data_9FF8
# 
_entry.id   9FF8 
# 
_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   9FF8         pdb_00009ff8 10.2210/pdb9ff8/pdb 
WWPDB D_1292138773 ?            ?                   
# 
_pdbx_audit_revision_history.ordinal             1 
_pdbx_audit_revision_history.data_content_type   'Structure model' 
_pdbx_audit_revision_history.major_revision      1 
_pdbx_audit_revision_history.minor_revision      0 
_pdbx_audit_revision_history.revision_date       2025-06-04 
_pdbx_audit_revision_history.part_number         ? 
# 
_pdbx_audit_revision_details.ordinal             1 
_pdbx_audit_revision_details.revision_ordinal    1 
_pdbx_audit_revision_details.data_content_type   'Structure model' 
_pdbx_audit_revision_details.provider            repository 
_pdbx_audit_revision_details.type                'Initial release' 
_pdbx_audit_revision_details.description         ? 
_pdbx_audit_revision_details.details             ? 
# 
_pdbx_database_status.status_code                     REL 
_pdbx_database_status.status_code_sf                  REL 
_pdbx_database_status.status_code_mr                  ? 
_pdbx_database_status.entry_id                        9FF8 
_pdbx_database_status.recvd_initial_deposition_date   2024-05-22 
_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 
# 
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 
7 susanna.nencetti@unipi.it     Susanna    Nencetti  ? 'principal investigator/group leader' 0000-0002-3547-7277 
8 elisabetta.orlandini@unipi.it Elisabetta Orlandini ? 'principal investigator/group leader' 0000-0003-3398-2787 
# 
loop_
_audit_author.name 
_audit_author.pdbx_ordinal 
_audit_author.identifier_ORCID 
'Ciccone, L.'    1 0000-0002-2762-1929 
'Shepard, W.'    2 0000-0002-5724-1193 
'Sirigu, S.'     3 0000-0003-0875-5590 
'Camodeca, C.'   4 0000-0002-8676-7311 
'Mazzoccchi, F.' 5 0009-0004-9586-2697 
'Fruchart, C.'   6 0000-0002-3149-4774 
'Nencetti, S.'   7 0000-0002-3547-7277 
'Orlandini, E.'  8 0000-0003-3398-2787 
# 
_citation.abstract                  ? 
_citation.abstract_id_CAS           ? 
_citation.book_id_ISBN              ? 
_citation.book_publisher            ? 
_citation.book_publisher_city       ? 
_citation.book_title                ? 
_citation.coordinate_linkage        ? 
_citation.country                   ? 
_citation.database_id_Medline       ? 
_citation.details                   ? 
_citation.id                        primary 
_citation.journal_abbrev            'To Be Published' 
_citation.journal_id_ASTM           ? 
_citation.journal_id_CSD            0353 
_citation.journal_id_ISSN           ? 
_citation.journal_full              ? 
_citation.journal_issue             ? 
_citation.journal_volume            ? 
_citation.language                  ? 
_citation.page_first                ? 
_citation.page_last                 ? 
_citation.title                     
'Human transthyretin (TTR) in complex with (E)-2-((((2-chlorobenzyl)oxy)imino)methyl)benzoic acid (Lic166)' 
_citation.year                      ? 
_citation.database_id_CSD           ? 
_citation.pdbx_database_id_DOI      ? 
_citation.pdbx_database_id_PubMed   ? 
_citation.pdbx_database_id_patent   ? 
_citation.unpublished_flag          ? 
# 
loop_
_citation_author.citation_id 
_citation_author.name 
_citation_author.ordinal 
_citation_author.identifier_ORCID 
primary 'Ciccone, L.'    1 0000-0002-2762-1929 
primary 'Shepard, W.'    2 0000-0002-5724-1193 
primary 'Sirigu, S.'     3 0000-0003-0875-5590 
primary 'Camodeca, C.'   4 0000-0002-8676-7311 
primary 'Mazzoccchi, F.' 5 0009-0004-9586-2697 
primary 'Fruchart, C.'   6 0000-0002-3149-4774 
primary 'Nencetti, S.'   7 0000-0002-3547-7277 
primary 'Orlandini, E.'  8 0000-0003-3398-2787 
# 
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 Transthyretin                                        13777.360 2   ? ? ? ? 
2 non-polymer syn 1,2-ETHANEDIOL                                       62.068    2   ? ? ? ? 
3 non-polymer syn '2-[(2-chlorophenyl)methoxyiminomethyl]benzoic acid' 289.714   2   ? ? ? ? 
4 non-polymer syn GLYCEROL                                             92.094    1   ? ? ? ? 
5 water       nat water                                                18.015    268 ? ? ? ? 
# 
_entity_name_com.entity_id   1 
_entity_name_com.name        ATTR,Prealbumin,TBPA 
# 
_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       
;GPTGTGESKCPLMVKVLDAVRGSPAINVAVHVFRKAADDTWEPFASGKTSESGELHGLTTEEEFVEGIYKVEIDTKSYWK
ALGISPFHEHAEVVFTANDSGPRRYTIAALLSPYSYSTTAVVTNPKE
;
_entity_poly.pdbx_seq_one_letter_code_can   
;GPTGTGESKCPLMVKVLDAVRGSPAINVAVHVFRKAADDTWEPFASGKTSESGELHGLTTEEEFVEGIYKVEIDTKSYWK
ALGISPFHEHAEVVFTANDSGPRRYTIAALLSPYSYSTTAVVTNPKE
;
_entity_poly.pdbx_strand_id                 A,B 
_entity_poly.pdbx_target_identifier         ? 
# 
loop_
_pdbx_entity_nonpoly.entity_id 
_pdbx_entity_nonpoly.name 
_pdbx_entity_nonpoly.comp_id 
2 1,2-ETHANEDIOL                                       EDO   
3 '2-[(2-chlorophenyl)methoxyiminomethyl]benzoic acid' A1ICF 
4 GLYCEROL                                             GOL   
5 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   THR n 
1 4   GLY n 
1 5   THR n 
1 6   GLY n 
1 7   GLU n 
1 8   SER n 
1 9   LYS n 
1 10  CYS n 
1 11  PRO n 
1 12  LEU n 
1 13  MET n 
1 14  VAL n 
1 15  LYS n 
1 16  VAL n 
1 17  LEU n 
1 18  ASP n 
1 19  ALA n 
1 20  VAL n 
1 21  ARG n 
1 22  GLY n 
1 23  SER n 
1 24  PRO n 
1 25  ALA n 
1 26  ILE n 
1 27  ASN n 
1 28  VAL n 
1 29  ALA n 
1 30  VAL n 
1 31  HIS n 
1 32  VAL n 
1 33  PHE n 
1 34  ARG n 
1 35  LYS n 
1 36  ALA n 
1 37  ALA n 
1 38  ASP n 
1 39  ASP n 
1 40  THR n 
1 41  TRP n 
1 42  GLU n 
1 43  PRO n 
1 44  PHE n 
1 45  ALA n 
1 46  SER n 
1 47  GLY n 
1 48  LYS n 
1 49  THR n 
1 50  SER n 
1 51  GLU n 
1 52  SER n 
1 53  GLY n 
1 54  GLU n 
1 55  LEU n 
1 56  HIS n 
1 57  GLY n 
1 58  LEU n 
1 59  THR n 
1 60  THR n 
1 61  GLU n 
1 62  GLU n 
1 63  GLU n 
1 64  PHE n 
1 65  VAL n 
1 66  GLU n 
1 67  GLY n 
1 68  ILE n 
1 69  TYR n 
1 70  LYS n 
1 71  VAL n 
1 72  GLU n 
1 73  ILE n 
1 74  ASP n 
1 75  THR n 
1 76  LYS n 
1 77  SER n 
1 78  TYR n 
1 79  TRP n 
1 80  LYS n 
1 81  ALA n 
1 82  LEU n 
1 83  GLY n 
1 84  ILE n 
1 85  SER n 
1 86  PRO n 
1 87  PHE n 
1 88  HIS n 
1 89  GLU n 
1 90  HIS n 
1 91  ALA n 
1 92  GLU n 
1 93  VAL n 
1 94  VAL n 
1 95  PHE n 
1 96  THR n 
1 97  ALA n 
1 98  ASN n 
1 99  ASP n 
1 100 SER n 
1 101 GLY n 
1 102 PRO n 
1 103 ARG n 
1 104 ARG n 
1 105 TYR n 
1 106 THR n 
1 107 ILE n 
1 108 ALA n 
1 109 ALA n 
1 110 LEU n 
1 111 LEU n 
1 112 SER n 
1 113 PRO n 
1 114 TYR n 
1 115 SER n 
1 116 TYR n 
1 117 SER n 
1 118 THR n 
1 119 THR n 
1 120 ALA n 
1 121 VAL n 
1 122 VAL n 
1 123 THR n 
1 124 ASN n 
1 125 PRO n 
1 126 LYS n 
1 127 GLU n 
# 
_entity_src_gen.entity_id                          1 
_entity_src_gen.pdbx_src_id                        1 
_entity_src_gen.pdbx_alt_source_flag               sample 
_entity_src_gen.pdbx_seq_type                      'Biological sequence' 
_entity_src_gen.pdbx_beg_seq_num                   1 
_entity_src_gen.pdbx_end_seq_num                   127 
_entity_src_gen.gene_src_common_name               human 
_entity_src_gen.gene_src_genus                     ? 
_entity_src_gen.pdbx_gene_src_gene                 'TTR, PALB' 
_entity_src_gen.gene_src_species                   ? 
_entity_src_gen.gene_src_strain                    ? 
_entity_src_gen.gene_src_tissue                    ? 
_entity_src_gen.gene_src_tissue_fraction           ? 
_entity_src_gen.gene_src_details                   ? 
_entity_src_gen.pdbx_gene_src_fragment             ? 
_entity_src_gen.pdbx_gene_src_scientific_name      'Homo sapiens' 
_entity_src_gen.pdbx_gene_src_ncbi_taxonomy_id     9606 
_entity_src_gen.pdbx_gene_src_variant              ? 
_entity_src_gen.pdbx_gene_src_cell_line            ? 
_entity_src_gen.pdbx_gene_src_atcc                 ? 
_entity_src_gen.pdbx_gene_src_organ                ? 
_entity_src_gen.pdbx_gene_src_organelle            ? 
_entity_src_gen.pdbx_gene_src_cell                 ? 
_entity_src_gen.pdbx_gene_src_cellular_location    ? 
_entity_src_gen.host_org_common_name               ? 
_entity_src_gen.pdbx_host_org_scientific_name      'Escherichia coli' 
_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 
A1ICF non-polymer         . '2-[(2-chlorophenyl)methoxyiminomethyl]benzoic acid' 
'(E)-2-((((2-chlorobenzyl)oxy)imino)methyl)benzoic acid' 'C15 H12 Cl N O3' 289.714 
ALA   'L-peptide linking' y ALANINE                                              ? 'C3 H7 N O2'      89.093  
ARG   'L-peptide linking' y ARGININE                                             ? 'C6 H15 N4 O2 1'  175.209 
ASN   'L-peptide linking' y ASPARAGINE                                           ? 'C4 H8 N2 O3'     132.118 
ASP   'L-peptide linking' y 'ASPARTIC ACID'                                      ? 'C4 H7 N O4'      133.103 
CYS   'L-peptide linking' y CYSTEINE                                             ? 'C3 H7 N O2 S'    121.158 
EDO   non-polymer         . 1,2-ETHANEDIOL                                       'ETHYLENE GLYCOL' 'C2 H6 O2'        62.068  
GLU   'L-peptide linking' y 'GLUTAMIC ACID'                                      ? 'C5 H9 N O4'      147.129 
GLY   'peptide linking'   y GLYCINE                                              ? 'C2 H5 N O2'      75.067  
GOL   non-polymer         . GLYCEROL                                             'GLYCERIN; PROPANE-1,2,3-TRIOL' 'C3 H8 O3'        
92.094  
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   THR 3   3   ?   ?   ?   A . n 
A 1 4   GLY 4   4   ?   ?   ?   A . n 
A 1 5   THR 5   5   ?   ?   ?   A . n 
A 1 6   GLY 6   6   ?   ?   ?   A . n 
A 1 7   GLU 7   7   ?   ?   ?   A . n 
A 1 8   SER 8   8   ?   ?   ?   A . n 
A 1 9   LYS 9   9   9   LYS LYS A . n 
A 1 10  CYS 10  10  10  CYS CYS A . n 
A 1 11  PRO 11  11  11  PRO PRO A . n 
A 1 12  LEU 12  12  12  LEU LEU A . n 
A 1 13  MET 13  13  13  MET MET A . n 
A 1 14  VAL 14  14  14  VAL VAL A . n 
A 1 15  LYS 15  15  15  LYS LYS A . n 
A 1 16  VAL 16  16  16  VAL VAL A . n 
A 1 17  LEU 17  17  17  LEU LEU A . n 
A 1 18  ASP 18  18  18  ASP ASP A . n 
A 1 19  ALA 19  19  19  ALA ALA A . n 
A 1 20  VAL 20  20  20  VAL VAL A . n 
A 1 21  ARG 21  21  21  ARG ARG A . n 
A 1 22  GLY 22  22  22  GLY GLY A . n 
A 1 23  SER 23  23  23  SER SER A . n 
A 1 24  PRO 24  24  24  PRO PRO A . n 
A 1 25  ALA 25  25  25  ALA ALA A . n 
A 1 26  ILE 26  26  26  ILE ILE A . n 
A 1 27  ASN 27  27  27  ASN ASN A . n 
A 1 28  VAL 28  28  28  VAL VAL A . n 
A 1 29  ALA 29  29  29  ALA ALA A . n 
A 1 30  VAL 30  30  30  VAL VAL A . n 
A 1 31  HIS 31  31  31  HIS HIS A . n 
A 1 32  VAL 32  32  32  VAL VAL A . n 
A 1 33  PHE 33  33  33  PHE PHE A . n 
A 1 34  ARG 34  34  34  ARG ARG A . n 
A 1 35  LYS 35  35  35  LYS LYS A . n 
A 1 36  ALA 36  36  36  ALA ALA A . n 
A 1 37  ALA 37  37  37  ALA ALA A . n 
A 1 38  ASP 38  38  38  ASP ASP A . n 
A 1 39  ASP 39  39  39  ASP ASP A . n 
A 1 40  THR 40  40  40  THR THR A . n 
A 1 41  TRP 41  41  41  TRP TRP A . n 
A 1 42  GLU 42  42  42  GLU GLU A . n 
A 1 43  PRO 43  43  43  PRO PRO A . n 
A 1 44  PHE 44  44  44  PHE PHE A . n 
A 1 45  ALA 45  45  45  ALA ALA A . n 
A 1 46  SER 46  46  46  SER SER A . n 
A 1 47  GLY 47  47  47  GLY GLY A . n 
A 1 48  LYS 48  48  48  LYS LYS A . n 
A 1 49  THR 49  49  49  THR THR A . n 
A 1 50  SER 50  50  50  SER SER A . n 
A 1 51  GLU 51  51  51  GLU GLU A . n 
A 1 52  SER 52  52  52  SER SER A . n 
A 1 53  GLY 53  53  53  GLY GLY A . n 
A 1 54  GLU 54  54  54  GLU GLU A . n 
A 1 55  LEU 55  55  55  LEU LEU A . n 
A 1 56  HIS 56  56  56  HIS HIS A . n 
A 1 57  GLY 57  57  57  GLY GLY A . n 
A 1 58  LEU 58  58  58  LEU LEU A . n 
A 1 59  THR 59  59  59  THR THR A . n 
A 1 60  THR 60  60  60  THR THR A . n 
A 1 61  GLU 61  61  61  GLU GLU A . n 
A 1 62  GLU 62  62  62  GLU GLU A . n 
A 1 63  GLU 63  63  63  GLU GLU A . n 
A 1 64  PHE 64  64  64  PHE PHE A . n 
A 1 65  VAL 65  65  65  VAL VAL A . n 
A 1 66  GLU 66  66  66  GLU GLU A . n 
A 1 67  GLY 67  67  67  GLY GLY A . n 
A 1 68  ILE 68  68  68  ILE ILE A . n 
A 1 69  TYR 69  69  69  TYR TYR A . n 
A 1 70  LYS 70  70  70  LYS LYS A . n 
A 1 71  VAL 71  71  71  VAL VAL A . n 
A 1 72  GLU 72  72  72  GLU GLU A . n 
A 1 73  ILE 73  73  73  ILE ILE A . n 
A 1 74  ASP 74  74  74  ASP ASP A . n 
A 1 75  THR 75  75  75  THR THR A . n 
A 1 76  LYS 76  76  76  LYS LYS A . n 
A 1 77  SER 77  77  77  SER SER A . n 
A 1 78  TYR 78  78  78  TYR TYR A . n 
A 1 79  TRP 79  79  79  TRP TRP A . n 
A 1 80  LYS 80  80  80  LYS LYS A . n 
A 1 81  ALA 81  81  81  ALA ALA A . n 
A 1 82  LEU 82  82  82  LEU LEU A . n 
A 1 83  GLY 83  83  83  GLY GLY A . n 
A 1 84  ILE 84  84  84  ILE ILE A . n 
A 1 85  SER 85  85  85  SER SER A . n 
A 1 86  PRO 86  86  86  PRO PRO A . n 
A 1 87  PHE 87  87  87  PHE PHE A . n 
A 1 88  HIS 88  88  88  HIS HIS A . n 
A 1 89  GLU 89  89  89  GLU GLU A . n 
A 1 90  HIS 90  90  90  HIS HIS A . n 
A 1 91  ALA 91  91  91  ALA ALA A . n 
A 1 92  GLU 92  92  92  GLU GLU A . n 
A 1 93  VAL 93  93  93  VAL VAL A . n 
A 1 94  VAL 94  94  94  VAL VAL A . n 
A 1 95  PHE 95  95  95  PHE PHE A . n 
A 1 96  THR 96  96  96  THR THR A . n 
A 1 97  ALA 97  97  97  ALA ALA A . n 
A 1 98  ASN 98  98  98  ASN ASN A . n 
A 1 99  ASP 99  99  99  ASP ASP A . n 
A 1 100 SER 100 100 100 SER SER A . n 
A 1 101 GLY 101 101 101 GLY GLY A . n 
A 1 102 PRO 102 102 102 PRO PRO A . n 
A 1 103 ARG 103 103 103 ARG ARG A . n 
A 1 104 ARG 104 104 104 ARG ARG A . n 
A 1 105 TYR 105 105 105 TYR TYR A . n 
A 1 106 THR 106 106 106 THR THR A . n 
A 1 107 ILE 107 107 107 ILE ILE A . n 
A 1 108 ALA 108 108 108 ALA ALA A . n 
A 1 109 ALA 109 109 109 ALA ALA A . n 
A 1 110 LEU 110 110 110 LEU LEU A . n 
A 1 111 LEU 111 111 111 LEU LEU A . n 
A 1 112 SER 112 112 112 SER SER A . n 
A 1 113 PRO 113 113 113 PRO PRO A . n 
A 1 114 TYR 114 114 114 TYR TYR A . n 
A 1 115 SER 115 115 115 SER SER A . n 
A 1 116 TYR 116 116 116 TYR TYR A . n 
A 1 117 SER 117 117 117 SER SER A . n 
A 1 118 THR 118 118 118 THR THR A . n 
A 1 119 THR 119 119 119 THR THR A . n 
A 1 120 ALA 120 120 120 ALA ALA A . n 
A 1 121 VAL 121 121 121 VAL VAL A . n 
A 1 122 VAL 122 122 122 VAL VAL A . n 
A 1 123 THR 123 123 123 THR THR A . n 
A 1 124 ASN 124 124 124 ASN ASN A . n 
A 1 125 PRO 125 125 125 PRO PRO A . n 
A 1 126 LYS 126 126 ?   ?   ?   A . n 
A 1 127 GLU 127 127 ?   ?   ?   A . n 
B 1 1   GLY 1   1   ?   ?   ?   B . n 
B 1 2   PRO 2   2   ?   ?   ?   B . n 
B 1 3   THR 3   3   ?   ?   ?   B . n 
B 1 4   GLY 4   4   ?   ?   ?   B . n 
B 1 5   THR 5   5   ?   ?   ?   B . n 
B 1 6   GLY 6   6   ?   ?   ?   B . n 
B 1 7   GLU 7   7   ?   ?   ?   B . n 
B 1 8   SER 8   8   ?   ?   ?   B . n 
B 1 9   LYS 9   9   9   LYS LYS B . n 
B 1 10  CYS 10  10  10  CYS CYS B . n 
B 1 11  PRO 11  11  11  PRO PRO B . n 
B 1 12  LEU 12  12  12  LEU LEU B . n 
B 1 13  MET 13  13  13  MET MET B . n 
B 1 14  VAL 14  14  14  VAL VAL B . n 
B 1 15  LYS 15  15  15  LYS LYS B . n 
B 1 16  VAL 16  16  16  VAL VAL B . n 
B 1 17  LEU 17  17  17  LEU LEU B . n 
B 1 18  ASP 18  18  18  ASP ASP B . n 
B 1 19  ALA 19  19  19  ALA ALA B . n 
B 1 20  VAL 20  20  20  VAL VAL B . n 
B 1 21  ARG 21  21  21  ARG ARG B . n 
B 1 22  GLY 22  22  22  GLY GLY B . n 
B 1 23  SER 23  23  23  SER SER B . n 
B 1 24  PRO 24  24  24  PRO PRO B . n 
B 1 25  ALA 25  25  25  ALA ALA B . n 
B 1 26  ILE 26  26  26  ILE ILE B . n 
B 1 27  ASN 27  27  27  ASN ASN B . n 
B 1 28  VAL 28  28  28  VAL VAL B . n 
B 1 29  ALA 29  29  29  ALA ALA B . n 
B 1 30  VAL 30  30  30  VAL VAL B . n 
B 1 31  HIS 31  31  31  HIS HIS B . n 
B 1 32  VAL 32  32  32  VAL VAL B . n 
B 1 33  PHE 33  33  33  PHE PHE B . n 
B 1 34  ARG 34  34  34  ARG ARG B . n 
B 1 35  LYS 35  35  35  LYS LYS B . n 
B 1 36  ALA 36  36  36  ALA ALA B . n 
B 1 37  ALA 37  37  37  ALA ALA B . n 
B 1 38  ASP 38  38  38  ASP ASP B . n 
B 1 39  ASP 39  39  39  ASP ASP B . n 
B 1 40  THR 40  40  40  THR THR B . n 
B 1 41  TRP 41  41  41  TRP TRP B . n 
B 1 42  GLU 42  42  42  GLU GLU B . n 
B 1 43  PRO 43  43  43  PRO PRO B . n 
B 1 44  PHE 44  44  44  PHE PHE B . n 
B 1 45  ALA 45  45  45  ALA ALA B . n 
B 1 46  SER 46  46  46  SER SER B . n 
B 1 47  GLY 47  47  47  GLY GLY B . n 
B 1 48  LYS 48  48  48  LYS LYS B . n 
B 1 49  THR 49  49  49  THR THR B . n 
B 1 50  SER 50  50  50  SER SER B . n 
B 1 51  GLU 51  51  51  GLU GLU B . n 
B 1 52  SER 52  52  52  SER SER B . n 
B 1 53  GLY 53  53  53  GLY GLY B . n 
B 1 54  GLU 54  54  54  GLU GLU B . n 
B 1 55  LEU 55  55  55  LEU LEU B . n 
B 1 56  HIS 56  56  56  HIS HIS B . n 
B 1 57  GLY 57  57  57  GLY GLY B . n 
B 1 58  LEU 58  58  58  LEU LEU B . n 
B 1 59  THR 59  59  59  THR THR B . n 
B 1 60  THR 60  60  60  THR THR B . n 
B 1 61  GLU 61  61  61  GLU GLU B . n 
B 1 62  GLU 62  62  62  GLU GLU B . n 
B 1 63  GLU 63  63  63  GLU GLU B . n 
B 1 64  PHE 64  64  64  PHE PHE B . n 
B 1 65  VAL 65  65  65  VAL VAL B . n 
B 1 66  GLU 66  66  66  GLU GLU B . n 
B 1 67  GLY 67  67  67  GLY GLY B . n 
B 1 68  ILE 68  68  68  ILE ILE B . n 
B 1 69  TYR 69  69  69  TYR TYR B . n 
B 1 70  LYS 70  70  70  LYS LYS B . n 
B 1 71  VAL 71  71  71  VAL VAL B . n 
B 1 72  GLU 72  72  72  GLU GLU B . n 
B 1 73  ILE 73  73  73  ILE ILE B . n 
B 1 74  ASP 74  74  74  ASP ASP B . n 
B 1 75  THR 75  75  75  THR THR B . n 
B 1 76  LYS 76  76  76  LYS LYS B . n 
B 1 77  SER 77  77  77  SER SER B . n 
B 1 78  TYR 78  78  78  TYR TYR B . n 
B 1 79  TRP 79  79  79  TRP TRP B . n 
B 1 80  LYS 80  80  80  LYS LYS B . n 
B 1 81  ALA 81  81  81  ALA ALA B . n 
B 1 82  LEU 82  82  82  LEU LEU B . n 
B 1 83  GLY 83  83  83  GLY GLY B . n 
B 1 84  ILE 84  84  84  ILE ILE B . n 
B 1 85  SER 85  85  85  SER SER B . n 
B 1 86  PRO 86  86  86  PRO PRO B . n 
B 1 87  PHE 87  87  87  PHE PHE B . n 
B 1 88  HIS 88  88  88  HIS HIS B . n 
B 1 89  GLU 89  89  89  GLU GLU B . n 
B 1 90  HIS 90  90  90  HIS HIS B . n 
B 1 91  ALA 91  91  91  ALA ALA B . n 
B 1 92  GLU 92  92  92  GLU GLU B . n 
B 1 93  VAL 93  93  93  VAL VAL B . n 
B 1 94  VAL 94  94  94  VAL VAL B . n 
B 1 95  PHE 95  95  95  PHE PHE B . n 
B 1 96  THR 96  96  96  THR THR B . n 
B 1 97  ALA 97  97  97  ALA ALA B . n 
B 1 98  ASN 98  98  98  ASN ASN B . n 
B 1 99  ASP 99  99  99  ASP ASP B . n 
B 1 100 SER 100 100 100 SER SER B . n 
B 1 101 GLY 101 101 101 GLY GLY B . n 
B 1 102 PRO 102 102 102 PRO PRO B . n 
B 1 103 ARG 103 103 103 ARG ARG B . n 
B 1 104 ARG 104 104 104 ARG ARG B . n 
B 1 105 TYR 105 105 105 TYR TYR B . n 
B 1 106 THR 106 106 106 THR THR B . n 
B 1 107 ILE 107 107 107 ILE ILE B . n 
B 1 108 ALA 108 108 108 ALA ALA B . n 
B 1 109 ALA 109 109 109 ALA ALA B . n 
B 1 110 LEU 110 110 110 LEU LEU B . n 
B 1 111 LEU 111 111 111 LEU LEU B . n 
B 1 112 SER 112 112 112 SER SER B . n 
B 1 113 PRO 113 113 113 PRO PRO B . n 
B 1 114 TYR 114 114 114 TYR TYR B . n 
B 1 115 SER 115 115 115 SER SER B . n 
B 1 116 TYR 116 116 116 TYR TYR B . n 
B 1 117 SER 117 117 117 SER SER B . n 
B 1 118 THR 118 118 118 THR THR B . n 
B 1 119 THR 119 119 119 THR THR B . n 
B 1 120 ALA 120 120 120 ALA ALA B . n 
B 1 121 VAL 121 121 121 VAL VAL B . n 
B 1 122 VAL 122 122 122 VAL VAL B . n 
B 1 123 THR 123 123 123 THR THR B . n 
B 1 124 ASN 124 124 124 ASN ASN B . n 
B 1 125 PRO 125 125 125 PRO PRO B . n 
B 1 126 LYS 126 126 ?   ?   ?   B . n 
B 1 127 GLU 127 127 ?   ?   ?   B . n 
# 
loop_
_pdbx_entity_instance_feature.ordinal 
_pdbx_entity_instance_feature.comp_id 
_pdbx_entity_instance_feature.asym_id 
_pdbx_entity_instance_feature.seq_num 
_pdbx_entity_instance_feature.auth_comp_id 
_pdbx_entity_instance_feature.auth_asym_id 
_pdbx_entity_instance_feature.auth_seq_num 
_pdbx_entity_instance_feature.feature_type 
_pdbx_entity_instance_feature.details 
1 EDO   ? ? EDO   ? ? 'SUBJECT OF INVESTIGATION' ? 
2 GOL   ? ? GOL   ? ? 'SUBJECT OF INVESTIGATION' ? 
3 A1ICF ? ? A1ICF ? ? 'SUBJECT OF INVESTIGATION' ? 
# 
loop_
_pdbx_nonpoly_scheme.asym_id 
_pdbx_nonpoly_scheme.entity_id 
_pdbx_nonpoly_scheme.mon_id 
_pdbx_nonpoly_scheme.ndb_seq_num 
_pdbx_nonpoly_scheme.pdb_seq_num 
_pdbx_nonpoly_scheme.auth_seq_num 
_pdbx_nonpoly_scheme.pdb_mon_id 
_pdbx_nonpoly_scheme.auth_mon_id 
_pdbx_nonpoly_scheme.pdb_strand_id 
_pdbx_nonpoly_scheme.pdb_ins_code 
C 2 EDO   1   201 1   EDO   EDO A . 
D 2 EDO   1   202 1   EDO   EDO A . 
E 3 A1ICF 1   203 1   A1ICF LC6 A . 
F 4 GOL   1   201 1   GOL   GOL B . 
G 3 A1ICF 1   202 1   A1ICF LC6 B . 
H 5 HOH   1   301 167 HOH   HOH A . 
H 5 HOH   2   302 303 HOH   HOH A . 
H 5 HOH   3   303 145 HOH   HOH A . 
H 5 HOH   4   304 173 HOH   HOH A . 
H 5 HOH   5   305 37  HOH   HOH A . 
H 5 HOH   6   306 25  HOH   HOH A . 
H 5 HOH   7   307 146 HOH   HOH A . 
H 5 HOH   8   308 266 HOH   HOH A . 
H 5 HOH   9   309 169 HOH   HOH A . 
H 5 HOH   10  310 316 HOH   HOH A . 
H 5 HOH   11  311 185 HOH   HOH A . 
H 5 HOH   12  312 107 HOH   HOH A . 
H 5 HOH   13  313 162 HOH   HOH A . 
H 5 HOH   14  314 143 HOH   HOH A . 
H 5 HOH   15  315 125 HOH   HOH A . 
H 5 HOH   16  316 138 HOH   HOH A . 
H 5 HOH   17  317 212 HOH   HOH A . 
H 5 HOH   18  318 256 HOH   HOH A . 
H 5 HOH   19  319 172 HOH   HOH A . 
H 5 HOH   20  320 141 HOH   HOH A . 
H 5 HOH   21  321 34  HOH   HOH A . 
H 5 HOH   22  322 96  HOH   HOH A . 
H 5 HOH   23  323 82  HOH   HOH A . 
H 5 HOH   24  324 114 HOH   HOH A . 
H 5 HOH   25  325 278 HOH   HOH A . 
H 5 HOH   26  326 54  HOH   HOH A . 
H 5 HOH   27  327 46  HOH   HOH A . 
H 5 HOH   28  328 38  HOH   HOH A . 
H 5 HOH   29  329 134 HOH   HOH A . 
H 5 HOH   30  330 148 HOH   HOH A . 
H 5 HOH   31  331 149 HOH   HOH A . 
H 5 HOH   32  332 273 HOH   HOH A . 
H 5 HOH   33  333 283 HOH   HOH A . 
H 5 HOH   34  334 28  HOH   HOH A . 
H 5 HOH   35  335 49  HOH   HOH A . 
H 5 HOH   36  336 173 HOH   HOH A . 
H 5 HOH   37  337 140 HOH   HOH A . 
H 5 HOH   38  338 155 HOH   HOH A . 
H 5 HOH   39  339 55  HOH   HOH A . 
H 5 HOH   40  340 250 HOH   HOH A . 
H 5 HOH   41  341 94  HOH   HOH A . 
H 5 HOH   42  342 32  HOH   HOH A . 
H 5 HOH   43  343 163 HOH   HOH A . 
H 5 HOH   44  344 136 HOH   HOH A . 
H 5 HOH   45  345 148 HOH   HOH A . 
H 5 HOH   46  346 48  HOH   HOH A . 
H 5 HOH   47  347 131 HOH   HOH A . 
H 5 HOH   48  348 164 HOH   HOH A . 
H 5 HOH   49  349 147 HOH   HOH A . 
H 5 HOH   50  350 163 HOH   HOH A . 
H 5 HOH   51  351 132 HOH   HOH A . 
H 5 HOH   52  352 169 HOH   HOH A . 
H 5 HOH   53  353 27  HOH   HOH A . 
H 5 HOH   54  354 117 HOH   HOH A . 
H 5 HOH   55  355 282 HOH   HOH A . 
H 5 HOH   56  356 240 HOH   HOH A . 
H 5 HOH   57  357 150 HOH   HOH A . 
H 5 HOH   58  358 130 HOH   HOH A . 
H 5 HOH   59  359 132 HOH   HOH A . 
H 5 HOH   60  360 139 HOH   HOH A . 
H 5 HOH   61  361 147 HOH   HOH A . 
H 5 HOH   62  362 72  HOH   HOH A . 
H 5 HOH   63  363 84  HOH   HOH A . 
H 5 HOH   64  364 116 HOH   HOH A . 
H 5 HOH   65  365 97  HOH   HOH A . 
H 5 HOH   66  366 144 HOH   HOH A . 
H 5 HOH   67  367 135 HOH   HOH A . 
H 5 HOH   68  368 133 HOH   HOH A . 
H 5 HOH   69  369 123 HOH   HOH A . 
H 5 HOH   70  370 71  HOH   HOH A . 
H 5 HOH   71  371 297 HOH   HOH A . 
H 5 HOH   72  372 22  HOH   HOH A . 
H 5 HOH   73  373 140 HOH   HOH A . 
H 5 HOH   74  374 166 HOH   HOH A . 
H 5 HOH   75  375 198 HOH   HOH A . 
H 5 HOH   76  376 274 HOH   HOH A . 
H 5 HOH   77  377 227 HOH   HOH A . 
H 5 HOH   78  378 23  HOH   HOH A . 
H 5 HOH   79  379 281 HOH   HOH A . 
H 5 HOH   80  380 261 HOH   HOH A . 
H 5 HOH   81  381 2   HOH   HOH A . 
H 5 HOH   82  382 85  HOH   HOH A . 
H 5 HOH   83  383 259 HOH   HOH A . 
H 5 HOH   84  384 219 HOH   HOH A . 
H 5 HOH   85  385 161 HOH   HOH A . 
H 5 HOH   86  386 156 HOH   HOH A . 
H 5 HOH   87  387 93  HOH   HOH A . 
H 5 HOH   88  388 299 HOH   HOH A . 
H 5 HOH   89  389 179 HOH   HOH A . 
H 5 HOH   90  390 92  HOH   HOH A . 
H 5 HOH   91  391 122 HOH   HOH A . 
H 5 HOH   92  392 178 HOH   HOH A . 
H 5 HOH   93  393 209 HOH   HOH A . 
H 5 HOH   94  394 170 HOH   HOH A . 
H 5 HOH   95  395 87  HOH   HOH A . 
H 5 HOH   96  396 211 HOH   HOH A . 
H 5 HOH   97  397 139 HOH   HOH A . 
H 5 HOH   98  398 176 HOH   HOH A . 
H 5 HOH   99  399 47  HOH   HOH A . 
H 5 HOH   100 400 77  HOH   HOH A . 
H 5 HOH   101 401 43  HOH   HOH A . 
H 5 HOH   102 402 318 HOH   HOH A . 
H 5 HOH   103 403 214 HOH   HOH A . 
H 5 HOH   104 404 174 HOH   HOH A . 
H 5 HOH   105 405 218 HOH   HOH A . 
H 5 HOH   106 406 201 HOH   HOH A . 
H 5 HOH   107 407 153 HOH   HOH A . 
H 5 HOH   108 408 76  HOH   HOH A . 
H 5 HOH   109 409 258 HOH   HOH A . 
H 5 HOH   110 410 52  HOH   HOH A . 
H 5 HOH   111 411 217 HOH   HOH A . 
H 5 HOH   112 412 307 HOH   HOH A . 
H 5 HOH   113 413 168 HOH   HOH A . 
H 5 HOH   114 414 136 HOH   HOH A . 
H 5 HOH   115 415 88  HOH   HOH A . 
H 5 HOH   116 416 151 HOH   HOH A . 
H 5 HOH   117 417 267 HOH   HOH A . 
H 5 HOH   118 418 165 HOH   HOH A . 
H 5 HOH   119 419 165 HOH   HOH A . 
H 5 HOH   120 420 238 HOH   HOH A . 
H 5 HOH   121 421 194 HOH   HOH A . 
H 5 HOH   122 422 9   HOH   HOH A . 
H 5 HOH   123 423 298 HOH   HOH A . 
H 5 HOH   124 424 63  HOH   HOH A . 
H 5 HOH   125 425 156 HOH   HOH A . 
H 5 HOH   126 426 12  HOH   HOH A . 
H 5 HOH   127 427 251 HOH   HOH A . 
H 5 HOH   128 428 304 HOH   HOH A . 
H 5 HOH   129 429 161 HOH   HOH A . 
H 5 HOH   130 430 215 HOH   HOH A . 
H 5 HOH   131 431 138 HOH   HOH A . 
H 5 HOH   132 432 182 HOH   HOH A . 
H 5 HOH   133 433 126 HOH   HOH A . 
H 5 HOH   134 434 225 HOH   HOH A . 
H 5 HOH   135 435 170 HOH   HOH A . 
H 5 HOH   136 436 295 HOH   HOH A . 
H 5 HOH   137 437 8   HOH   HOH A . 
H 5 HOH   138 438 213 HOH   HOH A . 
H 5 HOH   139 439 220 HOH   HOH A . 
H 5 HOH   140 440 124 HOH   HOH A . 
I 5 HOH   1   301 249 HOH   HOH B . 
I 5 HOH   2   302 319 HOH   HOH B . 
I 5 HOH   3   303 162 HOH   HOH B . 
I 5 HOH   4   304 31  HOH   HOH B . 
I 5 HOH   5   305 276 HOH   HOH B . 
I 5 HOH   6   306 187 HOH   HOH B . 
I 5 HOH   7   307 229 HOH   HOH B . 
I 5 HOH   8   308 66  HOH   HOH B . 
I 5 HOH   9   309 314 HOH   HOH B . 
I 5 HOH   10  310 308 HOH   HOH B . 
I 5 HOH   11  311 237 HOH   HOH B . 
I 5 HOH   12  312 129 HOH   HOH B . 
I 5 HOH   13  313 67  HOH   HOH B . 
I 5 HOH   14  314 133 HOH   HOH B . 
I 5 HOH   15  315 292 HOH   HOH B . 
I 5 HOH   16  316 272 HOH   HOH B . 
I 5 HOH   17  317 150 HOH   HOH B . 
I 5 HOH   18  318 17  HOH   HOH B . 
I 5 HOH   19  319 147 HOH   HOH B . 
I 5 HOH   20  320 120 HOH   HOH B . 
I 5 HOH   21  321 286 HOH   HOH B . 
I 5 HOH   22  322 132 HOH   HOH B . 
I 5 HOH   23  323 139 HOH   HOH B . 
I 5 HOH   24  324 83  HOH   HOH B . 
I 5 HOH   25  325 143 HOH   HOH B . 
I 5 HOH   26  326 148 HOH   HOH B . 
I 5 HOH   27  327 144 HOH   HOH B . 
I 5 HOH   28  328 305 HOH   HOH B . 
I 5 HOH   29  329 130 HOH   HOH B . 
I 5 HOH   30  330 175 HOH   HOH B . 
I 5 HOH   31  331 263 HOH   HOH B . 
I 5 HOH   32  332 7   HOH   HOH B . 
I 5 HOH   33  333 246 HOH   HOH B . 
I 5 HOH   34  334 284 HOH   HOH B . 
I 5 HOH   35  335 99  HOH   HOH B . 
I 5 HOH   36  336 221 HOH   HOH B . 
I 5 HOH   37  337 131 HOH   HOH B . 
I 5 HOH   38  338 102 HOH   HOH B . 
I 5 HOH   39  339 137 HOH   HOH B . 
I 5 HOH   40  340 135 HOH   HOH B . 
I 5 HOH   41  341 154 HOH   HOH B . 
I 5 HOH   42  342 109 HOH   HOH B . 
I 5 HOH   43  343 5   HOH   HOH B . 
I 5 HOH   44  344 131 HOH   HOH B . 
I 5 HOH   45  345 161 HOH   HOH B . 
I 5 HOH   46  346 150 HOH   HOH B . 
I 5 HOH   47  347 204 HOH   HOH B . 
I 5 HOH   48  348 45  HOH   HOH B . 
I 5 HOH   49  349 159 HOH   HOH B . 
I 5 HOH   50  350 112 HOH   HOH B . 
I 5 HOH   51  351 70  HOH   HOH B . 
I 5 HOH   52  352 59  HOH   HOH B . 
I 5 HOH   53  353 142 HOH   HOH B . 
I 5 HOH   54  354 146 HOH   HOH B . 
I 5 HOH   55  355 260 HOH   HOH B . 
I 5 HOH   56  356 61  HOH   HOH B . 
I 5 HOH   57  357 301 HOH   HOH B . 
I 5 HOH   58  358 98  HOH   HOH B . 
I 5 HOH   59  359 103 HOH   HOH B . 
I 5 HOH   60  360 108 HOH   HOH B . 
I 5 HOH   61  361 279 HOH   HOH B . 
I 5 HOH   62  362 16  HOH   HOH B . 
I 5 HOH   63  363 41  HOH   HOH B . 
I 5 HOH   64  364 15  HOH   HOH B . 
I 5 HOH   65  365 208 HOH   HOH B . 
I 5 HOH   66  366 79  HOH   HOH B . 
I 5 HOH   67  367 68  HOH   HOH B . 
I 5 HOH   68  368 130 HOH   HOH B . 
I 5 HOH   69  369 257 HOH   HOH B . 
I 5 HOH   70  370 111 HOH   HOH B . 
I 5 HOH   71  371 138 HOH   HOH B . 
I 5 HOH   72  372 142 HOH   HOH B . 
I 5 HOH   73  373 151 HOH   HOH B . 
I 5 HOH   74  374 10  HOH   HOH B . 
I 5 HOH   75  375 140 HOH   HOH B . 
I 5 HOH   76  376 24  HOH   HOH B . 
I 5 HOH   77  377 143 HOH   HOH B . 
I 5 HOH   78  378 158 HOH   HOH B . 
I 5 HOH   79  379 151 HOH   HOH B . 
I 5 HOH   80  380 56  HOH   HOH B . 
I 5 HOH   81  381 137 HOH   HOH B . 
I 5 HOH   82  382 89  HOH   HOH B . 
I 5 HOH   83  383 206 HOH   HOH B . 
I 5 HOH   84  384 39  HOH   HOH B . 
I 5 HOH   85  385 255 HOH   HOH B . 
I 5 HOH   86  386 285 HOH   HOH B . 
I 5 HOH   87  387 290 HOH   HOH B . 
I 5 HOH   88  388 291 HOH   HOH B . 
I 5 HOH   89  389 262 HOH   HOH B . 
I 5 HOH   90  390 180 HOH   HOH B . 
I 5 HOH   91  391 135 HOH   HOH B . 
I 5 HOH   92  392 11  HOH   HOH B . 
I 5 HOH   93  393 153 HOH   HOH B . 
I 5 HOH   94  394 145 HOH   HOH B . 
I 5 HOH   95  395 105 HOH   HOH B . 
I 5 HOH   96  396 288 HOH   HOH B . 
I 5 HOH   97  397 268 HOH   HOH B . 
I 5 HOH   98  398 235 HOH   HOH B . 
I 5 HOH   99  399 222 HOH   HOH B . 
I 5 HOH   100 400 36  HOH   HOH B . 
I 5 HOH   101 401 80  HOH   HOH B . 
I 5 HOH   102 402 270 HOH   HOH B . 
I 5 HOH   103 403 294 HOH   HOH B . 
I 5 HOH   104 404 200 HOH   HOH B . 
I 5 HOH   105 405 35  HOH   HOH B . 
I 5 HOH   106 406 271 HOH   HOH B . 
I 5 HOH   107 407 163 HOH   HOH B . 
I 5 HOH   108 408 216 HOH   HOH B . 
I 5 HOH   109 409 134 HOH   HOH B . 
I 5 HOH   110 410 168 HOH   HOH B . 
I 5 HOH   111 411 231 HOH   HOH B . 
I 5 HOH   112 412 310 HOH   HOH B . 
I 5 HOH   113 413 296 HOH   HOH B . 
I 5 HOH   114 414 166 HOH   HOH B . 
I 5 HOH   115 415 196 HOH   HOH B . 
I 5 HOH   116 416 242 HOH   HOH B . 
I 5 HOH   117 417 269 HOH   HOH B . 
I 5 HOH   118 418 232 HOH   HOH B . 
I 5 HOH   119 419 177 HOH   HOH B . 
I 5 HOH   120 420 6   HOH   HOH B . 
I 5 HOH   121 421 101 HOH   HOH B . 
I 5 HOH   122 422 90  HOH   HOH B . 
I 5 HOH   123 423 233 HOH   HOH B . 
I 5 HOH   124 424 91  HOH   HOH B . 
I 5 HOH   125 425 119 HOH   HOH B . 
I 5 HOH   126 426 100 HOH   HOH B . 
I 5 HOH   127 427 234 HOH   HOH B . 
I 5 HOH   128 428 280 HOH   HOH B . 
# 
loop_
_software.citation_id 
_software.classification 
_software.compiler_name 
_software.compiler_version 
_software.contact_author 
_software.contact_author_email 
_software.date 
_software.description 
_software.dependencies 
_software.hardware 
_software.language 
_software.location 
_software.mods 
_software.name 
_software.os 
_software.os_version 
_software.type 
_software.version 
_software.pdbx_ordinal 
? refinement       ? ? ? ? ? ? ? ? ? ? ? PHENIX ? ? ? 1.13-2998 1 
? 'data reduction' ? ? ? ? ? ? ? ? ? ? ? XDS    ? ? ? .         2 
? 'data scaling'   ? ? ? ? ? ? ? ? ? ? ? XSCALE ? ? ? .         3 
? phasing          ? ? ? ? ? ? ? ? ? ? ? MOLREP ? ? ? .         4 
# 
_cell.angle_alpha                  90.00 
_cell.angle_alpha_esd              ? 
_cell.angle_beta                   90.00 
_cell.angle_beta_esd               ? 
_cell.angle_gamma                  90.00 
_cell.angle_gamma_esd              ? 
_cell.entry_id                     9FF8 
_cell.details                      ? 
_cell.formula_units_Z              ? 
_cell.length_a                     42.981 
_cell.length_a_esd                 ? 
_cell.length_b                     85.247 
_cell.length_b_esd                 ? 
_cell.length_c                     64.004 
_cell.length_c_esd                 ? 
_cell.volume                       ? 
_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                         9FF8 
_symmetry.cell_setting                     ? 
_symmetry.Int_Tables_number                18 
_symmetry.space_group_name_Hall            ? 
_symmetry.space_group_name_H-M             'P 21 21 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                   9FF8 
_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             2.13 
_exptl_crystal.density_method               ? 
_exptl_crystal.density_percent_sol          42.19 
_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    
'Protein: 4.93 mg/mL, Tris pH 8.0, 150mM NaCl. Precipitant: 24% PEG 600, 0.2M imidazole malate pH 5.5.' 
_exptl_crystal_grow.pdbx_pH_range   ? 
_exptl_crystal_grow.temp            293 
# 
_diffrn.ambient_environment              ? 
_diffrn.ambient_temp                     100 
_diffrn.ambient_temp_details             ? 
_diffrn.ambient_temp_esd                 ? 
_diffrn.crystal_id                       1 
_diffrn.crystal_support                  ? 
_diffrn.crystal_treatment                ? 
_diffrn.details                          ? 
_diffrn.id                               1 
_diffrn.ambient_pressure                 ? 
_diffrn.ambient_pressure_esd             ? 
_diffrn.ambient_pressure_gt              ? 
_diffrn.ambient_pressure_lt              ? 
_diffrn.ambient_temp_gt                  ? 
_diffrn.ambient_temp_lt                  ? 
_diffrn.pdbx_serial_crystal_experiment   N 
# 
_diffrn_detector.details                      ? 
_diffrn_detector.detector                     PIXEL 
_diffrn_detector.diffrn_id                    1 
_diffrn_detector.type                         'DECTRIS EIGER X 9M' 
_diffrn_detector.area_resol_mean              ? 
_diffrn_detector.dtime                        ? 
_diffrn_detector.pdbx_frames_total            ? 
_diffrn_detector.pdbx_collection_time_total   ? 
_diffrn_detector.pdbx_collection_date         2023-06-28 
_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   0.980109 
_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                        'SOLEIL BEAMLINE PROXIMA 1' 
_diffrn_source.voltage                     ? 
_diffrn_source.take-off_angle              ? 
_diffrn_source.pdbx_wavelength_list        0.980109 
_diffrn_source.pdbx_wavelength             ? 
_diffrn_source.pdbx_synchrotron_beamline   'PROXIMA 1' 
_diffrn_source.pdbx_synchrotron_site       SOLEIL 
# 
_reflns.B_iso_Wilson_estimate                          ? 
_reflns.entry_id                                       9FF8 
_reflns.data_reduction_details                         ? 
_reflns.data_reduction_method                          ? 
_reflns.d_resolution_high                              1.42 
_reflns.d_resolution_low                               38.38 
_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                                     45148 
_reflns.observed_criterion                             ? 
_reflns.observed_criterion_F_max                       ? 
_reflns.observed_criterion_F_min                       ? 
_reflns.observed_criterion_I_max                       ? 
_reflns.observed_criterion_I_min                       ? 
_reflns.observed_criterion_sigma_F                     ? 
_reflns.observed_criterion_sigma_I                     ? 
_reflns.percent_possible_obs                           99.93 
_reflns.R_free_details                                 ? 
_reflns.Rmerge_F_all                                   ? 
_reflns.Rmerge_F_obs                                   ? 
_reflns.Friedel_coverage                               ? 
_reflns.number_gt                                      ? 
_reflns.threshold_expression                           ? 
_reflns.pdbx_redundancy                                6.5 
_reflns.pdbx_netI_over_av_sigmaI                       ? 
_reflns.pdbx_netI_over_sigmaI                          2.1 
_reflns.pdbx_res_netI_over_av_sigmaI_2                 ? 
_reflns.pdbx_res_netI_over_sigmaI_2                    ? 
_reflns.pdbx_chi_squared                               ? 
_reflns.pdbx_scaling_rejects                           ? 
_reflns.pdbx_d_res_high_opt                            ? 
_reflns.pdbx_d_res_low_opt                             ? 
_reflns.pdbx_d_res_opt_method                          ? 
_reflns.phase_calculation_details                      ? 
_reflns.pdbx_Rrim_I_all                                ? 
_reflns.pdbx_Rpim_I_all                                ? 
_reflns.pdbx_d_opt                                     ? 
_reflns.pdbx_number_measured_all                       ? 
_reflns.pdbx_diffrn_id                                 1 
_reflns.pdbx_ordinal                                   1 
_reflns.pdbx_CC_half                                   0.99 
_reflns.pdbx_CC_star                                   ? 
_reflns.pdbx_R_split                                   ? 
_reflns.pdbx_Rmerge_I_obs                              ? 
_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                                    1.42 
_reflns_shell.d_res_low                                     1.45 
_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                             42871 
_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                                  0.96 
_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                               ? 
_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                                 9FF8 
_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                            1.42 
_refine.ls_d_res_low                             38.38 
_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                     45148 
_refine.ls_number_reflns_R_free                  ? 
_refine.ls_number_reflns_R_work                  ? 
_refine.ls_number_restraints                     ? 
_refine.ls_percent_reflns_obs                    99.93 
_refine.ls_percent_reflns_R_free                 ? 
_refine.ls_R_factor_all                          ? 
_refine.ls_R_factor_obs                          ? 
_refine.ls_R_factor_R_free                       0.2138 
_refine.ls_R_factor_R_free_error                 ? 
_refine.ls_R_factor_R_free_error_details         ? 
_refine.ls_R_factor_R_work                       ? 
_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                    ? 
_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                          ? 
_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       ? 
_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             ? 
_refine.pdbx_solvent_ion_probe_radii             ? 
_refine.pdbx_solvent_shrinkage_radii             ? 
_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                 ? 
_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                            ? 
_refine.overall_SU_R_Cruickshank_DPI             ? 
_refine.overall_SU_R_free                        ? 
_refine.overall_FOM_free_R_set                   ? 
_refine.overall_FOM_work_R_set                   ? 
_refine.pdbx_average_fsc_overall                 ? 
_refine.pdbx_average_fsc_work                    ? 
_refine.pdbx_average_fsc_free                    ? 
# 
_refine_hist.pdbx_refine_id                   'X-RAY DIFFRACTION' 
_refine_hist.cycle_id                         LAST 
_refine_hist.pdbx_number_atoms_protein        1811 
_refine_hist.pdbx_number_atoms_nucleic_acid   0 
_refine_hist.pdbx_number_atoms_ligand         54 
_refine_hist.number_atoms_solvent             268 
_refine_hist.number_atoms_total               2133 
_refine_hist.d_res_high                       1.42 
_refine_hist.d_res_low                        38.38 
# 
_struct.entry_id                     9FF8 
_struct.title                        
'Human transthyretin (TTR) in complex with (E)-2-((((2-chlorobenzyl)oxy)imino)methyl)benzoic acid (Lic166)' 
_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        9FF8 
_struct_keywords.text            'TTR, fibril-inhibitors, Lic166-TTR crystal complex, PROTEIN TRANSPORT' 
_struct_keywords.pdbx_keywords   'PROTEIN TRANSPORT' 
# 
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 1 ? 
C N N 2 ? 
D N N 2 ? 
E N N 3 ? 
F N N 4 ? 
G N N 3 ? 
H N N 5 ? 
I N N 5 ? 
# 
_struct_ref.id                         1 
_struct_ref.db_name                    UNP 
_struct_ref.db_code                    TTHY_HUMAN 
_struct_ref.pdbx_db_accession          P02766 
_struct_ref.pdbx_db_isoform            ? 
_struct_ref.entity_id                  1 
_struct_ref.pdbx_seq_one_letter_code   
;GPTGTGESKCPLMVKVLDAVRGSPAINVAVHVFRKAADDTWEPFASGKTSESGELHGLTTEEEFVEGIYKVEIDTKSYWK
ALGISPFHEHAEVVFTANDSGPRRYTIAALLSPYSYSTTAVVTNPKE
;
_struct_ref.pdbx_align_begin           21 
# 
loop_
_struct_ref_seq.align_id 
_struct_ref_seq.ref_id 
_struct_ref_seq.pdbx_PDB_id_code 
_struct_ref_seq.pdbx_strand_id 
_struct_ref_seq.seq_align_beg 
_struct_ref_seq.pdbx_seq_align_beg_ins_code 
_struct_ref_seq.seq_align_end 
_struct_ref_seq.pdbx_seq_align_end_ins_code 
_struct_ref_seq.pdbx_db_accession 
_struct_ref_seq.db_align_beg 
_struct_ref_seq.pdbx_db_align_beg_ins_code 
_struct_ref_seq.db_align_end 
_struct_ref_seq.pdbx_db_align_end_ins_code 
_struct_ref_seq.pdbx_auth_seq_align_beg 
_struct_ref_seq.pdbx_auth_seq_align_end 
1 1 9FF8 A 1 ? 127 ? P02766 21 ? 147 ? 1 127 
2 1 9FF8 B 1 ? 127 ? P02766 21 ? 147 ? 1 127 
# 
_pdbx_struct_assembly.id                   1 
_pdbx_struct_assembly.details              author_defined_assembly 
_pdbx_struct_assembly.method_details       ? 
_pdbx_struct_assembly.oligomeric_details   dimeric 
_pdbx_struct_assembly.oligomeric_count     2 
# 
loop_
_pdbx_struct_assembly_prop.biol_id 
_pdbx_struct_assembly_prop.type 
_pdbx_struct_assembly_prop.value 
_pdbx_struct_assembly_prop.details 
1 'ABSA (A^2)' 2940  ? 
1 MORE         -8    ? 
1 'SSA (A^2)'  11680 ? 
# 
_pdbx_struct_assembly_gen.assembly_id       1 
_pdbx_struct_assembly_gen.oper_expression   1 
_pdbx_struct_assembly_gen.asym_id_list      A,B,C,D,E,F,G,H,I 
# 
_pdbx_struct_assembly_auth_evidence.id                     1 
_pdbx_struct_assembly_auth_evidence.assembly_id            1 
_pdbx_struct_assembly_auth_evidence.experimental_support   'mass spectrometry' 
_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 ASP A 74 ? LYS A 80 ? ASP A 74 LYS A 80 1 ? 7 
HELX_P HELX_P2 AA2 ASP B 74 ? LEU B 82 ? ASP B 74 LEU B 82 1 ? 9 
# 
_struct_conf_type.id          HELX_P 
_struct_conf_type.criteria    ? 
_struct_conf_type.reference   ? 
# 
loop_
_struct_sheet.id 
_struct_sheet.type 
_struct_sheet.number_strands 
_struct_sheet.details 
AA1 ? 8 ? 
AA2 ? 8 ? 
AA3 ? 8 ? 
# 
loop_
_struct_sheet_order.sheet_id 
_struct_sheet_order.range_id_1 
_struct_sheet_order.range_id_2 
_struct_sheet_order.offset 
_struct_sheet_order.sense 
AA1 1 2 ? anti-parallel 
AA1 2 3 ? parallel      
AA1 3 4 ? anti-parallel 
AA1 4 5 ? anti-parallel 
AA1 5 6 ? anti-parallel 
AA1 6 7 ? parallel      
AA1 7 8 ? anti-parallel 
AA2 1 2 ? anti-parallel 
AA2 2 3 ? parallel      
AA2 3 4 ? anti-parallel 
AA2 4 5 ? anti-parallel 
AA2 5 6 ? anti-parallel 
AA2 6 7 ? parallel      
AA2 7 8 ? anti-parallel 
AA3 1 2 ? anti-parallel 
AA3 2 3 ? anti-parallel 
AA3 3 4 ? anti-parallel 
AA3 4 5 ? anti-parallel 
AA3 5 6 ? anti-parallel 
AA3 6 7 ? anti-parallel 
AA3 7 8 ? anti-parallel 
# 
loop_
_struct_sheet_range.sheet_id 
_struct_sheet_range.id 
_struct_sheet_range.beg_label_comp_id 
_struct_sheet_range.beg_label_asym_id 
_struct_sheet_range.beg_label_seq_id 
_struct_sheet_range.pdbx_beg_PDB_ins_code 
_struct_sheet_range.end_label_comp_id 
_struct_sheet_range.end_label_asym_id 
_struct_sheet_range.end_label_seq_id 
_struct_sheet_range.pdbx_end_PDB_ins_code 
_struct_sheet_range.beg_auth_comp_id 
_struct_sheet_range.beg_auth_asym_id 
_struct_sheet_range.beg_auth_seq_id 
_struct_sheet_range.end_auth_comp_id 
_struct_sheet_range.end_auth_asym_id 
_struct_sheet_range.end_auth_seq_id 
AA1 1 SER A 23  ? PRO A 24  ? SER A 23  PRO A 24  
AA1 2 LEU A 12  ? ASP A 18  ? LEU A 12  ASP A 18  
AA1 3 ARG A 104 ? SER A 112 ? ARG A 104 SER A 112 
AA1 4 SER A 115 ? THR A 123 ? SER A 115 THR A 123 
AA1 5 SER B 115 ? THR B 123 ? SER B 115 THR B 123 
AA1 6 ARG B 104 ? LEU B 111 ? ARG B 104 LEU B 111 
AA1 7 LEU B 12  ? ASP B 18  ? LEU B 12  ASP B 18  
AA1 8 SER B 23  ? PRO B 24  ? SER B 23  PRO B 24  
AA2 1 GLU A 54  ? LEU A 55  ? GLU A 54  LEU A 55  
AA2 2 LEU A 12  ? ASP A 18  ? LEU A 12  ASP A 18  
AA2 3 ARG A 104 ? SER A 112 ? ARG A 104 SER A 112 
AA2 4 SER A 115 ? THR A 123 ? SER A 115 THR A 123 
AA2 5 SER B 115 ? THR B 123 ? SER B 115 THR B 123 
AA2 6 ARG B 104 ? LEU B 111 ? ARG B 104 LEU B 111 
AA2 7 LEU B 12  ? ASP B 18  ? LEU B 12  ASP B 18  
AA2 8 GLU B 54  ? LEU B 55  ? GLU B 54  LEU B 55  
AA3 1 TRP A 41  ? LYS A 48  ? TRP A 41  LYS A 48  
AA3 2 ALA A 29  ? LYS A 35  ? ALA A 29  LYS A 35  
AA3 3 GLY A 67  ? ILE A 73  ? GLY A 67  ILE A 73  
AA3 4 HIS A 88  ? ALA A 97  ? HIS A 88  ALA A 97  
AA3 5 HIS B 88  ? ALA B 97  ? HIS B 88  ALA B 97  
AA3 6 GLY B 67  ? ILE B 73  ? GLY B 67  ILE B 73  
AA3 7 ALA B 29  ? LYS B 35  ? ALA B 29  LYS B 35  
AA3 8 TRP B 41  ? LYS B 48  ? TRP B 41  LYS B 48  
# 
loop_
_pdbx_struct_sheet_hbond.sheet_id 
_pdbx_struct_sheet_hbond.range_id_1 
_pdbx_struct_sheet_hbond.range_id_2 
_pdbx_struct_sheet_hbond.range_1_label_atom_id 
_pdbx_struct_sheet_hbond.range_1_label_comp_id 
_pdbx_struct_sheet_hbond.range_1_label_asym_id 
_pdbx_struct_sheet_hbond.range_1_label_seq_id 
_pdbx_struct_sheet_hbond.range_1_PDB_ins_code 
_pdbx_struct_sheet_hbond.range_1_auth_atom_id 
_pdbx_struct_sheet_hbond.range_1_auth_comp_id 
_pdbx_struct_sheet_hbond.range_1_auth_asym_id 
_pdbx_struct_sheet_hbond.range_1_auth_seq_id 
_pdbx_struct_sheet_hbond.range_2_label_atom_id 
_pdbx_struct_sheet_hbond.range_2_label_comp_id 
_pdbx_struct_sheet_hbond.range_2_label_asym_id 
_pdbx_struct_sheet_hbond.range_2_label_seq_id 
_pdbx_struct_sheet_hbond.range_2_PDB_ins_code 
_pdbx_struct_sheet_hbond.range_2_auth_atom_id 
_pdbx_struct_sheet_hbond.range_2_auth_comp_id 
_pdbx_struct_sheet_hbond.range_2_auth_asym_id 
_pdbx_struct_sheet_hbond.range_2_auth_seq_id 
AA1 1 2 O SER A 23  ? O SER A 23  N ASP A 18  ? N ASP A 18  
AA1 2 3 N MET A 13  ? N MET A 13  O ILE A 107 ? O ILE A 107 
AA1 3 4 N LEU A 110 ? N LEU A 110 O SER A 117 ? O SER A 117 
AA1 4 5 N THR A 118 ? N THR A 118 O TYR B 116 ? O TYR B 116 
AA1 5 6 O SER B 117 ? O SER B 117 N LEU B 110 ? N LEU B 110 
AA1 6 7 O ILE B 107 ? O ILE B 107 N MET B 13  ? N MET B 13  
AA1 7 8 N ASP B 18  ? N ASP B 18  O SER B 23  ? O SER B 23  
AA2 1 2 O LEU A 55  ? O LEU A 55  N VAL A 14  ? N VAL A 14  
AA2 2 3 N MET A 13  ? N MET A 13  O ILE A 107 ? O ILE A 107 
AA2 3 4 N LEU A 110 ? N LEU A 110 O SER A 117 ? O SER A 117 
AA2 4 5 N THR A 118 ? N THR A 118 O TYR B 116 ? O TYR B 116 
AA2 5 6 O SER B 117 ? O SER B 117 N LEU B 110 ? N LEU B 110 
AA2 6 7 O ILE B 107 ? O ILE B 107 N MET B 13  ? N MET B 13  
AA2 7 8 N VAL B 14  ? N VAL B 14  O LEU B 55  ? O LEU B 55  
AA3 1 2 O ALA A 45  ? O ALA A 45  N VAL A 32  ? N VAL A 32  
AA3 2 3 N HIS A 31  ? N HIS A 31  O GLU A 72  ? O GLU A 72  
AA3 3 4 N ILE A 73  ? N ILE A 73  O ALA A 91  ? O ALA A 91  
AA3 4 5 N VAL A 94  ? N VAL A 94  O GLU B 89  ? O GLU B 89  
AA3 5 6 O ALA B 91  ? O ALA B 91  N ILE B 73  ? N ILE B 73  
AA3 6 7 O GLU B 72  ? O GLU B 72  N HIS B 31  ? N HIS B 31  
AA3 7 8 N VAL B 32  ? N VAL B 32  O ALA B 45  ? O ALA B 45  
# 
_pdbx_entry_details.entry_id                   9FF8 
_pdbx_entry_details.has_ligand_of_interest     Y 
_pdbx_entry_details.compound_details           ? 
_pdbx_entry_details.source_details             ? 
_pdbx_entry_details.nonpolymer_details         ? 
_pdbx_entry_details.sequence_details           ? 
_pdbx_entry_details.has_protein_modification   N 
# 
loop_
_pdbx_struct_special_symmetry.id 
_pdbx_struct_special_symmetry.PDB_model_num 
_pdbx_struct_special_symmetry.auth_asym_id 
_pdbx_struct_special_symmetry.auth_comp_id 
_pdbx_struct_special_symmetry.auth_seq_id 
_pdbx_struct_special_symmetry.PDB_ins_code 
_pdbx_struct_special_symmetry.label_asym_id 
_pdbx_struct_special_symmetry.label_comp_id 
_pdbx_struct_special_symmetry.label_seq_id 
1 1 A A1ICF 203 ? E A1ICF . 
2 1 A A1ICF 203 ? E A1ICF . 
3 1 B A1ICF 202 ? G A1ICF . 
4 1 B A1ICF 202 ? G A1ICF . 
# 
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 THR 3   ? A THR 3   
4  1 Y 1 A GLY 4   ? A GLY 4   
5  1 Y 1 A THR 5   ? A THR 5   
6  1 Y 1 A GLY 6   ? A GLY 6   
7  1 Y 1 A GLU 7   ? A GLU 7   
8  1 Y 1 A SER 8   ? A SER 8   
9  1 Y 1 A LYS 126 ? A LYS 126 
10 1 Y 1 A GLU 127 ? A GLU 127 
11 1 Y 1 B GLY 1   ? B GLY 1   
12 1 Y 1 B PRO 2   ? B PRO 2   
13 1 Y 1 B THR 3   ? B THR 3   
14 1 Y 1 B GLY 4   ? B GLY 4   
15 1 Y 1 B THR 5   ? B THR 5   
16 1 Y 1 B GLY 6   ? B GLY 6   
17 1 Y 1 B GLU 7   ? B GLU 7   
18 1 Y 1 B SER 8   ? B SER 8   
19 1 Y 1 B LYS 126 ? B LYS 126 
20 1 Y 1 B GLU 127 ? B GLU 127 
# 
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 
A1ICF C10  C  N N 1   
A1ICF C11  C  Y N 2   
A1ICF C12  C  Y N 3   
A1ICF C13  C  Y N 4   
A1ICF C14  C  Y N 5   
A1ICF C15  C  Y N 6   
A1ICF C16  C  Y N 7   
A1ICF C17  C  N N 8   
A1ICF C01  C  Y N 9   
A1ICF C02  C  Y N 10  
A1ICF C03  C  Y N 11  
A1ICF C04  C  Y N 12  
A1ICF C05  C  Y N 13  
A1ICF C06  C  Y N 14  
A1ICF C07  C  N N 15  
A1ICF N09  N  N N 16  
A1ICF O08  O  N N 17  
A1ICF O18  O  N N 18  
A1ICF O19  O  N N 19  
A1ICF CL20 CL N N 20  
A1ICF H3   H  N N 21  
A1ICF H4   H  N N 22  
A1ICF H5   H  N N 23  
A1ICF H6   H  N N 24  
A1ICF H7   H  N N 25  
A1ICF H8   H  N N 26  
A1ICF H9   H  N N 27  
A1ICF H10  H  N N 28  
A1ICF H11  H  N N 29  
A1ICF H12  H  N N 30  
A1ICF H14  H  N N 31  
A1ICF H1   H  N N 32  
ALA   N    N  N N 33  
ALA   CA   C  N S 34  
ALA   C    C  N N 35  
ALA   O    O  N N 36  
ALA   CB   C  N N 37  
ALA   OXT  O  N N 38  
ALA   H    H  N N 39  
ALA   H2   H  N N 40  
ALA   HA   H  N N 41  
ALA   HB1  H  N N 42  
ALA   HB2  H  N N 43  
ALA   HB3  H  N N 44  
ALA   HXT  H  N N 45  
ARG   N    N  N N 46  
ARG   CA   C  N S 47  
ARG   C    C  N N 48  
ARG   O    O  N N 49  
ARG   CB   C  N N 50  
ARG   CG   C  N N 51  
ARG   CD   C  N N 52  
ARG   NE   N  N N 53  
ARG   CZ   C  N N 54  
ARG   NH1  N  N N 55  
ARG   NH2  N  N N 56  
ARG   OXT  O  N N 57  
ARG   H    H  N N 58  
ARG   H2   H  N N 59  
ARG   HA   H  N N 60  
ARG   HB2  H  N N 61  
ARG   HB3  H  N N 62  
ARG   HG2  H  N N 63  
ARG   HG3  H  N N 64  
ARG   HD2  H  N N 65  
ARG   HD3  H  N N 66  
ARG   HE   H  N N 67  
ARG   HH11 H  N N 68  
ARG   HH12 H  N N 69  
ARG   HH21 H  N N 70  
ARG   HH22 H  N N 71  
ARG   HXT  H  N N 72  
ASN   N    N  N N 73  
ASN   CA   C  N S 74  
ASN   C    C  N N 75  
ASN   O    O  N N 76  
ASN   CB   C  N N 77  
ASN   CG   C  N N 78  
ASN   OD1  O  N N 79  
ASN   ND2  N  N N 80  
ASN   OXT  O  N N 81  
ASN   H    H  N N 82  
ASN   H2   H  N N 83  
ASN   HA   H  N N 84  
ASN   HB2  H  N N 85  
ASN   HB3  H  N N 86  
ASN   HD21 H  N N 87  
ASN   HD22 H  N N 88  
ASN   HXT  H  N N 89  
ASP   N    N  N N 90  
ASP   CA   C  N S 91  
ASP   C    C  N N 92  
ASP   O    O  N N 93  
ASP   CB   C  N N 94  
ASP   CG   C  N N 95  
ASP   OD1  O  N N 96  
ASP   OD2  O  N N 97  
ASP   OXT  O  N N 98  
ASP   H    H  N N 99  
ASP   H2   H  N N 100 
ASP   HA   H  N N 101 
ASP   HB2  H  N N 102 
ASP   HB3  H  N N 103 
ASP   HD2  H  N N 104 
ASP   HXT  H  N N 105 
CYS   N    N  N N 106 
CYS   CA   C  N R 107 
CYS   C    C  N N 108 
CYS   O    O  N N 109 
CYS   CB   C  N N 110 
CYS   SG   S  N N 111 
CYS   OXT  O  N N 112 
CYS   H    H  N N 113 
CYS   H2   H  N N 114 
CYS   HA   H  N N 115 
CYS   HB2  H  N N 116 
CYS   HB3  H  N N 117 
CYS   HG   H  N N 118 
CYS   HXT  H  N N 119 
EDO   C1   C  N N 120 
EDO   O1   O  N N 121 
EDO   C2   C  N N 122 
EDO   O2   O  N N 123 
EDO   H11  H  N N 124 
EDO   H12  H  N N 125 
EDO   HO1  H  N N 126 
EDO   H21  H  N N 127 
EDO   H22  H  N N 128 
EDO   HO2  H  N N 129 
GLU   N    N  N N 130 
GLU   CA   C  N S 131 
GLU   C    C  N N 132 
GLU   O    O  N N 133 
GLU   CB   C  N N 134 
GLU   CG   C  N N 135 
GLU   CD   C  N N 136 
GLU   OE1  O  N N 137 
GLU   OE2  O  N N 138 
GLU   OXT  O  N N 139 
GLU   H    H  N N 140 
GLU   H2   H  N N 141 
GLU   HA   H  N N 142 
GLU   HB2  H  N N 143 
GLU   HB3  H  N N 144 
GLU   HG2  H  N N 145 
GLU   HG3  H  N N 146 
GLU   HE2  H  N N 147 
GLU   HXT  H  N N 148 
GLY   N    N  N N 149 
GLY   CA   C  N N 150 
GLY   C    C  N N 151 
GLY   O    O  N N 152 
GLY   OXT  O  N N 153 
GLY   H    H  N N 154 
GLY   H2   H  N N 155 
GLY   HA2  H  N N 156 
GLY   HA3  H  N N 157 
GLY   HXT  H  N N 158 
GOL   C1   C  N N 159 
GOL   O1   O  N N 160 
GOL   C2   C  N N 161 
GOL   O2   O  N N 162 
GOL   C3   C  N N 163 
GOL   O3   O  N N 164 
GOL   H11  H  N N 165 
GOL   H12  H  N N 166 
GOL   HO1  H  N N 167 
GOL   H2   H  N N 168 
GOL   HO2  H  N N 169 
GOL   H31  H  N N 170 
GOL   H32  H  N N 171 
GOL   HO3  H  N N 172 
HIS   N    N  N N 173 
HIS   CA   C  N S 174 
HIS   C    C  N N 175 
HIS   O    O  N N 176 
HIS   CB   C  N N 177 
HIS   CG   C  Y N 178 
HIS   ND1  N  Y N 179 
HIS   CD2  C  Y N 180 
HIS   CE1  C  Y N 181 
HIS   NE2  N  Y N 182 
HIS   OXT  O  N N 183 
HIS   H    H  N N 184 
HIS   H2   H  N N 185 
HIS   HA   H  N N 186 
HIS   HB2  H  N N 187 
HIS   HB3  H  N N 188 
HIS   HD1  H  N N 189 
HIS   HD2  H  N N 190 
HIS   HE1  H  N N 191 
HIS   HE2  H  N N 192 
HIS   HXT  H  N N 193 
HOH   O    O  N N 194 
HOH   H1   H  N N 195 
HOH   H2   H  N N 196 
ILE   N    N  N N 197 
ILE   CA   C  N S 198 
ILE   C    C  N N 199 
ILE   O    O  N N 200 
ILE   CB   C  N S 201 
ILE   CG1  C  N N 202 
ILE   CG2  C  N N 203 
ILE   CD1  C  N N 204 
ILE   OXT  O  N N 205 
ILE   H    H  N N 206 
ILE   H2   H  N N 207 
ILE   HA   H  N N 208 
ILE   HB   H  N N 209 
ILE   HG12 H  N N 210 
ILE   HG13 H  N N 211 
ILE   HG21 H  N N 212 
ILE   HG22 H  N N 213 
ILE   HG23 H  N N 214 
ILE   HD11 H  N N 215 
ILE   HD12 H  N N 216 
ILE   HD13 H  N N 217 
ILE   HXT  H  N N 218 
LEU   N    N  N N 219 
LEU   CA   C  N S 220 
LEU   C    C  N N 221 
LEU   O    O  N N 222 
LEU   CB   C  N N 223 
LEU   CG   C  N N 224 
LEU   CD1  C  N N 225 
LEU   CD2  C  N N 226 
LEU   OXT  O  N N 227 
LEU   H    H  N N 228 
LEU   H2   H  N N 229 
LEU   HA   H  N N 230 
LEU   HB2  H  N N 231 
LEU   HB3  H  N N 232 
LEU   HG   H  N N 233 
LEU   HD11 H  N N 234 
LEU   HD12 H  N N 235 
LEU   HD13 H  N N 236 
LEU   HD21 H  N N 237 
LEU   HD22 H  N N 238 
LEU   HD23 H  N N 239 
LEU   HXT  H  N N 240 
LYS   N    N  N N 241 
LYS   CA   C  N S 242 
LYS   C    C  N N 243 
LYS   O    O  N N 244 
LYS   CB   C  N N 245 
LYS   CG   C  N N 246 
LYS   CD   C  N N 247 
LYS   CE   C  N N 248 
LYS   NZ   N  N N 249 
LYS   OXT  O  N N 250 
LYS   H    H  N N 251 
LYS   H2   H  N N 252 
LYS   HA   H  N N 253 
LYS   HB2  H  N N 254 
LYS   HB3  H  N N 255 
LYS   HG2  H  N N 256 
LYS   HG3  H  N N 257 
LYS   HD2  H  N N 258 
LYS   HD3  H  N N 259 
LYS   HE2  H  N N 260 
LYS   HE3  H  N N 261 
LYS   HZ1  H  N N 262 
LYS   HZ2  H  N N 263 
LYS   HZ3  H  N N 264 
LYS   HXT  H  N N 265 
MET   N    N  N N 266 
MET   CA   C  N S 267 
MET   C    C  N N 268 
MET   O    O  N N 269 
MET   CB   C  N N 270 
MET   CG   C  N N 271 
MET   SD   S  N N 272 
MET   CE   C  N N 273 
MET   OXT  O  N N 274 
MET   H    H  N N 275 
MET   H2   H  N N 276 
MET   HA   H  N N 277 
MET   HB2  H  N N 278 
MET   HB3  H  N N 279 
MET   HG2  H  N N 280 
MET   HG3  H  N N 281 
MET   HE1  H  N N 282 
MET   HE2  H  N N 283 
MET   HE3  H  N N 284 
MET   HXT  H  N N 285 
PHE   N    N  N N 286 
PHE   CA   C  N S 287 
PHE   C    C  N N 288 
PHE   O    O  N N 289 
PHE   CB   C  N N 290 
PHE   CG   C  Y N 291 
PHE   CD1  C  Y N 292 
PHE   CD2  C  Y N 293 
PHE   CE1  C  Y N 294 
PHE   CE2  C  Y N 295 
PHE   CZ   C  Y N 296 
PHE   OXT  O  N N 297 
PHE   H    H  N N 298 
PHE   H2   H  N N 299 
PHE   HA   H  N N 300 
PHE   HB2  H  N N 301 
PHE   HB3  H  N N 302 
PHE   HD1  H  N N 303 
PHE   HD2  H  N N 304 
PHE   HE1  H  N N 305 
PHE   HE2  H  N N 306 
PHE   HZ   H  N N 307 
PHE   HXT  H  N N 308 
PRO   N    N  N N 309 
PRO   CA   C  N S 310 
PRO   C    C  N N 311 
PRO   O    O  N N 312 
PRO   CB   C  N N 313 
PRO   CG   C  N N 314 
PRO   CD   C  N N 315 
PRO   OXT  O  N N 316 
PRO   H    H  N N 317 
PRO   HA   H  N N 318 
PRO   HB2  H  N N 319 
PRO   HB3  H  N N 320 
PRO   HG2  H  N N 321 
PRO   HG3  H  N N 322 
PRO   HD2  H  N N 323 
PRO   HD3  H  N N 324 
PRO   HXT  H  N N 325 
SER   N    N  N N 326 
SER   CA   C  N S 327 
SER   C    C  N N 328 
SER   O    O  N N 329 
SER   CB   C  N N 330 
SER   OG   O  N N 331 
SER   OXT  O  N N 332 
SER   H    H  N N 333 
SER   H2   H  N N 334 
SER   HA   H  N N 335 
SER   HB2  H  N N 336 
SER   HB3  H  N N 337 
SER   HG   H  N N 338 
SER   HXT  H  N N 339 
THR   N    N  N N 340 
THR   CA   C  N S 341 
THR   C    C  N N 342 
THR   O    O  N N 343 
THR   CB   C  N R 344 
THR   OG1  O  N N 345 
THR   CG2  C  N N 346 
THR   OXT  O  N N 347 
THR   H    H  N N 348 
THR   H2   H  N N 349 
THR   HA   H  N N 350 
THR   HB   H  N N 351 
THR   HG1  H  N N 352 
THR   HG21 H  N N 353 
THR   HG22 H  N N 354 
THR   HG23 H  N N 355 
THR   HXT  H  N N 356 
TRP   N    N  N N 357 
TRP   CA   C  N S 358 
TRP   C    C  N N 359 
TRP   O    O  N N 360 
TRP   CB   C  N N 361 
TRP   CG   C  Y N 362 
TRP   CD1  C  Y N 363 
TRP   CD2  C  Y N 364 
TRP   NE1  N  Y N 365 
TRP   CE2  C  Y N 366 
TRP   CE3  C  Y N 367 
TRP   CZ2  C  Y N 368 
TRP   CZ3  C  Y N 369 
TRP   CH2  C  Y N 370 
TRP   OXT  O  N N 371 
TRP   H    H  N N 372 
TRP   H2   H  N N 373 
TRP   HA   H  N N 374 
TRP   HB2  H  N N 375 
TRP   HB3  H  N N 376 
TRP   HD1  H  N N 377 
TRP   HE1  H  N N 378 
TRP   HE3  H  N N 379 
TRP   HZ2  H  N N 380 
TRP   HZ3  H  N N 381 
TRP   HH2  H  N N 382 
TRP   HXT  H  N N 383 
TYR   N    N  N N 384 
TYR   CA   C  N S 385 
TYR   C    C  N N 386 
TYR   O    O  N N 387 
TYR   CB   C  N N 388 
TYR   CG   C  Y N 389 
TYR   CD1  C  Y N 390 
TYR   CD2  C  Y N 391 
TYR   CE1  C  Y N 392 
TYR   CE2  C  Y N 393 
TYR   CZ   C  Y N 394 
TYR   OH   O  N N 395 
TYR   OXT  O  N N 396 
TYR   H    H  N N 397 
TYR   H2   H  N N 398 
TYR   HA   H  N N 399 
TYR   HB2  H  N N 400 
TYR   HB3  H  N N 401 
TYR   HD1  H  N N 402 
TYR   HD2  H  N N 403 
TYR   HE1  H  N N 404 
TYR   HE2  H  N N 405 
TYR   HH   H  N N 406 
TYR   HXT  H  N N 407 
VAL   N    N  N N 408 
VAL   CA   C  N S 409 
VAL   C    C  N N 410 
VAL   O    O  N N 411 
VAL   CB   C  N N 412 
VAL   CG1  C  N N 413 
VAL   CG2  C  N N 414 
VAL   OXT  O  N N 415 
VAL   H    H  N N 416 
VAL   H2   H  N N 417 
VAL   HA   H  N N 418 
VAL   HB   H  N N 419 
VAL   HG11 H  N N 420 
VAL   HG12 H  N N 421 
VAL   HG13 H  N N 422 
VAL   HG21 H  N N 423 
VAL   HG22 H  N N 424 
VAL   HG23 H  N N 425 
VAL   HXT  H  N N 426 
# 
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 
A1ICF C14 C15  doub Y N 1   
A1ICF C14 C13  sing Y N 2   
A1ICF C15 C16  sing Y N 3   
A1ICF O19 C17  doub N N 4   
A1ICF C13 C12  doub Y N 5   
A1ICF C17 C16  sing N N 6   
A1ICF C17 O18  sing N N 7   
A1ICF C16 C11  doub Y N 8   
A1ICF C12 C11  sing Y N 9   
A1ICF C11 C10  sing N N 10  
A1ICF C10 N09  doub N E 11  
A1ICF N09 O08  sing N N 12  
A1ICF O08 C07  sing N N 13  
A1ICF C07 C03  sing N N 14  
A1ICF C02 C03  doub Y N 15  
A1ICF C02 C01  sing Y N 16  
A1ICF C03 C04  sing Y N 17  
A1ICF C01 C06  doub Y N 18  
A1ICF C04 CL20 sing N N 19  
A1ICF C04 C05  doub Y N 20  
A1ICF C06 C05  sing Y N 21  
A1ICF C12 H3   sing N N 22  
A1ICF C13 H4   sing N N 23  
A1ICF C14 H5   sing N N 24  
A1ICF C15 H6   sing N N 25  
A1ICF C01 H7   sing N N 26  
A1ICF C02 H8   sing N N 27  
A1ICF C05 H9   sing N N 28  
A1ICF C06 H10  sing N N 29  
A1ICF C07 H11  sing N N 30  
A1ICF C07 H12  sing N N 31  
A1ICF O18 H14  sing N N 32  
A1ICF C10 H1   sing N N 33  
ALA   N   CA   sing N N 34  
ALA   N   H    sing N N 35  
ALA   N   H2   sing N N 36  
ALA   CA  C    sing N N 37  
ALA   CA  CB   sing N N 38  
ALA   CA  HA   sing N N 39  
ALA   C   O    doub N N 40  
ALA   C   OXT  sing N N 41  
ALA   CB  HB1  sing N N 42  
ALA   CB  HB2  sing N N 43  
ALA   CB  HB3  sing N N 44  
ALA   OXT HXT  sing N N 45  
ARG   N   CA   sing N N 46  
ARG   N   H    sing N N 47  
ARG   N   H2   sing N N 48  
ARG   CA  C    sing N N 49  
ARG   CA  CB   sing N N 50  
ARG   CA  HA   sing N N 51  
ARG   C   O    doub N N 52  
ARG   C   OXT  sing N N 53  
ARG   CB  CG   sing N N 54  
ARG   CB  HB2  sing N N 55  
ARG   CB  HB3  sing N N 56  
ARG   CG  CD   sing N N 57  
ARG   CG  HG2  sing N N 58  
ARG   CG  HG3  sing N N 59  
ARG   CD  NE   sing N N 60  
ARG   CD  HD2  sing N N 61  
ARG   CD  HD3  sing N N 62  
ARG   NE  CZ   sing N N 63  
ARG   NE  HE   sing N N 64  
ARG   CZ  NH1  sing N N 65  
ARG   CZ  NH2  doub N N 66  
ARG   NH1 HH11 sing N N 67  
ARG   NH1 HH12 sing N N 68  
ARG   NH2 HH21 sing N N 69  
ARG   NH2 HH22 sing N N 70  
ARG   OXT HXT  sing N N 71  
ASN   N   CA   sing N N 72  
ASN   N   H    sing N N 73  
ASN   N   H2   sing N N 74  
ASN   CA  C    sing N N 75  
ASN   CA  CB   sing N N 76  
ASN   CA  HA   sing N N 77  
ASN   C   O    doub N N 78  
ASN   C   OXT  sing N N 79  
ASN   CB  CG   sing N N 80  
ASN   CB  HB2  sing N N 81  
ASN   CB  HB3  sing N N 82  
ASN   CG  OD1  doub N N 83  
ASN   CG  ND2  sing N N 84  
ASN   ND2 HD21 sing N N 85  
ASN   ND2 HD22 sing N N 86  
ASN   OXT HXT  sing N N 87  
ASP   N   CA   sing N N 88  
ASP   N   H    sing N N 89  
ASP   N   H2   sing N N 90  
ASP   CA  C    sing N N 91  
ASP   CA  CB   sing N N 92  
ASP   CA  HA   sing N N 93  
ASP   C   O    doub N N 94  
ASP   C   OXT  sing N N 95  
ASP   CB  CG   sing N N 96  
ASP   CB  HB2  sing N N 97  
ASP   CB  HB3  sing N N 98  
ASP   CG  OD1  doub N N 99  
ASP   CG  OD2  sing N N 100 
ASP   OD2 HD2  sing N N 101 
ASP   OXT HXT  sing N N 102 
CYS   N   CA   sing N N 103 
CYS   N   H    sing N N 104 
CYS   N   H2   sing N N 105 
CYS   CA  C    sing N N 106 
CYS   CA  CB   sing N N 107 
CYS   CA  HA   sing N N 108 
CYS   C   O    doub N N 109 
CYS   C   OXT  sing N N 110 
CYS   CB  SG   sing N N 111 
CYS   CB  HB2  sing N N 112 
CYS   CB  HB3  sing N N 113 
CYS   SG  HG   sing N N 114 
CYS   OXT HXT  sing N N 115 
EDO   C1  O1   sing N N 116 
EDO   C1  C2   sing N N 117 
EDO   C1  H11  sing N N 118 
EDO   C1  H12  sing N N 119 
EDO   O1  HO1  sing N N 120 
EDO   C2  O2   sing N N 121 
EDO   C2  H21  sing N N 122 
EDO   C2  H22  sing N N 123 
EDO   O2  HO2  sing N N 124 
GLU   N   CA   sing N N 125 
GLU   N   H    sing N N 126 
GLU   N   H2   sing N N 127 
GLU   CA  C    sing N N 128 
GLU   CA  CB   sing N N 129 
GLU   CA  HA   sing N N 130 
GLU   C   O    doub N N 131 
GLU   C   OXT  sing N N 132 
GLU   CB  CG   sing N N 133 
GLU   CB  HB2  sing N N 134 
GLU   CB  HB3  sing N N 135 
GLU   CG  CD   sing N N 136 
GLU   CG  HG2  sing N N 137 
GLU   CG  HG3  sing N N 138 
GLU   CD  OE1  doub N N 139 
GLU   CD  OE2  sing N N 140 
GLU   OE2 HE2  sing N N 141 
GLU   OXT HXT  sing N N 142 
GLY   N   CA   sing N N 143 
GLY   N   H    sing N N 144 
GLY   N   H2   sing N N 145 
GLY   CA  C    sing N N 146 
GLY   CA  HA2  sing N N 147 
GLY   CA  HA3  sing N N 148 
GLY   C   O    doub N N 149 
GLY   C   OXT  sing N N 150 
GLY   OXT HXT  sing N N 151 
GOL   C1  O1   sing N N 152 
GOL   C1  C2   sing N N 153 
GOL   C1  H11  sing N N 154 
GOL   C1  H12  sing N N 155 
GOL   O1  HO1  sing N N 156 
GOL   C2  O2   sing N N 157 
GOL   C2  C3   sing N N 158 
GOL   C2  H2   sing N N 159 
GOL   O2  HO2  sing N N 160 
GOL   C3  O3   sing N N 161 
GOL   C3  H31  sing N N 162 
GOL   C3  H32  sing N N 163 
GOL   O3  HO3  sing N N 164 
HIS   N   CA   sing N N 165 
HIS   N   H    sing N N 166 
HIS   N   H2   sing N N 167 
HIS   CA  C    sing N N 168 
HIS   CA  CB   sing N N 169 
HIS   CA  HA   sing N N 170 
HIS   C   O    doub N N 171 
HIS   C   OXT  sing N N 172 
HIS   CB  CG   sing N N 173 
HIS   CB  HB2  sing N N 174 
HIS   CB  HB3  sing N N 175 
HIS   CG  ND1  sing Y N 176 
HIS   CG  CD2  doub Y N 177 
HIS   ND1 CE1  doub Y N 178 
HIS   ND1 HD1  sing N N 179 
HIS   CD2 NE2  sing Y N 180 
HIS   CD2 HD2  sing N N 181 
HIS   CE1 NE2  sing Y N 182 
HIS   CE1 HE1  sing N N 183 
HIS   NE2 HE2  sing N N 184 
HIS   OXT HXT  sing N N 185 
HOH   O   H1   sing N N 186 
HOH   O   H2   sing N N 187 
ILE   N   CA   sing N N 188 
ILE   N   H    sing N N 189 
ILE   N   H2   sing N N 190 
ILE   CA  C    sing N N 191 
ILE   CA  CB   sing N N 192 
ILE   CA  HA   sing N N 193 
ILE   C   O    doub N N 194 
ILE   C   OXT  sing N N 195 
ILE   CB  CG1  sing N N 196 
ILE   CB  CG2  sing N N 197 
ILE   CB  HB   sing N N 198 
ILE   CG1 CD1  sing N N 199 
ILE   CG1 HG12 sing N N 200 
ILE   CG1 HG13 sing N N 201 
ILE   CG2 HG21 sing N N 202 
ILE   CG2 HG22 sing N N 203 
ILE   CG2 HG23 sing N N 204 
ILE   CD1 HD11 sing N N 205 
ILE   CD1 HD12 sing N N 206 
ILE   CD1 HD13 sing N N 207 
ILE   OXT HXT  sing N N 208 
LEU   N   CA   sing N N 209 
LEU   N   H    sing N N 210 
LEU   N   H2   sing N N 211 
LEU   CA  C    sing N N 212 
LEU   CA  CB   sing N N 213 
LEU   CA  HA   sing N N 214 
LEU   C   O    doub N N 215 
LEU   C   OXT  sing N N 216 
LEU   CB  CG   sing N N 217 
LEU   CB  HB2  sing N N 218 
LEU   CB  HB3  sing N N 219 
LEU   CG  CD1  sing N N 220 
LEU   CG  CD2  sing N N 221 
LEU   CG  HG   sing N N 222 
LEU   CD1 HD11 sing N N 223 
LEU   CD1 HD12 sing N N 224 
LEU   CD1 HD13 sing N N 225 
LEU   CD2 HD21 sing N N 226 
LEU   CD2 HD22 sing N N 227 
LEU   CD2 HD23 sing N N 228 
LEU   OXT HXT  sing N N 229 
LYS   N   CA   sing N N 230 
LYS   N   H    sing N N 231 
LYS   N   H2   sing N N 232 
LYS   CA  C    sing N N 233 
LYS   CA  CB   sing N N 234 
LYS   CA  HA   sing N N 235 
LYS   C   O    doub N N 236 
LYS   C   OXT  sing N N 237 
LYS   CB  CG   sing N N 238 
LYS   CB  HB2  sing N N 239 
LYS   CB  HB3  sing N N 240 
LYS   CG  CD   sing N N 241 
LYS   CG  HG2  sing N N 242 
LYS   CG  HG3  sing N N 243 
LYS   CD  CE   sing N N 244 
LYS   CD  HD2  sing N N 245 
LYS   CD  HD3  sing N N 246 
LYS   CE  NZ   sing N N 247 
LYS   CE  HE2  sing N N 248 
LYS   CE  HE3  sing N N 249 
LYS   NZ  HZ1  sing N N 250 
LYS   NZ  HZ2  sing N N 251 
LYS   NZ  HZ3  sing N N 252 
LYS   OXT HXT  sing N N 253 
MET   N   CA   sing N N 254 
MET   N   H    sing N N 255 
MET   N   H2   sing N N 256 
MET   CA  C    sing N N 257 
MET   CA  CB   sing N N 258 
MET   CA  HA   sing N N 259 
MET   C   O    doub N N 260 
MET   C   OXT  sing N N 261 
MET   CB  CG   sing N N 262 
MET   CB  HB2  sing N N 263 
MET   CB  HB3  sing N N 264 
MET   CG  SD   sing N N 265 
MET   CG  HG2  sing N N 266 
MET   CG  HG3  sing N N 267 
MET   SD  CE   sing N N 268 
MET   CE  HE1  sing N N 269 
MET   CE  HE2  sing N N 270 
MET   CE  HE3  sing N N 271 
MET   OXT HXT  sing N N 272 
PHE   N   CA   sing N N 273 
PHE   N   H    sing N N 274 
PHE   N   H2   sing N N 275 
PHE   CA  C    sing N N 276 
PHE   CA  CB   sing N N 277 
PHE   CA  HA   sing N N 278 
PHE   C   O    doub N N 279 
PHE   C   OXT  sing N N 280 
PHE   CB  CG   sing N N 281 
PHE   CB  HB2  sing N N 282 
PHE   CB  HB3  sing N N 283 
PHE   CG  CD1  doub Y N 284 
PHE   CG  CD2  sing Y N 285 
PHE   CD1 CE1  sing Y N 286 
PHE   CD1 HD1  sing N N 287 
PHE   CD2 CE2  doub Y N 288 
PHE   CD2 HD2  sing N N 289 
PHE   CE1 CZ   doub Y N 290 
PHE   CE1 HE1  sing N N 291 
PHE   CE2 CZ   sing Y N 292 
PHE   CE2 HE2  sing N N 293 
PHE   CZ  HZ   sing N N 294 
PHE   OXT HXT  sing N N 295 
PRO   N   CA   sing N N 296 
PRO   N   CD   sing N N 297 
PRO   N   H    sing N N 298 
PRO   CA  C    sing N N 299 
PRO   CA  CB   sing N N 300 
PRO   CA  HA   sing N N 301 
PRO   C   O    doub N N 302 
PRO   C   OXT  sing N N 303 
PRO   CB  CG   sing N N 304 
PRO   CB  HB2  sing N N 305 
PRO   CB  HB3  sing N N 306 
PRO   CG  CD   sing N N 307 
PRO   CG  HG2  sing N N 308 
PRO   CG  HG3  sing N N 309 
PRO   CD  HD2  sing N N 310 
PRO   CD  HD3  sing N N 311 
PRO   OXT HXT  sing N N 312 
SER   N   CA   sing N N 313 
SER   N   H    sing N N 314 
SER   N   H2   sing N N 315 
SER   CA  C    sing N N 316 
SER   CA  CB   sing N N 317 
SER   CA  HA   sing N N 318 
SER   C   O    doub N N 319 
SER   C   OXT  sing N N 320 
SER   CB  OG   sing N N 321 
SER   CB  HB2  sing N N 322 
SER   CB  HB3  sing N N 323 
SER   OG  HG   sing N N 324 
SER   OXT HXT  sing N N 325 
THR   N   CA   sing N N 326 
THR   N   H    sing N N 327 
THR   N   H2   sing N N 328 
THR   CA  C    sing N N 329 
THR   CA  CB   sing N N 330 
THR   CA  HA   sing N N 331 
THR   C   O    doub N N 332 
THR   C   OXT  sing N N 333 
THR   CB  OG1  sing N N 334 
THR   CB  CG2  sing N N 335 
THR   CB  HB   sing N N 336 
THR   OG1 HG1  sing N N 337 
THR   CG2 HG21 sing N N 338 
THR   CG2 HG22 sing N N 339 
THR   CG2 HG23 sing N N 340 
THR   OXT HXT  sing N N 341 
TRP   N   CA   sing N N 342 
TRP   N   H    sing N N 343 
TRP   N   H2   sing N N 344 
TRP   CA  C    sing N N 345 
TRP   CA  CB   sing N N 346 
TRP   CA  HA   sing N N 347 
TRP   C   O    doub N N 348 
TRP   C   OXT  sing N N 349 
TRP   CB  CG   sing N N 350 
TRP   CB  HB2  sing N N 351 
TRP   CB  HB3  sing N N 352 
TRP   CG  CD1  doub Y N 353 
TRP   CG  CD2  sing Y N 354 
TRP   CD1 NE1  sing Y N 355 
TRP   CD1 HD1  sing N N 356 
TRP   CD2 CE2  doub Y N 357 
TRP   CD2 CE3  sing Y N 358 
TRP   NE1 CE2  sing Y N 359 
TRP   NE1 HE1  sing N N 360 
TRP   CE2 CZ2  sing Y N 361 
TRP   CE3 CZ3  doub Y N 362 
TRP   CE3 HE3  sing N N 363 
TRP   CZ2 CH2  doub Y N 364 
TRP   CZ2 HZ2  sing N N 365 
TRP   CZ3 CH2  sing Y N 366 
TRP   CZ3 HZ3  sing N N 367 
TRP   CH2 HH2  sing N N 368 
TRP   OXT HXT  sing N N 369 
TYR   N   CA   sing N N 370 
TYR   N   H    sing N N 371 
TYR   N   H2   sing N N 372 
TYR   CA  C    sing N N 373 
TYR   CA  CB   sing N N 374 
TYR   CA  HA   sing N N 375 
TYR   C   O    doub N N 376 
TYR   C   OXT  sing N N 377 
TYR   CB  CG   sing N N 378 
TYR   CB  HB2  sing N N 379 
TYR   CB  HB3  sing N N 380 
TYR   CG  CD1  doub Y N 381 
TYR   CG  CD2  sing Y N 382 
TYR   CD1 CE1  sing Y N 383 
TYR   CD1 HD1  sing N N 384 
TYR   CD2 CE2  doub Y N 385 
TYR   CD2 HD2  sing N N 386 
TYR   CE1 CZ   doub Y N 387 
TYR   CE1 HE1  sing N N 388 
TYR   CE2 CZ   sing Y N 389 
TYR   CE2 HE2  sing N N 390 
TYR   CZ  OH   sing N N 391 
TYR   OH  HH   sing N N 392 
TYR   OXT HXT  sing N N 393 
VAL   N   CA   sing N N 394 
VAL   N   H    sing N N 395 
VAL   N   H2   sing N N 396 
VAL   CA  C    sing N N 397 
VAL   CA  CB   sing N N 398 
VAL   CA  HA   sing N N 399 
VAL   C   O    doub N N 400 
VAL   C   OXT  sing N N 401 
VAL   CB  CG1  sing N N 402 
VAL   CB  CG2  sing N N 403 
VAL   CB  HB   sing N N 404 
VAL   CG1 HG11 sing N N 405 
VAL   CG1 HG12 sing N N 406 
VAL   CG1 HG13 sing N N 407 
VAL   CG2 HG21 sing N N 408 
VAL   CG2 HG22 sing N N 409 
VAL   CG2 HG23 sing N N 410 
VAL   OXT HXT  sing N N 411 
# 
_pdbx_audit_support.funding_organization   'Italian Ministry of Education' 
_pdbx_audit_support.country                Italy 
_pdbx_audit_support.grant_number           2022KJB3B7 
_pdbx_audit_support.ordinal                1 
# 
_pdbx_initial_refinement_model.id               1 
_pdbx_initial_refinement_model.entity_id_list   ? 
_pdbx_initial_refinement_model.type             'experimental model' 
_pdbx_initial_refinement_model.source_name      PDB 
_pdbx_initial_refinement_model.accession_code   6TI9 
_pdbx_initial_refinement_model.details          ? 
# 
_atom_sites.entry_id                    9FF8 
_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]   0.023266 
_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]   0.011731 
_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]   0.015624 
_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  
CL 
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    . LYS   A 1 9   ? 3.094   -13.293 6.013   1.00 39.52  ? 9   LYS   A N    1 
ATOM   2    C  CA   . LYS   A 1 9   ? 2.859   -12.026 6.694   1.00 44.55  ? 9   LYS   A CA   1 
ATOM   3    C  C    . LYS   A 1 9   ? 4.035   -11.112 6.452   1.00 55.14  ? 9   LYS   A C    1 
ATOM   4    O  O    . LYS   A 1 9   ? 3.897   -10.033 5.878   1.00 61.93  ? 9   LYS   A O    1 
ATOM   5    C  CB   . LYS   A 1 9   ? 2.667   -12.230 8.200   1.00 48.60  ? 9   LYS   A CB   1 
ATOM   6    C  CG   . LYS   A 1 9   ? 1.404   -12.983 8.602   1.00 57.36  ? 9   LYS   A CG   1 
ATOM   7    C  CD   . LYS   A 1 9   ? 1.292   -13.170 10.109  1.00 57.95  ? 9   LYS   A CD   1 
ATOM   8    C  CE   . LYS   A 1 9   ? 0.010   -13.901 10.464  1.00 53.04  ? 9   LYS   A CE   1 
ATOM   9    N  NZ   . LYS   A 1 9   ? -0.116  -14.120 11.935  1.00 50.12  ? 9   LYS   A NZ   1 
ATOM   10   N  N    . CYS   A 1 10  ? 5.199   -11.558 6.897   1.00 56.21  ? 10  CYS   A N    1 
ATOM   11   C  CA   . CYS   A 1 10  ? 6.422   -10.804 6.687   1.00 57.76  ? 10  CYS   A CA   1 
ATOM   12   C  C    . CYS   A 1 10  ? 6.989   -11.042 5.289   1.00 29.08  ? 10  CYS   A C    1 
ATOM   13   O  O    . CYS   A 1 10  ? 7.130   -10.083 4.521   1.00 35.87  ? 10  CYS   A O    1 
ATOM   14   C  CB   . CYS   A 1 10  ? 7.462   -11.117 7.771   1.00 55.19  ? 10  CYS   A CB   1 
ATOM   15   S  SG   . CYS   A 1 10  ? 6.969   -10.652 9.447   1.00 97.94  ? 10  CYS   A SG   1 
ATOM   16   N  N    . PRO   A 1 11  ? 7.330   -12.282 4.905   1.00 25.43  ? 11  PRO   A N    1 
ATOM   17   C  CA   . PRO   A 1 11  ? 8.188   -12.442 3.727   1.00 18.49  ? 11  PRO   A CA   1 
ATOM   18   C  C    . PRO   A 1 11  ? 7.471   -12.359 2.396   1.00 15.26  ? 11  PRO   A C    1 
ATOM   19   O  O    . PRO   A 1 11  ? 8.129   -12.057 1.394   1.00 17.23  ? 11  PRO   A O    1 
ATOM   20   C  CB   . PRO   A 1 11  ? 8.829   -13.819 3.942   1.00 23.39  ? 11  PRO   A CB   1 
ATOM   21   C  CG   . PRO   A 1 11  ? 7.798   -14.570 4.664   1.00 27.24  ? 11  PRO   A CG   1 
ATOM   22   C  CD   . PRO   A 1 11  ? 7.018   -13.592 5.508   1.00 31.73  ? 11  PRO   A CD   1 
ATOM   23   N  N    . LEU   A 1 12  ? 6.169   -12.624 2.338   1.00 16.49  ? 12  LEU   A N    1 
ATOM   24   C  CA   . LEU   A 1 12  ? 5.433   -12.591 1.072   1.00 16.54  ? 12  LEU   A CA   1 
ATOM   25   C  C    . LEU   A 1 12  ? 4.053   -12.023 1.332   1.00 16.33  ? 12  LEU   A C    1 
ATOM   26   O  O    . LEU   A 1 12  ? 3.275   -12.596 2.099   1.00 20.18  ? 12  LEU   A O    1 
ATOM   27   C  CB   . LEU   A 1 12  ? 5.301   -13.985 0.454   1.00 15.21  ? 12  LEU   A CB   1 
ATOM   28   C  CG   . LEU   A 1 12  ? 4.569   -14.038 -0.890  1.00 15.84  ? 12  LEU   A CG   1 
ATOM   29   C  CD1  . LEU   A 1 12  ? 5.298   -13.206 -1.949  1.00 15.60  ? 12  LEU   A CD1  1 
ATOM   30   C  CD2  . LEU   A 1 12  ? 4.447   -15.490 -1.327  1.00 19.45  ? 12  LEU   A CD2  1 
ATOM   31   N  N    A MET   A 1 13  ? 3.738   -10.886 0.704   0.59 14.24  ? 13  MET   A N    1 
ATOM   32   N  N    B MET   A 1 13  ? 3.750   -10.911 0.676   0.41 14.26  ? 13  MET   A N    1 
ATOM   33   C  CA   A MET   A 1 13  ? 2.426   -10.259 0.828   0.59 14.57  ? 13  MET   A CA   1 
ATOM   34   C  CA   B MET   A 1 13  ? 2.452   -10.275 0.774   0.41 14.62  ? 13  MET   A CA   1 
ATOM   35   C  C    A MET   A 1 13  ? 1.911   -9.901  -0.561  0.59 12.64  ? 13  MET   A C    1 
ATOM   36   C  C    B MET   A 1 13  ? 1.924   -10.037 -0.632  0.41 12.63  ? 13  MET   A C    1 
ATOM   37   O  O    A MET   A 1 13  ? 2.686   -9.491  -1.428  0.59 13.52  ? 13  MET   A O    1 
ATOM   38   O  O    B MET   A 1 13  ? 2.693   -9.876  -1.585  0.41 12.49  ? 13  MET   A O    1 
ATOM   39   C  CB   A MET   A 1 13  ? 2.481   -8.986  1.696   0.59 16.97  ? 13  MET   A CB   1 
ATOM   40   C  CB   B MET   A 1 13  ? 2.560   -8.956  1.542   0.41 16.86  ? 13  MET   A CB   1 
ATOM   41   C  CG   A MET   A 1 13  ? 1.106   -8.407  2.071   0.59 17.39  ? 13  MET   A CG   1 
ATOM   42   C  CG   B MET   A 1 13  ? 3.043   -9.154  2.967   0.41 24.60  ? 13  MET   A CG   1 
ATOM   43   S  SD   A MET   A 1 13  ? 0.437   -7.217  0.875   0.59 18.93  ? 13  MET   A SD   1 
ATOM   44   S  SD   B MET   A 1 13  ? 3.465   -7.629  3.821   0.41 40.55  ? 13  MET   A SD   1 
ATOM   45   C  CE   A MET   A 1 13  ? 1.145   -5.688  1.487   0.59 19.50  ? 13  MET   A CE   1 
ATOM   46   C  CE   B MET   A 1 13  ? 5.096   -7.304  3.162   0.41 26.22  ? 13  MET   A CE   1 
ATOM   47   N  N    . VAL   A 1 14  ? 0.603   -10.049 -0.766  1.00 12.74  ? 14  VAL   A N    1 
ATOM   48   C  CA   . VAL   A 1 14  ? -0.050  -9.773  -2.048  1.00 11.05  ? 14  VAL   A CA   1 
ATOM   49   C  C    . VAL   A 1 14  ? -1.103  -8.707  -1.815  1.00 14.02  ? 14  VAL   A C    1 
ATOM   50   O  O    . VAL   A 1 14  ? -1.898  -8.813  -0.872  1.00 15.31  ? 14  VAL   A O    1 
ATOM   51   C  CB   . VAL   A 1 14  ? -0.696  -11.041 -2.639  1.00 11.89  ? 14  VAL   A CB   1 
ATOM   52   C  CG1  . VAL   A 1 14  ? -1.340  -10.740 -3.990  1.00 13.70  ? 14  VAL   A CG1  1 
ATOM   53   C  CG2  . VAL   A 1 14  ? 0.352   -12.132 -2.809  1.00 14.69  ? 14  VAL   A CG2  1 
ATOM   54   N  N    . LYS   A 1 15  ? -1.120  -7.686  -2.669  1.00 11.95  ? 15  LYS   A N    1 
ATOM   55   C  CA   . LYS   A 1 15  ? -2.099  -6.612  -2.573  1.00 12.72  ? 15  LYS   A CA   1 
ATOM   56   C  C    . LYS   A 1 15  ? -2.762  -6.459  -3.926  1.00 13.60  ? 15  LYS   A C    1 
ATOM   57   O  O    . LYS   A 1 15  ? -2.070  -6.423  -4.948  1.00 14.66  ? 15  LYS   A O    1 
ATOM   58   C  CB   . LYS   A 1 15  ? -1.457  -5.290  -2.158  1.00 14.38  ? 15  LYS   A CB   1 
ATOM   59   C  CG   . LYS   A 1 15  ? -2.496  -4.191  -1.903  1.00 21.07  ? 15  LYS   A CG   1 
ATOM   60   C  CD   . LYS   A 1 15  ? -1.939  -3.055  -1.068  1.00 25.30  ? 15  LYS   A CD   1 
ATOM   61   C  CE   . LYS   A 1 15  ? -3.048  -2.079  -0.672  1.00 29.95  ? 15  LYS   A CE   1 
ATOM   62   N  NZ   . LYS   A 1 15  ? -2.571  -1.201  0.441   1.00 35.09  ? 15  LYS   A NZ   1 
ATOM   63   N  N    . VAL   A 1 16  ? -4.090  -6.388  -3.941  1.00 12.66  ? 16  VAL   A N    1 
ATOM   64   C  CA   . VAL   A 1 16  ? -4.827  -6.332  -5.200  1.00 11.15  ? 16  VAL   A CA   1 
ATOM   65   C  C    . VAL   A 1 16  ? -5.806  -5.170  -5.150  1.00 12.79  ? 16  VAL   A C    1 
ATOM   66   O  O    . VAL   A 1 16  ? -6.545  -5.014  -4.168  1.00 11.74  ? 16  VAL   A O    1 
ATOM   67   C  CB   . VAL   A 1 16  ? -5.559  -7.653  -5.480  1.00 12.23  ? 16  VAL   A CB   1 
ATOM   68   C  CG1  . VAL   A 1 16  ? -6.128  -7.673  -6.911  1.00 13.32  ? 16  VAL   A CG1  1 
ATOM   69   C  CG2  . VAL   A 1 16  ? -4.602  -8.846  -5.262  1.00 14.08  ? 16  VAL   A CG2  1 
ATOM   70   N  N    . LEU   A 1 17  ? -5.812  -4.370  -6.213  1.00 11.70  ? 17  LEU   A N    1 
ATOM   71   C  CA   . LEU   A 1 17  ? -6.651  -3.185  -6.332  1.00 11.14  ? 17  LEU   A CA   1 
ATOM   72   C  C    . LEU   A 1 17  ? -7.526  -3.294  -7.571  1.00 10.56  ? 17  LEU   A C    1 
ATOM   73   O  O    . LEU   A 1 17  ? -7.154  -3.928  -8.564  1.00 11.73  ? 17  LEU   A O    1 
ATOM   74   C  CB   . LEU   A 1 17  ? -5.791  -1.921  -6.452  1.00 12.83  ? 17  LEU   A CB   1 
ATOM   75   C  CG   . LEU   A 1 17  ? -4.875  -1.583  -5.280  1.00 14.12  ? 17  LEU   A CG   1 
ATOM   76   C  CD1  . LEU   A 1 17  ? -4.127  -0.325  -5.633  1.00 22.03  ? 17  LEU   A CD1  1 
ATOM   77   C  CD2  . LEU   A 1 17  ? -5.670  -1.391  -4.003  1.00 17.13  ? 17  LEU   A CD2  1 
ATOM   78   N  N    . ASP   A 1 18  ? -8.671  -2.621  -7.524  1.00 11.00  ? 18  ASP   A N    1 
ATOM   79   C  CA   . ASP   A 1 18  ? -9.672  -2.642  -8.584  1.00 11.56  ? 18  ASP   A CA   1 
ATOM   80   C  C    . ASP   A 1 18  ? -9.686  -1.275  -9.257  1.00 9.94   ? 18  ASP   A C    1 
ATOM   81   O  O    . ASP   A 1 18  ? -10.019 -0.267  -8.616  1.00 12.04  ? 18  ASP   A O    1 
ATOM   82   C  CB   . ASP   A 1 18  ? -11.017 -2.987  -7.940  1.00 12.31  ? 18  ASP   A CB   1 
ATOM   83   C  CG   . ASP   A 1 18  ? -12.165 -3.048  -8.919  1.00 15.97  ? 18  ASP   A CG   1 
ATOM   84   O  OD1  . ASP   A 1 18  ? -12.224 -2.231  -9.839  1.00 14.57  ? 18  ASP   A OD1  1 
ATOM   85   O  OD2  . ASP   A 1 18  ? -13.055 -3.904  -8.733  1.00 18.63  ? 18  ASP   A OD2  1 
ATOM   86   N  N    . ALA   A 1 19  ? -9.314  -1.243  -10.540 1.00 11.05  ? 19  ALA   A N    1 
ATOM   87   C  CA   . ALA   A 1 19  ? -9.221  -0.016  -11.317 1.00 12.03  ? 19  ALA   A CA   1 
ATOM   88   C  C    . ALA   A 1 19  ? -10.564 0.467   -11.850 1.00 11.62  ? 19  ALA   A C    1 
ATOM   89   O  O    . ALA   A 1 19  ? -10.619 1.578   -12.393 1.00 14.40  ? 19  ALA   A O    1 
ATOM   90   C  CB   . ALA   A 1 19  ? -8.260  -0.231  -12.491 1.00 13.20  ? 19  ALA   A CB   1 
ATOM   91   N  N    . VAL   A 1 20  ? -11.622 -0.329  -11.724 1.00 13.19  ? 20  VAL   A N    1 
ATOM   92   C  CA   . VAL   A 1 20  ? -12.960 0.075   -12.157 1.00 13.46  ? 20  VAL   A CA   1 
ATOM   93   C  C    . VAL   A 1 20  ? -13.693 0.794   -11.043 1.00 15.53  ? 20  VAL   A C    1 
ATOM   94   O  O    . VAL   A 1 20  ? -14.334 1.827   -11.273 1.00 20.76  ? 20  VAL   A O    1 
ATOM   95   C  CB   . VAL   A 1 20  ? -13.754 -1.150  -12.643 1.00 13.79  ? 20  VAL   A CB   1 
ATOM   96   C  CG1  . VAL   A 1 20  ? -15.210 -0.752  -12.927 1.00 16.92  ? 20  VAL   A CG1  1 
ATOM   97   C  CG2  . VAL   A 1 20  ? -13.128 -1.713  -13.882 1.00 16.42  ? 20  VAL   A CG2  1 
ATOM   98   N  N    . ARG   A 1 21  ? -13.582 0.258   -9.831  1.00 14.60  ? 21  ARG   A N    1 
ATOM   99   C  CA   . ARG   A 1 21  ? -14.300 0.766   -8.677  1.00 16.88  ? 21  ARG   A CA   1 
ATOM   100  C  C    . ARG   A 1 21  ? -13.475 1.727   -7.838  1.00 15.73  ? 21  ARG   A C    1 
ATOM   101  O  O    . ARG   A 1 21  ? -14.048 2.451   -7.011  1.00 18.60  ? 21  ARG   A O    1 
ATOM   102  C  CB   . ARG   A 1 21  ? -14.785 -0.409  -7.815  1.00 20.12  ? 21  ARG   A CB   1 
ATOM   103  C  CG   . ARG   A 1 21  ? -15.915 -1.192  -8.482  1.00 27.65  ? 21  ARG   A CG   1 
ATOM   104  C  CD   . ARG   A 1 21  ? -15.802 -2.692  -8.280  1.00 42.42  ? 21  ARG   A CD   1 
ATOM   105  N  NE   . ARG   A 1 21  ? -16.117 -3.111  -6.921  1.00 35.89  ? 21  ARG   A NE   1 
ATOM   106  C  CZ   . ARG   A 1 21  ? -17.312 -3.530  -6.527  1.00 51.28  ? 21  ARG   A CZ   1 
ATOM   107  N  NH1  . ARG   A 1 21  ? -18.335 -3.588  -7.366  1.00 54.35  ? 21  ARG   A NH1  1 
ATOM   108  N  NH2  . ARG   A 1 21  ? -17.486 -3.902  -5.263  1.00 49.07  ? 21  ARG   A NH2  1 
ATOM   109  N  N    . GLY   A 1 22  ? -12.160 1.767   -8.033  1.00 12.66  ? 22  GLY   A N    1 
ATOM   110  C  CA   . GLY   A 1 22  ? -11.309 2.599   -7.197  1.00 11.37  ? 22  GLY   A CA   1 
ATOM   111  C  C    . GLY   A 1 22  ? -11.288 2.129   -5.761  1.00 12.87  ? 22  GLY   A C    1 
ATOM   112  O  O    . GLY   A 1 22  ? -11.475 2.919   -4.830  1.00 13.23  ? 22  GLY   A O    1 
ATOM   113  N  N    . SER   A 1 23  ? -11.022 0.847   -5.560  1.00 12.02  ? 23  SER   A N    1 
ATOM   114  C  CA   . SER   A 1 23  ? -11.160 0.228   -4.254  1.00 10.62  ? 23  SER   A CA   1 
ATOM   115  C  C    . SER   A 1 23  ? -10.158 -0.906  -4.175  1.00 12.37  ? 23  SER   A C    1 
ATOM   116  O  O    . SER   A 1 23  ? -9.651  -1.359  -5.206  1.00 13.70  ? 23  SER   A O    1 
ATOM   117  C  CB   . SER   A 1 23  ? -12.565 -0.359  -4.099  1.00 15.61  ? 23  SER   A CB   1 
ATOM   118  O  OG   . SER   A 1 23  ? -12.723 -1.454  -4.994  1.00 18.80  ? 23  SER   A OG   1 
ATOM   119  N  N    . PRO   A 1 24  ? -9.872  -1.397  -2.979  1.00 10.94  ? 24  PRO   A N    1 
ATOM   120  C  CA   . PRO   A 1 24  ? -9.233  -2.709  -2.887  1.00 12.28  ? 24  PRO   A CA   1 
ATOM   121  C  C    . PRO   A 1 24  ? -10.087 -3.754  -3.586  1.00 13.94  ? 24  PRO   A C    1 
ATOM   122  O  O    . PRO   A 1 24  ? -11.311 -3.631  -3.693  1.00 13.76  ? 24  PRO   A O    1 
ATOM   123  C  CB   . PRO   A 1 24  ? -9.174  -2.970  -1.374  1.00 15.40  ? 24  PRO   A CB   1 
ATOM   124  C  CG   . PRO   A 1 24  ? -10.267 -2.120  -0.797  1.00 22.52  ? 24  PRO   A CG   1 
ATOM   125  C  CD   . PRO   A 1 24  ? -10.273 -0.884  -1.654  1.00 13.45  ? 24  PRO   A CD   1 
ATOM   126  N  N    . ALA   A 1 25  ? -9.423  -4.781  -4.104  1.00 12.16  ? 25  ALA   A N    1 
ATOM   127  C  CA   . ALA   A 1 25  ? -10.111 -5.947  -4.645  1.00 11.26  ? 25  ALA   A CA   1 
ATOM   128  C  C    . ALA   A 1 25  ? -10.223 -6.967  -3.511  1.00 12.58  ? 25  ALA   A C    1 
ATOM   129  O  O    . ALA   A 1 25  ? -9.218  -7.539  -3.070  1.00 13.95  ? 25  ALA   A O    1 
ATOM   130  C  CB   . ALA   A 1 25  ? -9.358  -6.501  -5.854  1.00 14.48  ? 25  ALA   A CB   1 
ATOM   131  N  N    . ILE   A 1 26  ? -11.429 -7.136  -2.996  1.00 13.55  ? 26  ILE   A N    1 
ATOM   132  C  CA   A ILE   A 1 26  ? -11.647 -7.936  -1.800  0.43 14.76  ? 26  ILE   A CA   1 
ATOM   133  C  CA   B ILE   A 1 26  ? -11.693 -7.924  -1.796  0.57 14.77  ? 26  ILE   A CA   1 
ATOM   134  C  C    . ILE   A 1 26  ? -12.064 -9.347  -2.182  1.00 14.81  ? 26  ILE   A C    1 
ATOM   135  O  O    . ILE   A 1 26  ? -12.724 -9.580  -3.204  1.00 16.11  ? 26  ILE   A O    1 
ATOM   136  C  CB   A ILE   A 1 26  ? -12.665 -7.271  -0.850  0.43 17.07  ? 26  ILE   A CB   1 
ATOM   137  C  CB   B ILE   A 1 26  ? -12.821 -7.245  -0.991  0.57 16.67  ? 26  ILE   A CB   1 
ATOM   138  C  CG1  A ILE   A 1 26  ? -14.049 -7.214  -1.497  0.43 19.17  ? 26  ILE   A CG1  1 
ATOM   139  C  CG1  B ILE   A 1 26  ? -12.465 -5.778  -0.757  0.57 15.69  ? 26  ILE   A CG1  1 
ATOM   140  C  CG2  A ILE   A 1 26  ? -12.184 -5.876  -0.485  0.43 15.57  ? 26  ILE   A CG2  1 
ATOM   141  C  CG2  B ILE   A 1 26  ? -13.078 -7.966  0.330   0.57 18.31  ? 26  ILE   A CG2  1 
ATOM   142  C  CD1  A ILE   A 1 26  ? -15.150 -6.783  -0.544  0.43 24.33  ? 26  ILE   A CD1  1 
ATOM   143  C  CD1  B ILE   A 1 26  ? -13.556 -4.996  -0.060  0.57 23.87  ? 26  ILE   A CD1  1 
ATOM   144  N  N    . ASN   A 1 27  ? -11.647 -10.303 -1.346  1.00 15.14  ? 27  ASN   A N    1 
ATOM   145  C  CA   A ASN   A 1 27  ? -12.031 -11.710 -1.510  0.50 16.18  ? 27  ASN   A CA   1 
ATOM   146  C  CA   B ASN   A 1 27  ? -12.010 -11.719 -1.495  0.50 16.15  ? 27  ASN   A CA   1 
ATOM   147  C  C    . ASN   A 1 27  ? -11.491 -12.317 -2.799  1.00 17.76  ? 27  ASN   A C    1 
ATOM   148  O  O    . ASN   A 1 27  ? -12.140 -13.171 -3.414  1.00 20.25  ? 27  ASN   A O    1 
ATOM   149  C  CB   A ASN   A 1 27  ? -13.548 -11.905 -1.432  0.50 22.65  ? 27  ASN   A CB   1 
ATOM   150  C  CB   B ASN   A 1 27  ? -13.517 -11.962 -1.335  0.50 22.79  ? 27  ASN   A CB   1 
ATOM   151  C  CG   A ASN   A 1 27  ? -14.105 -11.556 -0.079  0.50 19.82  ? 27  ASN   A CG   1 
ATOM   152  C  CG   B ASN   A 1 27  ? -13.827 -13.317 -0.711  0.50 16.70  ? 27  ASN   A CG   1 
ATOM   153  O  OD1  A ASN   A 1 27  ? -13.493 -11.839 0.946   0.50 26.60  ? 27  ASN   A OD1  1 
ATOM   154  O  OD1  B ASN   A 1 27  ? -13.200 -13.719 0.275   0.50 25.40  ? 27  ASN   A OD1  1 
ATOM   155  N  ND2  A ASN   A 1 27  ? -15.279 -10.928 -0.066  0.50 26.87  ? 27  ASN   A ND2  1 
ATOM   156  N  ND2  B ASN   A 1 27  ? -14.789 -14.028 -1.285  0.50 27.38  ? 27  ASN   A ND2  1 
ATOM   157  N  N    . VAL   A 1 28  ? -10.317 -11.882 -3.227  1.00 13.69  ? 28  VAL   A N    1 
ATOM   158  C  CA   . VAL   A 1 28  ? -9.676  -12.424 -4.419  1.00 15.62  ? 28  VAL   A CA   1 
ATOM   159  C  C    . VAL   A 1 28  ? -8.870  -13.641 -3.986  1.00 13.43  ? 28  VAL   A C    1 
ATOM   160  O  O    . VAL   A 1 28  ? -8.029  -13.543 -3.086  1.00 13.62  ? 28  VAL   A O    1 
ATOM   161  C  CB   . VAL   A 1 28  ? -8.754  -11.382 -5.068  1.00 13.06  ? 28  VAL   A CB   1 
ATOM   162  C  CG1  . VAL   A 1 28  ? -8.018  -11.989 -6.257  1.00 17.07  ? 28  VAL   A CG1  1 
ATOM   163  C  CG2  . VAL   A 1 28  ? -9.559  -10.168 -5.506  1.00 15.97  ? 28  VAL   A CG2  1 
ATOM   164  N  N    . ALA   A 1 29  ? -9.121  -14.784 -4.617  1.00 12.32  ? 29  ALA   A N    1 
ATOM   165  C  CA   . ALA   A 1 29  ? -8.329  -15.971 -4.317  1.00 12.57  ? 29  ALA   A CA   1 
ATOM   166  C  C    . ALA   A 1 29  ? -6.942  -15.861 -4.943  1.00 10.74  ? 29  ALA   A C    1 
ATOM   167  O  O    . ALA   A 1 29  ? -6.781  -15.410 -6.087  1.00 12.24  ? 29  ALA   A O    1 
ATOM   168  C  CB   . ALA   A 1 29  ? -9.036  -17.218 -4.846  1.00 13.13  ? 29  ALA   A CB   1 
ATOM   169  N  N    . VAL   A 1 30  ? -5.934  -16.296 -4.191  1.00 12.48  ? 30  VAL   A N    1 
ATOM   170  C  CA   . VAL   A 1 30  ? -4.539  -16.267 -4.612  1.00 13.14  ? 30  VAL   A CA   1 
ATOM   171  C  C    . VAL   A 1 30  ? -3.938  -17.628 -4.290  1.00 12.00  ? 30  VAL   A C    1 
ATOM   172  O  O    . VAL   A 1 30  ? -4.063  -18.111 -3.161  1.00 13.45  ? 30  VAL   A O    1 
ATOM   173  C  CB   . VAL   A 1 30  ? -3.760  -15.168 -3.867  1.00 14.07  ? 30  VAL   A CB   1 
ATOM   174  C  CG1  . VAL   A 1 30  ? -2.304  -15.203 -4.275  1.00 14.62  ? 30  VAL   A CG1  1 
ATOM   175  C  CG2  . VAL   A 1 30  ? -4.366  -13.786 -4.124  1.00 13.41  ? 30  VAL   A CG2  1 
ATOM   176  N  N    . HIS   A 1 31  ? -3.308  -18.253 -5.274  1.00 13.03  ? 31  HIS   A N    1 
ATOM   177  C  CA   . HIS   A 1 31  ? -2.608  -19.516 -5.083  1.00 13.59  ? 31  HIS   A CA   1 
ATOM   178  C  C    . HIS   A 1 31  ? -1.140  -19.317 -5.417  1.00 14.19  ? 31  HIS   A C    1 
ATOM   179  O  O    . HIS   A 1 31  ? -0.808  -18.796 -6.491  1.00 15.06  ? 31  HIS   A O    1 
ATOM   180  C  CB   . HIS   A 1 31  ? -3.180  -20.594 -5.995  1.00 13.56  ? 31  HIS   A CB   1 
ATOM   181  C  CG   . HIS   A 1 31  ? -4.608  -20.934 -5.697  1.00 13.46  ? 31  HIS   A CG   1 
ATOM   182  N  ND1  . HIS   A 1 31  ? -4.977  -22.130 -5.118  1.00 17.36  ? 31  HIS   A ND1  1 
ATOM   183  C  CD2  . HIS   A 1 31  ? -5.753  -20.243 -5.900  1.00 15.95  ? 31  HIS   A CD2  1 
ATOM   184  C  CE1  . HIS   A 1 31  ? -6.291  -22.159 -4.973  1.00 18.90  ? 31  HIS   A CE1  1 
ATOM   185  N  NE2  . HIS   A 1 31  ? -6.788  -21.033 -5.452  1.00 18.20  ? 31  HIS   A NE2  1 
ATOM   186  N  N    . VAL   A 1 32  ? -0.263  -19.761 -4.524  1.00 12.52  ? 32  VAL   A N    1 
ATOM   187  C  CA   . VAL   A 1 32  ? 1.174   -19.675 -4.741  1.00 11.52  ? 32  VAL   A CA   1 
ATOM   188  C  C    . VAL   A 1 32  ? 1.718   -21.076 -4.964  1.00 14.65  ? 32  VAL   A C    1 
ATOM   189  O  O    . VAL   A 1 32  ? 1.333   -22.026 -4.267  1.00 14.17  ? 32  VAL   A O    1 
ATOM   190  C  CB   . VAL   A 1 32  ? 1.876   -19.006 -3.555  1.00 12.36  ? 32  VAL   A CB   1 
ATOM   191  C  CG1  . VAL   A 1 32  ? 3.350   -18.776 -3.878  1.00 15.78  ? 32  VAL   A CG1  1 
ATOM   192  C  CG2  . VAL   A 1 32  ? 1.161   -17.695 -3.175  1.00 13.05  ? 32  VAL   A CG2  1 
ATOM   193  N  N    . PHE   A 1 33  ? 2.611   -21.198 -5.938  1.00 13.24  ? 33  PHE   A N    1 
ATOM   194  C  CA   . PHE   A 1 33  ? 3.263   -22.453 -6.274  1.00 14.20  ? 33  PHE   A CA   1 
ATOM   195  C  C    . PHE   A 1 33  ? 4.766   -22.240 -6.286  1.00 15.92  ? 33  PHE   A C    1 
ATOM   196  O  O    . PHE   A 1 33  ? 5.244   -21.122 -6.458  1.00 14.29  ? 33  PHE   A O    1 
ATOM   197  C  CB   . PHE   A 1 33  ? 2.825   -22.963 -7.657  1.00 16.24  ? 33  PHE   A CB   1 
ATOM   198  C  CG   . PHE   A 1 33  ? 1.335   -23.099 -7.802  1.00 15.52  ? 33  PHE   A CG   1 
ATOM   199  C  CD1  . PHE   A 1 33  ? 0.558   -22.020 -8.196  1.00 16.78  ? 33  PHE   A CD1  1 
ATOM   200  C  CD2  . PHE   A 1 33  ? 0.715   -24.303 -7.520  1.00 17.19  ? 33  PHE   A CD2  1 
ATOM   201  C  CE1  . PHE   A 1 33  ? -0.822  -22.142 -8.308  1.00 17.76  ? 33  PHE   A CE1  1 
ATOM   202  C  CE2  . PHE   A 1 33  ? -0.658  -24.432 -7.628  1.00 19.25  ? 33  PHE   A CE2  1 
ATOM   203  C  CZ   . PHE   A 1 33  ? -1.425  -23.352 -8.020  1.00 16.65  ? 33  PHE   A CZ   1 
ATOM   204  N  N    . ARG   A 1 34  ? 5.516   -23.329 -6.101  1.00 15.88  ? 34  ARG   A N    1 
ATOM   205  C  CA   . ARG   A 1 34  ? 6.974   -23.293 -6.120  1.00 14.39  ? 34  ARG   A CA   1 
ATOM   206  C  C    . ARG   A 1 34  ? 7.444   -24.412 -7.029  1.00 15.54  ? 34  ARG   A C    1 
ATOM   207  O  O    . ARG   A 1 34  ? 6.951   -25.539 -6.930  1.00 16.48  ? 34  ARG   A O    1 
ATOM   208  C  CB   . ARG   A 1 34  ? 7.551   -23.496 -4.717  1.00 16.33  ? 34  ARG   A CB   1 
ATOM   209  C  CG   . ARG   A 1 34  ? 9.073   -23.479 -4.679  1.00 16.37  ? 34  ARG   A CG   1 
ATOM   210  C  CD   . ARG   A 1 34  ? 9.599   -23.753 -3.275  1.00 18.33  ? 34  ARG   A CD   1 
ATOM   211  N  NE   . ARG   A 1 34  ? 11.058  -23.728 -3.270  1.00 19.82  ? 34  ARG   A NE   1 
ATOM   212  C  CZ   . ARG   A 1 34  ? 11.822  -24.743 -3.645  1.00 22.03  ? 34  ARG   A CZ   1 
ATOM   213  N  NH1  . ARG   A 1 34  ? 11.299  -25.912 -3.986  1.00 19.98  ? 34  ARG   A NH1  1 
ATOM   214  N  NH2  . ARG   A 1 34  ? 13.143  -24.581 -3.683  1.00 21.59  ? 34  ARG   A NH2  1 
ATOM   215  N  N    . LYS   A 1 35  ? 8.377   -24.114 -7.922  1.00 14.19  ? 35  LYS   A N    1 
ATOM   216  C  CA   A LYS   A 1 35  ? 8.861   -25.127 -8.851  0.54 16.22  ? 35  LYS   A CA   1 
ATOM   217  C  CA   B LYS   A 1 35  ? 8.851   -25.135 -8.846  0.46 16.22  ? 35  LYS   A CA   1 
ATOM   218  C  C    . LYS   A 1 35  ? 9.725   -26.151 -8.117  1.00 15.35  ? 35  LYS   A C    1 
ATOM   219  O  O    . LYS   A 1 35  ? 10.663  -25.792 -7.394  1.00 18.96  ? 35  LYS   A O    1 
ATOM   220  C  CB   A LYS   A 1 35  ? 9.654   -24.462 -9.975  0.54 19.93  ? 35  LYS   A CB   1 
ATOM   221  C  CB   B LYS   A 1 35  ? 9.596   -24.510 -10.028 0.46 19.96  ? 35  LYS   A CB   1 
ATOM   222  C  CG   A LYS   A 1 35  ? 10.064  -25.417 -11.073 0.54 18.51  ? 35  LYS   A CG   1 
ATOM   223  C  CG   B LYS   A 1 35  ? 8.807   -24.595 -11.327 0.46 24.55  ? 35  LYS   A CG   1 
ATOM   224  C  CD   A LYS   A 1 35  ? 10.796  -24.682 -12.188 0.54 24.18  ? 35  LYS   A CD   1 
ATOM   225  C  CD   B LYS   A 1 35  ? 9.700   -24.750 -12.542 0.46 29.83  ? 35  LYS   A CD   1 
ATOM   226  C  CE   A LYS   A 1 35  ? 9.884   -23.692 -12.905 0.54 32.42  ? 35  LYS   A CE   1 
ATOM   227  C  CE   B LYS   A 1 35  ? 10.437  -23.465 -12.874 0.46 31.77  ? 35  LYS   A CE   1 
ATOM   228  N  NZ   A LYS   A 1 35  ? 8.797   -24.359 -13.685 0.54 32.38  ? 35  LYS   A NZ   1 
ATOM   229  N  NZ   B LYS   A 1 35  ? 11.001  -23.512 -14.256 0.46 32.60  ? 35  LYS   A NZ   1 
ATOM   230  N  N    . ALA   A 1 36  ? 9.392   -27.431 -8.280  1.00 17.76  ? 36  ALA   A N    1 
ATOM   231  C  CA   . ALA   A 1 36  ? 10.123  -28.520 -7.648  1.00 19.17  ? 36  ALA   A CA   1 
ATOM   232  C  C    . ALA   A 1 36  ? 11.297  -28.941 -8.520  1.00 25.26  ? 36  ALA   A C    1 
ATOM   233  O  O    . ALA   A 1 36  ? 11.449  -28.492 -9.656  1.00 22.70  ? 36  ALA   A O    1 
ATOM   234  C  CB   . ALA   A 1 36  ? 9.194   -29.706 -7.405  1.00 24.99  ? 36  ALA   A CB   1 
ATOM   235  N  N    . ALA   A 1 37  ? 12.131  -29.833 -7.972  1.00 28.82  ? 37  ALA   A N    1 
ATOM   236  C  CA   . ALA   A 1 37  ? 13.315  -30.283 -8.698  1.00 34.16  ? 37  ALA   A CA   1 
ATOM   237  C  C    . ALA   A 1 37  ? 12.950  -30.948 -10.020 1.00 29.64  ? 37  ALA   A C    1 
ATOM   238  O  O    . ALA   A 1 37  ? 13.710  -30.854 -10.990 1.00 42.62  ? 37  ALA   A O    1 
ATOM   239  C  CB   . ALA   A 1 37  ? 14.144  -31.226 -7.828  1.00 43.08  ? 37  ALA   A CB   1 
ATOM   240  N  N    . ASP   A 1 38  ? 11.792  -31.602 -10.084 1.00 29.60  ? 38  ASP   A N    1 
ATOM   241  C  CA   . ASP   A 1 38  ? 11.324  -32.250 -11.305 1.00 33.50  ? 38  ASP   A CA   1 
ATOM   242  C  C    . ASP   A 1 38  ? 10.626  -31.291 -12.268 1.00 33.58  ? 38  ASP   A C    1 
ATOM   243  O  O    . ASP   A 1 38  ? 9.994   -31.751 -13.228 1.00 35.15  ? 38  ASP   A O    1 
ATOM   244  C  CB   . ASP   A 1 38  ? 10.420  -33.445 -10.971 1.00 36.18  ? 38  ASP   A CB   1 
ATOM   245  C  CG   . ASP   A 1 38  ? 9.150   -33.043 -10.237 1.00 50.29  ? 38  ASP   A CG   1 
ATOM   246  O  OD1  . ASP   A 1 38  ? 8.958   -31.839 -9.967  1.00 33.38  ? 38  ASP   A OD1  1 
ATOM   247  O  OD2  . ASP   A 1 38  ? 8.336   -33.942 -9.930  1.00 52.49  ? 38  ASP   A OD2  1 
ATOM   248  N  N    . ASP   A 1 39  ? 10.715  -29.983 -12.024 1.00 30.41  ? 39  ASP   A N    1 
ATOM   249  C  CA   . ASP   A 1 39  ? 10.180  -28.918 -12.873 1.00 32.88  ? 39  ASP   A CA   1 
ATOM   250  C  C    . ASP   A 1 39  ? 8.660   -28.798 -12.854 1.00 35.12  ? 39  ASP   A C    1 
ATOM   251  O  O    . ASP   A 1 39  ? 8.097   -28.119 -13.720 1.00 41.37  ? 39  ASP   A O    1 
ATOM   252  C  CB   . ASP   A 1 39  ? 10.703  -28.961 -14.317 1.00 42.42  ? 39  ASP   A CB   1 
ATOM   253  C  CG   . ASP   A 1 39  ? 12.087  -28.367 -14.451 1.00 51.38  ? 39  ASP   A CG   1 
ATOM   254  O  OD1  . ASP   A 1 39  ? 12.449  -27.521 -13.609 1.00 43.07  ? 39  ASP   A OD1  1 
ATOM   255  O  OD2  . ASP   A 1 39  ? 12.810  -28.739 -15.400 1.00 70.19  ? 39  ASP   A OD2  1 
ATOM   256  N  N    . THR   A 1 40  ? 7.978   -29.421 -11.900 1.00 26.96  ? 40  THR   A N    1 
ATOM   257  C  CA   . THR   A 1 40  ? 6.543   -29.224 -11.761 1.00 26.96  ? 40  THR   A CA   1 
ATOM   258  C  C    . THR   A 1 40  ? 6.259   -28.122 -10.741 1.00 24.62  ? 40  THR   A C    1 
ATOM   259  O  O    . THR   A 1 40  ? 7.104   -27.773 -9.914  1.00 25.54  ? 40  THR   A O    1 
ATOM   260  C  CB   . THR   A 1 40  ? 5.862   -30.520 -11.327 1.00 29.86  ? 40  THR   A CB   1 
ATOM   261  O  OG1  . THR   A 1 40  ? 6.320   -30.881 -10.020 1.00 33.46  ? 40  THR   A OG1  1 
ATOM   262  C  CG2  . THR   A 1 40  ? 6.188   -31.647 -12.302 1.00 40.20  ? 40  THR   A CG2  1 
ATOM   263  N  N    . TRP   A 1 41  ? 5.044   -27.576 -10.812 1.00 24.49  ? 41  TRP   A N    1 
ATOM   264  C  CA   . TRP   A 1 41  ? 4.605   -26.507 -9.917  1.00 20.80  ? 41  TRP   A CA   1 
ATOM   265  C  C    . TRP   A 1 41  ? 3.950   -27.127 -8.690  1.00 25.76  ? 41  TRP   A C    1 
ATOM   266  O  O    . TRP   A 1 41  ? 2.810   -27.592 -8.748  1.00 36.58  ? 41  TRP   A O    1 
ATOM   267  C  CB   . TRP   A 1 41  ? 3.630   -25.584 -10.637 1.00 18.98  ? 41  TRP   A CB   1 
ATOM   268  C  CG   . TRP   A 1 41  ? 4.272   -24.659 -11.632 1.00 26.06  ? 41  TRP   A CG   1 
ATOM   269  C  CD1  . TRP   A 1 41  ? 4.104   -24.664 -12.987 1.00 25.24  ? 41  TRP   A CD1  1 
ATOM   270  C  CD2  . TRP   A 1 41  ? 5.184   -23.591 -11.346 1.00 20.50  ? 41  TRP   A CD2  1 
ATOM   271  N  NE1  . TRP   A 1 41  ? 4.849   -23.661 -13.560 1.00 28.83  ? 41  TRP   A NE1  1 
ATOM   272  C  CE2  . TRP   A 1 41  ? 5.524   -22.991 -12.572 1.00 23.92  ? 41  TRP   A CE2  1 
ATOM   273  C  CE3  . TRP   A 1 41  ? 5.746   -23.087 -10.168 1.00 16.84  ? 41  TRP   A CE3  1 
ATOM   274  C  CZ2  . TRP   A 1 41  ? 6.399   -21.911 -12.656 1.00 26.32  ? 41  TRP   A CZ2  1 
ATOM   275  C  CZ3  . TRP   A 1 41  ? 6.607   -22.013 -10.253 1.00 18.00  ? 41  TRP   A CZ3  1 
ATOM   276  C  CH2  . TRP   A 1 41  ? 6.924   -21.437 -11.487 1.00 21.10  ? 41  TRP   A CH2  1 
ATOM   277  N  N    A GLU   A 1 42  ? 4.672   -27.134 -7.574  0.42 18.33  ? 42  GLU   A N    1 
ATOM   278  N  N    B GLU   A 1 42  ? 4.664   -27.119 -7.572  0.58 18.28  ? 42  GLU   A N    1 
ATOM   279  C  CA   A GLU   A 1 42  ? 4.080   -27.697 -6.367  0.42 19.34  ? 42  GLU   A CA   1 
ATOM   280  C  CA   B GLU   A 1 42  ? 4.066   -27.703 -6.380  0.58 19.29  ? 42  GLU   A CA   1 
ATOM   281  C  C    A GLU   A 1 42  ? 3.281   -26.626 -5.631  0.42 19.63  ? 42  GLU   A C    1 
ATOM   282  C  C    B GLU   A 1 42  ? 3.295   -26.637 -5.607  0.58 19.63  ? 42  GLU   A C    1 
ATOM   283  O  O    A GLU   A 1 42  ? 3.713   -25.472 -5.560  0.42 19.34  ? 42  GLU   A O    1 
ATOM   284  O  O    B GLU   A 1 42  ? 3.763   -25.500 -5.483  0.58 19.26  ? 42  GLU   A O    1 
ATOM   285  C  CB   A GLU   A 1 42  ? 5.168   -28.226 -5.436  0.42 24.60  ? 42  GLU   A CB   1 
ATOM   286  C  CB   B GLU   A 1 42  ? 5.148   -28.285 -5.477  0.58 24.66  ? 42  GLU   A CB   1 
ATOM   287  C  CG   A GLU   A 1 42  ? 5.829   -29.505 -5.921  0.42 31.57  ? 42  GLU   A CG   1 
ATOM   288  C  CG   B GLU   A 1 42  ? 5.914   -29.433 -6.112  0.58 31.43  ? 42  GLU   A CG   1 
ATOM   289  C  CD   A GLU   A 1 42  ? 6.751   -30.116 -4.884  0.42 31.32  ? 42  GLU   A CD   1 
ATOM   290  C  CD   B GLU   A 1 42  ? 5.047   -30.658 -6.357  0.58 32.69  ? 42  GLU   A CD   1 
ATOM   291  O  OE1  A GLU   A 1 42  ? 7.295   -29.360 -4.050  0.42 29.32  ? 42  GLU   A OE1  1 
ATOM   292  O  OE1  B GLU   A 1 42  ? 4.218   -30.986 -5.483  0.58 37.96  ? 42  GLU   A OE1  1 
ATOM   293  O  OE2  A GLU   A 1 42  ? 6.931   -31.353 -4.902  0.42 38.16  ? 42  GLU   A OE2  1 
ATOM   294  O  OE2  B GLU   A 1 42  ? 5.194   -31.290 -7.426  0.58 42.77  ? 42  GLU   A OE2  1 
ATOM   295  N  N    . PRO   A 1 43  ? 2.120   -26.972 -5.076  1.00 17.29  ? 43  PRO   A N    1 
ATOM   296  C  CA   . PRO   A 1 43  ? 1.393   -26.013 -4.242  1.00 15.74  ? 43  PRO   A CA   1 
ATOM   297  C  C    . PRO   A 1 43  ? 2.237   -25.575 -3.052  1.00 18.64  ? 43  PRO   A C    1 
ATOM   298  O  O    . PRO   A 1 43  ? 2.922   -26.383 -2.412  1.00 22.99  ? 43  PRO   A O    1 
ATOM   299  C  CB   . PRO   A 1 43  ? 0.157   -26.801 -3.788  1.00 19.49  ? 43  PRO   A CB   1 
ATOM   300  C  CG   . PRO   A 1 43  ? 0.048   -27.962 -4.733  1.00 22.63  ? 43  PRO   A CG   1 
ATOM   301  C  CD   . PRO   A 1 43  ? 1.462   -28.290 -5.134  1.00 20.45  ? 43  PRO   A CD   1 
ATOM   302  N  N    . PHE   A 1 44  ? 2.222   -24.269 -2.787  1.00 14.95  ? 44  PHE   A N    1 
ATOM   303  C  CA   . PHE   A 1 44  ? 3.020   -23.671 -1.726  1.00 14.70  ? 44  PHE   A CA   1 
ATOM   304  C  C    . PHE   A 1 44  ? 2.174   -22.986 -0.667  1.00 16.75  ? 44  PHE   A C    1 
ATOM   305  O  O    . PHE   A 1 44  ? 2.394   -23.197 0.530   1.00 16.26  ? 44  PHE   A O    1 
ATOM   306  C  CB   . PHE   A 1 44  ? 4.057   -22.699 -2.330  1.00 14.78  ? 44  PHE   A CB   1 
ATOM   307  C  CG   . PHE   A 1 44  ? 4.977   -22.071 -1.315  1.00 13.06  ? 44  PHE   A CG   1 
ATOM   308  C  CD1  . PHE   A 1 44  ? 6.047   -22.783 -0.780  1.00 18.31  ? 44  PHE   A CD1  1 
ATOM   309  C  CD2  . PHE   A 1 44  ? 4.775   -20.774 -0.882  1.00 13.78  ? 44  PHE   A CD2  1 
ATOM   310  C  CE1  . PHE   A 1 44  ? 6.878   -22.206 0.164   1.00 17.42  ? 44  PHE   A CE1  1 
ATOM   311  C  CE2  . PHE   A 1 44  ? 5.599   -20.195 0.069   1.00 17.75  ? 44  PHE   A CE2  1 
ATOM   312  C  CZ   . PHE   A 1 44  ? 6.652   -20.913 0.586   1.00 19.37  ? 44  PHE   A CZ   1 
ATOM   313  N  N    . ALA   A 1 45  ? 1.208   -22.164 -1.066  1.00 14.36  ? 45  ALA   A N    1 
ATOM   314  C  CA   . ALA   A 1 45  ? 0.354   -21.481 -0.106  1.00 14.35  ? 45  ALA   A CA   1 
ATOM   315  C  C    . ALA   A 1 45  ? -0.832  -20.916 -0.878  1.00 13.50  ? 45  ALA   A C    1 
ATOM   316  O  O    . ALA   A 1 45  ? -0.767  -20.750 -2.096  1.00 14.23  ? 45  ALA   A O    1 
ATOM   317  C  CB   . ALA   A 1 45  ? 1.116   -20.349 0.599   1.00 15.64  ? 45  ALA   A CB   1 
ATOM   318  N  N    . SER   A 1 46  ? -1.918  -20.620 -0.167  1.00 12.64  ? 46  SER   A N    1 
ATOM   319  C  CA   . SER   A 1 46  ? -3.035  -19.930 -0.802  1.00 12.54  ? 46  SER   A CA   1 
ATOM   320  C  C    . SER   A 1 46  ? -3.811  -19.134 0.240   1.00 12.59  ? 46  SER   A C    1 
ATOM   321  O  O    . SER   A 1 46  ? -3.654  -19.329 1.446   1.00 13.89  ? 46  SER   A O    1 
ATOM   322  C  CB   . SER   A 1 46  ? -3.951  -20.896 -1.571  1.00 12.90  ? 46  SER   A CB   1 
ATOM   323  O  OG   . SER   A 1 46  ? -4.593  -21.802 -0.676  1.00 14.76  ? 46  SER   A OG   1 
ATOM   324  N  N    . GLY   A 1 47  ? -4.646  -18.218 -0.239  1.00 11.92  ? 47  GLY   A N    1 
ATOM   325  C  CA   . GLY   A 1 47  ? -5.512  -17.460 0.646   1.00 14.16  ? 47  GLY   A CA   1 
ATOM   326  C  C    . GLY   A 1 47  ? -6.387  -16.531 -0.165  1.00 11.89  ? 47  GLY   A C    1 
ATOM   327  O  O    . GLY   A 1 47  ? -6.436  -16.618 -1.389  1.00 12.75  ? 47  GLY   A O    1 
ATOM   328  N  N    . LYS   A 1 48  ? -7.069  -15.624 0.533   1.00 13.66  ? 48  LYS   A N    1 
ATOM   329  C  CA   . LYS   A 1 48  ? -7.933  -14.641 -0.105  1.00 14.05  ? 48  LYS   A CA   1 
ATOM   330  C  C    . LYS   A 1 48  ? -7.625  -13.259 0.440   1.00 13.03  ? 48  LYS   A C    1 
ATOM   331  O  O    . LYS   A 1 48  ? -7.321  -13.100 1.625   1.00 14.39  ? 48  LYS   A O    1 
ATOM   332  C  CB   . LYS   A 1 48  ? -9.417  -14.944 0.155   1.00 23.27  ? 48  LYS   A CB   1 
ATOM   333  C  CG   . LYS   A 1 48  ? -10.000 -16.049 -0.721  1.00 28.39  ? 48  LYS   A CG   1 
ATOM   334  C  CD   . LYS   A 1 48  ? -11.456 -16.274 -0.361  1.00 32.23  ? 48  LYS   A CD   1 
ATOM   335  C  CE   . LYS   A 1 48  ? -11.938 -17.655 -0.759  1.00 38.23  ? 48  LYS   A CE   1 
ATOM   336  N  NZ   . LYS   A 1 48  ? -12.627 -17.682 -2.073  1.00 27.28  ? 48  LYS   A NZ   1 
ATOM   337  N  N    . THR   A 1 49  ? -7.708  -12.255 -0.438  1.00 13.37  ? 49  THR   A N    1 
ATOM   338  C  CA   . THR   A 1 49  ? -7.482  -10.887 0.012   1.00 12.74  ? 49  THR   A CA   1 
ATOM   339  C  C    . THR   A 1 49  ? -8.568  -10.434 0.987   1.00 13.07  ? 49  THR   A C    1 
ATOM   340  O  O    . THR   A 1 49  ? -9.738  -10.824 0.893   1.00 14.94  ? 49  THR   A O    1 
ATOM   341  C  CB   . THR   A 1 49  ? -7.397  -9.904  -1.162  1.00 12.39  ? 49  THR   A CB   1 
ATOM   342  O  OG1  . THR   A 1 49  ? -8.632  -9.886  -1.884  1.00 13.58  ? 49  THR   A OG1  1 
ATOM   343  C  CG2  . THR   A 1 49  ? -6.230  -10.236 -2.095  1.00 14.30  ? 49  THR   A CG2  1 
ATOM   344  N  N    . SER   A 1 50  ? -8.164  -9.575  1.903   1.00 14.28  ? 50  SER   A N    1 
ATOM   345  C  CA   . SER   A 1 50  ? -9.033  -9.057  2.945   1.00 15.48  ? 50  SER   A CA   1 
ATOM   346  C  C    . SER   A 1 50  ? -9.798  -7.843  2.432   1.00 17.76  ? 50  SER   A C    1 
ATOM   347  O  O    . SER   A 1 50  ? -9.719  -7.471  1.256   1.00 16.56  ? 50  SER   A O    1 
ATOM   348  C  CB   . SER   A 1 50  ? -8.177  -8.645  4.127   1.00 16.98  ? 50  SER   A CB   1 
ATOM   349  O  OG   . SER   A 1 50  ? -7.432  -7.493  3.762   1.00 18.86  ? 50  SER   A OG   1 
ATOM   350  N  N    . GLU   A 1 51  ? -10.522 -7.180  3.342   1.00 17.51  ? 51  GLU   A N    1 
ATOM   351  C  CA   B GLU   A 1 51  ? -11.248 -5.980  2.953   0.52 19.80  ? 51  GLU   A CA   1 
ATOM   352  C  CA   C GLU   A 1 51  ? -11.248 -5.967  2.985   0.48 19.85  ? 51  GLU   A CA   1 
ATOM   353  C  C    . GLU   A 1 51  ? -10.314 -4.842  2.551   1.00 17.25  ? 51  GLU   A C    1 
ATOM   354  O  O    . GLU   A 1 51  ? -10.761 -3.902  1.886   1.00 20.52  ? 51  GLU   A O    1 
ATOM   355  C  CB   B GLU   A 1 51  ? -12.209 -5.541  4.063   0.52 27.14  ? 51  GLU   A CB   1 
ATOM   356  C  CB   C GLU   A 1 51  ? -12.115 -5.508  4.162   0.48 26.97  ? 51  GLU   A CB   1 
ATOM   357  C  CG   B GLU   A 1 51  ? -11.548 -4.841  5.227   0.52 31.01  ? 51  GLU   A CG   1 
ATOM   358  C  CG   C GLU   A 1 51  ? -13.163 -6.523  4.596   0.48 24.93  ? 51  GLU   A CG   1 
ATOM   359  C  CD   B GLU   A 1 51  ? -12.561 -4.219  6.172   0.52 43.52  ? 51  GLU   A CD   1 
ATOM   360  C  CD   C GLU   A 1 51  ? -14.238 -6.752  3.550   0.48 27.56  ? 51  GLU   A CD   1 
ATOM   361  O  OE1  B GLU   A 1 51  ? -13.593 -4.869  6.448   0.52 42.57  ? 51  GLU   A OE1  1 
ATOM   362  O  OE1  C GLU   A 1 51  ? -14.539 -5.812  2.783   0.48 32.66  ? 51  GLU   A OE1  1 
ATOM   363  O  OE2  B GLU   A 1 51  ? -12.334 -3.077  6.626   0.52 38.49  ? 51  GLU   A OE2  1 
ATOM   364  O  OE2  C GLU   A 1 51  ? -14.790 -7.872  3.498   0.48 37.95  ? 51  GLU   A OE2  1 
ATOM   365  N  N    . SER   A 1 52  ? -9.034  -4.913  2.913   1.00 15.80  ? 52  SER   A N    1 
ATOM   366  C  CA   . SER   A 1 52  ? -8.031  -3.945  2.478   1.00 17.17  ? 52  SER   A CA   1 
ATOM   367  C  C    . SER   A 1 52  ? -7.371  -4.315  1.146   1.00 14.16  ? 52  SER   A C    1 
ATOM   368  O  O    . SER   A 1 52  ? -6.491  -3.580  0.682   1.00 15.05  ? 52  SER   A O    1 
ATOM   369  C  CB   . SER   A 1 52  ? -6.948  -3.779  3.554   1.00 20.54  ? 52  SER   A CB   1 
ATOM   370  O  OG   . SER   A 1 52  ? -6.138  -4.937  3.642   1.00 24.87  ? 52  SER   A OG   1 
ATOM   371  N  N    . GLY   A 1 53  ? -7.751  -5.442  0.540   1.00 13.21  ? 53  GLY   A N    1 
ATOM   372  C  CA   . GLY   A 1 53  ? -7.093  -5.931  -0.659  1.00 13.36  ? 53  GLY   A CA   1 
ATOM   373  C  C    . GLY   A 1 53  ? -5.795  -6.664  -0.415  1.00 12.81  ? 53  GLY   A C    1 
ATOM   374  O  O    . GLY   A 1 53  ? -5.106  -7.010  -1.381  1.00 13.32  ? 53  GLY   A O    1 
ATOM   375  N  N    . GLU   A 1 54  ? -5.439  -6.906  0.841   1.00 14.04  ? 54  GLU   A N    1 
ATOM   376  C  CA   . GLU   A 1 54  ? -4.149  -7.473  1.188   1.00 13.37  ? 54  GLU   A CA   1 
ATOM   377  C  C    . GLU   A 1 54  ? -4.293  -8.915  1.646   1.00 12.97  ? 54  GLU   A C    1 
ATOM   378  O  O    . GLU   A 1 54  ? -5.304  -9.314  2.229   1.00 14.69  ? 54  GLU   A O    1 
ATOM   379  C  CB   . GLU   A 1 54  ? -3.470  -6.634  2.275   1.00 16.01  ? 54  GLU   A CB   1 
ATOM   380  C  CG   . GLU   A 1 54  ? -3.164  -5.218  1.811   1.00 21.10  ? 54  GLU   A CG   1 
ATOM   381  C  CD   . GLU   A 1 54  ? -2.393  -4.400  2.829   1.00 30.22  ? 54  GLU   A CD   1 
ATOM   382  O  OE1  . GLU   A 1 54  ? -2.100  -4.911  3.931   1.00 31.07  ? 54  GLU   A OE1  1 
ATOM   383  O  OE2  . GLU   A 1 54  ? -2.083  -3.231  2.518   1.00 33.23  ? 54  GLU   A OE2  1 
ATOM   384  N  N    . LEU   A 1 55  ? -3.276  -9.705  1.341   1.00 12.79  ? 55  LEU   A N    1 
ATOM   385  C  CA   . LEU   A 1 55  ? -3.200  -11.089 1.784   1.00 12.46  ? 55  LEU   A CA   1 
ATOM   386  C  C    . LEU   A 1 55  ? -1.867  -11.261 2.483   1.00 17.40  ? 55  LEU   A C    1 
ATOM   387  O  O    . LEU   A 1 55  ? -0.808  -11.139 1.858   1.00 15.45  ? 55  LEU   A O    1 
ATOM   388  C  CB   . LEU   A 1 55  ? -3.329  -12.034 0.596   1.00 13.35  ? 55  LEU   A CB   1 
ATOM   389  C  CG   . LEU   A 1 55  ? -3.131  -13.527 0.841   1.00 14.26  ? 55  LEU   A CG   1 
ATOM   390  C  CD1  . LEU   A 1 55  ? -4.017  -14.021 1.980   1.00 17.81  ? 55  LEU   A CD1  1 
ATOM   391  C  CD2  . LEU   A 1 55  ? -3.482  -14.238 -0.460  1.00 16.21  ? 55  LEU   A CD2  1 
ATOM   392  N  N    . HIS   A 1 56  ? -1.938  -11.488 3.786   1.00 18.68  ? 56  HIS   A N    1 
ATOM   393  C  CA   . HIS   A 1 56  ? -0.799  -11.715 4.657   1.00 21.77  ? 56  HIS   A CA   1 
ATOM   394  C  C    . HIS   A 1 56  ? -0.844  -13.157 5.143   1.00 15.91  ? 56  HIS   A C    1 
ATOM   395  O  O    . HIS   A 1 56  ? -1.851  -13.859 5.011   1.00 21.00  ? 56  HIS   A O    1 
ATOM   396  C  CB   . HIS   A 1 56  ? -0.860  -10.777 5.873   1.00 22.35  ? 56  HIS   A CB   1 
ATOM   397  C  CG   . HIS   A 1 56  ? -0.875  -9.322  5.524   1.00 25.10  ? 56  HIS   A CG   1 
ATOM   398  N  ND1  . HIS   A 1 56  ? 0.276   -8.571  5.417   1.00 38.46  ? 56  HIS   A ND1  1 
ATOM   399  C  CD2  . HIS   A 1 56  ? -1.900  -8.478  5.258   1.00 30.00  ? 56  HIS   A CD2  1 
ATOM   400  C  CE1  . HIS   A 1 56  ? -0.039  -7.328  5.098   1.00 31.63  ? 56  HIS   A CE1  1 
ATOM   401  N  NE2  . HIS   A 1 56  ? -1.353  -7.244  4.996   1.00 31.94  ? 56  HIS   A NE2  1 
ATOM   402  N  N    . GLY   A 1 57  ? 0.268   -13.589 5.726   1.00 20.14  ? 57  GLY   A N    1 
ATOM   403  C  CA   . GLY   A 1 57  ? 0.292   -14.883 6.372   1.00 20.79  ? 57  GLY   A CA   1 
ATOM   404  C  C    . GLY   A 1 57  ? 0.436   -16.065 5.449   1.00 25.45  ? 57  GLY   A C    1 
ATOM   405  O  O    . GLY   A 1 57  ? 0.146   -17.193 5.861   1.00 26.23  ? 57  GLY   A O    1 
ATOM   406  N  N    . LEU   A 1 58  ? 0.870   -15.851 4.204   1.00 17.17  ? 58  LEU   A N    1 
ATOM   407  C  CA   . LEU   A 1 58  ? 0.998   -16.968 3.279   1.00 15.14  ? 58  LEU   A CA   1 
ATOM   408  C  C    . LEU   A 1 58  ? 2.093   -17.932 3.707   1.00 17.16  ? 58  LEU   A C    1 
ATOM   409  O  O    . LEU   A 1 58  ? 1.938   -19.152 3.553   1.00 20.45  ? 58  LEU   A O    1 
ATOM   410  C  CB   . LEU   A 1 58  ? 1.267   -16.454 1.866   1.00 15.57  ? 58  LEU   A CB   1 
ATOM   411  C  CG   . LEU   A 1 58  ? 0.037   -15.881 1.155   1.00 15.64  ? 58  LEU   A CG   1 
ATOM   412  C  CD1  . LEU   A 1 58  ? 0.459   -15.093 -0.077  1.00 20.99  ? 58  LEU   A CD1  1 
ATOM   413  C  CD2  . LEU   A 1 58  ? -0.915  -17.013 0.765   1.00 20.08  ? 58  LEU   A CD2  1 
ATOM   414  N  N    . THR   A 1 59  ? 3.206   -17.417 4.225   1.00 17.15  ? 59  THR   A N    1 
ATOM   415  C  CA   . THR   A 1 59  ? 4.348   -18.274 4.519   1.00 16.38  ? 59  THR   A CA   1 
ATOM   416  C  C    . THR   A 1 59  ? 5.159   -17.683 5.664   1.00 18.43  ? 59  THR   A C    1 
ATOM   417  O  O    . THR   A 1 59  ? 4.818   -16.647 6.241   1.00 20.65  ? 59  THR   A O    1 
ATOM   418  C  CB   . THR   A 1 59  ? 5.203   -18.475 3.264   1.00 18.37  ? 59  THR   A CB   1 
ATOM   419  O  OG1  . THR   A 1 59  ? 6.172   -19.508 3.504   1.00 17.63  ? 59  THR   A OG1  1 
ATOM   420  C  CG2  . THR   A 1 59  ? 5.910   -17.180 2.886   1.00 20.31  ? 59  THR   A CG2  1 
ATOM   421  N  N    . THR   A 1 60  ? 6.240   -18.375 6.005   1.00 21.32  ? 60  THR   A N    1 
ATOM   422  C  CA   . THR   A 1 60  ? 7.154   -17.959 7.051   1.00 19.09  ? 60  THR   A CA   1 
ATOM   423  C  C    . THR   A 1 60  ? 8.548   -17.848 6.454   1.00 20.20  ? 60  THR   A C    1 
ATOM   424  O  O    . THR   A 1 60  ? 8.830   -18.392 5.379   1.00 17.47  ? 60  THR   A O    1 
ATOM   425  C  CB   . THR   A 1 60  ? 7.203   -19.002 8.178   1.00 22.73  ? 60  THR   A CB   1 
ATOM   426  O  OG1  . THR   A 1 60  ? 7.699   -20.244 7.661   1.00 21.51  ? 60  THR   A OG1  1 
ATOM   427  C  CG2  . THR   A 1 60  ? 5.816   -19.236 8.764   1.00 27.37  ? 60  THR   A CG2  1 
ATOM   428  N  N    A GLU   A 1 61  ? 9.435   -17.157 7.170   0.42 20.13  ? 61  GLU   A N    1 
ATOM   429  N  N    B GLU   A 1 61  ? 9.424   -17.141 7.170   0.58 20.09  ? 61  GLU   A N    1 
ATOM   430  C  CA   A GLU   A 1 61  ? 10.812  -17.048 6.695   0.42 23.08  ? 61  GLU   A CA   1 
ATOM   431  C  CA   B GLU   A 1 61  ? 10.817  -17.042 6.744   0.58 23.07  ? 61  GLU   A CA   1 
ATOM   432  C  C    A GLU   A 1 61  ? 11.481  -18.416 6.582   0.42 22.81  ? 61  GLU   A C    1 
ATOM   433  C  C    B GLU   A 1 61  ? 11.438  -18.424 6.559   0.58 22.81  ? 61  GLU   A C    1 
ATOM   434  O  O    A GLU   A 1 61  ? 12.307  -18.628 5.687   0.42 22.67  ? 61  GLU   A O    1 
ATOM   435  O  O    B GLU   A 1 61  ? 12.181  -18.655 5.598   0.58 22.68  ? 61  GLU   A O    1 
ATOM   436  C  CB   A GLU   A 1 61  ? 11.622  -16.101 7.585   0.42 29.77  ? 61  GLU   A CB   1 
ATOM   437  C  CB   B GLU   A 1 61  ? 11.618  -16.222 7.757   0.58 29.80  ? 61  GLU   A CB   1 
ATOM   438  C  CG   A GLU   A 1 61  ? 13.039  -15.876 7.086   0.42 29.43  ? 61  GLU   A CG   1 
ATOM   439  C  CG   B GLU   A 1 61  ? 11.200  -14.761 7.847   0.58 25.76  ? 61  GLU   A CG   1 
ATOM   440  C  CD   A GLU   A 1 61  ? 13.768  -14.766 7.814   0.42 39.31  ? 61  GLU   A CD   1 
ATOM   441  C  CD   B GLU   A 1 61  ? 11.846  -14.037 9.014   0.58 34.76  ? 61  GLU   A CD   1 
ATOM   442  O  OE1  A GLU   A 1 61  ? 13.154  -13.709 8.069   0.42 39.63  ? 61  GLU   A OE1  1 
ATOM   443  O  OE1  B GLU   A 1 61  ? 12.193  -14.703 10.011  0.58 40.09  ? 61  GLU   A OE1  1 
ATOM   444  O  OE2  A GLU   A 1 61  ? 14.963  -14.956 8.128   0.42 39.26  ? 61  GLU   A OE2  1 
ATOM   445  O  OE2  B GLU   A 1 61  ? 12.010  -12.802 8.934   0.58 40.69  ? 61  GLU   A OE2  1 
ATOM   446  N  N    . GLU   A 1 62  ? 11.128  -19.361 7.459   1.00 18.43  ? 62  GLU   A N    1 
ATOM   447  C  CA   . GLU   A 1 62  ? 11.710  -20.704 7.375   1.00 19.01  ? 62  GLU   A CA   1 
ATOM   448  C  C    . GLU   A 1 62  ? 11.277  -21.437 6.106   1.00 15.79  ? 62  GLU   A C    1 
ATOM   449  O  O    . GLU   A 1 62  ? 12.099  -22.066 5.429   1.00 18.08  ? 62  GLU   A O    1 
ATOM   450  C  CB   . GLU   A 1 62  ? 11.344  -21.533 8.614   1.00 22.38  ? 62  GLU   A CB   1 
ATOM   451  C  CG   . GLU   A 1 62  ? 12.339  -21.430 9.738   1.00 33.85  ? 62  GLU   A CG   1 
ATOM   452  C  CD   . GLU   A 1 62  ? 12.082  -22.427 10.855  1.00 28.82  ? 62  GLU   A CD   1 
ATOM   453  O  OE1  . GLU   A 1 62  ? 11.440  -23.479 10.612  1.00 23.15  ? 62  GLU   A OE1  1 
ATOM   454  O  OE2  . GLU   A 1 62  ? 12.532  -22.151 11.985  1.00 33.40  ? 62  GLU   A OE2  1 
ATOM   455  N  N    . GLU   A 1 63  ? 9.986   -21.390 5.777   1.00 15.57  ? 63  GLU   A N    1 
ATOM   456  C  CA   . GLU   A 1 63  ? 9.467   -22.175 4.666   1.00 13.97  ? 63  GLU   A CA   1 
ATOM   457  C  C    . GLU   A 1 63  ? 9.708   -21.532 3.309   1.00 11.29  ? 63  GLU   A C    1 
ATOM   458  O  O    . GLU   A 1 63  ? 9.743   -22.237 2.303   1.00 15.01  ? 63  GLU   A O    1 
ATOM   459  C  CB   . GLU   A 1 63  ? 7.969   -22.427 4.840   1.00 18.52  ? 63  GLU   A CB   1 
ATOM   460  C  CG   . GLU   A 1 63  ? 7.620   -23.228 6.098   1.00 23.34  ? 63  GLU   A CG   1 
ATOM   461  C  CD   . GLU   A 1 63  ? 7.492   -24.706 5.852   1.00 47.36  ? 63  GLU   A CD   1 
ATOM   462  O  OE1  . GLU   A 1 63  ? 8.330   -25.265 5.113   1.00 43.86  ? 63  GLU   A OE1  1 
ATOM   463  O  OE2  . GLU   A 1 63  ? 6.548   -25.315 6.409   1.00 43.05  ? 63  GLU   A OE2  1 
ATOM   464  N  N    . PHE   A 1 64  ? 9.876   -20.213 3.276   1.00 13.51  ? 64  PHE   A N    1 
ATOM   465  C  CA   . PHE   A 1 64  ? 10.030  -19.464 2.029   1.00 13.66  ? 64  PHE   A CA   1 
ATOM   466  C  C    . PHE   A 1 64  ? 11.500  -19.482 1.607   1.00 13.39  ? 64  PHE   A C    1 
ATOM   467  O  O    . PHE   A 1 64  ? 12.218  -18.483 1.679   1.00 14.86  ? 64  PHE   A O    1 
ATOM   468  C  CB   . PHE   A 1 64  ? 9.537   -18.045 2.261   1.00 14.84  ? 64  PHE   A CB   1 
ATOM   469  C  CG   . PHE   A 1 64  ? 9.374   -17.213 1.010   1.00 14.48  ? 64  PHE   A CG   1 
ATOM   470  C  CD1  . PHE   A 1 64  ? 8.898   -17.752 -0.164  1.00 16.10  ? 64  PHE   A CD1  1 
ATOM   471  C  CD2  . PHE   A 1 64  ? 9.642   -15.861 1.071   1.00 17.02  ? 64  PHE   A CD2  1 
ATOM   472  C  CE1  . PHE   A 1 64  ? 8.734   -16.944 -1.301  1.00 16.76  ? 64  PHE   A CE1  1 
ATOM   473  C  CE2  . PHE   A 1 64  ? 9.467   -15.050 -0.044  1.00 18.16  ? 64  PHE   A CE2  1 
ATOM   474  C  CZ   . PHE   A 1 64  ? 9.018   -15.591 -1.216  1.00 15.31  ? 64  PHE   A CZ   1 
ATOM   475  N  N    . VAL   A 1 65  ? 11.943  -20.657 1.178   1.00 14.61  ? 65  VAL   A N    1 
ATOM   476  C  CA   . VAL   A 1 65  ? 13.331  -20.860 0.766   1.00 14.83  ? 65  VAL   A CA   1 
ATOM   477  C  C    . VAL   A 1 65  ? 13.551  -20.305 -0.635  1.00 13.29  ? 65  VAL   A C    1 
ATOM   478  O  O    . VAL   A 1 65  ? 12.606  -19.851 -1.301  1.00 13.99  ? 65  VAL   A O    1 
ATOM   479  C  CB   . VAL   A 1 65  ? 13.689  -22.356 0.812   1.00 11.09  ? 65  VAL   A CB   1 
ATOM   480  C  CG1  . VAL   A 1 65  ? 13.631  -22.865 2.264   1.00 16.56  ? 65  VAL   A CG1  1 
ATOM   481  C  CG2  . VAL   A 1 65  ? 12.745  -23.135 -0.076  1.00 14.03  ? 65  VAL   A CG2  1 
ATOM   482  N  N    . GLU   A 1 66  ? 14.797  -20.369 -1.108  1.00 13.99  ? 66  GLU   A N    1 
ATOM   483  C  CA   . GLU   A 1 66  ? 15.080  -20.008 -2.496  1.00 13.63  ? 66  GLU   A CA   1 
ATOM   484  C  C    . GLU   A 1 66  ? 14.250  -20.864 -3.438  1.00 13.77  ? 66  GLU   A C    1 
ATOM   485  O  O    . GLU   A 1 66  ? 13.999  -22.047 -3.190  1.00 15.09  ? 66  GLU   A O    1 
ATOM   486  C  CB   . GLU   A 1 66  ? 16.564  -20.218 -2.829  1.00 17.80  ? 66  GLU   A CB   1 
ATOM   487  C  CG   . GLU   A 1 66  ? 16.984  -19.619 -4.190  1.00 18.16  ? 66  GLU   A CG   1 
ATOM   488  C  CD   . GLU   A 1 66  ? 16.642  -20.487 -5.402  1.00 23.45  ? 66  GLU   A CD   1 
ATOM   489  O  OE1  . GLU   A 1 66  ? 16.500  -21.723 -5.271  1.00 24.79  ? 66  GLU   A OE1  1 
ATOM   490  O  OE2  . GLU   A 1 66  ? 16.496  -19.924 -6.514  1.00 25.91  ? 66  GLU   A OE2  1 
ATOM   491  N  N    . GLY   A 1 67  ? 13.833  -20.265 -4.544  1.00 14.03  ? 67  GLY   A N    1 
ATOM   492  C  CA   . GLY   A 1 67  ? 13.199  -21.037 -5.587  1.00 14.46  ? 67  GLY   A CA   1 
ATOM   493  C  C    . GLY   A 1 67  ? 12.492  -20.130 -6.565  1.00 14.70  ? 67  GLY   A C    1 
ATOM   494  O  O    . GLY   A 1 67  ? 12.530  -18.908 -6.451  1.00 13.53  ? 67  GLY   A O    1 
ATOM   495  N  N    . ILE   A 1 68  ? 11.839  -20.758 -7.530  1.00 12.72  ? 68  ILE   A N    1 
ATOM   496  C  CA   . ILE   A 1 68  ? 11.006  -20.046 -8.492  1.00 12.74  ? 68  ILE   A CA   1 
ATOM   497  C  C    . ILE   A 1 68  ? 9.567   -20.189 -8.038  1.00 13.46  ? 68  ILE   A C    1 
ATOM   498  O  O    . ILE   A 1 68  ? 9.075   -21.310 -7.851  1.00 14.13  ? 68  ILE   A O    1 
ATOM   499  C  CB   . ILE   A 1 68  ? 11.197  -20.587 -9.911  1.00 15.01  ? 68  ILE   A CB   1 
ATOM   500  C  CG1  . ILE   A 1 68  ? 12.660  -20.420 -10.327 1.00 17.47  ? 68  ILE   A CG1  1 
ATOM   501  C  CG2  . ILE   A 1 68  ? 10.270  -19.835 -10.863 1.00 17.23  ? 68  ILE   A CG2  1 
ATOM   502  C  CD1  . ILE   A 1 68  ? 12.982  -20.984 -11.694 1.00 22.56  ? 68  ILE   A CD1  1 
ATOM   503  N  N    . TYR   A 1 69  ? 8.908   -19.066 -7.811  1.00 13.19  ? 69  TYR   A N    1 
ATOM   504  C  CA   . TYR   A 1 69  ? 7.558   -19.053 -7.288  1.00 11.92  ? 69  TYR   A CA   1 
ATOM   505  C  C    . TYR   A 1 69  ? 6.619   -18.476 -8.333  1.00 14.08  ? 69  TYR   A C    1 
ATOM   506  O  O    . TYR   A 1 69  ? 7.003   -17.627 -9.143  1.00 12.41  ? 69  TYR   A O    1 
ATOM   507  C  CB   . TYR   A 1 69  ? 7.485   -18.218 -6.016  1.00 12.88  ? 69  TYR   A CB   1 
ATOM   508  C  CG   . TYR   A 1 69  ? 8.199   -18.881 -4.857  1.00 13.45  ? 69  TYR   A CG   1 
ATOM   509  C  CD1  . TYR   A 1 69  ? 9.566   -18.743 -4.700  1.00 14.10  ? 69  TYR   A CD1  1 
ATOM   510  C  CD2  . TYR   A 1 69  ? 7.496   -19.659 -3.941  1.00 14.33  ? 69  TYR   A CD2  1 
ATOM   511  C  CE1  . TYR   A 1 69  ? 10.228  -19.361 -3.647  1.00 13.74  ? 69  TYR   A CE1  1 
ATOM   512  C  CE2  . TYR   A 1 69  ? 8.145   -20.279 -2.894  1.00 14.01  ? 69  TYR   A CE2  1 
ATOM   513  C  CZ   . TYR   A 1 69  ? 9.502   -20.119 -2.753  1.00 14.18  ? 69  TYR   A CZ   1 
ATOM   514  O  OH   . TYR   A 1 69  ? 10.126  -20.739 -1.692  1.00 14.63  ? 69  TYR   A OH   1 
ATOM   515  N  N    . LYS   A 1 70  ? 5.388   -18.963 -8.325  1.00 11.65  ? 70  LYS   A N    1 
ATOM   516  C  CA   . LYS   A 1 70  ? 4.326   -18.433 -9.170  1.00 12.90  ? 70  LYS   A CA   1 
ATOM   517  C  C    . LYS   A 1 70  ? 3.170   -18.040 -8.267  1.00 13.82  ? 70  LYS   A C    1 
ATOM   518  O  O    . LYS   A 1 70  ? 2.659   -18.873 -7.505  1.00 15.31  ? 70  LYS   A O    1 
ATOM   519  C  CB   . LYS   A 1 70  ? 3.864   -19.483 -10.181 1.00 15.65  ? 70  LYS   A CB   1 
ATOM   520  C  CG   . LYS   A 1 70  ? 2.634   -19.039 -10.940 1.00 16.45  ? 70  LYS   A CG   1 
ATOM   521  C  CD   . LYS   A 1 70  ? 2.348   -19.931 -12.134 1.00 25.79  ? 70  LYS   A CD   1 
ATOM   522  C  CE   . LYS   A 1 70  ? 2.039   -21.346 -11.695 1.00 28.19  ? 70  LYS   A CE   1 
ATOM   523  N  NZ   . LYS   A 1 70  ? 1.412   -22.125 -12.808 1.00 44.63  ? 70  LYS   A NZ   1 
ATOM   524  N  N    . VAL   A 1 71  ? 2.776   -16.777 -8.342  1.00 12.72  ? 71  VAL   A N    1 
ATOM   525  C  CA   . VAL   A 1 71  ? 1.618   -16.248 -7.632  1.00 13.50  ? 71  VAL   A CA   1 
ATOM   526  C  C    . VAL   A 1 71  ? 0.519   -16.103 -8.662  1.00 15.01  ? 71  VAL   A C    1 
ATOM   527  O  O    . VAL   A 1 71  ? 0.635   -15.306 -9.602  1.00 14.50  ? 71  VAL   A O    1 
ATOM   528  C  CB   . VAL   A 1 71  ? 1.939   -14.904 -6.970  1.00 12.52  ? 71  VAL   A CB   1 
ATOM   529  C  CG1  . VAL   A 1 71  ? 0.701   -14.272 -6.333  1.00 17.51  ? 71  VAL   A CG1  1 
ATOM   530  C  CG2  . VAL   A 1 71  ? 3.048   -15.082 -5.930  1.00 16.13  ? 71  VAL   A CG2  1 
ATOM   531  N  N    . GLU   A 1 72  ? -0.524  -16.906 -8.514  1.00 12.37  ? 72  GLU   A N    1 
ATOM   532  C  CA   . GLU   A 1 72  ? -1.669  -16.908 -9.411  1.00 13.78  ? 72  GLU   A CA   1 
ATOM   533  C  C    . GLU   A 1 72  ? -2.814  -16.170 -8.724  1.00 13.59  ? 72  GLU   A C    1 
ATOM   534  O  O    . GLU   A 1 72  ? -3.268  -16.579 -7.653  1.00 14.43  ? 72  GLU   A O    1 
ATOM   535  C  CB   . GLU   A 1 72  ? -2.071  -18.357 -9.705  1.00 16.34  ? 72  GLU   A CB   1 
ATOM   536  C  CG   . GLU   A 1 72  ? -3.037  -18.595 -10.814 1.00 30.07  ? 72  GLU   A CG   1 
ATOM   537  C  CD   . GLU   A 1 72  ? -3.652  -19.969 -10.779 1.00 40.46  ? 72  GLU   A CD   1 
ATOM   538  O  OE1  . GLU   A 1 72  ? -4.826  -20.038 -10.343 1.00 45.92  ? 72  GLU   A OE1  1 
ATOM   539  O  OE2  . GLU   A 1 72  ? -2.961  -20.939 -11.015 1.00 38.95  ? 72  GLU   A OE2  1 
ATOM   540  N  N    . ILE   A 1 73  ? -3.272  -15.069 -9.325  1.00 11.70  ? 73  ILE   A N    1 
ATOM   541  C  CA   . ILE   A 1 73  ? -4.336  -14.245 -8.757  1.00 12.67  ? 73  ILE   A CA   1 
ATOM   542  C  C    . ILE   A 1 73  ? -5.584  -14.524 -9.569  1.00 13.92  ? 73  ILE   A C    1 
ATOM   543  O  O    . ILE   A 1 73  ? -5.577  -14.340 -10.791 1.00 13.56  ? 73  ILE   A O    1 
ATOM   544  C  CB   . ILE   A 1 73  ? -3.958  -12.756 -8.799  1.00 14.01  ? 73  ILE   A CB   1 
ATOM   545  C  CG1  . ILE   A 1 73  ? -2.653  -12.511 -8.044  1.00 14.93  ? 73  ILE   A CG1  1 
ATOM   546  C  CG2  . ILE   A 1 73  ? -5.066  -11.909 -8.243  1.00 13.88  ? 73  ILE   A CG2  1 
ATOM   547  C  CD1  . ILE   A 1 73  ? -2.135  -11.108 -8.212  1.00 16.96  ? 73  ILE   A CD1  1 
ATOM   548  N  N    . ASP   A 1 74  ? -6.635  -15.007 -8.914  1.00 11.75  ? 74  ASP   A N    1 
ATOM   549  C  CA   . ASP   A 1 74  ? -7.792  -15.559 -9.624  1.00 12.68  ? 74  ASP   A CA   1 
ATOM   550  C  C    . ASP   A 1 74  ? -8.726  -14.414 -10.009 1.00 14.62  ? 74  ASP   A C    1 
ATOM   551  O  O    . ASP   A 1 74  ? -9.802  -14.221 -9.453  1.00 14.36  ? 74  ASP   A O    1 
ATOM   552  C  CB   . ASP   A 1 74  ? -8.468  -16.646 -8.790  1.00 15.56  ? 74  ASP   A CB   1 
ATOM   553  C  CG   . ASP   A 1 74  ? -7.592  -17.879 -8.630  1.00 25.46  ? 74  ASP   A CG   1 
ATOM   554  O  OD1  . ASP   A 1 74  ? -6.686  -18.095 -9.462  1.00 21.86  ? 74  ASP   A OD1  1 
ATOM   555  O  OD2  . ASP   A 1 74  ? -7.795  -18.650 -7.684  1.00 21.94  ? 74  ASP   A OD2  1 
ATOM   556  N  N    . THR   A 1 75  ? -8.298  -13.670 -11.037 1.00 14.51  ? 75  THR   A N    1 
ATOM   557  C  CA   . THR   A 1 75  ? -9.003  -12.455 -11.444 1.00 14.94  ? 75  THR   A CA   1 
ATOM   558  C  C    . THR   A 1 75  ? -10.325 -12.760 -12.132 1.00 15.48  ? 75  THR   A C    1 
ATOM   559  O  O    . THR   A 1 75  ? -11.288 -12.006 -11.973 1.00 14.44  ? 75  THR   A O    1 
ATOM   560  C  CB   . THR   A 1 75  ? -8.116  -11.617 -12.363 1.00 12.69  ? 75  THR   A CB   1 
ATOM   561  O  OG1  . THR   A 1 75  ? -7.767  -12.375 -13.522 1.00 13.37  ? 75  THR   A OG1  1 
ATOM   562  C  CG2  . THR   A 1 75  ? -6.832  -11.221 -11.640 1.00 14.66  ? 75  THR   A CG2  1 
ATOM   563  N  N    . LYS   A 1 76  ? -10.395 -13.844 -12.912 1.00 15.76  ? 76  LYS   A N    1 
ATOM   564  C  CA   . LYS   A 1 76  ? -11.648 -14.141 -13.600 1.00 17.21  ? 76  LYS   A CA   1 
ATOM   565  C  C    . LYS   A 1 76  ? -12.765 -14.416 -12.602 1.00 19.49  ? 76  LYS   A C    1 
ATOM   566  O  O    . LYS   A 1 76  ? -13.881 -13.903 -12.754 1.00 21.08  ? 76  LYS   A O    1 
ATOM   567  C  CB   . LYS   A 1 76  ? -11.467 -15.325 -14.540 1.00 15.56  ? 76  LYS   A CB   1 
ATOM   568  C  CG   . LYS   A 1 76  ? -12.728 -15.615 -15.358 1.00 22.18  ? 76  LYS   A CG   1 
ATOM   569  C  CD   . LYS   A 1 76  ? -12.479 -16.716 -16.374 1.00 22.28  ? 76  LYS   A CD   1 
ATOM   570  C  CE   . LYS   A 1 76  ? -13.664 -16.897 -17.290 1.00 38.41  ? 76  LYS   A CE   1 
ATOM   571  N  NZ   . LYS   A 1 76  ? -13.213 -17.120 -18.693 1.00 43.69  ? 76  LYS   A NZ   1 
ATOM   572  N  N    . SER   A 1 77  ? -12.464 -15.197 -11.559 1.00 20.73  ? 77  SER   A N    1 
ATOM   573  C  CA   . SER   A 1 77  ? -13.446 -15.461 -10.511 1.00 22.26  ? 77  SER   A CA   1 
ATOM   574  C  C    . SER   A 1 77  ? -13.871 -14.174 -9.817  1.00 27.49  ? 77  SER   A C    1 
ATOM   575  O  O    . SER   A 1 77  ? -15.045 -14.008 -9.464  1.00 29.06  ? 77  SER   A O    1 
ATOM   576  C  CB   . SER   A 1 77  ? -12.883 -16.466 -9.500  1.00 25.91  ? 77  SER   A CB   1 
ATOM   577  O  OG   . SER   A 1 77  ? -12.660 -17.740 -10.101 1.00 33.88  ? 77  SER   A OG   1 
ATOM   578  N  N    . TYR   A 1 78  ? -12.929 -13.240 -9.630  1.00 18.10  ? 78  TYR   A N    1 
ATOM   579  C  CA   . TYR   A 1 78  ? -13.258 -11.948 -9.038  1.00 22.69  ? 78  TYR   A CA   1 
ATOM   580  C  C    . TYR   A 1 78  ? -14.263 -11.176 -9.888  1.00 23.78  ? 78  TYR   A C    1 
ATOM   581  O  O    . TYR   A 1 78  ? -15.303 -10.730 -9.385  1.00 24.80  ? 78  TYR   A O    1 
ATOM   582  C  CB   . TYR   A 1 78  ? -11.976 -11.136 -8.839  1.00 17.55  ? 78  TYR   A CB   1 
ATOM   583  C  CG   . TYR   A 1 78  ? -12.207 -9.710  -8.363  1.00 18.24  ? 78  TYR   A CG   1 
ATOM   584  C  CD1  . TYR   A 1 78  ? -12.509 -9.442  -7.033  1.00 17.76  ? 78  TYR   A CD1  1 
ATOM   585  C  CD2  . TYR   A 1 78  ? -12.115 -8.635  -9.240  1.00 16.10  ? 78  TYR   A CD2  1 
ATOM   586  C  CE1  . TYR   A 1 78  ? -12.714 -8.148  -6.588  1.00 18.85  ? 78  TYR   A CE1  1 
ATOM   587  C  CE2  . TYR   A 1 78  ? -12.318 -7.335  -8.811  1.00 16.99  ? 78  TYR   A CE2  1 
ATOM   588  C  CZ   . TYR   A 1 78  ? -12.616 -7.097  -7.478  1.00 16.89  ? 78  TYR   A CZ   1 
ATOM   589  O  OH   . TYR   A 1 78  ? -12.824 -5.815  -7.015  1.00 20.20  ? 78  TYR   A OH   1 
ATOM   590  N  N    . TRP   A 1 79  ? -13.962 -10.991 -11.181 1.00 17.74  ? 79  TRP   A N    1 
ATOM   591  C  CA   . TRP   A 1 79  ? -14.861 -10.246 -12.052 1.00 18.69  ? 79  TRP   A CA   1 
ATOM   592  C  C    . TRP   A 1 79  ? -16.190 -10.974 -12.227 1.00 20.59  ? 79  TRP   A C    1 
ATOM   593  O  O    . TRP   A 1 79  ? -17.240 -10.324 -12.308 1.00 29.30  ? 79  TRP   A O    1 
ATOM   594  C  CB   . TRP   A 1 79  ? -14.204 -9.974  -13.413 1.00 17.76  ? 79  TRP   A CB   1 
ATOM   595  C  CG   . TRP   A 1 79  ? -13.010 -9.056  -13.342 1.00 16.25  ? 79  TRP   A CG   1 
ATOM   596  C  CD1  . TRP   A 1 79  ? -11.708 -9.361  -13.636 1.00 15.02  ? 79  TRP   A CD1  1 
ATOM   597  C  CD2  . TRP   A 1 79  ? -13.022 -7.673  -12.952 1.00 17.48  ? 79  TRP   A CD2  1 
ATOM   598  N  NE1  . TRP   A 1 79  ? -10.911 -8.246  -13.454 1.00 13.36  ? 79  TRP   A NE1  1 
ATOM   599  C  CE2  . TRP   A 1 79  ? -11.693 -7.201  -13.030 1.00 13.83  ? 79  TRP   A CE2  1 
ATOM   600  C  CE3  . TRP   A 1 79  ? -14.028 -6.791  -12.546 1.00 20.50  ? 79  TRP   A CE3  1 
ATOM   601  C  CZ2  . TRP   A 1 79  ? -11.341 -5.884  -12.707 1.00 16.86  ? 79  TRP   A CZ2  1 
ATOM   602  C  CZ3  . TRP   A 1 79  ? -13.681 -5.482  -12.230 1.00 21.40  ? 79  TRP   A CZ3  1 
ATOM   603  C  CH2  . TRP   A 1 79  ? -12.351 -5.043  -12.307 1.00 19.91  ? 79  TRP   A CH2  1 
ATOM   604  N  N    . LYS   A 1 80  ? -16.163 -12.310 -12.244 1.00 24.57  ? 80  LYS   A N    1 
ATOM   605  C  CA   . LYS   A 1 80  ? -17.383 -13.101 -12.394 1.00 34.50  ? 80  LYS   A CA   1 
ATOM   606  C  C    . LYS   A 1 80  ? -18.297 -13.034 -11.179 1.00 43.26  ? 80  LYS   A C    1 
ATOM   607  O  O    . LYS   A 1 80  ? -19.394 -13.602 -11.220 1.00 46.91  ? 80  LYS   A O    1 
ATOM   608  C  CB   . LYS   A 1 80  ? -17.079 -14.546 -12.784 1.00 28.24  ? 80  LYS   A CB   1 
ATOM   609  C  CG   . LYS   A 1 80  ? -16.605 -14.695 -14.223 1.00 30.92  ? 80  LYS   A CG   1 
ATOM   610  C  CD   . LYS   A 1 80  ? -17.232 -15.898 -14.903 1.00 46.46  ? 80  LYS   A CD   1 
ATOM   611  C  CE   . LYS   A 1 80  ? -17.367 -17.071 -13.946 1.00 55.32  ? 80  LYS   A CE   1 
ATOM   612  N  NZ   . LYS   A 1 80  ? -17.314 -18.374 -14.664 1.00 58.47  ? 80  LYS   A NZ   1 
ATOM   613  N  N    . ALA   A 1 81  ? -17.897 -12.350 -10.115 1.00 43.28  ? 81  ALA   A N    1 
ATOM   614  C  CA   . ALA   A 1 81  ? -18.804 -12.053 -9.019  1.00 36.42  ? 81  ALA   A CA   1 
ATOM   615  C  C    . ALA   A 1 81  ? -19.376 -10.643 -9.094  1.00 46.62  ? 81  ALA   A C    1 
ATOM   616  O  O    . ALA   A 1 81  ? -20.281 -10.318 -8.318  1.00 53.16  ? 81  ALA   A O    1 
ATOM   617  C  CB   . ALA   A 1 81  ? -18.104 -12.268 -7.672  1.00 40.41  ? 81  ALA   A CB   1 
ATOM   618  N  N    . LEU   A 1 82  ? -18.889 -9.814  -10.018 1.00 34.06  ? 82  LEU   A N    1 
ATOM   619  C  CA   . LEU   A 1 82  ? -19.321 -8.430  -10.161 1.00 38.69  ? 82  LEU   A CA   1 
ATOM   620  C  C    . LEU   A 1 82  ? -20.104 -8.145  -11.443 1.00 37.00  ? 82  LEU   A C    1 
ATOM   621  O  O    . LEU   A 1 82  ? -20.415 -6.981  -11.709 1.00 38.72  ? 82  LEU   A O    1 
ATOM   622  C  CB   . LEU   A 1 82  ? -18.108 -7.492  -10.089 1.00 34.94  ? 82  LEU   A CB   1 
ATOM   623  C  CG   . LEU   A 1 82  ? -17.153 -7.633  -8.899  1.00 37.25  ? 82  LEU   A CG   1 
ATOM   624  C  CD1  . LEU   A 1 82  ? -16.004 -6.639  -9.041  1.00 27.97  ? 82  LEU   A CD1  1 
ATOM   625  C  CD2  . LEU   A 1 82  ? -17.882 -7.447  -7.572  1.00 40.89  ? 82  LEU   A CD2  1 
ATOM   626  N  N    A GLY   A 1 83  ? -20.418 -9.160  -12.244 0.49 43.13  ? 83  GLY   A N    1 
ATOM   627  N  N    B GLY   A 1 83  ? -20.417 -9.159  -12.246 0.51 43.15  ? 83  GLY   A N    1 
ATOM   628  C  CA   A GLY   A 1 83  ? -21.188 -8.958  -13.457 0.49 36.64  ? 83  GLY   A CA   1 
ATOM   629  C  CA   B GLY   A 1 83  ? -21.188 -8.955  -13.459 0.51 36.64  ? 83  GLY   A CA   1 
ATOM   630  C  C    A GLY   A 1 83  ? -20.380 -8.690  -14.707 0.49 37.09  ? 83  GLY   A C    1 
ATOM   631  C  C    B GLY   A 1 83  ? -20.381 -8.698  -14.711 0.51 37.10  ? 83  GLY   A C    1 
ATOM   632  O  O    A GLY   A 1 83  ? -20.964 -8.340  -15.740 0.49 31.07  ? 83  GLY   A O    1 
ATOM   633  O  O    B GLY   A 1 83  ? -20.966 -8.364  -15.748 0.51 31.04  ? 83  GLY   A O    1 
ATOM   634  N  N    . ILE   A 1 84  ? -19.062 -8.857  -14.655 1.00 28.09  ? 84  ILE   A N    1 
ATOM   635  C  CA   . ILE   A 1 84  ? -18.182 -8.581  -15.780 1.00 31.93  ? 84  ILE   A CA   1 
ATOM   636  C  C    . ILE   A 1 84  ? -17.622 -9.901  -16.289 1.00 28.26  ? 84  ILE   A C    1 
ATOM   637  O  O    . ILE   A 1 84  ? -17.212 -10.762 -15.498 1.00 26.82  ? 84  ILE   A O    1 
ATOM   638  C  CB   . ILE   A 1 84  ? -17.068 -7.593  -15.389 1.00 20.48  ? 84  ILE   A CB   1 
ATOM   639  C  CG1  . ILE   A 1 84  ? -17.684 -6.227  -15.079 1.00 30.26  ? 84  ILE   A CG1  1 
ATOM   640  C  CG2  . ILE   A 1 84  ? -16.066 -7.460  -16.504 1.00 28.26  ? 84  ILE   A CG2  1 
ATOM   641  C  CD1  . ILE   A 1 84  ? -16.810 -5.335  -14.241 1.00 30.37  ? 84  ILE   A CD1  1 
ATOM   642  N  N    . SER   A 1 85  ? -17.651 -10.076 -17.605 1.00 25.73  ? 85  SER   A N    1 
ATOM   643  C  CA   . SER   A 1 85  ? -16.964 -11.191 -18.234 1.00 21.67  ? 85  SER   A CA   1 
ATOM   644  C  C    . SER   A 1 85  ? -15.605 -10.679 -18.668 1.00 21.13  ? 85  SER   A C    1 
ATOM   645  O  O    . SER   A 1 85  ? -15.509 -9.952  -19.668 1.00 22.59  ? 85  SER   A O    1 
ATOM   646  C  CB   . SER   A 1 85  ? -17.757 -11.701 -19.441 1.00 22.10  ? 85  SER   A CB   1 
ATOM   647  O  OG   . SER   A 1 85  ? -19.063 -12.076 -19.048 1.00 28.37  ? 85  SER   A OG   1 
ATOM   648  N  N    . PRO   A 1 86  ? -14.531 -11.013 -17.959 1.00 19.36  ? 86  PRO   A N    1 
ATOM   649  C  CA   . PRO   A 1 86  ? -13.231 -10.406 -18.230 1.00 18.47  ? 86  PRO   A CA   1 
ATOM   650  C  C    . PRO   A 1 86  ? -12.447 -11.242 -19.234 1.00 14.64  ? 86  PRO   A C    1 
ATOM   651  O  O    . PRO   A 1 86  ? -12.836 -12.361 -19.594 1.00 18.97  ? 86  PRO   A O    1 
ATOM   652  C  CB   . PRO   A 1 86  ? -12.556 -10.483 -16.856 1.00 18.98  ? 86  PRO   A CB   1 
ATOM   653  C  CG   . PRO   A 1 86  ? -13.033 -11.780 -16.311 1.00 17.02  ? 86  PRO   A CG   1 
ATOM   654  C  CD   . PRO   A 1 86  ? -14.472 -11.957 -16.832 1.00 20.09  ? 86  PRO   A CD   1 
ATOM   655  N  N    . PHE   A 1 87  ? -11.321 -10.678 -19.660 1.00 16.35  ? 87  PHE   A N    1 
ATOM   656  C  CA   . PHE   A 1 87  ? -10.497 -11.303 -20.692 1.00 16.89  ? 87  PHE   A CA   1 
ATOM   657  C  C    . PHE   A 1 87  ? -9.640  -12.429 -20.122 1.00 17.18  ? 87  PHE   A C    1 
ATOM   658  O  O    . PHE   A 1 87  ? -9.593  -13.531 -20.688 1.00 16.55  ? 87  PHE   A O    1 
ATOM   659  C  CB   . PHE   A 1 87  ? -9.585  -10.263 -21.327 1.00 15.88  ? 87  PHE   A CB   1 
ATOM   660  C  CG   . PHE   A 1 87  ? -8.718  -10.805 -22.424 1.00 15.53  ? 87  PHE   A CG   1 
ATOM   661  C  CD1  . PHE   A 1 87  ? -9.265  -11.095 -23.664 1.00 23.83  ? 87  PHE   A CD1  1 
ATOM   662  C  CD2  . PHE   A 1 87  ? -7.367  -11.008 -22.227 1.00 20.30  ? 87  PHE   A CD2  1 
ATOM   663  C  CE1  . PHE   A 1 87  ? -8.476  -11.594 -24.686 1.00 20.93  ? 87  PHE   A CE1  1 
ATOM   664  C  CE2  . PHE   A 1 87  ? -6.571  -11.496 -23.249 1.00 20.71  ? 87  PHE   A CE2  1 
ATOM   665  C  CZ   . PHE   A 1 87  ? -7.129  -11.792 -24.472 1.00 20.56  ? 87  PHE   A CZ   1 
ATOM   666  N  N    . HIS   A 1 88  ? -8.932  -12.169 -19.023 1.00 15.32  ? 88  HIS   A N    1 
ATOM   667  C  CA   . HIS   A 1 88  ? -7.922  -13.099 -18.533 1.00 14.86  ? 88  HIS   A CA   1 
ATOM   668  C  C    . HIS   A 1 88  ? -8.522  -14.172 -17.637 1.00 14.51  ? 88  HIS   A C    1 
ATOM   669  O  O    . HIS   A 1 88  ? -9.496  -13.943 -16.911 1.00 16.29  ? 88  HIS   A O    1 
ATOM   670  C  CB   . HIS   A 1 88  ? -6.829  -12.350 -17.756 1.00 14.04  ? 88  HIS   A CB   1 
ATOM   671  C  CG   . HIS   A 1 88  ? -6.155  -11.285 -18.555 1.00 13.91  ? 88  HIS   A CG   1 
ATOM   672  N  ND1  . HIS   A 1 88  ? -6.590  -9.973  -18.556 1.00 15.39  ? 88  HIS   A ND1  1 
ATOM   673  C  CD2  . HIS   A 1 88  ? -5.106  -11.336 -19.408 1.00 16.53  ? 88  HIS   A CD2  1 
ATOM   674  C  CE1  . HIS   A 1 88  ? -5.829  -9.264  -19.366 1.00 15.74  ? 88  HIS   A CE1  1 
ATOM   675  N  NE2  . HIS   A 1 88  ? -4.918  -10.066 -19.896 1.00 18.71  ? 88  HIS   A NE2  1 
ATOM   676  N  N    . GLU   A 1 89  ? -7.897  -15.351 -17.660 1.00 12.20  ? 89  GLU   A N    1 
ATOM   677  C  CA   . GLU   A 1 89  ? -8.266  -16.384 -16.703 1.00 14.59  ? 89  GLU   A CA   1 
ATOM   678  C  C    . GLU   A 1 89  ? -7.763  -16.017 -15.323 1.00 15.30  ? 89  GLU   A C    1 
ATOM   679  O  O    . GLU   A 1 89  ? -8.454  -16.208 -14.320 1.00 18.83  ? 89  GLU   A O    1 
ATOM   680  C  CB   . GLU   A 1 89  ? -7.658  -17.719 -17.118 1.00 15.80  ? 89  GLU   A CB   1 
ATOM   681  C  CG   . GLU   A 1 89  ? -8.233  -18.279 -18.395 1.00 15.50  ? 89  GLU   A CG   1 
ATOM   682  C  CD   . GLU   A 1 89  ? -9.716  -18.528 -18.285 1.00 20.54  ? 89  GLU   A CD   1 
ATOM   683  O  OE1  . GLU   A 1 89  ? -10.118 -19.253 -17.351 1.00 25.36  ? 89  GLU   A OE1  1 
ATOM   684  O  OE2  . GLU   A 1 89  ? -10.464 -17.979 -19.116 1.00 25.39  ? 89  GLU   A OE2  1 
ATOM   685  N  N    . HIS   A 1 90  ? -6.551  -15.496 -15.264 1.00 13.73  ? 90  HIS   A N    1 
ATOM   686  C  CA   . HIS   A 1 90  ? -5.966  -15.050 -14.019 1.00 14.52  ? 90  HIS   A CA   1 
ATOM   687  C  C    . HIS   A 1 90  ? -4.777  -14.174 -14.354 1.00 16.33  ? 90  HIS   A C    1 
ATOM   688  O  O    . HIS   A 1 90  ? -4.439  -13.969 -15.522 1.00 22.68  ? 90  HIS   A O    1 
ATOM   689  C  CB   . HIS   A 1 90  ? -5.613  -16.227 -13.126 1.00 21.86  ? 90  HIS   A CB   1 
ATOM   690  C  CG   . HIS   A 1 90  ? -4.991  -17.385 -13.831 1.00 28.15  ? 90  HIS   A CG   1 
ATOM   691  N  ND1  . HIS   A 1 90  ? -5.616  -18.608 -13.943 1.00 36.22  ? 90  HIS   A ND1  1 
ATOM   692  C  CD2  . HIS   A 1 90  ? -3.786  -17.521 -14.429 1.00 39.94  ? 90  HIS   A CD2  1 
ATOM   693  C  CE1  . HIS   A 1 90  ? -4.827  -19.444 -14.591 1.00 38.25  ? 90  HIS   A CE1  1 
ATOM   694  N  NE2  . HIS   A 1 90  ? -3.709  -18.811 -14.895 1.00 44.10  ? 90  HIS   A NE2  1 
ATOM   695  N  N    . ALA   A 1 91  ? -4.166  -13.620 -13.318 1.00 15.36  ? 91  ALA   A N    1 
ATOM   696  C  CA   . ALA   A 1 91  ? -2.936  -12.867 -13.468 1.00 15.44  ? 91  ALA   A CA   1 
ATOM   697  C  C    . ALA   A 1 91  ? -1.855  -13.682 -12.791 1.00 18.57  ? 91  ALA   A C    1 
ATOM   698  O  O    . ALA   A 1 91  ? -2.056  -14.169 -11.674 1.00 21.21  ? 91  ALA   A O    1 
ATOM   699  C  CB   . ALA   A 1 91  ? -3.045  -11.513 -12.779 1.00 18.50  ? 91  ALA   A CB   1 
ATOM   700  N  N    . GLU   A 1 92  ? -0.751  -13.894 -13.479 1.00 19.19  ? 92  GLU   A N    1 
ATOM   701  C  CA   . GLU   A 1 92  ? 0.307   -14.742 -12.966 1.00 22.62  ? 92  GLU   A CA   1 
ATOM   702  C  C    . GLU   A 1 92  ? 1.575   -13.929 -12.792 1.00 28.47  ? 92  GLU   A C    1 
ATOM   703  O  O    . GLU   A 1 92  ? 1.917   -13.098 -13.639 1.00 26.21  ? 92  GLU   A O    1 
ATOM   704  C  CB   . GLU   A 1 92  ? 0.511   -15.975 -13.860 1.00 29.40  ? 92  GLU   A CB   1 
ATOM   705  C  CG   . GLU   A 1 92  ? -0.558  -17.024 -13.592 1.00 34.44  ? 92  GLU   A CG   1 
ATOM   706  C  CD   . GLU   A 1 92  ? -0.559  -18.174 -14.569 1.00 64.03  ? 92  GLU   A CD   1 
ATOM   707  O  OE1  . GLU   A 1 92  ? -1.384  -19.095 -14.407 1.00 64.82  ? 92  GLU   A OE1  1 
ATOM   708  O  OE2  . GLU   A 1 92  ? 0.254   -18.170 -15.500 1.00 63.60  ? 92  GLU   A OE2  1 
ATOM   709  N  N    . VAL   A 1 93  ? 2.230   -14.119 -11.652 1.00 16.31  ? 93  VAL   A N    1 
ATOM   710  C  CA   . VAL   A 1 93  ? 3.457   -13.415 -11.342 1.00 14.16  ? 93  VAL   A CA   1 
ATOM   711  C  C    . VAL   A 1 93  ? 4.484   -14.482 -10.995 1.00 13.89  ? 93  VAL   A C    1 
ATOM   712  O  O    . VAL   A 1 93  ? 4.362   -15.149 -9.959  1.00 15.12  ? 93  VAL   A O    1 
ATOM   713  C  CB   . VAL   A 1 93  ? 3.269   -12.430 -10.186 1.00 15.66  ? 93  VAL   A CB   1 
ATOM   714  C  CG1  . VAL   A 1 93  ? 4.581   -11.724 -9.889  1.00 17.21  ? 93  VAL   A CG1  1 
ATOM   715  C  CG2  . VAL   A 1 93  ? 2.135   -11.430 -10.530 1.00 17.03  ? 93  VAL   A CG2  1 
ATOM   716  N  N    . VAL   A 1 94  ? 5.496   -14.637 -11.840 1.00 12.41  ? 94  VAL   A N    1 
ATOM   717  C  CA   . VAL   A 1 94  ? 6.476   -15.709 -11.711 1.00 12.42  ? 94  VAL   A CA   1 
ATOM   718  C  C    . VAL   A 1 94  ? 7.844   -15.087 -11.510 1.00 14.48  ? 94  VAL   A C    1 
ATOM   719  O  O    . VAL   A 1 94  ? 8.276   -14.259 -12.315 1.00 12.20  ? 94  VAL   A O    1 
ATOM   720  C  CB   . VAL   A 1 94  ? 6.487   -16.614 -12.954 1.00 15.29  ? 94  VAL   A CB   1 
ATOM   721  C  CG1  . VAL   A 1 94  ? 7.424   -17.782 -12.717 1.00 15.09  ? 94  VAL   A CG1  1 
ATOM   722  C  CG2  . VAL   A 1 94  ? 5.076   -17.106 -13.271 1.00 19.52  ? 94  VAL   A CG2  1 
ATOM   723  N  N    . PHE   A 1 95  ? 8.536   -15.496 -10.449 1.00 11.93  ? 95  PHE   A N    1 
ATOM   724  C  CA   . PHE   A 1 95  ? 9.780   -14.843 -10.069 1.00 11.09  ? 95  PHE   A CA   1 
ATOM   725  C  C    . PHE   A 1 95  ? 10.655  -15.785 -9.251  1.00 13.93  ? 95  PHE   A C    1 
ATOM   726  O  O    . PHE   A 1 95  ? 10.162  -16.659 -8.532  1.00 13.95  ? 95  PHE   A O    1 
ATOM   727  C  CB   . PHE   A 1 95  ? 9.517   -13.553 -9.267  1.00 12.81  ? 95  PHE   A CB   1 
ATOM   728  C  CG   . PHE   A 1 95  ? 8.780   -13.771 -7.972  1.00 13.39  ? 95  PHE   A CG   1 
ATOM   729  C  CD1  . PHE   A 1 95  ? 7.410   -13.995 -7.962  1.00 15.55  ? 95  PHE   A CD1  1 
ATOM   730  C  CD2  . PHE   A 1 95  ? 9.454   -13.716 -6.763  1.00 16.31  ? 95  PHE   A CD2  1 
ATOM   731  C  CE1  . PHE   A 1 95  ? 6.729   -14.179 -6.760  1.00 17.25  ? 95  PHE   A CE1  1 
ATOM   732  C  CE2  . PHE   A 1 95  ? 8.771   -13.890 -5.555  1.00 14.25  ? 95  PHE   A CE2  1 
ATOM   733  C  CZ   . PHE   A 1 95  ? 7.418   -14.133 -5.564  1.00 13.85  ? 95  PHE   A CZ   1 
ATOM   734  N  N    . THR   A 1 96  ? 11.958  -15.579 -9.346  1.00 13.39  ? 96  THR   A N    1 
ATOM   735  C  CA   . THR   A 1 96  ? 12.885  -16.230 -8.433  1.00 12.87  ? 96  THR   A CA   1 
ATOM   736  C  C    . THR   A 1 96  ? 12.961  -15.422 -7.150  1.00 14.12  ? 96  THR   A C    1 
ATOM   737  O  O    . THR   A 1 96  ? 13.035  -14.187 -7.173  1.00 16.43  ? 96  THR   A O    1 
ATOM   738  C  CB   . THR   A 1 96  ? 14.267  -16.325 -9.075  1.00 13.64  ? 96  THR   A CB   1 
ATOM   739  O  OG1  . THR   A 1 96  ? 14.208  -17.142 -10.250 1.00 16.67  ? 96  THR   A OG1  1 
ATOM   740  C  CG2  . THR   A 1 96  ? 15.276  -16.913 -8.086  1.00 15.49  ? 96  THR   A CG2  1 
ATOM   741  N  N    . ALA   A 1 97  ? 12.914  -16.111 -6.018  1.00 14.13  ? 97  ALA   A N    1 
ATOM   742  C  CA   . ALA   A 1 97  ? 12.923  -15.463 -4.714  1.00 15.34  ? 97  ALA   A CA   1 
ATOM   743  C  C    . ALA   A 1 97  ? 14.080  -15.979 -3.874  1.00 13.40  ? 97  ALA   A C    1 
ATOM   744  O  O    . ALA   A 1 97  ? 14.436  -17.158 -3.955  1.00 15.35  ? 97  ALA   A O    1 
ATOM   745  C  CB   . ALA   A 1 97  ? 11.611  -15.724 -3.959  1.00 15.09  ? 97  ALA   A CB   1 
ATOM   746  N  N    . ASN   A 1 98  ? 14.654  -15.089 -3.061  1.00 13.67  ? 98  ASN   A N    1 
ATOM   747  C  CA   . ASN   A 1 98  ? 15.612  -15.438 -2.015  1.00 14.90  ? 98  ASN   A CA   1 
ATOM   748  C  C    . ASN   A 1 98  ? 16.911  -16.028 -2.552  1.00 20.78  ? 98  ASN   A C    1 
ATOM   749  O  O    . ASN   A 1 98  ? 17.617  -16.740 -1.823  1.00 21.15  ? 98  ASN   A O    1 
ATOM   750  C  CB   . ASN   A 1 98  ? 14.997  -16.349 -0.945  1.00 14.97  ? 98  ASN   A CB   1 
ATOM   751  C  CG   . ASN   A 1 98  ? 13.688  -15.828 -0.431  1.00 15.08  ? 98  ASN   A CG   1 
ATOM   752  O  OD1  . ASN   A 1 98  ? 13.614  -14.721 0.126   1.00 15.59  ? 98  ASN   A OD1  1 
ATOM   753  N  ND2  . ASN   A 1 98  ? 12.632  -16.611 -0.612  1.00 16.56  ? 98  ASN   A ND2  1 
ATOM   754  N  N    A ASP   A 1 99  ? 17.266  -15.750 -3.804  0.48 19.58  ? 99  ASP   A N    1 
ATOM   755  N  N    B ASP   A 1 99  ? 17.259  -15.746 -3.808  0.52 19.56  ? 99  ASP   A N    1 
ATOM   756  C  CA   A ASP   A 1 99  ? 18.482  -16.321 -4.374  0.48 22.90  ? 99  ASP   A CA   1 
ATOM   757  C  CA   B ASP   A 1 99  ? 18.478  -16.319 -4.367  0.52 22.89  ? 99  ASP   A CA   1 
ATOM   758  C  C    A ASP   A 1 99  ? 19.733  -15.507 -4.058  0.48 26.90  ? 99  ASP   A C    1 
ATOM   759  C  C    B ASP   A 1 99  ? 19.736  -15.629 -3.855  0.52 27.15  ? 99  ASP   A C    1 
ATOM   760  O  O    A ASP   A 1 99  ? 20.814  -15.840 -4.555  0.48 26.93  ? 99  ASP   A O    1 
ATOM   761  O  O    B ASP   A 1 99  ? 20.833  -16.181 -3.999  0.52 29.32  ? 99  ASP   A O    1 
ATOM   762  C  CB   A ASP   A 1 99  ? 18.335  -16.554 -5.882  0.48 25.65  ? 99  ASP   A CB   1 
ATOM   763  C  CB   B ASP   A 1 99  ? 18.443  -16.301 -5.896  0.52 26.27  ? 99  ASP   A CB   1 
ATOM   764  C  CG   A ASP   A 1 99  ? 18.335  -15.269 -6.676  0.48 27.40  ? 99  ASP   A CG   1 
ATOM   765  C  CG   B ASP   A 1 99  ? 19.367  -17.339 -6.511  0.52 26.66  ? 99  ASP   A CG   1 
ATOM   766  O  OD1  A ASP   A 1 99  ? 18.038  -14.206 -6.091  0.48 37.29  ? 99  ASP   A OD1  1 
ATOM   767  O  OD1  B ASP   A 1 99  ? 19.703  -18.324 -5.816  0.52 30.26  ? 99  ASP   A OD1  1 
ATOM   768  O  OD2  A ASP   A 1 99  ? 18.622  -15.321 -7.892  0.48 38.13  ? 99  ASP   A OD2  1 
ATOM   769  O  OD2  B ASP   A 1 99  ? 19.768  -17.166 -7.680  0.52 30.28  ? 99  ASP   A OD2  1 
ATOM   770  N  N    . SER   A 1 100 ? 19.602  -14.446 -3.259  1.00 27.94  ? 100 SER   A N    1 
ATOM   771  C  CA   . SER   A 1 100 ? 20.723  -13.736 -2.657  1.00 33.03  ? 100 SER   A CA   1 
ATOM   772  C  C    . SER   A 1 100 ? 20.483  -13.569 -1.163  1.00 29.21  ? 100 SER   A C    1 
ATOM   773  O  O    . SER   A 1 100 ? 20.854  -12.551 -0.574  1.00 36.28  ? 100 SER   A O    1 
ATOM   774  C  CB   . SER   A 1 100 ? 20.948  -12.375 -3.315  1.00 33.18  ? 100 SER   A CB   1 
ATOM   775  O  OG   . SER   A 1 100 ? 20.722  -12.429 -4.711  1.00 40.33  ? 100 SER   A OG   1 
ATOM   776  N  N    . GLY   A 1 101 ? 19.827  -14.549 -0.548  1.00 21.38  ? 101 GLY   A N    1 
ATOM   777  C  CA   . GLY   A 1 101 ? 19.438  -14.453 0.830   1.00 22.35  ? 101 GLY   A CA   1 
ATOM   778  C  C    . GLY   A 1 101 ? 18.002  -14.000 0.968   1.00 22.28  ? 101 GLY   A C    1 
ATOM   779  O  O    . GLY   A 1 101 ? 17.362  -13.565 -0.000  1.00 23.19  ? 101 GLY   A O    1 
ATOM   780  N  N    . PRO   A 1 102 ? 17.474  -14.080 2.186   1.00 20.41  ? 102 PRO   A N    1 
ATOM   781  C  CA   . PRO   A 1 102 ? 16.064  -13.746 2.404   1.00 18.98  ? 102 PRO   A CA   1 
ATOM   782  C  C    . PRO   A 1 102 ? 15.764  -12.298 2.041   1.00 19.11  ? 102 PRO   A C    1 
ATOM   783  O  O    . PRO   A 1 102 ? 16.540  -11.381 2.330   1.00 19.61  ? 102 PRO   A O    1 
ATOM   784  C  CB   . PRO   A 1 102 ? 15.858  -14.002 3.904   1.00 21.53  ? 102 PRO   A CB   1 
ATOM   785  C  CG   . PRO   A 1 102 ? 17.227  -14.068 4.501   1.00 26.20  ? 102 PRO   A CG   1 
ATOM   786  C  CD   . PRO   A 1 102 ? 18.153  -14.516 3.424   1.00 23.62  ? 102 PRO   A CD   1 
ATOM   787  N  N    . ARG   A 1 103 ? 14.623  -12.106 1.386   1.00 16.69  ? 103 ARG   A N    1 
ATOM   788  C  CA   . ARG   A 1 103 ? 14.062  -10.787 1.147   1.00 17.47  ? 103 ARG   A CA   1 
ATOM   789  C  C    . ARG   A 1 103 ? 12.582  -10.840 1.483   1.00 18.77  ? 103 ARG   A C    1 
ATOM   790  O  O    . ARG   A 1 103 ? 11.989  -11.918 1.591   1.00 17.88  ? 103 ARG   A O    1 
ATOM   791  C  CB   . ARG   A 1 103 ? 14.214  -10.370 -0.324  1.00 16.49  ? 103 ARG   A CB   1 
ATOM   792  C  CG   . ARG   A 1 103 ? 15.633  -10.289 -0.838  1.00 20.63  ? 103 ARG   A CG   1 
ATOM   793  C  CD   . ARG   A 1 103 ? 16.394  -9.150  -0.167  1.00 23.69  ? 103 ARG   A CD   1 
ATOM   794  N  NE   . ARG   A 1 103 ? 17.727  -9.016  -0.743  1.00 25.70  ? 103 ARG   A NE   1 
ATOM   795  C  CZ   . ARG   A 1 103 ? 18.801  -9.673  -0.328  1.00 30.37  ? 103 ARG   A CZ   1 
ATOM   796  N  NH1  . ARG   A 1 103 ? 18.753  -10.494 0.710   1.00 25.38  ? 103 ARG   A NH1  1 
ATOM   797  N  NH2  . ARG   A 1 103 ? 19.953  -9.505  -0.975  1.00 31.22  ? 103 ARG   A NH2  1 
ATOM   798  N  N    . ARG   A 1 104 ? 11.980  -9.661  1.640   1.00 17.19  ? 104 ARG   A N    1 
ATOM   799  C  CA   . ARG   A 1 104 ? 10.537  -9.551  1.790   1.00 15.22  ? 104 ARG   A CA   1 
ATOM   800  C  C    . ARG   A 1 104 ? 9.957   -9.048  0.480   1.00 15.62  ? 104 ARG   A C    1 
ATOM   801  O  O    . ARG   A 1 104 ? 10.464  -8.079  -0.090  1.00 17.14  ? 104 ARG   A O    1 
ATOM   802  C  CB   . ARG   A 1 104 ? 10.176  -8.588  2.909   1.00 17.86  ? 104 ARG   A CB   1 
ATOM   803  C  CG   . ARG   A 1 104 ? 10.662  -9.061  4.270   1.00 27.35  ? 104 ARG   A CG   1 
ATOM   804  C  CD   . ARG   A 1 104 ? 10.410  -8.050  5.361   1.00 40.35  ? 104 ARG   A CD   1 
ATOM   805  N  NE   . ARG   A 1 104 ? 10.696  -8.623  6.671   1.00 63.12  ? 104 ARG   A NE   1 
ATOM   806  C  CZ   . ARG   A 1 104 ? 10.954  -7.914  7.761   1.00 70.68  ? 104 ARG   A CZ   1 
ATOM   807  N  NH1  . ARG   A 1 104 ? 10.996  -6.592  7.730   1.00 70.34  ? 104 ARG   A NH1  1 
ATOM   808  N  NH2  . ARG   A 1 104 ? 11.182  -8.548  8.908   1.00 66.48  ? 104 ARG   A NH2  1 
ATOM   809  N  N    . TYR   A 1 105 ? 8.888   -9.692  0.027   1.00 14.73  ? 105 TYR   A N    1 
ATOM   810  C  CA   . TYR   A 1 105 ? 8.299   -9.413  -1.275  1.00 13.22  ? 105 TYR   A CA   1 
ATOM   811  C  C    . TYR   A 1 105 ? 6.860   -8.964  -1.106  1.00 14.48  ? 105 TYR   A C    1 
ATOM   812  O  O    . TYR   A 1 105 ? 6.051   -9.659  -0.482  1.00 15.69  ? 105 TYR   A O    1 
ATOM   813  C  CB   . TYR   A 1 105 ? 8.307   -10.671 -2.152  1.00 12.24  ? 105 TYR   A CB   1 
ATOM   814  C  CG   . TYR   A 1 105 ? 9.688   -11.155 -2.450  1.00 12.19  ? 105 TYR   A CG   1 
ATOM   815  C  CD1  . TYR   A 1 105 ? 10.375  -11.956 -1.541  1.00 14.24  ? 105 TYR   A CD1  1 
ATOM   816  C  CD2  . TYR   A 1 105 ? 10.331  -10.794 -3.631  1.00 14.24  ? 105 TYR   A CD2  1 
ATOM   817  C  CE1  . TYR   A 1 105 ? 11.666  -12.389 -1.808  1.00 13.06  ? 105 TYR   A CE1  1 
ATOM   818  C  CE2  . TYR   A 1 105 ? 11.624  -11.230 -3.913  1.00 14.96  ? 105 TYR   A CE2  1 
ATOM   819  C  CZ   . TYR   A 1 105 ? 12.291  -12.021 -2.986  1.00 14.89  ? 105 TYR   A CZ   1 
ATOM   820  O  OH   . TYR   A 1 105 ? 13.574  -12.421 -3.274  1.00 14.46  ? 105 TYR   A OH   1 
ATOM   821  N  N    . THR   A 1 106 ? 6.521   -7.828  -1.705  1.00 13.54  ? 106 THR   A N    1 
ATOM   822  C  CA   . THR   A 1 106 ? 5.131   -7.449  -1.887  1.00 12.99  ? 106 THR   A CA   1 
ATOM   823  C  C    . THR   A 1 106 ? 4.818   -7.499  -3.374  1.00 13.74  ? 106 THR   A C    1 
ATOM   824  O  O    . THR   A 1 106 ? 5.484   -6.833  -4.177  1.00 16.10  ? 106 THR   A O    1 
ATOM   825  C  CB   . THR   A 1 106 ? 4.863   -6.058  -1.326  1.00 17.55  ? 106 THR   A CB   1 
ATOM   826  O  OG1  . THR   A 1 106 ? 5.168   -6.055  0.074   1.00 20.04  ? 106 THR   A OG1  1 
ATOM   827  C  CG2  . THR   A 1 106 ? 3.397   -5.697  -1.507  1.00 18.59  ? 106 THR   A CG2  1 
ATOM   828  N  N    . ILE   A 1 107 ? 3.844   -8.315  -3.744  1.00 12.06  ? 107 ILE   A N    1 
ATOM   829  C  CA   . ILE   A 1 107 ? 3.364   -8.389  -5.117  1.00 11.66  ? 107 ILE   A CA   1 
ATOM   830  C  C    . ILE   A 1 107 ? 2.069   -7.600  -5.164  1.00 15.09  ? 107 ILE   A C    1 
ATOM   831  O  O    . ILE   A 1 107 ? 1.108   -7.942  -4.474  1.00 13.97  ? 107 ILE   A O    1 
ATOM   832  C  CB   . ILE   A 1 107 ? 3.118   -9.847  -5.535  1.00 13.66  ? 107 ILE   A CB   1 
ATOM   833  C  CG1  . ILE   A 1 107 ? 4.382   -10.704 -5.348  1.00 17.98  ? 107 ILE   A CG1  1 
ATOM   834  C  CG2  . ILE   A 1 107 ? 2.553   -9.924  -6.964  1.00 17.12  ? 107 ILE   A CG2  1 
ATOM   835  C  CD1  . ILE   A 1 107 ? 5.591   -10.203 -6.099  1.00 20.61  ? 107 ILE   A CD1  1 
ATOM   836  N  N    . ALA   A 1 108 ? 2.035   -6.537  -5.966  1.00 13.76  ? 108 ALA   A N    1 
ATOM   837  C  CA   . ALA   A 1 108 ? 0.829   -5.744  -6.131  1.00 12.83  ? 108 ALA   A CA   1 
ATOM   838  C  C    . ALA   A 1 108 ? 0.265   -5.947  -7.526  1.00 12.50  ? 108 ALA   A C    1 
ATOM   839  O  O    . ALA   A 1 108 ? 1.011   -6.076  -8.495  1.00 14.06  ? 108 ALA   A O    1 
ATOM   840  C  CB   . ALA   A 1 108 ? 1.122   -4.264  -5.960  1.00 15.17  ? 108 ALA   A CB   1 
ATOM   841  N  N    . ALA   A 1 109 ? -1.056  -5.958  -7.625  1.00 11.70  ? 109 ALA   A N    1 
ATOM   842  C  CA   . ALA   A 1 109 ? -1.733  -6.090  -8.902  1.00 11.21  ? 109 ALA   A CA   1 
ATOM   843  C  C    . ALA   A 1 109 ? -2.901  -5.121  -8.950  1.00 13.04  ? 109 ALA   A C    1 
ATOM   844  O  O    . ALA   A 1 109 ? -3.615  -4.942  -7.958  1.00 14.50  ? 109 ALA   A O    1 
ATOM   845  C  CB   . ALA   A 1 109 ? -2.258  -7.506  -9.093  1.00 14.49  ? 109 ALA   A CB   1 
ATOM   846  N  N    . LEU   A 1 110 ? -3.091  -4.517  -10.121 1.00 10.70  ? 110 LEU   A N    1 
ATOM   847  C  CA   . LEU   A 1 110 ? -4.160  -3.558  -10.372 1.00 10.90  ? 110 LEU   A CA   1 
ATOM   848  C  C    . LEU   A 1 110 ? -4.988  -4.117  -11.516 1.00 10.32  ? 110 LEU   A C    1 
ATOM   849  O  O    . LEU   A 1 110 ? -4.448  -4.388  -12.594 1.00 12.72  ? 110 LEU   A O    1 
ATOM   850  C  CB   . LEU   A 1 110 ? -3.560  -2.200  -10.730 1.00 12.53  ? 110 LEU   A CB   1 
ATOM   851  C  CG   . LEU   A 1 110 ? -4.549  -1.126  -11.189 1.00 12.49  ? 110 LEU   A CG   1 
ATOM   852  C  CD1  . LEU   A 1 110 ? -5.485  -0.747  -10.050 1.00 12.84  ? 110 LEU   A CD1  1 
ATOM   853  C  CD2  . LEU   A 1 110 ? -3.719  0.071   -11.602 1.00 16.42  ? 110 LEU   A CD2  1 
ATOM   854  N  N    . LEU   A 1 111 ? -6.285  -4.298  -11.292 1.00 11.15  ? 111 LEU   A N    1 
ATOM   855  C  CA   . LEU   A 1 111 ? -7.124  -5.092  -12.183 1.00 11.11  ? 111 LEU   A CA   1 
ATOM   856  C  C    . LEU   A 1 111 ? -8.171  -4.259  -12.919 1.00 14.07  ? 111 LEU   A C    1 
ATOM   857  O  O    . LEU   A 1 111 ? -8.885  -3.456  -12.306 1.00 13.20  ? 111 LEU   A O    1 
ATOM   858  C  CB   . LEU   A 1 111 ? -7.891  -6.140  -11.384 1.00 12.38  ? 111 LEU   A CB   1 
ATOM   859  C  CG   . LEU   A 1 111 ? -7.100  -7.079  -10.468 1.00 11.55  ? 111 LEU   A CG   1 
ATOM   860  C  CD1  . LEU   A 1 111 ? -8.016  -8.161  -9.914  1.00 12.08  ? 111 LEU   A CD1  1 
ATOM   861  C  CD2  . LEU   A 1 111 ? -5.904  -7.692  -11.212 1.00 12.24  ? 111 LEU   A CD2  1 
ATOM   862  N  N    . SER   A 1 112 ? -8.317  -4.534  -14.212 1.00 13.29  ? 112 SER   A N    1 
ATOM   863  C  CA   . SER   A 1 112 ? -9.416  -4.078  -15.053 1.00 12.71  ? 112 SER   A CA   1 
ATOM   864  C  C    . SER   A 1 112 ? -9.933  -5.287  -15.820 1.00 13.73  ? 112 SER   A C    1 
ATOM   865  O  O    . SER   A 1 112 ? -9.257  -6.316  -15.892 1.00 11.51  ? 112 SER   A O    1 
ATOM   866  C  CB   . SER   A 1 112 ? -8.914  -3.037  -16.065 1.00 15.43  ? 112 SER   A CB   1 
ATOM   867  O  OG   . SER   A 1 112 ? -8.424  -1.879  -15.396 1.00 20.75  ? 112 SER   A OG   1 
ATOM   868  N  N    . PRO   A 1 113 ? -11.131 -5.209  -16.401 1.00 12.18  ? 113 PRO   A N    1 
ATOM   869  C  CA   . PRO   A 1 113 ? -11.670 -6.403  -17.079 1.00 14.27  ? 113 PRO   A CA   1 
ATOM   870  C  C    . PRO   A 1 113 ? -10.809 -6.926  -18.217 1.00 14.13  ? 113 PRO   A C    1 
ATOM   871  O  O    . PRO   A 1 113 ? -10.755 -8.155  -18.392 1.00 15.45  ? 113 PRO   A O    1 
ATOM   872  C  CB   . PRO   A 1 113 ? -13.059 -5.953  -17.546 1.00 15.80  ? 113 PRO   A CB   1 
ATOM   873  C  CG   . PRO   A 1 113 ? -13.450 -4.926  -16.480 1.00 16.59  ? 113 PRO   A CG   1 
ATOM   874  C  CD   . PRO   A 1 113 ? -12.186 -4.206  -16.117 1.00 14.24  ? 113 PRO   A CD   1 
ATOM   875  N  N    . TYR   A 1 114 ? -10.123 -6.064  -18.972 1.00 13.03  ? 114 TYR   A N    1 
ATOM   876  C  CA   . TYR   A 1 114 ? -9.299  -6.513  -20.098 1.00 13.47  ? 114 TYR   A CA   1 
ATOM   877  C  C    . TYR   A 1 114 ? -7.818  -6.216  -19.908 1.00 13.37  ? 114 TYR   A C    1 
ATOM   878  O  O    . TYR   A 1 114 ? -7.044  -6.303  -20.861 1.00 16.28  ? 114 TYR   A O    1 
ATOM   879  C  CB   . TYR   A 1 114 ? -9.791  -5.927  -21.429 1.00 14.42  ? 114 TYR   A CB   1 
ATOM   880  C  CG   . TYR   A 1 114 ? -10.991 -6.645  -22.003 1.00 16.97  ? 114 TYR   A CG   1 
ATOM   881  C  CD1  . TYR   A 1 114 ? -12.243 -6.482  -21.446 1.00 21.35  ? 114 TYR   A CD1  1 
ATOM   882  C  CD2  . TYR   A 1 114 ? -10.870 -7.476  -23.114 1.00 16.89  ? 114 TYR   A CD2  1 
ATOM   883  C  CE1  . TYR   A 1 114 ? -13.355 -7.127  -21.966 1.00 25.46  ? 114 TYR   A CE1  1 
ATOM   884  C  CE2  . TYR   A 1 114 ? -11.981 -8.128  -23.639 1.00 18.97  ? 114 TYR   A CE2  1 
ATOM   885  C  CZ   . TYR   A 1 114 ? -13.211 -7.951  -23.059 1.00 25.21  ? 114 TYR   A CZ   1 
ATOM   886  O  OH   . TYR   A 1 114 ? -14.311 -8.596  -23.579 1.00 31.99  ? 114 TYR   A OH   1 
ATOM   887  N  N    . SER   A 1 115 ? -7.388  -5.926  -18.675 1.00 12.59  ? 115 SER   A N    1 
ATOM   888  C  CA   . SER   A 1 115 ? -6.020  -5.491  -18.456 1.00 12.06  ? 115 SER   A CA   1 
ATOM   889  C  C    . SER   A 1 115 ? -5.642  -5.725  -17.003 1.00 12.53  ? 115 SER   A C    1 
ATOM   890  O  O    . SER   A 1 115 ? -6.482  -5.654  -16.109 1.00 14.27  ? 115 SER   A O    1 
ATOM   891  C  CB   . SER   A 1 115 ? -5.852  -4.002  -18.771 1.00 15.74  ? 115 SER   A CB   1 
ATOM   892  O  OG   . SER   A 1 115 ? -4.513  -3.587  -18.630 1.00 22.99  ? 115 SER   A OG   1 
ATOM   893  N  N    . TYR   A 1 116 ? -4.360  -5.966  -16.769 1.00 13.08  ? 116 TYR   A N    1 
ATOM   894  C  CA   . TYR   A 1 116 ? -3.859  -5.846  -15.406 1.00 12.67  ? 116 TYR   A CA   1 
ATOM   895  C  C    . TYR   A 1 116 ? -2.431  -5.342  -15.432 1.00 13.74  ? 116 TYR   A C    1 
ATOM   896  O  O    . TYR   A 1 116 ? -1.705  -5.490  -16.417 1.00 12.28  ? 116 TYR   A O    1 
ATOM   897  C  CB   . TYR   A 1 116 ? -3.970  -7.144  -14.597 1.00 16.54  ? 116 TYR   A CB   1 
ATOM   898  C  CG   . TYR   A 1 116 ? -3.152  -8.292  -15.123 1.00 14.41  ? 116 TYR   A CG   1 
ATOM   899  C  CD1  . TYR   A 1 116 ? -3.702  -9.165  -16.049 1.00 17.41  ? 116 TYR   A CD1  1 
ATOM   900  C  CD2  . TYR   A 1 116 ? -1.864  -8.525  -14.678 1.00 14.97  ? 116 TYR   A CD2  1 
ATOM   901  C  CE1  . TYR   A 1 116 ? -3.001  -10.227 -16.522 1.00 18.32  ? 116 TYR   A CE1  1 
ATOM   902  C  CE2  . TYR   A 1 116 ? -1.125  -9.627  -15.174 1.00 16.68  ? 116 TYR   A CE2  1 
ATOM   903  C  CZ   . TYR   A 1 116 ? -1.734  -10.458 -16.093 1.00 16.56  ? 116 TYR   A CZ   1 
ATOM   904  O  OH   . TYR   A 1 116 ? -1.073  -11.544 -16.618 1.00 30.29  ? 116 TYR   A OH   1 
ATOM   905  N  N    . SER   A 1 117 ? -2.029  -4.736  -14.319 1.00 11.57  ? 117 SER   A N    1 
ATOM   906  C  CA   . SER   A 1 117 ? -0.657  -4.327  -14.106 1.00 13.45  ? 117 SER   A CA   1 
ATOM   907  C  C    . SER   A 1 117 ? -0.188  -4.943  -12.804 1.00 12.84  ? 117 SER   A C    1 
ATOM   908  O  O    . SER   A 1 117 ? -0.976  -5.132  -11.869 1.00 13.52  ? 117 SER   A O    1 
ATOM   909  C  CB   . SER   A 1 117 ? -0.540  -2.804  -13.998 1.00 16.46  ? 117 SER   A CB   1 
ATOM   910  O  OG   . SER   A 1 117 ? -1.026  -2.170  -15.176 1.00 22.49  ? 117 SER   A OG   1 
ATOM   911  N  N    . THR   A 1 118 ? 1.096   -5.264  -12.750 1.00 11.61  ? 118 THR   A N    1 
ATOM   912  C  CA   . THR   A 1 118 ? 1.661   -5.813  -11.535 1.00 11.38  ? 118 THR   A CA   1 
ATOM   913  C  C    . THR   A 1 118 ? 3.036   -5.214  -11.315 1.00 13.74  ? 118 THR   A C    1 
ATOM   914  O  O    . THR   A 1 118 ? 3.766   -4.927  -12.264 1.00 15.10  ? 118 THR   A O    1 
ATOM   915  C  CB   . THR   A 1 118 ? 1.693   -7.350  -11.596 1.00 13.61  ? 118 THR   A CB   1 
ATOM   916  O  OG1  . THR   A 1 118 ? 2.065   -7.876  -10.328 1.00 16.49  ? 118 THR   A OG1  1 
ATOM   917  C  CG2  . THR   A 1 118 ? 2.656   -7.869  -12.665 1.00 14.98  ? 118 THR   A CG2  1 
ATOM   918  N  N    . THR   A 1 119 ? 3.393   -5.039  -10.053 1.00 11.92  ? 119 THR   A N    1 
ATOM   919  C  CA   . THR   A 1 119 ? 4.736   -4.627  -9.707  1.00 12.01  ? 119 THR   A CA   1 
ATOM   920  C  C    . THR   A 1 119 ? 5.142   -5.376  -8.455  1.00 13.56  ? 119 THR   A C    1 
ATOM   921  O  O    . THR   A 1 119 ? 4.318   -5.999  -7.780  1.00 14.51  ? 119 THR   A O    1 
ATOM   922  C  CB   . THR   A 1 119 ? 4.851   -3.105  -9.523  1.00 15.31  ? 119 THR   A CB   1 
ATOM   923  O  OG1  . THR   A 1 119 ? 6.235   -2.727  -9.533  1.00 15.34  ? 119 THR   A OG1  1 
ATOM   924  C  CG2  . THR   A 1 119 ? 4.224   -2.659  -8.218  1.00 15.76  ? 119 THR   A CG2  1 
ATOM   925  N  N    . ALA   A 1 120 ? 6.431   -5.341  -8.175  1.00 13.10  ? 120 ALA   A N    1 
ATOM   926  C  CA   . ALA   A 1 120 ? 6.951   -5.971  -6.976  1.00 12.71  ? 120 ALA   A CA   1 
ATOM   927  C  C    . ALA   A 1 120 ? 7.751   -4.939  -6.204  1.00 13.29  ? 120 ALA   A C    1 
ATOM   928  O  O    . ALA   A 1 120 ? 8.441   -4.097  -6.795  1.00 14.43  ? 120 ALA   A O    1 
ATOM   929  C  CB   . ALA   A 1 120 ? 7.841   -7.159  -7.334  1.00 15.77  ? 120 ALA   A CB   1 
ATOM   930  N  N    . VAL   A 1 121 ? 7.641   -4.997  -4.883  1.00 12.76  ? 121 VAL   A N    1 
ATOM   931  C  CA   . VAL   A 1 121 ? 8.506   -4.250  -3.982  1.00 14.34  ? 121 VAL   A CA   1 
ATOM   932  C  C    . VAL   A 1 121 ? 9.286   -5.269  -3.180  1.00 13.70  ? 121 VAL   A C    1 
ATOM   933  O  O    . VAL   A 1 121 ? 8.690   -6.118  -2.505  1.00 16.56  ? 121 VAL   A O    1 
ATOM   934  C  CB   . VAL   A 1 121 ? 7.713   -3.322  -3.056  1.00 15.66  ? 121 VAL   A CB   1 
ATOM   935  C  CG1  . VAL   A 1 121 ? 8.650   -2.722  -1.998  1.00 21.76  ? 121 VAL   A CG1  1 
ATOM   936  C  CG2  . VAL   A 1 121 ? 7.084   -2.210  -3.865  1.00 21.75  ? 121 VAL   A CG2  1 
ATOM   937  N  N    . VAL   A 1 122 ? 10.606  -5.191  -3.261  1.00 14.01  ? 122 VAL   A N    1 
ATOM   938  C  CA   . VAL   A 1 122 ? 11.499  -6.163  -2.638  1.00 13.63  ? 122 VAL   A CA   1 
ATOM   939  C  C    . VAL   A 1 122 ? 12.362  -5.398  -1.651  1.00 15.76  ? 122 VAL   A C    1 
ATOM   940  O  O    . VAL   A 1 122 ? 13.029  -4.428  -2.034  1.00 17.12  ? 122 VAL   A O    1 
ATOM   941  C  CB   . VAL   A 1 122 ? 12.362  -6.874  -3.686  1.00 14.95  ? 122 VAL   A CB   1 
ATOM   942  C  CG1  . VAL   A 1 122 ? 13.277  -7.912  -3.017  1.00 18.14  ? 122 VAL   A CG1  1 
ATOM   943  C  CG2  . VAL   A 1 122 ? 11.462  -7.534  -4.725  1.00 17.18  ? 122 VAL   A CG2  1 
ATOM   944  N  N    . THR   A 1 123 ? 12.332  -5.813  -0.385  1.00 18.32  ? 123 THR   A N    1 
ATOM   945  C  CA   . THR   A 1 123 ? 13.110  -5.152  0.656   1.00 20.18  ? 123 THR   A CA   1 
ATOM   946  C  C    . THR   A 1 123 ? 14.016  -6.156  1.356   1.00 23.63  ? 123 THR   A C    1 
ATOM   947  O  O    . THR   A 1 123 ? 13.736  -7.361  1.395   1.00 21.26  ? 123 THR   A O    1 
ATOM   948  C  CB   . THR   A 1 123 ? 12.218  -4.445  1.685   1.00 28.04  ? 123 THR   A CB   1 
ATOM   949  O  OG1  . THR   A 1 123 ? 11.548  -5.419  2.488   1.00 36.49  ? 123 THR   A OG1  1 
ATOM   950  C  CG2  . THR   A 1 123 ? 11.176  -3.582  0.989   1.00 28.37  ? 123 THR   A CG2  1 
ATOM   951  N  N    . ASN   A 1 124 ? 15.119  -5.644  1.896   1.00 27.08  ? 124 ASN   A N    1 
ATOM   952  C  CA   . ASN   A 1 124 ? 16.074  -6.469  2.623   0.99 31.97  ? 124 ASN   A CA   1 
ATOM   953  C  C    . ASN   A 1 124 ? 15.919  -6.161  4.102   1.00 42.98  ? 124 ASN   A C    1 
ATOM   954  O  O    . ASN   A 1 124 ? 16.227  -5.038  4.530   1.00 41.17  ? 124 ASN   A O    1 
ATOM   955  C  CB   . ASN   A 1 124 ? 17.501  -6.166  2.160   1.00 28.47  ? 124 ASN   A CB   1 
ATOM   956  C  CG   . ASN   A 1 124 ? 18.514  -7.168  2.686   0.89 32.66  ? 124 ASN   A CG   1 
ATOM   957  O  OD1  . ASN   A 1 124 ? 18.246  -7.903  3.638   0.64 29.13  ? 124 ASN   A OD1  1 
ATOM   958  N  ND2  . ASN   A 1 124 ? 19.687  -7.202  2.065   1.00 34.40  ? 124 ASN   A ND2  1 
ATOM   959  N  N    . PRO   A 1 125 ? 15.451  -7.112  4.921   1.00 46.68  ? 125 PRO   A N    1 
ATOM   960  C  CA   . PRO   A 1 125 ? 15.188  -6.901  6.349   1.00 54.42  ? 125 PRO   A CA   1 
ATOM   961  C  C    . PRO   A 1 125 ? 16.456  -6.590  7.137   1.00 64.92  ? 125 PRO   A C    1 
ATOM   962  O  O    . PRO   A 1 125 ? 17.568  -6.659  6.608   1.00 65.36  ? 125 PRO   A O    1 
ATOM   963  C  CB   . PRO   A 1 125 ? 14.605  -8.246  6.795   1.00 53.04  ? 125 PRO   A CB   1 
ATOM   964  C  CG   . PRO   A 1 125 ? 15.166  -9.234  5.835   1.00 50.71  ? 125 PRO   A CG   1 
ATOM   965  C  CD   . PRO   A 1 125 ? 15.223  -8.511  4.521   1.00 35.54  ? 125 PRO   A CD   1 
ATOM   966  N  N    . LYS   B 1 9   ? -1.456  -9.627  -38.927 1.00 63.12  ? 9   LYS   B N    1 
ATOM   967  C  CA   . LYS   B 1 9   ? -2.344  -9.823  -40.068 1.00 84.15  ? 9   LYS   B CA   1 
ATOM   968  C  C    . LYS   B 1 9   ? -3.041  -11.181 -39.953 1.00 86.88  ? 9   LYS   B C    1 
ATOM   969  O  O    . LYS   B 1 9   ? -3.240  -11.883 -40.946 1.00 87.60  ? 9   LYS   B O    1 
ATOM   970  C  CB   . LYS   B 1 9   ? -1.549  -9.722  -41.373 1.00 88.03  ? 9   LYS   B CB   1 
ATOM   971  C  CG   . LYS   B 1 9   ? -2.385  -9.492  -42.625 1.00 95.47  ? 9   LYS   B CG   1 
ATOM   972  C  CD   . LYS   B 1 9   ? -1.493  -9.232  -43.829 1.00 101.50 ? 9   LYS   B CD   1 
ATOM   973  C  CE   . LYS   B 1 9   ? -0.371  -10.256 -43.918 1.00 96.32  ? 9   LYS   B CE   1 
ATOM   974  N  NZ   . LYS   B 1 9   ? 0.581   -9.947  -45.019 1.00 101.96 ? 9   LYS   B NZ   1 
ATOM   975  N  N    . CYS   B 1 10  ? -3.418  -11.535 -38.724 1.00 73.91  ? 10  CYS   B N    1 
ATOM   976  C  CA   . CYS   B 1 10  ? -3.972  -12.843 -38.396 1.00 52.32  ? 10  CYS   B CA   1 
ATOM   977  C  C    . CYS   B 1 10  ? -4.872  -12.682 -37.167 1.00 39.00  ? 10  CYS   B C    1 
ATOM   978  O  O    . CYS   B 1 10  ? -5.101  -11.545 -36.739 1.00 41.13  ? 10  CYS   B O    1 
ATOM   979  C  CB   . CYS   B 1 10  ? -2.815  -13.823 -38.172 1.00 59.68  ? 10  CYS   B CB   1 
ATOM   980  S  SG   . CYS   B 1 10  ? -1.872  -14.292 -39.649 1.00 78.02  ? 10  CYS   B SG   1 
ATOM   981  N  N    . PRO   B 1 11  ? -5.430  -13.751 -36.580 1.00 26.52  ? 11  PRO   B N    1 
ATOM   982  C  CA   . PRO   B 1 11  ? -6.334  -13.555 -35.437 1.00 24.07  ? 11  PRO   B CA   1 
ATOM   983  C  C    . PRO   B 1 11  ? -5.648  -13.238 -34.117 1.00 25.67  ? 11  PRO   B C    1 
ATOM   984  O  O    . PRO   B 1 11  ? -6.350  -12.894 -33.152 1.00 23.76  ? 11  PRO   B O    1 
ATOM   985  C  CB   . PRO   B 1 11  ? -7.070  -14.897 -35.344 1.00 28.38  ? 11  PRO   B CB   1 
ATOM   986  C  CG   . PRO   B 1 11  ? -6.117  -15.866 -35.895 1.00 25.38  ? 11  PRO   B CG   1 
ATOM   987  C  CD   . PRO   B 1 11  ? -5.497  -15.149 -37.051 1.00 28.23  ? 11  PRO   B CD   1 
ATOM   988  N  N    . LEU   B 1 12  ? -4.323  -13.353 -34.035 1.00 19.00  ? 12  LEU   B N    1 
ATOM   989  C  CA   . LEU   B 1 12  ? -3.597  -13.176 -32.779 1.00 17.49  ? 12  LEU   B CA   1 
ATOM   990  C  C    . LEU   B 1 12  ? -2.309  -12.424 -33.065 1.00 21.87  ? 12  LEU   B C    1 
ATOM   991  O  O    . LEU   B 1 12  ? -1.468  -12.904 -33.830 1.00 26.54  ? 12  LEU   B O    1 
ATOM   992  C  CB   . LEU   B 1 12  ? -3.270  -14.530 -32.133 1.00 17.89  ? 12  LEU   B CB   1 
ATOM   993  C  CG   . LEU   B 1 12  ? -2.502  -14.510 -30.808 1.00 20.70  ? 12  LEU   B CG   1 
ATOM   994  C  CD1  . LEU   B 1 12  ? -3.322  -13.839 -29.699 1.00 22.73  ? 12  LEU   B CD1  1 
ATOM   995  C  CD2  . LEU   B 1 12  ? -2.097  -15.922 -30.392 1.00 26.60  ? 12  LEU   B CD2  1 
ATOM   996  N  N    . MET   B 1 13  ? -2.148  -11.253 -32.441 1.00 17.34  ? 13  MET   B N    1 
ATOM   997  C  CA   A MET   B 1 13  ? -0.935  -10.456 -32.567 0.48 18.38  ? 13  MET   B CA   1 
ATOM   998  C  CA   B MET   B 1 13  ? -0.939  -10.455 -32.568 0.52 18.38  ? 13  MET   B CA   1 
ATOM   999  C  C    . MET   B 1 13  ? -0.451  -10.099 -31.172 1.00 17.10  ? 13  MET   B C    1 
ATOM   1000 O  O    . MET   B 1 13  ? -1.248  -9.972  -30.239 1.00 19.42  ? 13  MET   B O    1 
ATOM   1001 C  CB   A MET   B 1 13  ? -1.158  -9.162  -33.392 0.48 22.19  ? 13  MET   B CB   1 
ATOM   1002 C  CB   B MET   B 1 13  ? -1.208  -9.173  -33.373 0.52 22.20  ? 13  MET   B CB   1 
ATOM   1003 C  CG   A MET   B 1 13  ? 0.134   -8.429  -33.814 0.48 22.35  ? 13  MET   B CG   1 
ATOM   1004 C  CG   B MET   B 1 13  ? -1.978  -9.407  -34.664 0.52 29.03  ? 13  MET   B CG   1 
ATOM   1005 S  SD   A MET   B 1 13  ? 0.715   -7.117  -32.694 0.48 23.11  ? 13  MET   B SD   1 
ATOM   1006 S  SD   B MET   B 1 13  ? -2.412  -7.875  -35.508 0.52 43.70  ? 13  MET   B SD   1 
ATOM   1007 C  CE   A MET   B 1 13  ? -0.393  -5.779  -33.131 0.48 24.40  ? 13  MET   B CE   1 
ATOM   1008 C  CE   B MET   B 1 13  ? -3.585  -8.471  -36.723 0.52 51.23  ? 13  MET   B CE   1 
ATOM   1009 N  N    . VAL   B 1 14  ? 0.866   -9.971  -31.026 1.00 15.79  ? 14  VAL   B N    1 
ATOM   1010 C  CA   . VAL   B 1 14  ? 1.479   -9.626  -29.746 1.00 16.61  ? 14  VAL   B CA   1 
ATOM   1011 C  C    . VAL   B 1 14  ? 2.359   -8.404  -29.957 1.00 20.16  ? 14  VAL   B C    1 
ATOM   1012 O  O    . VAL   B 1 14  ? 3.122   -8.345  -30.925 1.00 20.76  ? 14  VAL   B O    1 
ATOM   1013 C  CB   . VAL   B 1 14  ? 2.290   -10.799 -29.162 1.00 18.82  ? 14  VAL   B CB   1 
ATOM   1014 C  CG1  . VAL   B 1 14  ? 2.989   -10.379 -27.867 1.00 19.96  ? 14  VAL   B CG1  1 
ATOM   1015 C  CG2  . VAL   B 1 14  ? 1.376   -11.992 -28.905 1.00 16.36  ? 14  VAL   B CG2  1 
ATOM   1016 N  N    . LYS   B 1 15  ? 2.237   -7.412  -29.078 1.00 16.17  ? 15  LYS   B N    1 
ATOM   1017 C  CA   . LYS   B 1 15  ? 3.055   -6.214  -29.172 1.00 14.44  ? 15  LYS   B CA   1 
ATOM   1018 C  C    . LYS   B 1 15  ? 3.678   -5.954  -27.815 1.00 13.55  ? 15  LYS   B C    1 
ATOM   1019 O  O    . LYS   B 1 15  ? 2.980   -6.018  -26.797 1.00 15.74  ? 15  LYS   B O    1 
ATOM   1020 C  CB   . LYS   B 1 15  ? 2.244   -4.991  -29.609 1.00 20.26  ? 15  LYS   B CB   1 
ATOM   1021 C  CG   . LYS   B 1 15  ? 3.099   -3.738  -29.729 1.00 24.50  ? 15  LYS   B CG   1 
ATOM   1022 C  CD   . LYS   B 1 15  ? 2.553   -2.730  -30.724 1.00 29.85  ? 15  LYS   B CD   1 
ATOM   1023 C  CE   . LYS   B 1 15  ? 3.593   -1.642  -30.984 1.00 29.37  ? 15  LYS   B CE   1 
ATOM   1024 N  NZ   . LYS   B 1 15  ? 3.334   -0.888  -32.245 1.00 43.76  ? 15  LYS   B NZ   1 
ATOM   1025 N  N    . VAL   B 1 16  ? 4.971   -5.646  -27.796 1.00 13.89  ? 16  VAL   B N    1 
ATOM   1026 C  CA   . VAL   B 1 16  ? 5.724   -5.512  -26.550 1.00 12.27  ? 16  VAL   B CA   1 
ATOM   1027 C  C    . VAL   B 1 16  ? 6.492   -4.201  -26.590 1.00 17.34  ? 16  VAL   B C    1 
ATOM   1028 O  O    . VAL   B 1 16  ? 7.196   -3.918  -27.570 1.00 15.12  ? 16  VAL   B O    1 
ATOM   1029 C  CB   . VAL   B 1 16  ? 6.678   -6.698  -26.310 1.00 14.54  ? 16  VAL   B CB   1 
ATOM   1030 C  CG1  . VAL   B 1 16  ? 7.255   -6.628  -24.889 1.00 14.14  ? 16  VAL   B CG1  1 
ATOM   1031 C  CG2  . VAL   B 1 16  ? 5.964   -8.035  -26.501 1.00 16.81  ? 16  VAL   B CG2  1 
ATOM   1032 N  N    . LEU   B 1 17  ? 6.359   -3.405  -25.522 1.00 14.62  ? 17  LEU   B N    1 
ATOM   1033 C  CA   . LEU   B 1 17  ? 7.006   -2.108  -25.391 1.00 12.34  ? 17  LEU   B CA   1 
ATOM   1034 C  C    . LEU   B 1 17  ? 7.892   -2.103  -24.157 1.00 11.55  ? 17  LEU   B C    1 
ATOM   1035 O  O    . LEU   B 1 17  ? 7.629   -2.823  -23.184 1.00 14.43  ? 17  LEU   B O    1 
ATOM   1036 C  CB   . LEU   B 1 17  ? 5.959   -0.998  -25.223 1.00 15.12  ? 17  LEU   B CB   1 
ATOM   1037 C  CG   . LEU   B 1 17  ? 4.954   -0.851  -26.369 1.00 16.56  ? 17  LEU   B CG   1 
ATOM   1038 C  CD1  . LEU   B 1 17  ? 3.992   0.300   -26.119 1.00 22.67  ? 17  LEU   B CD1  1 
ATOM   1039 C  CD2  . LEU   B 1 17  ? 5.720   -0.629  -27.657 1.00 19.76  ? 17  LEU   B CD2  1 
ATOM   1040 N  N    . ASP   B 1 18  ? 8.921   -1.262  -24.193 1.00 13.23  ? 18  ASP   B N    1 
ATOM   1041 C  CA   . ASP   B 1 18  ? 9.921   -1.138  -23.140 1.00 12.13  ? 18  ASP   B CA   1 
ATOM   1042 C  C    . ASP   B 1 18  ? 9.719   0.216   -22.467 1.00 13.75  ? 18  ASP   B C    1 
ATOM   1043 O  O    . ASP   B 1 18  ? 9.859   1.266   -23.112 1.00 14.14  ? 18  ASP   B O    1 
ATOM   1044 C  CB   . ASP   B 1 18  ? 11.310  -1.267  -23.780 1.00 11.97  ? 18  ASP   B CB   1 
ATOM   1045 C  CG   . ASP   B 1 18  ? 12.457  -1.110  -22.808 1.00 17.20  ? 18  ASP   B CG   1 
ATOM   1046 O  OD1  . ASP   B 1 18  ? 12.370  -0.335  -21.835 1.00 15.38  ? 18  ASP   B OD1  1 
ATOM   1047 O  OD2  . ASP   B 1 18  ? 13.498  -1.758  -23.047 1.00 17.60  ? 18  ASP   B OD2  1 
ATOM   1048 N  N    . ALA   B 1 19  ? 9.382   0.196   -21.174 1.00 12.45  ? 19  ALA   B N    1 
ATOM   1049 C  CA   . ALA   B 1 19  ? 9.063   1.405   -20.422 1.00 12.89  ? 19  ALA   B CA   1 
ATOM   1050 C  C    . ALA   B 1 19  ? 10.292  2.096   -19.862 1.00 13.77  ? 19  ALA   B C    1 
ATOM   1051 O  O    . ALA   B 1 19  ? 10.166  3.210   -19.341 1.00 16.01  ? 19  ALA   B O    1 
ATOM   1052 C  CB   . ALA   B 1 19  ? 8.112   1.070   -19.261 1.00 13.46  ? 19  ALA   B CB   1 
ATOM   1053 N  N    . VAL   B 1 20  ? 11.463  1.468   -19.951 1.00 13.15  ? 20  VAL   B N    1 
ATOM   1054 C  CA   . VAL   B 1 20  ? 12.719  2.064   -19.510 1.00 15.01  ? 20  VAL   B CA   1 
ATOM   1055 C  C    . VAL   B 1 20  ? 13.371  2.849   -20.632 1.00 17.58  ? 20  VAL   B C    1 
ATOM   1056 O  O    . VAL   B 1 20  ? 13.870  3.953   -20.409 1.00 23.33  ? 20  VAL   B O    1 
ATOM   1057 C  CB   . VAL   B 1 20  ? 13.659  0.959   -18.993 1.00 18.38  ? 20  VAL   B CB   1 
ATOM   1058 C  CG1  . VAL   B 1 20  ? 15.011  1.548   -18.598 1.00 23.17  ? 20  VAL   B CG1  1 
ATOM   1059 C  CG2  . VAL   B 1 20  ? 13.028  0.245   -17.821 1.00 19.30  ? 20  VAL   B CG2  1 
ATOM   1060 N  N    . ARG   B 1 21  ? 13.386  2.274   -21.830 1.00 16.62  ? 21  ARG   B N    1 
ATOM   1061 C  CA   . ARG   B 1 21  ? 14.027  2.885   -22.983 1.00 19.24  ? 21  ARG   B CA   1 
ATOM   1062 C  C    . ARG   B 1 21  ? 13.061  3.668   -23.862 1.00 19.19  ? 21  ARG   B C    1 
ATOM   1063 O  O    . ARG   B 1 21  ? 13.512  4.401   -24.754 1.00 19.76  ? 21  ARG   B O    1 
ATOM   1064 C  CB   . ARG   B 1 21  ? 14.751  1.806   -23.794 1.00 23.49  ? 21  ARG   B CB   1 
ATOM   1065 C  CG   . ARG   B 1 21  ? 15.778  1.059   -22.935 1.00 25.98  ? 21  ARG   B CG   1 
ATOM   1066 C  CD   . ARG   B 1 21  ? 16.151  -0.315  -23.477 1.00 32.74  ? 21  ARG   B CD   1 
ATOM   1067 N  NE   . ARG   B 1 21  ? 17.170  -0.278  -24.515 1.00 40.99  ? 21  ARG   B NE   1 
ATOM   1068 C  CZ   . ARG   B 1 21  ? 17.058  -0.877  -25.690 1.00 50.86  ? 21  ARG   B CZ   1 
ATOM   1069 N  NH1  . ARG   B 1 21  ? 15.973  -1.560  -26.016 1.00 49.30  ? 21  ARG   B NH1  1 
ATOM   1070 N  NH2  . ARG   B 1 21  ? 18.065  -0.801  -26.555 1.00 67.51  ? 21  ARG   B NH2  1 
ATOM   1071 N  N    . GLY   B 1 22  ? 11.755  3.546   -23.639 1.00 15.22  ? 22  GLY   B N    1 
ATOM   1072 C  CA   . GLY   B 1 22  ? 10.782  4.257   -24.461 1.00 14.75  ? 22  GLY   B CA   1 
ATOM   1073 C  C    . GLY   B 1 22  ? 10.796  3.771   -25.897 1.00 14.78  ? 22  GLY   B C    1 
ATOM   1074 O  O    . GLY   B 1 22  ? 10.796  4.564   -26.847 1.00 17.96  ? 22  GLY   B O    1 
ATOM   1075 N  N    . SER   B 1 23  ? 10.809  2.464   -26.065 1.00 15.22  ? 23  SER   B N    1 
ATOM   1076 C  CA   . SER   B 1 23  ? 11.000  1.885   -27.387 1.00 15.65  ? 23  SER   B CA   1 
ATOM   1077 C  C    . SER   B 1 23  ? 10.160  0.627   -27.517 1.00 17.53  ? 23  SER   B C    1 
ATOM   1078 O  O    . SER   B 1 23  ? 9.673   0.087   -26.512 1.00 16.63  ? 23  SER   B O    1 
ATOM   1079 C  CB   . SER   B 1 23  ? 12.472  1.502   -27.557 1.00 19.15  ? 23  SER   B CB   1 
ATOM   1080 O  OG   . SER   B 1 23  ? 12.848  0.486   -26.642 1.00 21.97  ? 23  SER   B OG   1 
ATOM   1081 N  N    . PRO   B 1 24  ? 9.984   0.113   -28.724 1.00 15.90  ? 24  PRO   B N    1 
ATOM   1082 C  CA   . PRO   B 1 24  ? 9.550   -1.275  -28.860 1.00 17.96  ? 24  PRO   B CA   1 
ATOM   1083 C  C    . PRO   B 1 24  ? 10.553  -2.176  -28.160 1.00 14.32  ? 24  PRO   B C    1 
ATOM   1084 O  O    . PRO   B 1 24  ? 11.744  -1.870  -28.079 1.00 17.74  ? 24  PRO   B O    1 
ATOM   1085 C  CB   . PRO   B 1 24  ? 9.583   -1.511  -30.377 1.00 16.30  ? 24  PRO   B CB   1 
ATOM   1086 C  CG   . PRO   B 1 24  ? 9.610   -0.154  -30.992 1.00 22.44  ? 24  PRO   B CG   1 
ATOM   1087 C  CD   . PRO   B 1 24  ? 10.308  0.738   -30.022 1.00 17.89  ? 24  PRO   B CD   1 
ATOM   1088 N  N    . ALA   B 1 25  ? 10.055  -3.293  -27.630 1.00 15.13  ? 25  ALA   B N    1 
ATOM   1089 C  CA   . ALA   B 1 25  ? 10.922  -4.341  -27.100 1.00 15.49  ? 25  ALA   B CA   1 
ATOM   1090 C  C    . ALA   B 1 25  ? 11.194  -5.314  -28.243 1.00 14.69  ? 25  ALA   B C    1 
ATOM   1091 O  O    . ALA   B 1 25  ? 10.327  -6.103  -28.618 1.00 16.21  ? 25  ALA   B O    1 
ATOM   1092 C  CB   . ALA   B 1 25  ? 10.275  -5.031  -25.901 1.00 17.03  ? 25  ALA   B CB   1 
ATOM   1093 N  N    A ILE   B 1 26  ? 12.409  -5.257  -28.781 0.63 16.69  ? 26  ILE   B N    1 
ATOM   1094 N  N    B ILE   B 1 26  ? 12.388  -5.240  -28.805 0.37 16.71  ? 26  ILE   B N    1 
ATOM   1095 C  CA   A ILE   B 1 26  ? 12.790  -5.964  -29.999 0.63 18.37  ? 26  ILE   B CA   1 
ATOM   1096 C  CA   B ILE   B 1 26  ? 12.723  -6.003  -30.000 0.37 18.34  ? 26  ILE   B CA   1 
ATOM   1097 C  C    A ILE   B 1 26  ? 13.441  -7.287  -29.623 0.63 16.99  ? 26  ILE   B C    1 
ATOM   1098 C  C    B ILE   B 1 26  ? 13.401  -7.304  -29.603 0.37 17.06  ? 26  ILE   B C    1 
ATOM   1099 O  O    A ILE   B 1 26  ? 14.157  -7.373  -28.617 0.63 18.62  ? 26  ILE   B O    1 
ATOM   1100 O  O    B ILE   B 1 26  ? 14.085  -7.398  -28.577 0.37 18.80  ? 26  ILE   B O    1 
ATOM   1101 C  CB   A ILE   B 1 26  ? 13.757  -5.089  -30.823 0.63 20.71  ? 26  ILE   B CB   1 
ATOM   1102 C  CB   B ILE   B 1 26  ? 13.589  -5.176  -30.975 0.37 20.91  ? 26  ILE   B CB   1 
ATOM   1103 C  CG1  A ILE   B 1 26  ? 13.158  -3.698  -31.062 0.63 19.85  ? 26  ILE   B CG1  1 
ATOM   1104 C  CG1  B ILE   B 1 26  ? 15.032  -5.083  -30.469 0.37 23.21  ? 26  ILE   B CG1  1 
ATOM   1105 C  CG2  A ILE   B 1 26  ? 14.096  -5.757  -32.139 0.63 23.41  ? 26  ILE   B CG2  1 
ATOM   1106 C  CG2  B ILE   B 1 26  ? 12.987  -3.788  -31.168 0.37 19.73  ? 26  ILE   B CG2  1 
ATOM   1107 C  CD1  A ILE   B 1 26  ? 14.144  -2.706  -31.681 0.63 22.40  ? 26  ILE   B CD1  1 
ATOM   1108 C  CD1  B ILE   B 1 26  ? 16.015  -4.585  -31.514 0.37 21.15  ? 26  ILE   B CD1  1 
ATOM   1109 N  N    . ASN   B 1 27  ? 13.198  -8.328  -30.430 1.00 17.97  ? 27  ASN   B N    1 
ATOM   1110 C  CA   A ASN   B 1 27  ? 13.856  -9.623  -30.256 0.59 18.87  ? 27  ASN   B CA   1 
ATOM   1111 C  CA   B ASN   B 1 27  ? 13.846  -9.631  -30.258 0.41 18.94  ? 27  ASN   B CA   1 
ATOM   1112 C  C    . ASN   B 1 27  ? 13.446  -10.316 -28.959 1.00 19.63  ? 27  ASN   B C    1 
ATOM   1113 O  O    . ASN   B 1 27  ? 14.241  -11.045 -28.363 1.00 21.33  ? 27  ASN   B O    1 
ATOM   1114 C  CB   A ASN   B 1 27  ? 15.383  -9.499  -30.348 0.59 20.43  ? 27  ASN   B CB   1 
ATOM   1115 C  CB   B ASN   B 1 27  ? 15.370  -9.548  -30.382 0.41 20.51  ? 27  ASN   B CB   1 
ATOM   1116 C  CG   A ASN   B 1 27  ? 16.039  -10.741 -30.895 0.59 26.45  ? 27  ASN   B CG   1 
ATOM   1117 C  CG   B ASN   B 1 27  ? 15.821  -9.328  -31.803 0.41 23.30  ? 27  ASN   B CG   1 
ATOM   1118 O  OD1  A ASN   B 1 27  ? 15.434  -11.486 -31.664 0.59 27.53  ? 27  ASN   B OD1  1 
ATOM   1119 O  OD1  B ASN   B 1 27  ? 15.253  -9.891  -32.738 0.41 25.73  ? 27  ASN   B OD1  1 
ATOM   1120 N  ND2  A ASN   B 1 27  ? 17.288  -10.969 -30.507 0.59 31.69  ? 27  ASN   B ND2  1 
ATOM   1121 N  ND2  B ASN   B 1 27  ? 16.849  -8.506  -31.977 0.41 25.28  ? 27  ASN   B ND2  1 
ATOM   1122 N  N    . VAL   B 1 28  ? 12.218  -10.087 -28.499 1.00 16.69  ? 28  VAL   B N    1 
ATOM   1123 C  CA   . VAL   B 1 28  ? 11.695  -10.773 -27.322 1.00 17.34  ? 28  VAL   B CA   1 
ATOM   1124 C  C    . VAL   B 1 28  ? 11.057  -12.075 -27.775 1.00 18.58  ? 28  VAL   B C    1 
ATOM   1125 O  O    . VAL   B 1 28  ? 10.180  -12.072 -28.650 1.00 16.17  ? 28  VAL   B O    1 
ATOM   1126 C  CB   . VAL   B 1 28  ? 10.656  -9.907  -26.594 1.00 16.64  ? 28  VAL   B CB   1 
ATOM   1127 C  CG1  . VAL   B 1 28  ? 10.117  -10.650 -25.371 1.00 18.62  ? 28  VAL   B CG1  1 
ATOM   1128 C  CG2  . VAL   B 1 28  ? 11.249  -8.591  -26.181 1.00 21.00  ? 28  VAL   B CG2  1 
ATOM   1129 N  N    . ALA   B 1 29  ? 11.476  -13.186 -27.173 1.00 15.57  ? 29  ALA   B N    1 
ATOM   1130 C  CA   . ALA   B 1 29  ? 10.853  -14.461 -27.496 1.00 15.33  ? 29  ALA   B CA   1 
ATOM   1131 C  C    . ALA   B 1 29  ? 9.465   -14.541 -26.883 1.00 15.62  ? 29  ALA   B C    1 
ATOM   1132 O  O    . ALA   B 1 29  ? 9.229   -14.108 -25.751 1.00 15.09  ? 29  ALA   B O    1 
ATOM   1133 C  CB   . ALA   B 1 29  ? 11.705  -15.630 -27.005 1.00 15.27  ? 29  ALA   B CB   1 
ATOM   1134 N  N    . VAL   B 1 30  ? 8.533   -15.084 -27.653 1.00 15.91  ? 30  VAL   B N    1 
ATOM   1135 C  CA   . VAL   B 1 30  ? 7.147   -15.240 -27.247 1.00 15.30  ? 30  VAL   B CA   1 
ATOM   1136 C  C    . VAL   B 1 30  ? 6.737   -16.660 -27.581 1.00 18.23  ? 30  VAL   B C    1 
ATOM   1137 O  O    . VAL   B 1 30  ? 6.875   -17.084 -28.731 1.00 20.09  ? 30  VAL   B O    1 
ATOM   1138 C  CB   . VAL   B 1 30  ? 6.238   -14.241 -27.982 1.00 16.60  ? 30  VAL   B CB   1 
ATOM   1139 C  CG1  . VAL   B 1 30  ? 4.774   -14.491 -27.621 1.00 16.81  ? 30  VAL   B CG1  1 
ATOM   1140 C  CG2  . VAL   B 1 30  ? 6.648   -12.813 -27.658 1.00 17.06  ? 30  VAL   B CG2  1 
ATOM   1141 N  N    . HIS   B 1 31  ? 6.220   -17.381 -26.594 1.00 15.51  ? 31  HIS   B N    1 
ATOM   1142 C  CA   . HIS   B 1 31  ? 5.734   -18.742 -26.779 1.00 18.92  ? 31  HIS   B CA   1 
ATOM   1143 C  C    . HIS   B 1 31  ? 4.260   -18.799 -26.412 1.00 22.59  ? 31  HIS   B C    1 
ATOM   1144 O  O    . HIS   B 1 31  ? 3.871   -18.374 -25.316 1.00 18.84  ? 31  HIS   B O    1 
ATOM   1145 C  CB   . HIS   B 1 31  ? 6.522   -19.728 -25.914 1.00 17.20  ? 31  HIS   B CB   1 
ATOM   1146 C  CG   . HIS   B 1 31  ? 7.969   -19.831 -26.281 1.00 19.69  ? 31  HIS   B CG   1 
ATOM   1147 N  ND1  . HIS   B 1 31  ? 8.490   -20.933 -26.927 1.00 22.96  ? 31  HIS   B ND1  1 
ATOM   1148 C  CD2  . HIS   B 1 31  ? 9.004   -18.977 -26.099 1.00 22.06  ? 31  HIS   B CD2  1 
ATOM   1149 C  CE1  . HIS   B 1 31  ? 9.782   -20.748 -27.134 1.00 22.34  ? 31  HIS   B CE1  1 
ATOM   1150 N  NE2  . HIS   B 1 31  ? 10.120  -19.571 -26.640 1.00 21.81  ? 31  HIS   B NE2  1 
ATOM   1151 N  N    . VAL   B 1 32  ? 3.448   -19.335 -27.319 1.00 18.12  ? 32  VAL   B N    1 
ATOM   1152 C  CA   . VAL   B 1 32  ? 2.014   -19.506 -27.105 1.00 17.85  ? 32  VAL   B CA   1 
ATOM   1153 C  C    . VAL   B 1 32  ? 1.718   -20.982 -26.894 1.00 20.45  ? 32  VAL   B C    1 
ATOM   1154 O  O    . VAL   B 1 32  ? 2.265   -21.841 -27.599 1.00 22.97  ? 32  VAL   B O    1 
ATOM   1155 C  CB   . VAL   B 1 32  ? 1.200   -18.958 -28.292 1.00 18.16  ? 32  VAL   B CB   1 
ATOM   1156 C  CG1  . VAL   B 1 32  ? -0.281  -18.953 -27.966 1.00 17.51  ? 32  VAL   B CG1  1 
ATOM   1157 C  CG2  . VAL   B 1 32  ? 1.665   -17.556 -28.656 1.00 17.70  ? 32  VAL   B CG2  1 
ATOM   1158 N  N    . PHE   B 1 33  ? 0.846   -21.268 -25.934 1.00 18.18  ? 33  PHE   B N    1 
ATOM   1159 C  CA   . PHE   B 1 33  ? 0.423   -22.619 -25.594 1.00 18.46  ? 33  PHE   B CA   1 
ATOM   1160 C  C    . PHE   B 1 33  ? -1.098  -22.677 -25.574 1.00 24.90  ? 33  PHE   B C    1 
ATOM   1161 O  O    . PHE   B 1 33  ? -1.772  -21.671 -25.331 1.00 19.65  ? 33  PHE   B O    1 
ATOM   1162 C  CB   . PHE   B 1 33  ? 0.950   -23.031 -24.204 1.00 20.72  ? 33  PHE   B CB   1 
ATOM   1163 C  CG   . PHE   B 1 33  ? 2.440   -22.869 -24.045 1.00 20.26  ? 33  PHE   B CG   1 
ATOM   1164 C  CD1  . PHE   B 1 33  ? 2.986   -21.658 -23.639 1.00 22.84  ? 33  PHE   B CD1  1 
ATOM   1165 C  CD2  . PHE   B 1 33  ? 3.292   -23.931 -24.298 1.00 24.97  ? 33  PHE   B CD2  1 
ATOM   1166 C  CE1  . PHE   B 1 33  ? 4.358   -21.511 -23.497 1.00 24.01  ? 33  PHE   B CE1  1 
ATOM   1167 C  CE2  . PHE   B 1 33  ? 4.665   -23.792 -24.158 1.00 26.30  ? 33  PHE   B CE2  1 
ATOM   1168 C  CZ   . PHE   B 1 33  ? 5.199   -22.582 -23.757 1.00 29.34  ? 33  PHE   B CZ   1 
ATOM   1169 N  N    . ARG   B 1 34  ? -1.644  -23.859 -25.853 1.00 20.60  ? 34  ARG   B N    1 
ATOM   1170 C  CA   A ARG   B 1 34  ? -3.075  -24.106 -25.741 0.38 17.41  ? 34  ARG   B CA   1 
ATOM   1171 C  CA   B ARG   B 1 34  ? -3.073  -24.098 -25.730 0.62 17.35  ? 34  ARG   B CA   1 
ATOM   1172 C  C    . ARG   B 1 34  ? -3.316  -25.207 -24.720 1.00 21.22  ? 34  ARG   B C    1 
ATOM   1173 O  O    . ARG   B 1 34  ? -2.589  -26.207 -24.690 1.00 24.14  ? 34  ARG   B O    1 
ATOM   1174 C  CB   A ARG   B 1 34  ? -3.694  -24.510 -27.091 0.38 22.19  ? 34  ARG   B CB   1 
ATOM   1175 C  CB   B ARG   B 1 34  ? -3.713  -24.465 -27.075 0.62 22.20  ? 34  ARG   B CB   1 
ATOM   1176 C  CG   A ARG   B 1 34  ? -5.222  -24.611 -27.064 0.38 25.91  ? 34  ARG   B CG   1 
ATOM   1177 C  CG   B ARG   B 1 34  ? -5.232  -24.591 -27.008 0.62 25.93  ? 34  ARG   B CG   1 
ATOM   1178 C  CD   A ARG   B 1 34  ? -5.800  -25.036 -28.416 0.38 28.77  ? 34  ARG   B CD   1 
ATOM   1179 C  CD   B ARG   B 1 34  ? -5.848  -24.547 -28.393 0.62 27.77  ? 34  ARG   B CD   1 
ATOM   1180 N  NE   A ARG   B 1 34  ? -7.259  -25.033 -28.410 0.38 30.27  ? 34  ARG   B NE   1 
ATOM   1181 N  NE   B ARG   B 1 34  ? -5.314  -25.586 -29.261 0.62 23.18  ? 34  ARG   B NE   1 
ATOM   1182 C  CZ   A ARG   B 1 34  ? -8.013  -26.091 -28.143 0.38 33.74  ? 34  ARG   B CZ   1 
ATOM   1183 C  CZ   B ARG   B 1 34  ? -5.402  -25.573 -30.583 0.62 26.27  ? 34  ARG   B CZ   1 
ATOM   1184 N  NH1  A ARG   B 1 34  ? -7.478  -27.271 -27.873 0.38 40.26  ? 34  ARG   B NH1  1 
ATOM   1185 N  NH1  B ARG   B 1 34  ? -5.981  -24.572 -31.227 0.62 23.10  ? 34  ARG   B NH1  1 
ATOM   1186 N  NH2  A ARG   B 1 34  ? -9.337  -25.963 -28.150 0.38 34.65  ? 34  ARG   B NH2  1 
ATOM   1187 N  NH2  B ARG   B 1 34  ? -4.890  -26.585 -31.278 0.62 23.19  ? 34  ARG   B NH2  1 
ATOM   1188 N  N    . LYS   B 1 35  ? -4.332  -25.023 -23.887 1.00 18.33  ? 35  LYS   B N    1 
ATOM   1189 C  CA   . LYS   B 1 35  ? -4.644  -26.005 -22.861 1.00 21.00  ? 35  LYS   B CA   1 
ATOM   1190 C  C    . LYS   B 1 35  ? -5.257  -27.246 -23.506 1.00 23.13  ? 35  LYS   B C    1 
ATOM   1191 O  O    . LYS   B 1 35  ? -6.187  -27.145 -24.311 1.00 22.87  ? 35  LYS   B O    1 
ATOM   1192 C  CB   . LYS   B 1 35  ? -5.604  -25.397 -21.841 1.00 24.26  ? 35  LYS   B CB   1 
ATOM   1193 C  CG   . LYS   B 1 35  ? -5.506  -26.022 -20.463 1.00 31.51  ? 35  LYS   B CG   1 
ATOM   1194 C  CD   . LYS   B 1 35  ? -6.175  -25.149 -19.416 1.00 36.87  ? 35  LYS   B CD   1 
ATOM   1195 C  CE   . LYS   B 1 35  ? -5.824  -25.615 -18.011 1.00 51.23  ? 35  LYS   B CE   1 
ATOM   1196 N  NZ   . LYS   B 1 35  ? -6.584  -24.870 -16.972 1.00 57.37  ? 35  LYS   B NZ   1 
ATOM   1197 N  N    . ALA   B 1 36  ? -4.706  -28.412 -23.185 1.00 22.18  ? 36  ALA   B N    1 
ATOM   1198 C  CA   . ALA   B 1 36  ? -5.189  -29.672 -23.728 1.00 24.69  ? 36  ALA   B CA   1 
ATOM   1199 C  C    . ALA   B 1 36  ? -6.245  -30.275 -22.807 1.00 33.42  ? 36  ALA   B C    1 
ATOM   1200 O  O    . ALA   B 1 36  ? -6.459  -29.822 -21.680 1.00 33.18  ? 36  ALA   B O    1 
ATOM   1201 C  CB   . ALA   B 1 36  ? -4.027  -30.643 -23.922 1.00 25.91  ? 36  ALA   B CB   1 
ATOM   1202 N  N    . ALA   B 1 37  ? -6.903  -31.329 -23.302 1.00 33.94  ? 37  ALA   B N    1 
ATOM   1203 C  CA   . ALA   B 1 37  ? -7.994  -31.947 -22.552 1.00 37.71  ? 37  ALA   B CA   1 
ATOM   1204 C  C    . ALA   B 1 37  ? -7.530  -32.483 -21.205 1.00 33.18  ? 37  ALA   B C    1 
ATOM   1205 O  O    . ALA   B 1 37  ? -8.315  -32.523 -20.252 1.00 38.81  ? 37  ALA   B O    1 
ATOM   1206 C  CB   . ALA   B 1 37  ? -8.635  -33.064 -23.379 1.00 39.72  ? 37  ALA   B CB   1 
ATOM   1207 N  N    . ASP   B 1 38  ? -6.268  -32.891 -21.100 1.00 32.65  ? 38  ASP   B N    1 
ATOM   1208 C  CA   . ASP   B 1 38  ? -5.716  -33.378 -19.843 1.00 36.37  ? 38  ASP   B CA   1 
ATOM   1209 C  C    . ASP   B 1 38  ? -5.188  -32.256 -18.956 1.00 43.62  ? 38  ASP   B C    1 
ATOM   1210 O  O    . ASP   B 1 38  ? -4.489  -32.533 -17.976 1.00 40.31  ? 38  ASP   B O    1 
ATOM   1211 C  CB   . ASP   B 1 38  ? -4.645  -34.452 -20.091 1.00 39.01  ? 38  ASP   B CB   1 
ATOM   1212 C  CG   . ASP   B 1 38  ? -3.398  -33.906 -20.773 1.00 42.95  ? 38  ASP   B CG   1 
ATOM   1213 O  OD1  . ASP   B 1 38  ? -3.363  -32.709 -21.128 1.00 33.37  ? 38  ASP   B OD1  1 
ATOM   1214 O  OD2  . ASP   B 1 38  ? -2.439  -34.685 -20.950 1.00 45.71  ? 38  ASP   B OD2  1 
ATOM   1215 N  N    . ASP   B 1 39  ? -5.501  -31.003 -19.290 1.00 38.84  ? 39  ASP   B N    1 
ATOM   1216 C  CA   . ASP   B 1 39  ? -5.167  -29.801 -18.525 1.00 38.54  ? 39  ASP   B CA   1 
ATOM   1217 C  C    . ASP   B 1 39  ? -3.695  -29.414 -18.580 1.00 36.12  ? 39  ASP   B C    1 
ATOM   1218 O  O    . ASP   B 1 39  ? -3.262  -28.552 -17.804 1.00 49.12  ? 39  ASP   B O    1 
ATOM   1219 C  CB   . ASP   B 1 39  ? -5.684  -29.826 -17.080 1.00 55.41  ? 39  ASP   B CB   1 
ATOM   1220 C  CG   . ASP   B 1 39  ? -7.099  -29.294 -16.961 1.00 56.68  ? 39  ASP   B CG   1 
ATOM   1221 O  OD1  . ASP   B 1 39  ? -7.678  -28.903 -17.998 1.00 56.55  ? 39  ASP   B OD1  1 
ATOM   1222 O  OD2  . ASP   B 1 39  ? -7.631  -29.262 -15.832 1.00 73.96  ? 39  ASP   B OD2  1 
ATOM   1223 N  N    . THR   B 1 40  ? -2.915  -30.008 -19.474 1.00 30.26  ? 40  THR   B N    1 
ATOM   1224 C  CA   . THR   B 1 40  ? -1.534  -29.600 -19.676 1.00 28.93  ? 40  THR   B CA   1 
ATOM   1225 C  C    . THR   B 1 40  ? -1.458  -28.520 -20.752 1.00 30.05  ? 40  THR   B C    1 
ATOM   1226 O  O    . THR   B 1 40  ? -2.391  -28.318 -21.532 1.00 26.64  ? 40  THR   B O    1 
ATOM   1227 C  CB   . THR   B 1 40  ? -0.680  -30.805 -20.074 1.00 34.46  ? 40  THR   B CB   1 
ATOM   1228 O  OG1  . THR   B 1 40  ? -1.087  -31.276 -21.365 1.00 31.02  ? 40  THR   B OG1  1 
ATOM   1229 C  CG2  . THR   B 1 40  ? -0.850  -31.929 -19.058 1.00 41.75  ? 40  THR   B CG2  1 
ATOM   1230 N  N    . TRP   B 1 41  ? -0.327  -27.825 -20.791 1.00 29.83  ? 41  TRP   B N    1 
ATOM   1231 C  CA   . TRP   B 1 41  ? -0.099  -26.764 -21.764 1.00 26.51  ? 41  TRP   B CA   1 
ATOM   1232 C  C    . TRP   B 1 41  ? 0.672   -27.320 -22.950 1.00 30.50  ? 41  TRP   B C    1 
ATOM   1233 O  O    . TRP   B 1 41  ? 1.831   -27.724 -22.808 1.00 33.09  ? 41  TRP   B O    1 
ATOM   1234 C  CB   . TRP   B 1 41  ? 0.679   -25.610 -21.141 1.00 27.79  ? 41  TRP   B CB   1 
ATOM   1235 C  CG   . TRP   B 1 41  ? -0.119  -24.843 -20.157 1.00 28.87  ? 41  TRP   B CG   1 
ATOM   1236 C  CD1  . TRP   B 1 41  ? 0.028   -24.847 -18.799 1.00 34.54  ? 41  TRP   B CD1  1 
ATOM   1237 C  CD2  . TRP   B 1 41  ? -1.210  -23.958 -20.442 1.00 23.36  ? 41  TRP   B CD2  1 
ATOM   1238 N  NE1  . TRP   B 1 41  ? -0.896  -24.014 -18.225 1.00 38.36  ? 41  TRP   B NE1  1 
ATOM   1239 C  CE2  . TRP   B 1 41  ? -1.668  -23.454 -19.210 1.00 27.92  ? 41  TRP   B CE2  1 
ATOM   1240 C  CE3  . TRP   B 1 41  ? -1.838  -23.539 -21.620 1.00 19.70  ? 41  TRP   B CE3  1 
ATOM   1241 C  CZ2  . TRP   B 1 41  ? -2.730  -22.557 -19.118 1.00 25.91  ? 41  TRP   B CZ2  1 
ATOM   1242 C  CZ3  . TRP   B 1 41  ? -2.895  -22.647 -21.526 1.00 23.32  ? 41  TRP   B CZ3  1 
ATOM   1243 C  CH2  . TRP   B 1 41  ? -3.326  -22.165 -20.287 1.00 23.03  ? 41  TRP   B CH2  1 
ATOM   1244 N  N    . GLU   B 1 42  ? 0.039   -27.319 -24.111 1.00 29.19  ? 42  GLU   B N    1 
ATOM   1245 C  CA   . GLU   B 1 42  ? 0.667   -27.827 -25.323 1.00 27.63  ? 42  GLU   B CA   1 
ATOM   1246 C  C    . GLU   B 1 42  ? 1.208   -26.676 -26.148 1.00 28.62  ? 42  GLU   B C    1 
ATOM   1247 O  O    . GLU   B 1 42  ? 0.473   -25.712 -26.398 1.00 25.23  ? 42  GLU   B O    1 
ATOM   1248 C  CB   . GLU   B 1 42  ? -0.356  -28.598 -26.152 1.00 34.72  ? 42  GLU   B CB   1 
ATOM   1249 C  CG   . GLU   B 1 42  ? -0.802  -29.896 -25.513 1.00 54.32  ? 42  GLU   B CG   1 
ATOM   1250 C  CD   . GLU   B 1 42  ? -1.323  -30.889 -26.529 1.00 68.06  ? 42  GLU   B CD   1 
ATOM   1251 O  OE1  . GLU   B 1 42  ? -1.875  -30.451 -27.562 1.00 61.38  ? 42  GLU   B OE1  1 
ATOM   1252 O  OE2  . GLU   B 1 42  ? -1.168  -32.107 -26.300 1.00 74.37  ? 42  GLU   B OE2  1 
ATOM   1253 N  N    . PRO   B 1 43  ? 2.463   -26.736 -26.590 1.00 23.66  ? 43  PRO   B N    1 
ATOM   1254 C  CA   . PRO   B 1 43  ? 2.987   -25.697 -27.485 1.00 25.70  ? 43  PRO   B CA   1 
ATOM   1255 C  C    . PRO   B 1 43  ? 2.096   -25.497 -28.701 1.00 25.81  ? 43  PRO   B C    1 
ATOM   1256 O  O    . PRO   B 1 43  ? 1.609   -26.454 -29.308 1.00 27.59  ? 43  PRO   B O    1 
ATOM   1257 C  CB   . PRO   B 1 43  ? 4.362   -26.243 -27.889 1.00 33.38  ? 43  PRO   B CB   1 
ATOM   1258 C  CG   . PRO   B 1 43  ? 4.752   -27.120 -26.767 1.00 24.85  ? 43  PRO   B CG   1 
ATOM   1259 C  CD   . PRO   B 1 43  ? 3.488   -27.736 -26.244 1.00 32.58  ? 43  PRO   B CD   1 
ATOM   1260 N  N    . PHE   B 1 44  ? 1.899   -24.231 -29.061 1.00 23.25  ? 44  PHE   B N    1 
ATOM   1261 C  CA   . PHE   B 1 44  ? 1.005   -23.839 -30.144 1.00 18.96  ? 44  PHE   B CA   1 
ATOM   1262 C  C    . PHE   B 1 44  ? 1.694   -23.000 -31.207 1.00 24.48  ? 44  PHE   B C    1 
ATOM   1263 O  O    . PHE   B 1 44  ? 1.517   -23.252 -32.406 1.00 24.98  ? 44  PHE   B O    1 
ATOM   1264 C  CB   . PHE   B 1 44  ? -0.195  -23.080 -29.541 1.00 22.00  ? 44  PHE   B CB   1 
ATOM   1265 C  CG   . PHE   B 1 44  ? -1.223  -22.655 -30.548 1.00 22.32  ? 44  PHE   B CG   1 
ATOM   1266 C  CD1  . PHE   B 1 44  ? -2.144  -23.567 -31.046 1.00 22.37  ? 44  PHE   B CD1  1 
ATOM   1267 C  CD2  . PHE   B 1 44  ? -1.296  -21.338 -30.973 1.00 20.02  ? 44  PHE   B CD2  1 
ATOM   1268 C  CE1  . PHE   B 1 44  ? -3.091  -23.172 -31.969 1.00 21.41  ? 44  PHE   B CE1  1 
ATOM   1269 C  CE2  . PHE   B 1 44  ? -2.249  -20.938 -31.890 1.00 23.55  ? 44  PHE   B CE2  1 
ATOM   1270 C  CZ   . PHE   B 1 44  ? -3.146  -21.867 -32.394 1.00 21.08  ? 44  PHE   B CZ   1 
ATOM   1271 N  N    . ALA   B 1 45  ? 2.489   -22.008 -30.812 1.00 20.79  ? 45  ALA   B N    1 
ATOM   1272 C  CA   . ALA   B 1 45  ? 3.115   -21.110 -31.766 1.00 20.82  ? 45  ALA   B CA   1 
ATOM   1273 C  C    . ALA   B 1 45  ? 4.188   -20.338 -31.019 1.00 21.79  ? 45  ALA   B C    1 
ATOM   1274 O  O    . ALA   B 1 45  ? 4.123   -20.202 -29.796 1.00 21.90  ? 45  ALA   B O    1 
ATOM   1275 C  CB   . ALA   B 1 45  ? 2.100   -20.145 -32.382 1.00 23.47  ? 45  ALA   B CB   1 
ATOM   1276 N  N    . SER   B 1 46  ? 5.174   -19.839 -31.757 1.00 20.61  ? 46  SER   B N    1 
ATOM   1277 C  CA   . SER   B 1 46  ? 6.205   -19.018 -31.130 1.00 17.73  ? 46  SER   B CA   1 
ATOM   1278 C  C    . SER   B 1 46  ? 6.874   -18.130 -32.166 1.00 19.49  ? 46  SER   B C    1 
ATOM   1279 O  O    . SER   B 1 46  ? 6.735   -18.320 -33.375 1.00 20.26  ? 46  SER   B O    1 
ATOM   1280 C  CB   . SER   B 1 46  ? 7.251   -19.852 -30.385 1.00 18.01  ? 46  SER   B CB   1 
ATOM   1281 O  OG   . SER   B 1 46  ? 7.954   -20.728 -31.276 1.00 18.18  ? 46  SER   B OG   1 
ATOM   1282 N  N    . GLY   B 1 47  ? 7.612   -17.150 -31.663 1.00 16.37  ? 47  GLY   B N    1 
ATOM   1283 C  CA   . GLY   B 1 47  ? 8.367   -16.254 -32.510 1.00 18.67  ? 47  GLY   B CA   1 
ATOM   1284 C  C    . GLY   B 1 47  ? 9.103   -15.248 -31.653 1.00 18.52  ? 47  GLY   B C    1 
ATOM   1285 O  O    . GLY   B 1 47  ? 9.145   -15.369 -30.424 1.00 18.42  ? 47  GLY   B O    1 
ATOM   1286 N  N    . LYS   B 1 48  ? 9.713   -14.270 -32.317 1.00 18.48  ? 48  LYS   B N    1 
ATOM   1287 C  CA   . LYS   B 1 48  ? 10.393  -13.173 -31.642 1.00 19.93  ? 48  LYS   B CA   1 
ATOM   1288 C  C    . LYS   B 1 48  ? 9.825   -11.865 -32.165 1.00 19.41  ? 48  LYS   B C    1 
ATOM   1289 O  O    . LYS   B 1 48  ? 9.542   -11.743 -33.361 1.00 20.64  ? 48  LYS   B O    1 
ATOM   1290 C  CB   . LYS   B 1 48  ? 11.911  -13.228 -31.860 1.00 22.69  ? 48  LYS   B CB   1 
ATOM   1291 C  CG   . LYS   B 1 48  ? 12.586  -14.406 -31.170 1.00 32.25  ? 48  LYS   B CG   1 
ATOM   1292 C  CD   . LYS   B 1 48  ? 14.091  -14.197 -31.058 1.00 38.03  ? 48  LYS   B CD   1 
ATOM   1293 C  CE   . LYS   B 1 48  ? 14.522  -13.987 -29.613 1.00 40.17  ? 48  LYS   B CE   1 
ATOM   1294 N  NZ   . LYS   B 1 48  ? 15.974  -13.664 -29.510 1.00 44.72  ? 48  LYS   B NZ   1 
ATOM   1295 N  N    . THR   B 1 49  ? 9.637   -10.890 -31.274 1.00 15.92  ? 49  THR   B N    1 
ATOM   1296 C  CA   . THR   B 1 49  ? 9.131   -9.600  -31.725 1.00 15.60  ? 49  THR   B CA   1 
ATOM   1297 C  C    . THR   B 1 49  ? 10.101  -8.971  -32.718 1.00 16.19  ? 49  THR   B C    1 
ATOM   1298 O  O    . THR   B 1 49  ? 11.320  -9.144  -32.637 1.00 17.32  ? 49  THR   B O    1 
ATOM   1299 C  CB   . THR   B 1 49  ? 8.954   -8.645  -30.545 1.00 15.92  ? 49  THR   B CB   1 
ATOM   1300 O  OG1  . THR   B 1 49  ? 10.199  -8.507  -29.850 1.00 15.34  ? 49  THR   B OG1  1 
ATOM   1301 C  CG2  . THR   B 1 49  ? 7.881   -9.169  -29.587 1.00 17.27  ? 49  THR   B CG2  1 
ATOM   1302 N  N    . SER   B 1 50  ? 9.539   -8.187  -33.626 1.00 16.18  ? 50  SER   B N    1 
ATOM   1303 C  CA   . SER   B 1 50  ? 10.284  -7.519  -34.677 1.00 19.53  ? 50  SER   B CA   1 
ATOM   1304 C  C    . SER   B 1 50  ? 10.865  -6.207  -34.162 1.00 23.19  ? 50  SER   B C    1 
ATOM   1305 O  O    . SER   B 1 50  ? 10.728  -5.845  -32.986 1.00 18.32  ? 50  SER   B O    1 
ATOM   1306 C  CB   . SER   B 1 50  ? 9.338   -7.203  -35.830 1.00 23.27  ? 50  SER   B CB   1 
ATOM   1307 O  OG   . SER   B 1 50  ? 8.393   -6.208  -35.438 1.00 22.51  ? 50  SER   B OG   1 
ATOM   1308 N  N    . GLU   B 1 51  ? 11.486  -5.455  -35.075 1.00 23.18  ? 51  GLU   B N    1 
ATOM   1309 C  CA   A GLU   B 1 51  ? 12.017  -4.143  -34.720 0.39 20.16  ? 51  GLU   B CA   1 
ATOM   1310 C  CA   B GLU   B 1 51  ? 12.017  -4.145  -34.718 0.61 20.04  ? 51  GLU   B CA   1 
ATOM   1311 C  C    . GLU   B 1 51  ? 10.924  -3.174  -34.288 1.00 19.82  ? 51  GLU   B C    1 
ATOM   1312 O  O    . GLU   B 1 51  ? 11.231  -2.150  -33.662 1.00 25.17  ? 51  GLU   B O    1 
ATOM   1313 C  CB   A GLU   B 1 51  ? 12.804  -3.549  -35.893 0.39 25.84  ? 51  GLU   B CB   1 
ATOM   1314 C  CB   B GLU   B 1 51  ? 12.819  -3.560  -35.886 0.61 25.86  ? 51  GLU   B CB   1 
ATOM   1315 C  CG   A GLU   B 1 51  ? 13.889  -4.460  -36.447 0.39 24.64  ? 51  GLU   B CG   1 
ATOM   1316 C  CG   B GLU   B 1 51  ? 12.020  -3.364  -37.158 0.61 30.61  ? 51  GLU   B CG   1 
ATOM   1317 C  CD   A GLU   B 1 51  ? 15.003  -4.743  -35.456 0.39 30.59  ? 51  GLU   B CD   1 
ATOM   1318 C  CD   B GLU   B 1 51  ? 12.846  -2.743  -38.269 0.61 40.01  ? 51  GLU   B CD   1 
ATOM   1319 O  OE1  A GLU   B 1 51  ? 15.595  -3.777  -34.927 0.39 28.64  ? 51  GLU   B OE1  1 
ATOM   1320 O  OE1  B GLU   B 1 51  ? 14.072  -2.588  -38.081 0.61 36.84  ? 51  GLU   B OE1  1 
ATOM   1321 O  OE2  A GLU   B 1 51  ? 15.289  -5.935  -35.207 0.39 36.10  ? 51  GLU   B OE2  1 
ATOM   1322 O  OE2  B GLU   B 1 51  ? 12.271  -2.409  -39.327 0.61 46.12  ? 51  GLU   B OE2  1 
ATOM   1323 N  N    . SER   B 1 52  ? 9.665   -3.461  -34.611 1.00 18.68  ? 52  SER   B N    1 
ATOM   1324 C  CA   . SER   B 1 52  ? 8.536   -2.650  -34.173 1.00 22.04  ? 52  SER   B CA   1 
ATOM   1325 C  C    . SER   B 1 52  ? 7.936   -3.165  -32.875 1.00 19.90  ? 52  SER   B C    1 
ATOM   1326 O  O    . SER   B 1 52  ? 6.917   -2.633  -32.416 1.00 21.37  ? 52  SER   B O    1 
ATOM   1327 C  CB   . SER   B 1 52  ? 7.450   -2.608  -35.255 1.00 23.70  ? 52  SER   B CB   1 
ATOM   1328 O  OG   . SER   B 1 52  ? 6.777   -3.851  -35.374 1.00 25.18  ? 52  SER   B OG   1 
ATOM   1329 N  N    . GLY   B 1 53  ? 8.542   -4.190  -32.278 1.00 16.96  ? 53  GLY   B N    1 
ATOM   1330 C  CA   . GLY   B 1 53  ? 7.993   -4.785  -31.074 1.00 17.22  ? 53  GLY   B CA   1 
ATOM   1331 C  C    . GLY   B 1 53  ? 6.820   -5.705  -31.305 1.00 19.65  ? 53  GLY   B C    1 
ATOM   1332 O  O    . GLY   B 1 53  ? 6.191   -6.138  -30.336 1.00 17.99  ? 53  GLY   B O    1 
ATOM   1333 N  N    . GLU   B 1 54  ? 6.507   -6.033  -32.556 1.00 18.86  ? 54  GLU   B N    1 
ATOM   1334 C  CA   . GLU   B 1 54  ? 5.308   -6.780  -32.880 1.00 18.57  ? 54  GLU   B CA   1 
ATOM   1335 C  C    . GLU   B 1 54  ? 5.652   -8.181  -33.357 1.00 17.34  ? 54  GLU   B C    1 
ATOM   1336 O  O    . GLU   B 1 54  ? 6.719   -8.434  -33.930 1.00 20.80  ? 54  GLU   B O    1 
ATOM   1337 C  CB   . GLU   B 1 54  ? 4.474   -6.060  -33.950 1.00 22.41  ? 54  GLU   B CB   1 
ATOM   1338 C  CG   . GLU   B 1 54  ? 4.070   -4.648  -33.540 1.00 25.18  ? 54  GLU   B CG   1 
ATOM   1339 C  CD   . GLU   B 1 54  ? 3.272   -3.919  -34.605 1.00 36.69  ? 54  GLU   B CD   1 
ATOM   1340 O  OE1  . GLU   B 1 54  ? 3.032   -4.501  -35.684 1.00 38.09  ? 54  GLU   B OE1  1 
ATOM   1341 O  OE2  . GLU   B 1 54  ? 2.881   -2.757  -34.357 1.00 39.34  ? 54  GLU   B OE2  1 
ATOM   1342 N  N    . LEU   B 1 55  ? 4.738   -9.093  -33.104 1.00 17.63  ? 55  LEU   B N    1 
ATOM   1343 C  CA   . LEU   B 1 55  ? 4.879   -10.467 -33.559 1.00 17.97  ? 55  LEU   B CA   1 
ATOM   1344 C  C    . LEU   B 1 55  ? 3.580   -10.825 -34.261 1.00 21.11  ? 55  LEU   B C    1 
ATOM   1345 O  O    . LEU   B 1 55  ? 2.532   -10.952 -33.616 1.00 21.22  ? 55  LEU   B O    1 
ATOM   1346 C  CB   . LEU   B 1 55  ? 5.171   -11.403 -32.386 1.00 18.69  ? 55  LEU   B CB   1 
ATOM   1347 C  CG   . LEU   B 1 55  ? 5.227   -12.890 -32.708 1.00 20.26  ? 55  LEU   B CG   1 
ATOM   1348 C  CD1  . LEU   B 1 55  ? 6.188   -13.176 -33.856 1.00 24.98  ? 55  LEU   B CD1  1 
ATOM   1349 C  CD2  . LEU   B 1 55  ? 5.641   -13.640 -31.458 1.00 23.15  ? 55  LEU   B CD2  1 
ATOM   1350 N  N    A HIS   B 1 56  ? 3.657   -10.958 -35.581 0.75 24.13  ? 56  HIS   B N    1 
ATOM   1351 N  N    B HIS   B 1 56  ? 3.634   -10.961 -35.583 0.25 24.22  ? 56  HIS   B N    1 
ATOM   1352 C  CA   A HIS   B 1 56  ? 2.548   -11.329 -36.440 0.75 26.51  ? 56  HIS   B CA   1 
ATOM   1353 C  CA   B HIS   B 1 56  ? 2.469   -11.337 -36.367 0.25 26.49  ? 56  HIS   B CA   1 
ATOM   1354 C  C    A HIS   B 1 56  ? 2.749   -12.762 -36.906 0.75 24.09  ? 56  HIS   B C    1 
ATOM   1355 C  C    B HIS   B 1 56  ? 2.750   -12.620 -37.136 0.25 25.16  ? 56  HIS   B C    1 
ATOM   1356 O  O    A HIS   B 1 56  ? 3.840   -13.328 -36.783 0.75 22.92  ? 56  HIS   B O    1 
ATOM   1357 O  O    B HIS   B 1 56  ? 3.903   -12.946 -37.438 0.25 26.27  ? 56  HIS   B O    1 
ATOM   1358 C  CB   A HIS   B 1 56  ? 2.493   -10.418 -37.676 0.75 26.80  ? 56  HIS   B CB   1 
ATOM   1359 C  CB   B HIS   B 1 56  ? 2.002   -10.212 -37.313 0.25 30.27  ? 56  HIS   B CB   1 
ATOM   1360 C  CG   A HIS   B 1 56  ? 2.303   -8.968  -37.356 0.75 25.43  ? 56  HIS   B CG   1 
ATOM   1361 C  CG   B HIS   B 1 56  ? 2.946   -9.918  -38.439 0.25 28.17  ? 56  HIS   B CG   1 
ATOM   1362 N  ND1  A HIS   B 1 56  ? 1.059   -8.380  -37.285 0.75 31.46  ? 56  HIS   B ND1  1 
ATOM   1363 N  ND1  B HIS   B 1 56  ? 3.682   -8.755  -38.508 0.25 26.42  ? 56  HIS   B ND1  1 
ATOM   1364 C  CD2  A HIS   B 1 56  ? 3.198   -7.987  -37.094 0.75 31.29  ? 56  HIS   B CD2  1 
ATOM   1365 C  CD2  B HIS   B 1 56  ? 3.252   -10.622 -39.555 0.25 30.06  ? 56  HIS   B CD2  1 
ATOM   1366 C  CE1  A HIS   B 1 56  ? 1.196   -7.099  -36.989 0.75 28.96  ? 56  HIS   B CE1  1 
ATOM   1367 C  CE1  B HIS   B 1 56  ? 4.408   -8.761  -39.611 0.25 34.98  ? 56  HIS   B CE1  1 
ATOM   1368 N  NE2  A HIS   B 1 56  ? 2.484   -6.835  -36.867 0.75 30.62  ? 56  HIS   B NE2  1 
ATOM   1369 N  NE2  B HIS   B 1 56  ? 4.169   -9.885  -40.262 0.25 31.60  ? 56  HIS   B NE2  1 
ATOM   1370 N  N    . GLY   B 1 57  ? 1.681   -13.344 -37.447 1.00 27.68  ? 57  GLY   B N    1 
ATOM   1371 C  CA   . GLY   B 1 57  ? 1.792   -14.634 -38.094 1.00 28.38  ? 57  GLY   B CA   1 
ATOM   1372 C  C    . GLY   B 1 57  ? 1.912   -15.814 -37.163 1.00 29.30  ? 57  GLY   B C    1 
ATOM   1373 O  O    . GLY   B 1 57  ? 2.352   -16.886 -37.596 1.00 29.29  ? 57  GLY   B O    1 
ATOM   1374 N  N    . LEU   B 1 58  ? 1.526   -15.662 -35.895 1.00 21.77  ? 58  LEU   B N    1 
ATOM   1375 C  CA   . LEU   B 1 58  ? 1.606   -16.782 -34.969 1.00 24.80  ? 58  LEU   B CA   1 
ATOM   1376 C  C    . LEU   B 1 58  ? 0.682   -17.915 -35.387 1.00 24.22  ? 58  LEU   B C    1 
ATOM   1377 O  O    . LEU   B 1 58  ? 1.057   -19.087 -35.302 1.00 23.09  ? 58  LEU   B O    1 
ATOM   1378 C  CB   . LEU   B 1 58  ? 1.292   -16.317 -33.546 1.00 21.39  ? 58  LEU   B CB   1 
ATOM   1379 C  CG   . LEU   B 1 58  ? 2.454   -15.615 -32.848 1.00 23.94  ? 58  LEU   B CG   1 
ATOM   1380 C  CD1  . LEU   B 1 58  ? 1.939   -14.849 -31.633 1.00 24.16  ? 58  LEU   B CD1  1 
ATOM   1381 C  CD2  . LEU   B 1 58  ? 3.519   -16.619 -32.438 1.00 24.07  ? 58  LEU   B CD2  1 
ATOM   1382 N  N    . THR   B 1 59  ? -0.523  -17.590 -35.849 1.00 22.95  ? 59  THR   B N    1 
ATOM   1383 C  CA   . THR   B 1 59  ? -1.503  -18.628 -36.135 1.00 20.99  ? 59  THR   B CA   1 
ATOM   1384 C  C    . THR   B 1 59  ? -2.419  -18.178 -37.268 1.00 23.41  ? 59  THR   B C    1 
ATOM   1385 O  O    . THR   B 1 59  ? -2.281  -17.083 -37.819 1.00 26.65  ? 59  THR   B O    1 
ATOM   1386 C  CB   . THR   B 1 59  ? -2.245  -19.040 -34.852 1.00 22.50  ? 59  THR   B CB   1 
ATOM   1387 O  OG1  . THR   B 1 59  ? -3.069  -20.189 -35.107 1.00 23.63  ? 59  THR   B OG1  1 
ATOM   1388 C  CG2  . THR   B 1 59  ? -3.110  -17.896 -34.319 1.00 18.97  ? 59  THR   B CG2  1 
ATOM   1389 N  N    . THR   B 1 60  ? -3.349  -19.054 -37.632 1.00 24.25  ? 60  THR   B N    1 
ATOM   1390 C  CA   . THR   B 1 60  ? -4.329  -18.780 -38.665 1.00 22.68  ? 60  THR   B CA   1 
ATOM   1391 C  C    . THR   B 1 60  ? -5.717  -18.866 -38.057 1.00 20.30  ? 60  THR   B C    1 
ATOM   1392 O  O    . THR   B 1 60  ? -5.911  -19.457 -36.990 1.00 20.58  ? 60  THR   B O    1 
ATOM   1393 C  CB   . THR   B 1 60  ? -4.219  -19.794 -39.812 1.00 23.43  ? 60  THR   B CB   1 
ATOM   1394 O  OG1  . THR   B 1 60  ? -4.408  -21.122 -39.300 1.00 27.41  ? 60  THR   B OG1  1 
ATOM   1395 C  CG2  . THR   B 1 60  ? -2.842  -19.681 -40.473 1.00 25.95  ? 60  THR   B CG2  1 
ATOM   1396 N  N    . GLU   B 1 61  ? -6.681  -18.255 -38.750 1.00 22.74  ? 61  GLU   B N    1 
ATOM   1397 C  CA   . GLU   B 1 61  ? -8.072  -18.362 -38.329 1.00 24.51  ? 61  GLU   B CA   1 
ATOM   1398 C  C    . GLU   B 1 61  ? -8.488  -19.820 -38.204 1.00 23.35  ? 61  GLU   B C    1 
ATOM   1399 O  O    . GLU   B 1 61  ? -9.203  -20.198 -37.268 1.00 23.70  ? 61  GLU   B O    1 
ATOM   1400 C  CB   . GLU   B 1 61  ? -8.964  -17.637 -39.338 1.00 28.57  ? 61  GLU   B CB   1 
ATOM   1401 C  CG   . GLU   B 1 61  ? -10.400 -17.482 -38.893 1.00 49.29  ? 61  GLU   B CG   1 
ATOM   1402 C  CD   . GLU   B 1 61  ? -10.511 -16.785 -37.556 1.00 63.83  ? 61  GLU   B CD   1 
ATOM   1403 O  OE1  . GLU   B 1 61  ? -10.334 -15.549 -37.507 1.00 70.11  ? 61  GLU   B OE1  1 
ATOM   1404 O  OE2  . GLU   B 1 61  ? -10.762 -17.476 -36.550 1.00 71.06  ? 61  GLU   B OE2  1 
ATOM   1405 N  N    . GLU   B 1 62  ? -8.020  -20.662 -39.127 1.00 22.51  ? 62  GLU   B N    1 
ATOM   1406 C  CA   . GLU   B 1 62  ? -8.412  -22.063 -39.127 1.00 20.51  ? 62  GLU   B CA   1 
ATOM   1407 C  C    . GLU   B 1 62  ? -7.988  -22.763 -37.840 1.00 19.23  ? 62  GLU   B C    1 
ATOM   1408 O  O    . GLU   B 1 62  ? -8.777  -23.501 -37.237 1.00 23.21  ? 62  GLU   B O    1 
ATOM   1409 C  CB   . GLU   B 1 62  ? -7.800  -22.745 -40.348 1.00 25.68  ? 62  GLU   B CB   1 
ATOM   1410 C  CG   . GLU   B 1 62  ? -8.142  -24.206 -40.491 1.00 29.52  ? 62  GLU   B CG   1 
ATOM   1411 C  CD   . GLU   B 1 62  ? -7.446  -24.841 -41.676 1.00 41.26  ? 62  GLU   B CD   1 
ATOM   1412 O  OE1  . GLU   B 1 62  ? -6.460  -25.576 -41.460 1.00 43.10  ? 62  GLU   B OE1  1 
ATOM   1413 O  OE2  . GLU   B 1 62  ? -7.878  -24.597 -42.822 1.00 43.01  ? 62  GLU   B OE2  1 
ATOM   1414 N  N    . GLU   B 1 63  ? -6.751  -22.532 -37.391 1.00 19.52  ? 63  GLU   B N    1 
ATOM   1415 C  CA   . GLU   B 1 63  ? -6.204  -23.264 -36.255 1.00 21.28  ? 63  GLU   B CA   1 
ATOM   1416 C  C    . GLU   B 1 63  ? -6.527  -22.634 -34.907 1.00 19.09  ? 63  GLU   B C    1 
ATOM   1417 O  O    . GLU   B 1 63  ? -6.488  -23.330 -33.887 1.00 21.06  ? 63  GLU   B O    1 
ATOM   1418 C  CB   . GLU   B 1 63  ? -4.678  -23.378 -36.374 1.00 22.97  ? 63  GLU   B CB   1 
ATOM   1419 C  CG   . GLU   B 1 63  ? -4.207  -24.380 -37.425 1.00 34.49  ? 63  GLU   B CG   1 
ATOM   1420 C  CD   . GLU   B 1 63  ? -4.625  -25.809 -37.105 1.00 47.90  ? 63  GLU   B CD   1 
ATOM   1421 O  OE1  . GLU   B 1 63  ? -4.782  -26.611 -38.051 1.00 51.34  ? 63  GLU   B OE1  1 
ATOM   1422 O  OE2  . GLU   B 1 63  ? -4.798  -26.133 -35.911 1.00 52.02  ? 63  GLU   B OE2  1 
ATOM   1423 N  N    . PHE   B 1 64  ? -6.858  -21.346 -34.879 1.00 18.02  ? 64  PHE   B N    1 
ATOM   1424 C  CA   . PHE   B 1 64  ? -7.067  -20.625 -33.618 1.00 20.67  ? 64  PHE   B CA   1 
ATOM   1425 C  C    . PHE   B 1 64  ? -8.519  -20.790 -33.168 1.00 17.09  ? 64  PHE   B C    1 
ATOM   1426 O  O    . PHE   B 1 64  ? -9.331  -19.857 -33.167 1.00 19.82  ? 64  PHE   B O    1 
ATOM   1427 C  CB   . PHE   B 1 64  ? -6.681  -19.161 -33.786 1.00 17.94  ? 64  PHE   B CB   1 
ATOM   1428 C  CG   . PHE   B 1 64  ? -6.658  -18.368 -32.497 1.00 17.03  ? 64  PHE   B CG   1 
ATOM   1429 C  CD1  . PHE   B 1 64  ? -5.802  -18.713 -31.467 1.00 19.39  ? 64  PHE   B CD1  1 
ATOM   1430 C  CD2  . PHE   B 1 64  ? -7.462  -17.250 -32.351 1.00 22.34  ? 64  PHE   B CD2  1 
ATOM   1431 C  CE1  . PHE   B 1 64  ? -5.763  -17.964 -30.288 1.00 20.35  ? 64  PHE   B CE1  1 
ATOM   1432 C  CE2  . PHE   B 1 64  ? -7.427  -16.497 -31.173 1.00 21.14  ? 64  PHE   B CE2  1 
ATOM   1433 C  CZ   . PHE   B 1 64  ? -6.574  -16.859 -30.155 1.00 19.09  ? 64  PHE   B CZ   1 
ATOM   1434 N  N    . VAL   B 1 65  ? -8.835  -22.017 -32.758 1.00 18.00  ? 65  VAL   B N    1 
ATOM   1435 C  CA   . VAL   B 1 65  ? -10.190 -22.364 -32.341 1.00 15.82  ? 65  VAL   B CA   1 
ATOM   1436 C  C    . VAL   B 1 65  ? -10.420 -21.935 -30.900 1.00 17.71  ? 65  VAL   B C    1 
ATOM   1437 O  O    . VAL   B 1 65  ? -9.478  -21.564 -30.190 1.00 18.73  ? 65  VAL   B O    1 
ATOM   1438 C  CB   . VAL   B 1 65  ? -10.477 -23.867 -32.513 1.00 16.06  ? 65  VAL   B CB   1 
ATOM   1439 C  CG1  . VAL   B 1 65  ? -10.266 -24.275 -33.964 1.00 19.38  ? 65  VAL   B CG1  1 
ATOM   1440 C  CG2  . VAL   B 1 65  ? -9.613  -24.698 -31.571 1.00 18.32  ? 65  VAL   B CG2  1 
ATOM   1441 N  N    . GLU   B 1 66  ? -11.667 -22.004 -30.452 1.00 18.31  ? 66  GLU   B N    1 
ATOM   1442 C  CA   . GLU   B 1 66  ? -11.963 -21.684 -29.064 1.00 19.24  ? 66  GLU   B CA   1 
ATOM   1443 C  C    . GLU   B 1 66  ? -11.167 -22.590 -28.134 1.00 19.01  ? 66  GLU   B C    1 
ATOM   1444 O  O    . GLU   B 1 66  ? -10.910 -23.760 -28.435 1.00 19.94  ? 66  GLU   B O    1 
ATOM   1445 C  CB   . GLU   B 1 66  ? -13.468 -21.805 -28.798 1.00 21.59  ? 66  GLU   B CB   1 
ATOM   1446 C  CG   . GLU   B 1 66  ? -14.280 -20.798 -29.618 1.00 23.73  ? 66  GLU   B CG   1 
ATOM   1447 C  CD   . GLU   B 1 66  ? -15.765 -20.771 -29.278 1.00 34.74  ? 66  GLU   B CD   1 
ATOM   1448 O  OE1  . GLU   B 1 66  ? -16.448 -21.803 -29.447 1.00 24.86  ? 66  GLU   B OE1  1 
ATOM   1449 O  OE2  . GLU   B 1 66  ? -16.253 -19.703 -28.839 1.00 36.13  ? 66  GLU   B OE2  1 
ATOM   1450 N  N    . GLY   B 1 67  ? -10.740 -22.029 -27.017 1.00 18.34  ? 67  GLY   B N    1 
ATOM   1451 C  CA   . GLY   B 1 67  ? -9.924  -22.757 -26.066 1.00 18.24  ? 67  GLY   B CA   1 
ATOM   1452 C  C    . GLY   B 1 67  ? -9.232  -21.768 -25.155 1.00 16.59  ? 67  GLY   B C    1 
ATOM   1453 O  O    . GLY   B 1 67  ? -9.364  -20.561 -25.314 1.00 16.94  ? 67  GLY   B O    1 
ATOM   1454 N  N    . ILE   B 1 68  ? -8.471  -22.310 -24.209 1.00 17.10  ? 68  ILE   B N    1 
ATOM   1455 C  CA   . ILE   B 1 68  ? -7.679  -21.499 -23.286 1.00 17.58  ? 68  ILE   B CA   1 
ATOM   1456 C  C    . ILE   B 1 68  ? -6.246  -21.443 -23.792 1.00 15.89  ? 68  ILE   B C    1 
ATOM   1457 O  O    . ILE   B 1 68  ? -5.622  -22.484 -24.033 1.00 18.51  ? 68  ILE   B O    1 
ATOM   1458 C  CB   . ILE   B 1 68  ? -7.746  -22.051 -21.853 1.00 17.31  ? 68  ILE   B CB   1 
ATOM   1459 C  CG1  . ILE   B 1 68  ? -9.193  -22.027 -21.355 1.00 19.14  ? 68  ILE   B CG1  1 
ATOM   1460 C  CG2  . ILE   B 1 68  ? -6.848  -21.222 -20.944 1.00 18.70  ? 68  ILE   B CG2  1 
ATOM   1461 C  CD1  . ILE   B 1 68  ? -9.397  -22.647 -19.967 1.00 23.58  ? 68  ILE   B CD1  1 
ATOM   1462 N  N    . TYR   B 1 69  ? -5.714  -20.230 -23.931 1.00 15.59  ? 69  TYR   B N    1 
ATOM   1463 C  CA   . TYR   B 1 69  ? -4.377  -20.016 -24.450 1.00 16.06  ? 69  TYR   B CA   1 
ATOM   1464 C  C    . TYR   B 1 69  ? -3.532  -19.297 -23.414 1.00 17.22  ? 69  TYR   B C    1 
ATOM   1465 O  O    . TYR   B 1 69  ? -4.043  -18.504 -22.618 1.00 17.11  ? 69  TYR   B O    1 
ATOM   1466 C  CB   . TYR   B 1 69  ? -4.413  -19.189 -25.746 1.00 16.02  ? 69  TYR   B CB   1 
ATOM   1467 C  CG   . TYR   B 1 69  ? -5.064  -19.922 -26.900 1.00 17.26  ? 69  TYR   B CG   1 
ATOM   1468 C  CD1  . TYR   B 1 69  ? -6.445  -19.938 -27.045 1.00 16.42  ? 69  TYR   B CD1  1 
ATOM   1469 C  CD2  . TYR   B 1 69  ? -4.290  -20.605 -27.837 1.00 19.24  ? 69  TYR   B CD2  1 
ATOM   1470 C  CE1  . TYR   B 1 69  ? -7.048  -20.629 -28.101 1.00 16.64  ? 69  TYR   B CE1  1 
ATOM   1471 C  CE2  . TYR   B 1 69  ? -4.879  -21.282 -28.900 1.00 18.50  ? 69  TYR   B CE2  1 
ATOM   1472 C  CZ   . TYR   B 1 69  ? -6.253  -21.285 -29.024 1.00 19.59  ? 69  TYR   B CZ   1 
ATOM   1473 O  OH   . TYR   B 1 69  ? -6.823  -21.961 -30.091 1.00 18.79  ? 69  TYR   B OH   1 
ATOM   1474 N  N    . LYS   B 1 70  ? -2.232  -19.580 -23.435 1.00 16.53  ? 70  LYS   B N    1 
ATOM   1475 C  CA   . LYS   B 1 70  ? -1.256  -18.876 -22.612 1.00 16.38  ? 70  LYS   B CA   1 
ATOM   1476 C  C    . LYS   B 1 70  ? -0.186  -18.296 -23.521 1.00 16.21  ? 70  LYS   B C    1 
ATOM   1477 O  O    . LYS   B 1 70  ? 0.408   -19.023 -24.327 1.00 18.11  ? 70  LYS   B O    1 
ATOM   1478 C  CB   . LYS   B 1 70  ? -0.619  -19.825 -21.595 1.00 15.65  ? 70  LYS   B CB   1 
ATOM   1479 C  CG   . LYS   B 1 70  ? 0.581   -19.219 -20.862 1.00 18.47  ? 70  LYS   B CG   1 
ATOM   1480 C  CD   . LYS   B 1 70  ? 0.996   -20.054 -19.659 1.00 24.83  ? 70  LYS   B CD   1 
ATOM   1481 C  CE   . LYS   B 1 70  ? 1.565   -21.394 -20.070 1.00 31.26  ? 70  LYS   B CE   1 
ATOM   1482 N  NZ   . LYS   B 1 70  ? 2.184   -22.095 -18.903 1.00 36.97  ? 70  LYS   B NZ   1 
ATOM   1483 N  N    . VAL   B 1 71  ? 0.046   -16.987 -23.405 1.00 15.30  ? 71  VAL   B N    1 
ATOM   1484 C  CA   . VAL   B 1 71  ? 1.121   -16.304 -24.110 1.00 15.12  ? 71  VAL   B CA   1 
ATOM   1485 C  C    . VAL   B 1 71  ? 2.206   -15.998 -23.090 1.00 15.31  ? 71  VAL   B C    1 
ATOM   1486 O  O    . VAL   B 1 71  ? 1.979   -15.226 -22.150 1.00 17.53  ? 71  VAL   B O    1 
ATOM   1487 C  CB   . VAL   B 1 71  ? 0.630   -15.002 -24.767 1.00 15.20  ? 71  VAL   B CB   1 
ATOM   1488 C  CG1  . VAL   B 1 71  ? 1.785   -14.269 -25.417 1.00 17.87  ? 71  VAL   B CG1  1 
ATOM   1489 C  CG2  . VAL   B 1 71  ? -0.494  -15.289 -25.780 1.00 17.15  ? 71  VAL   B CG2  1 
ATOM   1490 N  N    . GLU   B 1 72  ? 3.383   -16.600 -23.270 1.00 15.10  ? 72  GLU   B N    1 
ATOM   1491 C  CA   . GLU   B 1 72  ? 4.515   -16.384 -22.376 1.00 14.09  ? 72  GLU   B CA   1 
ATOM   1492 C  C    . GLU   B 1 72  ? 5.506   -15.470 -23.080 1.00 14.33  ? 72  GLU   B C    1 
ATOM   1493 O  O    . GLU   B 1 72  ? 5.965   -15.769 -24.189 1.00 16.65  ? 72  GLU   B O    1 
ATOM   1494 C  CB   . GLU   B 1 72  ? 5.178   -17.713 -22.009 1.00 17.73  ? 72  GLU   B CB   1 
ATOM   1495 C  CG   . GLU   B 1 72  ? 4.377   -18.554 -21.044 1.00 28.05  ? 72  GLU   B CG   1 
ATOM   1496 C  CD   . GLU   B 1 72  ? 5.218   -19.608 -20.340 1.00 30.95  ? 72  GLU   B CD   1 
ATOM   1497 O  OE1  . GLU   B 1 72  ? 6.416   -19.753 -20.677 1.00 32.43  ? 72  GLU   B OE1  1 
ATOM   1498 O  OE2  . GLU   B 1 72  ? 4.673   -20.288 -19.445 1.00 31.19  ? 72  GLU   B OE2  1 
ATOM   1499 N  N    . ILE   B 1 73  ? 5.825   -14.344 -22.454 1.00 13.57  ? 73  ILE   B N    1 
ATOM   1500 C  CA   . ILE   B 1 73  ? 6.741   -13.370 -23.020 1.00 13.94  ? 73  ILE   B CA   1 
ATOM   1501 C  C    . ILE   B 1 73  ? 8.020   -13.482 -22.213 1.00 14.38  ? 73  ILE   B C    1 
ATOM   1502 O  O    . ILE   B 1 73  ? 8.001   -13.331 -20.982 1.00 14.30  ? 73  ILE   B O    1 
ATOM   1503 C  CB   . ILE   B 1 73  ? 6.136   -11.965 -22.954 1.00 14.17  ? 73  ILE   B CB   1 
ATOM   1504 C  CG1  . ILE   B 1 73  ? 4.777   -11.966 -23.666 1.00 15.77  ? 73  ILE   B CG1  1 
ATOM   1505 C  CG2  . ILE   B 1 73  ? 7.103   -10.942 -23.504 1.00 16.95  ? 73  ILE   B CG2  1 
ATOM   1506 C  CD1  . ILE   B 1 73  ? 4.039   -10.642 -23.557 1.00 17.03  ? 73  ILE   B CD1  1 
ATOM   1507 N  N    A ASP   B 1 74  ? 9.134   -13.772 -22.880 0.74 13.65  ? 74  ASP   B N    1 
ATOM   1508 N  N    B ASP   B 1 74  ? 9.124   -13.768 -22.903 0.26 13.80  ? 74  ASP   B N    1 
ATOM   1509 C  CA   A ASP   B 1 74  ? 10.364  -14.105 -22.162 0.74 14.91  ? 74  ASP   B CA   1 
ATOM   1510 C  CA   B ASP   B 1 74  ? 10.415  -14.041 -22.278 0.26 15.09  ? 74  ASP   B CA   1 
ATOM   1511 C  C    A ASP   B 1 74  ? 11.131  -12.833 -21.783 0.74 13.46  ? 74  ASP   B C    1 
ATOM   1512 C  C    B ASP   B 1 74  ? 11.061  -12.714 -21.884 0.26 13.46  ? 74  ASP   B C    1 
ATOM   1513 O  O    A ASP   B 1 74  ? 12.176  -12.485 -22.336 0.74 13.42  ? 74  ASP   B O    1 
ATOM   1514 O  O    B ASP   B 1 74  ? 11.973  -12.199 -22.536 0.26 16.46  ? 74  ASP   B O    1 
ATOM   1515 C  CB   A ASP   B 1 74  ? 11.168  -15.128 -22.951 0.74 19.35  ? 74  ASP   B CB   1 
ATOM   1516 C  CB   B ASP   B 1 74  ? 11.281  -14.841 -23.243 0.26 17.24  ? 74  ASP   B CB   1 
ATOM   1517 C  CG   A ASP   B 1 74  ? 10.392  -16.428 -23.140 0.74 21.69  ? 74  ASP   B CG   1 
ATOM   1518 C  CG   B ASP   B 1 74  ? 12.704  -14.985 -22.773 0.26 22.14  ? 74  ASP   B CG   1 
ATOM   1519 O  OD1  A ASP   B 1 74  ? 9.556   -16.742 -22.266 0.74 20.83  ? 74  ASP   B OD1  1 
ATOM   1520 O  OD1  B ASP   B 1 74  ? 12.943  -14.991 -21.547 0.26 19.18  ? 74  ASP   B OD1  1 
ATOM   1521 O  OD2  A ASP   B 1 74  ? 10.587  -17.116 -24.160 0.74 26.37  ? 74  ASP   B OD2  1 
ATOM   1522 O  OD2  B ASP   B 1 74  ? 13.589  -15.077 -23.645 0.26 31.01  ? 74  ASP   B OD2  1 
ATOM   1523 N  N    . THR   B 1 75  ? 10.575  -12.152 -20.775 1.00 14.14  ? 75  THR   B N    1 
ATOM   1524 C  CA   . THR   B 1 75  ? 11.081  -10.849 -20.345 1.00 13.56  ? 75  THR   B CA   1 
ATOM   1525 C  C    . THR   B 1 75  ? 12.429  -10.940 -19.642 1.00 12.89  ? 75  THR   B C    1 
ATOM   1526 O  O    . THR   B 1 75  ? 13.245  -10.016 -19.769 1.00 13.91  ? 75  THR   B O    1 
ATOM   1527 C  CB   . THR   B 1 75  ? 10.061  -10.177 -19.428 1.00 14.51  ? 75  THR   B CB   1 
ATOM   1528 O  OG1  . THR   B 1 75  ? 9.841   -11.002 -18.275 1.00 14.23  ? 75  THR   B OG1  1 
ATOM   1529 C  CG2  . THR   B 1 75  ? 8.748   -9.985  -20.160 1.00 16.29  ? 75  THR   B CG2  1 
ATOM   1530 N  N    . LYS   B 1 76  ? 12.693  -12.032 -18.913 1.00 13.10  ? 76  LYS   B N    1 
ATOM   1531 C  CA   . LYS   B 1 76  ? 13.952  -12.112 -18.179 1.00 15.69  ? 76  LYS   B CA   1 
ATOM   1532 C  C    . LYS   B 1 76  ? 15.141  -12.054 -19.126 1.00 14.13  ? 76  LYS   B C    1 
ATOM   1533 O  O    . LYS   B 1 76  ? 16.103  -11.317 -18.889 1.00 15.06  ? 76  LYS   B O    1 
ATOM   1534 C  CB   . LYS   B 1 76  ? 13.997  -13.377 -17.316 1.00 19.38  ? 76  LYS   B CB   1 
ATOM   1535 C  CG   . LYS   B 1 76  ? 15.168  -13.380 -16.338 1.00 19.55  ? 76  LYS   B CG   1 
ATOM   1536 C  CD   . LYS   B 1 76  ? 15.102  -14.554 -15.362 1.00 24.03  ? 76  LYS   B CD   1 
ATOM   1537 C  CE   . LYS   B 1 76  ? 16.165  -14.426 -14.284 1.00 32.09  ? 76  LYS   B CE   1 
ATOM   1538 N  NZ   . LYS   B 1 76  ? 16.131  -15.586 -13.346 1.00 33.43  ? 76  LYS   B NZ   1 
ATOM   1539 N  N    A SER   B 1 77  ? 15.090  -12.825 -20.212 0.76 16.40  ? 77  SER   B N    1 
ATOM   1540 N  N    B SER   B 1 77  ? 15.096  -12.829 -20.213 0.24 16.42  ? 77  SER   B N    1 
ATOM   1541 C  CA   A SER   B 1 77  ? 16.195  -12.808 -21.164 0.76 16.97  ? 77  SER   B CA   1 
ATOM   1542 C  CA   B SER   B 1 77  ? 16.201  -12.806 -21.167 0.24 17.13  ? 77  SER   B CA   1 
ATOM   1543 C  C    A SER   B 1 77  ? 16.318  -11.457 -21.864 0.76 15.29  ? 77  SER   B C    1 
ATOM   1544 C  C    B SER   B 1 77  ? 16.319  -11.456 -21.864 0.24 15.43  ? 77  SER   B C    1 
ATOM   1545 O  O    A SER   B 1 77  ? 17.432  -11.020 -22.180 0.76 20.24  ? 77  SER   B O    1 
ATOM   1546 O  O    B SER   B 1 77  ? 17.428  -11.033 -22.210 0.24 20.25  ? 77  SER   B O    1 
ATOM   1547 C  CB   A SER   B 1 77  ? 16.031  -13.942 -22.176 0.76 23.25  ? 77  SER   B CB   1 
ATOM   1548 C  CB   B SER   B 1 77  ? 16.041  -13.922 -22.198 0.24 23.24  ? 77  SER   B CB   1 
ATOM   1549 O  OG   A SER   B 1 77  ? 16.108  -15.195 -21.515 0.76 22.95  ? 77  SER   B OG   1 
ATOM   1550 O  OG   B SER   B 1 77  ? 16.992  -13.791 -23.241 0.24 27.33  ? 77  SER   B OG   1 
ATOM   1551 N  N    . TYR   B 1 78  ? 15.195  -10.768 -22.075 1.00 15.14  ? 78  TYR   B N    1 
ATOM   1552 C  CA   . TYR   B 1 78  ? 15.240  -9.441  -22.679 1.00 17.01  ? 78  TYR   B CA   1 
ATOM   1553 C  C    . TYR   B 1 78  ? 16.028  -8.469  -21.806 1.00 15.11  ? 78  TYR   B C    1 
ATOM   1554 O  O    . TYR   B 1 78  ? 16.932  -7.774  -22.289 1.00 17.62  ? 78  TYR   B O    1 
ATOM   1555 C  CB   . TYR   B 1 78  ? 13.815  -8.931  -22.899 1.00 15.82  ? 78  TYR   B CB   1 
ATOM   1556 C  CG   . TYR   B 1 78  ? 13.761  -7.506  -23.396 1.00 15.73  ? 78  TYR   B CG   1 
ATOM   1557 C  CD1  . TYR   B 1 78  ? 13.998  -7.222  -24.734 1.00 17.16  ? 78  TYR   B CD1  1 
ATOM   1558 C  CD2  . TYR   B 1 78  ? 13.485  -6.450  -22.533 1.00 13.00  ? 78  TYR   B CD2  1 
ATOM   1559 C  CE1  . TYR   B 1 78  ? 13.950  -5.936  -25.199 1.00 17.29  ? 78  TYR   B CE1  1 
ATOM   1560 C  CE2  . TYR   B 1 78  ? 13.444  -5.146  -22.990 1.00 14.70  ? 78  TYR   B CE2  1 
ATOM   1561 C  CZ   . TYR   B 1 78  ? 13.683  -4.900  -24.324 1.00 15.99  ? 78  TYR   B CZ   1 
ATOM   1562 O  OH   . TYR   B 1 78  ? 13.644  -3.615  -24.814 1.00 18.64  ? 78  TYR   B OH   1 
ATOM   1563 N  N    . TRP   B 1 79  ? 15.687  -8.397  -20.513 1.00 13.00  ? 79  TRP   B N    1 
ATOM   1564 C  CA   . TRP   B 1 79  ? 16.389  -7.497  -19.608 1.00 13.67  ? 79  TRP   B CA   1 
ATOM   1565 C  C    . TRP   B 1 79  ? 17.841  -7.907  -19.424 1.00 20.66  ? 79  TRP   B C    1 
ATOM   1566 O  O    . TRP   B 1 79  ? 18.730  -7.046  -19.381 1.00 21.73  ? 79  TRP   B O    1 
ATOM   1567 C  CB   . TRP   B 1 79  ? 15.669  -7.428  -18.261 1.00 12.78  ? 79  TRP   B CB   1 
ATOM   1568 C  CG   . TRP   B 1 79  ? 14.321  -6.778  -18.346 1.00 14.61  ? 79  TRP   B CG   1 
ATOM   1569 C  CD1  . TRP   B 1 79  ? 13.102  -7.356  -18.102 1.00 12.14  ? 79  TRP   B CD1  1 
ATOM   1570 C  CD2  . TRP   B 1 79  ? 14.054  -5.428  -18.725 1.00 14.94  ? 79  TRP   B CD2  1 
ATOM   1571 N  NE1  . TRP   B 1 79  ? 12.100  -6.438  -18.301 1.00 12.87  ? 79  TRP   B NE1  1 
ATOM   1572 C  CE2  . TRP   B 1 79  ? 12.661  -5.250  -18.682 1.00 13.46  ? 79  TRP   B CE2  1 
ATOM   1573 C  CE3  . TRP   B 1 79  ? 14.862  -4.351  -19.098 1.00 17.72  ? 79  TRP   B CE3  1 
ATOM   1574 C  CZ2  . TRP   B 1 79  ? 12.050  -4.045  -19.009 1.00 15.30  ? 79  TRP   B CZ2  1 
ATOM   1575 C  CZ3  . TRP   B 1 79  ? 14.252  -3.142  -19.414 1.00 19.10  ? 79  TRP   B CZ3  1 
ATOM   1576 C  CH2  . TRP   B 1 79  ? 12.861  -3.004  -19.366 1.00 15.04  ? 79  TRP   B CH2  1 
ATOM   1577 N  N    . LYS   B 1 80  ? 18.097  -9.210  -19.305 1.00 18.24  ? 80  LYS   B N    1 
ATOM   1578 C  CA   . LYS   B 1 80  ? 19.471  -9.673  -19.132 1.00 23.78  ? 80  LYS   B CA   1 
ATOM   1579 C  C    . LYS   B 1 80  ? 20.341  -9.270  -20.316 1.00 21.83  ? 80  LYS   B C    1 
ATOM   1580 O  O    . LYS   B 1 80  ? 21.494  -8.860  -20.133 1.00 27.52  ? 80  LYS   B O    1 
ATOM   1581 C  CB   . LYS   B 1 80  ? 19.501  -11.184 -18.891 1.00 24.26  ? 80  LYS   B CB   1 
ATOM   1582 C  CG   . LYS   B 1 80  ? 19.149  -11.586 -17.457 1.00 27.38  ? 80  LYS   B CG   1 
ATOM   1583 C  CD   . LYS   B 1 80  ? 18.855  -13.082 -17.319 1.00 35.07  ? 80  LYS   B CD   1 
ATOM   1584 C  CE   . LYS   B 1 80  ? 19.972  -13.957 -17.876 1.00 39.79  ? 80  LYS   B CE   1 
ATOM   1585 N  NZ   . LYS   B 1 80  ? 19.662  -15.410 -17.687 1.00 42.98  ? 80  LYS   B NZ   1 
ATOM   1586 N  N    . ALA   B 1 81  ? 19.793  -9.327  -21.534 1.00 21.63  ? 81  ALA   B N    1 
ATOM   1587 C  CA   . ALA   B 1 81  ? 20.559  -8.916  -22.707 1.00 25.26  ? 81  ALA   B CA   1 
ATOM   1588 C  C    . ALA   B 1 81  ? 20.874  -7.424  -22.695 1.00 29.76  ? 81  ALA   B C    1 
ATOM   1589 O  O    . ALA   B 1 81  ? 21.818  -6.993  -23.367 1.00 36.45  ? 81  ALA   B O    1 
ATOM   1590 C  CB   . ALA   B 1 81  ? 19.840  -9.316  -23.998 1.00 29.14  ? 81  ALA   B CB   1 
ATOM   1591 N  N    . LEU   B 1 82  ? 20.110  -6.634  -21.943 1.00 25.16  ? 82  LEU   B N    1 
ATOM   1592 C  CA   . LEU   B 1 82  ? 20.359  -5.210  -21.769 1.00 26.92  ? 82  LEU   B CA   1 
ATOM   1593 C  C    . LEU   B 1 82  ? 21.218  -4.902  -20.551 1.00 26.07  ? 82  LEU   B C    1 
ATOM   1594 O  O    . LEU   B 1 82  ? 21.503  -3.726  -20.292 1.00 28.31  ? 82  LEU   B O    1 
ATOM   1595 C  CB   . LEU   B 1 82  ? 19.031  -4.449  -21.676 1.00 27.45  ? 82  LEU   B CB   1 
ATOM   1596 C  CG   . LEU   B 1 82  ? 18.200  -4.420  -22.953 1.00 26.33  ? 82  LEU   B CG   1 
ATOM   1597 C  CD1  . LEU   B 1 82  ? 16.825  -3.837  -22.649 1.00 25.47  ? 82  LEU   B CD1  1 
ATOM   1598 C  CD2  . LEU   B 1 82  ? 18.912  -3.592  -24.013 1.00 31.30  ? 82  LEU   B CD2  1 
ATOM   1599 N  N    . GLY   B 1 83  ? 21.636  -5.919  -19.797 1.00 26.37  ? 83  GLY   B N    1 
ATOM   1600 C  CA   . GLY   B 1 83  ? 22.408  -5.699  -18.590 1.00 29.60  ? 83  GLY   B CA   1 
ATOM   1601 C  C    . GLY   B 1 83  ? 21.616  -5.219  -17.398 1.00 28.89  ? 83  GLY   B C    1 
ATOM   1602 O  O    . GLY   B 1 83  ? 22.184  -4.595  -16.497 1.00 26.63  ? 83  GLY   B O    1 
ATOM   1603 N  N    . ILE   B 1 84  ? 20.314  -5.489  -17.357 1.00 22.60  ? 84  ILE   B N    1 
ATOM   1604 C  CA   . ILE   B 1 84  ? 19.426  -4.976  -16.324 1.00 26.46  ? 84  ILE   B CA   1 
ATOM   1605 C  C    . ILE   B 1 84  ? 18.868  -6.162  -15.552 1.00 33.51  ? 84  ILE   B C    1 
ATOM   1606 O  O    . ILE   B 1 84  ? 18.388  -7.129  -16.155 1.00 27.87  ? 84  ILE   B O    1 
ATOM   1607 C  CB   . ILE   B 1 84  ? 18.294  -4.134  -16.942 1.00 22.07  ? 84  ILE   B CB   1 
ATOM   1608 C  CG1  . ILE   B 1 84  ? 18.851  -2.833  -17.543 1.00 21.93  ? 84  ILE   B CG1  1 
ATOM   1609 C  CG2  . ILE   B 1 84  ? 17.225  -3.845  -15.909 1.00 29.30  ? 84  ILE   B CG2  1 
ATOM   1610 C  CD1  . ILE   B 1 84  ? 17.873  -2.116  -18.461 1.00 23.49  ? 84  ILE   B CD1  1 
ATOM   1611 N  N    . SER   B 1 85  ? 18.929  -6.090  -14.231 1.00 25.46  ? 85  SER   B N    1 
ATOM   1612 C  CA   . SER   B 1 85  ? 18.473  -7.196  -13.398 1.00 28.23  ? 85  SER   B CA   1 
ATOM   1613 C  C    . SER   B 1 85  ? 16.958  -7.137  -13.256 1.00 25.55  ? 85  SER   B C    1 
ATOM   1614 O  O    . SER   B 1 85  ? 16.433  -6.156  -12.715 1.00 26.02  ? 85  SER   B O    1 
ATOM   1615 C  CB   . SER   B 1 85  ? 19.122  -7.115  -12.022 1.00 30.31  ? 85  SER   B CB   1 
ATOM   1616 O  OG   . SER   B 1 85  ? 18.648  -8.160  -11.194 1.00 39.39  ? 85  SER   B OG   1 
ATOM   1617 N  N    . PRO   B 1 86  ? 16.216  -8.135  -13.735 1.00 21.25  ? 86  PRO   B N    1 
ATOM   1618 C  CA   . PRO   B 1 86  ? 14.759  -8.068  -13.643 1.00 19.20  ? 86  PRO   B CA   1 
ATOM   1619 C  C    . PRO   B 1 86  ? 14.175  -8.972  -12.575 1.00 17.58  ? 86  PRO   B C    1 
ATOM   1620 O  O    . PRO   B 1 86  ? 14.834  -9.887  -12.067 1.00 21.58  ? 86  PRO   B O    1 
ATOM   1621 C  CB   . PRO   B 1 86  ? 14.330  -8.552  -15.026 1.00 19.97  ? 86  PRO   B CB   1 
ATOM   1622 C  CG   . PRO   B 1 86  ? 15.319  -9.656  -15.286 1.00 19.83  ? 86  PRO   B CG   1 
ATOM   1623 C  CD   . PRO   B 1 86  ? 16.638  -9.254  -14.594 1.00 20.69  ? 86  PRO   B CD   1 
ATOM   1624 N  N    . PHE   B 1 87  ? 12.906  -8.748  -12.272 1.00 14.65  ? 87  PHE   B N    1 
ATOM   1625 C  CA   . PHE   B 1 87  ? 12.202  -9.489  -11.236 1.00 13.25  ? 87  PHE   B CA   1 
ATOM   1626 C  C    . PHE   B 1 87  ? 11.555  -10.760 -11.775 1.00 16.31  ? 87  PHE   B C    1 
ATOM   1627 O  O    . PHE   B 1 87  ? 11.681  -11.832 -11.175 1.00 15.09  ? 87  PHE   B O    1 
ATOM   1628 C  CB   . PHE   B 1 87  ? 11.133  -8.598  -10.618 1.00 16.08  ? 87  PHE   B CB   1 
ATOM   1629 C  CG   . PHE   B 1 87  ? 10.340  -9.274  -9.564  1.00 13.80  ? 87  PHE   B CG   1 
ATOM   1630 C  CD1  . PHE   B 1 87  ? 10.899  -9.515  -8.308  1.00 16.20  ? 87  PHE   B CD1  1 
ATOM   1631 C  CD2  . PHE   B 1 87  ? 9.037   -9.669  -9.806  1.00 14.73  ? 87  PHE   B CD2  1 
ATOM   1632 C  CE1  . PHE   B 1 87  ? 10.162  -10.148 -7.322  1.00 16.46  ? 87  PHE   B CE1  1 
ATOM   1633 C  CE2  . PHE   B 1 87  ? 8.297   -10.306 -8.821  1.00 16.42  ? 87  PHE   B CE2  1 
ATOM   1634 C  CZ   . PHE   B 1 87  ? 8.874   -10.541 -7.572  1.00 15.85  ? 87  PHE   B CZ   1 
ATOM   1635 N  N    . HIS   B 1 88  ? 10.849  -10.666 -12.894 1.00 13.25  ? 88  HIS   B N    1 
ATOM   1636 C  CA   . HIS   B 1 88  ? 10.014  -11.772 -13.339 1.00 12.56  ? 88  HIS   B CA   1 
ATOM   1637 C  C    . HIS   B 1 88  ? 10.814  -12.759 -14.169 1.00 12.94  ? 88  HIS   B C    1 
ATOM   1638 O  O    . HIS   B 1 88  ? 11.768  -12.395 -14.856 1.00 16.53  ? 88  HIS   B O    1 
ATOM   1639 C  CB   . HIS   B 1 88  ? 8.842   -11.246 -14.170 1.00 14.13  ? 88  HIS   B CB   1 
ATOM   1640 C  CG   . HIS   B 1 88  ? 7.970   -10.298 -13.415 1.00 12.95  ? 88  HIS   B CG   1 
ATOM   1641 N  ND1  . HIS   B 1 88  ? 8.119   -8.930  -13.487 1.00 14.75  ? 88  HIS   B ND1  1 
ATOM   1642 C  CD2  . HIS   B 1 88  ? 6.961   -10.523 -12.544 1.00 16.40  ? 88  HIS   B CD2  1 
ATOM   1643 C  CE1  . HIS   B 1 88  ? 7.238   -8.354  -12.694 1.00 15.84  ? 88  HIS   B CE1  1 
ATOM   1644 N  NE2  . HIS   B 1 88  ? 6.516   -9.297  -12.116 1.00 18.01  ? 88  HIS   B NE2  1 
ATOM   1645 N  N    . GLU   B 1 89  ? 10.410  -14.033 -14.099 1.00 12.81  ? 89  GLU   B N    1 
ATOM   1646 C  CA   . GLU   B 1 89  ? 10.944  -15.017 -15.038 1.00 13.74  ? 89  GLU   B CA   1 
ATOM   1647 C  C    . GLU   B 1 89  ? 10.428  -14.757 -16.446 1.00 14.95  ? 89  GLU   B C    1 
ATOM   1648 O  O    . GLU   B 1 89  ? 11.171  -14.869 -17.430 1.00 18.67  ? 89  GLU   B O    1 
ATOM   1649 C  CB   . GLU   B 1 89  ? 10.550  -16.422 -14.582 1.00 14.90  ? 89  GLU   B CB   1 
ATOM   1650 C  CG   . GLU   B 1 89  ? 11.241  -16.835 -13.314 1.00 16.38  ? 89  GLU   B CG   1 
ATOM   1651 C  CD   . GLU   B 1 89  ? 12.725  -17.000 -13.508 1.00 17.89  ? 89  GLU   B CD   1 
ATOM   1652 O  OE1  . GLU   B 1 89  ? 13.109  -17.820 -14.366 1.00 24.58  ? 89  GLU   B OE1  1 
ATOM   1653 O  OE2  . GLU   B 1 89  ? 13.507  -16.311 -12.822 1.00 20.18  ? 89  GLU   B OE2  1 
ATOM   1654 N  N    . HIS   B 1 90  ? 9.153   -14.427 -16.558 1.00 14.31  ? 90  HIS   B N    1 
ATOM   1655 C  CA   . HIS   B 1 90  ? 8.522   -14.093 -17.821 1.00 14.79  ? 90  HIS   B CA   1 
ATOM   1656 C  C    . HIS   B 1 90  ? 7.215   -13.407 -17.479 1.00 18.48  ? 90  HIS   B C    1 
ATOM   1657 O  O    . HIS   B 1 90  ? 6.821   -13.340 -16.314 1.00 20.67  ? 90  HIS   B O    1 
ATOM   1658 C  CB   . HIS   B 1 90  ? 8.300   -15.336 -18.698 1.00 19.42  ? 90  HIS   B CB   1 
ATOM   1659 C  CG   . HIS   B 1 90  ? 7.708   -16.491 -17.969 1.00 25.38  ? 90  HIS   B CG   1 
ATOM   1660 N  ND1  . HIS   B 1 90  ? 8.417   -17.638 -17.692 1.00 30.42  ? 90  HIS   B ND1  1 
ATOM   1661 C  CD2  . HIS   B 1 90  ? 6.476   -16.673 -17.447 1.00 34.87  ? 90  HIS   B CD2  1 
ATOM   1662 C  CE1  . HIS   B 1 90  ? 7.643   -18.482 -17.036 1.00 37.77  ? 90  HIS   B CE1  1 
ATOM   1663 N  NE2  . HIS   B 1 90  ? 6.458   -17.923 -16.879 1.00 34.48  ? 90  HIS   B NE2  1 
ATOM   1664 N  N    . ALA   B 1 91  ? 6.555   -12.869 -18.492 1.00 15.86  ? 91  ALA   B N    1 
ATOM   1665 C  CA   . ALA   B 1 91  ? 5.202   -12.368 -18.323 1.00 15.35  ? 91  ALA   B CA   1 
ATOM   1666 C  C    . ALA   B 1 91  ? 4.275   -13.378 -18.975 1.00 17.75  ? 91  ALA   B C    1 
ATOM   1667 O  O    . ALA   B 1 91  ? 4.582   -13.911 -20.045 1.00 22.26  ? 91  ALA   B O    1 
ATOM   1668 C  CB   . ALA   B 1 91  ? 5.020   -10.994 -18.966 1.00 17.34  ? 91  ALA   B CB   1 
ATOM   1669 N  N    . GLU   B 1 92  ? 3.171   -13.666 -18.285 1.00 19.63  ? 92  GLU   B N    1 
ATOM   1670 C  CA   . GLU   B 1 92  ? 2.208   -14.673 -18.787 1.00 20.03  ? 92  GLU   B CA   1 
ATOM   1671 C  C    . GLU   B 1 92  ? 0.840   -14.017 -18.970 1.00 24.39  ? 92  GLU   B C    1 
ATOM   1672 O  O    . GLU   B 1 92  ? 0.410   -13.259 -18.085 1.00 26.55  ? 92  GLU   B O    1 
ATOM   1673 C  CB   . GLU   B 1 92  ? 2.051   -15.857 -17.835 1.00 28.83  ? 92  GLU   B CB   1 
ATOM   1674 C  CG   . GLU   B 1 92  ? 2.998   -17.012 -18.134 1.00 41.34  ? 92  GLU   B CG   1 
ATOM   1675 C  CD   . GLU   B 1 92  ? 3.152   -17.937 -16.943 1.00 50.98  ? 92  GLU   B CD   1 
ATOM   1676 O  OE1  . GLU   B 1 92  ? 3.392   -19.139 -17.151 1.00 54.54  ? 92  GLU   B OE1  1 
ATOM   1677 O  OE2  . GLU   B 1 92  ? 3.032   -17.451 -15.802 1.00 52.99  ? 92  GLU   B OE2  1 
ATOM   1678 N  N    . VAL   B 1 93  ? 0.202   -14.281 -20.100 1.00 14.91  ? 93  VAL   B N    1 
ATOM   1679 C  CA   . VAL   B 1 93  ? -1.128  -13.771 -20.379 1.00 14.54  ? 93  VAL   B CA   1 
ATOM   1680 C  C    . VAL   B 1 93  ? -1.961  -14.995 -20.719 1.00 13.07  ? 93  VAL   B C    1 
ATOM   1681 O  O    . VAL   B 1 93  ? -1.690  -15.661 -21.724 1.00 14.87  ? 93  VAL   B O    1 
ATOM   1682 C  CB   . VAL   B 1 93  ? -1.133  -12.772 -21.543 1.00 16.04  ? 93  VAL   B CB   1 
ATOM   1683 C  CG1  . VAL   B 1 93  ? -2.544  -12.305 -21.826 1.00 19.59  ? 93  VAL   B CG1  1 
ATOM   1684 C  CG2  . VAL   B 1 93  ? -0.203  -11.583 -21.266 1.00 18.92  ? 93  VAL   B CG2  1 
ATOM   1685 N  N    . VAL   B 1 94  ? -2.952  -15.304 -19.890 1.00 12.59  ? 94  VAL   B N    1 
ATOM   1686 C  CA   . VAL   B 1 94  ? -3.769  -16.510 -20.033 1.00 13.18  ? 94  VAL   B CA   1 
ATOM   1687 C  C    . VAL   B 1 94  ? -5.210  -16.080 -20.245 1.00 15.20  ? 94  VAL   B C    1 
ATOM   1688 O  O    . VAL   B 1 94  ? -5.744  -15.299 -19.451 1.00 14.94  ? 94  VAL   B O    1 
ATOM   1689 C  CB   . VAL   B 1 94  ? -3.650  -17.420 -18.795 1.00 15.32  ? 94  VAL   B CB   1 
ATOM   1690 C  CG1  . VAL   B 1 94  ? -4.451  -18.709 -18.995 1.00 17.16  ? 94  VAL   B CG1  1 
ATOM   1691 C  CG2  . VAL   B 1 94  ? -2.190  -17.727 -18.518 1.00 18.77  ? 94  VAL   B CG2  1 
ATOM   1692 N  N    . PHE   B 1 95  ? -5.841  -16.580 -21.312 1.00 13.83  ? 95  PHE   B N    1 
ATOM   1693 C  CA   . PHE   B 1 95  ? -7.180  -16.116 -21.650 1.00 14.43  ? 95  PHE   B CA   1 
ATOM   1694 C  C    . PHE   B 1 95  ? -7.917  -17.191 -22.429 1.00 18.39  ? 95  PHE   B C    1 
ATOM   1695 O  O    . PHE   B 1 95  ? -7.307  -18.099 -22.990 1.00 15.89  ? 95  PHE   B O    1 
ATOM   1696 C  CB   . PHE   B 1 95  ? -7.119  -14.834 -22.494 1.00 15.08  ? 95  PHE   B CB   1 
ATOM   1697 C  CG   . PHE   B 1 95  ? -6.455  -15.015 -23.848 1.00 15.91  ? 95  PHE   B CG   1 
ATOM   1698 C  CD1  . PHE   B 1 95  ? -5.071  -14.984 -23.975 1.00 19.39  ? 95  PHE   B CD1  1 
ATOM   1699 C  CD2  . PHE   B 1 95  ? -7.224  -15.185 -24.995 1.00 18.81  ? 95  PHE   B CD2  1 
ATOM   1700 C  CE1  . PHE   B 1 95  ? -4.472  -15.135 -25.226 1.00 22.49  ? 95  PHE   B CE1  1 
ATOM   1701 C  CE2  . PHE   B 1 95  ? -6.635  -15.339 -26.237 1.00 21.22  ? 95  PHE   B CE2  1 
ATOM   1702 C  CZ   . PHE   B 1 95  ? -5.256  -15.320 -26.348 1.00 20.71  ? 95  PHE   B CZ   1 
ATOM   1703 N  N    . THR   B 1 96  ? -9.242  -17.066 -22.469 1.00 18.81  ? 96  THR   B N    1 
ATOM   1704 C  CA   . THR   B 1 96  ? -10.074 -17.912 -23.321 1.00 18.71  ? 96  THR   B CA   1 
ATOM   1705 C  C    . THR   B 1 96  ? -10.341 -17.191 -24.635 1.00 21.27  ? 96  THR   B C    1 
ATOM   1706 O  O    . THR   B 1 96  ? -10.751 -16.023 -24.638 1.00 23.30  ? 96  THR   B O    1 
ATOM   1707 C  CB   . THR   B 1 96  ? -11.391 -18.263 -22.628 1.00 17.22  ? 96  THR   B CB   1 
ATOM   1708 O  OG1  . THR   B 1 96  ? -11.117 -19.016 -21.448 1.00 21.13  ? 96  THR   B OG1  1 
ATOM   1709 C  CG2  . THR   B 1 96  ? -12.264 -19.129 -23.554 1.00 24.01  ? 96  THR   B CG2  1 
ATOM   1710 N  N    . ALA   B 1 97  ? -10.100 -17.882 -25.751 1.00 18.09  ? 97  ALA   B N    1 
ATOM   1711 C  CA   . ALA   B 1 97  ? -10.418 -17.350 -27.070 1.00 16.93  ? 97  ALA   B CA   1 
ATOM   1712 C  C    . ALA   B 1 97  ? -11.866 -17.676 -27.405 1.00 18.98  ? 97  ALA   B C    1 
ATOM   1713 O  O    . ALA   B 1 97  ? -12.299 -18.827 -27.258 1.00 21.23  ? 97  ALA   B O    1 
ATOM   1714 C  CB   . ALA   B 1 97  ? -9.495  -17.941 -28.136 1.00 24.79  ? 97  ALA   B CB   1 
ATOM   1715 N  N    . ASN   B 1 98  ? -12.591 -16.659 -27.869 1.00 23.70  ? 98  ASN   B N    1 
ATOM   1716 C  CA   . ASN   B 1 98  ? -14.040 -16.647 -27.987 1.00 38.41  ? 98  ASN   B CA   1 
ATOM   1717 C  C    . ASN   B 1 98  ? -14.416 -16.348 -29.431 1.00 41.37  ? 98  ASN   B C    1 
ATOM   1718 O  O    . ASN   B 1 98  ? -13.778 -15.521 -30.090 1.00 43.22  ? 98  ASN   B O    1 
ATOM   1719 C  CB   . ASN   B 1 98  ? -14.621 -15.560 -27.070 1.00 45.72  ? 98  ASN   B CB   1 
ATOM   1720 C  CG   . ASN   B 1 98  ? -16.111 -15.720 -26.828 1.00 61.51  ? 98  ASN   B CG   1 
ATOM   1721 O  OD1  . ASN   B 1 98  ? -16.723 -16.708 -27.236 1.00 52.68  ? 98  ASN   B OD1  1 
ATOM   1722 N  ND2  . ASN   B 1 98  ? -16.702 -14.746 -26.143 1.00 64.37  ? 98  ASN   B ND2  1 
ATOM   1723 N  N    . ASP   B 1 99  ? -15.397 -17.097 -29.947 1.00 40.10  ? 99  ASP   B N    1 
ATOM   1724 C  CA   . ASP   B 1 99  ? -15.734 -16.995 -31.392 1.00 44.76  ? 99  ASP   B CA   1 
ATOM   1725 C  C    . ASP   B 1 99  ? -16.885 -16.030 -31.670 1.00 48.90  ? 99  ASP   B C    1 
ATOM   1726 O  O    . ASP   B 1 99  ? -17.087 -15.705 -32.850 1.00 60.76  ? 99  ASP   B O    1 
ATOM   1727 C  CB   . ASP   B 1 99  ? -16.126 -18.356 -31.942 1.00 41.95  ? 99  ASP   B CB   1 
ATOM   1728 C  CG   . ASP   B 1 99  ? -15.032 -19.095 -32.695 1.00 33.52  ? 99  ASP   B CG   1 
ATOM   1729 O  OD1  . ASP   B 1 99  ? -13.906 -18.563 -32.761 1.00 51.42  ? 99  ASP   B OD1  1 
ATOM   1730 O  OD2  . ASP   B 1 99  ? -15.320 -20.196 -33.203 1.00 43.99  ? 99  ASP   B OD2  1 
ATOM   1731 N  N    . SER   B 1 100 ? -17.644 -15.640 -30.655 1.00 48.56  ? 100 SER   B N    1 
ATOM   1732 C  CA   . SER   B 1 100 ? -18.828 -14.777 -30.899 1.00 57.78  ? 100 SER   B CA   1 
ATOM   1733 C  C    . SER   B 1 100 ? -18.385 -13.735 -31.941 1.00 61.57  ? 100 SER   B C    1 
ATOM   1734 O  O    . SER   B 1 100 ? -17.498 -12.926 -31.611 1.00 60.63  ? 100 SER   B O    1 
ATOM   1735 C  CB   . SER   B 1 100 ? -19.331 -14.225 -29.600 1.00 67.85  ? 100 SER   B CB   1 
ATOM   1736 O  OG   . SER   B 1 100 ? -19.470 -15.268 -28.646 1.00 59.06  ? 100 SER   B OG   1 
ATOM   1737 N  N    . GLY   B 1 101 ? -18.977 -13.757 -33.146 1.00 53.94  ? 101 GLY   B N    1 
ATOM   1738 C  CA   . GLY   B 1 101 ? -18.583 -12.829 -34.232 1.00 57.39  ? 101 GLY   B CA   1 
ATOM   1739 C  C    . GLY   B 1 101 ? -17.142 -12.765 -34.719 1.00 63.15  ? 101 GLY   B C    1 
ATOM   1740 O  O    . GLY   B 1 101 ? -16.276 -13.483 -34.195 1.00 68.16  ? 101 GLY   B O    1 
ATOM   1741 N  N    . PRO   B 1 102 ? -16.780 -11.919 -35.723 1.00 62.52  ? 102 PRO   B N    1 
ATOM   1742 C  CA   . PRO   B 1 102 ? -15.417 -11.918 -36.234 1.00 63.45  ? 102 PRO   B CA   1 
ATOM   1743 C  C    . PRO   B 1 102 ? -14.510 -11.123 -35.306 1.00 70.61  ? 102 PRO   B C    1 
ATOM   1744 O  O    . PRO   B 1 102 ? -14.805 -9.951  -35.050 1.00 64.41  ? 102 PRO   B O    1 
ATOM   1745 C  CB   . PRO   B 1 102 ? -15.521 -11.289 -37.637 1.00 69.23  ? 102 PRO   B CB   1 
ATOM   1746 C  CG   . PRO   B 1 102 ? -16.789 -10.467 -37.610 1.00 56.00  ? 102 PRO   B CG   1 
ATOM   1747 C  CD   . PRO   B 1 102 ? -17.618 -10.930 -36.428 1.00 53.94  ? 102 PRO   B CD   1 
ATOM   1748 N  N    . ARG   B 1 103 ? -13.426 -11.727 -34.811 1.00 50.00  ? 103 ARG   B N    1 
ATOM   1749 C  CA   . ARG   B 1 103 ? -12.611 -11.000 -33.803 1.00 50.00  ? 103 ARG   B CA   1 
ATOM   1750 C  C    . ARG   B 1 103 ? -11.099 -11.194 -34.017 1.00 50.00  ? 103 ARG   B C    1 
ATOM   1751 O  O    . ARG   B 1 103 ? -10.691 -12.317 -34.375 1.00 50.00  ? 103 ARG   B O    1 
ATOM   1752 C  CB   . ARG   B 1 103 ? -12.984 -11.461 -32.387 1.00 50.00  ? 103 ARG   B CB   1 
ATOM   1753 C  CG   . ARG   B 1 103 ? -14.447 -11.630 -32.004 1.00 50.00  ? 103 ARG   B CG   1 
ATOM   1754 C  CD   . ARG   B 1 103 ? -15.147 -10.315 -31.709 1.00 50.00  ? 103 ARG   B CD   1 
ATOM   1755 N  NE   . ARG   B 1 103 ? -16.583 -10.426 -31.983 1.00 50.00  ? 103 ARG   B NE   1 
ATOM   1756 C  CZ   . ARG   B 1 103 ? -17.268 -9.615  -32.778 1.00 50.00  ? 103 ARG   B CZ   1 
ATOM   1757 N  NH1  . ARG   B 1 103 ? -16.639 -8.708  -33.502 1.00 50.00  ? 103 ARG   B NH1  1 
ATOM   1758 N  NH2  . ARG   B 1 103 ? -18.582 -9.710  -32.843 1.00 50.00  ? 103 ARG   B NH2  1 
ATOM   1759 N  N    . ARG   B 1 104 ? -10.307 -10.134 -33.813 1.00 50.00  ? 104 ARG   B N    1 
ATOM   1760 C  CA   . ARG   B 1 104 ? -8.826  -10.239 -33.883 1.00 50.00  ? 104 ARG   B CA   1 
ATOM   1761 C  C    . ARG   B 1 104 ? -8.261  -9.886  -32.495 1.00 50.00  ? 104 ARG   B C    1 
ATOM   1762 O  O    . ARG   B 1 104 ? -8.700  -8.867  -31.931 1.00 50.00  ? 104 ARG   B O    1 
ATOM   1763 C  CB   . ARG   B 1 104 ? -8.253  -9.309  -34.953 1.00 50.00  ? 104 ARG   B CB   1 
ATOM   1764 C  CG   . ARG   B 1 104 ? -6.774  -8.995  -34.786 1.00 50.00  ? 104 ARG   B CG   1 
ATOM   1765 C  CD   . ARG   B 1 104 ? -6.185  -8.446  -36.072 1.00 50.00  ? 104 ARG   B CD   1 
ATOM   1766 N  NE   . ARG   B 1 104 ? -6.625  -9.227  -37.233 1.00 50.00  ? 104 ARG   B NE   1 
ATOM   1767 C  CZ   . ARG   B 1 104 ? -6.170  -9.059  -38.467 1.00 50.00  ? 104 ARG   B CZ   1 
ATOM   1768 N  NH1  . ARG   B 1 104 ? -5.489  -7.971  -38.776 1.00 50.00  ? 104 ARG   B NH1  1 
ATOM   1769 N  NH2  . ARG   B 1 104 ? -6.394  -9.982  -39.385 1.00 50.00  ? 104 ARG   B NH2  1 
ATOM   1770 N  N    . TYR   B 1 105 ? -7.364  -10.709 -31.957 1.00 22.38  ? 105 TYR   B N    1 
ATOM   1771 C  CA   . TYR   B 1 105 ? -6.856  -10.478 -30.580 1.00 21.91  ? 105 TYR   B CA   1 
ATOM   1772 C  C    . TYR   B 1 105 ? -5.469  -9.871  -30.608 1.00 18.62  ? 105 TYR   B C    1 
ATOM   1773 O  O    . TYR   B 1 105 ? -4.555  -10.473 -31.190 1.00 20.95  ? 105 TYR   B O    1 
ATOM   1774 C  CB   . TYR   B 1 105 ? -6.761  -11.789 -29.793 1.00 22.84  ? 105 TYR   B CB   1 
ATOM   1775 C  CG   . TYR   B 1 105 ? -8.076  -12.433 -29.382 1.00 23.84  ? 105 TYR   B CG   1 
ATOM   1776 C  CD1  . TYR   B 1 105 ? -8.710  -13.359 -30.199 1.00 34.30  ? 105 TYR   B CD1  1 
ATOM   1777 C  CD2  . TYR   B 1 105 ? -8.671  -12.124 -28.168 1.00 28.42  ? 105 TYR   B CD2  1 
ATOM   1778 C  CE1  . TYR   B 1 105 ? -9.909  -13.944 -29.828 1.00 32.91  ? 105 TYR   B CE1  1 
ATOM   1779 C  CE2  . TYR   B 1 105 ? -9.867  -12.705 -27.784 1.00 28.07  ? 105 TYR   B CE2  1 
ATOM   1780 C  CZ   . TYR   B 1 105 ? -10.487 -13.617 -28.616 1.00 29.42  ? 105 TYR   B CZ   1 
ATOM   1781 O  OH   . TYR   B 1 105 ? -11.664 -14.183 -28.234 1.00 30.92  ? 105 TYR   B OH   1 
ATOM   1782 N  N    . THR   B 1 106 ? -5.318  -8.678  -30.038 1.00 17.94  ? 106 THR   B N    1 
ATOM   1783 C  CA   . THR   B 1 106 ? -3.995  -8.100  -29.856 1.00 14.95  ? 106 THR   B CA   1 
ATOM   1784 C  C    . THR   B 1 106 ? -3.676  -8.106  -28.373 1.00 17.87  ? 106 THR   B C    1 
ATOM   1785 O  O    . THR   B 1 106 ? -4.416  -7.524  -27.576 1.00 18.70  ? 106 THR   B O    1 
ATOM   1786 C  CB   . THR   B 1 106 ? -3.916  -6.682  -30.411 1.00 21.44  ? 106 THR   B CB   1 
ATOM   1787 O  OG1  . THR   B 1 106 ? -4.162  -6.726  -31.821 1.00 23.85  ? 106 THR   B OG1  1 
ATOM   1788 C  CG2  . THR   B 1 106 ? -2.538  -6.100  -30.165 1.00 22.00  ? 106 THR   B CG2  1 
ATOM   1789 N  N    . ILE   B 1 107 ? -2.591  -8.776  -28.011 1.00 14.25  ? 107 ILE   B N    1 
ATOM   1790 C  CA   . ILE   B 1 107 ? -2.098  -8.803  -26.638 1.00 15.12  ? 107 ILE   B CA   1 
ATOM   1791 C  C    . ILE   B 1 107 ? -0.941  -7.821  -26.565 1.00 14.92  ? 107 ILE   B C    1 
ATOM   1792 O  O    . ILE   B 1 107 ? 0.078   -8.002  -27.236 1.00 16.26  ? 107 ILE   B O    1 
ATOM   1793 C  CB   . ILE   B 1 107 ? -1.615  -10.213 -26.264 1.00 13.03  ? 107 ILE   B CB   1 
ATOM   1794 C  CG1  . ILE   B 1 107 ? -2.744  -11.238 -26.399 1.00 21.68  ? 107 ILE   B CG1  1 
ATOM   1795 C  CG2  . ILE   B 1 107 ? -1.005  -10.215 -24.866 1.00 17.47  ? 107 ILE   B CG2  1 
ATOM   1796 C  CD1  . ILE   B 1 107 ? -3.965  -10.929 -25.617 1.00 24.02  ? 107 ILE   B CD1  1 
ATOM   1797 N  N    . ALA   B 1 108 ? -1.080  -6.762  -25.769 1.00 14.02  ? 108 ALA   B N    1 
ATOM   1798 C  CA   . ALA   B 1 108 ? -0.022  -5.779  -25.630 1.00 15.98  ? 108 ALA   B CA   1 
ATOM   1799 C  C    . ALA   B 1 108 ? 0.581   -5.854  -24.233 1.00 13.44  ? 108 ALA   B C    1 
ATOM   1800 O  O    . ALA   B 1 108 ? -0.133  -6.064  -23.242 1.00 15.31  ? 108 ALA   B O    1 
ATOM   1801 C  CB   . ALA   B 1 108 ? -0.551  -4.362  -25.896 1.00 17.09  ? 108 ALA   B CB   1 
ATOM   1802 N  N    . ALA   B 1 109 ? 1.889   -5.694  -24.161 1.00 12.83  ? 109 ALA   B N    1 
ATOM   1803 C  CA   . ALA   B 1 109 ? 2.599   -5.732  -22.890 1.00 13.77  ? 109 ALA   B CA   1 
ATOM   1804 C  C    . ALA   B 1 109 ? 3.598   -4.594  -22.820 1.00 14.87  ? 109 ALA   B C    1 
ATOM   1805 O  O    . ALA   B 1 109 ? 4.313   -4.313  -23.788 1.00 16.34  ? 109 ALA   B O    1 
ATOM   1806 C  CB   . ALA   B 1 109 ? 3.329   -7.056  -22.678 1.00 16.19  ? 109 ALA   B CB   1 
ATOM   1807 N  N    . LEU   B 1 110 ? 3.652   -3.956  -21.657 1.00 12.87  ? 110 LEU   B N    1 
ATOM   1808 C  CA   . LEU   B 1 110 ? 4.553   -2.847  -21.378 1.00 14.04  ? 110 LEU   B CA   1 
ATOM   1809 C  C    . LEU   B 1 110 ? 5.457   -3.305  -20.247 1.00 13.24  ? 110 LEU   B C    1 
ATOM   1810 O  O    . LEU   B 1 110 ? 4.960   -3.666  -19.166 1.00 13.03  ? 110 LEU   B O    1 
ATOM   1811 C  CB   . LEU   B 1 110 ? 3.744   -1.621  -20.945 1.00 13.09  ? 110 LEU   B CB   1 
ATOM   1812 C  CG   . LEU   B 1 110 ? 4.593   -0.422  -20.541 1.00 13.13  ? 110 LEU   B CG   1 
ATOM   1813 C  CD1  . LEU   B 1 110 ? 5.427   0.025   -21.743 1.00 13.83  ? 110 LEU   B CD1  1 
ATOM   1814 C  CD2  . LEU   B 1 110 ? 3.660   0.683   -20.028 1.00 17.01  ? 110 LEU   B CD2  1 
ATOM   1815 N  N    . LEU   B 1 111 ? 6.763   -3.312  -20.486 1.00 12.29  ? 111 LEU   B N    1 
ATOM   1816 C  CA   . LEU   B 1 111 ? 7.713   -3.973  -19.596 1.00 12.26  ? 111 LEU   B CA   1 
ATOM   1817 C  C    . LEU   B 1 111 ? 8.598   -2.988  -18.845 1.00 12.07  ? 111 LEU   B C    1 
ATOM   1818 O  O    . LEU   B 1 111 ? 9.152   -2.055  -19.438 1.00 12.21  ? 111 LEU   B O    1 
ATOM   1819 C  CB   . LEU   B 1 111 ? 8.660   -4.876  -20.390 1.00 13.33  ? 111 LEU   B CB   1 
ATOM   1820 C  CG   . LEU   B 1 111 ? 8.038   -5.905  -21.322 1.00 13.50  ? 111 LEU   B CG   1 
ATOM   1821 C  CD1  . LEU   B 1 111 ? 9.164   -6.772  -21.936 1.00 15.47  ? 111 LEU   B CD1  1 
ATOM   1822 C  CD2  . LEU   B 1 111 ? 6.976   -6.765  -20.607 1.00 13.78  ? 111 LEU   B CD2  1 
ATOM   1823 N  N    . SER   B 1 112 ? 8.760   -3.231  -17.546 1.00 12.51  ? 112 SER   B N    1 
ATOM   1824 C  CA   . SER   B 1 112 ? 9.770   -2.599  -16.709 1.00 13.61  ? 112 SER   B CA   1 
ATOM   1825 C  C    . SER   B 1 112 ? 10.483  -3.700  -15.942 1.00 12.03  ? 112 SER   B C    1 
ATOM   1826 O  O    . SER   B 1 112 ? 9.998   -4.834  -15.882 1.00 12.58  ? 112 SER   B O    1 
ATOM   1827 C  CB   . SER   B 1 112 ? 9.157   -1.615  -15.702 1.00 14.89  ? 112 SER   B CB   1 
ATOM   1828 O  OG   . SER   B 1 112 ? 8.495   -0.542  -16.358 1.00 18.39  ? 112 SER   B OG   1 
ATOM   1829 N  N    . PRO   B 1 113 ? 11.648  -3.405  -15.354 1.00 12.42  ? 113 PRO   B N    1 
ATOM   1830 C  CA   . PRO   B 1 113 ? 12.381  -4.493  -14.681 1.00 12.07  ? 113 PRO   B CA   1 
ATOM   1831 C  C    . PRO   B 1 113 ? 11.617  -5.169  -13.556 1.00 13.75  ? 113 PRO   B C    1 
ATOM   1832 O  O    . PRO   B 1 113 ? 11.719  -6.396  -13.415 1.00 13.09  ? 113 PRO   B O    1 
ATOM   1833 C  CB   . PRO   B 1 113 ? 13.676  -3.810  -14.232 1.00 15.21  ? 113 PRO   B CB   1 
ATOM   1834 C  CG   . PRO   B 1 113 ? 13.897  -2.780  -15.295 1.00 14.50  ? 113 PRO   B CG   1 
ATOM   1835 C  CD   . PRO   B 1 113 ? 12.518  -2.229  -15.553 1.00 13.86  ? 113 PRO   B CD   1 
ATOM   1836 N  N    . TYR   B 1 114 ? 10.854  -4.426  -12.759 1.00 12.94  ? 114 TYR   B N    1 
ATOM   1837 C  CA   . TYR   B 1 114 ? 10.109  -5.035  -11.651 1.00 12.65  ? 114 TYR   B CA   1 
ATOM   1838 C  C    . TYR   B 1 114 ? 8.606   -5.044  -11.878 1.00 12.16  ? 114 TYR   B C    1 
ATOM   1839 O  O    . TYR   B 1 114 ? 7.825   -5.391  -10.998 1.00 12.02  ? 114 TYR   B O    1 
ATOM   1840 C  CB   . TYR   B 1 114 ? 10.450  -4.365  -10.315 1.00 11.66  ? 114 TYR   B CB   1 
ATOM   1841 C  CG   . TYR   B 1 114 ? 11.800  -4.781  -9.785  1.00 11.62  ? 114 TYR   B CG   1 
ATOM   1842 C  CD1  . TYR   B 1 114 ? 12.962  -4.252  -10.313 1.00 13.99  ? 114 TYR   B CD1  1 
ATOM   1843 C  CD2  . TYR   B 1 114 ? 11.908  -5.714  -8.769  1.00 13.37  ? 114 TYR   B CD2  1 
ATOM   1844 C  CE1  . TYR   B 1 114 ? 14.209  -4.638  -9.841  1.00 18.03  ? 114 TYR   B CE1  1 
ATOM   1845 C  CE2  . TYR   B 1 114 ? 13.140  -6.116  -8.299  1.00 11.47  ? 114 TYR   B CE2  1 
ATOM   1846 C  CZ   . TYR   B 1 114 ? 14.287  -5.567  -8.829  1.00 18.84  ? 114 TYR   B CZ   1 
ATOM   1847 O  OH   . TYR   B 1 114 ? 15.508  -5.966  -8.345  1.00 19.33  ? 114 TYR   B OH   1 
ATOM   1848 N  N    A SER   B 1 115 ? 8.093   -4.671  -13.034 0.70 12.06  ? 115 SER   B N    1 
ATOM   1849 N  N    C SER   B 1 115 ? 8.150   -4.611  -13.087 0.26 12.13  ? 115 SER   B N    1 
ATOM   1850 C  CA   A SER   B 1 115 ? 6.668   -4.469  -13.256 0.71 12.12  ? 115 SER   B CA   1 
ATOM   1851 C  CA   C SER   B 1 115 ? 6.716   -4.457  -13.289 0.27 12.28  ? 115 SER   B CA   1 
ATOM   1852 C  C    A SER   B 1 115 ? 6.338   -4.761  -14.710 0.70 12.27  ? 115 SER   B C    1 
ATOM   1853 C  C    C SER   B 1 115 ? 6.350   -4.795  -14.723 0.26 12.38  ? 115 SER   B C    1 
ATOM   1854 O  O    A SER   B 1 115 ? 7.171   -4.582  -15.601 0.70 14.14  ? 115 SER   B O    1 
ATOM   1855 O  O    C SER   B 1 115 ? 7.180   -4.691  -15.626 0.26 14.10  ? 115 SER   B O    1 
ATOM   1856 C  CB   A SER   B 1 115 ? 6.260   -3.020  -12.958 0.71 13.31  ? 115 SER   B CB   1 
ATOM   1857 C  CB   C SER   B 1 115 ? 6.286   -3.010  -13.019 0.27 13.40  ? 115 SER   B CB   1 
ATOM   1858 O  OG   A SER   B 1 115 ? 4.901   -2.797  -13.267 0.71 16.48  ? 115 SER   B OG   1 
ATOM   1859 O  OG   C SER   B 1 115 ? 6.904   -2.487  -11.857 0.27 16.61  ? 115 SER   B OG   1 
ATOM   1860 N  N    . TYR   B 1 116 ? 5.107   -5.195  -14.943 1.00 12.86  ? 116 TYR   B N    1 
ATOM   1861 C  CA   . TYR   B 1 116 ? 4.598   -5.195  -16.307 1.00 14.38  ? 116 TYR   B CA   1 
ATOM   1862 C  C    . TYR   B 1 116 ? 3.111   -4.917  -16.300 1.00 15.84  ? 116 TYR   B C    1 
ATOM   1863 O  O    . TYR   B 1 116 ? 2.411   -5.180  -15.319 1.00 14.22  ? 116 TYR   B O    1 
ATOM   1864 C  CB   . TYR   B 1 116 ? 4.953   -6.435  -17.133 1.00 14.94  ? 116 TYR   B CB   1 
ATOM   1865 C  CG   . TYR   B 1 116 ? 4.338   -7.725  -16.675 1.00 13.82  ? 116 TYR   B CG   1 
ATOM   1866 C  CD1  . TYR   B 1 116 ? 3.084   -8.112  -17.103 1.00 12.95  ? 116 TYR   B CD1  1 
ATOM   1867 C  CD2  . TYR   B 1 116 ? 5.028   -8.572  -15.807 1.00 17.00  ? 116 TYR   B CD2  1 
ATOM   1868 C  CE1  . TYR   B 1 116 ? 2.517   -9.319  -16.680 1.00 19.14  ? 116 TYR   B CE1  1 
ATOM   1869 C  CE2  . TYR   B 1 116 ? 4.482   -9.780  -15.403 1.00 18.69  ? 116 TYR   B CE2  1 
ATOM   1870 C  CZ   . TYR   B 1 116 ? 3.235   -10.137 -15.828 1.00 18.99  ? 116 TYR   B CZ   1 
ATOM   1871 O  OH   . TYR   B 1 116 ? 2.709   -11.347 -15.411 1.00 26.64  ? 116 TYR   B OH   1 
ATOM   1872 N  N    A SER   B 1 117 ? 2.657   -4.365  -17.429 0.35 13.45  ? 117 SER   B N    1 
ATOM   1873 N  N    B SER   B 1 117 ? 2.660   -4.359  -17.427 0.65 13.38  ? 117 SER   B N    1 
ATOM   1874 C  CA   A SER   B 1 117 ? 1.218   -4.082  -17.620 0.35 15.43  ? 117 SER   B CA   1 
ATOM   1875 C  CA   B SER   B 1 117 ? 1.222   -4.081  -17.631 0.65 15.47  ? 117 SER   B CA   1 
ATOM   1876 C  C    A SER   B 1 117 ? 0.799   -4.716  -18.950 0.35 12.95  ? 117 SER   B C    1 
ATOM   1877 C  C    B SER   B 1 117 ? 0.815   -4.749  -18.947 0.65 13.08  ? 117 SER   B C    1 
ATOM   1878 O  O    A SER   B 1 117 ? 1.681   -4.854  -19.820 0.35 15.83  ? 117 SER   B O    1 
ATOM   1879 O  O    B SER   B 1 117 ? 1.687   -4.887  -19.822 0.65 15.67  ? 117 SER   B O    1 
ATOM   1880 C  CB   A SER   B 1 117 ? 0.958   -2.608  -17.633 0.35 16.37  ? 117 SER   B CB   1 
ATOM   1881 C  CB   B SER   B 1 117 ? 0.956   -2.608  -17.699 0.65 16.31  ? 117 SER   B CB   1 
ATOM   1882 O  OG   A SER   B 1 117 ? -0.394  -2.342  -17.976 0.35 16.47  ? 117 SER   B OG   1 
ATOM   1883 O  OG   B SER   B 1 117 ? 1.392   -1.947  -16.521 0.65 16.75  ? 117 SER   B OG   1 
ATOM   1884 N  N    . THR   B 1 118 ? -0.345  -5.391  -18.955 1.00 11.95  ? 118 THR   B N    1 
ATOM   1885 C  CA   . THR   B 1 118 ? -0.819  -6.042  -20.158 1.00 15.17  ? 118 THR   B CA   1 
ATOM   1886 C  C    . THR   B 1 118 ? -2.284  -5.713  -20.378 1.00 15.36  ? 118 THR   B C    1 
ATOM   1887 O  O    . THR   B 1 118 ? -3.053  -5.518  -19.429 1.00 16.90  ? 118 THR   B O    1 
ATOM   1888 C  CB   . THR   B 1 118 ? -0.537  -7.552  -20.143 1.00 14.37  ? 118 THR   B CB   1 
ATOM   1889 O  OG1  . THR   B 1 118 ? -0.821  -8.092  -21.434 1.00 16.18  ? 118 THR   B OG1  1 
ATOM   1890 C  CG2  . THR   B 1 118 ? -1.399  -8.266  -19.115 1.00 15.36  ? 118 THR   B CG2  1 
ATOM   1891 N  N    . THR   B 1 119 ? -2.649  -5.606  -21.650 1.00 14.13  ? 119 THR   B N    1 
ATOM   1892 C  CA   A THR   B 1 119 ? -4.037  -5.384  -22.018 0.92 14.43  ? 119 THR   B CA   1 
ATOM   1893 C  CA   B THR   B 1 119 ? -4.016  -5.338  -22.055 0.08 14.49  ? 119 THR   B CA   1 
ATOM   1894 C  C    . THR   B 1 119 ? -4.337  -6.177  -23.279 1.00 15.11  ? 119 THR   B C    1 
ATOM   1895 O  O    . THR   B 1 119 ? -3.435  -6.629  -23.989 1.00 16.28  ? 119 THR   B O    1 
ATOM   1896 C  CB   A THR   B 1 119 ? -4.394  -3.890  -22.192 0.92 16.77  ? 119 THR   B CB   1 
ATOM   1897 C  CB   B THR   B 1 119 ? -4.175  -3.876  -22.445 0.08 16.35  ? 119 THR   B CB   1 
ATOM   1898 O  OG1  A THR   B 1 119 ? -5.823  -3.739  -22.195 0.92 15.85  ? 119 THR   B OG1  1 
ATOM   1899 O  OG1  B THR   B 1 119 ? -3.180  -3.100  -21.770 0.08 14.40  ? 119 THR   B OG1  1 
ATOM   1900 C  CG2  A THR   B 1 119 ? -3.808  -3.335  -23.495 0.92 15.27  ? 119 THR   B CG2  1 
ATOM   1901 C  CG2  B THR   B 1 119 ? -5.531  -3.405  -22.048 0.08 16.44  ? 119 THR   B CG2  1 
ATOM   1902 N  N    . ALA   B 1 120 ? -5.621  -6.366  -23.521 1.00 13.18  ? 120 ALA   B N    1 
ATOM   1903 C  CA   . ALA   B 1 120 ? -6.103  -7.033  -24.725 1.00 15.69  ? 120 ALA   B CA   1 
ATOM   1904 C  C    . ALA   B 1 120 ? -6.957  -6.052  -25.510 1.00 16.28  ? 120 ALA   B C    1 
ATOM   1905 O  O    . ALA   B 1 120 ? -7.782  -5.330  -24.939 1.00 16.84  ? 120 ALA   B O    1 
ATOM   1906 C  CB   . ALA   B 1 120 ? -6.933  -8.267  -24.375 1.00 17.02  ? 120 ALA   B CB   1 
ATOM   1907 N  N    . VAL   B 1 121 ? -6.734  -6.010  -26.817 1.00 16.91  ? 121 VAL   B N    1 
ATOM   1908 C  CA   . VAL   B 1 121 ? -7.598  -5.289  -27.737 1.00 20.59  ? 121 VAL   B CA   1 
ATOM   1909 C  C    . VAL   B 1 121 ? -8.255  -6.343  -28.609 1.00 21.14  ? 121 VAL   B C    1 
ATOM   1910 O  O    . VAL   B 1 121 ? -7.570  -7.107  -29.298 1.00 24.22  ? 121 VAL   B O    1 
ATOM   1911 C  CB   . VAL   B 1 121 ? -6.807  -4.273  -28.569 1.00 21.02  ? 121 VAL   B CB   1 
ATOM   1912 C  CG1  . VAL   B 1 121 ? -7.756  -3.382  -29.378 1.00 27.12  ? 121 VAL   B CG1  1 
ATOM   1913 C  CG2  . VAL   B 1 121 ? -5.918  -3.427  -27.662 1.00 30.04  ? 121 VAL   B CG2  1 
ATOM   1914 N  N    . VAL   B 1 122 ? -9.570  -6.418  -28.541 1.00 19.88  ? 122 VAL   B N    1 
ATOM   1915 C  CA   . VAL   B 1 122 ? -10.336 -7.426  -29.245 1.00 21.51  ? 122 VAL   B CA   1 
ATOM   1916 C  C    . VAL   B 1 122 ? -11.213 -6.660  -30.219 1.00 30.36  ? 122 VAL   B C    1 
ATOM   1917 O  O    . VAL   B 1 122 ? -12.173 -6.001  -29.802 1.00 25.67  ? 122 VAL   B O    1 
ATOM   1918 C  CB   . VAL   B 1 122 ? -11.157 -8.263  -28.257 1.00 22.03  ? 122 VAL   B CB   1 
ATOM   1919 C  CG1  . VAL   B 1 122 ? -12.032 -9.283  -28.970 1.00 38.61  ? 122 VAL   B CG1  1 
ATOM   1920 C  CG2  . VAL   B 1 122 ? -10.218 -8.952  -27.259 1.00 25.13  ? 122 VAL   B CG2  1 
ATOM   1921 N  N    . THR   B 1 123 ? -10.854 -6.704  -31.508 1.00 30.06  ? 123 THR   B N    1 
ATOM   1922 C  CA   . THR   B 1 123 ? -11.512 -5.906  -32.537 1.00 36.70  ? 123 THR   B CA   1 
ATOM   1923 C  C    . THR   B 1 123 ? -11.996 -6.775  -33.690 1.00 54.99  ? 123 THR   B C    1 
ATOM   1924 O  O    . THR   B 1 123 ? -11.928 -8.005  -33.635 1.00 45.39  ? 123 THR   B O    1 
ATOM   1925 C  CB   . THR   B 1 123 ? -10.566 -4.839  -33.107 1.00 39.65  ? 123 THR   B CB   1 
ATOM   1926 O  OG1  . THR   B 1 123 ? -9.390  -5.464  -33.642 1.00 42.49  ? 123 THR   B OG1  1 
ATOM   1927 C  CG2  . THR   B 1 123 ? -10.169 -3.832  -32.044 1.00 31.10  ? 123 THR   B CG2  1 
ATOM   1928 N  N    . ASN   B 1 124 ? -12.634 -6.090  -34.640 1.00 61.48  ? 124 ASN   B N    1 
ATOM   1929 C  CA   . ASN   B 1 124 ? -13.172 -6.763  -35.847 1.00 68.97  ? 124 ASN   B CA   1 
ATOM   1930 C  C    . ASN   B 1 124 ? -12.868 -5.799  -36.993 1.00 73.05  ? 124 ASN   B C    1 
ATOM   1931 O  O    . ASN   B 1 124 ? -13.634 -4.835  -37.193 1.00 72.81  ? 124 ASN   B O    1 
ATOM   1932 C  CB   . ASN   B 1 124 ? -14.653 -7.080  -35.681 1.00 66.26  ? 124 ASN   B CB   1 
ATOM   1933 C  CG   . ASN   B 1 124 ? -15.405 -7.129  -36.990 1.00 67.27  ? 124 ASN   B CG   1 
ATOM   1934 O  OD1  . ASN   B 1 124 ? -14.885 -7.621  -37.999 1.00 67.30  ? 124 ASN   B OD1  1 
ATOM   1935 N  ND2  . ASN   B 1 124 ? -16.632 -6.633  -36.993 1.00 70.46  ? 124 ASN   B ND2  1 
ATOM   1936 N  N    . PRO   B 1 125 ? -11.726 -5.963  -37.686 1.00 85.03  ? 125 PRO   B N    1 
ATOM   1937 C  CA   . PRO   B 1 125 ? -11.364 -5.075  -38.778 1.00 93.35  ? 125 PRO   B CA   1 
ATOM   1938 C  C    . PRO   B 1 125 ? -11.720 -5.676  -40.127 1.00 96.88  ? 125 PRO   B C    1 
ATOM   1939 O  O    . PRO   B 1 125 ? -12.457 -4.991  -40.863 1.00 98.20  ? 125 PRO   B O    1 
ATOM   1940 C  CB   . PRO   B 1 125 ? -9.860  -5.014  -38.542 1.00 90.33  ? 125 PRO   B CB   1 
ATOM   1941 C  CG   . PRO   B 1 125 ? -9.513  -6.433  -38.152 1.00 89.42  ? 125 PRO   B CG   1 
ATOM   1942 C  CD   . PRO   B 1 125 ? -10.730 -6.984  -37.429 1.00 85.69  ? 125 PRO   B CD   1 
HETATM 1943 C  C1   . EDO   C 2 .   ? 9.538   -20.820 14.171  1.00 58.01  ? 201 EDO   A C1   1 
HETATM 1944 O  O1   . EDO   C 2 .   ? 9.130   -19.782 15.034  1.00 68.60  ? 201 EDO   A O1   1 
HETATM 1945 C  C2   . EDO   C 2 .   ? 8.520   -21.934 14.189  1.00 61.61  ? 201 EDO   A C2   1 
HETATM 1946 O  O2   . EDO   C 2 .   ? 8.967   -23.012 13.395  1.00 53.02  ? 201 EDO   A O2   1 
HETATM 1947 C  C1   . EDO   D 2 .   ? -0.876  -21.514 -16.362 1.00 47.09  ? 202 EDO   A C1   1 
HETATM 1948 O  O1   . EDO   D 2 .   ? 0.108   -20.884 -15.576 1.00 57.56  ? 202 EDO   A O1   1 
HETATM 1949 C  C2   . EDO   D 2 .   ? -2.021  -21.996 -15.505 1.00 53.47  ? 202 EDO   A C2   1 
HETATM 1950 O  O2   . EDO   D 2 .   ? -1.545  -22.862 -14.499 1.00 65.59  ? 202 EDO   A O2   1 
HETATM 1951 C  C10  . A1ICF E 3 .   ? 0.106   -1.200  -4.310  0.47 34.22  ? 203 A1ICF A C10  1 
HETATM 1952 C  C11  . A1ICF E 3 .   ? 1.409   -1.437  -3.488  0.47 29.60  ? 203 A1ICF A C11  1 
HETATM 1953 C  C12  . A1ICF E 3 .   ? 2.483   -2.057  -4.114  0.47 30.51  ? 203 A1ICF A C12  1 
HETATM 1954 C  C13  . A1ICF E 3 .   ? 3.690   -2.329  -3.438  0.47 28.01  ? 203 A1ICF A C13  1 
HETATM 1955 C  C14  . A1ICF E 3 .   ? 3.828   -1.967  -2.079  0.47 24.70  ? 203 A1ICF A C14  1 
HETATM 1956 C  C15  . A1ICF E 3 .   ? 2.756   -1.356  -1.428  0.47 28.64  ? 203 A1ICF A C15  1 
HETATM 1957 C  C16  . A1ICF E 3 .   ? 1.549   -1.084  -2.100  0.47 31.18  ? 203 A1ICF A C16  1 
HETATM 1958 C  C17  . A1ICF E 3 .   ? 0.452   -0.409  -1.290  0.47 33.07  ? 203 A1ICF A C17  1 
HETATM 1959 C  C01  . A1ICF E 3 .   ? -0.224  2.300   -9.322  0.47 16.84  ? 203 A1ICF A C01  1 
HETATM 1960 C  C02  . A1ICF E 3 .   ? 0.013   1.401   -8.282  0.47 20.67  ? 203 A1ICF A C02  1 
HETATM 1961 C  C03  . A1ICF E 3 .   ? 0.158   0.033   -8.545  0.47 19.40  ? 203 A1ICF A C03  1 
HETATM 1962 C  C04  . A1ICF E 3 .   ? 0.065   -0.438  -9.872  0.47 15.65  ? 203 A1ICF A C04  1 
HETATM 1963 C  C05  . A1ICF E 3 .   ? -0.171  0.473   -10.921 0.47 18.70  ? 203 A1ICF A C05  1 
HETATM 1964 C  C06  . A1ICF E 3 .   ? -0.315  1.837   -10.652 0.47 16.19  ? 203 A1ICF A C06  1 
HETATM 1965 C  C07  . A1ICF E 3 .   ? 0.414   -0.942  -7.378  0.47 22.47  ? 203 A1ICF A C07  1 
HETATM 1966 N  N09  . A1ICF E 3 .   ? 0.150   -0.047  -5.205  0.47 29.07  ? 203 A1ICF A N09  1 
HETATM 1967 O  O08  . A1ICF E 3 .   ? 1.028   -0.275  -6.296  0.47 25.06  ? 203 A1ICF A O08  1 
HETATM 1968 O  O18  . A1ICF E 3 .   ? 0.492   -0.492  -0.037  0.47 30.29  ? 203 A1ICF A O18  1 
HETATM 1969 O  O19  . A1ICF E 3 .   ? -0.468  0.237   -1.830  0.47 28.79  ? 203 A1ICF A O19  1 
HETATM 1970 CL CL20 . A1ICF E 3 .   ? 0.252   -2.176  -10.253 0.47 21.40  ? 203 A1ICF A CL20 1 
HETATM 1971 C  C1   . GOL   F 4 .   ? 16.715  -6.208  -27.216 1.00 30.84  ? 201 GOL   B C1   1 
HETATM 1972 O  O1   . GOL   F 4 .   ? 17.310  -4.933  -27.099 1.00 52.31  ? 201 GOL   B O1   1 
HETATM 1973 C  C2   . GOL   F 4 .   ? 17.595  -7.254  -26.559 1.00 53.18  ? 201 GOL   B C2   1 
HETATM 1974 O  O2   . GOL   F 4 .   ? 17.228  -7.412  -25.205 1.00 32.89  ? 201 GOL   B O2   1 
HETATM 1975 C  C3   . GOL   F 4 .   ? 17.506  -8.574  -27.312 1.00 45.18  ? 201 GOL   B C3   1 
HETATM 1976 O  O3   . GOL   F 4 .   ? 18.257  -8.445  -28.505 1.00 47.95  ? 201 GOL   B O3   1 
HETATM 1977 C  C10  . A1ICF G 3 .   ? -0.098  -0.602  -27.580 0.43 26.46  ? 202 A1ICF B C10  1 
HETATM 1978 C  C11  . A1ICF G 3 .   ? 0.173   -0.027  -28.994 0.43 35.15  ? 202 A1ICF B C11  1 
HETATM 1979 C  C12  . A1ICF G 3 .   ? 1.197   0.910   -29.113 0.43 34.53  ? 202 A1ICF B C12  1 
HETATM 1980 C  C13  . A1ICF G 3 .   ? 1.514   1.484   -30.364 0.43 38.68  ? 202 A1ICF B C13  1 
HETATM 1981 C  C14  . A1ICF G 3 .   ? 0.777   1.103   -31.512 0.43 36.07  ? 202 A1ICF B C14  1 
HETATM 1982 C  C15  . A1ICF G 3 .   ? -0.252  0.160   -31.400 0.43 36.96  ? 202 A1ICF B C15  1 
HETATM 1983 C  C16  . A1ICF G 3 .   ? -0.579  -0.420  -30.160 0.43 28.70  ? 202 A1ICF B C16  1 
HETATM 1984 C  C17  . A1ICF G 3 .   ? -1.727  -1.434  -30.161 0.43 38.18  ? 202 A1ICF B C17  1 
HETATM 1985 C  C01  . A1ICF G 3 .   ? -0.002  -2.289  -22.407 0.43 13.69  ? 202 A1ICF B C01  1 
HETATM 1986 C  C02  . A1ICF G 3 .   ? 0.091   -1.375  -23.450 0.43 23.54  ? 202 A1ICF B C02  1 
HETATM 1987 C  C03  . A1ICF G 3 .   ? 0.077   0.001   -23.193 0.43 21.29  ? 202 A1ICF B C03  1 
HETATM 1988 C  C04  . A1ICF G 3 .   ? -0.030  0.463   -21.865 0.43 17.45  ? 202 A1ICF B C04  1 
HETATM 1989 C  C05  . A1ICF G 3 .   ? -0.126  -0.461  -20.812 0.43 15.00  ? 202 A1ICF B C05  1 
HETATM 1990 C  C06  . A1ICF G 3 .   ? -0.103  -1.833  -21.076 0.43 15.75  ? 202 A1ICF B C06  1 
HETATM 1991 C  C07  . A1ICF G 3 .   ? 0.177   0.979   -24.380 0.43 25.34  ? 202 A1ICF B C07  1 
HETATM 1992 N  N09  . A1ICF G 3 .   ? 0.478   0.285   -26.579 0.43 30.07  ? 202 A1ICF B N09  1 
HETATM 1993 O  O08  . A1ICF G 3 .   ? -0.437  0.381   -25.503 0.43 26.12  ? 202 A1ICF B O08  1 
HETATM 1994 O  O18  . A1ICF G 3 .   ? -2.160  -1.997  -29.122 0.43 37.54  ? 202 A1ICF B O18  1 
HETATM 1995 O  O19  . A1ICF G 3 .   ? -2.269  -1.718  -31.250 0.43 42.00  ? 202 A1ICF B O19  1 
HETATM 1996 CL CL20 . A1ICF G 3 .   ? -0.059  2.210   -21.494 0.43 21.37  ? 202 A1ICF B CL20 1 
HETATM 1997 O  O    . HOH   H 5 .   ? 9.268   -26.745 3.764   1.00 29.16  ? 301 HOH   A O    1 
HETATM 1998 O  O    . HOH   H 5 .   ? 14.509  -23.349 12.082  1.00 34.34  ? 302 HOH   A O    1 
HETATM 1999 O  O    . HOH   H 5 .   ? 8.843   -32.676 -4.828  1.00 47.02  ? 303 HOH   A O    1 
HETATM 2000 O  O    . HOH   H 5 .   ? -10.611 -15.984 -20.357 1.00 31.10  ? 304 HOH   A O    1 
HETATM 2001 O  O    . HOH   H 5 .   ? 11.224  -23.596 13.897  1.00 38.54  ? 305 HOH   A O    1 
HETATM 2002 O  O    . HOH   H 5 .   ? 1.030   -13.255 2.580   1.00 24.47  ? 306 HOH   A O    1 
HETATM 2003 O  O    . HOH   H 5 .   ? 3.934   -14.416 4.079   1.00 23.01  ? 307 HOH   A O    1 
HETATM 2004 O  O    . HOH   H 5 .   ? 13.291  -27.004 -11.402 1.00 47.73  ? 308 HOH   A O    1 
HETATM 2005 O  O    . HOH   H 5 .   ? 15.728  -13.700 -5.583  1.00 27.49  ? 309 HOH   A O    1 
HETATM 2006 O  O    A HOH   H 5 .   ? -20.572 -11.892 -12.526 0.46 47.86  ? 310 HOH   A O    1 
HETATM 2007 O  O    B HOH   H 5 .   ? -20.704 -11.446 -11.685 0.54 48.39  ? 310 HOH   A O    1 
HETATM 2008 O  O    . HOH   H 5 .   ? 13.671  -16.857 2.848   1.00 34.83  ? 311 HOH   A O    1 
HETATM 2009 O  O    . HOH   H 5 .   ? -16.331 -9.014  -22.187 1.00 42.88  ? 312 HOH   A O    1 
HETATM 2010 O  O    . HOH   H 5 .   ? 15.045  -11.280 -4.965  1.00 23.44  ? 313 HOH   A O    1 
HETATM 2011 O  O    . HOH   H 5 .   ? 7.080   -24.624 12.980  1.00 43.22  ? 314 HOH   A O    1 
HETATM 2012 O  O    . HOH   H 5 .   ? -15.144 -3.370  2.727   1.00 44.27  ? 315 HOH   A O    1 
HETATM 2013 O  O    . HOH   H 5 .   ? -12.168 -20.702 -17.617 1.00 39.93  ? 316 HOH   A O    1 
HETATM 2014 O  O    . HOH   H 5 .   ? -12.672 -2.261  1.629   1.00 37.61  ? 317 HOH   A O    1 
HETATM 2015 O  O    . HOH   H 5 .   ? 14.359  -17.260 5.061   1.00 38.26  ? 318 HOH   A O    1 
HETATM 2016 O  O    . HOH   H 5 .   ? 0.290   -24.182 -11.809 1.00 43.79  ? 319 HOH   A O    1 
HETATM 2017 O  O    . HOH   H 5 .   ? -2.937  -13.623 -17.553 1.00 18.00  ? 320 HOH   A O    1 
HETATM 2018 O  O    . HOH   H 5 .   ? -15.115 -18.167 -20.053 1.00 52.39  ? 321 HOH   A O    1 
HETATM 2019 O  O    . HOH   H 5 .   ? 0.301   -27.696 -9.292  1.00 41.72  ? 322 HOH   A O    1 
HETATM 2020 O  O    . HOH   H 5 .   ? 16.070  -21.204 -8.708  1.00 32.89  ? 323 HOH   A O    1 
HETATM 2021 O  O    A HOH   H 5 .   ? 5.033   -21.795 3.845   0.61 20.36  ? 324 HOH   A O    1 
HETATM 2022 O  O    B HOH   H 5 .   ? 4.125   -22.053 2.900   0.39 17.33  ? 324 HOH   A O    1 
HETATM 2023 O  O    . HOH   H 5 .   ? 8.098   -27.541 6.319   1.00 32.11  ? 325 HOH   A O    1 
HETATM 2024 O  O    . HOH   H 5 .   ? 18.819  -11.642 -6.332  1.00 39.78  ? 326 HOH   A O    1 
HETATM 2025 O  O    . HOH   H 5 .   ? -3.474  -24.258 -4.741  1.00 21.43  ? 327 HOH   A O    1 
HETATM 2026 O  O    . HOH   H 5 .   ? -8.485  -21.066 -16.349 1.00 36.54  ? 328 HOH   A O    1 
HETATM 2027 O  O    . HOH   H 5 .   ? -16.392 3.231   -12.168 1.00 29.47  ? 329 HOH   A O    1 
HETATM 2028 O  O    . HOH   H 5 .   ? 20.187  -6.375  6.276   1.00 53.37  ? 330 HOH   A O    1 
HETATM 2029 O  O    . HOH   H 5 .   ? 13.329  -12.096 -8.794  1.00 20.94  ? 331 HOH   A O    1 
HETATM 2030 O  O    . HOH   H 5 .   ? -3.856  -24.362 -0.484  1.00 27.48  ? 332 HOH   A O    1 
HETATM 2031 O  O    . HOH   H 5 .   ? 17.361  -12.995 -8.382  1.00 51.38  ? 333 HOH   A O    1 
HETATM 2032 O  O    . HOH   H 5 .   ? 16.085  -18.989 -10.786 1.00 29.24  ? 334 HOH   A O    1 
HETATM 2033 O  O    . HOH   H 5 .   ? -14.122 -13.017 -5.228  1.00 36.37  ? 335 HOH   A O    1 
HETATM 2034 O  O    A HOH   H 5 .   ? 11.759  -25.845 11.868  0.78 19.70  ? 336 HOH   A O    1 
HETATM 2035 O  O    . HOH   H 5 .   ? -9.695  -11.734 -15.300 1.00 15.32  ? 337 HOH   A O    1 
HETATM 2036 O  O    . HOH   H 5 .   ? 12.203  -23.597 -7.077  1.00 19.77  ? 338 HOH   A O    1 
HETATM 2037 O  O    . HOH   H 5 .   ? -14.563 -8.386  -26.263 1.00 32.10  ? 339 HOH   A O    1 
HETATM 2038 O  O    . HOH   H 5 .   ? 12.606  -17.233 10.874  1.00 46.32  ? 340 HOH   A O    1 
HETATM 2039 O  O    . HOH   H 5 .   ? 13.584  -24.184 -13.793 1.00 51.47  ? 341 HOH   A O    1 
HETATM 2040 O  O    . HOH   H 5 .   ? -15.007 -13.989 -19.669 1.00 28.60  ? 342 HOH   A O    1 
HETATM 2041 O  O    . HOH   H 5 .   ? 18.368  -10.551 4.236   1.00 36.71  ? 343 HOH   A O    1 
HETATM 2042 O  O    . HOH   H 5 .   ? 17.392  -12.706 -2.579  1.00 23.55  ? 344 HOH   A O    1 
HETATM 2043 O  O    . HOH   H 5 .   ? 7.670   -1.424  -7.623  1.00 15.60  ? 345 HOH   A O    1 
HETATM 2044 O  O    . HOH   H 5 .   ? -20.002 -15.867 -9.837  1.00 55.90  ? 346 HOH   A O    1 
HETATM 2045 O  O    . HOH   H 5 .   ? -8.837  -9.688  -17.033 1.00 13.87  ? 347 HOH   A O    1 
HETATM 2046 O  O    . HOH   H 5 .   ? -6.933  -12.133 4.154   1.00 27.66  ? 348 HOH   A O    1 
HETATM 2047 O  O    . HOH   H 5 .   ? -20.605 -12.120 -21.307 1.00 35.39  ? 349 HOH   A O    1 
HETATM 2048 O  O    . HOH   H 5 .   ? -6.121  -0.883  0.997   1.00 40.05  ? 350 HOH   A O    1 
HETATM 2049 O  O    . HOH   H 5 .   ? -11.557 -14.553 -22.303 1.00 35.04  ? 351 HOH   A O    1 
HETATM 2050 O  O    . HOH   H 5 .   ? 12.077  -30.701 -5.366  1.00 35.13  ? 352 HOH   A O    1 
HETATM 2051 O  O    . HOH   H 5 .   ? 7.589   -22.366 9.411   1.00 28.21  ? 353 HOH   A O    1 
HETATM 2052 O  O    . HOH   H 5 .   ? -4.699  -18.415 3.832   1.00 27.03  ? 354 HOH   A O    1 
HETATM 2053 O  O    . HOH   H 5 .   ? 22.492  -14.613 -6.384  1.00 50.58  ? 355 HOH   A O    1 
HETATM 2054 O  O    A HOH   H 5 .   ? 6.096   -8.515  2.482   0.64 24.63  ? 356 HOH   A O    1 
HETATM 2055 O  O    . HOH   H 5 .   ? -14.401 3.643   -4.530  1.00 21.04  ? 357 HOH   A O    1 
HETATM 2056 O  O    . HOH   H 5 .   ? -20.642 -11.234 -16.922 1.00 36.32  ? 358 HOH   A O    1 
HETATM 2057 O  O    . HOH   H 5 .   ? -8.047  -8.269  -14.297 1.00 13.75  ? 359 HOH   A O    1 
HETATM 2058 O  O    . HOH   H 5 .   ? 4.806   -8.321  -9.985  1.00 20.46  ? 360 HOH   A O    1 
HETATM 2059 O  O    . HOH   H 5 .   ? -18.762 -8.281  -19.444 1.00 29.19  ? 361 HOH   A O    1 
HETATM 2060 O  O    . HOH   H 5 .   ? 15.634  -2.923  1.478   1.00 34.61  ? 362 HOH   A O    1 
HETATM 2061 O  O    . HOH   H 5 .   ? 9.760   -21.048 -14.787 1.00 38.19  ? 363 HOH   A O    1 
HETATM 2062 O  O    . HOH   H 5 .   ? 4.084   -25.153 1.660   1.00 36.38  ? 364 HOH   A O    1 
HETATM 2063 O  O    . HOH   H 5 .   ? -16.825 2.890   -7.354  1.00 36.06  ? 365 HOH   A O    1 
HETATM 2064 O  O    . HOH   H 5 .   ? -10.940 -14.695 -6.903  1.00 16.98  ? 366 HOH   A O    1 
HETATM 2065 O  O    . HOH   H 5 .   ? 14.996  -26.711 -3.455  1.00 19.38  ? 367 HOH   A O    1 
HETATM 2066 O  O    . HOH   H 5 .   ? -13.626 -5.698  -4.294  1.00 22.81  ? 368 HOH   A O    1 
HETATM 2067 O  O    . HOH   H 5 .   ? -15.151 -16.845 -1.073  1.00 37.86  ? 369 HOH   A O    1 
HETATM 2068 O  O    . HOH   H 5 .   ? 12.736  -1.655  -1.463  1.00 26.69  ? 370 HOH   A O    1 
HETATM 2069 O  O    . HOH   H 5 .   ? 13.073  -27.809 -5.172  1.00 38.68  ? 371 HOH   A O    1 
HETATM 2070 O  O    . HOH   H 5 .   ? -15.118 -8.744  -4.530  1.00 28.26  ? 372 HOH   A O    1 
HETATM 2071 O  O    . HOH   H 5 .   ? -3.691  -2.213  -16.225 1.00 27.32  ? 373 HOH   A O    1 
HETATM 2072 O  O    . HOH   H 5 .   ? 12.331  -14.311 3.128   1.00 25.70  ? 374 HOH   A O    1 
HETATM 2073 O  O    A HOH   H 5 .   ? -5.069  -7.725  5.368   0.54 30.26  ? 375 HOH   A O    1 
HETATM 2074 O  O    B HOH   H 5 .   ? -4.933  -9.267  6.110   0.46 30.54  ? 375 HOH   A O    1 
HETATM 2075 O  O    . HOH   H 5 .   ? -6.170  -10.255 -14.632 1.00 27.21  ? 376 HOH   A O    1 
HETATM 2076 O  O    . HOH   H 5 .   ? 16.555  -12.608 7.609   1.00 52.66  ? 377 HOH   A O    1 
HETATM 2077 O  O    . HOH   H 5 .   ? -15.665 -10.406 -6.531  1.00 31.94  ? 378 HOH   A O    1 
HETATM 2078 O  O    . HOH   H 5 .   ? 20.723  -20.881 -6.712  1.00 44.43  ? 379 HOH   A O    1 
HETATM 2079 O  O    . HOH   H 5 .   ? 21.390  -18.898 -3.167  1.00 44.69  ? 380 HOH   A O    1 
HETATM 2080 O  O    . HOH   H 5 .   ? -1.151  -23.422 -3.719  1.00 22.19  ? 381 HOH   A O    1 
HETATM 2081 O  O    . HOH   H 5 .   ? 2.054   -18.563 7.579   1.00 45.29  ? 382 HOH   A O    1 
HETATM 2082 O  O    . HOH   H 5 .   ? 3.259   -28.799 -12.766 1.00 34.00  ? 383 HOH   A O    1 
HETATM 2083 O  O    . HOH   H 5 .   ? -15.294 -19.835 -16.189 1.00 63.68  ? 384 HOH   A O    1 
HETATM 2084 O  O    . HOH   H 5 .   ? 8.190   -15.663 9.381   1.00 36.38  ? 385 HOH   A O    1 
HETATM 2085 O  O    . HOH   H 5 .   ? -4.587  -11.484 5.052   1.00 26.46  ? 386 HOH   A O    1 
HETATM 2086 O  O    . HOH   H 5 .   ? -10.747 -7.857  6.190   1.00 45.45  ? 387 HOH   A O    1 
HETATM 2087 O  O    . HOH   H 5 .   ? -18.882 -13.141 -15.932 1.00 54.31  ? 388 HOH   A O    1 
HETATM 2088 O  O    . HOH   H 5 .   ? -0.786  -20.099 4.139   1.00 41.52  ? 389 HOH   A O    1 
HETATM 2089 O  O    . HOH   H 5 .   ? 8.579   -26.803 -4.753  1.00 23.15  ? 390 HOH   A O    1 
HETATM 2090 O  O    . HOH   H 5 .   ? -16.751 -9.928  -2.416  1.00 43.56  ? 391 HOH   A O    1 
HETATM 2091 O  O    . HOH   H 5 .   ? -11.499 -12.269 3.095   1.00 40.54  ? 392 HOH   A O    1 
HETATM 2092 O  O    . HOH   H 5 .   ? -1.636  -21.710 2.585   1.00 22.49  ? 393 HOH   A O    1 
HETATM 2093 O  O    . HOH   H 5 .   ? 8.188   -5.761  0.418   1.00 23.90  ? 394 HOH   A O    1 
HETATM 2094 O  O    . HOH   H 5 .   ? 10.080  -18.532 10.154  1.00 27.39  ? 395 HOH   A O    1 
HETATM 2095 O  O    . HOH   H 5 .   ? 11.333  -32.821 -7.369  1.00 40.34  ? 396 HOH   A O    1 
HETATM 2096 O  O    . HOH   H 5 .   ? -5.542  -2.419  -14.647 1.00 31.51  ? 397 HOH   A O    1 
HETATM 2097 O  O    . HOH   H 5 .   ? -3.763  -16.200 4.800   1.00 35.17  ? 398 HOH   A O    1 
HETATM 2098 O  O    . HOH   H 5 .   ? -16.444 -16.713 -9.366  1.00 43.44  ? 399 HOH   A O    1 
HETATM 2099 O  O    . HOH   H 5 .   ? 0.239   -25.292 1.032   1.00 42.53  ? 400 HOH   A O    1 
HETATM 2100 O  O    . HOH   H 5 .   ? 17.230  -7.418  -3.310  1.00 42.21  ? 401 HOH   A O    1 
HETATM 2101 O  O    A HOH   H 5 .   ? 2.275   -22.202 3.512   0.50 28.33  ? 402 HOH   A O    1 
HETATM 2102 O  O    B HOH   H 5 .   ? 3.489   -24.037 3.540   0.50 39.71  ? 402 HOH   A O    1 
HETATM 2103 O  O    . HOH   H 5 .   ? -15.724 -1.460  -4.251  1.00 43.74  ? 403 HOH   A O    1 
HETATM 2104 O  O    . HOH   H 5 .   ? 20.857  -11.820 2.564   1.00 37.50  ? 404 HOH   A O    1 
HETATM 2105 O  O    . HOH   H 5 .   ? -14.012 -15.708 -21.417 1.00 45.52  ? 405 HOH   A O    1 
HETATM 2106 O  O    . HOH   H 5 .   ? -8.322  -5.695  6.251   1.00 41.85  ? 406 HOH   A O    1 
HETATM 2107 O  O    . HOH   H 5 .   ? 8.188   -20.654 11.253  1.00 47.62  ? 407 HOH   A O    1 
HETATM 2108 O  O    . HOH   H 5 .   ? -1.225  -24.394 -1.308  1.00 27.28  ? 408 HOH   A O    1 
HETATM 2109 O  O    . HOH   H 5 .   ? -15.773 -18.084 -3.060  1.00 42.81  ? 409 HOH   A O    1 
HETATM 2110 O  O    . HOH   H 5 .   ? -16.642 -18.026 -17.928 1.00 51.44  ? 410 HOH   A O    1 
HETATM 2111 O  O    . HOH   H 5 .   ? -16.444 -6.881  -4.121  1.00 47.86  ? 411 HOH   A O    1 
HETATM 2112 O  O    . HOH   H 5 .   ? -17.207 -7.138  -20.641 1.00 47.35  ? 412 HOH   A O    1 
HETATM 2113 O  O    . HOH   H 5 .   ? 17.768  -16.580 7.008   1.00 29.19  ? 413 HOH   A O    1 
HETATM 2114 O  O    . HOH   H 5 .   ? 14.876  -24.214 -6.984  1.00 39.21  ? 414 HOH   A O    1 
HETATM 2115 O  O    B HOH   H 5 .   ? 12.304  -12.412 5.521   0.87 43.58  ? 415 HOH   A O    1 
HETATM 2116 O  O    . HOH   H 5 .   ? -5.924  -23.051 -8.305  1.00 35.09  ? 416 HOH   A O    1 
HETATM 2117 O  O    . HOH   H 5 .   ? -3.967  -12.872 7.607   1.00 46.44  ? 417 HOH   A O    1 
HETATM 2118 O  O    . HOH   H 5 .   ? 16.370  -5.534  -1.680  1.00 45.30  ? 418 HOH   A O    1 
HETATM 2119 O  O    . HOH   H 5 .   ? 16.598  -17.484 2.599   1.00 31.93  ? 419 HOH   A O    1 
HETATM 2120 O  O    . HOH   H 5 .   ? 1.505   -24.613 -15.335 1.00 54.14  ? 420 HOH   A O    1 
HETATM 2121 O  O    . HOH   H 5 .   ? 1.764   -20.953 6.634   1.00 42.23  ? 421 HOH   A O    1 
HETATM 2122 O  O    . HOH   H 5 .   ? 17.417  -10.355 -4.056  1.00 26.73  ? 422 HOH   A O    1 
HETATM 2123 O  O    . HOH   H 5 .   ? -14.795 -3.383  -2.642  1.00 53.58  ? 423 HOH   A O    1 
HETATM 2124 O  O    . HOH   H 5 .   ? -13.682 -12.291 -23.145 1.00 46.09  ? 424 HOH   A O    1 
HETATM 2125 O  O    . HOH   H 5 .   ? 6.609   -26.029 -2.138  1.00 35.57  ? 425 HOH   A O    1 
HETATM 2126 O  O    . HOH   H 5 .   ? -20.935 -12.746 -14.521 1.00 34.89  ? 426 HOH   A O    1 
HETATM 2127 O  O    . HOH   H 5 .   ? 14.373  -19.078 10.606  1.00 52.97  ? 427 HOH   A O    1 
HETATM 2128 O  O    . HOH   H 5 .   ? -23.156 -12.749 -11.503 1.00 64.61  ? 428 HOH   A O    1 
HETATM 2129 O  O    . HOH   H 5 .   ? -16.395 -15.033 -17.965 1.00 45.26  ? 429 HOH   A O    1 
HETATM 2130 O  O    . HOH   H 5 .   ? -18.046 -3.294  -11.401 1.00 54.17  ? 430 HOH   A O    1 
HETATM 2131 O  O    A HOH   H 5 .   ? 7.259   -2.994  1.746   0.48 33.79  ? 431 HOH   A O    1 
HETATM 2132 O  O    B HOH   H 5 .   ? 5.940   -2.800  0.561   0.52 29.12  ? 431 HOH   A O    1 
HETATM 2133 O  O    B HOH   H 5 .   ? 5.020   -32.922 -1.917  0.92 40.89  ? 432 HOH   A O    1 
HETATM 2134 O  O    . HOH   H 5 .   ? -12.337 -0.074  2.086   1.00 48.55  ? 433 HOH   A O    1 
HETATM 2135 O  O    . HOH   H 5 .   ? 19.150  -14.787 7.977   1.00 51.25  ? 434 HOH   A O    1 
HETATM 2136 O  O    . HOH   H 5 .   ? -7.746  -7.843  7.949   1.00 46.36  ? 435 HOH   A O    1 
HETATM 2137 O  O    . HOH   H 5 .   ? -19.217 -11.208 -23.188 1.00 38.94  ? 436 HOH   A O    1 
HETATM 2138 O  O    A HOH   H 5 .   ? 13.810  -9.944  -6.889  0.59 18.84  ? 437 HOH   A O    1 
HETATM 2139 O  O    B HOH   H 5 .   ? 14.813  -9.906  -7.971  0.41 28.11  ? 437 HOH   A O    1 
HETATM 2140 O  O    . HOH   H 5 .   ? -13.971 -1.290  -0.729  1.00 42.22  ? 438 HOH   A O    1 
HETATM 2141 O  O    . HOH   H 5 .   ? -5.412  -0.511  3.942   1.00 47.57  ? 439 HOH   A O    1 
HETATM 2142 O  O    . HOH   H 5 .   ? -9.008  0.752   1.475   1.00 45.79  ? 440 HOH   A O    1 
HETATM 2143 O  O    . HOH   I 5 .   ? 17.929  -6.890  -30.054 1.00 46.00  ? 301 HOH   B O    1 
HETATM 2144 O  O    . HOH   I 5 .   ? 8.201   -17.857 -20.892 1.00 54.10  ? 302 HOH   B O    1 
HETATM 2145 O  O    A HOH   I 5 .   ? -12.159 -19.410 -33.892 0.50 35.05  ? 303 HOH   B O    1 
HETATM 2146 O  O    B HOH   I 5 .   ? -11.316 -19.440 -35.663 0.50 35.05  ? 303 HOH   B O    1 
HETATM 2147 O  O    . HOH   I 5 .   ? 13.613  -9.129  -34.118 1.00 36.04  ? 304 HOH   B O    1 
HETATM 2148 O  O    . HOH   I 5 .   ? 19.668  -9.030  -15.900 1.00 41.33  ? 305 HOH   B O    1 
HETATM 2149 O  O    . HOH   I 5 .   ? 22.737  -9.366  -18.230 1.00 40.72  ? 306 HOH   B O    1 
HETATM 2150 O  O    . HOH   I 5 .   ? -9.892  -23.499 -43.322 1.00 39.43  ? 307 HOH   B O    1 
HETATM 2151 O  O    . HOH   I 5 .   ? -18.098 -22.618 -27.881 1.00 36.67  ? 308 HOH   B O    1 
HETATM 2152 O  O    . HOH   I 5 .   ? 2.335   -21.649 -16.512 1.00 47.15  ? 309 HOH   B O    1 
HETATM 2153 O  O    . HOH   I 5 .   ? -14.380 -14.718 -33.206 1.00 47.28  ? 310 HOH   B O    1 
HETATM 2154 O  O    . HOH   I 5 .   ? 4.350   -20.861 -15.651 1.00 40.92  ? 311 HOH   B O    1 
HETATM 2155 O  O    A HOH   I 5 .   ? -0.200  -22.966 -34.190 0.50 30.12  ? 312 HOH   B O    1 
HETATM 2156 O  O    B HOH   I 5 .   ? -1.384  -22.825 -35.582 0.50 30.12  ? 312 HOH   B O    1 
HETATM 2157 O  O    . HOH   I 5 .   ? 5.716   -14.944 -37.116 1.00 36.91  ? 313 HOH   B O    1 
HETATM 2158 O  O    . HOH   I 5 .   ? 13.298  -12.876 -24.839 1.00 20.64  ? 314 HOH   B O    1 
HETATM 2159 O  O    . HOH   I 5 .   ? -12.152 -25.794 -27.536 1.00 43.63  ? 315 HOH   B O    1 
HETATM 2160 O  O    . HOH   I 5 .   ? 1.039   -13.203 -34.179 1.00 26.31  ? 316 HOH   B O    1 
HETATM 2161 O  O    . HOH   I 5 .   ? 6.376   -6.574  -37.027 1.00 38.00  ? 317 HOH   B O    1 
HETATM 2162 O  O    . HOH   I 5 .   ? -11.674 -16.252 -31.439 1.00 34.75  ? 318 HOH   B O    1 
HETATM 2163 O  O    . HOH   I 5 .   ? 13.197  -14.103 -11.467 1.00 18.96  ? 319 HOH   B O    1 
HETATM 2164 O  O    . HOH   I 5 .   ? 3.740   -1.625  -15.407 0.59 25.53  ? 320 HOH   B O    1 
HETATM 2165 O  O    . HOH   I 5 .   ? 3.425   -0.284  -16.924 1.00 41.35  ? 321 HOH   B O    1 
HETATM 2166 O  O    . HOH   I 5 .   ? 11.645  -10.163 -16.508 1.00 13.99  ? 322 HOH   B O    1 
HETATM 2167 O  O    . HOH   I 5 .   ? 5.134   -13.040 -14.277 1.00 16.78  ? 323 HOH   B O    1 
HETATM 2168 O  O    . HOH   I 5 .   ? 11.697  -19.769 -15.510 1.00 35.28  ? 324 HOH   B O    1 
HETATM 2169 O  O    . HOH   I 5 .   ? -3.867  -25.622 -40.844 1.00 43.81  ? 325 HOH   B O    1 
HETATM 2170 O  O    . HOH   I 5 .   ? -12.767 -20.922 -20.576 1.00 32.86  ? 326 HOH   B O    1 
HETATM 2171 O  O    . HOH   I 5 .   ? -1.828  -14.897 -35.572 1.00 28.37  ? 327 HOH   B O    1 
HETATM 2172 O  O    . HOH   I 5 .   ? -0.897  -11.638 -37.258 1.00 41.46  ? 328 HOH   B O    1 
HETATM 2173 O  O    . HOH   I 5 .   ? 10.410  -8.268  -14.825 1.00 15.62  ? 329 HOH   B O    1 
HETATM 2174 O  O    . HOH   I 5 .   ? 5.542   -17.622 -35.686 1.00 32.55  ? 330 HOH   B O    1 
HETATM 2175 O  O    . HOH   I 5 .   ? -2.098  -22.216 -38.450 1.00 39.21  ? 331 HOH   B O    1 
HETATM 2176 O  O    . HOH   I 5 .   ? -6.287  -32.330 -25.726 1.00 36.81  ? 332 HOH   B O    1 
HETATM 2177 O  O    . HOH   I 5 .   ? 4.129   -14.979 -15.743 1.00 37.23  ? 333 HOH   B O    1 
HETATM 2178 O  O    . HOH   I 5 .   ? 17.360  -14.934 -11.023 1.00 45.03  ? 334 HOH   B O    1 
HETATM 2179 O  O    . HOH   I 5 .   ? 20.345  -4.218  -12.881 1.00 37.14  ? 335 HOH   B O    1 
HETATM 2180 O  O    A HOH   I 5 .   ? 8.249   -19.081 -22.657 0.81 26.08  ? 336 HOH   B O    1 
HETATM 2181 O  O    . HOH   I 5 .   ? -7.956  -29.004 -25.834 1.00 43.10  ? 337 HOH   B O    1 
HETATM 2182 O  O    . HOH   I 5 .   ? 21.510  -1.277  -21.519 1.00 47.99  ? 338 HOH   B O    1 
HETATM 2183 O  O    . HOH   I 5 .   ? -3.341  -9.009  -22.025 1.00 17.20  ? 339 HOH   B O    1 
HETATM 2184 O  O    . HOH   I 5 .   ? 1.767   -28.364 -19.094 1.00 38.23  ? 340 HOH   B O    1 
HETATM 2185 O  O    . HOH   I 5 .   ? -12.946 -3.404  -30.272 1.00 39.38  ? 341 HOH   B O    1 
HETATM 2186 O  O    . HOH   I 5 .   ? 17.311  -7.801  -35.298 1.00 55.62  ? 342 HOH   B O    1 
HETATM 2187 O  O    . HOH   I 5 .   ? -8.087  -25.189 -24.706 1.00 26.03  ? 343 HOH   B O    1 
HETATM 2188 O  O    . HOH   I 5 .   ? 9.291   -6.932  -17.523 1.00 14.56  ? 344 HOH   B O    1 
HETATM 2189 O  O    . HOH   I 5 .   ? 7.433   -23.473 -26.732 1.00 37.54  ? 345 HOH   B O    1 
HETATM 2190 O  O    . HOH   I 5 .   ? 13.695  5.709   -27.178 1.00 27.97  ? 346 HOH   B O    1 
HETATM 2191 O  O    . HOH   I 5 .   ? -7.328  -2.493  -24.147 1.00 17.60  ? 347 HOH   B O    1 
HETATM 2192 O  O    . HOH   I 5 .   ? 17.325  -11.077 -11.801 1.00 41.60  ? 348 HOH   B O    1 
HETATM 2193 O  O    . HOH   I 5 .   ? -6.908  -6.438  -32.140 1.00 32.24  ? 349 HOH   B O    1 
HETATM 2194 O  O    . HOH   I 5 .   ? -5.939  -16.430 -40.753 1.00 37.54  ? 350 HOH   B O    1 
HETATM 2195 O  O    . HOH   I 5 .   ? 2.143   -22.975 -35.131 1.00 39.93  ? 351 HOH   B O    1 
HETATM 2196 O  O    . HOH   I 5 .   ? 4.583   -27.237 -22.462 1.00 46.91  ? 352 HOH   B O    1 
HETATM 2197 O  O    . HOH   I 5 .   ? 14.366  -3.333  -27.529 1.00 22.64  ? 353 HOH   B O    1 
HETATM 2198 O  O    . HOH   I 5 .   ? 8.618   -11.001 -35.937 1.00 29.74  ? 354 HOH   B O    1 
HETATM 2199 O  O    . HOH   I 5 .   ? -4.107  -23.280 -41.119 1.00 56.13  ? 355 HOH   B O    1 
HETATM 2200 O  O    . HOH   I 5 .   ? 7.880   -9.295  -17.082 1.00 26.64  ? 356 HOH   B O    1 
HETATM 2201 O  O    . HOH   I 5 .   ? -10.413 -10.924 -30.908 1.00 64.33  ? 357 HOH   B O    1 
HETATM 2202 O  O    . HOH   I 5 .   ? 17.592  -4.405  -9.542  1.00 38.89  ? 358 HOH   B O    1 
HETATM 2203 O  O    . HOH   I 5 .   ? 19.691  -12.776 -21.976 1.00 31.64  ? 359 HOH   B O    1 
HETATM 2204 O  O    . HOH   I 5 .   ? 16.959  -15.675 -18.803 1.00 39.74  ? 360 HOH   B O    1 
HETATM 2205 O  O    . HOH   I 5 .   ? -4.824  -28.102 -27.098 1.00 45.33  ? 361 HOH   B O    1 
HETATM 2206 O  O    . HOH   I 5 .   ? -11.468 -18.524 -31.185 1.00 36.01  ? 362 HOH   B O    1 
HETATM 2207 O  O    . HOH   I 5 .   ? -16.394 -20.207 -35.903 1.00 30.64  ? 363 HOH   B O    1 
HETATM 2208 O  O    . HOH   I 5 .   ? 6.186   -10.460 -36.926 1.00 31.39  ? 364 HOH   B O    1 
HETATM 2209 O  O    B HOH   I 5 .   ? 5.946   0.370   -32.469 0.98 46.78  ? 365 HOH   B O    1 
HETATM 2210 O  O    . HOH   I 5 .   ? -12.892 -14.087 -36.443 1.00 60.60  ? 366 HOH   B O    1 
HETATM 2211 O  O    A HOH   I 5 .   ? -1.288  -26.790 -29.585 0.51 27.37  ? 367 HOH   B O    1 
HETATM 2212 O  O    B HOH   I 5 .   ? -1.255  -27.382 -31.803 0.49 45.98  ? 367 HOH   B O    1 
HETATM 2213 O  O    . HOH   I 5 .   ? 15.006  -12.552 -34.366 1.00 53.42  ? 368 HOH   B O    1 
HETATM 2214 O  O    . HOH   I 5 .   ? -0.189  -25.169 -33.843 1.00 40.36  ? 369 HOH   B O    1 
HETATM 2215 O  O    . HOH   I 5 .   ? -7.322  -19.634 -41.812 1.00 29.56  ? 370 HOH   B O    1 
HETATM 2216 O  O    . HOH   I 5 .   ? 9.664   -14.630 -35.273 1.00 32.77  ? 371 HOH   B O    1 
HETATM 2217 O  O    . HOH   I 5 .   ? 0.586   -18.424 -39.439 1.00 42.05  ? 372 HOH   B O    1 
HETATM 2218 O  O    . HOH   I 5 .   ? 5.738   -1.502  -16.982 1.00 28.76  ? 373 HOH   B O    1 
HETATM 2219 O  O    . HOH   I 5 .   ? 15.204  -11.076 -25.532 1.00 28.38  ? 374 HOH   B O    1 
HETATM 2220 O  O    . HOH   I 5 .   ? 4.053   -24.201 -19.937 1.00 46.25  ? 375 HOH   B O    1 
HETATM 2221 O  O    . HOH   I 5 .   ? 15.875  -6.425  -5.394  1.00 35.65  ? 376 HOH   B O    1 
HETATM 2222 O  O    . HOH   I 5 .   ? 12.255  -6.853  -37.628 1.00 26.58  ? 377 HOH   B O    1 
HETATM 2223 O  O    . HOH   I 5 .   ? 16.266  -8.763  -9.269  1.00 36.30  ? 378 HOH   B O    1 
HETATM 2224 O  O    B HOH   I 5 .   ? 11.334  -18.475 -18.065 0.09 26.96  ? 379 HOH   B O    1 
HETATM 2225 O  O    C HOH   I 5 .   ? 10.253  -17.790 -19.601 0.43 30.16  ? 379 HOH   B O    1 
HETATM 2226 O  O    D HOH   I 5 .   ? 10.564  -18.395 -17.902 0.48 27.21  ? 379 HOH   B O    1 
HETATM 2227 O  O    . HOH   I 5 .   ? -5.068  -34.034 -23.677 1.00 36.96  ? 380 HOH   B O    1 
HETATM 2228 O  O    . HOH   I 5 .   ? 16.441  5.131   -19.201 1.00 26.79  ? 381 HOH   B O    1 
HETATM 2229 O  O    . HOH   I 5 .   ? 16.391  5.443   -24.398 1.00 43.55  ? 382 HOH   B O    1 
HETATM 2230 O  O    A HOH   I 5 .   ? 12.745  -14.942 -20.111 0.92 23.79  ? 383 HOH   B O    1 
HETATM 2231 O  O    . HOH   I 5 .   ? -5.893  -21.796 -17.163 1.00 38.19  ? 384 HOH   B O    1 
HETATM 2232 O  O    . HOH   I 5 .   ? 25.159  -3.808  -17.330 1.00 34.13  ? 385 HOH   B O    1 
HETATM 2233 O  O    . HOH   I 5 .   ? -7.462  -4.572  -36.034 1.00 67.75  ? 386 HOH   B O    1 
HETATM 2234 O  O    . HOH   I 5 .   ? 4.126   -18.950 -39.310 1.00 57.49  ? 387 HOH   B O    1 
HETATM 2235 O  O    . HOH   I 5 .   ? -13.303 -23.913 -26.269 1.00 36.09  ? 388 HOH   B O    1 
HETATM 2236 O  O    . HOH   I 5 .   ? 19.313  -15.080 -20.883 1.00 38.63  ? 389 HOH   B O    1 
HETATM 2237 O  O    . HOH   I 5 .   ? 15.808  -19.404 -13.416 1.00 44.25  ? 390 HOH   B O    1 
HETATM 2238 O  O    . HOH   I 5 .   ? -14.542 -3.736  -33.387 1.00 57.00  ? 391 HOH   B O    1 
HETATM 2239 O  O    . HOH   I 5 .   ? 17.923  -11.889 -25.759 1.00 43.09  ? 392 HOH   B O    1 
HETATM 2240 O  O    . HOH   I 5 .   ? -3.322  -14.167 -43.338 1.00 68.14  ? 393 HOH   B O    1 
HETATM 2241 O  O    A HOH   I 5 .   ? 1.339   -31.419 -23.621 0.96 56.21  ? 394 HOH   B O    1 
HETATM 2242 O  O    . HOH   I 5 .   ? 8.930   -4.663  -38.333 1.00 44.28  ? 395 HOH   B O    1 
HETATM 2243 O  O    . HOH   I 5 .   ? -15.618 -18.281 -24.472 1.00 52.31  ? 396 HOH   B O    1 
HETATM 2244 O  O    . HOH   I 5 .   ? -19.297 -18.649 -26.256 1.00 59.32  ? 397 HOH   B O    1 
HETATM 2245 O  O    . HOH   I 5 .   ? 7.014   -8.248  -38.391 1.00 51.69  ? 398 HOH   B O    1 
HETATM 2246 O  O    . HOH   I 5 .   ? 7.206   -23.099 -20.638 1.00 54.95  ? 399 HOH   B O    1 
HETATM 2247 O  O    . HOH   I 5 .   ? -13.555 -22.129 -24.962 1.00 35.44  ? 400 HOH   B O    1 
HETATM 2248 O  O    . HOH   I 5 .   ? -1.782  -24.459 -35.205 1.00 47.09  ? 401 HOH   B O    1 
HETATM 2249 O  O    . HOH   I 5 .   ? 20.658  -1.072  -28.946 1.00 76.29  ? 402 HOH   B O    1 
HETATM 2250 O  O    . HOH   I 5 .   ? -5.775  -21.738 -42.847 1.00 46.64  ? 403 HOH   B O    1 
HETATM 2251 O  O    . HOH   I 5 .   ? -13.777 -17.245 -38.437 1.00 52.68  ? 404 HOH   B O    1 
HETATM 2252 O  O    . HOH   I 5 .   ? -10.746 -26.504 -24.807 1.00 45.71  ? 405 HOH   B O    1 
HETATM 2253 O  O    . HOH   I 5 .   ? 21.527  -2.030  -26.116 1.00 54.22  ? 406 HOH   B O    1 
HETATM 2254 O  O    . HOH   I 5 .   ? 1.220   -11.809 -41.541 1.00 66.73  ? 407 HOH   B O    1 
HETATM 2255 O  O    . HOH   I 5 .   ? 19.971  -5.630  -8.740  1.00 45.20  ? 408 HOH   B O    1 
HETATM 2256 O  O    A HOH   I 5 .   ? 7.829   -21.313 -15.836 0.74 43.39  ? 409 HOH   B O    1 
HETATM 2257 O  O    B HOH   I 5 .   ? 5.674   -20.864 -17.465 0.26 41.73  ? 409 HOH   B O    1 
HETATM 2258 O  O    . HOH   I 5 .   ? 9.814   -21.676 -23.421 1.00 42.24  ? 410 HOH   B O    1 
HETATM 2259 O  O    . HOH   I 5 .   ? 10.621  0.261   -37.127 1.00 53.20  ? 411 HOH   B O    1 
HETATM 2260 O  O    . HOH   I 5 .   ? 4.747   0.464   -15.281 1.00 48.16  ? 412 HOH   B O    1 
HETATM 2261 O  O    . HOH   I 5 .   ? -16.591 -13.477 -22.492 1.00 47.63  ? 413 HOH   B O    1 
HETATM 2262 O  O    . HOH   I 5 .   ? 9.686   1.253   -34.791 1.00 53.18  ? 414 HOH   B O    1 
HETATM 2263 O  O    . HOH   I 5 .   ? 15.856  -13.097 -10.062 1.00 43.79  ? 415 HOH   B O    1 
HETATM 2264 O  O    . HOH   I 5 .   ? 24.911  -4.787  -22.354 1.00 42.32  ? 416 HOH   B O    1 
HETATM 2265 O  O    . HOH   I 5 .   ? 15.871  -0.381  -30.052 1.00 57.19  ? 417 HOH   B O    1 
HETATM 2266 O  O    . HOH   I 5 .   ? -7.261  -36.114 -23.528 1.00 65.14  ? 418 HOH   B O    1 
HETATM 2267 O  O    . HOH   I 5 .   ? 8.175   -13.320 -36.994 1.00 42.96  ? 419 HOH   B O    1 
HETATM 2268 O  O    . HOH   I 5 .   ? -12.391 -23.398 -23.047 1.00 40.19  ? 420 HOH   B O    1 
HETATM 2269 O  O    . HOH   I 5 .   ? 24.368  -1.160  -17.709 1.00 39.07  ? 421 HOH   B O    1 
HETATM 2270 O  O    . HOH   I 5 .   ? 12.930  -9.176  -36.913 1.00 30.38  ? 422 HOH   B O    1 
HETATM 2271 O  O    . HOH   I 5 .   ? 10.311  -6.808  -39.514 1.00 47.04  ? 423 HOH   B O    1 
HETATM 2272 O  O    . HOH   I 5 .   ? 10.731  -10.422 -37.554 1.00 40.17  ? 424 HOH   B O    1 
HETATM 2273 O  O    . HOH   I 5 .   ? 19.052  -11.849 -13.931 1.00 37.91  ? 425 HOH   B O    1 
HETATM 2274 O  O    . HOH   I 5 .   ? 26.375  -2.498  -15.536 1.00 40.52  ? 426 HOH   B O    1 
HETATM 2275 O  O    . HOH   I 5 .   ? 8.959   -9.066  -39.552 1.00 40.21  ? 427 HOH   B O    1 
HETATM 2276 O  O    . HOH   I 5 .   ? 25.343  -0.214  -15.961 1.00 41.44  ? 428 HOH   B O    1 
# 
