data_8U52
# 
_entry.id   8U52 
# 
_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   8U52         pdb_00008u52 10.2210/pdb8u52/pdb 
WWPDB D_1000277369 ?            ?                   
# 
loop_
_pdbx_audit_revision_history.ordinal 
_pdbx_audit_revision_history.data_content_type 
_pdbx_audit_revision_history.major_revision 
_pdbx_audit_revision_history.minor_revision 
_pdbx_audit_revision_history.revision_date 
_pdbx_audit_revision_history.part_number 
1 'Structure model' 1 0 2025-03-05 ? 
2 'Structure model' 1 1 2025-05-28 ? 
# 
_pdbx_audit_revision_details.ordinal             1 
_pdbx_audit_revision_details.revision_ordinal    1 
_pdbx_audit_revision_details.data_content_type   'Structure model' 
_pdbx_audit_revision_details.provider            repository 
_pdbx_audit_revision_details.type                'Initial release' 
_pdbx_audit_revision_details.description         ? 
_pdbx_audit_revision_details.details             ? 
# 
_pdbx_audit_revision_group.ordinal             1 
_pdbx_audit_revision_group.revision_ordinal    2 
_pdbx_audit_revision_group.data_content_type   'Structure model' 
_pdbx_audit_revision_group.group               'Database references' 
# 
_pdbx_audit_revision_category.ordinal             1 
_pdbx_audit_revision_category.revision_ordinal    2 
_pdbx_audit_revision_category.data_content_type   'Structure model' 
_pdbx_audit_revision_category.category            citation 
# 
loop_
_pdbx_audit_revision_item.ordinal 
_pdbx_audit_revision_item.revision_ordinal 
_pdbx_audit_revision_item.data_content_type 
_pdbx_audit_revision_item.item 
1 2 'Structure model' '_citation.journal_volume' 
2 2 'Structure model' '_citation.page_first'     
3 2 'Structure model' '_citation.page_last'      
# 
_pdbx_database_status.status_code                     REL 
_pdbx_database_status.status_code_sf                  REL 
_pdbx_database_status.status_code_mr                  ? 
_pdbx_database_status.entry_id                        8U52 
_pdbx_database_status.recvd_initial_deposition_date   2023-09-11 
_pdbx_database_status.SG_entry                        N 
_pdbx_database_status.deposit_site                    RCSB 
_pdbx_database_status.process_site                    RCSB 
_pdbx_database_status.status_code_cs                  ? 
_pdbx_database_status.status_code_nmr_data            ? 
_pdbx_database_status.methods_development_category    ? 
_pdbx_database_status.pdb_format_compatible           Y 
# 
_pdbx_database_related.db_name        PDB 
_pdbx_database_related.details        '3HJ0 contains the same protein covalently complexed with a close ligand analogue.' 
_pdbx_database_related.db_id          3HJ0 
_pdbx_database_related.content_type   unspecified 
# 
_pdbx_contact_author.id                 2 
_pdbx_contact_author.email              jkelly@scripps.edu 
_pdbx_contact_author.name_first         Jeffery 
_pdbx_contact_author.name_last          Kelly 
_pdbx_contact_author.name_mi            ? 
_pdbx_contact_author.role               'principal investigator/group leader' 
_pdbx_contact_author.identifier_ORCID   0000-0001-8943-3395 
# 
loop_
_audit_author.name 
_audit_author.pdbx_ordinal 
_audit_author.identifier_ORCID 
'Yan, N.L.'    1 ? 
'Nugroho, K.'  2 ? 
'Kline, G.M.'  3 ? 
'Basanta, B.'  4 ? 
'Lander, G.C.' 5 ? 
'Wilson, I.A.' 6 ? 
'Kelly, J.W.'  7 ? 
# 
_citation.abstract                  ? 
_citation.abstract_id_CAS           ? 
_citation.book_id_ISBN              ? 
_citation.book_publisher            ? 
_citation.book_publisher_city       ? 
_citation.book_title                ? 
_citation.coordinate_linkage        ? 
_citation.country                   US 
_citation.database_id_Medline       ? 
_citation.details                   ? 
_citation.id                        primary 
_citation.journal_abbrev            Nat.Struct.Mol.Biol. 
_citation.journal_id_ASTM           ? 
_citation.journal_id_CSD            ? 
_citation.journal_id_ISSN           1545-9985 
_citation.journal_full              ? 
_citation.journal_issue             ? 
_citation.journal_volume            32 
_citation.language                  ? 
_citation.page_first                876 
_citation.page_last                 883 
_citation.title                     'The conformational landscape of human transthyretin revealed by cryo-EM.' 
_citation.year                      2025 
_citation.database_id_CSD           ? 
_citation.pdbx_database_id_DOI      10.1038/s41594-024-01472-7 
_citation.pdbx_database_id_PubMed   39843982 
_citation.pdbx_database_id_patent   ? 
_citation.unpublished_flag          ? 
# 
loop_
_citation_author.citation_id 
_citation_author.name 
_citation_author.ordinal 
_citation_author.identifier_ORCID 
primary 'Basanta, B.'       1  ?                   
primary 'Nugroho, K.'       2  ?                   
primary 'Yan, N.L.'         3  ?                   
primary 'Kline, G.M.'       4  ?                   
primary 'Powers, E.T.'      5  0000-0001-8185-8487 
primary 'Tsai, F.J.'        6  ?                   
primary 'Wu, M.'            7  ?                   
primary 'Hansel-Harris, A.' 8  0000-0001-7064-1119 
primary 'Chen, J.S.'        9  ?                   
primary 'Forli, S.'         10 0000-0002-5964-7111 
primary 'Kelly, J.W.'       11 0000-0001-8943-3395 
primary 'Lander, G.C.'      12 0000-0003-4921-1135 
# 
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 'S-(4-fluorophenyl) 3-(dimethylamino)-5-[(E)-2-(4-hydroxy-3,5-dimethylphenyl)ethenyl]benzenecarbothioate' 
421.527   2   ? ? ? ? 
3 water       nat water                                                                                                     18.015 
164 ? ? ? ? 
# 
_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 'S-(4-fluorophenyl) 3-(dimethylamino)-5-[(E)-2-(4-hydroxy-3,5-dimethylphenyl)ethenyl]benzenecarbothioate' 1W4 
3 water                                                                                                     HOH 
# 
loop_
_entity_poly_seq.entity_id 
_entity_poly_seq.num 
_entity_poly_seq.mon_id 
_entity_poly_seq.hetero 
1 1   GLY n 
1 2   PRO n 
1 3   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 
1W4 non-polymer         . 
'S-(4-fluorophenyl) 3-(dimethylamino)-5-[(E)-2-(4-hydroxy-3,5-dimethylphenyl)ethenyl]benzenecarbothioate' ? 'C25 H24 F N O2 S' 
421.527 
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 
GLU 'L-peptide linking' y 'GLUTAMIC ACID' ? 'C5 H9 N O4'       147.129 
GLY 'peptide linking'   y GLYCINE ? 'C2 H5 N O2'       75.067  
HIS 'L-peptide linking' y HISTIDINE ? 'C6 H10 N3 O2 1'   156.162 
HOH non-polymer         . WATER ? 'H2 O'             18.015  
ILE 'L-peptide linking' y ISOLEUCINE ? 'C6 H13 N O2'      131.173 
LEU 'L-peptide linking' y LEUCINE ? 'C6 H13 N O2'      131.173 
LYS 'L-peptide linking' y LYSINE ? 'C6 H15 N2 O2 1'   147.195 
MET 'L-peptide linking' y METHIONINE ? 'C5 H11 N O2 S'    149.211 
PHE 'L-peptide linking' y PHENYLALANINE ? 'C9 H11 N O2'      165.189 
PRO 'L-peptide linking' y PROLINE ? 'C5 H9 N O2'       115.130 
SER 'L-peptide linking' y SERINE ? 'C3 H7 N O3'       105.093 
THR 'L-peptide linking' y THREONINE ? 'C4 H9 N O3'       119.119 
TRP 'L-peptide linking' y TRYPTOPHAN ? 'C11 H12 N2 O2'    204.225 
TYR 'L-peptide linking' y TYROSINE ? 'C9 H11 N O3'      181.189 
VAL 'L-peptide linking' y VALINE ? 'C5 H11 N O2'      117.146 
# 
loop_
_pdbx_poly_seq_scheme.asym_id 
_pdbx_poly_seq_scheme.entity_id 
_pdbx_poly_seq_scheme.seq_id 
_pdbx_poly_seq_scheme.mon_id 
_pdbx_poly_seq_scheme.ndb_seq_num 
_pdbx_poly_seq_scheme.pdb_seq_num 
_pdbx_poly_seq_scheme.auth_seq_num 
_pdbx_poly_seq_scheme.pdb_mon_id 
_pdbx_poly_seq_scheme.auth_mon_id 
_pdbx_poly_seq_scheme.pdb_strand_id 
_pdbx_poly_seq_scheme.pdb_ins_code 
_pdbx_poly_seq_scheme.hetero 
A 1 1   GLY 1   1   ?   ?   ?   A . n 
A 1 2   PRO 2   2   ?   ?   ?   A . n 
A 1 3   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   ?   ?   ?   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 ?   ?   ?   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   ?   ?   ?   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 ?   ?   ?   B . n 
B 1 126 LYS 126 126 ?   ?   ?   B . n 
B 1 127 GLU 127 127 ?   ?   ?   B . n 
# 
_pdbx_entity_instance_feature.ordinal        1 
_pdbx_entity_instance_feature.comp_id        1W4 
_pdbx_entity_instance_feature.asym_id        ? 
_pdbx_entity_instance_feature.seq_num        ? 
_pdbx_entity_instance_feature.auth_comp_id   1W4 
_pdbx_entity_instance_feature.auth_asym_id   ? 
_pdbx_entity_instance_feature.auth_seq_num   ? 
_pdbx_entity_instance_feature.feature_type   'SUBJECT OF INVESTIGATION' 
_pdbx_entity_instance_feature.details        ? 
# 
loop_
_pdbx_nonpoly_scheme.asym_id 
_pdbx_nonpoly_scheme.entity_id 
_pdbx_nonpoly_scheme.mon_id 
_pdbx_nonpoly_scheme.ndb_seq_num 
_pdbx_nonpoly_scheme.pdb_seq_num 
_pdbx_nonpoly_scheme.auth_seq_num 
_pdbx_nonpoly_scheme.pdb_mon_id 
_pdbx_nonpoly_scheme.auth_mon_id 
_pdbx_nonpoly_scheme.pdb_strand_id 
_pdbx_nonpoly_scheme.pdb_ins_code 
C 2 1W4 1  201 201 1W4 TA2 A . 
D 2 1W4 1  201 201 1W4 TA2 B . 
E 3 HOH 1  301 128 HOH HOH A . 
E 3 HOH 2  302 164 HOH HOH A . 
E 3 HOH 3  303 106 HOH HOH A . 
E 3 HOH 4  304 130 HOH HOH A . 
E 3 HOH 5  305 105 HOH HOH A . 
E 3 HOH 6  306 120 HOH HOH A . 
E 3 HOH 7  307 78  HOH HOH A . 
E 3 HOH 8  308 24  HOH HOH A . 
E 3 HOH 9  309 158 HOH HOH A . 
E 3 HOH 10 310 109 HOH HOH A . 
E 3 HOH 11 311 143 HOH HOH A . 
E 3 HOH 12 312 37  HOH HOH A . 
E 3 HOH 13 313 151 HOH HOH A . 
E 3 HOH 14 314 104 HOH HOH A . 
E 3 HOH 15 315 102 HOH HOH A . 
E 3 HOH 16 316 101 HOH HOH A . 
E 3 HOH 17 317 122 HOH HOH A . 
E 3 HOH 18 318 157 HOH HOH A . 
E 3 HOH 19 319 12  HOH HOH A . 
E 3 HOH 20 320 29  HOH HOH A . 
E 3 HOH 21 321 134 HOH HOH A . 
E 3 HOH 22 322 30  HOH HOH A . 
E 3 HOH 23 323 40  HOH HOH A . 
E 3 HOH 24 324 96  HOH HOH A . 
E 3 HOH 25 325 57  HOH HOH A . 
E 3 HOH 26 326 135 HOH HOH A . 
E 3 HOH 27 327 75  HOH HOH A . 
E 3 HOH 28 328 118 HOH HOH A . 
E 3 HOH 29 329 129 HOH HOH A . 
E 3 HOH 30 330 63  HOH HOH A . 
E 3 HOH 31 331 36  HOH HOH A . 
E 3 HOH 32 332 42  HOH HOH A . 
E 3 HOH 33 333 26  HOH HOH A . 
E 3 HOH 34 334 88  HOH HOH A . 
E 3 HOH 35 335 85  HOH HOH A . 
E 3 HOH 36 336 10  HOH HOH A . 
E 3 HOH 37 337 65  HOH HOH A . 
E 3 HOH 38 338 3   HOH HOH A . 
E 3 HOH 39 339 41  HOH HOH A . 
E 3 HOH 40 340 149 HOH HOH A . 
E 3 HOH 41 341 9   HOH HOH A . 
E 3 HOH 42 342 58  HOH HOH A . 
E 3 HOH 43 343 19  HOH HOH A . 
E 3 HOH 44 344 71  HOH HOH A . 
E 3 HOH 45 345 14  HOH HOH A . 
E 3 HOH 46 346 25  HOH HOH A . 
E 3 HOH 47 347 22  HOH HOH A . 
E 3 HOH 48 348 67  HOH HOH A . 
E 3 HOH 49 349 68  HOH HOH A . 
E 3 HOH 50 350 17  HOH HOH A . 
E 3 HOH 51 351 112 HOH HOH A . 
E 3 HOH 52 352 2   HOH HOH A . 
E 3 HOH 53 353 43  HOH HOH A . 
E 3 HOH 54 354 27  HOH HOH A . 
E 3 HOH 55 355 66  HOH HOH A . 
E 3 HOH 56 356 32  HOH HOH A . 
E 3 HOH 57 357 79  HOH HOH A . 
E 3 HOH 58 358 95  HOH HOH A . 
E 3 HOH 59 359 20  HOH HOH A . 
E 3 HOH 60 360 38  HOH HOH A . 
E 3 HOH 61 361 145 HOH HOH A . 
E 3 HOH 62 362 92  HOH HOH A . 
E 3 HOH 63 363 115 HOH HOH A . 
E 3 HOH 64 364 87  HOH HOH A . 
E 3 HOH 65 365 86  HOH HOH A . 
E 3 HOH 66 366 54  HOH HOH A . 
E 3 HOH 67 367 74  HOH HOH A . 
E 3 HOH 68 368 146 HOH HOH A . 
E 3 HOH 69 369 28  HOH HOH A . 
E 3 HOH 70 370 69  HOH HOH A . 
E 3 HOH 71 371 98  HOH HOH A . 
E 3 HOH 72 372 97  HOH HOH A . 
E 3 HOH 73 373 55  HOH HOH A . 
E 3 HOH 74 374 160 HOH HOH A . 
E 3 HOH 75 375 76  HOH HOH A . 
E 3 HOH 76 376 116 HOH HOH A . 
E 3 HOH 77 377 45  HOH HOH A . 
E 3 HOH 78 378 142 HOH HOH A . 
E 3 HOH 79 379 107 HOH HOH A . 
E 3 HOH 80 380 62  HOH HOH A . 
E 3 HOH 81 381 53  HOH HOH A . 
E 3 HOH 82 382 47  HOH HOH A . 
E 3 HOH 83 383 152 HOH HOH A . 
E 3 HOH 84 384 99  HOH HOH A . 
E 3 HOH 85 385 108 HOH HOH A . 
E 3 HOH 86 386 23  HOH HOH A . 
E 3 HOH 87 387 100 HOH HOH A . 
E 3 HOH 88 388 156 HOH HOH A . 
E 3 HOH 89 389 49  HOH HOH A . 
E 3 HOH 90 390 125 HOH HOH A . 
E 3 HOH 91 391 138 HOH HOH A . 
E 3 HOH 92 392 127 HOH HOH A . 
F 3 HOH 1  301 131 HOH HOH B . 
F 3 HOH 2  302 163 HOH HOH B . 
F 3 HOH 3  303 89  HOH HOH B . 
F 3 HOH 4  304 154 HOH HOH B . 
F 3 HOH 5  305 59  HOH HOH B . 
F 3 HOH 6  306 48  HOH HOH B . 
F 3 HOH 7  307 155 HOH HOH B . 
F 3 HOH 8  308 84  HOH HOH B . 
F 3 HOH 9  309 4   HOH HOH B . 
F 3 HOH 10 310 123 HOH HOH B . 
F 3 HOH 11 311 31  HOH HOH B . 
F 3 HOH 12 312 141 HOH HOH B . 
F 3 HOH 13 313 93  HOH HOH B . 
F 3 HOH 14 314 114 HOH HOH B . 
F 3 HOH 15 315 13  HOH HOH B . 
F 3 HOH 16 316 73  HOH HOH B . 
F 3 HOH 17 317 140 HOH HOH B . 
F 3 HOH 18 318 81  HOH HOH B . 
F 3 HOH 19 319 126 HOH HOH B . 
F 3 HOH 20 320 18  HOH HOH B . 
F 3 HOH 21 321 103 HOH HOH B . 
F 3 HOH 22 322 35  HOH HOH B . 
F 3 HOH 23 323 159 HOH HOH B . 
F 3 HOH 24 324 16  HOH HOH B . 
F 3 HOH 25 325 91  HOH HOH B . 
F 3 HOH 26 326 52  HOH HOH B . 
F 3 HOH 27 327 56  HOH HOH B . 
F 3 HOH 28 328 64  HOH HOH B . 
F 3 HOH 29 329 1   HOH HOH B . 
F 3 HOH 30 330 39  HOH HOH B . 
F 3 HOH 31 331 33  HOH HOH B . 
F 3 HOH 32 332 15  HOH HOH B . 
F 3 HOH 33 333 70  HOH HOH B . 
F 3 HOH 34 334 11  HOH HOH B . 
F 3 HOH 35 335 44  HOH HOH B . 
F 3 HOH 36 336 136 HOH HOH B . 
F 3 HOH 37 337 119 HOH HOH B . 
F 3 HOH 38 338 5   HOH HOH B . 
F 3 HOH 39 339 82  HOH HOH B . 
F 3 HOH 40 340 60  HOH HOH B . 
F 3 HOH 41 341 77  HOH HOH B . 
F 3 HOH 42 342 162 HOH HOH B . 
F 3 HOH 43 343 110 HOH HOH B . 
F 3 HOH 44 344 137 HOH HOH B . 
F 3 HOH 45 345 139 HOH HOH B . 
F 3 HOH 46 346 148 HOH HOH B . 
F 3 HOH 47 347 6   HOH HOH B . 
F 3 HOH 48 348 111 HOH HOH B . 
F 3 HOH 49 349 147 HOH HOH B . 
F 3 HOH 50 350 51  HOH HOH B . 
F 3 HOH 51 351 8   HOH HOH B . 
F 3 HOH 52 352 21  HOH HOH B . 
F 3 HOH 53 353 117 HOH HOH B . 
F 3 HOH 54 354 7   HOH HOH B . 
F 3 HOH 55 355 150 HOH HOH B . 
F 3 HOH 56 356 50  HOH HOH B . 
F 3 HOH 57 357 46  HOH HOH B . 
F 3 HOH 58 358 144 HOH HOH B . 
F 3 HOH 59 359 34  HOH HOH B . 
F 3 HOH 60 360 132 HOH HOH B . 
F 3 HOH 61 361 113 HOH HOH B . 
F 3 HOH 62 362 90  HOH HOH B . 
F 3 HOH 63 363 94  HOH HOH B . 
F 3 HOH 64 364 124 HOH HOH B . 
F 3 HOH 65 365 161 HOH HOH B . 
F 3 HOH 66 366 72  HOH HOH B . 
F 3 HOH 67 367 83  HOH HOH B . 
F 3 HOH 68 368 61  HOH HOH B . 
F 3 HOH 69 369 121 HOH HOH B . 
F 3 HOH 70 370 80  HOH HOH B . 
F 3 HOH 71 371 133 HOH HOH B . 
F 3 HOH 72 372 153 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       ? ? ? ? ? ? ? ? ? ? ? REFMAC ? ? ? 5.8.0238 1 
? 'data reduction' ? ? ? ? ? ? ? ? ? ? ? XDS    ? ? ? .        2 
? 'data scaling'   ? ? ? ? ? ? ? ? ? ? ? SCALA  ? ? ? .        3 
? phasing          ? ? ? ? ? ? ? ? ? ? ? PHASER ? ? ? .        4 
# 
_cell.angle_alpha                  90.00 
_cell.angle_alpha_esd              ? 
_cell.angle_beta                   90.00 
_cell.angle_beta_esd               ? 
_cell.angle_gamma                  90.00 
_cell.angle_gamma_esd              ? 
_cell.entry_id                     8U52 
_cell.details                      ? 
_cell.formula_units_Z              ? 
_cell.length_a                     42.960 
_cell.length_a_esd                 ? 
_cell.length_b                     85.201 
_cell.length_b_esd                 ? 
_cell.length_c                     63.751 
_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                         8U52 
_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                   8U52 
_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             2.12 
_exptl_crystal.density_method               ? 
_exptl_crystal.density_percent_sol          41.90 
_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    
;The WT-TTR was concentrated to 4 mg/mL in 10 mM sodium phosphate, 100 mM KCl, at pH 7.6 and co-crystallized at room temperature using the vapor diffusion sitting drop method.
;
_exptl_crystal_grow.pdbx_pH_range   ? 
_exptl_crystal_grow.temp            298 
# 
_diffrn.ambient_environment              ? 
_diffrn.ambient_temp                     100 
_diffrn.ambient_temp_details             ? 
_diffrn.ambient_temp_esd                 ? 
_diffrn.crystal_id                       1 
_diffrn.crystal_support                  ? 
_diffrn.crystal_treatment                ? 
_diffrn.details                          ? 
_diffrn.id                               1 
_diffrn.ambient_pressure                 ? 
_diffrn.ambient_pressure_esd             ? 
_diffrn.ambient_pressure_gt              ? 
_diffrn.ambient_pressure_lt              ? 
_diffrn.ambient_temp_gt                  ? 
_diffrn.ambient_temp_lt                  ? 
_diffrn.pdbx_serial_crystal_experiment   N 
# 
_diffrn_detector.details                      ? 
_diffrn_detector.detector                     PIXEL 
_diffrn_detector.diffrn_id                    1 
_diffrn_detector.type                         'DECTRIS PILATUS3 2M' 
_diffrn_detector.area_resol_mean              ? 
_diffrn_detector.dtime                        ? 
_diffrn_detector.pdbx_frames_total            ? 
_diffrn_detector.pdbx_collection_time_total   ? 
_diffrn_detector.pdbx_collection_date         2021-12-20 
_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   0.97741 
_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                        'ALS BEAMLINE 5.0.1' 
_diffrn_source.voltage                     ? 
_diffrn_source.take-off_angle              ? 
_diffrn_source.pdbx_wavelength_list        0.97741 
_diffrn_source.pdbx_wavelength             ? 
_diffrn_source.pdbx_synchrotron_beamline   5.0.1 
_diffrn_source.pdbx_synchrotron_site       ALS 
# 
_reflns.B_iso_Wilson_estimate                          16 
_reflns.entry_id                                       8U52 
_reflns.data_reduction_details                         ? 
_reflns.data_reduction_method                          ? 
_reflns.d_resolution_high                              1.50 
_reflns.d_resolution_low                               42.64 
_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                                     36591 
_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                           95.7 
_reflns.R_free_details                                 ? 
_reflns.Rmerge_F_all                                   ? 
_reflns.Rmerge_F_obs                                   ? 
_reflns.Friedel_coverage                               ? 
_reflns.number_gt                                      ? 
_reflns.threshold_expression                           ? 
_reflns.pdbx_redundancy                                12.4 
_reflns.pdbx_netI_over_av_sigmaI                       ? 
_reflns.pdbx_netI_over_sigmaI                          42.8 
_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                                0.008 
_reflns.pdbx_d_opt                                     ? 
_reflns.pdbx_number_measured_all                       ? 
_reflns.pdbx_diffrn_id                                 1 
_reflns.pdbx_ordinal                                   1 
_reflns.pdbx_CC_half                                   1.00 
_reflns.pdbx_CC_star                                   ? 
_reflns.pdbx_R_split                                   ? 
_reflns.pdbx_Rmerge_I_obs                              ? 
_reflns.pdbx_Rmerge_I_all                              ? 
_reflns.pdbx_Rsym_value                                0.029 
_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                                    1.50 
_reflns_shell.d_res_low                                     1.58 
_reflns_shell.meanI_over_sigI_all                           ? 
_reflns_shell.meanI_over_sigI_obs                           4.9 
_reflns_shell.number_measured_all                           ? 
_reflns_shell.number_measured_obs                           ? 
_reflns_shell.number_possible                               ? 
_reflns_shell.number_unique_all                             ? 
_reflns_shell.number_unique_obs                             4326 
_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                               0.136 
_reflns_shell.pdbx_rejects                                  ? 
_reflns_shell.pdbx_ordinal                                  1 
_reflns_shell.pdbx_diffrn_id                                1 
_reflns_shell.pdbx_CC_half                                  0.94 
_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                               0.411 
_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]                            0.65 
_refine.aniso_B[1][2]                            0.00 
_refine.aniso_B[1][3]                            -0.00 
_refine.aniso_B[2][2]                            -0.69 
_refine.aniso_B[2][3]                            0.00 
_refine.aniso_B[3][3]                            0.04 
_refine.B_iso_max                                ? 
_refine.B_iso_mean                               22.971 
_refine.B_iso_min                                ? 
_refine.correlation_coeff_Fo_to_Fc               0.970 
_refine.correlation_coeff_Fo_to_Fc_free          0.963 
_refine.details                                  'HYDROGENS HAVE BEEN ADDED IN THE RIDING POSITIONS' 
_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                                 8U52 
_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                            1.50 
_refine.ls_d_res_low                             42.64 
_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                     34712 
_refine.ls_number_reflns_R_free                  1844 
_refine.ls_number_reflns_R_work                  ? 
_refine.ls_number_restraints                     ? 
_refine.ls_percent_reflns_obs                    95.49 
_refine.ls_percent_reflns_R_free                 5.0 
_refine.ls_R_factor_all                          ? 
_refine.ls_R_factor_obs                          0.16629 
_refine.ls_R_factor_R_free                       0.19389 
_refine.ls_R_factor_R_free_error                 ? 
_refine.ls_R_factor_R_free_error_details         ? 
_refine.ls_R_factor_R_work                       0.16483 
_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                    MASK 
_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               THROUGHOUT 
_refine.pdbx_method_to_determine_struct          'MOLECULAR REPLACEMENT' 
_refine.pdbx_starting_model                      ? 
_refine.pdbx_stereochemistry_target_values       'MAXIMUM LIKELIHOOD' 
_refine.pdbx_R_Free_selection_details            RANDOM 
_refine.pdbx_stereochem_target_val_spec_case     ? 
_refine.pdbx_overall_ESU_R                       0.071 
_refine.pdbx_overall_ESU_R_Free                  0.073 
_refine.pdbx_solvent_vdw_probe_radii             1.20 
_refine.pdbx_solvent_ion_probe_radii             0.80 
_refine.pdbx_solvent_shrinkage_radii             0.80 
_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                             1.202 
_refine.overall_SU_ML                            0.045 
_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                         1 
_refine_hist.details                          ? 
_refine_hist.d_res_high                       1.50 
_refine_hist.d_res_low                        42.64 
_refine_hist.number_atoms_solvent             164 
_refine_hist.number_atoms_total               1986 
_refine_hist.number_reflns_all                ? 
_refine_hist.number_reflns_obs                ? 
_refine_hist.number_reflns_R_free             ? 
_refine_hist.number_reflns_R_work             ? 
_refine_hist.R_factor_all                     ? 
_refine_hist.R_factor_obs                     ? 
_refine_hist.R_factor_R_free                  ? 
_refine_hist.R_factor_R_work                  ? 
_refine_hist.pdbx_number_residues_total       ? 
_refine_hist.pdbx_B_iso_mean_ligand           ? 
_refine_hist.pdbx_B_iso_mean_solvent          ? 
_refine_hist.pdbx_number_atoms_protein        1778 
_refine_hist.pdbx_number_atoms_nucleic_acid   0 
_refine_hist.pdbx_number_atoms_ligand         44 
_refine_hist.pdbx_number_atoms_lipid          ? 
_refine_hist.pdbx_number_atoms_carb           ? 
_refine_hist.pdbx_pseudo_atom_details         ? 
# 
loop_
_refine_ls_restr.pdbx_refine_id 
_refine_ls_restr.criterion 
_refine_ls_restr.dev_ideal 
_refine_ls_restr.dev_ideal_target 
_refine_ls_restr.number 
_refine_ls_restr.rejects 
_refine_ls_restr.type 
_refine_ls_restr.weight 
_refine_ls_restr.pdbx_restraint_function 
'X-RAY DIFFRACTION' ? 0.046  0.013  1933 ? r_bond_refined_d             ? ? 
'X-RAY DIFFRACTION' ? 0.004  0.017  1741 ? r_bond_other_d               ? ? 
'X-RAY DIFFRACTION' ? 2.890  1.682  2657 ? r_angle_refined_deg          ? ? 
'X-RAY DIFFRACTION' ? 1.604  1.594  4047 ? r_angle_other_deg            ? ? 
'X-RAY DIFFRACTION' ? 14.783 5.179  252  ? r_dihedral_angle_1_deg       ? ? 
'X-RAY DIFFRACTION' ? 32.671 22.759 87   ? r_dihedral_angle_2_deg       ? ? 
'X-RAY DIFFRACTION' ? 15.498 15.000 295  ? r_dihedral_angle_3_deg       ? ? 
'X-RAY DIFFRACTION' ? 14.571 15.000 8    ? r_dihedral_angle_4_deg       ? ? 
'X-RAY DIFFRACTION' ? 0.104  0.200  257  ? r_chiral_restr               ? ? 
'X-RAY DIFFRACTION' ? 0.013  0.020  2410 ? r_gen_planes_refined         ? ? 
'X-RAY DIFFRACTION' ? 0.008  0.020  420  ? r_gen_planes_other           ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?    ? r_nbd_refined                ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?    ? r_nbd_other                  ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?    ? r_nbtor_refined              ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?    ? r_nbtor_other                ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?    ? r_xyhbond_nbd_refined        ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?    ? r_xyhbond_nbd_other          ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?    ? r_metal_ion_refined          ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?    ? r_metal_ion_other            ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?    ? r_symmetry_vdw_refined       ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?    ? r_symmetry_vdw_other         ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?    ? r_symmetry_hbond_refined     ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?    ? r_symmetry_hbond_other       ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?    ? r_symmetry_metal_ion_refined ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?    ? r_symmetry_metal_ion_other   ? ? 
'X-RAY DIFFRACTION' ? 2.559  2.065  941  ? r_mcbond_it                  ? ? 
'X-RAY DIFFRACTION' ? 2.558  2.065  942  ? r_mcbond_other               ? ? 
'X-RAY DIFFRACTION' ? 3.701  3.086  1179 ? r_mcangle_it                 ? ? 
'X-RAY DIFFRACTION' ? 3.701  3.090  1180 ? r_mcangle_other              ? ? 
'X-RAY DIFFRACTION' ? 4.532  2.636  992  ? r_scbond_it                  ? ? 
'X-RAY DIFFRACTION' ? 4.530  2.635  993  ? r_scbond_other               ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?    ? r_scangle_it                 ? ? 
'X-RAY DIFFRACTION' ? 6.737  3.743  1470 ? r_scangle_other              ? ? 
'X-RAY DIFFRACTION' ? 8.623  25.995 2092 ? r_long_range_B_refined       ? ? 
'X-RAY DIFFRACTION' ? 8.631  26.023 2088 ? r_long_range_B_other         ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?    ? r_rigid_bond_restr           ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?    ? r_sphericity_free            ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?    ? r_sphericity_bonded          ? ? 
# 
_refine_ls_shell.pdbx_refine_id                   'X-RAY DIFFRACTION' 
_refine_ls_shell.d_res_high                       1.500 
_refine_ls_shell.d_res_low                        1.539 
_refine_ls_shell.number_reflns_all                ? 
_refine_ls_shell.number_reflns_obs                ? 
_refine_ls_shell.number_reflns_R_free             94 
_refine_ls_shell.number_reflns_R_work             1906 
_refine_ls_shell.percent_reflns_obs               71.53 
_refine_ls_shell.percent_reflns_R_free            ? 
_refine_ls_shell.R_factor_all                     ? 
_refine_ls_shell.R_factor_obs                     ? 
_refine_ls_shell.R_factor_R_free_error            ? 
_refine_ls_shell.R_factor_R_work                  0.235 
_refine_ls_shell.redundancy_reflns_all            ? 
_refine_ls_shell.redundancy_reflns_obs            ? 
_refine_ls_shell.wR_factor_all                    ? 
_refine_ls_shell.wR_factor_obs                    ? 
_refine_ls_shell.wR_factor_R_free                 ? 
_refine_ls_shell.wR_factor_R_work                 ? 
_refine_ls_shell.pdbx_R_complete                  ? 
_refine_ls_shell.pdbx_total_number_of_bins_used   20 
_refine_ls_shell.pdbx_phase_error                 ? 
_refine_ls_shell.pdbx_fsc_work                    ? 
_refine_ls_shell.pdbx_fsc_free                    ? 
_refine_ls_shell.R_factor_R_free                  0.287 
# 
_struct.entry_id                     8U52 
_struct.title                        
;Co-crystal structure of human transthyretin conjugated to the stilbene substructure derived from reaction with the fluorogenic covalent kinetic stabilizer A2
;
_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        8U52 
_struct_keywords.text            'transthyretin, amyloidosis, stabilizer, covalent, fluorogenic, TRANSPORT PROTEIN' 
_struct_keywords.pdbx_keywords   'TRANSPORT PROTEIN' 
# 
loop_
_struct_asym.id 
_struct_asym.pdbx_blank_PDB_chainid_flag 
_struct_asym.pdbx_modified 
_struct_asym.entity_id 
_struct_asym.details 
A N N 1 ? 
B N N 1 ? 
C N N 2 ? 
D N N 2 ? 
E N N 3 ? 
F N N 3 ? 
# 
_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 8U52 A 1 ? 127 ? P02766 21 ? 147 ? 1 127 
2 1 8U52 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   tetrameric 
_pdbx_struct_assembly.oligomeric_count     4 
# 
loop_
_pdbx_struct_assembly_gen.assembly_id 
_pdbx_struct_assembly_gen.oper_expression 
_pdbx_struct_assembly_gen.asym_id_list 
1 1 A,B,C,D,E,F 
1 2 A,B,C,D,E,F 
# 
loop_
_pdbx_struct_oper_list.id 
_pdbx_struct_oper_list.type 
_pdbx_struct_oper_list.name 
_pdbx_struct_oper_list.symmetry_operation 
_pdbx_struct_oper_list.matrix[1][1] 
_pdbx_struct_oper_list.matrix[1][2] 
_pdbx_struct_oper_list.matrix[1][3] 
_pdbx_struct_oper_list.vector[1] 
_pdbx_struct_oper_list.matrix[2][1] 
_pdbx_struct_oper_list.matrix[2][2] 
_pdbx_struct_oper_list.matrix[2][3] 
_pdbx_struct_oper_list.vector[2] 
_pdbx_struct_oper_list.matrix[3][1] 
_pdbx_struct_oper_list.matrix[3][2] 
_pdbx_struct_oper_list.matrix[3][3] 
_pdbx_struct_oper_list.vector[3] 
1 'identity operation'         1_555 x,y,z   1.0000000000  0.0000000000 0.0000000000 0.0000000000 0.0000000000 1.0000000000  
0.0000000000 0.0000000000 0.0000000000 0.0000000000 1.0000000000 0.0000000000 
2 'crystal symmetry operation' 2_555 -x,-y,z -1.0000000000 0.0000000000 0.0000000000 0.0000000000 0.0000000000 -1.0000000000 
0.0000000000 0.0000000000 0.0000000000 0.0000000000 1.0000000000 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 ? ALA A 81 ? ASP A 74 ALA A 81 1 ? 8 
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_conn.id 
_struct_conn.conn_type_id 
_struct_conn.pdbx_leaving_atom_flag 
_struct_conn.pdbx_PDB_id 
_struct_conn.ptnr1_label_asym_id 
_struct_conn.ptnr1_label_comp_id 
_struct_conn.ptnr1_label_seq_id 
_struct_conn.ptnr1_label_atom_id 
_struct_conn.pdbx_ptnr1_label_alt_id 
_struct_conn.pdbx_ptnr1_PDB_ins_code 
_struct_conn.pdbx_ptnr1_standard_comp_id 
_struct_conn.ptnr1_symmetry 
_struct_conn.ptnr2_label_asym_id 
_struct_conn.ptnr2_label_comp_id 
_struct_conn.ptnr2_label_seq_id 
_struct_conn.ptnr2_label_atom_id 
_struct_conn.pdbx_ptnr2_label_alt_id 
_struct_conn.pdbx_ptnr2_PDB_ins_code 
_struct_conn.ptnr1_auth_asym_id 
_struct_conn.ptnr1_auth_comp_id 
_struct_conn.ptnr1_auth_seq_id 
_struct_conn.ptnr2_auth_asym_id 
_struct_conn.ptnr2_auth_comp_id 
_struct_conn.ptnr2_auth_seq_id 
_struct_conn.ptnr2_symmetry 
_struct_conn.pdbx_ptnr3_label_atom_id 
_struct_conn.pdbx_ptnr3_label_seq_id 
_struct_conn.pdbx_ptnr3_label_comp_id 
_struct_conn.pdbx_ptnr3_label_asym_id 
_struct_conn.pdbx_ptnr3_label_alt_id 
_struct_conn.pdbx_ptnr3_PDB_ins_code 
_struct_conn.details 
_struct_conn.pdbx_dist_value 
_struct_conn.pdbx_value_order 
_struct_conn.pdbx_role 
covale1 covale one ? A LYS 15 NZ A ? ? 1_555 C 1W4 . C1 ? ? A LYS 15 A 1W4 201 1_555 ? ? ? ? ? ? ? 1.464 ? ? 
covale2 covale one ? B LYS 15 NZ A ? ? 1_555 D 1W4 . C1 ? ? B LYS 15 B 1W4 201 1_555 ? ? ? ? ? ? ? 1.507 ? ? 
# 
_struct_conn_type.id          covale 
_struct_conn_type.criteria    ? 
_struct_conn_type.reference   ? 
# 
loop_
_pdbx_modification_feature.ordinal 
_pdbx_modification_feature.label_comp_id 
_pdbx_modification_feature.label_asym_id 
_pdbx_modification_feature.label_seq_id 
_pdbx_modification_feature.label_alt_id 
_pdbx_modification_feature.modified_residue_label_comp_id 
_pdbx_modification_feature.modified_residue_label_asym_id 
_pdbx_modification_feature.modified_residue_label_seq_id 
_pdbx_modification_feature.modified_residue_label_alt_id 
_pdbx_modification_feature.auth_comp_id 
_pdbx_modification_feature.auth_asym_id 
_pdbx_modification_feature.auth_seq_id 
_pdbx_modification_feature.PDB_ins_code 
_pdbx_modification_feature.symmetry 
_pdbx_modification_feature.modified_residue_auth_comp_id 
_pdbx_modification_feature.modified_residue_auth_asym_id 
_pdbx_modification_feature.modified_residue_auth_seq_id 
_pdbx_modification_feature.modified_residue_PDB_ins_code 
_pdbx_modification_feature.modified_residue_symmetry 
_pdbx_modification_feature.comp_id_linking_atom 
_pdbx_modification_feature.modified_residue_id_linking_atom 
_pdbx_modification_feature.modified_residue_id 
_pdbx_modification_feature.ref_pcm_id 
_pdbx_modification_feature.ref_comp_id 
_pdbx_modification_feature.type 
_pdbx_modification_feature.category 
1 1W4 C . ? LYS A 15 A 1W4 A 201 ? 1_555 LYS A 15 ? 1_555 C1 NZ LYS 1 1W4 None 'Covalent chemical modification' 
2 1W4 D . ? LYS B 15 A 1W4 B 201 ? 1_555 LYS B 15 ? 1_555 C1 NZ LYS 1 1W4 None 'Covalent chemical modification' 
# 
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 ? SER B 112 ? ARG B 104 SER B 112 
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 ? SER B 112 ? ARG B 104 SER B 112 
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 LYS A 15  ? N LYS A 15  O ALA A 109 ? O ALA A 109 
AA1 3 4 N SER A 112 ? N SER A 112 O SER A 115 ? O SER A 115 
AA1 4 5 N TYR A 116 ? N TYR A 116 O THR B 118 ? O THR B 118 
AA1 5 6 O VAL B 121 ? O VAL B 121 N THR B 106 ? N THR B 106 
AA1 6 7 O LEU B 111 ? O LEU B 111 N LEU B 17  ? N LEU B 17  
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 LYS A 15  ? N LYS A 15  O ALA A 109 ? O ALA A 109 
AA2 3 4 N SER A 112 ? N SER A 112 O SER A 115 ? O SER A 115 
AA2 4 5 N TYR A 116 ? N TYR A 116 O THR B 118 ? O THR B 118 
AA2 5 6 O VAL B 121 ? O VAL B 121 N THR B 106 ? N THR B 106 
AA2 6 7 O LEU B 111 ? O LEU B 111 N LEU B 17  ? N LEU B 17  
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 GLU A 89  ? N GLU A 89  O VAL B 94  ? O VAL B 94  
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                   8U52 
_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   Y 
# 
_pdbx_validate_torsion.id              1 
_pdbx_validate_torsion.PDB_model_num   1 
_pdbx_validate_torsion.auth_comp_id    ASN 
_pdbx_validate_torsion.auth_asym_id    A 
_pdbx_validate_torsion.auth_seq_id     27 
_pdbx_validate_torsion.PDB_ins_code    ? 
_pdbx_validate_torsion.label_alt_id    ? 
_pdbx_validate_torsion.phi             70.03 
_pdbx_validate_torsion.psi             31.40 
# 
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 1W4 201 ? C 1W4 . 
2 1 A 1W4 201 ? C 1W4 . 
3 1 A 1W4 201 ? C 1W4 . 
4 1 B 1W4 201 ? D 1W4 . 
5 1 B 1W4 201 ? D 1W4 . 
6 1 B 1W4 201 ? D 1W4 . 
# 
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 9   ? A LYS 9   
10 1 Y 1 A PRO 125 ? A PRO 125 
11 1 Y 1 A LYS 126 ? A LYS 126 
12 1 Y 1 A GLU 127 ? A GLU 127 
13 1 Y 1 B GLY 1   ? B GLY 1   
14 1 Y 1 B PRO 2   ? B PRO 2   
15 1 Y 1 B THR 3   ? B THR 3   
16 1 Y 1 B GLY 4   ? B GLY 4   
17 1 Y 1 B THR 5   ? B THR 5   
18 1 Y 1 B GLY 6   ? B GLY 6   
19 1 Y 1 B GLU 7   ? B GLU 7   
20 1 Y 1 B SER 8   ? B SER 8   
21 1 Y 1 B LYS 9   ? B LYS 9   
22 1 Y 1 B PRO 125 ? B PRO 125 
23 1 Y 1 B LYS 126 ? B LYS 126 
24 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 
1W4 C1   C N N 1   
1W4 O2   O N N 2   
1W4 C3   C Y N 3   
1W4 C4   C Y N 4   
1W4 C5   C Y N 5   
1W4 C6   C Y N 6   
1W4 C7   C Y N 7   
1W4 C8   C Y N 8   
1W4 N9   N N N 9   
1W4 C10  C N N 10  
1W4 C11  C N N 11  
1W4 C12  C N N 12  
1W4 C13  C N N 13  
1W4 C14  C Y N 14  
1W4 C15  C Y N 15  
1W4 C16  C Y N 16  
1W4 C17  C Y N 17  
1W4 C18  C Y N 18  
1W4 C19  C Y N 19  
1W4 C26  C N N 20  
1W4 C27  C N N 21  
1W4 O28  O N N 22  
1W4 S1   S N N 23  
1W4 H1   H N N 24  
1W4 H2   H N N 25  
1W4 H3   H N N 26  
1W4 H4   H N N 27  
1W4 H5   H N N 28  
1W4 H6   H N N 29  
1W4 H7   H N N 30  
1W4 H8   H N N 31  
1W4 H9   H N N 32  
1W4 H10  H N N 33  
1W4 H11  H N N 34  
1W4 H12  H N N 35  
1W4 H13  H N N 36  
1W4 H14  H N N 37  
1W4 H15  H N N 38  
1W4 H16  H N N 39  
1W4 H17  H N N 40  
1W4 H18  H N N 41  
1W4 H19  H N N 42  
1W4 H20  H N N 43  
1W4 C2   C Y N 44  
1W4 C9   C Y N 45  
1W4 C20  C Y N 46  
1W4 C21  C Y N 47  
1W4 C22  C Y N 48  
1W4 C23  C Y N 49  
1W4 F1   F N N 50  
1W4 H21  H N N 51  
1W4 H22  H N N 52  
1W4 H23  H N N 53  
1W4 H24  H N N 54  
ALA N    N N N 55  
ALA CA   C N S 56  
ALA C    C N N 57  
ALA O    O N N 58  
ALA CB   C N N 59  
ALA OXT  O N N 60  
ALA H    H N N 61  
ALA H2   H N N 62  
ALA HA   H N N 63  
ALA HB1  H N N 64  
ALA HB2  H N N 65  
ALA HB3  H N N 66  
ALA HXT  H N N 67  
ARG N    N N N 68  
ARG CA   C N S 69  
ARG C    C N N 70  
ARG O    O N N 71  
ARG CB   C N N 72  
ARG CG   C N N 73  
ARG CD   C N N 74  
ARG NE   N N N 75  
ARG CZ   C N N 76  
ARG NH1  N N N 77  
ARG NH2  N N N 78  
ARG OXT  O N N 79  
ARG H    H N N 80  
ARG H2   H N N 81  
ARG HA   H N N 82  
ARG HB2  H N N 83  
ARG HB3  H N N 84  
ARG HG2  H N N 85  
ARG HG3  H N N 86  
ARG HD2  H N N 87  
ARG HD3  H N N 88  
ARG HE   H N N 89  
ARG HH11 H N N 90  
ARG HH12 H N N 91  
ARG HH21 H N N 92  
ARG HH22 H N N 93  
ARG HXT  H N N 94  
ASN N    N N N 95  
ASN CA   C N S 96  
ASN C    C N N 97  
ASN O    O N N 98  
ASN CB   C N N 99  
ASN CG   C N N 100 
ASN OD1  O N N 101 
ASN ND2  N N N 102 
ASN OXT  O N N 103 
ASN H    H N N 104 
ASN H2   H N N 105 
ASN HA   H N N 106 
ASN HB2  H N N 107 
ASN HB3  H N N 108 
ASN HD21 H N N 109 
ASN HD22 H N N 110 
ASN HXT  H N N 111 
ASP N    N N N 112 
ASP CA   C N S 113 
ASP C    C N N 114 
ASP O    O N N 115 
ASP CB   C N N 116 
ASP CG   C N N 117 
ASP OD1  O N N 118 
ASP OD2  O N N 119 
ASP OXT  O N N 120 
ASP H    H N N 121 
ASP H2   H N N 122 
ASP HA   H N N 123 
ASP HB2  H N N 124 
ASP HB3  H N N 125 
ASP HD2  H N N 126 
ASP HXT  H N N 127 
CYS N    N N N 128 
CYS CA   C N R 129 
CYS C    C N N 130 
CYS O    O N N 131 
CYS CB   C N N 132 
CYS SG   S N N 133 
CYS OXT  O N N 134 
CYS H    H N N 135 
CYS H2   H N N 136 
CYS HA   H N N 137 
CYS HB2  H N N 138 
CYS HB3  H N N 139 
CYS HG   H N N 140 
CYS HXT  H N N 141 
GLU N    N N N 142 
GLU CA   C N S 143 
GLU C    C N N 144 
GLU O    O N N 145 
GLU CB   C N N 146 
GLU CG   C N N 147 
GLU CD   C N N 148 
GLU OE1  O N N 149 
GLU OE2  O N N 150 
GLU OXT  O N N 151 
GLU H    H N N 152 
GLU H2   H N N 153 
GLU HA   H N N 154 
GLU HB2  H N N 155 
GLU HB3  H N N 156 
GLU HG2  H N N 157 
GLU HG3  H N N 158 
GLU HE2  H N N 159 
GLU HXT  H N N 160 
GLY N    N N N 161 
GLY CA   C N N 162 
GLY C    C N N 163 
GLY O    O N N 164 
GLY OXT  O N N 165 
GLY H    H N N 166 
GLY H2   H N N 167 
GLY HA2  H N N 168 
GLY HA3  H N N 169 
GLY HXT  H N N 170 
HIS N    N N N 171 
HIS CA   C N S 172 
HIS C    C N N 173 
HIS O    O N N 174 
HIS CB   C N N 175 
HIS CG   C Y N 176 
HIS ND1  N Y N 177 
HIS CD2  C Y N 178 
HIS CE1  C Y N 179 
HIS NE2  N Y N 180 
HIS OXT  O N N 181 
HIS H    H N N 182 
HIS H2   H N N 183 
HIS HA   H N N 184 
HIS HB2  H N N 185 
HIS HB3  H N N 186 
HIS HD1  H N N 187 
HIS HD2  H N N 188 
HIS HE1  H N N 189 
HIS HE2  H N N 190 
HIS HXT  H N N 191 
HOH O    O N N 192 
HOH H1   H N N 193 
HOH H2   H N N 194 
ILE N    N N N 195 
ILE CA   C N S 196 
ILE C    C N N 197 
ILE O    O N N 198 
ILE CB   C N S 199 
ILE CG1  C N N 200 
ILE CG2  C N N 201 
ILE CD1  C N N 202 
ILE OXT  O N N 203 
ILE H    H N N 204 
ILE H2   H N N 205 
ILE HA   H N N 206 
ILE HB   H N N 207 
ILE HG12 H N N 208 
ILE HG13 H N N 209 
ILE HG21 H N N 210 
ILE HG22 H N N 211 
ILE HG23 H N N 212 
ILE HD11 H N N 213 
ILE HD12 H N N 214 
ILE HD13 H N N 215 
ILE HXT  H N N 216 
LEU N    N N N 217 
LEU CA   C N S 218 
LEU C    C N N 219 
LEU O    O N N 220 
LEU CB   C N N 221 
LEU CG   C N N 222 
LEU CD1  C N N 223 
LEU CD2  C N N 224 
LEU OXT  O N N 225 
LEU H    H N N 226 
LEU H2   H N N 227 
LEU HA   H N N 228 
LEU HB2  H N N 229 
LEU HB3  H N N 230 
LEU HG   H N N 231 
LEU HD11 H N N 232 
LEU HD12 H N N 233 
LEU HD13 H N N 234 
LEU HD21 H N N 235 
LEU HD22 H N N 236 
LEU HD23 H N N 237 
LEU HXT  H N N 238 
LYS N    N N N 239 
LYS CA   C N S 240 
LYS C    C N N 241 
LYS O    O N N 242 
LYS CB   C N N 243 
LYS CG   C N N 244 
LYS CD   C N N 245 
LYS CE   C N N 246 
LYS NZ   N N N 247 
LYS OXT  O N N 248 
LYS H    H N N 249 
LYS H2   H N N 250 
LYS HA   H N N 251 
LYS HB2  H N N 252 
LYS HB3  H N N 253 
LYS HG2  H N N 254 
LYS HG3  H N N 255 
LYS HD2  H N N 256 
LYS HD3  H N N 257 
LYS HE2  H N N 258 
LYS HE3  H N N 259 
LYS HZ1  H N N 260 
LYS HZ2  H N N 261 
LYS HZ3  H N N 262 
LYS HXT  H N N 263 
MET N    N N N 264 
MET CA   C N S 265 
MET C    C N N 266 
MET O    O N N 267 
MET CB   C N N 268 
MET CG   C N N 269 
MET SD   S N N 270 
MET CE   C N N 271 
MET OXT  O N N 272 
MET H    H N N 273 
MET H2   H N N 274 
MET HA   H N N 275 
MET HB2  H N N 276 
MET HB3  H N N 277 
MET HG2  H N N 278 
MET HG3  H N N 279 
MET HE1  H N N 280 
MET HE2  H N N 281 
MET HE3  H N N 282 
MET HXT  H N N 283 
PHE N    N N N 284 
PHE CA   C N S 285 
PHE C    C N N 286 
PHE O    O N N 287 
PHE CB   C N N 288 
PHE CG   C Y N 289 
PHE CD1  C Y N 290 
PHE CD2  C Y N 291 
PHE CE1  C Y N 292 
PHE CE2  C Y N 293 
PHE CZ   C Y N 294 
PHE OXT  O N N 295 
PHE H    H N N 296 
PHE H2   H N N 297 
PHE HA   H N N 298 
PHE HB2  H N N 299 
PHE HB3  H N N 300 
PHE HD1  H N N 301 
PHE HD2  H N N 302 
PHE HE1  H N N 303 
PHE HE2  H N N 304 
PHE HZ   H N N 305 
PHE HXT  H N N 306 
PRO N    N N N 307 
PRO CA   C N S 308 
PRO C    C N N 309 
PRO O    O N N 310 
PRO CB   C N N 311 
PRO CG   C N N 312 
PRO CD   C N N 313 
PRO OXT  O N N 314 
PRO H    H N N 315 
PRO HA   H N N 316 
PRO HB2  H N N 317 
PRO HB3  H N N 318 
PRO HG2  H N N 319 
PRO HG3  H N N 320 
PRO HD2  H N N 321 
PRO HD3  H N N 322 
PRO HXT  H N N 323 
SER N    N N N 324 
SER CA   C N S 325 
SER C    C N N 326 
SER O    O N N 327 
SER CB   C N N 328 
SER OG   O N N 329 
SER OXT  O N N 330 
SER H    H N N 331 
SER H2   H N N 332 
SER HA   H N N 333 
SER HB2  H N N 334 
SER HB3  H N N 335 
SER HG   H N N 336 
SER HXT  H N N 337 
THR N    N N N 338 
THR CA   C N S 339 
THR C    C N N 340 
THR O    O N N 341 
THR CB   C N R 342 
THR OG1  O N N 343 
THR CG2  C N N 344 
THR OXT  O N N 345 
THR H    H N N 346 
THR H2   H N N 347 
THR HA   H N N 348 
THR HB   H N N 349 
THR HG1  H N N 350 
THR HG21 H N N 351 
THR HG22 H N N 352 
THR HG23 H N N 353 
THR HXT  H N N 354 
TRP N    N N N 355 
TRP CA   C N S 356 
TRP C    C N N 357 
TRP O    O N N 358 
TRP CB   C N N 359 
TRP CG   C Y N 360 
TRP CD1  C Y N 361 
TRP CD2  C Y N 362 
TRP NE1  N Y N 363 
TRP CE2  C Y N 364 
TRP CE3  C Y N 365 
TRP CZ2  C Y N 366 
TRP CZ3  C Y N 367 
TRP CH2  C Y N 368 
TRP OXT  O N N 369 
TRP H    H N N 370 
TRP H2   H N N 371 
TRP HA   H N N 372 
TRP HB2  H N N 373 
TRP HB3  H N N 374 
TRP HD1  H N N 375 
TRP HE1  H N N 376 
TRP HE3  H N N 377 
TRP HZ2  H N N 378 
TRP HZ3  H N N 379 
TRP HH2  H N N 380 
TRP HXT  H N N 381 
TYR N    N N N 382 
TYR CA   C N S 383 
TYR C    C N N 384 
TYR O    O N N 385 
TYR CB   C N N 386 
TYR CG   C Y N 387 
TYR CD1  C Y N 388 
TYR CD2  C Y N 389 
TYR CE1  C Y N 390 
TYR CE2  C Y N 391 
TYR CZ   C Y N 392 
TYR OH   O N N 393 
TYR OXT  O N N 394 
TYR H    H N N 395 
TYR H2   H N N 396 
TYR HA   H N N 397 
TYR HB2  H N N 398 
TYR HB3  H N N 399 
TYR HD1  H N N 400 
TYR HD2  H N N 401 
TYR HE1  H N N 402 
TYR HE2  H N N 403 
TYR HH   H N N 404 
TYR HXT  H N N 405 
VAL N    N N N 406 
VAL CA   C N S 407 
VAL C    C N N 408 
VAL O    O N N 409 
VAL CB   C N N 410 
VAL CG1  C N N 411 
VAL CG2  C N N 412 
VAL OXT  O N N 413 
VAL H    H N N 414 
VAL H2   H N N 415 
VAL HA   H N N 416 
VAL HB   H N N 417 
VAL HG11 H N N 418 
VAL HG12 H N N 419 
VAL HG13 H N N 420 
VAL HG21 H N N 421 
VAL HG22 H N N 422 
VAL HG23 H N N 423 
VAL HXT  H N N 424 
# 
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 
1W4 O28 C17  sing N N 1   
1W4 C27 C18  sing N N 2   
1W4 C17 C18  doub Y N 3   
1W4 C17 C16  sing Y N 4   
1W4 C26 C16  sing N N 5   
1W4 C18 C19  sing Y N 6   
1W4 C16 C15  doub Y N 7   
1W4 C19 C14  doub Y N 8   
1W4 C15 C14  sing Y N 9   
1W4 C14 C13  sing N N 10  
1W4 C13 C12  doub N E 11  
1W4 C12 C7   sing N N 12  
1W4 C7  C6   doub Y N 13  
1W4 C7  C8   sing Y N 14  
1W4 C6  C5   sing Y N 15  
1W4 C8  C3   doub Y N 16  
1W4 C5  N9   sing N N 17  
1W4 C5  C4   doub Y N 18  
1W4 C3  C4   sing Y N 19  
1W4 C3  C1   sing N N 20  
1W4 C10 N9   sing N N 21  
1W4 N9  C11  sing N N 22  
1W4 C1  O2   doub N N 23  
1W4 C1  S1   sing N N 24  
1W4 C4  H1   sing N N 25  
1W4 C6  H2   sing N N 26  
1W4 C8  H3   sing N N 27  
1W4 C10 H4   sing N N 28  
1W4 C10 H5   sing N N 29  
1W4 C10 H6   sing N N 30  
1W4 C11 H7   sing N N 31  
1W4 C11 H8   sing N N 32  
1W4 C11 H9   sing N N 33  
1W4 C12 H10  sing N N 34  
1W4 C13 H11  sing N N 35  
1W4 C15 H12  sing N N 36  
1W4 C19 H13  sing N N 37  
1W4 C26 H14  sing N N 38  
1W4 C26 H15  sing N N 39  
1W4 C26 H16  sing N N 40  
1W4 C27 H17  sing N N 41  
1W4 C27 H18  sing N N 42  
1W4 C27 H19  sing N N 43  
1W4 O28 H20  sing N N 44  
1W4 S1  C2   sing N N 45  
1W4 C2  C9   sing Y N 46  
1W4 C9  C20  doub Y N 47  
1W4 C20 C21  sing Y N 48  
1W4 C21 C22  doub Y N 49  
1W4 C22 C23  sing Y N 50  
1W4 C23 C2   doub Y N 51  
1W4 C21 F1   sing N N 52  
1W4 C9  H21  sing N N 53  
1W4 C20 H22  sing N N 54  
1W4 C22 H23  sing N N 55  
1W4 C23 H24  sing N N 56  
ALA N   CA   sing N N 57  
ALA N   H    sing N N 58  
ALA N   H2   sing N N 59  
ALA CA  C    sing N N 60  
ALA CA  CB   sing N N 61  
ALA CA  HA   sing N N 62  
ALA C   O    doub N N 63  
ALA C   OXT  sing N N 64  
ALA CB  HB1  sing N N 65  
ALA CB  HB2  sing N N 66  
ALA CB  HB3  sing N N 67  
ALA OXT HXT  sing N N 68  
ARG N   CA   sing N N 69  
ARG N   H    sing N N 70  
ARG N   H2   sing N N 71  
ARG CA  C    sing N N 72  
ARG CA  CB   sing N N 73  
ARG CA  HA   sing N N 74  
ARG C   O    doub N N 75  
ARG C   OXT  sing N N 76  
ARG CB  CG   sing N N 77  
ARG CB  HB2  sing N N 78  
ARG CB  HB3  sing N N 79  
ARG CG  CD   sing N N 80  
ARG CG  HG2  sing N N 81  
ARG CG  HG3  sing N N 82  
ARG CD  NE   sing N N 83  
ARG CD  HD2  sing N N 84  
ARG CD  HD3  sing N N 85  
ARG NE  CZ   sing N N 86  
ARG NE  HE   sing N N 87  
ARG CZ  NH1  sing N N 88  
ARG CZ  NH2  doub N N 89  
ARG NH1 HH11 sing N N 90  
ARG NH1 HH12 sing N N 91  
ARG NH2 HH21 sing N N 92  
ARG NH2 HH22 sing N N 93  
ARG OXT HXT  sing N N 94  
ASN N   CA   sing N N 95  
ASN N   H    sing N N 96  
ASN N   H2   sing N N 97  
ASN CA  C    sing N N 98  
ASN CA  CB   sing N N 99  
ASN CA  HA   sing N N 100 
ASN C   O    doub N N 101 
ASN C   OXT  sing N N 102 
ASN CB  CG   sing N N 103 
ASN CB  HB2  sing N N 104 
ASN CB  HB3  sing N N 105 
ASN CG  OD1  doub N N 106 
ASN CG  ND2  sing N N 107 
ASN ND2 HD21 sing N N 108 
ASN ND2 HD22 sing N N 109 
ASN OXT HXT  sing N N 110 
ASP N   CA   sing N N 111 
ASP N   H    sing N N 112 
ASP N   H2   sing N N 113 
ASP CA  C    sing N N 114 
ASP CA  CB   sing N N 115 
ASP CA  HA   sing N N 116 
ASP C   O    doub N N 117 
ASP C   OXT  sing N N 118 
ASP CB  CG   sing N N 119 
ASP CB  HB2  sing N N 120 
ASP CB  HB3  sing N N 121 
ASP CG  OD1  doub N N 122 
ASP CG  OD2  sing N N 123 
ASP OD2 HD2  sing N N 124 
ASP OXT HXT  sing N N 125 
CYS N   CA   sing N N 126 
CYS N   H    sing N N 127 
CYS N   H2   sing N N 128 
CYS CA  C    sing N N 129 
CYS CA  CB   sing N N 130 
CYS CA  HA   sing N N 131 
CYS C   O    doub N N 132 
CYS C   OXT  sing N N 133 
CYS CB  SG   sing N N 134 
CYS CB  HB2  sing N N 135 
CYS CB  HB3  sing N N 136 
CYS SG  HG   sing N N 137 
CYS OXT HXT  sing N N 138 
GLU N   CA   sing N N 139 
GLU N   H    sing N N 140 
GLU N   H2   sing N N 141 
GLU CA  C    sing N N 142 
GLU CA  CB   sing N N 143 
GLU CA  HA   sing N N 144 
GLU C   O    doub N N 145 
GLU C   OXT  sing N N 146 
GLU CB  CG   sing N N 147 
GLU CB  HB2  sing N N 148 
GLU CB  HB3  sing N N 149 
GLU CG  CD   sing N N 150 
GLU CG  HG2  sing N N 151 
GLU CG  HG3  sing N N 152 
GLU CD  OE1  doub N N 153 
GLU CD  OE2  sing N N 154 
GLU OE2 HE2  sing N N 155 
GLU OXT HXT  sing N N 156 
GLY N   CA   sing N N 157 
GLY N   H    sing N N 158 
GLY N   H2   sing N N 159 
GLY CA  C    sing N N 160 
GLY CA  HA2  sing N N 161 
GLY CA  HA3  sing N N 162 
GLY C   O    doub N N 163 
GLY C   OXT  sing N N 164 
GLY OXT HXT  sing N N 165 
HIS N   CA   sing N N 166 
HIS N   H    sing N N 167 
HIS N   H2   sing N N 168 
HIS CA  C    sing N N 169 
HIS CA  CB   sing N N 170 
HIS CA  HA   sing N N 171 
HIS C   O    doub N N 172 
HIS C   OXT  sing N N 173 
HIS CB  CG   sing N N 174 
HIS CB  HB2  sing N N 175 
HIS CB  HB3  sing N N 176 
HIS CG  ND1  sing Y N 177 
HIS CG  CD2  doub Y N 178 
HIS ND1 CE1  doub Y N 179 
HIS ND1 HD1  sing N N 180 
HIS CD2 NE2  sing Y N 181 
HIS CD2 HD2  sing N N 182 
HIS CE1 NE2  sing Y N 183 
HIS CE1 HE1  sing N N 184 
HIS NE2 HE2  sing N N 185 
HIS OXT HXT  sing N N 186 
HOH O   H1   sing N N 187 
HOH O   H2   sing N N 188 
ILE N   CA   sing N N 189 
ILE N   H    sing N N 190 
ILE N   H2   sing N N 191 
ILE CA  C    sing N N 192 
ILE CA  CB   sing N N 193 
ILE CA  HA   sing N N 194 
ILE C   O    doub N N 195 
ILE C   OXT  sing N N 196 
ILE CB  CG1  sing N N 197 
ILE CB  CG2  sing N N 198 
ILE CB  HB   sing N N 199 
ILE CG1 CD1  sing N N 200 
ILE CG1 HG12 sing N N 201 
ILE CG1 HG13 sing N N 202 
ILE CG2 HG21 sing N N 203 
ILE CG2 HG22 sing N N 204 
ILE CG2 HG23 sing N N 205 
ILE CD1 HD11 sing N N 206 
ILE CD1 HD12 sing N N 207 
ILE CD1 HD13 sing N N 208 
ILE OXT HXT  sing N N 209 
LEU N   CA   sing N N 210 
LEU N   H    sing N N 211 
LEU N   H2   sing N N 212 
LEU CA  C    sing N N 213 
LEU CA  CB   sing N N 214 
LEU CA  HA   sing N N 215 
LEU C   O    doub N N 216 
LEU C   OXT  sing N N 217 
LEU CB  CG   sing N N 218 
LEU CB  HB2  sing N N 219 
LEU CB  HB3  sing N N 220 
LEU CG  CD1  sing N N 221 
LEU CG  CD2  sing N N 222 
LEU CG  HG   sing N N 223 
LEU CD1 HD11 sing N N 224 
LEU CD1 HD12 sing N N 225 
LEU CD1 HD13 sing N N 226 
LEU CD2 HD21 sing N N 227 
LEU CD2 HD22 sing N N 228 
LEU CD2 HD23 sing N N 229 
LEU OXT HXT  sing N N 230 
LYS N   CA   sing N N 231 
LYS N   H    sing N N 232 
LYS N   H2   sing N N 233 
LYS CA  C    sing N N 234 
LYS CA  CB   sing N N 235 
LYS CA  HA   sing N N 236 
LYS C   O    doub N N 237 
LYS C   OXT  sing N N 238 
LYS CB  CG   sing N N 239 
LYS CB  HB2  sing N N 240 
LYS CB  HB3  sing N N 241 
LYS CG  CD   sing N N 242 
LYS CG  HG2  sing N N 243 
LYS CG  HG3  sing N N 244 
LYS CD  CE   sing N N 245 
LYS CD  HD2  sing N N 246 
LYS CD  HD3  sing N N 247 
LYS CE  NZ   sing N N 248 
LYS CE  HE2  sing N N 249 
LYS CE  HE3  sing N N 250 
LYS NZ  HZ1  sing N N 251 
LYS NZ  HZ2  sing N N 252 
LYS NZ  HZ3  sing N N 253 
LYS OXT HXT  sing N N 254 
MET N   CA   sing N N 255 
MET N   H    sing N N 256 
MET N   H2   sing N N 257 
MET CA  C    sing N N 258 
MET CA  CB   sing N N 259 
MET CA  HA   sing N N 260 
MET C   O    doub N N 261 
MET C   OXT  sing N N 262 
MET CB  CG   sing N N 263 
MET CB  HB2  sing N N 264 
MET CB  HB3  sing N N 265 
MET CG  SD   sing N N 266 
MET CG  HG2  sing N N 267 
MET CG  HG3  sing N N 268 
MET SD  CE   sing N N 269 
MET CE  HE1  sing N N 270 
MET CE  HE2  sing N N 271 
MET CE  HE3  sing N N 272 
MET OXT HXT  sing N N 273 
PHE N   CA   sing N N 274 
PHE N   H    sing N N 275 
PHE N   H2   sing N N 276 
PHE CA  C    sing N N 277 
PHE CA  CB   sing N N 278 
PHE CA  HA   sing N N 279 
PHE C   O    doub N N 280 
PHE C   OXT  sing N N 281 
PHE CB  CG   sing N N 282 
PHE CB  HB2  sing N N 283 
PHE CB  HB3  sing N N 284 
PHE CG  CD1  doub Y N 285 
PHE CG  CD2  sing Y N 286 
PHE CD1 CE1  sing Y N 287 
PHE CD1 HD1  sing N N 288 
PHE CD2 CE2  doub Y N 289 
PHE CD2 HD2  sing N N 290 
PHE CE1 CZ   doub Y N 291 
PHE CE1 HE1  sing N N 292 
PHE CE2 CZ   sing Y N 293 
PHE CE2 HE2  sing N N 294 
PHE CZ  HZ   sing N N 295 
PHE OXT HXT  sing N N 296 
PRO N   CA   sing N N 297 
PRO N   CD   sing N N 298 
PRO N   H    sing N N 299 
PRO CA  C    sing N N 300 
PRO CA  CB   sing N N 301 
PRO CA  HA   sing N N 302 
PRO C   O    doub N N 303 
PRO C   OXT  sing N N 304 
PRO CB  CG   sing N N 305 
PRO CB  HB2  sing N N 306 
PRO CB  HB3  sing N N 307 
PRO CG  CD   sing N N 308 
PRO CG  HG2  sing N N 309 
PRO CG  HG3  sing N N 310 
PRO CD  HD2  sing N N 311 
PRO CD  HD3  sing N N 312 
PRO OXT HXT  sing N N 313 
SER N   CA   sing N N 314 
SER N   H    sing N N 315 
SER N   H2   sing N N 316 
SER CA  C    sing N N 317 
SER CA  CB   sing N N 318 
SER CA  HA   sing N N 319 
SER C   O    doub N N 320 
SER C   OXT  sing N N 321 
SER CB  OG   sing N N 322 
SER CB  HB2  sing N N 323 
SER CB  HB3  sing N N 324 
SER OG  HG   sing N N 325 
SER OXT HXT  sing N N 326 
THR N   CA   sing N N 327 
THR N   H    sing N N 328 
THR N   H2   sing N N 329 
THR CA  C    sing N N 330 
THR CA  CB   sing N N 331 
THR CA  HA   sing N N 332 
THR C   O    doub N N 333 
THR C   OXT  sing N N 334 
THR CB  OG1  sing N N 335 
THR CB  CG2  sing N N 336 
THR CB  HB   sing N N 337 
THR OG1 HG1  sing N N 338 
THR CG2 HG21 sing N N 339 
THR CG2 HG22 sing N N 340 
THR CG2 HG23 sing N N 341 
THR OXT HXT  sing N N 342 
TRP N   CA   sing N N 343 
TRP N   H    sing N N 344 
TRP N   H2   sing N N 345 
TRP CA  C    sing N N 346 
TRP CA  CB   sing N N 347 
TRP CA  HA   sing N N 348 
TRP C   O    doub N N 349 
TRP C   OXT  sing N N 350 
TRP CB  CG   sing N N 351 
TRP CB  HB2  sing N N 352 
TRP CB  HB3  sing N N 353 
TRP CG  CD1  doub Y N 354 
TRP CG  CD2  sing Y N 355 
TRP CD1 NE1  sing Y N 356 
TRP CD1 HD1  sing N N 357 
TRP CD2 CE2  doub Y N 358 
TRP CD2 CE3  sing Y N 359 
TRP NE1 CE2  sing Y N 360 
TRP NE1 HE1  sing N N 361 
TRP CE2 CZ2  sing Y N 362 
TRP CE3 CZ3  doub Y N 363 
TRP CE3 HE3  sing N N 364 
TRP CZ2 CH2  doub Y N 365 
TRP CZ2 HZ2  sing N N 366 
TRP CZ3 CH2  sing Y N 367 
TRP CZ3 HZ3  sing N N 368 
TRP CH2 HH2  sing N N 369 
TRP OXT HXT  sing N N 370 
TYR N   CA   sing N N 371 
TYR N   H    sing N N 372 
TYR N   H2   sing N N 373 
TYR CA  C    sing N N 374 
TYR CA  CB   sing N N 375 
TYR CA  HA   sing N N 376 
TYR C   O    doub N N 377 
TYR C   OXT  sing N N 378 
TYR CB  CG   sing N N 379 
TYR CB  HB2  sing N N 380 
TYR CB  HB3  sing N N 381 
TYR CG  CD1  doub Y N 382 
TYR CG  CD2  sing Y N 383 
TYR CD1 CE1  sing Y N 384 
TYR CD1 HD1  sing N N 385 
TYR CD2 CE2  doub Y N 386 
TYR CD2 HD2  sing N N 387 
TYR CE1 CZ   doub Y N 388 
TYR CE1 HE1  sing N N 389 
TYR CE2 CZ   sing Y N 390 
TYR CE2 HE2  sing N N 391 
TYR CZ  OH   sing N N 392 
TYR OH  HH   sing N N 393 
TYR OXT HXT  sing N N 394 
VAL N   CA   sing N N 395 
VAL N   H    sing N N 396 
VAL N   H2   sing N N 397 
VAL CA  C    sing N N 398 
VAL CA  CB   sing N N 399 
VAL CA  HA   sing N N 400 
VAL C   O    doub N N 401 
VAL C   OXT  sing N N 402 
VAL CB  CG1  sing N N 403 
VAL CB  CG2  sing N N 404 
VAL CB  HB   sing N N 405 
VAL CG1 HG11 sing N N 406 
VAL CG1 HG12 sing N N 407 
VAL CG1 HG13 sing N N 408 
VAL CG2 HG21 sing N N 409 
VAL CG2 HG22 sing N N 410 
VAL CG2 HG23 sing N N 411 
VAL OXT HXT  sing N N 412 
# 
_pdbx_audit_support.funding_organization   
'National Institutes of Health/National Institute of Diabetes and Digestive and Kidney Disease (NIH/NIDDK)' 
_pdbx_audit_support.country                'United States' 
_pdbx_audit_support.grant_number           5R01DK046335-32 
_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   3TCT 
_pdbx_initial_refinement_model.details          'Search model was one TTR monomer with ligand removed.' 
# 
_atom_sites.entry_id                    8U52 
_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]   0.023277 
_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]   0.011737 
_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]   0.015686 
_atom_sites.fract_transf_vector[1]      0.00000 
_atom_sites.fract_transf_vector[2]      0.00000 
_atom_sites.fract_transf_vector[3]      0.00000 
_atom_sites.solution_primary            ? 
_atom_sites.solution_secondary          ? 
_atom_sites.solution_hydrogens          ? 
_atom_sites.special_details             ? 
# 
loop_
_atom_type.symbol 
C 
N 
O 
S 
# 
loop_
_atom_site.group_PDB 
_atom_site.id 
_atom_site.type_symbol 
_atom_site.label_atom_id 
_atom_site.label_alt_id 
_atom_site.label_comp_id 
_atom_site.label_asym_id 
_atom_site.label_entity_id 
_atom_site.label_seq_id 
_atom_site.pdbx_PDB_ins_code 
_atom_site.Cartn_x 
_atom_site.Cartn_y 
_atom_site.Cartn_z 
_atom_site.occupancy 
_atom_site.B_iso_or_equiv 
_atom_site.pdbx_formal_charge 
_atom_site.auth_seq_id 
_atom_site.auth_comp_id 
_atom_site.auth_asym_id 
_atom_site.auth_atom_id 
_atom_site.pdbx_PDB_model_num 
ATOM   1    N N   . CYS A 1 10  ? 6.718   11.210 -7.811  1.00 48.62 ? 10  CYS A N   1 
ATOM   2    C CA  . CYS A 1 10  ? 5.830   11.633 -6.667  1.00 39.95 ? 10  CYS A CA  1 
ATOM   3    C C   . CYS A 1 10  ? 6.598   11.473 -5.362  1.00 32.23 ? 10  CYS A C   1 
ATOM   4    O O   . CYS A 1 10  ? 6.762   10.375 -4.846  1.00 33.57 ? 10  CYS A O   1 
ATOM   5    C CB  . CYS A 1 10  ? 4.546   10.825 -6.622  1.00 45.02 ? 10  CYS A CB  1 
ATOM   6    S SG  . CYS A 1 10  ? 3.264   11.615 -5.613  1.00 51.10 ? 10  CYS A SG  1 
ATOM   7    N N   . PRO A 1 11  ? 7.163   12.558 -4.812  1.00 24.08 ? 11  PRO A N   1 
ATOM   8    C CA  . PRO A 1 11  ? 8.055   12.423 -3.669  1.00 21.99 ? 11  PRO A CA  1 
ATOM   9    C C   . PRO A 1 11  ? 7.341   12.376 -2.313  1.00 18.66 ? 11  PRO A C   1 
ATOM   10   O O   . PRO A 1 11  ? 8.003   12.122 -1.334  1.00 18.12 ? 11  PRO A O   1 
ATOM   11   C CB  . PRO A 1 11  ? 8.944   13.644 -3.786  1.00 25.41 ? 11  PRO A CB  1 
ATOM   12   C CG  . PRO A 1 11  ? 8.078   14.665 -4.412  1.00 24.53 ? 11  PRO A CG  1 
ATOM   13   C CD  . PRO A 1 11  ? 7.102   13.940 -5.322  1.00 26.25 ? 11  PRO A CD  1 
ATOM   14   N N   . LEU A 1 12  ? 6.063   12.695 -2.264  1.00 18.59 ? 12  LEU A N   1 
ATOM   15   C CA  . LEU A 1 12  ? 5.332   12.689 -0.944  1.00 17.42 ? 12  LEU A CA  1 
ATOM   16   C C   . LEU A 1 12  ? 3.950   12.164 -1.184  1.00 18.57 ? 12  LEU A C   1 
ATOM   17   O O   . LEU A 1 12  ? 3.165   12.820 -1.891  1.00 20.74 ? 12  LEU A O   1 
ATOM   18   C CB  . LEU A 1 12  ? 5.253   14.088 -0.362  1.00 18.87 ? 12  LEU A CB  1 
ATOM   19   C CG  . LEU A 1 12  ? 4.486   14.229 0.930   1.00 19.25 ? 12  LEU A CG  1 
ATOM   20   C CD1 . LEU A 1 12  ? 5.188   13.407 2.009   1.00 18.88 ? 12  LEU A CD1 1 
ATOM   21   C CD2 . LEU A 1 12  ? 4.411   15.679 1.328   1.00 21.18 ? 12  LEU A CD2 1 
ATOM   22   N N   . MET A 1 13  ? 3.662   10.992 -0.642  1.00 16.73 ? 13  MET A N   1 
ATOM   23   C CA  A MET A 1 13  ? 2.361   10.321 -0.782  0.50 17.37 ? 13  MET A CA  1 
ATOM   24   C CA  B MET A 1 13  ? 2.356   10.336 -0.776  0.50 17.88 ? 13  MET A CA  1 
ATOM   25   C C   . MET A 1 13  ? 1.819   10.039 0.628   1.00 16.39 ? 13  MET A C   1 
ATOM   26   O O   . MET A 1 13  ? 2.626   9.803  1.566   1.00 15.55 ? 13  MET A O   1 
ATOM   27   C CB  A MET A 1 13  ? 2.478   9.010  -1.568  0.50 20.67 ? 13  MET A CB  1 
ATOM   28   C CB  B MET A 1 13  ? 2.484   9.033  -1.562  0.50 22.03 ? 13  MET A CB  1 
ATOM   29   C CG  A MET A 1 13  ? 1.119   8.473  -2.025  0.50 23.88 ? 13  MET A CG  1 
ATOM   30   C CG  B MET A 1 13  ? 2.825   9.252  -3.009  0.50 26.87 ? 13  MET A CG  1 
ATOM   31   S SD  A MET A 1 13  ? 0.429   7.226  -0.926  0.50 32.11 ? 13  MET A SD  1 
ATOM   32   S SD  B MET A 1 13  ? 3.680   7.775  -3.613  0.50 35.53 ? 13  MET A SD  1 
ATOM   33   C CE  A MET A 1 13  ? 1.093   5.736  -1.673  0.50 30.37 ? 13  MET A CE  1 
ATOM   34   C CE  B MET A 1 13  ? 5.296   8.073  -2.897  0.50 31.32 ? 13  MET A CE  1 
ATOM   35   N N   . VAL A 1 14  ? 0.531   10.103 0.773   1.00 15.53 ? 14  VAL A N   1 
ATOM   36   C CA  . VAL A 1 14  ? -0.132  9.788  2.069   1.00 14.57 ? 14  VAL A CA  1 
ATOM   37   C C   . VAL A 1 14  ? -1.141  8.669  1.855   1.00 15.36 ? 14  VAL A C   1 
ATOM   38   O O   . VAL A 1 14  ? -1.929  8.733  0.851   1.00 17.09 ? 14  VAL A O   1 
ATOM   39   C CB  . VAL A 1 14  ? -0.763  11.032 2.692   1.00 15.03 ? 14  VAL A CB  1 
ATOM   40   C CG1 . VAL A 1 14  ? -1.445  10.690 4.013   1.00 16.32 ? 14  VAL A CG1 1 
ATOM   41   C CG2 . VAL A 1 14  ? 0.266   12.126 2.888   1.00 16.06 ? 14  VAL A CG2 1 
ATOM   42   N N   . LYS A 1 15  ? -1.053  7.646  2.689   1.00 15.08 ? 15  LYS A N   1 
ATOM   43   C CA  A LYS A 1 15  ? -2.005  6.494  2.662   0.50 16.26 ? 15  LYS A CA  1 
ATOM   44   C CA  B LYS A 1 15  ? -2.021  6.476  2.635   0.50 15.29 ? 15  LYS A CA  1 
ATOM   45   C C   . LYS A 1 15  ? -2.718  6.302  4.046   1.00 15.03 ? 15  LYS A C   1 
ATOM   46   O O   . LYS A 1 15  ? -2.145  6.327  5.209   1.00 15.54 ? 15  LYS A O   1 
ATOM   47   C CB  A LYS A 1 15  ? -1.233  5.220  2.327   0.50 19.25 ? 15  LYS A CB  1 
ATOM   48   C CB  B LYS A 1 15  ? -1.237  5.227  2.256   0.50 16.44 ? 15  LYS A CB  1 
ATOM   49   C CG  A LYS A 1 15  ? -1.410  4.693  0.914   0.50 26.14 ? 15  LYS A CG  1 
ATOM   50   C CG  B LYS A 1 15  ? -1.933  3.886  2.470   0.50 19.92 ? 15  LYS A CG  1 
ATOM   51   C CD  A LYS A 1 15  ? -1.432  3.185  0.852   0.50 28.48 ? 15  LYS A CD  1 
ATOM   52   C CD  B LYS A 1 15  ? -2.846  3.512  1.357   0.50 23.16 ? 15  LYS A CD  1 
ATOM   53   C CE  A LYS A 1 15  ? -0.503  2.605  -0.195  0.50 29.23 ? 15  LYS A CE  1 
ATOM   54   C CE  B LYS A 1 15  ? -3.000  2.011  1.224   0.50 25.16 ? 15  LYS A CE  1 
ATOM   55   N NZ  A LYS A 1 15  ? 0.905   2.460  0.283   0.50 30.82 ? 15  LYS A NZ  1 
ATOM   56   N NZ  B LYS A 1 15  ? -4.054  1.633  0.263   0.50 27.33 ? 15  LYS A NZ  1 
ATOM   57   N N   . VAL A 1 16  ? -4.038  6.224  3.963   1.00 13.22 ? 16  VAL A N   1 
ATOM   58   C CA  . VAL A 1 16  ? -4.802  6.179  5.217   1.00 12.87 ? 16  VAL A CA  1 
ATOM   59   C C   . VAL A 1 16  ? -5.771  4.991  5.165   1.00 13.03 ? 16  VAL A C   1 
ATOM   60   O O   . VAL A 1 16  ? -6.496  4.849  4.190   1.00 13.73 ? 16  VAL A O   1 
ATOM   61   C CB  . VAL A 1 16  ? -5.547  7.482  5.505   1.00 14.52 ? 16  VAL A CB  1 
ATOM   62   C CG1 . VAL A 1 16  ? -6.120  7.495  6.938   1.00 14.98 ? 16  VAL A CG1 1 
ATOM   63   C CG2 . VAL A 1 16  ? -4.647  8.729  5.278   1.00 14.32 ? 16  VAL A CG2 1 
ATOM   64   N N   . LEU A 1 17  ? -5.751  4.189  6.206   1.00 13.57 ? 17  LEU A N   1 
ATOM   65   C CA  . LEU A 1 17  ? -6.626  3.021  6.362   1.00 12.26 ? 17  LEU A CA  1 
ATOM   66   C C   . LEU A 1 17  ? -7.496  3.196  7.591   1.00 12.71 ? 17  LEU A C   1 
ATOM   67   O O   . LEU A 1 17  ? -7.090  3.834  8.582   1.00 12.66 ? 17  LEU A O   1 
ATOM   68   C CB  . LEU A 1 17  ? -5.723  1.789  6.474   1.00 13.83 ? 17  LEU A CB  1 
ATOM   69   C CG  . LEU A 1 17  ? -4.823  1.439  5.305   1.00 15.85 ? 17  LEU A CG  1 
ATOM   70   C CD1 . LEU A 1 17  ? -4.088  0.146  5.647   1.00 19.24 ? 17  LEU A CD1 1 
ATOM   71   C CD2 . LEU A 1 17  ? -5.609  1.230  4.036   1.00 20.31 ? 17  LEU A CD2 1 
ATOM   72   N N   . ASP A 1 18  ? -8.662  2.546  7.560   1.00 14.04 ? 18  ASP A N   1 
ATOM   73   C CA  . ASP A 1 18  ? -9.677  2.537  8.632   1.00 13.57 ? 18  ASP A CA  1 
ATOM   74   C C   . ASP A 1 18  ? -9.693  1.187  9.314   1.00 13.87 ? 18  ASP A C   1 
ATOM   75   O O   . ASP A 1 18  ? -9.978  0.174  8.604   1.00 14.39 ? 18  ASP A O   1 
ATOM   76   C CB  . ASP A 1 18  ? -11.001 2.927  8.010   1.00 14.96 ? 18  ASP A CB  1 
ATOM   77   C CG  . ASP A 1 18  ? -12.183 2.914  8.942   1.00 17.04 ? 18  ASP A CG  1 
ATOM   78   O OD1 . ASP A 1 18  ? -12.155 2.138  9.870   1.00 16.96 ? 18  ASP A OD1 1 
ATOM   79   O OD2 . ASP A 1 18  ? -13.098 3.795  8.764   1.00 18.70 ? 18  ASP A OD2 1 
ATOM   80   N N   . ALA A 1 19  ? -9.308  1.120  10.587  1.00 13.56 ? 19  ALA A N   1 
ATOM   81   C CA  . ALA A 1 19  ? -9.186  -0.130 11.333  1.00 13.79 ? 19  ALA A CA  1 
ATOM   82   C C   . ALA A 1 19  ? -10.543 -0.608 11.870  1.00 14.63 ? 19  ALA A C   1 
ATOM   83   O O   . ALA A 1 19  ? -10.539 -1.685 12.463  1.00 15.95 ? 19  ALA A O   1 
ATOM   84   C CB  . ALA A 1 19  ? -8.231  0.036  12.458  1.00 14.48 ? 19  ALA A CB  1 
ATOM   85   N N   . VAL A 1 20  ? -11.580 0.186  11.775  1.00 13.59 ? 20  VAL A N   1 
ATOM   86   C CA  . VAL A 1 20  ? -12.957 -0.187 12.187  1.00 15.01 ? 20  VAL A CA  1 
ATOM   87   C C   . VAL A 1 20  ? -13.644 -0.922 11.038  1.00 17.65 ? 20  VAL A C   1 
ATOM   88   O O   . VAL A 1 20  ? -14.249 -2.021 11.317  1.00 21.18 ? 20  VAL A O   1 
ATOM   89   C CB  . VAL A 1 20  ? -13.779 1.028  12.639  1.00 16.80 ? 20  VAL A CB  1 
ATOM   90   C CG1 . VAL A 1 20  ? -15.231 0.648  12.912  1.00 20.23 ? 20  VAL A CG1 1 
ATOM   91   C CG2 . VAL A 1 20  ? -13.177 1.675  13.868  1.00 18.11 ? 20  VAL A CG2 1 
ATOM   92   N N   . ARG A 1 21  ? -13.571 -0.367 9.836   1.00 16.13 ? 21  ARG A N   1 
ATOM   93   C CA  . ARG A 1 21  ? -14.271 -0.865 8.645   1.00 18.06 ? 21  ARG A CA  1 
ATOM   94   C C   . ARG A 1 21  ? -13.394 -1.839 7.876   1.00 16.91 ? 21  ARG A C   1 
ATOM   95   O O   . ARG A 1 21  ? -13.921 -2.600 7.019   1.00 20.76 ? 21  ARG A O   1 
ATOM   96   C CB  . ARG A 1 21  ? -14.718 0.307  7.787   1.00 21.72 ? 21  ARG A CB  1 
ATOM   97   C CG  . ARG A 1 21  ? -15.759 1.219  8.424   1.00 29.47 ? 21  ARG A CG  1 
ATOM   98   C CD  . ARG A 1 21  ? -15.855 2.528  7.646   1.00 36.74 ? 21  ARG A CD  1 
ATOM   99   N NE  . ARG A 1 21  ? -17.174 3.140  7.619   1.00 56.57 ? 21  ARG A NE  1 
ATOM   100  C CZ  . ARG A 1 21  ? -18.006 3.155  6.576   1.00 62.45 ? 21  ARG A CZ  1 
ATOM   101  N NH1 . ARG A 1 21  ? -17.672 2.576  5.434   1.00 65.31 ? 21  ARG A NH1 1 
ATOM   102  N NH2 . ARG A 1 21  ? -19.181 3.755  6.686   1.00 64.64 ? 21  ARG A NH2 1 
ATOM   103  N N   . GLY A 1 22  ? -12.091 -1.877 8.050   1.00 14.65 ? 22  GLY A N   1 
ATOM   104  C CA  . GLY A 1 22  ? -11.254 -2.731 7.212   1.00 13.82 ? 22  GLY A CA  1 
ATOM   105  C C   . GLY A 1 22  ? -11.218 -2.246 5.797   1.00 14.75 ? 22  GLY A C   1 
ATOM   106  O O   . GLY A 1 22  ? -11.365 -3.043 4.835   1.00 14.96 ? 22  GLY A O   1 
ATOM   107  N N   . SER A 1 23  ? -11.008 -0.942 5.593   1.00 14.41 ? 23  SER A N   1 
ATOM   108  C CA  . SER A 1 23  ? -11.138 -0.297 4.292   1.00 13.98 ? 23  SER A CA  1 
ATOM   109  C C   . SER A 1 23  ? -10.107 0.801  4.179   1.00 14.43 ? 23  SER A C   1 
ATOM   110  O O   . SER A 1 23  ? -9.589  1.226  5.223   1.00 15.49 ? 23  SER A O   1 
ATOM   111  C CB  . SER A 1 23  ? -12.526 0.236  4.180   1.00 17.53 ? 23  SER A CB  1 
ATOM   112  O OG  . SER A 1 23  ? -12.673 1.338  5.068   1.00 20.95 ? 23  SER A OG  1 
ATOM   113  N N   . PRO A 1 24  ? -9.849  1.277  2.980   1.00 13.91 ? 24  PRO A N   1 
ATOM   114  C CA  . PRO A 1 24  ? -9.210  2.580  2.836   1.00 14.84 ? 24  PRO A CA  1 
ATOM   115  C C   . PRO A 1 24  ? -10.053 3.596  3.584   1.00 15.36 ? 24  PRO A C   1 
ATOM   116  O O   . PRO A 1 24  ? -11.290 3.488  3.656   1.00 16.13 ? 24  PRO A O   1 
ATOM   117  C CB  . PRO A 1 24  ? -9.198  2.880  1.343   1.00 17.86 ? 24  PRO A CB  1 
ATOM   118  C CG  . PRO A 1 24  ? -10.102 1.891  0.744   1.00 24.48 ? 24  PRO A CG  1 
ATOM   119  C CD  . PRO A 1 24  ? -10.219 0.705  1.678   1.00 16.77 ? 24  PRO A CD  1 
ATOM   120  N N   . ALA A 1 25  ? -9.396  4.649  4.108   1.00 13.87 ? 25  ALA A N   1 
ATOM   121  C CA  . ALA A 1 25  ? -10.077 5.816  4.712   1.00 14.77 ? 25  ALA A CA  1 
ATOM   122  C C   . ALA A 1 25  ? -10.231 6.861  3.603   1.00 14.47 ? 25  ALA A C   1 
ATOM   123  O O   . ALA A 1 25  ? -9.194  7.388  3.114   1.00 16.02 ? 25  ALA A O   1 
ATOM   124  C CB  . ALA A 1 25  ? -9.328  6.361  5.879   1.00 14.90 ? 25  ALA A CB  1 
ATOM   125  N N   . ILE A 1 26  ? -11.435 6.996  3.070   1.00 15.87 ? 26  ILE A N   1 
ATOM   126  C CA  . ILE A 1 26  ? -11.707 7.795  1.848   1.00 17.11 ? 26  ILE A CA  1 
ATOM   127  C C   . ILE A 1 26  ? -12.101 9.210  2.242   1.00 16.14 ? 26  ILE A C   1 
ATOM   128  O O   . ILE A 1 26  ? -12.752 9.393  3.285   1.00 16.17 ? 26  ILE A O   1 
ATOM   129  C CB  . ILE A 1 26  ? -12.847 7.092  1.079   1.00 20.76 ? 26  ILE A CB  1 
ATOM   130  C CG1 . ILE A 1 26  ? -12.436 5.672  0.720   1.00 21.76 ? 26  ILE A CG1 1 
ATOM   131  C CG2 . ILE A 1 26  ? -13.289 7.884  -0.122  1.00 24.41 ? 26  ILE A CG2 1 
ATOM   132  C CD1 . ILE A 1 26  ? -13.632 4.814  0.267   1.00 28.62 ? 26  ILE A CD1 1 
ATOM   133  N N   . ASN A 1 27  ? -11.660 10.211 1.457   1.00 16.61 ? 27  ASN A N   1 
ATOM   134  C CA  A ASN A 1 27  ? -12.069 11.639 1.627   0.50 18.15 ? 27  ASN A CA  1 
ATOM   135  C CA  B ASN A 1 27  ? -12.139 11.615 1.655   0.50 18.79 ? 27  ASN A CA  1 
ATOM   136  C C   . ASN A 1 27  ? -11.567 12.183 2.964   1.00 17.56 ? 27  ASN A C   1 
ATOM   137  O O   . ASN A 1 27  ? -12.228 13.024 3.627   1.00 20.96 ? 27  ASN A O   1 
ATOM   138  C CB  A ASN A 1 27  ? -13.584 11.832 1.514   0.50 21.41 ? 27  ASN A CB  1 
ATOM   139  C CB  B ASN A 1 27  ? -13.681 11.669 1.659   0.50 22.66 ? 27  ASN A CB  1 
ATOM   140  C CG  A ASN A 1 27  ? -14.061 11.709 0.078   0.50 22.82 ? 27  ASN A CG  1 
ATOM   141  C CG  B ASN A 1 27  ? -14.287 13.004 1.249   0.50 27.36 ? 27  ASN A CG  1 
ATOM   142  O OD1 A ASN A 1 27  ? -13.387 12.146 -0.848  0.50 31.68 ? 27  ASN A OD1 1 
ATOM   143  O OD1 B ASN A 1 27  ? -14.193 13.408 0.090   0.50 38.49 ? 27  ASN A OD1 1 
ATOM   144  N ND2 A ASN A 1 27  ? -15.218 11.108 -0.112  0.50 29.24 ? 27  ASN A ND2 1 
ATOM   145  N ND2 B ASN A 1 27  ? -14.979 13.659 2.169   0.50 31.63 ? 27  ASN A ND2 1 
ATOM   146  N N   . VAL A 1 28  ? -10.375 11.742 3.334   1.00 15.51 ? 28  VAL A N   1 
ATOM   147  C CA  . VAL A 1 28  ? -9.694  12.263 4.538   1.00 16.15 ? 28  VAL A CA  1 
ATOM   148  C C   . VAL A 1 28  ? -8.904  13.499 4.104   1.00 13.77 ? 28  VAL A C   1 
ATOM   149  O O   . VAL A 1 28  ? -8.036  13.375 3.190   1.00 14.55 ? 28  VAL A O   1 
ATOM   150  C CB  . VAL A 1 28  ? -8.760  11.235 5.171   1.00 15.52 ? 28  VAL A CB  1 
ATOM   151  C CG1 . VAL A 1 28  ? -7.992  11.828 6.335   1.00 16.87 ? 28  VAL A CG1 1 
ATOM   152  C CG2 . VAL A 1 28  ? -9.559  9.994  5.618   1.00 16.79 ? 28  VAL A CG2 1 
ATOM   153  N N   . ALA A 1 29  ? -9.157  14.636 4.705   1.00 13.30 ? 29  ALA A N   1 
ATOM   154  C CA  . ALA A 1 29  ? -8.394  15.855 4.380   1.00 14.46 ? 29  ALA A CA  1 
ATOM   155  C C   . ALA A 1 29  ? -7.006  15.783 5.010   1.00 13.23 ? 29  ALA A C   1 
ATOM   156  O O   . ALA A 1 29  ? -6.849  15.280 6.140   1.00 13.86 ? 29  ALA A O   1 
ATOM   157  C CB  . ALA A 1 29  ? -9.138  17.063 4.883   1.00 13.53 ? 29  ALA A CB  1 
ATOM   158  N N   . VAL A 1 30  ? -6.017  16.229 4.248   1.00 13.23 ? 30  VAL A N   1 
ATOM   159  C CA  . VAL A 1 30  ? -4.585  16.234 4.647   1.00 13.79 ? 30  VAL A CA  1 
ATOM   160  C C   . VAL A 1 30  ? -4.007  17.603 4.340   1.00 13.77 ? 30  VAL A C   1 
ATOM   161  O O   . VAL A 1 30  ? -4.180  18.074 3.209   1.00 15.69 ? 30  VAL A O   1 
ATOM   162  C CB  . VAL A 1 30  ? -3.823  15.156 3.891   1.00 14.15 ? 30  VAL A CB  1 
ATOM   163  C CG1 . VAL A 1 30  ? -2.374  15.214 4.311   1.00 15.63 ? 30  VAL A CG1 1 
ATOM   164  C CG2 . VAL A 1 30  ? -4.405  13.768 4.103   1.00 14.46 ? 30  VAL A CG2 1 
ATOM   165  N N   . HIS A 1 31  ? -3.402  18.210 5.332   1.00 15.03 ? 31  HIS A N   1 
ATOM   166  C CA  . HIS A 1 31  ? -2.714  19.500 5.174   1.00 14.20 ? 31  HIS A CA  1 
ATOM   167  C C   . HIS A 1 31  ? -1.233  19.295 5.473   1.00 15.31 ? 31  HIS A C   1 
ATOM   168  O O   . HIS A 1 31  ? -0.905  18.761 6.539   1.00 17.49 ? 31  HIS A O   1 
ATOM   169  C CB  . HIS A 1 31  ? -3.318  20.526 6.111   1.00 15.40 ? 31  HIS A CB  1 
ATOM   170  C CG  . HIS A 1 31  ? -4.730  20.864 5.779   1.00 17.55 ? 31  HIS A CG  1 
ATOM   171  N ND1 . HIS A 1 31  ? -5.094  22.064 5.149   1.00 21.40 ? 31  HIS A ND1 1 
ATOM   172  C CD2 . HIS A 1 31  ? -5.874  20.191 6.006   1.00 20.05 ? 31  HIS A CD2 1 
ATOM   173  C CE1 . HIS A 1 31  ? -6.403  22.075 4.985   1.00 22.62 ? 31  HIS A CE1 1 
ATOM   174  N NE2 . HIS A 1 31  ? -6.914  20.957 5.495   1.00 20.05 ? 31  HIS A NE2 1 
ATOM   175  N N   . VAL A 1 32  ? -0.382  19.771 4.588   1.00 15.02 ? 32  VAL A N   1 
ATOM   176  C CA  . VAL A 1 32  ? 1.096   19.697 4.768   1.00 15.02 ? 32  VAL A CA  1 
ATOM   177  C C   . VAL A 1 32  ? 1.633   21.091 5.029   1.00 15.35 ? 32  VAL A C   1 
ATOM   178  O O   . VAL A 1 32  ? 1.172   22.016 4.326   1.00 15.94 ? 32  VAL A O   1 
ATOM   179  C CB  . VAL A 1 32  ? 1.774   19.040 3.592   1.00 14.93 ? 32  VAL A CB  1 
ATOM   180  C CG1 . VAL A 1 32  ? 3.222   18.834 3.896   1.00 17.35 ? 32  VAL A CG1 1 
ATOM   181  C CG2 . VAL A 1 32  ? 1.089   17.741 3.193   1.00 17.19 ? 32  VAL A CG2 1 
ATOM   182  N N   . PHE A 1 33  ? 2.487   21.199 6.042   1.00 14.76 ? 33  PHE A N   1 
ATOM   183  C CA  . PHE A 1 33  ? 3.148   22.492 6.388   1.00 16.44 ? 33  PHE A CA  1 
ATOM   184  C C   . PHE A 1 33  ? 4.633   22.271 6.361   1.00 16.75 ? 33  PHE A C   1 
ATOM   185  O O   . PHE A 1 33  ? 5.094   21.173 6.489   1.00 15.82 ? 33  PHE A O   1 
ATOM   186  C CB  . PHE A 1 33  ? 2.708   22.996 7.755   1.00 18.78 ? 33  PHE A CB  1 
ATOM   187  C CG  . PHE A 1 33  ? 1.214   23.137 7.900   1.00 18.97 ? 33  PHE A CG  1 
ATOM   188  C CD1 . PHE A 1 33  ? 0.449   22.035 8.229   1.00 20.29 ? 33  PHE A CD1 1 
ATOM   189  C CD2 . PHE A 1 33  ? 0.573   24.350 7.696   1.00 19.76 ? 33  PHE A CD2 1 
ATOM   190  C CE1 . PHE A 1 33  ? -0.928  22.115 8.372   1.00 20.56 ? 33  PHE A CE1 1 
ATOM   191  C CE2 . PHE A 1 33  ? -0.806  24.430 7.803   1.00 21.22 ? 33  PHE A CE2 1 
ATOM   192  C CZ  . PHE A 1 33  ? -1.563  23.311 8.078   1.00 21.28 ? 33  PHE A CZ  1 
ATOM   193  N N   . ARG A 1 34  ? 5.386   23.375 6.171   1.00 17.42 ? 34  ARG A N   1 
ATOM   194  C CA  . ARG A 1 34  ? 6.860   23.339 6.136   1.00 16.82 ? 34  ARG A CA  1 
ATOM   195  C C   . ARG A 1 34  ? 7.316   24.424 7.077   1.00 16.52 ? 34  ARG A C   1 
ATOM   196  O O   . ARG A 1 34  ? 6.788   25.557 7.000   1.00 18.60 ? 34  ARG A O   1 
ATOM   197  C CB  . ARG A 1 34  ? 7.457   23.578 4.758   1.00 17.50 ? 34  ARG A CB  1 
ATOM   198  C CG  . ARG A 1 34  ? 8.978   23.507 4.769   1.00 18.96 ? 34  ARG A CG  1 
ATOM   199  C CD  . ARG A 1 34  ? 9.469   23.830 3.397   1.00 20.81 ? 34  ARG A CD  1 
ATOM   200  N NE  . ARG A 1 34  ? 10.904  23.760 3.362   1.00 23.17 ? 34  ARG A NE  1 
ATOM   201  C CZ  . ARG A 1 34  ? 11.706  24.769 3.719   1.00 25.27 ? 34  ARG A CZ  1 
ATOM   202  N NH1 . ARG A 1 34  ? 11.207  25.958 4.038   1.00 23.08 ? 34  ARG A NH1 1 
ATOM   203  N NH2 . ARG A 1 34  ? 13.007  24.577 3.690   1.00 23.36 ? 34  ARG A NH2 1 
ATOM   204  N N   . LYS A 1 35  ? 8.208   24.128 7.979   1.00 16.81 ? 35  LYS A N   1 
ATOM   205  C CA  . LYS A 1 35  ? 8.730   25.148 8.902   1.00 18.07 ? 35  LYS A CA  1 
ATOM   206  C C   . LYS A 1 35  ? 9.586   26.170 8.148   1.00 18.70 ? 35  LYS A C   1 
ATOM   207  O O   . LYS A 1 35  ? 10.490  25.822 7.379   1.00 20.49 ? 35  LYS A O   1 
ATOM   208  C CB  . LYS A 1 35  ? 9.579   24.475 9.992   1.00 23.73 ? 35  LYS A CB  1 
ATOM   209  C CG  . LYS A 1 35  ? 9.745   25.247 11.269  1.00 32.41 ? 35  LYS A CG  1 
ATOM   210  C CD  . LYS A 1 35  ? 10.114  24.286 12.406  1.00 37.39 ? 35  LYS A CD  1 
ATOM   211  C CE  . LYS A 1 35  ? 9.448   24.614 13.731  1.00 47.54 ? 35  LYS A CE  1 
ATOM   212  N NZ  . LYS A 1 35  ? 10.299  24.176 14.867  1.00 51.52 ? 35  LYS A NZ  1 
ATOM   213  N N   . ALA A 1 36  ? 9.234   27.444 8.297   1.00 21.86 ? 36  ALA A N   1 
ATOM   214  C CA  . ALA A 1 36  ? 9.962   28.582 7.672   1.00 22.10 ? 36  ALA A CA  1 
ATOM   215  C C   . ALA A 1 36  ? 11.149  29.012 8.543   1.00 26.60 ? 36  ALA A C   1 
ATOM   216  O O   . ALA A 1 36  ? 11.313  28.484 9.635   1.00 25.02 ? 36  ALA A O   1 
ATOM   217  C CB  . ALA A 1 36  ? 8.998   29.710 7.439   1.00 24.53 ? 36  ALA A CB  1 
ATOM   218  N N   . ALA A 1 37  ? 11.980  29.896 7.999   1.00 29.34 ? 37  ALA A N   1 
ATOM   219  C CA  . ALA A 1 37  ? 13.227  30.347 8.651   1.00 34.81 ? 37  ALA A CA  1 
ATOM   220  C C   . ALA A 1 37  ? 12.939  30.953 10.021  1.00 34.75 ? 37  ALA A C   1 
ATOM   221  O O   . ALA A 1 37  ? 13.751  30.797 10.916  1.00 39.24 ? 37  ALA A O   1 
ATOM   222  C CB  . ALA A 1 37  ? 13.910  31.339 7.747   1.00 38.49 ? 37  ALA A CB  1 
ATOM   223  N N   . ASP A 1 38  ? 11.795  31.599 10.122  1.00 33.25 ? 38  ASP A N   1 
ATOM   224  C CA  . ASP A 1 38  ? 11.335  32.274 11.368  1.00 37.66 ? 38  ASP A CA  1 
ATOM   225  C C   . ASP A 1 38  ? 10.627  31.279 12.299  1.00 35.55 ? 38  ASP A C   1 
ATOM   226  O O   . ASP A 1 38  ? 10.005  31.748 13.264  1.00 41.36 ? 38  ASP A O   1 
ATOM   227  C CB  . ASP A 1 38  ? 10.473  33.486 11.003  1.00 36.66 ? 38  ASP A CB  1 
ATOM   228  C CG  . ASP A 1 38  ? 9.130   33.149 10.376  1.00 45.77 ? 38  ASP A CG  1 
ATOM   229  O OD1 . ASP A 1 38  ? 8.804   31.923 10.221  1.00 38.44 ? 38  ASP A OD1 1 
ATOM   230  O OD2 . ASP A 1 38  ? 8.393   34.104 10.052  1.00 48.56 ? 38  ASP A OD2 1 
ATOM   231  N N   . ASP A 1 39  ? 10.687  29.966 12.029  1.00 33.19 ? 39  ASP A N   1 
ATOM   232  C CA  . ASP A 1 39  ? 10.208  28.886 12.942  1.00 36.60 ? 39  ASP A CA  1 
ATOM   233  C C   . ASP A 1 39  ? 8.672   28.803 12.965  1.00 38.57 ? 39  ASP A C   1 
ATOM   234  O O   . ASP A 1 39  ? 8.137   28.029 13.784  1.00 43.13 ? 39  ASP A O   1 
ATOM   235  C CB  . ASP A 1 39  ? 10.761  29.035 14.368  1.00 40.56 ? 39  ASP A CB  1 
ATOM   236  C CG  . ASP A 1 39  ? 12.116  28.395 14.534  1.00 46.86 ? 39  ASP A CG  1 
ATOM   237  O OD1 . ASP A 1 39  ? 12.362  27.394 13.840  1.00 47.53 ? 39  ASP A OD1 1 
ATOM   238  O OD2 . ASP A 1 39  ? 12.929  28.923 15.339  1.00 61.58 ? 39  ASP A OD2 1 
ATOM   239  N N   . THR A 1 40  ? 7.988   29.498 12.068  1.00 32.18 ? 40  THR A N   1 
ATOM   240  C CA  . THR A 1 40  ? 6.522   29.346 11.865  1.00 33.05 ? 40  THR A CA  1 
ATOM   241  C C   . THR A 1 40  ? 6.247   28.248 10.832  1.00 29.32 ? 40  THR A C   1 
ATOM   242  O O   . THR A 1 40  ? 7.117   27.921 9.998   1.00 28.87 ? 40  THR A O   1 
ATOM   243  C CB  . THR A 1 40  ? 5.823   30.631 11.421  1.00 34.95 ? 40  THR A CB  1 
ATOM   244  O OG1 . THR A 1 40  ? 6.336   30.975 10.140  1.00 37.94 ? 40  THR A OG1 1 
ATOM   245  C CG2 . THR A 1 40  ? 6.021   31.767 12.404  1.00 41.53 ? 40  THR A CG2 1 
ATOM   246  N N   . TRP A 1 41  ? 5.094   27.622 10.979  1.00 28.78 ? 41  TRP A N   1 
ATOM   247  C CA  . TRP A 1 41  ? 4.573   26.629 10.029  1.00 25.81 ? 41  TRP A CA  1 
ATOM   248  C C   . TRP A 1 41  ? 3.937   27.351 8.866   1.00 29.12 ? 41  TRP A C   1 
ATOM   249  O O   . TRP A 1 41  ? 2.954   28.103 9.091   1.00 40.27 ? 41  TRP A O   1 
ATOM   250  C CB  . TRP A 1 41  ? 3.572   25.701 10.696  1.00 24.82 ? 41  TRP A CB  1 
ATOM   251  C CG  . TRP A 1 41  ? 4.187   24.767 11.673  1.00 28.27 ? 41  TRP A CG  1 
ATOM   252  C CD1 . TRP A 1 41  ? 4.068   24.795 13.028  1.00 32.21 ? 41  TRP A CD1 1 
ATOM   253  C CD2 . TRP A 1 41  ? 5.087   23.693 11.365  1.00 25.41 ? 41  TRP A CD2 1 
ATOM   254  N NE1 . TRP A 1 41  ? 4.771   23.760 13.586  1.00 35.18 ? 41  TRP A NE1 1 
ATOM   255  C CE2 . TRP A 1 41  ? 5.416   23.073 12.583  1.00 30.50 ? 41  TRP A CE2 1 
ATOM   256  C CE3 . TRP A 1 41  ? 5.584   23.168 10.178  1.00 22.37 ? 41  TRP A CE3 1 
ATOM   257  C CZ2 . TRP A 1 41  ? 6.263   21.969 12.642  1.00 30.11 ? 41  TRP A CZ2 1 
ATOM   258  C CZ3 . TRP A 1 41  ? 6.416   22.088 10.245  1.00 22.82 ? 41  TRP A CZ3 1 
ATOM   259  C CH2 . TRP A 1 41  ? 6.746   21.499 11.454  1.00 25.71 ? 41  TRP A CH2 1 
ATOM   260  N N   . GLU A 1 42  ? 4.455   27.131 7.693   1.00 21.15 ? 42  GLU A N   1 
ATOM   261  C CA  . GLU A 1 42  ? 3.880   27.704 6.468   1.00 22.95 ? 42  GLU A CA  1 
ATOM   262  C C   . GLU A 1 42  ? 3.094   26.632 5.737   1.00 21.57 ? 42  GLU A C   1 
ATOM   263  O O   . GLU A 1 42  ? 3.548   25.517 5.536   1.00 20.73 ? 42  GLU A O   1 
ATOM   264  C CB  . GLU A 1 42  ? 4.961   28.196 5.524   1.00 27.30 ? 42  GLU A CB  1 
ATOM   265  C CG  . GLU A 1 42  ? 5.660   29.441 6.023   1.00 36.81 ? 42  GLU A CG  1 
ATOM   266  C CD  . GLU A 1 42  ? 6.496   30.089 4.937   1.00 46.23 ? 42  GLU A CD  1 
ATOM   267  O OE1 . GLU A 1 42  ? 6.736   31.331 5.023   1.00 54.70 ? 42  GLU A OE1 1 
ATOM   268  O OE2 . GLU A 1 42  ? 6.914   29.337 3.999   1.00 51.18 ? 42  GLU A OE2 1 
ATOM   269  N N   . PRO A 1 43  ? 1.903   26.957 5.205   1.00 19.68 ? 43  PRO A N   1 
ATOM   270  C CA  . PRO A 1 43  ? 1.182   26.012 4.371   1.00 19.66 ? 43  PRO A CA  1 
ATOM   271  C C   . PRO A 1 43  ? 2.035   25.599 3.194   1.00 22.46 ? 43  PRO A C   1 
ATOM   272  O O   . PRO A 1 43  ? 2.695   26.448 2.530   1.00 24.81 ? 43  PRO A O   1 
ATOM   273  C CB  . PRO A 1 43  ? -0.069  26.775 3.917   1.00 22.39 ? 43  PRO A CB  1 
ATOM   274  C CG  . PRO A 1 43  ? -0.213  27.846 4.979   1.00 26.45 ? 43  PRO A CG  1 
ATOM   275  C CD  . PRO A 1 43  ? 1.199   28.246 5.376   1.00 24.80 ? 43  PRO A CD  1 
ATOM   276  N N   . PHE A 1 44  ? 2.073   24.300 2.889   1.00 17.70 ? 44  PHE A N   1 
ATOM   277  C CA  . PHE A 1 44  ? 2.871   23.727 1.797   1.00 16.60 ? 44  PHE A CA  1 
ATOM   278  C C   . PHE A 1 44  ? 2.020   23.083 0.707   1.00 18.02 ? 44  PHE A C   1 
ATOM   279  O O   . PHE A 1 44  ? 2.226   23.291 -0.487  1.00 20.03 ? 44  PHE A O   1 
ATOM   280  C CB  . PHE A 1 44  ? 3.933   22.768 2.357   1.00 17.42 ? 44  PHE A CB  1 
ATOM   281  C CG  . PHE A 1 44  ? 4.845   22.129 1.329   1.00 17.78 ? 44  PHE A CG  1 
ATOM   282  C CD1 . PHE A 1 44  ? 5.925   22.835 0.783   1.00 21.47 ? 44  PHE A CD1 1 
ATOM   283  C CD2 . PHE A 1 44  ? 4.697   20.828 0.907   1.00 17.49 ? 44  PHE A CD2 1 
ATOM   284  C CE1 . PHE A 1 44  ? 6.722   22.274 -0.199  1.00 17.29 ? 44  PHE A CE1 1 
ATOM   285  C CE2 . PHE A 1 44  ? 5.477   20.252 -0.087  1.00 19.28 ? 44  PHE A CE2 1 
ATOM   286  C CZ  . PHE A 1 44  ? 6.475   20.996 -0.691  1.00 19.58 ? 44  PHE A CZ  1 
ATOM   287  N N   . ALA A 1 45  ? 1.070   22.231 1.119   1.00 17.80 ? 45  ALA A N   1 
ATOM   288  C CA  . ALA A 1 45  ? 0.183   21.561 0.204   1.00 20.47 ? 45  ALA A CA  1 
ATOM   289  C C   . ALA A 1 45  ? -0.983  20.943 0.987   1.00 15.02 ? 45  ALA A C   1 
ATOM   290  O O   . ALA A 1 45  ? -0.898  20.758 2.192   1.00 17.36 ? 45  ALA A O   1 
ATOM   291  C CB  . ALA A 1 45  ? 0.949   20.440 -0.530  1.00 16.67 ? 45  ALA A CB  1 
ATOM   292  N N   . SER A 1 46  ? -2.048  20.579 0.233   1.00 14.62 ? 46  SER A N   1 
ATOM   293  C CA  . SER A 1 46  ? -3.181  19.914 0.868   1.00 14.66 ? 46  SER A CA  1 
ATOM   294  C C   . SER A 1 46  ? -3.931  19.123 -0.170  1.00 15.23 ? 46  SER A C   1 
ATOM   295  O O   . SER A 1 46  ? -3.782  19.318 -1.374  1.00 16.00 ? 46  SER A O   1 
ATOM   296  C CB  . SER A 1 46  ? -4.039  20.868 1.654   1.00 15.82 ? 46  SER A CB  1 
ATOM   297  O OG  . SER A 1 46  ? -4.747  21.778 0.772   1.00 15.92 ? 46  SER A OG  1 
ATOM   298  N N   . GLY A 1 47  ? -4.758  18.196 0.304   1.00 14.24 ? 47  GLY A N   1 
ATOM   299  C CA  . GLY A 1 47  ? -5.585  17.388 -0.577  1.00 15.27 ? 47  GLY A CA  1 
ATOM   300  C C   . GLY A 1 47  ? -6.423  16.425 0.240   1.00 14.82 ? 47  GLY A C   1 
ATOM   301  O O   . GLY A 1 47  ? -6.488  16.602 1.451   1.00 15.22 ? 47  GLY A O   1 
ATOM   302  N N   . LYS A 1 48  ? -7.111  15.531 -0.438  1.00 14.92 ? 48  LYS A N   1 
ATOM   303  C CA  . LYS A 1 48  ? -7.889  14.510 0.274   1.00 16.81 ? 48  LYS A CA  1 
ATOM   304  C C   . LYS A 1 48  ? -7.631  13.159 -0.336  1.00 14.45 ? 48  LYS A C   1 
ATOM   305  O O   . LYS A 1 48  ? -7.295  13.027 -1.465  1.00 16.12 ? 48  LYS A O   1 
ATOM   306  C CB  . LYS A 1 48  ? -9.362  14.861 0.325   1.00 23.14 ? 48  LYS A CB  1 
ATOM   307  C CG  . LYS A 1 48  ? -10.058 14.934 -0.990  1.00 29.36 ? 48  LYS A CG  1 
ATOM   308  C CD  . LYS A 1 48  ? -11.225 15.922 -0.901  1.00 43.40 ? 48  LYS A CD  1 
ATOM   309  C CE  . LYS A 1 48  ? -12.264 15.555 0.145   1.00 48.00 ? 48  LYS A CE  1 
ATOM   310  N NZ  . LYS A 1 48  ? -13.540 16.334 0.009   1.00 40.53 ? 48  LYS A NZ  1 
ATOM   311  N N   . THR A 1 49  ? -7.746  12.154 0.519   1.00 14.26 ? 49  THR A N   1 
ATOM   312  C CA  . THR A 1 49  ? -7.562  10.780 0.053   1.00 14.95 ? 49  THR A CA  1 
ATOM   313  C C   . THR A 1 49  ? -8.695  10.346 -0.907  1.00 15.75 ? 49  THR A C   1 
ATOM   314  O O   . THR A 1 49  ? -9.853  10.767 -0.752  1.00 17.11 ? 49  THR A O   1 
ATOM   315  C CB  . THR A 1 49  ? -7.428  9.777  1.194   1.00 13.91 ? 49  THR A CB  1 
ATOM   316  O OG1 . THR A 1 49  ? -8.650  9.752  1.936   1.00 14.57 ? 49  THR A OG1 1 
ATOM   317  C CG2 . THR A 1 49  ? -6.274  10.063 2.145   1.00 14.66 ? 49  THR A CG2 1 
ATOM   318  N N   . SER A 1 50  ? -8.275  9.541  -1.838  1.00 15.90 ? 50  SER A N   1 
ATOM   319  C CA  . SER A 1 50  ? -9.122  8.974  -2.897  1.00 16.66 ? 50  SER A CA  1 
ATOM   320  C C   . SER A 1 50  ? -9.924  7.788  -2.364  1.00 20.09 ? 50  SER A C   1 
ATOM   321  O O   . SER A 1 50  ? -9.775  7.371  -1.166  1.00 17.19 ? 50  SER A O   1 
ATOM   322  C CB  . SER A 1 50  ? -8.254  8.557  -4.011  1.00 19.13 ? 50  SER A CB  1 
ATOM   323  O OG  . SER A 1 50  ? -7.557  7.395  -3.620  1.00 20.85 ? 50  SER A OG  1 
ATOM   324  N N   . GLU A 1 51  ? -10.671 7.138  -3.265  1.00 20.63 ? 51  GLU A N   1 
ATOM   325  C CA  . GLU A 1 51  ? -11.382 5.882  -2.930  1.00 23.13 ? 51  GLU A CA  1 
ATOM   326  C C   . GLU A 1 51  ? -10.407 4.771  -2.531  1.00 19.36 ? 51  GLU A C   1 
ATOM   327  O O   . GLU A 1 51  ? -10.865 3.843  -1.833  1.00 21.75 ? 51  GLU A O   1 
ATOM   328  C CB  . GLU A 1 51  ? -12.277 5.489  -4.123  1.00 29.28 ? 51  GLU A CB  1 
ATOM   329  C CG  . GLU A 1 51  ? -13.325 6.569  -4.402  1.00 38.70 ? 51  GLU A CG  1 
ATOM   330  C CD  . GLU A 1 51  ? -14.566 6.610  -3.520  1.00 53.06 ? 51  GLU A CD  1 
ATOM   331  O OE1 . GLU A 1 51  ? -15.040 7.741  -3.195  1.00 58.86 ? 51  GLU A OE1 1 
ATOM   332  O OE2 . GLU A 1 51  ? -15.098 5.517  -3.190  1.00 69.61 ? 51  GLU A OE2 1 
ATOM   333  N N   . SER A 1 52  ? -9.125  4.843  -2.881  1.00 18.55 ? 52  SER A N   1 
ATOM   334  C CA  . SER A 1 52  ? -8.105  3.872  -2.463  1.00 19.41 ? 52  SER A CA  1 
ATOM   335  C C   . SER A 1 52  ? -7.424  4.262  -1.144  1.00 16.62 ? 52  SER A C   1 
ATOM   336  O O   . SER A 1 52  ? -6.525  3.559  -0.710  1.00 17.66 ? 52  SER A O   1 
ATOM   337  C CB  . SER A 1 52  ? -7.116  3.677  -3.569  1.00 23.28 ? 52  SER A CB  1 
ATOM   338  O OG  . SER A 1 52  ? -6.318  4.811  -3.751  1.00 26.97 ? 52  SER A OG  1 
ATOM   339  N N   . GLY A 1 53  ? -7.813  5.391  -0.532  1.00 16.76 ? 53  GLY A N   1 
ATOM   340  C CA  . GLY A 1 53  ? -7.155  5.885  0.693   1.00 16.06 ? 53  GLY A CA  1 
ATOM   341  C C   . GLY A 1 53  ? -5.830  6.545  0.426   1.00 16.09 ? 53  GLY A C   1 
ATOM   342  O O   . GLY A 1 53  ? -5.100  6.760  1.380   1.00 16.16 ? 53  GLY A O   1 
ATOM   343  N N   . GLU A 1 54  ? -5.566  6.895  -0.829  1.00 16.70 ? 54  GLU A N   1 
ATOM   344  C CA  . GLU A 1 54  ? -4.279  7.459  -1.220  1.00 15.66 ? 54  GLU A CA  1 
ATOM   345  C C   . GLU A 1 54  ? -4.395  8.902  -1.629  1.00 15.54 ? 54  GLU A C   1 
ATOM   346  O O   . GLU A 1 54  ? -5.408  9.348  -2.146  1.00 16.97 ? 54  GLU A O   1 
ATOM   347  C CB  . GLU A 1 54  ? -3.663  6.664  -2.371  1.00 19.75 ? 54  GLU A CB  1 
ATOM   348  C CG  . GLU A 1 54  ? -3.379  5.257  -1.974  1.00 25.15 ? 54  GLU A CG  1 
ATOM   349  C CD  . GLU A 1 54  ? -2.656  4.429  -3.011  1.00 34.42 ? 54  GLU A CD  1 
ATOM   350  O OE1 . GLU A 1 54  ? -2.525  4.880  -4.151  1.00 41.98 ? 54  GLU A OE1 1 
ATOM   351  O OE2 . GLU A 1 54  ? -2.328  3.308  -2.680  1.00 43.36 ? 54  GLU A OE2 1 
ATOM   352  N N   . LEU A 1 55  ? -3.366  9.671  -1.349  1.00 14.69 ? 55  LEU A N   1 
ATOM   353  C CA  . LEU A 1 55  ? -3.239  11.082 -1.761  1.00 14.00 ? 55  LEU A CA  1 
ATOM   354  C C   . LEU A 1 55  ? -1.879  11.253 -2.408  1.00 16.92 ? 55  LEU A C   1 
ATOM   355  O O   . LEU A 1 55  ? -0.866  11.097 -1.735  1.00 16.59 ? 55  LEU A O   1 
ATOM   356  C CB  . LEU A 1 55  ? -3.410  11.987 -0.549  1.00 15.10 ? 55  LEU A CB  1 
ATOM   357  C CG  . LEU A 1 55  ? -3.148  13.468 -0.746  1.00 16.75 ? 55  LEU A CG  1 
ATOM   358  C CD1 . LEU A 1 55  ? -3.961  13.995 -1.927  1.00 17.00 ? 55  LEU A CD1 1 
ATOM   359  C CD2 . LEU A 1 55  ? -3.536  14.175 0.539   1.00 16.59 ? 55  LEU A CD2 1 
ATOM   360  N N   . HIS A 1 56  ? -1.935  11.476 -3.726  1.00 19.36 ? 56  HIS A N   1 
ATOM   361  C CA  . HIS A 1 56  ? -0.778  11.688 -4.651  1.00 22.41 ? 56  HIS A CA  1 
ATOM   362  C C   . HIS A 1 56  ? -0.794  13.161 -5.110  1.00 21.49 ? 56  HIS A C   1 
ATOM   363  O O   . HIS A 1 56  ? -1.814  13.875 -4.923  1.00 23.53 ? 56  HIS A O   1 
ATOM   364  C CB  . HIS A 1 56  ? -0.924  10.750 -5.870  1.00 26.05 ? 56  HIS A CB  1 
ATOM   365  C CG  . HIS A 1 56  ? -0.885  9.298  -5.553  1.00 30.44 ? 56  HIS A CG  1 
ATOM   366  N ND1 . HIS A 1 56  ? 0.311   8.634  -5.384  1.00 37.98 ? 56  HIS A ND1 1 
ATOM   367  C CD2 . HIS A 1 56  ? -1.868  8.406  -5.316  1.00 35.90 ? 56  HIS A CD2 1 
ATOM   368  C CE1 . HIS A 1 56  ? 0.070   7.366  -5.103  1.00 39.61 ? 56  HIS A CE1 1 
ATOM   369  N NE2 . HIS A 1 56  ? -1.263  7.210  -5.026  1.00 41.32 ? 56  HIS A NE2 1 
ATOM   370  N N   . GLY A 1 57  ? 0.320   13.602 -5.674  1.00 22.94 ? 57  GLY A N   1 
ATOM   371  C CA  . GLY A 1 57  ? 0.319   14.888 -6.385  1.00 22.68 ? 57  GLY A CA  1 
ATOM   372  C C   . GLY A 1 57  ? 0.367   16.072 -5.462  1.00 23.86 ? 57  GLY A C   1 
ATOM   373  O O   . GLY A 1 57  ? -0.002  17.189 -5.885  1.00 26.98 ? 57  GLY A O   1 
ATOM   374  N N   . LEU A 1 58  ? 0.728   15.895 -4.192  1.00 20.54 ? 58  LEU A N   1 
ATOM   375  C CA  . LEU A 1 58  ? 0.866   17.018 -3.249  1.00 19.69 ? 58  LEU A CA  1 
ATOM   376  C C   . LEU A 1 58  ? 1.974   17.980 -3.677  1.00 19.45 ? 58  LEU A C   1 
ATOM   377  O O   . LEU A 1 58  ? 1.748   19.219 -3.501  1.00 22.40 ? 58  LEU A O   1 
ATOM   378  C CB  . LEU A 1 58  ? 1.130   16.484 -1.850  1.00 19.60 ? 58  LEU A CB  1 
ATOM   379  C CG  . LEU A 1 58  ? -0.094  15.890 -1.147  1.00 19.95 ? 58  LEU A CG  1 
ATOM   380  C CD1 . LEU A 1 58  ? 0.368   15.178 0.108   1.00 23.59 ? 58  LEU A CD1 1 
ATOM   381  C CD2 . LEU A 1 58  ? -1.067  17.016 -0.779  1.00 21.77 ? 58  LEU A CD2 1 
ATOM   382  N N   . THR A 1 59  ? 3.096   17.458 -4.153  1.00 19.88 ? 59  THR A N   1 
ATOM   383  C CA  . THR A 1 59  ? 4.239   18.350 -4.470  1.00 18.86 ? 59  THR A CA  1 
ATOM   384  C C   . THR A 1 59  ? 5.030   17.760 -5.607  1.00 20.83 ? 59  THR A C   1 
ATOM   385  O O   . THR A 1 59  ? 4.672   16.764 -6.201  1.00 23.31 ? 59  THR A O   1 
ATOM   386  C CB  . THR A 1 59  ? 5.055   18.581 -3.197  1.00 20.39 ? 59  THR A CB  1 
ATOM   387  O OG1 . THR A 1 59  ? 6.011   19.609 -3.461  1.00 20.62 ? 59  THR A OG1 1 
ATOM   388  C CG2 . THR A 1 59  ? 5.757   17.335 -2.737  1.00 18.60 ? 59  THR A CG2 1 
ATOM   389  N N   . THR A 1 60  ? 6.125   18.417 -5.923  1.00 22.11 ? 60  THR A N   1 
ATOM   390  C CA  . THR A 1 60  ? 7.032   18.016 -7.011  1.00 22.20 ? 60  THR A CA  1 
ATOM   391  C C   . THR A 1 60  ? 8.408   17.874 -6.391  1.00 21.15 ? 60  THR A C   1 
ATOM   392  O O   . THR A 1 60  ? 8.641   18.519 -5.347  1.00 20.69 ? 60  THR A O   1 
ATOM   393  C CB  . THR A 1 60  ? 7.052   19.061 -8.135  1.00 23.87 ? 60  THR A CB  1 
ATOM   394  O OG1 . THR A 1 60  ? 7.584   20.285 -7.644  1.00 24.59 ? 60  THR A OG1 1 
ATOM   395  C CG2 . THR A 1 60  ? 5.672   19.410 -8.646  1.00 28.81 ? 60  THR A CG2 1 
ATOM   396  N N   . GLU A 1 61  ? 9.302   17.155 -7.042  1.00 23.02 ? 61  GLU A N   1 
ATOM   397  C CA  . GLU A 1 61  ? 10.724  17.070 -6.637  1.00 27.22 ? 61  GLU A CA  1 
ATOM   398  C C   . GLU A 1 61  ? 11.339  18.462 -6.496  1.00 24.27 ? 61  GLU A C   1 
ATOM   399  O O   . GLU A 1 61  ? 12.061  18.697 -5.528  1.00 26.88 ? 61  GLU A O   1 
ATOM   400  C CB  . GLU A 1 61  ? 11.524  16.249 -7.645  1.00 33.42 ? 61  GLU A CB  1 
ATOM   401  C CG  . GLU A 1 61  ? 11.258  14.766 -7.543  1.00 40.29 ? 61  GLU A CG  1 
ATOM   402  C CD  . GLU A 1 61  ? 11.874  13.921 -8.643  1.00 48.80 ? 61  GLU A CD  1 
ATOM   403  O OE1 . GLU A 1 61  ? 12.401  14.502 -9.613  1.00 53.39 ? 61  GLU A OE1 1 
ATOM   404  O OE2 . GLU A 1 61  ? 11.828  12.679 -8.521  1.00 58.00 ? 61  GLU A OE2 1 
ATOM   405  N N   . GLU A 1 62  ? 11.026  19.401 -7.389  1.00 22.12 ? 62  GLU A N   1 
ATOM   406  C CA  . GLU A 1 62  ? 11.572  20.783 -7.324  1.00 22.60 ? 62  GLU A CA  1 
ATOM   407  C C   . GLU A 1 62  ? 11.132  21.537 -6.074  1.00 19.91 ? 62  GLU A C   1 
ATOM   408  O O   . GLU A 1 62  ? 11.927  22.223 -5.398  1.00 20.61 ? 62  GLU A O   1 
ATOM   409  C CB  . GLU A 1 62  ? 11.162  21.635 -8.530  1.00 30.09 ? 62  GLU A CB  1 
ATOM   410  C CG  . GLU A 1 62  ? 12.019  21.343 -9.724  1.00 37.68 ? 62  GLU A CG  1 
ATOM   411  C CD  . GLU A 1 62  ? 11.957  22.387 -10.824 1.00 39.45 ? 62  GLU A CD  1 
ATOM   412  O OE1 . GLU A 1 62  ? 11.215  23.404 -10.645 1.00 39.94 ? 62  GLU A OE1 1 
ATOM   413  O OE2 . GLU A 1 62  ? 12.660  22.185 -11.849 1.00 45.73 ? 62  GLU A OE2 1 
ATOM   414  N N   . GLU A 1 63  ? 9.848   21.476 -5.747  1.00 18.45 ? 63  GLU A N   1 
ATOM   415  C CA  A GLU A 1 63  ? 9.296   22.274 -4.632  0.50 18.34 ? 63  GLU A CA  1 
ATOM   416  C CA  B GLU A 1 63  ? 9.261   22.242 -4.644  0.50 18.52 ? 63  GLU A CA  1 
ATOM   417  C C   . GLU A 1 63  ? 9.576   21.616 -3.268  1.00 15.13 ? 63  GLU A C   1 
ATOM   418  O O   . GLU A 1 63  ? 9.618   22.345 -2.270  1.00 17.98 ? 63  GLU A O   1 
ATOM   419  C CB  A GLU A 1 63  ? 7.810   22.543 -4.841  0.50 21.54 ? 63  GLU A CB  1 
ATOM   420  C CB  B GLU A 1 63  ? 7.771   22.252 -4.912  0.50 22.10 ? 63  GLU A CB  1 
ATOM   421  C CG  A GLU A 1 63  ? 7.607   23.581 -5.936  0.50 22.90 ? 63  GLU A CG  1 
ATOM   422  C CG  B GLU A 1 63  ? 7.017   23.112 -3.954  0.50 24.94 ? 63  GLU A CG  1 
ATOM   423  C CD  A GLU A 1 63  ? 6.217   24.128 -6.198  0.50 28.53 ? 63  GLU A CD  1 
ATOM   424  C CD  B GLU A 1 63  ? 5.531   23.007 -4.241  0.50 26.50 ? 63  GLU A CD  1 
ATOM   425  O OE1 A GLU A 1 63  ? 5.229   23.362 -6.090  0.50 27.30 ? 63  GLU A OE1 1 
ATOM   426  O OE1 B GLU A 1 63  ? 4.897   22.031 -3.742  0.50 21.04 ? 63  GLU A OE1 1 
ATOM   427  O OE2 A GLU A 1 63  ? 6.143   25.333 -6.598  0.50 28.37 ? 63  GLU A OE2 1 
ATOM   428  O OE2 B GLU A 1 63  ? 5.041   23.853 -5.041  0.50 33.53 ? 63  GLU A OE2 1 
ATOM   429  N N   . PHE A 1 64  ? 9.767   20.302 -3.280  1.00 16.64 ? 64  PHE A N   1 
ATOM   430  C CA  . PHE A 1 64  ? 9.933   19.531 -2.030  1.00 16.37 ? 64  PHE A CA  1 
ATOM   431  C C   . PHE A 1 64  ? 11.397  19.548 -1.574  1.00 15.38 ? 64  PHE A C   1 
ATOM   432  O O   . PHE A 1 64  ? 12.121  18.521 -1.667  1.00 16.55 ? 64  PHE A O   1 
ATOM   433  C CB  . PHE A 1 64  ? 9.411   18.126 -2.200  1.00 16.42 ? 64  PHE A CB  1 
ATOM   434  C CG  . PHE A 1 64  ? 9.285   17.298 -0.939  1.00 16.92 ? 64  PHE A CG  1 
ATOM   435  C CD1 . PHE A 1 64  ? 8.753   17.806 0.224   1.00 17.97 ? 64  PHE A CD1 1 
ATOM   436  C CD2 . PHE A 1 64  ? 9.644   15.981 -1.004  1.00 19.80 ? 64  PHE A CD2 1 
ATOM   437  C CE1 . PHE A 1 64  ? 8.640   17.024 1.381   1.00 17.89 ? 64  PHE A CE1 1 
ATOM   438  C CE2 . PHE A 1 64  ? 9.490   15.181 0.126   1.00 20.54 ? 64  PHE A CE2 1 
ATOM   439  C CZ  . PHE A 1 64  ? 8.984   15.707 1.279   1.00 18.24 ? 64  PHE A CZ  1 
ATOM   440  N N   . VAL A 1 65  ? 11.821  20.722 -1.157  1.00 15.09 ? 65  VAL A N   1 
ATOM   441  C CA  . VAL A 1 65  ? 13.230  20.896 -0.787  1.00 15.16 ? 65  VAL A CA  1 
ATOM   442  C C   . VAL A 1 65  ? 13.468  20.383 0.633   1.00 15.37 ? 65  VAL A C   1 
ATOM   443  O O   . VAL A 1 65  ? 12.491  19.930 1.324   1.00 16.05 ? 65  VAL A O   1 
ATOM   444  C CB  . VAL A 1 65  ? 13.551  22.394 -0.828  1.00 14.72 ? 65  VAL A CB  1 
ATOM   445  C CG1 . VAL A 1 65  ? 13.505  22.911 -2.275  1.00 16.61 ? 65  VAL A CG1 1 
ATOM   446  C CG2 . VAL A 1 65  ? 12.656  23.207 0.049   1.00 17.19 ? 65  VAL A CG2 1 
ATOM   447  N N   . GLU A 1 66  ? 14.698  20.447 1.121   1.00 16.00 ? 66  GLU A N   1 
ATOM   448  C CA  A GLU A 1 66  ? 15.014  20.073 2.523   0.50 16.26 ? 66  GLU A CA  1 
ATOM   449  C CA  B GLU A 1 66  ? 15.041  20.101 2.524   0.50 16.72 ? 66  GLU A CA  1 
ATOM   450  C C   . GLU A 1 66  ? 14.159  20.910 3.459   1.00 17.44 ? 66  GLU A C   1 
ATOM   451  O O   . GLU A 1 66  ? 13.905  22.113 3.171   1.00 19.46 ? 66  GLU A O   1 
ATOM   452  C CB  A GLU A 1 66  ? 16.493  20.302 2.853   0.50 18.45 ? 66  GLU A CB  1 
ATOM   453  C CB  B GLU A 1 66  ? 16.487  20.490 2.845   0.50 19.26 ? 66  GLU A CB  1 
ATOM   454  C CG  A GLU A 1 66  ? 16.879  19.799 4.236   0.50 19.01 ? 66  GLU A CG  1 
ATOM   455  C CG  B GLU A 1 66  ? 17.539  19.578 2.291   0.50 21.91 ? 66  GLU A CG  1 
ATOM   456  C CD  A GLU A 1 66  ? 16.584  20.681 5.447   0.50 23.69 ? 66  GLU A CD  1 
ATOM   457  C CD  B GLU A 1 66  ? 18.887  19.859 2.948   0.50 23.43 ? 66  GLU A CD  1 
ATOM   458  O OE1 A GLU A 1 66  ? 16.454  21.889 5.283   0.50 26.13 ? 66  GLU A OE1 1 
ATOM   459  O OE1 B GLU A 1 66  ? 19.628  20.717 2.470   0.50 17.04 ? 66  GLU A OE1 1 
ATOM   460  O OE2 A GLU A 1 66  ? 16.456  20.146 6.592   0.50 25.58 ? 66  GLU A OE2 1 
ATOM   461  O OE2 B GLU A 1 66  ? 19.143  19.266 4.006   0.50 23.81 ? 66  GLU A OE2 1 
ATOM   462  N N   . GLY A 1 67  ? 13.707  20.349 4.570   1.00 16.55 ? 67  GLY A N   1 
ATOM   463  C CA  . GLY A 1 67  ? 13.003  21.124 5.554   1.00 16.60 ? 67  GLY A CA  1 
ATOM   464  C C   . GLY A 1 67  ? 12.370  20.229 6.597   1.00 15.45 ? 67  GLY A C   1 
ATOM   465  O O   . GLY A 1 67  ? 12.508  19.004 6.457   1.00 15.57 ? 67  GLY A O   1 
ATOM   466  N N   . ILE A 1 68  ? 11.725  20.862 7.530   1.00 14.57 ? 68  ILE A N   1 
ATOM   467  C CA  . ILE A 1 68  ? 10.906  20.130 8.534   1.00 14.29 ? 68  ILE A CA  1 
ATOM   468  C C   . ILE A 1 68  ? 9.479   20.276 8.051   1.00 15.08 ? 68  ILE A C   1 
ATOM   469  O O   . ILE A 1 68  ? 8.967   21.382 7.889   1.00 15.84 ? 68  ILE A O   1 
ATOM   470  C CB  . ILE A 1 68  ? 11.137  20.658 9.942   1.00 16.22 ? 68  ILE A CB  1 
ATOM   471  C CG1 . ILE A 1 68  ? 12.603  20.458 10.363  1.00 20.20 ? 68  ILE A CG1 1 
ATOM   472  C CG2 . ILE A 1 68  ? 10.153  19.963 10.864  1.00 17.58 ? 68  ILE A CG2 1 
ATOM   473  C CD1 . ILE A 1 68  ? 12.946  21.060 11.717  1.00 24.21 ? 68  ILE A CD1 1 
ATOM   474  N N   . TYR A 1 69  ? 8.806   19.149 7.838   1.00 14.22 ? 69  TYR A N   1 
ATOM   475  C CA  . TYR A 1 69  ? 7.450   19.103 7.310   1.00 13.77 ? 69  TYR A CA  1 
ATOM   476  C C   . TYR A 1 69  ? 6.491   18.546 8.369   1.00 13.75 ? 69  TYR A C   1 
ATOM   477  O O   . TYR A 1 69  ? 6.909   17.687 9.160   1.00 14.15 ? 69  TYR A O   1 
ATOM   478  C CB  . TYR A 1 69  ? 7.394   18.273 6.035   1.00 13.92 ? 69  TYR A CB  1 
ATOM   479  C CG  . TYR A 1 69  ? 8.109   18.903 4.863   1.00 15.11 ? 69  TYR A CG  1 
ATOM   480  C CD1 . TYR A 1 69  ? 9.475   18.822 4.760   1.00 15.78 ? 69  TYR A CD1 1 
ATOM   481  C CD2 . TYR A 1 69  ? 7.405   19.673 3.950   1.00 15.19 ? 69  TYR A CD2 1 
ATOM   482  C CE1 . TYR A 1 69  ? 10.130  19.403 3.675   1.00 15.56 ? 69  TYR A CE1 1 
ATOM   483  C CE2 . TYR A 1 69  ? 8.042   20.296 2.894   1.00 15.29 ? 69  TYR A CE2 1 
ATOM   484  C CZ  . TYR A 1 69  ? 9.405   20.181 2.775   1.00 16.76 ? 69  TYR A CZ  1 
ATOM   485  O OH  . TYR A 1 69  ? 10.032  20.802 1.694   1.00 16.82 ? 69  TYR A OH  1 
ATOM   486  N N   . LYS A 1 70  ? 5.293   19.004 8.339   1.00 14.35 ? 70  LYS A N   1 
ATOM   487  C CA  . LYS A 1 70  ? 4.214   18.493 9.210   1.00 14.21 ? 70  LYS A CA  1 
ATOM   488  C C   . LYS A 1 70  ? 3.085   18.059 8.300   1.00 15.39 ? 70  LYS A C   1 
ATOM   489  O O   . LYS A 1 70  ? 2.536   18.892 7.554   1.00 15.59 ? 70  LYS A O   1 
ATOM   490  C CB  . LYS A 1 70  ? 3.716   19.562 10.161  1.00 16.67 ? 70  LYS A CB  1 
ATOM   491  C CG  . LYS A 1 70  ? 2.500   19.099 10.954  1.00 21.51 ? 70  LYS A CG  1 
ATOM   492  C CD  . LYS A 1 70  ? 2.156   20.019 12.071  1.00 27.05 ? 70  LYS A CD  1 
ATOM   493  C CE  . LYS A 1 70  ? 1.802   21.395 11.598  1.00 31.37 ? 70  LYS A CE  1 
ATOM   494  N NZ  . LYS A 1 70  ? 1.173   22.203 12.687  1.00 39.91 ? 70  LYS A NZ  1 
ATOM   495  N N   . VAL A 1 71  ? 2.719   16.802 8.394   1.00 14.20 ? 71  VAL A N   1 
ATOM   496  C CA  . VAL A 1 71  ? 1.552   16.222 7.680   1.00 14.60 ? 71  VAL A CA  1 
ATOM   497  C C   . VAL A 1 71  ? 0.418   16.079 8.659   1.00 14.36 ? 71  VAL A C   1 
ATOM   498  O O   . VAL A 1 71  ? 0.555   15.261 9.598   1.00 16.54 ? 71  VAL A O   1 
ATOM   499  C CB  . VAL A 1 71  ? 1.903   14.893 7.006   1.00 14.15 ? 71  VAL A CB  1 
ATOM   500  C CG1 . VAL A 1 71  ? 0.667   14.268 6.347   1.00 16.18 ? 71  VAL A CG1 1 
ATOM   501  C CG2 . VAL A 1 71  ? 2.964   15.116 5.975   1.00 16.59 ? 71  VAL A CG2 1 
ATOM   502  N N   . GLU A 1 72  ? -0.606  16.891 8.543   1.00 14.28 ? 72  GLU A N   1 
ATOM   503  C CA  A GLU A 1 72  ? -1.766  16.924 9.451   0.50 14.85 ? 72  GLU A CA  1 
ATOM   504  C CA  B GLU A 1 72  ? -1.745  16.874 9.476   0.50 14.70 ? 72  GLU A CA  1 
ATOM   505  C C   . GLU A 1 72  ? -2.873  16.137 8.769   1.00 15.52 ? 72  GLU A C   1 
ATOM   506  O O   . GLU A 1 72  ? -3.332  16.555 7.717   1.00 16.30 ? 72  GLU A O   1 
ATOM   507  C CB  A GLU A 1 72  ? -2.180  18.374 9.693   0.50 16.67 ? 72  GLU A CB  1 
ATOM   508  C CB  B GLU A 1 72  ? -2.129  18.280 9.931   0.50 16.37 ? 72  GLU A CB  1 
ATOM   509  C CG  A GLU A 1 72  ? -3.078  18.574 10.888  0.50 18.98 ? 72  GLU A CG  1 
ATOM   510  C CG  B GLU A 1 72  ? -3.587  18.381 10.332  0.50 18.20 ? 72  GLU A CG  1 
ATOM   511  C CD  A GLU A 1 72  ? -3.050  20.011 11.388  0.50 21.36 ? 72  GLU A CD  1 
ATOM   512  C CD  B GLU A 1 72  ? -4.132  19.789 10.450  0.50 23.07 ? 72  GLU A CD  1 
ATOM   513  O OE1 A GLU A 1 72  ? -3.493  20.904 10.635  0.50 25.84 ? 72  GLU A OE1 1 
ATOM   514  O OE1 B GLU A 1 72  ? -5.201  20.044 9.816   0.50 25.31 ? 72  GLU A OE1 1 
ATOM   515  O OE2 A GLU A 1 72  ? -2.563  20.229 12.495  0.50 26.23 ? 72  GLU A OE2 1 
ATOM   516  O OE2 B GLU A 1 72  ? -3.505  20.603 11.207  0.50 25.80 ? 72  GLU A OE2 1 
ATOM   517  N N   . ILE A 1 73  ? -3.300  15.026 9.362   1.00 14.11 ? 73  ILE A N   1 
ATOM   518  C CA  . ILE A 1 73  ? -4.366  14.198 8.790   1.00 13.68 ? 73  ILE A CA  1 
ATOM   519  C C   . ILE A 1 73  ? -5.631  14.473 9.588   1.00 13.78 ? 73  ILE A C   1 
ATOM   520  O O   . ILE A 1 73  ? -5.589  14.281 10.842  1.00 14.32 ? 73  ILE A O   1 
ATOM   521  C CB  . ILE A 1 73  ? -3.946  12.719 8.857   1.00 14.62 ? 73  ILE A CB  1 
ATOM   522  C CG1 . ILE A 1 73  ? -2.614  12.495 8.142   1.00 15.06 ? 73  ILE A CG1 1 
ATOM   523  C CG2 . ILE A 1 73  ? -5.049  11.812 8.335   1.00 14.34 ? 73  ILE A CG2 1 
ATOM   524  C CD1 . ILE A 1 73  ? -2.032  11.119 8.323   1.00 17.45 ? 73  ILE A CD1 1 
ATOM   525  N N   . ASP A 1 74  ? -6.689  14.912 8.938   1.00 13.61 ? 74  ASP A N   1 
ATOM   526  C CA  . ASP A 1 74  ? -7.867  15.443 9.664   1.00 14.16 ? 74  ASP A CA  1 
ATOM   527  C C   . ASP A 1 74  ? -8.796  14.278 10.043  1.00 14.81 ? 74  ASP A C   1 
ATOM   528  O O   . ASP A 1 74  ? -9.841  14.043 9.460   1.00 15.57 ? 74  ASP A O   1 
ATOM   529  C CB  . ASP A 1 74  ? -8.496  16.564 8.863   1.00 17.03 ? 74  ASP A CB  1 
ATOM   530  C CG  . ASP A 1 74  ? -7.584  17.785 8.757   1.00 24.76 ? 74  ASP A CG  1 
ATOM   531  O OD1 . ASP A 1 74  ? -6.747  18.062 9.717   1.00 25.70 ? 74  ASP A OD1 1 
ATOM   532  O OD2 . ASP A 1 74  ? -7.776  18.524 7.771   1.00 28.22 ? 74  ASP A OD2 1 
ATOM   533  N N   . THR A 1 75  ? -8.354  13.510 11.038  1.00 14.12 ? 75  THR A N   1 
ATOM   534  C CA  . THR A 1 75  ? -9.055  12.288 11.484  1.00 14.21 ? 75  THR A CA  1 
ATOM   535  C C   . THR A 1 75  ? -10.380 12.625 12.173  1.00 16.24 ? 75  THR A C   1 
ATOM   536  O O   . THR A 1 75  ? -11.283 11.850 12.031  1.00 17.64 ? 75  THR A O   1 
ATOM   537  C CB  . THR A 1 75  ? -8.134  11.513 12.444  1.00 15.19 ? 75  THR A CB  1 
ATOM   538  O OG1 . THR A 1 75  ? -7.836  12.296 13.587  1.00 15.42 ? 75  THR A OG1 1 
ATOM   539  C CG2 . THR A 1 75  ? -6.849  11.075 11.767  1.00 15.05 ? 75  THR A CG2 1 
ATOM   540  N N   . LYS A 1 76  ? -10.474 13.720 12.905  1.00 16.16 ? 76  LYS A N   1 
ATOM   541  C CA  . LYS A 1 76  ? -11.737 14.049 13.617  1.00 18.28 ? 76  LYS A CA  1 
ATOM   542  C C   . LYS A 1 76  ? -12.876 14.280 12.608  1.00 18.62 ? 76  LYS A C   1 
ATOM   543  O O   . LYS A 1 76  ? -13.929 13.618 12.833  1.00 21.22 ? 76  LYS A O   1 
ATOM   544  C CB  . LYS A 1 76  ? -11.529 15.273 14.482  1.00 19.41 ? 76  LYS A CB  1 
ATOM   545  C CG  . LYS A 1 76  ? -12.779 15.585 15.277  1.00 23.57 ? 76  LYS A CG  1 
ATOM   546  C CD  . LYS A 1 76  ? -12.564 16.741 16.206  1.00 26.10 ? 76  LYS A CD  1 
ATOM   547  C CE  . LYS A 1 76  ? -13.675 16.841 17.211  1.00 33.76 ? 76  LYS A CE  1 
ATOM   548  N NZ  . LYS A 1 76  ? -13.430 18.004 18.095  1.00 40.58 ? 76  LYS A NZ  1 
ATOM   549  N N   . SER A 1 77  ? -12.619 15.021 11.538  1.00 20.51 ? 77  SER A N   1 
ATOM   550  C CA  . SER A 1 77  ? -13.625 15.258 10.446  1.00 22.18 ? 77  SER A CA  1 
ATOM   551  C C   . SER A 1 77  ? -14.026 13.924 9.851   1.00 25.39 ? 77  SER A C   1 
ATOM   552  O O   . SER A 1 77  ? -15.207 13.652 9.617   1.00 25.48 ? 77  SER A O   1 
ATOM   553  C CB  . SER A 1 77  ? -13.160 16.247 9.413   1.00 28.64 ? 77  SER A CB  1 
ATOM   554  O OG  . SER A 1 77  ? -12.842 17.497 10.011  1.00 34.41 ? 77  SER A OG  1 
ATOM   555  N N   . TYR A 1 78  ? -13.058 13.039 9.612   1.00 20.70 ? 78  TYR A N   1 
ATOM   556  C CA  . TYR A 1 78  ? -13.366 11.698 9.079   1.00 22.20 ? 78  TYR A CA  1 
ATOM   557  C C   . TYR A 1 78  ? -14.345 10.929 9.970   1.00 23.65 ? 78  TYR A C   1 
ATOM   558  O O   . TYR A 1 78  ? -15.338 10.394 9.459   1.00 25.25 ? 78  TYR A O   1 
ATOM   559  C CB  . TYR A 1 78  ? -12.055 10.951 8.870   1.00 18.82 ? 78  TYR A CB  1 
ATOM   560  C CG  . TYR A 1 78  ? -12.245 9.535  8.386   1.00 17.13 ? 78  TYR A CG  1 
ATOM   561  C CD1 . TYR A 1 78  ? -12.583 9.261  7.072   1.00 17.94 ? 78  TYR A CD1 1 
ATOM   562  C CD2 . TYR A 1 78  ? -12.145 8.450  9.258   1.00 16.78 ? 78  TYR A CD2 1 
ATOM   563  C CE1 . TYR A 1 78  ? -12.762 7.979  6.635   1.00 17.79 ? 78  TYR A CE1 1 
ATOM   564  C CE2 . TYR A 1 78  ? -12.333 7.150  8.854   1.00 16.81 ? 78  TYR A CE2 1 
ATOM   565  C CZ  . TYR A 1 78  ? -12.614 6.910  7.511   1.00 16.71 ? 78  TYR A CZ  1 
ATOM   566  O OH  . TYR A 1 78  ? -12.847 5.687  7.003   1.00 19.57 ? 78  TYR A OH  1 
ATOM   567  N N   . TRP A 1 79  ? -14.075 10.791 11.263  1.00 18.36 ? 79  TRP A N   1 
ATOM   568  C CA  . TRP A 1 79  ? -14.837 9.943  12.200  1.00 18.33 ? 79  TRP A CA  1 
ATOM   569  C C   . TRP A 1 79  ? -16.228 10.586 12.371  1.00 25.18 ? 79  TRP A C   1 
ATOM   570  O O   . TRP A 1 79  ? -17.183 9.805  12.502  1.00 27.53 ? 79  TRP A O   1 
ATOM   571  C CB  . TRP A 1 79  ? -14.152 9.751  13.535  1.00 18.90 ? 79  TRP A CB  1 
ATOM   572  C CG  . TRP A 1 79  ? -12.976 8.858  13.429  1.00 17.96 ? 79  TRP A CG  1 
ATOM   573  C CD1 . TRP A 1 79  ? -11.678 9.206  13.695  1.00 15.27 ? 79  TRP A CD1 1 
ATOM   574  C CD2 . TRP A 1 79  ? -12.965 7.472  13.057  1.00 17.81 ? 79  TRP A CD2 1 
ATOM   575  N NE1 . TRP A 1 79  ? -10.882 8.102  13.505  1.00 14.25 ? 79  TRP A NE1 1 
ATOM   576  C CE2 . TRP A 1 79  ? -11.628 7.034  13.058  1.00 16.81 ? 79  TRP A CE2 1 
ATOM   577  C CE3 . TRP A 1 79  ? -13.959 6.544  12.683  1.00 18.97 ? 79  TRP A CE3 1 
ATOM   578  C CZ2 . TRP A 1 79  ? -11.244 5.734  12.751  1.00 18.42 ? 79  TRP A CZ2 1 
ATOM   579  C CZ3 . TRP A 1 79  ? -13.553 5.264  12.343  1.00 19.70 ? 79  TRP A CZ3 1 
ATOM   580  C CH2 . TRP A 1 79  ? -12.236 4.869  12.333  1.00 20.52 ? 79  TRP A CH2 1 
ATOM   581  N N   . LYS A 1 80  ? -16.264 11.892 12.424  1.00 25.12 ? 80  LYS A N   1 
ATOM   582  C CA  . LYS A 1 80  ? -17.544 12.616 12.721  1.00 33.35 ? 80  LYS A CA  1 
ATOM   583  C C   . LYS A 1 80  ? -18.566 12.294 11.628  1.00 36.88 ? 80  LYS A C   1 
ATOM   584  O O   . LYS A 1 80  ? -19.738 11.948 12.021  1.00 34.47 ? 80  LYS A O   1 
ATOM   585  C CB  . LYS A 1 80  ? -17.277 14.098 12.949  1.00 32.78 ? 80  LYS A CB  1 
ATOM   586  C CG  . LYS A 1 80  ? -16.776 14.348 14.363  1.00 38.72 ? 80  LYS A CG  1 
ATOM   587  C CD  . LYS A 1 80  ? -16.772 15.796 14.781  1.00 43.71 ? 80  LYS A CD  1 
ATOM   588  C CE  . LYS A 1 80  ? -17.454 16.017 16.120  1.00 56.75 ? 80  LYS A CE  1 
ATOM   589  N NZ  . LYS A 1 80  ? -16.780 15.288 17.232  1.00 57.43 ? 80  LYS A NZ  1 
ATOM   590  N N   . ALA A 1 81  ? -18.100 12.232 10.374  1.00 36.28 ? 81  ALA A N   1 
ATOM   591  C CA  . ALA A 1 81  ? -18.892 11.914 9.150   1.00 38.80 ? 81  ALA A CA  1 
ATOM   592  C C   . ALA A 1 81  ? -19.393 10.462 9.130   1.00 40.61 ? 81  ALA A C   1 
ATOM   593  O O   . ALA A 1 81  ? -20.347 10.206 8.388   1.00 51.06 ? 81  ALA A O   1 
ATOM   594  C CB  . ALA A 1 81  ? -18.087 12.215 7.919   1.00 39.09 ? 81  ALA A CB  1 
ATOM   595  N N   . LEU A 1 82  ? -18.831 9.560  9.916   1.00 31.60 ? 82  LEU A N   1 
ATOM   596  C CA  . LEU A 1 82  ? -19.311 8.170  10.158  1.00 36.06 ? 82  LEU A CA  1 
ATOM   597  C C   . LEU A 1 82  ? -20.092 7.982  11.494  1.00 33.82 ? 82  LEU A C   1 
ATOM   598  O O   . LEU A 1 82  ? -20.353 6.831  11.853  1.00 34.80 ? 82  LEU A O   1 
ATOM   599  C CB  . LEU A 1 82  ? -18.071 7.273  10.108  1.00 35.27 ? 82  LEU A CB  1 
ATOM   600  C CG  . LEU A 1 82  ? -17.213 7.405  8.849   1.00 37.77 ? 82  LEU A CG  1 
ATOM   601  C CD1 . LEU A 1 82  ? -15.955 6.580  8.985   1.00 36.39 ? 82  LEU A CD1 1 
ATOM   602  C CD2 . LEU A 1 82  ? -17.997 6.979  7.607   1.00 43.17 ? 82  LEU A CD2 1 
ATOM   603  N N   . GLY A 1 83  ? -20.336 9.012  12.298  1.00 38.24 ? 83  GLY A N   1 
ATOM   604  C CA  . GLY A 1 83  ? -21.144 8.947  13.548  1.00 40.88 ? 83  GLY A CA  1 
ATOM   605  C C   . GLY A 1 83  ? -20.337 8.596  14.793  1.00 41.76 ? 83  GLY A C   1 
ATOM   606  O O   . GLY A 1 83  ? -20.938 8.170  15.835  1.00 31.32 ? 83  GLY A O   1 
ATOM   607  N N   . ILE A 1 84  ? -19.012 8.746  14.714  1.00 30.80 ? 84  ILE A N   1 
ATOM   608  C CA  . ILE A 1 84  ? -18.091 8.382  15.806  1.00 34.43 ? 84  ILE A CA  1 
ATOM   609  C C   . ILE A 1 84  ? -17.558 9.718  16.281  1.00 30.32 ? 84  ILE A C   1 
ATOM   610  O O   . ILE A 1 84  ? -17.247 10.598 15.431  1.00 30.45 ? 84  ILE A O   1 
ATOM   611  C CB  . ILE A 1 84  ? -17.028 7.356  15.366  1.00 31.08 ? 84  ILE A CB  1 
ATOM   612  C CG1 . ILE A 1 84  ? -17.705 5.987  15.167  1.00 32.87 ? 84  ILE A CG1 1 
ATOM   613  C CG2 . ILE A 1 84  ? -15.910 7.286  16.372  1.00 35.33 ? 84  ILE A CG2 1 
ATOM   614  C CD1 . ILE A 1 84  ? -16.871 4.903  14.478  1.00 36.08 ? 84  ILE A CD1 1 
ATOM   615  N N   . SER A 1 85  ? -17.710 9.933  17.573  1.00 28.71 ? 85  SER A N   1 
ATOM   616  C CA  . SER A 1 85  ? -17.043 11.064 18.246  1.00 27.01 ? 85  SER A CA  1 
ATOM   617  C C   . SER A 1 85  ? -15.700 10.515 18.670  1.00 22.46 ? 85  SER A C   1 
ATOM   618  O O   . SER A 1 85  ? -15.583 9.746  19.619  1.00 24.14 ? 85  SER A O   1 
ATOM   619  C CB  A SER A 1 85  ? -17.823 11.571 19.455  0.65 28.96 ? 85  SER A CB  1 
ATOM   620  C CB  B SER A 1 85  ? -17.873 11.567 19.412  0.35 28.11 ? 85  SER A CB  1 
ATOM   621  O OG  A SER A 1 85  ? -19.141 11.882 19.092  0.65 29.26 ? 85  SER A OG  1 
ATOM   622  O OG  B SER A 1 85  ? -17.230 12.662 20.038  0.35 28.70 ? 85  SER A OG  1 
ATOM   623  N N   . PRO A 1 86  ? -14.587 10.875 17.946  1.00 21.21 ? 86  PRO A N   1 
ATOM   624  C CA  . PRO A 1 86  ? -13.291 10.303 18.236  1.00 20.73 ? 86  PRO A CA  1 
ATOM   625  C C   . PRO A 1 86  ? -12.508 11.126 19.264  1.00 18.87 ? 86  PRO A C   1 
ATOM   626  O O   . PRO A 1 86  ? -12.947 12.239 19.645  1.00 22.00 ? 86  PRO A O   1 
ATOM   627  C CB  . PRO A 1 86  ? -12.601 10.439 16.854  1.00 19.44 ? 86  PRO A CB  1 
ATOM   628  C CG  . PRO A 1 86  ? -13.120 11.745 16.349  1.00 19.87 ? 86  PRO A CG  1 
ATOM   629  C CD  . PRO A 1 86  ? -14.566 11.838 16.850  1.00 21.44 ? 86  PRO A CD  1 
ATOM   630  N N   . PHE A 1 87  ? -11.398 10.595 19.668  1.00 17.18 ? 87  PHE A N   1 
ATOM   631  C CA  . PHE A 1 87  ? -10.527 11.159 20.721  1.00 17.21 ? 87  PHE A CA  1 
ATOM   632  C C   . PHE A 1 87  ? -9.727  12.323 20.120  1.00 18.09 ? 87  PHE A C   1 
ATOM   633  O O   . PHE A 1 87  ? -9.659  13.433 20.732  1.00 17.31 ? 87  PHE A O   1 
ATOM   634  C CB  . PHE A 1 87  ? -9.581  10.163 21.345  1.00 18.00 ? 87  PHE A CB  1 
ATOM   635  C CG  . PHE A 1 87  ? -8.792  10.723 22.498  1.00 17.92 ? 87  PHE A CG  1 
ATOM   636  C CD1 . PHE A 1 87  ? -9.459  10.996 23.684  1.00 22.67 ? 87  PHE A CD1 1 
ATOM   637  C CD2 . PHE A 1 87  ? -7.460  11.000 22.410  1.00 19.35 ? 87  PHE A CD2 1 
ATOM   638  C CE1 . PHE A 1 87  ? -8.778  11.541 24.754  1.00 22.23 ? 87  PHE A CE1 1 
ATOM   639  C CE2 . PHE A 1 87  ? -6.770  11.505 23.504  1.00 20.16 ? 87  PHE A CE2 1 
ATOM   640  C CZ  . PHE A 1 87  ? -7.445  11.777 24.656  1.00 21.03 ? 87  PHE A CZ  1 
ATOM   641  N N   . HIS A 1 88  ? -8.978  12.076 19.033  1.00 15.70 ? 88  HIS A N   1 
ATOM   642  C CA  . HIS A 1 88  ? -7.954  13.019 18.582  1.00 14.85 ? 88  HIS A CA  1 
ATOM   643  C C   . HIS A 1 88  ? -8.564  14.109 17.725  1.00 14.26 ? 88  HIS A C   1 
ATOM   644  O O   . HIS A 1 88  ? -9.545  13.885 17.002  1.00 16.08 ? 88  HIS A O   1 
ATOM   645  C CB  . HIS A 1 88  ? -6.843  12.282 17.829  1.00 14.33 ? 88  HIS A CB  1 
ATOM   646  C CG  . HIS A 1 88  ? -6.191  11.250 18.666  1.00 15.27 ? 88  HIS A CG  1 
ATOM   647  N ND1 . HIS A 1 88  ? -6.603  9.852  18.708  1.00 16.40 ? 88  HIS A ND1 1 
ATOM   648  C CD2 . HIS A 1 88  ? -5.167  11.336 19.512  1.00 16.79 ? 88  HIS A CD2 1 
ATOM   649  C CE1 . HIS A 1 88  ? -5.852  9.231  19.571  1.00 17.60 ? 88  HIS A CE1 1 
ATOM   650  N NE2 . HIS A 1 88  ? -4.946  10.110 20.084  1.00 18.40 ? 88  HIS A NE2 1 
ATOM   651  N N   . GLU A 1 89  ? -7.919  15.272 17.678  1.00 13.48 ? 89  GLU A N   1 
ATOM   652  C CA  . GLU A 1 89  ? -8.293  16.316 16.723  1.00 14.95 ? 89  GLU A CA  1 
ATOM   653  C C   . GLU A 1 89  ? -7.799  15.991 15.316  1.00 16.60 ? 89  GLU A C   1 
ATOM   654  O O   . GLU A 1 89  ? -8.501  16.242 14.340  1.00 19.76 ? 89  GLU A O   1 
ATOM   655  C CB  . GLU A 1 89  ? -7.700  17.653 17.144  1.00 18.28 ? 89  GLU A CB  1 
ATOM   656  C CG  . GLU A 1 89  ? -8.309  18.243 18.385  1.00 19.66 ? 89  GLU A CG  1 
ATOM   657  C CD  . GLU A 1 89  ? -9.792  18.530 18.242  1.00 23.65 ? 89  GLU A CD  1 
ATOM   658  O OE1 . GLU A 1 89  ? -10.128 19.260 17.325  1.00 27.56 ? 89  GLU A OE1 1 
ATOM   659  O OE2 . GLU A 1 89  ? -10.566 17.916 18.962  1.00 27.27 ? 89  GLU A OE2 1 
ATOM   660  N N   . HIS A 1 90  ? -6.610  15.458 15.250  1.00 14.89 ? 90  HIS A N   1 
ATOM   661  C CA  . HIS A 1 90  ? -5.924  15.118 14.004  1.00 16.69 ? 90  HIS A CA  1 
ATOM   662  C C   . HIS A 1 90  ? -4.801  14.178 14.343  1.00 17.49 ? 90  HIS A C   1 
ATOM   663  O O   . HIS A 1 90  ? -4.496  13.962 15.534  1.00 20.23 ? 90  HIS A O   1 
ATOM   664  C CB  . HIS A 1 90  ? -5.549  16.361 13.169  1.00 19.61 ? 90  HIS A CB  1 
ATOM   665  C CG  . HIS A 1 90  ? -5.089  17.548 13.895  1.00 24.02 ? 90  HIS A CG  1 
ATOM   666  N ND1 . HIS A 1 90  ? -3.885  17.538 14.527  1.00 35.73 ? 90  HIS A ND1 1 
ATOM   667  C CD2 . HIS A 1 90  ? -5.603  18.785 14.045  1.00 26.92 ? 90  HIS A CD2 1 
ATOM   668  C CE1 . HIS A 1 90  ? -3.661  18.734 15.046  1.00 31.77 ? 90  HIS A CE1 1 
ATOM   669  N NE2 . HIS A 1 90  ? -4.702  19.494 14.768  1.00 37.25 ? 90  HIS A NE2 1 
ATOM   670  N N   . ALA A 1 91  ? -4.180  13.624 13.352  1.00 16.63 ? 91  ALA A N   1 
ATOM   671  C CA  . ALA A 1 91  ? -2.921  12.888 13.519  1.00 15.71 ? 91  ALA A CA  1 
ATOM   672  C C   . ALA A 1 91  ? -1.868  13.753 12.857  1.00 19.56 ? 91  ALA A C   1 
ATOM   673  O O   . ALA A 1 91  ? -2.132  14.184 11.765  1.00 21.84 ? 91  ALA A O   1 
ATOM   674  C CB  . ALA A 1 91  ? -2.996  11.567 12.901  1.00 17.80 ? 91  ALA A CB  1 
ATOM   675  N N   . GLU A 1 92  ? -0.775  14.039 13.528  1.00 21.34 ? 92  GLU A N   1 
ATOM   676  C CA  . GLU A 1 92  ? 0.275   14.956 13.054  1.00 24.80 ? 92  GLU A CA  1 
ATOM   677  C C   . GLU A 1 92  ? 1.537   14.124 12.889  1.00 23.88 ? 92  GLU A C   1 
ATOM   678  O O   . GLU A 1 92  ? 1.865   13.264 13.760  1.00 28.01 ? 92  GLU A O   1 
ATOM   679  C CB  . GLU A 1 92  ? 0.491   16.073 14.083  1.00 31.34 ? 92  GLU A CB  1 
ATOM   680  C CG  . GLU A 1 92  ? -0.382  17.305 13.854  1.00 43.82 ? 92  GLU A CG  1 
ATOM   681  C CD  . GLU A 1 92  ? -0.220  18.339 14.972  1.00 49.70 ? 92  GLU A CD  1 
ATOM   682  O OE1 . GLU A 1 92  ? 0.438   18.013 15.984  1.00 64.36 ? 92  GLU A OE1 1 
ATOM   683  O OE2 . GLU A 1 92  ? -0.729  19.483 14.834  1.00 55.01 ? 92  GLU A OE2 1 
ATOM   684  N N   . VAL A 1 93  ? 2.169   14.236 11.725  1.00 16.62 ? 93  VAL A N   1 
ATOM   685  C CA  . VAL A 1 93  ? 3.401   13.501 11.405  1.00 15.80 ? 93  VAL A CA  1 
ATOM   686  C C   . VAL A 1 93  ? 4.450   14.562 11.085  1.00 14.61 ? 93  VAL A C   1 
ATOM   687  O O   . VAL A 1 93  ? 4.257   15.247 10.087  1.00 16.05 ? 93  VAL A O   1 
ATOM   688  C CB  . VAL A 1 93  ? 3.222   12.539 10.248  1.00 17.54 ? 93  VAL A CB  1 
ATOM   689  C CG1 . VAL A 1 93  ? 4.498   11.839 9.893   1.00 19.01 ? 93  VAL A CG1 1 
ATOM   690  C CG2 . VAL A 1 93  ? 2.116   11.526 10.584  1.00 19.53 ? 93  VAL A CG2 1 
ATOM   691  N N   . VAL A 1 94  ? 5.456   14.688 11.918  1.00 13.46 ? 94  VAL A N   1 
ATOM   692  C CA  . VAL A 1 94  ? 6.434   15.797 11.785  1.00 14.38 ? 94  VAL A CA  1 
ATOM   693  C C   . VAL A 1 94  ? 7.788   15.177 11.543  1.00 14.53 ? 94  VAL A C   1 
ATOM   694  O O   . VAL A 1 94  ? 8.236   14.338 12.368  1.00 13.53 ? 94  VAL A O   1 
ATOM   695  C CB  . VAL A 1 94  ? 6.446   16.713 12.999  1.00 16.23 ? 94  VAL A CB  1 
ATOM   696  C CG1 . VAL A 1 94  ? 7.454   17.838 12.740  1.00 16.92 ? 94  VAL A CG1 1 
ATOM   697  C CG2 . VAL A 1 94  ? 5.053   17.253 13.267  1.00 19.00 ? 94  VAL A CG2 1 
ATOM   698  N N   . PHE A 1 95  ? 8.497   15.583 10.495  1.00 13.49 ? 95  PHE A N   1 
ATOM   699  C CA  . PHE A 1 95  ? 9.761   14.951 10.094  1.00 13.86 ? 95  PHE A CA  1 
ATOM   700  C C   . PHE A 1 95  ? 10.645  15.907 9.304   1.00 14.54 ? 95  PHE A C   1 
ATOM   701  O O   . PHE A 1 95  ? 10.140  16.740 8.549   1.00 15.32 ? 95  PHE A O   1 
ATOM   702  C CB  . PHE A 1 95  ? 9.516   13.657 9.290   1.00 13.81 ? 95  PHE A CB  1 
ATOM   703  C CG  . PHE A 1 95  ? 8.779   13.859 7.985   1.00 15.88 ? 95  PHE A CG  1 
ATOM   704  C CD1 . PHE A 1 95  ? 7.418   14.044 7.957   1.00 16.62 ? 95  PHE A CD1 1 
ATOM   705  C CD2 . PHE A 1 95  ? 9.473   13.825 6.777   1.00 16.49 ? 95  PHE A CD2 1 
ATOM   706  C CE1 . PHE A 1 95  ? 6.749   14.196 6.746   1.00 18.77 ? 95  PHE A CE1 1 
ATOM   707  C CE2 . PHE A 1 95  ? 8.790   13.938 5.574   1.00 19.03 ? 95  PHE A CE2 1 
ATOM   708  C CZ  . PHE A 1 95  ? 7.451   14.182 5.586   1.00 18.31 ? 95  PHE A CZ  1 
ATOM   709  N N   . THR A 1 96  ? 11.931  15.670 9.392   1.00 15.43 ? 96  THR A N   1 
ATOM   710  C CA  . THR A 1 96  ? 12.889  16.296 8.447   1.00 14.34 ? 96  THR A CA  1 
ATOM   711  C C   . THR A 1 96  ? 12.928  15.504 7.176   1.00 16.35 ? 96  THR A C   1 
ATOM   712  O O   . THR A 1 96  ? 13.074  14.253 7.189   1.00 18.28 ? 96  THR A O   1 
ATOM   713  C CB  . THR A 1 96  ? 14.247  16.425 9.121   1.00 15.59 ? 96  THR A CB  1 
ATOM   714  O OG1 . THR A 1 96  ? 14.165  17.207 10.295  1.00 18.40 ? 96  THR A OG1 1 
ATOM   715  C CG2 . THR A 1 96  ? 15.269  16.984 8.149   1.00 19.51 ? 96  THR A CG2 1 
ATOM   716  N N   . ALA A 1 97  ? 12.803  16.203 6.043   1.00 16.03 ? 97  ALA A N   1 
ATOM   717  C CA  . ALA A 1 97  ? 12.837  15.571 4.712   1.00 15.59 ? 97  ALA A CA  1 
ATOM   718  C C   . ALA A 1 97  ? 14.062  16.010 3.928   1.00 16.46 ? 97  ALA A C   1 
ATOM   719  O O   . ALA A 1 97  ? 14.426  17.188 4.047   1.00 17.59 ? 97  ALA A O   1 
ATOM   720  C CB  . ALA A 1 97  ? 11.572  15.861 3.941   1.00 16.71 ? 97  ALA A CB  1 
ATOM   721  N N   . ASN A 1 98  ? 14.584  15.127 3.114   1.00 16.67 ? 98  ASN A N   1 
ATOM   722  C CA  . ASN A 1 98  ? 15.590  15.402 2.051   1.00 17.43 ? 98  ASN A CA  1 
ATOM   723  C C   . ASN A 1 98  ? 16.905  15.889 2.638   1.00 21.51 ? 98  ASN A C   1 
ATOM   724  O O   . ASN A 1 98  ? 17.648  16.551 1.845   1.00 24.73 ? 98  ASN A O   1 
ATOM   725  C CB  . ASN A 1 98  ? 15.003  16.360 1.030   1.00 19.20 ? 98  ASN A CB  1 
ATOM   726  C CG  . ASN A 1 98  ? 13.711  15.855 0.509   1.00 20.14 ? 98  ASN A CG  1 
ATOM   727  O OD1 . ASN A 1 98  ? 13.633  14.703 0.042   1.00 19.20 ? 98  ASN A OD1 1 
ATOM   728  N ND2 . ASN A 1 98  ? 12.684  16.680 0.638   1.00 19.71 ? 98  ASN A ND2 1 
ATOM   729  N N   . ASP A 1 99  ? 17.248  15.597 3.871   1.00 20.91 ? 99  ASP A N   1 
ATOM   730  C CA  . ASP A 1 99  ? 18.464  16.245 4.417   1.00 29.41 ? 99  ASP A CA  1 
ATOM   731  C C   . ASP A 1 99  ? 19.720  15.453 4.016   1.00 31.96 ? 99  ASP A C   1 
ATOM   732  O O   . ASP A 1 99  ? 20.830  15.985 4.256   1.00 30.96 ? 99  ASP A O   1 
ATOM   733  C CB  . ASP A 1 99  ? 18.306  16.679 5.870   1.00 34.05 ? 99  ASP A CB  1 
ATOM   734  C CG  . ASP A 1 99  ? 18.395  15.517 6.805   1.00 37.08 ? 99  ASP A CG  1 
ATOM   735  O OD1 . ASP A 1 99  ? 18.199  14.450 6.329   1.00 55.60 ? 99  ASP A OD1 1 
ATOM   736  O OD2 . ASP A 1 99  ? 18.723  15.709 7.979   1.00 53.59 ? 99  ASP A OD2 1 
ATOM   737  N N   . SER A 1 100 ? 19.584  14.288 3.384   1.00 30.82 ? 100 SER A N   1 
ATOM   738  C CA  . SER A 1 100 ? 20.679  13.534 2.706   1.00 34.80 ? 100 SER A CA  1 
ATOM   739  C C   . SER A 1 100 ? 20.384  13.444 1.211   1.00 32.88 ? 100 SER A C   1 
ATOM   740  O O   . SER A 1 100 ? 20.741  12.442 0.601   1.00 40.27 ? 100 SER A O   1 
ATOM   741  C CB  . SER A 1 100 ? 20.813  12.154 3.261   1.00 38.99 ? 100 SER A CB  1 
ATOM   742  O OG  . SER A 1 100 ? 21.016  12.193 4.653   1.00 42.73 ? 100 SER A OG  1 
ATOM   743  N N   . GLY A 1 101 ? 19.681  14.418 0.653   1.00 28.45 ? 101 GLY A N   1 
ATOM   744  C CA  . GLY A 1 101 ? 19.300  14.397 -0.749  1.00 26.09 ? 101 GLY A CA  1 
ATOM   745  C C   . GLY A 1 101 ? 17.864  13.946 -0.915  1.00 26.38 ? 101 GLY A C   1 
ATOM   746  O O   . GLY A 1 101 ? 17.247  13.489 0.071   1.00 26.71 ? 101 GLY A O   1 
ATOM   747  N N   . PRO A 1 102 ? 17.334  14.078 -2.137  1.00 24.26 ? 102 PRO A N   1 
ATOM   748  C CA  . PRO A 1 102 ? 15.956  13.782 -2.456  1.00 22.23 ? 102 PRO A CA  1 
ATOM   749  C C   . PRO A 1 102 ? 15.651  12.334 -2.061  1.00 24.65 ? 102 PRO A C   1 
ATOM   750  O O   . PRO A 1 102 ? 16.428  11.403 -2.341  1.00 24.19 ? 102 PRO A O   1 
ATOM   751  C CB  . PRO A 1 102 ? 15.794  13.985 -3.960  1.00 27.59 ? 102 PRO A CB  1 
ATOM   752  C CG  . PRO A 1 102 ? 17.224  14.079 -4.481  1.00 30.86 ? 102 PRO A CG  1 
ATOM   753  C CD  . PRO A 1 102 ? 18.083  14.526 -3.338  1.00 26.99 ? 102 PRO A CD  1 
ATOM   754  N N   . ARG A 1 103 ? 14.506  12.165 -1.385  1.00 20.53 ? 103 ARG A N   1 
ATOM   755  C CA  . ARG A 1 103 ? 13.930  10.846 -1.128  1.00 20.69 ? 103 ARG A CA  1 
ATOM   756  C C   . ARG A 1 103 ? 12.448  10.905 -1.491  1.00 18.66 ? 103 ARG A C   1 
ATOM   757  O O   . ARG A 1 103 ? 11.888  12.000 -1.627  1.00 20.23 ? 103 ARG A O   1 
ATOM   758  C CB  . ARG A 1 103 ? 14.117  10.465 0.337   1.00 18.69 ? 103 ARG A CB  1 
ATOM   759  C CG  . ARG A 1 103 ? 15.528  10.232 0.855   1.00 22.72 ? 103 ARG A CG  1 
ATOM   760  C CD  . ARG A 1 103 ? 16.139  9.088  0.100   1.00 24.49 ? 103 ARG A CD  1 
ATOM   761  N NE  . ARG A 1 103 ? 17.478  8.914  0.684   1.00 29.47 ? 103 ARG A NE  1 
ATOM   762  C CZ  . ARG A 1 103 ? 18.593  9.564  0.305   1.00 31.38 ? 103 ARG A CZ  1 
ATOM   763  N NH1 . ARG A 1 103 ? 18.587  10.409 -0.708  1.00 34.48 ? 103 ARG A NH1 1 
ATOM   764  N NH2 . ARG A 1 103 ? 19.740  9.324  0.925   1.00 37.00 ? 103 ARG A NH2 1 
ATOM   765  N N   . ARG A 1 104 ? 11.851  9.734  -1.637  1.00 19.44 ? 104 ARG A N   1 
ATOM   766  C CA  . ARG A 1 104 ? 10.398  9.574  -1.813  1.00 19.68 ? 104 ARG A CA  1 
ATOM   767  C C   . ARG A 1 104 ? 9.821   9.081  -0.481  1.00 18.11 ? 104 ARG A C   1 
ATOM   768  O O   . ARG A 1 104 ? 10.341  8.136  0.058   1.00 17.03 ? 104 ARG A O   1 
ATOM   769  C CB  . ARG A 1 104 ? 10.094  8.562  -2.887  1.00 24.66 ? 104 ARG A CB  1 
ATOM   770  C CG  . ARG A 1 104 ? 10.771  8.918  -4.209  1.00 36.64 ? 104 ARG A CG  1 
ATOM   771  C CD  . ARG A 1 104 ? 9.944   8.506  -5.414  1.00 47.90 ? 104 ARG A CD  1 
ATOM   772  N NE  . ARG A 1 104 ? 10.696  8.817  -6.624  1.00 60.47 ? 104 ARG A NE  1 
ATOM   773  C CZ  . ARG A 1 104 ? 10.927  10.043 -7.106  1.00 66.86 ? 104 ARG A CZ  1 
ATOM   774  N NH1 . ARG A 1 104 ? 10.452  11.125 -6.504  1.00 64.94 ? 104 ARG A NH1 1 
ATOM   775  N NH2 . ARG A 1 104 ? 11.641  10.174 -8.213  1.00 71.92 ? 104 ARG A NH2 1 
ATOM   776  N N   . TYR A 1 105 ? 8.807   9.764  -0.012  1.00 14.96 ? 105 TYR A N   1 
ATOM   777  C CA  . TYR A 1 105 ? 8.228   9.492  1.310   1.00 15.02 ? 105 TYR A CA  1 
ATOM   778  C C   . TYR A 1 105 ? 6.793   9.073  1.144   1.00 15.78 ? 105 TYR A C   1 
ATOM   779  O O   . TYR A 1 105 ? 5.957   9.782  0.533   1.00 17.10 ? 105 TYR A O   1 
ATOM   780  C CB  . TYR A 1 105 ? 8.237   10.724 2.185   1.00 14.81 ? 105 TYR A CB  1 
ATOM   781  C CG  . TYR A 1 105 ? 9.607   11.219 2.509   1.00 14.62 ? 105 TYR A CG  1 
ATOM   782  C CD1 . TYR A 1 105 ? 10.261  12.006 1.602   1.00 17.23 ? 105 TYR A CD1 1 
ATOM   783  C CD2 . TYR A 1 105 ? 10.301  10.860 3.662   1.00 15.74 ? 105 TYR A CD2 1 
ATOM   784  C CE1 . TYR A 1 105 ? 11.559  12.439 1.831   1.00 15.45 ? 105 TYR A CE1 1 
ATOM   785  C CE2 . TYR A 1 105 ? 11.587  11.294 3.908   1.00 16.22 ? 105 TYR A CE2 1 
ATOM   786  C CZ  . TYR A 1 105 ? 12.225  12.125 2.997   1.00 16.57 ? 105 TYR A CZ  1 
ATOM   787  O OH  . TYR A 1 105 ? 13.515  12.467 3.307   1.00 17.28 ? 105 TYR A OH  1 
ATOM   788  N N   . THR A 1 106 ? 6.450   7.915  1.744   1.00 15.64 ? 106 THR A N   1 
ATOM   789  C CA  . THR A 1 106 ? 5.040   7.547  1.952   1.00 16.15 ? 106 THR A CA  1 
ATOM   790  C C   . THR A 1 106 ? 4.750   7.602  3.433   1.00 14.63 ? 106 THR A C   1 
ATOM   791  O O   . THR A 1 106 ? 5.471   6.977  4.238   1.00 16.01 ? 106 THR A O   1 
ATOM   792  C CB  . THR A 1 106 ? 4.699   6.178  1.379   1.00 19.26 ? 106 THR A CB  1 
ATOM   793  O OG1 . THR A 1 106 ? 4.996   6.202  -0.021  1.00 22.53 ? 106 THR A OG1 1 
ATOM   794  C CG2 . THR A 1 106 ? 3.243   5.867  1.635   1.00 21.71 ? 106 THR A CG2 1 
ATOM   795  N N   . ILE A 1 107 ? 3.800   8.403  3.808   1.00 12.70 ? 107 ILE A N   1 
ATOM   796  C CA  . ILE A 1 107 ? 3.292   8.527  5.178   1.00 13.14 ? 107 ILE A CA  1 
ATOM   797  C C   . ILE A 1 107 ? 2.013   7.721  5.226   1.00 13.88 ? 107 ILE A C   1 
ATOM   798  O O   . ILE A 1 107 ? 1.079   8.021  4.491   1.00 15.14 ? 107 ILE A O   1 
ATOM   799  C CB  . ILE A 1 107 ? 3.048   9.972  5.587   1.00 14.55 ? 107 ILE A CB  1 
ATOM   800  C CG1 . ILE A 1 107 ? 4.309   10.853 5.370   1.00 17.34 ? 107 ILE A CG1 1 
ATOM   801  C CG2 . ILE A 1 107 ? 2.457   10.016 6.981   1.00 16.72 ? 107 ILE A CG2 1 
ATOM   802  C CD1 . ILE A 1 107 ? 5.462   10.451 6.179   1.00 20.06 ? 107 ILE A CD1 1 
ATOM   803  N N   . ALA A 1 108 ? 2.000   6.653  6.023   1.00 14.63 ? 108 ALA A N   1 
ATOM   804  C CA  . ALA A 1 108 ? 0.839   5.794  6.153   1.00 15.00 ? 108 ALA A CA  1 
ATOM   805  C C   . ALA A 1 108 ? 0.271   5.947  7.546   1.00 14.68 ? 108 ALA A C   1 
ATOM   806  O O   . ALA A 1 108 ? 1.036   6.106  8.530   1.00 15.74 ? 108 ALA A O   1 
ATOM   807  C CB  . ALA A 1 108 ? 1.192   4.405  5.888   1.00 14.63 ? 108 ALA A CB  1 
ATOM   808  N N   . ALA A 1 109 ? -1.044  5.899  7.640   1.00 13.43 ? 109 ALA A N   1 
ATOM   809  C CA  . ALA A 1 109 ? -1.737  5.999  8.916   1.00 13.14 ? 109 ALA A CA  1 
ATOM   810  C C   . ALA A 1 109 ? -2.861  4.984  8.967   1.00 14.13 ? 109 ALA A C   1 
ATOM   811  O O   . ALA A 1 109 ? -3.553  4.777  7.957   1.00 15.35 ? 109 ALA A O   1 
ATOM   812  C CB  . ALA A 1 109 ? -2.272  7.394  9.109   1.00 15.04 ? 109 ALA A CB  1 
ATOM   813  N N   . LEU A 1 110 ? -3.065  4.394  10.121  1.00 12.75 ? 110 LEU A N   1 
ATOM   814  C CA  . LEU A 1 110 ? -4.146  3.405  10.372  1.00 12.98 ? 110 LEU A CA  1 
ATOM   815  C C   . LEU A 1 110 ? -4.975  3.912  11.530  1.00 12.08 ? 110 LEU A C   1 
ATOM   816  O O   . LEU A 1 110 ? -4.404  4.136  12.632  1.00 13.82 ? 110 LEU A O   1 
ATOM   817  C CB  . LEU A 1 110 ? -3.515  2.067  10.679  1.00 14.32 ? 110 LEU A CB  1 
ATOM   818  C CG  . LEU A 1 110 ? -4.475  0.951  11.122  1.00 13.90 ? 110 LEU A CG  1 
ATOM   819  C CD1 . LEU A 1 110 ? -5.454  0.591  10.017  1.00 14.44 ? 110 LEU A CD1 1 
ATOM   820  C CD2 . LEU A 1 110 ? -3.638  -0.242 11.539  1.00 14.83 ? 110 LEU A CD2 1 
ATOM   821  N N   . LEU A 1 111 ? -6.223  4.205  11.281  1.00 12.65 ? 111 LEU A N   1 
ATOM   822  C CA  . LEU A 1 111 ? -7.078  4.979  12.179  1.00 12.76 ? 111 LEU A CA  1 
ATOM   823  C C   . LEU A 1 111 ? -8.075  4.130  12.963  1.00 14.20 ? 111 LEU A C   1 
ATOM   824  O O   . LEU A 1 111 ? -8.815  3.347  12.318  1.00 14.59 ? 111 LEU A O   1 
ATOM   825  C CB  . LEU A 1 111 ? -7.836  6.026  11.404  1.00 13.56 ? 111 LEU A CB  1 
ATOM   826  C CG  . LEU A 1 111 ? -7.028  6.969  10.506  1.00 14.53 ? 111 LEU A CG  1 
ATOM   827  C CD1 . LEU A 1 111 ? -7.981  8.008  9.946   1.00 14.03 ? 111 LEU A CD1 1 
ATOM   828  C CD2 . LEU A 1 111 ? -5.885  7.600  11.288  1.00 14.18 ? 111 LEU A CD2 1 
ATOM   829  N N   . SER A 1 112 ? -8.227  4.427  14.230  1.00 13.67 ? 112 SER A N   1 
ATOM   830  C CA  . SER A 1 112 ? -9.353  3.967  15.086  1.00 14.43 ? 112 SER A CA  1 
ATOM   831  C C   . SER A 1 112 ? -9.894  5.160  15.819  1.00 14.84 ? 112 SER A C   1 
ATOM   832  O O   . SER A 1 112 ? -9.242  6.208  15.894  1.00 14.92 ? 112 SER A O   1 
ATOM   833  C CB  . SER A 1 112 ? -8.877  2.945  16.066  1.00 14.45 ? 112 SER A CB  1 
ATOM   834  O OG  . SER A 1 112 ? -8.308  1.825  15.388  1.00 17.35 ? 112 SER A OG  1 
ATOM   835  N N   . PRO A 1 113 ? -11.089 5.087  16.386  1.00 15.63 ? 113 PRO A N   1 
ATOM   836  C CA  . PRO A 1 113 ? -11.639 6.243  17.080  1.00 15.11 ? 113 PRO A CA  1 
ATOM   837  C C   . PRO A 1 113 ? -10.742 6.770  18.197  1.00 14.50 ? 113 PRO A C   1 
ATOM   838  O O   . PRO A 1 113 ? -10.721 8.053  18.319  1.00 16.11 ? 113 PRO A O   1 
ATOM   839  C CB  . PRO A 1 113 ? -12.976 5.727  17.600  1.00 16.74 ? 113 PRO A CB  1 
ATOM   840  C CG  . PRO A 1 113 ? -13.349 4.725  16.503  1.00 17.44 ? 113 PRO A CG  1 
ATOM   841  C CD  . PRO A 1 113 ? -12.078 4.002  16.173  1.00 16.47 ? 113 PRO A CD  1 
ATOM   842  N N   . TYR A 1 114 ? -10.100 5.933  19.000  1.00 14.88 ? 114 TYR A N   1 
ATOM   843  C CA  . TYR A 1 114 ? -9.286  6.424  20.125  1.00 14.93 ? 114 TYR A CA  1 
ATOM   844  C C   . TYR A 1 114 ? -7.822  6.126  19.954  1.00 14.50 ? 114 TYR A C   1 
ATOM   845  O O   . TYR A 1 114 ? -7.028  6.311  20.867  1.00 16.88 ? 114 TYR A O   1 
ATOM   846  C CB  . TYR A 1 114 ? -9.774  5.867  21.478  1.00 16.92 ? 114 TYR A CB  1 
ATOM   847  C CG  . TYR A 1 114 ? -10.979 6.592  22.004  1.00 19.11 ? 114 TYR A CG  1 
ATOM   848  C CD1 . TYR A 1 114 ? -12.222 6.482  21.410  1.00 23.07 ? 114 TYR A CD1 1 
ATOM   849  C CD2 . TYR A 1 114 ? -10.857 7.398  23.124  1.00 17.81 ? 114 TYR A CD2 1 
ATOM   850  C CE1 . TYR A 1 114 ? -13.342 7.135  21.903  1.00 27.58 ? 114 TYR A CE1 1 
ATOM   851  C CE2 . TYR A 1 114 ? -11.967 8.094  23.591  1.00 19.54 ? 114 TYR A CE2 1 
ATOM   852  C CZ  . TYR A 1 114 ? -13.195 7.958  23.002  1.00 26.53 ? 114 TYR A CZ  1 
ATOM   853  O OH  . TYR A 1 114 ? -14.293 8.582  23.537  1.00 32.38 ? 114 TYR A OH  1 
ATOM   854  N N   . SER A 1 115 ? -7.374  5.804  18.708  1.00 14.61 ? 115 SER A N   1 
ATOM   855  C CA  . SER A 1 115 ? -5.995  5.382  18.489  1.00 14.75 ? 115 SER A CA  1 
ATOM   856  C C   . SER A 1 115 ? -5.624  5.582  17.049  1.00 15.03 ? 115 SER A C   1 
ATOM   857  O O   . SER A 1 115 ? -6.486  5.515  16.172  1.00 16.34 ? 115 SER A O   1 
ATOM   858  C CB  . SER A 1 115 ? -5.803  3.940  18.854  1.00 16.93 ? 115 SER A CB  1 
ATOM   859  O OG  . SER A 1 115 ? -4.493  3.520  18.717  1.00 25.61 ? 115 SER A OG  1 
ATOM   860  N N   . TYR A 1 116 ? -4.369  5.807  16.818  1.00 14.23 ? 116 TYR A N   1 
ATOM   861  C CA  . TYR A 1 116 ? -3.862  5.637  15.453  1.00 15.68 ? 116 TYR A CA  1 
ATOM   862  C C   . TYR A 1 116 ? -2.433  5.158  15.519  1.00 15.65 ? 116 TYR A C   1 
ATOM   863  O O   . TYR A 1 116 ? -1.662  5.309  16.496  1.00 14.77 ? 116 TYR A O   1 
ATOM   864  C CB  . TYR A 1 116 ? -3.960  6.903  14.618  1.00 15.41 ? 116 TYR A CB  1 
ATOM   865  C CG  . TYR A 1 116 ? -3.240  8.090  15.138  1.00 15.32 ? 116 TYR A CG  1 
ATOM   866  C CD1 . TYR A 1 116 ? -1.946  8.339  14.812  1.00 16.10 ? 116 TYR A CD1 1 
ATOM   867  C CD2 . TYR A 1 116 ? -3.910  8.937  16.003  1.00 17.68 ? 116 TYR A CD2 1 
ATOM   868  C CE1 . TYR A 1 116 ? -1.297  9.472  15.316  1.00 17.23 ? 116 TYR A CE1 1 
ATOM   869  C CE2 . TYR A 1 116 ? -3.276  10.025 16.532  1.00 18.25 ? 116 TYR A CE2 1 
ATOM   870  C CZ  . TYR A 1 116 ? -2.010  10.303 16.164  1.00 17.08 ? 116 TYR A CZ  1 
ATOM   871  O OH  . TYR A 1 116 ? -1.405  11.394 16.711  1.00 23.43 ? 116 TYR A OH  1 
ATOM   872  N N   . SER A 1 117 ? -2.027  4.571  14.394  1.00 14.75 ? 117 SER A N   1 
ATOM   873  C CA  A SER A 1 117 ? -0.630  4.193  14.107  0.50 15.96 ? 117 SER A CA  1 
ATOM   874  C CA  B SER A 1 117 ? -0.643  4.157  14.085  0.50 15.46 ? 117 SER A CA  1 
ATOM   875  C C   . SER A 1 117 ? -0.197  4.888  12.822  1.00 14.93 ? 117 SER A C   1 
ATOM   876  O O   . SER A 1 117 ? -1.018  5.099  11.940  1.00 14.81 ? 117 SER A O   1 
ATOM   877  C CB  A SER A 1 117 ? -0.387  2.719  14.064  0.50 18.43 ? 117 SER A CB  1 
ATOM   878  C CB  B SER A 1 117 ? -0.506  2.671  13.934  0.50 17.01 ? 117 SER A CB  1 
ATOM   879  O OG  A SER A 1 117 ? -1.079  2.100  13.033  0.50 23.03 ? 117 SER A OG  1 
ATOM   880  O OG  B SER A 1 117 ? -0.815  2.041  15.178  0.50 19.73 ? 117 SER A OG  1 
ATOM   881  N N   . THR A 1 118 ? 1.051   5.288  12.791  1.00 13.73 ? 118 THR A N   1 
ATOM   882  C CA  . THR A 1 118 ? 1.655   5.891  11.597  1.00 13.47 ? 118 THR A CA  1 
ATOM   883  C C   . THR A 1 118 ? 3.028   5.339  11.381  1.00 13.86 ? 118 THR A C   1 
ATOM   884  O O   . THR A 1 118 ? 3.785   5.099  12.351  1.00 15.76 ? 118 THR A O   1 
ATOM   885  C CB  . THR A 1 118 ? 1.577   7.410  11.698  1.00 14.74 ? 118 THR A CB  1 
ATOM   886  O OG1 . THR A 1 118 ? 1.959   7.945  10.448  1.00 16.17 ? 118 THR A OG1 1 
ATOM   887  C CG2 . THR A 1 118 ? 2.477   7.994  12.769  1.00 15.41 ? 118 THR A CG2 1 
ATOM   888  N N   . THR A 1 119 ? 3.398   5.203  10.117  1.00 12.87 ? 119 THR A N   1 
ATOM   889  C CA  . THR A 1 119 ? 4.732   4.791  9.709   1.00 12.72 ? 119 THR A CA  1 
ATOM   890  C C   . THR A 1 119 ? 5.140   5.570  8.482   1.00 14.01 ? 119 THR A C   1 
ATOM   891  O O   . THR A 1 119 ? 4.319   6.227  7.860   1.00 15.63 ? 119 THR A O   1 
ATOM   892  C CB  . THR A 1 119 ? 4.837   3.273  9.517   1.00 14.89 ? 119 THR A CB  1 
ATOM   893  O OG1 . THR A 1 119 ? 6.228   2.926  9.524   1.00 15.30 ? 119 THR A OG1 1 
ATOM   894  C CG2 . THR A 1 119 ? 4.216   2.825  8.230   1.00 15.15 ? 119 THR A CG2 1 
ATOM   895  N N   . ALA A 1 120 ? 6.408   5.509  8.205   1.00 14.98 ? 120 ALA A N   1 
ATOM   896  C CA  . ALA A 1 120 ? 6.917   6.106  6.957   1.00 13.85 ? 120 ALA A CA  1 
ATOM   897  C C   . ALA A 1 120 ? 7.659   5.060  6.183   1.00 13.09 ? 120 ALA A C   1 
ATOM   898  O O   . ALA A 1 120 ? 8.402   4.278  6.814   1.00 16.17 ? 120 ALA A O   1 
ATOM   899  C CB  . ALA A 1 120 ? 7.863   7.248  7.277   1.00 15.82 ? 120 ALA A CB  1 
ATOM   900  N N   . VAL A 1 121 ? 7.529   5.089  4.871   1.00 14.67 ? 121 VAL A N   1 
ATOM   901  C CA  . VAL A 1 121 ? 8.350   4.295  3.930   1.00 16.05 ? 121 VAL A CA  1 
ATOM   902  C C   . VAL A 1 121 ? 9.154   5.320  3.142   1.00 17.00 ? 121 VAL A C   1 
ATOM   903  O O   . VAL A 1 121 ? 8.499   6.134  2.446   1.00 18.39 ? 121 VAL A O   1 
ATOM   904  C CB  . VAL A 1 121 ? 7.510   3.402  3.031   1.00 20.84 ? 121 VAL A CB  1 
ATOM   905  C CG1 . VAL A 1 121 ? 8.401   2.589  2.102   1.00 24.11 ? 121 VAL A CG1 1 
ATOM   906  C CG2 . VAL A 1 121 ? 6.665   2.484  3.895   1.00 26.20 ? 121 VAL A CG2 1 
ATOM   907  N N   . VAL A 1 122 ? 10.453  5.243  3.255   1.00 17.05 ? 122 VAL A N   1 
ATOM   908  C CA  . VAL A 1 122 ? 11.398  6.224  2.673   1.00 16.58 ? 122 VAL A CA  1 
ATOM   909  C C   . VAL A 1 122 ? 12.220  5.466  1.652   1.00 18.99 ? 122 VAL A C   1 
ATOM   910  O O   . VAL A 1 122 ? 12.907  4.489  2.060   1.00 20.62 ? 122 VAL A O   1 
ATOM   911  C CB  . VAL A 1 122 ? 12.232  6.905  3.734   1.00 18.54 ? 122 VAL A CB  1 
ATOM   912  C CG1 . VAL A 1 122 ? 13.124  7.941  3.063   1.00 20.88 ? 122 VAL A CG1 1 
ATOM   913  C CG2 . VAL A 1 122 ? 11.284  7.542  4.725   1.00 18.66 ? 122 VAL A CG2 1 
ATOM   914  N N   . THR A 1 123 ? 12.138  5.877  0.397   1.00 20.52 ? 123 THR A N   1 
ATOM   915  C CA  . THR A 1 123 ? 12.897  5.208  -0.697  1.00 22.15 ? 123 THR A CA  1 
ATOM   916  C C   . THR A 1 123 ? 13.800  6.202  -1.419  1.00 24.60 ? 123 THR A C   1 
ATOM   917  O O   . THR A 1 123 ? 13.551  7.405  -1.392  1.00 22.83 ? 123 THR A O   1 
ATOM   918  C CB  . THR A 1 123 ? 11.952  4.496  -1.663  1.00 30.28 ? 123 THR A CB  1 
ATOM   919  O OG1 . THR A 1 123 ? 11.133  5.455  -2.297  1.00 34.58 ? 123 THR A OG1 1 
ATOM   920  C CG2 . THR A 1 123 ? 11.005  3.549  -0.975  1.00 32.01 ? 123 THR A CG2 1 
ATOM   921  N N   . ASN A 1 124 ? 14.907  5.679  -1.954  1.00 30.97 ? 124 ASN A N   1 
ATOM   922  C CA  . ASN A 1 124 ? 15.893  6.494  -2.711  1.00 35.80 ? 124 ASN A CA  1 
ATOM   923  C C   . ASN A 1 124 ? 15.562  6.349  -4.202  1.00 40.34 ? 124 ASN A C   1 
ATOM   924  O O   . ASN A 1 124 ? 15.865  5.288  -4.722  1.00 45.46 ? 124 ASN A O   1 
ATOM   925  C CB  . ASN A 1 124 ? 17.336  6.132  -2.347  1.00 35.38 ? 124 ASN A CB  1 
ATOM   926  C CG  . ASN A 1 124 ? 18.300  7.187  -2.851  1.00 40.42 ? 124 ASN A CG  1 
ATOM   927  O OD1 . ASN A 1 124 ? 17.993  7.888  -3.814  1.00 46.44 ? 124 ASN A OD1 1 
ATOM   928  N ND2 . ASN A 1 124 ? 19.445  7.319  -2.207  1.00 43.57 ? 124 ASN A ND2 1 
ATOM   929  N N   . CYS B 1 10  ? -4.921  12.232 39.642  1.00 47.46 ? 10  CYS B N   1 
ATOM   930  C CA  . CYS B 1 10  ? -4.101  12.427 38.395  1.00 45.95 ? 10  CYS B CA  1 
ATOM   931  C C   . CYS B 1 10  ? -5.027  12.366 37.187  1.00 34.93 ? 10  CYS B C   1 
ATOM   932  O O   . CYS B 1 10  ? -5.413  11.305 36.722  1.00 40.57 ? 10  CYS B O   1 
ATOM   933  C CB  . CYS B 1 10  ? -3.026  11.368 38.230  1.00 50.32 ? 10  CYS B CB  1 
ATOM   934  S SG  . CYS B 1 10  ? -1.519  12.050 37.496  1.00 58.13 ? 10  CYS B SG  1 
ATOM   935  N N   . PRO B 1 11  ? -5.464  13.508 36.646  1.00 27.66 ? 11  PRO B N   1 
ATOM   936  C CA  . PRO B 1 11  ? -6.342  13.500 35.492  1.00 26.44 ? 11  PRO B CA  1 
ATOM   937  C C   . PRO B 1 11  ? -5.650  13.154 34.161  1.00 22.56 ? 11  PRO B C   1 
ATOM   938  O O   . PRO B 1 11  ? -6.382  12.902 33.219  1.00 22.47 ? 11  PRO B O   1 
ATOM   939  C CB  . PRO B 1 11  ? -6.943  14.899 35.444  1.00 28.80 ? 11  PRO B CB  1 
ATOM   940  C CG  . PRO B 1 11  ? -6.015  15.752 36.234  1.00 30.09 ? 11  PRO B CG  1 
ATOM   941  C CD  . PRO B 1 11  ? -5.262  14.861 37.180  1.00 29.96 ? 11  PRO B CD  1 
ATOM   942  N N   . LEU B 1 12  ? -4.336  13.310 34.089  1.00 22.50 ? 12  LEU B N   1 
ATOM   943  C CA  . LEU B 1 12  ? -3.578  13.187 32.819  1.00 21.76 ? 12  LEU B CA  1 
ATOM   944  C C   . LEU B 1 12  ? -2.260  12.456 33.072  1.00 23.99 ? 12  LEU B C   1 
ATOM   945  O O   . LEU B 1 12  ? -1.408  12.952 33.838  1.00 27.83 ? 12  LEU B O   1 
ATOM   946  C CB  . LEU B 1 12  ? -3.315  14.560 32.204  1.00 23.47 ? 12  LEU B CB  1 
ATOM   947  C CG  . LEU B 1 12  ? -2.538  14.523 30.892  1.00 25.49 ? 12  LEU B CG  1 
ATOM   948  C CD1 . LEU B 1 12  ? -3.321  13.835 29.789  1.00 24.54 ? 12  LEU B CD1 1 
ATOM   949  C CD2 . LEU B 1 12  ? -2.187  15.945 30.478  1.00 27.28 ? 12  LEU B CD2 1 
ATOM   950  N N   . MET B 1 13  ? -2.120  11.246 32.516  1.00 20.51 ? 13  MET B N   1 
ATOM   951  C CA  . MET B 1 13  ? -0.898  10.447 32.615  1.00 21.84 ? 13  MET B CA  1 
ATOM   952  C C   . MET B 1 13  ? -0.421  10.104 31.205  1.00 20.01 ? 13  MET B C   1 
ATOM   953  O O   . MET B 1 13  ? -1.258  10.050 30.312  1.00 19.57 ? 13  MET B O   1 
ATOM   954  C CB  . MET B 1 13  ? -1.182  9.125  33.345  1.00 26.14 ? 13  MET B CB  1 
ATOM   955  C CG  . MET B 1 13  ? -1.620  9.384  34.773  1.00 39.86 ? 13  MET B CG  1 
ATOM   956  S SD  . MET B 1 13  ? -2.258  7.880  35.576  1.00 53.63 ? 13  MET B SD  1 
ATOM   957  C CE  . MET B 1 13  ? -3.966  7.913  35.027  1.00 52.15 ? 13  MET B CE  1 
ATOM   958  N N   . VAL B 1 14  ? 0.871   10.036 31.057  1.00 18.39 ? 14  VAL B N   1 
ATOM   959  C CA  . VAL B 1 14  ? 1.492   9.664  29.770  1.00 17.62 ? 14  VAL B CA  1 
ATOM   960  C C   . VAL B 1 14  ? 2.303   8.407  29.983  1.00 19.25 ? 14  VAL B C   1 
ATOM   961  O O   . VAL B 1 14  ? 3.050   8.287  30.998  1.00 21.75 ? 14  VAL B O   1 
ATOM   962  C CB  . VAL B 1 14  ? 2.321   10.829 29.190  1.00 18.16 ? 14  VAL B CB  1 
ATOM   963  C CG1 . VAL B 1 14  ? 3.025   10.397 27.930  1.00 19.18 ? 14  VAL B CG1 1 
ATOM   964  C CG2 . VAL B 1 14  ? 1.421   12.045 28.983  1.00 20.17 ? 14  VAL B CG2 1 
ATOM   965  N N   . LYS B 1 15  ? 2.098   7.426  29.111  1.00 17.33 ? 15  LYS B N   1 
ATOM   966  C CA  A LYS B 1 15  ? 2.894   6.156  29.132  0.50 17.67 ? 15  LYS B CA  1 
ATOM   967  C CA  B LYS B 1 15  ? 2.930   6.138  29.169  0.50 19.03 ? 15  LYS B CA  1 
ATOM   968  C C   . LYS B 1 15  ? 3.596   5.907  27.747  1.00 16.76 ? 15  LYS B C   1 
ATOM   969  O O   . LYS B 1 15  ? 3.063   6.058  26.573  1.00 17.57 ? 15  LYS B O   1 
ATOM   970  C CB  A LYS B 1 15  ? 2.007   4.974  29.544  0.50 18.27 ? 15  LYS B CB  1 
ATOM   971  C CB  B LYS B 1 15  ? 1.979   4.983  29.506  0.50 21.81 ? 15  LYS B CB  1 
ATOM   972  C CG  A LYS B 1 15  ? 0.796   5.340  30.393  0.50 26.54 ? 15  LYS B CG  1 
ATOM   973  C CG  B LYS B 1 15  ? 2.578   3.589  29.367  0.50 23.97 ? 15  LYS B CG  1 
ATOM   974  C CD  A LYS B 1 15  ? 0.530   4.486  31.630  0.50 34.01 ? 15  LYS B CD  1 
ATOM   975  C CD  B LYS B 1 15  ? 3.442   3.188  30.528  0.50 27.77 ? 15  LYS B CD  1 
ATOM   976  C CE  A LYS B 1 15  ? 0.593   2.995  31.380  0.50 36.87 ? 15  LYS B CE  1 
ATOM   977  C CE  B LYS B 1 15  ? 3.611   1.688  30.673  0.50 27.40 ? 15  LYS B CE  1 
ATOM   978  N NZ  A LYS B 1 15  ? -0.658  2.239  31.710  0.50 37.42 ? 15  LYS B NZ  1 
ATOM   979  N NZ  B LYS B 1 15  ? 4.025   1.321  32.049  0.50 29.49 ? 15  LYS B NZ  1 
ATOM   980  N N   . VAL B 1 16  ? 4.887   5.646  27.844  1.00 15.65 ? 16  VAL B N   1 
ATOM   981  C CA  . VAL B 1 16  ? 5.701   5.532  26.615  1.00 15.14 ? 16  VAL B CA  1 
ATOM   982  C C   . VAL B 1 16  ? 6.425   4.217  26.645  1.00 16.50 ? 16  VAL B C   1 
ATOM   983  O O   . VAL B 1 16  ? 7.158   3.934  27.627  1.00 15.07 ? 16  VAL B O   1 
ATOM   984  C CB  . VAL B 1 16  ? 6.614   6.745  26.375  1.00 16.35 ? 16  VAL B CB  1 
ATOM   985  C CG1 . VAL B 1 16  ? 7.208   6.661  24.972  1.00 16.57 ? 16  VAL B CG1 1 
ATOM   986  C CG2 . VAL B 1 16  ? 5.886   8.058  26.589  1.00 17.76 ? 16  VAL B CG2 1 
ATOM   987  N N   . LEU B 1 17  ? 6.309   3.423  25.572  1.00 15.15 ? 17  LEU B N   1 
ATOM   988  C CA  . LEU B 1 17  ? 6.958   2.122  25.447  1.00 15.11 ? 17  LEU B CA  1 
ATOM   989  C C   . LEU B 1 17  ? 7.860   2.127  24.227  1.00 14.62 ? 17  LEU B C   1 
ATOM   990  O O   . LEU B 1 17  ? 7.593   2.886  23.237  1.00 15.10 ? 17  LEU B O   1 
ATOM   991  C CB  . LEU B 1 17  ? 5.916   1.004  25.290  1.00 15.28 ? 17  LEU B CB  1 
ATOM   992  C CG  . LEU B 1 17  ? 4.944   0.826  26.454  1.00 17.76 ? 17  LEU B CG  1 
ATOM   993  C CD1 . LEU B 1 17  ? 3.924   -0.262 26.172  1.00 20.69 ? 17  LEU B CD1 1 
ATOM   994  C CD2 . LEU B 1 17  ? 5.679   0.497  27.720  1.00 21.49 ? 17  LEU B CD2 1 
ATOM   995  N N   . ASP B 1 18  ? 8.869   1.271  24.268  1.00 14.56 ? 18  ASP B N   1 
ATOM   996  C CA  . ASP B 1 18  ? 9.888   1.147  23.200  1.00 13.95 ? 18  ASP B CA  1 
ATOM   997  C C   . ASP B 1 18  ? 9.701   -0.210 22.524  1.00 14.97 ? 18  ASP B C   1 
ATOM   998  O O   . ASP B 1 18  ? 9.851   -1.193 23.178  1.00 15.18 ? 18  ASP B O   1 
ATOM   999  C CB  . ASP B 1 18  ? 11.277  1.387  23.798  1.00 13.92 ? 18  ASP B CB  1 
ATOM   1000 C CG  . ASP B 1 18  ? 12.460  1.146  22.884  1.00 17.09 ? 18  ASP B CG  1 
ATOM   1001 O OD1 . ASP B 1 18  ? 12.337  0.391  21.954  1.00 16.50 ? 18  ASP B OD1 1 
ATOM   1002 O OD2 . ASP B 1 18  ? 13.492  1.690  23.184  1.00 19.14 ? 18  ASP B OD2 1 
ATOM   1003 N N   . ALA B 1 19  ? 9.372   -0.180 21.238  1.00 14.17 ? 19  ALA B N   1 
ATOM   1004 C CA  . ALA B 1 19  ? 9.086   -1.378 20.433  1.00 14.61 ? 19  ALA B CA  1 
ATOM   1005 C C   . ALA B 1 19  ? 10.339  -2.056 19.888  1.00 17.52 ? 19  ALA B C   1 
ATOM   1006 O O   . ALA B 1 19  ? 10.253  -3.185 19.373  1.00 17.30 ? 19  ALA B O   1 
ATOM   1007 C CB  . ALA B 1 19  ? 8.106   -1.029 19.325  1.00 16.12 ? 19  ALA B CB  1 
ATOM   1008 N N   . VAL B 1 20  ? 11.514  -1.442 19.944  1.00 16.14 ? 20  VAL B N   1 
ATOM   1009 C CA  . VAL B 1 20  ? 12.813  -2.007 19.538  1.00 17.86 ? 20  VAL B CA  1 
ATOM   1010 C C   . VAL B 1 20  ? 13.392  -2.773 20.734  1.00 18.75 ? 20  VAL B C   1 
ATOM   1011 O O   . VAL B 1 20  ? 13.870  -3.865 20.493  1.00 23.42 ? 20  VAL B O   1 
ATOM   1012 C CB  . VAL B 1 20  ? 13.736  -0.876 19.057  1.00 19.80 ? 20  VAL B CB  1 
ATOM   1013 C CG1 . VAL B 1 20  ? 15.158  -1.370 18.830  1.00 22.13 ? 20  VAL B CG1 1 
ATOM   1014 C CG2 . VAL B 1 20  ? 13.173  -0.207 17.838  1.00 20.14 ? 20  VAL B CG2 1 
ATOM   1015 N N   . ARG B 1 21  ? 13.387  -2.201 21.922  1.00 19.17 ? 21  ARG B N   1 
ATOM   1016 C CA  . ARG B 1 21  ? 14.010  -2.844 23.109  1.00 20.82 ? 21  ARG B CA  1 
ATOM   1017 C C   . ARG B 1 21  ? 12.978  -3.682 23.872  1.00 22.76 ? 21  ARG B C   1 
ATOM   1018 O O   . ARG B 1 21  ? 13.413  -4.440 24.765  1.00 21.19 ? 21  ARG B O   1 
ATOM   1019 C CB  . ARG B 1 21  ? 14.626  -1.742 23.973  1.00 25.61 ? 21  ARG B CB  1 
ATOM   1020 C CG  . ARG B 1 21  ? 15.661  -0.958 23.175  1.00 33.24 ? 21  ARG B CG  1 
ATOM   1021 C CD  . ARG B 1 21  ? 16.783  -0.237 23.892  1.00 43.54 ? 21  ARG B CD  1 
ATOM   1022 N NE  . ARG B 1 21  ? 16.561  -0.019 25.311  1.00 51.82 ? 21  ARG B NE  1 
ATOM   1023 C CZ  . ARG B 1 21  ? 15.896  1.001  25.839  1.00 62.86 ? 21  ARG B CZ  1 
ATOM   1024 N NH1 . ARG B 1 21  ? 15.369  1.933  25.063  1.00 71.38 ? 21  ARG B NH1 1 
ATOM   1025 N NH2 . ARG B 1 21  ? 15.765  1.089  27.155  1.00 70.55 ? 21  ARG B NH2 1 
ATOM   1026 N N   . GLY B 1 22  ? 11.678  -3.493 23.674  1.00 17.16 ? 22  GLY B N   1 
ATOM   1027 C CA  . GLY B 1 22  ? 10.695  -4.201 24.504  1.00 16.03 ? 22  GLY B CA  1 
ATOM   1028 C C   . GLY B 1 22  ? 10.710  -3.743 25.927  1.00 17.17 ? 22  GLY B C   1 
ATOM   1029 O O   . GLY B 1 22  ? 10.732  -4.575 26.872  1.00 18.09 ? 22  GLY B O   1 
ATOM   1030 N N   . SER B 1 23  ? 10.687  -2.444 26.126  1.00 17.53 ? 23  SER B N   1 
ATOM   1031 C CA  . SER B 1 23  ? 10.952  -1.853 27.447  1.00 18.72 ? 23  SER B CA  1 
ATOM   1032 C C   . SER B 1 23  ? 10.097  -0.613 27.564  1.00 19.01 ? 23  SER B C   1 
ATOM   1033 O O   . SER B 1 23  ? 9.611   -0.057 26.570  1.00 17.96 ? 23  SER B O   1 
ATOM   1034 C CB  . SER B 1 23  ? 12.396  -1.507 27.594  1.00 21.14 ? 23  SER B CB  1 
ATOM   1035 O OG  . SER B 1 23  ? 12.763  -0.444 26.738  1.00 25.11 ? 23  SER B OG  1 
ATOM   1036 N N   . PRO B 1 24  ? 9.900   -0.095 28.776  1.00 18.32 ? 24  PRO B N   1 
ATOM   1037 C CA  . PRO B 1 24  ? 9.479   1.273  28.941  1.00 18.83 ? 24  PRO B CA  1 
ATOM   1038 C C   . PRO B 1 24  ? 10.490  2.176  28.239  1.00 18.03 ? 24  PRO B C   1 
ATOM   1039 O O   . PRO B 1 24  ? 11.656  1.855  28.149  1.00 19.47 ? 24  PRO B O   1 
ATOM   1040 C CB  . PRO B 1 24  ? 9.484   1.512  30.452  1.00 20.50 ? 24  PRO B CB  1 
ATOM   1041 C CG  . PRO B 1 24  ? 10.174  0.335  31.029  1.00 24.15 ? 24  PRO B CG  1 
ATOM   1042 C CD  . PRO B 1 24  ? 10.188  -0.792 30.051  1.00 19.68 ? 24  PRO B CD  1 
ATOM   1043 N N   . ALA B 1 25  ? 9.985   3.323  27.752  1.00 16.27 ? 25  ALA B N   1 
ATOM   1044 C CA  . ALA B 1 25  ? 10.842  4.356  27.147  1.00 16.49 ? 25  ALA B CA  1 
ATOM   1045 C C   . ALA B 1 25  ? 11.147  5.356  28.290  1.00 15.67 ? 25  ALA B C   1 
ATOM   1046 O O   . ALA B 1 25  ? 10.251  6.082  28.718  1.00 17.82 ? 25  ALA B O   1 
ATOM   1047 C CB  . ALA B 1 25  ? 10.162  4.958  25.954  1.00 16.08 ? 25  ALA B CB  1 
ATOM   1048 N N   . ILE B 1 26  ? 12.368  5.257  28.819  1.00 18.13 ? 26  ILE B N   1 
ATOM   1049 C CA  . ILE B 1 26  ? 12.809  5.958  30.040  1.00 20.36 ? 26  ILE B CA  1 
ATOM   1050 C C   . ILE B 1 26  ? 13.463  7.270  29.658  1.00 19.11 ? 26  ILE B C   1 
ATOM   1051 O O   . ILE B 1 26  ? 14.174  7.362  28.664  1.00 20.75 ? 26  ILE B O   1 
ATOM   1052 C CB  . ILE B 1 26  ? 13.742  5.034  30.852  1.00 22.84 ? 26  ILE B CB  1 
ATOM   1053 C CG1 . ILE B 1 26  ? 13.071  3.714  31.218  1.00 24.86 ? 26  ILE B CG1 1 
ATOM   1054 C CG2 . ILE B 1 26  ? 14.274  5.766  32.054  1.00 28.20 ? 26  ILE B CG2 1 
ATOM   1055 C CD1 . ILE B 1 26  ? 14.088  2.665  31.613  1.00 29.04 ? 26  ILE B CD1 1 
ATOM   1056 N N   . ASN B 1 27  ? 13.148  8.293  30.433  1.00 19.34 ? 27  ASN B N   1 
ATOM   1057 C CA  . ASN B 1 27  ? 13.810  9.613  30.279  1.00 23.33 ? 27  ASN B CA  1 
ATOM   1058 C C   . ASN B 1 27  ? 13.425  10.303 28.983  1.00 22.00 ? 27  ASN B C   1 
ATOM   1059 O O   . ASN B 1 27  ? 14.229  11.050 28.387  1.00 23.09 ? 27  ASN B O   1 
ATOM   1060 C CB  . ASN B 1 27  ? 15.311  9.510  30.481  1.00 26.38 ? 27  ASN B CB  1 
ATOM   1061 C CG  . ASN B 1 27  ? 15.571  10.258 31.756  1.00 42.65 ? 27  ASN B CG  1 
ATOM   1062 O OD1 . ASN B 1 27  ? 15.551  11.490 31.740  1.00 45.68 ? 27  ASN B OD1 1 
ATOM   1063 N ND2 . ASN B 1 27  ? 15.539  9.528  32.856  1.00 43.20 ? 27  ASN B ND2 1 
ATOM   1064 N N   . VAL B 1 28  ? 12.205  10.073 28.558  1.00 18.30 ? 28  VAL B N   1 
ATOM   1065 C CA  . VAL B 1 28  ? 11.656  10.767 27.372  1.00 18.23 ? 28  VAL B CA  1 
ATOM   1066 C C   . VAL B 1 28  ? 11.044  12.074 27.830  1.00 17.43 ? 28  VAL B C   1 
ATOM   1067 O O   . VAL B 1 28  ? 10.172  12.067 28.722  1.00 16.49 ? 28  VAL B O   1 
ATOM   1068 C CB  . VAL B 1 28  ? 10.626  9.904  26.640  1.00 20.31 ? 28  VAL B CB  1 
ATOM   1069 C CG1 . VAL B 1 28  ? 10.081  10.602 25.404  1.00 21.54 ? 28  VAL B CG1 1 
ATOM   1070 C CG2 . VAL B 1 28  ? 11.254  8.585  26.269  1.00 21.20 ? 28  VAL B CG2 1 
ATOM   1071 N N   . ALA B 1 29  ? 11.466  13.183 27.222  1.00 16.81 ? 29  ALA B N   1 
ATOM   1072 C CA  . ALA B 1 29  ? 10.819  14.470 27.520  1.00 16.83 ? 29  ALA B CA  1 
ATOM   1073 C C   . ALA B 1 29  ? 9.440   14.546 26.903  1.00 16.74 ? 29  ALA B C   1 
ATOM   1074 O O   . ALA B 1 29  ? 9.220   14.109 25.762  1.00 16.48 ? 29  ALA B O   1 
ATOM   1075 C CB  . ALA B 1 29  ? 11.626  15.622 27.016  1.00 16.13 ? 29  ALA B CB  1 
ATOM   1076 N N   . VAL B 1 30  ? 8.514   15.062 27.686  1.00 15.90 ? 30  VAL B N   1 
ATOM   1077 C CA  . VAL B 1 30  ? 7.116   15.252 27.292  1.00 15.13 ? 30  VAL B CA  1 
ATOM   1078 C C   . VAL B 1 30  ? 6.732   16.685 27.601  1.00 16.77 ? 30  VAL B C   1 
ATOM   1079 O O   . VAL B 1 30  ? 6.929   17.060 28.741  1.00 18.73 ? 30  VAL B O   1 
ATOM   1080 C CB  . VAL B 1 30  ? 6.224   14.255 27.990  1.00 16.40 ? 30  VAL B CB  1 
ATOM   1081 C CG1 . VAL B 1 30  ? 4.775   14.439 27.581  1.00 18.02 ? 30  VAL B CG1 1 
ATOM   1082 C CG2 . VAL B 1 30  ? 6.660   12.823 27.735  1.00 16.48 ? 30  VAL B CG2 1 
ATOM   1083 N N   . HIS B 1 31  ? 6.129   17.361 26.648  1.00 16.75 ? 31  HIS B N   1 
ATOM   1084 C CA  . HIS B 1 31  ? 5.600   18.731 26.809  1.00 17.35 ? 31  HIS B CA  1 
ATOM   1085 C C   . HIS B 1 31  ? 4.126   18.763 26.523  1.00 18.60 ? 31  HIS B C   1 
ATOM   1086 O O   . HIS B 1 31  ? 3.673   18.252 25.446  1.00 20.13 ? 31  HIS B O   1 
ATOM   1087 C CB  . HIS B 1 31  ? 6.338   19.736 25.942  1.00 18.75 ? 31  HIS B CB  1 
ATOM   1088 C CG  . HIS B 1 31  ? 7.779   19.821 26.282  1.00 21.43 ? 31  HIS B CG  1 
ATOM   1089 N ND1 . HIS B 1 31  ? 8.275   20.910 26.963  1.00 26.88 ? 31  HIS B ND1 1 
ATOM   1090 C CD2 . HIS B 1 31  ? 8.827   19.010 26.016  1.00 27.12 ? 31  HIS B CD2 1 
ATOM   1091 C CE1 . HIS B 1 31  ? 9.572   20.709 27.171  1.00 28.42 ? 31  HIS B CE1 1 
ATOM   1092 N NE2 . HIS B 1 31  ? 9.940   19.579 26.582  1.00 29.26 ? 31  HIS B NE2 1 
ATOM   1093 N N   . VAL B 1 32  ? 3.342   19.352 27.387  1.00 17.07 ? 32  VAL B N   1 
ATOM   1094 C CA  . VAL B 1 32  ? 1.884   19.449 27.205  1.00 18.34 ? 32  VAL B CA  1 
ATOM   1095 C C   . VAL B 1 32  ? 1.544   20.909 27.004  1.00 19.93 ? 32  VAL B C   1 
ATOM   1096 O O   . VAL B 1 32  ? 2.144   21.750 27.731  1.00 20.19 ? 32  VAL B O   1 
ATOM   1097 C CB  . VAL B 1 32  ? 1.111   18.866 28.381  1.00 18.59 ? 32  VAL B CB  1 
ATOM   1098 C CG1 . VAL B 1 32  ? -0.352  18.904 28.124  1.00 18.80 ? 32  VAL B CG1 1 
ATOM   1099 C CG2 . VAL B 1 32  ? 1.571   17.481 28.752  1.00 19.34 ? 32  VAL B CG2 1 
ATOM   1100 N N   . PHE B 1 33  ? 0.725   21.185 26.018  1.00 19.00 ? 33  PHE B N   1 
ATOM   1101 C CA  . PHE B 1 33  ? 0.309   22.548 25.615  1.00 21.06 ? 33  PHE B CA  1 
ATOM   1102 C C   . PHE B 1 33  ? -1.198  22.604 25.653  1.00 21.54 ? 33  PHE B C   1 
ATOM   1103 O O   . PHE B 1 33  ? -1.844  21.591 25.446  1.00 18.83 ? 33  PHE B O   1 
ATOM   1104 C CB  . PHE B 1 33  ? 0.854   22.917 24.236  1.00 21.17 ? 33  PHE B CB  1 
ATOM   1105 C CG  . PHE B 1 33  ? 2.342   22.783 24.075  1.00 23.29 ? 33  PHE B CG  1 
ATOM   1106 C CD1 . PHE B 1 33  ? 2.926   21.561 23.718  1.00 22.62 ? 33  PHE B CD1 1 
ATOM   1107 C CD2 . PHE B 1 33  ? 3.176   23.889 24.190  1.00 26.27 ? 33  PHE B CD2 1 
ATOM   1108 C CE1 . PHE B 1 33  ? 4.298   21.448 23.540  1.00 26.31 ? 33  PHE B CE1 1 
ATOM   1109 C CE2 . PHE B 1 33  ? 4.555   23.771 24.043  1.00 26.99 ? 33  PHE B CE2 1 
ATOM   1110 C CZ  . PHE B 1 33  ? 5.118   22.557 23.728  1.00 28.01 ? 33  PHE B CZ  1 
ATOM   1111 N N   . ARG B 1 34  ? -1.740  23.778 25.941  1.00 22.00 ? 34  ARG B N   1 
ATOM   1112 C CA  . ARG B 1 34  ? -3.187  24.032 25.838  1.00 21.14 ? 34  ARG B CA  1 
ATOM   1113 C C   . ARG B 1 34  ? -3.418  25.093 24.778  1.00 21.51 ? 34  ARG B C   1 
ATOM   1114 O O   . ARG B 1 34  ? -2.661  26.078 24.768  1.00 25.84 ? 34  ARG B O   1 
ATOM   1115 C CB  . ARG B 1 34  ? -3.781  24.449 27.192  1.00 24.22 ? 34  ARG B CB  1 
ATOM   1116 C CG  . ARG B 1 34  ? -5.296  24.567 27.173  1.00 28.15 ? 34  ARG B CG  1 
ATOM   1117 C CD  . ARG B 1 34  ? -5.874  24.896 28.559  1.00 32.40 ? 34  ARG B CD  1 
ATOM   1118 N NE  . ARG B 1 34  ? -7.330  24.892 28.475  1.00 37.33 ? 34  ARG B NE  1 
ATOM   1119 C CZ  . ARG B 1 34  ? -8.062  25.942 28.099  1.00 42.27 ? 34  ARG B CZ  1 
ATOM   1120 N NH1 . ARG B 1 34  ? -7.480  27.106 27.863  1.00 48.26 ? 34  ARG B NH1 1 
ATOM   1121 N NH2 . ARG B 1 34  ? -9.380  25.841 28.020  1.00 40.38 ? 34  ARG B NH2 1 
ATOM   1122 N N   . LYS B 1 35  ? -4.413  24.919 23.928  1.00 21.66 ? 35  LYS B N   1 
ATOM   1123 C CA  . LYS B 1 35  ? -4.710  25.875 22.828  1.00 27.73 ? 35  LYS B CA  1 
ATOM   1124 C C   . LYS B 1 35  ? -5.355  27.118 23.459  1.00 28.27 ? 35  LYS B C   1 
ATOM   1125 O O   . LYS B 1 35  ? -6.284  26.955 24.257  1.00 26.53 ? 35  LYS B O   1 
ATOM   1126 C CB  . LYS B 1 35  ? -5.579  25.251 21.735  1.00 31.19 ? 35  LYS B CB  1 
ATOM   1127 C CG  . LYS B 1 35  ? -5.394  25.880 20.366  1.00 39.10 ? 35  LYS B CG  1 
ATOM   1128 C CD  . LYS B 1 35  ? -6.162  25.209 19.241  1.00 45.25 ? 35  LYS B CD  1 
ATOM   1129 C CE  . LYS B 1 35  ? -7.592  25.695 19.097  1.00 56.33 ? 35  LYS B CE  1 
ATOM   1130 N NZ  . LYS B 1 35  ? -8.111  25.495 17.717  1.00 61.27 ? 35  LYS B NZ  1 
ATOM   1131 N N   . ALA B 1 36  ? -4.747  28.281 23.233  1.00 29.91 ? 36  ALA B N   1 
ATOM   1132 C CA  . ALA B 1 36  ? -5.254  29.572 23.741  1.00 34.52 ? 36  ALA B CA  1 
ATOM   1133 C C   . ALA B 1 36  ? -6.258  30.137 22.747  1.00 37.47 ? 36  ALA B C   1 
ATOM   1134 O O   . ALA B 1 36  ? -6.318  29.648 21.607  1.00 37.29 ? 36  ALA B O   1 
ATOM   1135 C CB  . ALA B 1 36  ? -4.124  30.515 23.970  1.00 35.26 ? 36  ALA B CB  1 
ATOM   1136 N N   . ALA B 1 37  ? -6.982  31.181 23.167  1.00 46.42 ? 37  ALA B N   1 
ATOM   1137 C CA  . ALA B 1 37  ? -8.082  31.837 22.410  1.00 47.38 ? 37  ALA B CA  1 
ATOM   1138 C C   . ALA B 1 37  ? -7.583  32.331 21.046  1.00 45.23 ? 37  ALA B C   1 
ATOM   1139 O O   . ALA B 1 37  ? -8.351  32.218 20.079  1.00 50.34 ? 37  ALA B O   1 
ATOM   1140 C CB  . ALA B 1 37  ? -8.661  32.970 23.232  1.00 49.92 ? 37  ALA B CB  1 
ATOM   1141 N N   . ASP B 1 38  ? -6.319  32.762 21.001  1.00 46.66 ? 38  ASP B N   1 
ATOM   1142 C CA  . ASP B 1 38  ? -5.644  33.273 19.779  1.00 49.82 ? 38  ASP B CA  1 
ATOM   1143 C C   . ASP B 1 38  ? -5.113  32.122 18.918  1.00 54.72 ? 38  ASP B C   1 
ATOM   1144 O O   . ASP B 1 38  ? -4.337  32.430 18.022  1.00 49.89 ? 38  ASP B O   1 
ATOM   1145 C CB  . ASP B 1 38  ? -4.587  34.331 20.088  1.00 47.71 ? 38  ASP B CB  1 
ATOM   1146 C CG  . ASP B 1 38  ? -3.336  33.775 20.720  1.00 50.80 ? 38  ASP B CG  1 
ATOM   1147 O OD1 . ASP B 1 38  ? -3.309  32.571 20.966  1.00 46.13 ? 38  ASP B OD1 1 
ATOM   1148 O OD2 . ASP B 1 38  ? -2.430  34.558 20.985  1.00 51.36 ? 38  ASP B OD2 1 
ATOM   1149 N N   . ASP B 1 39  ? -5.471  30.879 19.268  1.00 54.31 ? 39  ASP B N   1 
ATOM   1150 C CA  . ASP B 1 39  ? -5.203  29.641 18.486  1.00 53.55 ? 39  ASP B CA  1 
ATOM   1151 C C   . ASP B 1 39  ? -3.711  29.305 18.522  1.00 43.87 ? 39  ASP B C   1 
ATOM   1152 O O   . ASP B 1 39  ? -3.296  28.428 17.751  1.00 49.30 ? 39  ASP B O   1 
ATOM   1153 C CB  . ASP B 1 39  ? -5.699  29.733 17.035  1.00 62.12 ? 39  ASP B CB  1 
ATOM   1154 C CG  . ASP B 1 39  ? -7.081  29.145 16.818  1.00 65.80 ? 39  ASP B CG  1 
ATOM   1155 O OD1 . ASP B 1 39  ? -7.448  28.227 17.560  1.00 72.84 ? 39  ASP B OD1 1 
ATOM   1156 O OD2 . ASP B 1 39  ? -7.782  29.620 15.909  1.00 77.62 ? 39  ASP B OD2 1 
ATOM   1157 N N   . THR B 1 40  ? -2.946  29.906 19.427  1.00 35.66 ? 40  THR B N   1 
ATOM   1158 C CA  . THR B 1 40  ? -1.541  29.505 19.715  1.00 32.84 ? 40  THR B CA  1 
ATOM   1159 C C   . THR B 1 40  ? -1.498  28.443 20.822  1.00 33.10 ? 40  THR B C   1 
ATOM   1160 O O   . THR B 1 40  ? -2.445  28.330 21.581  1.00 33.73 ? 40  THR B O   1 
ATOM   1161 C CB  . THR B 1 40  ? -0.714  30.745 20.040  1.00 37.84 ? 40  THR B CB  1 
ATOM   1162 O OG1 . THR B 1 40  ? -1.164  31.164 21.323  1.00 36.43 ? 40  THR B OG1 1 
ATOM   1163 C CG2 . THR B 1 40  ? -0.902  31.839 19.008  1.00 42.54 ? 40  THR B CG2 1 
ATOM   1164 N N   . TRP B 1 41  ? -0.392  27.727 20.895  1.00 33.27 ? 41  TRP B N   1 
ATOM   1165 C CA  . TRP B 1 41  ? -0.136  26.629 21.848  1.00 33.64 ? 41  TRP B CA  1 
ATOM   1166 C C   . TRP B 1 41  ? 0.632   27.219 23.024  1.00 34.03 ? 41  TRP B C   1 
ATOM   1167 O O   . TRP B 1 41  ? 1.750   27.700 22.799  1.00 39.66 ? 41  TRP B O   1 
ATOM   1168 C CB  . TRP B 1 41  ? 0.673   25.536 21.170  1.00 30.23 ? 41  TRP B CB  1 
ATOM   1169 C CG  . TRP B 1 41  ? -0.119  24.752 20.187  1.00 31.71 ? 41  TRP B CG  1 
ATOM   1170 C CD1 . TRP B 1 41  ? 0.036   24.714 18.830  1.00 37.89 ? 41  TRP B CD1 1 
ATOM   1171 C CD2 . TRP B 1 41  ? -1.252  23.914 20.493  1.00 27.40 ? 41  TRP B CD2 1 
ATOM   1172 N NE1 . TRP B 1 41  ? -0.883  23.863 18.283  1.00 38.00 ? 41  TRP B NE1 1 
ATOM   1173 C CE2 . TRP B 1 41  ? -1.673  23.342 19.279  1.00 33.71 ? 41  TRP B CE2 1 
ATOM   1174 C CE3 . TRP B 1 41  ? -1.879  23.520 21.682  1.00 24.79 ? 41  TRP B CE3 1 
ATOM   1175 C CZ2 . TRP B 1 41  ? -2.757  22.469 19.204  1.00 30.04 ? 41  TRP B CZ2 1 
ATOM   1176 C CZ3 . TRP B 1 41  ? -2.911  22.617 21.613  1.00 27.15 ? 41  TRP B CZ3 1 
ATOM   1177 C CH2 . TRP B 1 41  ? -3.354  22.120 20.388  1.00 25.19 ? 41  TRP B CH2 1 
ATOM   1178 N N   . GLU B 1 42  ? 0.026   27.243 24.197  1.00 31.05 ? 42  GLU B N   1 
ATOM   1179 C CA  . GLU B 1 42  ? 0.669   27.727 25.439  1.00 33.66 ? 42  GLU B CA  1 
ATOM   1180 C C   . GLU B 1 42  ? 1.233   26.543 26.210  1.00 30.61 ? 42  GLU B C   1 
ATOM   1181 O O   . GLU B 1 42  ? 0.476   25.604 26.487  1.00 26.84 ? 42  GLU B O   1 
ATOM   1182 C CB  . GLU B 1 42  ? -0.356  28.396 26.344  1.00 41.13 ? 42  GLU B CB  1 
ATOM   1183 C CG  . GLU B 1 42  ? -1.173  29.455 25.642  1.00 51.23 ? 42  GLU B CG  1 
ATOM   1184 C CD  . GLU B 1 42  ? -1.257  30.755 26.420  1.00 58.61 ? 42  GLU B CD  1 
ATOM   1185 O OE1 . GLU B 1 42  ? -0.889  31.803 25.851  1.00 61.17 ? 42  GLU B OE1 1 
ATOM   1186 O OE2 . GLU B 1 42  ? -1.686  30.709 27.591  1.00 70.76 ? 42  GLU B OE2 1 
ATOM   1187 N N   . PRO B 1 43  ? 2.510   26.572 26.648  1.00 28.53 ? 43  PRO B N   1 
ATOM   1188 C CA  . PRO B 1 43  ? 3.009   25.564 27.574  1.00 26.80 ? 43  PRO B CA  1 
ATOM   1189 C C   . PRO B 1 43  ? 2.120   25.433 28.800  1.00 25.23 ? 43  PRO B C   1 
ATOM   1190 O O   . PRO B 1 43  ? 1.655   26.428 29.357  1.00 29.07 ? 43  PRO B O   1 
ATOM   1191 C CB  . PRO B 1 43  ? 4.416   26.057 27.962  1.00 29.15 ? 43  PRO B CB  1 
ATOM   1192 C CG  . PRO B 1 43  ? 4.825   26.909 26.801  1.00 29.81 ? 43  PRO B CG  1 
ATOM   1193 C CD  . PRO B 1 43  ? 3.552   27.554 26.306  1.00 30.31 ? 43  PRO B CD  1 
ATOM   1194 N N   . PHE B 1 44  ? 1.909   24.193 29.225  1.00 23.24 ? 44  PHE B N   1 
ATOM   1195 C CA  . PHE B 1 44  ? 0.931   23.785 30.268  1.00 23.28 ? 44  PHE B CA  1 
ATOM   1196 C C   . PHE B 1 44  ? 1.632   22.937 31.333  1.00 25.02 ? 44  PHE B C   1 
ATOM   1197 O O   . PHE B 1 44  ? 1.498   23.209 32.543  1.00 28.81 ? 44  PHE B O   1 
ATOM   1198 C CB  . PHE B 1 44  ? -0.279  23.099 29.602  1.00 23.99 ? 44  PHE B CB  1 
ATOM   1199 C CG  . PHE B 1 44  ? -1.314  22.648 30.592  1.00 27.05 ? 44  PHE B CG  1 
ATOM   1200 C CD1 . PHE B 1 44  ? -2.219  23.566 31.109  1.00 31.28 ? 44  PHE B CD1 1 
ATOM   1201 C CD2 . PHE B 1 44  ? -1.440  21.308 30.934  1.00 25.66 ? 44  PHE B CD2 1 
ATOM   1202 C CE1 . PHE B 1 44  ? -3.174  23.153 32.022  1.00 30.38 ? 44  PHE B CE1 1 
ATOM   1203 C CE2 . PHE B 1 44  ? -2.351  20.907 31.910  1.00 35.37 ? 44  PHE B CE2 1 
ATOM   1204 C CZ  . PHE B 1 44  ? -3.218  21.860 32.457  1.00 27.96 ? 44  PHE B CZ  1 
ATOM   1205 N N   . ALA B 1 45  ? 2.475   21.985 30.929  1.00 20.48 ? 45  ALA B N   1 
ATOM   1206 C CA  . ALA B 1 45  ? 3.055   20.982 31.839  1.00 24.85 ? 45  ALA B CA  1 
ATOM   1207 C C   . ALA B 1 45  ? 4.137   20.286 31.075  1.00 18.46 ? 45  ALA B C   1 
ATOM   1208 O O   . ALA B 1 45  ? 4.063   20.225 29.832  1.00 21.24 ? 45  ALA B O   1 
ATOM   1209 C CB  . ALA B 1 45  ? 2.034   20.059 32.405  1.00 22.03 ? 45  ALA B CB  1 
ATOM   1210 N N   . SER B 1 46  ? 5.127   19.810 31.765  1.00 17.69 ? 46  SER B N   1 
ATOM   1211 C CA  . SER B 1 46  ? 6.138   18.960 31.109  1.00 16.45 ? 46  SER B CA  1 
ATOM   1212 C C   . SER B 1 46  ? 6.818   18.084 32.141  1.00 18.43 ? 46  SER B C   1 
ATOM   1213 O O   . SER B 1 46  ? 6.698   18.306 33.343  1.00 19.86 ? 46  SER B O   1 
ATOM   1214 C CB  . SER B 1 46  ? 7.131   19.716 30.274  1.00 18.10 ? 46  SER B CB  1 
ATOM   1215 O OG  . SER B 1 46  ? 7.805   20.685 31.106  1.00 17.77 ? 46  SER B OG  1 
ATOM   1216 N N   . GLY B 1 47  ? 7.594   17.109 31.685  1.00 16.69 ? 47  GLY B N   1 
ATOM   1217 C CA  . GLY B 1 47  ? 8.412   16.260 32.529  1.00 17.86 ? 47  GLY B CA  1 
ATOM   1218 C C   . GLY B 1 47  ? 9.090   15.190 31.705  1.00 18.17 ? 47  GLY B C   1 
ATOM   1219 O O   . GLY B 1 47  ? 9.158   15.362 30.471  1.00 18.24 ? 47  GLY B O   1 
ATOM   1220 N N   . LYS B 1 48  ? 9.697   14.243 32.376  1.00 18.51 ? 48  LYS B N   1 
ATOM   1221 C CA  . LYS B 1 48  ? 10.441  13.165 31.705  1.00 19.72 ? 48  LYS B CA  1 
ATOM   1222 C C   . LYS B 1 48  ? 9.854   11.856 32.180  1.00 19.80 ? 48  LYS B C   1 
ATOM   1223 O O   . LYS B 1 48  ? 9.509   11.720 33.358  1.00 21.04 ? 48  LYS B O   1 
ATOM   1224 C CB  . LYS B 1 48  ? 11.942  13.218 32.002  1.00 26.14 ? 48  LYS B CB  1 
ATOM   1225 C CG  . LYS B 1 48  ? 12.655  14.385 31.347  1.00 33.92 ? 48  LYS B CG  1 
ATOM   1226 C CD  . LYS B 1 48  ? 13.844  13.975 30.527  1.00 42.73 ? 48  LYS B CD  1 
ATOM   1227 C CE  . LYS B 1 48  ? 14.989  14.958 30.569  1.00 50.99 ? 48  LYS B CE  1 
ATOM   1228 N NZ  . LYS B 1 48  ? 16.188  14.369 29.927  1.00 58.63 ? 48  LYS B NZ  1 
ATOM   1229 N N   . THR B 1 49  ? 9.683   10.875 31.289  1.00 18.26 ? 49  THR B N   1 
ATOM   1230 C CA  . THR B 1 49  ? 9.180   9.579  31.778  1.00 17.16 ? 49  THR B CA  1 
ATOM   1231 C C   . THR B 1 49  ? 10.158  8.938  32.783  1.00 17.15 ? 49  THR B C   1 
ATOM   1232 O O   . THR B 1 49  ? 11.380  9.061  32.666  1.00 18.59 ? 49  THR B O   1 
ATOM   1233 C CB  . THR B 1 49  ? 8.939   8.612  30.617  1.00 16.90 ? 49  THR B CB  1 
ATOM   1234 O OG1 . THR B 1 49  ? 10.173  8.483  29.902  1.00 17.10 ? 49  THR B OG1 1 
ATOM   1235 C CG2 . THR B 1 49  ? 7.810   9.103  29.710  1.00 18.47 ? 49  THR B CG2 1 
ATOM   1236 N N   . SER B 1 50  ? 9.565   8.205  33.692  1.00 19.83 ? 50  SER B N   1 
ATOM   1237 C CA  . SER B 1 50  ? 10.240  7.468  34.778  1.00 20.43 ? 50  SER B CA  1 
ATOM   1238 C C   . SER B 1 50  ? 10.884  6.210  34.226  1.00 24.44 ? 50  SER B C   1 
ATOM   1239 O O   . SER B 1 50  ? 10.746  5.853  33.004  1.00 20.87 ? 50  SER B O   1 
ATOM   1240 C CB  . SER B 1 50  ? 9.221   7.133  35.827  1.00 21.25 ? 50  SER B CB  1 
ATOM   1241 O OG  . SER B 1 50  ? 8.356   6.094  35.359  1.00 23.31 ? 50  SER B OG  1 
ATOM   1242 N N   . GLU B 1 51  ? 11.505  5.458  35.120  1.00 23.45 ? 51  GLU B N   1 
ATOM   1243 C CA  . GLU B 1 51  ? 12.035  4.114  34.794  1.00 25.65 ? 51  GLU B CA  1 
ATOM   1244 C C   . GLU B 1 51  ? 10.924  3.163  34.357  1.00 22.80 ? 51  GLU B C   1 
ATOM   1245 O O   . GLU B 1 51  ? 11.244  2.168  33.723  1.00 25.18 ? 51  GLU B O   1 
ATOM   1246 C CB  . GLU B 1 51  ? 12.680  3.486  36.032  1.00 30.85 ? 51  GLU B CB  1 
ATOM   1247 C CG  . GLU B 1 51  ? 14.100  3.924  36.298  1.00 41.16 ? 51  GLU B CG  1 
ATOM   1248 C CD  . GLU B 1 51  ? 14.784  2.955  37.270  1.00 52.26 ? 51  GLU B CD  1 
ATOM   1249 O OE1 . GLU B 1 51  ? 14.094  2.496  38.226  1.00 56.43 ? 51  GLU B OE1 1 
ATOM   1250 O OE2 . GLU B 1 51  ? 15.984  2.606  37.052  1.00 64.43 ? 51  GLU B OE2 1 
ATOM   1251 N N   . SER B 1 52  ? 9.662   3.433  34.653  1.00 22.73 ? 52  SER B N   1 
ATOM   1252 C CA  . SER B 1 52  ? 8.529   2.574  34.231  1.00 22.60 ? 52  SER B CA  1 
ATOM   1253 C C   . SER B 1 52  ? 7.889   3.139  32.936  1.00 19.79 ? 52  SER B C   1 
ATOM   1254 O O   . SER B 1 52  ? 6.818   2.663  32.529  1.00 22.29 ? 52  SER B O   1 
ATOM   1255 C CB  . SER B 1 52  ? 7.527   2.431  35.345  1.00 27.77 ? 52  SER B CB  1 
ATOM   1256 O OG  . SER B 1 52  ? 6.849   3.648  35.557  1.00 32.37 ? 52  SER B OG  1 
ATOM   1257 N N   . GLY B 1 53  ? 8.504   4.180  32.349  1.00 18.90 ? 53  GLY B N   1 
ATOM   1258 C CA  . GLY B 1 53  ? 7.974   4.802  31.122  1.00 19.64 ? 53  GLY B CA  1 
ATOM   1259 C C   . GLY B 1 53  ? 6.779   5.682  31.365  1.00 20.29 ? 53  GLY B C   1 
ATOM   1260 O O   . GLY B 1 53  ? 6.051   6.021  30.411  1.00 20.38 ? 53  GLY B O   1 
ATOM   1261 N N   . GLU B 1 54  ? 6.540   6.132  32.602  1.00 19.63 ? 54  GLU B N   1 
ATOM   1262 C CA  . GLU B 1 54  ? 5.313   6.844  32.975  1.00 18.94 ? 54  GLU B CA  1 
ATOM   1263 C C   . GLU B 1 54  ? 5.637   8.266  33.415  1.00 17.85 ? 54  GLU B C   1 
ATOM   1264 O O   . GLU B 1 54  ? 6.763   8.539  33.926  1.00 19.91 ? 54  GLU B O   1 
ATOM   1265 C CB  . GLU B 1 54  ? 4.584   6.156  34.131  1.00 25.25 ? 54  GLU B CB  1 
ATOM   1266 C CG  . GLU B 1 54  ? 4.132   4.769  33.762  1.00 32.35 ? 54  GLU B CG  1 
ATOM   1267 C CD  . GLU B 1 54  ? 3.375   4.025  34.859  1.00 43.07 ? 54  GLU B CD  1 
ATOM   1268 O OE1 . GLU B 1 54  ? 3.616   4.304  36.037  1.00 49.29 ? 54  GLU B OE1 1 
ATOM   1269 O OE2 . GLU B 1 54  ? 2.525   3.193  34.513  1.00 53.64 ? 54  GLU B OE2 1 
ATOM   1270 N N   . LEU B 1 55  ? 4.708   9.136  33.160  1.00 18.32 ? 55  LEU B N   1 
ATOM   1271 C CA  . LEU B 1 55  ? 4.771   10.528 33.623  1.00 18.88 ? 55  LEU B CA  1 
ATOM   1272 C C   . LEU B 1 55  ? 3.433   10.888 34.233  1.00 22.07 ? 55  LEU B C   1 
ATOM   1273 O O   . LEU B 1 55  ? 2.409   10.927 33.531  1.00 21.61 ? 55  LEU B O   1 
ATOM   1274 C CB  . LEU B 1 55  ? 5.168   11.420 32.440  1.00 19.53 ? 55  LEU B CB  1 
ATOM   1275 C CG  . LEU B 1 55  ? 5.286   12.895 32.738  1.00 21.85 ? 55  LEU B CG  1 
ATOM   1276 C CD1 . LEU B 1 55  ? 6.255   13.157 33.881  1.00 24.01 ? 55  LEU B CD1 1 
ATOM   1277 C CD2 . LEU B 1 55  ? 5.732   13.634 31.503  1.00 21.64 ? 55  LEU B CD2 1 
ATOM   1278 N N   . HIS B 1 56  ? 3.484   11.129 35.554  1.00 24.22 ? 56  HIS B N   1 
ATOM   1279 C CA  . HIS B 1 56  ? 2.355   11.430 36.466  1.00 26.47 ? 56  HIS B CA  1 
ATOM   1280 C C   . HIS B 1 56  ? 2.556   12.875 36.945  1.00 24.79 ? 56  HIS B C   1 
ATOM   1281 O O   . HIS B 1 56  ? 3.649   13.422 36.717  1.00 27.34 ? 56  HIS B O   1 
ATOM   1282 C CB  . HIS B 1 56  ? 2.373   10.510 37.712  1.00 29.41 ? 56  HIS B CB  1 
ATOM   1283 C CG  . HIS B 1 56  ? 2.215   9.063  37.440  1.00 36.30 ? 56  HIS B CG  1 
ATOM   1284 N ND1 . HIS B 1 56  ? 0.970   8.489  37.243  1.00 42.31 ? 56  HIS B ND1 1 
ATOM   1285 C CD2 . HIS B 1 56  ? 3.127   8.078  37.277  1.00 42.09 ? 56  HIS B CD2 1 
ATOM   1286 C CE1 . HIS B 1 56  ? 1.123   7.197  37.003  1.00 47.81 ? 56  HIS B CE1 1 
ATOM   1287 N NE2 . HIS B 1 56  ? 2.435   6.926  36.998  1.00 46.60 ? 56  HIS B NE2 1 
ATOM   1288 N N   . GLY B 1 57  ? 1.530   13.485 37.502  1.00 27.78 ? 57  GLY B N   1 
ATOM   1289 C CA  . GLY B 1 57  ? 1.699   14.759 38.219  1.00 27.99 ? 57  GLY B CA  1 
ATOM   1290 C C   . GLY B 1 57  ? 1.885   15.932 37.296  1.00 29.25 ? 57  GLY B C   1 
ATOM   1291 O O   . GLY B 1 57  ? 2.427   16.960 37.727  1.00 29.60 ? 57  GLY B O   1 
ATOM   1292 N N   . LEU B 1 58  ? 1.411   15.817 36.052  1.00 26.11 ? 58  LEU B N   1 
ATOM   1293 C CA  . LEU B 1 58  ? 1.483   16.911 35.072  1.00 25.39 ? 58  LEU B CA  1 
ATOM   1294 C C   . LEU B 1 58  ? 0.542   18.032 35.482  1.00 27.67 ? 58  LEU B C   1 
ATOM   1295 O O   . LEU B 1 58  ? 0.924   19.213 35.320  1.00 28.18 ? 58  LEU B O   1 
ATOM   1296 C CB  . LEU B 1 58  ? 1.158   16.358 33.685  1.00 26.20 ? 58  LEU B CB  1 
ATOM   1297 C CG  . LEU B 1 58  ? 2.297   15.546 33.090  1.00 23.55 ? 58  LEU B CG  1 
ATOM   1298 C CD1 . LEU B 1 58  ? 1.802   14.732 31.912  1.00 23.92 ? 58  LEU B CD1 1 
ATOM   1299 C CD2 . LEU B 1 58  ? 3.432   16.477 32.669  1.00 23.96 ? 58  LEU B CD2 1 
ATOM   1300 N N   . THR B 1 59  ? -0.641  17.675 35.970  1.00 25.47 ? 59  THR B N   1 
ATOM   1301 C CA  . THR B 1 59  ? -1.675  18.689 36.249  1.00 25.36 ? 59  THR B CA  1 
ATOM   1302 C C   . THR B 1 59  ? -2.586  18.204 37.361  1.00 25.23 ? 59  THR B C   1 
ATOM   1303 O O   . THR B 1 59  ? -2.344  17.140 37.955  1.00 26.89 ? 59  THR B O   1 
ATOM   1304 C CB  . THR B 1 59  ? -2.414  19.064 34.966  1.00 26.66 ? 59  THR B CB  1 
ATOM   1305 O OG1 . THR B 1 59  ? -3.315  20.155 35.194  1.00 26.91 ? 59  THR B OG1 1 
ATOM   1306 C CG2 . THR B 1 59  ? -3.203  17.907 34.381  1.00 25.44 ? 59  THR B CG2 1 
ATOM   1307 N N   . THR B 1 60  ? -3.584  19.030 37.687  1.00 26.45 ? 60  THR B N   1 
ATOM   1308 C CA  . THR B 1 60  ? -4.548  18.752 38.769  1.00 27.22 ? 60  THR B CA  1 
ATOM   1309 C C   . THR B 1 60  ? -5.940  18.776 38.165  1.00 22.97 ? 60  THR B C   1 
ATOM   1310 O O   . THR B 1 60  ? -6.127  19.382 37.096  1.00 23.12 ? 60  THR B O   1 
ATOM   1311 C CB  . THR B 1 60  ? -4.407  19.793 39.892  1.00 30.44 ? 60  THR B CB  1 
ATOM   1312 O OG1 . THR B 1 60  ? -4.664  21.084 39.344  1.00 29.09 ? 60  THR B OG1 1 
ATOM   1313 C CG2 . THR B 1 60  ? -3.022  19.779 40.520  1.00 35.23 ? 60  THR B CG2 1 
ATOM   1314 N N   . GLU B 1 61  ? -6.903  18.176 38.861  1.00 28.27 ? 61  GLU B N   1 
ATOM   1315 C CA  . GLU B 1 61  ? -8.318  18.249 38.447  1.00 29.87 ? 61  GLU B CA  1 
ATOM   1316 C C   . GLU B 1 61  ? -8.715  19.726 38.282  1.00 30.53 ? 61  GLU B C   1 
ATOM   1317 O O   . GLU B 1 61  ? -9.434  20.033 37.345  1.00 28.27 ? 61  GLU B O   1 
ATOM   1318 C CB  . GLU B 1 61  ? -9.243  17.593 39.469  1.00 37.68 ? 61  GLU B CB  1 
ATOM   1319 C CG  . GLU B 1 61  ? -9.009  16.113 39.711  1.00 48.12 ? 61  GLU B CG  1 
ATOM   1320 C CD  . GLU B 1 61  ? -10.074 15.524 40.629  1.00 59.05 ? 61  GLU B CD  1 
ATOM   1321 O OE1 . GLU B 1 61  ? -10.098 15.917 41.832  1.00 61.12 ? 61  GLU B OE1 1 
ATOM   1322 O OE2 . GLU B 1 61  ? -10.904 14.711 40.137  1.00 61.77 ? 61  GLU B OE2 1 
ATOM   1323 N N   . GLU B 1 62  ? -8.284  20.599 39.206  1.00 29.56 ? 62  GLU B N   1 
ATOM   1324 C CA  . GLU B 1 62  ? -8.629  22.043 39.176  1.00 31.33 ? 62  GLU B CA  1 
ATOM   1325 C C   . GLU B 1 62  ? -8.117  22.696 37.894  1.00 25.79 ? 62  GLU B C   1 
ATOM   1326 O O   . GLU B 1 62  ? -8.855  23.425 37.257  1.00 25.56 ? 62  GLU B O   1 
ATOM   1327 C CB  . GLU B 1 62  ? -8.053  22.782 40.394  1.00 35.08 ? 62  GLU B CB  1 
ATOM   1328 C CG  . GLU B 1 62  ? -8.770  22.456 41.691  1.00 44.94 ? 62  GLU B CG  1 
ATOM   1329 C CD  . GLU B 1 62  ? -8.914  23.633 42.640  1.00 47.57 ? 62  GLU B CD  1 
ATOM   1330 O OE1 . GLU B 1 62  ? -8.082  24.582 42.528  1.00 49.73 ? 62  GLU B OE1 1 
ATOM   1331 O OE2 . GLU B 1 62  ? -9.862  23.601 43.478  1.00 48.81 ? 62  GLU B OE2 1 
ATOM   1332 N N   . GLU B 1 63  ? -6.872  22.433 37.482  1.00 24.26 ? 63  GLU B N   1 
ATOM   1333 C CA  . GLU B 1 63  ? -6.264  23.174 36.365  1.00 25.50 ? 63  GLU B CA  1 
ATOM   1334 C C   . GLU B 1 63  ? -6.629  22.559 35.015  1.00 21.35 ? 63  GLU B C   1 
ATOM   1335 O O   . GLU B 1 63  ? -6.545  23.273 34.033  1.00 24.15 ? 63  GLU B O   1 
ATOM   1336 C CB  . GLU B 1 63  ? -4.744  23.114 36.516  1.00 28.83 ? 63  GLU B CB  1 
ATOM   1337 C CG  . GLU B 1 63  ? -4.005  23.969 35.519  1.00 36.40 ? 63  GLU B CG  1 
ATOM   1338 C CD  . GLU B 1 63  ? -2.495  23.761 35.455  1.00 45.26 ? 63  GLU B CD  1 
ATOM   1339 O OE1 . GLU B 1 63  ? -2.005  22.580 35.674  1.00 38.17 ? 63  GLU B OE1 1 
ATOM   1340 O OE2 . GLU B 1 63  ? -1.806  24.756 35.096  1.00 43.94 ? 63  GLU B OE2 1 
ATOM   1341 N N   . PHE B 1 64  ? -6.989  21.280 34.976  1.00 22.29 ? 64  PHE B N   1 
ATOM   1342 C CA  . PHE B 1 64  ? -7.204  20.560 33.697  1.00 23.38 ? 64  PHE B CA  1 
ATOM   1343 C C   . PHE B 1 64  ? -8.654  20.724 33.237  1.00 20.31 ? 64  PHE B C   1 
ATOM   1344 O O   . PHE B 1 64  ? -9.473  19.762 33.249  1.00 25.28 ? 64  PHE B O   1 
ATOM   1345 C CB  . PHE B 1 64  ? -6.832  19.084 33.844  1.00 21.16 ? 64  PHE B CB  1 
ATOM   1346 C CG  . PHE B 1 64  ? -6.719  18.296 32.547  1.00 22.28 ? 64  PHE B CG  1 
ATOM   1347 C CD1 . PHE B 1 64  ? -5.938  18.728 31.503  1.00 21.90 ? 64  PHE B CD1 1 
ATOM   1348 C CD2 . PHE B 1 64  ? -7.459  17.133 32.378  1.00 28.07 ? 64  PHE B CD2 1 
ATOM   1349 C CE1 . PHE B 1 64  ? -5.828  17.990 30.321  1.00 22.89 ? 64  PHE B CE1 1 
ATOM   1350 C CE2 . PHE B 1 64  ? -7.340  16.398 31.208  1.00 28.16 ? 64  PHE B CE2 1 
ATOM   1351 C CZ  . PHE B 1 64  ? -6.519  16.831 30.206  1.00 23.45 ? 64  PHE B CZ  1 
ATOM   1352 N N   . VAL B 1 65  ? -8.957  21.923 32.787  1.00 19.51 ? 65  VAL B N   1 
ATOM   1353 C CA  . VAL B 1 65  ? -10.307 22.277 32.323  1.00 17.98 ? 65  VAL B CA  1 
ATOM   1354 C C   . VAL B 1 65  ? -10.543 21.807 30.891  1.00 19.07 ? 65  VAL B C   1 
ATOM   1355 O O   . VAL B 1 65  ? -9.559  21.405 30.210  1.00 20.19 ? 65  VAL B O   1 
ATOM   1356 C CB  . VAL B 1 65  ? -10.545 23.786 32.415  1.00 19.97 ? 65  VAL B CB  1 
ATOM   1357 C CG1 . VAL B 1 65  ? -10.443 24.214 33.873  1.00 24.47 ? 65  VAL B CG1 1 
ATOM   1358 C CG2 . VAL B 1 65  ? -9.636  24.554 31.495  1.00 21.54 ? 65  VAL B CG2 1 
ATOM   1359 N N   . GLU B 1 66  ? -11.770 21.837 30.445  1.00 18.77 ? 66  GLU B N   1 
ATOM   1360 C CA  . GLU B 1 66  ? -12.047 21.510 29.035  1.00 19.96 ? 66  GLU B CA  1 
ATOM   1361 C C   . GLU B 1 66  ? -11.221 22.416 28.140  1.00 20.02 ? 66  GLU B C   1 
ATOM   1362 O O   . GLU B 1 66  ? -10.941 23.600 28.390  1.00 21.14 ? 66  GLU B O   1 
ATOM   1363 C CB  . GLU B 1 66  ? -13.521 21.683 28.699  1.00 19.10 ? 66  GLU B CB  1 
ATOM   1364 C CG  . GLU B 1 66  ? -14.362 20.713 29.430  1.00 21.08 ? 66  GLU B CG  1 
ATOM   1365 C CD  . GLU B 1 66  ? -15.835 20.719 29.104  1.00 24.87 ? 66  GLU B CD  1 
ATOM   1366 O OE1 . GLU B 1 66  ? -16.409 19.616 28.824  1.00 27.82 ? 66  GLU B OE1 1 
ATOM   1367 O OE2 . GLU B 1 66  ? -16.465 21.793 29.184  1.00 22.64 ? 66  GLU B OE2 1 
ATOM   1368 N N   . GLY B 1 67  ? -10.791 21.853 27.013  1.00 19.78 ? 67  GLY B N   1 
ATOM   1369 C CA  . GLY B 1 67  ? -10.003 22.595 26.042  1.00 19.89 ? 67  GLY B CA  1 
ATOM   1370 C C   . GLY B 1 67  ? -9.319  21.596 25.108  1.00 20.16 ? 67  GLY B C   1 
ATOM   1371 O O   . GLY B 1 67  ? -9.531  20.395 25.266  1.00 20.06 ? 67  GLY B O   1 
ATOM   1372 N N   . ILE B 1 68  ? -8.526  22.166 24.237  1.00 19.20 ? 68  ILE B N   1 
ATOM   1373 C CA  . ILE B 1 68  ? -7.711  21.365 23.294  1.00 18.96 ? 68  ILE B CA  1 
ATOM   1374 C C   . ILE B 1 68  ? -6.302  21.338 23.838  1.00 17.85 ? 68  ILE B C   1 
ATOM   1375 O O   . ILE B 1 68  ? -5.702  22.378 24.123  1.00 20.69 ? 68  ILE B O   1 
ATOM   1376 C CB  . ILE B 1 68  ? -7.826  21.907 21.875  1.00 20.04 ? 68  ILE B CB  1 
ATOM   1377 C CG1 . ILE B 1 68  ? -9.272  21.850 21.360  1.00 24.35 ? 68  ILE B CG1 1 
ATOM   1378 C CG2 . ILE B 1 68  ? -6.891  21.094 20.975  1.00 19.54 ? 68  ILE B CG2 1 
ATOM   1379 C CD1 . ILE B 1 68  ? -9.480  22.432 19.946  1.00 26.73 ? 68  ILE B CD1 1 
ATOM   1380 N N   . TYR B 1 69  ? -5.743  20.124 23.913  1.00 17.20 ? 69  TYR B N   1 
ATOM   1381 C CA  . TYR B 1 69  ? -4.429  19.871 24.492  1.00 17.40 ? 69  TYR B CA  1 
ATOM   1382 C C   . TYR B 1 69  ? -3.559  19.206 23.427  1.00 15.83 ? 69  TYR B C   1 
ATOM   1383 O O   . TYR B 1 69  ? -4.099  18.397 22.661  1.00 17.70 ? 69  TYR B O   1 
ATOM   1384 C CB  . TYR B 1 69  ? -4.521  19.079 25.784  1.00 17.23 ? 69  TYR B CB  1 
ATOM   1385 C CG  . TYR B 1 69  ? -5.193  19.820 26.919  1.00 18.78 ? 69  TYR B CG  1 
ATOM   1386 C CD1 . TYR B 1 69  ? -6.561  19.824 27.058  1.00 17.54 ? 69  TYR B CD1 1 
ATOM   1387 C CD2 . TYR B 1 69  ? -4.412  20.551 27.801  1.00 18.78 ? 69  TYR B CD2 1 
ATOM   1388 C CE1 . TYR B 1 69  ? -7.164  20.561 28.099  1.00 18.81 ? 69  TYR B CE1 1 
ATOM   1389 C CE2 . TYR B 1 69  ? -4.978  21.241 28.860  1.00 20.15 ? 69  TYR B CE2 1 
ATOM   1390 C CZ  . TYR B 1 69  ? -6.350  21.259 28.977  1.00 20.82 ? 69  TYR B CZ  1 
ATOM   1391 O OH  . TYR B 1 69  ? -6.928  21.953 30.022  1.00 20.84 ? 69  TYR B OH  1 
ATOM   1392 N N   . LYS B 1 70  ? -2.279  19.440 23.556  1.00 16.24 ? 70  LYS B N   1 
ATOM   1393 C CA  . LYS B 1 70  ? -1.270  18.760 22.718  1.00 17.33 ? 70  LYS B CA  1 
ATOM   1394 C C   . LYS B 1 70  ? -0.259  18.173 23.652  1.00 18.46 ? 70  LYS B C   1 
ATOM   1395 O O   . LYS B 1 70  ? 0.355   18.918 24.460  1.00 19.33 ? 70  LYS B O   1 
ATOM   1396 C CB  . LYS B 1 70  ? -0.627  19.719 21.718  1.00 18.41 ? 70  LYS B CB  1 
ATOM   1397 C CG  . LYS B 1 70  ? 0.537   19.120 20.932  1.00 21.98 ? 70  LYS B CG  1 
ATOM   1398 C CD  . LYS B 1 70  ? 1.004   20.010 19.785  1.00 28.58 ? 70  LYS B CD  1 
ATOM   1399 C CE  . LYS B 1 70  ? 1.772   21.238 20.202  1.00 38.70 ? 70  LYS B CE  1 
ATOM   1400 N NZ  . LYS B 1 70  ? 2.262   22.014 19.022  1.00 39.85 ? 70  LYS B NZ  1 
ATOM   1401 N N   . VAL B 1 71  ? 0.021   16.879 23.483  1.00 15.15 ? 71  VAL B N   1 
ATOM   1402 C CA  . VAL B 1 71  ? 1.095   16.161 24.167  1.00 15.23 ? 71  VAL B CA  1 
ATOM   1403 C C   . VAL B 1 71  ? 2.182   15.903 23.149  1.00 15.76 ? 71  VAL B C   1 
ATOM   1404 O O   . VAL B 1 71  ? 1.929   15.158 22.222  1.00 16.73 ? 71  VAL B O   1 
ATOM   1405 C CB  . VAL B 1 71  ? 0.592   14.898 24.849  1.00 14.97 ? 71  VAL B CB  1 
ATOM   1406 C CG1 . VAL B 1 71  ? 1.756   14.145 25.477  1.00 16.97 ? 71  VAL B CG1 1 
ATOM   1407 C CG2 . VAL B 1 71  ? -0.501  15.205 25.859  1.00 17.84 ? 71  VAL B CG2 1 
ATOM   1408 N N   . GLU B 1 72  ? 3.324   16.561 23.305  1.00 15.89 ? 72  GLU B N   1 
ATOM   1409 C CA  . GLU B 1 72  ? 4.465   16.380 22.395  1.00 16.07 ? 72  GLU B CA  1 
ATOM   1410 C C   . GLU B 1 72  ? 5.457   15.496 23.093  1.00 15.74 ? 72  GLU B C   1 
ATOM   1411 O O   . GLU B 1 72  ? 5.935   15.811 24.165  1.00 17.56 ? 72  GLU B O   1 
ATOM   1412 C CB  . GLU B 1 72  ? 5.030   17.757 22.059  1.00 20.51 ? 72  GLU B CB  1 
ATOM   1413 C CG  . GLU B 1 72  ? 6.131   17.718 21.042  1.00 25.53 ? 72  GLU B CG  1 
ATOM   1414 C CD  . GLU B 1 72  ? 6.356   19.137 20.498  1.00 32.53 ? 72  GLU B CD  1 
ATOM   1415 O OE1 . GLU B 1 72  ? 6.880   19.944 21.254  1.00 36.77 ? 72  GLU B OE1 1 
ATOM   1416 O OE2 . GLU B 1 72  ? 5.879   19.459 19.413  1.00 41.35 ? 72  GLU B OE2 1 
ATOM   1417 N N   . ILE B 1 73  ? 5.817   14.370 22.487  1.00 14.72 ? 73  ILE B N   1 
ATOM   1418 C CA  . ILE B 1 73  ? 6.749   13.384 23.024  1.00 14.45 ? 73  ILE B CA  1 
ATOM   1419 C C   . ILE B 1 73  ? 8.040   13.529 22.224  1.00 16.50 ? 73  ILE B C   1 
ATOM   1420 O O   . ILE B 1 73  ? 7.986   13.377 20.985  1.00 15.67 ? 73  ILE B O   1 
ATOM   1421 C CB  . ILE B 1 73  ? 6.136   11.989 22.956  1.00 16.18 ? 73  ILE B CB  1 
ATOM   1422 C CG1 . ILE B 1 73  ? 4.785   11.964 23.679  1.00 16.74 ? 73  ILE B CG1 1 
ATOM   1423 C CG2 . ILE B 1 73  ? 7.112   10.988 23.477  1.00 16.70 ? 73  ILE B CG2 1 
ATOM   1424 C CD1 . ILE B 1 73  ? 4.036   10.653 23.513  1.00 17.87 ? 73  ILE B CD1 1 
ATOM   1425 N N   . ASP B 1 74  ? 9.160   13.768 22.872  1.00 16.31 ? 74  ASP B N   1 
ATOM   1426 C CA  . ASP B 1 74  ? 10.448  14.093 22.207  1.00 17.31 ? 74  ASP B CA  1 
ATOM   1427 C C   . ASP B 1 74  ? 11.132  12.790 21.812  1.00 15.92 ? 74  ASP B C   1 
ATOM   1428 O O   . ASP B 1 74  ? 12.105  12.375 22.414  1.00 17.00 ? 74  ASP B O   1 
ATOM   1429 C CB  . ASP B 1 74  ? 11.207  15.094 23.060  1.00 19.24 ? 74  ASP B CB  1 
ATOM   1430 C CG  . ASP B 1 74  ? 10.462  16.440 23.162  1.00 26.86 ? 74  ASP B CG  1 
ATOM   1431 O OD1 . ASP B 1 74  ? 9.615   16.799 22.263  1.00 27.28 ? 74  ASP B OD1 1 
ATOM   1432 O OD2 . ASP B 1 74  ? 10.755  17.169 24.129  1.00 35.05 ? 74  ASP B OD2 1 
ATOM   1433 N N   . THR B 1 75  ? 10.562  12.142 20.811  1.00 15.60 ? 75  THR B N   1 
ATOM   1434 C CA  . THR B 1 75  ? 11.078  10.844 20.343  1.00 16.13 ? 75  THR B CA  1 
ATOM   1435 C C   . THR B 1 75  ? 12.427  10.969 19.660  1.00 16.43 ? 75  THR B C   1 
ATOM   1436 O O   . THR B 1 75  ? 13.229  10.020 19.775  1.00 14.84 ? 75  THR B O   1 
ATOM   1437 C CB  . THR B 1 75  ? 10.081  10.208 19.408  1.00 15.54 ? 75  THR B CB  1 
ATOM   1438 O OG1 . THR B 1 75  ? 9.863   11.062 18.288  1.00 16.06 ? 75  THR B OG1 1 
ATOM   1439 C CG2 . THR B 1 75  ? 8.760   9.918  20.102  1.00 17.16 ? 75  THR B CG2 1 
ATOM   1440 N N   . LYS B 1 76  ? 12.670  12.043 18.939  1.00 17.07 ? 76  LYS B N   1 
ATOM   1441 C CA  . LYS B 1 76  ? 13.943  12.134 18.209  1.00 17.53 ? 76  LYS B CA  1 
ATOM   1442 C C   . LYS B 1 76  ? 15.116  12.070 19.197  1.00 15.81 ? 76  LYS B C   1 
ATOM   1443 O O   . LYS B 1 76  ? 16.066  11.304 18.938  1.00 17.08 ? 76  LYS B O   1 
ATOM   1444 C CB  . LYS B 1 76  ? 14.007  13.412 17.367  1.00 19.30 ? 76  LYS B CB  1 
ATOM   1445 C CG  . LYS B 1 76  ? 15.195  13.442 16.432  1.00 22.46 ? 76  LYS B CG  1 
ATOM   1446 C CD  . LYS B 1 76  ? 15.162  14.630 15.517  1.00 27.85 ? 76  LYS B CD  1 
ATOM   1447 C CE  . LYS B 1 76  ? 16.294  14.695 14.509  1.00 36.37 ? 76  LYS B CE  1 
ATOM   1448 N NZ  . LYS B 1 76  ? 16.151  15.908 13.658  1.00 39.59 ? 76  LYS B NZ  1 
ATOM   1449 N N   . SER B 1 77  ? 15.099  12.807 20.300  1.00 19.76 ? 77  SER B N   1 
ATOM   1450 C CA  . SER B 1 77  ? 16.190  12.771 21.305  1.00 19.04 ? 77  SER B CA  1 
ATOM   1451 C C   . SER B 1 77  ? 16.322  11.400 21.954  1.00 19.11 ? 77  SER B C   1 
ATOM   1452 O O   . SER B 1 77  ? 17.441  10.952 22.246  1.00 21.13 ? 77  SER B O   1 
ATOM   1453 C CB  . SER B 1 77  ? 15.993  13.845 22.340  1.00 23.21 ? 77  SER B CB  1 
ATOM   1454 O OG  . SER B 1 77  ? 15.973  15.089 21.654  1.00 28.05 ? 77  SER B OG  1 
ATOM   1455 N N   . TYR B 1 78  ? 15.205  10.695 22.102  1.00 17.30 ? 78  TYR B N   1 
ATOM   1456 C CA  . TYR B 1 78  ? 15.256  9.354  22.705  1.00 17.23 ? 78  TYR B CA  1 
ATOM   1457 C C   . TYR B 1 78  ? 16.050  8.432  21.774  1.00 17.43 ? 78  TYR B C   1 
ATOM   1458 O O   . TYR B 1 78  ? 16.919  7.706  22.294  1.00 18.91 ? 78  TYR B O   1 
ATOM   1459 C CB  . TYR B 1 78  ? 13.816  8.885  22.944  1.00 17.20 ? 78  TYR B CB  1 
ATOM   1460 C CG  . TYR B 1 78  ? 13.732  7.470  23.430  1.00 18.05 ? 78  TYR B CG  1 
ATOM   1461 C CD1 . TYR B 1 78  ? 14.003  7.199  24.756  1.00 17.23 ? 78  TYR B CD1 1 
ATOM   1462 C CD2 . TYR B 1 78  ? 13.403  6.405  22.603  1.00 15.72 ? 78  TYR B CD2 1 
ATOM   1463 C CE1 . TYR B 1 78  ? 13.948  5.926  25.257  1.00 18.55 ? 78  TYR B CE1 1 
ATOM   1464 C CE2 . TYR B 1 78  ? 13.393  5.119  23.074  1.00 17.44 ? 78  TYR B CE2 1 
ATOM   1465 C CZ  . TYR B 1 78  ? 13.695  4.872  24.403  1.00 19.92 ? 78  TYR B CZ  1 
ATOM   1466 O OH  . TYR B 1 78  ? 13.628  3.613  24.923  1.00 20.13 ? 78  TYR B OH  1 
ATOM   1467 N N   . TRP B 1 79  ? 15.696  8.362  20.490  1.00 14.69 ? 79  TRP B N   1 
ATOM   1468 C CA  . TRP B 1 79  ? 16.374  7.478  19.528  1.00 15.01 ? 79  TRP B CA  1 
ATOM   1469 C C   . TRP B 1 79  ? 17.846  7.900  19.388  1.00 19.03 ? 79  TRP B C   1 
ATOM   1470 O O   . TRP B 1 79  ? 18.710  6.995  19.375  1.00 21.03 ? 79  TRP B O   1 
ATOM   1471 C CB  . TRP B 1 79  ? 15.642  7.413  18.216  1.00 15.59 ? 79  TRP B CB  1 
ATOM   1472 C CG  . TRP B 1 79  ? 14.303  6.760  18.312  1.00 15.27 ? 79  TRP B CG  1 
ATOM   1473 C CD1 . TRP B 1 79  ? 13.113  7.359  18.071  1.00 14.58 ? 79  TRP B CD1 1 
ATOM   1474 C CD2 . TRP B 1 79  ? 13.995  5.422  18.736  1.00 15.78 ? 79  TRP B CD2 1 
ATOM   1475 N NE1 . TRP B 1 79  ? 12.081  6.492  18.297  1.00 14.33 ? 79  TRP B NE1 1 
ATOM   1476 C CE2 . TRP B 1 79  ? 12.614  5.278  18.682  1.00 15.19 ? 79  TRP B CE2 1 
ATOM   1477 C CE3 . TRP B 1 79  ? 14.778  4.334  19.105  1.00 16.73 ? 79  TRP B CE3 1 
ATOM   1478 C CZ2 . TRP B 1 79  ? 11.983  4.105  19.090  1.00 15.97 ? 79  TRP B CZ2 1 
ATOM   1479 C CZ3 . TRP B 1 79  ? 14.164  3.156  19.464  1.00 18.16 ? 79  TRP B CZ3 1 
ATOM   1480 C CH2 . TRP B 1 79  ? 12.763  3.057  19.465  1.00 17.08 ? 79  TRP B CH2 1 
ATOM   1481 N N   . LYS B 1 80  ? 18.111  9.207  19.366  1.00 21.33 ? 80  LYS B N   1 
ATOM   1482 C CA  . LYS B 1 80  ? 19.507  9.697  19.246  1.00 24.81 ? 80  LYS B CA  1 
ATOM   1483 C C   . LYS B 1 80  ? 20.290  9.153  20.432  1.00 23.38 ? 80  LYS B C   1 
ATOM   1484 O O   . LYS B 1 80  ? 21.430  8.711  20.209  1.00 25.26 ? 80  LYS B O   1 
ATOM   1485 C CB  . LYS B 1 80  ? 19.498  11.208 19.038  1.00 28.35 ? 80  LYS B CB  1 
ATOM   1486 C CG  . LYS B 1 80  ? 19.148  11.579 17.595  1.00 32.19 ? 80  LYS B CG  1 
ATOM   1487 C CD  . LYS B 1 80  ? 19.026  13.075 17.338  1.00 40.47 ? 80  LYS B CD  1 
ATOM   1488 C CE  . LYS B 1 80  ? 20.328  13.825 17.537  1.00 45.47 ? 80  LYS B CE  1 
ATOM   1489 N NZ  . LYS B 1 80  ? 20.196  15.228 17.063  1.00 52.21 ? 80  LYS B NZ  1 
ATOM   1490 N N   . ALA B 1 81  ? 19.741  9.137  21.636  1.00 23.72 ? 81  ALA B N   1 
ATOM   1491 C CA  . ALA B 1 81  ? 20.478  8.674  22.836  1.00 24.81 ? 81  ALA B CA  1 
ATOM   1492 C C   . ALA B 1 81  ? 20.765  7.169  22.746  1.00 29.28 ? 81  ALA B C   1 
ATOM   1493 O O   . ALA B 1 81  ? 21.732  6.706  23.410  1.00 33.50 ? 81  ALA B O   1 
ATOM   1494 C CB  . ALA B 1 81  ? 19.799  9.070  24.121  1.00 27.41 ? 81  ALA B CB  1 
ATOM   1495 N N   . LEU B 1 82  ? 20.016  6.414  21.958  1.00 25.44 ? 82  LEU B N   1 
ATOM   1496 C CA  . LEU B 1 82  ? 20.228  4.974  21.762  1.00 28.27 ? 82  LEU B CA  1 
ATOM   1497 C C   . LEU B 1 82  ? 21.089  4.724  20.523  1.00 26.15 ? 82  LEU B C   1 
ATOM   1498 O O   . LEU B 1 82  ? 21.304  3.558  20.201  1.00 30.75 ? 82  LEU B O   1 
ATOM   1499 C CB  . LEU B 1 82  ? 18.860  4.283  21.642  1.00 27.63 ? 82  LEU B CB  1 
ATOM   1500 C CG  . LEU B 1 82  ? 18.012  4.297  22.908  1.00 31.25 ? 82  LEU B CG  1 
ATOM   1501 C CD1 . LEU B 1 82  ? 16.638  3.742  22.577  1.00 32.41 ? 82  LEU B CD1 1 
ATOM   1502 C CD2 . LEU B 1 82  ? 18.657  3.477  23.996  1.00 34.09 ? 82  LEU B CD2 1 
ATOM   1503 N N   . GLY B 1 83  ? 21.552  5.763  19.826  1.00 27.26 ? 83  GLY B N   1 
ATOM   1504 C CA  . GLY B 1 83  ? 22.326  5.634  18.576  1.00 27.37 ? 83  GLY B CA  1 
ATOM   1505 C C   . GLY B 1 83  ? 21.531  5.107  17.390  1.00 29.07 ? 83  GLY B C   1 
ATOM   1506 O O   . GLY B 1 83  ? 22.072  4.440  16.480  1.00 27.56 ? 83  GLY B O   1 
ATOM   1507 N N   . ILE B 1 84  ? 20.230  5.399  17.322  1.00 25.61 ? 84  ILE B N   1 
ATOM   1508 C CA  . ILE B 1 84  ? 19.361  4.917  16.247  1.00 23.24 ? 84  ILE B CA  1 
ATOM   1509 C C   . ILE B 1 84  ? 18.791  6.122  15.507  1.00 32.41 ? 84  ILE B C   1 
ATOM   1510 O O   . ILE B 1 84  ? 18.341  7.082  16.203  1.00 28.53 ? 84  ILE B O   1 
ATOM   1511 C CB  . ILE B 1 84  ? 18.248  4.047  16.876  1.00 26.34 ? 84  ILE B CB  1 
ATOM   1512 C CG1 . ILE B 1 84  ? 18.850  2.786  17.506  1.00 23.60 ? 84  ILE B CG1 1 
ATOM   1513 C CG2 . ILE B 1 84  ? 17.218  3.723  15.834  1.00 28.02 ? 84  ILE B CG2 1 
ATOM   1514 C CD1 . ILE B 1 84  ? 17.900  2.045  18.425  1.00 23.95 ? 84  ILE B CD1 1 
ATOM   1515 N N   . SER B 1 85  ? 18.913  6.112  14.188  1.00 27.73 ? 85  SER B N   1 
ATOM   1516 C CA  . SER B 1 85  ? 18.452  7.191  13.291  1.00 28.71 ? 85  SER B CA  1 
ATOM   1517 C C   . SER B 1 85  ? 16.932  7.121  13.257  1.00 23.99 ? 85  SER B C   1 
ATOM   1518 O O   . SER B 1 85  ? 16.334  6.122  12.805  1.00 26.17 ? 85  SER B O   1 
ATOM   1519 C CB  . SER B 1 85  ? 19.044  7.078  11.876  1.00 28.69 ? 85  SER B CB  1 
ATOM   1520 O OG  . SER B 1 85  ? 18.839  8.318  11.249  1.00 37.68 ? 85  SER B OG  1 
ATOM   1521 N N   . PRO B 1 86  ? 16.211  8.140  13.763  1.00 22.06 ? 86  PRO B N   1 
ATOM   1522 C CA  . PRO B 1 86  ? 14.758  8.129  13.649  1.00 21.48 ? 86  PRO B CA  1 
ATOM   1523 C C   . PRO B 1 86  ? 14.154  9.022  12.579  1.00 21.55 ? 86  PRO B C   1 
ATOM   1524 O O   . PRO B 1 86  ? 14.820  9.886  12.013  1.00 23.27 ? 86  PRO B O   1 
ATOM   1525 C CB  . PRO B 1 86  ? 14.353  8.725  14.986  1.00 24.25 ? 86  PRO B CB  1 
ATOM   1526 C CG  . PRO B 1 86  ? 15.392  9.797  15.178  1.00 22.78 ? 86  PRO B CG  1 
ATOM   1527 C CD  . PRO B 1 86  ? 16.685  9.300  14.513  1.00 22.55 ? 86  PRO B CD  1 
ATOM   1528 N N   . PHE B 1 87  ? 12.902  8.774  12.289  1.00 17.18 ? 87  PHE B N   1 
ATOM   1529 C CA  . PHE B 1 87  ? 12.174  9.468  11.224  1.00 15.82 ? 87  PHE B CA  1 
ATOM   1530 C C   . PHE B 1 87  ? 11.627  10.780 11.802  1.00 17.05 ? 87  PHE B C   1 
ATOM   1531 O O   . PHE B 1 87  ? 11.727  11.862 11.176  1.00 16.96 ? 87  PHE B O   1 
ATOM   1532 C CB  . PHE B 1 87  ? 11.026  8.638  10.681  1.00 17.64 ? 87  PHE B CB  1 
ATOM   1533 C CG  . PHE B 1 87  ? 10.263  9.339  9.618   1.00 16.82 ? 87  PHE B CG  1 
ATOM   1534 C CD1 . PHE B 1 87  ? 10.828  9.585  8.371   1.00 19.46 ? 87  PHE B CD1 1 
ATOM   1535 C CD2 . PHE B 1 87  ? 8.974   9.751  9.834   1.00 17.88 ? 87  PHE B CD2 1 
ATOM   1536 C CE1 . PHE B 1 87  ? 10.104  10.234 7.394   1.00 17.27 ? 87  PHE B CE1 1 
ATOM   1537 C CE2 . PHE B 1 87  ? 8.241   10.377 8.851   1.00 18.65 ? 87  PHE B CE2 1 
ATOM   1538 C CZ  . PHE B 1 87  ? 8.817   10.639 7.621   1.00 18.05 ? 87  PHE B CZ  1 
ATOM   1539 N N   . HIS B 1 88  ? 10.851  10.714 12.865  1.00 16.30 ? 88  HIS B N   1 
ATOM   1540 C CA  . HIS B 1 88  ? 10.019  11.844 13.321  1.00 14.59 ? 88  HIS B CA  1 
ATOM   1541 C C   . HIS B 1 88  ? 10.822  12.834 14.149  1.00 15.26 ? 88  HIS B C   1 
ATOM   1542 O O   . HIS B 1 88  ? 11.749  12.475 14.873  1.00 17.07 ? 88  HIS B O   1 
ATOM   1543 C CB  . HIS B 1 88  ? 8.832   11.340 14.165  1.00 15.10 ? 88  HIS B CB  1 
ATOM   1544 C CG  . HIS B 1 88  ? 7.961   10.373 13.431  1.00 14.56 ? 88  HIS B CG  1 
ATOM   1545 N ND1 . HIS B 1 88  ? 8.165   8.982  13.470  1.00 16.54 ? 88  HIS B ND1 1 
ATOM   1546 C CD2 . HIS B 1 88  ? 6.914   10.581 12.613  1.00 17.06 ? 88  HIS B CD2 1 
ATOM   1547 C CE1 . HIS B 1 88  ? 7.246   8.425  12.706  1.00 15.87 ? 88  HIS B CE1 1 
ATOM   1548 N NE2 . HIS B 1 88  ? 6.465   9.364  12.157  1.00 18.71 ? 88  HIS B NE2 1 
ATOM   1549 N N   . GLU B 1 89  ? 10.400  14.099 14.135  1.00 15.12 ? 89  GLU B N   1 
ATOM   1550 C CA  . GLU B 1 89  ? 10.961  15.108 15.067  1.00 17.25 ? 89  GLU B CA  1 
ATOM   1551 C C   . GLU B 1 89  ? 10.423  14.843 16.466  1.00 18.32 ? 89  GLU B C   1 
ATOM   1552 O O   . GLU B 1 89  ? 11.173  14.989 17.447  1.00 20.44 ? 89  GLU B O   1 
ATOM   1553 C CB  . GLU B 1 89  ? 10.567  16.506 14.626  1.00 18.27 ? 89  GLU B CB  1 
ATOM   1554 C CG  . GLU B 1 89  ? 11.242  16.885 13.363  1.00 19.78 ? 89  GLU B CG  1 
ATOM   1555 C CD  . GLU B 1 89  ? 12.737  17.043 13.540  1.00 21.98 ? 89  GLU B CD  1 
ATOM   1556 O OE1 . GLU B 1 89  ? 13.112  17.828 14.411  1.00 27.85 ? 89  GLU B OE1 1 
ATOM   1557 O OE2 . GLU B 1 89  ? 13.477  16.336 12.902  1.00 24.71 ? 89  GLU B OE2 1 
ATOM   1558 N N   . HIS B 1 90  ? 9.167   14.474 16.557  1.00 15.92 ? 90  HIS B N   1 
ATOM   1559 C CA  . HIS B 1 90  ? 8.459   14.202 17.816  1.00 17.96 ? 90  HIS B CA  1 
ATOM   1560 C C   . HIS B 1 90  ? 7.187   13.474 17.492  1.00 17.39 ? 90  HIS B C   1 
ATOM   1561 O O   . HIS B 1 90  ? 6.908   13.280 16.297  1.00 20.02 ? 90  HIS B O   1 
ATOM   1562 C CB  . HIS B 1 90  ? 8.215   15.444 18.696  1.00 21.76 ? 90  HIS B CB  1 
ATOM   1563 C CG  . HIS B 1 90  ? 7.859   16.671 17.981  1.00 25.58 ? 90  HIS B CG  1 
ATOM   1564 N ND1 . HIS B 1 90  ? 6.666   16.791 17.332  1.00 34.87 ? 90  HIS B ND1 1 
ATOM   1565 C CD2 . HIS B 1 90  ? 8.546   17.811 17.768  1.00 27.05 ? 90  HIS B CD2 1 
ATOM   1566 C CE1 . HIS B 1 90  ? 6.617   17.993 16.775  1.00 32.68 ? 90  HIS B CE1 1 
ATOM   1567 N NE2 . HIS B 1 90  ? 7.752   18.619 17.032  1.00 34.41 ? 90  HIS B NE2 1 
ATOM   1568 N N   . ALA B 1 91  ? 6.515   12.933 18.483  1.00 15.96 ? 91  ALA B N   1 
ATOM   1569 C CA  . ALA B 1 91  ? 5.152   12.391 18.316  1.00 16.94 ? 91  ALA B CA  1 
ATOM   1570 C C   . ALA B 1 91  ? 4.205   13.362 18.959  1.00 20.11 ? 91  ALA B C   1 
ATOM   1571 O O   . ALA B 1 91  ? 4.588   13.885 20.033  1.00 21.88 ? 91  ALA B O   1 
ATOM   1572 C CB  . ALA B 1 91  ? 5.006   11.042 18.941  1.00 18.18 ? 91  ALA B CB  1 
ATOM   1573 N N   . GLU B 1 92  ? 3.108   13.704 18.314  1.00 20.55 ? 92  GLU B N   1 
ATOM   1574 C CA  . GLU B 1 92  ? 2.199   14.753 18.783  1.00 22.38 ? 92  GLU B CA  1 
ATOM   1575 C C   . GLU B 1 92  ? 0.827   14.115 18.939  1.00 22.72 ? 92  GLU B C   1 
ATOM   1576 O O   . GLU B 1 92  ? 0.355   13.305 18.076  1.00 25.25 ? 92  GLU B O   1 
ATOM   1577 C CB  . GLU B 1 92  ? 2.122   15.933 17.815  1.00 30.53 ? 92  GLU B CB  1 
ATOM   1578 C CG  . GLU B 1 92  ? 3.253   16.938 18.029  1.00 43.95 ? 92  GLU B CG  1 
ATOM   1579 C CD  . GLU B 1 92  ? 3.284   18.075 17.015  1.00 53.87 ? 92  GLU B CD  1 
ATOM   1580 O OE1 . GLU B 1 92  ? 2.787   17.884 15.878  1.00 64.63 ? 92  GLU B OE1 1 
ATOM   1581 O OE2 . GLU B 1 92  ? 3.805   19.154 17.367  1.00 67.08 ? 92  GLU B OE2 1 
ATOM   1582 N N   . VAL B 1 93  ? 0.216   14.309 20.098  1.00 16.10 ? 93  VAL B N   1 
ATOM   1583 C CA  . VAL B 1 93  ? -1.121  13.753 20.351  1.00 15.43 ? 93  VAL B CA  1 
ATOM   1584 C C   . VAL B 1 93  ? -1.983  14.955 20.693  1.00 14.47 ? 93  VAL B C   1 
ATOM   1585 O O   . VAL B 1 93  ? -1.674  15.618 21.688  1.00 17.09 ? 93  VAL B O   1 
ATOM   1586 C CB  . VAL B 1 93  ? -1.069  12.755 21.488  1.00 17.16 ? 93  VAL B CB  1 
ATOM   1587 C CG1 . VAL B 1 93  ? -2.464  12.257 21.808  1.00 18.52 ? 93  VAL B CG1 1 
ATOM   1588 C CG2 . VAL B 1 93  ? -0.110  11.625 21.182  1.00 20.50 ? 93  VAL B CG2 1 
ATOM   1589 N N   . VAL B 1 94  ? -2.980  15.250 19.911  1.00 14.02 ? 94  VAL B N   1 
ATOM   1590 C CA  . VAL B 1 94  ? -3.794  16.483 20.056  1.00 15.81 ? 94  VAL B CA  1 
ATOM   1591 C C   . VAL B 1 94  ? -5.229  16.027 20.230  1.00 15.83 ? 94  VAL B C   1 
ATOM   1592 O O   . VAL B 1 94  ? -5.750  15.237 19.439  1.00 14.58 ? 94  VAL B O   1 
ATOM   1593 C CB  . VAL B 1 94  ? -3.654  17.391 18.831  1.00 17.35 ? 94  VAL B CB  1 
ATOM   1594 C CG1 . VAL B 1 94  ? -4.479  18.652 19.023  1.00 17.48 ? 94  VAL B CG1 1 
ATOM   1595 C CG2 . VAL B 1 94  ? -2.213  17.728 18.583  1.00 19.87 ? 94  VAL B CG2 1 
ATOM   1596 N N   . PHE B 1 95  ? -5.898  16.517 21.270  1.00 15.45 ? 95  PHE B N   1 
ATOM   1597 C CA  . PHE B 1 95  ? -7.221  15.997 21.657  1.00 16.16 ? 95  PHE B CA  1 
ATOM   1598 C C   . PHE B 1 95  ? -7.995  17.058 22.396  1.00 17.86 ? 95  PHE B C   1 
ATOM   1599 O O   . PHE B 1 95  ? -7.363  17.959 22.950  1.00 17.34 ? 95  PHE B O   1 
ATOM   1600 C CB  . PHE B 1 95  ? -7.039  14.727 22.478  1.00 16.61 ? 95  PHE B CB  1 
ATOM   1601 C CG  . PHE B 1 95  ? -6.396  14.934 23.822  1.00 16.08 ? 95  PHE B CG  1 
ATOM   1602 C CD1 . PHE B 1 95  ? -5.034  14.900 23.952  1.00 19.06 ? 95  PHE B CD1 1 
ATOM   1603 C CD2 . PHE B 1 95  ? -7.175  15.098 24.953  1.00 18.63 ? 95  PHE B CD2 1 
ATOM   1604 C CE1 . PHE B 1 95  ? -4.439  15.063 25.202  1.00 19.68 ? 95  PHE B CE1 1 
ATOM   1605 C CE2 . PHE B 1 95  ? -6.587  15.228 26.199  1.00 21.84 ? 95  PHE B CE2 1 
ATOM   1606 C CZ  . PHE B 1 95  ? -5.224  15.268 26.294  1.00 20.94 ? 95  PHE B CZ  1 
ATOM   1607 N N   . THR B 1 96  ? -9.305  16.913 22.420  1.00 20.04 ? 96  THR B N   1 
ATOM   1608 C CA  . THR B 1 96  ? -10.156 17.782 23.290  1.00 21.37 ? 96  THR B CA  1 
ATOM   1609 C C   . THR B 1 96  ? -10.439 17.044 24.602  1.00 22.26 ? 96  THR B C   1 
ATOM   1610 O O   . THR B 1 96  ? -10.781 15.854 24.595  1.00 22.95 ? 96  THR B O   1 
ATOM   1611 C CB  . THR B 1 96  ? -11.461 18.127 22.581  1.00 25.10 ? 96  THR B CB  1 
ATOM   1612 O OG1 . THR B 1 96  ? -11.186 18.930 21.427  1.00 23.75 ? 96  THR B OG1 1 
ATOM   1613 C CG2 . THR B 1 96  ? -12.433 18.854 23.498  1.00 29.58 ? 96  THR B CG2 1 
ATOM   1614 N N   . ALA B 1 97  ? -10.248 17.725 25.742  1.00 21.32 ? 97  ALA B N   1 
ATOM   1615 C CA  . ALA B 1 97  ? -10.667 17.201 27.061  1.00 21.07 ? 97  ALA B CA  1 
ATOM   1616 C C   . ALA B 1 97  ? -12.123 17.606 27.283  1.00 24.54 ? 97  ALA B C   1 
ATOM   1617 O O   . ALA B 1 97  ? -12.438 18.769 27.064  1.00 24.29 ? 97  ALA B O   1 
ATOM   1618 C CB  . ALA B 1 97  ? -9.782  17.761 28.142  1.00 26.43 ? 97  ALA B CB  1 
ATOM   1619 N N   . ASN B 1 98  ? -12.990 16.639 27.520  1.00 27.32 ? 98  ASN B N   1 
ATOM   1620 C CA  . ASN B 1 98  ? -14.430 16.952 27.655  1.00 27.71 ? 98  ASN B CA  1 
ATOM   1621 C C   . ASN B 1 98  ? -14.865 16.446 29.016  1.00 33.41 ? 98  ASN B C   1 
ATOM   1622 O O   . ASN B 1 98  ? -14.620 15.303 29.339  1.00 33.72 ? 98  ASN B O   1 
ATOM   1623 C CB  . ASN B 1 98  ? -15.257 16.490 26.456  1.00 38.99 ? 98  ASN B CB  1 
ATOM   1624 C CG  . ASN B 1 98  ? -16.735 16.606 26.744  1.00 42.37 ? 98  ASN B CG  1 
ATOM   1625 O OD1 . ASN B 1 98  ? -17.317 15.665 27.240  1.00 60.18 ? 98  ASN B OD1 1 
ATOM   1626 N ND2 . ASN B 1 98  ? -17.328 17.762 26.521  1.00 46.30 ? 98  ASN B ND2 1 
ATOM   1627 N N   . ASP B 1 99  ? -15.567 17.315 29.734  1.00 32.62 ? 99  ASP B N   1 
ATOM   1628 C CA  . ASP B 1 99  ? -15.950 17.061 31.141  1.00 32.50 ? 99  ASP B CA  1 
ATOM   1629 C C   . ASP B 1 99  ? -17.043 16.008 31.358  1.00 38.03 ? 99  ASP B C   1 
ATOM   1630 O O   . ASP B 1 99  ? -17.280 15.857 32.517  1.00 59.44 ? 99  ASP B O   1 
ATOM   1631 C CB  . ASP B 1 99  ? -16.397 18.355 31.828  1.00 32.43 ? 99  ASP B CB  1 
ATOM   1632 C CG  . ASP B 1 99  ? -15.269 19.078 32.544  1.00 32.12 ? 99  ASP B CG  1 
ATOM   1633 O OD1 . ASP B 1 99  ? -14.136 18.558 32.526  1.00 37.92 ? 99  ASP B OD1 1 
ATOM   1634 O OD2 . ASP B 1 99  ? -15.533 20.155 33.114  1.00 30.15 ? 99  ASP B OD2 1 
ATOM   1635 N N   . SER B 1 100 ? -17.657 15.409 30.324  1.00 38.90 ? 100 SER B N   1 
ATOM   1636 C CA  . SER B 1 100 ? -18.796 14.455 30.483  1.00 43.70 ? 100 SER B CA  1 
ATOM   1637 C C   . SER B 1 100 ? -18.388 13.511 31.633  1.00 43.58 ? 100 SER B C   1 
ATOM   1638 O O   . SER B 1 100 ? -17.499 12.699 31.399  1.00 51.56 ? 100 SER B O   1 
ATOM   1639 C CB  . SER B 1 100 ? -19.010 13.750 29.187  1.00 52.36 ? 100 SER B CB  1 
ATOM   1640 O OG  . SER B 1 100 ? -17.774 13.403 28.602  1.00 47.62 ? 100 SER B OG  1 
ATOM   1641 N N   . GLY B 1 101 ? -19.059 13.556 32.792  1.00 43.49 ? 101 GLY B N   1 
ATOM   1642 C CA  . GLY B 1 101 ? -18.618 12.774 33.963  1.00 40.26 ? 101 GLY B CA  1 
ATOM   1643 C C   . GLY B 1 101 ? -17.231 12.844 34.598  1.00 41.70 ? 101 GLY B C   1 
ATOM   1644 O O   . GLY B 1 101 ? -16.392 13.580 34.127  1.00 42.32 ? 101 GLY B O   1 
ATOM   1645 N N   . PRO B 1 102 ? -16.912 12.087 35.661  1.00 39.33 ? 102 PRO B N   1 
ATOM   1646 C CA  . PRO B 1 102 ? -15.552 12.060 36.142  1.00 38.01 ? 102 PRO B CA  1 
ATOM   1647 C C   . PRO B 1 102 ? -14.650 11.236 35.204  1.00 45.68 ? 102 PRO B C   1 
ATOM   1648 O O   . PRO B 1 102 ? -15.123 10.225 34.705  1.00 43.55 ? 102 PRO B O   1 
ATOM   1649 C CB  . PRO B 1 102 ? -15.672 11.462 37.549  1.00 42.69 ? 102 PRO B CB  1 
ATOM   1650 C CG  . PRO B 1 102 ? -17.002 10.761 37.583  1.00 39.59 ? 102 PRO B CG  1 
ATOM   1651 C CD  . PRO B 1 102 ? -17.828 11.242 36.414  1.00 39.14 ? 102 PRO B CD  1 
ATOM   1652 N N   . ARG B 1 103 ? -13.442 11.729 34.891  1.00 46.56 ? 103 ARG B N   1 
ATOM   1653 C CA  . ARG B 1 103 ? -12.541 10.920 34.018  1.00 47.34 ? 103 ARG B CA  1 
ATOM   1654 C C   . ARG B 1 103 ? -11.049 11.225 34.202  1.00 45.90 ? 103 ARG B C   1 
ATOM   1655 O O   . ARG B 1 103 ? -10.686 12.316 34.624  1.00 42.35 ? 103 ARG B O   1 
ATOM   1656 C CB  . ARG B 1 103 ? -12.895 10.954 32.529  1.00 55.30 ? 103 ARG B CB  1 
ATOM   1657 C CG  . ARG B 1 103 ? -13.204 12.306 31.932  1.00 59.56 ? 103 ARG B CG  1 
ATOM   1658 C CD  . ARG B 1 103 ? -14.005 12.076 30.668  1.00 64.36 ? 103 ARG B CD  1 
ATOM   1659 N NE  . ARG B 1 103 ? -15.385 11.778 30.980  1.00 71.16 ? 103 ARG B NE  1 
ATOM   1660 C CZ  . ARG B 1 103 ? -15.826 10.597 31.360  1.00 81.35 ? 103 ARG B CZ  1 
ATOM   1661 N NH1 . ARG B 1 103 ? -14.987 9.588  31.479  1.00 82.05 ? 103 ARG B NH1 1 
ATOM   1662 N NH2 . ARG B 1 103 ? -17.104 10.419 31.635  1.00 77.45 ? 103 ARG B NH2 1 
ATOM   1663 N N   . ARG B 1 104 ? -10.249 10.202 33.915  1.00 31.38 ? 104 ARG B N   1 
ATOM   1664 C CA  . ARG B 1 104 ? -8.783  10.228 33.898  1.00 29.05 ? 104 ARG B CA  1 
ATOM   1665 C C   . ARG B 1 104 ? -8.376  9.904  32.458  1.00 25.82 ? 104 ARG B C   1 
ATOM   1666 O O   . ARG B 1 104 ? -8.986  8.996  31.859  1.00 25.31 ? 104 ARG B O   1 
ATOM   1667 C CB  . ARG B 1 104 ? -8.177  9.185  34.830  1.00 32.96 ? 104 ARG B CB  1 
ATOM   1668 C CG  . ARG B 1 104 ? -8.835  9.082  36.199  1.00 50.45 ? 104 ARG B CG  1 
ATOM   1669 C CD  . ARG B 1 104 ? -7.855  8.593  37.260  1.00 60.18 ? 104 ARG B CD  1 
ATOM   1670 N NE  . ARG B 1 104 ? -8.305  8.924  38.610  1.00 69.34 ? 104 ARG B NE  1 
ATOM   1671 C CZ  . ARG B 1 104 ? -8.355  10.155 39.125  1.00 73.72 ? 104 ARG B CZ  1 
ATOM   1672 N NH1 . ARG B 1 104 ? -7.998  11.210 38.407  1.00 75.53 ? 104 ARG B NH1 1 
ATOM   1673 N NH2 . ARG B 1 104 ? -8.783  10.328 40.365  1.00 74.91 ? 104 ARG B NH2 1 
ATOM   1674 N N   . TYR B 1 105 ? -7.425  10.627 31.930  1.00 22.13 ? 105 TYR B N   1 
ATOM   1675 C CA  . TYR B 1 105 ? -6.886  10.400 30.564  1.00 21.10 ? 105 TYR B CA  1 
ATOM   1676 C C   . TYR B 1 105 ? -5.497  9.801  30.708  1.00 21.20 ? 105 TYR B C   1 
ATOM   1677 O O   . TYR B 1 105 ? -4.551  10.409 31.340  1.00 22.06 ? 105 TYR B O   1 
ATOM   1678 C CB  . TYR B 1 105 ? -6.778  11.714 29.791  1.00 22.97 ? 105 TYR B CB  1 
ATOM   1679 C CG  . TYR B 1 105 ? -8.062  12.410 29.483  1.00 25.21 ? 105 TYR B CG  1 
ATOM   1680 C CD1 . TYR B 1 105 ? -8.772  13.136 30.443  1.00 36.64 ? 105 TYR B CD1 1 
ATOM   1681 C CD2 . TYR B 1 105 ? -8.647  12.229 28.254  1.00 33.99 ? 105 TYR B CD2 1 
ATOM   1682 C CE1 . TYR B 1 105 ? -10.013 13.706 30.154  1.00 33.40 ? 105 TYR B CE1 1 
ATOM   1683 C CE2 . TYR B 1 105 ? -9.855  12.818 27.941  1.00 32.27 ? 105 TYR B CE2 1 
ATOM   1684 C CZ  . TYR B 1 105 ? -10.542 13.554 28.877  1.00 31.93 ? 105 TYR B CZ  1 
ATOM   1685 O OH  . TYR B 1 105 ? -11.718 14.061 28.424  1.00 34.44 ? 105 TYR B OH  1 
ATOM   1686 N N   . THR B 1 106 ? -5.285  8.630  30.095  1.00 19.58 ? 106 THR B N   1 
ATOM   1687 C CA  . THR B 1 106 ? -3.968  8.074  29.861  1.00 18.26 ? 106 THR B CA  1 
ATOM   1688 C C   . THR B 1 106 ? -3.680  8.136  28.368  1.00 19.12 ? 106 THR B C   1 
ATOM   1689 O O   . THR B 1 106 ? -4.431  7.579  27.582  1.00 18.81 ? 106 THR B O   1 
ATOM   1690 C CB  . THR B 1 106 ? -3.793  6.644  30.362  1.00 21.64 ? 106 THR B CB  1 
ATOM   1691 O OG1 . THR B 1 106 ? -4.053  6.775  31.774  1.00 25.66 ? 106 THR B OG1 1 
ATOM   1692 C CG2 . THR B 1 106 ? -2.406  6.122  30.133  1.00 23.01 ? 106 THR B CG2 1 
ATOM   1693 N N   . ILE B 1 107 ? -2.635  8.845  28.032  1.00 16.08 ? 107 ILE B N   1 
ATOM   1694 C CA  . ILE B 1 107 ? -2.110  8.906  26.650  1.00 15.12 ? 107 ILE B CA  1 
ATOM   1695 C C   . ILE B 1 107 ? -0.964  7.930  26.606  1.00 15.42 ? 107 ILE B C   1 
ATOM   1696 O O   . ILE B 1 107 ? 0.066   8.150  27.253  1.00 17.24 ? 107 ILE B O   1 
ATOM   1697 C CB  . ILE B 1 107 ? -1.639  10.322 26.276  1.00 15.42 ? 107 ILE B CB  1 
ATOM   1698 C CG1 . ILE B 1 107 ? -2.758  11.368 26.413  1.00 19.50 ? 107 ILE B CG1 1 
ATOM   1699 C CG2 . ILE B 1 107 ? -0.987  10.288 24.937  1.00 16.51 ? 107 ILE B CG2 1 
ATOM   1700 C CD1 . ILE B 1 107 ? -3.987  11.085 25.661  1.00 21.60 ? 107 ILE B CD1 1 
ATOM   1701 N N   . ALA B 1 108 ? -1.063  6.867  25.806  1.00 15.28 ? 108 ALA B N   1 
ATOM   1702 C CA  . ALA B 1 108 ? -0.014  5.874  25.662  1.00 15.54 ? 108 ALA B CA  1 
ATOM   1703 C C   . ALA B 1 108 ? 0.576   5.966  24.260  1.00 15.29 ? 108 ALA B C   1 
ATOM   1704 O O   . ALA B 1 108 ? -0.170  6.174  23.263  1.00 16.04 ? 108 ALA B O   1 
ATOM   1705 C CB  . ALA B 1 108 ? -0.502  4.476  25.960  1.00 15.83 ? 108 ALA B CB  1 
ATOM   1706 N N   . ALA B 1 109 ? 1.846   5.719  24.149  1.00 14.81 ? 109 ALA B N   1 
ATOM   1707 C CA  . ALA B 1 109 ? 2.582   5.724  22.882  1.00 14.34 ? 109 ALA B CA  1 
ATOM   1708 C C   . ALA B 1 109 ? 3.588   4.613  22.849  1.00 15.36 ? 109 ALA B C   1 
ATOM   1709 O O   . ALA B 1 109 ? 4.221   4.307  23.851  1.00 16.00 ? 109 ALA B O   1 
ATOM   1710 C CB  . ALA B 1 109 ? 3.213   7.052  22.647  1.00 16.31 ? 109 ALA B CB  1 
ATOM   1711 N N   . LEU B 1 110 ? 3.665   3.939  21.717  1.00 13.08 ? 110 LEU B N   1 
ATOM   1712 C CA  . LEU B 1 110 ? 4.550   2.824  21.452  1.00 13.61 ? 110 LEU B CA  1 
ATOM   1713 C C   . LEU B 1 110 ? 5.431   3.261  20.303  1.00 14.10 ? 110 LEU B C   1 
ATOM   1714 O O   . LEU B 1 110 ? 4.912   3.545  19.182  1.00 14.83 ? 110 LEU B O   1 
ATOM   1715 C CB  . LEU B 1 110 ? 3.702   1.606  21.055  1.00 14.02 ? 110 LEU B CB  1 
ATOM   1716 C CG  . LEU B 1 110 ? 4.473   0.370  20.690  1.00 13.71 ? 110 LEU B CG  1 
ATOM   1717 C CD1 . LEU B 1 110 ? 5.360   -0.142 21.791  1.00 14.46 ? 110 LEU B CD1 1 
ATOM   1718 C CD2 . LEU B 1 110 ? 3.506   -0.742 20.251  1.00 16.46 ? 110 LEU B CD2 1 
ATOM   1719 N N   . LEU B 1 111 ? 6.716   3.352  20.576  1.00 13.36 ? 111 LEU B N   1 
ATOM   1720 C CA  . LEU B 1 111 ? 7.692   3.989  19.677  1.00 12.68 ? 111 LEU B CA  1 
ATOM   1721 C C   . LEU B 1 111 ? 8.544   3.000  18.920  1.00 13.27 ? 111 LEU B C   1 
ATOM   1722 O O   . LEU B 1 111 ? 9.168   2.111  19.519  1.00 13.49 ? 111 LEU B O   1 
ATOM   1723 C CB  . LEU B 1 111 ? 8.604   4.891  20.497  1.00 12.33 ? 111 LEU B CB  1 
ATOM   1724 C CG  . LEU B 1 111 ? 7.975   5.923  21.385  1.00 14.36 ? 111 LEU B CG  1 
ATOM   1725 C CD1 . LEU B 1 111 ? 9.115   6.747  21.988  1.00 14.76 ? 111 LEU B CD1 1 
ATOM   1726 C CD2 . LEU B 1 111 ? 6.971   6.807  20.631  1.00 14.40 ? 111 LEU B CD2 1 
ATOM   1727 N N   . SER B 1 112 ? 8.711   3.260  17.624  1.00 13.16 ? 112 SER B N   1 
ATOM   1728 C CA  . SER B 1 112 ? 9.704   2.651  16.755  1.00 13.35 ? 112 SER B CA  1 
ATOM   1729 C C   . SER B 1 112 ? 10.455  3.752  15.992  1.00 13.80 ? 112 SER B C   1 
ATOM   1730 O O   . SER B 1 112 ? 9.987   4.876  15.950  1.00 13.45 ? 112 SER B O   1 
ATOM   1731 C CB  . SER B 1 112 ? 9.133   1.681  15.758  1.00 14.30 ? 112 SER B CB  1 
ATOM   1732 O OG  . SER B 1 112 ? 8.374   0.658  16.459  1.00 16.45 ? 112 SER B OG  1 
ATOM   1733 N N   . PRO B 1 113 ? 11.617  3.441  15.426  1.00 14.70 ? 113 PRO B N   1 
ATOM   1734 C CA  . PRO B 1 113 ? 12.368  4.520  14.772  1.00 14.78 ? 113 PRO B CA  1 
ATOM   1735 C C   . PRO B 1 113 ? 11.586  5.221  13.661  1.00 14.51 ? 113 PRO B C   1 
ATOM   1736 O O   . PRO B 1 113 ? 11.708  6.473  13.542  1.00 14.35 ? 113 PRO B O   1 
ATOM   1737 C CB  . PRO B 1 113 ? 13.616  3.812  14.318  1.00 15.23 ? 113 PRO B CB  1 
ATOM   1738 C CG  . PRO B 1 113 ? 13.815  2.744  15.355  1.00 16.35 ? 113 PRO B CG  1 
ATOM   1739 C CD  . PRO B 1 113 ? 12.406  2.216  15.561  1.00 15.74 ? 113 PRO B CD  1 
ATOM   1740 N N   . TYR B 1 114 ? 10.814  4.472  12.849  1.00 13.56 ? 114 TYR B N   1 
ATOM   1741 C CA  . TYR B 1 114 ? 10.088  5.049  11.700  1.00 13.83 ? 114 TYR B CA  1 
ATOM   1742 C C   . TYR B 1 114 ? 8.600   4.961  11.890  1.00 14.53 ? 114 TYR B C   1 
ATOM   1743 O O   . TYR B 1 114 ? 7.861   5.267  10.951  1.00 16.03 ? 114 TYR B O   1 
ATOM   1744 C CB  . TYR B 1 114 ? 10.515  4.411  10.379  1.00 15.09 ? 114 TYR B CB  1 
ATOM   1745 C CG  . TYR B 1 114 ? 11.779  4.998  9.818   1.00 16.46 ? 114 TYR B CG  1 
ATOM   1746 C CD1 . TYR B 1 114 ? 12.989  4.804  10.451  1.00 24.21 ? 114 TYR B CD1 1 
ATOM   1747 C CD2 . TYR B 1 114 ? 11.709  5.768  8.692   1.00 16.37 ? 114 TYR B CD2 1 
ATOM   1748 C CE1 . TYR B 1 114 ? 14.155  5.364  9.960   1.00 28.34 ? 114 TYR B CE1 1 
ATOM   1749 C CE2 . TYR B 1 114 ? 12.878  6.371  8.206   1.00 19.14 ? 114 TYR B CE2 1 
ATOM   1750 C CZ  . TYR B 1 114 ? 14.085  6.102  8.808   1.00 30.39 ? 114 TYR B CZ  1 
ATOM   1751 O OH  . TYR B 1 114 ? 15.271  6.611  8.339   1.00 39.30 ? 114 TYR B OH  1 
ATOM   1752 N N   . SER B 1 115 ? 8.108   4.717  13.104  1.00 14.17 ? 115 SER B N   1 
ATOM   1753 C CA  A SER B 1 115 ? 6.650   4.505  13.310  0.50 14.97 ? 115 SER B CA  1 
ATOM   1754 C CA  B SER B 1 115 ? 6.658   4.513  13.308  0.50 14.83 ? 115 SER B CA  1 
ATOM   1755 C C   . SER B 1 115 ? 6.294   4.804  14.761  1.00 14.23 ? 115 SER B C   1 
ATOM   1756 O O   . SER B 1 115 ? 7.147   4.607  15.631  1.00 15.09 ? 115 SER B O   1 
ATOM   1757 C CB  A SER B 1 115 ? 6.190   3.081  12.968  0.50 16.62 ? 115 SER B CB  1 
ATOM   1758 C CB  B SER B 1 115 ? 6.275   3.098  12.961  0.50 16.45 ? 115 SER B CB  1 
ATOM   1759 O OG  A SER B 1 115 ? 6.491   2.144  14.006  0.50 19.76 ? 115 SER B OG  1 
ATOM   1760 O OG  B SER B 1 115 ? 4.889   2.918  13.105  0.50 17.31 ? 115 SER B OG  1 
ATOM   1761 N N   . TYR B 1 116 ? 5.081   5.208  15.002  1.00 16.09 ? 116 TYR B N   1 
ATOM   1762 C CA  . TYR B 1 116 ? 4.559   5.131  16.369  1.00 16.51 ? 116 TYR B CA  1 
ATOM   1763 C C   . TYR B 1 116 ? 3.084   4.837  16.324  1.00 16.92 ? 116 TYR B C   1 
ATOM   1764 O O   . TYR B 1 116 ? 2.395   5.138  15.372  1.00 16.17 ? 116 TYR B O   1 
ATOM   1765 C CB  . TYR B 1 116 ? 4.907   6.373  17.179  1.00 17.82 ? 116 TYR B CB  1 
ATOM   1766 C CG  . TYR B 1 116 ? 4.326   7.668  16.694  1.00 18.57 ? 116 TYR B CG  1 
ATOM   1767 C CD1 . TYR B 1 116 ? 5.073   8.484  15.872  1.00 22.84 ? 116 TYR B CD1 1 
ATOM   1768 C CD2 . TYR B 1 116 ? 3.073   8.083  17.069  1.00 17.69 ? 116 TYR B CD2 1 
ATOM   1769 C CE1 . TYR B 1 116 ? 4.591   9.697  15.456  1.00 20.71 ? 116 TYR B CE1 1 
ATOM   1770 C CE2 . TYR B 1 116 ? 2.565   9.292  16.646  1.00 21.69 ? 116 TYR B CE2 1 
ATOM   1771 C CZ  . TYR B 1 116 ? 3.333   10.094 15.830  1.00 22.13 ? 116 TYR B CZ  1 
ATOM   1772 O OH  . TYR B 1 116 ? 2.903   11.308 15.421  1.00 28.12 ? 116 TYR B OH  1 
ATOM   1773 N N   A SER B 1 117 ? 2.609   4.271  17.424  0.50 15.41 ? 117 SER B N   1 
ATOM   1774 N N   B SER B 1 117 ? 2.614   4.253  17.419  0.50 14.59 ? 117 SER B N   1 
ATOM   1775 C CA  A SER B 1 117 ? 1.202   3.958  17.728  0.50 16.18 ? 117 SER B CA  1 
ATOM   1776 C CA  B SER B 1 117 ? 1.201   3.981  17.735  0.50 14.73 ? 117 SER B CA  1 
ATOM   1777 C C   A SER B 1 117 ? 0.822   4.777  18.966  0.50 14.04 ? 117 SER B C   1 
ATOM   1778 C C   B SER B 1 117 ? 0.829   4.801  18.968  0.50 13.33 ? 117 SER B C   1 
ATOM   1779 O O   A SER B 1 117 ? 1.698   4.918  19.845  0.50 14.88 ? 117 SER B O   1 
ATOM   1780 O O   B SER B 1 117 ? 1.701   4.945  19.848  0.50 14.23 ? 117 SER B O   1 
ATOM   1781 C CB  A SER B 1 117 ? 1.046   2.471  17.929  0.50 18.15 ? 117 SER B CB  1 
ATOM   1782 C CB  B SER B 1 117 ? 0.963   2.516  17.934  0.50 15.46 ? 117 SER B CB  1 
ATOM   1783 O OG  A SER B 1 117 ? -0.157  2.112  18.573  0.50 22.52 ? 117 SER B OG  1 
ATOM   1784 O OG  B SER B 1 117 ? 1.184   1.850  16.687  0.50 16.34 ? 117 SER B OG  1 
ATOM   1785 N N   . THR B 1 118 ? -0.359  5.366  19.025  1.00 13.19 ? 118 THR B N   1 
ATOM   1786 C CA  . THR B 1 118 ? -0.829  6.042  20.228  1.00 14.07 ? 118 THR B CA  1 
ATOM   1787 C C   . THR B 1 118 ? -2.255  5.691  20.476  1.00 14.93 ? 118 THR B C   1 
ATOM   1788 O O   . THR B 1 118 ? -3.016  5.504  19.492  1.00 16.39 ? 118 THR B O   1 
ATOM   1789 C CB  . THR B 1 118 ? -0.533  7.534  20.154  1.00 15.07 ? 118 THR B CB  1 
ATOM   1790 O OG1 . THR B 1 118 ? -0.804  8.114  21.418  1.00 16.26 ? 118 THR B OG1 1 
ATOM   1791 C CG2 . THR B 1 118 ? -1.342  8.200  19.093  1.00 15.25 ? 118 THR B CG2 1 
ATOM   1792 N N   . THR B 1 119 ? -2.637  5.597  21.733  1.00 14.33 ? 119 THR B N   1 
ATOM   1793 C CA  . THR B 1 119 ? -4.034  5.383  22.119  1.00 14.67 ? 119 THR B CA  1 
ATOM   1794 C C   . THR B 1 119 ? -4.350  6.214  23.343  1.00 14.54 ? 119 THR B C   1 
ATOM   1795 O O   . THR B 1 119 ? -3.381  6.662  23.996  1.00 16.57 ? 119 THR B O   1 
ATOM   1796 C CB  . THR B 1 119 ? -4.309  3.880  22.321  1.00 15.92 ? 119 THR B CB  1 
ATOM   1797 O OG1 . THR B 1 119 ? -5.731  3.752  22.249  1.00 16.86 ? 119 THR B OG1 1 
ATOM   1798 C CG2 . THR B 1 119 ? -3.717  3.350  23.594  1.00 16.58 ? 119 THR B CG2 1 
ATOM   1799 N N   . ALA B 1 120 ? -5.623  6.360  23.577  1.00 15.75 ? 120 ALA B N   1 
ATOM   1800 C CA  . ALA B 1 120 ? -6.123  7.058  24.788  1.00 15.59 ? 120 ALA B CA  1 
ATOM   1801 C C   . ALA B 1 120 ? -6.903  6.045  25.595  1.00 16.79 ? 120 ALA B C   1 
ATOM   1802 O O   . ALA B 1 120 ? -7.691  5.285  25.003  1.00 18.26 ? 120 ALA B O   1 
ATOM   1803 C CB  . ALA B 1 120 ? -6.943  8.218  24.409  1.00 17.12 ? 120 ALA B CB  1 
ATOM   1804 N N   . VAL B 1 121 ? -6.634  5.995  26.883  1.00 18.37 ? 121 VAL B N   1 
ATOM   1805 C CA  . VAL B 1 121 ? -7.427  5.164  27.820  1.00 19.16 ? 121 VAL B CA  1 
ATOM   1806 C C   . VAL B 1 121 ? -8.146  6.161  28.721  1.00 20.35 ? 121 VAL B C   1 
ATOM   1807 O O   . VAL B 1 121 ? -7.444  6.894  29.471  1.00 21.47 ? 121 VAL B O   1 
ATOM   1808 C CB  . VAL B 1 121 ? -6.557  4.178  28.585  1.00 20.37 ? 121 VAL B CB  1 
ATOM   1809 C CG1 . VAL B 1 121 ? -7.444  3.215  29.400  1.00 23.49 ? 121 VAL B CG1 1 
ATOM   1810 C CG2 . VAL B 1 121 ? -5.625  3.438  27.630  1.00 22.32 ? 121 VAL B CG2 1 
ATOM   1811 N N   . VAL B 1 122 ? -9.443  6.285  28.572  1.00 20.94 ? 122 VAL B N   1 
ATOM   1812 C CA  . VAL B 1 122 ? -10.238 7.307  29.290  1.00 22.18 ? 122 VAL B CA  1 
ATOM   1813 C C   . VAL B 1 122 ? -11.120 6.551  30.260  1.00 24.09 ? 122 VAL B C   1 
ATOM   1814 O O   . VAL B 1 122 ? -11.983 5.784  29.769  1.00 26.31 ? 122 VAL B O   1 
ATOM   1815 C CB  . VAL B 1 122 ? -11.022 8.195  28.328  1.00 23.23 ? 122 VAL B CB  1 
ATOM   1816 C CG1 . VAL B 1 122 ? -11.809 9.262  29.089  1.00 29.24 ? 122 VAL B CG1 1 
ATOM   1817 C CG2 . VAL B 1 122 ? -10.092 8.833  27.308  1.00 26.10 ? 122 VAL B CG2 1 
ATOM   1818 N N   . THR B 1 123 ? -10.907 6.736  31.577  1.00 25.79 ? 123 THR B N   1 
ATOM   1819 C CA  . THR B 1 123 ? -11.585 5.897  32.617  1.00 29.08 ? 123 THR B CA  1 
ATOM   1820 C C   . THR B 1 123 ? -12.319 6.787  33.619  1.00 36.48 ? 123 THR B C   1 
ATOM   1821 O O   . THR B 1 123 ? -12.067 7.990  33.611  1.00 30.73 ? 123 THR B O   1 
ATOM   1822 C CB  . THR B 1 123 ? -10.580 4.956  33.278  1.00 31.69 ? 123 THR B CB  1 
ATOM   1823 O OG1 . THR B 1 123 ? -9.458  5.685  33.772  1.00 37.30 ? 123 THR B OG1 1 
ATOM   1824 C CG2 . THR B 1 123 ? -10.117 3.879  32.319  1.00 31.26 ? 123 THR B CG2 1 
ATOM   1825 N N   . ASN B 1 124 ? -13.279 6.214  34.345  1.00 43.58 ? 124 ASN B N   1 
ATOM   1826 C CA  . ASN B 1 124 ? -14.069 6.906  35.410  1.00 53.82 ? 124 ASN B CA  1 
ATOM   1827 C C   . ASN B 1 124 ? -13.557 6.426  36.768  1.00 47.30 ? 124 ASN B C   1 
ATOM   1828 O O   . ASN B 1 124 ? -13.348 5.224  36.942  1.00 59.15 ? 124 ASN B O   1 
ATOM   1829 C CB  . ASN B 1 124 ? -15.576 6.685  35.239  1.00 57.94 ? 124 ASN B CB  1 
ATOM   1830 C CG  . ASN B 1 124 ? -16.140 7.404  34.029  1.00 71.67 ? 124 ASN B CG  1 
ATOM   1831 O OD1 . ASN B 1 124 ? -15.415 7.699  33.076  1.00 91.35 ? 124 ASN B OD1 1 
ATOM   1832 N ND2 . ASN B 1 124 ? -17.428 7.712  34.063  1.00 79.33 ? 124 ASN B ND2 1 
HETATM 1833 C C1  . 1W4 C 2 .   ? 1.466   1.277  0.939   0.50 46.85 ? 201 1W4 A C1  1 
HETATM 1834 O O2  . 1W4 C 2 .   ? 2.569   1.547  1.392   0.50 51.92 ? 201 1W4 A O2  1 
HETATM 1835 C C3  . 1W4 C 2 .   ? 0.467   0.461  1.673   0.50 40.93 ? 201 1W4 A C3  1 
HETATM 1836 C C4  . 1W4 C 2 .   ? -0.569  -0.151 0.982   0.50 40.41 ? 201 1W4 A C4  1 
HETATM 1837 C C5  . 1W4 C 2 .   ? -1.505  -0.904 1.654   0.50 43.20 ? 201 1W4 A C5  1 
HETATM 1838 C C6  . 1W4 C 2 .   ? -1.404  -1.020 3.020   0.50 36.87 ? 201 1W4 A C6  1 
HETATM 1839 C C7  . 1W4 C 2 .   ? -0.393  -0.415 3.710   0.50 34.26 ? 201 1W4 A C7  1 
HETATM 1840 C C8  . 1W4 C 2 .   ? 0.538   0.338  3.056   0.50 33.91 ? 201 1W4 A C8  1 
HETATM 1841 N N9  . 1W4 C 2 .   ? -2.569  -1.561 1.042   0.50 44.39 ? 201 1W4 A N9  1 
HETATM 1842 C C10 . 1W4 C 2 .   ? -2.356  -2.398 -0.122  0.50 44.10 ? 201 1W4 A C10 1 
HETATM 1843 C C11 . 1W4 C 2 .   ? -3.909  -1.397 1.566   0.50 43.61 ? 201 1W4 A C11 1 
HETATM 1844 C C12 . 1W4 C 2 .   ? -0.416  -0.628 5.179   0.50 30.81 ? 201 1W4 A C12 1 
HETATM 1845 C C13 . 1W4 C 2 .   ? 0.089   0.235  5.999   0.50 22.10 ? 201 1W4 A C13 1 
HETATM 1846 C C14 . 1W4 C 2 .   ? -0.000  -0.000 7.456   0.50 19.34 ? 201 1W4 A C14 1 
HETATM 1847 C C15 . 1W4 C 2 .   ? -0.214  -1.145 8.088   0.50 18.34 ? 201 1W4 A C15 1 
HETATM 1848 C C16 . 1W4 C 2 .   ? -0.244  -1.212 9.464   0.50 16.45 ? 201 1W4 A C16 1 
HETATM 1849 C C17 . 1W4 C 2 .   ? -0.000  -0.000 10.248  0.50 17.74 ? 201 1W4 A C17 1 
HETATM 1850 C C18 . 1W4 C 2 .   ? 0.264   1.232  9.521   0.50 16.47 ? 201 1W4 A C18 1 
HETATM 1851 C C19 . 1W4 C 2 .   ? 0.266   1.213  8.164   0.50 18.27 ? 201 1W4 A C19 1 
HETATM 1852 C C26 . 1W4 C 2 .   ? -0.507  -2.497 10.186  0.50 17.20 ? 201 1W4 A C26 1 
HETATM 1853 C C27 . 1W4 C 2 .   ? 0.514   2.512  10.247  0.50 17.19 ? 201 1W4 A C27 1 
HETATM 1854 O O28 . 1W4 C 2 .   ? -0.000  -0.000 11.571  0.50 15.84 ? 201 1W4 A O28 1 
HETATM 1855 C C1  . 1W4 D 2 .   ? -1.482  1.310  30.856  0.50 43.81 ? 201 1W4 B C1  1 
HETATM 1856 O O2  . 1W4 D 2 .   ? -2.372  1.957  30.350  0.50 56.09 ? 201 1W4 B O2  1 
HETATM 1857 C C3  . 1W4 D 2 .   ? -0.548  0.428  30.147  0.50 41.43 ? 201 1W4 B C3  1 
HETATM 1858 C C4  . 1W4 D 2 .   ? 0.405   -0.308 30.855  0.50 36.18 ? 201 1W4 B C4  1 
HETATM 1859 C C5  . 1W4 D 2 .   ? 1.288   -1.152 30.173  0.50 40.89 ? 201 1W4 B C5  1 
HETATM 1860 C C6  . 1W4 D 2 .   ? 1.145   -1.325 28.797  0.50 38.48 ? 201 1W4 B C6  1 
HETATM 1861 C C7  . 1W4 D 2 .   ? 0.243   -0.540 28.084  0.50 34.66 ? 201 1W4 B C7  1 
HETATM 1862 C C8  . 1W4 D 2 .   ? -0.582  0.346  28.759  0.50 35.00 ? 201 1W4 B C8  1 
HETATM 1863 N N9  . 1W4 D 2 .   ? 2.271   -1.807 30.843  0.50 42.63 ? 201 1W4 B N9  1 
HETATM 1864 C C10 . 1W4 D 2 .   ? 2.007   -2.374 32.153  0.50 46.16 ? 201 1W4 B C10 1 
HETATM 1865 C C11 . 1W4 D 2 .   ? 3.662   -1.616 30.472  0.50 40.26 ? 201 1W4 B C11 1 
HETATM 1866 C C12 . 1W4 D 2 .   ? 0.353   -0.597 26.636  0.50 30.87 ? 201 1W4 B C12 1 
HETATM 1867 C C13 . 1W4 D 2 .   ? 0.033   0.258  25.802  0.50 24.53 ? 201 1W4 B C13 1 
HETATM 1868 C C14 . 1W4 D 2 .   ? 0.000   0.102  24.360  0.50 19.94 ? 201 1W4 B C14 1 
HETATM 1869 C C15 . 1W4 D 2 .   ? 0.154   -1.112 23.692  0.50 20.19 ? 201 1W4 B C15 1 
HETATM 1870 C C16 . 1W4 D 2 .   ? 0.133   -1.186 22.305  0.50 16.72 ? 201 1W4 B C16 1 
HETATM 1871 C C17 . 1W4 D 2 .   ? -0.014  0.004  21.584  0.50 17.13 ? 201 1W4 B C17 1 
HETATM 1872 C C18 . 1W4 D 2 .   ? -0.178  1.234  22.227  0.50 16.83 ? 201 1W4 B C18 1 
HETATM 1873 C C19 . 1W4 D 2 .   ? -0.203  1.251  23.611  0.50 20.07 ? 201 1W4 B C19 1 
HETATM 1874 C C26 . 1W4 D 2 .   ? 0.227   -2.516 21.604  0.50 17.05 ? 201 1W4 B C26 1 
HETATM 1875 C C27 . 1W4 D 2 .   ? -0.249  2.526  21.459  0.50 17.12 ? 201 1W4 B C27 1 
HETATM 1876 O O28 . 1W4 D 2 .   ? 0.001   -0.011 20.253  0.50 16.71 ? 201 1W4 B O28 1 
HETATM 1877 O O   . HOH E 3 .   ? 0.308   24.088 11.967  1.00 43.39 ? 301 HOH A O   1 
HETATM 1878 O O   . HOH E 3 .   ? 20.470  22.269 3.785   1.00 30.00 ? 302 HOH A O   1 
HETATM 1879 O O   . HOH E 3 .   ? 22.655  17.263 4.632   1.00 41.93 ? 303 HOH A O   1 
HETATM 1880 O O   . HOH E 3 .   ? -10.692 15.899 20.161  1.00 30.61 ? 304 HOH A O   1 
HETATM 1881 O O   . HOH E 3 .   ? 0.551   12.361 15.739  1.00 27.71 ? 305 HOH A O   1 
HETATM 1882 O O   . HOH E 3 .   ? -3.797  23.134 11.487  1.00 47.64 ? 306 HOH A O   1 
HETATM 1883 O O   . HOH E 3 .   ? 15.964  21.207 8.731   1.00 38.37 ? 307 HOH A O   1 
HETATM 1884 O O   . HOH E 3 .   ? 0.819   13.277 -2.477  1.00 28.08 ? 308 HOH A O   1 
HETATM 1885 O O   . HOH E 3 .   ? 20.871  18.772 5.696   1.00 30.00 ? 309 HOH A O   1 
HETATM 1886 O O   . HOH E 3 .   ? -12.500 17.580 1.895   1.00 33.81 ? 310 HOH A O   1 
HETATM 1887 O O   . HOH E 3 .   ? 15.811  13.808 5.935   1.00 28.69 ? 311 HOH A O   1 
HETATM 1888 O O   . HOH E 3 .   ? 14.977  11.199 4.942   1.00 26.51 ? 312 HOH A O   1 
HETATM 1889 O O   . HOH E 3 .   ? -1.181  19.451 -5.882  1.00 49.97 ? 313 HOH A O   1 
HETATM 1890 O O   . HOH E 3 .   ? -3.072  13.458 17.600  1.00 19.93 ? 314 HOH A O   1 
HETATM 1891 O O   . HOH E 3 .   ? 14.224  17.367 -5.179  1.00 39.35 ? 315 HOH A O   1 
HETATM 1892 O O   . HOH E 3 .   ? 12.372  12.449 -5.380  1.00 47.93 ? 316 HOH A O   1 
HETATM 1893 O O   . HOH E 3 .   ? -14.948 13.897 19.581  1.00 44.72 ? 317 HOH A O   1 
HETATM 1894 O O   . HOH E 3 .   ? -3.931  24.250 0.531   1.00 30.00 ? 318 HOH A O   1 
HETATM 1895 O O   . HOH E 3 .   ? -9.680  11.688 15.338  1.00 16.03 ? 319 HOH A O   1 
HETATM 1896 O O   . HOH E 3 .   ? -3.664  24.227 4.733   1.00 25.89 ? 320 HOH A O   1 
HETATM 1897 O O   . HOH E 3 .   ? -13.384 12.988 6.005   1.00 40.13 ? 321 HOH A O   1 
HETATM 1898 O O   . HOH E 3 .   ? -16.396 -3.399 12.026  1.00 32.29 ? 322 HOH A O   1 
HETATM 1899 O O   . HOH E 3 .   ? 13.315  12.165 8.806   1.00 23.13 ? 323 HOH A O   1 
HETATM 1900 O O   . HOH E 3 .   ? -12.969 2.242  -1.622  1.00 49.66 ? 324 HOH A O   1 
HETATM 1901 O O   . HOH E 3 .   ? 18.062  10.664 -4.315  1.00 49.12 ? 325 HOH A O   1 
HETATM 1902 O O   . HOH E 3 .   ? -4.433  18.316 -3.772  1.00 40.02 ? 326 HOH A O   1 
HETATM 1903 O O   . HOH E 3 .   ? -20.954 12.440 14.364  1.00 38.59 ? 327 HOH A O   1 
HETATM 1904 O O   . HOH E 3 .   ? -12.028 21.105 17.771  1.00 48.87 ? 328 HOH A O   1 
HETATM 1905 O O   . HOH E 3 .   ? 12.083  23.655 7.244   1.00 22.71 ? 329 HOH A O   1 
HETATM 1906 O O   . HOH E 3 .   ? 15.999  19.117 10.813  1.00 33.61 ? 330 HOH A O   1 
HETATM 1907 O O   . HOH E 3 .   ? 3.707   14.592 -3.862  1.00 23.42 ? 331 HOH A O   1 
HETATM 1908 O O   . HOH E 3 .   ? -6.973  12.227 -4.037  1.00 28.32 ? 332 HOH A O   1 
HETATM 1909 O O   . HOH E 3 .   ? 7.427   22.386 -9.358  1.00 35.55 ? 333 HOH A O   1 
HETATM 1910 O O   . HOH E 3 .   ? 13.766  16.800 -3.017  1.00 38.26 ? 334 HOH A O   1 
HETATM 1911 O O   . HOH E 3 .   ? -17.135 15.614 9.497   1.00 40.67 ? 335 HOH A O   1 
HETATM 1912 O O   . HOH E 3 .   ? 7.591   1.553  7.564   1.00 18.19 ? 336 HOH A O   1 
HETATM 1913 O O   . HOH E 3 .   ? -12.356 15.774 3.838   1.00 28.59 ? 337 HOH A O   1 
HETATM 1914 O O   . HOH E 3 .   ? -5.679  2.177  14.621  1.00 25.71 ? 338 HOH A O   1 
HETATM 1915 O O   . HOH E 3 .   ? 17.366  12.550 2.668   1.00 27.07 ? 339 HOH A O   1 
HETATM 1916 O O   . HOH E 3 .   ? -6.313  0.850  -1.220  1.00 48.60 ? 340 HOH A O   1 
HETATM 1917 O O   . HOH E 3 .   ? 4.637   8.494  10.032  1.00 21.05 ? 341 HOH A O   1 
HETATM 1918 O O   . HOH E 3 .   ? 12.260  14.355 -3.046  1.00 29.41 ? 342 HOH A O   1 
HETATM 1919 O O   . HOH E 3 .   ? -8.839  9.644  17.041  1.00 15.57 ? 343 HOH A O   1 
HETATM 1920 O O   . HOH E 3 .   ? -15.147 8.678  4.507   1.00 33.06 ? 344 HOH A O   1 
HETATM 1921 O O   . HOH E 3 .   ? -8.043  8.197  14.361  1.00 15.08 ? 345 HOH A O   1 
HETATM 1922 O O   . HOH E 3 .   ? -14.248 -3.768 4.514   1.00 23.72 ? 346 HOH A O   1 
HETATM 1923 O O   . HOH E 3 .   ? -13.733 5.547  4.362   1.00 23.46 ? 347 HOH A O   1 
HETATM 1924 O O   . HOH E 3 .   ? -14.870 16.317 -2.447  1.00 40.58 ? 348 HOH A O   1 
HETATM 1925 O O   . HOH E 3 .   ? -16.677 -3.047 7.169   1.00 45.70 ? 349 HOH A O   1 
HETATM 1926 O O   . HOH E 3 .   ? -10.945 14.527 6.936   1.00 18.26 ? 350 HOH A O   1 
HETATM 1927 O O   . HOH E 3 .   ? 21.830  18.853 3.315   1.00 51.17 ? 351 HOH A O   1 
HETATM 1928 O O   . HOH E 3 .   ? -3.661  2.151  16.411  1.00 32.85 ? 352 HOH A O   1 
HETATM 1929 O O   . HOH E 3 .   ? -1.263  23.386 3.874   1.00 23.59 ? 353 HOH A O   1 
HETATM 1930 O O   . HOH E 3 .   ? 14.932  26.638 3.384   1.00 20.26 ? 354 HOH A O   1 
HETATM 1931 O O   . HOH E 3 .   ? 12.518  1.754  1.415   1.00 34.38 ? 355 HOH A O   1 
HETATM 1932 O O   . HOH E 3 .   ? 11.615  25.973 -11.787 1.00 26.48 ? 356 HOH A O   1 
HETATM 1933 O O   . HOH E 3 .   ? -8.173  21.115 16.420  1.00 50.63 ? 357 HOH A O   1 
HETATM 1934 O O   . HOH E 3 .   ? -20.699 11.972 21.481  1.00 41.58 ? 358 HOH A O   1 
HETATM 1935 O O   . HOH E 3 .   ? 8.312   5.757  -0.384  1.00 26.91 ? 359 HOH A O   1 
HETATM 1936 O O   . HOH E 3 .   ? -5.553  7.279  -5.668  1.00 44.41 ? 360 HOH A O   1 
HETATM 1937 O O   . HOH E 3 .   ? 12.944  27.796 5.421   1.00 39.21 ? 361 HOH A O   1 
HETATM 1938 O O   . HOH E 3 .   ? 3.941   25.509 -1.176  1.00 42.41 ? 362 HOH A O   1 
HETATM 1939 O O   . HOH E 3 .   ? 13.081  24.011 14.078  1.00 60.22 ? 363 HOH A O   1 
HETATM 1940 O O   . HOH E 3 .   ? -14.470 8.222  26.412  1.00 40.30 ? 364 HOH A O   1 
HETATM 1941 O O   . HOH E 3 .   ? 1.909   19.035 -7.127  1.00 57.17 ? 365 HOH A O   1 
HETATM 1942 O O   . HOH E 3 .   ? 8.393   26.909 4.743   1.00 25.98 ? 366 HOH A O   1 
HETATM 1943 O O   . HOH E 3 .   ? 15.660  2.910  -1.318  1.00 44.86 ? 367 HOH A O   1 
HETATM 1944 O O   . HOH E 3 .   ? -20.837 4.437  13.519  1.00 46.40 ? 368 HOH A O   1 
HETATM 1945 O O   . HOH E 3 .   ? -4.560  11.375 -5.102  1.00 25.46 ? 369 HOH A O   1 
HETATM 1946 O O   . HOH E 3 .   ? 8.098   15.506 -9.199  1.00 40.43 ? 370 HOH A O   1 
HETATM 1947 O O   . HOH E 3 .   ? 11.782  30.770 5.157   1.00 26.61 ? 371 HOH A O   1 
HETATM 1948 O O   . HOH E 3 .   ? 22.610  10.090 1.206   1.00 53.65 ? 372 HOH A O   1 
HETATM 1949 O O   . HOH E 3 .   ? 3.096   28.737 12.916  1.00 42.11 ? 373 HOH A O   1 
HETATM 1950 O O   . HOH E 3 .   ? -17.266 7.262  19.785  1.00 30.00 ? 374 HOH A O   1 
HETATM 1951 O O   . HOH E 3 .   ? -3.907  16.037 -4.733  1.00 36.52 ? 375 HOH A O   1 
HETATM 1952 O O   . HOH E 3 .   ? 11.000  32.935 7.536   1.00 43.98 ? 376 HOH A O   1 
HETATM 1953 O O   . HOH E 3 .   ? -15.643 10.380 6.445   1.00 34.40 ? 377 HOH A O   1 
HETATM 1954 O O   . HOH E 3 .   ? -11.408 8.597  -5.821  1.00 37.92 ? 378 HOH A O   1 
HETATM 1955 O O   . HOH E 3 .   ? 17.123  7.528  3.470   1.00 48.66 ? 379 HOH A O   1 
HETATM 1956 O O   . HOH E 3 .   ? 10.026  18.555 -10.234 1.00 32.92 ? 380 HOH A O   1 
HETATM 1957 O O   . HOH E 3 .   ? 20.747  11.816 -2.647  1.00 39.56 ? 381 HOH A O   1 
HETATM 1958 O O   . HOH E 3 .   ? -1.514  24.325 1.330   1.00 31.71 ? 382 HOH A O   1 
HETATM 1959 O O   . HOH E 3 .   ? 18.110  2.816  -4.785  1.00 58.33 ? 383 HOH A O   1 
HETATM 1960 O O   . HOH E 3 .   ? -5.989  21.732 17.123  1.00 35.98 ? 384 HOH A O   1 
HETATM 1961 O O   . HOH E 3 .   ? 16.211  5.675  1.898   1.00 56.32 ? 385 HOH A O   1 
HETATM 1962 O O   . HOH E 3 .   ? 9.455   20.766 14.744  1.00 35.45 ? 386 HOH A O   1 
HETATM 1963 O O   . HOH E 3 .   ? -6.253  23.070 8.351   1.00 37.31 ? 387 HOH A O   1 
HETATM 1964 O O   . HOH E 3 .   ? -5.088  24.904 2.432   1.00 30.00 ? 388 HOH A O   1 
HETATM 1965 O O   . HOH E 3 .   ? 17.249  10.111 4.035   1.00 34.86 ? 389 HOH A O   1 
HETATM 1966 O O   . HOH E 3 .   ? -13.608 15.495 21.185  1.00 50.85 ? 390 HOH A O   1 
HETATM 1967 O O   . HOH E 3 .   ? 17.446  11.103 8.438   1.00 45.65 ? 391 HOH A O   1 
HETATM 1968 O O   . HOH E 3 .   ? -3.814  25.806 6.772   1.00 41.95 ? 392 HOH A O   1 
HETATM 1969 O O   . HOH F 3 .   ? 0.059   22.052 35.059  1.00 43.53 ? 301 HOH B O   1 
HETATM 1970 O O   . HOH F 3 .   ? 8.427   19.069 22.621  1.00 30.00 ? 302 HOH B O   1 
HETATM 1971 O O   . HOH F 3 .   ? 4.283   18.473 38.114  1.00 39.62 ? 303 HOH B O   1 
HETATM 1972 O O   . HOH F 3 .   ? -19.135 19.449 26.640  1.00 30.00 ? 304 HOH B O   1 
HETATM 1973 O O   . HOH F 3 .   ? -12.635 20.821 20.535  1.00 35.36 ? 305 HOH B O   1 
HETATM 1974 O O   . HOH F 3 .   ? -18.360 22.000 27.498  1.00 40.45 ? 306 HOH B O   1 
HETATM 1975 O O   . HOH F 3 .   ? -18.848 18.873 28.901  1.00 30.00 ? 307 HOH B O   1 
HETATM 1976 O O   . HOH F 3 .   ? 4.831   20.703 15.604  1.00 49.22 ? 308 HOH B O   1 
HETATM 1977 O O   . HOH F 3 .   ? -16.483 20.011 35.491  1.00 28.50 ? 309 HOH B O   1 
HETATM 1978 O O   . HOH F 3 .   ? -12.988 3.424  30.000  1.00 45.60 ? 310 HOH B O   1 
HETATM 1979 O O   . HOH F 3 .   ? 13.089  14.202 11.513  1.00 20.81 ? 311 HOH B O   1 
HETATM 1980 O O   . HOH F 3 .   ? 7.238   23.291 27.019  1.00 39.12 ? 312 HOH B O   1 
HETATM 1981 O O   . HOH F 3 .   ? 16.618  8.578  9.456   1.00 47.85 ? 313 HOH B O   1 
HETATM 1982 O O   . HOH F 3 .   ? 4.096   23.692 19.914  1.00 61.64 ? 314 HOH B O   1 
HETATM 1983 O O   . HOH F 3 .   ? 11.631  10.209 16.501  1.00 16.00 ? 315 HOH B O   1 
HETATM 1984 O O   . HOH F 3 .   ? 5.561   15.254 36.924  1.00 40.49 ? 316 HOH B O   1 
HETATM 1985 O O   . HOH F 3 .   ? 7.270   17.051 35.619  1.00 40.32 ? 317 HOH B O   1 
HETATM 1986 O O   . HOH F 3 .   ? -11.496 14.067 22.744  1.00 33.19 ? 318 HOH B O   1 
HETATM 1987 O O   . HOH F 3 .   ? -10.094 18.218 35.340  1.00 39.40 ? 319 HOH B O   1 
HETATM 1988 O O   . HOH F 3 .   ? 14.379  3.341  27.569  1.00 26.83 ? 320 HOH B O   1 
HETATM 1989 O O   . HOH F 3 .   ? 5.108   13.103 14.307  1.00 19.08 ? 321 HOH B O   1 
HETATM 1990 O O   . HOH F 3 .   ? 6.528   6.140  37.338  1.00 42.82 ? 322 HOH B O   1 
HETATM 1991 O O   . HOH F 3 .   ? 23.819  8.181  19.080  1.00 30.00 ? 323 HOH B O   1 
HETATM 1992 O O   . HOH F 3 .   ? 10.347  8.383  14.936  1.00 17.46 ? 324 HOH B O   1 
HETATM 1993 O O   . HOH F 3 .   ? 15.879  -5.568 24.471  1.00 47.40 ? 325 HOH B O   1 
HETATM 1994 O O   . HOH F 3 .   ? -7.127  6.364  32.143  1.00 30.17 ? 326 HOH B O   1 
HETATM 1995 O O   . HOH F 3 .   ? -1.746  14.822 35.827  1.00 29.72 ? 327 HOH B O   1 
HETATM 1996 O O   . HOH F 3 .   ? 19.641  12.611 22.275  1.00 45.83 ? 328 HOH B O   1 
HETATM 1997 O O   . HOH F 3 .   ? -3.327  9.017  22.090  1.00 18.67 ? 329 HOH B O   1 
HETATM 1998 O O   . HOH F 3 .   ? 5.782   1.371  17.142  1.00 24.03 ? 330 HOH B O   1 
HETATM 1999 O O   . HOH F 3 .   ? 13.246  12.856 24.897  1.00 22.01 ? 331 HOH B O   1 
HETATM 2000 O O   . HOH F 3 .   ? 9.220   7.003  17.565  1.00 15.35 ? 332 HOH B O   1 
HETATM 2001 O O   . HOH F 3 .   ? 3.862   1.664  15.365  1.00 28.53 ? 333 HOH B O   1 
HETATM 2002 O O   . HOH F 3 .   ? -7.243  2.487  24.220  1.00 17.84 ? 334 HOH B O   1 
HETATM 2003 O O   . HOH F 3 .   ? 13.546  -5.683 27.268  1.00 29.11 ? 335 HOH B O   1 
HETATM 2004 O O   . HOH F 3 .   ? -8.275  24.992 24.555  1.00 30.53 ? 336 HOH B O   1 
HETATM 2005 O O   . HOH F 3 .   ? 15.512  19.080 13.645  1.00 44.06 ? 337 HOH B O   1 
HETATM 2006 O O   . HOH F 3 .   ? 8.534   10.932 35.879  1.00 30.73 ? 338 HOH B O   1 
HETATM 2007 O O   . HOH F 3 .   ? -8.936  29.503 27.510  1.00 49.57 ? 339 HOH B O   1 
HETATM 2008 O O   . HOH F 3 .   ? 16.435  6.084  27.497  1.00 47.55 ? 340 HOH B O   1 
HETATM 2009 O O   . HOH F 3 .   ? 7.882   9.389  17.110  1.00 28.32 ? 341 HOH B O   1 
HETATM 2010 O O   . HOH F 3 .   ? 5.191   17.956 35.749  1.00 30.00 ? 342 HOH B O   1 
HETATM 2011 O O   . HOH F 3 .   ? 11.577  19.963 15.550  1.00 43.71 ? 343 HOH B O   1 
HETATM 2012 O O   . HOH F 3 .   ? -6.041  16.583 41.097  1.00 38.16 ? 344 HOH B O   1 
HETATM 2013 O O   . HOH F 3 .   ? 20.052  3.800  12.889  1.00 35.81 ? 345 HOH B O   1 
HETATM 2014 O O   . HOH F 3 .   ? 1.477   28.249 18.756  1.00 48.43 ? 346 HOH B O   1 
HETATM 2015 O O   . HOH F 3 .   ? 9.623   14.690 35.238  1.00 27.65 ? 347 HOH B O   1 
HETATM 2016 O O   . HOH F 3 .   ? -7.548  19.680 41.869  1.00 38.99 ? 348 HOH B O   1 
HETATM 2017 O O   . HOH F 3 .   ? -11.502 18.441 31.289  1.00 38.38 ? 349 HOH B O   1 
HETATM 2018 O O   . HOH F 3 .   ? 15.129  11.042 25.604  1.00 29.22 ? 350 HOH B O   1 
HETATM 2019 O O   . HOH F 3 .   ? 6.006   10.487 36.931  1.00 30.41 ? 351 HOH B O   1 
HETATM 2020 O O   . HOH F 3 .   ? 12.256  6.789  37.675  1.00 29.76 ? 352 HOH B O   1 
HETATM 2021 O O   . HOH F 3 .   ? -5.170  9.569  40.989  1.00 58.98 ? 353 HOH B O   1 
HETATM 2022 O O   . HOH F 3 .   ? -14.512 20.256 25.490  1.00 38.85 ? 354 HOH B O   1 
HETATM 2023 O O   . HOH F 3 .   ? -0.819  27.855 16.109  1.00 53.99 ? 355 HOH B O   1 
HETATM 2024 O O   . HOH F 3 .   ? 16.287  -5.066 19.117  1.00 33.27 ? 356 HOH B O   1 
HETATM 2025 O O   . HOH F 3 .   ? 15.748  6.408  5.291   1.00 44.29 ? 357 HOH B O   1 
HETATM 2026 O O   . HOH F 3 .   ? -12.314 15.918 31.338  1.00 39.75 ? 358 HOH B O   1 
HETATM 2027 O O   . HOH F 3 .   ? 12.796  14.938 20.324  1.00 33.86 ? 359 HOH B O   1 
HETATM 2028 O O   . HOH F 3 .   ? 25.057  3.599  17.445  1.00 37.61 ? 360 HOH B O   1 
HETATM 2029 O O   . HOH F 3 .   ? 0.615   19.367 38.975  1.00 55.56 ? 361 HOH B O   1 
HETATM 2030 O O   . HOH F 3 .   ? 17.274  7.371  25.619  1.00 46.90 ? 362 HOH B O   1 
HETATM 2031 O O   . HOH F 3 .   ? 9.529   21.692 23.570  1.00 44.59 ? 363 HOH B O   1 
HETATM 2032 O O   . HOH F 3 .   ? 24.780  4.616  22.842  1.00 49.93 ? 364 HOH B O   1 
HETATM 2033 O O   . HOH F 3 .   ? 8.031   24.127 25.063  1.00 30.00 ? 365 HOH B O   1 
HETATM 2034 O O   . HOH F 3 .   ? 15.550  -3.738 27.834  1.00 57.64 ? 366 HOH B O   1 
HETATM 2035 O O   . HOH F 3 .   ? 14.757  15.412 25.274  1.00 47.39 ? 367 HOH B O   1 
HETATM 2036 O O   . HOH F 3 .   ? 13.789  10.021 7.068   1.00 30.35 ? 368 HOH B O   1 
HETATM 2037 O O   . HOH F 3 .   ? -11.381 16.193 35.076  1.00 30.99 ? 369 HOH B O   1 
HETATM 2038 O O   . HOH F 3 .   ? 16.146  12.748 9.508   1.00 47.26 ? 370 HOH B O   1 
HETATM 2039 O O   . HOH F 3 .   ? 10.667  10.015 37.542  1.00 40.49 ? 371 HOH B O   1 
HETATM 2040 O O   . HOH F 3 .   ? 13.522  -1.498 31.506  1.00 48.17 ? 372 HOH B O   1 
# 
