data_9HH7
# 
_entry.id   9HH7 
# 
_audit_conform.dict_name       mmcif_pdbx.dic 
_audit_conform.dict_version    5.403 
_audit_conform.dict_location   http://mmcif.pdb.org/dictionaries/ascii/mmcif_pdbx.dic 
# 
loop_
_database_2.database_id 
_database_2.database_code 
_database_2.pdbx_database_accession 
_database_2.pdbx_DOI 
PDB   9HH7         pdb_00009hh7 10.2210/pdb9hh7/pdb 
WWPDB D_1292143326 ?            ?                   
# 
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 ? 
# 
_pdbx_audit_revision_details.ordinal             1 
_pdbx_audit_revision_details.revision_ordinal    1 
_pdbx_audit_revision_details.data_content_type   'Structure model' 
_pdbx_audit_revision_details.provider            repository 
_pdbx_audit_revision_details.type                'Initial release' 
_pdbx_audit_revision_details.description         ? 
_pdbx_audit_revision_details.details             ? 
# 
_pdbx_audit_revision_group.ordinal             1 
_pdbx_audit_revision_group.revision_ordinal    2 
_pdbx_audit_revision_group.data_content_type   'Structure model' 
_pdbx_audit_revision_group.group               'Database references' 
# 
loop_
_pdbx_audit_revision_category.ordinal 
_pdbx_audit_revision_category.revision_ordinal 
_pdbx_audit_revision_category.data_content_type 
_pdbx_audit_revision_category.category 
1 2 'Structure model' citation        
2 2 'Structure model' citation_author 
# 
loop_
_pdbx_audit_revision_item.ordinal 
_pdbx_audit_revision_item.revision_ordinal 
_pdbx_audit_revision_item.data_content_type 
_pdbx_audit_revision_item.item 
1 2 'Structure model' '_citation.page_first'              
2 2 'Structure model' '_citation.page_last'               
3 2 'Structure model' '_citation.title'                   
4 2 'Structure model' '_citation_author.identifier_ORCID' 
# 
_pdbx_database_status.status_code                     REL 
_pdbx_database_status.status_code_sf                  REL 
_pdbx_database_status.status_code_mr                  ? 
_pdbx_database_status.entry_id                        9HH7 
_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            ? 
_citation.language                  ? 
_citation.page_first                e2500024 
_citation.page_last                 e2500024 
_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 'Bromodomain protein 1'                                                                            15827.206 1  
? ? ? ? 
2 non-polymer syn '3-methyl-4-(3-methyl-4-oxidanylidene-5,6,7,8-tetrahydro-2~{H}-cyclohepta[c]pyrrol-1-yl)benzamide' 296.364   1  
? ? ? ? 
3 water       nat water                                                                                              18.015    77 
? ? ? ? 
# 
_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       
;GPLGSPEFMNKQWYLLANQLILSLSKYEGGHIFEKLVDAKKQNCPDYYDVIKNPMSFSCIKTKLKKGQYAYPSEFVKDVQ
LIFDNCSLYNTSNSVVAITGKNIETYFNNQLIVMGYNNFILKEKKINDMLKLVEEEN
;
_entity_poly.pdbx_seq_one_letter_code_can   
;GPLGSPEFMNKQWYLLANQLILSLSKYEGGHIFEKLVDAKKQNCPDYYDVIKNPMSFSCIKTKLKKGQYAYPSEFVKDVQ
LIFDNCSLYNTSNSVVAITGKNIETYFNNQLIVMGYNNFILKEKKINDMLKLVEEEN
;
_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 '3-methyl-4-(3-methyl-4-oxidanylidene-5,6,7,8-tetrahydro-2~{H}-cyclohepta[c]pyrrol-1-yl)benzamide' A1IUW 
3 water                                                                                              HOH   
# 
loop_
_entity_poly_seq.entity_id 
_entity_poly_seq.num 
_entity_poly_seq.mon_id 
_entity_poly_seq.hetero 
1 1   GLY n 
1 2   PRO n 
1 3   LEU n 
1 4   GLY n 
1 5   SER n 
1 6   PRO n 
1 7   GLU n 
1 8   PHE n 
1 9   MET n 
1 10  ASN n 
1 11  LYS n 
1 12  GLN n 
1 13  TRP n 
1 14  TYR n 
1 15  LEU n 
1 16  LEU n 
1 17  ALA n 
1 18  ASN n 
1 19  GLN n 
1 20  LEU n 
1 21  ILE n 
1 22  LEU n 
1 23  SER n 
1 24  LEU n 
1 25  SER n 
1 26  LYS n 
1 27  TYR n 
1 28  GLU n 
1 29  GLY n 
1 30  GLY n 
1 31  HIS n 
1 32  ILE n 
1 33  PHE n 
1 34  GLU n 
1 35  LYS n 
1 36  LEU n 
1 37  VAL n 
1 38  ASP n 
1 39  ALA n 
1 40  LYS n 
1 41  LYS n 
1 42  GLN n 
1 43  ASN n 
1 44  CYS n 
1 45  PRO n 
1 46  ASP n 
1 47  TYR n 
1 48  TYR n 
1 49  ASP n 
1 50  VAL n 
1 51  ILE n 
1 52  LYS n 
1 53  ASN n 
1 54  PRO n 
1 55  MET n 
1 56  SER n 
1 57  PHE n 
1 58  SER n 
1 59  CYS n 
1 60  ILE n 
1 61  LYS n 
1 62  THR n 
1 63  LYS n 
1 64  LEU n 
1 65  LYS n 
1 66  LYS n 
1 67  GLY n 
1 68  GLN n 
1 69  TYR n 
1 70  ALA n 
1 71  TYR n 
1 72  PRO n 
1 73  SER n 
1 74  GLU n 
1 75  PHE n 
1 76  VAL n 
1 77  LYS n 
1 78  ASP n 
1 79  VAL n 
1 80  GLN n 
1 81  LEU n 
1 82  ILE n 
1 83  PHE n 
1 84  ASP n 
1 85  ASN n 
1 86  CYS n 
1 87  SER n 
1 88  LEU n 
1 89  TYR n 
1 90  ASN n 
1 91  THR n 
1 92  SER n 
1 93  ASN n 
1 94  SER n 
1 95  VAL n 
1 96  VAL n 
1 97  ALA n 
1 98  ILE n 
1 99  THR n 
1 100 GLY n 
1 101 LYS n 
1 102 ASN n 
1 103 ILE n 
1 104 GLU n 
1 105 THR n 
1 106 TYR n 
1 107 PHE n 
1 108 ASN n 
1 109 ASN n 
1 110 GLN n 
1 111 LEU n 
1 112 ILE n 
1 113 VAL n 
1 114 MET n 
1 115 GLY n 
1 116 TYR n 
1 117 ASN n 
1 118 ASN n 
1 119 PHE n 
1 120 ILE n 
1 121 LEU n 
1 122 LYS n 
1 123 GLU n 
1 124 LYS n 
1 125 LYS n 
1 126 ILE n 
1 127 ASN n 
1 128 ASP n 
1 129 MET n 
1 130 LEU n 
1 131 LYS n 
1 132 LEU n 
1 133 VAL n 
1 134 GLU n 
1 135 GLU n 
1 136 GLU n 
1 137 ASN 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                   137 
_entity_src_gen.gene_src_common_name               ? 
_entity_src_gen.gene_src_genus                     ? 
_entity_src_gen.pdbx_gene_src_gene                 PF3D7_1033700 
_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 falciparum 3D7' 
_entity_src_gen.pdbx_gene_src_ncbi_taxonomy_id     36329 
_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 
A1IUW non-polymer         . '3-methyl-4-(3-methyl-4-oxidanylidene-5,6,7,8-tetrahydro-2~{H}-cyclohepta[c]pyrrol-1-yl)benzamide' ? 
'C18 H20 N2 O2'  296.364 
ALA   'L-peptide linking' y ALANINE                                                                                            ? 
'C3 H7 N O2'     89.093  
ASN   'L-peptide linking' y ASPARAGINE                                                                                         ? 
'C4 H8 N2 O3'    132.118 
ASP   'L-peptide linking' y 'ASPARTIC ACID'                                                                                    ? 
'C4 H7 N O4'     133.103 
CYS   'L-peptide linking' y CYSTEINE                                                                                           ? 
'C3 H7 N O2 S'   121.158 
GLN   'L-peptide linking' y GLUTAMINE                                                                                          ? 
'C5 H10 N2 O3'   146.144 
GLU   'L-peptide linking' y 'GLUTAMIC ACID'                                                                                    ? 
'C5 H9 N O4'     147.129 
GLY   'peptide linking'   y GLYCINE                                                                                            ? 
'C2 H5 N O2'     75.067  
HIS   'L-peptide linking' y HISTIDINE                                                                                          ? 
'C6 H10 N3 O2 1' 156.162 
HOH   non-polymer         . WATER                                                                                              ? 
'H2 O'           18.015  
ILE   'L-peptide linking' y ISOLEUCINE                                                                                         ? 
'C6 H13 N O2'    131.173 
LEU   'L-peptide linking' y LEUCINE                                                                                            ? 
'C6 H13 N O2'    131.173 
LYS   'L-peptide linking' y LYSINE                                                                                             ? 
'C6 H15 N2 O2 1' 147.195 
MET   'L-peptide linking' y METHIONINE                                                                                         ? 
'C5 H11 N O2 S'  149.211 
PHE   'L-peptide linking' y PHENYLALANINE                                                                                      ? 
'C9 H11 N O2'    165.189 
PRO   'L-peptide linking' y PROLINE                                                                                            ? 
'C5 H9 N O2'     115.130 
SER   'L-peptide linking' y SERINE                                                                                             ? 
'C3 H7 N O3'     105.093 
THR   'L-peptide linking' y THREONINE                                                                                          ? 
'C4 H9 N O3'     119.119 
TRP   'L-peptide linking' y TRYPTOPHAN                                                                                         ? 
'C11 H12 N2 O2'  204.225 
TYR   'L-peptide linking' y TYROSINE                                                                                           ? 
'C9 H11 N O3'    181.189 
VAL   'L-peptide linking' y VALINE                                                                                             ? 
'C5 H11 N O2'    117.146 
# 
loop_
_pdbx_poly_seq_scheme.asym_id 
_pdbx_poly_seq_scheme.entity_id 
_pdbx_poly_seq_scheme.seq_id 
_pdbx_poly_seq_scheme.mon_id 
_pdbx_poly_seq_scheme.ndb_seq_num 
_pdbx_poly_seq_scheme.pdb_seq_num 
_pdbx_poly_seq_scheme.auth_seq_num 
_pdbx_poly_seq_scheme.pdb_mon_id 
_pdbx_poly_seq_scheme.auth_mon_id 
_pdbx_poly_seq_scheme.pdb_strand_id 
_pdbx_poly_seq_scheme.pdb_ins_code 
_pdbx_poly_seq_scheme.hetero 
A 1 1   GLY 1   1   ?   ?   ?   A . n 
A 1 2   PRO 2   2   ?   ?   ?   A . n 
A 1 3   LEU 3   3   3   LEU LEU A . n 
A 1 4   GLY 4   4   4   GLY GLY A . n 
A 1 5   SER 5   5   5   SER SER A . n 
A 1 6   PRO 6   6   6   PRO PRO A . n 
A 1 7   GLU 7   7   7   GLU GLU A . n 
A 1 8   PHE 8   8   8   PHE PHE A . n 
A 1 9   MET 9   9   9   MET MET A . n 
A 1 10  ASN 10  10  10  ASN ASN A . n 
A 1 11  LYS 11  11  11  LYS LYS A . n 
A 1 12  GLN 12  12  12  GLN GLN A . n 
A 1 13  TRP 13  13  13  TRP TRP A . n 
A 1 14  TYR 14  14  14  TYR TYR A . n 
A 1 15  LEU 15  15  15  LEU LEU A . n 
A 1 16  LEU 16  16  16  LEU LEU A . n 
A 1 17  ALA 17  17  17  ALA ALA A . n 
A 1 18  ASN 18  18  18  ASN ASN A . n 
A 1 19  GLN 19  19  19  GLN GLN A . n 
A 1 20  LEU 20  20  20  LEU LEU A . n 
A 1 21  ILE 21  21  21  ILE ILE A . n 
A 1 22  LEU 22  22  22  LEU LEU A . n 
A 1 23  SER 23  23  23  SER SER A . n 
A 1 24  LEU 24  24  24  LEU LEU A . n 
A 1 25  SER 25  25  25  SER SER A . n 
A 1 26  LYS 26  26  26  LYS LYS A . n 
A 1 27  TYR 27  27  27  TYR TYR A . n 
A 1 28  GLU 28  28  28  GLU GLU A . n 
A 1 29  GLY 29  29  29  GLY GLY A . n 
A 1 30  GLY 30  30  30  GLY GLY A . n 
A 1 31  HIS 31  31  31  HIS HIS A . n 
A 1 32  ILE 32  32  32  ILE ILE A . n 
A 1 33  PHE 33  33  33  PHE PHE A . n 
A 1 34  GLU 34  34  34  GLU GLU A . n 
A 1 35  LYS 35  35  35  LYS LYS A . n 
A 1 36  LEU 36  36  36  LEU LEU A . n 
A 1 37  VAL 37  37  37  VAL VAL A . n 
A 1 38  ASP 38  38  38  ASP ASP A . n 
A 1 39  ALA 39  39  39  ALA ALA A . n 
A 1 40  LYS 40  40  40  LYS LYS A . n 
A 1 41  LYS 41  41  41  LYS LYS A . n 
A 1 42  GLN 42  42  42  GLN GLN A . n 
A 1 43  ASN 43  43  43  ASN ASN A . n 
A 1 44  CYS 44  44  44  CYS CYS A . n 
A 1 45  PRO 45  45  45  PRO PRO A . n 
A 1 46  ASP 46  46  46  ASP ASP A . n 
A 1 47  TYR 47  47  47  TYR TYR A . n 
A 1 48  TYR 48  48  48  TYR TYR A . n 
A 1 49  ASP 49  49  49  ASP ASP A . n 
A 1 50  VAL 50  50  50  VAL VAL A . n 
A 1 51  ILE 51  51  51  ILE ILE A . n 
A 1 52  LYS 52  52  52  LYS LYS A . n 
A 1 53  ASN 53  53  53  ASN ASN A . n 
A 1 54  PRO 54  54  54  PRO PRO A . n 
A 1 55  MET 55  55  55  MET MET A . n 
A 1 56  SER 56  56  56  SER SER A . n 
A 1 57  PHE 57  57  57  PHE PHE A . n 
A 1 58  SER 58  58  58  SER SER A . n 
A 1 59  CYS 59  59  59  CYS CYS A . n 
A 1 60  ILE 60  60  60  ILE ILE A . n 
A 1 61  LYS 61  61  61  LYS LYS A . n 
A 1 62  THR 62  62  62  THR THR A . n 
A 1 63  LYS 63  63  63  LYS LYS A . n 
A 1 64  LEU 64  64  64  LEU LEU A . n 
A 1 65  LYS 65  65  65  LYS LYS A . n 
A 1 66  LYS 66  66  66  LYS LYS A . n 
A 1 67  GLY 67  67  67  GLY GLY A . n 
A 1 68  GLN 68  68  68  GLN GLN A . n 
A 1 69  TYR 69  69  69  TYR TYR A . n 
A 1 70  ALA 70  70  70  ALA ALA A . n 
A 1 71  TYR 71  71  71  TYR TYR A . n 
A 1 72  PRO 72  72  72  PRO PRO A . n 
A 1 73  SER 73  73  73  SER SER A . n 
A 1 74  GLU 74  74  74  GLU GLU A . n 
A 1 75  PHE 75  75  75  PHE PHE A . n 
A 1 76  VAL 76  76  76  VAL VAL A . n 
A 1 77  LYS 77  77  77  LYS LYS A . n 
A 1 78  ASP 78  78  78  ASP ASP A . n 
A 1 79  VAL 79  79  79  VAL VAL A . n 
A 1 80  GLN 80  80  80  GLN GLN A . n 
A 1 81  LEU 81  81  81  LEU LEU A . n 
A 1 82  ILE 82  82  82  ILE ILE A . n 
A 1 83  PHE 83  83  83  PHE PHE A . n 
A 1 84  ASP 84  84  84  ASP ASP A . n 
A 1 85  ASN 85  85  85  ASN ASN A . n 
A 1 86  CYS 86  86  86  CYS CYS 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  TYR 89  89  89  TYR TYR A . n 
A 1 90  ASN 90  90  90  ASN ASN A . n 
A 1 91  THR 91  91  91  THR THR A . n 
A 1 92  SER 92  92  92  SER SER A . n 
A 1 93  ASN 93  93  93  ASN ASN A . n 
A 1 94  SER 94  94  94  SER SER A . n 
A 1 95  VAL 95  95  95  VAL VAL A . n 
A 1 96  VAL 96  96  96  VAL VAL A . n 
A 1 97  ALA 97  97  97  ALA ALA A . n 
A 1 98  ILE 98  98  98  ILE ILE A . n 
A 1 99  THR 99  99  99  THR THR A . n 
A 1 100 GLY 100 100 100 GLY GLY A . n 
A 1 101 LYS 101 101 101 LYS LYS A . n 
A 1 102 ASN 102 102 102 ASN ASN A . n 
A 1 103 ILE 103 103 103 ILE ILE A . n 
A 1 104 GLU 104 104 104 GLU GLU A . n 
A 1 105 THR 105 105 105 THR THR A . n 
A 1 106 TYR 106 106 106 TYR TYR A . n 
A 1 107 PHE 107 107 107 PHE PHE A . n 
A 1 108 ASN 108 108 108 ASN ASN A . n 
A 1 109 ASN 109 109 109 ASN ASN A . n 
A 1 110 GLN 110 110 110 GLN GLN A . n 
A 1 111 LEU 111 111 111 LEU LEU A . n 
A 1 112 ILE 112 112 112 ILE ILE A . n 
A 1 113 VAL 113 113 113 VAL VAL A . n 
A 1 114 MET 114 114 114 MET MET A . n 
A 1 115 GLY 115 115 115 GLY GLY A . n 
A 1 116 TYR 116 116 116 TYR TYR A . n 
A 1 117 ASN 117 117 117 ASN ASN A . n 
A 1 118 ASN 118 118 118 ASN ASN A . n 
A 1 119 PHE 119 119 119 PHE PHE A . n 
A 1 120 ILE 120 120 120 ILE ILE A . n 
A 1 121 LEU 121 121 121 LEU LEU A . n 
A 1 122 LYS 122 122 122 LYS LYS A . n 
A 1 123 GLU 123 123 123 GLU GLU A . n 
A 1 124 LYS 124 124 124 LYS LYS A . n 
A 1 125 LYS 125 125 125 LYS LYS A . n 
A 1 126 ILE 126 126 126 ILE ILE A . n 
A 1 127 ASN 127 127 127 ASN ASN A . n 
A 1 128 ASP 128 128 128 ASP ASP A . n 
A 1 129 MET 129 129 129 MET MET A . n 
A 1 130 LEU 130 130 130 LEU LEU A . n 
A 1 131 LYS 131 131 131 LYS LYS A . n 
A 1 132 LEU 132 132 132 LEU LEU A . n 
A 1 133 VAL 133 133 133 VAL VAL A . n 
A 1 134 GLU 134 134 ?   ?   ?   A . n 
A 1 135 GLU 135 135 ?   ?   ?   A . n 
A 1 136 GLU 136 136 ?   ?   ?   A . n 
A 1 137 ASN 137 137 ?   ?   ?   A . n 
# 
_pdbx_entity_instance_feature.ordinal        1 
_pdbx_entity_instance_feature.comp_id        A1IUW 
_pdbx_entity_instance_feature.asym_id        ? 
_pdbx_entity_instance_feature.seq_num        ? 
_pdbx_entity_instance_feature.auth_comp_id   A1IUW 
_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 A1IUW 1  201 201 A1IUW RWA A . 
C 3 HOH   1  301 26  HOH   HOH A . 
C 3 HOH   2  302 65  HOH   HOH A . 
C 3 HOH   3  303 7   HOH   HOH A . 
C 3 HOH   4  304 32  HOH   HOH A . 
C 3 HOH   5  305 24  HOH   HOH A . 
C 3 HOH   6  306 8   HOH   HOH A . 
C 3 HOH   7  307 18  HOH   HOH A . 
C 3 HOH   8  308 5   HOH   HOH A . 
C 3 HOH   9  309 38  HOH   HOH A . 
C 3 HOH   10 310 31  HOH   HOH A . 
C 3 HOH   11 311 15  HOH   HOH A . 
C 3 HOH   12 312 11  HOH   HOH A . 
C 3 HOH   13 313 16  HOH   HOH A . 
C 3 HOH   14 314 20  HOH   HOH A . 
C 3 HOH   15 315 3   HOH   HOH A . 
C 3 HOH   16 316 1   HOH   HOH A . 
C 3 HOH   17 317 39  HOH   HOH A . 
C 3 HOH   18 318 70  HOH   HOH A . 
C 3 HOH   19 319 75  HOH   HOH A . 
C 3 HOH   20 320 33  HOH   HOH A . 
C 3 HOH   21 321 29  HOH   HOH A . 
C 3 HOH   22 322 77  HOH   HOH A . 
C 3 HOH   23 323 66  HOH   HOH A . 
C 3 HOH   24 324 14  HOH   HOH A . 
C 3 HOH   25 325 78  HOH   HOH A . 
C 3 HOH   26 326 19  HOH   HOH A . 
C 3 HOH   27 327 35  HOH   HOH A . 
C 3 HOH   28 328 54  HOH   HOH A . 
C 3 HOH   29 329 17  HOH   HOH A . 
C 3 HOH   30 330 4   HOH   HOH A . 
C 3 HOH   31 331 43  HOH   HOH A . 
C 3 HOH   32 332 25  HOH   HOH A . 
C 3 HOH   33 333 13  HOH   HOH A . 
C 3 HOH   34 334 10  HOH   HOH A . 
C 3 HOH   35 335 2   HOH   HOH A . 
C 3 HOH   36 336 9   HOH   HOH A . 
C 3 HOH   37 337 71  HOH   HOH A . 
C 3 HOH   38 338 6   HOH   HOH A . 
C 3 HOH   39 339 27  HOH   HOH A . 
C 3 HOH   40 340 76  HOH   HOH A . 
C 3 HOH   41 341 73  HOH   HOH A . 
C 3 HOH   42 342 37  HOH   HOH A . 
C 3 HOH   43 343 72  HOH   HOH A . 
C 3 HOH   44 344 28  HOH   HOH A . 
C 3 HOH   45 345 55  HOH   HOH A . 
C 3 HOH   46 346 12  HOH   HOH A . 
C 3 HOH   47 347 22  HOH   HOH A . 
C 3 HOH   48 348 50  HOH   HOH A . 
C 3 HOH   49 349 59  HOH   HOH A . 
C 3 HOH   50 350 74  HOH   HOH A . 
C 3 HOH   51 351 52  HOH   HOH A . 
C 3 HOH   52 352 51  HOH   HOH A . 
C 3 HOH   53 353 30  HOH   HOH A . 
C 3 HOH   54 354 80  HOH   HOH A . 
C 3 HOH   55 355 57  HOH   HOH A . 
C 3 HOH   56 356 69  HOH   HOH A . 
C 3 HOH   57 357 53  HOH   HOH A . 
C 3 HOH   58 358 79  HOH   HOH A . 
C 3 HOH   59 359 23  HOH   HOH A . 
C 3 HOH   60 360 42  HOH   HOH A . 
C 3 HOH   61 361 68  HOH   HOH A . 
C 3 HOH   62 362 21  HOH   HOH A . 
C 3 HOH   63 363 67  HOH   HOH A . 
C 3 HOH   64 364 44  HOH   HOH A . 
C 3 HOH   65 365 56  HOH   HOH A . 
C 3 HOH   66 366 64  HOH   HOH A . 
C 3 HOH   67 367 45  HOH   HOH A . 
C 3 HOH   68 368 41  HOH   HOH A . 
C 3 HOH   69 369 34  HOH   HOH A . 
C 3 HOH   70 370 63  HOH   HOH A . 
C 3 HOH   71 371 58  HOH   HOH A . 
C 3 HOH   72 372 47  HOH   HOH A . 
C 3 HOH   73 373 36  HOH   HOH A . 
C 3 HOH   74 374 60  HOH   HOH A . 
C 3 HOH   75 375 49  HOH   HOH A . 
C 3 HOH   76 376 48  HOH   HOH A . 
C 3 HOH   77 377 62  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 35  ? CE  ? A LYS 35  CE  
2  1 Y 1 A LYS 35  ? NZ  ? A LYS 35  NZ  
3  1 Y 1 A LYS 40  ? CG  ? A LYS 40  CG  
4  1 Y 1 A LYS 40  ? CD  ? A LYS 40  CD  
5  1 Y 1 A LYS 40  ? CE  ? A LYS 40  CE  
6  1 Y 1 A LYS 40  ? NZ  ? A LYS 40  NZ  
7  1 Y 1 A LYS 41  ? CD  ? A LYS 41  CD  
8  1 Y 1 A LYS 41  ? CE  ? A LYS 41  CE  
9  1 Y 1 A LYS 41  ? NZ  ? A LYS 41  NZ  
10 1 Y 1 A LYS 65  ? NZ  ? A LYS 65  NZ  
11 1 Y 1 A LYS 124 ? CG  ? A LYS 124 CG  
12 1 Y 1 A LYS 124 ? CD  ? A LYS 124 CD  
13 1 Y 1 A LYS 124 ? CE  ? A LYS 124 CE  
14 1 Y 1 A LYS 124 ? NZ  ? A LYS 124 NZ  
15 1 Y 1 A LYS 125 ? CG  ? A LYS 125 CG  
16 1 Y 1 A LYS 125 ? CD  ? A LYS 125 CD  
17 1 Y 1 A LYS 125 ? CE  ? A LYS 125 CE  
18 1 Y 1 A LYS 125 ? NZ  ? A LYS 125 NZ  
19 1 Y 1 A LEU 130 ? CD1 ? A LEU 130 CD1 
20 1 Y 1 A LEU 130 ? CD2 ? A LEU 130 CD2 
21 1 Y 1 A LYS 131 ? CG  ? A LYS 131 CG  
22 1 Y 1 A LYS 131 ? CD  ? A LYS 131 CD  
23 1 Y 1 A LYS 131 ? CE  ? A LYS 131 CE  
24 1 Y 1 A LYS 131 ? NZ  ? A LYS 131 NZ  
25 1 Y 1 A LEU 132 ? CG  ? A LEU 132 CG  
26 1 Y 1 A LEU 132 ? CD1 ? A LEU 132 CD1 
27 1 Y 1 A LEU 132 ? CD2 ? A LEU 132 CD2 
# 
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'   ? ? ? ? ? ? ? ? ? ? ? STARANISO ? ? ? .         2 
? phasing          ? ? ? ? ? ? ? ? ? ? ? PHASER    ? ? ? .         3 
? 'data reduction' ? ? ? ? ? ? ? ? ? ? ? XDS       ? ? ? .         4 
# 
_cell.angle_alpha                  90.000 
_cell.angle_alpha_esd              ? 
_cell.angle_beta                   90.000 
_cell.angle_beta_esd               ? 
_cell.angle_gamma                  90.000 
_cell.angle_gamma_esd              ? 
_cell.entry_id                     9HH7 
_cell.details                      ? 
_cell.formula_units_Z              ? 
_cell.length_a                     38.120 
_cell.length_a_esd                 ? 
_cell.length_b                     88.215 
_cell.length_b_esd                 ? 
_cell.length_c                     108.493 
_cell.length_c_esd                 ? 
_cell.volume                       364835.465 
_cell.volume_esd                   ? 
_cell.Z_PDB                        8 
_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                         9HH7 
_symmetry.cell_setting                     ? 
_symmetry.Int_Tables_number                23 
_symmetry.space_group_name_Hall            'I 2 2' 
_symmetry.space_group_name_H-M             'I 2 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                   9HH7 
_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             2.88 
_exptl_crystal.density_method               ? 
_exptl_crystal.density_percent_sol          57.31 
_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    
'20% PEG MMW (PEG 2K, 3350, 4K and 5K MME ;each 12.5 %) ,7% (v/v) Tacsimate, 0.1 M HEPES pH 7.2' 
_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 EIGER2 X CdTe 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         2022-02-15 
_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   0.88560 
_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                        'ESRF BEAMLINE ID23-1' 
_diffrn_source.voltage                     ? 
_diffrn_source.take-off_angle              ? 
_diffrn_source.pdbx_wavelength_list        0.88560 
_diffrn_source.pdbx_wavelength             ? 
_diffrn_source.pdbx_synchrotron_beamline   ID23-1 
_diffrn_source.pdbx_synchrotron_site       ESRF 
# 
_reflns.B_iso_Wilson_estimate                          ? 
_reflns.entry_id                                       9HH7 
_reflns.data_reduction_details                         ? 
_reflns.data_reduction_method                          ? 
_reflns.d_resolution_high                              1.787 
_reflns.d_resolution_low                               35.965 
_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                                     9402 
_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                           91.8 
_reflns.R_free_details                                 ? 
_reflns.Rmerge_F_all                                   ? 
_reflns.Rmerge_F_obs                                   ? 
_reflns.Friedel_coverage                               ? 
_reflns.number_gt                                      ? 
_reflns.threshold_expression                           ? 
_reflns.pdbx_redundancy                                6.3 
_reflns.pdbx_netI_over_av_sigmaI                       ? 
_reflns.pdbx_netI_over_sigmaI                          13.4 
_reflns.pdbx_res_netI_over_av_sigmaI_2                 ? 
_reflns.pdbx_res_netI_over_sigmaI_2                    ? 
_reflns.pdbx_chi_squared                               ? 
_reflns.pdbx_scaling_rejects                           ? 
_reflns.pdbx_d_res_high_opt                            ? 
_reflns.pdbx_d_res_low_opt                             ? 
_reflns.pdbx_d_res_opt_method                          ? 
_reflns.phase_calculation_details                      ? 
_reflns.pdbx_Rrim_I_all                                0.076 
_reflns.pdbx_Rpim_I_all                                ? 
_reflns.pdbx_d_opt                                     ? 
_reflns.pdbx_number_measured_all                       ? 
_reflns.pdbx_diffrn_id                                 1 
_reflns.pdbx_ordinal                                   1 
_reflns.pdbx_CC_half                                   0.999 
_reflns.pdbx_CC_star                                   ? 
_reflns.pdbx_R_split                                   ? 
_reflns.pdbx_Rmerge_I_obs                              0.070 
_reflns.pdbx_Rmerge_I_all                              ? 
_reflns.pdbx_Rsym_value                                ? 
_reflns.pdbx_CC_split_method                           ? 
_reflns.pdbx_aniso_diffraction_limit_axis_1_ortho[1]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_1_ortho[2]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_1_ortho[3]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_2_ortho[1]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_2_ortho[2]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_2_ortho[3]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_3_ortho[1]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_3_ortho[2]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_3_ortho[3]   ? 
_reflns.pdbx_aniso_diffraction_limit_1                 ? 
_reflns.pdbx_aniso_diffraction_limit_2                 ? 
_reflns.pdbx_aniso_diffraction_limit_3                 ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_1_ortho[1]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_1_ortho[2]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_1_ortho[3]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_2_ortho[1]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_2_ortho[2]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_2_ortho[3]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_3_ortho[1]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_3_ortho[2]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_3_ortho[3]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvalue_1               ? 
_reflns.pdbx_aniso_B_tensor_eigenvalue_2               ? 
_reflns.pdbx_aniso_B_tensor_eigenvalue_3               ? 
_reflns.pdbx_orthogonalization_convention              ? 
_reflns.pdbx_percent_possible_ellipsoidal              ? 
_reflns.pdbx_percent_possible_spherical                ? 
_reflns.pdbx_percent_possible_ellipsoidal_anomalous    ? 
_reflns.pdbx_percent_possible_spherical_anomalous      ? 
_reflns.pdbx_redundancy_anomalous                      ? 
_reflns.pdbx_CC_half_anomalous                         ? 
_reflns.pdbx_absDiff_over_sigma_anomalous              ? 
_reflns.pdbx_percent_possible_anomalous                ? 
_reflns.pdbx_observed_signal_threshold                 ? 
_reflns.pdbx_signal_type                               ? 
_reflns.pdbx_signal_details                            ? 
_reflns.pdbx_signal_software_id                        ? 
# 
_reflns_shell.d_res_high                                    1.787 
_reflns_shell.d_res_low                                     1.944 
_reflns_shell.meanI_over_sigI_all                           ? 
_reflns_shell.meanI_over_sigI_obs                           ? 
_reflns_shell.number_measured_all                           ? 
_reflns_shell.number_measured_obs                           ? 
_reflns_shell.number_possible                               ? 
_reflns_shell.number_unique_all                             ? 
_reflns_shell.number_unique_obs                             1146 
_reflns_shell.percent_possible_obs                          ? 
_reflns_shell.Rmerge_F_all                                  ? 
_reflns_shell.Rmerge_F_obs                                  ? 
_reflns_shell.meanI_over_sigI_gt                            ? 
_reflns_shell.meanI_over_uI_all                             ? 
_reflns_shell.meanI_over_uI_gt                              ? 
_reflns_shell.number_measured_gt                            ? 
_reflns_shell.number_unique_gt                              ? 
_reflns_shell.percent_possible_gt                           ? 
_reflns_shell.Rmerge_F_gt                                   ? 
_reflns_shell.Rmerge_I_gt                                   ? 
_reflns_shell.pdbx_redundancy                               ? 
_reflns_shell.pdbx_chi_squared                              ? 
_reflns_shell.pdbx_netI_over_sigmaI_all                     ? 
_reflns_shell.pdbx_netI_over_sigmaI_obs                     ? 
_reflns_shell.pdbx_Rrim_I_all                               ? 
_reflns_shell.pdbx_Rpim_I_all                               ? 
_reflns_shell.pdbx_rejects                                  ? 
_reflns_shell.pdbx_ordinal                                  1 
_reflns_shell.pdbx_diffrn_id                                1 
_reflns_shell.pdbx_CC_half                                  0.612 
_reflns_shell.pdbx_CC_star                                  ? 
_reflns_shell.pdbx_R_split                                  ? 
_reflns_shell.percent_possible_all                          ? 
_reflns_shell.Rmerge_I_all                                  ? 
_reflns_shell.Rmerge_I_obs                                  ? 
_reflns_shell.pdbx_Rsym_value                               ? 
_reflns_shell.pdbx_percent_possible_ellipsoidal             ? 
_reflns_shell.pdbx_percent_possible_spherical               ? 
_reflns_shell.pdbx_percent_possible_ellipsoidal_anomalous   ? 
_reflns_shell.pdbx_percent_possible_spherical_anomalous     ? 
_reflns_shell.pdbx_redundancy_anomalous                     ? 
_reflns_shell.pdbx_CC_half_anomalous                        ? 
_reflns_shell.pdbx_absDiff_over_sigma_anomalous             ? 
_reflns_shell.pdbx_percent_possible_anomalous               ? 
# 
_refine.aniso_B[1][1]                            ? 
_refine.aniso_B[1][2]                            ? 
_refine.aniso_B[1][3]                            ? 
_refine.aniso_B[2][2]                            ? 
_refine.aniso_B[2][3]                            ? 
_refine.aniso_B[3][3]                            ? 
_refine.B_iso_max                                ? 
_refine.B_iso_mean                               49.69 
_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                                 9HH7 
_refine.pdbx_refine_id                           'X-RAY DIFFRACTION' 
_refine.ls_abs_structure_details                 ? 
_refine.ls_abs_structure_Flack                   ? 
_refine.ls_abs_structure_Flack_esd               ? 
_refine.ls_abs_structure_Rogers                  ? 
_refine.ls_abs_structure_Rogers_esd              ? 
_refine.ls_d_res_high                            1.79 
_refine.ls_d_res_low                             35.96 
_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                     9398 
_refine.ls_number_reflns_R_free                  433 
_refine.ls_number_reflns_R_work                  8965 
_refine.ls_number_restraints                     ? 
_refine.ls_percent_reflns_obs                    52.79 
_refine.ls_percent_reflns_R_free                 4.61 
_refine.ls_R_factor_all                          ? 
_refine.ls_R_factor_obs                          0.2105 
_refine.ls_R_factor_R_free                       0.2432 
_refine.ls_R_factor_R_free_error                 ? 
_refine.ls_R_factor_R_free_error_details         ? 
_refine.ls_R_factor_R_work                       0.2089 
_refine.ls_R_Fsqd_factor_obs                     ? 
_refine.ls_R_I_factor_obs                        ? 
_refine.ls_redundancy_reflns_all                 ? 
_refine.ls_redundancy_reflns_obs                 ? 
_refine.ls_restrained_S_all                      ? 
_refine.ls_restrained_S_obs                      ? 
_refine.ls_shift_over_esd_max                    ? 
_refine.ls_shift_over_esd_mean                   ? 
_refine.ls_structure_factor_coef                 ? 
_refine.ls_weighting_details                     ? 
_refine.ls_weighting_scheme                      ? 
_refine.ls_wR_factor_all                         ? 
_refine.ls_wR_factor_obs                         ? 
_refine.ls_wR_factor_R_free                      ? 
_refine.ls_wR_factor_R_work                      ? 
_refine.occupancy_max                            ? 
_refine.occupancy_min                            ? 
_refine.solvent_model_details                    'FLAT BULK SOLVENT MODEL' 
_refine.solvent_model_param_bsol                 ? 
_refine.solvent_model_param_ksol                 ? 
_refine.pdbx_R_complete                          ? 
_refine.ls_R_factor_gt                           ? 
_refine.ls_goodness_of_fit_gt                    ? 
_refine.ls_goodness_of_fit_ref                   ? 
_refine.ls_shift_over_su_max                     ? 
_refine.ls_shift_over_su_max_lt                  ? 
_refine.ls_shift_over_su_mean                    ? 
_refine.ls_shift_over_su_mean_lt                 ? 
_refine.pdbx_ls_sigma_I                          ? 
_refine.pdbx_ls_sigma_F                          1.35 
_refine.pdbx_ls_sigma_Fsqd                       ? 
_refine.pdbx_data_cutoff_high_absF               ? 
_refine.pdbx_data_cutoff_high_rms_absF           ? 
_refine.pdbx_data_cutoff_low_absF                ? 
_refine.pdbx_isotropic_thermal_model             ? 
_refine.pdbx_ls_cross_valid_method               'FREE R-VALUE' 
_refine.pdbx_method_to_determine_struct          'MOLECULAR REPLACEMENT' 
_refine.pdbx_starting_model                      ? 
_refine.pdbx_stereochemistry_target_values       'GeoStd + Monomer Library + CDL v1.2' 
_refine.pdbx_R_Free_selection_details            ? 
_refine.pdbx_stereochem_target_val_spec_case     ? 
_refine.pdbx_overall_ESU_R                       ? 
_refine.pdbx_overall_ESU_R_Free                  ? 
_refine.pdbx_solvent_vdw_probe_radii             1.1000 
_refine.pdbx_solvent_ion_probe_radii             ? 
_refine.pdbx_solvent_shrinkage_radii             0.9000 
_refine.pdbx_real_space_R                        ? 
_refine.pdbx_density_correlation                 ? 
_refine.pdbx_pd_number_of_powder_patterns        ? 
_refine.pdbx_pd_number_of_points                 ? 
_refine.pdbx_pd_meas_number_of_points            ? 
_refine.pdbx_pd_proc_ls_prof_R_factor            ? 
_refine.pdbx_pd_proc_ls_prof_wR_factor           ? 
_refine.pdbx_pd_Marquardt_correlation_coeff      ? 
_refine.pdbx_pd_Fsqrd_R_factor                   ? 
_refine.pdbx_pd_ls_matrix_band_width             ? 
_refine.pdbx_overall_phase_error                 35.3742 
_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                            0.2075 
_refine.overall_SU_R_Cruickshank_DPI             ? 
_refine.overall_SU_R_free                        ? 
_refine.overall_FOM_free_R_set                   ? 
_refine.overall_FOM_work_R_set                   ? 
_refine.pdbx_average_fsc_overall                 ? 
_refine.pdbx_average_fsc_work                    ? 
_refine.pdbx_average_fsc_free                    ? 
# 
_refine_hist.pdbx_refine_id                   'X-RAY DIFFRACTION' 
_refine_hist.cycle_id                         LAST 
_refine_hist.details                          ? 
_refine_hist.d_res_high                       1.79 
_refine_hist.d_res_low                        35.96 
_refine_hist.number_atoms_solvent             77 
_refine_hist.number_atoms_total               1137 
_refine_hist.number_reflns_all                ? 
_refine_hist.number_reflns_obs                ? 
_refine_hist.number_reflns_R_free             ? 
_refine_hist.number_reflns_R_work             ? 
_refine_hist.R_factor_all                     ? 
_refine_hist.R_factor_obs                     ? 
_refine_hist.R_factor_R_free                  ? 
_refine_hist.R_factor_R_work                  ? 
_refine_hist.pdbx_number_residues_total       ? 
_refine_hist.pdbx_B_iso_mean_ligand           ? 
_refine_hist.pdbx_B_iso_mean_solvent          ? 
_refine_hist.pdbx_number_atoms_protein        1038 
_refine_hist.pdbx_number_atoms_nucleic_acid   0 
_refine_hist.pdbx_number_atoms_ligand         22 
_refine_hist.pdbx_number_atoms_lipid          ? 
_refine_hist.pdbx_number_atoms_carb           ? 
_refine_hist.pdbx_pseudo_atom_details         ? 
# 
loop_
_refine_ls_restr.pdbx_refine_id 
_refine_ls_restr.criterion 
_refine_ls_restr.dev_ideal 
_refine_ls_restr.dev_ideal_target 
_refine_ls_restr.number 
_refine_ls_restr.rejects 
_refine_ls_restr.type 
_refine_ls_restr.weight 
_refine_ls_restr.pdbx_restraint_function 
'X-RAY DIFFRACTION' ? 0.0021  ? 1126 ? f_bond_d           ? ? 
'X-RAY DIFFRACTION' ? 0.3931  ? 1532 ? f_angle_d          ? ? 
'X-RAY DIFFRACTION' ? 0.0349  ? 161  ? f_chiral_restr     ? ? 
'X-RAY DIFFRACTION' ? 0.0027  ? 228  ? f_plane_restr      ? ? 
'X-RAY DIFFRACTION' ? 10.6619 ? 431  ? f_dihedral_angle_d ? ? 
# 
loop_
_refine_ls_shell.pdbx_refine_id 
_refine_ls_shell.d_res_high 
_refine_ls_shell.d_res_low 
_refine_ls_shell.number_reflns_all 
_refine_ls_shell.number_reflns_obs 
_refine_ls_shell.number_reflns_R_free 
_refine_ls_shell.number_reflns_R_work 
_refine_ls_shell.percent_reflns_obs 
_refine_ls_shell.percent_reflns_R_free 
_refine_ls_shell.R_factor_all 
_refine_ls_shell.R_factor_obs 
_refine_ls_shell.R_factor_R_free_error 
_refine_ls_shell.R_factor_R_work 
_refine_ls_shell.redundancy_reflns_all 
_refine_ls_shell.redundancy_reflns_obs 
_refine_ls_shell.wR_factor_all 
_refine_ls_shell.wR_factor_obs 
_refine_ls_shell.wR_factor_R_free 
_refine_ls_shell.wR_factor_R_work 
_refine_ls_shell.pdbx_R_complete 
_refine_ls_shell.pdbx_total_number_of_bins_used 
_refine_ls_shell.pdbx_phase_error 
_refine_ls_shell.pdbx_fsc_work 
_refine_ls_shell.pdbx_fsc_free 
_refine_ls_shell.R_factor_R_free 
'X-RAY DIFFRACTION' 1.79 2.05  . . 54  1012 18.28 . . . . 0.3223 . . . . . . . . . . . 0.3511 
'X-RAY DIFFRACTION' 2.05 2.58  . . 125 2720 48.34 . . . . 0.2879 . . . . . . . . . . . 0.3269 
'X-RAY DIFFRACTION' 2.58 35.96 . . 254 5233 90.17 . . . . 0.1939 . . . . . . . . . . . 0.2279 
# 
_struct.entry_id                     9HH7 
_struct.title                        'Crystal Structure of the Plasmodium falciparum Bromodomain PfBDP1 in complex with RMM23' 
_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        9HH7 
_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 ? 
# 
_struct_ref.id                         1 
_struct_ref.db_name                    UNP 
_struct_ref.db_code                    Q8IJ72_PLAF7 
_struct_ref.pdbx_db_accession          Q8IJ72 
_struct_ref.pdbx_db_isoform            ? 
_struct_ref.entity_id                  1 
_struct_ref.pdbx_seq_one_letter_code   
;NKQWYLLANQLILSLSKYEGGHIFEKLVDAKKQNCPDYYDVIKNPMSFSCIKTKLKKGQYAYPSEFVKDVQLIFDNCSLY
NTSNSVVAITGKNIETYFNNQLIVMGYNNFILKEKKINDMLKLVEEEN
;
_struct_ref.pdbx_align_begin           333 
# 
_struct_ref_seq.align_id                      1 
_struct_ref_seq.ref_id                        1 
_struct_ref_seq.pdbx_PDB_id_code              9HH7 
_struct_ref_seq.pdbx_strand_id                A 
_struct_ref_seq.seq_align_beg                 10 
_struct_ref_seq.pdbx_seq_align_beg_ins_code   ? 
_struct_ref_seq.seq_align_end                 137 
_struct_ref_seq.pdbx_seq_align_end_ins_code   ? 
_struct_ref_seq.pdbx_db_accession             Q8IJ72 
_struct_ref_seq.db_align_beg                  333 
_struct_ref_seq.pdbx_db_align_beg_ins_code    ? 
_struct_ref_seq.db_align_end                  460 
_struct_ref_seq.pdbx_db_align_end_ins_code    ? 
_struct_ref_seq.pdbx_auth_seq_align_beg       10 
_struct_ref_seq.pdbx_auth_seq_align_end       137 
# 
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 9HH7 GLY A 1 ? UNP Q8IJ72 ? ? 'expression tag' 1 1 
1 9HH7 PRO A 2 ? UNP Q8IJ72 ? ? 'expression tag' 2 2 
1 9HH7 LEU A 3 ? UNP Q8IJ72 ? ? 'expression tag' 3 3 
1 9HH7 GLY A 4 ? UNP Q8IJ72 ? ? 'expression tag' 4 4 
1 9HH7 SER A 5 ? UNP Q8IJ72 ? ? 'expression tag' 5 5 
1 9HH7 PRO A 6 ? UNP Q8IJ72 ? ? 'expression tag' 6 6 
1 9HH7 GLU A 7 ? UNP Q8IJ72 ? ? 'expression tag' 7 7 
1 9HH7 PHE A 8 ? UNP Q8IJ72 ? ? 'expression tag' 8 8 
1 9HH7 MET A 9 ? UNP Q8IJ72 ? ? 'expression tag' 9 9 
# 
_pdbx_struct_assembly.id                   1 
_pdbx_struct_assembly.details              author_defined_assembly 
_pdbx_struct_assembly.method_details       ? 
_pdbx_struct_assembly.oligomeric_details   monomeric 
_pdbx_struct_assembly.oligomeric_count     1 
# 
loop_
_pdbx_struct_assembly_prop.biol_id 
_pdbx_struct_assembly_prop.type 
_pdbx_struct_assembly_prop.value 
_pdbx_struct_assembly_prop.details 
1 'ABSA (A^2)' 0    ? 
1 MORE         0    ? 
1 'SSA (A^2)'  7890 ? 
# 
_pdbx_struct_assembly_gen.assembly_id       1 
_pdbx_struct_assembly_gen.oper_expression   1 
_pdbx_struct_assembly_gen.asym_id_list      A,B,C 
# 
_pdbx_struct_assembly_auth_evidence.id                     1 
_pdbx_struct_assembly_auth_evidence.assembly_id            1 
_pdbx_struct_assembly_auth_evidence.experimental_support   '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 5   ? TYR A 27  ? SER A 5   TYR A 27  1 ? 23 
HELX_P HELX_P2 AA2 GLY A 29  ? GLU A 34  ? GLY A 29  GLU A 34  5 ? 6  
HELX_P HELX_P3 AA3 ASP A 46  ? ILE A 51  ? ASP A 46  ILE A 51  1 ? 6  
HELX_P HELX_P4 AA4 SER A 56  ? LYS A 66  ? SER A 56  LYS A 66  1 ? 11 
HELX_P HELX_P5 AA5 TYR A 71  ? ASN A 90  ? TYR A 71  ASN A 90  1 ? 20 
HELX_P HELX_P6 AA6 SER A 94  ? MET A 114 ? SER A 94  MET A 114 1 ? 21 
HELX_P HELX_P7 AA7 GLY A 115 ? LEU A 132 ? GLY A 115 LEU A 132 1 ? 18 
# 
_struct_conf_type.id          HELX_P 
_struct_conf_type.criteria    ? 
_struct_conf_type.reference   ? 
# 
_pdbx_entry_details.entry_id                   9HH7 
_pdbx_entry_details.nonpolymer_details         ? 
_pdbx_entry_details.sequence_details           ? 
_pdbx_entry_details.compound_details           ? 
_pdbx_entry_details.source_details             ? 
_pdbx_entry_details.has_ligand_of_interest     Y 
_pdbx_entry_details.has_protein_modification   N 
# 
_pdbx_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         2.91732545288 
_pdbx_refine_tls.origin_y         20.2820248253 
_pdbx_refine_tls.origin_z         12.9398573696 
_pdbx_refine_tls.T[1][1]          0.173029760141 
_pdbx_refine_tls.T[1][1]_esd      ? 
_pdbx_refine_tls.T[1][2]          -0.00584985093169 
_pdbx_refine_tls.T[1][2]_esd      ? 
_pdbx_refine_tls.T[1][3]          0.0120563201081 
_pdbx_refine_tls.T[1][3]_esd      ? 
_pdbx_refine_tls.T[2][2]          0.312778001262 
_pdbx_refine_tls.T[2][2]_esd      ? 
_pdbx_refine_tls.T[2][3]          0.132557350907 
_pdbx_refine_tls.T[2][3]_esd      ? 
_pdbx_refine_tls.T[3][3]          0.168889446937 
_pdbx_refine_tls.T[3][3]_esd      ? 
_pdbx_refine_tls.L[1][1]          2.90853896846 
_pdbx_refine_tls.L[1][1]_esd      ? 
_pdbx_refine_tls.L[1][2]          -0.925958997223 
_pdbx_refine_tls.L[1][2]_esd      ? 
_pdbx_refine_tls.L[1][3]          -0.831656171181 
_pdbx_refine_tls.L[1][3]_esd      ? 
_pdbx_refine_tls.L[2][2]          1.25322727904 
_pdbx_refine_tls.L[2][2]_esd      ? 
_pdbx_refine_tls.L[2][3]          0.433193206721 
_pdbx_refine_tls.L[2][3]_esd      ? 
_pdbx_refine_tls.L[3][3]          3.62847400076 
_pdbx_refine_tls.L[3][3]_esd      ? 
_pdbx_refine_tls.S[1][1]          -0.201694964041 
_pdbx_refine_tls.S[1][1]_esd      ? 
_pdbx_refine_tls.S[1][2]          0.776563681564 
_pdbx_refine_tls.S[1][2]_esd      ? 
_pdbx_refine_tls.S[1][3]          -0.270454456667 
_pdbx_refine_tls.S[1][3]_esd      ? 
_pdbx_refine_tls.S[2][1]          -0.219134379056 
_pdbx_refine_tls.S[2][1]_esd      ? 
_pdbx_refine_tls.S[2][2]          -0.0503090031418 
_pdbx_refine_tls.S[2][2]_esd      ? 
_pdbx_refine_tls.S[2][3]          -0.204306772263 
_pdbx_refine_tls.S[2][3]_esd      ? 
_pdbx_refine_tls.S[3][1]          0.138169211908 
_pdbx_refine_tls.S[3][1]_esd      ? 
_pdbx_refine_tls.S[3][2]          0.152632548196 
_pdbx_refine_tls.S[3][2]_esd      ? 
_pdbx_refine_tls.S[3][3]          0.18176569888 
_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   A 
_pdbx_refine_tls_group.beg_label_seq_id    1 
_pdbx_refine_tls_group.beg_auth_asym_id    A 
_pdbx_refine_tls_group.beg_auth_seq_id     3 
_pdbx_refine_tls_group.beg_PDB_ins_code    ? 
_pdbx_refine_tls_group.end_label_asym_id   C 
_pdbx_refine_tls_group.end_label_seq_id    ? 
_pdbx_refine_tls_group.end_auth_asym_id    C 
_pdbx_refine_tls_group.end_auth_seq_id     80 
_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 374 ? 6.03 . 
2 1 O ? A HOH 375 ? 6.04 . 
3 1 O ? A HOH 376 ? 6.13 . 
4 1 O ? A HOH 377 ? 6.44 . 
# 
loop_
_pdbx_unobs_or_zero_occ_residues.id 
_pdbx_unobs_or_zero_occ_residues.PDB_model_num 
_pdbx_unobs_or_zero_occ_residues.polymer_flag 
_pdbx_unobs_or_zero_occ_residues.occupancy_flag 
_pdbx_unobs_or_zero_occ_residues.auth_asym_id 
_pdbx_unobs_or_zero_occ_residues.auth_comp_id 
_pdbx_unobs_or_zero_occ_residues.auth_seq_id 
_pdbx_unobs_or_zero_occ_residues.PDB_ins_code 
_pdbx_unobs_or_zero_occ_residues.label_asym_id 
_pdbx_unobs_or_zero_occ_residues.label_comp_id 
_pdbx_unobs_or_zero_occ_residues.label_seq_id 
1 1 Y 1 A GLY 1   ? A GLY 1   
2 1 Y 1 A PRO 2   ? A PRO 2   
3 1 Y 1 A GLU 134 ? A GLU 134 
4 1 Y 1 A GLU 135 ? A GLU 135 
5 1 Y 1 A GLU 136 ? A GLU 136 
6 1 Y 1 A ASN 137 ? A ASN 137 
# 
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 
A1IUW N1   N Y N 1   
A1IUW C4   C Y N 2   
A1IUW C5   C Y N 3   
A1IUW C6   C Y N 4   
A1IUW C7   C Y N 5   
A1IUW C8   C Y N 6   
A1IUW C10  C Y N 7   
A1IUW C13  C Y N 8   
A1IUW C15  C N N 9   
A1IUW N    N N N 10  
A1IUW C    C N N 11  
A1IUW O    O N N 12  
A1IUW C1   C N N 13  
A1IUW C11  C N N 14  
A1IUW C12  C N N 15  
A1IUW C14  C Y N 16  
A1IUW C2   C N N 17  
A1IUW C3   C Y N 18  
A1IUW C9   C Y N 19  
A1IUW O1   O N N 20  
A1IUW C16  C N N 21  
A1IUW C17  C N N 22  
A1IUW HN1  H N N 23  
A1IUW H8   H N N 24  
A1IUW H10  H N N 25  
A1IUW H    H N N 26  
A1IUW H1   H N N 27  
A1IUW H3   H N N 28  
A1IUW H2   H N N 29  
A1IUW H4   H N N 30  
A1IUW H5   H N N 31  
A1IUW H11  H N N 32  
A1IUW H13  H N N 33  
A1IUW H12  H N N 34  
A1IUW H6   H N N 35  
A1IUW H7   H N N 36  
A1IUW H9   H N N 37  
A1IUW H14  H N N 38  
A1IUW H15  H N N 39  
A1IUW H17  H N N 40  
A1IUW H18  H N N 41  
A1IUW H16  H N N 42  
ALA   N    N N N 43  
ALA   CA   C N S 44  
ALA   C    C N N 45  
ALA   O    O N N 46  
ALA   CB   C N N 47  
ALA   OXT  O N N 48  
ALA   H    H N N 49  
ALA   H2   H N N 50  
ALA   HA   H N N 51  
ALA   HB1  H N N 52  
ALA   HB2  H N N 53  
ALA   HB3  H N N 54  
ALA   HXT  H N N 55  
ASN   N    N N N 56  
ASN   CA   C N S 57  
ASN   C    C N N 58  
ASN   O    O N N 59  
ASN   CB   C N N 60  
ASN   CG   C N N 61  
ASN   OD1  O N N 62  
ASN   ND2  N N N 63  
ASN   OXT  O N N 64  
ASN   H    H N N 65  
ASN   H2   H N N 66  
ASN   HA   H N N 67  
ASN   HB2  H N N 68  
ASN   HB3  H N N 69  
ASN   HD21 H N N 70  
ASN   HD22 H N N 71  
ASN   HXT  H N N 72  
ASP   N    N N N 73  
ASP   CA   C N S 74  
ASP   C    C N N 75  
ASP   O    O N N 76  
ASP   CB   C N N 77  
ASP   CG   C N N 78  
ASP   OD1  O N N 79  
ASP   OD2  O N N 80  
ASP   OXT  O N N 81  
ASP   H    H N N 82  
ASP   H2   H N N 83  
ASP   HA   H N N 84  
ASP   HB2  H N N 85  
ASP   HB3  H N N 86  
ASP   HD2  H N N 87  
ASP   HXT  H N N 88  
CYS   N    N N N 89  
CYS   CA   C N R 90  
CYS   C    C N N 91  
CYS   O    O N N 92  
CYS   CB   C N N 93  
CYS   SG   S N N 94  
CYS   OXT  O N N 95  
CYS   H    H N N 96  
CYS   H2   H N N 97  
CYS   HA   H N N 98  
CYS   HB2  H N N 99  
CYS   HB3  H N N 100 
CYS   HG   H N N 101 
CYS   HXT  H N N 102 
GLN   N    N N N 103 
GLN   CA   C N S 104 
GLN   C    C N N 105 
GLN   O    O N N 106 
GLN   CB   C N N 107 
GLN   CG   C N N 108 
GLN   CD   C N N 109 
GLN   OE1  O N N 110 
GLN   NE2  N N N 111 
GLN   OXT  O N N 112 
GLN   H    H N N 113 
GLN   H2   H N N 114 
GLN   HA   H N N 115 
GLN   HB2  H N N 116 
GLN   HB3  H N N 117 
GLN   HG2  H N N 118 
GLN   HG3  H N N 119 
GLN   HE21 H N N 120 
GLN   HE22 H N N 121 
GLN   HXT  H N N 122 
GLU   N    N N N 123 
GLU   CA   C N S 124 
GLU   C    C N N 125 
GLU   O    O N N 126 
GLU   CB   C N N 127 
GLU   CG   C N N 128 
GLU   CD   C N N 129 
GLU   OE1  O N N 130 
GLU   OE2  O N N 131 
GLU   OXT  O N N 132 
GLU   H    H N N 133 
GLU   H2   H N N 134 
GLU   HA   H N N 135 
GLU   HB2  H N N 136 
GLU   HB3  H N N 137 
GLU   HG2  H N N 138 
GLU   HG3  H N N 139 
GLU   HE2  H N N 140 
GLU   HXT  H N N 141 
GLY   N    N N N 142 
GLY   CA   C N N 143 
GLY   C    C N N 144 
GLY   O    O N N 145 
GLY   OXT  O N N 146 
GLY   H    H N N 147 
GLY   H2   H N N 148 
GLY   HA2  H N N 149 
GLY   HA3  H N N 150 
GLY   HXT  H N N 151 
HIS   N    N N N 152 
HIS   CA   C N S 153 
HIS   C    C N N 154 
HIS   O    O N N 155 
HIS   CB   C N N 156 
HIS   CG   C Y N 157 
HIS   ND1  N Y N 158 
HIS   CD2  C Y N 159 
HIS   CE1  C Y N 160 
HIS   NE2  N Y N 161 
HIS   OXT  O N N 162 
HIS   H    H N N 163 
HIS   H2   H N N 164 
HIS   HA   H N N 165 
HIS   HB2  H N N 166 
HIS   HB3  H N N 167 
HIS   HD1  H N N 168 
HIS   HD2  H N N 169 
HIS   HE1  H N N 170 
HIS   HE2  H N N 171 
HIS   HXT  H N N 172 
HOH   O    O N N 173 
HOH   H1   H N N 174 
HOH   H2   H N N 175 
ILE   N    N N N 176 
ILE   CA   C N S 177 
ILE   C    C N N 178 
ILE   O    O N N 179 
ILE   CB   C N S 180 
ILE   CG1  C N N 181 
ILE   CG2  C N N 182 
ILE   CD1  C N N 183 
ILE   OXT  O N N 184 
ILE   H    H N N 185 
ILE   H2   H N N 186 
ILE   HA   H N N 187 
ILE   HB   H N N 188 
ILE   HG12 H N N 189 
ILE   HG13 H N N 190 
ILE   HG21 H N N 191 
ILE   HG22 H N N 192 
ILE   HG23 H N N 193 
ILE   HD11 H N N 194 
ILE   HD12 H N N 195 
ILE   HD13 H N N 196 
ILE   HXT  H N N 197 
LEU   N    N N N 198 
LEU   CA   C N S 199 
LEU   C    C N N 200 
LEU   O    O N N 201 
LEU   CB   C N N 202 
LEU   CG   C N N 203 
LEU   CD1  C N N 204 
LEU   CD2  C N N 205 
LEU   OXT  O N N 206 
LEU   H    H N N 207 
LEU   H2   H N N 208 
LEU   HA   H N N 209 
LEU   HB2  H N N 210 
LEU   HB3  H N N 211 
LEU   HG   H N N 212 
LEU   HD11 H N N 213 
LEU   HD12 H N N 214 
LEU   HD13 H N N 215 
LEU   HD21 H N N 216 
LEU   HD22 H N N 217 
LEU   HD23 H N N 218 
LEU   HXT  H N N 219 
LYS   N    N N N 220 
LYS   CA   C N S 221 
LYS   C    C N N 222 
LYS   O    O N N 223 
LYS   CB   C N N 224 
LYS   CG   C N N 225 
LYS   CD   C N N 226 
LYS   CE   C N N 227 
LYS   NZ   N N N 228 
LYS   OXT  O N N 229 
LYS   H    H N N 230 
LYS   H2   H N N 231 
LYS   HA   H N N 232 
LYS   HB2  H N N 233 
LYS   HB3  H N N 234 
LYS   HG2  H N N 235 
LYS   HG3  H N N 236 
LYS   HD2  H N N 237 
LYS   HD3  H N N 238 
LYS   HE2  H N N 239 
LYS   HE3  H N N 240 
LYS   HZ1  H N N 241 
LYS   HZ2  H N N 242 
LYS   HZ3  H N N 243 
LYS   HXT  H N N 244 
MET   N    N N N 245 
MET   CA   C N S 246 
MET   C    C N N 247 
MET   O    O N N 248 
MET   CB   C N N 249 
MET   CG   C N N 250 
MET   SD   S N N 251 
MET   CE   C N N 252 
MET   OXT  O N N 253 
MET   H    H N N 254 
MET   H2   H N N 255 
MET   HA   H N N 256 
MET   HB2  H N N 257 
MET   HB3  H N N 258 
MET   HG2  H N N 259 
MET   HG3  H N N 260 
MET   HE1  H N N 261 
MET   HE2  H N N 262 
MET   HE3  H N N 263 
MET   HXT  H N N 264 
PHE   N    N N N 265 
PHE   CA   C N S 266 
PHE   C    C N N 267 
PHE   O    O N N 268 
PHE   CB   C N N 269 
PHE   CG   C Y N 270 
PHE   CD1  C Y N 271 
PHE   CD2  C Y N 272 
PHE   CE1  C Y N 273 
PHE   CE2  C Y N 274 
PHE   CZ   C Y N 275 
PHE   OXT  O N N 276 
PHE   H    H N N 277 
PHE   H2   H N N 278 
PHE   HA   H N N 279 
PHE   HB2  H N N 280 
PHE   HB3  H N N 281 
PHE   HD1  H N N 282 
PHE   HD2  H N N 283 
PHE   HE1  H N N 284 
PHE   HE2  H N N 285 
PHE   HZ   H N N 286 
PHE   HXT  H N N 287 
PRO   N    N N N 288 
PRO   CA   C N S 289 
PRO   C    C N N 290 
PRO   O    O N N 291 
PRO   CB   C N N 292 
PRO   CG   C N N 293 
PRO   CD   C N N 294 
PRO   OXT  O N N 295 
PRO   H    H N N 296 
PRO   HA   H N N 297 
PRO   HB2  H N N 298 
PRO   HB3  H N N 299 
PRO   HG2  H N N 300 
PRO   HG3  H N N 301 
PRO   HD2  H N N 302 
PRO   HD3  H N N 303 
PRO   HXT  H N N 304 
SER   N    N N N 305 
SER   CA   C N S 306 
SER   C    C N N 307 
SER   O    O N N 308 
SER   CB   C N N 309 
SER   OG   O N N 310 
SER   OXT  O N N 311 
SER   H    H N N 312 
SER   H2   H N N 313 
SER   HA   H N N 314 
SER   HB2  H N N 315 
SER   HB3  H N N 316 
SER   HG   H N N 317 
SER   HXT  H N N 318 
THR   N    N N N 319 
THR   CA   C N S 320 
THR   C    C N N 321 
THR   O    O N N 322 
THR   CB   C N R 323 
THR   OG1  O N N 324 
THR   CG2  C N N 325 
THR   OXT  O N N 326 
THR   H    H N N 327 
THR   H2   H N N 328 
THR   HA   H N N 329 
THR   HB   H N N 330 
THR   HG1  H N N 331 
THR   HG21 H N N 332 
THR   HG22 H N N 333 
THR   HG23 H N N 334 
THR   HXT  H N N 335 
TRP   N    N N N 336 
TRP   CA   C N S 337 
TRP   C    C N N 338 
TRP   O    O N N 339 
TRP   CB   C N N 340 
TRP   CG   C Y N 341 
TRP   CD1  C Y N 342 
TRP   CD2  C Y N 343 
TRP   NE1  N Y N 344 
TRP   CE2  C Y N 345 
TRP   CE3  C Y N 346 
TRP   CZ2  C Y N 347 
TRP   CZ3  C Y N 348 
TRP   CH2  C Y N 349 
TRP   OXT  O N N 350 
TRP   H    H N N 351 
TRP   H2   H N N 352 
TRP   HA   H N N 353 
TRP   HB2  H N N 354 
TRP   HB3  H N N 355 
TRP   HD1  H N N 356 
TRP   HE1  H N N 357 
TRP   HE3  H N N 358 
TRP   HZ2  H N N 359 
TRP   HZ3  H N N 360 
TRP   HH2  H N N 361 
TRP   HXT  H N N 362 
TYR   N    N N N 363 
TYR   CA   C N S 364 
TYR   C    C N N 365 
TYR   O    O N N 366 
TYR   CB   C N N 367 
TYR   CG   C Y N 368 
TYR   CD1  C Y N 369 
TYR   CD2  C Y N 370 
TYR   CE1  C Y N 371 
TYR   CE2  C Y N 372 
TYR   CZ   C Y N 373 
TYR   OH   O N N 374 
TYR   OXT  O N N 375 
TYR   H    H N N 376 
TYR   H2   H N N 377 
TYR   HA   H N N 378 
TYR   HB2  H N N 379 
TYR   HB3  H N N 380 
TYR   HD1  H N N 381 
TYR   HD2  H N N 382 
TYR   HE1  H N N 383 
TYR   HE2  H N N 384 
TYR   HH   H N N 385 
TYR   HXT  H N N 386 
VAL   N    N N N 387 
VAL   CA   C N S 388 
VAL   C    C N N 389 
VAL   O    O N N 390 
VAL   CB   C N N 391 
VAL   CG1  C N N 392 
VAL   CG2  C N N 393 
VAL   OXT  O N N 394 
VAL   H    H N N 395 
VAL   H2   H N N 396 
VAL   HA   H N N 397 
VAL   HB   H N N 398 
VAL   HG11 H N N 399 
VAL   HG12 H N N 400 
VAL   HG13 H N N 401 
VAL   HG21 H N N 402 
VAL   HG22 H N N 403 
VAL   HG23 H N N 404 
VAL   HXT  H N N 405 
# 
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 
A1IUW C   C1   sing N N 1   
A1IUW C1  C2   sing N N 2   
A1IUW C2  C3   sing N N 3   
A1IUW C3  C4   doub Y N 4   
A1IUW C5  C4   sing N N 5   
A1IUW C5  C6   doub Y N 6   
A1IUW C6  C7   sing Y N 7   
A1IUW C7  C8   doub Y N 8   
A1IUW C8  C9   sing Y N 9   
A1IUW C9  C10  doub Y N 10  
A1IUW C10 C5   sing Y N 11  
A1IUW C11 C8   sing N N 12  
A1IUW O   C11  doub N N 13  
A1IUW N   C11  sing N N 14  
A1IUW C12 C6   sing N N 15  
A1IUW C4  N1   sing Y N 16  
A1IUW N1  C13  sing Y N 17  
A1IUW C13 C14  doub Y N 18  
A1IUW C3  C14  sing Y N 19  
A1IUW C14 C15  sing N N 20  
A1IUW C16 C15  sing N N 21  
A1IUW C   C16  sing N N 22  
A1IUW C15 O1   doub N N 23  
A1IUW C17 C13  sing N N 24  
A1IUW N1  HN1  sing N N 25  
A1IUW C7  H8   sing N N 26  
A1IUW C10 H10  sing N N 27  
A1IUW N   H    sing N N 28  
A1IUW N   H1   sing N N 29  
A1IUW C   H3   sing N N 30  
A1IUW C   H2   sing N N 31  
A1IUW C1  H4   sing N N 32  
A1IUW C1  H5   sing N N 33  
A1IUW C12 H11  sing N N 34  
A1IUW C12 H13  sing N N 35  
A1IUW C12 H12  sing N N 36  
A1IUW C2  H6   sing N N 37  
A1IUW C2  H7   sing N N 38  
A1IUW C9  H9   sing N N 39  
A1IUW C16 H14  sing N N 40  
A1IUW C16 H15  sing N N 41  
A1IUW C17 H17  sing N N 42  
A1IUW C17 H18  sing N N 43  
A1IUW C17 H16  sing N N 44  
ALA   N   CA   sing N N 45  
ALA   N   H    sing N N 46  
ALA   N   H2   sing N N 47  
ALA   CA  C    sing N N 48  
ALA   CA  CB   sing N N 49  
ALA   CA  HA   sing N N 50  
ALA   C   O    doub N N 51  
ALA   C   OXT  sing N N 52  
ALA   CB  HB1  sing N N 53  
ALA   CB  HB2  sing N N 54  
ALA   CB  HB3  sing N N 55  
ALA   OXT HXT  sing N N 56  
ASN   N   CA   sing N N 57  
ASN   N   H    sing N N 58  
ASN   N   H2   sing N N 59  
ASN   CA  C    sing N N 60  
ASN   CA  CB   sing N N 61  
ASN   CA  HA   sing N N 62  
ASN   C   O    doub N N 63  
ASN   C   OXT  sing N N 64  
ASN   CB  CG   sing N N 65  
ASN   CB  HB2  sing N N 66  
ASN   CB  HB3  sing N N 67  
ASN   CG  OD1  doub N N 68  
ASN   CG  ND2  sing N N 69  
ASN   ND2 HD21 sing N N 70  
ASN   ND2 HD22 sing N N 71  
ASN   OXT HXT  sing N N 72  
ASP   N   CA   sing N N 73  
ASP   N   H    sing N N 74  
ASP   N   H2   sing N N 75  
ASP   CA  C    sing N N 76  
ASP   CA  CB   sing N N 77  
ASP   CA  HA   sing N N 78  
ASP   C   O    doub N N 79  
ASP   C   OXT  sing N N 80  
ASP   CB  CG   sing N N 81  
ASP   CB  HB2  sing N N 82  
ASP   CB  HB3  sing N N 83  
ASP   CG  OD1  doub N N 84  
ASP   CG  OD2  sing N N 85  
ASP   OD2 HD2  sing N N 86  
ASP   OXT HXT  sing N N 87  
CYS   N   CA   sing N N 88  
CYS   N   H    sing N N 89  
CYS   N   H2   sing N N 90  
CYS   CA  C    sing N N 91  
CYS   CA  CB   sing N N 92  
CYS   CA  HA   sing N N 93  
CYS   C   O    doub N N 94  
CYS   C   OXT  sing N N 95  
CYS   CB  SG   sing N N 96  
CYS   CB  HB2  sing N N 97  
CYS   CB  HB3  sing N N 98  
CYS   SG  HG   sing N N 99  
CYS   OXT HXT  sing N N 100 
GLN   N   CA   sing N N 101 
GLN   N   H    sing N N 102 
GLN   N   H2   sing N N 103 
GLN   CA  C    sing N N 104 
GLN   CA  CB   sing N N 105 
GLN   CA  HA   sing N N 106 
GLN   C   O    doub N N 107 
GLN   C   OXT  sing N N 108 
GLN   CB  CG   sing N N 109 
GLN   CB  HB2  sing N N 110 
GLN   CB  HB3  sing N N 111 
GLN   CG  CD   sing N N 112 
GLN   CG  HG2  sing N N 113 
GLN   CG  HG3  sing N N 114 
GLN   CD  OE1  doub N N 115 
GLN   CD  NE2  sing N N 116 
GLN   NE2 HE21 sing N N 117 
GLN   NE2 HE22 sing N N 118 
GLN   OXT HXT  sing N N 119 
GLU   N   CA   sing N N 120 
GLU   N   H    sing N N 121 
GLU   N   H2   sing N N 122 
GLU   CA  C    sing N N 123 
GLU   CA  CB   sing N N 124 
GLU   CA  HA   sing N N 125 
GLU   C   O    doub N N 126 
GLU   C   OXT  sing N N 127 
GLU   CB  CG   sing N N 128 
GLU   CB  HB2  sing N N 129 
GLU   CB  HB3  sing N N 130 
GLU   CG  CD   sing N N 131 
GLU   CG  HG2  sing N N 132 
GLU   CG  HG3  sing N N 133 
GLU   CD  OE1  doub N N 134 
GLU   CD  OE2  sing N N 135 
GLU   OE2 HE2  sing N N 136 
GLU   OXT HXT  sing N N 137 
GLY   N   CA   sing N N 138 
GLY   N   H    sing N N 139 
GLY   N   H2   sing N N 140 
GLY   CA  C    sing N N 141 
GLY   CA  HA2  sing N N 142 
GLY   CA  HA3  sing N N 143 
GLY   C   O    doub N N 144 
GLY   C   OXT  sing N N 145 
GLY   OXT HXT  sing N N 146 
HIS   N   CA   sing N N 147 
HIS   N   H    sing N N 148 
HIS   N   H2   sing N N 149 
HIS   CA  C    sing N N 150 
HIS   CA  CB   sing N N 151 
HIS   CA  HA   sing N N 152 
HIS   C   O    doub N N 153 
HIS   C   OXT  sing N N 154 
HIS   CB  CG   sing N N 155 
HIS   CB  HB2  sing N N 156 
HIS   CB  HB3  sing N N 157 
HIS   CG  ND1  sing Y N 158 
HIS   CG  CD2  doub Y N 159 
HIS   ND1 CE1  doub Y N 160 
HIS   ND1 HD1  sing N N 161 
HIS   CD2 NE2  sing Y N 162 
HIS   CD2 HD2  sing N N 163 
HIS   CE1 NE2  sing Y N 164 
HIS   CE1 HE1  sing N N 165 
HIS   NE2 HE2  sing N N 166 
HIS   OXT HXT  sing N N 167 
HOH   O   H1   sing N N 168 
HOH   O   H2   sing N N 169 
ILE   N   CA   sing N N 170 
ILE   N   H    sing N N 171 
ILE   N   H2   sing N N 172 
ILE   CA  C    sing N N 173 
ILE   CA  CB   sing N N 174 
ILE   CA  HA   sing N N 175 
ILE   C   O    doub N N 176 
ILE   C   OXT  sing N N 177 
ILE   CB  CG1  sing N N 178 
ILE   CB  CG2  sing N N 179 
ILE   CB  HB   sing N N 180 
ILE   CG1 CD1  sing N N 181 
ILE   CG1 HG12 sing N N 182 
ILE   CG1 HG13 sing N N 183 
ILE   CG2 HG21 sing N N 184 
ILE   CG2 HG22 sing N N 185 
ILE   CG2 HG23 sing N N 186 
ILE   CD1 HD11 sing N N 187 
ILE   CD1 HD12 sing N N 188 
ILE   CD1 HD13 sing N N 189 
ILE   OXT HXT  sing N N 190 
LEU   N   CA   sing N N 191 
LEU   N   H    sing N N 192 
LEU   N   H2   sing N N 193 
LEU   CA  C    sing N N 194 
LEU   CA  CB   sing N N 195 
LEU   CA  HA   sing N N 196 
LEU   C   O    doub N N 197 
LEU   C   OXT  sing N N 198 
LEU   CB  CG   sing N N 199 
LEU   CB  HB2  sing N N 200 
LEU   CB  HB3  sing N N 201 
LEU   CG  CD1  sing N N 202 
LEU   CG  CD2  sing N N 203 
LEU   CG  HG   sing N N 204 
LEU   CD1 HD11 sing N N 205 
LEU   CD1 HD12 sing N N 206 
LEU   CD1 HD13 sing N N 207 
LEU   CD2 HD21 sing N N 208 
LEU   CD2 HD22 sing N N 209 
LEU   CD2 HD23 sing N N 210 
LEU   OXT HXT  sing N N 211 
LYS   N   CA   sing N N 212 
LYS   N   H    sing N N 213 
LYS   N   H2   sing N N 214 
LYS   CA  C    sing N N 215 
LYS   CA  CB   sing N N 216 
LYS   CA  HA   sing N N 217 
LYS   C   O    doub N N 218 
LYS   C   OXT  sing N N 219 
LYS   CB  CG   sing N N 220 
LYS   CB  HB2  sing N N 221 
LYS   CB  HB3  sing N N 222 
LYS   CG  CD   sing N N 223 
LYS   CG  HG2  sing N N 224 
LYS   CG  HG3  sing N N 225 
LYS   CD  CE   sing N N 226 
LYS   CD  HD2  sing N N 227 
LYS   CD  HD3  sing N N 228 
LYS   CE  NZ   sing N N 229 
LYS   CE  HE2  sing N N 230 
LYS   CE  HE3  sing N N 231 
LYS   NZ  HZ1  sing N N 232 
LYS   NZ  HZ2  sing N N 233 
LYS   NZ  HZ3  sing N N 234 
LYS   OXT HXT  sing N N 235 
MET   N   CA   sing N N 236 
MET   N   H    sing N N 237 
MET   N   H2   sing N N 238 
MET   CA  C    sing N N 239 
MET   CA  CB   sing N N 240 
MET   CA  HA   sing N N 241 
MET   C   O    doub N N 242 
MET   C   OXT  sing N N 243 
MET   CB  CG   sing N N 244 
MET   CB  HB2  sing N N 245 
MET   CB  HB3  sing N N 246 
MET   CG  SD   sing N N 247 
MET   CG  HG2  sing N N 248 
MET   CG  HG3  sing N N 249 
MET   SD  CE   sing N N 250 
MET   CE  HE1  sing N N 251 
MET   CE  HE2  sing N N 252 
MET   CE  HE3  sing N N 253 
MET   OXT HXT  sing N N 254 
PHE   N   CA   sing N N 255 
PHE   N   H    sing N N 256 
PHE   N   H2   sing N N 257 
PHE   CA  C    sing N N 258 
PHE   CA  CB   sing N N 259 
PHE   CA  HA   sing N N 260 
PHE   C   O    doub N N 261 
PHE   C   OXT  sing N N 262 
PHE   CB  CG   sing N N 263 
PHE   CB  HB2  sing N N 264 
PHE   CB  HB3  sing N N 265 
PHE   CG  CD1  doub Y N 266 
PHE   CG  CD2  sing Y N 267 
PHE   CD1 CE1  sing Y N 268 
PHE   CD1 HD1  sing N N 269 
PHE   CD2 CE2  doub Y N 270 
PHE   CD2 HD2  sing N N 271 
PHE   CE1 CZ   doub Y N 272 
PHE   CE1 HE1  sing N N 273 
PHE   CE2 CZ   sing Y N 274 
PHE   CE2 HE2  sing N N 275 
PHE   CZ  HZ   sing N N 276 
PHE   OXT HXT  sing N N 277 
PRO   N   CA   sing N N 278 
PRO   N   CD   sing N N 279 
PRO   N   H    sing N N 280 
PRO   CA  C    sing N N 281 
PRO   CA  CB   sing N N 282 
PRO   CA  HA   sing N N 283 
PRO   C   O    doub N N 284 
PRO   C   OXT  sing N N 285 
PRO   CB  CG   sing N N 286 
PRO   CB  HB2  sing N N 287 
PRO   CB  HB3  sing N N 288 
PRO   CG  CD   sing N N 289 
PRO   CG  HG2  sing N N 290 
PRO   CG  HG3  sing N N 291 
PRO   CD  HD2  sing N N 292 
PRO   CD  HD3  sing N N 293 
PRO   OXT HXT  sing N N 294 
SER   N   CA   sing N N 295 
SER   N   H    sing N N 296 
SER   N   H2   sing N N 297 
SER   CA  C    sing N N 298 
SER   CA  CB   sing N N 299 
SER   CA  HA   sing N N 300 
SER   C   O    doub N N 301 
SER   C   OXT  sing N N 302 
SER   CB  OG   sing N N 303 
SER   CB  HB2  sing N N 304 
SER   CB  HB3  sing N N 305 
SER   OG  HG   sing N N 306 
SER   OXT HXT  sing N N 307 
THR   N   CA   sing N N 308 
THR   N   H    sing N N 309 
THR   N   H2   sing N N 310 
THR   CA  C    sing N N 311 
THR   CA  CB   sing N N 312 
THR   CA  HA   sing N N 313 
THR   C   O    doub N N 314 
THR   C   OXT  sing N N 315 
THR   CB  OG1  sing N N 316 
THR   CB  CG2  sing N N 317 
THR   CB  HB   sing N N 318 
THR   OG1 HG1  sing N N 319 
THR   CG2 HG21 sing N N 320 
THR   CG2 HG22 sing N N 321 
THR   CG2 HG23 sing N N 322 
THR   OXT HXT  sing N N 323 
TRP   N   CA   sing N N 324 
TRP   N   H    sing N N 325 
TRP   N   H2   sing N N 326 
TRP   CA  C    sing N N 327 
TRP   CA  CB   sing N N 328 
TRP   CA  HA   sing N N 329 
TRP   C   O    doub N N 330 
TRP   C   OXT  sing N N 331 
TRP   CB  CG   sing N N 332 
TRP   CB  HB2  sing N N 333 
TRP   CB  HB3  sing N N 334 
TRP   CG  CD1  doub Y N 335 
TRP   CG  CD2  sing Y N 336 
TRP   CD1 NE1  sing Y N 337 
TRP   CD1 HD1  sing N N 338 
TRP   CD2 CE2  doub Y N 339 
TRP   CD2 CE3  sing Y N 340 
TRP   NE1 CE2  sing Y N 341 
TRP   NE1 HE1  sing N N 342 
TRP   CE2 CZ2  sing Y N 343 
TRP   CE3 CZ3  doub Y N 344 
TRP   CE3 HE3  sing N N 345 
TRP   CZ2 CH2  doub Y N 346 
TRP   CZ2 HZ2  sing N N 347 
TRP   CZ3 CH2  sing Y N 348 
TRP   CZ3 HZ3  sing N N 349 
TRP   CH2 HH2  sing N N 350 
TRP   OXT HXT  sing N N 351 
TYR   N   CA   sing N N 352 
TYR   N   H    sing N N 353 
TYR   N   H2   sing N N 354 
TYR   CA  C    sing N N 355 
TYR   CA  CB   sing N N 356 
TYR   CA  HA   sing N N 357 
TYR   C   O    doub N N 358 
TYR   C   OXT  sing N N 359 
TYR   CB  CG   sing N N 360 
TYR   CB  HB2  sing N N 361 
TYR   CB  HB3  sing N N 362 
TYR   CG  CD1  doub Y N 363 
TYR   CG  CD2  sing Y N 364 
TYR   CD1 CE1  sing Y N 365 
TYR   CD1 HD1  sing N N 366 
TYR   CD2 CE2  doub Y N 367 
TYR   CD2 HD2  sing N N 368 
TYR   CE1 CZ   doub Y N 369 
TYR   CE1 HE1  sing N N 370 
TYR   CE2 CZ   sing Y N 371 
TYR   CE2 HE2  sing N N 372 
TYR   CZ  OH   sing N N 373 
TYR   OH  HH   sing N N 374 
TYR   OXT HXT  sing N N 375 
VAL   N   CA   sing N N 376 
VAL   N   H    sing N N 377 
VAL   N   H2   sing N N 378 
VAL   CA  C    sing N N 379 
VAL   CA  CB   sing N N 380 
VAL   CA  HA   sing N N 381 
VAL   C   O    doub N N 382 
VAL   C   OXT  sing N N 383 
VAL   CB  CG1  sing N N 384 
VAL   CB  CG2  sing N N 385 
VAL   CB  HB   sing N N 386 
VAL   CG1 HG11 sing N N 387 
VAL   CG1 HG12 sing N N 388 
VAL   CG1 HG13 sing N N 389 
VAL   CG2 HG21 sing N N 390 
VAL   CG2 HG22 sing N N 391 
VAL   CG2 HG23 sing N N 392 
VAL   OXT HXT  sing N N 393 
# 
_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                    9HH7 
_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]   0.026233 
_atom_sites.fract_transf_matrix[1][2]   0.000000 
_atom_sites.fract_transf_matrix[1][3]   0.000000 
_atom_sites.fract_transf_matrix[2][1]   0.000000 
_atom_sites.fract_transf_matrix[2][2]   0.011336 
_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]   0.009217 
_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   . LEU   A 1 3   ? 29.95772  28.45781 7.51393   1.000 78.26141  ? 3   LEU   A N   1 
ATOM   2    C CA  . LEU   A 1 3   ? 29.24806  28.30256 8.77885   1.000 81.99584  ? 3   LEU   A CA  1 
ATOM   3    C C   . LEU   A 1 3   ? 27.95785  29.11954 8.77986   1.000 107.22856 ? 3   LEU   A C   1 
ATOM   4    O O   . LEU   A 1 3   ? 26.99164  28.77404 9.45884   1.000 115.65801 ? 3   LEU   A O   1 
ATOM   5    C CB  . LEU   A 1 3   ? 30.14458  28.71308 9.95060   1.000 91.68857  ? 3   LEU   A CB  1 
ATOM   6    C CG  . LEU   A 1 3   ? 29.57375  28.54602 11.36175  1.000 73.51513  ? 3   LEU   A CG  1 
ATOM   7    C CD1 . LEU   A 1 3   ? 30.54235  27.78515 12.25253  1.000 71.55069  ? 3   LEU   A CD1 1 
ATOM   8    C CD2 . LEU   A 1 3   ? 29.24224  29.90007 11.96906  1.000 83.94353  ? 3   LEU   A CD2 1 
ATOM   9    N N   . GLY   A 1 4   ? 27.95069  30.20827 8.01687   1.000 105.98981 ? 4   GLY   A N   1 
ATOM   10   C CA  . GLY   A 1 4   ? 26.77653  31.03619 7.84120   1.000 109.77176 ? 4   GLY   A CA  1 
ATOM   11   C C   . GLY   A 1 4   ? 26.07023  30.84967 6.51749   1.000 97.12408  ? 4   GLY   A C   1 
ATOM   12   O O   . GLY   A 1 4   ? 25.17359  31.63824 6.19352   1.000 85.22028  ? 4   GLY   A O   1 
ATOM   13   N N   . SER   A 1 5   ? 26.44251  29.82789 5.74435   1.000 86.38147  ? 5   SER   A N   1 
ATOM   14   C CA  . SER   A 1 5   ? 25.87232  29.60863 4.42863   1.000 94.42252  ? 5   SER   A CA  1 
ATOM   15   C C   . SER   A 1 5   ? 24.37469  29.32938 4.53331   1.000 77.32144  ? 5   SER   A C   1 
ATOM   16   O O   . SER   A 1 5   ? 23.88053  28.92328 5.58848   1.000 72.80390  ? 5   SER   A O   1 
ATOM   17   C CB  . SER   A 1 5   ? 26.58116  28.44165 3.74035   1.000 100.23549 ? 5   SER   A CB  1 
ATOM   18   O OG  . SER   A 1 5   ? 27.95880  28.72041 3.55327   1.000 97.07900  ? 5   SER   A OG  1 
ATOM   19   N N   . PRO   A 1 6   ? 23.62614  29.55937 3.45051   1.000 75.45404  ? 6   PRO   A N   1 
ATOM   20   C CA  . PRO   A 1 6   ? 22.20798  29.16826 3.45900   1.000 69.57203  ? 6   PRO   A CA  1 
ATOM   21   C C   . PRO   A 1 6   ? 22.00379  27.68488 3.70315   1.000 75.42559  ? 6   PRO   A C   1 
ATOM   22   O O   . PRO   A 1 6   ? 20.96069  27.29241 4.23992   1.000 82.29550  ? 6   PRO   A O   1 
ATOM   23   C CB  . PRO   A 1 6   ? 21.71991  29.58631 2.06462   1.000 71.13638  ? 6   PRO   A CB  1 
ATOM   24   C CG  . PRO   A 1 6   ? 22.66138  30.65794 1.63800   1.000 80.45146  ? 6   PRO   A CG  1 
ATOM   25   C CD  . PRO   A 1 6   ? 23.99188  30.29205 2.22565   1.000 73.07514  ? 6   PRO   A CD  1 
ATOM   26   N N   . GLU   A 1 7   ? 22.97360  26.84626 3.32850   1.000 84.17996  ? 7   GLU   A N   1 
ATOM   27   C CA  . GLU   A 1 7   ? 22.85269  25.41528 3.58650   1.000 76.11336  ? 7   GLU   A CA  1 
ATOM   28   C C   . GLU   A 1 7   ? 23.01068  25.10738 5.07021   1.000 89.93614  ? 7   GLU   A C   1 
ATOM   29   O O   . GLU   A 1 7   ? 22.33759  24.21415 5.59684   1.000 102.30575 ? 7   GLU   A O   1 
ATOM   30   C CB  . GLU   A 1 7   ? 23.88029  24.64134 2.75908   1.000 84.48349  ? 7   GLU   A CB  1 
ATOM   31   C CG  . GLU   A 1 7   ? 25.32735  25.04314 3.01091   1.000 93.07027  ? 7   GLU   A CG  1 
ATOM   32   C CD  . GLU   A 1 7   ? 26.10229  23.99235 3.78594   1.000 124.09340 ? 7   GLU   A CD  1 
ATOM   33   O OE1 . GLU   A 1 7   ? 25.52707  22.92295 4.08347   1.000 100.93821 ? 7   GLU   A OE1 1 
ATOM   34   O OE2 . GLU   A 1 7   ? 27.28892  24.23444 4.09476   1.000 103.30618 ? 7   GLU   A OE2 1 
ATOM   35   N N   . PHE   A 1 8   ? 23.89251  25.83590 5.76253   1.000 69.99393  ? 8   PHE   A N   1 
ATOM   36   C CA  . PHE   A 1 8   ? 24.04644  25.62845 7.19869   1.000 69.66179  ? 8   PHE   A CA  1 
ATOM   37   C C   . PHE   A 1 8   ? 22.76156  25.98047 7.93669   1.000 69.56511  ? 8   PHE   A C   1 
ATOM   38   O O   . PHE   A 1 8   ? 22.34661  25.26285 8.85435   1.000 66.88742  ? 8   PHE   A O   1 
ATOM   39   C CB  . PHE   A 1 8   ? 25.22077  26.45246 7.73055   1.000 59.22269  ? 8   PHE   A CB  1 
ATOM   40   C CG  . PHE   A 1 8   ? 25.71549  26.00806 9.08308   1.000 62.31457  ? 8   PHE   A CG  1 
ATOM   41   C CD1 . PHE   A 1 8   ? 25.09702  26.44556 10.24410  1.000 57.15997  ? 8   PHE   A CD1 1 
ATOM   42   C CD2 . PHE   A 1 8   ? 26.80453  25.15727 9.19183   1.000 73.34986  ? 8   PHE   A CD2 1 
ATOM   43   C CE1 . PHE   A 1 8   ? 25.55212  26.03953 11.48647  1.000 70.46582  ? 8   PHE   A CE1 1 
ATOM   44   C CE2 . PHE   A 1 8   ? 27.26409  24.74842 10.43236  1.000 70.58452  ? 8   PHE   A CE2 1 
ATOM   45   C CZ  . PHE   A 1 8   ? 26.63633  25.19042 11.57998  1.000 96.84380  ? 8   PHE   A CZ  1 
ATOM   46   N N   . MET   A 1 9   ? 22.11038  27.07756 7.54165   1.000 61.26578  ? 9   MET   A N   1 
ATOM   47   C CA  . MET   A 1 9   ? 20.82457  27.41940 8.13839   1.000 63.29809  ? 9   MET   A CA  1 
ATOM   48   C C   . MET   A 1 9   ? 19.75428  26.40535 7.75802   1.000 59.63512  ? 9   MET   A C   1 
ATOM   49   O O   . MET   A 1 9   ? 18.92439  26.03145 8.59482   1.000 59.82004  ? 9   MET   A O   1 
ATOM   50   C CB  . MET   A 1 9   ? 20.39860  28.82522 7.71945   1.000 63.86671  ? 9   MET   A CB  1 
ATOM   51   C CG  . MET   A 1 9   ? 21.31175  29.93083 8.21223   1.000 72.20818  ? 9   MET   A CG  1 
ATOM   52   S SD  . MET   A 1 9   ? 20.52856  31.54408 8.04572   1.000 100.59790 ? 9   MET   A SD  1 
ATOM   53   C CE  . MET   A 1 9   ? 20.01187  31.48934 6.33065   1.000 76.17503  ? 9   MET   A CE  1 
ATOM   54   N N   A ASN   A 1 10  ? 19.75270  25.95100 6.50159   0.503 59.83158  ? 10  ASN   A N   1 
ATOM   55   N N   B ASN   A 1 10  ? 19.75739  25.94944 6.50112   0.497 59.83040  ? 10  ASN   A N   1 
ATOM   56   C CA  A ASN   A 1 10  ? 18.76859  24.95913 6.08088   0.503 58.14169  ? 10  ASN   A CA  1 
ATOM   57   C CA  B ASN   A 1 10  ? 18.77864  24.95379 6.07327   0.497 58.14009  ? 10  ASN   A CA  1 
ATOM   58   C C   A ASN   A 1 10  ? 18.95876  23.63477 6.80906   0.503 57.44613  ? 10  ASN   A C   1 
ATOM   59   C C   B ASN   A 1 10  ? 18.95598  23.64661 6.83381   0.497 57.43190  ? 10  ASN   A C   1 
ATOM   60   O O   A ASN   A 1 10  ? 17.97678  22.93659 7.08613   0.503 53.68782  ? 10  ASN   A O   1 
ATOM   61   O O   B ASN   A 1 10  ? 17.97324  22.96906 7.15745   0.497 53.51569  ? 10  ASN   A O   1 
ATOM   62   C CB  A ASN   A 1 10  ? 18.83785  24.75673 4.56749   0.503 57.79040  ? 10  ASN   A CB  1 
ATOM   63   C CB  B ASN   A 1 10  ? 18.88612  24.71790 4.56606   0.497 57.81618  ? 10  ASN   A CB  1 
ATOM   64   C CG  A ASN   A 1 10  ? 18.29890  25.94771 3.79515   0.503 56.59397  ? 10  ASN   A CG  1 
ATOM   65   C CG  B ASN   A 1 10  ? 17.92047  23.65466 4.07048   0.497 55.60936  ? 10  ASN   A CG  1 
ATOM   66   O OD1 A ASN   A 1 10  ? 17.24828  26.49649 4.12981   0.503 46.34876  ? 10  ASN   A OD1 1 
ATOM   67   O OD1 B ASN   A 1 10  ? 16.72171  23.90172 3.93807   0.497 55.18337  ? 10  ASN   A OD1 1 
ATOM   68   N ND2 A ASN   A 1 10  ? 19.02206  26.35725 2.75928   0.503 64.35315  ? 10  ASN   A ND2 1 
ATOM   69   N ND2 B ASN   A 1 10  ? 18.44199  22.46636 3.78626   0.497 54.72009  ? 10  ASN   A ND2 1 
ATOM   70   N N   . LYS   A 1 11  ? 20.20328  23.27519 7.13083   1.000 56.67361  ? 11  LYS   A N   1 
ATOM   71   C CA  . LYS   A 1 11  ? 20.43547  22.08441 7.93825   1.000 50.55119  ? 11  LYS   A CA  1 
ATOM   72   C C   . LYS   A 1 11  ? 20.03874  22.31821 9.39126   1.000 51.72225  ? 11  LYS   A C   1 
ATOM   73   O O   . LYS   A 1 11  ? 19.64342  21.37393 10.08420  1.000 52.34686  ? 11  LYS   A O   1 
ATOM   74   C CB  . LYS   A 1 11  ? 21.90222  21.65545 7.84398   1.000 47.40321  ? 11  LYS   A CB  1 
ATOM   75   C CG  . LYS   A 1 11  ? 22.20584  20.60808 6.76803   1.000 56.15872  ? 11  LYS   A CG  1 
ATOM   76   C CD  . LYS   A 1 11  ? 21.94776  21.12680 5.35952   1.000 67.86143  ? 11  LYS   A CD  1 
ATOM   77   C CE  . LYS   A 1 11  ? 22.44784  20.15309 4.30336   1.000 70.34904  ? 11  LYS   A CE  1 
ATOM   78   N NZ  . LYS   A 1 11  ? 21.80511  18.81754 4.43590   1.000 77.44916  ? 11  LYS   A NZ  1 
ATOM   79   N N   . GLN   A 1 12  ? 20.11790  23.56579 9.86169   1.000 54.54221  ? 12  GLN   A N   1 
ATOM   80   C CA  . GLN   A 1 12  ? 19.79739  23.86556 11.25487  1.000 61.87920  ? 12  GLN   A CA  1 
ATOM   81   C C   . GLN   A 1 12  ? 18.31260  23.67096 11.53985  1.000 41.70505  ? 12  GLN   A C   1 
ATOM   82   O O   . GLN   A 1 12  ? 17.93518  22.88021 12.41243  1.000 49.65064  ? 12  GLN   A O   1 
ATOM   83   C CB  . GLN   A 1 12  ? 20.23061  25.29145 11.59926  1.000 45.10762  ? 12  GLN   A CB  1 
ATOM   84   C CG  . GLN   A 1 12  ? 21.68525  25.40853 12.01144  1.000 55.04740  ? 12  GLN   A CG  1 
ATOM   85   C CD  . GLN   A 1 12  ? 22.09975  26.83773 12.28980  1.000 54.08814  ? 12  GLN   A CD  1 
ATOM   86   O OE1 . GLN   A 1 12  ? 21.78420  27.74907 11.52400  1.000 63.58049  ? 12  GLN   A OE1 1 
ATOM   87   N NE2 . GLN   A 1 12  ? 22.81086  27.04243 13.39284  1.000 55.45722  ? 12  GLN   A NE2 1 
ATOM   88   N N   . TRP   A 1 13  ? 17.44811  24.38848 10.81474  1.000 39.42303  ? 13  TRP   A N   1 
ATOM   89   C CA  . TRP   A 1 13  ? 16.02084  24.29856 11.09954  1.000 47.24849  ? 13  TRP   A CA  1 
ATOM   90   C C   . TRP   A 1 13  ? 15.43596  22.94461 10.71577  1.000 44.74206  ? 13  TRP   A C   1 
ATOM   91   O O   . TRP   A 1 13  ? 14.35088  22.59976 11.19355  1.000 51.04885  ? 13  TRP   A O   1 
ATOM   92   C CB  . TRP   A 1 13  ? 15.25350  25.43724 10.41265  1.000 42.46294  ? 13  TRP   A CB  1 
ATOM   93   C CG  . TRP   A 1 13  ? 15.19256  25.39948 8.90772   1.000 48.11688  ? 13  TRP   A CG  1 
ATOM   94   C CD1 . TRP   A 1 13  ? 15.99089  26.08420 8.03850   1.000 47.56986  ? 13  TRP   A CD1 1 
ATOM   95   C CD2 . TRP   A 1 13  ? 14.25489  24.67304 8.10073   1.000 46.16605  ? 13  TRP   A CD2 1 
ATOM   96   N NE1 . TRP   A 1 13  ? 15.62237  25.81526 6.74241   1.000 50.31077  ? 13  TRP   A NE1 1 
ATOM   97   C CE2 . TRP   A 1 13  ? 14.55965  24.95127 6.75312   1.000 50.19403  ? 13  TRP   A CE2 1 
ATOM   98   C CE3 . TRP   A 1 13  ? 13.19583  23.80612 8.38697   1.000 47.48075  ? 13  TRP   A CE3 1 
ATOM   99   C CZ2 . TRP   A 1 13  ? 13.84394  24.39441 5.69498   1.000 49.02350  ? 13  TRP   A CZ2 1 
ATOM   100  C CZ3 . TRP   A 1 13  ? 12.48611  23.25552 7.33528   1.000 50.88968  ? 13  TRP   A CZ3 1 
ATOM   101  C CH2 . TRP   A 1 13  ? 12.81287  23.55190 6.00680   1.000 46.28391  ? 13  TRP   A CH2 1 
ATOM   102  N N   . TYR   A 1 14  ? 16.12495  22.16669 9.87586   1.000 38.96553  ? 14  TYR   A N   1 
ATOM   103  C CA  . TYR   A 1 14  ? 15.71994  20.77721 9.68449   1.000 39.55838  ? 14  TYR   A CA  1 
ATOM   104  C C   . TYR   A 1 14  ? 15.98719  19.96028 10.94153  1.000 45.74146  ? 14  TYR   A C   1 
ATOM   105  O O   . TYR   A 1 14  ? 15.19885  19.07573 11.29478  1.000 43.89486  ? 14  TYR   A O   1 
ATOM   106  C CB  . TYR   A 1 14  ? 16.44006  20.16703 8.47975   1.000 39.43023  ? 14  TYR   A CB  1 
ATOM   107  C CG  . TYR   A 1 14  ? 15.53407  19.92758 7.28877   1.000 49.09996  ? 14  TYR   A CG  1 
ATOM   108  C CD1 . TYR   A 1 14  ? 15.33888  20.91357 6.33087   1.000 56.66869  ? 14  TYR   A CD1 1 
ATOM   109  C CD2 . TYR   A 1 14  ? 14.86699  18.71865 7.12724   1.000 49.67451  ? 14  TYR   A CD2 1 
ATOM   110  C CE1 . TYR   A 1 14  ? 14.50967  20.70257 5.24439   1.000 56.07127  ? 14  TYR   A CE1 1 
ATOM   111  C CE2 . TYR   A 1 14  ? 14.03336  18.49844 6.04234   1.000 42.10251  ? 14  TYR   A CE2 1 
ATOM   112  C CZ  . TYR   A 1 14  ? 13.85867  19.49502 5.10510   1.000 51.65130  ? 14  TYR   A CZ  1 
ATOM   113  O OH  . TYR   A 1 14  ? 13.03222  19.28782 4.02214   1.000 49.78332  ? 14  TYR   A OH  1 
ATOM   114  N N   . LEU   A 1 15  ? 17.09069  20.24991 11.63483  1.000 39.51618  ? 15  LEU   A N   1 
ATOM   115  C CA  . LEU   A 1 15  ? 17.36834  19.57473 12.89765  1.000 38.31175  ? 15  LEU   A CA  1 
ATOM   116  C C   . LEU   A 1 15  ? 16.44813  20.07345 14.00461  1.000 34.54327  ? 15  LEU   A C   1 
ATOM   117  O O   . LEU   A 1 15  ? 15.99099  19.28518 14.84053  1.000 37.06790  ? 15  LEU   A O   1 
ATOM   118  C CB  . LEU   A 1 15  ? 18.83313  19.77124 13.28086  1.000 35.55907  ? 15  LEU   A CB  1 
ATOM   119  C CG  . LEU   A 1 15  ? 19.84293  19.08303 12.36102  1.000 38.09781  ? 15  LEU   A CG  1 
ATOM   120  C CD1 . LEU   A 1 15  ? 21.22871  19.64719 12.57937  1.000 44.25333  ? 15  LEU   A CD1 1 
ATOM   121  C CD2 . LEU   A 1 15  ? 19.83911  17.57795 12.58672  1.000 46.19632  ? 15  LEU   A CD2 1 
ATOM   122  N N   . LEU   A 1 16  ? 16.15890  21.37732 14.02428  1.000 37.31731  ? 16  LEU   A N   1 
ATOM   123  C CA  . LEU   A 1 16  ? 15.24324  21.91365 15.02685  1.000 37.10121  ? 16  LEU   A CA  1 
ATOM   124  C C   . LEU   A 1 16  ? 13.83553  21.36439 14.83858  1.000 40.81965  ? 16  LEU   A C   1 
ATOM   125  O O   . LEU   A 1 16  ? 13.15503  21.03521 15.81804  1.000 36.08134  ? 16  LEU   A O   1 
ATOM   126  C CB  . LEU   A 1 16  ? 15.22937  23.44036 14.97058  1.000 36.12171  ? 16  LEU   A CB  1 
ATOM   127  C CG  . LEU   A 1 16  ? 16.49383  24.15484 15.43974  1.000 36.18822  ? 16  LEU   A CG  1 
ATOM   128  C CD1 . LEU   A 1 16  ? 16.31449  25.65604 15.32326  1.000 36.25059  ? 16  LEU   A CD1 1 
ATOM   129  C CD2 . LEU   A 1 16  ? 16.82871  23.75776 16.86753  1.000 38.49481  ? 16  LEU   A CD2 1 
ATOM   130  N N   . ALA   A 1 17  ? 13.37868  21.26576 13.58814  1.000 32.06074  ? 17  ALA   A N   1 
ATOM   131  C CA  . ALA   A 1 17  ? 12.06285  20.69270 13.32982  1.000 30.86099  ? 17  ALA   A CA  1 
ATOM   132  C C   . ALA   A 1 17  ? 12.02241  19.22009 13.71413  1.000 30.94807  ? 17  ALA   A C   1 
ATOM   133  O O   . ALA   A 1 17  ? 11.01862  18.73955 14.25422  1.000 36.41466  ? 17  ALA   A O   1 
ATOM   134  C CB  . ALA   A 1 17  ? 11.68720  20.87358 11.85947  1.000 29.38553  ? 17  ALA   A CB  1 
ATOM   135  N N   . ASN   A 1 18  ? 13.10368  18.48785 13.44094  1.000 33.13045  ? 18  ASN   A N   1 
ATOM   136  C CA  . ASN   A 1 18  ? 13.14330  17.07529 13.79825  1.000 38.83258  ? 18  ASN   A CA  1 
ATOM   137  C C   . ASN   A 1 18  ? 13.10162  16.89359 15.30831  1.000 42.88360  ? 18  ASN   A C   1 
ATOM   138  O O   . ASN   A 1 18  ? 12.46294  15.96245 15.81059  1.000 53.23930  ? 18  ASN   A O   1 
ATOM   139  C CB  . ASN   A 1 18  ? 14.39012  16.42121 13.20695  1.000 40.85921  ? 18  ASN   A CB  1 
ATOM   140  C CG  . ASN   A 1 18  ? 14.07637  15.13410 12.47717  1.000 77.33063  ? 18  ASN   A CG  1 
ATOM   141  O OD1 . ASN   A 1 18  ? 13.35346  14.27805 12.98812  1.000 100.73381 ? 18  ASN   A OD1 1 
ATOM   142  N ND2 . ASN   A 1 18  ? 14.60469  14.99699 11.26661  1.000 57.76705  ? 18  ASN   A ND2 1 
ATOM   143  N N   . GLN   A 1 19  ? 13.77178  17.77727 16.04894  1.000 42.67985  ? 19  GLN   A N   1 
ATOM   144  C CA  . GLN   A 1 19  ? 13.67358  17.73767 17.50241  1.000 43.50583  ? 19  GLN   A CA  1 
ATOM   145  C C   . GLN   A 1 19  ? 12.29910  18.19460 17.97947  1.000 37.97541  ? 19  GLN   A C   1 
ATOM   146  O O   . GLN   A 1 19  ? 11.78969  17.67873 18.97975  1.000 43.05960  ? 19  GLN   A O   1 
ATOM   147  C CB  . GLN   A 1 19  ? 14.77795  18.59611 18.12041  1.000 53.86141  ? 19  GLN   A CB  1 
ATOM   148  C CG  . GLN   A 1 19  ? 14.87182  18.50365 19.63148  1.000 97.98920  ? 19  GLN   A CG  1 
ATOM   149  C CD  . GLN   A 1 19  ? 15.99401  19.35091 20.19509  1.000 95.90479  ? 19  GLN   A CD  1 
ATOM   150  O OE1 . GLN   A 1 19  ? 16.72680  20.00566 19.45227  1.000 72.80645  ? 19  GLN   A OE1 1 
ATOM   151  N NE2 . GLN   A 1 19  ? 16.13460  19.34342 21.51657  1.000 72.51601  ? 19  GLN   A NE2 1 
ATOM   152  N N   . LEU   A 1 20  ? 11.68143  19.14512 17.27268  1.000 37.74636  ? 20  LEU   A N   1 
ATOM   153  C CA  . LEU   A 1 20  ? 10.34335  19.60220 17.63887  1.000 31.39406  ? 20  LEU   A CA  1 
ATOM   154  C C   . LEU   A 1 20  ? 9.31791   18.48798 17.48259  1.000 37.01151  ? 20  LEU   A C   1 
ATOM   155  O O   . LEU   A 1 20  ? 8.49230   18.25682 18.37402  1.000 39.55460  ? 20  LEU   A O   1 
ATOM   156  C CB  . LEU   A 1 20  ? 9.94907   20.80457 16.78311  1.000 40.35226  ? 20  LEU   A CB  1 
ATOM   157  C CG  . LEU   A 1 20  ? 10.42380  22.17930 17.24076  1.000 42.10328  ? 20  LEU   A CG  1 
ATOM   158  C CD1 . LEU   A 1 20  ? 10.53652  23.12245 16.05662  1.000 62.49340  ? 20  LEU   A CD1 1 
ATOM   159  C CD2 . LEU   A 1 20  ? 9.45629   22.72879 18.26170  1.000 42.24321  ? 20  LEU   A CD2 1 
ATOM   160  N N   . ILE   A 1 21  ? 9.34663   17.79265 16.34404  1.000 40.91429  ? 21  ILE   A N   1 
ATOM   161  C CA  . ILE   A 1 21  ? 8.37653   16.73536 16.10522  1.000 38.22731  ? 21  ILE   A CA  1 
ATOM   162  C C   . ILE   A 1 21  ? 8.59816   15.55841 17.04744  1.000 65.69053  ? 21  ILE   A C   1 
ATOM   163  O O   . ILE   A 1 21  ? 7.66820   14.78209 17.29409  1.000 49.02000  ? 21  ILE   A O   1 
ATOM   164  C CB  . ILE   A 1 21  ? 8.42509   16.30126 14.62734  1.000 39.42769  ? 21  ILE   A CB  1 
ATOM   165  C CG1 . ILE   A 1 21  ? 7.09183   15.68049 14.21132  1.000 38.89683  ? 21  ILE   A CG1 1 
ATOM   166  C CG2 . ILE   A 1 21  ? 9.57614   15.33812 14.38212  1.000 46.46065  ? 21  ILE   A CG2 1 
ATOM   167  C CD1 . ILE   A 1 21  ? 5.92086   16.62399 14.36960  1.000 30.15987  ? 21  ILE   A CD1 1 
ATOM   168  N N   . LEU   A 1 22  ? 9.80604   15.41206 17.59821  1.000 42.46467  ? 22  LEU   A N   1 
ATOM   169  C CA  . LEU   A 1 22  ? 10.03846  14.37715 18.59923  1.000 34.18051  ? 22  LEU   A CA  1 
ATOM   170  C C   . LEU   A 1 22  ? 9.47213   14.77876 19.95432  1.000 36.62061  ? 22  LEU   A C   1 
ATOM   171  O O   . LEU   A 1 22  ? 8.84022   13.96072 20.63216  1.000 38.15990  ? 22  LEU   A O   1 
ATOM   172  C CB  . LEU   A 1 22  ? 11.53272  14.07831 18.71497  1.000 39.58000  ? 22  LEU   A CB  1 
ATOM   173  C CG  . LEU   A 1 22  ? 12.15328  13.32722 17.53841  1.000 46.13741  ? 22  LEU   A CG  1 
ATOM   174  C CD1 . LEU   A 1 22  ? 13.64980  13.18646 17.73439  1.000 55.40349  ? 22  LEU   A CD1 1 
ATOM   175  C CD2 . LEU   A 1 22  ? 11.49722  11.96668 17.36833  1.000 62.95631  ? 22  LEU   A CD2 1 
ATOM   176  N N   . SER   A 1 23  ? 9.68760   16.03109 20.36409  1.000 35.69359  ? 23  SER   A N   1 
ATOM   177  C CA  . SER   A 1 23  ? 9.15256   16.48810 21.64060  1.000 30.41801  ? 23  SER   A CA  1 
ATOM   178  C C   . SER   A 1 23  ? 7.63072   16.50238 21.63019  1.000 30.64176  ? 23  SER   A C   1 
ATOM   179  O O   . SER   A 1 23  ? 7.00222   16.30416 22.67663  1.000 34.58122  ? 23  SER   A O   1 
ATOM   180  C CB  . SER   A 1 23  ? 9.69920   17.87670 21.97551  1.000 33.33933  ? 23  SER   A CB  1 
ATOM   181  O OG  . SER   A 1 23  ? 9.12922   18.87183 21.14139  1.000 43.34524  ? 23  SER   A OG  1 
ATOM   182  N N   . LEU   A 1 24  ? 7.02361   16.72530 20.46256  1.000 33.62395  ? 24  LEU   A N   1 
ATOM   183  C CA  . LEU   A 1 24  ? 5.56852   16.67864 20.36827  1.000 31.45128  ? 24  LEU   A CA  1 
ATOM   184  C C   . LEU   A 1 24  ? 5.05635   15.24878 20.49010  1.000 39.46167  ? 24  LEU   A C   1 
ATOM   185  O O   . LEU   A 1 24  ? 4.01841   15.00404 21.11769  1.000 41.44551  ? 24  LEU   A O   1 
ATOM   186  C CB  . LEU   A 1 24  ? 5.10936   17.31007 19.05420  1.000 26.63847  ? 24  LEU   A CB  1 
ATOM   187  C CG  . LEU   A 1 24  ? 4.56452   18.73897 19.14162  1.000 22.58324  ? 24  LEU   A CG  1 
ATOM   188  C CD1 . LEU   A 1 24  ? 5.52409   19.66120 19.87882  1.000 32.44199  ? 24  LEU   A CD1 1 
ATOM   189  C CD2 . LEU   A 1 24  ? 4.27629   19.27069 17.75165  1.000 34.17516  ? 24  LEU   A CD2 1 
ATOM   190  N N   . SER   A 1 25  ? 5.77448   14.29294 19.89463  1.000 37.17590  ? 25  SER   A N   1 
ATOM   191  C CA  . SER   A 1 25  ? 5.43110   12.88240 20.02439  1.000 29.48920  ? 25  SER   A CA  1 
ATOM   192  C C   . SER   A 1 25  ? 5.59641   12.36357 21.44914  1.000 38.37840  ? 25  SER   A C   1 
ATOM   193  O O   . SER   A 1 25  ? 4.92098   11.39795 21.82113  1.000 48.52091  ? 25  SER   A O   1 
ATOM   194  C CB  . SER   A 1 25  ? 6.29241   12.05155 19.06971  1.000 32.80767  ? 25  SER   A CB  1 
ATOM   195  O OG  . SER   A 1 25  ? 6.10859   12.44409 17.72009  1.000 43.16888  ? 25  SER   A OG  1 
ATOM   196  N N   . LYS   A 1 26  ? 6.46726   12.97717 22.25090  1.000 43.83550  ? 26  LYS   A N   1 
ATOM   197  C CA  . LYS   A 1 26  ? 6.67719   12.53124 23.62255  1.000 35.02154  ? 26  LYS   A CA  1 
ATOM   198  C C   . LYS   A 1 26  ? 5.81207   13.26937 24.63152  1.000 35.01085  ? 26  LYS   A C   1 
ATOM   199  O O   . LYS   A 1 26  ? 5.70068   12.81479 25.77536  1.000 42.90177  ? 26  LYS   A O   1 
ATOM   200  C CB  . LYS   A 1 26  ? 8.14751   12.69449 24.03287  1.000 43.53857  ? 26  LYS   A CB  1 
ATOM   201  C CG  . LYS   A 1 26  ? 9.14389   11.91650 23.18479  1.000 46.72199  ? 26  LYS   A CG  1 
ATOM   202  C CD  . LYS   A 1 26  ? 10.52981  11.90689 23.82806  1.000 62.06066  ? 26  LYS   A CD  1 
ATOM   203  C CE  . LYS   A 1 26  ? 11.07464  13.31255 24.04294  1.000 63.42114  ? 26  LYS   A CE  1 
ATOM   204  N NZ  . LYS   A 1 26  ? 11.43217  13.97929 22.76035  1.000 87.06293  ? 26  LYS   A NZ  1 
ATOM   205  N N   . TYR   A 1 27  ? 5.21054   14.39143 24.24612  1.000 39.11019  ? 27  TYR   A N   1 
ATOM   206  C CA  . TYR   A 1 27  ? 4.40751   15.16635 25.17792  1.000 48.23163  ? 27  TYR   A CA  1 
ATOM   207  C C   . TYR   A 1 27  ? 3.14149   14.40264 25.55979  1.000 41.39253  ? 27  TYR   A C   1 
ATOM   208  O O   . TYR   A 1 27  ? 2.71137   13.47090 24.87201  1.000 46.95692  ? 27  TYR   A O   1 
ATOM   209  C CB  . TYR   A 1 27  ? 4.04723   16.52236 24.57046  1.000 34.55231  ? 27  TYR   A CB  1 
ATOM   210  C CG  . TYR   A 1 27  ? 3.52603   17.53337 25.56582  1.000 33.73446  ? 27  TYR   A CG  1 
ATOM   211  C CD1 . TYR   A 1 27  ? 4.39482   18.22425 26.39869  1.000 63.89588  ? 27  TYR   A CD1 1 
ATOM   212  C CD2 . TYR   A 1 27  ? 2.16820   17.80514 25.66479  1.000 33.50668  ? 27  TYR   A CD2 1 
ATOM   213  C CE1 . TYR   A 1 27  ? 3.92704   19.15311 27.30895  1.000 38.99408  ? 27  TYR   A CE1 1 
ATOM   214  C CE2 . TYR   A 1 27  ? 1.68917   18.73266 26.57217  1.000 38.70975  ? 27  TYR   A CE2 1 
ATOM   215  C CZ  . TYR   A 1 27  ? 2.57443   19.40470 27.39076  1.000 42.43976  ? 27  TYR   A CZ  1 
ATOM   216  O OH  . TYR   A 1 27  ? 2.10697   20.33072 28.29530  1.000 44.56514  ? 27  TYR   A OH  1 
ATOM   217  N N   . GLU   A 1 28  ? 2.54994   14.81113 26.68250  1.000 37.54748  ? 28  GLU   A N   1 
ATOM   218  C CA  . GLU   A 1 28  ? 1.32895   14.18394 27.17441  1.000 36.15569  ? 28  GLU   A CA  1 
ATOM   219  C C   . GLU   A 1 28  ? 0.23304   14.23168 26.11830  1.000 40.89594  ? 28  GLU   A C   1 
ATOM   220  O O   . GLU   A 1 28  ? -0.06524  15.29167 25.55965  1.000 49.91043  ? 28  GLU   A O   1 
ATOM   221  C CB  . GLU   A 1 28  ? 0.85872   14.88024 28.45164  1.000 67.88339  ? 28  GLU   A CB  1 
ATOM   222  C CG  . GLU   A 1 28  ? -0.53895  14.47497 28.90617  1.000 71.76122  ? 28  GLU   A CG  1 
ATOM   223  C CD  . GLU   A 1 28  ? -0.60613  13.04490 29.41161  1.000 81.47695  ? 28  GLU   A CD  1 
ATOM   224  O OE1 . GLU   A 1 28  ? 0.29344   12.63955 30.17785  1.000 74.92978  ? 28  GLU   A OE1 1 
ATOM   225  O OE2 . GLU   A 1 28  ? -1.55776  12.32512 29.03933  1.000 95.25455  ? 28  GLU   A OE2 1 
ATOM   226  N N   . GLY   A 1 29  ? -0.36613  13.07375 25.84856  1.000 30.73621  ? 29  GLY   A N   1 
ATOM   227  C CA  . GLY   A 1 29  ? -1.40824  12.96129 24.85404  1.000 33.90068  ? 29  GLY   A CA  1 
ATOM   228  C C   . GLY   A 1 29  ? -0.93305  12.99904 23.42034  1.000 37.90589  ? 29  GLY   A C   1 
ATOM   229  O O   . GLY   A 1 29  ? -1.76450  12.88761 22.51012  1.000 37.09628  ? 29  GLY   A O   1 
ATOM   230  N N   . GLY   A 1 30  ? 0.37342   13.14488 23.18541  1.000 36.99397  ? 30  GLY   A N   1 
ATOM   231  C CA  . GLY   A 1 30  ? 0.88536   13.23966 21.82910  1.000 37.41563  ? 30  GLY   A CA  1 
ATOM   232  C C   . GLY   A 1 30  ? 0.66260   11.99637 20.99553  1.000 40.55428  ? 30  GLY   A C   1 
ATOM   233  O O   . GLY   A 1 30  ? 0.73315   12.06414 19.76304  1.000 46.13463  ? 30  GLY   A O   1 
ATOM   234  N N   . HIS   A 1 31  ? 0.39286   10.85837 21.63879  1.000 43.77008  ? 31  HIS   A N   1 
ATOM   235  C CA  . HIS   A 1 31  ? 0.16164   9.62065  20.90549  1.000 35.84510  ? 31  HIS   A CA  1 
ATOM   236  C C   . HIS   A 1 31  ? -1.07543  9.69313  20.01975  1.000 42.52350  ? 31  HIS   A C   1 
ATOM   237  O O   . HIS   A 1 31  ? -1.17986  8.92408  19.05796  1.000 50.12602  ? 31  HIS   A O   1 
ATOM   238  C CB  . HIS   A 1 31  ? 0.03455   8.45482  21.88551  1.000 39.74222  ? 31  HIS   A CB  1 
ATOM   239  C CG  . HIS   A 1 31  ? -1.04721  8.64020  22.90195  1.000 39.03204  ? 31  HIS   A CG  1 
ATOM   240  N ND1 . HIS   A 1 31  ? -0.85705  9.34492  24.07111  1.000 49.70803  ? 31  HIS   A ND1 1 
ATOM   241  C CD2 . HIS   A 1 31  ? -2.33382  8.21912  22.92168  1.000 46.46341  ? 31  HIS   A CD2 1 
ATOM   242  C CE1 . HIS   A 1 31  ? -1.97899  9.34724  24.76888  1.000 51.18863  ? 31  HIS   A CE1 1 
ATOM   243  N NE2 . HIS   A 1 31  ? -2.89090  8.67139  24.09340  1.000 60.66624  ? 31  HIS   A NE2 1 
ATOM   244  N N   . ILE   A 1 32  ? -2.01163  10.60128 20.31369  1.000 41.31097  ? 32  ILE   A N   1 
ATOM   245  C CA  . ILE   A 1 32  ? -3.23724  10.69797 19.52213  1.000 43.64805  ? 32  ILE   A CA  1 
ATOM   246  C C   . ILE   A 1 32  ? -3.04261  11.45844 18.22094  1.000 35.39412  ? 32  ILE   A C   1 
ATOM   247  O O   . ILE   A 1 32  ? -3.95489  11.47483 17.38446  1.000 38.19040  ? 32  ILE   A O   1 
ATOM   248  C CB  . ILE   A 1 32  ? -4.36984  11.36087 20.32962  1.000 34.16839  ? 32  ILE   A CB  1 
ATOM   249  C CG1 . ILE   A 1 32  ? -4.23326  12.88221 20.31510  1.000 49.73456  ? 32  ILE   A CG1 1 
ATOM   250  C CG2 . ILE   A 1 32  ? -4.37636  10.84556 21.76275  1.000 43.98116  ? 32  ILE   A CG2 1 
ATOM   251  C CD1 . ILE   A 1 32  ? -5.35185  13.59295 21.03808  1.000 35.96544  ? 32  ILE   A CD1 1 
ATOM   252  N N   . PHE   A 1 33  ? -1.88394  12.08664 18.02320  1.000 38.63676  ? 33  PHE   A N   1 
ATOM   253  C CA  . PHE   A 1 33  ? -1.56948  12.78583 16.78552  1.000 36.16284  ? 33  PHE   A CA  1 
ATOM   254  C C   . PHE   A 1 33  ? -0.45023  12.12070 15.99747  1.000 37.78911  ? 33  PHE   A C   1 
ATOM   255  O O   . PHE   A 1 33  ? -0.09144  12.61489 14.92344  1.000 40.43056  ? 33  PHE   A O   1 
ATOM   256  C CB  . PHE   A 1 33  ? -1.18707  14.24197 17.07911  1.000 34.63207  ? 33  PHE   A CB  1 
ATOM   257  C CG  . PHE   A 1 33  ? -2.21911  14.99508 17.86879  1.000 35.75013  ? 33  PHE   A CG  1 
ATOM   258  C CD1 . PHE   A 1 33  ? -3.43474  15.32932 17.30003  1.000 29.81887  ? 33  PHE   A CD1 1 
ATOM   259  C CD2 . PHE   A 1 33  ? -1.96832  15.37892 19.17542  1.000 34.98840  ? 33  PHE   A CD2 1 
ATOM   260  C CE1 . PHE   A 1 33  ? -4.38597  16.02394 18.02027  1.000 25.11323  ? 33  PHE   A CE1 1 
ATOM   261  C CE2 . PHE   A 1 33  ? -2.91589  16.07523 19.90042  1.000 37.13173  ? 33  PHE   A CE2 1 
ATOM   262  C CZ  . PHE   A 1 33  ? -4.12589  16.39742 19.32144  1.000 35.72475  ? 33  PHE   A CZ  1 
ATOM   263  N N   . GLU   A 1 34  ? 0.10764   11.01404 16.49711  1.000 44.04761  ? 34  GLU   A N   1 
ATOM   264  C CA  . GLU   A 1 34  ? 1.26834   10.40602 15.85166  1.000 43.50742  ? 34  GLU   A CA  1 
ATOM   265  C C   . GLU   A 1 34  ? 0.90461   9.81816  14.49313  1.000 48.56834  ? 34  GLU   A C   1 
ATOM   266  O O   . GLU   A 1 34  ? 1.56954   10.09324 13.48768  1.000 45.07799  ? 34  GLU   A O   1 
ATOM   267  C CB  . GLU   A 1 34  ? 1.86989   9.33274  16.76081  1.000 44.99373  ? 34  GLU   A CB  1 
ATOM   268  C CG  . GLU   A 1 34  ? 3.14069   8.69453  16.21518  1.000 48.60038  ? 34  GLU   A CG  1 
ATOM   269  C CD  . GLU   A 1 34  ? 4.31197   9.66103  16.17050  1.000 81.81569  ? 34  GLU   A CD  1 
ATOM   270  O OE1 . GLU   A 1 34  ? 4.29678   10.65616 16.92738  1.000 52.85415  ? 34  GLU   A OE1 1 
ATOM   271  O OE2 . GLU   A 1 34  ? 5.24836   9.42564  15.37681  1.000 59.32062  ? 34  GLU   A OE2 1 
ATOM   272  N N   . LYS   A 1 35  ? -0.14170  9.00219  14.44431  1.000 49.07462  ? 35  LYS   A N   1 
ATOM   273  C CA  . LYS   A 1 35  ? -0.59830  8.38170  13.21206  1.000 43.97099  ? 35  LYS   A CA  1 
ATOM   274  C C   . LYS   A 1 35  ? -1.93530  8.98095  12.79703  1.000 46.75303  ? 35  LYS   A C   1 
ATOM   275  O O   . LYS   A 1 35  ? -2.65253  9.57289  13.60827  1.000 57.47389  ? 35  LYS   A O   1 
ATOM   276  C CB  . LYS   A 1 35  ? -0.72621  6.86337  13.37858  1.000 51.83297  ? 35  LYS   A CB  1 
ATOM   277  C CG  . LYS   A 1 35  ? 0.52754   6.18830  13.91726  1.000 47.73068  ? 35  LYS   A CG  1 
ATOM   278  C CD  . LYS   A 1 35  ? 1.72495   6.42302  13.00838  1.000 58.00873  ? 35  LYS   A CD  1 
ATOM   279  N N   . LEU   A 1 36  ? -2.26052  8.82767  11.51422  1.000 56.84818  ? 36  LEU   A N   1 
ATOM   280  C CA  . LEU   A 1 36  ? -3.53218  9.32628  11.00888  1.000 43.89338  ? 36  LEU   A CA  1 
ATOM   281  C C   . LEU   A 1 36  ? -4.69081  8.58808  11.67014  1.000 56.25710  ? 36  LEU   A C   1 
ATOM   282  O O   . LEU   A 1 36  ? -4.56422  7.43594  12.09359  1.000 58.14376  ? 36  LEU   A O   1 
ATOM   283  C CB  . LEU   A 1 36  ? -3.60297  9.17829  9.48690   1.000 43.63469  ? 36  LEU   A CB  1 
ATOM   284  C CG  . LEU   A 1 36  ? -2.73043  10.14740 8.68392   1.000 38.80552  ? 36  LEU   A CG  1 
ATOM   285  C CD1 . LEU   A 1 36  ? -2.77625  9.82641  7.19887   1.000 41.13794  ? 36  LEU   A CD1 1 
ATOM   286  C CD2 . LEU   A 1 36  ? -3.16278  11.58547 8.93508   1.000 44.44312  ? 36  LEU   A CD2 1 
ATOM   287  N N   . VAL   A 1 37  ? -5.82941  9.27167  11.76380  1.000 71.30074  ? 37  VAL   A N   1 
ATOM   288  C CA  . VAL   A 1 37  ? -6.98216  8.73177  12.47625  1.000 60.37040  ? 37  VAL   A CA  1 
ATOM   289  C C   . VAL   A 1 37  ? -7.57613  7.57976  11.67672  1.000 59.69084  ? 37  VAL   A C   1 
ATOM   290  O O   . VAL   A 1 37  ? -8.00628  7.75697  10.53120  1.000 62.34010  ? 37  VAL   A O   1 
ATOM   291  C CB  . VAL   A 1 37  ? -8.02797  9.82489  12.72895  1.000 50.60238  ? 37  VAL   A CB  1 
ATOM   292  C CG1 . VAL   A 1 37  ? -9.21962  9.25737  13.48505  1.000 51.33650  ? 37  VAL   A CG1 1 
ATOM   293  C CG2 . VAL   A 1 37  ? -7.40787  10.98547 13.48933  1.000 50.20759  ? 37  VAL   A CG2 1 
ATOM   294  N N   . ASP   A 1 38  ? -7.60175  6.39175  12.27765  1.000 63.05047  ? 38  ASP   A N   1 
ATOM   295  C CA  . ASP   A 1 38  ? -8.30680  5.25604  11.69267  1.000 66.37640  ? 38  ASP   A CA  1 
ATOM   296  C C   . ASP   A 1 38  ? -9.77974  5.38395  12.05980  1.000 61.31922  ? 38  ASP   A C   1 
ATOM   297  O O   . ASP   A 1 38  ? -10.15601 5.19879  13.22209  1.000 81.10911  ? 38  ASP   A O   1 
ATOM   298  C CB  . ASP   A 1 38  ? -7.71734  3.93753  12.18564  1.000 72.50404  ? 38  ASP   A CB  1 
ATOM   299  C CG  . ASP   A 1 38  ? -8.12709  2.75441  11.32386  1.000 93.40359  ? 38  ASP   A CG  1 
ATOM   300  O OD1 . ASP   A 1 38  ? -8.99278  2.92671  10.43987  1.000 89.48723  ? 38  ASP   A OD1 1 
ATOM   301  O OD2 . ASP   A 1 38  ? -7.57607  1.65121  11.52473  1.000 120.85801 ? 38  ASP   A OD2 1 
ATOM   302  N N   . ALA   A 1 39  ? -10.61129 5.70901  11.06645  1.000 56.64112  ? 39  ALA   A N   1 
ATOM   303  C CA  . ALA   A 1 39  ? -12.01190 6.02790  11.32895  1.000 58.65737  ? 39  ALA   A CA  1 
ATOM   304  C C   . ALA   A 1 39  ? -12.75141 4.87738  12.00375  1.000 84.31701  ? 39  ALA   A C   1 
ATOM   305  O O   . ALA   A 1 39  ? -13.61354 5.11286  12.85768  1.000 75.55514  ? 39  ALA   A O   1 
ATOM   306  C CB  . ALA   A 1 39  ? -12.70597 6.41591  10.02304  1.000 62.75600  ? 39  ALA   A CB  1 
ATOM   307  N N   . LYS   A 1 40  ? -12.42509 3.63290  11.64987  1.000 76.16647  ? 40  LYS   A N   1 
ATOM   308  C CA  . LYS   A 1 40  ? -13.12293 2.48977  12.22946  1.000 82.56174  ? 40  LYS   A CA  1 
ATOM   309  C C   . LYS   A 1 40  ? -12.63862 2.18625  13.64361  1.000 85.35957  ? 40  LYS   A C   1 
ATOM   310  O O   . LYS   A 1 40  ? -13.45216 1.91773  14.53567  1.000 89.82923  ? 40  LYS   A O   1 
ATOM   311  C CB  . LYS   A 1 40  ? -12.95225 1.26419  11.33394  1.000 91.10659  ? 40  LYS   A CB  1 
ATOM   312  N N   . LYS   A 1 41  ? -11.32404 2.23152  13.87065  1.000 81.86741  ? 41  LYS   A N   1 
ATOM   313  C CA  . LYS   A 1 41  ? -10.79004 1.86482  15.17864  1.000 86.28841  ? 41  LYS   A CA  1 
ATOM   314  C C   . LYS   A 1 41  ? -11.10345 2.91465  16.23724  1.000 96.88061  ? 41  LYS   A C   1 
ATOM   315  O O   . LYS   A 1 41  ? -11.22230 2.57833  17.42080  1.000 118.65372 ? 41  LYS   A O   1 
ATOM   316  C CB  . LYS   A 1 41  ? -9.28028  1.63930  15.09186  1.000 80.44312  ? 41  LYS   A CB  1 
ATOM   317  C CG  . LYS   A 1 41  ? -8.86974  0.47001  14.21309  1.000 79.13684  ? 41  LYS   A CG  1 
ATOM   318  N N   . GLN   A 1 42  ? -11.23416 4.18035  15.84246  1.000 97.11233  ? 42  GLN   A N   1 
ATOM   319  C CA  . GLN   A 1 42  ? -11.53477 5.25876  16.77472  1.000 87.08900  ? 42  GLN   A CA  1 
ATOM   320  C C   . GLN   A 1 42  ? -13.01704 5.60479  16.82070  1.000 95.63825  ? 42  GLN   A C   1 
ATOM   321  O O   . GLN   A 1 42  ? -13.39588 6.54985  17.52107  1.000 86.68501  ? 42  GLN   A O   1 
ATOM   322  C CB  . GLN   A 1 42  ? -10.72188 6.50959  16.41839  1.000 70.75501  ? 42  GLN   A CB  1 
ATOM   323  C CG  . GLN   A 1 42  ? -9.24806  6.24574  16.12981  1.000 73.18195  ? 42  GLN   A CG  1 
ATOM   324  C CD  . GLN   A 1 42  ? -8.49273  5.68704  17.32283  1.000 95.76666  ? 42  GLN   A CD  1 
ATOM   325  O OE1 . GLN   A 1 42  ? -8.94010  5.78984  18.46686  1.000 79.04173  ? 42  GLN   A OE1 1 
ATOM   326  N NE2 . GLN   A 1 42  ? -7.33521  5.09057  17.05774  1.000 74.49620  ? 42  GLN   A NE2 1 
ATOM   327  N N   . ASN   A 1 43  ? -13.85583 4.86518  16.09013  1.000 82.70053  ? 43  ASN   A N   1 
ATOM   328  C CA  . ASN   A 1 43  ? -15.30622 5.07139  16.07087  1.000 85.01164  ? 43  ASN   A CA  1 
ATOM   329  C C   . ASN   A 1 43  ? -15.66356 6.48927  15.62476  1.000 82.94069  ? 43  ASN   A C   1 
ATOM   330  O O   . ASN   A 1 43  ? -16.39384 7.21624  16.30178  1.000 85.32413  ? 43  ASN   A O   1 
ATOM   331  C CB  . ASN   A 1 43  ? -15.92684 4.74823  17.43246  1.000 73.80070  ? 43  ASN   A CB  1 
ATOM   332  C CG  . ASN   A 1 43  ? -15.76667 3.29025  17.81173  1.000 101.88304 ? 43  ASN   A CG  1 
ATOM   333  O OD1 . ASN   A 1 43  ? -15.17815 2.96624  18.84332  1.000 119.74460 ? 43  ASN   A OD1 1 
ATOM   334  N ND2 . ASN   A 1 43  ? -16.28981 2.40017  16.97533  1.000 102.48411 ? 43  ASN   A ND2 1 
ATOM   335  N N   . CYS   A 1 44  ? -15.14606 6.87584  14.46075  1.000 75.70469  ? 44  CYS   A N   1 
ATOM   336  C CA  . CYS   A 1 44  ? -15.40305 8.19364  13.87798  1.000 76.58943  ? 44  CYS   A CA  1 
ATOM   337  C C   . CYS   A 1 44  ? -15.56000 8.04623  12.37400  1.000 73.39136  ? 44  CYS   A C   1 
ATOM   338  O O   . CYS   A 1 44  ? -14.65198 8.37362  11.60071  1.000 69.48099  ? 44  CYS   A O   1 
ATOM   339  C CB  . CYS   A 1 44  ? -14.28141 9.17435  14.22427  1.000 65.29721  ? 44  CYS   A CB  1 
ATOM   340  S SG  . CYS   A 1 44  ? -14.28791 9.67053  15.95235  1.000 110.86142 ? 44  CYS   A SG  1 
ATOM   341  N N   . PRO   A 1 45  ? -16.72143 7.56615  11.91705  1.000 71.39319  ? 45  PRO   A N   1 
ATOM   342  C CA  . PRO   A 1 45  ? -16.89419 7.28469  10.48257  1.000 71.31484  ? 45  PRO   A CA  1 
ATOM   343  C C   . PRO   A 1 45  ? -16.97491 8.52574  9.61207   1.000 69.99304  ? 45  PRO   A C   1 
ATOM   344  O O   . PRO   A 1 45  ? -16.93846 8.39710  8.38105   1.000 91.21042  ? 45  PRO   A O   1 
ATOM   345  C CB  . PRO   A 1 45  ? -18.21112 6.50018  10.43933  1.000 76.20573  ? 45  PRO   A CB  1 
ATOM   346  C CG  . PRO   A 1 45  ? -18.96795 6.99759  11.62614  1.000 63.70535  ? 45  PRO   A CG  1 
ATOM   347  C CD  . PRO   A 1 45  ? -17.93718 7.26449  12.69281  1.000 68.39416  ? 45  PRO   A CD  1 
ATOM   348  N N   . ASP   A 1 46  ? -17.08570 9.71618  10.19871  1.000 61.30382  ? 46  ASP   A N   1 
ATOM   349  C CA  . ASP   A 1 46  ? -17.24138 10.94601 9.43434   1.000 63.07810  ? 46  ASP   A CA  1 
ATOM   350  C C   . ASP   A 1 46  ? -16.01823 11.84987 9.52289   1.000 60.73368  ? 46  ASP   A C   1 
ATOM   351  O O   . ASP   A 1 46  ? -16.11117 13.03509 9.18987   1.000 107.88099 ? 46  ASP   A O   1 
ATOM   352  C CB  . ASP   A 1 46  ? -18.47811 11.70770 9.90922   1.000 60.75095  ? 46  ASP   A CB  1 
ATOM   353  C CG  . ASP   A 1 46  ? -18.36622 12.14839 11.35409  1.000 66.09253  ? 46  ASP   A CG  1 
ATOM   354  O OD1 . ASP   A 1 46  ? -17.86993 11.35558 12.18336  1.000 60.06711  ? 46  ASP   A OD1 1 
ATOM   355  O OD2 . ASP   A 1 46  ? -18.76868 13.29139 11.65800  1.000 66.91701  ? 46  ASP   A OD2 1 
ATOM   356  N N   . TYR   A 1 47  ? -14.87750 11.31929 9.97170   1.000 48.47618  ? 47  TYR   A N   1 
ATOM   357  C CA  . TYR   A 1 47  ? -13.69685 12.15803 10.15207  1.000 51.31009  ? 47  TYR   A CA  1 
ATOM   358  C C   . TYR   A 1 47  ? -13.19994 12.71050 8.82047   1.000 46.89986  ? 47  TYR   A C   1 
ATOM   359  O O   . TYR   A 1 47  ? -12.95566 13.91611 8.69007   1.000 70.84845  ? 47  TYR   A O   1 
ATOM   360  C CB  . TYR   A 1 47  ? -12.58996 11.37136 10.85806  1.000 40.73966  ? 47  TYR   A CB  1 
ATOM   361  C CG  . TYR   A 1 47  ? -11.36097 12.20762 11.13013  1.000 49.76522  ? 47  TYR   A CG  1 
ATOM   362  C CD1 . TYR   A 1 47  ? -11.29664 13.04114 12.23923  1.000 43.95357  ? 47  TYR   A CD1 1 
ATOM   363  C CD2 . TYR   A 1 47  ? -10.27126 12.17771 10.26916  1.000 37.87579  ? 47  TYR   A CD2 1 
ATOM   364  C CE1 . TYR   A 1 47  ? -10.17804 13.81684 12.48736  1.000 45.57427  ? 47  TYR   A CE1 1 
ATOM   365  C CE2 . TYR   A 1 47  ? -9.14894  12.95049 10.50819  1.000 49.81316  ? 47  TYR   A CE2 1 
ATOM   366  C CZ  . TYR   A 1 47  ? -9.10800  13.76811 11.61845  1.000 39.81382  ? 47  TYR   A CZ  1 
ATOM   367  O OH  . TYR   A 1 47  ? -7.99431  14.53763 11.86304  1.000 42.77114  ? 47  TYR   A OH  1 
ATOM   368  N N   . TYR   A 1 48  ? -13.05333 11.84751 7.81723   1.000 59.08930  ? 48  TYR   A N   1 
ATOM   369  C CA  . TYR   A 1 48  ? -12.53713 12.26927 6.52012   1.000 70.55050  ? 48  TYR   A CA  1 
ATOM   370  C C   . TYR   A 1 48  ? -13.60726 12.86610 5.61771   1.000 62.70652  ? 48  TYR   A C   1 
ATOM   371  O O   . TYR   A 1 48  ? -13.29390 13.25852 4.48727   1.000 68.36172  ? 48  TYR   A O   1 
ATOM   372  C CB  . TYR   A 1 48  ? -11.84274 11.09275 5.82809   1.000 60.98714  ? 48  TYR   A CB  1 
ATOM   373  C CG  . TYR   A 1 48  ? -10.64412 10.60569 6.60654   1.000 55.54326  ? 48  TYR   A CG  1 
ATOM   374  C CD1 . TYR   A 1 48  ? -9.42504  11.26725 6.52752   1.000 49.71001  ? 48  TYR   A CD1 1 
ATOM   375  C CD2 . TYR   A 1 48  ? -10.73858 9.50424  7.44535   1.000 60.20489  ? 48  TYR   A CD2 1 
ATOM   376  C CE1 . TYR   A 1 48  ? -8.32984  10.83428 7.25143   1.000 54.96432  ? 48  TYR   A CE1 1 
ATOM   377  C CE2 . TYR   A 1 48  ? -9.65024  9.06428  8.17062   1.000 44.48920  ? 48  TYR   A CE2 1 
ATOM   378  C CZ  . TYR   A 1 48  ? -8.44841  9.73230  8.07091   1.000 48.91333  ? 48  TYR   A CZ  1 
ATOM   379  O OH  . TYR   A 1 48  ? -7.36289  9.29737  8.79525   1.000 50.36743  ? 48  TYR   A OH  1 
ATOM   380  N N   . ASP   A 1 49  ? -14.85377 12.93500 6.08185   1.000 54.71877  ? 49  ASP   A N   1 
ATOM   381  C CA  . ASP   A 1 49  ? -15.86938 13.75569 5.44018   1.000 62.14635  ? 49  ASP   A CA  1 
ATOM   382  C C   . ASP   A 1 49  ? -15.82456 15.20089 5.91335   1.000 51.45998  ? 49  ASP   A C   1 
ATOM   383  O O   . ASP   A 1 49  ? -16.38877 16.07960 5.25043   1.000 58.56759  ? 49  ASP   A O   1 
ATOM   384  C CB  . ASP   A 1 49  ? -17.26403 13.17634 5.69834   1.000 68.80913  ? 49  ASP   A CB  1 
ATOM   385  C CG  . ASP   A 1 49  ? -17.46963 11.82696 5.03098   1.000 93.01331  ? 49  ASP   A CG  1 
ATOM   386  O OD1 . ASP   A 1 49  ? -17.10135 11.68645 3.84495   1.000 94.55796  ? 49  ASP   A OD1 1 
ATOM   387  O OD2 . ASP   A 1 49  ? -17.99884 10.90647 5.69288   1.000 92.04617  ? 49  ASP   A OD2 1 
ATOM   388  N N   . VAL   A 1 50  ? -15.16323 15.46181 7.03621   1.000 51.53530  ? 50  VAL   A N   1 
ATOM   389  C CA  . VAL   A 1 50  ? -14.96206 16.80834 7.55204   1.000 56.25150  ? 50  VAL   A CA  1 
ATOM   390  C C   . VAL   A 1 50  ? -13.51769 17.25911 7.36127   1.000 44.25930  ? 50  VAL   A C   1 
ATOM   391  O O   . VAL   A 1 50  ? -13.25971 18.37534 6.90839   1.000 41.09367  ? 50  VAL   A O   1 
ATOM   392  C CB  . VAL   A 1 50  ? -15.37876 16.89738 9.03810   1.000 49.09477  ? 50  VAL   A CB  1 
ATOM   393  C CG1 . VAL   A 1 50  ? -15.18961 18.31340 9.56477   1.000 50.49978  ? 50  VAL   A CG1 1 
ATOM   394  C CG2 . VAL   A 1 50  ? -16.82170 16.44575 9.21342   1.000 50.11888  ? 50  VAL   A CG2 1 
ATOM   395  N N   . ILE   A 1 51  ? -12.56323 16.39294 7.68951   1.000 50.47146  ? 51  ILE   A N   1 
ATOM   396  C CA  . ILE   A 1 51  ? -11.14242 16.69708 7.55749   1.000 44.68758  ? 51  ILE   A CA  1 
ATOM   397  C C   . ILE   A 1 51  ? -10.68562 16.22371 6.18230   1.000 49.77961  ? 51  ILE   A C   1 
ATOM   398  O O   . ILE   A 1 51  ? -10.51419 15.02314 5.95403   1.000 52.11930  ? 51  ILE   A O   1 
ATOM   399  C CB  . ILE   A 1 51  ? -10.32370 16.03649 8.67241   1.000 41.66760  ? 51  ILE   A CB  1 
ATOM   400  C CG1 . ILE   A 1 51  ? -10.84820 16.46798 10.04313  1.000 31.74440  ? 51  ILE   A CG1 1 
ATOM   401  C CG2 . ILE   A 1 51  ? -8.84739  16.36662 8.51991   1.000 42.41556  ? 51  ILE   A CG2 1 
ATOM   402  C CD1 . ILE   A 1 51  ? -10.92145 17.96632 10.22626  1.000 50.60661  ? 51  ILE   A CD1 1 
ATOM   403  N N   . LYS   A 1 52  ? -10.48308 17.16820 5.26345   1.000 42.86998  ? 52  LYS   A N   1 
ATOM   404  C CA  . LYS   A 1 52  ? -10.08531 16.84146 3.90047   1.000 46.65054  ? 52  LYS   A CA  1 
ATOM   405  C C   . LYS   A 1 52  ? -8.57981  16.92019 3.68029   1.000 48.59099  ? 52  LYS   A C   1 
ATOM   406  O O   . LYS   A 1 52  ? -8.09169  16.41915 2.66080   1.000 45.29886  ? 52  LYS   A O   1 
ATOM   407  C CB  . LYS   A 1 52  ? -10.79313 17.76743 2.90017   1.000 44.05140  ? 52  LYS   A CB  1 
ATOM   408  C CG  . LYS   A 1 52  ? -12.26399 18.03504 3.20395   1.000 49.21727  ? 52  LYS   A CG  1 
ATOM   409  C CD  . LYS   A 1 52  ? -13.07588 16.75467 3.34831   1.000 47.95477  ? 52  LYS   A CD  1 
ATOM   410  C CE  . LYS   A 1 52  ? -13.16041 15.98709 2.04893   1.000 55.55940  ? 52  LYS   A CE  1 
ATOM   411  N NZ  . LYS   A 1 52  ? -14.00354 14.76837 2.20237   1.000 53.51724  ? 52  LYS   A NZ  1 
ATOM   412  N N   . ASN   A 1 53  ? -7.83557  17.53432 4.60246   1.000 53.07014  ? 53  ASN   A N   1 
ATOM   413  C CA  . ASN   A 1 53  ? -6.38074  17.64162 4.52291   1.000 47.17846  ? 53  ASN   A CA  1 
ATOM   414  C C   . ASN   A 1 53  ? -5.80043  17.04537 5.80120   1.000 41.53560  ? 53  ASN   A C   1 
ATOM   415  O O   . ASN   A 1 53  ? -5.39177  17.78038 6.71354   1.000 41.01457  ? 53  ASN   A O   1 
ATOM   416  C CB  . ASN   A 1 53  ? -5.94231  19.09205 4.32608   1.000 43.63579  ? 53  ASN   A CB  1 
ATOM   417  C CG  . ASN   A 1 53  ? -4.47507  19.21544 3.96603   1.000 60.94612  ? 53  ASN   A CG  1 
ATOM   418  O OD1 . ASN   A 1 53  ? -3.80537  18.22172 3.68262   1.000 67.55669  ? 53  ASN   A OD1 1 
ATOM   419  N ND2 . ASN   A 1 53  ? -3.96932  20.44239 3.96654   1.000 49.18432  ? 53  ASN   A ND2 1 
ATOM   420  N N   . PRO   A 1 54  ? -5.75820  15.71847 5.90764   1.000 35.17747  ? 54  PRO   A N   1 
ATOM   421  C CA  . PRO   A 1 54  ? -5.27542  15.09008 7.14151   1.000 40.52252  ? 54  PRO   A CA  1 
ATOM   422  C C   . PRO   A 1 54  ? -3.77547  15.27042 7.30984   1.000 47.48098  ? 54  PRO   A C   1 
ATOM   423  O O   . PRO   A 1 54  ? -3.02773  15.46483 6.34899   1.000 51.16531  ? 54  PRO   A O   1 
ATOM   424  C CB  . PRO   A 1 54  ? -5.63473  13.61006 6.95731   1.000 40.24851  ? 54  PRO   A CB  1 
ATOM   425  C CG  . PRO   A 1 54  ? -6.61033  13.57653 5.81018   1.000 42.50585  ? 54  PRO   A CG  1 
ATOM   426  C CD  . PRO   A 1 54  ? -6.23418  14.72202 4.93586   1.000 42.57445  ? 54  PRO   A CD  1 
ATOM   427  N N   . MET   A 1 55  ? -3.33909  15.19802 8.56495   1.000 49.94629  ? 55  MET   A N   1 
ATOM   428  C CA  . MET   A 1 55  ? -1.93202  15.38119 8.88596   1.000 42.18541  ? 55  MET   A CA  1 
ATOM   429  C C   . MET   A 1 55  ? -1.65095  14.76408 10.24746  1.000 34.94549  ? 55  MET   A C   1 
ATOM   430  O O   . MET   A 1 55  ? -2.46067  14.88693 11.16979  1.000 36.21798  ? 55  MET   A O   1 
ATOM   431  C CB  . MET   A 1 55  ? -1.54926  16.86640 8.87912   1.000 33.08903  ? 55  MET   A CB  1 
ATOM   432  C CG  . MET   A 1 55  ? -0.06413  17.12528 9.06258   1.000 32.22420  ? 55  MET   A CG  1 
ATOM   433  S SD  . MET   A 1 55  ? 0.94469   16.36215 7.78173   1.000 46.93831  ? 55  MET   A SD  1 
ATOM   434  C CE  . MET   A 1 55  ? 0.37997   17.24787 6.32920   1.000 44.45673  ? 55  MET   A CE  1 
ATOM   435  N N   . SER   A 1 56  ? -0.50195  14.10207 10.36066  1.000 37.86986  ? 56  SER   A N   1 
ATOM   436  C CA  . SER   A 1 56  ? -0.08187  13.46641 11.59967  1.000 33.18846  ? 56  SER   A CA  1 
ATOM   437  C C   . SER   A 1 56  ? 1.40997   13.69866 11.78932  1.000 39.07846  ? 56  SER   A C   1 
ATOM   438  O O   . SER   A 1 56  ? 2.10629   14.17302 10.88694  1.000 47.79961  ? 56  SER   A O   1 
ATOM   439  C CB  . SER   A 1 56  ? -0.39102  11.96489 11.59567  1.000 39.01037  ? 56  SER   A CB  1 
ATOM   440  O OG  . SER   A 1 56  ? 0.41062   11.29045 10.63951  1.000 46.76454  ? 56  SER   A OG  1 
ATOM   441  N N   . PHE   A 1 57  ? 1.90034   13.35623 12.98439  1.000 34.74064  ? 57  PHE   A N   1 
ATOM   442  C CA  . PHE   A 1 57  ? 3.32866   13.48215 13.25955  1.000 32.46280  ? 57  PHE   A CA  1 
ATOM   443  C C   . PHE   A 1 57  ? 4.14608   12.58309 12.33818  1.000 37.99155  ? 57  PHE   A C   1 
ATOM   444  O O   . PHE   A 1 57  ? 5.22661   12.97058 11.87821  1.000 41.40484  ? 57  PHE   A O   1 
ATOM   445  C CB  . PHE   A 1 57  ? 3.61809   13.15062 14.72610  1.000 37.14363  ? 57  PHE   A CB  1 
ATOM   446  C CG  . PHE   A 1 57  ? 3.05518   14.14719 15.70865  1.000 36.82800  ? 57  PHE   A CG  1 
ATOM   447  C CD1 . PHE   A 1 57  ? 2.71684   15.43075 15.31074  1.000 41.42406  ? 57  PHE   A CD1 1 
ATOM   448  C CD2 . PHE   A 1 57  ? 2.87477   13.79666 17.03793  1.000 37.12037  ? 57  PHE   A CD2 1 
ATOM   449  C CE1 . PHE   A 1 57  ? 2.20359   16.34343 16.21992  1.000 33.83178  ? 57  PHE   A CE1 1 
ATOM   450  C CE2 . PHE   A 1 57  ? 2.36342   14.70408 17.95016  1.000 30.52936  ? 57  PHE   A CE2 1 
ATOM   451  C CZ  . PHE   A 1 57  ? 2.02771   15.97850 17.53928  1.000 28.46061  ? 57  PHE   A CZ  1 
ATOM   452  N N   . SER   A 1 58  ? 3.64060   11.37949 12.05084  1.000 44.25194  ? 58  SER   A N   1 
ATOM   453  C CA  . SER   A 1 58  ? 4.35214   10.46504 11.16226  1.000 42.26112  ? 58  SER   A CA  1 
ATOM   454  C C   . SER   A 1 58  ? 4.42808   11.01818 9.74483   1.000 45.41554  ? 58  SER   A C   1 
ATOM   455  O O   . SER   A 1 58  ? 5.42151   10.80318 9.03965   1.000 45.02353  ? 58  SER   A O   1 
ATOM   456  C CB  . SER   A 1 58  ? 3.67052   9.09904  11.16664  1.000 50.62789  ? 58  SER   A CB  1 
ATOM   457  O OG  . SER   A 1 58  ? 2.32739   9.20476  10.72500  1.000 65.52473  ? 58  SER   A OG  1 
ATOM   458  N N   . CYS   A 1 59  ? 3.38347   11.72727 9.30882   1.000 44.96071  ? 59  CYS   A N   1 
ATOM   459  C CA  . CYS   A 1 59  ? 3.40705   12.35019 7.99045   1.000 45.88376  ? 59  CYS   A CA  1 
ATOM   460  C C   . CYS   A 1 59  ? 4.43771   13.46858 7.92137   1.000 40.61944  ? 59  CYS   A C   1 
ATOM   461  O O   . CYS   A 1 59  ? 5.04599   13.68599 6.86774   1.000 51.31509  ? 59  CYS   A O   1 
ATOM   462  C CB  . CYS   A 1 59  ? 2.01877   12.88460 7.63906   1.000 38.50574  ? 59  CYS   A CB  1 
ATOM   463  S SG  . CYS   A 1 59  ? 0.69314   11.65697 7.74039   1.000 57.28425  ? 59  CYS   A SG  1 
ATOM   464  N N   . ILE   A 1 60  ? 4.65166   14.17980 9.02868   1.000 39.28658  ? 60  ILE   A N   1 
ATOM   465  C CA  . ILE   A 1 60  ? 5.63427   15.25756 9.04401   1.000 34.93408  ? 60  ILE   A CA  1 
ATOM   466  C C   . ILE   A 1 60  ? 7.04615   14.70014 9.16091   1.000 37.41300  ? 60  ILE   A C   1 
ATOM   467  O O   . ILE   A 1 60  ? 7.98383   15.22137 8.54548   1.000 42.14884  ? 60  ILE   A O   1 
ATOM   468  C CB  . ILE   A 1 60  ? 5.31033   16.24143 10.18088  1.000 39.31814  ? 60  ILE   A CB  1 
ATOM   469  C CG1 . ILE   A 1 60  ? 3.89961   16.79621 9.99631   1.000 26.29199  ? 60  ILE   A CG1 1 
ATOM   470  C CG2 . ILE   A 1 60  ? 6.32561   17.37132 10.22091  1.000 34.50413  ? 60  ILE   A CG2 1 
ATOM   471  C CD1 . ILE   A 1 60  ? 3.44414   17.68407 11.12039  1.000 23.92268  ? 60  ILE   A CD1 1 
ATOM   472  N N   . LYS   A 1 61  ? 7.22317   13.63473 9.94641   1.000 41.56075  ? 61  LYS   A N   1 
ATOM   473  C CA  . LYS   A 1 61  ? 8.53802   13.00986 10.05016  1.000 37.46798  ? 61  LYS   A CA  1 
ATOM   474  C C   . LYS   A 1 61  ? 8.98196   12.44312 8.70809   1.000 46.00643  ? 61  LYS   A C   1 
ATOM   475  O O   . LYS   A 1 61  ? 10.17059  12.48722 8.36881   1.000 45.24356  ? 61  LYS   A O   1 
ATOM   476  C CB  . LYS   A 1 61  ? 8.51835   11.91841 11.12042  1.000 36.84718  ? 61  LYS   A CB  1 
ATOM   477  C CG  . LYS   A 1 61  ? 8.28171   12.43602 12.53172  1.000 33.55327  ? 61  LYS   A CG  1 
ATOM   478  C CD  . LYS   A 1 61  ? 8.08898   11.28788 13.51517  1.000 40.32358  ? 61  LYS   A CD  1 
ATOM   479  C CE  . LYS   A 1 61  ? 7.82874   11.79764 14.92375  1.000 52.30221  ? 61  LYS   A CE  1 
ATOM   480  N NZ  . LYS   A 1 61  ? 7.61392   10.68291 15.89083  1.000 45.16210  ? 61  LYS   A NZ  1 
ATOM   481  N N   . THR   A 1 62  ? 8.03793   11.91723 7.92409   1.000 40.75365  ? 62  THR   A N   1 
ATOM   482  C CA  . THR   A 1 62  ? 8.38390   11.39749 6.60560   1.000 41.80213  ? 62  THR   A CA  1 
ATOM   483  C C   . THR   A 1 62  ? 8.80346   12.51939 5.66418   1.000 45.55782  ? 62  THR   A C   1 
ATOM   484  O O   . THR   A 1 62  ? 9.80327   12.39349 4.94714   1.000 51.60011  ? 62  THR   A O   1 
ATOM   485  C CB  . THR   A 1 62  ? 7.20688   10.61608 6.02315   1.000 46.18750  ? 62  THR   A CB  1 
ATOM   486  O OG1 . THR   A 1 62  ? 6.94729   9.46526  6.83704   1.000 63.96545  ? 62  THR   A OG1 1 
ATOM   487  C CG2 . THR   A 1 62  ? 7.51324   10.16776 4.60288   1.000 49.54907  ? 62  THR   A CG2 1 
ATOM   488  N N   . LYS   A 1 63  ? 8.05701   13.62765 5.65720   1.000 41.61210  ? 63  LYS   A N   1 
ATOM   489  C CA  . LYS   A 1 63  ? 8.41890   14.75359 4.80114   1.000 47.39296  ? 63  LYS   A CA  1 
ATOM   490  C C   . LYS   A 1 63  ? 9.76235   15.35137 5.19926   1.000 44.81807  ? 63  LYS   A C   1 
ATOM   491  O O   . LYS   A 1 63  ? 10.49702  15.85418 4.34004   1.000 48.87852  ? 63  LYS   A O   1 
ATOM   492  C CB  . LYS   A 1 63  ? 7.32312   15.81874 4.84232   1.000 39.33079  ? 63  LYS   A CB  1 
ATOM   493  C CG  . LYS   A 1 63  ? 5.98460   15.34447 4.29844   1.000 49.68032  ? 63  LYS   A CG  1 
ATOM   494  C CD  . LYS   A 1 63  ? 4.91629   16.42179 4.40908   1.000 48.30772  ? 63  LYS   A CD  1 
ATOM   495  C CE  . LYS   A 1 63  ? 5.26073   17.63491 3.55998   1.000 50.69007  ? 63  LYS   A CE  1 
ATOM   496  N NZ  . LYS   A 1 63  ? 4.18305   18.66508 3.59692   1.000 56.05518  ? 63  LYS   A NZ  1 
ATOM   497  N N   . LEU   A 1 64  ? 10.10127  15.30857 6.49055   1.000 49.27991  ? 64  LEU   A N   1 
ATOM   498  C CA  . LEU   A 1 64  ? 11.42511  15.74862 6.91811   1.000 38.89789  ? 64  LEU   A CA  1 
ATOM   499  C C   . LEU   A 1 64  ? 12.50313  14.78132 6.44700   1.000 44.98175  ? 64  LEU   A C   1 
ATOM   500  O O   . LEU   A 1 64  ? 13.58417  15.20576 6.02220   1.000 49.29970  ? 64  LEU   A O   1 
ATOM   501  C CB  . LEU   A 1 64  ? 11.46623  15.89454 8.43927   1.000 37.91096  ? 64  LEU   A CB  1 
ATOM   502  C CG  . LEU   A 1 64  ? 10.80007  17.13331 9.03828   1.000 37.19762  ? 64  LEU   A CG  1 
ATOM   503  C CD1 . LEU   A 1 64  ? 10.74064  17.02909 10.55301  1.000 39.13518  ? 64  LEU   A CD1 1 
ATOM   504  C CD2 . LEU   A 1 64  ? 11.55403  18.38284 8.61863   1.000 35.91889  ? 64  LEU   A CD2 1 
ATOM   505  N N   . LYS   A 1 65  ? 12.22512  13.47655 6.51400   1.000 50.66910  ? 65  LYS   A N   1 
ATOM   506  C CA  . LYS   A 1 65  ? 13.21104  12.48544 6.09547   1.000 47.44327  ? 65  LYS   A CA  1 
ATOM   507  C C   . LYS   A 1 65  ? 13.44535  12.53893 4.59103   1.000 58.56125  ? 65  LYS   A C   1 
ATOM   508  O O   . LYS   A 1 65  ? 14.57587  12.35135 4.12610   1.000 64.66177  ? 65  LYS   A O   1 
ATOM   509  C CB  . LYS   A 1 65  ? 12.76196  11.08728 6.52302   1.000 48.42581  ? 65  LYS   A CB  1 
ATOM   510  C CG  . LYS   A 1 65  ? 13.79652  9.99907  6.27895   1.000 67.36018  ? 65  LYS   A CG  1 
ATOM   511  C CD  . LYS   A 1 65  ? 13.30996  8.64482  6.77201   1.000 72.94572  ? 65  LYS   A CD  1 
ATOM   512  C CE  . LYS   A 1 65  ? 14.36610  7.56899  6.56227   1.000 66.52516  ? 65  LYS   A CE  1 
ATOM   513  N N   . LYS   A 1 66  ? 12.39490  12.79510 3.81588   1.000 57.23572  ? 66  LYS   A N   1 
ATOM   514  C CA  . LYS   A 1 66  ? 12.50731  12.88456 2.36724   1.000 43.80191  ? 66  LYS   A CA  1 
ATOM   515  C C   . LYS   A 1 66  ? 12.86630  14.28301 1.88301   1.000 43.59989  ? 66  LYS   A C   1 
ATOM   516  O O   . LYS   A 1 66  ? 12.93594  14.50018 0.67002   1.000 54.75846  ? 66  LYS   A O   1 
ATOM   517  C CB  . LYS   A 1 66  ? 11.20171  12.42849 1.70575   1.000 51.30255  ? 66  LYS   A CB  1 
ATOM   518  C CG  . LYS   A 1 66  ? 10.89855  10.95119 1.90377   1.000 63.56215  ? 66  LYS   A CG  1 
ATOM   519  C CD  . LYS   A 1 66  ? 9.65574   10.52629 1.13878   1.000 61.81803  ? 66  LYS   A CD  1 
ATOM   520  C CE  . LYS   A 1 66  ? 9.38711   9.03956  1.31207   1.000 65.62705  ? 66  LYS   A CE  1 
ATOM   521  N NZ  . LYS   A 1 66  ? 8.15680   8.60644  0.59336   1.000 78.62909  ? 66  LYS   A NZ  1 
ATOM   522  N N   . GLY   A 1 67  ? 13.09789  15.22695 2.78999   1.000 46.21607  ? 67  GLY   A N   1 
ATOM   523  C CA  . GLY   A 1 67  ? 13.48884  16.56808 2.38234   1.000 47.79284  ? 67  GLY   A CA  1 
ATOM   524  C C   . GLY   A 1 67  ? 12.43177  17.30052 1.58547   1.000 39.30375  ? 67  GLY   A C   1 
ATOM   525  O O   . GLY   A 1 67  ? 12.75419  17.96924 0.59537   1.000 44.60152  ? 67  GLY   A O   1 
ATOM   526  N N   . GLN   A 1 68  ? 11.17148  17.19478 1.99833   1.000 42.14806  ? 68  GLN   A N   1 
ATOM   527  C CA  . GLN   A 1 68  ? 10.05833  17.78688 1.27158   1.000 43.54887  ? 68  GLN   A CA  1 
ATOM   528  C C   . GLN   A 1 68  ? 9.61361   19.12613 1.84821   1.000 44.40124  ? 68  GLN   A C   1 
ATOM   529  O O   . GLN   A 1 68  ? 8.53435   19.61143 1.49446   1.000 72.36372  ? 68  GLN   A O   1 
ATOM   530  C CB  . GLN   A 1 68  ? 8.88292   16.80993 1.23499   1.000 40.29019  ? 68  GLN   A CB  1 
ATOM   531  C CG  . GLN   A 1 68  ? 9.15322   15.58430 0.38061   1.000 51.07182  ? 68  GLN   A CG  1 
ATOM   532  C CD  . GLN   A 1 68  ? 8.04541   14.56132 0.46296   1.000 53.01216  ? 68  GLN   A CD  1 
ATOM   533  O OE1 . GLN   A 1 68  ? 7.22622   14.58885 1.38086   1.000 62.45282  ? 68  GLN   A OE1 1 
ATOM   534  N NE2 . GLN   A 1 68  ? 8.01136   13.64924 -0.50082  1.000 83.89319  ? 68  GLN   A NE2 1 
ATOM   535  N N   . TYR   A 1 69  ? 10.41447  19.73453 2.72039   1.000 48.24941  ? 69  TYR   A N   1 
ATOM   536  C CA  . TYR   A 1 69  ? 10.15268  21.07617 3.22862   1.000 45.49935  ? 69  TYR   A CA  1 
ATOM   537  C C   . TYR   A 1 69  ? 11.19008  22.03096 2.65338   1.000 44.86134  ? 69  TYR   A C   1 
ATOM   538  O O   . TYR   A 1 69  ? 12.39510  21.82855 2.83720   1.000 50.14090  ? 69  TYR   A O   1 
ATOM   539  C CB  . TYR   A 1 69  ? 10.17910  21.11130 4.75691   1.000 48.11876  ? 69  TYR   A CB  1 
ATOM   540  C CG  . TYR   A 1 69  ? 8.98379   20.45400 5.40612   1.000 43.31245  ? 69  TYR   A CG  1 
ATOM   541  C CD1 . TYR   A 1 69  ? 7.71586   21.00727 5.28922   1.000 44.02959  ? 69  TYR   A CD1 1 
ATOM   542  C CD2 . TYR   A 1 69  ? 9.12398   19.28587 6.14453   1.000 37.99423  ? 69  TYR   A CD2 1 
ATOM   543  C CE1 . TYR   A 1 69  ? 6.61814   20.41008 5.88333   1.000 40.80188  ? 69  TYR   A CE1 1 
ATOM   544  C CE2 . TYR   A 1 69  ? 8.03437   18.68430 6.74275   1.000 35.09483  ? 69  TYR   A CE2 1 
ATOM   545  C CZ  . TYR   A 1 69  ? 6.78423   19.24954 6.60854   1.000 35.03018  ? 69  TYR   A CZ  1 
ATOM   546  O OH  . TYR   A 1 69  ? 5.69790   18.65239 7.19965   1.000 36.76610  ? 69  TYR   A OH  1 
ATOM   547  N N   . ALA   A 1 70  ? 10.71841  23.06775 1.96008   1.000 49.12610  ? 70  ALA   A N   1 
ATOM   548  C CA  . ALA   A 1 70  ? 11.59152  24.07356 1.36663   1.000 59.48280  ? 70  ALA   A CA  1 
ATOM   549  C C   . ALA   A 1 70  ? 11.85818  25.24403 2.30583   1.000 58.66255  ? 70  ALA   A C   1 
ATOM   550  O O   . ALA   A 1 70  ? 12.97251  25.77853 2.32708   1.000 63.63976  ? 70  ALA   A O   1 
ATOM   551  C CB  . ALA   A 1 70  ? 10.98634  24.59144 0.06013   1.000 60.75470  ? 70  ALA   A CB  1 
ATOM   552  N N   . TYR   A 1 71  ? 10.85483  25.66020 3.07542   1.000 44.17278  ? 71  TYR   A N   1 
ATOM   553  C CA  . TYR   A 1 71  ? 10.97414  26.75971 4.01697   1.000 52.30352  ? 71  TYR   A CA  1 
ATOM   554  C C   . TYR   A 1 71  ? 10.66703  26.27704 5.42936   1.000 45.35989  ? 71  TYR   A C   1 
ATOM   555  O O   . TYR   A 1 71  ? 9.90957   25.31797 5.60878   1.000 46.54977  ? 71  TYR   A O   1 
ATOM   556  C CB  . TYR   A 1 71  ? 10.01790  27.90624 3.66190   1.000 56.75671  ? 71  TYR   A CB  1 
ATOM   557  C CG  . TYR   A 1 71  ? 10.29673  28.57713 2.33517   1.000 65.60903  ? 71  TYR   A CG  1 
ATOM   558  C CD1 . TYR   A 1 71  ? 11.31806  29.50817 2.20795   1.000 74.19763  ? 71  TYR   A CD1 1 
ATOM   559  C CD2 . TYR   A 1 71  ? 9.52638   28.29328 1.21502   1.000 68.64831  ? 71  TYR   A CD2 1 
ATOM   560  C CE1 . TYR   A 1 71  ? 11.57227  30.13152 1.00095   1.000 72.89193  ? 71  TYR   A CE1 1 
ATOM   561  C CE2 . TYR   A 1 71  ? 9.77361   28.91104 0.00282   1.000 73.22058  ? 71  TYR   A CE2 1 
ATOM   562  C CZ  . TYR   A 1 71  ? 10.79786  29.82912 -0.09783  1.000 73.38222  ? 71  TYR   A CZ  1 
ATOM   563  O OH  . TYR   A 1 71  ? 11.04845  30.44849 -1.30027  1.000 90.32952  ? 71  TYR   A OH  1 
ATOM   564  N N   . PRO   A 1 72  ? 11.24098  26.91414 6.45485   1.000 46.13483  ? 72  PRO   A N   1 
ATOM   565  C CA  . PRO   A 1 72  ? 10.86808  26.55226 7.83180   1.000 42.35378  ? 72  PRO   A CA  1 
ATOM   566  C C   . PRO   A 1 72  ? 9.41784   26.85708 8.16875   1.000 41.09738  ? 72  PRO   A C   1 
ATOM   567  O O   . PRO   A 1 72  ? 8.87164   26.23737 9.09061   1.000 40.14802  ? 72  PRO   A O   1 
ATOM   568  C CB  . PRO   A 1 72  ? 11.83092  27.38296 8.69324   1.000 41.43355  ? 72  PRO   A CB  1 
ATOM   569  C CG  . PRO   A 1 72  ? 12.31719  28.47227 7.79777   1.000 42.55667  ? 72  PRO   A CG  1 
ATOM   570  C CD  . PRO   A 1 72  ? 12.34581  27.88673 6.41844   1.000 44.63781  ? 72  PRO   A CD  1 
ATOM   571  N N   . SER   A 1 73  ? 8.77392   27.78096 7.45175   1.000 39.41262  ? 73  SER   A N   1 
ATOM   572  C CA  . SER   A 1 73  ? 7.36803   28.07310 7.70577   1.000 38.50574  ? 73  SER   A CA  1 
ATOM   573  C C   . SER   A 1 73  ? 6.45279   26.94424 7.25234   1.000 34.31399  ? 73  SER   A C   1 
ATOM   574  O O   . SER   A 1 73  ? 5.32141   26.84732 7.74033   1.000 38.68412  ? 73  SER   A O   1 
ATOM   575  C CB  . SER   A 1 73  ? 6.96575   29.37353 7.01037   1.000 44.77706  ? 73  SER   A CB  1 
ATOM   576  O OG  . SER   A 1 73  ? 7.00919   29.22745 5.60161   1.000 46.57916  ? 73  SER   A OG  1 
ATOM   577  N N   . GLU   A 1 74  ? 6.91435   26.09715 6.32841   1.000 40.27129  ? 74  GLU   A N   1 
ATOM   578  C CA  . GLU   A 1 74  ? 6.11508   24.97318 5.85314   1.000 45.09312  ? 74  GLU   A CA  1 
ATOM   579  C C   . GLU   A 1 74  ? 5.99526   23.87045 6.89443   1.000 40.41409  ? 74  GLU   A C   1 
ATOM   580  O O   . GLU   A 1 74  ? 4.95901   23.20001 6.96280   1.000 41.55825  ? 74  GLU   A O   1 
ATOM   581  C CB  . GLU   A 1 74  ? 6.72022   24.41159 4.56591   1.000 46.49353  ? 74  GLU   A CB  1 
ATOM   582  C CG  . GLU   A 1 74  ? 6.77639   25.41857 3.43122   1.000 43.09891  ? 74  GLU   A CG  1 
ATOM   583  C CD  . GLU   A 1 74  ? 7.44710   24.86789 2.19064   1.000 63.34891  ? 74  GLU   A CD  1 
ATOM   584  O OE1 . GLU   A 1 74  ? 7.93918   23.71770 2.22731   1.000 61.21926  ? 74  GLU   A OE1 1 
ATOM   585  O OE2 . GLU   A 1 74  ? 7.48052   25.59431 1.17669   1.000 86.41314  ? 74  GLU   A OE2 1 
ATOM   586  N N   . PHE   A 1 75  ? 7.03948   23.66574 7.69965   1.000 36.56395  ? 75  PHE   A N   1 
ATOM   587  C CA  . PHE   A 1 75  ? 6.96522   22.68611 8.77931   1.000 34.39491  ? 75  PHE   A CA  1 
ATOM   588  C C   . PHE   A 1 75  ? 5.92291   23.09239 9.80998   1.000 39.79105  ? 75  PHE   A C   1 
ATOM   589  O O   . PHE   A 1 75  ? 5.12644   22.26114 10.26258  1.000 33.46113  ? 75  PHE   A O   1 
ATOM   590  C CB  . PHE   A 1 75  ? 8.34293   22.52482 9.43119   1.000 31.00875  ? 75  PHE   A CB  1 
ATOM   591  C CG  . PHE   A 1 75  ? 8.32756   21.78307 10.74666  1.000 28.38167  ? 75  PHE   A CG  1 
ATOM   592  C CD1 . PHE   A 1 75  ? 8.26471   20.39865 10.78177  1.000 32.05123  ? 75  PHE   A CD1 1 
ATOM   593  C CD2 . PHE   A 1 75  ? 8.40559   22.47351 11.94728  1.000 30.18264  ? 75  PHE   A CD2 1 
ATOM   594  C CE1 . PHE   A 1 75  ? 8.25999   19.71893 11.99036  1.000 27.97164  ? 75  PHE   A CE1 1 
ATOM   595  C CE2 . PHE   A 1 75  ? 8.40302   21.79733 13.15736  1.000 28.68073  ? 75  PHE   A CE2 1 
ATOM   596  C CZ  . PHE   A 1 75  ? 8.32909   20.41948 13.17779  1.000 33.31518  ? 75  PHE   A CZ  1 
ATOM   597  N N   . VAL   A 1 76  ? 5.90384   24.37376 10.17983  1.000 30.78867  ? 76  VAL   A N   1 
ATOM   598  C CA  . VAL   A 1 76  ? 4.94631   24.85025 11.17071  1.000 31.61181  ? 76  VAL   A CA  1 
ATOM   599  C C   . VAL   A 1 76  ? 3.52034   24.71923 10.64837  1.000 33.11157  ? 76  VAL   A C   1 
ATOM   600  O O   . VAL   A 1 76  ? 2.59664   24.39475 11.40580  1.000 34.30450  ? 76  VAL   A O   1 
ATOM   601  C CB  . VAL   A 1 76  ? 5.27877   26.29949 11.57140  1.000 32.99966  ? 76  VAL   A CB  1 
ATOM   602  C CG1 . VAL   A 1 76  ? 4.29602   26.80549 12.60953  1.000 30.23312  ? 76  VAL   A CG1 1 
ATOM   603  C CG2 . VAL   A 1 76  ? 6.70460   26.38594 12.09922  1.000 27.82016  ? 76  VAL   A CG2 1 
ATOM   604  N N   . LYS   A 1 77  ? 3.31623   24.95660 9.34876   1.000 34.97140  ? 77  LYS   A N   1 
ATOM   605  C CA  . LYS   A 1 77  ? 1.97046   24.87377 8.78634   1.000 36.85400  ? 77  LYS   A CA  1 
ATOM   606  C C   . LYS   A 1 77  ? 1.41506   23.45830 8.87812   1.000 37.45900  ? 77  LYS   A C   1 
ATOM   607  O O   . LYS   A 1 77  ? 0.22355   23.26850 9.14999   1.000 41.55587  ? 77  LYS   A O   1 
ATOM   608  C CB  . LYS   A 1 77  ? 1.97132   25.35457 7.33613   1.000 45.97640  ? 77  LYS   A CB  1 
ATOM   609  C CG  . LYS   A 1 77  ? 1.54268   26.80201 7.16223   1.000 51.35273  ? 77  LYS   A CG  1 
ATOM   610  C CD  . LYS   A 1 77  ? 1.54793   27.22654 5.69760   1.000 52.69314  ? 77  LYS   A CD  1 
ATOM   611  C CE  . LYS   A 1 77  ? 0.64136   26.35165 4.84117   1.000 64.62264  ? 77  LYS   A CE  1 
ATOM   612  N NZ  . LYS   A 1 77  ? 1.37340   25.22098 4.19823   1.000 53.62998  ? 77  LYS   A NZ  1 
ATOM   613  N N   . ASP   A 1 78  ? 2.26288   22.45064 8.65543   1.000 32.62055  ? 78  ASP   A N   1 
ATOM   614  C CA  . ASP   A 1 78  ? 1.80829   21.06862 8.77451   1.000 41.95626  ? 78  ASP   A CA  1 
ATOM   615  C C   . ASP   A 1 78  ? 1.50617   20.70731 10.22501  1.000 41.87055  ? 78  ASP   A C   1 
ATOM   616  O O   . ASP   A 1 78  ? 0.52483   20.00784 10.50334  1.000 37.00589  ? 78  ASP   A O   1 
ATOM   617  C CB  . ASP   A 1 78  ? 2.84816   20.11767 8.18120   1.000 32.99889  ? 78  ASP   A CB  1 
ATOM   618  C CG  . ASP   A 1 78  ? 2.72792   19.98591 6.67082   1.000 43.72486  ? 78  ASP   A CG  1 
ATOM   619  O OD1 . ASP   A 1 78  ? 1.84996   20.64695 6.07533   1.000 47.44907  ? 78  ASP   A OD1 1 
ATOM   620  O OD2 . ASP   A 1 78  ? 3.51169   19.21310 6.07826   1.000 42.34432  ? 78  ASP   A OD2 1 
ATOM   621  N N   . VAL   A 1 79  ? 2.33163   21.17575 11.16464  1.000 35.62188  ? 79  VAL   A N   1 
ATOM   622  C CA  . VAL   A 1 79  ? 2.04210   20.94405 12.57662  1.000 34.99525  ? 79  VAL   A CA  1 
ATOM   623  C C   . VAL   A 1 79  ? 0.76542   21.66953 12.98283  1.000 27.68207  ? 79  VAL   A C   1 
ATOM   624  O O   . VAL   A 1 79  ? -0.09770  21.10068 13.66150  1.000 29.44293  ? 79  VAL   A O   1 
ATOM   625  C CB  . VAL   A 1 79  ? 3.23875   21.36502 13.45129  1.000 25.91069  ? 79  VAL   A CB  1 
ATOM   626  C CG1 . VAL   A 1 79  ? 2.91451   21.17633 14.92774  1.000 24.93545  ? 79  VAL   A CG1 1 
ATOM   627  C CG2 . VAL   A 1 79  ? 4.47741   20.57289 13.07160  1.000 24.36577  ? 79  VAL   A CG2 1 
ATOM   628  N N   . GLN   A 1 80  ? 0.61533   22.92974 12.56327  1.000 29.21037  ? 80  GLN   A N   1 
ATOM   629  C CA  . GLN   A 1 80  ? -0.58223  23.68605 12.91497  1.000 32.59734  ? 80  GLN   A CA  1 
ATOM   630  C C   . GLN   A 1 80  ? -1.82885  23.08815 12.27675  1.000 27.02280  ? 80  GLN   A C   1 
ATOM   631  O O   . GLN   A 1 80  ? -2.92854  23.21387 12.82766  1.000 36.79378  ? 80  GLN   A O   1 
ATOM   632  C CB  . GLN   A 1 80  ? -0.42325  25.14870 12.50289  1.000 29.69101  ? 80  GLN   A CB  1 
ATOM   633  C CG  . GLN   A 1 80  ? -1.55195  26.04636 12.98217  1.000 38.32714  ? 80  GLN   A CG  1 
ATOM   634  C CD  . GLN   A 1 80  ? -1.69114  26.04485 14.49291  1.000 32.46784  ? 80  GLN   A CD  1 
ATOM   635  O OE1 . GLN   A 1 80  ? -0.70672  26.17734 15.21985  1.000 34.40532  ? 80  GLN   A OE1 1 
ATOM   636  N NE2 . GLN   A 1 80  ? -2.91963  25.88908 14.97367  1.000 35.43160  ? 80  GLN   A NE2 1 
ATOM   637  N N   . LEU   A 1 81  ? -1.67820  22.43792 11.12157  1.000 33.77273  ? 81  LEU   A N   1 
ATOM   638  C CA  . LEU   A 1 81  ? -2.81672  21.78511 10.48578  1.000 37.66479  ? 81  LEU   A CA  1 
ATOM   639  C C   . LEU   A 1 81  ? -3.37101  20.67404 11.36715  1.000 33.52823  ? 81  LEU   A C   1 
ATOM   640  O O   . LEU   A 1 81  ? -4.58964  20.47038 11.43170  1.000 36.27618  ? 81  LEU   A O   1 
ATOM   641  C CB  . LEU   A 1 81  ? -2.40651  21.24144 9.11739   1.000 32.67097  ? 81  LEU   A CB  1 
ATOM   642  C CG  . LEU   A 1 81  ? -3.44967  20.43288 8.34809   1.000 37.12581  ? 81  LEU   A CG  1 
ATOM   643  C CD1 . LEU   A 1 81  ? -4.68846  21.26948 8.05766   1.000 35.26085  ? 81  LEU   A CD1 1 
ATOM   644  C CD2 . LEU   A 1 81  ? -2.84180  19.89715 7.06245   1.000 34.74282  ? 81  LEU   A CD2 1 
ATOM   645  N N   . ILE   A 1 82  ? -2.48970  19.94928 12.05981  1.000 32.07537  ? 82  ILE   A N   1 
ATOM   646  C CA  . ILE   A 1 82  ? -2.94027  18.92027 12.99292  1.000 24.81586  ? 82  ILE   A CA  1 
ATOM   647  C C   . ILE   A 1 82  ? -3.82188  19.53630 14.06978  1.000 27.40317  ? 82  ILE   A C   1 
ATOM   648  O O   . ILE   A 1 82  ? -4.89933  19.02066 14.39068  1.000 34.59294  ? 82  ILE   A O   1 
ATOM   649  C CB  . ILE   A 1 82  ? -1.73444  18.19057 13.60947  1.000 29.40096  ? 82  ILE   A CB  1 
ATOM   650  C CG1 . ILE   A 1 82  ? -0.88524  17.54531 12.51630  1.000 34.73800  ? 82  ILE   A CG1 1 
ATOM   651  C CG2 . ILE   A 1 82  ? -2.20319  17.15024 14.60449  1.000 25.99875  ? 82  ILE   A CG2 1 
ATOM   652  C CD1 . ILE   A 1 82  ? 0.39223   16.92871 13.02825  1.000 27.37130  ? 82  ILE   A CD1 1 
ATOM   653  N N   . PHE   A 1 83  ? -3.37702  20.65744 14.63867  1.000 35.66125  ? 83  PHE   A N   1 
ATOM   654  C CA  . PHE   A 1 83  ? -4.13639  21.29867 15.70410  1.000 21.98261  ? 83  PHE   A CA  1 
ATOM   655  C C   . PHE   A 1 83  ? -5.39735  21.96574 15.16965  1.000 37.67616  ? 83  PHE   A C   1 
ATOM   656  O O   . PHE   A 1 83  ? -6.38150  22.10741 15.90494  1.000 32.99491  ? 83  PHE   A O   1 
ATOM   657  C CB  . PHE   A 1 83  ? -3.25326  22.31354 16.42899  1.000 21.80413  ? 83  PHE   A CB  1 
ATOM   658  C CG  . PHE   A 1 83  ? -1.95469  21.73986 16.92724  1.000 27.59126  ? 83  PHE   A CG  1 
ATOM   659  C CD1 . PHE   A 1 83  ? -1.88764  20.43556 17.38927  1.000 29.73693  ? 83  PHE   A CD1 1 
ATOM   660  C CD2 . PHE   A 1 83  ? -0.79965  22.50319 16.92571  1.000 31.22503  ? 83  PHE   A CD2 1 
ATOM   661  C CE1 . PHE   A 1 83  ? -0.69495  19.90534 17.84458  1.000 26.81224  ? 83  PHE   A CE1 1 
ATOM   662  C CE2 . PHE   A 1 83  ? 0.39695   21.97887 17.38047  1.000 31.51786  ? 83  PHE   A CE2 1 
ATOM   663  C CZ  . PHE   A 1 83  ? 0.44921   20.67769 17.84138  1.000 23.53734  ? 83  PHE   A CZ  1 
ATOM   664  N N   . ASP   A 1 84  ? -5.39195  22.37422 13.89943  1.000 32.29510  ? 84  ASP   A N   1 
ATOM   665  C CA  . ASP   A 1 84  ? -6.58771  22.95920 13.30364  1.000 28.86989  ? 84  ASP   A CA  1 
ATOM   666  C C   . ASP   A 1 84  ? -7.62593  21.89512 12.97555  1.000 37.22666  ? 84  ASP   A C   1 
ATOM   667  O O   . ASP   A 1 84  ? -8.82709  22.12008 13.16017  1.000 35.31036  ? 84  ASP   A O   1 
ATOM   668  C CB  . ASP   A 1 84  ? -6.21803  23.74996 12.05119  1.000 30.31499  ? 84  ASP   A CB  1 
ATOM   669  C CG  . ASP   A 1 84  ? -5.45641  25.01569 12.37175  1.000 44.71148  ? 84  ASP   A CG  1 
ATOM   670  O OD1 . ASP   A 1 84  ? -5.33096  25.34252 13.57110  1.000 37.97255  ? 84  ASP   A OD1 1 
ATOM   671  O OD2 . ASP   A 1 84  ? -4.98517  25.68371 11.42761  1.000 48.96962  ? 84  ASP   A OD2 1 
ATOM   672  N N   . ASN   A 1 85  ? -7.18719  20.73520 12.48260  1.000 28.58500  ? 85  ASN   A N   1 
ATOM   673  C CA  . ASN   A 1 85  ? -8.12213  19.63455 12.28146  1.000 33.12813  ? 85  ASN   A CA  1 
ATOM   674  C C   . ASN   A 1 85  ? -8.68047  19.14111 13.60798  1.000 26.59751  ? 85  ASN   A C   1 
ATOM   675  O O   . ASN   A 1 85  ? -9.83410  18.69787 13.67101  1.000 34.92667  ? 85  ASN   A O   1 
ATOM   676  C CB  . ASN   A 1 85  ? -7.44157  18.48982 11.53023  1.000 30.96787  ? 85  ASN   A CB  1 
ATOM   677  C CG  . ASN   A 1 85  ? -7.05893  18.86686 10.11125  1.000 36.44101  ? 85  ASN   A CG  1 
ATOM   678  O OD1 . ASN   A 1 85  ? -7.64090  19.77447 9.51657   1.000 42.33430  ? 85  ASN   A OD1 1 
ATOM   679  N ND2 . ASN   A 1 85  ? -6.07841  18.16343 9.55851   1.000 36.33092  ? 85  ASN   A ND2 1 
ATOM   680  N N   . CYS   A 1 86  ? -7.88167  19.21898 14.67492  1.000 27.86820  ? 86  CYS   A N   1 
ATOM   681  C CA  . CYS   A 1 86  ? -8.35432  18.81375 15.99352  1.000 24.60286  ? 86  CYS   A CA  1 
ATOM   682  C C   . CYS   A 1 86  ? -9.41553  19.77134 16.51666  1.000 30.69628  ? 86  CYS   A C   1 
ATOM   683  O O   . CYS   A 1 86  ? -10.44715 19.33891 17.04294  1.000 30.86252  ? 86  CYS   A O   1 
ATOM   684  C CB  . CYS   A 1 86  ? -7.17825  18.73414 16.96753  1.000 22.69928  ? 86  CYS   A CB  1 
ATOM   685  S SG  . CYS   A 1 86  ? -7.60495  18.13402 18.61076  1.000 35.03457  ? 86  CYS   A SG  1 
ATOM   686  N N   . SER   A 1 87  ? -9.18244  21.07635 16.37808  1.000 31.60545  ? 87  SER   A N   1 
ATOM   687  C CA  . SER   A 1 87  ? -10.13998 22.05767 16.87071  1.000 31.85812  ? 87  SER   A CA  1 
ATOM   688  C C   . SER   A 1 87  ? -11.41592 22.09073 16.04235  1.000 34.30790  ? 87  SER   A C   1 
ATOM   689  O O   . SER   A 1 87  ? -12.43307 22.60251 16.52037  1.000 44.46674  ? 87  SER   A O   1 
ATOM   690  C CB  . SER   A 1 87  ? -9.49792  23.44344 16.89561  1.000 25.74033  ? 87  SER   A CB  1 
ATOM   691  O OG  . SER   A 1 87  ? -9.22521  23.88826 15.57907  1.000 40.33349  ? 87  SER   A OG  1 
ATOM   692  N N   . LEU   A 1 88  ? -11.38580 21.55918 14.81952  1.000 33.58813  ? 88  LEU   A N   1 
ATOM   693  C CA  . LEU   A 1 88  ? -12.55704 21.52093 13.94764  1.000 30.92837  ? 88  LEU   A CA  1 
ATOM   694  C C   . LEU   A 1 88  ? -13.46481 20.33418 14.25942  1.000 38.10800  ? 88  LEU   A C   1 
ATOM   695  O O   . LEU   A 1 88  ? -14.64580 20.51487 14.57098  1.000 41.14726  ? 88  LEU   A O   1 
ATOM   696  C CB  . LEU   A 1 88  ? -12.12598 21.47938 12.47535  1.000 34.56645  ? 88  LEU   A CB  1 
ATOM   697  C CG  . LEU   A 1 88  ? -13.26687 21.34025 11.46262  1.000 34.37508  ? 88  LEU   A CG  1 
ATOM   698  C CD1 . LEU   A 1 88  ? -14.27670 22.46870 11.62405  1.000 31.18713  ? 88  LEU   A CD1 1 
ATOM   699  C CD2 . LEU   A 1 88  ? -12.74103 21.29012 10.03056  1.000 43.25046  ? 88  LEU   A CD2 1 
ATOM   700  N N   . TYR   A 1 89  ? -12.92422 19.11722 14.17542  1.000 33.77659  ? 89  TYR   A N   1 
ATOM   701  C CA  . TYR   A 1 89  ? -13.76216 17.92840 14.29938  1.000 45.91987  ? 89  TYR   A CA  1 
ATOM   702  C C   . TYR   A 1 89  ? -14.24892 17.71188 15.72656  1.000 38.67775  ? 89  TYR   A C   1 
ATOM   703  O O   . TYR   A 1 89  ? -15.36508 17.21932 15.92735  1.000 44.44776  ? 89  TYR   A O   1 
ATOM   704  C CB  . TYR   A 1 89  ? -13.00398 16.69088 13.81157  1.000 36.35652  ? 89  TYR   A CB  1 
ATOM   705  C CG  . TYR   A 1 89  ? -13.80682 15.40928 13.89478  1.000 46.24130  ? 89  TYR   A CG  1 
ATOM   706  C CD1 . TYR   A 1 89  ? -14.66776 15.03728 12.86951  1.000 48.28414  ? 89  TYR   A CD1 1 
ATOM   707  C CD2 . TYR   A 1 89  ? -13.70520 14.57197 14.99984  1.000 45.86255  ? 89  TYR   A CD2 1 
ATOM   708  C CE1 . TYR   A 1 89  ? -15.40664 13.86820 12.94401  1.000 55.54474  ? 89  TYR   A CE1 1 
ATOM   709  C CE2 . TYR   A 1 89  ? -14.44031 13.40204 15.08246  1.000 52.16017  ? 89  TYR   A CE2 1 
ATOM   710  C CZ  . TYR   A 1 89  ? -15.28793 13.05558 14.05212  1.000 58.88071  ? 89  TYR   A CZ  1 
ATOM   711  O OH  . TYR   A 1 89  ? -16.01896 11.89347 14.13044  1.000 72.42231  ? 89  TYR   A OH  1 
ATOM   712  N N   . ASN   A 1 90  ? -13.44052 18.06228 16.72242  1.000 33.79031  ? 90  ASN   A N   1 
ATOM   713  C CA  . ASN   A 1 90  ? -13.73632 17.74401 18.11249  1.000 39.15889  ? 90  ASN   A CA  1 
ATOM   714  C C   . ASN   A 1 90  ? -14.42233 18.91159 18.81042  1.000 36.58016  ? 90  ASN   A C   1 
ATOM   715  O O   . ASN   A 1 90  ? -14.08165 20.07648 18.58070  1.000 34.98575  ? 90  ASN   A O   1 
ATOM   716  C CB  . ASN   A 1 90  ? -12.45695 17.36843 18.86076  1.000 36.64925  ? 90  ASN   A CB  1 
ATOM   717  C CG  . ASN   A 1 90  ? -11.68760 16.25739 18.17314  1.000 36.24465  ? 90  ASN   A CG  1 
ATOM   718  O OD1 . ASN   A 1 90  ? -12.03563 15.08179 18.29090  1.000 44.25916  ? 90  ASN   A OD1 1 
ATOM   719  N ND2 . ASN   A 1 90  ? -10.63457 16.62373 17.45240  1.000 28.21797  ? 90  ASN   A ND2 1 
ATOM   720  N N   . THR   A 1 91  ? -15.38852 18.58466 19.66724  1.000 33.46247  ? 91  THR   A N   1 
ATOM   721  C CA  . THR   A 1 91  ? -16.08881 19.58869 20.45683  1.000 27.12516  ? 91  THR   A CA  1 
ATOM   722  C C   . THR   A 1 91  ? -15.14279 20.23217 21.46548  1.000 23.00249  ? 91  THR   A C   1 
ATOM   723  O O   . THR   A 1 91  ? -14.17616 19.61765 21.92421  1.000 29.38280  ? 91  THR   A O   1 
ATOM   724  C CB  . THR   A 1 91  ? -17.27986 18.96080 21.18221  1.000 23.46734  ? 91  THR   A CB  1 
ATOM   725  O OG1 . THR   A 1 91  ? -16.83621 17.83649 21.95191  1.000 44.14381  ? 91  THR   A OG1 1 
ATOM   726  C CG2 . THR   A 1 91  ? -18.32783 18.49746 20.18146  1.000 28.25760  ? 91  THR   A CG2 1 
ATOM   727  N N   . SER   A 1 92  ? -15.44337 21.48418 21.82303  1.000 39.79484  ? 92  SER   A N   1 
ATOM   728  C CA  . SER   A 1 92  ? -14.50695 22.29616 22.59664  1.000 35.49316  ? 92  SER   A CA  1 
ATOM   729  C C   . SER   A 1 92  ? -14.25395 21.75276 23.99892  1.000 34.95898  ? 92  SER   A C   1 
ATOM   730  O O   . SER   A 1 92  ? -13.20400 22.04762 24.58080  1.000 33.09812  ? 92  SER   A O   1 
ATOM   731  C CB  . SER   A 1 92  ? -15.01273 23.73810 22.68303  1.000 36.86716  ? 92  SER   A CB  1 
ATOM   732  O OG  . SER   A 1 92  ? -16.32046 23.79327 23.22480  1.000 70.18252  ? 92  SER   A OG  1 
ATOM   733  N N   . ASN   A 1 93  ? -15.17843 20.97501 24.55996  1.000 37.59582  ? 93  ASN   A N   1 
ATOM   734  C CA  . ASN   A 1 93  ? -15.00572 20.41748 25.89526  1.000 29.48503  ? 93  ASN   A CA  1 
ATOM   735  C C   . ASN   A 1 93  ? -14.59453 18.94983 25.87584  1.000 30.36166  ? 93  ASN   A C   1 
ATOM   736  O O   . ASN   A 1 93  ? -14.60019 18.30182 26.92785  1.000 29.29211  ? 93  ASN   A O   1 
ATOM   737  C CB  . ASN   A 1 93  ? -16.28566 20.59496 26.71751  1.000 27.76856  ? 93  ASN   A CB  1 
ATOM   738  C CG  . ASN   A 1 93  ? -17.51163 20.01964 26.03376  1.000 26.33067  ? 93  ASN   A CG  1 
ATOM   739  O OD1 . ASN   A 1 93  ? -17.40990 19.32365 25.02395  1.000 28.85498  ? 93  ASN   A OD1 1 
ATOM   740  N ND2 . ASN   A 1 93  ? -18.68336 20.30324 26.59185  1.000 28.78693  ? 93  ASN   A ND2 1 
ATOM   741  N N   . SER   A 1 94  ? -14.23893 18.41445 24.71131  1.000 29.81052  ? 94  SER   A N   1 
ATOM   742  C CA  . SER   A 1 94  ? -13.81067 17.02929 24.61103  1.000 26.37196  ? 94  SER   A CA  1 
ATOM   743  C C   . SER   A 1 94  ? -12.35716 16.88573 25.05041  1.000 26.76380  ? 94  SER   A C   1 
ATOM   744  O O   . SER   A 1 94  ? -11.57513 17.84007 25.02923  1.000 29.40222  ? 94  SER   A O   1 
ATOM   745  C CB  . SER   A 1 94  ? -13.97354 16.51629 23.18041  1.000 34.33542  ? 94  SER   A CB  1 
ATOM   746  O OG  . SER   A 1 94  ? -13.11701 17.21343 22.29221  1.000 34.10876  ? 94  SER   A OG  1 
ATOM   747  N N   . VAL   A 1 95  ? -11.99822 15.66303 25.44731  1.000 27.05199  ? 95  VAL   A N   1 
ATOM   748  C CA  . VAL   A 1 95  ? -10.63404 15.40137 25.89810  1.000 33.03212  ? 95  VAL   A CA  1 
ATOM   749  C C   . VAL   A 1 95  ? -9.64057  15.64339 24.76913  1.000 36.66394  ? 95  VAL   A C   1 
ATOM   750  O O   . VAL   A 1 95  ? -8.55600  16.19899 24.98616  1.000 33.51117  ? 95  VAL   A O   1 
ATOM   751  C CB  . VAL   A 1 95  ? -10.52250 13.97143 26.45886  1.000 39.40449  ? 95  VAL   A CB  1 
ATOM   752  C CG1 . VAL   A 1 95  ? -9.06988  13.61813 26.73235  1.000 30.48136  ? 95  VAL   A CG1 1 
ATOM   753  C CG2 . VAL   A 1 95  ? -11.35344 13.83684 27.72753  1.000 29.68915  ? 95  VAL   A CG2 1 
ATOM   754  N N   . VAL   A 1 96  ? -9.99728  15.24503 23.54469  1.000 28.89298  ? 96  VAL   A N   1 
ATOM   755  C CA  . VAL   A 1 96  ? -9.08427  15.41114 22.41611  1.000 28.42325  ? 96  VAL   A CA  1 
ATOM   756  C C   . VAL   A 1 96  ? -8.82861  16.88815 22.14599  1.000 36.23559  ? 96  VAL   A C   1 
ATOM   757  O O   . VAL   A 1 96  ? -7.68453  17.30360 21.92475  1.000 29.06773  ? 96  VAL   A O   1 
ATOM   758  C CB  . VAL   A 1 96  ? -9.63493  14.69451 21.16910  1.000 34.81572  ? 96  VAL   A CB  1 
ATOM   759  C CG1 . VAL   A 1 96  ? -8.70789  14.90357 19.98473  1.000 40.20930  ? 96  VAL   A CG1 1 
ATOM   760  C CG2 . VAL   A 1 96  ? -9.81773  13.21186 21.44867  1.000 36.01141  ? 96  VAL   A CG2 1 
ATOM   761  N N   . ALA   A 1 97  ? -9.88594  17.70539 22.16398  1.000 31.25484  ? 97  ALA   A N   1 
ATOM   762  C CA  . ALA   A 1 97  ? -9.71963  19.13224 21.90039  1.000 28.23510  ? 97  ALA   A CA  1 
ATOM   763  C C   . ALA   A 1 97  ? -8.87375  19.80223 22.97564  1.000 29.30824  ? 97  ALA   A C   1 
ATOM   764  O O   . ALA   A 1 97  ? -8.07507  20.69778 22.67559  1.000 28.48623  ? 97  ALA   A O   1 
ATOM   765  C CB  . ALA   A 1 97  ? -11.08238 19.81084 21.79257  1.000 30.03880  ? 97  ALA   A CB  1 
ATOM   766  N N   . ILE   A 1 98  ? -9.03852  19.38816 24.23350  1.000 27.67361  ? 98  ILE   A N   1 
ATOM   767  C CA  . ILE   A 1 98  ? -8.20248  19.92456 25.30293  1.000 21.19059  ? 98  ILE   A CA  1 
ATOM   768  C C   . ILE   A 1 98  ? -6.75376  19.50556 25.10131  1.000 24.72237  ? 98  ILE   A C   1 
ATOM   769  O O   . ILE   A 1 98  ? -5.83370  20.32398 25.21963  1.000 30.19237  ? 98  ILE   A O   1 
ATOM   770  C CB  . ILE   A 1 98  ? -8.73596  19.47407 26.67453  1.000 24.36852  ? 98  ILE   A CB  1 
ATOM   771  C CG1 . ILE   A 1 98  ? -10.16713 19.97232 26.88350  1.000 24.63859  ? 98  ILE   A CG1 1 
ATOM   772  C CG2 . ILE   A 1 98  ? -7.83197  19.97494 27.78525  1.000 30.53374  ? 98  ILE   A CG2 1 
ATOM   773  C CD1 . ILE   A 1 98  ? -10.83658 19.40208 28.11377  1.000 19.58052  ? 98  ILE   A CD1 1 
ATOM   774  N N   . THR   A 1 99  ? -6.53023  18.22484 24.79162  1.000 28.24049  ? 99  THR   A N   1 
ATOM   775  C CA  . THR   A 1 99  ? -5.17911  17.73955 24.53139  1.000 21.69081  ? 99  THR   A CA  1 
ATOM   776  C C   . THR   A 1 99  ? -4.54870  18.46662 23.34955  1.000 31.87912  ? 99  THR   A C   1 
ATOM   777  O O   . THR   A 1 99  ? -3.37320  18.84852 23.40110  1.000 31.20811  ? 99  THR   A O   1 
ATOM   778  C CB  . THR   A 1 99  ? -5.21015  16.23289 24.27640  1.000 35.91360  ? 99  THR   A CB  1 
ATOM   779  O OG1 . THR   A 1 99  ? -5.71491  15.56044 25.43694  1.000 35.73182  ? 99  THR   A OG1 1 
ATOM   780  C CG2 . THR   A 1 99  ? -3.81837  15.71271 23.95450  1.000 27.87931  ? 99  THR   A CG2 1 
ATOM   781  N N   . GLY   A 1 100 ? -5.31772  18.66928 22.27673  1.000 22.14644  ? 100 GLY   A N   1 
ATOM   782  C CA  . GLY   A 1 100 ? -4.79188  19.38182 21.12395  1.000 21.90811  ? 100 GLY   A CA  1 
ATOM   783  C C   . GLY   A 1 100 ? -4.37756  20.80286 21.45237  1.000 31.17090  ? 100 GLY   A C   1 
ATOM   784  O O   . GLY   A 1 100 ? -3.33812  21.27854 20.98958  1.000 26.43534  ? 100 GLY   A O   1 
ATOM   785  N N   . LYS   A 1 101 ? -5.18287  21.50113 22.25759  1.000 20.59534  ? 101 LYS   A N   1 
ATOM   786  C CA  . LYS   A 1 101 ? -4.81093  22.85161 22.66497  1.000 23.08622  ? 101 LYS   A CA  1 
ATOM   787  C C   . LYS   A 1 101 ? -3.58091  22.84996 23.56444  1.000 27.95207  ? 101 LYS   A C   1 
ATOM   788  O O   . LYS   A 1 101 ? -2.77807  23.78891 23.51249  1.000 28.15762  ? 101 LYS   A O   1 
ATOM   789  C CB  . LYS   A 1 101 ? -5.98224  23.53549 23.36950  1.000 24.68939  ? 101 LYS   A CB  1 
ATOM   790  C CG  . LYS   A 1 101 ? -7.17680  23.81568 22.47319  1.000 29.02036  ? 101 LYS   A CG  1 
ATOM   791  C CD  . LYS   A 1 101 ? -6.87558  24.91658 21.46722  1.000 38.30578  ? 101 LYS   A CD  1 
ATOM   792  C CE  . LYS   A 1 101 ? -8.02445  25.09294 20.48522  1.000 53.39847  ? 101 LYS   A CE  1 
ATOM   793  N NZ  . LYS   A 1 101 ? -9.32485  25.32419 21.17414  1.000 85.30860  ? 101 LYS   A NZ  1 
ATOM   794  N N   . ASN   A 1 102 ? -3.40911  21.81292 24.38924  1.000 26.36327  ? 102 ASN   A N   1 
ATOM   795  C CA  . ASN   A 1 102 ? -2.24771  21.76699 25.27165  1.000 22.85589  ? 102 ASN   A CA  1 
ATOM   796  C C   . ASN   A 1 102 ? -0.96051  21.56064 24.48481  1.000 25.08878  ? 102 ASN   A C   1 
ATOM   797  O O   . ASN   A 1 102 ? 0.06393   22.18285 24.78841  1.000 24.86491  ? 102 ASN   A O   1 
ATOM   798  C CB  . ASN   A 1 102 ? -2.41152  20.66298 26.31484  1.000 22.95646  ? 102 ASN   A CB  1 
ATOM   799  C CG  . ASN   A 1 102 ? -3.45999  20.99144 27.35191  1.000 34.59631  ? 102 ASN   A CG  1 
ATOM   800  O OD1 . ASN   A 1 102 ? -3.88193  22.14191 27.48619  1.000 33.17500  ? 102 ASN   A OD1 1 
ATOM   801  N ND2 . ASN   A 1 102 ? -3.87941  19.98062 28.10544  1.000 29.14809  ? 102 ASN   A ND2 1 
ATOM   802  N N   . ILE   A 1 103 ? -0.98732  20.68237 23.47964  1.000 27.68116  ? 103 ILE   A N   1 
ATOM   803  C CA  . ILE   A 1 103 ? 0.20493   20.46176 22.66997  1.000 24.07138  ? 103 ILE   A CA  1 
ATOM   804  C C   . ILE   A 1 103 ? 0.43652   21.63840 21.73465  1.000 25.94475  ? 103 ILE   A C   1 
ATOM   805  O O   . ILE   A 1 103 ? 1.58054   21.94192 21.37626  1.000 24.51111  ? 103 ILE   A O   1 
ATOM   806  C CB  . ILE   A 1 103 ? 0.09015   19.13710 21.89525  1.000 21.39236  ? 103 ILE   A CB  1 
ATOM   807  C CG1 . ILE   A 1 103 ? -0.25638  17.99907 22.85145  1.000 36.02198  ? 103 ILE   A CG1 1 
ATOM   808  C CG2 . ILE   A 1 103 ? 1.39228   18.81865 21.18458  1.000 20.01983  ? 103 ILE   A CG2 1 
ATOM   809  C CD1 . ILE   A 1 103 ? -0.27322  16.64375 22.18994  1.000 56.28418  ? 103 ILE   A CD1 1 
ATOM   810  N N   . GLU   A 1 104 ? -0.63331  22.31963 21.32485  1.000 20.20162  ? 104 GLU   A N   1 
ATOM   811  C CA  . GLU   A 1 104 ? -0.47348  23.52022 20.51346  1.000 25.18655  ? 104 GLU   A CA  1 
ATOM   812  C C   . GLU   A 1 104 ? 0.32150   24.57839 21.26789  1.000 31.15050  ? 104 GLU   A C   1 
ATOM   813  O O   . GLU   A 1 104 ? 1.26825   25.16309 20.72880  1.000 29.45162  ? 104 GLU   A O   1 
ATOM   814  C CB  . GLU   A 1 104 ? -1.84346  24.05652 20.10466  1.000 19.97387  ? 104 GLU   A CB  1 
ATOM   815  C CG  . GLU   A 1 104 ? -1.79312  25.17969 19.09660  1.000 30.53771  ? 104 GLU   A CG  1 
ATOM   816  C CD  . GLU   A 1 104 ? -3.14548  25.82058 18.89616  1.000 38.54267  ? 104 GLU   A CD  1 
ATOM   817  O OE1 . GLU   A 1 104 ? -3.89312  25.94627 19.88905  1.000 43.58304  ? 104 GLU   A OE1 1 
ATOM   818  O OE2 . GLU   A 1 104 ? -3.46441  26.19016 17.74732  1.000 50.65008  ? 104 GLU   A OE2 1 
ATOM   819  N N   . THR   A 1 105 ? -0.04453  24.82796 22.52874  1.000 26.45126  ? 105 THR   A N   1 
ATOM   820  C CA  . THR   A 1 105 ? 0.71142   25.77325 23.34449  1.000 29.61767  ? 105 THR   A CA  1 
ATOM   821  C C   . THR   A 1 105 ? 2.15242   25.31511 23.51931  1.000 27.31314  ? 105 THR   A C   1 
ATOM   822  O O   . THR   A 1 105 ? 3.08696   26.11807 23.41050  1.000 35.61160  ? 105 THR   A O   1 
ATOM   823  C CB  . THR   A 1 105 ? 0.04162   25.94785 24.70731  1.000 29.76846  ? 105 THR   A CB  1 
ATOM   824  O OG1 . THR   A 1 105 ? -1.31971  26.35542 24.52431  1.000 41.09899  ? 105 THR   A OG1 1 
ATOM   825  C CG2 . THR   A 1 105 ? 0.77416   27.00075 25.53053  1.000 27.07902  ? 105 THR   A CG2 1 
ATOM   826  N N   . TYR   A 1 106 ? 2.34897   24.02401 23.79134  1.000 29.04784  ? 106 TYR   A N   1 
ATOM   827  C CA  . TYR   A 1 106 ? 3.69693   23.48780 23.93849  1.000 22.59443  ? 106 TYR   A CA  1 
ATOM   828  C C   . TYR   A 1 106 ? 4.51336   23.68978 22.66816  1.000 22.93364  ? 106 TYR   A C   1 
ATOM   829  O O   . TYR   A 1 106 ? 5.68263   24.08980 22.72926  1.000 24.88574  ? 106 TYR   A O   1 
ATOM   830  C CB  . TYR   A 1 106 ? 3.61714   22.00729 24.30555  1.000 22.24777  ? 106 TYR   A CB  1 
ATOM   831  C CG  . TYR   A 1 106 ? 4.94714   21.30818 24.44068  1.000 24.58491  ? 106 TYR   A CG  1 
ATOM   832  C CD1 . TYR   A 1 106 ? 5.73582   21.48397 25.56929  1.000 27.46774  ? 106 TYR   A CD1 1 
ATOM   833  C CD2 . TYR   A 1 106 ? 5.40356   20.45085 23.44993  1.000 23.46469  ? 106 TYR   A CD2 1 
ATOM   834  C CE1 . TYR   A 1 106 ? 6.94754   20.83371 25.70138  1.000 24.96199  ? 106 TYR   A CE1 1 
ATOM   835  C CE2 . TYR   A 1 106 ? 6.61360   19.79571 23.57378  1.000 31.07223  ? 106 TYR   A CE2 1 
ATOM   836  C CZ  . TYR   A 1 106 ? 7.37998   19.99108 24.70103  1.000 29.77786  ? 106 TYR   A CZ  1 
ATOM   837  O OH  . TYR   A 1 106 ? 8.58404   19.34013 24.82694  1.000 33.20071  ? 106 TYR   A OH  1 
ATOM   838  N N   . PHE   A 1 107 ? 3.90817   23.43146 21.50525  1.000 26.10876  ? 107 PHE   A N   1 
ATOM   839  C CA  . PHE   A 1 107 ? 4.62467   23.59765 20.24554  1.000 23.78539  ? 107 PHE   A CA  1 
ATOM   840  C C   . PHE   A 1 107 ? 5.00019   25.05524 20.01211  1.000 28.76812  ? 107 PHE   A C   1 
ATOM   841  O O   . PHE   A 1 107 ? 6.13641   25.35434 19.62740  1.000 29.53987  ? 107 PHE   A O   1 
ATOM   842  C CB  . PHE   A 1 107 ? 3.77972   23.06312 19.08832  1.000 20.16056  ? 107 PHE   A CB  1 
ATOM   843  C CG  . PHE   A 1 107 ? 4.34898   23.36186 17.72840  1.000 28.50828  ? 107 PHE   A CG  1 
ATOM   844  C CD1 . PHE   A 1 107 ? 5.49146   22.71867 17.28213  1.000 31.28487  ? 107 PHE   A CD1 1 
ATOM   845  C CD2 . PHE   A 1 107 ? 3.73361   24.27824 16.89184  1.000 22.96361  ? 107 PHE   A CD2 1 
ATOM   846  C CE1 . PHE   A 1 107 ? 6.01484   22.99005 16.03060  1.000 30.69494  ? 107 PHE   A CE1 1 
ATOM   847  C CE2 . PHE   A 1 107 ? 4.25061   24.55368 15.63862  1.000 27.89885  ? 107 PHE   A CE2 1 
ATOM   848  C CZ  . PHE   A 1 107 ? 5.39286   23.90888 15.20667  1.000 23.51451  ? 107 PHE   A CZ  1 
ATOM   849  N N   . ASN   A 1 108 ? 4.06367   25.97651 20.25098  1.000 25.27366  ? 108 ASN   A N   1 
ATOM   850  C CA  . ASN   A 1 108 ? 4.34476   27.39187 20.03037  1.000 27.37366  ? 108 ASN   A CA  1 
ATOM   851  C C   . ASN   A 1 108 ? 5.38865   27.90999 21.00928  1.000 32.77127  ? 108 ASN   A C   1 
ATOM   852  O O   . ASN   A 1 108 ? 6.20746   28.76751 20.65605  1.000 36.64614  ? 108 ASN   A O   1 
ATOM   853  C CB  . ASN   A 1 108 ? 3.05641   28.20430 20.13756  1.000 33.55733  ? 108 ASN   A CB  1 
ATOM   854  C CG  . ASN   A 1 108 ? 2.10689   27.93149 18.99374  1.000 32.88207  ? 108 ASN   A CG  1 
ATOM   855  O OD1 . ASN   A 1 108 ? 2.53418   27.65265 17.87371  1.000 33.18789  ? 108 ASN   A OD1 1 
ATOM   856  N ND2 . ASN   A 1 108 ? 0.81057   28.00720 19.26730  1.000 28.89086  ? 108 ASN   A ND2 1 
ATOM   857  N N   . ASN   A 1 109 ? 5.37503   27.40721 22.24533  1.000 25.49810  ? 109 ASN   A N   1 
ATOM   858  C CA  . ASN   A 1 109 ? 6.39767   27.81200 23.20163  1.000 26.89238  ? 109 ASN   A CA  1 
ATOM   859  C C   . ASN   A 1 109 ? 7.74628   27.18675 22.87303  1.000 31.78715  ? 109 ASN   A C   1 
ATOM   860  O O   . ASN   A 1 109 ? 8.78942   27.79207 23.14197  1.000 30.84764  ? 109 ASN   A O   1 
ATOM   861  C CB  . ASN   A 1 109 ? 5.96346   27.45295 24.62022  1.000 24.61323  ? 109 ASN   A CB  1 
ATOM   862  C CG  . ASN   A 1 109 ? 4.85057   28.34476 25.12409  1.000 34.24787  ? 109 ASN   A CG  1 
ATOM   863  O OD1 . ASN   A 1 109 ? 4.70660   29.48299 24.67724  1.000 34.50274  ? 109 ASN   A OD1 1 
ATOM   864  N ND2 . ASN   A 1 109 ? 4.05507   27.83453 26.05738  1.000 29.15498  ? 109 ASN   A ND2 1 
ATOM   865  N N   . GLN   A 1 110 ? 7.74942   25.98746 22.28679  1.000 33.67808  ? 110 GLN   A N   1 
ATOM   866  C CA  . GLN   A 1 110 ? 9.00708   25.39500 21.84789  1.000 27.26371  ? 110 GLN   A CA  1 
ATOM   867  C C   . GLN   A 1 110 ? 9.60205   26.15106 20.66674  1.000 31.56375  ? 110 GLN   A C   1 
ATOM   868  O O   . GLN   A 1 110 ? 10.82874  26.19904 20.52149  1.000 35.46568  ? 110 GLN   A O   1 
ATOM   869  C CB  . GLN   A 1 110 ? 8.80618   23.92456 21.48780  1.000 29.13055  ? 110 GLN   A CB  1 
ATOM   870  C CG  . GLN   A 1 110 ? 8.73779   22.98549 22.67714  1.000 23.36362  ? 110 GLN   A CG  1 
ATOM   871  C CD  . GLN   A 1 110 ? 10.09818  22.70040 23.29214  1.000 19.67192  ? 110 GLN   A CD  1 
ATOM   872  O OE1 . GLN   A 1 110 ? 11.08018  23.39339 23.02221  1.000 40.13177  ? 110 GLN   A OE1 1 
ATOM   873  N NE2 . GLN   A 1 110 ? 10.16082  21.66739 24.12306  1.000 44.75898  ? 110 GLN   A NE2 1 
ATOM   874  N N   . LEU   A 1 111 ? 8.75888   26.74232 19.81456  1.000 34.54873  ? 111 LEU   A N   1 
ATOM   875  C CA  . LEU   A 1 111 ? 9.27427   27.58286 18.73729  1.000 36.00707  ? 111 LEU   A CA  1 
ATOM   876  C C   . LEU   A 1 111 ? 9.99586   28.80527 19.28564  1.000 40.69952  ? 111 LEU   A C   1 
ATOM   877  O O   . LEU   A 1 111 ? 10.95965  29.28360 18.67778  1.000 41.98712  ? 111 LEU   A O   1 
ATOM   878  C CB  . LEU   A 1 111 ? 8.13802   28.01760 17.80917  1.000 29.50918  ? 111 LEU   A CB  1 
ATOM   879  C CG  . LEU   A 1 111 ? 7.40884   26.93266 17.01211  1.000 22.97228  ? 111 LEU   A CG  1 
ATOM   880  C CD1 . LEU   A 1 111 ? 6.32540   27.53270 16.12037  1.000 21.30596  ? 111 LEU   A CD1 1 
ATOM   881  C CD2 . LEU   A 1 111 ? 8.39637   26.12808 16.18609  1.000 28.57851  ? 111 LEU   A CD2 1 
ATOM   882  N N   . ILE   A 1 112 ? 9.54570   29.31892 20.43088  1.000 35.79631  ? 112 ILE   A N   1 
ATOM   883  C CA  . ILE   A 1 112 ? 10.19791  30.46965 21.04750  1.000 34.57638  ? 112 ILE   A CA  1 
ATOM   884  C C   . ILE   A 1 112 ? 11.51404  30.05786 21.69372  1.000 35.38119  ? 112 ILE   A C   1 
ATOM   885  O O   . ILE   A 1 112 ? 12.54079  30.72912 21.53649  1.000 40.23355  ? 112 ILE   A O   1 
ATOM   886  C CB  . ILE   A 1 112 ? 9.25580   31.12698 22.06842  1.000 28.46456  ? 112 ILE   A CB  1 
ATOM   887  C CG1 . ILE   A 1 112 ? 7.95933   31.56555 21.38505  1.000 26.92491  ? 112 ILE   A CG1 1 
ATOM   888  C CG2 . ILE   A 1 112 ? 9.95254   32.29347 22.75500  1.000 39.04679  ? 112 ILE   A CG2 1 
ATOM   889  C CD1 . ILE   A 1 112 ? 6.91273   32.08540 22.34711  1.000 33.97476  ? 112 ILE   A CD1 1 
ATOM   890  N N   . VAL   A 1 113 ? 11.49967  28.95254 22.43879  1.000 35.28382  ? 113 VAL   A N   1 
ATOM   891  C CA  . VAL   A 1 113 ? 12.69191  28.52341 23.16110  1.000 33.83325  ? 113 VAL   A CA  1 
ATOM   892  C C   . VAL   A 1 113 ? 13.78544  28.09340 22.19109  1.000 35.99458  ? 113 VAL   A C   1 
ATOM   893  O O   . VAL   A 1 113 ? 14.96755  28.39983 22.39036  1.000 43.08786  ? 113 VAL   A O   1 
ATOM   894  C CB  . VAL   A 1 113 ? 12.33493  27.39918 24.14941  1.000 32.63428  ? 113 VAL   A CB  1 
ATOM   895  C CG1 . VAL   A 1 113 ? 13.58574  26.87020 24.82141  1.000 35.03585  ? 113 VAL   A CG1 1 
ATOM   896  C CG2 . VAL   A 1 113 ? 11.34200  27.90374 25.18355  1.000 23.32859  ? 113 VAL   A CG2 1 
ATOM   897  N N   . MET   A 1 114 ? 13.41427  27.38738 21.12389  1.000 36.88190  ? 114 MET   A N   1 
ATOM   898  C CA  . MET   A 1 114 ? 14.40239  26.89913 20.17231  1.000 41.53575  ? 114 MET   A CA  1 
ATOM   899  C C   . MET   A 1 114 ? 14.84460  27.95943 19.17460  1.000 40.64206  ? 114 MET   A C   1 
ATOM   900  O O   . MET   A 1 114 ? 15.77894  27.70718 18.40640  1.000 48.51499  ? 114 MET   A O   1 
ATOM   901  C CB  . MET   A 1 114 ? 13.85626  25.68744 19.41336  1.000 40.82333  ? 114 MET   A CB  1 
ATOM   902  C CG  . MET   A 1 114 ? 13.56204  24.47965 20.28507  1.000 33.37276  ? 114 MET   A CG  1 
ATOM   903  S SD  . MET   A 1 114 ? 13.18588  23.01935 19.29581  1.000 52.39980  ? 114 MET   A SD  1 
ATOM   904  C CE  . MET   A 1 114 ? 12.72919  21.84295 20.56831  1.000 44.17613  ? 114 MET   A CE  1 
ATOM   905  N N   . GLY   A 1 115 ? 14.21140  29.13014 19.16786  1.000 42.44952  ? 115 GLY   A N   1 
ATOM   906  C CA  . GLY   A 1 115 ? 14.54223  30.13208 18.17656  1.000 32.76328  ? 115 GLY   A CA  1 
ATOM   907  C C   . GLY   A 1 115 ? 14.16237  29.75615 16.76534  1.000 38.56188  ? 115 GLY   A C   1 
ATOM   908  O O   . GLY   A 1 115 ? 14.76777  30.25861 15.81538  1.000 46.64946  ? 115 GLY   A O   1 
ATOM   909  N N   . TYR   A 1 116 ? 13.17462  28.87269 16.60000  1.000 40.69090  ? 116 TYR   A N   1 
ATOM   910  C CA  . TYR   A 1 116 ? 12.75323  28.47139 15.26244  1.000 35.48029  ? 116 TYR   A CA  1 
ATOM   911  C C   . TYR   A 1 116 ? 12.10150  29.62455 14.51242  1.000 44.11773  ? 116 TYR   A C   1 
ATOM   912  O O   . TYR   A 1 116 ? 12.19516  29.69259 13.28162  1.000 44.71884  ? 116 TYR   A O   1 
ATOM   913  C CB  . TYR   A 1 116 ? 11.79261  27.28499 15.35162  1.000 30.28472  ? 116 TYR   A CB  1 
ATOM   914  C CG  . TYR   A 1 116 ? 11.51101  26.59907 14.03206  1.000 30.60398  ? 116 TYR   A CG  1 
ATOM   915  C CD1 . TYR   A 1 116 ? 10.50188  27.05130 13.18865  1.000 35.15086  ? 116 TYR   A CD1 1 
ATOM   916  C CD2 . TYR   A 1 116 ? 12.24614  25.48918 13.63576  1.000 38.86371  ? 116 TYR   A CD2 1 
ATOM   917  C CE1 . TYR   A 1 116 ? 10.24183  26.42374 11.98405  1.000 35.10774  ? 116 TYR   A CE1 1 
ATOM   918  C CE2 . TYR   A 1 116 ? 11.99181  24.85377 12.43405  1.000 41.31725  ? 116 TYR   A CE2 1 
ATOM   919  C CZ  . TYR   A 1 116 ? 10.98907  25.32479 11.61362  1.000 39.95079  ? 116 TYR   A CZ  1 
ATOM   920  O OH  . TYR   A 1 116 ? 10.73412  24.69233 10.41941  1.000 38.89974  ? 116 TYR   A OH  1 
ATOM   921  N N   . ASN   A 1 117 ? 11.44368  30.53772 15.23116  1.000 40.62324  ? 117 ASN   A N   1 
ATOM   922  C CA  . ASN   A 1 117 ? 10.77419  31.65373 14.57227  1.000 45.61937  ? 117 ASN   A CA  1 
ATOM   923  C C   . ASN   A 1 117 ? 11.76441  32.58191 13.88235  1.000 50.37253  ? 117 ASN   A C   1 
ATOM   924  O O   . ASN   A 1 117 ? 11.43081  33.18814 12.85762  1.000 55.48112  ? 117 ASN   A O   1 
ATOM   925  C CB  . ASN   A 1 117 ? 9.93336   32.42890 15.58359  1.000 50.05699  ? 117 ASN   A CB  1 
ATOM   926  C CG  . ASN   A 1 117 ? 8.81217   31.59629 16.15838  1.000 52.62205  ? 117 ASN   A CG  1 
ATOM   927  O OD1 . ASN   A 1 117 ? 8.27717   30.71274 15.48825  1.000 42.35269  ? 117 ASN   A OD1 1 
ATOM   928  N ND2 . ASN   A 1 117 ? 8.45089   31.86815 17.40707  1.000 50.29778  ? 117 ASN   A ND2 1 
ATOM   929  N N   . ASN   A 1 118 ? 12.97943  32.70601 14.41997  1.000 49.82448  ? 118 ASN   A N   1 
ATOM   930  C CA  . ASN   A 1 118 ? 13.98374  33.53609 13.76592  1.000 49.69156  ? 118 ASN   A CA  1 
ATOM   931  C C   . ASN   A 1 118 ? 14.38838  32.96120 12.41458  1.000 48.92734  ? 118 ASN   A C   1 
ATOM   932  O O   . ASN   A 1 118 ? 14.81722  33.70935 11.52881  1.000 52.43867  ? 118 ASN   A O   1 
ATOM   933  C CB  . ASN   A 1 118 ? 15.20332  33.69763 14.67212  1.000 45.52683  ? 118 ASN   A CB  1 
ATOM   934  C CG  . ASN   A 1 118 ? 14.84681  34.27910 16.02597  1.000 59.58809  ? 118 ASN   A CG  1 
ATOM   935  O OD1 . ASN   A 1 118 ? 15.17008  33.70442 17.06578  1.000 71.87237  ? 118 ASN   A OD1 1 
ATOM   936  N ND2 . ASN   A 1 118 ? 14.17021  35.42263 16.01979  1.000 77.38519  ? 118 ASN   A ND2 1 
ATOM   937  N N   . PHE   A 1 119 ? 14.25654  31.64359 12.23497  1.000 47.47907  ? 119 PHE   A N   1 
ATOM   938  C CA  . PHE   A 1 119 ? 14.50014  31.05245 10.92358  1.000 39.96864  ? 119 PHE   A CA  1 
ATOM   939  C C   . PHE   A 1 119 ? 13.40040  31.41417 9.93596   1.000 40.69204  ? 119 PHE   A C   1 
ATOM   940  O O   . PHE   A 1 119 ? 13.67133  31.58082 8.74142   1.000 53.65486  ? 119 PHE   A O   1 
ATOM   941  C CB  . PHE   A 1 119 ? 14.62659  29.53408 11.04155  1.000 47.38827  ? 119 PHE   A CB  1 
ATOM   942  C CG  . PHE   A 1 119 ? 15.95451  29.07839 11.56532  1.000 39.52665  ? 119 PHE   A CG  1 
ATOM   943  C CD1 . PHE   A 1 119 ? 16.16567  28.93770 12.92582  1.000 41.18952  ? 119 PHE   A CD1 1 
ATOM   944  C CD2 . PHE   A 1 119 ? 16.99459  28.79386 10.69574  1.000 48.50959  ? 119 PHE   A CD2 1 
ATOM   945  C CE1 . PHE   A 1 119 ? 17.39009  28.52009 13.41103  1.000 39.75199  ? 119 PHE   A CE1 1 
ATOM   946  C CE2 . PHE   A 1 119 ? 18.22006  28.37552 11.17460  1.000 48.48860  ? 119 PHE   A CE2 1 
ATOM   947  C CZ  . PHE   A 1 119 ? 18.41807  28.23890 12.53455  1.000 50.56769  ? 119 PHE   A CZ  1 
ATOM   948  N N   . ILE   A 1 120 ? 12.16060  31.53943 10.41071  1.000 37.47999  ? 120 ILE   A N   1 
ATOM   949  C CA  . ILE   A 1 120 ? 11.06753  31.92873 9.52785   1.000 48.46525  ? 120 ILE   A CA  1 
ATOM   950  C C   . ILE   A 1 120 ? 11.21112  33.38855 9.11434   1.000 56.80208  ? 120 ILE   A C   1 
ATOM   951  O O   . ILE   A 1 120 ? 10.92978  33.75311 7.96618   1.000 55.28959  ? 120 ILE   A O   1 
ATOM   952  C CB  . ILE   A 1 120 ? 9.71515   31.65497 10.21033  1.000 41.55219  ? 120 ILE   A CB  1 
ATOM   953  C CG1 . ILE   A 1 120 ? 9.65221   30.20188 10.68495  1.000 37.63365  ? 120 ILE   A CG1 1 
ATOM   954  C CG2 . ILE   A 1 120 ? 8.56501   31.94862 9.26125   1.000 51.83141  ? 120 ILE   A CG2 1 
ATOM   955  C CD1 . ILE   A 1 120 ? 8.38842   29.85417 11.43549  1.000 46.66728  ? 120 ILE   A CD1 1 
ATOM   956  N N   . LEU   A 1 121 ? 11.66437  34.24421 10.03472  1.000 57.11677  ? 121 LEU   A N   1 
ATOM   957  C CA  . LEU   A 1 121 ? 11.82065  35.66003 9.71407   1.000 50.69635  ? 121 LEU   A CA  1 
ATOM   958  C C   . LEU   A 1 121 ? 12.90880  35.87523 8.67033   1.000 52.08762  ? 121 LEU   A C   1 
ATOM   959  O O   . LEU   A 1 121 ? 12.72672  36.65431 7.72673   1.000 58.11087  ? 121 LEU   A O   1 
ATOM   960  C CB  . LEU   A 1 121 ? 12.12857  36.45479 10.98204  1.000 51.80684  ? 121 LEU   A CB  1 
ATOM   961  C CG  . LEU   A 1 121 ? 11.08695  36.35843 12.09888  1.000 53.64020  ? 121 LEU   A CG  1 
ATOM   962  C CD1 . LEU   A 1 121 ? 11.52463  37.16648 13.31050  1.000 58.40646  ? 121 LEU   A CD1 1 
ATOM   963  C CD2 . LEU   A 1 121 ? 9.71743   36.81307 11.60861  1.000 57.20152  ? 121 LEU   A CD2 1 
ATOM   964  N N   . LYS   A 1 122 ? 14.04847  35.19671 8.82284   1.000 49.98306  ? 122 LYS   A N   1 
ATOM   965  C CA  . LYS   A 1 122 ? 15.10246  35.30279 7.82138   1.000 52.24836  ? 122 LYS   A CA  1 
ATOM   966  C C   . LYS   A 1 122 ? 14.66632  34.70241 6.49076   1.000 59.41989  ? 122 LYS   A C   1 
ATOM   967  O O   . LYS   A 1 122 ? 15.13782  35.13472 5.43270   1.000 72.95118  ? 122 LYS   A O   1 
ATOM   968  C CB  . LYS   A 1 122 ? 16.37572  34.62952 8.32995   1.000 43.92128  ? 122 LYS   A CB  1 
ATOM   969  C CG  . LYS   A 1 122 ? 17.60926  34.95000 7.50913   1.000 63.86259  ? 122 LYS   A CG  1 
ATOM   970  C CD  . LYS   A 1 122 ? 18.87557  34.70847 8.30988   1.000 95.48895  ? 122 LYS   A CD  1 
ATOM   971  C CE  . LYS   A 1 122 ? 18.93449  35.61034 9.53359   1.000 77.06788  ? 122 LYS   A CE  1 
ATOM   972  N NZ  . LYS   A 1 122 ? 18.91469  37.05422 9.16728   1.000 85.49424  ? 122 LYS   A NZ  1 
ATOM   973  N N   . GLU   A 1 123 ? 13.77044  33.71131 6.52477   1.000 59.38925  ? 123 GLU   A N   1 
ATOM   974  C CA  . GLU   A 1 123 ? 13.17256  33.20428 5.29350   1.000 58.32039  ? 123 GLU   A CA  1 
ATOM   975  C C   . GLU   A 1 123 ? 12.40802  34.30218 4.56415   1.000 61.07481  ? 123 GLU   A C   1 
ATOM   976  O O   . GLU   A 1 123 ? 12.50329  34.42837 3.33707   1.000 54.39963  ? 123 GLU   A O   1 
ATOM   977  C CB  . GLU   A 1 123 ? 12.24985  32.02440 5.60871   1.000 52.10220  ? 123 GLU   A CB  1 
ATOM   978  C CG  . GLU   A 1 123 ? 11.03733  31.91341 4.68976   1.000 67.84960  ? 123 GLU   A CG  1 
ATOM   979  C CD  . GLU   A 1 123 ? 9.95355   30.99596 5.23600   1.000 61.64631  ? 123 GLU   A CD  1 
ATOM   980  O OE1 . GLU   A 1 123 ? 10.19186  30.32038 6.25917   1.000 58.14845  ? 123 GLU   A OE1 1 
ATOM   981  O OE2 . GLU   A 1 123 ? 8.85678   30.95456 4.63945   1.000 73.02673  ? 123 GLU   A OE2 1 
ATOM   982  N N   . LYS   A 1 124 ? 11.65036  35.11337 5.30634   1.000 58.16285  ? 124 LYS   A N   1 
ATOM   983  C CA  . LYS   A 1 124 ? 10.87712  36.18169 4.68249   1.000 57.27279  ? 124 LYS   A CA  1 
ATOM   984  C C   . LYS   A 1 124 ? 11.78477  37.27872 4.14095   1.000 67.73404  ? 124 LYS   A C   1 
ATOM   985  O O   . LYS   A 1 124 ? 11.53480  37.81959 3.05737   1.000 79.26911  ? 124 LYS   A O   1 
ATOM   986  C CB  . LYS   A 1 124 ? 9.87607   36.75546 5.68540   1.000 45.71730  ? 124 LYS   A CB  1 
ATOM   987  N N   . LYS   A 1 125 ? 12.84362  37.61939 4.87958   1.000 65.92038  ? 125 LYS   A N   1 
ATOM   988  C CA  . LYS   A 1 125 ? 13.76295  38.65591 4.42082   1.000 56.80839  ? 125 LYS   A CA  1 
ATOM   989  C C   . LYS   A 1 125 ? 14.52415  38.21043 3.17825   1.000 60.40289  ? 125 LYS   A C   1 
ATOM   990  O O   . LYS   A 1 125 ? 14.75542  39.01188 2.26520   1.000 90.35443  ? 125 LYS   A O   1 
ATOM   991  C CB  . LYS   A 1 125 ? 14.73350  39.02875 5.54125   1.000 49.63193  ? 125 LYS   A CB  1 
ATOM   992  N N   . ILE   A 1 126 ? 14.91983  36.93609 3.12495   1.000 59.66895  ? 126 ILE   A N   1 
ATOM   993  C CA  . ILE   A 1 126 ? 15.64281  36.42743 1.96118   1.000 68.60230  ? 126 ILE   A CA  1 
ATOM   994  C C   . ILE   A 1 126 ? 14.75366  36.46648 0.72336   1.000 77.07524  ? 126 ILE   A C   1 
ATOM   995  O O   . ILE   A 1 126 ? 15.20814  36.81022 -0.37566  1.000 73.61333  ? 126 ILE   A O   1 
ATOM   996  C CB  . ILE   A 1 126 ? 16.18090  35.00962 2.24384   1.000 68.78557  ? 126 ILE   A CB  1 
ATOM   997  C CG1 . ILE   A 1 126 ? 17.64036  35.06536 2.70738   1.000 76.03248  ? 126 ILE   A CG1 1 
ATOM   998  C CG2 . ILE   A 1 126 ? 16.05980  34.11635 1.01438   1.000 69.76186  ? 126 ILE   A CG2 1 
ATOM   999  C CD1 . ILE   A 1 126 ? 17.87889  35.91365 3.93765   1.000 74.06459  ? 126 ILE   A CD1 1 
ATOM   1000 N N   . ASN   A 1 127 ? 13.46906  36.13349 0.88319   1.000 77.95171  ? 127 ASN   A N   1 
ATOM   1001 C CA  . ASN   A 1 127 ? 12.53995  36.21929 -0.23932  1.000 74.09142  ? 127 ASN   A CA  1 
ATOM   1002 C C   . ASN   A 1 127 ? 12.37270  37.65640 -0.71816  1.000 81.78030  ? 127 ASN   A C   1 
ATOM   1003 O O   . ASN   A 1 127 ? 12.17482  37.89316 -1.91572  1.000 76.36697  ? 127 ASN   A O   1 
ATOM   1004 C CB  . ASN   A 1 127 ? 11.18713  35.62054 0.15183   1.000 76.89429  ? 127 ASN   A CB  1 
ATOM   1005 C CG  . ASN   A 1 127 ? 11.23698  34.10722 0.29814   1.000 86.22941  ? 127 ASN   A CG  1 
ATOM   1006 O OD1 . ASN   A 1 127 ? 12.29051  33.48946 0.13931   1.000 87.04180  ? 127 ASN   A OD1 1 
ATOM   1007 N ND2 . ASN   A 1 127 ? 10.09414  33.50456 0.60759   1.000 72.49203  ? 127 ASN   A ND2 1 
ATOM   1008 N N   . ASP   A 1 128 ? 12.45811  38.62567 0.19501   1.000 93.65666  ? 128 ASP   A N   1 
ATOM   1009 C CA  . ASP   A 1 128 ? 12.37141  40.02736 -0.19971  1.000 96.92737  ? 128 ASP   A CA  1 
ATOM   1010 C C   . ASP   A 1 128 ? 13.62599  40.46395 -0.94562  1.000 81.55437  ? 128 ASP   A C   1 
ATOM   1011 O O   . ASP   A 1 128 ? 13.54207  41.06494 -2.02396  1.000 89.64845  ? 128 ASP   A O   1 
ATOM   1012 C CB  . ASP   A 1 128 ? 12.13578  40.90274 1.03180   1.000 80.74555  ? 128 ASP   A CB  1 
ATOM   1013 C CG  . ASP   A 1 128 ? 10.83963  40.56420 1.74640   1.000 106.38770 ? 128 ASP   A CG  1 
ATOM   1014 O OD1 . ASP   A 1 128 ? 10.15476  39.61197 1.31603   1.000 111.94864 ? 128 ASP   A OD1 1 
ATOM   1015 O OD2 . ASP   A 1 128 ? 10.50288  41.25052 2.73564   1.000 108.01179 ? 128 ASP   A OD2 1 
ATOM   1016 N N   A MET   A 1 129 ? 14.80122  40.17223 -0.39101  0.270 75.91695  ? 129 MET   A N   1 
ATOM   1017 N N   B MET   A 1 129 ? 14.80196  40.15983 -0.38586  0.730 75.31225  ? 129 MET   A N   1 
ATOM   1018 C CA  A MET   A 1 129 ? 16.04027  40.55060 -1.06829  0.270 85.05079  ? 129 MET   A CA  1 
ATOM   1019 C CA  B MET   A 1 129 ? 16.09443  40.45241 -0.98701  0.730 85.26390  ? 129 MET   A CA  1 
ATOM   1020 C C   A MET   A 1 129 ? 16.33431  39.68362 -2.28506  0.270 87.43652  ? 129 MET   A C   1 
ATOM   1021 C C   B MET   A 1 129 ? 16.37887  39.58912 -2.21185  0.730 87.91422  ? 129 MET   A C   1 
ATOM   1022 O O   A MET   A 1 129 ? 17.42331  39.78170 -2.85812  0.270 88.52728  ? 129 MET   A O   1 
ATOM   1023 O O   B MET   A 1 129 ? 17.51070  39.56507 -2.70252  0.730 88.31457  ? 129 MET   A O   1 
ATOM   1024 C CB  A MET   A 1 129 ? 17.21481  40.50888 -0.08644  0.270 89.75600  ? 129 MET   A CB  1 
ATOM   1025 C CB  B MET   A 1 129 ? 17.21282  40.26902 0.04444   0.730 92.21256  ? 129 MET   A CB  1 
ATOM   1026 C CG  A MET   A 1 129 ? 17.69808  39.11677 0.27569   0.270 81.24625  ? 129 MET   A CG  1 
ATOM   1027 C CG  B MET   A 1 129 ? 17.05601  41.08239 1.32722   0.730 86.09239  ? 129 MET   A CG  1 
ATOM   1028 S SD  A MET   A 1 129 ? 19.13015  39.17942 1.37090   0.270 70.27741  ? 129 MET   A SD  1 
ATOM   1029 S SD  B MET   A 1 129 ? 17.11398  42.85797 1.03554   0.730 108.32187 ? 129 MET   A SD  1 
ATOM   1030 C CE  A MET   A 1 129 ? 19.79275  37.52738 1.17858   0.270 77.27414  ? 129 MET   A CE  1 
ATOM   1031 C CE  B MET   A 1 129 ? 17.51059  43.46536 2.67226   0.730 71.18536  ? 129 MET   A CE  1 
ATOM   1032 N N   . LEU   A 1 130 ? 15.38603  38.84922 -2.70027  1.000 87.21246  ? 130 LEU   A N   1 
ATOM   1033 C CA  . LEU   A 1 130 ? 15.50175  38.03190 -3.90367  1.000 95.35556  ? 130 LEU   A CA  1 
ATOM   1034 C C   . LEU   A 1 130 ? 14.48474  38.41966 -4.96298  1.000 93.67903  ? 130 LEU   A C   1 
ATOM   1035 O O   . LEU   A 1 130 ? 14.80009  38.40633 -6.15697  1.000 92.51147  ? 130 LEU   A O   1 
ATOM   1036 C CB  . LEU   A 1 130 ? 15.34379  36.53759 -3.55720  1.000 73.12225  ? 130 LEU   A CB  1 
ATOM   1037 C CG  . LEU   A 1 130 ? 15.83595  35.52736 -4.59772  1.000 78.43605  ? 130 LEU   A CG  1 
ATOM   1038 N N   . LYS   A 1 131 ? 13.26640  38.77800 -4.54798  1.000 103.91461 ? 131 LYS   A N   1 
ATOM   1039 C CA  . LYS   A 1 131 ? 12.29652  39.34044 -5.47523  1.000 85.12316  ? 131 LYS   A CA  1 
ATOM   1040 C C   . LYS   A 1 131 ? 12.71455  40.72514 -5.95016  1.000 112.73189 ? 131 LYS   A C   1 
ATOM   1041 O O   . LYS   A 1 131 ? 12.26574  41.16534 -7.01349  1.000 110.21055 ? 131 LYS   A O   1 
ATOM   1042 C CB  . LYS   A 1 131 ? 10.91288  39.38710 -4.82032  1.000 76.50615  ? 131 LYS   A CB  1 
ATOM   1043 N N   . LEU   A 1 132 ? 13.58322  41.40875 -5.19791  1.000 96.60951  ? 132 LEU   A N   1 
ATOM   1044 C CA  . LEU   A 1 132 ? 14.16770  42.67956 -5.60724  1.000 82.21678  ? 132 LEU   A CA  1 
ATOM   1045 C C   . LEU   A 1 132 ? 15.26399  42.50885 -6.64653  1.000 85.57672  ? 132 LEU   A C   1 
ATOM   1046 O O   . LEU   A 1 132 ? 16.09161  43.41303 -6.82372  1.000 102.72387 ? 132 LEU   A O   1 
ATOM   1047 C CB  . LEU   A 1 132 ? 14.71384  43.43370 -4.39020  1.000 75.93451  ? 132 LEU   A CB  1 
ATOM   1048 N N   . VAL   A 1 133 ? 15.28995  41.37120 -7.33569  1.000 94.91036  ? 133 VAL   A N   1 
ATOM   1049 C CA  . VAL   A 1 133 ? 16.26645  41.11136 -8.39029  1.000 116.73035 ? 133 VAL   A CA  1 
ATOM   1050 C C   . VAL   A 1 133 ? 15.82666  39.90881 -9.21211  1.000 95.65243  ? 133 VAL   A C   1 
ATOM   1051 O O   . VAL   A 1 133 ? 15.22317  40.04770 -10.27602 1.000 99.96977  ? 133 VAL   A O   1 
ATOM   1052 C CB  . VAL   A 1 133 ? 17.68721  40.88270 -7.82264  1.000 93.88369  ? 133 VAL   A CB  1 
ATOM   1053 C CG1 . VAL   A 1 133 ? 17.65986  39.83360 -6.72757  1.000 78.41291  ? 133 VAL   A CG1 1 
ATOM   1054 C CG2 . VAL   A 1 133 ? 18.65454  40.45562 -8.93860  1.000 112.49357 ? 133 VAL   A CG2 1 
HETATM 1055 N N1  A A1IUW B 2 .   ? -6.47840  11.59986 17.37905  0.426 45.83100  ? 201 A1IUW A N1  1 
HETATM 1056 N N1  B A1IUW B 2 .   ? -6.46174  11.56594 17.26196  0.574 45.78473  ? 201 A1IUW A N1  1 
HETATM 1057 C C4  A A1IUW B 2 .   ? -7.34183  10.66313 17.89578  0.426 47.53761  ? 201 A1IUW A C4  1 
HETATM 1058 C C4  B A1IUW B 2 .   ? -7.32020  10.64680 17.81950  0.574 47.62282  ? 201 A1IUW A C4  1 
HETATM 1059 C C5  A A1IUW B 2 .   ? -6.82955  9.44457  18.55111  0.426 51.55722  ? 201 A1IUW A C5  1 
HETATM 1060 C C5  B A1IUW B 2 .   ? -6.80990  9.42671  18.47440  0.574 51.17648  ? 201 A1IUW A C5  1 
HETATM 1061 C C6  A A1IUW B 2 .   ? -7.03370  9.21986  19.92507  0.426 51.47074  ? 201 A1IUW A C6  1 
HETATM 1062 C C6  B A1IUW B 2 .   ? -6.02692  8.50496  17.75691  0.574 53.93056  ? 201 A1IUW A C6  1 
HETATM 1063 C C7  A A1IUW B 2 .   ? -6.45293  8.09423  20.50218  0.426 57.09896  ? 201 A1IUW A C7  1 
HETATM 1064 C C7  B A1IUW B 2 .   ? -5.49077  7.42020  18.44453  0.574 56.80934  ? 201 A1IUW A C7  1 
HETATM 1065 C C8  A A1IUW B 2 .   ? -5.68659  7.20130  19.75976  0.426 59.15407  ? 201 A1IUW A C8  1 
HETATM 1066 C C8  B A1IUW B 2 .   ? -5.71916  7.22671  19.80332  0.574 59.12382  ? 201 A1IUW A C8  1 
HETATM 1067 C C10 A A1IUW B 2 .   ? -6.07849  8.54049  17.80004  0.426 53.83140  ? 201 A1IUW A C10 1 
HETATM 1068 C C10 B A1IUW B 2 .   ? -7.06150  9.22359  19.83141  0.574 51.22920  ? 201 A1IUW A C10 1 
HETATM 1069 C C13 A A1IUW B 2 .   ? -7.15838  12.62423 16.80428  0.426 43.47060  ? 201 A1IUW A C13 1 
HETATM 1070 C C13 B A1IUW B 2 .   ? -7.14835  12.60343 16.72045  0.574 43.25441  ? 201 A1IUW A C13 1 
HETATM 1071 C C15 A A1IUW B 2 .   ? -9.57988  13.27142 16.47788  0.426 47.11010  ? 201 A1IUW A C15 1 
HETATM 1072 C C15 B A1IUW B 2 .   ? -9.58039  13.27922 16.49355  0.574 44.02082  ? 201 A1IUW A C15 1 
HETATM 1073 N N   A A1IUW B 2 .   ? -4.87734  4.91710  19.71994  0.426 65.57953  ? 201 A1IUW A N   1 
HETATM 1074 N N   B A1IUW B 2 .   ? -4.96225  4.92492  19.84494  0.574 65.67474  ? 201 A1IUW A N   1 
HETATM 1075 C C   A A1IUW B 2 .   ? -11.60995 11.77862 16.73063  0.426 46.11253  ? 201 A1IUW A C   1 
HETATM 1076 C C   B A1IUW B 2 .   ? -11.62007 11.81122 16.84822  0.574 45.91317  ? 201 A1IUW A C   1 
HETATM 1077 O O   A A1IUW B 2 .   ? -4.68091  6.11954  21.61369  0.426 77.13759  ? 201 A1IUW A O   1 
HETATM 1078 O O   B A1IUW B 2 .   ? -4.68932  6.20466  21.67750  0.574 77.15869  ? 201 A1IUW A O   1 
HETATM 1079 C C1  A A1IUW B 2 .   ? -10.99205 10.41247 16.95766  0.426 49.52407  ? 201 A1IUW A C1  1 
HETATM 1080 C C1  B A1IUW B 2 .   ? -11.00957 10.44253 17.08743  0.574 49.53047  ? 201 A1IUW A C1  1 
HETATM 1081 C C11 A A1IUW B 2 .   ? -5.04090  6.02406  20.43292  0.426 65.61483  ? 201 A1IUW A C11 1 
HETATM 1082 C C11 B A1IUW B 2 .   ? -5.08240  6.06565  20.51166  0.574 65.67925  ? 201 A1IUW A C11 1 
HETATM 1083 C C12 A A1IUW B 2 .   ? -7.83999  10.14835 20.79679  0.426 45.67033  ? 201 A1IUW A C12 1 
HETATM 1084 C C12 B A1IUW B 2 .   ? -5.76508  8.63304  16.27817  0.574 54.05435  ? 201 A1IUW A C12 1 
HETATM 1085 C C14 A A1IUW B 2 .   ? -8.51537  12.35862 16.95531  0.426 45.11621  ? 201 A1IUW A C14 1 
HETATM 1086 C C14 B A1IUW B 2 .   ? -8.50255  12.36504 16.93317  0.574 45.14687  ? 201 A1IUW A C14 1 
HETATM 1087 C C2  A A1IUW B 2 .   ? -9.89957  10.37442 18.02189  0.426 49.80457  ? 201 A1IUW A C2  1 
HETATM 1088 C C2  B A1IUW B 2 .   ? -9.86588  10.41891 18.09806  0.574 49.77454  ? 201 A1IUW A C2  1 
HETATM 1089 C C3  A A1IUW B 2 .   ? -8.63985  11.10411 17.64504  0.426 45.51444  ? 201 A1IUW A C3  1 
HETATM 1090 C C3  B A1IUW B 2 .   ? -8.61746  11.11589 17.63392  0.574 45.87189  ? 201 A1IUW A C3  1 
HETATM 1091 C C9  A A1IUW B 2 .   ? -5.51239  7.43243  18.40197  0.426 56.80562  ? 201 A1IUW A C9  1 
HETATM 1092 C C9  B A1IUW B 2 .   ? -6.51853  8.13381  20.48616  0.574 57.07617  ? 201 A1IUW A C9  1 
HETATM 1093 O O1  A A1IUW B 2 .   ? -9.47713  14.48409 16.61968  0.426 55.81018  ? 201 A1IUW A O1  1 
HETATM 1094 O O1  B A1IUW B 2 .   ? -9.46539  14.49264 16.61887  0.574 55.90618  ? 201 A1IUW A O1  1 
HETATM 1095 C C16 A A1IUW B 2 .   ? -10.80468 12.69840 15.81717  0.426 46.39589  ? 201 A1IUW A C16 1 
HETATM 1096 C C16 B A1IUW B 2 .   ? -10.83442 12.70471 15.89106  0.574 46.24378  ? 201 A1IUW A C16 1 
HETATM 1097 C C17 A A1IUW B 2 .   ? -6.43702  13.75450 16.14411  0.426 40.76119  ? 201 A1IUW A C17 1 
HETATM 1098 C C17 B A1IUW B 2 .   ? -6.43536  13.72512 16.03431  0.574 39.89429  ? 201 A1IUW A C17 1 
HETATM 1099 O O   . HOH   C 3 .   ? 3.89533   28.25479 8.96983   1.000 43.04499  ? 301 HOH   A O   1 
HETATM 1100 O O   . HOH   C 3 .   ? 0.10176   24.24108 2.33459   1.000 68.46176  ? 302 HOH   A O   1 
HETATM 1101 O O   . HOH   C 3 .   ? 13.52059  22.92073 23.74771  1.000 39.82921  ? 303 HOH   A O   1 
HETATM 1102 O O   . HOH   C 3 .   ? -4.32046  24.65438 9.11903   1.000 40.41768  ? 304 HOH   A O   1 
HETATM 1103 O O   . HOH   C 3 .   ? -11.26388 19.98897 6.39481   1.000 45.38649  ? 305 HOH   A O   1 
HETATM 1104 O O   . HOH   C 3 .   ? -17.57778 15.82195 15.78262  1.000 44.30413  ? 306 HOH   A O   1 
HETATM 1105 O O   . HOH   C 3 .   ? 8.13557   16.59250 25.06775  1.000 39.65431  ? 307 HOH   A O   1 
HETATM 1106 O O   . HOH   C 3 .   ? -8.19922  15.87385 14.18057  1.000 34.93553  ? 308 HOH   A O   1 
HETATM 1107 O O   . HOH   C 3 .   ? -17.52034 15.24269 22.27705  1.000 52.79507  ? 309 HOH   A O   1 
HETATM 1108 O O   . HOH   C 3 .   ? 8.09382   32.02136 1.71342   1.000 54.29639  ? 310 HOH   A O   1 
HETATM 1109 O O   . HOH   C 3 .   ? -5.38986  16.34096 14.27575  1.000 34.48837  ? 311 HOH   A O   1 
HETATM 1110 O O   . HOH   C 3 .   ? 0.69056   10.62002 26.46661  1.000 45.25716  ? 312 HOH   A O   1 
HETATM 1111 O O   . HOH   C 3 .   ? -8.78332  19.87896 7.01637   1.000 43.10953  ? 313 HOH   A O   1 
HETATM 1112 O O   . HOH   C 3 .   ? 1.88265   27.11138 15.06746  1.000 36.09153  ? 314 HOH   A O   1 
HETATM 1113 O O   . HOH   C 3 .   ? -2.61658  17.61255 27.46451  1.000 40.32437  ? 315 HOH   A O   1 
HETATM 1114 O O   . HOH   C 3 .   ? -1.83511  25.06372 8.72553   1.000 32.14933  ? 316 HOH   A O   1 
HETATM 1115 O O   . HOH   C 3 .   ? -13.86997 13.63169 25.23146  1.000 49.10410  ? 317 HOH   A O   1 
HETATM 1116 O O   . HOH   C 3 .   ? -6.22467  25.77328 17.88668  1.000 67.93502  ? 318 HOH   A O   1 
HETATM 1117 O O   . HOH   C 3 .   ? -4.26824  11.73158 14.36825  1.000 53.59992  ? 319 HOH   A O   1 
HETATM 1118 O O   . HOH   C 3 .   ? 3.82458   9.81568  19.56074  1.000 52.94969  ? 320 HOH   A O   1 
HETATM 1119 O O   . HOH   C 3 .   ? -10.62580 22.97831 20.35627  1.000 39.84281  ? 321 HOH   A O   1 
HETATM 1120 O O   . HOH   C 3 .   ? -5.60990  15.76993 10.94505  1.000 45.25776  ? 322 HOH   A O   1 
HETATM 1121 O O   . HOH   C 3 .   ? 3.34103   22.56426 4.64946   1.000 51.14071  ? 323 HOH   A O   1 
HETATM 1122 O O   . HOH   C 3 .   ? -1.33643  19.85379 3.10992   1.000 61.25686  ? 324 HOH   A O   1 
HETATM 1123 O O   . HOH   C 3 .   ? -8.57528  22.44854 9.32300   1.000 53.74203  ? 325 HOH   A O   1 
HETATM 1124 O O   . HOH   C 3 .   ? -7.07997  26.09119 15.70658  1.000 37.17832  ? 326 HOH   A O   1 
HETATM 1125 O O   . HOH   C 3 .   ? -13.01087 22.91187 19.30436  1.000 39.45360  ? 327 HOH   A O   1 
HETATM 1126 O O   . HOH   C 3 .   ? -18.78707 14.29006 14.37788  1.000 53.35538  ? 328 HOH   A O   1 
HETATM 1127 O O   . HOH   C 3 .   ? -0.62982  20.47509 29.25095  1.000 50.73195  ? 329 HOH   A O   1 
HETATM 1128 O O   . HOH   C 3 .   ? -8.37732  21.38339 19.86850  1.000 30.44598  ? 330 HOH   A O   1 
HETATM 1129 O O   . HOH   C 3 .   ? -2.49691  8.72425  16.47481  1.000 45.62596  ? 331 HOH   A O   1 
HETATM 1130 O O   . HOH   C 3 .   ? 5.64449   30.95090 18.82048  1.000 30.32107  ? 332 HOH   A O   1 
HETATM 1131 O O   . HOH   C 3 .   ? -1.06601  28.52569 16.91300  1.000 39.51484  ? 333 HOH   A O   1 
HETATM 1132 O O   . HOH   C 3 .   ? -6.11599  23.05876 18.65292  1.000 28.17251  ? 334 HOH   A O   1 
HETATM 1133 O O   . HOH   C 3 .   ? -17.71075 16.44844 24.50715  1.000 38.05999  ? 335 HOH   A O   1 
HETATM 1134 O O   . HOH   C 3 .   ? -15.92113 15.69208 19.93096  1.000 43.97698  ? 336 HOH   A O   1 
HETATM 1135 O O   . HOH   C 3 .   ? -0.45516  28.91713 21.78150  1.000 46.96739  ? 337 HOH   A O   1 
HETATM 1136 O O   . HOH   C 3 .   ? -21.53583 19.36429 26.42077  1.000 51.25005  ? 338 HOH   A O   1 
HETATM 1137 O O   . HOH   C 3 .   ? -10.56912 23.40679 24.03736  1.000 35.54265  ? 339 HOH   A O   1 
HETATM 1138 O O   . HOH   C 3 .   ? -3.92514  13.86600 13.60214  1.000 46.72412  ? 340 HOH   A O   1 
HETATM 1139 O O   . HOH   C 3 .   ? 1.99554   8.88823  7.73710   1.000 61.80142  ? 341 HOH   A O   1 
HETATM 1140 O O   . HOH   C 3 .   ? 2.70189   10.56418 23.99746  1.000 43.54213  ? 342 HOH   A O   1 
HETATM 1141 O O   . HOH   C 3 .   ? -0.26067  7.35085  9.76369   1.000 41.34380  ? 343 HOH   A O   1 
HETATM 1142 O O   . HOH   C 3 .   ? -9.81308  13.58696 3.31684   1.000 62.22164  ? 344 HOH   A O   1 
HETATM 1143 O O   . HOH   C 3 .   ? -16.11548 23.15121 15.22087  1.000 54.07474  ? 345 HOH   A O   1 
HETATM 1144 O O   . HOH   C 3 .   ? -12.44864 13.27558 23.37147  1.000 46.51784  ? 346 HOH   A O   1 
HETATM 1145 O O   . HOH   C 3 .   ? 12.86662  20.55996 25.48982  1.000 45.65050  ? 347 HOH   A O   1 
HETATM 1146 O O   . HOH   C 3 .   ? -12.69336 7.94577  20.39715  1.000 62.54990  ? 348 HOH   A O   1 
HETATM 1147 O O   . HOH   C 3 .   ? 20.18347  23.76570 0.95786   1.000 68.35980  ? 349 HOH   A O   1 
HETATM 1148 O O   . HOH   C 3 .   ? -11.76961 11.38193 2.06420   1.000 52.48098  ? 350 HOH   A O   1 
HETATM 1149 O O   . HOH   C 3 .   ? -13.82970 13.42166 20.71923  1.000 46.67617  ? 351 HOH   A O   1 
HETATM 1150 O O   . HOH   C 3 .   ? -12.19461 3.96591  20.42205  1.000 67.29839  ? 352 HOH   A O   1 
HETATM 1151 O O   . HOH   C 3 .   ? 18.37389  18.71089 5.04579   1.000 53.07433  ? 353 HOH   A O   1 
HETATM 1152 O O   . HOH   C 3 .   ? -20.78816 15.25476 9.48059   1.000 56.44289  ? 354 HOH   A O   1 
HETATM 1153 O O   . HOH   C 3 .   ? -5.78287  17.71836 0.27780   1.000 55.79774  ? 355 HOH   A O   1 
HETATM 1154 O O   . HOH   C 3 .   ? -1.74728  13.05126 33.17277  1.000 54.50424  ? 356 HOH   A O   1 
HETATM 1155 O O   . HOH   C 3 .   ? -16.58207 12.86837 17.62157  1.000 54.10236  ? 357 HOH   A O   1 
HETATM 1156 O O   . HOH   C 3 .   ? -4.19034  2.73632  22.97583  1.000 64.95806  ? 358 HOH   A O   1 
HETATM 1157 O O   . HOH   C 3 .   ? -6.15720  10.23678 25.07731  1.000 47.12364  ? 359 HOH   A O   1 
HETATM 1158 O O   . HOH   C 3 .   ? -17.68970 21.31372 16.76828  1.000 42.45082  ? 360 HOH   A O   1 
HETATM 1159 O O   . HOH   C 3 .   ? -4.54563  12.03695 26.57993  1.000 44.81549  ? 361 HOH   A O   1 
HETATM 1160 O O   . HOH   C 3 .   ? 1.67796   28.66245 13.28277  1.000 35.62400  ? 362 HOH   A O   1 
HETATM 1161 O O   . HOH   C 3 .   ? -6.28582  6.33939  6.32926   1.000 55.07571  ? 363 HOH   A O   1 
HETATM 1162 O O   . HOH   C 3 .   ? 3.35437   10.87415 4.52129   1.000 53.93240  ? 364 HOH   A O   1 
HETATM 1163 O O   . HOH   C 3 .   ? 20.29753  31.54512 12.76587  1.000 53.57003  ? 365 HOH   A O   1 
HETATM 1164 O O   . HOH   C 3 .   ? 2.78777   30.06928 6.48384   1.000 47.06469  ? 366 HOH   A O   1 
HETATM 1165 O O   . HOH   C 3 .   ? 1.41059   19.59947 0.34502   1.000 55.11867  ? 367 HOH   A O   1 
HETATM 1166 O O   . HOH   C 3 .   ? -16.62165 14.58809 25.77688  1.000 47.26786  ? 368 HOH   A O   1 
HETATM 1167 O O   . HOH   C 3 .   ? -5.19503  26.67246 7.02501   1.000 58.15446  ? 369 HOH   A O   1 
HETATM 1168 O O   . HOH   C 3 .   ? -1.31762  27.65609 9.45165   1.000 40.08505  ? 370 HOH   A O   1 
HETATM 1169 O O   . HOH   C 3 .   ? -3.91351  15.02947 -0.28152  1.000 58.12927  ? 371 HOH   A O   1 
HETATM 1170 O O   . HOH   C 3 .   ? -0.41966  3.98931  23.52452  1.000 61.98680  ? 372 HOH   A O   1 
HETATM 1171 O O   . HOH   C 3 .   ? 0.45479   30.39684 6.44368   1.000 53.95296  ? 373 HOH   A O   1 
HETATM 1172 O O   . HOH   C 3 .   ? -20.98630 14.73273 26.64938  1.000 49.14797  ? 374 HOH   A O   1 
HETATM 1173 O O   . HOH   C 3 .   ? -11.34586 9.36388  23.79758  1.000 57.25891  ? 375 HOH   A O   1 
HETATM 1174 O O   . HOH   C 3 .   ? -8.10296  6.87212  26.77336  1.000 77.16027  ? 376 HOH   A O   1 
HETATM 1175 O O   . HOH   C 3 .   ? -18.12536 12.93036 27.42229  1.000 49.06651  ? 377 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   . LEU   A 3   ? 0.61976 1.40244 0.95138 -0.15625 0.12619  0.20968  3   LEU   A N   
2    C CA  . LEU   A 3   ? 0.67791 1.43055 1.00701 -0.14931 0.10908  0.20329  3   LEU   A CA  
3    C C   . LEU   A 3   ? 1.02636 1.71657 1.33127 -0.16039 0.10370  0.21243  3   LEU   A C   
4    O O   . LEU   A 3   ? 1.14894 1.80597 1.43956 -0.14832 0.09160  0.20969  3   LEU   A O   
5    C CB  . LEU   A 3   ? 0.78040 1.56048 1.14287 -0.16162 0.10110  0.19457  3   LEU   A CB  
6    C CG  . LEU   A 3   ? 0.55781 1.31479 0.92063 -0.15357 0.08312  0.18675  3   LEU   A CG  
7    C CD1 . LEU   A 3   ? 0.50860 1.31426 0.89574 -0.13795 0.07681  0.17346  3   LEU   A CD1 
8    C CD2 . LEU   A 3   ? 0.69930 1.42244 1.06773 -0.18163 0.07635  0.18938  3   LEU   A CD2 
9    N N   . GLY   A 4   ? 1.01769 1.69174 1.31770 -0.18241 0.11353  0.22376  4   GLY   A N   
10   C CA  . GLY   A 4   ? 1.09369 1.70898 1.36816 -0.19091 0.11070  0.23360  4   GLY   A CA  
11   C C   . GLY   A 4   ? 0.94917 1.54817 1.19293 -0.18085 0.11984  0.24289  4   GLY   A C   
12   O O   . GLY   A 4   ? 0.82094 1.37441 1.04263 -0.18772 0.11978  0.25237  4   GLY   A O   
13   N N   . SER   A 5   ? 0.80190 1.43731 1.04290 -0.16338 0.12760  0.23944  5   SER   A N   
14   C CA  . SER   A 5   ? 0.91555 1.54324 1.12884 -0.15361 0.13676  0.24623  5   SER   A CA  
15   C C   . SER   A 5   ? 0.72355 1.30581 0.90851 -0.13962 0.12579  0.24522  5   SER   A C   
16   O O   . SER   A 5   ? 0.67086 1.23669 0.85866 -0.13170 0.11231  0.23736  5   SER   A O   
17   C CB  . SER   A 5   ? 0.97133 1.64838 1.18878 -0.13535 0.14567  0.23886  5   SER   A CB  
18   O OG  . SER   A 5   ? 0.90744 1.63001 1.15111 -0.14782 0.15660  0.24019  5   SER   A OG  
19   N N   . PRO   A 6   ? 0.71540 1.27850 0.87301 -0.13627 0.13159  0.25315  6   PRO   A N   
20   C CA  . PRO   A 6   ? 0.66117 1.18894 0.79331 -0.12123 0.12162  0.24981  6   PRO   A CA  
21   C C   . PRO   A 6   ? 0.72965 1.27427 0.86191 -0.09864 0.11710  0.23491  6   PRO   A C   
22   O O   . PRO   A 6   ? 0.82979 1.34589 0.95117 -0.08884 0.10633  0.22915  6   PRO   A O   
23   C CB  . PRO   A 6   ? 0.69246 1.21232 0.79808 -0.12033 0.13151  0.25991  6   PRO   A CB  
24   C CG  . PRO   A 6   ? 0.80404 1.33339 0.91936 -0.14107 0.14456  0.27307  6   PRO   A CG  
25   C CD  . PRO   A 6   ? 0.68565 1.25663 0.83424 -0.14711 0.14737  0.26621  6   PRO   A CD  
26   N N   . GLU   A 7   ? 0.82174 1.41081 0.96591 -0.08965 0.12617  0.22811  7   GLU   A N   
27   C CA  . GLU   A 7   ? 0.71534 1.31708 0.85955 -0.06696 0.12420  0.21300  7   GLU   A CA  
28   C C   . GLU   A 7   ? 0.88577 1.48211 1.04927 -0.06411 0.11328  0.20658  7   GLU   A C   
29   O O   . GLU   A 7   ? 1.04966 1.63047 1.20703 -0.04808 0.10748  0.19732  7   GLU   A O   
30   C CB  . GLU   A 7   ? 0.80336 1.45274 0.95389 -0.05612 0.13762  0.20691  7   GLU   A CB  
31   C CG  . GLU   A 7   ? 0.88978 1.57765 1.06882 -0.06744 0.14316  0.21034  7   GLU   A CG  
32   C CD  . GLU   A 7   ? 1.26624 1.98322 1.46552 -0.05089 0.14151  0.19719  7   GLU   A CD  
33   O OE1 . GLU   A 7   ? 0.98039 1.68442 1.17038 -0.03005 0.13788  0.18599  7   GLU   A OE1 
34   O OE2 . GLU   A 7   ? 0.98259 1.73539 1.20718 -0.05821 0.14452  0.19776  7   GLU   A OE2 
35   N N   . PHE   A 8   ? 0.62093 1.23061 0.80791 -0.07964 0.11103  0.21092  8   PHE   A N   
36   C CA  . PHE   A 8   ? 0.61178 1.21863 0.81642 -0.07698 0.09967  0.20497  8   PHE   A CA  
37   C C   . PHE   A 8   ? 0.63176 1.18877 0.82262 -0.07908 0.08659  0.20741  8   PHE   A C   
38   O O   . PHE   A 8   ? 0.60094 1.14722 0.79326 -0.06537 0.07853  0.20051  8   PHE   A O   
39   C CB  . PHE   A 8   ? 0.46151 1.09460 0.69408 -0.09590 0.09969  0.20756  8   PHE   A CB  
40   C CG  . PHE   A 8   ? 0.48837 1.13693 0.74238 -0.08841 0.09002  0.19838  8   PHE   A CG  
41   C CD1 . PHE   A 8   ? 0.43327 1.05029 0.68826 -0.09396 0.07611  0.19844  8   PHE   A CD1 
42   C CD2 . PHE   A 8   ? 0.60643 1.30199 0.87853 -0.07401 0.09471  0.18952  8   PHE   A CD2 
43   C CE1 . PHE   A 8   ? 0.59036 1.22341 0.86361 -0.08548 0.06707  0.18990  8   PHE   A CE1 
44   C CE2 . PHE   A 8   ? 0.56037 1.27111 0.85042 -0.06438 0.08550  0.18112  8   PHE   A CE2 
45   C CZ  . PHE   A 8   ? 0.90310 1.58298 1.19354 -0.07021 0.07166  0.18130  8   PHE   A CZ  
46   N N   . MET   A 9   ? 0.54190 1.06732 0.71860 -0.09463 0.08508  0.21748  9   MET   A N   
47   C CA  . MET   A 9   ? 0.58847 1.06661 0.74996 -0.09455 0.07288  0.21926  9   MET   A CA  
48   C C   . MET   A 9   ? 0.55359 1.01781 0.69446 -0.07500 0.07230  0.21287  9   MET   A C   
49   O O   . MET   A 9   ? 0.56544 1.00515 0.70231 -0.06692 0.06258  0.20865  9   MET   A O   
50   C CB  . MET   A 9   ? 0.61006 1.05701 0.75958 -0.11259 0.07295  0.23057  9   MET   A CB  
51   C CG  . MET   A 9   ? 0.70755 1.15896 0.87707 -0.13503 0.07385  0.23562  9   MET   A CG  
52   S SD  . MET   A 9   ? 1.09085 1.48884 1.24257 -0.15236 0.07255  0.24707  9   MET   A SD  
53   C CE  . MET   A 9   ? 0.79151 1.18754 0.91525 -0.14425 0.08522  0.25514  9   MET   A CE  
54   N N   A ASN   A 10  ? 0.55500 1.03546 0.68287 -0.06784 0.08321  0.21138  10  ASN   A N   
55   N N   B ASN   A 10  ? 0.55492 1.03552 0.68284 -0.06783 0.08325  0.21137  10  ASN   A N   
56   C CA  A ASN   A 10  ? 0.54331 1.01355 0.65226 -0.05091 0.08400  0.20245  10  ASN   A CA  
57   C CA  B ASN   A 10  ? 0.54314 1.01376 0.65215 -0.05086 0.08412  0.20242  10  ASN   A CA  
58   C C   A ASN   A 10  ? 0.52738 1.00863 0.64669 -0.03343 0.08440  0.19008  10  ASN   A C   
59   C C   B ASN   A 10  ? 0.52726 1.00810 0.64679 -0.03359 0.08417  0.19019  10  ASN   A C   
60   O O   A ASN   A 10  ? 0.49070 0.95005 0.59914 -0.02257 0.08126  0.18277  10  ASN   A O   
61   O O   B ASN   A 10  ? 0.48863 0.94694 0.59778 -0.02299 0.08060  0.18312  10  ASN   A O   
62   C CB  A ASN   A 10  ? 0.53747 1.02761 0.63070 -0.04695 0.09602  0.20193  10  ASN   A CB  
63   C CB  B ASN   A 10  ? 0.53702 1.02880 0.63093 -0.04657 0.09639  0.20160  10  ASN   A CB  
64   C CG  A ASN   A 10  ? 0.53421 1.00561 0.61049 -0.05906 0.09589  0.21422  10  ASN   A CG  
65   C CG  B ASN   A 10  ? 0.51771 1.00292 0.59226 -0.03029 0.09827  0.18915  10  ASN   A CG  
66   O OD1 A ASN   A 10  ? 0.42022 0.85576 0.48507 -0.06200 0.08638  0.21723  10  ASN   A OD1 
67   O OD1 B ASN   A 10  ? 0.52746 0.98501 0.58425 -0.03084 0.09198  0.18951  10  ASN   A OD1 
68   N ND2 A ASN   A 10  ? 0.62510 1.12063 0.69940 -0.06479 0.10729  0.22155  10  ASN   A ND2 
69   N ND2 B ASN   A 10  ? 0.49670 1.00769 0.57472 -0.01543 0.10749  0.17651  10  ASN   A ND2 
70   N N   . LYS   A 11  ? 0.49943 1.01408 0.63982 -0.02976 0.08906  0.18727  11  LYS   A N   
71   C CA  . LYS   A 11  ? 0.41582 0.93810 0.56679 -0.01053 0.08936  0.17647  11  LYS   A CA  
72   C C   . LYS   A 11  ? 0.43571 0.93399 0.59551 -0.01231 0.07631  0.17929  11  LYS   A C   
73   O O   . LYS   A 11  ? 0.44745 0.93399 0.60750 0.00456  0.07516  0.17220  11  LYS   A O   
74   C CB  . LYS   A 11  ? 0.35446 0.92177 0.52488 -0.00341 0.09736  0.17215  11  LYS   A CB  
75   C CG  . LYS   A 11  ? 0.46088 1.05004 0.62285 0.01376  0.11115  0.16154  11  LYS   A CG  
76   C CD  . LYS   A 11  ? 0.61369 1.20673 0.75801 0.00348  0.11806  0.16607  11  LYS   A CD  
77   C CE  . LYS   A 11  ? 0.63791 1.25917 0.77587 0.01992  0.13179  0.15480  11  LYS   A CE  
78   N NZ  . LYS   A 11  ? 0.73725 1.34077 0.86469 0.04188  0.13500  0.13831  11  LYS   A NZ  
79   N N   . GLN   A 12  ? 0.47245 0.96119 0.63871 -0.03195 0.06727  0.18915  12  GLN   A N   
80   C CA  . GLN   A 12  ? 0.56946 1.03775 0.74392 -0.03424 0.05429  0.19120  12  GLN   A CA  
81   C C   . GLN   A 12  ? 0.33402 0.76035 0.49024 -0.02883 0.04782  0.19134  12  GLN   A C   
82   O O   . GLN   A 12  ? 0.43717 0.85331 0.59602 -0.01447 0.04483  0.18704  12  GLN   A O   
83   C CB  . GLN   A 12  ? 0.35439 0.82061 0.53889 -0.05773 0.04739  0.19932  12  GLN   A CB  
84   C CG  . GLN   A 12  ? 0.45775 0.96536 0.66845 -0.06264 0.04929  0.19632  12  GLN   A CG  
85   C CD  . GLN   A 12  ? 0.44315 0.94724 0.66471 -0.08865 0.04459  0.20218  12  GLN   A CD  
86   O OE1 . GLN   A 12  ? 0.57354 1.05850 0.78372 -0.10389 0.04804  0.21006  12  GLN   A OE1 
87   N NE2 . GLN   A 12  ? 0.44737 0.96905 0.69071 -0.09304 0.03723  0.19716  12  GLN   A NE2 
88   N N   . TRP   A 13  ? 0.31949 0.72121 0.45719 -0.03901 0.04601  0.19592  13  TRP   A N   
89   C CA  . TRP   A 13  ? 0.43665 0.80045 0.55813 -0.03481 0.03872  0.19451  13  TRP   A CA  
90   C C   . TRP   A 13  ? 0.40834 0.77198 0.51967 -0.01766 0.04714  0.18439  13  TRP   A C   
91   O O   . TRP   A 13  ? 0.50034 0.83639 0.60289 -0.01226 0.04251  0.18126  13  TRP   A O   
92   C CB  . TRP   A 13  ? 0.39001 0.72896 0.49443 -0.04714 0.03445  0.19957  13  TRP   A CB  
93   C CG  . TRP   A 13  ? 0.46252 0.81386 0.55184 -0.04706 0.04483  0.19913  13  TRP   A CG  
94   C CD1 . TRP   A 13  ? 0.44906 0.81899 0.53939 -0.05703 0.05221  0.20614  13  TRP   A CD1 
95   C CD2 . TRP   A 13  ? 0.44567 0.79256 0.51586 -0.03708 0.04920  0.19141  13  TRP   A CD2 
96   N NE1 . TRP   A 13  ? 0.48694 0.86525 0.55939 -0.05204 0.06049  0.20426  13  TRP   A NE1 
97   C CE2 . TRP   A 13  ? 0.49387 0.85958 0.55369 -0.04006 0.05829  0.19438  13  TRP   A CE2 
98   C CE3 . TRP   A 13  ? 0.47100 0.80126 0.53180 -0.02674 0.04712  0.18193  13  TRP   A CE3 
99   C CZ2 . TRP   A 13  ? 0.48392 0.85485 0.52390 -0.03218 0.06389  0.18736  13  TRP   A CZ2 
100  C CZ3 . TRP   A 13  ? 0.51900 0.85383 0.56075 -0.02096 0.05342  0.17408  13  TRP   A CZ3 
101  C CH2 . TRP   A 13  ? 0.45700 0.81323 0.48835 -0.02322 0.06099  0.17636  13  TRP   A CH2 
102  N N   . TYR   A 14  ? 0.32507 0.71799 0.43745 -0.00910 0.06013  0.17776  14  TYR   A N   
103  C CA  . TYR   A 14  ? 0.33503 0.72713 0.44088 0.00884  0.06979  0.16499  14  TYR   A CA  
104  C C   . TYR   A 14  ? 0.40899 0.79814 0.53084 0.02405  0.06945  0.16194  14  TYR   A C   
105  O O   . TYR   A 14  ? 0.39447 0.76255 0.51078 0.03628  0.07316  0.15483  14  TYR   A O   
106  C CB  . TYR   A 14  ? 0.32417 0.74727 0.42673 0.01612  0.08367  0.15648  14  TYR   A CB  
107  C CG  . TYR   A 14  ? 0.45680 0.87349 0.53528 0.01598  0.08924  0.14873  14  TYR   A CG  
108  C CD1 . TYR   A 14  ? 0.55579 0.97602 0.62134 0.00286  0.08674  0.15649  14  TYR   A CD1 
109  C CD2 . TYR   A 14  ? 0.47063 0.87772 0.53906 0.02970  0.09750  0.13266  14  TYR   A CD2 
110  C CE1 . TYR   A 14  ? 0.55617 0.97521 0.59908 0.00442  0.09059  0.14910  14  TYR   A CE1 
111  C CE2 . TYR   A 14  ? 0.38269 0.78835 0.42866 0.02864  0.10178  0.12282  14  TYR   A CE2 
112  C CZ  . TYR   A 14  ? 0.50519 0.91907 0.53825 0.01651  0.09736  0.13148  14  TYR   A CZ  
113  O OH  . TYR   A 14  ? 0.48806 0.90516 0.49831 0.01721  0.10026  0.12157  14  TYR   A OH  
114  N N   . LEU   A 15  ? 0.31664 0.72665 0.45815 0.02404  0.06545  0.16675  15  LEU   A N   
115  C CA  . LEU   A 15  ? 0.29778 0.70492 0.45297 0.04059  0.06275  0.16460  15  LEU   A CA  
116  C C   . LEU   A 15  ? 0.26094 0.63638 0.41516 0.03499  0.05006  0.17204  15  LEU   A C   
117  O O   . LEU   A 15  ? 0.29914 0.65496 0.45431 0.05142  0.04996  0.16893  15  LEU   A O   
118  C CB  . LEU   A 15  ? 0.24469 0.68731 0.41908 0.04194  0.06091  0.16532  15  LEU   A CB  
119  C CG  . LEU   A 15  ? 0.26447 0.74077 0.44231 0.05282  0.07379  0.15709  15  LEU   A CG  
120  C CD1 . LEU   A 15  ? 0.32294 0.83837 0.52011 0.04584  0.07082  0.15971  15  LEU   A CD1 
121  C CD2 . LEU   A 15  ? 0.37101 0.83835 0.54589 0.08221  0.08268  0.14563  15  LEU   A CD2 
122  N N   . LEU   A 16  ? 0.30023 0.66646 0.45120 0.01341  0.03946  0.18139  16  LEU   A N   
123  C CA  . LEU   A 16  ? 0.30885 0.64382 0.45700 0.00813  0.02688  0.18774  16  LEU   A CA  
124  C C   . LEU   A 16  ? 0.37240 0.67541 0.50315 0.01355  0.02965  0.18458  16  LEU   A C   
125  O O   . LEU   A 16  ? 0.32168 0.59850 0.45074 0.02159  0.02429  0.18435  16  LEU   A O   
126  C CB  . LEU   A 16  ? 0.30003 0.62667 0.44576 -0.01423 0.01569  0.19553  16  LEU   A CB  
127  C CG  . LEU   A 16  ? 0.28626 0.63847 0.45025 -0.02441 0.01157  0.19825  16  LEU   A CG  
128  C CD1 . LEU   A 16  ? 0.29435 0.62913 0.45387 -0.04621 0.00285  0.20447  16  LEU   A CD1 
129  C CD2 . LEU   A 16  ? 0.30988 0.66572 0.48703 -0.01335 0.00499  0.19538  16  LEU   A CD2 
130  N N   . ALA   A 17  ? 0.26808 0.56828 0.38180 0.00953  0.03637  0.17885  17  ALA   A N   
131  C CA  . ALA   A 17  ? 0.26853 0.54058 0.36347 0.01323  0.03916  0.17177  17  ALA   A CA  
132  C C   . ALA   A 17  ? 0.27222 0.53433 0.36934 0.03298  0.04908  0.16011  17  ALA   A C   
133  O O   . ALA   A 17  ? 0.35698 0.58252 0.44408 0.03749  0.04603  0.15390  17  ALA   A O   
134  C CB  . ALA   A 17  ? 0.25363 0.53211 0.33078 0.00620  0.04373  0.16565  17  ALA   A CB  
135  N N   . ASN   A 18  ? 0.28690 0.57612 0.39579 0.04599  0.06014  0.15465  18  ASN   A N   
136  C CA  . ASN   A 18  ? 0.36559 0.63596 0.47391 0.06793  0.06920  0.14157  18  ASN   A CA  
137  C C   . ASN   A 18  ? 0.42244 0.66890 0.53804 0.07893  0.06080  0.14691  18  ASN   A C   
138  O O   . ASN   A 18  ? 0.56908 0.77785 0.67593 0.09092  0.06486  0.13961  18  ASN   A O   
139  C CB  . ASN   A 18  ? 0.37528 0.68266 0.49452 0.08245  0.08261  0.13593  18  ASN   A CB  
140  C CG  . ASN   A 18  ? 0.84761 1.13745 0.95315 0.09582  0.09758  0.11695  18  ASN   A CG  
141  O OD1 . ASN   A 18  ? 1.16154 1.40771 1.25817 0.10484  0.10009  0.10809  18  ASN   A OD1 
142  N ND2 . ASN   A 18  ? 0.58953 0.91256 0.69279 0.09623  0.10847  0.11000  18  ASN   A ND2 
143  N N   . GLN   A 19  ? 0.40743 0.67564 0.53857 0.07442  0.04963  0.15928  19  GLN   A N   
144  C CA  . GLN   A 19  ? 0.42283 0.67186 0.55834 0.08446  0.03964  0.16447  19  GLN   A CA  
145  C C   . GLN   A 19  ? 0.37177 0.57952 0.49160 0.07317  0.03000  0.16665  19  GLN   A C   
146  O O   . GLN   A 19  ? 0.45249 0.62275 0.56083 0.07850  0.02966  0.15828  19  GLN   A O   
147  C CB  . GLN   A 19  ? 0.54154 0.81692 0.68802 0.07638  0.02990  0.16876  19  GLN   A CB  
148  C CG  . GLN   A 19  ? 1.11116 1.36144 1.25054 0.08226  0.02208  0.16373  19  GLN   A CG  
149  C CD  . GLN   A 19  ? 1.07012 1.35128 1.22255 0.07463  0.01279  0.16492  19  GLN   A CD  
150  O OE1 . GLN   A 19  ? 0.76026 1.07904 0.92701 0.06303  0.01265  0.16993  19  GLN   A OE1 
151  N NE2 . GLN   A 19  ? 0.78053 1.04683 0.92792 0.08002  0.00538  0.15864  19  GLN   A NE2 
152  N N   . LEU   A 20  ? 0.37165 0.57918 0.48336 0.05233  0.02503  0.16989  20  LEU   A N   
153  C CA  . LEU   A 20  ? 0.30867 0.47848 0.40568 0.04025  0.01770  0.16225  20  LEU   A CA  
154  C C   . LEU   A 20  ? 0.39411 0.53479 0.47736 0.04940  0.02539  0.15604  20  LEU   A C   
155  O O   . LEU   A 20  ? 0.43917 0.54792 0.51581 0.04907  0.02238  0.14492  20  LEU   A O   
156  C CB  . LEU   A 20  ? 0.42127 0.59820 0.51373 0.02093  0.01147  0.16270  20  LEU   A CB  
157  C CG  . LEU   A 20  ? 0.43751 0.62180 0.54043 0.00750  0.00112  0.16500  20  LEU   A CG  
158  C CD1 . LEU   A 20  ? 0.69169 0.89108 0.79170 -0.00522 -0.00087 0.17013  20  LEU   A CD1 
159  C CD2 . LEU   A 20  ? 0.45465 0.60238 0.54802 0.00322  -0.00707 0.15055  20  LEU   A CD2 
160  N N   . ILE   A 21  ? 0.44243 0.59172 0.52041 0.05127  0.03771  0.14874  21  ILE   A N   
161  C CA  . ILE   A 21  ? 0.42205 0.54207 0.48834 0.05448  0.04693  0.13428  21  ILE   A CA  
162  C C   . ILE   A 21  ? 0.77736 0.87089 0.84769 0.07370  0.05522  0.13105  21  ILE   A C   
163  O O   . ILE   A 21  ? 0.58045 0.63950 0.64258 0.07479  0.06132  0.12266  21  ILE   A O   
164  C CB  . ILE   A 21  ? 0.43377 0.57122 0.49308 0.05046  0.05809  0.12051  21  ILE   A CB  
165  C CG1 . ILE   A 21  ? 0.43980 0.55268 0.48542 0.04370  0.06238  0.10447  21  ILE   A CG1 
166  C CG2 . ILE   A 21  ? 0.51614 0.66548 0.58367 0.06724  0.07172  0.11359  21  ILE   A CG2 
167  C CD1 . ILE   A 21  ? 0.33379 0.44109 0.37105 0.02953  0.04919  0.11059  21  ILE   A CD1 
168  N N   . LEU   A 22  ? 0.47362 0.58339 0.55645 0.08923  0.05608  0.13817  22  LEU   A N   
169  C CA  . LEU   A 22  ? 0.37674 0.46109 0.46088 0.11130  0.06319  0.13901  22  LEU   A CA  
170  C C   . LEU   A 22  ? 0.41767 0.48016 0.49359 0.10161  0.05161  0.13812  22  LEU   A C   
171  O O   . LEU   A 22  ? 0.45180 0.48041 0.51769 0.10479  0.05689  0.13125  22  LEU   A O   
172  C CB  . LEU   A 22  ? 0.43046 0.54563 0.52777 0.13044  0.06730  0.14237  22  LEU   A CB  
173  C CG  . LEU   A 22  ? 0.50810 0.63859 0.60632 0.13777  0.08264  0.13011  22  LEU   A CG  
174  C CD1 . LEU   A 22  ? 0.60826 0.77628 0.72054 0.15608  0.08431  0.13457  22  LEU   A CD1 
175  C CD2 . LEU   A 22  ? 0.74123 0.82478 0.82604 0.14742  0.09891  0.11630  22  LEU   A CD2 
176  N N   . SER   A 23  ? 0.39842 0.48027 0.47750 0.08662  0.03685  0.13893  23  SER   A N   
177  C CA  . SER   A 23  ? 0.34068 0.40421 0.41086 0.07708  0.02623  0.12955  23  SER   A CA  
178  C C   . SER   A 23  ? 0.35559 0.39364 0.41501 0.06644  0.02428  0.12181  23  SER   A C   
179  O O   . SER   A 23  ? 0.41536 0.43338 0.46519 0.06498  0.02080  0.11368  23  SER   A O   
180  C CB  . SER   A 23  ? 0.36898 0.45298 0.44478 0.06535  0.01354  0.13014  23  SER   A CB  
181  O OG  . SER   A 23  ? 0.49331 0.58344 0.57017 0.04974  0.00861  0.13116  23  SER   A OG  
182  N N   . LEU   A 24  ? 0.39176 0.43400 0.45179 0.05946  0.02608  0.12497  24  LEU   A N   
183  C CA  . LEU   A 24  ? 0.37421 0.39639 0.42441 0.05052  0.02457  0.11827  24  LEU   A CA  
184  C C   . LEU   A 24  ? 0.48603 0.48017 0.53317 0.06000  0.03901  0.11745  24  LEU   A C   
185  O O   . LEU   A 24  ? 0.51983 0.49480 0.56011 0.05475  0.03775  0.11048  24  LEU   A O   
186  C CB  . LEU   A 24  ? 0.30885 0.34590 0.35739 0.04029  0.02233  0.12259  24  LEU   A CB  
187  C CG  . LEU   A 24  ? 0.25742 0.30018 0.30046 0.02644  0.00820  0.11508  24  LEU   A CG  
188  C CD1 . LEU   A 24  ? 0.37770 0.42875 0.42620 0.02493  0.00132  0.11343  24  LEU   A CD1 
189  C CD2 . LEU   A 24  ? 0.39957 0.46008 0.43886 0.01831  0.00715  0.11990  24  LEU   A CD2 
190  N N   . SER   A 25  ? 0.45729 0.44621 0.50902 0.07497  0.05471  0.12353  25  SER   A N   
191  C CA  . SER   A 25  ? 0.37367 0.32516 0.42163 0.08485  0.07267  0.11846  25  SER   A CA  
192  C C   . SER   A 25  ? 0.49162 0.43217 0.53442 0.08925  0.07044  0.11378  25  SER   A C   
193  O O   . SER   A 25  ? 0.63210 0.54237 0.66910 0.08954  0.08081  0.10864  25  SER   A O   
194  C CB  . SER   A 25  ? 0.41432 0.36691 0.46531 0.09722  0.08811  0.11215  25  SER   A CB  
195  O OG  . SER   A 25  ? 0.53750 0.51615 0.58657 0.08095  0.08629  0.09961  25  SER   A OG  
196  N N   . LYS   A 26  ? 0.55260 0.51622 0.59673 0.09147  0.05819  0.11585  26  LYS   A N   
197  C CA  . LYS   A 26  ? 0.44598 0.40128 0.48340 0.09677  0.05588  0.11372  26  LYS   A CA  
198  C C   . LYS   A 26  ? 0.44776 0.40321 0.47928 0.08378  0.04179  0.10790  26  LYS   A C   
199  O O   . LYS   A 26  ? 0.55194 0.49940 0.57873 0.08950  0.04475  0.10937  26  LYS   A O   
200  C CB  . LYS   A 26  ? 0.54529 0.52252 0.58645 0.10839  0.05215  0.11824  26  LYS   A CB  
201  C CG  . LYS   A 26  ? 0.58282 0.56386 0.62855 0.12554  0.06552  0.12307  26  LYS   A CG  
202  C CD  . LYS   A 26  ? 0.76892 0.77212 0.81698 0.13882  0.06153  0.12686  26  LYS   A CD  
203  C CE  . LYS   A 26  ? 0.77189 0.80883 0.82899 0.12876  0.04553  0.12825  26  LYS   A CE  
204  N NZ  . LYS   A 26  ? 1.05827 1.12174 1.12798 0.12451  0.04569  0.13291  26  LYS   A NZ  
205  N N   . TYR   A 27  ? 0.49608 0.46184 0.52809 0.07009  0.03089  0.10427  27  TYR   A N   
206  C CA  . TYR   A 27  ? 0.61086 0.58062 0.64110 0.06365  0.02457  0.10276  27  TYR   A CA  
207  C C   . TYR   A 27  ? 0.53253 0.48235 0.55784 0.06199  0.03131  0.10087  27  TYR   A C   
208  O O   . TYR   A 27  ? 0.60992 0.54115 0.63308 0.06086  0.03919  0.09894  27  TYR   A O   
209  C CB  . TYR   A 27  ? 0.43231 0.41614 0.46438 0.05164  0.01431  0.10006  27  TYR   A CB  
210  C CG  . TYR   A 27  ? 0.42009 0.41010 0.45157 0.04742  0.00723  0.09845  27  TYR   A CG  
211  C CD1 . TYR   A 27  ? 0.79770 0.79848 0.83157 0.05021  0.00198  0.10048  27  TYR   A CD1 
212  C CD2 . TYR   A 27  ? 0.42035 0.40468 0.44807 0.04127  0.00553  0.09485  27  TYR   A CD2 
213  C CE1 . TYR   A 27  ? 0.48275 0.48491 0.51394 0.04705  -0.00447 0.09839  27  TYR   A CE1 
214  C CE2 . TYR   A 27  ? 0.48538 0.47386 0.51156 0.03902  -0.00038 0.09321  27  TYR   A CE2 
215  C CZ  . TYR   A 27  ? 0.52993 0.52551 0.55708 0.04188  -0.00522 0.09470  27  TYR   A CZ  
216  O OH  . TYR   A 27  ? 0.55821 0.55372 0.58134 0.04037  -0.01120 0.09253  27  TYR   A OH  
217  N N   . GLU   A 28  ? 0.48342 0.43617 0.50704 0.06145  0.02865  0.10132  28  GLU   A N   
218  C CA  . GLU   A 28  ? 0.47203 0.40950 0.49222 0.05987  0.03508  0.10088  28  GLU   A CA  
219  C C   . GLU   A 28  ? 0.53465 0.46509 0.55411 0.04832  0.03357  0.09600  28  GLU   A C   
220  O O   . GLU   A 28  ? 0.64442 0.58795 0.66399 0.04086  0.02377  0.09319  28  GLU   A O   
221  C CB  . GLU   A 28  ? 0.87156 0.81774 0.88996 0.06077  0.03042  0.10205  28  GLU   A CB  
222  C CG  . GLU   A 28  ? 0.92508 0.86031 0.94121 0.05772  0.03553  0.10200  28  GLU   A CG  
223  C CD  . GLU   A 28  ? 1.05574 0.97076 1.06925 0.06531  0.05074  0.10686  28  GLU   A CD  
224  O OE1 . GLU   A 28  ? 0.97395 0.88866 0.98438 0.07704  0.05587  0.11229  28  GLU   A OE1 
225  O OE2 . GLU   A 28  ? 1.23587 1.13386 1.24951 0.05929  0.05821  0.10542  28  GLU   A OE2 
226  N N   . GLY   A 29  ? 0.41404 0.32206 0.43174 0.04644  0.04428  0.09504  29  GLY   A N   
227  C CA  . GLY   A 29  ? 0.45729 0.35616 0.47462 0.03437  0.04607  0.09124  29  GLY   A CA  
228  C C   . GLY   A 29  ? 0.50566 0.40578 0.52881 0.03279  0.05164  0.09242  29  GLY   A C   
229  O O   . GLY   A 29  ? 0.49642 0.38975 0.52332 0.02223  0.05923  0.09109  29  GLY   A O   
230  N N   . GLY   A 30  ? 0.49043 0.39994 0.51523 0.04163  0.04980  0.09511  30  GLY   A N   
231  C CA  . GLY   A 30  ? 0.49256 0.40627 0.52279 0.04177  0.05584  0.09857  30  GLY   A CA  
232  C C   . GLY   A 30  ? 0.54201 0.42346 0.57540 0.04097  0.07984  0.09523  30  GLY   A C   
233  O O   . GLY   A 30  ? 0.61015 0.49762 0.64514 0.03433  0.08543  0.09056  30  GLY   A O   
234  N N   . HIS   A 31  ? 0.59245 0.44648 0.62414 0.04350  0.09228  0.08953  31  HIS   A N   
235  C CA  . HIS   A 31  ? 0.50428 0.32017 0.53751 0.03893  0.11657  0.07802  31  HIS   A CA  
236  C C   . HIS   A 31  ? 0.58811 0.40261 0.62497 0.01411  0.12131  0.06297  31  HIS   A C   
237  O O   . HIS   A 31  ? 0.68635 0.49424 0.72397 0.00411  0.13250  0.04051  31  HIS   A O   
238  C CB  . HIS   A 31  ? 0.56279 0.35531 0.59192 0.04411  0.12622  0.07572  31  HIS   A CB  
239  C CG  . HIS   A 31  ? 0.55208 0.35085 0.58010 0.03599  0.11824  0.07826  31  HIS   A CG  
240  N ND1 . HIS   A 31  ? 0.68037 0.50406 0.70425 0.04387  0.10045  0.08780  31  HIS   A ND1 
241  C CD2 . HIS   A 31  ? 0.65018 0.43406 0.68116 0.01966  0.12655  0.07028  31  HIS   A CD2 
242  C CE1 . HIS   A 31  ? 0.69992 0.52193 0.72308 0.03572  0.09874  0.08749  31  HIS   A CE1 
243  N NE2 . HIS   A 31  ? 0.82580 0.62532 0.85393 0.02144  0.11426  0.07853  31  HIS   A NE2 
244  N N   . ILE   A 32  ? 0.56501 0.40176 0.60287 0.00342  0.10762  0.06835  32  ILE   A N   
245  C CA  . ILE   A 32  ? 0.58659 0.44426 0.62757 -0.02011 0.10525  0.04863  32  ILE   A CA  
246  C C   . ILE   A 32  ? 0.46847 0.37017 0.50617 -0.02537 0.09212  0.03860  32  ILE   A C   
247  O O   . ILE   A 32  ? 0.49582 0.42061 0.53463 -0.04266 0.09000  0.01964  32  ILE   A O   
248  C CB  . ILE   A 32  ? 0.46257 0.33025 0.50542 -0.02699 0.09637  0.05820  32  ILE   A CB  
249  C CG1 . ILE   A 32  ? 0.64910 0.55385 0.68674 -0.02017 0.07339  0.07242  32  ILE   A CG1 
250  C CG2 . ILE   A 32  ? 0.59601 0.43897 0.63610 -0.01459 0.09936  0.06896  32  ILE   A CG2 
251  C CD1 . ILE   A 32  ? 0.47061 0.38743 0.50849 -0.02433 0.06400  0.08034  32  ILE   A CD1 
252  N N   . PHE   A 33  ? 0.50587 0.42252 0.53963 -0.01103 0.08374  0.05093  33  PHE   A N   
253  C CA  . PHE   A 33  ? 0.46298 0.41909 0.49195 -0.01452 0.07393  0.04467  33  PHE   A CA  
254  C C   . PHE   A 33  ? 0.48435 0.43912 0.51234 -0.00693 0.08437  0.03516  33  PHE   A C   
255  O O   . PHE   A 33  ? 0.50834 0.49646 0.53138 -0.00876 0.07869  0.03025  33  PHE   A O   
256  C CB  . PHE   A 33  ? 0.43684 0.41677 0.46225 -0.00720 0.05548  0.06701  33  PHE   A CB  
257  C CG  . PHE   A 33  ? 0.45070 0.43249 0.47515 -0.01103 0.04438  0.07693  33  PHE   A CG  
258  C CD1 . PHE   A 33  ? 0.36896 0.37347 0.39055 -0.02405 0.03846  0.06615  33  PHE   A CD1 
259  C CD2 . PHE   A 33  ? 0.44632 0.41097 0.47211 0.00012  0.03947  0.09622  33  PHE   A CD2 
260  C CE1 . PHE   A 33  ? 0.30822 0.31708 0.32888 -0.02520 0.02869  0.07501  33  PHE   A CE1 
261  C CE2 . PHE   A 33  ? 0.47331 0.44124 0.49629 -0.00169 0.02894  0.10158  33  PHE   A CE2 
262  C CZ  . PHE   A 33  ? 0.44911 0.43780 0.47047 -0.01403 0.02471  0.09403  33  PHE   A CZ  
263  N N   . GLU   A 34  ? 0.57506 0.49232 0.60622 0.00328  0.10033  0.03330  34  GLU   A N   
264  C CA  . GLU   A 34  ? 0.56899 0.48512 0.59898 0.01522  0.11037  0.02609  34  GLU   A CA  
265  C C   . GLU   A 34  ? 0.63078 0.55791 0.65669 0.00238  0.11797  -0.00314 34  GLU   A C   
266  O O   . GLU   A 34  ? 0.57762 0.53595 0.59919 0.00571  0.11560  -0.00863 34  GLU   A O   
267  C CB  . GLU   A 34  ? 0.60246 0.47247 0.63462 0.03240  0.12634  0.03181  34  GLU   A CB  
268  C CG  . GLU   A 34  ? 0.64895 0.51768 0.67996 0.04981  0.13709  0.02621  34  GLU   A CG  
269  C CD  . GLU   A 34  ? 1.05514 0.96418 1.08930 0.06295  0.12455  0.04384  34  GLU   A CD  
270  O OE1 . GLU   A 34  ? 0.68247 0.60592 0.71983 0.06327  0.10978  0.06376  34  GLU   A OE1 
271  O OE2 . GLU   A 34  ? 0.76431 0.69133 0.79827 0.07223  0.13006  0.03675  34  GLU   A OE2 
272  N N   . LYS   A 35  ? 0.64446 0.54827 0.67189 -0.01301 0.12764  -0.02301 35  LYS   A N   
273  C CA  . LYS   A 35  ? 0.57745 0.49160 0.60165 -0.02743 0.13455  -0.05509 35  LYS   A CA  
274  C C   . LYS   A 35  ? 0.60130 0.54912 0.62598 -0.04875 0.12237  -0.06552 35  LYS   A C   
275  O O   . LYS   A 35  ? 0.73512 0.68452 0.76411 -0.05347 0.11354  -0.05064 35  LYS   A O   
276  C CB  . LYS   A 35  ? 0.69407 0.55454 0.72080 -0.03044 0.15715  -0.07494 35  LYS   A CB  
277  C CG  . LYS   A 35  ? 0.65537 0.47782 0.68036 -0.00526 0.17058  -0.06288 35  LYS   A CG  
278  C CD  . LYS   A 35  ? 0.77683 0.63104 0.79620 0.01034  0.16813  -0.06476 35  LYS   A CD  
279  N N   . LEU   A 36  ? 0.72075 0.69910 0.74012 -0.05973 0.12168  -0.09185 36  LEU   A N   
280  C CA  . LEU   A 36  ? 0.54376 0.56096 0.56302 -0.07808 0.11004  -0.10472 36  LEU   A CA  
281  C C   . LEU   A 36  ? 0.70535 0.69533 0.73684 -0.09677 0.11859  -0.11813 36  LEU   A C   
282  O O   . LEU   A 36  ? 0.74385 0.68416 0.78119 -0.09985 0.13719  -0.12817 36  LEU   A O   
283  C CB  . LEU   A 36  ? 0.53040 0.58730 0.54022 -0.08452 0.10874  -0.13291 36  LEU   A CB  
284  C CG  . LEU   A 36  ? 0.46006 0.55808 0.45630 -0.06963 0.09811  -0.11840 36  LEU   A CG  
285  C CD1 . LEU   A 36  ? 0.48116 0.61587 0.46602 -0.07429 0.09969  -0.14806 36  LEU   A CD1 
286  C CD2 . LEU   A 36  ? 0.52199 0.65221 0.51444 -0.06746 0.07896  -0.09230 36  LEU   A CD2 
287  N N   . VAL   A 37  ? 0.88371 0.90653 0.91887 -0.10870 0.10582  -0.11724 37  VAL   A N   
288  C CA  . VAL   A 37  ? 0.74658 0.75161 0.79562 -0.12725 0.11293  -0.12635 37  VAL   A CA  
289  C C   . VAL   A 37  ? 0.73674 0.73902 0.79222 -0.14985 0.12589  -0.16719 37  VAL   A C   
290  O O   . VAL   A 37  ? 0.75549 0.80621 0.80694 -0.15895 0.11729  -0.19077 37  VAL   A O   
291  C CB  . VAL   A 37  ? 0.60762 0.65605 0.65899 -0.13169 0.09505  -0.11533 37  VAL   A CB  
292  C CG1 . VAL   A 37  ? 0.61594 0.65093 0.68368 -0.15147 0.10366  -0.12448 37  VAL   A CG1 
293  C CG2 . VAL   A 37  ? 0.60548 0.65292 0.64926 -0.11000 0.08239  -0.07759 37  VAL   A CG2 
294  N N   . ASP   A 38  ? 0.79543 0.74025 0.85996 -0.15875 0.14708  -0.17607 38  ASP   A N   
295  C CA  . ASP   A 38  ? 0.83800 0.77226 0.91173 -0.18506 0.16138  -0.21611 38  ASP   A CA  
296  C C   . ASP   A 38  ? 0.75999 0.71975 0.85011 -0.20982 0.15783  -0.22448 38  ASP   A C   
297  O O   . ASP   A 38  ? 1.01852 0.94487 1.11839 -0.21379 0.16675  -0.20722 38  ASP   A O   
298  C CB  . ASP   A 38  ? 0.94105 0.79732 1.01645 -0.18397 0.18757  -0.22078 38  ASP   A CB  
299  C CG  . ASP   A 38  ? 1.20780 1.05322 1.28789 -0.20495 0.20137  -0.26197 38  ASP   A CG  
300  O OD1 . ASP   A 38  ? 1.13792 1.03935 1.22283 -0.22259 0.19050  -0.28713 38  ASP   A OD1 
301  O OD2 . ASP   A 38  ? 1.57454 1.36540 1.65212 -0.19684 0.21958  -0.26110 38  ASP   A OD2 
302  N N   . ALA   A 39  ? 0.67872 0.70194 0.77144 -0.22510 0.14483  -0.25062 39  ALA   A N   
303  C CA  . ALA   A 39  ? 0.68589 0.75027 0.79256 -0.24141 0.13694  -0.25423 39  ALA   A CA  
304  C C   . ALA   A 39  ? 1.01982 1.04445 1.13939 -0.25408 0.15597  -0.25846 39  ALA   A C   
305  O O   . ALA   A 39  ? 0.90384 0.93504 1.03187 -0.25730 0.15414  -0.24374 39  ALA   A O   
306  C CB  . ALA   A 39  ? 0.71366 0.85406 0.81672 -0.24680 0.12069  -0.27914 39  ALA   A CB  
307  N N   . LYS   A 40  ? 0.93000 0.91383 1.05015 -0.26036 0.17419  -0.27751 40  LYS   A N   
308  C CA  . LYS   A 40  ? 1.01940 0.96664 1.15093 -0.27382 0.19264  -0.28208 40  LYS   A CA  
309  C C   . LYS   A 40  ? 1.07739 0.95961 1.20628 -0.26025 0.20592  -0.24880 40  LYS   A C   
310  O O   . LYS   A 40  ? 1.13476 1.00653 1.27182 -0.26685 0.21196  -0.23806 40  LYS   A O   
311  C CB  . LYS   A 40  ? 1.13382 1.06126 1.26655 -0.28481 0.20688  -0.31313 40  LYS   A CB  
312  N N   . LYS   A 41  ? 1.05081 0.89247 1.16731 -0.23927 0.21012  -0.23159 41  LYS   A N   
313  C CA  . LYS   A 41  ? 1.12784 0.91160 1.23912 -0.22128 0.22222  -0.19897 41  LYS   A CA  
314  C C   . LYS   A 41  ? 1.25615 1.05684 1.36804 -0.21149 0.20967  -0.16792 41  LYS   A C   
315  O O   . LYS   A 41  ? 1.54288 1.31183 1.65359 -0.20242 0.21752  -0.14461 41  LYS   A O   
316  C CB  . LYS   A 41  ? 1.07221 0.81467 1.16959 -0.19791 0.22892  -0.18884 41  LYS   A CB  
317  C CG  . LYS   A 41  ? 1.06543 0.78144 1.15998 -0.20262 0.24326  -0.21543 41  LYS   A CG  
318  N N   . GLN   A 42  ? 1.24164 1.09403 1.35416 -0.21201 0.18970  -0.16674 42  GLN   A N   
319  C CA  . GLN   A 42  ? 1.10792 0.98024 1.22083 -0.20210 0.17636  -0.13768 42  GLN   A CA  
320  C C   . GLN   A 42  ? 1.19595 1.11721 1.32066 -0.21897 0.16721  -0.14654 42  GLN   A C   
321  O O   . GLN   A 42  ? 1.07459 1.01898 1.20007 -0.21124 0.15509  -0.12506 42  GLN   A O   
322  C CB  . GLN   A 42  ? 0.89440 0.79338 1.00058 -0.19003 0.16041  -0.12548 42  GLN   A CB  
323  C CG  . GLN   A 42  ? 0.94124 0.80587 1.03347 -0.16901 0.16519  -0.11899 42  GLN   A CG  
324  C CD  . GLN   A 42  ? 1.25013 1.05106 1.33750 -0.15062 0.18048  -0.09289 42  GLN   A CD  
325  O OE1 . GLN   A 42  ? 1.04038 0.83511 1.12774 -0.14259 0.17862  -0.07090 42  GLN   A OE1 
326  N NE2 . GLN   A 42  ? 0.99606 0.75965 1.07481 -0.13625 0.19118  -0.09397 42  GLN   A NE2 
327  N N   . ASN   A 43  ? 1.02320 0.96213 1.15691 -0.24037 0.17284  -0.17766 43  ASN   A N   
328  C CA  . ASN   A 43  ? 1.03226 1.01972 1.17807 -0.25625 0.16567  -0.18877 43  ASN   A CA  
329  C C   . ASN   A 43  ? 0.98382 1.03968 1.12787 -0.25068 0.14104  -0.18578 43  ASN   A C   
330  O O   . ASN   A 43  ? 1.00390 1.08605 1.15198 -0.24670 0.13152  -0.16976 43  ASN   A O   
331  C CB  . ASN   A 43  ? 0.89730 0.85769 1.04910 -0.25612 0.17514  -0.16814 43  ASN   A CB  
332  C CG  . ASN   A 43  ? 1.27271 1.17260 1.42579 -0.26267 0.19936  -0.17245 43  ASN   A CG  
333  O OD1 . ASN   A 43  ? 1.51793 1.36846 1.66336 -0.24714 0.20911  -0.14692 43  ASN   A OD1 
334  N ND2 . ASN   A 43  ? 1.27547 1.18125 1.43721 -0.28433 0.20880  -0.20457 43  ASN   A ND2 
335  N N   . CYS   A 44  ? 0.88448 0.97081 1.02115 -0.24872 0.13073  -0.20102 44  CYS   A N   
336  C CA  . CYS   A 44  ? 0.87526 1.02873 1.00606 -0.24002 0.10678  -0.19790 44  CYS   A CA  
337  C C   . CYS   A 44  ? 0.82122 1.01991 0.94740 -0.24690 0.10022  -0.22971 44  CYS   A C   
338  O O   . CYS   A 44  ? 0.77245 0.98057 0.88695 -0.23873 0.09352  -0.23304 44  CYS   A O   
339  C CB  . CYS   A 44  ? 0.73874 0.88272 0.85954 -0.22089 0.09782  -0.16940 44  CYS   A CB  
340  S SG  . CYS   A 44  ? 1.32628 1.43633 1.44962 -0.20752 0.10042  -0.12951 44  CYS   A SG  
341  N N   . PRO   A 45  ? 0.78224 1.01328 0.91710 -0.26125 0.10206  -0.25337 45  PRO   A N   
342  C CA  . PRO   A 45  ? 0.76846 1.04141 0.89976 -0.26722 0.09855  -0.28443 45  PRO   A CA  
343  C C   . PRO   A 45  ? 0.73438 1.07412 0.85092 -0.24969 0.07574  -0.27958 45  PRO   A C   
344  O O   . PRO   A 45  ? 0.99334 1.36840 1.10384 -0.24943 0.07213  -0.30059 45  PRO   A O   
345  C CB  . PRO   A 45  ? 0.81933 1.10933 0.96681 -0.28744 0.10741  -0.30683 45  PRO   A CB  
346  C CG  . PRO   A 45  ? 0.65859 0.94900 0.81292 -0.28520 0.10431  -0.28411 45  PRO   A CG  
347  C CD  . PRO   A 45  ? 0.73858 0.97249 0.88760 -0.27254 0.10784  -0.25259 45  PRO   A CD  
348  N N   . ASP   A 46  ? 0.62088 0.97786 0.73053 -0.23297 0.06103  -0.25088 46  ASP   A N   
349  C CA  . ASP   A 46  ? 0.62961 1.04460 0.72247 -0.21226 0.04076  -0.24090 46  ASP   A CA  
350  C C   . ASP   A 46  ? 0.60977 1.01175 0.68608 -0.19307 0.03049  -0.21457 46  ASP   A C   
351  O O   . ASP   A 46  ? 1.20044 1.63765 1.26089 -0.17177 0.01449  -0.19559 46  ASP   A O   
352  C CB  . ASP   A 46  ? 0.58746 1.03813 0.68267 -0.20478 0.03125  -0.22874 46  ASP   A CB  
353  C CG  . ASP   A 46  ? 0.66511 1.08115 0.76496 -0.19962 0.03068  -0.20021 46  ASP   A CG  
354  O OD1 . ASP   A 46  ? 0.60302 0.96456 0.71469 -0.21230 0.04542  -0.19822 46  ASP   A OD1 
355  O OD2 . ASP   A 46  ? 0.67014 1.11124 0.76116 -0.18080 0.01692  -0.17849 46  ASP   A OD2 
356  N N   . TYR   A 47  ? 0.47095 0.82040 0.55053 -0.19920 0.04097  -0.21163 47  TYR   A N   
357  C CA  . TYR   A 47  ? 0.51804 0.84985 0.58166 -0.17826 0.03325  -0.18212 47  TYR   A CA  
358  C C   . TYR   A 47  ? 0.45624 0.82794 0.49780 -0.16467 0.02154  -0.18610 47  TYR   A C   
359  O O   . TYR   A 47  ? 0.75885 1.15013 0.78294 -0.14294 0.00713  -0.15938 47  TYR   A O   
360  C CB  . TYR   A 47  ? 0.40857 0.66471 0.47464 -0.17696 0.05152  -0.17214 47  TYR   A CB  
361  C CG  . TYR   A 47  ? 0.53679 0.76862 0.58544 -0.15035 0.04558  -0.13710 47  TYR   A CG  
362  C CD1 . TYR   A 47  ? 0.46930 0.68402 0.51671 -0.13628 0.03916  -0.10393 47  TYR   A CD1 
363  C CD2 . TYR   A 47  ? 0.39195 0.62112 0.42603 -0.14008 0.04650  -0.13862 47  TYR   A CD2 
364  C CE1 . TYR   A 47  ? 0.50106 0.69588 0.53467 -0.11488 0.03345  -0.07464 47  TYR   A CE1 
365  C CE2 . TYR   A 47  ? 0.55333 0.76481 0.57454 -0.11860 0.04169  -0.10765 47  TYR   A CE2 
366  C CZ  . TYR   A 47  ? 0.43229 0.62640 0.45405 -0.10716 0.03495  -0.07645 47  TYR   A CZ  
367  O OH  . TYR   A 47  ? 0.47862 0.65678 0.48971 -0.08868 0.03005  -0.04834 47  TYR   A OH  
368  N N   . TYR   A 48  ? 0.60707 0.99010 0.64795 -0.17707 0.02841  -0.21935 48  TYR   A N   
369  C CA  . TYR   A 48  ? 0.74783 1.16611 0.76666 -0.16205 0.02058  -0.22184 48  TYR   A CA  
370  C C   . TYR   A 48  ? 0.62947 1.10733 0.64576 -0.15136 0.01085  -0.22193 48  TYR   A C   
371  O O   . TYR   A 48  ? 0.69548 1.20427 0.69769 -0.13739 0.00553  -0.22036 48  TYR   A O   
372  C CB  . TYR   A 48  ? 0.63394 1.03108 0.65221 -0.17302 0.03502  -0.25242 48  TYR   A CB  
373  C CG  . TYR   A 48  ? 0.58889 0.91266 0.60884 -0.16743 0.05036  -0.23608 48  TYR   A CG  
374  C CD1 . TYR   A 48  ? 0.52525 0.83517 0.52833 -0.14412 0.04785  -0.20684 48  TYR   A CD1 
375  C CD2 . TYR   A 48  ? 0.65998 0.92850 0.69904 -0.18385 0.06827  -0.24703 48  TYR   A CD2 
376  C CE1 . TYR   A 48  ? 0.61104 0.86006 0.61729 -0.13633 0.06119  -0.19096 48  TYR   A CE1 
377  C CE2 . TYR   A 48  ? 0.48275 0.68568 0.52196 -0.17393 0.08234  -0.22917 48  TYR   A CE2 
378  C CZ  . TYR   A 48  ? 0.54626 0.74263 0.56959 -0.14957 0.07789  -0.20192 48  TYR   A CZ  
379  O OH  . TYR   A 48  ? 0.58359 0.72194 0.60820 -0.13821 0.09086  -0.18504 48  TYR   A OH  
380  N N   . ASP   A 49  ? 0.51844 1.01227 0.54836 -0.15682 0.00974  -0.22341 49  ASP   A N   
381  C CA  . ASP   A 49  ? 0.59620 1.14319 0.62188 -0.14208 -0.00017 -0.21699 49  ASP   A CA  
382  C C   . ASP   A 49  ? 0.46596 1.01158 0.47771 -0.11759 -0.01213 -0.17814 49  ASP   A C   
383  O O   . ASP   A 49  ? 0.54671 1.12790 0.55070 -0.09948 -0.01956 -0.16730 49  ASP   A O   
384  C CB  . ASP   A 49  ? 0.66747 1.23467 0.71229 -0.15824 0.00510  -0.23794 49  ASP   A CB  
385  C CG  . ASP   A 49  ? 0.96725 1.54059 1.02624 -0.18107 0.01724  -0.27702 49  ASP   A CG  
386  O OD1 . ASP   A 49  ? 0.98058 1.57931 1.03287 -0.17649 0.01589  -0.28992 49  ASP   A OD1 
387  O OD2 . ASP   A 49  ? 0.95657 1.50716 1.03361 -0.20314 0.02880  -0.29386 49  ASP   A OD2 
388  N N   . VAL   A 50  ? 0.48191 0.98461 0.49159 -0.11636 -0.01311 -0.15730 50  VAL   A N   
389  C CA  . VAL   A 50  ? 0.54997 1.04074 0.54659 -0.09339 -0.02300 -0.11986 50  VAL   A CA  
390  C C   . VAL   A 50  ? 0.41199 0.87774 0.39192 -0.08212 -0.02532 -0.09983 50  VAL   A C   
391  O O   . VAL   A 50  ? 0.37599 0.84333 0.34206 -0.06094 -0.03099 -0.07537 50  VAL   A O   
392  C CB  . VAL   A 50  ? 0.46436 0.92910 0.47191 -0.09795 -0.02343 -0.10809 50  VAL   A CB  
393  C CG1 . VAL   A 50  ? 0.49253 0.93965 0.48659 -0.07308 -0.03245 -0.07102 50  VAL   A CG1 
394  C CG2 . VAL   A 50  ? 0.46333 0.95441 0.48655 -0.10936 -0.01974 -0.12741 50  VAL   A CG2 
395  N N   . ILE   A 51  ? 0.49864 0.93798 0.48106 -0.09697 -0.01912 -0.11094 51  ILE   A N   
396  C CA  . ILE   A 51  ? 0.43908 0.85368 0.40516 -0.08687 -0.01856 -0.09292 51  ILE   A CA  
397  C C   . ILE   A 51  ? 0.49877 0.93844 0.45418 -0.08793 -0.01424 -0.11362 51  ILE   A C   
398  O O   . ILE   A 51  ? 0.52874 0.95817 0.49338 -0.10392 -0.00262 -0.14328 51  ILE   A O   
399  C CB  . ILE   A 51  ? 0.41802 0.76624 0.39893 -0.09188 -0.00445 -0.08436 51  ILE   A CB  
400  C CG1 . ILE   A 51  ? 0.29648 0.62157 0.28810 -0.08974 -0.00779 -0.06478 51  ILE   A CG1 
401  C CG2 . ILE   A 51  ? 0.44060 0.76159 0.40940 -0.07839 -0.00094 -0.06338 51  ILE   A CG2 
402  C CD1 . ILE   A 51  ? 0.53635 0.87415 0.51232 -0.07020 -0.02338 -0.03421 51  ILE   A CD1 
403  N N   . LYS   A 52  ? 0.40907 0.86784 0.35195 -0.06823 -0.01925 -0.09437 52  LYS   A N   
404  C CA  . LYS   A 52  ? 0.45077 0.93569 0.38605 -0.06566 -0.01571 -0.10928 52  LYS   A CA  
405  C C   . LYS   A 52  ? 0.48751 0.95184 0.40688 -0.05876 -0.01051 -0.09616 52  LYS   A C   
406  O O   . LYS   A 52  ? 0.44237 0.92317 0.35561 -0.05858 -0.00509 -0.11215 52  LYS   A O   
407  C CB  . LYS   A 52  ? 0.40675 0.92816 0.33884 -0.04915 -0.02273 -0.09863 52  LYS   A CB  
408  C CG  . LYS   A 52  ? 0.46156 1.00284 0.40564 -0.04925 -0.02737 -0.10231 52  LYS   A CG  
409  C CD  . LYS   A 52  ? 0.43421 0.99197 0.39588 -0.07175 -0.02207 -0.13948 52  LYS   A CD  
410  C CE  . LYS   A 52  ? 0.51766 1.11223 0.48112 -0.07770 -0.01853 -0.16912 52  LYS   A CE  
411  N NZ  . LYS   A 52  ? 0.48175 1.08645 0.46521 -0.10141 -0.01147 -0.20575 52  LYS   A NZ  
412  N N   . ASN   A 53  ? 0.55759 0.98752 0.47131 -0.05245 -0.01117 -0.06711 53  ASN   A N   
413  C CA  . ASN   A 53  ? 0.49357 0.90381 0.39519 -0.04592 -0.00372 -0.05139 53  ASN   A CA  
414  C C   . ASN   A 53  ? 0.43417 0.78652 0.35748 -0.05157 0.00590  -0.04621 53  ASN   A C   
415  O O   . ASN   A 53  ? 0.43600 0.75983 0.36255 -0.04483 0.00247  -0.01735 53  ASN   A O   
416  C CB  . ASN   A 53  ? 0.45255 0.85425 0.35116 -0.02882 -0.01021 -0.01364 53  ASN   A CB  
417  C CG  . ASN   A 53  ? 0.67785 1.06898 0.56884 -0.02335 -0.00217 0.00033  53  ASN   A CG  
418  O OD1 . ASN   A 53  ? 0.76154 1.15747 0.64784 -0.02856 0.00919  -0.01824 53  ASN   A OD1 
419  N ND2 . ASN   A 53  ? 0.53425 0.90814 0.42639 -0.01319 -0.00558 0.03035  53  ASN   A ND2 
420  N N   . PRO   A 54  ? 0.35546 0.68830 0.29282 -0.06309 0.01825  -0.07387 54  PRO   A N   
421  C CA  . PRO   A 54  ? 0.43552 0.71276 0.39139 -0.06599 0.02833  -0.06811 54  PRO   A CA  
422  C C   . PRO   A 54  ? 0.53209 0.78582 0.48615 -0.05382 0.03466  -0.04729 54  PRO   A C   
423  O O   . PRO   A 54  ? 0.57526 0.85189 0.51690 -0.04704 0.03671  -0.04631 54  PRO   A O   
424  C CB  . PRO   A 54  ? 0.43252 0.69708 0.39966 -0.08084 0.04153  -0.10514 54  PRO   A CB  
425  C CG  . PRO   A 54  ? 0.44599 0.76467 0.40437 -0.08923 0.03454  -0.13193 54  PRO   A CG  
426  C CD  . PRO   A 54  ? 0.44064 0.80012 0.37687 -0.07403 0.02365  -0.11290 54  PRO   A CD  
427  N N   . MET   A 55  ? 0.57320 0.78430 0.54023 -0.05073 0.03801  -0.03066 55  MET   A N   
428  C CA  . MET   A 55  ? 0.48059 0.67268 0.44958 -0.03927 0.04288  -0.01086 55  MET   A CA  
429  C C   . MET   A 55  ? 0.39951 0.54392 0.38434 -0.03724 0.05003  -0.00482 55  MET   A C   
430  O O   . MET   A 55  ? 0.41888 0.54712 0.41011 -0.04147 0.04540  0.00039  55  MET   A O   
431  C CB  . MET   A 55  ? 0.36289 0.57170 0.32264 -0.03158 0.03063  0.01963  55  MET   A CB  
432  C CG  . MET   A 55  ? 0.35376 0.55332 0.31729 -0.02261 0.03538  0.03808  55  MET   A CG  
433  S SD  . MET   A 55  ? 0.53447 0.75640 0.49257 -0.01861 0.04927  0.02142  55  MET   A SD  
434  C CE  . MET   A 55  ? 0.49385 0.76685 0.42845 -0.02040 0.04124  0.02154  55  MET   A CE  
435  N N   . SER   A 56  ? 0.44143 0.56607 0.43138 -0.02880 0.06171  -0.00492 56  SER   A N   
436  C CA  . SER   A 56  ? 0.39263 0.47356 0.39482 -0.02234 0.06969  0.00244  56  SER   A CA  
437  C C   . SER   A 56  ? 0.46638 0.54688 0.47154 -0.00727 0.07202  0.01993  56  SER   A C   
438  O O   . SER   A 56  ? 0.56845 0.68012 0.56760 -0.00420 0.07058  0.02287  56  SER   A O   
439  C CB  . SER   A 56  ? 0.47504 0.52496 0.48222 -0.02737 0.08636  -0.02355 56  SER   A CB  
440  O OG  . SER   A 56  ? 0.57256 0.62898 0.57529 -0.02192 0.09729  -0.03989 56  SER   A OG  
441  N N   . PHE   A 57  ? 0.41907 0.46715 0.43376 0.00255  0.07604  0.03190  57  PHE   A N   
442  C CA  . PHE   A 57  ? 0.38717 0.43872 0.40754 0.01779  0.07824  0.04665  57  PHE   A CA  
443  C C   . PHE   A 57  ? 0.45552 0.51357 0.47441 0.02532  0.09261  0.03015  57  PHE   A C   
444  O O   . PHE   A 57  ? 0.48906 0.57469 0.50944 0.03308  0.09263  0.03802  57  PHE   A O   
445  C CB  . PHE   A 57  ? 0.45489 0.47243 0.48397 0.02937  0.08018  0.06016  57  PHE   A CB  
446  C CG  . PHE   A 57  ? 0.45135 0.46637 0.48157 0.02559  0.06536  0.07836  57  PHE   A CG  
447  C CD1 . PHE   A 57  ? 0.50200 0.54474 0.52719 0.01622  0.05077  0.08701  57  PHE   A CD1 
448  C CD2 . PHE   A 57  ? 0.46422 0.44760 0.49858 0.03329  0.06689  0.08730  57  PHE   A CD2 
449  C CE1 . PHE   A 57  ? 0.40772 0.44510 0.43263 0.01448  0.03766  0.10222  57  PHE   A CE1 
450  C CE2 . PHE   A 57  ? 0.38123 0.36346 0.41529 0.03129  0.05347  0.10240  57  PHE   A CE2 
451  C CZ  . PHE   A 57  ? 0.34772 0.35626 0.37739 0.02183  0.03867  0.10886  57  PHE   A CZ  
452  N N   . SER   A 58  ? 0.54399 0.57709 0.56029 0.02251  0.10573  0.00625  58  SER   A N   
453  C CA  . SER   A 58  ? 0.51917 0.55446 0.53210 0.03077  0.12023  -0.01276 58  SER   A CA  
454  C C   . SER   A 58  ? 0.54636 0.62983 0.54940 0.02424  0.11597  -0.02173 58  SER   A C   
455  O O   . SER   A 58  ? 0.53547 0.63884 0.53638 0.03501  0.12353  -0.02593 58  SER   A O   
456  C CB  . SER   A 58  ? 0.63979 0.63266 0.65117 0.02607  0.13530  -0.03854 58  SER   A CB  
457  O OG  . SER   A 58  ? 0.82721 0.82785 0.83458 0.00450  0.12994  -0.05495 58  SER   A OG  
458  N N   . CYS   A 59  ? 0.53583 0.64079 0.53169 0.00850  0.10443  -0.02413 59  CYS   A N   
459  C CA  . CYS   A 59  ? 0.53584 0.68846 0.51907 0.00432  0.09966  -0.02887 59  CYS   A CA  
460  C C   . CYS   A 59  ? 0.45919 0.64093 0.44323 0.01159  0.09338  -0.00128 59  CYS   A C   
461  O O   . CYS   A 59  ? 0.58566 0.80262 0.56147 0.01488  0.09689  -0.00315 59  CYS   A O   
462  C CB  . CYS   A 59  ? 0.43951 0.60928 0.41425 -0.01104 0.08796  -0.03534 59  CYS   A CB  
463  S SG  . CYS   A 59  ? 0.68551 0.82755 0.66348 -0.02539 0.09470  -0.06913 59  CYS   A SG  
464  N N   . ILE   A 60  ? 0.44345 0.61185 0.43741 0.01333  0.08485  0.02359  60  ILE   A N   
465  C CA  . ILE   A 60  ? 0.37875 0.57225 0.37634 0.01681  0.07924  0.04853  60  ILE   A CA  
466  C C   . ILE   A 60  ? 0.40498 0.60260 0.41394 0.03109  0.09038  0.05015  60  ILE   A C   
467  O O   . ILE   A 60  ? 0.45309 0.68532 0.46305 0.03345  0.09251  0.05964  60  ILE   A O   
468  C CB  . ILE   A 60  ? 0.43728 0.61569 0.44094 0.01253  0.06528  0.07108  60  ILE   A CB  
469  C CG1 . ILE   A 60  ? 0.27622 0.45491 0.26784 0.00128  0.05475  0.06907  60  ILE   A CG1 
470  C CG2 . ILE   A 60  ? 0.36686 0.56823 0.37591 0.01276  0.05998  0.09484  60  ILE   A CG2 
471  C CD1 . ILE   A 60  ? 0.25090 0.41161 0.24644 -0.00134 0.04169  0.08793  60  ILE   A CD1 
472  N N   . LYS   A 61  ? 0.46597 0.62974 0.48341 0.04175  0.09856  0.04186  61  LYS   A N   
473  C CA  . LYS   A 61  ? 0.40920 0.57804 0.43638 0.05951  0.10972  0.04216  61  LYS   A CA  
474  C C   . LYS   A 61  ? 0.51177 0.70588 0.53038 0.06428  0.12215  0.02337  61  LYS   A C   
475  O O   . LYS   A 61  ? 0.49009 0.71396 0.51500 0.07531  0.12836  0.02877  61  LYS   A O   
476  C CB  . LYS   A 61  ? 0.41467 0.53721 0.44814 0.07264  0.11733  0.03729  61  LYS   A CB  
477  C CG  . LYS   A 61  ? 0.37704 0.47905 0.41878 0.07238  0.10613  0.05724  61  LYS   A CG  
478  C CD  . LYS   A 61  ? 0.47850 0.53169 0.52192 0.08531  0.11568  0.05266  61  LYS   A CD  
479  C CE  . LYS   A 61  ? 0.63402 0.66999 0.68323 0.08656  0.10472  0.07238  61  LYS   A CE  
480  N NZ  . LYS   A 61  ? 0.56006 0.54759 0.60830 0.10014  0.11560  0.07086  61  LYS   A NZ  
481  N N   . THR   A 62  ? 0.45239 0.63906 0.45700 0.05595  0.12581  -0.00001 62  THR   A N   
482  C CA  . THR   A 62  ? 0.46068 0.67328 0.45433 0.06044  0.13684  -0.02065 62  THR   A CA  
483  C C   . THR   A 62  ? 0.49240 0.75923 0.47936 0.05528  0.13164  -0.00690 62  THR   A C   
484  O O   . THR   A 62  ? 0.55858 0.85709 0.54490 0.06548  0.14118  -0.00859 62  THR   A O   
485  C CB  . THR   A 62  ? 0.52661 0.72099 0.50732 0.05044  0.14033  -0.05126 62  THR   A CB  
486  O OG1 . THR   A 62  ? 0.76774 0.90790 0.75476 0.05528  0.14954  -0.06424 62  THR   A OG1 
487  C CG2 . THR   A 62  ? 0.56337 0.78921 0.53006 0.05471  0.15008  -0.07454 62  THR   A CG2 
488  N N   . LYS   A 63  ? 0.44078 0.71835 0.42194 0.04058  0.11770  0.00791  63  LYS   A N   
489  C CA  . LYS   A 63  ? 0.50168 0.82470 0.47433 0.03563  0.11403  0.02471  63  LYS   A CA  
490  C C   . LYS   A 63  ? 0.45751 0.79892 0.44646 0.04088  0.11605  0.04881  63  LYS   A C   
491  O O   . LYS   A 63  ? 0.49813 0.87556 0.48347 0.04075  0.11961  0.05683  63  LYS   A O   
492  C CB  . LYS   A 63  ? 0.40292 0.72614 0.36533 0.02164  0.09900  0.03755  63  LYS   A CB  
493  C CG  . LYS   A 63  ? 0.54046 0.85982 0.48735 0.01536  0.09596  0.01330  63  LYS   A CG  
494  C CD  . LYS   A 63  ? 0.52517 0.84763 0.46267 0.00518  0.08067  0.02758  63  LYS   A CD  
495  C CE  . LYS   A 63  ? 0.54779 0.90705 0.47116 0.00456  0.07748  0.04969  63  LYS   A CE  
496  N NZ  . LYS   A 63  ? 0.62066 0.97414 0.53504 -0.00146 0.06098  0.06183  63  LYS   A NZ  
497  N N   . LEU   A 64  ? 0.51659 0.83179 0.52403 0.04467  0.11210  0.05950  64  LEU   A N   
498  C CA  . LEU   A 64  ? 0.37154 0.70874 0.39767 0.05002  0.11394  0.07806  64  LEU   A CA  
499  C C   . LEU   A 64  ? 0.43974 0.79764 0.47173 0.06768  0.12982  0.06508  64  LEU   A C   
500  O O   . LEU   A 64  ? 0.48172 0.87037 0.52107 0.06805  0.13090  0.07388  64  LEU   A O   
501  C CB  . LEU   A 64  ? 0.36355 0.67069 0.40621 0.05165  0.10459  0.09017  64  LEU   A CB  
502  C CG  . LEU   A 64  ? 0.35869 0.65422 0.40043 0.03580  0.08856  0.10894  64  LEU   A CG  
503  C CD1 . LEU   A 64  ? 0.38946 0.65306 0.44444 0.04068  0.08051  0.11524  64  LEU   A CD1 
504  C CD2 . LEU   A 64  ? 0.33097 0.65694 0.37684 0.02498  0.08378  0.12745  64  LEU   A CD2 
505  N N   . LYS   A 65  ? 0.52318 0.85136 0.55066 0.08044  0.13833  0.04184  65  LYS   A N   
506  C CA  . LYS   A 65  ? 0.47652 0.81862 0.50748 0.10076  0.15422  0.02783  65  LYS   A CA  
507  C C   . LYS   A 65  ? 0.60942 0.98992 0.62573 0.09874  0.16142  0.01706  65  LYS   A C   
508  O O   . LYS   A 65  ? 0.67722 1.08036 0.69928 0.10799  0.16690  0.01664  65  LYS   A O   
509  C CB  . LYS   A 65  ? 0.50752 0.79823 0.53421 0.11381  0.16235  0.00528  65  LYS   A CB  
510  C CG  . LYS   A 65  ? 0.74466 1.04006 0.77466 0.13943  0.17921  -0.00838 65  LYS   A CG  
511  C CD  . LYS   A 65  ? 0.83767 1.07201 0.86193 0.15168  0.18852  -0.02857 65  LYS   A CD  
512  C CE  . LYS   A 65  ? 0.75573 0.99041 0.78152 0.18095  0.20600  -0.04111 65  LYS   A CE  
513  N N   . LYS   A 66  ? 0.59846 0.98129 0.59494 0.08550  0.15780  0.00795  66  LYS   A N   
514  C CA  . LYS   A 66  ? 0.42481 0.83519 0.40427 0.08230  0.15973  -0.00186 66  LYS   A CA  
515  C C   . LYS   A 66  ? 0.41333 0.85121 0.39206 0.06881  0.14888  0.02418  66  LYS   A C   
516  O O   . LYS   A 66  ? 0.55162 1.01341 0.51553 0.06678  0.14973  0.02056  66  LYS   A O   
517  C CB  . LYS   A 66  ? 0.53016 0.93153 0.48757 0.07621  0.15982  -0.02705 66  LYS   A CB  
518  C CG  . LYS   A 66  ? 0.69653 1.06667 0.65187 0.08805  0.17263  -0.05982 66  LYS   A CG  
519  C CD  . LYS   A 66  ? 0.68333 1.04686 0.61862 0.07749  0.17048  -0.08873 66  LYS   A CD  
520  C CE  . LYS   A 66  ? 0.74702 1.06440 0.68211 0.08447  0.18156  -0.12227 66  LYS   A CE  
521  N NZ  . LYS   A 66  ? 0.91851 1.23190 0.83713 0.07082  0.17907  -0.15392 66  LYS   A NZ  
522  N N   . GLY   A 67  ? 0.44321 0.87574 0.43705 0.06025  0.13907  0.04937  67  GLY   A N   
523  C CA  . GLY   A 67  ? 0.45699 0.90785 0.45107 0.04737  0.13015  0.07255  67  GLY   A CA  
524  C C   . GLY   A 67  ? 0.35661 0.80787 0.32888 0.03657  0.12185  0.07566  67  GLY   A C   
525  O O   . GLY   A 67  ? 0.41923 0.89244 0.38299 0.03295  0.12140  0.08434  67  GLY   A O   
526  N N   . GLN   A 68  ? 0.40309 0.83186 0.36649 0.03249  0.11549  0.06921  68  GLN   A N   
527  C CA  . GLN   A 68  ? 0.42699 0.85807 0.36960 0.02520  0.10653  0.06950  68  GLN   A CA  
528  C C   . GLN   A 68  ? 0.44271 0.85610 0.38823 0.01419  0.09212  0.09386  68  GLN   A C   
529  O O   . GLN   A 68  ? 0.80306 1.21267 0.73376 0.01034  0.08324  0.09449  68  GLN   A O   
530  C CB  . GLN   A 68  ? 0.39293 0.81490 0.32301 0.02725  0.10821  0.04288  68  GLN   A CB  
531  C CG  . GLN   A 68  ? 0.52719 0.96392 0.44939 0.03750  0.12127  0.01379  68  GLN   A CG  
532  C CD  . GLN   A 68  ? 0.55946 0.98180 0.47297 0.03703  0.12386  -0.01722 68  GLN   A CD  
533  O OE1 . GLN   A 68  ? 0.68478 1.08552 0.60263 0.03044  0.11898  -0.01676 68  GLN   A OE1 
534  N NE2 . GLN   A 68  ? 0.95075 1.38426 0.85255 0.04293  0.13156  -0.04587 68  GLN   A NE2 
535  N N   . TYR   A 69  ? 0.48859 0.89123 0.45344 0.01003  0.08915  0.11182  69  TYR   A N   
536  C CA  . TYR   A 69  ? 0.45899 0.84187 0.42790 -0.00006 0.07629  0.13228  69  TYR   A CA  
537  C C   . TYR   A 69  ? 0.44398 0.84242 0.41813 -0.00512 0.07847  0.14809  69  TYR   A C   
538  O O   . TYR   A 69  ? 0.50067 0.91399 0.49047 -0.00437 0.08530  0.15055  69  TYR   A O   
539  C CB  . TYR   A 69  ? 0.49523 0.85107 0.48199 -0.00261 0.06986  0.13786  69  TYR   A CB  
540  C CG  . TYR   A 69  ? 0.44341 0.77815 0.42411 -0.00039 0.06650  0.12703  69  TYR   A CG  
541  C CD1 . TYR   A 69  ? 0.46176 0.78260 0.42856 -0.00462 0.05607  0.12771  69  TYR   A CD1 
542  C CD2 . TYR   A 69  ? 0.37472 0.70393 0.36496 0.00698  0.07497  0.11603  69  TYR   A CD2 
543  C CE1 . TYR   A 69  ? 0.42786 0.73284 0.38958 -0.00413 0.05336  0.11765  69  TYR   A CE1 
544  C CE2 . TYR   A 69  ? 0.34611 0.65578 0.33156 0.00761  0.07435  0.10662  69  TYR   A CE2 
545  C CZ  . TYR   A 69  ? 0.35375 0.65286 0.32438 0.00056  0.06313  0.10747  69  TYR   A CZ  
546  O OH  . TYR   A 69  ? 0.38431 0.65931 0.35332 -0.00014 0.05959  0.09439  69  TYR   A OH  
547  N N   . ALA   A 70  ? 0.50316 0.89882 0.46459 -0.00971 0.07373  0.15855  70  ALA   A N   
548  C CA  . ALA   A 70  ? 0.63001 1.03627 0.59380 -0.01592 0.07773  0.17466  70  ALA   A CA  
549  C C   . ALA   A 70  ? 0.62408 1.00315 0.60168 -0.02714 0.07043  0.18980  70  ALA   A C   
550  O O   . ALA   A 70  ? 0.67997 1.06816 0.66989 -0.03471 0.07538  0.20000  70  ALA   A O   
551  C CB  . ALA   A 70  ? 0.65033 1.06684 0.59124 -0.01315 0.07913  0.17850  70  ALA   A CB  
552  N N   . TYR   A 71  ? 0.45199 0.79879 0.42759 -0.02863 0.05919  0.18974  71  TYR   A N   
553  C CA  . TYR   A 71  ? 0.56126 0.87857 0.54747 -0.03798 0.05167  0.19982  71  TYR   A CA  
554  C C   . TYR   A 71  ? 0.47515 0.77334 0.47498 -0.03673 0.04277  0.19209  71  TYR   A C   
555  O O   . TYR   A 71  ? 0.49209 0.78943 0.48716 -0.02901 0.04110  0.18063  71  TYR   A O   
556  C CB  . TYR   A 71  ? 0.63203 0.92354 0.60093 -0.03909 0.04690  0.20675  71  TYR   A CB  
557  C CG  . TYR   A 71  ? 0.74497 1.04961 0.69826 -0.04004 0.05597  0.21810  71  TYR   A CG  
558  C CD1 . TYR   A 71  ? 0.85272 1.15508 0.81138 -0.05084 0.06273  0.23224  71  TYR   A CD1 
559  C CD2 . TYR   A 71  ? 0.78523 1.10536 0.71773 -0.03045 0.05819  0.21481  71  TYR   A CD2 
560  C CE1 . TYR   A 71  ? 0.83818 1.15036 0.78102 -0.05182 0.07270  0.24430  71  TYR   A CE1 
561  C CE2 . TYR   A 71  ? 0.84426 1.17693 0.76085 -0.02975 0.06670  0.22636  71  TYR   A CE2 
562  C CZ  . TYR   A 71  ? 0.84663 1.17368 0.76788 -0.04033 0.07449  0.24188  71  TYR   A CZ  
563  O OH  . TYR   A 71  ? 1.06352 1.40119 0.96740 -0.03984 0.08457  0.25498  71  TYR   A OH  
564  N N   . PRO   A 72  ? 0.48448 0.76794 0.50050 -0.04449 0.03756  0.19788  72  PRO   A N   
565  C CA  . PRO   A 72  ? 0.43933 0.70340 0.46652 -0.04206 0.02826  0.19129  72  PRO   A CA  
566  C C   . PRO   A 72  ? 0.43787 0.67068 0.45296 -0.03863 0.01946  0.18506  72  PRO   A C   
567  O O   . PRO   A 72  ? 0.42839 0.64856 0.44848 -0.03389 0.01407  0.17673  72  PRO   A O   
568  C CB  . PRO   A 72  ? 0.42342 0.68282 0.46805 -0.05227 0.02446  0.19931  72  PRO   A CB  
569  C CG  . PRO   A 72  ? 0.43894 0.70105 0.47697 -0.06203 0.03052  0.21022  72  PRO   A CG  
570  C CD  . PRO   A 72  ? 0.46077 0.74890 0.48636 -0.05620 0.04109  0.20986  72  PRO   A CD  
571  N N   . SER   A 73  ? 0.42618 0.64648 0.42484 -0.03984 0.01903  0.18896  73  SER   A N   
572  C CA  . SER   A 73  ? 0.42750 0.62171 0.41383 -0.03487 0.01187  0.18201  73  SER   A CA  
573  C C   . SER   A 73  ? 0.37284 0.58079 0.35015 -0.02685 0.01278  0.17185  73  SER   A C   
574  O O   . SER   A 73  ? 0.43553 0.62612 0.40816 -0.02305 0.00661  0.16363  73  SER   A O   
575  C CB  . SER   A 73  ? 0.51827 0.69619 0.48687 -0.03600 0.01265  0.19034  73  SER   A CB  
576  O OG  . SER   A 73  ? 0.53755 0.73976 0.49248 -0.03315 0.02029  0.19563  73  SER   A OG  
577  N N   . GLU   A 74  ? 0.43880 0.67881 0.41251 -0.02450 0.02113  0.17106  74  GLU   A N   
578  C CA  . GLU   A 74  ? 0.49804 0.75444 0.46086 -0.01809 0.02328  0.15933  74  GLU   A CA  
579  C C   . GLU   A 74  ? 0.43793 0.68722 0.41040 -0.01629 0.02268  0.15034  74  GLU   A C   
580  O O   . GLU   A 74  ? 0.45579 0.70369 0.41954 -0.01350 0.02102  0.14021  74  GLU   A O   
581  C CB  . GLU   A 74  ? 0.50670 0.79934 0.46051 -0.01530 0.03398  0.15774  74  GLU   A CB  
582  C CG  . GLU   A 74  ? 0.46505 0.76629 0.40622 -0.01556 0.03600  0.16790  74  GLU   A CG  
583  C CD  . GLU   A 74  ? 0.71194 1.05021 0.64481 -0.01202 0.04688  0.16554  74  GLU   A CD  
584  O OE1 . GLU   A 74  ? 0.67745 1.03356 0.61504 -0.00922 0.05360  0.15428  74  GLU   A OE1 
585  O OE2 . GLU   A 74  ? 1.00494 1.35304 0.92533 -0.01090 0.04977  0.17433  74  GLU   A OE2 
586  N N   . PHE   A 75  ? 0.38434 0.63083 0.37409 -0.01766 0.02469  0.15435  75  PHE   A N   
587  C CA  . PHE   A 75  ? 0.35750 0.59309 0.35626 -0.01392 0.02518  0.14863  75  PHE   A CA  
588  C C   . PHE   A 75  ? 0.43611 0.63932 0.43645 -0.01473 0.01388  0.14582  75  PHE   A C   
589  O O   . PHE   A 75  ? 0.36035 0.55426 0.35676 -0.01168 0.01406  0.13863  75  PHE   A O   
590  C CB  . PHE   A 75  ? 0.30569 0.54864 0.32387 -0.01310 0.02893  0.15503  75  PHE   A CB  
591  C CG  . PHE   A 75  ? 0.27403 0.50060 0.30374 -0.00739 0.02801  0.15318  75  PHE   A CG  
592  C CD1 . PHE   A 75  ? 0.31930 0.55128 0.34722 0.00120  0.04058  0.14594  75  PHE   A CD1 
593  C CD2 . PHE   A 75  ? 0.29940 0.50543 0.34197 -0.00959 0.01691  0.15706  75  PHE   A CD2 
594  C CE1 . PHE   A 75  ? 0.27046 0.48365 0.30868 0.00880  0.04180  0.14659  75  PHE   A CE1 
595  C CE2 . PHE   A 75  ? 0.28196 0.47366 0.33412 -0.00237 0.01601  0.15586  75  PHE   A CE2 
596  C CZ  . PHE   A 75  ? 0.34114 0.53450 0.39019 0.00759  0.02810  0.15342  75  PHE   A CZ  
597  N N   . VAL   A 76  ? 0.32654 0.51210 0.33119 -0.01897 0.00593  0.14995  76  VAL   A N   
598  C CA  . VAL   A 76  ? 0.34700 0.50226 0.35184 -0.01848 -0.00256 0.14341  76  VAL   A CA  
599  C C   . VAL   A 76  ? 0.37198 0.52509 0.36102 -0.01587 -0.00430 0.13683  76  VAL   A C   
600  O O   . VAL   A 76  ? 0.39252 0.52976 0.38113 -0.01373 -0.00808 0.12916  76  VAL   A O   
601  C CB  . VAL   A 76  ? 0.36922 0.50752 0.37710 -0.02307 -0.00759 0.14746  76  VAL   A CB  
602  C CG1 . VAL   A 76  ? 0.34546 0.45356 0.34970 -0.02073 -0.01410 0.13785  76  VAL   A CG1 
603  C CG2 . VAL   A 76  ? 0.29441 0.44280 0.31982 -0.02731 -0.00697 0.15478  76  VAL   A CG2 
604  N N   . LYS   A 77  ? 0.39351 0.56589 0.36935 -0.01564 -0.00143 0.13981  77  LYS   A N   
605  C CA  . LYS   A 77  ? 0.42032 0.59838 0.38158 -0.01249 -0.00397 0.13364  77  LYS   A CA  
606  C C   . LYS   A 77  ? 0.42400 0.61686 0.38241 -0.01197 -0.00170 0.12441  77  LYS   A C   
607  O O   . LYS   A 77  ? 0.47859 0.66797 0.43237 -0.01121 -0.00629 0.11737  77  LYS   A O   
608  C CB  . LYS   A 77  ? 0.53322 0.73354 0.48014 -0.01072 -0.00085 0.13834  77  LYS   A CB  
609  C CG  . LYS   A 77  ? 0.61100 0.79098 0.54920 -0.00862 -0.00488 0.14469  77  LYS   A CG  
610  C CD  . LYS   A 77  ? 0.62602 0.82793 0.54815 -0.00521 -0.00097 0.15133  77  LYS   A CD  
611  C CE  . LYS   A 77  ? 0.76957 1.00458 0.68122 -0.00026 -0.00092 0.14120  77  LYS   A CE  
612  N NZ  . LYS   A 77  ? 0.61912 0.88763 0.53094 -0.00187 0.00645  0.13573  77  LYS   A NZ  
613  N N   . ASP   A 78  ? 0.35663 0.56677 0.31604 -0.01255 0.00704  0.12348  78  ASP   A N   
614  C CA  . ASP   A 78  ? 0.47363 0.69440 0.42611 -0.01332 0.01385  0.11242  78  ASP   A CA  
615  C C   . ASP   A 78  ? 0.47885 0.66960 0.44244 -0.01352 0.01107  0.11436  78  ASP   A C   
616  O O   . ASP   A 78  ? 0.41958 0.60503 0.38145 -0.01578 0.01146  0.10156  78  ASP   A O   
617  C CB  . ASP   A 78  ? 0.35319 0.59614 0.30448 -0.01193 0.02972  0.10671  78  ASP   A CB  
618  C CG  . ASP   A 78  ? 0.48284 0.76075 0.41776 -0.01118 0.03441  0.09492  78  ASP   A CG  
619  O OD1 . ASP   A 78  ? 0.53070 0.81673 0.45542 -0.01133 0.02474  0.09422  78  ASP   A OD1 
620  O OD2 . ASP   A 78  ? 0.45962 0.75362 0.39565 -0.00811 0.04695  0.08358  78  ASP   A OD2 
621  N N   . VAL   A 79  ? 0.40188 0.56912 0.38246 -0.01100 0.00756  0.12254  79  VAL   A N   
622  C CA  . VAL   A 79  ? 0.40021 0.53781 0.39163 -0.00877 0.00366  0.12186  79  VAL   A CA  
623  C C   . VAL   A 79  ? 0.31342 0.43654 0.30183 -0.00993 -0.00621 0.11598  79  VAL   A C   
624  O O   . VAL   A 79  ? 0.33941 0.45174 0.32755 -0.00990 -0.00707 0.11252  79  VAL   A O   
625  C CB  . VAL   A 79  ? 0.28393 0.40832 0.29224 -0.00568 0.00183  0.12598  79  VAL   A CB  
626  C CG1 . VAL   A 79  ? 0.27826 0.37462 0.29456 -0.00202 -0.00196 0.12057  79  VAL   A CG1 
627  C CG2 . VAL   A 79  ? 0.25650 0.39963 0.26966 -0.00207 0.01316  0.13280  79  VAL   A CG2 
628  N N   . GLN   A 80  ? 0.33416 0.45632 0.31938 -0.01048 -0.01129 0.11568  80  GLN   A N   
629  C CA  . GLN   A 80  ? 0.38355 0.49132 0.36368 -0.00898 -0.01735 0.10981  80  GLN   A CA  
630  C C   . GLN   A 80  ? 0.30911 0.43846 0.27918 -0.00984 -0.01841 0.10629  80  GLN   A C   
631  O O   . GLN   A 80  ? 0.43580 0.55715 0.40505 -0.00851 -0.02242 0.10133  80  GLN   A O   
632  C CB  . GLN   A 80  ? 0.35154 0.45092 0.32567 -0.00787 -0.01974 0.11225  80  GLN   A CB  
633  C CG  . GLN   A 80  ? 0.46525 0.55443 0.43658 -0.00506 -0.02478 0.11070  80  GLN   A CG  
634  C CD  . GLN   A 80  ? 0.39257 0.46572 0.37533 -0.00511 -0.02671 0.10708  80  GLN   A CD  
635  O OE1 . GLN   A 80  ? 0.41581 0.48217 0.40926 -0.00734 -0.02630 0.10874  80  GLN   A OE1 
636  N NE2 . GLN   A 80  ? 0.43204 0.50211 0.41209 -0.00246 -0.02889 0.10196  80  GLN   A NE2 
637  N N   . LEU   A 81  ? 0.38700 0.54854 0.34767 -0.01231 -0.01434 0.10622  81  LEU   A N   
638  C CA  . LEU   A 81  ? 0.43032 0.62206 0.37871 -0.01526 -0.01531 0.09620  81  LEU   A CA  
639  C C   . LEU   A 81  ? 0.37860 0.56697 0.32834 -0.02133 -0.01338 0.09043  81  LEU   A C   
640  O O   . LEU   A 81  ? 0.40986 0.60893 0.35954 -0.02467 -0.01719 0.07836  81  LEU   A O   
641  C CB  . LEU   A 81  ? 0.35947 0.58768 0.29420 -0.01731 -0.00878 0.08890  81  LEU   A CB  
642  C CG  . LEU   A 81  ? 0.40778 0.67372 0.32911 -0.02270 -0.00820 0.06659  81  LEU   A CG  
643  C CD1 . LEU   A 81  ? 0.38082 0.65532 0.30361 -0.01780 -0.01802 0.06490  81  LEU   A CD1 
644  C CD2 . LEU   A 81  ? 0.37131 0.66455 0.28421 -0.02305 0.00081  0.05272  81  LEU   A CD2 
645  N N   . ILE   A 82  ? 0.36438 0.52591 0.32842 -0.02154 -0.00448 0.08945  82  ILE   A N   
646  C CA  . ILE   A 82  ? 0.27610 0.41274 0.25405 -0.02505 0.00191  0.07705  82  ILE   A CA  
647  C C   . ILE   A 82  ? 0.31252 0.43693 0.29175 -0.02312 -0.00789 0.08785  82  ILE   A C   
648  O O   . ILE   A 82  ? 0.40190 0.52629 0.38618 -0.02884 -0.00647 0.07533  82  ILE   A O   
649  C CB  . ILE   A 82  ? 0.33939 0.44860 0.32911 -0.02041 0.01241  0.07963  82  ILE   A CB  
650  C CG1 . ILE   A 82  ? 0.40277 0.52622 0.39090 -0.02038 0.02302  0.06738  82  ILE   A CG1 
651  C CG2 . ILE   A 82  ? 0.30267 0.38148 0.30368 -0.02220 0.02066  0.07045  82  ILE   A CG2 
652  C CD1 . ILE   A 82  ? 0.31283 0.41566 0.31150 -0.01208 0.03277  0.07154  82  ILE   A CD1 
653  N N   . PHE   A 83  ? 0.42164 0.53169 0.40164 -0.01510 -0.01615 0.10269  83  PHE   A N   
654  C CA  . PHE   A 83  ? 0.25324 0.34259 0.23941 -0.01074 -0.02128 0.09796  83  PHE   A CA  
655  C C   . PHE   A 83  ? 0.44848 0.55598 0.42707 -0.01061 -0.02700 0.09313  83  PHE   A C   
656  O O   . PHE   A 83  ? 0.39031 0.49241 0.37094 -0.00904 -0.02946 0.09001  83  PHE   A O   
657  C CB  . PHE   A 83  ? 0.25867 0.32093 0.24886 -0.00458 -0.02181 0.09320  83  PHE   A CB  
658  C CG  . PHE   A 83  ? 0.33290 0.38459 0.33085 -0.00317 -0.01727 0.09527  83  PHE   A CG  
659  C CD1 . PHE   A 83  ? 0.36038 0.40605 0.36344 -0.00271 -0.01142 0.09915  83  PHE   A CD1 
660  C CD2 . PHE   A 83  ? 0.37929 0.42747 0.37965 -0.00218 -0.01770 0.09495  83  PHE   A CD2 
661  C CE1 . PHE   A 83  ? 0.32456 0.35995 0.33423 0.00171  -0.00626 0.10074  83  PHE   A CE1 
662  C CE2 . PHE   A 83  ? 0.38153 0.42622 0.38978 -0.00013 -0.01425 0.09715  83  PHE   A CE2 
663  C CZ  . PHE   A 83  ? 0.28099 0.31971 0.29361 0.00314  -0.00880 0.09958  83  PHE   A CZ  
664  N N   . ASP   A 84  ? 0.37590 0.50561 0.34556 -0.01068 -0.02815 0.09199  84  ASP   A N   
665  C CA  . ASP   A 84  ? 0.32899 0.47659 0.29134 -0.00784 -0.03246 0.08639  84  ASP   A CA  
666  C C   . ASP   A 84  ? 0.42213 0.61018 0.38213 -0.01614 -0.03412 0.07682  84  ASP   A C   
667  O O   . ASP   A 84  ? 0.39381 0.59263 0.35519 -0.01452 -0.03754 0.07087  84  ASP   A O   
668  C CB  . ASP   A 84  ? 0.34734 0.50425 0.30024 -0.00384 -0.03236 0.08819  84  ASP   A CB  
669  C CG  . ASP   A 84  ? 0.54214 0.66297 0.49373 0.00150  -0.03238 0.09363  84  ASP   A CG  
670  O OD1 . ASP   A 84  ? 0.46160 0.55985 0.42134 0.00211  -0.03267 0.09437  84  ASP   A OD1 
671  O OD2 . ASP   A 84  ? 0.59730 0.72233 0.54099 0.00353  -0.03172 0.09842  84  ASP   A OD2 
672  N N   . ASN   A 85  ? 0.30655 0.51857 0.26098 -0.02685 -0.03081 0.06979  85  ASN   A N   
673  C CA  . ASN   A 85  ? 0.35478 0.58366 0.32028 -0.03941 -0.02454 0.04211  85  ASN   A CA  
674  C C   . ASN   A 85  ? 0.27537 0.47816 0.25706 -0.04434 -0.02040 0.04081  85  ASN   A C   
675  O O   . ASN   A 85  ? 0.37156 0.59369 0.36180 -0.05356 -0.01959 0.02434  85  ASN   A O   
676  C CB  . ASN   A 85  ? 0.32635 0.55382 0.29647 -0.04845 -0.01137 0.02174  85  ASN   A CB  
677  C CG  . ASN   A 85  ? 0.38982 0.65181 0.34296 -0.04425 -0.01434 0.01917  85  ASN   A CG  
678  O OD1 . ASN   A 85  ? 0.45834 0.75361 0.39657 -0.03729 -0.02561 0.02601  85  ASN   A OD1 
679  N ND2 . ASN   A 85  ? 0.39055 0.64550 0.34436 -0.04647 -0.00350 0.00998  85  ASN   A ND2 
680  N N   . CYS   A 86  ? 0.30341 0.46592 0.28954 -0.03832 -0.01754 0.05798  86  CYS   A N   
681  C CA  . CYS   A 86  ? 0.26641 0.40373 0.26465 -0.04012 -0.01318 0.06032  86  CYS   A CA  
682  C C   . CYS   A 86  ? 0.33969 0.49312 0.33351 -0.03349 -0.02557 0.06984  86  CYS   A C   
683  O O   . CYS   A 86  ? 0.33614 0.49641 0.34008 -0.04016 -0.02231 0.06076  86  CYS   A O   
684  C CB  . CYS   A 86  ? 0.25508 0.35114 0.25625 -0.03191 -0.00871 0.07691  86  CYS   A CB  
685  S SG  . CYS   A 86  ? 0.41850 0.48153 0.43113 -0.03122 -0.00103 0.08198  86  CYS   A SG  
686  N N   . SER   A 87  ? 0.35533 0.50806 0.33748 -0.02005 -0.03581 0.08372  87  SER   A N   
687  C CA  . SER   A 87  ? 0.36115 0.50512 0.34420 -0.01051 -0.03800 0.07994  87  SER   A CA  
688  C C   . SER   A 87  ? 0.37888 0.56551 0.35915 -0.01279 -0.04169 0.06954  87  SER   A C   
689  O O   . SER   A 87  ? 0.50672 0.69451 0.48830 -0.00686 -0.04325 0.06736  87  SER   A O   
690  C CB  . SER   A 87  ? 0.29844 0.40533 0.27425 0.00110  -0.03789 0.07870  87  SER   A CB  
691  O OG  . SER   A 87  ? 0.48154 0.60156 0.44940 0.00217  -0.03926 0.07840  87  SER   A OG  
692  N N   . LEU   A 88  ? 0.35912 0.58152 0.33556 -0.02078 -0.04226 0.05946  88  LEU   A N   
693  C CA  . LEU   A 88  ? 0.31140 0.57625 0.28749 -0.02291 -0.04387 0.04332  88  LEU   A CA  
694  C C   . LEU   A 88  ? 0.38534 0.68631 0.37628 -0.04195 -0.04301 0.02330  88  LEU   A C   
695  O O   . LEU   A 88  ? 0.41644 0.73382 0.41314 -0.04024 -0.04341 0.01809  88  LEU   A O   
696  C CB  . LEU   A 88  ? 0.35315 0.63972 0.32049 -0.02334 -0.04302 0.03545  88  LEU   A CB  
697  C CG  . LEU   A 88  ? 0.33510 0.66803 0.30297 -0.02504 -0.04356 0.01670  88  LEU   A CG  
698  C CD1 . LEU   A 88  ? 0.29634 0.62638 0.26225 -0.00968 -0.04666 0.02500  88  LEU   A CD1 
699  C CD2 . LEU   A 88  ? 0.44369 0.79725 0.40238 -0.02379 -0.04223 0.01009  88  LEU   A CD2 
700  N N   . TYR   A 89  ? 0.32955 0.62159 0.33222 -0.05987 -0.03306 0.00802  89  TYR   A N   
701  C CA  . TYR   A 89  ? 0.47264 0.77570 0.49641 -0.08126 -0.02180 -0.01836 89  TYR   A CA  
702  C C   . TYR   A 89  ? 0.38467 0.66254 0.42237 -0.08411 -0.01541 -0.00992 89  TYR   A C   
703  O O   . TYR   A 89  ? 0.44404 0.74696 0.49782 -0.09815 -0.01107 -0.02610 89  TYR   A O   
704  C CB  . TYR   A 89  ? 0.35722 0.63631 0.38786 -0.09639 -0.00652 -0.03725 89  TYR   A CB  
705  C CG  . TYR   A 89  ? 0.47400 0.75660 0.52636 -0.12142 0.00745  -0.06615 89  TYR   A CG  
706  C CD1 . TYR   A 89  ? 0.48068 0.81493 0.53896 -0.13634 0.00514  -0.09649 89  TYR   A CD1 
707  C CD2 . TYR   A 89  ? 0.48046 0.71507 0.54704 -0.13053 0.02353  -0.06324 89  TYR   A CD2 
708  C CE1 . TYR   A 89  ? 0.56448 0.90120 0.64476 -0.16285 0.01871  -0.12507 89  TYR   A CE1 
709  C CE2 . TYR   A 89  ? 0.55420 0.78687 0.64079 -0.15559 0.03861  -0.08862 89  TYR   A CE2 
710  C CZ  . TYR   A 89  ? 0.61983 0.90294 0.71443 -0.17326 0.03627  -0.12043 89  TYR   A CZ  
711  O OH  . TYR   A 89  ? 0.78876 1.06255 0.90040 -0.19657 0.05162  -0.14510 89  TYR   A OH  
712  N N   . ASN   A 90  ? 0.33979 0.57204 0.37205 -0.07153 -0.01439 0.01440  90  ASN   A N   
713  C CA  . ASN   A 90  ? 0.41364 0.61758 0.45665 -0.07279 -0.00619 0.02333  90  ASN   A CA  
714  C C   . ASN   A 90  ? 0.37783 0.59829 0.41376 -0.05644 -0.01960 0.04035  90  ASN   A C   
715  O O   . ASN   A 90  ? 0.36194 0.58687 0.38049 -0.03864 -0.03404 0.05576  90  ASN   A O   
716  C CB  . ASN   A 90  ? 0.40146 0.54891 0.44213 -0.06678 0.00289  0.03832  90  ASN   A CB  
717  C CG  . ASN   A 90  ? 0.40124 0.52932 0.44658 -0.07851 0.01639  0.02283  90  ASN   A CG  
718  O OD1 . ASN   A 90  ? 0.50260 0.61727 0.56178 -0.09530 0.03247  0.00646  90  ASN   A OD1 
719  N ND2 . ASN   A 90  ? 0.30443 0.42965 0.33807 -0.06980 0.01104  0.02785  90  ASN   A ND2 
720  N N   . THR   A 91  ? 0.33151 0.55926 0.38065 -0.06263 -0.01344 0.03748  91  THR   A N   
721  C CA  . THR   A 91  ? 0.24833 0.49067 0.29163 -0.04613 -0.02408 0.05227  91  THR   A CA  
722  C C   . THR   A 91  ? 0.21596 0.41239 0.24563 -0.02745 -0.02800 0.07737  91  THR   A C   
723  O O   . THR   A 91  ? 0.31026 0.46469 0.34147 -0.03010 -0.01817 0.08294  91  THR   A O   
724  C CB  . THR   A 91  ? 0.18924 0.45061 0.25180 -0.05880 -0.01353 0.04300  91  THR   A CB  
725  O OG1 . THR   A 91  ? 0.46233 0.67930 0.53563 -0.07155 0.00580  0.04374  91  THR   A OG1 
726  C CG2 . THR   A 91  ? 0.22621 0.54370 0.30376 -0.07734 -0.01270 0.01614  91  THR   A CG2 
727  N N   . SER   A 92  ? 0.43430 0.62688 0.45084 -0.00820 -0.03691 0.08526  92  SER   A N   
728  C CA  . SER   A 92  ? 0.40315 0.53577 0.40965 0.00524  -0.03381 0.08614  92  SER   A CA  
729  C C   . SER   A 92  ? 0.40206 0.51209 0.41414 0.00630  -0.02742 0.09375  92  SER   A C   
730  O O   . SER   A 92  ? 0.39484 0.46377 0.39897 0.01194  -0.02527 0.08678  92  SER   A O   
731  C CB  . SER   A 92  ? 0.43089 0.54542 0.42447 0.01773  -0.03803 0.07571  92  SER   A CB  
732  O OG  . SER   A 92  ? 0.84263 0.98317 0.84081 0.02042  -0.03792 0.07654  92  SER   A OG  
733  N N   . ASN   A 93  ? 0.42216 0.56111 0.44520 0.00027  -0.02419 0.10566  93  ASN   A N   
734  C CA  . ASN   A 93  ? 0.32746 0.43851 0.35432 0.00271  -0.01389 0.11384  93  ASN   A CA  
735  C C   . ASN   A 93  ? 0.34192 0.43228 0.37940 -0.01446 0.00437  0.11595  93  ASN   A C   
736  O O   . ASN   A 93  ? 0.33513 0.40179 0.37605 -0.01427 0.01772  0.12340  93  ASN   A O   
737  C CB  . ASN   A 93  ? 0.29549 0.43340 0.32618 0.00672  -0.01256 0.11863  93  ASN   A CB  
738  C CG  . ASN   A 93  ? 0.25562 0.44170 0.30313 -0.01181 -0.00688 0.10508  93  ASN   A CG  
739  O OD1 . ASN   A 93  ? 0.28179 0.47529 0.33927 -0.03021 -0.00135 0.08944  93  ASN   A OD1 
740  N ND2 . ASN   A 93  ? 0.27379 0.49327 0.32672 -0.00784 -0.00697 0.10478  93  ASN   A ND2 
741  N N   . SER   A 94  ? 0.33200 0.42551 0.37515 -0.02855 0.00766  0.10177  94  SER   A N   
742  C CA  . SER   A 94  ? 0.29427 0.35945 0.34830 -0.04455 0.02732  0.09329  94  SER   A CA  
743  C C   . SER   A 94  ? 0.31729 0.33813 0.36149 -0.03160 0.02933  0.10779  94  SER   A C   
744  O O   . SER   A 94  ? 0.35627 0.37436 0.38652 -0.01430 0.01281  0.10880  94  SER   A O   
745  C CB  . SER   A 94  ? 0.38498 0.47204 0.44757 -0.06327 0.02965  0.06993  94  SER   A CB  
746  O OG  . SER   A 94  ? 0.38468 0.47653 0.43477 -0.05386 0.01590  0.07184  94  SER   A OG  
747  N N   . VAL   A 95  ? 0.33148 0.31756 0.37881 -0.03703 0.04676  0.10199  95  VAL   A N   
748  C CA  . VAL   A 95  ? 0.42287 0.37721 0.45499 -0.02118 0.04317  0.09971  95  VAL   A CA  
749  C C   . VAL   A 95  ? 0.46859 0.42527 0.49920 -0.02068 0.03750  0.09750  95  VAL   A C   
750  O O   . VAL   A 95  ? 0.43367 0.38701 0.45259 -0.00642 0.02569  0.09498  95  VAL   A O   
751  C CB  . VAL   A 95  ? 0.51276 0.43757 0.54686 -0.02608 0.05986  0.09590  95  VAL   A CB  
752  C CG1 . VAL   A 95  ? 0.40882 0.31585 0.43348 -0.01163 0.05593  0.09471  95  VAL   A CG1 
753  C CG2 . VAL   A 95  ? 0.39046 0.31427 0.42331 -0.02311 0.06374  0.10080  95  VAL   A CG2 
754  N N   . VAL   A 96  ? 0.36069 0.33051 0.40660 -0.04027 0.04710  0.09367  96  VAL   A N   
755  C CA  . VAL   A 96  ? 0.35401 0.33039 0.39556 -0.03938 0.04110  0.08710  96  VAL   A CA  
756  C C   . VAL   A 96  ? 0.44848 0.44961 0.47870 -0.02732 0.01945  0.09792  96  VAL   A C   
757  O O   . VAL   A 96  ? 0.36258 0.35689 0.38497 -0.01666 0.01262  0.10044  96  VAL   A O   
758  C CB  . VAL   A 96  ? 0.42592 0.42103 0.47589 -0.05989 0.04852  0.06076  96  VAL   A CB  
759  C CG1 . VAL   A 96  ? 0.49293 0.49866 0.53618 -0.05726 0.04259  0.05457  96  VAL   A CG1 
760  C CG2 . VAL   A 96  ? 0.44843 0.41040 0.50943 -0.07340 0.07187  0.04935  96  VAL   A CG2 
761  N N   . ALA   A 97  ? 0.37643 0.40669 0.40442 -0.02752 0.00842  0.09800  97  ALA   A N   
762  C CA  . ALA   A 97  ? 0.33651 0.38388 0.35242 -0.01479 -0.01042 0.10418  97  ALA   A CA  
763  C C   . ALA   A 97  ? 0.36165 0.38122 0.37071 0.00034  -0.01230 0.09075  97  ALA   A C   
764  O O   . ALA   A 97  ? 0.35527 0.37045 0.35663 0.00482  -0.01697 0.08221  97  ALA   A O   
765  C CB  . ALA   A 97  ? 0.34844 0.43107 0.36183 -0.01545 -0.01990 0.10519  97  ALA   A CB  
766  N N   . ILE   A 98  ? 0.34670 0.34982 0.35495 0.00408  -0.00701 0.08893  98  ILE   A N   
767  C CA  . ILE   A 98  ? 0.26740 0.26293 0.27482 0.01176  -0.00879 0.08399  98  ILE   A CA  
768  C C   . ILE   A 98  ? 0.31459 0.30136 0.32339 0.01298  -0.00627 0.08343  98  ILE   A C   
769  O O   . ILE   A 98  ? 0.38132 0.37353 0.39232 0.01522  -0.01029 0.08210  98  ILE   A O   
770  C CB  . ILE   A 98  ? 0.30944 0.29841 0.31805 0.01527  -0.00396 0.08641  98  ILE   A CB  
771  C CG1 . ILE   A 98  ? 0.30912 0.31021 0.31683 0.01490  -0.00667 0.08770  98  ILE   A CG1 
772  C CG2 . ILE   A 98  ? 0.38762 0.37538 0.39714 0.02187  -0.00515 0.08551  98  ILE   A CG2 
773  C CD1 . ILE   A 98  ? 0.24653 0.24223 0.25521 0.01732  -0.00029 0.09184  98  ILE   A CD1 
774  N N   . THR   A 99  ? 0.36544 0.33590 0.37166 0.01017  0.00171  0.08466  99  THR   A N   
775  C CA  . THR   A 99  ? 0.28457 0.24756 0.29202 0.01262  0.00462  0.08463  99  THR   A CA  
776  C C   . THR   A 99  ? 0.40994 0.38470 0.41662 0.01069  -0.00099 0.08360  99  THR   A C   
777  O O   . THR   A 99  ? 0.39813 0.37843 0.40920 0.01419  -0.00301 0.08397  99  THR   A O   
778  C CB  . THR   A 99  ? 0.47153 0.41345 0.47957 0.00815  0.01714  0.08689  99  THR   A CB  
779  O OG1 . THR   A 99  ? 0.47351 0.40327 0.48087 0.00971  0.02261  0.08717  99  THR   A OG1 
780  C CG2 . THR   A 99  ? 0.37133 0.30670 0.38125 0.01303  0.02053  0.08712  99  THR   A CG2 
781  N N   . GLY   A 100 ? 0.28360 0.26864 0.28923 0.00445  -0.00262 0.08615  100 GLY   A N   
782  C CA  . GLY   A 100 ? 0.27565 0.27615 0.28061 0.00278  -0.00797 0.08711  100 GLY   A CA  
783  C C   . GLY   A 100 ? 0.38971 0.39843 0.39621 0.00582  -0.01512 0.08299  100 GLY   A C   
784  O O   . GLY   A 100 ? 0.32718 0.34095 0.33629 0.00549  -0.01644 0.08428  100 GLY   A O   
785  N N   . LYS   A 101 ? 0.25427 0.26594 0.26231 0.00700  -0.01817 0.08180  101 LYS   A N   
786  C CA  . LYS   A 101 ? 0.28417 0.29898 0.29402 0.00774  -0.02254 0.08150  101 LYS   A CA  
787  C C   . LYS   A 101 ? 0.34611 0.35532 0.36062 0.00994  -0.02150 0.08182  101 LYS   A C   
788  O O   . LYS   A 101 ? 0.34753 0.35866 0.36367 0.00844  -0.02479 0.08294  101 LYS   A O   
789  C CB  . LYS   A 101 ? 0.30576 0.32050 0.31183 0.00997  -0.02507 0.08014  101 LYS   A CB  
790  C CG  . LYS   A 101 ? 0.35917 0.38359 0.35988 0.00917  -0.02748 0.08037  101 LYS   A CG  
791  C CD  . LYS   A 101 ? 0.47690 0.50564 0.47290 0.00874  -0.03109 0.08197  101 LYS   A CD  
792  C CE  . LYS   A 101 ? 0.66608 0.70792 0.65490 0.00982  -0.03357 0.08220  101 LYS   A CE  
793  N NZ  . LYS   A 101 ? 1.07023 1.11479 1.05632 0.01405  -0.03524 0.08066  101 LYS   A NZ  
794  N N   . ASN   A 102 ? 0.32799 0.32996 0.34373 0.01369  -0.01696 0.08180  102 ASN   A N   
795  C CA  . ASN   A 102 ? 0.28370 0.28265 0.30207 0.01733  -0.01626 0.08281  102 ASN   A CA  
796  C C   . ASN   A 102 ? 0.30911 0.31218 0.33197 0.01646  -0.01526 0.08515  102 ASN   A C   
797  O O   . ASN   A 102 ? 0.30382 0.31083 0.33010 0.01643  -0.01804 0.08673  102 ASN   A O   
798  C CB  . ASN   A 102 ? 0.28839 0.27843 0.30542 0.02305  -0.01073 0.08371  102 ASN   A CB  
799  C CG  . ASN   A 102 ? 0.43785 0.42578 0.45087 0.02492  -0.01182 0.08273  102 ASN   A CG  
800  O OD1 . ASN   A 102 ? 0.41982 0.41091 0.42977 0.02347  -0.01730 0.08073  102 ASN   A OD1 
801  N ND2 . ASN   A 102 ? 0.37134 0.35241 0.38375 0.02887  -0.00579 0.08494  102 ASN   A ND2 
802  N N   . ILE   A 103 ? 0.34286 0.34423 0.36467 0.01586  -0.01134 0.08588  103 ILE   A N   
803  C CA  . ILE   A 103 ? 0.29476 0.30045 0.31939 0.01607  -0.00977 0.08866  103 ILE   A CA  
804  C C   . ILE   A 103 ? 0.31372 0.33198 0.34008 0.01003  -0.01482 0.09022  103 ILE   A C   
805  O O   . ILE   A 103 ? 0.29133 0.31735 0.32263 0.00915  -0.01527 0.09379  103 ILE   A O   
806  C CB  . ILE   A 103 ? 0.26640 0.26113 0.28528 0.01757  -0.00321 0.08901  103 ILE   A CB  
807  C CG1 . ILE   A 103 ? 0.45772 0.43571 0.47524 0.02241  0.00310  0.08842  103 ILE   A CG1 
808  C CG2 . ILE   A 103 ? 0.24717 0.24559 0.26791 0.01991  -0.00046 0.09241  103 ILE   A CG2 
809  C CD1 . ILE   A 103 ? 0.72023 0.68215 0.73617 0.02297  0.01319  0.09084  103 ILE   A CD1 
810  N N   . GLU   A 104 ? 0.24156 0.26233 0.26368 0.00623  -0.01825 0.08868  104 GLU   A N   
811  C CA  . GLU   A 104 ? 0.30182 0.33140 0.32375 0.00151  -0.02244 0.09133  104 GLU   A CA  
812  C C   . GLU   A 104 ? 0.37557 0.40481 0.40319 -0.00021 -0.02633 0.09324  104 GLU   A C   
813  O O   . GLU   A 104 ? 0.35055 0.38635 0.38213 -0.00376 -0.02785 0.09789  104 GLU   A O   
814  C CB  . GLU   A 104 ? 0.23800 0.26850 0.25241 0.00038  -0.02504 0.08980  104 GLU   A CB  
815  C CG  . GLU   A 104 ? 0.37103 0.40805 0.38121 -0.00238 -0.02807 0.09377  104 GLU   A CG  
816  C CD  . GLU   A 104 ? 0.47548 0.51221 0.47676 -0.00048 -0.03078 0.09278  104 GLU   A CD  
817  O OE1 . GLU   A 104 ? 0.54178 0.57164 0.54254 0.00211  -0.03192 0.08954  104 GLU   A OE1 
818  O OE2 . GLU   A 104 ? 0.62880 0.67338 0.62230 -0.00040 -0.03161 0.09562  104 GLU   A OE2 
819  N N   . THR   A 105 ? 0.31895 0.34034 0.34574 0.00212  -0.02817 0.09027  105 THR   A N   
820  C CA  . THR   A 105 ? 0.35906 0.37776 0.38852 0.00078  -0.03273 0.09167  105 THR   A CA  
821  C C   . THR   A 105 ? 0.32510 0.34998 0.36270 0.00121  -0.03142 0.09501  105 THR   A C   
822  O O   . THR   A 105 ? 0.42700 0.45631 0.46977 -0.00333 -0.03534 0.09925  105 THR   A O   
823  C CB  . THR   A 105 ? 0.36617 0.37506 0.38984 0.00526  -0.03437 0.08761  105 THR   A CB  
824  O OG1 . THR   A 105 ? 0.51359 0.51841 0.52958 0.00612  -0.03517 0.08527  105 THR   A OG1 
825  C CG2 . THR   A 105 ? 0.33372 0.33788 0.35728 0.00426  -0.04038 0.08871  105 THR   A CG2 
826  N N   . TYR   A 106 ? 0.34696 0.37154 0.38518 0.00719  -0.02594 0.09406  106 TYR   A N   
827  C CA  . TYR   A 106 ? 0.26117 0.29189 0.30542 0.01047  -0.02389 0.09785  106 TYR   A CA  
828  C C   . TYR   A 106 ? 0.25941 0.30240 0.30957 0.00583  -0.02332 0.10304  106 TYR   A C   
829  O O   . TYR   A 106 ? 0.27861 0.33100 0.33593 0.00398  -0.02547 0.10804  106 TYR   A O   
830  C CB  . TYR   A 106 ? 0.25993 0.28432 0.30107 0.01936  -0.01714 0.09657  106 TYR   A CB  
831  C CG  . TYR   A 106 ? 0.28623 0.31614 0.33175 0.02609  -0.01407 0.10075  106 TYR   A CG  
832  C CD1 . TYR   A 106 ? 0.32158 0.35388 0.36820 0.03109  -0.01711 0.10232  106 TYR   A CD1 
833  C CD2 . TYR   A 106 ? 0.27065 0.30336 0.31754 0.02915  -0.00851 0.10315  106 TYR   A CD2 
834  C CE1 . TYR   A 106 ? 0.28594 0.32609 0.33641 0.03933  -0.01488 0.10639  106 TYR   A CE1 
835  C CE2 . TYR   A 106 ? 0.36366 0.40250 0.41444 0.03761  -0.00539 0.10719  106 TYR   A CE2 
836  C CZ  . TYR   A 106 ? 0.34477 0.38867 0.39798 0.04287  -0.00866 0.10890  106 TYR   A CZ  
837  O OH  . TYR   A 106 ? 0.38358 0.43698 0.44092 0.05329  -0.00629 0.11280  106 TYR   A OH  
838  N N   . PHE   A 107 ? 0.30055 0.34480 0.34667 0.00403  -0.02076 0.10259  107 PHE   A N   
839  C CA  . PHE   A 107 ? 0.26627 0.32282 0.31464 0.00054  -0.01960 0.10805  107 PHE   A CA  
840  C C   . PHE   A 107 ? 0.32593 0.38872 0.37841 -0.00785 -0.02546 0.11284  107 PHE   A C   
841  O O   . PHE   A 107 ? 0.32943 0.40430 0.38865 -0.01112 -0.02573 0.11953  107 PHE   A O   
842  C CB  . PHE   A 107 ? 0.22412 0.27927 0.26262 0.00083  -0.01635 0.10623  107 PHE   A CB  
843  C CG  . PHE   A 107 ? 0.32626 0.39456 0.36237 -0.00286 -0.01498 0.11184  107 PHE   A CG  
844  C CD1 . PHE   A 107 ? 0.35182 0.43901 0.39786 -0.00078 -0.01009 0.12143  107 PHE   A CD1 
845  C CD2 . PHE   A 107 ? 0.25695 0.32880 0.28676 -0.00796 -0.01772 0.11349  107 PHE   A CD2 
846  C CE1 . PHE   A 107 ? 0.33617 0.44627 0.38383 -0.00495 -0.00774 0.13103  107 PHE   A CE1 
847  C CE2 . PHE   A 107 ? 0.31581 0.40203 0.34219 -0.01118 -0.01553 0.12023  107 PHE   A CE2 
848  C CZ  . PHE   A 107 ? 0.24921 0.35809 0.28614 -0.01084 -0.01067 0.12994  107 PHE   A CZ  
849  N N   . ASN   A 108 ? 0.28639 0.34002 0.33387 -0.01096 -0.03005 0.11035  108 ASN   A N   
850  C CA  . ASN   A 108 ? 0.31302 0.36609 0.36097 -0.01792 -0.03570 0.11551  108 ASN   A CA  
851  C C   . ASN   A 108 ? 0.37832 0.43185 0.43499 -0.02119 -0.04049 0.11830  108 ASN   A C   
852  O O   . ASN   A 108 ? 0.42447 0.48266 0.48525 -0.02818 -0.04405 0.12553  108 ASN   A O   
853  C CB  . ASN   A 108 ? 0.39927 0.43903 0.43673 -0.01750 -0.03895 0.11229  108 ASN   A CB  
854  C CG  . ASN   A 108 ? 0.39303 0.43529 0.42105 -0.01526 -0.03552 0.11188  108 ASN   A CG  
855  O OD1 . ASN   A 108 ? 0.39370 0.44654 0.42075 -0.01654 -0.03230 0.11623  108 ASN   A OD1 
856  N ND2 . ASN   A 108 ? 0.34796 0.38196 0.36780 -0.01148 -0.03624 0.10701  108 ASN   A ND2 
857  N N   . ASN   A 109 ? 0.28754 0.33589 0.34539 -0.01614 -0.04076 0.11339  109 ASN   A N   
858  C CA  . ASN   A 109 ? 0.30250 0.35256 0.36673 -0.01792 -0.04578 0.11607  109 ASN   A CA  
859  C C   . ASN   A 109 ? 0.35527 0.42322 0.42928 -0.01730 -0.04275 0.12236  109 ASN   A C   
860  O O   . ASN   A 109 ? 0.33827 0.41423 0.41957 -0.02249 -0.04792 0.12821  109 ASN   A O   
861  C CB  . ASN   A 109 ? 0.27913 0.31854 0.33753 -0.01016 -0.04673 0.10942  109 ASN   A CB  
862  C CG  . ASN   A 109 ? 0.40958 0.43319 0.45850 -0.01092 -0.05128 0.10469  109 ASN   A CG  
863  O OD1 . ASN   A 109 ? 0.41514 0.43335 0.46245 -0.01754 -0.05621 0.10728  109 ASN   A OD1 
864  N ND2 . ASN   A 109 ? 0.35047 0.36594 0.39135 -0.00292 -0.04933 0.09856  109 ASN   A ND2 
865  N N   . GLN   A 110 ? 0.37721 0.45176 0.45064 -0.01062 -0.03486 0.12162  110 GLN   A N   
866  C CA  . GLN   A 110 ? 0.28575 0.38102 0.36913 -0.00867 -0.03143 0.12969  110 GLN   A CA  
867  C C   . GLN   A 110 ? 0.32741 0.44683 0.42503 -0.02115 -0.03312 0.14444  110 GLN   A C   
868  O O   . GLN   A 110 ? 0.36003 0.51066 0.47684 -0.02623 -0.03394 0.15990  110 GLN   A O   
869  C CB  . GLN   A 110 ? 0.31071 0.40603 0.39009 0.00239  -0.02276 0.12713  110 GLN   A CB  
870  C CG  . GLN   A 110 ? 0.24439 0.32654 0.31678 0.01480  -0.02113 0.11991  110 GLN   A CG  
871  C CD  . GLN   A 110 ? 0.18816 0.28866 0.27062 0.02210  -0.02227 0.12624  110 GLN   A CD  
872  O OE1 . GLN   A 110 ? 0.43312 0.56016 0.53155 0.01511  -0.02568 0.13787  110 GLN   A OE1 
873  N NE2 . GLN   A 110 ? 0.51184 0.60212 0.58668 0.03594  -0.01992 0.12033  110 GLN   A NE2 
874  N N   . LEU   A 111 ? 0.37313 0.48039 0.45918 -0.02513 -0.03344 0.14044  111 LEU   A N   
875  C CA  . LEU   A 111 ? 0.38428 0.50772 0.47610 -0.03554 -0.03548 0.15287  111 LEU   A CA  
876  C C   . LEU   A 111 ? 0.43896 0.56600 0.54144 -0.04758 -0.04521 0.16223  111 LEU   A C   
877  O O   . LEU   A 111 ? 0.44470 0.59324 0.55738 -0.05766 -0.04708 0.17686  111 LEU   A O   
878  C CB  . LEU   A 111 ? 0.31568 0.41916 0.38637 -0.03438 -0.03294 0.14572  111 LEU   A CB  
879  C CG  . LEU   A 111 ? 0.23597 0.34009 0.29678 -0.02658 -0.02569 0.14004  111 LEU   A CG  
880  C CD1 . LEU   A 111 ? 0.22453 0.31667 0.26833 -0.02705 -0.02522 0.13752  111 LEU   A CD1 
881  C CD2 . LEU   A 111 ? 0.29270 0.42840 0.36475 -0.02639 -0.01988 0.15159  111 LEU   A CD2 
882  N N   . ILE   A 112 ? 0.38592 0.49095 0.48323 -0.04703 -0.05120 0.15398  112 ILE   A N   
883  C CA  . ILE   A 112 ? 0.36671 0.47279 0.47425 -0.05989 -0.06290 0.16359  112 ILE   A CA  
884  C C   . ILE   A 112 ? 0.35714 0.49664 0.49055 -0.06625 -0.06798 0.17745  112 ILE   A C   
885  O O   . ILE   A 112 ? 0.40603 0.56791 0.55475 -0.08100 -0.07712 0.19442  112 ILE   A O   
886  C CB  . ILE   A 112 ? 0.30566 0.37855 0.39732 -0.05557 -0.06737 0.15044  112 ILE   A CB  
887  C CG1 . ILE   A 112 ? 0.30285 0.35016 0.37002 -0.04845 -0.06099 0.14023  112 ILE   A CG1 
888  C CG2 . ILE   A 112 ? 0.43665 0.50782 0.53913 -0.07040 -0.08213 0.16122  112 ILE   A CG2 
889  C CD1 . ILE   A 112 ? 0.40235 0.42842 0.46011 -0.04437 -0.06599 0.13240  112 ILE   A CD1 
890  N N   . VAL   A 113 ? 0.35725 0.49604 0.48733 -0.05238 -0.06118 0.16921  113 VAL   A N   
891  C CA  . VAL   A 113 ? 0.32682 0.49021 0.46847 -0.04948 -0.06355 0.17640  113 VAL   A CA  
892  C C   . VAL   A 113 ? 0.33511 0.54032 0.49220 -0.05319 -0.05804 0.19219  113 VAL   A C   
893  O O   . VAL   A 113 ? 0.40935 0.64590 0.58190 -0.05880 -0.06366 0.19443  113 VAL   A O   
894  C CB  . VAL   A 113 ? 0.32227 0.46980 0.44788 -0.02595 -0.05824 0.15724  113 VAL   A CB  
895  C CG1 . VAL   A 113 ? 0.33892 0.51685 0.47544 -0.01569 -0.06135 0.15649  113 VAL   A CG1 
896  C CG2 . VAL   A 113 ? 0.22211 0.33473 0.32954 -0.02173 -0.06316 0.14239  113 VAL   A CG2 
897  N N   . MET   A 114 ? 0.34523 0.55609 0.50002 -0.04840 -0.04652 0.19390  114 MET   A N   
898  C CA  . MET   A 114 ? 0.38912 0.63804 0.55102 -0.04700 -0.03992 0.20656  114 MET   A CA  
899  C C   . MET   A 114 ? 0.37379 0.63251 0.53791 -0.06386 -0.04305 0.21186  114 MET   A C   
900  O O   . MET   A 114 ? 0.46130 0.74924 0.63281 -0.06635 -0.03240 0.21018  114 MET   A O   
901  C CB  . MET   A 114 ? 0.38179 0.63144 0.53787 -0.03269 -0.02637 0.20174  114 MET   A CB  
902  C CG  . MET   A 114 ? 0.29795 0.52654 0.44353 -0.01050 -0.02235 0.18415  114 MET   A CG  
903  S SD  . MET   A 114 ? 0.54040 0.77169 0.67886 0.00612  -0.00840 0.18188  114 MET   A SD  
904  C CE  . MET   A 114 ? 0.45255 0.64866 0.57728 0.02648  -0.00650 0.16422  114 MET   A CE  
905  N N   . GLY   A 115 ? 0.40951 0.63822 0.56516 -0.07509 -0.05146 0.21006  115 GLY   A N   
906  C CA  . GLY   A 115 ? 0.29110 0.51361 0.44015 -0.09045 -0.04553 0.21061  115 GLY   A CA  
907  C C   . GLY   A 115 ? 0.36921 0.59151 0.50445 -0.08439 -0.03375 0.20874  115 GLY   A C   
908  O O   . GLY   A 115 ? 0.46904 0.70052 0.60291 -0.09504 -0.02488 0.21259  115 GLY   A O   
909  N N   . TYR   A 116 ? 0.40251 0.61522 0.52834 -0.06858 -0.03217 0.20140  116 TYR   A N   
910  C CA  . TYR   A 116 ? 0.34113 0.55440 0.45256 -0.06349 -0.02161 0.19838  116 TYR   A CA  
911  C C   . TYR   A 116 ? 0.46567 0.65186 0.55875 -0.07048 -0.02048 0.19742  116 TYR   A C   
912  O O   . TYR   A 116 ? 0.47391 0.66779 0.55740 -0.07220 -0.01130 0.20099  116 TYR   A O   
913  C CB  . TYR   A 116 ? 0.27996 0.48552 0.38520 -0.04778 -0.01933 0.18817  116 TYR   A CB  
914  C CG  . TYR   A 116 ? 0.28533 0.49978 0.37770 -0.04233 -0.00870 0.18610  116 TYR   A CG  
915  C CD1 . TYR   A 116 ? 0.35592 0.55088 0.42877 -0.04306 -0.00742 0.18097  116 TYR   A CD1 
916  C CD2 . TYR   A 116 ? 0.37790 0.62225 0.47649 -0.03522 0.00090  0.18896  116 TYR   A CD2 
917  C CE1 . TYR   A 116 ? 0.35520 0.56267 0.41606 -0.03869 0.00129  0.17978  116 TYR   A CE1 
918  C CE2 . TYR   A 116 ? 0.41018 0.66402 0.49567 -0.03057 0.01110  0.18540  116 TYR   A CE2 
919  C CZ  . TYR   A 116 ? 0.40485 0.64140 0.47170 -0.03315 0.01034  0.18138  116 TYR   A CZ  
920  O OH  . TYR   A 116 ? 0.39137 0.64200 0.44465 -0.02883 0.01970  0.17804  116 TYR   A OH  
921  N N   . ASN   A 117 ? 0.43392 0.58905 0.52053 -0.07302 -0.02844 0.19313  117 ASN   A N   
922  C CA  . ASN   A 117 ? 0.51338 0.64009 0.57985 -0.07628 -0.02556 0.19335  117 ASN   A CA  
923  C C   . ASN   A 117 ? 0.57141 0.70336 0.63916 -0.09157 -0.01877 0.20631  117 ASN   A C   
924  O O   . ASN   A 117 ? 0.64625 0.76505 0.69673 -0.09252 -0.01085 0.21068  117 ASN   A O   
925  C CB  . ASN   A 117 ? 0.58350 0.67659 0.64184 -0.07411 -0.03372 0.18549  117 ASN   A CB  
926  C CG  . ASN   A 117 ? 0.62061 0.70498 0.67381 -0.05978 -0.03620 0.17022  117 ASN   A CG  
927  O OD1 . ASN   A 117 ? 0.49016 0.58172 0.53732 -0.05165 -0.03075 0.16515  117 ASN   A OD1 
928  N ND2 . ASN   A 117 ? 0.59603 0.66445 0.65061 -0.05767 -0.04340 0.16253  117 ASN   A ND2 
929  N N   . ASN   A 118 ? 0.55124 0.70282 0.63905 -0.10411 -0.02033 0.21242  118 ASN   A N   
930  C CA  . ASN   A 118 ? 0.54580 0.70445 0.63781 -0.12143 -0.01068 0.22224  118 ASN   A CA  
931  C C   . ASN   A 118 ? 0.52798 0.71386 0.61718 -0.11907 0.00226  0.22684  118 ASN   A C   
932  O O   . ASN   A 118 ? 0.57503 0.75875 0.65865 -0.12973 0.01321  0.23513  118 ASN   A O   
933  C CB  . ASN   A 118 ? 0.47751 0.65735 0.59495 -0.13654 -0.01425 0.22373  118 ASN   A CB  
934  C CG  . ASN   A 118 ? 0.66310 0.81784 0.78314 -0.13985 -0.02790 0.21933  118 ASN   A CG  
935  O OD1 . ASN   A 118 ? 0.80734 0.98018 0.94330 -0.13770 -0.03734 0.21605  118 ASN   A OD1 
936  N ND2 . ASN   A 118 ? 0.90810 1.02101 1.01118 -0.14374 -0.02823 0.21955  118 ASN   A ND2 
937  N N   . PHE   A 119 ? 0.50056 0.71084 0.59259 -0.10516 0.00240  0.22180  119 PHE   A N   
938  C CA  . PHE   A 119 ? 0.39926 0.63404 0.48533 -0.10082 0.01437  0.22438  119 PHE   A CA  
939  C C   . PHE   A 119 ? 0.42476 0.63626 0.48509 -0.09441 0.01778  0.22498  119 PHE   A C   
940  O O   . PHE   A 119 ? 0.58802 0.81132 0.63930 -0.09672 0.02871  0.23178  119 PHE   A O   
941  C CB  . PHE   A 119 ? 0.48090 0.74439 0.57524 -0.08707 0.01493  0.21764  119 PHE   A CB  
942  C CG  . PHE   A 119 ? 0.36159 0.66057 0.47968 -0.09099 0.01743  0.21853  119 PHE   A CG  
943  C CD1 . PHE   A 119 ? 0.37760 0.67670 0.51072 -0.09054 0.00765  0.21623  119 PHE   A CD1 
944  C CD2 . PHE   A 119 ? 0.46083 0.79593 0.58639 -0.09394 0.02998  0.22073  119 PHE   A CD2 
945  C CE1 . PHE   A 119 ? 0.33969 0.67547 0.49524 -0.09236 0.01030  0.21516  119 PHE   A CE1 
946  C CE2 . PHE   A 119 ? 0.44072 0.81214 0.58949 -0.09573 0.03286  0.21858  119 PHE   A CE2 
947  C CZ  . PHE   A 119 ? 0.46167 0.83402 0.62566 -0.09458 0.02292  0.21522  119 PHE   A CZ  
948  N N   . ILE   A 120 ? 0.39830 0.57934 0.44643 -0.08571 0.00921  0.21762  120 ILE   A N   
949  C CA  . ILE   A 120 ? 0.55246 0.71319 0.57580 -0.07868 0.01213  0.21746  120 ILE   A CA  
950  C C   . ILE   A 120 ? 0.67071 0.80646 0.68105 -0.08848 0.01785  0.22879  120 ILE   A C   
951  O O   . ILE   A 120 ? 0.65897 0.79144 0.65033 -0.08625 0.02611  0.23602  120 ILE   A O   
952  C CB  . ILE   A 120 ? 0.47536 0.61288 0.49055 -0.06690 0.00278  0.20460  120 ILE   A CB  
953  C CG1 . ILE   A 120 ? 0.41452 0.57264 0.44275 -0.05903 -0.00039 0.19479  120 ILE   A CG1 
954  C CG2 . ILE   A 120 ? 0.61878 0.74181 0.60876 -0.05852 0.00563  0.20389  120 ILE   A CG2 
955  C CD1 . ILE   A 120 ? 0.53802 0.67452 0.56061 -0.04954 -0.00752 0.18135  120 ILE   A CD1 
956  N N   . LEU   A 121 ? 0.67793 0.79516 0.69708 -0.09959 0.01436  0.23122  121 LEU   A N   
957  C CA  . LEU   A 121 ? 0.61093 0.69838 0.61692 -0.11022 0.02193  0.24224  121 LEU   A CA  
958  C C   . LEU   A 121 ? 0.62032 0.72898 0.62979 -0.12256 0.03642  0.25507  121 LEU   A C   
959  O O   . LEU   A 121 ? 0.70971 0.80015 0.69809 -0.12404 0.04701  0.26581  121 LEU   A O   
960  C CB  . LEU   A 121 ? 0.62878 0.69381 0.64584 -0.12128 0.01541  0.24059  121 LEU   A CB  
961  C CG  . LEU   A 121 ? 0.66049 0.70411 0.67349 -0.10932 0.00196  0.22802  121 LEU   A CG  
962  C CD1 . LEU   A 121 ? 0.72312 0.74844 0.74762 -0.12179 -0.00438 0.22739  121 LEU   A CD1 
963  C CD2 . LEU   A 121 ? 0.72637 0.73814 0.70889 -0.09451 0.00384  0.22589  121 LEU   A CD2 
964  N N   . LYS   A 122 ? 0.57223 0.71997 0.60693 -0.13066 0.03809  0.25437  122 LYS   A N   
965  C CA  . LYS   A 122 ? 0.59047 0.76445 0.63028 -0.14153 0.05311  0.26459  122 LYS   A CA  
966  C C   . LYS   A 122 ? 0.68178 0.87251 0.70339 -0.12831 0.06010  0.26734  122 LYS   A C   
967  O O   . LYS   A 122 ? 0.85354 1.05167 0.86660 -0.13448 0.07397  0.27874  122 LYS   A O   
968  C CB  . LYS   A 122 ? 0.46043 0.67684 0.53154 -0.15038 0.05311  0.26061  122 LYS   A CB  
969  C CG  . LYS   A 122 ? 0.70052 0.94388 0.78209 -0.16564 0.06945  0.26978  122 LYS   A CG  
970  C CD  . LYS   A 122 ? 1.07855 1.35601 1.19359 -0.17869 0.06856  0.26451  122 LYS   A CD  
971  C CE  . LYS   A 122 ? 0.85081 1.10053 0.97689 -0.19324 0.06032  0.26162  122 LYS   A CE  
972  N NZ  . LYS   A 122 ? 0.97405 1.18521 1.08913 -0.21012 0.07099  0.27178  122 LYS   A NZ  
973  N N   . GLU   A 123 ? 0.68117 0.87861 0.69675 -0.11095 0.05142  0.25687  123 GLU   A N   
974  C CA  . GLU   A 123 ? 0.66968 0.88031 0.66593 -0.09842 0.05663  0.25767  123 GLU   A CA  
975  C C   . GLU   A 123 ? 0.72524 0.90270 0.69262 -0.09661 0.06126  0.26765  123 GLU   A C   
976  O O   . GLU   A 123 ? 0.64176 0.83148 0.59370 -0.09470 0.07178  0.27697  123 GLU   A O   
977  C CB  . GLU   A 123 ? 0.58854 0.80671 0.58440 -0.08277 0.04658  0.24303  123 GLU   A CB  
978  C CG  . GLU   A 123 ? 0.79848 1.01049 0.76900 -0.06990 0.04660  0.24127  123 GLU   A CG  
979  C CD  . GLU   A 123 ? 0.72094 0.92986 0.69148 -0.05809 0.03622  0.22603  123 GLU   A CD  
980  O OE1 . GLU   A 123 ? 0.66920 0.88191 0.65827 -0.05847 0.03030  0.21761  123 GLU   A OE1 
981  O OE2 . GLU   A 123 ? 0.87320 1.07666 0.82483 -0.04857 0.03454  0.22294  123 GLU   A OE2 
982  N N   . LYS   A 124 ? 0.70559 0.84095 0.66339 -0.09586 0.05404  0.26607  124 LYS   A N   
983  C CA  . LYS   A 124 ? 0.71662 0.81619 0.64330 -0.09178 0.05855  0.27563  124 LYS   A CA  
984  C C   . LYS   A 124 ? 0.85574 0.94195 0.77590 -0.10721 0.07368  0.29322  124 LYS   A C   
985  O O   . LYS   A 124 ? 1.01384 1.09017 0.90786 -0.10393 0.08314  0.30566  124 LYS   A O   
986  C CB  . LYS   A 124 ? 0.58732 0.64509 0.50464 -0.08583 0.04796  0.26807  124 LYS   A CB  
987  N N   . LYS   A 125 ? 0.82488 0.91135 0.76844 -0.12489 0.07661  0.29468  125 LYS   A N   
988  C CA  . LYS   A 125 ? 0.71461 0.78826 0.65558 -0.14318 0.09311  0.31045  125 LYS   A CA  
989  C C   . LYS   A 125 ? 0.74631 0.86027 0.68846 -0.14571 0.10642  0.31933  125 LYS   A C   
990  O O   . LYS   A 125 ? 1.13675 1.23660 1.05970 -0.15210 0.12164  0.33522  125 LYS   A O   
991  C CB  . LYS   A 125 ? 0.61449 0.68606 0.58524 -0.16320 0.09244  0.30713  125 LYS   A CB  
992  N N   . ILE   A 126 ? 0.71389 0.87692 0.67633 -0.14005 0.10189  0.30954  126 ILE   A N   
993  C CA  . ILE   A 126 ? 0.81266 1.01776 0.77616 -0.14015 0.11448  0.31590  126 ILE   A CA  
994  C C   . ILE   A 126 ? 0.93259 1.13352 0.86240 -0.12483 0.11839  0.32310  126 ILE   A C   
995  O O   . ILE   A 126 ? 0.88928 1.10132 0.80637 -0.12831 0.13330  0.33672  126 ILE   A O   
996  C CB  . ILE   A 126 ? 0.78980 1.04459 0.77915 -0.13453 0.10851  0.30203  126 ILE   A CB  
997  C CG1 . ILE   A 126 ? 0.86267 1.14302 0.88319 -0.15291 0.11533  0.30268  126 ILE   A CG1 
998  C CG2 . ILE   A 126 ? 0.79400 1.08537 0.77126 -0.12025 0.11411  0.30130  126 ILE   A CG2 
999  C CD1 . ILE   A 126 ? 0.84267 1.09310 0.87835 -0.16897 0.11005  0.30163  126 ILE   A CD1 
1000 N N   . ASN   A 127 ? 0.95337 1.14008 0.86836 -0.10788 0.10529  0.31408  127 ASN   A N   
1001 C CA  . ASN   A 127 ? 0.91586 1.10020 0.79908 -0.09297 0.10715  0.31987  127 ASN   A CA  
1002 C C   . ASN   A 127 ? 1.03708 1.17867 0.89152 -0.09828 0.11712  0.33865  127 ASN   A C   
1003 O O   . ASN   A 127 ? 0.97461 1.12284 0.80415 -0.09156 0.12562  0.35065  127 ASN   A O   
1004 C CB  . ASN   A 127 ? 0.95568 1.13367 0.83229 -0.07601 0.09097  0.30488  127 ASN   A CB  
1005 C CG  . ASN   A 127 ? 1.05299 1.27361 0.94973 -0.06871 0.08438  0.28813  127 ASN   A CG  
1006 O OD1 . ASN   A 127 ? 1.04588 1.30068 0.96064 -0.07451 0.09096  0.28711  127 ASN   A OD1 
1007 N ND2 . ASN   A 127 ? 0.88130 1.09907 0.77400 -0.05607 0.07234  0.27464  127 ASN   A ND2 
1008 N N   . ASP   A 128 ? 1.20196 1.29897 1.05760 -0.10996 0.11678  0.34163  128 ASP   A N   
1009 C CA  . ASP   A 128 ? 1.26909 1.31868 1.09503 -0.11676 0.12817  0.35992  128 ASP   A CA  
1010 C C   . ASP   A 128 ? 1.06917 1.13111 0.89842 -0.13443 0.14883  0.37634  128 ASP   A C   
1011 O O   . ASP   A 128 ? 1.18519 1.23631 0.98474 -0.13289 0.16085  0.39361  128 ASP   A O   
1012 C CB  . ASP   A 128 ? 1.08129 1.07903 0.90764 -0.12454 0.12304  0.35650  128 ASP   A CB  
1013 C CG  . ASP   A 128 ? 1.41216 1.39705 1.23304 -0.10654 0.10385  0.34162  128 ASP   A CG  
1014 O OD1 . ASP   A 128 ? 1.47255 1.48893 1.29206 -0.09025 0.09497  0.33289  128 ASP   A OD1 
1015 O OD2 . ASP   A 128 ? 1.44596 1.39220 1.26580 -0.10923 0.09824  0.33927  128 ASP   A OD2 
1016 N N   A MET   A 129 ? 0.97757 1.06418 0.84275 -0.15148 0.15331  0.37149  129 MET   A N   
1017 N N   B MET   A 129 ? 0.96967 1.05671 0.83514 -0.15141 0.15318  0.37131  129 MET   A N   
1018 C CA  A MET   A 129 ? 1.08527 1.18849 0.95778 -0.16987 0.17398  0.38554  129 MET   A CA  
1019 C CA  B MET   A 129 ? 1.08535 1.19250 0.96179 -0.17013 0.17297  0.38381  129 MET   A CA  
1020 C C   A MET   A 129 ? 1.09845 1.25533 0.96840 -0.15975 0.18023  0.38850  129 MET   A C   
1021 C C   B MET   A 129 ? 1.10219 1.26256 0.97560 -0.15985 0.17927  0.38683  129 MET   A C   
1022 O O   A MET   A 129 ? 1.10046 1.28255 0.98062 -0.17325 0.19696  0.39778  129 MET   A O   
1023 O O   B MET   A 129 ? 1.09261 1.28273 0.98021 -0.17309 0.19462  0.39394  129 MET   A O   
1024 C CB  A MET   A 129 ? 1.12584 1.24427 1.04021 -0.19156 0.17612  0.37796  129 MET   A CB  
1025 C CB  B MET   A 129 ? 1.15257 1.27878 1.07231 -0.18967 0.17280  0.37421  129 MET   A CB  
1026 C CG  A MET   A 129 ? 0.98743 1.16435 0.93520 -0.18582 0.16539  0.36122  129 MET   A CG  
1027 C CG  B MET   A 129 ? 1.08791 1.16763 1.01558 -0.20123 0.16666  0.36929  129 MET   A CG  
1028 S SD  A MET   A 129 ? 0.82561 1.02377 0.82084 -0.21161 0.16789  0.35374  129 MET   A SD  
1029 S SD  B MET   A 129 ? 1.40166 1.41357 1.30051 -0.21925 0.18705  0.38972  129 MET   A SD  
1030 C CE  A MET   A 129 ? 0.88091 1.15334 0.90181 -0.20040 0.16237  0.34056  129 MET   A CE  
1031 C CE  B MET   A 129 ? 0.93029 0.91421 0.86021 -0.23902 0.18154  0.37808  129 MET   A CE  
1032 N N   . LEU   A 130 ? 1.09362 1.26953 0.95053 -0.13666 0.16803  0.38008  130 LEU   A N   
1033 C CA  . LEU   A 130 ? 1.18270 1.40763 1.03274 -0.12422 0.17322  0.38138  130 LEU   A CA  
1034 C C   . LEU   A 130 ? 1.17955 1.39088 0.98895 -0.10783 0.17423  0.39245  130 LEU   A C   
1035 O O   . LEU   A 130 ? 1.16122 1.39814 0.95565 -0.10415 0.18676  0.40414  130 LEU   A O   
1036 C CB  . LEU   A 130 ? 0.87935 1.14751 0.75145 -0.11125 0.15906  0.35946  130 LEU   A CB  
1037 C CG  . LEU   A 130 ? 0.92663 1.25243 0.80116 -0.10213 0.16597  0.35631  130 LEU   A CG  
1038 N N   . LYS   A 131 ? 1.32785 1.50151 1.11892 -0.09713 0.16107  0.38897  131 LYS   A N   
1039 C CA  . LYS   A 131 ? 1.10874 1.26527 0.86027 -0.08246 0.16151  0.40126  131 LYS   A CA  
1040 C C   . LYS   A 131 ? 1.48052 1.59652 1.20626 -0.09552 0.17869  0.42640  131 LYS   A C   
1041 O O   . LYS   A 131 ? 1.46052 1.57370 1.15328 -0.08507 0.18425  0.44188  131 LYS   A O   
1042 C CB  . LYS   A 131 ? 1.01271 1.14049 0.75368 -0.06849 0.14273  0.39002  131 LYS   A CB  
1043 N N   . LEU   A 132 ? 1.28147 1.36752 1.02174 -0.11868 0.18786  0.43089  132 LEU   A N   
1044 C CA  . LEU   A 132 ? 1.11913 1.16640 0.83834 -0.13641 0.20764  0.45418  132 LEU   A CA  
1045 C C   . LEU   A 132 ? 1.14646 1.23444 0.87062 -0.14530 0.22769  0.46682  132 LEU   A C   
1046 O O   . LEU   A 132 ? 1.37329 1.43725 1.09250 -0.16690 0.24737  0.48351  132 LEU   A O   
1047 C CB  . LEU   A 132 ? 1.04864 1.05167 0.78486 -0.15968 0.21125  0.45168  132 LEU   A CB  
1048 N N   . VAL   A 133 ? 1.24142 1.39005 0.97469 -0.12978 0.22405  0.45862  133 VAL   A N   
1049 C CA  . VAL   A 133 ? 1.50197 1.69515 1.23810 -0.13437 0.24217  0.46909  133 VAL   A CA  
1050 C C   . VAL   A 133 ? 1.21665 1.46745 0.95026 -0.10964 0.23364  0.45842  133 VAL   A C   
1051 O O   . VAL   A 133 ? 1.27950 1.53768 0.98122 -0.09346 0.23587  0.46930  133 VAL   A O   
1052 C CB  . VAL   A 133 ? 1.19102 1.40763 0.96850 -0.15772 0.25268  0.46349  133 VAL   A CB  
1053 C CG1 . VAL   A 133 ? 0.97502 1.21533 0.78899 -0.15362 0.23376  0.43750  133 VAL   A CG1 
1054 C CG2 . VAL   A 133 ? 1.40712 1.67815 1.18897 -0.15927 0.27011  0.47154  133 VAL   A CG2 
1055 N N1  A A1IUW B .   ? 0.57955 0.53388 0.62794 -0.07400 0.08570  -0.00014 201 A1IUW A N1  
1056 N N1  B A1IUW B .   ? 0.57851 0.53435 0.62675 -0.07472 0.08593  -0.00217 201 A1IUW A N1  
1057 C C4  A A1IUW B .   ? 0.60574 0.53611 0.66436 -0.08865 0.10063  -0.01086 201 A1IUW A C4  
1058 C C4  B A1IUW B .   ? 0.60656 0.53786 0.66503 -0.08897 0.10067  -0.01209 201 A1IUW A C4  
1059 C C5  A A1IUW B .   ? 0.67464 0.54831 0.73599 -0.08534 0.12231  -0.00926 201 A1IUW A C5  
1060 C C5  B A1IUW B .   ? 0.66957 0.54409 0.73081 -0.08572 0.12236  -0.01059 201 A1IUW A C5  
1061 C C6  A A1IUW B .   ? 0.68385 0.52450 0.74730 -0.07943 0.13054  0.01021  201 A1IUW A C6  
1062 C C6  B A1IUW B .   ? 0.71284 0.56442 0.77186 -0.08452 0.13542  -0.02635 201 A1IUW A C6  
1063 C C7  A A1IUW B .   ? 0.77193 0.56535 0.83222 -0.06893 0.14699  0.01366  201 A1IUW A C7  
1064 C C7  B A1IUW B .   ? 0.76846 0.56271 0.82732 -0.07647 0.15593  -0.02109 201 A1IUW A C7  
1065 C C8  A A1IUW B .   ? 0.80760 0.57340 0.86658 -0.06849 0.16184  -0.00098 201 A1IUW A C8  
1066 C C8  B A1IUW B .   ? 0.80694 0.57356 0.86594 -0.06840 0.16132  -0.00026 201 A1IUW A C8  
1067 C C10 A A1IUW B .   ? 0.71123 0.56362 0.77050 -0.08482 0.13495  -0.02565 201 A1IUW A C10 
1068 C C10 B A1IUW B .   ? 0.67992 0.52296 0.74360 -0.08059 0.13017  0.00838  201 A1IUW A C10 
1069 C C13 A A1IUW B .   ? 0.53518 0.53650 0.58001 -0.07825 0.06863  -0.00190 201 A1IUW A C13 
1070 C C13 B A1IUW B .   ? 0.53206 0.53467 0.57674 -0.07874 0.06873  -0.00328 201 A1IUW A C13 
1071 C C15 A A1IUW B .   ? 0.55689 0.62307 0.61001 -0.10082 0.05505  -0.02006 201 A1IUW A C15 
1072 C C15 B A1IUW B .   ? 0.51784 0.58381 0.57094 -0.10067 0.05498  -0.01973 201 A1IUW A C15 
1073 N N   A A1IUW B .   ? 0.91289 0.61307 0.96577 -0.05862 0.19216  -0.01607 201 A1IUW A N   
1074 N N   B A1IUW B .   ? 0.91384 0.61467 0.96684 -0.05859 0.19162  -0.01442 201 A1IUW A N   
1075 C C   A A1IUW B .   ? 0.53313 0.60488 0.61405 -0.13980 0.07505  -0.05650 201 A1IUW A C   
1076 C C   B A1IUW B .   ? 0.53120 0.60105 0.61224 -0.13893 0.07505  -0.05423 201 A1IUW A C   
1077 O O   A A1IUW B .   ? 1.05244 0.78070 1.09774 -0.03067 0.16777  0.02687  201 A1IUW A O   
1078 O O   B A1IUW B .   ? 1.05202 0.78253 1.09713 -0.02992 0.16628  0.02837  201 A1IUW A O   
1079 C C1  A A1IUW B .   ? 0.59334 0.60873 0.67962 -0.14699 0.09800  -0.06505 201 A1IUW A C1  
1080 C C1  B A1IUW B .   ? 0.59402 0.60742 0.68050 -0.14616 0.09809  -0.06257 201 A1IUW A C1  
1081 C C11 A A1IUW B .   ? 0.90434 0.63235 0.95638 -0.05084 0.17463  0.00485  201 A1IUW A C11 
1082 C C11 B A1IUW B .   ? 0.90475 0.63402 0.95675 -0.05050 0.17374  0.00618  201 A1IUW A C11 
1083 C C12 A A1IUW B .   ? 0.60276 0.46513 0.66737 -0.07810 0.11827  0.02703  201 A1IUW A C12 
1084 C C12 B A1IUW B .   ? 0.70421 0.59057 0.75904 -0.08956 0.12895  -0.04832 201 A1IUW A C12 
1085 C C14 A A1IUW B .   ? 0.54862 0.56266 0.60293 -0.09528 0.07111  -0.01526 201 A1IUW A C14 
1086 C C14 B A1IUW B .   ? 0.54892 0.56340 0.60305 -0.09519 0.07097  -0.01539 201 A1IUW A C14 
1087 C C2  A A1IUW B .   ? 0.61633 0.58093 0.69508 -0.12585 0.10406  -0.03623 201 A1IUW A C2  
1088 C C2  B A1IUW B .   ? 0.61652 0.57989 0.69480 -0.12444 0.10368  -0.03405 201 A1IUW A C2  
1089 C C3  A A1IUW B .   ? 0.56531 0.53441 0.62962 -0.10407 0.09203  -0.02150 201 A1IUW A C3  
1090 C C3  B A1IUW B .   ? 0.56986 0.53913 0.63394 -0.10374 0.09183  -0.02133 201 A1IUW A C3  
1091 C C9  A A1IUW B .   ? 0.76786 0.56367 0.82682 -0.07712 0.15559  -0.02194 201 A1IUW A C9  
1092 C C9  B A1IUW B .   ? 0.77086 0.56614 0.83163 -0.07009 0.14656  0.01324  201 A1IUW A C9  
1093 O O1  A A1IUW B .   ? 0.66408 0.74896 0.70749 -0.08679 0.03887  -0.00076 201 A1IUW A O1  
1094 O O1  B A1IUW B .   ? 0.66537 0.75018 0.70863 -0.08660 0.03877  -0.00055 201 A1IUW A O1  
1095 C C16 A A1IUW B .   ? 0.53390 0.63094 0.59798 -0.12350 0.05890  -0.04979 201 A1IUW A C16 
1096 C C16 B A1IUW B .   ? 0.53218 0.62818 0.59669 -0.12344 0.05904  -0.04886 201 A1IUW A C16 
1097 C C17 A A1IUW B .   ? 0.49523 0.52541 0.52810 -0.06580 0.05274  0.00982  201 A1IUW A C17 
1098 C C17 B A1IUW B .   ? 0.48370 0.51575 0.51635 -0.06652 0.05293  0.00801  201 A1IUW A C17 
1099 O O   . HOH   C .   ? 0.51084 0.64841 0.47627 -0.02084 -0.00525 0.15773  301 HOH   A O   
1100 O O   . HOH   C .   ? 0.79448 1.12452 0.68224 0.00641  0.00719  0.11450  302 HOH   A O   
1101 O O   . HOH   C .   ? 0.40331 0.58460 0.52542 0.02947  -0.02891 0.14805  303 HOH   A O   
1102 O O   . HOH   C .   ? 0.47104 0.65966 0.40498 -0.00043 -0.02573 0.09975  304 HOH   A O   
1103 O O   . HOH   C .   ? 0.45274 0.87960 0.39214 -0.03247 -0.03414 -0.02706 305 HOH   A O   
1104 O O   . HOH   C .   ? 0.41170 0.77092 0.50073 -0.13598 0.00223  -0.07224 306 HOH   A O   
1105 O O   . HOH   C .   ? 0.47845 0.50253 0.52570 0.07461  0.01180  0.11218  307 HOH   A O   
1106 O O   . HOH   C .   ? 0.38995 0.53253 0.40491 -0.07180 0.01822  0.00003  308 HOH   A O   
1107 O O   . HOH   C .   ? 0.56718 0.76052 0.67827 -0.11955 0.04665  0.01480  309 HOH   A O   
1108 O O   . HOH   C .   ? 0.64945 0.86532 0.54825 -0.03740 0.04920  0.24343  310 HOH   A O   
1109 O O   . HOH   C .   ? 0.40085 0.50433 0.40522 -0.04767 0.02071  0.03201  311 HOH   A O   
1110 O O   . HOH   C .   ? 0.61138 0.48175 0.62643 0.06488  0.07098  0.10047  312 HOH   A O   
1111 O O   . HOH   C .   ? 0.44603 0.81847 0.37346 -0.03337 -0.02828 -0.00291 313 HOH   A O   
1112 O O   . HOH   C .   ? 0.43093 0.50245 0.43793 -0.01464 -0.02520 0.12122  314 HOH   A O   
1113 O O   . HOH   C .   ? 0.51723 0.48149 0.53343 0.03345  0.00823  0.08966  315 HOH   A O   
1114 O O   . HOH   C .   ? 0.36861 0.54543 0.30749 -0.00386 -0.01746 0.11504  316 HOH   A O   
1115 O O   . HOH   C .   ? 0.59730 0.58908 0.67936 -0.08329 0.08413  0.07677  317 HOH   A O   
1116 O O   . HOH   C .   ? 0.84866 0.90133 0.83124 0.00548  -0.03421 0.08904  318 HOH   A O   
1117 O O   . HOH   C .   ? 0.66863 0.66993 0.69799 -0.06222 0.08118  -0.02317 319 HOH   A O   
1118 O O   . HOH   C .   ? 0.70756 0.55952 0.74477 0.08292  0.11855  0.08874  320 HOH   A O   
1119 O O   . HOH   C .   ? 0.48468 0.55611 0.47305 0.00578  -0.03383 0.07793  321 HOH   A O   
1120 O O   . HOH   C .   ? 0.51696 0.69919 0.50344 -0.06110 0.02349  -0.01512 322 HOH   A O   
1121 O O   . HOH   C .   ? 0.57316 0.87052 0.49943 -0.00748 0.02436  0.12055  323 HOH   A O   
1122 O O   . HOH   C .   ? 0.68898 1.06504 0.57346 -0.01052 0.01475  0.03645  324 HOH   A O   
1123 O O   . HOH   C .   ? 0.61012 0.88500 0.54683 -0.00995 -0.03562 0.05520  325 HOH   A O   
1124 O O   . HOH   C .   ? 0.45542 0.53526 0.42192 0.00799  -0.03727 0.09087  326 HOH   A O   
1125 O O   . HOH   C .   ? 0.45585 0.59683 0.44638 0.00178  -0.04040 0.07567  327 HOH   A O   
1126 O O   . HOH   C .   ? 0.51120 0.90402 0.61205 -0.16612 0.01454  -0.12534 328 HOH   A O   
1127 O O   . HOH   C .   ? 0.64322 0.62763 0.65673 0.03820  -0.01028 0.08802  329 HOH   A O   
1128 O O   . HOH   C .   ? 0.36614 0.42663 0.36404 -0.00379 -0.02639 0.08780  330 HOH   A O   
1129 O O   . HOH   C .   ? 0.61244 0.46939 0.65174 -0.03659 0.13119  -0.01410 331 HOH   A O   
1130 O O   . HOH   C .   ? 0.35505 0.39945 0.39757 -0.03739 -0.04674 0.13723  332 HOH   A O   
1131 O O   . HOH   C .   ? 0.48874 0.52908 0.48356 -0.00668 -0.03471 0.11128  333 HOH   A O   
1132 O O   . HOH   C .   ? 0.34397 0.39171 0.33474 0.00094  -0.02771 0.08362  334 HOH   A O   
1133 O O   . HOH   C .   ? 0.39163 0.56686 0.48761 -0.08474 0.04003  0.05677  335 HOH   A O   
1134 O O   . HOH   C .   ? 0.46087 0.66049 0.54956 -0.11162 0.02750  0.00079  336 HOH   A O   
1135 O O   . HOH   C .   ? 0.58741 0.59672 0.60042 -0.00544 -0.04273 0.09791  337 HOH   A O   
1136 O O   . HOH   C .   ? 0.50876 0.83282 0.60569 -0.04066 0.01024  0.07408  338 HOH   A O   
1137 O O   . HOH   C .   ? 0.43873 0.47552 0.43621 0.01500  -0.02754 0.07994  339 HOH   A O   
1138 O O   . HOH   C .   ? 0.56624 0.62875 0.58031 -0.05143 0.05348  0.00036  340 HOH   A O   
1139 O O   . HOH   C .   ? 0.76423 0.83452 0.74942 -0.00983 0.13303  -0.10794 341 HOH   A O   
1140 O O   . HOH   C .   ? 0.58504 0.46044 0.60893 0.07481  0.07936  0.10061  342 HOH   A O   
1141 O O   . HOH   C .   ? 0.53176 0.50139 0.53773 -0.03911 0.14597  -0.12545 343 HOH   A O   
1142 O O   . HOH   C .   ? 0.64618 1.11904 0.59892 -0.10926 0.01028  -0.19809 344 HOH   A O   
1143 O O   . HOH   C .   ? 0.59455 0.88216 0.57788 -0.00100 -0.04838 0.04043  345 HOH   A O   
1144 O O   . HOH   C .   ? 0.56919 0.55138 0.64689 -0.08762 0.08002  0.05730  346 HOH   A O   
1145 O O   . HOH   C .   ? 0.50225 0.63744 0.59482 0.06448  -0.02191 0.12750  347 HOH   A O   
1146 O O   . HOH   C .   ? 0.78678 0.69300 0.89684 -0.16399 0.14536  -0.04556 348 HOH   A O   
1147 O O   . HOH   C .   ? 0.65008 1.22792 0.71935 -0.03061 0.13187  0.19594  349 HOH   A O   
1148 O O   . HOH   C .   ? 0.49528 1.01159 0.48717 -0.14624 0.02252  -0.27744 350 HOH   A O   
1149 O O   . HOH   C .   ? 0.53568 0.61014 0.62766 -0.12099 0.06646  0.00585  351 HOH   A O   
1150 O O   . HOH   C .   ? 0.88916 0.66955 0.99832 -0.17753 0.20128  -0.07631 352 HOH   A O   
1151 O O   . HOH   C .   ? 0.47301 0.98209 0.56148 0.03667  0.12006  0.13268  353 HOH   A O   
1152 O O   . HOH   C .   ? 0.50068 1.07971 0.56418 -0.14135 -0.00879 -0.18138 354 HOH   A O   
1153 O O   . HOH   C .   ? 0.57822 1.08306 0.45878 -0.02430 -0.00120 -0.07295 355 HOH   A O   
1154 O O   . HOH   C .   ? 0.71681 0.63574 0.71836 0.08385  0.06077  0.12089  356 HOH   A O   
1155 O O   . HOH   C .   ? 0.56944 0.79313 0.69307 -0.17724 0.05702  -0.07888 357 HOH   A O   
1156 O O   . HOH   C .   ? 0.93182 0.57154 0.96475 -0.01448 0.21076  0.02884  358 HOH   A O   
1157 O O   . HOH   C .   ? 0.64077 0.47605 0.67367 -0.00727 0.09513  0.08047  359 HOH   A O   
1158 O O   . HOH   C .   ? 0.41995 0.76009 0.43289 -0.02811 -0.04382 0.02166  360 HOH   A O   
1159 O O   . HOH   C .   ? 0.60377 0.47921 0.61980 0.02074  0.05883  0.09175  361 HOH   A O   
1160 O O   . HOH   C .   ? 0.42995 0.50593 0.41767 -0.01570 -0.02489 0.13391  362 HOH   A O   
1161 O O   . HOH   C .   ? 0.65694 0.76497 0.67071 -0.15319 0.12779  -0.27868 363 HOH   A O   
1162 O O   . HOH   C .   ? 0.62710 0.84477 0.57731 0.00201  0.11919  -0.10050 364 HOH   A O   
1163 O O   . HOH   C .   ? 0.49010 0.86097 0.68434 -0.15510 0.02681  0.22513  365 HOH   A O   
1164 O O   . HOH   C .   ? 0.57664 0.71510 0.49650 -0.01236 -0.00136 0.17385  366 HOH   A O   
1165 O O   . HOH   C .   ? 0.59979 1.02578 0.46869 0.00309  0.03761  0.03738  367 HOH   A O   
1166 O O   . HOH   C .   ? 0.53817 0.61943 0.63837 -0.09495 0.07590  0.06983  368 HOH   A O   
1167 O O   . HOH   C .   ? 0.69956 0.90404 0.60600 0.01482  -0.02929 0.10832  369 HOH   A O   
1168 O O   . HOH   C .   ? 0.48719 0.61114 0.42471 -0.00071 -0.02145 0.12856  370 HOH   A O   
1169 O O   . HOH   C .   ? 0.61566 1.10259 0.49040 -0.03800 0.02887  -0.13043 371 HOH   A O   
1170 O O   . HOH   C .   ? 0.88599 0.56907 0.90016 0.05132  0.18185  0.06643  372 HOH   A O   
1171 O O   . HOH   C .   ? 0.67111 0.80466 0.57419 0.00084  -0.01081 0.16719  373 HOH   A O   
1172 O O   . HOH   C .   ? 0.49935 0.71995 0.64810 -0.12756 0.08652  0.04606  374 HOH   A O   
1173 O O   . HOH   C .   ? 0.74424 0.60941 0.82193 -0.09612 0.12703  0.03717  375 HOH   A O   
1174 O O   . HOH   C .   ? 1.04271 0.80615 1.08288 -0.02544 0.14621  0.07460  376 HOH   A O   
1175 O O   . HOH   C .   ? 0.56064 0.62432 0.67935 -0.11973 0.11086  0.07071  377 HOH   A O   
# 
