data_9H7B
# 
_entry.id   9H7B 
# 
_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   9H7B         pdb_00009h7b 10.2210/pdb9h7b/pdb 
WWPDB D_1292142622 ?            ?                   
# 
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                        9H7B 
_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    1  ? ? ? ? 
3 non-polymer syn 'biphenyl-4-carboxylic acid' 198.217   2  ? ? ? ? 
4 water       nat water                        18.015    73 ? ? ? ? 
# 
_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 'biphenyl-4-carboxylic acid' Z7Z 
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                    'Human Plasma' 
_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                Liver 
_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               'Human Plasma' 
_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 
Z7Z non-polymer         . 'biphenyl-4-carboxylic acid' ? 'C13 H10 O2'     198.217 
# 
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  ?   ?   ?   A . n 
A 1 39  ASP 39  39  ?   ?   ?   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  ?   ?   ?   B . n 
B 1 38  ASP 38  38  ?   ?   ?   B . n 
B 1 39  ASP 39  39  ?   ?   ?   B . n 
B 1 40  THR 40  40  ?   ?   ?   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  ?   ?   ?   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 ?   ?   ?   B . n 
B 1 124 ASN 124 124 ?   ?   ?   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        Z7Z 
_pdbx_entity_instance_feature.asym_id        ? 
_pdbx_entity_instance_feature.seq_num        ? 
_pdbx_entity_instance_feature.auth_comp_id   Z7Z 
_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 3 Z7Z 1  202 1  Z7Z A28 A . 
E 3 Z7Z 1  201 1  Z7Z A28 B . 
F 4 HOH 1  301 19 HOH HOH A . 
F 4 HOH 2  302 46 HOH HOH A . 
F 4 HOH 3  303 40 HOH HOH A . 
F 4 HOH 4  304 20 HOH HOH A . 
F 4 HOH 5  305 22 HOH HOH A . 
F 4 HOH 6  306 57 HOH HOH A . 
F 4 HOH 7  307 13 HOH HOH A . 
F 4 HOH 8  308 23 HOH HOH A . 
F 4 HOH 9  309 6  HOH HOH A . 
F 4 HOH 10 310 15 HOH HOH A . 
F 4 HOH 11 311 10 HOH HOH A . 
F 4 HOH 12 312 3  HOH HOH A . 
F 4 HOH 13 313 70 HOH HOH A . 
F 4 HOH 14 314 35 HOH HOH A . 
F 4 HOH 15 315 39 HOH HOH A . 
F 4 HOH 16 316 24 HOH HOH A . 
F 4 HOH 17 317 12 HOH HOH A . 
F 4 HOH 18 318 36 HOH HOH A . 
F 4 HOH 19 319 52 HOH HOH A . 
F 4 HOH 20 320 7  HOH HOH A . 
F 4 HOH 21 321 8  HOH HOH A . 
F 4 HOH 22 322 58 HOH HOH A . 
F 4 HOH 23 323 11 HOH HOH A . 
F 4 HOH 24 324 61 HOH HOH A . 
F 4 HOH 25 325 60 HOH HOH A . 
F 4 HOH 26 326 56 HOH HOH A . 
F 4 HOH 27 327 38 HOH HOH A . 
F 4 HOH 28 328 50 HOH HOH A . 
F 4 HOH 29 329 53 HOH HOH A . 
F 4 HOH 30 330 4  HOH HOH A . 
F 4 HOH 31 331 55 HOH HOH A . 
F 4 HOH 32 332 33 HOH HOH A . 
F 4 HOH 33 333 29 HOH HOH A . 
F 4 HOH 34 334 59 HOH HOH A . 
F 4 HOH 35 335 69 HOH HOH A . 
F 4 HOH 36 336 30 HOH HOH A . 
F 4 HOH 37 337 17 HOH HOH A . 
F 4 HOH 38 338 18 HOH HOH A . 
F 4 HOH 39 339 63 HOH HOH A . 
F 4 HOH 40 340 44 HOH HOH A . 
F 4 HOH 41 341 54 HOH HOH A . 
F 4 HOH 42 342 62 HOH HOH A . 
F 4 HOH 43 343 68 HOH HOH A . 
F 4 HOH 44 344 42 HOH HOH A . 
F 4 HOH 45 345 67 HOH HOH A . 
F 4 HOH 46 346 43 HOH HOH A . 
F 4 HOH 47 347 27 HOH HOH A . 
F 4 HOH 48 348 72 HOH HOH A . 
F 4 HOH 49 349 26 HOH HOH A . 
F 4 HOH 50 350 41 HOH HOH A . 
G 4 HOH 1  301 65 HOH HOH B . 
G 4 HOH 2  302 32 HOH HOH B . 
G 4 HOH 3  303 28 HOH HOH B . 
G 4 HOH 4  304 21 HOH HOH B . 
G 4 HOH 5  305 14 HOH HOH B . 
G 4 HOH 6  306 1  HOH HOH B . 
G 4 HOH 7  307 45 HOH HOH B . 
G 4 HOH 8  308 49 HOH HOH B . 
G 4 HOH 9  309 9  HOH HOH B . 
G 4 HOH 10 310 31 HOH HOH B . 
G 4 HOH 11 311 16 HOH HOH B . 
G 4 HOH 12 312 2  HOH HOH B . 
G 4 HOH 13 313 37 HOH HOH B . 
G 4 HOH 14 314 34 HOH HOH B . 
G 4 HOH 15 315 48 HOH HOH B . 
G 4 HOH 16 316 5  HOH HOH B . 
G 4 HOH 17 317 73 HOH HOH B . 
G 4 HOH 18 318 25 HOH HOH B . 
G 4 HOH 19 319 64 HOH HOH B . 
G 4 HOH 20 320 51 HOH HOH B . 
G 4 HOH 21 321 47 HOH HOH B . 
G 4 HOH 22 322 66 HOH HOH B . 
G 4 HOH 23 323 71 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 ARG 21  ? NH1 ? A ARG 21  NH1 
5  1 Y 1 A ARG 21  ? NH2 ? A ARG 21  NH2 
6  1 Y 1 A LYS 35  ? CE  ? A LYS 35  CE  
7  1 Y 1 A LYS 35  ? NZ  ? A LYS 35  NZ  
8  1 Y 1 A GLU 42  ? CG  ? A GLU 42  CG  
9  1 Y 1 A GLU 42  ? CD  ? A GLU 42  CD  
10 1 Y 1 A GLU 42  ? OE1 ? A GLU 42  OE1 
11 1 Y 1 A GLU 42  ? OE2 ? A GLU 42  OE2 
12 1 Y 1 A GLU 51  ? OE1 ? A GLU 51  OE1 
13 1 Y 1 A GLU 51  ? OE2 ? A GLU 51  OE2 
14 1 Y 1 A GLU 61  ? OE1 ? A GLU 61  OE1 
15 1 Y 1 A GLU 61  ? OE2 ? A GLU 61  OE2 
16 1 Y 1 A LYS 76  ? NZ  ? A LYS 76  NZ  
17 1 Y 1 A LYS 80  ? CE  ? A LYS 80  CE  
18 1 Y 1 A LYS 80  ? NZ  ? A LYS 80  NZ  
19 1 Y 1 A GLU 89  ? OE1 ? A GLU 89  OE1 
20 1 Y 1 A GLU 89  ? OE2 ? A GLU 89  OE2 
21 1 Y 1 A GLU 92  ? CG  ? A GLU 92  CG  
22 1 Y 1 A GLU 92  ? CD  ? A GLU 92  CD  
23 1 Y 1 A GLU 92  ? OE1 ? A GLU 92  OE1 
24 1 Y 1 A GLU 92  ? OE2 ? A GLU 92  OE2 
25 1 Y 1 A ARG 104 ? NH1 ? A ARG 104 NH1 
26 1 Y 1 A ARG 104 ? NH2 ? A ARG 104 NH2 
27 1 Y 1 B CYS 10  ? N   ? B CYS 10  N   
28 1 Y 1 B CYS 10  ? CA  ? B CYS 10  CA  
29 1 Y 1 B CYS 10  ? SG  ? B CYS 10  SG  
30 1 Y 1 B LYS 15  ? NZ  ? B LYS 15  NZ  
31 1 Y 1 B ASN 27  ? ND2 ? B ASN 27  ND2 
32 1 Y 1 B ARG 34  ? CZ  ? B ARG 34  CZ  
33 1 Y 1 B ARG 34  ? NH1 ? B ARG 34  NH1 
34 1 Y 1 B ARG 34  ? NH2 ? B ARG 34  NH2 
35 1 Y 1 B LYS 35  ? CE  ? B LYS 35  CE  
36 1 Y 1 B LYS 35  ? NZ  ? B LYS 35  NZ  
37 1 Y 1 B ALA 36  ? CB  ? B ALA 36  CB  
38 1 Y 1 B GLU 42  ? CG  ? B GLU 42  CG  
39 1 Y 1 B GLU 42  ? CD  ? B GLU 42  CD  
40 1 Y 1 B GLU 42  ? OE1 ? B GLU 42  OE1 
41 1 Y 1 B GLU 42  ? OE2 ? B GLU 42  OE2 
42 1 Y 1 B GLU 51  ? CG  ? B GLU 51  CG  
43 1 Y 1 B GLU 51  ? CD  ? B GLU 51  CD  
44 1 Y 1 B GLU 51  ? OE1 ? B GLU 51  OE1 
45 1 Y 1 B GLU 51  ? OE2 ? B GLU 51  OE2 
46 1 Y 1 B GLU 61  ? CG  ? B GLU 61  CG  
47 1 Y 1 B GLU 61  ? CD  ? B GLU 61  CD  
48 1 Y 1 B GLU 61  ? OE1 ? B GLU 61  OE1 
49 1 Y 1 B GLU 61  ? OE2 ? B GLU 61  OE2 
50 1 Y 1 B GLU 62  ? OE1 ? B GLU 62  OE1 
51 1 Y 1 B GLU 62  ? OE2 ? B GLU 62  OE2 
52 1 Y 1 B GLU 63  ? CD  ? B GLU 63  CD  
53 1 Y 1 B GLU 63  ? OE1 ? B GLU 63  OE1 
54 1 Y 1 B GLU 63  ? OE2 ? B GLU 63  OE2 
55 1 Y 1 B GLU 72  ? OE2 ? B GLU 72  OE2 
56 1 Y 1 B LYS 80  ? NZ  ? B LYS 80  NZ  
57 1 Y 1 B GLU 92  ? CB  ? B GLU 92  CB  
58 1 Y 1 B GLU 92  ? CG  ? B GLU 92  CG  
59 1 Y 1 B GLU 92  ? CD  ? B GLU 92  CD  
60 1 Y 1 B GLU 92  ? OE1 ? B GLU 92  OE1 
61 1 Y 1 B GLU 92  ? OE2 ? B GLU 92  OE2 
62 1 Y 1 B ASN 98  ? CB  ? B ASN 98  CB  
63 1 Y 1 B ASN 98  ? CG  ? B ASN 98  CG  
64 1 Y 1 B ASN 98  ? OD1 ? B ASN 98  OD1 
65 1 Y 1 B ASN 98  ? ND2 ? B ASN 98  ND2 
66 1 Y 1 B ARG 104 ? CG  ? B ARG 104 CG  
67 1 Y 1 B ARG 104 ? CD  ? B ARG 104 CD  
68 1 Y 1 B ARG 104 ? NE  ? B ARG 104 NE  
69 1 Y 1 B ARG 104 ? CZ  ? B ARG 104 CZ  
70 1 Y 1 B ARG 104 ? NH1 ? B ARG 104 NH1 
71 1 Y 1 B ARG 104 ? NH2 ? B ARG 104 NH2 
72 1 Y 1 B VAL 122 ? CG1 ? B VAL 122 CG1 
73 1 Y 1 B VAL 122 ? CG2 ? B VAL 122 CG2 
# 
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         ? ? ? 5.6.0117 1 
? 'data reduction' ? ? ? ? ? ? ? ? ? ? ? xia2.multiplex ? ? ? .        2 
? 'data scaling'   ? ? ? ? ? ? ? ? ? ? ? xia2.multiplex ? ? ? .        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                     9H7B 
_cell.details                      ? 
_cell.formula_units_Z              ? 
_cell.length_a                     83.486 
_cell.length_a_esd                 ? 
_cell.length_b                     41.105 
_cell.length_b_esd                 ? 
_cell.length_c                     62.775 
_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                         9H7B 
_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                   9H7B 
_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             1.95 
_exptl_crystal.density_method               ? 
_exptl_crystal.density_percent_sol          37.07 
_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                     CCD 
_diffrn_detector.diffrn_id                    1 
_diffrn_detector.type                         'ADSC QUANTUM 315' 
_diffrn_detector.area_resol_mean              ? 
_diffrn_detector.dtime                        ? 
_diffrn_detector.pdbx_frames_total            ? 
_diffrn_detector.pdbx_collection_time_total   ? 
_diffrn_detector.pdbx_collection_date         2012-05-29 
_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   0.979 
_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' 
_diffrn_source.voltage                     ? 
_diffrn_source.take-off_angle              ? 
_diffrn_source.pdbx_wavelength_list        0.979 
_diffrn_source.pdbx_wavelength             ? 
_diffrn_source.pdbx_synchrotron_beamline   I04 
_diffrn_source.pdbx_synchrotron_site       Diamond 
# 
_reflns.B_iso_Wilson_estimate                          ? 
_reflns.entry_id                                       9H7B 
_reflns.data_reduction_details                         ? 
_reflns.data_reduction_method                          ? 
_reflns.d_resolution_high                              1.51 
_reflns.d_resolution_low                               50.17 
_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                                     34677 
_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                                4.8 
_reflns.pdbx_netI_over_av_sigmaI                       ? 
_reflns.pdbx_netI_over_sigmaI                          12.5 
_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                                0.043 
_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                              0.056 
_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                                    1.51 
_reflns_shell.d_res_low                                     1.549 
_reflns_shell.meanI_over_sigI_all                           ? 
_reflns_shell.meanI_over_sigI_obs                           2.4 
_reflns_shell.number_measured_all                           ? 
_reflns_shell.number_measured_obs                           ? 
_reflns_shell.number_possible                               ? 
_reflns_shell.number_unique_all                             ? 
_reflns_shell.number_unique_obs                             2199 
_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                               0.375 
_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                                  0.491 
_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]                            -0.09 
_refine.aniso_B[1][2]                            -0.00 
_refine.aniso_B[1][3]                            0.00 
_refine.aniso_B[2][2]                            0.09 
_refine.aniso_B[2][3]                            0.00 
_refine.aniso_B[3][3]                            0.00 
_refine.B_iso_max                                ? 
_refine.B_iso_mean                               16.590 
_refine.B_iso_min                                ? 
_refine.correlation_coeff_Fo_to_Fc               0.961 
_refine.correlation_coeff_Fo_to_Fc_free          0.944 
_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                                 9H7B 
_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                            1.51 
_refine.ls_d_res_low                             31.80 
_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                     32886 
_refine.ls_number_reflns_R_free                  1743 
_refine.ls_number_reflns_R_work                  ? 
_refine.ls_number_restraints                     ? 
_refine.ls_percent_reflns_obs                    99.71 
_refine.ls_percent_reflns_R_free                 5.0 
_refine.ls_R_factor_all                          ? 
_refine.ls_R_factor_obs                          0.17227 
_refine.ls_R_factor_R_free                       0.22810 
_refine.ls_R_factor_R_free_error                 ? 
_refine.ls_R_factor_R_free_error_details         ? 
_refine.ls_R_factor_R_work                       0.16940 
_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                       0.082 
_refine.pdbx_overall_ESU_R_Free                  0.080 
_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                             3.033 
_refine.overall_SU_ML                            0.051 
_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                       1.51 
_refine_hist.d_res_low                        31.80 
_refine_hist.number_atoms_solvent             73 
_refine_hist.number_atoms_total               1714 
_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        1610 
_refine_hist.pdbx_number_atoms_nucleic_acid   0 
_refine_hist.pdbx_number_atoms_ligand         31 
_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' ? 0.020  0.020  1698 ? r_bond_refined_d             ? ? 
'X-RAY DIFFRACTION' ? 0.007  0.020  1082 ? r_bond_other_d               ? ? 
'X-RAY DIFFRACTION' ? 1.932  1.955  2312 ? r_angle_refined_deg          ? ? 
'X-RAY DIFFRACTION' ? 1.076  3.000  2641 ? r_angle_other_deg            ? ? 
'X-RAY DIFFRACTION' ? 6.628  5.000  216  ? r_dihedral_angle_1_deg       ? ? 
'X-RAY DIFFRACTION' ? 27.651 22.549 51   ? r_dihedral_angle_2_deg       ? ? 
'X-RAY DIFFRACTION' ? 13.030 15.000 242  ? r_dihedral_angle_3_deg       ? ? 
'X-RAY DIFFRACTION' ? 24.587 15.000 5    ? r_dihedral_angle_4_deg       ? ? 
'X-RAY DIFFRACTION' ? 0.139  0.200  265  ? r_chiral_restr               ? ? 
'X-RAY DIFFRACTION' ? 0.011  0.021  1874 ? r_gen_planes_refined         ? ? 
'X-RAY DIFFRACTION' ? 0.001  0.020  365  ? 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' ? ?      ?      ?    ? r_mcbond_it                  ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?    ? r_mcbond_other               ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?    ? r_mcangle_it                 ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?    ? r_mcangle_other              ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?    ? r_scbond_it                  ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?    ? r_scbond_other               ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?    ? r_scangle_it                 ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?    ? r_scangle_other              ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?    ? r_long_range_B_refined       ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?    ? r_long_range_B_other         ? ? 
'X-RAY DIFFRACTION' ? 5.960  3.000  2778 ? r_rigid_bond_restr           ? ? 
'X-RAY DIFFRACTION' ? 18.863 5.000  27   ? r_sphericity_free            ? ? 
'X-RAY DIFFRACTION' ? 13.437 5.000  2782 ? r_sphericity_bonded          ? ? 
# 
_refine_ls_shell.pdbx_refine_id                   'X-RAY DIFFRACTION' 
_refine_ls_shell.d_res_high                       1.510 
_refine_ls_shell.d_res_low                        1.549 
_refine_ls_shell.number_reflns_all                ? 
_refine_ls_shell.number_reflns_obs                ? 
_refine_ls_shell.number_reflns_R_free             123 
_refine_ls_shell.number_reflns_R_work             2199 
_refine_ls_shell.percent_reflns_obs               99.96 
_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                  0.242 
_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                  0.359 
# 
_struct.entry_id                     9H7B 
_struct.title                        'Human Transthyretin in Complex with Biphenyl-4-carboxylic Acid' 
_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        9H7B 
_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 3 ? 
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 9H7B A 1 ? 127 ? P02766 21 ? 147 ? 1 127 
2 1 9H7B B 1 ? 127 ? P02766 21 ? 147 ? 1 127 
# 
_pdbx_struct_assembly.id                   1 
_pdbx_struct_assembly.details              author_defined_assembly 
_pdbx_struct_assembly.method_details       ? 
_pdbx_struct_assembly.oligomeric_details   tetrameric 
_pdbx_struct_assembly.oligomeric_count     4 
# 
loop_
_pdbx_struct_assembly_gen.assembly_id 
_pdbx_struct_assembly_gen.oper_expression 
_pdbx_struct_assembly_gen.asym_id_list 
1 1 A,B,C,D,E,F,G 
1 2 A,B,C,D,E,F,G 
# 
_pdbx_struct_assembly_auth_evidence.id                     1 
_pdbx_struct_assembly_auth_evidence.assembly_id            1 
_pdbx_struct_assembly_auth_evidence.experimental_support   homology 
_pdbx_struct_assembly_auth_evidence.details                ? 
# 
loop_
_pdbx_struct_oper_list.id 
_pdbx_struct_oper_list.type 
_pdbx_struct_oper_list.name 
_pdbx_struct_oper_list.symmetry_operation 
_pdbx_struct_oper_list.matrix[1][1] 
_pdbx_struct_oper_list.matrix[1][2] 
_pdbx_struct_oper_list.matrix[1][3] 
_pdbx_struct_oper_list.vector[1] 
_pdbx_struct_oper_list.matrix[2][1] 
_pdbx_struct_oper_list.matrix[2][2] 
_pdbx_struct_oper_list.matrix[2][3] 
_pdbx_struct_oper_list.vector[2] 
_pdbx_struct_oper_list.matrix[3][1] 
_pdbx_struct_oper_list.matrix[3][2] 
_pdbx_struct_oper_list.matrix[3][3] 
_pdbx_struct_oper_list.vector[3] 
1 'identity operation'         1_555 x,y,z     1.0000000000  0.0000000000 0.0000000000 0.0000000000 0.0000000000 1.0000000000  
0.0000000000 0.0000000000   0.0000000000 0.0000000000 1.0000000000 0.0000000000 
2 'crystal symmetry operation' 2_545 -x,-y-1,z -1.0000000000 0.0000000000 0.0000000000 0.0000000000 0.0000000000 -1.0000000000 
0.0000000000 -41.1050000000 0.0000000000 0.0000000000 1.0000000000 0.0000000000 
# 
loop_
_struct_conf.conf_type_id 
_struct_conf.id 
_struct_conf.pdbx_PDB_helix_id 
_struct_conf.beg_label_comp_id 
_struct_conf.beg_label_asym_id 
_struct_conf.beg_label_seq_id 
_struct_conf.pdbx_beg_PDB_ins_code 
_struct_conf.end_label_comp_id 
_struct_conf.end_label_asym_id 
_struct_conf.end_label_seq_id 
_struct_conf.pdbx_end_PDB_ins_code 
_struct_conf.beg_auth_comp_id 
_struct_conf.beg_auth_asym_id 
_struct_conf.beg_auth_seq_id 
_struct_conf.end_auth_comp_id 
_struct_conf.end_auth_asym_id 
_struct_conf.end_auth_seq_id 
_struct_conf.pdbx_PDB_helix_class 
_struct_conf.details 
_struct_conf.pdbx_PDB_helix_length 
HELX_P HELX_P1 AA1 ASP A 74 ? 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 OE1 ? ? ? 1_555 C CA  . CA ? ? A GLU 66  A CA  201 1_555 ? ? ? ? ? ? ? 2.327 ? ? 
metalc2 metalc ? ? A ASP 99 O   ? ? ? 1_555 C CA  . CA ? ? A ASP 99  A CA  201 1_555 ? ? ? ? ? ? ? 2.378 ? ? 
metalc3 metalc ? ? A ASP 99 OD1 ? ? ? 1_555 C CA  . CA ? ? A ASP 99  A CA  201 1_555 ? ? ? ? ? ? ? 2.240 ? ? 
metalc4 metalc ? ? C CA  .  CA  ? ? ? 1_555 F HOH . O  ? ? A CA  201 A HOH 316 1_555 ? ? ? ? ? ? ? 2.341 ? ? 
metalc5 metalc ? ? C CA  .  CA  ? ? ? 1_555 F HOH . O  ? ? A CA  201 A HOH 348 1_565 ? ? ? ? ? ? ? 2.339 ? ? 
# 
_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  OE1 ? 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 94.3  ? 
2  OE1 ? 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 83.9  ? 
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 76.1  ? 
4  OE1 ? A GLU 66 ? A GLU 66  ? 1_555 CA ? C CA . ? A CA 201 ? 1_555 O   ? F HOH .  ? A HOH 316 ? 1_555 80.6  ? 
5  O   ? A ASP 99 ? A ASP 99  ? 1_555 CA ? C CA . ? A CA 201 ? 1_555 O   ? F HOH .  ? A HOH 316 ? 1_555 137.8 ? 
6  OD1 ? A ASP 99 ? A ASP 99  ? 1_555 CA ? C CA . ? A CA 201 ? 1_555 O   ? F HOH .  ? A HOH 316 ? 1_555 143.4 ? 
7  OE1 ? A GLU 66 ? A GLU 66  ? 1_555 CA ? C CA . ? A CA 201 ? 1_555 O   ? F HOH .  ? A HOH 348 ? 1_565 152.6 ? 
8  O   ? A ASP 99 ? A ASP 99  ? 1_555 CA ? C CA . ? A CA 201 ? 1_555 O   ? F HOH .  ? A HOH 348 ? 1_565 110.0 ? 
9  OD1 ? A ASP 99 ? A ASP 99  ? 1_555 CA ? C CA . ? A CA 201 ? 1_555 O   ? F HOH .  ? A HOH 348 ? 1_565 89.7  ? 
10 O   ? F HOH .  ? A HOH 316 ? 1_555 CA ? C CA . ? A CA 201 ? 1_555 O   ? F HOH .  ? A HOH 348 ? 1_565 89.1  ? 
# 
loop_
_struct_sheet.id 
_struct_sheet.type 
_struct_sheet.number_strands 
_struct_sheet.details 
AA1 ? 8 ? 
AA2 ? 8 ? 
AA3 ? 8 ? 
# 
loop_
_struct_sheet_order.sheet_id 
_struct_sheet_order.range_id_1 
_struct_sheet_order.range_id_2 
_struct_sheet_order.offset 
_struct_sheet_order.sense 
AA1 1 2 ? anti-parallel 
AA1 2 3 ? parallel      
AA1 3 4 ? anti-parallel 
AA1 4 5 ? anti-parallel 
AA1 5 6 ? anti-parallel 
AA1 6 7 ? parallel      
AA1 7 8 ? anti-parallel 
AA2 1 2 ? anti-parallel 
AA2 2 3 ? parallel      
AA2 3 4 ? anti-parallel 
AA2 4 5 ? anti-parallel 
AA2 5 6 ? anti-parallel 
AA2 6 7 ? parallel      
AA2 7 8 ? anti-parallel 
AA3 1 2 ? anti-parallel 
AA3 2 3 ? anti-parallel 
AA3 3 4 ? anti-parallel 
AA3 4 5 ? anti-parallel 
AA3 5 6 ? anti-parallel 
AA3 6 7 ? anti-parallel 
AA3 7 8 ? anti-parallel 
# 
loop_
_struct_sheet_range.sheet_id 
_struct_sheet_range.id 
_struct_sheet_range.beg_label_comp_id 
_struct_sheet_range.beg_label_asym_id 
_struct_sheet_range.beg_label_seq_id 
_struct_sheet_range.pdbx_beg_PDB_ins_code 
_struct_sheet_range.end_label_comp_id 
_struct_sheet_range.end_label_asym_id 
_struct_sheet_range.end_label_seq_id 
_struct_sheet_range.pdbx_end_PDB_ins_code 
_struct_sheet_range.beg_auth_comp_id 
_struct_sheet_range.beg_auth_asym_id 
_struct_sheet_range.beg_auth_seq_id 
_struct_sheet_range.end_auth_comp_id 
_struct_sheet_range.end_auth_asym_id 
_struct_sheet_range.end_auth_seq_id 
AA1 1 SER A 23  ? PRO A 24  ? SER A 23  PRO A 24  
AA1 2 LEU A 12  ? ASP A 18  ? LEU A 12  ASP A 18  
AA1 3 ARG A 104 ? SER A 112 ? ARG A 104 SER A 112 
AA1 4 SER A 115 ? THR A 123 ? SER A 115 THR A 123 
AA1 5 SER B 115 ? VAL B 121 ? SER B 115 VAL B 121 
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 121 ? SER B 115 VAL B 121 
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 HIS A 88  ? ALA A 97  ? HIS A 88  ALA A 97  
AA3 5 HIS B 88  ? ALA B 97  ? HIS B 88  ALA B 97  
AA3 6 GLY B 67  ? ILE B 73  ? GLY B 67  ILE B 73  
AA3 7 ALA B 29  ? ARG B 34  ? ALA B 29  ARG B 34  
AA3 8 GLU B 42  ? LYS B 48  ? GLU B 42  LYS B 48  
# 
loop_
_pdbx_struct_sheet_hbond.sheet_id 
_pdbx_struct_sheet_hbond.range_id_1 
_pdbx_struct_sheet_hbond.range_id_2 
_pdbx_struct_sheet_hbond.range_1_label_atom_id 
_pdbx_struct_sheet_hbond.range_1_label_comp_id 
_pdbx_struct_sheet_hbond.range_1_label_asym_id 
_pdbx_struct_sheet_hbond.range_1_label_seq_id 
_pdbx_struct_sheet_hbond.range_1_PDB_ins_code 
_pdbx_struct_sheet_hbond.range_1_auth_atom_id 
_pdbx_struct_sheet_hbond.range_1_auth_comp_id 
_pdbx_struct_sheet_hbond.range_1_auth_asym_id 
_pdbx_struct_sheet_hbond.range_1_auth_seq_id 
_pdbx_struct_sheet_hbond.range_2_label_atom_id 
_pdbx_struct_sheet_hbond.range_2_label_comp_id 
_pdbx_struct_sheet_hbond.range_2_label_asym_id 
_pdbx_struct_sheet_hbond.range_2_label_seq_id 
_pdbx_struct_sheet_hbond.range_2_PDB_ins_code 
_pdbx_struct_sheet_hbond.range_2_auth_atom_id 
_pdbx_struct_sheet_hbond.range_2_auth_comp_id 
_pdbx_struct_sheet_hbond.range_2_auth_asym_id 
_pdbx_struct_sheet_hbond.range_2_auth_seq_id 
AA1 1 2 O SER A 23  ? O SER A 23  N ASP A 18  ? N ASP A 18  
AA1 2 3 N 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 THR A 118 ? N THR A 118 O TYR B 116 ? O TYR B 116 
AA1 5 6 O SER B 115 ? O SER B 115 N SER B 112 ? N SER B 112 
AA1 6 7 O ILE B 107 ? O ILE B 107 N MET B 13  ? N MET B 13  
AA1 7 8 N ASP B 18  ? N ASP B 18  O SER B 23  ? O SER B 23  
AA2 1 2 O LEU A 55  ? O LEU A 55  N VAL A 14  ? N VAL A 14  
AA2 2 3 N 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 THR A 118 ? N THR A 118 O TYR B 116 ? O TYR B 116 
AA2 5 6 O SER B 115 ? O SER B 115 N SER B 112 ? N SER B 112 
AA2 6 7 O ILE B 107 ? O ILE B 107 N MET B 13  ? N MET B 13  
AA2 7 8 N VAL B 14  ? N VAL B 14  O LEU B 55  ? O LEU B 55  
AA3 1 2 O ALA A 45  ? O ALA A 45  N VAL A 32  ? N VAL A 32  
AA3 2 3 N HIS A 31  ? N HIS A 31  O GLU A 72  ? O GLU A 72  
AA3 3 4 N TYR A 69  ? N TYR A 69  O PHE A 95  ? O PHE A 95  
AA3 4 5 N VAL A 94  ? N VAL A 94  O GLU B 89  ? O GLU B 89  
AA3 5 6 O VAL B 93  ? O VAL B 93  N VAL B 71  ? N VAL B 71  
AA3 6 7 O GLU B 72  ? O GLU B 72  N HIS B 31  ? N HIS B 31  
AA3 7 8 N VAL B 32  ? N VAL B 32  O ALA B 45  ? O ALA B 45  
# 
_pdbx_entry_details.entry_id                   9H7B 
_pdbx_entry_details.nonpolymer_details         ? 
_pdbx_entry_details.sequence_details           ? 
_pdbx_entry_details.compound_details           ? 
_pdbx_entry_details.source_details             ? 
_pdbx_entry_details.has_ligand_of_interest     Y 
_pdbx_entry_details.has_protein_modification   N 
# 
loop_
_pdbx_struct_special_symmetry.id 
_pdbx_struct_special_symmetry.PDB_model_num 
_pdbx_struct_special_symmetry.auth_asym_id 
_pdbx_struct_special_symmetry.auth_comp_id 
_pdbx_struct_special_symmetry.auth_seq_id 
_pdbx_struct_special_symmetry.PDB_ins_code 
_pdbx_struct_special_symmetry.label_asym_id 
_pdbx_struct_special_symmetry.label_comp_id 
_pdbx_struct_special_symmetry.label_seq_id 
1 1 A Z7Z 202 ? D Z7Z . 
2 1 A Z7Z 202 ? D Z7Z . 
3 1 A Z7Z 202 ? D Z7Z . 
4 1 B Z7Z 201 ? E Z7Z . 
5 1 B Z7Z 201 ? E Z7Z . 
6 1 B Z7Z 201 ? E Z7Z . 
# 
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 ASP 38  ? A ASP 38  
11 1 Y 1 A ASP 39  ? A ASP 39  
12 1 Y 1 A PRO 125 ? A PRO 125 
13 1 Y 1 A LYS 126 ? A LYS 126 
14 1 Y 1 A GLU 127 ? A GLU 127 
15 1 Y 1 B GLY 1   ? B GLY 1   
16 1 Y 1 B PRO 2   ? B PRO 2   
17 1 Y 1 B THR 3   ? B THR 3   
18 1 Y 1 B GLY 4   ? B GLY 4   
19 1 Y 1 B THR 5   ? B THR 5   
20 1 Y 1 B GLY 6   ? B GLY 6   
21 1 Y 1 B GLU 7   ? B GLU 7   
22 1 Y 1 B SER 8   ? B SER 8   
23 1 Y 1 B LYS 9   ? B LYS 9   
24 1 Y 1 B ALA 37  ? B ALA 37  
25 1 Y 1 B ASP 38  ? B ASP 38  
26 1 Y 1 B ASP 39  ? B ASP 39  
27 1 Y 1 B THR 40  ? B THR 40  
28 1 Y 1 B ASP 99  ? B ASP 99  
29 1 Y 1 B SER 100 ? B SER 100 
30 1 Y 1 B GLY 101 ? B GLY 101 
31 1 Y 1 B PRO 102 ? B PRO 102 
32 1 Y 1 B ARG 103 ? B ARG 103 
33 1 Y 1 B THR 123 ? B THR 123 
34 1 Y 1 B ASN 124 ? B ASN 124 
35 1 Y 1 B PRO 125 ? B PRO 125 
36 1 Y 1 B LYS 126 ? B LYS 126 
37 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 
Z7Z O1   O  N N 372 
Z7Z C1   C  N N 373 
Z7Z O2   O  N N 374 
Z7Z C2   C  Y N 375 
Z7Z C3   C  Y N 376 
Z7Z C4   C  Y N 377 
Z7Z C5   C  Y N 378 
Z7Z C6   C  Y N 379 
Z7Z C7   C  Y N 380 
Z7Z C8   C  Y N 381 
Z7Z C9   C  Y N 382 
Z7Z C10  C  Y N 383 
Z7Z C11  C  Y N 384 
Z7Z C12  C  Y N 385 
Z7Z C13  C  Y N 386 
Z7Z H1O  H  N N 387 
Z7Z H31  H  N N 388 
Z7Z H41  H  N N 389 
Z7Z H51  H  N N 390 
Z7Z H61  H  N N 391 
Z7Z H91  H  N N 392 
Z7Z H101 H  N N 393 
Z7Z H111 H  N N 394 
Z7Z H121 H  N N 395 
Z7Z H131 H  N N 396 
# 
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 
Z7Z O1  C1   sing N N 357 
Z7Z O1  H1O  sing N N 358 
Z7Z C1  O2   doub N N 359 
Z7Z C1  C2   sing N N 360 
Z7Z C2  C3   doub Y N 361 
Z7Z C2  C5   sing Y N 362 
Z7Z C3  C4   sing Y N 363 
Z7Z C3  H31  sing N N 364 
Z7Z C4  C7   doub Y N 365 
Z7Z C4  H41  sing N N 366 
Z7Z C5  C6   doub Y N 367 
Z7Z C5  H51  sing N N 368 
Z7Z C6  C7   sing Y N 369 
Z7Z C6  H61  sing N N 370 
Z7Z C7  C8   sing N N 371 
Z7Z C8  C9   doub Y N 372 
Z7Z C8  C10  sing Y N 373 
Z7Z C9  C11  sing Y N 374 
Z7Z C9  H91  sing N N 375 
Z7Z C10 C12  doub Y N 376 
Z7Z C10 H101 sing N N 377 
Z7Z C11 C13  doub Y N 378 
Z7Z C11 H111 sing N N 379 
Z7Z C12 C13  sing Y N 380 
Z7Z C12 H121 sing N N 381 
Z7Z C13 H131 sing N N 382 
# 
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                    9H7B 
_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]   0.011978 
_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]   0.024328 
_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]   0.015930 
_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  ? -11.070 -13.726 -6.683  1.00 44.16 ? 10  CYS A CA  1 
ATOM   2    C  C   . CYS A 1 10  ? -10.843 -12.879 -5.419  1.00 28.57 ? 10  CYS A C   1 
ATOM   3    O  O   . CYS A 1 10  ? -9.747  -12.763 -4.960  1.00 31.11 ? 10  CYS A O   1 
ATOM   4    N  N   . PRO A 1 11  ? -11.871 -12.196 -4.926  1.00 22.64 ? 11  PRO A N   1 
ATOM   5    C  CA  . PRO A 1 11  ? -11.600 -11.314 -3.802  1.00 19.77 ? 11  PRO A CA  1 
ATOM   6    C  C   . PRO A 1 11  ? -11.566 -11.899 -2.411  1.00 19.54 ? 11  PRO A C   1 
ATOM   7    O  O   . PRO A 1 11  ? -11.267 -11.238 -1.433  1.00 18.14 ? 11  PRO A O   1 
ATOM   8    C  CB  . PRO A 1 11  ? -12.723 -10.306 -3.887  1.00 22.03 ? 11  PRO A CB  1 
ATOM   9    C  CG  . PRO A 1 11  ? -13.826 -10.945 -4.512  1.00 23.27 ? 11  PRO A CG  1 
ATOM   10   C  CD  . PRO A 1 11  ? -13.196 -11.880 -5.511  1.00 23.03 ? 11  PRO A CD  1 
ATOM   11   N  N   . LEU A 1 12  ? -11.973 -13.156 -2.317  1.00 16.27 ? 12  LEU A N   1 
ATOM   12   C  CA  . LEU A 1 12  ? -11.960 -13.886 -1.060  1.00 13.83 ? 12  LEU A CA  1 
ATOM   13   C  C   . LEU A 1 12  ? -11.460 -15.305 -1.311  1.00 13.64 ? 12  LEU A C   1 
ATOM   14   O  O   . LEU A 1 12  ? -12.108 -16.088 -2.035  1.00 18.33 ? 12  LEU A O   1 
ATOM   15   C  CB  . LEU A 1 12  ? -13.366 -13.902 -0.411  1.00 16.76 ? 12  LEU A CB  1 
ATOM   16   C  CG  . LEU A 1 12  ? -13.505 -14.629 0.924   1.00 18.24 ? 12  LEU A CG  1 
ATOM   17   C  CD1 . LEU A 1 12  ? -12.568 -14.012 1.984   1.00 17.06 ? 12  LEU A CD1 1 
ATOM   18   C  CD2 . LEU A 1 12  ? -14.949 -14.705 1.441   1.00 19.80 ? 12  LEU A CD2 1 
ATOM   19   N  N   . MET A 1 13  ? -10.306 -15.642 -0.742  1.00 12.73 ? 13  MET A N   1 
ATOM   20   C  CA  . MET A 1 13  ? -9.669  -16.910 -0.955  1.00 13.51 ? 13  MET A CA  1 
ATOM   21   C  C   . MET A 1 13  ? -9.413  -17.476 0.415   1.00 12.55 ? 13  MET A C   1 
ATOM   22   O  O   . MET A 1 13  ? -9.156  -16.745 1.382   1.00 12.72 ? 13  MET A O   1 
ATOM   23   C  CB  . MET A 1 13  ? -8.334  -16.665 -1.715  0.50 11.00 ? 13  MET A CB  1 
ATOM   24   C  CG  . MET A 1 13  ? -8.525  -16.113 -3.140  0.50 16.13 ? 13  MET A CG  1 
ATOM   25   S  SD  . MET A 1 13  ? -7.033  -15.337 -3.833  0.50 26.31 ? 13  MET A SD  1 
ATOM   26   C  CE  . MET A 1 13  ? -7.381  -15.140 -5.586  0.50 28.62 ? 13  MET A CE  1 
ATOM   27   N  N   . VAL A 1 14  ? -9.494  -18.790 0.534   1.00 14.42 ? 14  VAL A N   1 
ATOM   28   C  CA  . VAL A 1 14  ? -9.280  -19.500 1.821   1.00 13.77 ? 14  VAL A CA  1 
ATOM   29   C  C   . VAL A 1 14  ? -8.296  -20.634 1.545   1.00 12.48 ? 14  VAL A C   1 
ATOM   30   O  O   . VAL A 1 14  ? -8.429  -21.346 0.540   1.00 15.65 ? 14  VAL A O   1 
ATOM   31   C  CB  . VAL A 1 14  ? -10.574 -20.028 2.426   1.00 11.04 ? 14  VAL A CB  1 
ATOM   32   C  CG1 . VAL A 1 14  ? -10.328 -20.802 3.707   1.00 12.53 ? 14  VAL A CG1 1 
ATOM   33   C  CG2 . VAL A 1 14  ? -11.631 -18.895 2.639   1.00 12.88 ? 14  VAL A CG2 1 
ATOM   34   N  N   . LYS A 1 15  ? -7.314  -20.766 2.438   1.00 12.61 ? 15  LYS A N   1 
ATOM   35   C  CA  . LYS A 1 15  ? -6.313  -21.796 2.289   1.00 12.67 ? 15  LYS A CA  1 
ATOM   36   C  C   . LYS A 1 15  ? -6.205  -22.520 3.621   1.00 15.32 ? 15  LYS A C   1 
ATOM   37   O  O   . LYS A 1 15  ? -6.070  -21.857 4.656   1.00 18.95 ? 15  LYS A O   1 
ATOM   38   C  CB  . LYS A 1 15  ? -4.949  -21.245 1.895   1.00 19.25 ? 15  LYS A CB  1 
ATOM   39   C  CG  . LYS A 1 15  ? -3.793  -22.264 1.995   1.00 31.89 ? 15  LYS A CG  1 
ATOM   40   C  CD  . LYS A 1 15  ? -3.389  -22.940 0.698   1.00 39.20 ? 15  LYS A CD  1 
ATOM   41   C  CE  . LYS A 1 15  ? -1.951  -23.418 0.682   0.50 37.07 ? 15  LYS A CE  1 
ATOM   42   N  NZ  . LYS A 1 15  ? -1.528  -23.548 -0.744  0.50 40.68 ? 15  LYS A NZ  1 
ATOM   43   N  N   . VAL A 1 16  ? -6.200  -23.860 3.608   1.00 14.89 ? 16  VAL A N   1 
ATOM   44   C  CA  . VAL A 1 16  ? -6.183  -24.616 4.848   1.00 12.78 ? 16  VAL A CA  1 
ATOM   45   C  C   . VAL A 1 16  ? -5.155  -25.702 4.821   1.00 11.76 ? 16  VAL A C   1 
ATOM   46   O  O   . VAL A 1 16  ? -5.077  -26.426 3.859   1.00 14.14 ? 16  VAL A O   1 
ATOM   47   C  CB  . VAL A 1 16  ? -7.582  -25.182 5.119   1.00 13.76 ? 16  VAL A CB  1 
ATOM   48   C  CG1 . VAL A 1 16  ? -7.727  -25.680 6.548   1.00 13.80 ? 16  VAL A CG1 1 
ATOM   49   C  CG2 . VAL A 1 16  ? -8.654  -24.158 4.698   1.00 16.77 ? 16  VAL A CG2 1 
ATOM   50   N  N   . LEU A 1 17  ? -4.427  -25.842 5.916   1.00 11.05 ? 17  LEU A N   1 
ATOM   51   C  CA  . LEU A 1 17  ? -3.373  -26.801 6.058   1.00 10.79 ? 17  LEU A CA  1 
ATOM   52   C  C   . LEU A 1 17  ? -3.650  -27.669 7.296   1.00 11.28 ? 17  LEU A C   1 
ATOM   53   O  O   . LEU A 1 17  ? -4.254  -27.204 8.278   1.00 12.40 ? 17  LEU A O   1 
ATOM   54   C  CB  . LEU A 1 17  ? -2.033  -26.082 6.200   1.00 13.47 ? 17  LEU A CB  1 
ATOM   55   C  CG  . LEU A 1 17  ? -1.555  -25.262 5.016   1.00 13.28 ? 17  LEU A CG  1 
ATOM   56   C  CD1 . LEU A 1 17  ? -0.175  -24.662 5.282   1.00 19.43 ? 17  LEU A CD1 1 
ATOM   57   C  CD2 . LEU A 1 17  ? -1.532  -26.036 3.678   1.00 16.04 ? 17  LEU A CD2 1 
ATOM   58   N  N   . ASP A 1 18  ? -3.148  -28.905 7.254   1.00 10.42 ? 18  ASP A N   1 
ATOM   59   C  CA  . ASP A 1 18  ? -3.345  -29.898 8.299   1.00 9.60  ? 18  ASP A CA  1 
ATOM   60   C  C   . ASP A 1 18  ? -2.003  -30.191 8.979   1.00 10.77 ? 18  ASP A C   1 
ATOM   61   O  O   . ASP A 1 18  ? -1.063  -30.667 8.332   1.00 10.71 ? 18  ASP A O   1 
ATOM   62   C  CB  . ASP A 1 18  ? -3.910  -31.147 7.585   1.00 10.96 ? 18  ASP A CB  1 
ATOM   63   C  CG  . ASP A 1 18  ? -4.074  -32.366 8.437   1.00 13.09 ? 18  ASP A CG  1 
ATOM   64   O  OD1 . ASP A 1 18  ? -3.389  -32.509 9.456   1.00 11.67 ? 18  ASP A OD1 1 
ATOM   65   O  OD2 . ASP A 1 18  ? -4.887  -33.246 8.046   1.00 14.29 ? 18  ASP A OD2 1 
ATOM   66   N  N   . ALA A 1 19  ? -1.973  -29.867 10.270  1.00 8.91  ? 19  ALA A N   1 
ATOM   67   C  CA  . ALA A 1 19  ? -0.777  -29.966 11.116  1.00 10.69 ? 19  ALA A CA  1 
ATOM   68   C  C   . ALA A 1 19  ? -0.488  -31.394 11.595  1.00 10.03 ? 19  ALA A C   1 
ATOM   69   O  O   . ALA A 1 19  ? 0.540   -31.635 12.201  1.00 12.10 ? 19  ALA A O   1 
ATOM   70   C  CB  . ALA A 1 19  ? -0.847  -29.018 12.280  1.00 13.98 ? 19  ALA A CB  1 
ATOM   71   N  N   . VAL A 1 20  ? -1.468  -32.287 11.495  1.00 11.64 ? 20  VAL A N   1 
ATOM   72   C  CA  . VAL A 1 20  ? -1.348  -33.651 11.963  1.00 12.66 ? 20  VAL A CA  1 
ATOM   73   C  C   . VAL A 1 20  ? -0.729  -34.531 10.871  1.00 13.76 ? 20  VAL A C   1 
ATOM   74   O  O   . VAL A 1 20  ? 0.134   -35.381 11.151  1.00 17.74 ? 20  VAL A O   1 
ATOM   75   C  CB  . VAL A 1 20  ? -2.725  -34.221 12.407  1.00 12.16 ? 20  VAL A CB  1 
ATOM   76   C  CG1 . VAL A 1 20  ? -2.664  -35.736 12.582  1.00 16.10 ? 20  VAL A CG1 1 
ATOM   77   C  CG2 . VAL A 1 20  ? -3.252  -33.501 13.678  1.00 13.79 ? 20  VAL A CG2 1 
ATOM   78   N  N   . ARG A 1 21  ? -1.183  -34.320 9.640   1.00 14.51 ? 21  ARG A N   1 
ATOM   79   C  CA  . ARG A 1 21  ? -0.755  -35.113 8.507   1.00 12.04 ? 21  ARG A CA  1 
ATOM   80   C  C   . ARG A 1 21  ? 0.336   -34.469 7.663   1.00 13.19 ? 21  ARG A C   1 
ATOM   81   O  O   . ARG A 1 21  ? 0.973   -35.155 6.848   1.00 15.00 ? 21  ARG A O   1 
ATOM   82   C  CB  . ARG A 1 21  ? -1.945  -35.451 7.609   1.00 15.52 ? 21  ARG A CB  1 
ATOM   83   C  CG  . ARG A 1 21  ? -3.009  -36.347 8.252   1.00 23.81 ? 21  ARG A CG  1 
ATOM   84   C  CD  . ARG A 1 21  ? -4.247  -36.335 7.381   1.00 28.15 ? 21  ARG A CD  1 
ATOM   85   N  NE  . ARG A 1 21  ? -4.207  -37.198 6.239   1.00 41.63 ? 21  ARG A NE  1 
ATOM   86   C  CZ  . ARG A 1 21  ? -4.244  -36.787 4.975   1.00 33.22 ? 21  ARG A CZ  1 
ATOM   87   N  N   . GLY A 1 22  ? 0.560   -33.178 7.822   1.00 12.10 ? 22  GLY A N   1 
ATOM   88   C  CA  . GLY A 1 22  ? 1.599   -32.525 7.061   1.00 12.60 ? 22  GLY A CA  1 
ATOM   89   C  C   . GLY A 1 22  ? 1.190   -32.403 5.582   1.00 12.74 ? 22  GLY A C   1 
ATOM   90   O  O   . GLY A 1 22  ? 1.920   -32.663 4.642   1.00 12.22 ? 22  GLY A O   1 
ATOM   91   N  N   . SER A 1 23  ? -0.022  -31.922 5.417   1.00 13.03 ? 23  SER A N   1 
ATOM   92   C  CA  . SER A 1 23  ? -0.639  -31.854 4.091   1.00 14.12 ? 23  SER A CA  1 
ATOM   93   C  C   . SER A 1 23  ? -1.560  -30.681 4.033   1.00 11.31 ? 23  SER A C   1 
ATOM   94   O  O   . SER A 1 23  ? -1.995  -30.143 5.052   1.00 12.08 ? 23  SER A O   1 
ATOM   95   C  CB  . SER A 1 23  ? -1.440  -33.130 3.806   1.00 14.51 ? 23  SER A CB  1 
ATOM   96   O  OG  . SER A 1 23  ? -2.571  -33.226 4.643   1.00 18.34 ? 23  SER A OG  1 
ATOM   97   N  N   . PRO A 1 24  ? -1.986  -30.344 2.832   1.00 11.01 ? 24  PRO A N   1 
ATOM   98   C  CA  . PRO A 1 24  ? -3.142  -29.513 2.750   1.00 10.60 ? 24  PRO A CA  1 
ATOM   99   C  C   . PRO A 1 24  ? -4.347  -30.177 3.332   1.00 11.95 ? 24  PRO A C   1 
ATOM   100  O  O   . PRO A 1 24  ? -4.412  -31.404 3.345   1.00 12.24 ? 24  PRO A O   1 
ATOM   101  C  CB  . PRO A 1 24  ? -3.331  -29.287 1.246   1.00 13.00 ? 24  PRO A CB  1 
ATOM   102  C  CG  . PRO A 1 24  ? -2.447  -30.245 0.572   1.00 23.50 ? 24  PRO A CG  1 
ATOM   103  C  CD  . PRO A 1 24  ? -1.522  -30.826 1.531   1.00 14.32 ? 24  PRO A CD  1 
ATOM   104  N  N   . ALA A 1 25  ? -5.312  -29.367 3.795   1.00 10.38 ? 25  ALA A N   1 
ATOM   105  C  CA  . ALA A 1 25  ? -6.564  -29.915 4.256   1.00 9.89  ? 25  ALA A CA  1 
ATOM   106  C  C   . ALA A 1 25  ? -7.493  -29.956 3.048   1.00 11.67 ? 25  ALA A C   1 
ATOM   107  O  O   . ALA A 1 25  ? -7.985  -28.927 2.598   1.00 11.83 ? 25  ALA A O   1 
ATOM   108  C  CB  . ALA A 1 25  ? -7.123  -29.077 5.396   1.00 14.16 ? 25  ALA A CB  1 
ATOM   109  N  N   . ILE A 1 26  ? -7.683  -31.165 2.527   1.00 13.53 ? 26  ILE A N   1 
ATOM   110  C  CA  . ILE A 1 26  ? -8.380  -31.367 1.301   1.00 12.67 ? 26  ILE A CA  1 
ATOM   111  C  C   . ILE A 1 26  ? -9.862  -31.676 1.534   1.00 12.20 ? 26  ILE A C   1 
ATOM   112  O  O   . ILE A 1 26  ? -10.216 -32.370 2.475   1.00 13.21 ? 26  ILE A O   1 
ATOM   113  C  CB  . ILE A 1 26  ? -7.723  -32.529 0.516   1.00 16.25 ? 26  ILE A CB  1 
ATOM   114  C  CG1 . ILE A 1 26  ? -6.212  -32.331 0.260   1.00 16.96 ? 26  ILE A CG1 1 
ATOM   115  C  CG2 . ILE A 1 26  ? -8.457  -32.901 -0.765  1.00 21.03 ? 26  ILE A CG2 1 
ATOM   116  C  CD1 . ILE A 1 26  ? -5.460  -33.607 -0.159  1.00 23.15 ? 26  ILE A CD1 1 
ATOM   117  N  N   . ASN A 1 27  ? -10.705 -31.098 0.662   1.00 12.45 ? 27  ASN A N   1 
ATOM   118  C  CA  . ASN A 1 27  ? -12.162 -31.298 0.733   1.00 14.50 ? 27  ASN A CA  1 
ATOM   119  C  C   . ASN A 1 27  ? -12.788 -30.941 2.109   1.00 12.51 ? 27  ASN A C   1 
ATOM   120  O  O   . ASN A 1 27  ? -13.704 -31.611 2.587   1.00 16.92 ? 27  ASN A O   1 
ATOM   121  C  CB  . ASN A 1 27  ? -12.458 -32.749 0.412   1.00 13.37 ? 27  ASN A CB  1 
ATOM   122  C  CG  . ASN A 1 27  ? -12.141 -33.094 -1.034  1.00 17.52 ? 27  ASN A CG  1 
ATOM   123  O  OD1 . ASN A 1 27  ? -11.785 -34.237 -1.341  1.00 24.82 ? 27  ASN A OD1 1 
ATOM   124  N  ND2 . ASN A 1 27  ? -12.247 -32.118 -1.927  1.00 20.00 ? 27  ASN A ND2 1 
ATOM   125  N  N   . VAL A 1 28  ? -12.317 -29.842 2.698   1.00 13.16 ? 28  VAL A N   1 
ATOM   126  C  CA  . VAL A 1 28  ? -12.872 -29.308 3.920   1.00 12.22 ? 28  VAL A CA  1 
ATOM   127  C  C   . VAL A 1 28  ? -13.934 -28.260 3.521   1.00 12.38 ? 28  VAL A C   1 
ATOM   128  O  O   . VAL A 1 28  ? -13.685 -27.394 2.679   1.00 12.09 ? 28  VAL A O   1 
ATOM   129  C  CB  . VAL A 1 28  ? -11.809 -28.620 4.786   1.00 17.78 ? 28  VAL A CB  1 
ATOM   130  C  CG1 . VAL A 1 28  ? -12.503 -28.230 6.094   1.00 19.31 ? 28  VAL A CG1 1 
ATOM   131  C  CG2 . VAL A 1 28  ? -10.649 -29.523 5.108   1.00 26.69 ? 28  VAL A CG2 1 
ATOM   132  N  N   . ALA A 1 29  ? -15.087 -28.345 4.129   1.00 10.96 ? 29  ALA A N   1 
ATOM   133  C  CA  . ALA A 1 29  ? -16.202 -27.415 3.889   1.00 10.20 ? 29  ALA A CA  1 
ATOM   134  C  C   . ALA A 1 29  ? -15.912 -26.070 4.507   1.00 11.06 ? 29  ALA A C   1 
ATOM   135  O  O   . ALA A 1 29  ? -15.484 -25.982 5.631   1.00 12.72 ? 29  ALA A O   1 
ATOM   136  C  CB  . ALA A 1 29  ? -17.527 -27.977 4.422   1.00 13.51 ? 29  ALA A CB  1 
ATOM   137  N  N   . VAL A 1 30  ? -16.172 -25.008 3.744   1.00 10.75 ? 30  VAL A N   1 
ATOM   138  C  CA  . VAL A 1 30  ? -16.031 -23.651 4.179   1.00 11.77 ? 30  VAL A CA  1 
ATOM   139  C  C   . VAL A 1 30  ? -17.346 -22.916 3.897   1.00 10.44 ? 30  VAL A C   1 
ATOM   140  O  O   . VAL A 1 30  ? -17.792 -22.886 2.765   1.00 11.15 ? 30  VAL A O   1 
ATOM   141  C  CB  . VAL A 1 30  ? -14.883 -22.940 3.495   1.00 12.30 ? 30  VAL A CB  1 
ATOM   142  C  CG1 . VAL A 1 30  ? -14.714 -21.474 4.019   1.00 14.58 ? 30  VAL A CG1 1 
ATOM   143  C  CG2 . VAL A 1 30  ? -13.587 -23.711 3.732   1.00 13.40 ? 30  VAL A CG2 1 
ATOM   144  N  N   . HIS A 1 31  ? -17.919 -22.340 4.948   1.00 10.10 ? 31  HIS A N   1 
ATOM   145  C  CA  . HIS A 1 31  ? -19.141 -21.521 4.782   1.00 10.54 ? 31  HIS A CA  1 
ATOM   146  C  C   . HIS A 1 31  ? -18.853 -20.067 5.142   1.00 12.11 ? 31  HIS A C   1 
ATOM   147  O  O   . HIS A 1 31  ? -18.235 -19.824 6.169   1.00 16.81 ? 31  HIS A O   1 
ATOM   148  C  CB  . HIS A 1 31  ? -20.260 -21.994 5.699   1.00 15.67 ? 31  HIS A CB  1 
ATOM   149  C  CG  . HIS A 1 31  ? -20.710 -23.385 5.425   1.00 21.45 ? 31  HIS A CG  1 
ATOM   150  N  ND1 . HIS A 1 31  ? -21.839 -23.651 4.698   1.00 24.22 ? 31  HIS A ND1 1 
ATOM   151  C  CD2 . HIS A 1 31  ? -20.187 -24.577 5.774   1.00 25.69 ? 31  HIS A CD2 1 
ATOM   152  C  CE1 . HIS A 1 31  ? -22.006 -24.952 4.612   1.00 28.97 ? 31  HIS A CE1 1 
ATOM   153  N  NE2 . HIS A 1 31  ? -21.010 -25.539 5.268   1.00 33.88 ? 31  HIS A NE2 1 
ATOM   154  N  N   . VAL A 1 32  ? -19.332 -19.160 4.299   1.00 10.26 ? 32  VAL A N   1 
ATOM   155  C  CA  . VAL A 1 32  ? -19.152 -17.753 4.558   1.00 10.94 ? 32  VAL A CA  1 
ATOM   156  C  C   . VAL A 1 32  ? -20.535 -17.174 4.793   1.00 12.07 ? 32  VAL A C   1 
ATOM   157  O  O   . VAL A 1 32  ? -21.480 -17.419 4.047   1.00 11.74 ? 32  VAL A O   1 
ATOM   158  C  CB  . VAL A 1 32  ? -18.484 -17.052 3.376   1.00 10.66 ? 32  VAL A CB  1 
ATOM   159  C  CG1 . VAL A 1 32  ? -18.156 -15.602 3.732   1.00 11.49 ? 32  VAL A CG1 1 
ATOM   160  C  CG2 . VAL A 1 32  ? -17.230 -17.744 2.926   1.00 13.16 ? 32  VAL A CG2 1 
ATOM   161  N  N   . PHE A 1 33  ? -20.671 -16.412 5.830   1.00 11.66 ? 33  PHE A N   1 
ATOM   162  C  CA  . PHE A 1 33  ? -21.891 -15.637 6.143   1.00 12.57 ? 33  PHE A CA  1 
ATOM   163  C  C   . PHE A 1 33  ? -21.577 -14.164 6.231   1.00 13.68 ? 33  PHE A C   1 
ATOM   164  O  O   . PHE A 1 33  ? -20.432 -13.812 6.415   1.00 12.32 ? 33  PHE A O   1 
ATOM   165  C  CB  . PHE A 1 33  ? -22.477 -16.092 7.463   1.00 10.39 ? 33  PHE A CB  1 
ATOM   166  C  CG  . PHE A 1 33  ? -22.687 -17.568 7.555   1.00 11.87 ? 33  PHE A CG  1 
ATOM   167  C  CD1 . PHE A 1 33  ? -21.661 -18.435 7.927   1.00 14.62 ? 33  PHE A CD1 1 
ATOM   168  C  CD2 . PHE A 1 33  ? -23.926 -18.091 7.325   1.00 17.43 ? 33  PHE A CD2 1 
ATOM   169  C  CE1 . PHE A 1 33  ? -21.877 -19.817 8.090   1.00 15.09 ? 33  PHE A CE1 1 
ATOM   170  C  CE2 . PHE A 1 33  ? -24.169 -19.431 7.444   1.00 18.67 ? 33  PHE A CE2 1 
ATOM   171  C  CZ  . PHE A 1 33  ? -23.151 -20.293 7.828   1.00 14.18 ? 33  PHE A CZ  1 
ATOM   172  N  N   . ARG A 1 34  ? -22.616 -13.360 6.039   1.00 11.34 ? 34  ARG A N   1 
ATOM   173  C  CA  . ARG A 1 34  ? -22.478 -11.895 6.140   1.00 11.77 ? 34  ARG A CA  1 
ATOM   174  C  C   . ARG A 1 34  ? -23.538 -11.403 7.126   1.00 12.11 ? 34  ARG A C   1 
ATOM   175  O  O   . ARG A 1 34  ? -24.664 -11.854 7.060   1.00 14.26 ? 34  ARG A O   1 
ATOM   176  C  CB  . ARG A 1 34  ? -22.616 -11.251 4.758   1.00 14.07 ? 34  ARG A CB  1 
ATOM   177  C  CG  . ARG A 1 34  ? -22.309 -9.761  4.739   1.00 17.06 ? 34  ARG A CG  1 
ATOM   178  C  CD  . ARG A 1 34  ? -22.753 -9.073  3.462   1.00 20.05 ? 34  ARG A CD  1 
ATOM   179  N  NE  . ARG A 1 34  ? -22.700 -7.633  3.641   1.00 27.20 ? 34  ARG A NE  1 
ATOM   180  C  CZ  . ARG A 1 34  ? -23.737 -6.877  3.976   1.00 21.85 ? 34  ARG A CZ  1 
ATOM   181  N  NH1 . ARG A 1 34  ? -24.928 -7.423  4.157   1.00 22.49 ? 34  ARG A NH1 1 
ATOM   182  N  NH2 . ARG A 1 34  ? -23.575 -5.577  4.130   1.00 24.04 ? 34  ARG A NH2 1 
ATOM   183  N  N   . LYS A 1 35  ? -23.138 -10.492 8.000   1.00 12.86 ? 35  LYS A N   1 
ATOM   184  C  CA  . LYS A 1 35  ? -24.055 -10.026 9.022   1.00 16.11 ? 35  LYS A CA  1 
ATOM   185  C  C   . LYS A 1 35  ? -25.224 -9.193  8.531   1.00 19.97 ? 35  LYS A C   1 
ATOM   186  O  O   . LYS A 1 35  ? -24.998 -8.212  7.850   1.00 16.97 ? 35  LYS A O   1 
ATOM   187  C  CB  . LYS A 1 35  ? -23.287 -9.357  10.169  1.00 14.93 ? 35  LYS A CB  1 
ATOM   188  C  CG  . LYS A 1 35  ? -24.095 -9.112  11.430  1.00 23.54 ? 35  LYS A CG  1 
ATOM   189  C  CD  . LYS A 1 35  ? -23.172 -8.732  12.591  1.00 27.80 ? 35  LYS A CD  1 
ATOM   190  N  N   . ALA A 1 36  ? -26.472 -9.610  8.867   1.00 20.56 ? 36  ALA A N   1 
ATOM   191  C  CA  . ALA A 1 36  ? -27.591 -8.964  8.271   1.00 23.08 ? 36  ALA A CA  1 
ATOM   192  C  C   . ALA A 1 36  ? -28.046 -7.810  9.137   1.00 27.62 ? 36  ALA A C   1 
ATOM   193  O  O   . ALA A 1 36  ? -27.568 -7.582  10.254  1.00 29.00 ? 36  ALA A O   1 
ATOM   194  C  CB  . ALA A 1 36  ? -28.724 -9.947  7.968   1.00 32.60 ? 36  ALA A CB  1 
ATOM   195  N  N   . ALA A 1 37  ? -28.987 -7.057  8.573   1.00 35.57 ? 37  ALA A N   1 
ATOM   196  C  CA  . ALA A 1 37  ? -29.646 -5.961  9.231   1.00 31.27 ? 37  ALA A CA  1 
ATOM   197  C  C   . ALA A 1 37  ? -29.953 -6.232  10.755  1.00 34.27 ? 37  ALA A C   1 
ATOM   198  O  O   . ALA A 1 37  ? -29.662 -5.370  11.603  1.00 34.20 ? 37  ALA A O   1 
ATOM   199  C  CB  . ALA A 1 37  ? -30.902 -5.529  8.417   1.00 30.81 ? 37  ALA A CB  1 
ATOM   200  N  N   . THR A 1 40  ? -28.233 -11.169 12.601  1.00 35.20 ? 40  THR A N   1 
ATOM   201  C  CA  . THR A 1 40  ? -28.270 -12.556 12.166  1.00 30.21 ? 40  THR A CA  1 
ATOM   202  C  C   . THR A 1 40  ? -27.326 -12.747 10.963  1.00 30.72 ? 40  THR A C   1 
ATOM   203  O  O   . THR A 1 40  ? -27.102 -11.855 10.173  1.00 31.60 ? 40  THR A O   1 
ATOM   204  C  CB  . THR A 1 40  ? -29.687 -13.076 11.875  1.00 26.57 ? 40  THR A CB  1 
ATOM   205  O  OG1 . THR A 1 40  ? -30.135 -12.606 10.614  1.00 37.07 ? 40  THR A OG1 1 
ATOM   206  C  CG2 . THR A 1 40  ? -30.646 -12.697 12.954  1.00 36.99 ? 40  THR A CG2 1 
ATOM   207  N  N   . TRP A 1 41  ? -26.795 -13.954 10.876  1.00 28.54 ? 41  TRP A N   1 
ATOM   208  C  CA  . TRP A 1 41  ? -25.842 -14.345 9.843   1.00 25.46 ? 41  TRP A CA  1 
ATOM   209  C  C   . TRP A 1 41  ? -26.517 -14.879 8.603   1.00 27.11 ? 41  TRP A C   1 
ATOM   210  O  O   . TRP A 1 41  ? -27.086 -16.002 8.642   1.00 36.68 ? 41  TRP A O   1 
ATOM   211  C  CB  . TRP A 1 41  ? -24.988 -15.457 10.426  1.00 22.40 ? 41  TRP A CB  1 
ATOM   212  C  CG  . TRP A 1 41  ? -24.044 -14.981 11.475  1.00 22.62 ? 41  TRP A CG  1 
ATOM   213  C  CD1 . TRP A 1 41  ? -23.949 -15.374 12.821  1.00 27.45 ? 41  TRP A CD1 1 
ATOM   214  C  CD2 . TRP A 1 41  ? -22.986 -14.066 11.247  1.00 26.90 ? 41  TRP A CD2 1 
ATOM   215  N  NE1 . TRP A 1 41  ? -22.916 -14.719 13.433  1.00 29.39 ? 41  TRP A NE1 1 
ATOM   216  C  CE2 . TRP A 1 41  ? -22.279 -13.914 12.519  1.00 30.20 ? 41  TRP A CE2 1 
ATOM   217  C  CE3 . TRP A 1 41  ? -22.534 -13.386 10.130  1.00 18.40 ? 41  TRP A CE3 1 
ATOM   218  C  CZ2 . TRP A 1 41  ? -21.172 -13.070 12.635  1.00 26.69 ? 41  TRP A CZ2 1 
ATOM   219  C  CZ3 . TRP A 1 41  ? -21.442 -12.607 10.280  1.00 16.52 ? 41  TRP A CZ3 1 
ATOM   220  C  CH2 . TRP A 1 41  ? -20.800 -12.402 11.516  1.00 18.74 ? 41  TRP A CH2 1 
ATOM   221  N  N   . GLU A 1 42  ? -26.483 -14.111 7.498   1.00 20.85 ? 42  GLU A N   1 
ATOM   222  C  CA  . GLU A 1 42  ? -27.097 -14.564 6.272   1.00 18.75 ? 42  GLU A CA  1 
ATOM   223  C  C   . GLU A 1 42  ? -26.058 -15.339 5.491   1.00 16.90 ? 42  GLU A C   1 
ATOM   224  O  O   . GLU A 1 42  ? -24.915 -14.932 5.362   1.00 14.18 ? 42  GLU A O   1 
ATOM   225  C  CB  . GLU A 1 42  ? -27.622 -13.491 5.393   1.00 24.98 ? 42  GLU A CB  1 
ATOM   226  N  N   . PRO A 1 43  ? -26.488 -16.445 4.903   1.00 14.22 ? 43  PRO A N   1 
ATOM   227  C  CA  . PRO A 1 43  ? -25.567 -17.178 4.016   1.00 15.08 ? 43  PRO A CA  1 
ATOM   228  C  C   . PRO A 1 43  ? -25.027 -16.280 2.899   1.00 14.41 ? 43  PRO A C   1 
ATOM   229  O  O   . PRO A 1 43  ? -25.773 -15.502 2.302   1.00 18.06 ? 43  PRO A O   1 
ATOM   230  C  CB  . PRO A 1 43  ? -26.466 -18.276 3.413   1.00 20.08 ? 43  PRO A CB  1 
ATOM   231  C  CG  . PRO A 1 43  ? -27.890 -17.681 3.484   1.00 29.25 ? 43  PRO A CG  1 
ATOM   232  C  CD  . PRO A 1 43  ? -27.884 -16.940 4.808   1.00 26.94 ? 43  PRO A CD  1 
ATOM   233  N  N   . PHE A 1 44  ? -23.735 -16.372 2.632   1.00 12.70 ? 44  PHE A N   1 
ATOM   234  C  CA  . PHE A 1 44  ? -23.089 -15.585 1.594   1.00 12.38 ? 44  PHE A CA  1 
ATOM   235  C  C   . PHE A 1 44  ? -22.487 -16.460 0.448   1.00 11.87 ? 44  PHE A C   1 
ATOM   236  O  O   . PHE A 1 44  ? -22.764 -16.190 -0.716  1.00 14.09 ? 44  PHE A O   1 
ATOM   237  C  CB  . PHE A 1 44  ? -22.072 -14.615 2.225   1.00 14.06 ? 44  PHE A CB  1 
ATOM   238  C  CG  . PHE A 1 44  ? -21.327 -13.817 1.234   1.00 10.64 ? 44  PHE A CG  1 
ATOM   239  C  CD1 . PHE A 1 44  ? -21.885 -12.689 0.666   1.00 12.92 ? 44  PHE A CD1 1 
ATOM   240  C  CD2 . PHE A 1 44  ? -20.067 -14.227 0.762   1.00 13.24 ? 44  PHE A CD2 1 
ATOM   241  C  CE1 . PHE A 1 44  ? -21.167 -11.998 -0.308  1.00 12.21 ? 44  PHE A CE1 1 
ATOM   242  C  CE2 . PHE A 1 44  ? -19.375 -13.509 -0.208  1.00 14.32 ? 44  PHE A CE2 1 
ATOM   243  C  CZ  . PHE A 1 44  ? -19.953 -12.396 -0.739  1.00 13.98 ? 44  PHE A CZ  1 
ATOM   244  N  N   . ALA A 1 45  ? -21.682 -17.475 0.780   1.00 12.55 ? 45  ALA A N   1 
ATOM   245  C  CA  . ALA A 1 45  ? -21.062 -18.325 -0.192  1.00 13.95 ? 45  ALA A CA  1 
ATOM   246  C  C   . ALA A 1 45  ? -20.509 -19.504 0.565   1.00 12.02 ? 45  ALA A C   1 
ATOM   247  O  O   . ALA A 1 45  ? -20.293 -19.426 1.777   1.00 13.61 ? 45  ALA A O   1 
ATOM   248  C  CB  . ALA A 1 45  ? -19.902 -17.606 -0.897  1.00 17.78 ? 45  ALA A CB  1 
ATOM   249  N  N   . SER A 1 46  ? -20.226 -20.588 -0.127  1.00 13.68 ? 46  SER A N   1 
ATOM   250  C  CA  . SER A 1 46  ? -19.574 -21.724 0.479   1.00 10.71 ? 46  SER A CA  1 
ATOM   251  C  C   . SER A 1 46  ? -18.918 -22.585 -0.586  1.00 11.12 ? 46  SER A C   1 
ATOM   252  O  O   . SER A 1 46  ? -19.125 -22.438 -1.767  1.00 12.59 ? 46  SER A O   1 
ATOM   253  C  CB  . SER A 1 46  ? -20.582 -22.533 1.295   1.00 12.00 ? 46  SER A CB  1 
ATOM   254  O  OG  . SER A 1 46  ? -21.716 -22.940 0.512   1.00 13.05 ? 46  SER A OG  1 
ATOM   255  N  N   . GLY A 1 47  ? -18.021 -23.448 -0.163  1.00 11.12 ? 47  GLY A N   1 
ATOM   256  C  CA  . GLY A 1 47  ? -17.275 -24.275 -1.029  1.00 11.57 ? 47  GLY A CA  1 
ATOM   257  C  C   . GLY A 1 47  ? -16.480 -25.293 -0.264  1.00 9.93  ? 47  GLY A C   1 
ATOM   258  O  O   . GLY A 1 47  ? -16.619 -25.385 0.968   1.00 10.52 ? 47  GLY A O   1 
ATOM   259  N  N   . LYS A 1 48  ? -15.709 -26.093 -0.986  1.00 11.30 ? 48  LYS A N   1 
ATOM   260  C  CA  . LYS A 1 48  ? -14.769 -27.057 -0.381  1.00 12.38 ? 48  LYS A CA  1 
ATOM   261  C  C   . LYS A 1 48  ? -13.377 -26.803 -0.871  1.00 12.24 ? 48  LYS A C   1 
ATOM   262  O  O   . LYS A 1 48  ? -13.175 -26.420 -2.033  1.00 12.67 ? 48  LYS A O   1 
ATOM   263  C  CB  . LYS A 1 48  ? -15.171 -28.517 -0.652  1.00 16.17 ? 48  LYS A CB  1 
ATOM   264  C  CG  . LYS A 1 48  ? -16.324 -29.032 0.268   1.00 17.83 ? 48  LYS A CG  1 
ATOM   265  C  CD  . LYS A 1 48  ? -16.280 -30.538 0.463   1.00 21.67 ? 48  LYS A CD  1 
ATOM   266  C  CE  . LYS A 1 48  ? -16.973 -31.028 1.735   1.00 27.98 ? 48  LYS A CE  1 
ATOM   267  N  NZ  . LYS A 1 48  ? -16.424 -32.381 1.986   1.00 38.80 ? 48  LYS A NZ  1 
ATOM   268  N  N   . THR A 1 49  ? -12.403 -26.996 -0.013  1.00 10.97 ? 49  THR A N   1 
ATOM   269  C  CA  . THR A 1 49  ? -11.031 -26.895 -0.444  1.00 12.85 ? 49  THR A CA  1 
ATOM   270  C  C   . THR A 1 49  ? -10.638 -27.939 -1.467  1.00 13.32 ? 49  THR A C   1 
ATOM   271  O  O   . THR A 1 49  ? -11.100 -29.084 -1.428  1.00 12.65 ? 49  THR A O   1 
ATOM   272  C  CB  . THR A 1 49  ? -10.087 -26.915 0.743   1.00 11.74 ? 49  THR A CB  1 
ATOM   273  O  OG1 . THR A 1 49  ? -10.184 -28.168 1.430   1.00 11.76 ? 49  THR A OG1 1 
ATOM   274  C  CG2 . THR A 1 49  ? -10.309 -25.744 1.715   1.00 13.00 ? 49  THR A CG2 1 
ATOM   275  N  N   . SER A 1 50  ? -9.729  -27.545 -2.341  1.00 11.19 ? 50  SER A N   1 
ATOM   276  C  CA  . SER A 1 50  ? -9.145  -28.394 -3.338  1.00 11.67 ? 50  SER A CA  1 
ATOM   277  C  C   . SER A 1 50  ? -8.067  -29.326 -2.823  1.00 11.79 ? 50  SER A C   1 
ATOM   278  O  O   . SER A 1 50  ? -7.760  -29.340 -1.615  1.00 12.88 ? 50  SER A O   1 
ATOM   279  C  CB  . SER A 1 50  ? -8.566  -27.534 -4.430  1.00 14.64 ? 50  SER A CB  1 
ATOM   280  O  OG  . SER A 1 50  ? -7.357  -26.957 -3.951  1.00 15.05 ? 50  SER A OG  1 
ATOM   281  N  N   . GLU A 1 51  ? -7.465  -30.060 -3.772  1.00 15.95 ? 51  GLU A N   1 
ATOM   282  C  CA  . GLU A 1 51  ? -6.372  -30.943 -3.442  1.00 14.89 ? 51  GLU A CA  1 
ATOM   283  C  C   . GLU A 1 51  ? -5.145  -30.203 -2.907  1.00 15.18 ? 51  GLU A C   1 
ATOM   284  O  O   . GLU A 1 51  ? -4.284  -30.798 -2.244  1.00 19.04 ? 51  GLU A O   1 
ATOM   285  C  CB  . GLU A 1 51  ? -6.004  -31.837 -4.664  1.00 19.60 ? 51  GLU A CB  1 
ATOM   286  C  CG  . GLU A 1 51  ? -6.888  -33.078 -4.920  1.00 25.12 ? 51  GLU A CG  1 
ATOM   287  C  CD  . GLU A 1 51  ? -6.560  -33.890 -6.243  1.00 33.85 ? 51  GLU A CD  1 
ATOM   288  N  N   . SER A 1 52  ? -5.042  -28.909 -3.213  1.00 13.94 ? 52  SER A N   1 
ATOM   289  C  CA  . SER A 1 52  ? -4.005  -28.068 -2.634  1.00 13.96 ? 52  SER A CA  1 
ATOM   290  C  C   . SER A 1 52  ? -4.364  -27.326 -1.333  1.00 12.94 ? 52  SER A C   1 
ATOM   291  O  O   . SER A 1 52  ? -3.638  -26.460 -0.897  1.00 15.31 ? 52  SER A O   1 
ATOM   292  C  CB  . SER A 1 52  ? -3.546  -27.044 -3.699  1.00 23.26 ? 52  SER A CB  1 
ATOM   293  O  OG  . SER A 1 52  ? -4.607  -26.122 -3.952  1.00 28.11 ? 52  SER A OG  1 
ATOM   294  N  N   . GLY A 1 53  ? -5.556  -27.570 -0.799  1.00 12.68 ? 53  GLY A N   1 
ATOM   295  C  CA  . GLY A 1 53  ? -6.042  -26.910 0.378   1.00 12.13 ? 53  GLY A CA  1 
ATOM   296  C  C   . GLY A 1 53  ? -6.646  -25.540 0.107   1.00 11.54 ? 53  GLY A C   1 
ATOM   297  O  O   . GLY A 1 53  ? -6.896  -24.835 1.066   1.00 14.52 ? 53  GLY A O   1 
ATOM   298  N  N   . GLU A 1 54  ? -6.910  -25.231 -1.156  1.00 13.21 ? 54  GLU A N   1 
ATOM   299  C  CA  . GLU A 1 54  ? -7.330  -23.867 -1.472  1.00 13.14 ? 54  GLU A CA  1 
ATOM   300  C  C   . GLU A 1 54  ? -8.753  -23.840 -1.982  1.00 12.65 ? 54  GLU A C   1 
ATOM   301  O  O   . GLU A 1 54  ? -9.191  -24.792 -2.577  1.00 13.75 ? 54  GLU A O   1 
ATOM   302  C  CB  . GLU A 1 54  ? -6.441  -23.288 -2.566  1.00 16.81 ? 54  GLU A CB  1 
ATOM   303  C  CG  . GLU A 1 54  ? -5.002  -23.066 -2.169  1.00 17.87 ? 54  GLU A CG  1 
ATOM   304  C  CD  . GLU A 1 54  ? -4.204  -22.591 -3.369  1.00 25.58 ? 54  GLU A CD  1 
ATOM   305  O  OE1 . GLU A 1 54  ? -3.869  -21.410 -3.413  1.00 32.25 ? 54  GLU A OE1 1 
ATOM   306  O  OE2 . GLU A 1 54  ? -3.979  -23.402 -4.280  1.00 36.42 ? 54  GLU A OE2 1 
ATOM   307  N  N   . LEU A 1 55  ? -9.411  -22.721 -1.739  1.00 12.72 ? 55  LEU A N   1 
ATOM   308  C  CA  . LEU A 1 55  ? -10.733 -22.557 -2.175  1.00 14.31 ? 55  LEU A CA  1 
ATOM   309  C  C   . LEU A 1 55  ? -10.761 -21.157 -2.803  1.00 16.42 ? 55  LEU A C   1 
ATOM   310  O  O   . LEU A 1 55  ? -10.677 -20.097 -2.106  1.00 15.60 ? 55  LEU A O   1 
ATOM   311  C  CB  . LEU A 1 55  ? -11.633 -22.617 -0.948  1.00 15.18 ? 55  LEU A CB  1 
ATOM   312  C  CG  . LEU A 1 55  ? -13.086 -22.270 -1.157  1.00 16.26 ? 55  LEU A CG  1 
ATOM   313  C  CD1 . LEU A 1 55  ? -13.724 -22.974 -2.362  1.00 18.35 ? 55  LEU A CD1 1 
ATOM   314  C  CD2 . LEU A 1 55  ? -13.876 -22.500 0.128   1.00 21.21 ? 55  LEU A CD2 1 
ATOM   315  N  N   . HIS A 1 56  ? -10.853 -21.223 -4.119  1.00 20.78 ? 56  HIS A N   1 
ATOM   316  C  CA  . HIS A 1 56  ? -10.972 -20.126 -5.020  1.00 23.12 ? 56  HIS A CA  1 
ATOM   317  C  C   . HIS A 1 56  ? -12.412 -20.165 -5.534  1.00 23.11 ? 56  HIS A C   1 
ATOM   318  O  O   . HIS A 1 56  ? -13.124 -21.194 -5.542  1.00 27.07 ? 56  HIS A O   1 
ATOM   319  C  CB  . HIS A 1 56  ? -9.985  -20.288 -6.199  1.00 27.45 ? 56  HIS A CB  1 
ATOM   320  C  CG  . HIS A 1 56  ? -8.540  -20.271 -5.793  1.00 32.84 ? 56  HIS A CG  1 
ATOM   321  N  ND1 . HIS A 1 56  ? -7.860  -19.122 -5.595  1.00 36.65 ? 56  HIS A ND1 1 
ATOM   322  C  CD2 . HIS A 1 56  ? -7.651  -21.314 -5.539  1.00 38.52 ? 56  HIS A CD2 1 
ATOM   323  C  CE1 . HIS A 1 56  ? -6.590  -19.421 -5.223  1.00 36.74 ? 56  HIS A CE1 1 
ATOM   324  N  NE2 . HIS A 1 56  ? -6.470  -20.763 -5.183  1.00 34.17 ? 56  HIS A NE2 1 
ATOM   325  N  N   . GLY A 1 57  ? -12.848 -19.031 -5.981  1.00 24.31 ? 57  GLY A N   1 
ATOM   326  C  CA  . GLY A 1 57  ? -14.129 -18.928 -6.592  1.00 23.59 ? 57  GLY A CA  1 
ATOM   327  C  C   . GLY A 1 57  ? -15.333 -18.879 -5.670  1.00 19.60 ? 57  GLY A C   1 
ATOM   328  O  O   . GLY A 1 57  ? -16.466 -19.076 -6.124  1.00 22.52 ? 57  GLY A O   1 
ATOM   329  N  N   . LEU A 1 58  ? -15.103 -18.529 -4.410  1.00 17.27 ? 58  LEU A N   1 
ATOM   330  C  CA  . LEU A 1 58  ? -16.221 -18.314 -3.498  1.00 16.07 ? 58  LEU A CA  1 
ATOM   331  C  C   . LEU A 1 58  ? -17.176 -17.252 -3.916  1.00 20.32 ? 58  LEU A C   1 
ATOM   332  O  O   . LEU A 1 58  ? -18.381 -17.431 -3.778  1.00 23.24 ? 58  LEU A O   1 
ATOM   333  C  CB  . LEU A 1 58  ? -15.726 -17.997 -2.106  1.00 18.20 ? 58  LEU A CB  1 
ATOM   334  C  CG  . LEU A 1 58  ? -15.357 -19.098 -1.243  1.00 19.31 ? 58  LEU A CG  1 
ATOM   335  C  CD1 . LEU A 1 58  ? -14.617 -18.563 -0.033  1.00 22.48 ? 58  LEU A CD1 1 
ATOM   336  C  CD2 . LEU A 1 58  ? -16.594 -19.943 -0.891  1.00 20.26 ? 58  LEU A CD2 1 
ATOM   337  N  N   . THR A 1 59  ? -16.637 -16.136 -4.371  1.00 19.51 ? 59  THR A N   1 
ATOM   338  C  CA  . THR A 1 59  ? -17.455 -15.002 -4.652  1.00 17.67 ? 59  THR A CA  1 
ATOM   339  C  C   . THR A 1 59  ? -16.871 -14.235 -5.776  1.00 19.68 ? 59  THR A C   1 
ATOM   340  O  O   . THR A 1 59  ? -15.844 -14.637 -6.358  1.00 22.22 ? 59  THR A O   1 
ATOM   341  C  CB  . THR A 1 59  ? -17.650 -14.136 -3.423  1.00 19.74 ? 59  THR A CB  1 
ATOM   342  O  OG1 . THR A 1 59  ? -18.724 -13.262 -3.638  1.00 21.80 ? 59  THR A OG1 1 
ATOM   343  C  CG2 . THR A 1 59  ? -16.379 -13.332 -3.107  1.00 20.52 ? 59  THR A CG2 1 
ATOM   344  N  N   . THR A 1 60  ? -17.550 -13.146 -6.101  1.00 19.56 ? 60  THR A N   1 
ATOM   345  C  CA  . THR A 1 60  ? -17.113 -12.247 -7.144  1.00 16.34 ? 60  THR A CA  1 
ATOM   346  C  C   . THR A 1 60  ? -17.005 -10.819 -6.631  1.00 18.47 ? 60  THR A C   1 
ATOM   347  O  O   . THR A 1 60  ? -17.536 -10.484 -5.584  1.00 19.88 ? 60  THR A O   1 
ATOM   348  C  CB  . THR A 1 60  ? -18.124 -12.223 -8.293  1.00 20.97 ? 60  THR A CB  1 
ATOM   349  O  OG1 . THR A 1 60  ? -19.426 -11.883 -7.794  1.00 22.78 ? 60  THR A OG1 1 
ATOM   350  C  CG2 . THR A 1 60  ? -18.224 -13.616 -8.919  1.00 24.11 ? 60  THR A CG2 1 
ATOM   351  N  N   . GLU A 1 61  ? -16.283 -9.983  -7.361  1.00 18.82 ? 61  GLU A N   1 
ATOM   352  C  CA  . GLU A 1 61  ? -16.132 -8.573  -7.003  1.00 23.51 ? 61  GLU A CA  1 
ATOM   353  C  C   . GLU A 1 61  ? -17.531 -7.934  -6.851  1.00 20.57 ? 61  GLU A C   1 
ATOM   354  O  O   . GLU A 1 61  ? -17.740 -7.141  -5.979  1.00 19.24 ? 61  GLU A O   1 
ATOM   355  C  CB  . GLU A 1 61  ? -15.402 -7.822  -8.136  1.00 25.73 ? 61  GLU A CB  1 
ATOM   356  C  CG  . GLU A 1 61  ? -13.877 -7.938  -8.205  1.00 34.02 ? 61  GLU A CG  1 
ATOM   357  C  CD  . GLU A 1 61  ? -13.291 -6.874  -9.152  1.00 35.60 ? 61  GLU A CD  1 
ATOM   358  N  N   . GLU A 1 62  ? -18.478 -8.289  -7.724  1.00 16.95 ? 62  GLU A N   1 
ATOM   359  C  CA  . GLU A 1 62  ? -19.790 -7.666  -7.670  1.00 21.93 ? 62  GLU A CA  1 
ATOM   360  C  C   . GLU A 1 62  ? -20.598 -8.134  -6.461  1.00 17.61 ? 62  GLU A C   1 
ATOM   361  O  O   . GLU A 1 62  ? -21.418 -7.365  -5.961  1.00 21.70 ? 62  GLU A O   1 
ATOM   362  C  CB  . GLU A 1 62  ? -20.579 -7.887  -8.972  1.00 25.80 ? 62  GLU A CB  1 
ATOM   363  C  CG  . GLU A 1 62  ? -19.909 -7.327  -10.208 1.00 31.18 ? 62  GLU A CG  1 
ATOM   364  C  CD  . GLU A 1 62  ? -18.695 -8.114  -10.702 1.00 31.71 ? 62  GLU A CD  1 
ATOM   365  O  OE1 . GLU A 1 62  ? -18.468 -9.304  -10.310 1.00 29.42 ? 62  GLU A OE1 1 
ATOM   366  O  OE2 . GLU A 1 62  ? -17.918 -7.478  -11.457 1.00 41.43 ? 62  GLU A OE2 1 
ATOM   367  N  N   . GLU A 1 63  ? -20.426 -9.384  -6.015  1.00 14.34 ? 63  GLU A N   1 
ATOM   368  C  CA  . GLU A 1 63  ? -21.196 -9.854  -4.868  1.00 14.74 ? 63  GLU A CA  1 
ATOM   369  C  C   . GLU A 1 63  ? -20.610 -9.453  -3.547  1.00 13.00 ? 63  GLU A C   1 
ATOM   370  O  O   . GLU A 1 63  ? -21.341 -9.403  -2.581  1.00 12.90 ? 63  GLU A O   1 
ATOM   371  C  CB  . GLU A 1 63  ? -21.360 -11.369 -4.865  1.00 15.03 ? 63  GLU A CB  1 
ATOM   372  C  CG  . GLU A 1 63  ? -22.205 -11.901 -6.005  1.00 17.78 ? 63  GLU A CG  1 
ATOM   373  C  CD  . GLU A 1 63  ? -22.180 -13.423 -6.105  1.00 21.40 ? 63  GLU A CD  1 
ATOM   374  O  OE1 . GLU A 1 63  ? -21.273 -13.952 -6.814  1.00 25.69 ? 63  GLU A OE1 1 
ATOM   375  O  OE2 . GLU A 1 63  ? -23.105 -14.099 -5.506  1.00 26.21 ? 63  GLU A OE2 1 
ATOM   376  N  N   . PHE A 1 64  ? -19.282 -9.213  -3.498  1.00 14.65 ? 64  PHE A N   1 
ATOM   377  C  CA  . PHE A 1 64  ? -18.551 -9.007  -2.231  1.00 13.99 ? 64  PHE A CA  1 
ATOM   378  C  C   . PHE A 1 64  ? -18.546 -7.565  -1.808  1.00 14.18 ? 64  PHE A C   1 
ATOM   379  O  O   . PHE A 1 64  ? -17.601 -6.800  -2.016  1.00 19.59 ? 64  PHE A O   1 
ATOM   380  C  CB  . PHE A 1 64  ? -17.144 -9.578  -2.410  1.00 13.39 ? 64  PHE A CB  1 
ATOM   381  C  CG  . PHE A 1 64  ? -16.294 -9.552  -1.184  1.00 13.53 ? 64  PHE A CG  1 
ATOM   382  C  CD1 . PHE A 1 64  ? -16.692 -10.242 -0.050  1.00 9.46  ? 64  PHE A CD1 1 
ATOM   383  C  CD2 . PHE A 1 64  ? -15.000 -9.069  -1.223  1.00 13.95 ? 64  PHE A CD2 1 
ATOM   384  C  CE1 . PHE A 1 64  ? -15.899 -10.310 1.108   1.00 14.40 ? 64  PHE A CE1 1 
ATOM   385  C  CE2 . PHE A 1 64  ? -14.189 -9.203  -0.088  1.00 17.67 ? 64  PHE A CE2 1 
ATOM   386  C  CZ  . PHE A 1 64  ? -14.665 -9.809  1.078   1.00 17.07 ? 64  PHE A CZ  1 
ATOM   387  N  N   . VAL A 1 65  ? -19.567 -7.249  -1.040  1.00 11.83 ? 65  VAL A N   1 
ATOM   388  C  CA  . VAL A 1 65  ? -19.832 -5.912  -0.572  1.00 10.27 ? 65  VAL A CA  1 
ATOM   389  C  C   . VAL A 1 65  ? -19.202 -5.633  0.801   1.00 10.82 ? 65  VAL A C   1 
ATOM   390  O  O   . VAL A 1 65  ? -18.656 -6.540  1.455   1.00 11.55 ? 65  VAL A O   1 
ATOM   391  C  CB  . VAL A 1 65  ? -21.338 -5.696  -0.556  1.00 12.25 ? 65  VAL A CB  1 
ATOM   392  C  CG1 . VAL A 1 65  ? -21.897 -5.738  -1.990  1.00 14.50 ? 65  VAL A CG1 1 
ATOM   393  C  CG2 . VAL A 1 65  ? -22.092 -6.696  0.364   1.00 15.44 ? 65  VAL A CG2 1 
ATOM   394  N  N   . GLU A 1 66  ? -19.289 -4.395  1.238   1.00 10.42 ? 66  GLU A N   1 
ATOM   395  C  CA  . GLU A 1 66  ? -18.874 -4.084  2.614   1.00 10.86 ? 66  GLU A CA  1 
ATOM   396  C  C   . GLU A 1 66  ? -19.735 -4.913  3.566   1.00 12.17 ? 66  GLU A C   1 
ATOM   397  O  O   . GLU A 1 66  ? -20.871 -5.226  3.238   1.00 13.99 ? 66  GLU A O   1 
ATOM   398  C  CB  . GLU A 1 66  ? -19.227 -2.637  2.981   1.00 19.87 ? 66  GLU A CB  1 
ATOM   399  C  CG  . GLU A 1 66  ? -18.572 -1.537  2.204   1.00 20.83 ? 66  GLU A CG  1 
ATOM   400  C  CD  . GLU A 1 66  ? -18.950 -0.256  2.925   1.00 18.28 ? 66  GLU A CD  1 
ATOM   401  O  OE1 . GLU A 1 66  ? -18.255 0.079   3.883   1.00 18.86 ? 66  GLU A OE1 1 
ATOM   402  O  OE2 . GLU A 1 66  ? -19.982 0.350   2.577   1.00 19.87 ? 66  GLU A OE2 1 
ATOM   403  N  N   . GLY A 1 67  ? -19.176 -5.262  4.714   1.00 12.82 ? 67  GLY A N   1 
ATOM   404  C  CA  . GLY A 1 67  ? -19.954 -5.960  5.745   1.00 15.08 ? 67  GLY A CA  1 
ATOM   405  C  C   . GLY A 1 67  ? -19.067 -6.669  6.741   1.00 12.64 ? 67  GLY A C   1 
ATOM   406  O  O   . GLY A 1 67  ? -17.832 -6.627  6.609   1.00 12.72 ? 67  GLY A O   1 
ATOM   407  N  N   . ILE A 1 68  ? -19.698 -7.302  7.712   1.00 11.54 ? 68  ILE A N   1 
ATOM   408  C  CA  . ILE A 1 68  ? -19.006 -8.173  8.640   1.00 12.06 ? 68  ILE A CA  1 
ATOM   409  C  C   . ILE A 1 68  ? -19.227 -9.578  8.109   1.00 11.26 ? 68  ILE A C   1 
ATOM   410  O  O   . ILE A 1 68  ? -20.361 -10.013 7.939   1.00 13.08 ? 68  ILE A O   1 
ATOM   411  C  CB  . ILE A 1 68  ? -19.507 -8.012  10.058  1.00 12.17 ? 68  ILE A CB  1 
ATOM   412  C  CG1 . ILE A 1 68  ? -19.147 -6.622  10.594  1.00 17.88 ? 68  ILE A CG1 1 
ATOM   413  C  CG2 . ILE A 1 68  ? -18.789 -9.033  11.003  1.00 14.80 ? 68  ILE A CG2 1 
ATOM   414  C  CD1 . ILE A 1 68  ? -19.677 -6.316  11.988  1.00 19.49 ? 68  ILE A CD1 1 
ATOM   415  N  N   . TYR A 1 69  ? -18.138 -10.294 7.865   1.00 9.78  ? 69  TYR A N   1 
ATOM   416  C  CA  . TYR A 1 69  ? -18.160 -11.641 7.334   1.00 9.07  ? 69  TYR A CA  1 
ATOM   417  C  C   . TYR A 1 69  ? -17.663 -12.643 8.319   1.00 10.75 ? 69  TYR A C   1 
ATOM   418  O  O   . TYR A 1 69  ? -16.743 -12.344 9.065   1.00 12.15 ? 69  TYR A O   1 
ATOM   419  C  CB  . TYR A 1 69  ? -17.320 -11.718 6.063   1.00 8.84  ? 69  TYR A CB  1 
ATOM   420  C  CG  . TYR A 1 69  ? -17.916 -10.987 4.860   1.00 9.73  ? 69  TYR A CG  1 
ATOM   421  C  CD1 . TYR A 1 69  ? -17.736 -9.624  4.634   1.00 10.29 ? 69  TYR A CD1 1 
ATOM   422  C  CD2 . TYR A 1 69  ? -18.715 -11.666 3.939   1.00 10.44 ? 69  TYR A CD2 1 
ATOM   423  C  CE1 . TYR A 1 69  ? -18.341 -8.983  3.566   1.00 12.79 ? 69  TYR A CE1 1 
ATOM   424  C  CE2 . TYR A 1 69  ? -19.273 -11.034 2.858   1.00 12.72 ? 69  TYR A CE2 1 
ATOM   425  C  CZ  . TYR A 1 69  ? -19.071 -9.685  2.682   1.00 11.84 ? 69  TYR A CZ  1 
ATOM   426  O  OH  . TYR A 1 69  ? -19.595 -9.061  1.599   1.00 14.09 ? 69  TYR A OH  1 
ATOM   427  N  N   . LYS A 1 70  ? -18.252 -13.809 8.298   1.00 11.07 ? 70  LYS A N   1 
ATOM   428  C  CA  . LYS A 1 70  ? -17.845 -14.936 9.105   1.00 11.31 ? 70  LYS A CA  1 
ATOM   429  C  C   . LYS A 1 70  ? -17.499 -16.066 8.158   1.00 12.37 ? 70  LYS A C   1 
ATOM   430  O  O   . LYS A 1 70  ? -18.321 -16.538 7.409   1.00 14.49 ? 70  LYS A O   1 
ATOM   431  C  CB  . LYS A 1 70  ? -18.962 -15.358 10.086  1.00 12.46 ? 70  LYS A CB  1 
ATOM   432  C  CG  . LYS A 1 70  ? -18.615 -16.690 10.768  1.00 14.88 ? 70  LYS A CG  1 
ATOM   433  C  CD  . LYS A 1 70  ? -19.550 -17.013 11.890  1.00 20.30 ? 70  LYS A CD  1 
ATOM   434  C  CE  . LYS A 1 70  ? -21.006 -17.204 11.449  1.00 25.36 ? 70  LYS A CE  1 
ATOM   435  N  NZ  . LYS A 1 70  ? -21.836 -18.073 12.391  1.00 34.98 ? 70  LYS A NZ  1 
ATOM   436  N  N   . VAL A 1 71  ? -16.253 -16.548 8.239   1.00 13.77 ? 71  VAL A N   1 
ATOM   437  C  CA  . VAL A 1 71  ? -15.819 -17.738 7.511   1.00 13.15 ? 71  VAL A CA  1 
ATOM   438  C  C   . VAL A 1 71  ? -15.756 -18.864 8.536   1.00 13.50 ? 71  VAL A C   1 
ATOM   439  O  O   . VAL A 1 71  ? -14.952 -18.757 9.488   1.00 16.67 ? 71  VAL A O   1 
ATOM   440  C  CB  . VAL A 1 71  ? -14.432 -17.466 6.908   1.00 11.80 ? 71  VAL A CB  1 
ATOM   441  C  CG1 . VAL A 1 71  ? -13.878 -18.704 6.192   1.00 16.47 ? 71  VAL A CG1 1 
ATOM   442  C  CG2 . VAL A 1 71  ? -14.502 -16.317 5.927   1.00 13.70 ? 71  VAL A CG2 1 
ATOM   443  N  N   . GLU A 1 72  ? -16.541 -19.921 8.311   1.00 13.18 ? 72  GLU A N   1 
ATOM   444  C  CA  . GLU A 1 72  ? -16.583 -21.088 9.210   1.00 15.42 ? 72  GLU A CA  1 
ATOM   445  C  C   . GLU A 1 72  ? -15.971 -22.263 8.423   1.00 12.70 ? 72  GLU A C   1 
ATOM   446  O  O   . GLU A 1 72  ? -16.461 -22.624 7.365   1.00 15.40 ? 72  GLU A O   1 
ATOM   447  C  CB  . GLU A 1 72  ? -18.010 -21.462 9.621   1.00 20.05 ? 72  GLU A CB  1 
ATOM   448  C  CG  . GLU A 1 72  ? -18.638 -20.565 10.646  1.00 28.92 ? 72  GLU A CG  1 
ATOM   449  C  CD  . GLU A 1 72  ? -19.941 -21.159 11.195  1.00 24.57 ? 72  GLU A CD  1 
ATOM   450  O  OE1 . GLU A 1 72  ? -20.368 -22.179 10.661  1.00 30.51 ? 72  GLU A OE1 1 
ATOM   451  O  OE2 . GLU A 1 72  ? -20.543 -20.593 12.108  1.00 34.98 ? 72  GLU A OE2 1 
ATOM   452  N  N   . ILE A 1 73  ? -14.944 -22.858 8.961   1.00 16.34 ? 73  ILE A N   1 
ATOM   453  C  CA  . ILE A 1 73  ? -14.259 -23.998 8.362   1.00 15.12 ? 73  ILE A CA  1 
ATOM   454  C  C   . ILE A 1 73  ? -14.707 -25.206 9.143   1.00 13.35 ? 73  ILE A C   1 
ATOM   455  O  O   . ILE A 1 73  ? -14.548 -25.225 10.382  1.00 15.55 ? 73  ILE A O   1 
ATOM   456  C  CB  . ILE A 1 73  ? -12.759 -23.819 8.449   1.00 14.40 ? 73  ILE A CB  1 
ATOM   457  C  CG1 . ILE A 1 73  ? -12.303 -22.575 7.687   1.00 15.47 ? 73  ILE A CG1 1 
ATOM   458  C  CG2 . ILE A 1 73  ? -11.995 -25.005 7.874   1.00 14.92 ? 73  ILE A CG2 1 
ATOM   459  C  CD1 . ILE A 1 73  ? -10.878 -22.146 7.917   1.00 18.46 ? 73  ILE A CD1 1 
ATOM   460  N  N   . ASP A 1 74  ? -15.317 -26.193 8.488   1.00 14.85 ? 74  ASP A N   1 
ATOM   461  C  CA  . ASP A 1 74  ? -15.870 -27.376 9.185   1.00 16.72 ? 74  ASP A CA  1 
ATOM   462  C  C   . ASP A 1 74  ? -14.794 -28.404 9.596   1.00 13.17 ? 74  ASP A C   1 
ATOM   463  O  O   . ASP A 1 74  ? -14.624 -29.474 8.944   1.00 15.23 ? 74  ASP A O   1 
ATOM   464  C  CB  . ASP A 1 74  ? -16.893 -28.046 8.254   1.00 16.53 ? 74  ASP A CB  1 
ATOM   465  C  CG  . ASP A 1 74  ? -17.502 -29.328 8.834   1.00 20.33 ? 74  ASP A CG  1 
ATOM   466  O  OD1 . ASP A 1 74  ? -17.540 -29.519 10.049  1.00 22.72 ? 74  ASP A OD1 1 
ATOM   467  O  OD2 . ASP A 1 74  ? -17.966 -30.154 8.011   1.00 29.70 ? 74  ASP A OD2 1 
ATOM   468  N  N   . THR A 1 75  ? -14.070 -28.044 10.619  1.00 13.83 ? 75  THR A N   1 
ATOM   469  C  CA  . THR A 1 75  ? -13.012 -28.867 11.156  1.00 14.14 ? 75  THR A CA  1 
ATOM   470  C  C   . THR A 1 75  ? -13.550 -30.175 11.738  1.00 12.78 ? 75  THR A C   1 
ATOM   471  O  O   . THR A 1 75  ? -12.914 -31.207 11.651  1.00 12.84 ? 75  THR A O   1 
ATOM   472  C  CB  . THR A 1 75  ? -12.227 -28.090 12.211  1.00 13.86 ? 75  THR A CB  1 
ATOM   473  O  OG1 . THR A 1 75  ? -13.088 -27.661 13.250  1.00 15.97 ? 75  THR A OG1 1 
ATOM   474  C  CG2 . THR A 1 75  ? -11.567 -26.906 11.573  1.00 15.35 ? 75  THR A CG2 1 
ATOM   475  N  N   . LYS A 1 76  ? -14.733 -30.143 12.308  1.00 13.32 ? 76  LYS A N   1 
ATOM   476  C  CA  . LYS A 1 76  ? -15.247 -31.350 12.896  1.00 13.97 ? 76  LYS A CA  1 
ATOM   477  C  C   . LYS A 1 76  ? -15.399 -32.480 11.890  1.00 13.48 ? 76  LYS A C   1 
ATOM   478  O  O   . LYS A 1 76  ? -14.971 -33.600 12.166  1.00 14.30 ? 76  LYS A O   1 
ATOM   479  C  CB  . LYS A 1 76  ? -16.583 -31.105 13.625  1.00 20.05 ? 76  LYS A CB  1 
ATOM   480  C  CG  . LYS A 1 76  ? -17.400 -32.321 14.031  1.00 24.20 ? 76  LYS A CG  1 
ATOM   481  C  CD  . LYS A 1 76  ? -18.735 -31.885 14.703  1.00 31.36 ? 76  LYS A CD  1 
ATOM   482  C  CE  . LYS A 1 76  ? -19.663 -33.082 14.999  1.00 39.45 ? 76  LYS A CE  1 
ATOM   483  N  N   . SER A 1 77  ? -16.021 -32.228 10.743  1.00 12.06 ? 77  SER A N   1 
ATOM   484  C  CA  . SER A 1 77  ? -16.262 -33.275 9.763   1.00 11.60 ? 77  SER A CA  1 
ATOM   485  C  C   . SER A 1 77  ? -14.918 -33.784 9.215   1.00 11.93 ? 77  SER A C   1 
ATOM   486  O  O   . SER A 1 77  ? -14.756 -34.956 8.890   1.00 14.66 ? 77  SER A O   1 
ATOM   487  C  CB  . SER A 1 77  ? -17.099 -32.782 8.603   1.00 16.39 ? 77  SER A CB  1 
ATOM   488  O  OG  . SER A 1 77  ? -18.291 -32.342 9.073   1.00 24.41 ? 77  SER A OG  1 
ATOM   489  N  N   . TYR A 1 78  ? -13.990 -32.853 9.053   1.00 12.14 ? 78  TYR A N   1 
ATOM   490  C  CA  . TYR A 1 78  ? -12.707 -33.132 8.461   1.00 12.58 ? 78  TYR A CA  1 
ATOM   491  C  C   . TYR A 1 78  ? -11.973 -34.085 9.348   1.00 13.04 ? 78  TYR A C   1 
ATOM   492  O  O   . TYR A 1 78  ? -11.495 -35.133 8.887   1.00 13.64 ? 78  TYR A O   1 
ATOM   493  C  CB  . TYR A 1 78  ? -11.914 -31.860 8.378   1.00 13.36 ? 78  TYR A CB  1 
ATOM   494  C  CG  . TYR A 1 78  ? -10.521 -32.074 7.799   1.00 11.54 ? 78  TYR A CG  1 
ATOM   495  C  CD1 . TYR A 1 78  ? -10.309 -32.322 6.430   1.00 10.83 ? 78  TYR A CD1 1 
ATOM   496  C  CD2 . TYR A 1 78  ? -9.410  -32.085 8.659   1.00 13.45 ? 78  TYR A CD2 1 
ATOM   497  C  CE1 . TYR A 1 78  ? -9.029  -32.492 5.982   1.00 10.47 ? 78  TYR A CE1 1 
ATOM   498  C  CE2 . TYR A 1 78  ? -8.148  -32.240 8.206   1.00 15.28 ? 78  TYR A CE2 1 
ATOM   499  C  CZ  . TYR A 1 78  ? -7.957  -32.485 6.825   1.00 12.44 ? 78  TYR A CZ  1 
ATOM   500  O  OH  . TYR A 1 78  ? -6.690  -32.720 6.315   1.00 14.42 ? 78  TYR A OH  1 
ATOM   501  N  N   . TRP A 1 79  ? -11.839 -33.767 10.638  1.00 11.07 ? 79  TRP A N   1 
ATOM   502  C  CA  . TRP A 1 79  ? -11.149 -34.716 11.560  1.00 14.47 ? 79  TRP A CA  1 
ATOM   503  C  C   . TRP A 1 79  ? -11.873 -35.999 11.703  1.00 12.39 ? 79  TRP A C   1 
ATOM   504  O  O   . TRP A 1 79  ? -11.246 -37.038 11.710  1.00 14.22 ? 79  TRP A O   1 
ATOM   505  C  CB  . TRP A 1 79  ? -10.916 -34.101 12.924  1.00 12.49 ? 79  TRP A CB  1 
ATOM   506  C  CG  . TRP A 1 79  ? -9.966  -32.896 12.923  1.00 12.25 ? 79  TRP A CG  1 
ATOM   507  C  CD1 . TRP A 1 79  ? -10.208 -31.630 13.411  1.00 13.36 ? 79  TRP A CD1 1 
ATOM   508  C  CD2 . TRP A 1 79  ? -8.606  -32.856 12.427  1.00 11.97 ? 79  TRP A CD2 1 
ATOM   509  N  NE1 . TRP A 1 79  ? -9.127  -30.839 13.247  1.00 12.50 ? 79  TRP A NE1 1 
ATOM   510  C  CE2 . TRP A 1 79  ? -8.126  -31.522 12.651  1.00 13.60 ? 79  TRP A CE2 1 
ATOM   511  C  CE3 . TRP A 1 79  ? -7.752  -33.782 11.829  1.00 11.10 ? 79  TRP A CE3 1 
ATOM   512  C  CZ2 . TRP A 1 79  ? -6.850  -31.137 12.279  1.00 12.97 ? 79  TRP A CZ2 1 
ATOM   513  C  CZ3 . TRP A 1 79  ? -6.469  -33.360 11.421  1.00 13.54 ? 79  TRP A CZ3 1 
ATOM   514  C  CH2 . TRP A 1 79  ? -6.034  -32.070 11.685  1.00 14.96 ? 79  TRP A CH2 1 
ATOM   515  N  N   . LYS A 1 80  ? -13.213 -35.983 11.845  1.00 11.83 ? 80  LYS A N   1 
ATOM   516  C  CA  . LYS A 1 80  ? -13.952 -37.237 12.050  1.00 11.19 ? 80  LYS A CA  1 
ATOM   517  C  C   . LYS A 1 80  ? -13.706 -38.160 10.852  1.00 17.01 ? 80  LYS A C   1 
ATOM   518  O  O   . LYS A 1 80  ? -13.554 -39.372 11.059  1.00 14.77 ? 80  LYS A O   1 
ATOM   519  C  CB  . LYS A 1 80  ? -15.463 -36.962 12.174  1.00 17.16 ? 80  LYS A CB  1 
ATOM   520  C  CG  . LYS A 1 80  ? -15.901 -36.472 13.505  1.00 27.32 ? 80  LYS A CG  1 
ATOM   521  C  CD  . LYS A 1 80  ? -17.417 -36.222 13.590  1.00 28.18 ? 80  LYS A CD  1 
ATOM   522  N  N   . ALA A 1 81  ? -13.653 -37.602 9.631   1.00 14.20 ? 81  ALA A N   1 
ATOM   523  C  CA  . ALA A 1 81  ? -13.476 -38.425 8.432   1.00 12.64 ? 81  ALA A CA  1 
ATOM   524  C  C   . ALA A 1 81  ? -12.071 -39.089 8.340   1.00 15.11 ? 81  ALA A C   1 
ATOM   525  O  O   . ALA A 1 81  ? -11.873 -40.005 7.596   1.00 20.78 ? 81  ALA A O   1 
ATOM   526  C  CB  . ALA A 1 81  ? -13.831 -37.702 7.118   1.00 16.90 ? 81  ALA A CB  1 
ATOM   527  N  N   . LEU A 1 82  ? -11.111 -38.582 9.101   1.00 16.74 ? 82  LEU A N   1 
ATOM   528  C  CA  . LEU A 1 82  ? -9.754  -39.048 9.102   1.00 16.35 ? 82  LEU A CA  1 
ATOM   529  C  C   . LEU A 1 82  ? -9.524  -39.916 10.324  1.00 15.53 ? 82  LEU A C   1 
ATOM   530  O  O   . LEU A 1 82  ? -8.436  -40.376 10.565  1.00 22.65 ? 82  LEU A O   1 
ATOM   531  C  CB  . LEU A 1 82  ? -8.801  -37.856 9.147   1.00 17.28 ? 82  LEU A CB  1 
ATOM   532  C  CG  . LEU A 1 82  ? -8.749  -36.986 7.863   1.00 17.90 ? 82  LEU A CG  1 
ATOM   533  C  CD1 . LEU A 1 82  ? -7.871  -35.816 8.184   1.00 24.94 ? 82  LEU A CD1 1 
ATOM   534  C  CD2 . LEU A 1 82  ? -8.272  -37.783 6.630   1.00 19.42 ? 82  LEU A CD2 1 
ATOM   535  N  N   . GLY A 1 83  ? -10.567 -40.092 11.127  1.00 17.98 ? 83  GLY A N   1 
ATOM   536  C  CA  . GLY A 1 83  ? -10.482 -40.910 12.320  1.00 21.44 ? 83  GLY A CA  1 
ATOM   537  C  C   . GLY A 1 83  ? -9.749  -40.266 13.484  1.00 18.87 ? 83  GLY A C   1 
ATOM   538  O  O   . GLY A 1 83  ? -9.170  -40.959 14.328  1.00 21.22 ? 83  GLY A O   1 
ATOM   539  N  N   . ILE A 1 84  ? -9.845  -38.925 13.542  1.00 18.69 ? 84  ILE A N   1 
ATOM   540  C  CA  . ILE A 1 84  ? -9.201  -38.122 14.570  1.00 17.02 ? 84  ILE A CA  1 
ATOM   541  C  C   . ILE A 1 84  ? -10.304 -37.432 15.391  1.00 14.91 ? 84  ILE A C   1 
ATOM   542  O  O   . ILE A 1 84  ? -11.366 -37.084 14.882  1.00 18.66 ? 84  ILE A O   1 
ATOM   543  C  CB  . ILE A 1 84  ? -8.268  -37.055 13.894  1.00 21.23 ? 84  ILE A CB  1 
ATOM   544  C  CG1 . ILE A 1 84  ? -7.087  -37.743 13.137  1.00 21.48 ? 84  ILE A CG1 1 
ATOM   545  C  CG2 . ILE A 1 84  ? -7.872  -36.027 14.934  1.00 18.25 ? 84  ILE A CG2 1 
ATOM   546  C  CD1 . ILE A 1 84  ? -5.927  -38.220 13.985  1.00 26.86 ? 84  ILE A CD1 1 
ATOM   547  N  N   . SER A 1 85  ? -10.050 -37.235 16.662  1.00 15.56 ? 85  SER A N   1 
ATOM   548  C  CA  . SER A 1 85  ? -11.005 -36.598 17.522  1.00 19.59 ? 85  SER A CA  1 
ATOM   549  C  C   . SER A 1 85  ? -10.841 -35.090 17.460  1.00 21.61 ? 85  SER A C   1 
ATOM   550  O  O   . SER A 1 85  ? -9.800  -34.560 17.794  1.00 31.92 ? 85  SER A O   1 
ATOM   551  C  CB  . SER A 1 85  ? -10.848 -37.047 18.976  1.00 28.93 ? 85  SER A CB  1 
ATOM   552  O  OG  . SER A 1 85  ? -11.482 -36.108 19.799  1.00 43.61 ? 85  SER A OG  1 
ATOM   553  N  N   . PRO A 1 86  ? -11.878 -34.404 17.074  1.00 22.55 ? 86  PRO A N   1 
ATOM   554  C  CA  . PRO A 1 86  ? -11.821 -32.951 16.927  1.00 25.96 ? 86  PRO A CA  1 
ATOM   555  C  C   . PRO A 1 86  ? -12.268 -32.374 18.218  1.00 18.46 ? 86  PRO A C   1 
ATOM   556  O  O   . PRO A 1 86  ? -13.134 -32.880 18.798  1.00 24.76 ? 86  PRO A O   1 
ATOM   557  C  CB  . PRO A 1 86  ? -12.907 -32.664 15.879  1.00 27.30 ? 86  PRO A CB  1 
ATOM   558  C  CG  . PRO A 1 86  ? -13.903 -33.788 16.046  1.00 26.87 ? 86  PRO A CG  1 
ATOM   559  C  CD  . PRO A 1 86  ? -13.131 -34.971 16.587  1.00 23.39 ? 86  PRO A CD  1 
ATOM   560  N  N   . PHE A 1 87  ? -11.655 -31.270 18.634  1.00 24.87 ? 87  PHE A N   1 
ATOM   561  C  CA  . PHE A 1 87  ? -12.170 -30.544 19.813  1.00 20.57 ? 87  PHE A CA  1 
ATOM   562  C  C   . PHE A 1 87  ? -13.072 -29.435 19.284  1.00 20.20 ? 87  PHE A C   1 
ATOM   563  O  O   . PHE A 1 87  ? -14.193 -29.303 19.753  1.00 16.39 ? 87  PHE A O   1 
ATOM   564  C  CB  . PHE A 1 87  ? -11.002 -29.973 20.604  1.00 24.77 ? 87  PHE A CB  1 
ATOM   565  C  CG  . PHE A 1 87  ? -11.362 -29.122 21.785  1.00 24.72 ? 87  PHE A CG  1 
ATOM   566  C  CD1 . PHE A 1 87  ? -11.839 -29.699 22.947  1.00 25.79 ? 87  PHE A CD1 1 
ATOM   567  C  CD2 . PHE A 1 87  ? -11.212 -27.748 21.733  1.00 23.73 ? 87  PHE A CD2 1 
ATOM   568  C  CE1 . PHE A 1 87  ? -12.166 -28.912 24.036  1.00 28.26 ? 87  PHE A CE1 1 
ATOM   569  C  CE2 . PHE A 1 87  ? -11.548 -26.964 22.822  1.00 26.70 ? 87  PHE A CE2 1 
ATOM   570  C  CZ  . PHE A 1 87  ? -12.014 -27.550 23.972  1.00 27.01 ? 87  PHE A CZ  1 
ATOM   571  N  N   . HIS A 1 88  ? -12.543 -28.649 18.330  1.00 19.89 ? 88  HIS A N   1 
ATOM   572  C  CA  . HIS A 1 88  ? -13.329 -27.531 17.813  1.00 25.18 ? 88  HIS A CA  1 
ATOM   573  C  C   . HIS A 1 88  ? -14.379 -28.061 16.893  1.00 19.55 ? 88  HIS A C   1 
ATOM   574  O  O   . HIS A 1 88  ? -14.137 -28.983 16.047  1.00 24.08 ? 88  HIS A O   1 
ATOM   575  C  CB  . HIS A 1 88  ? -12.474 -26.411 17.132  1.00 23.61 ? 88  HIS A CB  1 
ATOM   576  C  CG  . HIS A 1 88  ? -11.449 -25.817 18.047  1.00 20.96 ? 88  HIS A CG  1 
ATOM   577  N  ND1 . HIS A 1 88  ? -10.164 -26.274 18.108  1.00 27.08 ? 88  HIS A ND1 1 
ATOM   578  C  CD2 . HIS A 1 88  ? -11.549 -24.772 18.982  1.00 27.22 ? 88  HIS A CD2 1 
ATOM   579  C  CE1 . HIS A 1 88  ? -9.498  -25.567 19.036  1.00 25.34 ? 88  HIS A CE1 1 
ATOM   580  N  NE2 . HIS A 1 88  ? -10.351 -24.655 19.581  1.00 25.73 ? 88  HIS A NE2 1 
ATOM   581  N  N   . GLU A 1 89  ? -15.515 -27.427 16.964  1.00 23.77 ? 89  GLU A N   1 
ATOM   582  C  CA  . GLU A 1 89  ? -16.632 -27.793 16.177  1.00 24.99 ? 89  GLU A CA  1 
ATOM   583  C  C   . GLU A 1 89  ? -16.351 -27.225 14.748  1.00 22.79 ? 89  GLU A C   1 
ATOM   584  O  O   . GLU A 1 89  ? -16.652 -27.847 13.711  1.00 21.46 ? 89  GLU A O   1 
ATOM   585  C  CB  . GLU A 1 89  ? -17.992 -27.369 16.872  1.00 34.12 ? 89  GLU A CB  1 
ATOM   586  C  CG  . GLU A 1 89  ? -18.971 -28.607 17.092  1.00 34.06 ? 89  GLU A CG  1 
ATOM   587  C  CD  . GLU A 1 89  ? -20.218 -28.617 16.221  1.00 28.54 ? 89  GLU A CD  1 
ATOM   588  N  N   . HIS A 1 90  ? -15.710 -26.065 14.702  1.00 16.15 ? 90  HIS A N   1 
ATOM   589  C  CA  . HIS A 1 90  ? -15.431 -25.391 13.458  1.00 18.59 ? 90  HIS A CA  1 
ATOM   590  C  C   . HIS A 1 90  ? -14.493 -24.268 13.794  1.00 21.83 ? 90  HIS A C   1 
ATOM   591  O  O   . HIS A 1 90  ? -14.378 -23.905 14.990  1.00 35.55 ? 90  HIS A O   1 
ATOM   592  C  CB  . HIS A 1 90  ? -16.751 -24.916 12.724  1.00 24.32 ? 90  HIS A CB  1 
ATOM   593  C  CG  . HIS A 1 90  ? -17.741 -24.108 13.594  1.00 24.05 ? 90  HIS A CG  1 
ATOM   594  N  ND1 . HIS A 1 90  ? -18.683 -24.681 14.368  1.00 33.27 ? 90  HIS A ND1 1 
ATOM   595  C  CD2 . HIS A 1 90  ? -17.868 -22.742 13.781  1.00 31.26 ? 90  HIS A CD2 1 
ATOM   596  C  CE1 . HIS A 1 90  ? -19.391 -23.722 15.025  1.00 34.65 ? 90  HIS A CE1 1 
ATOM   597  N  NE2 . HIS A 1 90  ? -18.881 -22.528 14.654  1.00 33.12 ? 90  HIS A NE2 1 
ATOM   598  N  N   . ALA A 1 91  ? -13.739 -23.774 12.812  1.00 25.80 ? 91  ALA A N   1 
ATOM   599  C  CA  . ALA A 1 91  ? -12.821 -22.605 12.963  1.00 26.93 ? 91  ALA A CA  1 
ATOM   600  C  C   . ALA A 1 91  ? -13.425 -21.455 12.279  1.00 29.45 ? 91  ALA A C   1 
ATOM   601  O  O   . ALA A 1 91  ? -13.540 -21.562 11.040  1.00 26.24 ? 91  ALA A O   1 
ATOM   602  C  CB  . ALA A 1 91  ? -11.430 -22.901 12.353  1.00 32.29 ? 91  ALA A CB  1 
ATOM   603  N  N   . GLU A 1 92  ? -13.771 -20.384 13.067  1.00 38.43 ? 92  GLU A N   1 
ATOM   604  C  CA  . GLU A 1 92  ? -14.673 -19.224 12.688  1.00 30.59 ? 92  GLU A CA  1 
ATOM   605  C  C   . GLU A 1 92  ? -14.106 -17.831 12.797  1.00 40.60 ? 92  GLU A C   1 
ATOM   606  O  O   . GLU A 1 92  ? -14.234 -17.152 13.889  1.00 32.75 ? 92  GLU A O   1 
ATOM   607  C  CB  . GLU A 1 92  ? -15.937 -19.168 13.563  1.00 37.69 ? 92  GLU A CB  1 
ATOM   608  N  N   . VAL A 1 93  ? -13.710 -17.344 11.619  1.00 23.55 ? 93  VAL A N   1 
ATOM   609  C  CA  . VAL A 1 93  ? -12.922 -16.142 11.456  1.00 19.44 ? 93  VAL A CA  1 
ATOM   610  C  C   . VAL A 1 93  ? -13.954 -15.037 11.086  1.00 12.55 ? 93  VAL A C   1 
ATOM   611  O  O   . VAL A 1 93  ? -14.632 -15.167 10.135  1.00 14.04 ? 93  VAL A O   1 
ATOM   612  C  CB  . VAL A 1 93  ? -11.946 -16.382 10.309  1.00 20.44 ? 93  VAL A CB  1 
ATOM   613  C  CG1 . VAL A 1 93  ? -10.994 -15.257 10.216  1.00 22.92 ? 93  VAL A CG1 1 
ATOM   614  C  CG2 . VAL A 1 93  ? -11.208 -17.707 10.589  1.00 29.44 ? 93  VAL A CG2 1 
ATOM   615  N  N   . VAL A 1 94  ? -14.008 -13.941 11.827  1.00 11.14 ? 94  VAL A N   1 
ATOM   616  C  CA  . VAL A 1 94  ? -15.009 -12.904 11.671  1.00 11.21 ? 94  VAL A CA  1 
ATOM   617  C  C   . VAL A 1 94  ? -14.267 -11.572 11.506  1.00 10.93 ? 94  VAL A C   1 
ATOM   618  O  O   . VAL A 1 94  ? -13.455 -11.222 12.357  1.00 10.79 ? 94  VAL A O   1 
ATOM   619  C  CB  . VAL A 1 94  ? -16.023 -12.851 12.812  1.00 10.94 ? 94  VAL A CB  1 
ATOM   620  C  CG1 . VAL A 1 94  ? -17.010 -11.726 12.588  1.00 13.06 ? 94  VAL A CG1 1 
ATOM   621  C  CG2 . VAL A 1 94  ? -16.759 -14.168 13.015  1.00 15.18 ? 94  VAL A CG2 1 
ATOM   622  N  N   . PHE A 1 95  ? -14.620 -10.838 10.466  1.00 10.87 ? 95  PHE A N   1 
ATOM   623  C  CA  . PHE A 1 95  ? -13.919 -9.629  10.082  1.00 11.28 ? 95  PHE A CA  1 
ATOM   624  C  C   . PHE A 1 95  ? -14.797 -8.659  9.320   1.00 11.80 ? 95  PHE A C   1 
ATOM   625  O  O   . PHE A 1 95  ? -15.672 -9.074  8.582   1.00 12.33 ? 95  PHE A O   1 
ATOM   626  C  CB  . PHE A 1 95  ? -12.644 -9.972  9.309   1.00 13.31 ? 95  PHE A CB  1 
ATOM   627  C  CG  . PHE A 1 95  ? -12.846 -10.594 7.943   1.00 14.95 ? 95  PHE A CG  1 
ATOM   628  C  CD1 . PHE A 1 95  ? -13.109 -11.970 7.817   1.00 14.43 ? 95  PHE A CD1 1 
ATOM   629  C  CD2 . PHE A 1 95  ? -12.774 -9.818  6.805   1.00 13.57 ? 95  PHE A CD2 1 
ATOM   630  C  CE1 . PHE A 1 95  ? -13.304 -12.520 6.550   1.00 15.93 ? 95  PHE A CE1 1 
ATOM   631  C  CE2 . PHE A 1 95  ? -12.978 -10.368 5.551   1.00 15.67 ? 95  PHE A CE2 1 
ATOM   632  C  CZ  . PHE A 1 95  ? -13.204 -11.707 5.441   1.00 17.72 ? 95  PHE A CZ  1 
ATOM   633  N  N   . THR A 1 96  ? -14.514 -7.376  9.434   1.00 12.49 ? 96  THR A N   1 
ATOM   634  C  CA  . THR A 1 96  ? -15.097 -6.378  8.560   1.00 12.48 ? 96  THR A CA  1 
ATOM   635  C  C   . THR A 1 96  ? -14.315 -6.259  7.277   1.00 11.77 ? 96  THR A C   1 
ATOM   636  O  O   . THR A 1 96  ? -13.132 -6.150  7.288   1.00 15.59 ? 96  THR A O   1 
ATOM   637  C  CB  . THR A 1 96  ? -15.106 -5.005  9.250   1.00 14.13 ? 96  THR A CB  1 
ATOM   638  O  OG1 . THR A 1 96  ? -15.849 -5.026  10.476  1.00 16.21 ? 96  THR A OG1 1 
ATOM   639  C  CG2 . THR A 1 96  ? -15.637 -3.916  8.291   1.00 17.58 ? 96  THR A CG2 1 
ATOM   640  N  N   . ALA A 1 97  ? -15.010 -6.317  6.167   1.00 11.16 ? 97  ALA A N   1 
ATOM   641  C  CA  . ALA A 1 97  ? -14.443 -6.296  4.818   1.00 11.67 ? 97  ALA A CA  1 
ATOM   642  C  C   . ALA A 1 97  ? -14.832 -5.014  4.070   1.00 10.59 ? 97  ALA A C   1 
ATOM   643  O  O   . ALA A 1 97  ? -15.953 -4.556  4.145   1.00 12.45 ? 97  ALA A O   1 
ATOM   644  C  CB  . ALA A 1 97  ? -14.859 -7.498  4.008   1.00 13.85 ? 97  ALA A CB  1 
ATOM   645  N  N   . ASN A 1 98  ? -13.895 -4.515  3.255   1.00 11.70 ? 98  ASN A N   1 
ATOM   646  C  CA  . ASN A 1 98  ? -14.135 -3.471  2.266   1.00 12.66 ? 98  ASN A CA  1 
ATOM   647  C  C   . ASN A 1 98  ? -14.612 -2.132  2.818   1.00 9.94  ? 98  ASN A C   1 
ATOM   648  O  O   . ASN A 1 98  ? -15.148 -1.318  2.066   1.00 12.96 ? 98  ASN A O   1 
ATOM   649  C  CB  . ASN A 1 98  ? -15.154 -3.974  1.225   1.00 13.19 ? 98  ASN A CB  1 
ATOM   650  C  CG  . ASN A 1 98  ? -14.727 -5.326  0.599   1.00 14.09 ? 98  ASN A CG  1 
ATOM   651  O  OD1 . ASN A 1 98  ? -13.579 -5.482  0.088   1.00 14.86 ? 98  ASN A OD1 1 
ATOM   652  N  ND2 . ASN A 1 98  ? -15.621 -6.322  0.652   1.00 13.24 ? 98  ASN A ND2 1 
ATOM   653  N  N   . ASP A 1 99  ? -14.418 -1.858  4.097   1.00 12.07 ? 99  ASP A N   1 
ATOM   654  C  CA  . ASP A 1 99  ? -15.036 -0.670  4.697   1.00 14.00 ? 99  ASP A CA  1 
ATOM   655  C  C   . ASP A 1 99  ? -14.439 0.626   4.145   1.00 15.42 ? 99  ASP A C   1 
ATOM   656  O  O   . ASP A 1 99  ? -15.189 1.651   4.052   1.00 15.89 ? 99  ASP A O   1 
ATOM   657  C  CB  . ASP A 1 99  ? -14.917 -0.753  6.211   1.00 14.87 ? 99  ASP A CB  1 
ATOM   658  C  CG  . ASP A 1 99  ? -15.888 0.126   6.970   1.00 15.32 ? 99  ASP A CG  1 
ATOM   659  O  OD1 . ASP A 1 99  ? -16.681 0.909   6.364   1.00 16.36 ? 99  ASP A OD1 1 
ATOM   660  O  OD2 . ASP A 1 99  ? -15.862 -0.026  8.249   1.00 18.21 ? 99  ASP A OD2 1 
ATOM   661  N  N   . SER A 1 100 ? -13.172 0.596   3.729   1.00 15.38 ? 100 SER A N   1 
ATOM   662  C  CA  . SER A 1 100 ? -12.551 1.820   3.188   1.00 18.39 ? 100 SER A CA  1 
ATOM   663  C  C   . SER A 1 100 ? -12.291 1.625   1.674   1.00 18.59 ? 100 SER A C   1 
ATOM   664  O  O   . SER A 1 100 ? -11.522 2.337   1.041   1.00 22.68 ? 100 SER A O   1 
ATOM   665  C  CB  . SER A 1 100 ? -11.296 2.259   4.001   1.00 24.26 ? 100 SER A CB  1 
ATOM   666  O  OG  . SER A 1 100 ? -10.297 1.267   3.975   1.00 33.17 ? 100 SER A OG  1 
ATOM   667  N  N   . GLY A 1 101 ? -13.027 0.692   1.087   1.00 16.40 ? 101 GLY A N   1 
ATOM   668  C  CA  . GLY A 1 101 ? -12.873 0.356   -0.325  1.00 16.37 ? 101 GLY A CA  1 
ATOM   669  C  C   . GLY A 1 101 ? -12.609 -1.113  -0.558  1.00 16.23 ? 101 GLY A C   1 
ATOM   670  O  O   . GLY A 1 101 ? -12.227 -1.833  0.323   1.00 15.47 ? 101 GLY A O   1 
ATOM   671  N  N   . PRO A 1 102 ? -12.818 -1.563  -1.814  1.00 13.00 ? 102 PRO A N   1 
ATOM   672  C  CA  . PRO A 1 102 ? -12.642 -2.983  -2.089  1.00 15.44 ? 102 PRO A CA  1 
ATOM   673  C  C   . PRO A 1 102 ? -11.194 -3.464  -1.835  1.00 15.38 ? 102 PRO A C   1 
ATOM   674  O  O   . PRO A 1 102 ? -10.232 -2.846  -2.280  1.00 16.75 ? 102 PRO A O   1 
ATOM   675  C  CB  . PRO A 1 102 ? -13.103 -3.157  -3.536  1.00 19.28 ? 102 PRO A CB  1 
ATOM   676  C  CG  . PRO A 1 102 ? -13.838 -1.892  -3.897  1.00 24.87 ? 102 PRO A CG  1 
ATOM   677  C  CD  . PRO A 1 102 ? -13.431 -0.831  -2.923  1.00 17.37 ? 102 PRO A CD  1 
ATOM   678  N  N   . ARG A 1 103 ? -11.090 -4.626  -1.208  1.00 14.41 ? 103 ARG A N   1 
ATOM   679  C  CA  . ARG A 1 103 ? -9.801  -5.263  -1.068  1.00 12.92 ? 103 ARG A CA  1 
ATOM   680  C  C   . ARG A 1 103 ? -9.958  -6.746  -1.446  1.00 12.53 ? 103 ARG A C   1 
ATOM   681  O  O   . ARG A 1 103 ? -11.075 -7.298  -1.504  1.00 15.70 ? 103 ARG A O   1 
ATOM   682  C  CB  . ARG A 1 103 ? -9.301  -5.161  0.400   1.00 14.09 ? 103 ARG A CB  1 
ATOM   683  C  CG  . ARG A 1 103 ? -9.227  -3.756  0.942   1.00 15.45 ? 103 ARG A CG  1 
ATOM   684  C  CD  . ARG A 1 103 ? -8.063  -2.999  0.309   1.00 15.07 ? 103 ARG A CD  1 
ATOM   685  N  NE  . ARG A 1 103 ? -7.962  -1.657  0.865   1.00 24.39 ? 103 ARG A NE  1 
ATOM   686  C  CZ  . ARG A 1 103 ? -8.515  -0.549  0.371   1.00 25.46 ? 103 ARG A CZ  1 
ATOM   687  N  NH1 . ARG A 1 103 ? -9.263  -0.572  -0.713  1.00 23.96 ? 103 ARG A NH1 1 
ATOM   688  N  NH2 . ARG A 1 103 ? -8.342  0.604   1.018   1.00 32.07 ? 103 ARG A NH2 1 
ATOM   689  N  N   . ARG A 1 104 ? -8.833  -7.407  -1.579  1.00 15.58 ? 104 ARG A N   1 
ATOM   690  C  CA  . ARG A 1 104 ? -8.807  -8.858  -1.727  1.00 14.49 ? 104 ARG A CA  1 
ATOM   691  C  C   . ARG A 1 104 ? -8.218  -9.442  -0.466  1.00 14.08 ? 104 ARG A C   1 
ATOM   692  O  O   . ARG A 1 104 ? -7.250  -8.932  0.071   1.00 15.00 ? 104 ARG A O   1 
ATOM   693  C  CB  . ARG A 1 104 ? -7.940  -9.219  -2.902  1.00 18.38 ? 104 ARG A CB  1 
ATOM   694  C  CG  . ARG A 1 104 ? -8.445  -8.584  -4.216  1.00 24.26 ? 104 ARG A CG  1 
ATOM   695  C  CD  . ARG A 1 104 ? -7.508  -8.901  -5.351  1.00 28.10 ? 104 ARG A CD  1 
ATOM   696  N  NE  . ARG A 1 104 ? -7.357  -10.312 -5.589  1.00 30.72 ? 104 ARG A NE  1 
ATOM   697  C  CZ  . ARG A 1 104 ? -7.616  -10.941 -6.763  1.00 41.01 ? 104 ARG A CZ  1 
ATOM   698  N  N   . TYR A 1 105 ? -8.887  -10.449 0.026   1.00 6.92  ? 105 TYR A N   1 
ATOM   699  C  CA  . TYR A 1 105 ? -8.565  -11.193 1.292   1.00 11.24 ? 105 TYR A CA  1 
ATOM   700  C  C   . TYR A 1 105 ? -8.232  -12.645 1.064   1.00 12.52 ? 105 TYR A C   1 
ATOM   701  O  O   . TYR A 1 105 ? -9.017  -13.370 0.430   1.00 13.27 ? 105 TYR A O   1 
ATOM   702  C  CB  . TYR A 1 105 ? -9.793  -11.126 2.187   1.00 12.95 ? 105 TYR A CB  1 
ATOM   703  C  CG  . TYR A 1 105 ? -10.224 -9.735  2.493   1.00 11.66 ? 105 TYR A CG  1 
ATOM   704  C  CD1 . TYR A 1 105 ? -11.082 -9.039  1.675   1.00 11.71 ? 105 TYR A CD1 1 
ATOM   705  C  CD2 . TYR A 1 105 ? -9.753  -9.092  3.607   1.00 12.86 ? 105 TYR A CD2 1 
ATOM   706  C  CE1 . TYR A 1 105 ? -11.441 -7.737  2.003   1.00 14.82 ? 105 TYR A CE1 1 
ATOM   707  C  CE2 . TYR A 1 105 ? -10.106 -7.784  3.942   1.00 12.99 ? 105 TYR A CE2 1 
ATOM   708  C  CZ  . TYR A 1 105 ? -10.916 -7.107  3.106   1.00 13.72 ? 105 TYR A CZ  1 
ATOM   709  O  OH  . TYR A 1 105 ? -11.346 -5.811  3.334   1.00 11.91 ? 105 TYR A OH  1 
ATOM   710  N  N   . THR A 1 106 ? -7.123  -13.088 1.659   1.00 12.04 ? 106 THR A N   1 
ATOM   711  C  CA  . THR A 1 106 ? -6.871  -14.457 1.827   1.00 12.51 ? 106 THR A CA  1 
ATOM   712  C  C   . THR A 1 106 ? -6.898  -14.810 3.275   1.00 13.82 ? 106 THR A C   1 
ATOM   713  O  O   . THR A 1 106 ? -6.223  -14.175 4.081   1.00 13.43 ? 106 THR A O   1 
ATOM   714  C  CB  . THR A 1 106 ? -5.536  -14.818 1.298   1.00 15.17 ? 106 THR A CB  1 
ATOM   715  O  OG1 . THR A 1 106 ? -5.474  -14.469 -0.085  1.00 19.62 ? 106 THR A OG1 1 
ATOM   716  C  CG2 . THR A 1 106 ? -5.237  -16.332 1.461   1.00 16.41 ? 106 THR A CG2 1 
ATOM   717  N  N   . ILE A 1 107 ? -7.720  -15.806 3.593   1.00 12.40 ? 107 ILE A N   1 
ATOM   718  C  CA  . ILE A 1 107 ? -7.809  -16.323 4.967   1.00 11.57 ? 107 ILE A CA  1 
ATOM   719  C  C   . ILE A 1 107 ? -7.096  -17.658 5.002   1.00 13.17 ? 107 ILE A C   1 
ATOM   720  O  O   . ILE A 1 107 ? -7.498  -18.575 4.292   1.00 14.14 ? 107 ILE A O   1 
ATOM   721  C  CB  . ILE A 1 107 ? -9.263  -16.510 5.439   1.00 13.63 ? 107 ILE A CB  1 
ATOM   722  C  CG1 . ILE A 1 107 ? -10.099 -15.215 5.288   1.00 17.30 ? 107 ILE A CG1 1 
ATOM   723  C  CG2 . ILE A 1 107 ? -9.318  -17.137 6.851   1.00 14.88 ? 107 ILE A CG2 1 
ATOM   724  C  CD1 . ILE A 1 107 ? -9.544  -14.075 6.063   1.00 17.09 ? 107 ILE A CD1 1 
ATOM   725  N  N   . ALA A 1 108 ? -6.000  -17.730 5.748   1.00 13.30 ? 108 ALA A N   1 
ATOM   726  C  CA  . ALA A 1 108 ? -5.219  -18.962 5.869   1.00 15.32 ? 108 ALA A CA  1 
ATOM   727  C  C   . ALA A 1 108 ? -5.444  -19.549 7.267   1.00 17.31 ? 108 ALA A C   1 
ATOM   728  O  O   . ALA A 1 108 ? -5.535  -18.812 8.248   1.00 15.66 ? 108 ALA A O   1 
ATOM   729  C  CB  . ALA A 1 108 ? -3.723  -18.620 5.688   1.00 17.30 ? 108 ALA A CB  1 
ATOM   730  N  N   . ALA A 1 109 ? -5.588  -20.874 7.337   1.00 15.06 ? 109 ALA A N   1 
ATOM   731  C  CA  . ALA A 1 109 ? -5.844  -21.560 8.580   1.00 15.87 ? 109 ALA A CA  1 
ATOM   732  C  C   . ALA A 1 109 ? -5.002  -22.816 8.667   1.00 13.91 ? 109 ALA A C   1 
ATOM   733  O  O   . ALA A 1 109 ? -4.762  -23.500 7.696   1.00 16.79 ? 109 ALA A O   1 
ATOM   734  C  CB  . ALA A 1 109 ? -7.320  -21.878 8.772   1.00 16.54 ? 109 ALA A CB  1 
ATOM   735  N  N   . LEU A 1 110 ? -4.428  -23.035 9.845   1.00 9.65  ? 110 LEU A N   1 
ATOM   736  C  CA  . LEU A 1 110 ? -3.640  -24.217 10.130  1.00 10.68 ? 110 LEU A CA  1 
ATOM   737  C  C   . LEU A 1 110 ? -4.393  -24.988 11.179  1.00 9.68  ? 110 LEU A C   1 
ATOM   738  O  O   . LEU A 1 110 ? -4.659  -24.476 12.304  1.00 11.67 ? 110 LEU A O   1 
ATOM   739  C  CB  . LEU A 1 110 ? -2.266  -23.822 10.619  1.00 11.22 ? 110 LEU A CB  1 
ATOM   740  C  CG  . LEU A 1 110 ? -1.315  -24.913 11.116  1.00 12.63 ? 110 LEU A CG  1 
ATOM   741  C  CD1 . LEU A 1 110 ? -0.989  -25.798 9.920   1.00 12.92 ? 110 LEU A CD1 1 
ATOM   742  C  CD2 . LEU A 1 110 ? -0.100  -24.236 11.701  1.00 15.87 ? 110 LEU A CD2 1 
ATOM   743  N  N   . LEU A 1 111 ? -4.727  -26.263 10.878  1.00 11.91 ? 111 LEU A N   1 
ATOM   744  C  CA  . LEU A 1 111 ? -5.560  -27.022 11.787  1.00 10.62 ? 111 LEU A CA  1 
ATOM   745  C  C   . LEU A 1 111 ? -4.892  -28.141 12.569  1.00 10.85 ? 111 LEU A C   1 
ATOM   746  O  O   . LEU A 1 111 ? -4.148  -28.903 12.016  1.00 10.57 ? 111 LEU A O   1 
ATOM   747  C  CB  . LEU A 1 111 ? -6.655  -27.726 10.976  1.00 10.34 ? 111 LEU A CB  1 
ATOM   748  C  CG  . LEU A 1 111 ? -7.477  -26.848 10.030  1.00 12.35 ? 111 LEU A CG  1 
ATOM   749  C  CD1 . LEU A 1 111 ? -8.562  -27.740 9.440   1.00 14.44 ? 111 LEU A CD1 1 
ATOM   750  C  CD2 . LEU A 1 111 ? -8.115  -25.638 10.763  1.00 12.71 ? 111 LEU A CD2 1 
ATOM   751  N  N   . SER A 1 112 ? -5.166  -28.169 13.882  1.00 11.29 ? 112 SER A N   1 
ATOM   752  C  CA  . SER A 1 112 ? -4.833  -29.291 14.747  1.00 10.89 ? 112 SER A CA  1 
ATOM   753  C  C   . SER A 1 112 ? -6.111  -29.682 15.501  1.00 12.40 ? 112 SER A C   1 
ATOM   754  O  O   . SER A 1 112 ? -7.049  -28.891 15.626  1.00 14.87 ? 112 SER A O   1 
ATOM   755  C  CB  . SER A 1 112 ? -3.722  -28.951 15.755  1.00 13.11 ? 112 SER A CB  1 
ATOM   756  O  OG  . SER A 1 112 ? -2.542  -28.580 15.107  1.00 13.48 ? 112 SER A OG  1 
ATOM   757  N  N   . PRO A 1 113 ? -6.116  -30.881 16.132  1.00 12.91 ? 113 PRO A N   1 
ATOM   758  C  CA  . PRO A 1 113 ? -7.377  -31.301 16.793  1.00 14.11 ? 113 PRO A CA  1 
ATOM   759  C  C   . PRO A 1 113 ? -7.800  -30.398 17.926  1.00 15.01 ? 113 PRO A C   1 
ATOM   760  O  O   . PRO A 1 113 ? -8.997  -30.260 18.105  1.00 16.69 ? 113 PRO A O   1 
ATOM   761  C  CB  . PRO A 1 113 ? -7.071  -32.738 17.239  1.00 15.81 ? 113 PRO A CB  1 
ATOM   762  C  CG  . PRO A 1 113 ? -6.162  -33.198 16.171  1.00 19.04 ? 113 PRO A CG  1 
ATOM   763  C  CD  . PRO A 1 113 ? -5.208  -32.005 15.887  1.00 16.43 ? 113 PRO A CD  1 
ATOM   764  N  N   . TYR A 1 114 ? -6.833  -29.837 18.681  1.00 13.16 ? 114 TYR A N   1 
ATOM   765  C  CA  . TYR A 1 114 ? -7.142  -28.998 19.834  1.00 13.15 ? 114 TYR A CA  1 
ATOM   766  C  C   . TYR A 1 114 ? -6.690  -27.558 19.662  1.00 12.67 ? 114 TYR A C   1 
ATOM   767  O  O   . TYR A 1 114 ? -6.735  -26.790 20.618  1.00 15.02 ? 114 TYR A O   1 
ATOM   768  C  CB  . TYR A 1 114 ? -6.600  -29.561 21.157  1.00 13.54 ? 114 TYR A CB  1 
ATOM   769  C  CG  . TYR A 1 114 ? -7.370  -30.706 21.652  1.00 14.33 ? 114 TYR A CG  1 
ATOM   770  C  CD1 . TYR A 1 114 ? -7.188  -31.922 21.120  1.00 17.52 ? 114 TYR A CD1 1 
ATOM   771  C  CD2 . TYR A 1 114 ? -8.223  -30.583 22.723  1.00 17.19 ? 114 TYR A CD2 1 
ATOM   772  C  CE1 . TYR A 1 114 ? -7.850  -33.020 21.604  1.00 22.05 ? 114 TYR A CE1 1 
ATOM   773  C  CE2 . TYR A 1 114 ? -8.919  -31.661 23.206  1.00 21.16 ? 114 TYR A CE2 1 
ATOM   774  C  CZ  . TYR A 1 114 ? -8.767  -32.859 22.594  1.00 19.90 ? 114 TYR A CZ  1 
ATOM   775  O  OH  . TYR A 1 114 ? -9.459  -33.915 23.116  1.00 26.73 ? 114 TYR A OH  1 
ATOM   776  N  N   . SER A 1 115 ? -6.337  -27.184 18.437  1.00 14.20 ? 115 SER A N   1 
ATOM   777  C  CA  . SER A 1 115 ? -5.855  -25.827 18.198  1.00 13.43 ? 115 SER A CA  1 
ATOM   778  C  C   . SER A 1 115 ? -6.059  -25.406 16.758  1.00 13.87 ? 115 SER A C   1 
ATOM   779  O  O   . SER A 1 115 ? -5.981  -26.227 15.849  1.00 13.17 ? 115 SER A O   1 
ATOM   780  C  CB  . SER A 1 115 ? -4.375  -25.751 18.506  1.00 15.35 ? 115 SER A CB  1 
ATOM   781  O  OG  . SER A 1 115 ? -3.885  -24.422 18.336  1.00 19.27 ? 115 SER A OG  1 
ATOM   782  N  N   . TYR A 1 116 ? -6.176  -24.104 16.557  1.00 11.86 ? 116 TYR A N   1 
ATOM   783  C  CA  . TYR A 1 116 ? -6.074  -23.631 15.156  1.00 9.35  ? 116 TYR A CA  1 
ATOM   784  C  C   . TYR A 1 116 ? -5.424  -22.247 15.143  1.00 9.12  ? 116 TYR A C   1 
ATOM   785  O  O   . TYR A 1 116 ? -5.485  -21.540 16.131  1.00 13.32 ? 116 TYR A O   1 
ATOM   786  C  CB  . TYR A 1 116 ? -7.365  -23.682 14.322  1.00 13.56 ? 116 TYR A CB  1 
ATOM   787  C  CG  . TYR A 1 116 ? -8.452  -22.814 14.862  1.00 15.26 ? 116 TYR A CG  1 
ATOM   788  C  CD1 . TYR A 1 116 ? -9.277  -23.315 15.841  1.00 16.94 ? 116 TYR A CD1 1 
ATOM   789  C  CD2 . TYR A 1 116 ? -8.613  -21.512 14.430  1.00 23.07 ? 116 TYR A CD2 1 
ATOM   790  C  CE1 . TYR A 1 116 ? -10.273 -22.540 16.380  1.00 21.70 ? 116 TYR A CE1 1 
ATOM   791  C  CE2 . TYR A 1 116 ? -9.606  -20.714 14.966  1.00 20.59 ? 116 TYR A CE2 1 
ATOM   792  C  CZ  . TYR A 1 116 ? -10.427 -21.246 15.939  1.00 18.88 ? 116 TYR A CZ  1 
ATOM   793  O  OH  . TYR A 1 116 ? -11.398 -20.538 16.547  1.00 40.35 ? 116 TYR A OH  1 
ATOM   794  N  N   . SER A 1 117 ? -4.732  -21.957 14.058  1.00 11.28 ? 117 SER A N   1 
ATOM   795  C  CA  . SER A 1 117 ? -4.156  -20.664 13.834  1.00 12.20 ? 117 SER A CA  1 
ATOM   796  C  C   . SER A 1 117 ? -4.715  -20.118 12.549  1.00 13.36 ? 117 SER A C   1 
ATOM   797  O  O   . SER A 1 117 ? -4.861  -20.830 11.579  1.00 12.43 ? 117 SER A O   1 
ATOM   798  C  CB  . SER A 1 117 ? -2.610  -20.745 13.711  1.00 12.52 ? 117 SER A CB  1 
ATOM   799  O  OG  . SER A 1 117 ? -2.001  -21.327 14.872  1.00 16.11 ? 117 SER A OG  1 
ATOM   800  N  N   . THR A 1 118 ? -4.987  -18.846 12.521  1.00 11.71 ? 118 THR A N   1 
ATOM   801  C  CA  . THR A 1 118 ? -5.492  -18.228 11.325  1.00 10.71 ? 118 THR A CA  1 
ATOM   802  C  C   . THR A 1 118 ? -4.875  -16.845 11.085  1.00 11.44 ? 118 THR A C   1 
ATOM   803  O  O   . THR A 1 118 ? -4.561  -16.134 12.027  1.00 13.08 ? 118 THR A O   1 
ATOM   804  C  CB  . THR A 1 118 ? -7.017  -18.196 11.398  1.00 14.87 ? 118 THR A CB  1 
ATOM   805  O  OG1 . THR A 1 118 ? -7.441  -17.743 10.173  1.00 15.40 ? 118 THR A OG1 1 
ATOM   806  C  CG2 . THR A 1 118 ? -7.589  -17.288 12.476  1.00 17.43 ? 118 THR A CG2 1 
ATOM   807  N  N   . THR A 1 119 ? -4.561  -16.533 9.838   1.00 11.17 ? 119 THR A N   1 
ATOM   808  C  CA  . THR A 1 119 ? -4.107  -15.182 9.492   1.00 10.78 ? 119 THR A CA  1 
ATOM   809  C  C   . THR A 1 119 ? -4.827  -14.651 8.263   1.00 11.00 ? 119 THR A C   1 
ATOM   810  O  O   . THR A 1 119 ? -5.454  -15.404 7.547   1.00 13.04 ? 119 THR A O   1 
ATOM   811  C  CB  . THR A 1 119 ? -2.577  -15.133 9.277   1.00 11.85 ? 119 THR A CB  1 
ATOM   812  O  OG1 . THR A 1 119 ? -2.119  -13.784 9.387   1.00 12.86 ? 119 THR A OG1 1 
ATOM   813  C  CG2 . THR A 1 119 ? -2.083  -15.810 7.993   1.00 16.86 ? 119 THR A CG2 1 
ATOM   814  N  N   . ALA A 1 120 ? -4.684  -13.374 8.010   1.00 10.78 ? 120 ALA A N   1 
ATOM   815  C  CA  . ALA A 1 120 ? -5.242  -12.738 6.849   1.00 10.34 ? 120 ALA A CA  1 
ATOM   816  C  C   . ALA A 1 120 ? -4.179  -11.996 6.073   1.00 9.87  ? 120 ALA A C   1 
ATOM   817  O  O   . ALA A 1 120 ? -3.293  -11.333 6.637   1.00 12.58 ? 120 ALA A O   1 
ATOM   818  C  CB  . ALA A 1 120 ? -6.334  -11.777 7.323   1.00 12.96 ? 120 ALA A CB  1 
ATOM   819  N  N   . VAL A 1 121 ? -4.238  -12.140 4.770   1.00 9.77  ? 121 VAL A N   1 
ATOM   820  C  CA  . VAL A 1 121 ? -3.541  -11.295 3.843   1.00 12.17 ? 121 VAL A CA  1 
ATOM   821  C  C   . VAL A 1 121 ? -4.517  -10.435 3.102   1.00 12.12 ? 121 VAL A C   1 
ATOM   822  O  O   . VAL A 1 121 ? -5.454  -10.951 2.416   1.00 17.04 ? 121 VAL A O   1 
ATOM   823  C  CB  . VAL A 1 121 ? -2.740  -12.159 2.858   1.00 16.09 ? 121 VAL A CB  1 
ATOM   824  C  CG1 . VAL A 1 121 ? -1.975  -11.301 1.848   1.00 18.82 ? 121 VAL A CG1 1 
ATOM   825  C  CG2 . VAL A 1 121 ? -1.774  -13.041 3.622   1.00 20.76 ? 121 VAL A CG2 1 
ATOM   826  N  N   . VAL A 1 122 ? -4.296  -9.123  3.170   1.00 12.33 ? 122 VAL A N   1 
ATOM   827  C  CA  . VAL A 1 122 ? -5.183  -8.133  2.582   1.00 13.99 ? 122 VAL A CA  1 
ATOM   828  C  C   . VAL A 1 122 ? -4.391  -7.353  1.558   1.00 15.57 ? 122 VAL A C   1 
ATOM   829  O  O   . VAL A 1 122 ? -3.356  -6.811  1.887   1.00 19.34 ? 122 VAL A O   1 
ATOM   830  C  CB  . VAL A 1 122 ? -5.747  -7.159  3.621   1.00 15.15 ? 122 VAL A CB  1 
ATOM   831  C  CG1 . VAL A 1 122 ? -6.799  -6.249  2.978   1.00 16.20 ? 122 VAL A CG1 1 
ATOM   832  C  CG2 . VAL A 1 122 ? -6.389  -7.920  4.746   1.00 16.50 ? 122 VAL A CG2 1 
ATOM   833  N  N   . THR A 1 123 ? -4.910  -7.324  0.325   1.00 15.93 ? 123 THR A N   1 
ATOM   834  C  CA  . THR A 1 123 ? -4.268  -6.594  -0.802  1.00 19.02 ? 123 THR A CA  1 
ATOM   835  C  C   . THR A 1 123 ? -5.201  -5.602  -1.466  1.00 18.12 ? 123 THR A C   1 
ATOM   836  O  O   . THR A 1 123 ? -6.415  -5.808  -1.412  1.00 17.92 ? 123 THR A O   1 
ATOM   837  C  CB  . THR A 1 123 ? -3.642  -7.577  -1.812  1.00 29.75 ? 123 THR A CB  1 
ATOM   838  O  OG1 . THR A 1 123 ? -4.653  -8.327  -2.490  1.00 36.28 ? 123 THR A OG1 1 
ATOM   839  C  CG2 . THR A 1 123 ? -2.715  -8.551  -1.096  1.00 29.55 ? 123 THR A CG2 1 
ATOM   840  N  N   . ASN A 1 124 ? -4.593  -4.563  -2.077  1.00 24.42 ? 124 ASN A N   1 
ATOM   841  C  CA  . ASN A 1 124 ? -5.113  -3.422  -2.971  1.00 36.14 ? 124 ASN A CA  1 
ATOM   842  C  C   . ASN A 1 124 ? -6.094  -2.359  -2.434  1.00 40.19 ? 124 ASN A C   1 
ATOM   843  O  O   . ASN A 1 124 ? -6.346  -1.302  -3.075  1.00 38.92 ? 124 ASN A O   1 
ATOM   844  C  CB  . ASN A 1 124 ? -5.334  -3.867  -4.452  1.00 36.75 ? 124 ASN A CB  1 
ATOM   845  C  CG  . ASN A 1 124 ? -6.778  -4.245  -4.800  1.00 25.89 ? 124 ASN A CG  1 
ATOM   846  O  OD1 . ASN A 1 124 ? -7.741  -3.970  -4.036  1.00 40.69 ? 124 ASN A OD1 1 
ATOM   847  N  ND2 . ASN A 1 124 ? -6.957  -4.836  -6.007  1.00 39.87 ? 124 ASN A ND2 1 
ATOM   848  C  C   . CYS B 1 10  ? -12.224 -24.473 36.966  1.00 37.11 ? 10  CYS B C   1 
ATOM   849  O  O   . CYS B 1 10  ? -11.180 -24.775 36.414  1.00 42.24 ? 10  CYS B O   1 
ATOM   850  C  CB  . CYS B 1 10  ? -11.380 -24.839 39.379  1.00 39.45 ? 10  CYS B CB  1 
ATOM   851  N  N   . PRO B 1 11  ? -13.407 -24.860 36.489  1.00 30.55 ? 11  PRO B N   1 
ATOM   852  C  CA  . PRO B 1 11  ? -13.429 -25.755 35.344  1.00 29.61 ? 11  PRO B CA  1 
ATOM   853  C  C   . PRO B 1 11  ? -13.099 -25.159 34.002  1.00 25.99 ? 11  PRO B C   1 
ATOM   854  O  O   . PRO B 1 11  ? -12.791 -25.888 33.131  1.00 26.68 ? 11  PRO B O   1 
ATOM   855  C  CB  . PRO B 1 11  ? -14.858 -26.286 35.310  1.00 38.50 ? 11  PRO B CB  1 
ATOM   856  C  CG  . PRO B 1 11  ? -15.666 -25.320 36.089  1.00 33.57 ? 11  PRO B CG  1 
ATOM   857  C  CD  . PRO B 1 11  ? -14.739 -24.645 37.063  1.00 31.40 ? 11  PRO B CD  1 
ATOM   858  N  N   . LEU B 1 12  ? -13.142 -23.845 33.860  1.00 22.29 ? 12  LEU B N   1 
ATOM   859  C  CA  . LEU B 1 12  ? -12.903 -23.189 32.560  1.00 22.65 ? 12  LEU B CA  1 
ATOM   860  C  C   . LEU B 1 12  ? -12.121 -21.923 32.836  1.00 23.06 ? 12  LEU B C   1 
ATOM   861  O  O   . LEU B 1 12  ? -12.561 -21.065 33.581  1.00 25.08 ? 12  LEU B O   1 
ATOM   862  C  CB  . LEU B 1 12  ? -14.201 -22.844 31.838  1.00 21.99 ? 12  LEU B CB  1 
ATOM   863  C  CG  . LEU B 1 12  ? -14.146 -22.196 30.471  1.00 26.69 ? 12  LEU B CG  1 
ATOM   864  C  CD1 . LEU B 1 12  ? -13.461 -23.033 29.399  1.00 23.67 ? 12  LEU B CD1 1 
ATOM   865  C  CD2 . LEU B 1 12  ? -15.570 -21.842 30.083  1.00 25.52 ? 12  LEU B CD2 1 
ATOM   866  N  N   . MET B 1 13  ? -10.947 -21.818 32.255  1.00 24.60 ? 13  MET B N   1 
ATOM   867  C  CA  A MET B 1 13  ? -10.039 -20.669 32.360  0.50 22.37 ? 13  MET B CA  1 
ATOM   868  C  CA  B MET B 1 13  ? -10.215 -20.548 32.311  0.50 20.72 ? 13  MET B CA  1 
ATOM   869  C  C   . MET B 1 13  ? -9.763  -20.167 30.941  1.00 19.04 ? 13  MET B C   1 
ATOM   870  O  O   . MET B 1 13  ? -9.599  -20.993 30.032  1.00 19.94 ? 13  MET B O   1 
ATOM   871  C  CB  A MET B 1 13  ? -8.718  -21.146 33.050  0.50 17.24 ? 13  MET B CB  1 
ATOM   872  C  CB  B MET B 1 13  ? -9.036  -20.585 33.307  0.50 23.82 ? 13  MET B CB  1 
ATOM   873  C  CG  A MET B 1 13  ? -8.906  -21.580 34.532  0.50 25.32 ? 13  MET B CG  1 
ATOM   874  C  CG  B MET B 1 13  ? -7.638  -20.833 32.763  0.50 29.38 ? 13  MET B CG  1 
ATOM   875  S  SD  A MET B 1 13  ? -7.563  -22.593 35.224  0.50 42.75 ? 13  MET B SD  1 
ATOM   876  S  SD  B MET B 1 13  ? -6.702  -19.354 32.254  0.50 28.12 ? 13  MET B SD  1 
ATOM   877  C  CE  A MET B 1 13  ? -7.825  -22.460 36.996  0.50 44.58 ? 13  MET B CE  1 
ATOM   878  C  CE  B MET B 1 13  ? -5.120  -20.199 32.426  0.50 31.40 ? 13  MET B CE  1 
ATOM   879  N  N   . VAL B 1 14  ? -9.614  -18.853 30.802  1.00 17.55 ? 14  VAL B N   1 
ATOM   880  C  CA  . VAL B 1 14  ? -9.242  -18.295 29.504  1.00 18.17 ? 14  VAL B CA  1 
ATOM   881  C  C   . VAL B 1 14  ? -8.010  -17.466 29.714  1.00 18.71 ? 14  VAL B C   1 
ATOM   882  O  O   . VAL B 1 14  ? -7.887  -16.790 30.731  1.00 21.15 ? 14  VAL B O   1 
ATOM   883  C  CB  . VAL B 1 14  ? -10.419 -17.483 28.859  1.00 19.16 ? 14  VAL B CB  1 
ATOM   884  C  CG1 . VAL B 1 14  ? -9.996  -16.666 27.650  1.00 22.07 ? 14  VAL B CG1 1 
ATOM   885  C  CG2 . VAL B 1 14  ? -11.557 -18.389 28.506  1.00 21.84 ? 14  VAL B CG2 1 
ATOM   886  N  N   . LYS B 1 15  ? -7.057  -17.579 28.813  1.00 20.88 ? 15  LYS B N   1 
ATOM   887  C  CA  . LYS B 1 15  ? -5.837  -16.820 28.885  1.00 17.89 ? 15  LYS B CA  1 
ATOM   888  C  C   . LYS B 1 15  ? -5.599  -16.156 27.504  1.00 20.15 ? 15  LYS B C   1 
ATOM   889  O  O   . LYS B 1 15  ? -5.807  -16.780 26.469  1.00 18.72 ? 15  LYS B O   1 
ATOM   890  C  CB  . LYS B 1 15  ? -4.685  -17.774 29.245  1.00 21.65 ? 15  LYS B CB  1 
ATOM   891  C  CG  . LYS B 1 15  ? -3.348  -17.068 29.267  1.00 28.74 ? 15  LYS B CG  1 
ATOM   892  C  CD  . LYS B 1 15  ? -2.256  -17.797 30.017  1.00 33.64 ? 15  LYS B CD  1 
ATOM   893  C  CE  . LYS B 1 15  ? -1.185  -16.799 30.533  1.00 39.43 ? 15  LYS B CE  1 
ATOM   894  N  N   . VAL B 1 16  ? -5.138  -14.910 27.520  1.00 16.35 ? 16  VAL B N   1 
ATOM   895  C  CA  . VAL B 1 16  ? -4.958  -14.181 26.290  1.00 14.99 ? 16  VAL B CA  1 
ATOM   896  C  C   . VAL B 1 16  ? -3.607  -13.472 26.307  1.00 16.20 ? 16  VAL B C   1 
ATOM   897  O  O   . VAL B 1 16  ? -3.244  -12.794 27.309  1.00 15.30 ? 16  VAL B O   1 
ATOM   898  C  CB  . VAL B 1 16  ? -6.109  -13.148 26.078  1.00 13.55 ? 16  VAL B CB  1 
ATOM   899  C  CG1 . VAL B 1 16  ? -6.010  -12.477 24.703  1.00 16.39 ? 16  VAL B CG1 1 
ATOM   900  C  CG2 . VAL B 1 16  ? -7.487  -13.758 26.326  1.00 15.75 ? 16  VAL B CG2 1 
ATOM   901  N  N   . LEU B 1 17  ? -2.860  -13.669 25.221  1.00 14.05 ? 17  LEU B N   1 
ATOM   902  C  CA  . LEU B 1 17  ? -1.470  -13.188 25.110  1.00 14.95 ? 17  LEU B CA  1 
ATOM   903  C  C   . LEU B 1 17  ? -1.377  -12.310 23.872  1.00 14.41 ? 17  LEU B C   1 
ATOM   904  O  O   . LEU B 1 17  ? -2.064  -12.562 22.889  1.00 14.22 ? 17  LEU B O   1 
ATOM   905  C  CB  . LEU B 1 17  ? -0.544  -14.391 25.016  1.00 14.82 ? 17  LEU B CB  1 
ATOM   906  C  CG  . LEU B 1 17  ? -0.537  -15.343 26.246  1.00 20.16 ? 17  LEU B CG  1 
ATOM   907  C  CD1 . LEU B 1 17  ? 0.335   -16.555 25.936  1.00 29.65 ? 17  LEU B CD1 1 
ATOM   908  C  CD2 . LEU B 1 17  ? -0.053  -14.617 27.460  1.00 22.17 ? 17  LEU B CD2 1 
ATOM   909  N  N   . ASP B 1 18  ? -0.482  -11.323 23.944  1.00 13.01 ? 18  ASP B N   1 
ATOM   910  C  CA  . ASP B 1 18  ? -0.234  -10.377 22.852  1.00 14.01 ? 18  ASP B CA  1 
ATOM   911  C  C   . ASP B 1 18  ? 1.119   -10.671 22.210  1.00 11.27 ? 18  ASP B C   1 
ATOM   912  O  O   . ASP B 1 18  ? 2.186   -10.572 22.874  1.00 14.43 ? 18  ASP B O   1 
ATOM   913  C  CB  . ASP B 1 18  ? -0.272  -8.996  23.495  1.00 15.40 ? 18  ASP B CB  1 
ATOM   914  C  CG  . ASP B 1 18  ? 0.008   -7.845  22.563  1.00 12.64 ? 18  ASP B CG  1 
ATOM   915  O  OD1 . ASP B 1 18  ? 0.763   -8.017  21.551  1.00 12.98 ? 18  ASP B OD1 1 
ATOM   916  O  OD2 . ASP B 1 18  ? -0.472  -6.724  22.861  1.00 15.57 ? 18  ASP B OD2 1 
ATOM   917  N  N   . ALA B 1 19  ? 1.072   -11.071 20.948  1.00 12.52 ? 19  ALA B N   1 
ATOM   918  C  CA  . ALA B 1 19  ? 2.262   -11.507 20.188  1.00 11.56 ? 19  ALA B CA  1 
ATOM   919  C  C   . ALA B 1 19  ? 3.060   -10.337 19.578  1.00 11.95 ? 19  ALA B C   1 
ATOM   920  O  O   . ALA B 1 19  ? 4.092   -10.580 19.004  1.00 14.21 ? 19  ALA B O   1 
ATOM   921  C  CB  . ALA B 1 19  ? 1.853   -12.509 19.067  1.00 14.10 ? 19  ALA B CB  1 
ATOM   922  N  N   . VAL B 1 20  ? 2.554   -9.113  19.716  1.00 12.83 ? 20  VAL B N   1 
ATOM   923  C  CA  . VAL B 1 20  ? 3.181   -7.956  19.140  1.00 14.57 ? 20  VAL B CA  1 
ATOM   924  C  C   . VAL B 1 20  ? 4.034   -7.246  20.205  1.00 16.95 ? 20  VAL B C   1 
ATOM   925  O  O   . VAL B 1 20  ? 5.163   -6.912  19.977  1.00 17.66 ? 20  VAL B O   1 
ATOM   926  C  CB  . VAL B 1 20  ? 2.195   -6.979  18.486  1.00 17.16 ? 20  VAL B CB  1 
ATOM   927  C  CG1 . VAL B 1 20  ? 2.891   -5.671  18.123  1.00 25.90 ? 20  VAL B CG1 1 
ATOM   928  C  CG2 . VAL B 1 20  ? 1.459   -7.633  17.317  1.00 22.02 ? 20  VAL B CG2 1 
ATOM   929  N  N   . ARG B 1 21  ? 3.506   -7.134  21.382  1.00 16.96 ? 21  ARG B N   1 
ATOM   930  C  CA  . ARG B 1 21  ? 4.197   -6.587  22.497  1.00 14.49 ? 21  ARG B CA  1 
ATOM   931  C  C   . ARG B 1 21  ? 4.860   -7.568  23.464  1.00 15.75 ? 21  ARG B C   1 
ATOM   932  O  O   . ARG B 1 21  ? 5.633   -7.118  24.341  1.00 19.96 ? 21  ARG B O   1 
ATOM   933  C  CB  . ARG B 1 21  ? 3.337   -5.599  23.244  1.00 20.94 ? 21  ARG B CB  1 
ATOM   934  C  CG  . ARG B 1 21  ? 2.571   -4.611  22.359  1.00 23.05 ? 21  ARG B CG  1 
ATOM   935  C  CD  . ARG B 1 21  ? 1.875   -3.609  23.247  1.00 25.52 ? 21  ARG B CD  1 
ATOM   936  N  NE  . ARG B 1 21  ? 0.806   -4.207  23.989  1.00 25.45 ? 21  ARG B NE  1 
ATOM   937  C  CZ  . ARG B 1 21  ? 0.456   -3.892  25.237  1.00 29.39 ? 21  ARG B CZ  1 
ATOM   938  N  NH1 . ARG B 1 21  ? 1.141   -3.006  25.984  1.00 31.72 ? 21  ARG B NH1 1 
ATOM   939  N  NH2 . ARG B 1 21  ? -0.542  -4.561  25.793  1.00 34.12 ? 21  ARG B NH2 1 
ATOM   940  N  N   . GLY B 1 22  ? 4.547   -8.861  23.322  1.00 18.48 ? 22  GLY B N   1 
ATOM   941  C  CA  . GLY B 1 22  ? 5.118   -9.922  24.134  1.00 19.81 ? 22  GLY B CA  1 
ATOM   942  C  C   . GLY B 1 22  ? 4.658   -9.851  25.585  1.00 16.61 ? 22  GLY B C   1 
ATOM   943  O  O   . GLY B 1 22  ? 5.478   -9.889  26.533  1.00 20.51 ? 22  GLY B O   1 
ATOM   944  N  N   . SER B 1 23  ? 3.369   -9.675  25.752  1.00 17.14 ? 23  SER B N   1 
ATOM   945  C  CA  . SER B 1 23  ? 2.808   -9.426  27.062  1.00 18.17 ? 23  SER B CA  1 
ATOM   946  C  C   . SER B 1 23  ? 1.474   -10.118 27.197  1.00 17.84 ? 23  SER B C   1 
ATOM   947  O  O   . SER B 1 23  ? 0.817   -10.449 26.198  1.00 16.41 ? 23  SER B O   1 
ATOM   948  C  CB  . SER B 1 23  ? 2.606   -7.923  27.251  1.00 27.11 ? 23  SER B CB  1 
ATOM   949  O  OG  . SER B 1 23  ? 1.563   -7.504  26.417  1.00 32.47 ? 23  SER B OG  1 
ATOM   950  N  N   . PRO B 1 24  ? 1.033   -10.286 28.439  1.00 16.65 ? 24  PRO B N   1 
ATOM   951  C  CA  . PRO B 1 24  ? -0.381  -10.678 28.619  1.00 15.42 ? 24  PRO B CA  1 
ATOM   952  C  C   . PRO B 1 24  ? -1.303  -9.596  27.990  1.00 18.98 ? 24  PRO B C   1 
ATOM   953  O  O   . PRO B 1 24  ? -0.950  -8.398  28.023  1.00 18.56 ? 24  PRO B O   1 
ATOM   954  C  CB  . PRO B 1 24  ? -0.563  -10.712 30.138  1.00 21.26 ? 24  PRO B CB  1 
ATOM   955  C  CG  . PRO B 1 24  ? 0.815   -10.716 30.708  1.00 27.83 ? 24  PRO B CG  1 
ATOM   956  C  CD  . PRO B 1 24  ? 1.707   -10.039 29.703  1.00 17.89 ? 24  PRO B CD  1 
ATOM   957  N  N   . ALA B 1 25  ? -2.484  -9.993  27.503  1.00 17.82 ? 25  ALA B N   1 
ATOM   958  C  CA  . ALA B 1 25  ? -3.496  -9.025  27.008  1.00 14.95 ? 25  ALA B CA  1 
ATOM   959  C  C   . ALA B 1 25  ? -4.467  -8.760  28.185  1.00 13.43 ? 25  ALA B C   1 
ATOM   960  O  O   . ALA B 1 25  ? -5.273  -9.581  28.521  1.00 16.77 ? 25  ALA B O   1 
ATOM   961  C  CB  . ALA B 1 25  ? -4.272  -9.589  25.834  1.00 14.54 ? 25  ALA B CB  1 
ATOM   962  N  N   . ILE B 1 26  ? -4.343  -7.566  28.762  1.00 17.97 ? 26  ILE B N   1 
ATOM   963  C  CA  . ILE B 1 26  ? -5.049  -7.109  29.920  1.00 15.77 ? 26  ILE B CA  1 
ATOM   964  C  C   . ILE B 1 26  ? -6.323  -6.407  29.637  1.00 15.45 ? 26  ILE B C   1 
ATOM   965  O  O   . ILE B 1 26  ? -6.416  -5.691  28.735  1.00 19.33 ? 26  ILE B O   1 
ATOM   966  C  CB  . ILE B 1 26  ? -4.121  -6.186  30.777  1.00 19.96 ? 26  ILE B CB  1 
ATOM   967  C  CG1 . ILE B 1 26  ? -2.806  -6.945  31.063  1.00 19.23 ? 26  ILE B CG1 1 
ATOM   968  C  CG2 . ILE B 1 26  ? -4.818  -5.634  32.055  1.00 27.04 ? 26  ILE B CG2 1 
ATOM   969  C  CD1 . ILE B 1 26  ? -1.699  -6.099  31.649  1.00 28.60 ? 26  ILE B CD1 1 
ATOM   970  N  N   . ASN B 1 27  ? -7.326  -6.672  30.468  1.00 18.10 ? 27  ASN B N   1 
ATOM   971  C  CA  . ASN B 1 27  ? -8.624  -6.027  30.383  1.00 18.77 ? 27  ASN B CA  1 
ATOM   972  C  C   . ASN B 1 27  ? -9.356  -6.326  29.086  1.00 19.37 ? 27  ASN B C   1 
ATOM   973  O  O   . ASN B 1 27  ? -10.065 -5.488  28.545  1.00 23.07 ? 27  ASN B O   1 
ATOM   974  C  CB  . ASN B 1 27  ? -8.460  -4.511  30.550  1.00 21.51 ? 27  ASN B CB  1 
ATOM   975  C  CG  . ASN B 1 27  ? -9.624  -3.850  31.261  1.00 32.08 ? 27  ASN B CG  1 
ATOM   976  O  OD1 . ASN B 1 27  ? -10.522 -4.506  31.828  1.00 33.02 ? 27  ASN B OD1 1 
ATOM   977  N  N   . VAL B 1 28  ? -9.215  -7.553  28.608  1.00 16.25 ? 28  VAL B N   1 
ATOM   978  C  CA  . VAL B 1 28  ? -9.921  -7.981  27.448  1.00 16.02 ? 28  VAL B CA  1 
ATOM   979  C  C   . VAL B 1 28  ? -11.213 -8.668  27.835  1.00 16.78 ? 28  VAL B C   1 
ATOM   980  O  O   . VAL B 1 28  ? -11.221 -9.577  28.672  1.00 18.29 ? 28  VAL B O   1 
ATOM   981  C  CB  . VAL B 1 28  ? -9.025  -8.914  26.568  1.00 15.86 ? 28  VAL B CB  1 
ATOM   982  C  CG1 . VAL B 1 28  ? -9.762  -9.402  25.329  1.00 18.03 ? 28  VAL B CG1 1 
ATOM   983  C  CG2 . VAL B 1 28  ? -7.723  -8.205  26.164  1.00 20.06 ? 28  VAL B CG2 1 
ATOM   984  N  N   . ALA B 1 29  ? -12.291 -8.259  27.149  1.00 13.67 ? 29  ALA B N   1 
ATOM   985  C  CA  . ALA B 1 29  ? -13.610 -8.877  27.356  1.00 16.04 ? 29  ALA B CA  1 
ATOM   986  C  C   . ALA B 1 29  ? -13.651 -10.238 26.699  1.00 15.70 ? 29  ALA B C   1 
ATOM   987  O  O   . ALA B 1 29  ? -13.222 -10.430 25.582  1.00 16.72 ? 29  ALA B O   1 
ATOM   988  C  CB  . ALA B 1 29  ? -14.801 -7.991  26.860  1.00 19.47 ? 29  ALA B CB  1 
ATOM   989  N  N   . VAL B 1 30  ? -14.177 -11.187 27.464  1.00 14.61 ? 30  VAL B N   1 
ATOM   990  C  CA  . VAL B 1 30  ? -14.367 -12.564 27.073  1.00 16.70 ? 30  VAL B CA  1 
ATOM   991  C  C   . VAL B 1 30  ? -15.790 -12.992 27.364  1.00 17.57 ? 30  VAL B C   1 
ATOM   992  O  O   . VAL B 1 30  ? -16.260 -12.860 28.511  1.00 16.39 ? 30  VAL B O   1 
ATOM   993  C  CB  . VAL B 1 30  ? -13.389 -13.504 27.811  1.00 14.89 ? 30  VAL B CB  1 
ATOM   994  C  CG1 . VAL B 1 30  ? -13.609 -14.944 27.390  1.00 20.90 ? 30  VAL B CG1 1 
ATOM   995  C  CG2 . VAL B 1 30  ? -11.963 -13.160 27.586  1.00 17.57 ? 30  VAL B CG2 1 
ATOM   996  N  N   . HIS B 1 31  ? -16.463 -13.534 26.342  1.00 19.38 ? 31  HIS B N   1 
ATOM   997  C  CA  . HIS B 1 31  ? -17.829 -13.998 26.508  1.00 20.82 ? 31  HIS B CA  1 
ATOM   998  C  C   . HIS B 1 31  ? -17.885 -15.456 26.154  1.00 17.59 ? 31  HIS B C   1 
ATOM   999  O  O   . HIS B 1 31  ? -17.350 -15.882 25.153  1.00 23.60 ? 31  HIS B O   1 
ATOM   1000 C  CB  . HIS B 1 31  ? -18.808 -13.196 25.620  1.00 24.10 ? 31  HIS B CB  1 
ATOM   1001 C  CG  . HIS B 1 31  ? -19.087 -11.813 26.137  1.00 25.58 ? 31  HIS B CG  1 
ATOM   1002 N  ND1 . HIS B 1 31  ? -18.246 -10.774 25.898  1.00 29.90 ? 31  HIS B ND1 1 
ATOM   1003 C  CD2 . HIS B 1 31  ? -20.113 -11.324 26.933  1.00 31.13 ? 31  HIS B CD2 1 
ATOM   1004 C  CE1 . HIS B 1 31  ? -18.721 -9.674  26.495  1.00 37.58 ? 31  HIS B CE1 1 
ATOM   1005 N  NE2 . HIS B 1 31  ? -19.868 -10.010 27.145  1.00 35.35 ? 31  HIS B NE2 1 
ATOM   1006 N  N   . VAL B 1 32  ? -18.579 -16.222 26.950  1.00 19.74 ? 32  VAL B N   1 
ATOM   1007 C  CA  . VAL B 1 32  ? -18.738 -17.645 26.691  1.00 19.55 ? 32  VAL B CA  1 
ATOM   1008 C  C   . VAL B 1 32  ? -20.229 -17.898 26.471  1.00 20.61 ? 32  VAL B C   1 
ATOM   1009 O  O   . VAL B 1 32  ? -21.087 -17.353 27.218  1.00 23.82 ? 32  VAL B O   1 
ATOM   1010 C  CB  . VAL B 1 32  ? -18.200 -18.506 27.861  1.00 15.56 ? 32  VAL B CB  1 
ATOM   1011 C  CG1 . VAL B 1 32  ? -18.251 -19.982 27.533  1.00 16.22 ? 32  VAL B CG1 1 
ATOM   1012 C  CG2 . VAL B 1 32  ? -16.805 -18.101 28.329  1.00 16.98 ? 32  VAL B CG2 1 
ATOM   1013 N  N   . PHE B 1 33  ? -20.542 -18.688 25.452  1.00 19.27 ? 33  PHE B N   1 
ATOM   1014 C  CA  . PHE B 1 33  ? -21.934 -19.058 25.100  1.00 25.70 ? 33  PHE B CA  1 
ATOM   1015 C  C   . PHE B 1 33  ? -22.029 -20.573 25.096  1.00 23.86 ? 33  PHE B C   1 
ATOM   1016 O  O   . PHE B 1 33  ? -21.032 -21.256 24.902  1.00 20.84 ? 33  PHE B O   1 
ATOM   1017 C  CB  . PHE B 1 33  ? -22.352 -18.516 23.718  1.00 31.77 ? 33  PHE B CB  1 
ATOM   1018 C  CG  . PHE B 1 33  ? -22.152 -17.045 23.575  1.00 33.76 ? 33  PHE B CG  1 
ATOM   1019 C  CD1 . PHE B 1 33  ? -23.144 -16.153 23.944  1.00 40.93 ? 33  PHE B CD1 1 
ATOM   1020 C  CD2 . PHE B 1 33  ? -20.926 -16.553 23.149  1.00 28.04 ? 33  PHE B CD2 1 
ATOM   1021 C  CE1 . PHE B 1 33  ? -22.939 -14.773 23.842  1.00 37.17 ? 33  PHE B CE1 1 
ATOM   1022 C  CE2 . PHE B 1 33  ? -20.707 -15.183 23.043  1.00 32.79 ? 33  PHE B CE2 1 
ATOM   1023 C  CZ  . PHE B 1 33  ? -21.720 -14.297 23.389  1.00 30.63 ? 33  PHE B CZ  1 
ATOM   1024 N  N   . ARG B 1 34  ? -23.227 -21.090 25.398  1.00 26.15 ? 34  ARG B N   1 
ATOM   1025 C  CA  . ARG B 1 34  ? -23.541 -22.507 25.279  1.00 27.55 ? 34  ARG B CA  1 
ATOM   1026 C  C   . ARG B 1 34  ? -24.659 -22.637 24.283  1.00 31.03 ? 34  ARG B C   1 
ATOM   1027 O  O   . ARG B 1 34  ? -25.648 -21.935 24.351  1.00 38.44 ? 34  ARG B O   1 
ATOM   1028 C  CB  . ARG B 1 34  ? -23.988 -23.095 26.626  1.00 29.29 ? 34  ARG B CB  1 
ATOM   1029 C  CG  . ARG B 1 34  ? -24.178 -24.626 26.652  1.00 28.91 ? 34  ARG B CG  1 
ATOM   1030 C  CD  . ARG B 1 34  ? -24.580 -25.101 28.045  1.00 30.33 ? 34  ARG B CD  1 
ATOM   1031 N  NE  . ARG B 1 34  ? -24.251 -26.497 28.224  1.00 37.15 ? 34  ARG B NE  1 
ATOM   1032 N  N   . LYS B 1 35  ? -24.551 -23.625 23.417  1.00 29.85 ? 35  LYS B N   1 
ATOM   1033 C  CA  . LYS B 1 35  ? -25.580 -23.879 22.423  1.00 31.42 ? 35  LYS B CA  1 
ATOM   1034 C  C   . LYS B 1 35  ? -26.832 -24.518 23.034  1.00 37.76 ? 35  LYS B C   1 
ATOM   1035 O  O   . LYS B 1 35  ? -26.755 -25.559 23.693  1.00 30.11 ? 35  LYS B O   1 
ATOM   1036 C  CB  . LYS B 1 35  ? -25.007 -24.775 21.349  1.00 29.53 ? 35  LYS B CB  1 
ATOM   1037 C  CG  . LYS B 1 35  ? -25.855 -24.939 20.108  1.00 38.11 ? 35  LYS B CG  1 
ATOM   1038 C  CD  . LYS B 1 35  ? -25.163 -25.810 19.056  1.00 39.42 ? 35  LYS B CD  1 
ATOM   1039 N  N   . ALA B 1 36  ? -27.988 -23.895 22.782  1.00 38.28 ? 36  ALA B N   1 
ATOM   1040 C  CA  . ALA B 1 36  ? -29.263 -24.293 23.396  1.00 39.68 ? 36  ALA B CA  1 
ATOM   1041 C  C   . ALA B 1 36  ? -29.807 -25.545 22.721  1.00 41.34 ? 36  ALA B C   1 
ATOM   1042 O  O   . ALA B 1 36  ? -29.766 -25.605 21.506  1.00 36.80 ? 36  ALA B O   1 
ATOM   1043 N  N   . TRP B 1 41  ? -27.289 -19.627 20.647  1.00 55.75 ? 41  TRP B N   1 
ATOM   1044 C  CA  . TRP B 1 41  ? -26.277 -19.282 21.666  1.00 40.49 ? 41  TRP B CA  1 
ATOM   1045 C  C   . TRP B 1 41  ? -26.872 -18.646 22.893  1.00 46.49 ? 41  TRP B C   1 
ATOM   1046 O  O   . TRP B 1 41  ? -27.373 -17.533 22.827  1.00 52.18 ? 41  TRP B O   1 
ATOM   1047 C  CB  . TRP B 1 41  ? -25.250 -18.308 21.096  1.00 43.63 ? 41  TRP B CB  1 
ATOM   1048 C  CG  . TRP B 1 41  ? -24.396 -18.937 20.056  1.00 37.48 ? 41  TRP B CG  1 
ATOM   1049 C  CD1 . TRP B 1 41  ? -24.269 -18.559 18.730  1.00 41.82 ? 41  TRP B CD1 1 
ATOM   1050 C  CD2 . TRP B 1 41  ? -23.562 -20.153 20.189  1.00 42.03 ? 41  TRP B CD2 1 
ATOM   1051 N  NE1 . TRP B 1 41  ? -23.404 -19.390 18.087  1.00 40.68 ? 41  TRP B NE1 1 
ATOM   1052 C  CE2 . TRP B 1 41  ? -22.952 -20.363 18.885  1.00 40.80 ? 41  TRP B CE2 1 
ATOM   1053 C  CE3 . TRP B 1 41  ? -23.242 -21.029 21.233  1.00 34.97 ? 41  TRP B CE3 1 
ATOM   1054 C  CZ2 . TRP B 1 41  ? -22.075 -21.415 18.637  1.00 41.60 ? 41  TRP B CZ2 1 
ATOM   1055 C  CZ3 . TRP B 1 41  ? -22.324 -22.068 20.983  1.00 26.29 ? 41  TRP B CZ3 1 
ATOM   1056 C  CH2 . TRP B 1 41  ? -21.799 -22.284 19.713  1.00 35.60 ? 41  TRP B CH2 1 
ATOM   1057 N  N   . GLU B 1 42  ? -26.818 -19.354 24.011  1.00 37.33 ? 42  GLU B N   1 
ATOM   1058 C  CA  . GLU B 1 42  ? -27.221 -18.842 25.289  1.00 34.44 ? 42  GLU B CA  1 
ATOM   1059 C  C   . GLU B 1 42  ? -25.979 -18.230 25.967  1.00 39.29 ? 42  GLU B C   1 
ATOM   1060 O  O   . GLU B 1 42  ? -24.948 -18.903 26.125  1.00 34.14 ? 42  GLU B O   1 
ATOM   1061 C  CB  . GLU B 1 42  ? -27.799 -19.990 26.118  1.00 38.43 ? 42  GLU B CB  1 
ATOM   1062 N  N   . PRO B 1 43  ? -26.054 -16.944 26.375  1.00 43.09 ? 43  PRO B N   1 
ATOM   1063 C  CA  . PRO B 1 43  ? -24.898 -16.508 27.172  1.00 35.43 ? 43  PRO B CA  1 
ATOM   1064 C  C   . PRO B 1 43  ? -24.751 -17.396 28.370  1.00 29.54 ? 43  PRO B C   1 
ATOM   1065 O  O   . PRO B 1 43  ? -25.760 -17.791 29.016  1.00 38.49 ? 43  PRO B O   1 
ATOM   1066 C  CB  . PRO B 1 43  ? -25.253 -15.069 27.580  1.00 33.45 ? 43  PRO B CB  1 
ATOM   1067 C  CG  . PRO B 1 43  ? -26.208 -14.623 26.517  1.00 36.17 ? 43  PRO B CG  1 
ATOM   1068 C  CD  . PRO B 1 43  ? -27.034 -15.852 26.202  1.00 35.75 ? 43  PRO B CD  1 
ATOM   1069 N  N   . PHE B 1 44  ? -23.495 -17.710 28.673  1.00 27.29 ? 44  PHE B N   1 
ATOM   1070 C  CA  . PHE B 1 44  ? -23.159 -18.684 29.708  1.00 24.99 ? 44  PHE B CA  1 
ATOM   1071 C  C   . PHE B 1 44  ? -22.226 -18.084 30.789  1.00 27.52 ? 44  PHE B C   1 
ATOM   1072 O  O   . PHE B 1 44  ? -22.479 -18.280 31.986  1.00 27.81 ? 44  PHE B O   1 
ATOM   1073 C  CB  . PHE B 1 44  ? -22.515 -19.908 29.053  1.00 21.26 ? 44  PHE B CB  1 
ATOM   1074 C  CG  . PHE B 1 44  ? -21.976 -20.926 30.052  1.00 24.22 ? 44  PHE B CG  1 
ATOM   1075 C  CD1 . PHE B 1 44  ? -22.807 -21.892 30.630  1.00 29.14 ? 44  PHE B CD1 1 
ATOM   1076 C  CD2 . PHE B 1 44  ? -20.627 -20.936 30.379  1.00 22.00 ? 44  PHE B CD2 1 
ATOM   1077 C  CE1 . PHE B 1 44  ? -22.293 -22.848 31.488  1.00 24.84 ? 44  PHE B CE1 1 
ATOM   1078 C  CE2 . PHE B 1 44  ? -20.142 -21.839 31.301  1.00 22.63 ? 44  PHE B CE2 1 
ATOM   1079 C  CZ  . PHE B 1 44  ? -20.960 -22.778 31.847  1.00 24.23 ? 44  PHE B CZ  1 
ATOM   1080 N  N   . ALA B 1 45  ? -21.221 -17.305 30.396  1.00 19.76 ? 45  ALA B N   1 
ATOM   1081 C  CA  . ALA B 1 45  ? -20.251 -16.757 31.375  1.00 20.80 ? 45  ALA B CA  1 
ATOM   1082 C  C   . ALA B 1 45  ? -19.505 -15.659 30.682  1.00 21.35 ? 45  ALA B C   1 
ATOM   1083 O  O   . ALA B 1 45  ? -19.447 -15.659 29.482  1.00 22.94 ? 45  ALA B O   1 
ATOM   1084 C  CB  . ALA B 1 45  ? -19.264 -17.809 31.875  1.00 20.69 ? 45  ALA B CB  1 
ATOM   1085 N  N   . SER B 1 46  ? -18.975 -14.714 31.441  1.00 20.00 ? 46  SER B N   1 
ATOM   1086 C  CA  . SER B 1 46  ? -18.110 -13.705 30.835  1.00 16.74 ? 46  SER B CA  1 
ATOM   1087 C  C   . SER B 1 46  ? -17.254 -13.015 31.882  1.00 16.99 ? 46  SER B C   1 
ATOM   1088 O  O   . SER B 1 46  ? -17.487 -13.158 33.067  1.00 19.39 ? 46  SER B O   1 
ATOM   1089 C  CB  . SER B 1 46  ? -18.944 -12.696 29.998  1.00 19.03 ? 46  SER B CB  1 
ATOM   1090 O  OG  . SER B 1 46  ? -19.982 -12.148 30.742  1.00 20.75 ? 46  SER B OG  1 
ATOM   1091 N  N   . GLY B 1 47  ? -16.294 -12.226 31.433  1.00 17.18 ? 47  GLY B N   1 
ATOM   1092 C  CA  . GLY B 1 47  ? -15.465 -11.478 32.326  1.00 15.79 ? 47  GLY B CA  1 
ATOM   1093 C  C   . GLY B 1 47  ? -14.474 -10.614 31.533  1.00 14.55 ? 47  GLY B C   1 
ATOM   1094 O  O   . GLY B 1 47  ? -14.520 -10.660 30.279  1.00 18.80 ? 47  GLY B O   1 
ATOM   1095 N  N   . LYS B 1 48  ? -13.485 -10.060 32.227  1.00 19.25 ? 48  LYS B N   1 
ATOM   1096 C  CA  . LYS B 1 48  ? -12.371 -9.353  31.619  1.00 22.27 ? 48  LYS B CA  1 
ATOM   1097 C  C   . LYS B 1 48  ? -11.068 -10.006 32.146  1.00 17.49 ? 48  LYS B C   1 
ATOM   1098 O  O   . LYS B 1 48  ? -10.961 -10.394 33.333  1.00 18.54 ? 48  LYS B O   1 
ATOM   1099 C  CB  . LYS B 1 48  ? -12.432 -7.808  31.911  1.00 21.83 ? 48  LYS B CB  1 
ATOM   1100 C  CG  . LYS B 1 48  ? -13.603 -7.139  31.190  1.00 23.79 ? 48  LYS B CG  1 
ATOM   1101 C  CD  . LYS B 1 48  ? -13.555 -5.645  30.852  1.00 37.79 ? 48  LYS B CD  1 
ATOM   1102 C  CE  . LYS B 1 48  ? -14.999 -5.236  30.501  1.00 35.43 ? 48  LYS B CE  1 
ATOM   1103 N  NZ  . LYS B 1 48  ? -15.194 -3.863  29.972  1.00 46.55 ? 48  LYS B NZ  1 
ATOM   1104 N  N   . THR B 1 49  ? -10.081 -10.159 31.276  1.00 10.08 ? 49  THR B N   1 
ATOM   1105 C  CA  . THR B 1 49  ? -8.775  -10.534 31.630  1.00 13.30 ? 49  THR B CA  1 
ATOM   1106 C  C   . THR B 1 49  ? -8.118  -9.664  32.692  1.00 15.11 ? 49  THR B C   1 
ATOM   1107 O  O   . THR B 1 49  ? -8.241  -8.459  32.662  1.00 18.57 ? 49  THR B O   1 
ATOM   1108 C  CB  . THR B 1 49  ? -7.840  -10.830 30.447  1.00 14.17 ? 49  THR B CB  1 
ATOM   1109 O  OG1 . THR B 1 49  ? -7.612  -9.618  29.760  1.00 16.87 ? 49  THR B OG1 1 
ATOM   1110 C  CG2 . THR B 1 49  ? -8.420  -11.949 29.463  1.00 16.57 ? 49  THR B CG2 1 
ATOM   1111 N  N   . SER B 1 50  ? -7.398  -10.315 33.585  1.00 17.01 ? 50  SER B N   1 
ATOM   1112 C  CA  . SER B 1 50  ? -6.600  -9.671  34.645  1.00 19.52 ? 50  SER B CA  1 
ATOM   1113 C  C   . SER B 1 50  ? -5.256  -9.193  34.131  1.00 23.79 ? 50  SER B C   1 
ATOM   1114 O  O   . SER B 1 50  ? -4.924  -9.348  32.961  1.00 20.82 ? 50  SER B O   1 
ATOM   1115 C  CB  . SER B 1 50  ? -6.326  -10.676 35.761  1.00 23.17 ? 50  SER B CB  1 
ATOM   1116 O  OG  . SER B 1 50  ? -5.377  -11.625 35.271  1.00 24.80 ? 50  SER B OG  1 
ATOM   1117 N  N   . GLU B 1 51  ? -4.436  -8.746  35.043  1.00 23.56 ? 51  GLU B N   1 
ATOM   1118 C  CA  . GLU B 1 51  ? -3.084  -8.205  34.745  1.00 23.33 ? 51  GLU B CA  1 
ATOM   1119 C  C   . GLU B 1 51  ? -2.174  -9.303  34.191  1.00 27.37 ? 51  GLU B C   1 
ATOM   1120 O  O   . GLU B 1 51  ? -1.191  -9.043  33.491  1.00 28.80 ? 51  GLU B O   1 
ATOM   1121 C  CB  . GLU B 1 51  ? -2.515  -7.563  36.039  1.00 27.36 ? 51  GLU B CB  1 
ATOM   1122 N  N   . SER B 1 52  ? -2.521  -10.559 34.482  1.00 22.33 ? 52  SER B N   1 
ATOM   1123 C  CA  . SER B 1 52  ? -1.745  -11.696 33.988  1.00 27.82 ? 52  SER B CA  1 
ATOM   1124 C  C   . SER B 1 52  ? -2.280  -12.216 32.680  1.00 24.18 ? 52  SER B C   1 
ATOM   1125 O  O   . SER B 1 52  ? -1.806  -13.185 32.174  1.00 24.34 ? 52  SER B O   1 
ATOM   1126 C  CB  . SER B 1 52  ? -1.809  -12.829 35.014  1.00 32.73 ? 52  SER B CB  1 
ATOM   1127 O  OG  . SER B 1 52  ? -3.130  -13.349 35.128  1.00 35.34 ? 52  SER B OG  1 
ATOM   1128 N  N   . GLY B 1 53  ? -3.325  -11.598 32.148  1.00 19.25 ? 53  GLY B N   1 
ATOM   1129 C  CA  . GLY B 1 53  ? -3.964  -12.108 30.890  1.00 17.75 ? 53  GLY B CA  1 
ATOM   1130 C  C   . GLY B 1 53  ? -4.928  -13.244 31.120  1.00 17.60 ? 53  GLY B C   1 
ATOM   1131 O  O   . GLY B 1 53  ? -5.424  -13.828 30.192  1.00 19.93 ? 53  GLY B O   1 
ATOM   1132 N  N   . GLU B 1 54  ? -5.215  -13.545 32.379  1.00 18.58 ? 54  GLU B N   1 
ATOM   1133 C  CA  . GLU B 1 54  ? -6.013  -14.710 32.691  1.00 20.43 ? 54  GLU B CA  1 
ATOM   1134 C  C   . GLU B 1 54  ? -7.361  -14.284 33.252  1.00 20.15 ? 54  GLU B C   1 
ATOM   1135 O  O   . GLU B 1 54  ? -7.522  -13.211 33.843  1.00 21.48 ? 54  GLU B O   1 
ATOM   1136 C  CB  . GLU B 1 54  ? -5.309  -15.622 33.696  1.00 23.16 ? 54  GLU B CB  1 
ATOM   1137 C  CG  . GLU B 1 54  ? -3.982  -16.230 33.218  0.50 26.10 ? 54  GLU B CG  1 
ATOM   1138 C  CD  . GLU B 1 54  ? -3.188  -16.980 34.298  0.50 32.39 ? 54  GLU B CD  1 
ATOM   1139 O  OE1 . GLU B 1 54  ? -3.641  -17.095 35.432  0.50 30.68 ? 54  GLU B OE1 1 
ATOM   1140 O  OE2 . GLU B 1 54  ? -2.068  -17.388 33.972  0.50 56.83 ? 54  GLU B OE2 1 
ATOM   1141 N  N   . LEU B 1 55  ? -8.364  -15.098 32.967  1.00 18.51 ? 55  LEU B N   1 
ATOM   1142 C  CA  . LEU B 1 55  ? -9.684  -14.894 33.474  1.00 20.49 ? 55  LEU B CA  1 
ATOM   1143 C  C   . LEU B 1 55  ? -10.134 -16.208 34.111  1.00 21.62 ? 55  LEU B C   1 
ATOM   1144 O  O   . LEU B 1 55  ? -10.278 -17.229 33.450  1.00 19.17 ? 55  LEU B O   1 
ATOM   1145 C  CB  . LEU B 1 55  ? -10.579 -14.488 32.326  1.00 19.59 ? 55  LEU B CB  1 
ATOM   1146 C  CG  . LEU B 1 55  ? -12.077 -14.423 32.639  1.00 22.19 ? 55  LEU B CG  1 
ATOM   1147 C  CD1 . LEU B 1 55  ? -12.369 -13.504 33.839  1.00 22.02 ? 55  LEU B CD1 1 
ATOM   1148 C  CD2 . LEU B 1 55  ? -12.864 -14.021 31.399  1.00 24.64 ? 55  LEU B CD2 1 
ATOM   1149 N  N   . HIS B 1 56  ? -10.223 -16.141 35.423  1.00 25.28 ? 56  HIS B N   1 
ATOM   1150 C  CA  . HIS B 1 56  ? -10.616 -17.200 36.303  1.00 25.95 ? 56  HIS B CA  1 
ATOM   1151 C  C   . HIS B 1 56  ? -12.025 -16.914 36.773  1.00 24.26 ? 56  HIS B C   1 
ATOM   1152 O  O   . HIS B 1 56  ? -12.525 -15.811 36.653  1.00 30.69 ? 56  HIS B O   1 
ATOM   1153 C  CB  . HIS B 1 56  ? -9.675  -17.202 37.510  1.00 29.35 ? 56  HIS B CB  1 
ATOM   1154 C  CG  . HIS B 1 56  ? -8.269  -17.587 37.165  1.00 31.14 ? 56  HIS B CG  1 
ATOM   1155 N  ND1 . HIS B 1 56  ? -7.905  -18.880 36.959  1.00 35.27 ? 56  HIS B ND1 1 
ATOM   1156 C  CD2 . HIS B 1 56  ? -7.122  -16.804 36.935  1.00 41.35 ? 56  HIS B CD2 1 
ATOM   1157 C  CE1 . HIS B 1 56  ? -6.592  -18.928 36.618  1.00 36.93 ? 56  HIS B CE1 1 
ATOM   1158 N  NE2 . HIS B 1 56  ? -6.112  -17.655 36.611  1.00 42.29 ? 56  HIS B NE2 1 
ATOM   1159 N  N   . GLY B 1 57  ? -12.661 -17.911 37.368  1.00 33.44 ? 57  GLY B N   1 
ATOM   1160 C  CA  . GLY B 1 57  ? -13.949 -17.686 38.044  1.00 28.87 ? 57  GLY B CA  1 
ATOM   1161 C  C   . GLY B 1 57  ? -15.113 -17.553 37.095  1.00 30.10 ? 57  GLY B C   1 
ATOM   1162 O  O   . GLY B 1 57  ? -16.147 -17.037 37.501  1.00 32.06 ? 57  GLY B O   1 
ATOM   1163 N  N   . LEU B 1 58  ? -14.945 -17.948 35.823  1.00 26.90 ? 58  LEU B N   1 
ATOM   1164 C  CA  . LEU B 1 58  ? -16.020 -17.847 34.821  1.00 24.12 ? 58  LEU B CA  1 
ATOM   1165 C  C   . LEU B 1 58  ? -17.268 -18.644 35.215  1.00 28.91 ? 58  LEU B C   1 
ATOM   1166 O  O   . LEU B 1 58  ? -18.407 -18.178 35.066  1.00 25.69 ? 58  LEU B O   1 
ATOM   1167 C  CB  . LEU B 1 58  ? -15.520 -18.293 33.449  1.00 21.56 ? 58  LEU B CB  1 
ATOM   1168 C  CG  . LEU B 1 58  ? -14.861 -17.220 32.616  1.00 21.44 ? 58  LEU B CG  1 
ATOM   1169 C  CD1 . LEU B 1 58  ? -14.105 -17.878 31.428  1.00 24.54 ? 58  LEU B CD1 1 
ATOM   1170 C  CD2 . LEU B 1 58  ? -15.879 -16.221 32.121  1.00 25.72 ? 58  LEU B CD2 1 
ATOM   1171 N  N   . THR B 1 59  ? -17.037 -19.859 35.680  1.00 27.61 ? 59  THR B N   1 
ATOM   1172 C  CA  . THR B 1 59  ? -18.130 -20.814 35.895  1.00 25.30 ? 59  THR B CA  1 
ATOM   1173 C  C   . THR B 1 59  ? -17.829 -21.730 37.079  1.00 30.27 ? 59  THR B C   1 
ATOM   1174 O  O   . THR B 1 59  ? -16.800 -21.609 37.770  1.00 34.82 ? 59  THR B O   1 
ATOM   1175 C  CB  . THR B 1 59  ? -18.450 -21.586 34.580  1.00 25.87 ? 59  THR B CB  1 
ATOM   1176 O  OG1 . THR B 1 59  ? -19.759 -22.185 34.650  1.00 28.59 ? 59  THR B OG1 1 
ATOM   1177 C  CG2 . THR B 1 59  ? -17.429 -22.717 34.248  1.00 26.47 ? 59  THR B CG2 1 
ATOM   1178 N  N   . THR B 1 60  ? -18.778 -22.616 37.316  1.00 32.62 ? 60  THR B N   1 
ATOM   1179 C  CA  . THR B 1 60  ? -18.672 -23.610 38.356  1.00 28.53 ? 60  THR B CA  1 
ATOM   1180 C  C   . THR B 1 60  ? -18.846 -24.978 37.723  1.00 27.39 ? 60  THR B C   1 
ATOM   1181 O  O   . THR B 1 60  ? -19.383 -25.120 36.617  1.00 28.36 ? 60  THR B O   1 
ATOM   1182 C  CB  . THR B 1 60  ? -19.743 -23.435 39.457  1.00 29.88 ? 60  THR B CB  1 
ATOM   1183 O  OG1 . THR B 1 60  ? -21.063 -23.510 38.879  1.00 33.54 ? 60  THR B OG1 1 
ATOM   1184 C  CG2 . THR B 1 60  ? -19.616 -22.091 40.169  1.00 31.06 ? 60  THR B CG2 1 
ATOM   1185 N  N   . GLU B 1 61  ? -18.376 -25.989 38.432  1.00 32.25 ? 61  GLU B N   1 
ATOM   1186 C  CA  . GLU B 1 61  ? -18.499 -27.347 37.995  1.00 31.16 ? 61  GLU B CA  1 
ATOM   1187 C  C   . GLU B 1 61  ? -19.977 -27.725 37.819  1.00 35.04 ? 61  GLU B C   1 
ATOM   1188 O  O   . GLU B 1 61  ? -20.302 -28.500 36.889  1.00 34.43 ? 61  GLU B O   1 
ATOM   1189 C  CB  . GLU B 1 61  ? -17.767 -28.246 38.998  1.00 32.88 ? 61  GLU B CB  1 
ATOM   1190 N  N   . GLU B 1 62  ? -20.857 -27.153 38.659  1.00 30.05 ? 62  GLU B N   1 
ATOM   1191 C  CA  . GLU B 1 62  ? -22.283 -27.450 38.591  1.00 34.42 ? 62  GLU B CA  1 
ATOM   1192 C  C   . GLU B 1 62  ? -22.837 -26.931 37.270  1.00 30.29 ? 62  GLU B C   1 
ATOM   1193 O  O   . GLU B 1 62  ? -23.584 -27.649 36.577  1.00 34.15 ? 62  GLU B O   1 
ATOM   1194 C  CB  . GLU B 1 62  ? -23.122 -26.885 39.792  1.00 34.08 ? 62  GLU B CB  1 
ATOM   1195 C  CG  . GLU B 1 62  ? -22.493 -27.103 41.180  1.00 32.97 ? 62  GLU B CG  1 
ATOM   1196 C  CD  . GLU B 1 62  ? -21.200 -26.271 41.332  1.00 33.08 ? 62  GLU B CD  1 
ATOM   1197 N  N   . GLU B 1 63  ? -22.443 -25.711 36.890  1.00 30.02 ? 63  GLU B N   1 
ATOM   1198 C  CA  . GLU B 1 63  ? -22.965 -25.086 35.665  1.00 32.41 ? 63  GLU B CA  1 
ATOM   1199 C  C   . GLU B 1 63  ? -22.347 -25.651 34.378  1.00 26.00 ? 63  GLU B C   1 
ATOM   1200 O  O   . GLU B 1 63  ? -22.992 -25.653 33.328  1.00 26.12 ? 63  GLU B O   1 
ATOM   1201 C  CB  . GLU B 1 63  ? -22.776 -23.519 35.691  1.00 32.19 ? 63  GLU B CB  1 
ATOM   1202 C  CG  . GLU B 1 63  ? -23.953 -22.771 36.329  1.00 37.73 ? 63  GLU B CG  1 
ATOM   1203 N  N   . PHE B 1 64  ? -21.102 -26.116 34.447  1.00 28.65 ? 64  PHE B N   1 
ATOM   1204 C  CA  . PHE B 1 64  ? -20.343 -26.378 33.206  1.00 28.84 ? 64  PHE B CA  1 
ATOM   1205 C  C   . PHE B 1 64  ? -20.604 -27.814 32.752  1.00 20.79 ? 64  PHE B C   1 
ATOM   1206 O  O   . PHE B 1 64  ? -19.789 -28.709 32.947  1.00 35.08 ? 64  PHE B O   1 
ATOM   1207 C  CB  . PHE B 1 64  ? -18.845 -26.101 33.420  1.00 25.80 ? 64  PHE B CB  1 
ATOM   1208 C  CG  . PHE B 1 64  ? -18.003 -26.246 32.180  1.00 25.21 ? 64  PHE B CG  1 
ATOM   1209 C  CD1 . PHE B 1 64  ? -18.249 -25.466 31.054  1.00 25.69 ? 64  PHE B CD1 1 
ATOM   1210 C  CD2 . PHE B 1 64  ? -16.983 -27.129 32.153  1.00 28.71 ? 64  PHE B CD2 1 
ATOM   1211 C  CE1 . PHE B 1 64  ? -17.456 -25.566 29.923  1.00 23.84 ? 64  PHE B CE1 1 
ATOM   1212 C  CE2 . PHE B 1 64  ? -16.221 -27.248 31.038  1.00 32.88 ? 64  PHE B CE2 1 
ATOM   1213 C  CZ  . PHE B 1 64  ? -16.444 -26.459 29.936  1.00 29.88 ? 64  PHE B CZ  1 
ATOM   1214 N  N   . VAL B 1 65  ? -21.717 -27.993 32.073  1.00 20.67 ? 65  VAL B N   1 
ATOM   1215 C  CA  . VAL B 1 65  ? -22.121 -29.324 31.697  1.00 24.42 ? 65  VAL B CA  1 
ATOM   1216 C  C   . VAL B 1 65  ? -21.581 -29.618 30.293  1.00 24.83 ? 65  VAL B C   1 
ATOM   1217 O  O   . VAL B 1 65  ? -21.090 -28.740 29.629  1.00 25.97 ? 65  VAL B O   1 
ATOM   1218 C  CB  . VAL B 1 65  ? -23.638 -29.472 31.731  1.00 21.52 ? 65  VAL B CB  1 
ATOM   1219 C  CG1 . VAL B 1 65  ? -24.212 -29.287 33.159  1.00 21.78 ? 65  VAL B CG1 1 
ATOM   1220 C  CG2 . VAL B 1 65  ? -24.311 -28.514 30.790  1.00 24.70 ? 65  VAL B CG2 1 
ATOM   1221 N  N   . GLU B 1 66  ? -21.583 -30.873 29.862  1.00 23.59 ? 66  GLU B N   1 
ATOM   1222 C  CA  . GLU B 1 66  ? -21.173 -31.183 28.532  1.00 23.78 ? 66  GLU B CA  1 
ATOM   1223 C  C   . GLU B 1 66  ? -22.041 -30.384 27.577  1.00 20.17 ? 66  GLU B C   1 
ATOM   1224 O  O   . GLU B 1 66  ? -23.174 -30.058 27.875  1.00 27.74 ? 66  GLU B O   1 
ATOM   1225 C  CB  . GLU B 1 66  ? -21.304 -32.715 28.244  1.00 25.61 ? 66  GLU B CB  1 
ATOM   1226 C  CG  . GLU B 1 66  ? -20.272 -33.527 28.999  1.00 23.34 ? 66  GLU B CG  1 
ATOM   1227 C  CD  . GLU B 1 66  ? -20.392 -35.044 28.767  1.00 28.57 ? 66  GLU B CD  1 
ATOM   1228 O  OE1 . GLU B 1 66  ? -21.543 -35.547 28.501  1.00 28.07 ? 66  GLU B OE1 1 
ATOM   1229 O  OE2 . GLU B 1 66  ? -19.309 -35.691 28.824  1.00 31.39 ? 66  GLU B OE2 1 
ATOM   1230 N  N   . GLY B 1 67  ? -21.466 -30.056 26.420  1.00 24.95 ? 67  GLY B N   1 
ATOM   1231 C  CA  . GLY B 1 67  ? -22.202 -29.439 25.326  1.00 25.25 ? 67  GLY B CA  1 
ATOM   1232 C  C   . GLY B 1 67  ? -21.258 -28.665 24.447  1.00 20.14 ? 67  GLY B C   1 
ATOM   1233 O  O   . GLY B 1 67  ? -20.048 -28.939 24.436  1.00 25.56 ? 67  GLY B O   1 
ATOM   1234 N  N   . ILE B 1 68  ? -21.822 -27.773 23.648  1.00 23.33 ? 68  ILE B N   1 
ATOM   1235 C  CA  . ILE B 1 68  ? -21.048 -27.070 22.664  1.00 23.76 ? 68  ILE B CA  1 
ATOM   1236 C  C   . ILE B 1 68  ? -20.953 -25.640 23.170  1.00 21.87 ? 68  ILE B C   1 
ATOM   1237 O  O   . ILE B 1 68  ? -21.956 -25.005 23.460  1.00 22.95 ? 68  ILE B O   1 
ATOM   1238 C  CB  . ILE B 1 68  ? -21.681 -27.101 21.269  1.00 26.50 ? 68  ILE B CB  1 
ATOM   1239 C  CG1 . ILE B 1 68  ? -21.904 -28.529 20.797  1.00 27.53 ? 68  ILE B CG1 1 
ATOM   1240 C  CG2 . ILE B 1 68  ? -20.764 -26.391 20.294  1.00 28.96 ? 68  ILE B CG2 1 
ATOM   1241 C  CD1 . ILE B 1 68  ? -22.499 -28.626 19.391  1.00 28.32 ? 68  ILE B CD1 1 
ATOM   1242 N  N   . TYR B 1 69  ? -19.728 -25.178 23.314  1.00 21.90 ? 69  TYR B N   1 
ATOM   1243 C  CA  . TYR B 1 69  ? -19.423 -23.825 23.856  1.00 17.72 ? 69  TYR B CA  1 
ATOM   1244 C  C   . TYR B 1 69  ? -18.734 -22.962 22.781  1.00 19.06 ? 69  TYR B C   1 
ATOM   1245 O  O   . TYR B 1 69  ? -17.962 -23.481 21.993  1.00 22.29 ? 69  TYR B O   1 
ATOM   1246 C  CB  . TYR B 1 69  ? -18.562 -23.948 25.108  1.00 17.49 ? 69  TYR B CB  1 
ATOM   1247 C  CG  . TYR B 1 69  ? -19.329 -24.543 26.263  1.00 20.10 ? 69  TYR B CG  1 
ATOM   1248 C  CD1 . TYR B 1 69  ? -19.488 -25.917 26.384  1.00 20.57 ? 69  TYR B CD1 1 
ATOM   1249 C  CD2 . TYR B 1 69  ? -19.929 -23.710 27.200  1.00 18.51 ? 69  TYR B CD2 1 
ATOM   1250 C  CE1 . TYR B 1 69  ? -20.181 -26.435 27.469  1.00 20.23 ? 69  TYR B CE1 1 
ATOM   1251 C  CE2 . TYR B 1 69  ? -20.623 -24.209 28.272  1.00 22.69 ? 69  TYR B CE2 1 
ATOM   1252 C  CZ  . TYR B 1 69  ? -20.773 -25.582 28.376  1.00 18.16 ? 69  TYR B CZ  1 
ATOM   1253 O  OH  . TYR B 1 69  ? -21.485 -26.072 29.450  1.00 20.87 ? 69  TYR B OH  1 
ATOM   1254 N  N   . LYS B 1 70  ? -19.017 -21.657 22.811  1.00 22.99 ? 70  LYS B N   1 
ATOM   1255 C  CA  . LYS B 1 70  ? -18.255 -20.635 22.062  1.00 26.04 ? 70  LYS B CA  1 
ATOM   1256 C  C   . LYS B 1 70  ? -17.601 -19.681 23.063  1.00 22.83 ? 70  LYS B C   1 
ATOM   1257 O  O   . LYS B 1 70  ? -18.261 -19.130 23.926  1.00 23.28 ? 70  LYS B O   1 
ATOM   1258 C  CB  . LYS B 1 70  ? -19.227 -19.869 21.177  1.00 26.73 ? 70  LYS B CB  1 
ATOM   1259 C  CG  . LYS B 1 70  ? -18.665 -18.651 20.582  1.00 27.50 ? 70  LYS B CG  1 
ATOM   1260 C  CD  . LYS B 1 70  ? -19.360 -18.201 19.361  1.00 25.97 ? 70  LYS B CD  1 
ATOM   1261 C  CE  . LYS B 1 70  ? -20.710 -17.560 19.548  1.00 31.71 ? 70  LYS B CE  1 
ATOM   1262 N  NZ  . LYS B 1 70  ? -20.717 -16.505 18.517  1.00 40.34 ? 70  LYS B NZ  1 
ATOM   1263 N  N   . VAL B 1 71  ? -16.293 -19.517 22.956  1.00 20.74 ? 71  VAL B N   1 
ATOM   1264 C  CA  . VAL B 1 71  ? -15.598 -18.497 23.698  1.00 22.82 ? 71  VAL B CA  1 
ATOM   1265 C  C   . VAL B 1 71  ? -15.258 -17.391 22.686  1.00 20.95 ? 71  VAL B C   1 
ATOM   1266 O  O   . VAL B 1 71  ? -14.572 -17.653 21.673  1.00 23.73 ? 71  VAL B O   1 
ATOM   1267 C  CB  . VAL B 1 71  ? -14.324 -19.042 24.351  1.00 19.33 ? 71  VAL B CB  1 
ATOM   1268 C  CG1 . VAL B 1 71  ? -13.515 -17.908 24.981  1.00 22.12 ? 71  VAL B CG1 1 
ATOM   1269 C  CG2 . VAL B 1 71  ? -14.620 -20.138 25.408  1.00 22.28 ? 71  VAL B CG2 1 
ATOM   1270 N  N   . GLU B 1 72  ? -15.785 -16.198 22.924  1.00 22.75 ? 72  GLU B N   1 
ATOM   1271 C  CA  . GLU B 1 72  ? -15.599 -15.029 22.034  1.00 22.47 ? 72  GLU B CA  1 
ATOM   1272 C  C   . GLU B 1 72  ? -14.797 -13.986 22.767  1.00 19.51 ? 72  GLU B C   1 
ATOM   1273 O  O   . GLU B 1 72  ? -15.239 -13.477 23.795  1.00 20.56 ? 72  GLU B O   1 
ATOM   1274 C  CB  . GLU B 1 72  ? -16.923 -14.403 21.687  1.00 30.73 ? 72  GLU B CB  1 
ATOM   1275 C  CG  . GLU B 1 72  ? -16.838 -13.291 20.679  1.00 31.60 ? 72  GLU B CG  1 
ATOM   1276 C  CD  . GLU B 1 72  ? -18.164 -12.618 20.441  1.00 32.04 ? 72  GLU B CD  1 
ATOM   1277 O  OE1 . GLU B 1 72  ? -19.057 -13.358 20.074  1.00 47.05 ? 72  GLU B OE1 1 
ATOM   1278 N  N   . ILE B 1 73  ? -13.648 -13.660 22.233  1.00 17.68 ? 73  ILE B N   1 
ATOM   1279 C  CA  . ILE B 1 73  ? -12.699 -12.744 22.855  1.00 14.38 ? 73  ILE B CA  1 
ATOM   1280 C  C   . ILE B 1 73  ? -12.723 -11.462 22.051  1.00 16.08 ? 73  ILE B C   1 
ATOM   1281 O  O   . ILE B 1 73  ? -12.500 -11.465 20.846  1.00 17.02 ? 73  ILE B O   1 
ATOM   1282 C  CB  . ILE B 1 73  ? -11.286 -13.310 22.857  1.00 17.15 ? 73  ILE B CB  1 
ATOM   1283 C  CG1 . ILE B 1 73  ? -11.325 -14.714 23.474  1.00 19.36 ? 73  ILE B CG1 1 
ATOM   1284 C  CG2 . ILE B 1 73  ? -10.319 -12.397 23.614  1.00 18.47 ? 73  ILE B CG2 1 
ATOM   1285 C  CD1 . ILE B 1 73  ? -10.069 -15.494 23.349  1.00 19.51 ? 73  ILE B CD1 1 
ATOM   1286 N  N   . ASP B 1 74  ? -12.985 -10.369 22.734  1.00 13.95 ? 74  ASP B N   1 
ATOM   1287 C  CA  . ASP B 1 74  ? -13.127 -9.056  22.093  1.00 13.53 ? 74  ASP B CA  1 
ATOM   1288 C  C   . ASP B 1 74  ? -11.783 -8.420  21.760  1.00 15.21 ? 74  ASP B C   1 
ATOM   1289 O  O   . ASP B 1 74  ? -11.339 -7.455  22.388  1.00 15.94 ? 74  ASP B O   1 
ATOM   1290 C  CB  . ASP B 1 74  ? -14.013 -8.122  22.879  1.00 16.24 ? 74  ASP B CB  1 
ATOM   1291 C  CG  . ASP B 1 74  ? -14.288 -6.826  22.112  1.00 19.35 ? 74  ASP B CG  1 
ATOM   1292 O  OD1 . ASP B 1 74  ? -13.848 -6.704  20.914  1.00 17.26 ? 74  ASP B OD1 1 
ATOM   1293 O  OD2 . ASP B 1 74  ? -14.891 -5.922  22.730  1.00 24.80 ? 74  ASP B OD2 1 
ATOM   1294 N  N   . THR B 1 75  ? -11.124 -9.025  20.786  1.00 13.46 ? 75  THR B N   1 
ATOM   1295 C  CA  . THR B 1 75  ? -9.852  -8.595  20.345  1.00 10.71 ? 75  THR B CA  1 
ATOM   1296 C  C   . THR B 1 75  ? -9.871  -7.220  19.692  1.00 13.40 ? 75  THR B C   1 
ATOM   1297 O  O   . THR B 1 75  ? -8.892  -6.485  19.768  1.00 13.39 ? 75  THR B O   1 
ATOM   1298 C  CB  . THR B 1 75  ? -9.214  -9.638  19.431  1.00 12.88 ? 75  THR B CB  1 
ATOM   1299 O  OG1 . THR B 1 75  ? -10.003 -9.854  18.291  1.00 14.31 ? 75  THR B OG1 1 
ATOM   1300 C  CG2 . THR B 1 75  ? -9.066  -11.009 20.147  1.00 14.96 ? 75  THR B CG2 1 
ATOM   1301 N  N   . LYS B 1 76  ? -10.927 -6.928  18.964  1.00 11.36 ? 76  LYS B N   1 
ATOM   1302 C  CA  . LYS B 1 76  ? -11.026 -5.634  18.280  1.00 12.14 ? 76  LYS B CA  1 
ATOM   1303 C  C   . LYS B 1 76  ? -10.891 -4.455  19.280  1.00 11.23 ? 76  LYS B C   1 
ATOM   1304 O  O   . LYS B 1 76  ? -10.144 -3.488  19.022  1.00 12.87 ? 76  LYS B O   1 
ATOM   1305 C  CB  . LYS B 1 76  ? -12.327 -5.533  17.475  1.00 16.62 ? 76  LYS B CB  1 
ATOM   1306 C  CG  . LYS B 1 76  ? -12.364 -4.325  16.583  1.00 20.54 ? 76  LYS B CG  1 
ATOM   1307 C  CD  . LYS B 1 76  ? -13.642 -4.335  15.803  1.00 24.31 ? 76  LYS B CD  1 
ATOM   1308 C  CE  . LYS B 1 76  ? -13.512 -3.339  14.637  1.00 36.22 ? 76  LYS B CE  1 
ATOM   1309 N  NZ  . LYS B 1 76  ? -14.726 -3.150  13.793  1.00 33.79 ? 76  LYS B NZ  1 
ATOM   1310 N  N   . SER B 1 77  ? -11.635 -4.504  20.383  1.00 13.25 ? 77  SER B N   1 
ATOM   1311 C  CA  . SER B 1 77  ? -11.527 -3.484  21.389  1.00 14.32 ? 77  SER B CA  1 
ATOM   1312 C  C   . SER B 1 77  ? -10.133 -3.402  21.991  1.00 14.13 ? 77  SER B C   1 
ATOM   1313 O  O   . SER B 1 77  ? -9.666  -2.299  22.371  1.00 14.81 ? 77  SER B O   1 
ATOM   1314 C  CB  . SER B 1 77  ? -12.540 -3.684  22.501  1.00 16.99 ? 77  SER B CB  1 
ATOM   1315 O  OG  . SER B 1 77  ? -13.842 -3.490  22.004  1.00 22.20 ? 77  SER B OG  1 
ATOM   1316 N  N   . TYR B 1 78  ? -9.478  -4.545  22.125  1.00 14.71 ? 78  TYR B N   1 
ATOM   1317 C  CA  . TYR B 1 78  ? -8.145  -4.573  22.675  1.00 15.44 ? 78  TYR B CA  1 
ATOM   1318 C  C   . TYR B 1 78  ? -7.156  -3.797  21.796  1.00 14.36 ? 78  TYR B C   1 
ATOM   1319 O  O   . TYR B 1 78  ? -6.434  -2.916  22.259  1.00 15.56 ? 78  TYR B O   1 
ATOM   1320 C  CB  . TYR B 1 78  ? -7.710  -6.046  22.834  1.00 15.88 ? 78  TYR B CB  1 
ATOM   1321 C  CG  . TYR B 1 78  ? -6.297  -6.198  23.327  1.00 12.34 ? 78  TYR B CG  1 
ATOM   1322 C  CD1 . TYR B 1 78  ? -5.953  -5.927  24.635  1.00 15.86 ? 78  TYR B CD1 1 
ATOM   1323 C  CD2 . TYR B 1 78  ? -5.285  -6.556  22.449  1.00 12.33 ? 78  TYR B CD2 1 
ATOM   1324 C  CE1 . TYR B 1 78  ? -4.648  -6.062  25.051  1.00 16.78 ? 78  TYR B CE1 1 
ATOM   1325 C  CE2 . TYR B 1 78  ? -3.967  -6.705  22.857  1.00 15.48 ? 78  TYR B CE2 1 
ATOM   1326 C  CZ  . TYR B 1 78  ? -3.644  -6.433  24.153  1.00 17.26 ? 78  TYR B CZ  1 
ATOM   1327 O  OH  . TYR B 1 78  ? -2.375  -6.524  24.603  1.00 18.30 ? 78  TYR B OH  1 
ATOM   1328 N  N   . TRP B 1 79  ? -7.109  -4.154  20.508  1.00 12.37 ? 79  TRP B N   1 
ATOM   1329 C  CA  . TRP B 1 79  ? -6.179  -3.502  19.594  1.00 12.08 ? 79  TRP B CA  1 
ATOM   1330 C  C   . TRP B 1 79  ? -6.493  -2.017  19.477  1.00 12.54 ? 79  TRP B C   1 
ATOM   1331 O  O   . TRP B 1 79  ? -5.544  -1.173  19.369  1.00 14.93 ? 79  TRP B O   1 
ATOM   1332 C  CB  . TRP B 1 79  ? -6.173  -4.168  18.240  1.00 11.77 ? 79  TRP B CB  1 
ATOM   1333 C  CG  . TRP B 1 79  ? -5.595  -5.556  18.278  1.00 11.21 ? 79  TRP B CG  1 
ATOM   1334 C  CD1 . TRP B 1 79  ? -6.251  -6.753  18.002  1.00 12.32 ? 79  TRP B CD1 1 
ATOM   1335 C  CD2 . TRP B 1 79  ? -4.235  -5.930  18.632  1.00 11.30 ? 79  TRP B CD2 1 
ATOM   1336 N  NE1 . TRP B 1 79  ? -5.384  -7.826  18.126  1.00 11.72 ? 79  TRP B NE1 1 
ATOM   1337 C  CE2 . TRP B 1 79  ? -4.147  -7.381  18.499  1.00 12.20 ? 79  TRP B CE2 1 
ATOM   1338 C  CE3 . TRP B 1 79  ? -3.087  -5.227  18.985  1.00 13.66 ? 79  TRP B CE3 1 
ATOM   1339 C  CZ2 . TRP B 1 79  ? -2.963  -8.069  18.806  1.00 11.29 ? 79  TRP B CZ2 1 
ATOM   1340 C  CZ3 . TRP B 1 79  ? -1.940  -5.946  19.313  1.00 15.24 ? 79  TRP B CZ3 1 
ATOM   1341 C  CH2 . TRP B 1 79  ? -1.882  -7.342  19.170  1.00 13.32 ? 79  TRP B CH2 1 
ATOM   1342 N  N   . LYS B 1 80  ? -7.794  -1.681  19.424  1.00 13.32 ? 80  LYS B N   1 
ATOM   1343 C  CA  . LYS B 1 80  ? -8.159  -0.295  19.201  1.00 16.29 ? 80  LYS B CA  1 
ATOM   1344 C  C   . LYS B 1 80  ? -7.682  0.572   20.365  1.00 14.65 ? 80  LYS B C   1 
ATOM   1345 O  O   . LYS B 1 80  ? -7.229  1.669   20.158  1.00 17.92 ? 80  LYS B O   1 
ATOM   1346 C  CB  . LYS B 1 80  ? -9.651  -0.154  18.953  1.00 18.11 ? 80  LYS B CB  1 
ATOM   1347 C  CG  . LYS B 1 80  ? -9.977  -0.634  17.557  1.00 24.34 ? 80  LYS B CG  1 
ATOM   1348 C  CD  . LYS B 1 80  ? -11.406 -0.347  17.083  1.00 29.34 ? 80  LYS B CD  1 
ATOM   1349 C  CE  . LYS B 1 80  ? -12.429 -0.358  18.196  1.00 32.69 ? 80  LYS B CE  1 
ATOM   1350 N  N   . ALA B 1 81  ? -7.696  0.038   21.568  1.00 16.10 ? 81  ALA B N   1 
ATOM   1351 C  CA  . ALA B 1 81  ? -7.223  0.771   22.733  1.00 18.13 ? 81  ALA B CA  1 
ATOM   1352 C  C   . ALA B 1 81  ? -5.736  1.022   22.678  1.00 18.85 ? 81  ALA B C   1 
ATOM   1353 O  O   . ALA B 1 81  ? -5.235  1.970   23.294  1.00 18.60 ? 81  ALA B O   1 
ATOM   1354 C  CB  . ALA B 1 81  ? -7.537  -0.000  24.013  1.00 21.11 ? 81  ALA B CB  1 
ATOM   1355 N  N   . LEU B 1 82  ? -5.018  0.147   21.993  1.00 19.42 ? 82  LEU B N   1 
ATOM   1356 C  CA  . LEU B 1 82  ? -3.591  0.306   21.848  1.00 20.70 ? 82  LEU B CA  1 
ATOM   1357 C  C   . LEU B 1 82  ? -3.202  1.201   20.661  1.00 20.83 ? 82  LEU B C   1 
ATOM   1358 O  O   . LEU B 1 82  ? -2.025  1.426   20.428  1.00 23.37 ? 82  LEU B O   1 
ATOM   1359 C  CB  . LEU B 1 82  ? -2.995  -1.061  21.574  1.00 21.13 ? 82  LEU B CB  1 
ATOM   1360 C  CG  . LEU B 1 82  ? -2.700  -1.971  22.729  1.00 23.55 ? 82  LEU B CG  1 
ATOM   1361 C  CD1 . LEU B 1 82  ? -3.778  -2.207  23.757  1.00 31.78 ? 82  LEU B CD1 1 
ATOM   1362 C  CD2 . LEU B 1 82  ? -2.129  -3.284  22.159  1.00 23.57 ? 82  LEU B CD2 1 
ATOM   1363 N  N   . GLY B 1 83  ? -4.163  1.599   19.851  1.00 16.40 ? 83  GLY B N   1 
ATOM   1364 C  CA  . GLY B 1 83  ? -3.897  2.397   18.712  1.00 20.86 ? 83  GLY B CA  1 
ATOM   1365 C  C   . GLY B 1 83  ? -3.523  1.620   17.486  1.00 17.91 ? 83  GLY B C   1 
ATOM   1366 O  O   . GLY B 1 83  ? -2.962  2.197   16.526  1.00 17.97 ? 83  GLY B O   1 
ATOM   1367 N  N   . ILE B 1 84  ? -3.866  0.326   17.455  1.00 15.76 ? 84  ILE B N   1 
ATOM   1368 C  CA  . ILE B 1 84  ? -3.513  -0.547  16.328  1.00 15.32 ? 84  ILE B CA  1 
ATOM   1369 C  C   . ILE B 1 84  ? -4.773  -0.992  15.633  1.00 14.07 ? 84  ILE B C   1 
ATOM   1370 O  O   . ILE B 1 84  ? -5.726  -1.451  16.292  1.00 16.48 ? 84  ILE B O   1 
ATOM   1371 C  CB  . ILE B 1 84  ? -2.743  -1.755  16.860  1.00 16.71 ? 84  ILE B CB  1 
ATOM   1372 C  CG1 . ILE B 1 84  ? -1.415  -1.295  17.449  1.00 17.28 ? 84  ILE B CG1 1 
ATOM   1373 C  CG2 . ILE B 1 84  ? -2.502  -2.825  15.776  1.00 16.11 ? 84  ILE B CG2 1 
ATOM   1374 C  CD1 . ILE B 1 84  ? -0.688  -2.330  18.298  1.00 20.92 ? 84  ILE B CD1 1 
ATOM   1375 N  N   . SER B 1 85  ? -4.797  -0.845  14.313  1.00 15.28 ? 85  SER B N   1 
ATOM   1376 C  CA  . SER B 1 85  ? -5.935  -1.306  13.535  1.00 16.76 ? 85  SER B CA  1 
ATOM   1377 C  C   . SER B 1 85  ? -5.950  -2.835  13.354  1.00 15.44 ? 85  SER B C   1 
ATOM   1378 O  O   . SER B 1 85  ? -4.998  -3.400  12.824  1.00 17.18 ? 85  SER B O   1 
ATOM   1379 C  CB  . SER B 1 85  ? -5.887  -0.645  12.185  1.00 21.72 ? 85  SER B CB  1 
ATOM   1380 O  OG  . SER B 1 85  ? -6.928  -1.156  11.422  1.00 24.77 ? 85  SER B OG  1 
ATOM   1381 N  N   . PRO B 1 86  ? -7.010  -3.514  13.824  1.00 13.58 ? 86  PRO B N   1 
ATOM   1382 C  CA  . PRO B 1 86  ? -7.086  -4.959  13.810  1.00 14.82 ? 86  PRO B CA  1 
ATOM   1383 C  C   . PRO B 1 86  ? -7.900  -5.476  12.669  1.00 15.52 ? 86  PRO B C   1 
ATOM   1384 O  O   . PRO B 1 86  ? -8.756  -4.772  12.184  1.00 15.87 ? 86  PRO B O   1 
ATOM   1385 C  CB  . PRO B 1 86  ? -7.800  -5.245  15.122  1.00 18.63 ? 86  PRO B CB  1 
ATOM   1386 C  CG  . PRO B 1 86  ? -8.814  -4.157  15.188  1.00 21.46 ? 86  PRO B CG  1 
ATOM   1387 C  CD  . PRO B 1 86  ? -8.063  -2.951  14.691  1.00 16.08 ? 86  PRO B CD  1 
ATOM   1388 N  N   . PHE B 1 87  ? -7.622  -6.699  12.287  1.00 10.94 ? 87  PHE B N   1 
ATOM   1389 C  CA  . PHE B 1 87  ? -8.348  -7.327  11.240  1.00 10.35 ? 87  PHE B CA  1 
ATOM   1390 C  C   . PHE B 1 87  ? -9.679  -7.932  11.702  1.00 10.33 ? 87  PHE B C   1 
ATOM   1391 O  O   . PHE B 1 87  ? -10.744 -7.725  11.077  1.00 10.97 ? 87  PHE B O   1 
ATOM   1392 C  CB  . PHE B 1 87  ? -7.513  -8.420  10.653  1.00 11.92 ? 87  PHE B CB  1 
ATOM   1393 C  CG  . PHE B 1 87  ? -8.219  -9.128  9.527   1.00 10.74 ? 87  PHE B CG  1 
ATOM   1394 C  CD1 . PHE B 1 87  ? -8.374  -8.505  8.278   1.00 13.08 ? 87  PHE B CD1 1 
ATOM   1395 C  CD2 . PHE B 1 87  ? -8.700  -10.399 9.667   1.00 9.79  ? 87  PHE B CD2 1 
ATOM   1396 C  CE1 . PHE B 1 87  ? -9.058  -9.073  7.256   1.00 14.82 ? 87  PHE B CE1 1 
ATOM   1397 C  CE2 . PHE B 1 87  ? -9.403  -10.994 8.611   1.00 12.45 ? 87  PHE B CE2 1 
ATOM   1398 C  CZ  . PHE B 1 87  ? -9.582  -10.340 7.415   1.00 14.20 ? 87  PHE B CZ  1 
ATOM   1399 N  N   . HIS B 1 88  ? -9.639  -8.686  12.776  1.00 11.68 ? 88  HIS B N   1 
ATOM   1400 C  CA  . HIS B 1 88  ? -10.770 -9.470  13.184  1.00 11.52 ? 88  HIS B CA  1 
ATOM   1401 C  C   . HIS B 1 88  ? -11.696 -8.711  14.132  1.00 9.85  ? 88  HIS B C   1 
ATOM   1402 O  O   . HIS B 1 88  ? -11.324 -7.812  14.863  1.00 14.30 ? 88  HIS B O   1 
ATOM   1403 C  CB  . HIS B 1 88  ? -10.323 -10.755 13.903  1.00 11.95 ? 88  HIS B CB  1 
ATOM   1404 C  CG  . HIS B 1 88  ? -9.417  -11.648 13.139  1.00 12.79 ? 88  HIS B CG  1 
ATOM   1405 N  ND1 . HIS B 1 88  ? -8.050  -11.604 13.216  1.00 12.07 ? 88  HIS B ND1 1 
ATOM   1406 C  CD2 . HIS B 1 88  ? -9.721  -12.635 12.262  1.00 15.02 ? 88  HIS B CD2 1 
ATOM   1407 C  CE1 . HIS B 1 88  ? -7.553  -12.547 12.426  1.00 15.20 ? 88  HIS B CE1 1 
ATOM   1408 N  NE2 . HIS B 1 88  ? -8.575  -13.169 11.822  1.00 16.14 ? 88  HIS B NE2 1 
ATOM   1409 N  N   . GLU B 1 89  ? -12.967 -9.114  14.165  1.00 13.10 ? 89  GLU B N   1 
ATOM   1410 C  CA  . GLU B 1 89  ? -13.928 -8.597  15.166  1.00 17.02 ? 89  GLU B CA  1 
ATOM   1411 C  C   . GLU B 1 89  ? -13.642 -9.192  16.517  1.00 17.81 ? 89  GLU B C   1 
ATOM   1412 O  O   . GLU B 1 89  ? -13.779 -8.538  17.562  1.00 21.53 ? 89  GLU B O   1 
ATOM   1413 C  CB  . GLU B 1 89  ? -15.348 -8.924  14.707  1.00 16.08 ? 89  GLU B CB  1 
ATOM   1414 C  CG  . GLU B 1 89  ? -15.806 -8.134  13.491  1.00 19.02 ? 89  GLU B CG  1 
ATOM   1415 C  CD  . GLU B 1 89  ? -15.921 -6.662  13.798  1.00 23.18 ? 89  GLU B CD  1 
ATOM   1416 O  OE1 . GLU B 1 89  ? -16.673 -6.294  14.738  1.00 24.28 ? 89  GLU B OE1 1 
ATOM   1417 O  OE2 . GLU B 1 89  ? -15.236 -5.897  13.117  1.00 26.37 ? 89  GLU B OE2 1 
ATOM   1418 N  N   . HIS B 1 90  ? -13.304 -10.461 16.499  1.00 21.25 ? 90  HIS B N   1 
ATOM   1419 C  CA  . HIS B 1 90  ? -13.057 -11.169 17.772  1.00 20.53 ? 90  HIS B CA  1 
ATOM   1420 C  C   . HIS B 1 90  ? -12.291 -12.449 17.489  1.00 25.46 ? 90  HIS B C   1 
ATOM   1421 O  O   . HIS B 1 90  ? -12.151 -12.761 16.304  1.00 26.82 ? 90  HIS B O   1 
ATOM   1422 C  CB  . HIS B 1 90  ? -14.395 -11.397 18.520  1.00 27.78 ? 90  HIS B CB  1 
ATOM   1423 C  CG  . HIS B 1 90  ? -15.599 -11.705 17.702  1.00 34.38 ? 90  HIS B CG  1 
ATOM   1424 N  ND1 . HIS B 1 90  ? -15.760 -12.906 17.050  1.00 40.70 ? 90  HIS B ND1 1 
ATOM   1425 C  CD2 . HIS B 1 90  ? -16.735 -11.006 17.500  1.00 40.89 ? 90  HIS B CD2 1 
ATOM   1426 C  CE1 . HIS B 1 90  ? -16.926 -12.917 16.444  1.00 45.50 ? 90  HIS B CE1 1 
ATOM   1427 N  NE2 . HIS B 1 90  ? -17.542 -11.762 16.700  1.00 47.80 ? 90  HIS B NE2 1 
ATOM   1428 N  N   . ALA B 1 91  ? -11.603 -13.023 18.466  1.00 28.59 ? 91  ALA B N   1 
ATOM   1429 C  CA  . ALA B 1 91  ? -11.072 -14.359 18.313  1.00 29.02 ? 91  ALA B CA  1 
ATOM   1430 C  C   . ALA B 1 91  ? -12.168 -15.233 18.904  1.00 28.96 ? 91  ALA B C   1 
ATOM   1431 O  O   . ALA B 1 91  ? -12.521 -15.047 20.024  1.00 30.54 ? 91  ALA B O   1 
ATOM   1432 C  CB  . ALA B 1 91  ? -9.759  -14.507 19.073  1.00 29.92 ? 91  ALA B CB  1 
ATOM   1433 N  N   . GLU B 1 92  ? -12.908 -15.971 18.052  1.00 43.10 ? 92  GLU B N   1 
ATOM   1434 C  CA  . GLU B 1 92  ? -14.120 -16.725 18.487  1.00 32.94 ? 92  GLU B CA  1 
ATOM   1435 C  C   . GLU B 1 92  ? -13.817 -18.200 18.446  1.00 31.89 ? 92  GLU B C   1 
ATOM   1436 O  O   . GLU B 1 92  ? -13.422 -18.661 17.399  1.00 34.87 ? 92  GLU B O   1 
ATOM   1437 N  N   . VAL B 1 93  ? -14.147 -18.940 19.493  1.00 24.28 ? 93  VAL B N   1 
ATOM   1438 C  CA  . VAL B 1 93  ? -13.659 -20.264 19.598  1.00 25.40 ? 93  VAL B CA  1 
ATOM   1439 C  C   . VAL B 1 93  ? -14.667 -21.303 20.093  1.00 24.39 ? 93  VAL B C   1 
ATOM   1440 O  O   . VAL B 1 93  ? -15.158 -21.206 21.167  1.00 22.77 ? 93  VAL B O   1 
ATOM   1441 C  CB  . VAL B 1 93  ? -12.422 -20.183 20.417  1.00 23.04 ? 93  VAL B CB  1 
ATOM   1442 C  CG1 . VAL B 1 93  ? -11.958 -21.671 20.685  1.00 28.45 ? 93  VAL B CG1 1 
ATOM   1443 C  CG2 . VAL B 1 93  ? -11.451 -19.299 19.601  1.00 33.66 ? 93  VAL B CG2 1 
ATOM   1444 N  N   . VAL B 1 94  ? -14.955 -22.296 19.242  1.00 21.70 ? 94  VAL B N   1 
ATOM   1445 C  CA  . VAL B 1 94  ? -16.171 -23.131 19.367  1.00 22.58 ? 94  VAL B CA  1 
ATOM   1446 C  C   . VAL B 1 94  ? -15.828 -24.615 19.481  1.00 23.08 ? 94  VAL B C   1 
ATOM   1447 O  O   . VAL B 1 94  ? -15.185 -25.184 18.599  1.00 23.41 ? 94  VAL B O   1 
ATOM   1448 C  CB  . VAL B 1 94  ? -17.150 -22.971 18.191  1.00 26.25 ? 94  VAL B CB  1 
ATOM   1449 C  CG1 . VAL B 1 94  ? -18.402 -23.838 18.454  1.00 23.99 ? 94  VAL B CG1 1 
ATOM   1450 C  CG2 . VAL B 1 94  ? -17.514 -21.493 17.945  1.00 28.91 ? 94  VAL B CG2 1 
ATOM   1451 N  N   . PHE B 1 95  ? -16.256 -25.244 20.564  1.00 20.03 ? 95  PHE B N   1 
ATOM   1452 C  CA  . PHE B 1 95  ? -15.784 -26.591 20.900  1.00 23.98 ? 95  PHE B CA  1 
ATOM   1453 C  C   . PHE B 1 95  ? -16.815 -27.414 21.635  1.00 17.54 ? 95  PHE B C   1 
ATOM   1454 O  O   . PHE B 1 95  ? -17.736 -26.890 22.209  1.00 20.19 ? 95  PHE B O   1 
ATOM   1455 C  CB  . PHE B 1 95  ? -14.540 -26.521 21.753  1.00 21.09 ? 95  PHE B CB  1 
ATOM   1456 C  CG  . PHE B 1 95  ? -14.770 -25.869 23.122  1.00 21.51 ? 95  PHE B CG  1 
ATOM   1457 C  CD1 . PHE B 1 95  ? -14.638 -24.499 23.299  1.00 26.64 ? 95  PHE B CD1 1 
ATOM   1458 C  CD2 . PHE B 1 95  ? -15.079 -26.645 24.251  1.00 23.17 ? 95  PHE B CD2 1 
ATOM   1459 C  CE1 . PHE B 1 95  ? -14.834 -23.924 24.560  1.00 26.27 ? 95  PHE B CE1 1 
ATOM   1460 C  CE2 . PHE B 1 95  ? -15.254 -26.062 25.516  1.00 24.28 ? 95  PHE B CE2 1 
ATOM   1461 C  CZ  . PHE B 1 95  ? -15.114 -24.694 25.668  1.00 21.92 ? 95  PHE B CZ  1 
ATOM   1462 N  N   . THR B 1 96  ? -16.669 -28.741 21.540  1.00 21.48 ? 96  THR B N   1 
ATOM   1463 C  CA  . THR B 1 96  ? -17.533 -29.612 22.278  1.00 20.69 ? 96  THR B CA  1 
ATOM   1464 C  C   . THR B 1 96  ? -16.799 -30.016 23.530  1.00 27.55 ? 96  THR B C   1 
ATOM   1465 O  O   . THR B 1 96  ? -15.668 -30.453 23.452  1.00 31.02 ? 96  THR B O   1 
ATOM   1466 C  CB  . THR B 1 96  ? -17.890 -30.858 21.457  1.00 30.95 ? 96  THR B CB  1 
ATOM   1467 O  OG1 . THR B 1 96  ? -18.722 -30.490 20.345  1.00 36.88 ? 96  THR B OG1 1 
ATOM   1468 C  CG2 . THR B 1 96  ? -18.638 -31.913 22.306  1.00 37.13 ? 96  THR B CG2 1 
ATOM   1469 N  N   . ALA B 1 97  ? -17.466 -29.877 24.665  1.00 26.65 ? 97  ALA B N   1 
ATOM   1470 C  CA  . ALA B 1 97  ? -16.934 -30.228 25.964  1.00 23.18 ? 97  ALA B CA  1 
ATOM   1471 C  C   . ALA B 1 97  ? -17.427 -31.642 26.290  1.00 32.52 ? 97  ALA B C   1 
ATOM   1472 O  O   . ALA B 1 97  ? -18.611 -31.818 26.507  1.00 27.90 ? 97  ALA B O   1 
ATOM   1473 C  CB  . ALA B 1 97  ? -17.462 -29.264 27.038  1.00 27.98 ? 97  ALA B CB  1 
ATOM   1474 N  N   . ASN B 1 98  ? -16.558 -32.648 26.315  1.00 37.14 ? 98  ASN B N   1 
ATOM   1475 C  CA  . ASN B 1 98  ? -16.949 -34.010 26.698  1.00 36.76 ? 98  ASN B CA  1 
ATOM   1476 C  C   . ASN B 1 98  ? -16.986 -35.059 25.566  1.00 44.57 ? 98  ASN B C   1 
ATOM   1477 O  O   . ASN B 1 98  ? -17.578 -36.169 25.729  1.00 40.04 ? 98  ASN B O   1 
ATOM   1478 N  N   . ARG B 1 104 ? -10.517 -30.020 33.729  1.00 32.56 ? 104 ARG B N   1 
ATOM   1479 C  CA  . ARG B 1 104 ? -10.453 -28.564 33.663  1.00 26.78 ? 104 ARG B CA  1 
ATOM   1480 C  C   . ARG B 1 104 ? -9.937  -28.127 32.292  1.00 30.15 ? 104 ARG B C   1 
ATOM   1481 O  O   . ARG B 1 104 ? -8.939  -28.703 31.736  1.00 26.75 ? 104 ARG B O   1 
ATOM   1482 C  CB  . ARG B 1 104 ? -9.488  -28.018 34.712  1.00 34.15 ? 104 ARG B CB  1 
ATOM   1483 N  N   . TYR B 1 105 ? -10.594 -27.114 31.744  1.00 21.67 ? 105 TYR B N   1 
ATOM   1484 C  CA  . TYR B 1 105 ? -10.266 -26.598 30.410  1.00 20.60 ? 105 TYR B CA  1 
ATOM   1485 C  C   . TYR B 1 105 ? -9.609  -25.257 30.504  1.00 26.19 ? 105 TYR B C   1 
ATOM   1486 O  O   . TYR B 1 105 ? -10.118 -24.347 31.155  1.00 27.25 ? 105 TYR B O   1 
ATOM   1487 C  CB  . TYR B 1 105 ? -11.550 -26.406 29.576  1.00 23.92 ? 105 TYR B CB  1 
ATOM   1488 C  CG  . TYR B 1 105 ? -12.262 -27.678 29.171  1.00 26.68 ? 105 TYR B CG  1 
ATOM   1489 C  CD1 . TYR B 1 105 ? -12.988 -28.441 30.091  1.00 31.12 ? 105 TYR B CD1 1 
ATOM   1490 C  CD2 . TYR B 1 105 ? -12.198 -28.115 27.884  1.00 29.08 ? 105 TYR B CD2 1 
ATOM   1491 C  CE1 . TYR B 1 105 ? -13.625 -29.618 29.696  1.00 37.11 ? 105 TYR B CE1 1 
ATOM   1492 C  CE2 . TYR B 1 105 ? -12.836 -29.262 27.477  1.00 34.15 ? 105 TYR B CE2 1 
ATOM   1493 C  CZ  . TYR B 1 105 ? -13.549 -30.006 28.371  1.00 32.07 ? 105 TYR B CZ  1 
ATOM   1494 O  OH  . TYR B 1 105 ? -14.152 -31.135 27.845  1.00 36.80 ? 105 TYR B OH  1 
ATOM   1495 N  N   . THR B 1 106 ? -8.500  -25.118 29.794  1.00 20.41 ? 106 THR B N   1 
ATOM   1496 C  CA  . THR B 1 106 ? -7.886  -23.818 29.652  1.00 19.97 ? 106 THR B CA  1 
ATOM   1497 C  C   . THR B 1 106 ? -7.938  -23.500 28.188  1.00 16.63 ? 106 THR B C   1 
ATOM   1498 O  O   . THR B 1 106 ? -7.406  -24.251 27.359  1.00 19.26 ? 106 THR B O   1 
ATOM   1499 C  CB  . THR B 1 106 ? -6.452  -23.771 30.141  1.00 24.15 ? 106 THR B CB  1 
ATOM   1500 O  OG1 . THR B 1 106 ? -6.413  -24.035 31.562  1.00 29.27 ? 106 THR B OG1 1 
ATOM   1501 C  CG2 . THR B 1 106 ? -5.755  -22.387 29.819  1.00 24.02 ? 106 THR B CG2 1 
ATOM   1502 N  N   . ILE B 1 107 ? -8.545  -22.364 27.851  1.00 18.36 ? 107 ILE B N   1 
ATOM   1503 C  CA  . ILE B 1 107 ? -8.598  -21.931 26.461  1.00 17.66 ? 107 ILE B CA  1 
ATOM   1504 C  C   . ILE B 1 107 ? -7.645  -20.755 26.341  1.00 17.68 ? 107 ILE B C   1 
ATOM   1505 O  O   . ILE B 1 107 ? -7.889  -19.748 26.960  1.00 23.20 ? 107 ILE B O   1 
ATOM   1506 C  CB  . ILE B 1 107 ? -10.041 -21.495 26.135  1.00 19.76 ? 107 ILE B CB  1 
ATOM   1507 C  CG1 . ILE B 1 107 ? -11.037 -22.710 26.319  1.00 20.92 ? 107 ILE B CG1 1 
ATOM   1508 C  CG2 . ILE B 1 107 ? -10.128 -20.799 24.787  1.00 22.46 ? 107 ILE B CG2 1 
ATOM   1509 C  CD1 . ILE B 1 107 ? -10.871 -23.903 25.401  1.00 23.27 ? 107 ILE B CD1 1 
ATOM   1510 N  N   . ALA B 1 108 ? -6.598  -20.853 25.539  1.00 16.33 ? 108 ALA B N   1 
ATOM   1511 C  CA  . ALA B 1 108 ? -5.615  -19.800 25.364  1.00 16.90 ? 108 ALA B CA  1 
ATOM   1512 C  C   . ALA B 1 108 ? -5.701  -19.246 23.974  1.00 19.25 ? 108 ALA B C   1 
ATOM   1513 O  O   . ALA B 1 108 ? -5.899  -19.988 23.009  1.00 19.92 ? 108 ALA B O   1 
ATOM   1514 C  CB  . ALA B 1 108 ? -4.202  -20.298 25.624  1.00 23.46 ? 108 ALA B CB  1 
ATOM   1515 N  N   . ALA B 1 109 ? -5.533  -17.924 23.882  1.00 15.71 ? 109 ALA B N   1 
ATOM   1516 C  CA  . ALA B 1 109 ? -5.554  -17.205 22.608  1.00 13.23 ? 109 ALA B CA  1 
ATOM   1517 C  C   . ALA B 1 109 ? -4.327  -16.295 22.538  1.00 15.35 ? 109 ALA B C   1 
ATOM   1518 O  O   . ALA B 1 109 ? -3.994  -15.606 23.495  1.00 17.92 ? 109 ALA B O   1 
ATOM   1519 C  CB  . ALA B 1 109 ? -6.826  -16.370 22.429  1.00 17.69 ? 109 ALA B CB  1 
ATOM   1520 N  N   . LEU B 1 110 ? -3.626  -16.396 21.419  1.00 12.95 ? 110 LEU B N   1 
ATOM   1521 C  CA  . LEU B 1 110 ? -2.444  -15.585 21.106  1.00 13.12 ? 110 LEU B CA  1 
ATOM   1522 C  C   . LEU B 1 110 ? -2.771  -14.659 19.989  1.00 13.47 ? 110 LEU B C   1 
ATOM   1523 O  O   . LEU B 1 110 ? -3.098  -15.124 18.914  1.00 11.75 ? 110 LEU B O   1 
ATOM   1524 C  CB  . LEU B 1 110 ? -1.329  -16.522 20.672  1.00 14.10 ? 110 LEU B CB  1 
ATOM   1525 C  CG  . LEU B 1 110 ? -0.015  -15.852 20.288  1.00 15.08 ? 110 LEU B CG  1 
ATOM   1526 C  CD1 . LEU B 1 110 ? 0.612   -15.147 21.486  1.00 16.19 ? 110 LEU B CD1 1 
ATOM   1527 C  CD2 . LEU B 1 110 ? 0.938   -16.869 19.693  1.00 20.42 ? 110 LEU B CD2 1 
ATOM   1528 N  N   . LEU B 1 111 ? -2.663  -13.359 20.236  1.00 10.47 ? 111 LEU B N   1 
ATOM   1529 C  CA  . LEU B 1 111 ? -3.221  -12.320 19.372  1.00 12.10 ? 111 LEU B CA  1 
ATOM   1530 C  C   . LEU B 1 111 ? -2.174  -11.540 18.594  1.00 10.67 ? 111 LEU B C   1 
ATOM   1531 O  O   . LEU B 1 111 ? -1.197  -11.069 19.177  1.00 10.69 ? 111 LEU B O   1 
ATOM   1532 C  CB  . LEU B 1 111 ? -4.031  -11.334 20.226  1.00 11.67 ? 111 LEU B CB  1 
ATOM   1533 C  CG  . LEU B 1 111 ? -5.057  -11.876 21.142  1.00 11.75 ? 111 LEU B CG  1 
ATOM   1534 C  CD1 . LEU B 1 111 ? -5.819  -10.709 21.781  1.00 14.31 ? 111 LEU B CD1 1 
ATOM   1535 C  CD2 . LEU B 1 111 ? -6.012  -12.839 20.368  1.00 11.70 ? 111 LEU B CD2 1 
ATOM   1536 N  N   . SER B 1 112 ? -2.398  -11.366 17.308  1.00 9.41  ? 112 SER B N   1 
ATOM   1537 C  CA  . SER B 1 112 ? -1.685  -10.406 16.506  1.00 10.64 ? 112 SER B CA  1 
ATOM   1538 C  C   . SER B 1 112 ? -2.759  -9.587  15.732  1.00 9.68  ? 112 SER B C   1 
ATOM   1539 O  O   . SER B 1 112 ? -3.920  -9.946  15.642  1.00 11.64 ? 112 SER B O   1 
ATOM   1540 C  CB  . SER B 1 112 ? -0.758  -11.108 15.513  1.00 13.21 ? 112 SER B CB  1 
ATOM   1541 O  OG  . SER B 1 112 ? 0.145   -11.913 16.244  1.00 13.71 ? 112 SER B OG  1 
ATOM   1542 N  N   . PRO B 1 113 ? -2.362  -8.439  15.133  1.00 11.34 ? 113 PRO B N   1 
ATOM   1543 C  CA  . PRO B 1 113 ? -3.383  -7.633  14.517  1.00 11.96 ? 113 PRO B CA  1 
ATOM   1544 C  C   . PRO B 1 113 ? -4.129  -8.316  13.415  1.00 9.56  ? 113 PRO B C   1 
ATOM   1545 O  O   . PRO B 1 113 ? -5.321  -8.079  13.285  1.00 11.53 ? 113 PRO B O   1 
ATOM   1546 C  CB  . PRO B 1 113 ? -2.615  -6.345  14.083  1.00 12.88 ? 113 PRO B CB  1 
ATOM   1547 C  CG  . PRO B 1 113 ? -1.507  -6.244  15.085  1.00 13.97 ? 113 PRO B CG  1 
ATOM   1548 C  CD  . PRO B 1 113 ? -1.119  -7.683  15.362  1.00 13.31 ? 113 PRO B CD  1 
ATOM   1549 N  N   . TYR B 1 114 ? -3.435  -9.150  12.598  1.00 10.44 ? 114 TYR B N   1 
ATOM   1550 C  CA  . TYR B 1 114 ? -4.059  -9.874  11.519  1.00 11.49 ? 114 TYR B CA  1 
ATOM   1551 C  C   . TYR B 1 114 ? -4.108  -11.357 11.719  1.00 12.73 ? 114 TYR B C   1 
ATOM   1552 O  O   . TYR B 1 114 ? -4.426  -12.054 10.796  1.00 13.38 ? 114 TYR B O   1 
ATOM   1553 C  CB  . TYR B 1 114 ? -3.361  -9.560  10.160  1.00 11.27 ? 114 TYR B CB  1 
ATOM   1554 C  CG  . TYR B 1 114 ? -3.660  -8.188  9.694   1.00 10.18 ? 114 TYR B CG  1 
ATOM   1555 C  CD1 . TYR B 1 114 ? -2.953  -7.082  10.202  1.00 13.47 ? 114 TYR B CD1 1 
ATOM   1556 C  CD2 . TYR B 1 114 ? -4.596  -7.969  8.729   1.00 10.77 ? 114 TYR B CD2 1 
ATOM   1557 C  CE1 . TYR B 1 114 ? -3.239  -5.799  9.795   1.00 15.07 ? 114 TYR B CE1 1 
ATOM   1558 C  CE2 . TYR B 1 114 ? -4.895  -6.701  8.333   1.00 14.00 ? 114 TYR B CE2 1 
ATOM   1559 C  CZ  . TYR B 1 114 ? -4.218  -5.637  8.876   1.00 15.11 ? 114 TYR B CZ  1 
ATOM   1560 O  OH  . TYR B 1 114 ? -4.511  -4.362  8.489   1.00 17.76 ? 114 TYR B OH  1 
ATOM   1561 N  N   . SER B 1 115 ? -3.931  -11.845 12.919  1.00 11.24 ? 115 SER B N   1 
ATOM   1562 C  CA  . SER B 1 115 ? -3.900  -13.262 13.151  1.00 9.61  ? 115 SER B CA  1 
ATOM   1563 C  C   . SER B 1 115 ? -4.231  -13.590 14.589  1.00 10.93 ? 115 SER B C   1 
ATOM   1564 O  O   . SER B 1 115 ? -3.981  -12.788 15.495  1.00 11.81 ? 115 SER B O   1 
ATOM   1565 C  CB  . SER B 1 115 ? -2.511  -13.827 12.906  1.00 12.47 ? 115 SER B CB  1 
ATOM   1566 O  OG  . SER B 1 115 ? -2.421  -15.192 13.131  1.00 18.66 ? 115 SER B OG  1 
ATOM   1567 N  N   . TYR B 1 116 ? -4.725  -14.815 14.799  1.00 12.33 ? 116 TYR B N   1 
ATOM   1568 C  CA  . TYR B 1 116 ? -4.742  -15.379 16.141  1.00 10.05 ? 116 TYR B CA  1 
ATOM   1569 C  C   . TYR B 1 116 ? -4.612  -16.912 16.098  1.00 9.96  ? 116 TYR B C   1 
ATOM   1570 O  O   . TYR B 1 116 ? -4.923  -17.560 15.074  1.00 13.50 ? 116 TYR B O   1 
ATOM   1571 C  CB  . TYR B 1 116 ? -5.998  -14.990 16.948  1.00 12.03 ? 116 TYR B CB  1 
ATOM   1572 C  CG  . TYR B 1 116 ? -7.304  -15.517 16.430  1.00 10.03 ? 116 TYR B CG  1 
ATOM   1573 C  CD1 . TYR B 1 116 ? -7.795  -16.743 16.842  1.00 13.39 ? 116 TYR B CD1 1 
ATOM   1574 C  CD2 . TYR B 1 116 ? -7.999  -14.816 15.499  1.00 16.65 ? 116 TYR B CD2 1 
ATOM   1575 C  CE1 . TYR B 1 116 ? -8.982  -17.219 16.353  1.00 16.02 ? 116 TYR B CE1 1 
ATOM   1576 C  CE2 . TYR B 1 116 ? -9.147  -15.260 15.010  1.00 22.35 ? 116 TYR B CE2 1 
ATOM   1577 C  CZ  . TYR B 1 116 ? -9.633  -16.456 15.451  1.00 16.10 ? 116 TYR B CZ  1 
ATOM   1578 O  OH  . TYR B 1 116 ? -10.806 -16.872 14.903  1.00 32.15 ? 116 TYR B OH  1 
ATOM   1579 N  N   . SER B 1 117 ? -4.038  -17.443 17.163  1.00 11.80 ? 117 SER B N   1 
ATOM   1580 C  CA  . SER B 1 117 ? -4.010  -18.838 17.363  1.00 12.29 ? 117 SER B CA  1 
ATOM   1581 C  C   . SER B 1 117 ? -4.823  -19.101 18.646  1.00 12.96 ? 117 SER B C   1 
ATOM   1582 O  O   . SER B 1 117 ? -4.715  -18.366 19.627  1.00 13.08 ? 117 SER B O   1 
ATOM   1583 C  CB  . SER B 1 117 ? -2.551  -19.282 17.559  1.00 14.60 ? 117 SER B CB  1 
ATOM   1584 O  OG  . SER B 1 117 ? -1.833  -19.149 16.328  1.00 17.44 ? 117 SER B OG  1 
ATOM   1585 N  N   . THR B 1 118 ? -5.544  -20.204 18.680  1.00 12.84 ? 118 THR B N   1 
ATOM   1586 C  CA  . THR B 1 118 ? -6.174  -20.650 19.910  1.00 12.14 ? 118 THR B CA  1 
ATOM   1587 C  C   . THR B 1 118 ? -5.960  -22.105 20.143  1.00 14.68 ? 118 THR B C   1 
ATOM   1588 O  O   . THR B 1 118 ? -5.811  -22.869 19.203  1.00 17.16 ? 118 THR B O   1 
ATOM   1589 C  CB  . THR B 1 118 ? -7.654  -20.340 19.871  1.00 15.67 ? 118 THR B CB  1 
ATOM   1590 O  OG1 . THR B 1 118 ? -8.226  -20.692 21.110  1.00 22.38 ? 118 THR B OG1 1 
ATOM   1591 C  CG2 . THR B 1 118 ? -8.377  -20.973 18.729  1.00 16.78 ? 118 THR B CG2 1 
ATOM   1592 N  N   . THR B 1 119 ? -5.854  -22.459 21.415  1.00 14.43 ? 119 THR B N   1 
ATOM   1593 C  CA  . THR B 1 119 ? -5.692  -23.834 21.801  1.00 14.41 ? 119 THR B CA  1 
ATOM   1594 C  C   . THR B 1 119 ? -6.505  -24.114 23.063  1.00 15.27 ? 119 THR B C   1 
ATOM   1595 O  O   . THR B 1 119 ? -6.867  -23.214 23.796  1.00 19.00 ? 119 THR B O   1 
ATOM   1596 C  CB  . THR B 1 119 ? -4.231  -24.230 22.012  1.00 21.64 ? 119 THR B CB  1 
ATOM   1597 O  OG1 . THR B 1 119 ? -4.073  -25.686 21.962  1.00 24.98 ? 119 THR B OG1 1 
ATOM   1598 C  CG2 . THR B 1 119 ? -3.635  -23.666 23.246  1.00 23.24 ? 119 THR B CG2 1 
ATOM   1599 N  N   . ALA B 1 120 ? -6.695  -25.397 23.318  1.00 15.93 ? 120 ALA B N   1 
ATOM   1600 C  CA  . ALA B 1 120 ? -7.372  -25.883 24.517  1.00 17.01 ? 120 ALA B CA  1 
ATOM   1601 C  C   . ALA B 1 120 ? -6.484  -26.910 25.147  1.00 18.33 ? 120 ALA B C   1 
ATOM   1602 O  O   . ALA B 1 120 ? -5.885  -27.750 24.460  1.00 18.44 ? 120 ALA B O   1 
ATOM   1603 C  CB  . ALA B 1 120 ? -8.719  -26.485 24.199  1.00 21.94 ? 120 ALA B CB  1 
ATOM   1604 N  N   . VAL B 1 121 ? -6.311  -26.773 26.450  1.00 19.15 ? 121 VAL B N   1 
ATOM   1605 C  CA  . VAL B 1 121 ? -5.545  -27.710 27.220  1.00 20.98 ? 121 VAL B CA  1 
ATOM   1606 C  C   . VAL B 1 121 ? -6.555  -28.288 28.257  1.00 22.71 ? 121 VAL B C   1 
ATOM   1607 O  O   . VAL B 1 121 ? -7.164  -27.539 29.024  1.00 22.90 ? 121 VAL B O   1 
ATOM   1608 C  CB  . VAL B 1 121 ? -4.353  -27.044 28.007  1.00 22.02 ? 121 VAL B CB  1 
ATOM   1609 C  CG1 . VAL B 1 121 ? -3.547  -28.156 28.632  1.00 31.67 ? 121 VAL B CG1 1 
ATOM   1610 C  CG2 . VAL B 1 121 ? -3.486  -26.119 27.120  1.00 26.84 ? 121 VAL B CG2 1 
ATOM   1611 N  N   . VAL B 1 122 ? -6.733  -29.605 28.218  1.00 24.97 ? 122 VAL B N   1 
ATOM   1612 C  CA  . VAL B 1 122 ? -7.702  -30.302 29.020  1.00 25.75 ? 122 VAL B CA  1 
ATOM   1613 C  C   . VAL B 1 122 ? -6.894  -31.371 29.734  1.00 42.03 ? 122 VAL B C   1 
ATOM   1614 O  O   . VAL B 1 122 ? -6.736  -31.173 30.989  1.00 57.06 ? 122 VAL B O   1 
ATOM   1615 C  CB  . VAL B 1 122 ? -8.799  -30.958 28.124  1.00 43.55 ? 122 VAL B CB  1 
HETATM 1616 CA CA  . CA  C 2 .   ? -17.444 2.123   4.643   1.00 16.44 ? 201 CA  A CA  1 
HETATM 1617 O  O1  . Z7Z D 3 .   ? 0.192   -18.955 1.650   0.50 62.07 ? 202 Z7Z A O1  1 
HETATM 1618 C  C1  . Z7Z D 3 .   ? 0.031   -20.158 2.201   0.50 34.24 ? 202 Z7Z A C1  1 
HETATM 1619 O  O2  . Z7Z D 3 .   ? -0.074  -21.113 1.480   0.50 34.84 ? 202 Z7Z A O2  1 
HETATM 1620 C  C2  . Z7Z D 3 .   ? -0.010  -20.296 3.710   0.50 35.50 ? 202 Z7Z A C2  1 
HETATM 1621 C  C3  . Z7Z D 3 .   ? 0.963   -19.634 4.455   0.50 36.07 ? 202 Z7Z A C3  1 
HETATM 1622 C  C4  . Z7Z D 3 .   ? 0.956   -19.730 5.844   0.50 32.71 ? 202 Z7Z A C4  1 
HETATM 1623 C  C5  . Z7Z D 3 .   ? -0.987  -21.059 4.365   0.50 38.48 ? 202 Z7Z A C5  1 
HETATM 1624 C  C6  . Z7Z D 3 .   ? -0.989  -21.146 5.761   0.50 30.94 ? 202 Z7Z A C6  1 
HETATM 1625 C  C7  . Z7Z D 3 .   ? -0.008  -20.491 6.506   0.50 31.09 ? 202 Z7Z A C7  1 
HETATM 1626 C  C8  . Z7Z D 3 .   ? 0.013   -20.548 8.004   0.50 22.75 ? 202 Z7Z A C8  1 
HETATM 1627 C  C9  . Z7Z D 3 .   ? 1.187   -20.821 8.704   0.50 24.50 ? 202 Z7Z A C9  1 
HETATM 1628 C  C10 . Z7Z D 3 .   ? -1.160  -20.281 8.707   0.50 24.29 ? 202 Z7Z A C10 1 
HETATM 1629 C  C11 . Z7Z D 3 .   ? 1.174   -20.859 10.092  0.50 21.72 ? 202 Z7Z A C11 1 
HETATM 1630 C  C12 . Z7Z D 3 .   ? -1.163  -20.289 10.093  0.50 22.40 ? 202 Z7Z A C12 1 
HETATM 1631 C  C13 . Z7Z D 3 .   ? 0.002   -20.587 10.793  0.50 27.09 ? 202 Z7Z A C13 1 
HETATM 1632 O  O1  . Z7Z E 3 .   ? 1.122   -19.232 29.320  0.50 33.01 ? 201 Z7Z B O1  1 
HETATM 1633 C  C1  . Z7Z E 3 .   ? 0.364   -20.222 28.847  0.50 30.08 ? 201 Z7Z B C1  1 
HETATM 1634 O  O2  . Z7Z E 3 .   ? -0.194  -20.973 29.644  0.50 32.27 ? 201 Z7Z B O2  1 
HETATM 1635 C  C2  . Z7Z E 3 .   ? 0.213   -20.361 27.357  0.50 26.25 ? 201 Z7Z B C2  1 
HETATM 1636 C  C3  . Z7Z E 3 .   ? -0.796  -21.125 26.777  0.50 33.01 ? 201 Z7Z B C3  1 
HETATM 1637 C  C4  . Z7Z E 3 .   ? -0.894  -21.216 25.393  0.50 32.16 ? 201 Z7Z B C4  1 
HETATM 1638 C  C5  . Z7Z E 3 .   ? 1.112   -19.684 26.545  0.50 32.11 ? 201 Z7Z B C5  1 
HETATM 1639 C  C6  . Z7Z E 3 .   ? 1.004   -19.767 25.173  0.50 30.54 ? 201 Z7Z B C6  1 
HETATM 1640 C  C7  . Z7Z E 3 .   ? 0.013   -20.533 24.595  0.50 28.69 ? 201 Z7Z B C7  1 
HETATM 1641 C  C8  . Z7Z E 3 .   ? -0.023  -20.564 23.132  0.50 24.43 ? 201 Z7Z B C8  1 
HETATM 1642 C  C9  . Z7Z E 3 .   ? -1.222  -20.367 22.455  0.50 26.65 ? 201 Z7Z B C9  1 
HETATM 1643 C  C10 . Z7Z E 3 .   ? 1.170   -20.753 22.443  0.50 27.24 ? 201 Z7Z B C10 1 
HETATM 1644 C  C11 . Z7Z E 3 .   ? -1.224  -20.372 21.054  0.50 26.28 ? 201 Z7Z B C11 1 
HETATM 1645 C  C12 . Z7Z E 3 .   ? 1.162   -20.775 21.045  0.50 25.94 ? 201 Z7Z B C12 1 
HETATM 1646 C  C13 . Z7Z E 3 .   ? -0.035  -20.582 20.366  0.50 30.06 ? 201 Z7Z B C13 1 
HETATM 1647 O  O   . HOH F 4 .   ? -22.712 -7.131  7.455   1.00 22.10 ? 301 HOH A O   1 
HETATM 1648 O  O   . HOH F 4 .   ? -6.154  -25.228 -5.805  1.00 29.30 ? 302 HOH A O   1 
HETATM 1649 O  O   . HOH F 4 .   ? -15.867 -4.976  -2.598  1.00 29.76 ? 303 HOH A O   1 
HETATM 1650 O  O   . HOH F 4 .   ? 0.417   -37.407 12.760  1.00 19.33 ? 304 HOH A O   1 
HETATM 1651 O  O   . HOH F 4 .   ? -13.472 -22.169 16.722  1.00 22.67 ? 305 HOH A O   1 
HETATM 1652 O  O   . HOH F 4 .   ? -23.969 -22.076 4.428   1.00 26.32 ? 306 HOH A O   1 
HETATM 1653 O  O   . HOH F 4 .   ? -25.958 -4.361  4.207   1.00 16.42 ? 307 HOH A O   1 
HETATM 1654 O  O   . HOH F 4 .   ? -9.957  -4.270  5.050   1.00 20.64 ? 308 HOH A O   1 
HETATM 1655 O  O   . HOH F 4 .   ? -12.120 -25.745 -4.421  1.00 20.50 ? 309 HOH A O   1 
HETATM 1656 O  O   . HOH F 4 .   ? -8.874  -28.032 13.816  1.00 17.63 ? 310 HOH A O   1 
HETATM 1657 O  O   . HOH F 4 .   ? -7.791  -15.094 9.678   1.00 18.46 ? 311 HOH A O   1 
HETATM 1658 O  O   . HOH F 4 .   ? -10.974 -5.962  8.932   1.00 14.35 ? 312 HOH A O   1 
HETATM 1659 O  O   . HOH F 4 .   ? -15.906 -5.325  -5.058  1.00 33.25 ? 313 HOH A O   1 
HETATM 1660 O  O   . HOH F 4 .   ? -13.171 -6.850  -3.237  1.00 26.91 ? 314 HOH A O   1 
HETATM 1661 O  O   . HOH F 4 .   ? -2.377  -23.810 16.018  1.00 23.57 ? 315 HOH A O   1 
HETATM 1662 O  O   . HOH F 4 .   ? -19.396 2.859   3.581   1.00 22.64 ? 316 HOH A O   1 
HETATM 1663 O  O   . HOH F 4 .   ? -11.257 -1.492  2.912   1.00 18.83 ? 317 HOH A O   1 
HETATM 1664 O  O   . HOH F 4 .   ? -6.551  -33.667 3.694   1.00 21.92 ? 318 HOH A O   1 
HETATM 1665 O  O   . HOH F 4 .   ? -10.778 -31.729 -4.277  1.00 31.99 ? 319 HOH A O   1 
HETATM 1666 O  O   . HOH F 4 .   ? -2.802  -25.864 14.452  1.00 19.55 ? 320 HOH A O   1 
HETATM 1667 O  O   . HOH F 4 .   ? -16.978 -36.667 8.729   1.00 19.56 ? 321 HOH A O   1 
HETATM 1668 O  O   . HOH F 4 .   ? -23.469 -20.742 0.735   1.00 26.11 ? 322 HOH A O   1 
HETATM 1669 O  O   . HOH F 4 .   ? -13.604 -15.299 -4.314  1.00 19.43 ? 323 HOH A O   1 
HETATM 1670 O  O   . HOH F 4 .   ? -13.940 -41.960 9.883   1.00 28.64 ? 324 HOH A O   1 
HETATM 1671 O  O   . HOH F 4 .   ? -21.035 -14.957 -3.489  1.00 27.87 ? 325 HOH A O   1 
HETATM 1672 O  O   . HOH F 4 .   ? -10.352 -23.747 -5.413  1.00 33.30 ? 326 HOH A O   1 
HETATM 1673 O  O   . HOH F 4 .   ? -15.566 -30.506 5.982   1.00 29.32 ? 327 HOH A O   1 
HETATM 1674 O  O   . HOH F 4 .   ? -30.234 -7.408  5.984   1.00 26.18 ? 328 HOH A O   1 
HETATM 1675 O  O   . HOH F 4 .   ? -0.573  -7.495  1.277   1.00 33.95 ? 329 HOH A O   1 
HETATM 1676 O  O   . HOH F 4 .   ? 0.810   -28.651 7.279   1.00 14.78 ? 330 HOH A O   1 
HETATM 1677 O  O   . HOH F 4 .   ? -14.635 -11.225 -9.473  1.00 37.94 ? 331 HOH A O   1 
HETATM 1678 O  O   . HOH F 4 .   ? -7.353  -35.618 19.103  1.00 27.27 ? 332 HOH A O   1 
HETATM 1679 O  O   . HOH F 4 .   ? -8.822  -30.273 -6.431  1.00 25.16 ? 333 HOH A O   1 
HETATM 1680 O  O   . HOH F 4 .   ? -23.022 -19.911 3.415   1.00 25.17 ? 334 HOH A O   1 
HETATM 1681 O  O   . HOH F 4 .   ? -11.868 -42.940 8.317   1.00 28.99 ? 335 HOH A O   1 
HETATM 1682 O  O   . HOH F 4 .   ? -5.196  -11.401 -0.567  1.00 25.68 ? 336 HOH A O   1 
HETATM 1683 O  O   . HOH F 4 .   ? -11.379 -35.575 5.879   1.00 22.51 ? 337 HOH A O   1 
HETATM 1684 O  O   . HOH F 4 .   ? -12.688 -3.333  6.131   1.00 14.57 ? 338 HOH A O   1 
HETATM 1685 O  O   . HOH F 4 .   ? -31.878 -7.936  8.036   1.00 36.01 ? 339 HOH A O   1 
HETATM 1686 O  O   . HOH F 4 .   ? 1.056   -25.214 0.773   1.00 33.20 ? 340 HOH A O   1 
HETATM 1687 O  O   . HOH F 4 .   ? -14.641 4.484   1.712   1.00 31.92 ? 341 HOH A O   1 
HETATM 1688 O  O   . HOH F 4 .   ? -23.499 -1.812  4.125   1.00 34.58 ? 342 HOH A O   1 
HETATM 1689 O  O   . HOH F 4 .   ? -15.934 -31.397 -2.798  1.00 28.47 ? 343 HOH A O   1 
HETATM 1690 O  O   . HOH F 4 .   ? -17.223 -39.263 9.560   1.00 25.10 ? 344 HOH A O   1 
HETATM 1691 O  O   . HOH F 4 .   ? 0.488   -24.093 16.240  1.00 31.18 ? 345 HOH A O   1 
HETATM 1692 O  O   . HOH F 4 .   ? -8.877  -5.412  7.269   1.00 25.09 ? 346 HOH A O   1 
HETATM 1693 O  O   . HOH F 4 .   ? -11.304 -30.301 -6.057  1.00 16.26 ? 347 HOH A O   1 
HETATM 1694 O  O   . HOH F 4 .   ? -17.531 -37.098 6.026   1.00 30.09 ? 348 HOH A O   1 
HETATM 1695 O  O   . HOH F 4 .   ? -9.747  6.095   3.498   1.00 30.27 ? 349 HOH A O   1 
HETATM 1696 O  O   . HOH F 4 .   ? -1.244  -39.061 14.227  1.00 30.59 ? 350 HOH A O   1 
HETATM 1697 O  O   . HOH G 4 .   ? -18.415 -37.873 28.447  1.00 32.71 ? 301 HOH B O   1 
HETATM 1698 O  O   . HOH G 4 .   ? -21.735 -37.378 26.858  1.00 24.53 ? 302 HOH B O   1 
HETATM 1699 O  O   . HOH G 4 .   ? -13.082 -6.264  11.645  1.00 19.38 ? 303 HOH B O   1 
HETATM 1700 O  O   . HOH G 4 .   ? -2.666  -2.478  11.976  1.00 19.81 ? 304 HOH B O   1 
HETATM 1701 O  O   . HOH G 4 .   ? -12.415 -14.313 14.157  1.00 17.60 ? 305 HOH B O   1 
HETATM 1702 O  O   . HOH G 4 .   ? -9.149  -8.162  16.417  1.00 13.56 ? 306 HOH B O   1 
HETATM 1703 O  O   . HOH G 4 .   ? -9.255  -23.070 21.737  1.00 27.97 ? 307 HOH B O   1 
HETATM 1704 O  O   . HOH G 4 .   ? -2.918  -2.301  9.207   1.00 23.45 ? 308 HOH B O   1 
HETATM 1705 O  O   . HOH G 4 .   ? -7.313  -9.318  14.657  1.00 15.41 ? 309 HOH B O   1 
HETATM 1706 O  O   . HOH G 4 .   ? -11.790 -6.380  24.895  1.00 22.41 ? 310 HOH B O   1 
HETATM 1707 O  O   . HOH G 4 .   ? -7.473  3.023   17.756  1.00 21.33 ? 311 HOH B O   1 
HETATM 1708 O  O   . HOH G 4 .   ? -5.980  -10.611 17.379  1.00 11.65 ? 312 HOH B O   1 
HETATM 1709 O  O   . HOH G 4 .   ? -14.461 -21.280 35.658  1.00 27.46 ? 313 HOH B O   1 
HETATM 1710 O  O   . HOH G 4 .   ? -9.433  -13.799 36.816  1.00 30.72 ? 314 HOH B O   1 
HETATM 1711 O  O   . HOH G 4 .   ? -2.298  -5.645  27.743  1.00 24.20 ? 315 HOH B O   1 
HETATM 1712 O  O   . HOH G 4 .   ? -1.157  -14.387 16.795  1.00 15.92 ? 316 HOH B O   1 
HETATM 1713 O  O   . HOH G 4 .   ? -24.639 -27.483 24.045  1.00 32.51 ? 317 HOH B O   1 
HETATM 1714 O  O   . HOH G 4 .   ? -8.485  -11.881 16.904  1.00 17.20 ? 318 HOH B O   1 
HETATM 1715 O  O   . HOH G 4 .   ? -6.064  -2.656  25.135  1.00 35.89 ? 319 HOH B O   1 
HETATM 1716 O  O   . HOH G 4 .   ? -2.500  0.194   12.755  1.00 28.46 ? 320 HOH B O   1 
HETATM 1717 O  O   . HOH G 4 .   ? 3.098   -13.378 23.774  1.00 30.05 ? 321 HOH B O   1 
HETATM 1718 O  O   . HOH G 4 .   ? -10.365 2.672   22.116  1.00 34.50 ? 322 HOH B O   1 
HETATM 1719 O  O   . HOH G 4 .   ? -27.812 -30.726 27.647  1.00 29.47 ? 323 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  ? 0.9786 0.4716 0.2274 -0.0502 -0.0199 -0.0030 10  CYS A CA  
2    C  C   . CYS A 10  ? 0.3455 0.4505 0.2895 0.0585  -0.0837 -0.0080 10  CYS A C   
3    O  O   . CYS A 10  ? 0.3175 0.4965 0.3681 0.0323  -0.0429 0.1280  10  CYS A O   
4    N  N   . PRO A 11  ? 0.2826 0.2771 0.3003 0.0201  -0.0190 0.0512  11  PRO A N   
5    C  CA  . PRO A 11  ? 0.2058 0.2510 0.2940 -0.0051 -0.0539 0.0454  11  PRO A CA  
6    C  C   . PRO A 11  ? 0.2262 0.1828 0.3332 0.0390  0.0139  0.0376  11  PRO A C   
7    O  O   . PRO A 11  ? 0.2234 0.1942 0.2715 0.0261  -0.0793 0.0311  11  PRO A O   
8    C  CB  . PRO A 11  ? 0.3406 0.2645 0.2318 0.0334  0.0127  -0.0109 11  PRO A CB  
9    C  CG  . PRO A 11  ? 0.2729 0.2554 0.3559 0.0463  -0.0418 0.0497  11  PRO A CG  
10   C  CD  . PRO A 11  ? 0.3420 0.3490 0.1838 -0.0054 -0.0783 -0.0164 11  PRO A CD  
11   N  N   . LEU A 12  ? 0.2457 0.1575 0.2146 0.0062  -0.0917 0.0174  12  LEU A N   
12   C  CA  . LEU A 12  ? 0.2028 0.1646 0.1579 -0.0017 -0.0476 -0.0330 12  LEU A CA  
13   C  C   . LEU A 12  ? 0.1942 0.1630 0.1609 -0.0166 -0.0575 -0.0261 12  LEU A C   
14   O  O   . LEU A 12  ? 0.2745 0.1591 0.2626 0.0344  -0.1418 -0.0832 12  LEU A O   
15   C  CB  . LEU A 12  ? 0.1925 0.1895 0.2546 -0.0201 -0.0377 0.0065  12  LEU A CB  
16   C  CG  . LEU A 12  ? 0.1924 0.2212 0.2794 -0.0730 -0.0209 -0.0049 12  LEU A CG  
17   C  CD1 . LEU A 12  ? 0.2149 0.2404 0.1927 -0.0660 -0.0155 -0.0133 12  LEU A CD1 
18   C  CD2 . LEU A 12  ? 0.1630 0.2673 0.3218 -0.0657 0.0104  0.0191  12  LEU A CD2 
19   N  N   . MET A 13  ? 0.1641 0.1409 0.1784 -0.0064 -0.0467 -0.0394 13  MET A N   
20   C  CA  . MET A 13  ? 0.1963 0.1280 0.1889 0.0180  -0.0591 0.0235  13  MET A CA  
21   C  C   . MET A 13  ? 0.1485 0.1621 0.1659 0.0294  -0.0270 0.0006  13  MET A C   
22   O  O   . MET A 13  ? 0.1784 0.1449 0.1600 -0.0062 -0.0314 0.0252  13  MET A O   
23   C  CB  . MET A 13  ? 0.1658 0.1621 0.0900 0.0759  -0.0329 -0.0368 13  MET A CB  
24   C  CG  . MET A 13  ? 0.2920 0.2300 0.0909 0.0438  -0.0110 -0.0209 13  MET A CG  
25   S  SD  . MET A 13  ? 0.3410 0.3182 0.3403 0.0598  0.0682  0.0046  13  MET A SD  
26   C  CE  . MET A 13  ? 0.4300 0.3310 0.3264 0.1371  0.2297  0.0634  13  MET A CE  
27   N  N   . VAL A 14  ? 0.2026 0.1633 0.1819 0.0013  -0.0745 -0.0309 14  VAL A N   
28   C  CA  . VAL A 14  ? 0.1562 0.1779 0.1891 0.0131  -0.0401 -0.0046 14  VAL A CA  
29   C  C   . VAL A 14  ? 0.1813 0.1426 0.1502 -0.0079 -0.0657 -0.0009 14  VAL A C   
30   O  O   . VAL A 14  ? 0.2470 0.1709 0.1767 0.0444  -0.0782 -0.0443 14  VAL A O   
31   C  CB  . VAL A 14  ? 0.1450 0.1395 0.1349 0.0222  -0.0512 0.0275  14  VAL A CB  
32   C  CG1 . VAL A 14  ? 0.1624 0.2077 0.1059 0.0265  -0.0418 0.0361  14  VAL A CG1 
33   C  CG2 . VAL A 14  ? 0.1785 0.1102 0.2005 0.0316  -0.0504 0.0102  14  VAL A CG2 
34   N  N   . LYS A 15  ? 0.1790 0.1255 0.1746 0.0169  -0.0928 -0.0401 15  LYS A N   
35   C  CA  . LYS A 15  ? 0.2226 0.0823 0.1764 0.0276  -0.0845 0.0116  15  LYS A CA  
36   C  C   . LYS A 15  ? 0.2657 0.1606 0.1555 0.0415  -0.0731 0.0167  15  LYS A C   
37   O  O   . LYS A 15  ? 0.3212 0.1424 0.2563 0.0116  -0.1068 -0.0098 15  LYS A O   
38   C  CB  . LYS A 15  ? 0.2808 0.2173 0.2330 0.0347  -0.0541 0.0032  15  LYS A CB  
39   C  CG  . LYS A 15  ? 0.3739 0.4121 0.4255 0.1352  -0.0773 0.0174  15  LYS A CG  
40   C  CD  . LYS A 15  ? 0.4059 0.6476 0.4358 -0.0250 -0.0696 -0.0267 15  LYS A CD  
41   C  CE  . LYS A 15  ? 0.4997 0.4621 0.4466 0.1777  -0.0517 0.0843  15  LYS A CE  
42   N  NZ  . LYS A 15  ? 0.3772 0.7610 0.4072 0.2664  -0.0991 -0.0019 15  LYS A NZ  
43   N  N   . VAL A 16  ? 0.2270 0.1566 0.1819 0.0511  -0.0686 0.0316  16  VAL A N   
44   C  CA  . VAL A 16  ? 0.2002 0.1510 0.1343 0.0569  -0.0959 -0.0254 16  VAL A CA  
45   C  C   . VAL A 16  ? 0.1873 0.1309 0.1284 0.0332  -0.0314 0.0095  16  VAL A C   
46   O  O   . VAL A 16  ? 0.1949 0.1633 0.1789 0.0288  -0.0754 -0.0429 16  VAL A O   
47   C  CB  . VAL A 16  ? 0.2175 0.1202 0.1848 0.0466  0.0023  0.0124  16  VAL A CB  
48   C  CG1 . VAL A 16  ? 0.1921 0.1483 0.1837 0.0419  0.0070  0.0215  16  VAL A CG1 
49   C  CG2 . VAL A 16  ? 0.1949 0.1242 0.3180 0.0509  -0.0636 -0.0577 16  VAL A CG2 
50   N  N   . LEU A 17  ? 0.1625 0.0922 0.1651 0.0274  -0.0445 -0.0201 17  LEU A N   
51   C  CA  . LEU A 17  ? 0.1184 0.1367 0.1546 0.0293  -0.0375 -0.0267 17  LEU A CA  
52   C  C   . LEU A 17  ? 0.1032 0.1769 0.1484 0.0141  -0.0233 -0.0425 17  LEU A C   
53   O  O   . LEU A 17  ? 0.1733 0.1471 0.1508 0.0539  -0.0075 -0.0230 17  LEU A O   
54   C  CB  . LEU A 17  ? 0.1448 0.1920 0.1747 -0.0017 -0.0549 0.0089  17  LEU A CB  
55   C  CG  . LEU A 17  ? 0.1298 0.2048 0.1699 -0.0103 -0.0498 0.0098  17  LEU A CG  
56   C  CD1 . LEU A 17  ? 0.1478 0.2629 0.3275 -0.0754 -0.0520 0.0692  17  LEU A CD1 
57   C  CD2 . LEU A 17  ? 0.1663 0.2700 0.1728 0.0288  0.0069  0.0003  17  LEU A CD2 
58   N  N   . ASP A 18  ? 0.0890 0.1584 0.1482 0.0021  -0.0010 0.0026  18  ASP A N   
59   C  CA  . ASP A 18  ? 0.1165 0.1332 0.1149 -0.0065 -0.0022 -0.0152 18  ASP A CA  
60   C  C   . ASP A 18  ? 0.1252 0.1390 0.1448 -0.0072 -0.0051 0.0156  18  ASP A C   
61   O  O   . ASP A 18  ? 0.1035 0.1591 0.1441 0.0049  -0.0280 0.0079  18  ASP A O   
62   C  CB  . ASP A 18  ? 0.1131 0.1486 0.1545 -0.0066 -0.0357 -0.0156 18  ASP A CB  
63   C  CG  . ASP A 18  ? 0.1328 0.1917 0.1726 -0.0065 0.0015  0.0052  18  ASP A CG  
64   O  OD1 . ASP A 18  ? 0.1183 0.1622 0.1626 -0.0093 -0.0017 -0.0059 18  ASP A OD1 
65   O  OD2 . ASP A 18  ? 0.1291 0.1737 0.2400 -0.0162 0.0008  0.0253  18  ASP A OD2 
66   N  N   . ALA A 19  ? 0.0770 0.1230 0.1384 0.0103  -0.0058 0.0362  19  ALA A N   
67   C  CA  . ALA A 19  ? 0.0939 0.1861 0.1261 -0.0152 -0.0129 0.0348  19  ALA A CA  
68   C  C   . ALA A 19  ? 0.1106 0.1769 0.0935 -0.0013 -0.0365 0.0233  19  ALA A C   
69   O  O   . ALA A 19  ? 0.1177 0.1970 0.1452 0.0062  -0.0582 0.0086  19  ALA A O   
70   C  CB  . ALA A 19  ? 0.1886 0.1836 0.1590 -0.0089 -0.0519 0.0126  19  ALA A CB  
71   N  N   . VAL A 20  ? 0.1270 0.1393 0.1759 0.0036  -0.0144 0.0280  20  VAL A N   
72   C  CA  . VAL A 20  ? 0.1598 0.1413 0.1799 -0.0133 0.0007  0.0420  20  VAL A CA  
73   C  C   . VAL A 20  ? 0.1224 0.1847 0.2157 0.0011  0.0215  0.0471  20  VAL A C   
74   O  O   . VAL A 20  ? 0.1714 0.1858 0.3168 0.0287  0.0277  0.0290  20  VAL A O   
75   C  CB  . VAL A 20  ? 0.1735 0.1425 0.1460 -0.0314 0.0056  0.0376  20  VAL A CB  
76   C  CG1 . VAL A 20  ? 0.1969 0.1463 0.2682 0.0270  0.0226  0.0667  20  VAL A CG1 
77   C  CG2 . VAL A 20  ? 0.2299 0.1581 0.1357 0.0296  -0.0242 0.0126  20  VAL A CG2 
78   N  N   . ARG A 21  ? 0.2149 0.1655 0.1707 0.0729  0.0666  0.0295  21  ARG A N   
79   C  CA  . ARG A 21  ? 0.1672 0.1344 0.1557 0.0606  0.0424  0.0430  21  ARG A CA  
80   C  C   . ARG A 21  ? 0.1335 0.1303 0.2374 0.0393  0.0595  0.0113  21  ARG A C   
81   O  O   . ARG A 21  ? 0.1587 0.1487 0.2623 0.0336  0.0571  -0.0129 21  ARG A O   
82   C  CB  . ARG A 21  ? 0.1626 0.1925 0.2344 0.0278  0.0673  -0.0220 21  ARG A CB  
83   C  CG  . ARG A 21  ? 0.2036 0.2582 0.4427 0.0382  0.1196  0.0104  21  ARG A CG  
84   C  CD  . ARG A 21  ? 0.1423 0.4159 0.5113 0.0013  0.1668  -0.0400 21  ARG A CD  
85   N  NE  . ARG A 21  ? 0.4565 0.5961 0.5289 -0.0243 0.0072  -0.0555 21  ARG A NE  
86   C  CZ  . ARG A 21  ? 0.3866 0.4622 0.4131 -0.0574 -0.0046 -0.0334 21  ARG A CZ  
87   N  N   . GLY A 22  ? 0.1297 0.1571 0.1726 0.0182  -0.0259 0.0178  22  GLY A N   
88   C  CA  . GLY A 22  ? 0.1510 0.1583 0.1694 0.0195  0.0160  0.0004  22  GLY A CA  
89   C  C   . GLY A 22  ? 0.1511 0.1582 0.1746 0.0094  -0.0081 -0.0249 22  GLY A C   
90   O  O   . GLY A 22  ? 0.1418 0.1827 0.1397 0.0059  -0.0092 -0.0021 22  GLY A O   
91   N  N   . SER A 23  ? 0.1455 0.1806 0.1688 0.0215  0.0182  0.0250  23  SER A N   
92   C  CA  . SER A 23  ? 0.1540 0.1796 0.2027 0.0463  -0.0081 -0.0372 23  SER A CA  
93   C  C   . SER A 23  ? 0.1086 0.1517 0.1692 0.0163  -0.0363 0.0098  23  SER A C   
94   O  O   . SER A 23  ? 0.1350 0.1697 0.1542 0.0060  -0.0007 0.0124  23  SER A O   
95   C  CB  . SER A 23  ? 0.1594 0.1611 0.2308 0.0458  -0.0317 -0.0245 23  SER A CB  
96   O  OG  . SER A 23  ? 0.1965 0.2112 0.2890 0.0447  -0.0498 0.0005  23  SER A OG  
97   N  N   . PRO A 24  ? 0.0931 0.1699 0.1553 0.0307  -0.0080 -0.0096 24  PRO A N   
98   C  CA  . PRO A 24  ? 0.1069 0.1307 0.1651 0.0270  -0.0290 -0.0039 24  PRO A CA  
99   C  C   . PRO A 24  ? 0.1269 0.1556 0.1713 0.0311  -0.0154 0.0005  24  PRO A C   
100  O  O   . PRO A 24  ? 0.1047 0.1664 0.1938 0.0211  -0.0088 0.0044  24  PRO A O   
101  C  CB  . PRO A 24  ? 0.1250 0.1912 0.1776 0.0109  -0.0072 -0.0088 24  PRO A CB  
102  C  CG  . PRO A 24  ? 0.2278 0.4616 0.2034 0.1356  0.0386  -0.0149 24  PRO A CG  
103  C  CD  . PRO A 24  ? 0.1675 0.1983 0.1782 0.0222  0.0173  -0.0009 24  PRO A CD  
104  N  N   . ALA A 25  ? 0.1407 0.1279 0.1258 0.0229  -0.0045 0.0057  25  ALA A N   
105  C  CA  . ALA A 25  ? 0.1184 0.1316 0.1257 0.0338  -0.0147 0.0211  25  ALA A CA  
106  C  C   . ALA A 25  ? 0.1070 0.1806 0.1557 0.0244  -0.0229 -0.0062 25  ALA A C   
107  O  O   . ALA A 25  ? 0.1497 0.1452 0.1543 0.0167  -0.0467 -0.0017 25  ALA A O   
108  C  CB  . ALA A 25  ? 0.1878 0.2402 0.1099 0.0227  -0.0241 -0.0298 25  ALA A CB  
109  N  N   . ILE A 26  ? 0.1194 0.1894 0.2050 0.0048  -0.0119 0.0060  26  ILE A N   
110  C  CA  . ILE A 26  ? 0.1523 0.1558 0.1730 -0.0032 -0.0036 -0.0100 26  ILE A CA  
111  C  C   . ILE A 26  ? 0.1366 0.1424 0.1843 0.0374  0.0011  -0.0024 26  ILE A C   
112  O  O   . ILE A 26  ? 0.1034 0.2256 0.1729 0.0035  -0.0255 -0.0072 26  ILE A O   
113  C  CB  . ILE A 26  ? 0.2059 0.1989 0.2126 0.0080  0.0384  -0.0449 26  ILE A CB  
114  C  CG1 . ILE A 26  ? 0.1692 0.2417 0.2332 0.0721  -0.0241 -0.0352 26  ILE A CG1 
115  C  CG2 . ILE A 26  ? 0.2117 0.3037 0.2834 0.0421  -0.0028 -0.1344 26  ILE A CG2 
116  C  CD1 . ILE A 26  ? 0.2067 0.2436 0.4290 0.0607  0.0051  -0.1031 26  ILE A CD1 
117  N  N   . ASN A 27  ? 0.1420 0.1068 0.2240 0.0290  -0.0062 -0.0538 27  ASN A N   
118  C  CA  . ASN A 27  ? 0.1409 0.1322 0.2776 0.0532  -0.0524 -0.0686 27  ASN A CA  
119  C  C   . ASN A 27  ? 0.1146 0.1366 0.2241 0.0573  -0.0493 0.0089  27  ASN A C   
120  O  O   . ASN A 27  ? 0.1961 0.1746 0.2722 -0.0095 -0.0374 -0.0036 27  ASN A O   
121  C  CB  . ASN A 27  ? 0.1377 0.1236 0.2467 0.0499  -0.0832 -0.0271 27  ASN A CB  
122  C  CG  . ASN A 27  ? 0.2271 0.2035 0.2348 0.0718  -0.1220 -0.0949 27  ASN A CG  
123  O  OD1 . ASN A 27  ? 0.2717 0.1784 0.4926 0.0282  -0.0427 -0.1048 27  ASN A OD1 
124  N  ND2 . ASN A 27  ? 0.2089 0.2613 0.2897 0.0733  -0.1303 -0.0720 27  ASN A ND2 
125  N  N   . VAL A 28  ? 0.1399 0.1794 0.1807 0.0149  -0.0203 -0.0089 28  VAL A N   
126  C  CA  . VAL A 28  ? 0.1468 0.1674 0.1499 0.0086  0.0032  0.0194  28  VAL A CA  
127  C  C   . VAL A 28  ? 0.1386 0.1536 0.1779 -0.0029 -0.0228 -0.0223 28  VAL A C   
128  O  O   . VAL A 28  ? 0.1253 0.1469 0.1871 -0.0135 -0.0051 -0.0201 28  VAL A O   
129  C  CB  . VAL A 28  ? 0.2281 0.2543 0.1929 0.0977  -0.0489 -0.1058 28  VAL A CB  
130  C  CG1 . VAL A 28  ? 0.1456 0.3705 0.2177 0.1290  -0.0556 -0.1339 28  VAL A CG1 
131  C  CG2 . VAL A 28  ? 0.3311 0.3427 0.3403 0.1448  -0.0674 -0.0172 28  VAL A CG2 
132  N  N   . ALA A 29  ? 0.1435 0.1327 0.1401 0.0301  -0.0046 0.0096  29  ALA A N   
133  C  CA  . ALA A 29  ? 0.0940 0.1411 0.1522 0.0033  -0.0664 -0.0335 29  ALA A CA  
134  C  C   . ALA A 29  ? 0.1338 0.1442 0.1421 0.0087  -0.0563 -0.0419 29  ALA A C   
135  O  O   . ALA A 29  ? 0.1668 0.1720 0.1443 0.0060  -0.0601 -0.0184 29  ALA A O   
136  C  CB  . ALA A 29  ? 0.0874 0.1688 0.2571 0.0055  -0.0243 -0.0519 29  ALA A CB  
137  N  N   . VAL A 30  ? 0.1193 0.1267 0.1624 0.0103  -0.0604 -0.0291 30  VAL A N   
138  C  CA  . VAL A 30  ? 0.1664 0.1328 0.1479 0.0164  -0.0717 -0.0221 30  VAL A CA  
139  C  C   . VAL A 30  ? 0.1312 0.1192 0.1464 0.0137  -0.0200 -0.0233 30  VAL A C   
140  O  O   . VAL A 30  ? 0.1265 0.1281 0.1688 0.0228  -0.0582 -0.0095 30  VAL A O   
141  C  CB  . VAL A 30  ? 0.1339 0.1392 0.1940 0.0148  -0.0506 -0.0206 30  VAL A CB  
142  C  CG1 . VAL A 30  ? 0.1722 0.1181 0.2635 -0.0110 -0.0444 -0.0115 30  VAL A CG1 
143  C  CG2 . VAL A 30  ? 0.0839 0.2252 0.2000 0.0215  -0.0049 -0.0185 30  VAL A CG2 
144  N  N   . HIS A 31  ? 0.1620 0.1220 0.0998 0.0378  -0.0408 -0.0068 31  HIS A N   
145  C  CA  . HIS A 31  ? 0.1494 0.1009 0.1500 0.0306  -0.0288 -0.0149 31  HIS A CA  
146  C  C   . HIS A 31  ? 0.1306 0.1200 0.2096 0.0020  -0.0496 -0.0137 31  HIS A C   
147  O  O   . HIS A 31  ? 0.2777 0.1314 0.2295 0.0052  -0.0859 0.0000  31  HIS A O   
148  C  CB  . HIS A 31  ? 0.1895 0.1641 0.2417 0.0055  0.0325  -0.0255 31  HIS A CB  
149  C  CG  . HIS A 31  ? 0.2925 0.1905 0.3317 -0.0307 0.1102  -0.0610 31  HIS A CG  
150  N  ND1 . HIS A 31  ? 0.2638 0.2755 0.3810 -0.1054 0.1395  -0.1760 31  HIS A ND1 
151  C  CD2 . HIS A 31  ? 0.3380 0.1914 0.4467 -0.0350 0.2403  -0.0986 31  HIS A CD2 
152  C  CE1 . HIS A 31  ? 0.3528 0.2577 0.4902 -0.1920 0.2785  -0.1521 31  HIS A CE1 
153  N  NE2 . HIS A 31  ? 0.4909 0.2900 0.5063 -0.1045 0.1844  -0.1675 31  HIS A NE2 
154  N  N   . VAL A 32  ? 0.1039 0.1092 0.1768 -0.0019 -0.0653 -0.0254 32  VAL A N   
155  C  CA  . VAL A 32  ? 0.1496 0.1079 0.1580 0.0112  -0.0634 -0.0182 32  VAL A CA  
156  C  C   . VAL A 32  ? 0.1564 0.1542 0.1478 0.0172  -0.0472 0.0273  32  VAL A C   
157  O  O   . VAL A 32  ? 0.1433 0.0873 0.2151 0.0056  -0.0472 0.0004  32  VAL A O   
158  C  CB  . VAL A 32  ? 0.1316 0.0941 0.1790 0.0266  -0.0514 -0.0069 32  VAL A CB  
159  C  CG1 . VAL A 32  ? 0.1850 0.1088 0.1428 0.0093  -0.0025 -0.0414 32  VAL A CG1 
160  C  CG2 . VAL A 32  ? 0.1627 0.1028 0.2343 0.0257  -0.0215 -0.0174 32  VAL A CG2 
161  N  N   . PHE A 33  ? 0.1227 0.1531 0.1671 0.0008  -0.0689 -0.0067 33  PHE A N   
162  C  CA  . PHE A 33  ? 0.1431 0.1459 0.1886 0.0060  -0.0136 -0.0121 33  PHE A CA  
163  C  C   . PHE A 33  ? 0.0981 0.1555 0.2660 0.0087  -0.0394 -0.0220 33  PHE A C   
164  O  O   . PHE A 33  ? 0.0994 0.1363 0.2325 0.0095  -0.0441 -0.0021 33  PHE A O   
165  C  CB  . PHE A 33  ? 0.0909 0.1301 0.1735 0.0046  -0.0209 -0.0252 33  PHE A CB  
166  C  CG  . PHE A 33  ? 0.1528 0.1403 0.1578 0.0120  0.0253  -0.0629 33  PHE A CG  
167  C  CD1 . PHE A 33  ? 0.1227 0.1450 0.2877 -0.0144 0.0027  0.0179  33  PHE A CD1 
168  C  CD2 . PHE A 33  ? 0.1562 0.1838 0.3221 -0.0031 -0.0403 -0.0073 33  PHE A CD2 
169  C  CE1 . PHE A 33  ? 0.2029 0.1504 0.2200 0.0015  -0.0291 -0.0010 33  PHE A CE1 
170  C  CE2 . PHE A 33  ? 0.2442 0.1801 0.2848 -0.0035 -0.0042 0.0031  33  PHE A CE2 
171  C  CZ  . PHE A 33  ? 0.2510 0.1081 0.1795 -0.0457 -0.0126 0.0259  33  PHE A CZ  
172  N  N   . ARG A 34  ? 0.1298 0.1182 0.1826 0.0026  -0.0882 -0.0237 34  ARG A N   
173  C  CA  . ARG A 34  ? 0.1083 0.1302 0.2087 0.0046  -0.0298 -0.0411 34  ARG A CA  
174  C  C   . ARG A 34  ? 0.1519 0.1491 0.1590 0.0179  -0.0252 -0.0113 34  ARG A C   
175  O  O   . ARG A 34  ? 0.1549 0.1630 0.2240 -0.0073 -0.0236 -0.0346 34  ARG A O   
176  C  CB  . ARG A 34  ? 0.1779 0.1475 0.2091 0.0398  -0.0301 -0.0360 34  ARG A CB  
177  C  CG  . ARG A 34  ? 0.2839 0.1856 0.1786 -0.0356 -0.0386 -0.0237 34  ARG A CG  
178  C  CD  . ARG A 34  ? 0.4045 0.2306 0.1264 -0.0035 0.0314  0.0387  34  ARG A CD  
179  N  NE  . ARG A 34  ? 0.3703 0.3811 0.2819 0.1479  0.0089  0.0162  34  ARG A NE  
180  C  CZ  . ARG A 34  ? 0.2142 0.3604 0.2555 0.1338  -0.0119 0.1288  34  ARG A CZ  
181  N  NH1 . ARG A 34  ? 0.3288 0.1755 0.3502 0.0892  0.0779  -0.0140 34  ARG A NH1 
182  N  NH2 . ARG A 34  ? 0.2125 0.4564 0.2443 0.0299  0.0052  0.0610  34  ARG A NH2 
183  N  N   . LYS A 35  ? 0.0991 0.1864 0.2028 0.0080  0.0052  -0.0457 35  LYS A N   
184  C  CA  . LYS A 35  ? 0.1695 0.2715 0.1709 0.0215  0.0254  -0.0375 35  LYS A CA  
185  C  C   . LYS A 35  ? 0.3068 0.1687 0.2833 0.0300  0.0254  0.0087  35  LYS A C   
186  O  O   . LYS A 35  ? 0.2670 0.2306 0.1468 0.0265  -0.0141 0.0196  35  LYS A O   
187  C  CB  . LYS A 35  ? 0.1556 0.2456 0.1661 0.0203  -0.0454 0.0230  35  LYS A CB  
188  C  CG  . LYS A 35  ? 0.2747 0.3617 0.2579 -0.0645 0.0497  -0.0205 35  LYS A CG  
189  C  CD  . LYS A 35  ? 0.4243 0.4736 0.1583 -0.0300 0.0304  -0.0546 35  LYS A CD  
190  N  N   . ALA A 36  ? 0.3328 0.2330 0.2152 0.0036  -0.0366 0.0040  36  ALA A N   
191  C  CA  . ALA A 36  ? 0.2637 0.2985 0.3144 -0.0078 -0.0388 -0.1568 36  ALA A CA  
192  C  C   . ALA A 36  ? 0.3961 0.3481 0.3050 -0.1032 0.0213  -0.2213 36  ALA A C   
193  O  O   . ALA A 36  ? 0.4246 0.3318 0.3454 0.0722  -0.0703 -0.1817 36  ALA A O   
194  C  CB  . ALA A 36  ? 0.3437 0.3605 0.5341 -0.1147 -0.2462 0.0404  36  ALA A CB  
195  N  N   . ALA A 37  ? 0.4795 0.4284 0.4435 -0.1053 -0.0206 -0.0828 37  ALA A N   
196  C  CA  . ALA A 37  ? 0.4051 0.4035 0.3794 0.0016  0.1060  0.0382  37  ALA A CA  
197  C  C   . ALA A 37  ? 0.6262 0.4170 0.2588 0.0795  -0.0801 0.0057  37  ALA A C   
198  O  O   . ALA A 37  ? 0.4600 0.3691 0.4702 0.0700  0.0149  -0.1244 37  ALA A O   
199  C  CB  . ALA A 37  ? 0.5085 0.2700 0.3919 0.0813  0.0733  0.0246  37  ALA A CB  
200  N  N   . THR A 40  ? 0.5226 0.3560 0.4588 0.0428  0.0606  -0.0439 40  THR A N   
201  C  CA  . THR A 40  ? 0.3729 0.3935 0.3815 -0.0493 -0.0622 -0.0731 40  THR A CA  
202  C  C   . THR A 40  ? 0.4017 0.4096 0.3557 -0.0563 -0.0175 -0.0071 40  THR A C   
203  O  O   . THR A 40  ? 0.4814 0.3496 0.3694 -0.0734 0.1693  -0.0139 40  THR A O   
204  C  CB  . THR A 40  ? 0.3353 0.2569 0.4172 -0.0631 0.0470  -0.0551 40  THR A CB  
205  O  OG1 . THR A 40  ? 0.4124 0.3492 0.6468 -0.0082 0.0669  0.0286  40  THR A OG1 
206  C  CG2 . THR A 40  ? 0.3426 0.5094 0.5531 -0.0331 0.0701  -0.0443 40  THR A CG2 
207  N  N   . TRP A 41  ? 0.3098 0.3883 0.3860 -0.0073 -0.0061 -0.0669 41  TRP A N   
208  C  CA  . TRP A 41  ? 0.3364 0.2573 0.3735 -0.0434 0.0428  0.0467  41  TRP A CA  
209  C  C   . TRP A 41  ? 0.2608 0.3593 0.4099 -0.0395 0.0534  -0.0105 41  TRP A C   
210  O  O   . TRP A 41  ? 0.4889 0.4788 0.4258 -0.1776 0.1505  0.0450  41  TRP A O   
211  C  CB  . TRP A 41  ? 0.2951 0.2383 0.3176 -0.0459 0.0720  -0.0117 41  TRP A CB  
212  C  CG  . TRP A 41  ? 0.3381 0.2253 0.2957 0.0047  0.0661  0.0278  41  TRP A CG  
213  C  CD1 . TRP A 41  ? 0.4232 0.3745 0.2450 -0.0107 0.0198  0.0029  41  TRP A CD1 
214  C  CD2 . TRP A 41  ? 0.3312 0.3846 0.3059 -0.0557 0.0686  0.0930  41  TRP A CD2 
215  N  NE1 . TRP A 41  ? 0.4874 0.4228 0.2062 -0.0458 0.0215  -0.0193 41  TRP A NE1 
216  C  CE2 . TRP A 41  ? 0.3402 0.3900 0.4173 -0.0457 0.0184  0.0457  41  TRP A CE2 
217  C  CE3 . TRP A 41  ? 0.3017 0.1511 0.2460 -0.0300 0.0474  0.0324  41  TRP A CE3 
218  C  CZ2 . TRP A 41  ? 0.4234 0.3713 0.2194 -0.0941 0.0013  0.0312  41  TRP A CZ2 
219  C  CZ3 . TRP A 41  ? 0.2121 0.1659 0.2495 0.0414  0.0147  0.0767  41  TRP A CZ3 
220  C  CH2 . TRP A 41  ? 0.2268 0.2104 0.2745 0.0084  -0.0257 0.0933  41  TRP A CH2 
221  N  N   . GLU A 42  ? 0.1871 0.3488 0.2561 -0.1194 0.0685  -0.1679 42  GLU A N   
222  C  CA  . GLU A 42  ? 0.1759 0.2728 0.2633 -0.0124 -0.0228 -0.0938 42  GLU A CA  
223  C  C   . GLU A 42  ? 0.1801 0.1708 0.2910 -0.0412 0.0264  -0.0277 42  GLU A C   
224  O  O   . GLU A 42  ? 0.1353 0.1822 0.2211 -0.0112 -0.0356 0.0042  42  GLU A O   
225  C  CB  . GLU A 42  ? 0.2001 0.1151 0.6339 0.0422  0.1732  0.0121  42  GLU A CB  
226  N  N   . PRO A 43  ? 0.1278 0.1982 0.2142 -0.0335 0.0000  -0.0336 43  PRO A N   
227  C  CA  . PRO A 43  ? 0.1782 0.1734 0.2214 -0.0196 0.0004  -0.0590 43  PRO A CA  
228  C  C   . PRO A 43  ? 0.1601 0.1538 0.2336 0.0063  -0.0469 -0.0348 43  PRO A C   
229  O  O   . PRO A 43  ? 0.1876 0.2514 0.2470 0.0204  -0.0507 0.0031  43  PRO A O   
230  C  CB  . PRO A 43  ? 0.1754 0.2594 0.3280 -0.0727 -0.0039 -0.0945 43  PRO A CB  
231  C  CG  . PRO A 43  ? 0.2969 0.3956 0.4188 -0.0188 -0.0459 -0.0693 43  PRO A CG  
232  C  CD  . PRO A 43  ? 0.1921 0.3596 0.4719 -0.1354 0.0321  -0.1606 43  PRO A CD  
233  N  N   . PHE A 44  ? 0.1495 0.1568 0.1759 0.0117  -0.0589 0.0063  44  PHE A N   
234  C  CA  . PHE A 44  ? 0.1626 0.1344 0.1733 0.0540  -0.0511 -0.0062 44  PHE A CA  
235  C  C   . PHE A 44  ? 0.1430 0.1069 0.2010 -0.0040 -0.0443 -0.0344 44  PHE A C   
236  O  O   . PHE A 44  ? 0.1922 0.1307 0.2123 0.0109  -0.0561 0.0032  44  PHE A O   
237  C  CB  . PHE A 44  ? 0.1511 0.1507 0.2323 0.0091  -0.0373 0.0179  44  PHE A CB  
238  C  CG  . PHE A 44  ? 0.1583 0.1173 0.1287 0.0157  -0.0653 0.0095  44  PHE A CG  
239  C  CD1 . PHE A 44  ? 0.1480 0.1436 0.1991 0.0300  -0.0133 0.0695  44  PHE A CD1 
240  C  CD2 . PHE A 44  ? 0.1606 0.1376 0.2045 -0.0277 -0.0156 -0.0036 44  PHE A CD2 
241  C  CE1 . PHE A 44  ? 0.1728 0.1718 0.1194 -0.0055 -0.0529 0.0347  44  PHE A CE1 
242  C  CE2 . PHE A 44  ? 0.2208 0.1137 0.2094 -0.0306 0.0114  -0.0253 44  PHE A CE2 
243  C  CZ  . PHE A 44  ? 0.2308 0.1480 0.1520 -0.0308 -0.0015 -0.0358 44  PHE A CZ  
244  N  N   . ALA A 45  ? 0.1867 0.1408 0.1493 0.0087  -0.0826 -0.0022 45  ALA A N   
245  C  CA  . ALA A 45  ? 0.1773 0.1932 0.1594 0.0278  -0.0714 -0.0125 45  ALA A CA  
246  C  C   . ALA A 45  ? 0.1362 0.1620 0.1583 0.0233  -0.0537 -0.0298 45  ALA A C   
247  O  O   . ALA A 45  ? 0.2032 0.1356 0.1782 0.0230  -0.0498 -0.0447 45  ALA A O   
248  C  CB  . ALA A 45  ? 0.1952 0.1897 0.2905 0.0524  -0.0181 0.0245  45  ALA A CB  
249  N  N   . SER A 46  ? 0.1634 0.1250 0.2311 0.0205  -0.1105 -0.0382 46  SER A N   
250  C  CA  . SER A 46  ? 0.0945 0.1430 0.1692 0.0358  -0.0514 -0.0151 46  SER A CA  
251  C  C   . SER A 46  ? 0.1593 0.1493 0.1136 0.0208  -0.0431 0.0013  46  SER A C   
252  O  O   . SER A 46  ? 0.1824 0.1696 0.1264 0.0212  -0.0825 -0.0113 46  SER A O   
253  C  CB  . SER A 46  ? 0.1013 0.1573 0.1972 0.0390  -0.0442 -0.0465 46  SER A CB  
254  O  OG  . SER A 46  ? 0.1238 0.1886 0.1835 0.0190  -0.0615 -0.0322 46  SER A OG  
255  N  N   . GLY A 47  ? 0.1242 0.1747 0.1235 0.0287  -0.0376 -0.0054 47  GLY A N   
256  C  CA  . GLY A 47  ? 0.1478 0.1699 0.1217 0.0249  -0.0223 0.0075  47  GLY A CA  
257  C  C   . GLY A 47  ? 0.0954 0.1708 0.1108 0.0182  -0.0148 0.0007  47  GLY A C   
258  O  O   . GLY A 47  ? 0.1117 0.1577 0.1302 0.0191  -0.0130 -0.0138 47  GLY A O   
259  N  N   . LYS A 48  ? 0.1224 0.1311 0.1758 0.0003  -0.0004 -0.0070 48  LYS A N   
260  C  CA  . LYS A 48  ? 0.1509 0.1769 0.1424 0.0257  -0.0219 -0.0280 48  LYS A CA  
261  C  C   . LYS A 48  ? 0.1529 0.1703 0.1416 0.0077  -0.0413 0.0112  48  LYS A C   
262  O  O   . LYS A 48  ? 0.1368 0.1925 0.1518 0.0249  -0.0201 0.0039  48  LYS A O   
263  C  CB  . LYS A 48  ? 0.1845 0.1796 0.2500 0.0219  -0.0032 -0.0165 48  LYS A CB  
264  C  CG  . LYS A 48  ? 0.1904 0.1515 0.3356 -0.0231 0.0077  -0.0802 48  LYS A CG  
265  C  CD  . LYS A 48  ? 0.2872 0.2285 0.3076 -0.0300 -0.0401 0.1368  48  LYS A CD  
266  C  CE  . LYS A 48  ? 0.4440 0.2684 0.3506 -0.0842 0.0683  -0.0114 48  LYS A CE  
267  N  NZ  . LYS A 48  ? 0.3970 0.3922 0.6849 -0.0572 0.0514  0.0934  48  LYS A NZ  
268  N  N   . THR A 49  ? 0.1356 0.1716 0.1094 0.0325  -0.0127 -0.0070 49  THR A N   
269  C  CA  . THR A 49  ? 0.1464 0.2001 0.1414 0.0434  -0.0108 0.0098  49  THR A CA  
270  C  C   . THR A 49  ? 0.1543 0.1268 0.2247 0.0201  0.0021  0.0092  49  THR A C   
271  O  O   . THR A 49  ? 0.1265 0.1318 0.2221 0.0484  -0.0540 0.0199  49  THR A O   
272  C  CB  . THR A 49  ? 0.1387 0.1796 0.1276 0.0302  -0.0094 0.0261  49  THR A CB  
273  O  OG1 . THR A 49  ? 0.1296 0.1375 0.1797 0.0377  0.0144  0.0129  49  THR A OG1 
274  C  CG2 . THR A 49  ? 0.1587 0.1780 0.1569 0.0099  -0.0245 -0.0015 49  THR A CG2 
275  N  N   . SER A 50  ? 0.1507 0.1106 0.1636 0.0142  -0.0427 -0.0120 50  SER A N   
276  C  CA  . SER A 50  ? 0.1193 0.1619 0.1622 0.0135  -0.0281 -0.0328 50  SER A CA  
277  C  C   . SER A 50  ? 0.1289 0.1700 0.1489 0.0200  0.0162  -0.0074 50  SER A C   
278  O  O   . SER A 50  ? 0.1495 0.1626 0.1771 0.0074  -0.0081 -0.0175 50  SER A O   
279  C  CB  . SER A 50  ? 0.1899 0.1678 0.1985 0.0161  -0.0125 -0.0230 50  SER A CB  
280  O  OG  . SER A 50  ? 0.1951 0.2069 0.1698 0.0028  -0.0122 0.0063  50  SER A OG  
281  N  N   . GLU A 51  ? 0.1997 0.2153 0.1908 0.0534  0.0144  -0.0468 51  GLU A N   
282  C  CA  . GLU A 51  ? 0.1592 0.2083 0.1980 0.0160  0.0218  -0.0036 51  GLU A CA  
283  C  C   . GLU A 51  ? 0.2121 0.1912 0.1734 0.0389  0.0004  -0.0348 51  GLU A C   
284  O  O   . GLU A 51  ? 0.2271 0.2580 0.2382 0.0647  0.0073  0.0626  51  GLU A O   
285  C  CB  . GLU A 51  ? 0.2254 0.2679 0.2512 0.0529  -0.0014 -0.0749 51  GLU A CB  
286  C  CG  . GLU A 51  ? 0.3663 0.2859 0.3021 0.0167  -0.0013 -0.0721 51  GLU A CG  
287  C  CD  . GLU A 51  ? 0.5925 0.4289 0.2646 0.0502  -0.0746 -0.1394 51  GLU A CD  
288  N  N   . SER A 52  ? 0.1540 0.1951 0.1804 0.0353  0.0209  -0.0186 52  SER A N   
289  C  CA  . SER A 52  ? 0.1479 0.2155 0.1669 0.0118  0.0095  -0.0199 52  SER A CA  
290  C  C   . SER A 52  ? 0.1703 0.1880 0.1332 -0.0008 0.0006  0.0212  52  SER A C   
291  O  O   . SER A 52  ? 0.1908 0.2002 0.1905 -0.0291 0.0000  0.0478  52  SER A O   
292  C  CB  . SER A 52  ? 0.2804 0.3145 0.2888 -0.0393 -0.0222 0.0914  52  SER A CB  
293  O  OG  . SER A 52  ? 0.3058 0.4384 0.3237 -0.1069 -0.1233 0.1055  52  SER A OG  
294  N  N   . GLY A 53  ? 0.1632 0.1742 0.1443 0.0110  -0.0042 -0.0305 53  GLY A N   
295  C  CA  . GLY A 53  ? 0.1696 0.1293 0.1617 0.0023  0.0076  -0.0039 53  GLY A CA  
296  C  C   . GLY A 53  ? 0.1790 0.1543 0.1050 0.0214  -0.0232 0.0084  53  GLY A C   
297  O  O   . GLY A 53  ? 0.1891 0.1707 0.1918 0.0277  -0.0230 -0.0212 53  GLY A O   
298  N  N   . GLU A 54  ? 0.2127 0.1905 0.0988 0.0481  -0.0077 0.0077  54  GLU A N   
299  C  CA  . GLU A 54  ? 0.2142 0.1588 0.1259 0.0239  0.0136  -0.0256 54  GLU A CA  
300  C  C   . GLU A 54  ? 0.2138 0.1158 0.1510 0.0118  0.0185  -0.0411 54  GLU A C   
301  O  O   . GLU A 54  ? 0.2186 0.1462 0.1574 -0.0195 -0.0399 -0.0156 54  GLU A O   
302  C  CB  . GLU A 54  ? 0.1512 0.2200 0.2674 0.0360  0.0236  0.0277  54  GLU A CB  
303  C  CG  . GLU A 54  ? 0.2333 0.2507 0.1950 -0.0319 -0.0479 0.0048  54  GLU A CG  
304  C  CD  . GLU A 54  ? 0.3166 0.3053 0.3497 -0.0305 0.1268  -0.0080 54  GLU A CD  
305  O  OE1 . GLU A 54  ? 0.4295 0.3186 0.4772 -0.0767 0.0620  0.0348  54  GLU A OE1 
306  O  OE2 . GLU A 54  ? 0.4215 0.5093 0.4530 -0.0041 0.2417  -0.0373 54  GLU A OE2 
307  N  N   . LEU A 55  ? 0.1492 0.1352 0.1989 0.0164  -0.0145 -0.0270 55  LEU A N   
308  C  CA  . LEU A 55  ? 0.1421 0.1764 0.2249 -0.0156 -0.0297 -0.0128 55  LEU A CA  
309  C  C   . LEU A 55  ? 0.2009 0.1666 0.2562 -0.0214 -0.0264 -0.0426 55  LEU A C   
310  O  O   . LEU A 55  ? 0.2037 0.1466 0.2424 0.0011  -0.0284 -0.0226 55  LEU A O   
311  C  CB  . LEU A 55  ? 0.2123 0.1390 0.2253 -0.0060 -0.0123 -0.0434 55  LEU A CB  
312  C  CG  . LEU A 55  ? 0.2120 0.1843 0.2212 0.0283  0.0085  -0.0521 55  LEU A CG  
313  C  CD1 . LEU A 55  ? 0.2496 0.2684 0.1791 0.0638  0.0003  -0.0596 55  LEU A CD1 
314  C  CD2 . LEU A 55  ? 0.2638 0.2536 0.2884 0.0472  0.0710  0.1002  55  LEU A CD2 
315  N  N   . HIS A 56  ? 0.2911 0.2875 0.2107 0.0909  -0.0281 0.0089  56  HIS A N   
316  C  CA  . HIS A 56  ? 0.2190 0.3559 0.3033 0.1359  0.0265  0.0455  56  HIS A CA  
317  C  C   . HIS A 56  ? 0.2679 0.3428 0.2673 0.0531  -0.0306 0.0715  56  HIS A C   
318  O  O   . HIS A 56  ? 0.3832 0.3771 0.2682 -0.0121 -0.0493 0.0794  56  HIS A O   
319  C  CB  . HIS A 56  ? 0.3270 0.4907 0.2252 0.0433  0.0197  0.0406  56  HIS A CB  
320  C  CG  . HIS A 56  ? 0.3037 0.4517 0.4924 -0.0002 0.0275  0.1484  56  HIS A CG  
321  N  ND1 . HIS A 56  ? 0.3019 0.5108 0.5798 0.0064  -0.0256 0.1230  56  HIS A ND1 
322  C  CD2 . HIS A 56  ? 0.3856 0.4628 0.6150 0.0346  -0.0120 0.0805  56  HIS A CD2 
323  C  CE1 . HIS A 56  ? 0.2858 0.3685 0.7414 -0.0869 -0.0396 0.0878  56  HIS A CE1 
324  N  NE2 . HIS A 56  ? 0.4269 0.3662 0.5050 0.0122  0.0218  0.1199  56  HIS A NE2 
325  N  N   . GLY A 57  ? 0.2614 0.2888 0.3734 0.0713  0.0296  0.0262  57  GLY A N   
326  C  CA  . GLY A 57  ? 0.2474 0.2900 0.3588 -0.0251 -0.0157 -0.0013 57  GLY A CA  
327  C  C   . GLY A 57  ? 0.2431 0.2099 0.2918 -0.0185 -0.0358 -0.0524 57  GLY A C   
328  O  O   . GLY A 57  ? 0.2688 0.2756 0.3111 0.0059  -0.0928 -0.0453 57  GLY A O   
329  N  N   . LEU A 58  ? 0.1831 0.1987 0.2744 0.0273  -0.0023 -0.0431 58  LEU A N   
330  C  CA  . LEU A 58  ? 0.1749 0.2507 0.1850 0.0080  -0.0695 -0.0494 58  LEU A CA  
331  C  C   . LEU A 58  ? 0.2215 0.2590 0.2914 0.0215  -0.0356 -0.0410 58  LEU A C   
332  O  O   . LEU A 58  ? 0.2123 0.3532 0.3173 -0.0080 -0.0664 -0.0709 58  LEU A O   
333  C  CB  . LEU A 58  ? 0.2260 0.2772 0.1881 -0.0241 -0.0903 -0.0173 58  LEU A CB  
334  C  CG  . LEU A 58  ? 0.2385 0.1814 0.3135 -0.0646 -0.0646 -0.0106 58  LEU A CG  
335  C  CD1 . LEU A 58  ? 0.2478 0.2208 0.3855 -0.0345 -0.0794 -0.0693 58  LEU A CD1 
336  C  CD2 . LEU A 58  ? 0.2140 0.1148 0.4409 0.0027  0.0082  0.0493  58  LEU A CD2 
337  N  N   . THR A 59  ? 0.2380 0.2484 0.2545 0.0492  -0.0302 -0.0178 59  THR A N   
338  C  CA  . THR A 59  ? 0.1760 0.2774 0.2176 0.0440  -0.0518 -0.0243 59  THR A CA  
339  C  C   . THR A 59  ? 0.2992 0.2479 0.2006 0.0804  -0.0033 -0.0461 59  THR A C   
340  O  O   . THR A 59  ? 0.2525 0.3213 0.2703 0.1015  -0.0445 -0.0867 59  THR A O   
341  C  CB  . THR A 59  ? 0.2506 0.2777 0.2216 0.0785  -0.1091 -0.0063 59  THR A CB  
342  O  OG1 . THR A 59  ? 0.2648 0.3532 0.2102 0.1318  -0.0654 -0.0310 59  THR A OG1 
343  C  CG2 . THR A 59  ? 0.1919 0.3134 0.2744 0.0555  -0.0625 -0.0772 59  THR A CG2 
344  N  N   . THR A 60  ? 0.2209 0.3189 0.2033 0.0798  -0.0035 -0.0017 60  THR A N   
345  C  CA  . THR A 60  ? 0.2330 0.2758 0.1118 0.0775  0.0227  -0.0540 60  THR A CA  
346  C  C   . THR A 60  ? 0.2249 0.2405 0.2363 0.0421  -0.0374 -0.0311 60  THR A C   
347  O  O   . THR A 60  ? 0.2261 0.3227 0.2066 0.1533  -0.0654 -0.0054 60  THR A O   
348  C  CB  . THR A 60  ? 0.2405 0.3453 0.2109 -0.0024 -0.0263 -0.1049 60  THR A CB  
349  O  OG1 . THR A 60  ? 0.2437 0.3693 0.2523 0.0674  -0.0386 -0.0816 60  THR A OG1 
350  C  CG2 . THR A 60  ? 0.3435 0.2857 0.2869 0.0278  -0.0312 -0.1101 60  THR A CG2 
351  N  N   . GLU A 61  ? 0.1439 0.3014 0.2697 0.0762  0.0020  0.0378  61  GLU A N   
352  C  CA  . GLU A 61  ? 0.2130 0.3275 0.3525 0.0742  -0.0408 0.0136  61  GLU A CA  
353  C  C   . GLU A 61  ? 0.2160 0.2756 0.2898 0.0401  -0.0049 -0.0497 61  GLU A C   
354  O  O   . GLU A 61  ? 0.2030 0.2570 0.2707 0.0350  0.0216  -0.0063 61  GLU A O   
355  C  CB  . GLU A 61  ? 0.2486 0.3225 0.4065 0.0269  0.0342  -0.0232 61  GLU A CB  
356  C  CG  . GLU A 61  ? 0.3094 0.5042 0.4788 -0.0727 0.0289  -0.0023 61  GLU A CG  
357  C  CD  . GLU A 61  ? 0.5288 0.4604 0.3633 -0.0493 0.0888  0.0220  61  GLU A CD  
358  N  N   . GLU A 62  ? 0.1862 0.2703 0.1874 0.0437  0.0062  0.0287  62  GLU A N   
359  C  CA  . GLU A 62  ? 0.1941 0.3277 0.3111 0.0518  0.0316  -0.0040 62  GLU A CA  
360  C  C   . GLU A 62  ? 0.2193 0.1443 0.3054 -0.0049 0.0014  -0.0011 62  GLU A C   
361  O  O   . GLU A 62  ? 0.2090 0.2385 0.3767 0.0484  0.0108  -0.0217 62  GLU A O   
362  C  CB  . GLU A 62  ? 0.2262 0.4218 0.3322 0.0036  0.0182  0.1085  62  GLU A CB  
363  C  CG  . GLU A 62  ? 0.3512 0.5078 0.3254 0.0651  0.0483  0.0795  62  GLU A CG  
364  C  CD  . GLU A 62  ? 0.4561 0.3334 0.4151 0.0724  0.0915  0.0287  62  GLU A CD  
365  O  OE1 . GLU A 62  ? 0.3923 0.3521 0.3731 0.1189  -0.0221 0.0377  62  GLU A OE1 
366  O  OE2 . GLU A 62  ? 0.4349 0.5835 0.5557 0.0773  0.1306  0.1503  62  GLU A OE2 
367  N  N   . GLU A 63  ? 0.1202 0.1860 0.2387 0.0304  -0.0489 0.0108  63  GLU A N   
368  C  CA  . GLU A 63  ? 0.1810 0.1636 0.2152 0.0140  -0.0326 -0.0211 63  GLU A CA  
369  C  C   . GLU A 63  ? 0.1368 0.1568 0.2001 0.0070  0.0013  -0.0411 63  GLU A C   
370  O  O   . GLU A 63  ? 0.1369 0.1734 0.1796 -0.0048 -0.0231 0.0076  63  GLU A O   
371  C  CB  . GLU A 63  ? 0.1871 0.1644 0.2195 0.0493  -0.0510 -0.0038 63  GLU A CB  
372  C  CG  . GLU A 63  ? 0.2974 0.1687 0.2093 0.0454  -0.0980 0.0215  63  GLU A CG  
373  C  CD  . GLU A 63  ? 0.3168 0.1830 0.3132 0.0224  -0.0060 -0.0249 63  GLU A CD  
374  O  OE1 . GLU A 63  ? 0.3344 0.3021 0.3393 0.0891  -0.0212 -0.1004 63  GLU A OE1 
375  O  OE2 . GLU A 63  ? 0.3624 0.2106 0.4227 -0.0428 -0.0165 0.0479  63  GLU A OE2 
376  N  N   . PHE A 64  ? 0.1617 0.2048 0.1900 0.0159  -0.0470 -0.0194 64  PHE A N   
377  C  CA  . PHE A 64  ? 0.1379 0.1948 0.1989 0.0102  -0.0345 -0.0329 64  PHE A CA  
378  C  C   . PHE A 64  ? 0.1641 0.1618 0.2127 0.0049  0.0250  0.0407  64  PHE A C   
379  O  O   . PHE A 64  ? 0.2697 0.1831 0.2914 -0.0517 0.1126  -0.0439 64  PHE A O   
380  C  CB  . PHE A 64  ? 0.1506 0.1527 0.2052 0.0077  -0.0274 -0.0185 64  PHE A CB  
381  C  CG  . PHE A 64  ? 0.1452 0.1793 0.1896 -0.0017 -0.0120 -0.0308 64  PHE A CG  
382  C  CD1 . PHE A 64  ? 0.1816 0.0411 0.1365 0.0068  -0.0307 -0.0417 64  PHE A CD1 
383  C  CD2 . PHE A 64  ? 0.1653 0.2053 0.1592 -0.0099 -0.0101 0.0470  64  PHE A CD2 
384  C  CE1 . PHE A 64  ? 0.1465 0.2218 0.1788 0.0019  -0.0155 -0.0271 64  PHE A CE1 
385  C  CE2 . PHE A 64  ? 0.1556 0.3339 0.1818 -0.0376 -0.0331 0.0025  64  PHE A CE2 
386  C  CZ  . PHE A 64  ? 0.1691 0.1961 0.2833 0.0016  -0.0058 0.0390  64  PHE A CZ  
387  N  N   . VAL A 65  ? 0.1395 0.1235 0.1866 0.0229  -0.0044 0.0326  65  VAL A N   
388  C  CA  . VAL A 65  ? 0.1440 0.1004 0.1457 -0.0043 -0.0321 0.0325  65  VAL A CA  
389  C  C   . VAL A 65  ? 0.1319 0.1371 0.1420 0.0216  -0.0361 0.0103  65  VAL A C   
390  O  O   . VAL A 65  ? 0.1208 0.1234 0.1947 0.0266  -0.0611 -0.0069 65  VAL A O   
391  C  CB  . VAL A 65  ? 0.1420 0.1385 0.1848 0.0222  0.0022  0.0161  65  VAL A CB  
392  C  CG1 . VAL A 65  ? 0.1546 0.1694 0.2266 -0.0080 -0.0527 0.0167  65  VAL A CG1 
393  C  CG2 . VAL A 65  ? 0.0997 0.1844 0.3024 0.0046  0.0148  0.0647  65  VAL A CG2 
394  N  N   . GLU A 66  ? 0.1046 0.1392 0.1521 0.0091  -0.0442 -0.0101 66  GLU A N   
395  C  CA  . GLU A 66  ? 0.1449 0.1146 0.1532 -0.0023 -0.0649 0.0276  66  GLU A CA  
396  C  C   . GLU A 66  ? 0.1494 0.1462 0.1665 0.0397  -0.0391 0.0487  66  GLU A C   
397  O  O   . GLU A 66  ? 0.1359 0.1945 0.2012 0.0386  -0.0128 -0.0010 66  GLU A O   
398  C  CB  . GLU A 66  ? 0.3967 0.1448 0.2132 -0.0070 -0.0869 0.0072  66  GLU A CB  
399  C  CG  . GLU A 66  ? 0.3088 0.2325 0.2502 -0.0478 -0.1006 -0.0382 66  GLU A CG  
400  C  CD  . GLU A 66  ? 0.2645 0.0921 0.3377 -0.0081 -0.1467 -0.0065 66  GLU A CD  
401  O  OE1 . GLU A 66  ? 0.2065 0.2138 0.2963 0.0031  -0.0901 -0.0324 66  GLU A OE1 
402  O  OE2 . GLU A 66  ? 0.2354 0.1665 0.3529 -0.0265 -0.1401 0.0219  66  GLU A OE2 
403  N  N   . GLY A 67  ? 0.1610 0.1659 0.1601 0.0601  -0.0388 0.0342  67  GLY A N   
404  C  CA  . GLY A 67  ? 0.1936 0.2398 0.1395 0.0324  -0.0147 0.0020  67  GLY A CA  
405  C  C   . GLY A 67  ? 0.1715 0.1275 0.1811 0.0159  -0.0069 0.0043  67  GLY A C   
406  O  O   . GLY A 67  ? 0.1656 0.1639 0.1536 0.0133  -0.0200 0.0227  67  GLY A O   
407  N  N   . ILE A 68  ? 0.1362 0.1516 0.1505 0.0047  -0.0112 -0.0237 68  ILE A N   
408  C  CA  . ILE A 68  ? 0.1200 0.1635 0.1744 0.0406  0.0133  0.0002  68  ILE A CA  
409  C  C   . ILE A 68  ? 0.1109 0.1537 0.1631 0.0040  -0.0496 0.0207  68  ILE A C   
410  O  O   . ILE A 68  ? 0.1065 0.1531 0.2371 0.0141  -0.0106 -0.0023 68  ILE A O   
411  C  CB  . ILE A 68  ? 0.1750 0.1478 0.1395 0.0103  -0.0286 -0.0150 68  ILE A CB  
412  C  CG1 . ILE A 68  ? 0.2976 0.1780 0.2036 -0.0347 -0.0047 -0.0180 68  ILE A CG1 
413  C  CG2 . ILE A 68  ? 0.1786 0.2362 0.1474 0.0686  0.0053  0.0372  68  ILE A CG2 
414  C  CD1 . ILE A 68  ? 0.3117 0.2162 0.2125 -0.0250 0.0279  -0.0051 68  ILE A CD1 
415  N  N   . TYR A 69  ? 0.1053 0.1120 0.1540 -0.0266 -0.0458 0.0043  69  TYR A N   
416  C  CA  . TYR A 69  ? 0.1168 0.1151 0.1123 -0.0056 -0.0406 0.0026  69  TYR A CA  
417  C  C   . TYR A 69  ? 0.1403 0.1134 0.1544 -0.0476 -0.0600 0.0268  69  TYR A C   
418  O  O   . TYR A 69  ? 0.1400 0.1270 0.1943 -0.0059 -0.0656 -0.0296 69  TYR A O   
419  C  CB  . TYR A 69  ? 0.1117 0.1124 0.1117 0.0134  -0.0278 0.0002  69  TYR A CB  
420  C  CG  . TYR A 69  ? 0.1163 0.1260 0.1272 -0.0171 -0.0330 0.0282  69  TYR A CG  
421  C  CD1 . TYR A 69  ? 0.1243 0.1156 0.1509 -0.0203 -0.0178 0.0055  69  TYR A CD1 
422  C  CD2 . TYR A 69  ? 0.0979 0.1299 0.1686 -0.0416 -0.0283 0.0118  69  TYR A CD2 
423  C  CE1 . TYR A 69  ? 0.1446 0.1741 0.1671 -0.0040 -0.0067 0.0091  69  TYR A CE1 
424  C  CE2 . TYR A 69  ? 0.1754 0.1131 0.1948 0.0123  -0.0364 -0.0050 69  TYR A CE2 
425  C  CZ  . TYR A 69  ? 0.1556 0.1441 0.1502 0.0180  -0.0390 0.0546  69  TYR A CZ  
426  O  OH  . TYR A 69  ? 0.2203 0.1686 0.1463 0.0280  -0.0652 0.0514  69  TYR A OH  
427  N  N   . LYS A 70  ? 0.1164 0.0943 0.2098 -0.0268 -0.0473 -0.0030 70  LYS A N   
428  C  CA  . LYS A 70  ? 0.1332 0.1118 0.1845 0.0076  -0.0131 -0.0020 70  LYS A CA  
429  C  C   . LYS A 70  ? 0.1408 0.0959 0.2330 -0.0068 -0.0420 -0.0254 70  LYS A C   
430  O  O   . LYS A 70  ? 0.1803 0.1296 0.2404 0.0447  -0.0843 -0.0608 70  LYS A O   
431  C  CB  . LYS A 70  ? 0.1430 0.1412 0.1892 -0.0180 -0.0211 0.0143  70  LYS A CB  
432  C  CG  . LYS A 70  ? 0.1982 0.1293 0.2378 -0.0475 -0.0220 0.0050  70  LYS A CG  
433  C  CD  . LYS A 70  ? 0.2839 0.2266 0.2606 -0.0043 0.0211  0.0436  70  LYS A CD  
434  C  CE  . LYS A 70  ? 0.3122 0.2997 0.3514 -0.0009 0.0403  0.0213  70  LYS A CE  
435  N  NZ  . LYS A 70  ? 0.5233 0.4517 0.3541 -0.0273 0.0919  0.1013  70  LYS A NZ  
436  N  N   . VAL A 71  ? 0.1345 0.1995 0.1890 0.0037  -0.0379 -0.0216 71  VAL A N   
437  C  CA  . VAL A 71  ? 0.1428 0.1741 0.1827 -0.0058 -0.0568 -0.0273 71  VAL A CA  
438  C  C   . VAL A 71  ? 0.1605 0.1683 0.1841 0.0037  -0.0477 -0.0514 71  VAL A C   
439  O  O   . VAL A 71  ? 0.2128 0.1702 0.2502 0.0234  -0.1064 -0.0289 71  VAL A O   
440  C  CB  . VAL A 71  ? 0.1286 0.1649 0.1546 0.0233  -0.0633 -0.0415 71  VAL A CB  
441  C  CG1 . VAL A 71  ? 0.2808 0.2095 0.1353 0.0539  -0.0416 -0.0800 71  VAL A CG1 
442  C  CG2 . VAL A 71  ? 0.1956 0.1902 0.1345 -0.0307 -0.0449 -0.0139 71  VAL A CG2 
443  N  N   . GLU A 72  ? 0.1959 0.1308 0.1739 0.0147  -0.0509 -0.0384 72  GLU A N   
444  C  CA  . GLU A 72  ? 0.2504 0.1433 0.1920 0.0186  -0.0656 -0.0237 72  GLU A CA  
445  C  C   . GLU A 72  ? 0.2036 0.1116 0.1673 -0.0196 -0.0472 -0.0184 72  GLU A C   
446  O  O   . GLU A 72  ? 0.2628 0.1438 0.1784 0.0476  -0.0915 -0.0130 72  GLU A O   
447  C  CB  . GLU A 72  ? 0.2796 0.2309 0.2513 0.0290  -0.0435 -0.0364 72  GLU A CB  
448  C  CG  . GLU A 72  ? 0.4032 0.3479 0.3477 0.0035  0.0553  -0.0166 72  GLU A CG  
449  C  CD  . GLU A 72  ? 0.3049 0.2777 0.3508 0.0581  0.0344  0.0721  72  GLU A CD  
450  O  OE1 . GLU A 72  ? 0.3347 0.3851 0.4394 -0.0860 0.0541  0.0779  72  GLU A OE1 
451  O  OE2 . GLU A 72  ? 0.4995 0.4819 0.3474 -0.0031 0.0444  0.0025  72  GLU A OE2 
452  N  N   . ILE A 73  ? 0.2423 0.1972 0.1813 0.0350  -0.0394 -0.0081 73  ILE A N   
453  C  CA  . ILE A 73  ? 0.2473 0.1591 0.1681 0.0363  -0.0151 0.0150  73  ILE A CA  
454  C  C   . ILE A 73  ? 0.2011 0.1829 0.1229 0.0244  -0.0141 0.0129  73  ILE A C   
455  O  O   . ILE A 73  ? 0.3098 0.1463 0.1347 0.0246  -0.0528 0.0332  73  ILE A O   
456  C  CB  . ILE A 73  ? 0.2129 0.1677 0.1665 0.0582  -0.0612 -0.0117 73  ILE A CB  
457  C  CG1 . ILE A 73  ? 0.1496 0.2014 0.2366 0.0440  -0.0767 0.0078  73  ILE A CG1 
458  C  CG2 . ILE A 73  ? 0.1837 0.1779 0.2050 0.0638  -0.0600 -0.0210 73  ILE A CG2 
459  C  CD1 . ILE A 73  ? 0.1694 0.2535 0.2785 -0.0085 -0.1081 0.0216  73  ILE A CD1 
460  N  N   . ASP A 74  ? 0.2421 0.1640 0.1578 0.0349  -0.0414 -0.0063 74  ASP A N   
461  C  CA  . ASP A 74  ? 0.2275 0.1633 0.2443 0.0417  -0.0511 -0.0101 74  ASP A CA  
462  C  C   . ASP A 74  ? 0.1565 0.1865 0.1574 0.0362  -0.0419 -0.0334 74  ASP A C   
463  O  O   . ASP A 74  ? 0.2349 0.1990 0.1445 0.0566  -0.0382 -0.0251 74  ASP A O   
464  C  CB  . ASP A 74  ? 0.2256 0.1833 0.2189 0.0262  -0.0504 0.0440  74  ASP A CB  
465  C  CG  . ASP A 74  ? 0.2380 0.2044 0.3299 0.0151  -0.0115 0.0278  74  ASP A CG  
466  O  OD1 . ASP A 74  ? 0.2889 0.3125 0.2615 0.0063  0.0899  -0.0340 74  ASP A OD1 
467  O  OD2 . ASP A 74  ? 0.3289 0.2879 0.5114 0.0538  -0.2013 -0.0388 74  ASP A OD2 
468  N  N   . THR A 75  ? 0.1741 0.1800 0.1712 0.0275  -0.0219 -0.0249 75  THR A N   
469  C  CA  . THR A 75  ? 0.1819 0.1629 0.1922 0.0286  -0.0245 -0.0414 75  THR A CA  
470  C  C   . THR A 75  ? 0.1365 0.1372 0.2117 0.0747  -0.0372 -0.0081 75  THR A C   
471  O  O   . THR A 75  ? 0.1767 0.1411 0.1697 0.0865  -0.0275 -0.0298 75  THR A O   
472  C  CB  . THR A 75  ? 0.1649 0.1958 0.1660 0.0261  -0.0458 -0.0038 75  THR A CB  
473  O  OG1 . THR A 75  ? 0.2303 0.1743 0.2020 0.0080  -0.0317 0.0070  75  THR A OG1 
474  C  CG2 . THR A 75  ? 0.1679 0.1312 0.2841 0.0118  -0.0377 -0.0240 75  THR A CG2 
475  N  N   . LYS A 76  ? 0.1772 0.1492 0.1795 -0.0031 -0.0269 -0.0324 76  LYS A N   
476  C  CA  . LYS A 76  ? 0.1884 0.1874 0.1548 -0.0119 0.0107  -0.0063 76  LYS A CA  
477  C  C   . LYS A 76  ? 0.1578 0.1739 0.1804 0.0414  -0.0190 -0.0194 76  LYS A C   
478  O  O   . LYS A 76  ? 0.2036 0.1566 0.1828 0.0396  0.0155  0.0045  76  LYS A O   
479  C  CB  . LYS A 76  ? 0.2630 0.2707 0.2278 0.0752  0.0471  -0.0378 76  LYS A CB  
480  C  CG  . LYS A 76  ? 0.2967 0.3622 0.2602 0.0469  0.0771  -0.0246 76  LYS A CG  
481  C  CD  . LYS A 76  ? 0.4207 0.4326 0.3379 0.0482  0.2379  -0.0246 76  LYS A CD  
482  C  CE  . LYS A 76  ? 0.4918 0.6222 0.3847 -0.0967 0.2257  0.0026  76  LYS A CE  
483  N  N   . SER A 77  ? 0.1679 0.1255 0.1645 -0.0010 0.0068  0.0067  77  SER A N   
484  C  CA  . SER A 77  ? 0.1345 0.1302 0.1758 -0.0160 -0.0131 -0.0013 77  SER A CA  
485  C  C   . SER A 77  ? 0.1361 0.1755 0.1417 -0.0063 -0.0321 -0.0262 77  SER A C   
486  O  O   . SER A 77  ? 0.1678 0.1458 0.2433 -0.0282 -0.0095 -0.0094 77  SER A O   
487  C  CB  . SER A 77  ? 0.1720 0.2861 0.1644 -0.0434 -0.0813 -0.0405 77  SER A CB  
488  O  OG  . SER A 77  ? 0.2481 0.3458 0.3334 -0.0656 -0.0064 0.0631  77  SER A OG  
489  N  N   . TYR A 78  ? 0.1480 0.1558 0.1573 -0.0019 -0.0004 -0.0030 78  TYR A N   
490  C  CA  . TYR A 78  ? 0.1743 0.1191 0.1844 0.0070  0.0380  0.0015  78  TYR A CA  
491  C  C   . TYR A 78  ? 0.1414 0.1678 0.1863 0.0067  -0.0219 -0.0187 78  TYR A C   
492  O  O   . TYR A 78  ? 0.1404 0.1626 0.2153 -0.0125 0.0011  -0.0331 78  TYR A O   
493  C  CB  . TYR A 78  ? 0.1548 0.1449 0.2077 -0.0108 -0.0036 0.0204  78  TYR A CB  
494  C  CG  . TYR A 78  ? 0.1443 0.1572 0.1368 -0.0222 0.0107  -0.0213 78  TYR A CG  
495  C  CD1 . TYR A 78  ? 0.1353 0.1225 0.1533 -0.0029 0.0210  -0.0091 78  TYR A CD1 
496  C  CD2 . TYR A 78  ? 0.1865 0.1457 0.1789 -0.0186 -0.0194 -0.0279 78  TYR A CD2 
497  C  CE1 . TYR A 78  ? 0.1058 0.1720 0.1199 -0.0229 -0.0190 -0.0269 78  TYR A CE1 
498  C  CE2 . TYR A 78  ? 0.1976 0.2000 0.1829 -0.0537 0.0056  -0.0187 78  TYR A CE2 
499  C  CZ  . TYR A 78  ? 0.0967 0.2244 0.1514 -0.0911 -0.0169 0.0170  78  TYR A CZ  
500  O  OH  . TYR A 78  ? 0.1328 0.2050 0.2099 -0.0618 0.0131  0.0092  78  TYR A OH  
501  N  N   . TRP A 79  ? 0.1236 0.1300 0.1669 -0.0042 0.0104  0.0038  79  TRP A N   
502  C  CA  . TRP A 79  ? 0.1296 0.1733 0.2466 0.0245  -0.0238 -0.0099 79  TRP A CA  
503  C  C   . TRP A 79  ? 0.1107 0.1447 0.2152 0.0277  -0.0546 -0.0060 79  TRP A C   
504  O  O   . TRP A 79  ? 0.1610 0.1286 0.2504 0.0118  0.0090  -0.0175 79  TRP A O   
505  C  CB  . TRP A 79  ? 0.1332 0.1390 0.2021 0.0016  -0.0094 0.0228  79  TRP A CB  
506  C  CG  . TRP A 79  ? 0.1547 0.1211 0.1896 0.0085  -0.0046 0.0113  79  TRP A CG  
507  C  CD1 . TRP A 79  ? 0.1582 0.1340 0.2153 0.0059  -0.0231 -0.0003 79  TRP A CD1 
508  C  CD2 . TRP A 79  ? 0.1273 0.1429 0.1847 0.0232  -0.0546 -0.0325 79  TRP A CD2 
509  N  NE1 . TRP A 79  ? 0.1510 0.1586 0.1652 0.0052  0.0311  0.0030  79  TRP A NE1 
510  C  CE2 . TRP A 79  ? 0.1311 0.1839 0.2015 -0.0100 -0.0232 -0.0816 79  TRP A CE2 
511  C  CE3 . TRP A 79  ? 0.1391 0.0842 0.1982 -0.0036 -0.0039 -0.0166 79  TRP A CE3 
512  C  CZ2 . TRP A 79  ? 0.1380 0.1643 0.1904 -0.0290 -0.0512 0.0040  79  TRP A CZ2 
513  C  CZ3 . TRP A 79  ? 0.1322 0.1636 0.2186 0.0059  0.0196  -0.0291 79  TRP A CZ3 
514  C  CH2 . TRP A 79  ? 0.1872 0.1648 0.2162 -0.0122 -0.0551 0.0071  79  TRP A CH2 
515  N  N   . LYS A 80  ? 0.1222 0.1048 0.2222 -0.0121 -0.0039 0.0046  80  LYS A N   
516  C  CA  . LYS A 80  ? 0.1578 0.1010 0.1662 -0.0164 -0.0003 0.0057  80  LYS A CA  
517  C  C   . LYS A 80  ? 0.2120 0.1647 0.2694 0.0150  -0.0221 -0.0732 80  LYS A C   
518  O  O   . LYS A 80  ? 0.1644 0.1882 0.2085 0.0134  -0.0370 -0.0385 80  LYS A O   
519  C  CB  . LYS A 80  ? 0.1874 0.2227 0.2415 -0.0248 -0.0127 0.0031  80  LYS A CB  
520  C  CG  . LYS A 80  ? 0.3203 0.3292 0.3882 -0.0235 0.0275  -0.0045 80  LYS A CG  
521  C  CD  . LYS A 80  ? 0.2765 0.3743 0.4199 -0.0040 0.0503  -0.0343 80  LYS A CD  
522  N  N   . ALA A 81  ? 0.1559 0.1420 0.2415 -0.0100 -0.0318 -0.0935 81  ALA A N   
523  C  CA  . ALA A 81  ? 0.1513 0.1535 0.1754 -0.0238 -0.0353 -0.0414 81  ALA A CA  
524  C  C   . ALA A 81  ? 0.1743 0.1737 0.2259 0.0221  0.0105  -0.0648 81  ALA A C   
525  O  O   . ALA A 81  ? 0.2939 0.2019 0.2935 0.0054  -0.0012 -0.1172 81  ALA A O   
526  C  CB  . ALA A 81  ? 0.2532 0.2319 0.1567 -0.0361 -0.0420 -0.0125 81  ALA A CB  
527  N  N   . LEU A 82  ? 0.1699 0.2024 0.2637 0.0097  0.0119  -0.1024 82  LEU A N   
528  C  CA  . LEU A 82  ? 0.1706 0.1937 0.2567 0.0251  0.0511  -0.0065 82  LEU A CA  
529  C  C   . LEU A 82  ? 0.1874 0.1153 0.2873 0.0258  -0.0374 -0.0310 82  LEU A C   
530  O  O   . LEU A 82  ? 0.2462 0.2022 0.4119 0.0889  -0.1093 -0.0428 82  LEU A O   
531  C  CB  . LEU A 82  ? 0.1792 0.1732 0.3038 0.0803  -0.0036 -0.0616 82  LEU A CB  
532  C  CG  . LEU A 82  ? 0.1648 0.2404 0.2749 0.0176  -0.0223 -0.0815 82  LEU A CG  
533  C  CD1 . LEU A 82  ? 0.3004 0.2817 0.3653 -0.0526 0.0700  -0.1889 82  LEU A CD1 
534  C  CD2 . LEU A 82  ? 0.2612 0.2228 0.2538 -0.0060 0.0454  -0.0375 82  LEU A CD2 
535  N  N   . GLY A 83  ? 0.1779 0.2296 0.2756 0.0646  -0.0273 -0.0527 83  GLY A N   
536  C  CA  . GLY A 83  ? 0.2625 0.2292 0.3228 0.0138  -0.0834 0.0172  83  GLY A CA  
537  C  C   . GLY A 83  ? 0.2030 0.2197 0.2942 0.0078  -0.0592 0.0525  83  GLY A C   
538  O  O   . GLY A 83  ? 0.3450 0.1953 0.2658 0.0552  -0.1412 -0.0302 83  GLY A O   
539  N  N   . ILE A 84  ? 0.2577 0.2246 0.2277 0.0671  -0.1356 0.0667  84  ILE A N   
540  C  CA  . ILE A 84  ? 0.2059 0.2225 0.2182 0.0904  -0.0809 0.0511  84  ILE A CA  
541  C  C   . ILE A 84  ? 0.1915 0.1425 0.2324 -0.0141 -0.0674 -0.0463 84  ILE A C   
542  O  O   . ILE A 84  ? 0.2597 0.2227 0.2266 0.0769  -0.0579 0.0043  84  ILE A O   
543  C  CB  . ILE A 84  ? 0.3355 0.2240 0.2471 0.0023  -0.0247 -0.0059 84  ILE A CB  
544  C  CG1 . ILE A 84  ? 0.2992 0.2117 0.3051 -0.0580 -0.1148 -0.0863 84  ILE A CG1 
545  C  CG2 . ILE A 84  ? 0.2171 0.1738 0.3024 -0.0103 -0.0283 0.0006  84  ILE A CG2 
546  C  CD1 . ILE A 84  ? 0.2954 0.4295 0.2954 -0.0480 -0.0635 -0.0487 84  ILE A CD1 
547  N  N   . SER A 85  ? 0.2069 0.1919 0.1921 0.0152  -0.0507 0.0074  85  SER A N   
548  C  CA  . SER A 85  ? 0.2380 0.2343 0.2721 0.0300  -0.0611 -0.0377 85  SER A CA  
549  C  C   . SER A 85  ? 0.3924 0.2151 0.2135 0.0721  0.0380  -0.0517 85  SER A C   
550  O  O   . SER A 85  ? 0.4747 0.2370 0.5011 0.0139  0.0596  -0.0103 85  SER A O   
551  C  CB  . SER A 85  ? 0.3184 0.5177 0.2631 0.0888  -0.0502 -0.0522 85  SER A CB  
552  O  OG  . SER A 85  ? 0.6256 0.5597 0.4715 0.0654  -0.0216 -0.1805 85  SER A OG  
553  N  N   . PRO A 86  ? 0.3858 0.2329 0.2380 0.0604  -0.0055 -0.1018 86  PRO A N   
554  C  CA  . PRO A 86  ? 0.3472 0.2297 0.4091 0.0117  0.0207  -0.0746 86  PRO A CA  
555  C  C   . PRO A 86  ? 0.2007 0.1832 0.3174 0.0099  0.0789  0.0516  86  PRO A C   
556  O  O   . PRO A 86  ? 0.2541 0.2809 0.4058 -0.0408 0.1664  -0.0098 86  PRO A O   
557  C  CB  . PRO A 86  ? 0.4068 0.3148 0.3157 0.0491  0.0807  -0.0787 86  PRO A CB  
558  C  CG  . PRO A 86  ? 0.4058 0.2533 0.3619 0.0477  0.0392  0.0853  86  PRO A CG  
559  C  CD  . PRO A 86  ? 0.2596 0.2478 0.3810 0.0861  0.0308  -0.0548 86  PRO A CD  
560  N  N   . PHE A 87  ? 0.2971 0.3500 0.2977 0.0337  0.1117  -0.0887 87  PHE A N   
561  C  CA  . PHE A 87  ? 0.2856 0.3261 0.1698 0.0247  0.0459  -0.0126 87  PHE A CA  
562  C  C   . PHE A 87  ? 0.1176 0.3260 0.3238 -0.0483 0.0160  0.0733  87  PHE A C   
563  O  O   . PHE A 87  ? 0.1675 0.1904 0.2646 -0.0184 0.0319  -0.0028 87  PHE A O   
564  C  CB  . PHE A 87  ? 0.1701 0.4257 0.3451 0.0609  0.0529  -0.0220 87  PHE A CB  
565  C  CG  . PHE A 87  ? 0.2406 0.3446 0.3538 0.0845  0.0069  0.0154  87  PHE A CG  
566  C  CD1 . PHE A 87  ? 0.2944 0.4112 0.2743 0.1247  -0.0417 0.0340  87  PHE A CD1 
567  C  CD2 . PHE A 87  ? 0.2951 0.3640 0.2426 -0.0388 0.0163  -0.0753 87  PHE A CD2 
568  C  CE1 . PHE A 87  ? 0.4539 0.4110 0.2086 -0.0028 -0.0244 0.0138  87  PHE A CE1 
569  C  CE2 . PHE A 87  ? 0.3130 0.4945 0.2069 -0.0457 -0.0326 -0.1078 87  PHE A CE2 
570  C  CZ  . PHE A 87  ? 0.2459 0.4553 0.3251 -0.0559 0.0965  -0.0665 87  PHE A CZ  
571  N  N   . HIS A 88  ? 0.1748 0.3234 0.2572 -0.0045 0.0588  0.0282  88  HIS A N   
572  C  CA  . HIS A 88  ? 0.3501 0.3224 0.2841 -0.0020 -0.0102 -0.0194 88  HIS A CA  
573  C  C   . HIS A 88  ? 0.3697 0.2617 0.1113 0.0624  -0.0346 0.0095  88  HIS A C   
574  O  O   . HIS A 88  ? 0.4619 0.1815 0.2713 -0.0028 -0.0404 -0.0163 88  HIS A O   
575  C  CB  . HIS A 88  ? 0.4405 0.1806 0.2757 0.0381  -0.0492 -0.0218 88  HIS A CB  
576  C  CG  . HIS A 88  ? 0.2528 0.2115 0.3320 -0.0375 0.0255  0.0755  88  HIS A CG  
577  N  ND1 . HIS A 88  ? 0.2618 0.3636 0.4033 0.0466  0.0049  -0.0317 88  HIS A ND1 
578  C  CD2 . HIS A 88  ? 0.2962 0.2970 0.4408 -0.0297 -0.0555 0.0090  88  HIS A CD2 
579  C  CE1 . HIS A 88  ? 0.2387 0.4284 0.2955 0.0752  -0.0493 -0.0309 88  HIS A CE1 
580  N  NE2 . HIS A 88  ? 0.2022 0.3419 0.4335 0.0193  -0.0066 0.0764  88  HIS A NE2 
581  N  N   . GLU A 89  ? 0.2735 0.4202 0.2094 -0.0689 0.0567  -0.0265 89  GLU A N   
582  C  CA  . GLU A 89  ? 0.3067 0.3390 0.3036 -0.0419 -0.0478 -0.0094 89  GLU A CA  
583  C  C   . GLU A 89  ? 0.3478 0.2486 0.2696 0.0582  -0.0039 -0.0354 89  GLU A C   
584  O  O   . GLU A 89  ? 0.2927 0.2621 0.2603 0.0317  0.0209  -0.0509 89  GLU A O   
585  C  CB  . GLU A 89  ? 0.3629 0.4996 0.4337 -0.1003 -0.0347 -0.2022 89  GLU A CB  
586  C  CG  . GLU A 89  ? 0.2466 0.4932 0.5540 -0.0213 0.0951  -0.1881 89  GLU A CG  
587  C  CD  . GLU A 89  ? 0.3065 0.4092 0.3684 -0.1480 0.1454  -0.0746 89  GLU A CD  
588  N  N   . HIS A 90  ? 0.2345 0.2604 0.1185 0.0640  -0.0345 -0.0556 90  HIS A N   
589  C  CA  . HIS A 90  ? 0.3587 0.1783 0.1692 0.0399  -0.0748 -0.0344 90  HIS A CA  
590  C  C   . HIS A 90  ? 0.4102 0.1759 0.2432 0.0621  -0.1493 -0.0846 90  HIS A C   
591  O  O   . HIS A 90  ? 0.9305 0.1887 0.2315 -0.0815 -0.2341 0.0367  90  HIS A O   
592  C  CB  . HIS A 90  ? 0.3522 0.2267 0.3452 0.0817  -0.0668 -0.0061 90  HIS A CB  
593  C  CG  . HIS A 90  ? 0.3285 0.3528 0.2322 0.0222  0.0480  0.0996  90  HIS A CG  
594  N  ND1 . HIS A 90  ? 0.3917 0.6260 0.2463 0.0841  0.1397  0.0035  90  HIS A ND1 
595  C  CD2 . HIS A 90  ? 0.4962 0.4248 0.2667 0.0755  0.0313  0.1283  90  HIS A CD2 
596  C  CE1 . HIS A 90  ? 0.3104 0.6919 0.3140 0.0081  0.2142  0.0095  90  HIS A CE1 
597  N  NE2 . HIS A 90  ? 0.5607 0.4269 0.2707 0.1601  0.0161  0.0518  90  HIS A NE2 
598  N  N   . ALA A 91  ? 0.4983 0.2085 0.2735 -0.0292 -0.1927 -0.0520 91  ALA A N   
599  C  CA  . ALA A 91  ? 0.6646 0.1981 0.1604 -0.0664 -0.1764 -0.0408 91  ALA A CA  
600  C  C   . ALA A 91  ? 0.6900 0.1995 0.2293 -0.0094 -0.0465 0.0612  91  ALA A C   
601  O  O   . ALA A 91  ? 0.4851 0.2511 0.2608 -0.0258 -0.0476 -0.0218 91  ALA A O   
602  C  CB  . ALA A 91  ? 0.6470 0.2856 0.2942 -0.0711 -0.1019 0.0509  91  ALA A CB  
603  N  N   . GLU A 92  ? 0.8121 0.2457 0.4020 0.0734  -0.1683 0.0039  92  GLU A N   
604  C  CA  . GLU A 92  ? 0.4610 0.2970 0.4042 -0.0844 -0.1746 0.0062  92  GLU A CA  
605  C  C   . GLU A 92  ? 0.8871 0.2920 0.3632 -0.1039 -0.0325 -0.0402 92  GLU A C   
606  O  O   . GLU A 92  ? 0.4536 0.4984 0.2923 -0.1524 -0.0129 -0.0255 92  GLU A O   
607  C  CB  . GLU A 92  ? 0.4246 0.5991 0.4082 -0.1692 -0.1915 -0.0058 92  GLU A CB  
608  N  N   . VAL A 93  ? 0.4193 0.3139 0.1613 0.0540  -0.1918 -0.0782 93  VAL A N   
609  C  CA  . VAL A 93  ? 0.1887 0.3430 0.2069 0.1108  -0.0818 0.0150  93  VAL A CA  
610  C  C   . VAL A 93  ? 0.1810 0.1113 0.1845 0.0030  -0.0553 -0.0226 93  VAL A C   
611  O  O   . VAL A 93  ? 0.1767 0.1695 0.1873 0.0078  -0.0445 -0.0130 93  VAL A O   
612  C  CB  . VAL A 93  ? 0.2507 0.2658 0.2601 0.0617  -0.0511 -0.0065 93  VAL A CB  
613  C  CG1 . VAL A 93  ? 0.3290 0.2772 0.2645 -0.0286 0.0120  -0.0637 93  VAL A CG1 
614  C  CG2 . VAL A 93  ? 0.3902 0.2820 0.4464 0.0928  -0.0703 -0.0192 93  VAL A CG2 
615  N  N   . VAL A 94  ? 0.1180 0.1676 0.1376 0.0063  -0.0610 -0.0454 94  VAL A N   
616  C  CA  . VAL A 94  ? 0.1065 0.1579 0.1613 -0.0127 -0.0380 -0.0168 94  VAL A CA  
617  C  C   . VAL A 94  ? 0.1070 0.1631 0.1451 -0.0168 -0.0083 -0.0162 94  VAL A C   
618  O  O   . VAL A 94  ? 0.1327 0.1570 0.1203 -0.0124 -0.0081 -0.0234 94  VAL A O   
619  C  CB  . VAL A 94  ? 0.1486 0.1197 0.1472 0.0255  -0.0206 0.0106  94  VAL A CB  
620  C  CG1 . VAL A 94  ? 0.1024 0.1757 0.2179 0.0455  0.0185  0.0524  94  VAL A CG1 
621  C  CG2 . VAL A 94  ? 0.1834 0.1571 0.2362 -0.0288 -0.0174 -0.0038 94  VAL A CG2 
622  N  N   . PHE A 95  ? 0.0999 0.1496 0.1632 -0.0015 -0.0286 -0.0230 95  PHE A N   
623  C  CA  . PHE A 95  ? 0.1178 0.1707 0.1400 -0.0183 -0.0404 -0.0272 95  PHE A CA  
624  C  C   . PHE A 95  ? 0.1534 0.1552 0.1394 -0.0235 -0.0144 -0.0007 95  PHE A C   
625  O  O   . PHE A 95  ? 0.1301 0.1846 0.1535 -0.0129 -0.0175 0.0104  95  PHE A O   
626  C  CB  . PHE A 95  ? 0.1247 0.1618 0.2191 -0.0201 0.0075  -0.0357 95  PHE A CB  
627  C  CG  . PHE A 95  ? 0.1705 0.2174 0.1798 -0.0123 0.0074  0.0007  95  PHE A CG  
628  C  CD1 . PHE A 95  ? 0.1470 0.2422 0.1588 -0.0084 0.0280  -0.0457 95  PHE A CD1 
629  C  CD2 . PHE A 95  ? 0.1811 0.1968 0.1375 0.0203  -0.0377 -0.0332 95  PHE A CD2 
630  C  CE1 . PHE A 95  ? 0.1745 0.2318 0.1988 -0.0181 0.0087  -0.0758 95  PHE A CE1 
631  C  CE2 . PHE A 95  ? 0.1460 0.3122 0.1372 0.0145  -0.0624 -0.0429 95  PHE A CE2 
632  C  CZ  . PHE A 95  ? 0.1927 0.2895 0.1912 0.0136  -0.0073 -0.1025 95  PHE A CZ  
633  N  N   . THR A 96  ? 0.1530 0.1446 0.1769 -0.0127 -0.0613 -0.0198 96  THR A N   
634  C  CA  . THR A 96  ? 0.1469 0.1533 0.1738 0.0035  -0.0499 -0.0248 96  THR A CA  
635  C  C   . THR A 96  ? 0.1301 0.1615 0.1554 -0.0314 -0.0734 -0.0106 96  THR A C   
636  O  O   . THR A 96  ? 0.1316 0.2650 0.1957 -0.0518 -0.0024 0.0325  96  THR A O   
637  C  CB  . THR A 96  ? 0.2416 0.1696 0.1255 -0.0093 -0.0365 -0.0539 96  THR A CB  
638  O  OG1 . THR A 96  ? 0.2581 0.1601 0.1977 0.0180  -0.0032 -0.0286 96  THR A OG1 
639  C  CG2 . THR A 96  ? 0.2782 0.1209 0.2686 0.0262  -0.0297 -0.0038 96  THR A CG2 
640  N  N   . ALA A 97  ? 0.1104 0.1823 0.1312 -0.0370 -0.0500 -0.0117 97  ALA A N   
641  C  CA  . ALA A 97  ? 0.1603 0.1314 0.1514 -0.0186 -0.0154 0.0067  97  ALA A CA  
642  C  C   . ALA A 97  ? 0.1195 0.1486 0.1342 0.0102  -0.0398 -0.0106 97  ALA A C   
643  O  O   . ALA A 97  ? 0.1095 0.1553 0.2079 -0.0087 -0.0015 0.0259  97  ALA A O   
644  C  CB  . ALA A 97  ? 0.1872 0.1286 0.2102 -0.0385 -0.0575 0.0056  97  ALA A CB  
645  N  N   . ASN A 98  ? 0.1263 0.1617 0.1562 -0.0038 -0.0360 -0.0126 98  ASN A N   
646  C  CA  . ASN A 98  ? 0.1196 0.1306 0.2307 0.0028  -0.0178 0.0164  98  ASN A CA  
647  C  C   . ASN A 98  ? 0.1157 0.1465 0.1152 0.0004  -0.0115 0.0180  98  ASN A C   
648  O  O   . ASN A 98  ? 0.1253 0.1935 0.1737 0.0281  -0.0293 0.0380  98  ASN A O   
649  C  CB  . ASN A 98  ? 0.1555 0.1608 0.1848 0.0166  -0.0124 0.0078  98  ASN A CB  
650  C  CG  . ASN A 98  ? 0.2121 0.1606 0.1625 -0.0427 0.0012  -0.0387 98  ASN A CG  
651  O  OD1 . ASN A 98  ? 0.2243 0.1600 0.1801 0.0297  0.0074  -0.0012 98  ASN A OD1 
652  N  ND2 . ASN A 98  ? 0.1952 0.1447 0.1631 -0.0252 -0.0504 0.0073  98  ASN A ND2 
653  N  N   . ASP A 99  ? 0.1219 0.1826 0.1539 -0.0114 0.0060  -0.0080 99  ASP A N   
654  C  CA  . ASP A 99  ? 0.1359 0.1900 0.2060 0.0764  0.0094  0.0253  99  ASP A CA  
655  C  C   . ASP A 99  ? 0.1838 0.1700 0.2321 0.0223  -0.0027 -0.0249 99  ASP A C   
656  O  O   . ASP A 99  ? 0.2043 0.1648 0.2347 0.0162  -0.0254 -0.0107 99  ASP A O   
657  C  CB  . ASP A 99  ? 0.2092 0.1546 0.2011 -0.0182 -0.0031 -0.0038 99  ASP A CB  
658  C  CG  . ASP A 99  ? 0.2714 0.1382 0.1722 -0.0074 -0.0497 -0.0629 99  ASP A CG  
659  O  OD1 . ASP A 99  ? 0.2079 0.1958 0.2176 0.0266  -0.0051 0.0037  99  ASP A OD1 
660  O  OD2 . ASP A 99  ? 0.2809 0.2059 0.2050 -0.0411 -0.0561 -0.0152 99  ASP A OD2 
661  N  N   . SER A 100 ? 0.1835 0.1366 0.2640 0.0180  0.0177  0.0248  100 SER A N   
662  C  CA  . SER A 100 ? 0.2429 0.1873 0.2682 -0.0474 -0.0419 0.0245  100 SER A CA  
663  C  C   . SER A 100 ? 0.2530 0.2021 0.2512 -0.0820 -0.0175 0.0734  100 SER A C   
664  O  O   . SER A 100 ? 0.2831 0.2589 0.3196 -0.1115 0.0574  0.0259  100 SER A O   
665  C  CB  . SER A 100 ? 0.2435 0.2406 0.4376 -0.0801 -0.0800 0.0717  100 SER A CB  
666  O  OG  . SER A 100 ? 0.2750 0.3884 0.5965 -0.0556 0.0138  0.0454  100 SER A OG  
667  N  N   . GLY A 101 ? 0.1718 0.1793 0.2720 -0.0054 -0.0060 0.0136  101 GLY A N   
668  C  CA  . GLY A 101 ? 0.2017 0.1904 0.2296 0.0130  0.0011  0.0208  101 GLY A CA  
669  C  C   . GLY A 101 ? 0.2013 0.1785 0.2368 -0.0199 -0.0229 0.0084  101 GLY A C   
670  O  O   . GLY A 101 ? 0.1437 0.1744 0.2695 0.0139  -0.0130 -0.0007 101 GLY A O   
671  N  N   . PRO A 102 ? 0.1567 0.1291 0.2079 0.0280  -0.0281 0.0126  102 PRO A N   
672  C  CA  . PRO A 102 ? 0.2313 0.1334 0.2219 -0.0015 0.0389  0.0238  102 PRO A CA  
673  C  C   . PRO A 102 ? 0.2090 0.1565 0.2186 0.0012  0.0283  0.0166  102 PRO A C   
674  O  O   . PRO A 102 ? 0.1864 0.1963 0.2535 -0.0054 0.0259  0.0555  102 PRO A O   
675  C  CB  . PRO A 102 ? 0.3214 0.1329 0.2782 -0.0353 -0.0064 0.0164  102 PRO A CB  
676  C  CG  . PRO A 102 ? 0.4334 0.1743 0.3373 0.0398  0.0100  -0.0116 102 PRO A CG  
677  C  CD  . PRO A 102 ? 0.2687 0.1608 0.2305 0.0652  -0.0365 0.0349  102 PRO A CD  
678  N  N   . ARG A 103 ? 0.1617 0.1512 0.2346 -0.0027 -0.0072 0.0115  103 ARG A N   
679  C  CA  . ARG A 103 ? 0.1492 0.1385 0.2032 -0.0103 -0.0205 0.0327  103 ARG A CA  
680  C  C   . ARG A 103 ? 0.1942 0.1435 0.1382 -0.0126 0.0128  0.0479  103 ARG A C   
681  O  O   . ARG A 103 ? 0.1836 0.1632 0.2495 0.0047  -0.0193 0.0291  103 ARG A O   
682  C  CB  . ARG A 103 ? 0.1794 0.1272 0.2286 -0.0149 -0.0285 0.0409  103 ARG A CB  
683  C  CG  . ARG A 103 ? 0.1696 0.1893 0.2281 -0.0034 0.0318  -0.0064 103 ARG A CG  
684  C  CD  . ARG A 103 ? 0.1173 0.2298 0.2255 0.0038  -0.0214 0.0164  103 ARG A CD  
685  N  NE  . ARG A 103 ? 0.3071 0.2309 0.3887 -0.0681 -0.0488 0.0097  103 ARG A NE  
686  C  CZ  . ARG A 103 ? 0.3601 0.2102 0.3971 -0.0515 -0.0678 -0.0524 103 ARG A CZ  
687  N  NH1 . ARG A 103 ? 0.2828 0.1839 0.4433 -0.0398 -0.0641 0.0537  103 ARG A NH1 
688  N  NH2 . ARG A 103 ? 0.5250 0.2118 0.4817 -0.1085 0.0079  -0.0609 103 ARG A NH2 
689  N  N   . ARG A 104 ? 0.1918 0.1571 0.2428 -0.0031 0.0016  0.0178  104 ARG A N   
690  C  CA  . ARG A 104 ? 0.2119 0.1721 0.1666 -0.0275 -0.0250 -0.0036 104 ARG A CA  
691  C  C   . ARG A 104 ? 0.1652 0.1956 0.1741 -0.0056 0.0104  -0.0222 104 ARG A C   
692  O  O   . ARG A 104 ? 0.1837 0.2045 0.1816 -0.0394 -0.0220 0.0522  104 ARG A O   
693  C  CB  . ARG A 104 ? 0.2393 0.2552 0.2037 0.0016  0.0146  0.0133  104 ARG A CB  
694  C  CG  . ARG A 104 ? 0.3593 0.2886 0.2739 0.0319  -0.0130 0.0185  104 ARG A CG  
695  C  CD  . ARG A 104 ? 0.3710 0.3370 0.3595 -0.0190 0.0189  0.0064  104 ARG A CD  
696  N  NE  . ARG A 104 ? 0.4424 0.3818 0.3431 0.0060  -0.0089 -0.0231 104 ARG A NE  
697  C  CZ  . ARG A 104 ? 0.6356 0.5712 0.3511 -0.0251 -0.0329 -0.0929 104 ARG A CZ  
698  N  N   . TYR A 105 ? 0.1234 0.0931 0.0464 0.0176  -0.0269 0.0036  105 TYR A N   
699  C  CA  . TYR A 105 ? 0.1789 0.1410 0.1071 -0.0064 -0.0685 0.0606  105 TYR A CA  
700  C  C   . TYR A 105 ? 0.1420 0.1854 0.1483 0.0177  -0.0255 -0.0165 105 TYR A C   
701  O  O   . TYR A 105 ? 0.1596 0.1705 0.1740 0.0398  -0.0727 -0.0039 105 TYR A O   
702  C  CB  . TYR A 105 ? 0.1787 0.1349 0.1783 -0.0222 -0.0238 -0.0010 105 TYR A CB  
703  C  CG  . TYR A 105 ? 0.1190 0.1580 0.1659 -0.0090 -0.0567 -0.0067 105 TYR A CG  
704  C  CD1 . TYR A 105 ? 0.1267 0.1397 0.1785 -0.0299 -0.0490 0.0265  105 TYR A CD1 
705  C  CD2 . TYR A 105 ? 0.1824 0.1934 0.1127 0.0461  -0.0672 0.0129  105 TYR A CD2 
706  C  CE1 . TYR A 105 ? 0.2101 0.1683 0.1845 0.0228  -0.0966 0.0671  105 TYR A CE1 
707  C  CE2 . TYR A 105 ? 0.1576 0.1888 0.1472 0.0000  0.0174  -0.0290 105 TYR A CE2 
708  C  CZ  . TYR A 105 ? 0.1461 0.1588 0.2164 0.0036  0.0003  -0.0079 105 TYR A CZ  
709  O  OH  . TYR A 105 ? 0.1140 0.1604 0.1779 0.0056  -0.0130 -0.0060 105 TYR A OH  
710  N  N   . THR A 106 ? 0.1218 0.1330 0.2024 -0.0043 -0.0304 -0.0109 106 THR A N   
711  C  CA  . THR A 106 ? 0.1576 0.1408 0.1768 0.0064  -0.0465 0.0291  106 THR A CA  
712  C  C   . THR A 106 ? 0.1567 0.1826 0.1856 0.0145  -0.0526 -0.0023 106 THR A C   
713  O  O   . THR A 106 ? 0.1748 0.1215 0.2140 -0.0166 -0.0635 0.0111  106 THR A O   
714  C  CB  . THR A 106 ? 0.1713 0.2369 0.1682 0.0233  -0.0344 0.0575  106 THR A CB  
715  O  OG1 . THR A 106 ? 0.2621 0.3248 0.1584 0.0005  0.0140  0.0476  106 THR A OG1 
716  C  CG2 . THR A 106 ? 0.1517 0.2315 0.2401 0.0205  -0.0420 0.0168  106 THR A CG2 
717  N  N   . ILE A 107 ? 0.1505 0.1315 0.1889 0.0275  -0.0364 0.0115  107 ILE A N   
718  C  CA  . ILE A 107 ? 0.1691 0.1094 0.1611 -0.0145 -0.0601 -0.0056 107 ILE A CA  
719  C  C   . ILE A 107 ? 0.1723 0.1243 0.2037 -0.0110 -0.0513 0.0170  107 ILE A C   
720  O  O   . ILE A 107 ? 0.1980 0.1287 0.2102 -0.0175 -0.0635 0.0177  107 ILE A O   
721  C  CB  . ILE A 107 ? 0.1577 0.1685 0.1914 -0.0455 -0.0567 0.0130  107 ILE A CB  
722  C  CG1 . ILE A 107 ? 0.1576 0.2137 0.2858 -0.0446 -0.0339 -0.0132 107 ILE A CG1 
723  C  CG2 . ILE A 107 ? 0.2440 0.1439 0.1774 -0.0310 -0.0159 -0.0056 107 ILE A CG2 
724  C  CD1 . ILE A 107 ? 0.1365 0.2092 0.3035 0.0283  -0.0944 -0.0047 107 ILE A CD1 
725  N  N   . ALA A 108 ? 0.2175 0.1096 0.1780 0.0049  -0.0824 -0.0150 108 ALA A N   
726  C  CA  . ALA A 108 ? 0.2754 0.1677 0.1390 0.0557  -0.1430 -0.0454 108 ALA A CA  
727  C  C   . ALA A 108 ? 0.3261 0.1793 0.1523 0.0263  -0.1205 -0.0445 108 ALA A C   
728  O  O   . ALA A 108 ? 0.3165 0.1337 0.1447 0.0422  -0.0786 -0.0252 108 ALA A O   
729  C  CB  . ALA A 108 ? 0.2762 0.1802 0.2008 0.0930  -0.0804 -0.0023 108 ALA A CB  
730  N  N   . ALA A 109 ? 0.2670 0.1553 0.1498 0.0558  -0.0794 -0.0429 109 ALA A N   
731  C  CA  . ALA A 109 ? 0.2467 0.1743 0.1818 0.0673  -0.0915 -0.0083 109 ALA A CA  
732  C  C   . ALA A 109 ? 0.1758 0.2024 0.1502 0.0693  -0.0760 -0.0428 109 ALA A C   
733  O  O   . ALA A 109 ? 0.2961 0.1754 0.1661 0.0933  -0.0702 -0.0512 109 ALA A O   
734  C  CB  . ALA A 109 ? 0.2628 0.1330 0.2326 0.0226  -0.0219 -0.0108 109 ALA A CB  
735  N  N   . LEU A 110 ? 0.1285 0.1029 0.1352 0.0153  -0.0653 -0.0420 110 LEU A N   
736  C  CA  . LEU A 110 ? 0.1185 0.1265 0.1608 0.0394  0.0063  -0.0113 110 LEU A CA  
737  C  C   . LEU A 110 ? 0.1554 0.1300 0.0823 0.0514  -0.0054 -0.0110 110 LEU A C   
738  O  O   . LEU A 110 ? 0.1708 0.1658 0.1065 0.0164  0.0356  -0.0175 110 LEU A O   
739  C  CB  . LEU A 110 ? 0.1370 0.1344 0.1548 0.0185  0.0179  -0.0273 110 LEU A CB  
740  C  CG  . LEU A 110 ? 0.1200 0.1970 0.1627 0.0077  -0.0375 -0.0142 110 LEU A CG  
741  C  CD1 . LEU A 110 ? 0.1346 0.1638 0.1924 0.0104  0.0283  -0.0084 110 LEU A CD1 
742  C  CD2 . LEU A 110 ? 0.1322 0.2151 0.2554 0.0265  -0.0888 -0.0479 110 LEU A CD2 
743  N  N   . LEU A 111 ? 0.1295 0.1303 0.1924 0.0417  -0.0052 -0.0052 111 LEU A N   
744  C  CA  . LEU A 111 ? 0.1152 0.1322 0.1558 0.0001  -0.0272 -0.0216 111 LEU A CA  
745  C  C   . LEU A 111 ? 0.1288 0.1205 0.1628 0.0079  0.0016  -0.0199 111 LEU A C   
746  O  O   . LEU A 111 ? 0.1364 0.1340 0.1312 0.0347  -0.0137 -0.0161 111 LEU A O   
747  C  CB  . LEU A 111 ? 0.0901 0.1540 0.1488 -0.0070 -0.0233 -0.0109 111 LEU A CB  
748  C  CG  . LEU A 111 ? 0.1743 0.1770 0.1180 0.0136  -0.0495 -0.0143 111 LEU A CG  
749  C  CD1 . LEU A 111 ? 0.1824 0.1756 0.1905 0.0106  -0.0848 0.0040  111 LEU A CD1 
750  C  CD2 . LEU A 111 ? 0.1830 0.1860 0.1137 0.0337  -0.0616 -0.0137 111 LEU A CD2 
751  N  N   . SER A 112 ? 0.1461 0.1175 0.1651 0.0139  -0.0221 -0.0048 112 SER A N   
752  C  CA  . SER A 112 ? 0.1403 0.1480 0.1253 -0.0195 -0.0212 0.0219  112 SER A CA  
753  C  C   . SER A 112 ? 0.1689 0.1097 0.1923 -0.0388 0.0165  0.0320  112 SER A C   
754  O  O   . SER A 112 ? 0.1914 0.1424 0.2309 -0.0114 0.0096  -0.0034 112 SER A O   
755  C  CB  . SER A 112 ? 0.1355 0.1660 0.1965 -0.0030 -0.0594 0.0378  112 SER A CB  
756  O  OG  . SER A 112 ? 0.1417 0.2079 0.1624 -0.0066 -0.0252 0.0157  112 SER A OG  
757  N  N   . PRO A 113 ? 0.1988 0.1222 0.1692 -0.0036 0.0204  0.0445  113 PRO A N   
758  C  CA  . PRO A 113 ? 0.1877 0.1749 0.1733 -0.0325 -0.0170 0.0202  113 PRO A CA  
759  C  C   . PRO A 113 ? 0.1639 0.1748 0.2315 -0.0382 -0.0114 0.0015  113 PRO A C   
760  O  O   . PRO A 113 ? 0.1691 0.2579 0.2072 -0.0075 -0.0562 0.0184  113 PRO A O   
761  C  CB  . PRO A 113 ? 0.2489 0.1766 0.1752 -0.0554 0.0551  0.0363  113 PRO A CB  
762  C  CG  . PRO A 113 ? 0.3335 0.1987 0.1912 -0.0273 0.0773  0.0278  113 PRO A CG  
763  C  CD  . PRO A 113 ? 0.2411 0.1670 0.2159 0.0166  0.0246  0.0441  113 PRO A CD  
764  N  N   . TYR A 114 ? 0.1446 0.1558 0.1995 -0.0294 -0.0046 -0.0060 114 TYR A N   
765  C  CA  . TYR A 114 ? 0.1555 0.1672 0.1769 -0.0039 -0.0410 -0.0013 114 TYR A CA  
766  C  C   . TYR A 114 ? 0.1704 0.1748 0.1362 0.0018  -0.0273 0.0027  114 TYR A C   
767  O  O   . TYR A 114 ? 0.2417 0.1826 0.1465 -0.0193 -0.0026 -0.0002 114 TYR A O   
768  C  CB  . TYR A 114 ? 0.1215 0.2296 0.1633 -0.0147 -0.0088 0.0290  114 TYR A CB  
769  C  CG  . TYR A 114 ? 0.1494 0.1983 0.1967 0.0394  -0.0152 0.0472  114 TYR A CG  
770  C  CD1 . TYR A 114 ? 0.2898 0.1906 0.1851 -0.0211 0.0336  0.0094  114 TYR A CD1 
771  C  CD2 . TYR A 114 ? 0.2247 0.2526 0.1758 -0.0078 -0.0099 0.0075  114 TYR A CD2 
772  C  CE1 . TYR A 114 ? 0.3167 0.2111 0.3097 -0.0565 0.0052  0.0110  114 TYR A CE1 
773  C  CE2 . TYR A 114 ? 0.2173 0.3432 0.2434 -0.0107 0.0781  0.0569  114 TYR A CE2 
774  C  CZ  . TYR A 114 ? 0.3041 0.2478 0.2042 -0.0246 -0.0349 0.1316  114 TYR A CZ  
775  O  OH  . TYR A 114 ? 0.3830 0.3323 0.3002 -0.0762 -0.0046 0.1599  114 TYR A OH  
776  N  N   . SER A 115 ? 0.2010 0.1419 0.1965 0.0081  -0.0040 0.0739  115 SER A N   
777  C  CA  . SER A 115 ? 0.1867 0.1470 0.1763 -0.0040 -0.0097 0.0329  115 SER A CA  
778  C  C   . SER A 115 ? 0.2207 0.1319 0.1740 0.0030  -0.0064 0.0164  115 SER A C   
779  O  O   . SER A 115 ? 0.1856 0.1231 0.1914 0.0004  0.0248  -0.0069 115 SER A O   
780  C  CB  . SER A 115 ? 0.1827 0.1610 0.2393 -0.0113 -0.0393 0.0167  115 SER A CB  
781  O  OG  . SER A 115 ? 0.2295 0.2231 0.2795 -0.0148 -0.0353 0.0463  115 SER A OG  
782  N  N   . TYR A 116 ? 0.1685 0.1280 0.1540 -0.0048 -0.0133 0.0135  116 TYR A N   
783  C  CA  . TYR A 116 ? 0.1265 0.1053 0.1232 0.0346  0.0014  -0.0291 116 TYR A CA  
784  C  C   . TYR A 116 ? 0.1008 0.1184 0.1271 0.0054  0.0221  -0.0022 116 TYR A C   
785  O  O   . TYR A 116 ? 0.2056 0.1322 0.1680 0.0271  -0.0022 -0.0261 116 TYR A O   
786  C  CB  . TYR A 116 ? 0.1521 0.1915 0.1715 -0.0255 -0.0317 0.0157  116 TYR A CB  
787  C  CG  . TYR A 116 ? 0.1323 0.2276 0.2199 -0.0110 -0.0389 0.0060  116 TYR A CG  
788  C  CD1 . TYR A 116 ? 0.1153 0.2921 0.2362 0.0541  -0.0193 0.0216  116 TYR A CD1 
789  C  CD2 . TYR A 116 ? 0.1645 0.2631 0.4486 0.0318  -0.0204 0.0317  116 TYR A CD2 
790  C  CE1 . TYR A 116 ? 0.2922 0.2706 0.2615 0.1252  -0.0273 -0.0558 116 TYR A CE1 
791  C  CE2 . TYR A 116 ? 0.1357 0.1819 0.4647 0.0083  -0.0862 -0.0433 116 TYR A CE2 
792  C  CZ  . TYR A 116 ? 0.2918 0.1367 0.2887 0.0432  -0.0654 -0.0921 116 TYR A CZ  
793  O  OH  . TYR A 116 ? 0.2269 0.4237 0.8825 0.0798  -0.1392 -0.4179 116 TYR A OH  
794  N  N   . SER A 117 ? 0.1744 0.1167 0.1375 0.0070  0.0617  -0.0323 117 SER A N   
795  C  CA  . SER A 117 ? 0.1864 0.1251 0.1518 -0.0179 0.0177  -0.0282 117 SER A CA  
796  C  C   . SER A 117 ? 0.2031 0.1258 0.1787 -0.0205 -0.0256 -0.0407 117 SER A C   
797  O  O   . SER A 117 ? 0.2117 0.0947 0.1658 -0.0090 -0.0275 -0.0109 117 SER A O   
798  C  CB  . SER A 117 ? 0.1774 0.1571 0.1412 0.0104  -0.0183 -0.0095 117 SER A CB  
799  O  OG  . SER A 117 ? 0.2237 0.1798 0.2083 0.0251  -0.0381 0.0214  117 SER A OG  
800  N  N   . THR A 118 ? 0.1818 0.1403 0.1226 -0.0059 0.0110  -0.0162 118 THR A N   
801  C  CA  . THR A 118 ? 0.1483 0.1200 0.1385 0.0024  -0.0332 -0.0217 118 THR A CA  
802  C  C   . THR A 118 ? 0.1473 0.1424 0.1448 -0.0084 -0.0285 0.0191  118 THR A C   
803  O  O   . THR A 118 ? 0.1948 0.1653 0.1367 0.0062  -0.0215 0.0133  118 THR A O   
804  C  CB  . THR A 118 ? 0.1891 0.2040 0.1717 0.0038  -0.0232 -0.0468 118 THR A CB  
805  O  OG1 . THR A 118 ? 0.1606 0.2653 0.1591 -0.0238 -0.0252 0.0218  118 THR A OG1 
806  C  CG2 . THR A 118 ? 0.2319 0.2017 0.2287 0.0739  -0.0246 -0.0677 118 THR A CG2 
807  N  N   . THR A 119 ? 0.1397 0.1345 0.1500 -0.0070 -0.0176 -0.0012 119 THR A N   
808  C  CA  . THR A 119 ? 0.1227 0.1286 0.1582 -0.0059 -0.0065 -0.0144 119 THR A CA  
809  C  C   . THR A 119 ? 0.1247 0.1469 0.1461 -0.0054 0.0134  -0.0231 119 THR A C   
810  O  O   . THR A 119 ? 0.1411 0.1363 0.2180 0.0050  -0.0555 0.0037  119 THR A O   
811  C  CB  . THR A 119 ? 0.1244 0.1938 0.1320 0.0064  -0.0014 -0.0042 119 THR A CB  
812  O  OG1 . THR A 119 ? 0.1504 0.1841 0.1539 0.0107  0.0110  -0.0018 119 THR A OG1 
813  C  CG2 . THR A 119 ? 0.1736 0.2735 0.1935 0.0366  0.0385  -0.0574 119 THR A CG2 
814  N  N   . ALA A 120 ? 0.1329 0.1227 0.1538 -0.0088 -0.0019 -0.0185 120 ALA A N   
815  C  CA  . ALA A 120 ? 0.0945 0.1145 0.1838 0.0014  0.0148  -0.0006 120 ALA A CA  
816  C  C   . ALA A 120 ? 0.1175 0.1499 0.1072 -0.0074 0.0184  -0.0234 120 ALA A C   
817  O  O   . ALA A 120 ? 0.1415 0.1609 0.1754 -0.0249 -0.0047 -0.0077 120 ALA A O   
818  C  CB  . ALA A 120 ? 0.1152 0.1571 0.2201 0.0436  0.0021  -0.0173 120 ALA A CB  
819  N  N   . VAL A 121 ? 0.1384 0.1283 0.1044 -0.0161 -0.0220 -0.0261 121 VAL A N   
820  C  CA  . VAL A 121 ? 0.1198 0.1845 0.1579 -0.0047 -0.0228 0.0460  121 VAL A CA  
821  C  C   . VAL A 121 ? 0.1685 0.1817 0.1099 -0.0248 -0.0364 0.0671  121 VAL A C   
822  O  O   . VAL A 121 ? 0.1755 0.2463 0.2253 -0.0423 -0.0834 0.0577  121 VAL A O   
823  C  CB  . VAL A 121 ? 0.1663 0.2373 0.2075 0.0022  0.0152  0.0367  121 VAL A CB  
824  C  CG1 . VAL A 121 ? 0.2756 0.2854 0.1540 -0.0837 0.0068  0.0096  121 VAL A CG1 
825  C  CG2 . VAL A 121 ? 0.2485 0.2813 0.2588 0.0961  -0.0149 0.0014  121 VAL A CG2 
826  N  N   . VAL A 122 ? 0.1266 0.1943 0.1476 -0.0265 -0.0253 0.0085  122 VAL A N   
827  C  CA  . VAL A 122 ? 0.1462 0.2307 0.1544 -0.0070 -0.0455 0.0401  122 VAL A CA  
828  C  C   . VAL A 122 ? 0.1809 0.1540 0.2564 -0.0439 -0.0369 0.0287  122 VAL A C   
829  O  O   . VAL A 122 ? 0.2016 0.2636 0.2697 -0.0908 -0.0638 0.0724  122 VAL A O   
830  C  CB  . VAL A 122 ? 0.1551 0.1896 0.2309 0.0020  -0.0184 0.0469  122 VAL A CB  
831  C  CG1 . VAL A 122 ? 0.1968 0.2121 0.2066 0.0441  -0.0354 0.0308  122 VAL A CG1 
832  C  CG2 . VAL A 122 ? 0.1527 0.2231 0.2510 -0.0040 -0.0127 0.0604  122 VAL A CG2 
833  N  N   . THR A 123 ? 0.1938 0.2317 0.1797 -0.0430 0.0150  0.0662  123 THR A N   
834  C  CA  . THR A 123 ? 0.1905 0.3090 0.2233 -0.0355 -0.0050 0.1341  123 THR A CA  
835  C  C   . THR A 123 ? 0.1578 0.3780 0.1524 0.0078  0.0095  0.1188  123 THR A C   
836  O  O   . THR A 123 ? 0.1758 0.2404 0.2647 -0.0226 -0.0212 0.1056  123 THR A O   
837  C  CB  . THR A 123 ? 0.2592 0.4389 0.4321 0.0976  -0.0346 0.0525  123 THR A CB  
838  O  OG1 . THR A 123 ? 0.4451 0.4307 0.5024 -0.0360 0.0678  -0.0403 123 THR A OG1 
839  C  CG2 . THR A 123 ? 0.3440 0.5443 0.2344 0.0670  -0.0639 0.0932  123 THR A CG2 
840  N  N   . ASN A 124 ? 0.2852 0.3690 0.2733 -0.0412 0.0587  0.1398  124 ASN A N   
841  C  CA  . ASN A 124 ? 0.4303 0.4510 0.4917 0.1788  -0.2388 0.0408  124 ASN A CA  
842  C  C   . ASN A 124 ? 0.5908 0.4726 0.4634 0.1351  0.0553  0.1922  124 ASN A C   
843  O  O   . ASN A 124 ? 0.5642 0.3412 0.5734 0.0279  0.2194  0.2032  124 ASN A O   
844  C  CB  . ASN A 124 ? 0.4091 0.6188 0.3682 0.1368  -0.0619 0.0983  124 ASN A CB  
845  C  CG  . ASN A 124 ? 0.3589 0.4412 0.1834 0.1596  -0.0681 -0.0474 124 ASN A CG  
846  O  OD1 . ASN A 124 ? 0.4324 0.7186 0.3948 0.0410  0.1011  -0.0370 124 ASN A OD1 
847  N  ND2 . ASN A 124 ? 0.7138 0.4528 0.3481 0.0929  -0.1266 -0.1547 124 ASN A ND2 
848  C  C   . CYS B 10  ? 0.4490 0.4658 0.4951 0.0178  0.1198  0.1241  10  CYS B C   
849  O  O   . CYS B 10  ? 0.3720 0.6290 0.6038 0.0451  0.1003  0.1003  10  CYS B O   
850  C  CB  . CYS B 10  ? 0.5432 0.5245 0.4311 -0.0373 0.1424  -0.1865 10  CYS B CB  
851  N  N   . PRO B 11  ? 0.5099 0.3080 0.3428 -0.0167 0.2182  0.1137  11  PRO B N   
852  C  CA  . PRO B 11  ? 0.4319 0.3361 0.3568 0.1264  0.1414  0.0499  11  PRO B CA  
853  C  C   . PRO B 11  ? 0.4118 0.2064 0.3692 -0.0445 0.1405  -0.0207 11  PRO B C   
854  O  O   . PRO B 11  ? 0.4693 0.2374 0.3068 -0.0818 0.1681  -0.0157 11  PRO B O   
855  C  CB  . PRO B 11  ? 0.5623 0.5567 0.3436 -0.1321 0.1589  -0.0427 11  PRO B CB  
856  C  CG  . PRO B 11  ? 0.3195 0.4687 0.4874 -0.2191 0.2435  0.0666  11  PRO B CG  
857  C  CD  . PRO B 11  ? 0.4098 0.3928 0.3902 -0.1187 0.1832  0.0006  11  PRO B CD  
858  N  N   . LEU B 12  ? 0.3766 0.2247 0.2455 -0.0093 0.1551  0.0212  12  LEU B N   
859  C  CA  . LEU B 12  ? 0.3943 0.1881 0.2780 -0.0049 0.0785  0.0748  12  LEU B CA  
860  C  C   . LEU B 12  ? 0.4195 0.2129 0.2436 0.0035  0.0797  -0.0007 12  LEU B C   
861  O  O   . LEU B 12  ? 0.3803 0.2098 0.3626 -0.0440 0.1925  -0.0209 12  LEU B O   
862  C  CB  . LEU B 12  ? 0.3913 0.1836 0.2605 0.0887  0.1385  -0.0619 12  LEU B CB  
863  C  CG  . LEU B 12  ? 0.3733 0.3572 0.2835 0.0227  0.0516  0.0093  12  LEU B CG  
864  C  CD1 . LEU B 12  ? 0.2557 0.2611 0.3823 0.0840  0.0729  0.0304  12  LEU B CD1 
865  C  CD2 . LEU B 12  ? 0.3227 0.3064 0.3405 0.0372  0.0599  -0.0284 12  LEU B CD2 
866  N  N   . MET B 13  ? 0.4085 0.2039 0.3221 -0.0142 0.1166  0.0156  13  MET B N   
867  C  CA  A MET B 13  ? 0.3567 0.3049 0.1882 -0.0337 0.1160  0.0019  13  MET B CA  
868  C  CA  B MET B 13  ? 0.3406 0.2732 0.1734 -0.0231 0.0788  0.0176  13  MET B CA  
869  C  C   . MET B 13  ? 0.3438 0.1940 0.1857 -0.0775 0.0993  -0.0108 13  MET B C   
870  O  O   . MET B 13  ? 0.3806 0.1752 0.2017 0.0043  0.0354  -0.0169 13  MET B O   
871  C  CB  A MET B 13  ? 0.2945 0.1336 0.2266 -0.0209 0.1124  -0.1330 13  MET B CB  
872  C  CB  B MET B 13  ? 0.4614 0.3297 0.1140 -0.0320 0.0009  0.0240  13  MET B CB  
873  C  CG  A MET B 13  ? 0.4426 0.2447 0.2746 -0.0160 0.1680  -0.1623 13  MET B CG  
874  C  CG  B MET B 13  ? 0.4949 0.3694 0.2521 -0.0139 0.0273  0.0230  13  MET B CG  
875  S  SD  A MET B 13  ? 0.5619 0.5009 0.5612 -0.0972 -0.0464 0.0831  13  MET B SD  
876  S  SD  B MET B 13  ? 0.4099 0.3435 0.3150 0.0021  0.0536  -0.0026 13  MET B SD  
877  C  CE  A MET B 13  ? 0.5997 0.5532 0.5409 -0.2326 -0.1071 -0.0326 13  MET B CE  
878  C  CE  B MET B 13  ? 0.5252 0.3212 0.3465 0.1536  0.1267  0.0742  13  MET B CE  
879  N  N   . VAL B 14  ? 0.3448 0.1735 0.1485 -0.0553 0.1064  -0.0636 14  VAL B N   
880  C  CA  . VAL B 14  ? 0.2798 0.2398 0.1706 -0.0502 0.1003  -0.0015 14  VAL B CA  
881  C  C   . VAL B 14  ? 0.2708 0.2894 0.1507 -0.0489 0.0359  -0.0494 14  VAL B C   
882  O  O   . VAL B 14  ? 0.3797 0.2279 0.1961 -0.0884 0.1331  -0.0828 14  VAL B O   
883  C  CB  . VAL B 14  ? 0.2967 0.2266 0.2045 -0.0168 0.1038  -0.0005 14  VAL B CB  
884  C  CG1 . VAL B 14  ? 0.3722 0.2271 0.2391 -0.0171 0.1736  -0.0143 14  VAL B CG1 
885  C  CG2 . VAL B 14  ? 0.2616 0.2533 0.3146 0.0155  0.1208  0.0009  14  VAL B CG2 
886  N  N   . LYS B 15  ? 0.3055 0.2281 0.2595 -0.0898 0.0757  -0.0295 15  LYS B N   
887  C  CA  . LYS B 15  ? 0.2538 0.2469 0.1788 -0.0489 0.0570  -0.0071 15  LYS B CA  
888  C  C   . LYS B 15  ? 0.3292 0.2367 0.1996 -0.0610 0.0683  -0.0100 15  LYS B C   
889  O  O   . LYS B 15  ? 0.3229 0.2000 0.1882 -0.0642 0.0922  -0.0052 15  LYS B O   
890  C  CB  . LYS B 15  ? 0.3290 0.2718 0.2219 0.0110  0.0003  -0.0364 15  LYS B CB  
891  C  CG  . LYS B 15  ? 0.3362 0.3829 0.3725 0.0273  0.0041  0.0134  15  LYS B CG  
892  C  CD  . LYS B 15  ? 0.3490 0.4796 0.4494 0.0081  -0.0965 0.0513  15  LYS B CD  
893  C  CE  . LYS B 15  ? 0.4815 0.4733 0.5431 -0.1242 -0.0593 -0.0088 15  LYS B CE  
894  N  N   . VAL B 16  ? 0.3007 0.2016 0.1190 -0.0318 0.0968  -0.0332 16  VAL B N   
895  C  CA  . VAL B 16  ? 0.2130 0.2154 0.1410 -0.0079 0.0589  -0.0056 16  VAL B CA  
896  C  C   . VAL B 16  ? 0.2457 0.1912 0.1783 -0.0167 0.0719  -0.0395 16  VAL B C   
897  O  O   . VAL B 16  ? 0.2075 0.2327 0.1411 -0.0058 0.0536  -0.0311 16  VAL B O   
898  C  CB  . VAL B 16  ? 0.1927 0.1773 0.1448 -0.0105 0.0480  -0.0014 16  VAL B CB  
899  C  CG1 . VAL B 16  ? 0.2244 0.2371 0.1612 0.0259  0.0556  0.0291  16  VAL B CG1 
900  C  CG2 . VAL B 16  ? 0.2487 0.1986 0.1511 -0.0583 0.0717  -0.0108 16  VAL B CG2 
901  N  N   . LEU B 17  ? 0.2110 0.1852 0.1373 -0.0269 0.0503  -0.0127 17  LEU B N   
902  C  CA  . LEU B 17  ? 0.2464 0.1948 0.1267 -0.0181 0.0463  -0.0174 17  LEU B CA  
903  C  C   . LEU B 17  ? 0.2364 0.1345 0.1764 -0.0051 -0.0035 0.0068  17  LEU B C   
904  O  O   . LEU B 17  ? 0.2395 0.1415 0.1591 -0.0313 0.0162  -0.0309 17  LEU B O   
905  C  CB  . LEU B 17  ? 0.2373 0.2068 0.1189 -0.0239 0.0227  -0.0413 17  LEU B CB  
906  C  CG  . LEU B 17  ? 0.3137 0.2386 0.2135 -0.0377 0.0255  0.0229  17  LEU B CG  
907  C  CD1 . LEU B 17  ? 0.5595 0.2315 0.3355 0.0169  0.0320  -0.0453 17  LEU B CD1 
908  C  CD2 . LEU B 17  ? 0.2728 0.3858 0.1837 0.0084  -0.0162 0.0025  17  LEU B CD2 
909  N  N   . ASP B 18  ? 0.2068 0.1616 0.1257 -0.0084 -0.0194 -0.0417 18  ASP B N   
910  C  CA  . ASP B 18  ? 0.1570 0.1755 0.1995 -0.0143 0.0092  -0.0167 18  ASP B CA  
911  C  C   . ASP B 18  ? 0.1617 0.1257 0.1407 0.0000  0.0081  0.0035  18  ASP B C   
912  O  O   . ASP B 18  ? 0.1582 0.2079 0.1819 -0.0074 0.0074  0.0081  18  ASP B O   
913  C  CB  . ASP B 18  ? 0.1897 0.1994 0.1957 0.0192  0.0050  -0.0550 18  ASP B CB  
914  C  CG  . ASP B 18  ? 0.1644 0.1821 0.1336 0.0366  -0.0352 -0.0417 18  ASP B CG  
915  O  OD1 . ASP B 18  ? 0.1874 0.1539 0.1516 -0.0274 -0.0135 0.0099  18  ASP B OD1 
916  O  OD2 . ASP B 18  ? 0.1816 0.1657 0.2443 0.0180  -0.0033 -0.0496 18  ASP B OD2 
917  N  N   . ALA B 19  ? 0.1606 0.1667 0.1481 0.0144  0.0199  0.0020  19  ALA B N   
918  C  CA  . ALA B 19  ? 0.1402 0.1496 0.1492 0.0227  0.0036  0.0441  19  ALA B CA  
919  C  C   . ALA B 19  ? 0.1542 0.1581 0.1416 -0.0091 0.0156  -0.0012 19  ALA B C   
920  O  O   . ALA B 19  ? 0.1218 0.2470 0.1707 -0.0350 0.0098  0.0066  19  ALA B O   
921  C  CB  . ALA B 19  ? 0.1737 0.1408 0.2213 -0.0061 0.0499  0.0070  19  ALA B CB  
922  N  N   . VAL B 20  ? 0.1544 0.1553 0.1776 0.0016  -0.0099 -0.0059 20  VAL B N   
923  C  CA  . VAL B 20  ? 0.1668 0.1856 0.2011 -0.0336 0.0081  0.0320  20  VAL B CA  
924  C  C   . VAL B 20  ? 0.1905 0.1732 0.2801 -0.0246 -0.0155 0.0106  20  VAL B C   
925  O  O   . VAL B 20  ? 0.2052 0.2535 0.2121 -0.0868 -0.0290 0.0362  20  VAL B O   
926  C  CB  . VAL B 20  ? 0.1905 0.2074 0.2538 -0.0725 -0.0388 0.0646  20  VAL B CB  
927  C  CG1 . VAL B 20  ? 0.2715 0.3002 0.4121 -0.1516 -0.1901 0.1981  20  VAL B CG1 
928  C  CG2 . VAL B 20  ? 0.2163 0.3317 0.2887 -0.0534 -0.0757 0.0485  20  VAL B CG2 
929  N  N   . ARG B 21  ? 0.1837 0.2391 0.2215 -0.0648 -0.0471 0.0148  21  ARG B N   
930  C  CA  . ARG B 21  ? 0.1383 0.2437 0.1684 -0.1103 0.0008  0.0360  21  ARG B CA  
931  C  C   . ARG B 21  ? 0.1643 0.2352 0.1988 -0.0603 -0.0641 -0.0079 21  ARG B C   
932  O  O   . ARG B 21  ? 0.1672 0.3472 0.2438 -0.0729 -0.0615 -0.0572 21  ARG B O   
933  C  CB  . ARG B 21  ? 0.2730 0.2546 0.2677 -0.0324 0.0201  -0.0018 21  ARG B CB  
934  C  CG  . ARG B 21  ? 0.3499 0.2516 0.2740 -0.0542 0.0028  0.0093  21  ARG B CG  
935  C  CD  . ARG B 21  ? 0.3541 0.2961 0.3194 -0.0303 0.0521  0.0319  21  ARG B CD  
936  N  NE  . ARG B 21  ? 0.3917 0.2469 0.3282 -0.0738 0.0068  0.0179  21  ARG B NE  
937  C  CZ  . ARG B 21  ? 0.4655 0.2837 0.3671 -0.1012 0.0501  -0.0957 21  ARG B CZ  
938  N  NH1 . ARG B 21  ? 0.4967 0.3863 0.3220 -0.1524 0.0264  -0.0420 21  ARG B NH1 
939  N  NH2 . ARG B 21  ? 0.3205 0.5611 0.4146 -0.0067 0.0151  -0.0562 21  ARG B NH2 
940  N  N   . GLY B 22  ? 0.2236 0.2606 0.2179 -0.0376 0.0022  -0.0079 22  GLY B N   
941  C  CA  . GLY B 22  ? 0.2536 0.2604 0.2384 0.0245  -0.0058 -0.0405 22  GLY B CA  
942  C  C   . GLY B 22  ? 0.1439 0.2709 0.2162 -0.0192 -0.0508 -0.0076 22  GLY B C   
943  O  O   . GLY B 22  ? 0.2249 0.3461 0.2081 0.0257  -0.0694 -0.0619 22  GLY B O   
944  N  N   . SER B 23  ? 0.1770 0.2753 0.1988 0.0100  0.0272  -0.0652 23  SER B N   
945  C  CA  . SER B 23  ? 0.1884 0.2831 0.2186 0.0572  0.0491  -0.0505 23  SER B CA  
946  C  C   . SER B 23  ? 0.2488 0.2547 0.1739 0.0144  0.0313  -0.0796 23  SER B C   
947  O  O   . SER B 23  ? 0.2074 0.2423 0.1738 -0.0049 0.0036  -0.0467 23  SER B O   
948  C  CB  . SER B 23  ? 0.3575 0.2806 0.3917 -0.0122 0.0484  -0.0555 23  SER B CB  
949  O  OG  . SER B 23  ? 0.4348 0.2407 0.5579 0.0315  0.1127  0.0314  23  SER B OG  
950  N  N   . PRO B 24  ? 0.2483 0.2244 0.1599 -0.0195 -0.0157 -0.0524 24  PRO B N   
951  C  CA  . PRO B 24  ? 0.2401 0.1669 0.1789 0.0033  0.0433  -0.0453 24  PRO B CA  
952  C  C   . PRO B 24  ? 0.2239 0.2235 0.2737 -0.0015 0.0171  0.0008  24  PRO B C   
953  O  O   . PRO B 24  ? 0.2591 0.2254 0.2204 -0.0263 0.0036  -0.0283 24  PRO B O   
954  C  CB  . PRO B 24  ? 0.2813 0.3558 0.1705 -0.0627 0.0581  -0.0266 24  PRO B CB  
955  C  CG  . PRO B 24  ? 0.3212 0.4792 0.2568 -0.0767 0.0434  0.0634  24  PRO B CG  
956  C  CD  . PRO B 24  ? 0.2911 0.2676 0.1210 -0.0392 -0.0173 0.0167  24  PRO B CD  
957  N  N   . ALA B 25  ? 0.2517 0.2044 0.2207 -0.0452 0.0423  0.0041  25  ALA B N   
958  C  CA  . ALA B 25  ? 0.2367 0.2399 0.0915 -0.0434 0.0455  -0.0324 25  ALA B CA  
959  C  C   . ALA B 25  ? 0.1739 0.1935 0.1426 -0.0306 0.0390  -0.0406 25  ALA B C   
960  O  O   . ALA B 25  ? 0.2369 0.2054 0.1948 -0.0467 0.0356  -0.0355 25  ALA B O   
961  C  CB  . ALA B 25  ? 0.1898 0.1821 0.1804 -0.0333 -0.0125 -0.0274 25  ALA B CB  
962  N  N   . ILE B 26  ? 0.2717 0.1787 0.2322 -0.0317 0.0653  -0.0432 26  ILE B N   
963  C  CA  . ILE B 26  ? 0.2430 0.2060 0.1502 -0.0120 -0.0051 0.0089  26  ILE B CA  
964  C  C   . ILE B 26  ? 0.2162 0.1704 0.2002 -0.0466 0.0348  -0.0462 26  ILE B C   
965  O  O   . ILE B 26  ? 0.2810 0.2680 0.1852 -0.0533 0.0631  -0.0156 26  ILE B O   
966  C  CB  . ILE B 26  ? 0.2993 0.2507 0.2083 -0.0286 -0.0205 -0.0449 26  ILE B CB  
967  C  CG1 . ILE B 26  ? 0.3083 0.2535 0.1688 -0.0320 0.0093  -0.0160 26  ILE B CG1 
968  C  CG2 . ILE B 26  ? 0.4779 0.1966 0.3528 -0.0242 0.0824  -0.0619 26  ILE B CG2 
969  C  CD1 . ILE B 26  ? 0.2831 0.4926 0.3109 -0.0431 -0.1070 -0.0416 26  ILE B CD1 
970  N  N   . ASN B 27  ? 0.2545 0.2197 0.2136 -0.0706 0.0700  -0.0346 27  ASN B N   
971  C  CA  . ASN B 27  ? 0.2205 0.2073 0.2852 -0.0909 0.0339  -0.0071 27  ASN B CA  
972  C  C   . ASN B 27  ? 0.1839 0.2402 0.3115 -0.0580 0.0456  -0.0422 27  ASN B C   
973  O  O   . ASN B 27  ? 0.3443 0.2609 0.2710 -0.0088 0.0510  -0.0485 27  ASN B O   
974  C  CB  . ASN B 27  ? 0.2954 0.1910 0.3307 -0.0293 0.0392  -0.0485 27  ASN B CB  
975  C  CG  . ASN B 27  ? 0.3424 0.4978 0.3786 -0.0995 0.2132  -0.1312 27  ASN B CG  
976  O  OD1 . ASN B 27  ? 0.3462 0.4160 0.4924 -0.0521 0.1975  -0.0686 27  ASN B OD1 
977  N  N   . VAL B 28  ? 0.2225 0.2158 0.1791 -0.0794 0.0204  -0.0318 28  VAL B N   
978  C  CA  . VAL B 28  ? 0.1663 0.2385 0.2039 -0.0338 -0.0391 0.0335  28  VAL B CA  
979  C  C   . VAL B 28  ? 0.2191 0.2478 0.1705 -0.0514 0.0496  -0.0528 28  VAL B C   
980  O  O   . VAL B 28  ? 0.2331 0.2335 0.2283 -0.0082 0.0371  -0.0416 28  VAL B O   
981  C  CB  . VAL B 28  ? 0.1937 0.2581 0.1507 -0.0209 0.0308  0.0446  28  VAL B CB  
982  C  CG1 . VAL B 28  ? 0.2630 0.2869 0.1350 0.0102  0.0269  0.0164  28  VAL B CG1 
983  C  CG2 . VAL B 28  ? 0.2020 0.3742 0.1858 -0.0653 0.0372  0.0178  28  VAL B CG2 
984  N  N   . ALA B 29  ? 0.2056 0.1796 0.1340 -0.0200 0.0816  -0.0130 29  ALA B N   
985  C  CA  . ALA B 29  ? 0.2076 0.1963 0.2053 -0.0477 0.0995  -0.0237 29  ALA B CA  
986  C  C   . ALA B 29  ? 0.2177 0.1903 0.1885 -0.0930 0.0590  0.0088  29  ALA B C   
987  O  O   . ALA B 29  ? 0.2359 0.2248 0.1744 -0.0082 0.0089  -0.0165 29  ALA B O   
988  C  CB  . ALA B 29  ? 0.1940 0.2314 0.3144 -0.0163 0.0947  -0.0670 29  ALA B CB  
989  N  N   . VAL B 30  ? 0.2604 0.1604 0.1343 -0.0532 0.1133  -0.0121 30  VAL B N   
990  C  CA  . VAL B 30  ? 0.2808 0.1785 0.1751 -0.0171 0.1050  -0.0566 30  VAL B CA  
991  C  C   . VAL B 30  ? 0.2928 0.1820 0.1925 -0.0412 0.0723  -0.0316 30  VAL B C   
992  O  O   . VAL B 30  ? 0.2577 0.1930 0.1718 -0.0368 0.0447  -0.0362 30  VAL B O   
993  C  CB  . VAL B 30  ? 0.2426 0.1743 0.1485 0.0140  0.1319  -0.0714 30  VAL B CB  
994  C  CG1 . VAL B 30  ? 0.3621 0.1500 0.2818 0.0000  0.1353  -0.0726 30  VAL B CG1 
995  C  CG2 . VAL B 30  ? 0.2007 0.2426 0.2243 0.0175  0.0920  -0.0594 30  VAL B CG2 
996  N  N   . HIS B 31  ? 0.3066 0.2098 0.2200 -0.0652 0.0641  -0.0339 31  HIS B N   
997  C  CA  . HIS B 31  ? 0.2852 0.1936 0.3120 -0.0570 0.0341  -0.0499 31  HIS B CA  
998  C  C   . HIS B 31  ? 0.2682 0.1597 0.2404 -0.0529 0.0345  0.0209  31  HIS B C   
999  O  O   . HIS B 31  ? 0.3879 0.1905 0.3182 -0.0754 0.1001  -0.0512 31  HIS B O   
1000 C  CB  . HIS B 31  ? 0.2833 0.2408 0.3914 -0.0209 0.0310  -0.0196 31  HIS B CB  
1001 C  CG  . HIS B 31  ? 0.3602 0.2374 0.3744 0.0054  -0.0496 0.0086  31  HIS B CG  
1002 N  ND1 . HIS B 31  ? 0.4871 0.3063 0.3425 -0.0396 -0.0258 0.0505  31  HIS B ND1 
1003 C  CD2 . HIS B 31  ? 0.3092 0.3421 0.5313 -0.0195 -0.0207 0.0440  31  HIS B CD2 
1004 C  CE1 . HIS B 31  ? 0.4367 0.3209 0.6702 0.0609  0.0081  0.0678  31  HIS B CE1 
1005 N  NE2 . HIS B 31  ? 0.3924 0.3245 0.6261 0.1134  -0.0125 -0.0465 31  HIS B NE2 
1006 N  N   . VAL B 32  ? 0.3133 0.1896 0.2471 -0.0780 0.0995  -0.0122 32  VAL B N   
1007 C  CA  . VAL B 32  ? 0.3512 0.2005 0.1911 -0.0233 0.0579  -0.0341 32  VAL B CA  
1008 C  C   . VAL B 32  ? 0.3342 0.1967 0.2521 -0.0447 0.0464  -0.0498 32  VAL B C   
1009 O  O   . VAL B 32  ? 0.3664 0.2085 0.3300 -0.0748 0.1061  -0.0152 32  VAL B O   
1010 C  CB  . VAL B 32  ? 0.2051 0.2072 0.1786 -0.0255 0.0573  -0.0484 32  VAL B CB  
1011 C  CG1 . VAL B 32  ? 0.2188 0.1774 0.2199 -0.0773 0.0339  -0.0344 32  VAL B CG1 
1012 C  CG2 . VAL B 32  ? 0.2246 0.2063 0.2139 -0.0703 0.0280  -0.0372 32  VAL B CG2 
1013 N  N   . PHE B 33  ? 0.3219 0.1732 0.2368 -0.0616 0.0019  -0.0053 33  PHE B N   
1014 C  CA  . PHE B 33  ? 0.3619 0.1979 0.4164 -0.0106 0.0272  -0.1190 33  PHE B CA  
1015 C  C   . PHE B 33  ? 0.2596 0.1970 0.4497 -0.0409 -0.0556 0.0189  33  PHE B C   
1016 O  O   . PHE B 33  ? 0.2878 0.2132 0.2909 -0.0399 0.0582  0.0029  33  PHE B O   
1017 C  CB  . PHE B 33  ? 0.4718 0.2482 0.4871 -0.0494 -0.0751 -0.1072 33  PHE B CB  
1018 C  CG  . PHE B 33  ? 0.4440 0.2894 0.5493 -0.0714 -0.0907 -0.0475 33  PHE B CG  
1019 C  CD1 . PHE B 33  ? 0.5082 0.3090 0.7379 -0.0166 -0.0555 -0.0012 33  PHE B CD1 
1020 C  CD2 . PHE B 33  ? 0.4691 0.2048 0.3913 -0.0907 -0.0884 -0.0247 33  PHE B CD2 
1021 C  CE1 . PHE B 33  ? 0.4147 0.3237 0.6736 -0.0323 -0.0040 0.0060  33  PHE B CE1 
1022 C  CE2 . PHE B 33  ? 0.5255 0.2121 0.5083 -0.1127 -0.0126 -0.0251 33  PHE B CE2 
1023 C  CZ  . PHE B 33  ? 0.4998 0.2435 0.4203 -0.1583 -0.0969 0.0168  33  PHE B CZ  
1024 N  N   . ARG B 34  ? 0.2962 0.2467 0.4506 -0.0211 0.0964  0.0212  34  ARG B N   
1025 C  CA  . ARG B 34  ? 0.3752 0.2546 0.4167 -0.0601 -0.0499 -0.0466 34  ARG B CA  
1026 C  C   . ARG B 34  ? 0.4387 0.2567 0.4836 -0.0279 -0.1012 -0.0613 34  ARG B C   
1027 O  O   . ARG B 34  ? 0.4782 0.3667 0.6157 0.0301  -0.1192 -0.1464 34  ARG B O   
1028 C  CB  . ARG B 34  ? 0.3581 0.2551 0.4994 -0.0544 -0.0091 -0.0408 34  ARG B CB  
1029 C  CG  . ARG B 34  ? 0.3969 0.2774 0.4238 -0.0386 0.0421  -0.0105 34  ARG B CG  
1030 C  CD  . ARG B 34  ? 0.4786 0.2998 0.3737 -0.1298 -0.0910 0.0243  34  ARG B CD  
1031 N  NE  . ARG B 34  ? 0.4748 0.4814 0.4552 0.0507  0.0404  0.1268  34  ARG B NE  
1032 N  N   . LYS B 35  ? 0.3199 0.2626 0.5514 0.0280  -0.0935 -0.0803 35  LYS B N   
1033 C  CA  . LYS B 35  ? 0.4035 0.4004 0.3897 0.0202  -0.0986 0.0069  35  LYS B CA  
1034 C  C   . LYS B 35  ? 0.5397 0.3515 0.5435 -0.0376 0.0010  0.0337  35  LYS B C   
1035 O  O   . LYS B 35  ? 0.3714 0.3018 0.4706 -0.1285 0.0255  -0.0235 35  LYS B O   
1036 C  CB  . LYS B 35  ? 0.3527 0.3425 0.4266 0.0271  -0.0157 0.0301  35  LYS B CB  
1037 C  CG  . LYS B 35  ? 0.5017 0.4322 0.5139 -0.0206 -0.0554 -0.0495 35  LYS B CG  
1038 C  CD  . LYS B 35  ? 0.5347 0.5884 0.3744 0.0330  -0.0324 -0.0569 35  LYS B CD  
1039 N  N   . ALA B 36  ? 0.5011 0.4716 0.4816 -0.0486 0.0184  0.0366  36  ALA B N   
1040 C  CA  . ALA B 36  ? 0.4319 0.5471 0.5284 -0.0898 0.0243  -0.0203 36  ALA B CA  
1041 C  C   . ALA B 36  ? 0.5670 0.5658 0.4379 0.0185  0.0082  -0.1029 36  ALA B C   
1042 O  O   . ALA B 36  ? 0.5198 0.4349 0.4436 -0.0415 -0.1141 -0.0935 36  ALA B O   
1043 N  N   . TRP B 41  ? 0.5234 0.8946 0.7003 0.1550  -0.1485 0.0314  41  TRP B N   
1044 C  CA  . TRP B 41  ? 0.4136 0.5272 0.5976 0.0585  -0.0095 0.0260  41  TRP B CA  
1045 C  C   . TRP B 41  ? 0.6942 0.4395 0.6325 0.0922  -0.0780 -0.0234 41  TRP B C   
1046 O  O   . TRP B 41  ? 0.7439 0.3909 0.8475 0.1061  -0.0989 -0.0670 41  TRP B O   
1047 C  CB  . TRP B 41  ? 0.5681 0.5213 0.5683 -0.0026 -0.0292 0.0206  41  TRP B CB  
1048 C  CG  . TRP B 41  ? 0.5263 0.3916 0.5061 -0.0048 -0.0538 -0.0266 41  TRP B CG  
1049 C  CD1 . TRP B 41  ? 0.5412 0.5276 0.5199 0.0753  0.0267  -0.1024 41  TRP B CD1 
1050 C  CD2 . TRP B 41  ? 0.5466 0.5779 0.4722 0.0908  -0.1486 0.0209  41  TRP B CD2 
1051 N  NE1 . TRP B 41  ? 0.6440 0.4198 0.4819 0.2428  -0.0529 -0.0024 41  TRP B NE1 
1052 C  CE2 . TRP B 41  ? 0.6176 0.4666 0.4660 0.0683  -0.1050 0.0367  41  TRP B CE2 
1053 C  CE3 . TRP B 41  ? 0.5944 0.2167 0.5174 -0.0066 0.0239  -0.0026 41  TRP B CE3 
1054 C  CZ2 . TRP B 41  ? 0.7300 0.4769 0.3737 0.1477  -0.0772 -0.0313 41  TRP B CZ2 
1055 C  CZ3 . TRP B 41  ? 0.3536 0.3367 0.3085 -0.0343 -0.0224 0.0515  41  TRP B CZ3 
1056 C  CH2 . TRP B 41  ? 0.5763 0.3813 0.3948 -0.0997 0.1424  0.0538  41  TRP B CH2 
1057 N  N   . GLU B 42  ? 0.3873 0.5194 0.5114 0.1277  -0.1259 -0.0962 42  GLU B N   
1058 C  CA  . GLU B 42  ? 0.4010 0.4603 0.4471 0.0060  -0.0735 -0.0542 42  GLU B CA  
1059 C  C   . GLU B 42  ? 0.3947 0.3906 0.7074 0.0178  -0.0451 -0.1700 42  GLU B C   
1060 O  O   . GLU B 42  ? 0.2953 0.3740 0.6279 -0.0531 0.0195  -0.0121 42  GLU B O   
1061 C  CB  . GLU B 42  ? 0.5234 0.4530 0.4836 -0.0265 0.0306  -0.0586 42  GLU B CB  
1062 N  N   . PRO B 43  ? 0.5080 0.3126 0.8163 0.0639  -0.0761 -0.0715 43  PRO B N   
1063 C  CA  . PRO B 43  ? 0.5574 0.3086 0.4800 0.0677  -0.0574 -0.0320 43  PRO B CA  
1064 C  C   . PRO B 43  ? 0.3492 0.3781 0.3948 0.0289  0.1277  -0.0608 43  PRO B C   
1065 O  O   . PRO B 43  ? 0.2836 0.4539 0.7248 0.0479  0.1754  -0.0026 43  PRO B O   
1066 C  CB  . PRO B 43  ? 0.4483 0.3010 0.5213 -0.0471 -0.0005 -0.0657 43  PRO B CB  
1067 C  CG  . PRO B 43  ? 0.4747 0.3170 0.5825 0.0088  -0.0944 -0.1286 43  PRO B CG  
1068 C  CD  . PRO B 43  ? 0.4854 0.2845 0.5881 0.0255  -0.0581 -0.1065 43  PRO B CD  
1069 N  N   . PHE B 44  ? 0.2850 0.2746 0.4773 -0.0562 0.0597  0.0088  44  PHE B N   
1070 C  CA  . PHE B 44  ? 0.3317 0.2847 0.3332 -0.0212 0.1291  -0.0503 44  PHE B CA  
1071 C  C   . PHE B 44  ? 0.3978 0.3094 0.3381 -0.1067 0.2156  -0.0899 44  PHE B C   
1072 O  O   . PHE B 44  ? 0.3255 0.4005 0.3304 -0.0983 0.1235  0.0302  44  PHE B O   
1073 C  CB  . PHE B 44  ? 0.2659 0.2030 0.3388 -0.0788 0.1595  -0.0352 44  PHE B CB  
1074 C  CG  . PHE B 44  ? 0.3562 0.2475 0.3164 -0.0656 0.1585  -0.0805 44  PHE B CG  
1075 C  CD1 . PHE B 44  ? 0.4589 0.2379 0.4104 0.0028  0.1711  0.0685  44  PHE B CD1 
1076 C  CD2 . PHE B 44  ? 0.3559 0.1884 0.2914 -0.1056 0.1490  0.0402  44  PHE B CD2 
1077 C  CE1 . PHE B 44  ? 0.3169 0.2100 0.4169 -0.0887 0.2325  0.0973  44  PHE B CE1 
1078 C  CE2 . PHE B 44  ? 0.4070 0.2223 0.2305 -0.0793 0.1343  -0.0299 44  PHE B CE2 
1079 C  CZ  . PHE B 44  ? 0.3383 0.3048 0.2774 -0.0911 0.1539  -0.0054 44  PHE B CZ  
1080 N  N   . ALA B 45  ? 0.3410 0.1623 0.2475 -0.0242 0.1536  -0.0186 45  ALA B N   
1081 C  CA  . ALA B 45  ? 0.3608 0.2691 0.1605 -0.0091 0.1770  -0.0844 45  ALA B CA  
1082 C  C   . ALA B 45  ? 0.3837 0.2145 0.2130 -0.0054 0.0706  0.0067  45  ALA B C   
1083 O  O   . ALA B 45  ? 0.3721 0.2539 0.2453 -0.1000 0.0141  0.0111  45  ALA B O   
1084 C  CB  . ALA B 45  ? 0.3282 0.2347 0.2229 -0.0690 0.0506  -0.0743 45  ALA B CB  
1085 N  N   . SER B 46  ? 0.2424 0.2640 0.2534 -0.0045 0.1662  -0.0636 46  SER B N   
1086 C  CA  . SER B 46  ? 0.2189 0.2374 0.1797 0.0312  0.1363  -0.0645 46  SER B CA  
1087 C  C   . SER B 46  ? 0.2905 0.1568 0.1981 -0.0249 0.0682  -0.0016 46  SER B C   
1088 O  O   . SER B 46  ? 0.3244 0.2111 0.2010 -0.0119 0.1025  -0.0367 46  SER B O   
1089 C  CB  . SER B 46  ? 0.1862 0.2509 0.2858 0.0046  0.0634  -0.0544 46  SER B CB  
1090 O  OG  . SER B 46  ? 0.2498 0.1786 0.3600 0.0030  0.1662  -0.0067 46  SER B OG  
1091 N  N   . GLY B 47  ? 0.2789 0.1903 0.1834 -0.0295 0.0913  -0.0469 47  GLY B N   
1092 C  CA  . GLY B 47  ? 0.2776 0.1815 0.1405 -0.0359 0.0751  0.0034  47  GLY B CA  
1093 C  C   . GLY B 47  ? 0.2340 0.1347 0.1841 -0.0151 0.0854  -0.0228 47  GLY B C   
1094 O  O   . GLY B 47  ? 0.2628 0.2028 0.2487 -0.0277 0.0609  -0.0131 47  GLY B O   
1095 N  N   . LYS B 48  ? 0.2483 0.1437 0.3392 -0.0088 0.0814  0.0157  48  LYS B N   
1096 C  CA  . LYS B 48  ? 0.2315 0.3123 0.3024 -0.0856 0.0523  -0.0251 48  LYS B CA  
1097 C  C   . LYS B 48  ? 0.2658 0.2167 0.1820 -0.0928 0.0759  0.1022  48  LYS B C   
1098 O  O   . LYS B 48  ? 0.3283 0.2439 0.1322 -0.0210 0.0818  0.0430  48  LYS B O   
1099 C  CB  . LYS B 48  ? 0.2836 0.2972 0.2485 -0.0646 0.0494  -0.0353 48  LYS B CB  
1100 C  CG  . LYS B 48  ? 0.2759 0.2679 0.3598 -0.0607 0.0486  -0.0225 48  LYS B CG  
1101 C  CD  . LYS B 48  ? 0.4518 0.3621 0.6218 -0.0361 0.0084  0.0568  48  LYS B CD  
1102 C  CE  . LYS B 48  ? 0.4689 0.4430 0.4341 -0.0024 0.0301  0.0394  48  LYS B CE  
1103 N  NZ  . LYS B 48  ? 0.8181 0.5063 0.4444 0.1574  0.2419  0.0107  48  LYS B NZ  
1104 N  N   . THR B 49  ? 0.2970 0.0263 0.0595 -0.0114 0.0238  -0.0051 49  THR B N   
1105 C  CA  . THR B 49  ? 0.2640 0.1181 0.1231 -0.0022 0.0641  -0.0339 49  THR B CA  
1106 C  C   . THR B 49  ? 0.2586 0.1688 0.1466 -0.0032 0.0432  -0.0572 49  THR B C   
1107 O  O   . THR B 49  ? 0.3381 0.1514 0.2159 -0.0505 0.0586  -0.0130 49  THR B O   
1108 C  CB  . THR B 49  ? 0.1776 0.2574 0.1033 -0.0409 0.0461  0.0128  49  THR B CB  
1109 O  OG1 . THR B 49  ? 0.2779 0.2325 0.1304 -0.0162 0.0705  0.0207  49  THR B OG1 
1110 C  CG2 . THR B 49  ? 0.2060 0.2117 0.2116 -0.0599 0.0257  -0.0192 49  THR B CG2 
1111 N  N   . SER B 50  ? 0.2801 0.2306 0.1354 -0.0400 0.0160  -0.0249 50  SER B N   
1112 C  CA  . SER B 50  ? 0.3316 0.2776 0.1321 -0.0048 -0.0340 -0.0274 50  SER B CA  
1113 C  C   . SER B 50  ? 0.3322 0.3718 0.2000 -0.0577 -0.0156 -0.0517 50  SER B C   
1114 O  O   . SER B 50  ? 0.3193 0.2817 0.1898 -0.0443 -0.0159 -0.0797 50  SER B O   
1115 C  CB  . SER B 50  ? 0.3512 0.3494 0.1796 0.0050  -0.0049 0.0407  50  SER B CB  
1116 O  OG  . SER B 50  ? 0.3073 0.4130 0.2219 0.0275  -0.0292 -0.0288 50  SER B OG  
1117 N  N   . GLU B 51  ? 0.2912 0.3701 0.2339 -0.0423 -0.0474 -0.0351 51  GLU B N   
1118 C  CA  . GLU B 51  ? 0.3222 0.3412 0.2230 -0.1140 -0.0490 -0.0233 51  GLU B CA  
1119 C  C   . GLU B 51  ? 0.3696 0.3206 0.3495 -0.0779 -0.0076 0.0366  51  GLU B C   
1120 O  O   . GLU B 51  ? 0.3429 0.4440 0.3073 -0.0752 -0.0532 0.0241  51  GLU B O   
1121 C  CB  . GLU B 51  ? 0.3089 0.4917 0.2386 -0.0699 -0.1232 -0.0341 51  GLU B CB  
1122 N  N   . SER B 52  ? 0.2698 0.3397 0.2386 -0.0693 -0.0630 0.0145  52  SER B N   
1123 C  CA  . SER B 52  ? 0.3420 0.3820 0.3331 0.0092  -0.0504 0.0205  52  SER B CA  
1124 C  C   . SER B 52  ? 0.3363 0.2837 0.2985 0.0019  -0.0106 0.0194  52  SER B C   
1125 O  O   . SER B 52  ? 0.3827 0.3280 0.2140 0.0354  0.0335  0.0589  52  SER B O   
1126 C  CB  . SER B 52  ? 0.4950 0.4904 0.2579 0.0291  -0.0697 0.0347  52  SER B CB  
1127 O  OG  . SER B 52  ? 0.6827 0.3170 0.3427 -0.0500 0.0653  0.0373  52  SER B OG  
1128 N  N   . GLY B 53  ? 0.2930 0.2415 0.1967 -0.0364 0.0008  -0.0098 53  GLY B N   
1129 C  CA  . GLY B 53  ? 0.2358 0.2393 0.1993 -0.0495 -0.0324 0.0329  53  GLY B CA  
1130 C  C   . GLY B 53  ? 0.2996 0.1999 0.1691 -0.0509 0.0212  -0.0091 53  GLY B C   
1131 O  O   . GLY B 53  ? 0.3711 0.2413 0.1447 -0.0519 0.0633  -0.0403 53  GLY B O   
1132 N  N   . GLU B 54  ? 0.2861 0.2452 0.1745 -0.0170 0.0503  -0.0215 54  GLU B N   
1133 C  CA  . GLU B 54  ? 0.2925 0.2915 0.1922 -0.0655 -0.0041 0.0235  54  GLU B CA  
1134 C  C   . GLU B 54  ? 0.3144 0.2375 0.2134 0.0168  -0.0494 0.0216  54  GLU B C   
1135 O  O   . GLU B 54  ? 0.3793 0.2627 0.1741 -0.0585 0.0555  0.0073  54  GLU B O   
1136 C  CB  . GLU B 54  ? 0.3512 0.3163 0.2122 -0.0316 -0.0060 0.0652  54  GLU B CB  
1137 C  CG  . GLU B 54  ? 0.3044 0.3543 0.3326 0.0743  -0.0356 0.1136  54  GLU B CG  
1138 C  CD  . GLU B 54  ? 0.3371 0.5609 0.3325 0.2852  0.2144  0.2686  54  GLU B CD  
1139 O  OE1 . GLU B 54  ? 0.3070 0.5818 0.2769 0.0798  0.0983  0.3684  54  GLU B OE1 
1140 O  OE2 . GLU B 54  ? 0.6235 0.8630 0.6728 0.6792  0.5050  0.4523  54  GLU B OE2 
1141 N  N   . LEU B 55  ? 0.3274 0.2234 0.1525 -0.0116 0.0522  -0.0505 55  LEU B N   
1142 C  CA  . LEU B 55  ? 0.2706 0.2343 0.2733 -0.0695 -0.0111 -0.0280 55  LEU B CA  
1143 C  C   . LEU B 55  ? 0.3312 0.2386 0.2514 -0.0314 0.0817  -0.0733 55  LEU B C   
1144 O  O   . LEU B 55  ? 0.3637 0.1785 0.1862 -0.0381 0.1179  -0.0312 55  LEU B O   
1145 C  CB  . LEU B 55  ? 0.2656 0.2965 0.1821 0.0069  0.0279  -0.0702 55  LEU B CB  
1146 C  CG  . LEU B 55  ? 0.2827 0.3347 0.2255 0.0299  0.0802  -0.0698 55  LEU B CG  
1147 C  CD1 . LEU B 55  ? 0.3583 0.2791 0.1993 0.0064  0.1769  -0.0239 55  LEU B CD1 
1148 C  CD2 . LEU B 55  ? 0.3859 0.3045 0.2457 -0.1079 0.0290  0.0348  55  LEU B CD2 
1149 N  N   . HIS B 56  ? 0.3467 0.3915 0.2221 -0.0341 0.0824  0.0237  56  HIS B N   
1150 C  CA  . HIS B 56  ? 0.3310 0.3842 0.2706 -0.0314 0.1050  0.0274  56  HIS B CA  
1151 C  C   . HIS B 56  ? 0.3534 0.3984 0.1700 -0.0158 0.1003  -0.0367 56  HIS B C   
1152 O  O   . HIS B 56  ? 0.4759 0.3383 0.3518 -0.0239 0.1863  -0.0348 56  HIS B O   
1153 C  CB  . HIS B 56  ? 0.4207 0.3673 0.3270 -0.0305 0.0249  0.0478  56  HIS B CB  
1154 C  CG  . HIS B 56  ? 0.3738 0.4136 0.3956 -0.0261 -0.0471 0.0754  56  HIS B CG  
1155 N  ND1 . HIS B 56  ? 0.4418 0.4560 0.4421 0.0049  0.0494  0.1167  56  HIS B ND1 
1156 C  CD2 . HIS B 56  ? 0.4394 0.4779 0.6537 -0.0856 -0.0559 0.0421  56  HIS B CD2 
1157 C  CE1 . HIS B 56  ? 0.4434 0.4781 0.4815 -0.0365 0.0531  -0.0913 56  HIS B CE1 
1158 N  NE2 . HIS B 56  ? 0.5615 0.5037 0.5414 -0.0390 -0.0093 0.0452  56  HIS B NE2 
1159 N  N   . GLY B 57  ? 0.4539 0.5511 0.2656 -0.1188 0.1048  0.0497  57  GLY B N   
1160 C  CA  . GLY B 57  ? 0.3875 0.4010 0.3083 -0.0708 0.0553  -0.0249 57  GLY B CA  
1161 C  C   . GLY B 57  ? 0.3773 0.4254 0.3409 0.0275  0.0913  -0.0313 57  GLY B C   
1162 O  O   . GLY B 57  ? 0.4713 0.3958 0.3510 0.0048  0.2011  -0.0299 57  GLY B O   
1163 N  N   . LEU B 58  ? 0.4514 0.2590 0.3115 -0.0336 0.1354  0.0391  58  LEU B N   
1164 C  CA  . LEU B 58  ? 0.3947 0.2571 0.2647 -0.0044 0.1826  -0.0544 58  LEU B CA  
1165 C  C   . LEU B 58  ? 0.3885 0.3503 0.3593 0.0038  0.1767  -0.0064 58  LEU B C   
1166 O  O   . LEU B 58  ? 0.3881 0.2146 0.3734 -0.0352 0.1343  -0.0449 58  LEU B O   
1167 C  CB  . LEU B 58  ? 0.3033 0.2800 0.2357 -0.0025 0.1381  -0.0572 58  LEU B CB  
1168 C  CG  . LEU B 58  ? 0.2073 0.3111 0.2959 -0.0203 0.1222  -0.0506 58  LEU B CG  
1169 C  CD1 . LEU B 58  ? 0.3447 0.2763 0.3112 -0.0607 0.1599  -0.0795 58  LEU B CD1 
1170 C  CD2 . LEU B 58  ? 0.3125 0.2664 0.3982 0.0058  0.1037  0.0256  58  LEU B CD2 
1171 N  N   . THR B 59  ? 0.4206 0.2804 0.3478 -0.0990 0.1902  -0.0377 59  THR B N   
1172 C  CA  . THR B 59  ? 0.3378 0.2391 0.3840 0.0022  0.1908  -0.0667 59  THR B CA  
1173 C  C   . THR B 59  ? 0.4374 0.4268 0.2856 -0.0351 0.2028  -0.0077 59  THR B C   
1174 O  O   . THR B 59  ? 0.5643 0.3365 0.4221 -0.0106 0.1549  -0.0509 59  THR B O   
1175 C  CB  . THR B 59  ? 0.3586 0.2891 0.3351 -0.0165 0.1355  -0.0800 59  THR B CB  
1176 O  OG1 . THR B 59  ? 0.3301 0.3626 0.3933 0.0142  0.1488  -0.0967 59  THR B OG1 
1177 C  CG2 . THR B 59  ? 0.3022 0.2802 0.4231 -0.0312 0.1229  -0.1228 59  THR B CG2 
1178 N  N   . THR B 60  ? 0.5636 0.3423 0.3333 -0.1135 0.0249  0.0487  60  THR B N   
1179 C  CA  . THR B 60  ? 0.5372 0.3185 0.2280 -0.0328 0.0876  -0.0131 60  THR B CA  
1180 C  C   . THR B 60  ? 0.3816 0.3324 0.3265 -0.1158 0.0355  -0.0072 60  THR B C   
1181 O  O   . THR B 60  ? 0.4059 0.3879 0.2835 -0.1538 0.1110  0.0399  60  THR B O   
1182 C  CB  . THR B 60  ? 0.4428 0.3282 0.3641 0.0016  0.1372  -0.0395 60  THR B CB  
1183 O  OG1 . THR B 60  ? 0.4540 0.4418 0.3782 -0.0824 0.1841  0.0376  60  THR B OG1 
1184 C  CG2 . THR B 60  ? 0.4933 0.2458 0.4410 -0.0050 0.0810  -0.0230 60  THR B CG2 
1185 N  N   . GLU B 61  ? 0.5076 0.3694 0.3480 -0.0678 0.1375  0.0382  61  GLU B N   
1186 C  CA  . GLU B 61  ? 0.4268 0.3769 0.3802 -0.0560 0.0768  0.0109  61  GLU B CA  
1187 C  C   . GLU B 61  ? 0.4666 0.4085 0.4563 -0.0350 0.0854  -0.0632 61  GLU B C   
1188 O  O   . GLU B 61  ? 0.4618 0.3735 0.4729 -0.0208 0.1584  -0.0830 61  GLU B O   
1189 C  CB  . GLU B 61  ? 0.6590 0.3244 0.2656 -0.0403 0.0102  0.0211  61  GLU B CB  
1190 N  N   . GLU B 62  ? 0.5111 0.3794 0.2510 -0.0961 0.1590  0.0614  62  GLU B N   
1191 C  CA  . GLU B 62  ? 0.5129 0.3491 0.4456 0.0250  0.1314  0.0110  62  GLU B CA  
1192 C  C   . GLU B 62  ? 0.4171 0.2685 0.4650 -0.0450 0.1369  0.0164  62  GLU B C   
1193 O  O   . GLU B 62  ? 0.3998 0.3328 0.5648 -0.1234 0.1568  0.0219  62  GLU B O   
1194 C  CB  . GLU B 62  ? 0.5047 0.4480 0.3422 -0.0745 0.0884  0.0110  62  GLU B CB  
1195 C  CG  . GLU B 62  ? 0.4312 0.4763 0.3450 -0.0343 0.1236  0.0728  62  GLU B CG  
1196 C  CD  . GLU B 62  ? 0.4700 0.3942 0.3926 -0.0210 0.0510  0.0614  62  GLU B CD  
1197 N  N   . GLU B 63  ? 0.4482 0.2281 0.4640 0.0059  0.2591  -0.0154 63  GLU B N   
1198 C  CA  . GLU B 63  ? 0.5552 0.2598 0.4162 -0.0397 0.1465  -0.0687 63  GLU B CA  
1199 C  C   . GLU B 63  ? 0.4458 0.2076 0.3345 -0.0610 0.0852  -0.0402 63  GLU B C   
1200 O  O   . GLU B 63  ? 0.2968 0.2770 0.4186 -0.0096 0.1003  -0.0254 63  GLU B O   
1201 C  CB  . GLU B 63  ? 0.4282 0.2536 0.5410 -0.0530 0.2198  -0.0628 63  GLU B CB  
1202 C  CG  . GLU B 63  ? 0.4112 0.4887 0.5336 0.0430  0.1041  -0.1386 63  GLU B CG  
1203 N  N   . PHE B 64  ? 0.4663 0.2183 0.4039 -0.0792 0.2023  0.0267  64  PHE B N   
1204 C  CA  . PHE B 64  ? 0.4246 0.2806 0.3904 -0.0503 0.1532  -0.0668 64  PHE B CA  
1205 C  C   . PHE B 64  ? 0.3130 0.2347 0.2421 -0.0417 0.1025  0.0673  64  PHE B C   
1206 O  O   . PHE B 64  ? 0.5571 0.2546 0.5210 0.0329  0.1133  0.0855  64  PHE B O   
1207 C  CB  . PHE B 64  ? 0.4141 0.1916 0.3743 -0.0701 0.1711  -0.0075 64  PHE B CB  
1208 C  CG  . PHE B 64  ? 0.3533 0.2234 0.3809 0.0169  0.1205  -0.0619 64  PHE B CG  
1209 C  CD1 . PHE B 64  ? 0.2646 0.4274 0.2842 0.0404  0.1576  -0.0520 64  PHE B CD1 
1210 C  CD2 . PHE B 64  ? 0.3197 0.5235 0.2475 0.1226  0.0598  0.0087  64  PHE B CD2 
1211 C  CE1 . PHE B 64  ? 0.3202 0.3537 0.2318 -0.0089 0.1383  -0.0228 64  PHE B CE1 
1212 C  CE2 . PHE B 64  ? 0.4263 0.6034 0.2194 0.0994  0.0718  -0.0795 64  PHE B CE2 
1213 C  CZ  . PHE B 64  ? 0.2945 0.5791 0.2616 0.0724  -0.0461 -0.0965 64  PHE B CZ  
1214 N  N   . VAL B 65  ? 0.2811 0.1757 0.3286 -0.0370 0.1611  -0.0398 65  VAL B N   
1215 C  CA  . VAL B 65  ? 0.3270 0.2288 0.3721 -0.0597 0.0805  -0.0589 65  VAL B CA  
1216 C  C   . VAL B 65  ? 0.4135 0.1862 0.3434 -0.0842 0.1272  -0.0046 65  VAL B C   
1217 O  O   . VAL B 65  ? 0.4021 0.1893 0.3953 -0.0461 0.2081  -0.0191 65  VAL B O   
1218 C  CB  . VAL B 65  ? 0.2871 0.2688 0.2615 -0.0516 0.1777  -0.0277 65  VAL B CB  
1219 C  CG1 . VAL B 65  ? 0.3185 0.2275 0.2815 -0.0756 0.2178  -0.0458 65  VAL B CG1 
1220 C  CG2 . VAL B 65  ? 0.4732 0.2223 0.2428 -0.0574 0.1786  0.0417  65  VAL B CG2 
1221 N  N   . GLU B 66  ? 0.4031 0.1715 0.3214 -0.0175 0.2278  0.0029  66  GLU B N   
1222 C  CA  . GLU B 66  ? 0.3797 0.1933 0.3305 -0.0073 0.2021  -0.0032 66  GLU B CA  
1223 C  C   . GLU B 66  ? 0.3080 0.1619 0.2962 -0.0536 0.2285  0.0274  66  GLU B C   
1224 O  O   . GLU B 66  ? 0.2593 0.3219 0.4728 -0.0403 0.2379  -0.0472 66  GLU B O   
1225 C  CB  . GLU B 66  ? 0.3997 0.1870 0.3863 -0.0338 0.1446  -0.0135 66  GLU B CB  
1226 C  CG  . GLU B 66  ? 0.3635 0.2146 0.3085 -0.0262 0.1496  0.0012  66  GLU B CG  
1227 C  CD  . GLU B 66  ? 0.3713 0.2099 0.5040 0.0888  0.1853  0.0142  66  GLU B CD  
1228 O  OE1 . GLU B 66  ? 0.4447 0.2951 0.3267 0.0104  0.1974  -0.0892 66  GLU B OE1 
1229 O  OE2 . GLU B 66  ? 0.4151 0.2801 0.4975 0.1310  0.2665  0.0487  66  GLU B OE2 
1230 N  N   . GLY B 67  ? 0.3372 0.3409 0.2696 -0.1138 0.2058  0.0565  67  GLY B N   
1231 C  CA  . GLY B 67  ? 0.4070 0.2977 0.2546 -0.0694 0.1386  0.0142  67  GLY B CA  
1232 C  C   . GLY B 67  ? 0.2935 0.1827 0.2888 -0.1188 0.0534  -0.0343 67  GLY B C   
1233 O  O   . GLY B 67  ? 0.3400 0.3458 0.2853 -0.0549 0.1374  0.0330  67  GLY B O   
1234 N  N   . ILE B 68  ? 0.3358 0.2030 0.3476 -0.0703 0.0810  -0.0071 68  ILE B N   
1235 C  CA  . ILE B 68  ? 0.3567 0.2011 0.3448 -0.0815 0.0751  -0.0269 68  ILE B CA  
1236 C  C   . ILE B 68  ? 0.3212 0.2538 0.2558 -0.0838 -0.0184 -0.0773 68  ILE B C   
1237 O  O   . ILE B 68  ? 0.3304 0.2088 0.3325 -0.0810 -0.0360 -0.0436 68  ILE B O   
1238 C  CB  . ILE B 68  ? 0.3631 0.2799 0.3638 -0.0635 0.0577  -0.0616 68  ILE B CB  
1239 C  CG1 . ILE B 68  ? 0.3923 0.3387 0.3151 -0.0674 -0.0958 -0.0935 68  ILE B CG1 
1240 C  CG2 . ILE B 68  ? 0.5942 0.3151 0.1908 -0.0660 0.0168  0.0305  68  ILE B CG2 
1241 C  CD1 . ILE B 68  ? 0.3857 0.4191 0.2711 -0.1196 -0.0367 -0.0242 68  ILE B CD1 
1242 N  N   . TYR B 69  ? 0.3386 0.2398 0.2533 -0.1356 0.0435  -0.0602 69  TYR B N   
1243 C  CA  . TYR B 69  ? 0.2826 0.1970 0.1937 -0.1010 0.0786  0.0033  69  TYR B CA  
1244 C  C   . TYR B 69  ? 0.2865 0.2815 0.1560 -0.1469 0.0913  -0.0302 69  TYR B C   
1245 O  O   . TYR B 69  ? 0.4049 0.2322 0.2098 -0.0999 0.1520  -0.0647 69  TYR B O   
1246 C  CB  . TYR B 69  ? 0.2365 0.2421 0.1857 -0.0915 0.0850  -0.0768 69  TYR B CB  
1247 C  CG  . TYR B 69  ? 0.2736 0.2698 0.2200 -0.0329 0.0994  -0.0171 69  TYR B CG  
1248 C  CD1 . TYR B 69  ? 0.3035 0.2493 0.2286 0.0231  0.1589  -0.0876 69  TYR B CD1 
1249 C  CD2 . TYR B 69  ? 0.2907 0.2302 0.1822 -0.0181 0.0635  -0.0135 69  TYR B CD2 
1250 C  CE1 . TYR B 69  ? 0.2452 0.2445 0.2788 -0.0303 0.1396  -0.0501 69  TYR B CE1 
1251 C  CE2 . TYR B 69  ? 0.4966 0.1742 0.1911 0.0293  0.2089  -0.0754 69  TYR B CE2 
1252 C  CZ  . TYR B 69  ? 0.2877 0.2022 0.1999 -0.0580 0.1148  -0.0303 69  TYR B CZ  
1253 O  OH  . TYR B 69  ? 0.3431 0.2403 0.2093 -0.0233 0.1392  0.0185  69  TYR B OH  
1254 N  N   . LYS B 70  ? 0.3683 0.2752 0.2299 -0.1282 0.0310  -0.0226 70  LYS B N   
1255 C  CA  . LYS B 70  ? 0.4198 0.2383 0.3312 -0.1558 0.0032  -0.0489 70  LYS B CA  
1256 C  C   . LYS B 70  ? 0.3787 0.1941 0.2945 -0.1434 0.0688  -0.0649 70  LYS B C   
1257 O  O   . LYS B 70  ? 0.3405 0.2770 0.2669 -0.1165 0.0759  -0.0402 70  LYS B O   
1258 C  CB  . LYS B 70  ? 0.4216 0.2812 0.3126 -0.1483 0.0022  -0.0225 70  LYS B CB  
1259 C  CG  . LYS B 70  ? 0.4428 0.3177 0.2842 -0.1797 -0.0632 -0.0132 70  LYS B CG  
1260 C  CD  . LYS B 70  ? 0.4403 0.2729 0.2733 -0.0193 -0.0208 -0.0151 70  LYS B CD  
1261 C  CE  . LYS B 70  ? 0.4717 0.3864 0.3465 -0.0559 0.0228  0.0774  70  LYS B CE  
1262 N  NZ  . LYS B 70  ? 0.7826 0.3699 0.3801 -0.1147 -0.1428 0.1219  70  LYS B NZ  
1263 N  N   . VAL B 71  ? 0.3679 0.2481 0.1717 -0.1228 0.0934  -0.0194 71  VAL B N   
1264 C  CA  . VAL B 71  ? 0.4253 0.1515 0.2900 -0.0933 0.1121  -0.0420 71  VAL B CA  
1265 C  C   . VAL B 71  ? 0.4482 0.2418 0.1058 -0.1295 0.0119  -0.0565 71  VAL B C   
1266 O  O   . VAL B 71  ? 0.4480 0.2854 0.1679 -0.1842 0.0870  -0.0068 71  VAL B O   
1267 C  CB  . VAL B 71  ? 0.3030 0.2430 0.1883 -0.0839 0.1659  -0.1123 71  VAL B CB  
1268 C  CG1 . VAL B 71  ? 0.4159 0.2158 0.2084 -0.1126 0.0443  -0.0418 71  VAL B CG1 
1269 C  CG2 . VAL B 71  ? 0.3425 0.1864 0.3175 -0.1113 0.1187  -0.0401 71  VAL B CG2 
1270 N  N   . GLU B 72  ? 0.5246 0.1986 0.1411 -0.1436 0.1060  -0.0473 72  GLU B N   
1271 C  CA  . GLU B 72  ? 0.4485 0.2074 0.1978 -0.1308 0.0941  -0.0270 72  GLU B CA  
1272 C  C   . GLU B 72  ? 0.3502 0.1867 0.2042 -0.0931 0.0693  -0.0254 72  GLU B C   
1273 O  O   . GLU B 72  ? 0.2981 0.2223 0.2606 -0.1013 0.0556  -0.0442 72  GLU B O   
1274 C  CB  . GLU B 72  ? 0.4471 0.4396 0.2808 -0.1632 0.0579  0.0013  72  GLU B CB  
1275 C  CG  . GLU B 72  ? 0.4558 0.4716 0.2732 -0.1196 0.0141  0.0085  72  GLU B CG  
1276 C  CD  . GLU B 72  ? 0.3201 0.5567 0.3403 -0.1769 0.2069  -0.0697 72  GLU B CD  
1277 O  OE1 . GLU B 72  ? 0.3908 0.8321 0.5647 -0.2967 -0.1535 0.2016  72  GLU B OE1 
1278 N  N   . ILE B 73  ? 0.2859 0.1856 0.2001 -0.0631 0.0493  -0.0592 73  ILE B N   
1279 C  CA  . ILE B 73  ? 0.2416 0.2010 0.1038 -0.0361 0.0367  -0.0162 73  ILE B CA  
1280 C  C   . ILE B 73  ? 0.2250 0.1640 0.2217 -0.0067 0.0423  -0.0315 73  ILE B C   
1281 O  O   . ILE B 73  ? 0.2699 0.1777 0.1988 -0.0682 0.0145  -0.0298 73  ILE B O   
1282 C  CB  . ILE B 73  ? 0.2681 0.1914 0.1920 0.0138  0.0396  -0.0023 73  ILE B CB  
1283 C  CG1 . ILE B 73  ? 0.3335 0.1825 0.2195 -0.0126 0.0661  -0.0155 73  ILE B CG1 
1284 C  CG2 . ILE B 73  ? 0.1895 0.2294 0.2825 0.0339  0.0257  -0.0048 73  ILE B CG2 
1285 C  CD1 . ILE B 73  ? 0.3347 0.2289 0.1774 0.0425  0.0730  0.0104  73  ILE B CD1 
1286 N  N   . ASP B 74  ? 0.2291 0.1715 0.1294 -0.0140 0.0910  -0.0274 74  ASP B N   
1287 C  CA  . ASP B 74  ? 0.1995 0.1881 0.1264 0.0042  0.0284  -0.0106 74  ASP B CA  
1288 C  C   . ASP B 74  ? 0.2086 0.1547 0.2145 -0.0020 0.0194  -0.0109 74  ASP B C   
1289 O  O   . ASP B 74  ? 0.2312 0.1781 0.1961 -0.0255 0.0783  -0.0336 74  ASP B O   
1290 C  CB  . ASP B 74  ? 0.2104 0.1869 0.2197 0.0017  0.0667  -0.0256 74  ASP B CB  
1291 C  CG  . ASP B 74  ? 0.2635 0.2535 0.2181 0.0751  0.0477  -0.0176 74  ASP B CG  
1292 O  OD1 . ASP B 74  ? 0.2413 0.1836 0.2306 -0.0040 0.0115  0.0012  74  ASP B OD1 
1293 O  OD2 . ASP B 74  ? 0.3006 0.2482 0.3933 0.0927  0.2001  0.0273  74  ASP B OD2 
1294 N  N   . THR B 75  ? 0.1420 0.1703 0.1989 -0.0085 -0.0087 -0.0169 75  THR B N   
1295 C  CA  . THR B 75  ? 0.1749 0.1494 0.0824 -0.0306 0.0203  -0.0173 75  THR B CA  
1296 C  C   . THR B 75  ? 0.1721 0.1368 0.2000 0.0180  0.0219  -0.0295 75  THR B C   
1297 O  O   . THR B 75  ? 0.1742 0.1546 0.1799 -0.0168 0.0159  -0.0048 75  THR B O   
1298 C  CB  . THR B 75  ? 0.1967 0.1678 0.1248 0.0111  0.0397  -0.0103 75  THR B CB  
1299 O  OG1 . THR B 75  ? 0.1904 0.1805 0.1727 -0.0181 0.0312  -0.0070 75  THR B OG1 
1300 C  CG2 . THR B 75  ? 0.2422 0.2177 0.1083 0.0134  0.0043  0.0368  75  THR B CG2 
1301 N  N   . LYS B 76  ? 0.1500 0.1361 0.1455 -0.0180 0.0093  -0.0092 76  LYS B N   
1302 C  CA  . LYS B 76  ? 0.1730 0.1384 0.1499 -0.0424 0.0148  0.0156  76  LYS B CA  
1303 C  C   . LYS B 76  ? 0.1348 0.1326 0.1591 -0.0126 0.0373  0.0053  76  LYS B C   
1304 O  O   . LYS B 76  ? 0.1933 0.1497 0.1460 -0.0391 0.0304  0.0220  76  LYS B O   
1305 C  CB  . LYS B 76  ? 0.2015 0.1931 0.2369 -0.0229 -0.0099 -0.0068 76  LYS B CB  
1306 C  CG  . LYS B 76  ? 0.2433 0.2787 0.2582 0.0379  0.0002  0.0131  76  LYS B CG  
1307 C  CD  . LYS B 76  ? 0.3219 0.2101 0.3913 0.0413  -0.1448 0.0140  76  LYS B CD  
1308 C  CE  . LYS B 76  ? 0.4793 0.4417 0.4549 -0.0748 -0.1327 0.0571  76  LYS B CE  
1309 N  NZ  . LYS B 76  ? 0.5050 0.4992 0.2794 0.0518  -0.0828 0.0432  76  LYS B NZ  
1310 N  N   . SER B 77  ? 0.1576 0.1541 0.1915 -0.0200 0.0397  0.0117  77  SER B N   
1311 C  CA  . SER B 77  ? 0.1928 0.1566 0.1945 0.0120  0.0283  -0.0196 77  SER B CA  
1312 C  C   . SER B 77  ? 0.1645 0.1695 0.2029 0.0037  0.0448  -0.0437 77  SER B C   
1313 O  O   . SER B 77  ? 0.2410 0.1728 0.1488 -0.0049 0.0095  -0.0254 77  SER B O   
1314 C  CB  . SER B 77  ? 0.2172 0.2246 0.2037 0.0195  0.0125  0.0283  77  SER B CB  
1315 O  OG  . SER B 77  ? 0.2058 0.2965 0.3411 0.0566  0.0243  -0.0395 77  SER B OG  
1316 N  N   . TYR B 78  ? 0.1809 0.1910 0.1867 -0.0090 0.0377  -0.0178 78  TYR B N   
1317 C  CA  . TYR B 78  ? 0.2302 0.1664 0.1898 -0.0095 -0.0244 0.0398  78  TYR B CA  
1318 C  C   . TYR B 78  ? 0.1856 0.1685 0.1916 0.0089  0.0346  -0.0561 78  TYR B C   
1319 O  O   . TYR B 78  ? 0.2070 0.1835 0.2007 -0.0008 0.0038  -0.0562 78  TYR B O   
1320 C  CB  . TYR B 78  ? 0.2332 0.1866 0.1833 0.0263  0.0207  0.0351  78  TYR B CB  
1321 C  CG  . TYR B 78  ? 0.2042 0.1211 0.1436 0.0134  0.0231  -0.0066 78  TYR B CG  
1322 C  CD1 . TYR B 78  ? 0.2234 0.1947 0.1845 0.0048  -0.0586 -0.0319 78  TYR B CD1 
1323 C  CD2 . TYR B 78  ? 0.2254 0.1124 0.1305 0.0275  0.0343  -0.0158 78  TYR B CD2 
1324 C  CE1 . TYR B 78  ? 0.2191 0.2323 0.1861 0.0368  -0.0741 -0.0707 78  TYR B CE1 
1325 C  CE2 . TYR B 78  ? 0.2422 0.1220 0.2240 0.0068  0.0033  0.0123  78  TYR B CE2 
1326 C  CZ  . TYR B 78  ? 0.2167 0.2091 0.2297 0.0710  -0.0452 -0.0138 78  TYR B CZ  
1327 O  OH  . TYR B 78  ? 0.2133 0.2058 0.2761 0.0308  -0.0239 -0.0556 78  TYR B OH  
1328 N  N   . TRP B 79  ? 0.1907 0.1345 0.1449 0.0074  -0.0008 0.0249  79  TRP B N   
1329 C  CA  . TRP B 79  ? 0.1711 0.1287 0.1590 -0.0043 0.0132  -0.0190 79  TRP B CA  
1330 C  C   . TRP B 79  ? 0.1679 0.1274 0.1810 -0.0049 -0.0029 0.0070  79  TRP B C   
1331 O  O   . TRP B 79  ? 0.2012 0.1354 0.2307 -0.0269 0.0354  -0.0308 79  TRP B O   
1332 C  CB  . TRP B 79  ? 0.1394 0.1440 0.1636 0.0010  -0.0153 -0.0188 79  TRP B CB  
1333 C  CG  . TRP B 79  ? 0.1405 0.1466 0.1387 -0.0159 -0.0440 -0.0091 79  TRP B CG  
1334 C  CD1 . TRP B 79  ? 0.1487 0.1284 0.1909 -0.0174 -0.0358 0.0238  79  TRP B CD1 
1335 C  CD2 . TRP B 79  ? 0.1236 0.1126 0.1929 0.0037  0.0010  0.0068  79  TRP B CD2 
1336 N  NE1 . TRP B 79  ? 0.1449 0.1201 0.1801 -0.0120 0.0035  -0.0061 79  TRP B NE1 
1337 C  CE2 . TRP B 79  ? 0.1352 0.1381 0.1900 -0.0117 0.0178  -0.0413 79  TRP B CE2 
1338 C  CE3 . TRP B 79  ? 0.1377 0.1484 0.2326 0.0039  -0.0370 -0.0411 79  TRP B CE3 
1339 C  CZ2 . TRP B 79  ? 0.1246 0.1184 0.1858 -0.0180 0.0220  -0.0619 79  TRP B CZ2 
1340 C  CZ3 . TRP B 79  ? 0.1335 0.1342 0.3112 -0.0068 -0.0232 -0.0734 79  TRP B CZ3 
1341 C  CH2 . TRP B 79  ? 0.1246 0.1276 0.2536 -0.0069 -0.0152 -0.0638 79  TRP B CH2 
1342 N  N   . LYS B 80  ? 0.2024 0.1322 0.1715 -0.0209 -0.0425 -0.0264 80  LYS B N   
1343 C  CA  . LYS B 80  ? 0.2419 0.1315 0.2453 -0.0232 -0.0059 -0.0043 80  LYS B CA  
1344 C  C   . LYS B 80  ? 0.1816 0.1112 0.2639 -0.0179 0.0160  -0.0216 80  LYS B C   
1345 O  O   . LYS B 80  ? 0.2438 0.1109 0.3260 -0.0276 0.0409  0.0084  80  LYS B O   
1346 C  CB  . LYS B 80  ? 0.2473 0.1469 0.2938 -0.0401 -0.0003 -0.0161 80  LYS B CB  
1347 C  CG  . LYS B 80  ? 0.3747 0.2283 0.3218 -0.1193 -0.0964 0.0073  80  LYS B CG  
1348 C  CD  . LYS B 80  ? 0.2986 0.2948 0.5214 -0.0501 0.0136  -0.0054 80  LYS B CD  
1349 C  CE  . LYS B 80  ? 0.3674 0.4298 0.4447 -0.0734 0.0132  0.0792  80  LYS B CE  
1350 N  N   . ALA B 81  ? 0.2146 0.1511 0.2458 0.0133  0.0045  -0.0371 81  ALA B N   
1351 C  CA  . ALA B 81  ? 0.3096 0.1081 0.2710 -0.0619 0.0110  -0.0414 81  ALA B CA  
1352 C  C   . ALA B 81  ? 0.2756 0.2179 0.2227 -0.0428 -0.0475 -0.1262 81  ALA B C   
1353 O  O   . ALA B 81  ? 0.3192 0.1616 0.2258 -0.0364 -0.0823 -0.0883 81  ALA B O   
1354 C  CB  . ALA B 81  ? 0.4002 0.1390 0.2629 -0.0908 -0.0166 0.0048  81  ALA B CB  
1355 N  N   . LEU B 82  ? 0.2675 0.2553 0.2150 0.0343  -0.0238 -0.0658 82  LEU B N   
1356 C  CA  . LEU B 82  ? 0.3093 0.1512 0.3257 0.0069  -0.0545 -0.0461 82  LEU B CA  
1357 C  C   . LEU B 82  ? 0.2034 0.2600 0.3279 -0.0261 -0.0276 -0.0389 82  LEU B C   
1358 O  O   . LEU B 82  ? 0.1596 0.2726 0.4556 -0.0208 -0.0302 -0.1714 82  LEU B O   
1359 C  CB  . LEU B 82  ? 0.2704 0.1723 0.3600 0.0183  -0.0297 -0.0744 82  LEU B CB  
1360 C  CG  . LEU B 82  ? 0.3135 0.2735 0.3077 0.0407  -0.0404 -0.0238 82  LEU B CG  
1361 C  CD1 . LEU B 82  ? 0.3641 0.4986 0.3447 0.0114  -0.0116 -0.0279 82  LEU B CD1 
1362 C  CD2 . LEU B 82  ? 0.3927 0.2160 0.2864 0.0061  -0.0990 -0.0633 82  LEU B CD2 
1363 N  N   . GLY B 83  ? 0.2172 0.1351 0.2706 0.0094  -0.0052 -0.0435 83  GLY B N   
1364 C  CA  . GLY B 83  ? 0.3002 0.2071 0.2850 -0.0877 0.0176  -0.0307 83  GLY B CA  
1365 C  C   . GLY B 83  ? 0.2579 0.2091 0.2133 -0.0433 -0.0513 0.0082  83  GLY B C   
1366 O  O   . GLY B 83  ? 0.2655 0.1694 0.2478 -0.0626 -0.0012 -0.0447 83  GLY B O   
1367 N  N   . ILE B 84  ? 0.1970 0.2042 0.1974 -0.0033 -0.0001 -0.0116 84  ILE B N   
1368 C  CA  . ILE B 84  ? 0.1788 0.1679 0.2352 -0.0604 0.0046  -0.0481 84  ILE B CA  
1369 C  C   . ILE B 84  ? 0.1932 0.1111 0.2303 -0.0166 -0.0282 -0.0101 84  ILE B C   
1370 O  O   . ILE B 84  ? 0.2009 0.1956 0.2294 -0.0367 -0.0108 0.0096  84  ILE B O   
1371 C  CB  . ILE B 84  ? 0.2160 0.1668 0.2518 -0.0155 -0.0244 -0.0543 84  ILE B CB  
1372 C  CG1 . ILE B 84  ? 0.1979 0.2381 0.2204 0.0312  -0.0122 -0.0398 84  ILE B CG1 
1373 C  CG2 . ILE B 84  ? 0.2064 0.1433 0.2624 -0.0110 -0.0725 -0.0527 84  ILE B CG2 
1374 C  CD1 . ILE B 84  ? 0.1921 0.1881 0.4146 0.0390  -0.1105 -0.0205 84  ILE B CD1 
1375 N  N   . SER B 85  ? 0.1650 0.1735 0.2419 -0.0124 -0.0278 -0.0394 85  SER B N   
1376 C  CA  . SER B 85  ? 0.1675 0.1924 0.2769 -0.0090 -0.0278 -0.0816 85  SER B CA  
1377 C  C   . SER B 85  ? 0.1781 0.1778 0.2307 -0.0613 -0.0476 -0.0183 85  SER B C   
1378 O  O   . SER B 85  ? 0.2354 0.2190 0.1980 -0.0338 -0.0359 0.0230  85  SER B O   
1379 C  CB  . SER B 85  ? 0.2527 0.2797 0.2929 -0.0007 0.0202  -0.0358 85  SER B CB  
1380 O  OG  . SER B 85  ? 0.4016 0.1902 0.3493 0.0083  0.0017  0.0098  85  SER B OG  
1381 N  N   . PRO B 86  ? 0.1447 0.1630 0.2082 0.0204  -0.0388 -0.0115 86  PRO B N   
1382 C  CA  . PRO B 86  ? 0.1852 0.1588 0.2188 -0.0334 -0.0665 0.0268  86  PRO B CA  
1383 C  C   . PRO B 86  ? 0.1890 0.1482 0.2524 -0.0200 -0.0547 -0.0051 86  PRO B C   
1384 O  O   . PRO B 86  ? 0.1948 0.1615 0.2466 0.0312  -0.0731 -0.0558 86  PRO B O   
1385 C  CB  . PRO B 86  ? 0.2676 0.1986 0.2417 -0.0625 -0.0638 0.0410  86  PRO B CB  
1386 C  CG  . PRO B 86  ? 0.2310 0.2838 0.3004 -0.0800 -0.0004 -0.0147 86  PRO B CG  
1387 C  CD  . PRO B 86  ? 0.1762 0.2216 0.2129 -0.0039 -0.0114 -0.0231 86  PRO B CD  
1388 N  N   . PHE B 87  ? 0.1458 0.1459 0.1236 -0.0235 -0.0097 0.0274  87  PHE B N   
1389 C  CA  . PHE B 87  ? 0.1122 0.1267 0.1542 -0.0175 -0.0093 0.0013  87  PHE B CA  
1390 C  C   . PHE B 87  ? 0.0995 0.1326 0.1602 0.0090  0.0055  0.0172  87  PHE B C   
1391 O  O   . PHE B 87  ? 0.0895 0.1688 0.1585 0.0002  0.0140  0.0134  87  PHE B O   
1392 C  CB  . PHE B 87  ? 0.1482 0.1403 0.1644 -0.0001 0.0139  0.0108  87  PHE B CB  
1393 C  CG  . PHE B 87  ? 0.1014 0.1635 0.1431 0.0168  0.0029  0.0119  87  PHE B CG  
1394 C  CD1 . PHE B 87  ? 0.2281 0.1576 0.1111 0.0460  -0.0017 -0.0184 87  PHE B CD1 
1395 C  CD2 . PHE B 87  ? 0.0861 0.1575 0.1281 0.0151  -0.0290 -0.0273 87  PHE B CD2 
1396 C  CE1 . PHE B 87  ? 0.1961 0.2005 0.1663 0.0221  -0.0207 0.0068  87  PHE B CE1 
1397 C  CE2 . PHE B 87  ? 0.1175 0.2267 0.1286 0.0207  -0.0360 -0.0528 87  PHE B CE2 
1398 C  CZ  . PHE B 87  ? 0.1409 0.2304 0.1681 0.0225  0.0061  -0.0199 87  PHE B CZ  
1399 N  N   . HIS B 88  ? 0.1246 0.1915 0.1274 -0.0049 -0.0410 0.0148  88  HIS B N   
1400 C  CA  . HIS B 88  ? 0.1319 0.1543 0.1514 -0.0057 -0.0150 -0.0011 88  HIS B CA  
1401 C  C   . HIS B 88  ? 0.1295 0.1447 0.0997 -0.0564 0.0183  0.0004  88  HIS B C   
1402 O  O   . HIS B 88  ? 0.1421 0.1959 0.2050 -0.0438 0.0023  -0.0707 88  HIS B O   
1403 C  CB  . HIS B 88  ? 0.1212 0.1739 0.1587 -0.0447 -0.0329 0.0404  88  HIS B CB  
1404 C  CG  . HIS B 88  ? 0.0881 0.2159 0.1818 -0.0216 -0.0460 0.0483  88  HIS B CG  
1405 N  ND1 . HIS B 88  ? 0.0874 0.1696 0.2014 -0.0282 -0.0450 0.0256  88  HIS B ND1 
1406 C  CD2 . HIS B 88  ? 0.1297 0.1641 0.2766 0.0399  0.0008  -0.0128 88  HIS B CD2 
1407 C  CE1 . HIS B 88  ? 0.1679 0.1155 0.2939 0.0224  -0.0478 0.0377  88  HIS B CE1 
1408 N  NE2 . HIS B 88  ? 0.1030 0.1536 0.3564 0.0354  -0.0020 0.0007  88  HIS B NE2 
1409 N  N   . GLU B 89  ? 0.1316 0.2307 0.1354 -0.0698 0.0320  -0.0447 89  GLU B N   
1410 C  CA  . GLU B 89  ? 0.1330 0.2938 0.2196 -0.0516 0.0343  -0.0809 89  GLU B CA  
1411 C  C   . GLU B 89  ? 0.1803 0.2860 0.2103 -0.1010 0.0556  -0.0667 89  GLU B C   
1412 O  O   . GLU B 89  ? 0.2710 0.3578 0.1891 -0.1314 0.0537  -0.0871 89  GLU B O   
1413 C  CB  . GLU B 89  ? 0.1534 0.2749 0.1826 -0.0334 0.0061  -0.0901 89  GLU B CB  
1414 C  CG  . GLU B 89  ? 0.1370 0.3500 0.2357 -0.0651 -0.0062 -0.0471 89  GLU B CG  
1415 C  CD  . GLU B 89  ? 0.2854 0.3328 0.2624 0.0500  0.0520  -0.0358 89  GLU B CD  
1416 O  OE1 . GLU B 89  ? 0.2690 0.3810 0.2722 0.0517  0.0530  -0.0338 89  GLU B OE1 
1417 O  OE2 . GLU B 89  ? 0.2961 0.3824 0.3233 0.0221  -0.0603 -0.0005 89  GLU B OE2 
1418 N  N   . HIS B 90  ? 0.2762 0.3149 0.2161 -0.1323 0.0285  -0.0664 90  HIS B N   
1419 C  CA  . HIS B 90  ? 0.3110 0.2783 0.1906 -0.1696 0.0557  -0.0430 90  HIS B CA  
1420 C  C   . HIS B 90  ? 0.6730 0.1537 0.1406 -0.1548 0.0541  -0.0561 90  HIS B C   
1421 O  O   . HIS B 90  ? 0.6582 0.1873 0.1734 -0.1290 0.1295  -0.0708 90  HIS B O   
1422 C  CB  . HIS B 90  ? 0.3734 0.4117 0.2704 -0.2389 0.0910  -0.0092 90  HIS B CB  
1423 C  CG  . HIS B 90  ? 0.4339 0.5448 0.3275 -0.1174 0.0882  0.2096  90  HIS B CG  
1424 N  ND1 . HIS B 90  ? 0.5422 0.7021 0.3021 -0.0370 0.0933  0.0625  90  HIS B ND1 
1425 C  CD2 . HIS B 90  ? 0.4892 0.5640 0.5003 -0.0861 0.1155  -0.0216 90  HIS B CD2 
1426 C  CE1 . HIS B 90  ? 0.5769 0.6677 0.4841 -0.1012 0.0048  -0.2294 90  HIS B CE1 
1427 N  NE2 . HIS B 90  ? 0.5335 0.5287 0.7538 -0.0753 0.0192  -0.0480 90  HIS B NE2 
1428 N  N   . ALA B 91  ? 0.6202 0.2920 0.1738 -0.1076 0.1569  0.0112  91  ALA B N   
1429 C  CA  . ALA B 91  ? 0.7204 0.2596 0.1223 -0.1145 0.1672  0.0379  91  ALA B CA  
1430 C  C   . ALA B 91  ? 0.7121 0.2872 0.1010 -0.1237 0.1308  -0.0153 91  ALA B C   
1431 O  O   . ALA B 91  ? 0.8115 0.2121 0.1365 -0.0393 0.1954  0.0078  91  ALA B O   
1432 C  CB  . ALA B 91  ? 0.8319 0.1456 0.1592 0.1667  0.1815  -0.0451 91  ALA B CB  
1433 N  N   . GLU B 92  ? 0.9109 0.3934 0.3332 -0.3370 0.1368  0.0239  92  GLU B N   
1434 C  CA  . GLU B 92  ? 0.6623 0.3527 0.2364 -0.2009 0.0946  -0.1362 92  GLU B CA  
1435 C  C   . GLU B 92  ? 0.5853 0.3635 0.2626 0.0980  0.1695  0.0404  92  GLU B C   
1436 O  O   . GLU B 92  ? 0.6601 0.4083 0.2562 0.0803  0.0291  -0.0515 92  GLU B O   
1437 N  N   . VAL B 93  ? 0.3193 0.3257 0.2773 -0.1070 0.1072  -0.0984 93  VAL B N   
1438 C  CA  . VAL B 93  ? 0.3955 0.2871 0.2826 -0.1071 0.0642  0.0709  93  VAL B CA  
1439 C  C   . VAL B 93  ? 0.4773 0.2326 0.2166 -0.1676 0.1036  -0.0558 93  VAL B C   
1440 O  O   . VAL B 93  ? 0.4253 0.2230 0.2166 -0.1384 0.0877  -0.0453 93  VAL B O   
1441 C  CB  . VAL B 93  ? 0.2749 0.2783 0.3219 0.0912  0.0875  -0.1500 93  VAL B CB  
1442 C  CG1 . VAL B 93  ? 0.3634 0.1106 0.6070 -0.0550 0.1710  -0.1459 93  VAL B CG1 
1443 C  CG2 . VAL B 93  ? 0.3410 0.0468 0.8909 -0.0783 -0.0684 0.0590  93  VAL B CG2 
1444 N  N   . VAL B 94  ? 0.3289 0.2895 0.2061 -0.1851 0.0443  -0.0580 94  VAL B N   
1445 C  CA  . VAL B 94  ? 0.3369 0.2769 0.2443 -0.1593 0.0558  0.0219  94  VAL B CA  
1446 C  C   . VAL B 94  ? 0.3925 0.2908 0.1936 -0.1006 0.1274  -0.0555 94  VAL B C   
1447 O  O   . VAL B 94  ? 0.3390 0.3124 0.2378 -0.0964 0.1339  -0.0782 94  VAL B O   
1448 C  CB  . VAL B 94  ? 0.3701 0.3895 0.2376 -0.1189 0.0241  -0.0293 94  VAL B CB  
1449 C  CG1 . VAL B 94  ? 0.4280 0.3168 0.1666 -0.1390 0.0259  -0.0655 94  VAL B CG1 
1450 C  CG2 . VAL B 94  ? 0.5249 0.3863 0.1871 -0.2033 -0.0486 -0.0232 94  VAL B CG2 
1451 N  N   . PHE B 95  ? 0.2715 0.2459 0.2433 -0.0912 0.1018  -0.0287 95  PHE B N   
1452 C  CA  . PHE B 95  ? 0.4001 0.2548 0.2562 -0.0706 0.0956  -0.0389 95  PHE B CA  
1453 C  C   . PHE B 95  ? 0.3040 0.1678 0.1945 -0.0077 0.0354  -0.0344 95  PHE B C   
1454 O  O   . PHE B 95  ? 0.3014 0.1824 0.2834 -0.0620 0.1024  -0.0291 95  PHE B O   
1455 C  CB  . PHE B 95  ? 0.3017 0.2965 0.2029 -0.0939 0.1374  -0.0605 95  PHE B CB  
1456 C  CG  . PHE B 95  ? 0.3164 0.3280 0.1728 -0.0777 0.0750  -0.0669 95  PHE B CG  
1457 C  CD1 . PHE B 95  ? 0.3791 0.3526 0.2801 -0.0614 0.1244  -0.0495 95  PHE B CD1 
1458 C  CD2 . PHE B 95  ? 0.3141 0.3065 0.2596 -0.0756 0.2035  -0.0526 95  PHE B CD2 
1459 C  CE1 . PHE B 95  ? 0.3481 0.3007 0.3491 0.0061  0.1568  -0.0732 95  PHE B CE1 
1460 C  CE2 . PHE B 95  ? 0.3357 0.3150 0.2717 -0.0357 0.1023  -0.0672 95  PHE B CE2 
1461 C  CZ  . PHE B 95  ? 0.3421 0.3282 0.1624 -0.0262 -0.0095 -0.1299 95  PHE B CZ  
1462 N  N   . THR B 96  ? 0.4042 0.1511 0.2605 -0.0766 0.0729  0.0020  96  THR B N   
1463 C  CA  . THR B 96  ? 0.2555 0.1839 0.3466 -0.0955 0.0094  0.0513  96  THR B CA  
1464 C  C   . THR B 96  ? 0.3387 0.3558 0.3521 -0.0432 -0.0231 0.0133  96  THR B C   
1465 O  O   . THR B 96  ? 0.3699 0.4176 0.3909 -0.1261 0.0722  0.0672  96  THR B O   
1466 C  CB  . THR B 96  ? 0.5406 0.2353 0.4000 -0.1420 0.0922  0.0144  96  THR B CB  
1467 O  OG1 . THR B 96  ? 0.6330 0.2229 0.5454 -0.0210 -0.1027 -0.0563 96  THR B OG1 
1468 C  CG2 . THR B 96  ? 0.4600 0.3000 0.6506 -0.2196 0.0059  0.1325  96  THR B CG2 
1469 N  N   . ALA B 97  ? 0.3350 0.3278 0.3496 -0.0451 0.0026  0.0736  97  ALA B N   
1470 C  CA  . ALA B 97  ? 0.2854 0.2696 0.3256 -0.0209 -0.0171 -0.0531 97  ALA B CA  
1471 C  C   . ALA B 97  ? 0.3965 0.3909 0.4480 -0.0899 0.0645  0.0976  97  ALA B C   
1472 O  O   . ALA B 97  ? 0.3867 0.2259 0.4473 0.0142  0.0877  0.0352  97  ALA B O   
1473 C  CB  . ALA B 97  ? 0.4532 0.3146 0.2950 -0.0260 0.1171  -0.0195 97  ALA B CB  
1474 N  N   . ASN B 98  ? 0.4198 0.4909 0.5004 -0.0130 0.1235  0.0351  98  ASN B N   
1475 C  CA  . ASN B 98  ? 0.4736 0.3722 0.5508 -0.0350 0.0298  -0.0119 98  ASN B CA  
1476 C  C   . ASN B 98  ? 0.7589 0.4258 0.5087 -0.0896 0.0801  -0.0387 98  ASN B C   
1477 O  O   . ASN B 98  ? 0.5660 0.3390 0.6162 0.0181  0.0069  -0.1343 98  ASN B O   
1478 N  N   . ARG B 104 ? 0.6390 0.2710 0.3270 0.0681  0.0504  -0.0785 104 ARG B N   
1479 C  CA  . ARG B 104 ? 0.4756 0.2447 0.2971 0.0648  0.1275  -0.0721 104 ARG B CA  
1480 C  C   . ARG B 104 ? 0.3637 0.4125 0.3690 0.0380  0.1214  0.0187  104 ARG B C   
1481 O  O   . ARG B 104 ? 0.4326 0.3498 0.2338 0.1029  0.0726  0.0682  104 ARG B O   
1482 C  CB  . ARG B 104 ? 0.5925 0.5098 0.1952 0.0450  0.1059  -0.0547 104 ARG B CB  
1483 N  N   . TYR B 105 ? 0.3429 0.2932 0.1873 -0.0248 0.1533  0.0316  105 TYR B N   
1484 C  CA  . TYR B 105 ? 0.3314 0.2361 0.2150 0.0056  0.1721  0.0342  105 TYR B CA  
1485 C  C   . TYR B 105 ? 0.3398 0.3221 0.3330 -0.0406 0.1006  0.0650  105 TYR B C   
1486 O  O   . TYR B 105 ? 0.4442 0.3079 0.2831 -0.0454 0.1682  0.0492  105 TYR B O   
1487 C  CB  . TYR B 105 ? 0.3568 0.2630 0.2890 -0.0032 0.1127  0.0455  105 TYR B CB  
1488 C  CG  . TYR B 105 ? 0.4272 0.2237 0.3627 0.0442  0.0413  0.0117  105 TYR B CG  
1489 C  CD1 . TYR B 105 ? 0.3878 0.3199 0.4748 -0.0852 0.1448  -0.1340 105 TYR B CD1 
1490 C  CD2 . TYR B 105 ? 0.5085 0.2567 0.3395 -0.1249 0.0347  0.0077  105 TYR B CD2 
1491 C  CE1 . TYR B 105 ? 0.6298 0.2978 0.4822 -0.0287 -0.0364 -0.1591 105 TYR B CE1 
1492 C  CE2 . TYR B 105 ? 0.5401 0.4085 0.3487 -0.1259 -0.0480 -0.1426 105 TYR B CE2 
1493 C  CZ  . TYR B 105 ? 0.4023 0.3097 0.5065 0.0409  0.0926  -0.2185 105 TYR B CZ  
1494 O  OH  . TYR B 105 ? 0.6620 0.3331 0.4030 0.0106  -0.1401 -0.1258 105 TYR B OH  
1495 N  N   . THR B 106 ? 0.3301 0.2270 0.2184 0.0579  0.0819  0.0513  106 THR B N   
1496 C  CA  . THR B 106 ? 0.3455 0.2491 0.1640 0.0116  0.1224  0.0501  106 THR B CA  
1497 C  C   . THR B 106 ? 0.2782 0.1955 0.1582 -0.0027 0.1388  0.0504  106 THR B C   
1498 O  O   . THR B 106 ? 0.3256 0.1728 0.2334 -0.0167 0.1287  -0.0108 106 THR B O   
1499 C  CB  . THR B 106 ? 0.2860 0.2687 0.3628 -0.0037 0.0900  0.0405  106 THR B CB  
1500 O  OG1 . THR B 106 ? 0.3763 0.3591 0.3765 -0.0565 0.0677  0.0431  106 THR B OG1 
1501 C  CG2 . THR B 106 ? 0.3848 0.1707 0.3570 0.0300  0.0796  -0.0316 106 THR B CG2 
1502 N  N   . ILE B 107 ? 0.3196 0.1672 0.2106 -0.0006 0.1128  0.0150  107 ILE B N   
1503 C  CA  . ILE B 107 ? 0.2956 0.1795 0.1959 -0.0344 0.1389  -0.0152 107 ILE B CA  
1504 C  C   . ILE B 107 ? 0.2662 0.1913 0.2141 -0.0214 0.1209  -0.0184 107 ILE B C   
1505 O  O   . ILE B 107 ? 0.3921 0.2047 0.2844 -0.0598 0.2506  -0.0610 107 ILE B O   
1506 C  CB  . ILE B 107 ? 0.2707 0.2319 0.2479 -0.0242 0.0906  -0.0395 107 ILE B CB  
1507 C  CG1 . ILE B 107 ? 0.2974 0.2180 0.2792 0.0123  0.0917  0.0047  107 ILE B CG1 
1508 C  CG2 . ILE B 107 ? 0.3779 0.2120 0.2635 0.0231  0.0627  -0.0081 107 ILE B CG2 
1509 C  CD1 . ILE B 107 ? 0.3308 0.1764 0.3768 0.0399  0.1084  -0.0136 107 ILE B CD1 
1510 N  N   . ALA B 108 ? 0.2022 0.2298 0.1883 -0.0159 0.0779  -0.0134 108 ALA B N   
1511 C  CA  . ALA B 108 ? 0.2805 0.1894 0.1721 -0.0246 0.0721  -0.0583 108 ALA B CA  
1512 C  C   . ALA B 108 ? 0.3244 0.1696 0.2373 -0.0327 0.0662  -0.0073 108 ALA B C   
1513 O  O   . ALA B 108 ? 0.3976 0.1497 0.2094 -0.0623 0.1430  -0.0128 108 ALA B O   
1514 C  CB  . ALA B 108 ? 0.3158 0.3385 0.2369 -0.0412 0.0333  0.0424  108 ALA B CB  
1515 N  N   . ALA B 109 ? 0.2877 0.1626 0.1467 -0.0416 0.0929  -0.0199 109 ALA B N   
1516 C  CA  . ALA B 109 ? 0.1937 0.1765 0.1321 -0.0560 0.0428  -0.0214 109 ALA B CA  
1517 C  C   . ALA B 109 ? 0.1488 0.2116 0.2228 -0.0293 0.0567  -0.0059 109 ALA B C   
1518 O  O   . ALA B 109 ? 0.2404 0.2376 0.2027 -0.0563 0.0519  -0.0248 109 ALA B O   
1519 C  CB  . ALA B 109 ? 0.1953 0.2156 0.2613 -0.0409 0.1169  0.0159  109 ALA B CB  
1520 N  N   . LEU B 110 ? 0.1860 0.1571 0.1487 -0.0300 0.0260  -0.0366 110 LEU B N   
1521 C  CA  . LEU B 110 ? 0.1851 0.1374 0.1758 -0.0326 0.0162  -0.0232 110 LEU B CA  
1522 C  C   . LEU B 110 ? 0.2100 0.1517 0.1500 -0.0468 0.0156  -0.0310 110 LEU B C   
1523 O  O   . LEU B 110 ? 0.1743 0.1234 0.1484 -0.0321 0.0222  -0.0125 110 LEU B O   
1524 C  CB  . LEU B 110 ? 0.2063 0.1590 0.1704 -0.0265 0.0240  -0.0805 110 LEU B CB  
1525 C  CG  . LEU B 110 ? 0.1932 0.2023 0.1772 -0.0020 0.0179  -0.0303 110 LEU B CG  
1526 C  CD1 . LEU B 110 ? 0.1670 0.2449 0.2033 -0.0247 0.0011  -0.0359 110 LEU B CD1 
1527 C  CD2 . LEU B 110 ? 0.2410 0.2911 0.2436 -0.0018 0.1069  -0.0873 110 LEU B CD2 
1528 N  N   . LEU B 111 ? 0.1562 0.1456 0.0957 -0.0245 0.0217  -0.0273 111 LEU B N   
1529 C  CA  . LEU B 111 ? 0.1667 0.1360 0.1568 -0.0048 0.0578  0.0011  111 LEU B CA  
1530 C  C   . LEU B 111 ? 0.1463 0.1255 0.1334 -0.0372 0.0098  -0.0255 111 LEU B C   
1531 O  O   . LEU B 111 ? 0.1408 0.1455 0.1199 -0.0168 -0.0001 -0.0267 111 LEU B O   
1532 C  CB  . LEU B 111 ? 0.1659 0.1377 0.1398 -0.0258 0.0266  -0.0227 111 LEU B CB  
1533 C  CG  . LEU B 111 ? 0.1457 0.1420 0.1586 -0.0066 0.0409  -0.0309 111 LEU B CG  
1534 C  CD1 . LEU B 111 ? 0.1936 0.1394 0.2105 -0.0224 0.1115  -0.0382 111 LEU B CD1 
1535 C  CD2 . LEU B 111 ? 0.1479 0.1584 0.1381 -0.0157 0.0084  -0.0127 111 LEU B CD2 
1536 N  N   . SER B 112 ? 0.1023 0.1342 0.1209 -0.0135 0.0155  -0.0219 112 SER B N   
1537 C  CA  . SER B 112 ? 0.1339 0.1423 0.1279 -0.0139 0.0134  -0.0002 112 SER B CA  
1538 C  C   . SER B 112 ? 0.1425 0.0934 0.1319 0.0145  0.0358  0.0007  112 SER B C   
1539 O  O   . SER B 112 ? 0.1441 0.1483 0.1496 -0.0067 0.0372  -0.0162 112 SER B O   
1540 C  CB  . SER B 112 ? 0.1519 0.1794 0.1704 0.0017  0.0202  -0.0158 112 SER B CB  
1541 O  OG  . SER B 112 ? 0.1630 0.1889 0.1690 0.0300  0.0339  -0.0185 112 SER B OG  
1542 N  N   . PRO B 113 ? 0.1466 0.0989 0.1852 -0.0044 0.0243  -0.0067 113 PRO B N   
1543 C  CA  . PRO B 113 ? 0.1368 0.1450 0.1727 -0.0043 0.0056  -0.0088 113 PRO B CA  
1544 C  C   . PRO B 113 ? 0.0978 0.1377 0.1274 -0.0147 0.0603  -0.0144 113 PRO B C   
1545 O  O   . PRO B 113 ? 0.1061 0.1653 0.1666 0.0079  0.0135  0.0256  113 PRO B O   
1546 C  CB  . PRO B 113 ? 0.1701 0.1375 0.1818 -0.0046 -0.0219 -0.0058 113 PRO B CB  
1547 C  CG  . PRO B 113 ? 0.1905 0.1731 0.1672 -0.0405 -0.0027 -0.0082 113 PRO B CG  
1548 C  CD  . PRO B 113 ? 0.1426 0.1716 0.1913 0.0010  0.0154  -0.0104 113 PRO B CD  
1549 N  N   . TYR B 114 ? 0.1357 0.1242 0.1365 0.0181  0.0267  -0.0200 114 TYR B N   
1550 C  CA  . TYR B 114 ? 0.1055 0.1668 0.1640 -0.0139 0.0212  -0.0181 114 TYR B CA  
1551 C  C   . TYR B 114 ? 0.1576 0.1639 0.1622 -0.0232 0.0230  -0.0421 114 TYR B C   
1552 O  O   . TYR B 114 ? 0.2009 0.1606 0.1466 -0.0107 0.0080  -0.0261 114 TYR B O   
1553 C  CB  . TYR B 114 ? 0.1052 0.1511 0.1720 -0.0172 0.0252  0.0026  114 TYR B CB  
1554 C  CG  . TYR B 114 ? 0.1305 0.1783 0.0779 -0.0043 0.0137  -0.0204 114 TYR B CG  
1555 C  CD1 . TYR B 114 ? 0.1774 0.1688 0.1656 -0.0103 -0.0654 0.0013  114 TYR B CD1 
1556 C  CD2 . TYR B 114 ? 0.1239 0.1692 0.1159 -0.0179 0.0042  -0.0038 114 TYR B CD2 
1557 C  CE1 . TYR B 114 ? 0.2141 0.1822 0.1761 -0.0423 -0.0449 0.0201  114 TYR B CE1 
1558 C  CE2 . TYR B 114 ? 0.1430 0.2253 0.1635 -0.0295 -0.0631 0.0686  114 TYR B CE2 
1559 C  CZ  . TYR B 114 ? 0.2573 0.1609 0.1559 0.0239  -0.0494 0.0195  114 TYR B CZ  
1560 O  OH  . TYR B 114 ? 0.1692 0.1866 0.3187 -0.0130 -0.0134 0.0765  114 TYR B OH  
1561 N  N   . SER B 115 ? 0.1269 0.1136 0.1867 -0.0327 0.0111  -0.0404 115 SER B N   
1562 C  CA  . SER B 115 ? 0.1232 0.1203 0.1215 -0.0342 0.0055  -0.0234 115 SER B CA  
1563 C  C   . SER B 115 ? 0.1592 0.1268 0.1291 -0.0214 0.0123  0.0057  115 SER B C   
1564 O  O   . SER B 115 ? 0.1786 0.1488 0.1210 -0.0199 0.0366  -0.0184 115 SER B O   
1565 C  CB  . SER B 115 ? 0.1683 0.1194 0.1861 -0.0396 0.1327  -0.0527 115 SER B CB  
1566 O  OG  . SER B 115 ? 0.2168 0.2021 0.2899 -0.0236 0.0273  -0.0771 115 SER B OG  
1567 N  N   . TYR B 116 ? 0.1545 0.1497 0.1643 -0.0345 -0.0094 0.0045  116 TYR B N   
1568 C  CA  . TYR B 116 ? 0.1016 0.1344 0.1455 -0.0190 0.0333  -0.0119 116 TYR B CA  
1569 C  C   . TYR B 116 ? 0.1035 0.1321 0.1426 -0.0143 -0.0003 -0.0105 116 TYR B C   
1570 O  O   . TYR B 116 ? 0.1971 0.1608 0.1549 -0.0355 0.0355  -0.0348 116 TYR B O   
1571 C  CB  . TYR B 116 ? 0.1328 0.2100 0.1141 -0.0146 0.0321  -0.0535 116 TYR B CB  
1572 C  CG  . TYR B 116 ? 0.1520 0.1582 0.0708 0.0187  -0.0118 -0.0146 116 TYR B CG  
1573 C  CD1 . TYR B 116 ? 0.1178 0.1834 0.2075 -0.0033 -0.0179 0.0054  116 TYR B CD1 
1574 C  CD2 . TYR B 116 ? 0.1925 0.3041 0.1360 0.1039  -0.0149 0.0033  116 TYR B CD2 
1575 C  CE1 . TYR B 116 ? 0.1554 0.1594 0.2937 -0.0089 -0.0198 -0.0507 116 TYR B CE1 
1576 C  CE2 . TYR B 116 ? 0.2616 0.3156 0.2719 0.0794  -0.0852 0.0329  116 TYR B CE2 
1577 C  CZ  . TYR B 116 ? 0.1173 0.2579 0.2363 0.0230  -0.0243 -0.0501 116 TYR B CZ  
1578 O  OH  . TYR B 116 ? 0.1708 0.5498 0.5007 0.0973  -0.1525 -0.3119 116 TYR B OH  
1579 N  N   . SER B 117 ? 0.1579 0.1117 0.1784 -0.0176 -0.0441 -0.0281 117 SER B N   
1580 C  CA  . SER B 117 ? 0.1855 0.1040 0.1771 -0.0456 0.0040  -0.0289 117 SER B CA  
1581 C  C   . SER B 117 ? 0.2068 0.1501 0.1355 -0.0227 -0.0096 -0.0384 117 SER B C   
1582 O  O   . SER B 117 ? 0.2316 0.1464 0.1190 -0.0839 -0.0011 -0.0203 117 SER B O   
1583 C  CB  . SER B 117 ? 0.1891 0.1430 0.2224 -0.0001 0.0555  0.0008  117 SER B CB  
1584 O  OG  . SER B 117 ? 0.1875 0.2460 0.2290 -0.0269 0.0583  -0.0447 117 SER B OG  
1585 N  N   . THR B 118 ? 0.2126 0.1651 0.1101 -0.0354 -0.0077 -0.0042 118 THR B N   
1586 C  CA  . THR B 118 ? 0.2013 0.1451 0.1147 -0.0222 -0.0071 -0.0258 118 THR B CA  
1587 C  C   . THR B 118 ? 0.2286 0.1718 0.1573 -0.0468 -0.0572 0.0148  118 THR B C   
1588 O  O   . THR B 118 ? 0.3000 0.2013 0.1506 -0.0176 -0.0751 0.0336  118 THR B O   
1589 C  CB  . THR B 118 ? 0.2256 0.1933 0.1763 -0.0159 -0.0058 -0.0030 118 THR B CB  
1590 O  OG1 . THR B 118 ? 0.2976 0.2950 0.2576 0.0233  0.0651  0.0233  118 THR B OG1 
1591 C  CG2 . THR B 118 ? 0.1937 0.3235 0.1202 -0.0565 -0.0055 0.0238  118 THR B CG2 
1592 N  N   . THR B 119 ? 0.2404 0.1391 0.1686 -0.0629 -0.0539 0.0133  119 THR B N   
1593 C  CA  . THR B 119 ? 0.2212 0.1398 0.1864 -0.0203 0.0129  0.0285  119 THR B CA  
1594 C  C   . THR B 119 ? 0.2205 0.2021 0.1577 -0.0065 -0.0009 0.0046  119 THR B C   
1595 O  O   . THR B 119 ? 0.3604 0.1760 0.1855 -0.0259 0.0802  0.0035  119 THR B O   
1596 C  CB  . THR B 119 ? 0.2478 0.2837 0.2906 0.0359  -0.0194 0.0207  119 THR B CB  
1597 O  OG1 . THR B 119 ? 0.3326 0.2955 0.3208 0.0440  0.0470  0.0563  119 THR B OG1 
1598 C  CG2 . THR B 119 ? 0.2665 0.4011 0.2151 -0.0774 0.0942  0.0194  119 THR B CG2 
1599 N  N   . ALA B 120 ? 0.2376 0.1671 0.2003 -0.0077 -0.0033 -0.0417 120 ALA B N   
1600 C  CA  . ALA B 120 ? 0.2770 0.1912 0.1779 0.0122  -0.0136 -0.0077 120 ALA B CA  
1601 C  C   . ALA B 120 ? 0.3142 0.1245 0.2575 0.0094  0.0184  -0.0104 120 ALA B C   
1602 O  O   . ALA B 120 ? 0.3141 0.1808 0.2054 0.0236  0.0494  -0.0135 120 ALA B O   
1603 C  CB  . ALA B 120 ? 0.3033 0.2339 0.2963 -0.0340 0.0045  0.0091  120 ALA B CB  
1604 N  N   . VAL B 121 ? 0.3670 0.1304 0.2299 0.0121  0.0402  -0.0065 121 VAL B N   
1605 C  CA  . VAL B 121 ? 0.3579 0.2211 0.2179 0.0796  0.0647  0.0156  121 VAL B CA  
1606 C  C   . VAL B 121 ? 0.3740 0.2327 0.2560 0.1067  0.0886  0.0267  121 VAL B C   
1607 O  O   . VAL B 121 ? 0.4006 0.2608 0.2085 0.0763  0.1223  0.0493  121 VAL B O   
1608 C  CB  . VAL B 121 ? 0.3220 0.3273 0.1873 0.0301  0.0525  0.0849  121 VAL B CB  
1609 C  CG1 . VAL B 121 ? 0.4471 0.4953 0.2606 0.1415  -0.0711 0.0578  121 VAL B CG1 
1610 C  CG2 . VAL B 121 ? 0.4297 0.4227 0.1673 -0.0657 0.0366  0.0530  121 VAL B CG2 
1611 N  N   . VAL B 122 ? 0.4916 0.2512 0.2058 0.0893  0.1968  0.0776  122 VAL B N   
1612 C  CA  . VAL B 122 ? 0.5852 0.2261 0.1671 0.1431  0.2475  0.0231  122 VAL B CA  
1613 C  C   . VAL B 122 ? 0.8360 0.4740 0.2869 0.1168  0.2474  0.3191  122 VAL B C   
1614 O  O   . VAL B 122 ? 0.9673 0.7773 0.4232 0.1700  0.1540  0.1526  122 VAL B O   
1615 C  CB  . VAL B 122 ? 0.5619 0.5242 0.5686 -0.0579 0.1960  -0.2256 122 VAL B CB  
1616 CA CA  . CA  C .   ? 0.2161 0.1529 0.2557 0.0140  -0.0635 -0.0075 201 CA  A CA  
1617 O  O1  . Z7Z D .   ? 1.0069 0.5811 0.7703 0.1318  -0.0107 0.0678  202 Z7Z A O1  
1618 C  C1  . Z7Z D .   ? 0.5779 0.4797 0.2430 0.2529  -0.1144 -0.0364 202 Z7Z A C1  
1619 O  O2  . Z7Z D .   ? 0.5334 0.5048 0.2853 0.0459  -0.1623 -0.1004 202 Z7Z A O2  
1620 C  C2  . Z7Z D .   ? 0.5665 0.5535 0.2285 0.0603  0.0380  -0.1313 202 Z7Z A C2  
1621 C  C3  . Z7Z D .   ? 0.5474 0.4930 0.3298 0.1380  -0.0084 -0.1242 202 Z7Z A C3  
1622 C  C4  . Z7Z D .   ? 0.5191 0.3872 0.3362 0.1361  0.0515  -0.0781 202 Z7Z A C4  
1623 C  C5  . Z7Z D .   ? 0.5510 0.5914 0.3195 0.1589  -0.0225 0.0924  202 Z7Z A C5  
1624 C  C6  . Z7Z D .   ? 0.4513 0.4255 0.2987 0.1852  0.0655  -0.0921 202 Z7Z A C6  
1625 C  C7  . Z7Z D .   ? 0.3897 0.4002 0.3914 0.1058  0.0146  -0.0224 202 Z7Z A C7  
1626 C  C8  . Z7Z D .   ? 0.3029 0.1859 0.3756 -0.0149 -0.0039 -0.0022 202 Z7Z A C8  
1627 C  C9  . Z7Z D .   ? 0.3688 0.2948 0.2673 -0.0370 -0.0263 -0.0407 202 Z7Z A C9  
1628 C  C10 . Z7Z D .   ? 0.3783 0.2724 0.2722 -0.0346 0.0217  0.0340  202 Z7Z A C10 
1629 C  C11 . Z7Z D .   ? 0.3030 0.2510 0.2710 -0.0833 -0.0715 -0.0632 202 Z7Z A C11 
1630 C  C12 . Z7Z D .   ? 0.3118 0.2613 0.2778 -0.0778 0.0635  0.0544  202 Z7Z A C12 
1631 C  C13 . Z7Z D .   ? 0.3324 0.3481 0.3485 -0.1056 -0.0015 -0.0042 202 Z7Z A C13 
1632 O  O1  . Z7Z E .   ? 0.4190 0.3847 0.4502 -0.0639 -0.0444 0.0484  201 Z7Z B O1  
1633 C  C1  . Z7Z E .   ? 0.4396 0.3602 0.3429 -0.0303 -0.0611 0.0277  201 Z7Z B C1  
1634 O  O2  . Z7Z E .   ? 0.3686 0.3215 0.5360 -0.0273 -0.0029 0.0756  201 Z7Z B O2  
1635 C  C2  . Z7Z E .   ? 0.3609 0.2912 0.3452 0.1094  0.0188  0.0310  201 Z7Z B C2  
1636 C  C3  . Z7Z E .   ? 0.4467 0.4425 0.3651 0.0183  0.0093  0.0103  201 Z7Z B C3  
1637 C  C4  . Z7Z E .   ? 0.3670 0.4866 0.3682 -0.0061 -0.0246 0.0138  201 Z7Z B C4  
1638 C  C5  . Z7Z E .   ? 0.4712 0.4253 0.3236 0.0152  0.0368  -0.0220 201 Z7Z B C5  
1639 C  C6  . Z7Z E .   ? 0.3390 0.4752 0.3459 -0.0290 0.0643  -0.0062 201 Z7Z B C6  
1640 C  C7  . Z7Z E .   ? 0.2934 0.4271 0.3695 0.0512  -0.0020 -0.0052 201 Z7Z B C7  
1641 C  C8  . Z7Z E .   ? 0.3141 0.2682 0.3460 -0.0084 0.0014  0.0009  201 Z7Z B C8  
1642 C  C9  . Z7Z E .   ? 0.3311 0.3746 0.3066 -0.0329 0.0299  0.0957  201 Z7Z B C9  
1643 C  C10 . Z7Z E .   ? 0.3507 0.3797 0.3046 -0.0248 -0.0111 -0.0919 201 Z7Z B C10 
1644 C  C11 . Z7Z E .   ? 0.3723 0.2979 0.3281 -0.0400 -0.0207 0.0427  201 Z7Z B C11 
1645 C  C12 . Z7Z E .   ? 0.3828 0.2818 0.3210 -0.0518 0.0029  -0.0546 201 Z7Z B C12 
1646 C  C13 . Z7Z E .   ? 0.4387 0.3183 0.3850 0.0162  -0.0004 0.0007  201 Z7Z B C13 
1647 O  O   . HOH F .   ? 0.2627 0.2227 0.3541 0.1010  -0.0864 -0.0201 301 HOH A O   
1648 O  O   . HOH F .   ? 0.4315 0.3727 0.3089 -0.0688 0.0221  0.0158  302 HOH A O   
1649 O  O   . HOH F .   ? 0.3583 0.4151 0.3571 -0.1781 -0.1498 0.1919  303 HOH A O   
1650 O  O   . HOH F .   ? 0.2575 0.1775 0.2992 0.0178  -0.0172 0.0275  304 HOH A O   
1651 O  O   . HOH F .   ? 0.3783 0.2673 0.2155 -0.1055 0.0544  -0.0055 305 HOH A O   
1652 O  O   . HOH F .   ? 0.3738 0.2722 0.3540 -0.0869 -0.0149 0.0265  306 HOH A O   
1653 O  O   . HOH F .   ? 0.2214 0.1533 0.2491 0.0595  -0.0730 -0.0111 307 HOH A O   
1654 O  O   . HOH F .   ? 0.2713 0.2624 0.2503 -0.0454 -0.0393 -0.0881 308 HOH A O   
1655 O  O   . HOH F .   ? 0.2941 0.2812 0.2037 -0.0220 0.0141  0.0046  309 HOH A O   
1656 O  O   . HOH F .   ? 0.2335 0.1542 0.2821 0.0062  -0.0608 -0.0415 310 HOH A O   
1657 O  O   . HOH F .   ? 0.1560 0.2664 0.2788 0.0382  0.0776  -0.0186 311 HOH A O   
1658 O  O   . HOH F .   ? 0.1980 0.1760 0.1711 -0.0134 -0.0228 0.0255  312 HOH A O   
1659 O  O   . HOH F .   ? 0.4094 0.3937 0.4600 -0.0100 0.1211  -0.0678 313 HOH A O   
1660 O  O   . HOH F .   ? 0.2594 0.3230 0.4398 -0.0513 -0.1162 0.0644  314 HOH A O   
1661 O  O   . HOH F .   ? 0.3308 0.2518 0.3127 -0.0284 -0.0512 0.0077  315 HOH A O   
1662 O  O   . HOH F .   ? 0.2448 0.2744 0.3409 0.0399  -0.1548 -0.0326 316 HOH A O   
1663 O  O   . HOH F .   ? 0.2267 0.2110 0.2776 0.0219  -0.0538 -0.0257 317 HOH A O   
1664 O  O   . HOH F .   ? 0.3223 0.2244 0.2860 0.0283  -0.0114 -0.0276 318 HOH A O   
1665 O  O   . HOH F .   ? 0.3987 0.2128 0.6039 -0.0244 -0.0571 0.0383  319 HOH A O   
1666 O  O   . HOH F .   ? 0.2996 0.2437 0.1995 -0.0261 -0.0257 -0.0102 320 HOH A O   
1667 O  O   . HOH F .   ? 0.2227 0.2179 0.3024 0.0081  -0.0885 0.0435  321 HOH A O   
1668 O  O   . HOH F .   ? 0.2117 0.3560 0.4242 -0.0254 -0.0467 -0.0728 322 HOH A O   
1669 O  O   . HOH F .   ? 0.2134 0.3011 0.2235 -0.0364 -0.0499 0.0195  323 HOH A O   
1670 O  O   . HOH F .   ? 0.4251 0.2491 0.4140 0.0027  -0.1706 0.0524  324 HOH A O   
1671 O  O   . HOH F .   ? 0.3627 0.3226 0.3734 0.0584  -0.0207 0.0016  325 HOH A O   
1672 O  O   . HOH F .   ? 0.5700 0.4160 0.2793 -0.0867 -0.0404 -0.0952 326 HOH A O   
1673 O  O   . HOH F .   ? 0.5434 0.1522 0.4184 0.0650  0.2513  0.1008  327 HOH A O   
1674 O  O   . HOH F .   ? 0.4154 0.3388 0.2405 -0.0017 0.0035  0.0624  328 HOH A O   
1675 O  O   . HOH F .   ? 0.2750 0.5360 0.4787 0.1018  0.0680  0.1472  329 HOH A O   
1676 O  O   . HOH F .   ? 0.1438 0.1352 0.2825 -0.0128 -0.0262 -0.0106 330 HOH A O   
1677 O  O   . HOH F .   ? 0.5764 0.5956 0.2693 0.1898  0.2287  0.0101  331 HOH A O   
1678 O  O   . HOH F .   ? 0.4080 0.3074 0.3205 -0.1515 -0.0668 0.0068  332 HOH A O   
1679 O  O   . HOH F .   ? 0.3161 0.2560 0.3836 0.0176  -0.0549 -0.0216 333 HOH A O   
1680 O  O   . HOH F .   ? 0.3459 0.2874 0.3231 -0.0268 0.0186  -0.1188 334 HOH A O   
1681 O  O   . HOH F .   ? 0.3599 0.3184 0.4230 0.0138  -0.1077 -0.0713 335 HOH A O   
1682 O  O   . HOH F .   ? 0.3320 0.3886 0.2549 0.1068  0.0301  0.0870  336 HOH A O   
1683 O  O   . HOH F .   ? 0.2805 0.2268 0.3479 0.0420  -0.0463 -0.0516 337 HOH A O   
1684 O  O   . HOH F .   ? 0.1599 0.1673 0.2261 -0.0098 -0.0157 0.0316  338 HOH A O   
1685 O  O   . HOH F .   ? 0.3128 0.6106 0.4447 0.0973  -0.0584 0.0122  339 HOH A O   
1686 O  O   . HOH F .   ? 0.2840 0.6858 0.2914 0.0016  0.0024  0.0816  340 HOH A O   
1687 O  O   . HOH F .   ? 0.3958 0.3890 0.4278 0.0766  0.0264  0.1251  341 HOH A O   
1688 O  O   . HOH F .   ? 0.3931 0.5219 0.3988 -0.1079 0.0409  -0.0067 342 HOH A O   
1689 O  O   . HOH F .   ? 0.4054 0.2996 0.3764 -0.0057 -0.0825 -0.0055 343 HOH A O   
1690 O  O   . HOH F .   ? 0.3343 0.2172 0.4021 -0.0383 0.0854  -0.0117 344 HOH A O   
1691 O  O   . HOH F .   ? 0.3876 0.3798 0.4170 -0.0368 -0.1421 0.0514  345 HOH A O   
1692 O  O   . HOH F .   ? 0.2333 0.3396 0.3805 0.0297  -0.0107 0.1332  346 HOH A O   
1693 O  O   . HOH F .   ? 0.2032 0.1948 0.2198 0.0057  0.0403  -0.0260 347 HOH A O   
1694 O  O   . HOH F .   ? 0.4229 0.2726 0.4477 0.0919  -0.1033 0.0088  348 HOH A O   
1695 O  O   . HOH F .   ? 0.5987 0.2537 0.2977 0.0016  0.0008  0.0324  349 HOH A O   
1696 O  O   . HOH F .   ? 0.4323 0.2763 0.4535 -0.0632 0.0589  0.0644  350 HOH A O   
1697 O  O   . HOH G .   ? 0.4152 0.3575 0.4699 0.0808  0.1493  0.0563  301 HOH B O   
1698 O  O   . HOH G .   ? 0.3551 0.3060 0.2707 -0.0498 0.2040  -0.0060 302 HOH B O   
1699 O  O   . HOH G .   ? 0.2054 0.2117 0.3193 0.0087  -0.0633 -0.0973 303 HOH B O   
1700 O  O   . HOH G .   ? 0.2148 0.2257 0.3119 -0.0175 0.0104  0.0270  304 HOH B O   
1701 O  O   . HOH G .   ? 0.2702 0.2200 0.1785 0.1361  -0.0643 -0.0399 305 HOH B O   
1702 O  O   . HOH G .   ? 0.1597 0.1627 0.1928 -0.0693 0.0060  -0.0141 306 HOH B O   
1703 O  O   . HOH G .   ? 0.2301 0.4630 0.3695 -0.0045 0.0447  0.0347  307 HOH B O   
1704 O  O   . HOH G .   ? 0.2382 0.2239 0.4288 -0.0485 -0.0137 0.0015  308 HOH B O   
1705 O  O   . HOH G .   ? 0.1147 0.2473 0.2233 -0.0157 0.0006  -0.0076 309 HOH B O   
1706 O  O   . HOH G .   ? 0.3323 0.2684 0.2507 -0.0385 0.0267  0.0010  310 HOH B O   
1707 O  O   . HOH G .   ? 0.2434 0.2134 0.3536 -0.0208 -0.0586 0.0916  311 HOH B O   
1708 O  O   . HOH G .   ? 0.1675 0.1364 0.1385 -0.0194 0.0184  -0.0098 312 HOH B O   
1709 O  O   . HOH G .   ? 0.5409 0.2576 0.2446 -0.0328 0.2351  0.0095  313 HOH B O   
1710 O  O   . HOH G .   ? 0.5064 0.3675 0.2931 -0.0180 -0.1158 -0.0630 314 HOH B O   
1711 O  O   . HOH G .   ? 0.2803 0.3421 0.2971 -0.0995 0.0020  -0.0322 315 HOH B O   
1712 O  O   . HOH G .   ? 0.2039 0.1884 0.2123 -0.0235 0.0189  0.0092  316 HOH B O   
1713 O  O   . HOH G .   ? 0.4126 0.3556 0.4668 -0.0842 0.0124  -0.0205 317 HOH B O   
1714 O  O   . HOH G .   ? 0.2125 0.2004 0.2406 0.0193  0.0586  -0.0143 318 HOH B O   
1715 O  O   . HOH G .   ? 0.5958 0.2752 0.4924 0.0011  -0.0446 -0.0526 319 HOH B O   
1716 O  O   . HOH G .   ? 0.3872 0.3437 0.3501 -0.0568 0.1083  -0.0782 320 HOH B O   
1717 O  O   . HOH G .   ? 0.3823 0.3408 0.4186 -0.0437 -0.1492 -0.0226 321 HOH B O   
1718 O  O   . HOH G .   ? 0.4504 0.3290 0.5311 -0.0381 -0.0528 0.0271  322 HOH B O   
1719 O  O   . HOH G .   ? 0.3895 0.4981 0.2321 0.0627  0.0685  0.0900  323 HOH B O   
# 
