data_9H7H
# 
_entry.id   9H7H 
# 
_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   9H7H         pdb_00009h7h 10.2210/pdb9h7h/pdb 
WWPDB D_1292142793 ?            ?                   
# 
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 2025-03-12 ? 
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' 
# 
loop_
_pdbx_audit_revision_category.ordinal 
_pdbx_audit_revision_category.revision_ordinal 
_pdbx_audit_revision_category.data_content_type 
_pdbx_audit_revision_category.category 
1 2 'Structure model' citation        
2 2 'Structure model' citation_author 
# 
_pdbx_database_status.status_code                     REL 
_pdbx_database_status.status_code_sf                  REL 
_pdbx_database_status.status_code_mr                  ? 
_pdbx_database_status.entry_id                        9H7H 
_pdbx_database_status.recvd_initial_deposition_date   2024-10-27 
_pdbx_database_status.SG_entry                        N 
_pdbx_database_status.deposit_site                    PDBE 
_pdbx_database_status.process_site                    PDBE 
_pdbx_database_status.status_code_cs                  ? 
_pdbx_database_status.status_code_nmr_data            ? 
_pdbx_database_status.methods_development_category    ? 
_pdbx_database_status.pdb_format_compatible           Y 
# 
_pdbx_contact_author.id                 2 
_pdbx_contact_author.email              s.wood@ucl.ac.uk 
_pdbx_contact_author.name_first         Stephen 
_pdbx_contact_author.name_last          Wood 
_pdbx_contact_author.name_mi            ? 
_pdbx_contact_author.role               'principal investigator/group leader' 
_pdbx_contact_author.identifier_ORCID   0000-0002-4106-775X 
# 
_audit_author.name               'Chen, W.' 
_audit_author.pdbx_ordinal       1 
_audit_author.identifier_ORCID   0000-0002-8180-366X 
# 
loop_
_citation.abstract 
_citation.abstract_id_CAS 
_citation.book_id_ISBN 
_citation.book_publisher 
_citation.book_publisher_city 
_citation.book_title 
_citation.coordinate_linkage 
_citation.country 
_citation.database_id_Medline 
_citation.details 
_citation.id 
_citation.journal_abbrev 
_citation.journal_id_ASTM 
_citation.journal_id_CSD 
_citation.journal_id_ISSN 
_citation.journal_full 
_citation.journal_issue 
_citation.journal_volume 
_citation.language 
_citation.page_first 
_citation.page_last 
_citation.title 
_citation.year 
_citation.database_id_CSD 
_citation.pdbx_database_id_DOI 
_citation.pdbx_database_id_PubMed 
_citation.pdbx_database_id_patent 
_citation.unpublished_flag 
? ? ? ? ? ? ? US ? ? primary 'Plos One' ? ? 1932-6203 ? ? 20 ? e0323816 e0323816 
'Fragment-based drug discovery for transthyretin kinetic stabilisers using a novel capillary zone electrophoresis method.' 2025 ? 
10.1371/journal.pone.0323816 40367241 ? ? 
? ? ? ? ? ? ? US ? ? 1       Biorxiv    ? ? 2692-8205 ? ? ?  ? ?        ?        
'Fragment-Based Drug Discovery for Transthyretin Kinetic Stabilisers Using a Novel Capillary Zone Electrophoresis Method'  2025 ? 
10.1101/2025.02.22.639275    ?        ? ? 
# 
loop_
_citation_author.citation_id 
_citation_author.name 
_citation_author.ordinal 
_citation_author.identifier_ORCID 
primary 'Chen, W.' 1 0000-0002-8180-366X 
1       'Chen, W.' 2 0000-0002-8180-366X 
# 
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 'CALCIUM ION'       40.078    2  ? ? ? ? 
3 non-polymer syn isoquinolin-3-amine 144.173   1  ? ? ? ? 
4 water       nat water               18.015    97 ? ? ? ? 
# 
_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 'CALCIUM ION'       CA  
3 isoquinolin-3-amine WLX 
4 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                    Blood 
_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      'Homo sapiens' 
_entity_src_gen.pdbx_host_org_ncbi_taxonomy_id     9606 
_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 
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 
CA  non-polymer         . 'CALCIUM ION'       ? 'Ca 2'           40.078  
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 
WLX non-polymer         . isoquinolin-3-amine ? 'C9 H8 N2'       144.173 
# 
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 ALA 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 ?   ?   ?   B . n 
B 1 101 GLY 101 101 ?   ?   ?   B . n 
B 1 102 PRO 102 102 ?   ?   ?   B . n 
B 1 103 ARG 103 103 ?   ?   ?   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        WLX 
_pdbx_entity_instance_feature.asym_id        ? 
_pdbx_entity_instance_feature.seq_num        ? 
_pdbx_entity_instance_feature.auth_comp_id   WLX 
_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 CA  1  201 1  CA  CA  A . 
D 2 CA  1  201 1  CA  CA  B . 
E 3 WLX 1  202 1  WLX 029 B . 
F 4 HOH 1  301 84 HOH HOH A . 
F 4 HOH 2  302 78 HOH HOH A . 
F 4 HOH 3  303 35 HOH HOH A . 
F 4 HOH 4  304 26 HOH HOH A . 
F 4 HOH 5  305 94 HOH HOH A . 
F 4 HOH 6  306 77 HOH HOH A . 
F 4 HOH 7  307 28 HOH HOH A . 
F 4 HOH 8  308 59 HOH HOH A . 
F 4 HOH 9  309 57 HOH HOH A . 
F 4 HOH 10 310 2  HOH HOH A . 
F 4 HOH 11 311 38 HOH HOH A . 
F 4 HOH 12 312 17 HOH HOH A . 
F 4 HOH 13 313 52 HOH HOH A . 
F 4 HOH 14 314 7  HOH HOH A . 
F 4 HOH 15 315 36 HOH HOH A . 
F 4 HOH 16 316 50 HOH HOH A . 
F 4 HOH 17 317 53 HOH HOH A . 
F 4 HOH 18 318 19 HOH HOH A . 
F 4 HOH 19 319 58 HOH HOH A . 
F 4 HOH 20 320 32 HOH HOH A . 
F 4 HOH 21 321 24 HOH HOH A . 
F 4 HOH 22 322 91 HOH HOH A . 
F 4 HOH 23 323 11 HOH HOH A . 
F 4 HOH 24 324 3  HOH HOH A . 
F 4 HOH 25 325 14 HOH HOH A . 
F 4 HOH 26 326 90 HOH HOH A . 
F 4 HOH 27 327 23 HOH HOH A . 
F 4 HOH 28 328 67 HOH HOH A . 
F 4 HOH 29 329 51 HOH HOH A . 
F 4 HOH 30 330 85 HOH HOH A . 
F 4 HOH 31 331 46 HOH HOH A . 
F 4 HOH 32 332 61 HOH HOH A . 
F 4 HOH 33 333 39 HOH HOH A . 
F 4 HOH 34 334 18 HOH HOH A . 
F 4 HOH 35 335 29 HOH HOH A . 
F 4 HOH 36 336 66 HOH HOH A . 
F 4 HOH 37 337 6  HOH HOH A . 
F 4 HOH 38 338 68 HOH HOH A . 
F 4 HOH 39 339 37 HOH HOH A . 
F 4 HOH 40 340 49 HOH HOH A . 
F 4 HOH 41 341 5  HOH HOH A . 
F 4 HOH 42 342 31 HOH HOH A . 
F 4 HOH 43 343 27 HOH HOH A . 
F 4 HOH 44 344 96 HOH HOH A . 
F 4 HOH 45 345 22 HOH HOH A . 
F 4 HOH 46 346 79 HOH HOH A . 
F 4 HOH 47 347 81 HOH HOH A . 
F 4 HOH 48 348 83 HOH HOH A . 
F 4 HOH 49 349 72 HOH HOH A . 
F 4 HOH 50 350 69 HOH HOH A . 
F 4 HOH 51 351 95 HOH HOH A . 
F 4 HOH 52 352 65 HOH HOH A . 
F 4 HOH 53 353 55 HOH HOH A . 
F 4 HOH 54 354 8  HOH HOH A . 
F 4 HOH 55 355 60 HOH HOH A . 
F 4 HOH 56 356 75 HOH HOH A . 
F 4 HOH 57 357 30 HOH HOH A . 
F 4 HOH 58 358 63 HOH HOH A . 
F 4 HOH 59 359 20 HOH HOH A . 
F 4 HOH 60 360 62 HOH HOH A . 
F 4 HOH 61 361 15 HOH HOH A . 
F 4 HOH 62 362 21 HOH HOH A . 
F 4 HOH 63 363 33 HOH HOH A . 
G 4 HOH 1  301 97 HOH HOH B . 
G 4 HOH 2  302 76 HOH HOH B . 
G 4 HOH 3  303 10 HOH HOH B . 
G 4 HOH 4  304 41 HOH HOH B . 
G 4 HOH 5  305 56 HOH HOH B . 
G 4 HOH 6  306 4  HOH HOH B . 
G 4 HOH 7  307 40 HOH HOH B . 
G 4 HOH 8  308 73 HOH HOH B . 
G 4 HOH 9  309 13 HOH HOH B . 
G 4 HOH 10 310 9  HOH HOH B . 
G 4 HOH 11 311 47 HOH HOH B . 
G 4 HOH 12 312 64 HOH HOH B . 
G 4 HOH 13 313 1  HOH HOH B . 
G 4 HOH 14 314 89 HOH HOH B . 
G 4 HOH 15 315 54 HOH HOH B . 
G 4 HOH 16 316 12 HOH HOH B . 
G 4 HOH 17 317 34 HOH HOH B . 
G 4 HOH 18 318 86 HOH HOH B . 
G 4 HOH 19 319 25 HOH HOH B . 
G 4 HOH 20 320 16 HOH HOH B . 
G 4 HOH 21 321 92 HOH HOH B . 
G 4 HOH 22 322 44 HOH HOH B . 
G 4 HOH 23 323 45 HOH HOH B . 
G 4 HOH 24 324 42 HOH HOH B . 
G 4 HOH 25 325 48 HOH HOH B . 
G 4 HOH 26 326 74 HOH HOH B . 
G 4 HOH 27 327 43 HOH HOH B . 
G 4 HOH 28 328 88 HOH HOH B . 
G 4 HOH 29 329 71 HOH HOH B . 
G 4 HOH 30 330 80 HOH HOH B . 
G 4 HOH 31 331 93 HOH HOH B . 
G 4 HOH 32 332 82 HOH HOH B . 
G 4 HOH 33 333 70 HOH HOH B . 
G 4 HOH 34 334 87 HOH HOH B . 
# 
loop_
_pdbx_unobs_or_zero_occ_atoms.id 
_pdbx_unobs_or_zero_occ_atoms.PDB_model_num 
_pdbx_unobs_or_zero_occ_atoms.polymer_flag 
_pdbx_unobs_or_zero_occ_atoms.occupancy_flag 
_pdbx_unobs_or_zero_occ_atoms.auth_asym_id 
_pdbx_unobs_or_zero_occ_atoms.auth_comp_id 
_pdbx_unobs_or_zero_occ_atoms.auth_seq_id 
_pdbx_unobs_or_zero_occ_atoms.PDB_ins_code 
_pdbx_unobs_or_zero_occ_atoms.auth_atom_id 
_pdbx_unobs_or_zero_occ_atoms.label_alt_id 
_pdbx_unobs_or_zero_occ_atoms.label_asym_id 
_pdbx_unobs_or_zero_occ_atoms.label_comp_id 
_pdbx_unobs_or_zero_occ_atoms.label_seq_id 
_pdbx_unobs_or_zero_occ_atoms.label_atom_id 
1  1 Y 1 A CYS 10  ? N   ? A CYS 10  N   
2  1 Y 1 A CYS 10  ? CB  ? A CYS 10  CB  
3  1 Y 1 A CYS 10  ? SG  ? A CYS 10  SG  
4  1 Y 1 A LYS 15  ? CG  ? A LYS 15  CG  
5  1 Y 1 A LYS 15  ? CD  ? A LYS 15  CD  
6  1 Y 1 A LYS 15  ? CE  ? A LYS 15  CE  
7  1 Y 1 A LYS 15  ? NZ  ? A LYS 15  NZ  
8  1 Y 1 A ARG 21  ? NH1 ? A ARG 21  NH1 
9  1 Y 1 A ARG 21  ? NH2 ? A ARG 21  NH2 
10 1 Y 1 A LYS 35  ? CE  ? A LYS 35  CE  
11 1 Y 1 A LYS 35  ? NZ  ? A LYS 35  NZ  
12 1 Y 1 A ASP 39  ? CG  ? A ASP 39  CG  
13 1 Y 1 A ASP 39  ? OD1 ? A ASP 39  OD1 
14 1 Y 1 A ASP 39  ? OD2 ? A ASP 39  OD2 
15 1 Y 1 A GLU 42  ? CG  ? A GLU 42  CG  
16 1 Y 1 A GLU 42  ? CD  ? A GLU 42  CD  
17 1 Y 1 A GLU 42  ? OE1 ? A GLU 42  OE1 
18 1 Y 1 A GLU 42  ? OE2 ? A GLU 42  OE2 
19 1 Y 1 A LYS 48  ? CE  ? A LYS 48  CE  
20 1 Y 1 A LYS 48  ? NZ  ? A LYS 48  NZ  
21 1 Y 1 A GLU 51  ? CG  ? A GLU 51  CG  
22 1 Y 1 A GLU 51  ? CD  ? A GLU 51  CD  
23 1 Y 1 A GLU 51  ? OE1 ? A GLU 51  OE1 
24 1 Y 1 A GLU 51  ? OE2 ? A GLU 51  OE2 
25 1 Y 1 A LYS 70  ? NZ  ? A LYS 70  NZ  
26 1 Y 1 A ARG 104 ? CG  ? A ARG 104 CG  
27 1 Y 1 A ARG 104 ? CD  ? A ARG 104 CD  
28 1 Y 1 A ARG 104 ? NE  ? A ARG 104 NE  
29 1 Y 1 A ARG 104 ? CZ  ? A ARG 104 CZ  
30 1 Y 1 A ARG 104 ? NH1 ? A ARG 104 NH1 
31 1 Y 1 A ARG 104 ? NH2 ? A ARG 104 NH2 
32 1 Y 1 B CYS 10  ? N   ? B CYS 10  N   
33 1 Y 1 B CYS 10  ? CA  ? B CYS 10  CA  
34 1 Y 1 B CYS 10  ? CB  ? B CYS 10  CB  
35 1 Y 1 B CYS 10  ? SG  ? B CYS 10  SG  
36 1 Y 1 B LYS 15  ? CE  ? B LYS 15  CE  
37 1 Y 1 B LYS 15  ? NZ  ? B LYS 15  NZ  
38 1 Y 1 B ARG 21  ? CZ  ? B ARG 21  CZ  
39 1 Y 1 B ARG 21  ? NH1 ? B ARG 21  NH1 
40 1 Y 1 B ARG 21  ? NH2 ? B ARG 21  NH2 
41 1 Y 1 B LYS 35  ? CE  ? B LYS 35  CE  
42 1 Y 1 B LYS 35  ? NZ  ? B LYS 35  NZ  
43 1 Y 1 B ASP 39  ? CG  ? B ASP 39  CG  
44 1 Y 1 B ASP 39  ? OD1 ? B ASP 39  OD1 
45 1 Y 1 B ASP 39  ? OD2 ? B ASP 39  OD2 
46 1 Y 1 B LYS 48  ? CE  ? B LYS 48  CE  
47 1 Y 1 B LYS 48  ? NZ  ? B LYS 48  NZ  
48 1 Y 1 B GLU 51  ? CG  ? B GLU 51  CG  
49 1 Y 1 B GLU 51  ? CD  ? B GLU 51  CD  
50 1 Y 1 B GLU 51  ? OE1 ? B GLU 51  OE1 
51 1 Y 1 B GLU 51  ? OE2 ? B GLU 51  OE2 
52 1 Y 1 B GLU 62  ? CG  ? B GLU 62  CG  
53 1 Y 1 B GLU 62  ? CD  ? B GLU 62  CD  
54 1 Y 1 B GLU 62  ? OE1 ? B GLU 62  OE1 
55 1 Y 1 B GLU 62  ? OE2 ? B GLU 62  OE2 
56 1 Y 1 B LYS 80  ? CG  ? B LYS 80  CG  
57 1 Y 1 B LYS 80  ? CD  ? B LYS 80  CD  
58 1 Y 1 B LYS 80  ? CE  ? B LYS 80  CE  
59 1 Y 1 B LYS 80  ? NZ  ? B LYS 80  NZ  
60 1 Y 1 B ARG 104 ? CG  ? B ARG 104 CG  
61 1 Y 1 B ARG 104 ? CD  ? B ARG 104 CD  
62 1 Y 1 B ARG 104 ? NE  ? B ARG 104 NE  
63 1 Y 1 B ARG 104 ? CZ  ? B ARG 104 CZ  
64 1 Y 1 B ARG 104 ? NH1 ? B ARG 104 NH1 
65 1 Y 1 B ARG 104 ? NH2 ? B ARG 104 NH2 
66 1 Y 1 B ASN 124 ? CG  ? B ASN 124 CG  
67 1 Y 1 B ASN 124 ? OD1 ? B ASN 124 OD1 
68 1 Y 1 B ASN 124 ? ND2 ? B ASN 124 ND2 
# 
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 ? ? ? 5.7.0032 1 
? 'data reduction' ? ? ? ? ? ? ? ? ? ? ? xia2   ? ? ? .        2 
? 'data scaling'   ? ? ? ? ? ? ? ? ? ? ? xia2   ? ? ? .        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                     9H7H 
_cell.details                      ? 
_cell.formula_units_Z              ? 
_cell.length_a                     85.640 
_cell.length_a_esd                 ? 
_cell.length_b                     42.500 
_cell.length_b_esd                 ? 
_cell.length_c                     64.930 
_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                         9H7H 
_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                   9H7H 
_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             2.14 
_exptl_crystal.density_method               ? 
_exptl_crystal.density_percent_sol          42.63 
_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, HANGING DROP' 
_exptl_crystal_grow.method_ref      ? 
_exptl_crystal_grow.pH              7.5 
_exptl_crystal_grow.pressure        ? 
_exptl_crystal_grow.pressure_esd    ? 
_exptl_crystal_grow.seeding         ? 
_exptl_crystal_grow.seeding_ref     ? 
_exptl_crystal_grow.temp_details    ? 
_exptl_crystal_grow.temp_esd        ? 
_exptl_crystal_grow.time            ? 
_exptl_crystal_grow.pdbx_details    '100 mM HEPES, 200 mM CaCl2, 28% v/v PEG400, pH 7.5' 
_exptl_crystal_grow.pdbx_pH_range   ? 
_exptl_crystal_grow.temp            294.15 
# 
_diffrn.ambient_environment              ? 
_diffrn.ambient_temp                     100 
_diffrn.ambient_temp_details             ? 
_diffrn.ambient_temp_esd                 ? 
_diffrn.crystal_id                       1 
_diffrn.crystal_support                  ? 
_diffrn.crystal_treatment                ? 
_diffrn.details                          ? 
_diffrn.id                               1 
_diffrn.ambient_pressure                 ? 
_diffrn.ambient_pressure_esd             ? 
_diffrn.ambient_pressure_gt              ? 
_diffrn.ambient_pressure_lt              ? 
_diffrn.ambient_temp_gt                  ? 
_diffrn.ambient_temp_lt                  ? 
_diffrn.pdbx_serial_crystal_experiment   N 
# 
_diffrn_detector.details                      ? 
_diffrn_detector.detector                     PIXEL 
_diffrn_detector.diffrn_id                    1 
_diffrn_detector.type                         'DECTRIS PILATUS 6M' 
_diffrn_detector.area_resol_mean              ? 
_diffrn_detector.dtime                        ? 
_diffrn_detector.pdbx_frames_total            ? 
_diffrn_detector.pdbx_collection_time_total   ? 
_diffrn_detector.pdbx_collection_date         2012-10-06 
_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   0.92 
_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                        'DIAMOND BEAMLINE I04-1' 
_diffrn_source.voltage                     ? 
_diffrn_source.take-off_angle              ? 
_diffrn_source.pdbx_wavelength_list        0.92 
_diffrn_source.pdbx_wavelength             ? 
_diffrn_source.pdbx_synchrotron_beamline   I04-1 
_diffrn_source.pdbx_synchrotron_site       Diamond 
# 
_reflns.B_iso_Wilson_estimate                          ? 
_reflns.entry_id                                       9H7H 
_reflns.data_reduction_details                         ? 
_reflns.data_reduction_method                          ? 
_reflns.d_resolution_high                              1.47 
_reflns.d_resolution_low                               35.75 
_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                                     41047 
_reflns.observed_criterion                             ? 
_reflns.observed_criterion_F_max                       ? 
_reflns.observed_criterion_F_min                       ? 
_reflns.observed_criterion_I_max                       ? 
_reflns.observed_criterion_I_min                       ? 
_reflns.observed_criterion_sigma_F                     ? 
_reflns.observed_criterion_sigma_I                     ? 
_reflns.percent_possible_obs                           99.8 
_reflns.R_free_details                                 ? 
_reflns.Rmerge_F_all                                   ? 
_reflns.Rmerge_F_obs                                   ? 
_reflns.Friedel_coverage                               ? 
_reflns.number_gt                                      ? 
_reflns.threshold_expression                           ? 
_reflns.pdbx_redundancy                                12.8 
_reflns.pdbx_netI_over_av_sigmaI                       ? 
_reflns.pdbx_netI_over_sigmaI                          22.7 
_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                                0.017 
_reflns.pdbx_d_opt                                     ? 
_reflns.pdbx_number_measured_all                       ? 
_reflns.pdbx_diffrn_id                                 1 
_reflns.pdbx_ordinal                                   1 
_reflns.pdbx_CC_half                                   ? 
_reflns.pdbx_CC_star                                   ? 
_reflns.pdbx_R_split                                   ? 
_reflns.pdbx_Rmerge_I_obs                              0.055 
_reflns.pdbx_Rmerge_I_all                              ? 
_reflns.pdbx_Rsym_value                                ? 
_reflns.pdbx_CC_split_method                           ? 
_reflns.pdbx_aniso_diffraction_limit_axis_1_ortho[1]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_1_ortho[2]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_1_ortho[3]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_2_ortho[1]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_2_ortho[2]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_2_ortho[3]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_3_ortho[1]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_3_ortho[2]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_3_ortho[3]   ? 
_reflns.pdbx_aniso_diffraction_limit_1                 ? 
_reflns.pdbx_aniso_diffraction_limit_2                 ? 
_reflns.pdbx_aniso_diffraction_limit_3                 ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_1_ortho[1]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_1_ortho[2]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_1_ortho[3]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_2_ortho[1]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_2_ortho[2]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_2_ortho[3]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_3_ortho[1]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_3_ortho[2]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_3_ortho[3]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvalue_1               ? 
_reflns.pdbx_aniso_B_tensor_eigenvalue_2               ? 
_reflns.pdbx_aniso_B_tensor_eigenvalue_3               ? 
_reflns.pdbx_orthogonalization_convention              ? 
_reflns.pdbx_percent_possible_ellipsoidal              ? 
_reflns.pdbx_percent_possible_spherical                ? 
_reflns.pdbx_percent_possible_ellipsoidal_anomalous    ? 
_reflns.pdbx_percent_possible_spherical_anomalous      ? 
_reflns.pdbx_redundancy_anomalous                      ? 
_reflns.pdbx_CC_half_anomalous                         ? 
_reflns.pdbx_absDiff_over_sigma_anomalous              ? 
_reflns.pdbx_percent_possible_anomalous                ? 
_reflns.pdbx_observed_signal_threshold                 ? 
_reflns.pdbx_signal_type                               ? 
_reflns.pdbx_signal_details                            ? 
_reflns.pdbx_signal_software_id                        ? 
# 
_reflns_shell.d_res_high                                    1.47 
_reflns_shell.d_res_low                                     1.51 
_reflns_shell.meanI_over_sigI_all                           ? 
_reflns_shell.meanI_over_sigI_obs                           ? 
_reflns_shell.number_measured_all                           ? 
_reflns_shell.number_measured_obs                           ? 
_reflns_shell.number_possible                               ? 
_reflns_shell.number_unique_all                             ? 
_reflns_shell.number_unique_obs                             2973 
_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                               0.215 
_reflns_shell.pdbx_rejects                                  ? 
_reflns_shell.pdbx_ordinal                                  1 
_reflns_shell.pdbx_diffrn_id                                1 
_reflns_shell.pdbx_CC_half                                  ? 
_reflns_shell.pdbx_CC_star                                  ? 
_reflns_shell.pdbx_R_split                                  ? 
_reflns_shell.percent_possible_all                          ? 
_reflns_shell.Rmerge_I_all                                  ? 
_reflns_shell.Rmerge_I_obs                                  0.662 
_reflns_shell.pdbx_Rsym_value                               ? 
_reflns_shell.pdbx_percent_possible_ellipsoidal             ? 
_reflns_shell.pdbx_percent_possible_spherical               ? 
_reflns_shell.pdbx_percent_possible_ellipsoidal_anomalous   ? 
_reflns_shell.pdbx_percent_possible_spherical_anomalous     ? 
_reflns_shell.pdbx_redundancy_anomalous                     ? 
_reflns_shell.pdbx_CC_half_anomalous                        ? 
_reflns_shell.pdbx_absDiff_over_sigma_anomalous             ? 
_reflns_shell.pdbx_percent_possible_anomalous               ? 
# 
_refine.aniso_B[1][1]                            -0.08 
_refine.aniso_B[1][2]                            -0.00 
_refine.aniso_B[1][3]                            0.00 
_refine.aniso_B[2][2]                            0.22 
_refine.aniso_B[2][3]                            0.00 
_refine.aniso_B[3][3]                            -0.15 
_refine.B_iso_max                                ? 
_refine.B_iso_mean                               19.272 
_refine.B_iso_min                                ? 
_refine.correlation_coeff_Fo_to_Fc               0.969 
_refine.correlation_coeff_Fo_to_Fc_free          0.950 
_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                                 9H7H 
_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                            1.47 
_refine.ls_d_res_low                             35.75 
_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                     38944 
_refine.ls_number_reflns_R_free                  2059 
_refine.ls_number_reflns_R_work                  ? 
_refine.ls_number_restraints                     ? 
_refine.ls_percent_reflns_obs                    99.77 
_refine.ls_percent_reflns_R_free                 5.0 
_refine.ls_R_factor_all                          ? 
_refine.ls_R_factor_obs                          0.16441 
_refine.ls_R_factor_R_free                       0.21508 
_refine.ls_R_factor_R_free_error                 ? 
_refine.ls_R_factor_R_free_error_details         ? 
_refine.ls_R_factor_R_work                       0.16174 
_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                       0.069 
_refine.pdbx_overall_ESU_R_Free                  0.070 
_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                             2.299 
_refine.overall_SU_ML                            0.040 
_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                       1.47 
_refine_hist.d_res_low                        35.75 
_refine_hist.number_atoms_solvent             97 
_refine_hist.number_atoms_total               1792 
_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        1682 
_refine_hist.pdbx_number_atoms_nucleic_acid   0 
_refine_hist.pdbx_number_atoms_ligand         13 
_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' ? 0.019  0.019  1771 ? r_bond_refined_d             ? ? 
'X-RAY DIFFRACTION' ? 0.001  0.020  1590 ? r_bond_other_d               ? ? 
'X-RAY DIFFRACTION' ? 1.819  1.941  2437 ? r_angle_refined_deg          ? ? 
'X-RAY DIFFRACTION' ? 0.866  3.000  3664 ? r_angle_other_deg            ? ? 
'X-RAY DIFFRACTION' ? 5.857  5.000  235  ? r_dihedral_angle_1_deg       ? ? 
'X-RAY DIFFRACTION' ? 33.436 24.154 65   ? r_dihedral_angle_2_deg       ? ? 
'X-RAY DIFFRACTION' ? 12.846 15.000 246  ? r_dihedral_angle_3_deg       ? ? 
'X-RAY DIFFRACTION' ? 21.384 15.000 4    ? r_dihedral_angle_4_deg       ? ? 
'X-RAY DIFFRACTION' ? 0.117  0.200  288  ? r_chiral_restr               ? ? 
'X-RAY DIFFRACTION' ? 0.010  0.021  2015 ? r_gen_planes_refined         ? ? 
'X-RAY DIFFRACTION' ? 0.001  0.020  399  ? 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' ? 3.461  1.771  912  ? r_mcbond_it                  ? ? 
'X-RAY DIFFRACTION' ? 3.365  1.768  911  ? r_mcbond_other               ? ? 
'X-RAY DIFFRACTION' ? 3.977  2.654  1138 ? r_mcangle_it                 ? ? 
'X-RAY DIFFRACTION' ? 3.975  2.654  1139 ? r_mcangle_other              ? ? 
'X-RAY DIFFRACTION' ? 4.389  2.086  859  ? r_scbond_it                  ? ? 
'X-RAY DIFFRACTION' ? 4.387  2.086  860  ? r_scbond_other               ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?    ? r_scangle_it                 ? ? 
'X-RAY DIFFRACTION' ? 4.758  3.029  1293 ? r_scangle_other              ? ? 
'X-RAY DIFFRACTION' ? 4.677  15.503 1881 ? r_long_range_B_refined       ? ? 
'X-RAY DIFFRACTION' ? 4.675  15.509 1882 ? r_long_range_B_other         ? ? 
'X-RAY DIFFRACTION' ? 7.313  3.000  3359 ? r_rigid_bond_restr           ? ? 
'X-RAY DIFFRACTION' ? 17.515 5.000  32   ? r_sphericity_free            ? ? 
'X-RAY DIFFRACTION' ? 12.017 5.000  3374 ? r_sphericity_bonded          ? ? 
# 
_refine_ls_shell.pdbx_refine_id                   'X-RAY DIFFRACTION' 
_refine_ls_shell.d_res_high                       1.470 
_refine_ls_shell.d_res_low                        1.508 
_refine_ls_shell.number_reflns_all                ? 
_refine_ls_shell.number_reflns_obs                ? 
_refine_ls_shell.number_reflns_R_free             146 
_refine_ls_shell.number_reflns_R_work             2822 
_refine_ls_shell.percent_reflns_obs               99.80 
_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                  0.232 
_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                  0.324 
# 
_struct.entry_id                     9H7H 
_struct.title                        'Human Transthyretin in Complex with Isoquinolin-3-amine' 
_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        9H7H 
_struct_keywords.text            'Amyloidosis, Retinol, Thyroxine, RBP, 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 4 ? 
G N N 4 ? 
# 
_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 9H7H A 1 ? 127 ? P02766 21 ? 147 ? 1 127 
2 1 9H7H B 1 ? 127 ? P02766 21 ? 147 ? 1 127 
# 
_pdbx_struct_assembly.id                   1 
_pdbx_struct_assembly.details              author_defined_assembly 
_pdbx_struct_assembly.method_details       ? 
_pdbx_struct_assembly.oligomeric_details   dimeric 
_pdbx_struct_assembly.oligomeric_count     2 
# 
loop_
_pdbx_struct_assembly_prop.biol_id 
_pdbx_struct_assembly_prop.type 
_pdbx_struct_assembly_prop.value 
_pdbx_struct_assembly_prop.details 
1 'ABSA (A^2)' 1850  ? 
1 MORE         -21   ? 
1 'SSA (A^2)'  10780 ? 
# 
_pdbx_struct_assembly_gen.assembly_id       1 
_pdbx_struct_assembly_gen.oper_expression   1 
_pdbx_struct_assembly_gen.asym_id_list      A,B,C,D,E,F,G 
# 
_pdbx_struct_oper_list.id                   1 
_pdbx_struct_oper_list.type                 'identity operation' 
_pdbx_struct_oper_list.name                 1_555 
_pdbx_struct_oper_list.symmetry_operation   x,y,z 
_pdbx_struct_oper_list.matrix[1][1]         1.0000000000 
_pdbx_struct_oper_list.matrix[1][2]         0.0000000000 
_pdbx_struct_oper_list.matrix[1][3]         0.0000000000 
_pdbx_struct_oper_list.vector[1]            0.0000000000 
_pdbx_struct_oper_list.matrix[2][1]         0.0000000000 
_pdbx_struct_oper_list.matrix[2][2]         1.0000000000 
_pdbx_struct_oper_list.matrix[2][3]         0.0000000000 
_pdbx_struct_oper_list.vector[2]            0.0000000000 
_pdbx_struct_oper_list.matrix[3][1]         0.0000000000 
_pdbx_struct_oper_list.matrix[3][2]         0.0000000000 
_pdbx_struct_oper_list.matrix[3][3]         1.0000000000 
_pdbx_struct_oper_list.vector[3]            0.0000000000 
# 
loop_
_struct_conf.conf_type_id 
_struct_conf.id 
_struct_conf.pdbx_PDB_helix_id 
_struct_conf.beg_label_comp_id 
_struct_conf.beg_label_asym_id 
_struct_conf.beg_label_seq_id 
_struct_conf.pdbx_beg_PDB_ins_code 
_struct_conf.end_label_comp_id 
_struct_conf.end_label_asym_id 
_struct_conf.end_label_seq_id 
_struct_conf.pdbx_end_PDB_ins_code 
_struct_conf.beg_auth_comp_id 
_struct_conf.beg_auth_asym_id 
_struct_conf.beg_auth_seq_id 
_struct_conf.end_auth_comp_id 
_struct_conf.end_auth_asym_id 
_struct_conf.end_auth_seq_id 
_struct_conf.pdbx_PDB_helix_class 
_struct_conf.details 
_struct_conf.pdbx_PDB_helix_length 
HELX_P HELX_P1 AA1 ASP A 74 ? LEU A 82 ? ASP A 74 LEU A 82 1 ? 9 
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 
metalc1  metalc ? ? A GLU 66 OE2 ? ? ? 1_555 C CA  . CA ? ? A GLU 66  A CA  201 1_555 ? ? ? ? ? ? ? 2.492 ? ? 
metalc2  metalc ? ? A ASP 99 O   ? ? ? 1_555 C CA  . CA ? ? A ASP 99  A CA  201 1_555 ? ? ? ? ? ? ? 2.630 ? ? 
metalc3  metalc ? ? A ASP 99 OD1 ? ? ? 1_555 C CA  . CA ? ? A ASP 99  A CA  201 1_555 ? ? ? ? ? ? ? 2.531 ? ? 
metalc4  metalc ? ? C CA  .  CA  ? ? ? 1_555 F HOH . O  ? ? A CA  201 A HOH 326 3_445 ? ? ? ? ? ? ? 2.210 ? ? 
metalc5  metalc ? ? C CA  .  CA  ? ? ? 1_555 F HOH . O  ? ? A CA  201 A HOH 336 3_445 ? ? ? ? ? ? ? 2.213 ? ? 
metalc6  metalc ? ? C CA  .  CA  ? ? ? 1_555 F HOH . O  ? ? A CA  201 A HOH 348 1_555 ? ? ? ? ? ? ? 3.041 ? ? 
metalc7  metalc ? ? C CA  .  CA  ? ? ? 1_555 F HOH . O  ? ? A CA  201 A HOH 352 1_555 ? ? ? ? ? ? ? 2.649 ? ? 
metalc8  metalc ? ? B GLU 66 OE2 ? ? ? 1_555 D CA  . CA ? ? B GLU 66  B CA  201 3_454 ? ? ? ? ? ? ? 2.877 ? ? 
metalc9  metalc ? ? B ASN 98 OD1 ? ? ? 1_555 D CA  . CA ? ? B ASN 98  B CA  201 3_454 ? ? ? ? ? ? ? 2.719 ? ? 
metalc10 metalc ? ? D CA  .  CA  ? ? ? 1_555 G HOH . O  ? ? B CA  201 B HOH 301 1_555 ? ? ? ? ? ? ? 2.209 ? ? 
metalc11 metalc ? ? D CA  .  CA  ? ? ? 1_555 G HOH . O  ? ? B CA  201 B HOH 308 1_555 ? ? ? ? ? ? ? 2.553 ? ? 
# 
_struct_conn_type.id          metalc 
_struct_conn_type.criteria    ? 
_struct_conn_type.reference   ? 
# 
loop_
_pdbx_struct_conn_angle.id 
_pdbx_struct_conn_angle.ptnr1_label_atom_id 
_pdbx_struct_conn_angle.ptnr1_label_alt_id 
_pdbx_struct_conn_angle.ptnr1_label_asym_id 
_pdbx_struct_conn_angle.ptnr1_label_comp_id 
_pdbx_struct_conn_angle.ptnr1_label_seq_id 
_pdbx_struct_conn_angle.ptnr1_auth_atom_id 
_pdbx_struct_conn_angle.ptnr1_auth_asym_id 
_pdbx_struct_conn_angle.ptnr1_auth_comp_id 
_pdbx_struct_conn_angle.ptnr1_auth_seq_id 
_pdbx_struct_conn_angle.ptnr1_PDB_ins_code 
_pdbx_struct_conn_angle.ptnr1_symmetry 
_pdbx_struct_conn_angle.ptnr2_label_atom_id 
_pdbx_struct_conn_angle.ptnr2_label_alt_id 
_pdbx_struct_conn_angle.ptnr2_label_asym_id 
_pdbx_struct_conn_angle.ptnr2_label_comp_id 
_pdbx_struct_conn_angle.ptnr2_label_seq_id 
_pdbx_struct_conn_angle.ptnr2_auth_atom_id 
_pdbx_struct_conn_angle.ptnr2_auth_asym_id 
_pdbx_struct_conn_angle.ptnr2_auth_comp_id 
_pdbx_struct_conn_angle.ptnr2_auth_seq_id 
_pdbx_struct_conn_angle.ptnr2_PDB_ins_code 
_pdbx_struct_conn_angle.ptnr2_symmetry 
_pdbx_struct_conn_angle.ptnr3_label_atom_id 
_pdbx_struct_conn_angle.ptnr3_label_alt_id 
_pdbx_struct_conn_angle.ptnr3_label_asym_id 
_pdbx_struct_conn_angle.ptnr3_label_comp_id 
_pdbx_struct_conn_angle.ptnr3_label_seq_id 
_pdbx_struct_conn_angle.ptnr3_auth_atom_id 
_pdbx_struct_conn_angle.ptnr3_auth_asym_id 
_pdbx_struct_conn_angle.ptnr3_auth_comp_id 
_pdbx_struct_conn_angle.ptnr3_auth_seq_id 
_pdbx_struct_conn_angle.ptnr3_PDB_ins_code 
_pdbx_struct_conn_angle.ptnr3_symmetry 
_pdbx_struct_conn_angle.value 
_pdbx_struct_conn_angle.value_esd 
1  OE2 ? A GLU 66 ? A GLU 66  ? 1_555 CA ? C CA . ? A CA 201 ? 1_555 O   ? A ASP 99 ? A ASP 99  ? 1_555 98.1  ? 
2  OE2 ? A GLU 66 ? A GLU 66  ? 1_555 CA ? C CA . ? A CA 201 ? 1_555 OD1 ? A ASP 99 ? A ASP 99  ? 1_555 78.9  ? 
3  O   ? A ASP 99 ? A ASP 99  ? 1_555 CA ? C CA . ? A CA 201 ? 1_555 OD1 ? A ASP 99 ? A ASP 99  ? 1_555 67.8  ? 
4  OE2 ? A GLU 66 ? A GLU 66  ? 1_555 CA ? C CA . ? A CA 201 ? 1_555 O   ? F HOH .  ? A HOH 326 ? 3_445 112.7 ? 
5  O   ? A ASP 99 ? A ASP 99  ? 1_555 CA ? C CA . ? A CA 201 ? 1_555 O   ? F HOH .  ? A HOH 326 ? 3_445 124.6 ? 
6  OD1 ? A ASP 99 ? A ASP 99  ? 1_555 CA ? C CA . ? A CA 201 ? 1_555 O   ? F HOH .  ? A HOH 326 ? 3_445 159.0 ? 
7  OE2 ? A GLU 66 ? A GLU 66  ? 1_555 CA ? C CA . ? A CA 201 ? 1_555 O   ? F HOH .  ? A HOH 336 ? 3_445 168.3 ? 
8  O   ? A ASP 99 ? A ASP 99  ? 1_555 CA ? C CA . ? A CA 201 ? 1_555 O   ? F HOH .  ? A HOH 336 ? 3_445 80.7  ? 
9  OD1 ? A ASP 99 ? A ASP 99  ? 1_555 CA ? C CA . ? A CA 201 ? 1_555 O   ? F HOH .  ? A HOH 336 ? 3_445 89.9  ? 
10 O   ? F HOH .  ? A HOH 326 ? 3_445 CA ? C CA . ? A CA 201 ? 1_555 O   ? F HOH .  ? A HOH 336 ? 3_445 76.9  ? 
11 OE2 ? A GLU 66 ? A GLU 66  ? 1_555 CA ? C CA . ? A CA 201 ? 1_555 O   ? F HOH .  ? A HOH 348 ? 1_555 74.3  ? 
12 O   ? A ASP 99 ? A ASP 99  ? 1_555 CA ? C CA . ? A CA 201 ? 1_555 O   ? F HOH .  ? A HOH 348 ? 1_555 65.5  ? 
13 OD1 ? A ASP 99 ? A ASP 99  ? 1_555 CA ? C CA . ? A CA 201 ? 1_555 O   ? F HOH .  ? A HOH 348 ? 1_555 121.1 ? 
14 O   ? F HOH .  ? A HOH 326 ? 3_445 CA ? C CA . ? A CA 201 ? 1_555 O   ? F HOH .  ? A HOH 348 ? 1_555 79.6  ? 
15 O   ? F HOH .  ? A HOH 336 ? 3_445 CA ? C CA . ? A CA 201 ? 1_555 O   ? F HOH .  ? A HOH 348 ? 1_555 115.1 ? 
16 OE2 ? A GLU 66 ? A GLU 66  ? 1_555 CA ? C CA . ? A CA 201 ? 1_555 O   ? F HOH .  ? A HOH 352 ? 1_555 92.2  ? 
17 O   ? A ASP 99 ? A ASP 99  ? 1_555 CA ? C CA . ? A CA 201 ? 1_555 O   ? F HOH .  ? A HOH 352 ? 1_555 145.5 ? 
18 OD1 ? A ASP 99 ? A ASP 99  ? 1_555 CA ? C CA . ? A CA 201 ? 1_555 O   ? F HOH .  ? A HOH 352 ? 1_555 82.1  ? 
19 O   ? F HOH .  ? A HOH 326 ? 3_445 CA ? C CA . ? A CA 201 ? 1_555 O   ? F HOH .  ? A HOH 352 ? 1_555 80.1  ? 
20 O   ? F HOH .  ? A HOH 336 ? 3_445 CA ? C CA . ? A CA 201 ? 1_555 O   ? F HOH .  ? A HOH 352 ? 1_555 82.7  ? 
21 O   ? F HOH .  ? A HOH 348 ? 1_555 CA ? C CA . ? A CA 201 ? 1_555 O   ? F HOH .  ? A HOH 352 ? 1_555 148.8 ? 
22 OE2 ? B GLU 66 ? B GLU 66  ? 1_555 CA ? D CA . ? B CA 201 ? 3_454 OD1 ? B ASN 98 ? B ASN 98  ? 1_555 63.3  ? 
23 OE2 ? B GLU 66 ? B GLU 66  ? 1_555 CA ? D CA . ? B CA 201 ? 3_454 O   ? G HOH .  ? B HOH 301 ? 1_555 17.9  ? 
24 OD1 ? B ASN 98 ? B ASN 98  ? 1_555 CA ? D CA . ? B CA 201 ? 3_454 O   ? G HOH .  ? B HOH 301 ? 1_555 61.7  ? 
25 OE2 ? B GLU 66 ? B GLU 66  ? 1_555 CA ? D CA . ? B CA 201 ? 3_454 O   ? G HOH .  ? B HOH 308 ? 1_555 22.3  ? 
26 OD1 ? B ASN 98 ? B ASN 98  ? 1_555 CA ? D CA . ? B CA 201 ? 3_454 O   ? G HOH .  ? B HOH 308 ? 1_555 69.5  ? 
27 O   ? G HOH .  ? B HOH 301 ? 1_555 CA ? D CA . ? B CA 201 ? 3_454 O   ? G HOH .  ? B HOH 308 ? 1_555 8.3   ? 
# 
loop_
_struct_sheet.id 
_struct_sheet.type 
_struct_sheet.number_strands 
_struct_sheet.details 
AA1 ? 8 ? 
AA2 ? 8 ? 
AA3 ? 4 ? 
AA4 ? 4 ? 
# 
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 
AA4 1 2 ? anti-parallel 
AA4 2 3 ? anti-parallel 
AA4 3 4 ? 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 ? VAL B 122 ? SER B 115 VAL B 122 
AA1 6 TYR B 105 ? SER B 112 ? TYR B 105 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 ? VAL B 122 ? SER B 115 VAL B 122 
AA2 6 TYR B 105 ? SER B 112 ? TYR B 105 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 ALA A 91  ? ALA A 97  ? ALA A 91  ALA A 97  
AA4 1 TRP B 41  ? LYS B 48  ? TRP B 41  LYS B 48  
AA4 2 ALA B 29  ? LYS B 35  ? ALA B 29  LYS B 35  
AA4 3 GLY B 67  ? ILE B 73  ? GLY B 67  ILE B 73  
AA4 4 ALA B 91  ? ALA B 97  ? ALA B 91  ALA B 97  
# 
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 LEU A 17  ? N LEU A 17  O LEU A 111 ? O LEU A 111 
AA1 3 4 N ARG A 104 ? N ARG A 104 O THR A 123 ? O THR A 123 
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 LEU A 17  ? N LEU A 17  O LEU A 111 ? O LEU A 111 
AA2 3 4 N ARG A 104 ? N ARG A 104 O THR A 123 ? O THR A 123 
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  
AA4 1 2 O ALA B 45  ? O ALA B 45  N VAL B 32  ? N VAL B 32  
AA4 2 3 N HIS B 31  ? N HIS B 31  O GLU B 72  ? O GLU B 72  
AA4 3 4 N ILE B 73  ? N ILE B 73  O ALA B 91  ? O ALA B 91  
# 
_pdbx_entry_details.entry_id                   9H7H 
_pdbx_entry_details.nonpolymer_details         ? 
_pdbx_entry_details.sequence_details           ? 
_pdbx_entry_details.compound_details           ? 
_pdbx_entry_details.source_details             ? 
_pdbx_entry_details.has_ligand_of_interest     Y 
_pdbx_entry_details.has_protein_modification   N 
# 
_pdbx_validate_rmsd_angle.id                         1 
_pdbx_validate_rmsd_angle.PDB_model_num              1 
_pdbx_validate_rmsd_angle.auth_atom_id_1             CB 
_pdbx_validate_rmsd_angle.auth_asym_id_1             B 
_pdbx_validate_rmsd_angle.auth_comp_id_1             MET 
_pdbx_validate_rmsd_angle.auth_seq_id_1              13 
_pdbx_validate_rmsd_angle.PDB_ins_code_1             ? 
_pdbx_validate_rmsd_angle.label_alt_id_1             ? 
_pdbx_validate_rmsd_angle.auth_atom_id_2             CG 
_pdbx_validate_rmsd_angle.auth_asym_id_2             B 
_pdbx_validate_rmsd_angle.auth_comp_id_2             MET 
_pdbx_validate_rmsd_angle.auth_seq_id_2              13 
_pdbx_validate_rmsd_angle.PDB_ins_code_2             ? 
_pdbx_validate_rmsd_angle.label_alt_id_2             ? 
_pdbx_validate_rmsd_angle.auth_atom_id_3             SD 
_pdbx_validate_rmsd_angle.auth_asym_id_3             B 
_pdbx_validate_rmsd_angle.auth_comp_id_3             MET 
_pdbx_validate_rmsd_angle.auth_seq_id_3              13 
_pdbx_validate_rmsd_angle.PDB_ins_code_3             ? 
_pdbx_validate_rmsd_angle.label_alt_id_3             ? 
_pdbx_validate_rmsd_angle.angle_value                90.45 
_pdbx_validate_rmsd_angle.angle_target_value         112.40 
_pdbx_validate_rmsd_angle.angle_deviation            -21.95 
_pdbx_validate_rmsd_angle.angle_standard_deviation   3.00 
_pdbx_validate_rmsd_angle.linker_flag                N 
# 
loop_
_pdbx_struct_special_symmetry.id 
_pdbx_struct_special_symmetry.PDB_model_num 
_pdbx_struct_special_symmetry.auth_asym_id 
_pdbx_struct_special_symmetry.auth_comp_id 
_pdbx_struct_special_symmetry.auth_seq_id 
_pdbx_struct_special_symmetry.PDB_ins_code 
_pdbx_struct_special_symmetry.label_asym_id 
_pdbx_struct_special_symmetry.label_comp_id 
_pdbx_struct_special_symmetry.label_seq_id 
1 1 A HOH 330 ? F HOH . 
2 1 B HOH 304 ? G HOH . 
# 
loop_
_pdbx_distant_solvent_atoms.id 
_pdbx_distant_solvent_atoms.PDB_model_num 
_pdbx_distant_solvent_atoms.auth_atom_id 
_pdbx_distant_solvent_atoms.label_alt_id 
_pdbx_distant_solvent_atoms.auth_asym_id 
_pdbx_distant_solvent_atoms.auth_comp_id 
_pdbx_distant_solvent_atoms.auth_seq_id 
_pdbx_distant_solvent_atoms.PDB_ins_code 
_pdbx_distant_solvent_atoms.neighbor_macromolecule_distance 
_pdbx_distant_solvent_atoms.neighbor_ligand_distance 
1 1 O ? A HOH 363 ? 6.57 . 
2 1 O ? B HOH 334 ? 6.13 . 
# 
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 SER 100 ? B SER 100 
23 1 Y 1 B GLY 101 ? B GLY 101 
24 1 Y 1 B PRO 102 ? B PRO 102 
25 1 Y 1 B ARG 103 ? B ARG 103 
26 1 Y 1 B PRO 125 ? B PRO 125 
27 1 Y 1 B LYS 126 ? B LYS 126 
28 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 
ALA N    N  N N 1   
ALA CA   C  N S 2   
ALA C    C  N N 3   
ALA O    O  N N 4   
ALA CB   C  N N 5   
ALA OXT  O  N N 6   
ALA H    H  N N 7   
ALA H2   H  N N 8   
ALA HA   H  N N 9   
ALA HB1  H  N N 10  
ALA HB2  H  N N 11  
ALA HB3  H  N N 12  
ALA HXT  H  N N 13  
ARG N    N  N N 14  
ARG CA   C  N S 15  
ARG C    C  N N 16  
ARG O    O  N N 17  
ARG CB   C  N N 18  
ARG CG   C  N N 19  
ARG CD   C  N N 20  
ARG NE   N  N N 21  
ARG CZ   C  N N 22  
ARG NH1  N  N N 23  
ARG NH2  N  N N 24  
ARG OXT  O  N N 25  
ARG H    H  N N 26  
ARG H2   H  N N 27  
ARG HA   H  N N 28  
ARG HB2  H  N N 29  
ARG HB3  H  N N 30  
ARG HG2  H  N N 31  
ARG HG3  H  N N 32  
ARG HD2  H  N N 33  
ARG HD3  H  N N 34  
ARG HE   H  N N 35  
ARG HH11 H  N N 36  
ARG HH12 H  N N 37  
ARG HH21 H  N N 38  
ARG HH22 H  N N 39  
ARG HXT  H  N N 40  
ASN N    N  N N 41  
ASN CA   C  N S 42  
ASN C    C  N N 43  
ASN O    O  N N 44  
ASN CB   C  N N 45  
ASN CG   C  N N 46  
ASN OD1  O  N N 47  
ASN ND2  N  N N 48  
ASN OXT  O  N N 49  
ASN H    H  N N 50  
ASN H2   H  N N 51  
ASN HA   H  N N 52  
ASN HB2  H  N N 53  
ASN HB3  H  N N 54  
ASN HD21 H  N N 55  
ASN HD22 H  N N 56  
ASN HXT  H  N N 57  
ASP N    N  N N 58  
ASP CA   C  N S 59  
ASP C    C  N N 60  
ASP O    O  N N 61  
ASP CB   C  N N 62  
ASP CG   C  N N 63  
ASP OD1  O  N N 64  
ASP OD2  O  N N 65  
ASP OXT  O  N N 66  
ASP H    H  N N 67  
ASP H2   H  N N 68  
ASP HA   H  N N 69  
ASP HB2  H  N N 70  
ASP HB3  H  N N 71  
ASP HD2  H  N N 72  
ASP HXT  H  N N 73  
CA  CA   CA N N 74  
CYS N    N  N N 75  
CYS CA   C  N R 76  
CYS C    C  N N 77  
CYS O    O  N N 78  
CYS CB   C  N N 79  
CYS SG   S  N N 80  
CYS OXT  O  N N 81  
CYS H    H  N N 82  
CYS H2   H  N N 83  
CYS HA   H  N N 84  
CYS HB2  H  N N 85  
CYS HB3  H  N N 86  
CYS HG   H  N N 87  
CYS HXT  H  N N 88  
GLU N    N  N N 89  
GLU CA   C  N S 90  
GLU C    C  N N 91  
GLU O    O  N N 92  
GLU CB   C  N N 93  
GLU CG   C  N N 94  
GLU CD   C  N N 95  
GLU OE1  O  N N 96  
GLU OE2  O  N N 97  
GLU OXT  O  N N 98  
GLU H    H  N N 99  
GLU H2   H  N N 100 
GLU HA   H  N N 101 
GLU HB2  H  N N 102 
GLU HB3  H  N N 103 
GLU HG2  H  N N 104 
GLU HG3  H  N N 105 
GLU HE2  H  N N 106 
GLU HXT  H  N N 107 
GLY N    N  N N 108 
GLY CA   C  N N 109 
GLY C    C  N N 110 
GLY O    O  N N 111 
GLY OXT  O  N N 112 
GLY H    H  N N 113 
GLY H2   H  N N 114 
GLY HA2  H  N N 115 
GLY HA3  H  N N 116 
GLY HXT  H  N N 117 
HIS N    N  N N 118 
HIS CA   C  N S 119 
HIS C    C  N N 120 
HIS O    O  N N 121 
HIS CB   C  N N 122 
HIS CG   C  Y N 123 
HIS ND1  N  Y N 124 
HIS CD2  C  Y N 125 
HIS CE1  C  Y N 126 
HIS NE2  N  Y N 127 
HIS OXT  O  N N 128 
HIS H    H  N N 129 
HIS H2   H  N N 130 
HIS HA   H  N N 131 
HIS HB2  H  N N 132 
HIS HB3  H  N N 133 
HIS HD1  H  N N 134 
HIS HD2  H  N N 135 
HIS HE1  H  N N 136 
HIS HE2  H  N N 137 
HIS HXT  H  N N 138 
HOH O    O  N N 139 
HOH H1   H  N N 140 
HOH H2   H  N N 141 
ILE N    N  N N 142 
ILE CA   C  N S 143 
ILE C    C  N N 144 
ILE O    O  N N 145 
ILE CB   C  N S 146 
ILE CG1  C  N N 147 
ILE CG2  C  N N 148 
ILE CD1  C  N N 149 
ILE OXT  O  N N 150 
ILE H    H  N N 151 
ILE H2   H  N N 152 
ILE HA   H  N N 153 
ILE HB   H  N N 154 
ILE HG12 H  N N 155 
ILE HG13 H  N N 156 
ILE HG21 H  N N 157 
ILE HG22 H  N N 158 
ILE HG23 H  N N 159 
ILE HD11 H  N N 160 
ILE HD12 H  N N 161 
ILE HD13 H  N N 162 
ILE HXT  H  N N 163 
LEU N    N  N N 164 
LEU CA   C  N S 165 
LEU C    C  N N 166 
LEU O    O  N N 167 
LEU CB   C  N N 168 
LEU CG   C  N N 169 
LEU CD1  C  N N 170 
LEU CD2  C  N N 171 
LEU OXT  O  N N 172 
LEU H    H  N N 173 
LEU H2   H  N N 174 
LEU HA   H  N N 175 
LEU HB2  H  N N 176 
LEU HB3  H  N N 177 
LEU HG   H  N N 178 
LEU HD11 H  N N 179 
LEU HD12 H  N N 180 
LEU HD13 H  N N 181 
LEU HD21 H  N N 182 
LEU HD22 H  N N 183 
LEU HD23 H  N N 184 
LEU HXT  H  N N 185 
LYS N    N  N N 186 
LYS CA   C  N S 187 
LYS C    C  N N 188 
LYS O    O  N N 189 
LYS CB   C  N N 190 
LYS CG   C  N N 191 
LYS CD   C  N N 192 
LYS CE   C  N N 193 
LYS NZ   N  N N 194 
LYS OXT  O  N N 195 
LYS H    H  N N 196 
LYS H2   H  N N 197 
LYS HA   H  N N 198 
LYS HB2  H  N N 199 
LYS HB3  H  N N 200 
LYS HG2  H  N N 201 
LYS HG3  H  N N 202 
LYS HD2  H  N N 203 
LYS HD3  H  N N 204 
LYS HE2  H  N N 205 
LYS HE3  H  N N 206 
LYS HZ1  H  N N 207 
LYS HZ2  H  N N 208 
LYS HZ3  H  N N 209 
LYS HXT  H  N N 210 
MET N    N  N N 211 
MET CA   C  N S 212 
MET C    C  N N 213 
MET O    O  N N 214 
MET CB   C  N N 215 
MET CG   C  N N 216 
MET SD   S  N N 217 
MET CE   C  N N 218 
MET OXT  O  N N 219 
MET H    H  N N 220 
MET H2   H  N N 221 
MET HA   H  N N 222 
MET HB2  H  N N 223 
MET HB3  H  N N 224 
MET HG2  H  N N 225 
MET HG3  H  N N 226 
MET HE1  H  N N 227 
MET HE2  H  N N 228 
MET HE3  H  N N 229 
MET HXT  H  N N 230 
PHE N    N  N N 231 
PHE CA   C  N S 232 
PHE C    C  N N 233 
PHE O    O  N N 234 
PHE CB   C  N N 235 
PHE CG   C  Y N 236 
PHE CD1  C  Y N 237 
PHE CD2  C  Y N 238 
PHE CE1  C  Y N 239 
PHE CE2  C  Y N 240 
PHE CZ   C  Y N 241 
PHE OXT  O  N N 242 
PHE H    H  N N 243 
PHE H2   H  N N 244 
PHE HA   H  N N 245 
PHE HB2  H  N N 246 
PHE HB3  H  N N 247 
PHE HD1  H  N N 248 
PHE HD2  H  N N 249 
PHE HE1  H  N N 250 
PHE HE2  H  N N 251 
PHE HZ   H  N N 252 
PHE HXT  H  N N 253 
PRO N    N  N N 254 
PRO CA   C  N S 255 
PRO C    C  N N 256 
PRO O    O  N N 257 
PRO CB   C  N N 258 
PRO CG   C  N N 259 
PRO CD   C  N N 260 
PRO OXT  O  N N 261 
PRO H    H  N N 262 
PRO HA   H  N N 263 
PRO HB2  H  N N 264 
PRO HB3  H  N N 265 
PRO HG2  H  N N 266 
PRO HG3  H  N N 267 
PRO HD2  H  N N 268 
PRO HD3  H  N N 269 
PRO HXT  H  N N 270 
SER N    N  N N 271 
SER CA   C  N S 272 
SER C    C  N N 273 
SER O    O  N N 274 
SER CB   C  N N 275 
SER OG   O  N N 276 
SER OXT  O  N N 277 
SER H    H  N N 278 
SER H2   H  N N 279 
SER HA   H  N N 280 
SER HB2  H  N N 281 
SER HB3  H  N N 282 
SER HG   H  N N 283 
SER HXT  H  N N 284 
THR N    N  N N 285 
THR CA   C  N S 286 
THR C    C  N N 287 
THR O    O  N N 288 
THR CB   C  N R 289 
THR OG1  O  N N 290 
THR CG2  C  N N 291 
THR OXT  O  N N 292 
THR H    H  N N 293 
THR H2   H  N N 294 
THR HA   H  N N 295 
THR HB   H  N N 296 
THR HG1  H  N N 297 
THR HG21 H  N N 298 
THR HG22 H  N N 299 
THR HG23 H  N N 300 
THR HXT  H  N N 301 
TRP N    N  N N 302 
TRP CA   C  N S 303 
TRP C    C  N N 304 
TRP O    O  N N 305 
TRP CB   C  N N 306 
TRP CG   C  Y N 307 
TRP CD1  C  Y N 308 
TRP CD2  C  Y N 309 
TRP NE1  N  Y N 310 
TRP CE2  C  Y N 311 
TRP CE3  C  Y N 312 
TRP CZ2  C  Y N 313 
TRP CZ3  C  Y N 314 
TRP CH2  C  Y N 315 
TRP OXT  O  N N 316 
TRP H    H  N N 317 
TRP H2   H  N N 318 
TRP HA   H  N N 319 
TRP HB2  H  N N 320 
TRP HB3  H  N N 321 
TRP HD1  H  N N 322 
TRP HE1  H  N N 323 
TRP HE3  H  N N 324 
TRP HZ2  H  N N 325 
TRP HZ3  H  N N 326 
TRP HH2  H  N N 327 
TRP HXT  H  N N 328 
TYR N    N  N N 329 
TYR CA   C  N S 330 
TYR C    C  N N 331 
TYR O    O  N N 332 
TYR CB   C  N N 333 
TYR CG   C  Y N 334 
TYR CD1  C  Y N 335 
TYR CD2  C  Y N 336 
TYR CE1  C  Y N 337 
TYR CE2  C  Y N 338 
TYR CZ   C  Y N 339 
TYR OH   O  N N 340 
TYR OXT  O  N N 341 
TYR H    H  N N 342 
TYR H2   H  N N 343 
TYR HA   H  N N 344 
TYR HB2  H  N N 345 
TYR HB3  H  N N 346 
TYR HD1  H  N N 347 
TYR HD2  H  N N 348 
TYR HE1  H  N N 349 
TYR HE2  H  N N 350 
TYR HH   H  N N 351 
TYR HXT  H  N N 352 
VAL N    N  N N 353 
VAL CA   C  N S 354 
VAL C    C  N N 355 
VAL O    O  N N 356 
VAL CB   C  N N 357 
VAL CG1  C  N N 358 
VAL CG2  C  N N 359 
VAL OXT  O  N N 360 
VAL H    H  N N 361 
VAL H2   H  N N 362 
VAL HA   H  N N 363 
VAL HB   H  N N 364 
VAL HG11 H  N N 365 
VAL HG12 H  N N 366 
VAL HG13 H  N N 367 
VAL HG21 H  N N 368 
VAL HG22 H  N N 369 
VAL HG23 H  N N 370 
VAL HXT  H  N N 371 
WLX C10  C  Y N 372 
WLX C11  C  Y N 373 
WLX N1   N  Y N 374 
WLX C2   C  Y N 375 
WLX C3   C  Y N 376 
WLX C4   C  Y N 377 
WLX C5   C  Y N 378 
WLX C6   C  Y N 379 
WLX N7   N  N N 380 
WLX C8   C  Y N 381 
WLX C9   C  Y N 382 
WLX H18  H  N N 383 
WLX H19  H  N N 384 
WLX H12  H  N N 385 
WLX H13  H  N N 386 
WLX H15  H  N N 387 
WLX H14  H  N N 388 
WLX H16  H  N N 389 
WLX H17  H  N N 390 
# 
loop_
_chem_comp_bond.comp_id 
_chem_comp_bond.atom_id_1 
_chem_comp_bond.atom_id_2 
_chem_comp_bond.value_order 
_chem_comp_bond.pdbx_aromatic_flag 
_chem_comp_bond.pdbx_stereo_config 
_chem_comp_bond.pdbx_ordinal 
ALA N   CA   sing N N 1   
ALA N   H    sing N N 2   
ALA N   H2   sing N N 3   
ALA CA  C    sing N N 4   
ALA CA  CB   sing N N 5   
ALA CA  HA   sing N N 6   
ALA C   O    doub N N 7   
ALA C   OXT  sing N N 8   
ALA CB  HB1  sing N N 9   
ALA CB  HB2  sing N N 10  
ALA CB  HB3  sing N N 11  
ALA OXT HXT  sing N N 12  
ARG N   CA   sing N N 13  
ARG N   H    sing N N 14  
ARG N   H2   sing N N 15  
ARG CA  C    sing N N 16  
ARG CA  CB   sing N N 17  
ARG CA  HA   sing N N 18  
ARG C   O    doub N N 19  
ARG C   OXT  sing N N 20  
ARG CB  CG   sing N N 21  
ARG CB  HB2  sing N N 22  
ARG CB  HB3  sing N N 23  
ARG CG  CD   sing N N 24  
ARG CG  HG2  sing N N 25  
ARG CG  HG3  sing N N 26  
ARG CD  NE   sing N N 27  
ARG CD  HD2  sing N N 28  
ARG CD  HD3  sing N N 29  
ARG NE  CZ   sing N N 30  
ARG NE  HE   sing N N 31  
ARG CZ  NH1  sing N N 32  
ARG CZ  NH2  doub N N 33  
ARG NH1 HH11 sing N N 34  
ARG NH1 HH12 sing N N 35  
ARG NH2 HH21 sing N N 36  
ARG NH2 HH22 sing N N 37  
ARG OXT HXT  sing N N 38  
ASN N   CA   sing N N 39  
ASN N   H    sing N N 40  
ASN N   H2   sing N N 41  
ASN CA  C    sing N N 42  
ASN CA  CB   sing N N 43  
ASN CA  HA   sing N N 44  
ASN C   O    doub N N 45  
ASN C   OXT  sing N N 46  
ASN CB  CG   sing N N 47  
ASN CB  HB2  sing N N 48  
ASN CB  HB3  sing N N 49  
ASN CG  OD1  doub N N 50  
ASN CG  ND2  sing N N 51  
ASN ND2 HD21 sing N N 52  
ASN ND2 HD22 sing N N 53  
ASN OXT HXT  sing N N 54  
ASP N   CA   sing N N 55  
ASP N   H    sing N N 56  
ASP N   H2   sing N N 57  
ASP CA  C    sing N N 58  
ASP CA  CB   sing N N 59  
ASP CA  HA   sing N N 60  
ASP C   O    doub N N 61  
ASP C   OXT  sing N N 62  
ASP CB  CG   sing N N 63  
ASP CB  HB2  sing N N 64  
ASP CB  HB3  sing N N 65  
ASP CG  OD1  doub N N 66  
ASP CG  OD2  sing N N 67  
ASP OD2 HD2  sing N N 68  
ASP OXT HXT  sing N N 69  
CYS N   CA   sing N N 70  
CYS N   H    sing N N 71  
CYS N   H2   sing N N 72  
CYS CA  C    sing N N 73  
CYS CA  CB   sing N N 74  
CYS CA  HA   sing N N 75  
CYS C   O    doub N N 76  
CYS C   OXT  sing N N 77  
CYS CB  SG   sing N N 78  
CYS CB  HB2  sing N N 79  
CYS CB  HB3  sing N N 80  
CYS SG  HG   sing N N 81  
CYS OXT HXT  sing N N 82  
GLU N   CA   sing N N 83  
GLU N   H    sing N N 84  
GLU N   H2   sing N N 85  
GLU CA  C    sing N N 86  
GLU CA  CB   sing N N 87  
GLU CA  HA   sing N N 88  
GLU C   O    doub N N 89  
GLU C   OXT  sing N N 90  
GLU CB  CG   sing N N 91  
GLU CB  HB2  sing N N 92  
GLU CB  HB3  sing N N 93  
GLU CG  CD   sing N N 94  
GLU CG  HG2  sing N N 95  
GLU CG  HG3  sing N N 96  
GLU CD  OE1  doub N N 97  
GLU CD  OE2  sing N N 98  
GLU OE2 HE2  sing N N 99  
GLU OXT HXT  sing N N 100 
GLY N   CA   sing N N 101 
GLY N   H    sing N N 102 
GLY N   H2   sing N N 103 
GLY CA  C    sing N N 104 
GLY CA  HA2  sing N N 105 
GLY CA  HA3  sing N N 106 
GLY C   O    doub N N 107 
GLY C   OXT  sing N N 108 
GLY OXT HXT  sing N N 109 
HIS N   CA   sing N N 110 
HIS N   H    sing N N 111 
HIS N   H2   sing N N 112 
HIS CA  C    sing N N 113 
HIS CA  CB   sing N N 114 
HIS CA  HA   sing N N 115 
HIS C   O    doub N N 116 
HIS C   OXT  sing N N 117 
HIS CB  CG   sing N N 118 
HIS CB  HB2  sing N N 119 
HIS CB  HB3  sing N N 120 
HIS CG  ND1  sing Y N 121 
HIS CG  CD2  doub Y N 122 
HIS ND1 CE1  doub Y N 123 
HIS ND1 HD1  sing N N 124 
HIS CD2 NE2  sing Y N 125 
HIS CD2 HD2  sing N N 126 
HIS CE1 NE2  sing Y N 127 
HIS CE1 HE1  sing N N 128 
HIS NE2 HE2  sing N N 129 
HIS OXT HXT  sing N N 130 
HOH O   H1   sing N N 131 
HOH O   H2   sing N N 132 
ILE N   CA   sing N N 133 
ILE N   H    sing N N 134 
ILE N   H2   sing N N 135 
ILE CA  C    sing N N 136 
ILE CA  CB   sing N N 137 
ILE CA  HA   sing N N 138 
ILE C   O    doub N N 139 
ILE C   OXT  sing N N 140 
ILE CB  CG1  sing N N 141 
ILE CB  CG2  sing N N 142 
ILE CB  HB   sing N N 143 
ILE CG1 CD1  sing N N 144 
ILE CG1 HG12 sing N N 145 
ILE CG1 HG13 sing N N 146 
ILE CG2 HG21 sing N N 147 
ILE CG2 HG22 sing N N 148 
ILE CG2 HG23 sing N N 149 
ILE CD1 HD11 sing N N 150 
ILE CD1 HD12 sing N N 151 
ILE CD1 HD13 sing N N 152 
ILE OXT HXT  sing N N 153 
LEU N   CA   sing N N 154 
LEU N   H    sing N N 155 
LEU N   H2   sing N N 156 
LEU CA  C    sing N N 157 
LEU CA  CB   sing N N 158 
LEU CA  HA   sing N N 159 
LEU C   O    doub N N 160 
LEU C   OXT  sing N N 161 
LEU CB  CG   sing N N 162 
LEU CB  HB2  sing N N 163 
LEU CB  HB3  sing N N 164 
LEU CG  CD1  sing N N 165 
LEU CG  CD2  sing N N 166 
LEU CG  HG   sing N N 167 
LEU CD1 HD11 sing N N 168 
LEU CD1 HD12 sing N N 169 
LEU CD1 HD13 sing N N 170 
LEU CD2 HD21 sing N N 171 
LEU CD2 HD22 sing N N 172 
LEU CD2 HD23 sing N N 173 
LEU OXT HXT  sing N N 174 
LYS N   CA   sing N N 175 
LYS N   H    sing N N 176 
LYS N   H2   sing N N 177 
LYS CA  C    sing N N 178 
LYS CA  CB   sing N N 179 
LYS CA  HA   sing N N 180 
LYS C   O    doub N N 181 
LYS C   OXT  sing N N 182 
LYS CB  CG   sing N N 183 
LYS CB  HB2  sing N N 184 
LYS CB  HB3  sing N N 185 
LYS CG  CD   sing N N 186 
LYS CG  HG2  sing N N 187 
LYS CG  HG3  sing N N 188 
LYS CD  CE   sing N N 189 
LYS CD  HD2  sing N N 190 
LYS CD  HD3  sing N N 191 
LYS CE  NZ   sing N N 192 
LYS CE  HE2  sing N N 193 
LYS CE  HE3  sing N N 194 
LYS NZ  HZ1  sing N N 195 
LYS NZ  HZ2  sing N N 196 
LYS NZ  HZ3  sing N N 197 
LYS OXT HXT  sing N N 198 
MET N   CA   sing N N 199 
MET N   H    sing N N 200 
MET N   H2   sing N N 201 
MET CA  C    sing N N 202 
MET CA  CB   sing N N 203 
MET CA  HA   sing N N 204 
MET C   O    doub N N 205 
MET C   OXT  sing N N 206 
MET CB  CG   sing N N 207 
MET CB  HB2  sing N N 208 
MET CB  HB3  sing N N 209 
MET CG  SD   sing N N 210 
MET CG  HG2  sing N N 211 
MET CG  HG3  sing N N 212 
MET SD  CE   sing N N 213 
MET CE  HE1  sing N N 214 
MET CE  HE2  sing N N 215 
MET CE  HE3  sing N N 216 
MET OXT HXT  sing N N 217 
PHE N   CA   sing N N 218 
PHE N   H    sing N N 219 
PHE N   H2   sing N N 220 
PHE CA  C    sing N N 221 
PHE CA  CB   sing N N 222 
PHE CA  HA   sing N N 223 
PHE C   O    doub N N 224 
PHE C   OXT  sing N N 225 
PHE CB  CG   sing N N 226 
PHE CB  HB2  sing N N 227 
PHE CB  HB3  sing N N 228 
PHE CG  CD1  doub Y N 229 
PHE CG  CD2  sing Y N 230 
PHE CD1 CE1  sing Y N 231 
PHE CD1 HD1  sing N N 232 
PHE CD2 CE2  doub Y N 233 
PHE CD2 HD2  sing N N 234 
PHE CE1 CZ   doub Y N 235 
PHE CE1 HE1  sing N N 236 
PHE CE2 CZ   sing Y N 237 
PHE CE2 HE2  sing N N 238 
PHE CZ  HZ   sing N N 239 
PHE OXT HXT  sing N N 240 
PRO N   CA   sing N N 241 
PRO N   CD   sing N N 242 
PRO N   H    sing N N 243 
PRO CA  C    sing N N 244 
PRO CA  CB   sing N N 245 
PRO CA  HA   sing N N 246 
PRO C   O    doub N N 247 
PRO C   OXT  sing N N 248 
PRO CB  CG   sing N N 249 
PRO CB  HB2  sing N N 250 
PRO CB  HB3  sing N N 251 
PRO CG  CD   sing N N 252 
PRO CG  HG2  sing N N 253 
PRO CG  HG3  sing N N 254 
PRO CD  HD2  sing N N 255 
PRO CD  HD3  sing N N 256 
PRO OXT HXT  sing N N 257 
SER N   CA   sing N N 258 
SER N   H    sing N N 259 
SER N   H2   sing N N 260 
SER CA  C    sing N N 261 
SER CA  CB   sing N N 262 
SER CA  HA   sing N N 263 
SER C   O    doub N N 264 
SER C   OXT  sing N N 265 
SER CB  OG   sing N N 266 
SER CB  HB2  sing N N 267 
SER CB  HB3  sing N N 268 
SER OG  HG   sing N N 269 
SER OXT HXT  sing N N 270 
THR N   CA   sing N N 271 
THR N   H    sing N N 272 
THR N   H2   sing N N 273 
THR CA  C    sing N N 274 
THR CA  CB   sing N N 275 
THR CA  HA   sing N N 276 
THR C   O    doub N N 277 
THR C   OXT  sing N N 278 
THR CB  OG1  sing N N 279 
THR CB  CG2  sing N N 280 
THR CB  HB   sing N N 281 
THR OG1 HG1  sing N N 282 
THR CG2 HG21 sing N N 283 
THR CG2 HG22 sing N N 284 
THR CG2 HG23 sing N N 285 
THR OXT HXT  sing N N 286 
TRP N   CA   sing N N 287 
TRP N   H    sing N N 288 
TRP N   H2   sing N N 289 
TRP CA  C    sing N N 290 
TRP CA  CB   sing N N 291 
TRP CA  HA   sing N N 292 
TRP C   O    doub N N 293 
TRP C   OXT  sing N N 294 
TRP CB  CG   sing N N 295 
TRP CB  HB2  sing N N 296 
TRP CB  HB3  sing N N 297 
TRP CG  CD1  doub Y N 298 
TRP CG  CD2  sing Y N 299 
TRP CD1 NE1  sing Y N 300 
TRP CD1 HD1  sing N N 301 
TRP CD2 CE2  doub Y N 302 
TRP CD2 CE3  sing Y N 303 
TRP NE1 CE2  sing Y N 304 
TRP NE1 HE1  sing N N 305 
TRP CE2 CZ2  sing Y N 306 
TRP CE3 CZ3  doub Y N 307 
TRP CE3 HE3  sing N N 308 
TRP CZ2 CH2  doub Y N 309 
TRP CZ2 HZ2  sing N N 310 
TRP CZ3 CH2  sing Y N 311 
TRP CZ3 HZ3  sing N N 312 
TRP CH2 HH2  sing N N 313 
TRP OXT HXT  sing N N 314 
TYR N   CA   sing N N 315 
TYR N   H    sing N N 316 
TYR N   H2   sing N N 317 
TYR CA  C    sing N N 318 
TYR CA  CB   sing N N 319 
TYR CA  HA   sing N N 320 
TYR C   O    doub N N 321 
TYR C   OXT  sing N N 322 
TYR CB  CG   sing N N 323 
TYR CB  HB2  sing N N 324 
TYR CB  HB3  sing N N 325 
TYR CG  CD1  doub Y N 326 
TYR CG  CD2  sing Y N 327 
TYR CD1 CE1  sing Y N 328 
TYR CD1 HD1  sing N N 329 
TYR CD2 CE2  doub Y N 330 
TYR CD2 HD2  sing N N 331 
TYR CE1 CZ   doub Y N 332 
TYR CE1 HE1  sing N N 333 
TYR CE2 CZ   sing Y N 334 
TYR CE2 HE2  sing N N 335 
TYR CZ  OH   sing N N 336 
TYR OH  HH   sing N N 337 
TYR OXT HXT  sing N N 338 
VAL N   CA   sing N N 339 
VAL N   H    sing N N 340 
VAL N   H2   sing N N 341 
VAL CA  C    sing N N 342 
VAL CA  CB   sing N N 343 
VAL CA  HA   sing N N 344 
VAL C   O    doub N N 345 
VAL C   OXT  sing N N 346 
VAL CB  CG1  sing N N 347 
VAL CB  CG2  sing N N 348 
VAL CB  HB   sing N N 349 
VAL CG1 HG11 sing N N 350 
VAL CG1 HG12 sing N N 351 
VAL CG1 HG13 sing N N 352 
VAL CG2 HG21 sing N N 353 
VAL CG2 HG22 sing N N 354 
VAL CG2 HG23 sing N N 355 
VAL OXT HXT  sing N N 356 
WLX N1  C2   doub Y N 357 
WLX C2  C3   sing Y N 358 
WLX C3  C4   doub Y N 359 
WLX N1  C5   sing Y N 360 
WLX C4  C6   sing Y N 361 
WLX C5  C6   doub Y N 362 
WLX C2  N7   sing N N 363 
WLX C4  C8   sing Y N 364 
WLX C6  C9   sing Y N 365 
WLX C8  C10  doub Y N 366 
WLX C9  C11  doub Y N 367 
WLX C10 C11  sing Y N 368 
WLX C10 H18  sing N N 369 
WLX C11 H19  sing N N 370 
WLX C3  H12  sing N N 371 
WLX C5  H13  sing N N 372 
WLX N7  H15  sing N N 373 
WLX N7  H14  sing N N 374 
WLX C8  H16  sing N N 375 
WLX C9  H17  sing N N 376 
# 
loop_
_pdbx_audit_support.funding_organization 
_pdbx_audit_support.country 
_pdbx_audit_support.grant_number 
_pdbx_audit_support.ordinal 
'University of College London' 'United Kingdom' BXTX 1 
'Other private'                ?                HN9A 2 
# 
_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   1DVQ 
_pdbx_initial_refinement_model.details          ? 
# 
_atom_sites.entry_id                    9H7H 
_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]   0.011677 
_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]   0.023529 
_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]   0.015401 
_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  
CA 
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    C  CA  . CYS A 1 10  ? -11.837 15.498 6.397   1.00 42.54 ? 10  CYS A CA  1 
ATOM   2    C  C   . CYS A 1 10  ? -11.607 14.628 5.137   1.00 30.86 ? 10  CYS A C   1 
ATOM   3    O  O   . CYS A 1 10  ? -10.506 14.484 4.666   1.00 37.24 ? 10  CYS A O   1 
ATOM   4    N  N   . PRO A 1 11  ? -12.662 13.998 4.619   1.00 23.29 ? 11  PRO A N   1 
ATOM   5    C  CA  . PRO A 1 11  ? -12.463 13.183 3.448   1.00 18.98 ? 11  PRO A CA  1 
ATOM   6    C  C   . PRO A 1 11  ? -12.374 13.828 2.118   1.00 16.86 ? 11  PRO A C   1 
ATOM   7    O  O   . PRO A 1 11  ? -12.016 13.170 1.144   1.00 17.19 ? 11  PRO A O   1 
ATOM   8    C  CB  . PRO A 1 11  ? -13.616 12.235 3.471   1.00 22.92 ? 11  PRO A CB  1 
ATOM   9    C  CG  . PRO A 1 11  ? -14.656 12.955 4.158   1.00 25.39 ? 11  PRO A CG  1 
ATOM   10   C  CD  . PRO A 1 11  ? -14.001 13.824 5.184   1.00 21.60 ? 11  PRO A CD  1 
ATOM   11   N  N   . LEU A 1 12  ? -12.696 15.096 2.045   1.00 15.51 ? 12  LEU A N   1 
ATOM   12   C  CA  . LEU A 1 12  ? -12.639 15.841 0.767   1.00 16.12 ? 12  LEU A CA  1 
ATOM   13   C  C   . LEU A 1 12  ? -12.070 17.193 1.029   1.00 17.00 ? 12  LEU A C   1 
ATOM   14   O  O   . LEU A 1 12  ? -12.639 17.906 1.829   1.00 20.65 ? 12  LEU A O   1 
ATOM   15   C  CB  . LEU A 1 12  ? -14.055 15.944 0.120   1.00 16.28 ? 12  LEU A CB  1 
ATOM   16   C  CG  . LEU A 1 12  ? -14.148 16.726 -1.180  1.00 16.23 ? 12  LEU A CG  1 
ATOM   17   C  CD1 . LEU A 1 12  ? -13.255 16.074 -2.271  1.00 19.58 ? 12  LEU A CD1 1 
ATOM   18   C  CD2 . LEU A 1 12  ? -15.608 16.787 -1.584  1.00 19.00 ? 12  LEU A CD2 1 
ATOM   19   N  N   . MET A 1 13  ? -10.947 17.512 0.388   1.00 13.33 ? 13  MET A N   1 
ATOM   20   C  CA  . MET A 1 13  ? -10.292 18.794 0.531   1.00 14.07 ? 13  MET A CA  1 
ATOM   21   C  C   . MET A 1 13  ? -9.997  19.338 -0.871  1.00 14.13 ? 13  MET A C   1 
ATOM   22   O  O   . MET A 1 13  ? -9.709  18.602 -1.793  1.00 14.01 ? 13  MET A O   1 
ATOM   23   C  CB  . MET A 1 13  ? -8.963  18.695 1.280   1.00 17.11 ? 13  MET A CB  1 
ATOM   24   C  CG  . MET A 1 13  ? -8.411  20.074 1.640   0.50 15.78 ? 13  MET A CG  1 
ATOM   25   S  SD  . MET A 1 13  ? -7.129  20.816 0.576   0.50 18.47 ? 13  MET A SD  1 
ATOM   26   C  CE  . MET A 1 13  ? -5.672  19.955 1.229   0.50 24.75 ? 13  MET A CE  1 
ATOM   27   N  N   . VAL A 1 14  ? -10.078 20.665 -1.031  1.00 12.32 ? 14  VAL A N   1 
ATOM   28   C  CA  . VAL A 1 14  ? -9.802  21.293 -2.339  1.00 11.88 ? 14  VAL A CA  1 
ATOM   29   C  C   . VAL A 1 14  ? -8.723  22.368 -2.116  1.00 12.16 ? 14  VAL A C   1 
ATOM   30   O  O   . VAL A 1 14  ? -8.846  23.121 -1.149  1.00 15.03 ? 14  VAL A O   1 
ATOM   31   C  CB  . VAL A 1 14  ? -11.081 21.945 -2.928  1.00 13.13 ? 14  VAL A CB  1 
ATOM   32   C  CG1 . VAL A 1 14  ? -10.762 22.662 -4.235  1.00 14.87 ? 14  VAL A CG1 1 
ATOM   33   C  CG2 . VAL A 1 14  ? -12.176 20.896 -3.100  1.00 14.07 ? 14  VAL A CG2 1 
ATOM   34   N  N   . LYS A 1 15  ? -7.698  22.419 -2.973  1.00 11.06 ? 15  LYS A N   1 
ATOM   35   C  CA  . LYS A 1 15  ? -6.632  23.405 -2.869  1.00 12.82 ? 15  LYS A CA  1 
ATOM   36   C  C   . LYS A 1 15  ? -6.515  24.100 -4.224  1.00 12.08 ? 15  LYS A C   1 
ATOM   37   O  O   . LYS A 1 15  ? -6.485  23.452 -5.260  1.00 13.59 ? 15  LYS A O   1 
ATOM   38   C  CB  . LYS A 1 15  ? -5.320  22.719 -2.513  1.00 15.49 ? 15  LYS A CB  1 
ATOM   39   N  N   . VAL A 1 16  ? -6.426  25.428 -4.232  1.00 11.93 ? 16  VAL A N   1 
ATOM   40   C  CA  . VAL A 1 16  ? -6.350  26.182 -5.504  1.00 13.29 ? 16  VAL A CA  1 
ATOM   41   C  C   . VAL A 1 16  ? -5.202  27.157 -5.474  1.00 11.92 ? 16  VAL A C   1 
ATOM   42   O  O   . VAL A 1 16  ? -5.023  27.884 -4.502  1.00 12.54 ? 16  VAL A O   1 
ATOM   43   C  CB  . VAL A 1 16  ? -7.647  26.938 -5.777  1.00 12.79 ? 16  VAL A CB  1 
ATOM   44   C  CG1 . VAL A 1 16  ? -7.641  27.504 -7.205  1.00 12.99 ? 16  VAL A CG1 1 
ATOM   45   C  CG2 . VAL A 1 16  ? -8.881  26.037 -5.578  1.00 12.81 ? 16  VAL A CG2 1 
ATOM   46   N  N   . LEU A 1 17  ? -4.367  27.122 -6.519  1.00 11.42 ? 17  LEU A N   1 
ATOM   47   C  CA  . LEU A 1 17  ? -3.231  28.016 -6.694  1.00 11.02 ? 17  LEU A CA  1 
ATOM   48   C  C   . LEU A 1 17  ? -3.382  28.900 -7.945  1.00 10.17 ? 17  LEU A C   1 
ATOM   49   O  O   . LEU A 1 17  ? -3.969  28.499 -8.938  1.00 11.50 ? 17  LEU A O   1 
ATOM   50   C  CB  . LEU A 1 17  ? -1.929  27.197 -6.815  1.00 13.30 ? 17  LEU A CB  1 
ATOM   51   C  CG  . LEU A 1 17  ? -1.537  26.354 -5.611  1.00 16.19 ? 17  LEU A CG  1 
ATOM   52   C  CD1 . LEU A 1 17  ? -0.238  25.631 -5.977  1.00 18.00 ? 17  LEU A CD1 1 
ATOM   53   C  CD2 . LEU A 1 17  ? -1.356  27.227 -4.366  1.00 17.87 ? 17  LEU A CD2 1 
ATOM   54   N  N   . ASP A 1 18  ? -2.741  30.077 -7.887  1.00 10.91 ? 18  ASP A N   1 
ATOM   55   C  CA  . ASP A 1 18  ? -2.724  31.074 -8.979  1.00 10.39 ? 18  ASP A CA  1 
ATOM   56   C  C   . ASP A 1 18  ? -1.361  31.061 -9.632  1.00 9.33  ? 18  ASP A C   1 
ATOM   57   O  O   . ASP A 1 18  ? -0.356  31.421 -8.987  1.00 10.86 ? 18  ASP A O   1 
ATOM   58   C  CB  . ASP A 1 18  ? -3.092  32.441 -8.386  1.00 10.91 ? 18  ASP A CB  1 
ATOM   59   C  CG  . ASP A 1 18  ? -3.066  33.588 -9.367  1.00 12.32 ? 18  ASP A CG  1 
ATOM   60   O  OD1 . ASP A 1 18  ? -2.288  33.608 -10.294 1.00 11.85 ? 18  ASP A OD1 1 
ATOM   61   O  OD2 . ASP A 1 18  ? -3.865  34.526 -9.145  1.00 15.01 ? 18  ASP A OD2 1 
ATOM   62   N  N   . ALA A 1 19  ? -1.284  30.637 -10.877 1.00 10.82 ? 19  ALA A N   1 
ATOM   63   C  CA  . ALA A 1 19  ? -0.027  30.514 -11.618 1.00 9.99  ? 19  ALA A CA  1 
ATOM   64   C  C   . ALA A 1 19  ? 0.492   31.828 -12.187 1.00 10.76 ? 19  ALA A C   1 
ATOM   65   O  O   . ALA A 1 19  ? 1.598   31.840 -12.716 1.00 13.07 ? 19  ALA A O   1 
ATOM   66   C  CB  . ALA A 1 19  ? -0.191  29.486 -12.721 1.00 12.09 ? 19  ALA A CB  1 
ATOM   67   N  N   . VAL A 1 20  ? -0.304  32.898 -12.185 1.00 11.10 ? 20  VAL A N   1 
ATOM   68   C  CA  . VAL A 1 20  ? 0.182   34.223 -12.586 1.00 13.08 ? 20  VAL A CA  1 
ATOM   69   C  C   . VAL A 1 20  ? 0.946   34.920 -11.481 1.00 13.28 ? 20  VAL A C   1 
ATOM   70   O  O   . VAL A 1 20  ? 1.983   35.520 -11.724 1.00 15.15 ? 20  VAL A O   1 
ATOM   71   C  CB  . VAL A 1 20  ? -1.038  35.089 -13.055 1.00 13.75 ? 20  VAL A CB  1 
ATOM   72   C  CG1 . VAL A 1 20  ? -0.616  36.499 -13.280 1.00 14.66 ? 20  VAL A CG1 1 
ATOM   73   C  CG2 . VAL A 1 20  ? -1.652  34.512 -14.305 1.00 16.99 ? 20  VAL A CG2 1 
ATOM   74   N  N   . ARG A 1 21  ? 0.414   34.853 -10.283 1.00 12.74 ? 21  ARG A N   1 
ATOM   75   C  CA  . ARG A 1 21  ? 0.965   35.523 -9.132  1.00 14.28 ? 21  ARG A CA  1 
ATOM   76   C  C   . ARG A 1 21  ? 1.885   34.631 -8.292  1.00 14.53 ? 21  ARG A C   1 
ATOM   77   O  O   . ARG A 1 21  ? 2.670   35.123 -7.506  1.00 15.89 ? 21  ARG A O   1 
ATOM   78   C  CB  . ARG A 1 21  ? -0.182  36.100 -8.251  1.00 19.74 ? 21  ARG A CB  1 
ATOM   79   C  CG  . ARG A 1 21  ? -1.103  37.097 -8.943  0.50 22.17 ? 21  ARG A CG  1 
ATOM   80   C  CD  . ARG A 1 21  ? -2.515  37.039 -8.333  0.50 31.19 ? 21  ARG A CD  1 
ATOM   81   N  NE  . ARG A 1 21  ? -3.035  38.283 -7.855  1.00 41.54 ? 21  ARG A NE  1 
ATOM   82   C  CZ  . ARG A 1 21  ? -3.708  38.415 -6.715  0.50 30.82 ? 21  ARG A CZ  1 
ATOM   83   N  N   . GLY A 1 22  ? 1.849   33.322 -8.474  1.00 12.68 ? 22  GLY A N   1 
ATOM   84   C  CA  . GLY A 1 22  ? 2.622   32.477 -7.601  1.00 12.61 ? 22  GLY A CA  1 
ATOM   85   C  C   . GLY A 1 22  ? 2.150   32.473 -6.174  1.00 10.16 ? 22  GLY A C   1 
ATOM   86   O  O   . GLY A 1 22  ? 2.916   32.643 -5.236  1.00 11.68 ? 22  GLY A O   1 
ATOM   87   N  N   . SER A 1 23  ? 0.867   32.306 -5.992  1.00 11.60 ? 23  SER A N   1 
ATOM   88   C  CA  . SER A 1 23  ? 0.191   32.459 -4.721  1.00 11.26 ? 23  SER A CA  1 
ATOM   89   C  C   . SER A 1 23  ? -0.981  31.500 -4.597  1.00 12.86 ? 23  SER A C   1 
ATOM   90   O  O   . SER A 1 23  ? -1.479  30.993 -5.563  1.00 14.17 ? 23  SER A O   1 
ATOM   91   C  CB  . SER A 1 23  ? -0.360  33.865 -4.576  1.00 15.21 ? 23  SER A CB  1 
ATOM   92   O  OG  . SER A 1 23  ? -1.480  34.035 -5.402  1.00 21.69 ? 23  SER A OG  1 
ATOM   93   N  N   . PRO A 1 24  ? -1.433  31.293 -3.381  1.00 12.11 ? 24  PRO A N   1 
ATOM   94   C  CA  . PRO A 1 24  ? -2.742  30.681 -3.211  1.00 13.51 ? 24  PRO A CA  1 
ATOM   95   C  C   . PRO A 1 24  ? -3.824  31.524 -3.878  1.00 13.80 ? 24  PRO A C   1 
ATOM   96   O  O   . PRO A 1 24  ? -3.723  32.724 -3.960  1.00 15.09 ? 24  PRO A O   1 
ATOM   97   C  CB  . PRO A 1 24  ? -2.925  30.616 -1.717  1.00 16.27 ? 24  PRO A CB  1 
ATOM   98   C  CG  . PRO A 1 24  ? -1.885  31.462 -1.150  1.00 26.31 ? 24  PRO A CG  1 
ATOM   99   C  CD  . PRO A 1 24  ? -0.813  31.627 -2.091  1.00 13.51 ? 24  PRO A CD  1 
ATOM   100  N  N   . ALA A 1 25  ? -4.840  30.867 -4.387  1.00 12.53 ? 25  ALA A N   1 
ATOM   101  C  CA  . ALA A 1 25  ? -6.015  31.493 -4.928  1.00 12.37 ? 25  ALA A CA  1 
ATOM   102  C  C   . ALA A 1 25  ? -7.032  31.580 -3.797  1.00 12.68 ? 25  ALA A C   1 
ATOM   103  O  O   . ALA A 1 25  ? -7.626  30.577 -3.378  1.00 13.86 ? 25  ALA A O   1 
ATOM   104  C  CB  . ALA A 1 25  ? -6.552  30.721 -6.127  1.00 14.32 ? 25  ALA A CB  1 
ATOM   105  N  N   . ILE A 1 26  ? -7.187  32.771 -3.268  1.00 13.41 ? 26  ILE A N   1 
ATOM   106  C  CA  A ILE A 1 26  ? -7.950  33.062 -2.052  0.50 12.97 ? 26  ILE A CA  1 
ATOM   107  C  CA  B ILE A 1 26  ? -7.969  33.016 -2.053  0.50 13.38 ? 26  ILE A CA  1 
ATOM   108  C  C   . ILE A 1 26  ? -9.419  33.445 -2.362  1.00 13.48 ? 26  ILE A C   1 
ATOM   109  O  O   . ILE A 1 26  ? -9.653  34.029 -3.396  1.00 15.96 ? 26  ILE A O   1 
ATOM   110  C  CB  A ILE A 1 26  ? -7.290  34.181 -1.243  0.50 15.86 ? 26  ILE A CB  1 
ATOM   111  C  CB  B ILE A 1 26  ? -7.339  34.034 -1.107  0.50 14.59 ? 26  ILE A CB  1 
ATOM   112  C  CG1 A ILE A 1 26  ? -5.835  33.806 -0.908  0.50 16.67 ? 26  ILE A CG1 1 
ATOM   113  C  CG1 B ILE A 1 26  ? -7.477  35.452 -1.654  0.50 15.32 ? 26  ILE A CG1 1 
ATOM   114  C  CG2 A ILE A 1 26  ? -8.062  34.467 0.042   0.50 15.81 ? 26  ILE A CG2 1 
ATOM   115  C  CG2 B ILE A 1 26  ? -5.851  33.774 -0.909  0.50 17.46 ? 26  ILE A CG2 1 
ATOM   116  C  CD1 A ILE A 1 26  ? -4.915  34.962 -0.581  0.50 22.41 ? 26  ILE A CD1 1 
ATOM   117  C  CD1 B ILE A 1 26  ? -7.108  36.494 -0.602  0.50 20.44 ? 26  ILE A CD1 1 
ATOM   118  N  N   . ASN A 1 27  ? -10.363 33.002 -1.544  1.00 13.26 ? 27  ASN A N   1 
ATOM   119  C  CA  A ASN A 1 27  ? -11.787 33.392 -1.727  0.50 13.44 ? 27  ASN A CA  1 
ATOM   120  C  CA  B ASN A 1 27  ? -11.763 33.387 -1.745  0.50 14.17 ? 27  ASN A CA  1 
ATOM   121  C  C   . ASN A 1 27  ? -12.439 32.871 -3.048  1.00 13.98 ? 27  ASN A C   1 
ATOM   122  O  O   . ASN A 1 27  ? -13.327 33.484 -3.632  1.00 17.12 ? 27  ASN A O   1 
ATOM   123  C  CB  A ASN A 1 27  ? -12.041 34.919 -1.668  0.50 14.77 ? 27  ASN A CB  1 
ATOM   124  C  CB  B ASN A 1 27  ? -11.915 34.897 -1.684  0.50 18.45 ? 27  ASN A CB  1 
ATOM   125  C  CG  A ASN A 1 27  ? -11.607 35.557 -0.385  0.50 18.32 ? 27  ASN A CG  1 
ATOM   126  C  CG  B ASN A 1 27  ? -12.555 35.354 -0.426  0.50 27.39 ? 27  ASN A CG  1 
ATOM   127  O  OD1 A ASN A 1 27  ? -10.911 36.629 -0.373  0.50 25.48 ? 27  ASN A OD1 1 
ATOM   128  O  OD1 B ASN A 1 27  ? -11.981 35.213 0.641   0.50 30.87 ? 27  ASN A OD1 1 
ATOM   129  N  ND2 A ASN A 1 27  ? -11.999 34.949 0.713   0.50 21.47 ? 27  ASN A ND2 1 
ATOM   130  N  ND2 B ASN A 1 27  ? -13.764 35.900 -0.538  0.50 37.00 ? 27  ASN A ND2 1 
ATOM   131  N  N   . VAL A 1 28  ? -12.017 31.671 -3.450  1.00 13.73 ? 28  VAL A N   1 
ATOM   132  C  CA  . VAL A 1 28  ? -12.555 30.994 -4.606  1.00 13.30 ? 28  VAL A CA  1 
ATOM   133  C  C   . VAL A 1 28  ? -13.749 30.133 -4.163  1.00 12.20 ? 28  VAL A C   1 
ATOM   134  O  O   . VAL A 1 28  ? -13.606 29.292 -3.257  1.00 12.99 ? 28  VAL A O   1 
ATOM   135  C  CB  . VAL A 1 28  ? -11.488 30.091 -5.286  1.00 12.69 ? 28  VAL A CB  1 
ATOM   136  C  CG1 . VAL A 1 28  ? -12.107 29.296 -6.464  1.00 17.04 ? 28  VAL A CG1 1 
ATOM   137  C  CG2 . VAL A 1 28  ? -10.314 30.936 -5.804  1.00 14.59 ? 28  VAL A CG2 1 
ATOM   138  N  N   . ALA A 1 29  ? -14.892 30.357 -4.789  1.00 10.89 ? 29  ALA A N   1 
ATOM   139  C  CA  . ALA A 1 29  ? -16.085 29.563 -4.459  1.00 11.39 ? 29  ALA A CA  1 
ATOM   140  C  C   . ALA A 1 29  ? -15.968 28.190 -5.111  1.00 11.93 ? 29  ALA A C   1 
ATOM   141  O  O   . ALA A 1 29  ? -15.576 28.065 -6.264  1.00 12.13 ? 29  ALA A O   1 
ATOM   142  C  CB  . ALA A 1 29  ? -17.313 30.255 -4.961  1.00 11.46 ? 29  ALA A CB  1 
ATOM   143  N  N   . VAL A 1 30  ? -16.389 27.178 -4.345  1.00 10.67 ? 30  VAL A N   1 
ATOM   144  C  CA  . VAL A 1 30  ? -16.339 25.768 -4.776  1.00 11.64 ? 30  VAL A CA  1 
ATOM   145  C  C   . VAL A 1 30  ? -17.705 25.143 -4.452  1.00 10.89 ? 30  VAL A C   1 
ATOM   146  O  O   . VAL A 1 30  ? -18.174 25.213 -3.324  1.00 12.99 ? 30  VAL A O   1 
ATOM   147  C  CB  . VAL A 1 30  ? -15.227 25.017 -4.054  1.00 11.86 ? 30  VAL A CB  1 
ATOM   148  C  CG1 . VAL A 1 30  ? -15.214 23.525 -4.472  1.00 14.60 ? 30  VAL A CG1 1 
ATOM   149  C  CG2 . VAL A 1 30  ? -13.888 25.680 -4.284  1.00 12.82 ? 30  VAL A CG2 1 
ATOM   150  N  N   . HIS A 1 31  ? -18.314 24.536 -5.438  1.00 12.02 ? 31  HIS A N   1 
ATOM   151  C  CA  . HIS A 1 31  ? -19.586 23.847 -5.280  1.00 12.20 ? 31  HIS A CA  1 
ATOM   152  C  C   . HIS A 1 31  ? -19.458 22.382 -5.617  1.00 12.75 ? 31  HIS A C   1 
ATOM   153  O  O   . HIS A 1 31  ? -18.903 22.047 -6.643  1.00 13.26 ? 31  HIS A O   1 
ATOM   154  C  CB  . HIS A 1 31  ? -20.634 24.456 -6.211  1.00 13.44 ? 31  HIS A CB  1 
ATOM   155  C  CG  . HIS A 1 31  ? -21.092 25.815 -5.801  1.00 15.73 ? 31  HIS A CG  1 
ATOM   156  N  ND1 . HIS A 1 31  ? -20.428 26.979 -6.094  1.00 18.77 ? 31  HIS A ND1 1 
ATOM   157  C  CD2 . HIS A 1 31  ? -22.181 26.159 -5.103  1.00 13.64 ? 31  HIS A CD2 1 
ATOM   158  C  CE1 . HIS A 1 31  ? -21.127 28.000 -5.580  1.00 15.32 ? 31  HIS A CE1 1 
ATOM   159  N  NE2 . HIS A 1 31  ? -22.182 27.505 -4.973  1.00 20.97 ? 31  HIS A NE2 1 
ATOM   160  N  N   . VAL A 1 32  ? -19.923 21.527 -4.718  1.00 11.83 ? 32  VAL A N   1 
ATOM   161  C  CA  . VAL A 1 32  ? -19.834 20.065 -4.928  1.00 12.51 ? 32  VAL A CA  1 
ATOM   162  C  C   . VAL A 1 32  ? -21.243 19.511 -5.147  1.00 10.89 ? 32  VAL A C   1 
ATOM   163  O  O   . VAL A 1 32  ? -22.163 19.881 -4.395  1.00 11.85 ? 32  VAL A O   1 
ATOM   164  C  CB  . VAL A 1 32  ? -19.139 19.357 -3.729  1.00 11.82 ? 32  VAL A CB  1 
ATOM   165  C  CG1 . VAL A 1 32  ? -18.998 17.877 -3.963  1.00 13.53 ? 32  VAL A CG1 1 
ATOM   166  C  CG2 . VAL A 1 32  ? -17.788 19.992 -3.463  1.00 14.17 ? 32  VAL A CG2 1 
ATOM   167  N  N   . PHE A 1 33  ? -21.389 18.634 -6.155  1.00 12.44 ? 33  PHE A N   1 
ATOM   168  C  CA  . PHE A 1 33  ? -22.681 17.972 -6.463  1.00 12.71 ? 33  PHE A CA  1 
ATOM   169  C  C   . PHE A 1 33  ? -22.458 16.475 -6.440  1.00 12.98 ? 33  PHE A C   1 
ATOM   170  O  O   . PHE A 1 33  ? -21.342 16.036 -6.637  1.00 11.52 ? 33  PHE A O   1 
ATOM   171  C  CB  . PHE A 1 33  ? -23.173 18.447 -7.824  1.00 15.10 ? 33  PHE A CB  1 
ATOM   172  C  CG  . PHE A 1 33  ? -23.335 19.936 -7.919  1.00 15.43 ? 33  PHE A CG  1 
ATOM   173  C  CD1 . PHE A 1 33  ? -22.259 20.733 -8.316  1.00 16.37 ? 33  PHE A CD1 1 
ATOM   174  C  CD2 . PHE A 1 33  ? -24.516 20.528 -7.618  1.00 17.54 ? 33  PHE A CD2 1 
ATOM   175  C  CE1 . PHE A 1 33  ? -22.381 22.116 -8.395  1.00 17.13 ? 33  PHE A CE1 1 
ATOM   176  C  CE2 . PHE A 1 33  ? -24.634 21.895 -7.699  1.00 18.44 ? 33  PHE A CE2 1 
ATOM   177  C  CZ  . PHE A 1 33  ? -23.564 22.673 -8.073  1.00 17.83 ? 33  PHE A CZ  1 
ATOM   178  N  N   . ARG A 1 34  ? -23.529 15.707 -6.247  1.00 13.49 ? 34  ARG A N   1 
ATOM   179  C  CA  . ARG A 1 34  ? -23.501 14.253 -6.267  1.00 13.06 ? 34  ARG A CA  1 
ATOM   180  C  C   . ARG A 1 34  ? -24.603 13.818 -7.202  1.00 13.28 ? 34  ARG A C   1 
ATOM   181  O  O   . ARG A 1 34  ? -25.736 14.254 -7.059  1.00 15.45 ? 34  ARG A O   1 
ATOM   182  C  CB  . ARG A 1 34  ? -23.683 13.676 -4.860  1.00 13.96 ? 34  ARG A CB  1 
ATOM   183  C  CG  . ARG A 1 34  ? -23.598 12.155 -4.825  1.00 14.43 ? 34  ARG A CG  1 
ATOM   184  C  CD  . ARG A 1 34  ? -23.861 11.626 -3.405  1.00 15.70 ? 34  ARG A CD  1 
ATOM   185  N  NE  . ARG A 1 34  ? -23.912 10.204 -3.367  1.00 16.16 ? 34  ARG A NE  1 
ATOM   186  C  CZ  . ARG A 1 34  ? -24.948 9.467  -3.694  1.00 16.74 ? 34  ARG A CZ  1 
ATOM   187  N  NH1 . ARG A 1 34  ? -26.084 10.010 -4.075  1.00 17.38 ? 34  ARG A NH1 1 
ATOM   188  N  NH2 . ARG A 1 34  ? -24.817 8.137  -3.625  1.00 16.30 ? 34  ARG A NH2 1 
ATOM   189  N  N   . LYS A 1 35  ? -24.323 12.845 -8.058  1.00 13.61 ? 35  LYS A N   1 
ATOM   190  C  CA  . LYS A 1 35  ? -25.344 12.347 -8.980  1.00 14.12 ? 35  LYS A CA  1 
ATOM   191  C  C   . LYS A 1 35  ? -26.425 11.509 -8.238  1.00 14.41 ? 35  LYS A C   1 
ATOM   192  O  O   . LYS A 1 35  ? -26.123 10.642 -7.447  1.00 16.47 ? 35  LYS A O   1 
ATOM   193  C  CB  . LYS A 1 35  ? -24.686 11.505 -10.098 1.00 16.62 ? 35  LYS A CB  1 
ATOM   194  C  CG  . LYS A 1 35  ? -25.513 11.312 -11.347 1.00 28.10 ? 35  LYS A CG  1 
ATOM   195  C  CD  . LYS A 1 35  ? -24.651 10.724 -12.515 1.00 34.25 ? 35  LYS A CD  1 
ATOM   196  N  N   . ALA A 1 36  ? -27.667 11.875 -8.427  1.00 15.76 ? 36  ALA A N   1 
ATOM   197  C  CA  . ALA A 1 36  ? -28.816 11.218 -7.816  1.00 17.14 ? 36  ALA A CA  1 
ATOM   198  C  C   . ALA A 1 36  ? -29.231 10.003 -8.596  1.00 22.49 ? 36  ALA A C   1 
ATOM   199  O  O   . ALA A 1 36  ? -28.727 9.768  -9.678  1.00 22.08 ? 36  ALA A O   1 
ATOM   200  C  CB  . ALA A 1 36  ? -29.972 12.202 -7.688  1.00 22.22 ? 36  ALA A CB  1 
ATOM   201  N  N   . ALA A 1 37  ? -30.192 9.275  -8.019  1.00 25.30 ? 37  ALA A N   1 
ATOM   202  C  CA  . ALA A 1 37  ? -30.653 8.037  -8.588  1.00 33.35 ? 37  ALA A CA  1 
ATOM   203  C  C   . ALA A 1 37  ? -31.257 8.281  -9.980  1.00 33.34 ? 37  ALA A C   1 
ATOM   204  O  O   . ALA A 1 37  ? -31.247 7.405  -10.860 1.00 37.19 ? 37  ALA A O   1 
ATOM   205  C  CB  . ALA A 1 37  ? -31.707 7.376  -7.637  1.00 43.29 ? 37  ALA A CB  1 
ATOM   206  N  N   . ASP A 1 38  ? -31.813 9.468  -10.162 1.00 29.55 ? 38  ASP A N   1 
ATOM   207  C  CA  . ASP A 1 38  ? -32.439 9.805  -11.438 1.00 30.47 ? 38  ASP A CA  1 
ATOM   208  C  C   . ASP A 1 38  ? -31.491 10.419 -12.409 1.00 23.97 ? 38  ASP A C   1 
ATOM   209  O  O   . ASP A 1 38  ? -31.909 10.943 -13.440 1.00 34.48 ? 38  ASP A O   1 
ATOM   210  C  CB  . ASP A 1 38  ? -33.663 10.696 -11.213 1.00 32.89 ? 38  ASP A CB  1 
ATOM   211  C  CG  . ASP A 1 38  ? -33.312 12.035 -10.697 1.00 36.29 ? 38  ASP A CG  1 
ATOM   212  O  OD1 . ASP A 1 38  ? -32.120 12.337 -10.537 1.00 35.03 ? 38  ASP A OD1 1 
ATOM   213  O  OD2 . ASP A 1 38  ? -34.225 12.836 -10.462 1.00 42.35 ? 38  ASP A OD2 1 
ATOM   214  N  N   . ASP A 1 39  ? -30.211 10.370 -12.094 1.00 28.08 ? 39  ASP A N   1 
ATOM   215  C  CA  . ASP A 1 39  ? -29.175 10.856 -13.000 1.00 37.08 ? 39  ASP A CA  1 
ATOM   216  C  C   . ASP A 1 39  ? -29.040 12.372 -13.029 1.00 28.35 ? 39  ASP A C   1 
ATOM   217  O  O   . ASP A 1 39  ? -28.395 12.850 -13.837 1.00 37.06 ? 39  ASP A O   1 
ATOM   218  C  CB  . ASP A 1 39  ? -29.345 10.356 -14.443 1.00 40.88 ? 39  ASP A CB  1 
ATOM   219  N  N   . THR A 1 40  ? -29.690 13.108 -12.139 1.00 27.81 ? 40  THR A N   1 
ATOM   220  C  CA  . THR A 1 40  ? -29.491 14.556 -12.082 1.00 26.97 ? 40  THR A CA  1 
ATOM   221  C  C   . THR A 1 40  ? -28.411 14.901 -11.053 1.00 24.62 ? 40  THR A C   1 
ATOM   222  O  O   . THR A 1 40  ? -28.107 14.110 -10.197 1.00 21.19 ? 40  THR A O   1 
ATOM   223  C  CB  . THR A 1 40  ? -30.792 15.271 -11.720 1.00 29.80 ? 40  THR A CB  1 
ATOM   224  O  OG1 . THR A 1 40  ? -31.168 14.964 -10.381 1.00 30.92 ? 40  THR A OG1 1 
ATOM   225  C  CG2 . THR A 1 40  ? -31.931 14.848 -12.702 1.00 43.14 ? 40  THR A CG2 1 
ATOM   226  N  N   . TRP A 1 41  ? -27.846 16.101 -11.116 1.00 26.09 ? 41  TRP A N   1 
ATOM   227  C  CA  . TRP A 1 41  ? -26.901 16.543 -10.113 1.00 20.69 ? 41  TRP A CA  1 
ATOM   228  C  C   . TRP A 1 41  ? -27.610 17.173 -8.974  1.00 22.48 ? 41  TRP A C   1 
ATOM   229  O  O   . TRP A 1 41  ? -28.318 18.135 -9.154  1.00 47.88 ? 41  TRP A O   1 
ATOM   230  C  CB  . TRP A 1 41  ? -25.917 17.576 -10.721 1.00 20.70 ? 41  TRP A CB  1 
ATOM   231  C  CG  . TRP A 1 41  ? -24.935 16.982 -11.670 1.00 22.04 ? 41  TRP A CG  1 
ATOM   232  C  CD1 . TRP A 1 41  ? -24.897 17.178 -13.015 1.00 24.79 ? 41  TRP A CD1 1 
ATOM   233  C  CD2 . TRP A 1 41  ? -23.854 16.065 -11.377 1.00 18.49 ? 41  TRP A CD2 1 
ATOM   234  N  NE1 . TRP A 1 41  ? -23.858 16.503 -13.572 1.00 32.71 ? 41  TRP A NE1 1 
ATOM   235  C  CE2 . TRP A 1 41  ? -23.196 15.805 -12.603 1.00 23.33 ? 41  TRP A CE2 1 
ATOM   236  C  CE3 . TRP A 1 41  ? -23.351 15.509 -10.216 1.00 16.39 ? 41  TRP A CE3 1 
ATOM   237  C  CZ2 . TRP A 1 41  ? -22.100 14.964 -12.691 1.00 26.01 ? 41  TRP A CZ2 1 
ATOM   238  C  CZ3 . TRP A 1 41  ? -22.288 14.681 -10.323 1.00 15.74 ? 41  TRP A CZ3 1 
ATOM   239  C  CH2 . TRP A 1 41  ? -21.687 14.390 -11.542 1.00 19.61 ? 41  TRP A CH2 1 
ATOM   240  N  N   . GLU A 1 42  ? -27.359 16.659 -7.777  1.00 18.19 ? 42  GLU A N   1 
ATOM   241  C  CA  . GLU A 1 42  ? -27.906 17.245 -6.588  1.00 19.62 ? 42  GLU A CA  1 
ATOM   242  C  C   . GLU A 1 42  ? -26.844 17.941 -5.782  1.00 17.91 ? 42  GLU A C   1 
ATOM   243  O  O   . GLU A 1 42  ? -25.702 17.504 -5.697  1.00 17.70 ? 42  GLU A O   1 
ATOM   244  C  CB  . GLU A 1 42  ? -28.470 16.163 -5.655  1.00 23.04 ? 42  GLU A CB  1 
ATOM   245  N  N   . PRO A 1 43  ? -27.216 19.084 -5.156  1.00 16.59 ? 43  PRO A N   1 
ATOM   246  C  CA  . PRO A 1 43  ? -26.225 19.794 -4.318  1.00 16.94 ? 43  PRO A CA  1 
ATOM   247  C  C   . PRO A 1 43  ? -25.751 18.965 -3.181  1.00 19.11 ? 43  PRO A C   1 
ATOM   248  O  O   . PRO A 1 43  ? -26.584 18.248 -2.570  1.00 24.22 ? 43  PRO A O   1 
ATOM   249  C  CB  . PRO A 1 43  ? -27.012 21.065 -3.833  1.00 20.46 ? 43  PRO A CB  1 
ATOM   250  C  CG  . PRO A 1 43  ? -28.141 21.184 -4.777  1.00 25.99 ? 43  PRO A CG  1 
ATOM   251  C  CD  . PRO A 1 43  ? -28.519 19.774 -5.154  1.00 19.89 ? 43  PRO A CD  1 
ATOM   252  N  N   . PHE A 1 44  ? -24.458 18.958 -2.937  1.00 15.69 ? 44  PHE A N   1 
ATOM   253  C  CA  . PHE A 1 44  ? -23.828 18.194 -1.870  1.00 13.55 ? 44  PHE A CA  1 
ATOM   254  C  C   . PHE A 1 44  ? -23.169 19.005 -0.791  1.00 14.25 ? 44  PHE A C   1 
ATOM   255  O  O   . PHE A 1 44  ? -23.374 18.765 0.400   1.00 15.27 ? 44  PHE A O   1 
ATOM   256  C  CB  . PHE A 1 44  ? -22.884 17.119 -2.477  1.00 13.90 ? 44  PHE A CB  1 
ATOM   257  C  CG  . PHE A 1 44  ? -22.238 16.235 -1.469  1.00 15.98 ? 44  PHE A CG  1 
ATOM   258  C  CD1 . PHE A 1 44  ? -22.904 15.135 -0.964  1.00 18.21 ? 44  PHE A CD1 1 
ATOM   259  C  CD2 . PHE A 1 44  ? -20.959 16.485 -1.012  1.00 14.96 ? 44  PHE A CD2 1 
ATOM   260  C  CE1 . PHE A 1 44  ? -22.291 14.329 -0.004  1.00 17.22 ? 44  PHE A CE1 1 
ATOM   261  C  CE2 . PHE A 1 44  ? -20.410 15.754 -0.035  1.00 16.50 ? 44  PHE A CE2 1 
ATOM   262  C  CZ  . PHE A 1 44  ? -21.079 14.605 0.439   1.00 16.94 ? 44  PHE A CZ  1 
ATOM   263  N  N   . ALA A 1 45  ? -22.349 19.963 -1.192  1.00 12.80 ? 45  ALA A N   1 
ATOM   264  C  CA  . ALA A 1 45  ? -21.665 20.840 -0.223  1.00 13.69 ? 45  ALA A CA  1 
ATOM   265  C  C   . ALA A 1 45  ? -21.061 22.012 -1.015  1.00 11.89 ? 45  ALA A C   1 
ATOM   266  O  O   . ALA A 1 45  ? -20.876 21.898 -2.222  1.00 13.75 ? 45  ALA A O   1 
ATOM   267  C  CB  . ALA A 1 45  ? -20.530 20.086 0.506   1.00 13.85 ? 45  ALA A CB  1 
ATOM   268  N  N   . SER A 1 46  ? -20.783 23.111 -0.324  1.00 11.48 ? 46  SER A N   1 
ATOM   269  C  CA  . SER A 1 46  ? -20.077 24.222 -0.956  1.00 10.95 ? 46  SER A CA  1 
ATOM   270  C  C   . SER A 1 46  ? -19.280 24.983 0.080   1.00 11.87 ? 46  SER A C   1 
ATOM   271  O  O   . SER A 1 46  ? -19.505 24.893 1.259   1.00 12.42 ? 46  SER A O   1 
ATOM   272  C  CB  . SER A 1 46  ? -21.030 25.134 -1.738  1.00 11.42 ? 46  SER A CB  1 
ATOM   273  O  OG  . SER A 1 46  ? -21.935 25.820 -0.892  1.00 12.87 ? 46  SER A OG  1 
ATOM   274  N  N   . GLY A 1 47  ? -18.338 25.792 -0.407  1.00 12.13 ? 47  GLY A N   1 
ATOM   275  C  CA  . GLY A 1 47  ? -17.521 26.607 0.506   1.00 12.44 ? 47  GLY A CA  1 
ATOM   276  C  C   . GLY A 1 47  ? -16.619 27.531 -0.289  1.00 11.69 ? 47  GLY A C   1 
ATOM   277  O  O   . GLY A 1 47  ? -16.751 27.607 -1.471  1.00 12.13 ? 47  GLY A O   1 
ATOM   278  N  N   . LYS A 1 48  ? -15.709 28.197 0.382   1.00 13.38 ? 48  LYS A N   1 
ATOM   279  C  CA  . LYS A 1 48  ? -14.717 28.993 -0.332  1.00 14.45 ? 48  LYS A CA  1 
ATOM   280  C  C   . LYS A 1 48  ? -13.319 28.821 0.196   1.00 13.48 ? 48  LYS A C   1 
ATOM   281  O  O   . LYS A 1 48  ? -13.138 28.527 1.372   1.00 14.24 ? 48  LYS A O   1 
ATOM   282  C  CB  . LYS A 1 48  ? -15.061 30.452 -0.344  1.00 20.71 ? 48  LYS A CB  1 
ATOM   283  C  CG  . LYS A 1 48  ? -15.166 31.083 0.982   1.00 24.92 ? 48  LYS A CG  1 
ATOM   284  C  CD  . LYS A 1 48  ? -15.667 32.618 0.963   1.00 42.49 ? 48  LYS A CD  1 
ATOM   285  N  N   . THR A 1 49  ? -12.313 28.995 -0.676  1.00 11.36 ? 49  THR A N   1 
ATOM   286  C  CA  . THR A 1 49  ? -10.933 28.808 -0.213  1.00 12.18 ? 49  THR A CA  1 
ATOM   287  C  C   . THR A 1 49  ? -10.479 29.885 0.762   1.00 12.44 ? 49  THR A C   1 
ATOM   288  O  O   . THR A 1 49  ? -10.907 31.051 0.670   1.00 15.22 ? 49  THR A O   1 
ATOM   289  C  CB  . THR A 1 49  ? -9.927  28.753 -1.358  1.00 11.61 ? 49  THR A CB  1 
ATOM   290  O  OG1 . THR A 1 49  ? -9.945  29.977 -2.115  1.00 13.12 ? 49  THR A OG1 1 
ATOM   291  C  CG2 . THR A 1 49  ? -10.188 27.544 -2.308  1.00 13.22 ? 49  THR A CG2 1 
ATOM   292  N  N   . SER A 1 50  ? -9.637  29.500 1.696   1.00 13.76 ? 50  SER A N   1 
ATOM   293  C  CA  . SER A 1 50  ? -9.085  30.401 2.711   1.00 15.58 ? 50  SER A CA  1 
ATOM   294  C  C   . SER A 1 50  ? -7.872  31.148 2.194   1.00 16.66 ? 50  SER A C   1 
ATOM   295  O  O   . SER A 1 50  ? -7.522  31.036 1.027   1.00 16.47 ? 50  SER A O   1 
ATOM   296  C  CB  . SER A 1 50  ? -8.667  29.548 3.902   1.00 18.13 ? 50  SER A CB  1 
ATOM   297  O  OG  . SER A 1 50  ? -7.466  28.812 3.519   1.00 20.58 ? 50  SER A OG  1 
ATOM   298  N  N   . GLU A 1 51  ? -7.199  31.872 3.109   1.00 17.68 ? 51  GLU A N   1 
ATOM   299  C  CA  . GLU A 1 51  ? -6.015  32.650 2.786   1.00 20.09 ? 51  GLU A CA  1 
ATOM   300  C  C   . GLU A 1 51  ? -4.875  31.730 2.309   1.00 18.78 ? 51  GLU A C   1 
ATOM   301  O  O   . GLU A 1 51  ? -3.945  32.174 1.630   1.00 19.46 ? 51  GLU A O   1 
ATOM   302  C  CB  . GLU A 1 51  ? -5.592  33.549 4.003   1.00 27.26 ? 51  GLU A CB  1 
ATOM   303  N  N   . SER A 1 52  ? -4.940  30.450 2.654   1.00 18.36 ? 52  SER A N   1 
ATOM   304  C  CA  . SER A 1 52  ? -3.937  29.477 2.189   1.00 17.16 ? 52  SER A CA  1 
ATOM   305  C  C   . SER A 1 52  ? -4.337  28.802 0.892   1.00 15.57 ? 52  SER A C   1 
ATOM   306  O  O   . SER A 1 52  ? -3.599  27.948 0.410   1.00 15.84 ? 52  SER A O   1 
ATOM   307  C  CB  . SER A 1 52  ? -3.748  28.386 3.247   1.00 23.01 ? 52  SER A CB  1 
ATOM   308  O  OG  . SER A 1 52  ? -4.890  27.539 3.338   1.00 24.31 ? 52  SER A OG  1 
ATOM   309  N  N   . GLY A 1 53  ? -5.489  29.147 0.317   1.00 14.84 ? 53  GLY A N   1 
ATOM   310  C  CA  . GLY A 1 53  ? -5.978  28.499 -0.911  1.00 13.87 ? 53  GLY A CA  1 
ATOM   311  C  C   . GLY A 1 53  ? -6.643  27.187 -0.690  1.00 12.90 ? 53  GLY A C   1 
ATOM   312  O  O   . GLY A 1 53  ? -7.005  26.533 -1.627  1.00 13.39 ? 53  GLY A O   1 
ATOM   313  N  N   . GLU A 1 54  ? -6.920  26.865 0.564   1.00 15.09 ? 54  GLU A N   1 
ATOM   314  C  CA  . GLU A 1 54  ? -7.476  25.563 0.934   1.00 12.76 ? 54  GLU A CA  1 
ATOM   315  C  C   . GLU A 1 54  ? -8.881  25.652 1.403   1.00 12.86 ? 54  GLU A C   1 
ATOM   316  O  O   . GLU A 1 54  ? -9.270  26.619 2.018   1.00 15.50 ? 54  GLU A O   1 
ATOM   317  C  CB  . GLU A 1 54  ? -6.625  24.804 1.974   1.00 16.97 ? 54  GLU A CB  1 
ATOM   318  C  CG  . GLU A 1 54  ? -5.191  24.576 1.489   1.00 21.28 ? 54  GLU A CG  1 
ATOM   319  C  CD  . GLU A 1 54  ? -4.278  23.877 2.459   1.00 30.20 ? 54  GLU A CD  1 
ATOM   320  O  OE1 . GLU A 1 54  ? -4.578  23.792 3.627   1.00 40.99 ? 54  GLU A OE1 1 
ATOM   321  O  OE2 . GLU A 1 54  ? -3.204  23.458 2.035   1.00 36.54 ? 54  GLU A OE2 1 
ATOM   322  N  N   . LEU A 1 55  ? -9.652  24.606 1.114   1.00 12.87 ? 55  LEU A N   1 
ATOM   323  C  CA  . LEU A 1 55  ? -10.989 24.485 1.583   1.00 11.95 ? 55  LEU A CA  1 
ATOM   324  C  C   . LEU A 1 55  ? -11.158 23.190 2.298   1.00 14.03 ? 55  LEU A C   1 
ATOM   325  O  O   . LEU A 1 55  ? -11.097 22.139 1.665   1.00 13.95 ? 55  LEU A O   1 
ATOM   326  C  CB  . LEU A 1 55  ? -11.956 24.651 0.422   1.00 13.93 ? 55  LEU A CB  1 
ATOM   327  C  CG  . LEU A 1 55  ? -13.430 24.286 0.586   1.00 13.54 ? 55  LEU A CG  1 
ATOM   328  C  CD1 . LEU A 1 55  ? -13.983 25.076 1.773   1.00 13.51 ? 55  LEU A CD1 1 
ATOM   329  C  CD2 . LEU A 1 55  ? -14.210 24.611 -0.667  1.00 14.74 ? 55  LEU A CD2 1 
ATOM   330  N  N   . HIS A 1 56  ? -11.365 23.296 3.574   1.00 16.42 ? 56  HIS A N   1 
ATOM   331  C  CA  . HIS A 1 56  ? -11.598 22.185 4.499   1.00 19.40 ? 56  HIS A CA  1 
ATOM   332  C  C   . HIS A 1 56  ? -13.025 22.194 5.000   1.00 18.99 ? 56  HIS A C   1 
ATOM   333  O  O   . HIS A 1 56  ? -13.718 23.193 4.898   1.00 20.30 ? 56  HIS A O   1 
ATOM   334  C  CB  . HIS A 1 56  ? -10.639 22.254 5.720   1.00 21.50 ? 56  HIS A CB  1 
ATOM   335  C  CG  . HIS A 1 56  ? -9.187  22.096 5.369   1.00 23.72 ? 56  HIS A CG  1 
ATOM   336  N  ND1 . HIS A 1 56  ? -8.352  23.163 5.151   1.00 31.55 ? 56  HIS A ND1 1 
ATOM   337  C  CD2 . HIS A 1 56  ? -8.413  20.990 5.238   1.00 25.12 ? 56  HIS A CD2 1 
ATOM   338  C  CE1 . HIS A 1 56  ? -7.147  22.732 4.867   1.00 25.96 ? 56  HIS A CE1 1 
ATOM   339  N  NE2 . HIS A 1 56  ? -7.147  21.421 4.923   1.00 32.76 ? 56  HIS A NE2 1 
ATOM   340  N  N   . GLY A 1 57  ? -13.486 21.076 5.526   1.00 20.70 ? 57  GLY A N   1 
ATOM   341  C  CA  . GLY A 1 57  ? -14.772 21.024 6.187   1.00 21.06 ? 57  GLY A CA  1 
ATOM   342  C  C   . GLY A 1 57  ? -15.972 20.962 5.250   1.00 17.82 ? 57  GLY A C   1 
ATOM   343  O  O   . GLY A 1 57  ? -17.094 21.214 5.675   1.00 19.83 ? 57  GLY A O   1 
ATOM   344  N  N   . LEU A 1 58  ? -15.756 20.606 3.982   1.00 17.03 ? 58  LEU A N   1 
ATOM   345  C  CA  . LEU A 1 58  ? -16.865 20.410 3.086   1.00 15.72 ? 58  LEU A CA  1 
ATOM   346  C  C   . LEU A 1 58  ? -17.831 19.315 3.539   1.00 14.49 ? 58  LEU A C   1 
ATOM   347  O  O   . LEU A 1 58  ? -19.060 19.489 3.378   1.00 16.01 ? 58  LEU A O   1 
ATOM   348  C  CB  . LEU A 1 58  ? -16.445 20.129 1.669   1.00 13.89 ? 58  LEU A CB  1 
ATOM   349  C  CG  . LEU A 1 58  ? -16.021 21.321 0.820   1.00 14.40 ? 58  LEU A CG  1 
ATOM   350  C  CD1 . LEU A 1 58  ? -15.230 20.869 -0.417  1.00 15.11 ? 58  LEU A CD1 1 
ATOM   351  C  CD2 . LEU A 1 58  ? -17.194 22.185 0.410   1.00 17.84 ? 58  LEU A CD2 1 
ATOM   352  N  N   . THR A 1 59  ? -17.315 18.189 4.037   1.00 15.07 ? 59  THR A N   1 
ATOM   353  C  CA  . THR A 1 59  ? -18.182 17.046 4.355   1.00 13.96 ? 59  THR A CA  1 
ATOM   354  C  C   . THR A 1 59  ? -17.604 16.237 5.489   1.00 15.89 ? 59  THR A C   1 
ATOM   355  O  O   . THR A 1 59  ? -16.605 16.577 6.090   1.00 17.91 ? 59  THR A O   1 
ATOM   356  C  CB  . THR A 1 59  ? -18.434 16.212 3.081   1.00 15.50 ? 59  THR A CB  1 
ATOM   357  O  OG1 . THR A 1 59  ? -19.502 15.317 3.303   1.00 15.12 ? 59  THR A OG1 1 
ATOM   358  C  CG2 . THR A 1 59  ? -17.215 15.477 2.551   1.00 17.13 ? 59  THR A CG2 1 
ATOM   359  N  N   . THR A 1 60  ? -18.246 15.141 5.790   1.00 18.25 ? 60  THR A N   1 
ATOM   360  C  CA  . THR A 1 60  ? -17.848 14.281 6.890   1.00 14.65 ? 60  THR A CA  1 
ATOM   361  C  C   . THR A 1 60  ? -17.712 12.865 6.377   1.00 17.02 ? 60  THR A C   1 
ATOM   362  O  O   . THR A 1 60  ? -18.267 12.548 5.332   1.00 14.50 ? 60  THR A O   1 
ATOM   363  C  CB  . THR A 1 60  ? -18.880 14.266 8.028   1.00 15.15 ? 60  THR A CB  1 
ATOM   364  O  OG1 . THR A 1 60  ? -20.121 13.739 7.517   1.00 18.75 ? 60  THR A OG1 1 
ATOM   365  C  CG2 . THR A 1 60  ? -19.098 15.622 8.552   1.00 20.88 ? 60  THR A CG2 1 
ATOM   366  N  N   . GLU A 1 61  ? -17.140 11.995 7.178   1.00 18.22 ? 61  GLU A N   1 
ATOM   367  C  CA  . GLU A 1 61  ? -17.059 10.562 6.793   1.00 18.54 ? 61  GLU A CA  1 
ATOM   368  C  C   . GLU A 1 61  ? -18.443 9.951  6.652   1.00 17.81 ? 61  GLU A C   1 
ATOM   369  O  O   . GLU A 1 61  ? -18.664 9.072  5.827   1.00 19.89 ? 61  GLU A O   1 
ATOM   370  C  CB  . GLU A 1 61  ? -16.261 9.818  7.844   1.00 21.39 ? 61  GLU A CB  1 
ATOM   371  C  CG  . GLU A 1 61  ? -14.795 10.127 7.883   0.50 24.10 ? 61  GLU A CG  1 
ATOM   372  C  CD  . GLU A 1 61  ? -14.060 9.369  8.974   0.50 28.84 ? 61  GLU A CD  1 
ATOM   373  O  OE1 . GLU A 1 61  ? -14.693 8.816  9.904   0.50 34.20 ? 61  GLU A OE1 1 
ATOM   374  O  OE2 . GLU A 1 61  ? -12.825 9.316  8.878   0.50 34.98 ? 61  GLU A OE2 1 
ATOM   375  N  N   . GLU A 1 62  ? -19.415 10.397 7.450   1.00 14.71 ? 62  GLU A N   1 
ATOM   376  C  CA  . GLU A 1 62  ? -20.753 9.813  7.403   1.00 18.74 ? 62  GLU A CA  1 
ATOM   377  C  C   . GLU A 1 62  ? -21.507 10.243 6.149   1.00 18.08 ? 62  GLU A C   1 
ATOM   378  O  O   . GLU A 1 62  ? -22.191 9.475  5.518   1.00 17.81 ? 62  GLU A O   1 
ATOM   379  C  CB  . GLU A 1 62  ? -21.564 10.240 8.648   1.00 21.63 ? 62  GLU A CB  1 
ATOM   380  C  CG  . GLU A 1 62  ? -21.090 9.685  9.934   1.00 25.18 ? 62  GLU A CG  1 
ATOM   381  C  CD  . GLU A 1 62  ? -19.828 10.251 10.531  1.00 28.73 ? 62  GLU A CD  1 
ATOM   382  O  OE1 . GLU A 1 62  ? -19.521 11.433 10.259  1.00 29.58 ? 62  GLU A OE1 1 
ATOM   383  O  OE2 . GLU A 1 62  ? -19.159 9.513  11.328  1.00 41.60 ? 62  GLU A OE2 1 
ATOM   384  N  N   . GLU A 1 63  ? -21.366 11.515 5.784   1.00 14.90 ? 63  GLU A N   1 
ATOM   385  C  CA  . GLU A 1 63  ? -22.109 12.076 4.658   1.00 14.65 ? 63  GLU A CA  1 
ATOM   386  C  C   . GLU A 1 63  ? -21.559 11.693 3.270   1.00 12.45 ? 63  GLU A C   1 
ATOM   387  O  O   . GLU A 1 63  ? -22.263 11.592 2.313   1.00 12.66 ? 63  GLU A O   1 
ATOM   388  C  CB  . GLU A 1 63  ? -22.144 13.603 4.820   1.00 16.41 ? 63  GLU A CB  1 
ATOM   389  C  CG  . GLU A 1 63  ? -22.981 14.377 3.801   1.00 18.92 ? 63  GLU A CG  1 
ATOM   390  C  CD  . GLU A 1 63  ? -22.918 15.870 4.029   1.00 19.70 ? 63  GLU A CD  1 
ATOM   391  O  OE1 . GLU A 1 63  ? -23.970 16.379 4.480   1.00 23.87 ? 63  GLU A OE1 1 
ATOM   392  O  OE2 . GLU A 1 63  ? -21.862 16.541 3.769   1.00 23.23 ? 63  GLU A OE2 1 
ATOM   393  N  N   . PHE A 1 64  ? -20.250 11.488 3.216   1.00 12.60 ? 64  PHE A N   1 
ATOM   394  C  CA  . PHE A 1 64  ? -19.514 11.260 1.965   1.00 13.10 ? 64  PHE A CA  1 
ATOM   395  C  C   . PHE A 1 64  ? -19.528 9.812  1.571   1.00 13.37 ? 64  PHE A C   1 
ATOM   396  O  O   . PHE A 1 64  ? -18.537 9.108  1.705   1.00 14.93 ? 64  PHE A O   1 
ATOM   397  C  CB  . PHE A 1 64  ? -18.097 11.854 2.126   1.00 12.78 ? 64  PHE A CB  1 
ATOM   398  C  CG  . PHE A 1 64  ? -17.287 11.900 0.872   1.00 12.45 ? 64  PHE A CG  1 
ATOM   399  C  CD1 . PHE A 1 64  ? -17.772 12.484 -0.292  1.00 14.19 ? 64  PHE A CD1 1 
ATOM   400  C  CD2 . PHE A 1 64  ? -16.011 11.348 0.838   1.00 17.42 ? 64  PHE A CD2 1 
ATOM   401  C  CE1 . PHE A 1 64  ? -17.009 12.577 -1.429  1.00 16.45 ? 64  PHE A CE1 1 
ATOM   402  C  CE2 . PHE A 1 64  ? -15.250 11.396 -0.308  1.00 19.14 ? 64  PHE A CE2 1 
ATOM   403  C  CZ  . PHE A 1 64  ? -15.746 12.021 -1.434  1.00 14.32 ? 64  PHE A CZ  1 
ATOM   404  N  N   . VAL A 1 65  ? -20.668 9.404  1.108   1.00 11.47 ? 65  VAL A N   1 
ATOM   405  C  CA  . VAL A 1 65  ? -20.909 8.017  0.713   1.00 11.15 ? 65  VAL A CA  1 
ATOM   406  C  C   . VAL A 1 65  ? -20.387 7.779  -0.689  1.00 12.02 ? 65  VAL A C   1 
ATOM   407  O  O   . VAL A 1 65  ? -19.912 8.634  -1.383  1.00 12.78 ? 65  VAL A O   1 
ATOM   408  C  CB  . VAL A 1 65  ? -22.433 7.706  0.838   1.00 11.87 ? 65  VAL A CB  1 
ATOM   409  C  CG1 . VAL A 1 65  ? -22.906 7.795  2.264   1.00 13.43 ? 65  VAL A CG1 1 
ATOM   410  C  CG2 . VAL A 1 65  ? -23.278 8.614  -0.056  1.00 14.29 ? 65  VAL A CG2 1 
ATOM   411  N  N   . GLU A 1 66  ? -20.483 6.544  -1.170  1.00 12.00 ? 66  GLU A N   1 
ATOM   412  C  CA  . GLU A 1 66  ? -20.187 6.221  -2.565  1.00 12.28 ? 66  GLU A CA  1 
ATOM   413  C  C   . GLU A 1 66  ? -21.013 7.091  -3.471  1.00 12.49 ? 66  GLU A C   1 
ATOM   414  O  O   . GLU A 1 66  ? -22.149 7.427  -3.122  1.00 14.76 ? 66  GLU A O   1 
ATOM   415  C  CB  . GLU A 1 66  ? -20.575 4.768  -2.902  1.00 15.25 ? 66  GLU A CB  1 
ATOM   416  C  CG  . GLU A 1 66  ? -19.711 3.725  -2.234  1.00 16.09 ? 66  GLU A CG  1 
ATOM   417  C  CD  . GLU A 1 66  ? -20.022 2.364  -2.883  1.00 19.69 ? 66  GLU A CD  1 
ATOM   418  O  OE1 . GLU A 1 66  ? -20.784 1.566  -2.293  1.00 17.16 ? 66  GLU A OE1 1 
ATOM   419  O  OE2 . GLU A 1 66  ? -19.497 2.088  -3.974  1.00 19.25 ? 66  GLU A OE2 1 
ATOM   420  N  N   . GLY A 1 67  ? -20.483 7.427  -4.611  1.00 12.18 ? 67  GLY A N   1 
ATOM   421  C  CA  . GLY A 1 67  ? -21.225 8.132  -5.613  1.00 13.05 ? 67  GLY A CA  1 
ATOM   422  C  C   . GLY A 1 67  ? -20.355 8.697  -6.678  1.00 12.09 ? 67  GLY A C   1 
ATOM   423  O  O   . GLY A 1 67  ? -19.133 8.594  -6.600  1.00 12.15 ? 67  GLY A O   1 
ATOM   424  N  N   . ILE A 1 68  ? -20.977 9.384  -7.643  1.00 11.73 ? 68  ILE A N   1 
ATOM   425  C  CA  . ILE A 1 68  ? -20.262 10.155 -8.623  1.00 12.58 ? 68  ILE A CA  1 
ATOM   426  C  C   . ILE A 1 68  ? -20.428 11.621 -8.219  1.00 12.46 ? 68  ILE A C   1 
ATOM   427  O  O   . ILE A 1 68  ? -21.532 12.117 -8.040  1.00 13.37 ? 68  ILE A O   1 
ATOM   428  C  CB  . ILE A 1 68  ? -20.787 9.935  -10.053 1.00 12.39 ? 68  ILE A CB  1 
ATOM   429  C  CG1 . ILE A 1 68  ? -20.682 8.431  -10.443 1.00 16.78 ? 68  ILE A CG1 1 
ATOM   430  C  CG2 . ILE A 1 68  ? -20.027 10.845 -11.019 1.00 16.29 ? 68  ILE A CG2 1 
ATOM   431  C  CD1 . ILE A 1 68  ? -21.340 8.112  -11.785 1.00 20.10 ? 68  ILE A CD1 1 
ATOM   432  N  N   . TYR A 1 69  ? -19.310 12.278 -8.021  1.00 11.73 ? 69  TYR A N   1 
ATOM   433  C  CA  . TYR A 1 69  ? -19.254 13.645 -7.505  1.00 11.27 ? 69  TYR A CA  1 
ATOM   434  C  C   . TYR A 1 69  ? -18.689 14.594 -8.531  1.00 11.71 ? 69  TYR A C   1 
ATOM   435  O  O   . TYR A 1 69  ? -17.842 14.214 -9.324  1.00 12.46 ? 69  TYR A O   1 
ATOM   436  C  CB  . TYR A 1 69  ? -18.391 13.657 -6.225  1.00 12.23 ? 69  TYR A CB  1 
ATOM   437  C  CG  . TYR A 1 69  ? -19.033 13.032 -5.033  1.00 10.39 ? 69  TYR A CG  1 
ATOM   438  C  CD1 . TYR A 1 69  ? -18.926 11.663 -4.835  1.00 12.74 ? 69  TYR A CD1 1 
ATOM   439  C  CD2 . TYR A 1 69  ? -19.761 13.754 -4.130  1.00 13.34 ? 69  TYR A CD2 1 
ATOM   440  C  CE1 . TYR A 1 69  ? -19.515 11.045 -3.763  1.00 12.15 ? 69  TYR A CE1 1 
ATOM   441  C  CE2 . TYR A 1 69  ? -20.350 13.139 -3.034  1.00 11.97 ? 69  TYR A CE2 1 
ATOM   442  C  CZ  . TYR A 1 69  ? -20.216 11.777 -2.853  1.00 11.98 ? 69  TYR A CZ  1 
ATOM   443  O  OH  . TYR A 1 69  ? -20.831 11.189 -1.760  1.00 13.96 ? 69  TYR A OH  1 
ATOM   444  N  N   . LYS A 1 70  ? -19.167 15.826 -8.491  1.00 11.27 ? 70  LYS A N   1 
ATOM   445  C  CA  . LYS A 1 70  ? -18.624 16.900 -9.313  1.00 12.91 ? 70  LYS A CA  1 
ATOM   446  C  C   . LYS A 1 70  ? -18.227 18.075 -8.419  1.00 13.01 ? 70  LYS A C   1 
ATOM   447  O  O   . LYS A 1 70  ? -19.026 18.542 -7.638  1.00 14.02 ? 70  LYS A O   1 
ATOM   448  C  CB  . LYS A 1 70  ? -19.690 17.387 -10.282 1.00 14.08 ? 70  LYS A CB  1 
ATOM   449  C  CG  . LYS A 1 70  ? -19.307 18.676 -11.041 1.00 18.97 ? 70  LYS A CG  1 
ATOM   450  C  CD  . LYS A 1 70  ? -20.112 18.943 -12.250 1.00 25.10 ? 70  LYS A CD  1 
ATOM   451  C  CE  . LYS A 1 70  ? -21.562 19.000 -11.849 1.00 34.21 ? 70  LYS A CE  1 
ATOM   452  N  N   . VAL A 1 71  ? -17.010 18.531 -8.609  1.00 12.62 ? 71  VAL A N   1 
ATOM   453  C  CA  . VAL A 1 71  ? -16.469 19.689 -7.913  1.00 12.93 ? 71  VAL A CA  1 
ATOM   454  C  C   . VAL A 1 71  ? -16.319 20.775 -8.910  1.00 13.16 ? 71  VAL A C   1 
ATOM   455  O  O   . VAL A 1 71  ? -15.543 20.648 -9.867  1.00 15.73 ? 71  VAL A O   1 
ATOM   456  C  CB  . VAL A 1 71  ? -15.116 19.350 -7.242  1.00 13.94 ? 71  VAL A CB  1 
ATOM   457  C  CG1 . VAL A 1 71  ? -14.540 20.586 -6.546  1.00 15.37 ? 71  VAL A CG1 1 
ATOM   458  C  CG2 . VAL A 1 71  ? -15.278 18.198 -6.271  1.00 16.80 ? 71  VAL A CG2 1 
ATOM   459  N  N   . GLU A 1 72  ? -17.101 21.829 -8.721  1.00 13.63 ? 72  GLU A N   1 
ATOM   460  C  CA  . GLU A 1 72  ? -17.079 22.971 -9.647  1.00 14.00 ? 72  GLU A CA  1 
ATOM   461  C  C   . GLU A 1 72  ? -16.404 24.138 -8.982  1.00 12.40 ? 72  GLU A C   1 
ATOM   462  O  O   . GLU A 1 72  ? -16.910 24.674 -7.999  1.00 14.30 ? 72  GLU A O   1 
ATOM   463  C  CB  . GLU A 1 72  ? -18.498 23.357 -9.946  1.00 17.17 ? 72  GLU A CB  1 
ATOM   464  C  CG  . GLU A 1 72  ? -18.677 24.289 -11.037 1.00 23.35 ? 72  GLU A CG  1 
ATOM   465  C  CD  . GLU A 1 72  ? -20.141 24.671 -11.084 0.50 22.14 ? 72  GLU A CD  1 
ATOM   466  O  OE1 . GLU A 1 72  ? -20.880 23.930 -11.680 0.50 24.05 ? 72  GLU A OE1 1 
ATOM   467  O  OE2 . GLU A 1 72  ? -20.506 25.698 -10.453 0.50 36.40 ? 72  GLU A OE2 1 
ATOM   468  N  N   . ILE A 1 73  ? -15.269 24.548 -9.528  1.00 12.19 ? 73  ILE A N   1 
ATOM   469  C  CA  . ILE A 1 73  ? -14.487 25.639 -8.955  1.00 12.78 ? 73  ILE A CA  1 
ATOM   470  C  C   . ILE A 1 73  ? -14.774 26.915 -9.759  1.00 12.44 ? 73  ILE A C   1 
ATOM   471  O  O   . ILE A 1 73  ? -14.545 26.920 -10.976 1.00 12.67 ? 73  ILE A O   1 
ATOM   472  C  CB  . ILE A 1 73  ? -12.988 25.275 -8.962  1.00 13.30 ? 73  ILE A CB  1 
ATOM   473  C  CG1 . ILE A 1 73  ? -12.749 23.939 -8.222  1.00 13.94 ? 73  ILE A CG1 1 
ATOM   474  C  CG2 . ILE A 1 73  ? -12.141 26.438 -8.388  1.00 12.00 ? 73  ILE A CG2 1 
ATOM   475  C  CD1 . ILE A 1 73  ? -11.370 23.426 -8.408  1.00 16.37 ? 73  ILE A CD1 1 
ATOM   476  N  N   . ASP A 1 74  ? -15.217 27.976 -9.083  1.00 12.67 ? 74  ASP A N   1 
ATOM   477  C  CA  . ASP A 1 74  ? -15.631 29.193 -9.809  1.00 14.84 ? 74  ASP A CA  1 
ATOM   478  C  C   . ASP A 1 74  ? -14.443 30.078 -10.171 1.00 13.60 ? 74  ASP A C   1 
ATOM   479  O  O   . ASP A 1 74  ? -14.186 31.102 -9.580  1.00 13.20 ? 74  ASP A O   1 
ATOM   480  C  CB  . ASP A 1 74  ? -16.682 29.945 -9.039  1.00 13.90 ? 74  ASP A CB  1 
ATOM   481  C  CG  . ASP A 1 74  ? -17.164 31.198 -9.767  1.00 18.33 ? 74  ASP A CG  1 
ATOM   482  O  OD1 . ASP A 1 74  ? -16.878 31.366 -11.007 1.00 19.73 ? 74  ASP A OD1 1 
ATOM   483  O  OD2 . ASP A 1 74  ? -17.913 32.003 -9.121  1.00 23.87 ? 74  ASP A OD2 1 
ATOM   484  N  N   . THR A 1 75  ? -13.708 29.641 -11.157 1.00 13.56 ? 75  THR A N   1 
ATOM   485  C  CA  . THR A 1 75  ? -12.520 30.323 -11.621 1.00 13.88 ? 75  THR A CA  1 
ATOM   486  C  C   . THR A 1 75  ? -12.873 31.627 -12.323 1.00 13.37 ? 75  THR A C   1 
ATOM   487  O  O   . THR A 1 75  ? -12.124 32.597 -12.220 1.00 13.79 ? 75  THR A O   1 
ATOM   488  C  CB  . THR A 1 75  ? -11.695 29.422 -12.566 1.00 13.81 ? 75  THR A CB  1 
ATOM   489  O  OG1 . THR A 1 75  ? -12.479 29.067 -13.689 1.00 13.81 ? 75  THR A OG1 1 
ATOM   490  C  CG2 . THR A 1 75  ? -11.263 28.123 -11.918 1.00 15.11 ? 75  THR A CG2 1 
ATOM   491  N  N   . LYS A 1 76  ? -14.005 31.721 -12.986 1.00 14.09 ? 76  LYS A N   1 
ATOM   492  C  CA  . LYS A 1 76  ? -14.349 32.950 -13.689 1.00 14.85 ? 76  LYS A CA  1 
ATOM   493  C  C   . LYS A 1 76  ? -14.546 34.095 -12.714 1.00 14.87 ? 76  LYS A C   1 
ATOM   494  O  O   . LYS A 1 76  ? -13.986 35.214 -12.957 1.00 16.13 ? 76  LYS A O   1 
ATOM   495  C  CB  . LYS A 1 76  ? -15.628 32.750 -14.531 1.00 16.76 ? 76  LYS A CB  1 
ATOM   496  C  CG  . LYS A 1 76  ? -16.049 33.972 -15.360 1.00 20.80 ? 76  LYS A CG  1 
ATOM   497  C  CD  . LYS A 1 76  ? -17.222 33.647 -16.229 1.00 27.13 ? 76  LYS A CD  1 
ATOM   498  C  CE  . LYS A 1 76  ? -17.503 34.746 -17.202 0.50 26.43 ? 76  LYS A CE  1 
ATOM   499  N  NZ  . LYS A 1 76  ? -18.792 34.479 -17.894 0.50 36.74 ? 76  LYS A NZ  1 
ATOM   500  N  N   . SER A 1 77  ? -15.242 33.877 -11.624 1.00 16.59 ? 77  SER A N   1 
ATOM   501  C  CA  . SER A 1 77  ? -15.419 34.974 -10.630 1.00 17.34 ? 77  SER A CA  1 
ATOM   502  C  C   . SER A 1 77  ? -14.077 35.401 -10.049 1.00 18.55 ? 77  SER A C   1 
ATOM   503  O  O   . SER A 1 77  ? -13.870 36.609 -9.719  1.00 19.90 ? 77  SER A O   1 
ATOM   504  C  CB  . SER A 1 77  ? -16.344 34.582 -9.495  1.00 21.64 ? 77  SER A CB  1 
ATOM   505  O  OG  . SER A 1 77  ? -17.633 34.443 -10.016 1.00 21.85 ? 77  SER A OG  1 
ATOM   506  N  N   . TYR A 1 78  ? -13.186 34.447 -9.834  1.00 15.25 ? 78  TYR A N   1 
ATOM   507  C  CA  . TYR A 1 78  ? -11.862 34.708 -9.262  1.00 15.09 ? 78  TYR A CA  1 
ATOM   508  C  C   . TYR A 1 78  ? -11.109 35.691 -10.146 1.00 16.01 ? 78  TYR A C   1 
ATOM   509  O  O   . TYR A 1 78  ? -10.591 36.738 -9.680  1.00 16.91 ? 78  TYR A O   1 
ATOM   510  C  CB  . TYR A 1 78  ? -11.080 33.422 -9.060  1.00 13.92 ? 78  TYR A CB  1 
ATOM   511  C  CG  . TYR A 1 78  ? -9.657  33.641 -8.623  1.00 13.70 ? 78  TYR A CG  1 
ATOM   512  C  CD1 . TYR A 1 78  ? -9.362  33.957 -7.313  1.00 13.83 ? 78  TYR A CD1 1 
ATOM   513  C  CD2 . TYR A 1 78  ? -8.572  33.535 -9.512  1.00 12.92 ? 78  TYR A CD2 1 
ATOM   514  C  CE1 . TYR A 1 78  ? -8.084  34.177 -6.884  1.00 14.31 ? 78  TYR A CE1 1 
ATOM   515  C  CE2 . TYR A 1 78  ? -7.261  33.759 -9.065  1.00 14.55 ? 78  TYR A CE2 1 
ATOM   516  C  CZ  . TYR A 1 78  ? -7.027  34.058 -7.769  1.00 13.33 ? 78  TYR A CZ  1 
ATOM   517  O  OH  . TYR A 1 78  ? -5.770  34.288 -7.313  1.00 15.37 ? 78  TYR A OH  1 
ATOM   518  N  N   . TRP A 1 79  ? -11.028 35.371 -11.422 1.00 13.93 ? 79  TRP A N   1 
ATOM   519  C  CA  . TRP A 1 79  ? -10.307 36.229 -12.352 1.00 14.89 ? 79  TRP A CA  1 
ATOM   520  C  C   . TRP A 1 79  ? -11.012 37.572 -12.544 1.00 16.85 ? 79  TRP A C   1 
ATOM   521  O  O   . TRP A 1 79  ? -10.334 38.585 -12.570 1.00 21.27 ? 79  TRP A O   1 
ATOM   522  C  CB  . TRP A 1 79  ? -10.082 35.511 -13.703 1.00 14.63 ? 79  TRP A CB  1 
ATOM   523  C  CG  . TRP A 1 79  ? -9.149  34.355 -13.630 1.00 13.48 ? 79  TRP A CG  1 
ATOM   524  C  CD1 . TRP A 1 79  ? -9.430  33.017 -13.899 1.00 14.62 ? 79  TRP A CD1 1 
ATOM   525  C  CD2 . TRP A 1 79  ? -7.744  34.402 -13.344 1.00 13.23 ? 79  TRP A CD2 1 
ATOM   526  N  NE1 . TRP A 1 79  ? -8.322  32.279 -13.745 1.00 13.87 ? 79  TRP A NE1 1 
ATOM   527  C  CE2 . TRP A 1 79  ? -7.273  33.061 -13.393 1.00 13.62 ? 79  TRP A CE2 1 
ATOM   528  C  CE3 . TRP A 1 79  ? -6.857  35.417 -12.963 1.00 16.48 ? 79  TRP A CE3 1 
ATOM   529  C  CZ2 . TRP A 1 79  ? -5.985  32.721 -13.089 1.00 16.34 ? 79  TRP A CZ2 1 
ATOM   530  C  CZ3 . TRP A 1 79  ? -5.549  35.082 -12.711 1.00 17.57 ? 79  TRP A CZ3 1 
ATOM   531  C  CH2 . TRP A 1 79  ? -5.131  33.763 -12.738 1.00 16.20 ? 79  TRP A CH2 1 
ATOM   532  N  N   . LYS A 1 80  ? -12.306 37.605 -12.622 1.00 17.04 ? 80  LYS A N   1 
ATOM   533  C  CA  . LYS A 1 80  ? -13.056 38.863 -12.769 1.00 19.63 ? 80  LYS A CA  1 
ATOM   534  C  C   . LYS A 1 80  ? -12.866 39.802 -11.583 1.00 23.91 ? 80  LYS A C   1 
ATOM   535  O  O   . LYS A 1 80  ? -12.697 41.017 -11.763 1.00 24.40 ? 80  LYS A O   1 
ATOM   536  C  CB  . LYS A 1 80  ? -14.531 38.595 -13.041 1.00 19.76 ? 80  LYS A CB  1 
ATOM   537  C  CG  . LYS A 1 80  ? -14.750 38.097 -14.449 1.00 27.99 ? 80  LYS A CG  1 
ATOM   538  C  CD  . LYS A 1 80  ? -16.182 37.955 -14.920 0.50 26.10 ? 80  LYS A CD  1 
ATOM   539  C  CE  . LYS A 1 80  ? -16.279 37.399 -16.359 0.50 30.89 ? 80  LYS A CE  1 
ATOM   540  N  NZ  . LYS A 1 80  ? -15.638 38.020 -17.582 0.50 30.52 ? 80  LYS A NZ  1 
ATOM   541  N  N   . ALA A 1 81  ? -12.771 39.242 -10.383 1.00 23.63 ? 81  ALA A N   1 
ATOM   542  C  CA  . ALA A 1 81  ? -12.537 40.110 -9.189  1.00 20.25 ? 81  ALA A CA  1 
ATOM   543  C  C   . ALA A 1 81  ? -11.152 40.752 -9.239  1.00 22.85 ? 81  ALA A C   1 
ATOM   544  O  O   . ALA A 1 81  ? -10.942 41.824 -8.692  1.00 28.00 ? 81  ALA A O   1 
ATOM   545  C  CB  . ALA A 1 81  ? -12.697 39.291 -7.929  1.00 25.62 ? 81  ALA A CB  1 
ATOM   546  N  N   . LEU A 1 82  ? -10.217 40.105 -9.919  1.00 21.02 ? 82  LEU A N   1 
ATOM   547  C  CA  . LEU A 1 82  ? -8.859  40.637 -10.049 1.00 24.70 ? 82  LEU A CA  1 
ATOM   548  C  C   . LEU A 1 82  ? -8.748  41.553 -11.236 1.00 22.34 ? 82  LEU A C   1 
ATOM   549  O  O   . LEU A 1 82  ? -7.656  41.904 -11.650 1.00 29.35 ? 82  LEU A O   1 
ATOM   550  C  CB  . LEU A 1 82  ? -7.863  39.502 -10.195 1.00 20.19 ? 82  LEU A CB  1 
ATOM   551  C  CG  . LEU A 1 82  ? -7.746  38.723 -8.929  1.00 25.34 ? 82  LEU A CG  1 
ATOM   552  C  CD1 . LEU A 1 82  ? -6.952  37.440 -9.239  1.00 23.26 ? 82  LEU A CD1 1 
ATOM   553  C  CD2 . LEU A 1 82  ? -7.222  39.551 -7.752  1.00 26.38 ? 82  LEU A CD2 1 
ATOM   554  N  N   . GLY A 1 83  ? -9.888  41.788 -11.884 1.00 21.94 ? 83  GLY A N   1 
ATOM   555  C  CA  . GLY A 1 83  ? -9.980  42.701 -12.992 1.00 18.76 ? 83  GLY A CA  1 
ATOM   556  C  C   . GLY A 1 83  ? -9.580  42.107 -14.309 1.00 20.13 ? 83  GLY A C   1 
ATOM   557  O  O   . GLY A 1 83  ? -9.249  42.849 -15.202 1.00 27.66 ? 83  GLY A O   1 
ATOM   558  N  N   . ILE A 1 84  ? -9.607  40.747 -14.433 1.00 27.57 ? 84  ILE A N   1 
ATOM   559  C  CA  . ILE A 1 84  ? -9.090  40.030 -15.596 1.00 20.63 ? 84  ILE A CA  1 
ATOM   560  C  C   . ILE A 1 84  ? -10.288 39.294 -16.288 1.00 25.38 ? 84  ILE A C   1 
ATOM   561  O  O   . ILE A 1 84  ? -11.186 38.834 -15.590 1.00 23.87 ? 84  ILE A O   1 
ATOM   562  C  CB  . ILE A 1 84  ? -8.051  38.960 -15.113 1.00 23.85 ? 84  ILE A CB  1 
ATOM   563  C  CG1 . ILE A 1 84  ? -6.716  39.588 -14.656 1.00 32.92 ? 84  ILE A CG1 1 
ATOM   564  C  CG2 . ILE A 1 84  ? -7.724  37.970 -16.205 1.00 23.37 ? 84  ILE A CG2 1 
ATOM   565  C  CD1 . ILE A 1 84  ? -5.528  38.621 -14.799 1.00 46.29 ? 84  ILE A CD1 1 
ATOM   566  N  N   . SER A 1 85  ? -10.359 39.243 -17.618 1.00 19.95 ? 85  SER A N   1 
ATOM   567  C  CA  . SER A 1 85  ? -11.359 38.527 -18.350 1.00 19.66 ? 85  SER A CA  1 
ATOM   568  C  C   . SER A 1 85  ? -10.858 37.100 -18.745 1.00 20.31 ? 85  SER A C   1 
ATOM   569  O  O   . SER A 1 85  ? -10.060 36.919 -19.661 1.00 26.83 ? 85  SER A O   1 
ATOM   570  C  CB  . SER A 1 85  ? -11.656 39.222 -19.680 1.00 22.62 ? 85  SER A CB  1 
ATOM   571  O  OG  . SER A 1 85  ? -12.100 40.485 -19.505 1.00 31.21 ? 85  SER A OG  1 
ATOM   572  N  N   . PRO A 1 86  ? -11.332 36.051 -18.053 1.00 19.80 ? 86  PRO A N   1 
ATOM   573  C  CA  . PRO A 1 86  ? -10.771 34.753 -18.355 1.00 16.73 ? 86  PRO A CA  1 
ATOM   574  C  C   . PRO A 1 86  ? -11.506 33.957 -19.401 1.00 17.88 ? 86  PRO A C   1 
ATOM   575  O  O   . PRO A 1 86  ? -12.613 34.318 -19.780 1.00 19.54 ? 86  PRO A O   1 
ATOM   576  C  CB  . PRO A 1 86  ? -10.937 34.022 -17.025 1.00 19.95 ? 86  PRO A CB  1 
ATOM   577  C  CG  . PRO A 1 86  ? -12.288 34.509 -16.600 1.00 22.11 ? 86  PRO A CG  1 
ATOM   578  C  CD  . PRO A 1 86  ? -12.240 35.970 -16.918 1.00 22.49 ? 86  PRO A CD  1 
ATOM   579  N  N   . PHE A 1 87  ? -10.915 32.847 -19.835 1.00 15.41 ? 87  PHE A N   1 
ATOM   580  C  CA  . PHE A 1 87  ? -11.517 32.012 -20.861 1.00 17.22 ? 87  PHE A CA  1 
ATOM   581  C  C   . PHE A 1 87  ? -12.616 31.083 -20.343 1.00 16.96 ? 87  PHE A C   1 
ATOM   582  O  O   . PHE A 1 87  ? -13.715 31.007 -20.947 1.00 17.34 ? 87  PHE A O   1 
ATOM   583  C  CB  . PHE A 1 87  ? -10.447 31.212 -21.582 1.00 18.37 ? 87  PHE A CB  1 
ATOM   584  C  CG  . PHE A 1 87  ? -10.966 30.411 -22.725 1.00 20.08 ? 87  PHE A CG  1 
ATOM   585  C  CD1 . PHE A 1 87  ? -11.308 31.054 -23.902 1.00 21.03 ? 87  PHE A CD1 1 
ATOM   586  C  CD2 . PHE A 1 87  ? -11.095 29.068 -22.642 1.00 19.73 ? 87  PHE A CD2 1 
ATOM   587  C  CE1 . PHE A 1 87  ? -11.806 30.337 -24.978 1.00 24.12 ? 87  PHE A CE1 1 
ATOM   588  C  CE2 . PHE A 1 87  ? -11.643 28.324 -23.710 1.00 21.86 ? 87  PHE A CE2 1 
ATOM   589  C  CZ  . PHE A 1 87  ? -11.961 28.953 -24.890 1.00 21.51 ? 87  PHE A CZ  1 
ATOM   590  N  N   . HIS A 1 88  ? -12.328 30.328 -19.311 1.00 15.83 ? 88  HIS A N   1 
ATOM   591  C  CA  . HIS A 1 88  ? -13.263 29.273 -18.873 1.00 14.36 ? 88  HIS A CA  1 
ATOM   592  C  C   . HIS A 1 88  ? -14.349 29.797 -17.955 1.00 13.84 ? 88  HIS A C   1 
ATOM   593  O  O   . HIS A 1 88  ? -14.125 30.747 -17.206 1.00 14.95 ? 88  HIS A O   1 
ATOM   594  C  CB  . HIS A 1 88  ? -12.513 28.106 -18.124 1.00 13.95 ? 88  HIS A CB  1 
ATOM   595  C  CG  . HIS A 1 88  ? -11.448 27.505 -18.952 1.00 14.57 ? 88  HIS A CG  1 
ATOM   596  N  ND1 . HIS A 1 88  ? -10.147 27.938 -18.945 1.00 15.34 ? 88  HIS A ND1 1 
ATOM   597  C  CD2 . HIS A 1 88  ? -11.517 26.549 -19.909 1.00 16.04 ? 88  HIS A CD2 1 
ATOM   598  C  CE1 . HIS A 1 88  ? -9.440  27.229 -19.804 1.00 20.09 ? 88  HIS A CE1 1 
ATOM   599  N  NE2 . HIS A 1 88  ? -10.271 26.394 -20.421 1.00 18.46 ? 88  HIS A NE2 1 
ATOM   600  N  N   . GLU A 1 89  ? -15.501 29.163 -17.980 1.00 14.17 ? 89  GLU A N   1 
ATOM   601  C  CA  . GLU A 1 89  ? -16.555 29.456 -17.043 1.00 16.30 ? 89  GLU A CA  1 
ATOM   602  C  C   . GLU A 1 89  ? -16.230 28.953 -15.645 1.00 17.41 ? 89  GLU A C   1 
ATOM   603  O  O   . GLU A 1 89  ? -16.626 29.554 -14.631 1.00 18.83 ? 89  GLU A O   1 
ATOM   604  C  CB  . GLU A 1 89  ? -17.875 28.812 -17.498 1.00 18.85 ? 89  GLU A CB  1 
ATOM   605  C  CG  . GLU A 1 89  ? -18.428 29.473 -18.704 1.00 20.64 ? 89  GLU A CG  1 
ATOM   606  C  CD  . GLU A 1 89  ? -18.789 30.955 -18.460 1.00 23.04 ? 89  GLU A CD  1 
ATOM   607  O  OE1 . GLU A 1 89  ? -19.621 31.237 -17.602 1.00 30.79 ? 89  GLU A OE1 1 
ATOM   608  O  OE2 . GLU A 1 89  ? -18.232 31.788 -19.180 1.00 32.98 ? 89  GLU A OE2 1 
ATOM   609  N  N   . HIS A 1 90  ? -15.549 27.835 -15.600 1.00 15.60 ? 90  HIS A N   1 
ATOM   610  C  CA  . HIS A 1 90  ? -15.218 27.162 -14.330 1.00 15.98 ? 90  HIS A CA  1 
ATOM   611  C  C   . HIS A 1 90  ? -14.280 26.066 -14.589 1.00 17.23 ? 90  HIS A C   1 
ATOM   612  O  O   . HIS A 1 90  ? -13.929 25.817 -15.713 1.00 21.37 ? 90  HIS A O   1 
ATOM   613  C  CB  . HIS A 1 90  ? -16.481 26.640 -13.564 1.00 19.33 ? 90  HIS A CB  1 
ATOM   614  C  CG  . HIS A 1 90  ? -17.378 25.796 -14.377 1.00 29.29 ? 90  HIS A CG  1 
ATOM   615  N  ND1 . HIS A 1 90  ? -17.044 24.519 -14.765 1.00 35.13 ? 90  HIS A ND1 1 
ATOM   616  C  CD2 . HIS A 1 90  ? -18.635 26.015 -14.821 1.00 39.69 ? 90  HIS A CD2 1 
ATOM   617  C  CE1 . HIS A 1 90  ? -18.043 23.996 -15.446 1.00 33.50 ? 90  HIS A CE1 1 
ATOM   618  N  NE2 . HIS A 1 90  ? -19.018 24.891 -15.504 1.00 39.79 ? 90  HIS A NE2 1 
ATOM   619  N  N   . ALA A 1 91  ? -13.783 25.457 -13.544 1.00 16.90 ? 91  ALA A N   1 
ATOM   620  C  CA  . ALA A 1 91  ? -13.065 24.237 -13.684 1.00 17.27 ? 91  ALA A CA  1 
ATOM   621  C  C   . ALA A 1 91  ? -13.855 23.172 -12.954 1.00 19.50 ? 91  ALA A C   1 
ATOM   622  O  O   . ALA A 1 91  ? -14.170 23.359 -11.818 1.00 19.95 ? 91  ALA A O   1 
ATOM   623  C  CB  . ALA A 1 91  ? -11.691 24.387 -13.091 1.00 18.62 ? 91  ALA A CB  1 
ATOM   624  N  N   . GLU A 1 92  ? -14.252 22.082 -13.679 1.00 23.56 ? 92  GLU A N   1 
ATOM   625  C  CA  . GLU A 1 92  ? -15.061 20.973 -13.133 1.00 24.35 ? 92  GLU A CA  1 
ATOM   626  C  C   . GLU A 1 92  ? -14.208 19.714 -12.995 1.00 26.21 ? 92  GLU A C   1 
ATOM   627  O  O   . GLU A 1 92  ? -13.439 19.320 -13.916 1.00 55.42 ? 92  GLU A O   1 
ATOM   628  C  CB  . GLU A 1 92  ? -16.170 20.632 -14.125 1.00 33.95 ? 92  GLU A CB  1 
ATOM   629  C  CG  . GLU A 1 92  ? -17.515 21.281 -13.903 0.50 34.25 ? 92  GLU A CG  1 
ATOM   630  C  CD  . GLU A 1 92  ? -18.454 21.219 -15.139 0.50 33.70 ? 92  GLU A CD  1 
ATOM   631  O  OE1 . GLU A 1 92  ? -18.016 21.171 -16.318 0.50 28.59 ? 92  GLU A OE1 1 
ATOM   632  O  OE2 . GLU A 1 92  ? -19.659 21.340 -14.911 0.50 42.62 ? 92  GLU A OE2 1 
ATOM   633  N  N   . VAL A 1 93  ? -14.376 19.010 -11.878 1.00 19.74 ? 93  VAL A N   1 
ATOM   634  C  CA  . VAL A 1 93  ? -13.691 17.769 -11.675 1.00 17.69 ? 93  VAL A CA  1 
ATOM   635  C  C   . VAL A 1 93  ? -14.763 16.714 -11.345 1.00 13.98 ? 93  VAL A C   1 
ATOM   636  O  O   . VAL A 1 93  ? -15.506 16.901 -10.402 1.00 15.80 ? 93  VAL A O   1 
ATOM   637  C  CB  . VAL A 1 93  ? -12.745 17.937 -10.545 1.00 23.27 ? 93  VAL A CB  1 
ATOM   638  C  CG1 . VAL A 1 93  ? -12.014 16.635 -10.355 1.00 23.07 ? 93  VAL A CG1 1 
ATOM   639  C  CG2 . VAL A 1 93  ? -11.705 19.039 -10.878 1.00 28.59 ? 93  VAL A CG2 1 
ATOM   640  N  N   . VAL A 1 94  ? -14.878 15.679 -12.180 1.00 12.36 ? 94  VAL A N   1 
ATOM   641  C  CA  . VAL A 1 94  ? -15.954 14.639 -12.018 1.00 12.21 ? 94  VAL A CA  1 
ATOM   642  C  C   . VAL A 1 94  ? -15.307 13.274 -11.805 1.00 11.96 ? 94  VAL A C   1 
ATOM   643  O  O   . VAL A 1 94  ? -14.504 12.871 -12.586 1.00 12.27 ? 94  VAL A O   1 
ATOM   644  C  CB  . VAL A 1 94  ? -16.926 14.622 -13.215 1.00 14.12 ? 94  VAL A CB  1 
ATOM   645  C  CG1 . VAL A 1 94  ? -18.051 13.640 -12.969 1.00 14.67 ? 94  VAL A CG1 1 
ATOM   646  C  CG2 . VAL A 1 94  ? -17.523 16.006 -13.360 1.00 16.59 ? 94  VAL A CG2 1 
ATOM   647  N  N   . PHE A 1 95  ? -15.716 12.603 -10.717 1.00 11.34 ? 95  PHE A N   1 
ATOM   648  C  CA  . PHE A 1 95  ? -15.092 11.346 -10.323 1.00 11.85 ? 95  PHE A CA  1 
ATOM   649  C  C   . PHE A 1 95  ? -16.021 10.456 -9.525  1.00 9.86  ? 95  PHE A C   1 
ATOM   650  O  O   . PHE A 1 95  ? -16.864 10.928 -8.780  1.00 12.65 ? 95  PHE A O   1 
ATOM   651  C  CB  . PHE A 1 95  ? -13.781 11.578 -9.531  1.00 12.79 ? 95  PHE A CB  1 
ATOM   652  C  CG  . PHE A 1 95  ? -13.972 12.256 -8.203  1.00 14.44 ? 95  PHE A CG  1 
ATOM   653  C  CD1 . PHE A 1 95  ? -14.173 13.596 -8.121  1.00 14.91 ? 95  PHE A CD1 1 
ATOM   654  C  CD2 . PHE A 1 95  ? -13.896 11.534 -7.032  1.00 14.03 ? 95  PHE A CD2 1 
ATOM   655  C  CE1 . PHE A 1 95  ? -14.294 14.215 -6.866  1.00 19.26 ? 95  PHE A CE1 1 
ATOM   656  C  CE2 . PHE A 1 95  ? -14.039 12.117 -5.819  1.00 17.05 ? 95  PHE A CE2 1 
ATOM   657  C  CZ  . PHE A 1 95  ? -14.242 13.464 -5.737  1.00 17.33 ? 95  PHE A CZ  1 
ATOM   658  N  N   . THR A 1 96  ? -15.772 9.150  -9.582  1.00 12.37 ? 96  THR A N   1 
ATOM   659  C  CA  . THR A 1 96  ? -16.417 8.190  -8.717  1.00 12.64 ? 96  THR A CA  1 
ATOM   660  C  C   . THR A 1 96  ? -15.642 8.098  -7.429  1.00 13.35 ? 96  THR A C   1 
ATOM   661  O  O   . THR A 1 96  ? -14.433 7.885  -7.446  1.00 15.54 ? 96  THR A O   1 
ATOM   662  C  CB  . THR A 1 96  ? -16.514 6.799  -9.394  1.00 14.40 ? 96  THR A CB  1 
ATOM   663  O  OG1 . THR A 1 96  ? -17.320 6.893  -10.562 1.00 15.94 ? 96  THR A OG1 1 
ATOM   664  C  CG2 . THR A 1 96  ? -17.182 5.790  -8.465  1.00 17.14 ? 96  THR A CG2 1 
ATOM   665  N  N   . ALA A 1 97  ? -16.310 8.199  -6.294  1.00 12.56 ? 97  ALA A N   1 
ATOM   666  C  CA  . ALA A 1 97  ? -15.655 8.186  -4.982  1.00 13.25 ? 97  ALA A CA  1 
ATOM   667  C  C   . ALA A 1 97  ? -16.048 6.973  -4.157  1.00 12.92 ? 97  ALA A C   1 
ATOM   668  O  O   . ALA A 1 97  ? -17.183 6.514  -4.189  1.00 13.61 ? 97  ALA A O   1 
ATOM   669  C  CB  . ALA A 1 97  ? -16.040 9.420  -4.190  1.00 14.53 ? 97  ALA A CB  1 
ATOM   670  N  N   . ASN A 1 98  ? -15.103 6.470  -3.394  1.00 12.42 ? 98  ASN A N   1 
ATOM   671  C  CA  . ASN A 1 98  ? -15.372 5.454  -2.402  1.00 14.50 ? 98  ASN A CA  1 
ATOM   672  C  C   . ASN A 1 98  ? -15.786 4.061  -2.906  1.00 14.55 ? 98  ASN A C   1 
ATOM   673  O  O   . ASN A 1 98  ? -16.324 3.255  -2.133  1.00 17.55 ? 98  ASN A O   1 
ATOM   674  C  CB  . ASN A 1 98  ? -16.313 5.990  -1.317  1.00 13.25 ? 98  ASN A CB  1 
ATOM   675  C  CG  . ASN A 1 98  ? -15.919 7.316  -0.790  1.00 14.20 ? 98  ASN A CG  1 
ATOM   676  O  OD1 . ASN A 1 98  ? -16.745 8.291  -0.789  1.00 19.91 ? 98  ASN A OD1 1 
ATOM   677  N  ND2 . ASN A 1 98  ? -14.733 7.415  -0.358  1.00 11.62 ? 98  ASN A ND2 1 
ATOM   678  N  N   . ASP A 1 99  ? -15.543 3.755  -4.143  1.00 15.22 ? 99  ASP A N   1 
ATOM   679  C  CA  . ASP A 1 99  ? -16.042 2.475  -4.736  1.00 15.71 ? 99  ASP A CA  1 
ATOM   680  C  C   . ASP A 1 99  ? -15.444 1.228  -4.081  1.00 19.26 ? 99  ASP A C   1 
ATOM   681  O  O   . ASP A 1 99  ? -16.112 0.217  -4.041  1.00 18.78 ? 99  ASP A O   1 
ATOM   682  C  CB  . ASP A 1 99  ? -15.875 2.411  -6.247  1.00 21.32 ? 99  ASP A CB  1 
ATOM   683  C  CG  . ASP A 1 99  ? -16.520 1.158  -6.798  0.50 28.40 ? 99  ASP A CG  1 
ATOM   684  O  OD1 . ASP A 1 99  ? -17.713 0.896  -6.337  0.50 19.67 ? 99  ASP A OD1 1 
ATOM   685  O  OD2 . ASP A 1 99  ? -15.761 0.421  -7.537  0.50 33.38 ? 99  ASP A OD2 1 
ATOM   686  N  N   . SER A 1 100 ? -14.190 1.297  -3.659  1.00 20.57 ? 100 SER A N   1 
ATOM   687  C  CA  . SER A 1 100 ? -13.524 0.199  -2.997  1.00 21.59 ? 100 SER A CA  1 
ATOM   688  C  C   . SER A 1 100 ? -13.350 0.477  -1.496  1.00 23.24 ? 100 SER A C   1 
ATOM   689  O  O   . SER A 1 100 ? -12.377 0.057  -0.869  1.00 30.31 ? 100 SER A O   1 
ATOM   690  C  CB  . SER A 1 100 ? -12.173 -0.154 -3.621  1.00 28.78 ? 100 SER A CB  1 
ATOM   691  O  OG  . SER A 1 100 ? -12.352 -0.706 -4.916  1.00 38.63 ? 100 SER A OG  1 
ATOM   692  N  N   . GLY A 1 101 ? -14.278 1.255  -0.939  1.00 21.32 ? 101 GLY A N   1 
ATOM   693  C  CA  . GLY A 1 101 ? -14.199 1.671  0.433   1.00 23.51 ? 101 GLY A CA  1 
ATOM   694  C  C   . GLY A 1 101 ? -13.825 3.134  0.548   1.00 19.54 ? 101 GLY A C   1 
ATOM   695  O  O   . GLY A 1 101 ? -13.356 3.773  -0.391  1.00 18.36 ? 101 GLY A O   1 
ATOM   696  N  N   . PRO A 1 102 ? -13.948 3.655  1.776   1.00 17.29 ? 102 PRO A N   1 
ATOM   697  C  CA  . PRO A 1 102 ? -13.651 5.062  1.998   1.00 16.19 ? 102 PRO A CA  1 
ATOM   698  C  C   . PRO A 1 102 ? -12.221 5.440  1.702   1.00 19.26 ? 102 PRO A C   1 
ATOM   699  O  O   . PRO A 1 102 ? -11.274 4.681  2.082   1.00 18.75 ? 102 PRO A O   1 
ATOM   700  C  CB  . PRO A 1 102 ? -13.873 5.252  3.480   1.00 19.27 ? 102 PRO A CB  1 
ATOM   701  C  CG  . PRO A 1 102 ? -14.799 4.181  3.889   1.00 26.77 ? 102 PRO A CG  1 
ATOM   702  C  CD  . PRO A 1 102 ? -14.467 3.016  2.993   1.00 19.77 ? 102 PRO A CD  1 
ATOM   703  N  N   . ARG A 1 103 ? -12.054 6.589  1.039   1.00 15.53 ? 103 ARG A N   1 
ATOM   704  C  CA  . ARG A 1 103 ? -10.738 7.182  0.785   1.00 16.64 ? 103 ARG A CA  1 
ATOM   705  C  C   . ARG A 1 103 ? -10.755 8.661  1.141   1.00 15.90 ? 103 ARG A C   1 
ATOM   706  O  O   . ARG A 1 103 ? -11.844 9.250  1.279   1.00 16.55 ? 103 ARG A O   1 
ATOM   707  C  CB  . ARG A 1 103 ? -10.275 6.999  -0.661  1.00 16.20 ? 103 ARG A CB  1 
ATOM   708  C  CG  . ARG A 1 103 ? -10.242 5.582  -1.169  1.00 17.21 ? 103 ARG A CG  1 
ATOM   709  C  CD  . ARG A 1 103 ? -9.083  4.868  -0.489  1.00 18.13 ? 103 ARG A CD  1 
ATOM   710  N  NE  . ARG A 1 103 ? -8.885  3.542  -1.106  1.00 23.76 ? 103 ARG A NE  1 
ATOM   711  C  CZ  . ARG A 1 103 ? -9.486  2.422  -0.704  1.00 25.42 ? 103 ARG A CZ  1 
ATOM   712  N  NH1 . ARG A 1 103 ? -10.309 2.426  0.345   1.00 24.35 ? 103 ARG A NH1 1 
ATOM   713  N  NH2 . ARG A 1 103 ? -9.254  1.291  -1.353  1.00 27.94 ? 103 ARG A NH2 1 
ATOM   714  N  N   . ARG A 1 104 ? -9.584  9.259  1.297   1.00 16.42 ? 104 ARG A N   1 
ATOM   715  C  CA  . ARG A 1 104 ? -9.484  10.698 1.485   1.00 14.77 ? 104 ARG A CA  1 
ATOM   716  C  C   . ARG A 1 104 ? -9.035  11.255 0.138   1.00 12.68 ? 104 ARG A C   1 
ATOM   717  O  O   . ARG A 1 104 ? -8.060  10.783 -0.394  1.00 14.04 ? 104 ARG A O   1 
ATOM   718  C  CB  . ARG A 1 104 ? -8.440  11.013 2.504   1.00 18.75 ? 104 ARG A CB  1 
ATOM   719  N  N   . TYR A 1 105 ? -9.703  12.327 -0.374  1.00 12.66 ? 105 TYR A N   1 
ATOM   720  C  CA  . TYR A 1 105 ? -9.479  12.951 -1.675  1.00 13.66 ? 105 TYR A CA  1 
ATOM   721  C  C   . TYR A 1 105 ? -9.013  14.369 -1.521  1.00 13.37 ? 105 TYR A C   1 
ATOM   722  O  O   . TYR A 1 105 ? -9.707  15.160 -0.861  1.00 14.45 ? 105 TYR A O   1 
ATOM   723  C  CB  . TYR A 1 105 ? -10.752 12.939 -2.500  1.00 14.20 ? 105 TYR A CB  1 
ATOM   724  C  CG  . TYR A 1 105 ? -11.246 11.540 -2.795  1.00 13.29 ? 105 TYR A CG  1 
ATOM   725  C  CD1 . TYR A 1 105 ? -12.088 10.899 -1.956  1.00 13.64 ? 105 TYR A CD1 1 
ATOM   726  C  CD2 . TYR A 1 105 ? -10.896 10.896 -3.951  1.00 13.64 ? 105 TYR A CD2 1 
ATOM   727  C  CE1 . TYR A 1 105 ? -12.481 9.597  -2.204  1.00 14.99 ? 105 TYR A CE1 1 
ATOM   728  C  CE2 . TYR A 1 105 ? -11.306 9.577  -4.216  1.00 13.24 ? 105 TYR A CE2 1 
ATOM   729  C  CZ  . TYR A 1 105 ? -12.144 8.969  -3.327  1.00 12.73 ? 105 TYR A CZ  1 
ATOM   730  O  OH  . TYR A 1 105 ? -12.524 7.682  -3.572  1.00 14.68 ? 105 TYR A OH  1 
ATOM   731  N  N   . THR A 1 106 ? -7.896  14.733 -2.122  1.00 12.33 ? 106 THR A N   1 
ATOM   732  C  CA  . THR A 1 106 ? -7.539  16.156 -2.259  1.00 12.68 ? 106 THR A CA  1 
ATOM   733  C  C   . THR A 1 106 ? -7.582  16.482 -3.718  1.00 12.39 ? 106 THR A C   1 
ATOM   734  O  O   . THR A 1 106 ? -6.912  15.848 -4.513  1.00 13.21 ? 106 THR A O   1 
ATOM   735  C  CB  . THR A 1 106 ? -6.129  16.418 -1.696  1.00 14.02 ? 106 THR A CB  1 
ATOM   736  O  OG1 . THR A 1 106 ? -6.079  16.121 -0.285  1.00 20.08 ? 106 THR A OG1 1 
ATOM   737  C  CG2 . THR A 1 106 ? -5.719  17.827 -1.914  1.00 17.39 ? 106 THR A CG2 1 
ATOM   738  N  N   . ILE A 1 107 ? -8.364  17.470 -4.086  1.00 12.47 ? 107 ILE A N   1 
ATOM   739  C  CA  . ILE A 1 107 ? -8.484  17.965 -5.443  1.00 12.69 ? 107 ILE A CA  1 
ATOM   740  C  C   . ILE A 1 107 ? -7.729  19.291 -5.493  1.00 13.88 ? 107 ILE A C   1 
ATOM   741  O  O   . ILE A 1 107 ? -8.100  20.226 -4.846  1.00 15.10 ? 107 ILE A O   1 
ATOM   742  C  CB  . ILE A 1 107 ? -9.975  18.174 -5.825  1.00 14.63 ? 107 ILE A CB  1 
ATOM   743  C  CG1 . ILE A 1 107 ? -10.798 16.859 -5.612  1.00 17.55 ? 107 ILE A CG1 1 
ATOM   744  C  CG2 . ILE A 1 107 ? -10.101 18.724 -7.250  1.00 17.93 ? 107 ILE A CG2 1 
ATOM   745  C  CD1 . ILE A 1 107 ? -10.329 15.637 -6.396  1.00 18.68 ? 107 ILE A CD1 1 
ATOM   746  N  N   . ALA A 1 108 ? -6.678  19.324 -6.260  1.00 12.52 ? 108 ALA A N   1 
ATOM   747  C  CA  . ALA A 1 108 ? -5.890  20.541 -6.418  1.00 13.41 ? 108 ALA A CA  1 
ATOM   748  C  C   . ALA A 1 108 ? -6.103  21.112 -7.810  1.00 15.02 ? 108 ALA A C   1 
ATOM   749  O  O   . ALA A 1 108 ? -6.224  20.365 -8.785  1.00 17.92 ? 108 ALA A O   1 
ATOM   750  C  CB  . ALA A 1 108 ? -4.422  20.239 -6.194  1.00 18.91 ? 108 ALA A CB  1 
ATOM   751  N  N   . ALA A 1 109 ? -6.123  22.412 -7.897  1.00 13.05 ? 109 ALA A N   1 
ATOM   752  C  CA  . ALA A 1 109 ? -6.274  23.091 -9.204  1.00 13.43 ? 109 ALA A CA  1 
ATOM   753  C  C   . ALA A 1 109 ? -5.250  24.207 -9.290  1.00 12.34 ? 109 ALA A C   1 
ATOM   754  O  O   . ALA A 1 109 ? -5.011  24.926 -8.299  1.00 14.59 ? 109 ALA A O   1 
ATOM   755  C  CB  . ALA A 1 109 ? -7.671  23.642 -9.346  1.00 14.92 ? 109 ALA A CB  1 
ATOM   756  N  N   . LEU A 1 110 ? -4.669  24.354 -10.448 1.00 11.08 ? 110 LEU A N   1 
ATOM   757  C  CA  . LEU A 1 110 ? -3.694  25.409 -10.764 1.00 11.28 ? 110 LEU A CA  1 
ATOM   758  C  C   . LEU A 1 110 ? -4.289  26.250 -11.889 1.00 10.70 ? 110 LEU A C   1 
ATOM   759  O  O   . LEU A 1 110 ? -4.590  25.772 -12.950 1.00 13.21 ? 110 LEU A O   1 
ATOM   760  C  CB  . LEU A 1 110 ? -2.413  24.784 -11.249 1.00 14.16 ? 110 LEU A CB  1 
ATOM   761  C  CG  . LEU A 1 110 ? -1.291  25.733 -11.621 1.00 13.81 ? 110 LEU A CG  1 
ATOM   762  C  CD1 . LEU A 1 110 ? -0.803  26.501 -10.446 1.00 13.70 ? 110 LEU A CD1 1 
ATOM   763  C  CD2 . LEU A 1 110 ? -0.151  24.931 -12.210 1.00 21.96 ? 110 LEU A CD2 1 
ATOM   764  N  N   . LEU A 1 111 ? -4.422  27.534 -11.618 1.00 10.08 ? 111 LEU A N   1 
ATOM   765  C  CA  . LEU A 1 111 ? -5.185  28.437 -12.530 1.00 10.56 ? 111 LEU A CA  1 
ATOM   766  C  C   . LEU A 1 111 ? -4.350  29.486 -13.265 1.00 11.08 ? 111 LEU A C   1 
ATOM   767  O  O   . LEU A 1 111 ? -3.526  30.159 -12.649 1.00 10.76 ? 111 LEU A O   1 
ATOM   768  C  CB  . LEU A 1 111 ? -6.212  29.206 -11.707 1.00 11.35 ? 111 LEU A CB  1 
ATOM   769  C  CG  . LEU A 1 111 ? -7.138  28.414 -10.774 1.00 11.19 ? 111 LEU A CG  1 
ATOM   770  C  CD1 . LEU A 1 111 ? -8.162  29.369 -10.188 1.00 14.96 ? 111 LEU A CD1 1 
ATOM   771  C  CD2 . LEU A 1 111 ? -7.834  27.272 -11.513 1.00 13.91 ? 111 LEU A CD2 1 
ATOM   772  N  N   . SER A 1 112 ? -4.637  29.620 -14.534 1.00 11.04 ? 112 SER A N   1 
ATOM   773  C  CA  . SER A 1 112 ? -4.189  30.695 -15.371 1.00 11.11 ? 112 SER A CA  1 
ATOM   774  C  C   . SER A 1 112 ? -5.411  31.225 -16.125 1.00 12.54 ? 112 SER A C   1 
ATOM   775  O  O   . SER A 1 112 ? -6.414  30.579 -16.254 1.00 12.82 ? 112 SER A O   1 
ATOM   776  C  CB  . SER A 1 112 ? -3.094  30.270 -16.370 1.00 11.87 ? 112 SER A CB  1 
ATOM   777  O  OG  . SER A 1 112 ? -1.983  29.671 -15.734 1.00 15.96 ? 112 SER A OG  1 
ATOM   778  N  N   . PRO A 1 113 ? -5.314  32.445 -16.725 1.00 12.53 ? 113 PRO A N   1 
ATOM   779  C  CA  . PRO A 1 113 ? -6.495  32.969 -17.364 1.00 13.58 ? 113 PRO A CA  1 
ATOM   780  C  C   . PRO A 1 113 ? -7.015  32.115 -18.506 1.00 13.32 ? 113 PRO A C   1 
ATOM   781  O  O   . PRO A 1 113 ? -8.241  32.109 -18.721 1.00 14.53 ? 113 PRO A O   1 
ATOM   782  C  CB  . PRO A 1 113 ? -6.056  34.392 -17.806 1.00 16.61 ? 113 PRO A CB  1 
ATOM   783  C  CG  . PRO A 1 113 ? -5.123  34.833 -16.712 1.00 15.24 ? 113 PRO A CG  1 
ATOM   784  C  CD  . PRO A 1 113 ? -4.340  33.527 -16.507 1.00 14.17 ? 113 PRO A CD  1 
ATOM   785  N  N   . TYR A 1 114 ? -6.169  31.471 -19.283 1.00 12.54 ? 114 TYR A N   1 
ATOM   786  C  CA  . TYR A 1 114 ? -6.625  30.668 -20.434 1.00 13.82 ? 114 TYR A CA  1 
ATOM   787  C  C   . TYR A 1 114 ? -6.319  29.196 -20.231 1.00 12.81 ? 114 TYR A C   1 
ATOM   788  O  O   . TYR A 1 114 ? -6.331  28.443 -21.203 1.00 16.21 ? 114 TYR A O   1 
ATOM   789  C  CB  . TYR A 1 114 ? -6.038  31.180 -21.734 1.00 14.91 ? 114 TYR A CB  1 
ATOM   790  C  CG  . TYR A 1 114 ? -6.767  32.373 -22.321 1.00 13.99 ? 114 TYR A CG  1 
ATOM   791  C  CD1 . TYR A 1 114 ? -6.669  33.612 -21.718 1.00 18.42 ? 114 TYR A CD1 1 
ATOM   792  C  CD2 . TYR A 1 114 ? -7.586  32.245 -23.402 1.00 16.03 ? 114 TYR A CD2 1 
ATOM   793  C  CE1 . TYR A 1 114 ? -7.352  34.691 -22.233 1.00 25.60 ? 114 TYR A CE1 1 
ATOM   794  C  CE2 . TYR A 1 114 ? -8.285  33.297 -23.930 1.00 18.71 ? 114 TYR A CE2 1 
ATOM   795  C  CZ  . TYR A 1 114 ? -8.203  34.544 -23.356 1.00 20.66 ? 114 TYR A CZ  1 
ATOM   796  O  OH  . TYR A 1 114 ? -8.872  35.621 -23.919 1.00 44.05 ? 114 TYR A OH  1 
ATOM   797  N  N   . SER A 1 115 ? -6.051  28.757 -18.990 1.00 13.65 ? 115 SER A N   1 
ATOM   798  C  CA  . SER A 1 115 ? -5.606  27.371 -18.811 1.00 12.85 ? 115 SER A CA  1 
ATOM   799  C  C   . SER A 1 115 ? -5.835  26.968 -17.361 1.00 13.43 ? 115 SER A C   1 
ATOM   800  O  O   . SER A 1 115 ? -5.747  27.776 -16.479 1.00 14.76 ? 115 SER A O   1 
ATOM   801  C  CB  . SER A 1 115 ? -4.160  27.256 -19.114 1.00 16.23 ? 115 SER A CB  1 
ATOM   802  O  OG  . SER A 1 115 ? -3.717  25.925 -19.040 1.00 18.66 ? 115 SER A OG  1 
ATOM   803  N  N   . TYR A 1 116 ? -6.139  25.689 -17.129 1.00 11.65 ? 116 TYR A N   1 
ATOM   804  C  CA  . TYR A 1 116 ? -6.096  25.138 -15.754 1.00 11.74 ? 116 TYR A CA  1 
ATOM   805  C  C   . TYR A 1 116 ? -5.644  23.720 -15.785 1.00 10.46 ? 116 TYR A C   1 
ATOM   806  O  O   . TYR A 1 116 ? -5.810  23.000 -16.749 1.00 11.80 ? 116 TYR A O   1 
ATOM   807  C  CB  . TYR A 1 116 ? -7.403  25.286 -14.980 1.00 13.62 ? 116 TYR A CB  1 
ATOM   808  C  CG  . TYR A 1 116 ? -8.547  24.484 -15.518 1.00 14.75 ? 116 TYR A CG  1 
ATOM   809  C  CD1 . TYR A 1 116 ? -8.736  23.203 -15.142 1.00 16.85 ? 116 TYR A CD1 1 
ATOM   810  C  CD2 . TYR A 1 116 ? -9.382  25.053 -16.449 1.00 18.05 ? 116 TYR A CD2 1 
ATOM   811  C  CE1 . TYR A 1 116 ? -9.807  22.461 -15.672 1.00 18.14 ? 116 TYR A CE1 1 
ATOM   812  C  CE2 . TYR A 1 116 ? -10.402 24.389 -16.986 1.00 19.37 ? 116 TYR A CE2 1 
ATOM   813  C  CZ  . TYR A 1 116 ? -10.639 23.095 -16.602 1.00 17.86 ? 116 TYR A CZ  1 
ATOM   814  O  OH  . TYR A 1 116 ? -11.705 22.493 -17.239 1.00 21.48 ? 116 TYR A OH  1 
ATOM   815  N  N   . SER A 1 117 ? -5.037  23.326 -14.692 1.00 10.97 ? 117 SER A N   1 
ATOM   816  C  CA  A SER A 1 117 ? -4.833  21.897 -14.475 0.50 12.34 ? 117 SER A CA  1 
ATOM   817  C  CA  B SER A 1 117 ? -4.705  21.915 -14.416 0.25 12.66 ? 117 SER A CA  1 
ATOM   818  C  CA  C SER A 1 117 ? -4.694  21.931 -14.413 0.25 12.46 ? 117 SER A CA  1 
ATOM   819  C  C   . SER A 1 117 ? -5.390  21.427 -13.142 1.00 14.36 ? 117 SER A C   1 
ATOM   820  O  O   . SER A 1 117 ? -5.601  22.211 -12.240 1.00 15.47 ? 117 SER A O   1 
ATOM   821  C  CB  A SER A 1 117 ? -3.354  21.568 -14.557 0.50 18.06 ? 117 SER A CB  1 
ATOM   822  C  CB  B SER A 1 117 ? -3.188  21.749 -14.225 0.25 18.34 ? 117 SER A CB  1 
ATOM   823  C  CB  C SER A 1 117 ? -3.179  21.851 -14.216 0.25 15.46 ? 117 SER A CB  1 
ATOM   824  O  OG  A SER A 1 117 ? -2.729  22.108 -13.431 0.50 20.87 ? 117 SER A OG  1 
ATOM   825  O  OG  B SER A 1 117 ? -2.452  22.259 -15.324 0.25 21.10 ? 117 SER A OG  1 
ATOM   826  O  OG  C SER A 1 117 ? -2.743  20.515 -14.148 0.25 16.27 ? 117 SER A OG  1 
ATOM   827  N  N   . THR A 1 118 ? -5.756  20.166 -13.085 1.00 15.20 ? 118 THR A N   1 
ATOM   828  C  CA  . THR A 1 118 ? -6.299  19.599 -11.863 1.00 14.57 ? 118 THR A CA  1 
ATOM   829  C  C   . THR A 1 118 ? -5.623  18.271 -11.610 1.00 15.71 ? 118 THR A C   1 
ATOM   830  O  O   . THR A 1 118 ? -5.346  17.522 -12.541 1.00 17.29 ? 118 THR A O   1 
ATOM   831  C  CB  . THR A 1 118 ? -7.826  19.489 -11.899 1.00 17.33 ? 118 THR A CB  1 
ATOM   832  O  OG1 . THR A 1 118 ? -8.287  19.142 -10.638 1.00 19.54 ? 118 THR A OG1 1 
ATOM   833  C  CG2 . THR A 1 118 ? -8.412  18.543 -12.926 1.00 18.54 ? 118 THR A CG2 1 
ATOM   834  N  N   . THR A 1 119 ? -5.422  17.970 -10.336 1.00 13.66 ? 119 THR A N   1 
ATOM   835  C  CA  . THR A 1 119 ? -4.830  16.695 -9.920  1.00 14.00 ? 119 THR A CA  1 
ATOM   836  C  C   . THR A 1 119 ? -5.557  16.192 -8.718  1.00 12.00 ? 119 THR A C   1 
ATOM   837  O  O   . THR A 1 119 ? -6.107  16.926 -7.942  1.00 14.81 ? 119 THR A O   1 
ATOM   838  C  CB  . THR A 1 119 ? -3.335  16.862 -9.633  1.00 20.57 ? 119 THR A CB  1 
ATOM   839  O  OG1 . THR A 1 119 ? -2.776  17.609 -10.727 1.00 25.24 ? 119 THR A OG1 1 
ATOM   840  C  CG2 . THR A 1 119 ? -2.715  15.457 -9.511  1.00 23.94 ? 119 THR A CG2 1 
ATOM   841  N  N   . ALA A 1 120 ? -5.647  14.870 -8.596  1.00 13.65 ? 120 ALA A N   1 
ATOM   842  C  CA  . ALA A 1 120 ? -6.243  14.240 -7.409  1.00 12.72 ? 120 ALA A CA  1 
ATOM   843  C  C   . ALA A 1 120 ? -5.202  13.479 -6.658  1.00 13.13 ? 120 ALA A C   1 
ATOM   844  O  O   . ALA A 1 120 ? -4.411  12.759 -7.261  1.00 14.39 ? 120 ALA A O   1 
ATOM   845  C  CB  . ALA A 1 120 ? -7.357  13.342 -7.863  1.00 15.97 ? 120 ALA A CB  1 
ATOM   846  N  N   . VAL A 1 121 ? -5.173  13.647 -5.353  1.00 12.18 ? 121 VAL A N   1 
ATOM   847  C  CA  . VAL A 1 121 ? -4.350  12.831 -4.461  1.00 12.27 ? 121 VAL A CA  1 
ATOM   848  C  C   . VAL A 1 121 ? -5.287  12.019 -3.598  1.00 12.80 ? 121 VAL A C   1 
ATOM   849  O  O   . VAL A 1 121 ? -6.134  12.592 -2.894  1.00 15.37 ? 121 VAL A O   1 
ATOM   850  C  CB  . VAL A 1 121 ? -3.411  13.707 -3.595  1.00 15.49 ? 121 VAL A CB  1 
ATOM   851  C  CG1 . VAL A 1 121 ? -2.607  12.811 -2.670  1.00 19.91 ? 121 VAL A CG1 1 
ATOM   852  C  CG2 . VAL A 1 121 ? -2.513  14.588 -4.457  1.00 23.94 ? 121 VAL A CG2 1 
ATOM   853  N  N   . VAL A 1 122 ? -5.227  10.708 -3.703  1.00 13.17 ? 122 VAL A N   1 
ATOM   854  C  CA  . VAL A 1 122 ? -6.175  9.802  -3.047  1.00 13.53 ? 122 VAL A CA  1 
ATOM   855  C  C   . VAL A 1 122 ? -5.363  8.956  -2.071  1.00 14.19 ? 122 VAL A C   1 
ATOM   856  O  O   . VAL A 1 122 ? -4.420  8.290  -2.458  1.00 16.70 ? 122 VAL A O   1 
ATOM   857  C  CB  . VAL A 1 122 ? -6.902  8.938  -4.079  1.00 15.29 ? 122 VAL A CB  1 
ATOM   858  C  CG1 . VAL A 1 122 ? -7.913  8.024  -3.385  1.00 17.00 ? 122 VAL A CG1 1 
ATOM   859  C  CG2 . VAL A 1 122 ? -7.562  9.773  -5.152  1.00 16.44 ? 122 VAL A CG2 1 
ATOM   860  N  N   . THR A 1 123 ? -5.787  8.932  -0.825  1.00 13.36 ? 123 THR A N   1 
ATOM   861  C  CA  . THR A 1 123 ? -5.150  8.156  0.165   1.00 16.15 ? 123 THR A CA  1 
ATOM   862  C  C   . THR A 1 123 ? -6.085  7.302  1.000   1.00 21.12 ? 123 THR A C   1 
ATOM   863  O  O   . THR A 1 123 ? -7.256  7.586  1.073   1.00 16.99 ? 123 THR A O   1 
ATOM   864  C  CB  . THR A 1 123 ? -4.347  9.015  1.105   1.00 23.63 ? 123 THR A CB  1 
ATOM   865  O  OG1 . THR A 1 123 ? -5.212  9.878  1.833   1.00 32.52 ? 123 THR A OG1 1 
ATOM   866  C  CG2 . THR A 1 123 ? -3.339  9.815  0.366   1.00 30.66 ? 123 THR A CG2 1 
ATOM   867  N  N   . ASN A 1 124 ? -5.532  6.244  1.605   1.00 26.75 ? 124 ASN A N   1 
ATOM   868  C  CA  . ASN A 1 124 ? -6.290  5.261  2.371   1.00 26.74 ? 124 ASN A CA  1 
ATOM   869  C  C   . ASN A 1 124 ? -5.947  5.504  3.827   1.00 41.40 ? 124 ASN A C   1 
ATOM   870  O  O   . ASN A 1 124 ? -6.766  6.130  4.543   1.00 49.44 ? 124 ASN A O   1 
ATOM   871  C  CB  . ASN A 1 124 ? -5.959  3.818  1.921   1.00 32.00 ? 124 ASN A CB  1 
ATOM   872  C  CG  . ASN A 1 124 ? -7.029  2.825  2.368   1.00 29.84 ? 124 ASN A CG  1 
ATOM   873  O  OD1 . ASN A 1 124 ? -7.804  3.118  3.293   1.00 35.11 ? 124 ASN A OD1 1 
ATOM   874  N  ND2 . ASN A 1 124 ? -7.032  1.622  1.789   1.00 33.04 ? 124 ASN A ND2 1 
ATOM   875  C  C   . CYS B 1 10  ? -12.357 26.471 -37.682 1.00 40.45 ? 10  CYS B C   1 
ATOM   876  O  O   . CYS B 1 10  ? -11.296 26.628 -37.084 1.00 38.98 ? 10  CYS B O   1 
ATOM   877  N  N   . PRO B 1 11  ? -13.521 26.817 -37.132 1.00 27.61 ? 11  PRO B N   1 
ATOM   878  C  CA  . PRO B 1 11  ? -13.652 27.647 -35.949 1.00 25.34 ? 11  PRO B CA  1 
ATOM   879  C  C   . PRO B 1 11  ? -13.269 26.978 -34.664 1.00 24.62 ? 11  PRO B C   1 
ATOM   880  O  O   . PRO B 1 11  ? -12.850 27.679 -33.774 1.00 20.95 ? 11  PRO B O   1 
ATOM   881  C  CB  . PRO B 1 11  ? -15.128 28.025 -35.893 1.00 33.57 ? 11  PRO B CB  1 
ATOM   882  C  CG  . PRO B 1 11  ? -15.751 27.199 -36.905 1.00 35.87 ? 11  PRO B CG  1 
ATOM   883  C  CD  . PRO B 1 11  ? -14.738 26.785 -37.906 1.00 32.16 ? 11  PRO B CD  1 
ATOM   884  N  N   . LEU B 1 12  ? -13.427 25.649 -34.576 1.00 22.11 ? 12  LEU B N   1 
ATOM   885  C  CA  . LEU B 1 12  ? -13.241 24.926 -33.332 1.00 19.92 ? 12  LEU B CA  1 
ATOM   886  C  C   . LEU B 1 12  ? -12.515 23.659 -33.588 1.00 20.39 ? 12  LEU B C   1 
ATOM   887  O  O   . LEU B 1 12  ? -12.960 22.794 -34.384 1.00 26.37 ? 12  LEU B O   1 
ATOM   888  C  CB  . LEU B 1 12  ? -14.593 24.612 -32.678 1.00 23.18 ? 12  LEU B CB  1 
ATOM   889  C  CG  . LEU B 1 12  ? -14.528 23.876 -31.353 1.00 21.97 ? 12  LEU B CG  1 
ATOM   890  C  CD1 . LEU B 1 12  ? -13.828 24.673 -30.281 1.00 22.51 ? 12  LEU B CD1 1 
ATOM   891  C  CD2 . LEU B 1 12  ? -15.914 23.429 -30.896 1.00 26.78 ? 12  LEU B CD2 1 
ATOM   892  N  N   . MET B 1 13  ? -11.423 23.472 -32.880 1.00 17.53 ? 13  MET B N   1 
ATOM   893  C  CA  . MET B 1 13  ? -10.790 22.205 -32.937 1.00 19.42 ? 13  MET B CA  1 
ATOM   894  C  C   . MET B 1 13  ? -10.231 21.751 -31.606 1.00 17.32 ? 13  MET B C   1 
ATOM   895  O  O   . MET B 1 13  ? -10.046 22.542 -30.692 1.00 16.75 ? 13  MET B O   1 
ATOM   896  C  CB  . MET B 1 13  ? -9.882  22.257 -34.057 1.00 29.98 ? 13  MET B CB  1 
ATOM   897  C  CG  . MET B 1 13  ? -8.548  22.532 -33.794 0.80 25.69 ? 13  MET B CG  1 
ATOM   898  S  SD  . MET B 1 13  ? -8.081  20.912 -34.395 0.80 46.41 ? 13  MET B SD  1 
ATOM   899  C  CE  . MET B 1 13  ? -7.122  20.555 -32.998 0.80 14.83 ? 13  MET B CE  1 
ATOM   900  N  N   . VAL B 1 14  ? -10.086 20.439 -31.461 1.00 16.03 ? 14  VAL B N   1 
ATOM   901  C  CA  . VAL B 1 14  ? -9.705  19.831 -30.173 1.00 15.59 ? 14  VAL B CA  1 
ATOM   902  C  C   . VAL B 1 14  ? -8.474  18.970 -30.385 1.00 15.86 ? 14  VAL B C   1 
ATOM   903  O  O   . VAL B 1 14  ? -8.410  18.186 -31.368 1.00 19.61 ? 14  VAL B O   1 
ATOM   904  C  CB  . VAL B 1 14  ? -10.848 19.014 -29.570 1.00 16.53 ? 14  VAL B CB  1 
ATOM   905  C  CG1 . VAL B 1 14  ? -10.454 18.315 -28.314 1.00 16.69 ? 14  VAL B CG1 1 
ATOM   906  C  CG2 . VAL B 1 14  ? -12.091 19.895 -29.364 1.00 16.54 ? 14  VAL B CG2 1 
ATOM   907  N  N   . LYS B 1 15  ? -7.492  19.150 -29.515 1.00 15.20 ? 15  LYS B N   1 
ATOM   908  C  CA  . LYS B 1 15  ? -6.265  18.353 -29.559 1.00 16.56 ? 15  LYS B CA  1 
ATOM   909  C  C   . LYS B 1 15  ? -6.019  17.696 -28.205 1.00 15.58 ? 15  LYS B C   1 
ATOM   910  O  O   . LYS B 1 15  ? -6.104  18.341 -27.179 1.00 17.50 ? 15  LYS B O   1 
ATOM   911  C  CB  . LYS B 1 15  ? -5.052  19.219 -29.974 1.00 20.97 ? 15  LYS B CB  1 
ATOM   912  C  CG  . LYS B 1 15  ? -3.767  18.371 -30.140 1.00 26.17 ? 15  LYS B CG  1 
ATOM   913  C  CD  . LYS B 1 15  ? -2.557  19.204 -30.587 1.00 41.81 ? 15  LYS B CD  1 
ATOM   914  N  N   . VAL B 1 16  ? -5.710  16.394 -28.214 1.00 14.86 ? 16  VAL B N   1 
ATOM   915  C  CA  . VAL B 1 16  ? -5.509  15.620 -26.974 1.00 15.76 ? 16  VAL B CA  1 
ATOM   916  C  C   . VAL B 1 16  ? -4.181  14.895 -27.020 1.00 15.96 ? 16  VAL B C   1 
ATOM   917  O  O   . VAL B 1 16  ? -3.875  14.204 -27.979 1.00 16.02 ? 16  VAL B O   1 
ATOM   918  C  CB  . VAL B 1 16  ? -6.686  14.685 -26.693 1.00 16.57 ? 16  VAL B CB  1 
ATOM   919  C  CG1 . VAL B 1 16  ? -6.627  14.128 -25.281 1.00 15.82 ? 16  VAL B CG1 1 
ATOM   920  C  CG2 . VAL B 1 16  ? -8.005  15.395 -26.920 1.00 17.61 ? 16  VAL B CG2 1 
ATOM   921  N  N   . LEU B 1 17  ? -3.423  15.040 -25.940 1.00 13.82 ? 17  LEU B N   1 
ATOM   922  C  CA  . LEU B 1 17  ? -2.108  14.386 -25.731 1.00 13.39 ? 17  LEU B CA  1 
ATOM   923  C  C   . LEU B 1 17  ? -2.115  13.479 -24.487 1.00 11.27 ? 17  LEU B C   1 
ATOM   924  O  O   . LEU B 1 17  ? -2.848  13.695 -23.528 1.00 14.18 ? 17  LEU B O   1 
ATOM   925  C  CB  . LEU B 1 17  ? -0.971  15.414 -25.590 1.00 15.36 ? 17  LEU B CB  1 
ATOM   926  C  CG  . LEU B 1 17  ? -0.737  16.313 -26.842 1.00 18.76 ? 17  LEU B CG  1 
ATOM   927  C  CD1 . LEU B 1 17  ? 0.409   17.242 -26.493 1.00 23.42 ? 17  LEU B CD1 1 
ATOM   928  C  CD2 . LEU B 1 17  ? -0.416  15.529 -28.075 1.00 21.94 ? 17  LEU B CD2 1 
ATOM   929  N  N   . ASP B 1 18  ? -1.287  12.430 -24.555 1.00 12.44 ? 18  ASP B N   1 
ATOM   930  C  CA  . ASP B 1 18  ? -1.131  11.436 -23.492 1.00 11.43 ? 18  ASP B CA  1 
ATOM   931  C  C   . ASP B 1 18  ? 0.242   11.588 -22.854 1.00 11.19 ? 18  ASP B C   1 
ATOM   932  O  O   . ASP B 1 18  ? 1.276   11.384 -23.480 1.00 12.69 ? 18  ASP B O   1 
ATOM   933  C  CB  . ASP B 1 18  ? -1.322  10.052 -24.146 1.00 12.99 ? 18  ASP B CB  1 
ATOM   934  C  CG  . ASP B 1 18  ? -1.096  8.872  -23.213 1.00 14.13 ? 18  ASP B CG  1 
ATOM   935  O  OD1 . ASP B 1 18  ? -0.364  8.923  -22.234 1.00 13.29 ? 18  ASP B OD1 1 
ATOM   936  O  OD2 . ASP B 1 18  ? -1.647  7.802  -23.583 1.00 15.97 ? 18  ASP B OD2 1 
ATOM   937  N  N   . ALA B 1 19  ? 0.249   11.982 -21.591 1.00 11.42 ? 19  ALA B N   1 
ATOM   938  C  CA  . ALA B 1 19  ? 1.447   12.246 -20.810 1.00 11.84 ? 19  ALA B CA  1 
ATOM   939  C  C   . ALA B 1 19  ? 2.141   10.995 -20.273 1.00 12.60 ? 19  ALA B C   1 
ATOM   940  O  O   . ALA B 1 19  ? 3.234   11.111 -19.744 1.00 13.94 ? 19  ALA B O   1 
ATOM   941  C  CB  . ALA B 1 19  ? 1.118   13.174 -19.663 1.00 13.55 ? 19  ALA B CB  1 
ATOM   942  N  N   . VAL B 1 20  ? 1.458   9.846  -20.327 1.00 13.58 ? 20  VAL B N   1 
ATOM   943  C  CA  . VAL B 1 20  ? 2.037   8.582  -19.888 1.00 14.44 ? 20  VAL B CA  1 
ATOM   944  C  C   . VAL B 1 20  ? 2.869   7.926  -20.978 1.00 15.45 ? 20  VAL B C   1 
ATOM   945  O  O   . VAL B 1 20  ? 3.974   7.482  -20.738 1.00 19.98 ? 20  VAL B O   1 
ATOM   946  C  CB  . VAL B 1 20  ? 0.952   7.626  -19.413 1.00 15.40 ? 20  VAL B CB  1 
ATOM   947  C  CG1 . VAL B 1 20  ? 1.555   6.244  -19.106 1.00 18.62 ? 20  VAL B CG1 1 
ATOM   948  C  CG2 . VAL B 1 20  ? 0.298   8.182  -18.179 1.00 18.96 ? 20  VAL B CG2 1 
ATOM   949  N  N   . ARG B 1 21  ? 2.339   7.909  -22.162 1.00 14.77 ? 21  ARG B N   1 
ATOM   950  C  CA  . ARG B 1 21  ? 3.004   7.270  -23.298 1.00 17.03 ? 21  ARG B CA  1 
ATOM   951  C  C   . ARG B 1 21  ? 3.781   8.260  -24.169 1.00 15.79 ? 21  ARG B C   1 
ATOM   952  O  O   . ARG B 1 21  ? 4.533   7.856  -25.012 1.00 19.38 ? 21  ARG B O   1 
ATOM   953  C  CB  . ARG B 1 21  ? 1.999   6.493  -24.104 1.00 21.54 ? 21  ARG B CB  1 
ATOM   954  C  CG  . ARG B 1 21  ? 1.207   5.494  -23.228 0.50 19.89 ? 21  ARG B CG  1 
ATOM   955  C  CD  . ARG B 1 21  ? 0.421   4.497  -24.028 0.50 30.11 ? 21  ARG B CD  1 
ATOM   956  N  NE  . ARG B 1 21  ? -0.322  5.070  -25.151 0.50 29.33 ? 21  ARG B NE  1 
ATOM   957  N  N   . GLY B 1 22  ? 3.609   9.569  -23.953 1.00 14.54 ? 22  GLY B N   1 
ATOM   958  C  CA  . GLY B 1 22  ? 4.297   10.545 -24.779 1.00 15.76 ? 22  GLY B CA  1 
ATOM   959  C  C   . GLY B 1 22  ? 3.807   10.512 -26.205 1.00 15.74 ? 22  GLY B C   1 
ATOM   960  O  O   . GLY B 1 22  ? 4.611   10.409 -27.124 1.00 15.49 ? 22  GLY B O   1 
ATOM   961  N  N   . SER B 1 23  ? 2.513   10.568 -26.409 1.00 14.85 ? 23  SER B N   1 
ATOM   962  C  CA  . SER B 1 23  ? 1.931   10.375 -27.713 1.00 16.07 ? 23  SER B CA  1 
ATOM   963  C  C   . SER B 1 23  ? 0.658   11.203 -27.839 1.00 15.14 ? 23  SER B C   1 
ATOM   964  O  O   . SER B 1 23  ? 0.061   11.616 -26.884 1.00 16.14 ? 23  SER B O   1 
ATOM   965  C  CB  . SER B 1 23  ? 1.620   8.886  -27.952 1.00 21.81 ? 23  SER B CB  1 
ATOM   966  O  OG  . SER B 1 23  ? 0.485   8.540  -27.139 1.00 24.09 ? 23  SER B OG  1 
ATOM   967  N  N   . PRO B 1 24  ? 0.201   11.353 -29.062 1.00 15.04 ? 24  PRO B N   1 
ATOM   968  C  CA  . PRO B 1 24  ? -1.155  11.827 -29.263 1.00 15.76 ? 24  PRO B CA  1 
ATOM   969  C  C   . PRO B 1 24  ? -2.124  10.871 -28.623 1.00 15.13 ? 24  PRO B C   1 
ATOM   970  O  O   . PRO B 1 24  ? -1.843  9.693  -28.574 1.00 16.01 ? 24  PRO B O   1 
ATOM   971  C  CB  . PRO B 1 24  ? -1.341  11.852 -30.771 1.00 18.35 ? 24  PRO B CB  1 
ATOM   972  C  CG  . PRO B 1 24  ? 0.017   11.700 -31.307 1.00 25.86 ? 24  PRO B CG  1 
ATOM   973  C  CD  . PRO B 1 24  ? 0.889   11.099 -30.322 1.00 15.47 ? 24  PRO B CD  1 
ATOM   974  N  N   . ALA B 1 25  ? -3.264  11.334 -28.128 1.00 14.45 ? 25  ALA B N   1 
ATOM   975  C  CA  . ALA B 1 25  ? -4.301  10.469 -27.628 1.00 13.33 ? 25  ALA B CA  1 
ATOM   976  C  C   . ALA B 1 25  ? -5.293  10.188 -28.757 1.00 15.12 ? 25  ALA B C   1 
ATOM   977  O  O   . ALA B 1 25  ? -6.078  11.020 -29.152 1.00 15.53 ? 25  ALA B O   1 
ATOM   978  C  CB  . ALA B 1 25  ? -4.992  11.064 -26.419 1.00 14.18 ? 25  ALA B CB  1 
ATOM   979  N  N   . ILE B 1 26  ? -5.194  8.976  -29.289 1.00 15.78 ? 26  ILE B N   1 
ATOM   980  C  CA  . ILE B 1 26  ? -5.914  8.516  -30.476 1.00 16.39 ? 26  ILE B CA  1 
ATOM   981  C  C   . ILE B 1 26  ? -7.233  7.877  -30.124 1.00 15.70 ? 26  ILE B C   1 
ATOM   982  O  O   . ILE B 1 26  ? -7.343  7.119  -29.139 1.00 18.43 ? 26  ILE B O   1 
ATOM   983  C  CB  . ILE B 1 26  ? -5.005  7.532  -31.256 1.00 22.07 ? 26  ILE B CB  1 
ATOM   984  C  CG1 . ILE B 1 26  ? -3.654  8.223  -31.580 1.00 21.31 ? 26  ILE B CG1 1 
ATOM   985  C  CG2 . ILE B 1 26  ? -5.720  6.984  -32.454 1.00 22.05 ? 26  ILE B CG2 1 
ATOM   986  C  CD1 . ILE B 1 26  ? -2.556  7.349  -32.175 1.00 26.69 ? 26  ILE B CD1 1 
ATOM   987  N  N   . ASN B 1 27  ? -8.245  8.154  -30.946 1.00 17.40 ? 27  ASN B N   1 
ATOM   988  C  CA  . ASN B 1 27  ? -9.560  7.542  -30.803 1.00 19.78 ? 27  ASN B CA  1 
ATOM   989  C  C   . ASN B 1 27  ? -10.251 7.864  -29.494 1.00 18.75 ? 27  ASN B C   1 
ATOM   990  O  O   . ASN B 1 27  ? -11.027 7.065  -28.972 1.00 21.25 ? 27  ASN B O   1 
ATOM   991  C  CB  . ASN B 1 27  ? -9.442  6.027  -31.048 1.00 19.34 ? 27  ASN B CB  1 
ATOM   992  C  CG  . ASN B 1 27  ? -10.722 5.390  -31.442 1.00 34.59 ? 27  ASN B CG  1 
ATOM   993  O  OD1 . ASN B 1 27  ? -11.457 5.922  -32.247 1.00 44.27 ? 27  ASN B OD1 1 
ATOM   994  N  ND2 . ASN B 1 27  ? -10.983 4.215  -30.884 1.00 35.70 ? 27  ASN B ND2 1 
ATOM   995  N  N   . VAL B 1 28  ? -10.097 9.129  -29.058 1.00 16.40 ? 28  VAL B N   1 
ATOM   996  C  CA  . VAL B 1 28  ? -10.756 9.623  -27.909 1.00 17.03 ? 28  VAL B CA  1 
ATOM   997  C  C   . VAL B 1 28  ? -12.087 10.240 -28.361 1.00 15.47 ? 28  VAL B C   1 
ATOM   998  O  O   . VAL B 1 28  ? -12.097 11.098 -29.231 1.00 15.07 ? 28  VAL B O   1 
ATOM   999  C  CB  . VAL B 1 28  ? -9.951  10.692 -27.156 1.00 16.67 ? 28  VAL B CB  1 
ATOM   1000 C  CG1 . VAL B 1 28  ? -10.731 11.201 -25.928 1.00 22.99 ? 28  VAL B CG1 1 
ATOM   1001 C  CG2 . VAL B 1 28  ? -8.629  10.200 -26.704 1.00 19.94 ? 28  VAL B CG2 1 
ATOM   1002 N  N   . ALA B 1 29  ? -13.182 9.835  -27.721 1.00 16.30 ? 29  ALA B N   1 
ATOM   1003 C  CA  . ALA B 1 29  ? -14.498 10.429 -28.022 1.00 15.41 ? 29  ALA B CA  1 
ATOM   1004 C  C   . ALA B 1 29  ? -14.654 11.826 -27.378 1.00 16.08 ? 29  ALA B C   1 
ATOM   1005 O  O   . ALA B 1 29  ? -14.242 12.058 -26.242 1.00 15.73 ? 29  ALA B O   1 
ATOM   1006 C  CB  . ALA B 1 29  ? -15.615 9.530  -27.553 1.00 16.13 ? 29  ALA B CB  1 
ATOM   1007 N  N   . VAL B 1 30  ? -15.145 12.752 -28.180 1.00 15.07 ? 30  VAL B N   1 
ATOM   1008 C  CA  . VAL B 1 30  ? -15.358 14.131 -27.755 1.00 15.70 ? 30  VAL B CA  1 
ATOM   1009 C  C   . VAL B 1 30  ? -16.743 14.561 -28.124 1.00 15.39 ? 30  VAL B C   1 
ATOM   1010 O  O   . VAL B 1 30  ? -17.109 14.406 -29.280 1.00 16.61 ? 30  VAL B O   1 
ATOM   1011 C  CB  . VAL B 1 30  ? -14.344 15.056 -28.456 1.00 15.68 ? 30  VAL B CB  1 
ATOM   1012 C  CG1 . VAL B 1 30  ? -14.606 16.508 -28.057 1.00 18.10 ? 30  VAL B CG1 1 
ATOM   1013 C  CG2 . VAL B 1 30  ? -12.903 14.617 -28.212 1.00 17.14 ? 30  VAL B CG2 1 
ATOM   1014 N  N   . HIS B 1 31  ? -17.507 15.098 -27.174 1.00 16.16 ? 31  HIS B N   1 
ATOM   1015 C  CA  . HIS B 1 31  ? -18.819 15.649 -27.475 1.00 17.05 ? 31  HIS B CA  1 
ATOM   1016 C  C   . HIS B 1 31  ? -18.852 17.109 -27.112 1.00 16.98 ? 31  HIS B C   1 
ATOM   1017 O  O   . HIS B 1 31  ? -18.390 17.468 -26.045 1.00 19.57 ? 31  HIS B O   1 
ATOM   1018 C  CB  . HIS B 1 31  ? -19.902 14.922 -26.674 1.00 21.49 ? 31  HIS B CB  1 
ATOM   1019 C  CG  . HIS B 1 31  ? -20.141 13.514 -27.154 1.00 27.75 ? 31  HIS B CG  1 
ATOM   1020 N  ND1 . HIS B 1 31  ? -19.295 12.467 -26.860 1.00 30.55 ? 31  HIS B ND1 1 
ATOM   1021 C  CD2 . HIS B 1 31  ? -21.106 13.006 -27.954 1.00 28.36 ? 31  HIS B CD2 1 
ATOM   1022 C  CE1 . HIS B 1 31  ? -19.769 11.357 -27.419 1.00 28.53 ? 31  HIS B CE1 1 
ATOM   1023 N  NE2 . HIS B 1 31  ? -20.853 11.659 -28.109 1.00 32.82 ? 31  HIS B NE2 1 
ATOM   1024 N  N   . VAL B 1 32  ? -19.452 17.938 -27.976 1.00 16.29 ? 32  VAL B N   1 
ATOM   1025 C  CA  . VAL B 1 32  ? -19.571 19.372 -27.736 1.00 16.17 ? 32  VAL B CA  1 
ATOM   1026 C  C   . VAL B 1 32  ? -21.019 19.720 -27.622 1.00 16.62 ? 32  VAL B C   1 
ATOM   1027 O  O   . VAL B 1 32  ? -21.853 19.161 -28.371 1.00 21.13 ? 32  VAL B O   1 
ATOM   1028 C  CB  . VAL B 1 32  ? -18.960 20.189 -28.887 1.00 17.04 ? 32  VAL B CB  1 
ATOM   1029 C  CG1 . VAL B 1 32  ? -18.989 21.682 -28.557 1.00 18.26 ? 32  VAL B CG1 1 
ATOM   1030 C  CG2 . VAL B 1 32  ? -17.556 19.722 -29.253 1.00 18.00 ? 32  VAL B CG2 1 
ATOM   1031 N  N   . PHE B 1 33  ? -21.345 20.484 -26.598 1.00 18.28 ? 33  PHE B N   1 
ATOM   1032 C  CA  . PHE B 1 33  ? -22.702 20.937 -26.261 1.00 18.15 ? 33  PHE B CA  1 
ATOM   1033 C  C   . PHE B 1 33  ? -22.730 22.458 -26.268 1.00 21.46 ? 33  PHE B C   1 
ATOM   1034 O  O   . PHE B 1 33  ? -21.733 23.107 -26.040 1.00 19.34 ? 33  PHE B O   1 
ATOM   1035 C  CB  . PHE B 1 33  ? -23.085 20.383 -24.877 1.00 21.63 ? 33  PHE B CB  1 
ATOM   1036 C  CG  . PHE B 1 33  ? -22.995 18.899 -24.788 1.00 23.70 ? 33  PHE B CG  1 
ATOM   1037 C  CD1 . PHE B 1 33  ? -21.811 18.259 -24.383 1.00 22.46 ? 33  PHE B CD1 1 
ATOM   1038 C  CD2 . PHE B 1 33  ? -24.092 18.162 -25.097 1.00 29.98 ? 33  PHE B CD2 1 
ATOM   1039 C  CE1 . PHE B 1 33  ? -21.742 16.863 -24.254 1.00 25.06 ? 33  PHE B CE1 1 
ATOM   1040 C  CE2 . PHE B 1 33  ? -24.062 16.751 -25.023 1.00 31.69 ? 33  PHE B CE2 1 
ATOM   1041 C  CZ  . PHE B 1 33  ? -22.871 16.102 -24.613 1.00 27.11 ? 33  PHE B CZ  1 
ATOM   1042 N  N   . ARG B 1 34  ? -23.886 23.000 -26.583 1.00 23.11 ? 34  ARG B N   1 
ATOM   1043 C  CA  . ARG B 1 34  ? -24.167 24.426 -26.455 1.00 23.15 ? 34  ARG B CA  1 
ATOM   1044 C  C   . ARG B 1 34  ? -25.240 24.586 -25.371 1.00 21.82 ? 34  ARG B C   1 
ATOM   1045 O  O   . ARG B 1 34  ? -26.241 23.857 -25.336 1.00 25.67 ? 34  ARG B O   1 
ATOM   1046 C  CB  . ARG B 1 34  ? -24.606 24.996 -27.848 1.00 24.31 ? 34  ARG B CB  1 
ATOM   1047 C  CG  . ARG B 1 34  ? -24.769 26.502 -27.902 1.00 26.93 ? 34  ARG B CG  1 
ATOM   1048 C  CD  . ARG B 1 34  ? -24.979 27.102 -29.294 0.50 24.26 ? 34  ARG B CD  1 
ATOM   1049 N  NE  . ARG B 1 34  ? -25.007 28.529 -29.118 0.50 23.61 ? 34  ARG B NE  1 
ATOM   1050 C  CZ  . ARG B 1 34  ? -26.086 29.250 -28.835 0.50 25.75 ? 34  ARG B CZ  1 
ATOM   1051 N  NH1 . ARG B 1 34  ? -27.266 28.680 -28.779 0.50 27.11 ? 34  ARG B NH1 1 
ATOM   1052 N  NH2 . ARG B 1 34  ? -25.963 30.564 -28.649 0.50 25.98 ? 34  ARG B NH2 1 
ATOM   1053 N  N   . LYS B 1 35  ? -25.095 25.587 -24.550 1.00 19.74 ? 35  LYS B N   1 
ATOM   1054 C  CA  . LYS B 1 35  ? -26.097 25.875 -23.465 1.00 22.65 ? 35  LYS B CA  1 
ATOM   1055 C  C   . LYS B 1 35  ? -27.352 26.523 -24.063 1.00 26.39 ? 35  LYS B C   1 
ATOM   1056 O  O   . LYS B 1 35  ? -27.277 27.479 -24.791 1.00 26.99 ? 35  LYS B O   1 
ATOM   1057 C  CB  . LYS B 1 35  ? -25.491 26.775 -22.418 1.00 24.08 ? 35  LYS B CB  1 
ATOM   1058 C  CG  . LYS B 1 35  ? -26.194 26.679 -21.076 1.00 30.32 ? 35  LYS B CG  1 
ATOM   1059 C  CD  . LYS B 1 35  ? -25.543 27.601 -20.050 1.00 32.89 ? 35  LYS B CD  1 
ATOM   1060 N  N   . ALA B 1 36  ? -28.493 25.893 -23.808 1.00 26.26 ? 36  ALA B N   1 
ATOM   1061 C  CA  . ALA B 1 36  ? -29.768 26.390 -24.272 1.00 30.58 ? 36  ALA B CA  1 
ATOM   1062 C  C   . ALA B 1 36  ? -30.358 27.411 -23.308 1.00 31.69 ? 36  ALA B C   1 
ATOM   1063 O  O   . ALA B 1 36  ? -29.914 27.521 -22.169 1.00 29.66 ? 36  ALA B O   1 
ATOM   1064 C  CB  . ALA B 1 36  ? -30.745 25.246 -24.465 1.00 31.73 ? 36  ALA B CB  1 
ATOM   1065 N  N   . ALA B 1 37  ? -31.382 28.136 -23.777 1.00 33.91 ? 37  ALA B N   1 
ATOM   1066 C  CA  . ALA B 1 37  ? -32.088 29.180 -22.982 1.00 40.16 ? 37  ALA B CA  1 
ATOM   1067 C  C   . ALA B 1 37  ? -32.646 28.594 -21.692 1.00 36.88 ? 37  ALA B C   1 
ATOM   1068 O  O   . ALA B 1 37  ? -32.787 29.317 -20.745 1.00 41.40 ? 37  ALA B O   1 
ATOM   1069 C  CB  . ALA B 1 37  ? -33.229 29.787 -23.803 1.00 44.20 ? 37  ALA B CB  1 
ATOM   1070 N  N   . ASP B 1 38  ? -32.974 27.292 -21.737 1.00 37.80 ? 38  ASP B N   1 
ATOM   1071 C  CA  . ASP B 1 38  ? -33.270 26.341 -20.605 1.00 43.49 ? 38  ASP B CA  1 
ATOM   1072 C  C   . ASP B 1 38  ? -32.278 26.255 -19.432 1.00 43.14 ? 38  ASP B C   1 
ATOM   1073 O  O   . ASP B 1 38  ? -32.609 25.733 -18.353 1.00 43.30 ? 38  ASP B O   1 
ATOM   1074 C  CB  . ASP B 1 38  ? -33.240 24.866 -21.178 1.00 41.31 ? 38  ASP B CB  1 
ATOM   1075 C  CG  . ASP B 1 38  ? -34.557 24.203 -21.147 1.00 39.72 ? 38  ASP B CG  1 
ATOM   1076 O  OD1 . ASP B 1 38  ? -35.373 24.557 -20.282 1.00 68.99 ? 38  ASP B OD1 1 
ATOM   1077 O  OD2 . ASP B 1 38  ? -34.793 23.313 -21.987 1.00 44.17 ? 38  ASP B OD2 1 
ATOM   1078 N  N   . ASP B 1 39  ? -31.037 26.639 -19.707 1.00 40.31 ? 39  ASP B N   1 
ATOM   1079 C  CA  . ASP B 1 39  ? -29.865 26.227 -18.926 1.00 38.21 ? 39  ASP B CA  1 
ATOM   1080 C  C   . ASP B 1 39  ? -29.537 24.741 -19.044 1.00 32.10 ? 39  ASP B C   1 
ATOM   1081 O  O   . ASP B 1 39  ? -28.850 24.223 -18.151 1.00 49.31 ? 39  ASP B O   1 
ATOM   1082 C  CB  . ASP B 1 39  ? -29.999 26.614 -17.448 1.00 47.00 ? 39  ASP B CB  1 
ATOM   1083 N  N   . THR B 1 40  ? -29.999 24.054 -20.089 1.00 33.78 ? 40  THR B N   1 
ATOM   1084 C  CA  . THR B 1 40  ? -29.642 22.642 -20.295 1.00 31.46 ? 40  THR B CA  1 
ATOM   1085 C  C   . THR B 1 40  ? -28.630 22.609 -21.429 1.00 31.45 ? 40  THR B C   1 
ATOM   1086 O  O   . THR B 1 40  ? -28.507 23.557 -22.157 1.00 29.73 ? 40  THR B O   1 
ATOM   1087 C  CB  . THR B 1 40  ? -30.833 21.748 -20.670 1.00 37.45 ? 40  THR B CB  1 
ATOM   1088 O  OG1 . THR B 1 40  ? -31.359 22.120 -21.951 1.00 33.88 ? 40  THR B OG1 1 
ATOM   1089 C  CG2 . THR B 1 40  ? -31.904 21.798 -19.580 1.00 46.49 ? 40  THR B CG2 1 
ATOM   1090 N  N   . TRP B 1 41  ? -27.925 21.496 -21.562 1.00 30.94 ? 41  TRP B N   1 
ATOM   1091 C  CA  . TRP B 1 41  ? -26.866 21.372 -22.534 1.00 31.80 ? 41  TRP B CA  1 
ATOM   1092 C  C   . TRP B 1 41  ? -27.384 20.666 -23.750 1.00 30.24 ? 41  TRP B C   1 
ATOM   1093 O  O   . TRP B 1 41  ? -27.761 19.489 -23.636 1.00 43.39 ? 41  TRP B O   1 
ATOM   1094 C  CB  . TRP B 1 41  ? -25.725 20.550 -21.949 1.00 33.58 ? 41  TRP B CB  1 
ATOM   1095 C  CG  . TRP B 1 41  ? -24.959 21.286 -20.930 1.00 30.48 ? 41  TRP B CG  1 
ATOM   1096 C  CD1 . TRP B 1 41  ? -24.892 21.005 -19.606 1.00 36.05 ? 41  TRP B CD1 1 
ATOM   1097 C  CD2 . TRP B 1 41  ? -24.127 22.440 -21.147 1.00 27.28 ? 41  TRP B CD2 1 
ATOM   1098 N  NE1 . TRP B 1 41  ? -24.033 21.893 -18.976 1.00 36.18 ? 41  TRP B NE1 1 
ATOM   1099 C  CE2 . TRP B 1 41  ? -23.546 22.775 -19.910 1.00 32.08 ? 41  TRP B CE2 1 
ATOM   1100 C  CE3 . TRP B 1 41  ? -23.751 23.156 -22.279 1.00 28.04 ? 41  TRP B CE3 1 
ATOM   1101 C  CZ2 . TRP B 1 41  ? -22.693 23.860 -19.766 1.00 28.37 ? 41  TRP B CZ2 1 
ATOM   1102 C  CZ3 . TRP B 1 41  ? -22.887 24.245 -22.127 1.00 24.42 ? 41  TRP B CZ3 1 
ATOM   1103 C  CH2 . TRP B 1 41  ? -22.394 24.590 -20.900 1.00 23.96 ? 41  TRP B CH2 1 
ATOM   1104 N  N   . GLU B 1 42  ? -27.355 21.327 -24.902 1.00 30.27 ? 42  GLU B N   1 
ATOM   1105 C  CA  . GLU B 1 42  ? -27.833 20.755 -26.161 1.00 29.01 ? 42  GLU B CA  1 
ATOM   1106 C  C   . GLU B 1 42  ? -26.676 20.239 -27.013 1.00 35.86 ? 42  GLU B C   1 
ATOM   1107 O  O   . GLU B 1 42  ? -25.708 20.970 -27.277 1.00 25.95 ? 42  GLU B O   1 
ATOM   1108 C  CB  . GLU B 1 42  ? -28.543 21.842 -26.976 1.00 36.39 ? 42  GLU B CB  1 
ATOM   1109 C  CG  . GLU B 1 42  ? -29.663 22.507 -26.190 1.00 44.58 ? 42  GLU B CG  1 
ATOM   1110 C  CD  . GLU B 1 42  ? -30.917 22.666 -27.007 1.00 40.90 ? 42  GLU B CD  1 
ATOM   1111 O  OE1 . GLU B 1 42  ? -30.805 23.165 -28.147 1.00 68.89 ? 42  GLU B OE1 1 
ATOM   1112 O  OE2 . GLU B 1 42  ? -32.005 22.312 -26.495 1.00 47.13 ? 42  GLU B OE2 1 
ATOM   1113 N  N   . PRO B 1 43  ? -26.780 18.981 -27.495 1.00 31.76 ? 43  PRO B N   1 
ATOM   1114 C  CA  . PRO B 1 43  ? -25.758 18.451 -28.389 1.00 27.58 ? 43  PRO B CA  1 
ATOM   1115 C  C   . PRO B 1 43  ? -25.512 19.382 -29.552 1.00 24.33 ? 43  PRO B C   1 
ATOM   1116 O  O   . PRO B 1 43  ? -26.458 19.876 -30.134 1.00 29.91 ? 43  PRO B O   1 
ATOM   1117 C  CB  . PRO B 1 43  ? -26.349 17.141 -28.879 1.00 27.27 ? 43  PRO B CB  1 
ATOM   1118 C  CG  . PRO B 1 43  ? -27.269 16.710 -27.778 1.00 37.07 ? 43  PRO B CG  1 
ATOM   1119 C  CD  . PRO B 1 43  ? -27.696 17.929 -26.996 1.00 34.66 ? 43  PRO B CD  1 
ATOM   1120 N  N   . PHE B 1 44  ? -24.248 19.587 -29.868 1.00 24.88 ? 44  PHE B N   1 
ATOM   1121 C  CA  . PHE B 1 44  ? -23.785 20.501 -30.922 1.00 20.94 ? 44  PHE B CA  1 
ATOM   1122 C  C   . PHE B 1 44  ? -22.866 19.852 -31.992 1.00 20.72 ? 44  PHE B C   1 
ATOM   1123 O  O   . PHE B 1 44  ? -23.050 20.060 -33.234 1.00 26.19 ? 44  PHE B O   1 
ATOM   1124 C  CB  . PHE B 1 44  ? -23.087 21.711 -30.240 1.00 21.62 ? 44  PHE B CB  1 
ATOM   1125 C  CG  . PHE B 1 44  ? -22.619 22.772 -31.230 1.00 25.17 ? 44  PHE B CG  1 
ATOM   1126 C  CD1 . PHE B 1 44  ? -23.508 23.709 -31.737 1.00 25.65 ? 44  PHE B CD1 1 
ATOM   1127 C  CD2 . PHE B 1 44  ? -21.298 22.859 -31.576 1.00 22.10 ? 44  PHE B CD2 1 
ATOM   1128 C  CE1 . PHE B 1 44  ? -23.065 24.673 -32.625 1.00 28.02 ? 44  PHE B CE1 1 
ATOM   1129 C  CE2 . PHE B 1 44  ? -20.848 23.803 -32.465 1.00 26.49 ? 44  PHE B CE2 1 
ATOM   1130 C  CZ  . PHE B 1 44  ? -21.724 24.722 -32.983 1.00 25.57 ? 44  PHE B CZ  1 
ATOM   1131 N  N   . ALA B 1 45  ? -21.933 19.012 -31.563 1.00 22.37 ? 45  ALA B N   1 
ATOM   1132 C  CA  . ALA B 1 45  ? -20.973 18.382 -32.475 1.00 19.75 ? 45  ALA B CA  1 
ATOM   1133 C  C   . ALA B 1 45  ? -20.278 17.256 -31.720 1.00 20.51 ? 45  ALA B C   1 
ATOM   1134 O  O   . ALA B 1 45  ? -20.271 17.273 -30.479 1.00 20.12 ? 45  ALA B O   1 
ATOM   1135 C  CB  . ALA B 1 45  ? -19.951 19.382 -33.034 1.00 20.43 ? 45  ALA B CB  1 
ATOM   1136 N  N   . SER B 1 46  ? -19.773 16.253 -32.427 1.00 18.77 ? 46  SER B N   1 
ATOM   1137 C  CA  . SER B 1 46  ? -18.952 15.226 -31.774 1.00 16.44 ? 46  SER B CA  1 
ATOM   1138 C  C   . SER B 1 46  ? -18.070 14.513 -32.778 1.00 17.41 ? 46  SER B C   1 
ATOM   1139 O  O   . SER B 1 46  ? -18.201 14.683 -33.963 1.00 19.63 ? 46  SER B O   1 
ATOM   1140 C  CB  . SER B 1 46  ? -19.825 14.185 -31.015 1.00 16.60 ? 46  SER B CB  1 
ATOM   1141 O  OG  . SER B 1 46  ? -20.772 13.582 -31.817 1.00 19.45 ? 46  SER B OG  1 
ATOM   1142 N  N   . GLY B 1 47  ? -17.108 13.781 -32.276 1.00 15.66 ? 47  GLY B N   1 
ATOM   1143 C  CA  . GLY B 1 47  ? -16.202 13.028 -33.127 1.00 17.33 ? 47  GLY B CA  1 
ATOM   1144 C  C   . GLY B 1 47  ? -15.180 12.250 -32.263 1.00 15.35 ? 47  GLY B C   1 
ATOM   1145 O  O   . GLY B 1 47  ? -15.293 12.239 -31.063 1.00 19.41 ? 47  GLY B O   1 
ATOM   1146 N  N   . LYS B 1 48  ? -14.224 11.625 -32.934 1.00 17.27 ? 48  LYS B N   1 
ATOM   1147 C  CA  . LYS B 1 48  ? -13.134 10.773 -32.362 1.00 11.62 ? 48  LYS B CA  1 
ATOM   1148 C  C   . LYS B 1 48  ? -11.811 11.421 -32.760 1.00 16.31 ? 48  LYS B C   1 
ATOM   1149 O  O   . LYS B 1 48  ? -11.653 11.754 -33.917 1.00 18.45 ? 48  LYS B O   1 
ATOM   1150 C  CB  . LYS B 1 48  ? -13.183 9.247  -32.681 1.00 22.45 ? 48  LYS B CB  1 
ATOM   1151 C  CG  . LYS B 1 48  ? -14.406 8.595  -32.095 1.00 26.46 ? 48  LYS B CG  1 
ATOM   1152 C  CD  . LYS B 1 48  ? -14.163 7.979  -30.717 1.00 37.97 ? 48  LYS B CD  1 
ATOM   1153 N  N   . THR B 1 49  ? -10.886 11.684 -31.807 1.00 16.94 ? 49  THR B N   1 
ATOM   1154 C  CA  . THR B 1 49  ? -9.610  12.179 -32.263 1.00 15.91 ? 49  THR B CA  1 
ATOM   1155 C  C   . THR B 1 49  ? -8.926  11.215 -33.269 1.00 19.64 ? 49  THR B C   1 
ATOM   1156 O  O   . THR B 1 49  ? -9.048  10.012 -33.157 1.00 18.57 ? 49  THR B O   1 
ATOM   1157 C  CB  . THR B 1 49  ? -8.619  12.384 -31.131 1.00 16.04 ? 49  THR B CB  1 
ATOM   1158 O  OG1 . THR B 1 49  ? -8.462  11.157 -30.401 1.00 15.84 ? 49  THR B OG1 1 
ATOM   1159 C  CG2 . THR B 1 49  ? -9.105  13.455 -30.201 1.00 16.91 ? 49  THR B CG2 1 
ATOM   1160 N  N   . SER B 1 50  ? -8.139  11.776 -34.166 1.00 17.18 ? 50  SER B N   1 
ATOM   1161 C  CA  . SER B 1 50  ? -7.403  11.081 -35.211 1.00 18.58 ? 50  SER B CA  1 
ATOM   1162 C  C   . SER B 1 50  ? -6.082  10.522 -34.701 1.00 21.58 ? 50  SER B C   1 
ATOM   1163 O  O   . SER B 1 50  ? -5.758  10.655 -33.492 1.00 20.42 ? 50  SER B O   1 
ATOM   1164 C  CB  . SER B 1 50  ? -7.097  12.087 -36.345 1.00 21.41 ? 50  SER B CB  1 
ATOM   1165 O  OG  . SER B 1 50  ? -6.063  12.956 -35.933 1.00 23.40 ? 50  SER B OG  1 
ATOM   1166 N  N   . GLU B 1 51  ? -5.308  9.944  -35.617 1.00 22.93 ? 51  GLU B N   1 
ATOM   1167 C  CA  . GLU B 1 51  ? -3.971  9.448  -35.296 1.00 22.12 ? 51  GLU B CA  1 
ATOM   1168 C  C   . GLU B 1 51  ? -3.022  10.521 -34.796 1.00 21.32 ? 51  GLU B C   1 
ATOM   1169 O  O   . GLU B 1 51  ? -2.000  10.216 -34.180 1.00 23.50 ? 51  GLU B O   1 
ATOM   1170 C  CB  . GLU B 1 51  ? -3.304  8.768  -36.549 1.00 27.92 ? 51  GLU B CB  1 
ATOM   1171 N  N   . SER B 1 52  ? -3.315  11.766 -35.095 1.00 20.51 ? 52  SER B N   1 
ATOM   1172 C  CA  . SER B 1 52  ? -2.500  12.839 -34.619 1.00 21.37 ? 52  SER B CA  1 
ATOM   1173 C  C   . SER B 1 52  ? -3.074  13.445 -33.315 1.00 19.35 ? 52  SER B C   1 
ATOM   1174 O  O   . SER B 1 52  ? -2.577  14.467 -32.839 1.00 20.63 ? 52  SER B O   1 
ATOM   1175 C  CB  . SER B 1 52  ? -2.446  13.960 -35.666 1.00 26.45 ? 52  SER B CB  1 
ATOM   1176 O  OG  . SER B 1 52  ? -3.713  14.642 -35.795 1.00 30.40 ? 52  SER B OG  1 
ATOM   1177 N  N   . GLY B 1 53  ? -4.121  12.850 -32.765 1.00 18.14 ? 53  GLY B N   1 
ATOM   1178 C  CA  . GLY B 1 53  ? -4.690  13.399 -31.550 1.00 16.30 ? 53  GLY B CA  1 
ATOM   1179 C  C   . GLY B 1 53  ? -5.643  14.553 -31.763 1.00 17.35 ? 53  GLY B C   1 
ATOM   1180 O  O   . GLY B 1 53  ? -6.064  15.186 -30.820 1.00 17.16 ? 53  GLY B O   1 
ATOM   1181 N  N   . GLU B 1 54  ? -6.006  14.823 -33.010 1.00 18.77 ? 54  GLU B N   1 
ATOM   1182 C  CA  . GLU B 1 54  ? -6.777  16.020 -33.351 1.00 18.56 ? 54  GLU B CA  1 
ATOM   1183 C  C   . GLU B 1 54  ? -8.159  15.697 -33.866 1.00 17.60 ? 54  GLU B C   1 
ATOM   1184 O  O   . GLU B 1 54  ? -8.420  14.644 -34.442 1.00 20.27 ? 54  GLU B O   1 
ATOM   1185 C  CB  . GLU B 1 54  ? -6.036  16.894 -34.403 1.00 19.61 ? 54  GLU B CB  1 
ATOM   1186 C  CG  . GLU B 1 54  ? -4.674  17.404 -33.936 1.00 22.77 ? 54  GLU B CG  1 
ATOM   1187 C  CD  . GLU B 1 54  ? -3.906  18.233 -34.956 1.00 28.77 ? 54  GLU B CD  1 
ATOM   1188 O  OE1 . GLU B 1 54  ? -4.296  18.268 -36.114 1.00 45.22 ? 54  GLU B OE1 1 
ATOM   1189 O  OE2 . GLU B 1 54  ? -2.862  18.816 -34.613 1.00 39.99 ? 54  GLU B OE2 1 
ATOM   1190 N  N   . LEU B 1 55  ? -9.087  16.612 -33.637 1.00 18.13 ? 55  LEU B N   1 
ATOM   1191 C  CA  . LEU B 1 55  ? -10.429 16.462 -34.095 1.00 19.05 ? 55  LEU B CA  1 
ATOM   1192 C  C   . LEU B 1 55  ? -10.824 17.763 -34.772 1.00 22.29 ? 55  LEU B C   1 
ATOM   1193 O  O   . LEU B 1 55  ? -10.962 18.800 -34.091 1.00 20.26 ? 55  LEU B O   1 
ATOM   1194 C  CB  . LEU B 1 55  ? -11.349 16.107 -32.943 1.00 19.71 ? 55  LEU B CB  1 
ATOM   1195 C  CG  . LEU B 1 55  ? -12.840 16.022 -33.219 1.00 20.08 ? 55  LEU B CG  1 
ATOM   1196 C  CD1 . LEU B 1 55  ? -13.160 15.125 -34.404 1.00 21.68 ? 55  LEU B CD1 1 
ATOM   1197 C  CD2 . LEU B 1 55  ? -13.589 15.570 -31.973 1.00 21.99 ? 55  LEU B CD2 1 
ATOM   1198 N  N   . HIS B 1 56  ? -10.893 17.723 -36.098 1.00 21.58 ? 56  HIS B N   1 
ATOM   1199 C  CA  . HIS B 1 56  ? -11.193 18.867 -36.964 1.00 24.25 ? 56  HIS B CA  1 
ATOM   1200 C  C   . HIS B 1 56  ? -12.605 18.638 -37.488 1.00 25.12 ? 56  HIS B C   1 
ATOM   1201 O  O   . HIS B 1 56  ? -13.159 17.546 -37.392 1.00 28.32 ? 56  HIS B O   1 
ATOM   1202 C  CB  . HIS B 1 56  ? -10.201 18.881 -38.165 1.00 28.38 ? 56  HIS B CB  1 
ATOM   1203 C  CG  . HIS B 1 56  ? -8.801  19.248 -37.808 1.00 29.52 ? 56  HIS B CG  1 
ATOM   1204 N  ND1 . HIS B 1 56  ? -7.848  18.328 -37.459 1.00 42.58 ? 56  HIS B ND1 1 
ATOM   1205 C  CD2 . HIS B 1 56  ? -8.198  20.461 -37.729 1.00 33.47 ? 56  HIS B CD2 1 
ATOM   1206 C  CE1 . HIS B 1 56  ? -6.719  18.946 -37.175 1.00 36.16 ? 56  HIS B CE1 1 
ATOM   1207 N  NE2 . HIS B 1 56  ? -6.903  20.243 -37.346 1.00 44.81 ? 56  HIS B NE2 1 
ATOM   1208 N  N   . GLY B 1 57  ? -13.177 19.641 -38.076 1.00 26.72 ? 57  GLY B N   1 
ATOM   1209 C  CA  . GLY B 1 57  ? -14.443 19.477 -38.774 1.00 26.18 ? 57  GLY B CA  1 
ATOM   1210 C  C   . GLY B 1 57  ? -15.666 19.463 -37.901 1.00 23.11 ? 57  GLY B C   1 
ATOM   1211 O  O   . GLY B 1 57  ? -16.688 19.048 -38.339 1.00 32.54 ? 57  GLY B O   1 
ATOM   1212 N  N   . LEU B 1 58  ? -15.529 19.866 -36.642 1.00 23.91 ? 58  LEU B N   1 
ATOM   1213 C  CA  . LEU B 1 58  ? -16.623 19.857 -35.687 1.00 24.63 ? 58  LEU B CA  1 
ATOM   1214 C  C   . LEU B 1 58  ? -17.767 20.756 -36.097 1.00 25.16 ? 58  LEU B C   1 
ATOM   1215 O  O   . LEU B 1 58  ? -18.937 20.389 -35.986 1.00 28.11 ? 58  LEU B O   1 
ATOM   1216 C  CB  . LEU B 1 58  ? -16.113 20.253 -34.281 1.00 22.31 ? 58  LEU B CB  1 
ATOM   1217 C  CG  . LEU B 1 58  ? -15.436 19.095 -33.557 1.00 22.72 ? 58  LEU B CG  1 
ATOM   1218 C  CD1 . LEU B 1 58  ? -14.703 19.638 -32.379 1.00 25.47 ? 58  LEU B CD1 1 
ATOM   1219 C  CD2 . LEU B 1 58  ? -16.431 18.003 -33.166 1.00 22.96 ? 58  LEU B CD2 1 
ATOM   1220 N  N   . THR B 1 59  ? -17.425 21.946 -36.592 1.00 26.08 ? 59  THR B N   1 
ATOM   1221 C  CA  . THR B 1 59  ? -18.468 22.916 -36.907 1.00 25.35 ? 59  THR B CA  1 
ATOM   1222 C  C   . THR B 1 59  ? -18.089 23.808 -38.032 1.00 23.28 ? 59  THR B C   1 
ATOM   1223 O  O   . THR B 1 59  ? -17.046 23.638 -38.607 1.00 25.37 ? 59  THR B O   1 
ATOM   1224 C  CB  . THR B 1 59  ? -18.848 23.711 -35.650 1.00 25.85 ? 59  THR B CB  1 
ATOM   1225 O  OG1 . THR B 1 59  ? -20.052 24.433 -35.836 1.00 26.55 ? 59  THR B OG1 1 
ATOM   1226 C  CG2 . THR B 1 59  ? -17.746 24.686 -35.231 1.00 25.19 ? 59  THR B CG2 1 
ATOM   1227 N  N   . THR B 1 60  ? -18.977 24.761 -38.348 1.00 29.12 ? 60  THR B N   1 
ATOM   1228 C  CA  . THR B 1 60  ? -18.677 25.771 -39.361 1.00 26.60 ? 60  THR B CA  1 
ATOM   1229 C  C   . THR B 1 60  ? -18.850 27.147 -38.773 1.00 24.39 ? 60  THR B C   1 
ATOM   1230 O  O   . THR B 1 60  ? -19.469 27.280 -37.744 1.00 23.96 ? 60  THR B O   1 
ATOM   1231 C  CB  . THR B 1 60  ? -19.605 25.643 -40.581 1.00 30.33 ? 60  THR B CB  1 
ATOM   1232 O  OG1 . THR B 1 60  ? -20.980 25.842 -40.180 1.00 32.84 ? 60  THR B OG1 1 
ATOM   1233 C  CG2 . THR B 1 60  ? -19.443 24.235 -41.246 1.00 32.30 ? 60  THR B CG2 1 
ATOM   1234 N  N   . GLU B 1 61  ? -18.353 28.145 -39.496 1.00 27.61 ? 61  GLU B N   1 
ATOM   1235 C  CA  . GLU B 1 61  ? -18.444 29.517 -39.068 1.00 28.96 ? 61  GLU B CA  1 
ATOM   1236 C  C   . GLU B 1 61  ? -19.920 29.912 -38.871 1.00 27.32 ? 61  GLU B C   1 
ATOM   1237 O  O   . GLU B 1 61  ? -20.278 30.574 -37.887 1.00 26.45 ? 61  GLU B O   1 
ATOM   1238 C  CB  . GLU B 1 61  ? -17.831 30.440 -40.130 1.00 37.43 ? 61  GLU B CB  1 
ATOM   1239 C  CG  . GLU B 1 61  ? -16.336 30.306 -40.354 0.50 28.75 ? 61  GLU B CG  1 
ATOM   1240 C  CD  . GLU B 1 61  ? -15.823 31.368 -41.297 0.50 33.34 ? 61  GLU B CD  1 
ATOM   1241 O  OE1 . GLU B 1 61  ? -16.222 31.356 -42.474 0.50 37.47 ? 61  GLU B OE1 1 
ATOM   1242 O  OE2 . GLU B 1 61  ? -15.016 32.207 -40.867 0.50 43.65 ? 61  GLU B OE2 1 
ATOM   1243 N  N   . GLU B 1 62  ? -20.771 29.489 -39.803 1.00 24.85 ? 62  GLU B N   1 
ATOM   1244 C  CA  . GLU B 1 62  ? -22.156 29.920 -39.763 1.00 28.83 ? 62  GLU B CA  1 
ATOM   1245 C  C   . GLU B 1 62  ? -22.840 29.249 -38.524 1.00 28.27 ? 62  GLU B C   1 
ATOM   1246 O  O   . GLU B 1 62  ? -23.722 29.825 -37.925 1.00 35.80 ? 62  GLU B O   1 
ATOM   1247 C  CB  . GLU B 1 62  ? -22.915 29.659 -41.105 1.00 35.01 ? 62  GLU B CB  1 
ATOM   1248 N  N   . GLU B 1 63  ? -22.420 28.025 -38.150 1.00 29.02 ? 63  GLU B N   1 
ATOM   1249 C  CA  . GLU B 1 63  ? -23.084 27.316 -37.060 1.00 24.77 ? 63  GLU B CA  1 
ATOM   1250 C  C   . GLU B 1 63  ? -22.626 27.783 -35.678 1.00 22.40 ? 63  GLU B C   1 
ATOM   1251 O  O   . GLU B 1 63  ? -23.360 27.699 -34.684 1.00 27.10 ? 63  GLU B O   1 
ATOM   1252 C  CB  . GLU B 1 63  ? -22.917 25.760 -37.209 1.00 27.63 ? 63  GLU B CB  1 
ATOM   1253 C  CG  . GLU B 1 63  ? -23.456 25.176 -38.523 0.50 25.84 ? 63  GLU B CG  1 
ATOM   1254 C  CD  . GLU B 1 63  ? -23.033 23.721 -38.674 0.50 26.73 ? 63  GLU B CD  1 
ATOM   1255 O  OE1 . GLU B 1 63  ? -21.894 23.424 -39.094 0.50 27.96 ? 63  GLU B OE1 1 
ATOM   1256 O  OE2 . GLU B 1 63  ? -23.833 22.887 -38.286 0.50 31.02 ? 63  GLU B OE2 1 
ATOM   1257 N  N   . PHE B 1 64  ? -21.385 28.208 -35.602 1.00 20.60 ? 64  PHE B N   1 
ATOM   1258 C  CA  . PHE B 1 64  ? -20.723 28.453 -34.309 1.00 21.84 ? 64  PHE B CA  1 
ATOM   1259 C  C   . PHE B 1 64  ? -20.912 29.906 -33.863 1.00 24.64 ? 64  PHE B C   1 
ATOM   1260 O  O   . PHE B 1 64  ? -20.005 30.736 -33.922 1.00 29.69 ? 64  PHE B O   1 
ATOM   1261 C  CB  . PHE B 1 64  ? -19.236 28.109 -34.446 1.00 22.29 ? 64  PHE B CB  1 
ATOM   1262 C  CG  . PHE B 1 64  ? -18.462 28.119 -33.166 1.00 21.34 ? 64  PHE B CG  1 
ATOM   1263 C  CD1 . PHE B 1 64  ? -18.829 27.324 -32.101 1.00 23.78 ? 64  PHE B CD1 1 
ATOM   1264 C  CD2 . PHE B 1 64  ? -17.316 28.886 -33.049 1.00 31.12 ? 64  PHE B CD2 1 
ATOM   1265 C  CE1 . PHE B 1 64  ? -18.062 27.260 -30.943 1.00 24.54 ? 64  PHE B CE1 1 
ATOM   1266 C  CE2 . PHE B 1 64  ? -16.549 28.839 -31.891 1.00 39.01 ? 64  PHE B CE2 1 
ATOM   1267 C  CZ  . PHE B 1 64  ? -16.926 28.019 -30.833 1.00 25.72 ? 64  PHE B CZ  1 
ATOM   1268 N  N   . VAL B 1 65  ? -22.044 30.144 -33.285 1.00 17.32 ? 65  VAL B N   1 
ATOM   1269 C  CA  . VAL B 1 65  ? -22.444 31.473 -32.781 1.00 17.07 ? 65  VAL B CA  1 
ATOM   1270 C  C   . VAL B 1 65  ? -21.947 31.700 -31.373 1.00 23.39 ? 65  VAL B C   1 
ATOM   1271 O  O   . VAL B 1 65  ? -21.536 30.783 -30.708 1.00 22.00 ? 65  VAL B O   1 
ATOM   1272 C  CB  . VAL B 1 65  ? -24.024 31.614 -32.825 1.00 19.80 ? 65  VAL B CB  1 
ATOM   1273 C  CG1 . VAL B 1 65  ? -24.499 31.559 -34.295 1.00 24.22 ? 65  VAL B CG1 1 
ATOM   1274 C  CG2 . VAL B 1 65  ? -24.794 30.567 -31.953 1.00 24.07 ? 65  VAL B CG2 1 
ATOM   1275 N  N   . GLU B 1 66  ? -21.978 32.946 -30.955 1.00 18.98 ? 66  GLU B N   1 
ATOM   1276 C  CA  . GLU B 1 66  ? -21.690 33.268 -29.605 1.00 20.80 ? 66  GLU B CA  1 
ATOM   1277 C  C   . GLU B 1 66  ? -22.541 32.425 -28.645 1.00 20.63 ? 66  GLU B C   1 
ATOM   1278 O  O   . GLU B 1 66  ? -23.719 32.150 -28.899 1.00 26.39 ? 66  GLU B O   1 
ATOM   1279 C  CB  . GLU B 1 66  ? -21.892 34.790 -29.285 1.00 22.34 ? 66  GLU B CB  1 
ATOM   1280 C  CG  . GLU B 1 66  ? -20.901 35.689 -29.984 1.00 24.52 ? 66  GLU B CG  1 
ATOM   1281 C  CD  . GLU B 1 66  ? -21.068 37.151 -29.527 1.00 26.65 ? 66  GLU B CD  1 
ATOM   1282 O  OE1 . GLU B 1 66  ? -22.153 37.725 -29.678 1.00 26.38 ? 66  GLU B OE1 1 
ATOM   1283 O  OE2 . GLU B 1 66  ? -20.063 37.761 -29.138 1.00 33.87 ? 66  GLU B OE2 1 
ATOM   1284 N  N   . GLY B 1 67  ? -21.973 32.039 -27.529 1.00 20.73 ? 67  GLY B N   1 
ATOM   1285 C  CA  . GLY B 1 67  ? -22.718 31.308 -26.538 1.00 23.45 ? 67  GLY B CA  1 
ATOM   1286 C  C   . GLY B 1 67  ? -21.757 30.561 -25.615 1.00 22.47 ? 67  GLY B C   1 
ATOM   1287 O  O   . GLY B 1 67  ? -20.554 30.735 -25.709 1.00 21.54 ? 67  GLY B O   1 
ATOM   1288 N  N   . ILE B 1 68  ? -22.322 29.768 -24.732 1.00 20.10 ? 68  ILE B N   1 
ATOM   1289 C  CA  . ILE B 1 68  ? -21.555 28.999 -23.772 1.00 17.83 ? 68  ILE B CA  1 
ATOM   1290 C  C   . ILE B 1 68  ? -21.491 27.539 -24.268 1.00 16.58 ? 68  ILE B C   1 
ATOM   1291 O  O   . ILE B 1 68  ? -22.515 26.952 -24.590 1.00 18.26 ? 68  ILE B O   1 
ATOM   1292 C  CB  . ILE B 1 68  ? -22.140 29.021 -22.393 1.00 18.35 ? 68  ILE B CB  1 
ATOM   1293 C  CG1 . ILE B 1 68  ? -22.137 30.437 -21.827 1.00 23.49 ? 68  ILE B CG1 1 
ATOM   1294 C  CG2 . ILE B 1 68  ? -21.288 28.159 -21.459 1.00 19.28 ? 68  ILE B CG2 1 
ATOM   1295 C  CD1 . ILE B 1 68  ? -22.884 30.606 -20.545 1.00 26.39 ? 68  ILE B CD1 1 
ATOM   1296 N  N   . TYR B 1 69  ? -20.293 27.014 -24.421 1.00 17.07 ? 69  TYR B N   1 
ATOM   1297 C  CA  . TYR B 1 69  ? -20.044 25.685 -24.933 1.00 15.77 ? 69  TYR B CA  1 
ATOM   1298 C  C   . TYR B 1 69  ? -19.375 24.800 -23.922 1.00 15.06 ? 69  TYR B C   1 
ATOM   1299 O  O   . TYR B 1 69  ? -18.620 25.267 -23.096 1.00 16.82 ? 69  TYR B O   1 
ATOM   1300 C  CB  . TYR B 1 69  ? -19.208 25.775 -26.218 1.00 14.99 ? 69  TYR B CB  1 
ATOM   1301 C  CG  . TYR B 1 69  ? -19.944 26.411 -27.380 1.00 16.39 ? 69  TYR B CG  1 
ATOM   1302 C  CD1 . TYR B 1 69  ? -19.981 27.784 -27.533 1.00 16.45 ? 69  TYR B CD1 1 
ATOM   1303 C  CD2 . TYR B 1 69  ? -20.560 25.657 -28.353 1.00 18.36 ? 69  TYR B CD2 1 
ATOM   1304 C  CE1 . TYR B 1 69  ? -20.658 28.355 -28.587 1.00 19.45 ? 69  TYR B CE1 1 
ATOM   1305 C  CE2 . TYR B 1 69  ? -21.202 26.210 -29.440 1.00 19.19 ? 69  TYR B CE2 1 
ATOM   1306 C  CZ  . TYR B 1 69  ? -21.279 27.584 -29.553 1.00 19.57 ? 69  TYR B CZ  1 
ATOM   1307 O  OH  . TYR B 1 69  ? -21.978 28.138 -30.624 1.00 22.42 ? 69  TYR B OH  1 
ATOM   1308 N  N   . LYS B 1 70  ? -19.647 23.492 -24.019 1.00 15.31 ? 70  LYS B N   1 
ATOM   1309 C  CA  . LYS B 1 70  ? -18.997 22.463 -23.207 1.00 15.27 ? 70  LYS B CA  1 
ATOM   1310 C  C   . LYS B 1 70  ? -18.399 21.434 -24.120 1.00 16.00 ? 70  LYS B C   1 
ATOM   1311 O  O   . LYS B 1 70  ? -19.070 20.885 -24.950 1.00 17.39 ? 70  LYS B O   1 
ATOM   1312 C  CB  . LYS B 1 70  ? -19.995 21.814 -22.215 1.00 16.76 ? 70  LYS B CB  1 
ATOM   1313 C  CG  . LYS B 1 70  ? -19.373 20.678 -21.382 1.00 18.89 ? 70  LYS B CG  1 
ATOM   1314 C  CD  . LYS B 1 70  ? -20.318 20.190 -20.283 1.00 24.82 ? 70  LYS B CD  1 
ATOM   1315 C  CE  . LYS B 1 70  ? -21.520 19.483 -20.851 0.50 23.28 ? 70  LYS B CE  1 
ATOM   1316 N  NZ  . LYS B 1 70  ? -22.268 18.742 -19.785 0.50 29.34 ? 70  LYS B NZ  1 
ATOM   1317 N  N   . VAL B 1 71  ? -17.130 21.160 -23.888 1.00 15.24 ? 71  VAL B N   1 
ATOM   1318 C  CA  . VAL B 1 71  ? -16.421 20.116 -24.578 1.00 14.99 ? 71  VAL B CA  1 
ATOM   1319 C  C   . VAL B 1 71  ? -16.159 18.992 -23.555 1.00 14.46 ? 71  VAL B C   1 
ATOM   1320 O  O   . VAL B 1 71  ? -15.397 19.190 -22.632 1.00 17.32 ? 71  VAL B O   1 
ATOM   1321 C  CB  . VAL B 1 71  ? -15.108 20.597 -25.210 1.00 15.00 ? 71  VAL B CB  1 
ATOM   1322 C  CG1 . VAL B 1 71  ? -14.249 19.491 -25.846 1.00 17.91 ? 71  VAL B CG1 1 
ATOM   1323 C  CG2 . VAL B 1 71  ? -15.347 21.771 -26.158 1.00 16.83 ? 71  VAL B CG2 1 
ATOM   1324 N  N   . GLU B 1 72  ? -16.787 17.863 -23.752 1.00 15.81 ? 72  GLU B N   1 
ATOM   1325 C  CA  . GLU B 1 72  ? -16.600 16.708 -22.885 1.00 17.12 ? 72  GLU B CA  1 
ATOM   1326 C  C   . GLU B 1 72  ? -15.713 15.652 -23.570 1.00 16.18 ? 72  GLU B C   1 
ATOM   1327 O  O   . GLU B 1 72  ? -16.056 15.114 -24.596 1.00 16.29 ? 72  GLU B O   1 
ATOM   1328 C  CB  . GLU B 1 72  ? -17.974 16.097 -22.557 1.00 20.81 ? 72  GLU B CB  1 
ATOM   1329 C  CG  . GLU B 1 72  ? -17.934 15.075 -21.458 0.50 23.87 ? 72  GLU B CG  1 
ATOM   1330 C  CD  . GLU B 1 72  ? -19.289 14.487 -21.146 0.50 29.73 ? 72  GLU B CD  1 
ATOM   1331 O  OE1 . GLU B 1 72  ? -20.299 15.184 -21.195 0.50 30.69 ? 72  GLU B OE1 1 
ATOM   1332 O  OE2 . GLU B 1 72  ? -19.318 13.303 -20.815 0.50 27.43 ? 72  GLU B OE2 1 
ATOM   1333 N  N   . ILE B 1 73  ? -14.578 15.376 -22.955 1.00 15.52 ? 73  ILE B N   1 
ATOM   1334 C  CA  . ILE B 1 73  ? -13.585 14.467 -23.480 1.00 14.55 ? 73  ILE B CA  1 
ATOM   1335 C  C   . ILE B 1 73  ? -13.724 13.165 -22.685 1.00 16.12 ? 73  ILE B C   1 
ATOM   1336 O  O   . ILE B 1 73  ? -13.535 13.176 -21.475 1.00 15.13 ? 73  ILE B O   1 
ATOM   1337 C  CB  . ILE B 1 73  ? -12.210 15.085 -23.371 1.00 15.78 ? 73  ILE B CB  1 
ATOM   1338 C  CG1 . ILE B 1 73  ? -12.196 16.486 -24.054 1.00 18.00 ? 73  ILE B CG1 1 
ATOM   1339 C  CG2 . ILE B 1 73  ? -11.132 14.210 -23.947 1.00 16.10 ? 73  ILE B CG2 1 
ATOM   1340 C  CD1 . ILE B 1 73  ? -10.917 17.279 -23.860 1.00 19.74 ? 73  ILE B CD1 1 
ATOM   1341 N  N   . ASP B 1 74  ? -13.991 12.057 -23.357 1.00 14.88 ? 74  ASP B N   1 
ATOM   1342 C  CA  . ASP B 1 74  ? -14.178 10.762 -22.620 1.00 15.54 ? 74  ASP B CA  1 
ATOM   1343 C  C   . ASP B 1 74  ? -12.843 10.104 -22.233 1.00 14.39 ? 74  ASP B C   1 
ATOM   1344 O  O   . ASP B 1 74  ? -12.372 9.156  -22.848 1.00 15.45 ? 74  ASP B O   1 
ATOM   1345 C  CB  . ASP B 1 74  ? -15.071 9.803  -23.406 1.00 17.98 ? 74  ASP B CB  1 
ATOM   1346 C  CG  . ASP B 1 74  ? -15.383 8.551  -22.614 1.00 20.24 ? 74  ASP B CG  1 
ATOM   1347 O  OD1 . ASP B 1 74  ? -14.920 8.429  -21.443 1.00 20.31 ? 74  ASP B OD1 1 
ATOM   1348 O  OD2 . ASP B 1 74  ? -16.095 7.723  -23.185 1.00 25.22 ? 74  ASP B OD2 1 
ATOM   1349 N  N   . THR B 1 75  ? -12.203 10.658 -21.233 1.00 14.05 ? 75  THR B N   1 
ATOM   1350 C  CA  . THR B 1 75  ? -10.912 10.224 -20.787 1.00 13.70 ? 75  THR B CA  1 
ATOM   1351 C  C   . THR B 1 75  ? -10.947 8.821  -20.136 1.00 13.38 ? 75  THR B C   1 
ATOM   1352 O  O   . THR B 1 75  ? -10.044 8.053  -20.278 1.00 13.96 ? 75  THR B O   1 
ATOM   1353 C  CB  . THR B 1 75  ? -10.286 11.236 -19.801 1.00 14.54 ? 75  THR B CB  1 
ATOM   1354 O  OG1 . THR B 1 75  ? -11.121 11.382 -18.660 1.00 14.69 ? 75  THR B OG1 1 
ATOM   1355 C  CG2 . THR B 1 75  ? -10.081 12.596 -20.486 1.00 15.52 ? 75  THR B CG2 1 
ATOM   1356 N  N   . LYS B 1 76  ? -12.050 8.507  -19.433 1.00 14.45 ? 76  LYS B N   1 
ATOM   1357 C  CA  . LYS B 1 76  ? -12.105 7.247  -18.758 1.00 15.66 ? 76  LYS B CA  1 
ATOM   1358 C  C   . LYS B 1 76  ? -12.086 6.105  -19.753 1.00 15.95 ? 76  LYS B C   1 
ATOM   1359 O  O   . LYS B 1 76  ? -11.382 5.116  -19.507 1.00 16.64 ? 76  LYS B O   1 
ATOM   1360 C  CB  . LYS B 1 76  ? -13.377 7.186  -17.871 1.00 15.87 ? 76  LYS B CB  1 
ATOM   1361 C  CG  . LYS B 1 76  ? -13.477 5.964  -16.978 1.00 20.04 ? 76  LYS B CG  1 
ATOM   1362 C  CD  . LYS B 1 76  ? -14.784 5.996  -16.190 1.00 22.00 ? 76  LYS B CD  1 
ATOM   1363 C  CE  . LYS B 1 76  ? -14.706 5.013  -15.019 1.00 28.59 ? 76  LYS B CE  1 
ATOM   1364 N  NZ  . LYS B 1 76  ? -15.939 4.935  -14.223 1.00 32.17 ? 76  LYS B NZ  1 
ATOM   1365 N  N   . SER B 1 77  ? -12.815 6.216  -20.850 1.00 15.81 ? 77  SER B N   1 
ATOM   1366 C  CA  . SER B 1 77  ? -12.786 5.180  -21.885 1.00 16.81 ? 77  SER B CA  1 
ATOM   1367 C  C   . SER B 1 77  ? -11.436 5.040  -22.512 1.00 17.12 ? 77  SER B C   1 
ATOM   1368 O  O   . SER B 1 77  ? -10.984 3.910  -22.907 1.00 17.36 ? 77  SER B O   1 
ATOM   1369 C  CB  . SER B 1 77  ? -13.856 5.352  -22.925 1.00 17.35 ? 77  SER B CB  1 
ATOM   1370 O  OG  . SER B 1 77  ? -15.150 5.253  -22.371 1.00 24.27 ? 77  SER B OG  1 
ATOM   1371 N  N   . TYR B 1 78  ? -10.770 6.168  -22.712 1.00 16.17 ? 78  TYR B N   1 
ATOM   1372 C  CA  . TYR B 1 78  ? -9.431  6.150  -23.289 1.00 14.26 ? 78  TYR B CA  1 
ATOM   1373 C  C   . TYR B 1 78  ? -8.437  5.328  -22.428 1.00 14.59 ? 78  TYR B C   1 
ATOM   1374 O  O   . TYR B 1 78  ? -7.702  4.430  -22.938 1.00 17.07 ? 78  TYR B O   1 
ATOM   1375 C  CB  . TYR B 1 78  ? -8.928  7.606  -23.435 1.00 15.46 ? 78  TYR B CB  1 
ATOM   1376 C  CG  . TYR B 1 78  ? -7.490  7.650  -23.922 1.00 14.74 ? 78  TYR B CG  1 
ATOM   1377 C  CD1 . TYR B 1 78  ? -7.178  7.448  -25.255 1.00 15.23 ? 78  TYR B CD1 1 
ATOM   1378 C  CD2 . TYR B 1 78  ? -6.454  7.967  -23.054 1.00 14.92 ? 78  TYR B CD2 1 
ATOM   1379 C  CE1 . TYR B 1 78  ? -5.881  7.477  -25.697 1.00 16.48 ? 78  TYR B CE1 1 
ATOM   1380 C  CE2 . TYR B 1 78  ? -5.155  8.036  -23.492 1.00 14.20 ? 78  TYR B CE2 1 
ATOM   1381 C  CZ  . TYR B 1 78  ? -4.869  7.767  -24.802 1.00 15.98 ? 78  TYR B CZ  1 
ATOM   1382 O  OH  . TYR B 1 78  ? -3.603  7.781  -25.321 1.00 15.97 ? 78  TYR B OH  1 
ATOM   1383 N  N   . TRP B 1 79  ? -8.409  5.615  -21.139 1.00 14.58 ? 79  TRP B N   1 
ATOM   1384 C  CA  . TRP B 1 79  ? -7.523  4.928  -20.253 1.00 15.94 ? 79  TRP B CA  1 
ATOM   1385 C  C   . TRP B 1 79  ? -7.865  3.448  -20.162 1.00 17.29 ? 79  TRP B C   1 
ATOM   1386 O  O   . TRP B 1 79  ? -6.965  2.591  -20.248 1.00 19.26 ? 79  TRP B O   1 
ATOM   1387 C  CB  . TRP B 1 79  ? -7.395  5.578  -18.865 1.00 15.23 ? 79  TRP B CB  1 
ATOM   1388 C  CG  . TRP B 1 79  ? -6.774  6.971  -18.880 1.00 13.70 ? 79  TRP B CG  1 
ATOM   1389 C  CD1 . TRP B 1 79  ? -7.375  8.153  -18.542 1.00 13.77 ? 79  TRP B CD1 1 
ATOM   1390 C  CD2 . TRP B 1 79  ? -5.439  7.302  -19.258 1.00 13.60 ? 79  TRP B CD2 1 
ATOM   1391 N  NE1 . TRP B 1 79  ? -6.502  9.164  -18.697 1.00 12.60 ? 79  TRP B NE1 1 
ATOM   1392 C  CE2 . TRP B 1 79  ? -5.306  8.695  -19.121 1.00 12.66 ? 79  TRP B CE2 1 
ATOM   1393 C  CE3 . TRP B 1 79  ? -4.344  6.570  -19.690 1.00 15.99 ? 79  TRP B CE3 1 
ATOM   1394 C  CZ2 . TRP B 1 79  ? -4.124  9.363  -19.404 1.00 13.10 ? 79  TRP B CZ2 1 
ATOM   1395 C  CZ3 . TRP B 1 79  ? -3.168  7.242  -19.969 1.00 16.79 ? 79  TRP B CZ3 1 
ATOM   1396 C  CH2 . TRP B 1 79  ? -3.085  8.658  -19.849 1.00 16.35 ? 79  TRP B CH2 1 
ATOM   1397 N  N   . LYS B 1 80  ? -9.150  3.123  -20.119 1.00 18.32 ? 80  LYS B N   1 
ATOM   1398 C  CA  . LYS B 1 80  ? -9.541  1.736  -20.020 1.00 20.46 ? 80  LYS B CA  1 
ATOM   1399 C  C   . LYS B 1 80  ? -9.064  0.929  -21.261 1.00 21.55 ? 80  LYS B C   1 
ATOM   1400 O  O   . LYS B 1 80  ? -8.639  -0.234 -21.160 1.00 23.70 ? 80  LYS B O   1 
ATOM   1401 C  CB  . LYS B 1 80  ? -11.050 1.649  -19.780 1.00 29.85 ? 80  LYS B CB  1 
ATOM   1402 N  N   . ALA B 1 81  ? -9.086  1.534  -22.431 1.00 20.73 ? 81  ALA B N   1 
ATOM   1403 C  CA  . ALA B 1 81  ? -8.676  0.851  -23.644 1.00 23.21 ? 81  ALA B CA  1 
ATOM   1404 C  C   . ALA B 1 81  ? -7.173  0.576  -23.675 1.00 26.78 ? 81  ALA B C   1 
ATOM   1405 O  O   . ALA B 1 81  ? -6.715  -0.343 -24.400 1.00 25.35 ? 81  ALA B O   1 
ATOM   1406 C  CB  . ALA B 1 81  ? -9.075  1.636  -24.871 1.00 23.70 ? 81  ALA B CB  1 
ATOM   1407 N  N   . LEU B 1 82  ? -6.423  1.350  -22.853 1.00 22.11 ? 82  LEU B N   1 
ATOM   1408 C  CA  . LEU B 1 82  ? -5.000  1.175  -22.687 1.00 22.63 ? 82  LEU B CA  1 
ATOM   1409 C  C   . LEU B 1 82  ? -4.633  0.222  -21.534 1.00 23.21 ? 82  LEU B C   1 
ATOM   1410 O  O   . LEU B 1 82  ? -3.429  -0.051 -21.272 1.00 29.08 ? 82  LEU B O   1 
ATOM   1411 C  CB  . LEU B 1 82  ? -4.317  2.530  -22.476 1.00 24.20 ? 82  LEU B CB  1 
ATOM   1412 C  CG  . LEU B 1 82  ? -4.329  3.363  -23.751 1.00 30.11 ? 82  LEU B CG  1 
ATOM   1413 C  CD1 . LEU B 1 82  ? -3.720  4.701  -23.430 1.00 36.76 ? 82  LEU B CD1 1 
ATOM   1414 C  CD2 . LEU B 1 82  ? -3.627  2.645  -24.904 1.00 38.57 ? 82  LEU B CD2 1 
ATOM   1415 N  N   . GLY B 1 83  ? -5.633  -0.289 -20.824 1.00 22.25 ? 83  GLY B N   1 
ATOM   1416 C  CA  . GLY B 1 83  ? -5.392  -1.072 -19.635 1.00 26.32 ? 83  GLY B CA  1 
ATOM   1417 C  C   . GLY B 1 83  ? -4.876  -0.307 -18.429 1.00 23.11 ? 83  GLY B C   1 
ATOM   1418 O  O   . GLY B 1 83  ? -4.217  -0.883 -17.552 1.00 27.03 ? 83  GLY B O   1 
ATOM   1419 N  N   . ILE B 1 84  ? -5.149  1.001  -18.360 1.00 24.76 ? 84  ILE B N   1 
ATOM   1420 C  CA  . ILE B 1 84  ? -4.628  1.837  -17.303 1.00 20.43 ? 84  ILE B CA  1 
ATOM   1421 C  C   . ILE B 1 84  ? -5.753  2.312  -16.443 1.00 24.62 ? 84  ILE B C   1 
ATOM   1422 O  O   . ILE B 1 84  ? -6.768  2.751  -16.990 1.00 21.76 ? 84  ILE B O   1 
ATOM   1423 C  CB  . ILE B 1 84  ? -3.830  3.049  -17.852 1.00 19.46 ? 84  ILE B CB  1 
ATOM   1424 C  CG1 . ILE B 1 84  ? -2.546  2.560  -18.563 1.00 22.90 ? 84  ILE B CG1 1 
ATOM   1425 C  CG2 . ILE B 1 84  ? -3.572  4.036  -16.705 1.00 24.47 ? 84  ILE B CG2 1 
ATOM   1426 C  CD1 . ILE B 1 84  ? -1.892  3.573  -19.497 1.00 28.26 ? 84  ILE B CD1 1 
ATOM   1427 N  N   . SER B 1 85  ? -5.585  2.315  -15.127 1.00 24.79 ? 85  SER B N   1 
ATOM   1428 C  CA  . SER B 1 85  ? -6.677  2.705  -14.199 1.00 20.74 ? 85  SER B CA  1 
ATOM   1429 C  C   . SER B 1 85  ? -6.805  4.257  -14.012 1.00 19.40 ? 85  SER B C   1 
ATOM   1430 O  O   . SER B 1 85  ? -5.877  4.901  -13.551 1.00 21.19 ? 85  SER B O   1 
ATOM   1431 C  CB  . SER B 1 85  ? -6.429  2.112  -12.855 1.00 25.13 ? 85  SER B CB  1 
ATOM   1432 O  OG  . SER B 1 85  ? -7.450  2.443  -11.915 1.00 27.05 ? 85  SER B OG  1 
ATOM   1433 N  N   . PRO B 1 86  ? -7.958  4.855  -14.371 1.00 19.31 ? 86  PRO B N   1 
ATOM   1434 C  CA  . PRO B 1 86  ? -8.169  6.296  -14.262 1.00 19.94 ? 86  PRO B CA  1 
ATOM   1435 C  C   . PRO B 1 86  ? -9.014  6.814  -13.119 1.00 20.82 ? 86  PRO B C   1 
ATOM   1436 O  O   . PRO B 1 86  ? -9.846  6.087  -12.569 1.00 22.75 ? 86  PRO B O   1 
ATOM   1437 C  CB  . PRO B 1 86  ? -8.894  6.586  -15.591 1.00 24.44 ? 86  PRO B CB  1 
ATOM   1438 C  CG  . PRO B 1 86  ? -9.871  5.408  -15.704 1.00 24.37 ? 86  PRO B CG  1 
ATOM   1439 C  CD  . PRO B 1 86  ? -9.082  4.235  -15.137 1.00 19.53 ? 86  PRO B CD  1 
ATOM   1440 N  N   . PHE B 1 87  ? -8.784  8.087  -12.742 1.00 14.60 ? 87  PHE B N   1 
ATOM   1441 C  CA  . PHE B 1 87  ? -9.520  8.788  -11.717 1.00 16.40 ? 87  PHE B CA  1 
ATOM   1442 C  C   . PHE B 1 87  ? -10.821 9.444  -12.199 1.00 15.39 ? 87  PHE B C   1 
ATOM   1443 O  O   . PHE B 1 87  ? -11.863 9.291  -11.580 1.00 14.89 ? 87  PHE B O   1 
ATOM   1444 C  CB  . PHE B 1 87  ? -8.644  9.823  -11.078 1.00 16.80 ? 87  PHE B CB  1 
ATOM   1445 C  CG  . PHE B 1 87  ? -9.332  10.599 -9.990  1.00 16.69 ? 87  PHE B CG  1 
ATOM   1446 C  CD1 . PHE B 1 87  ? -9.585  10.025 -8.770  1.00 20.69 ? 87  PHE B CD1 1 
ATOM   1447 C  CD2 . PHE B 1 87  ? -9.698  11.879 -10.199 1.00 16.68 ? 87  PHE B CD2 1 
ATOM   1448 C  CE1 . PHE B 1 87  ? -10.265 10.727 -7.809  1.00 20.17 ? 87  PHE B CE1 1 
ATOM   1449 C  CE2 . PHE B 1 87  ? -10.361 12.605 -9.254  1.00 19.69 ? 87  PHE B CE2 1 
ATOM   1450 C  CZ  . PHE B 1 87  ? -10.616 12.018 -8.026  1.00 19.07 ? 87  PHE B CZ  1 
ATOM   1451 N  N   . HIS B 1 88  ? -10.745 10.274 -13.222 1.00 15.07 ? 88  HIS B N   1 
ATOM   1452 C  CA  . HIS B 1 88  ? -11.876 11.086 -13.643 1.00 13.95 ? 88  HIS B CA  1 
ATOM   1453 C  C   . HIS B 1 88  ? -12.867 10.347 -14.465 1.00 13.05 ? 88  HIS B C   1 
ATOM   1454 O  O   . HIS B 1 88  ? -12.516 9.415  -15.183 1.00 14.77 ? 88  HIS B O   1 
ATOM   1455 C  CB  . HIS B 1 88  ? -11.410 12.316 -14.456 1.00 14.79 ? 88  HIS B CB  1 
ATOM   1456 C  CG  . HIS B 1 88  ? -10.438 13.182 -13.728 1.00 14.85 ? 88  HIS B CG  1 
ATOM   1457 N  ND1 . HIS B 1 88  ? -9.078  12.992 -13.779 1.00 15.10 ? 88  HIS B ND1 1 
ATOM   1458 C  CD2 . HIS B 1 88  ? -10.641 14.139 -12.807 1.00 18.63 ? 88  HIS B CD2 1 
ATOM   1459 C  CE1 . HIS B 1 88  ? -8.489  13.894 -13.028 1.00 16.30 ? 88  HIS B CE1 1 
ATOM   1460 N  NE2 . HIS B 1 88  ? -9.418  14.590 -12.403 1.00 20.99 ? 88  HIS B NE2 1 
ATOM   1461 N  N   . GLU B 1 89  ? -14.147 10.709 -14.382 1.00 13.56 ? 89  GLU B N   1 
ATOM   1462 C  CA  . GLU B 1 89  ? -15.140 10.197 -15.312 1.00 13.25 ? 89  GLU B CA  1 
ATOM   1463 C  C   . GLU B 1 89  ? -14.903 10.701 -16.750 1.00 15.66 ? 89  GLU B C   1 
ATOM   1464 O  O   . GLU B 1 89  ? -15.134 9.989  -17.755 1.00 19.90 ? 89  GLU B O   1 
ATOM   1465 C  CB  . GLU B 1 89  ? -16.572 10.559 -14.866 1.00 15.03 ? 89  GLU B CB  1 
ATOM   1466 C  CG  . GLU B 1 89  ? -17.035 9.778  -13.641 1.00 16.54 ? 89  GLU B CG  1 
ATOM   1467 C  CD  . GLU B 1 89  ? -17.165 8.310  -13.896 1.00 19.04 ? 89  GLU B CD  1 
ATOM   1468 O  OE1 . GLU B 1 89  ? -17.983 7.910  -14.779 1.00 23.73 ? 89  GLU B OE1 1 
ATOM   1469 O  OE2 . GLU B 1 89  ? -16.441 7.572  -13.246 1.00 22.85 ? 89  GLU B OE2 1 
ATOM   1470 N  N   . HIS B 1 90  ? -14.463 11.917 -16.864 1.00 14.81 ? 90  HIS B N   1 
ATOM   1471 C  CA  . HIS B 1 90  ? -14.238 12.596 -18.159 1.00 15.09 ? 90  HIS B CA  1 
ATOM   1472 C  C   . HIS B 1 90  ? -13.570 13.894 -17.843 1.00 15.20 ? 90  HIS B C   1 
ATOM   1473 O  O   . HIS B 1 90  ? -13.298 14.193 -16.679 1.00 20.56 ? 90  HIS B O   1 
ATOM   1474 C  CB  . HIS B 1 90  ? -15.548 12.850 -18.932 1.00 19.87 ? 90  HIS B CB  1 
ATOM   1475 C  CG  . HIS B 1 90  ? -16.701 13.322 -18.115 1.00 24.79 ? 90  HIS B CG  1 
ATOM   1476 N  ND1 . HIS B 1 90  ? -16.762 14.589 -17.614 1.00 34.50 ? 90  HIS B ND1 1 
ATOM   1477 C  CD2 . HIS B 1 90  ? -17.839 12.696 -17.727 1.00 27.62 ? 90  HIS B CD2 1 
ATOM   1478 C  CE1 . HIS B 1 90  ? -17.886 14.748 -16.951 1.00 29.41 ? 90  HIS B CE1 1 
ATOM   1479 N  NE2 . HIS B 1 90  ? -18.560 13.610 -17.001 1.00 40.52 ? 90  HIS B NE2 1 
ATOM   1480 N  N   . ALA B 1 91  ? -13.214 14.632 -18.887 1.00 17.57 ? 91  ALA B N   1 
ATOM   1481 C  CA  . ALA B 1 91  ? -12.770 15.994 -18.686 1.00 19.61 ? 91  ALA B CA  1 
ATOM   1482 C  C   . ALA B 1 91  ? -13.713 16.901 -19.450 1.00 22.07 ? 91  ALA B C   1 
ATOM   1483 O  O   . ALA B 1 91  ? -13.896 16.698 -20.631 1.00 22.80 ? 91  ALA B O   1 
ATOM   1484 C  CB  . ALA B 1 91  ? -11.358 16.180 -19.209 1.00 22.41 ? 91  ALA B CB  1 
ATOM   1485 N  N   . GLU B 1 92  ? -14.322 17.879 -18.750 1.00 23.10 ? 92  GLU B N   1 
ATOM   1486 C  CA  . GLU B 1 92  ? -15.312 18.851 -19.298 1.00 19.88 ? 92  GLU B CA  1 
ATOM   1487 C  C   . GLU B 1 92  ? -14.666 20.219 -19.334 1.00 23.81 ? 92  GLU B C   1 
ATOM   1488 O  O   . GLU B 1 92  ? -14.206 20.715 -18.292 1.00 35.49 ? 92  GLU B O   1 
ATOM   1489 C  CB  . GLU B 1 92  ? -16.540 19.004 -18.396 1.00 28.91 ? 92  GLU B CB  1 
ATOM   1490 C  CG  . GLU B 1 92  ? -17.335 17.757 -18.089 0.50 27.51 ? 92  GLU B CG  1 
ATOM   1491 C  CD  . GLU B 1 92  ? -18.227 17.904 -16.863 0.50 28.13 ? 92  GLU B CD  1 
ATOM   1492 O  OE1 . GLU B 1 92  ? -17.758 18.311 -15.737 0.50 25.78 ? 92  GLU B OE1 1 
ATOM   1493 O  OE2 . GLU B 1 92  ? -19.399 17.530 -17.005 0.50 36.20 ? 92  GLU B OE2 1 
ATOM   1494 N  N   . VAL B 1 93  ? -14.675 20.865 -20.509 1.00 17.33 ? 93  VAL B N   1 
ATOM   1495 C  CA  . VAL B 1 93  ? -14.100 22.173 -20.638 1.00 16.51 ? 93  VAL B CA  1 
ATOM   1496 C  C   . VAL B 1 93  ? -15.232 23.115 -21.062 1.00 12.92 ? 93  VAL B C   1 
ATOM   1497 O  O   . VAL B 1 93  ? -15.812 22.923 -22.077 1.00 15.50 ? 93  VAL B O   1 
ATOM   1498 C  CB  . VAL B 1 93  ? -13.004 22.129 -21.686 1.00 17.00 ? 93  VAL B CB  1 
ATOM   1499 C  CG1 . VAL B 1 93  ? -12.429 23.487 -21.907 1.00 18.05 ? 93  VAL B CG1 1 
ATOM   1500 C  CG2 . VAL B 1 93  ? -11.927 21.125 -21.321 1.00 20.50 ? 93  VAL B CG2 1 
ATOM   1501 N  N   . VAL B 1 94  ? -15.549 24.116 -20.251 1.00 14.31 ? 94  VAL B N   1 
ATOM   1502 C  CA  . VAL B 1 94  ? -16.701 25.010 -20.444 1.00 14.12 ? 94  VAL B CA  1 
ATOM   1503 C  C   . VAL B 1 94  ? -16.209 26.440 -20.617 1.00 15.23 ? 94  VAL B C   1 
ATOM   1504 O  O   . VAL B 1 94  ? -15.462 26.983 -19.785 1.00 14.98 ? 94  VAL B O   1 
ATOM   1505 C  CB  . VAL B 1 94  ? -17.689 24.896 -19.244 1.00 16.29 ? 94  VAL B CB  1 
ATOM   1506 C  CG1 . VAL B 1 94  ? -18.901 25.751 -19.523 1.00 18.94 ? 94  VAL B CG1 1 
ATOM   1507 C  CG2 . VAL B 1 94  ? -18.173 23.422 -19.123 1.00 20.37 ? 94  VAL B CG2 1 
ATOM   1508 N  N   . PHE B 1 95  ? -16.703 27.066 -21.680 1.00 16.83 ? 95  PHE B N   1 
ATOM   1509 C  CA  . PHE B 1 95  ? -16.213 28.391 -22.060 1.00 14.86 ? 95  PHE B CA  1 
ATOM   1510 C  C   . PHE B 1 95  ? -17.222 29.208 -22.818 1.00 14.56 ? 95  PHE B C   1 
ATOM   1511 O  O   . PHE B 1 95  ? -18.110 28.657 -23.454 1.00 16.96 ? 95  PHE B O   1 
ATOM   1512 C  CB  . PHE B 1 95  ? -14.911 28.270 -22.871 1.00 17.80 ? 95  PHE B CB  1 
ATOM   1513 C  CG  . PHE B 1 95  ? -15.096 27.638 -24.217 1.00 17.90 ? 95  PHE B CG  1 
ATOM   1514 C  CD1 . PHE B 1 95  ? -15.068 26.273 -24.344 1.00 19.96 ? 95  PHE B CD1 1 
ATOM   1515 C  CD2 . PHE B 1 95  ? -15.230 28.431 -25.358 1.00 19.95 ? 95  PHE B CD2 1 
ATOM   1516 C  CE1 . PHE B 1 95  ? -15.201 25.711 -25.611 1.00 21.71 ? 95  PHE B CE1 1 
ATOM   1517 C  CE2 . PHE B 1 95  ? -15.358 27.888 -26.606 1.00 22.35 ? 95  PHE B CE2 1 
ATOM   1518 C  CZ  . PHE B 1 95  ? -15.340 26.525 -26.727 1.00 22.14 ? 95  PHE B CZ  1 
ATOM   1519 N  N   . THR B 1 96  ? -17.118 30.531 -22.754 1.00 19.92 ? 96  THR B N   1 
ATOM   1520 C  CA  . THR B 1 96  ? -17.927 31.388 -23.618 1.00 19.98 ? 96  THR B CA  1 
ATOM   1521 C  C   . THR B 1 96  ? -17.209 31.730 -24.894 1.00 22.07 ? 96  THR B C   1 
ATOM   1522 O  O   . THR B 1 96  ? -16.072 32.111 -24.875 1.00 23.41 ? 96  THR B O   1 
ATOM   1523 C  CB  . THR B 1 96  ? -18.316 32.706 -22.853 1.00 21.58 ? 96  THR B CB  1 
ATOM   1524 O  OG1 . THR B 1 96  ? -19.097 32.396 -21.719 1.00 23.44 ? 96  THR B OG1 1 
ATOM   1525 C  CG2 . THR B 1 96  ? -19.184 33.666 -23.682 1.00 24.56 ? 96  THR B CG2 1 
ATOM   1526 N  N   . ALA B 1 97  ? -17.876 31.577 -26.037 1.00 20.96 ? 97  ALA B N   1 
ATOM   1527 C  CA  . ALA B 1 97  ? -17.340 32.085 -27.313 1.00 20.74 ? 97  ALA B CA  1 
ATOM   1528 C  C   . ALA B 1 97  ? -17.820 33.530 -27.552 1.00 30.04 ? 97  ALA B C   1 
ATOM   1529 O  O   . ALA B 1 97  ? -18.971 33.823 -27.442 1.00 25.63 ? 97  ALA B O   1 
ATOM   1530 C  CB  . ALA B 1 97  ? -17.745 31.157 -28.425 1.00 29.81 ? 97  ALA B CB  1 
ATOM   1531 N  N   . ASN B 1 98  ? -16.890 34.439 -27.769 1.00 28.71 ? 98  ASN B N   1 
ATOM   1532 C  CA  . ASN B 1 98  ? -17.234 35.866 -27.917 1.00 29.84 ? 98  ASN B CA  1 
ATOM   1533 C  C   . ASN B 1 98  ? -16.692 36.317 -29.246 1.00 32.12 ? 98  ASN B C   1 
ATOM   1534 O  O   . ASN B 1 98  ? -15.537 36.045 -29.554 1.00 31.27 ? 98  ASN B O   1 
ATOM   1535 C  CB  . ASN B 1 98  ? -16.625 36.637 -26.751 1.00 32.58 ? 98  ASN B CB  1 
ATOM   1536 C  CG  . ASN B 1 98  ? -17.002 38.097 -26.737 1.00 34.43 ? 98  ASN B CG  1 
ATOM   1537 O  OD1 . ASN B 1 98  ? -17.687 38.572 -27.609 1.00 52.40 ? 98  ASN B OD1 1 
ATOM   1538 N  ND2 . ASN B 1 98  ? -16.584 38.795 -25.696 1.00 53.88 ? 98  ASN B ND2 1 
ATOM   1539 N  N   . ASP B 1 99  ? -17.506 36.969 -30.052 1.00 32.10 ? 99  ASP B N   1 
ATOM   1540 C  CA  . ASP B 1 99  ? -17.063 37.420 -31.414 1.00 30.89 ? 99  ASP B CA  1 
ATOM   1541 C  C   . ASP B 1 99  ? -16.046 38.602 -31.465 1.00 48.32 ? 99  ASP B C   1 
ATOM   1542 O  O   . ASP B 1 99  ? -15.844 39.306 -30.474 1.00 45.33 ? 99  ASP B O   1 
ATOM   1543 C  CB  . ASP B 1 99  ? -18.326 37.739 -32.245 1.00 28.38 ? 99  ASP B CB  1 
ATOM   1544 C  CG  . ASP B 1 99  ? -18.936 36.518 -32.857 1.00 33.09 ? 99  ASP B CG  1 
ATOM   1545 O  OD1 . ASP B 1 99  ? -18.361 35.423 -32.774 1.00 44.15 ? 99  ASP B OD1 1 
ATOM   1546 O  OD2 . ASP B 1 99  ? -20.027 36.641 -33.475 1.00 30.96 ? 99  ASP B OD2 1 
ATOM   1547 N  N   . ARG B 1 104 ? -10.467 31.797 -34.098 1.00 27.07 ? 104 ARG B N   1 
ATOM   1548 C  CA  . ARG B 1 104 ? -10.404 30.360 -34.151 1.00 24.40 ? 104 ARG B CA  1 
ATOM   1549 C  C   . ARG B 1 104 ? -9.985  29.851 -32.778 1.00 26.29 ? 104 ARG B C   1 
ATOM   1550 O  O   . ARG B 1 104 ? -9.051  30.351 -32.216 1.00 23.57 ? 104 ARG B O   1 
ATOM   1551 C  CB  . ARG B 1 104 ? -9.336  29.946 -35.146 1.00 27.93 ? 104 ARG B CB  1 
ATOM   1552 N  N   . TYR B 1 105 ? -10.604 28.768 -32.338 1.00 24.57 ? 105 TYR B N   1 
ATOM   1553 C  CA  . TYR B 1 105 ? -10.411 28.248 -30.994 1.00 20.86 ? 105 TYR B CA  1 
ATOM   1554 C  C   . TYR B 1 105 ? -9.822  26.884 -31.087 1.00 16.50 ? 105 TYR B C   1 
ATOM   1555 O  O   . TYR B 1 105 ? -10.417 26.005 -31.719 1.00 20.87 ? 105 TYR B O   1 
ATOM   1556 C  CB  . TYR B 1 105 ? -11.742 28.093 -30.261 1.00 23.10 ? 105 TYR B CB  1 
ATOM   1557 C  CG  . TYR B 1 105 ? -12.449 29.370 -29.939 1.00 24.93 ? 105 TYR B CG  1 
ATOM   1558 C  CD1 . TYR B 1 105 ? -13.181 30.052 -30.919 1.00 32.26 ? 105 TYR B CD1 1 
ATOM   1559 C  CD2 . TYR B 1 105 ? -12.346 29.955 -28.695 1.00 30.84 ? 105 TYR B CD2 1 
ATOM   1560 C  CE1 . TYR B 1 105 ? -13.857 31.204 -30.629 1.00 28.90 ? 105 TYR B CE1 1 
ATOM   1561 C  CE2 . TYR B 1 105 ? -13.009 31.148 -28.405 1.00 29.39 ? 105 TYR B CE2 1 
ATOM   1562 C  CZ  . TYR B 1 105 ? -13.752 31.758 -29.354 1.00 27.14 ? 105 TYR B CZ  1 
ATOM   1563 O  OH  . TYR B 1 105 ? -14.396 32.912 -29.041 1.00 32.91 ? 105 TYR B OH  1 
ATOM   1564 N  N   . THR B 1 106 ? -8.709  26.646 -30.400 1.00 16.35 ? 106 THR B N   1 
ATOM   1565 C  CA  . THR B 1 106 ? -8.191  25.311 -30.234 1.00 15.13 ? 106 THR B CA  1 
ATOM   1566 C  C   . THR B 1 106 ? -8.258  24.990 -28.757 1.00 15.94 ? 106 THR B C   1 
ATOM   1567 O  O   . THR B 1 106 ? -7.692  25.729 -27.927 1.00 17.29 ? 106 THR B O   1 
ATOM   1568 C  CB  . THR B 1 106 ? -6.750  25.147 -30.736 1.00 21.97 ? 106 THR B CB  1 
ATOM   1569 O  OG1 . THR B 1 106 ? -6.722  25.343 -32.153 1.00 23.25 ? 106 THR B OG1 1 
ATOM   1570 C  CG2 . THR B 1 106 ? -6.211  23.808 -30.408 1.00 20.95 ? 106 THR B CG2 1 
ATOM   1571 N  N   . ILE B 1 107 ? -8.937  23.907 -28.396 1.00 14.58 ? 107 ILE B N   1 
ATOM   1572 C  CA  . ILE B 1 107 ? -8.986  23.407 -27.064 1.00 14.95 ? 107 ILE B CA  1 
ATOM   1573 C  C   . ILE B 1 107 ? -8.025  22.250 -26.960 1.00 15.23 ? 107 ILE B C   1 
ATOM   1574 O  O   . ILE B 1 107 ? -8.223  21.213 -27.603 1.00 17.37 ? 107 ILE B O   1 
ATOM   1575 C  CB  . ILE B 1 107 ? -10.426 22.962 -26.689 1.00 18.28 ? 107 ILE B CB  1 
ATOM   1576 C  CG1 . ILE B 1 107 ? -11.411 24.133 -26.857 1.00 20.27 ? 107 ILE B CG1 1 
ATOM   1577 C  CG2 . ILE B 1 107 ? -10.425 22.367 -25.308 1.00 18.19 ? 107 ILE B CG2 1 
ATOM   1578 C  CD1 . ILE B 1 107 ? -11.174 25.391 -26.005 1.00 20.84 ? 107 ILE B CD1 1 
ATOM   1579 N  N   . ALA B 1 108 ? -6.993  22.411 -26.164 1.00 15.09 ? 108 ALA B N   1 
ATOM   1580 C  CA  . ALA B 1 108 ? -6.005  21.378 -26.045 1.00 16.91 ? 108 ALA B CA  1 
ATOM   1581 C  C   . ALA B 1 108 ? -6.043  20.776 -24.653 1.00 18.82 ? 108 ALA B C   1 
ATOM   1582 O  O   . ALA B 1 108 ? -6.219  21.472 -23.680 1.00 17.85 ? 108 ALA B O   1 
ATOM   1583 C  CB  . ALA B 1 108 ? -4.620  21.920 -26.325 1.00 18.62 ? 108 ALA B CB  1 
ATOM   1584 N  N   . ALA B 1 109 ? -5.838  19.488 -24.554 1.00 13.27 ? 109 ALA B N   1 
ATOM   1585 C  CA  . ALA B 1 109 ? -5.844  18.782 -23.265 1.00 13.29 ? 109 ALA B CA  1 
ATOM   1586 C  C   . ALA B 1 109 ? -4.674  17.799 -23.190 1.00 14.50 ? 109 ALA B C   1 
ATOM   1587 O  O   . ALA B 1 109 ? -4.326  17.129 -24.155 1.00 16.17 ? 109 ALA B O   1 
ATOM   1588 C  CB  . ALA B 1 109 ? -7.151  18.048 -23.094 1.00 15.59 ? 109 ALA B CB  1 
ATOM   1589 N  N   . LEU B 1 110 ? -4.060  17.746 -22.014 1.00 12.44 ? 110 LEU B N   1 
ATOM   1590 C  CA  . LEU B 1 110 ? -2.943  16.856 -21.724 1.00 12.59 ? 110 LEU B CA  1 
ATOM   1591 C  C   . LEU B 1 110 ? -3.405  15.938 -20.604 1.00 12.18 ? 110 LEU B C   1 
ATOM   1592 O  O   . LEU B 1 110 ? -3.782  16.401 -19.529 1.00 12.91 ? 110 LEU B O   1 
ATOM   1593 C  CB  . LEU B 1 110 ? -1.745  17.648 -21.241 1.00 13.63 ? 110 LEU B CB  1 
ATOM   1594 C  CG  . LEU B 1 110 ? -0.525  16.822 -20.860 1.00 14.73 ? 110 LEU B CG  1 
ATOM   1595 C  CD1 . LEU B 1 110 ? 0.022   16.069 -22.041 1.00 14.50 ? 110 LEU B CD1 1 
ATOM   1596 C  CD2 . LEU B 1 110 ? 0.532   17.782 -20.244 1.00 18.32 ? 110 LEU B CD2 1 
ATOM   1597 N  N   . LEU B 1 111 ? -3.422  14.658 -20.880 1.00 11.48 ? 111 LEU B N   1 
ATOM   1598 C  CA  . LEU B 1 111 ? -4.008  13.678 -19.980 1.00 11.73 ? 111 LEU B CA  1 
ATOM   1599 C  C   . LEU B 1 111 ? -3.023  12.790 -19.241 1.00 12.42 ? 111 LEU B C   1 
ATOM   1600 O  O   . LEU B 1 111 ? -2.103  12.228 -19.849 1.00 11.35 ? 111 LEU B O   1 
ATOM   1601 C  CB  . LEU B 1 111 ? -4.911  12.720 -20.755 1.00 11.30 ? 111 LEU B CB  1 
ATOM   1602 C  CG  . LEU B 1 111 ? -5.963  13.312 -21.708 1.00 11.07 ? 111 LEU B CG  1 
ATOM   1603 C  CD1 . LEU B 1 111 ? -6.762  12.169 -22.310 1.00 13.45 ? 111 LEU B CD1 1 
ATOM   1604 C  CD2 . LEU B 1 111 ? -6.852  14.317 -20.991 1.00 12.08 ? 111 LEU B CD2 1 
ATOM   1605 N  N   . SER B 1 112 ? -3.242  12.657 -17.947 1.00 11.98 ? 112 SER B N   1 
ATOM   1606 C  CA  . SER B 1 112 ? -2.641  11.633 -17.096 1.00 11.50 ? 112 SER B CA  1 
ATOM   1607 C  C   . SER B 1 112 ? -3.767  10.949 -16.338 1.00 11.65 ? 112 SER B C   1 
ATOM   1608 O  O   . SER B 1 112 ? -4.874  11.405 -16.246 1.00 12.72 ? 112 SER B O   1 
ATOM   1609 C  CB  . SER B 1 112 ? -1.646  12.232 -16.080 1.00 12.63 ? 112 SER B CB  1 
ATOM   1610 O  OG  . SER B 1 112 ? -0.564  12.898 -16.748 1.00 14.31 ? 112 SER B OG  1 
ATOM   1611 N  N   . PRO B 1 113 ? -3.446  9.784  -15.737 1.00 11.65 ? 113 PRO B N   1 
ATOM   1612 C  CA  . PRO B 1 113 ? -4.539  9.048  -15.109 1.00 11.74 ? 113 PRO B CA  1 
ATOM   1613 C  C   . PRO B 1 113 ? -5.238  9.746  -13.962 1.00 12.07 ? 113 PRO B C   1 
ATOM   1614 O  O   . PRO B 1 113 ? -6.449  9.589  -13.821 1.00 12.96 ? 113 PRO B O   1 
ATOM   1615 C  CB  . PRO B 1 113 ? -3.883  7.732  -14.681 1.00 13.18 ? 113 PRO B CB  1 
ATOM   1616 C  CG  . PRO B 1 113 ? -2.843  7.522  -15.707 1.00 12.58 ? 113 PRO B CG  1 
ATOM   1617 C  CD  . PRO B 1 113 ? -2.299  8.908  -15.959 1.00 12.49 ? 113 PRO B CD  1 
ATOM   1618 N  N   . TYR B 1 114 ? -4.495  10.489 -13.164 1.00 11.36 ? 114 TYR B N   1 
ATOM   1619 C  CA  . TYR B 1 114 ? -5.030  11.229 -12.030 1.00 10.73 ? 114 TYR B CA  1 
ATOM   1620 C  C   . TYR B 1 114 ? -4.900  12.725 -12.188 1.00 12.74 ? 114 TYR B C   1 
ATOM   1621 O  O   . TYR B 1 114 ? -5.078  13.397 -11.199 1.00 13.40 ? 114 TYR B O   1 
ATOM   1622 C  CB  . TYR B 1 114 ? -4.385  10.772 -10.700 1.00 12.58 ? 114 TYR B CB  1 
ATOM   1623 C  CG  . TYR B 1 114 ? -4.985  9.469  -10.185 1.00 12.05 ? 114 TYR B CG  1 
ATOM   1624 C  CD1 . TYR B 1 114 ? -4.821  8.297  -10.853 1.00 18.67 ? 114 TYR B CD1 1 
ATOM   1625 C  CD2 . TYR B 1 114 ? -5.747  9.464  -9.041  1.00 11.98 ? 114 TYR B CD2 1 
ATOM   1626 C  CE1 . TYR B 1 114 ? -5.384  7.124  -10.361 1.00 20.18 ? 114 TYR B CE1 1 
ATOM   1627 C  CE2 . TYR B 1 114 ? -6.345  8.278  -8.550  1.00 15.07 ? 114 TYR B CE2 1 
ATOM   1628 C  CZ  . TYR B 1 114 ? -6.108  7.084  -9.241  1.00 19.55 ? 114 TYR B CZ  1 
ATOM   1629 O  OH  . TYR B 1 114 ? -6.625  5.879  -8.783  1.00 30.51 ? 114 TYR B OH  1 
ATOM   1630 N  N   . SER B 1 115 ? -4.703  13.208 -13.381 1.00 12.31 ? 115 SER B N   1 
ATOM   1631 C  CA  . SER B 1 115 ? -4.560  14.666 -13.590 1.00 11.89 ? 115 SER B CA  1 
ATOM   1632 C  C   . SER B 1 115 ? -4.826  14.977 -15.040 1.00 11.64 ? 115 SER B C   1 
ATOM   1633 O  O   . SER B 1 115 ? -4.499  14.234 -15.920 1.00 13.44 ? 115 SER B O   1 
ATOM   1634 C  CB  . SER B 1 115 ? -3.097  15.101 -13.280 1.00 13.77 ? 115 SER B CB  1 
ATOM   1635 O  OG  . SER B 1 115 ? -2.913  16.489 -13.421 1.00 17.62 ? 115 SER B OG  1 
ATOM   1636 N  N   . TYR B 1 116 ? -5.348  16.162 -15.318 1.00 12.13 ? 116 TYR B N   1 
ATOM   1637 C  CA  . TYR B 1 116 ? -5.385  16.699 -16.680 1.00 11.29 ? 116 TYR B CA  1 
ATOM   1638 C  C   . TYR B 1 116 ? -5.214  18.168 -16.629 1.00 11.91 ? 116 TYR B C   1 
ATOM   1639 O  O   . TYR B 1 116 ? -5.516  18.822 -15.679 1.00 11.69 ? 116 TYR B O   1 
ATOM   1640 C  CB  . TYR B 1 116 ? -6.590  16.305 -17.491 1.00 13.77 ? 116 TYR B CB  1 
ATOM   1641 C  CG  . TYR B 1 116 ? -7.880  16.863 -17.021 1.00 16.43 ? 116 TYR B CG  1 
ATOM   1642 C  CD1 . TYR B 1 116 ? -8.332  18.082 -17.432 1.00 17.37 ? 116 TYR B CD1 1 
ATOM   1643 C  CD2 . TYR B 1 116 ? -8.652  16.129 -16.115 1.00 20.75 ? 116 TYR B CD2 1 
ATOM   1644 C  CE1 . TYR B 1 116 ? -9.580  18.560 -16.947 1.00 23.32 ? 116 TYR B CE1 1 
ATOM   1645 C  CE2 . TYR B 1 116 ? -9.807  16.592 -15.656 1.00 21.68 ? 116 TYR B CE2 1 
ATOM   1646 C  CZ  . TYR B 1 116 ? -10.244 17.804 -16.015 1.00 16.30 ? 116 TYR B CZ  1 
ATOM   1647 O  OH  . TYR B 1 116 ? -11.461 18.224 -15.463 1.00 29.05 ? 116 TYR B OH  1 
ATOM   1648 N  N   . SER B 1 117 ? -4.709  18.667 -17.748 1.00 11.10 ? 117 SER B N   1 
ATOM   1649 C  CA  A SER B 1 117 ? -4.701  20.126 -17.996 0.50 11.57 ? 117 SER B CA  1 
ATOM   1650 C  CA  B SER B 1 117 ? -4.508  20.109 -18.060 0.25 11.54 ? 117 SER B CA  1 
ATOM   1651 C  CA  C SER B 1 117 ? -4.533  20.102 -18.049 0.25 11.44 ? 117 SER B CA  1 
ATOM   1652 C  C   . SER B 1 117 ? -5.277  20.479 -19.338 1.00 13.07 ? 117 SER B C   1 
ATOM   1653 O  O   . SER B 1 117 ? -5.362  19.676 -20.264 1.00 13.07 ? 117 SER B O   1 
ATOM   1654 C  CB  A SER B 1 117 ? -3.335  20.704 -17.871 0.50 17.58 ? 117 SER B CB  1 
ATOM   1655 C  CB  B SER B 1 117 ? -3.017  20.398 -18.283 0.25 16.78 ? 117 SER B CB  1 
ATOM   1656 C  CB  C SER B 1 117 ? -3.046  20.381 -18.211 0.25 16.19 ? 117 SER B CB  1 
ATOM   1657 O  OG  A SER B 1 117 ? -2.605  20.296 -18.982 0.50 19.59 ? 117 SER B OG  1 
ATOM   1658 O  OG  B SER B 1 117 ? -2.217  20.206 -17.113 0.25 17.69 ? 117 SER B OG  1 
ATOM   1659 O  OG  C SER B 1 117 ? -2.792  21.762 -18.394 0.25 17.01 ? 117 SER B OG  1 
ATOM   1660 N  N   . THR B 1 118 ? -5.876  21.669 -19.363 1.00 13.03 ? 118 THR B N   1 
ATOM   1661 C  CA  . THR B 1 118 ? -6.484  22.136 -20.597 1.00 14.78 ? 118 THR B CA  1 
ATOM   1662 C  C   . THR B 1 118 ? -6.087  23.581 -20.790 1.00 14.05 ? 118 THR B C   1 
ATOM   1663 O  O   . THR B 1 118 ? -6.025  24.361 -19.865 1.00 16.88 ? 118 THR B O   1 
ATOM   1664 C  CB  . THR B 1 118 ? -8.008  21.914 -20.595 1.00 16.02 ? 118 THR B CB  1 
ATOM   1665 O  OG1 . THR B 1 118 ? -8.482  22.206 -21.874 1.00 18.68 ? 118 THR B OG1 1 
ATOM   1666 C  CG2 . THR B 1 118 ? -8.746  22.714 -19.536 1.00 13.65 ? 118 THR B CG2 1 
ATOM   1667 N  N   . THR B 1 119 ? -5.825  23.915 -22.052 1.00 12.98 ? 119 THR B N   1 
ATOM   1668 C  CA  A THR B 1 119 ? -5.512  25.303 -22.456 0.50 13.18 ? 119 THR B CA  1 
ATOM   1669 C  CA  B THR B 1 119 ? -5.520  25.319 -22.428 0.50 13.11 ? 119 THR B CA  1 
ATOM   1670 C  C   . THR B 1 119 ? -6.268  25.711 -23.715 1.00 13.80 ? 119 THR B C   1 
ATOM   1671 O  O   . THR B 1 119 ? -6.665  24.840 -24.453 1.00 15.25 ? 119 THR B O   1 
ATOM   1672 C  CB  A THR B 1 119 ? -4.016  25.488 -22.700 0.50 15.70 ? 119 THR B CB  1 
ATOM   1673 C  CB  B THR B 1 119 ? -3.994  25.565 -22.544 0.50 18.65 ? 119 THR B CB  1 
ATOM   1674 O  OG1 A THR B 1 119 ? -3.335  24.802 -21.652 0.50 28.63 ? 119 THR B OG1 1 
ATOM   1675 O  OG1 B THR B 1 119 ? -3.493  25.143 -23.803 0.50 23.74 ? 119 THR B OG1 1 
ATOM   1676 C  CG2 A THR B 1 119 ? -3.722  27.010 -22.697 0.50 9.36  ? 119 THR B CG2 1 
ATOM   1677 C  CG2 B THR B 1 119 ? -3.327  24.775 -21.538 0.50 19.89 ? 119 THR B CG2 1 
ATOM   1678 N  N   . ALA B 1 120 ? -6.637  26.950 -23.857 1.00 14.59 ? 120 ALA B N   1 
ATOM   1679 C  CA  . ALA B 1 120 ? -7.267  27.434 -25.084 1.00 14.86 ? 120 ALA B CA  1 
ATOM   1680 C  C   . ALA B 1 120 ? -6.251  28.264 -25.847 1.00 15.61 ? 120 ALA B C   1 
ATOM   1681 O  O   . ALA B 1 120 ? -5.541  29.085 -25.272 1.00 17.19 ? 120 ALA B O   1 
ATOM   1682 C  CB  . ALA B 1 120 ? -8.480  28.255 -24.701 1.00 17.52 ? 120 ALA B CB  1 
ATOM   1683 N  N   . VAL B 1 121 ? -6.173  28.032 -27.136 1.00 15.74 ? 121 VAL B N   1 
ATOM   1684 C  CA  . VAL B 1 121 ? -5.347  28.798 -28.034 1.00 17.26 ? 121 VAL B CA  1 
ATOM   1685 C  C   . VAL B 1 121 ? -6.349  29.471 -28.960 1.00 17.13 ? 121 VAL B C   1 
ATOM   1686 O  O   . VAL B 1 121 ? -7.079  28.865 -29.717 1.00 20.92 ? 121 VAL B O   1 
ATOM   1687 C  CB  . VAL B 1 121 ? -4.372  27.906 -28.807 1.00 20.58 ? 121 VAL B CB  1 
ATOM   1688 C  CG1 . VAL B 1 121 ? -3.321  28.716 -29.555 1.00 25.86 ? 121 VAL B CG1 1 
ATOM   1689 C  CG2 . VAL B 1 121 ? -3.653  26.966 -27.830 1.00 24.68 ? 121 VAL B CG2 1 
ATOM   1690 N  N   . VAL B 1 122 ? -6.384  30.801 -28.891 1.00 20.45 ? 122 VAL B N   1 
ATOM   1691 C  CA  . VAL B 1 122 ? -7.374  31.568 -29.586 1.00 23.80 ? 122 VAL B CA  1 
ATOM   1692 C  C   . VAL B 1 122 ? -6.625  32.516 -30.507 1.00 24.86 ? 122 VAL B C   1 
ATOM   1693 O  O   . VAL B 1 122 ? -5.934  33.354 -30.012 1.00 24.08 ? 122 VAL B O   1 
ATOM   1694 C  CB  . VAL B 1 122 ? -8.315  32.312 -28.601 1.00 27.18 ? 122 VAL B CB  1 
ATOM   1695 C  CG1 . VAL B 1 122 ? -9.444  33.038 -29.344 1.00 34.54 ? 122 VAL B CG1 1 
ATOM   1696 C  CG2 . VAL B 1 122 ? -8.892  31.353 -27.541 1.00 29.32 ? 122 VAL B CG2 1 
ATOM   1697 N  N   . THR B 1 123 ? -6.824  32.393 -31.831 1.00 31.71 ? 123 THR B N   1 
ATOM   1698 C  CA  . THR B 1 123 ? -6.016  33.124 -32.844 1.00 33.39 ? 123 THR B CA  1 
ATOM   1699 C  C   . THR B 1 123 ? -6.940  33.740 -33.868 1.00 36.92 ? 123 THR B C   1 
ATOM   1700 O  O   . THR B 1 123 ? -8.142  33.446 -33.919 1.00 34.78 ? 123 THR B O   1 
ATOM   1701 C  CB  . THR B 1 123 ? -5.020  32.160 -33.587 1.00 39.89 ? 123 THR B CB  1 
ATOM   1702 O  OG1 . THR B 1 123 ? -5.763  31.079 -34.195 1.00 39.11 ? 123 THR B OG1 1 
ATOM   1703 C  CG2 . THR B 1 123 ? -3.951  31.539 -32.627 1.00 47.20 ? 123 THR B CG2 1 
ATOM   1704 N  N   . ASN B 1 124 ? -6.362  34.608 -34.678 1.00 43.12 ? 124 ASN B N   1 
ATOM   1705 C  CA  . ASN B 1 124 ? -7.080  35.360 -35.754 1.00 44.34 ? 124 ASN B CA  1 
ATOM   1706 C  C   . ASN B 1 124 ? -6.586  35.002 -37.151 1.00 45.77 ? 124 ASN B C   1 
ATOM   1707 O  O   . ASN B 1 124 ? -5.357  34.900 -37.395 1.00 47.25 ? 124 ASN B O   1 
ATOM   1708 C  CB  . ASN B 1 124 ? -6.980  36.859 -35.496 1.00 49.13 ? 124 ASN B CB  1 
HETATM 1709 CA CA  . CA  C 2 .   ? -18.688 -0.246 -4.299  0.80 27.69 ? 201 CA  A CA  1 
HETATM 1710 CA CA  . CA  D 2 .   ? -22.794 18.652 -37.713 1.00 51.28 ? 201 CA  B CA  1 
HETATM 1711 C  C10 . WLX E 3 .   ? 2.866   20.790 -21.618 0.50 22.47 ? 202 WLX B C10 1 
HETATM 1712 C  C11 . WLX E 3 .   ? 3.057   20.928 -22.997 0.50 27.24 ? 202 WLX B C11 1 
HETATM 1713 N  N1  . WLX E 3 .   ? -1.580  21.575 -23.810 0.50 32.46 ? 202 WLX B N1  1 
HETATM 1714 C  C2  . WLX E 3 .   ? -1.854  21.496 -22.465 0.50 21.06 ? 202 WLX B C2  1 
HETATM 1715 C  C3  . WLX E 3 .   ? -0.827  21.282 -21.541 0.50 24.71 ? 202 WLX B C3  1 
HETATM 1716 C  C4  . WLX E 3 .   ? 0.488   21.169 -21.996 0.50 25.68 ? 202 WLX B C4  1 
HETATM 1717 C  C5  . WLX E 3 .   ? -0.355  21.488 -24.355 0.50 30.16 ? 202 WLX B C5  1 
HETATM 1718 C  C6  . WLX E 3 .   ? 0.711   21.264 -23.459 0.50 27.49 ? 202 WLX B C6  1 
HETATM 1719 N  N7  . WLX E 3 .   ? -3.153  21.651 -21.973 0.50 20.76 ? 202 WLX B N7  1 
HETATM 1720 C  C8  . WLX E 3 .   ? 1.573   20.952 -21.108 0.50 24.41 ? 202 WLX B C8  1 
HETATM 1721 C  C9  . WLX E 3 .   ? 2.028   21.158 -23.905 0.50 32.66 ? 202 WLX B C9  1 
HETATM 1722 O  O   . HOH F 4 .   ? -16.189 31.877 -20.572 1.00 34.21 ? 301 HOH A O   1 
HETATM 1723 O  O   . HOH F 4 .   ? -0.176  23.184 -16.208 1.00 29.66 ? 302 HOH A O   1 
HETATM 1724 O  O   . HOH F 4 .   ? -13.290 20.421 2.292   1.00 19.01 ? 303 HOH A O   1 
HETATM 1725 O  O   . HOH F 4 .   ? -13.845 24.269 -17.849 1.00 19.88 ? 304 HOH A O   1 
HETATM 1726 O  O   . HOH F 4 .   ? -12.512 43.116 -7.006  1.00 31.05 ? 305 HOH A O   1 
HETATM 1727 O  O   . HOH F 4 .   ? -16.835 7.380  4.937   1.00 27.43 ? 306 HOH A O   1 
HETATM 1728 O  O   . HOH F 4 .   ? -19.842 0.456  -7.928  1.00 17.67 ? 307 HOH A O   1 
HETATM 1729 O  O   . HOH F 4 .   ? -11.249 6.010  -5.259  1.00 26.68 ? 308 HOH A O   1 
HETATM 1730 O  O   . HOH F 4 .   ? -22.502 0.592  -4.135  1.00 25.15 ? 309 HOH A O   1 
HETATM 1731 O  O   . HOH F 4 .   ? -11.964 31.005 -15.544 1.00 16.17 ? 310 HOH A O   1 
HETATM 1732 O  O   . HOH F 4 .   ? -14.259 8.789  2.472   1.00 26.27 ? 311 HOH A O   1 
HETATM 1733 O  O   . HOH F 4 .   ? -23.837 9.101  -7.244  1.00 18.97 ? 312 HOH A O   1 
HETATM 1734 O  O   . HOH F 4 .   ? -8.537  16.431 -10.136 1.00 26.15 ? 313 HOH A O   1 
HETATM 1735 O  O   . HOH F 4 .   ? -9.887  30.228 -17.409 1.00 15.47 ? 314 HOH A O   1 
HETATM 1736 O  O   . HOH F 4 .   ? -12.428 3.401  -2.979  1.00 21.05 ? 315 HOH A O   1 
HETATM 1737 O  O   . HOH F 4 .   ? -7.639  38.158 -20.222 1.00 26.66 ? 316 HOH A O   1 
HETATM 1738 O  O   . HOH F 4 .   ? -16.081 33.720 -3.939  1.00 23.72 ? 317 HOH A O   1 
HETATM 1739 O  O   . HOH F 4 .   ? -12.215 7.689  -9.115  1.00 19.80 ? 318 HOH A O   1 
HETATM 1740 O  O   . HOH F 4 .   ? -19.247 5.041  -11.341 1.00 25.87 ? 319 HOH A O   1 
HETATM 1741 O  O   . HOH F 4 .   ? -16.983 6.878  2.337   1.00 23.12 ? 320 HOH A O   1 
HETATM 1742 O  O   . HOH F 4 .   ? -14.398 17.375 3.934   1.00 18.55 ? 321 HOH A O   1 
HETATM 1743 O  O   . HOH F 4 .   ? -18.983 19.482 6.842   1.00 34.04 ? 322 HOH A O   1 
HETATM 1744 O  O   . HOH F 4 .   ? -14.767 32.218 -7.060  1.00 15.24 ? 323 HOH A O   1 
HETATM 1745 O  O   . HOH F 4 .   ? -8.369  29.423 -14.580 1.00 13.86 ? 324 HOH A O   1 
HETATM 1746 O  O   . HOH F 4 .   ? -2.501  27.001 -14.957 1.00 22.24 ? 325 HOH A O   1 
HETATM 1747 O  O   . HOH F 4 .   ? -22.996 19.532 3.104   1.00 42.59 ? 326 HOH A O   1 
HETATM 1748 O  O   . HOH F 4 .   ? 3.751   35.601 -4.924  1.00 20.75 ? 327 HOH A O   1 
HETATM 1749 O  O   . HOH F 4 .   ? -2.223  25.242 -16.723 1.00 34.85 ? 328 HOH A O   1 
HETATM 1750 O  O   . HOH F 4 .   ? -10.464 27.567 -15.015 1.00 23.27 ? 329 HOH A O   1 
HETATM 1751 O  O   . HOH F 4 .   ? 0.000   21.250 -14.283 0.50 27.15 ? 330 HOH A O   1 
HETATM 1752 O  O   . HOH F 4 .   ? -24.605 25.745 -1.882  1.00 21.13 ? 331 HOH A O   1 
HETATM 1753 O  O   . HOH F 4 .   ? -10.202 37.268 -6.903  1.00 28.52 ? 332 HOH A O   1 
HETATM 1754 O  O   . HOH F 4 .   ? -18.619 4.262  -5.638  1.00 20.41 ? 333 HOH A O   1 
HETATM 1755 O  O   . HOH F 4 .   ? -27.020 6.301  -3.373  1.00 16.30 ? 334 HOH A O   1 
HETATM 1756 O  O   . HOH F 4 .   ? -5.651  35.077 -4.536  1.00 24.28 ? 335 HOH A O   1 
HETATM 1757 O  O   . HOH F 4 .   ? -24.919 19.063 5.014   1.00 33.56 ? 336 HOH A O   1 
HETATM 1758 O  O   . HOH F 4 .   ? -23.769 22.174 -3.622  1.00 18.54 ? 337 HOH A O   1 
HETATM 1759 O  O   . HOH F 4 .   ? -13.345 34.607 -6.313  1.00 29.50 ? 338 HOH A O   1 
HETATM 1760 O  O   . HOH F 4 .   ? -30.912 9.561  -5.196  1.00 26.36 ? 339 HOH A O   1 
HETATM 1761 O  O   . HOH F 4 .   ? -16.074 24.920 4.623   1.00 23.75 ? 340 HOH A O   1 
HETATM 1762 O  O   . HOH F 4 .   ? -26.999 12.820 -4.798  1.00 19.84 ? 341 HOH A O   1 
HETATM 1763 O  O   . HOH F 4 .   ? -11.310 25.909 4.971   1.00 22.36 ? 342 HOH A O   1 
HETATM 1764 O  O   . HOH F 4 .   ? -5.618  12.755 0.027   1.00 27.62 ? 343 HOH A O   1 
HETATM 1765 O  O   . HOH F 4 .   ? -8.418  32.534 5.782   1.00 37.87 ? 344 HOH A O   1 
HETATM 1766 O  O   . HOH F 4 .   ? -13.909 5.141  -6.309  1.00 19.16 ? 345 HOH A O   1 
HETATM 1767 O  O   . HOH F 4 .   ? -15.330 13.231 9.278   1.00 30.90 ? 346 HOH A O   1 
HETATM 1768 O  O   . HOH F 4 .   ? -3.211  20.636 -10.626 1.00 28.80 ? 347 HOH A O   1 
HETATM 1769 O  O   . HOH F 4 .   ? -17.821 0.540  -1.492  1.00 44.38 ? 348 HOH A O   1 
HETATM 1770 O  O   . HOH F 4 .   ? -17.585 33.560 -6.370  1.00 29.53 ? 349 HOH A O   1 
HETATM 1771 O  O   . HOH F 4 .   ? -1.378  13.627 -7.765  1.00 31.05 ? 350 HOH A O   1 
HETATM 1772 O  O   . HOH F 4 .   ? -26.815 19.764 0.268   1.00 36.22 ? 351 HOH A O   1 
HETATM 1773 O  O   . HOH F 4 .   ? -20.647 -0.798 -5.995  1.00 35.44 ? 352 HOH A O   1 
HETATM 1774 O  O   . HOH F 4 .   ? -26.247 14.768 -2.410  1.00 29.57 ? 353 HOH A O   1 
HETATM 1775 O  O   . HOH F 4 .   ? -24.339 24.693 -4.573  1.00 18.34 ? 354 HOH A O   1 
HETATM 1776 O  O   . HOH F 4 .   ? -10.151 3.828  -4.498  1.00 26.27 ? 355 HOH A O   1 
HETATM 1777 O  O   . HOH F 4 .   ? -24.802 6.520  -6.993  1.00 31.15 ? 356 HOH A O   1 
HETATM 1778 O  O   . HOH F 4 .   ? -24.178 3.005  -3.769  1.00 23.32 ? 357 HOH A O   1 
HETATM 1779 O  O   . HOH F 4 .   ? -18.215 1.423  1.122   1.00 40.85 ? 358 HOH A O   1 
HETATM 1780 O  O   . HOH F 4 .   ? -30.445 6.958  -3.982  1.00 26.29 ? 359 HOH A O   1 
HETATM 1781 O  O   . HOH F 4 .   ? -25.937 25.344 -6.829  1.00 31.65 ? 360 HOH A O   1 
HETATM 1782 O  O   . HOH F 4 .   ? -17.777 33.251 -1.779  1.00 22.31 ? 361 HOH A O   1 
HETATM 1783 O  O   . HOH F 4 .   ? -5.000  37.445 -19.799 1.00 21.87 ? 362 HOH A O   1 
HETATM 1784 O  O   . HOH F 4 .   ? -3.809  38.790 -17.783 1.00 25.27 ? 363 HOH A O   1 
HETATM 1785 O  O   . HOH G 4 .   ? -20.870 18.783 -36.635 1.00 40.75 ? 301 HOH B O   1 
HETATM 1786 O  O   . HOH G 4 .   ? -8.391  -1.825 -19.063 1.00 29.97 ? 302 HOH B O   1 
HETATM 1787 O  O   . HOH G 4 .   ? -14.307 8.035  -11.750 1.00 16.52 ? 303 HOH B O   1 
HETATM 1788 O  O   . HOH G 4 .   ? -0.000  21.250 -18.128 0.50 26.27 ? 304 HOH B O   1 
HETATM 1789 O  O   . HOH G 4 .   ? -2.029  17.581 -15.683 1.00 27.97 ? 305 HOH B O   1 
HETATM 1790 O  O   . HOH G 4 .   ? -10.260 9.610  -16.867 1.00 16.03 ? 306 HOH B O   1 
HETATM 1791 O  O   . HOH G 4 .   ? -20.002 9.410  -15.746 1.00 32.35 ? 307 HOH B O   1 
HETATM 1792 O  O   . HOH G 4 .   ? -24.014 18.935 -35.488 1.00 37.81 ? 308 HOH B O   1 
HETATM 1793 O  O   . HOH G 4 .   ? -8.418  10.836 -15.308 1.00 17.24 ? 309 HOH B O   1 
HETATM 1794 O  O   . HOH G 4 .   ? -13.309 15.972 -14.593 1.00 16.86 ? 310 HOH B O   1 
HETATM 1795 O  O   . HOH G 4 .   ? -14.298 32.885 -22.925 1.00 31.11 ? 311 HOH B O   1 
HETATM 1796 O  O   . HOH G 4 .   ? -14.653 23.271 -36.513 1.00 29.17 ? 312 HOH B O   1 
HETATM 1797 O  O   . HOH G 4 .   ? -7.020  12.008 -17.891 1.00 12.94 ? 313 HOH B O   1 
HETATM 1798 O  O   . HOH G 4 .   ? -12.638 1.685  -23.040 1.00 32.48 ? 314 HOH B O   1 
HETATM 1799 O  O   . HOH G 4 .   ? -9.505  13.250 -17.391 1.00 25.84 ? 315 HOH B O   1 
HETATM 1800 O  O   . HOH G 4 .   ? -9.277  24.767 -22.607 1.00 20.10 ? 316 HOH B O   1 
HETATM 1801 O  O   . HOH G 4 .   ? -10.935 12.789 -36.427 1.00 29.23 ? 317 HOH B O   1 
HETATM 1802 O  O   . HOH G 4 .   ? 5.781   7.590  -27.520 1.00 31.76 ? 318 HOH B O   1 
HETATM 1803 O  O   . HOH G 4 .   ? -12.694 8.009  -25.401 1.00 21.25 ? 319 HOH B O   1 
HETATM 1804 O  O   . HOH G 4 .   ? -3.219  4.720  -12.632 1.00 20.92 ? 320 HOH B O   1 
HETATM 1805 O  O   . HOH G 4 .   ? -6.415  28.618 -32.459 1.00 30.68 ? 321 HOH B O   1 
HETATM 1806 O  O   . HOH G 4 .   ? -1.296  15.540 -17.493 1.00 26.54 ? 322 HOH B O   1 
HETATM 1807 O  O   . HOH G 4 .   ? -3.277  6.919  -28.020 1.00 21.45 ? 323 HOH B O   1 
HETATM 1808 O  O   . HOH G 4 .   ? -10.193 15.167 -37.388 1.00 31.09 ? 324 HOH B O   1 
HETATM 1809 O  O   . HOH G 4 .   ? -14.667 11.598 -35.851 1.00 26.38 ? 325 HOH B O   1 
HETATM 1810 O  O   . HOH G 4 .   ? -17.398 12.445 -24.342 1.00 25.29 ? 326 HOH B O   1 
HETATM 1811 O  O   . HOH G 4 .   ? 2.559   13.944 -24.593 1.00 25.98 ? 327 HOH B O   1 
HETATM 1812 O  O   . HOH G 4 .   ? -7.373  4.154  -25.985 1.00 31.41 ? 328 HOH B O   1 
HETATM 1813 O  O   . HOH G 4 .   ? -22.633 16.182 -28.574 1.00 33.69 ? 329 HOH B O   1 
HETATM 1814 O  O   . HOH G 4 .   ? -6.306  5.560  -5.680  1.00 32.89 ? 330 HOH B O   1 
HETATM 1815 O  O   . HOH G 4 .   ? -11.913 -0.793 -22.232 1.00 35.24 ? 331 HOH B O   1 
HETATM 1816 O  O   . HOH G 4 .   ? -21.249 11.743 -14.845 1.00 32.82 ? 332 HOH B O   1 
HETATM 1817 O  O   . HOH G 4 .   ? -1.267  3.110  -14.044 1.00 30.63 ? 333 HOH B O   1 
HETATM 1818 O  O   . HOH G 4 .   ? 0.189   3.998  -16.326 1.00 33.67 ? 334 HOH B O   1 
# 
loop_
_atom_site_anisotrop.id 
_atom_site_anisotrop.type_symbol 
_atom_site_anisotrop.pdbx_label_atom_id 
_atom_site_anisotrop.pdbx_label_alt_id 
_atom_site_anisotrop.pdbx_label_comp_id 
_atom_site_anisotrop.pdbx_label_asym_id 
_atom_site_anisotrop.pdbx_label_seq_id 
_atom_site_anisotrop.pdbx_PDB_ins_code 
_atom_site_anisotrop.U[1][1] 
_atom_site_anisotrop.U[2][2] 
_atom_site_anisotrop.U[3][3] 
_atom_site_anisotrop.U[1][2] 
_atom_site_anisotrop.U[1][3] 
_atom_site_anisotrop.U[2][3] 
_atom_site_anisotrop.pdbx_auth_seq_id 
_atom_site_anisotrop.pdbx_auth_comp_id 
_atom_site_anisotrop.pdbx_auth_asym_id 
_atom_site_anisotrop.pdbx_auth_atom_id 
1    C  CA  . CYS A 10  ? 0.5348 0.7323 0.3491 0.1412  0.0301  -0.0187 10  CYS A CA  
2    C  C   . CYS A 10  ? 0.4000 0.3836 0.3890 -0.0693 -0.0113 0.1195  10  CYS A C   
3    O  O   . CYS A 10  ? 0.3160 0.5360 0.5629 -0.0459 -0.0536 0.2588  10  CYS A O   
4    N  N   . PRO A 11  ? 0.3676 0.2190 0.2980 -0.0017 0.0407  0.1033  11  PRO A N   
5    C  CA  . PRO A 11  ? 0.1604 0.2529 0.3079 0.0485  0.0445  0.0397  11  PRO A CA  
6    C  C   . PRO A 11  ? 0.1705 0.2205 0.2493 0.0161  0.0663  -0.0064 11  PRO A C   
7    O  O   . PRO A 11  ? 0.2197 0.1848 0.2484 -0.0036 0.0965  0.0455  11  PRO A O   
8    C  CB  . PRO A 11  ? 0.3534 0.3237 0.1935 -0.0948 0.0324  0.0203  11  PRO A CB  
9    C  CG  . PRO A 11  ? 0.2080 0.3428 0.4136 -0.1078 0.1053  0.0469  11  PRO A CG  
10   C  CD  . PRO A 11  ? 0.3431 0.2493 0.2282 -0.0219 0.0639  0.0016  11  PRO A CD  
11   N  N   . LEU A 12  ? 0.2057 0.1599 0.2236 0.0305  0.0709  0.0034  12  LEU A N   
12   C  CA  . LEU A 12  ? 0.2288 0.1906 0.1929 -0.0343 0.0446  -0.0024 12  LEU A CA  
13   C  C   . LEU A 12  ? 0.2618 0.1703 0.2137 -0.0201 0.0981  0.0148  12  LEU A C   
14   O  O   . LEU A 12  ? 0.3064 0.1725 0.3057 -0.0343 0.1612  0.0000  12  LEU A O   
15   C  CB  . LEU A 12  ? 0.2258 0.1639 0.2289 -0.0121 0.0556  0.0214  12  LEU A CB  
16   C  CG  . LEU A 12  ? 0.2519 0.1224 0.2423 -0.0100 0.0179  0.0193  12  LEU A CG  
17   C  CD1 . LEU A 12  ? 0.2761 0.2355 0.2324 0.0473  0.0321  0.0573  12  LEU A CD1 
18   C  CD2 . LEU A 12  ? 0.2297 0.1812 0.3110 0.0386  0.0248  0.0674  12  LEU A CD2 
19   N  N   . MET A 13  ? 0.2165 0.0884 0.2014 0.0006  0.0429  0.0058  13  MET A N   
20   C  CA  . MET A 13  ? 0.2060 0.1209 0.2076 -0.0126 0.0407  0.0267  13  MET A CA  
21   C  C   . MET A 13  ? 0.2118 0.1341 0.1907 -0.0119 0.0327  0.0239  13  MET A C   
22   O  O   . MET A 13  ? 0.1964 0.1374 0.1984 0.0052  0.0299  0.0203  13  MET A O   
23   C  CB  . MET A 13  ? 0.2969 0.1543 0.1988 -0.0554 0.0011  0.0534  13  MET A CB  
24   C  CG  . MET A 13  ? 0.2445 0.1514 0.2033 0.0083  -0.0237 0.0508  13  MET A CG  
25   S  SD  . MET A 13  ? 0.1952 0.2392 0.2672 0.0063  0.0161  0.0568  13  MET A SD  
26   C  CE  . MET A 13  ? 0.2625 0.3499 0.3280 0.0827  -0.0954 -0.0550 13  MET A CE  
27   N  N   . VAL A 14  ? 0.1838 0.1230 0.1613 -0.0050 0.0084  -0.0030 14  VAL A N   
28   C  CA  . VAL A 14  ? 0.1493 0.1279 0.1739 -0.0039 0.0091  0.0199  14  VAL A CA  
29   C  C   . VAL A 14  ? 0.2119 0.1062 0.1439 -0.0210 0.0260  -0.0077 14  VAL A C   
30   O  O   . VAL A 14  ? 0.2460 0.1506 0.1744 -0.0283 0.0667  -0.0327 14  VAL A O   
31   C  CB  . VAL A 14  ? 0.1828 0.1374 0.1787 0.0200  0.0130  -0.0115 14  VAL A CB  
32   C  CG1 . VAL A 14  ? 0.1942 0.1762 0.1946 0.0338  -0.0081 0.0004  14  VAL A CG1 
33   C  CG2 . VAL A 14  ? 0.2069 0.1095 0.2180 0.0287  -0.0381 0.0092  14  VAL A CG2 
34   N  N   . LYS A 15  ? 0.1886 0.0853 0.1460 -0.0344 0.0159  0.0044  15  LYS A N   
35   C  CA  . LYS A 15  ? 0.1981 0.1613 0.1276 -0.0561 -0.0040 0.0211  15  LYS A CA  
36   C  C   . LYS A 15  ? 0.2083 0.1162 0.1343 -0.0122 0.0044  0.0123  15  LYS A C   
37   O  O   . LYS A 15  ? 0.2560 0.1342 0.1259 -0.0274 0.0234  0.0153  15  LYS A O   
38   C  CB  . LYS A 15  ? 0.2213 0.1915 0.1757 -0.0380 -0.0134 0.0471  15  LYS A CB  
39   N  N   . VAL A 16  ? 0.1987 0.1177 0.1366 -0.0128 -0.0108 -0.0121 16  VAL A N   
40   C  CA  . VAL A 16  ? 0.1780 0.1783 0.1485 -0.0297 -0.0038 -0.0114 16  VAL A CA  
41   C  C   . VAL A 16  ? 0.2007 0.1290 0.1232 -0.0299 0.0015  0.0010  16  VAL A C   
42   O  O   . VAL A 16  ? 0.1851 0.1472 0.1441 -0.0456 -0.0020 -0.0079 16  VAL A O   
43   C  CB  . VAL A 16  ? 0.1602 0.1470 0.1788 -0.0531 -0.0096 0.0067  16  VAL A CB  
44   C  CG1 . VAL A 16  ? 0.2039 0.1049 0.1845 -0.0296 -0.0012 0.0203  16  VAL A CG1 
45   C  CG2 . VAL A 16  ? 0.1522 0.1521 0.1824 -0.0291 0.0150  0.0053  16  VAL A CG2 
46   N  N   . LEU A 17  ? 0.1591 0.1167 0.1579 -0.0551 -0.0016 0.0054  17  LEU A N   
47   C  CA  . LEU A 17  ? 0.1457 0.1398 0.1331 -0.0464 -0.0125 0.0009  17  LEU A CA  
48   C  C   . LEU A 17  ? 0.1454 0.0960 0.1449 -0.0162 -0.0130 -0.0042 17  LEU A C   
49   O  O   . LEU A 17  ? 0.1626 0.1390 0.1353 -0.0437 -0.0333 0.0224  17  LEU A O   
50   C  CB  . LEU A 17  ? 0.1620 0.1364 0.2067 -0.0483 -0.0157 0.0130  17  LEU A CB  
51   C  CG  . LEU A 17  ? 0.2350 0.1867 0.1932 -0.0133 -0.0149 0.0252  17  LEU A CG  
52   C  CD1 . LEU A 17  ? 0.2094 0.2251 0.2492 0.0026  -0.0836 0.0250  17  LEU A CD1 
53   C  CD2 . LEU A 17  ? 0.2636 0.2077 0.2073 -0.0121 -0.0824 0.0268  17  LEU A CD2 
54   N  N   . ASP A 18  ? 0.1536 0.1094 0.1513 -0.0419 -0.0282 0.0142  18  ASP A N   
55   C  CA  . ASP A 18  ? 0.1369 0.1139 0.1438 -0.0099 0.0029  0.0000  18  ASP A CA  
56   C  C   . ASP A 18  ? 0.1341 0.0605 0.1597 -0.0058 -0.0267 0.0030  18  ASP A C   
57   O  O   . ASP A 18  ? 0.1443 0.1180 0.1504 -0.0111 -0.0289 -0.0013 18  ASP A O   
58   C  CB  . ASP A 18  ? 0.1160 0.1342 0.1642 -0.0160 0.0229  -0.0111 18  ASP A CB  
59   C  CG  . ASP A 18  ? 0.1774 0.1217 0.1689 -0.0028 0.0479  -0.0198 18  ASP A CG  
60   O  OD1 . ASP A 18  ? 0.1564 0.1061 0.1877 -0.0069 0.0069  0.0251  18  ASP A OD1 
61   O  OD2 . ASP A 18  ? 0.1846 0.1497 0.2359 0.0076  0.0323  0.0027  18  ASP A OD2 
62   N  N   . ALA A 19  ? 0.1438 0.0879 0.1794 -0.0158 -0.0006 0.0174  19  ALA A N   
63   C  CA  . ALA A 19  ? 0.1398 0.1167 0.1228 -0.0118 -0.0290 0.0173  19  ALA A CA  
64   C  C   . ALA A 19  ? 0.1014 0.1263 0.1807 -0.0113 0.0137  0.0209  19  ALA A C   
65   O  O   . ALA A 19  ? 0.1307 0.1639 0.2019 -0.0337 0.0182  0.0120  19  ALA A O   
66   C  CB  . ALA A 19  ? 0.1559 0.1353 0.1680 0.0185  0.0204  -0.0037 19  ALA A CB  
67   N  N   . VAL A 20  ? 0.1020 0.1222 0.1972 -0.0276 -0.0053 0.0226  20  VAL A N   
68   C  CA  . VAL A 20  ? 0.1355 0.1679 0.1935 -0.0362 0.0062  0.0514  20  VAL A CA  
69   C  C   . VAL A 20  ? 0.1428 0.1400 0.2218 -0.0098 -0.0045 0.0490  20  VAL A C   
70   O  O   . VAL A 20  ? 0.1760 0.1500 0.2494 -0.0334 0.0087  0.0138  20  VAL A O   
71   C  CB  . VAL A 20  ? 0.1749 0.1255 0.2220 -0.0242 -0.0225 0.0486  20  VAL A CB  
72   C  CG1 . VAL A 20  ? 0.1935 0.1182 0.2450 -0.0173 -0.0460 0.0331  20  VAL A CG1 
73   C  CG2 . VAL A 20  ? 0.2169 0.1989 0.2295 -0.0145 -0.0469 0.0918  20  VAL A CG2 
74   N  N   . ARG A 21  ? 0.1854 0.1185 0.1800 -0.0259 -0.0084 -0.0013 21  ARG A N   
75   C  CA  . ARG A 21  ? 0.1748 0.1662 0.2013 -0.0279 0.0040  -0.0302 21  ARG A CA  
76   C  C   . ARG A 21  ? 0.1549 0.1940 0.2030 -0.0292 -0.0195 -0.0218 21  ARG A C   
77   O  O   . ARG A 21  ? 0.2021 0.1840 0.2174 -0.0549 -0.0180 -0.0173 21  ARG A O   
78   C  CB  . ARG A 21  ? 0.3089 0.1994 0.2416 0.0409  0.0015  -0.0784 21  ARG A CB  
79   C  CG  . ARG A 21  ? 0.3137 0.1811 0.3472 0.0207  0.0026  -0.0360 21  ARG A CG  
80   C  CD  . ARG A 21  ? 0.3555 0.3272 0.5022 0.0478  -0.0077 0.0487  21  ARG A CD  
81   N  NE  . ARG A 21  ? 0.4812 0.5463 0.5506 0.0233  0.0565  -0.0674 21  ARG A NE  
82   C  CZ  . ARG A 21  ? 0.3252 0.3834 0.4621 -0.0046 0.0600  0.1604  21  ARG A CZ  
83   N  N   . GLY A 22  ? 0.1369 0.1841 0.1605 -0.0390 -0.0088 -0.0098 22  GLY A N   
84   C  CA  . GLY A 22  ? 0.1492 0.1508 0.1789 -0.0279 -0.0260 -0.0181 22  GLY A CA  
85   C  C   . GLY A 22  ? 0.1098 0.1148 0.1614 -0.0072 -0.0253 -0.0119 22  GLY A C   
86   O  O   . GLY A 22  ? 0.1332 0.1296 0.1809 0.0087  -0.0142 -0.0298 22  GLY A O   
87   N  N   . SER A 23  ? 0.1219 0.1355 0.1832 -0.0184 -0.0003 -0.0096 23  SER A N   
88   C  CA  . SER A 23  ? 0.1438 0.1211 0.1629 -0.0118 -0.0167 -0.0202 23  SER A CA  
89   C  C   . SER A 23  ? 0.1402 0.1650 0.1833 0.0033  0.0188  0.0005  23  SER A C   
90   O  O   . SER A 23  ? 0.1810 0.1822 0.1749 -0.0641 -0.0102 0.0221  23  SER A O   
91   C  CB  . SER A 23  ? 0.1851 0.1576 0.2349 -0.0157 0.0261  -0.0036 23  SER A CB  
92   O  OG  . SER A 23  ? 0.2529 0.2544 0.3167 0.0231  -0.0001 -0.0057 23  SER A OG  
93   N  N   . PRO A 24  ? 0.1302 0.1670 0.1628 -0.0103 -0.0095 -0.0259 24  PRO A N   
94   C  CA  . PRO A 24  ? 0.1497 0.1639 0.1996 -0.0205 0.0037  -0.0125 24  PRO A CA  
95   C  C   . PRO A 24  ? 0.1685 0.1540 0.2016 -0.0019 -0.0161 -0.0148 24  PRO A C   
96   O  O   . PRO A 24  ? 0.1739 0.1657 0.2334 -0.0513 0.0138  -0.0154 24  PRO A O   
97   C  CB  . PRO A 24  ? 0.1822 0.1888 0.2469 -0.0434 0.0330  0.0000  24  PRO A CB  
98   C  CG  . PRO A 24  ? 0.3076 0.5409 0.1511 -0.1543 -0.0187 -0.0368 24  PRO A CG  
99   C  CD  . PRO A 24  ? 0.1804 0.1736 0.1591 0.0027  -0.0029 0.0199  24  PRO A CD  
100  N  N   . ALA A 25  ? 0.1592 0.1132 0.2034 -0.0277 -0.0146 0.0070  25  ALA A N   
101  C  CA  . ALA A 25  ? 0.1816 0.0903 0.1979 -0.0218 0.0197  0.0079  25  ALA A CA  
102  C  C   . ALA A 25  ? 0.1400 0.1497 0.1919 -0.0368 -0.0020 0.0004  25  ALA A C   
103  O  O   . ALA A 25  ? 0.1640 0.1471 0.2152 -0.0490 0.0243  -0.0101 25  ALA A O   
104  C  CB  . ALA A 25  ? 0.1737 0.1782 0.1922 -0.0370 0.0220  0.0201  25  ALA A CB  
105  N  N   . ILE A 26  ? 0.1657 0.1249 0.2189 -0.0191 0.0047  0.0402  26  ILE A N   
106  C  CA  A ILE A 26  ? 0.1857 0.1035 0.2034 -0.0388 -0.0044 0.0081  26  ILE A CA  
107  C  CA  B ILE A 26  ? 0.1857 0.1183 0.2041 -0.0390 -0.0043 0.0096  26  ILE A CA  
108  C  C   . ILE A 26  ? 0.1982 0.1161 0.1976 -0.0308 0.0015  0.0019  26  ILE A C   
109  O  O   . ILE A 26  ? 0.1750 0.1980 0.2332 -0.0143 0.0145  -0.0178 26  ILE A O   
110  C  CB  A ILE A 26  ? 0.2019 0.1776 0.2230 -0.0483 -0.0254 -0.0295 26  ILE A CB  
111  C  CB  B ILE A 26  ? 0.1854 0.1552 0.2138 -0.0755 0.0086  0.0071  26  ILE A CB  
112  C  CG1 A ILE A 26  ? 0.2029 0.1806 0.2496 -0.0524 -0.0188 -0.0155 26  ILE A CG1 
113  C  CG1 B ILE A 26  ? 0.2092 0.1631 0.2095 -0.0361 -0.0756 0.0023  26  ILE A CG1 
114  C  CG2 A ILE A 26  ? 0.2807 0.1082 0.2115 0.0097  -0.0249 -0.0429 26  ILE A CG2 
115  C  CG2 B ILE A 26  ? 0.2086 0.1995 0.2553 -0.0477 -0.0125 -0.0010 26  ILE A CG2 
116  C  CD1 A ILE A 26  ? 0.2149 0.2747 0.3617 -0.0778 -0.0312 -0.1335 26  ILE A CD1 
117  C  CD1 B ILE A 26  ? 0.2896 0.2009 0.2859 -0.0588 -0.0340 -0.0751 26  ILE A CD1 
118  N  N   . ASN A 27  ? 0.1890 0.1370 0.1777 -0.0227 0.0105  0.0252  27  ASN A N   
119  C  CA  A ASN A 27  ? 0.1601 0.0987 0.2517 -0.0152 0.0269  0.0208  27  ASN A CA  
120  C  CA  B ASN A 27  ? 0.1679 0.1138 0.2564 -0.0119 0.0194  0.0245  27  ASN A CA  
121  C  C   . ASN A 27  ? 0.1690 0.1180 0.2440 -0.0220 0.0046  0.0299  27  ASN A C   
122  O  O   . ASN A 27  ? 0.2117 0.1547 0.2838 0.0116  -0.0439 0.0118  27  ASN A O   
123  C  CB  A ASN A 27  ? 0.1721 0.1250 0.2637 0.0444  0.0299  0.0101  27  ASN A CB  
124  C  CB  B ASN A 27  ? 0.2305 0.1221 0.3484 0.0001  -0.0071 0.0446  27  ASN A CB  
125  C  CG  A ASN A 27  ? 0.1305 0.2818 0.2836 0.0083  -0.0144 -0.0001 27  ASN A CG  
126  C  CG  B ASN A 27  ? 0.3866 0.3189 0.3350 0.0032  0.0465  0.1252  27  ASN A CG  
127  O  OD1 A ASN A 27  ? 0.3281 0.1716 0.4682 0.0658  -0.0115 -0.0387 27  ASN A OD1 
128  O  OD1 B ASN A 27  ? 0.5117 0.3497 0.3114 -0.0841 -0.0293 -0.0972 27  ASN A OD1 
129  N  ND2 A ASN A 27  ? 0.4584 0.0554 0.3019 0.1000  -0.0076 -0.0135 27  ASN A ND2 
130  N  ND2 B ASN A 27  ? 0.2826 0.6204 0.5028 -0.0879 -0.0620 0.0496  27  ASN A ND2 
131  N  N   . VAL A 28  ? 0.1594 0.1528 0.2095 -0.0047 0.0119  0.0048  28  VAL A N   
132  C  CA  . VAL A 28  ? 0.1682 0.1504 0.1866 -0.0155 0.0009  0.0281  28  VAL A CA  
133  C  C   . VAL A 28  ? 0.1526 0.1377 0.1732 -0.0074 -0.0031 0.0112  28  VAL A C   
134  O  O   . VAL A 28  ? 0.1468 0.1482 0.1983 -0.0084 -0.0089 0.0199  28  VAL A O   
135  C  CB  . VAL A 28  ? 0.1662 0.1158 0.1999 -0.0227 0.0035  0.0219  28  VAL A CB  
136  C  CG1 . VAL A 28  ? 0.1908 0.2512 0.2055 -0.0663 0.0476  0.0060  28  VAL A CG1 
137  C  CG2 . VAL A 28  ? 0.1643 0.1609 0.2289 -0.0332 0.0289  -0.0131 28  VAL A CG2 
138  N  N   . ALA A 29  ? 0.1271 0.1064 0.1801 0.0000  0.0225  0.0074  29  ALA A N   
139  C  CA  . ALA A 29  ? 0.1206 0.1306 0.1813 -0.0097 0.0006  -0.0019 29  ALA A CA  
140  C  C   . ALA A 29  ? 0.1737 0.1348 0.1445 -0.0182 -0.0051 0.0039  29  ALA A C   
141  O  O   . ALA A 29  ? 0.1811 0.0887 0.1909 -0.0085 0.0038  0.0238  29  ALA A O   
142  C  CB  . ALA A 29  ? 0.1577 0.0894 0.1881 -0.0053 0.0083  0.0053  29  ALA A CB  
143  N  N   . VAL A 30  ? 0.1289 0.1254 0.1509 -0.0065 0.0179  -0.0050 30  VAL A N   
144  C  CA  . VAL A 30  ? 0.1551 0.1201 0.1670 0.0018  0.0146  -0.0263 30  VAL A CA  
145  C  C   . VAL A 30  ? 0.1788 0.0926 0.1423 0.0319  0.0061  0.0118  30  VAL A C   
146  O  O   . VAL A 30  ? 0.1594 0.1470 0.1870 -0.0174 0.0164  -0.0200 30  VAL A O   
147  C  CB  . VAL A 30  ? 0.1486 0.1101 0.1919 -0.0146 0.0334  0.0141  30  VAL A CB  
148  C  CG1 . VAL A 30  ? 0.1509 0.1450 0.2585 0.0027  -0.0067 -0.0077 30  VAL A CG1 
149  C  CG2 . VAL A 30  ? 0.1415 0.1345 0.2111 0.0063  0.0295  0.0061  30  VAL A CG2 
150  N  N   . HIS A 31  ? 0.1558 0.1245 0.1764 -0.0124 0.0277  0.0099  31  HIS A N   
151  C  CA  . HIS A 31  ? 0.1342 0.1163 0.2128 -0.0025 0.0356  0.0002  31  HIS A CA  
152  C  C   . HIS A 31  ? 0.1769 0.1333 0.1742 -0.0009 0.0414  -0.0105 31  HIS A C   
153  O  O   . HIS A 31  ? 0.1955 0.1048 0.2032 -0.0208 0.0484  0.0061  31  HIS A O   
154  C  CB  . HIS A 31  ? 0.1520 0.1535 0.2049 -0.0182 0.0277  0.0120  31  HIS A CB  
155  C  CG  . HIS A 31  ? 0.1808 0.1798 0.2371 0.0072  0.0063  -0.0030 31  HIS A CG  
156  N  ND1 . HIS A 31  ? 0.2234 0.2434 0.2462 0.0325  -0.0027 -0.0210 31  HIS A ND1 
157  C  CD2 . HIS A 31  ? 0.1410 0.1455 0.2315 0.0181  0.0063  -0.0097 31  HIS A CD2 
158  C  CE1 . HIS A 31  ? 0.1914 0.0920 0.2987 0.0316  0.0003  0.0406  31  HIS A CE1 
159  N  NE2 . HIS A 31  ? 0.2695 0.1924 0.3348 0.0400  -0.0290 -0.0162 31  HIS A NE2 
160  N  N   . VAL A 32  ? 0.1426 0.1452 0.1614 -0.0140 0.0550  -0.0263 32  VAL A N   
161  C  CA  . VAL A 32  ? 0.1317 0.1370 0.2063 0.0183  0.0194  -0.0144 32  VAL A CA  
162  C  C   . VAL A 32  ? 0.1381 0.0765 0.1990 0.0085  0.0365  -0.0120 32  VAL A C   
163  O  O   . VAL A 32  ? 0.1462 0.0937 0.2101 -0.0149 0.0328  -0.0253 32  VAL A O   
164  C  CB  . VAL A 32  ? 0.1741 0.0868 0.1880 -0.0168 0.0086  -0.0126 32  VAL A CB  
165  C  CG1 . VAL A 32  ? 0.1732 0.0938 0.2469 -0.0254 -0.0003 -0.0072 32  VAL A CG1 
166  C  CG2 . VAL A 32  ? 0.1775 0.1217 0.2393 0.0024  -0.0092 -0.0220 32  VAL A CG2 
167  N  N   . PHE A 33  ? 0.1438 0.1111 0.2176 -0.0147 -0.0017 -0.0231 33  PHE A N   
168  C  CA  . PHE A 33  ? 0.1291 0.1277 0.2261 0.0118  0.0179  -0.0335 33  PHE A CA  
169  C  C   . PHE A 33  ? 0.1215 0.1313 0.2401 0.0176  0.0473  -0.0308 33  PHE A C   
170  O  O   . PHE A 33  ? 0.1275 0.1042 0.2059 -0.0027 0.0284  -0.0089 33  PHE A O   
171  C  CB  . PHE A 33  ? 0.1879 0.1168 0.2688 0.0105  -0.0418 -0.0326 33  PHE A CB  
172  C  CG  . PHE A 33  ? 0.1749 0.1172 0.2942 -0.0034 -0.0016 -0.0422 33  PHE A CG  
173  C  CD1 . PHE A 33  ? 0.1753 0.1569 0.2896 -0.0013 -0.0168 -0.0155 33  PHE A CD1 
174  C  CD2 . PHE A 33  ? 0.1630 0.1711 0.3321 -0.0138 -0.0104 -0.0305 33  PHE A CD2 
175  C  CE1 . PHE A 33  ? 0.1966 0.1712 0.2830 -0.0121 -0.0449 0.0025  33  PHE A CE1 
176  C  CE2 . PHE A 33  ? 0.1915 0.1839 0.3251 0.0206  0.0284  0.0220  33  PHE A CE2 
177  C  CZ  . PHE A 33  ? 0.2073 0.1280 0.3419 0.0125  -0.0174 0.0395  33  PHE A CZ  
178  N  N   . ARG A 34  ? 0.1501 0.0826 0.2797 0.0122  0.0222  -0.0240 34  ARG A N   
179  C  CA  . ARG A 34  ? 0.1540 0.0954 0.2466 -0.0160 0.0243  -0.0354 34  ARG A CA  
180  C  C   . ARG A 34  ? 0.1348 0.0938 0.2758 -0.0085 -0.0005 -0.0006 34  ARG A C   
181  O  O   . ARG A 34  ? 0.1604 0.1501 0.2762 -0.0080 0.0203  -0.0718 34  ARG A O   
182  C  CB  . ARG A 34  ? 0.1487 0.1158 0.2656 0.0138  0.0236  -0.0386 34  ARG A CB  
183  C  CG  . ARG A 34  ? 0.1487 0.1259 0.2734 -0.0114 -0.0331 0.0013  34  ARG A CG  
184  C  CD  . ARG A 34  ? 0.2104 0.1410 0.2451 0.0406  0.0167  -0.0771 34  ARG A CD  
185  N  NE  . ARG A 34  ? 0.1963 0.1821 0.2356 0.0295  0.0020  -0.0522 34  ARG A NE  
186  C  CZ  . ARG A 34  ? 0.2464 0.1499 0.2396 0.0103  -0.0359 -0.0472 34  ARG A CZ  
187  N  NH1 . ARG A 34  ? 0.2022 0.2001 0.2578 -0.0357 0.0186  0.0062  34  ARG A NH1 
188  N  NH2 . ARG A 34  ? 0.1650 0.1537 0.3006 -0.0188 0.0024  -0.0055 34  ARG A NH2 
189  N  N   . LYS A 35  ? 0.1376 0.1422 0.2372 0.0027  0.0022  -0.0175 35  LYS A N   
190  C  CA  . LYS A 35  ? 0.1668 0.1468 0.2227 0.0172  0.0033  -0.0261 35  LYS A CA  
191  C  C   . LYS A 35  ? 0.1574 0.1514 0.2385 -0.0085 -0.0242 -0.0019 35  LYS A C   
192  O  O   . LYS A 35  ? 0.1672 0.1829 0.2756 -0.0216 -0.0191 0.0078  35  LYS A O   
193  C  CB  . LYS A 35  ? 0.2224 0.1567 0.2520 0.0139  0.0231  -0.0593 35  LYS A CB  
194  C  CG  . LYS A 35  ? 0.3357 0.3857 0.3459 0.0269  -0.0134 -0.1387 35  LYS A CG  
195  C  CD  . LYS A 35  ? 0.4681 0.3445 0.4888 0.0590  -0.0160 -0.2358 35  LYS A CD  
196  N  N   . ALA A 36  ? 0.1849 0.1243 0.2895 0.0133  0.0137  0.0191  36  ALA A N   
197  C  CA  . ALA A 36  ? 0.1768 0.2179 0.2562 -0.0179 0.0095  -0.0038 36  ALA A CA  
198  C  C   . ALA A 36  ? 0.2244 0.2778 0.3522 -0.0415 -0.0131 -0.0147 36  ALA A C   
199  O  O   . ALA A 36  ? 0.2695 0.2080 0.3612 -0.0467 -0.0464 -0.0426 36  ALA A O   
200  C  CB  . ALA A 36  ? 0.1833 0.3025 0.3584 -0.0285 -0.0055 -0.0460 36  ALA A CB  
201  N  N   . ALA A 37  ? 0.3144 0.3519 0.2949 -0.1266 -0.0632 0.0800  37  ALA A N   
202  C  CA  . ALA A 37  ? 0.5257 0.3186 0.4226 -0.1321 -0.1530 0.1137  37  ALA A CA  
203  C  C   . ALA A 37  ? 0.5974 0.3800 0.2893 -0.0773 -0.0053 0.0605  37  ALA A C   
204  O  O   . ALA A 37  ? 0.5363 0.4388 0.4378 -0.0619 -0.1060 -0.0663 37  ALA A O   
205  C  CB  . ALA A 37  ? 0.8750 0.3388 0.4308 -0.5046 -0.0248 -0.0599 37  ALA A CB  
206  N  N   . ASP A 38  ? 0.2908 0.4108 0.4212 -0.1585 -0.1499 0.0683  38  ASP A N   
207  C  CA  . ASP A 38  ? 0.3076 0.4886 0.3614 -0.1740 -0.0984 0.0667  38  ASP A CA  
208  C  C   . ASP A 38  ? 0.2755 0.3286 0.3066 -0.0958 -0.0781 0.0147  38  ASP A C   
209  O  O   . ASP A 38  ? 0.3938 0.6067 0.3094 -0.0495 -0.1458 0.0114  38  ASP A O   
210  C  CB  . ASP A 38  ? 0.3620 0.4653 0.4223 -0.0869 -0.0707 0.1700  38  ASP A CB  
211  C  CG  . ASP A 38  ? 0.2432 0.5050 0.6304 0.0567  -0.0264 -0.0141 38  ASP A CG  
212  O  OD1 . ASP A 38  ? 0.2432 0.5462 0.5416 -0.0152 -0.1091 0.1333  38  ASP A OD1 
213  O  OD2 . ASP A 38  ? 0.3206 0.6110 0.6775 0.1386  -0.0297 -0.0461 38  ASP A OD2 
214  N  N   . ASP A 39  ? 0.2917 0.3450 0.4302 -0.0544 -0.1076 -0.1337 39  ASP A N   
215  C  CA  . ASP A 39  ? 0.3789 0.5361 0.4939 -0.2808 -0.1337 0.0252  39  ASP A CA  
216  C  C   . ASP A 39  ? 0.2342 0.7167 0.1260 -0.2333 -0.0036 0.1259  39  ASP A C   
217  O  O   . ASP A 39  ? 0.3532 0.8465 0.2082 -0.3985 -0.0024 0.2512  39  ASP A O   
218  C  CB  . ASP A 39  ? 0.6532 0.5096 0.3903 -0.1644 -0.1538 0.1487  39  ASP A CB  
219  N  N   . THR A 40  ? 0.4393 0.3780 0.2392 0.0046  -0.0218 0.0798  40  THR A N   
220  C  CA  . THR A 40  ? 0.2915 0.3148 0.4182 0.0247  -0.0641 0.0082  40  THR A CA  
221  C  C   . THR A 40  ? 0.2334 0.2858 0.4162 0.0340  -0.0741 0.0818  40  THR A C   
222  O  O   . THR A 40  ? 0.2217 0.2349 0.3482 0.0009  -0.0269 0.0407  40  THR A O   
223  C  CB  . THR A 40  ? 0.3356 0.3774 0.4192 0.0967  -0.0996 0.0445  40  THR A CB  
224  O  OG1 . THR A 40  ? 0.2590 0.4446 0.4710 0.1106  -0.0556 -0.0159 40  THR A OG1 
225  C  CG2 . THR A 40  ? 0.3819 0.5369 0.7203 0.0061  -0.2213 0.1179  40  THR A CG2 
226  N  N   . TRP A 41  ? 0.2762 0.3342 0.3809 -0.0058 -0.0708 0.1349  41  TRP A N   
227  C  CA  . TRP A 41  ? 0.2506 0.1701 0.3652 0.0772  -0.0079 0.0563  41  TRP A CA  
228  C  C   . TRP A 41  ? 0.2458 0.1504 0.4578 0.1583  -0.0461 0.0362  41  TRP A C   
229  O  O   . TRP A 41  ? 0.3450 0.3040 1.1702 0.2152  0.0445  0.2584  41  TRP A O   
230  C  CB  . TRP A 41  ? 0.2439 0.2060 0.3365 0.0090  -0.0585 0.0224  41  TRP A CB  
231  C  CG  . TRP A 41  ? 0.3179 0.2349 0.2846 0.0322  -0.0482 0.0836  41  TRP A CG  
232  C  CD1 . TRP A 41  ? 0.3488 0.2775 0.3153 0.2066  -0.1449 0.0719  41  TRP A CD1 
233  C  CD2 . TRP A 41  ? 0.2656 0.1634 0.2734 0.0222  0.0151  0.0079  41  TRP A CD2 
234  N  NE1 . TRP A 41  ? 0.5125 0.4324 0.2977 0.2556  -0.0622 0.0274  41  TRP A NE1 
235  C  CE2 . TRP A 41  ? 0.3028 0.3521 0.2313 0.0740  -0.0480 0.0549  41  TRP A CE2 
236  C  CE3 . TRP A 41  ? 0.1706 0.1852 0.2667 -0.0026 -0.0302 -0.0127 41  TRP A CE3 
237  C  CZ2 . TRP A 41  ? 0.2769 0.4354 0.2759 0.0420  0.0239  0.0386  41  TRP A CZ2 
238  C  CZ3 . TRP A 41  ? 0.1561 0.1926 0.2493 -0.0217 0.0059  0.0488  41  TRP A CZ3 
239  C  CH2 . TRP A 41  ? 0.2369 0.1799 0.3281 0.0094  0.0484  0.0968  41  TRP A CH2 
240  N  N   . GLU A 42  ? 0.2037 0.1732 0.3141 -0.0081 -0.0009 -0.0345 42  GLU A N   
241  C  CA  . GLU A 42  ? 0.1799 0.1813 0.3843 0.0438  -0.0013 -0.1181 42  GLU A CA  
242  C  C   . GLU A 42  ? 0.1943 0.1253 0.3608 -0.0010 0.0038  -0.0778 42  GLU A C   
243  O  O   . GLU A 42  ? 0.1631 0.1265 0.3827 -0.0069 0.0243  -0.0431 42  GLU A O   
244  C  CB  . GLU A 42  ? 0.2037 0.2988 0.3726 -0.0100 0.0170  -0.0438 42  GLU A CB  
245  N  N   . PRO A 43  ? 0.1666 0.1357 0.3280 0.0360  0.0050  -0.0356 43  PRO A N   
246  C  CA  . PRO A 43  ? 0.1666 0.2022 0.2747 0.0352  0.0349  -0.0601 43  PRO A CA  
247  C  C   . PRO A 43  ? 0.1700 0.2661 0.2899 -0.0978 0.0251  -0.0107 43  PRO A C   
248  O  O   . PRO A 43  ? 0.1536 0.3558 0.4105 -0.0674 0.0202  0.0925  43  PRO A O   
249  C  CB  . PRO A 43  ? 0.1784 0.2333 0.3655 0.0223  0.0255  -0.1362 43  PRO A CB  
250  C  CG  . PRO A 43  ? 0.3054 0.2060 0.4758 0.0735  -0.0604 -0.1544 43  PRO A CG  
251  C  CD  . PRO A 43  ? 0.2092 0.1772 0.3691 0.0557  -0.0179 -0.0880 43  PRO A CD  
252  N  N   . PHE A 44  ? 0.1413 0.1534 0.3013 -0.0658 0.0091  -0.0091 44  PHE A N   
253  C  CA  . PHE A 44  ? 0.1637 0.1390 0.2120 -0.0395 0.0789  -0.0023 44  PHE A CA  
254  C  C   . PHE A 44  ? 0.1802 0.1525 0.2088 -0.0443 0.0387  0.0227  44  PHE A C   
255  O  O   . PHE A 44  ? 0.2441 0.0880 0.2477 -0.0137 0.0304  0.0022  44  PHE A O   
256  C  CB  . PHE A 44  ? 0.1704 0.1340 0.2235 -0.0311 0.0611  -0.0045 44  PHE A CB  
257  C  CG  . PHE A 44  ? 0.2299 0.1489 0.2282 -0.0220 0.0248  0.0214  44  PHE A CG  
258  C  CD1 . PHE A 44  ? 0.2662 0.1160 0.3094 0.0030  0.0625  -0.0155 44  PHE A CD1 
259  C  CD2 . PHE A 44  ? 0.2111 0.1142 0.2431 0.0412  0.0355  -0.0159 44  PHE A CD2 
260  C  CE1 . PHE A 44  ? 0.2678 0.1103 0.2761 0.0163  0.0543  0.0005  44  PHE A CE1 
261  C  CE2 . PHE A 44  ? 0.2882 0.0717 0.2667 0.0160  0.0037  -0.0243 44  PHE A CE2 
262  C  CZ  . PHE A 44  ? 0.3618 0.0744 0.2072 0.0258  0.0234  -0.0052 44  PHE A CZ  
263  N  N   . ALA A 45  ? 0.1752 0.1105 0.2005 -0.0227 0.0353  0.0014  45  ALA A N   
264  C  CA  . ALA A 45  ? 0.1883 0.1497 0.1819 -0.0171 0.0347  0.0104  45  ALA A CA  
265  C  C   . ALA A 45  ? 0.1963 0.1099 0.1453 -0.0098 -0.0071 0.0044  45  ALA A C   
266  O  O   . ALA A 45  ? 0.2030 0.1262 0.1930 -0.0136 0.0438  0.0149  45  ALA A O   
267  C  CB  . ALA A 45  ? 0.2470 0.0632 0.2160 -0.0224 0.0370  0.0283  45  ALA A CB  
268  N  N   . SER A 46  ? 0.1699 0.1075 0.1586 -0.0166 0.0683  -0.0109 46  SER A N   
269  C  CA  . SER A 46  ? 0.1598 0.1044 0.1517 -0.0093 0.0454  0.0092  46  SER A CA  
270  C  C   . SER A 46  ? 0.1643 0.0994 0.1873 0.0036  0.0310  0.0129  46  SER A C   
271  O  O   . SER A 46  ? 0.1867 0.0867 0.1985 -0.0094 0.0427  0.0024  46  SER A O   
272  C  CB  . SER A 46  ? 0.1407 0.1039 0.1891 -0.0153 0.0448  -0.0049 46  SER A CB  
273  O  OG  . SER A 46  ? 0.1707 0.1187 0.1994 0.0135  0.0363  -0.0294 46  SER A OG  
274  N  N   . GLY A 47  ? 0.1589 0.1284 0.1734 0.0051  0.0365  0.0024  47  GLY A N   
275  C  CA  . GLY A 47  ? 0.1473 0.1419 0.1834 0.0150  0.0234  0.0307  47  GLY A CA  
276  C  C   . GLY A 47  ? 0.1523 0.1063 0.1854 -0.0003 0.0025  0.0050  47  GLY A C   
277  O  O   . GLY A 47  ? 0.1616 0.0891 0.2100 -0.0222 0.0215  0.0002  47  GLY A O   
278  N  N   . LYS A 48  ? 0.1512 0.1748 0.1823 -0.0315 0.0167  0.0273  48  LYS A N   
279  C  CA  . LYS A 48  ? 0.1527 0.1497 0.2465 -0.0305 0.0419  0.0151  48  LYS A CA  
280  C  C   . LYS A 48  ? 0.1595 0.1673 0.1853 -0.0501 0.0290  0.0008  48  LYS A C   
281  O  O   . LYS A 48  ? 0.1718 0.1651 0.2041 -0.0352 0.0305  -0.0159 48  LYS A O   
282  C  CB  . LYS A 48  ? 0.2031 0.1821 0.4015 -0.0056 0.0174  0.0444  48  LYS A CB  
283  C  CG  . LYS A 48  ? 0.3350 0.2113 0.4004 0.0119  0.0627  0.0081  48  LYS A CG  
284  C  CD  . LYS A 48  ? 0.5552 0.3668 0.6922 0.2677  0.0233  -0.0842 48  LYS A CD  
285  N  N   . THR A 49  ? 0.1515 0.1222 0.1576 -0.0198 -0.0074 0.0113  49  THR A N   
286  C  CA  . THR A 49  ? 0.1492 0.1629 0.1507 -0.0144 0.0060  -0.0047 49  THR A CA  
287  C  C   . THR A 49  ? 0.1721 0.1348 0.1656 -0.0201 0.0231  -0.0071 49  THR A C   
288  O  O   . THR A 49  ? 0.1911 0.1644 0.2225 -0.0172 0.0165  -0.0019 49  THR A O   
289  C  CB  . THR A 49  ? 0.1440 0.1462 0.1508 -0.0080 0.0041  0.0000  49  THR A CB  
290  O  OG1 . THR A 49  ? 0.1530 0.1415 0.2038 -0.0233 0.0076  0.0223  49  THR A OG1 
291  C  CG2 . THR A 49  ? 0.1696 0.1286 0.2039 -0.0035 0.0259  -0.0033 49  THR A CG2 
292  N  N   . SER A 50  ? 0.1918 0.1468 0.1843 -0.0276 -0.0105 -0.0077 50  SER A N   
293  C  CA  . SER A 50  ? 0.2049 0.2078 0.1792 -0.0415 -0.0003 -0.0356 50  SER A CA  
294  C  C   . SER A 50  ? 0.2338 0.1854 0.2137 -0.0397 0.0198  -0.0681 50  SER A C   
295  O  O   . SER A 50  ? 0.2008 0.2089 0.2158 -0.0180 -0.0067 -0.0517 50  SER A O   
296  C  CB  . SER A 50  ? 0.2506 0.2221 0.2161 -0.0727 -0.0227 -0.0270 50  SER A CB  
297  O  OG  . SER A 50  ? 0.2613 0.2328 0.2878 -0.0532 -0.0395 -0.0419 50  SER A OG  
298  N  N   . GLU A 51  ? 0.2340 0.2296 0.2079 -0.0338 0.0168  -0.0676 51  GLU A N   
299  C  CA  . GLU A 51  ? 0.2843 0.2501 0.2287 -0.0474 0.0245  -0.0036 51  GLU A CA  
300  C  C   . GLU A 51  ? 0.2298 0.2890 0.1947 -0.0462 -0.0313 -0.0090 51  GLU A C   
301  O  O   . GLU A 51  ? 0.2196 0.2478 0.2719 -0.0284 -0.0172 -0.0318 51  GLU A O   
302  C  CB  . GLU A 51  ? 0.3246 0.3984 0.3125 -0.1497 -0.0415 -0.0621 51  GLU A CB  
303  N  N   . SER A 52  ? 0.2284 0.2640 0.2050 -0.0335 -0.0199 -0.0329 52  SER A N   
304  C  CA  . SER A 52  ? 0.2324 0.2301 0.1892 -0.0525 -0.0151 -0.0067 52  SER A CA  
305  C  C   . SER A 52  ? 0.1612 0.2301 0.2003 -0.0378 0.0194  0.0036  52  SER A C   
306  O  O   . SER A 52  ? 0.1946 0.1877 0.2193 -0.0166 -0.0175 0.0160  52  SER A O   
307  C  CB  . SER A 52  ? 0.3271 0.2874 0.2594 -0.0425 -0.0904 0.0060  52  SER A CB  
308  O  OG  . SER A 52  ? 0.3869 0.2583 0.2785 0.0196  0.0092  0.0753  52  SER A OG  
309  N  N   . GLY A 53  ? 0.1758 0.1985 0.1895 -0.0259 -0.0100 -0.0283 53  GLY A N   
310  C  CA  . GLY A 53  ? 0.1854 0.1483 0.1932 0.0012  0.0056  -0.0102 53  GLY A CA  
311  C  C   . GLY A 53  ? 0.1585 0.1601 0.1715 -0.0042 -0.0195 0.0010  53  GLY A C   
312  O  O   . GLY A 53  ? 0.1906 0.1675 0.1503 -0.0054 -0.0021 -0.0083 53  GLY A O   
313  N  N   . GLU A 54  ? 0.2153 0.1670 0.1910 -0.0686 -0.0186 -0.0152 54  GLU A N   
314  C  CA  . GLU A 54  ? 0.2092 0.1323 0.1433 -0.0107 0.0091  0.0024  54  GLU A CA  
315  C  C   . GLU A 54  ? 0.2277 0.1281 0.1327 -0.0161 0.0278  0.0034  54  GLU A C   
316  O  O   . GLU A 54  ? 0.2374 0.1431 0.2082 -0.0497 0.0125  -0.0240 54  GLU A O   
317  C  CB  . GLU A 54  ? 0.2032 0.2244 0.2171 -0.0104 -0.0027 0.0710  54  GLU A CB  
318  C  CG  . GLU A 54  ? 0.2522 0.2942 0.2621 -0.0107 0.0051  0.0034  54  GLU A CG  
319  C  CD  . GLU A 54  ? 0.2764 0.5038 0.3673 0.0437  0.0028  0.0615  54  GLU A CD  
320  O  OE1 . GLU A 54  ? 0.2946 0.8586 0.4040 0.0622  -0.0638 0.1574  54  GLU A OE1 
321  O  OE2 . GLU A 54  ? 0.3846 0.4284 0.5750 0.1021  0.0008  0.0084  54  GLU A OE2 
322  N  N   . LEU A 55  ? 0.1676 0.1178 0.2035 0.0095  0.0390  -0.0349 55  LEU A N   
323  C  CA  . LEU A 55  ? 0.1863 0.0998 0.1679 -0.0259 0.0162  -0.0293 55  LEU A CA  
324  C  C   . LEU A 55  ? 0.1745 0.1426 0.2157 -0.0196 0.0205  -0.0039 55  LEU A C   
325  O  O   . LEU A 55  ? 0.1885 0.1312 0.2101 -0.0207 0.0036  0.0136  55  LEU A O   
326  C  CB  . LEU A 55  ? 0.1874 0.1330 0.2089 -0.0041 0.0244  -0.0078 55  LEU A CB  
327  C  CG  . LEU A 55  ? 0.1908 0.1262 0.1974 -0.0167 -0.0018 0.0106  55  LEU A CG  
328  C  CD1 . LEU A 55  ? 0.1696 0.1462 0.1973 -0.0231 0.0100  0.0158  55  LEU A CD1 
329  C  CD2 . LEU A 55  ? 0.1712 0.1624 0.2261 -0.0279 -0.0003 0.0319  55  LEU A CD2 
330  N  N   . HIS A 56  ? 0.2410 0.2106 0.1721 -0.0640 0.0117  0.0223  56  HIS A N   
331  C  CA  . HIS A 56  ? 0.2524 0.2638 0.2206 -0.0353 0.0206  0.0703  56  HIS A CA  
332  C  C   . HIS A 56  ? 0.2503 0.2325 0.2385 0.0242  0.0298  0.0447  56  HIS A C   
333  O  O   . HIS A 56  ? 0.2480 0.2599 0.2633 -0.0153 0.0421  0.0306  56  HIS A O   
334  C  CB  . HIS A 56  ? 0.2523 0.3252 0.2391 -0.0002 -0.0098 0.0875  56  HIS A CB  
335  C  CG  . HIS A 56  ? 0.2941 0.3476 0.2593 0.0482  0.0113  0.0392  56  HIS A CG  
336  N  ND1 . HIS A 56  ? 0.2603 0.4952 0.4432 -0.0033 -0.0525 0.0716  56  HIS A ND1 
337  C  CD2 . HIS A 56  ? 0.3251 0.2139 0.4152 -0.0374 0.0579  0.0543  56  HIS A CD2 
338  C  CE1 . HIS A 56  ? 0.1925 0.3799 0.4139 -0.0403 -0.0747 0.1066  56  HIS A CE1 
339  N  NE2 . HIS A 56  ? 0.2795 0.4374 0.5275 -0.0052 0.0354  -0.0008 56  HIS A NE2 
340  N  N   . GLY A 57  ? 0.2802 0.2445 0.2618 -0.0334 0.0211  0.0201  57  GLY A N   
341  C  CA  . GLY A 57  ? 0.2877 0.3005 0.2119 -0.1025 0.0194  0.0008  57  GLY A CA  
342  C  C   . GLY A 57  ? 0.2091 0.1714 0.2965 -0.0204 0.0550  0.0059  57  GLY A C   
343  O  O   . GLY A 57  ? 0.2273 0.2335 0.2924 -0.0455 0.0736  -0.0582 57  GLY A O   
344  N  N   . LEU A 58  ? 0.2012 0.1562 0.2894 -0.0076 0.0346  0.0003  58  LEU A N   
345  C  CA  . LEU A 58  ? 0.1892 0.1504 0.2575 0.0167  0.0632  0.0017  58  LEU A CA  
346  C  C   . LEU A 58  ? 0.1851 0.1141 0.2511 0.0004  0.0127  0.0185  58  LEU A C   
347  O  O   . LEU A 58  ? 0.2031 0.1481 0.2568 -0.0024 0.0296  0.0190  58  LEU A O   
348  C  CB  . LEU A 58  ? 0.1742 0.1153 0.2382 -0.0185 0.0144  -0.0010 58  LEU A CB  
349  C  CG  . LEU A 58  ? 0.1976 0.1000 0.2494 -0.0087 0.0334  0.0081  58  LEU A CG  
350  C  CD1 . LEU A 58  ? 0.1981 0.1302 0.2454 -0.0147 0.0272  0.0137  58  LEU A CD1 
351  C  CD2 . LEU A 58  ? 0.1904 0.2121 0.2752 0.0015  0.0351  0.0272  58  LEU A CD2 
352  N  N   . THR A 59  ? 0.1926 0.1349 0.2448 -0.0281 0.0327  0.0066  59  THR A N   
353  C  CA  . THR A 59  ? 0.1679 0.1408 0.2216 -0.0271 0.0445  -0.0288 59  THR A CA  
354  C  C   . THR A 59  ? 0.2059 0.1878 0.2098 -0.0172 0.0258  -0.0273 59  THR A C   
355  O  O   . THR A 59  ? 0.2557 0.1877 0.2371 -0.0517 0.0022  0.0320  59  THR A O   
356  C  CB  . THR A 59  ? 0.1654 0.1870 0.2365 -0.0385 0.0129  -0.0036 59  THR A CB  
357  O  OG1 . THR A 59  ? 0.1742 0.1876 0.2127 -0.0336 0.0252  -0.0164 59  THR A OG1 
358  C  CG2 . THR A 59  ? 0.1714 0.2183 0.2610 -0.0401 0.0427  -0.0068 59  THR A CG2 
359  N  N   . THR A 60  ? 0.2249 0.2381 0.2304 -0.0476 0.0069  0.0181  60  THR A N   
360  C  CA  . THR A 60  ? 0.1717 0.1833 0.2015 -0.0153 0.0200  -0.0014 60  THR A CA  
361  C  C   . THR A 60  ? 0.2391 0.2086 0.1989 -0.0171 0.0210  -0.0326 60  THR A C   
362  O  O   . THR A 60  ? 0.2018 0.1524 0.1965 -0.0142 0.0266  0.0095  60  THR A O   
363  C  CB  . THR A 60  ? 0.2039 0.1495 0.2220 0.0129  0.0186  0.0041  60  THR A CB  
364  O  OG1 . THR A 60  ? 0.2527 0.2329 0.2269 -0.0344 0.0402  -0.0253 60  THR A OG1 
365  C  CG2 . THR A 60  ? 0.3016 0.2011 0.2904 -0.0146 0.0993  -0.0449 60  THR A CG2 
366  N  N   . GLU A 61  ? 0.2480 0.1978 0.2462 -0.0516 0.0478  -0.0097 61  GLU A N   
367  C  CA  . GLU A 61  ? 0.2609 0.2094 0.2341 0.0104  0.0293  0.0161  61  GLU A CA  
368  C  C   . GLU A 61  ? 0.2569 0.1360 0.2837 0.0076  -0.0029 -0.0161 61  GLU A C   
369  O  O   . GLU A 61  ? 0.2480 0.1887 0.3187 -0.0152 -0.0025 -0.0353 61  GLU A O   
370  C  CB  . GLU A 61  ? 0.3172 0.1829 0.3124 0.0190  -0.0322 0.0008  61  GLU A CB  
371  C  CG  . GLU A 61  ? 0.3087 0.2737 0.3331 0.0288  0.0375  -0.0469 61  GLU A CG  
372  C  CD  . GLU A 61  ? 0.3348 0.4435 0.3173 -0.0083 0.0092  0.0068  61  GLU A CD  
373  O  OE1 . GLU A 61  ? 0.4152 0.5372 0.3470 -0.0171 -0.0337 0.1411  61  GLU A OE1 
374  O  OE2 . GLU A 61  ? 0.3279 0.5422 0.4587 0.0953  -0.0445 0.0093  61  GLU A OE2 
375  N  N   . GLU A 62  ? 0.2446 0.1073 0.2068 -0.0335 0.0008  0.0330  62  GLU A N   
376  C  CA  . GLU A 62  ? 0.2475 0.1420 0.3224 -0.0617 0.0684  0.0040  62  GLU A CA  
377  C  C   . GLU A 62  ? 0.2029 0.1533 0.3305 -0.0173 0.0159  -0.0499 62  GLU A C   
378  O  O   . GLU A 62  ? 0.2325 0.1557 0.2882 -0.0224 0.0040  -0.0025 62  GLU A O   
379  C  CB  . GLU A 62  ? 0.2980 0.2525 0.2711 -0.1024 0.0778  0.0336  62  GLU A CB  
380  C  CG  . GLU A 62  ? 0.3814 0.2404 0.3349 -0.0799 0.0672  0.0536  62  GLU A CG  
381  C  CD  . GLU A 62  ? 0.3935 0.3577 0.3403 -0.0609 0.0218  0.0745  62  GLU A CD  
382  O  OE1 . GLU A 62  ? 0.4787 0.3014 0.3438 -0.0159 -0.0155 0.0632  62  GLU A OE1 
383  O  OE2 . GLU A 62  ? 0.5917 0.4673 0.5213 -0.0738 -0.1346 0.1426  62  GLU A OE2 
384  N  N   . GLU A 63  ? 0.1985 0.1660 0.2016 -0.0365 0.0540  -0.0133 63  GLU A N   
385  C  CA  . GLU A 63  ? 0.1987 0.1426 0.2153 -0.0393 0.0575  -0.0155 63  GLU A CA  
386  C  C   . GLU A 63  ? 0.1715 0.1032 0.1982 -0.0282 0.0408  0.0105  63  GLU A C   
387  O  O   . GLU A 63  ? 0.1786 0.1080 0.1943 0.0010  0.0284  -0.0069 63  GLU A O   
388  C  CB  . GLU A 63  ? 0.2415 0.1673 0.2147 0.0064  0.0600  -0.0278 63  GLU A CB  
389  C  CG  . GLU A 63  ? 0.2656 0.1738 0.2794 0.0211  0.0501  -0.0304 63  GLU A CG  
390  C  CD  . GLU A 63  ? 0.2625 0.1808 0.3052 0.0402  0.0747  -0.0347 63  GLU A CD  
391  O  OE1 . GLU A 63  ? 0.2415 0.2407 0.4244 0.0169  0.1222  -0.0003 63  GLU A OE1 
392  O  OE2 . GLU A 63  ? 0.2414 0.2715 0.3698 -0.0087 0.0429  -0.0882 63  GLU A OE2 
393  N  N   . PHE A 64  ? 0.1801 0.0955 0.2031 -0.0280 0.0155  -0.0058 64  PHE A N   
394  C  CA  . PHE A 64  ? 0.1816 0.1205 0.1955 0.0043  0.0235  0.0139  64  PHE A CA  
395  C  C   . PHE A 64  ? 0.1904 0.1125 0.2051 0.0116  -0.0163 0.0318  64  PHE A C   
396  O  O   . PHE A 64  ? 0.1812 0.1491 0.2368 -0.0071 0.0173  0.0194  64  PHE A O   
397  C  CB  . PHE A 64  ? 0.1864 0.1302 0.1689 -0.0261 0.0236  -0.0251 64  PHE A CB  
398  C  CG  . PHE A 64  ? 0.1535 0.1271 0.1922 -0.0296 0.0314  -0.0416 64  PHE A CG  
399  C  CD1 . PHE A 64  ? 0.1533 0.1460 0.2397 -0.0260 0.0510  -0.0220 64  PHE A CD1 
400  C  CD2 . PHE A 64  ? 0.1696 0.2141 0.2780 -0.0097 0.0626  0.0667  64  PHE A CD2 
401  C  CE1 . PHE A 64  ? 0.2042 0.1829 0.2379 -0.0428 0.0400  -0.0308 64  PHE A CE1 
402  C  CE2 . PHE A 64  ? 0.1632 0.3387 0.2251 0.0057  0.0516  -0.0451 64  PHE A CE2 
403  C  CZ  . PHE A 64  ? 0.2059 0.1759 0.1623 -0.0334 0.0555  -0.0251 64  PHE A CZ  
404  N  N   . VAL A 65  ? 0.1927 0.0621 0.1808 0.0052  0.0355  -0.0326 65  VAL A N   
405  C  CA  . VAL A 65  ? 0.1641 0.0536 0.2057 -0.0019 0.0196  -0.0169 65  VAL A CA  
406  C  C   . VAL A 65  ? 0.1576 0.1093 0.1895 0.0000  0.0407  -0.0095 65  VAL A C   
407  O  O   . VAL A 65  ? 0.1794 0.1306 0.1753 -0.0126 0.0334  0.0070  65  VAL A O   
408  C  CB  . VAL A 65  ? 0.1694 0.1019 0.1797 -0.0375 0.0089  -0.0090 65  VAL A CB  
409  C  CG1 . VAL A 65  ? 0.1417 0.1591 0.2093 -0.0047 0.0531  -0.0097 65  VAL A CG1 
410  C  CG2 . VAL A 65  ? 0.1713 0.1441 0.2274 -0.0260 0.0251  0.0113  65  VAL A CG2 
411  N  N   . GLU A 66  ? 0.1952 0.0812 0.1793 -0.0223 0.0659  0.0432  66  GLU A N   
412  C  CA  . GLU A 66  ? 0.1426 0.1287 0.1952 -0.0424 0.0393  0.0045  66  GLU A CA  
413  C  C   . GLU A 66  ? 0.1428 0.1475 0.1840 -0.0390 0.0229  -0.0282 66  GLU A C   
414  O  O   . GLU A 66  ? 0.1629 0.1805 0.2172 -0.0114 0.0267  0.0009  66  GLU A O   
415  C  CB  . GLU A 66  ? 0.1990 0.1469 0.2334 -0.0477 0.0412  0.0139  66  GLU A CB  
416  C  CG  . GLU A 66  ? 0.2158 0.1782 0.2171 0.0169  0.0674  0.0141  66  GLU A CG  
417  C  CD  . GLU A 66  ? 0.3103 0.1641 0.2735 -0.0403 0.0551  0.0260  66  GLU A CD  
418  O  OE1 . GLU A 66  ? 0.2686 0.1318 0.2513 0.0228  0.0872  -0.0054 66  GLU A OE1 
419  O  OE2 . GLU A 66  ? 0.2553 0.1521 0.3237 -0.0525 0.0524  -0.0104 66  GLU A OE2 
420  N  N   . GLY A 67  ? 0.1472 0.1096 0.2060 0.0133  0.0342  0.0253  67  GLY A N   
421  C  CA  . GLY A 67  ? 0.1659 0.1343 0.1957 -0.0162 0.0158  0.0263  67  GLY A CA  
422  C  C   . GLY A 67  ? 0.1623 0.1213 0.1756 -0.0111 0.0199  -0.0046 67  GLY A C   
423  O  O   . GLY A 67  ? 0.1622 0.0919 0.2072 0.0049  0.0090  -0.0033 67  GLY A O   
424  N  N   . ILE A 68  ? 0.1505 0.1177 0.1774 -0.0168 0.0215  -0.0084 68  ILE A N   
425  C  CA  . ILE A 68  ? 0.1714 0.1232 0.1834 -0.0061 0.0365  -0.0034 68  ILE A CA  
426  C  C   . ILE A 68  ? 0.1386 0.1220 0.2128 0.0304  0.0498  0.0095  68  ILE A C   
427  O  O   . ILE A 68  ? 0.1372 0.1267 0.2440 -0.0002 0.0219  -0.0204 68  ILE A O   
428  C  CB  . ILE A 68  ? 0.1598 0.1122 0.1986 0.0009  0.0173  0.0054  68  ILE A CB  
429  C  CG1 . ILE A 68  ? 0.2658 0.1420 0.2296 0.0137  -0.0201 -0.0354 68  ILE A CG1 
430  C  CG2 . ILE A 68  ? 0.2277 0.2285 0.1625 0.0002  0.0158  0.0166  68  ILE A CG2 
431  C  CD1 . ILE A 68  ? 0.3526 0.1709 0.2398 0.0528  -0.0160 -0.0629 68  ILE A CD1 
432  N  N   . TYR A 69  ? 0.1389 0.1078 0.1987 0.0073  0.0326  -0.0072 69  TYR A N   
433  C  CA  . TYR A 69  ? 0.1386 0.1232 0.1664 -0.0094 0.0268  -0.0141 69  TYR A CA  
434  C  C   . TYR A 69  ? 0.1319 0.1459 0.1670 0.0090  0.0235  0.0027  69  TYR A C   
435  O  O   . TYR A 69  ? 0.1666 0.1167 0.1901 0.0019  0.0426  0.0213  69  TYR A O   
436  C  CB  . TYR A 69  ? 0.1528 0.1239 0.1877 -0.0298 0.0294  -0.0038 69  TYR A CB  
437  C  CG  . TYR A 69  ? 0.1403 0.0992 0.1549 -0.0198 0.0149  0.0009  69  TYR A CG  
438  C  CD1 . TYR A 69  ? 0.1627 0.1058 0.2155 0.0039  0.0630  -0.0089 69  TYR A CD1 
439  C  CD2 . TYR A 69  ? 0.1690 0.1495 0.1883 -0.0039 0.0379  -0.0005 69  TYR A CD2 
440  C  CE1 . TYR A 69  ? 0.1625 0.1048 0.1941 -0.0051 0.0471  -0.0187 69  TYR A CE1 
441  C  CE2 . TYR A 69  ? 0.1593 0.0966 0.1989 0.0190  0.0205  0.0046  69  TYR A CE2 
442  C  CZ  . TYR A 69  ? 0.1894 0.0951 0.1705 0.0021  0.0558  -0.0081 69  TYR A CZ  
443  O  OH  . TYR A 69  ? 0.2202 0.1138 0.1963 0.0057  0.0525  0.0053  69  TYR A OH  
444  N  N   . LYS A 70  ? 0.1083 0.1269 0.1929 0.0002  0.0297  0.0088  70  LYS A N   
445  C  CA  . LYS A 70  ? 0.1551 0.1449 0.1905 -0.0160 0.0316  0.0009  70  LYS A CA  
446  C  C   . LYS A 70  ? 0.1836 0.1381 0.1725 -0.0188 0.0392  0.0123  70  LYS A C   
447  O  O   . LYS A 70  ? 0.2001 0.1090 0.2235 -0.0208 0.0344  -0.0232 70  LYS A O   
448  C  CB  . LYS A 70  ? 0.1815 0.1424 0.2110 -0.0168 0.0021  0.0045  70  LYS A CB  
449  C  CG  . LYS A 70  ? 0.2580 0.1942 0.2685 0.0117  -0.0145 0.0703  70  LYS A CG  
450  C  CD  . LYS A 70  ? 0.3580 0.2118 0.3838 0.0468  -0.0739 0.0899  70  LYS A CD  
451  C  CE  . LYS A 70  ? 0.3564 0.5727 0.3707 0.0801  -0.0654 0.2224  70  LYS A CE  
452  N  N   . VAL A 71  ? 0.1639 0.1426 0.1730 -0.0226 0.0387  0.0014  71  VAL A N   
453  C  CA  . VAL A 71  ? 0.1662 0.1467 0.1781 -0.0298 0.0285  0.0005  71  VAL A CA  
454  C  C   . VAL A 71  ? 0.1648 0.1716 0.1636 -0.0315 0.0443  -0.0078 71  VAL A C   
455  O  O   . VAL A 71  ? 0.2205 0.1621 0.2149 -0.0163 0.0828  0.0211  71  VAL A O   
456  C  CB  . VAL A 71  ? 0.1788 0.1387 0.2120 -0.0336 0.0386  -0.0014 71  VAL A CB  
457  C  CG1 . VAL A 71  ? 0.2134 0.1778 0.1926 -0.0486 0.0150  0.0038  71  VAL A CG1 
458  C  CG2 . VAL A 71  ? 0.2128 0.1779 0.2474 -0.0021 -0.0012 0.0176  71  VAL A CG2 
459  N  N   . GLU A 72  ? 0.1733 0.1312 0.2133 -0.0224 0.0462  -0.0165 72  GLU A N   
460  C  CA  . GLU A 72  ? 0.1641 0.1698 0.1979 -0.0296 -0.0072 -0.0253 72  GLU A CA  
461  C  C   . GLU A 72  ? 0.1763 0.1292 0.1656 -0.0229 0.0027  0.0013  72  GLU A C   
462  O  O   . GLU A 72  ? 0.1902 0.1515 0.2016 -0.0456 0.0220  -0.0088 72  GLU A O   
463  C  CB  . GLU A 72  ? 0.2322 0.1587 0.2613 -0.0232 -0.0579 -0.0424 72  GLU A CB  
464  C  CG  . GLU A 72  ? 0.2311 0.3255 0.3304 -0.0113 -0.0379 0.0252  72  GLU A CG  
465  C  CD  . GLU A 72  ? 0.2668 0.1528 0.4216 0.0766  -0.1529 0.0089  72  GLU A CD  
466  O  OE1 . GLU A 72  ? 0.2561 0.2160 0.4415 -0.0827 -0.1176 0.0906  72  GLU A OE1 
467  O  OE2 . GLU A 72  ? 0.5309 0.1620 0.6898 0.0844  -0.1944 -0.0987 72  GLU A OE2 
468  N  N   . ILE A 73  ? 0.1798 0.1385 0.1447 -0.0312 -0.0022 0.0013  73  ILE A N   
469  C  CA  . ILE A 73  ? 0.1792 0.1474 0.1589 -0.0366 -0.0269 0.0111  73  ILE A CA  
470  C  C   . ILE A 73  ? 0.1785 0.1530 0.1410 -0.0296 -0.0047 0.0129  73  ILE A C   
471  O  O   . ILE A 73  ? 0.1889 0.1327 0.1597 -0.0164 0.0199  0.0162  73  ILE A O   
472  C  CB  . ILE A 73  ? 0.1790 0.1497 0.1766 -0.0316 -0.0086 0.0349  73  ILE A CB  
473  C  CG1 . ILE A 73  ? 0.1818 0.1617 0.1862 0.0124  0.0567  0.0415  73  ILE A CG1 
474  C  CG2 . ILE A 73  ? 0.1568 0.1203 0.1789 -0.0142 -0.0085 0.0429  73  ILE A CG2 
475  C  CD1 . ILE A 73  ? 0.2027 0.1793 0.2398 0.0200  0.0380  0.0254  73  ILE A CD1 
476  N  N   . ASP A 74  ? 0.1764 0.1411 0.1637 -0.0279 -0.0083 0.0248  74  ASP A N   
477  C  CA  . ASP A 74  ? 0.2015 0.1873 0.1749 -0.0172 0.0228  0.0651  74  ASP A CA  
478  C  C   . ASP A 74  ? 0.2085 0.1238 0.1843 -0.0271 0.0196  -0.0095 74  ASP A C   
479  O  O   . ASP A 74  ? 0.1773 0.1146 0.2095 -0.0087 -0.0126 0.0361  74  ASP A O   
480  C  CB  . ASP A 74  ? 0.1751 0.1105 0.2422 -0.0404 -0.0015 0.0399  74  ASP A CB  
481  C  CG  . ASP A 74  ? 0.2423 0.1627 0.2914 0.0054  -0.0234 0.0564  74  ASP A CG  
482  O  OD1 . ASP A 74  ? 0.2411 0.1769 0.3314 -0.0289 -0.0286 0.0428  74  ASP A OD1 
483  O  OD2 . ASP A 74  ? 0.2449 0.2160 0.4457 0.0297  0.0303  0.0659  74  ASP A OD2 
484  N  N   . THR A 75  ? 0.1645 0.1604 0.1903 -0.0275 0.0045  0.0327  75  THR A N   
485  C  CA  . THR A 75  ? 0.1419 0.1733 0.2121 -0.0182 -0.0054 0.0447  75  THR A CA  
486  C  C   . THR A 75  ? 0.1792 0.1462 0.1824 -0.0657 -0.0078 0.0069  75  THR A C   
487  O  O   . THR A 75  ? 0.1841 0.1029 0.2367 -0.0449 -0.0195 0.0004  75  THR A O   
488  C  CB  . THR A 75  ? 0.1698 0.1506 0.2042 -0.0165 -0.0099 0.0450  75  THR A CB  
489  O  OG1 . THR A 75  ? 0.1944 0.1387 0.1914 -0.0082 0.0094  0.0231  75  THR A OG1 
490  C  CG2 . THR A 75  ? 0.1664 0.1918 0.2159 -0.0188 0.0191  0.0848  75  THR A CG2 
491  N  N   . LYS A 76  ? 0.1997 0.1093 0.2264 -0.0516 -0.0349 0.0422  76  LYS A N   
492  C  CA  . LYS A 76  ? 0.2424 0.1246 0.1971 0.0009  -0.0267 0.0220  76  LYS A CA  
493  C  C   . LYS A 76  ? 0.2159 0.1029 0.2460 -0.0128 -0.0087 0.0263  76  LYS A C   
494  O  O   . LYS A 76  ? 0.2461 0.1102 0.2564 -0.0601 -0.0508 0.0284  76  LYS A O   
495  C  CB  . LYS A 76  ? 0.2658 0.1321 0.2388 0.0011  -0.0537 0.0030  76  LYS A CB  
496  C  CG  . LYS A 76  ? 0.3598 0.1576 0.2726 0.0452  -0.1101 -0.0173 76  LYS A CG  
497  C  CD  . LYS A 76  ? 0.4144 0.2799 0.3366 0.0197  -0.1553 -0.0703 76  LYS A CD  
498  C  CE  . LYS A 76  ? 0.5102 0.2501 0.2438 -0.0023 -0.1121 -0.0562 76  LYS A CE  
499  N  NZ  . LYS A 76  ? 0.5507 0.4413 0.4039 0.1205  -0.2383 -0.0034 76  LYS A NZ  
500  N  N   . SER A 77  ? 0.2085 0.1659 0.2560 0.0125  -0.0212 0.0325  77  SER A N   
501  C  CA  . SER A 77  ? 0.2428 0.1554 0.2606 0.0787  -0.0591 0.0164  77  SER A CA  
502  C  C   . SER A 77  ? 0.2471 0.1761 0.2813 0.0089  -0.0439 -0.0262 77  SER A C   
503  O  O   . SER A 77  ? 0.2842 0.1434 0.3283 0.0138  -0.0803 -0.0468 77  SER A O   
504  C  CB  . SER A 77  ? 0.2818 0.2508 0.2895 0.0346  -0.0537 0.0185  77  SER A CB  
505  O  OG  . SER A 77  ? 0.2615 0.1746 0.3940 0.0417  -0.0227 0.0238  77  SER A OG  
506  N  N   . TYR A 78  ? 0.2039 0.1419 0.2335 -0.0172 -0.0113 0.0099  78  TYR A N   
507  C  CA  . TYR A 78  ? 0.2159 0.1332 0.2240 0.0115  -0.0296 0.0398  78  TYR A CA  
508  C  C   . TYR A 78  ? 0.2488 0.1255 0.2337 -0.0282 -0.0477 0.0547  78  TYR A C   
509  O  O   . TYR A 78  ? 0.2284 0.1235 0.2904 -0.0045 -0.0384 0.0060  78  TYR A O   
510  C  CB  . TYR A 78  ? 0.1905 0.1588 0.1795 0.0246  -0.0147 0.0129  78  TYR A CB  
511  C  CG  . TYR A 78  ? 0.1838 0.1387 0.1980 0.0062  -0.0065 0.0299  78  TYR A CG  
512  C  CD1 . TYR A 78  ? 0.2066 0.1452 0.1735 0.0120  0.0506  0.0117  78  TYR A CD1 
513  C  CD2 . TYR A 78  ? 0.2124 0.1148 0.1637 0.0078  0.0193  -0.0051 78  TYR A CD2 
514  C  CE1 . TYR A 78  ? 0.1889 0.1554 0.1994 0.0355  0.0109  0.0372  78  TYR A CE1 
515  C  CE2 . TYR A 78  ? 0.1975 0.1626 0.1926 0.0064  0.0227  -0.0083 78  TYR A CE2 
516  C  CZ  . TYR A 78  ? 0.1745 0.1268 0.2049 0.0035  -0.0102 -0.0045 78  TYR A CZ  
517  O  OH  . TYR A 78  ? 0.1993 0.1680 0.2166 0.0016  -0.0140 0.0013  78  TYR A OH  
518  N  N   . TRP A 79  ? 0.2122 0.0992 0.2178 -0.0415 -0.0288 0.0152  79  TRP A N   
519  C  CA  . TRP A 79  ? 0.1849 0.1640 0.2167 -0.0234 -0.0569 0.0549  79  TRP A CA  
520  C  C   . TRP A 79  ? 0.2418 0.1314 0.2669 -0.0239 -0.0124 0.0312  79  TRP A C   
521  O  O   . TRP A 79  ? 0.2794 0.1569 0.3716 -0.0560 -0.0935 0.0563  79  TRP A O   
522  C  CB  . TRP A 79  ? 0.2007 0.1324 0.2225 -0.0457 -0.0094 0.0834  79  TRP A CB  
523  C  CG  . TRP A 79  ? 0.1634 0.1263 0.2224 -0.0232 0.0114  0.0094  79  TRP A CG  
524  C  CD1 . TRP A 79  ? 0.1865 0.1331 0.2357 -0.0689 -0.0711 0.0477  79  TRP A CD1 
525  C  CD2 . TRP A 79  ? 0.1657 0.1364 0.2005 -0.0399 -0.0103 0.0177  79  TRP A CD2 
526  N  NE1 . TRP A 79  ? 0.1816 0.1372 0.2080 -0.0383 0.0075  0.0561  79  TRP A NE1 
527  C  CE2 . TRP A 79  ? 0.1802 0.1554 0.1818 -0.0154 0.0164  0.0116  79  TRP A CE2 
528  C  CE3 . TRP A 79  ? 0.2232 0.1527 0.2502 -0.0724 -0.0292 0.0317  79  TRP A CE3 
529  C  CZ2 . TRP A 79  ? 0.1832 0.2190 0.2184 -0.0869 0.0082  0.0819  79  TRP A CZ2 
530  C  CZ3 . TRP A 79  ? 0.2230 0.2041 0.2403 -0.0675 -0.0113 -0.0237 79  TRP A CZ3 
531  C  CH2 . TRP A 79  ? 0.1987 0.1887 0.2280 -0.0384 0.0160  0.0093  79  TRP A CH2 
532  N  N   . LYS A 80  ? 0.2601 0.0669 0.3201 -0.0212 -0.0092 0.0359  80  LYS A N   
533  C  CA  . LYS A 80  ? 0.2898 0.0882 0.3675 -0.0044 -0.0518 0.0710  80  LYS A CA  
534  C  C   . LYS A 80  ? 0.3486 0.1524 0.4073 -0.1803 -0.0787 0.0287  80  LYS A C   
535  O  O   . LYS A 80  ? 0.2991 0.1197 0.5082 -0.0390 -0.0880 0.0317  80  LYS A O   
536  C  CB  . LYS A 80  ? 0.2839 0.1333 0.3335 0.0527  -0.0166 0.0192  80  LYS A CB  
537  C  CG  . LYS A 80  ? 0.4084 0.2836 0.3714 0.0029  -0.0527 0.0484  80  LYS A CG  
538  C  CD  . LYS A 80  ? 0.3068 0.2580 0.4269 -0.0275 -0.0166 0.0528  80  LYS A CD  
539  C  CE  . LYS A 80  ? 0.3996 0.2823 0.4916 0.0833  -0.0115 0.0224  80  LYS A CE  
540  N  NZ  . LYS A 80  ? 0.3361 0.3734 0.4500 0.0602  -0.1226 0.0744  80  LYS A NZ  
541  N  N   . ALA A 81  ? 0.3933 0.1625 0.3420 0.1004  -0.0208 -0.0522 81  ALA A N   
542  C  CA  . ALA A 81  ? 0.2451 0.1844 0.3397 0.0946  0.0051  -0.0816 81  ALA A CA  
543  C  C   . ALA A 81  ? 0.3397 0.1668 0.3616 0.0106  -0.0522 -0.0602 81  ALA A C   
544  O  O   . ALA A 81  ? 0.4188 0.1777 0.4674 -0.0205 -0.0709 -0.1006 81  ALA A O   
545  C  CB  . ALA A 81  ? 0.3414 0.3336 0.2984 0.0215  0.0115  -0.1341 81  ALA A CB  
546  N  N   . LEU A 82  ? 0.3153 0.1449 0.3384 0.0076  -0.0061 -0.0180 82  LEU A N   
547  C  CA  . LEU A 82  ? 0.3650 0.1643 0.4089 -0.0026 0.0288  -0.0030 82  LEU A CA  
548  C  C   . LEU A 82  ? 0.3302 0.1499 0.3686 0.0723  -0.0293 -0.0141 82  LEU A C   
549  O  O   . LEU A 82  ? 0.3738 0.2424 0.4990 -0.0266 -0.0878 0.1654  82  LEU A O   
550  C  CB  . LEU A 82  ? 0.2365 0.2259 0.3045 -0.0342 -0.0229 -0.0233 82  LEU A CB  
551  C  CG  . LEU A 82  ? 0.4062 0.1968 0.3595 -0.0101 -0.0444 -0.0173 82  LEU A CG  
552  C  CD1 . LEU A 82  ? 0.3060 0.2379 0.3399 0.0079  -0.0755 -0.0164 82  LEU A CD1 
553  C  CD2 . LEU A 82  ? 0.4145 0.1682 0.4193 0.0089  -0.0901 0.0012  82  LEU A CD2 
554  N  N   . GLY A 83  ? 0.3363 0.0896 0.4074 -0.0054 -0.0815 0.0288  83  GLY A N   
555  C  CA  . GLY A 83  ? 0.2761 0.0922 0.3443 0.0123  -0.0278 -0.0195 83  GLY A CA  
556  C  C   . GLY A 83  ? 0.3122 0.1831 0.2693 -0.0222 0.0625  -0.0183 83  GLY A C   
557  O  O   . GLY A 83  ? 0.4144 0.2770 0.3593 -0.0641 0.0019  0.1016  83  GLY A O   
558  N  N   . ILE A 84  ? 0.4252 0.1709 0.4513 0.0011  -0.1240 -0.0200 84  ILE A N   
559  C  CA  . ILE A 84  ? 0.3114 0.1898 0.2824 -0.0604 -0.0006 0.1479  84  ILE A CA  
560  C  C   . ILE A 84  ? 0.2787 0.3355 0.3499 -0.0523 -0.0052 0.0918  84  ILE A C   
561  O  O   . ILE A 84  ? 0.3090 0.2772 0.3205 -0.0972 0.0205  -0.0816 84  ILE A O   
562  C  CB  . ILE A 84  ? 0.3771 0.2422 0.2866 0.0570  0.0343  0.0579  84  ILE A CB  
563  C  CG1 . ILE A 84  ? 0.5006 0.2908 0.4591 0.1332  0.0573  -0.1730 84  ILE A CG1 
564  C  CG2 . ILE A 84  ? 0.4203 0.2275 0.2401 0.0266  0.1423  0.0943  84  ILE A CG2 
565  C  CD1 . ILE A 84  ? 0.5965 0.3890 0.7734 0.1316  0.1829  -0.1089 84  ILE A CD1 
566  N  N   . SER A 85  ? 0.2337 0.1559 0.3683 -0.0598 -0.0443 0.0689  85  SER A N   
567  C  CA  . SER A 85  ? 0.2948 0.1665 0.2856 -0.0657 -0.0722 0.0196  85  SER A CA  
568  C  C   . SER A 85  ? 0.3439 0.1621 0.2655 -0.0527 -0.0550 0.0003  85  SER A C   
569  O  O   . SER A 85  ? 0.3440 0.2431 0.4320 -0.0602 0.0303  0.1510  85  SER A O   
570  C  CB  . SER A 85  ? 0.3714 0.1370 0.3508 -0.0103 -0.0554 0.0885  85  SER A CB  
571  O  OG  . SER A 85  ? 0.4938 0.2205 0.4713 0.0157  -0.1334 0.0343  85  SER A OG  
572  N  N   . PRO A 86  ? 0.2720 0.2062 0.2739 -0.0432 -0.0703 0.0078  86  PRO A N   
573  C  CA  . PRO A 86  ? 0.2581 0.1454 0.2322 -0.0472 -0.0286 0.0533  86  PRO A CA  
574  C  C   . PRO A 86  ? 0.2403 0.1812 0.2576 -0.0738 -0.0314 0.0688  86  PRO A C   
575  O  O   . PRO A 86  ? 0.2914 0.1566 0.2942 -0.0565 -0.0657 0.0152  86  PRO A O   
576  C  CB  . PRO A 86  ? 0.2982 0.2267 0.2329 -0.1239 -0.1186 0.0612  86  PRO A CB  
577  C  CG  . PRO A 86  ? 0.3011 0.1682 0.3706 -0.1060 -0.0196 0.0254  86  PRO A CG  
578  C  CD  . PRO A 86  ? 0.3451 0.1685 0.3406 0.0107  -0.0409 0.0738  86  PRO A CD  
579  N  N   . PHE A 87  ? 0.1895 0.1660 0.2300 -0.0106 -0.0770 0.0611  87  PHE A N   
580  C  CA  . PHE A 87  ? 0.2172 0.2460 0.1907 -0.0525 -0.0964 0.0908  87  PHE A CA  
581  C  C   . PHE A 87  ? 0.2005 0.2136 0.2303 -0.0202 -0.0285 0.0244  87  PHE A C   
582  O  O   . PHE A 87  ? 0.2073 0.2088 0.2424 -0.0489 -0.0405 0.0578  87  PHE A O   
583  C  CB  . PHE A 87  ? 0.2115 0.2412 0.2451 -0.0876 -0.0571 0.0803  87  PHE A CB  
584  C  CG  . PHE A 87  ? 0.2098 0.2874 0.2654 -0.0862 -0.0001 0.0354  87  PHE A CG  
585  C  CD1 . PHE A 87  ? 0.2738 0.2843 0.2409 -0.0482 -0.0152 0.0190  87  PHE A CD1 
586  C  CD2 . PHE A 87  ? 0.2350 0.2692 0.2455 -0.0815 -0.0662 0.0164  87  PHE A CD2 
587  C  CE1 . PHE A 87  ? 0.2943 0.3560 0.2660 -0.0155 -0.0086 -0.0098 87  PHE A CE1 
588  C  CE2 . PHE A 87  ? 0.2299 0.2946 0.3058 -0.0039 -0.0561 0.0178  87  PHE A CE2 
589  C  CZ  . PHE A 87  ? 0.1890 0.3127 0.3154 -0.0037 -0.0426 -0.0163 87  PHE A CZ  
590  N  N   . HIS A 88  ? 0.1834 0.2315 0.1863 -0.0714 -0.0608 0.0137  88  HIS A N   
591  C  CA  . HIS A 88  ? 0.2003 0.1689 0.1764 -0.0610 -0.0592 0.0385  88  HIS A CA  
592  C  C   . HIS A 88  ? 0.1951 0.1621 0.1685 -0.0098 -0.0367 0.0327  88  HIS A C   
593  O  O   . HIS A 88  ? 0.2118 0.1673 0.1888 -0.0360 0.0024  0.0116  88  HIS A O   
594  C  CB  . HIS A 88  ? 0.1824 0.1402 0.2073 -0.0674 -0.0317 0.0201  88  HIS A CB  
595  C  CG  . HIS A 88  ? 0.1752 0.1482 0.2302 -0.0160 -0.0226 0.0359  88  HIS A CG  
596  N  ND1 . HIS A 88  ? 0.2009 0.1664 0.2155 -0.0545 -0.0051 0.0067  88  HIS A ND1 
597  C  CD2 . HIS A 88  ? 0.1671 0.1479 0.2945 -0.0289 -0.0022 0.0017  88  HIS A CD2 
598  C  CE1 . HIS A 88  ? 0.1671 0.2527 0.3434 -0.0511 -0.0043 -0.0696 88  HIS A CE1 
599  N  NE2 . HIS A 88  ? 0.1895 0.2167 0.2951 -0.0373 0.0154  -0.0211 88  HIS A NE2 
600  N  N   . GLU A 89  ? 0.2042 0.1496 0.1845 -0.0078 -0.0147 0.0452  89  GLU A N   
601  C  CA  . GLU A 89  ? 0.2506 0.1661 0.2023 -0.0466 0.0142  -0.0192 89  GLU A CA  
602  C  C   . GLU A 89  ? 0.2169 0.2474 0.1970 -0.0002 0.0663  -0.0183 89  GLU A C   
603  O  O   . GLU A 89  ? 0.3128 0.1963 0.2060 -0.0049 0.0462  0.0214  89  GLU A O   
604  C  CB  . GLU A 89  ? 0.2325 0.2378 0.2458 -0.0487 0.0054  0.0084  89  GLU A CB  
605  C  CG  . GLU A 89  ? 0.3018 0.2373 0.2450 -0.1020 0.0025  -0.0044 89  GLU A CG  
606  C  CD  . GLU A 89  ? 0.2918 0.2793 0.3041 0.0382  -0.0789 0.0075  89  GLU A CD  
607  O  OE1 . GLU A 89  ? 0.4096 0.3438 0.4163 0.0940  0.0272  0.0266  89  GLU A OE1 
608  O  OE2 . GLU A 89  ? 0.4343 0.4333 0.3854 -0.0997 -0.1941 0.1081  89  GLU A OE2 
609  N  N   . HIS A 90  ? 0.2540 0.1783 0.1603 -0.0534 0.0151  0.0088  90  HIS A N   
610  C  CA  . HIS A 90  ? 0.2343 0.1804 0.1925 -0.0538 0.0116  0.0161  90  HIS A CA  
611  C  C   . HIS A 90  ? 0.2933 0.1640 0.1973 -0.0470 0.0063  0.0022  90  HIS A C   
612  O  O   . HIS A 90  ? 0.4273 0.1615 0.2230 0.0091  0.0412  0.0479  90  HIS A O   
613  C  CB  . HIS A 90  ? 0.2934 0.1555 0.2854 -0.0882 0.0577  0.0074  90  HIS A CB  
614  C  CG  . HIS A 90  ? 0.4496 0.3154 0.3478 -0.2226 0.0152  0.1455  90  HIS A CG  
615  N  ND1 . HIS A 90  ? 0.4347 0.4533 0.4467 -0.2138 -0.1406 -0.0060 90  HIS A ND1 
616  C  CD2 . HIS A 90  ? 0.4671 0.5361 0.5046 -0.2073 -0.0356 0.1050  90  HIS A CD2 
617  C  CE1 . HIS A 90  ? 0.4267 0.4864 0.3595 -0.2155 -0.1294 0.0188  90  HIS A CE1 
618  N  NE2 . HIS A 90  ? 0.4710 0.4666 0.5741 -0.2121 -0.0414 0.1561  90  HIS A NE2 
619  N  N   . ALA A 91  ? 0.3162 0.1311 0.1946 0.0280  0.0234  -0.0114 91  ALA A N   
620  C  CA  . ALA A 91  ? 0.3208 0.1156 0.2196 0.0214  0.0790  0.0259  91  ALA A CA  
621  C  C   . ALA A 91  ? 0.4157 0.1350 0.1901 -0.0116 0.0960  0.0240  91  ALA A C   
622  O  O   . ALA A 91  ? 0.3377 0.2233 0.1968 0.0014  0.0957  -0.0003 91  ALA A O   
623  C  CB  . ALA A 91  ? 0.2882 0.1607 0.2583 0.0244  0.1001  0.0483  91  ALA A CB  
624  N  N   . GLU A 92  ? 0.4942 0.2005 0.2003 -0.0513 0.0766  0.0207  92  GLU A N   
625  C  CA  . GLU A 92  ? 0.4481 0.2474 0.2295 -0.0579 0.0530  0.0618  92  GLU A CA  
626  C  C   . GLU A 92  ? 0.4155 0.3503 0.2301 -0.0078 0.1298  0.1051  92  GLU A C   
627  O  O   . GLU A 92  ? 1.1995 0.2355 0.6707 0.2139  0.3032  -0.1195 92  GLU A O   
628  C  CB  . GLU A 92  ? 0.4760 0.3710 0.4429 -0.0041 -0.0721 0.1070  92  GLU A CB  
629  C  CG  . GLU A 92  ? 0.4401 0.4243 0.4368 -0.0381 -0.0314 -0.1075 92  GLU A CG  
630  C  CD  . GLU A 92  ? 0.4105 0.5039 0.3657 -0.0525 0.0044  -0.1394 92  GLU A CD  
631  O  OE1 . GLU A 92  ? 0.3723 0.3691 0.3446 0.0325  -0.1215 0.0143  92  GLU A OE1 
632  O  OE2 . GLU A 92  ? 0.3828 0.4812 0.7551 -0.1126 -0.1541 -0.0998 92  GLU A OE2 
633  N  N   . VAL A 93  ? 0.3400 0.1886 0.2214 -0.0861 0.1134  0.0118  93  VAL A N   
634  C  CA  . VAL A 93  ? 0.1881 0.2754 0.2085 -0.0355 0.0557  0.0231  93  VAL A CA  
635  C  C   . VAL A 93  ? 0.1906 0.1900 0.1502 0.0071  0.0412  0.0410  93  VAL A C   
636  O  O   . VAL A 93  ? 0.2324 0.1380 0.2299 -0.0530 0.0930  -0.0343 93  VAL A O   
637  C  CB  . VAL A 93  ? 0.2096 0.3791 0.2954 -0.0069 0.0542  -0.0105 93  VAL A CB  
638  C  CG1 . VAL A 93  ? 0.3252 0.2522 0.2990 0.0141  -0.0145 -0.0235 93  VAL A CG1 
639  C  CG2 . VAL A 93  ? 0.2298 0.5908 0.2657 -0.1209 -0.0166 -0.0343 93  VAL A CG2 
640  N  N   . VAL A 94  ? 0.1429 0.1571 0.1696 -0.0108 0.0090  0.0423  94  VAL A N   
641  C  CA  . VAL A 94  ? 0.1440 0.1461 0.1739 0.0079  0.0103  -0.0185 94  VAL A CA  
642  C  C   . VAL A 94  ? 0.1428 0.1844 0.1272 0.0073  -0.0075 -0.0030 94  VAL A C   
643  O  O   . VAL A 94  ? 0.1510 0.1541 0.1610 0.0303  0.0271  0.0138  94  VAL A O   
644  C  CB  . VAL A 94  ? 0.1694 0.1457 0.2211 0.0180  -0.0061 0.0197  94  VAL A CB  
645  C  CG1 . VAL A 94  ? 0.1708 0.1679 0.2183 0.0215  0.0062  -0.0164 94  VAL A CG1 
646  C  CG2 . VAL A 94  ? 0.2189 0.1625 0.2487 0.0254  -0.0379 0.0021  94  VAL A CG2 
647  N  N   . PHE A 95  ? 0.1291 0.1310 0.1708 0.0149  0.0099  0.0070  95  PHE A N   
648  C  CA  . PHE A 95  ? 0.1295 0.1616 0.1590 0.0076  -0.0065 0.0414  95  PHE A CA  
649  C  C   . PHE A 95  ? 0.1244 0.1137 0.1364 0.0093  0.0162  0.0013  95  PHE A C   
650  O  O   . PHE A 95  ? 0.1492 0.1483 0.1831 0.0300  0.0299  0.0153  95  PHE A O   
651  C  CB  . PHE A 95  ? 0.1379 0.1855 0.1625 -0.0084 0.0045  0.0440  95  PHE A CB  
652  C  CG  . PHE A 95  ? 0.1601 0.1809 0.2075 -0.0003 0.0030  0.0108  95  PHE A CG  
653  C  CD1 . PHE A 95  ? 0.1578 0.2023 0.2061 0.0236  -0.0346 0.0007  95  PHE A CD1 
654  C  CD2 . PHE A 95  ? 0.1463 0.2043 0.1823 0.0385  0.0444  -0.0145 95  PHE A CD2 
655  C  CE1 . PHE A 95  ? 0.2096 0.2613 0.2607 -0.0001 -0.0206 -0.0161 95  PHE A CE1 
656  C  CE2 . PHE A 95  ? 0.1448 0.2589 0.2441 -0.0283 0.0271  0.0007  95  PHE A CE2 
657  C  CZ  . PHE A 95  ? 0.1831 0.2627 0.2126 -0.0300 0.0391  -0.0602 95  PHE A CZ  
658  N  N   . THR A 96  ? 0.1673 0.1356 0.1670 0.0109  0.0556  -0.0071 96  THR A N   
659  C  CA  . THR A 96  ? 0.1676 0.1635 0.1489 0.0204  0.0624  -0.0096 96  THR A CA  
660  C  C   . THR A 96  ? 0.1628 0.1654 0.1789 -0.0074 0.0212  0.0232  96  THR A C   
661  O  O   . THR A 96  ? 0.1783 0.2078 0.2043 0.0370  0.0179  0.0278  96  THR A O   
662  C  CB  . THR A 96  ? 0.1631 0.1799 0.2038 0.0262  0.0420  0.0017  96  THR A CB  
663  O  OG1 . THR A 96  ? 0.2185 0.1424 0.2447 0.0086  0.0040  -0.0109 96  THR A OG1 
664  C  CG2 . THR A 96  ? 0.2322 0.1649 0.2541 -0.0121 0.0709  -0.0023 96  THR A CG2 
665  N  N   . ALA A 97  ? 0.1411 0.1444 0.1916 0.0205  0.0302  0.0373  97  ALA A N   
666  C  CA  . ALA A 97  ? 0.1637 0.1508 0.1888 0.0236  0.0276  0.0157  97  ALA A CA  
667  C  C   . ALA A 97  ? 0.1282 0.1521 0.2103 0.0268  0.0188  0.0138  97  ALA A C   
668  O  O   . ALA A 97  ? 0.1465 0.1416 0.2290 0.0213  0.0373  0.0361  97  ALA A O   
669  C  CB  . ALA A 97  ? 0.2018 0.1425 0.2077 0.0188  0.0494  0.0151  97  ALA A CB  
670  N  N   . ASN A 98  ? 0.1395 0.1371 0.1951 -0.0033 0.0216  0.0318  98  ASN A N   
671  C  CA  . ASN A 98  ? 0.1858 0.1713 0.1935 -0.0135 0.0355  0.0371  98  ASN A CA  
672  C  C   . ASN A 98  ? 0.1515 0.2118 0.1892 -0.0177 0.0087  0.0429  98  ASN A C   
673  O  O   . ASN A 98  ? 0.2352 0.1750 0.2564 -0.0018 0.0456  0.0192  98  ASN A O   
674  C  CB  . ASN A 98  ? 0.2177 0.1289 0.1569 -0.0329 -0.0050 0.0337  98  ASN A CB  
675  C  CG  . ASN A 98  ? 0.1715 0.1634 0.2047 -0.0297 -0.0014 -0.0100 98  ASN A CG  
676  O  OD1 . ASN A 98  ? 0.2910 0.2127 0.2526 0.0724  0.0522  0.0221  98  ASN A OD1 
677  N  ND2 . ASN A 98  ? 0.1594 0.0494 0.2324 -0.0152 0.0105  0.0121  98  ASN A ND2 
678  N  N   . ASP A 99  ? 0.2176 0.1420 0.2183 -0.0570 0.0584  0.0281  99  ASP A N   
679  C  CA  . ASP A 99  ? 0.1902 0.1396 0.2669 -0.0529 0.0251  0.0145  99  ASP A CA  
680  C  C   . ASP A 99  ? 0.2623 0.1660 0.3032 -0.0166 0.0542  0.0645  99  ASP A C   
681  O  O   . ASP A 99  ? 0.2770 0.1569 0.2793 0.0074  0.0003  -0.0012 99  ASP A O   
682  C  CB  . ASP A 99  ? 0.3146 0.2314 0.2639 -0.0192 0.0301  -0.0250 99  ASP A CB  
683  C  CG  . ASP A 99  ? 0.4540 0.3438 0.2811 -0.2093 0.1224  -0.0531 99  ASP A CG  
684  O  OD1 . ASP A 99  ? 0.2607 0.0691 0.4175 0.0061  -0.0968 0.0081  99  ASP A OD1 
685  O  OD2 . ASP A 99  ? 0.5918 0.3362 0.3401 -0.3209 0.1032  -0.1519 99  ASP A OD2 
686  N  N   . SER A 100 ? 0.3171 0.1764 0.2880 0.0063  0.0248  0.0749  100 SER A N   
687  C  CA  . SER A 100 ? 0.2738 0.1820 0.3645 0.0059  0.0212  0.0976  100 SER A CA  
688  C  C   . SER A 100 ? 0.3298 0.1464 0.4067 0.0175  -0.0264 0.0752  100 SER A C   
689  O  O   . SER A 100 ? 0.3209 0.3624 0.4681 0.0827  -0.0013 0.1061  100 SER A O   
690  C  CB  . SER A 100 ? 0.3445 0.3543 0.3947 0.1449  0.0065  0.1593  100 SER A CB  
691  O  OG  . SER A 100 ? 0.4127 0.5689 0.4858 0.2063  0.1159  -0.0329 100 SER A OG  
692  N  N   . GLY A 101 ? 0.3168 0.1612 0.3322 -0.0232 0.0124  0.0303  101 GLY A N   
693  C  CA  . GLY A 101 ? 0.3282 0.2309 0.3342 -0.0529 0.0095  0.0787  101 GLY A CA  
694  C  C   . GLY A 101 ? 0.2726 0.2134 0.2562 0.0061  0.0163  0.0270  101 GLY A C   
695  O  O   . GLY A 101 ? 0.2228 0.1828 0.2919 0.0119  0.0112  0.0489  101 GLY A O   
696  N  N   . PRO A 102 ? 0.2363 0.1597 0.2610 -0.0209 0.0438  0.1015  102 PRO A N   
697  C  CA  . PRO A 102 ? 0.2186 0.1310 0.2654 0.0102  -0.0204 0.0567  102 PRO A CA  
698  C  C   . PRO A 102 ? 0.2296 0.2235 0.2786 0.0214  0.0254  0.1055  102 PRO A C   
699  O  O   . PRO A 102 ? 0.2138 0.1970 0.3016 -0.0004 0.0199  0.0991  102 PRO A O   
700  C  CB  . PRO A 102 ? 0.2295 0.2040 0.2986 0.0285  0.0121  0.0528  102 PRO A CB  
701  C  CG  . PRO A 102 ? 0.4031 0.3428 0.2712 -0.0595 0.1145  0.0631  102 PRO A CG  
702  C  CD  . PRO A 102 ? 0.2845 0.2296 0.2370 -0.0743 0.0629  0.0714  102 PRO A CD  
703  N  N   . ARG A 103 ? 0.1914 0.1739 0.2248 0.0533  0.0290  0.0719  103 ARG A N   
704  C  CA  . ARG A 103 ? 0.2028 0.1683 0.2612 0.0239  0.0305  0.0337  103 ARG A CA  
705  C  C   . ARG A 103 ? 0.1991 0.1646 0.2402 0.0225  0.0703  0.0358  103 ARG A C   
706  O  O   . ARG A 103 ? 0.2100 0.1680 0.2507 -0.0087 0.0395  0.0672  103 ARG A O   
707  C  CB  . ARG A 103 ? 0.2067 0.1358 0.2729 -0.0001 0.0292  0.0381  103 ARG A CB  
708  C  CG  . ARG A 103 ? 0.1944 0.1940 0.2653 -0.0510 0.0084  0.0107  103 ARG A CG  
709  C  CD  . ARG A 103 ? 0.1696 0.2110 0.3083 -0.0113 0.0261  -0.0041 103 ARG A CD  
710  N  NE  . ARG A 103 ? 0.2485 0.2110 0.4433 0.0740  0.0892  0.0121  103 ARG A NE  
711  C  CZ  . ARG A 103 ? 0.4449 0.1552 0.3657 0.0474  0.0613  0.0035  103 ARG A CZ  
712  N  NH1 . ARG A 103 ? 0.3537 0.1466 0.4247 0.0598  0.0375  0.0443  103 ARG A NH1 
713  N  NH2 . ARG A 103 ? 0.4241 0.1721 0.4652 0.0710  -0.0026 -0.0478 103 ARG A NH2 
714  N  N   . ARG A 104 ? 0.2570 0.1095 0.2573 -0.0106 0.0064  0.0984  104 ARG A N   
715  C  CA  . ARG A 104 ? 0.2202 0.1652 0.1758 -0.0065 0.1023  0.0728  104 ARG A CA  
716  C  C   . ARG A 104 ? 0.1505 0.2307 0.1004 -0.0084 0.0276  0.0501  104 ARG A C   
717  O  O   . ARG A 104 ? 0.2251 0.1084 0.1997 0.0365  0.0494  0.0255  104 ARG A O   
718  C  CB  . ARG A 104 ? 0.2786 0.1675 0.2659 -0.0057 -0.0326 0.0838  104 ARG A CB  
719  N  N   . TYR A 105 ? 0.1793 0.0898 0.2119 0.0154  0.0370  0.0349  105 TYR A N   
720  C  CA  . TYR A 105 ? 0.1695 0.1554 0.1940 -0.0072 0.0172  -0.0065 105 TYR A CA  
721  C  C   . TYR A 105 ? 0.1425 0.1627 0.2028 0.0077  0.0502  -0.0316 105 TYR A C   
722  O  O   . TYR A 105 ? 0.1964 0.1274 0.2250 -0.0128 0.0851  0.0213  105 TYR A O   
723  C  CB  . TYR A 105 ? 0.1516 0.1780 0.2097 0.0279  0.0455  0.0387  105 TYR A CB  
724  C  CG  . TYR A 105 ? 0.1418 0.1745 0.1887 -0.0206 0.0064  0.0272  105 TYR A CG  
725  C  CD1 . TYR A 105 ? 0.1788 0.1636 0.1756 0.0173  0.0630  0.0085  105 TYR A CD1 
726  C  CD2 . TYR A 105 ? 0.1788 0.1469 0.1923 -0.0464 0.0147  0.0327  105 TYR A CD2 
727  C  CE1 . TYR A 105 ? 0.1903 0.1585 0.2204 0.0120  0.0808  0.0685  105 TYR A CE1 
728  C  CE2 . TYR A 105 ? 0.1727 0.1544 0.1759 0.0106  0.0436  -0.0145 105 TYR A CE2 
729  C  CZ  . TYR A 105 ? 0.1589 0.1226 0.2021 0.0050  0.0003  0.0276  105 TYR A CZ  
730  O  OH  . TYR A 105 ? 0.1668 0.1362 0.2547 0.0116  0.0128  -0.0066 105 TYR A OH  
731  N  N   . THR A 106 ? 0.1570 0.1042 0.2072 0.0128  0.0252  0.0190  106 THR A N   
732  C  CA  . THR A 106 ? 0.2001 0.1151 0.1664 0.0093  -0.0026 -0.0074 106 THR A CA  
733  C  C   . THR A 106 ? 0.1606 0.1380 0.1719 0.0006  0.0213  -0.0051 106 THR A C   
734  O  O   . THR A 106 ? 0.2194 0.1006 0.1819 0.0324  0.0524  0.0330  106 THR A O   
735  C  CB  . THR A 106 ? 0.2086 0.1453 0.1788 -0.0105 0.0301  0.0350  106 THR A CB  
736  O  OG1 . THR A 106 ? 0.2644 0.3078 0.1907 0.0021  -0.0049 0.0339  106 THR A OG1 
737  C  CG2 . THR A 106 ? 0.2090 0.1705 0.2810 -0.0440 0.0290  -0.0084 106 THR A CG2 
738  N  N   . ILE A 107 ? 0.1981 0.1083 0.1673 0.0222  0.0444  0.0182  107 ILE A N   
739  C  CA  . ILE A 107 ? 0.1997 0.1120 0.1705 -0.0090 0.0134  -0.0033 107 ILE A CA  
740  C  C   . ILE A 107 ? 0.2247 0.1162 0.1864 0.0053  0.0317  0.0187  107 ILE A C   
741  O  O   . ILE A 107 ? 0.2673 0.1204 0.1857 0.0054  0.0422  0.0168  107 ILE A O   
742  C  CB  . ILE A 107 ? 0.2212 0.1493 0.1852 0.0096  -0.0131 -0.0179 107 ILE A CB  
743  C  CG1 . ILE A 107 ? 0.2153 0.1944 0.2570 0.0122  -0.0178 -0.0113 107 ILE A CG1 
744  C  CG2 . ILE A 107 ? 0.2733 0.1593 0.2485 0.0080  0.0017  0.0250  107 ILE A CG2 
745  C  CD1 . ILE A 107 ? 0.2330 0.1656 0.3109 0.0157  0.0134  0.0173  107 ILE A CD1 
746  N  N   . ALA A 108 ? 0.2069 0.1042 0.1643 -0.0294 0.0154  0.0282  108 ALA A N   
747  C  CA  . ALA A 108 ? 0.2633 0.1010 0.1451 -0.0609 0.0116  0.0057  108 ALA A CA  
748  C  C   . ALA A 108 ? 0.2935 0.1432 0.1337 -0.0208 0.0231  0.0012  108 ALA A C   
749  O  O   . ALA A 108 ? 0.3709 0.1737 0.1361 -0.0318 0.0223  0.0227  108 ALA A O   
750  C  CB  . ALA A 108 ? 0.2486 0.2424 0.2272 -0.1169 -0.0017 -0.0106 108 ALA A CB  
751  N  N   . ALA A 109 ? 0.2146 0.1237 0.1573 -0.0570 -0.0123 -0.0272 109 ALA A N   
752  C  CA  . ALA A 109 ? 0.1894 0.1518 0.1690 -0.0548 -0.0183 -0.0154 109 ALA A CA  
753  C  C   . ALA A 109 ? 0.1755 0.1368 0.1566 -0.0251 0.0066  -0.0081 109 ALA A C   
754  O  O   . ALA A 109 ? 0.2575 0.1400 0.1566 -0.0594 0.0197  0.0055  109 ALA A O   
755  C  CB  . ALA A 109 ? 0.2160 0.1510 0.1996 -0.0725 0.0221  -0.0274 109 ALA A CB  
756  N  N   . LEU A 110 ? 0.1393 0.1236 0.1580 -0.0355 -0.0079 0.0011  110 LEU A N   
757  C  CA  . LEU A 110 ? 0.1650 0.1196 0.1440 -0.0469 -0.0133 0.0128  110 LEU A CA  
758  C  C   . LEU A 110 ? 0.1613 0.1102 0.1348 -0.0425 0.0027  0.0059  110 LEU A C   
759  O  O   . LEU A 110 ? 0.2033 0.1456 0.1530 -0.0176 -0.0116 0.0227  110 LEU A O   
760  C  CB  . LEU A 110 ? 0.1865 0.1588 0.1925 -0.0360 0.0051  0.0491  110 LEU A CB  
761  C  CG  . LEU A 110 ? 0.1923 0.1391 0.1931 -0.0465 -0.0035 0.0352  110 LEU A CG  
762  C  CD1 . LEU A 110 ? 0.1418 0.1716 0.2071 -0.0507 -0.0105 0.0497  110 LEU A CD1 
763  C  CD2 . LEU A 110 ? 0.2037 0.3510 0.2796 0.0005  0.0560  0.0159  110 LEU A CD2 
764  N  N   . LEU A 111 ? 0.1388 0.0927 0.1515 -0.0505 -0.0329 0.0171  111 LEU A N   
765  C  CA  . LEU A 111 ? 0.1244 0.1397 0.1370 -0.0435 -0.0298 0.0355  111 LEU A CA  
766  C  C   . LEU A 111 ? 0.1620 0.1249 0.1338 -0.0515 -0.0432 0.0393  111 LEU A C   
767  O  O   . LEU A 111 ? 0.1523 0.1045 0.1519 -0.0349 -0.0281 0.0216  111 LEU A O   
768  C  CB  . LEU A 111 ? 0.1484 0.1344 0.1483 -0.0457 -0.0233 0.0349  111 LEU A CB  
769  C  CG  . LEU A 111 ? 0.1448 0.1481 0.1322 -0.0243 -0.0198 0.0411  111 LEU A CG  
770  C  CD1 . LEU A 111 ? 0.2015 0.1753 0.1915 -0.0106 0.0306  0.0351  111 LEU A CD1 
771  C  CD2 . LEU A 111 ? 0.1549 0.1862 0.1873 -0.0656 -0.0104 0.0051  111 LEU A CD2 
772  N  N   . SER A 112 ? 0.1514 0.1130 0.1547 -0.0637 -0.0388 0.0242  112 SER A N   
773  C  CA  . SER A 112 ? 0.1407 0.1563 0.1249 -0.0226 -0.0066 0.0402  112 SER A CA  
774  C  C   . SER A 112 ? 0.1570 0.1435 0.1757 -0.0305 -0.0259 0.0537  112 SER A C   
775  O  O   . SER A 112 ? 0.1406 0.1476 0.1990 -0.0382 -0.0229 0.0374  112 SER A O   
776  C  CB  . SER A 112 ? 0.1087 0.1660 0.1762 -0.0288 -0.0085 0.0128  112 SER A CB  
777  O  OG  . SER A 112 ? 0.1536 0.2369 0.2157 -0.0231 -0.0173 0.0352  112 SER A OG  
778  N  N   . PRO A 113 ? 0.1365 0.1536 0.1859 -0.0613 -0.0351 0.0398  113 PRO A N   
779  C  CA  . PRO A 113 ? 0.1853 0.1477 0.1826 -0.0265 -0.0314 0.0595  113 PRO A CA  
780  C  C   . PRO A 113 ? 0.1836 0.1713 0.1510 -0.0054 -0.0122 0.0850  113 PRO A C   
781  O  O   . PRO A 113 ? 0.1777 0.1714 0.2029 -0.0149 -0.0238 0.0434  113 PRO A O   
782  C  CB  . PRO A 113 ? 0.2069 0.1752 0.2488 -0.0395 -0.0686 0.0833  113 PRO A CB  
783  C  CG  . PRO A 113 ? 0.2306 0.1360 0.2121 -0.0932 -0.0320 0.0641  113 PRO A CG  
784  C  CD  . PRO A 113 ? 0.1708 0.1535 0.2140 -0.0591 -0.0518 0.0215  113 PRO A CD  
785  N  N   . TYR A 114 ? 0.1564 0.1447 0.1751 -0.0265 -0.0007 0.0372  114 TYR A N   
786  C  CA  . TYR A 114 ? 0.1878 0.1680 0.1694 -0.0393 -0.0113 0.0505  114 TYR A CA  
787  C  C   . TYR A 114 ? 0.1649 0.1713 0.1504 -0.0140 -0.0465 0.0129  114 TYR A C   
788  O  O   . TYR A 114 ? 0.2383 0.2306 0.1471 -0.0499 -0.0281 0.0196  114 TYR A O   
789  C  CB  . TYR A 114 ? 0.1886 0.1947 0.1830 -0.0556 -0.0085 0.0465  114 TYR A CB  
790  C  CG  . TYR A 114 ? 0.1684 0.1811 0.1820 -0.0628 0.0163  0.0268  114 TYR A CG  
791  C  CD1 . TYR A 114 ? 0.3278 0.1890 0.1827 -0.0332 -0.0970 0.0336  114 TYR A CD1 
792  C  CD2 . TYR A 114 ? 0.1857 0.1874 0.2356 -0.0742 -0.0281 0.0718  114 TYR A CD2 
793  C  CE1 . TYR A 114 ? 0.5367 0.2134 0.2223 0.0109  -0.1212 0.0576  114 TYR A CE1 
794  C  CE2 . TYR A 114 ? 0.3007 0.2401 0.1700 -0.0368 -0.0404 0.0519  114 TYR A CE2 
795  C  CZ  . TYR A 114 ? 0.3584 0.1924 0.2339 0.0623  -0.0836 0.0643  114 TYR A CZ  
796  O  OH  . TYR A 114 ? 0.8078 0.3391 0.5265 0.1863  -0.0875 0.1524  114 TYR A OH  
797  N  N   . SER A 115 ? 0.2034 0.1383 0.1769 -0.0529 -0.0571 0.0318  115 SER A N   
798  C  CA  . SER A 115 ? 0.1742 0.1442 0.1695 -0.0797 -0.0521 0.0022  115 SER A CA  
799  C  C   . SER A 115 ? 0.2181 0.1331 0.1588 -0.0790 -0.0071 0.0044  115 SER A C   
800  O  O   . SER A 115 ? 0.2549 0.1328 0.1730 -0.0347 -0.0684 0.0210  115 SER A O   
801  C  CB  . SER A 115 ? 0.2046 0.1907 0.2211 -0.0020 -0.0187 -0.0095 115 SER A CB  
802  O  OG  . SER A 115 ? 0.1881 0.2345 0.2863 0.0117  -0.0283 -0.0126 115 SER A OG  
803  N  N   . TYR A 116 ? 0.1938 0.1074 0.1415 -0.0280 -0.0445 0.0155  116 TYR A N   
804  C  CA  . TYR A 116 ? 0.2032 0.0999 0.1428 -0.0303 -0.0010 0.0141  116 TYR A CA  
805  C  C   . TYR A 116 ? 0.1616 0.1161 0.1196 -0.0237 -0.0506 0.0019  116 TYR A C   
806  O  O   . TYR A 116 ? 0.1645 0.1582 0.1254 -0.0299 -0.0273 0.0135  116 TYR A O   
807  C  CB  . TYR A 116 ? 0.2018 0.1299 0.1858 0.0109  -0.0129 0.0472  116 TYR A CB  
808  C  CG  . TYR A 116 ? 0.1796 0.1867 0.1939 0.0133  -0.0030 -0.0011 116 TYR A CG  
809  C  CD1 . TYR A 116 ? 0.1880 0.2034 0.2485 0.0056  0.0081  -0.0141 116 TYR A CD1 
810  C  CD2 . TYR A 116 ? 0.1806 0.2655 0.2397 0.0386  -0.0104 -0.0480 116 TYR A CD2 
811  C  CE1 . TYR A 116 ? 0.2125 0.1971 0.2798 -0.0129 -0.0057 -0.0726 116 TYR A CE1 
812  C  CE2 . TYR A 116 ? 0.2061 0.2588 0.2711 0.0093  0.0172  -0.0209 116 TYR A CE2 
813  C  CZ  . TYR A 116 ? 0.1583 0.2391 0.2810 -0.0783 0.0238  0.0439  116 TYR A CZ  
814  O  OH  . TYR A 116 ? 0.1961 0.3045 0.3154 -0.0378 -0.0271 0.0615  116 TYR A OH  
815  N  N   . SER A 117 ? 0.1798 0.0993 0.1376 -0.0146 -0.0296 0.0103  117 SER A N   
816  C  CA  A SER A 117 ? 0.2103 0.1196 0.1389 0.0081  -0.0220 0.0379  117 SER A CA  
817  C  CA  B SER A 117 ? 0.2192 0.1216 0.1401 0.0060  -0.0141 0.0367  117 SER A CA  
818  C  CA  C SER A 117 ? 0.2133 0.1213 0.1385 0.0100  -0.0121 0.0346  117 SER A CA  
819  C  C   . SER A 117 ? 0.2288 0.1621 0.1544 -0.0213 0.0120  0.0160  117 SER A C   
820  O  O   . SER A 117 ? 0.3194 0.1078 0.1604 0.0282  0.0182  0.0567  117 SER A O   
821  C  CB  A SER A 117 ? 0.2054 0.2546 0.2260 0.0049  0.0083  -0.0170 117 SER A CB  
822  C  CB  B SER A 117 ? 0.2098 0.2467 0.2400 0.0070  0.0050  0.0048  117 SER A CB  
823  C  CB  C SER A 117 ? 0.2032 0.1707 0.2134 0.0434  0.0167  0.0124  117 SER A CB  
824  O  OG  A SER A 117 ? 0.2151 0.2592 0.3187 0.0239  -0.0652 -0.0698 117 SER A OG  
825  O  OG  B SER A 117 ? 0.2768 0.2933 0.2314 0.0343  0.0192  0.0348  117 SER A OG  
826  O  OG  C SER A 117 ? 0.2939 0.1833 0.1407 0.0977  0.0491  0.0409  117 SER A OG  
827  N  N   . THR A 118 ? 0.2932 0.1133 0.1710 -0.0212 -0.0086 0.0094  118 THR A N   
828  C  CA  . THR A 118 ? 0.2711 0.1269 0.1556 0.0102  -0.0078 0.0075  118 THR A CA  
829  C  C   . THR A 118 ? 0.3200 0.1361 0.1407 0.0334  0.0350  0.0181  118 THR A C   
830  O  O   . THR A 118 ? 0.3490 0.1509 0.1571 0.0202  0.0198  0.0128  118 THR A O   
831  C  CB  . THR A 118 ? 0.2657 0.1673 0.2255 0.0048  0.0054  0.0058  118 THR A CB  
832  O  OG1 . THR A 118 ? 0.2580 0.2135 0.2708 0.0133  0.0348  0.0083  118 THR A OG1 
833  C  CG2 . THR A 118 ? 0.2740 0.2307 0.1996 -0.0560 -0.0098 0.0005  118 THR A CG2 
834  N  N   . THR A 119 ? 0.2826 0.0850 0.1513 -0.0251 0.0262  0.0267  119 THR A N   
835  C  CA  . THR A 119 ? 0.1930 0.1683 0.1704 0.0174  0.0372  0.0581  119 THR A CA  
836  C  C   . THR A 119 ? 0.1589 0.1344 0.1625 -0.0117 0.0120  0.0266  119 THR A C   
837  O  O   . THR A 119 ? 0.2558 0.1135 0.1931 -0.0051 0.0455  0.0381  119 THR A O   
838  C  CB  . THR A 119 ? 0.2132 0.2738 0.2945 -0.0571 0.0748  0.0708  119 THR A CB  
839  O  OG1 . THR A 119 ? 0.2682 0.3658 0.3246 -0.0728 0.0896  0.0241  119 THR A OG1 
840  C  CG2 . THR A 119 ? 0.1371 0.4172 0.3551 -0.0448 0.0470  0.1249  119 THR A CG2 
841  N  N   . ALA A 120 ? 0.1963 0.1409 0.1815 -0.0215 0.0389  0.0212  120 ALA A N   
842  C  CA  . ALA A 120 ? 0.1399 0.1379 0.2054 0.0319  0.0390  0.0488  120 ALA A CA  
843  C  C   . ALA A 120 ? 0.1593 0.1394 0.2001 0.0033  0.0111  0.0432  120 ALA A C   
844  O  O   . ALA A 120 ? 0.2250 0.1363 0.1852 0.0407  0.0309  0.0352  120 ALA A O   
845  C  CB  . ALA A 120 ? 0.1548 0.1667 0.2850 0.0113  -0.0134 0.1055  120 ALA A CB  
846  N  N   . VAL A 121 ? 0.1312 0.1298 0.2018 0.0077  0.0090  0.0583  121 VAL A N   
847  C  CA  . VAL A 121 ? 0.1172 0.1891 0.1597 0.0163  0.0105  0.0344  121 VAL A CA  
848  C  C   . VAL A 121 ? 0.1637 0.1656 0.1569 -0.0014 0.0248  0.0235  121 VAL A C   
849  O  O   . VAL A 121 ? 0.2143 0.1455 0.2242 0.0520  0.0834  0.0724  121 VAL A O   
850  C  CB  . VAL A 121 ? 0.2124 0.2120 0.1640 0.0023  -0.0007 0.0093  121 VAL A CB  
851  C  CG1 . VAL A 121 ? 0.2556 0.2737 0.2270 0.0049  -0.0590 -0.0037 121 VAL A CG1 
852  C  CG2 . VAL A 121 ? 0.2718 0.3532 0.2843 -0.0738 0.0137  0.0035  121 VAL A CG2 
853  N  N   . VAL A 122 ? 0.1477 0.1647 0.1880 -0.0081 0.0416  0.0359  122 VAL A N   
854  C  CA  . VAL A 122 ? 0.1677 0.1818 0.1644 -0.0054 0.0445  0.0367  122 VAL A CA  
855  C  C   . VAL A 122 ? 0.1560 0.1756 0.2075 0.0198  0.0573  0.0290  122 VAL A C   
856  O  O   . VAL A 122 ? 0.1860 0.1796 0.2687 0.0396  0.0543  0.0468  122 VAL A O   
857  C  CB  . VAL A 122 ? 0.1541 0.1964 0.2302 0.0061  0.0452  0.0433  122 VAL A CB  
858  C  CG1 . VAL A 122 ? 0.1573 0.1854 0.3032 -0.0045 0.0182  0.0800  122 VAL A CG1 
859  C  CG2 . VAL A 122 ? 0.1974 0.2346 0.1926 -0.0181 0.0370  0.0092  122 VAL A CG2 
860  N  N   . THR A 123 ? 0.1729 0.1413 0.1931 0.0005  -0.0079 0.0548  123 THR A N   
861  C  CA  . THR A 123 ? 0.1768 0.2201 0.2167 0.0906  0.0027  0.0716  123 THR A CA  
862  C  C   . THR A 123 ? 0.1711 0.2876 0.3436 0.0166  0.0256  0.0903  123 THR A C   
863  O  O   . THR A 123 ? 0.2272 0.1566 0.2615 0.0009  0.0075  0.1056  123 THR A O   
864  C  CB  . THR A 123 ? 0.3725 0.3046 0.2207 0.0082  -0.0269 0.0877  123 THR A CB  
865  O  OG1 . THR A 123 ? 0.4399 0.4407 0.3550 0.0940  -0.0681 -0.0554 123 THR A OG1 
866  C  CG2 . THR A 123 ? 0.3951 0.4394 0.3302 -0.0635 -0.0199 0.0886  123 THR A CG2 
867  N  N   . ASN A 124 ? 0.3212 0.2695 0.4256 0.0362  0.0445  0.1286  124 ASN A N   
868  C  CA  . ASN A 124 ? 0.2948 0.3163 0.4046 0.0274  0.1116  0.0591  124 ASN A CA  
869  C  C   . ASN A 124 ? 0.6516 0.5398 0.3815 -0.1807 0.2038  0.0143  124 ASN A C   
870  O  O   . ASN A 124 ? 0.9723 0.6632 0.2430 0.2055  0.1095  0.0160  124 ASN A O   
871  C  CB  . ASN A 124 ? 0.4352 0.3053 0.4751 0.0647  0.0881  0.1548  124 ASN A CB  
872  C  CG  . ASN A 124 ? 0.4365 0.1906 0.5065 0.0453  0.0339  0.0146  124 ASN A CG  
873  O  OD1 . ASN A 124 ? 0.4491 0.3982 0.4865 0.0785  0.0540  0.1548  124 ASN A OD1 
874  N  ND2 . ASN A 124 ? 0.5073 0.2239 0.5242 0.0064  0.0064  0.0234  124 ASN A ND2 
875  C  C   . CYS B 10  ? 0.3997 0.4394 0.6974 0.0774  0.0483  0.2862  10  CYS B C   
876  O  O   . CYS B 10  ? 0.4513 0.4696 0.5601 0.0668  0.0344  0.1241  10  CYS B O   
877  N  N   . PRO B 11  ? 0.3804 0.3652 0.3032 -0.0002 -0.1046 0.1111  11  PRO B N   
878  C  CA  . PRO B 11  ? 0.3637 0.2769 0.3220 -0.1251 -0.0213 0.1149  11  PRO B CA  
879  C  C   . PRO B 11  ? 0.3824 0.2804 0.2725 -0.0470 -0.1540 0.0048  11  PRO B C   
880  O  O   . PRO B 11  ? 0.3232 0.1936 0.2790 -0.0217 -0.1315 0.0292  11  PRO B O   
881  C  CB  . PRO B 11  ? 0.5071 0.4122 0.3561 0.1494  -0.1077 0.0010  11  PRO B CB  
882  C  CG  . PRO B 11  ? 0.3754 0.3901 0.5970 -0.0270 -0.2006 0.0872  11  PRO B CG  
883  C  CD  . PRO B 11  ? 0.4497 0.3767 0.3953 -0.0695 -0.1907 0.0795  11  PRO B CD  
884  N  N   . LEU B 12  ? 0.3452 0.2201 0.2747 0.0118  -0.1633 0.0234  12  LEU B N   
885  C  CA  . LEU B 12  ? 0.2796 0.2278 0.2492 0.0151  -0.0727 -0.0121 12  LEU B CA  
886  C  C   . LEU B 12  ? 0.2687 0.2702 0.2356 0.0024  -0.0779 -0.0223 12  LEU B C   
887  O  O   . LEU B 12  ? 0.4172 0.2456 0.3389 0.0136  -0.1597 -0.0341 12  LEU B O   
888  C  CB  . LEU B 12  ? 0.2986 0.2622 0.3198 0.0289  -0.1262 0.0554  12  LEU B CB  
889  C  CG  . LEU B 12  ? 0.3277 0.1944 0.3125 -0.0858 -0.0450 0.0379  12  LEU B CG  
890  C  CD1 . LEU B 12  ? 0.3104 0.2161 0.3285 -0.0268 -0.0241 -0.0494 12  LEU B CD1 
891  C  CD2 . LEU B 12  ? 0.3700 0.2332 0.4142 -0.0662 -0.0025 0.0238  12  LEU B CD2 
892  N  N   . MET B 13  ? 0.2828 0.1513 0.2317 -0.0134 -0.0848 0.0025  13  MET B N   
893  C  CA  . MET B 13  ? 0.3261 0.2324 0.1792 0.0108  -0.1002 -0.0150 13  MET B CA  
894  C  C   . MET B 13  ? 0.2784 0.2220 0.1574 0.0017  -0.0337 0.0199  13  MET B C   
895  O  O   . MET B 13  ? 0.2839 0.1430 0.2093 -0.0137 -0.0975 0.0224  13  MET B O   
896  C  CB  . MET B 13  ? 0.4193 0.2907 0.4291 0.1199  -0.0226 0.0310  13  MET B CB  
897  C  CG  . MET B 13  ? 0.4198 0.3441 0.2122 -0.0607 -0.0275 0.1418  13  MET B CG  
898  S  SD  . MET B 13  ? 0.6648 0.5405 0.5581 0.0437  -0.0909 0.0136  13  MET B SD  
899  C  CE  . MET B 13  ? 0.1922 0.1888 0.1822 -0.0667 0.0538  0.0070  13  MET B CE  
900  N  N   . VAL B 14  ? 0.2533 0.1839 0.1717 -0.0001 -0.0584 -0.0341 14  VAL B N   
901  C  CA  . VAL B 14  ? 0.2245 0.1826 0.1851 -0.0102 -0.0275 -0.0165 14  VAL B CA  
902  C  C   . VAL B 14  ? 0.2351 0.1986 0.1687 0.0011  -0.0164 -0.0029 14  VAL B C   
903  O  O   . VAL B 14  ? 0.2953 0.2338 0.2158 0.0789  -0.0717 -0.0532 14  VAL B O   
904  C  CB  . VAL B 14  ? 0.2444 0.2000 0.1835 -0.0015 -0.0564 0.0173  14  VAL B CB  
905  C  CG1 . VAL B 14  ? 0.2021 0.1979 0.2338 0.0048  -0.0212 0.0472  14  VAL B CG1 
906  C  CG2 . VAL B 14  ? 0.2303 0.1974 0.2006 -0.0436 -0.0313 -0.0367 14  VAL B CG2 
907  N  N   . LYS B 15  ? 0.2309 0.1628 0.1835 0.0115  -0.0499 -0.0043 15  LYS B N   
908  C  CA  . LYS B 15  ? 0.2468 0.2182 0.1639 0.0143  -0.0472 -0.0025 15  LYS B CA  
909  C  C   . LYS B 15  ? 0.2357 0.1855 0.1707 0.0591  -0.0298 -0.0227 15  LYS B C   
910  O  O   . LYS B 15  ? 0.3148 0.1802 0.1699 0.0509  -0.0203 -0.0100 15  LYS B O   
911  C  CB  . LYS B 15  ? 0.2536 0.2991 0.2439 0.0170  -0.0243 0.0449  15  LYS B CB  
912  C  CG  . LYS B 15  ? 0.2518 0.3800 0.3624 0.0090  -0.0358 0.0813  15  LYS B CG  
913  C  CD  . LYS B 15  ? 0.4215 0.6572 0.5097 -0.1967 -0.0089 0.1580  15  LYS B CD  
914  N  N   . VAL B 16  ? 0.2482 0.1679 0.1483 0.0228  -0.0154 0.0110  16  VAL B N   
915  C  CA  . VAL B 16  ? 0.2316 0.2075 0.1595 0.0445  -0.0040 0.0492  16  VAL B CA  
916  C  C   . VAL B 16  ? 0.2158 0.2207 0.1695 0.0273  0.0043  0.0323  16  VAL B C   
917  O  O   . VAL B 16  ? 0.2485 0.1859 0.1742 0.0455  -0.0156 -0.0001 16  VAL B O   
918  C  CB  . VAL B 16  ? 0.2499 0.1879 0.1918 0.0375  0.0055  0.0097  16  VAL B CB  
919  C  CG1 . VAL B 16  ? 0.2268 0.1612 0.2130 0.0582  0.0071  -0.0051 16  VAL B CG1 
920  C  CG2 . VAL B 16  ? 0.2642 0.2254 0.1794 0.0164  -0.0116 0.0189  16  VAL B CG2 
921  N  N   . LEU B 17  ? 0.1919 0.1554 0.1779 0.0021  -0.0009 0.0105  17  LEU B N   
922  C  CA  . LEU B 17  ? 0.1935 0.1463 0.1688 0.0092  0.0033  0.0173  17  LEU B CA  
923  C  C   . LEU B 17  ? 0.1666 0.1094 0.1520 -0.0007 0.0395  0.0125  17  LEU B C   
924  O  O   . LEU B 17  ? 0.1961 0.1774 0.1651 0.0429  0.0480  0.0076  17  LEU B O   
925  C  CB  . LEU B 17  ? 0.1962 0.1592 0.2282 0.0393  0.0028  0.0284  17  LEU B CB  
926  C  CG  . LEU B 17  ? 0.2782 0.2079 0.2264 -0.0079 0.0427  0.0290  17  LEU B CG  
927  C  CD1 . LEU B 17  ? 0.3992 0.1762 0.3143 -0.0616 0.0426  0.0450  17  LEU B CD1 
928  C  CD2 . LEU B 17  ? 0.3691 0.2373 0.2269 -0.0380 0.0817  0.0214  17  LEU B CD2 
929  N  N   . ASP B 18  ? 0.1731 0.1225 0.1768 0.0208  0.0071  -0.0121 18  ASP B N   
930  C  CA  . ASP B 18  ? 0.1513 0.1376 0.1451 -0.0053 0.0152  -0.0139 18  ASP B CA  
931  C  C   . ASP B 18  ? 0.1622 0.0762 0.1865 0.0044  0.0172  -0.0233 18  ASP B C   
932  O  O   . ASP B 18  ? 0.1859 0.1222 0.1739 0.0118  0.0161  -0.0091 18  ASP B O   
933  C  CB  . ASP B 18  ? 0.1780 0.1359 0.1797 -0.0053 -0.0171 0.0025  18  ASP B CB  
934  C  CG  . ASP B 18  ? 0.2297 0.1252 0.1818 -0.0416 0.0071  -0.0090 18  ASP B CG  
935  O  OD1 . ASP B 18  ? 0.1717 0.1211 0.2122 0.0071  0.0178  0.0115  18  ASP B OD1 
936  O  OD2 . ASP B 18  ? 0.2139 0.1416 0.2513 -0.0499 -0.0110 -0.0435 18  ASP B OD2 
937  N  N   . ALA B 19  ? 0.1306 0.1353 0.1678 0.0071  0.0321  0.0011  19  ALA B N   
938  C  CA  . ALA B 19  ? 0.1389 0.1557 0.1553 0.0170  0.0288  0.0016  19  ALA B CA  
939  C  C   . ALA B 19  ? 0.1326 0.1806 0.1655 0.0124  0.0016  -0.0310 19  ALA B C   
940  O  O   . ALA B 19  ? 0.1488 0.1946 0.1862 0.0130  0.0049  -0.0109 19  ALA B O   
941  C  CB  . ALA B 19  ? 0.2059 0.1092 0.1995 -0.0038 0.0050  -0.0022 19  ALA B CB  
942  N  N   . VAL B 20  ? 0.1614 0.1588 0.1954 0.0506  0.0017  0.0021  20  VAL B N   
943  C  CA  . VAL B 20  ? 0.1591 0.1845 0.2049 0.0213  0.0000  0.0359  20  VAL B CA  
944  C  C   . VAL B 20  ? 0.1826 0.1509 0.2532 0.0280  -0.0089 0.0049  20  VAL B C   
945  O  O   . VAL B 20  ? 0.1967 0.2668 0.2955 0.0516  0.0376  0.0765  20  VAL B O   
946  C  CB  . VAL B 20  ? 0.1516 0.1665 0.2671 0.0173  0.0358  0.0567  20  VAL B CB  
947  C  CG1 . VAL B 20  ? 0.2480 0.1826 0.2766 0.0440  0.0517  0.0236  20  VAL B CG1 
948  C  CG2 . VAL B 20  ? 0.2078 0.2360 0.2764 0.0455  0.0087  0.0487  20  VAL B CG2 
949  N  N   . ARG B 21  ? 0.1776 0.1706 0.2126 0.0036  0.0492  0.0039  21  ARG B N   
950  C  CA  . ARG B 21  ? 0.2052 0.2328 0.2091 0.0119  0.0451  -0.0242 21  ARG B CA  
951  C  C   . ARG B 21  ? 0.1785 0.2090 0.2124 0.0502  0.0407  -0.0156 21  ARG B C   
952  O  O   . ARG B 21  ? 0.2280 0.2483 0.2599 0.0428  0.0676  -0.0147 21  ARG B O   
953  C  CB  . ARG B 21  ? 0.3599 0.1627 0.2957 -0.0006 0.0585  -0.0663 21  ARG B CB  
954  C  CG  . ARG B 21  ? 0.2674 0.1847 0.3035 -0.0066 -0.0046 -0.0205 21  ARG B CG  
955  C  CD  . ARG B 21  ? 0.3949 0.4683 0.2807 -0.0918 -0.0266 -0.1367 21  ARG B CD  
956  N  NE  . ARG B 21  ? 0.4189 0.3775 0.3177 -0.2278 -0.1181 -0.1577 21  ARG B NE  
957  N  N   . GLY B 22  ? 0.1768 0.1602 0.2153 0.0022  0.0094  -0.0110 22  GLY B N   
958  C  CA  . GLY B 22  ? 0.1638 0.2008 0.2340 0.0066  0.0093  0.0151  22  GLY B CA  
959  C  C   . GLY B 22  ? 0.2013 0.1912 0.2053 -0.0291 0.0543  0.0000  22  GLY B C   
960  O  O   . GLY B 22  ? 0.2342 0.1576 0.1967 -0.0505 0.0446  -0.0207 22  GLY B O   
961  N  N   . SER B 23  ? 0.1943 0.2028 0.1668 -0.0069 0.0176  -0.0123 23  SER B N   
962  C  CA  . SER B 23  ? 0.2182 0.1895 0.2029 0.0179  -0.0092 0.0007  23  SER B CA  
963  C  C   . SER B 23  ? 0.1945 0.1948 0.1857 0.0137  -0.0059 -0.0030 23  SER B C   
964  O  O   . SER B 23  ? 0.2363 0.1723 0.2046 0.0323  0.0230  -0.0136 23  SER B O   
965  C  CB  . SER B 23  ? 0.2867 0.2536 0.2882 -0.0322 -0.0159 -0.0747 23  SER B CB  
966  O  OG  . SER B 23  ? 0.3778 0.1818 0.3557 -0.0178 -0.0047 -0.0126 23  SER B OG  
967  N  N   . PRO B 24  ? 0.2075 0.1712 0.1925 -0.0072 0.0397  -0.0069 24  PRO B N   
968  C  CA  . PRO B 24  ? 0.2062 0.2057 0.1868 0.0374  0.0197  -0.0154 24  PRO B CA  
969  C  C   . PRO B 24  ? 0.2285 0.1343 0.2120 0.0190  -0.0158 0.0176  24  PRO B C   
970  O  O   . PRO B 24  ? 0.1969 0.1629 0.2482 0.0218  -0.0079 0.0032  24  PRO B O   
971  C  CB  . PRO B 24  ? 0.2561 0.2240 0.2170 0.0433  0.0016  -0.0052 24  PRO B CB  
972  C  CG  . PRO B 24  ? 0.3316 0.4561 0.1946 0.0439  0.0532  -0.0122 24  PRO B CG  
973  C  CD  . PRO B 24  ? 0.1882 0.2130 0.1863 -0.0553 0.0148  -0.0317 24  PRO B CD  
974  N  N   . ALA B 25  ? 0.1854 0.1813 0.1822 -0.0178 -0.0068 0.0242  25  ALA B N   
975  C  CA  . ALA B 25  ? 0.2208 0.0991 0.1865 -0.0001 0.0137  0.0121  25  ALA B CA  
976  C  C   . ALA B 25  ? 0.2313 0.1678 0.1751 0.0242  -0.0115 0.0216  25  ALA B C   
977  O  O   . ALA B 25  ? 0.2116 0.1637 0.2147 0.0125  -0.0221 0.0006  25  ALA B O   
978  C  CB  . ALA B 25  ? 0.1848 0.1419 0.2119 0.0089  -0.0294 -0.0042 25  ALA B CB  
979  N  N   . ILE B 26  ? 0.2046 0.1544 0.2404 0.0010  -0.0480 0.0107  26  ILE B N   
980  C  CA  . ILE B 26  ? 0.2182 0.1761 0.2282 0.0088  -0.0169 -0.0274 26  ILE B CA  
981  C  C   . ILE B 26  ? 0.2296 0.1497 0.2170 -0.0089 -0.0615 -0.0389 26  ILE B C   
982  O  O   . ILE B 26  ? 0.2680 0.1938 0.2382 -0.0095 -0.0336 0.0204  26  ILE B O   
983  C  CB  . ILE B 26  ? 0.2906 0.3200 0.2277 0.0515  0.0578  -0.0347 26  ILE B CB  
984  C  CG1 . ILE B 26  ? 0.2755 0.2670 0.2670 0.0367  0.0244  -0.0635 26  ILE B CG1 
985  C  CG2 . ILE B 26  ? 0.2941 0.2265 0.3170 0.0472  0.0703  -0.0393 26  ILE B CG2 
986  C  CD1 . ILE B 26  ? 0.2840 0.3129 0.4172 -0.0125 0.0631  -0.0530 26  ILE B CD1 
987  N  N   . ASN B 27  ? 0.2770 0.1727 0.2113 0.0625  -0.0561 -0.0389 27  ASN B N   
988  C  CA  . ASN B 27  ? 0.3066 0.1364 0.3084 0.0512  -0.0211 -0.0080 27  ASN B CA  
989  C  C   . ASN B 27  ? 0.2341 0.1759 0.3025 0.0112  -0.0178 0.0312  27  ASN B C   
990  O  O   . ASN B 27  ? 0.3192 0.1880 0.2999 0.0006  0.0299  -0.0068 27  ASN B O   
991  C  CB  . ASN B 27  ? 0.2792 0.1389 0.3164 0.0174  -0.0423 0.0039  27  ASN B CB  
992  C  CG  . ASN B 27  ? 0.4322 0.4217 0.4602 -0.0966 -0.1625 -0.0210 27  ASN B CG  
993  O  OD1 . ASN B 27  ? 0.7016 0.4686 0.5115 -0.0528 -0.2645 -0.0444 27  ASN B OD1 
994  N  ND2 . ASN B 27  ? 0.4369 0.3949 0.5247 -0.0391 -0.0792 -0.0456 27  ASN B ND2 
995  N  N   . VAL B 28  ? 0.2336 0.1588 0.2306 -0.0024 0.0266  0.0169  28  VAL B N   
996  C  CA  . VAL B 28  ? 0.2062 0.1950 0.2459 -0.0058 0.0166  0.0158  28  VAL B CA  
997  C  C   . VAL B 28  ? 0.2241 0.1742 0.1891 0.0430  0.0253  0.0078  28  VAL B C   
998  O  O   . VAL B 28  ? 0.1990 0.1790 0.1944 -0.0029 -0.0320 0.0162  28  VAL B O   
999  C  CB  . VAL B 28  ? 0.1899 0.2337 0.2097 0.0274  -0.0318 0.0197  28  VAL B CB  
1000 C  CG1 . VAL B 28  ? 0.2396 0.3659 0.2681 0.0011  -0.0069 -0.0902 28  VAL B CG1 
1001 C  CG2 . VAL B 28  ? 0.2136 0.2340 0.3099 0.0791  -0.0088 0.0371  28  VAL B CG2 
1002 N  N   . ALA B 29  ? 0.2216 0.1700 0.2276 0.0259  -0.0187 0.0091  29  ALA B N   
1003 C  CA  . ALA B 29  ? 0.1903 0.1478 0.2472 0.0140  0.0035  0.0056  29  ALA B CA  
1004 C  C   . ALA B 29  ? 0.2534 0.1767 0.1806 0.0177  -0.0301 0.0052  29  ALA B C   
1005 O  O   . ALA B 29  ? 0.2520 0.1589 0.1868 0.0328  -0.0251 0.0219  29  ALA B O   
1006 C  CB  . ALA B 29  ? 0.2279 0.1461 0.2386 -0.0193 -0.0071 0.0072  29  ALA B CB  
1007 N  N   . VAL B 30  ? 0.2255 0.1825 0.1646 0.0137  -0.0398 0.0083  30  VAL B N   
1008 C  CA  . VAL B 30  ? 0.2185 0.1919 0.1862 -0.0043 0.0076  -0.0469 30  VAL B CA  
1009 C  C   . VAL B 30  ? 0.2307 0.1588 0.1951 -0.0226 -0.0456 -0.0184 30  VAL B C   
1010 O  O   . VAL B 30  ? 0.2424 0.1673 0.2211 0.0246  -0.0566 -0.0426 30  VAL B O   
1011 C  CB  . VAL B 30  ? 0.1993 0.1920 0.2043 -0.0237 -0.0033 -0.0345 30  VAL B CB  
1012 C  CG1 . VAL B 30  ? 0.2475 0.1822 0.2580 -0.0184 -0.0318 -0.0251 30  VAL B CG1 
1013 C  CG2 . VAL B 30  ? 0.1998 0.2283 0.2231 -0.0572 -0.0142 -0.0019 30  VAL B CG2 
1014 N  N   . HIS B 31  ? 0.2293 0.1829 0.2016 -0.0035 -0.0462 0.0063  31  HIS B N   
1015 C  CA  . HIS B 31  ? 0.2059 0.1693 0.2725 0.0077  -0.0647 -0.0137 31  HIS B CA  
1016 C  C   . HIS B 31  ? 0.2426 0.1924 0.2101 -0.0073 -0.0504 0.0013  31  HIS B C   
1017 O  O   . HIS B 31  ? 0.2708 0.2220 0.2505 0.0519  -0.0521 0.0069  31  HIS B O   
1018 C  CB  . HIS B 31  ? 0.2444 0.2571 0.3149 0.0341  -0.0075 -0.0342 31  HIS B CB  
1019 C  CG  . HIS B 31  ? 0.3457 0.2832 0.4254 -0.0418 0.0269  -0.0652 31  HIS B CG  
1020 N  ND1 . HIS B 31  ? 0.3633 0.2889 0.5085 -0.0528 -0.0081 -0.0630 31  HIS B ND1 
1021 C  CD2 . HIS B 31  ? 0.3234 0.2727 0.4815 -0.1152 -0.0271 -0.0062 31  HIS B CD2 
1022 C  CE1 . HIS B 31  ? 0.3156 0.3003 0.4679 -0.0456 0.0100  -0.0474 31  HIS B CE1 
1023 N  NE2 . HIS B 31  ? 0.3261 0.2951 0.6258 -0.0955 -0.0273 0.0093  31  HIS B NE2 
1024 N  N   . VAL B 32  ? 0.2448 0.1315 0.2424 0.0028  -0.0817 -0.0287 32  VAL B N   
1025 C  CA  . VAL B 32  ? 0.2214 0.1448 0.2481 -0.0299 -0.0525 -0.0363 32  VAL B CA  
1026 C  C   . VAL B 32  ? 0.2251 0.1772 0.2288 -0.0430 -0.0600 0.0091  32  VAL B C   
1027 O  O   . VAL B 32  ? 0.2595 0.2401 0.3030 -0.0287 -0.0870 -0.0677 32  VAL B O   
1028 C  CB  . VAL B 32  ? 0.2471 0.1418 0.2585 -0.0191 -0.0570 -0.0426 32  VAL B CB  
1029 C  CG1 . VAL B 32  ? 0.2477 0.1255 0.3204 -0.0193 -0.0526 -0.0325 32  VAL B CG1 
1030 C  CG2 . VAL B 32  ? 0.2700 0.1988 0.2149 -0.0308 -0.0468 0.0150  32  VAL B CG2 
1031 N  N   . PHE B 33  ? 0.1773 0.2034 0.3138 -0.0088 -0.0342 -0.0689 33  PHE B N   
1032 C  CA  . PHE B 33  ? 0.1904 0.1787 0.3204 -0.0339 -0.0326 -0.0548 33  PHE B CA  
1033 C  C   . PHE B 33  ? 0.2276 0.1817 0.4058 0.0078  -0.0738 -0.0587 33  PHE B C   
1034 O  O   . PHE B 33  ? 0.2289 0.2229 0.2830 -0.0016 -0.0706 0.0200  33  PHE B O   
1035 C  CB  . PHE B 33  ? 0.2134 0.2233 0.3848 0.0253  0.0149  -0.0318 33  PHE B CB  
1036 C  CG  . PHE B 33  ? 0.2574 0.2525 0.3904 -0.0078 -0.0010 -0.0191 33  PHE B CG  
1037 C  CD1 . PHE B 33  ? 0.2845 0.1737 0.3951 0.0233  0.0290  0.0017  33  PHE B CD1 
1038 C  CD2 . PHE B 33  ? 0.3558 0.1918 0.5915 -0.0768 0.0392  -0.0577 33  PHE B CD2 
1039 C  CE1 . PHE B 33  ? 0.2678 0.1810 0.5031 0.0476  0.0185  0.0048  33  PHE B CE1 
1040 C  CE2 . PHE B 33  ? 0.3878 0.1885 0.6277 -0.0256 0.0065  0.0392  33  PHE B CE2 
1041 C  CZ  . PHE B 33  ? 0.3451 0.2409 0.4440 -0.0066 0.0022  -0.0387 33  PHE B CZ  
1042 N  N   . ARG B 34  ? 0.2689 0.1981 0.4109 -0.0215 -0.1136 -0.0331 34  ARG B N   
1043 C  CA  . ARG B 34  ? 0.2677 0.2316 0.3801 0.0055  -0.0798 -0.0254 34  ARG B CA  
1044 C  C   . ARG B 34  ? 0.2559 0.2332 0.3397 -0.0152 -0.0969 -0.0494 34  ARG B C   
1045 O  O   . ARG B 34  ? 0.2215 0.2832 0.4705 -0.0172 -0.0586 -0.0927 34  ARG B O   
1046 C  CB  . ARG B 34  ? 0.2994 0.2764 0.3476 0.0339  -0.0535 0.0129  34  ARG B CB  
1047 C  CG  . ARG B 34  ? 0.2962 0.3268 0.4000 -0.0050 -0.0674 -0.0171 34  ARG B CG  
1048 C  CD  . ARG B 34  ? 0.3689 0.2368 0.3161 0.0571  0.0902  0.0156  34  ARG B CD  
1049 N  NE  . ARG B 34  ? 0.2098 0.2935 0.3938 0.0616  -0.1109 0.0793  34  ARG B NE  
1050 C  CZ  . ARG B 34  ? 0.2512 0.3006 0.4266 0.0099  -0.0009 -0.0789 34  ARG B CZ  
1051 N  NH1 . ARG B 34  ? 0.2333 0.3361 0.4606 0.0026  0.0371  -0.0188 34  ARG B NH1 
1052 N  NH2 . ARG B 34  ? 0.2509 0.2712 0.4650 0.0608  -0.0350 -0.0391 34  ARG B NH2 
1053 N  N   . LYS B 35  ? 0.2259 0.2105 0.3135 0.0393  -0.0703 -0.0531 35  LYS B N   
1054 C  CA  . LYS B 35  ? 0.2449 0.3221 0.2935 0.0273  -0.0705 -0.0387 35  LYS B CA  
1055 C  C   . LYS B 35  ? 0.2911 0.3483 0.3633 0.0526  -0.0834 -0.0350 35  LYS B C   
1056 O  O   . LYS B 35  ? 0.2496 0.4033 0.3724 0.0338  -0.0218 0.0034  35  LYS B O   
1057 C  CB  . LYS B 35  ? 0.2950 0.2759 0.3440 0.0339  -0.0455 -0.0601 35  LYS B CB  
1058 C  CG  . LYS B 35  ? 0.4310 0.3815 0.3394 0.0134  -0.0573 0.0000  35  LYS B CG  
1059 C  CD  . LYS B 35  ? 0.3755 0.4442 0.4298 -0.0158 -0.0540 -0.0689 35  LYS B CD  
1060 N  N   . ALA B 36  ? 0.2856 0.3516 0.3605 0.0635  -0.0212 0.0309  36  ALA B N   
1061 C  CA  . ALA B 36  ? 0.3742 0.3507 0.4368 0.0864  -0.0842 0.0806  36  ALA B CA  
1062 C  C   . ALA B 36  ? 0.4194 0.3516 0.4329 0.0714  -0.0835 -0.0456 36  ALA B C   
1063 O  O   . ALA B 36  ? 0.4020 0.3230 0.4018 0.0230  -0.0096 0.0129  36  ALA B O   
1064 C  CB  . ALA B 36  ? 0.3151 0.4003 0.4900 0.0846  -0.1156 0.0228  36  ALA B CB  
1065 N  N   . ALA B 37  ? 0.4049 0.4603 0.4229 0.1075  0.0514  0.1237  37  ALA B N   
1066 C  CA  . ALA B 37  ? 0.5447 0.5334 0.4476 0.1564  0.0139  0.0477  37  ALA B CA  
1067 C  C   . ALA B 37  ? 0.4484 0.5234 0.4292 0.1961  0.0746  0.0158  37  ALA B C   
1068 O  O   . ALA B 37  ? 0.5416 0.5679 0.4632 0.0900  0.0862  0.0694  37  ALA B O   
1069 C  CB  . ALA B 37  ? 0.4996 0.5861 0.5936 0.2051  -0.0013 0.0883  37  ALA B CB  
1070 N  N   . ASP B 38  ? 0.4764 0.4763 0.4835 0.0054  -0.0216 0.0666  38  ASP B N   
1071 C  CA  . ASP B 38  ? 0.6171 0.5730 0.4621 0.0214  0.0137  0.0568  38  ASP B CA  
1072 C  C   . ASP B 38  ? 0.5323 0.7059 0.4009 0.0217  0.1033  0.0343  38  ASP B C   
1073 O  O   . ASP B 38  ? 0.5015 0.6439 0.4996 0.0549  0.1563  0.0857  38  ASP B O   
1074 C  CB  . ASP B 38  ? 0.5554 0.4720 0.5421 -0.1920 -0.0423 0.1573  38  ASP B CB  
1075 C  CG  . ASP B 38  ? 0.3679 0.6599 0.4814 -0.0354 0.0579  -0.0007 38  ASP B CG  
1076 O  OD1 . ASP B 38  ? 0.9413 1.1770 0.5028 0.4237  0.1087  -0.0053 38  ASP B OD1 
1077 O  OD2 . ASP B 38  ? 0.5432 0.5150 0.6200 0.0057  0.0793  -0.0150 38  ASP B OD2 
1078 N  N   . ASP B 39  ? 0.4436 0.5296 0.5582 0.0788  -0.0032 0.0230  39  ASP B N   
1079 C  CA  . ASP B 39  ? 0.4651 0.5068 0.4797 0.0224  -0.0088 0.0593  39  ASP B CA  
1080 C  C   . ASP B 39  ? 0.4157 0.4948 0.3092 -0.0133 -0.0209 0.0678  39  ASP B C   
1081 O  O   . ASP B 39  ? 0.4771 0.8451 0.5512 0.1021  -0.1586 0.1759  39  ASP B O   
1082 C  CB  . ASP B 39  ? 0.6194 0.6995 0.4666 0.0777  0.1028  0.1098  39  ASP B CB  
1083 N  N   . THR B 40  ? 0.4033 0.3750 0.5048 0.0073  -0.0298 -0.0437 40  THR B N   
1084 C  CA  . THR B 40  ? 0.4005 0.3739 0.4205 0.0008  0.0416  0.0742  40  THR B CA  
1085 C  C   . THR B 40  ? 0.3261 0.4278 0.4410 -0.0233 0.0658  0.0899  40  THR B C   
1086 O  O   . THR B 40  ? 0.2943 0.3775 0.4578 -0.0597 0.0778  0.0229  40  THR B O   
1087 C  CB  . THR B 40  ? 0.4433 0.4824 0.4973 -0.0360 0.0250  0.0828  40  THR B CB  
1088 O  OG1 . THR B 40  ? 0.3835 0.3610 0.5426 -0.0152 0.0214  -0.0342 40  THR B OG1 
1089 C  CG2 . THR B 40  ? 0.5436 0.5949 0.6276 0.0287  0.1427  0.1336  40  THR B CG2 
1090 N  N   . TRP B 41  ? 0.2606 0.3948 0.5200 -0.0569 0.0232  0.0597  41  TRP B N   
1091 C  CA  . TRP B 41  ? 0.2881 0.4287 0.4915 -0.1240 0.0116  0.0687  41  TRP B CA  
1092 C  C   . TRP B 41  ? 0.3072 0.2386 0.6032 0.0282  0.0198  -0.0197 41  TRP B C   
1093 O  O   . TRP B 41  ? 0.5932 0.2913 0.7640 -0.1286 -0.1135 -0.0198 41  TRP B O   
1094 C  CB  . TRP B 41  ? 0.2463 0.4312 0.5981 -0.1217 -0.0202 0.0303  41  TRP B CB  
1095 C  CG  . TRP B 41  ? 0.4114 0.2927 0.4540 -0.0193 -0.0621 0.0529  41  TRP B CG  
1096 C  CD1 . TRP B 41  ? 0.3808 0.5206 0.4682 -0.1468 0.0215  0.0573  41  TRP B CD1 
1097 C  CD2 . TRP B 41  ? 0.3345 0.2702 0.4318 -0.0169 -0.0521 -0.0473 41  TRP B CD2 
1098 N  NE1 . TRP B 41  ? 0.4788 0.4559 0.4398 -0.1251 -0.0544 0.0561  41  TRP B NE1 
1099 C  CE2 . TRP B 41  ? 0.4535 0.3947 0.3704 -0.0929 0.0207  0.0017  41  TRP B CE2 
1100 C  CE3 . TRP B 41  ? 0.3675 0.2749 0.4230 0.0382  -0.0480 -0.0197 41  TRP B CE3 
1101 C  CZ2 . TRP B 41  ? 0.4914 0.2598 0.3266 -0.0716 -0.0997 0.0100  41  TRP B CZ2 
1102 C  CZ3 . TRP B 41  ? 0.3131 0.2603 0.3543 0.0515  -0.0773 0.0042  41  TRP B CZ3 
1103 C  CH2 . TRP B 41  ? 0.3034 0.2610 0.3458 0.0962  -0.0838 0.0591  41  TRP B CH2 
1104 N  N   . GLU B 42  ? 0.2842 0.3603 0.5053 -0.0627 -0.0328 -0.1138 42  GLU B N   
1105 C  CA  . GLU B 42  ? 0.2902 0.3468 0.4650 -0.0437 -0.0840 -0.0854 42  GLU B CA  
1106 C  C   . GLU B 42  ? 0.4028 0.3756 0.5840 -0.0679 0.0096  -0.2061 42  GLU B C   
1107 O  O   . GLU B 42  ? 0.3020 0.2387 0.4452 0.0003  -0.0612 -0.0632 42  GLU B O   
1108 C  CB  . GLU B 42  ? 0.3249 0.4941 0.5633 0.1293  -0.0820 -0.1103 42  GLU B CB  
1109 C  CG  . GLU B 42  ? 0.5001 0.5473 0.6463 0.1410  0.0160  0.0255  42  GLU B CG  
1110 C  CD  . GLU B 42  ? 0.4684 0.5615 0.5237 0.0541  -0.0469 -0.0208 42  GLU B CD  
1111 O  OE1 . GLU B 42  ? 1.1166 0.8819 0.6189 -0.1572 -0.2823 0.1392  42  GLU B OE1 
1112 O  OE2 . GLU B 42  ? 0.5272 0.6688 0.5948 -0.1517 -0.1020 -0.0269 42  GLU B OE2 
1113 N  N   . PRO B 43  ? 0.2729 0.3300 0.6037 -0.0619 0.0024  -0.0926 43  PRO B N   
1114 C  CA  . PRO B 43  ? 0.3053 0.2772 0.4652 -0.0938 -0.0431 -0.1143 43  PRO B CA  
1115 C  C   . PRO B 43  ? 0.2768 0.2316 0.4160 -0.0290 -0.0810 -0.1220 43  PRO B C   
1116 O  O   . PRO B 43  ? 0.2678 0.3296 0.5389 0.0175  -0.1403 -0.1242 43  PRO B O   
1117 C  CB  . PRO B 43  ? 0.3010 0.2336 0.5014 -0.0371 -0.0238 -0.1306 43  PRO B CB  
1118 C  CG  . PRO B 43  ? 0.2689 0.4614 0.6782 -0.2454 -0.1119 -0.1921 43  PRO B CG  
1119 C  CD  . PRO B 43  ? 0.4666 0.2472 0.6028 -0.0599 0.0028  -0.0635 43  PRO B CD  
1120 N  N   . PHE B 44  ? 0.2485 0.2509 0.4457 0.0285  -0.0691 -0.0244 44  PHE B N   
1121 C  CA  . PHE B 44  ? 0.2356 0.2802 0.2797 0.0387  -0.0974 -0.0508 44  PHE B CA  
1122 C  C   . PHE B 44  ? 0.2744 0.2218 0.2909 0.0036  -0.1232 -0.0596 44  PHE B C   
1123 O  O   . PHE B 44  ? 0.3595 0.2843 0.3509 0.0672  -0.1069 -0.0389 44  PHE B O   
1124 C  CB  . PHE B 44  ? 0.3038 0.1856 0.3318 0.0414  -0.1465 -0.0076 44  PHE B CB  
1125 C  CG  . PHE B 44  ? 0.3519 0.1852 0.4191 0.1145  -0.0727 -0.0667 44  PHE B CG  
1126 C  CD1 . PHE B 44  ? 0.3625 0.1991 0.4128 0.0675  -0.1271 -0.0334 44  PHE B CD1 
1127 C  CD2 . PHE B 44  ? 0.3165 0.1882 0.3351 0.0873  -0.0890 0.0333  44  PHE B CD2 
1128 C  CE1 . PHE B 44  ? 0.4136 0.3003 0.3506 0.0257  -0.0937 0.0104  44  PHE B CE1 
1129 C  CE2 . PHE B 44  ? 0.4277 0.2868 0.2920 0.0070  -0.1232 -0.0420 44  PHE B CE2 
1130 C  CZ  . PHE B 44  ? 0.4788 0.2163 0.2763 0.0363  -0.1140 -0.0285 44  PHE B CZ  
1131 N  N   . ALA B 45  ? 0.3221 0.2276 0.3000 0.0382  -0.1334 -0.0210 45  ALA B N   
1132 C  CA  . ALA B 45  ? 0.2528 0.2455 0.2522 -0.0504 -0.1086 0.0074  45  ALA B CA  
1133 C  C   . ALA B 45  ? 0.3011 0.2134 0.2646 0.0213  -0.0544 -0.0159 45  ALA B C   
1134 O  O   . ALA B 45  ? 0.3334 0.1499 0.2811 0.0432  -0.0550 -0.0024 45  ALA B O   
1135 C  CB  . ALA B 45  ? 0.3124 0.1445 0.3190 -0.0001 -0.0438 -0.0208 45  ALA B CB  
1136 N  N   . SER B 46  ? 0.2501 0.2350 0.2280 0.0299  -0.1317 -0.0243 46  SER B N   
1137 C  CA  . SER B 46  ? 0.1973 0.1944 0.2328 -0.0182 -0.1061 -0.0252 46  SER B CA  
1138 C  C   . SER B 46  ? 0.2392 0.1978 0.2245 -0.0371 -0.0308 0.0188  46  SER B C   
1139 O  O   . SER B 46  ? 0.2868 0.2325 0.2267 0.0557  -0.0927 -0.0474 46  SER B O   
1140 C  CB  . SER B 46  ? 0.1959 0.1598 0.2748 0.0115  -0.0708 -0.0452 46  SER B CB  
1141 O  OG  . SER B 46  ? 0.2236 0.2219 0.2934 0.0005  -0.1232 -0.0619 46  SER B OG  
1142 N  N   . GLY B 47  ? 0.2386 0.1473 0.2089 -0.0051 -0.0469 -0.0463 47  GLY B N   
1143 C  CA  . GLY B 47  ? 0.2350 0.1980 0.2252 0.0233  -0.0269 -0.0131 47  GLY B CA  
1144 C  C   . GLY B 47  ? 0.2538 0.0780 0.2514 -0.0040 -0.0448 -0.0297 47  GLY B C   
1145 O  O   . GLY B 47  ? 0.2669 0.2481 0.2222 -0.0008 -0.0531 -0.0341 47  GLY B O   
1146 N  N   . LYS B 48  ? 0.2528 0.2115 0.1915 0.0606  -0.0944 -0.0612 48  LYS B N   
1147 C  CA  . LYS B 48  ? 0.2691 0.1229 0.0492 0.0257  -0.0391 0.0022  48  LYS B CA  
1148 C  C   . LYS B 48  ? 0.1931 0.2770 0.1493 0.0433  -0.0048 -0.0499 48  LYS B C   
1149 O  O   . LYS B 48  ? 0.2779 0.2603 0.1625 -0.0185 -0.0433 0.0479  48  LYS B O   
1150 C  CB  . LYS B 48  ? 0.2907 0.1245 0.4377 0.0210  -0.0635 0.0118  48  LYS B CB  
1151 C  CG  . LYS B 48  ? 0.3365 0.1779 0.4910 -0.0033 -0.0920 0.1057  48  LYS B CG  
1152 C  CD  . LYS B 48  ? 0.5816 0.3773 0.4838 -0.0155 -0.0741 0.0965  48  LYS B CD  
1153 N  N   . THR B 49  ? 0.2333 0.2019 0.2083 -0.0061 -0.0335 -0.0006 49  THR B N   
1154 C  CA  . THR B 49  ? 0.2323 0.1366 0.2356 0.0235  -0.0387 0.0024  49  THR B CA  
1155 C  C   . THR B 49  ? 0.2428 0.2099 0.2936 0.0135  -0.0440 -0.0837 49  THR B C   
1156 O  O   . THR B 49  ? 0.2265 0.2211 0.2579 0.0178  -0.0323 0.0532  49  THR B O   
1157 C  CB  . THR B 49  ? 0.2490 0.1911 0.1691 -0.0125 -0.0274 -0.0140 49  THR B CB  
1158 O  OG1 . THR B 49  ? 0.2266 0.1720 0.2031 0.0054  -0.0169 -0.0005 49  THR B OG1 
1159 C  CG2 . THR B 49  ? 0.2525 0.2142 0.1755 0.0232  -0.0128 0.0016  49  THR B CG2 
1160 N  N   . SER B 50  ? 0.2643 0.1819 0.2065 0.0535  -0.0175 -0.0240 50  SER B N   
1161 C  CA  . SER B 50  ? 0.2803 0.2049 0.2206 0.0476  -0.0045 -0.0402 50  SER B CA  
1162 C  C   . SER B 50  ? 0.2544 0.3193 0.2460 0.0145  -0.0136 -0.0744 50  SER B C   
1163 O  O   . SER B 50  ? 0.2908 0.2327 0.2521 0.0540  -0.0176 -0.0553 50  SER B O   
1164 C  CB  . SER B 50  ? 0.3233 0.2884 0.2016 -0.0494 -0.0033 -0.0414 50  SER B CB  
1165 O  OG  . SER B 50  ? 0.3042 0.2978 0.2868 -0.0027 -0.0137 0.0132  50  SER B OG  
1166 N  N   . GLU B 51  ? 0.3224 0.3078 0.2407 0.0369  0.0499  -0.0489 51  GLU B N   
1167 C  CA  . GLU B 51  ? 0.3161 0.2527 0.2716 0.0145  0.0157  -0.0180 51  GLU B CA  
1168 C  C   . GLU B 51  ? 0.2735 0.2941 0.2423 0.0448  0.0253  -0.0356 51  GLU B C   
1169 O  O   . GLU B 51  ? 0.2706 0.3472 0.2748 0.0444  -0.0051 -0.0296 51  GLU B O   
1170 C  CB  . GLU B 51  ? 0.3790 0.3988 0.2830 0.0197  0.0111  -0.0930 51  GLU B CB  
1171 N  N   . SER B 52  ? 0.2868 0.2817 0.2107 0.0390  0.0001  -0.0751 52  SER B N   
1172 C  CA  . SER B 52  ? 0.2578 0.3478 0.2061 -0.0335 -0.0368 0.0095  52  SER B CA  
1173 C  C   . SER B 52  ? 0.2697 0.2132 0.2521 -0.0060 0.0128  -0.0174 52  SER B C   
1174 O  O   . SER B 52  ? 0.2693 0.2675 0.2468 -0.0451 0.0337  0.0573  52  SER B O   
1175 C  CB  . SER B 52  ? 0.3845 0.3458 0.2747 -0.0272 0.0344  0.0565  52  SER B CB  
1176 O  OG  . SER B 52  ? 0.4676 0.3150 0.3722 -0.0260 -0.0090 0.0912  52  SER B OG  
1177 N  N   . GLY B 53  ? 0.2816 0.2339 0.1735 0.0417  0.0147  -0.0312 53  GLY B N   
1178 C  CA  . GLY B 53  ? 0.2575 0.1598 0.2020 -0.0368 0.0461  -0.0250 53  GLY B CA  
1179 C  C   . GLY B 53  ? 0.2400 0.2468 0.1723 0.0009  -0.0128 -0.0420 53  GLY B C   
1180 O  O   . GLY B 53  ? 0.3015 0.1856 0.1648 0.0237  -0.0046 -0.0148 53  GLY B O   
1181 N  N   . GLU B 54  ? 0.2862 0.2537 0.1729 0.0525  -0.0319 -0.0325 54  GLU B N   
1182 C  CA  . GLU B 54  ? 0.2872 0.2586 0.1592 0.0414  -0.0212 -0.0016 54  GLU B CA  
1183 C  C   . GLU B 54  ? 0.3051 0.1919 0.1717 0.0048  -0.0452 0.0031  54  GLU B C   
1184 O  O   . GLU B 54  ? 0.3540 0.2079 0.2081 0.0272  -0.0669 -0.0335 54  GLU B O   
1185 C  CB  . GLU B 54  ? 0.2959 0.2211 0.2279 0.0265  -0.0161 -0.0017 54  GLU B CB  
1186 C  CG  . GLU B 54  ? 0.3351 0.2341 0.2959 0.0114  0.0160  0.0183  54  GLU B CG  
1187 C  CD  . GLU B 54  ? 0.3757 0.3826 0.3348 -0.0600 0.0046  0.0722  54  GLU B CD  
1188 O  OE1 . GLU B 54  ? 0.4751 0.8927 0.3501 -0.1264 -0.0374 0.1575  54  GLU B OE1 
1189 O  OE2 . GLU B 54  ? 0.5614 0.3682 0.5898 -0.1463 0.1041  0.0234  54  GLU B OE2 
1190 N  N   . LEU B 55  ? 0.2959 0.1733 0.2193 -0.0005 -0.0414 -0.0210 55  LEU B N   
1191 C  CA  . LEU B 55  ? 0.2981 0.1941 0.2314 0.0166  -0.0241 -0.0254 55  LEU B CA  
1192 C  C   . LEU B 55  ? 0.3699 0.2359 0.2408 0.0611  -0.0175 -0.0092 55  LEU B C   
1193 O  O   . LEU B 55  ? 0.3146 0.2111 0.2438 0.0287  -0.0254 -0.0180 55  LEU B O   
1194 C  CB  . LEU B 55  ? 0.2849 0.2058 0.2579 0.0199  -0.0132 -0.0292 55  LEU B CB  
1195 C  CG  . LEU B 55  ? 0.2986 0.1917 0.2724 0.0881  -0.0328 -0.0259 55  LEU B CG  
1196 C  CD1 . LEU B 55  ? 0.3592 0.2169 0.2476 0.0293  -0.0777 -0.0222 55  LEU B CD1 
1197 C  CD2 . LEU B 55  ? 0.2561 0.2661 0.3131 0.0708  -0.0319 0.0244  55  LEU B CD2 
1198 N  N   . HIS B 56  ? 0.3463 0.2452 0.2283 0.0110  -0.0703 0.0376  56  HIS B N   
1199 C  CA  . HIS B 56  ? 0.3172 0.2776 0.3264 0.0562  -0.0789 0.0686  56  HIS B CA  
1200 C  C   . HIS B 56  ? 0.3419 0.3057 0.3069 0.0233  -0.0714 0.0911  56  HIS B C   
1201 O  O   . HIS B 56  ? 0.3941 0.3468 0.3351 -0.0549 -0.0914 0.0615  56  HIS B O   
1202 C  CB  . HIS B 56  ? 0.4441 0.3243 0.3096 -0.0184 -0.0655 0.1145  56  HIS B CB  
1203 C  CG  . HIS B 56  ? 0.4069 0.3957 0.3190 0.0148  0.0788  0.0151  56  HIS B CG  
1204 N  ND1 . HIS B 56  ? 0.4752 0.4844 0.6580 -0.0459 0.0077  0.1410  56  HIS B ND1 
1205 C  CD2 . HIS B 56  ? 0.4284 0.4904 0.3527 -0.1325 -0.1223 0.1121  56  HIS B CD2 
1206 C  CE1 . HIS B 56  ? 0.3689 0.5162 0.4885 -0.0766 0.0098  0.2345  56  HIS B CE1 
1207 N  NE2 . HIS B 56  ? 0.4700 0.5830 0.6496 -0.1223 -0.1591 -0.0253 56  HIS B NE2 
1208 N  N   . GLY B 57  ? 0.4112 0.2694 0.3344 0.0235  -0.1028 0.0728  57  GLY B N   
1209 C  CA  . GLY B 57  ? 0.3282 0.3546 0.3119 0.1172  -0.0454 0.0231  57  GLY B CA  
1210 C  C   . GLY B 57  ? 0.3461 0.1939 0.3380 0.0328  -0.0535 0.0262  57  GLY B C   
1211 O  O   . GLY B 57  ? 0.4441 0.4367 0.3556 -0.0418 -0.1403 -0.0312 57  GLY B O   
1212 N  N   . LEU B 58  ? 0.3590 0.2621 0.2871 0.0202  -0.0641 -0.0023 58  LEU B N   
1213 C  CA  . LEU B 58  ? 0.3548 0.2686 0.3124 -0.0069 -0.0782 0.0009  58  LEU B CA  
1214 C  C   . LEU B 58  ? 0.3265 0.3067 0.3224 -0.0175 -0.0784 -0.0251 58  LEU B C   
1215 O  O   . LEU B 58  ? 0.3164 0.3653 0.3861 -0.0126 -0.1176 0.0241  58  LEU B O   
1216 C  CB  . LEU B 58  ? 0.3223 0.2161 0.3091 -0.0175 -0.0436 0.0018  58  LEU B CB  
1217 C  CG  . LEU B 58  ? 0.2466 0.3148 0.3016 0.0119  -0.0790 0.0149  58  LEU B CG  
1218 C  CD1 . LEU B 58  ? 0.3239 0.3206 0.3233 0.0754  -0.1427 0.0334  58  LEU B CD1 
1219 C  CD2 . LEU B 58  ? 0.2738 0.2462 0.3523 0.0419  -0.1144 -0.0449 58  LEU B CD2 
1220 N  N   . THR B 59  ? 0.3492 0.2622 0.3792 -0.0153 -0.1371 -0.0096 59  THR B N   
1221 C  CA  . THR B 59  ? 0.3594 0.2665 0.3371 -0.0099 -0.1716 -0.0319 59  THR B CA  
1222 C  C   . THR B 59  ? 0.2738 0.3398 0.2708 0.0653  -0.1225 -0.0284 59  THR B C   
1223 O  O   . THR B 59  ? 0.3893 0.3060 0.2685 0.0193  -0.0542 0.0484  59  THR B O   
1224 C  CB  . THR B 59  ? 0.3297 0.3458 0.3066 0.0536  -0.1310 -0.0368 59  THR B CB  
1225 O  OG1 . THR B 59  ? 0.3468 0.3284 0.3332 0.0389  -0.1056 -0.0301 59  THR B OG1 
1226 C  CG2 . THR B 59  ? 0.3713 0.2245 0.3611 0.0330  -0.1234 -0.0518 59  THR B CG2 
1227 N  N   . THR B 60  ? 0.3921 0.3443 0.3699 0.0926  -0.1338 0.0510  60  THR B N   
1228 C  CA  . THR B 60  ? 0.4554 0.2813 0.2740 0.0583  -0.0990 -0.0807 60  THR B CA  
1229 C  C   . THR B 60  ? 0.4209 0.2266 0.2789 -0.0019 -0.0711 -0.0533 60  THR B C   
1230 O  O   . THR B 60  ? 0.3321 0.2813 0.2970 0.0462  -0.1042 0.0501  60  THR B O   
1231 C  CB  . THR B 60  ? 0.4532 0.3161 0.3828 0.0429  -0.1565 -0.1289 60  THR B CB  
1232 O  OG1 . THR B 60  ? 0.4476 0.3386 0.4614 0.0507  -0.1931 -0.0115 60  THR B OG1 
1233 C  CG2 . THR B 60  ? 0.5890 0.3034 0.3345 0.0466  -0.1655 -0.1123 60  THR B CG2 
1234 N  N   . GLU B 61  ? 0.4157 0.2879 0.3453 -0.0239 -0.1172 -0.0286 61  GLU B N   
1235 C  CA  . GLU B 61  ? 0.4130 0.2892 0.3982 0.0187  -0.0803 -0.0512 61  GLU B CA  
1236 C  C   . GLU B 61  ? 0.4441 0.2893 0.3046 0.0804  -0.1080 -0.0033 61  GLU B C   
1237 O  O   . GLU B 61  ? 0.3348 0.2744 0.3959 0.0551  -0.0704 -0.0257 61  GLU B O   
1238 C  CB  . GLU B 61  ? 0.4659 0.4436 0.5125 0.0051  -0.0382 0.0376  61  GLU B CB  
1239 C  CG  . GLU B 61  ? 0.3943 0.2645 0.4333 0.0020  -0.0421 0.0085  61  GLU B CG  
1240 C  CD  . GLU B 61  ? 0.5237 0.4069 0.3359 -0.0755 -0.0546 -0.0239 61  GLU B CD  
1241 O  OE1 . GLU B 61  ? 0.7390 0.3224 0.3620 0.1265  -0.1134 0.0135  61  GLU B OE1 
1242 O  OE2 . GLU B 61  ? 0.6112 0.4285 0.6188 -0.1775 0.0064  0.0015  61  GLU B OE2 
1243 N  N   . GLU B 62  ? 0.4117 0.2912 0.2413 0.0734  -0.0629 0.0655  62  GLU B N   
1244 C  CA  . GLU B 62  ? 0.3157 0.3097 0.4700 -0.0502 -0.1074 -0.0190 62  GLU B CA  
1245 C  C   . GLU B 62  ? 0.4379 0.3052 0.3309 0.0168  -0.1014 -0.0572 62  GLU B C   
1246 O  O   . GLU B 62  ? 0.4469 0.2583 0.6551 0.1404  -0.0702 0.0482  62  GLU B O   
1247 C  CB  . GLU B 62  ? 0.3859 0.4801 0.4641 -0.0437 -0.1803 0.1189  62  GLU B CB  
1248 N  N   . GLU B 63  ? 0.4204 0.3026 0.3794 -0.0122 -0.1661 0.0328  63  GLU B N   
1249 C  CA  . GLU B 63  ? 0.3560 0.2197 0.3652 0.0047  -0.1146 -0.0113 63  GLU B CA  
1250 C  C   . GLU B 63  ? 0.3481 0.1941 0.3086 0.0117  -0.0951 0.0143  63  GLU B C   
1251 O  O   . GLU B 63  ? 0.3358 0.2649 0.4287 0.0231  -0.0965 0.0462  63  GLU B O   
1252 C  CB  . GLU B 63  ? 0.4064 0.2316 0.4116 0.0040  -0.1619 -0.0299 63  GLU B CB  
1253 C  CG  . GLU B 63  ? 0.3178 0.2177 0.4460 0.0222  -0.1519 -0.0729 63  GLU B CG  
1254 C  CD  . GLU B 63  ? 0.3526 0.1771 0.4860 -0.0462 -0.0472 -0.0219 63  GLU B CD  
1255 O  OE1 . GLU B 63  ? 0.3843 0.2894 0.3883 -0.0267 -0.0431 -0.0304 63  GLU B OE1 
1256 O  OE2 . GLU B 63  ? 0.3803 0.3018 0.4965 -0.0901 0.0189  -0.0365 63  GLU B OE2 
1257 N  N   . PHE B 64  ? 0.3310 0.1303 0.3211 0.0529  -0.0619 0.0119  64  PHE B N   
1258 C  CA  . PHE B 64  ? 0.3554 0.1814 0.2928 0.0141  -0.1019 0.0633  64  PHE B CA  
1259 C  C   . PHE B 64  ? 0.3157 0.2497 0.3707 0.0628  0.0242  0.0050  64  PHE B C   
1260 O  O   . PHE B 64  ? 0.4344 0.3196 0.3738 -0.0027 -0.0216 -0.0360 64  PHE B O   
1261 C  CB  . PHE B 64  ? 0.3326 0.2420 0.2722 -0.0135 -0.0749 -0.0319 64  PHE B CB  
1262 C  CG  . PHE B 64  ? 0.2742 0.2619 0.2746 -0.0035 -0.0362 -0.0856 64  PHE B CG  
1263 C  CD1 . PHE B 64  ? 0.3430 0.2967 0.2638 0.0326  -0.1024 -0.0533 64  PHE B CD1 
1264 C  CD2 . PHE B 64  ? 0.2882 0.4322 0.4617 -0.0377 -0.0883 0.1048  64  PHE B CD2 
1265 C  CE1 . PHE B 64  ? 0.3183 0.3638 0.2501 -0.0235 -0.0527 0.0102  64  PHE B CE1 
1266 C  CE2 . PHE B 64  ? 0.5269 0.6193 0.3359 -0.1242 -0.1170 -0.0335 64  PHE B CE2 
1267 C  CZ  . PHE B 64  ? 0.2987 0.4194 0.2589 0.0320  -0.1078 -0.0520 64  PHE B CZ  
1268 N  N   . VAL B 65  ? 0.2681 0.0884 0.3015 0.0151  -0.0980 -0.0082 65  VAL B N   
1269 C  CA  . VAL B 65  ? 0.2806 0.0601 0.3078 0.0044  -0.0661 0.0948  65  VAL B CA  
1270 C  C   . VAL B 65  ? 0.3097 0.1649 0.4138 0.0598  -0.1536 -0.0511 65  VAL B C   
1271 O  O   . VAL B 65  ? 0.3380 0.1698 0.3281 0.0447  -0.1358 -0.0049 65  VAL B O   
1272 C  CB  . VAL B 65  ? 0.2889 0.1796 0.2837 0.0413  -0.0605 0.0435  65  VAL B CB  
1273 C  CG1 . VAL B 65  ? 0.3646 0.3337 0.2220 0.0685  -0.0465 -0.0110 65  VAL B CG1 
1274 C  CG2 . VAL B 65  ? 0.3131 0.1958 0.4054 -0.0585 -0.1624 0.0973  65  VAL B CG2 
1275 N  N   . GLU B 66  ? 0.3154 0.1438 0.2620 0.0446  -0.1079 -0.0434 66  GLU B N   
1276 C  CA  . GLU B 66  ? 0.2760 0.2367 0.2775 0.0447  -0.0641 -0.0553 66  GLU B CA  
1277 C  C   . GLU B 66  ? 0.2816 0.2320 0.2703 0.0434  -0.1175 0.0258  66  GLU B C   
1278 O  O   . GLU B 66  ? 0.3286 0.3390 0.3351 0.0669  -0.1462 0.0320  66  GLU B O   
1279 C  CB  . GLU B 66  ? 0.3085 0.2113 0.3287 0.0269  -0.1150 0.0650  66  GLU B CB  
1280 C  CG  . GLU B 66  ? 0.3295 0.2591 0.3427 0.0021  -0.1169 0.0564  66  GLU B CG  
1281 C  CD  . GLU B 66  ? 0.3123 0.3200 0.3801 -0.0154 -0.0471 -0.0387 66  GLU B CD  
1282 O  OE1 . GLU B 66  ? 0.3712 0.2833 0.3476 0.0219  -0.1188 -0.0168 66  GLU B OE1 
1283 O  OE2 . GLU B 66  ? 0.4042 0.3157 0.5669 -0.0626 -0.1930 0.0906  66  GLU B OE2 
1284 N  N   . GLY B 67  ? 0.2498 0.2662 0.2714 0.0570  -0.0778 0.0645  67  GLY B N   
1285 C  CA  . GLY B 67  ? 0.2407 0.2866 0.3637 0.1120  -0.0316 0.0498  67  GLY B CA  
1286 C  C   . GLY B 67  ? 0.2319 0.2818 0.3398 0.1090  -0.0237 0.0501  67  GLY B C   
1287 O  O   . GLY B 67  ? 0.2631 0.2156 0.3398 0.0306  -0.0780 0.0512  67  GLY B O   
1288 N  N   . ILE B 68  ? 0.2816 0.2072 0.2747 0.0725  -0.0820 -0.0087 68  ILE B N   
1289 C  CA  . ILE B 68  ? 0.2701 0.1863 0.2210 0.0560  -0.0671 -0.0013 68  ILE B CA  
1290 C  C   . ILE B 68  ? 0.1887 0.1780 0.2633 -0.0056 -0.0589 0.0075  68  ILE B C   
1291 O  O   . ILE B 68  ? 0.1981 0.1907 0.3048 0.0379  -0.0672 -0.0183 68  ILE B O   
1292 C  CB  . ILE B 68  ? 0.2473 0.1786 0.2710 0.0264  -0.0299 0.0076  68  ILE B CB  
1293 C  CG1 . ILE B 68  ? 0.3699 0.2010 0.3215 0.0021  -0.0109 -0.0062 68  ILE B CG1 
1294 C  CG2 . ILE B 68  ? 0.2412 0.2508 0.2404 0.0319  -0.0196 0.0178  68  ILE B CG2 
1295 C  CD1 . ILE B 68  ? 0.4597 0.2374 0.3054 -0.0033 -0.0240 -0.0636 68  ILE B CD1 
1296 N  N   . TYR B 69  ? 0.2091 0.1882 0.2512 0.0104  -0.0572 0.0127  69  TYR B N   
1297 C  CA  . TYR B 69  ? 0.1719 0.1861 0.2410 0.0049  -0.0687 0.0166  69  TYR B CA  
1298 C  C   . TYR B 69  ? 0.1973 0.1636 0.2110 0.0142  -0.0509 -0.0011 69  TYR B C   
1299 O  O   . TYR B 69  ? 0.2049 0.1492 0.2849 -0.0126 -0.0474 0.0139  69  TYR B O   
1300 C  CB  . TYR B 69  ? 0.2147 0.1308 0.2240 0.0243  -0.0507 0.0009  69  TYR B CB  
1301 C  CG  . TYR B 69  ? 0.2579 0.1449 0.2196 -0.0097 -0.0647 0.0402  69  TYR B CG  
1302 C  CD1 . TYR B 69  ? 0.2281 0.1416 0.2552 0.0009  -0.0807 0.0294  69  TYR B CD1 
1303 C  CD2 . TYR B 69  ? 0.2732 0.1675 0.2565 0.0317  -0.0857 0.0199  69  TYR B CD2 
1304 C  CE1 . TYR B 69  ? 0.2616 0.1801 0.2970 0.0649  -0.1157 0.0322  69  TYR B CE1 
1305 C  CE2 . TYR B 69  ? 0.2641 0.1733 0.2915 0.0023  -0.0958 0.0468  69  TYR B CE2 
1306 C  CZ  . TYR B 69  ? 0.2518 0.1924 0.2993 0.0338  -0.0925 0.0475  69  TYR B CZ  
1307 O  OH  . TYR B 69  ? 0.2904 0.2301 0.3311 0.0423  -0.1129 0.0386  69  TYR B OH  
1308 N  N   . LYS B 70  ? 0.1857 0.1750 0.2208 -0.0028 -0.0619 -0.0089 70  LYS B N   
1309 C  CA  . LYS B 70  ? 0.1983 0.1667 0.2150 -0.0045 -0.0446 0.0013  70  LYS B CA  
1310 C  C   . LYS B 70  ? 0.2130 0.1926 0.2023 -0.0216 -0.0646 -0.0102 70  LYS B C   
1311 O  O   . LYS B 70  ? 0.2171 0.1950 0.2485 0.0190  -0.0850 -0.0607 70  LYS B O   
1312 C  CB  . LYS B 70  ? 0.2559 0.1111 0.2696 0.0142  0.0092  0.0000  70  LYS B CB  
1313 C  CG  . LYS B 70  ? 0.3238 0.1147 0.2793 -0.0034 0.0244  0.0292  70  LYS B CG  
1314 C  CD  . LYS B 70  ? 0.3675 0.2363 0.3392 -0.0259 0.0281  0.1212  70  LYS B CD  
1315 C  CE  . LYS B 70  ? 0.2647 0.3125 0.3072 -0.0131 0.0997  0.0059  70  LYS B CE  
1316 N  NZ  . LYS B 70  ? 0.3258 0.3833 0.4056 -0.0227 0.0992  0.1026  70  LYS B NZ  
1317 N  N   . VAL B 71  ? 0.2047 0.1463 0.2279 0.0133  -0.0367 0.0092  71  VAL B N   
1318 C  CA  . VAL B 71  ? 0.1936 0.1538 0.2220 0.0351  -0.0444 -0.0032 71  VAL B CA  
1319 C  C   . VAL B 71  ? 0.2196 0.1551 0.1745 -0.0139 -0.0225 -0.0001 71  VAL B C   
1320 O  O   . VAL B 71  ? 0.2402 0.1824 0.2351 0.0160  -0.0631 0.0158  71  VAL B O   
1321 C  CB  . VAL B 71  ? 0.1992 0.1711 0.1996 0.0246  -0.0408 0.0022  71  VAL B CB  
1322 C  CG1 . VAL B 71  ? 0.2629 0.2283 0.1890 -0.0016 -0.0160 -0.0300 71  VAL B CG1 
1323 C  CG2 . VAL B 71  ? 0.2495 0.1254 0.2645 -0.0016 -0.0483 -0.0107 71  VAL B CG2 
1324 N  N   . GLU B 72  ? 0.2417 0.1177 0.2411 0.0018  -0.0309 0.0027  72  GLU B N   
1325 C  CA  . GLU B 72  ? 0.2622 0.1509 0.2372 0.0408  -0.0089 -0.0014 72  GLU B CA  
1326 C  C   . GLU B 72  ? 0.2573 0.1957 0.1616 0.0447  -0.0012 0.0146  72  GLU B C   
1327 O  O   . GLU B 72  ? 0.2547 0.1586 0.2055 0.0669  -0.0344 0.0294  72  GLU B O   
1328 C  CB  . GLU B 72  ? 0.2514 0.2371 0.3020 0.0256  -0.0009 0.0069  72  GLU B CB  
1329 C  CG  . GLU B 72  ? 0.2465 0.2830 0.3772 0.0064  0.0366  0.0764  72  GLU B CG  
1330 C  CD  . GLU B 72  ? 0.3036 0.2765 0.5492 -0.0181 0.1160  0.1649  72  GLU B CD  
1331 O  OE1 . GLU B 72  ? 0.3907 0.2582 0.5171 0.0564  0.2104  0.0637  72  GLU B OE1 
1332 O  OE2 . GLU B 72  ? 0.3164 0.2641 0.4614 -0.1097 -0.0063 0.0965  72  GLU B OE2 
1333 N  N   . ILE B 73  ? 0.2595 0.1587 0.1713 0.0398  0.0142  0.0252  73  ILE B N   
1334 C  CA  . ILE B 73  ? 0.2045 0.1841 0.1641 0.0385  -0.0148 0.0196  73  ILE B CA  
1335 C  C   . ILE B 73  ? 0.2391 0.1955 0.1778 0.0269  -0.0260 0.0204  73  ILE B C   
1336 O  O   . ILE B 73  ? 0.2250 0.1610 0.1889 0.0196  -0.0147 0.0077  73  ILE B O   
1337 C  CB  . ILE B 73  ? 0.2246 0.1917 0.1833 0.0148  -0.0246 0.0248  73  ILE B CB  
1338 C  CG1 . ILE B 73  ? 0.2650 0.2160 0.2027 -0.0496 -0.0403 0.0234  73  ILE B CG1 
1339 C  CG2 . ILE B 73  ? 0.2698 0.1896 0.1521 0.0091  0.0073  0.0397  73  ILE B CG2 
1340 C  CD1 . ILE B 73  ? 0.2436 0.2209 0.2854 -0.0112 -0.0171 0.0281  73  ILE B CD1 
1341 N  N   . ASP B 74  ? 0.2099 0.1784 0.1771 -0.0023 -0.0150 0.0345  74  ASP B N   
1342 C  CA  . ASP B 74  ? 0.2381 0.1450 0.2071 -0.0076 -0.0033 0.0234  74  ASP B CA  
1343 C  C   . ASP B 74  ? 0.2416 0.1147 0.1904 0.0181  0.0076  -0.0045 74  ASP B C   
1344 O  O   . ASP B 74  ? 0.1919 0.1573 0.2375 0.0069  -0.0124 0.0030  74  ASP B O   
1345 C  CB  . ASP B 74  ? 0.2181 0.2000 0.2651 0.0197  -0.0457 0.0055  74  ASP B CB  
1346 C  CG  . ASP B 74  ? 0.2257 0.2602 0.2829 -0.0313 -0.0276 0.0389  74  ASP B CG  
1347 O  OD1 . ASP B 74  ? 0.2301 0.2165 0.3248 0.0188  -0.0467 0.0638  74  ASP B OD1 
1348 O  OD2 . ASP B 74  ? 0.3100 0.2057 0.4424 -0.0373 -0.0731 0.0527  74  ASP B OD2 
1349 N  N   . THR B 75  ? 0.1846 0.1482 0.2007 -0.0183 -0.0218 0.0183  75  THR B N   
1350 C  CA  . THR B 75  ? 0.1851 0.1568 0.1786 -0.0433 -0.0273 0.0337  75  THR B CA  
1351 C  C   . THR B 75  ? 0.1763 0.1546 0.1775 0.0213  0.0308  0.0332  75  THR B C   
1352 O  O   . THR B 75  ? 0.1756 0.1214 0.2334 0.0067  -0.0194 0.0162  75  THR B O   
1353 C  CB  . THR B 75  ? 0.1933 0.1666 0.1926 -0.0053 0.0040  0.0306  75  THR B CB  
1354 O  OG1 . THR B 75  ? 0.1731 0.1784 0.2065 0.0140  0.0057  -0.0159 75  THR B OG1 
1355 C  CG2 . THR B 75  ? 0.1804 0.1694 0.2399 0.0152  -0.0031 0.0560  75  THR B CG2 
1356 N  N   . LYS B 76  ? 0.1869 0.1303 0.2316 0.0129  0.0248  0.0292  76  LYS B N   
1357 C  CA  . LYS B 76  ? 0.1873 0.1695 0.2380 0.0167  -0.0171 0.0775  76  LYS B CA  
1358 C  C   . LYS B 76  ? 0.1841 0.1824 0.2393 -0.0053 -0.0125 0.0766  76  LYS B C   
1359 O  O   . LYS B 76  ? 0.2063 0.1611 0.2645 0.0038  -0.0203 0.0400  76  LYS B O   
1360 C  CB  . LYS B 76  ? 0.2050 0.1403 0.2576 0.0153  -0.0056 0.0205  76  LYS B CB  
1361 C  CG  . LYS B 76  ? 0.2732 0.2362 0.2519 -0.0273 0.0357  0.0736  76  LYS B CG  
1362 C  CD  . LYS B 76  ? 0.3376 0.2152 0.2830 -0.0214 0.1054  0.0330  76  LYS B CD  
1363 C  CE  . LYS B 76  ? 0.3951 0.3051 0.3860 -0.0406 0.1081  0.0719  76  LYS B CE  
1364 N  NZ  . LYS B 76  ? 0.3813 0.3011 0.5397 0.0280  0.1619  0.1064  76  LYS B NZ  
1365 N  N   . SER B 77  ? 0.1878 0.1628 0.2501 -0.0052 0.0057  0.0176  77  SER B N   
1366 C  CA  . SER B 77  ? 0.2696 0.1564 0.2128 -0.0201 0.0009  0.0396  77  SER B CA  
1367 C  C   . SER B 77  ? 0.2374 0.1511 0.2617 0.0008  0.0075  -0.0077 77  SER B C   
1368 O  O   . SER B 77  ? 0.2296 0.1483 0.2815 -0.0157 -0.0031 0.0161  77  SER B O   
1369 C  CB  . SER B 77  ? 0.2503 0.1808 0.2278 -0.0079 -0.0066 0.0213  77  SER B CB  
1370 O  OG  . SER B 77  ? 0.2341 0.3133 0.3748 0.0022  -0.0311 0.0212  77  SER B OG  
1371 N  N   . TYR B 78  ? 0.1822 0.1626 0.2694 0.0049  -0.0223 0.0582  78  TYR B N   
1372 C  CA  . TYR B 78  ? 0.2185 0.1045 0.2188 0.0155  0.0036  0.0138  78  TYR B CA  
1373 C  C   . TYR B 78  ? 0.1860 0.1074 0.2607 0.0223  0.0087  0.0072  78  TYR B C   
1374 O  O   . TYR B 78  ? 0.2208 0.1261 0.3016 0.0285  -0.0024 -0.0339 78  TYR B O   
1375 C  CB  . TYR B 78  ? 0.2151 0.1277 0.2445 -0.0290 -0.0412 0.0217  78  TYR B CB  
1376 C  CG  . TYR B 78  ? 0.2441 0.1113 0.2044 -0.0232 0.0029  -0.0069 78  TYR B CG  
1377 C  CD1 . TYR B 78  ? 0.1955 0.1696 0.2134 -0.0201 -0.0378 -0.0042 78  TYR B CD1 
1378 C  CD2 . TYR B 78  ? 0.1990 0.1341 0.2337 0.0177  -0.0176 -0.0214 78  TYR B CD2 
1379 C  CE1 . TYR B 78  ? 0.2357 0.1835 0.2068 -0.0180 0.0095  -0.0452 78  TYR B CE1 
1380 C  CE2 . TYR B 78  ? 0.2064 0.1346 0.1982 -0.0044 -0.0304 0.0220  78  TYR B CE2 
1381 C  CZ  . TYR B 78  ? 0.1867 0.1820 0.2384 -0.0564 0.0086  0.0193  78  TYR B CZ  
1382 O  OH  . TYR B 78  ? 0.2400 0.1457 0.2211 -0.0264 0.0112  0.0030  78  TYR B OH  
1383 N  N   . TRP B 79  ? 0.1785 0.1229 0.2524 0.0137  -0.0200 0.0450  79  TRP B N   
1384 C  CA  . TRP B 79  ? 0.1847 0.1349 0.2859 -0.0123 -0.0277 0.0638  79  TRP B CA  
1385 C  C   . TRP B 79  ? 0.2458 0.0853 0.3258 0.0438  0.0081  -0.0083 79  TRP B C   
1386 O  O   . TRP B 79  ? 0.2478 0.1221 0.3619 0.0505  -0.0689 -0.0099 79  TRP B O   
1387 C  CB  . TRP B 79  ? 0.1353 0.1472 0.2959 -0.0036 0.0056  0.0761  79  TRP B CB  
1388 C  CG  . TRP B 79  ? 0.1719 0.1304 0.2180 0.0049  -0.0231 0.0326  79  TRP B CG  
1389 C  CD1 . TRP B 79  ? 0.1784 0.1442 0.2006 0.0095  0.0164  0.0384  79  TRP B CD1 
1390 C  CD2 . TRP B 79  ? 0.1800 0.1401 0.1964 0.0240  0.0039  -0.0165 79  TRP B CD2 
1391 N  NE1 . TRP B 79  ? 0.1676 0.1184 0.1927 0.0261  0.0070  0.0285  79  TRP B NE1 
1392 C  CE2 . TRP B 79  ? 0.1687 0.1479 0.1643 0.0051  -0.0059 0.0036  79  TRP B CE2 
1393 C  CE3 . TRP B 79  ? 0.1640 0.1896 0.2538 0.0176  0.0112  -0.0452 79  TRP B CE3 
1394 C  CZ2 . TRP B 79  ? 0.1865 0.1362 0.1748 0.0035  -0.0070 -0.0115 79  TRP B CZ2 
1395 C  CZ3 . TRP B 79  ? 0.1356 0.1897 0.3123 0.0459  -0.0037 -0.0285 79  TRP B CZ3 
1396 C  CH2 . TRP B 79  ? 0.2004 0.1901 0.2304 -0.0180 0.0455  -0.0201 79  TRP B CH2 
1397 N  N   . LYS B 80  ? 0.2800 0.0741 0.3420 0.0059  -0.0252 0.0732  80  LYS B N   
1398 C  CA  . LYS B 80  ? 0.3195 0.0831 0.3748 -0.0012 0.0106  0.1293  80  LYS B CA  
1399 C  C   . LYS B 80  ? 0.2583 0.2271 0.3335 -0.0321 -0.0454 0.0381  80  LYS B C   
1400 O  O   . LYS B 80  ? 0.2843 0.1593 0.4566 -0.0313 -0.0558 0.0271  80  LYS B O   
1401 C  CB  . LYS B 80  ? 0.3733 0.1326 0.6281 -0.0992 0.1394  -0.0158 80  LYS B CB  
1402 N  N   . ALA B 81  ? 0.3002 0.1201 0.3671 0.0047  -0.0102 0.0183  81  ALA B N   
1403 C  CA  . ALA B 81  ? 0.3588 0.1683 0.3548 0.0430  -0.0456 0.0376  81  ALA B CA  
1404 C  C   . ALA B 81  ? 0.3696 0.2361 0.4118 0.0707  -0.0302 -0.0457 81  ALA B C   
1405 O  O   . ALA B 81  ? 0.3545 0.2357 0.3728 0.0123  -0.0136 -0.0702 81  ALA B O   
1406 C  CB  . ALA B 81  ? 0.3763 0.1946 0.3293 0.0209  -0.0232 0.0296  81  ALA B CB  
1407 N  N   . LEU B 82  ? 0.2757 0.1346 0.4297 0.0119  -0.0041 0.0353  82  LEU B N   
1408 C  CA  . LEU B 82  ? 0.2672 0.1271 0.4653 -0.0050 0.0118  0.0776  82  LEU B CA  
1409 C  C   . LEU B 82  ? 0.3337 0.1267 0.4211 0.0891  -0.0531 -0.0034 82  LEU B C   
1410 O  O   . LEU B 82  ? 0.3262 0.1842 0.5945 0.0969  -0.0755 -0.0119 82  LEU B O   
1411 C  CB  . LEU B 82  ? 0.2530 0.1939 0.4727 -0.0303 0.0591  -0.0209 82  LEU B CB  
1412 C  CG  . LEU B 82  ? 0.3131 0.3108 0.5199 -0.0497 0.0532  -0.0311 82  LEU B CG  
1413 C  CD1 . LEU B 82  ? 0.5967 0.2529 0.5470 -0.0603 0.0242  0.0222  82  LEU B CD1 
1414 C  CD2 . LEU B 82  ? 0.5410 0.4127 0.5117 -0.0436 0.1562  0.0321  82  LEU B CD2 
1415 N  N   . GLY B 83  ? 0.3304 0.1659 0.3489 0.0240  -0.0890 -0.0790 83  GLY B N   
1416 C  CA  . GLY B 83  ? 0.3520 0.2266 0.4213 0.0533  -0.1666 -0.0103 83  GLY B CA  
1417 C  C   . GLY B 83  ? 0.4056 0.1745 0.2979 0.0869  -0.0616 -0.0303 83  GLY B C   
1418 O  O   . GLY B 83  ? 0.3570 0.1528 0.5171 0.0458  -0.1338 0.0156  83  GLY B O   
1419 N  N   . ILE B 84  ? 0.3601 0.1542 0.4262 0.0021  -0.1135 0.0120  84  ILE B N   
1420 C  CA  . ILE B 84  ? 0.3130 0.1421 0.3209 0.0198  -0.1322 0.1166  84  ILE B CA  
1421 C  C   . ILE B 84  ? 0.3593 0.1613 0.4148 -0.0158 -0.0863 0.0156  84  ILE B C   
1422 O  O   . ILE B 84  ? 0.3631 0.1556 0.3078 -0.0551 -0.0599 0.0814  84  ILE B O   
1423 C  CB  . ILE B 84  ? 0.3313 0.1524 0.2555 0.0376  -0.0158 0.0563  84  ILE B CB  
1424 C  CG1 . ILE B 84  ? 0.2944 0.1938 0.3818 0.0068  -0.0740 -0.0878 84  ILE B CG1 
1425 C  CG2 . ILE B 84  ? 0.2592 0.2820 0.3884 0.0243  -0.0070 -0.1043 84  ILE B CG2 
1426 C  CD1 . ILE B 84  ? 0.3043 0.3019 0.4673 0.0375  0.0126  -0.0213 84  ILE B CD1 
1427 N  N   . SER B 85  ? 0.3882 0.1399 0.4138 -0.0513 -0.1319 0.0482  85  SER B N   
1428 C  CA  . SER B 85  ? 0.3496 0.1321 0.3064 -0.0080 -0.0707 0.0767  85  SER B CA  
1429 C  C   . SER B 85  ? 0.2840 0.1395 0.3135 0.0039  -0.0839 0.0344  85  SER B C   
1430 O  O   . SER B 85  ? 0.2265 0.1944 0.3841 -0.0250 -0.0685 0.0462  85  SER B O   
1431 C  CB  . SER B 85  ? 0.4484 0.1901 0.3163 0.0757  -0.1736 0.0229  85  SER B CB  
1432 O  OG  . SER B 85  ? 0.4826 0.1940 0.3510 -0.1075 -0.0526 0.0314  85  SER B OG  
1433 N  N   . PRO B 86  ? 0.2313 0.1663 0.3360 -0.0510 -0.0449 0.0630  86  PRO B N   
1434 C  CA  . PRO B 86  ? 0.2687 0.1735 0.3151 0.0003  -0.0193 0.0243  86  PRO B CA  
1435 C  C   . PRO B 86  ? 0.2825 0.2581 0.2502 -0.0119 -0.0115 0.0943  86  PRO B C   
1436 O  O   . PRO B 86  ? 0.2989 0.2762 0.2891 -0.0080 0.0532  0.1205  86  PRO B O   
1437 C  CB  . PRO B 86  ? 0.2834 0.2800 0.3650 0.1153  0.0024  0.0790  86  PRO B CB  
1438 C  CG  . PRO B 86  ? 0.2296 0.3425 0.3537 0.0794  0.0134  0.0796  86  PRO B CG  
1439 C  CD  . PRO B 86  ? 0.2606 0.1848 0.2967 -0.0538 -0.0316 0.0753  86  PRO B CD  
1440 N  N   . PHE B 87  ? 0.1439 0.1818 0.2290 -0.0257 0.0013  0.0868  87  PHE B N   
1441 C  CA  . PHE B 87  ? 0.1698 0.2374 0.2158 -0.0013 0.0153  0.0787  87  PHE B CA  
1442 C  C   . PHE B 87  ? 0.1757 0.2352 0.1736 0.0325  0.0334  0.0591  87  PHE B C   
1443 O  O   . PHE B 87  ? 0.1436 0.2202 0.2016 -0.0187 0.0048  0.0644  87  PHE B O   
1444 C  CB  . PHE B 87  ? 0.1896 0.2470 0.2017 0.0002  0.0093  0.0798  87  PHE B CB  
1445 C  CG  . PHE B 87  ? 0.1444 0.2785 0.2112 -0.0014 -0.0252 0.0197  87  PHE B CG  
1446 C  CD1 . PHE B 87  ? 0.2038 0.3562 0.2259 -0.0582 -0.0232 0.0327  87  PHE B CD1 
1447 C  CD2 . PHE B 87  ? 0.2057 0.2516 0.1764 -0.0554 0.0011  0.0307  87  PHE B CD2 
1448 C  CE1 . PHE B 87  ? 0.2309 0.3249 0.2103 -0.0516 -0.0231 0.0443  87  PHE B CE1 
1449 C  CE2 . PHE B 87  ? 0.2081 0.3197 0.2201 -0.0534 -0.0153 -0.0188 87  PHE B CE2 
1450 C  CZ  . PHE B 87  ? 0.1520 0.3060 0.2664 -0.0478 0.0362  0.0027  87  PHE B CZ  
1451 N  N   . HIS B 88  ? 0.1287 0.2400 0.2036 0.0081  0.0036  0.0640  88  HIS B N   
1452 C  CA  . HIS B 88  ? 0.1357 0.2003 0.1937 0.0455  0.0101  0.0297  88  HIS B CA  
1453 C  C   . HIS B 88  ? 0.1842 0.1476 0.1638 0.0236  0.0173  0.0018  88  HIS B C   
1454 O  O   . HIS B 88  ? 0.1755 0.1994 0.1861 0.0535  -0.0002 -0.0021 88  HIS B O   
1455 C  CB  . HIS B 88  ? 0.1880 0.1566 0.2172 0.0505  -0.0160 0.0090  88  HIS B CB  
1456 C  CG  . HIS B 88  ? 0.1252 0.2025 0.2363 0.0137  0.0193  0.0439  88  HIS B CG  
1457 N  ND1 . HIS B 88  ? 0.1427 0.2074 0.2236 0.0164  0.0315  0.0356  88  HIS B ND1 
1458 C  CD2 . HIS B 88  ? 0.1429 0.2003 0.3642 0.0217  -0.0064 -0.0174 88  HIS B CD2 
1459 C  CE1 . HIS B 88  ? 0.1315 0.1808 0.3070 0.0256  0.0292  0.0329  88  HIS B CE1 
1460 N  NE2 . HIS B 88  ? 0.1454 0.2165 0.4355 0.0337  -0.0217 -0.0445 88  HIS B NE2 
1461 N  N   . GLU B 89  ? 0.1715 0.1751 0.1686 0.0533  0.0060  -0.0284 89  GLU B N   
1462 C  CA  . GLU B 89  ? 0.1901 0.1289 0.1844 0.0597  -0.0149 -0.0228 89  GLU B CA  
1463 C  C   . GLU B 89  ? 0.2061 0.1947 0.1939 0.0725  -0.0196 -0.0205 89  GLU B C   
1464 O  O   . GLU B 89  ? 0.3297 0.2190 0.2071 0.0794  -0.0467 -0.0183 89  GLU B O   
1465 C  CB  . GLU B 89  ? 0.1750 0.1774 0.2187 0.0405  -0.0289 -0.0167 89  GLU B CB  
1466 C  CG  . GLU B 89  ? 0.1925 0.2212 0.2148 0.0576  -0.0061 -0.0036 89  GLU B CG  
1467 C  CD  . GLU B 89  ? 0.2267 0.2626 0.2341 -0.0469 0.0218  -0.0171 89  GLU B CD  
1468 O  OE1 . GLU B 89  ? 0.2733 0.3111 0.3171 -0.0393 -0.0464 0.0133  89  GLU B OE1 
1469 O  OE2 . GLU B 89  ? 0.2587 0.2748 0.3346 -0.0102 0.0531  0.0580  89  GLU B OE2 
1470 N  N   . HIS B 90  ? 0.2079 0.1757 0.1789 0.0427  -0.0321 0.0197  90  HIS B N   
1471 C  CA  . HIS B 90  ? 0.2240 0.1690 0.1801 0.0501  -0.0434 0.0060  90  HIS B CA  
1472 C  C   . HIS B 90  ? 0.2445 0.1666 0.1663 0.0489  -0.0090 0.0027  90  HIS B C   
1473 O  O   . HIS B 90  ? 0.3890 0.2361 0.1558 0.0394  -0.0308 0.0354  90  HIS B O   
1474 C  CB  . HIS B 90  ? 0.2227 0.2912 0.2408 0.0104  -0.0681 0.0007  90  HIS B CB  
1475 C  CG  . HIS B 90  ? 0.2286 0.3847 0.3284 0.0697  -0.0943 0.0702  90  HIS B CG  
1476 N  ND1 . HIS B 90  ? 0.3505 0.4989 0.4612 0.1424  0.0398  0.0467  90  HIS B ND1 
1477 C  CD2 . HIS B 90  ? 0.2663 0.4134 0.3695 0.0847  -0.0475 0.0331  90  HIS B CD2 
1478 C  CE1 . HIS B 90  ? 0.2832 0.4854 0.3489 0.1929  0.0154  -0.0451 90  HIS B CE1 
1479 N  NE2 . HIS B 90  ? 0.3498 0.6067 0.5830 0.1314  -0.0619 -0.0898 90  HIS B NE2 
1480 N  N   . ALA B 91  ? 0.3002 0.2193 0.1479 -0.0011 -0.0457 0.0062  91  ALA B N   
1481 C  CA  . ALA B 91  ? 0.3495 0.2285 0.1670 -0.0170 -0.0788 0.0313  91  ALA B CA  
1482 C  C   . ALA B 91  ? 0.4192 0.1842 0.2351 0.0137  -0.0818 0.0580  91  ALA B C   
1483 O  O   . ALA B 91  ? 0.4063 0.1921 0.2679 0.0673  -0.1034 0.0041  91  ALA B O   
1484 C  CB  . ALA B 91  ? 0.3508 0.2511 0.2496 -0.0432 -0.0617 0.0796  91  ALA B CB  
1485 N  N   . GLU B 92  ? 0.3757 0.2594 0.2426 0.0136  -0.0625 0.0689  92  GLU B N   
1486 C  CA  . GLU B 92  ? 0.2999 0.1967 0.2586 0.0383  0.0153  0.0492  92  GLU B CA  
1487 C  C   . GLU B 92  ? 0.4035 0.2648 0.2363 -0.0284 -0.1247 0.0257  92  GLU B C   
1488 O  O   . GLU B 92  ? 0.7430 0.3447 0.2605 -0.0560 -0.1583 0.0264  92  GLU B O   
1489 C  CB  . GLU B 92  ? 0.3275 0.3080 0.4627 -0.0147 0.0392  0.0206  92  GLU B CB  
1490 C  CG  . GLU B 92  ? 0.2850 0.3021 0.4581 -0.0038 0.0745  0.0622  92  GLU B CG  
1491 C  CD  . GLU B 92  ? 0.3547 0.2774 0.4364 -0.0571 0.0410  -0.1008 92  GLU B CD  
1492 O  OE1 . GLU B 92  ? 0.3679 0.3311 0.2804 -0.0291 0.0447  0.1045  92  GLU B OE1 
1493 O  OE2 . GLU B 92  ? 0.2715 0.4251 0.6789 0.0179  0.0266  -0.0764 92  GLU B OE2 
1494 N  N   . VAL B 93  ? 0.2461 0.1607 0.2515 0.0468  -0.0587 0.0056  93  VAL B N   
1495 C  CA  . VAL B 93  ? 0.2054 0.2176 0.2042 0.0128  -0.0760 0.0254  93  VAL B CA  
1496 C  C   . VAL B 93  ? 0.1981 0.1586 0.1339 0.0137  -0.0186 0.0299  93  VAL B C   
1497 O  O   . VAL B 93  ? 0.2265 0.1576 0.2046 0.0159  -0.0620 -0.0086 93  VAL B O   
1498 C  CB  . VAL B 93  ? 0.2075 0.1733 0.2648 -0.0072 -0.0543 0.0038  93  VAL B CB  
1499 C  CG1 . VAL B 93  ? 0.2827 0.1326 0.2704 -0.0149 0.0392  -0.0297 93  VAL B CG1 
1500 C  CG2 . VAL B 93  ? 0.2192 0.2808 0.2788 0.0132  -0.0344 0.0325  93  VAL B CG2 
1501 N  N   . VAL B 94  ? 0.1787 0.1751 0.1897 0.0096  -0.0477 0.0096  94  VAL B N   
1502 C  CA  . VAL B 94  ? 0.1987 0.1463 0.1914 -0.0017 -0.0317 0.0235  94  VAL B CA  
1503 C  C   . VAL B 94  ? 0.2096 0.1691 0.1999 -0.0447 -0.0347 -0.0010 94  VAL B C   
1504 O  O   . VAL B 94  ? 0.2185 0.1783 0.1721 0.0103  -0.0509 0.0053  94  VAL B O   
1505 C  CB  . VAL B 94  ? 0.2096 0.1736 0.2357 0.0004  -0.0139 -0.0046 94  VAL B CB  
1506 C  CG1 . VAL B 94  ? 0.1929 0.2252 0.3015 -0.0281 0.0150  -0.0363 94  VAL B CG1 
1507 C  CG2 . VAL B 94  ? 0.2576 0.2340 0.2823 -0.0370 -0.0018 -0.0604 94  VAL B CG2 
1508 N  N   . PHE B 95  ? 0.1959 0.2250 0.2183 -0.0210 -0.0416 0.0063  95  PHE B N   
1509 C  CA  . PHE B 95  ? 0.2251 0.1680 0.1715 0.0057  -0.0620 0.0040  95  PHE B CA  
1510 C  C   . PHE B 95  ? 0.2088 0.1642 0.1800 0.0059  -0.0564 0.0087  95  PHE B C   
1511 O  O   . PHE B 95  ? 0.2000 0.1891 0.2550 -0.0007 -0.0346 0.0166  95  PHE B O   
1512 C  CB  . PHE B 95  ? 0.2439 0.1701 0.2621 0.0094  -0.0474 0.0407  95  PHE B CB  
1513 C  CG  . PHE B 95  ? 0.1997 0.2221 0.2580 0.0414  -0.0125 0.0055  95  PHE B CG  
1514 C  CD1 . PHE B 95  ? 0.2422 0.2337 0.2823 0.0152  -0.0108 -0.0184 95  PHE B CD1 
1515 C  CD2 . PHE B 95  ? 0.2307 0.2957 0.2316 -0.0271 -0.0705 -0.0521 95  PHE B CD2 
1516 C  CE1 . PHE B 95  ? 0.2347 0.2439 0.3461 -0.0652 -0.0055 -0.0794 95  PHE B CE1 
1517 C  CE2 . PHE B 95  ? 0.3194 0.3151 0.2146 0.0247  -0.0073 -0.0469 95  PHE B CE2 
1518 C  CZ  . PHE B 95  ? 0.2407 0.3097 0.2907 0.0096  0.0112  -0.1235 95  PHE B CZ  
1519 N  N   . THR B 96  ? 0.2968 0.1735 0.2863 -0.0042 -0.0906 0.0120  96  THR B N   
1520 C  CA  . THR B 96  ? 0.2802 0.2164 0.2624 0.0526  -0.0585 0.0017  96  THR B CA  
1521 C  C   . THR B 96  ? 0.2705 0.2637 0.3042 0.0430  -0.0451 -0.0234 96  THR B C   
1522 O  O   . THR B 96  ? 0.3189 0.2812 0.2892 0.0041  -0.0464 0.1085  96  THR B O   
1523 C  CB  . THR B 96  ? 0.3487 0.1452 0.3260 0.0250  -0.0162 0.0136  96  THR B CB  
1524 O  OG1 . THR B 96  ? 0.3105 0.2711 0.3089 0.0136  -0.0172 0.0061  96  THR B OG1 
1525 C  CG2 . THR B 96  ? 0.4251 0.1385 0.3694 0.0905  -0.0510 -0.0307 96  THR B CG2 
1526 N  N   . ALA B 97  ? 0.2804 0.2020 0.3140 -0.0391 -0.0397 0.0515  97  ALA B N   
1527 C  CA  . ALA B 97  ? 0.2226 0.2659 0.2993 0.0025  -0.0943 0.0648  97  ALA B CA  
1528 C  C   . ALA B 97  ? 0.3204 0.3244 0.4964 -0.0003 -0.1447 0.2087  97  ALA B C   
1529 O  O   . ALA B 97  ? 0.3457 0.2399 0.3880 -0.0227 -0.1348 0.0735  97  ALA B O   
1530 C  CB  . ALA B 97  ? 0.3604 0.5142 0.2579 -0.0656 -0.1078 -0.0028 97  ALA B CB  
1531 N  N   . ASN B 98  ? 0.3364 0.2854 0.4688 0.0186  -0.0636 0.0567  98  ASN B N   
1532 C  CA  . ASN B 98  ? 0.3982 0.3197 0.4158 0.0170  -0.1240 -0.0196 98  ASN B CA  
1533 C  C   . ASN B 98  ? 0.4936 0.2884 0.4381 0.1052  -0.0920 0.0591  98  ASN B C   
1534 O  O   . ASN B 98  ? 0.4875 0.2715 0.4289 0.0674  -0.0167 0.0789  98  ASN B O   
1535 C  CB  . ASN B 98  ? 0.5478 0.2289 0.4612 -0.0851 -0.1637 0.0257  98  ASN B CB  
1536 C  CG  . ASN B 98  ? 0.6335 0.3178 0.3566 -0.0540 -0.0666 0.0129  98  ASN B CG  
1537 O  OD1 . ASN B 98  ? 0.7502 0.5548 0.6858 -0.0153 -0.1780 0.2616  98  ASN B OD1 
1538 N  ND2 . ASN B 98  ? 0.8989 0.6085 0.5396 -0.0797 -0.2532 -0.0931 98  ASN B ND2 
1539 N  N   . ASP B 99  ? 0.3762 0.4319 0.4116 0.0171  -0.0978 0.1057  99  ASP B N   
1540 C  CA  . ASP B 99  ? 0.3471 0.4550 0.3714 -0.0834 -0.1616 0.0099  99  ASP B CA  
1541 C  C   . ASP B 99  ? 0.6357 0.5015 0.6987 -0.1927 -0.1990 0.1284  99  ASP B C   
1542 O  O   . ASP B 99  ? 0.6037 0.3246 0.7940 -0.1662 -0.1464 0.1249  99  ASP B O   
1543 C  CB  . ASP B 99  ? 0.3753 0.2541 0.4487 -0.0242 -0.1501 0.1405  99  ASP B CB  
1544 C  CG  . ASP B 99  ? 0.3389 0.4141 0.5042 -0.0364 -0.1313 0.0279  99  ASP B CG  
1545 O  OD1 . ASP B 99  ? 0.5577 0.4588 0.6609 0.0506  0.0519  0.0314  99  ASP B OD1 
1546 O  OD2 . ASP B 99  ? 0.3190 0.3646 0.4928 0.0046  -0.1002 0.0934  99  ASP B OD2 
1547 N  N   . ARG B 104 ? 0.3964 0.3066 0.3254 0.0239  -0.1230 0.1155  104 ARG B N   
1548 C  CA  . ARG B 104 ? 0.3810 0.2343 0.3118 -0.0285 -0.0815 0.0722  104 ARG B CA  
1549 C  C   . ARG B 104 ? 0.3765 0.2744 0.3477 -0.0150 -0.1371 0.0187  104 ARG B C   
1550 O  O   . ARG B 104 ? 0.3467 0.2690 0.2798 -0.0606 -0.0683 0.0897  104 ARG B O   
1551 C  CB  . ARG B 104 ? 0.5054 0.2630 0.2926 -0.0281 -0.0384 0.1135  104 ARG B CB  
1552 N  N   . TYR B 105 ? 0.3657 0.2590 0.3086 -0.0615 -0.2210 -0.0012 105 TYR B N   
1553 C  CA  . TYR B 105 ? 0.3042 0.2364 0.2520 -0.0035 -0.0843 0.0039  105 TYR B CA  
1554 C  C   . TYR B 105 ? 0.2247 0.1639 0.2380 -0.0373 -0.0767 0.0080  105 TYR B C   
1555 O  O   . TYR B 105 ? 0.3343 0.1882 0.2702 -0.0123 -0.1488 -0.0082 105 TYR B O   
1556 C  CB  . TYR B 105 ? 0.2721 0.3218 0.2838 -0.0717 -0.0517 0.0230  105 TYR B CB  
1557 C  CG  . TYR B 105 ? 0.3575 0.3170 0.2725 -0.0402 -0.0452 0.0268  105 TYR B CG  
1558 C  CD1 . TYR B 105 ? 0.4271 0.3596 0.4389 0.0458  -0.1694 -0.0457 105 TYR B CD1 
1559 C  CD2 . TYR B 105 ? 0.4907 0.3276 0.3535 -0.0036 -0.0427 -0.0185 105 TYR B CD2 
1560 C  CE1 . TYR B 105 ? 0.4089 0.2798 0.4091 0.0063  -0.0972 0.0936  105 TYR B CE1 
1561 C  CE2 . TYR B 105 ? 0.4132 0.4085 0.2948 -0.0302 -0.0162 0.0125  105 TYR B CE2 
1562 C  CZ  . TYR B 105 ? 0.3893 0.1587 0.4830 0.0175  -0.0201 -0.0093 105 TYR B CZ  
1563 O  OH  . TYR B 105 ? 0.4915 0.2065 0.5521 0.0041  0.0647  -0.0840 105 TYR B OH  
1564 N  N   . THR B 106 ? 0.2560 0.1321 0.2329 -0.0447 -0.0431 0.0077  106 THR B N   
1565 C  CA  . THR B 106 ? 0.2630 0.1223 0.1892 -0.0354 -0.0161 -0.0056 106 THR B CA  
1566 C  C   . THR B 106 ? 0.3162 0.1169 0.1723 -0.0508 -0.0254 0.0049  106 THR B C   
1567 O  O   . THR B 106 ? 0.2758 0.1531 0.2279 -0.0491 -0.0562 0.0339  106 THR B O   
1568 C  CB  . THR B 106 ? 0.3109 0.3010 0.2227 -0.0491 0.0069  0.0341  106 THR B CB  
1569 O  OG1 . THR B 106 ? 0.3487 0.2905 0.2441 -0.1286 -0.0106 -0.0094 106 THR B OG1 
1570 C  CG2 . THR B 106 ? 0.2763 0.2774 0.2420 -0.0182 0.0019  -0.0626 106 THR B CG2 
1571 N  N   . ILE B 107 ? 0.2501 0.1454 0.1581 -0.0503 -0.0527 -0.0073 107 ILE B N   
1572 C  CA  . ILE B 107 ? 0.2558 0.1377 0.1745 -0.0096 -0.0293 -0.0330 107 ILE B CA  
1573 C  C   . ILE B 107 ? 0.2502 0.1819 0.1465 -0.0034 -0.0206 -0.0300 107 ILE B C   
1574 O  O   . ILE B 107 ? 0.2977 0.1710 0.1912 0.0017  -0.0410 -0.0311 107 ILE B O   
1575 C  CB  . ILE B 107 ? 0.2878 0.2012 0.2056 -0.0136 0.0155  0.0045  107 ILE B CB  
1576 C  CG1 . ILE B 107 ? 0.2829 0.2134 0.2737 -0.0571 0.0268  -0.0056 107 ILE B CG1 
1577 C  CG2 . ILE B 107 ? 0.3477 0.1357 0.2074 -0.0236 0.0231  -0.0103 107 ILE B CG2 
1578 C  CD1 . ILE B 107 ? 0.2830 0.2043 0.3045 -0.0144 -0.0677 0.0132  107 ILE B CD1 
1579 N  N   . ALA B 108 ? 0.2400 0.1830 0.1502 0.0167  -0.0343 0.0424  108 ALA B N   
1580 C  CA  . ALA B 108 ? 0.2574 0.1960 0.1889 0.0326  0.0042  0.0371  108 ALA B CA  
1581 C  C   . ALA B 108 ? 0.3617 0.2054 0.1478 -0.0021 -0.0243 -0.0153 108 ALA B C   
1582 O  O   . ALA B 108 ? 0.3714 0.1521 0.1545 0.0170  -0.0244 0.0130  108 ALA B O   
1583 C  CB  . ALA B 108 ? 0.2769 0.2397 0.1908 0.0556  -0.0175 0.0800  108 ALA B CB  
1584 N  N   . ALA B 109 ? 0.2059 0.1565 0.1417 0.0256  -0.0126 -0.0144 109 ALA B N   
1585 C  CA  . ALA B 109 ? 0.1782 0.1646 0.1618 0.0302  0.0028  -0.0043 109 ALA B CA  
1586 C  C   . ALA B 109 ? 0.2226 0.1388 0.1892 0.0406  0.0023  0.0158  109 ALA B C   
1587 O  O   . ALA B 109 ? 0.2217 0.2213 0.1714 0.0434  -0.0174 -0.0163 109 ALA B O   
1588 C  CB  . ALA B 109 ? 0.1954 0.1833 0.2134 0.0447  -0.0164 0.0112  109 ALA B CB  
1589 N  N   . LEU B 110 ? 0.1901 0.1433 0.1392 0.0108  0.0220  0.0092  110 LEU B N   
1590 C  CA  . LEU B 110 ? 0.1601 0.1657 0.1524 0.0223  0.0187  -0.0163 110 LEU B CA  
1591 C  C   . LEU B 110 ? 0.1440 0.1692 0.1494 0.0351  0.0232  -0.0099 110 LEU B C   
1592 O  O   . LEU B 110 ? 0.1891 0.1461 0.1552 -0.0142 0.0196  0.0176  110 LEU B O   
1593 C  CB  . LEU B 110 ? 0.1602 0.1576 0.2001 0.0174  -0.0055 0.0572  110 LEU B CB  
1594 C  CG  . LEU B 110 ? 0.1863 0.1540 0.2193 0.0395  -0.0101 0.0219  110 LEU B CG  
1595 C  CD1 . LEU B 110 ? 0.2046 0.1478 0.1983 0.0146  0.0050  0.0406  110 LEU B CD1 
1596 C  CD2 . LEU B 110 ? 0.2207 0.2512 0.2241 -0.0084 -0.0545 0.0436  110 LEU B CD2 
1597 N  N   . LEU B 111 ? 0.1432 0.1339 0.1589 0.0228  0.0232  0.0001  111 LEU B N   
1598 C  CA  . LEU B 111 ? 0.1559 0.1181 0.1716 0.0104  0.0088  0.0240  111 LEU B CA  
1599 C  C   . LEU B 111 ? 0.1395 0.1433 0.1889 0.0241  0.0103  0.0008  111 LEU B C   
1600 O  O   . LEU B 111 ? 0.1444 0.1162 0.1704 0.0091  0.0205  0.0110  111 LEU B O   
1601 C  CB  . LEU B 111 ? 0.1573 0.1228 0.1493 0.0142  0.0086  0.0196  111 LEU B CB  
1602 C  CG  . LEU B 111 ? 0.1477 0.1340 0.1390 -0.0033 0.0122  0.0158  111 LEU B CG  
1603 C  CD1 . LEU B 111 ? 0.1505 0.1750 0.1853 0.0108  -0.0191 0.0060  111 LEU B CD1 
1604 C  CD2 . LEU B 111 ? 0.1671 0.0991 0.1927 -0.0074 0.0200  0.0157  111 LEU B CD2 
1605 N  N   . SER B 112 ? 0.1594 0.1234 0.1724 0.0487  0.0095  -0.0128 112 SER B N   
1606 C  CA  . SER B 112 ? 0.1546 0.1337 0.1486 0.0141  0.0199  -0.0083 112 SER B CA  
1607 C  C   . SER B 112 ? 0.1741 0.1111 0.1573 -0.0067 0.0021  0.0256  112 SER B C   
1608 O  O   . SER B 112 ? 0.1538 0.1420 0.1873 -0.0100 0.0024  0.0238  112 SER B O   
1609 C  CB  . SER B 112 ? 0.1559 0.1584 0.1654 -0.0077 0.0018  0.0305  112 SER B CB  
1610 O  OG  . SER B 112 ? 0.1791 0.1762 0.1882 -0.0259 0.0132  0.0179  112 SER B OG  
1611 N  N   . PRO B 113 ? 0.1246 0.1358 0.1821 0.0281  0.0246  0.0121  113 PRO B N   
1612 C  CA  . PRO B 113 ? 0.1266 0.1484 0.1709 -0.0136 -0.0095 0.0457  113 PRO B CA  
1613 C  C   . PRO B 113 ? 0.1440 0.1260 0.1886 0.0107  -0.0177 0.0443  113 PRO B C   
1614 O  O   . PRO B 113 ? 0.1373 0.1610 0.1941 0.0194  -0.0069 0.0363  113 PRO B O   
1615 C  CB  . PRO B 113 ? 0.1636 0.1161 0.2207 -0.0325 0.0083  0.0120  113 PRO B CB  
1616 C  CG  . PRO B 113 ? 0.1959 0.0960 0.1859 0.0329  -0.0084 0.0129  113 PRO B CG  
1617 C  CD  . PRO B 113 ? 0.1794 0.0927 0.2022 0.0270  0.0233  0.0197  113 PRO B CD  
1618 N  N   . TYR B 114 ? 0.1370 0.1297 0.1647 0.0017  0.0090  0.0107  114 TYR B N   
1619 C  CA  . TYR B 114 ? 0.1153 0.1212 0.1711 0.0053  0.0010  0.0475  114 TYR B CA  
1620 C  C   . TYR B 114 ? 0.1614 0.1547 0.1678 0.0007  0.0330  0.0214  114 TYR B C   
1621 O  O   . TYR B 114 ? 0.1931 0.1310 0.1848 0.0123  0.0442  0.0390  114 TYR B O   
1622 C  CB  . TYR B 114 ? 0.1393 0.1429 0.1958 0.0120  -0.0064 0.0495  114 TYR B CB  
1623 C  CG  . TYR B 114 ? 0.1488 0.1311 0.1780 -0.0069 0.0101  0.0316  114 TYR B CG  
1624 C  CD1 . TYR B 114 ? 0.3739 0.1103 0.2250 0.0428  0.0860  0.0706  114 TYR B CD1 
1625 C  CD2 . TYR B 114 ? 0.1405 0.1494 0.1652 -0.0059 -0.0231 0.0569  114 TYR B CD2 
1626 C  CE1 . TYR B 114 ? 0.4452 0.0886 0.2327 0.0605  0.0615  0.0588  114 TYR B CE1 
1627 C  CE2 . TYR B 114 ? 0.1962 0.1710 0.2052 -0.0217 0.0120  0.0933  114 TYR B CE2 
1628 C  CZ  . TYR B 114 ? 0.2967 0.1878 0.2582 -0.0641 0.0415  0.1097  114 TYR B CZ  
1629 O  OH  . TYR B 114 ? 0.6276 0.2038 0.3275 -0.1805 -0.0236 0.1000  114 TYR B OH  
1630 N  N   . SER B 115 ? 0.1753 0.1239 0.1685 0.0154  0.0557  0.0449  115 SER B N   
1631 C  CA  . SER B 115 ? 0.1764 0.1231 0.1521 0.0053  0.0349  0.0203  115 SER B CA  
1632 C  C   . SER B 115 ? 0.1910 0.1038 0.1471 0.0083  0.0273  0.0150  115 SER B C   
1633 O  O   . SER B 115 ? 0.2190 0.1204 0.1710 0.0403  0.0455  0.0066  115 SER B O   
1634 C  CB  . SER B 115 ? 0.1814 0.1412 0.2003 0.0031  0.0195  0.0535  115 SER B CB  
1635 O  OG  . SER B 115 ? 0.2007 0.1908 0.2779 -0.0014 0.0095  0.0474  115 SER B OG  
1636 N  N   . TYR B 116 ? 0.1856 0.1319 0.1433 0.0169  0.0341  0.0306  116 TYR B N   
1637 C  CA  . TYR B 116 ? 0.1631 0.1187 0.1472 0.0045  0.0192  0.0244  116 TYR B CA  
1638 C  C   . TYR B 116 ? 0.2138 0.1404 0.0983 0.0018  0.0272  0.0093  116 TYR B C   
1639 O  O   . TYR B 116 ? 0.1592 0.1395 0.1454 0.0118  0.0157  0.0249  116 TYR B O   
1640 C  CB  . TYR B 116 ? 0.2107 0.1492 0.1630 -0.0023 -0.0121 0.0260  116 TYR B CB  
1641 C  CG  . TYR B 116 ? 0.2155 0.1909 0.2178 -0.0474 -0.0135 -0.0414 116 TYR B CG  
1642 C  CD1 . TYR B 116 ? 0.1838 0.2019 0.2740 -0.0506 -0.0058 0.0001  116 TYR B CD1 
1643 C  CD2 . TYR B 116 ? 0.2363 0.2505 0.3017 -0.1089 0.0138  -0.0424 116 TYR B CD2 
1644 C  CE1 . TYR B 116 ? 0.2269 0.3010 0.3578 -0.0824 0.0575  -0.0290 116 TYR B CE1 
1645 C  CE2 . TYR B 116 ? 0.2441 0.2356 0.3439 -0.0688 0.0211  0.0276  116 TYR B CE2 
1646 C  CZ  . TYR B 116 ? 0.1380 0.2077 0.2737 -0.0076 0.0004  -0.0471 116 TYR B CZ  
1647 O  OH  . TYR B 116 ? 0.1800 0.4403 0.4833 0.0337  0.0716  -0.0250 116 TYR B OH  
1648 N  N   . SER B 117 ? 0.1787 0.1056 0.1373 0.0205  0.0128  0.0169  117 SER B N   
1649 C  CA  A SER B 117 ? 0.1883 0.1179 0.1332 0.0459  -0.0090 0.0207  117 SER B CA  
1650 C  CA  B SER B 117 ? 0.2001 0.1132 0.1251 0.0276  -0.0035 0.0229  117 SER B CA  
1651 C  CA  C SER B 117 ? 0.1948 0.1139 0.1257 0.0277  -0.0064 0.0197  117 SER B CA  
1652 C  C   . SER B 117 ? 0.2061 0.1607 0.1296 0.0309  -0.0092 0.0346  117 SER B C   
1653 O  O   . SER B 117 ? 0.2332 0.1152 0.1480 0.0289  -0.0224 0.0149  117 SER B O   
1654 C  CB  A SER B 117 ? 0.2015 0.2814 0.1849 -0.0032 -0.0120 0.0242  117 SER B CB  
1655 C  CB  B SER B 117 ? 0.2236 0.2148 0.1988 -0.0260 0.0081  0.0088  117 SER B CB  
1656 C  CB  C SER B 117 ? 0.2030 0.2345 0.1774 -0.0233 -0.0331 -0.0230 117 SER B CB  
1657 O  OG  A SER B 117 ? 0.1945 0.3230 0.2267 0.0113  0.0366  0.0422  117 SER B OG  
1658 O  OG  B SER B 117 ? 0.2711 0.1850 0.2159 0.0029  0.0132  0.0592  117 SER B OG  
1659 O  OG  C SER B 117 ? 0.2308 0.2150 0.2005 0.0016  -0.0102 -0.0189 117 SER B OG  
1660 N  N   . THR B 118 ? 0.2073 0.1554 0.1322 0.0243  -0.0098 -0.0095 118 THR B N   
1661 C  CA  . THR B 118 ? 0.2550 0.1505 0.1561 0.0222  -0.0248 -0.0084 118 THR B CA  
1662 C  C   . THR B 118 ? 0.2558 0.1507 0.1273 0.0425  -0.0225 -0.0162 118 THR B C   
1663 O  O   . THR B 118 ? 0.3678 0.1293 0.1443 0.0237  0.0081  -0.0001 118 THR B O   
1664 C  CB  . THR B 118 ? 0.2445 0.1546 0.2095 0.0293  -0.0111 0.0156  118 THR B CB  
1665 O  OG1 . THR B 118 ? 0.2556 0.2194 0.2346 0.0323  -0.0331 0.0140  118 THR B OG1 
1666 C  CG2 . THR B 118 ? 0.1698 0.1433 0.2055 0.0098  0.0009  0.0467  118 THR B CG2 
1667 N  N   . THR B 119 ? 0.2203 0.0933 0.1794 0.0276  -0.0107 -0.0013 119 THR B N   
1668 C  CA  A THR B 119 ? 0.2019 0.1265 0.1723 -0.0177 -0.0341 0.0241  119 THR B CA  
1669 C  CA  B THR B 119 ? 0.2041 0.1210 0.1730 -0.0086 -0.0317 0.0207  119 THR B CA  
1670 C  C   . THR B 119 ? 0.1727 0.1593 0.1923 0.0019  -0.0411 0.0334  119 THR B C   
1671 O  O   . THR B 119 ? 0.2325 0.1429 0.2038 -0.0069 -0.0445 0.0457  119 THR B O   
1672 C  CB  A THR B 119 ? 0.2250 0.1257 0.2457 -0.0338 -0.0310 0.0343  119 THR B CB  
1673 C  CB  B THR B 119 ? 0.2233 0.2316 0.2536 -0.0156 -0.0757 0.0393  119 THR B CB  
1674 O  OG1 A THR B 119 ? 0.3832 0.4278 0.2766 0.0872  -0.0864 0.0226  119 THR B OG1 
1675 O  OG1 B THR B 119 ? 0.2478 0.3263 0.3279 0.0578  -0.0645 0.0005  119 THR B OG1 
1676 C  CG2 A THR B 119 ? 0.0883 0.1207 0.1465 -0.0528 -0.0451 0.0740  119 THR B CG2 
1677 C  CG2 B THR B 119 ? 0.2399 0.2798 0.2357 0.0270  -0.0273 0.0438  119 THR B CG2 
1678 N  N   . ALA B 120 ? 0.2272 0.1395 0.1873 -0.0166 -0.0363 0.0246  120 ALA B N   
1679 C  CA  . ALA B 120 ? 0.1944 0.1934 0.1767 -0.0388 -0.0599 0.0301  120 ALA B CA  
1680 C  C   . ALA B 120 ? 0.2122 0.1768 0.2039 -0.0420 -0.0597 0.0288  120 ALA B C   
1681 O  O   . ALA B 120 ? 0.2788 0.1886 0.1854 -0.0912 -0.0697 0.0643  120 ALA B O   
1682 C  CB  . ALA B 120 ? 0.2319 0.1940 0.2396 -0.0441 -0.0133 0.0621  120 ALA B CB  
1683 N  N   . VAL B 121 ? 0.2308 0.1550 0.2120 -0.0621 -0.0461 0.0463  121 VAL B N   
1684 C  CA  . VAL B 121 ? 0.2470 0.1769 0.2317 -0.0785 -0.0416 0.0298  121 VAL B CA  
1685 C  C   . VAL B 121 ? 0.2877 0.1876 0.1755 -0.0746 -0.0874 0.0218  121 VAL B C   
1686 O  O   . VAL B 121 ? 0.3511 0.2215 0.2220 -0.1122 -0.1078 0.0484  121 VAL B O   
1687 C  CB  . VAL B 121 ? 0.2545 0.3031 0.2241 -0.0302 -0.0316 0.0129  121 VAL B CB  
1688 C  CG1 . VAL B 121 ? 0.2328 0.3698 0.3797 -0.0806 -0.0766 0.0089  121 VAL B CG1 
1689 C  CG2 . VAL B 121 ? 0.3440 0.2942 0.2995 -0.0418 0.0189  0.0383  121 VAL B CG2 
1690 N  N   . VAL B 122 ? 0.3106 0.2070 0.2592 -0.0427 -0.0737 0.0430  122 VAL B N   
1691 C  CA  . VAL B 122 ? 0.3323 0.2761 0.2957 -0.0886 -0.0954 0.1007  122 VAL B CA  
1692 C  C   . VAL B 122 ? 0.3474 0.3335 0.2636 -0.0995 -0.1014 0.1238  122 VAL B C   
1693 O  O   . VAL B 122 ? 0.3452 0.2508 0.3188 -0.0174 -0.1111 0.0952  122 VAL B O   
1694 C  CB  . VAL B 122 ? 0.3650 0.3467 0.3206 -0.0220 -0.0883 0.1362  122 VAL B CB  
1695 C  CG1 . VAL B 122 ? 0.4797 0.4515 0.3810 0.1298  -0.1420 0.0985  122 VAL B CG1 
1696 C  CG2 . VAL B 122 ? 0.3800 0.4022 0.3318 -0.0415 0.0053  0.0928  122 VAL B CG2 
1697 N  N   . THR B 123 ? 0.3144 0.4732 0.4173 -0.0876 -0.1271 0.2503  123 THR B N   
1698 C  CA  . THR B 123 ? 0.3027 0.5406 0.4255 -0.0559 -0.0665 0.2539  123 THR B CA  
1699 C  C   . THR B 123 ? 0.4077 0.6836 0.3112 -0.0831 -0.1607 0.3040  123 THR B C   
1700 O  O   . THR B 123 ? 0.4131 0.4362 0.4720 -0.0596 -0.0987 0.2549  123 THR B O   
1701 C  CB  . THR B 123 ? 0.3912 0.7580 0.3661 0.0696  -0.2410 0.1168  123 THR B CB  
1702 O  OG1 . THR B 123 ? 0.6678 0.5880 0.2299 0.0248  -0.0275 0.0146  123 THR B OG1 
1703 C  CG2 . THR B 123 ? 0.3580 0.8825 0.5525 0.0625  -0.0762 0.3170  123 THR B CG2 
1704 N  N   . ASN B 124 ? 0.5626 0.6278 0.4478 -0.0530 -0.0320 0.2335  124 ASN B N   
1705 C  CA  . ASN B 124 ? 0.5248 0.6641 0.4956 0.0210  -0.1413 0.1566  124 ASN B CA  
1706 C  C   . ASN B 124 ? 0.4429 0.7271 0.5688 0.1432  0.1780  0.3565  124 ASN B C   
1707 O  O   . ASN B 124 ? 0.4423 0.8794 0.4733 0.0042  0.0601  0.1089  124 ASN B O   
1708 C  CB  . ASN B 124 ? 0.7864 0.5832 0.4969 0.0538  -0.1043 0.4286  124 ASN B CB  
1709 CA CA  . CA  C .   ? 0.3630 0.1999 0.4889 -0.0271 0.0867  -0.0749 201 CA  A CA  
1710 CA CA  . CA  D .   ? 0.7108 0.5791 0.6583 -0.0291 -0.2156 0.0151  201 CA  B CA  
1711 C  C10 . WLX E .   ? 0.2663 0.3636 0.2235 -0.0500 -0.0326 -0.0635 202 WLX B C10 
1712 C  C11 . WLX E .   ? 0.2671 0.4932 0.2745 -0.0112 0.0492  -0.0580 202 WLX B C11 
1713 N  N1  . WLX E .   ? 0.3138 0.5932 0.3263 0.0820  -0.0318 0.0477  202 WLX B N1  
1714 C  C2  . WLX E .   ? 0.2310 0.3072 0.2619 0.0192  0.0179  -0.0069 202 WLX B C2  
1715 C  C3  . WLX E .   ? 0.2876 0.3467 0.3043 0.0250  0.0283  0.0192  202 WLX B C3  
1716 C  C4  . WLX E .   ? 0.2808 0.3419 0.3529 0.0304  -0.0009 0.0007  202 WLX B C4  
1717 C  C5  . WLX E .   ? 0.2959 0.5299 0.3198 0.0691  -0.0193 0.0335  202 WLX B C5  
1718 C  C6  . WLX E .   ? 0.2957 0.4176 0.3310 0.0653  -0.0379 -0.0169 202 WLX B C6  
1719 N  N7  . WLX E .   ? 0.2325 0.3441 0.2119 0.0199  -0.0151 0.0778  202 WLX B N7  
1720 C  C8  . WLX E .   ? 0.2699 0.3500 0.3075 -0.0161 0.0024  -0.0457 202 WLX B C8  
1721 C  C9  . WLX E .   ? 0.3408 0.5633 0.3368 -0.0076 0.0175  0.0070  202 WLX B C9  
1722 O  O   . HOH F .   ? 0.3852 0.4855 0.4289 0.0138  -0.1566 -0.0100 301 HOH A O   
1723 O  O   . HOH F .   ? 0.3309 0.2675 0.5283 -0.0390 0.0402  -0.0551 302 HOH A O   
1724 O  O   . HOH F .   ? 0.2511 0.1717 0.2992 0.0211  0.0243  -0.0080 303 HOH A O   
1725 O  O   . HOH F .   ? 0.2382 0.2725 0.2445 0.0551  -0.0615 -0.0450 304 HOH A O   
1726 O  O   . HOH F .   ? 0.4421 0.2809 0.4565 0.0081  -0.0017 -0.0757 305 HOH A O   
1727 O  O   . HOH F .   ? 0.3695 0.3474 0.3250 0.0708  -0.0196 -0.0980 306 HOH A O   
1728 O  O   . HOH F .   ? 0.2464 0.1654 0.2594 0.0282  0.0057  -0.0083 307 HOH A O   
1729 O  O   . HOH F .   ? 0.2848 0.3401 0.3888 0.0070  0.0437  -0.1190 308 HOH A O   
1730 O  O   . HOH F .   ? 0.2885 0.2458 0.4210 -0.1180 0.0004  0.0590  309 HOH A O   
1731 O  O   . HOH F .   ? 0.2632 0.1501 0.2010 -0.0543 -0.0148 0.0399  310 HOH A O   
1732 O  O   . HOH F .   ? 0.2277 0.2167 0.5537 0.0356  0.0081  -0.0162 311 HOH A O   
1733 O  O   . HOH F .   ? 0.1426 0.2006 0.3775 -0.0198 0.0196  0.0735  312 HOH A O   
1734 O  O   . HOH F .   ? 0.2585 0.3100 0.4249 -0.0599 -0.0414 0.0933  313 HOH A O   
1735 O  O   . HOH F .   ? 0.1975 0.1975 0.1928 -0.0504 -0.0128 0.0493  314 HOH A O   
1736 O  O   . HOH F .   ? 0.2353 0.2188 0.3455 -0.0028 0.0271  -0.0081 315 HOH A O   
1737 O  O   . HOH F .   ? 0.3262 0.1702 0.5164 0.0044  0.0141  -0.0180 316 HOH A O   
1738 O  O   . HOH F .   ? 0.2473 0.2893 0.3646 0.0046  0.0738  0.0321  317 HOH A O   
1739 O  O   . HOH F .   ? 0.2219 0.2675 0.2628 0.0052  0.0647  0.0342  318 HOH A O   
1740 O  O   . HOH F .   ? 0.3228 0.2446 0.4155 -0.0426 -0.0430 0.0137  319 HOH A O   
1741 O  O   . HOH F .   ? 0.2564 0.2660 0.3559 0.0055  0.0825  0.0640  320 HOH A O   
1742 O  O   . HOH F .   ? 0.2149 0.1954 0.2943 -0.0378 0.0515  0.0059  321 HOH A O   
1743 O  O   . HOH F .   ? 0.5158 0.3862 0.3911 -0.1118 0.1508  -0.0294 322 HOH A O   
1744 O  O   . HOH F .   ? 0.2067 0.1348 0.2374 -0.0060 -0.0060 0.0363  323 HOH A O   
1745 O  O   . HOH F .   ? 0.2023 0.1295 0.1946 -0.0019 -0.0023 0.0095  324 HOH A O   
1746 O  O   . HOH F .   ? 0.3751 0.1757 0.2939 -0.0753 -0.0219 0.0631  325 HOH A O   
1747 O  O   . HOH F .   ? 0.7989 0.4543 0.3649 -0.3340 0.2207  -0.1593 326 HOH A O   
1748 O  O   . HOH F .   ? 0.3641 0.1526 0.2715 -0.0252 -0.0823 -0.0450 327 HOH A O   
1749 O  O   . HOH F .   ? 0.5946 0.3381 0.3913 0.1347  -0.1240 0.0039  328 HOH A O   
1750 O  O   . HOH F .   ? 0.2727 0.2857 0.3257 -0.0243 0.0301  0.0218  329 HOH A O   
1751 O  O   . HOH F .   ? 0.2611 0.3942 0.3761 -0.0068 0.0000  -0.0001 330 HOH A O   
1752 O  O   . HOH F .   ? 0.2516 0.2232 0.3279 -0.0234 0.0405  -0.0789 331 HOH A O   
1753 O  O   . HOH F .   ? 0.4947 0.2234 0.3653 0.0602  -0.0544 -0.0707 332 HOH A O   
1754 O  O   . HOH F .   ? 0.2316 0.2415 0.3024 0.0005  0.0740  0.0088  333 HOH A O   
1755 O  O   . HOH F .   ? 0.2569 0.1622 0.1999 -0.0176 0.0170  0.0176  334 HOH A O   
1756 O  O   . HOH F .   ? 0.3710 0.1983 0.3529 -0.1239 0.0944  -0.0383 335 HOH A O   
1757 O  O   . HOH F .   ? 0.3484 0.5326 0.3938 -0.2212 0.1421  -0.0977 336 HOH A O   
1758 O  O   . HOH F .   ? 0.2630 0.1387 0.3025 0.0349  0.0375  -0.0229 337 HOH A O   
1759 O  O   . HOH F .   ? 0.4622 0.3047 0.3537 -0.1202 0.0402  0.0342  338 HOH A O   
1760 O  O   . HOH F .   ? 0.2859 0.4425 0.2728 -0.0353 0.0509  0.1154  339 HOH A O   
1761 O  O   . HOH F .   ? 0.2506 0.3198 0.3320 -0.0195 0.0221  0.0341  340 HOH A O   
1762 O  O   . HOH F .   ? 0.2384 0.1957 0.3195 0.0068  0.0546  -0.0494 341 HOH A O   
1763 O  O   . HOH F .   ? 0.4224 0.1657 0.2613 -0.0497 0.0031  -0.0148 342 HOH A O   
1764 O  O   . HOH F .   ? 0.3475 0.4272 0.2744 -0.1072 0.0070  0.0462  343 HOH A O   
1765 O  O   . HOH F .   ? 0.5740 0.4951 0.3695 -0.0616 0.0538  -0.0136 344 HOH A O   
1766 O  O   . HOH F .   ? 0.2671 0.2106 0.2502 0.0570  0.0755  0.0529  345 HOH A O   
1767 O  O   . HOH F .   ? 0.4698 0.3192 0.3848 0.0054  -0.1075 -0.0416 346 HOH A O   
1768 O  O   . HOH F .   ? 0.3119 0.4029 0.3793 -0.0017 -0.0081 0.1744  347 HOH A O   
1769 O  O   . HOH F .   ? 0.4861 0.6284 0.5716 0.1790  0.1986  0.2712  348 HOH A O   
1770 O  O   . HOH F .   ? 0.4103 0.2599 0.4519 0.0398  0.1931  0.0040  349 HOH A O   
1771 O  O   . HOH F .   ? 0.3622 0.3825 0.4348 -0.0440 0.0009  0.0081  350 HOH A O   
1772 O  O   . HOH F .   ? 0.3132 0.4524 0.6103 0.0627  0.0518  -0.1238 351 HOH A O   
1773 O  O   . HOH F .   ? 0.3983 0.3791 0.5691 0.0942  0.1595  0.2226  352 HOH A O   
1774 O  O   . HOH F .   ? 0.3205 0.4234 0.3794 0.0609  0.0687  -0.0566 353 HOH A O   
1775 O  O   . HOH F .   ? 0.2382 0.1532 0.3052 0.0264  0.0279  -0.0029 354 HOH A O   
1776 O  O   . HOH F .   ? 0.2872 0.3200 0.3909 -0.0275 0.0723  0.0312  355 HOH A O   
1777 O  O   . HOH F .   ? 0.4504 0.1862 0.5469 -0.0464 -0.0641 0.0215  356 HOH A O   
1778 O  O   . HOH F .   ? 0.3712 0.2562 0.2585 -0.0535 0.0158  -0.0274 357 HOH A O   
1779 O  O   . HOH F .   ? 0.4000 0.7999 0.3520 -0.2671 -0.0143 0.0783  358 HOH A O   
1780 O  O   . HOH F .   ? 0.3929 0.3855 0.2202 0.0230  -0.0139 0.0087  359 HOH A O   
1781 O  O   . HOH F .   ? 0.4174 0.4624 0.3227 0.1666  0.0648  0.0956  360 HOH A O   
1782 O  O   . HOH F .   ? 0.2174 0.2503 0.3797 -0.0486 0.0305  -0.0045 361 HOH A O   
1783 O  O   . HOH F .   ? 0.2812 0.1736 0.3759 0.0350  0.0301  -0.0254 362 HOH A O   
1784 O  O   . HOH F .   ? 0.3824 0.2048 0.3729 0.0879  -0.1149 -0.0275 363 HOH A O   
1785 O  O   . HOH G .   ? 0.6443 0.4988 0.4050 -0.1453 -0.2077 0.0054  301 HOH B O   
1786 O  O   . HOH G .   ? 0.3496 0.3373 0.4517 -0.1081 -0.0176 0.1185  302 HOH B O   
1787 O  O   . HOH G .   ? 0.2185 0.1761 0.2327 0.0263  0.0588  -0.0036 303 HOH B O   
1788 O  O   . HOH G .   ? 0.1703 0.3569 0.4707 0.0035  0.0000  0.0000  304 HOH B O   
1789 O  O   . HOH G .   ? 0.3397 0.2977 0.4252 0.0074  -0.0108 0.0999  305 HOH B O   
1790 O  O   . HOH G .   ? 0.1931 0.1971 0.2186 0.0754  0.0446  0.0275  306 HOH B O   
1791 O  O   . HOH G .   ? 0.2869 0.5017 0.4404 -0.0569 -0.0561 0.0019  307 HOH B O   
1792 O  O   . HOH G .   ? 0.5740 0.5130 0.3495 -0.0179 -0.1187 0.0047  308 HOH B O   
1793 O  O   . HOH G .   ? 0.1562 0.2600 0.2385 0.0640  0.0254  0.0507  309 HOH B O   
1794 O  O   . HOH G .   ? 0.1843 0.2485 0.2077 -0.0365 0.0380  -0.0336 310 HOH B O   
1795 O  O   . HOH G .   ? 0.4023 0.3773 0.4023 0.0417  -0.1799 0.0653  311 HOH B O   
1796 O  O   . HOH G .   ? 0.3381 0.4156 0.3543 0.0188  -0.1374 -0.0017 312 HOH B O   
1797 O  O   . HOH G .   ? 0.1814 0.1137 0.1963 -0.0013 0.0118  0.0292  313 HOH B O   
1798 O  O   . HOH G .   ? 0.3341 0.2525 0.6472 -0.0152 -0.0924 0.0191  314 HOH B O   
1799 O  O   . HOH G .   ? 0.3539 0.3097 0.3182 0.0165  0.0288  0.0356  315 HOH B O   
1800 O  O   . HOH G .   ? 0.2182 0.2097 0.3357 -0.0007 -0.0180 -0.0049 316 HOH B O   
1801 O  O   . HOH G .   ? 0.4723 0.3721 0.2659 -0.0083 -0.0081 -0.0304 317 HOH B O   
1802 O  O   . HOH G .   ? 0.5499 0.2692 0.3876 0.0103  0.1313  -0.0908 318 HOH B O   
1803 O  O   . HOH G .   ? 0.3155 0.2075 0.2845 0.0491  -0.0427 0.0447  319 HOH B O   
1804 O  O   . HOH G .   ? 0.2623 0.1377 0.3948 -0.0248 -0.0818 0.0333  320 HOH B O   
1805 O  O   . HOH G .   ? 0.4721 0.4261 0.2675 0.0206  0.0137  0.0605  321 HOH B O   
1806 O  O   . HOH G .   ? 0.5433 0.1695 0.2956 -0.0044 0.0862  -0.0045 322 HOH B O   
1807 O  O   . HOH G .   ? 0.3115 0.1897 0.3136 0.0235  0.0014  -0.0260 323 HOH B O   
1808 O  O   . HOH G .   ? 0.5157 0.3677 0.2979 -0.0066 -0.0288 -0.1151 324 HOH B O   
1809 O  O   . HOH G .   ? 0.3470 0.4365 0.2188 -0.0561 -0.0633 -0.0396 325 HOH B O   
1810 O  O   . HOH G .   ? 0.3599 0.1913 0.4095 0.0262  -0.0878 0.0145  326 HOH B O   
1811 O  O   . HOH G .   ? 0.3346 0.3090 0.3432 -0.0434 0.0531  0.0466  327 HOH B O   
1812 O  O   . HOH G .   ? 0.5296 0.2334 0.4303 -0.0396 -0.0890 -0.0100 328 HOH B O   
1813 O  O   . HOH G .   ? 0.3385 0.3442 0.5970 -0.0440 -0.0356 -0.1536 329 HOH B O   
1814 O  O   . HOH G .   ? 0.4352 0.3787 0.4358 -0.1335 0.0481  -0.0412 330 HOH B O   
1815 O  O   . HOH G .   ? 0.4522 0.3220 0.5647 0.0653  -0.0686 0.0365  331 HOH B O   
1816 O  O   . HOH G .   ? 0.4030 0.5074 0.3363 0.0031  0.0123  -0.0826 332 HOH B O   
1817 O  O   . HOH G .   ? 0.4125 0.2869 0.4644 -0.0532 -0.0950 0.0092  333 HOH B O   
1818 O  O   . HOH G .   ? 0.4526 0.4126 0.4139 -0.1170 -0.0060 -0.1386 334 HOH B O   
# 
