A 1 63  ? 28.392 -6.326  1.129   1.00 52.02  ? 63  GLY   A CA  1 
ATOM   520  C C   . GLY   A 1 63  ? 27.763 -6.542  2.489   1.00 51.82  ? 63  GLY   A C   1 
ATOM   521  O O   . GLY   A 1 63  ? 28.093 -5.849  3.456   1.00 53.46  ? 63  GLY   A O   1 
ATOM   522  N N   . LEU   A 1 64  ? 26.855 -7.509  2.574   1.00 50.40  ? 64  LEU   A N   1 
ATOM   523  C CA  . LEU   A 1 64  ? 26.132 -7.814  3.796   1.00 50.39  ? 64  LEU   A CA  1 
ATOM   524  C C   . LEU   A 1 64  ? 26.250 -9.298  4.110   1.00 48.16  ? 64  LEU   A C   1 
ATOM   525  O O   . LEU   A 1 64  ? 26.313 -10.126 3.196   1.00 48.34  ? 64  LEU   A O   1 
ATOM   526  C CB  . LEU   A 1 64  ? 24.651 -7.431  3.668   1.00 54.58  ? 64  LEU   A CB  1 
ATOM   527  C CG  . LEU   A 1 64  ? 24.362 -5.954  3.386   1.00 58.33  ? 64  LEU   A CG  1 
ATOM   528  C CD1 . LEU   A 1 64  ? 22.912 -5.753  2.970   1.00 58.59  ? 64  LEU   A CD1 1 
ATOM   529  C CD2 . LEU   A 1 64  ? 24.696 -5.102  4.602   1.00 58.97  ? 64  LEU   A CD2 1 
ATOM   530  N N   . PRO   A 1 65  ? 26.287 -9.662  5.394   1.00 48.19  ? 65  PRO   A N   1 
ATOM   531  C CA  . PRO   A 1 65  ? 26.380 -11.089 5.745   1.00 46.36  ? 65  PRO   A CA  1 
ATOM   532  C C   . PRO   A 1 65  ? 25.184 -11.905 5.287   1.00 45.58  ? 65  PRO   A C   1 
ATOM   533  O O   . PRO   A 1 65  ? 25.307 -13.127 5.148   1.00 44.10  ? 65  PRO   A O   1 
ATOM   534  C CB  . PRO   A 1 65  ? 26.498 -11.069 7.277   1.00 47.15  ? 65  PRO   A CB  1 
ATOM   535  C CG  . PRO   A 1 65  ? 25.917 -9.753  7.686   1.00 49.27  ? 65  PRO   A CG  1 
ATOM   536  C CD  . PRO   A 1 65  ? 26.268 -8.798  6.586   1.00 49.88  ? 65  PRO   A CD  1 
ATOM   537  N N   . THR   A 1 66  ? 24.033 -11.272 5.047   1.00 46.76  ? 66  THR   A N   1 
ATOM   538  C CA  . THR   A 1 66  ? 22.866 -11.996 4.559   1.00 46.27  ? 66  THR   A CA  1 
ATOM   539  C C   . THR   A 1 66  ? 23.027 -12.430 3.109   1.00 45.05  ? 66  THR   A C   1 
ATOM   540  O O   . THR   A 1 66  ? 22.390 -13.404 2.691   1.00 48.36  ? 66  THR   A O   1 
ATOM   541  C CB  . THR   A 1 66  ? 21.610 -11.135 4.700   1.00 49.58  ? 66  THR   A CB  1 
ATOM   542  O OG1 . THR   A 1 66  ? 21.769 -9.927  3.946   1.00 61.18  ? 66  THR   A OG1 1 
ATOM   543  C CG2 . THR   A 1 66  ? 21.363 -10.789 6.157   1.00 52.10  ? 66  THR   A CG2 1 
ATOM   544  N N   . GLU   A 1 67  ? 23.856 -11.728 2.330   1.00 45.93  ? 67  GLU   A N   1 
ATOM   545  C CA  . GLU   A 1 67  ? 24.064 -12.114 0.938   1.00 49.23  ? 67  GLU   A CA  1 
ATOM   546  C C   . GLU   A 1 67  ? 24.746 -13.472 0.832   1.00 47.78  ? 67  GLU   A C   1 
ATOM   547  O O   . GLU   A 1 67  ? 24.512 -14.209 -0.132  1.00 54.25  ? 67  GLU   A O   1 
ATOM   548  C CB  . GLU   A 1 67  ? 24.881 -11.043 0.216   1.00 45.35  ? 67  GLU   A CB  1 
ATOM   549  C CG  . GLU   A 1 67  ? 24.161 -9.713  0.062   1.00 47.56  ? 67  GLU   A CG  1 
ATOM   550  C CD  . GLU   A 1 67  ? 25.103 -8.576  -0.287  1.00 58.50  ? 67  GLU   A CD  1 
ATOM   551  O OE1 . GLU   A 1 67  ? 26.270 -8.614  0.153   1.00 56.73  ? 67  GLU   A OE1 1 
ATOM   552  O OE2 . GLU   A 1 67  ? 24.678 -7.645  -1.003  1.00 69.63  ? 67  GLU   A OE2 1 
ATOM   553  N N   . PHE   A 1 68  ? 25.585 -13.819 1.811   1.00 44.72  ? 68  PHE   A N   1 
ATOM   554  C CA  . PHE   A 1 68  ? 26.199 -15.141 1.832   1.00 43.08  ? 68  PHE   A CA  1 
ATOM   555  C C   . PHE   A 1 68  ? 25.156 -16.220 2.089   1.00 46.28  ? 68  PHE   A C   1 
ATOM   556  O O   . PHE   A 1 68  ? 25.143 -17.258 1.418   1.00 45.64  ? 68  PHE   A O   1 
ATOM   557  C CB  . PHE   A 1 68  ? 27.303 -15.183 2.890   1.00 47.49  ? 68  PHE   A CB  1 
ATOM   558  C CG  . PHE   A 1 68  ? 27.783 -16.571 3.223   1.00 39.85  ? 68  PHE   A CG  1 
ATOM   559  C CD1 . PHE   A 1 68  ? 28.581 -17.275 2.338   1.00 42.05  ? 68  PHE   A CD1 1 
ATOM   560  C CD2 . PHE   A 1 68  ? 27.450 -17.162 4.432   1.00 42.60  ? 68  PHE   A CD2 1 
ATOM   561  C CE1 . PHE   A 1 68  ? 29.028 -18.548 2.645   1.00 41.31  ? 68  PHE   A CE1 1 
ATOM   562  C CE2 . PHE   A 1 68  ? 27.893 -18.434 4.745   1.00 39.47  ? 68  PHE   A CE2 1 
ATOM   563  C CZ  . PHE   A 1 68  ? 28.684 -19.128 3.850   1.00 38.80  ? 68  PHE   A CZ  1 
ATOM   564  N N   . ILE   A 1 69  ? 24.260 -15.982 3.050   1.00 40.90  ? 69  ILE   A N   1 
ATOM   565  C CA  . ILE   A 1 69  ? 23.243 -16.972 3.393   1.00 45.46  ? 69  ILE   A CA  1 
ATOM   566  C C   . ILE   A 1 69  ? 22.302 -17.204 2.218   1.00 45.02  ? 69  ILE   A C   1 
ATOM   567  O O   . ILE   A 1 69  ? 21.864 -18.333 1.967   1.00 48.12  ? 69  ILE   A O   1 
ATOM   568  C CB  . ILE   A 1 69  ? 22.479 -16.525 4.654   1.00 42.06  ? 69  ILE   A CB  1 
ATOM   569  C CG1 . ILE   A 1 69  ? 23.419 -16.468 5.861   1.00 46.30  ? 69  ILE   A CG1 1 
ATOM   570  C CG2 . ILE   A 1 69  ? 21.307 -17.452 4.933   1.00 42.23  ? 69  ILE   A CG2 1 
ATOM   571  C CD1 . ILE   A 1 69  ? 22.734 -16.039 7.140   1.00 44.97  ? 69  ILE   A CD1 1 
ATOM   572  N N   . LYS   A 1 70  ? 21.984 -16.143 1.474   1.00 44.28  ? 70  LYS   A N   1 
ATOM   573  C CA  . LYS   A 1 70  ? 21.037 -16.271 0.371   1.00 45.98  ? 70  LYS   A CA  1 
ATOM   574  C C   . LYS   A 1 70  ? 21.616 -17.102 -0.767  1.00 43.93  ? 70  LYS   A C   1 
ATOM   575  O O   . LYS   A 1 70  ? 20.902 -17.900 -1.384  1.00 44.10  ? 70  LYS   A O   1 
ATOM   576  C CB  . LYS   A 1 70  ? 20.626 -14.887 -0.128  1.00 42.81  ? 70  LYS   A CB  1 
ATOM   577  C CG  . LYS   A 1 70  ? 19.280 -14.411 0.399   1.00 58.28  ? 70  LYS   A CG  1 
ATOM   578  C CD  . LYS   A 1 70  ? 19.201 -14.496 1.917   1.00 53.70  ? 70  LYS   A CD  1 
ATOM   579  N N   . ASP   A 1 71  ? 22.906 -16.930 -1.062  1.00 43.82  ? 71  ASP   A N   1 
ATOM   580  C CA  . ASP   A 1 71  ? 23.520 -17.707 -2.134  1.00 45.65  ? 71  ASP   A CA  1 
ATOM   581  C C   . ASP   A 1 71  ? 23.615 -19.181 -1.765  1.00 43.46  ? 71  ASP   A C   1 
ATOM   582  O O   . ASP   A 1 71  ? 23.416 -20.054 -2.619  1.00 43.19  ? 71  ASP   A O   1 
ATOM   583  C CB  . ASP   A 1 71  ? 24.900 -17.144 -2.468  1.00 45.26  ? 71  ASP   A CB  1 
ATOM   584  C CG  . ASP   A 1 71  ? 24.826 -15.886 -3.308  1.00 49.10  ? 71  ASP   A CG  1 
ATOM   585  O OD1 . ASP   A 1 71  ? 23.705 -15.486 -3.688  1.00 49.14  ? 71  ASP   A OD1 1 
ATOM   586  O OD2 . ASP   A 1 71  ? 25.890 -15.298 -3.592  1.00 42.48  ? 71  ASP   A OD2 1 
ATOM   587  N N   . VAL   A 1 72  ? 23.915 -19.480 -0.500  1.00 39.39  ? 72  VAL   A N   1 
ATOM   588  C CA  . VAL   A 1 72  ? 23.986 -20.871 -0.063  1.00 38.10  ? 72  VAL   A CA  1 
ATOM   589  C C   . VAL   A 1 72  ? 22.600 -21.502 -0.084  1.00 44.36  ? 72  VAL   A C   1 
ATOM   590  O O   . VAL   A 1 72  ? 22.421 -22.634 -0.550  1.00 42.26  ? 72  VAL   A O   1 
ATOM   591  C CB  . VAL   A 1 72  ? 24.629 -20.963 1.333   1.00 47.22  ? 72  VAL   A CB  1 
ATOM   592  C CG1 . VAL   A 1 72  ? 24.648 -22.409 1.816   1.00 37.11  ? 72  VAL   A CG1 1 
ATOM   593  C CG2 . VAL   A 1 72  ? 26.034 -20.383 1.308   1.00 40.16  ? 72  VAL   A CG2 1 
ATOM   594  N N   . GLN   A 1 73  ? 21.597 -20.777 0.419   1.00 42.88  ? 73  GLN   A N   1 
ATOM   595  C CA  . GLN   A 1 73  ? 20.231 -21.288 0.390   1.00 40.96  ? 73  GLN   A CA  1 
ATOM   596  C C   . GLN   A 1 73  ? 19.735 -21.468 -1.038  1.00 40.72  ? 73  GLN   A C   1 
ATOM   597  O O   . GLN   A 1 73  ? 18.888 -22.331 -1.295  1.00 40.16  ? 73  GLN   A O   1 
ATOM   598  C CB  . GLN   A 1 73  ? 19.303 -20.351 1.165   1.00 39.89  ? 73  GLN   A CB  1 
ATOM   599  C CG  . GLN   A 1 73  ? 17.891 -20.885 1.345   1.00 42.73  ? 73  GLN   A CG  1 
ATOM   600  C CD  . GLN   A 1 73  ? 17.862 -22.205 2.094   1.00 54.51  ? 73  GLN   A CD  1 
ATOM   601  O OE1 . GLN   A 1 73  ? 18.681 -22.448 2.981   1.00 51.85  ? 73  GLN   A OE1 1 
ATOM   602  N NE2 . GLN   A 1 73  ? 16.916 -23.067 1.739   1.00 43.39  ? 73  GLN   A NE2 1 
ATOM   603  N N   . LEU   A 1 74  ? 20.252 -20.672 -1.976  1.00 40.66  ? 74  LEU   A N   1 
ATOM   604  C CA  . LEU   A 1 74  ? 19.877 -20.835 -3.377  1.00 38.56  ? 74  LEU   A CA  1 
ATOM   605  C C   . LEU   A 1 74  ? 20.323 -22.189 -3.913  1.00 43.02  ? 74  LEU   A C   1 
ATOM   606  O O   . LEU   A 1 74  ? 19.633 -22.793 -4.743  1.00 40.08  ? 74  LEU   A O   1 
ATOM   607  C CB  . LEU   A 1 74  ? 20.472 -19.699 -4.210  1.00 44.44  ? 74  LEU   A CB  1 
ATOM   608  C CG  . LEU   A 1 74  ? 20.322 -19.786 -5.729  1.00 40.30  ? 74  LEU   A CG  1 
ATOM   609  C CD1 . LEU   A 1 74  ? 18.855 -19.860 -6.125  1.00 42.77  ? 74  LEU   A CD1 1 
ATOM   610  C CD2 . LEU   A 1 74  ? 21.001 -18.601 -6.394  1.00 38.97  ? 74  LEU   A CD2 1 
ATOM   611  N N   . ILE   A 1 75  ? 21.474 -22.683 -3.449  1.00 38.93  ? 75  ILE   A N   1 
ATOM   612  C CA  . ILE   A 1 75  ? 21.943 -24.004 -3.858  1.00 40.41  ? 75  ILE   A CA  1 
ATOM   613  C C   . ILE   A 1 75  ? 20.949 -25.074 -3.425  1.00 41.69  ? 75  ILE   A C   1 
ATOM   614  O O   . ILE   A 1 75  ? 20.564 -25.948 -4.210  1.00 36.60  ? 75  ILE   A O   1 
ATOM   615  C CB  . ILE   A 1 75  ? 23.343 -24.278 -3.280  1.00 39.54  ? 75  ILE   A CB  1 
ATOM   616  C CG1 . ILE   A 1 75  ? 24.337 -23.212 -3.741  1.00 46.20  ? 75  ILE   A CG1 1 
ATOM   617  C CG2 . ILE   A 1 75  ? 23.822 -25.663 -3.680  1.00 35.49  ? 75  ILE   A CG2 1 
ATOM   618  C CD1 . ILE   A 1 75  ? 25.696 -23.331 -3.096  1.00 37.43  ? 75  ILE   A CD1 1 
ATOM   619  N N   . PHE   A 1 76  ? 20.517 -25.014 -2.164  1.00 36.71  ? 76  PHE   A N   1 
ATOM   620  C CA  . PHE   A 1 76  ? 19.584 -26.009 -1.649  1.00 38.48  ? 76  PHE   A CA  1 
ATOM   621  C C   . PHE   A 1 76  ? 18.183 -25.814 -2.211  1.00 40.79  ? 76  PHE   A C   1 
ATOM   622  O O   . PHE   A 1 76  ? 17.428 -26.784 -2.337  1.00 48.10  ? 76  PHE   A O   1 
ATOM   623  C CB  . PHE   A 1 76  ? 19.568 -25.955 -0.123  1.00 39.51  ? 76  PHE   A CB  1 
ATOM   624  C CG  . PHE   A 1 76  ? 20.930 -26.088 0.497   1.00 50.72  ? 76  PHE   A CG  1 
ATOM   625  C CD1 . PHE   A 1 76  ? 21.820 -27.048 0.043   1.00 49.84  ? 76  PHE   A CD1 1 
ATOM   626  C CD2 . PHE   A 1 76  ? 21.328 -25.244 1.521   1.00 46.74  ? 76  PHE   A CD2 1 
ATOM   627  C CE1 . PHE   A 1 76  ? 23.076 -27.172 0.606   1.00 52.17  ? 76  PHE   A CE1 1 
ATOM   628  C CE2 . PHE   A 1 76  ? 22.584 -25.363 2.087   1.00 45.73  ? 76  PHE   A CE2 1 
ATOM   629  C CZ  . PHE   A 1 76  ? 23.458 -26.328 1.629   1.00 51.36  ? 76  PHE   A CZ  1 
ATOM   630  N N   . ASP   A 1 77  ? 17.818 -24.577 -2.554  1.00 42.27  ? 77  ASP   A N   1 
ATOM   631  C CA  . ASP   A 1 77  ? 16.522 -24.341 -3.181  1.00 40.63  ? 77  ASP   A CA  1 
ATOM   632  C C   . ASP   A 1 77  ? 16.505 -24.852 -4.614  1.00 38.74  ? 77  ASP   A C   1 
ATOM   633  O O   . ASP   A 1 77  ? 15.513 -25.443 -5.056  1.00 42.74  ? 77  ASP   A O   1 
ATOM   634  C CB  . ASP   A 1 77  ? 16.177 -22.853 -3.129  1.00 49.75  ? 77  ASP   A CB  1 
ATOM   635  C CG  . ASP   A 1 77  ? 15.767 -22.401 -1.740  1.00 56.72  ? 77  ASP   A CG  1 
ATOM   636  O OD1 . ASP   A 1 77  ? 15.557 -23.271 -0.868  1.00 46.85  ? 77  ASP   A OD1 1 
ATOM   637  O OD2 . ASP   A 1 77  ? 15.653 -21.177 -1.518  1.00 56.81  ? 77  ASP   A OD2 1 
ATOM   638  N N   . ASN   A 1 78  ? 17.593 -24.632 -5.358  1.00 42.17  ? 78  ASN   A N   1 
ATOM   639  C CA  . ASN   A 1 78  ? 17.712 -25.236 -6.680  1.00 45.16  ? 78  ASN   A CA  1 
ATOM   640  C C   . ASN   A 1 78  ? 17.722 -26.757 -6.591  1.00 46.48  ? 78  ASN   A C   1 
ATOM   641  O O   . ASN   A 1 78  ? 17.222 -27.437 -7.495  1.00 41.59  ? 78  ASN   A O   1 
ATOM   642  C CB  . ASN   A 1 78  ? 18.981 -24.740 -7.380  1.00 38.01  ? 78  ASN   A CB  1 
ATOM   643  C CG  . ASN   A 1 78  ? 18.920 -23.271 -7.736  1.00 37.51  ? 78  ASN   A CG  1 
ATOM   644  O OD1 . ASN   A 1 78  ? 17.843 -22.706 -7.909  1.00 41.48  ? 78  ASN   A OD1 1 
ATOM   645  N ND2 . ASN   A 1 78  ? 20.085 -22.644 -7.851  1.00 41.36  ? 78  ASN   A ND2 1 
ATOM   646  N N   . CYS   A 1 79  ? 18.284 -27.307 -5.512  1.00 42.81  ? 79  CYS   A N   1 
ATOM   647  C CA  . CYS   A 1 79  ? 18.348 -28.756 -5.358  1.00 37.45  ? 79  CYS   A CA  1 
ATOM   648  C C   . CYS   A 1 79  ? 16.957 -29.350 -5.168  1.00 45.92  ? 79  CYS   A C   1 
ATOM   649  O O   . CYS   A 1 79  ? 16.557 -30.267 -5.894  1.00 38.89  ? 79  CYS   A O   1 
ATOM   650  C CB  . CYS   A 1 79  ? 19.257 -29.112 -4.180  1.00 37.72  ? 79  CYS   A CB  1 
ATOM   651  S SG  . CYS   A 1 79  ? 19.397 -30.878 -3.853  1.00 42.66  ? 79  CYS   A SG  1 
ATOM   652  N N   . SER   A 1 80  ? 16.202 -28.833 -4.196  1.00 39.55  ? 80  SER   A N   1 
ATOM   653  C CA  . SER   A 1 80  ? 14.861 -29.347 -3.942  1.00 47.25  ? 80  SER   A CA  1 
ATOM   654  C C   . SER   A 1 80  ? 13.906 -29.068 -5.094  1.00 43.47  ? 80  SER   A C   1 
ATOM   655  O O   . SER   A 1 80  ? 12.874 -29.738 -5.202  1.00 46.91  ? 80  SER   A O   1 
ATOM   656  C CB  . SER   A 1 80  ? 14.305 -28.748 -2.651  1.00 47.21  ? 80  SER   A CB  1 
ATOM   657  O OG  . SER   A 1 80  ? 14.185 -27.341 -2.755  1.00 56.76  ? 80  SER   A OG  1 
ATOM   658  N N   . LEU   A 1 81  ? 14.223 -28.098 -5.952  1.00 42.90  ? 81  LEU   A N   1 
ATOM   659  C CA  . LEU   A 1 81  ? 13.354 -27.796 -7.083  1.00 44.06  ? 81  LEU   A CA  1 
ATOM   660  C C   . LEU   A 1 81  ? 13.532 -28.808 -8.208  1.00 44.46  ? 81  LEU   A C   1 
ATOM   661  O O   . LEU   A 1 81  ? 12.555 -29.398 -8.683  1.00 45.18  ? 81  LEU   A O   1 
ATOM   662  C CB  . LEU   A 1 81  ? 13.627 -26.379 -7.591  1.00 40.82  ? 81  LEU   A CB  1 
ATOM   663  C CG  . LEU   A 1 81  ? 12.946 -25.982 -8.902  1.00 41.63  ? 81  LEU   A CG  1 
ATOM   664  C CD1 . LEU   A 1 81  ? 11.434 -26.143 -8.798  1.00 43.30  ? 81  LEU   A CD1 1 
ATOM   665  C CD2 . LEU   A 1 81  ? 13.314 -24.553 -9.279  1.00 41.81  ? 81  LEU   A CD2 1 
ATOM   666  N N   . TYR   A 1 82  ? 14.773 -29.025 -8.649  1.00 40.46  ? 82  TYR   A N   1 
ATOM   667  C CA  . TYR   A 1 82  ? 15.000 -29.889 -9.801  1.00 44.96  ? 82  TYR   A CA  1 
ATOM   668  C C   . TYR   A 1 82  ? 14.903 -31.367 -9.447  1.00 40.20  ? 82  TYR   A C   1 
ATOM   669  O O   . TYR   A 1 82  ? 14.525 -32.176 -10.302 1.00 46.85  ? 82  TYR   A O   1 
ATOM   670  C CB  . TYR   A 1 82  ? 16.363 -29.591 -10.430 1.00 42.12  ? 82  TYR   A CB  1 
ATOM   671  C CG  . TYR   A 1 82  ? 16.627 -30.379 -11.693 1.00 44.58  ? 82  TYR   A CG  1 
ATOM   672  C CD1 . TYR   A 1 82  ? 16.170 -29.927 -12.925 1.00 45.52  ? 82  TYR   A CD1 1 
ATOM   673  C CD2 . TYR   A 1 82  ? 17.326 -31.580 -11.654 1.00 44.99  ? 82  TYR   A CD2 1 
ATOM   674  C CE1 . TYR   A 1 82  ? 16.405 -30.646 -14.081 1.00 42.42  ? 82  TYR   A CE1 1 
ATOM   675  C CE2 . TYR   A 1 82  ? 17.563 -32.306 -12.805 1.00 39.56  ? 82  TYR   A CE2 1 
ATOM   676  C CZ  . TYR   A 1 82  ? 17.101 -31.834 -14.014 1.00 47.17  ? 82  TYR   A CZ  1 
ATOM   677  O OH  . TYR   A 1 82  ? 17.336 -32.555 -15.161 1.00 54.53  ? 82  TYR   A OH  1 
ATOM   678  N N   . ASN   A 1 83  ? 15.224 -31.740 -8.213  1.00 40.13  ? 83  ASN   A N   1 
ATOM   679  C CA  . ASN   A 1 83  ? 15.322 -33.141 -7.828  1.00 40.79  ? 83  ASN   A CA  1 
ATOM   680  C C   . ASN   A 1 83  ? 14.083 -33.591 -7.062  1.00 42.34  ? 83  ASN   A C   1 
ATOM   681  O O   . ASN   A 1 83  ? 13.568 -32.866 -6.207  1.00 49.42  ? 83  ASN   A O   1 
ATOM   682  C CB  . ASN   A 1 83  ? 16.578 -33.382 -6.988  1.00 40.24  ? 83  ASN   A CB  1 
ATOM   683  C CG  . ASN   A 1 83  ? 17.853 -33.089 -7.757  1.00 39.56  ? 83  ASN   A CG  1 
ATOM   684  O OD1 . ASN   A 1 83  ? 18.321 -33.913 -8.539  1.00 44.41  ? 83  ASN   A OD1 1 
ATOM   685  N ND2 . ASN   A 1 83  ? 18.421 -31.908 -7.537  1.00 39.61  ? 83  ASN   A ND2 1 
ATOM   686  N N   . THR   A 1 84  ? 13.615 -34.799 -7.380  1.00 47.74  ? 84  THR   A N   1 
ATOM   687  C CA  . THR   A 1 84  ? 12.448 -35.362 -6.714  1.00 44.92  ? 84  THR   A CA  1 
ATOM   688  C C   . THR   A 1 84  ? 12.732 -35.552 -5.228  1.00 45.31  ? 84  THR   A C   1 
ATOM   689  O O   . THR   A 1 84  ? 13.859 -35.861 -4.832  1.00 52.45  ? 84  THR   A O   1 
ATOM   690  C CB  . THR   A 1 84  ? 12.065 -36.694 -7.365  1.00 46.22  ? 84  THR   A CB  1 
ATOM   691  O OG1 . THR   A 1 84  ? 11.867 -36.495 -8.769  1.00 45.98  ? 84  THR   A OG1 1 
ATOM   692  C CG2 . THR   A 1 84  ? 10.781 -37.247 -6.769  1.00 48.23  ? 84  THR   A CG2 1 
ATOM   693  N N   . SER   A 1 85  ? 11.690 -35.371 -4.408  1.00 49.11  ? 85  SER   A N   1 
ATOM   694  C CA  . SER   A 1 85  ? 11.850 -35.288 -2.958  1.00 51.06  ? 85  SER   A CA  1 
ATOM   695  C C   . SER   A 1 85  ? 12.629 -36.464 -2.378  1.00 57.45  ? 85  SER   A C   1 
ATOM   696  O O   . SER   A 1 85  ? 13.348 -36.303 -1.387  1.00 71.70  ? 85  SER   A O   1 
ATOM   697  C CB  . SER   A 1 85  ? 10.475 -35.191 -2.291  1.00 51.60  ? 85  SER   A CB  1 
ATOM   698  O OG  . SER   A 1 85  ? 10.587 -35.208 -0.880  1.00 68.92  ? 85  SER   A OG  1 
ATOM   699  N N   . GLY   A 1 86  ? 12.515 -37.643 -2.977  1.00 50.28  ? 86  GLY   A N   1 
ATOM   700  C CA  . GLY   A 1 86  ? 13.162 -38.819 -2.438  1.00 67.21  ? 86  GLY   A CA  1 
ATOM   701  C C   . GLY   A 1 86  ? 14.482 -39.211 -3.065  1.00 55.96  ? 86  GLY   A C   1 
ATOM   702  O O   . GLY   A 1 86  ? 15.100 -40.180 -2.611  1.00 49.92  ? 86  GLY   A O   1 
ATOM   703  N N   . SER   A 1 87  ? 14.941 -38.489 -4.085  1.00 46.98  ? 87  SER   A N   1 
ATOM   704  C CA  . SER   A 1 87  ? 16.144 -38.876 -4.809  1.00 48.38  ? 87  SER   A CA  1 
ATOM   705  C C   . SER   A 1 87  ? 17.389 -38.718 -3.936  1.00 47.35  ? 87  SER   A C   1 
ATOM   706  O O   . SER   A 1 87  ? 17.379 -38.043 -2.903  1.00 49.86  ? 87  SER   A O   1 
ATOM   707  C CB  . SER   A 1 87  ? 16.297 -38.039 -6.079  1.00 44.80  ? 87  SER   A CB  1 
ATOM   708  O OG  . SER   A 1 87  ? 16.534 -36.680 -5.763  1.00 44.14  ? 87  SER   A OG  1 
ATOM   709  N N   . LEU   A 1 88  ? 18.482 -39.351 -4.381  1.00 46.13  ? 88  LEU   A N   1 
ATOM   710  C CA  . LEU   A 1 88  ? 19.749 -39.262 -3.656  1.00 47.52  ? 88  LEU   A CA  1 
ATOM   711  C C   . LEU   A 1 88  ? 20.231 -37.821 -3.551  1.00 44.02  ? 88  LEU   A C   1 
ATOM   712  O O   . LEU   A 1 88  ? 20.705 -37.395 -2.492  1.00 44.94  ? 88  LEU   A O   1 
ATOM   713  C CB  . LEU   A 1 88  ? 20.814 -40.125 -4.339  1.00 46.76  ? 88  LEU   A CB  1 
ATOM   714  C CG  . LEU   A 1 88  ? 20.646 -41.646 -4.319  1.00 49.16  ? 88  LEU   A CG  1 
ATOM   715  C CD1 . LEU   A 1 88  ? 21.893 -42.327 -4.871  1.00 50.07  ? 88  LEU   A CD1 1 
ATOM   716  C CD2 . LEU   A 1 88  ? 20.338 -42.136 -2.913  1.00 50.73  ? 88  LEU   A CD2 1 
ATOM   717  N N   . VAL   A 1 89  ? 20.122 -37.058 -4.641  1.00 42.70  ? 89  VAL   A N   1 
ATOM   718  C CA  . VAL   A 1 89  ? 20.585 -35.671 -4.632  1.00 41.11  ? 89  VAL   A CA  1 
ATOM   719  C C   . VAL   A 1 89  ? 19.752 -34.840 -3.665  1.00 41.70  ? 89  VAL   A C   1 
ATOM   720  O O   . VAL   A 1 89  ? 20.285 -34.045 -2.882  1.00 40.27  ? 89  VAL   A O   1 
ATOM   721  C CB  . VAL   A 1 89  ? 20.551 -35.082 -6.053  1.00 41.64  ? 89  VAL   A CB  1 
ATOM   722  C CG1 . VAL   A 1 89  ? 20.894 -33.604 -6.019  1.00 38.87  ? 89  VAL   A CG1 1 
ATOM   723  C CG2 . VAL   A 1 89  ? 21.514 -35.827 -6.957  1.00 40.64  ? 89  VAL   A CG2 1 
ATOM   724  N N   . ALA   A 1 90  ? 18.429 -35.014 -3.702  1.00 41.48  ? 90  ALA   A N   1 
ATOM   725  C CA  . ALA   A 1 90  ? 17.561 -34.234 -2.827  1.00 41.60  ? 90  ALA   A CA  1 
ATOM   726  C C   . ALA   A 1 90  ? 17.795 -34.581 -1.363  1.00 42.52  ? 90  ALA   A C   1 
ATOM   727  O O   . ALA   A 1 90  ? 17.710 -33.710 -0.489  1.00 44.09  ? 90  ALA   A O   1 
ATOM   728  C CB  . ALA   A 1 90  ? 16.097 -34.456 -3.203  1.00 47.46  ? 90  ALA   A CB  1 
ATOM   729  N N   . ILE   A 1 91  ? 18.088 -35.850 -1.074  1.00 43.78  ? 91  ILE   A N   1 
ATOM   730  C CA  . ILE   A 1 91  ? 18.359 -36.259 0.302   1.00 45.00  ? 91  ILE   A CA  1 
ATOM   731  C C   . ILE   A 1 91  ? 19.602 -35.551 0.829   1.00 50.87  ? 91  ILE   A C   1 
ATOM   732  O O   . ILE   A 1 91  ? 19.595 -34.973 1.922   1.00 47.97  ? 91  ILE   A O   1 
ATOM   733  C CB  . ILE   A 1 91  ? 18.500 -37.790 0.387   1.00 46.86  ? 91  ILE   A CB  1 
ATOM   734  C CG1 . ILE   A 1 91  ? 17.139 -38.467 0.207   1.00 48.29  ? 91  ILE   A CG1 1 
ATOM   735  C CG2 . ILE   A 1 91  ? 19.133 -38.191 1.705   1.00 48.17  ? 91  ILE   A CG2 1 
ATOM   736  C CD1 . ILE   A 1 91  ? 17.222 -39.970 0.033   1.00 50.23  ? 91  ILE   A CD1 1 
ATOM   737  N N   . THR   A 1 92  ? 20.689 -35.583 0.053   1.00 45.12  ? 92  THR   A N   1 
ATOM   738  C CA  . THR   A 1 92  ? 21.924 -34.931 0.477   1.00 45.86  ? 92  THR   A CA  1 
ATOM   739  C C   . THR   A 1 92  ? 21.759 -33.420 0.559   1.00 42.57  ? 92  THR   A C   1 
ATOM   740  O O   . THR   A 1 92  ? 22.388 -32.774 1.403   1.00 41.18  ? 92  THR   A O   1 
ATOM   741  C CB  . THR   A 1 92  ? 23.063 -35.278 -0.480  1.00 46.66  ? 92  THR   A CB  1 
ATOM   742  O OG1 . THR   A 1 92  ? 22.739 -34.804 -1.793  1.00 60.04  ? 92  THR   A OG1 1 
ATOM   743  C CG2 . THR   A 1 92  ? 23.286 -36.784 -0.530  1.00 43.95  ? 92  THR   A CG2 1 
ATOM   744  N N   . GLY   A 1 93  ? 20.930 -32.843 -0.312  1.00 46.19  ? 93  GLY   A N   1 
ATOM   745  C CA  . GLY   A 1 93  ? 20.662 -31.417 -0.224  1.00 41.47  ? 93  GLY   A CA  1 
ATOM   746  C C   . GLY   A 1 93  ? 19.986 -31.045 1.079   1.00 43.30  ? 93  GLY   A C   1 
ATOM   747  O O   . GLY   A 1 93  ? 20.376 -30.084 1.746   1.00 48.77  ? 93  GLY   A O   1 
ATOM   748  N N   . LYS   A 1 94  ? 18.969 -31.816 1.467   1.00 45.07  ? 94  LYS   A N   1 
ATOM   749  C CA  . LYS   A 1 94  ? 18.298 -31.578 2.740   1.00 50.36  ? 94  LYS   A CA  1 
ATOM   750  C C   . LYS   A 1 94  ? 19.247 -31.794 3.912   1.00 47.87  ? 94  LYS   A C   1 
ATOM   751  O O   . LYS   A 1 94  ? 19.155 -31.099 4.931   1.00 45.98  ? 94  LYS   A O   1 
ATOM   752  C CB  . LYS   A 1 94  ? 17.078 -32.490 2.865   1.00 44.97  ? 94  LYS   A CB  1 
ATOM   753  C CG  . LYS   A 1 94  ? 15.981 -32.229 1.837   1.00 54.95  ? 94  LYS   A CG  1 
ATOM   754  C CD  . LYS   A 1 94  ? 15.261 -30.916 2.107   1.00 60.65  ? 94  LYS   A CD  1 
ATOM   755  C CE  . LYS   A 1 94  ? 14.103 -30.715 1.139   1.00 66.91  ? 94  LYS   A CE  1 
ATOM   756  N NZ  . LYS   A 1 94  ? 13.365 -29.450 1.409   1.00 75.38  ? 94  LYS   A NZ  1 
ATOM   757  N N   . ASN   A 1 95  ? 20.168 -32.753 3.786   1.00 48.65  ? 95  ASN   A N   1 
ATOM   758  C CA  . ASN   A 1 95  ? 21.116 -33.018 4.864   1.00 46.81  ? 95  ASN   A CA  1 
ATOM   759  C C   . ASN   A 1 95  ? 22.053 -31.836 5.075   1.00 43.08  ? 95  ASN   A C   1 
ATOM   760  O O   . ASN   A 1 95  ? 22.211 -31.342 6.199   1.00 44.02  ? 95  ASN   A O   1 
ATOM   761  C CB  . ASN   A 1 95  ? 21.912 -34.290 4.566   1.00 45.50  ? 95  ASN   A CB  1 
ATOM   762  C CG  . ASN   A 1 95  ? 21.058 -35.546 4.648   1.00 53.61  ? 95  ASN   A CG  1 
ATOM   763  O OD1 . ASN   A 1 95  ? 20.050 -35.577 5.355   1.00 51.39  ? 95  ASN   A OD1 1 
ATOM   764  N ND2 . ASN   A 1 95  ? 21.465 -36.590 3.932   1.00 59.66  ? 95  ASN   A ND2 1 
ATOM   765  N N   . ILE   A 1 96  ? 22.685 -31.365 3.998   1.00 46.40  ? 96  ILE   A N   1 
ATOM   766  C CA  . ILE   A 1 96  ? 23.643 -30.272 4.118   1.00 43.42  ? 96  ILE   A CA  1 
ATOM   767  C C   . ILE   A 1 96  ? 22.936 -28.975 4.487   1.00 48.46  ? 96  ILE   A C   1 
ATOM   768  O O   . ILE   A 1 96  ? 23.491 -28.140 5.215   1.00 44.25  ? 96  ILE   A O   1 
ATOM   769  C CB  . ILE   A 1 96  ? 24.450 -30.136 2.814   1.00 45.86  ? 96  ILE   A CB  1 
ATOM   770  C CG1 . ILE   A 1 96  ? 25.122 -31.465 2.473   1.00 45.20  ? 96  ILE   A CG1 1 
ATOM   771  C CG2 . ILE   A 1 96  ? 25.499 -29.038 2.934   1.00 47.76  ? 96  ILE   A CG2 1 
ATOM   772  C CD1 . ILE   A 1 96  ? 25.893 -31.442 1.178   1.00 48.53  ? 96  ILE   A CD1 1 
ATOM   773  N N   . GLU   A 1 97  ? 21.706 -28.783 4.002   1.00 43.53  ? 97  GLU   A N   1 
ATOM   774  C CA  . GLU   A 1 97  ? 20.945 -27.593 4.370   1.00 42.97  ? 97  GLU   A CA  1 
ATOM   775  C C   . GLU   A 1 97  ? 20.701 -27.550 5.872   1.00 42.58  ? 97  GLU   A C   1 
ATOM   776  O O   . GLU   A 1 97  ? 20.862 -26.503 6.510   1.00 49.14  ? 97  GLU   A O   1 
ATOM   777  C CB  . GLU   A 1 97  ? 19.621 -27.555 3.607   1.00 40.61  ? 97  GLU   A CB  1 
ATOM   778  C CG  . GLU   A 1 97  ? 18.637 -26.513 4.121   1.00 49.60  ? 97  GLU   A CG  1 
ATOM   779  C CD  . GLU   A 1 97  ? 17.298 -26.570 3.409   1.00 58.38  ? 97  GLU   A CD  1 
ATOM   780  O OE1 . GLU   A 1 97  ? 17.209 -26.081 2.262   1.00 58.39  ? 97  GLU   A OE1 1 
ATOM   781  O OE2 . GLU   A 1 97  ? 16.334 -27.110 3.995   1.00 62.92  ? 97  GLU   A OE2 1 
ATOM   782  N N   . ALA   A 1 98  ? 20.311 -28.686 6.454   1.00 43.00  ? 98  ALA   A N   1 
ATOM   783  C CA  . ALA   A 1 98  ? 20.133 -28.746 7.900   1.00 45.46  ? 98  ALA   A CA  1 
ATOM   784  C C   . ALA   A 1 98  ? 21.452 -28.515 8.620   1.00 46.02  ? 98  ALA   A C   1 
ATOM   785  O O   . ALA   A 1 98  ? 21.490 -27.860 9.670   1.00 45.40  ? 98  ALA   A O   1 
ATOM   786  C CB  . ALA   A 1 98  ? 19.532 -30.091 8.300   1.00 46.22  ? 98  ALA   A CB  1 
ATOM   787  N N   . TYR   A 1 99  ? 22.546 -29.045 8.070   1.00 43.83  ? 99  TYR   A N   1 
ATOM   788  C CA  . TYR   A 1 99  ? 23.859 -28.802 8.657   1.00 45.76  ? 99  TYR   A CA  1 
ATOM   789  C C   . TYR   A 1 99  ? 24.254 -27.339 8.525   1.00 43.92  ? 99  TYR   A C   1 
ATOM   790  O O   . TYR   A 1 99  ? 24.817 -26.751 9.457   1.00 53.51  ? 99  TYR   A O   1 
ATOM   791  C CB  . TYR   A 1 99  ? 24.901 -29.704 7.997   1.00 52.69  ? 99  TYR   A CB  1 
ATOM   792  C CG  . TYR   A 1 99  ? 26.316 -29.504 8.494   1.00 48.64  ? 99  TYR   A CG  1 
ATOM   793  C CD1 . TYR   A 1 99  ? 26.753 -30.106 9.666   1.00 54.29  ? 99  TYR   A CD1 1 
ATOM   794  C CD2 . TYR   A 1 99  ? 27.219 -28.724 7.784   1.00 47.30  ? 99  TYR   A CD2 1 
ATOM   795  C CE1 . TYR   A 1 99  ? 28.050 -29.932 10.122  1.00 54.37  ? 99  TYR   A CE1 1 
ATOM   796  C CE2 . TYR   A 1 99  ? 28.520 -28.542 8.232   1.00 54.14  ? 99  TYR   A CE2 1 
ATOM   797  C CZ  . TYR   A 1 99  ? 28.929 -29.149 9.401   1.00 57.07  ? 99  TYR   A CZ  1 
ATOM   798  O OH  . TYR   A 1 99  ? 30.219 -28.971 9.850   1.00 60.36  ? 99  TYR   A OH  1 
ATOM   799  N N   . PHE   A 1 100 ? 23.960 -26.732 7.373   1.00 46.42  ? 100 PHE   A N   1 
ATOM   800  C CA  . PHE   A 1 100 ? 24.302 -25.331 7.158   1.00 40.84  ? 100 PHE   A CA  1 
ATOM   801  C C   . PHE   A 1 100 ? 23.529 -24.420 8.104   1.00 44.37  ? 100 PHE   A C   1 
ATOM   802  O O   . PHE   A 1 100 ? 24.098 -23.483 8.677   1.00 46.63  ? 100 PHE   A O   1 
ATOM   803  C CB  . PHE   A 1 100 ? 24.035 -24.946 5.702   1.00 39.61  ? 100 PHE   A CB  1 
ATOM   804  C CG  . PHE   A 1 100 ? 24.119 -23.469 5.440   1.00 46.73  ? 100 PHE   A CG  1 
ATOM   805  C CD1 . PHE   A 1 100 ? 25.342 -22.820 5.458   1.00 45.43  ? 100 PHE   A CD1 1 
ATOM   806  C CD2 . PHE   A 1 100 ? 22.977 -22.732 5.172   1.00 40.84  ? 100 PHE   A CD2 1 
ATOM   807  C CE1 . PHE   A 1 100 ? 25.424 -21.460 5.219   1.00 47.34  ? 100 PHE   A CE1 1 
ATOM   808  C CE2 . PHE   A 1 100 ? 23.053 -21.373 4.930   1.00 39.50  ? 100 PHE   A CE2 1 
ATOM   809  C CZ  . PHE   A 1 100 ? 24.278 -20.737 4.954   1.00 49.11  ? 100 PHE   A CZ  1 
ATOM   810  N N   . ASN   A 1 101 ? 22.232 -24.682 8.283   1.00 43.89  ? 101 ASN   A N   1 
ATOM   811  C CA  . ASN   A 1 101 ? 21.427 -23.850 9.172   1.00 49.94  ? 101 ASN   A CA  1 
ATOM   812  C C   . ASN   A 1 101 ? 21.883 -23.969 10.621  1.00 51.30  ? 101 ASN   A C   1 
ATOM   813  O O   . ASN   A 1 101 ? 21.808 -22.993 11.377  1.00 54.41  ? 101 ASN   A O   1 
ATOM   814  C CB  . ASN   A 1 101 ? 19.949 -24.220 9.047   1.00 44.58  ? 101 ASN   A CB  1 
ATOM   815  C CG  . ASN   A 1 101 ? 19.346 -23.778 7.727   1.00 45.47  ? 101 ASN   A CG  1 
ATOM   816  O OD1 . ASN   A 1 101 ? 19.765 -22.776 7.145   1.00 46.93  ? 101 ASN   A OD1 1 
ATOM   817  N ND2 . ASN   A 1 101 ? 18.356 -24.522 7.248   1.00 47.87  ? 101 ASN   A ND2 1 
ATOM   818  N N   . ASN   A 1 102 ? 22.355 -25.149 11.029  1.00 47.46  ? 102 ASN   A N   1 
ATOM   819  C CA  . ASN   A 1 102 ? 22.857 -25.303 12.390  1.00 47.03  ? 102 ASN   A CA  1 
ATOM   820  C C   . ASN   A 1 102 ? 24.217 -24.639 12.560  1.00 55.65  ? 102 ASN   A C   1 
ATOM   821  O O   . ASN   A 1 102 ? 24.534 -24.149 13.651  1.00 52.48  ? 102 ASN   A O   1 
ATOM   822  C CB  . ASN   A 1 102 ? 22.935 -26.784 12.758  1.00 53.86  ? 102 ASN   A CB  1 
ATOM   823  C CG  . ASN   A 1 102 ? 23.168 -27.007 14.240  1.00 57.58  ? 102 ASN   A CG  1 
ATOM   824  O OD1 . ASN   A 1 102 ? 22.249 -26.879 15.051  1.00 65.02  ? 102 ASN   A OD1 1 
ATOM   825  N ND2 . ASN   A 1 102 ? 24.399 -27.352 14.602  1.00 63.55  ? 102 ASN   A ND2 1 
ATOM   826  N N   . GLN   A 1 103 ? 25.028 -24.605 11.499  1.00 48.76  ? 103 GLN   A N   1 
ATOM   827  C CA  . GLN   A 1 103 ? 26.330 -23.951 11.586  1.00 54.76  ? 103 GLN   A CA  1 
ATOM   828  C C   . GLN   A 1 103 ? 26.182 -22.444 11.739  1.00 48.29  ? 103 GLN   A C   1 
ATOM   829  O O   . GLN   A 1 103 ? 26.986 -21.804 12.427  1.00 50.69  ? 103 GLN   A O   1 
ATOM   830  C CB  . GLN   A 1 103 ? 27.175 -24.284 10.357  1.00 45.98  ? 103 GLN   A CB  1 
ATOM   831  C CG  . GLN   A 1 103 ? 27.745 -25.690 10.364  1.00 55.78  ? 103 GLN   A CG  1 
ATOM   832  C CD  . GLN   A 1 103 ? 28.596 -25.963 11.587  1.00 55.07  ? 103 GLN   A CD  1 
ATOM   833  O OE1 . GLN   A 1 103 ? 28.434 -26.986 12.253  1.00 65.65  ? 103 GLN   A OE1 1 
ATOM   834  N NE2 . GLN   A 1 103 ? 29.512 -25.049 11.889  1.00 52.25  ? 103 GLN   A NE2 1 
ATOM   835  N N   . LEU   A 1 104 ? 25.162 -21.859 11.106  1.00 47.01  ? 104 LEU   A N   1 
ATOM   836  C CA  . LEU   A 1 104 ? 24.922 -20.428 11.254  1.00 49.46  ? 104 LEU   A CA  1 
ATOM   837  C C   . LEU   A 1 104 ? 24.651 -20.052 12.704  1.00 54.87  ? 104 LEU   A C   1 
ATOM   838  O O   . LEU   A 1 104 ? 24.864 -18.900 13.096  1.00 60.81  ? 104 LEU   A O   1 
ATOM   839  C CB  . LEU   A 1 104 ? 23.754 -19.995 10.368  1.00 48.98  ? 104 LEU   A CB  1 
ATOM   840  C CG  . LEU   A 1 104 ? 23.942 -20.137 8.857   1.00 49.08  ? 104 LEU   A CG  1 
ATOM   841  C CD1 . LEU   A 1 104 ? 22.690 -19.691 8.115   1.00 42.62  ? 104 LEU   A CD1 1 
ATOM   842  C CD2 . LEU   A 1 104 ? 25.156 -19.347 8.393   1.00 44.23  ? 104 LEU   A CD2 1 
ATOM   843  N N   . ILE   A 1 105 ? 24.193 -21.004 13.511  1.00 52.55  ? 105 ILE   A N   1 
ATOM   844  C CA  . ILE   A 1 105 ? 23.905 -20.745 14.918  1.00 49.35  ? 105 ILE   A CA  1 
ATOM   845  C C   . ILE   A 1 105 ? 25.129 -20.987 15.790  1.00 55.44  ? 105 ILE   A C   1 
ATOM   846  O O   . ILE   A 1 105 ? 25.466 -20.163 16.645  1.00 58.94  ? 105 ILE   A O   1 
ATOM   847  C CB  . ILE   A 1 105 ? 22.712 -21.609 15.379  1.00 51.75  ? 105 ILE   A CB  1 
ATOM   848  C CG1 . ILE   A 1 105 ? 21.513 -21.409 14.452  1.00 50.10  ? 105 ILE   A CG1 1 
ATOM   849  C CG2 . ILE   A 1 105 ? 22.339 -21.278 16.816  1.00 52.98  ? 105 ILE   A CG2 1 
ATOM   850  C CD1 . ILE   A 1 105 ? 20.319 -22.261 14.816  1.00 51.49  ? 105 ILE   A CD1 1 
ATOM   851  N N   . VAL   A 1 106 ? 25.816 -22.114 15.588  1.00 50.81  ? 106 VAL   A N   1 
ATOM   852  C CA  . VAL   A 1 106 ? 26.915 -22.482 16.478  1.00 54.94  ? 106 VAL   A CA  1 
ATOM   853  C C   . VAL   A 1 106 ? 28.144 -21.615 16.230  1.00 56.01  ? 106 VAL   A C   1 
ATOM   854  O O   . VAL   A 1 106 ? 28.932 -21.370 17.151  1.00 51.77  ? 106 VAL   A O   1 
ATOM   855  C CB  . VAL   A 1 106 ? 27.240 -23.981 16.336  1.00 56.26  ? 106 VAL   A CB  1 
ATOM   856  C CG1 . VAL   A 1 106 ? 26.014 -24.818 16.661  1.00 58.96  ? 106 VAL   A CG1 1 
ATOM   857  C CG2 . VAL   A 1 106 ? 27.747 -24.296 14.937  1.00 53.90  ? 106 VAL   A CG2 1 
ATOM   858  N N   . THR   A 1 107 ? 28.338 -21.140 14.998  1.00 59.01  ? 107 THR   A N   1 
ATOM   859  C CA  . THR   A 1 107 ? 29.449 -20.238 14.726  1.00 51.55  ? 107 THR   A CA  1 
ATOM   860  C C   . THR   A 1 107 ? 29.142 -18.804 15.131  1.00 58.31  ? 107 THR   A C   1 
ATOM   861  O O   . THR   A 1 107 ? 30.068 -17.992 15.238  1.00 62.69  ? 107 THR   A O   1 
ATOM   862  C CB  . THR   A 1 107 ? 29.823 -20.273 13.241  1.00 51.38  ? 107 THR   A CB  1 
ATOM   863  O OG1 . THR   A 1 107 ? 28.713 -19.823 12.455  1.00 49.24  ? 107 THR   A OG1 1 
ATOM   864  C CG2 . THR   A 1 107 ? 30.211 -21.683 12.815  1.00 47.73  ? 107 THR   A CG2 1 
ATOM   865  N N   . GLY   A 1 108 ? 27.874 -18.478 15.367  1.00 57.99  ? 108 GLY   A N   1 
ATOM   866  C CA  . GLY   A 1 108 ? 27.490 -17.114 15.651  1.00 59.30  ? 108 GLY   A CA  1 
ATOM   867  C C   . GLY   A 1 108 ? 27.333 -16.235 14.433  1.00 59.29  ? 108 GLY   A C   1 
ATOM   868  O O   . GLY   A 1 108 ? 27.289 -15.008 14.577  1.00 54.93  ? 108 GLY   A O   1 
ATOM   869  N N   . TYR   A 1 109 ? 27.251 -16.822 13.235  1.00 57.13  ? 109 TYR   A N   1 
ATOM   870  C CA  . TYR   A 1 109 ? 27.102 -16.018 12.027  1.00 49.95  ? 109 TYR   A CA  1 
ATOM   871  C C   . TYR   A 1 109 ? 25.790 -15.247 12.030  1.00 52.52  ? 109 TYR   A C   1 
ATOM   872  O O   . TYR   A 1 109 ? 25.705 -14.166 11.435  1.00 59.25  ? 109 TYR   A O   1 
ATOM   873  C CB  . TYR   A 1 109 ? 27.196 -16.910 10.789  1.00 48.71  ? 109 TYR   A CB  1 
ATOM   874  C CG  . TYR   A 1 109 ? 27.322 -16.150 9.487   1.00 45.54  ? 109 TYR   A CG  1 
ATOM   875  C CD1 . TYR   A 1 109 ? 26.195 -15.765 8.771   1.00 46.10  ? 109 TYR   A CD1 1 
ATOM   876  C CD2 . TYR   A 1 109 ? 28.569 -15.826 8.969   1.00 43.56  ? 109 TYR   A CD2 1 
ATOM   877  C CE1 . TYR   A 1 109 ? 26.307 -15.071 7.580   1.00 47.51  ? 109 TYR   A CE1 1 
ATOM   878  C CE2 . TYR   A 1 109 ? 28.691 -15.134 7.778   1.00 44.19  ? 109 TYR   A CE2 1 
ATOM   879  C CZ  . TYR   A 1 109 ? 27.557 -14.760 7.089   1.00 43.12  ? 109 TYR   A CZ  1 
ATOM   880  O OH  . TYR   A 1 109 ? 27.672 -14.072 5.904   1.00 46.82  ? 109 TYR   A OH  1 
ATOM   881  N N   . ASN   A 1 110 ? 24.757 -15.783 12.688  1.00 57.59  ? 110 ASN   A N   1 
ATOM   882  C CA  . ASN   A 1 110 ? 23.493 -15.062 12.790  1.00 58.50  ? 110 ASN   A CA  1 
ATOM   883  C C   . ASN   A 1 110 ? 23.650 -13.762 13.568  1.00 57.56  ? 110 ASN   A C   1 
ATOM   884  O O   . ASN   A 1 110 ? 22.889 -12.812 13.347  1.00 57.16  ? 110 ASN   A O   1 
ATOM   885  C CB  . ASN   A 1 110 ? 22.430 -15.945 13.446  1.00 52.00  ? 110 ASN   A CB  1 
ATOM   886  C CG  . ASN   A 1 110 ? 21.947 -17.056 12.533  1.00 57.61  ? 110 ASN   A CG  1 
ATOM   887  O OD1 . ASN   A 1 110 ? 22.038 -16.953 11.310  1.00 60.11  ? 110 ASN   A OD1 1 
ATOM   888  N ND2 . ASN   A 1 110 ? 21.423 -18.123 13.125  1.00 54.26  ? 110 ASN   A ND2 1 
ATOM   889  N N   . ASN   A 1 111 ? 24.622 -13.699 14.482  1.00 55.79  ? 111 ASN   A N   1 
ATOM   890  C CA  . ASN   A 1 111 ? 24.863 -12.462 15.216  1.00 61.52  ? 111 ASN   A CA  1 
ATOM   891  C C   . ASN   A 1 111 ? 25.322 -11.352 14.281  1.00 57.49  ? 111 ASN   A C   1 
ATOM   892  O O   . ASN   A 1 111 ? 24.920 -10.194 14.438  1.00 55.88  ? 111 ASN   A O   1 
ATOM   893  C CB  . ASN   A 1 111 ? 25.893 -12.698 16.321  1.00 62.20  ? 111 ASN   A CB  1 
ATOM   894  C CG  . ASN   A 1 111 ? 25.445 -13.748 17.318  1.00 70.39  ? 111 ASN   A CG  1 
ATOM   895  O OD1 . ASN   A 1 111 ? 24.270 -13.816 17.680  1.00 61.77  ? 111 ASN   A OD1 1 
ATOM   896  N ND2 . ASN   A 1 111 ? 26.382 -14.576 17.766  1.00 74.51  ? 111 ASN   A ND2 1 
ATOM   897  N N   . PHE   A 1 112 ? 26.163 -11.686 13.299  1.00 56.78  ? 112 PHE   A N   1 
ATOM   898  C CA  . PHE   A 1 112 ? 26.523 -10.707 12.279  1.00 54.68  ? 112 PHE   A CA  1 
ATOM   899  C C   . PHE   A 1 112 ? 25.316 -10.313 11.442  1.00 57.73  ? 112 PHE   A C   1 
ATOM   900  O O   . PHE   A 1 112 ? 25.223 -9.168  10.985  1.00 53.91  ? 112 PHE   A O   1 
ATOM   901  C CB  . PHE   A 1 112 ? 27.632 -11.258 11.382  1.00 50.50  ? 112 PHE   A CB  1 
ATOM   902  C CG  . PHE   A 1 112 ? 28.959 -11.389 12.071  1.00 53.91  ? 112 PHE   A CG  1 
ATOM   903  C CD1 . PHE   A 1 112 ? 29.306 -12.562 12.721  1.00 54.30  ? 112 PHE   A CD1 1 
ATOM   904  C CD2 . PHE   A 1 112 ? 29.862 -10.338 12.065  1.00 53.76  ? 112 PHE   A CD2 1 
ATOM   905  C CE1 . PHE   A 1 112 ? 30.528 -12.684 13.355  1.00 58.58  ? 112 PHE   A CE1 1 
ATOM   906  C CE2 . PHE   A 1 112 ? 31.086 -10.454 12.697  1.00 64.70  ? 112 PHE   A CE2 1 
ATOM   907  C CZ  . PHE   A 1 112 ? 31.419 -11.628 13.343  1.00 59.84  ? 112 PHE   A CZ  1 
ATOM   908  N N   . VAL   A 1 113 ? 24.384 -11.244 11.231  1.00 53.86  ? 113 VAL   A N   1 
ATOM   909  C CA  . VAL   A 1 113 ? 23.157 -10.925 10.511  1.00 56.80  ? 113 VAL   A CA  1 
ATOM   910  C C   . VAL   A 1 113 ? 22.284 -9.986  11.334  1.00 66.13  ? 113 VAL   A C   1 
ATOM   911  O O   . VAL   A 1 113 ? 21.726 -9.015  10.810  1.00 62.90  ? 113 VAL   A O   1 
ATOM   912  C CB  . VAL   A 1 113 ? 22.411 -12.220 10.142  1.00 52.75  ? 113 VAL   A CB  1 
ATOM   913  C CG1 . VAL   A 1 113 ? 21.042 -11.905 9.567   1.00 56.83  ? 113 VAL   A CG1 1 
ATOM   914  C CG2 . VAL   A 1 113 ? 23.232 -13.041 9.161   1.00 53.62  ? 113 VAL   A CG2 1 
ATOM   915  N N   . THR   A 1 114 ? 22.162 -10.254 12.637  1.00 63.18  ? 114 THR   A N   1 
ATOM   916  C CA  . THR   A 1 114 ? 21.313 -9.431  13.493  1.00 64.65  ? 114 THR   A CA  1 
ATOM   917  C C   . THR   A 1 114 ? 21.838 -8.003  13.583  1.00 70.31  ? 114 THR   A C   1 
ATOM   918  O O   . THR   A 1 114 ? 21.075 -7.038  13.454  1.00 75.08  ? 114 THR   A O   1 
ATOM   919  C CB  . THR   A 1 114 ? 21.211 -10.055 14.886  1.00 59.01  ? 114 THR   A CB  1 
ATOM   920  O OG1 . THR   A 1 114 ? 20.577 -11.337 14.791  1.00 67.93  ? 114 THR   A OG1 1 
ATOM   921  C CG2 . THR   A 1 114 ? 20.400 -9.163  15.813  1.00 70.15  ? 114 THR   A CG2 1 
ATOM   922  N N   . LYS   A 1 115 ? 23.146 -7.848  13.800  1.00 68.96  ? 115 LYS   A N   1 
ATOM   923  C CA  . LYS   A 1 115 ? 23.710 -6.508  13.918  1.00 70.63  ? 115 LYS   A CA  1 
ATOM   924  C C   . LYS   A 1 115 ? 23.681 -5.767  12.588  1.00 67.54  ? 115 LYS   A C   1 
ATOM   925  O O   . LYS   A 1 115 ? 23.602 -4.534  12.570  1.00 78.49  ? 115 LYS   A O   1 
ATOM   926  C CB  . LYS   A 1 115 ? 25.138 -6.579  14.460  1.00 65.07  ? 115 LYS   A CB  1 
ATOM   927  C CG  . LYS   A 1 115 ? 25.268 -7.351  15.766  1.00 76.18  ? 115 LYS   A CG  1 
ATOM   928  C CD  . LYS   A 1 115 ? 26.263 -6.699  16.711  1.00 74.97  ? 115 LYS   A CD  1 
ATOM   929  C CE  . LYS   A 1 115 ? 25.683 -5.435  17.327  1.00 76.80  ? 115 LYS   A CE  1 
ATOM   930  N NZ  . LYS   A 1 115 ? 26.589 -4.853  18.354  1.00 71.33  ? 115 LYS   A NZ  1 
ATOM   931  N N   . ALA   A 1 116 ? 23.731 -6.495  11.469  1.00 63.80  ? 116 ALA   A N   1 
ATOM   932  C CA  . ALA   A 1 116 ? 23.719 -5.853  10.160  1.00 64.95  ? 116 ALA   A CA  1 
ATOM   933  C C   . ALA   A 1 116 ? 22.339 -5.327  9.788   1.00 81.69  ? 116 ALA   A C   1 
ATOM   934  O O   . ALA   A 1 116 ? 22.239 -4.310  9.093   1.00 87.34  ? 116 ALA   A O   1 
ATOM   935  C CB  . ALA   A 1 116 ? 24.210 -6.828  9.088   1.00 55.42  ? 116 ALA   A CB  1 
ATOM   936  N N   . ASN   A 1 117 ? 21.272 -6.001  10.225  1.00 81.60  ? 117 ASN   A N   1 
ATOM   937  C CA  . ASN   A 1 117 ? 19.928 -5.538  9.895   1.00 80.49  ? 117 ASN   A CA  1 
ATOM   938  C C   . ASN   A 1 117 ? 19.583 -4.246  10.625  1.00 87.75  ? 117 ASN   A C   1 
ATOM   939  O O   . ASN   A 1 117 ? 18.860 -3.403  10.082  1.00 93.87  ? 117 ASN   A O   1 
ATOM   940  C CB  . ASN   A 1 117 ? 18.900 -6.621  10.218  1.00 80.70  ? 117 ASN   A CB  1 
ATOM   941  C CG  . ASN   A 1 117 ? 19.141 -7.904  9.446   1.00 87.82  ? 117 ASN   A CG  1 
ATOM   942  O OD1 . ASN   A 1 117 ? 19.030 -9.000  9.994   1.00 81.58  ? 117 ASN   A OD1 1 
ATOM   943  N ND2 . ASN   A 1 117 ? 19.477 -7.773  8.167   1.00 86.22  ? 117 ASN   A ND2 1 
ATOM   944  N N   . THR   A 1 118 ? 20.086 -4.072  11.849  1.00 86.18  ? 118 THR   A N   1 
ATOM   945  C CA  . THR   A 1 118 ? 19.841 -2.831  12.577  1.00 93.68  ? 118 THR   A CA  1 
ATOM   946  C C   . THR   A 1 118 ? 20.613 -1.672  11.960  1.00 95.92  ? 118 THR   A C   1 
ATOM   947  O O   . THR   A 1 118 ? 20.119 -0.538  11.927  1.00 97.98  ? 118 THR   A O   1 
ATOM   948  C CB  . THR   A 1 118 ? 20.214 -3.004  14.049  1.00 96.18  ? 118 THR   A CB  1 
ATOM   949  O OG1 . THR   A 1 118 ? 19.526 -4.141  14.587  1.00 95.23  ? 118 THR   A OG1 1 
ATOM   950  C CG2 . THR   A 1 118 ? 19.832 -1.764  14.847  1.00 104.11 ? 118 THR   A CG2 1 
ATOM   951  N N   . ILE   A 1 119 ? 21.826 -1.937  11.467  1.00 96.23  ? 119 ILE   A N   1 
ATOM   952  C CA  . ILE   A 1 119 ? 22.609 -0.900  10.800  1.00 90.19  ? 119 ILE   A CA  1 
ATOM   953  C C   . ILE   A 1 119 ? 21.864 -0.375  9.580   1.00 97.27  ? 119 ILE   A C   1 
ATOM   954  O O   . ILE   A 1 119 ? 21.837 0.835   9.320   1.00 106.07 ? 119 ILE   A O   1 
ATOM   955  C CB  . ILE   A 1 119 ? 24.000 -1.444  10.423  1.00 84.77  ? 119 ILE   A CB  1 
ATOM   956  C CG1 . ILE   A 1 119 ? 24.804 -1.776  11.681  1.00 73.60  ? 119 ILE   A CG1 1 
ATOM   957  C CG2 . ILE   A 1 119 ? 24.752 -0.450  9.552   1.00 78.86  ? 119 ILE   A CG2 1 
ATOM   958  C CD1 . ILE   A 1 119 ? 26.055 -2.581  11.407  1.00 68.07  ? 119 ILE   A CD1 1 
ATOM   959  N N   . ASN   A 1 120 ? 21.239 -1.269  8.821   1.00 103.56 ? 120 ASN   A N   1 
ATOM   960  C CA  . ASN   A 1 120 ? 20.501 -0.885  7.625   1.00 103.59 ? 120 ASN   A CA  1 
ATOM   961  C C   . ASN   A 1 120 ? 19.000 -0.843  7.898   1.00 100.74 ? 120 ASN   A C   1 
ATOM   962  O O   . ASN   A 1 120 ? 18.214 -0.429  7.045   1.00 97.85  ? 120 ASN   A O   1 
ATOM   963  C CB  . ASN   A 1 120 ? 20.807 -1.853  6.482   1.00 106.87 ? 120 ASN   A CB  1 
ATOM   964  C CG  . ASN   A 1 120 ? 22.296 -2.020  6.245   1.00 99.60  ? 120 ASN   A CG  1 
ATOM   965  O OD1 . ASN   A 1 120 ? 22.858 -3.089  6.481   1.00 89.65  ? 120 ASN   A OD1 1 
ATOM   966  N ND2 . ASN   A 1 120 ? 22.944 -0.960  5.776   1.00 104.16 ? 120 ASN   A ND2 1 
HETATM 967  S S   . SO4   B 2 .   ? 34.647 -25.972 -13.414 1.00 79.74  ? 201 SO4   A S   1 
HETATM 968  O O1  . SO4   B 2 .   ? 34.514 -26.010 -14.906 1.00 67.32  ? 201 SO4   A O1  1 
HETATM 969  O O2  . SO4   B 2 .   ? 34.163 -24.650 -12.903 1.00 57.50  ? 201 SO4   A O2  1 
HETATM 970  O O3  . SO4   B 2 .   ? 33.831 -27.079 -12.816 1.00 59.74  ? 201 SO4   A O3  1 
HETATM 971  O O4  . SO4   B 2 .   ? 36.086 -26.155 -13.037 1.00 92.06  ? 201 SO4   A O4  1 
HETATM 972  C C01 A A1IUY C 3 .   ? 23.180 -34.064 -10.772 0.51 48.78  ? 202 A1IUY A C01 1 
HETATM 973  C C01 B A1IUY C 3 .   ? 23.030 -34.081 -10.685 0.49 48.69  ? 202 A1IUY A C01 1 
HETATM 974  C C02 A A1IUY C 3 .   ? 22.583 -33.449 -12.046 0.51 48.65  ? 202 A1IUY A C02 1 
HETATM 975  C C02 B A1IUY C 3 .   ? 22.808 -33.457 -12.081 0.49 48.71  ? 202 A1IUY A C02 1 
HETATM 976  C C03 A A1IUY C 3 .   ? 21.080 -33.209 -11.927 0.51 44.70  ? 202 A1IUY A C03 1 
HETATM 977  C C03 B A1IUY C 3 .   ? 21.679 -32.414 -12.119 0.49 46.54  ? 202 A1IUY A C03 1 
HETATM 978  C C04 A A1IUY C 3 .   ? 20.647 -32.997 -10.468 0.51 43.93  ? 202 A1IUY A C04 1 
HETATM 979  C C04 B A1IUY C 3 .   ? 20.855 -32.379 -10.823 0.49 44.46  ? 202 A1IUY A C04 1 
HETATM 980  C C05 A A1IUY C 3 .   ? 21.430 -31.975 -9.625  0.51 43.71  ? 202 A1IUY A C05 1 
HETATM 981  C C05 B A1IUY C 3 .   ? 21.530 -31.834 -9.555  0.49 43.66  ? 202 A1IUY A C05 1 
HETATM 982  C C07 A A1IUY C 3 .   ? 22.843 -32.059 -9.191  0.51 44.47  ? 202 A1IUY A C07 1 
HETATM 983  C C07 B A1IUY C 3 .   ? 22.920 -32.058 -9.111  0.49 44.44  ? 202 A1IUY A C07 1 
HETATM 984  C C08 A A1IUY C 3 .   ? 23.692 -33.095 -9.757  0.51 48.12  ? 202 A1IUY A C08 1 
HETATM 985  C C08 B A1IUY C 3 .   ? 23.653 -33.180 -9.665  0.49 48.19  ? 202 A1IUY A C08 1 
HETATM 986  C C09 A A1IUY C 3 .   ? 23.627 -31.323 -8.277  0.51 42.83  ? 202 A1IUY A C09 1 
HETATM 987  C C09 B A1IUY C 3 .   ? 23.764 -31.409 -8.193  0.49 42.77  ? 202 A1IUY A C09 1 
HETATM 988  C C10 A A1IUY C 3 .   ? 23.298 -30.154 -7.403  0.51 42.50  ? 202 A1IUY A C10 1 
HETATM 989  C C10 B A1IUY C 3 .   ? 23.545 -30.210 -7.330  0.49 42.75  ? 202 A1IUY A C10 1 
HETATM 990  C C12 A A1IUY C 3 .   ? 24.974 -32.948 -9.164  0.51 46.17  ? 202 A1IUY A C12 1 
HETATM 991  C C12 B A1IUY C 3 .   ? 24.946 -33.168 -9.061  0.49 46.31  ? 202 A1IUY A C12 1 
HETATM 992  C C13 A A1IUY C 3 .   ? 26.238 -33.690 -9.349  0.51 51.42  ? 202 A1IUY A C13 1 
HETATM 993  C C13 B A1IUY C 3 .   ? 26.136 -34.040 -9.223  0.49 51.33  ? 202 A1IUY A C13 1 
HETATM 994  C C14 A A1IUY C 3 .   ? 27.299 -32.960 -9.915  0.51 51.13  ? 202 A1IUY A C14 1 
HETATM 995  C C14 B A1IUY C 3 .   ? 27.291 -33.423 -9.743  0.49 53.23  ? 202 A1IUY A C14 1 
HETATM 996  C C15 A A1IUY C 3 .   ? 28.530 -33.585 -10.128 0.51 54.41  ? 202 A1IUY A C15 1 
HETATM 997  C C15 B A1IUY C 3 .   ? 28.454 -34.178 -9.925  0.49 55.85  ? 202 A1IUY A C15 1 
HETATM 998  C C16 A A1IUY C 3 .   ? 28.698 -34.934 -9.780  0.51 56.76  ? 202 A1IUY A C16 1 
HETATM 999  C C16 B A1IUY C 3 .   ? 28.464 -35.543 -9.590  0.49 56.27  ? 202 A1IUY A C16 1 
HETATM 1000 C C17 A A1IUY C 3 .   ? 27.654 -35.705 -9.210  0.51 55.83  ? 202 A1IUY A C17 1 
HETATM 1001 C C17 B A1IUY C 3 .   ? 27.323 -36.198 -9.063  0.49 55.56  ? 202 A1IUY A C17 1 
HETATM 1002 C C18 A A1IUY C 3 .   ? 26.396 -35.064 -8.993  0.51 51.76  ? 202 A1IUY A C18 1 
HETATM 1003 C C18 B A1IUY C 3 .   ? 26.139 -35.426 -8.881  0.49 52.75  ? 202 A1IUY A C18 1 
HETATM 1004 C C19 A A1IUY C 3 .   ? 25.230 -35.815 -8.390  0.51 53.57  ? 202 A1IUY A C19 1 
HETATM 1005 C C19 B A1IUY C 3 .   ? 24.886 -36.057 -8.325  0.49 52.57  ? 202 A1IUY A C19 1 
HETATM 1006 C C24 A A1IUY C 3 .   ? 28.419 -39.851 -9.068  0.51 56.47  ? 202 A1IUY A C24 1 
HETATM 1007 C C24 B A1IUY C 3 .   ? 29.263 -39.706 -8.788  0.49 54.29  ? 202 A1IUY A C24 1 
HETATM 1008 N N11 A A1IUY C 3 .   ? 24.893 -31.875 -8.289  0.51 46.72  ? 202 A1IUY A N11 1 
HETATM 1009 N N11 B A1IUY C 3 .   ? 24.966 -32.088 -8.188  0.49 46.73  ? 202 A1IUY A N11 1 
HETATM 1010 N N20 A A1IUY C 3 .   ? 27.924 -37.110 -8.880  0.51 58.93  ? 202 A1IUY A N20 1 
HETATM 1011 N N20 B A1IUY C 3 .   ? 27.410 -37.631 -8.742  0.49 56.26  ? 202 A1IUY A N20 1 
HETATM 1012 O O06 A A1IUY C 3 .   ? 20.766 -30.979 -9.290  0.51 39.58  ? 202 A1IUY A O06 1 
HETATM 1013 O O06 B A1IUY C 3 .   ? 20.791 -31.123 -8.853  0.49 39.62  ? 202 A1IUY A O06 1 
HETATM 1014 O O22 A A1IUY C 3 .   ? 28.326 -38.291 -11.125 0.51 54.56  ? 202 A1IUY A O22 1 
HETATM 1015 O O22 B A1IUY C 3 .   ? 27.922 -39.055 -6.665  0.49 46.43  ? 202 A1IUY A O22 1 
HETATM 1016 O O23 A A1IUY C 3 .   ? 26.287 -38.691 -10.020 0.51 61.62  ? 202 A1IUY A O23 1 
HETATM 1017 O O23 B A1IUY C 3 .   ? 29.565 -37.535 -7.380  0.49 64.23  ? 202 A1IUY A O23 1 
HETATM 1018 S S21 A A1IUY C 3 .   ? 27.680 -38.472 -9.876  0.51 64.77  ? 202 A1IUY A S21 1 
HETATM 1019 S S21 B A1IUY C 3 .   ? 28.557 -38.449 -7.779  0.49 56.41  ? 202 A1IUY A S21 1 
HETATM 1020 O O   . HOH   D 4 .   ? 14.583 -35.126 0.098   1.00 46.61  ? 301 HOH   A O   1 
HETATM 1021 O O   . HOH   D 4 .   ? 19.583 -27.743 11.147  1.00 58.31  ? 302 HOH   A O   1 
HETATM 1022 O O   . HOH   D 4 .   ? 20.590 -28.206 -8.367  1.00 44.62  ? 303 HOH   A O   1 
HETATM 1023 O O   . HOH   D 4 .   ? 19.692 -20.894 4.569   1.00 46.55  ? 304 HOH   A O   1 
HETATM 1024 O O   . HOH   D 4 .   ? 32.386 -33.594 0.575   1.00 44.51  ? 305 HOH   A O   1 
HETATM 1025 O O   . HOH   D 4 .   ? 26.197 -28.424 -7.931  1.00 39.29  ? 306 HOH   A O   1 
HETATM 1026 O O   . HOH   D 4 .   ? 17.127 -20.982 -9.731  1.00 40.32  ? 307 HOH   A O   1 
HETATM 1027 O O   . HOH   D 4 .   ? 11.135 -31.328 -7.617  1.00 55.93  ? 308 HOH   A O   1 
HETATM 1028 O O   . HOH   D 4 .   ? 21.918 -27.074 -6.163  1.00 35.94  ? 309 HOH   A O   1 
HETATM 1029 O O   . HOH   D 4 .   ? 28.350 -5.439  6.240   1.00 54.54  ? 310 HOH   A O   1 
HETATM 1030 O O   . HOH   D 4 .   ? 30.115 -30.636 -8.159  1.00 42.75  ? 311 HOH   A O   1 
HETATM 1031 O O   . HOH   D 4 .   ? 16.796 -19.584 -3.319  1.00 56.66  ? 312 HOH   A O   1 
HETATM 1032 O O   . HOH   D 4 .   ? 19.818 -26.954 -19.603 1.00 42.41  ? 313 HOH   A O   1 
HETATM 1033 O O   . HOH   D 4 .   ? 19.400 -38.267 -6.917  1.00 45.19  ? 314 HOH   A O   1 
HETATM 1034 O O   . HOH   D 4 .   ? 31.885 -30.441 7.617   1.00 45.84  ? 315 HOH   A O   1 
HETATM 1035 O O   . HOH   D 4 .   ? 33.212 -30.582 -2.013  1.00 45.97  ? 316 HOH   A O   1 
HETATM 1036 O O   . HOH   D 4 .   ? 29.804 -35.275 6.665   1.00 61.98  ? 317 HOH   A O   1 
HETATM 1037 O O   . HOH   D 4 .   ? 17.705 -28.995 -0.688  1.00 41.90  ? 318 HOH   A O   1 
HETATM 1038 O O   . HOH   D 4 .   ? 17.003 -29.416 5.528   1.00 48.82  ? 319 HOH   A O   1 
HETATM 1039 O O   . HOH   D 4 .   ? 11.251 -31.780 -4.186  1.00 58.59  ? 320 HOH   A O   1 
HETATM 1040 O O   . HOH   D 4 .   ? 17.866 -36.613 -9.217  1.00 48.67  ? 321 HOH   A O   1 
HETATM 1041 O O   . HOH   D 4 .   ? 22.478 -24.725 -8.605  1.00 43.23  ? 322 HOH   A O   1 
HETATM 1042 O O   . HOH   D 4 .   ? 31.673 -24.623 -11.506 1.00 44.76  ? 323 HOH   A O   1 
HETATM 1043 O O   . HOH   D 4 .   ? 14.996 -36.419 -9.296  1.00 49.11  ? 324 HOH   A O   1 
HETATM 1044 O O   . HOH   D 4 .   ? 24.619 -26.765 -6.929  1.00 44.45  ? 325 HOH   A O   1 
HETATM 1045 O O   . HOH   D 4 .   ? 19.074 -21.639 -19.995 1.00 63.01  ? 326 HOH   A O   1 
HETATM 1046 O O   . HOH   D 4 .   ? 38.362 -14.385 4.475   1.00 48.94  ? 327 HOH   A O   1 
HETATM 1047 O O   . HOH   D 4 .   ? 16.769 -31.169 -1.560  1.00 46.31  ? 328 HOH   A O   1 
HETATM 1048 O O   . HOH   D 4 .   ? 36.036 -21.096 -6.073  1.00 49.95  ? 329 HOH   A O   1 
HETATM 1049 O O   . HOH   D 4 .   ? 31.635 -21.725 -10.182 1.00 54.27  ? 330 HOH   A O   1 
HETATM 1050 O O   . HOH   D 4 .   ? 17.935 -17.815 -1.366  1.00 44.59  ? 331 HOH   A O   1 
HETATM 1051 O O   . HOH   D 4 .   ? 34.523 -5.408  -1.344  1.00 60.42  ? 332 HOH   A O   1 
HETATM 1052 O O   . HOH   D 4 .   ? 22.991 -17.230 -10.483 1.00 53.01  ? 333 HOH   A O   1 
HETATM 1053 O O   . HOH   D 4 .   ? 29.377 -6.024  18.622  1.00 73.02  ? 334 HOH   A O   1 
HETATM 1054 O O   . HOH   D 4 .   ? 15.241 -21.727 -6.682  1.00 55.09  ? 335 HOH   A O   1 
HETATM 1055 O O   . HOH   D 4 .   ? 14.791 -21.419 -11.043 1.00 43.25  ? 336 HOH   A O   1 
HETATM 1056 O O   . HOH   D 4 .   ? 33.023 -36.561 4.807   1.00 65.52  ? 337 HOH   A O   1 
HETATM 1057 O O   . HOH   D 4 .   ? 34.146 -22.104 11.727  1.00 57.61  ? 338 HOH   A O   1 
HETATM 1058 O O   . HOH   D 4 .   ? 38.603 -24.695 -1.930  1.00 53.19  ? 339 HOH   A O   1 
HETATM 1059 O O   . HOH   D 4 .   ? 32.560 -5.478  1.219   1.00 56.13  ? 340 HOH   A O   1 
HETATM 1060 O O   . HOH   D 4 .   ? 19.453 -20.479 9.502   1.00 54.09  ? 341 HOH   A O   1 
HETATM 1061 O O   . HOH   D 4 .   ? 17.222 -26.787 9.438   1.00 53.48  ? 342 HOH   A O   1 
HETATM 1062 O O   . HOH   D 4 .   ? 13.143 -31.956 -2.580  1.00 46.20  ? 343 HOH   A O   1 
HETATM 1063 O O   . HOH   D 4 .   ? 29.696 -19.006 19.737  1.00 65.89  ? 344 HOH   A O   1 
HETATM 1064 O O   . HOH   D 4 .   ? 23.095 -40.003 -8.790  0.50 63.41  ? 345 HOH   A O   1 
HETATM 1065 O O   . HOH   D 4 .   ? 12.170 -41.670 -4.677  1.00 57.03  ? 346 HOH   A O   1 
HETATM 1066 O O   . HOH   D 4 .   ? 21.763 -19.521 -16.474 1.00 69.27  ? 347 HOH   A O   1 
HETATM 1067 O O   . HOH   D 4 .   ? 28.460 -37.212 8.103   1.00 71.89  ? 348 HOH   A O   1 
HETATM 1068 O O   . HOH   D 4 .   ? 15.892 -28.256 8.267   1.00 57.11  ? 349 HOH   A O   1 
HETATM 1069 O O   . HOH   D 4 .   ? 22.938 -13.243 -11.635 0.50 61.96  ? 350 HOH   A O   1 
HETATM 1070 O O   . HOH   D 4 .   ? 22.134 -40.589 1.278   1.00 53.64  ? 351 HOH   A O   1 
HETATM 1071 O O   . HOH   D 4 .   ? 37.991 -9.422  3.039   1.00 71.79  ? 352 HOH   A O   1 
HETATM 1072 O O   . HOH   D 4 .   ? 32.480 -38.596 -18.169 1.00 74.96  ? 353 HOH   A O   1 
HETATM 1073 O O   . HOH   D 4 .   ? 22.448 -16.810 -18.385 1.00 66.89  ? 354 HOH   A O   1 
HETATM 1074 O O   . HOH   D 4 .   ? 30.347 -17.521 -11.635 0.50 74.48  ? 355 HOH   A O   1 
# 
loop_
_atom_site_anisotrop.id 
_atom_site_anisotrop.type_symbol 
_atom_site_anisotrop.pdbx_label_atom_id 
_atom_site_anisotrop.pdbx_label_alt_id 
_atom_site_anisotrop.pdbx_label_comp_id 
_atom_site_anisotrop.pdbx_label_asym_id 
_atom_site_anisotrop.pdbx_label_seq_id 
_atom_site_anisotrop.pdbx_PDB_ins_code 
_atom_site_anisotrop.U[1][1] 
_atom_site_anisotrop.U[2][2] 
_atom_site_anisotrop.U[3][3] 
_atom_site_anisotrop.U[1][2] 
_atom_site_anisotrop.U[1][3] 
_atom_site_anisotrop.U[2][3] 
_atom_site_anisotrop.pdbx_auth_seq_id 
_atom_site_anisotrop.pdbx_auth_comp_id 
_atom_site_anisotrop.pdbx_auth_asym_id 
_atom_site_anisotrop.pdbx_auth_atom_id 
1    N N   . SER   A 1   ? 0.7678 0.5702 0.8686 -0.2291 0.0125  -0.1517 1   SER   A N   
2    C CA  . SER   A 1   ? 0.8213 0.5720 0.9188 -0.2182 0.0180  -0.1495 1   SER   A CA  
3    C C   . SER   A 1   ? 0.7585 0.5109 0.8682 -0.1882 0.0226  -0.1447 1   SER   A C   
4    O O   . SER   A 1   ? 0.7930 0.5846 0.9166 -0.1773 0.0210  -0.1355 1   SER   A O   
5    C CB  . SER   A 1   ? 0.7877 0.5286 0.8901 -0.2289 0.0161  -0.1360 1   SER   A CB  
6    O OG  . SER   A 1   ? 0.8525 0.5442 0.9518 -0.2150 0.0181  -0.1308 1   SER   A OG  
7    N N   . PHE   A 2   ? 0.7829 0.4920 0.8875 -0.1749 0.0275  -0.1520 2   PHE   A N   
8    C CA  . PHE   A 2   ? 0.7603 0.4738 0.8780 -0.1481 0.0328  -0.1500 2   PHE   A CA  
9    C C   . PHE   A 2   ? 0.7219 0.4530 0.8589 -0.1369 0.0306  -0.1297 2   PHE   A C   
10   O O   . PHE   A 2   ? 0.6863 0.4504 0.8350 -0.1249 0.0319  -0.1229 2   PHE   A O   
11   C CB  . PHE   A 2   ? 0.7971 0.4631 0.9104 -0.1346 0.0368  -0.1636 2   PHE   A CB  
12   C CG  . PHE   A 2   ? 0.7759 0.4507 0.9062 -0.1076 0.0425  -0.1637 2   PHE   A CG  
13   C CD1 . PHE   A 2   ? 0.7685 0.4685 0.8985 -0.1004 0.0507  -0.1768 2   PHE   A CD1 
14   C CD2 . PHE   A 2   ? 0.7662 0.4264 0.9114 -0.0918 0.0396  -0.1510 2   PHE   A CD2 
15   C CE1 . PHE   A 2   ? 0.7507 0.4638 0.8968 -0.0790 0.0571  -0.1782 2   PHE   A CE1 
16   C CE2 . PHE   A 2   ? 0.7585 0.4317 0.9212 -0.0683 0.0445  -0.1523 2   PHE   A CE2 
17   C CZ  . PHE   A 2   ? 0.7387 0.4398 0.9029 -0.0625 0.0538  -0.1664 2   PHE   A CZ  
18   N N   . ASN   A 3   ? 0.7334 0.4404 0.8708 -0.1427 0.0268  -0.1198 3   ASN   A N   
19   C CA  . ASN   A 3   ? 0.7011 0.4241 0.8544 -0.1338 0.0251  -0.1018 3   ASN   A CA  
20   C C   . ASN   A 3   ? 0.6664 0.4401 0.8297 -0.1425 0.0227  -0.0941 3   ASN   A C   
21   O O   . ASN   A 3   ? 0.6309 0.4293 0.8096 -0.1296 0.0225  -0.0836 3   ASN   A O   
22   C CB  . ASN   A 3   ? 0.7297 0.4129 0.8753 -0.1415 0.0210  -0.0928 3   ASN   A CB  
23   C CG  . ASN   A 3   ? 0.7624 0.3951 0.9038 -0.1240 0.0199  -0.0977 3   ASN   A CG  
24   O OD1 . ASN   A 3   ? 0.7482 0.3879 0.9020 -0.1010 0.0238  -0.1042 3   ASN   A OD1 
25   N ND2 . ASN   A 3   ? 0.8103 0.3921 0.9339 -0.1352 0.0136  -0.0953 3   ASN   A ND2 
26   N N   . LYS   A 4   ? 0.6758 0.4664 0.8315 -0.1634 0.0198  -0.1005 4   LYS   A N   
27   C CA  . LYS   A 4   ? 0.6705 0.5128 0.8393 -0.1686 0.0154  -0.0960 4   LYS   A CA  
28   C C   . LYS   A 4   ? 0.6675 0.5380 0.8437 -0.1513 0.0134  -0.0958 4   LYS   A C   
29   O O   . LYS   A 4   ? 0.6219 0.5266 0.8133 -0.1436 0.0089  -0.0882 4   LYS   A O   
30   C CB  . LYS   A 4   ? 0.6652 0.5231 0.8260 -0.1950 0.0117  -0.1049 4   LYS   A CB  
31   C CG  . LYS   A 4   ? 0.8546 0.6986 1.0093 -0.2183 0.0126  -0.1017 4   LYS   A CG  
32   C CD  . LYS   A 4   ? 0.9136 0.7811 1.0622 -0.2470 0.0093  -0.1120 4   LYS   A CD  
33   C CE  . LYS   A 4   ? 0.8578 0.7147 0.9977 -0.2755 0.0110  -0.1082 4   LYS   A CE  
34   N NZ  . LYS   A 4   ? 0.9538 0.8371 1.0882 -0.3068 0.0084  -0.1197 4   LYS   A NZ  
35   N N   . GLN   A 5   ? 0.6604 0.5156 0.8240 -0.1459 0.0164  -0.1046 5   GLN   A N   
36   C CA  . GLN   A 5   ? 0.6149 0.4940 0.7781 -0.1353 0.0138  -0.1033 5   GLN   A CA  
37   C C   . GLN   A 5   ? 0.6352 0.5152 0.8104 -0.1151 0.0167  -0.0925 5   GLN   A C   
38   O O   . GLN   A 5   ? 0.6206 0.5256 0.8035 -0.1076 0.0105  -0.0837 5   GLN   A O   
39   C CB  . GLN   A 5   ? 0.6419 0.5079 0.7847 -0.1398 0.0177  -0.1172 5   GLN   A CB  
40   C CG  . GLN   A 5   ? 0.8756 0.7474 1.0043 -0.1609 0.0127  -0.1284 5   GLN   A CG  
41   C CD  . GLN   A 5   ? 0.9497 0.8627 1.0870 -0.1676 0.0004  -0.1220 5   GLN   A CD  
42   O OE1 . GLN   A 5   ? 0.9846 0.9083 1.1261 -0.1836 -0.0034 -0.1253 5   GLN   A OE1 
43   N NE2 . GLN   A 5   ? 0.7261 0.6627 0.8660 -0.1558 -0.0069 -0.1138 5   GLN   A NE2 
44   N N   . TRP   A 6   ? 0.5946 0.4471 0.7719 -0.1057 0.0246  -0.0935 6   TRP   A N   
45   C CA  . TRP   A 6   ? 0.6137 0.4706 0.8031 -0.0885 0.0272  -0.0842 6   TRP   A CA  
46   C C   . TRP   A 6   ? 0.5515 0.4178 0.7565 -0.0850 0.0233  -0.0712 6   TRP   A C   
47   O O   . TRP   A 6   ? 0.6381 0.5150 0.8530 -0.0729 0.0231  -0.0626 6   TRP   A O   
48   C CB  . TRP   A 6   ? 0.5839 0.4155 0.7742 -0.0774 0.0358  -0.0913 6   TRP   A CB  
49   C CG  . TRP   A 6   ? 0.6028 0.4018 0.7961 -0.0762 0.0360  -0.0922 6   TRP   A CG  
50   C CD1 . TRP   A 6   ? 0.6398 0.4069 0.8217 -0.0819 0.0372  -0.1048 6   TRP   A CD1 
51   C CD2 . TRP   A 6   ? 0.5925 0.3824 0.7973 -0.0690 0.0333  -0.0797 6   TRP   A CD2 
52   N NE1 . TRP   A 6   ? 0.6559 0.3910 0.8404 -0.0786 0.0339  -0.0993 6   TRP   A NE1 
53   C CE2 . TRP   A 6   ? 0.6269 0.3770 0.8247 -0.0713 0.0316  -0.0834 6   TRP   A CE2 
54   C CE3 . TRP   A 6   ? 0.5617 0.3712 0.7797 -0.0616 0.0314  -0.0659 6   TRP   A CE3 
55   C CZ2 . TRP   A 6   ? 0.6325 0.3620 0.8341 -0.0674 0.0271  -0.0718 6   TRP   A CZ2 
56   C CZ3 . TRP   A 6   ? 0.5640 0.3573 0.7873 -0.0581 0.0287  -0.0563 6   TRP   A CZ3 
57   C CH2 . TRP   A 6   ? 0.5996 0.3534 0.8138 -0.0613 0.0261  -0.0583 6   TRP   A CH2 
58   N N   . TYR   A 7   ? 0.5566 0.4202 0.7623 -0.0977 0.0208  -0.0704 7   TYR   A N   
59   C CA  . TYR   A 7   ? 0.5422 0.4262 0.7613 -0.0985 0.0175  -0.0607 7   TYR   A CA  
60   C C   . TYR   A 7   ? 0.5678 0.4902 0.7954 -0.0954 0.0105  -0.0598 7   TYR   A C   
61   O O   . TYR   A 7   ? 0.5111 0.4500 0.7514 -0.0844 0.0080  -0.0527 7   TYR   A O   
62   C CB  . TYR   A 7   ? 0.5554 0.4318 0.7698 -0.1180 0.0173  -0.0615 7   TYR   A CB  
63   C CG  . TYR   A 7   ? 0.6146 0.4623 0.8270 -0.1177 0.0198  -0.0531 7   TYR   A CG  
64   C CD1 . TYR   A 7   ? 0.5936 0.3969 0.7951 -0.1131 0.0214  -0.0548 7   TYR   A CD1 
65   C CD2 . TYR   A 7   ? 0.5522 0.4176 0.7728 -0.1215 0.0193  -0.0442 7   TYR   A CD2 
66   C CE1 . TYR   A 7   ? 0.6090 0.3828 0.8067 -0.1116 0.0200  -0.0456 7   TYR   A CE1 
67   C CE2 . TYR   A 7   ? 0.6072 0.4450 0.8214 -0.1231 0.0199  -0.0348 7   TYR   A CE2 
68   C CZ  . TYR   A 7   ? 0.5961 0.3864 0.7982 -0.1178 0.0190  -0.0343 7   TYR   A CZ  
69   O OH  . TYR   A 7   ? 0.6160 0.3758 0.8100 -0.1180 0.0160  -0.0235 7   TYR   A OH  
70   N N   A LEU   A 8   ? 0.5260 0.4615 0.7461 -0.1044 0.0055  -0.0675 8   LEU   A N   
71   N N   B LEU   A 8   ? 0.5260 0.4615 0.7461 -0.1044 0.0055  -0.0675 8   LEU   A N   
72   C CA  A LEU   A 8   ? 0.5603 0.5285 0.7869 -0.0989 -0.0050 -0.0667 8   LEU   A CA  
73   C CA  B LEU   A 8   ? 0.5603 0.5287 0.7871 -0.0988 -0.0050 -0.0666 8   LEU   A CA  
74   C C   A LEU   A 8   ? 0.5557 0.5176 0.7781 -0.0828 -0.0070 -0.0599 8   LEU   A C   
75   C C   B LEU   A 8   ? 0.5555 0.5175 0.7779 -0.0828 -0.0071 -0.0599 8   LEU   A C   
76   O O   A LEU   A 8   ? 0.5454 0.5239 0.7775 -0.0716 -0.0151 -0.0541 8   LEU   A O   
77   O O   B LEU   A 8   ? 0.5456 0.5242 0.7774 -0.0716 -0.0152 -0.0541 8   LEU   A O   
78   C CB  A LEU   A 8   ? 0.5344 0.5152 0.7506 -0.1124 -0.0113 -0.0761 8   LEU   A CB  
79   C CB  B LEU   A 8   ? 0.5342 0.5160 0.7511 -0.1122 -0.0116 -0.0760 8   LEU   A CB  
80   C CG  A LEU   A 8   ? 0.6126 0.6175 0.8275 -0.1050 -0.0253 -0.0750 8   LEU   A CG  
81   C CG  B LEU   A 8   ? 0.5592 0.5630 0.7837 -0.1304 -0.0134 -0.0832 8   LEU   A CG  
82   C CD1 A LEU   A 8   ? 0.6041 0.6459 0.8429 -0.0968 -0.0355 -0.0736 8   LEU   A CD1 
83   C CD1 B LEU   A 8   ? 0.5885 0.6033 0.8007 -0.1442 -0.0201 -0.0932 8   LEU   A CD1 
84   C CD2 A LEU   A 8   ? 0.6403 0.6503 0.8385 -0.1197 -0.0306 -0.0842 8   LEU   A CD2 
85   C CD2 B LEU   A 8   ? 0.5156 0.5602 0.7647 -0.1240 -0.0197 -0.0815 8   LEU   A CD2 
86   N N   . LEU   A 9   ? 0.5927 0.5307 0.8000 -0.0824 0.0002  -0.0619 9   LEU   A N   
87   C CA  . LEU   A 9   ? 0.5188 0.4523 0.7186 -0.0725 -0.0002 -0.0559 9   LEU   A CA  
88   C C   . LEU   A 9   ? 0.5609 0.4912 0.7750 -0.0600 0.0030  -0.0471 9   LEU   A C   
89   O O   . LEU   A 9   ? 0.5083 0.4427 0.7215 -0.0521 -0.0026 -0.0395 9   LEU   A O   
90   C CB  . LEU   A 9   ? 0.5337 0.4500 0.7159 -0.0775 0.0092  -0.0638 9   LEU   A CB  
91   C CG  . LEU   A 9   ? 0.7697 0.6872 0.9341 -0.0770 0.0078  -0.0603 9   LEU   A CG  
92   C CD1 . LEU   A 9   ? 0.7761 0.7069 0.9282 -0.0813 -0.0080 -0.0555 9   LEU   A CD1 
93   C CD2 . LEU   A 9   ? 0.6593 0.5669 0.8081 -0.0841 0.0198  -0.0726 9   LEU   A CD2 
94   N N   . ALA   A 10  ? 0.5241 0.4442 0.7488 -0.0591 0.0105  -0.0474 10  ALA   A N   
95   C CA  . ALA   A 10  ? 0.5486 0.4676 0.7860 -0.0486 0.0126  -0.0393 10  ALA   A CA  
96   C C   . ALA   A 10  ? 0.5239 0.4642 0.7735 -0.0446 0.0044  -0.0345 10  ALA   A C   
97   O O   . ALA   A 10  ? 0.5583 0.5009 0.8140 -0.0348 0.0026  -0.0283 10  ALA   A O   
98   C CB  . ALA   A 10  ? 0.4727 0.3741 0.7154 -0.0493 0.0196  -0.0397 10  ALA   A CB  
99   N N   . ASN   A 11  ? 0.4966 0.4545 0.7508 -0.0523 -0.0004 -0.0393 11  ASN   A N   
100  C CA  . ASN   A 11  ? 0.4794 0.4647 0.7490 -0.0468 -0.0082 -0.0391 11  ASN   A CA  
101  C C   . ASN   A 11  ? 0.5054 0.4960 0.7721 -0.0351 -0.0200 -0.0366 11  ASN   A C   
102  O O   . ASN   A 11  ? 0.5156 0.5134 0.7924 -0.0232 -0.0255 -0.0339 11  ASN   A O   
103  C CB  . ASN   A 11  ? 0.4748 0.4847 0.7516 -0.0595 -0.0103 -0.0474 11  ASN   A CB  
104  C CG  . ASN   A 11  ? 0.5862 0.6010 0.8707 -0.0692 -0.0023 -0.0475 11  ASN   A CG  
105  O OD1 . ASN   A 11  ? 0.5514 0.5738 0.8460 -0.0620 -0.0006 -0.0441 11  ASN   A OD1 
106  N ND2 . ASN   A 11  ? 0.6488 0.6567 0.9252 -0.0877 0.0023  -0.0511 11  ASN   A ND2 
107  N N   . GLN   A 12  ? 0.4593 0.4432 0.7096 -0.0391 -0.0252 -0.0375 12  GLN   A N   
108  C CA  . GLN   A 12  ? 0.5150 0.4966 0.7555 -0.0303 -0.0389 -0.0325 12  GLN   A CA  
109  C C   . GLN   A 12  ? 0.5024 0.4612 0.7339 -0.0239 -0.0357 -0.0233 12  GLN   A C   
110  O O   . GLN   A 12  ? 0.5643 0.5187 0.7948 -0.0135 -0.0468 -0.0177 12  GLN   A O   
111  C CB  . GLN   A 12  ? 0.4928 0.4710 0.7122 -0.0398 -0.0447 -0.0345 12  GLN   A CB  
112  C CG  . GLN   A 12  ? 0.7511 0.7559 0.9786 -0.0461 -0.0525 -0.0435 12  GLN   A CG  
113  C CD  . GLN   A 12  ? 0.8790 0.8787 1.0829 -0.0589 -0.0555 -0.0467 12  GLN   A CD  
114  O OE1 . GLN   A 12  ? 0.8652 0.8447 1.0523 -0.0683 -0.0432 -0.0482 12  GLN   A OE1 
115  N NE2 . GLN   A 12  ? 1.0553 1.0756 1.2586 -0.0585 -0.0725 -0.0494 12  GLN   A NE2 
116  N N   . ILE   A 13  ? 0.5654 0.5095 0.7910 -0.0299 -0.0212 -0.0228 13  ILE   A N   
117  C CA  . ILE   A 13  ? 0.4933 0.4217 0.7115 -0.0268 -0.0169 -0.0158 13  ILE   A CA  
118  C C   . ILE   A 13  ? 0.5044 0.4356 0.7400 -0.0166 -0.0173 -0.0123 13  ILE   A C   
119  O O   . ILE   A 13  ? 0.5049 0.4269 0.7353 -0.0112 -0.0235 -0.0059 13  ILE   A O   
120  C CB  . ILE   A 13  ? 0.4694 0.3891 0.6822 -0.0338 -0.0016 -0.0199 13  ILE   A CB  
121  C CG1 . ILE   A 13  ? 0.4923 0.4088 0.6835 -0.0446 -0.0007 -0.0248 13  ILE   A CG1 
122  C CG2 . ILE   A 13  ? 0.4649 0.3775 0.6775 -0.0310 0.0044  -0.0147 13  ILE   A CG2 
123  C CD1 . ILE   A 13  ? 0.4978 0.4094 0.6866 -0.0495 0.0146  -0.0339 13  ILE   A CD1 
124  N N   . ILE   A 14  ? 0.4583 0.4004 0.7116 -0.0159 -0.0113 -0.0162 14  ILE   A N   
125  C CA  . ILE   A 14  ? 0.4223 0.3697 0.6901 -0.0082 -0.0108 -0.0140 14  ILE   A CA  
126  C C   . ILE   A 14  ? 0.5598 0.5191 0.8349 0.0015  -0.0238 -0.0158 14  ILE   A C   
127  O O   . ILE   A 14  ? 0.5247 0.4821 0.8057 0.0098  -0.0264 -0.0142 14  ILE   A O   
128  C CB  . ILE   A 14  ? 0.4861 0.4411 0.7657 -0.0131 -0.0021 -0.0168 14  ILE   A CB  
129  C CG1 . ILE   A 14  ? 0.4882 0.4454 0.7774 -0.0077 0.0005  -0.0134 14  ILE   A CG1 
130  C CG2 . ILE   A 14  ? 0.4666 0.4430 0.7541 -0.0183 -0.0056 -0.0238 14  ILE   A CG2 
131  C CD1 . ILE   A 14  ? 0.4594 0.4004 0.7437 -0.0050 0.0051  -0.0076 14  ILE   A CD1 
132  N N   . GLN   A 15  ? 0.5178 0.4901 0.7934 0.0016  -0.0332 -0.0207 15  GLN   A N   
133  C CA  . GLN   A 15  ? 0.4723 0.4577 0.7578 0.0148  -0.0483 -0.0246 15  GLN   A CA  
134  C C   . GLN   A 15  ? 0.5202 0.4784 0.7876 0.0225  -0.0609 -0.0163 15  GLN   A C   
135  O O   . GLN   A 15  ? 0.4894 0.4443 0.7632 0.0362  -0.0717 -0.0174 15  GLN   A O   
136  C CB  . GLN   A 15  ? 0.5157 0.5270 0.8088 0.0130  -0.0563 -0.0330 15  GLN   A CB  
137  C CG  . GLN   A 15  ? 0.8612 0.8989 1.1751 0.0288  -0.0706 -0.0423 15  GLN   A CG  
138  C CD  . GLN   A 15  ? 0.9877 1.0531 1.3255 0.0300  -0.0608 -0.0519 15  GLN   A CD  
139  O OE1 . GLN   A 15  ? 0.8307 0.9009 1.1805 0.0447  -0.0661 -0.0566 15  GLN   A OE1 
140  N NE2 . GLN   A 15  ? 0.7644 0.8464 1.1068 0.0131  -0.0469 -0.0551 15  GLN   A NE2 
141  N N   . SER   A 16  ? 0.4689 0.4060 0.7117 0.0126  -0.0598 -0.0086 16  SER   A N   
142  C CA  . SER   A 16  ? 0.5677 0.4754 0.7866 0.0141  -0.0710 0.0015  16  SER   A CA  
143  C C   . SER   A 16  ? 0.5607 0.4517 0.7784 0.0147  -0.0642 0.0064  16  SER   A C   
144  O O   . SER   A 16  ? 0.5582 0.4255 0.7630 0.0199  -0.0765 0.0127  16  SER   A O   
145  C CB  . SER   A 16  ? 0.5227 0.4173 0.7134 -0.0012 -0.0688 0.0071  16  SER   A CB  
146  O OG  . SER   A 16  ? 0.6270 0.5208 0.8156 -0.0127 -0.0489 0.0065  16  SER   A OG  
147  N N   . LEU   A 17  ? 0.4864 0.3873 0.7160 0.0092  -0.0465 0.0039  17  LEU   A N   
148  C CA  . LEU   A 17  ? 0.4607 0.3520 0.6928 0.0100  -0.0408 0.0071  17  LEU   A CA  
149  C C   . LEU   A 17  ? 0.5159 0.4126 0.7645 0.0240  -0.0486 0.0022  17  LEU   A C   
150  O O   . LEU   A 17  ? 0.5504 0.4300 0.7936 0.0269  -0.0524 0.0054  17  LEU   A O   
151  C CB  . LEU   A 17  ? 0.4387 0.3413 0.6813 0.0032  -0.0230 0.0052  17  LEU   A CB  
152  C CG  . LEU   A 17  ? 0.4617 0.3629 0.6933 -0.0080 -0.0131 0.0053  17  LEU   A CG  
153  C CD1 . LEU   A 17  ? 0.4260 0.3355 0.6714 -0.0093 0.0008  0.0024  17  LEU   A CD1 
154  C CD2 . LEU   A 17  ? 0.5038 0.3881 0.7105 -0.0173 -0.0154 0.0117  17  LEU   A CD2 
155  N N   . SER   A 18  ? 0.4425 0.3647 0.7109 0.0314  -0.0506 -0.0071 18  SER   A N   
156  C CA  . SER   A 18  ? 0.4387 0.3731 0.7249 0.0451  -0.0568 -0.0159 18  SER   A CA  
157  C C   . SER   A 18  ? 0.5556 0.4716 0.8346 0.0593  -0.0776 -0.0162 18  SER   A C   
158  O O   . SER   A 18  ? 0.6207 0.5303 0.9064 0.0713  -0.0842 -0.0216 18  SER   A O   
159  C CB  . SER   A 18  ? 0.4562 0.4290 0.7653 0.0458  -0.0520 -0.0274 18  SER   A CB  
160  O OG  . SER   A 18  ? 0.4973 0.4785 0.8082 0.0320  -0.0355 -0.0252 18  SER   A OG  
161  N N   . LYS   A 19  ? 0.5376 0.4424 0.8013 0.0586  -0.0894 -0.0109 19  LYS   A N   
162  C CA  . LYS   A 19  ? 0.5241 0.4045 0.7761 0.0723  -0.1131 -0.0085 19  LYS   A CA  
163  C C   . LYS   A 19  ? 0.5558 0.3883 0.7741 0.0641  -0.1188 0.0063  19  LYS   A C   
164  O O   . LYS   A 19  ? 0.6523 0.4532 0.8552 0.0745  -0.1403 0.0105  19  LYS   A O   
165  C CB  . LYS   A 19  ? 0.5510 0.4420 0.7994 0.0742  -0.1261 -0.0087 19  LYS   A CB  
166  C CG  . LYS   A 19  ? 0.6689 0.6101 0.9496 0.0790  -0.1214 -0.0240 19  LYS   A CG  
167  C CD  . LYS   A 19  ? 0.7529 0.7066 1.0271 0.0739  -0.1299 -0.0232 19  LYS   A CD  
168  C CE  . LYS   A 19  ? 0.8496 0.7852 1.1128 0.0902  -0.1592 -0.0200 19  LYS   A CE  
169  N N   . TYR   A 20  ? 0.5661 0.3925 0.7722 0.0453  -0.1011 0.0137  20  TYR   A N   
170  C CA  . TYR   A 20  ? 0.6115 0.3990 0.7859 0.0327  -0.1038 0.0266  20  TYR   A CA  
171  C C   . TYR   A 20  ? 0.6184 0.3834 0.7941 0.0416  -0.1111 0.0249  20  TYR   A C   
172  O O   . TYR   A 20  ? 0.6106 0.3968 0.8132 0.0522  -0.1046 0.0135  20  TYR   A O   
173  C CB  . TYR   A 20  ? 0.6292 0.4267 0.7980 0.0121  -0.0816 0.0305  20  TYR   A CB  
174  C CG  . TYR   A 20  ? 0.6726 0.4396 0.8053 -0.0073 -0.0824 0.0430  20  TYR   A CG  
175  C CD1 . TYR   A 20  ? 0.7734 0.5322 0.8793 -0.0204 -0.0855 0.0501  20  TYR   A CD1 
176  C CD2 . TYR   A 20  ? 0.6828 0.4313 0.8065 -0.0155 -0.0795 0.0471  20  TYR   A CD2 
177  C CE1 . TYR   A 20  ? 0.8175 0.5516 0.8873 -0.0423 -0.0847 0.0612  20  TYR   A CE1 
178  C CE2 . TYR   A 20  ? 0.7832 0.5069 0.8725 -0.0376 -0.0790 0.0581  20  TYR   A CE2 
179  C CZ  . TYR   A 20  ? 0.7954 0.5126 0.8573 -0.0516 -0.0812 0.0653  20  TYR   A CZ  
180  O OH  . TYR   A 20  ? 0.8836 0.5790 0.9081 -0.0776 -0.0794 0.0759  20  TYR   A OH  
181  N N   . GLU   A 21  ? 0.6342 0.3536 0.7771 0.0352  -0.1249 0.0363  21  GLU   A N   
182  C CA  . GLU   A 21  ? 0.6987 0.3867 0.8365 0.0423  -0.1347 0.0350  21  GLU   A CA  
183  C C   . GLU   A 21  ? 0.7469 0.4531 0.8996 0.0333  -0.1141 0.0301  21  GLU   A C   
184  O O   . GLU   A 21  ? 0.6875 0.3981 0.8293 0.0120  -0.0989 0.0372  21  GLU   A O   
185  C CB  . GLU   A 21  ? 0.7250 0.3558 0.8171 0.0290  -0.1513 0.0514  21  GLU   A CB  
186  C CG  . GLU   A 21  ? 0.8981 0.4863 0.9777 0.0321  -0.1626 0.0515  21  GLU   A CG  
187  C CD  . GLU   A 21  ? 1.0593 0.5827 1.0892 0.0204  -0.1848 0.0688  21  GLU   A CD  
188  O OE1 . GLU   A 21  ? 1.3056 0.8052 1.3237 0.0354  -0.2091 0.0728  21  GLU   A OE1 
189  O OE2 . GLU   A 21  ? 1.1502 0.6467 1.1515 -0.0053 -0.1789 0.0789  21  GLU   A OE2 
190  N N   . GLY   A 22  ? 0.6833 0.4033 0.8616 0.0497  -0.1139 0.0164  22  GLY   A N   
191  C CA  . GLY   A 22  ? 0.6020 0.3426 0.7954 0.0429  -0.0964 0.0109  22  GLY   A CA  
192  C C   . GLY   A 22  ? 0.5720 0.3610 0.7910 0.0403  -0.0772 0.0059  22  GLY   A C   
193  O O   . GLY   A 22  ? 0.5208 0.3275 0.7515 0.0350  -0.0642 0.0026  22  GLY   A O   
194  N N   . GLY   A 23  ? 0.5686 0.3770 0.7946 0.0432  -0.0764 0.0057  23  GLY   A N   
195  C CA  . GLY   A 23  ? 0.4809 0.3271 0.7263 0.0387  -0.0597 0.0022  23  GLY   A CA  
196  C C   . GLY   A 23  ? 0.5039 0.3798 0.7753 0.0484  -0.0544 -0.0104 23  GLY   A C   
197  O O   . GLY   A 23  ? 0.4368 0.3377 0.7199 0.0418  -0.0409 -0.0115 23  GLY   A O   
198  N N   . HIS   A 24  ? 0.4905 0.3634 0.7695 0.0634  -0.0654 -0.0207 24  HIS   A N   
199  C CA  . HIS   A 24  ? 0.4517 0.3581 0.7545 0.0709  -0.0593 -0.0354 24  HIS   A CA  
200  C C   . HIS   A 24  ? 0.4944 0.4083 0.7984 0.0603  -0.0457 -0.0344 24  HIS   A C   
201  O O   . HIS   A 24  ? 0.5011 0.4462 0.8200 0.0590  -0.0365 -0.0425 24  HIS   A O   
202  C CB  . HIS   A 24  ? 0.4740 0.3752 0.7853 0.0911  -0.0742 -0.0499 24  HIS   A CB  
203  C CG  . HIS   A 24  ? 0.5315 0.3897 0.8246 0.0936  -0.0840 -0.0469 24  HIS   A CG  
204  N ND1 . HIS   A 24  ? 0.5543 0.3681 0.8241 0.0958  -0.1007 -0.0368 24  HIS   A ND1 
205  C CD2 . HIS   A 24  ? 0.5290 0.3797 0.8205 0.0915  -0.0800 -0.0524 24  HIS   A CD2 
206  C CE1 . HIS   A 24  ? 0.6342 0.4126 0.8885 0.0943  -0.1064 -0.0360 24  HIS   A CE1 
207  N NE2 . HIS   A 24  ? 0.6161 0.4173 0.8845 0.0922  -0.0939 -0.0462 24  HIS   A NE2 
208  N N   . ILE   A 25  ? 0.4488 0.3367 0.7362 0.0509  -0.0448 -0.0245 25  ILE   A N   
209  C CA  . ILE   A 25  ? 0.4757 0.3727 0.7649 0.0415  -0.0342 -0.0235 25  ILE   A CA  
210  C C   . ILE   A 25  ? 0.4741 0.3932 0.7695 0.0315  -0.0216 -0.0168 25  ILE   A C   
211  O O   . ILE   A 25  ? 0.5297 0.4637 0.8301 0.0261  -0.0142 -0.0171 25  ILE   A O   
212  C CB  . ILE   A 25  ? 0.4938 0.3607 0.7650 0.0327  -0.0373 -0.0161 25  ILE   A CB  
213  C CG1 . ILE   A 25  ? 0.4554 0.3133 0.7144 0.0203  -0.0336 -0.0029 25  ILE   A CG1 
214  C CG2 . ILE   A 25  ? 0.5486 0.3822 0.8083 0.0422  -0.0528 -0.0211 25  ILE   A CG2 
215  C CD1 . ILE   A 25  ? 0.4779 0.3158 0.7206 0.0064  -0.0335 0.0037  25  ILE   A CD1 
216  N N   . PHE   A 26  ? 0.4391 0.3582 0.7324 0.0290  -0.0203 -0.0110 26  PHE   A N   
217  C CA  . PHE   A 26  ? 0.3858 0.3200 0.6843 0.0217  -0.0103 -0.0063 26  PHE   A CA  
218  C C   . PHE   A 26  ? 0.4224 0.3774 0.7312 0.0235  -0.0083 -0.0121 26  PHE   A C   
219  O O   . PHE   A 26  ? 0.5062 0.4679 0.8165 0.0168  -0.0017 -0.0082 26  PHE   A O   
220  C CB  . PHE   A 26  ? 0.4300 0.3517 0.7188 0.0156  -0.0083 0.0016  26  PHE   A CB  
221  C CG  . PHE   A 26  ? 0.4009 0.3076 0.6788 0.0091  -0.0084 0.0069  26  PHE   A CG  
222  C CD1 . PHE   A 26  ? 0.3927 0.3078 0.6758 0.0042  -0.0024 0.0087  26  PHE   A CD1 
223  C CD2 . PHE   A 26  ? 0.4881 0.3729 0.7490 0.0060  -0.0153 0.0104  26  PHE   A CD2 
224  C CE1 . PHE   A 26  ? 0.4661 0.3732 0.7408 -0.0044 -0.0018 0.0120  26  PHE   A CE1 
225  C CE2 . PHE   A 26  ? 0.5039 0.3759 0.7520 -0.0047 -0.0144 0.0153  26  PHE   A CE2 
226  C CZ  . PHE   A 26  ? 0.4558 0.3416 0.7124 -0.0103 -0.0069 0.0152  26  PHE   A CZ  
227  N N   . GLU   A 27  ? 0.4170 0.3827 0.7335 0.0322  -0.0144 -0.0225 27  GLU   A N   
228  C CA  . GLU   A 27  ? 0.4314 0.4234 0.7591 0.0315  -0.0122 -0.0298 27  GLU   A CA  
229  C C   . GLU   A 27  ? 0.3771 0.3898 0.7092 0.0217  -0.0022 -0.0315 27  GLU   A C   
230  O O   . GLU   A 27  ? 0.4434 0.4636 0.7743 0.0112  0.0037  -0.0278 27  GLU   A O   
231  C CB  . GLU   A 27  ? 0.3828 0.3873 0.7215 0.0453  -0.0222 -0.0433 27  GLU   A CB  
232  C CG  . GLU   A 27  ? 0.4240 0.4626 0.7769 0.0436  -0.0204 -0.0530 27  GLU   A CG  
233  C CD  . GLU   A 27  ? 0.5393 0.5716 0.8859 0.0372  -0.0216 -0.0456 27  GLU   A CD  
234  O OE1 . GLU   A 27  ? 0.5137 0.5176 0.8468 0.0397  -0.0277 -0.0365 27  GLU   A OE1 
235  O OE2 . GLU   A 27  ? 0.4625 0.5184 0.8155 0.0275  -0.0159 -0.0494 27  GLU   A OE2 
236  N N   . LYS   A 28  ? 0.4257 0.4450 0.7596 0.0233  -0.0009 -0.0369 28  LYS   A N   
237  C CA  . LYS   A 28  ? 0.3970 0.4355 0.7302 0.0121  0.0075  -0.0379 28  LYS   A CA  
238  C C   . LYS   A 28  ? 0.4481 0.4698 0.7707 0.0067  0.0093  -0.0267 28  LYS   A C   
239  O O   . LYS   A 28  ? 0.3856 0.3869 0.7046 0.0120  0.0052  -0.0221 28  LYS   A O   
240  C CB  . LYS   A 28  ? 0.3778 0.4447 0.7212 0.0162  0.0086  -0.0557 28  LYS   A CB  
241  C CG  . LYS   A 28  ? 0.4265 0.5153 0.7861 0.0266  0.0041  -0.0706 28  LYS   A CG  
242  C CD  . LYS   A 28  ? 0.5134 0.6162 0.8750 0.0159  0.0078  -0.0671 28  LYS   A CD  
243  C CE  . LYS   A 28  ? 0.6431 0.7705 1.0002 -0.0045 0.0193  -0.0674 28  LYS   A CE  
244  N N   . LEU   A 29  ? 0.4183 0.4496 0.7348 -0.0055 0.0148  -0.0220 29  LEU   A N   
245  C CA  . LEU   A 29  ? 0.4329 0.4532 0.7405 -0.0099 0.0143  -0.0121 29  LEU   A CA  
246  C C   . LEU   A 29  ? 0.4298 0.4563 0.7374 -0.0066 0.0130  -0.0207 29  LEU   A C   
247  O O   . LEU   A 29  ? 0.4280 0.4732 0.7403 -0.0046 0.0148  -0.0352 29  LEU   A O   
248  C CB  . LEU   A 29  ? 0.3923 0.4170 0.6891 -0.0241 0.0174  -0.0035 29  LEU   A CB  
249  C CG  . LEU   A 29  ? 0.4946 0.5036 0.7876 -0.0281 0.0171  0.0065  29  LEU   A CG  
250  C CD1 . LEU   A 29  ? 0.4327 0.4446 0.7111 -0.0452 0.0192  0.0127  29  LEU   A CD1 
251  C CD2 . LEU   A 29  ? 0.4132 0.3995 0.7067 -0.0206 0.0126  0.0166  29  LEU   A CD2 
252  N N   . VAL   A 30  ? 0.3995 0.4122 0.7029 -0.0061 0.0098  -0.0136 30  VAL   A N   
253  C CA  . VAL   A 30  ? 0.4344 0.4479 0.7357 -0.0045 0.0077  -0.0217 30  VAL   A CA  
254  C C   . VAL   A 30  ? 0.3849 0.4199 0.6795 -0.0138 0.0115  -0.0272 30  VAL   A C   
255  O O   . VAL   A 30  ? 0.4762 0.5159 0.7620 -0.0243 0.0126  -0.0165 30  VAL   A O   
256  C CB  . VAL   A 30  ? 0.4570 0.4553 0.7552 -0.0057 0.0039  -0.0127 30  VAL   A CB  
257  C CG1 . VAL   A 30  ? 0.5016 0.5002 0.7949 -0.0077 0.0016  -0.0209 30  VAL   A CG1 
258  C CG2 . VAL   A 30  ? 0.5105 0.4903 0.8118 0.0002  0.0016  -0.0092 30  VAL   A CG2 
259  N N   . ASP   A 31  ? 0.4201 0.4671 0.7174 -0.0101 0.0128  -0.0446 31  ASP   A N   
260  C CA  . ASP   A 31  ? 0.4596 0.5286 0.7486 -0.0199 0.0172  -0.0533 31  ASP   A CA  
261  C C   . ASP   A 31  ? 0.5045 0.5619 0.7852 -0.0224 0.0127  -0.0513 31  ASP   A C   
262  O O   . ASP   A 31  ? 0.5061 0.5478 0.7901 -0.0137 0.0084  -0.0598 31  ASP   A O   
263  C CB  . ASP   A 31  ? 0.4729 0.5646 0.7715 -0.0133 0.0213  -0.0772 31  ASP   A CB  
264  C CG  . ASP   A 31  ? 0.5199 0.6432 0.8091 -0.0272 0.0292  -0.0882 31  ASP   A CG  
265  O OD1 . ASP   A 31  ? 0.5283 0.6484 0.8019 -0.0379 0.0283  -0.0815 31  ASP   A OD1 
266  O OD2 . ASP   A 31  ? 0.4583 0.6128 0.7554 -0.0285 0.0365  -0.1043 31  ASP   A OD2 
267  N N   . ALA   A 32  ? 0.5290 0.5921 0.7970 -0.0352 0.0121  -0.0395 32  ALA   A N   
268  C CA  . ALA   A 32  ? 0.4999 0.5555 0.7614 -0.0388 0.0065  -0.0357 32  ALA   A CA  
269  C C   . ALA   A 32  ? 0.5446 0.6066 0.8015 -0.0396 0.0077  -0.0554 32  ALA   A C   
270  O O   . ALA   A 32  ? 0.5303 0.5769 0.7868 -0.0375 0.0029  -0.0588 32  ALA   A O   
271  C CB  . ALA   A 32  ? 0.5434 0.6061 0.7921 -0.0508 0.0029  -0.0195 32  ALA   A CB  
272  N N   . LYS   A 33  ? 0.5080 0.5934 0.7610 -0.0438 0.0147  -0.0701 33  LYS   A N   
273  C CA  . LYS   A 33  ? 0.6748 0.7683 0.9240 -0.0434 0.0166  -0.0927 33  LYS   A CA  
274  C C   . LYS   A 33  ? 0.6136 0.6912 0.8777 -0.0246 0.0144  -0.1104 33  LYS   A C   
275  O O   . LYS   A 33  ? 0.6102 0.6688 0.8714 -0.0200 0.0094  -0.1212 33  LYS   A O   
276  C CB  . LYS   A 33  ? 0.6639 0.7934 0.9036 -0.0557 0.0261  -0.1049 33  LYS   A CB  
277  C CG  . LYS   A 33  ? 0.7946 0.9349 1.0112 -0.0766 0.0253  -0.0896 33  LYS   A CG  
278  N N   . LYS   A 34  ? 0.6152 0.6979 0.8937 -0.0139 0.0164  -0.1132 34  LYS   A N   
279  C CA  . LYS   A 34  ? 0.6044 0.6727 0.8967 0.0062  0.0115  -0.1303 34  LYS   A CA  
280  C C   . LYS   A 34  ? 0.5454 0.5694 0.8347 0.0129  0.0006  -0.1188 34  LYS   A C   
281  O O   . LYS   A 34  ? 0.6634 0.6623 0.9515 0.0233  -0.0068 -0.1319 34  LYS   A O   
282  C CB  . LYS   A 34  ? 0.5596 0.6477 0.8685 0.0149  0.0146  -0.1346 34  LYS   A CB  
283  C CG  . LYS   A 34  ? 0.6637 0.7998 0.9782 0.0090  0.0259  -0.1538 34  LYS   A CG  
284  N N   . GLN   A 35  ? 0.5846 0.5975 0.8711 0.0062  -0.0006 -0.0954 35  GLN   A N   
285  C CA  . GLN   A 35  ? 0.6053 0.5820 0.8876 0.0084  -0.0088 -0.0842 35  GLN   A CA  
286  C C   . GLN   A 35  ? 0.6004 0.5649 0.8701 -0.0039 -0.0114 -0.0800 35  GLN   A C   
287  O O   . GLN   A 35  ? 0.5525 0.4922 0.8170 -0.0076 -0.0164 -0.0697 35  GLN   A O   
288  C CB  . GLN   A 35  ? 0.5794 0.5543 0.8658 0.0067  -0.0077 -0.0646 35  GLN   A CB  
289  C CG  . GLN   A 35  ? 0.5796 0.5413 0.8734 0.0199  -0.0120 -0.0659 35  GLN   A CG  
290  C CD  . GLN   A 35  ? 0.6815 0.6714 0.9880 0.0273  -0.0076 -0.0769 35  GLN   A CD  
291  O OE1 . GLN   A 35  ? 0.5255 0.5380 0.8349 0.0194  -0.0004 -0.0697 35  GLN   A OE1 
292  N NE2 . GLN   A 35  ? 0.6985 0.6873 1.0128 0.0422  -0.0128 -0.0954 35  GLN   A NE2 
293  N N   . ASN   A 36  ? 0.5594 0.5434 0.8229 -0.0126 -0.0079 -0.0882 36  ASN   A N   
294  C CA  . ASN   A 36  ? 0.5816 0.5576 0.8331 -0.0251 -0.0113 -0.0876 36  ASN   A CA  
295  C C   . ASN   A 36  ? 0.6546 0.6316 0.9063 -0.0353 -0.0130 -0.0662 36  ASN   A C   
296  O O   . ASN   A 36  ? 0.6437 0.6038 0.8903 -0.0428 -0.0176 -0.0627 36  ASN   A O   
297  C CB  . ASN   A 36  ? 0.6040 0.5441 0.8482 -0.0204 -0.0186 -0.1011 36  ASN   A CB  
298  C CG  . ASN   A 36  ? 0.6759 0.6178 0.9221 -0.0080 -0.0181 -0.1268 36  ASN   A CG  
299  O OD1 . ASN   A 36  ? 0.7521 0.6735 1.0044 0.0089  -0.0233 -0.1361 36  ASN   A OD1 
300  N ND2 . ASN   A 36  ? 0.7778 0.7457 1.0187 -0.0157 -0.0125 -0.1396 36  ASN   A ND2 
301  N N   A CYS   A 37  ? 0.5749 0.5730 0.8328 -0.0361 -0.0095 -0.0531 37  CYS   A N   
302  N N   B CYS   A 37  ? 0.5800 0.5780 0.8380 -0.0361 -0.0095 -0.0531 37  CYS   A N   
303  C CA  A CYS   A 37  ? 0.5585 0.5626 0.8208 -0.0418 -0.0116 -0.0353 37  CYS   A CA  
304  C CA  B CYS   A 37  ? 0.5583 0.5624 0.8206 -0.0418 -0.0116 -0.0353 37  CYS   A CA  
305  C C   A CYS   A 37  ? 0.5167 0.5450 0.7770 -0.0463 -0.0110 -0.0265 37  CYS   A C   
306  C C   B CYS   A 37  ? 0.5157 0.5440 0.7759 -0.0463 -0.0110 -0.0266 37  CYS   A C   
307  O O   A CYS   A 37  ? 0.4938 0.5254 0.7592 -0.0420 -0.0095 -0.0163 37  CYS   A O   
308  O O   B CYS   A 37  ? 0.4823 0.5139 0.7475 -0.0420 -0.0093 -0.0166 37  CYS   A O   
309  C CB  A CYS   A 37  ? 0.5418 0.5327 0.8136 -0.0341 -0.0107 -0.0265 37  CYS   A CB  
310  C CB  B CYS   A 37  ? 0.5420 0.5330 0.8138 -0.0341 -0.0107 -0.0264 37  CYS   A CB  
311  S SG  A CYS   A 37  ? 0.5259 0.5180 0.8036 -0.0223 -0.0060 -0.0288 37  CYS   A SG  
312  S SG  B CYS   A 37  ? 0.5698 0.5264 0.8368 -0.0322 -0.0141 -0.0319 37  CYS   A SG  
313  N N   . PRO   A 38  ? 0.5420 0.5844 0.7914 -0.0565 -0.0136 -0.0297 38  PRO   A N   
314  C CA  . PRO   A 38  ? 0.5680 0.6291 0.8086 -0.0630 -0.0151 -0.0202 38  PRO   A CA  
315  C C   . PRO   A 38  ? 0.5204 0.5846 0.7678 -0.0613 -0.0224 -0.0011 38  PRO   A C   
316  O O   . PRO   A 38  ? 0.5226 0.5931 0.7612 -0.0646 -0.0259 0.0099  38  PRO   A O   
317  C CB  . PRO   A 38  ? 0.6222 0.6962 0.8475 -0.0752 -0.0174 -0.0296 38  PRO   A CB  
318  C CG  . PRO   A 38  ? 0.6525 0.7118 0.8794 -0.0730 -0.0150 -0.0480 38  PRO   A CG  
319  C CD  . PRO   A 38  ? 0.4712 0.5103 0.7124 -0.0642 -0.0162 -0.0419 38  PRO   A CD  
320  N N   . ASP   A 39  ? 0.4423 0.5020 0.7039 -0.0569 -0.0253 0.0023  39  ASP   A N   
321  C CA  . ASP   A 39  ? 0.4829 0.5500 0.7562 -0.0521 -0.0323 0.0161  39  ASP   A CA  
322  C C   . ASP   A 39  ? 0.4836 0.5387 0.7697 -0.0407 -0.0282 0.0210  39  ASP   A C   
323  O O   . ASP   A 39  ? 0.5820 0.6427 0.8820 -0.0342 -0.0326 0.0281  39  ASP   A O   
324  C CB  . ASP   A 39  ? 0.4728 0.5530 0.7559 -0.0566 -0.0374 0.0140  39  ASP   A CB  
325  C CG  . ASP   A 39  ? 0.5296 0.5979 0.8198 -0.0576 -0.0307 0.0059  39  ASP   A CG  
326  O OD1 . ASP   A 39  ? 0.5815 0.6295 0.8649 -0.0553 -0.0242 -0.0008 39  ASP   A OD1 
327  O OD2 . ASP   A 39  ? 0.6728 0.7532 0.9746 -0.0615 -0.0327 0.0060  39  ASP   A OD2 
328  N N   . TYR   A 40  ? 0.5353 0.5766 0.8182 -0.0377 -0.0203 0.0157  40  TYR   A N   
329  C CA  . TYR   A 40  ? 0.4397 0.4696 0.7331 -0.0286 -0.0163 0.0188  40  TYR   A CA  
330  C C   . TYR   A 40  ? 0.4550 0.4841 0.7509 -0.0233 -0.0205 0.0307  40  TYR   A C   
331  O O   . TYR   A 40  ? 0.4380 0.4651 0.7470 -0.0154 -0.0215 0.0344  40  TYR   A O   
332  C CB  . TYR   A 40  ? 0.3910 0.4095 0.6803 -0.0263 -0.0093 0.0104  40  TYR   A CB  
333  C CG  . TYR   A 40  ? 0.4216 0.4287 0.7192 -0.0185 -0.0059 0.0131  40  TYR   A CG  
334  C CD1 . TYR   A 40  ? 0.4206 0.4187 0.7238 -0.0165 -0.0047 0.0109  40  TYR   A CD1 
335  C CD2 . TYR   A 40  ? 0.3794 0.3839 0.6762 -0.0161 -0.0041 0.0178  40  TYR   A CD2 
336  C CE1 . TYR   A 40  ? 0.4570 0.4461 0.7648 -0.0111 -0.0016 0.0128  40  TYR   A CE1 
337  C CE2 . TYR   A 40  ? 0.4065 0.4010 0.7096 -0.0101 -0.0012 0.0190  40  TYR   A CE2 
338  C CZ  . TYR   A 40  ? 0.3781 0.3660 0.6868 -0.0071 0.0001  0.0162  40  TYR   A CZ  
339  O OH  . TYR   A 40  ? 0.3721 0.3512 0.6842 -0.0028 0.0029  0.0169  40  TYR   A OH  
340  N N   . TYR   A 41  ? 0.4081 0.4371 0.6895 -0.0287 -0.0231 0.0361  41  TYR   A N   
341  C CA  . TYR   A 41  ? 0.4628 0.4820 0.7404 -0.0256 -0.0293 0.0488  41  TYR   A CA  
342  C C   . TYR   A 41  ? 0.5151 0.5398 0.7937 -0.0227 -0.0429 0.0588  41  TYR   A C   
343  O O   . TYR   A 41  ? 0.6251 0.6363 0.8990 -0.0183 -0.0518 0.0703  41  TYR   A O   
344  C CB  . TYR   A 41  ? 0.4371 0.4513 0.6945 -0.0364 -0.0261 0.0513  41  TYR   A CB  
345  C CG  . TYR   A 41  ? 0.4279 0.4407 0.6894 -0.0362 -0.0145 0.0407  41  TYR   A CG  
346  C CD1 . TYR   A 41  ? 0.4515 0.4509 0.7220 -0.0288 -0.0119 0.0424  41  TYR   A CD1 
347  C CD2 . TYR   A 41  ? 0.4166 0.4428 0.6741 -0.0421 -0.0071 0.0274  41  TYR   A CD2 
348  C CE1 . TYR   A 41  ? 0.4015 0.4019 0.6762 -0.0282 -0.0035 0.0331  41  TYR   A CE1 
349  C CE2 . TYR   A 41  ? 0.4064 0.4340 0.6707 -0.0389 0.0009  0.0168  41  TYR   A CE2 
350  C CZ  . TYR   A 41  ? 0.4589 0.4741 0.7315 -0.0324 0.0021  0.0206  41  TYR   A CZ  
351  O OH  . TYR   A 41  ? 0.4228 0.4416 0.7025 -0.0291 0.0080  0.0104  41  TYR   A OH  
352  N N   . ASP   A 42  ? 0.5400 0.5830 0.8243 -0.0251 -0.0464 0.0544  42  ASP   A N   
353  C CA  . ASP   A 42  ? 0.5521 0.6070 0.8467 -0.0185 -0.0600 0.0611  42  ASP   A CA  
354  C C   . ASP   A 42  ? 0.4415 0.5045 0.7638 -0.0058 -0.0581 0.0559  42  ASP   A C   
355  O O   . ASP   A 42  ? 0.5410 0.6123 0.8779 0.0058  -0.0691 0.0602  42  ASP   A O   
356  C CB  . ASP   A 42  ? 0.4447 0.5205 0.7337 -0.0289 -0.0648 0.0575  42  ASP   A CB  
357  C CG  . ASP   A 42  ? 0.6054 0.6780 0.8655 -0.0432 -0.0659 0.0603  42  ASP   A CG  
358  O OD1 . ASP   A 42  ? 0.6797 0.7368 0.9230 -0.0451 -0.0696 0.0712  42  ASP   A OD1 
359  O OD2 . ASP   A 42  ? 0.5988 0.6839 0.8511 -0.0542 -0.0626 0.0509  42  ASP   A OD2 
360  N N   . VAL   A 43  ? 0.4428 0.5042 0.7718 -0.0078 -0.0449 0.0460  43  VAL   A N   
361  C CA  . VAL   A 43  ? 0.3931 0.4635 0.7439 -0.0002 -0.0402 0.0399  43  VAL   A CA  
362  C C   . VAL   A 43  ? 0.4820 0.5331 0.8354 0.0091  -0.0350 0.0409  43  VAL   A C   
363  O O   . VAL   A 43  ? 0.4815 0.5388 0.8525 0.0205  -0.0363 0.0388  43  VAL   A O   
364  C CB  . VAL   A 43  ? 0.3831 0.4602 0.7343 -0.0115 -0.0308 0.0300  43  VAL   A CB  
365  C CG1 . VAL   A 43  ? 0.3744 0.4621 0.7433 -0.0085 -0.0242 0.0239  43  VAL   A CG1 
366  C CG2 . VAL   A 43  ? 0.4004 0.4959 0.7489 -0.0221 -0.0365 0.0276  43  VAL   A CG2 
367  N N   . ILE   A 44  ? 0.4122 0.4429 0.7494 0.0045  -0.0290 0.0421  44  ILE   A N   
368  C CA  . ILE   A 44  ? 0.4054 0.4177 0.7424 0.0103  -0.0241 0.0426  44  ILE   A CA  
369  C C   . ILE   A 44  ? 0.4544 0.4493 0.7783 0.0115  -0.0320 0.0530  44  ILE   A C   
370  O O   . ILE   A 44  ? 0.4535 0.4427 0.7591 0.0010  -0.0313 0.0564  44  ILE   A O   
371  C CB  . ILE   A 44  ? 0.4093 0.4130 0.7382 0.0039  -0.0137 0.0364  44  ILE   A CB  
372  C CG1 . ILE   A 44  ? 0.3894 0.4019 0.7250 0.0006  -0.0084 0.0286  44  ILE   A CG1 
373  C CG2 . ILE   A 44  ? 0.3785 0.3657 0.7062 0.0083  -0.0097 0.0368  44  ILE   A CG2 
374  C CD1 . ILE   A 44  ? 0.4287 0.4512 0.7803 0.0062  -0.0061 0.0256  44  ILE   A CD1 
375  N N   . LYS   A 45  ? 0.4207 0.4066 0.7528 0.0235  -0.0398 0.0572  45  LYS   A N   
376  C CA  . LYS   A 45  ? 0.5670 0.5277 0.8830 0.0240  -0.0501 0.0690  45  LYS   A CA  
377  C C   . LYS   A 45  ? 0.4542 0.3899 0.7623 0.0227  -0.0441 0.0688  45  LYS   A C   
378  O O   . LYS   A 45  ? 0.5040 0.4146 0.7926 0.0172  -0.0508 0.0789  45  LYS   A O   
379  C CB  . LYS   A 45  ? 0.5837 0.5423 0.9114 0.0399  -0.0662 0.0740  45  LYS   A CB  
380  C CG  . LYS   A 45  ? 0.6997 0.6906 1.0423 0.0431  -0.0725 0.0714  45  LYS   A CG  
381  C CD  . LYS   A 45  ? 0.7996 0.7861 1.1235 0.0378  -0.0886 0.0850  45  LYS   A CD  
382  C CE  . LYS   A 45  ? 0.6567 0.6426 0.9540 0.0161  -0.0811 0.0882  45  LYS   A CE  
383  N N   . ASN   A 46  ? 0.4340 0.3749 0.7538 0.0254  -0.0324 0.0580  46  ASN   A N   
384  C CA  . ASN   A 46  ? 0.4488 0.3699 0.7619 0.0230  -0.0263 0.0559  46  ASN   A CA  
385  C C   . ASN   A 46  ? 0.4565 0.3903 0.7694 0.0148  -0.0138 0.0476  46  ASN   A C   
386  O O   . ASN   A 46  ? 0.4177 0.3555 0.7405 0.0192  -0.0070 0.0394  46  ASN   A O   
387  C CB  . ASN   A 46  ? 0.5529 0.4641 0.8804 0.0378  -0.0275 0.0500  46  ASN   A CB  
388  C CG  . ASN   A 46  ? 0.6595 0.5501 0.9862 0.0493  -0.0430 0.0575  46  ASN   A CG  
389  O OD1 . ASN   A 46  ? 0.7985 0.7016 1.1450 0.0649  -0.0494 0.0530  46  ASN   A OD1 
390  N ND2 . ASN   A 46  ? 0.8102 0.6689 1.1136 0.0411  -0.0501 0.0686  46  ASN   A ND2 
391  N N   . PRO   A 47  ? 0.4753 0.4160 0.7764 0.0031  -0.0114 0.0489  47  PRO   A N   
392  C CA  . PRO   A 47  ? 0.4441 0.3961 0.7470 -0.0009 -0.0026 0.0398  47  PRO   A CA  
393  C C   . PRO   A 47  ? 0.4291 0.3714 0.7298 -0.0027 0.0022  0.0363  47  PRO   A C   
394  O O   . PRO   A 47  ? 0.4206 0.3478 0.7127 -0.0069 0.0002  0.0411  47  PRO   A O   
395  C CB  . PRO   A 47  ? 0.4563 0.4199 0.7485 -0.0111 -0.0023 0.0398  47  PRO   A CB  
396  C CG  . PRO   A 47  ? 0.4426 0.3951 0.7201 -0.0183 -0.0085 0.0507  47  PRO   A CG  
397  C CD  . PRO   A 47  ? 0.4972 0.4361 0.7815 -0.0069 -0.0171 0.0576  47  PRO   A CD  
398  N N   . MET   A 48  ? 0.4274 0.3764 0.7337 -0.0006 0.0072  0.0283  48  MET   A N   
399  C CA  . MET   A 48  ? 0.4088 0.3519 0.7138 -0.0019 0.0106  0.0241  48  MET   A CA  
400  C C   . MET   A 48  ? 0.4867 0.4401 0.7941 -0.0009 0.0124  0.0166  48  MET   A C   
401  O O   . MET   A 48  ? 0.4197 0.3754 0.7298 0.0029  0.0115  0.0149  48  MET   A O   
402  C CB  . MET   A 48  ? 0.4168 0.3477 0.7260 0.0044  0.0114  0.0233  48  MET   A CB  
403  C CG  . MET   A 48  ? 0.4599 0.3825 0.7650 0.0011  0.0142  0.0191  48  MET   A CG  
404  S SD  . MET   A 48  ? 0.5093 0.4188 0.8027 -0.0098 0.0123  0.0236  48  MET   A SD  
405  C CE  . MET   A 48  ? 0.4652 0.3514 0.7571 -0.0027 0.0057  0.0312  48  MET   A CE  
406  N N   . SER   A 49  ? 0.5223 0.4809 0.8283 -0.0046 0.0136  0.0118  49  SER   A N   
407  C CA  . SER   A 49  ? 0.3994 0.3668 0.7088 -0.0006 0.0120  0.0041  49  SER   A CA  
408  C C   . SER   A 49  ? 0.4052 0.3717 0.7141 -0.0019 0.0119  0.0006  49  SER   A C   
409  O O   . SER   A 49  ? 0.4672 0.4275 0.7726 -0.0081 0.0144  0.0030  49  SER   A O   
410  C CB  . SER   A 49  ? 0.4196 0.4059 0.7321 -0.0020 0.0118  -0.0027 49  SER   A CB  
411  O OG  . SER   A 49  ? 0.3876 0.3871 0.6990 -0.0118 0.0152  -0.0047 49  SER   A OG  
412  N N   . PHE   A 50  ? 0.4027 0.3730 0.7137 0.0039  0.0074  -0.0050 50  PHE   A N   
413  C CA  . PHE   A 50  ? 0.4764 0.4498 0.7869 0.0027  0.0052  -0.0089 50  PHE   A CA  
414  C C   . PHE   A 50  ? 0.3855 0.3786 0.7012 -0.0055 0.0079  -0.0141 50  PHE   A C   
415  O O   . PHE   A 50  ? 0.4048 0.3969 0.7174 -0.0129 0.0092  -0.0148 50  PHE   A O   
416  C CB  . PHE   A 50  ? 0.3929 0.3663 0.7038 0.0120  -0.0039 -0.0131 50  PHE   A CB  
417  C CG  . PHE   A 50  ? 0.4536 0.4044 0.7528 0.0143  -0.0067 -0.0068 50  PHE   A CG  
418  C CD1 . PHE   A 50  ? 0.4956 0.4357 0.7885 0.0083  0.0002  -0.0011 50  PHE   A CD1 
419  C CD2 . PHE   A 50  ? 0.4313 0.3718 0.7252 0.0216  -0.0167 -0.0073 50  PHE   A CD2 
420  C CE1 . PHE   A 50  ? 0.4944 0.4203 0.7763 0.0067  -0.0004 0.0031  50  PHE   A CE1 
421  C CE2 . PHE   A 50  ? 0.4584 0.3766 0.7366 0.0187  -0.0191 -0.0003 50  PHE   A CE2 
422  C CZ  . PHE   A 50  ? 0.4953 0.4096 0.7678 0.0097  -0.0097 0.0045  50  PHE   A CZ  
423  N N   . SER   A 51  ? 0.4110 0.4236 0.7333 -0.0067 0.0094  -0.0190 51  SER   A N   
424  C CA  . SER   A 51  ? 0.4350 0.4716 0.7607 -0.0189 0.0137  -0.0248 51  SER   A CA  
425  C C   . SER   A 51  ? 0.4528 0.4734 0.7654 -0.0341 0.0189  -0.0152 51  SER   A C   
426  O O   . SER   A 51  ? 0.4647 0.4933 0.7740 -0.0481 0.0216  -0.0172 51  SER   A O   
427  C CB  . SER   A 51  ? 0.3647 0.4288 0.6991 -0.0178 0.0156  -0.0342 51  SER   A CB  
428  O OG  . SER   A 51  ? 0.5462 0.5981 0.8727 -0.0190 0.0180  -0.0271 51  SER   A OG  
429  N N   . CYS   A 52  ? 0.4560 0.4534 0.7607 -0.0318 0.0191  -0.0050 52  CYS   A N   
430  C CA  . CYS   A 52  ? 0.4212 0.3958 0.7127 -0.0421 0.0203  0.0047  52  CYS   A CA  
431  C C   . CYS   A 52  ? 0.4074 0.3640 0.6955 -0.0431 0.0197  0.0044  52  CYS   A C   
432  O O   . CYS   A 52  ? 0.4628 0.4078 0.7405 -0.0565 0.0206  0.0066  52  CYS   A O   
433  C CB  . CYS   A 52  ? 0.4169 0.3735 0.7051 -0.0348 0.0179  0.0139  52  CYS   A CB  
434  S SG  . CYS   A 52  ? 0.5945 0.5700 0.8833 -0.0352 0.0181  0.0140  52  CYS   A SG  
435  N N   . VAL   A 53  ? 0.3977 0.3502 0.6915 -0.0311 0.0181  0.0013  53  VAL   A N   
436  C CA  . VAL   A 53  ? 0.4690 0.4070 0.7582 -0.0323 0.0183  -0.0012 53  VAL   A CA  
437  C C   . VAL   A 53  ? 0.4679 0.4222 0.7572 -0.0427 0.0180  -0.0085 53  VAL   A C   
438  O O   . VAL   A 53  ? 0.5180 0.4595 0.7991 -0.0526 0.0190  -0.0099 53  VAL   A O   
439  C CB  . VAL   A 53  ? 0.4520 0.3856 0.7438 -0.0203 0.0173  -0.0028 53  VAL   A CB  
440  C CG1 . VAL   A 53  ? 0.4421 0.3648 0.7274 -0.0230 0.0183  -0.0075 53  VAL   A CG1 
441  C CG2 . VAL   A 53  ? 0.3963 0.3194 0.6902 -0.0124 0.0184  0.0026  53  VAL   A CG2 
442  N N   . LYS   A 54  ? 0.4802 0.4640 0.7800 -0.0403 0.0159  -0.0147 54  LYS   A N   
443  C CA  . LYS   A 54  ? 0.4008 0.4092 0.7056 -0.0491 0.0146  -0.0237 54  LYS   A CA  
444  C C   . LYS   A 54  ? 0.4252 0.4388 0.7234 -0.0699 0.0198  -0.0235 54  LYS   A C   
445  O O   . LYS   A 54  ? 0.4276 0.4460 0.7221 -0.0836 0.0202  -0.0281 54  LYS   A O   
446  C CB  . LYS   A 54  ? 0.3871 0.4282 0.7082 -0.0384 0.0098  -0.0326 54  LYS   A CB  
447  C CG  . LYS   A 54  ? 0.5004 0.5323 0.8228 -0.0213 0.0015  -0.0323 54  LYS   A CG  
448  C CD  . LYS   A 54  ? 0.4232 0.4801 0.7609 -0.0080 -0.0060 -0.0412 54  LYS   A CD  
449  C CE  . LYS   A 54  ? 0.5121 0.5517 0.8451 0.0069  -0.0171 -0.0387 54  LYS   A CE  
450  N NZ  . LYS   A 54  ? 0.4656 0.5222 0.8127 0.0230  -0.0273 -0.0479 54  LYS   A NZ  
451  N N   . THR   A 55  ? 0.4185 0.4303 0.7122 -0.0752 0.0233  -0.0177 55  THR   A N   
452  C CA  . THR   A 55  ? 0.4777 0.4893 0.7585 -0.0988 0.0276  -0.0147 55  THR   A CA  
453  C C   . THR   A 55  ? 0.4671 0.4349 0.7288 -0.1081 0.0262  -0.0065 55  THR   A C   
454  O O   . THR   A 55  ? 0.4895 0.4546 0.7401 -0.1292 0.0278  -0.0079 55  THR   A O   
455  C CB  . THR   A 55  ? 0.4901 0.5054 0.7653 -0.1028 0.0302  -0.0086 55  THR   A CB  
456  O OG1 . THR   A 55  ? 0.4239 0.4803 0.7172 -0.0942 0.0319  -0.0199 55  THR   A OG1 
457  C CG2 . THR   A 55  ? 0.4726 0.4839 0.7277 -0.1314 0.0340  -0.0032 55  THR   A CG2 
458  N N   . LYS   A 56  ? 0.4681 0.4023 0.7264 -0.0926 0.0230  0.0004  56  LYS   A N   
459  C CA  . LYS   A 56  ? 0.5629 0.4540 0.8056 -0.0967 0.0206  0.0051  56  LYS   A CA  
460  C C   . LYS   A 56  ? 0.5162 0.4067 0.7585 -0.1015 0.0211  -0.0045 56  LYS   A C   
461  O O   . LYS   A 56  ? 0.5735 0.4370 0.8001 -0.1161 0.0203  -0.0042 56  LYS   A O   
462  C CB  . LYS   A 56  ? 0.4943 0.3600 0.7398 -0.0760 0.0175  0.0104  56  LYS   A CB  
463  C CG  . LYS   A 56  ? 0.4913 0.3574 0.7362 -0.0718 0.0153  0.0202  56  LYS   A CG  
464  C CD  . LYS   A 56  ? 0.5300 0.3821 0.7830 -0.0507 0.0121  0.0228  56  LYS   A CD  
465  C CE  . LYS   A 56  ? 0.6241 0.4343 0.8660 -0.0477 0.0054  0.0289  56  LYS   A CE  
466  N NZ  . LYS   A 56  ? 0.6368 0.4426 0.8908 -0.0268 0.0017  0.0301  56  LYS   A NZ  
467  N N   . LEU   A 57  ? 0.4829 0.4000 0.7397 -0.0904 0.0212  -0.0128 57  LEU   A N   
468  C CA  . LEU   A 57  ? 0.5144 0.4368 0.7698 -0.0968 0.0204  -0.0221 57  LEU   A CA  
469  C C   . LEU   A 57  ? 0.5058 0.4547 0.7608 -0.1189 0.0214  -0.0276 57  LEU   A C   
470  O O   . LEU   A 57  ? 0.5975 0.5398 0.8438 -0.1332 0.0210  -0.0332 57  LEU   A O   
471  C CB  . LEU   A 57  ? 0.4607 0.4032 0.7277 -0.0803 0.0175  -0.0273 57  LEU   A CB  
472  C CG  . LEU   A 57  ? 0.4749 0.3946 0.7392 -0.0644 0.0180  -0.0250 57  LEU   A CG  
473  C CD1 . LEU   A 57  ? 0.4846 0.4234 0.7559 -0.0521 0.0141  -0.0268 57  LEU   A CD1 
474  C CD2 . LEU   A 57  ? 0.5768 0.4699 0.8284 -0.0697 0.0197  -0.0304 57  LEU   A CD2 
475  N N   . LYS   A 58  ? 0.4800 0.4618 0.7445 -0.1233 0.0234  -0.0279 58  LYS   A N   
476  C CA  . LYS   A 58  ? 0.4881 0.5045 0.7550 -0.1461 0.0261  -0.0355 58  LYS   A CA  
477  C C   . LYS   A 58  ? 0.5257 0.5125 0.7681 -0.1736 0.0293  -0.0283 58  LYS   A C   
478  O O   . LYS   A 58  ? 0.5465 0.5389 0.7812 -0.1965 0.0303  -0.0340 58  LYS   A O   
479  C CB  . LYS   A 58  ? 0.4661 0.5299 0.7517 -0.1418 0.0283  -0.0411 58  LYS   A CB  
480  C CG  . LYS   A 58  ? 0.4742 0.5838 0.7654 -0.1665 0.0332  -0.0515 58  LYS   A CG  
481  C CD  . LYS   A 58  ? 0.4738 0.6292 0.7828 -0.1614 0.0371  -0.0591 58  LYS   A CD  
482  C CE  . LYS   A 58  ? 0.6032 0.8138 0.9209 -0.1870 0.0437  -0.0730 58  LYS   A CE  
483  N NZ  . LYS   A 58  ? 0.7069 0.9660 1.0427 -0.1821 0.0491  -0.0841 58  LYS   A NZ  
484  N N   . LYS   A 59  ? 0.5393 0.4923 0.7672 -0.1729 0.0294  -0.0153 59  LYS   A N   
485  C CA  . LYS   A 59  ? 0.5831 0.5008 0.7827 -0.1990 0.0295  -0.0055 59  LYS   A CA  
486  C C   . LYS   A 59  ? 0.6169 0.4756 0.7975 -0.1993 0.0241  -0.0016 59  LYS   A C   
487  O O   . LYS   A 59  ? 0.6623 0.4855 0.8164 -0.2236 0.0222  0.0050  59  LYS   A O   
488  C CB  . LYS   A 59  ? 0.5895 0.4936 0.7789 -0.1975 0.0288  0.0079  59  LYS   A CB  
489  C CG  . LYS   A 59  ? 0.5595 0.5186 0.7661 -0.1957 0.0346  0.0024  59  LYS   A CG  
490  C CD  . LYS   A 59  ? 0.5733 0.5728 0.7753 -0.2281 0.0421  -0.0046 59  LYS   A CD  
491  C CE  . LYS   A 59  ? 0.5481 0.6012 0.7668 -0.2247 0.0484  -0.0123 59  LYS   A CE  
492  N NZ  . LYS   A 59  ? 0.5647 0.6627 0.7785 -0.2586 0.0576  -0.0207 59  LYS   A NZ  
493  N N   . GLY   A 60  ? 0.6168 0.4626 0.8083 -0.1741 0.0216  -0.0063 60  GLY   A N   
494  C CA  . GLY   A 60  ? 0.6334 0.4265 0.8098 -0.1713 0.0173  -0.0066 60  GLY   A CA  
495  C C   . GLY   A 60  ? 0.6571 0.4013 0.8217 -0.1591 0.0112  0.0054  60  GLY   A C   
496  O O   . GLY   A 60  ? 0.7059 0.3993 0.8465 -0.1708 0.0054  0.0109  60  GLY   A O   
497  N N   . GLN   A 61  ? 0.6267 0.3843 0.8073 -0.1356 0.0110  0.0094  61  GLN   A N   
498  C CA  . GLN   A 61  ? 0.6998 0.4201 0.8745 -0.1206 0.0038  0.0198  61  GLN   A CA  
499  C C   . GLN   A 61  ? 0.6746 0.3747 0.8603 -0.0943 0.0017  0.0118  61  GLN   A C   
500  O O   . GLN   A 61  ? 0.7252 0.3911 0.9075 -0.0802 -0.0061 0.0173  61  GLN   A O   
501  C CB  . GLN   A 61  ? 0.6157 0.3650 0.8010 -0.1126 0.0044  0.0280  61  GLN   A CB  
502  C CG  . GLN   A 61  ? 0.6637 0.4340 0.8370 -0.1381 0.0071  0.0348  61  GLN   A CG  
503  C CD  . GLN   A 61  ? 0.6228 0.4106 0.8006 -0.1307 0.0062  0.0433  61  GLN   A CD  
504  O OE1 . GLN   A 61  ? 0.7663 0.5359 0.9487 -0.1104 0.0000  0.0489  61  GLN   A OE1 
505  N NE2 . GLN   A 61  ? 0.6736 0.5002 0.8513 -0.1473 0.0124  0.0422  61  GLN   A NE2 
506  N N   . TYR   A 62  ? 0.6531 0.3755 0.8515 -0.0877 0.0079  -0.0017 62  TYR   A N   
507  C CA  . TYR   A 62  ? 0.6197 0.3306 0.8279 -0.0661 0.0086  -0.0120 62  TYR   A CA  
508  C C   . TYR   A 62  ? 0.6701 0.3411 0.8630 -0.0724 0.0065  -0.0217 62  TYR   A C   
509  O O   . TYR   A 62  ? 0.6717 0.3461 0.8540 -0.0924 0.0089  -0.0268 62  TYR   A O   
510  C CB  . TYR   A 62  ? 0.5982 0.3520 0.8228 -0.0580 0.0159  -0.0205 62  TYR   A CB  
511  C CG  . TYR   A 62  ? 0.6265 0.4124 0.8661 -0.0481 0.0171  -0.0132 62  TYR   A CG  
512  C CD1 . TYR   A 62  ? 0.6326 0.4091 0.8773 -0.0361 0.0132  -0.0049 62  TYR   A CD1 
513  C CD2 . TYR   A 62  ? 0.5920 0.4156 0.8397 -0.0504 0.0204  -0.0151 62  TYR   A CD2 
514  C CE1 . TYR   A 62  ? 0.6725 0.4773 0.9294 -0.0290 0.0143  0.0006  62  TYR   A CE1 
515  C CE2 . TYR   A 62  ? 0.6441 0.4913 0.9033 -0.0416 0.0206  -0.0096 62  TYR   A CE2 
516  C CZ  . TYR   A 62  ? 0.6566 0.4947 0.9200 -0.0321 0.0184  -0.0021 62  TYR   A CZ  
517  O OH  . TYR   A 62  ? 0.5810 0.4416 0.8544 -0.0252 0.0186  0.0022  62  TYR   A OH  
518  N N   . GLY   A 63  ? 0.6900 0.3247 0.8832 -0.0546 0.0014  -0.0261 63  GLY   A N   
519  C CA  . GLY   A 63  ? 0.7344 0.3276 0.9143 -0.0564 -0.0010 -0.0387 63  GLY   A CA  
520  C C   . GLY   A 63  ? 0.7218 0.3317 0.9155 -0.0405 0.0069  -0.0586 63  GLY   A C   
521  O O   . GLY   A 63  ? 0.7520 0.3443 0.9350 -0.0472 0.0091  -0.0731 63  GLY   A O   
522  N N   . LEU   A 64  ? 0.6850 0.3298 0.9003 -0.0218 0.0116  -0.0601 64  LEU   A N   
523  C CA  . LEU   A 64  ? 0.6736 0.3399 0.9011 -0.0087 0.0204  -0.0784 64  LEU   A CA  
524  C C   . LEU   A 64  ? 0.6249 0.3428 0.8623 -0.0116 0.0283  -0.0745 64  LEU   A C   
525  O O   . LEU   A 64  ? 0.6187 0.3550 0.8629 -0.0118 0.0261  -0.0596 64  LEU   A O   
526  C CB  . LEU   A 64  ? 0.7247 0.3800 0.9690 0.0182  0.0179  -0.0871 64  LEU   A CB  
527  C CG  . LEU   A 64  ? 0.7943 0.3919 1.0301 0.0274  0.0067  -0.0925 64  LEU   A CG  
528  C CD1 . LEU   A 64  ? 0.7914 0.3855 1.0493 0.0575  0.0005  -0.0978 64  LEU   A CD1 
529  C CD2 . LEU   A 64  ? 0.8138 0.3896 1.0372 0.0220  0.0111  -0.1136 64  LEU   A CD2 
530  N N   . PRO   A 65  ? 0.6189 0.3579 0.8543 -0.0147 0.0365  -0.0876 65  PRO   A N   
531  C CA  . PRO   A 65  ? 0.5803 0.3609 0.8203 -0.0180 0.0413  -0.0824 65  PRO   A CA  
532  C C   . PRO   A 65  ? 0.5577 0.3587 0.8153 -0.0029 0.0437  -0.0784 65  PRO   A C   
533  O O   . PRO   A 65  ? 0.5295 0.3565 0.7896 -0.0063 0.0445  -0.0689 65  PRO   A O   
534  C CB  . PRO   A 65  ? 0.5905 0.3814 0.8196 -0.0249 0.0483  -0.0982 65  PRO   A CB  
535  C CG  . PRO   A 65  ? 0.6275 0.3893 0.8552 -0.0171 0.0504  -0.1160 65  PRO   A CG  
536  C CD  . PRO   A 65  ? 0.6488 0.3721 0.8743 -0.0167 0.0408  -0.1076 65  PRO   A CD  
537  N N   . THR   A 66  ? 0.5721 0.3621 0.8424 0.0138  0.0438  -0.0864 66  THR   A N   
538  C CA  . THR   A 66  ? 0.5518 0.3653 0.8410 0.0271  0.0455  -0.0837 66  THR   A CA  
539  C C   . THR   A 66  ? 0.5356 0.3470 0.8293 0.0279  0.0370  -0.0641 66  THR   A C   
540  O O   . THR   A 66  ? 0.5653 0.4019 0.8703 0.0322  0.0383  -0.0583 66  THR   A O   
541  C CB  . THR   A 66  ? 0.5904 0.3974 0.8958 0.0472  0.0463  -0.1002 66  THR   A CB  
542  O OG1 . THR   A 66  ? 0.7528 0.5165 1.0553 0.0550  0.0347  -0.0973 66  THR   A OG1 
543  C CG2 . THR   A 66  ? 0.6206 0.4365 0.9225 0.0460  0.0571  -0.1232 66  THR   A CG2 
544  N N   . GLU   A 67  ? 0.5600 0.3423 0.8428 0.0215  0.0287  -0.0543 67  GLU   A N   
545  C CA  . GLU   A 67  ? 0.6016 0.3839 0.8851 0.0192  0.0216  -0.0367 67  GLU   A CA  
546  C C   . GLU   A 67  ? 0.5731 0.3865 0.8558 0.0085  0.0252  -0.0287 67  GLU   A C   
547  O O   . GLU   A 67  ? 0.6486 0.4750 0.9377 0.0107  0.0226  -0.0186 67  GLU   A O   
548  C CB  . GLU   A 67  ? 0.5704 0.3154 0.8373 0.0093  0.0132  -0.0285 67  GLU   A CB  
549  C CG  . GLU   A 67  ? 0.6126 0.3165 0.8779 0.0223  0.0049  -0.0331 67  GLU   A CG  
550  C CD  . GLU   A 67  ? 0.7740 0.4336 1.0151 0.0067  -0.0026 -0.0271 67  GLU   A CD  
551  O OE1 . GLU   A 67  ? 0.7540 0.4188 0.9825 -0.0135 0.0025  -0.0282 67  GLU   A OE1 
552  O OE2 . GLU   A 67  ? 0.9310 0.5501 1.1646 0.0136  -0.0146 -0.0211 67  GLU   A OE2 
553  N N   . PHE   A 68  ? 0.5335 0.3576 0.8080 -0.0021 0.0297  -0.0339 68  PHE   A N   
554  C CA  . PHE   A 68  ? 0.5040 0.3546 0.7784 -0.0085 0.0305  -0.0280 68  PHE   A CA  
555  C C   . PHE   A 68  ? 0.5348 0.4055 0.8179 -0.0006 0.0342  -0.0286 68  PHE   A C   
556  O O   . PHE   A 68  ? 0.5208 0.4051 0.8081 -0.0001 0.0321  -0.0203 68  PHE   A O   
557  C CB  . PHE   A 68  ? 0.5618 0.4177 0.8250 -0.0201 0.0314  -0.0336 68  PHE   A CB  
558  C CG  . PHE   A 68  ? 0.4573 0.3370 0.7198 -0.0225 0.0298  -0.0299 68  PHE   A CG  
559  C CD1 . PHE   A 68  ? 0.4794 0.3719 0.7465 -0.0244 0.0250  -0.0223 68  PHE   A CD1 
560  C CD2 . PHE   A 68  ? 0.4917 0.3797 0.7472 -0.0230 0.0324  -0.0348 68  PHE   A CD2 
561  C CE1 . PHE   A 68  ? 0.4645 0.3739 0.7314 -0.0234 0.0209  -0.0201 68  PHE   A CE1 
562  C CE2 . PHE   A 68  ? 0.4490 0.3508 0.6999 -0.0249 0.0277  -0.0296 68  PHE   A CE2 
563  C CZ  . PHE   A 68  ? 0.4352 0.3460 0.6929 -0.0233 0.0210  -0.0225 68  PHE   A CZ  
564  N N   . ILE   A 69  ? 0.4652 0.3386 0.7502 0.0041  0.0404  -0.0397 69  ILE   A N   
565  C CA  . ILE   A 69  ? 0.5137 0.4090 0.8045 0.0069  0.0454  -0.0414 69  ILE   A CA  
566  C C   . ILE   A 69  ? 0.5006 0.4024 0.8074 0.0167  0.0429  -0.0356 69  ILE   A C   
567  O O   . ILE   A 69  ? 0.5333 0.4519 0.8430 0.0147  0.0436  -0.0304 69  ILE   A O   
568  C CB  . ILE   A 69  ? 0.4688 0.3708 0.7586 0.0078  0.0544  -0.0576 69  ILE   A CB  
569  C CG1 . ILE   A 69  ? 0.5304 0.4285 0.8004 -0.0047 0.0562  -0.0623 69  ILE   A CG1 
570  C CG2 . ILE   A 69  ? 0.4599 0.3883 0.7562 0.0074  0.0611  -0.0603 69  ILE   A CG2 
571  C CD1 . ILE   A 69  ? 0.5122 0.4189 0.7775 -0.0065 0.0662  -0.0800 69  ILE   A CD1 
572  N N   . LYS   A 70  ? 0.4937 0.3798 0.8090 0.0266  0.0383  -0.0360 70  LYS   A N   
573  C CA  . LYS   A 70  ? 0.5079 0.4008 0.8381 0.0368  0.0337  -0.0307 70  LYS   A CA  
574  C C   . LYS   A 70  ? 0.4827 0.3782 0.8083 0.0304  0.0283  -0.0158 70  LYS   A C   
575  O O   . LYS   A 70  ? 0.4763 0.3887 0.8107 0.0328  0.0273  -0.0118 70  LYS   A O   
576  C CB  . LYS   A 70  ? 0.4736 0.3427 0.8101 0.0499  0.0264  -0.0333 70  LYS   A CB  
577  C CG  . LYS   A 70  ? 0.6591 0.5404 1.0150 0.0661  0.0293  -0.0493 70  LYS   A CG  
578  C CD  . LYS   A 70  ? 0.5970 0.4928 0.9504 0.0612  0.0418  -0.0658 70  LYS   A CD  
579  N N   . ASP   A 71  ? 0.4900 0.3722 0.8028 0.0211  0.0253  -0.0095 71  ASP   A N   
580  C CA  . ASP   A 71  ? 0.5119 0.4011 0.8216 0.0151  0.0216  0.0009  71  ASP   A CA  
581  C C   . ASP   A 71  ? 0.4776 0.3863 0.7873 0.0116  0.0245  0.0007  71  ASP   A C   
582  O O   . ASP   A 71  ? 0.4700 0.3884 0.7828 0.0117  0.0223  0.0059  71  ASP   A O   
583  C CB  . ASP   A 71  ? 0.5149 0.3921 0.8128 0.0045  0.0192  0.0046  71  ASP   A CB  
584  C CG  . ASP   A 71  ? 0.5737 0.4262 0.8657 0.0040  0.0133  0.0103  71  ASP   A CG  
585  O OD1 . ASP   A 71  ? 0.5746 0.4189 0.8735 0.0154  0.0090  0.0118  71  ASP   A OD1 
586  O OD2 . ASP   A 71  ? 0.4977 0.3391 0.7774 -0.0085 0.0119  0.0133  71  ASP   A OD2 
587  N N   . VAL   A 72  ? 0.4273 0.3385 0.7308 0.0078  0.0283  -0.0052 72  VAL   A N   
588  C CA  . VAL   A 72  ? 0.4092 0.3308 0.7077 0.0039  0.0284  -0.0038 72  VAL   A CA  
589  C C   . VAL   A 72  ? 0.4828 0.4152 0.7874 0.0057  0.0316  -0.0043 72  VAL   A C   
590  O O   . VAL   A 72  ? 0.4550 0.3924 0.7584 0.0034  0.0292  0.0004  72  VAL   A O   
591  C CB  . VAL   A 72  ? 0.5297 0.4488 0.8156 -0.0021 0.0295  -0.0083 72  VAL   A CB  
592  C CG1 . VAL   A 72  ? 0.4039 0.3261 0.6799 -0.0063 0.0264  -0.0047 72  VAL   A CG1 
593  C CG2 . VAL   A 72  ? 0.4432 0.3574 0.7255 -0.0053 0.0256  -0.0088 72  VAL   A CG2 
594  N N   . GLN   A 73  ? 0.4598 0.3975 0.7719 0.0096  0.0372  -0.0118 73  GLN   A N   
595  C CA  . GLN   A 73  ? 0.4262 0.3823 0.7479 0.0101  0.0412  -0.0147 73  GLN   A CA  
596  C C   . GLN   A 73  ? 0.4173 0.3788 0.7510 0.0159  0.0357  -0.0085 73  GLN   A C   
597  O O   . GLN   A 73  ? 0.4035 0.3806 0.7418 0.0123  0.0367  -0.0078 73  GLN   A O   
598  C CB  . GLN   A 73  ? 0.4057 0.3723 0.7378 0.0158  0.0484  -0.0279 73  GLN   A CB  
599  C CG  . GLN   A 73  ? 0.4280 0.4234 0.7720 0.0138  0.0547  -0.0346 73  GLN   A CG  
600  C CD  . GLN   A 73  ? 0.5810 0.5831 0.9069 -0.0041 0.0593  -0.0316 73  GLN   A CD  
601  O OE1 . GLN   A 73  ? 0.5587 0.5473 0.8641 -0.0129 0.0599  -0.0297 73  GLN   A OE1 
602  N NE2 . GLN   A 73  ? 0.4320 0.4533 0.7634 -0.0108 0.0610  -0.0305 73  GLN   A NE2 
603  N N   . LEU   A 74  ? 0.4201 0.3686 0.7561 0.0222  0.0294  -0.0036 74  LEU   A N   
604  C CA  . LEU   A 74  ? 0.3900 0.3425 0.7327 0.0256  0.0230  0.0036  74  LEU   A CA  
605  C C   . LEU   A 74  ? 0.4476 0.4044 0.7824 0.0173  0.0215  0.0090  74  LEU   A C   
606  O O   . LEU   A 74  ? 0.4050 0.3728 0.7450 0.0169  0.0189  0.0116  74  LEU   A O   
607  C CB  . LEU   A 74  ? 0.4718 0.4054 0.8112 0.0296  0.0162  0.0093  74  LEU   A CB  
608  C CG  . LEU   A 74  ? 0.4193 0.3535 0.7584 0.0299  0.0084  0.0186  74  LEU   A CG  
609  C CD1 . LEU   A 74  ? 0.4398 0.3905 0.7947 0.0386  0.0047  0.0173  74  LEU   A CD1 
610  C CD2 . LEU   A 74  ? 0.4138 0.3246 0.7425 0.0290  0.0020  0.0255  74  LEU   A CD2 
611  N N   . ILE   A 75  ? 0.4027 0.3509 0.7255 0.0117  0.0221  0.0095  75  ILE   A N   
612  C CA  . ILE   A 75  ? 0.4236 0.3724 0.7395 0.0070  0.0192  0.0120  75  ILE   A CA  
613  C C   . ILE   A 75  ? 0.4383 0.3932 0.7524 0.0017  0.0211  0.0110  75  ILE   A C   
614  O O   . ILE   A 75  ? 0.3727 0.3311 0.6868 -0.0010 0.0183  0.0128  75  ILE   A O   
615  C CB  . ILE   A 75  ? 0.4185 0.3588 0.7249 0.0052  0.0174  0.0107  75  ILE   A CB  
616  C CG1 . ILE   A 75  ? 0.5030 0.4415 0.8109 0.0061  0.0167  0.0108  75  ILE   A CG1 
617  C CG2 . ILE   A 75  ? 0.3697 0.3081 0.6709 0.0044  0.0124  0.0109  75  ILE   A CG2 
618  C CD1 . ILE   A 75  ? 0.3940 0.3315 0.6966 0.0042  0.0148  0.0074  75  ILE   A CD1 
619  N N   . PHE   A 76  ? 0.3761 0.3324 0.6864 -0.0023 0.0262  0.0074  76  PHE   A N   
620  C CA  . PHE   A 76  ? 0.3985 0.3610 0.7027 -0.0126 0.0291  0.0067  76  PHE   A CA  
621  C C   . PHE   A 76  ? 0.4144 0.4001 0.7353 -0.0121 0.0323  0.0035  76  PHE   A C   
622  O O   . PHE   A 76  ? 0.5054 0.4989 0.8234 -0.0223 0.0330  0.0040  76  PHE   A O   
623  C CB  . PHE   A 76  ? 0.4164 0.3766 0.7083 -0.0202 0.0345  0.0034  76  PHE   A CB  
624  C CG  . PHE   A 76  ? 0.5703 0.5103 0.8465 -0.0199 0.0292  0.0064  76  PHE   A CG  
625  C CD1 . PHE   A 76  ? 0.5675 0.4915 0.8349 -0.0185 0.0197  0.0117  76  PHE   A CD1 
626  C CD2 . PHE   A 76  ? 0.5217 0.4608 0.7935 -0.0198 0.0327  0.0020  76  PHE   A CD2 
627  C CE1 . PHE   A 76  ? 0.6049 0.5155 0.8619 -0.0159 0.0130  0.0129  76  PHE   A CE1 
628  C CE2 . PHE   A 76  ? 0.5180 0.4426 0.7768 -0.0197 0.0264  0.0043  76  PHE   A CE2 
629  C CZ  . PHE   A 76  ? 0.5956 0.5076 0.8483 -0.0171 0.0160  0.0099  76  PHE   A CZ  
630  N N   . ASP   A 77  ? 0.4240 0.4200 0.7622 -0.0006 0.0330  0.0000  77  ASP   A N   
631  C CA  . ASP   A 77  ? 0.3886 0.4091 0.7462 0.0036  0.0327  -0.0036 77  ASP   A CA  
632  C C   . ASP   A 77  ? 0.3644 0.3846 0.7231 0.0038  0.0248  0.0034  77  ASP   A C   
633  O O   . ASP   A 77  ? 0.4059 0.4458 0.7723 -0.0013 0.0242  0.0019  77  ASP   A O   
634  C CB  . ASP   A 77  ? 0.4968 0.5223 0.8713 0.0190  0.0322  -0.0095 77  ASP   A CB  
635  C CG  . ASP   A 77  ? 0.5800 0.6166 0.9584 0.0186  0.0419  -0.0216 77  ASP   A CG  
636  O OD1 . ASP   A 77  ? 0.4556 0.5013 0.8234 0.0039  0.0495  -0.0244 77  ASP   A OD1 
637  O OD2 . ASP   A 77  ? 0.5783 0.6125 0.9678 0.0320  0.0415  -0.0287 77  ASP   A OD2 
638  N N   . ASN   A 78  ? 0.4169 0.4181 0.7674 0.0078  0.0192  0.0098  78  ASN   A N   
639  C CA  . ASN   A 78  ? 0.4558 0.4571 0.8030 0.0053  0.0130  0.0148  78  ASN   A CA  
640  C C   . ASN   A 78  ? 0.4774 0.4755 0.8133 -0.0063 0.0139  0.0140  78  ASN   A C   
641  O O   . ASN   A 78  ? 0.4127 0.4185 0.7490 -0.0110 0.0104  0.0145  78  ASN   A O   
642  C CB  . ASN   A 78  ? 0.3734 0.3588 0.7120 0.0086  0.0092  0.0196  78  ASN   A CB  
643  C CG  . ASN   A 78  ? 0.3665 0.3478 0.7108 0.0170  0.0054  0.0230  78  ASN   A CG  
644  O OD1 . ASN   A 78  ? 0.4093 0.4007 0.7662 0.0240  0.0020  0.0226  78  ASN   A OD1 
645  N ND2 . ASN   A 78  ? 0.4237 0.3894 0.7583 0.0163  0.0049  0.0259  78  ASN   A ND2 
646  N N   . CYS   A 79  ? 0.4398 0.4236 0.7634 -0.0114 0.0170  0.0129  79  CYS   A N   
647  C CA  . CYS   A 79  ? 0.3812 0.3522 0.6897 -0.0220 0.0150  0.0133  79  CYS   A CA  
648  C C   . CYS   A 79  ? 0.4828 0.4692 0.7930 -0.0347 0.0183  0.0115  79  CYS   A C   
649  O O   . CYS   A 79  ? 0.3954 0.3811 0.7012 -0.0426 0.0148  0.0115  79  CYS   A O   
650  C CB  . CYS   A 79  ? 0.3971 0.3464 0.6896 -0.0238 0.0146  0.0142  79  CYS   A CB  
651  S SG  . CYS   A 79  ? 0.4769 0.3985 0.7455 -0.0355 0.0080  0.0164  79  CYS   A SG  
652  N N   . SER   A 80  ? 0.3943 0.3975 0.7111 -0.0382 0.0255  0.0080  80  SER   A N   
653  C CA  . SER   A 80  ? 0.4828 0.5091 0.8033 -0.0529 0.0305  0.0041  80  SER   A CA  
654  C C   . SER   A 80  ? 0.4180 0.4734 0.7602 -0.0486 0.0278  0.0012  80  SER   A C   
655  O O   . SER   A 80  ? 0.4540 0.5295 0.7990 -0.0629 0.0297  -0.0021 80  SER   A O   
656  C CB  . SER   A 80  ? 0.4745 0.5195 0.7996 -0.0568 0.0406  -0.0024 80  SER   A CB  
657  O OG  . SER   A 80  ? 0.5820 0.6442 0.9303 -0.0384 0.0420  -0.0079 80  SER   A OG  
658  N N   . LEU   A 81  ? 0.4055 0.4633 0.7612 -0.0312 0.0224  0.0029  81  LEU   A N   
659  C CA  . LEU   A 81  ? 0.4059 0.4887 0.7795 -0.0261 0.0166  0.0019  81  LEU   A CA  
660  C C   . LEU   A 81  ? 0.4180 0.4915 0.7796 -0.0346 0.0102  0.0057  81  LEU   A C   
661  O O   . LEU   A 81  ? 0.4183 0.5129 0.7855 -0.0447 0.0086  0.0028  81  LEU   A O   
662  C CB  . LEU   A 81  ? 0.3608 0.4429 0.7472 -0.0063 0.0108  0.0043  81  LEU   A CB  
663  C CG  . LEU   A 81  ? 0.3608 0.4606 0.7603 0.0010  0.0003  0.0069  81  LEU   A CG  
664  C CD1 . LEU   A 81  ? 0.3608 0.5018 0.7826 -0.0017 0.0008  -0.0016 81  LEU   A CD1 
665  C CD2 . LEU   A 81  ? 0.3654 0.4532 0.7701 0.0189  -0.0071 0.0116  81  LEU   A CD2 
666  N N   . TYR   A 82  ? 0.3822 0.4269 0.7280 -0.0312 0.0069  0.0101  82  TYR   A N   
667  C CA  . TYR   A 82  ? 0.4452 0.4825 0.7806 -0.0371 0.0013  0.0107  82  TYR   A CA  
668  C C   . TYR   A 82  ? 0.3958 0.4171 0.7146 -0.0531 0.0024  0.0078  82  TYR   A C   
669  O O   . TYR   A 82  ? 0.4814 0.5042 0.7947 -0.0621 -0.0016 0.0054  82  TYR   A O   
670  C CB  . TYR   A 82  ? 0.4184 0.4369 0.7449 -0.0281 -0.0015 0.0131  82  TYR   A CB  
671  C CG  . TYR   A 82  ? 0.4540 0.4691 0.7705 -0.0331 -0.0062 0.0106  82  TYR   A CG  
672  C CD1 . TYR   A 82  ? 0.4585 0.4916 0.7793 -0.0327 -0.0115 0.0129  82  TYR   A CD1 
673  C CD2 . TYR   A 82  ? 0.4716 0.4645 0.7733 -0.0377 -0.0065 0.0052  82  TYR   A CD2 
674  C CE1 . TYR   A 82  ? 0.4235 0.4556 0.7329 -0.0390 -0.0149 0.0090  82  TYR   A CE1 
675  C CE2 . TYR   A 82  ? 0.4065 0.3970 0.6995 -0.0415 -0.0100 -0.0004 82  TYR   A CE2 
676  C CZ  . TYR   A 82  ? 0.4947 0.5064 0.7912 -0.0433 -0.0132 0.0011  82  TYR   A CZ  
677  O OH  . TYR   A 82  ? 0.5916 0.6029 0.8774 -0.0487 -0.0158 -0.0061 82  TYR   A OH  
678  N N   . ASN   A 83  ? 0.4047 0.4075 0.7123 -0.0579 0.0064  0.0083  83  ASN   A N   
679  C CA  . ASN   A 83  ? 0.4299 0.4050 0.7150 -0.0726 0.0044  0.0080  83  ASN   A CA  
680  C C   . ASN   A 83  ? 0.4460 0.4348 0.7281 -0.0930 0.0096  0.0073  83  ASN   A C   
681  O O   . ASN   A 83  ? 0.5245 0.5359 0.8175 -0.0936 0.0170  0.0065  83  ASN   A O   
682  C CB  . ASN   A 83  ? 0.4396 0.3805 0.7089 -0.0662 0.0022  0.0105  83  ASN   A CB  
683  C CG  . ASN   A 83  ? 0.4328 0.3649 0.7055 -0.0490 -0.0022 0.0084  83  ASN   A CG  
684  O OD1 . ASN   A 83  ? 0.5019 0.4188 0.7667 -0.0479 -0.0078 0.0040  83  ASN   A OD1 
685  N ND2 . ASN   A 83  ? 0.4260 0.3690 0.7101 -0.0368 0.0009  0.0100  83  ASN   A ND2 
686  N N   . THR   A 84  ? 0.5237 0.4998 0.7903 -0.1110 0.0063  0.0062  84  THR   A N   
687  C CA  . THR   A 84  ? 0.4859 0.4751 0.7457 -0.1364 0.0116  0.0053  84  THR   A CA  
688  C C   . THR   A 84  ? 0.5049 0.4722 0.7444 -0.1458 0.0155  0.0102  84  THR   A C   
689  O O   . THR   A 84  ? 0.6153 0.5414 0.8360 -0.1377 0.0094  0.0152  84  THR   A O   
690  C CB  . THR   A 84  ? 0.5153 0.4847 0.7563 -0.1560 0.0055  0.0038  84  THR   A CB  
691  O OG1 . THR   A 84  ? 0.4997 0.4900 0.7573 -0.1474 0.0014  -0.0011 84  THR   A OG1 
692  C CG2 . THR   A 84  ? 0.5366 0.5251 0.7706 -0.1870 0.0118  0.0024  84  THR   A CG2 
693  N N   . SER   A 85  ? 0.5413 0.5400 0.7848 -0.1635 0.0255  0.0076  85  SER   A N   
694  C CA  . SER   A 85  ? 0.5750 0.5639 0.8013 -0.1730 0.0316  0.0111  85  SER   A CA  
695  C C   . SER   A 85  ? 0.6906 0.6179 0.8743 -0.1856 0.0224  0.0211  85  SER   A C   
696  O O   . SER   A 85  ? 0.8839 0.7890 1.0515 -0.1822 0.0214  0.0266  85  SER   A O   
697  C CB  . SER   A 85  ? 0.5639 0.5992 0.7975 -0.1971 0.0447  0.0042  85  SER   A CB  
698  O OG  . SER   A 85  ? 0.7938 0.8198 1.0050 -0.2113 0.0515  0.0072  85  SER   A OG  
699  N N   . GLY   A 86  ? 0.6165 0.5132 0.7806 -0.1993 0.0139  0.0234  86  GLY   A N   
700  C CA  . GLY   A 86  ? 0.8664 0.6989 0.9883 -0.2109 0.0022  0.0328  86  GLY   A CA  
701  C C   . GLY   A 86  ? 0.7406 0.5282 0.8573 -0.1855 -0.0128 0.0337  86  GLY   A C   
702  O O   . GLY   A 86  ? 0.6944 0.4250 0.7775 -0.1901 -0.0257 0.0407  86  GLY   A O   
703  N N   . SER   A 87  ? 0.6085 0.4202 0.7565 -0.1593 -0.0121 0.0263  87  SER   A N   
704  C CA  . SER   A 87  ? 0.6375 0.4167 0.7842 -0.1368 -0.0241 0.0232  87  SER   A CA  
705  C C   . SER   A 87  ? 0.6367 0.3885 0.7739 -0.1201 -0.0313 0.0280  87  SER   A C   
706  O O   . SER   A 87  ? 0.6644 0.4290 0.8011 -0.1225 -0.0254 0.0333  87  SER   A O   
707  C CB  . SER   A 87  ? 0.5682 0.3858 0.7482 -0.1172 -0.0198 0.0146  87  SER   A CB  
708  O OG  . SER   A 87  ? 0.5411 0.3923 0.7438 -0.1028 -0.0119 0.0155  87  SER   A OG  
709  N N   . LEU   A 88  ? 0.6349 0.3516 0.7661 -0.1023 -0.0445 0.0242  88  LEU   A N   
710  C CA  . LEU   A 88  ? 0.6619 0.3559 0.7877 -0.0837 -0.0540 0.0268  88  LEU   A CA  
711  C C   . LEU   A 88  ? 0.5934 0.3311 0.7479 -0.0678 -0.0440 0.0247  88  LEU   A C   
712  O O   . LEU   A 88  ? 0.6082 0.3426 0.7568 -0.0650 -0.0451 0.0304  88  LEU   A O   
713  C CB  . LEU   A 88  ? 0.6645 0.3242 0.7878 -0.0635 -0.0694 0.0181  88  LEU   A CB  
714  C CG  . LEU   A 88  ? 0.7261 0.3258 0.8161 -0.0740 -0.0849 0.0195  88  LEU   A CG  
715  C CD1 . LEU   A 88  ? 0.7463 0.3162 0.8399 -0.0461 -0.1010 0.0074  88  LEU   A CD1 
716  C CD2 . LEU   A 88  ? 0.7715 0.3317 0.8242 -0.0941 -0.0926 0.0358  88  LEU   A CD2 
717  N N   . VAL   A 89  ? 0.5545 0.3307 0.7372 -0.0587 -0.0352 0.0169  89  VAL   A N   
718  C CA  . VAL   A 89  ? 0.5145 0.3261 0.7212 -0.0453 -0.0269 0.0154  89  VAL   A CA  
719  C C   . VAL   A 89  ? 0.5146 0.3473 0.7227 -0.0572 -0.0165 0.0215  89  VAL   A C   
720  O O   . VAL   A 89  ? 0.4930 0.3324 0.7047 -0.0505 -0.0141 0.0233  89  VAL   A O   
721  C CB  . VAL   A 89  ? 0.5032 0.3458 0.7332 -0.0368 -0.0214 0.0080  89  VAL   A CB  
722  C CG1 . VAL   A 89  ? 0.4512 0.3245 0.7011 -0.0270 -0.0137 0.0086  89  VAL   A CG1 
723  C CG2 . VAL   A 89  ? 0.4956 0.3231 0.7253 -0.0242 -0.0299 -0.0015 89  VAL   A CG2 
724  N N   . ALA   A 90  ? 0.5077 0.3542 0.7142 -0.0754 -0.0098 0.0226  90  ALA   A N   
725  C CA  . ALA   A 90  ? 0.4983 0.3721 0.7100 -0.0860 0.0015  0.0242  90  ALA   A CA  
726  C C   . ALA   A 90  ? 0.5270 0.3767 0.7118 -0.0973 -0.0004 0.0308  90  ALA   A C   
727  O O   . ALA   A 90  ? 0.5394 0.4074 0.7285 -0.0977 0.0075  0.0303  90  ALA   A O   
728  C CB  . ALA   A 90  ? 0.5620 0.4615 0.7797 -0.1038 0.0084  0.0216  90  ALA   A CB  
729  N N   . ILE   A 91  ? 0.5678 0.3735 0.7223 -0.1069 -0.0120 0.0368  91  ILE   A N   
730  C CA  . ILE   A 91  ? 0.6037 0.3801 0.7262 -0.1191 -0.0172 0.0457  91  ILE   A CA  
731  C C   . ILE   A 91  ? 0.6770 0.4508 0.8052 -0.0986 -0.0219 0.0459  91  ILE   A C   
732  O O   . ILE   A 91  ? 0.6400 0.4226 0.7601 -0.1050 -0.0166 0.0484  91  ILE   A O   
733  C CB  . ILE   A 91  ? 0.6578 0.3784 0.7442 -0.1311 -0.0331 0.0533  91  ILE   A CB  
734  C CG1 . ILE   A 91  ? 0.6794 0.4028 0.7526 -0.1608 -0.0267 0.0545  91  ILE   A CG1 
735  C CG2 . ILE   A 91  ? 0.6990 0.3807 0.7504 -0.1369 -0.0445 0.0644  91  ILE   A CG2 
736  C CD1 . ILE   A 91  ? 0.7354 0.3994 0.7738 -0.1728 -0.0430 0.0606  91  ILE   A CD1 
737  N N   . THR   A 92  ? 0.6022 0.3674 0.7445 -0.0751 -0.0312 0.0416  92  THR   A N   
738  C CA  . THR   A 92  ? 0.6083 0.3758 0.7585 -0.0567 -0.0360 0.0402  92  THR   A CA  
739  C C   . THR   A 92  ? 0.5444 0.3541 0.7191 -0.0525 -0.0210 0.0352  92  THR   A C   
740  O O   . THR   A 92  ? 0.5263 0.3394 0.6990 -0.0484 -0.0212 0.0359  92  THR   A O   
741  C CB  . THR   A 92  ? 0.6167 0.3754 0.7809 -0.0340 -0.0470 0.0332  92  THR   A CB  
742  O OG1 . THR   A 92  ? 0.7676 0.5558 0.9579 -0.0285 -0.0374 0.0252  92  THR   A OG1 
743  C CG2 . THR   A 92  ? 0.6064 0.3173 0.7463 -0.0343 -0.0643 0.0360  92  THR   A CG2 
744  N N   . GLY   A 93  ? 0.5729 0.4124 0.7697 -0.0531 -0.0097 0.0301  93  GLY   A N   
745  C CA  . GLY   A 93  ? 0.4949 0.3679 0.7129 -0.0484 0.0023  0.0255  93  GLY   A CA  
746  C C   . GLY   A 93  ? 0.5189 0.4006 0.7256 -0.0627 0.0108  0.0262  93  GLY   A C   
747  O O   . GLY   A 93  ? 0.5835 0.4747 0.7946 -0.0576 0.0150  0.0233  93  GLY   A O   
748  N N   . LYS   A 94  ? 0.5476 0.4268 0.7381 -0.0829 0.0139  0.0289  94  LYS   A N   
749  C CA  . LYS   A 94  ? 0.6155 0.5063 0.7917 -0.1005 0.0234  0.0282  94  LYS   A CA  
750  C C   . LYS   A 94  ? 0.6028 0.4654 0.7505 -0.1038 0.0153  0.0349  94  LYS   A C   
751  O O   . LYS   A 94  ? 0.5762 0.4526 0.7183 -0.1098 0.0232  0.0314  94  LYS   A O   
752  C CB  . LYS   A 94  ? 0.5511 0.4453 0.7122 -0.1260 0.0280  0.0301  94  LYS   A CB  
753  C CG  . LYS   A 94  ? 0.6555 0.5861 0.8462 -0.1251 0.0363  0.0220  94  LYS   A CG  
754  C CD  . LYS   A 94  ? 0.7028 0.6801 0.9216 -0.1191 0.0506  0.0098  94  LYS   A CD  
755  C CE  . LYS   A 94  ? 0.7597 0.7748 1.0079 -0.1177 0.0560  0.0019  94  LYS   A CE  
756  N NZ  . LYS   A 94  ? 0.8421 0.9018 1.1201 -0.1082 0.0674  -0.0119 94  LYS   A NZ  
757  N N   . ASN   A 95  ? 0.6318 0.4555 0.7613 -0.0988 -0.0016 0.0433  95  ASN   A N   
758  C CA  . ASN   A 95  ? 0.6269 0.4226 0.7291 -0.0997 -0.0135 0.0506  95  ASN   A CA  
759  C C   . ASN   A 95  ? 0.5674 0.3809 0.6885 -0.0820 -0.0119 0.0443  95  ASN   A C   
760  O O   . ASN   A 95  ? 0.5827 0.4000 0.6898 -0.0894 -0.0092 0.0444  95  ASN   A O   
761  C CB  . ASN   A 95  ? 0.6316 0.3819 0.7154 -0.0929 -0.0347 0.0589  95  ASN   A CB  
762  C CG  . ASN   A 95  ? 0.7546 0.4746 0.8076 -0.1158 -0.0392 0.0675  95  ASN   A CG  
763  O OD1 . ASN   A 95  ? 0.7299 0.4586 0.7642 -0.1420 -0.0285 0.0705  95  ASN   A OD1 
764  N ND2 . ASN   A 95  ? 0.8451 0.5298 0.8920 -0.1072 -0.0547 0.0701  95  ASN   A ND2 
765  N N   . ILE   A 96  ? 0.5957 0.4207 0.7466 -0.0611 -0.0133 0.0382  96  ILE   A N   
766  C CA  . ILE   A 96  ? 0.5475 0.3875 0.7147 -0.0471 -0.0125 0.0324  96  ILE   A CA  
767  C C   . ILE   A 96  ? 0.5978 0.4663 0.7773 -0.0518 0.0043  0.0248  96  ILE   A C   
768  O O   . ILE   A 96  ? 0.5428 0.4172 0.7213 -0.0500 0.0060  0.0211  96  ILE   A O   
769  C CB  . ILE   A 96  ? 0.5676 0.4143 0.7606 -0.0281 -0.0170 0.0277  96  ILE   A CB  
770  C CG1 . ILE   A 96  ? 0.5717 0.3912 0.7545 -0.0209 -0.0337 0.0313  96  ILE   A CG1 
771  C CG2 . ILE   A 96  ? 0.5818 0.4439 0.7891 -0.0178 -0.0164 0.0220  96  ILE   A CG2 
772  C CD1 . ILE   A 96  ? 0.6019 0.4326 0.8093 -0.0038 -0.0367 0.0237  96  ILE   A CD1 
773  N N   . GLU   A 97  ? 0.5249 0.4119 0.7171 -0.0570 0.0159  0.0210  97  GLU   A N   
774  C CA  . GLU   A 97  ? 0.5042 0.4182 0.7101 -0.0585 0.0304  0.0113  97  GLU   A CA  
775  C C   . GLU   A 97  ? 0.5070 0.4220 0.6890 -0.0747 0.0358  0.0096  97  GLU   A C   
776  O O   . GLU   A 97  ? 0.5850 0.5113 0.7710 -0.0720 0.0424  0.0011  97  GLU   A O   
777  C CB  . GLU   A 97  ? 0.4605 0.3972 0.6853 -0.0603 0.0392  0.0068  97  GLU   A CB  
778  C CG  . GLU   A 97  ? 0.5594 0.5264 0.7986 -0.0617 0.0534  -0.0057 97  GLU   A CG  
779  C CD  . GLU   A 97  ? 0.6546 0.6491 0.9145 -0.0629 0.0600  -0.0110 97  GLU   A CD  
780  O OE1 . GLU   A 97  ? 0.6448 0.6456 0.9282 -0.0476 0.0569  -0.0119 97  GLU   A OE1 
781  O OE2 . GLU   A 97  ? 0.7093 0.7207 0.9608 -0.0809 0.0679  -0.0143 97  GLU   A OE2 
782  N N   . ALA   A 98  ? 0.5264 0.4275 0.6798 -0.0935 0.0328  0.0175  98  ALA   A N   
783  C CA  . ALA   A 98  ? 0.5679 0.4679 0.6913 -0.1130 0.0370  0.0177  98  ALA   A CA  
784  C C   . ALA   A 98  ? 0.5867 0.4675 0.6944 -0.1071 0.0258  0.0215  98  ALA   A C   
785  O O   . ALA   A 98  ? 0.5794 0.4701 0.6754 -0.1151 0.0323  0.0154  98  ALA   A O   
786  C CB  . ALA   A 98  ? 0.5949 0.4767 0.6847 -0.1375 0.0335  0.0285  98  ALA   A CB  
787  N N   . TYR   A 99  ? 0.5669 0.4233 0.6752 -0.0932 0.0086  0.0298  99  TYR   A N   
788  C CA  . TYR   A 99  ? 0.5982 0.4429 0.6976 -0.0854 -0.0036 0.0319  99  TYR   A CA  
789  C C   . TYR   A 99  ? 0.5581 0.4268 0.6838 -0.0736 0.0055  0.0193  99  TYR   A C   
790  O O   . TYR   A 99  ? 0.6826 0.5534 0.7971 -0.0770 0.0046  0.0159  99  TYR   A O   
791  C CB  . TYR   A 99  ? 0.6936 0.5140 0.7944 -0.0704 -0.0236 0.0398  99  TYR   A CB  
792  C CG  . TYR   A 99  ? 0.6453 0.4601 0.7428 -0.0598 -0.0383 0.0403  99  TYR   A CG  
793  C CD1 . TYR   A 99  ? 0.7362 0.5282 0.7984 -0.0691 -0.0530 0.0496  99  TYR   A CD1 
794  C CD2 . TYR   A 99  ? 0.6117 0.4452 0.7402 -0.0423 -0.0383 0.0317  99  TYR   A CD2 
795  C CE1 . TYR   A 99  ? 0.7379 0.5289 0.7992 -0.0585 -0.0683 0.0494  99  TYR   A CE1 
796  C CE2 . TYR   A 99  ? 0.6979 0.5329 0.8262 -0.0341 -0.0515 0.0304  99  TYR   A CE2 
797  C CZ  . TYR   A 99  ? 0.7523 0.5675 0.8488 -0.0409 -0.0670 0.0388  99  TYR   A CZ  
798  O OH  . TYR   A 99  ? 0.7915 0.6121 0.8897 -0.0319 -0.0819 0.0368  99  TYR   A OH  
799  N N   . PHE   A 100 ? 0.5739 0.4580 0.7318 -0.0612 0.0132  0.0129  100 PHE   A N   
800  C CA  . PHE   A 100 ? 0.4909 0.3903 0.6705 -0.0513 0.0202  0.0025  100 PHE   A CA  
801  C C   . PHE   A 100 ? 0.5323 0.4461 0.7077 -0.0603 0.0344  -0.0086 100 PHE   A C   
802  O O   . PHE   A 100 ? 0.5605 0.4763 0.7348 -0.0592 0.0361  -0.0160 100 PHE   A O   
803  C CB  . PHE   A 100 ? 0.4627 0.3707 0.6717 -0.0384 0.0237  0.0004  100 PHE   A CB  
804  C CG  . PHE   A 100 ? 0.5434 0.4611 0.7709 -0.0308 0.0309  -0.0090 100 PHE   A CG  
805  C CD1 . PHE   A 100 ? 0.5277 0.4414 0.7571 -0.0268 0.0256  -0.0107 100 PHE   A CD1 
806  C CD2 . PHE   A 100 ? 0.4596 0.3897 0.7023 -0.0279 0.0417  -0.0166 100 PHE   A CD2 
807  C CE1 . PHE   A 100 ? 0.5472 0.4627 0.7889 -0.0226 0.0311  -0.0183 100 PHE   A CE1 
808  C CE2 . PHE   A 100 ? 0.4379 0.3684 0.6945 -0.0198 0.0455  -0.0246 100 PHE   A CE2 
809  C CZ  . PHE   A 100 ? 0.5640 0.4841 0.8179 -0.0184 0.0402  -0.0247 100 PHE   A CZ  
810  N N   . ASN   A 101 ? 0.5225 0.4490 0.6961 -0.0698 0.0452  -0.0118 101 ASN   A N   
811  C CA  . ASN   A 101 ? 0.5928 0.5392 0.7654 -0.0774 0.0602  -0.0263 101 ASN   A CA  
812  C C   . ASN   A 101 ? 0.6233 0.5634 0.7623 -0.0935 0.0591  -0.0264 101 ASN   A C   
813  O O   . ASN   A 101 ? 0.6592 0.6107 0.7972 -0.0955 0.0683  -0.0404 101 ASN   A O   
814  C CB  . ASN   A 101 ? 0.5151 0.4841 0.6948 -0.0857 0.0720  -0.0313 101 ASN   A CB  
815  C CG  . ASN   A 101 ? 0.5100 0.4919 0.7258 -0.0686 0.0743  -0.0353 101 ASN   A CG  
816  O OD1 . ASN   A 101 ? 0.5232 0.5012 0.7588 -0.0514 0.0722  -0.0398 101 ASN   A OD1 
817  N ND2 . ASN   A 101 ? 0.5338 0.5296 0.7555 -0.0750 0.0775  -0.0332 101 ASN   A ND2 
818  N N   . ASN   A 102 ? 0.5915 0.5112 0.7007 -0.1050 0.0466  -0.0112 102 ASN   A N   
819  C CA  . ASN   A 102 ? 0.6011 0.5117 0.6740 -0.1208 0.0419  -0.0086 102 ASN   A CA  
820  C C   . ASN   A 102 ? 0.7120 0.6144 0.7880 -0.1095 0.0313  -0.0100 102 ASN   A C   
821  O O   . ASN   A 102 ? 0.6775 0.5829 0.7337 -0.1195 0.0329  -0.0160 102 ASN   A O   
822  C CB  . ASN   A 102 ? 0.7082 0.5931 0.7452 -0.1361 0.0282  0.0099  102 ASN   A CB  
823  C CG  . ASN   A 102 ? 0.7731 0.6492 0.7655 -0.1578 0.0243  0.0140  102 ASN   A CG  
824  O OD1 . ASN   A 102 ? 0.8676 0.7610 0.8417 -0.1792 0.0395  0.0067  102 ASN   A OD1 
825  N ND2 . ASN   A 102 ? 0.8627 0.7148 0.8373 -0.1530 0.0033  0.0249  102 ASN   A ND2 
826  N N   . GLN   A 103 ? 0.6191 0.5145 0.7191 -0.0908 0.0213  -0.0058 103 GLN   A N   
827  C CA  . GLN   A 103 ? 0.6937 0.5874 0.7996 -0.0822 0.0122  -0.0086 103 GLN   A CA  
828  C C   . GLN   A 103 ? 0.6021 0.5098 0.7228 -0.0804 0.0260  -0.0254 103 GLN   A C   
829  O O   . GLN   A 103 ? 0.6354 0.5434 0.7474 -0.0839 0.0227  -0.0311 103 GLN   A O   
830  C CB  . GLN   A 103 ? 0.5763 0.4653 0.7054 -0.0650 0.0006  -0.0024 103 GLN   A CB  
831  C CG  . GLN   A 103 ? 0.7116 0.5824 0.8253 -0.0628 -0.0184 0.0114  103 GLN   A CG  
832  C CD  . GLN   A 103 ? 0.7152 0.5769 0.8004 -0.0699 -0.0332 0.0160  103 GLN   A CD  
833  O OE1 . GLN   A 103 ? 0.8663 0.7077 0.9206 -0.0792 -0.0441 0.0275  103 GLN   A OE1 
834  N NE2 . GLN   A 103 ? 0.6724 0.5473 0.7656 -0.0672 -0.0351 0.0078  103 GLN   A NE2 
835  N N   . LEU   A 104 ? 0.5753 0.4931 0.7179 -0.0745 0.0401  -0.0340 104 LEU   A N   
836  C CA  . LEU   A 104 ? 0.5996 0.5245 0.7553 -0.0705 0.0515  -0.0510 104 LEU   A CA  
837  C C   . LEU   A 104 ? 0.6735 0.6056 0.8055 -0.0853 0.0598  -0.0630 104 LEU   A C   
838  O O   . LEU   A 104 ? 0.7479 0.6799 0.8827 -0.0840 0.0652  -0.0776 104 LEU   A O   
839  C CB  . LEU   A 104 ? 0.5814 0.5156 0.7640 -0.0596 0.0622  -0.0578 104 LEU   A CB  
840  C CG  . LEU   A 104 ? 0.5770 0.5051 0.7827 -0.0457 0.0554  -0.0481 104 LEU   A CG  
841  C CD1 . LEU   A 104 ? 0.4837 0.4224 0.7133 -0.0356 0.0642  -0.0550 104 LEU   A CD1 
842  C CD2 . LEU   A 104 ? 0.5174 0.4333 0.7298 -0.0399 0.0480  -0.0474 104 LEU   A CD2 
843  N N   . ILE   A 105 ? 0.6516 0.5880 0.7571 -0.1012 0.0608  -0.0575 105 ILE   A N   
844  C CA  . ILE   A 105 ? 0.6171 0.5632 0.6949 -0.1191 0.0695  -0.0687 105 ILE   A CA  
845  C C   . ILE   A 105 ? 0.7088 0.6416 0.7562 -0.1292 0.0547  -0.0606 105 ILE   A C   
846  O O   . ILE   A 105 ? 0.7558 0.6925 0.7913 -0.1360 0.0585  -0.0736 105 ILE   A O   
847  C CB  . ILE   A 105 ? 0.6485 0.6088 0.7091 -0.1360 0.0795  -0.0672 105 ILE   A CB  
848  C CG1 . ILE   A 105 ? 0.6099 0.5889 0.7048 -0.1248 0.0923  -0.0758 105 ILE   A CG1 
849  C CG2 . ILE   A 105 ? 0.6687 0.6444 0.6999 -0.1569 0.0915  -0.0816 105 ILE   A CG2 
850  C CD1 . ILE   A 105 ? 0.6253 0.6241 0.7069 -0.1436 0.1030  -0.0757 105 ILE   A CD1 
851  N N   . VAL   A 106 ? 0.6598 0.5764 0.6945 -0.1293 0.0363  -0.0402 106 VAL   A N   
852  C CA  . VAL   A 106 ? 0.7259 0.6312 0.7304 -0.1381 0.0190  -0.0314 106 VAL   A CA  
853  C C   . VAL   A 106 ? 0.7328 0.6396 0.7556 -0.1264 0.0109  -0.0374 106 VAL   A C   
854  O O   . VAL   A 106 ? 0.6860 0.5931 0.6878 -0.1354 0.0023  -0.0395 106 VAL   A O   
855  C CB  . VAL   A 106 ? 0.7556 0.6402 0.7418 -0.1389 -0.0008 -0.0088 106 VAL   A CB  
856  C CG1 . VAL   A 106 ? 0.7990 0.6800 0.7613 -0.1565 0.0077  -0.0026 106 VAL   A CG1 
857  C CG2 . VAL   A 106 ? 0.7162 0.5950 0.7368 -0.1163 -0.0100 -0.0023 106 VAL   A CG2 
858  N N   . THR   A 107 ? 0.7579 0.6667 0.8174 -0.1090 0.0130  -0.0401 107 THR   A N   
859  C CA  . THR   A 107 ? 0.6570 0.5689 0.7327 -0.1024 0.0076  -0.0469 107 THR   A CA  
860  C C   . THR   A 107 ? 0.7404 0.6561 0.8190 -0.1074 0.0228  -0.0667 107 THR   A C   
861  O O   . THR   A 107 ? 0.7946 0.7106 0.8766 -0.1089 0.0186  -0.0737 107 THR   A O   
862  C CB  . THR   A 107 ? 0.6437 0.5556 0.7529 -0.0856 0.0041  -0.0418 107 THR   A CB  
863  O OG1 . THR   A 107 ? 0.6105 0.5218 0.7388 -0.0790 0.0193  -0.0471 107 THR   A OG1 
864  C CG2 . THR   A 107 ? 0.5995 0.5067 0.7076 -0.0784 -0.0118 -0.0256 107 THR   A CG2 
865  N N   . GLY   A 108 ? 0.7355 0.6547 0.8132 -0.1099 0.0398  -0.0773 108 GLY   A N   
866  C CA  . GLY   A 108 ? 0.7497 0.6694 0.8339 -0.1100 0.0537  -0.0987 108 GLY   A CA  
867  C C   . GLY   A 108 ? 0.7417 0.6524 0.8587 -0.0936 0.0577  -0.1035 108 GLY   A C   
868  O O   . GLY   A 108 ? 0.6876 0.5899 0.8094 -0.0921 0.0644  -0.1201 108 GLY   A O   
869  N N   . TYR   A 109 ? 0.7081 0.6173 0.8451 -0.0821 0.0529  -0.0895 109 TYR   A N   
870  C CA  . TYR   A 109 ? 0.6118 0.5106 0.7755 -0.0684 0.0550  -0.0916 109 TYR   A CA  
871  C C   . TYR   A 109 ? 0.6405 0.5390 0.8160 -0.0601 0.0686  -0.1074 109 TYR   A C   
872  O O   . TYR   A 109 ? 0.7264 0.6086 0.9163 -0.0506 0.0697  -0.1148 109 TYR   A O   
873  C CB  . TYR   A 109 ? 0.5902 0.4909 0.7696 -0.0594 0.0477  -0.0742 109 TYR   A CB  
874  C CG  . TYR   A 109 ? 0.5466 0.4359 0.7477 -0.0492 0.0466  -0.0726 109 TYR   A CG  
875  C CD1 . TYR   A 109 ? 0.5495 0.4347 0.7673 -0.0375 0.0531  -0.0758 109 TYR   A CD1 
876  C CD2 . TYR   A 109 ? 0.5225 0.4067 0.7260 -0.0525 0.0382  -0.0679 109 TYR   A CD2 
877  C CE1 . TYR   A 109 ? 0.5674 0.4380 0.7997 -0.0296 0.0498  -0.0721 109 TYR   A CE1 
878  C CE2 . TYR   A 109 ? 0.5298 0.4020 0.7473 -0.0475 0.0373  -0.0650 109 TYR   A CE2 
879  C CZ  . TYR   A 109 ? 0.5154 0.3778 0.7451 -0.0362 0.0423  -0.0660 109 TYR   A CZ  
880  O OH  . TYR   A 109 ? 0.5646 0.4111 0.8032 -0.0326 0.0392  -0.0609 109 TYR   A OH  
881  N N   . ASN   A 110 ? 0.7009 0.6172 0.8701 -0.0639 0.0782  -0.1132 110 ASN   A N   
882  C CA  . ASN   A 110 ? 0.7047 0.6294 0.8888 -0.0547 0.0916  -0.1326 110 ASN   A CA  
883  C C   . ASN   A 110 ? 0.6985 0.6123 0.8763 -0.0555 0.0971  -0.1548 110 ASN   A C   
884  O O   . ASN   A 110 ? 0.6890 0.5978 0.8852 -0.0410 0.1034  -0.1720 110 ASN   A O   
885  C CB  . ASN   A 110 ? 0.6154 0.5686 0.7918 -0.0638 0.1023  -0.1362 110 ASN   A CB  
886  C CG  . ASN   A 110 ? 0.6798 0.6416 0.8676 -0.0605 0.0986  -0.1187 110 ASN   A CG  
887  O OD1 . ASN   A 110 ? 0.7079 0.6591 0.9170 -0.0463 0.0916  -0.1096 110 ASN   A OD1 
888  N ND2 . ASN   A 110 ? 0.6372 0.6168 0.8076 -0.0760 0.1033  -0.1140 110 ASN   A ND2 
889  N N   . ASN   A 111 ? 0.6862 0.5952 0.8382 -0.0713 0.0935  -0.1558 111 ASN   A N   
890  C CA  . ASN   A 111 ? 0.7661 0.6620 0.9094 -0.0742 0.0979  -0.1776 111 ASN   A CA  
891  C C   . ASN   A 111 ? 0.7205 0.5841 0.8797 -0.0623 0.0909  -0.1785 111 ASN   A C   
892  O O   . ASN   A 111 ? 0.7040 0.5503 0.8687 -0.0541 0.0960  -0.1991 111 ASN   A O   
893  C CB  . ASN   A 111 ? 0.7845 0.6833 0.8956 -0.0953 0.0931  -0.1761 111 ASN   A CB  
894  C CG  . ASN   A 111 ? 0.8875 0.8122 0.9750 -0.1104 0.0984  -0.1739 111 ASN   A CG  
895  O OD1 . ASN   A 111 ? 0.7711 0.7146 0.8613 -0.1097 0.1128  -0.1873 111 ASN   A OD1 
896  N ND2 . ASN   A 111 ? 0.9471 0.8734 1.0106 -0.1246 0.0861  -0.1570 111 ASN   A ND2 
897  N N   . PHE   A 112 ? 0.7128 0.5666 0.8779 -0.0621 0.0789  -0.1572 112 PHE   A N   
898  C CA  . PHE   A 112 ? 0.6924 0.5155 0.8696 -0.0542 0.0724  -0.1550 112 PHE   A CA  
899  C C   . PHE   A 112 ? 0.7261 0.5404 0.9268 -0.0331 0.0754  -0.1591 112 PHE   A C   
900  O O   . PHE   A 112 ? 0.6867 0.4688 0.8928 -0.0243 0.0721  -0.1665 112 PHE   A O   
901  C CB  . PHE   A 112 ? 0.6388 0.4621 0.8177 -0.0604 0.0608  -0.1326 112 PHE   A CB  
902  C CG  . PHE   A 112 ? 0.6859 0.5160 0.8464 -0.0787 0.0546  -0.1307 112 PHE   A CG  
903  C CD1 . PHE   A 112 ? 0.6858 0.5419 0.8356 -0.0860 0.0511  -0.1227 112 PHE   A CD1 
904  C CD2 . PHE   A 112 ? 0.6934 0.5029 0.8464 -0.0893 0.0504  -0.1367 112 PHE   A CD2 
905  C CE1 . PHE   A 112 ? 0.7420 0.6069 0.8769 -0.1006 0.0426  -0.1212 112 PHE   A CE1 
906  C CE2 . PHE   A 112 ? 0.8326 0.6543 0.9713 -0.1066 0.0439  -0.1363 112 PHE   A CE2 
907  C CZ  . PHE   A 112 ? 0.7638 0.6150 0.8949 -0.1108 0.0394  -0.1288 112 PHE   A CZ  
908  N N   . VAL   A 113 ? 0.6640 0.5050 0.8774 -0.0253 0.0802  -0.1541 113 VAL   A N   
909  C CA  . VAL   A 113 ? 0.6931 0.5337 0.9314 -0.0046 0.0825  -0.1598 113 VAL   A CA  
910  C C   . VAL   A 113 ? 0.8097 0.6498 1.0532 0.0053  0.0920  -0.1890 113 VAL   A C   
911  O O   . VAL   A 113 ? 0.7708 0.5886 1.0306 0.0243  0.0884  -0.1991 113 VAL   A O   
912  C CB  . VAL   A 113 ? 0.6270 0.5008 0.8766 -0.0024 0.0855  -0.1483 113 VAL   A CB  
913  C CG1 . VAL   A 113 ? 0.6664 0.5493 0.9436 0.0184  0.0886  -0.1580 113 VAL   A CG1 
914  C CG2 . VAL   A 113 ? 0.6398 0.5097 0.8876 -0.0077 0.0751  -0.1224 113 VAL   A CG2 
915  N N   . THR   A 114 ? 0.7693 0.6332 0.9979 -0.0070 0.1033  -0.2039 114 THR   A N   
916  C CA  . THR   A 114 ? 0.7839 0.6548 1.0178 0.0015  0.1148  -0.2358 114 THR   A CA  
917  C C   . THR   A 114 ? 0.8724 0.6986 1.1003 0.0070  0.1091  -0.2501 114 THR   A C   
918  O O   . THR   A 114 ? 0.9321 0.7430 1.1775 0.0280  0.1098  -0.2708 114 THR   A O   
919  C CB  . THR   A 114 ? 0.7081 0.6138 0.9203 -0.0186 0.1282  -0.2472 114 THR   A CB  
920  O OG1 . THR   A 114 ? 0.8074 0.7501 1.0235 -0.0246 0.1333  -0.2349 114 THR   A OG1 
921  C CG2 . THR   A 114 ? 0.8440 0.7606 1.0607 -0.0113 0.1419  -0.2841 114 THR   A CG2 
922  N N   . LYS   A 115 ? 0.8710 0.6748 1.0742 -0.0117 0.1022  -0.2401 115 LYS   A N   
923  C CA  . LYS   A 115 ? 0.9106 0.6694 1.1037 -0.0116 0.0967  -0.2532 115 LYS   A CA  
924  C C   . LYS   A 115 ? 0.8810 0.5972 1.0881 0.0044  0.0835  -0.2424 115 LYS   A C   
925  O O   . LYS   A 115 ? 1.0344 0.7082 1.2397 0.0137  0.0788  -0.2580 115 LYS   A O   
926  C CB  . LYS   A 115 ? 0.8521 0.6040 1.0163 -0.0384 0.0922  -0.2447 115 LYS   A CB  
927  C CG  . LYS   A 115 ? 0.9867 0.7767 1.1312 -0.0563 0.1016  -0.2514 115 LYS   A CG  
928  C CD  . LYS   A 115 ? 0.9855 0.7606 1.1024 -0.0763 0.1001  -0.2635 115 LYS   A CD  
929  C CE  . LYS   A 115 ? 1.0169 0.7691 1.1320 -0.0679 0.1079  -0.2974 115 LYS   A CE  
930  N NZ  . LYS   A 115 ? 0.9614 0.7021 1.0468 -0.0898 0.1077  -0.3117 115 LYS   A NZ  
931  N N   . ALA   A 116 ? 0.8273 0.5511 1.0457 0.0073  0.0764  -0.2161 116 ALA   A N   
932  C CA  . ALA   A 116 ? 0.8522 0.5365 1.0791 0.0193  0.0630  -0.2031 116 ALA   A CA  
933  C C   . ALA   A 116 ? 1.0582 0.7355 1.3104 0.0495  0.0615  -0.2173 116 ALA   A C   
934  O O   . ALA   A 116 ? 1.1453 0.7745 1.3986 0.0622  0.0491  -0.2171 116 ALA   A O   
935  C CB  . ALA   A 116 ? 0.7256 0.4244 0.9556 0.0118  0.0567  -0.1727 116 ALA   A CB  
936  N N   . ASN   A 117 ? 1.0346 0.7590 1.3066 0.0606  0.0728  -0.2294 117 ASN   A N   
937  C CA  . ASN   A 117 ? 1.0098 0.7374 1.3111 0.0908  0.0713  -0.2458 117 ASN   A CA  
938  C C   . ASN   A 117 ? 1.1110 0.8100 1.4132 0.1056  0.0723  -0.2785 117 ASN   A C   
939  O O   . ASN   A 117 ? 1.1915 0.8629 1.5122 0.1330  0.0617  -0.2885 117 ASN   A O   
940  C CB  . ASN   A 117 ? 0.9839 0.7763 1.3062 0.0947  0.0848  -0.2523 117 ASN   A CB  
941  C CG  . ASN   A 117 ? 1.0663 0.8821 1.3883 0.0825  0.0824  -0.2217 117 ASN   A CG  
942  O OD1 . ASN   A 117 ? 0.9746 0.8327 1.2924 0.0677  0.0936  -0.2190 117 ASN   A OD1 
943  N ND2 . ASN   A 117 ? 1.0554 0.8414 1.3790 0.0875  0.0673  -0.1989 117 ASN   A ND2 
944  N N   . THR   A 118 ? 1.0963 0.7998 1.3783 0.0886  0.0835  -0.2960 118 THR   A N   
945  C CA  . THR   A 118 ? 1.2020 0.8753 1.4819 0.1010  0.0849  -0.3294 118 THR   A CA  
946  C C   . THR   A 118 ? 1.2622 0.8584 1.5241 0.1013  0.0666  -0.3212 118 THR   A C   
947  O O   . THR   A 118 ? 1.3000 0.8544 1.5685 0.1241  0.0585  -0.3418 118 THR   A O   
948  C CB  . THR   A 118 ? 1.2318 0.9321 1.4905 0.0790  0.1018  -0.3497 118 THR   A CB  
949  O OG1 . THR   A 118 ? 1.1933 0.9623 1.4627 0.0737  0.1181  -0.3536 118 THR   A OG1 
950  C CG2 . THR   A 118 ? 1.3407 1.0155 1.5995 0.0934  0.1054  -0.3895 118 THR   A CG2 
951  N N   . ILE   A 119 ? 1.2806 0.8573 1.5185 0.0755  0.0594  -0.2915 119 ILE   A N   
952  C CA  . ILE   A 119 ? 1.2346 0.7403 1.4519 0.0694  0.0425  -0.2803 119 ILE   A CA  
953  C C   . ILE   A 119 ? 1.3312 0.7997 1.5649 0.0967  0.0254  -0.2711 119 ILE   A C   
954  O O   . ILE   A 119 ? 1.4680 0.8812 1.6808 0.1054  0.0116  -0.2712 119 ILE   A O   
955  C CB  . ILE   A 119 ? 1.1734 0.6806 1.3670 0.0357  0.0398  -0.2505 119 ILE   A CB  
956  C CG1 . ILE   A 119 ? 1.0288 0.5642 1.2035 0.0100  0.0522  -0.2612 119 ILE   A CG1 
957  C CG2 . ILE   A 119 ? 1.1286 0.5670 1.3007 0.0258  0.0228  -0.2355 119 ILE   A CG2 
958  C CD1 . ILE   A 119 ? 0.9565 0.5129 1.1170 -0.0186 0.0505  -0.2345 119 ILE   A CD1 
959  N N   . ASN   A 120 ? 1.3903 0.8975 1.6471 0.1080  0.0249  -0.2547 120 ASN   A N   
960  C CA  . ASN   A 120 ? 1.3952 0.8799 1.6610 0.1319  0.0076  -0.2398 120 ASN   A CA  
961  C C   . ASN   A 120 ? 1.3364 0.8585 1.6327 0.1654  0.0110  -0.2615 120 ASN   A C   
962  O O   . ASN   A 120 ? 1.3013 0.8116 1.6048 0.1885  -0.0033 -0.2527 120 ASN   A O   
963  C CB  . ASN   A 120 ? 1.4294 0.9291 1.7022 0.1218  0.0028  -0.2083 120 ASN   A CB  
964  C CG  . ASN   A 120 ? 1.3536 0.8366 1.5941 0.0857  0.0022  -0.1852 120 ASN   A CG  
965  O OD1 . ASN   A 120 ? 1.2127 0.7424 1.4513 0.0662  0.0136  -0.1753 120 ASN   A OD1 
966  N ND2 . ASN   A 120 ? 1.4422 0.8588 1.6565 0.0764  -0.0119 -0.1770 120 ASN   A ND2 
967  S S   . SO4   B .   ? 0.8306 1.0225 1.1766 -0.0352 0.0407  -0.0864 201 SO4   A S   
968  O O1  . SO4   B .   ? 0.6714 0.8817 1.0049 -0.0500 0.0487  -0.0905 201 SO4   A O1  
969  O O2  . SO4   B .   ? 0.5637 0.7275 0.8936 -0.0489 0.0402  -0.0646 201 SO4   A O2  
970  O O3  . SO4   B .   ? 0.5861 0.7469 0.9370 -0.0124 0.0305  -0.0849 201 SO4   A O3  
971  O O4  . SO4   B .   ? 0.9652 1.1987 1.3339 -0.0305 0.0423  -0.1070 201 SO4   A O4  
972  C C01 A A1IUY C .   ? 0.5557 0.4666 0.8310 0.0000  -0.0171 -0.0261 202 A1IUY A C01 
973  C C01 B A1IUY C .   ? 0.5555 0.4648 0.8298 -0.0013 -0.0171 -0.0247 202 A1IUY A C01 
974  C C02 A A1IUY C .   ? 0.5438 0.4813 0.8235 -0.0074 -0.0117 -0.0254 202 A1IUY A C02 
975  C C02 B A1IUY C .   ? 0.5442 0.4821 0.8245 -0.0056 -0.0118 -0.0270 202 A1IUY A C02 
976  C C03 A A1IUY C .   ? 0.4924 0.4346 0.7714 -0.0189 -0.0106 -0.0152 202 A1IUY A C03 
977  C C03 B A1IUY C .   ? 0.5096 0.4640 0.7946 -0.0138 -0.0079 -0.0145 202 A1IUY A C03 
978  C C04 A A1IUY C .   ? 0.4862 0.4178 0.7650 -0.0207 -0.0096 -0.0066 202 A1IUY A C04 
979  C C04 B A1IUY C .   ? 0.4869 0.4307 0.7715 -0.0177 -0.0077 -0.0060 202 A1IUY A C04 
980  C C05 A A1IUY C .   ? 0.4802 0.4150 0.7657 -0.0120 -0.0067 -0.0027 202 A1IUY A C05 
981  C C05 B A1IUY C .   ? 0.4789 0.4147 0.7654 -0.0110 -0.0063 -0.0023 202 A1IUY A C05 
982  C C07 A A1IUY C .   ? 0.4930 0.4186 0.7780 -0.0017 -0.0091 -0.0077 202 A1IUY A C07 
983  C C07 B A1IUY C .   ? 0.4930 0.4177 0.7779 -0.0011 -0.0093 -0.0077 202 A1IUY A C07 
984  C C08 A A1IUY C .   ? 0.5436 0.4595 0.8251 0.0049  -0.0146 -0.0192 202 A1IUY A C08 
985  C C08 B A1IUY C .   ? 0.5457 0.4590 0.8262 0.0047  -0.0152 -0.0189 202 A1IUY A C08 
986  C C09 A A1IUY C .   ? 0.4708 0.3970 0.7595 0.0042  -0.0080 -0.0054 202 A1IUY A C09 
987  C C09 B A1IUY C .   ? 0.4709 0.3952 0.7591 0.0052  -0.0087 -0.0061 202 A1IUY A C09 
988  C C10 A A1IUY C .   ? 0.4633 0.3957 0.7560 0.0023  -0.0030 0.0024  202 A1IUY A C10 
989  C C10 B A1IUY C .   ? 0.4669 0.3979 0.7593 0.0037  -0.0037 0.0014  202 A1IUY A C10 
990  C C12 A A1IUY C .   ? 0.5177 0.4326 0.8039 0.0161  -0.0173 -0.0237 202 A1IUY A C12 
991  C C12 B A1IUY C .   ? 0.5219 0.4315 0.8061 0.0164  -0.0188 -0.0239 202 A1IUY A C12 
992  C C13 A A1IUY C .   ? 0.5841 0.4957 0.8741 0.0294  -0.0237 -0.0376 202 A1IUY A C13 
993  C C13 B A1IUY C .   ? 0.5872 0.4894 0.8736 0.0299  -0.0264 -0.0378 202 A1IUY A C13 
994  C C14 A A1IUY C .   ? 0.5656 0.5078 0.8693 0.0345  -0.0186 -0.0460 202 A1IUY A C14 
995  C C14 B A1IUY C .   ? 0.5966 0.5282 0.8976 0.0372  -0.0223 -0.0475 202 A1IUY A C14 
996  C C15 A A1IUY C .   ? 0.6016 0.5512 0.9145 0.0483  -0.0237 -0.0628 202 A1IUY A C15 
997  C C15 B A1IUY C .   ? 0.6262 0.5605 0.9352 0.0522  -0.0289 -0.0643 202 A1IUY A C15 
998  C C16 A A1IUY C .   ? 0.6432 0.5629 0.9506 0.0602  -0.0362 -0.0704 202 A1IUY A C16 
999  C C16 B A1IUY C .   ? 0.6460 0.5457 0.9464 0.0620  -0.0418 -0.0701 202 A1IUY A C16 
1000 C C17 A A1IUY C .   ? 0.6511 0.5308 0.9396 0.0540  -0.0431 -0.0597 202 A1IUY A C17 
1001 C C17 B A1IUY C .   ? 0.6564 0.5180 0.9368 0.0527  -0.0472 -0.0579 202 A1IUY A C17 
1002 C C18 A A1IUY C .   ? 0.6024 0.4817 0.8825 0.0367  -0.0354 -0.0433 202 A1IUY A C18 
1003 C C18 B A1IUY C .   ? 0.6209 0.4882 0.8953 0.0351  -0.0380 -0.0421 202 A1IUY A C18 
1004 C C19 A A1IUY C .   ? 0.6432 0.4885 0.9038 0.0253  -0.0402 -0.0329 202 A1IUY A C19 
1005 C C19 B A1IUY C .   ? 0.6351 0.4719 0.8902 0.0214  -0.0412 -0.0309 202 A1IUY A C19 
1006 C C24 A A1IUY C .   ? 0.7065 0.4724 0.9668 0.0899  -0.0883 -0.0893 202 A1IUY A C24 
1007 C C24 B A1IUY C .   ? 0.6713 0.4481 0.9432 0.1032  -0.0926 -0.0950 202 A1IUY A C24 
1008 N N11 A A1IUY C .   ? 0.5216 0.4426 0.8110 0.0139  -0.0131 -0.0143 202 A1IUY A N11 
1009 N N11 B A1IUY C .   ? 0.5236 0.4404 0.8114 0.0149  -0.0146 -0.0151 202 A1IUY A N11 
1010 N N20 A A1IUY C .   ? 0.7065 0.5475 0.9850 0.0657  -0.0586 -0.0670 202 A1IUY A N20 
1011 N N20 B A1IUY C .   ? 0.6843 0.5026 0.9510 0.0612  -0.0626 -0.0632 202 A1IUY A N20 
1012 O O06 A A1IUY C .   ? 0.4208 0.3690 0.7139 -0.0139 -0.0026 0.0041  202 A1IUY A O06 
1013 O O06 B A1IUY C .   ? 0.4240 0.3665 0.7149 -0.0143 -0.0027 0.0045  202 A1IUY A O06 
1014 O O22 A A1IUY C .   ? 0.6434 0.4981 0.9314 0.0760  -0.0572 -0.1012 202 A1IUY A O22 
1015 O O22 B A1IUY C .   ? 0.5951 0.3359 0.8330 0.0746  -0.0933 -0.0529 202 A1IUY A O22 
1016 O O23 A A1IUY C .   ? 0.7630 0.5625 1.0157 0.0492  -0.0615 -0.0705 202 A1IUY A O23 
1017 O O23 B A1IUY C .   ? 0.7780 0.6008 1.0618 0.0922  -0.0796 -0.0714 202 A1IUY A O23 
1018 S S21 A A1IUY C .   ? 0.7912 0.6083 1.0616 0.0693  -0.0651 -0.0821 202 A1IUY A S21 
1019 S S21 B A1IUY C .   ? 0.6965 0.4852 0.9614 0.0830  -0.0822 -0.0691 202 A1IUY A S21 
1020 O O   . HOH   D .   ? 0.5698 0.4674 0.7337 -0.1626 0.0239  0.0300  301 HOH   A O   
1021 O O   . HOH   D .   ? 0.7388 0.6666 0.8101 -0.1529 0.0591  0.0028  302 HOH   A O   
1022 O O   . HOH   D .   ? 0.4723 0.4398 0.7833 -0.0057 0.0050  0.0138  303 HOH   A O   
1023 O O   . HOH   D .   ? 0.5009 0.4744 0.7935 -0.0114 0.0649  -0.0429 304 HOH   A O   
1024 O O   . HOH   D .   ? 0.5305 0.3718 0.7888 0.0848  -0.1080 -0.0152 305 HOH   A O   
1025 O O   . HOH   D .   ? 0.4078 0.3695 0.7154 0.0127  0.0005  -0.0070 306 HOH   A O   
1026 O O   . HOH   D .   ? 0.3957 0.3795 0.7568 0.0376  -0.0176 0.0349  307 HOH   A O   
1027 O O   . HOH   D .   ? 0.5535 0.6641 0.9075 -0.0848 0.0183  -0.0046 308 HOH   A O   
1028 O O   . HOH   D .   ? 0.3682 0.3207 0.6766 0.0007  0.0095  0.0137  309 HOH   A O   
1029 O O   . HOH   D .   ? 0.7645 0.3684 0.9392 -0.0528 0.0232  -0.1129 310 HOH   A O   
1030 O O   . HOH   D .   ? 0.4354 0.4239 0.7650 0.0435  -0.0153 -0.0483 311 HOH   A O   
1031 O O   . HOH   D .   ? 0.5926 0.5811 0.9790 0.0505  0.0220  -0.0131 312 HOH   A O   
1032 O O   . HOH   D .   ? 0.4382 0.4894 0.6837 -0.0529 -0.0260 0.0311  313 HOH   A O   
1033 O O   . HOH   D .   ? 0.5858 0.3596 0.7715 -0.0648 -0.0382 0.0030  314 HOH   A O   
1034 O O   . HOH   D .   ? 0.5905 0.4120 0.7391 0.0137  -0.1088 0.0297  315 HOH   A O   
1035 O O   . HOH   D .   ? 0.4882 0.4472 0.8113 0.0719  -0.0609 -0.0403 316 HOH   A O   
1036 O O   . HOH   D .   ? 0.8682 0.5421 0.9446 0.0129  -0.1468 0.0611  317 HOH   A O   
1037 O O   . HOH   D .   ? 0.4529 0.4145 0.7246 -0.0516 0.0321  0.0105  318 HOH   A O   
1038 O O   . HOH   D .   ? 0.5739 0.5313 0.7498 -0.1215 0.0573  0.0073  319 HOH   A O   
1039 O O   . HOH   D .   ? 0.6041 0.6962 0.9258 -0.1128 0.0395  -0.0064 320 HOH   A O   
1040 O O   . HOH   D .   ? 0.5835 0.4510 0.8146 -0.0685 -0.0200 -0.0040 321 HOH   A O   
1041 O O   . HOH   D .   ? 0.4538 0.4197 0.7690 0.0034  0.0073  0.0210  322 HOH   A O   
1042 O O   . HOH   D .   ? 0.4338 0.5159 0.7510 -0.0298 0.0264  -0.0335 323 HOH   A O   
1043 O O   . HOH   D .   ? 0.5675 0.4885 0.8099 -0.1037 -0.0102 0.0001  324 HOH   A O   
1044 O O   . HOH   D .   ? 0.4755 0.4304 0.7828 0.0064  0.0065  0.0075  325 HOH   A O   
1045 O O   . HOH   D .   ? 0.7295 0.7196 0.9449 -0.0452 -0.0640 0.0929  326 HOH   A O   
1046 O O   . HOH   D .   ? 0.5288 0.5427 0.7881 -0.1260 0.0010  -0.0673 327 HOH   A O   
1047 O O   . HOH   D .   ? 0.5192 0.4675 0.7729 -0.0743 0.0256  0.0159  328 HOH   A O   
1048 O O   . HOH   D .   ? 0.4827 0.5937 0.8216 -0.0532 0.0219  -0.0469 329 HOH   A O   
1049 O O   . HOH   D .   ? 0.5734 0.6172 0.8714 -0.0511 0.0269  -0.0095 330 HOH   A O   
1050 O O   . HOH   D .   ? 0.4557 0.4092 0.8292 0.0545  0.0299  -0.0275 331 HOH   A O   
1051 O O   . HOH   D .   ? 0.8543 0.4830 0.9584 -0.2067 0.0024  -0.0057 332 HOH   A O   
1052 O O   . HOH   D .   ? 0.6217 0.4967 0.8959 -0.0041 -0.0177 0.0601  333 HOH   A O   
1053 O O   . HOH   D .   ? 0.9873 0.7510 1.0361 -0.1374 0.0857  -0.2694 334 HOH   A O   
1054 O O   . HOH   D .   ? 0.5547 0.5854 0.9529 0.0426  0.0040  0.0061  335 HOH   A O   
1055 O O   . HOH   D .   ? 0.4098 0.4373 0.7962 0.0460  -0.0328 0.0352  336 HOH   A O   
1056 O O   . HOH   D .   ? 0.8828 0.5738 1.0330 0.0938  -0.1918 0.0264  337 HOH   A O   
1057 O O   . HOH   D .   ? 0.6987 0.6408 0.8494 -0.0548 -0.0554 -0.0236 338 HOH   A O   
1058 O O   . HOH   D .   ? 0.4903 0.6480 0.8825 0.0186  -0.0294 -0.0815 339 HOH   A O   
1059 O O   . HOH   D .   ? 0.7985 0.4046 0.9294 -0.1480 0.0036  -0.0347 340 HOH   A O   
1060 O O   . HOH   D .   ? 0.6088 0.6079 0.8383 -0.0545 0.0942  -0.0781 341 HOH   A O   
1061 O O   . HOH   D .   ? 0.6281 0.6280 0.7760 -0.1376 0.0871  -0.0237 342 HOH   A O   
1062 O O   . HOH   D .   ? 0.4827 0.5094 0.7634 -0.1105 0.0388  0.0041  343 HOH   A O   
1063 O O   . HOH   D .   ? 0.8733 0.7985 0.8316 -0.1674 0.0141  -0.0780 344 HOH   A O   
1064 O O   . HOH   D .   ? 0.8304 0.5533 1.0258 -0.0017 0.0000  0.0000  345 HOH   A O   
1065 O O   . HOH   D .   ? 0.7707 0.5406 0.8556 -0.2494 -0.0173 0.0267  346 HOH   A O   
1066 O O   . HOH   D .   ? 0.8231 0.7561 1.0527 -0.0362 -0.0391 0.0862  347 HOH   A O   
1067 O O   . HOH   D .   ? 1.0570 0.6331 1.0415 -0.0243 -0.1686 0.0934  348 HOH   A O   
1068 O O   . HOH   D .   ? 0.6687 0.6782 0.8231 -0.1527 0.0872  -0.0152 349 HOH   A O   
1069 O O   . HOH   D .   ? 0.7072 0.6366 1.0104 -0.0612 0.0269  0.0466  350 HOH   A O   
1070 O O   . HOH   D .   ? 0.8240 0.3734 0.8409 -0.0864 -0.1053 0.0680  351 HOH   A O   
1071 O O   . HOH   D .   ? 0.8842 0.7657 1.0777 -0.1966 0.0178  -0.0623 352 HOH   A O   
1072 O O   . HOH   D .   ? 0.7995 0.8885 1.1602 0.0964  -0.0062 -0.2459 353 HOH   A O   
1073 O O   . HOH   D .   ? 0.8382 0.7077 0.9957 -0.0689 -0.0631 0.1242  354 HOH   A O   
1074 O O   . HOH   D .   ? 0.9057 0.8121 1.1123 -0.0810 0.0207  0.0359  355 HOH   A O   
# 
