data_9H7F
# 
_entry.id   9H7F 
# 
_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   9H7F         pdb_00009h7f 10.2210/pdb9h7f/pdb 
WWPDB D_1292142788 ?            ?                   
# 
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                        9H7F 
_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           N 
# 
_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 '3,5-bis(chloranyl)aniline' 162.017   1   ? ? ? ? 
3 water       nat water                       18.015    105 ? ? ? ? 
# 
_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 '3,5-bis(chloranyl)aniline' A1ISU 
3 water                       HOH   
# 
loop_
_entity_poly_seq.entity_id 
_entity_poly_seq.num 
_entity_poly_seq.mon_id 
_entity_poly_seq.hetero 
1 1   GLY n 
1 2   PRO n 
1 3   THR n 
1 4   GLY n 
1 5   THR n 
1 6   GLY n 
1 7   GLU n 
1 8   SER n 
1 9   LYS n 
1 10  CYS n 
1 11  PRO n 
1 12  LEU n 
1 13  MET n 
1 14  VAL n 
1 15  LYS n 
1 16  VAL n 
1 17  LEU n 
1 18  ASP n 
1 19  ALA n 
1 20  VAL n 
1 21  ARG n 
1 22  GLY n 
1 23  SER n 
1 24  PRO n 
1 25  ALA n 
1 26  ILE n 
1 27  ASN n 
1 28  VAL n 
1 29  ALA n 
1 30  VAL n 
1 31  HIS n 
1 32  VAL n 
1 33  PHE n 
1 34  ARG n 
1 35  LYS n 
1 36  ALA n 
1 37  ALA n 
1 38  ASP n 
1 39  ASP n 
1 40  THR n 
1 41  TRP n 
1 42  GLU n 
1 43  PRO n 
1 44  PHE n 
1 45  ALA n 
1 46  SER n 
1 47  GLY n 
1 48  LYS n 
1 49  THR n 
1 50  SER n 
1 51  GLU n 
1 52  SER n 
1 53  GLY n 
1 54  GLU n 
1 55  LEU n 
1 56  HIS n 
1 57  GLY n 
1 58  LEU n 
1 59  THR n 
1 60  THR n 
1 61  GLU n 
1 62  GLU n 
1 63  GLU n 
1 64  PHE n 
1 65  VAL n 
1 66  GLU n 
1 67  GLY n 
1 68  ILE n 
1 69  TYR n 
1 70  LYS n 
1 71  VAL n 
1 72  GLU n 
1 73  ILE n 
1 74  ASP n 
1 75  THR n 
1 76  LYS n 
1 77  SER n 
1 78  TYR n 
1 79  TRP n 
1 80  LYS n 
1 81  ALA n 
1 82  LEU n 
1 83  GLY n 
1 84  ILE n 
1 85  SER n 
1 86  PRO n 
1 87  PHE n 
1 88  HIS n 
1 89  GLU n 
1 90  HIS n 
1 91  ALA n 
1 92  GLU n 
1 93  VAL n 
1 94  VAL n 
1 95  PHE n 
1 96  THR n 
1 97  ALA n 
1 98  ASN n 
1 99  ASP n 
1 100 SER n 
1 101 GLY n 
1 102 PRO n 
1 103 ARG n 
1 104 ARG n 
1 105 TYR n 
1 106 THR n 
1 107 ILE n 
1 108 ALA n 
1 109 ALA n 
1 110 LEU n 
1 111 LEU n 
1 112 SER n 
1 113 PRO n 
1 114 TYR n 
1 115 SER n 
1 116 TYR n 
1 117 SER n 
1 118 THR n 
1 119 THR n 
1 120 ALA n 
1 121 VAL n 
1 122 VAL n 
1 123 THR n 
1 124 ASN n 
1 125 PRO n 
1 126 LYS n 
1 127 GLU n 
# 
_entity_src_gen.entity_id                          1 
_entity_src_gen.pdbx_src_id                        1 
_entity_src_gen.pdbx_alt_source_flag               sample 
_entity_src_gen.pdbx_seq_type                      'Biological sequence' 
_entity_src_gen.pdbx_beg_seq_num                   1 
_entity_src_gen.pdbx_end_seq_num                   127 
_entity_src_gen.gene_src_common_name               human 
_entity_src_gen.gene_src_genus                     ? 
_entity_src_gen.pdbx_gene_src_gene                 'TTR, PALB' 
_entity_src_gen.gene_src_species                   ? 
_entity_src_gen.gene_src_strain                    ? 
_entity_src_gen.gene_src_tissue                    Blood 
_entity_src_gen.gene_src_tissue_fraction           ? 
_entity_src_gen.gene_src_details                   ? 
_entity_src_gen.pdbx_gene_src_fragment             ? 
_entity_src_gen.pdbx_gene_src_scientific_name      'Homo sapiens' 
_entity_src_gen.pdbx_gene_src_ncbi_taxonomy_id     9606 
_entity_src_gen.pdbx_gene_src_variant              ? 
_entity_src_gen.pdbx_gene_src_cell_line            ? 
_entity_src_gen.pdbx_gene_src_atcc                 ? 
_entity_src_gen.pdbx_gene_src_organ                ? 
_entity_src_gen.pdbx_gene_src_organelle            ? 
_entity_src_gen.pdbx_gene_src_cell                 ? 
_entity_src_gen.pdbx_gene_src_cellular_location    ? 
_entity_src_gen.host_org_common_name               ? 
_entity_src_gen.pdbx_host_org_scientific_name      'Homo sapiens' 
_entity_src_gen.pdbx_host_org_ncbi_taxonomy_id     9606 
_entity_src_gen.host_org_genus                     ? 
_entity_src_gen.pdbx_host_org_gene                 ? 
_entity_src_gen.pdbx_host_org_organ                ? 
_entity_src_gen.host_org_species                   ? 
_entity_src_gen.pdbx_host_org_tissue               ? 
_entity_src_gen.pdbx_host_org_tissue_fraction      ? 
_entity_src_gen.pdbx_host_org_strain               ? 
_entity_src_gen.pdbx_host_org_variant              ? 
_entity_src_gen.pdbx_host_org_cell_line            ? 
_entity_src_gen.pdbx_host_org_atcc                 ? 
_entity_src_gen.pdbx_host_org_culture_collection   ? 
_entity_src_gen.pdbx_host_org_cell                 ? 
_entity_src_gen.pdbx_host_org_organelle            ? 
_entity_src_gen.pdbx_host_org_cellular_location    ? 
_entity_src_gen.pdbx_host_org_vector_type          ? 
_entity_src_gen.pdbx_host_org_vector               ? 
_entity_src_gen.host_org_details                   ? 
_entity_src_gen.expression_system_id               ? 
_entity_src_gen.plasmid_name                       ? 
_entity_src_gen.plasmid_details                    ? 
_entity_src_gen.pdbx_description                   ? 
# 
loop_
_chem_comp.id 
_chem_comp.type 
_chem_comp.mon_nstd_flag 
_chem_comp.name 
_chem_comp.pdbx_synonyms 
_chem_comp.formula 
_chem_comp.formula_weight 
A1ISU non-polymer         . '3,5-bis(chloranyl)aniline' 3,5-dichloroaniline 'C6 H5 Cl2 N'    162.017 
ALA   'L-peptide linking' y ALANINE                     ?                   'C3 H7 N O2'     89.093  
ARG   'L-peptide linking' y ARGININE                    ?                   'C6 H15 N4 O2 1' 175.209 
ASN   'L-peptide linking' y ASPARAGINE                  ?                   'C4 H8 N2 O3'    132.118 
ASP   'L-peptide linking' y 'ASPARTIC ACID'             ?                   'C4 H7 N O4'     133.103 
CYS   'L-peptide linking' y CYSTEINE                    ?                   'C3 H7 N O2 S'   121.158 
GLU   'L-peptide linking' y 'GLUTAMIC ACID'             ?                   'C5 H9 N O4'     147.129 
GLY   'peptide linking'   y GLYCINE                     ?                   'C2 H5 N O2'     75.067  
HIS   'L-peptide linking' y HISTIDINE                   ?                   'C6 H10 N3 O2 1' 156.162 
HOH   non-polymer         . WATER                       ?                   'H2 O'           18.015  
ILE   'L-peptide linking' y ISOLEUCINE                  ?                   'C6 H13 N O2'    131.173 
LEU   'L-peptide linking' y LEUCINE                     ?                   'C6 H13 N O2'    131.173 
LYS   'L-peptide linking' y LYSINE                      ?                   'C6 H15 N2 O2 1' 147.195 
MET   'L-peptide linking' y METHIONINE                  ?                   'C5 H11 N O2 S'  149.211 
PHE   'L-peptide linking' y PHENYLALANINE               ?                   'C9 H11 N O2'    165.189 
PRO   'L-peptide linking' y PROLINE                     ?                   'C5 H9 N O2'     115.130 
SER   'L-peptide linking' y SERINE                      ?                   'C3 H7 N O3'     105.093 
THR   'L-peptide linking' y THREONINE                   ?                   'C4 H9 N O3'     119.119 
TRP   'L-peptide linking' y TRYPTOPHAN                  ?                   'C11 H12 N2 O2'  204.225 
TYR   'L-peptide linking' y TYROSINE                    ?                   'C9 H11 N O3'    181.189 
VAL   'L-peptide linking' y VALINE                      ?                   'C5 H11 N O2'    117.146 
# 
loop_
_pdbx_poly_seq_scheme.asym_id 
_pdbx_poly_seq_scheme.entity_id 
_pdbx_poly_seq_scheme.seq_id 
_pdbx_poly_seq_scheme.mon_id 
_pdbx_poly_seq_scheme.ndb_seq_num 
_pdbx_poly_seq_scheme.pdb_seq_num 
_pdbx_poly_seq_scheme.auth_seq_num 
_pdbx_poly_seq_scheme.pdb_mon_id 
_pdbx_poly_seq_scheme.auth_mon_id 
_pdbx_poly_seq_scheme.pdb_strand_id 
_pdbx_poly_seq_scheme.pdb_ins_code 
_pdbx_poly_seq_scheme.hetero 
A 1 1   GLY 1   1   ?   ?   ?   A . n 
A 1 2   PRO 2   2   ?   ?   ?   A . n 
A 1 3   THR 3   3   ?   ?   ?   A . n 
A 1 4   GLY 4   4   ?   ?   ?   A . n 
A 1 5   THR 5   5   ?   ?   ?   A . n 
A 1 6   GLY 6   6   ?   ?   ?   A . n 
A 1 7   GLU 7   7   ?   ?   ?   A . n 
A 1 8   SER 8   8   ?   ?   ?   A . n 
A 1 9   LYS 9   9   ?   ?   ?   A . n 
A 1 10  CYS 10  10  10  CYS CYS A . n 
A 1 11  PRO 11  11  11  PRO PRO A . n 
A 1 12  LEU 12  12  12  LEU LEU A . n 
A 1 13  MET 13  13  13  MET MET A . n 
A 1 14  VAL 14  14  14  VAL VAL A . n 
A 1 15  LYS 15  15  15  LYS LYS A . n 
A 1 16  VAL 16  16  16  VAL VAL A . n 
A 1 17  LEU 17  17  17  LEU LEU A . n 
A 1 18  ASP 18  18  18  ASP ASP A . n 
A 1 19  ALA 19  19  19  ALA ALA A . n 
A 1 20  VAL 20  20  20  VAL VAL A . n 
A 1 21  ARG 21  21  21  ARG ARG A . n 
A 1 22  GLY 22  22  22  GLY GLY A . n 
A 1 23  SER 23  23  23  SER SER A . n 
A 1 24  PRO 24  24  24  PRO PRO A . n 
A 1 25  ALA 25  25  25  ALA ALA A . n 
A 1 26  ILE 26  26  26  ILE ILE A . n 
A 1 27  ASN 27  27  27  ASN ASN A . n 
A 1 28  VAL 28  28  28  VAL VAL A . n 
A 1 29  ALA 29  29  29  ALA ALA A . n 
A 1 30  VAL 30  30  30  VAL VAL A . n 
A 1 31  HIS 31  31  31  HIS HIS A . n 
A 1 32  VAL 32  32  32  VAL VAL A . n 
A 1 33  PHE 33  33  33  PHE PHE A . n 
A 1 34  ARG 34  34  34  ARG ARG A . n 
A 1 35  LYS 35  35  35  LYS LYS A . n 
A 1 36  ALA 36  36  36  ALA ALA A . n 
A 1 37  ALA 37  37  37  ALA ALA A . n 
A 1 38  ASP 38  38  38  ASP ASP A . n 
A 1 39  ASP 39  39  39  ASP ASP A . n 
A 1 40  THR 40  40  40  THR THR A . n 
A 1 41  TRP 41  41  41  TRP TRP A . n 
A 1 42  GLU 42  42  42  GLU GLU A . n 
A 1 43  PRO 43  43  43  PRO PRO A . n 
A 1 44  PHE 44  44  44  PHE PHE A . n 
A 1 45  ALA 45  45  45  ALA ALA A . n 
A 1 46  SER 46  46  46  SER SER A . n 
A 1 47  GLY 47  47  47  GLY GLY A . n 
A 1 48  LYS 48  48  48  LYS LYS A . n 
A 1 49  THR 49  49  49  THR THR A . n 
A 1 50  SER 50  50  50  SER SER A . n 
A 1 51  GLU 51  51  51  GLU GLU A . n 
A 1 52  SER 52  52  52  SER SER A . n 
A 1 53  GLY 53  53  53  GLY GLY A . n 
A 1 54  GLU 54  54  54  GLU GLU A . n 
A 1 55  LEU 55  55  55  LEU LEU A . n 
A 1 56  HIS 56  56  56  HIS HIS A . n 
A 1 57  GLY 57  57  57  GLY GLY A . n 
A 1 58  LEU 58  58  58  LEU LEU A . n 
A 1 59  THR 59  59  59  THR THR A . n 
A 1 60  THR 60  60  60  THR THR A . n 
A 1 61  GLU 61  61  61  GLU GLU A . n 
A 1 62  GLU 62  62  62  GLU GLU A . n 
A 1 63  GLU 63  63  63  GLU GLU A . n 
A 1 64  PHE 64  64  64  PHE PHE A . n 
A 1 65  VAL 65  65  65  VAL VAL A . n 
A 1 66  GLU 66  66  66  GLU GLU A . n 
A 1 67  GLY 67  67  67  GLY GLY A . n 
A 1 68  ILE 68  68  68  ILE ILE A . n 
A 1 69  TYR 69  69  69  TYR TYR A . n 
A 1 70  LYS 70  70  70  LYS LYS A . n 
A 1 71  VAL 71  71  71  VAL VAL A . n 
A 1 72  GLU 72  72  72  GLU GLU A . n 
A 1 73  ILE 73  73  73  ILE ILE A . n 
A 1 74  ASP 74  74  74  ASP ASP A . n 
A 1 75  THR 75  75  75  THR THR A . n 
A 1 76  LYS 76  76  76  LYS LYS A . n 
A 1 77  SER 77  77  77  SER SER A . n 
A 1 78  TYR 78  78  78  TYR TYR A . n 
A 1 79  TRP 79  79  79  TRP TRP A . n 
A 1 80  LYS 80  80  80  LYS LYS A . n 
A 1 81  ALA 81  81  81  ALA ALA A . n 
A 1 82  LEU 82  82  82  LEU LEU A . n 
A 1 83  GLY 83  83  83  GLY GLY A . n 
A 1 84  ILE 84  84  84  ILE ILE A . n 
A 1 85  SER 85  85  85  SER SER A . n 
A 1 86  PRO 86  86  86  PRO PRO A . n 
A 1 87  PHE 87  87  87  PHE PHE A . n 
A 1 88  HIS 88  88  88  HIS HIS A . n 
A 1 89  GLU 89  89  89  GLU GLU A . n 
A 1 90  HIS 90  90  90  HIS HIS A . n 
A 1 91  ALA 91  91  91  ALA ALA A . n 
A 1 92  GLU 92  92  92  GLU GLU A . n 
A 1 93  VAL 93  93  93  VAL VAL A . n 
A 1 94  VAL 94  94  94  VAL VAL A . n 
A 1 95  PHE 95  95  95  PHE PHE A . n 
A 1 96  THR 96  96  96  THR THR A . n 
A 1 97  ALA 97  97  97  ALA ALA A . n 
A 1 98  ASN 98  98  98  ASN ASN A . n 
A 1 99  ASP 99  99  99  ASP ASP A . n 
A 1 100 SER 100 100 100 SER SER A . n 
A 1 101 GLY 101 101 101 GLY GLY A . n 
A 1 102 PRO 102 102 102 PRO PRO A . n 
A 1 103 ARG 103 103 103 ARG ARG A . n 
A 1 104 ARG 104 104 104 ARG ARG A . n 
A 1 105 TYR 105 105 105 TYR TYR A . n 
A 1 106 THR 106 106 106 THR THR A . n 
A 1 107 ILE 107 107 107 ILE ILE A . n 
A 1 108 ALA 108 108 108 ALA ALA A . n 
A 1 109 ALA 109 109 109 ALA ALA A . n 
A 1 110 LEU 110 110 110 LEU LEU A . n 
A 1 111 LEU 111 111 111 LEU LEU A . n 
A 1 112 SER 112 112 112 SER SER A . n 
A 1 113 PRO 113 113 113 PRO PRO A . n 
A 1 114 TYR 114 114 114 TYR TYR A . n 
A 1 115 SER 115 115 115 SER SER A . n 
A 1 116 TYR 116 116 116 TYR TYR A . n 
A 1 117 SER 117 117 117 SER SER A . n 
A 1 118 THR 118 118 118 THR THR A . n 
A 1 119 THR 119 119 119 THR THR A . n 
A 1 120 ALA 120 120 120 ALA ALA A . n 
A 1 121 VAL 121 121 121 VAL VAL A . n 
A 1 122 VAL 122 122 122 VAL VAL A . n 
A 1 123 THR 123 123 123 THR THR A . n 
A 1 124 ASN 124 124 124 ASN ASN A . n 
A 1 125 PRO 125 125 125 PRO PRO A . n 
A 1 126 LYS 126 126 ?   ?   ?   A . n 
A 1 127 GLU 127 127 ?   ?   ?   A . n 
B 1 1   GLY 1   1   ?   ?   ?   B . n 
B 1 2   PRO 2   2   ?   ?   ?   B . n 
B 1 3   THR 3   3   ?   ?   ?   B . n 
B 1 4   GLY 4   4   ?   ?   ?   B . n 
B 1 5   THR 5   5   ?   ?   ?   B . n 
B 1 6   GLY 6   6   ?   ?   ?   B . n 
B 1 7   GLU 7   7   ?   ?   ?   B . n 
B 1 8   SER 8   8   ?   ?   ?   B . n 
B 1 9   LYS 9   9   ?   ?   ?   B . n 
B 1 10  CYS 10  10  10  CYS CYS B . n 
B 1 11  PRO 11  11  11  PRO PRO B . n 
B 1 12  LEU 12  12  12  LEU LEU B . n 
B 1 13  MET 13  13  13  MET MET B . n 
B 1 14  VAL 14  14  14  VAL VAL B . n 
B 1 15  LYS 15  15  15  LYS LYS B . n 
B 1 16  VAL 16  16  16  VAL VAL B . n 
B 1 17  LEU 17  17  17  LEU LEU B . n 
B 1 18  ASP 18  18  18  ASP ASP B . n 
B 1 19  ALA 19  19  19  ALA ALA B . n 
B 1 20  VAL 20  20  20  VAL VAL B . n 
B 1 21  ARG 21  21  21  ARG ARG B . n 
B 1 22  GLY 22  22  22  GLY GLY B . n 
B 1 23  SER 23  23  23  SER SER B . n 
B 1 24  PRO 24  24  24  PRO PRO B . n 
B 1 25  ALA 25  25  25  ALA ALA B . n 
B 1 26  ILE 26  26  26  ILE ILE B . n 
B 1 27  ASN 27  27  27  ASN ASN B . n 
B 1 28  VAL 28  28  28  VAL VAL B . n 
B 1 29  ALA 29  29  29  ALA ALA B . n 
B 1 30  VAL 30  30  30  VAL VAL B . n 
B 1 31  HIS 31  31  31  HIS HIS B . n 
B 1 32  VAL 32  32  32  VAL VAL B . n 
B 1 33  PHE 33  33  33  PHE PHE B . n 
B 1 34  ARG 34  34  34  ARG ARG B . n 
B 1 35  LYS 35  35  35  LYS LYS B . n 
B 1 36  ALA 36  36  36  ALA ALA B . n 
B 1 37  ALA 37  37  37  ALA ALA B . n 
B 1 38  ASP 38  38  38  ASP ASP B . n 
B 1 39  ASP 39  39  39  ASP ASP B . n 
B 1 40  THR 40  40  40  THR THR B . n 
B 1 41  TRP 41  41  41  TRP TRP B . n 
B 1 42  GLU 42  42  42  GLU GLU B . n 
B 1 43  PRO 43  43  43  PRO PRO B . n 
B 1 44  PHE 44  44  44  PHE PHE B . n 
B 1 45  ALA 45  45  45  ALA ALA B . n 
B 1 46  SER 46  46  46  SER SER B . n 
B 1 47  GLY 47  47  47  GLY GLY B . n 
B 1 48  LYS 48  48  48  LYS LYS B . n 
B 1 49  THR 49  49  49  THR THR B . n 
B 1 50  SER 50  50  50  SER SER B . n 
B 1 51  GLU 51  51  51  GLU GLU B . n 
B 1 52  SER 52  52  52  SER SER B . n 
B 1 53  GLY 53  53  53  GLY GLY B . n 
B 1 54  GLU 54  54  54  GLU GLU B . n 
B 1 55  LEU 55  55  55  LEU LEU B . n 
B 1 56  HIS 56  56  56  HIS HIS B . n 
B 1 57  GLY 57  57  57  GLY GLY B . n 
B 1 58  LEU 58  58  58  LEU LEU B . n 
B 1 59  THR 59  59  59  THR THR B . n 
B 1 60  THR 60  60  60  THR THR B . n 
B 1 61  GLU 61  61  61  GLU GLU B . n 
B 1 62  GLU 62  62  62  GLU GLU B . n 
B 1 63  GLU 63  63  63  GLU GLU B . n 
B 1 64  PHE 64  64  64  PHE PHE B . n 
B 1 65  VAL 65  65  65  VAL VAL B . n 
B 1 66  GLU 66  66  66  GLU GLU B . n 
B 1 67  GLY 67  67  67  GLY GLY B . n 
B 1 68  ILE 68  68  68  ILE ILE B . n 
B 1 69  TYR 69  69  69  TYR TYR B . n 
B 1 70  LYS 70  70  70  LYS LYS B . n 
B 1 71  VAL 71  71  71  VAL VAL B . n 
B 1 72  GLU 72  72  72  GLU GLU B . n 
B 1 73  ILE 73  73  73  ILE ILE B . n 
B 1 74  ASP 74  74  74  ASP ASP B . n 
B 1 75  THR 75  75  75  THR THR B . n 
B 1 76  LYS 76  76  76  LYS LYS B . n 
B 1 77  SER 77  77  77  SER SER B . n 
B 1 78  TYR 78  78  78  TYR TYR B . n 
B 1 79  TRP 79  79  79  TRP TRP B . n 
B 1 80  LYS 80  80  80  LYS LYS B . n 
B 1 81  ALA 81  81  81  ALA ALA B . n 
B 1 82  LEU 82  82  82  LEU LEU B . n 
B 1 83  GLY 83  83  83  GLY GLY B . n 
B 1 84  ILE 84  84  84  ILE ILE B . n 
B 1 85  SER 85  85  85  SER SER B . n 
B 1 86  PRO 86  86  86  PRO PRO B . n 
B 1 87  PHE 87  87  87  PHE PHE B . n 
B 1 88  HIS 88  88  88  HIS HIS B . n 
B 1 89  GLU 89  89  89  GLU GLU B . n 
B 1 90  HIS 90  90  90  HIS HIS B . n 
B 1 91  ALA 91  91  91  ALA ALA B . n 
B 1 92  GLU 92  92  92  GLU GLU B . n 
B 1 93  VAL 93  93  93  VAL VAL B . n 
B 1 94  VAL 94  94  94  VAL VAL B . n 
B 1 95  PHE 95  95  95  PHE PHE B . n 
B 1 96  THR 96  96  96  THR THR B . n 
B 1 97  ALA 97  97  97  ALA ALA B . n 
B 1 98  ASN 98  98  98  ASN ASN B . n 
B 1 99  ASP 99  99  99  ASP ASP B . n 
B 1 100 SER 100 100 100 SER SER B . n 
B 1 101 GLY 101 101 101 GLY GLY B . n 
B 1 102 PRO 102 102 102 PRO PRO B . n 
B 1 103 ARG 103 103 103 ARG ARG B . n 
B 1 104 ARG 104 104 104 ARG ARG B . n 
B 1 105 TYR 105 105 105 TYR TYR B . n 
B 1 106 THR 106 106 106 THR THR B . n 
B 1 107 ILE 107 107 107 ILE ILE B . n 
B 1 108 ALA 108 108 108 ALA ALA B . n 
B 1 109 ALA 109 109 109 ALA ALA B . n 
B 1 110 LEU 110 110 110 LEU LEU B . n 
B 1 111 LEU 111 111 111 LEU LEU B . n 
B 1 112 SER 112 112 112 SER SER B . n 
B 1 113 PRO 113 113 113 PRO PRO B . n 
B 1 114 TYR 114 114 114 TYR TYR B . n 
B 1 115 SER 115 115 115 SER SER B . n 
B 1 116 TYR 116 116 116 TYR TYR B . n 
B 1 117 SER 117 117 117 SER SER B . n 
B 1 118 THR 118 118 118 THR THR B . n 
B 1 119 THR 119 119 119 THR THR B . n 
B 1 120 ALA 120 120 120 ALA ALA B . n 
B 1 121 VAL 121 121 121 VAL VAL B . n 
B 1 122 VAL 122 122 122 VAL VAL B . n 
B 1 123 THR 123 123 123 THR THR B . n 
B 1 124 ASN 124 124 ?   ?   ?   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        A1ISU 
_pdbx_entity_instance_feature.asym_id        ? 
_pdbx_entity_instance_feature.seq_num        ? 
_pdbx_entity_instance_feature.auth_comp_id   A1ISU 
_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 A1ISU 1  201 1   A1ISU DIA B . 
D 3 HOH   1  201 103 HOH   HOH A . 
D 3 HOH   2  202 72  HOH   HOH A . 
D 3 HOH   3  203 36  HOH   HOH A . 
D 3 HOH   4  204 31  HOH   HOH A . 
D 3 HOH   5  205 81  HOH   HOH A . 
D 3 HOH   6  206 9   HOH   HOH A . 
D 3 HOH   7  207 52  HOH   HOH A . 
D 3 HOH   8  208 3   HOH   HOH A . 
D 3 HOH   9  209 13  HOH   HOH A . 
D 3 HOH   10 210 50  HOH   HOH A . 
D 3 HOH   11 211 5   HOH   HOH A . 
D 3 HOH   12 212 4   HOH   HOH A . 
D 3 HOH   13 213 75  HOH   HOH A . 
D 3 HOH   14 214 26  HOH   HOH A . 
D 3 HOH   15 215 58  HOH   HOH A . 
D 3 HOH   16 216 15  HOH   HOH A . 
D 3 HOH   17 217 24  HOH   HOH A . 
D 3 HOH   18 218 69  HOH   HOH A . 
D 3 HOH   19 219 88  HOH   HOH A . 
D 3 HOH   20 220 47  HOH   HOH A . 
D 3 HOH   21 221 22  HOH   HOH A . 
D 3 HOH   22 222 27  HOH   HOH A . 
D 3 HOH   23 223 32  HOH   HOH A . 
D 3 HOH   24 224 39  HOH   HOH A . 
D 3 HOH   25 225 18  HOH   HOH A . 
D 3 HOH   26 226 7   HOH   HOH A . 
D 3 HOH   27 227 100 HOH   HOH A . 
D 3 HOH   28 228 25  HOH   HOH A . 
D 3 HOH   29 229 106 HOH   HOH A . 
D 3 HOH   30 230 54  HOH   HOH A . 
D 3 HOH   31 231 63  HOH   HOH A . 
D 3 HOH   32 232 85  HOH   HOH A . 
D 3 HOH   33 233 2   HOH   HOH A . 
D 3 HOH   34 234 49  HOH   HOH A . 
D 3 HOH   35 235 41  HOH   HOH A . 
D 3 HOH   36 236 42  HOH   HOH A . 
D 3 HOH   37 237 70  HOH   HOH A . 
D 3 HOH   38 238 21  HOH   HOH A . 
D 3 HOH   39 239 16  HOH   HOH A . 
D 3 HOH   40 240 19  HOH   HOH A . 
D 3 HOH   41 241 46  HOH   HOH A . 
D 3 HOH   42 242 23  HOH   HOH A . 
D 3 HOH   43 243 34  HOH   HOH A . 
D 3 HOH   44 244 65  HOH   HOH A . 
D 3 HOH   45 245 82  HOH   HOH A . 
D 3 HOH   46 246 20  HOH   HOH A . 
D 3 HOH   47 247 86  HOH   HOH A . 
D 3 HOH   48 248 95  HOH   HOH A . 
D 3 HOH   49 249 87  HOH   HOH A . 
D 3 HOH   50 250 62  HOH   HOH A . 
D 3 HOH   51 251 48  HOH   HOH A . 
D 3 HOH   52 252 104 HOH   HOH A . 
D 3 HOH   53 253 99  HOH   HOH A . 
D 3 HOH   54 254 94  HOH   HOH A . 
D 3 HOH   55 255 67  HOH   HOH A . 
D 3 HOH   56 256 78  HOH   HOH A . 
D 3 HOH   57 257 77  HOH   HOH A . 
D 3 HOH   58 258 79  HOH   HOH A . 
D 3 HOH   59 259 80  HOH   HOH A . 
E 3 HOH   1  301 96  HOH   HOH B . 
E 3 HOH   2  302 64  HOH   HOH B . 
E 3 HOH   3  303 61  HOH   HOH B . 
E 3 HOH   4  304 12  HOH   HOH B . 
E 3 HOH   5  305 14  HOH   HOH B . 
E 3 HOH   6  306 74  HOH   HOH B . 
E 3 HOH   7  307 73  HOH   HOH B . 
E 3 HOH   8  308 105 HOH   HOH B . 
E 3 HOH   9  309 10  HOH   HOH B . 
E 3 HOH   10 310 40  HOH   HOH B . 
E 3 HOH   11 311 44  HOH   HOH B . 
E 3 HOH   12 312 83  HOH   HOH B . 
E 3 HOH   13 313 107 HOH   HOH B . 
E 3 HOH   14 314 45  HOH   HOH B . 
E 3 HOH   15 315 55  HOH   HOH B . 
E 3 HOH   16 316 51  HOH   HOH B . 
E 3 HOH   17 317 11  HOH   HOH B . 
E 3 HOH   18 318 30  HOH   HOH B . 
E 3 HOH   19 319 6   HOH   HOH B . 
E 3 HOH   20 320 8   HOH   HOH B . 
E 3 HOH   21 321 35  HOH   HOH B . 
E 3 HOH   22 322 1   HOH   HOH B . 
E 3 HOH   23 323 56  HOH   HOH B . 
E 3 HOH   24 324 53  HOH   HOH B . 
E 3 HOH   25 325 17  HOH   HOH B . 
E 3 HOH   26 326 38  HOH   HOH B . 
E 3 HOH   27 327 37  HOH   HOH B . 
E 3 HOH   28 328 29  HOH   HOH B . 
E 3 HOH   29 329 68  HOH   HOH B . 
E 3 HOH   30 330 33  HOH   HOH B . 
E 3 HOH   31 331 28  HOH   HOH B . 
E 3 HOH   32 332 57  HOH   HOH B . 
E 3 HOH   33 333 66  HOH   HOH B . 
E 3 HOH   34 334 89  HOH   HOH B . 
E 3 HOH   35 335 60  HOH   HOH B . 
E 3 HOH   36 336 101 HOH   HOH B . 
E 3 HOH   37 337 43  HOH   HOH B . 
E 3 HOH   38 338 71  HOH   HOH B . 
E 3 HOH   39 339 84  HOH   HOH B . 
E 3 HOH   40 340 59  HOH   HOH B . 
E 3 HOH   41 341 97  HOH   HOH B . 
E 3 HOH   42 342 98  HOH   HOH B . 
E 3 HOH   43 343 76  HOH   HOH B . 
E 3 HOH   44 344 92  HOH   HOH B . 
E 3 HOH   45 345 91  HOH   HOH B . 
E 3 HOH   46 346 93  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  ? CA  ? A CYS 10  CA  
3  1 Y 1 A CYS 10  ? CB  ? A CYS 10  CB  
4  1 Y 1 A CYS 10  ? SG  ? A CYS 10  SG  
5  1 Y 1 A ARG 21  ? CG  ? A ARG 21  CG  
6  1 Y 1 A ARG 21  ? CD  ? A ARG 21  CD  
7  1 Y 1 A ARG 21  ? NE  ? A ARG 21  NE  
8  1 Y 1 A ARG 21  ? CZ  ? A ARG 21  CZ  
9  1 Y 1 A ARG 21  ? NH1 ? A ARG 21  NH1 
10 1 Y 1 A ARG 21  ? NH2 ? A ARG 21  NH2 
11 1 Y 1 A ALA 36  ? CB  ? A ALA 36  CB  
12 1 Y 1 A ALA 37  ? CB  ? A ALA 37  CB  
13 1 Y 1 A ASP 38  ? CG  ? A ASP 38  CG  
14 1 Y 1 A ASP 38  ? OD1 ? A ASP 38  OD1 
15 1 Y 1 A ASP 38  ? OD2 ? A ASP 38  OD2 
16 1 Y 1 A ASP 39  ? O   ? A ASP 39  O   
17 1 Y 1 A ASP 39  ? CB  ? A ASP 39  CB  
18 1 Y 1 A ASP 39  ? CG  ? A ASP 39  CG  
19 1 Y 1 A ASP 39  ? OD1 ? A ASP 39  OD1 
20 1 Y 1 A ASP 39  ? OD2 ? A ASP 39  OD2 
21 1 Y 1 A GLU 42  ? CG  ? A GLU 42  CG  
22 1 Y 1 A GLU 42  ? CD  ? A GLU 42  CD  
23 1 Y 1 A GLU 42  ? OE1 ? A GLU 42  OE1 
24 1 Y 1 A GLU 42  ? OE2 ? A GLU 42  OE2 
25 1 Y 1 A LYS 48  ? CD  ? A LYS 48  CD  
26 1 Y 1 A LYS 48  ? CE  ? A LYS 48  CE  
27 1 Y 1 A LYS 48  ? NZ  ? A LYS 48  NZ  
28 1 Y 1 A GLU 51  ? CG  ? A GLU 51  CG  
29 1 Y 1 A GLU 51  ? CD  ? A GLU 51  CD  
30 1 Y 1 A GLU 51  ? OE1 ? A GLU 51  OE1 
31 1 Y 1 A GLU 51  ? OE2 ? A GLU 51  OE2 
32 1 Y 1 A GLU 61  ? CG  ? A GLU 61  CG  
33 1 Y 1 A GLU 61  ? CD  ? A GLU 61  CD  
34 1 Y 1 A GLU 61  ? OE1 ? A GLU 61  OE1 
35 1 Y 1 A GLU 61  ? OE2 ? A GLU 61  OE2 
36 1 Y 1 A GLU 63  ? CG  ? A GLU 63  CG  
37 1 Y 1 A GLU 63  ? CD  ? A GLU 63  CD  
38 1 Y 1 A GLU 63  ? OE1 ? A GLU 63  OE1 
39 1 Y 1 A GLU 63  ? OE2 ? A GLU 63  OE2 
40 1 Y 1 A GLU 92  ? CG  ? A GLU 92  CG  
41 1 Y 1 A GLU 92  ? CD  ? A GLU 92  CD  
42 1 Y 1 A GLU 92  ? OE1 ? A GLU 92  OE1 
43 1 Y 1 A GLU 92  ? OE2 ? A GLU 92  OE2 
44 1 Y 1 A ASP 99  ? CG  ? A ASP 99  CG  
45 1 Y 1 A ASP 99  ? OD1 ? A ASP 99  OD1 
46 1 Y 1 A ASP 99  ? OD2 ? A ASP 99  OD2 
47 1 Y 1 A ARG 104 ? NE  ? A ARG 104 NE  
48 1 Y 1 A ARG 104 ? CZ  ? A ARG 104 CZ  
49 1 Y 1 A ARG 104 ? NH1 ? A ARG 104 NH1 
50 1 Y 1 A ARG 104 ? NH2 ? A ARG 104 NH2 
51 1 Y 1 B CYS 10  ? N   ? B CYS 10  N   
52 1 Y 1 B CYS 10  ? CA  ? B CYS 10  CA  
53 1 Y 1 B CYS 10  ? CB  ? B CYS 10  CB  
54 1 Y 1 B CYS 10  ? SG  ? B CYS 10  SG  
55 1 Y 1 B ARG 21  ? NH1 ? B ARG 21  NH1 
56 1 Y 1 B ARG 21  ? NH2 ? B ARG 21  NH2 
57 1 Y 1 B ARG 34  ? CG  ? B ARG 34  CG  
58 1 Y 1 B ARG 34  ? CD  ? B ARG 34  CD  
59 1 Y 1 B ARG 34  ? NE  ? B ARG 34  NE  
60 1 Y 1 B ARG 34  ? CZ  ? B ARG 34  CZ  
61 1 Y 1 B ARG 34  ? NH1 ? B ARG 34  NH1 
62 1 Y 1 B ARG 34  ? NH2 ? B ARG 34  NH2 
63 1 Y 1 B LYS 48  ? CE  ? B LYS 48  CE  
64 1 Y 1 B LYS 48  ? NZ  ? B LYS 48  NZ  
65 1 Y 1 B GLU 51  ? CG  ? B GLU 51  CG  
66 1 Y 1 B GLU 51  ? CD  ? B GLU 51  CD  
67 1 Y 1 B GLU 51  ? OE1 ? B GLU 51  OE1 
68 1 Y 1 B GLU 51  ? OE2 ? B GLU 51  OE2 
69 1 Y 1 B GLU 61  ? CG  ? B GLU 61  CG  
70 1 Y 1 B GLU 61  ? CD  ? B GLU 61  CD  
71 1 Y 1 B GLU 61  ? OE1 ? B GLU 61  OE1 
72 1 Y 1 B GLU 61  ? OE2 ? B GLU 61  OE2 
73 1 Y 1 B GLU 62  ? CB  ? B GLU 62  CB  
74 1 Y 1 B GLU 62  ? CG  ? B GLU 62  CG  
75 1 Y 1 B GLU 62  ? CD  ? B GLU 62  CD  
76 1 Y 1 B GLU 62  ? OE1 ? B GLU 62  OE1 
77 1 Y 1 B GLU 62  ? OE2 ? B GLU 62  OE2 
78 1 Y 1 B GLU 63  ? CG  ? B GLU 63  CG  
79 1 Y 1 B GLU 63  ? CD  ? B GLU 63  CD  
80 1 Y 1 B GLU 63  ? OE1 ? B GLU 63  OE1 
81 1 Y 1 B GLU 63  ? OE2 ? B GLU 63  OE2 
82 1 Y 1 B GLU 66  ? OE2 ? B GLU 66  OE2 
83 1 Y 1 B GLU 92  ? CG  ? B GLU 92  CG  
84 1 Y 1 B GLU 92  ? CD  ? B GLU 92  CD  
85 1 Y 1 B GLU 92  ? OE1 ? B GLU 92  OE1 
86 1 Y 1 B GLU 92  ? OE2 ? B GLU 92  OE2 
87 1 Y 1 B ASP 99  ? CG  ? B ASP 99  CG  
88 1 Y 1 B ASP 99  ? OD1 ? B ASP 99  OD1 
89 1 Y 1 B ASP 99  ? OD2 ? B ASP 99  OD2 
90 1 Y 1 B SER 100 ? O   ? B SER 100 O   
91 1 Y 1 B ARG 104 ? CG  ? B ARG 104 CG  
92 1 Y 1 B ARG 104 ? CD  ? B ARG 104 CD  
93 1 Y 1 B ARG 104 ? NE  ? B ARG 104 NE  
94 1 Y 1 B ARG 104 ? CZ  ? B ARG 104 CZ  
95 1 Y 1 B ARG 104 ? NH1 ? B ARG 104 NH1 
96 1 Y 1 B ARG 104 ? NH2 ? B ARG 104 NH2 
# 
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   ? ? ? .        2 
? 'data scaling'   ? ? ? ? ? ? ? ? ? ? ? xia2   ? ? ? .        3 
? phasing          ? ? ? ? ? ? ? ? ? ? ? PHASER ? ? ? .        4 
# 
_cell.angle_alpha                  90.00 
_cell.angle_alpha_esd              ? 
_cell.angle_beta                   90.00 
_cell.angle_beta_esd               ? 
_cell.angle_gamma                  90.00 
_cell.angle_gamma_esd              ? 
_cell.entry_id                     9H7F 
_cell.details                      ? 
_cell.formula_units_Z              ? 
_cell.length_a                     85.110 
_cell.length_a_esd                 ? 
_cell.length_b                     43.800 
_cell.length_b_esd                 ? 
_cell.length_c                     64.760 
_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                         9H7F 
_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                   9H7F 
_exptl.crystals_number            1 
_exptl.details                    ? 
_exptl.method                     'X-RAY DIFFRACTION' 
_exptl.method_details             ? 
# 
_exptl_crystal.colour                       ? 
_exptl_crystal.density_diffrn               ? 
_exptl_crystal.density_Matthews             2.19 
_exptl_crystal.density_method               ? 
_exptl_crystal.density_percent_sol          43.84 
_exptl_crystal.description                  ? 
_exptl_crystal.F_000                        ? 
_exptl_crystal.id                           1 
_exptl_crystal.preparation                  ? 
_exptl_crystal.size_max                     ? 
_exptl_crystal.size_mid                     ? 
_exptl_crystal.size_min                     ? 
_exptl_crystal.size_rad                     ? 
_exptl_crystal.colour_lustre                ? 
_exptl_crystal.colour_modifier              ? 
_exptl_crystal.colour_primary               ? 
_exptl_crystal.density_meas                 ? 
_exptl_crystal.density_meas_esd             ? 
_exptl_crystal.density_meas_gt              ? 
_exptl_crystal.density_meas_lt              ? 
_exptl_crystal.density_meas_temp            ? 
_exptl_crystal.density_meas_temp_esd        ? 
_exptl_crystal.density_meas_temp_gt         ? 
_exptl_crystal.density_meas_temp_lt         ? 
_exptl_crystal.pdbx_crystal_image_url       ? 
_exptl_crystal.pdbx_crystal_image_format    ? 
_exptl_crystal.pdbx_mosaicity               ? 
_exptl_crystal.pdbx_mosaicity_esd           ? 
_exptl_crystal.pdbx_mosaic_method           ? 
_exptl_crystal.pdbx_mosaic_block_size       ? 
_exptl_crystal.pdbx_mosaic_block_size_esd   ? 
# 
_exptl_crystal_grow.apparatus       ? 
_exptl_crystal_grow.atmosphere      ? 
_exptl_crystal_grow.crystal_id      1 
_exptl_crystal_grow.details         ? 
_exptl_crystal_grow.method          'VAPOR DIFFUSION, HANGING DROP' 
_exptl_crystal_grow.method_ref      ? 
_exptl_crystal_grow.pH              7.5 
_exptl_crystal_grow.pressure        ? 
_exptl_crystal_grow.pressure_esd    ? 
_exptl_crystal_grow.seeding         ? 
_exptl_crystal_grow.seeding_ref     ? 
_exptl_crystal_grow.temp_details    ? 
_exptl_crystal_grow.temp_esd        ? 
_exptl_crystal_grow.time            ? 
_exptl_crystal_grow.pdbx_details    '100 mM HEPES, 200 mM CaCl2, 28% v/v PEG400, pH 7.5' 
_exptl_crystal_grow.pdbx_pH_range   ? 
_exptl_crystal_grow.temp            294.15 
# 
_diffrn.ambient_environment              ? 
_diffrn.ambient_temp                     100 
_diffrn.ambient_temp_details             ? 
_diffrn.ambient_temp_esd                 ? 
_diffrn.crystal_id                       1 
_diffrn.crystal_support                  ? 
_diffrn.crystal_treatment                ? 
_diffrn.details                          ? 
_diffrn.id                               1 
_diffrn.ambient_pressure                 ? 
_diffrn.ambient_pressure_esd             ? 
_diffrn.ambient_pressure_gt              ? 
_diffrn.ambient_pressure_lt              ? 
_diffrn.ambient_temp_gt                  ? 
_diffrn.ambient_temp_lt                  ? 
_diffrn.pdbx_serial_crystal_experiment   N 
# 
_diffrn_detector.details                      ? 
_diffrn_detector.detector                     PIXEL 
_diffrn_detector.diffrn_id                    1 
_diffrn_detector.type                         'DECTRIS PILATUS 6M' 
_diffrn_detector.area_resol_mean              ? 
_diffrn_detector.dtime                        ? 
_diffrn_detector.pdbx_frames_total            ? 
_diffrn_detector.pdbx_collection_time_total   ? 
_diffrn_detector.pdbx_collection_date         2011-10-30 
_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   0.97780 
_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 I24' 
_diffrn_source.voltage                     ? 
_diffrn_source.take-off_angle              ? 
_diffrn_source.pdbx_wavelength_list        0.97780 
_diffrn_source.pdbx_wavelength             ? 
_diffrn_source.pdbx_synchrotron_beamline   I24 
_diffrn_source.pdbx_synchrotron_site       Diamond 
# 
_reflns.B_iso_Wilson_estimate                          ? 
_reflns.entry_id                                       9H7F 
_reflns.data_reduction_details                         ? 
_reflns.data_reduction_method                          ? 
_reflns.d_resolution_high                              1.23 
_reflns.d_resolution_low                               64.76 
_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                                     71035 
_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                           99.91 
_reflns.R_free_details                                 ? 
_reflns.Rmerge_F_all                                   ? 
_reflns.Rmerge_F_obs                                   ? 
_reflns.Friedel_coverage                               ? 
_reflns.number_gt                                      ? 
_reflns.threshold_expression                           ? 
_reflns.pdbx_redundancy                                12.7 
_reflns.pdbx_netI_over_av_sigmaI                       ? 
_reflns.pdbx_netI_over_sigmaI                          16.1 
_reflns.pdbx_res_netI_over_av_sigmaI_2                 ? 
_reflns.pdbx_res_netI_over_sigmaI_2                    ? 
_reflns.pdbx_chi_squared                               ? 
_reflns.pdbx_scaling_rejects                           ? 
_reflns.pdbx_d_res_high_opt                            ? 
_reflns.pdbx_d_res_low_opt                             ? 
_reflns.pdbx_d_res_opt_method                          ? 
_reflns.phase_calculation_details                      ? 
_reflns.pdbx_Rrim_I_all                                ? 
_reflns.pdbx_Rpim_I_all                                0.033 
_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                              0.079 
_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                                    1.24 
_reflns_shell.d_res_low                                     1.272 
_reflns_shell.meanI_over_sigI_all                           ? 
_reflns_shell.meanI_over_sigI_obs                           ? 
_reflns_shell.number_measured_all                           ? 
_reflns_shell.number_measured_obs                           ? 
_reflns_shell.number_possible                               ? 
_reflns_shell.number_unique_all                             ? 
_reflns_shell.number_unique_obs                             4512 
_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                               0.344 
_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                                  0.777 
_reflns_shell.pdbx_Rsym_value                               ? 
_reflns_shell.pdbx_percent_possible_ellipsoidal             ? 
_reflns_shell.pdbx_percent_possible_spherical               ? 
_reflns_shell.pdbx_percent_possible_ellipsoidal_anomalous   ? 
_reflns_shell.pdbx_percent_possible_spherical_anomalous     ? 
_reflns_shell.pdbx_redundancy_anomalous                     ? 
_reflns_shell.pdbx_CC_half_anomalous                        ? 
_reflns_shell.pdbx_absDiff_over_sigma_anomalous             ? 
_reflns_shell.pdbx_percent_possible_anomalous               ? 
# 
_refine.aniso_B[1][1]                            0.08 
_refine.aniso_B[1][2]                            0.00 
_refine.aniso_B[1][3]                            -0.00 
_refine.aniso_B[2][2]                            0.13 
_refine.aniso_B[2][3]                            -0.00 
_refine.aniso_B[3][3]                            -0.21 
_refine.B_iso_max                                ? 
_refine.B_iso_mean                               16.616 
_refine.B_iso_min                                ? 
_refine.correlation_coeff_Fo_to_Fc               0.973 
_refine.correlation_coeff_Fo_to_Fc_free          0.971 
_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                                 9H7F 
_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                            1.24 
_refine.ls_d_res_low                             30.26 
_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                     65798 
_refine.ls_number_reflns_R_free                  3507 
_refine.ls_number_reflns_R_work                  ? 
_refine.ls_number_restraints                     ? 
_refine.ls_percent_reflns_obs                    99.91 
_refine.ls_percent_reflns_R_free                 5.1 
_refine.ls_R_factor_all                          ? 
_refine.ls_R_factor_obs                          0.15652 
_refine.ls_R_factor_R_free                       0.17765 
_refine.ls_R_factor_R_free_error                 ? 
_refine.ls_R_factor_R_free_error_details         ? 
_refine.ls_R_factor_R_work                       0.15540 
_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                    'BABINET MODEL WITH 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                       0.038 
_refine.pdbx_overall_ESU_R_Free                  0.038 
_refine.pdbx_solvent_vdw_probe_radii             1.20 
_refine.pdbx_solvent_ion_probe_radii             0.80 
_refine.pdbx_solvent_shrinkage_radii             0.80 
_refine.pdbx_real_space_R                        ? 
_refine.pdbx_density_correlation                 ? 
_refine.pdbx_pd_number_of_powder_patterns        ? 
_refine.pdbx_pd_number_of_points                 ? 
_refine.pdbx_pd_meas_number_of_points            ? 
_refine.pdbx_pd_proc_ls_prof_R_factor            ? 
_refine.pdbx_pd_proc_ls_prof_wR_factor           ? 
_refine.pdbx_pd_Marquardt_correlation_coeff      ? 
_refine.pdbx_pd_Fsqrd_R_factor                   ? 
_refine.pdbx_pd_ls_matrix_band_width             ? 
_refine.pdbx_overall_phase_error                 ? 
_refine.pdbx_overall_SU_R_free_Cruickshank_DPI   ? 
_refine.pdbx_overall_SU_R_free_Blow_DPI          ? 
_refine.pdbx_overall_SU_R_Blow_DPI               ? 
_refine.pdbx_TLS_residual_ADP_flag               ? 
_refine.pdbx_diffrn_id                           1 
_refine.overall_SU_B                             1.133 
_refine.overall_SU_ML                            0.023 
_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                       1.24 
_refine_hist.d_res_low                        30.26 
_refine_hist.number_atoms_solvent             105 
_refine_hist.number_atoms_total               1795 
_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        1681 
_refine_hist.pdbx_number_atoms_nucleic_acid   0 
_refine_hist.pdbx_number_atoms_ligand         9 
_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' ? 0.023  0.020  1828 ? r_bond_refined_d             ? ? 
'X-RAY DIFFRACTION' ? 0.001  0.020  1186 ? r_bond_other_d               ? ? 
'X-RAY DIFFRACTION' ? 2.072  1.945  2514 ? r_angle_refined_deg          ? ? 
'X-RAY DIFFRACTION' ? 1.438  3.000  2909 ? r_angle_other_deg            ? ? 
'X-RAY DIFFRACTION' ? 6.772  5.000  251  ? r_dihedral_angle_1_deg       ? ? 
'X-RAY DIFFRACTION' ? 25.351 22.623 61   ? r_dihedral_angle_2_deg       ? ? 
'X-RAY DIFFRACTION' ? 12.777 15.000 269  ? r_dihedral_angle_3_deg       ? ? 
'X-RAY DIFFRACTION' ? 15.695 15.000 7    ? r_dihedral_angle_4_deg       ? ? 
'X-RAY DIFFRACTION' ? 0.127  0.200  293  ? r_chiral_restr               ? ? 
'X-RAY DIFFRACTION' ? 0.012  0.021  2058 ? r_gen_planes_refined         ? ? 
'X-RAY DIFFRACTION' ? 0.005  0.020  394  ? 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' ? 8.005  3.000  3012 ? r_rigid_bond_restr           ? ? 
'X-RAY DIFFRACTION' ? 25.935 5.000  35   ? r_sphericity_free            ? ? 
'X-RAY DIFFRACTION' ? 13.650 5.000  3021 ? r_sphericity_bonded          ? ? 
# 
_refine_ls_shell.pdbx_refine_id                   'X-RAY DIFFRACTION' 
_refine_ls_shell.d_res_high                       1.240 
_refine_ls_shell.d_res_low                        1.272 
_refine_ls_shell.number_reflns_all                ? 
_refine_ls_shell.number_reflns_obs                ? 
_refine_ls_shell.number_reflns_R_free             235 
_refine_ls_shell.number_reflns_R_work             4512 
_refine_ls_shell.percent_reflns_obs               99.92 
_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                  0.164 
_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                  0.202 
# 
_struct.entry_id                     9H7F 
_struct.title                        'Human Transthyretin in Complex with 3,5-dichloroaniline' 
_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        9H7F 
_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 ? 
# 
_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 9H7F A 1 ? 127 ? P02766 21 ? 147 ? 1 127 
2 1 9H7F B 1 ? 127 ? P02766 21 ? 147 ? 1 127 
# 
_pdbx_struct_assembly.id                   1 
_pdbx_struct_assembly.details              author_and_software_defined_assembly 
_pdbx_struct_assembly.method_details       PISA 
_pdbx_struct_assembly.oligomeric_details   tetrameric 
_pdbx_struct_assembly.oligomeric_count     4 
# 
loop_
_pdbx_struct_assembly_prop.biol_id 
_pdbx_struct_assembly_prop.type 
_pdbx_struct_assembly_prop.value 
_pdbx_struct_assembly_prop.details 
1 'ABSA (A^2)' 6800  ? 
1 MORE         -43   ? 
1 'SSA (A^2)'  18270 ? 
# 
_pdbx_struct_assembly_gen.assembly_id       1 
_pdbx_struct_assembly_gen.oper_expression   1,2 
_pdbx_struct_assembly_gen.asym_id_list      A,B,C,D,E 
# 
_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_555 -x,-y,z -1.0000000000 0.0000000000 0.0000000000 0.0000000000 0.0000000000 -1.0000000000 
0.0000000000 0.0000000000 0.0000000000 0.0000000000 1.0000000000 0.0000000000 
# 
loop_
_struct_conf.conf_type_id 
_struct_conf.id 
_struct_conf.pdbx_PDB_helix_id 
_struct_conf.beg_label_comp_id 
_struct_conf.beg_label_asym_id 
_struct_conf.beg_label_seq_id 
_struct_conf.pdbx_beg_PDB_ins_code 
_struct_conf.end_label_comp_id 
_struct_conf.end_label_asym_id 
_struct_conf.end_label_seq_id 
_struct_conf.pdbx_end_PDB_ins_code 
_struct_conf.beg_auth_comp_id 
_struct_conf.beg_auth_asym_id 
_struct_conf.beg_auth_seq_id 
_struct_conf.end_auth_comp_id 
_struct_conf.end_auth_asym_id 
_struct_conf.end_auth_seq_id 
_struct_conf.pdbx_PDB_helix_class 
_struct_conf.details 
_struct_conf.pdbx_PDB_helix_length 
HELX_P HELX_P1 AA1 ASP A 74 ? 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_sheet.id 
_struct_sheet.type 
_struct_sheet.number_strands 
_struct_sheet.details 
AA1 ? 8 ? 
AA2 ? 8 ? 
AA3 ? 4 ? 
AA4 ? 4 ? 
# 
loop_
_struct_sheet_order.sheet_id 
_struct_sheet_order.range_id_1 
_struct_sheet_order.range_id_2 
_struct_sheet_order.offset 
_struct_sheet_order.sense 
AA1 1 2 ? anti-parallel 
AA1 2 3 ? parallel      
AA1 3 4 ? anti-parallel 
AA1 4 5 ? anti-parallel 
AA1 5 6 ? anti-parallel 
AA1 6 7 ? parallel      
AA1 7 8 ? anti-parallel 
AA2 1 2 ? anti-parallel 
AA2 2 3 ? parallel      
AA2 3 4 ? anti-parallel 
AA2 4 5 ? anti-parallel 
AA2 5 6 ? anti-parallel 
AA2 6 7 ? parallel      
AA2 7 8 ? anti-parallel 
AA3 1 2 ? anti-parallel 
AA3 2 3 ? anti-parallel 
AA3 3 4 ? anti-parallel 
AA4 1 2 ? anti-parallel 
AA4 2 3 ? anti-parallel 
AA4 3 4 ? anti-parallel 
# 
loop_
_struct_sheet_range.sheet_id 
_struct_sheet_range.id 
_struct_sheet_range.beg_label_comp_id 
_struct_sheet_range.beg_label_asym_id 
_struct_sheet_range.beg_label_seq_id 
_struct_sheet_range.pdbx_beg_PDB_ins_code 
_struct_sheet_range.end_label_comp_id 
_struct_sheet_range.end_label_asym_id 
_struct_sheet_range.end_label_seq_id 
_struct_sheet_range.pdbx_end_PDB_ins_code 
_struct_sheet_range.beg_auth_comp_id 
_struct_sheet_range.beg_auth_asym_id 
_struct_sheet_range.beg_auth_seq_id 
_struct_sheet_range.end_auth_comp_id 
_struct_sheet_range.end_auth_asym_id 
_struct_sheet_range.end_auth_seq_id 
AA1 1 SER A 23  ? PRO A 24  ? SER A 23  PRO A 24  
AA1 2 LEU A 12  ? ASP A 18  ? LEU A 12  ASP A 18  
AA1 3 ARG A 104 ? SER A 112 ? ARG A 104 SER A 112 
AA1 4 SER A 115 ? THR A 123 ? SER A 115 THR A 123 
AA1 5 SER B 115 ? THR B 123 ? SER B 115 THR B 123 
AA1 6 ARG B 104 ? SER B 112 ? ARG B 104 SER B 112 
AA1 7 LEU B 12  ? ASP B 18  ? LEU B 12  ASP B 18  
AA1 8 SER B 23  ? PRO B 24  ? SER B 23  PRO B 24  
AA2 1 GLU A 54  ? LEU A 55  ? GLU A 54  LEU A 55  
AA2 2 LEU A 12  ? ASP A 18  ? LEU A 12  ASP A 18  
AA2 3 ARG A 104 ? SER A 112 ? ARG A 104 SER A 112 
AA2 4 SER A 115 ? THR A 123 ? SER A 115 THR A 123 
AA2 5 SER B 115 ? THR B 123 ? SER B 115 THR B 123 
AA2 6 ARG B 104 ? SER B 112 ? ARG B 104 SER B 112 
AA2 7 LEU B 12  ? ASP B 18  ? LEU B 12  ASP B 18  
AA2 8 GLU B 54  ? LEU B 55  ? GLU B 54  LEU B 55  
AA3 1 TRP A 41  ? LYS A 48  ? TRP A 41  LYS A 48  
AA3 2 ALA A 29  ? LYS A 35  ? ALA A 29  LYS A 35  
AA3 3 GLY A 67  ? ILE A 73  ? GLY A 67  ILE A 73  
AA3 4 ALA A 91  ? ALA A 97  ? ALA A 91  ALA A 97  
AA4 1 TRP B 41  ? LYS B 48  ? TRP B 41  LYS B 48  
AA4 2 ALA B 29  ? LYS B 35  ? ALA B 29  LYS B 35  
AA4 3 GLY B 67  ? ILE B 73  ? GLY B 67  ILE B 73  
AA4 4 ALA B 91  ? ALA B 97  ? ALA B 91  ALA B 97  
# 
loop_
_pdbx_struct_sheet_hbond.sheet_id 
_pdbx_struct_sheet_hbond.range_id_1 
_pdbx_struct_sheet_hbond.range_id_2 
_pdbx_struct_sheet_hbond.range_1_label_atom_id 
_pdbx_struct_sheet_hbond.range_1_label_comp_id 
_pdbx_struct_sheet_hbond.range_1_label_asym_id 
_pdbx_struct_sheet_hbond.range_1_label_seq_id 
_pdbx_struct_sheet_hbond.range_1_PDB_ins_code 
_pdbx_struct_sheet_hbond.range_1_auth_atom_id 
_pdbx_struct_sheet_hbond.range_1_auth_comp_id 
_pdbx_struct_sheet_hbond.range_1_auth_asym_id 
_pdbx_struct_sheet_hbond.range_1_auth_seq_id 
_pdbx_struct_sheet_hbond.range_2_label_atom_id 
_pdbx_struct_sheet_hbond.range_2_label_comp_id 
_pdbx_struct_sheet_hbond.range_2_label_asym_id 
_pdbx_struct_sheet_hbond.range_2_label_seq_id 
_pdbx_struct_sheet_hbond.range_2_PDB_ins_code 
_pdbx_struct_sheet_hbond.range_2_auth_atom_id 
_pdbx_struct_sheet_hbond.range_2_auth_comp_id 
_pdbx_struct_sheet_hbond.range_2_auth_asym_id 
_pdbx_struct_sheet_hbond.range_2_auth_seq_id 
AA1 1 2 O SER A 23  ? O SER A 23  N ASP A 18  ? N ASP A 18  
AA1 2 3 N LEU A 17  ? N LEU A 17  O LEU A 111 ? O LEU A 111 
AA1 3 4 N ALA A 108 ? N ALA A 108 O THR A 119 ? O THR A 119 
AA1 4 5 N TYR A 116 ? N TYR A 116 O THR B 118 ? O THR B 118 
AA1 5 6 O SER B 115 ? O SER B 115 N SER B 112 ? N SER B 112 
AA1 6 7 O LEU B 111 ? O LEU B 111 N LEU B 17  ? N LEU B 17  
AA1 7 8 N ASP B 18  ? N ASP B 18  O SER B 23  ? O SER B 23  
AA2 1 2 O LEU A 55  ? O LEU A 55  N VAL A 14  ? N VAL A 14  
AA2 2 3 N LEU A 17  ? N LEU A 17  O LEU A 111 ? O LEU A 111 
AA2 3 4 N ALA A 108 ? N ALA A 108 O THR A 119 ? O THR A 119 
AA2 4 5 N TYR A 116 ? N TYR A 116 O THR B 118 ? O THR B 118 
AA2 5 6 O SER B 115 ? O SER B 115 N SER B 112 ? N SER B 112 
AA2 6 7 O LEU B 111 ? O LEU B 111 N LEU B 17  ? N LEU B 17  
AA2 7 8 N VAL B 14  ? N VAL B 14  O LEU B 55  ? O LEU B 55  
AA3 1 2 O ALA A 45  ? O ALA A 45  N VAL A 32  ? N VAL A 32  
AA3 2 3 N HIS A 31  ? N HIS A 31  O GLU A 72  ? O GLU A 72  
AA3 3 4 N ILE A 73  ? N ILE A 73  O ALA A 91  ? O ALA A 91  
AA4 1 2 O ALA B 45  ? O ALA B 45  N VAL B 32  ? N VAL B 32  
AA4 2 3 N HIS B 31  ? N HIS B 31  O GLU B 72  ? O GLU B 72  
AA4 3 4 N ILE B 73  ? N ILE B 73  O ALA B 91  ? O ALA B 91  
# 
_pdbx_entry_details.entry_id                   9H7F 
_pdbx_entry_details.nonpolymer_details         ? 
_pdbx_entry_details.sequence_details           ? 
_pdbx_entry_details.compound_details           ? 
_pdbx_entry_details.source_details             ? 
_pdbx_entry_details.has_ligand_of_interest     Y 
_pdbx_entry_details.has_protein_modification   N 
# 
_pdbx_validate_torsion.id              1 
_pdbx_validate_torsion.PDB_model_num   1 
_pdbx_validate_torsion.auth_comp_id    ASP 
_pdbx_validate_torsion.auth_asym_id    A 
_pdbx_validate_torsion.auth_seq_id     39 
_pdbx_validate_torsion.PDB_ins_code    ? 
_pdbx_validate_torsion.label_alt_id    ? 
_pdbx_validate_torsion.phi             83.27 
_pdbx_validate_torsion.psi             -14.45 
# 
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 B A1ISU 201 ? C A1ISU . 
2 1 B A1ISU 201 ? C A1ISU . 
3 1 B A1ISU 201 ? C A1ISU . 
4 1 B HOH   303 ? E HOH   . 
# 
loop_
_pdbx_distant_solvent_atoms.id 
_pdbx_distant_solvent_atoms.PDB_model_num 
_pdbx_distant_solvent_atoms.auth_atom_id 
_pdbx_distant_solvent_atoms.label_alt_id 
_pdbx_distant_solvent_atoms.auth_asym_id 
_pdbx_distant_solvent_atoms.auth_comp_id 
_pdbx_distant_solvent_atoms.auth_seq_id 
_pdbx_distant_solvent_atoms.PDB_ins_code 
_pdbx_distant_solvent_atoms.neighbor_macromolecule_distance 
_pdbx_distant_solvent_atoms.neighbor_ligand_distance 
1 1 O ? A HOH 258 ? 5.82  . 
2 1 O ? A HOH 259 ? 6.80  . 
3 1 O ? B HOH 344 ? 9.47  . 
4 1 O ? B HOH 345 ? 9.67  . 
5 1 O ? B HOH 346 ? 13.00 . 
# 
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 LYS 126 ? A LYS 126 
11 1 Y 1 A GLU 127 ? A GLU 127 
12 1 Y 1 B GLY 1   ? B GLY 1   
13 1 Y 1 B PRO 2   ? B PRO 2   
14 1 Y 1 B THR 3   ? B THR 3   
15 1 Y 1 B GLY 4   ? B GLY 4   
16 1 Y 1 B THR 5   ? B THR 5   
17 1 Y 1 B GLY 6   ? B GLY 6   
18 1 Y 1 B GLU 7   ? B GLU 7   
19 1 Y 1 B SER 8   ? B SER 8   
20 1 Y 1 B LYS 9   ? B LYS 9   
21 1 Y 1 B ASN 124 ? B ASN 124 
22 1 Y 1 B PRO 125 ? B PRO 125 
23 1 Y 1 B LYS 126 ? B LYS 126 
24 1 Y 1 B GLU 127 ? B GLU 127 
# 
loop_
_chem_comp_atom.comp_id 
_chem_comp_atom.atom_id 
_chem_comp_atom.type_symbol 
_chem_comp_atom.pdbx_aromatic_flag 
_chem_comp_atom.pdbx_stereo_config 
_chem_comp_atom.pdbx_ordinal 
A1ISU C1   C  Y N 1   
A1ISU C2   C  Y N 2   
A1ISU C3   C  Y N 3   
A1ISU C4   C  Y N 4   
A1ISU C5   C  Y N 5   
A1ISU CL1  CL N N 6   
A1ISU N    N  N N 7   
A1ISU CL   CL N N 8   
A1ISU C    C  Y N 9   
A1ISU H1   H  N N 10  
A1ISU H2   H  N N 11  
A1ISU H3   H  N N 12  
A1ISU H4   H  N N 13  
A1ISU H5   H  N N 14  
ALA   N    N  N N 15  
ALA   CA   C  N S 16  
ALA   C    C  N N 17  
ALA   O    O  N N 18  
ALA   CB   C  N N 19  
ALA   OXT  O  N N 20  
ALA   H    H  N N 21  
ALA   H2   H  N N 22  
ALA   HA   H  N N 23  
ALA   HB1  H  N N 24  
ALA   HB2  H  N N 25  
ALA   HB3  H  N N 26  
ALA   HXT  H  N N 27  
ARG   N    N  N N 28  
ARG   CA   C  N S 29  
ARG   C    C  N N 30  
ARG   O    O  N N 31  
ARG   CB   C  N N 32  
ARG   CG   C  N N 33  
ARG   CD   C  N N 34  
ARG   NE   N  N N 35  
ARG   CZ   C  N N 36  
ARG   NH1  N  N N 37  
ARG   NH2  N  N N 38  
ARG   OXT  O  N N 39  
ARG   H    H  N N 40  
ARG   H2   H  N N 41  
ARG   HA   H  N N 42  
ARG   HB2  H  N N 43  
ARG   HB3  H  N N 44  
ARG   HG2  H  N N 45  
ARG   HG3  H  N N 46  
ARG   HD2  H  N N 47  
ARG   HD3  H  N N 48  
ARG   HE   H  N N 49  
ARG   HH11 H  N N 50  
ARG   HH12 H  N N 51  
ARG   HH21 H  N N 52  
ARG   HH22 H  N N 53  
ARG   HXT  H  N N 54  
ASN   N    N  N N 55  
ASN   CA   C  N S 56  
ASN   C    C  N N 57  
ASN   O    O  N N 58  
ASN   CB   C  N N 59  
ASN   CG   C  N N 60  
ASN   OD1  O  N N 61  
ASN   ND2  N  N N 62  
ASN   OXT  O  N N 63  
ASN   H    H  N N 64  
ASN   H2   H  N N 65  
ASN   HA   H  N N 66  
ASN   HB2  H  N N 67  
ASN   HB3  H  N N 68  
ASN   HD21 H  N N 69  
ASN   HD22 H  N N 70  
ASN   HXT  H  N N 71  
ASP   N    N  N N 72  
ASP   CA   C  N S 73  
ASP   C    C  N N 74  
ASP   O    O  N N 75  
ASP   CB   C  N N 76  
ASP   CG   C  N N 77  
ASP   OD1  O  N N 78  
ASP   OD2  O  N N 79  
ASP   OXT  O  N N 80  
ASP   H    H  N N 81  
ASP   H2   H  N N 82  
ASP   HA   H  N N 83  
ASP   HB2  H  N N 84  
ASP   HB3  H  N N 85  
ASP   HD2  H  N N 86  
ASP   HXT  H  N N 87  
CYS   N    N  N N 88  
CYS   CA   C  N R 89  
CYS   C    C  N N 90  
CYS   O    O  N N 91  
CYS   CB   C  N N 92  
CYS   SG   S  N N 93  
CYS   OXT  O  N N 94  
CYS   H    H  N N 95  
CYS   H2   H  N N 96  
CYS   HA   H  N N 97  
CYS   HB2  H  N N 98  
CYS   HB3  H  N N 99  
CYS   HG   H  N N 100 
CYS   HXT  H  N N 101 
GLU   N    N  N N 102 
GLU   CA   C  N S 103 
GLU   C    C  N N 104 
GLU   O    O  N N 105 
GLU   CB   C  N N 106 
GLU   CG   C  N N 107 
GLU   CD   C  N N 108 
GLU   OE1  O  N N 109 
GLU   OE2  O  N N 110 
GLU   OXT  O  N N 111 
GLU   H    H  N N 112 
GLU   H2   H  N N 113 
GLU   HA   H  N N 114 
GLU   HB2  H  N N 115 
GLU   HB3  H  N N 116 
GLU   HG2  H  N N 117 
GLU   HG3  H  N N 118 
GLU   HE2  H  N N 119 
GLU   HXT  H  N N 120 
GLY   N    N  N N 121 
GLY   CA   C  N N 122 
GLY   C    C  N N 123 
GLY   O    O  N N 124 
GLY   OXT  O  N N 125 
GLY   H    H  N N 126 
GLY   H2   H  N N 127 
GLY   HA2  H  N N 128 
GLY   HA3  H  N N 129 
GLY   HXT  H  N N 130 
HIS   N    N  N N 131 
HIS   CA   C  N S 132 
HIS   C    C  N N 133 
HIS   O    O  N N 134 
HIS   CB   C  N N 135 
HIS   CG   C  Y N 136 
HIS   ND1  N  Y N 137 
HIS   CD2  C  Y N 138 
HIS   CE1  C  Y N 139 
HIS   NE2  N  Y N 140 
HIS   OXT  O  N N 141 
HIS   H    H  N N 142 
HIS   H2   H  N N 143 
HIS   HA   H  N N 144 
HIS   HB2  H  N N 145 
HIS   HB3  H  N N 146 
HIS   HD1  H  N N 147 
HIS   HD2  H  N N 148 
HIS   HE1  H  N N 149 
HIS   HE2  H  N N 150 
HIS   HXT  H  N N 151 
HOH   O    O  N N 152 
HOH   H1   H  N N 153 
HOH   H2   H  N N 154 
ILE   N    N  N N 155 
ILE   CA   C  N S 156 
ILE   C    C  N N 157 
ILE   O    O  N N 158 
ILE   CB   C  N S 159 
ILE   CG1  C  N N 160 
ILE   CG2  C  N N 161 
ILE   CD1  C  N N 162 
ILE   OXT  O  N N 163 
ILE   H    H  N N 164 
ILE   H2   H  N N 165 
ILE   HA   H  N N 166 
ILE   HB   H  N N 167 
ILE   HG12 H  N N 168 
ILE   HG13 H  N N 169 
ILE   HG21 H  N N 170 
ILE   HG22 H  N N 171 
ILE   HG23 H  N N 172 
ILE   HD11 H  N N 173 
ILE   HD12 H  N N 174 
ILE   HD13 H  N N 175 
ILE   HXT  H  N N 176 
LEU   N    N  N N 177 
LEU   CA   C  N S 178 
LEU   C    C  N N 179 
LEU   O    O  N N 180 
LEU   CB   C  N N 181 
LEU   CG   C  N N 182 
LEU   CD1  C  N N 183 
LEU   CD2  C  N N 184 
LEU   OXT  O  N N 185 
LEU   H    H  N N 186 
LEU   H2   H  N N 187 
LEU   HA   H  N N 188 
LEU   HB2  H  N N 189 
LEU   HB3  H  N N 190 
LEU   HG   H  N N 191 
LEU   HD11 H  N N 192 
LEU   HD12 H  N N 193 
LEU   HD13 H  N N 194 
LEU   HD21 H  N N 195 
LEU   HD22 H  N N 196 
LEU   HD23 H  N N 197 
LEU   HXT  H  N N 198 
LYS   N    N  N N 199 
LYS   CA   C  N S 200 
LYS   C    C  N N 201 
LYS   O    O  N N 202 
LYS   CB   C  N N 203 
LYS   CG   C  N N 204 
LYS   CD   C  N N 205 
LYS   CE   C  N N 206 
LYS   NZ   N  N N 207 
LYS   OXT  O  N N 208 
LYS   H    H  N N 209 
LYS   H2   H  N N 210 
LYS   HA   H  N N 211 
LYS   HB2  H  N N 212 
LYS   HB3  H  N N 213 
LYS   HG2  H  N N 214 
LYS   HG3  H  N N 215 
LYS   HD2  H  N N 216 
LYS   HD3  H  N N 217 
LYS   HE2  H  N N 218 
LYS   HE3  H  N N 219 
LYS   HZ1  H  N N 220 
LYS   HZ2  H  N N 221 
LYS   HZ3  H  N N 222 
LYS   HXT  H  N N 223 
MET   N    N  N N 224 
MET   CA   C  N S 225 
MET   C    C  N N 226 
MET   O    O  N N 227 
MET   CB   C  N N 228 
MET   CG   C  N N 229 
MET   SD   S  N N 230 
MET   CE   C  N N 231 
MET   OXT  O  N N 232 
MET   H    H  N N 233 
MET   H2   H  N N 234 
MET   HA   H  N N 235 
MET   HB2  H  N N 236 
MET   HB3  H  N N 237 
MET   HG2  H  N N 238 
MET   HG3  H  N N 239 
MET   HE1  H  N N 240 
MET   HE2  H  N N 241 
MET   HE3  H  N N 242 
MET   HXT  H  N N 243 
PHE   N    N  N N 244 
PHE   CA   C  N S 245 
PHE   C    C  N N 246 
PHE   O    O  N N 247 
PHE   CB   C  N N 248 
PHE   CG   C  Y N 249 
PHE   CD1  C  Y N 250 
PHE   CD2  C  Y N 251 
PHE   CE1  C  Y N 252 
PHE   CE2  C  Y N 253 
PHE   CZ   C  Y N 254 
PHE   OXT  O  N N 255 
PHE   H    H  N N 256 
PHE   H2   H  N N 257 
PHE   HA   H  N N 258 
PHE   HB2  H  N N 259 
PHE   HB3  H  N N 260 
PHE   HD1  H  N N 261 
PHE   HD2  H  N N 262 
PHE   HE1  H  N N 263 
PHE   HE2  H  N N 264 
PHE   HZ   H  N N 265 
PHE   HXT  H  N N 266 
PRO   N    N  N N 267 
PRO   CA   C  N S 268 
PRO   C    C  N N 269 
PRO   O    O  N N 270 
PRO   CB   C  N N 271 
PRO   CG   C  N N 272 
PRO   CD   C  N N 273 
PRO   OXT  O  N N 274 
PRO   H    H  N N 275 
PRO   HA   H  N N 276 
PRO   HB2  H  N N 277 
PRO   HB3  H  N N 278 
PRO   HG2  H  N N 279 
PRO   HG3  H  N N 280 
PRO   HD2  H  N N 281 
PRO   HD3  H  N N 282 
PRO   HXT  H  N N 283 
SER   N    N  N N 284 
SER   CA   C  N S 285 
SER   C    C  N N 286 
SER   O    O  N N 287 
SER   CB   C  N N 288 
SER   OG   O  N N 289 
SER   OXT  O  N N 290 
SER   H    H  N N 291 
SER   H2   H  N N 292 
SER   HA   H  N N 293 
SER   HB2  H  N N 294 
SER   HB3  H  N N 295 
SER   HG   H  N N 296 
SER   HXT  H  N N 297 
THR   N    N  N N 298 
THR   CA   C  N S 299 
THR   C    C  N N 300 
THR   O    O  N N 301 
THR   CB   C  N R 302 
THR   OG1  O  N N 303 
THR   CG2  C  N N 304 
THR   OXT  O  N N 305 
THR   H    H  N N 306 
THR   H2   H  N N 307 
THR   HA   H  N N 308 
THR   HB   H  N N 309 
THR   HG1  H  N N 310 
THR   HG21 H  N N 311 
THR   HG22 H  N N 312 
THR   HG23 H  N N 313 
THR   HXT  H  N N 314 
TRP   N    N  N N 315 
TRP   CA   C  N S 316 
TRP   C    C  N N 317 
TRP   O    O  N N 318 
TRP   CB   C  N N 319 
TRP   CG   C  Y N 320 
TRP   CD1  C  Y N 321 
TRP   CD2  C  Y N 322 
TRP   NE1  N  Y N 323 
TRP   CE2  C  Y N 324 
TRP   CE3  C  Y N 325 
TRP   CZ2  C  Y N 326 
TRP   CZ3  C  Y N 327 
TRP   CH2  C  Y N 328 
TRP   OXT  O  N N 329 
TRP   H    H  N N 330 
TRP   H2   H  N N 331 
TRP   HA   H  N N 332 
TRP   HB2  H  N N 333 
TRP   HB3  H  N N 334 
TRP   HD1  H  N N 335 
TRP   HE1  H  N N 336 
TRP   HE3  H  N N 337 
TRP   HZ2  H  N N 338 
TRP   HZ3  H  N N 339 
TRP   HH2  H  N N 340 
TRP   HXT  H  N N 341 
TYR   N    N  N N 342 
TYR   CA   C  N S 343 
TYR   C    C  N N 344 
TYR   O    O  N N 345 
TYR   CB   C  N N 346 
TYR   CG   C  Y N 347 
TYR   CD1  C  Y N 348 
TYR   CD2  C  Y N 349 
TYR   CE1  C  Y N 350 
TYR   CE2  C  Y N 351 
TYR   CZ   C  Y N 352 
TYR   OH   O  N N 353 
TYR   OXT  O  N N 354 
TYR   H    H  N N 355 
TYR   H2   H  N N 356 
TYR   HA   H  N N 357 
TYR   HB2  H  N N 358 
TYR   HB3  H  N N 359 
TYR   HD1  H  N N 360 
TYR   HD2  H  N N 361 
TYR   HE1  H  N N 362 
TYR   HE2  H  N N 363 
TYR   HH   H  N N 364 
TYR   HXT  H  N N 365 
VAL   N    N  N N 366 
VAL   CA   C  N S 367 
VAL   C    C  N N 368 
VAL   O    O  N N 369 
VAL   CB   C  N N 370 
VAL   CG1  C  N N 371 
VAL   CG2  C  N N 372 
VAL   OXT  O  N N 373 
VAL   H    H  N N 374 
VAL   H2   H  N N 375 
VAL   HA   H  N N 376 
VAL   HB   H  N N 377 
VAL   HG11 H  N N 378 
VAL   HG12 H  N N 379 
VAL   HG13 H  N N 380 
VAL   HG21 H  N N 381 
VAL   HG22 H  N N 382 
VAL   HG23 H  N N 383 
VAL   HXT  H  N N 384 
# 
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 
A1ISU CL1 C3   sing N N 1   
A1ISU CL  C5   sing N N 2   
A1ISU C4  C3   doub Y N 3   
A1ISU C4  C5   sing Y N 4   
A1ISU C3  C2   sing Y N 5   
A1ISU C5  C    doub Y N 6   
A1ISU C2  C1   doub Y N 7   
A1ISU C   C1   sing Y N 8   
A1ISU C1  N    sing N N 9   
A1ISU C2  H1   sing N N 10  
A1ISU C4  H2   sing N N 11  
A1ISU N   H3   sing N N 12  
A1ISU N   H4   sing N N 13  
A1ISU C   H5   sing N N 14  
ALA   N   CA   sing N N 15  
ALA   N   H    sing N N 16  
ALA   N   H2   sing N N 17  
ALA   CA  C    sing N N 18  
ALA   CA  CB   sing N N 19  
ALA   CA  HA   sing N N 20  
ALA   C   O    doub N N 21  
ALA   C   OXT  sing N N 22  
ALA   CB  HB1  sing N N 23  
ALA   CB  HB2  sing N N 24  
ALA   CB  HB3  sing N N 25  
ALA   OXT HXT  sing N N 26  
ARG   N   CA   sing N N 27  
ARG   N   H    sing N N 28  
ARG   N   H2   sing N N 29  
ARG   CA  C    sing N N 30  
ARG   CA  CB   sing N N 31  
ARG   CA  HA   sing N N 32  
ARG   C   O    doub N N 33  
ARG   C   OXT  sing N N 34  
ARG   CB  CG   sing N N 35  
ARG   CB  HB2  sing N N 36  
ARG   CB  HB3  sing N N 37  
ARG   CG  CD   sing N N 38  
ARG   CG  HG2  sing N N 39  
ARG   CG  HG3  sing N N 40  
ARG   CD  NE   sing N N 41  
ARG   CD  HD2  sing N N 42  
ARG   CD  HD3  sing N N 43  
ARG   NE  CZ   sing N N 44  
ARG   NE  HE   sing N N 45  
ARG   CZ  NH1  sing N N 46  
ARG   CZ  NH2  doub N N 47  
ARG   NH1 HH11 sing N N 48  
ARG   NH1 HH12 sing N N 49  
ARG   NH2 HH21 sing N N 50  
ARG   NH2 HH22 sing N N 51  
ARG   OXT HXT  sing N N 52  
ASN   N   CA   sing N N 53  
ASN   N   H    sing N N 54  
ASN   N   H2   sing N N 55  
ASN   CA  C    sing N N 56  
ASN   CA  CB   sing N N 57  
ASN   CA  HA   sing N N 58  
ASN   C   O    doub N N 59  
ASN   C   OXT  sing N N 60  
ASN   CB  CG   sing N N 61  
ASN   CB  HB2  sing N N 62  
ASN   CB  HB3  sing N N 63  
ASN   CG  OD1  doub N N 64  
ASN   CG  ND2  sing N N 65  
ASN   ND2 HD21 sing N N 66  
ASN   ND2 HD22 sing N N 67  
ASN   OXT HXT  sing N N 68  
ASP   N   CA   sing N N 69  
ASP   N   H    sing N N 70  
ASP   N   H2   sing N N 71  
ASP   CA  C    sing N N 72  
ASP   CA  CB   sing N N 73  
ASP   CA  HA   sing N N 74  
ASP   C   O    doub N N 75  
ASP   C   OXT  sing N N 76  
ASP   CB  CG   sing N N 77  
ASP   CB  HB2  sing N N 78  
ASP   CB  HB3  sing N N 79  
ASP   CG  OD1  doub N N 80  
ASP   CG  OD2  sing N N 81  
ASP   OD2 HD2  sing N N 82  
ASP   OXT HXT  sing N N 83  
CYS   N   CA   sing N N 84  
CYS   N   H    sing N N 85  
CYS   N   H2   sing N N 86  
CYS   CA  C    sing N N 87  
CYS   CA  CB   sing N N 88  
CYS   CA  HA   sing N N 89  
CYS   C   O    doub N N 90  
CYS   C   OXT  sing N N 91  
CYS   CB  SG   sing N N 92  
CYS   CB  HB2  sing N N 93  
CYS   CB  HB3  sing N N 94  
CYS   SG  HG   sing N N 95  
CYS   OXT HXT  sing N N 96  
GLU   N   CA   sing N N 97  
GLU   N   H    sing N N 98  
GLU   N   H2   sing N N 99  
GLU   CA  C    sing N N 100 
GLU   CA  CB   sing N N 101 
GLU   CA  HA   sing N N 102 
GLU   C   O    doub N N 103 
GLU   C   OXT  sing N N 104 
GLU   CB  CG   sing N N 105 
GLU   CB  HB2  sing N N 106 
GLU   CB  HB3  sing N N 107 
GLU   CG  CD   sing N N 108 
GLU   CG  HG2  sing N N 109 
GLU   CG  HG3  sing N N 110 
GLU   CD  OE1  doub N N 111 
GLU   CD  OE2  sing N N 112 
GLU   OE2 HE2  sing N N 113 
GLU   OXT HXT  sing N N 114 
GLY   N   CA   sing N N 115 
GLY   N   H    sing N N 116 
GLY   N   H2   sing N N 117 
GLY   CA  C    sing N N 118 
GLY   CA  HA2  sing N N 119 
GLY   CA  HA3  sing N N 120 
GLY   C   O    doub N N 121 
GLY   C   OXT  sing N N 122 
GLY   OXT HXT  sing N N 123 
HIS   N   CA   sing N N 124 
HIS   N   H    sing N N 125 
HIS   N   H2   sing N N 126 
HIS   CA  C    sing N N 127 
HIS   CA  CB   sing N N 128 
HIS   CA  HA   sing N N 129 
HIS   C   O    doub N N 130 
HIS   C   OXT  sing N N 131 
HIS   CB  CG   sing N N 132 
HIS   CB  HB2  sing N N 133 
HIS   CB  HB3  sing N N 134 
HIS   CG  ND1  sing Y N 135 
HIS   CG  CD2  doub Y N 136 
HIS   ND1 CE1  doub Y N 137 
HIS   ND1 HD1  sing N N 138 
HIS   CD2 NE2  sing Y N 139 
HIS   CD2 HD2  sing N N 140 
HIS   CE1 NE2  sing Y N 141 
HIS   CE1 HE1  sing N N 142 
HIS   NE2 HE2  sing N N 143 
HIS   OXT HXT  sing N N 144 
HOH   O   H1   sing N N 145 
HOH   O   H2   sing N N 146 
ILE   N   CA   sing N N 147 
ILE   N   H    sing N N 148 
ILE   N   H2   sing N N 149 
ILE   CA  C    sing N N 150 
ILE   CA  CB   sing N N 151 
ILE   CA  HA   sing N N 152 
ILE   C   O    doub N N 153 
ILE   C   OXT  sing N N 154 
ILE   CB  CG1  sing N N 155 
ILE   CB  CG2  sing N N 156 
ILE   CB  HB   sing N N 157 
ILE   CG1 CD1  sing N N 158 
ILE   CG1 HG12 sing N N 159 
ILE   CG1 HG13 sing N N 160 
ILE   CG2 HG21 sing N N 161 
ILE   CG2 HG22 sing N N 162 
ILE   CG2 HG23 sing N N 163 
ILE   CD1 HD11 sing N N 164 
ILE   CD1 HD12 sing N N 165 
ILE   CD1 HD13 sing N N 166 
ILE   OXT HXT  sing N N 167 
LEU   N   CA   sing N N 168 
LEU   N   H    sing N N 169 
LEU   N   H2   sing N N 170 
LEU   CA  C    sing N N 171 
LEU   CA  CB   sing N N 172 
LEU   CA  HA   sing N N 173 
LEU   C   O    doub N N 174 
LEU   C   OXT  sing N N 175 
LEU   CB  CG   sing N N 176 
LEU   CB  HB2  sing N N 177 
LEU   CB  HB3  sing N N 178 
LEU   CG  CD1  sing N N 179 
LEU   CG  CD2  sing N N 180 
LEU   CG  HG   sing N N 181 
LEU   CD1 HD11 sing N N 182 
LEU   CD1 HD12 sing N N 183 
LEU   CD1 HD13 sing N N 184 
LEU   CD2 HD21 sing N N 185 
LEU   CD2 HD22 sing N N 186 
LEU   CD2 HD23 sing N N 187 
LEU   OXT HXT  sing N N 188 
LYS   N   CA   sing N N 189 
LYS   N   H    sing N N 190 
LYS   N   H2   sing N N 191 
LYS   CA  C    sing N N 192 
LYS   CA  CB   sing N N 193 
LYS   CA  HA   sing N N 194 
LYS   C   O    doub N N 195 
LYS   C   OXT  sing N N 196 
LYS   CB  CG   sing N N 197 
LYS   CB  HB2  sing N N 198 
LYS   CB  HB3  sing N N 199 
LYS   CG  CD   sing N N 200 
LYS   CG  HG2  sing N N 201 
LYS   CG  HG3  sing N N 202 
LYS   CD  CE   sing N N 203 
LYS   CD  HD2  sing N N 204 
LYS   CD  HD3  sing N N 205 
LYS   CE  NZ   sing N N 206 
LYS   CE  HE2  sing N N 207 
LYS   CE  HE3  sing N N 208 
LYS   NZ  HZ1  sing N N 209 
LYS   NZ  HZ2  sing N N 210 
LYS   NZ  HZ3  sing N N 211 
LYS   OXT HXT  sing N N 212 
MET   N   CA   sing N N 213 
MET   N   H    sing N N 214 
MET   N   H2   sing N N 215 
MET   CA  C    sing N N 216 
MET   CA  CB   sing N N 217 
MET   CA  HA   sing N N 218 
MET   C   O    doub N N 219 
MET   C   OXT  sing N N 220 
MET   CB  CG   sing N N 221 
MET   CB  HB2  sing N N 222 
MET   CB  HB3  sing N N 223 
MET   CG  SD   sing N N 224 
MET   CG  HG2  sing N N 225 
MET   CG  HG3  sing N N 226 
MET   SD  CE   sing N N 227 
MET   CE  HE1  sing N N 228 
MET   CE  HE2  sing N N 229 
MET   CE  HE3  sing N N 230 
MET   OXT HXT  sing N N 231 
PHE   N   CA   sing N N 232 
PHE   N   H    sing N N 233 
PHE   N   H2   sing N N 234 
PHE   CA  C    sing N N 235 
PHE   CA  CB   sing N N 236 
PHE   CA  HA   sing N N 237 
PHE   C   O    doub N N 238 
PHE   C   OXT  sing N N 239 
PHE   CB  CG   sing N N 240 
PHE   CB  HB2  sing N N 241 
PHE   CB  HB3  sing N N 242 
PHE   CG  CD1  doub Y N 243 
PHE   CG  CD2  sing Y N 244 
PHE   CD1 CE1  sing Y N 245 
PHE   CD1 HD1  sing N N 246 
PHE   CD2 CE2  doub Y N 247 
PHE   CD2 HD2  sing N N 248 
PHE   CE1 CZ   doub Y N 249 
PHE   CE1 HE1  sing N N 250 
PHE   CE2 CZ   sing Y N 251 
PHE   CE2 HE2  sing N N 252 
PHE   CZ  HZ   sing N N 253 
PHE   OXT HXT  sing N N 254 
PRO   N   CA   sing N N 255 
PRO   N   CD   sing N N 256 
PRO   N   H    sing N N 257 
PRO   CA  C    sing N N 258 
PRO   CA  CB   sing N N 259 
PRO   CA  HA   sing N N 260 
PRO   C   O    doub N N 261 
PRO   C   OXT  sing N N 262 
PRO   CB  CG   sing N N 263 
PRO   CB  HB2  sing N N 264 
PRO   CB  HB3  sing N N 265 
PRO   CG  CD   sing N N 266 
PRO   CG  HG2  sing N N 267 
PRO   CG  HG3  sing N N 268 
PRO   CD  HD2  sing N N 269 
PRO   CD  HD3  sing N N 270 
PRO   OXT HXT  sing N N 271 
SER   N   CA   sing N N 272 
SER   N   H    sing N N 273 
SER   N   H2   sing N N 274 
SER   CA  C    sing N N 275 
SER   CA  CB   sing N N 276 
SER   CA  HA   sing N N 277 
SER   C   O    doub N N 278 
SER   C   OXT  sing N N 279 
SER   CB  OG   sing N N 280 
SER   CB  HB2  sing N N 281 
SER   CB  HB3  sing N N 282 
SER   OG  HG   sing N N 283 
SER   OXT HXT  sing N N 284 
THR   N   CA   sing N N 285 
THR   N   H    sing N N 286 
THR   N   H2   sing N N 287 
THR   CA  C    sing N N 288 
THR   CA  CB   sing N N 289 
THR   CA  HA   sing N N 290 
THR   C   O    doub N N 291 
THR   C   OXT  sing N N 292 
THR   CB  OG1  sing N N 293 
THR   CB  CG2  sing N N 294 
THR   CB  HB   sing N N 295 
THR   OG1 HG1  sing N N 296 
THR   CG2 HG21 sing N N 297 
THR   CG2 HG22 sing N N 298 
THR   CG2 HG23 sing N N 299 
THR   OXT HXT  sing N N 300 
TRP   N   CA   sing N N 301 
TRP   N   H    sing N N 302 
TRP   N   H2   sing N N 303 
TRP   CA  C    sing N N 304 
TRP   CA  CB   sing N N 305 
TRP   CA  HA   sing N N 306 
TRP   C   O    doub N N 307 
TRP   C   OXT  sing N N 308 
TRP   CB  CG   sing N N 309 
TRP   CB  HB2  sing N N 310 
TRP   CB  HB3  sing N N 311 
TRP   CG  CD1  doub Y N 312 
TRP   CG  CD2  sing Y N 313 
TRP   CD1 NE1  sing Y N 314 
TRP   CD1 HD1  sing N N 315 
TRP   CD2 CE2  doub Y N 316 
TRP   CD2 CE3  sing Y N 317 
TRP   NE1 CE2  sing Y N 318 
TRP   NE1 HE1  sing N N 319 
TRP   CE2 CZ2  sing Y N 320 
TRP   CE3 CZ3  doub Y N 321 
TRP   CE3 HE3  sing N N 322 
TRP   CZ2 CH2  doub Y N 323 
TRP   CZ2 HZ2  sing N N 324 
TRP   CZ3 CH2  sing Y N 325 
TRP   CZ3 HZ3  sing N N 326 
TRP   CH2 HH2  sing N N 327 
TRP   OXT HXT  sing N N 328 
TYR   N   CA   sing N N 329 
TYR   N   H    sing N N 330 
TYR   N   H2   sing N N 331 
TYR   CA  C    sing N N 332 
TYR   CA  CB   sing N N 333 
TYR   CA  HA   sing N N 334 
TYR   C   O    doub N N 335 
TYR   C   OXT  sing N N 336 
TYR   CB  CG   sing N N 337 
TYR   CB  HB2  sing N N 338 
TYR   CB  HB3  sing N N 339 
TYR   CG  CD1  doub Y N 340 
TYR   CG  CD2  sing Y N 341 
TYR   CD1 CE1  sing Y N 342 
TYR   CD1 HD1  sing N N 343 
TYR   CD2 CE2  doub Y N 344 
TYR   CD2 HD2  sing N N 345 
TYR   CE1 CZ   doub Y N 346 
TYR   CE1 HE1  sing N N 347 
TYR   CE2 CZ   sing Y N 348 
TYR   CE2 HE2  sing N N 349 
TYR   CZ  OH   sing N N 350 
TYR   OH  HH   sing N N 351 
TYR   OXT HXT  sing N N 352 
VAL   N   CA   sing N N 353 
VAL   N   H    sing N N 354 
VAL   N   H2   sing N N 355 
VAL   CA  C    sing N N 356 
VAL   CA  CB   sing N N 357 
VAL   CA  HA   sing N N 358 
VAL   C   O    doub N N 359 
VAL   C   OXT  sing N N 360 
VAL   CB  CG1  sing N N 361 
VAL   CB  CG2  sing N N 362 
VAL   CB  HB   sing N N 363 
VAL   CG1 HG11 sing N N 364 
VAL   CG1 HG12 sing N N 365 
VAL   CG1 HG13 sing N N 366 
VAL   CG2 HG21 sing N N 367 
VAL   CG2 HG22 sing N N 368 
VAL   CG2 HG23 sing N N 369 
VAL   OXT HXT  sing N N 370 
# 
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                    9H7F 
_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]   0.011750 
_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]   0.022831 
_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]   0.015442 
_atom_sites.fract_transf_vector[1]      0.00000 
_atom_sites.fract_transf_vector[2]      0.00000 
_atom_sites.fract_transf_vector[3]      0.00000 
_atom_sites.solution_primary            ? 
_atom_sites.solution_secondary          ? 
_atom_sites.solution_hydrogens          ? 
_atom_sites.special_details             ? 
# 
loop_
_atom_type.symbol 
C  
CL 
N  
O  
S  
# 
loop_
_atom_site.group_PDB 
_atom_site.id 
_atom_site.type_symbol 
_atom_site.label_atom_id 
_atom_site.label_alt_id 
_atom_site.label_comp_id 
_atom_site.label_asym_id 
_atom_site.label_entity_id 
_atom_site.label_seq_id 
_atom_site.pdbx_PDB_ins_code 
_atom_site.Cartn_x 
_atom_site.Cartn_y 
_atom_site.Cartn_z 
_atom_site.occupancy 
_atom_site.B_iso_or_equiv 
_atom_site.pdbx_formal_charge 
_atom_site.auth_seq_id 
_atom_site.auth_comp_id 
_atom_site.auth_asym_id 
_atom_site.auth_atom_id 
_atom_site.pdbx_PDB_model_num 
ATOM   1    C  C   . CYS   A 1 10  ? -11.660 6.068   -5.154  1.00 38.78 ? 10  CYS   A C   1 
ATOM   2    O  O   . CYS   A 1 10  ? -10.508 6.251   -4.732  1.00 44.22 ? 10  CYS   A O   1 
ATOM   3    N  N   . PRO   A 1 11  ? -12.721 6.652   -4.581  1.00 23.78 ? 11  PRO   A N   1 
ATOM   4    C  CA  . PRO   A 1 11  ? -12.566 7.463   -3.426  1.00 20.14 ? 11  PRO   A CA  1 
ATOM   5    C  C   . PRO   A 1 11  ? -12.469 6.742   -2.065  1.00 17.64 ? 11  PRO   A C   1 
ATOM   6    O  O   . PRO   A 1 11  ? -12.156 7.385   -1.098  1.00 17.47 ? 11  PRO   A O   1 
ATOM   7    C  CB  . PRO   A 1 11  ? -13.799 8.377   -3.427  1.00 29.09 ? 11  PRO   A CB  1 
ATOM   8    C  CG  . PRO   A 1 11  ? -14.785 7.613   -4.059  1.00 34.67 ? 11  PRO   A CG  1 
ATOM   9    C  CD  . PRO   A 1 11  ? -14.066 6.852   -5.136  1.00 27.26 ? 11  PRO   A CD  1 
ATOM   10   N  N   . LEU   A 1 12  ? -12.766 5.460   -2.039  1.00 17.67 ? 12  LEU   A N   1 
ATOM   11   C  CA  . LEU   A 1 12  ? -12.694 4.693   -0.791  1.00 17.03 ? 12  LEU   A CA  1 
ATOM   12   C  C   . LEU   A 1 12  ? -12.079 3.354   -1.058  1.00 17.02 ? 12  LEU   A C   1 
ATOM   13   O  O   . LEU   A 1 12  ? -12.582 2.580   -1.882  1.00 23.28 ? 12  LEU   A O   1 
ATOM   14   C  CB  . LEU   A 1 12  ? -14.080 4.523   -0.210  1.00 17.60 ? 12  LEU   A CB  1 
ATOM   15   C  CG  . LEU   A 1 12  ? -14.212 3.789   1.109   1.00 18.82 ? 12  LEU   A CG  1 
ATOM   16   C  CD1 . LEU   A 1 12  ? -13.412 4.522   2.176   1.00 19.09 ? 12  LEU   A CD1 1 
ATOM   17   C  CD2 . LEU   A 1 12  ? -15.674 3.629   1.497   1.00 23.17 ? 12  LEU   A CD2 1 
ATOM   18   N  N   . MET   A 1 13  ? -11.007 3.057   -0.367  1.00 14.98 ? 13  MET   A N   1 
ATOM   19   C  CA  . MET   A 1 13  ? -10.311 1.744   -0.478  1.00 15.27 ? 13  MET   A CA  1 
ATOM   20   C  C   . MET   A 1 13  ? -10.056 1.241   0.923   1.00 13.84 ? 13  MET   A C   1 
ATOM   21   O  O   . MET   A 1 13  ? -9.771  2.052   1.794   1.00 14.28 ? 13  MET   A O   1 
ATOM   22   C  CB  . MET   A 1 13  ? -8.943  1.935   -1.215  1.00 19.42 ? 13  MET   A CB  1 
ATOM   23   C  CG  . MET   A 1 13  ? -8.314  0.547   -1.589  1.00 23.61 ? 13  MET   A CG  1 
ATOM   24   S  SD  . MET   A 1 13  ? -7.181  -0.099  -0.404  0.50 19.11 ? 13  MET   A SD  1 
ATOM   25   C  CE  . MET   A 1 13  ? -5.681  0.761   -0.886  0.50 22.57 ? 13  MET   A CE  1 
ATOM   26   N  N   . VAL   A 1 14  ? -10.159 -0.049  1.119   1.00 13.70 ? 14  VAL   A N   1 
ATOM   27   C  CA  . VAL   A 1 14  ? -9.906  -0.672  2.385   1.00 13.41 ? 14  VAL   A CA  1 
ATOM   28   C  C   . VAL   A 1 14  ? -8.792  -1.702  2.187   1.00 13.69 ? 14  VAL   A C   1 
ATOM   29   O  O   . VAL   A 1 14  ? -8.852  -2.478  1.232   1.00 17.15 ? 14  VAL   A O   1 
ATOM   30   C  CB  . VAL   A 1 14  ? -11.156 -1.324  2.993   1.00 14.58 ? 14  VAL   A CB  1 
ATOM   31   C  CG1 . VAL   A 1 14  ? -10.868 -2.004  4.313   1.00 17.45 ? 14  VAL   A CG1 1 
ATOM   32   C  CG2 . VAL   A 1 14  ? -12.283 -0.277  3.087   1.00 15.55 ? 14  VAL   A CG2 1 
ATOM   33   N  N   . LYS   A 1 15  ? -7.817  -1.713  3.094   1.00 12.66 ? 15  LYS   A N   1 
ATOM   34   C  CA  . LYS   A 1 15  ? -6.690  -2.632  3.025   1.00 13.83 ? 15  LYS   A CA  1 
ATOM   35   C  C   . LYS   A 1 15  ? -6.533  -3.312  4.349   1.00 12.58 ? 15  LYS   A C   1 
ATOM   36   O  O   . LYS   A 1 15  ? -6.569  -2.640  5.363   1.00 14.80 ? 15  LYS   A O   1 
ATOM   37   C  CB  . LYS   A 1 15  ? -5.401  -1.859  2.651   1.00 16.84 ? 15  LYS   A CB  1 
ATOM   38   C  CG  . LYS   A 1 15  ? -4.204  -2.773  2.603   0.50 18.77 ? 15  LYS   A CG  1 
ATOM   39   C  CD  . LYS   A 1 15  ? -3.029  -2.204  1.835   0.50 28.79 ? 15  LYS   A CD  1 
ATOM   40   C  CE  . LYS   A 1 15  ? -1.904  -3.233  1.651   0.50 28.44 ? 15  LYS   A CE  1 
ATOM   41   N  NZ  . LYS   A 1 15  ? -1.259  -2.959  0.349   0.50 36.32 ? 15  LYS   A NZ  1 
ATOM   42   N  N   . VAL   A 1 16  ? -6.383  -4.623  4.349   1.00 12.13 ? 16  VAL   A N   1 
ATOM   43   C  CA  . VAL   A 1 16  ? -6.326  -5.382  5.594   1.00 11.61 ? 16  VAL   A CA  1 
ATOM   44   C  C   . VAL   A 1 16  ? -5.096  -6.302  5.562   1.00 11.28 ? 16  VAL   A C   1 
ATOM   45   O  O   . VAL   A 1 16  ? -4.912  -7.027  4.581   1.00 12.84 ? 16  VAL   A O   1 
ATOM   46   C  CB  . VAL   A 1 16  ? -7.617  -6.192  5.838   1.00 12.92 ? 16  VAL   A CB  1 
ATOM   47   C  CG1 . VAL   A 1 16  ? -7.604  -6.802  7.232   1.00 13.83 ? 16  VAL   A CG1 1 
ATOM   48   C  CG2 . VAL   A 1 16  ? -8.873  -5.335  5.641   1.00 14.17 ? 16  VAL   A CG2 1 
ATOM   49   N  N   . LEU   A 1 17  ? -4.315  -6.259  6.599   1.00 11.57 ? 17  LEU   A N   1 
ATOM   50   C  CA  . LEU   A 1 17  ? -3.108  -7.045  6.789   1.00 11.35 ? 17  LEU   A CA  1 
ATOM   51   C  C   . LEU   A 1 17  ? -3.188  -7.859  8.027   1.00 11.21 ? 17  LEU   A C   1 
ATOM   52   O  O   . LEU   A 1 17  ? -3.833  -7.536  8.993   1.00 12.36 ? 17  LEU   A O   1 
ATOM   53   C  CB  . LEU   A 1 17  ? -1.882  -6.132  6.872   1.00 13.83 ? 17  LEU   A CB  1 
ATOM   54   C  CG  . LEU   A 1 17  ? -1.510  -5.292  5.653   1.00 16.18 ? 17  LEU   A CG  1 
ATOM   55   C  CD1 . LEU   A 1 17  ? -0.292  -4.415  6.010   1.00 19.27 ? 17  LEU   A CD1 1 
ATOM   56   C  CD2 . LEU   A 1 17  ? -1.269  -6.212  4.459   1.00 20.60 ? 17  LEU   A CD2 1 
ATOM   57   N  N   . ASP   A 1 18  ? -2.499  -9.030  7.971   1.00 12.38 ? 18  ASP   A N   1 
ATOM   58   C  CA  . ASP   A 1 18  ? -2.423  -10.003 9.073   1.00 11.97 ? 18  ASP   A CA  1 
ATOM   59   C  C   . ASP   A 1 18  ? -1.016  -9.894  9.703   1.00 11.99 ? 18  ASP   A C   1 
ATOM   60   O  O   . ASP   A 1 18  ? -0.006  -10.178 9.027   1.00 12.31 ? 18  ASP   A O   1 
ATOM   61   C  CB  . ASP   A 1 18  ? -2.668  -11.417 8.491   1.00 12.45 ? 18  ASP   A CB  1 
ATOM   62   C  CG  . ASP   A 1 18  ? -2.564  -12.529 9.464   1.00 13.03 ? 18  ASP   A CG  1 
ATOM   63   O  OD1 . ASP   A 1 18  ? -1.733  -12.496 10.381  1.00 14.52 ? 18  ASP   A OD1 1 
ATOM   64   O  OD2 . ASP   A 1 18  ? -3.246  -13.538 9.274   1.00 16.74 ? 18  ASP   A OD2 1 
ATOM   65   N  N   . ALA   A 1 19  ? -0.959  -9.463  10.938  1.00 11.09 ? 19  ALA   A N   1 
ATOM   66   C  CA  . ALA   A 1 19  ? 0.283   -9.215  11.683  1.00 11.50 ? 19  ALA   A CA  1 
ATOM   67   C  C   . ALA   A 1 19  ? 0.914   -10.480 12.239  1.00 10.38 ? 19  ALA   A C   1 
ATOM   68   O  O   . ALA   A 1 19  ? 2.030   -10.429 12.763  1.00 13.14 ? 19  ALA   A O   1 
ATOM   69   C  CB  . ALA   A 1 19  ? 0.042   -8.223  12.804  1.00 13.03 ? 19  ALA   A CB  1 
ATOM   70   N  N   . VAL   A 1 20  ? 0.225   -11.606 12.207  1.00 11.79 ? 20  VAL   A N   1 
ATOM   71   C  CA  . VAL   A 1 20  ? 0.774   -12.887 12.627  1.00 12.68 ? 20  VAL   A CA  1 
ATOM   72   C  C   . VAL   A 1 20  ? 1.629   -13.494 11.504  1.00 13.57 ? 20  VAL   A C   1 
ATOM   73   O  O   . VAL   A 1 20  ? 2.752   -13.940 11.757  1.00 15.48 ? 20  VAL   A O   1 
ATOM   74   C  CB  . VAL   A 1 20  ? -0.352  -13.844 13.102  1.00 13.49 ? 20  VAL   A CB  1 
ATOM   75   C  CG1 . VAL   A 1 20  ? 0.236   -15.278 13.365  1.00 16.62 ? 20  VAL   A CG1 1 
ATOM   76   C  CG2 . VAL   A 1 20  ? -1.049  -13.283 14.344  1.00 15.41 ? 20  VAL   A CG2 1 
ATOM   77   N  N   . ARG   A 1 21  ? 1.105   -13.457 10.296  1.00 13.70 ? 21  ARG   A N   1 
ATOM   78   C  CA  . ARG   A 1 21  ? 1.795   -14.091 9.150   1.00 15.84 ? 21  ARG   A CA  1 
ATOM   79   C  C   . ARG   A 1 21  ? 2.550   -13.077 8.292   1.00 13.78 ? 21  ARG   A C   1 
ATOM   80   O  O   . ARG   A 1 21  ? 3.324   -13.501 7.450   1.00 16.60 ? 21  ARG   A O   1 
ATOM   81   C  CB  . ARG   A 1 21  ? 0.719   -14.762 8.304   1.00 20.34 ? 21  ARG   A CB  1 
ATOM   82   N  N   . GLY   A 1 22  ? 2.342   -11.776 8.495   1.00 13.27 ? 22  GLY   A N   1 
ATOM   83   C  CA  . GLY   A 1 22  ? 2.967   -10.793 7.627   1.00 13.87 ? 22  GLY   A CA  1 
ATOM   84   C  C   . GLY   A 1 22  ? 2.487   -10.916 6.200   1.00 12.36 ? 22  GLY   A C   1 
ATOM   85   O  O   . GLY   A 1 22  ? 3.282   -10.980 5.271   1.00 14.42 ? 22  GLY   A O   1 
ATOM   86   N  N   . SER   A 1 23  ? 1.206   -10.895 6.044   1.00 13.33 ? 23  SER   A N   1 
ATOM   87   C  CA  . SER   A 1 23  ? 0.579   -11.100 4.762   1.00 13.28 ? 23  SER   A CA  1 
ATOM   88   C  C   . SER   A 1 23  ? -0.670  -10.269 4.620   1.00 13.19 ? 23  SER   A C   1 
ATOM   89   O  O   . SER   A 1 23  ? -1.248  -9.870  5.612   1.00 14.81 ? 23  SER   A O   1 
ATOM   90   C  CB  . SER   A 1 23  ? 0.154   -12.565 4.665   1.00 16.10 ? 23  SER   A CB  1 
ATOM   91   O  OG  . SER   A 1 23  ? -0.950  -12.812 5.558   1.00 20.42 ? 23  SER   A OG  1 
ATOM   92   N  N   . PRO   A 1 24  ? -1.168  -10.138 3.412   1.00 13.53 ? 24  PRO   A N   1 
ATOM   93   C  CA  . PRO   A 1 24  ? -2.533  -9.635  3.248   1.00 14.87 ? 24  PRO   A CA  1 
ATOM   94   C  C   . PRO   A 1 24  ? -3.506  -10.510 3.950   1.00 14.35 ? 24  PRO   A C   1 
ATOM   95   O  O   . PRO   A 1 24  ? -3.320  -11.739 4.019   1.00 16.18 ? 24  PRO   A O   1 
ATOM   96   C  CB  . PRO   A 1 24  ? -2.761  -9.694  1.748   1.00 17.47 ? 24  PRO   A CB  1 
ATOM   97   C  CG  . PRO   A 1 24  ? -1.476  -9.960  1.205   1.00 26.66 ? 24  PRO   A CG  1 
ATOM   98   C  CD  . PRO   A 1 24  ? -0.494  -10.407 2.149   1.00 15.71 ? 24  PRO   A CD  1 
ATOM   99   N  N   . ALA   A 1 25  ? -4.599  -9.935  4.459   1.00 13.41 ? 25  ALA   A N   1 
ATOM   100  C  CA  . ALA   A 1 25  ? -5.710  -10.693 5.026   1.00 13.27 ? 25  ALA   A CA  1 
ATOM   101  C  C   . ALA   A 1 25  ? -6.710  -10.827 3.883   1.00 13.52 ? 25  ALA   A C   1 
ATOM   102  O  O   . ALA   A 1 25  ? -7.368  -9.847  3.504   1.00 14.36 ? 25  ALA   A O   1 
ATOM   103  C  CB  . ALA   A 1 25  ? -6.298  -9.970  6.226   1.00 14.01 ? 25  ALA   A CB  1 
ATOM   104  N  N   . ILE   A 1 26  ? -6.808  -12.020 3.300   1.00 14.63 ? 26  ILE   A N   1 
ATOM   105  C  CA  A ILE   A 1 26  ? -7.583  -12.291 2.115   0.50 14.43 ? 26  ILE   A CA  1 
ATOM   106  C  CA  B ILE   A 1 26  ? -7.615  -12.210 2.136   0.50 15.32 ? 26  ILE   A CA  1 
ATOM   107  C  C   . ILE   A 1 26  ? -9.038  -12.681 2.456   1.00 16.81 ? 26  ILE   A C   1 
ATOM   108  O  O   . ILE   A 1 26  ? -9.245  -13.331 3.462   1.00 17.31 ? 26  ILE   A O   1 
ATOM   109  C  CB  A ILE   A 1 26  ? -6.890  -13.400 1.233   0.50 17.82 ? 26  ILE   A CB  1 
ATOM   110  C  CB  B ILE   A 1 26  ? -6.939  -13.194 1.177   0.50 18.69 ? 26  ILE   A CB  1 
ATOM   111  C  CG1 A ILE   A 1 26  ? -5.487  -12.938 0.823   0.50 19.90 ? 26  ILE   A CG1 1 
ATOM   112  C  CG1 B ILE   A 1 26  ? -6.991  -14.597 1.733   0.50 20.24 ? 26  ILE   A CG1 1 
ATOM   113  C  CG2 A ILE   A 1 26  ? -7.733  -13.731 0.008   0.50 20.63 ? 26  ILE   A CG2 1 
ATOM   114  C  CG2 B ILE   A 1 26  ? -5.480  -12.822 1.022   0.50 18.75 ? 26  ILE   A CG2 1 
ATOM   115  C  CD1 A ILE   A 1 26  ? -4.608  -14.035 0.267   0.50 24.40 ? 26  ILE   A CD1 1 
ATOM   116  C  CD1 B ILE   A 1 26  ? -6.677  -15.575 0.635   0.50 28.70 ? 26  ILE   A CD1 1 
ATOM   117  N  N   . ASN   A 1 27  ? -10.015 -12.319 1.618   1.00 16.24 ? 27  ASN   A N   1 
ATOM   118  C  CA  A ASN   A 1 27  ? -11.403 -12.795 1.814   0.50 17.62 ? 27  ASN   A CA  1 
ATOM   119  C  CA  B ASN   A 1 27  ? -11.380 -12.770 1.802   0.50 17.41 ? 27  ASN   A CA  1 
ATOM   120  C  C   . ASN   A 1 27  ? -12.028 -12.305 3.073   1.00 14.79 ? 27  ASN   A C   1 
ATOM   121  O  O   . ASN   A 1 27  ? -12.894 -12.931 3.609   1.00 17.76 ? 27  ASN   A O   1 
ATOM   122  C  CB  A ASN   A 1 27  ? -11.608 -14.319 1.658   0.50 19.06 ? 27  ASN   A CB  1 
ATOM   123  C  CB  B ASN   A 1 27  ? -11.479 -14.268 1.662   0.50 21.34 ? 27  ASN   A CB  1 
ATOM   124  C  CG  A ASN   A 1 27  ? -13.028 -14.670 1.168   0.50 19.98 ? 27  ASN   A CG  1 
ATOM   125  C  CG  B ASN   A 1 27  ? -11.031 -14.744 0.303   0.50 26.64 ? 27  ASN   A CG  1 
ATOM   126  O  OD1 A ASN   A 1 27  ? -13.610 -13.885 0.394   0.50 26.00 ? 27  ASN   A OD1 1 
ATOM   127  O  OD1 B ASN   A 1 27  ? -11.260 -14.087 -0.720  0.50 29.02 ? 27  ASN   A OD1 1 
ATOM   128  N  ND2 A ASN   A 1 27  ? -13.537 -15.830 1.598   0.50 29.47 ? 27  ASN   A ND2 1 
ATOM   129  N  ND2 B ASN   A 1 27  ? -10.371 -15.906 0.294   0.50 28.97 ? 27  ASN   A ND2 1 
ATOM   130  N  N   . VAL   A 1 28  ? -11.641 -11.111 3.533   1.00 15.21 ? 28  VAL   A N   1 
ATOM   131  C  CA  . VAL   A 1 28  ? -12.235 -10.454 4.684   1.00 13.76 ? 28  VAL   A CA  1 
ATOM   132  C  C   . VAL   A 1 28  ? -13.448 -9.699  4.249   1.00 13.05 ? 28  VAL   A C   1 
ATOM   133  O  O   . VAL   A 1 28  ? -13.332 -8.854  3.381   1.00 14.14 ? 28  VAL   A O   1 
ATOM   134  C  CB  . VAL   A 1 28  ? -11.227 -9.568  5.436   1.00 13.83 ? 28  VAL   A CB  1 
ATOM   135  C  CG1 . VAL   A 1 28  ? -11.894 -8.913  6.609   1.00 15.22 ? 28  VAL   A CG1 1 
ATOM   136  C  CG2 . VAL   A 1 28  ? -10.012 -10.378 5.903   1.00 15.80 ? 28  VAL   A CG2 1 
ATOM   137  N  N   . ALA   A 1 29  ? -14.600 -9.933  4.893   1.00 13.94 ? 29  ALA   A N   1 
ATOM   138  C  CA  . ALA   A 1 29  ? -15.828 -9.232  4.549   1.00 13.21 ? 29  ALA   A CA  1 
ATOM   139  C  C   . ALA   A 1 29  ? -15.760 -7.795  5.133   1.00 13.04 ? 29  ALA   A C   1 
ATOM   140  O  O   . ALA   A 1 29  ? -15.343 -7.639  6.267   1.00 13.99 ? 29  ALA   A O   1 
ATOM   141  C  CB  . ALA   A 1 29  ? -17.054 -9.943  5.093   1.00 15.35 ? 29  ALA   A CB  1 
ATOM   142  N  N   . VAL   A 1 30  ? -16.225 -6.839  4.368   1.00 12.73 ? 30  VAL   A N   1 
ATOM   143  C  CA  . VAL   A 1 30  ? -16.257 -5.413  4.743   1.00 12.03 ? 30  VAL   A CA  1 
ATOM   144  C  C   . VAL   A 1 30  ? -17.635 -4.884  4.362   1.00 12.69 ? 30  VAL   A C   1 
ATOM   145  O  O   . VAL   A 1 30  ? -18.066 -4.998  3.242   1.00 13.92 ? 30  VAL   A O   1 
ATOM   146  C  CB  . VAL   A 1 30  ? -15.159 -4.648  4.015   1.00 13.58 ? 30  VAL   A CB  1 
ATOM   147  C  CG1 . VAL   A 1 30  ? -15.190 -3.168  4.392   1.00 15.70 ? 30  VAL   A CG1 1 
ATOM   148  C  CG2 . VAL   A 1 30  ? -13.747 -5.244  4.296   1.00 15.16 ? 30  VAL   A CG2 1 
ATOM   149  N  N   . HIS   A 1 31  ? -18.248 -4.218  5.330   1.00 13.00 ? 31  HIS   A N   1 
ATOM   150  C  CA  . HIS   A 1 31  ? -19.548 -3.554  5.112   1.00 12.99 ? 31  HIS   A CA  1 
ATOM   151  C  C   . HIS   A 1 31  ? -19.416 -2.092  5.449   1.00 13.73 ? 31  HIS   A C   1 
ATOM   152  O  O   . HIS   A 1 31  ? -18.841 -1.747  6.481   1.00 16.09 ? 31  HIS   A O   1 
ATOM   153  C  CB  . HIS   A 1 31  ? -20.633 -4.174  5.974   1.00 15.85 ? 31  HIS   A CB  1 
ATOM   154  C  CG  . HIS   A 1 31  ? -20.943 -5.601  5.563   1.00 17.39 ? 31  HIS   A CG  1 
ATOM   155  N  ND1 . HIS   A 1 31  ? -22.064 -5.924  4.839   1.00 20.77 ? 31  HIS   A ND1 1 
ATOM   156  C  CD2 . HIS   A 1 31  ? -20.305 -6.730  5.796   1.00 18.39 ? 31  HIS   A CD2 1 
ATOM   157  C  CE1 . HIS   A 1 31  ? -22.056 -7.232  4.649   1.00 23.74 ? 31  HIS   A CE1 1 
ATOM   158  N  NE2 . HIS   A 1 31  ? -20.998 -7.730  5.233   1.00 20.75 ? 31  HIS   A NE2 1 
ATOM   159  N  N   . VAL   A 1 32  ? -19.897 -1.224  4.572   1.00 13.06 ? 32  VAL   A N   1 
ATOM   160  C  CA  . VAL   A 1 32  ? -19.833 0.191   4.774   1.00 12.57 ? 32  VAL   A CA  1 
ATOM   161  C  C   . VAL   A 1 32  ? -21.254 0.735   4.941   1.00 13.68 ? 32  VAL   A C   1 
ATOM   162  O  O   . VAL   A 1 32  ? -22.151 0.301   4.195   1.00 14.02 ? 32  VAL   A O   1 
ATOM   163  C  CB  . VAL   A 1 32  ? -19.169 0.897   3.575   1.00 13.77 ? 32  VAL   A CB  1 
ATOM   164  C  CG1 . VAL   A 1 32  ? -18.967 2.423   3.854   1.00 15.51 ? 32  VAL   A CG1 1 
ATOM   165  C  CG2 . VAL   A 1 32  ? -17.801 0.272   3.280   1.00 15.60 ? 32  VAL   A CG2 1 
ATOM   166  N  N   . PHE   A 1 33  ? -21.450 1.646   5.882   1.00 13.93 ? 33  PHE   A N   1 
ATOM   167  C  CA  . PHE   A 1 33  ? -22.740 2.256   6.201   1.00 14.44 ? 33  PHE   A CA  1 
ATOM   168  C  C   . PHE   A 1 33  ? -22.584 3.765   6.181   1.00 14.48 ? 33  PHE   A C   1 
ATOM   169  O  O   . PHE   A 1 33  ? -21.463 4.276   6.411   1.00 15.01 ? 33  PHE   A O   1 
ATOM   170  C  CB  . PHE   A 1 33  ? -23.235 1.813   7.573   1.00 16.21 ? 33  PHE   A CB  1 
ATOM   171  C  CG  . PHE   A 1 33  ? -23.311 0.311   7.737   1.00 17.94 ? 33  PHE   A CG  1 
ATOM   172  C  CD1 . PHE   A 1 33  ? -22.186 -0.405  8.095   1.00 18.17 ? 33  PHE   A CD1 1 
ATOM   173  C  CD2 . PHE   A 1 33  ? -24.516 -0.361  7.514   1.00 21.08 ? 33  PHE   A CD2 1 
ATOM   174  C  CE1 . PHE   A 1 33  ? -22.206 -1.802  8.225   1.00 21.56 ? 33  PHE   A CE1 1 
ATOM   175  C  CE2 . PHE   A 1 33  ? -24.518 -1.740  7.603   1.00 23.84 ? 33  PHE   A CE2 1 
ATOM   176  C  CZ  . PHE   A 1 33  ? -23.390 -2.444  7.944   1.00 22.42 ? 33  PHE   A CZ  1 
ATOM   177  N  N   . ARG   A 1 34  ? -23.656 4.499   5.956   1.00 17.04 ? 34  ARG   A N   1 
ATOM   178  C  CA  . ARG   A 1 34  ? -23.634 5.970   6.043   1.00 17.26 ? 34  ARG   A CA  1 
ATOM   179  C  C   . ARG   A 1 34  ? -24.742 6.350   7.014   1.00 19.73 ? 34  ARG   A C   1 
ATOM   180  O  O   . ARG   A 1 34  ? -25.867 5.845   6.914   1.00 24.85 ? 34  ARG   A O   1 
ATOM   181  C  CB  . ARG   A 1 34  ? -23.936 6.535   4.654   1.00 20.56 ? 34  ARG   A CB  1 
ATOM   182  C  CG  . ARG   A 1 34  ? -23.832 8.091   4.575   1.00 22.80 ? 34  ARG   A CG  1 
ATOM   183  C  CD  . ARG   A 1 34  ? -24.061 8.741   3.190   0.50 16.66 ? 34  ARG   A CD  1 
ATOM   184  N  NE  . ARG   A 1 34  ? -23.991 10.196  3.264   0.50 17.49 ? 34  ARG   A NE  1 
ATOM   185  C  CZ  . ARG   A 1 34  ? -25.024 10.959  3.601   0.50 17.10 ? 34  ARG   A CZ  1 
ATOM   186  N  NH1 . ARG   A 1 34  ? -26.181 10.476  3.871   0.50 16.94 ? 34  ARG   A NH1 1 
ATOM   187  N  NH2 . ARG   A 1 34  ? -24.863 12.245  3.687   0.50 15.50 ? 34  ARG   A NH2 1 
ATOM   188  N  N   . LYS   A 1 35  ? -24.467 7.305   7.879   1.00 20.50 ? 35  LYS   A N   1 
ATOM   189  C  CA  . LYS   A 1 35  ? -25.477 7.796   8.746   1.00 25.11 ? 35  LYS   A CA  1 
ATOM   190  C  C   . LYS   A 1 35  ? -26.503 8.771   8.045   1.00 23.15 ? 35  LYS   A C   1 
ATOM   191  O  O   . LYS   A 1 35  ? -26.154 9.667   7.299   1.00 27.94 ? 35  LYS   A O   1 
ATOM   192  C  CB  . LYS   A 1 35  ? -24.767 8.582   9.886   1.00 26.54 ? 35  LYS   A CB  1 
ATOM   193  C  CG  . LYS   A 1 35  ? -25.597 8.646   11.152  1.00 32.98 ? 35  LYS   A CG  1 
ATOM   194  C  CD  . LYS   A 1 35  ? -24.908 9.499   12.196  0.50 24.90 ? 35  LYS   A CD  1 
ATOM   195  C  CE  . LYS   A 1 35  ? -24.081 8.708   13.167  0.50 29.18 ? 35  LYS   A CE  1 
ATOM   196  N  NZ  . LYS   A 1 35  ? -24.316 9.158   14.564  0.50 37.81 ? 35  LYS   A NZ  1 
ATOM   197  N  N   . ALA   A 1 36  ? -27.774 8.418   8.082   1.00 25.90 ? 36  ALA   A N   1 
ATOM   198  C  CA  . ALA   A 1 36  ? -28.842 9.178   7.443   1.00 27.03 ? 36  ALA   A CA  1 
ATOM   199  C  C   . ALA   A 1 36  ? -29.229 10.378  8.290   1.00 27.75 ? 36  ALA   A C   1 
ATOM   200  O  O   . ALA   A 1 36  ? -28.840 10.497  9.456   1.00 27.88 ? 36  ALA   A O   1 
ATOM   201  N  N   . ALA   A 1 37  ? -30.085 11.243  7.741   1.00 37.51 ? 37  ALA   A N   1 
ATOM   202  C  CA  . ALA   A 1 37  ? -30.444 12.463  8.456   1.00 40.85 ? 37  ALA   A CA  1 
ATOM   203  C  C   . ALA   A 1 37  ? -31.346 12.107  9.672   1.00 37.34 ? 37  ALA   A C   1 
ATOM   204  O  O   . ALA   A 1 37  ? -31.447 12.877  10.612  1.00 44.78 ? 37  ALA   A O   1 
ATOM   205  N  N   . ASP   A 1 38  ? -31.881 10.883  9.667   0.70 36.33 ? 38  ASP   A N   1 
ATOM   206  C  CA  . ASP   A 1 38  ? -32.613 10.349  10.816  0.70 37.04 ? 38  ASP   A CA  1 
ATOM   207  C  C   . ASP   A 1 38  ? -31.668 9.732   11.882  0.70 27.02 ? 38  ASP   A C   1 
ATOM   208  O  O   . ASP   A 1 38  ? -32.173 9.175   12.862  0.70 37.16 ? 38  ASP   A O   1 
ATOM   209  C  CB  . ASP   A 1 38  ? -33.664 9.302   10.351  0.70 43.26 ? 38  ASP   A CB  1 
ATOM   210  N  N   . ASP   A 1 39  ? -30.324 9.764   11.721  1.00 36.52 ? 39  ASP   A N   1 
ATOM   211  C  CA  . ASP   A 1 39  ? -29.415 9.094   12.674  1.00 46.82 ? 39  ASP   A CA  1 
ATOM   212  C  C   . ASP   A 1 39  ? -29.128 7.592   12.529  1.00 42.35 ? 39  ASP   A C   1 
ATOM   213  N  N   . THR   A 1 40  ? -29.949 6.911   11.726  0.50 28.37 ? 40  THR   A N   1 
ATOM   214  C  CA  . THR   A 1 40  ? -29.797 5.465   11.567  0.50 26.09 ? 40  THR   A CA  1 
ATOM   215  C  C   . THR   A 1 40  ? -28.596 5.169   10.621  0.50 37.58 ? 40  THR   A C   1 
ATOM   216  O  O   . THR   A 1 40  ? -28.268 6.019   9.819   0.50 29.19 ? 40  THR   A O   1 
ATOM   217  C  CB  . THR   A 1 40  ? -31.105 4.799   11.021  0.50 28.23 ? 40  THR   A CB  1 
ATOM   218  O  OG1 . THR   A 1 40  ? -31.278 5.198   9.662   0.50 32.52 ? 40  THR   A OG1 1 
ATOM   219  C  CG2 . THR   A 1 40  ? -32.313 5.312   11.733  0.50 25.75 ? 40  THR   A CG2 1 
ATOM   220  N  N   . TRP   A 1 41  ? -27.967 3.993   10.762  0.90 61.10 ? 41  TRP   A N   1 
ATOM   221  C  CA  . TRP   A 1 41  ? -26.934 3.488   9.787   0.90 33.79 ? 41  TRP   A CA  1 
ATOM   222  C  C   . TRP   A 1 41  ? -27.473 2.782   8.540   0.90 31.17 ? 41  TRP   A C   1 
ATOM   223  O  O   . TRP   A 1 41  ? -28.016 1.654   8.616   0.90 43.96 ? 41  TRP   A O   1 
ATOM   224  C  CB  . TRP   A 1 41  ? -25.990 2.472   10.440  0.90 31.19 ? 41  TRP   A CB  1 
ATOM   225  C  CG  . TRP   A 1 41  ? -25.110 3.080   11.448  0.90 32.45 ? 41  TRP   A CG  1 
ATOM   226  C  CD1 . TRP   A 1 41  ? -25.171 2.939   12.813  0.90 36.89 ? 41  TRP   A CD1 1 
ATOM   227  C  CD2 . TRP   A 1 41  ? -24.082 4.078   11.208  0.90 25.95 ? 41  TRP   A CD2 1 
ATOM   228  N  NE1 . TRP   A 1 41  ? -24.231 3.699   13.436  0.90 39.70 ? 41  TRP   A NE1 1 
ATOM   229  C  CE2 . TRP   A 1 41  ? -23.539 4.419   12.522  0.90 34.95 ? 41  TRP   A CE2 1 
ATOM   230  C  CE3 . TRP   A 1 41  ? -23.502 4.642   10.057  0.90 22.46 ? 41  TRP   A CE3 1 
ATOM   231  C  CZ2 . TRP   A 1 41  ? -22.484 5.324   12.678  0.90 31.15 ? 41  TRP   A CZ2 1 
ATOM   232  C  CZ3 . TRP   A 1 41  ? -22.477 5.562   10.245  0.90 22.98 ? 41  TRP   A CZ3 1 
ATOM   233  C  CH2 . TRP   A 1 41  ? -21.966 5.884   11.533  0.90 25.90 ? 41  TRP   A CH2 1 
ATOM   234  N  N   . GLU   A 1 42  ? -27.372 3.450   7.394   1.00 25.97 ? 42  GLU   A N   1 
ATOM   235  C  CA  . GLU   A 1 42  ? -27.932 2.994   6.163   1.00 24.75 ? 42  GLU   A CA  1 
ATOM   236  C  C   . GLU   A 1 42  ? -26.845 2.172   5.426   1.00 22.90 ? 42  GLU   A C   1 
ATOM   237  O  O   . GLU   A 1 42  ? -25.746 2.638   5.232   1.00 20.84 ? 42  GLU   A O   1 
ATOM   238  C  CB  . GLU   A 1 42  ? -28.308 4.155   5.234   1.00 28.00 ? 42  GLU   A CB  1 
ATOM   239  N  N   . PRO   A 1 43  ? -27.121 0.916   5.022   1.00 22.91 ? 43  PRO   A N   1 
ATOM   240  C  CA  . PRO   A 1 43  ? -26.133 0.191   4.279   1.00 20.11 ? 43  PRO   A CA  1 
ATOM   241  C  C   . PRO   A 1 43  ? -25.764 1.015   3.043   1.00 19.73 ? 43  PRO   A C   1 
ATOM   242  O  O   . PRO   A 1 43  ? -26.586 1.572   2.396   1.00 25.53 ? 43  PRO   A O   1 
ATOM   243  C  CB  . PRO   A 1 43  ? -26.880 -1.060  3.876   1.00 23.37 ? 43  PRO   A CB  1 
ATOM   244  C  CG  . PRO   A 1 43  ? -27.935 -1.247  4.896   1.00 38.42 ? 43  PRO   A CG  1 
ATOM   245  C  CD  . PRO   A 1 43  ? -28.360 0.143   5.224   1.00 25.96 ? 43  PRO   A CD  1 
ATOM   246  N  N   . PHE   A 1 44  ? -24.448 1.058   2.766   1.00 18.60 ? 44  PHE   A N   1 
ATOM   247  C  CA  . PHE   A 1 44  ? -23.862 1.888   1.690   1.00 18.18 ? 44  PHE   A CA  1 
ATOM   248  C  C   . PHE   A 1 44  ? -23.089 1.067   0.642   1.00 16.39 ? 44  PHE   A C   1 
ATOM   249  O  O   . PHE   A 1 44  ? -23.279 1.294   -0.542  1.00 20.22 ? 44  PHE   A O   1 
ATOM   250  C  CB  . PHE   A 1 44  ? -22.979 3.020   2.330   1.00 17.90 ? 44  PHE   A CB  1 
ATOM   251  C  CG  . PHE   A 1 44  ? -22.406 3.958   1.323   1.00 17.51 ? 44  PHE   A CG  1 
ATOM   252  C  CD1 . PHE   A 1 44  ? -23.179 4.993   0.817   1.00 21.59 ? 44  PHE   A CD1 1 
ATOM   253  C  CD2 . PHE   A 1 44  ? -21.099 3.879   0.899   1.00 17.78 ? 44  PHE   A CD2 1 
ATOM   254  C  CE1 . PHE   A 1 44  ? -22.641 5.880   -0.086  1.00 22.85 ? 44  PHE   A CE1 1 
ATOM   255  C  CE2 . PHE   A 1 44  ? -20.530 4.732   0.010   1.00 22.72 ? 44  PHE   A CE2 1 
ATOM   256  C  CZ  . PHE   A 1 44  ? -21.335 5.726   -0.513  1.00 23.14 ? 44  PHE   A CZ  1 
ATOM   257  N  N   . ALA   A 1 45  ? -22.266 0.147   1.070   1.00 16.36 ? 45  ALA   A N   1 
ATOM   258  C  CA  . ALA   A 1 45  ? -21.520 -0.712  0.106   1.00 15.96 ? 45  ALA   A CA  1 
ATOM   259  C  C   . ALA   A 1 45  ? -20.992 -1.920  0.888   1.00 14.19 ? 45  ALA   A C   1 
ATOM   260  O  O   . ALA   A 1 45  ? -20.861 -1.850  2.083   1.00 15.49 ? 45  ALA   A O   1 
ATOM   261  C  CB  . ALA   A 1 45  ? -20.382 0.060   -0.485  1.00 18.13 ? 45  ALA   A CB  1 
ATOM   262  N  N   . SER   A 1 46  ? -20.637 -2.994  0.200   1.00 13.94 ? 46  SER   A N   1 
ATOM   263  C  CA  . SER   A 1 46  ? -19.911 -4.102  0.849   1.00 13.55 ? 46  SER   A CA  1 
ATOM   264  C  C   . SER   A 1 46  ? -19.053 -4.803  -0.152  1.00 14.14 ? 46  SER   A C   1 
ATOM   265  O  O   . SER   A 1 46  ? -19.213 -4.663  -1.353  1.00 15.23 ? 46  SER   A O   1 
ATOM   266  C  CB  . SER   A 1 46  ? -20.893 -5.012  1.542   1.00 14.52 ? 46  SER   A CB  1 
ATOM   267  O  OG  . SER   A 1 46  ? -21.692 -5.708  0.621   1.00 16.36 ? 46  SER   A OG  1 
ATOM   268  N  N   . GLY   A 1 47  ? -18.134 -5.626  0.347   1.00 13.73 ? 47  GLY   A N   1 
ATOM   269  C  CA  . GLY   A 1 47  ? -17.311 -6.429  -0.482  1.00 14.57 ? 47  GLY   A CA  1 
ATOM   270  C  C   . GLY   A 1 47  ? -16.371 -7.274  0.332   1.00 12.99 ? 47  GLY   A C   1 
ATOM   271  O  O   . GLY   A 1 47  ? -16.515 -7.301  1.514   1.00 14.42 ? 47  GLY   A O   1 
ATOM   272  N  N   . LYS   A 1 48  ? -15.418 -7.888  -0.343  1.00 14.39 ? 48  LYS   A N   1 
ATOM   273  C  CA  . LYS   A 1 48  ? -14.409 -8.691  0.385   1.00 16.17 ? 48  LYS   A CA  1 
ATOM   274  C  C   . LYS   A 1 48  ? -13.014 -8.365  -0.142  1.00 14.18 ? 48  LYS   A C   1 
ATOM   275  O  O   . LYS   A 1 48  ? -12.862 -8.054  -1.309  1.00 16.50 ? 48  LYS   A O   1 
ATOM   276  C  CB  . LYS   A 1 48  ? -14.710 -10.184 0.269   1.00 24.82 ? 48  LYS   A CB  1 
ATOM   277  C  CG  . LYS   A 1 48  ? -14.824 -10.715 -1.149  1.00 21.27 ? 48  LYS   A CG  1 
ATOM   278  N  N   . THR   A 1 49  ? -12.046 -8.496  0.761   1.00 13.64 ? 49  THR   A N   1 
ATOM   279  C  CA  . THR   A 1 49  ? -10.675 -8.203  0.348   1.00 13.09 ? 49  THR   A CA  1 
ATOM   280  C  C   . THR   A 1 49  ? -10.176 -9.258  -0.652  1.00 14.36 ? 49  THR   A C   1 
ATOM   281  O  O   . THR   A 1 49  ? -10.473 -10.416 -0.568  1.00 19.49 ? 49  THR   A O   1 
ATOM   282  C  CB  . THR   A 1 49  ? -9.705  -8.074  1.521   1.00 13.19 ? 49  THR   A CB  1 
ATOM   283  O  OG1 . THR   A 1 49  ? -9.702  -9.325  2.225   1.00 13.64 ? 49  THR   A OG1 1 
ATOM   284  C  CG2 . THR   A 1 49  ? -10.082 -6.954  2.420   1.00 14.37 ? 49  THR   A CG2 1 
ATOM   285  N  N   . SER   A 1 50  ? -9.389  -8.785  -1.624  1.00 16.40 ? 50  SER   A N   1 
ATOM   286  C  CA  . SER   A 1 50  ? -8.745  -9.609  -2.671  1.00 19.76 ? 50  SER   A CA  1 
ATOM   287  C  C   . SER   A 1 50  ? -7.515  -10.298 -2.113  1.00 19.34 ? 50  SER   A C   1 
ATOM   288  O  O   . SER   A 1 50  ? -7.162  -10.197 -0.954  1.00 18.23 ? 50  SER   A O   1 
ATOM   289  C  CB  . SER   A 1 50  ? -8.289  -8.663  -3.795  1.00 25.57 ? 50  SER   A CB  1 
ATOM   290  O  OG  . SER   A 1 50  ? -7.189  -7.850  -3.286  1.00 24.60 ? 50  SER   A OG  1 
ATOM   291  N  N   . GLU   A 1 51  ? -6.807  -10.983 -2.994  1.00 20.70 ? 51  GLU   A N   1 
ATOM   292  C  CA  . GLU   A 1 51  ? -5.564  -11.617 -2.663  1.00 21.38 ? 51  GLU   A CA  1 
ATOM   293  C  C   . GLU   A 1 51  ? -4.497  -10.692 -2.218  1.00 20.48 ? 51  GLU   A C   1 
ATOM   294  O  O   . GLU   A 1 51  ? -3.596  -11.073 -1.546  1.00 21.90 ? 51  GLU   A O   1 
ATOM   295  C  CB  . GLU   A 1 51  ? -5.076  -12.496 -3.851  1.00 29.39 ? 51  GLU   A CB  1 
ATOM   296  N  N   . SER   A 1 52  ? -4.562  -9.400  -2.556  1.00 20.82 ? 52  SER   A N   1 
ATOM   297  C  CA  . SER   A 1 52  ? -3.654  -8.379  -2.020  1.00 20.02 ? 52  SER   A CA  1 
ATOM   298  C  C   . SER   A 1 52  ? -4.120  -7.762  -0.756  1.00 17.05 ? 52  SER   A C   1 
ATOM   299  O  O   . SER   A 1 52  ? -3.483  -6.863  -0.237  1.00 17.89 ? 52  SER   A O   1 
ATOM   300  C  CB  . SER   A 1 52  ? -3.535  -7.255  -3.048  1.00 24.15 ? 52  SER   A CB  1 
ATOM   301  O  OG  . SER   A 1 52  ? -4.761  -6.587  -3.230  1.00 33.03 ? 52  SER   A OG  1 
ATOM   302  N  N   . GLY   A 1 53  ? -5.240  -8.223  -0.203  1.00 15.57 ? 53  GLY   A N   1 
ATOM   303  C  CA  . GLY   A 1 53  ? -5.792  -7.655  1.019   1.00 14.60 ? 53  GLY   A CA  1 
ATOM   304  C  C   . GLY   A 1 53  ? -6.539  -6.344  0.839   1.00 13.43 ? 53  GLY   A C   1 
ATOM   305  O  O   . GLY   A 1 53  ? -6.900  -5.720  1.783   1.00 14.98 ? 53  GLY   A O   1 
ATOM   306  N  N   . GLU   A 1 54  ? -6.837  -6.004  -0.404  1.00 14.93 ? 54  GLU   A N   1 
ATOM   307  C  CA  . GLU   A 1 54  ? -7.456  -4.741  -0.753  1.00 14.31 ? 54  GLU   A CA  1 
ATOM   308  C  C   . GLU   A 1 54  ? -8.846  -4.929  -1.293  1.00 14.03 ? 54  GLU   A C   1 
ATOM   309  O  O   . GLU   A 1 54  ? -9.215  -5.933  -1.878  1.00 16.62 ? 54  GLU   A O   1 
ATOM   310  C  CB  . GLU   A 1 54  ? -6.617  -4.018  -1.816  1.00 18.15 ? 54  GLU   A CB  1 
ATOM   311  C  CG  . GLU   A 1 54  ? -5.198  -3.656  -1.335  1.00 22.53 ? 54  GLU   A CG  1 
ATOM   312  C  CD  . GLU   A 1 54  ? -4.375  -2.759  -2.213  0.50 22.60 ? 54  GLU   A CD  1 
ATOM   313  O  OE1 . GLU   A 1 54  ? -4.760  -2.520  -3.330  0.50 33.31 ? 54  GLU   A OE1 1 
ATOM   314  O  OE2 . GLU   A 1 54  ? -3.284  -2.396  -1.798  0.50 30.29 ? 54  GLU   A OE2 1 
ATOM   315  N  N   . LEU   A 1 55  ? -9.663  -3.930  -1.002  1.00 14.19 ? 55  LEU   A N   1 
ATOM   316  C  CA  . LEU   A 1 55  ? -10.998 -3.852  -1.531  1.00 13.95 ? 55  LEU   A CA  1 
ATOM   317  C  C   . LEU   A 1 55  ? -11.202 -2.467  -2.141  1.00 14.92 ? 55  LEU   A C   1 
ATOM   318  O  O   . LEU   A 1 55  ? -11.182 -1.439  -1.456  1.00 16.29 ? 55  LEU   A O   1 
ATOM   319  C  CB  . LEU   A 1 55  ? -11.976 -4.097  -0.403  1.00 14.45 ? 55  LEU   A CB  1 
ATOM   320  C  CG  . LEU   A 1 55  ? -13.467 -3.906  -0.701  1.00 15.02 ? 55  LEU   A CG  1 
ATOM   321  C  CD1 . LEU   A 1 55  ? -13.938 -4.681  -1.922  1.00 16.94 ? 55  LEU   A CD1 1 
ATOM   322  C  CD2 . LEU   A 1 55  ? -14.285 -4.247  0.532   1.00 15.96 ? 55  LEU   A CD2 1 
ATOM   323  N  N   . HIS   A 1 56  ? -11.396 -2.462  -3.471  1.00 18.24 ? 56  HIS   A N   1 
ATOM   324  C  CA  . HIS   A 1 56  ? -11.589 -1.310  -4.297  1.00 21.67 ? 56  HIS   A CA  1 
ATOM   325  C  C   . HIS   A 1 56  ? -12.998 -1.321  -4.836  1.00 21.89 ? 56  HIS   A C   1 
ATOM   326  O  O   . HIS   A 1 56  ? -13.701 -2.291  -4.710  1.00 23.96 ? 56  HIS   A O   1 
ATOM   327  C  CB  . HIS   A 1 56  ? -10.665 -1.417  -5.526  1.00 28.14 ? 56  HIS   A CB  1 
ATOM   328  C  CG  . HIS   A 1 56  ? -9.241  -1.356  -5.187  1.00 28.53 ? 56  HIS   A CG  1 
ATOM   329  N  ND1 . HIS   A 1 56  ? -8.473  -2.428  -5.056  1.00 43.04 ? 56  HIS   A ND1 1 
ATOM   330  C  CD2 . HIS   A 1 56  ? -8.403  -0.245  -5.094  1.00 32.27 ? 56  HIS   A CD2 1 
ATOM   331  C  CE1 . HIS   A 1 56  ? -7.198  -2.022  -4.853  1.00 37.45 ? 56  HIS   A CE1 1 
ATOM   332  N  NE2 . HIS   A 1 56  ? -7.173  -0.696  -4.826  1.00 36.79 ? 56  HIS   A NE2 1 
ATOM   333  N  N   . GLY   A 1 57  ? -13.418 -0.237  -5.445  1.00 21.55 ? 57  GLY   A N   1 
ATOM   334  C  CA  . GLY   A 1 57  ? -14.676 -0.274  -6.182  1.00 23.23 ? 57  GLY   A CA  1 
ATOM   335  C  C   . GLY   A 1 57  ? -15.912 -0.132  -5.299  1.00 22.47 ? 57  GLY   A C   1 
ATOM   336  O  O   . GLY   A 1 57  ? -17.011 -0.389  -5.769  1.00 27.51 ? 57  GLY   A O   1 
ATOM   337  N  N   . LEU   A 1 58  ? -15.772 0.275   -4.044  1.00 20.50 ? 58  LEU   A N   1 
ATOM   338  C  CA  . LEU   A 1 58  ? -16.920 0.345   -3.163  1.00 18.15 ? 58  LEU   A CA  1 
ATOM   339  C  C   . LEU   A 1 58  ? -17.896 1.465   -3.573  1.00 20.19 ? 58  LEU   A C   1 
ATOM   340  O  O   . LEU   A 1 58  ? -19.111 1.323   -3.414  1.00 22.10 ? 58  LEU   A O   1 
ATOM   341  C  CB  . LEU   A 1 58  ? -16.484 0.553   -1.710  1.00 19.58 ? 58  LEU   A CB  1 
ATOM   342  C  CG  . LEU   A 1 58  ? -15.925 -0.705  -0.993  1.00 19.58 ? 58  LEU   A CG  1 
ATOM   343  C  CD1 . LEU   A 1 58  ? -15.160 -0.254  0.251   1.00 22.02 ? 58  LEU   A CD1 1 
ATOM   344  C  CD2 . LEU   A 1 58  ? -17.057 -1.675  -0.698  1.00 22.85 ? 58  LEU   A CD2 1 
ATOM   345  N  N   . THR   A 1 59  ? -17.385 2.579   -4.081  1.00 20.14 ? 59  THR   A N   1 
ATOM   346  C  CA  . THR   A 1 59  ? -18.227 3.752   -4.405  1.00 20.27 ? 59  THR   A CA  1 
ATOM   347  C  C   . THR   A 1 59  ? -17.604 4.553   -5.494  1.00 20.28 ? 59  THR   A C   1 
ATOM   348  O  O   . THR   A 1 59  ? -16.599 4.245   -6.002  1.00 22.81 ? 59  THR   A O   1 
ATOM   349  C  CB  . THR   A 1 59  ? -18.469 4.561   -3.094  1.00 19.37 ? 59  THR   A CB  1 
ATOM   350  O  OG1 . THR   A 1 59  ? -19.475 5.532   -3.331  1.00 21.32 ? 59  THR   A OG1 1 
ATOM   351  C  CG2 . THR   A 1 59  ? -17.258 5.234   -2.595  1.00 20.88 ? 59  THR   A CG2 1 
ATOM   352  N  N   . THR   A 1 60  ? -18.238 5.670   -5.787  1.00 23.43 ? 60  THR   A N   1 
ATOM   353  C  CA  . THR   A 1 60  ? -17.846 6.603   -6.846  1.00 23.70 ? 60  THR   A CA  1 
ATOM   354  C  C   . THR   A 1 60  ? -17.774 7.988   -6.222  1.00 20.77 ? 60  THR   A C   1 
ATOM   355  O  O   . THR   A 1 60  ? -18.385 8.256   -5.181  1.00 21.05 ? 60  THR   A O   1 
ATOM   356  C  CB  . THR   A 1 60  ? -18.821 6.628   -8.020  1.00 26.29 ? 60  THR   A CB  1 
ATOM   357  O  OG1 . THR   A 1 60  ? -20.058 7.166   -7.521  1.00 27.50 ? 60  THR   A OG1 1 
ATOM   358  C  CG2 . THR   A 1 60  ? -19.027 5.217   -8.562  1.00 34.50 ? 60  THR   A CG2 1 
ATOM   359  N  N   . GLU   A 1 61  ? -17.056 8.905   -6.876  1.00 26.83 ? 61  GLU   A N   1 
ATOM   360  C  CA  . GLU   A 1 61  ? -16.939 10.300  -6.396  1.00 32.00 ? 61  GLU   A CA  1 
ATOM   361  C  C   . GLU   A 1 61  ? -18.307 10.914  -6.230  1.00 27.76 ? 61  GLU   A C   1 
ATOM   362  O  O   . GLU   A 1 61  ? -18.555 11.668  -5.299  1.00 28.62 ? 61  GLU   A O   1 
ATOM   363  C  CB  . GLU   A 1 61  ? -16.072 11.181  -7.353  1.00 36.57 ? 61  GLU   A CB  1 
ATOM   364  N  N   . GLU   A 1 62  ? -19.212 10.642  -7.139  1.00 26.47 ? 62  GLU   A N   1 
ATOM   365  C  CA  . GLU   A 1 62  ? -20.512 11.284  -7.052  1.00 26.80 ? 62  GLU   A CA  1 
ATOM   366  C  C   . GLU   A 1 62  ? -21.373 10.720  -5.940  1.00 21.14 ? 62  GLU   A C   1 
ATOM   367  O  O   . GLU   A 1 62  ? -22.147 11.423  -5.303  1.00 22.02 ? 62  GLU   A O   1 
ATOM   368  C  CB  . GLU   A 1 62  ? -21.211 11.137  -8.359  1.00 33.38 ? 62  GLU   A CB  1 
ATOM   369  C  CG  . GLU   A 1 62  ? -22.275 12.188  -8.440  0.50 27.51 ? 62  GLU   A CG  1 
ATOM   370  C  CD  . GLU   A 1 62  ? -22.561 12.619  -9.852  0.50 23.62 ? 62  GLU   A CD  1 
ATOM   371  O  OE1 . GLU   A 1 62  ? -22.101 11.922  -10.816 0.50 23.22 ? 62  GLU   A OE1 1 
ATOM   372  O  OE2 . GLU   A 1 62  ? -23.213 13.682  -9.984  0.50 27.89 ? 62  GLU   A OE2 1 
ATOM   373  N  N   . GLU   A 1 63  ? -21.309 9.409   -5.681  1.00 18.60 ? 63  GLU   A N   1 
ATOM   374  C  CA  . GLU   A 1 63  ? -22.208 8.848   -4.631  1.00 18.08 ? 63  GLU   A CA  1 
ATOM   375  C  C   . GLU   A 1 63  ? -21.638 9.121   -3.239  1.00 16.98 ? 63  GLU   A C   1 
ATOM   376  O  O   . GLU   A 1 63  ? -22.397 9.178   -2.307  1.00 17.62 ? 63  GLU   A O   1 
ATOM   377  C  CB  . GLU   A 1 63  ? -22.339 7.325   -4.772  1.00 30.00 ? 63  GLU   A CB  1 
ATOM   378  N  N   . PHE   A 1 64  ? -20.319 9.299   -3.153  1.00 17.17 ? 64  PHE   A N   1 
ATOM   379  C  CA  . PHE   A 1 64  ? -19.639 9.390   -1.882  1.00 16.33 ? 64  PHE   A CA  1 
ATOM   380  C  C   . PHE   A 1 64  ? -19.691 10.835  -1.483  1.00 14.87 ? 64  PHE   A C   1 
ATOM   381  O  O   . PHE   A 1 64  ? -18.663 11.552  -1.442  1.00 19.31 ? 64  PHE   A O   1 
ATOM   382  C  CB  . PHE   A 1 64  ? -18.222 8.875   -2.040  1.00 16.77 ? 64  PHE   A CB  1 
ATOM   383  C  CG  . PHE   A 1 64  ? -17.445 8.662   -0.748  1.00 16.13 ? 64  PHE   A CG  1 
ATOM   384  C  CD1 . PHE   A 1 64  ? -17.979 8.109   0.388   1.00 19.03 ? 64  PHE   A CD1 1 
ATOM   385  C  CD2 . PHE   A 1 64  ? -16.143 9.039   -0.715  1.00 20.65 ? 64  PHE   A CD2 1 
ATOM   386  C  CE1 . PHE   A 1 64  ? -17.239 7.922   1.531   1.00 20.26 ? 64  PHE   A CE1 1 
ATOM   387  C  CE2 . PHE   A 1 64  ? -15.376 8.824   0.378   1.00 26.83 ? 64  PHE   A CE2 1 
ATOM   388  C  CZ  . PHE   A 1 64  ? -15.929 8.242   1.517   1.00 21.10 ? 64  PHE   A CZ  1 
ATOM   389  N  N   . VAL   A 1 65  ? -20.863 11.280  -1.066  1.00 17.43 ? 65  VAL   A N   1 
ATOM   390  C  CA  . VAL   A 1 65  ? -21.094 12.610  -0.557  1.00 16.38 ? 65  VAL   A CA  1 
ATOM   391  C  C   . VAL   A 1 65  ? -20.601 12.808  0.831   1.00 17.33 ? 65  VAL   A C   1 
ATOM   392  O  O   . VAL   A 1 65  ? -20.248 11.899  1.519   1.00 18.20 ? 65  VAL   A O   1 
ATOM   393  C  CB  . VAL   A 1 65  ? -22.592 13.014  -0.753  1.00 17.12 ? 65  VAL   A CB  1 
ATOM   394  C  CG1 . VAL   A 1 65  ? -22.976 12.970  -2.231  1.00 20.82 ? 65  VAL   A CG1 1 
ATOM   395  C  CG2 . VAL   A 1 65  ? -23.424 12.121  0.123   1.00 20.09 ? 65  VAL   A CG2 1 
ATOM   396  N  N   . GLU   A 1 66  ? -20.626 14.046  1.296   1.00 17.94 ? 66  GLU   A N   1 
ATOM   397  C  CA  . GLU   A 1 66  ? -20.352 14.325  2.703   1.00 17.50 ? 66  GLU   A CA  1 
ATOM   398  C  C   . GLU   A 1 66  ? -21.227 13.490  3.593   1.00 17.11 ? 66  GLU   A C   1 
ATOM   399  O  O   . GLU   A 1 66  ? -22.423 13.343  3.291   1.00 22.14 ? 66  GLU   A O   1 
ATOM   400  C  CB  . GLU   A 1 66  ? -20.633 15.817  3.094   1.00 21.67 ? 66  GLU   A CB  1 
ATOM   401  C  CG  . GLU   A 1 66  ? -19.949 16.902  2.387   0.50 21.94 ? 66  GLU   A CG  1 
ATOM   402  C  CD  . GLU   A 1 66  ? -20.229 18.208  3.097   0.50 20.85 ? 66  GLU   A CD  1 
ATOM   403  O  OE1 . GLU   A 1 66  ? -20.771 19.116  2.510   0.50 17.69 ? 66  GLU   A OE1 1 
ATOM   404  O  OE2 . GLU   A 1 66  ? -19.843 18.340  4.273   0.50 20.83 ? 66  GLU   A OE2 1 
ATOM   405  N  N   . GLY   A 1 67  ? -20.698 13.014  4.699   1.00 17.42 ? 67  GLY   A N   1 
ATOM   406  C  CA  . GLY   A 1 67  ? -21.457 12.296  5.636   1.00 19.27 ? 67  GLY   A CA  1 
ATOM   407  C  C   . GLY   A 1 67  ? -20.576 11.606  6.672   1.00 15.43 ? 67  GLY   A C   1 
ATOM   408  O  O   . GLY   A 1 67  ? -19.373 11.695  6.585   1.00 16.47 ? 67  GLY   A O   1 
ATOM   409  N  N   . ILE   A 1 68  ? -21.198 10.914  7.579   1.00 15.58 ? 68  ILE   A N   1 
ATOM   410  C  CA  . ILE   A 1 68  ? -20.493 10.094  8.550   1.00 13.83 ? 68  ILE   A CA  1 
ATOM   411  C  C   . ILE   A 1 68  ? -20.639 8.626   8.068   1.00 14.28 ? 68  ILE   A C   1 
ATOM   412  O  O   . ILE   A 1 68  ? -21.764 8.168   7.841   1.00 16.65 ? 68  ILE   A O   1 
ATOM   413  C  CB  . ILE   A 1 68  ? -21.051 10.225  9.993   1.00 16.15 ? 68  ILE   A CB  1 
ATOM   414  C  CG1 . ILE   A 1 68  ? -20.906 11.682  10.471  1.00 19.13 ? 68  ILE   A CG1 1 
ATOM   415  C  CG2 . ILE   A 1 68  ? -20.273 9.258   10.926  1.00 18.56 ? 68  ILE   A CG2 1 
ATOM   416  C  CD1 . ILE   A 1 68  ? -21.551 11.918  11.810  1.00 23.76 ? 68  ILE   A CD1 1 
ATOM   417  N  N   . TYR   A 1 69  ? -19.505 7.977   7.893   1.00 13.23 ? 69  TYR   A N   1 
ATOM   418  C  CA  . TYR   A 1 69  ? -19.418 6.644   7.352   1.00 13.25 ? 69  TYR   A CA  1 
ATOM   419  C  C   . TYR   A 1 69  ? -18.897 5.716   8.394   1.00 12.14 ? 69  TYR   A C   1 
ATOM   420  O  O   . TYR   A 1 69  ? -18.061 6.093   9.218   1.00 13.69 ? 69  TYR   A O   1 
ATOM   421  C  CB  . TYR   A 1 69  ? -18.603 6.636   6.061   1.00 13.42 ? 69  TYR   A CB  1 
ATOM   422  C  CG  . TYR   A 1 69  ? -19.272 7.345   4.926   1.00 14.22 ? 69  TYR   A CG  1 
ATOM   423  C  CD1 . TYR   A 1 69  ? -19.138 8.739   4.764   1.00 14.56 ? 69  TYR   A CD1 1 
ATOM   424  C  CD2 . TYR   A 1 69  ? -20.010 6.665   3.992   1.00 16.03 ? 69  TYR   A CD2 1 
ATOM   425  C  CE1 . TYR   A 1 69  ? -19.709 9.399   3.720   1.00 16.04 ? 69  TYR   A CE1 1 
ATOM   426  C  CE2 . TYR   A 1 69  ? -20.611 7.335   2.929   1.00 16.75 ? 69  TYR   A CE2 1 
ATOM   427  C  CZ  . TYR   A 1 69  ? -20.459 8.691   2.792   1.00 17.08 ? 69  TYR   A CZ  1 
ATOM   428  O  OH  . TYR   A 1 69  ? -21.102 9.333   1.757   1.00 18.38 ? 69  TYR   A OH  1 
ATOM   429  N  N   . LYS   A 1 70  ? -19.301 4.474   8.327   1.00 13.05 ? 70  LYS   A N   1 
ATOM   430  C  CA  . LYS   A 1 70  ? -18.783 3.399   9.147   1.00 13.44 ? 70  LYS   A CA  1 
ATOM   431  C  C   . LYS   A 1 70  ? -18.328 2.261   8.258   1.00 12.52 ? 70  LYS   A C   1 
ATOM   432  O  O   . LYS   A 1 70  ? -19.071 1.797   7.429   1.00 15.12 ? 70  LYS   A O   1 
ATOM   433  C  CB  . LYS   A 1 70  ? -19.902 2.878   10.101  1.00 16.54 ? 70  LYS   A CB  1 
ATOM   434  C  CG  . LYS   A 1 70  ? -19.549 1.665   10.919  1.00 20.58 ? 70  LYS   A CG  1 
ATOM   435  C  CD  . LYS   A 1 70  ? -20.521 1.412   12.071  1.00 31.47 ? 70  LYS   A CD  1 
ATOM   436  C  CE  . LYS   A 1 70  ? -21.886 1.109   11.542  0.50 30.59 ? 70  LYS   A CE  1 
ATOM   437  N  NZ  . LYS   A 1 70  ? -22.707 0.687   12.717  0.50 33.28 ? 70  LYS   A NZ  1 
ATOM   438  N  N   . VAL   A 1 71  ? -17.108 1.804   8.476   1.00 12.77 ? 71  VAL   A N   1 
ATOM   439  C  CA  . VAL   A 1 71  ? -16.522 0.666   7.798   1.00 12.77 ? 71  VAL   A CA  1 
ATOM   440  C  C   . VAL   A 1 71  ? -16.377 -0.446  8.799   1.00 12.82 ? 71  VAL   A C   1 
ATOM   441  O  O   . VAL   A 1 71  ? -15.604 -0.282  9.742   1.00 15.45 ? 71  VAL   A O   1 
ATOM   442  C  CB  . VAL   A 1 71  ? -15.172 1.045   7.146   1.00 13.98 ? 71  VAL   A CB  1 
ATOM   443  C  CG1 . VAL   A 1 71  ? -14.526 -0.230  6.521   1.00 16.14 ? 71  VAL   A CG1 1 
ATOM   444  C  CG2 . VAL   A 1 71  ? -15.324 2.153   6.179   1.00 16.35 ? 71  VAL   A CG2 1 
ATOM   445  N  N   . GLU   A 1 72  ? -17.120 -1.513  8.646   1.00 12.62 ? 72  GLU   A N   1 
ATOM   446  C  CA  . GLU   A 1 72  ? -17.066 -2.639  9.547   1.00 13.35 ? 72  GLU   A CA  1 
ATOM   447  C  C   . GLU   A 1 72  ? -16.359 -3.789  8.894   1.00 12.66 ? 72  GLU   A C   1 
ATOM   448  O  O   . GLU   A 1 72  ? -16.827 -4.305  7.892   1.00 14.33 ? 72  GLU   A O   1 
ATOM   449  C  CB  . GLU   A 1 72  ? -18.459 -3.100  9.954   1.00 16.34 ? 72  GLU   A CB  1 
ATOM   450  C  CG  . GLU   A 1 72  ? -18.427 -4.125  11.078  0.50 17.70 ? 72  GLU   A CG  1 
ATOM   451  C  CD  . GLU   A 1 72  ? -19.787 -4.688  11.500  0.50 25.60 ? 72  GLU   A CD  1 
ATOM   452  O  OE1 . GLU   A 1 72  ? -20.880 -4.107  11.251  0.50 30.04 ? 72  GLU   A OE1 1 
ATOM   453  O  OE2 . GLU   A 1 72  ? -19.707 -5.808  12.114  0.50 24.02 ? 72  GLU   A OE2 1 
ATOM   454  N  N   . ILE   A 1 73  ? -15.247 -4.198  9.468   1.00 12.40 ? 73  ILE   A N   1 
ATOM   455  C  CA  . ILE   A 1 73  ? -14.405 -5.261  8.945   1.00 12.50 ? 73  ILE   A CA  1 
ATOM   456  C  C   . ILE   A 1 73  ? -14.629 -6.520  9.761   1.00 12.52 ? 73  ILE   A C   1 
ATOM   457  O  O   . ILE   A 1 73  ? -14.428 -6.478  10.983  1.00 13.40 ? 73  ILE   A O   1 
ATOM   458  C  CB  . ILE   A 1 73  ? -12.923 -4.803  8.978   1.00 13.05 ? 73  ILE   A CB  1 
ATOM   459  C  CG1 . ILE   A 1 73  ? -12.749 -3.473  8.256   1.00 14.45 ? 73  ILE   A CG1 1 
ATOM   460  C  CG2 . ILE   A 1 73  ? -12.023 -5.909  8.441   1.00 14.62 ? 73  ILE   A CG2 1 
ATOM   461  C  CD1 . ILE   A 1 73  ? -11.375 -2.819  8.416   1.00 17.13 ? 73  ILE   A CD1 1 
ATOM   462  N  N   . ASP   A 1 74  ? -15.043 -7.604  9.129   1.00 13.00 ? 74  ASP   A N   1 
ATOM   463  C  CA  . ASP   A 1 74  ? -15.386 -8.837  9.868   1.00 13.55 ? 74  ASP   A CA  1 
ATOM   464  C  C   . ASP   A 1 74  ? -14.094 -9.607  10.181  1.00 12.88 ? 74  ASP   A C   1 
ATOM   465  O  O   . ASP   A 1 74  ? -13.792 -10.642 9.610   1.00 14.64 ? 74  ASP   A O   1 
ATOM   466  C  CB  . ASP   A 1 74  ? -16.369 -9.665  9.095   1.00 15.50 ? 74  ASP   A CB  1 
ATOM   467  C  CG  . ASP   A 1 74  ? -16.780 -10.959 9.854   0.80 15.16 ? 74  ASP   A CG  1 
ATOM   468  O  OD1 . ASP   A 1 74  ? -16.407 -11.044 11.074  0.80 16.86 ? 74  ASP   A OD1 1 
ATOM   469  O  OD2 . ASP   A 1 74  ? -17.470 -11.758 9.243   0.80 20.43 ? 74  ASP   A OD2 1 
ATOM   470  N  N   . THR   A 1 75  ? -13.393 -9.145  11.171  1.00 12.38 ? 75  THR   A N   1 
ATOM   471  C  CA  . THR   A 1 75  ? -12.191 -9.750  11.612  1.00 12.19 ? 75  THR   A CA  1 
ATOM   472  C  C   . THR   A 1 75  ? -12.414 -11.089 12.352  1.00 12.70 ? 75  THR   A C   1 
ATOM   473  O  O   . THR   A 1 75  ? -11.586 -11.990 12.256  1.00 13.40 ? 75  THR   A O   1 
ATOM   474  C  CB  . THR   A 1 75  ? -11.394 -8.778  12.487  1.00 13.73 ? 75  THR   A CB  1 
ATOM   475  O  OG1 . THR   A 1 75  ? -12.169 -8.464  13.659  1.00 13.15 ? 75  THR   A OG1 1 
ATOM   476  C  CG2 . THR   A 1 75  ? -11.092 -7.452  11.809  1.00 14.64 ? 75  THR   A CG2 1 
ATOM   477  N  N   . LYS   A 1 76  ? -13.543 -11.236 13.022  1.00 13.20 ? 76  LYS   A N   1 
ATOM   478  C  CA  . LYS   A 1 76  ? -13.810 -12.466 13.757  1.00 13.65 ? 76  LYS   A CA  1 
ATOM   479  C  C   . LYS   A 1 76  ? -13.878 -13.653 12.824  1.00 13.73 ? 76  LYS   A C   1 
ATOM   480  O  O   . LYS   A 1 76  ? -13.279 -14.664 13.102  1.00 14.39 ? 76  LYS   A O   1 
ATOM   481  C  CB  . LYS   A 1 76  ? -15.027 -12.360 14.644  1.00 14.47 ? 76  LYS   A CB  1 
ATOM   482  C  CG  . LYS   A 1 76  ? -15.294 -13.530 15.500  1.00 16.22 ? 76  LYS   A CG  1 
ATOM   483  C  CD  . LYS   A 1 76  ? -16.467 -13.368 16.381  1.00 20.90 ? 76  LYS   A CD  1 
ATOM   484  C  CE  . LYS   A 1 76  ? -16.631 -14.552 17.335  1.00 23.63 ? 76  LYS   A CE  1 
ATOM   485  N  NZ  . LYS   A 1 76  ? -17.822 -14.337 18.160  1.00 27.71 ? 76  LYS   A NZ  1 
ATOM   486  N  N   . SER   A 1 77  ? -14.593 -13.532 11.723  1.00 13.99 ? 77  SER   A N   1 
ATOM   487  C  CA  . SER   A 1 77  ? -14.674 -14.645 10.819  1.00 15.32 ? 77  SER   A CA  1 
ATOM   488  C  C   . SER   A 1 77  ? -13.351 -14.985 10.201  1.00 14.58 ? 77  SER   A C   1 
ATOM   489  O  O   . SER   A 1 77  ? -13.077 -16.163 9.939   1.00 15.29 ? 77  SER   A O   1 
ATOM   490  C  CB  . SER   A 1 77  ? -15.693 -14.347 9.698   1.00 15.80 ? 77  SER   A CB  1 
ATOM   491  O  OG  . SER   A 1 77  ? -16.972 -14.195 10.187  1.00 19.90 ? 77  SER   A OG  1 
ATOM   492  N  N   . TYR   A 1 78  ? -12.505 -13.984 9.909   1.00 14.15 ? 78  TYR   A N   1 
ATOM   493  C  CA  . TYR   A 1 78  ? -11.190 -14.190 9.425   1.00 13.52 ? 78  TYR   A CA  1 
ATOM   494  C  C   . TYR   A 1 78  ? -10.366 -15.070 10.373  1.00 13.69 ? 78  TYR   A C   1 
ATOM   495  O  O   . TYR   A 1 78  ? -9.821  -16.117 9.947   1.00 14.51 ? 78  TYR   A O   1 
ATOM   496  C  CB  . TYR   A 1 78  ? -10.497 -12.832 9.247   1.00 13.67 ? 78  TYR   A CB  1 
ATOM   497  C  CG  . TYR   A 1 78  ? -9.037  -13.004 8.780   1.00 13.57 ? 78  TYR   A CG  1 
ATOM   498  C  CD1 . TYR   A 1 78  ? -8.772  -13.292 7.477   1.00 14.03 ? 78  TYR   A CD1 1 
ATOM   499  C  CD2 . TYR   A 1 78  ? -8.005  -12.858 9.658   1.00 13.72 ? 78  TYR   A CD2 1 
ATOM   500  C  CE1 . TYR   A 1 78  ? -7.458  -13.513 7.029   1.00 14.54 ? 78  TYR   A CE1 1 
ATOM   501  C  CE2 . TYR   A 1 78  ? -6.681  -13.039 9.242   1.00 13.59 ? 78  TYR   A CE2 1 
ATOM   502  C  CZ  . TYR   A 1 78  ? -6.406  -13.368 7.941   1.00 13.69 ? 78  TYR   A CZ  1 
ATOM   503  O  OH  . TYR   A 1 78  ? -5.154  -13.538 7.470   1.00 16.39 ? 78  TYR   A OH  1 
ATOM   504  N  N   . TRP   A 1 79  ? -10.316 -14.741 11.649  1.00 12.23 ? 79  TRP   A N   1 
ATOM   505  C  CA  . TRP   A 1 79  ? -9.570  -15.527 12.621  1.00 13.34 ? 79  TRP   A CA  1 
ATOM   506  C  C   . TRP   A 1 79  ? -10.172 -16.884 12.836  1.00 13.26 ? 79  TRP   A C   1 
ATOM   507  O  O   . TRP   A 1 79  ? -9.455  -17.865 12.943  1.00 13.61 ? 79  TRP   A O   1 
ATOM   508  C  CB  . TRP   A 1 79  ? -9.461  -14.760 13.932  1.00 12.39 ? 79  TRP   A CB  1 
ATOM   509  C  CG  . TRP   A 1 79  ? -8.601  -13.550 13.837  1.00 11.04 ? 79  TRP   A CG  1 
ATOM   510  C  CD1 . TRP   A 1 79  ? -8.949  -12.238 14.004  1.00 11.50 ? 79  TRP   A CD1 1 
ATOM   511  C  CD2 . TRP   A 1 79  ? -7.186  -13.546 13.507  1.00 11.87 ? 79  TRP   A CD2 1 
ATOM   512  N  NE1 . TRP   A 1 79  ? -7.849  -11.416 13.802  1.00 11.52 ? 79  TRP   A NE1 1 
ATOM   513  C  CE2 . TRP   A 1 79  ? -6.774  -12.199 13.499  1.00 11.41 ? 79  TRP   A CE2 1 
ATOM   514  C  CE3 . TRP   A 1 79  ? -6.236  -14.540 13.244  1.00 13.05 ? 79  TRP   A CE3 1 
ATOM   515  C  CZ2 . TRP   A 1 79  ? -5.484  -11.827 13.174  1.00 11.89 ? 79  TRP   A CZ2 1 
ATOM   516  C  CZ3 . TRP   A 1 79  ? -4.948  -14.164 12.943  1.00 13.46 ? 79  TRP   A CZ3 1 
ATOM   517  C  CH2 . TRP   A 1 79  ? -4.557  -12.839 12.906  1.00 13.62 ? 79  TRP   A CH2 1 
ATOM   518  N  N   . LYS   A 1 80  ? -11.506 -16.978 12.904  1.00 13.24 ? 80  LYS   A N   1 
ATOM   519  C  CA  . LYS   A 1 80  ? -12.171 -18.242 13.153  1.00 14.81 ? 80  LYS   A CA  1 
ATOM   520  C  C   . LYS   A 1 80  ? -11.829 -19.241 12.067  1.00 15.26 ? 80  LYS   A C   1 
ATOM   521  O  O   . LYS   A 1 80  ? -11.679 -20.436 12.344  1.00 16.11 ? 80  LYS   A O   1 
ATOM   522  C  CB  . LYS   A 1 80  ? -13.677 -18.054 13.322  1.00 15.40 ? 80  LYS   A CB  1 
ATOM   523  C  CG  . LYS   A 1 80  ? -14.088 -17.476 14.638  1.00 17.03 ? 80  LYS   A CG  1 
ATOM   524  C  CD  . LYS   A 1 80  ? -14.042 -18.481 15.753  1.00 19.34 ? 80  LYS   A CD  1 
ATOM   525  C  CE  . LYS   A 1 80  ? -14.638 -17.976 17.061  1.00 21.08 ? 80  LYS   A CE  1 
ATOM   526  N  NZ  . LYS   A 1 80  ? -14.744 -19.087 18.059  1.00 24.91 ? 80  LYS   A NZ  1 
ATOM   527  N  N   . ALA   A 1 81  ? -11.755 -18.791 10.832  1.00 16.27 ? 81  ALA   A N   1 
ATOM   528  C  CA  . ALA   A 1 81  ? -11.418 -19.687 9.726   1.00 17.70 ? 81  ALA   A CA  1 
ATOM   529  C  C   . ALA   A 1 81  ? -9.993  -20.219 9.794   1.00 17.37 ? 81  ALA   A C   1 
ATOM   530  O  O   . ALA   A 1 81  ? -9.688  -21.229 9.169   1.00 20.97 ? 81  ALA   A O   1 
ATOM   531  C  CB  . ALA   A 1 81  ? -11.668 -18.980 8.385   1.00 20.92 ? 81  ALA   A CB  1 
ATOM   532  N  N   . LEU   A 1 82  ? -9.126  -19.567 10.562  1.00 16.06 ? 82  LEU   A N   1 
ATOM   533  C  CA  . LEU   A 1 82  ? -7.776  -19.982 10.864  1.00 16.30 ? 82  LEU   A CA  1 
ATOM   534  C  C   . LEU   A 1 82  ? -7.697  -20.721 12.159  1.00 16.14 ? 82  LEU   A C   1 
ATOM   535  O  O   . LEU   A 1 82  ? -6.572  -21.031 12.627  1.00 18.90 ? 82  LEU   A O   1 
ATOM   536  C  CB  . LEU   A 1 82  ? -6.813  -18.761 10.872  1.00 17.44 ? 82  LEU   A CB  1 
ATOM   537  C  CG  . LEU   A 1 82  ? -6.728  -18.040 9.557   1.00 18.08 ? 82  LEU   A CG  1 
ATOM   538  C  CD1 . LEU   A 1 82  ? -6.052  -16.691 9.699   1.00 23.53 ? 82  LEU   A CD1 1 
ATOM   539  C  CD2 . LEU   A 1 82  ? -5.976  -18.890 8.526   1.00 25.56 ? 82  LEU   A CD2 1 
ATOM   540  N  N   . GLY   A 1 83  ? -8.828  -21.061 12.789  1.00 15.48 ? 83  GLY   A N   1 
ATOM   541  C  CA  . GLY   A 1 83  ? -8.880  -21.846 14.003  1.00 16.80 ? 83  GLY   A CA  1 
ATOM   542  C  C   . GLY   A 1 83  ? -8.758  -21.018 15.274  1.00 14.94 ? 83  GLY   A C   1 
ATOM   543  O  O   . GLY   A 1 83  ? -8.714  -21.598 16.366  1.00 16.06 ? 83  GLY   A O   1 
ATOM   544  N  N   . ILE   A 1 84  ? -8.733  -19.674 15.148  1.00 14.26 ? 84  ILE   A N   1 
ATOM   545  C  CA  . ILE   A 1 84  ? -8.471  -18.804 16.305  1.00 14.64 ? 84  ILE   A CA  1 
ATOM   546  C  C   . ILE   A 1 84  ? -9.758  -18.186 16.790  1.00 14.66 ? 84  ILE   A C   1 
ATOM   547  O  O   . ILE   A 1 84  ? -10.560 -17.726 15.974  1.00 15.15 ? 84  ILE   A O   1 
ATOM   548  C  CB  . ILE   A 1 84  ? -7.440  -17.726 15.895  1.00 15.93 ? 84  ILE   A CB  1 
ATOM   549  C  CG1 . ILE   A 1 84  ? -6.096  -18.439 15.636  1.00 21.93 ? 84  ILE   A CG1 1 
ATOM   550  C  CG2 . ILE   A 1 84  ? -7.333  -16.562 16.883  1.00 17.34 ? 84  ILE   A CG2 1 
ATOM   551  C  CD1 . ILE   A 1 84  ? -5.094  -17.742 14.891  1.00 25.93 ? 84  ILE   A CD1 1 
ATOM   552  N  N   . SER   A 1 85  ? -9.927  -18.075 18.107  1.00 15.12 ? 85  SER   A N   1 
ATOM   553  C  CA  . SER   A 1 85  ? -11.013 -17.335 18.750  1.00 16.54 ? 85  SER   A CA  1 
ATOM   554  C  C   . SER   A 1 85  ? -10.465 -15.999 19.160  1.00 15.25 ? 85  SER   A C   1 
ATOM   555  O  O   . SER   A 1 85  ? -9.765  -15.901 20.163  1.00 17.44 ? 85  SER   A O   1 
ATOM   556  C  CB  . SER   A 1 85  ? -11.598 -18.103 19.938  1.00 18.75 ? 85  SER   A CB  1 
ATOM   557  O  OG  . SER   A 1 85  ? -12.159 -19.325 19.481  1.00 19.72 ? 85  SER   A OG  1 
ATOM   558  N  N   . PRO   A 1 86  ? -10.676 -14.933 18.365  1.00 13.61 ? 86  PRO   A N   1 
ATOM   559  C  CA  . PRO   A 1 86  ? -10.037 -13.656 18.639  1.00 13.56 ? 86  PRO   A CA  1 
ATOM   560  C  C   . PRO   A 1 86  ? -10.787 -12.861 19.651  1.00 13.61 ? 86  PRO   A C   1 
ATOM   561  O  O   . PRO   A 1 86  ? -11.928 -13.183 20.012  1.00 15.03 ? 86  PRO   A O   1 
ATOM   562  C  CB  . PRO   A 1 86  ? -10.124 -12.990 17.264  1.00 13.26 ? 86  PRO   A CB  1 
ATOM   563  C  CG  . PRO   A 1 86  ? -11.456 -13.409 16.770  1.00 13.31 ? 86  PRO   A CG  1 
ATOM   564  C  CD  . PRO   A 1 86  ? -11.569 -14.888 17.188  1.00 14.21 ? 86  PRO   A CD  1 
ATOM   565  N  N   . PHE   A 1 87  ? -10.230 -11.757 20.103  1.00 12.94 ? 87  PHE   A N   1 
ATOM   566  C  CA  . PHE   A 1 87  ? -10.898 -10.919 21.041  1.00 12.98 ? 87  PHE   A CA  1 
ATOM   567  C  C   . PHE   A 1 87  ? -12.056 -10.148 20.460  1.00 12.26 ? 87  PHE   A C   1 
ATOM   568  O  O   . PHE   A 1 87  ? -13.162 -10.116 21.063  1.00 13.75 ? 87  PHE   A O   1 
ATOM   569  C  CB  . PHE   A 1 87  ? -9.910  -9.966  21.668  1.00 13.78 ? 87  PHE   A CB  1 
ATOM   570  C  CG  . PHE   A 1 87  ? -10.491 -9.025  22.649  1.00 16.87 ? 87  PHE   A CG  1 
ATOM   571  C  CD1 . PHE   A 1 87  ? -10.781 -9.440  23.895  1.00 19.25 ? 87  PHE   A CD1 1 
ATOM   572  C  CD2 . PHE   A 1 87  ? -10.726 -7.702  22.326  1.00 18.41 ? 87  PHE   A CD2 1 
ATOM   573  C  CE1 . PHE   A 1 87  ? -11.439 -8.589  24.819  1.00 24.34 ? 87  PHE   A CE1 1 
ATOM   574  C  CE2 . PHE   A 1 87  ? -11.264 -6.815  23.261  1.00 27.26 ? 87  PHE   A CE2 1 
ATOM   575  C  CZ  . PHE   A 1 87  ? -11.621 -7.283  24.499  1.00 28.36 ? 87  PHE   A CZ  1 
ATOM   576  N  N   . HIS   A 1 88  ? -11.826 -9.454  19.365  1.00 12.63 ? 88  HIS   A N   1 
ATOM   577  C  CA  . HIS   A 1 88  ? -12.816 -8.522  18.843  1.00 12.83 ? 88  HIS   A CA  1 
ATOM   578  C  C   . HIS   A 1 88  ? -13.852 -9.182  17.964  1.00 12.14 ? 88  HIS   A C   1 
ATOM   579  O  O   . HIS   A 1 88  ? -13.581 -10.130 17.241  1.00 13.81 ? 88  HIS   A O   1 
ATOM   580  C  CB  . HIS   A 1 88  ? -12.111 -7.432  18.013  1.00 12.97 ? 88  HIS   A CB  1 
ATOM   581  C  CG  . HIS   A 1 88  ? -11.050 -6.661  18.728  1.00 14.99 ? 88  HIS   A CG  1 
ATOM   582  N  ND1 . HIS   A 1 88  ? -9.739  -7.073  18.789  1.00 14.20 ? 88  HIS   A ND1 1 
ATOM   583  C  CD2 . HIS   A 1 88  ? -11.118 -5.488  19.379  1.00 21.83 ? 88  HIS   A CD2 1 
ATOM   584  C  CE1 . HIS   A 1 88  ? -9.074  -6.174  19.475  1.00 18.52 ? 88  HIS   A CE1 1 
ATOM   585  N  NE2 . HIS   A 1 88  ? -9.924  -5.252  19.906  1.00 24.11 ? 88  HIS   A NE2 1 
ATOM   586  N  N   . GLU   A 1 89  ? -15.071 -8.687  18.001  1.00 12.45 ? 89  GLU   A N   1 
ATOM   587  C  CA  . GLU   A 1 89  ? -16.129 -9.095  17.091  1.00 13.21 ? 89  GLU   A CA  1 
ATOM   588  C  C   . GLU   A 1 89  ? -15.856 -8.626  15.691  1.00 14.95 ? 89  GLU   A C   1 
ATOM   589  O  O   . GLU   A 1 89  ? -16.210 -9.289  14.724  1.00 17.94 ? 89  GLU   A O   1 
ATOM   590  C  CB  . GLU   A 1 89  ? -17.444 -8.606  17.545  1.00 15.41 ? 89  GLU   A CB  1 
ATOM   591  C  CG  . GLU   A 1 89  ? -17.966 -9.256  18.762  1.00 18.68 ? 89  GLU   A CG  1 
ATOM   592  C  CD  . GLU   A 1 89  ? -18.292 -10.744 18.532  1.00 21.30 ? 89  GLU   A CD  1 
ATOM   593  O  OE1 . GLU   A 1 89  ? -19.159 -10.987 17.700  1.00 25.01 ? 89  GLU   A OE1 1 
ATOM   594  O  OE2 . GLU   A 1 89  ? -17.685 -11.581 19.221  1.00 21.28 ? 89  GLU   A OE2 1 
ATOM   595  N  N   . HIS   A 1 90  ? -15.278 -7.444  15.584  1.00 14.22 ? 90  HIS   A N   1 
ATOM   596  C  CA  . HIS   A 1 90  ? -15.000 -6.834  14.275  1.00 13.74 ? 90  HIS   A CA  1 
ATOM   597  C  C   . HIS   A 1 90  ? -14.111 -5.640  14.542  1.00 15.00 ? 90  HIS   A C   1 
ATOM   598  O  O   . HIS   A 1 90  ? -13.787 -5.400  15.695  1.00 18.01 ? 90  HIS   A O   1 
ATOM   599  C  CB  . HIS   A 1 90  ? -16.298 -6.312  13.627  1.00 16.95 ? 90  HIS   A CB  1 
ATOM   600  C  CG  . HIS   A 1 90  ? -17.004 -5.295  14.464  1.00 23.30 ? 90  HIS   A CG  1 
ATOM   601  N  ND1 . HIS   A 1 90  ? -18.261 -5.509  14.972  1.00 31.27 ? 90  HIS   A ND1 1 
ATOM   602  C  CD2 . HIS   A 1 90  ? -16.628 -4.075  14.904  1.00 33.74 ? 90  HIS   A CD2 1 
ATOM   603  C  CE1 . HIS   A 1 90  ? -18.639 -4.465  15.677  1.00 30.67 ? 90  HIS   A CE1 1 
ATOM   604  N  NE2 . HIS   A 1 90  ? -17.655 -3.569  15.653  1.00 32.00 ? 90  HIS   A NE2 1 
ATOM   605  N  N   . ALA   A 1 91  ? -13.706 -4.967  13.489  1.00 15.61 ? 91  ALA   A N   1 
ATOM   606  C  CA  . ALA   A 1 91  ? -13.003 -3.682  13.622  1.00 17.50 ? 91  ALA   A CA  1 
ATOM   607  C  C   . ALA   A 1 91  ? -13.904 -2.709  12.892  1.00 17.99 ? 91  ALA   A C   1 
ATOM   608  O  O   . ALA   A 1 91  ? -14.189 -2.918  11.745  1.00 17.69 ? 91  ALA   A O   1 
ATOM   609  C  CB  . ALA   A 1 91  ? -11.635 -3.763  12.928  1.00 19.83 ? 91  ALA   A CB  1 
ATOM   610  N  N   . GLU   A 1 92  ? -14.362 -1.667  13.579  1.00 19.27 ? 92  GLU   A N   1 
ATOM   611  C  CA  . GLU   A 1 92  ? -15.237 -0.630  13.042  1.00 21.27 ? 92  GLU   A CA  1 
ATOM   612  C  C   . GLU   A 1 92  ? -14.588 0.721   13.001  1.00 20.93 ? 92  GLU   A C   1 
ATOM   613  O  O   . GLU   A 1 92  ? -13.957 1.076   13.955  1.00 32.01 ? 92  GLU   A O   1 
ATOM   614  C  CB  . GLU   A 1 92  ? -16.453 -0.490  13.890  1.00 27.43 ? 92  GLU   A CB  1 
ATOM   615  N  N   . VAL   A 1 93  ? -14.566 1.294   11.855  1.00 16.31 ? 93  VAL   A N   1 
ATOM   616  C  CA  . VAL   A 1 93  ? -13.881 2.608   11.646  1.00 16.03 ? 93  VAL   A CA  1 
ATOM   617  C  C   . VAL   A 1 93  ? -15.016 3.604   11.271  1.00 14.10 ? 93  VAL   A C   1 
ATOM   618  O  O   . VAL   A 1 93  ? -15.688 3.387   10.295  1.00 15.14 ? 93  VAL   A O   1 
ATOM   619  C  CB  . VAL   A 1 93  ? -12.839 2.457   10.517  1.00 17.43 ? 93  VAL   A CB  1 
ATOM   620  C  CG1 . VAL   A 1 93  ? -12.122 3.709   10.333  1.00 21.84 ? 93  VAL   A CG1 1 
ATOM   621  C  CG2 . VAL   A 1 93  ? -11.856 1.277   10.818  1.00 23.50 ? 93  VAL   A CG2 1 
ATOM   622  N  N   . VAL   A 1 94  ? -15.177 4.659   12.062  1.00 13.17 ? 94  VAL   A N   1 
ATOM   623  C  CA  . VAL   A 1 94  ? -16.263 5.621   11.896  1.00 13.25 ? 94  VAL   A CA  1 
ATOM   624  C  C   . VAL   A 1 94  ? -15.657 6.990   11.720  1.00 12.37 ? 94  VAL   A C   1 
ATOM   625  O  O   . VAL   A 1 94  ? -14.824 7.410   12.513  1.00 12.93 ? 94  VAL   A O   1 
ATOM   626  C  CB  . VAL   A 1 94  ? -17.222 5.589   13.101  1.00 14.80 ? 94  VAL   A CB  1 
ATOM   627  C  CG1 . VAL   A 1 94  ? -18.375 6.606   12.852  1.00 17.55 ? 94  VAL   A CG1 1 
ATOM   628  C  CG2 . VAL   A 1 94  ? -17.754 4.183   13.294  1.00 18.05 ? 94  VAL   A CG2 1 
ATOM   629  N  N   . PHE   A 1 95  ? -16.030 7.705   10.669  1.00 12.92 ? 95  PHE   A N   1 
ATOM   630  C  CA  . PHE   A 1 95  ? -15.359 8.962   10.289  1.00 12.23 ? 95  PHE   A CA  1 
ATOM   631  C  C   . PHE   A 1 95  ? -16.298 9.799   9.474   1.00 12.83 ? 95  PHE   A C   1 
ATOM   632  O  O   . PHE   A 1 95  ? -17.140 9.337   8.739   1.00 14.06 ? 95  PHE   A O   1 
ATOM   633  C  CB  . PHE   A 1 95  ? -14.081 8.665   9.521   1.00 13.04 ? 95  PHE   A CB  1 
ATOM   634  C  CG  . PHE   A 1 95  ? -14.261 7.990   8.200   1.00 15.33 ? 95  PHE   A CG  1 
ATOM   635  C  CD1 . PHE   A 1 95  ? -14.466 6.653   8.143   1.00 19.97 ? 95  PHE   A CD1 1 
ATOM   636  C  CD2 . PHE   A 1 95  ? -14.205 8.715   7.053   1.00 17.46 ? 95  PHE   A CD2 1 
ATOM   637  C  CE1 . PHE   A 1 95  ? -14.584 6.018   6.892   1.00 23.45 ? 95  PHE   A CE1 1 
ATOM   638  C  CE2 . PHE   A 1 95  ? -14.311 8.102   5.844   1.00 23.07 ? 95  PHE   A CE2 1 
ATOM   639  C  CZ  . PHE   A 1 95  ? -14.498 6.781   5.756   1.00 24.09 ? 95  PHE   A CZ  1 
ATOM   640  N  N   . THR   A 1 96  ? -16.123 11.124  9.552   1.00 13.46 ? 96  THR   A N   1 
ATOM   641  C  CA  . THR   A 1 96  ? -16.732 12.085  8.656   1.00 13.57 ? 96  THR   A CA  1 
ATOM   642  C  C   . THR   A 1 96  ? -15.915 12.180  7.400   1.00 14.49 ? 96  THR   A C   1 
ATOM   643  O  O   . THR   A 1 96  ? -14.693 12.343  7.478   1.00 18.86 ? 96  THR   A O   1 
ATOM   644  C  CB  . THR   A 1 96  ? -16.854 13.450  9.326   1.00 15.83 ? 96  THR   A CB  1 
ATOM   645  O  OG1 . THR   A 1 96  ? -17.669 13.346  10.484  1.00 19.14 ? 96  THR   A OG1 1 
ATOM   646  C  CG2 . THR   A 1 96  ? -17.461 14.466  8.404   1.00 21.54 ? 96  THR   A CG2 1 
ATOM   647  N  N   . ALA   A 1 97  ? -16.550 12.097  6.244   1.00 15.19 ? 97  ALA   A N   1 
ATOM   648  C  CA  . ALA   A 1 97  ? -15.871 12.130  4.964   1.00 15.55 ? 97  ALA   A CA  1 
ATOM   649  C  C   . ALA   A 1 97  ? -16.296 13.372  4.197   1.00 16.04 ? 97  ALA   A C   1 
ATOM   650  O  O   . ALA   A 1 97  ? -17.450 13.826  4.264   1.00 18.85 ? 97  ALA   A O   1 
ATOM   651  C  CB  . ALA   A 1 97  ? -16.165 10.890  4.136   1.00 20.56 ? 97  ALA   A CB  1 
ATOM   652  N  N   . ASN   A 1 98  ? -15.362 13.899  3.402   1.00 16.30 ? 98  ASN   A N   1 
ATOM   653  C  CA  . ASN   A 1 98  ? -15.585 14.941  2.443   1.00 18.11 ? 98  ASN   A CA  1 
ATOM   654  C  C   . ASN   A 1 98  ? -16.117 16.230  2.996   1.00 20.14 ? 98  ASN   A C   1 
ATOM   655  O  O   . ASN   A 1 98  ? -16.763 16.996  2.258   1.00 25.94 ? 98  ASN   A O   1 
ATOM   656  C  CB  . ASN   A 1 98  ? -16.502 14.446  1.314   1.00 20.67 ? 98  ASN   A CB  1 
ATOM   657  C  CG  . ASN   A 1 98  ? -16.042 13.125  0.786   1.00 18.25 ? 98  ASN   A CG  1 
ATOM   658  O  OD1 . ASN   A 1 98  ? -16.789 12.102  0.845   1.00 22.82 ? 98  ASN   A OD1 1 
ATOM   659  N  ND2 . ASN   A 1 98  ? -14.844 13.084  0.310   1.00 17.88 ? 98  ASN   A ND2 1 
ATOM   660  N  N   . ASP   A 1 99  ? -15.799 16.511  4.256   1.00 20.86 ? 99  ASP   A N   1 
ATOM   661  C  CA  . ASP   A 1 99  ? -16.290 17.738  4.907   1.00 22.35 ? 99  ASP   A CA  1 
ATOM   662  C  C   . ASP   A 1 99  ? -15.699 19.003  4.371   1.00 26.10 ? 99  ASP   A C   1 
ATOM   663  O  O   . ASP   A 1 99  ? -16.311 20.088  4.537   1.00 30.54 ? 99  ASP   A O   1 
ATOM   664  C  CB  . ASP   A 1 99  ? -16.122 17.624  6.458   1.00 24.70 ? 99  ASP   A CB  1 
ATOM   665  N  N   . SER   A 1 100 ? -14.512 18.901  3.791   1.00 28.00 ? 100 SER   A N   1 
ATOM   666  C  CA  . SER   A 1 100 ? -13.966 20.115  3.137   1.00 31.42 ? 100 SER   A CA  1 
ATOM   667  C  C   . SER   A 1 100 ? -13.696 19.910  1.651   1.00 30.47 ? 100 SER   A C   1 
ATOM   668  O  O   . SER   A 1 100 ? -12.765 20.460  1.082   1.00 48.52 ? 100 SER   A O   1 
ATOM   669  C  CB  . SER   A 1 100 ? -12.790 20.794  3.861   0.50 33.11 ? 100 SER   A CB  1 
ATOM   670  O  OG  . SER   A 1 100 ? -12.136 19.974  4.784   0.50 38.22 ? 100 SER   A OG  1 
ATOM   671  N  N   . GLY   A 1 101 ? -14.560 19.085  1.048   1.00 25.69 ? 101 GLY   A N   1 
ATOM   672  C  CA  . GLY   A 1 101 ? -14.536 18.731  -0.382  1.00 23.07 ? 101 GLY   A CA  1 
ATOM   673  C  C   . GLY   A 1 101 ? -14.100 17.321  -0.571  1.00 21.49 ? 101 GLY   A C   1 
ATOM   674  O  O   . GLY   A 1 101 ? -13.725 16.626  0.400   1.00 22.87 ? 101 GLY   A O   1 
ATOM   675  N  N   . PRO   A 1 102 ? -14.173 16.843  -1.814  1.00 21.73 ? 102 PRO   A N   1 
ATOM   676  C  CA  . PRO   A 1 102 ? -13.906 15.447  -2.074  1.00 20.80 ? 102 PRO   A CA  1 
ATOM   677  C  C   . PRO   A 1 102 ? -12.466 15.099  -1.763  1.00 20.69 ? 102 PRO   A C   1 
ATOM   678  O  O   . PRO   A 1 102 ? -11.539 15.789  -2.127  1.00 21.81 ? 102 PRO   A O   1 
ATOM   679  C  CB  . PRO   A 1 102 ? -14.186 15.286  -3.563  1.00 23.39 ? 102 PRO   A CB  1 
ATOM   680  C  CG  . PRO   A 1 102 ? -14.190 16.669  -4.120  1.00 31.37 ? 102 PRO   A CG  1 
ATOM   681  C  CD  . PRO   A 1 102 ? -14.569 17.595  -3.017  1.00 23.96 ? 102 PRO   A CD  1 
ATOM   682  N  N   . ARG   A 1 103 ? -12.264 13.950  -1.135  1.00 18.59 ? 103 ARG   A N   1 
ATOM   683  C  CA  . ARG   A 1 103 ? -10.944 13.372  -0.858  1.00 16.50 ? 103 ARG   A CA  1 
ATOM   684  C  C   . ARG   A 1 103 ? -10.984 11.895  -1.218  1.00 16.93 ? 103 ARG   A C   1 
ATOM   685  O  O   . ARG   A 1 103 ? -12.080 11.315  -1.341  1.00 18.76 ? 103 ARG   A O   1 
ATOM   686  C  CB  . ARG   A 1 103 ? -10.566 13.576  0.623   1.00 18.24 ? 103 ARG   A CB  1 
ATOM   687  C  CG  . ARG   A 1 103 ? -10.509 15.009  1.081   1.00 19.28 ? 103 ARG   A CG  1 
ATOM   688  C  CD  . ARG   A 1 103 ? -9.302  15.699  0.466   1.00 23.00 ? 103 ARG   A CD  1 
ATOM   689  N  NE  . ARG   A 1 103 ? -9.138  17.069  0.976   1.00 28.85 ? 103 ARG   A NE  1 
ATOM   690  C  CZ  . ARG   A 1 103 ? -9.804  18.103  0.562   1.00 31.61 ? 103 ARG   A CZ  1 
ATOM   691  N  NH1 . ARG   A 1 103 ? -10.651 17.996  -0.427  1.00 28.84 ? 103 ARG   A NH1 1 
ATOM   692  N  NH2 . ARG   A 1 103 ? -9.548  19.275  1.123   1.00 33.95 ? 103 ARG   A NH2 1 
ATOM   693  N  N   . ARG   A 1 104 ? -9.792  11.294  -1.339  1.00 16.56 ? 104 ARG   A N   1 
ATOM   694  C  CA  . ARG   A 1 104 ? -9.646  9.833   -1.435  1.00 16.91 ? 104 ARG   A CA  1 
ATOM   695  C  C   . ARG   A 1 104 ? -9.199  9.306   -0.117  1.00 14.43 ? 104 ARG   A C   1 
ATOM   696  O  O   . ARG   A 1 104 ? -8.262  9.803   0.503   1.00 17.15 ? 104 ARG   A O   1 
ATOM   697  C  CB  . ARG   A 1 104 ? -8.646  9.534   -2.540  1.00 19.86 ? 104 ARG   A CB  1 
ATOM   698  C  CG  . ARG   A 1 104 ? -9.030  10.036  -3.965  1.00 30.78 ? 104 ARG   A CG  1 
ATOM   699  C  CD  . ARG   A 1 104 ? -7.960  9.696   -5.011  1.00 35.57 ? 104 ARG   A CD  1 
ATOM   700  N  N   . TYR   A 1 105 ? -9.843  8.273   0.324   1.00 14.45 ? 105 TYR   A N   1 
ATOM   701  C  CA  . TYR   A 1 105 ? -9.614  7.662   1.625   1.00 13.87 ? 105 TYR   A CA  1 
ATOM   702  C  C   . TYR   A 1 105 ? -9.142  6.225   1.462   1.00 13.66 ? 105 TYR   A C   1 
ATOM   703  O  O   . TYR   A 1 105 ? -9.808  5.422   0.817   1.00 16.39 ? 105 TYR   A O   1 
ATOM   704  C  CB  . TYR   A 1 105 ? -10.931 7.653   2.441   1.00 14.91 ? 105 TYR   A CB  1 
ATOM   705  C  CG  . TYR   A 1 105 ? -11.428 9.024   2.751   1.00 15.09 ? 105 TYR   A CG  1 
ATOM   706  C  CD1 . TYR   A 1 105 ? -12.228 9.698   1.838   1.00 15.48 ? 105 TYR   A CD1 1 
ATOM   707  C  CD2 . TYR   A 1 105 ? -11.153 9.630   3.976   1.00 16.27 ? 105 TYR   A CD2 1 
ATOM   708  C  CE1 . TYR   A 1 105 ? -12.650 10.990  2.122   1.00 16.40 ? 105 TYR   A CE1 1 
ATOM   709  C  CE2 . TYR   A 1 105 ? -11.567 10.921  4.238   1.00 16.12 ? 105 TYR   A CE2 1 
ATOM   710  C  CZ  . TYR   A 1 105 ? -12.358 11.564  3.336   1.00 15.30 ? 105 TYR   A CZ  1 
ATOM   711  O  OH  . TYR   A 1 105 ? -12.755 12.853  3.531   1.00 16.39 ? 105 TYR   A OH  1 
ATOM   712  N  N   . THR   A 1 106 ? -8.030  5.891   2.115   1.00 13.25 ? 106 THR   A N   1 
ATOM   713  C  CA  . THR   A 1 106 ? -7.601  4.504   2.287   1.00 13.79 ? 106 THR   A CA  1 
ATOM   714  C  C   . THR   A 1 106 ? -7.720  4.207   3.745   1.00 13.27 ? 106 THR   A C   1 
ATOM   715  O  O   . THR   A 1 106 ? -7.092  4.894   4.577   1.00 15.17 ? 106 THR   A O   1 
ATOM   716  C  CB  . THR   A 1 106 ? -6.193  4.286   1.811   1.00 16.78 ? 106 THR   A CB  1 
ATOM   717  O  OG1 . THR   A 1 106 ? -6.153  4.550   0.408   1.00 23.66 ? 106 THR   A OG1 1 
ATOM   718  C  CG2 . THR   A 1 106 ? -5.749  2.814   2.105   1.00 21.12 ? 106 THR   A CG2 1 
ATOM   719  N  N   . ILE   A 1 107 ? -8.514  3.214   4.086   1.00 13.11 ? 107 ILE   A N   1 
ATOM   720  C  CA  . ILE   A 1 107 ? -8.687  2.744   5.422   1.00 13.92 ? 107 ILE   A CA  1 
ATOM   721  C  C   . ILE   A 1 107 ? -7.896  1.482   5.567   1.00 13.67 ? 107 ILE   A C   1 
ATOM   722  O  O   . ILE   A 1 107 ? -8.205  0.483   4.950   1.00 15.26 ? 107 ILE   A O   1 
ATOM   723  C  CB  . ILE   A 1 107 ? -10.182 2.492   5.806   1.00 15.59 ? 107 ILE   A CB  1 
ATOM   724  C  CG1 . ILE   A 1 107 ? -11.079 3.748   5.554   1.00 19.82 ? 107 ILE   A CG1 1 
ATOM   725  C  CG2 . ILE   A 1 107 ? -10.296 1.956   7.223   1.00 19.54 ? 107 ILE   A CG2 1 
ATOM   726  C  CD1 . ILE   A 1 107 ? -10.651 4.960   6.340   1.00 21.24 ? 107 ILE   A CD1 1 
ATOM   727  N  N   . ALA   A 1 108 ? -6.843  1.499   6.344   1.00 13.34 ? 108 ALA   A N   1 
ATOM   728  C  CA  . ALA   A 1 108 ? -5.969  0.332   6.509   1.00 14.37 ? 108 ALA   A CA  1 
ATOM   729  C  C   . ALA   A 1 108 ? -6.236  -0.256  7.889   1.00 13.61 ? 108 ALA   A C   1 
ATOM   730  O  O   . ALA   A 1 108 ? -6.407  0.481   8.866   1.00 17.52 ? 108 ALA   A O   1 
ATOM   731  C  CB  . ALA   A 1 108 ? -4.509  0.722   6.335   1.00 16.82 ? 108 ALA   A CB  1 
ATOM   732  N  N   . ALA   A 1 109 ? -6.232  -1.566  7.992   1.00 12.38 ? 109 ALA   A N   1 
ATOM   733  C  CA  . ALA   A 1 109 ? -6.353  -2.257  9.275   1.00 12.11 ? 109 ALA   A CA  1 
ATOM   734  C  C   . ALA   A 1 109 ? -5.251  -3.346  9.351   1.00 11.41 ? 109 ALA   A C   1 
ATOM   735  O  O   . ALA   A 1 109 ? -5.005  -4.061  8.381   1.00 14.42 ? 109 ALA   A O   1 
ATOM   736  C  CB  . ALA   A 1 109 ? -7.701  -2.935  9.454   1.00 14.27 ? 109 ALA   A CB  1 
ATOM   737  N  N   . LEU   A 1 110 ? -4.633  -3.455  10.488  1.00 10.98 ? 110 LEU   A N   1 
ATOM   738  C  CA  . LEU   A 1 110 ? -3.600  -4.430  10.786  1.00 11.09 ? 110 LEU   A CA  1 
ATOM   739  C  C   . LEU   A 1 110 ? -4.091  -5.298  11.913  1.00 11.38 ? 110 LEU   A C   1 
ATOM   740  O  O   . LEU   A 1 110 ? -4.369  -4.834  12.993  1.00 12.59 ? 110 LEU   A O   1 
ATOM   741  C  CB  . LEU   A 1 110 ? -2.313  -3.714  11.209  1.00 12.83 ? 110 LEU   A CB  1 
ATOM   742  C  CG  . LEU   A 1 110 ? -1.165  -4.597  11.619  1.00 14.79 ? 110 LEU   A CG  1 
ATOM   743  C  CD1 . LEU   A 1 110 ? -0.689  -5.401  10.411  1.00 16.30 ? 110 LEU   A CD1 1 
ATOM   744  C  CD2 . LEU   A 1 110 ? -0.005  -3.767  12.233  1.00 20.81 ? 110 LEU   A CD2 1 
ATOM   745  N  N   . LEU   A 1 111 ? -4.251  -6.587  11.647  1.00 10.75 ? 111 LEU   A N   1 
ATOM   746  C  CA  . LEU   A 1 111 ? -4.959  -7.506  12.535  1.00 11.19 ? 111 LEU   A CA  1 
ATOM   747  C  C   . LEU   A 1 111 ? -4.041  -8.467  13.295  1.00 10.66 ? 111 LEU   A C   1 
ATOM   748  O  O   . LEU   A 1 111 ? -3.191  -9.119  12.710  1.00 10.92 ? 111 LEU   A O   1 
ATOM   749  C  CB  . LEU   A 1 111 ? -5.941  -8.365  11.761  1.00 11.86 ? 111 LEU   A CB  1 
ATOM   750  C  CG  . LEU   A 1 111 ? -6.906  -7.628  10.827  1.00 12.24 ? 111 LEU   A CG  1 
ATOM   751  C  CD1 . LEU   A 1 111 ? -7.881  -8.662  10.259  1.00 14.16 ? 111 LEU   A CD1 1 
ATOM   752  C  CD2 . LEU   A 1 111 ? -7.628  -6.489  11.558  1.00 13.76 ? 111 LEU   A CD2 1 
ATOM   753  N  N   . SER   A 1 112 ? -4.309  -8.566  14.595  1.00 10.70 ? 112 SER   A N   1 
ATOM   754  C  CA  . SER   A 1 112 ? -3.768  -9.640  15.426  1.00 11.05 ? 112 SER   A CA  1 
ATOM   755  C  C   . SER   A 1 112 ? -4.915  -10.249 16.211  1.00 9.89  ? 112 SER   A C   1 
ATOM   756  O  O   . SER   A 1 112 ? -5.963  -9.628  16.378  1.00 11.52 ? 112 SER   A O   1 
ATOM   757  C  CB  . SER   A 1 112 ? -2.718  -9.115  16.390  1.00 11.64 ? 112 SER   A CB  1 
ATOM   758  O  OG  . SER   A 1 112 ? -1.672  -8.480  15.711  1.00 14.29 ? 112 SER   A OG  1 
ATOM   759  N  N   . PRO   A 1 113 ? -4.777  -11.433 16.815  1.00 10.68 ? 113 PRO   A N   1 
ATOM   760  C  CA  . PRO   A 1 113 ? -5.914  -12.025 17.490  1.00 11.27 ? 113 PRO   A CA  1 
ATOM   761  C  C   . PRO   A 1 113 ? -6.476  -11.166 18.624  1.00 10.59 ? 113 PRO   A C   1 
ATOM   762  O  O   . PRO   A 1 113 ? -7.709  -11.185 18.818  1.00 12.62 ? 113 PRO   A O   1 
ATOM   763  C  CB  . PRO   A 1 113 ? -5.384  -13.338 17.966  1.00 12.47 ? 113 PRO   A CB  1 
ATOM   764  C  CG  . PRO   A 1 113 ? -4.444  -13.767 16.852  1.00 13.60 ? 113 PRO   A CG  1 
ATOM   765  C  CD  . PRO   A 1 113 ? -3.724  -12.443 16.512  1.00 11.72 ? 113 PRO   A CD  1 
ATOM   766  N  N   . TYR   A 1 114 ? -5.671  -10.446 19.367  1.00 10.77 ? 114 TYR   A N   1 
ATOM   767  C  CA  . TYR   A 1 114 ? -6.092  -9.645  20.487  1.00 11.29 ? 114 TYR   A CA  1 
ATOM   768  C  C   . TYR   A 1 114 ? -5.856  -8.156  20.306  1.00 11.68 ? 114 TYR   A C   1 
ATOM   769  O  O   . TYR   A 1 114 ? -5.955  -7.401  21.268  1.00 13.79 ? 114 TYR   A O   1 
ATOM   770  C  CB  . TYR   A 1 114 ? -5.510  -10.162 21.810  1.00 12.15 ? 114 TYR   A CB  1 
ATOM   771  C  CG  . TYR   A 1 114 ? -6.236  -11.331 22.394  1.00 12.01 ? 114 TYR   A CG  1 
ATOM   772  C  CD1 . TYR   A 1 114 ? -6.128  -12.571 21.815  1.00 18.72 ? 114 TYR   A CD1 1 
ATOM   773  C  CD2 . TYR   A 1 114 ? -7.055  -11.230 23.489  1.00 13.34 ? 114 TYR   A CD2 1 
ATOM   774  C  CE1 . TYR   A 1 114 ? -6.812  -13.659 22.325  1.00 25.26 ? 114 TYR   A CE1 1 
ATOM   775  C  CE2 . TYR   A 1 114 ? -7.774  -12.293 23.986  1.00 17.44 ? 114 TYR   A CE2 1 
ATOM   776  C  CZ  . TYR   A 1 114 ? -7.639  -13.480 23.406  1.00 22.54 ? 114 TYR   A CZ  1 
ATOM   777  O  OH  . TYR   A 1 114 ? -8.297  -14.559 23.872  1.00 32.28 ? 114 TYR   A OH  1 
ATOM   778  N  N   . SER   A 1 115 ? -5.598  -7.704  19.093  1.00 11.87 ? 115 SER   A N   1 
ATOM   779  C  CA  . SER   A 1 115 ? -5.341  -6.339  18.824  1.00 10.98 ? 115 SER   A CA  1 
ATOM   780  C  C   . SER   A 1 115 ? -5.613  -6.003  17.394  1.00 12.10 ? 115 SER   A C   1 
ATOM   781  O  O   . SER   A 1 115 ? -5.421  -6.807  16.505  1.00 13.80 ? 115 SER   A O   1 
ATOM   782  C  CB  . SER   A 1 115 ? -3.844  -6.047  19.117  1.00 12.82 ? 115 SER   A CB  1 
ATOM   783  O  OG  . SER   A 1 115 ? -3.501  -4.709  19.037  1.00 17.04 ? 115 SER   A OG  1 
ATOM   784  N  N   . TYR   A 1 116 ? -5.961  -4.732  17.171  1.00 12.13 ? 116 TYR   A N   1 
ATOM   785  C  CA  . TYR   A 1 116 ? -5.995  -4.231  15.777  1.00 12.60 ? 116 TYR   A CA  1 
ATOM   786  C  C   . TYR   A 1 116 ? -5.568  -2.756  15.809  1.00 11.34 ? 116 TYR   A C   1 
ATOM   787  O  O   . TYR   A 1 116 ? -5.729  -2.069  16.804  1.00 12.19 ? 116 TYR   A O   1 
ATOM   788  C  CB  . TYR   A 1 116 ? -7.325  -4.464  15.060  1.00 14.84 ? 116 TYR   A CB  1 
ATOM   789  C  CG  . TYR   A 1 116 ? -8.431  -3.495  15.401  1.00 15.04 ? 116 TYR   A CG  1 
ATOM   790  C  CD1 . TYR   A 1 116 ? -8.532  -2.282  14.743  1.00 16.85 ? 116 TYR   A CD1 1 
ATOM   791  C  CD2 . TYR   A 1 116 ? -9.396  -3.794  16.349  1.00 18.46 ? 116 TYR   A CD2 1 
ATOM   792  C  CE1 . TYR   A 1 116 ? -9.545  -1.383  15.024  1.00 22.93 ? 116 TYR   A CE1 1 
ATOM   793  C  CE2 . TYR   A 1 116 ? -10.415 -2.900  16.647  1.00 20.26 ? 116 TYR   A CE2 1 
ATOM   794  C  CZ  . TYR   A 1 116 ? -10.487 -1.690  15.982  1.00 26.12 ? 116 TYR   A CZ  1 
ATOM   795  O  OH  . TYR   A 1 116 ? -11.473 -0.782  16.245  1.00 30.71 ? 116 TYR   A OH  1 
ATOM   796  N  N   . SER   A 1 117 ? -4.979  -2.350  14.700  1.00 12.23 ? 117 SER   A N   1 
ATOM   797  C  CA  A SER   A 1 117 ? -4.632  -0.976  14.451  0.50 12.75 ? 117 SER   A CA  1 
ATOM   798  C  CA  B SER   A 1 117 ? -4.735  -0.950  14.500  0.50 12.81 ? 117 SER   A CA  1 
ATOM   799  C  C   . SER   A 1 117 ? -5.381  -0.565  13.202  1.00 14.16 ? 117 SER   A C   1 
ATOM   800  O  O   . SER   A 1 117 ? -5.546  -1.347  12.266  1.00 16.86 ? 117 SER   A O   1 
ATOM   801  C  CB  A SER   A 1 117 ? -3.143  -0.860  14.209  0.50 17.95 ? 117 SER   A CB  1 
ATOM   802  C  CB  B SER   A 1 117 ? -3.298  -0.565  14.442  0.50 17.52 ? 117 SER   A CB  1 
ATOM   803  O  OG  A SER   A 1 117 ? -2.693  0.415   13.868  0.50 23.76 ? 117 SER   A OG  1 
ATOM   804  O  OG  B SER   A 1 117 ? -2.798  -1.007  13.210  0.50 19.11 ? 117 SER   A OG  1 
ATOM   805  N  N   . THR   A 1 118 ? -5.756  0.681   13.115  1.00 14.49 ? 118 THR   A N   1 
ATOM   806  C  CA  . THR   A 1 118 ? -6.329  1.234   11.934  1.00 14.13 ? 118 THR   A CA  1 
ATOM   807  C  C   . THR   A 1 118 ? -5.807  2.613   11.648  1.00 14.33 ? 118 THR   A C   1 
ATOM   808  O  O   . THR   A 1 118 ? -5.560  3.384   12.546  1.00 17.11 ? 118 THR   A O   1 
ATOM   809  C  CB  . THR   A 1 118 ? -7.826  1.220   11.990  1.00 15.98 ? 118 THR   A CB  1 
ATOM   810  O  OG1 . THR   A 1 118 ? -8.341  1.537   10.726  1.00 17.27 ? 118 THR   A OG1 1 
ATOM   811  C  CG2 . THR   A 1 118 ? -8.491  2.120   13.002  1.00 17.59 ? 118 THR   A CG2 1 
ATOM   812  N  N   . THR   A 1 119 ? -5.573  2.900   10.393  1.00 13.38 ? 119 THR   A N   1 
ATOM   813  C  CA  . THR   A 1 119 ? -4.964  4.139   9.958   1.00 13.38 ? 119 THR   A CA  1 
ATOM   814  C  C   . THR   A 1 119 ? -5.759  4.626   8.771   1.00 12.33 ? 119 THR   A C   1 
ATOM   815  O  O   . THR   A 1 119 ? -6.257  3.845   7.996   1.00 17.06 ? 119 THR   A O   1 
ATOM   816  C  CB  . THR   A 1 119 ? -3.493  3.892   9.528   1.00 21.63 ? 119 THR   A CB  1 
ATOM   817  O  OG1 . THR   A 1 119 ? -2.874  3.247   10.654  1.00 24.12 ? 119 THR   A OG1 1 
ATOM   818  C  CG2 . THR   A 1 119 ? -2.871  5.249   9.276   0.50 27.89 ? 119 THR   A CG2 1 
ATOM   819  N  N   . ALA   A 1 120 ? -5.878  5.927   8.619   1.00 12.56 ? 120 ALA   A N   1 
ATOM   820  C  CA  . ALA   A 1 120 ? -6.478  6.553   7.437   1.00 13.22 ? 120 ALA   A CA  1 
ATOM   821  C  C   . ALA   A 1 120 ? -5.426  7.313   6.690   1.00 13.43 ? 120 ALA   A C   1 
ATOM   822  O  O   . ALA   A 1 120 ? -4.699  8.124   7.295   1.00 14.38 ? 120 ALA   A O   1 
ATOM   823  C  CB  . ALA   A 1 120 ? -7.626  7.438   7.841   1.00 17.15 ? 120 ALA   A CB  1 
ATOM   824  N  N   . VAL   A 1 121 ? -5.355  7.123   5.382   1.00 13.22 ? 121 VAL   A N   1 
ATOM   825  C  CA  . VAL   A 1 121 ? -4.551  7.952   4.511   1.00 14.67 ? 121 VAL   A CA  1 
ATOM   826  C  C   . VAL   A 1 121 ? -5.551  8.693   3.655   1.00 13.64 ? 121 VAL   A C   1 
ATOM   827  O  O   . VAL   A 1 121 ? -6.336  8.102   2.929   1.00 15.85 ? 121 VAL   A O   1 
ATOM   828  C  CB  . VAL   A 1 121 ? -3.547  7.136   3.642   1.00 17.22 ? 121 VAL   A CB  1 
ATOM   829  C  CG1 . VAL   A 1 121 ? -2.771  8.089   2.759   1.00 21.46 ? 121 VAL   A CG1 1 
ATOM   830  C  CG2 . VAL   A 1 121 ? -2.634  6.359   4.581   1.00 24.96 ? 121 VAL   A CG2 1 
ATOM   831  N  N   . VAL   A 1 122 ? -5.495  10.010  3.714   1.00 13.82 ? 122 VAL   A N   1 
ATOM   832  C  CA  . VAL   A 1 122 ? -6.479  10.898  3.054   1.00 14.78 ? 122 VAL   A CA  1 
ATOM   833  C  C   . VAL   A 1 122 ? -5.700  11.805  2.109   1.00 15.94 ? 122 VAL   A C   1 
ATOM   834  O  O   . VAL   A 1 122 ? -4.797  12.469  2.499   1.00 17.93 ? 122 VAL   A O   1 
ATOM   835  C  CB  . VAL   A 1 122 ? -7.301  11.691  4.077   1.00 16.22 ? 122 VAL   A CB  1 
ATOM   836  C  CG1 . VAL   A 1 122 ? -8.328  12.572  3.364   1.00 18.35 ? 122 VAL   A CG1 1 
ATOM   837  C  CG2 . VAL   A 1 122 ? -7.944  10.768  5.105   1.00 18.93 ? 122 VAL   A CG2 1 
ATOM   838  N  N   . THR   A 1 123 ? -6.042  11.702  0.838   1.00 16.83 ? 123 THR   A N   1 
ATOM   839  C  CA  . THR   A 1 123 ? -5.328  12.477  -0.200  1.00 20.04 ? 123 THR   A CA  1 
ATOM   840  C  C   . THR   A 1 123 ? -6.317  13.344  -0.971  1.00 21.71 ? 123 THR   A C   1 
ATOM   841  O  O   . THR   A 1 123 ? -7.496  13.032  -1.034  1.00 21.48 ? 123 THR   A O   1 
ATOM   842  C  CB  . THR   A 1 123 ? -4.541  11.526  -1.107  1.00 31.83 ? 123 THR   A CB  1 
ATOM   843  O  OG1 . THR   A 1 123 ? -5.439  10.671  -1.813  1.00 32.23 ? 123 THR   A OG1 1 
ATOM   844  C  CG2 . THR   A 1 123 ? -3.540  10.696  -0.333  0.70 20.33 ? 123 THR   A CG2 1 
ATOM   845  N  N   . ASN   A 1 124 ? -5.793  14.414  -1.541  0.70 23.68 ? 124 ASN   A N   1 
ATOM   846  C  CA  . ASN   A 1 124 ? -6.617  15.313  -2.241  0.70 26.34 ? 124 ASN   A CA  1 
ATOM   847  C  C   . ASN   A 1 124 ? -6.230  15.143  -3.663  0.70 33.28 ? 124 ASN   A C   1 
ATOM   848  O  O   . ASN   A 1 124 ? -5.175  15.567  -4.015  0.70 36.70 ? 124 ASN   A O   1 
ATOM   849  C  CB  . ASN   A 1 124 ? -6.335  16.757  -1.791  0.70 27.95 ? 124 ASN   A CB  1 
ATOM   850  C  CG  . ASN   A 1 124 ? -7.239  17.709  -2.447  0.70 28.01 ? 124 ASN   A CG  1 
ATOM   851  O  OD1 . ASN   A 1 124 ? -7.736  17.435  -3.555  0.70 37.80 ? 124 ASN   A OD1 1 
ATOM   852  N  ND2 . ASN   A 1 124 ? -7.423  18.866  -1.815  0.70 37.63 ? 124 ASN   A ND2 1 
ATOM   853  N  N   . PRO   A 1 125 ? -7.102  14.566  -4.500  0.70 36.00 ? 125 PRO   A N   1 
ATOM   854  C  CA  . PRO   A 1 125 ? -6.738  14.283  -5.889  0.70 47.32 ? 125 PRO   A CA  1 
ATOM   855  C  C   . PRO   A 1 125 ? -6.767  15.527  -6.770  0.70 47.92 ? 125 PRO   A C   1 
ATOM   856  O  O   . PRO   A 1 125 ? -5.719  15.936  -7.223  0.70 48.26 ? 125 PRO   A O   1 
ATOM   857  C  CB  . PRO   A 1 125 ? -7.831  13.308  -6.324  0.70 51.67 ? 125 PRO   A CB  1 
ATOM   858  C  CG  . PRO   A 1 125 ? -9.041  13.751  -5.532  0.70 44.62 ? 125 PRO   A CG  1 
ATOM   859  C  CD  . PRO   A 1 125 ? -8.561  14.542  -4.340  0.70 35.57 ? 125 PRO   A CD  1 
ATOM   860  C  C   . CYS   B 1 10  ? -12.466 -5.689  37.566  1.00 43.88 ? 10  CYS   B C   1 
ATOM   861  O  O   . CYS   B 1 10  ? -11.354 -5.828  37.094  1.00 46.19 ? 10  CYS   B O   1 
ATOM   862  N  N   . PRO   B 1 11  ? -13.562 -6.047  36.873  1.00 26.06 ? 11  PRO   B N   1 
ATOM   863  C  CA  . PRO   B 1 11  ? -13.312 -6.848  35.728  1.00 23.29 ? 11  PRO   B CA  1 
ATOM   864  C  C   . PRO   B 1 11  ? -13.003 -6.132  34.409  1.00 19.68 ? 11  PRO   B C   1 
ATOM   865  O  O   . PRO   B 1 11  ? -12.675 -6.775  33.471  1.00 21.27 ? 11  PRO   B O   1 
ATOM   866  C  CB  . PRO   B 1 11  ? -14.581 -7.655  35.544  1.00 34.58 ? 11  PRO   B CB  1 
ATOM   867  C  CG  . PRO   B 1 11  ? -15.594 -6.984  36.272  1.00 34.78 ? 11  PRO   B CG  1 
ATOM   868  C  CD  . PRO   B 1 11  ? -14.989 -6.061  37.268  1.00 28.37 ? 11  PRO   B CD  1 
ATOM   869  N  N   . LEU   B 1 12  ? -13.199 -4.833  34.385  1.00 18.72 ? 12  LEU   B N   1 
ATOM   870  C  CA  . LEU   B 1 12  ? -13.014 -4.094  33.141  1.00 18.09 ? 12  LEU   B CA  1 
ATOM   871  C  C   . LEU   B 1 12  ? -12.317 -2.793  33.463  1.00 18.85 ? 12  LEU   B C   1 
ATOM   872  O  O   . LEU   B 1 12  ? -12.796 -2.020  34.253  1.00 24.13 ? 12  LEU   B O   1 
ATOM   873  C  CB  . LEU   B 1 12  ? -14.400 -3.808  32.499  1.00 19.51 ? 12  LEU   B CB  1 
ATOM   874  C  CG  . LEU   B 1 12  ? -14.366 -3.054  31.157  1.00 21.29 ? 12  LEU   B CG  1 
ATOM   875  C  CD1 . LEU   B 1 12  ? -13.571 -3.814  30.131  1.00 21.30 ? 12  LEU   B CD1 1 
ATOM   876  C  CD2 . LEU   B 1 12  ? -15.800 -2.782  30.691  1.00 27.17 ? 12  LEU   B CD2 1 
ATOM   877  N  N   . MET   B 1 13  ? -11.201 -2.546  32.795  1.00 16.73 ? 13  MET   B N   1 
ATOM   878  C  CA  A MET   B 1 13  ? -10.449 -1.303  32.900  0.50 17.13 ? 13  MET   B CA  1 
ATOM   879  C  CA  B MET   B 1 13  ? -10.399 -1.367  32.907  0.50 18.21 ? 13  MET   B CA  1 
ATOM   880  C  C   . MET   B 1 13  ? -10.105 -0.867  31.481  1.00 14.91 ? 13  MET   B C   1 
ATOM   881  O  O   . MET   B 1 13  ? -9.895  -1.676  30.597  1.00 16.17 ? 13  MET   B O   1 
ATOM   882  C  CB  A MET   B 1 13  ? -9.154  -1.475  33.726  0.50 22.24 ? 13  MET   B CB  1 
ATOM   883  C  CB  B MET   B 1 13  ? -9.076  -1.760  33.579  0.50 19.61 ? 13  MET   B CB  1 
ATOM   884  C  CG  A MET   B 1 13  ? -8.419  -0.172  34.080  0.50 22.56 ? 13  MET   B CG  1 
ATOM   885  C  CG  B MET   B 1 13  ? -8.105  -0.611  33.624  0.50 27.70 ? 13  MET   B CG  1 
ATOM   886  S  SD  A MET   B 1 13  ? -7.120  0.325   32.912  0.50 20.98 ? 13  MET   B SD  1 
ATOM   887  S  SD  B MET   B 1 13  ? -6.825  -0.883  34.825  0.50 47.93 ? 13  MET   B SD  1 
ATOM   888  C  CE  A MET   B 1 13  ? -5.743  -0.675  33.440  0.50 20.93 ? 13  MET   B CE  1 
ATOM   889  C  CE  B MET   B 1 13  ? -5.630  0.356   34.330  0.50 48.49 ? 13  MET   B CE  1 
ATOM   890  N  N   . VAL   B 1 14  ? -10.062 0.429   31.316  1.00 14.01 ? 14  VAL   B N   1 
ATOM   891  C  CA  . VAL   B 1 14  ? -9.690  1.044   30.035  1.00 14.30 ? 14  VAL   B CA  1 
ATOM   892  C  C   . VAL   B 1 14  ? -8.510  1.944   30.287  1.00 14.84 ? 14  VAL   B C   1 
ATOM   893  O  O   . VAL   B 1 14  ? -8.530  2.731   31.205  1.00 18.20 ? 14  VAL   B O   1 
ATOM   894  C  CB  . VAL   B 1 14  ? -10.879 1.808   29.420  1.00 15.41 ? 14  VAL   B CB  1 
ATOM   895  C  CG1 . VAL   B 1 14  ? -10.502 2.469   28.129  1.00 17.06 ? 14  VAL   B CG1 1 
ATOM   896  C  CG2 . VAL   B 1 14  ? -12.102 0.849   29.255  1.00 17.27 ? 14  VAL   B CG2 1 
ATOM   897  N  N   . LYS   B 1 15  ? -7.515  1.863   29.403  1.00 13.88 ? 15  LYS   B N   1 
ATOM   898  C  CA  . LYS   B 1 15  ? -6.313  2.667   29.479  1.00 14.02 ? 15  LYS   B CA  1 
ATOM   899  C  C   . LYS   B 1 15  ? -6.088  3.308   28.125  1.00 13.43 ? 15  LYS   B C   1 
ATOM   900  O  O   . LYS   B 1 15  ? -6.128  2.598   27.130  1.00 15.85 ? 15  LYS   B O   1 
ATOM   901  C  CB  . LYS   B 1 15  ? -5.079  1.804   29.884  1.00 16.98 ? 15  LYS   B CB  1 
ATOM   902  C  CG  . LYS   B 1 15  ? -3.854  2.677   30.042  1.00 26.58 ? 15  LYS   B CG  1 
ATOM   903  C  CD  . LYS   B 1 15  ? -2.731  1.955   30.746  0.50 25.73 ? 15  LYS   B CD  1 
ATOM   904  C  CE  . LYS   B 1 15  ? -1.555  2.913   31.041  0.50 32.01 ? 15  LYS   B CE  1 
ATOM   905  N  NZ  . LYS   B 1 15  ? -0.803  2.492   32.266  0.50 33.83 ? 15  LYS   B NZ  1 
ATOM   906  N  N   . VAL   B 1 16  ? -5.827  4.600   28.107  1.00 13.84 ? 16  VAL   B N   1 
ATOM   907  C  CA  . VAL   B 1 16  ? -5.685  5.343   26.874  1.00 13.35 ? 16  VAL   B CA  1 
ATOM   908  C  C   . VAL   B 1 16  ? -4.383  6.148   26.910  1.00 13.21 ? 16  VAL   B C   1 
ATOM   909  O  O   . VAL   B 1 16  ? -4.150  6.872   27.878  1.00 14.49 ? 16  VAL   B O   1 
ATOM   910  C  CB  . VAL   B 1 16  ? -6.914  6.244   26.609  1.00 13.58 ? 16  VAL   B CB  1 
ATOM   911  C  CG1 . VAL   B 1 16  ? -6.883  6.826   25.231  1.00 16.27 ? 16  VAL   B CG1 1 
ATOM   912  C  CG2 . VAL   B 1 16  ? -8.241  5.532   26.851  1.00 15.71 ? 16  VAL   B CG2 1 
ATOM   913  N  N   . LEU   B 1 17  ? -3.623  6.066   25.837  1.00 12.03 ? 17  LEU   B N   1 
ATOM   914  C  CA  . LEU   B 1 17  ? -2.361  6.768   25.659  1.00 12.36 ? 17  LEU   B CA  1 
ATOM   915  C  C   . LEU   B 1 17  ? -2.432  7.659   24.441  1.00 11.25 ? 17  LEU   B C   1 
ATOM   916  O  O   . LEU   B 1 17  ? -3.101  7.358   23.448  1.00 13.43 ? 17  LEU   B O   1 
ATOM   917  C  CB  . LEU   B 1 17  ? -1.192  5.800   25.516  1.00 14.44 ? 17  LEU   B CB  1 
ATOM   918  C  CG  . LEU   B 1 17  ? -0.865  4.907   26.748  1.00 17.45 ? 17  LEU   B CG  1 
ATOM   919  C  CD1 . LEU   B 1 17  ? 0.363   4.038   26.335  1.00 21.78 ? 17  LEU   B CD1 1 
ATOM   920  C  CD2 . LEU   B 1 17  ? -0.659  5.711   27.983  1.00 20.25 ? 17  LEU   B CD2 1 
ATOM   921  N  N   . ASP   B 1 18  ? -1.690  8.767   24.482  1.00 11.88 ? 18  ASP   B N   1 
ATOM   922  C  CA  . ASP   B 1 18  ? -1.593  9.757   23.440  1.00 11.62 ? 18  ASP   B CA  1 
ATOM   923  C  C   . ASP   B 1 18  ? -0.199  9.702   22.818  1.00 12.01 ? 18  ASP   B C   1 
ATOM   924  O  O   . ASP   B 1 18  ? 0.808   9.970   23.459  1.00 12.97 ? 18  ASP   B O   1 
ATOM   925  C  CB  . ASP   B 1 18  ? -1.820  11.143  24.083  1.00 12.46 ? 18  ASP   B CB  1 
ATOM   926  C  CG  . ASP   B 1 18  ? -1.680  12.328  23.171  1.00 13.07 ? 18  ASP   B CG  1 
ATOM   927  O  OD1 . ASP   B 1 18  ? -0.974  12.229  22.185  1.00 13.87 ? 18  ASP   B OD1 1 
ATOM   928  O  OD2 . ASP   B 1 18  ? -2.284  13.358  23.524  1.00 16.71 ? 18  ASP   B OD2 1 
ATOM   929  N  N   . ALA   B 1 19  ? -0.159  9.266   21.570  1.00 11.72 ? 19  ALA   B N   1 
ATOM   930  C  CA  . ALA   B 1 19  ? 1.056   9.044   20.784  1.00 12.89 ? 19  ALA   B CA  1 
ATOM   931  C  C   . ALA   B 1 19  ? 1.681   10.328  20.264  1.00 13.33 ? 19  ALA   B C   1 
ATOM   932  O  O   . ALA   B 1 19  ? 2.808   10.291  19.730  1.00 16.15 ? 19  ALA   B O   1 
ATOM   933  C  CB  . ALA   B 1 19  ? 0.761   8.072   19.616  1.00 13.95 ? 19  ALA   B CB  1 
ATOM   934  N  N   . VAL   B 1 20  ? 0.964   11.442  20.312  1.00 13.27 ? 20  VAL   B N   1 
ATOM   935  C  CA  . VAL   B 1 20  ? 1.455   12.730  19.903  1.00 14.85 ? 20  VAL   B CA  1 
ATOM   936  C  C   . VAL   B 1 20  ? 2.248   13.423  20.995  1.00 15.91 ? 20  VAL   B C   1 
ATOM   937  O  O   . VAL   B 1 20  ? 3.340   13.971  20.770  1.00 20.00 ? 20  VAL   B O   1 
ATOM   938  C  CB  . VAL   B 1 20  ? 0.320   13.643  19.372  1.00 15.40 ? 20  VAL   B CB  1 
ATOM   939  C  CG1 . VAL   B 1 20  ? 0.805   15.101  19.177  1.00 19.79 ? 20  VAL   B CG1 1 
ATOM   940  C  CG2 . VAL   B 1 20  ? -0.276  13.032  18.141  1.00 18.70 ? 20  VAL   B CG2 1 
ATOM   941  N  N   . ARG   B 1 21  ? 1.707   13.373  22.171  1.00 14.61 ? 21  ARG   B N   1 
ATOM   942  C  CA  . ARG   B 1 21  ? 2.275   14.029  23.344  1.00 16.43 ? 21  ARG   B CA  1 
ATOM   943  C  C   . ARG   B 1 21  ? 3.147   13.117  24.153  1.00 14.40 ? 21  ARG   B C   1 
ATOM   944  O  O   . ARG   B 1 21  ? 3.908   13.594  24.983  1.00 18.20 ? 21  ARG   B O   1 
ATOM   945  C  CB  . ARG   B 1 21  ? 1.142   14.612  24.183  1.00 20.65 ? 21  ARG   B CB  1 
ATOM   946  C  CG  . ARG   B 1 21  ? 0.404   15.762  23.501  0.50 20.19 ? 21  ARG   B CG  1 
ATOM   947  C  CD  . ARG   B 1 21  ? -0.789  16.264  24.376  0.50 26.23 ? 21  ARG   B CD  1 
ATOM   948  N  NE  . ARG   B 1 21  ? -0.421  16.994  25.583  0.50 30.46 ? 21  ARG   B NE  1 
ATOM   949  C  CZ  . ARG   B 1 21  ? -1.171  17.933  26.157  0.50 31.16 ? 21  ARG   B CZ  1 
ATOM   950  N  N   . GLY   B 1 22  ? 3.054   11.802  23.986  1.00 13.87 ? 22  GLY   B N   1 
ATOM   951  C  CA  . GLY   B 1 22  ? 3.778   10.867  24.815  1.00 14.23 ? 22  GLY   B CA  1 
ATOM   952  C  C   . GLY   B 1 22  ? 3.315   10.914  26.243  1.00 13.44 ? 22  GLY   B C   1 
ATOM   953  O  O   . GLY   B 1 22  ? 4.120   10.986  27.159  1.00 13.88 ? 22  GLY   B O   1 
ATOM   954  N  N   . SER   B 1 23  ? 2.037   10.727  26.415  1.00 14.40 ? 23  SER   B N   1 
ATOM   955  C  CA  . SER   B 1 23  ? 1.451   10.882  27.747  1.00 15.85 ? 23  SER   B CA  1 
ATOM   956  C  C   . SER   B 1 23  ? 0.227   10.032  27.860  1.00 14.45 ? 23  SER   B C   1 
ATOM   957  O  O   . SER   B 1 23  ? -0.353  9.649   26.837  1.00 15.51 ? 23  SER   B O   1 
ATOM   958  C  CB  . SER   B 1 23  ? 1.059   12.350  27.986  1.00 18.77 ? 23  SER   B CB  1 
ATOM   959  O  OG  . SER   B 1 23  ? -0.023  12.666  27.155  1.00 22.29 ? 23  SER   B OG  1 
ATOM   960  N  N   . PRO   B 1 24  ? -0.256  9.804   29.066  1.00 14.26 ? 24  PRO   B N   1 
ATOM   961  C  CA  . PRO   B 1 24  ? -1.644  9.317   29.192  1.00 15.74 ? 24  PRO   B CA  1 
ATOM   962  C  C   . PRO   B 1 24  ? -2.603  10.282  28.536  1.00 14.39 ? 24  PRO   B C   1 
ATOM   963  O  O   . PRO   B 1 24  ? -2.352  11.471  28.464  1.00 15.92 ? 24  PRO   B O   1 
ATOM   964  C  CB  . PRO   B 1 24  ? -1.881  9.336   30.688  1.00 17.52 ? 24  PRO   B CB  1 
ATOM   965  C  CG  . PRO   B 1 24  ? -0.855  10.301  31.196  1.00 26.75 ? 24  PRO   B CG  1 
ATOM   966  C  CD  . PRO   B 1 24  ? 0.338   10.128  30.359  1.00 15.92 ? 24  PRO   B CD  1 
ATOM   967  N  N   . ALA   B 1 25  ? -3.705  9.773   27.992  1.00 14.29 ? 25  ALA   B N   1 
ATOM   968  C  CA  . ALA   B 1 25  ? -4.755  10.584  27.463  1.00 14.28 ? 25  ALA   B CA  1 
ATOM   969  C  C   . ALA   B 1 25  ? -5.735  10.818  28.595  1.00 13.95 ? 25  ALA   B C   1 
ATOM   970  O  O   . ALA   B 1 25  ? -6.455  9.886   28.984  1.00 14.57 ? 25  ALA   B O   1 
ATOM   971  C  CB  . ALA   B 1 25  ? -5.411  9.913   26.252  1.00 15.44 ? 25  ALA   B CB  1 
ATOM   972  N  N   . ILE   B 1 26  ? -5.778  12.037  29.136  1.00 15.30 ? 26  ILE   B N   1 
ATOM   973  C  CA  . ILE   B 1 26  ? -6.500  12.381  30.316  1.00 15.58 ? 26  ILE   B CA  1 
ATOM   974  C  C   . ILE   B 1 26  ? -7.855  12.970  29.932  1.00 15.25 ? 26  ILE   B C   1 
ATOM   975  O  O   . ILE   B 1 26  ? -8.008  13.667  28.928  1.00 16.53 ? 26  ILE   B O   1 
ATOM   976  C  CB  . ILE   B 1 26  ? -5.706  13.404  31.142  1.00 20.17 ? 26  ILE   B CB  1 
ATOM   977  C  CG1 . ILE   B 1 26  ? -4.342  12.762  31.489  1.00 19.88 ? 26  ILE   B CG1 1 
ATOM   978  C  CG2 . ILE   B 1 26  ? -6.474  13.840  32.344  1.00 28.59 ? 26  ILE   B CG2 1 
ATOM   979  C  CD1 . ILE   B 1 26  ? -3.247  13.799  31.875  1.00 33.27 ? 26  ILE   B CD1 1 
ATOM   980  N  N   . ASN   B 1 27  ? -8.871  12.692  30.759  1.00 15.78 ? 27  ASN   B N   1 
ATOM   981  C  CA  . ASN   B 1 27  ? -10.196 13.234  30.564  1.00 15.82 ? 27  ASN   B CA  1 
ATOM   982  C  C   . ASN   B 1 27  ? -10.873 12.782  29.288  1.00 16.48 ? 27  ASN   B C   1 
ATOM   983  O  O   . ASN   B 1 27  ? -11.667 13.506  28.715  1.00 20.03 ? 27  ASN   B O   1 
ATOM   984  C  CB  . ASN   B 1 27  ? -10.212 14.727  30.731  1.00 18.06 ? 27  ASN   B CB  1 
ATOM   985  C  CG  . ASN   B 1 27  ? -9.877  15.143  32.132  1.00 24.14 ? 27  ASN   B CG  1 
ATOM   986  O  OD1 . ASN   B 1 27  ? -10.334 14.509  33.133  1.00 28.93 ? 27  ASN   B OD1 1 
ATOM   987  N  ND2 . ASN   B 1 27  ? -9.106  16.243  32.238  1.00 29.28 ? 27  ASN   B ND2 1 
ATOM   988  N  N   . VAL   B 1 28  ? -10.576 11.576  28.868  1.00 15.41 ? 28  VAL   B N   1 
ATOM   989  C  CA  . VAL   B 1 28  ? -11.233 11.028  27.696  1.00 15.37 ? 28  VAL   B CA  1 
ATOM   990  C  C   . VAL   B 1 28  ? -12.506 10.327  28.174  1.00 14.47 ? 28  VAL   B C   1 
ATOM   991  O  O   . VAL   B 1 28  ? -12.477 9.457   29.031  1.00 15.76 ? 28  VAL   B O   1 
ATOM   992  C  CB  . VAL   B 1 28  ? -10.314 9.971   26.983  1.00 15.06 ? 28  VAL   B CB  1 
ATOM   993  C  CG1 . VAL   B 1 28  ? -11.003 9.323   25.812  1.00 17.45 ? 28  VAL   B CG1 1 
ATOM   994  C  CG2 . VAL   B 1 28  ? -8.976  10.595  26.544  1.00 17.90 ? 28  VAL   B CG2 1 
ATOM   995  N  N   . ALA   B 1 29  ? -13.611 10.647  27.531  1.00 14.86 ? 29  ALA   B N   1 
ATOM   996  C  CA  . ALA   B 1 29  ? -14.905 10.010  27.845  1.00 14.59 ? 29  ALA   B CA  1 
ATOM   997  C  C   . ALA   B 1 29  ? -14.947 8.616   27.241  1.00 14.12 ? 29  ALA   B C   1 
ATOM   998  O  O   . ALA   B 1 29  ? -14.558 8.437   26.098  1.00 14.83 ? 29  ALA   B O   1 
ATOM   999  C  CB  . ALA   B 1 29  ? -16.084 10.839  27.317  1.00 16.99 ? 29  ALA   B CB  1 
ATOM   1000 N  N   . VAL   B 1 30  ? -15.478 7.698   28.016  1.00 13.98 ? 30  VAL   B N   1 
ATOM   1001 C  CA  . VAL   B 1 30  ? -15.611 6.301   27.624  1.00 13.59 ? 30  VAL   B CA  1 
ATOM   1002 C  C   . VAL   B 1 30  ? -17.015 5.851   28.020  1.00 14.41 ? 30  VAL   B C   1 
ATOM   1003 O  O   . VAL   B 1 30  ? -17.433 6.045   29.157  1.00 16.01 ? 30  VAL   B O   1 
ATOM   1004 C  CB  . VAL   B 1 30  ? -14.596 5.434   28.350  1.00 14.38 ? 30  VAL   B CB  1 
ATOM   1005 C  CG1 . VAL   B 1 30  ? -14.759 3.966   27.962  1.00 16.74 ? 30  VAL   B CG1 1 
ATOM   1006 C  CG2 . VAL   B 1 30  ? -13.167 5.933   28.083  1.00 16.34 ? 30  VAL   B CG2 1 
ATOM   1007 N  N   . HIS   B 1 31  ? -17.710 5.244   27.087  1.00 14.56 ? 31  HIS   B N   1 
ATOM   1008 C  CA  . HIS   B 1 31  ? -19.060 4.698   27.287  1.00 14.58 ? 31  HIS   B CA  1 
ATOM   1009 C  C   . HIS   B 1 31  ? -19.031 3.202   26.974  1.00 14.08 ? 31  HIS   B C   1 
ATOM   1010 O  O   . HIS   B 1 31  ? -18.464 2.814   25.979  1.00 16.00 ? 31  HIS   B O   1 
ATOM   1011 C  CB  . HIS   B 1 31  ? -20.058 5.391   26.368  1.00 17.86 ? 31  HIS   B CB  1 
ATOM   1012 C  CG  . HIS   B 1 31  ? -20.317 6.833   26.815  1.00 20.07 ? 31  HIS   B CG  1 
ATOM   1013 N  ND1 . HIS   B 1 31  ? -19.518 7.875   26.583  1.00 26.61 ? 31  HIS   B ND1 1 
ATOM   1014 C  CD2 . HIS   B 1 31  ? -21.368 7.299   27.566  1.00 21.48 ? 31  HIS   B CD2 1 
ATOM   1015 C  CE1 . HIS   B 1 31  ? -20.069 8.970   27.141  1.00 22.73 ? 31  HIS   B CE1 1 
ATOM   1016 N  NE2 . HIS   B 1 31  ? -21.157 8.593   27.773  1.00 29.59 ? 31  HIS   B NE2 1 
ATOM   1017 N  N   . VAL   B 1 32  ? -19.691 2.442   27.807  1.00 15.05 ? 32  VAL   B N   1 
ATOM   1018 C  CA  . VAL   B 1 32  ? -19.734 0.984   27.639  1.00 15.10 ? 32  VAL   B CA  1 
ATOM   1019 C  C   . VAL   B 1 32  ? -21.206 0.575   27.427  1.00 15.36 ? 32  VAL   B C   1 
ATOM   1020 O  O   . VAL   B 1 32  ? -22.129 1.098   28.124  1.00 18.19 ? 32  VAL   B O   1 
ATOM   1021 C  CB  . VAL   B 1 32  ? -19.147 0.274   28.857  1.00 15.90 ? 32  VAL   B CB  1 
ATOM   1022 C  CG1 . VAL   B 1 32  ? -19.035 -1.273  28.644  1.00 16.43 ? 32  VAL   B CG1 1 
ATOM   1023 C  CG2 . VAL   B 1 32  ? -17.763 0.831   29.217  1.00 18.81 ? 32  VAL   B CG2 1 
ATOM   1024 N  N   . PHE   B 1 33  ? -21.443 -0.360  26.522  1.00 15.80 ? 33  PHE   B N   1 
ATOM   1025 C  CA  . PHE   B 1 33  ? -22.753 -0.800  26.161  1.00 16.49 ? 33  PHE   B CA  1 
ATOM   1026 C  C   . PHE   B 1 33  ? -22.765 -2.334  26.188  1.00 16.89 ? 33  PHE   B C   1 
ATOM   1027 O  O   . PHE   B 1 33  ? -21.737 -2.954  25.956  1.00 16.01 ? 33  PHE   B O   1 
ATOM   1028 C  CB  . PHE   B 1 33  ? -23.126 -0.357  24.758  1.00 18.63 ? 33  PHE   B CB  1 
ATOM   1029 C  CG  . PHE   B 1 33  ? -22.983 1.112   24.476  1.00 21.05 ? 33  PHE   B CG  1 
ATOM   1030 C  CD1 . PHE   B 1 33  ? -21.750 1.694   24.213  1.00 19.56 ? 33  PHE   B CD1 1 
ATOM   1031 C  CD2 . PHE   B 1 33  ? -24.098 1.883   24.384  1.00 30.17 ? 33  PHE   B CD2 1 
ATOM   1032 C  CE1 . PHE   B 1 33  ? -21.679 3.037   23.921  1.00 23.20 ? 33  PHE   B CE1 1 
ATOM   1033 C  CE2 . PHE   B 1 33  ? -24.030 3.202   24.066  1.00 34.17 ? 33  PHE   B CE2 1 
ATOM   1034 C  CZ  . PHE   B 1 33  ? -22.825 3.802   23.865  1.00 34.15 ? 33  PHE   B CZ  1 
ATOM   1035 N  N   . ARG   B 1 34  ? -23.953 -2.891  26.407  1.00 17.50 ? 34  ARG   B N   1 
ATOM   1036 C  CA  . ARG   B 1 34  ? -24.142 -4.349  26.328  1.00 18.33 ? 34  ARG   B CA  1 
ATOM   1037 C  C   . ARG   B 1 34  ? -25.174 -4.528  25.229  1.00 19.57 ? 34  ARG   B C   1 
ATOM   1038 O  O   . ARG   B 1 34  ? -26.110 -3.734  25.145  1.00 24.31 ? 34  ARG   B O   1 
ATOM   1039 C  CB  . ARG   B 1 34  ? -24.622 -4.918  27.666  1.00 20.01 ? 34  ARG   B CB  1 
ATOM   1040 N  N   . LYS   B 1 35  ? -24.956 -5.494  24.382  1.00 20.75 ? 35  LYS   B N   1 
ATOM   1041 C  CA  . LYS   B 1 35  ? -25.899 -5.777  23.334  1.00 23.43 ? 35  LYS   B CA  1 
ATOM   1042 C  C   . LYS   B 1 35  ? -27.114 -6.422  23.930  1.00 23.49 ? 35  LYS   B C   1 
ATOM   1043 O  O   . LYS   B 1 35  ? -27.032 -7.406  24.681  1.00 25.14 ? 35  LYS   B O   1 
ATOM   1044 C  CB  . LYS   B 1 35  ? -25.240 -6.655  22.267  1.00 24.98 ? 35  LYS   B CB  1 
ATOM   1045 C  CG  . LYS   B 1 35  ? -25.862 -6.562  20.886  1.00 30.31 ? 35  LYS   B CG  1 
ATOM   1046 C  CD  . LYS   B 1 35  ? -24.967 -7.290  19.903  1.00 36.34 ? 35  LYS   B CD  1 
ATOM   1047 C  CE  . LYS   B 1 35  ? -25.019 -6.643  18.544  0.50 36.18 ? 35  LYS   B CE  1 
ATOM   1048 N  NZ  . LYS   B 1 35  ? -24.707 -7.646  17.498  0.50 37.17 ? 35  LYS   B NZ  1 
ATOM   1049 N  N   . ALA   B 1 36  ? -28.285 -5.889  23.621  1.00 25.60 ? 36  ALA   B N   1 
ATOM   1050 C  CA  . ALA   B 1 36  ? -29.596 -6.340  24.036  1.00 24.83 ? 36  ALA   B CA  1 
ATOM   1051 C  C   . ALA   B 1 36  ? -30.109 -7.476  23.121  1.00 32.12 ? 36  ALA   B C   1 
ATOM   1052 O  O   . ALA   B 1 36  ? -29.581 -7.705  22.014  1.00 32.17 ? 36  ALA   B O   1 
ATOM   1053 C  CB  . ALA   B 1 36  ? -30.576 -5.122  24.075  1.00 31.33 ? 36  ALA   B CB  1 
ATOM   1054 N  N   . ALA   B 1 37  ? -31.124 -8.189  23.568  1.00 30.52 ? 37  ALA   B N   1 
ATOM   1055 C  CA  . ALA   B 1 37  ? -31.743 -9.277  22.763  1.00 36.03 ? 37  ALA   B CA  1 
ATOM   1056 C  C   . ALA   B 1 37  ? -32.295 -8.772  21.395  1.00 37.48 ? 37  ALA   B C   1 
ATOM   1057 O  O   . ALA   B 1 37  ? -32.316 -9.543  20.427  1.00 56.05 ? 37  ALA   B O   1 
ATOM   1058 C  CB  . ALA   B 1 37  ? -32.812 -9.987  23.578  1.00 39.79 ? 37  ALA   B CB  1 
ATOM   1059 N  N   . ASP   B 1 38  ? -32.673 -7.476  21.296  1.00 37.06 ? 38  ASP   B N   1 
ATOM   1060 C  CA  . ASP   B 1 38  ? -33.217 -6.903  20.036  1.00 35.37 ? 38  ASP   B CA  1 
ATOM   1061 C  C   . ASP   B 1 38  ? -32.067 -6.419  19.121  1.00 41.47 ? 38  ASP   B C   1 
ATOM   1062 O  O   . ASP   B 1 38  ? -32.290 -5.651  18.143  1.00 45.12 ? 38  ASP   B O   1 
ATOM   1063 C  CB  . ASP   B 1 38  ? -34.306 -5.817  20.330  1.00 40.77 ? 38  ASP   B CB  1 
ATOM   1064 C  CG  . ASP   B 1 38  ? -33.772 -4.595  21.044  0.50 36.51 ? 38  ASP   B CG  1 
ATOM   1065 O  OD1 . ASP   B 1 38  ? -32.566 -4.539  21.236  0.50 29.20 ? 38  ASP   B OD1 1 
ATOM   1066 O  OD2 . ASP   B 1 38  ? -34.522 -3.643  21.372  0.50 37.58 ? 38  ASP   B OD2 1 
ATOM   1067 N  N   . ASP   B 1 39  ? -30.831 -6.857  19.428  1.00 38.23 ? 39  ASP   B N   1 
ATOM   1068 C  CA  . ASP   B 1 39  ? -29.609 -6.417  18.687  1.00 41.17 ? 39  ASP   B CA  1 
ATOM   1069 C  C   . ASP   B 1 39  ? -29.260 -4.917  18.819  1.00 42.23 ? 39  ASP   B C   1 
ATOM   1070 O  O   . ASP   B 1 39  ? -28.316 -4.458  18.158  1.00 43.00 ? 39  ASP   B O   1 
ATOM   1071 C  CB  . ASP   B 1 39  ? -29.672 -6.817  17.181  0.50 36.91 ? 39  ASP   B CB  1 
ATOM   1072 C  CG  . ASP   B 1 39  ? -28.951 -8.130  16.883  0.50 46.18 ? 39  ASP   B CG  1 
ATOM   1073 O  OD1 . ASP   B 1 39  ? -28.459 -8.767  17.828  0.50 40.26 ? 39  ASP   B OD1 1 
ATOM   1074 O  OD2 . ASP   B 1 39  ? -28.880 -8.529  15.697  0.50 42.54 ? 39  ASP   B OD2 1 
ATOM   1075 N  N   . THR   B 1 40  ? -29.955 -4.177  19.685  0.80 28.91 ? 40  THR   B N   1 
ATOM   1076 C  CA  . THR   B 1 40  ? -29.569 -2.790  20.023  0.80 30.19 ? 40  THR   B CA  1 
ATOM   1077 C  C   . THR   B 1 40  ? -28.502 -2.739  21.136  0.80 25.41 ? 40  THR   B C   1 
ATOM   1078 O  O   . THR   B 1 40  ? -28.329 -3.627  21.870  0.80 23.48 ? 40  THR   B O   1 
ATOM   1079 C  CB  . THR   B 1 40  ? -30.798 -1.927  20.453  0.80 42.26 ? 40  THR   B CB  1 
ATOM   1080 O  OG1 . THR   B 1 40  ? -31.287 -2.343  21.746  0.80 60.64 ? 40  THR   B OG1 1 
ATOM   1081 C  CG2 . THR   B 1 40  ? -31.917 -2.001  19.408  0.80 40.96 ? 40  THR   B CG2 1 
ATOM   1082 N  N   . TRP   B 1 41  ? -27.808 -1.609  21.173  1.00 28.90 ? 41  TRP   B N   1 
ATOM   1083 C  CA  . TRP   B 1 41  ? -26.742 -1.413  22.174  1.00 26.82 ? 41  TRP   B CA  1 
ATOM   1084 C  C   . TRP   B 1 41  ? -27.328 -0.697  23.372  1.00 30.76 ? 41  TRP   B C   1 
ATOM   1085 O  O   . TRP   B 1 41  ? -27.798 0.434   23.219  1.00 41.17 ? 41  TRP   B O   1 
ATOM   1086 C  CB  . TRP   B 1 41  ? -25.599 -0.602  21.556  1.00 27.37 ? 41  TRP   B CB  1 
ATOM   1087 C  CG  . TRP   B 1 41  ? -24.738 -1.393  20.629  1.00 28.84 ? 41  TRP   B CG  1 
ATOM   1088 C  CD1 . TRP   B 1 41  ? -24.603 -1.250  19.280  1.00 37.10 ? 41  TRP   B CD1 1 
ATOM   1089 C  CD2 . TRP   B 1 41  ? -23.880 -2.475  21.008  1.00 21.50 ? 41  TRP   B CD2 1 
ATOM   1090 N  NE1 . TRP   B 1 41  ? -23.714 -2.168  18.794  1.00 33.62 ? 41  TRP   B NE1 1 
ATOM   1091 C  CE2 . TRP   B 1 41  ? -23.255 -2.935  19.832  1.00 25.27 ? 41  TRP   B CE2 1 
ATOM   1092 C  CE3 . TRP   B 1 41  ? -23.581 -3.088  22.225  1.00 20.19 ? 41  TRP   B CE3 1 
ATOM   1093 C  CZ2 . TRP   B 1 41  ? -22.348 -3.990  19.844  1.00 28.69 ? 41  TRP   B CZ2 1 
ATOM   1094 C  CZ3 . TRP   B 1 41  ? -22.686 -4.129  22.234  1.00 23.13 ? 41  TRP   B CZ3 1 
ATOM   1095 C  CH2 . TRP   B 1 41  ? -22.083 -4.571  21.059  1.00 24.38 ? 41  TRP   B CH2 1 
ATOM   1096 N  N   . GLU   B 1 42  ? -27.312 -1.350  24.510  1.00 27.26 ? 42  GLU   B N   1 
ATOM   1097 C  CA  . GLU   B 1 42  ? -27.851 -0.743  25.731  1.00 27.42 ? 42  GLU   B CA  1 
ATOM   1098 C  C   . GLU   B 1 42  ? -26.698 -0.138  26.520  1.00 24.60 ? 42  GLU   B C   1 
ATOM   1099 O  O   . GLU   B 1 42  ? -25.853 -0.869  27.008  1.00 22.46 ? 42  GLU   B O   1 
ATOM   1100 C  CB  . GLU   B 1 42  ? -28.564 -1.813  26.542  1.00 29.57 ? 42  GLU   B CB  1 
ATOM   1101 C  CG  . GLU   B 1 42  ? -29.058 -1.349  27.891  0.50 27.24 ? 42  GLU   B CG  1 
ATOM   1102 C  CD  . GLU   B 1 42  ? -29.688 -2.501  28.649  0.50 30.22 ? 42  GLU   B CD  1 
ATOM   1103 O  OE1 . GLU   B 1 42  ? -30.488 -3.234  28.035  0.50 34.91 ? 42  GLU   B OE1 1 
ATOM   1104 O  OE2 . GLU   B 1 42  ? -29.358 -2.678  29.835  0.50 37.10 ? 42  GLU   B OE2 1 
ATOM   1105 N  N   . PRO   B 1 43  ? -26.664 1.190   26.661  1.00 26.40 ? 43  PRO   B N   1 
ATOM   1106 C  CA  . PRO   B 1 43  ? -25.557 1.821   27.355  1.00 26.53 ? 43  PRO   B CA  1 
ATOM   1107 C  C   . PRO   B 1 43  ? -25.714 1.460   28.825  1.00 24.58 ? 43  PRO   B C   1 
ATOM   1108 O  O   . PRO   B 1 43  ? -26.830 1.510   29.292  1.00 33.99 ? 43  PRO   B O   1 
ATOM   1109 C  CB  . PRO   B 1 43  ? -25.763 3.316   27.089  0.50 21.09 ? 43  PRO   B CB  1 
ATOM   1110 C  CG  . PRO   B 1 43  ? -27.246 3.447   26.798  0.50 20.73 ? 43  PRO   B CG  1 
ATOM   1111 C  CD  . PRO   B 1 43  ? -27.663 2.134   26.166  0.50 22.84 ? 43  PRO   B CD  1 
ATOM   1112 N  N   . PHE   B 1 44  ? -24.632 1.086   29.503  1.00 22.81 ? 44  PHE   B N   1 
ATOM   1113 C  CA  . PHE   B 1 44  ? -24.826 0.810   30.937  1.00 27.70 ? 44  PHE   B CA  1 
ATOM   1114 C  C   . PHE   B 1 44  ? -23.702 1.330   31.838  1.00 32.91 ? 44  PHE   B C   1 
ATOM   1115 O  O   . PHE   B 1 44  ? -23.922 1.298   33.039  1.00 34.74 ? 44  PHE   B O   1 
ATOM   1116 C  CB  . PHE   B 1 44  ? -24.995 -0.687  31.146  1.00 30.34 ? 44  PHE   B CB  1 
ATOM   1117 C  CG  . PHE   B 1 44  ? -23.735 -1.467  30.903  1.00 30.00 ? 44  PHE   B CG  1 
ATOM   1118 C  CD1 . PHE   B 1 44  ? -23.408 -1.893  29.632  1.00 24.56 ? 44  PHE   B CD1 1 
ATOM   1119 C  CD2 . PHE   B 1 44  ? -22.882 -1.774  31.947  1.00 30.59 ? 44  PHE   B CD2 1 
ATOM   1120 C  CE1 . PHE   B 1 44  ? -22.254 -2.623  29.415  1.00 23.05 ? 44  PHE   B CE1 1 
ATOM   1121 C  CE2 . PHE   B 1 44  ? -21.721 -2.490  31.727  1.00 25.82 ? 44  PHE   B CE2 1 
ATOM   1122 C  CZ  . PHE   B 1 44  ? -21.415 -2.917  30.462  1.00 27.19 ? 44  PHE   B CZ  1 
ATOM   1123 N  N   . ALA   B 1 45  ? -22.560 1.767   31.302  1.00 27.73 ? 45  ALA   B N   1 
ATOM   1124 C  CA  . ALA   B 1 45  ? -21.530 2.374   32.170  1.00 24.49 ? 45  ALA   B CA  1 
ATOM   1125 C  C   . ALA   B 1 45  ? -20.720 3.424   31.405  1.00 20.42 ? 45  ALA   B C   1 
ATOM   1126 O  O   . ALA   B 1 45  ? -20.666 3.368   30.189  1.00 22.13 ? 45  ALA   B O   1 
ATOM   1127 C  CB  . ALA   B 1 45  ? -20.613 1.351   32.749  1.00 26.68 ? 45  ALA   B CB  1 
ATOM   1128 N  N   . SER   B 1 46  ? -20.178 4.377   32.155  1.00 18.75 ? 46  SER   B N   1 
ATOM   1129 C  CA  . SER   B 1 46  ? -19.342 5.411   31.511  1.00 16.94 ? 46  SER   B CA  1 
ATOM   1130 C  C   . SER   B 1 46  ? -18.425 6.020   32.524  1.00 17.35 ? 46  SER   B C   1 
ATOM   1131 O  O   . SER   B 1 46  ? -18.617 5.905   33.727  1.00 17.65 ? 46  SER   B O   1 
ATOM   1132 C  CB  . SER   B 1 46  ? -20.155 6.459   30.756  1.00 16.52 ? 46  SER   B CB  1 
ATOM   1133 O  OG  . SER   B 1 46  ? -20.961 7.170   31.668  1.00 18.27 ? 46  SER   B OG  1 
ATOM   1134 N  N   . GLY   B 1 47  ? -17.453 6.775   32.037  1.00 16.53 ? 47  GLY   B N   1 
ATOM   1135 C  CA  . GLY   B 1 47  ? -16.567 7.512   32.878  1.00 15.77 ? 47  GLY   B CA  1 
ATOM   1136 C  C   . GLY   B 1 47  ? -15.575 8.277   32.032  1.00 15.20 ? 47  GLY   B C   1 
ATOM   1137 O  O   . GLY   B 1 47  ? -15.708 8.309   30.812  1.00 16.74 ? 47  GLY   B O   1 
ATOM   1138 N  N   . LYS   B 1 48  ? -14.633 8.912   32.689  1.00 18.36 ? 48  LYS   B N   1 
ATOM   1139 C  CA  A LYS   B 1 48  ? -13.547 9.532   31.926  0.50 16.47 ? 48  LYS   B CA  1 
ATOM   1140 C  CA  B LYS   B 1 48  ? -13.572 9.581   32.028  0.50 17.15 ? 48  LYS   B CA  1 
ATOM   1141 C  C   . LYS   B 1 48  ? -12.217 9.156   32.514  1.00 16.11 ? 48  LYS   B C   1 
ATOM   1142 O  O   . LYS   B 1 48  ? -12.058 8.856   33.701  1.00 17.95 ? 48  LYS   B O   1 
ATOM   1143 C  CB  A LYS   B 1 48  ? -13.692 11.063  31.945  0.50 18.83 ? 48  LYS   B CB  1 
ATOM   1144 C  CB  B LYS   B 1 48  ? -13.686 11.040  32.410  0.50 10.28 ? 48  LYS   B CB  1 
ATOM   1145 C  CG  A LYS   B 1 48  ? -13.540 11.692  33.373  0.50 25.72 ? 48  LYS   B CG  1 
ATOM   1146 C  CG  B LYS   B 1 48  ? -14.375 12.046  31.567  0.50 23.41 ? 48  LYS   B CG  1 
ATOM   1147 C  CD  A LYS   B 1 48  ? -13.820 13.206  33.339  0.50 28.47 ? 48  LYS   B CD  1 
ATOM   1148 C  CD  B LYS   B 1 48  ? -14.352 13.404  32.233  0.50 31.45 ? 48  LYS   B CD  1 
ATOM   1149 N  N   . THR   B 1 49  ? -11.215 9.105   31.665  1.00 15.05 ? 49  THR   B N   1 
ATOM   1150 C  CA  . THR   B 1 49  ? -9.905  8.624   32.074  1.00 14.69 ? 49  THR   B CA  1 
ATOM   1151 C  C   . THR   B 1 49  ? -9.309  9.606   33.096  1.00 15.16 ? 49  THR   B C   1 
ATOM   1152 O  O   . THR   B 1 49  ? -9.451  10.804  32.957  1.00 17.59 ? 49  THR   B O   1 
ATOM   1153 C  CB  . THR   B 1 49  ? -8.954  8.438   30.891  1.00 14.32 ? 49  THR   B CB  1 
ATOM   1154 O  OG1 . THR   B 1 49  ? -8.825  9.648   30.171  1.00 14.33 ? 49  THR   B OG1 1 
ATOM   1155 C  CG2 . THR   B 1 49  ? -9.406  7.302   30.008  1.00 15.02 ? 49  THR   B CG2 1 
ATOM   1156 N  N   . SER   B 1 50  ? -8.553  9.068   34.017  1.00 15.31 ? 50  SER   B N   1 
ATOM   1157 C  CA  . SER   B 1 50  ? -7.834  9.786   35.097  1.00 17.65 ? 50  SER   B CA  1 
ATOM   1158 C  C   . SER   B 1 50  ? -6.563  10.412  34.562  1.00 17.19 ? 50  SER   B C   1 
ATOM   1159 O  O   . SER   B 1 50  ? -6.205  10.300  33.389  1.00 16.95 ? 50  SER   B O   1 
ATOM   1160 C  CB  . SER   B 1 50  ? -7.475  8.761   36.176  1.00 20.42 ? 50  SER   B CB  1 
ATOM   1161 O  OG  . SER   B 1 50  ? -6.406  7.951   35.673  1.00 19.88 ? 50  SER   B OG  1 
ATOM   1162 N  N   . GLU   B 1 51  ? -5.798  11.059  35.452  1.00 18.55 ? 51  GLU   B N   1 
ATOM   1163 C  CA  . GLU   B 1 51  ? -4.488  11.625  35.159  1.00 20.75 ? 51  GLU   B CA  1 
ATOM   1164 C  C   . GLU   B 1 51  ? -3.491  10.617  34.665  1.00 19.53 ? 51  GLU   B C   1 
ATOM   1165 O  O   . GLU   B 1 51  ? -2.538  10.946  34.018  1.00 21.17 ? 51  GLU   B O   1 
ATOM   1166 C  CB  . GLU   B 1 51  ? -3.913  12.366  36.411  1.00 28.26 ? 51  GLU   B CB  1 
ATOM   1167 N  N   . SER   B 1 52  ? -3.734  9.330   34.932  1.00 18.43 ? 52  SER   B N   1 
ATOM   1168 C  CA  . SER   B 1 52  ? -2.890  8.237   34.451  1.00 18.12 ? 52  SER   B CA  1 
ATOM   1169 C  C   . SER   B 1 52  ? -3.449  7.625   33.211  1.00 16.58 ? 52  SER   B C   1 
ATOM   1170 O  O   . SER   B 1 52  ? -2.904  6.653   32.706  1.00 18.12 ? 52  SER   B O   1 
ATOM   1171 C  CB  . SER   B 1 52  ? -2.756  7.190   35.504  1.00 23.72 ? 52  SER   B CB  1 
ATOM   1172 O  OG  . SER   B 1 52  ? -3.936  6.509   35.716  1.00 27.96 ? 52  SER   B OG  1 
ATOM   1173 N  N   . GLY   B 1 53  ? -4.500  8.172   32.637  1.00 15.62 ? 53  GLY   B N   1 
ATOM   1174 C  CA  . GLY   B 1 53  ? -5.076  7.615   31.426  1.00 15.20 ? 53  GLY   B CA  1 
ATOM   1175 C  C   . GLY   B 1 53  ? -5.938  6.391   31.634  1.00 14.63 ? 53  GLY   B C   1 
ATOM   1176 O  O   . GLY   B 1 53  ? -6.349  5.757   30.700  1.00 16.18 ? 53  GLY   B O   1 
ATOM   1177 N  N   . GLU   B 1 54  ? -6.326  6.122   32.867  1.00 16.06 ? 54  GLU   B N   1 
ATOM   1178 C  CA  . GLU   B 1 54  ? -7.035  4.909   33.204  1.00 15.26 ? 54  GLU   B CA  1 
ATOM   1179 C  C   . GLU   B 1 54  ? -8.424  5.209   33.696  1.00 15.86 ? 54  GLU   B C   1 
ATOM   1180 O  O   . GLU   B 1 54  ? -8.730  6.248   34.295  1.00 17.36 ? 54  GLU   B O   1 
ATOM   1181 C  CB  . GLU   B 1 54  ? -6.296  4.171   34.328  1.00 19.50 ? 54  GLU   B CB  1 
ATOM   1182 C  CG  . GLU   B 1 54  ? -4.926  3.701   33.854  1.00 23.46 ? 54  GLU   B CG  1 
ATOM   1183 C  CD  . GLU   B 1 54  ? -4.120  2.842   34.785  0.50 31.74 ? 54  GLU   B CD  1 
ATOM   1184 O  OE1 . GLU   B 1 54  ? -4.568  2.523   35.868  0.50 31.38 ? 54  GLU   B OE1 1 
ATOM   1185 O  OE2 . GLU   B 1 54  ? -3.012  2.503   34.396  0.50 31.83 ? 54  GLU   B OE2 1 
ATOM   1186 N  N   . LEU   B 1 55  ? -9.320  4.255   33.433  1.00 15.68 ? 55  LEU   B N   1 
ATOM   1187 C  CA  . LEU   B 1 55  ? -10.674 4.285   33.944  1.00 14.82 ? 55  LEU   B CA  1 
ATOM   1188 C  C   . LEU   B 1 55  ? -10.998 2.932   34.540  1.00 15.95 ? 55  LEU   B C   1 
ATOM   1189 O  O   . LEU   B 1 55  ? -11.036 1.955   33.831  1.00 18.08 ? 55  LEU   B O   1 
ATOM   1190 C  CB  . LEU   B 1 55  ? -11.606 4.638   32.786  1.00 16.17 ? 55  LEU   B CB  1 
ATOM   1191 C  CG  . LEU   B 1 55  ? -13.084 4.653   33.110  1.00 16.87 ? 55  LEU   B CG  1 
ATOM   1192 C  CD1 . LEU   B 1 55  ? -13.426 5.579   34.313  1.00 19.00 ? 55  LEU   B CD1 1 
ATOM   1193 C  CD2 . LEU   B 1 55  ? -13.896 5.062   31.925  1.00 18.99 ? 55  LEU   B CD2 1 
ATOM   1194 N  N   . HIS   B 1 56  ? -11.239 2.941   35.831  1.00 20.47 ? 56  HIS   B N   1 
ATOM   1195 C  CA  . HIS   B 1 56  ? -11.550 1.821   36.679  1.00 26.02 ? 56  HIS   B CA  1 
ATOM   1196 C  C   . HIS   B 1 56  ? -12.967 1.927   37.159  1.00 23.45 ? 56  HIS   B C   1 
ATOM   1197 O  O   . HIS   B 1 56  ? -13.617 2.971   37.018  1.00 24.87 ? 56  HIS   B O   1 
ATOM   1198 C  CB  . HIS   B 1 56  ? -10.633 1.857   37.949  1.00 28.74 ? 56  HIS   B CB  1 
ATOM   1199 C  CG  . HIS   B 1 56  ? -9.192  1.618   37.686  1.00 28.37 ? 56  HIS   B CG  1 
ATOM   1200 N  ND1 . HIS   B 1 56  ? -8.350  2.570   37.384  1.00 39.08 ? 56  HIS   B ND1 1 
ATOM   1201 C  CD2 . HIS   B 1 56  ? -8.450  0.426   37.704  1.00 36.88 ? 56  HIS   B CD2 1 
ATOM   1202 C  CE1 . HIS   B 1 56  ? -7.105  2.063   37.210  1.00 32.06 ? 56  HIS   B CE1 1 
ATOM   1203 N  NE2 . HIS   B 1 56  ? -7.167  0.744   37.419  1.00 43.77 ? 56  HIS   B NE2 1 
ATOM   1204 N  N   . GLY   B 1 57  ? -13.494 0.868   37.733  1.00 25.97 ? 57  GLY   B N   1 
ATOM   1205 C  CA  . GLY   B 1 57  ? -14.760 1.003   38.440  1.00 30.63 ? 57  GLY   B CA  1 
ATOM   1206 C  C   . GLY   B 1 57  ? -15.975 1.036   37.533  1.00 28.47 ? 57  GLY   B C   1 
ATOM   1207 O  O   . GLY   B 1 57  ? -17.062 1.390   37.965  1.00 33.25 ? 57  GLY   B O   1 
ATOM   1208 N  N   . LEU   B 1 58  ? -15.838 0.606   36.296  1.00 25.92 ? 58  LEU   B N   1 
ATOM   1209 C  CA  . LEU   B 1 58  ? -17.002 0.570   35.365  1.00 24.28 ? 58  LEU   B CA  1 
ATOM   1210 C  C   . LEU   B 1 58  ? -18.024 -0.467  35.715  1.00 27.10 ? 58  LEU   B C   1 
ATOM   1211 O  O   . LEU   B 1 58  ? -19.216 -0.214  35.543  1.00 30.01 ? 58  LEU   B O   1 
ATOM   1212 C  CB  . LEU   B 1 58  ? -16.531 0.378   33.930  1.00 26.36 ? 58  LEU   B CB  1 
ATOM   1213 C  CG  . LEU   B 1 58  ? -15.795 1.548   33.344  1.00 24.25 ? 58  LEU   B CG  1 
ATOM   1214 C  CD1 . LEU   B 1 58  ? -14.945 1.095   32.202  1.00 29.77 ? 58  LEU   B CD1 1 
ATOM   1215 C  CD2 . LEU   B 1 58  ? -16.722 2.680   32.955  1.00 29.25 ? 58  LEU   B CD2 1 
ATOM   1216 N  N   . THR   B 1 59  ? -17.643 -1.641  36.191  1.00 27.72 ? 59  THR   B N   1 
ATOM   1217 C  CA  . THR   B 1 59  ? -18.606 -2.674  36.454  1.00 28.23 ? 59  THR   B CA  1 
ATOM   1218 C  C   . THR   B 1 59  ? -18.057 -3.466  37.627  1.00 28.24 ? 59  THR   B C   1 
ATOM   1219 O  O   . THR   B 1 59  ? -17.040 -3.195  38.205  1.00 30.32 ? 59  THR   B O   1 
ATOM   1220 C  CB  . THR   B 1 59  ? -18.898 -3.510  35.185  1.00 27.26 ? 59  THR   B CB  1 
ATOM   1221 O  OG1 . THR   B 1 59  ? -20.027 -4.413  35.364  1.00 32.13 ? 59  THR   B OG1 1 
ATOM   1222 C  CG2 . THR   B 1 59  ? -17.693 -4.320  34.812  1.00 25.11 ? 59  THR   B CG2 1 
ATOM   1223 N  N   . THR   B 1 60  ? -18.810 -4.480  37.960  1.00 30.93 ? 60  THR   B N   1 
ATOM   1224 C  CA  . THR   B 1 60  ? -18.523 -5.455  39.028  1.00 29.82 ? 60  THR   B CA  1 
ATOM   1225 C  C   . THR   B 1 60  ? -18.596 -6.793  38.470  1.00 24.95 ? 60  THR   B C   1 
ATOM   1226 O  O   . THR   B 1 60  ? -19.221 -6.996  37.434  1.00 22.83 ? 60  THR   B O   1 
ATOM   1227 C  CB  . THR   B 1 60  ? -19.544 -5.380  40.164  1.00 32.76 ? 60  THR   B CB  1 
ATOM   1228 O  OG1 . THR   B 1 60  ? -20.893 -5.617  39.653  1.00 38.95 ? 60  THR   B OG1 1 
ATOM   1229 C  CG2 . THR   B 1 60  ? -19.436 -4.026  40.890  1.00 37.12 ? 60  THR   B CG2 1 
ATOM   1230 N  N   . GLU   B 1 61  ? -18.025 -7.732  39.206  1.00 26.62 ? 61  GLU   B N   1 
ATOM   1231 C  CA  . GLU   B 1 61  ? -18.005 -9.139  38.852  1.00 25.91 ? 61  GLU   B CA  1 
ATOM   1232 C  C   . GLU   B 1 61  ? -19.425 -9.654  38.645  1.00 29.04 ? 61  GLU   B C   1 
ATOM   1233 O  O   . GLU   B 1 61  ? -19.680 -10.415 37.725  1.00 32.04 ? 61  GLU   B O   1 
ATOM   1234 C  CB  . GLU   B 1 61  ? -17.302 -9.927  39.987  1.00 35.97 ? 61  GLU   B CB  1 
ATOM   1235 N  N   . GLU   B 1 62  ? -20.350 -9.294  39.505  1.00 30.69 ? 62  GLU   B N   1 
ATOM   1236 C  CA  . GLU   B 1 62  ? -21.680 -9.907  39.430  1.00 34.96 ? 62  GLU   B CA  1 
ATOM   1237 C  C   . GLU   B 1 62  ? -22.398 -9.382  38.179  1.00 32.86 ? 62  GLU   B C   1 
ATOM   1238 O  O   . GLU   B 1 62  ? -23.072 -10.169 37.499  1.00 29.68 ? 62  GLU   B O   1 
ATOM   1239 N  N   . GLU   B 1 63  ? -22.255 -8.097  37.843  1.00 26.02 ? 63  GLU   B N   1 
ATOM   1240 C  CA  . GLU   B 1 63  ? -23.039 -7.519  36.724  1.00 24.21 ? 63  GLU   B CA  1 
ATOM   1241 C  C   . GLU   B 1 63  ? -22.419 -7.833  35.375  1.00 20.04 ? 63  GLU   B C   1 
ATOM   1242 O  O   . GLU   B 1 63  ? -23.132 -7.835  34.392  1.00 23.18 ? 63  GLU   B O   1 
ATOM   1243 C  CB  . GLU   B 1 63  ? -23.086 -5.993  36.847  1.00 30.00 ? 63  GLU   B CB  1 
ATOM   1244 N  N   . PHE   B 1 64  ? -21.121 -8.124  35.372  1.00 19.96 ? 64  PHE   B N   1 
ATOM   1245 C  CA  . PHE   B 1 64  ? -20.383 -8.273  34.092  1.00 19.55 ? 64  PHE   B CA  1 
ATOM   1246 C  C   . PHE   B 1 64  ? -20.522 -9.691  33.677  1.00 18.39 ? 64  PHE   B C   1 
ATOM   1247 O  O   . PHE   B 1 64  ? -19.551 -10.457 33.694  1.00 19.70 ? 64  PHE   B O   1 
ATOM   1248 C  CB  . PHE   B 1 64  ? -18.995 -7.789  34.298  1.00 19.25 ? 64  PHE   B CB  1 
ATOM   1249 C  CG  . PHE   B 1 64  ? -18.155 -7.692  33.050  1.00 19.08 ? 64  PHE   B CG  1 
ATOM   1250 C  CD1 . PHE   B 1 64  ? -18.598 -6.958  31.937  1.00 21.54 ? 64  PHE   B CD1 1 
ATOM   1251 C  CD2 . PHE   B 1 64  ? -16.910 -8.308  32.996  1.00 24.35 ? 64  PHE   B CD2 1 
ATOM   1252 C  CE1 . PHE   B 1 64  ? -17.828 -6.852  30.813  1.00 25.15 ? 64  PHE   B CE1 1 
ATOM   1253 C  CE2 . PHE   B 1 64  ? -16.130 -8.184  31.902  1.00 26.17 ? 64  PHE   B CE2 1 
ATOM   1254 C  CZ  . PHE   B 1 64  ? -16.593 -7.486  30.800  1.00 23.34 ? 64  PHE   B CZ  1 
ATOM   1255 N  N   . VAL   B 1 65  ? -21.709 -10.035 33.291  1.00 18.22 ? 65  VAL   B N   1 
ATOM   1256 C  CA  . VAL   B 1 65  ? -21.975 -11.473 32.812  1.00 22.12 ? 65  VAL   B CA  1 
ATOM   1257 C  C   . VAL   B 1 65  ? -21.613 -11.645 31.263  1.00 18.78 ? 65  VAL   B C   1 
ATOM   1258 O  O   . VAL   B 1 65  ? -21.324 -10.599 30.615  1.00 20.88 ? 65  VAL   B O   1 
ATOM   1259 C  CB  . VAL   B 1 65  ? -23.454 -11.905 33.094  1.00 21.50 ? 65  VAL   B CB  1 
ATOM   1260 C  CG1 . VAL   B 1 65  ? -23.891 -11.713 34.541  1.00 22.57 ? 65  VAL   B CG1 1 
ATOM   1261 C  CG2 . VAL   B 1 65  ? -24.293 -11.033 32.095  1.00 28.57 ? 65  VAL   B CG2 1 
ATOM   1262 N  N   . GLU   B 1 66  ? -21.608 -12.852 30.835  1.00 18.10 ? 66  GLU   B N   1 
ATOM   1263 C  CA  . GLU   B 1 66  ? -21.334 -13.083 29.493  1.00 18.95 ? 66  GLU   B CA  1 
ATOM   1264 C  C   . GLU   B 1 66  ? -22.249 -12.256 28.611  1.00 20.78 ? 66  GLU   B C   1 
ATOM   1265 O  O   . GLU   B 1 66  ? -23.414 -12.032 28.917  1.00 25.86 ? 66  GLU   B O   1 
ATOM   1266 C  CB  . GLU   B 1 66  ? -21.648 -14.534 29.146  1.00 19.56 ? 66  GLU   B CB  1 
ATOM   1267 C  CG  . GLU   B 1 66  ? -20.761 -15.506 29.768  1.00 22.46 ? 66  GLU   B CG  1 
ATOM   1268 C  CD  . GLU   B 1 66  ? -20.907 -16.845 29.013  0.70 25.24 ? 66  GLU   B CD  1 
ATOM   1269 O  OE1 . GLU   B 1 66  ? -21.349 -17.725 29.797  0.70 19.87 ? 66  GLU   B OE1 1 
ATOM   1270 N  N   . GLY   B 1 67  ? -21.683 -11.785 27.525  1.00 21.24 ? 67  GLY   B N   1 
ATOM   1271 C  CA  . GLY   B 1 67  ? -22.478 -10.994 26.593  1.00 21.92 ? 67  GLY   B CA  1 
ATOM   1272 C  C   . GLY   B 1 67  ? -21.498 -10.339 25.652  1.00 18.78 ? 67  GLY   B C   1 
ATOM   1273 O  O   . GLY   B 1 67  ? -20.291 -10.518 25.749  1.00 17.16 ? 67  GLY   B O   1 
ATOM   1274 N  N   . ILE   B 1 68  ? -22.042 -9.639  24.684  1.00 19.76 ? 68  ILE   B N   1 
ATOM   1275 C  CA  . ILE   B 1 68  ? -21.256 -8.828  23.793  1.00 17.39 ? 68  ILE   B CA  1 
ATOM   1276 C  C   . ILE   B 1 68  ? -21.304 -7.403  24.267  1.00 16.26 ? 68  ILE   B C   1 
ATOM   1277 O  O   . ILE   B 1 68  ? -22.390 -6.877  24.571  1.00 19.31 ? 68  ILE   B O   1 
ATOM   1278 C  CB  . ILE   B 1 68  ? -21.763 -8.908  22.350  1.00 18.87 ? 68  ILE   B CB  1 
ATOM   1279 C  CG1 . ILE   B 1 68  ? -21.770 -10.366 21.879  1.00 22.51 ? 68  ILE   B CG1 1 
ATOM   1280 C  CG2 . ILE   B 1 68  ? -20.936 -7.998  21.435  1.00 20.78 ? 68  ILE   B CG2 1 
ATOM   1281 C  CD1 . ILE   B 1 68  ? -22.383 -10.567 20.526  1.00 25.53 ? 68  ILE   B CD1 1 
ATOM   1282 N  N   . TYR   B 1 69  ? -20.121 -6.802  24.422  1.00 15.50 ? 69  TYR   B N   1 
ATOM   1283 C  CA  . TYR   B 1 69  ? -19.960 -5.476  24.964  1.00 15.41 ? 69  TYR   B CA  1 
ATOM   1284 C  C   . TYR   B 1 69  ? -19.254 -4.574  23.959  1.00 14.74 ? 69  TYR   B C   1 
ATOM   1285 O  O   . TYR   B 1 69  ? -18.468 -5.028  23.154  1.00 15.77 ? 69  TYR   B O   1 
ATOM   1286 C  CB  . TYR   B 1 69  ? -19.167 -5.535  26.290  1.00 16.24 ? 69  TYR   B CB  1 
ATOM   1287 C  CG  . TYR   B 1 69  ? -19.862 -6.213  27.442  1.00 16.91 ? 69  TYR   B CG  1 
ATOM   1288 C  CD1 . TYR   B 1 69  ? -19.815 -7.580  27.572  1.00 16.69 ? 69  TYR   B CD1 1 
ATOM   1289 C  CD2 . TYR   B 1 69  ? -20.590 -5.486  28.356  1.00 20.86 ? 69  TYR   B CD2 1 
ATOM   1290 C  CE1 . TYR   B 1 69  ? -20.499 -8.224  28.589  1.00 18.08 ? 69  TYR   B CE1 1 
ATOM   1291 C  CE2 . TYR   B 1 69  ? -21.253 -6.123  29.399  1.00 19.46 ? 69  TYR   B CE2 1 
ATOM   1292 C  CZ  . TYR   B 1 69  ? -21.158 -7.486  29.514  1.00 18.15 ? 69  TYR   B CZ  1 
ATOM   1293 O  OH  . TYR   B 1 69  ? -21.825 -8.061  30.581  1.00 19.47 ? 69  TYR   B OH  1 
ATOM   1294 N  N   . LYS   B 1 70  ? -19.576 -3.290  23.994  1.00 14.12 ? 70  LYS   B N   1 
ATOM   1295 C  CA  . LYS   B 1 70  ? -18.955 -2.271  23.207  1.00 13.71 ? 70  LYS   B CA  1 
ATOM   1296 C  C   . LYS   B 1 70  ? -18.397 -1.205  24.132  1.00 14.43 ? 70  LYS   B C   1 
ATOM   1297 O  O   . LYS   B 1 70  ? -19.066 -0.728  25.024  1.00 15.83 ? 70  LYS   B O   1 
ATOM   1298 C  CB  . LYS   B 1 70  ? -20.002 -1.656  22.221  1.00 16.87 ? 70  LYS   B CB  1 
ATOM   1299 C  CG  . LYS   B 1 70  ? -19.434 -0.484  21.461  1.00 18.10 ? 70  LYS   B CG  1 
ATOM   1300 C  CD  . LYS   B 1 70  ? -20.225 -0.102  20.283  1.00 22.64 ? 70  LYS   B CD  1 
ATOM   1301 C  CE  . LYS   B 1 70  ? -21.547 0.444   20.685  1.00 26.18 ? 70  LYS   B CE  1 
ATOM   1302 N  NZ  . LYS   B 1 70  ? -22.191 1.157   19.492  1.00 37.21 ? 70  LYS   B NZ  1 
ATOM   1303 N  N   . VAL   B 1 71  ? -17.149 -0.836  23.907  1.00 13.72 ? 71  VAL   B N   1 
ATOM   1304 C  CA  . VAL   B 1 71  ? -16.492 0.253   24.583  1.00 13.31 ? 71  VAL   B CA  1 
ATOM   1305 C  C   . VAL   B 1 71  ? -16.228 1.324   23.554  1.00 14.06 ? 71  VAL   B C   1 
ATOM   1306 O  O   . VAL   B 1 71  ? -15.512 1.061   22.591  1.00 16.67 ? 71  VAL   B O   1 
ATOM   1307 C  CB  . VAL   B 1 71  ? -15.175 -0.180  25.257  1.00 14.77 ? 71  VAL   B CB  1 
ATOM   1308 C  CG1 . VAL   B 1 71  ? -14.485 1.036   25.877  1.00 17.29 ? 71  VAL   B CG1 1 
ATOM   1309 C  CG2 . VAL   B 1 71  ? -15.476 -1.273  26.277  1.00 18.32 ? 71  VAL   B CG2 1 
ATOM   1310 N  N   . GLU   B 1 72  ? -16.842 2.479   23.715  1.00 14.24 ? 72  GLU   B N   1 
ATOM   1311 C  CA  . GLU   B 1 72  ? -16.660 3.614   22.823  1.00 14.37 ? 72  GLU   B CA  1 
ATOM   1312 C  C   . GLU   B 1 72  ? -15.842 4.689   23.492  1.00 13.40 ? 72  GLU   B C   1 
ATOM   1313 O  O   . GLU   B 1 72  ? -16.227 5.202   24.527  1.00 15.88 ? 72  GLU   B O   1 
ATOM   1314 C  CB  . GLU   B 1 72  ? -18.009 4.202   22.360  1.00 17.98 ? 72  GLU   B CB  1 
ATOM   1315 C  CG  . GLU   B 1 72  ? -18.789 3.401   21.336  0.50 21.15 ? 72  GLU   B CG  1 
ATOM   1316 C  CD  . GLU   B 1 72  ? -19.846 4.194   20.603  0.50 27.45 ? 72  GLU   B CD  1 
ATOM   1317 O  OE1 . GLU   B 1 72  ? -20.128 5.333   21.025  0.50 36.19 ? 72  GLU   B OE1 1 
ATOM   1318 O  OE2 . GLU   B 1 72  ? -20.388 3.581   19.646  0.50 35.08 ? 72  GLU   B OE2 1 
ATOM   1319 N  N   . ILE   B 1 73  ? -14.727 4.988   22.898  1.00 13.26 ? 73  ILE   B N   1 
ATOM   1320 C  CA  . ILE   B 1 73  ? -13.756 5.989   23.437  1.00 13.74 ? 73  ILE   B CA  1 
ATOM   1321 C  C   . ILE   B 1 73  ? -13.902 7.262   22.607  1.00 12.81 ? 73  ILE   B C   1 
ATOM   1322 O  O   . ILE   B 1 73  ? -13.743 7.218   21.388  1.00 14.54 ? 73  ILE   B O   1 
ATOM   1323 C  CB  . ILE   B 1 73  ? -12.333 5.415   23.382  1.00 14.29 ? 73  ILE   B CB  1 
ATOM   1324 C  CG1 . ILE   B 1 73  ? -12.252 4.075   24.110  1.00 15.56 ? 73  ILE   B CG1 1 
ATOM   1325 C  CG2 . ILE   B 1 73  ? -11.351 6.451   23.921  1.00 16.37 ? 73  ILE   B CG2 1 
ATOM   1326 C  CD1 . ILE   B 1 73  ? -10.927 3.369   23.934  1.00 17.82 ? 73  ILE   B CD1 1 
ATOM   1327 N  N   . ASP   B 1 74  ? -14.220 8.342   23.239  1.00 13.81 ? 74  ASP   B N   1 
ATOM   1328 C  CA  . ASP   B 1 74  ? -14.516 9.619   22.522  1.00 13.86 ? 74  ASP   B CA  1 
ATOM   1329 C  C   . ASP   B 1 74  ? -13.225 10.340  22.150  1.00 14.67 ? 74  ASP   B C   1 
ATOM   1330 O  O   . ASP   B 1 74  ? -12.811 11.333  22.760  1.00 15.47 ? 74  ASP   B O   1 
ATOM   1331 C  CB  . ASP   B 1 74  ? -15.417 10.537  23.311  1.00 16.48 ? 74  ASP   B CB  1 
ATOM   1332 C  CG  . ASP   B 1 74  ? -15.834 11.770  22.554  1.00 19.45 ? 74  ASP   B CG  1 
ATOM   1333 O  OD1 . ASP   B 1 74  ? -15.391 11.940  21.353  1.00 19.70 ? 74  ASP   B OD1 1 
ATOM   1334 O  OD2 . ASP   B 1 74  ? -16.565 12.595  23.085  1.00 25.01 ? 74  ASP   B OD2 1 
ATOM   1335 N  N   . THR   B 1 75  ? -12.547 9.811   21.158  1.00 13.65 ? 75  THR   B N   1 
ATOM   1336 C  CA  . THR   B 1 75  ? -11.308 10.326  20.693  1.00 13.15 ? 75  THR   B CA  1 
ATOM   1337 C  C   . THR   B 1 75  ? -11.467 11.685  20.031  1.00 12.68 ? 75  THR   B C   1 
ATOM   1338 O  O   . THR   B 1 75  ? -10.556 12.526  20.122  1.00 13.10 ? 75  THR   B O   1 
ATOM   1339 C  CB  . THR   B 1 75  ? -10.629 9.332   19.722  1.00 13.71 ? 75  THR   B CB  1 
ATOM   1340 O  OG1 . THR   B 1 75  ? -11.487 9.090   18.606  1.00 13.57 ? 75  THR   B OG1 1 
ATOM   1341 C  CG2 . THR   B 1 75  ? -10.345 7.964   20.410  1.00 14.96 ? 75  THR   B CG2 1 
ATOM   1342 N  N   . LYS   B 1 76  ? -12.564 11.901  19.332  1.00 12.66 ? 76  LYS   B N   1 
ATOM   1343 C  CA  . LYS   B 1 76  ? -12.738 13.154  18.621  1.00 13.74 ? 76  LYS   B CA  1 
ATOM   1344 C  C   . LYS   B 1 76  ? -12.740 14.331  19.576  1.00 13.58 ? 76  LYS   B C   1 
ATOM   1345 O  O   . LYS   B 1 76  ? -12.088 15.333  19.318  1.00 14.64 ? 76  LYS   B O   1 
ATOM   1346 C  CB  . LYS   B 1 76  ? -14.028 13.104  17.768  1.00 14.68 ? 76  LYS   B CB  1 
ATOM   1347 C  CG  . LYS   B 1 76  ? -14.216 14.333  16.934  1.00 18.21 ? 76  LYS   B CG  1 
ATOM   1348 C  CD  . LYS   B 1 76  ? -15.389 14.176  16.024  1.00 21.27 ? 76  LYS   B CD  1 
ATOM   1349 C  CE  . LYS   B 1 76  ? -15.600 15.256  15.063  1.00 28.82 ? 76  LYS   B CE  1 
ATOM   1350 N  NZ  . LYS   B 1 76  ? -16.842 15.142  14.280  1.00 33.79 ? 76  LYS   B NZ  1 
ATOM   1351 N  N   . SER   B 1 77  ? -13.454 14.212  20.677  1.00 13.94 ? 77  SER   B N   1 
ATOM   1352 C  CA  . SER   B 1 77  ? -13.510 15.268  21.646  1.00 15.15 ? 77  SER   B CA  1 
ATOM   1353 C  C   . SER   B 1 77  ? -12.158 15.528  22.269  1.00 14.59 ? 77  SER   B C   1 
ATOM   1354 O  O   . SER   B 1 77  ? -11.780 16.671  22.583  1.00 16.01 ? 77  SER   B O   1 
ATOM   1355 C  CB  . SER   B 1 77  ? -14.537 15.078  22.744  1.00 19.33 ? 77  SER   B CB  1 
ATOM   1356 O  OG  . SER   B 1 77  ? -15.822 14.983  22.198  1.00 22.14 ? 77  SER   B OG  1 
ATOM   1357 N  N   . TYR   B 1 78  ? -11.387 14.477  22.464  1.00 14.68 ? 78  TYR   B N   1 
ATOM   1358 C  CA  . TYR   B 1 78  ? -10.051 14.576  23.053  1.00 14.47 ? 78  TYR   B CA  1 
ATOM   1359 C  C   . TYR   B 1 78  ? -9.148  15.410  22.114  1.00 13.52 ? 78  TYR   B C   1 
ATOM   1360 O  O   . TYR   B 1 78  ? -8.525  16.401  22.566  1.00 14.91 ? 78  TYR   B O   1 
ATOM   1361 C  CB  . TYR   B 1 78  ? -9.481  13.153  23.261  1.00 14.97 ? 78  TYR   B CB  1 
ATOM   1362 C  CG  . TYR   B 1 78  ? -8.051  13.189  23.764  1.00 13.98 ? 78  TYR   B CG  1 
ATOM   1363 C  CD1 . TYR   B 1 78  ? -7.796  13.527  25.097  1.00 14.14 ? 78  TYR   B CD1 1 
ATOM   1364 C  CD2 . TYR   B 1 78  ? -6.972  12.955  22.914  1.00 14.69 ? 78  TYR   B CD2 1 
ATOM   1365 C  CE1 . TYR   B 1 78  ? -6.489  13.560  25.577  1.00 15.74 ? 78  TYR   B CE1 1 
ATOM   1366 C  CE2 . TYR   B 1 78  ? -5.673  13.005  23.416  1.00 15.55 ? 78  TYR   B CE2 1 
ATOM   1367 C  CZ  . TYR   B 1 78  ? -5.439  13.318  24.713  1.00 15.22 ? 78  TYR   B CZ  1 
ATOM   1368 O  OH  . TYR   B 1 78  ? -4.189  13.362  25.216  1.00 16.58 ? 78  TYR   B OH  1 
ATOM   1369 N  N   . TRP   B 1 79  ? -9.095  15.068  20.841  1.00 13.08 ? 79  TRP   B N   1 
ATOM   1370 C  CA  . TRP   B 1 79  ? -8.274  15.823  19.938  1.00 12.52 ? 79  TRP   B CA  1 
ATOM   1371 C  C   . TRP   B 1 79  ? -8.722  17.258  19.742  1.00 13.51 ? 79  TRP   B C   1 
ATOM   1372 O  O   . TRP   B 1 79  ? -7.924  18.181  19.645  1.00 13.74 ? 79  TRP   B O   1 
ATOM   1373 C  CB  . TRP   B 1 79  ? -8.183  15.142  18.581  1.00 12.47 ? 79  TRP   B CB  1 
ATOM   1374 C  CG  . TRP   B 1 79  ? -7.470  13.809  18.626  1.00 11.99 ? 79  TRP   B CG  1 
ATOM   1375 C  CD1 . TRP   B 1 79  ? -7.999  12.549  18.356  1.00 12.09 ? 79  TRP   B CD1 1 
ATOM   1376 C  CD2 . TRP   B 1 79  ? -6.098  13.573  19.035  1.00 11.36 ? 79  TRP   B CD2 1 
ATOM   1377 N  NE1 . TRP   B 1 79  ? -7.042  11.607  18.558  1.00 11.53 ? 79  TRP   B NE1 1 
ATOM   1378 C  CE2 . TRP   B 1 79  ? -5.881  12.174  18.969  1.00 11.49 ? 79  TRP   B CE2 1 
ATOM   1379 C  CE3 . TRP   B 1 79  ? -5.020  14.400  19.429  1.00 12.25 ? 79  TRP   B CE3 1 
ATOM   1380 C  CZ2 . TRP   B 1 79  ? -4.645  11.592  19.324  1.00 12.19 ? 79  TRP   B CZ2 1 
ATOM   1381 C  CZ3 . TRP   B 1 79  ? -3.805  13.800  19.806  1.00 13.48 ? 79  TRP   B CZ3 1 
ATOM   1382 C  CH2 . TRP   B 1 79  ? -3.626  12.436  19.701  1.00 13.28 ? 79  TRP   B CH2 1 
ATOM   1383 N  N   . LYS   B 1 80  ? -10.051 17.450  19.680  1.00 13.87 ? 80  LYS   B N   1 
ATOM   1384 C  CA  . LYS   B 1 80  ? -10.587 18.815  19.602  1.00 15.18 ? 80  LYS   B CA  1 
ATOM   1385 C  C   . LYS   B 1 80  ? -10.147 19.645  20.784  1.00 15.46 ? 80  LYS   B C   1 
ATOM   1386 O  O   . LYS   B 1 80  ? -9.803  20.823  20.610  1.00 16.91 ? 80  LYS   B O   1 
ATOM   1387 C  CB  . LYS   B 1 80  ? -12.130 18.742  19.481  1.00 16.53 ? 80  LYS   B CB  1 
ATOM   1388 C  CG  . LYS   B 1 80  ? -12.622 18.424  18.080  1.00 17.54 ? 80  LYS   B CG  1 
ATOM   1389 C  CD  . LYS   B 1 80  ? -14.116 18.182  18.049  1.00 23.39 ? 80  LYS   B CD  1 
ATOM   1390 C  CE  . LYS   B 1 80  ? -14.974 19.240  18.654  0.50 22.77 ? 80  LYS   B CE  1 
ATOM   1391 N  NZ  . LYS   B 1 80  ? -15.114 20.314  17.654  0.50 31.40 ? 80  LYS   B NZ  1 
ATOM   1392 N  N   . ALA   B 1 81  ? -10.150 19.104  22.000  1.00 16.14 ? 81  ALA   B N   1 
ATOM   1393 C  CA  . ALA   B 1 81  ? -9.728  19.831  23.180  1.00 19.18 ? 81  ALA   B CA  1 
ATOM   1394 C  C   . ALA   B 1 81  ? -8.279  20.237  23.136  1.00 20.45 ? 81  ALA   B C   1 
ATOM   1395 O  O   . ALA   B 1 81  ? -7.894  21.191  23.736  1.00 24.52 ? 81  ALA   B O   1 
ATOM   1396 C  CB  . ALA   B 1 81  ? -10.011 19.031  24.433  1.00 20.14 ? 81  ALA   B CB  1 
ATOM   1397 N  N   . LEU   B 1 82  ? -7.452  19.487  22.389  1.00 19.26 ? 82  LEU   B N   1 
ATOM   1398 C  CA  . LEU   B 1 82  ? -6.027  19.794  22.148  1.00 17.97 ? 82  LEU   B CA  1 
ATOM   1399 C  C   . LEU   B 1 82  ? -5.782  20.647  20.922  1.00 18.29 ? 82  LEU   B C   1 
ATOM   1400 O  O   . LEU   B 1 82  ? -4.636  20.950  20.626  1.00 20.08 ? 82  LEU   B O   1 
ATOM   1401 C  CB  . LEU   B 1 82  ? -5.274  18.451  22.069  1.00 18.83 ? 82  LEU   B CB  1 
ATOM   1402 C  CG  . LEU   B 1 82  ? -5.096  17.599  23.310  1.00 25.75 ? 82  LEU   B CG  1 
ATOM   1403 C  CD1 . LEU   B 1 82  ? -4.269  16.346  22.935  1.00 29.58 ? 82  LEU   B CD1 1 
ATOM   1404 C  CD2 . LEU   B 1 82  ? -4.376  18.426  24.376  1.00 27.08 ? 82  LEU   B CD2 1 
ATOM   1405 N  N   . GLY   B 1 83  ? -6.786  20.975  20.136  1.00 17.72 ? 83  GLY   B N   1 
ATOM   1406 C  CA  . GLY   B 1 83  ? -6.596  21.835  18.978  1.00 16.60 ? 83  GLY   B CA  1 
ATOM   1407 C  C   . GLY   B 1 83  ? -5.966  21.114  17.808  1.00 16.96 ? 83  GLY   B C   1 
ATOM   1408 O  O   . GLY   B 1 83  ? -5.308  21.703  16.988  1.00 19.19 ? 83  GLY   B O   1 
ATOM   1409 N  N   . ILE   B 1 84  ? -6.220  19.788  17.702  1.00 15.35 ? 84  ILE   B N   1 
ATOM   1410 C  CA  . ILE   B 1 84  ? -5.635  18.917  16.716  1.00 15.36 ? 84  ILE   B CA  1 
ATOM   1411 C  C   . ILE   B 1 84  ? -6.742  18.313  15.870  1.00 14.31 ? 84  ILE   B C   1 
ATOM   1412 O  O   . ILE   B 1 84  ? -7.661  17.737  16.445  1.00 14.92 ? 84  ILE   B O   1 
ATOM   1413 C  CB  . ILE   B 1 84  ? -4.777  17.812  17.380  1.00 16.65 ? 84  ILE   B CB  1 
ATOM   1414 C  CG1 . ILE   B 1 84  ? -3.608  18.472  18.101  1.00 18.00 ? 84  ILE   B CG1 1 
ATOM   1415 C  CG2 . ILE   B 1 84  ? -4.325  16.779  16.331  1.00 23.23 ? 84  ILE   B CG2 1 
ATOM   1416 C  CD1 . ILE   B 1 84  ? -2.907  17.486  19.047  1.00 21.16 ? 84  ILE   B CD1 1 
ATOM   1417 N  N   . SER   B 1 85  ? -6.630  18.352  14.548  1.00 14.95 ? 85  SER   B N   1 
ATOM   1418 C  CA  A SER   B 1 85  ? -7.696  17.809  13.676  0.50 14.93 ? 85  SER   B CA  1 
ATOM   1419 C  CA  B SER   B 1 85  ? -7.703  17.842  13.700  0.50 14.71 ? 85  SER   B CA  1 
ATOM   1420 C  C   . SER   B 1 85  ? -7.704  16.295  13.684  1.00 13.75 ? 85  SER   B C   1 
ATOM   1421 O  O   . SER   B 1 85  ? -6.697  15.696  13.359  1.00 15.61 ? 85  SER   B O   1 
ATOM   1422 C  CB  A SER   B 1 85  ? -7.486  18.194  12.229  0.50 18.45 ? 85  SER   B CB  1 
ATOM   1423 C  CB  B SER   B 1 85  ? -7.528  18.397  12.297  0.50 18.23 ? 85  SER   B CB  1 
ATOM   1424 O  OG  A SER   B 1 85  ? -7.656  19.618  12.054  0.50 16.06 ? 85  SER   B OG  1 
ATOM   1425 O  OG  B SER   B 1 85  ? -8.632  18.060  11.468  0.50 22.63 ? 85  SER   B OG  1 
ATOM   1426 N  N   . PRO   B 1 86  ? -8.806  15.637  14.046  1.00 13.90 ? 86  PRO   B N   1 
ATOM   1427 C  CA  . PRO   B 1 86  ? -8.829  14.193  14.113  1.00 14.94 ? 86  PRO   B CA  1 
ATOM   1428 C  C   . PRO   B 1 86  ? -9.540  13.586  12.935  1.00 13.15 ? 86  PRO   B C   1 
ATOM   1429 O  O   . PRO   B 1 86  ? -10.400 14.186  12.310  1.00 16.23 ? 86  PRO   B O   1 
ATOM   1430 C  CB  . PRO   B 1 86  ? -9.655  13.968  15.363  1.00 18.19 ? 86  PRO   B CB  1 
ATOM   1431 C  CG  . PRO   B 1 86  ? -10.658 15.061  15.340  1.00 18.17 ? 86  PRO   B CG  1 
ATOM   1432 C  CD  . PRO   B 1 86  ? -9.955  16.226  14.775  1.00 14.81 ? 86  PRO   B CD  1 
ATOM   1433 N  N   . PHE   B 1 87  ? -9.291  12.329  12.621  1.00 11.82 ? 87  PHE   B N   1 
ATOM   1434 C  CA  . PHE   B 1 87  ? -9.998  11.604  11.608  1.00 12.43 ? 87  PHE   B CA  1 
ATOM   1435 C  C   . PHE   B 1 87  ? -11.241 10.929  12.112  1.00 11.67 ? 87  PHE   B C   1 
ATOM   1436 O  O   . PHE   B 1 87  ? -12.299 11.041  11.462  1.00 12.70 ? 87  PHE   B O   1 
ATOM   1437 C  CB  . PHE   B 1 87  ? -9.059  10.566  10.995  1.00 13.21 ? 87  PHE   B CB  1 
ATOM   1438 C  CG  . PHE   B 1 87  ? -9.743  9.766   9.942   1.00 13.57 ? 87  PHE   B CG  1 
ATOM   1439 C  CD1 . PHE   B 1 87  ? -9.974  10.296  8.709   1.00 15.59 ? 87  PHE   B CD1 1 
ATOM   1440 C  CD2 . PHE   B 1 87  ? -10.096 8.445   10.150  1.00 14.38 ? 87  PHE   B CD2 1 
ATOM   1441 C  CE1 . PHE   B 1 87  ? -10.641 9.567   7.711   1.00 18.01 ? 87  PHE   B CE1 1 
ATOM   1442 C  CE2 . PHE   B 1 87  ? -10.742 7.715   9.202   1.00 17.01 ? 87  PHE   B CE2 1 
ATOM   1443 C  CZ  . PHE   B 1 87  ? -10.984 8.267   7.990   1.00 17.61 ? 87  PHE   B CZ  1 
ATOM   1444 N  N   . HIS   B 1 88  ? -11.157 10.148  13.156  1.00 11.45 ? 88  HIS   B N   1 
ATOM   1445 C  CA  . HIS   B 1 88  ? -12.253 9.291   13.543  1.00 11.50 ? 88  HIS   B CA  1 
ATOM   1446 C  C   . HIS   B 1 88  ? -13.262 10.035  14.401  1.00 12.37 ? 88  HIS   B C   1 
ATOM   1447 O  O   . HIS   B 1 88  ? -12.964 10.945  15.135  1.00 13.07 ? 88  HIS   B O   1 
ATOM   1448 C  CB  . HIS   B 1 88  ? -11.722 8.075   14.322  1.00 12.41 ? 88  HIS   B CB  1 
ATOM   1449 C  CG  . HIS   B 1 88  ? -10.649 7.296   13.624  1.00 14.20 ? 88  HIS   B CG  1 
ATOM   1450 N  ND1 . HIS   B 1 88  ? -10.865 6.251   12.802  1.00 19.18 ? 88  HIS   B ND1 1 
ATOM   1451 C  CD2 . HIS   B 1 88  ? -9.288  7.495   13.691  1.00 12.38 ? 88  HIS   B CD2 1 
ATOM   1452 C  CE1 . HIS   B 1 88  ? -9.677  5.829   12.333  1.00 15.84 ? 88  HIS   B CE1 1 
ATOM   1453 N  NE2 . HIS   B 1 88  ? -8.718  6.600   12.901  1.00 21.09 ? 88  HIS   B NE2 1 
ATOM   1454 N  N   . GLU   B 1 89  ? -14.530 9.531   14.380  1.00 12.48 ? 89  GLU   B N   1 
ATOM   1455 C  CA  . GLU   B 1 89  ? -15.528 9.987   15.296  1.00 13.06 ? 89  GLU   B CA  1 
ATOM   1456 C  C   . GLU   B 1 89  ? -15.229 9.529   16.720  1.00 14.16 ? 89  GLU   B C   1 
ATOM   1457 O  O   . GLU   B 1 89  ? -15.474 10.210  17.665  1.00 18.41 ? 89  GLU   B O   1 
ATOM   1458 C  CB  . GLU   B 1 89  ? -16.926 9.549   14.852  1.00 14.95 ? 89  GLU   B CB  1 
ATOM   1459 C  CG  . GLU   B 1 89  ? -17.374 10.269  13.607  1.00 17.18 ? 89  GLU   B CG  1 
ATOM   1460 C  CD  . GLU   B 1 89  ? -17.638 11.781  13.849  1.00 19.12 ? 89  GLU   B CD  1 
ATOM   1461 O  OE1 . GLU   B 1 89  ? -18.414 12.118  14.701  1.00 24.40 ? 89  GLU   B OE1 1 
ATOM   1462 O  OE2 . GLU   B 1 89  ? -16.963 12.567  13.200  1.00 20.63 ? 89  GLU   B OE2 1 
ATOM   1463 N  N   . HIS   B 1 90  ? -14.737 8.314   16.839  1.00 14.19 ? 90  HIS   B N   1 
ATOM   1464 C  CA  . HIS   B 1 90  ? -14.478 7.638   18.111  1.00 14.04 ? 90  HIS   B CA  1 
ATOM   1465 C  C   . HIS   B 1 90  ? -13.692 6.407   17.794  1.00 16.20 ? 90  HIS   B C   1 
ATOM   1466 O  O   . HIS   B 1 90  ? -13.460 6.103   16.650  1.00 17.92 ? 90  HIS   B O   1 
ATOM   1467 C  CB  . HIS   B 1 90  ? -15.789 7.301   18.849  1.00 17.02 ? 90  HIS   B CB  1 
ATOM   1468 C  CG  . HIS   B 1 90  ? -16.729 6.503   18.015  1.00 23.39 ? 90  HIS   B CG  1 
ATOM   1469 N  ND1 . HIS   B 1 90  ? -16.536 5.172   17.700  1.00 33.17 ? 90  HIS   B ND1 1 
ATOM   1470 C  CD2 . HIS   B 1 90  ? -17.859 6.872   17.403  1.00 25.38 ? 90  HIS   B CD2 1 
ATOM   1471 C  CE1 . HIS   B 1 90  ? -17.525 4.732   16.945  1.00 34.95 ? 90  HIS   B CE1 1 
ATOM   1472 N  NE2 . HIS   B 1 90  ? -18.385 5.758   16.776  1.00 34.13 ? 90  HIS   B NE2 1 
ATOM   1473 N  N   . ALA   B 1 91  ? -13.207 5.715   18.827  1.00 17.29 ? 91  ALA   B N   1 
ATOM   1474 C  CA  . ALA   B 1 91  ? -12.632 4.388   18.705  1.00 18.96 ? 91  ALA   B CA  1 
ATOM   1475 C  C   . ALA   B 1 91  ? -13.541 3.464   19.445  1.00 19.31 ? 91  ALA   B C   1 
ATOM   1476 O  O   . ALA   B 1 91  ? -13.890 3.760   20.556  1.00 19.34 ? 91  ALA   B O   1 
ATOM   1477 C  CB  . ALA   B 1 91  ? -11.221 4.398   19.305  1.00 21.35 ? 91  ALA   B CB  1 
ATOM   1478 N  N   . GLU   B 1 92  ? -14.017 2.400   18.786  0.95 25.20 ? 92  GLU   B N   1 
ATOM   1479 C  CA  . GLU   B 1 92  ? -14.967 1.399   19.276  0.95 23.20 ? 92  GLU   B CA  1 
ATOM   1480 C  C   . GLU   B 1 92  ? -14.293 0.064   19.410  0.95 25.59 ? 92  GLU   B C   1 
ATOM   1481 O  O   . GLU   B 1 92  ? -13.559 -0.371  18.542  0.95 30.76 ? 92  GLU   B O   1 
ATOM   1482 C  CB  . GLU   B 1 92  ? -16.225 1.253   18.398  0.95 34.24 ? 92  GLU   B CB  1 
ATOM   1483 N  N   . VAL   B 1 93  ? -14.504 -0.541  20.524  1.00 18.72 ? 93  VAL   B N   1 
ATOM   1484 C  CA  . VAL   B 1 93  ? -13.990 -1.919  20.762  1.00 16.80 ? 93  VAL   B CA  1 
ATOM   1485 C  C   . VAL   B 1 93  ? -15.223 -2.762  21.048  1.00 13.21 ? 93  VAL   B C   1 
ATOM   1486 O  O   . VAL   B 1 93  ? -15.889 -2.478  22.007  1.00 15.97 ? 93  VAL   B O   1 
ATOM   1487 C  CB  . VAL   B 1 93  ? -12.999 -1.804  21.938  1.00 18.89 ? 93  VAL   B CB  1 
ATOM   1488 C  CG1 . VAL   B 1 93  ? -12.520 -3.169  22.159  1.00 22.68 ? 93  VAL   B CG1 1 
ATOM   1489 C  CG2 . VAL   B 1 93  ? -11.811 -0.854  21.608  1.00 23.98 ? 93  VAL   B CG2 1 
ATOM   1490 N  N   . VAL   B 1 94  ? -15.466 -3.826  20.293  1.00 13.64 ? 94  VAL   B N   1 
ATOM   1491 C  CA  . VAL   B 1 94  ? -16.628 -4.695  20.506  1.00 13.25 ? 94  VAL   B CA  1 
ATOM   1492 C  C   . VAL   B 1 94  ? -16.105 -6.124  20.736  1.00 13.13 ? 94  VAL   B C   1 
ATOM   1493 O  O   . VAL   B 1 94  ? -15.279 -6.597  19.936  1.00 13.76 ? 94  VAL   B O   1 
ATOM   1494 C  CB  . VAL   B 1 94  ? -17.602 -4.644  19.340  1.00 14.76 ? 94  VAL   B CB  1 
ATOM   1495 C  CG1 . VAL   B 1 94  ? -18.790 -5.639  19.567  1.00 18.36 ? 94  VAL   B CG1 1 
ATOM   1496 C  CG2 . VAL   B 1 94  ? -18.142 -3.262  19.129  1.00 18.25 ? 94  VAL   B CG2 1 
ATOM   1497 N  N   . PHE   B 1 95  ? -16.526 -6.782  21.786  1.00 13.31 ? 95  PHE   B N   1 
ATOM   1498 C  CA  . PHE   B 1 95  ? -15.935 -8.085  22.183  1.00 13.71 ? 95  PHE   B CA  1 
ATOM   1499 C  C   . PHE   B 1 95  ? -16.999 -8.861  22.921  1.00 14.21 ? 95  PHE   B C   1 
ATOM   1500 O  O   . PHE   B 1 95  ? -17.870 -8.316  23.587  1.00 16.01 ? 95  PHE   B O   1 
ATOM   1501 C  CB  . PHE   B 1 95  ? -14.688 -7.871  23.023  1.00 14.50 ? 95  PHE   B CB  1 
ATOM   1502 C  CG  . PHE   B 1 95  ? -14.908 -7.256  24.373  1.00 15.07 ? 95  PHE   B CG  1 
ATOM   1503 C  CD1 . PHE   B 1 95  ? -15.078 -5.941  24.537  1.00 16.38 ? 95  PHE   B CD1 1 
ATOM   1504 C  CD2 . PHE   B 1 95  ? -14.890 -8.052  25.489  1.00 17.34 ? 95  PHE   B CD2 1 
ATOM   1505 C  CE1 . PHE   B 1 95  ? -15.234 -5.363  25.844  1.00 19.64 ? 95  PHE   B CE1 1 
ATOM   1506 C  CE2 . PHE   B 1 95  ? -15.016 -7.526  26.731  1.00 22.01 ? 95  PHE   B CE2 1 
ATOM   1507 C  CZ  . PHE   B 1 95  ? -15.198 -6.201  26.936  1.00 20.31 ? 95  PHE   B CZ  1 
ATOM   1508 N  N   . THR   B 1 96  ? -16.911 -10.194 22.867  1.00 16.83 ? 96  THR   B N   1 
ATOM   1509 C  CA  . THR   B 1 96  ? -17.695 -11.108 23.652  1.00 17.47 ? 96  THR   B CA  1 
ATOM   1510 C  C   . THR   B 1 96  ? -16.924 -11.334 24.934  1.00 18.46 ? 96  THR   B C   1 
ATOM   1511 O  O   . THR   B 1 96  ? -15.740 -11.712 24.893  1.00 20.03 ? 96  THR   B O   1 
ATOM   1512 C  CB  . THR   B 1 96  ? -17.905 -12.442 22.944  1.00 18.83 ? 96  THR   B CB  1 
ATOM   1513 O  OG1 . THR   B 1 96  ? -18.666 -12.155 21.783  1.00 20.96 ? 96  THR   B OG1 1 
ATOM   1514 C  CG2 . THR   B 1 96  ? -18.675 -13.405 23.831  1.00 23.34 ? 96  THR   B CG2 1 
ATOM   1515 N  N   . ALA   B 1 97  ? -17.543 -11.140 26.082  1.00 17.56 ? 97  ALA   B N   1 
ATOM   1516 C  CA  . ALA   B 1 97  ? -16.910 -11.297 27.346  1.00 19.06 ? 97  ALA   B CA  1 
ATOM   1517 C  C   . ALA   B 1 97  ? -17.209 -12.637 27.961  1.00 21.21 ? 97  ALA   B C   1 
ATOM   1518 O  O   . ALA   B 1 97  ? -18.354 -13.165 27.843  1.00 23.25 ? 97  ALA   B O   1 
ATOM   1519 C  CB  . ALA   B 1 97  ? -17.334 -10.122 28.249  1.00 23.53 ? 97  ALA   B CB  1 
ATOM   1520 N  N   . ASN   B 1 98  ? -16.225 -13.117 28.703  1.00 22.42 ? 98  ASN   B N   1 
ATOM   1521 C  CA  . ASN   B 1 98  ? -16.424 -14.194 29.677  1.00 23.00 ? 98  ASN   B CA  1 
ATOM   1522 C  C   . ASN   B 1 98  ? -16.836 -15.535 29.077  1.00 27.10 ? 98  ASN   B C   1 
ATOM   1523 O  O   . ASN   B 1 98  ? -17.451 -16.373 29.737  1.00 32.40 ? 98  ASN   B O   1 
ATOM   1524 C  CB  . ASN   B 1 98  ? -17.365 -13.731 30.802  1.00 22.37 ? 98  ASN   B CB  1 
ATOM   1525 C  CG  . ASN   B 1 98  ? -16.915 -12.443 31.375  1.00 25.29 ? 98  ASN   B CG  1 
ATOM   1526 O  OD1 . ASN   B 1 98  ? -15.732 -12.266 31.775  1.00 22.52 ? 98  ASN   B OD1 1 
ATOM   1527 N  ND2 . ASN   B 1 98  ? -17.861 -11.502 31.388  1.00 39.58 ? 98  ASN   B ND2 1 
ATOM   1528 N  N   . ASP   B 1 99  ? -16.648 -15.650 27.775  0.50 18.43 ? 99  ASP   B N   1 
ATOM   1529 C  CA  . ASP   B 1 99  ? -17.072 -16.849 27.020  0.50 21.09 ? 99  ASP   B CA  1 
ATOM   1530 C  C   . ASP   B 1 99  ? -16.584 -18.176 27.563  0.50 26.19 ? 99  ASP   B C   1 
ATOM   1531 O  O   . ASP   B 1 99  ? -17.215 -19.233 27.328  0.50 23.49 ? 99  ASP   B O   1 
ATOM   1532 C  CB  . ASP   B 1 99  ? -16.566 -16.753 25.603  0.50 25.13 ? 99  ASP   B CB  1 
ATOM   1533 N  N   . SER   B 1 100 ? -15.489 -18.126 28.305  1.00 32.11 ? 100 SER   B N   1 
ATOM   1534 C  CA  . SER   B 1 100 ? -14.847 -19.338 28.917  1.00 39.42 ? 100 SER   B CA  1 
ATOM   1535 C  C   . SER   B 1 100 ? -14.672 -19.329 30.452  1.00 49.41 ? 100 SER   B C   1 
ATOM   1536 C  CB  . SER   B 1 100 ? -13.458 -19.601 28.297  1.00 38.24 ? 100 SER   B CB  1 
ATOM   1537 O  OG  . SER   B 1 100 ? -13.558 -19.776 26.910  0.50 38.25 ? 100 SER   B OG  1 
ATOM   1538 N  N   . GLY   B 1 101 ? -15.467 -18.471 31.093  1.00 30.53 ? 101 GLY   B N   1 
ATOM   1539 C  CA  . GLY   B 1 101 ? -15.263 -18.086 32.473  1.00 36.07 ? 101 GLY   B CA  1 
ATOM   1540 C  C   . GLY   B 1 101 ? -15.130 -16.578 32.602  1.00 38.58 ? 101 GLY   B C   1 
ATOM   1541 O  O   . GLY   B 1 101 ? -14.729 -15.917 31.687  1.00 29.58 ? 101 GLY   B O   1 
ATOM   1542 N  N   . PRO   B 1 102 ? -15.371 -16.025 33.779  1.00 27.10 ? 102 PRO   B N   1 
ATOM   1543 C  CA  . PRO   B 1 102 ? -15.022 -14.644 34.069  1.00 28.94 ? 102 PRO   B CA  1 
ATOM   1544 C  C   . PRO   B 1 102 ? -13.531 -14.329 33.890  1.00 30.23 ? 102 PRO   B C   1 
ATOM   1545 O  O   . PRO   B 1 102 ? -12.645 -15.028 34.278  1.00 34.25 ? 102 PRO   B O   1 
ATOM   1546 C  CB  . PRO   B 1 102 ? -15.450 -14.432 35.526  1.00 30.73 ? 102 PRO   B CB  1 
ATOM   1547 C  CG  . PRO   B 1 102 ? -15.631 -15.782 36.072  1.00 36.45 ? 102 PRO   B CG  1 
ATOM   1548 C  CD  . PRO   B 1 102 ? -15.843 -16.764 34.961  1.00 30.25 ? 102 PRO   B CD  1 
ATOM   1549 N  N   . ARG   B 1 103 ? -13.257 -13.208 33.279  0.50 18.86 ? 103 ARG   B N   1 
ATOM   1550 C  CA  . ARG   B 1 103 ? -11.875 -12.731 33.095  0.50 18.52 ? 103 ARG   B CA  1 
ATOM   1551 C  C   . ARG   B 1 103 ? -11.750 -11.300 33.572  0.50 21.03 ? 103 ARG   B C   1 
ATOM   1552 O  O   . ARG   B 1 103 ? -12.789 -10.611 33.676  0.50 23.16 ? 103 ARG   B O   1 
ATOM   1553 C  CB  . ARG   B 1 103 ? -11.410 -12.925 31.635  0.50 22.91 ? 103 ARG   B CB  1 
ATOM   1554 C  CG  . ARG   B 1 103 ? -11.475 -14.321 31.103  0.50 24.00 ? 103 ARG   B CG  1 
ATOM   1555 C  CD  . ARG   B 1 103 ? -10.383 -15.153 31.754  0.50 23.07 ? 103 ARG   B CD  1 
ATOM   1556 N  NE  . ARG   B 1 103 ? -10.208 -16.435 31.100  0.50 30.72 ? 103 ARG   B NE  1 
ATOM   1557 C  CZ  . ARG   B 1 103 ? -10.920 -17.478 31.486  0.50 36.37 ? 103 ARG   B CZ  1 
ATOM   1558 N  NH1 . ARG   B 1 103 ? -11.746 -17.328 32.500  0.50 30.44 ? 103 ARG   B NH1 1 
ATOM   1559 N  NH2 . ARG   B 1 103 ? -10.797 -18.667 30.925  0.50 34.91 ? 103 ARG   B NH2 1 
ATOM   1560 N  N   . ARG   B 1 104 ? -10.478 -10.840 33.834  1.00 23.91 ? 104 ARG   B N   1 
ATOM   1561 C  CA  . ARG   B 1 104 ? -10.214 -9.405  33.914  1.00 21.31 ? 104 ARG   B CA  1 
ATOM   1562 C  C   . ARG   B 1 104 ? -9.776  -8.914  32.576  1.00 20.17 ? 104 ARG   B C   1 
ATOM   1563 O  O   . ARG   B 1 104 ? -8.826  -9.464  31.994  1.00 21.63 ? 104 ARG   B O   1 
ATOM   1564 C  CB  . ARG   B 1 104 ? -9.094  -9.112  34.924  1.00 28.58 ? 104 ARG   B CB  1 
ATOM   1565 N  N   . TYR   B 1 105 ? -10.372 -7.831  32.120  1.00 17.16 ? 105 TYR   B N   1 
ATOM   1566 C  CA  . TYR   B 1 105 ? -10.117 -7.235  30.824  1.00 16.77 ? 105 TYR   B CA  1 
ATOM   1567 C  C   . TYR   B 1 105 ? -9.544  -5.856  31.033  1.00 16.49 ? 105 TYR   B C   1 
ATOM   1568 O  O   . TYR   B 1 105 ? -10.155 -5.021  31.651  1.00 18.37 ? 105 TYR   B O   1 
ATOM   1569 C  CB  . TYR   B 1 105 ? -11.375 -7.110  29.972  1.00 18.05 ? 105 TYR   B CB  1 
ATOM   1570 C  CG  . TYR   B 1 105 ? -11.956 -8.417  29.630  1.00 18.63 ? 105 TYR   B CG  1 
ATOM   1571 C  CD1 . TYR   B 1 105 ? -11.650 -9.013  28.442  1.00 22.29 ? 105 TYR   B CD1 1 
ATOM   1572 C  CD2 . TYR   B 1 105 ? -12.902 -8.969  30.434  1.00 20.25 ? 105 TYR   B CD2 1 
ATOM   1573 C  CE1 . TYR   B 1 105 ? -12.196 -10.247 28.086  1.00 23.07 ? 105 TYR   B CE1 1 
ATOM   1574 C  CE2 . TYR   B 1 105 ? -13.468 -10.240 30.110  1.00 22.52 ? 105 TYR   B CE2 1 
ATOM   1575 C  CZ  . TYR   B 1 105 ? -13.105 -10.863 28.905  1.00 19.06 ? 105 TYR   B CZ  1 
ATOM   1576 O  OH  . TYR   B 1 105 ? -13.674 -12.116 28.615  1.00 23.33 ? 105 TYR   B OH  1 
ATOM   1577 N  N   . THR   B 1 106 ? -8.425  -5.598  30.370  1.00 14.47 ? 106 THR   B N   1 
ATOM   1578 C  CA  . THR   B 1 106 ? -7.898  -4.260  30.182  1.00 15.07 ? 106 THR   B CA  1 
ATOM   1579 C  C   . THR   B 1 106 ? -7.963  -3.973  28.715  1.00 15.16 ? 106 THR   B C   1 
ATOM   1580 O  O   . THR   B 1 106 ? -7.379  -4.737  27.909  1.00 16.29 ? 106 THR   B O   1 
ATOM   1581 C  CB  . THR   B 1 106 ? -6.510  -4.078  30.657  1.00 17.29 ? 106 THR   B CB  1 
ATOM   1582 O  OG1 . THR   B 1 106 ? -6.473  -4.269  32.082  1.00 22.83 ? 106 THR   B OG1 1 
ATOM   1583 C  CG2 . THR   B 1 106 ? -5.952  -2.636  30.358  1.00 21.55 ? 106 THR   B CG2 1 
ATOM   1584 N  N   . ILE   B 1 107 ? -8.645  -2.915  28.337  1.00 14.36 ? 107 ILE   B N   1 
ATOM   1585 C  CA  . ILE   B 1 107 ? -8.735  -2.438  26.961  1.00 15.02 ? 107 ILE   B CA  1 
ATOM   1586 C  C   . ILE   B 1 107 ? -7.754  -1.293  26.881  1.00 14.91 ? 107 ILE   B C   1 
ATOM   1587 O  O   . ILE   B 1 107 ? -7.978  -0.274  27.512  1.00 16.11 ? 107 ILE   B O   1 
ATOM   1588 C  CB  . ILE   B 1 107 ? -10.159 -1.996  26.566  1.00 16.98 ? 107 ILE   B CB  1 
ATOM   1589 C  CG1 . ILE   B 1 107 ? -11.222 -3.053  26.774  1.00 25.82 ? 107 ILE   B CG1 1 
ATOM   1590 C  CG2 . ILE   B 1 107 ? -10.206 -1.383  25.154  1.00 19.99 ? 107 ILE   B CG2 1 
ATOM   1591 C  CD1 . ILE   B 1 107 ? -10.902 -4.307  26.186  1.00 22.81 ? 107 ILE   B CD1 1 
ATOM   1592 N  N   . ALA   B 1 108 ? -6.709  -1.439  26.092  1.00 13.97 ? 108 ALA   B N   1 
ATOM   1593 C  CA  . ALA   B 1 108 ? -5.708  -0.420  25.946  1.00 17.22 ? 108 ALA   B CA  1 
ATOM   1594 C  C   . ALA   B 1 108 ? -5.806  0.195   24.588  1.00 16.44 ? 108 ALA   B C   1 
ATOM   1595 O  O   . ALA   B 1 108 ? -5.917  -0.520  23.592  1.00 22.18 ? 108 ALA   B O   1 
ATOM   1596 C  CB  . ALA   B 1 108 ? -4.338  -1.022  26.171  1.00 20.33 ? 108 ALA   B CB  1 
ATOM   1597 N  N   . ALA   B 1 109 ? -5.822  1.487   24.510  1.00 13.36 ? 109 ALA   B N   1 
ATOM   1598 C  CA  . ALA   B 1 109 ? -5.905  2.188   23.222  1.00 13.32 ? 109 ALA   B CA  1 
ATOM   1599 C  C   . ALA   B 1 109 ? -4.755  3.183   23.140  1.00 12.79 ? 109 ALA   B C   1 
ATOM   1600 O  O   . ALA   B 1 109 ? -4.469  3.917   24.101  1.00 15.71 ? 109 ALA   B O   1 
ATOM   1601 C  CB  . ALA   B 1 109 ? -7.211  2.956   23.138  1.00 15.65 ? 109 ALA   B CB  1 
ATOM   1602 N  N   . LEU   B 1 110 ? -4.130  3.239   21.990  1.00 11.53 ? 110 LEU   B N   1 
ATOM   1603 C  CA  . LEU   B 1 110 ? -3.060  4.139   21.695  1.00 11.32 ? 110 LEU   B CA  1 
ATOM   1604 C  C   . LEU   B 1 110 ? -3.553  5.014   20.542  1.00 11.45 ? 110 LEU   B C   1 
ATOM   1605 O  O   . LEU   B 1 110 ? -3.884  4.560   19.496  1.00 13.98 ? 110 LEU   B O   1 
ATOM   1606 C  CB  . LEU   B 1 110 ? -1.844  3.369   21.223  1.00 13.09 ? 110 LEU   B CB  1 
ATOM   1607 C  CG  . LEU   B 1 110 ? -0.639  4.230   20.781  1.00 15.33 ? 110 LEU   B CG  1 
ATOM   1608 C  CD1 . LEU   B 1 110 ? -0.118  5.105   21.915  1.00 17.01 ? 110 LEU   B CD1 1 
ATOM   1609 C  CD2 . LEU   B 1 110 ? 0.419   3.282   20.202  1.00 21.87 ? 110 LEU   B CD2 1 
ATOM   1610 N  N   . LEU   B 1 111 ? -3.617  6.313   20.812  1.00 11.04 ? 111 LEU   B N   1 
ATOM   1611 C  CA  . LEU   B 1 111 ? -4.273  7.286   19.942  1.00 10.95 ? 111 LEU   B CA  1 
ATOM   1612 C  C   . LEU   B 1 111 ? -3.303  8.227   19.200  1.00 10.61 ? 111 LEU   B C   1 
ATOM   1613 O  O   . LEU   B 1 111 ? -2.458  8.851   19.825  1.00 11.00 ? 111 LEU   B O   1 
ATOM   1614 C  CB  . LEU   B 1 111 ? -5.231  8.180   20.745  1.00 12.23 ? 111 LEU   B CB  1 
ATOM   1615 C  CG  . LEU   B 1 111 ? -6.263  7.485   21.618  1.00 11.94 ? 111 LEU   B CG  1 
ATOM   1616 C  CD1 . LEU   B 1 111 ? -7.118  8.594   22.235  1.00 13.86 ? 111 LEU   B CD1 1 
ATOM   1617 C  CD2 . LEU   B 1 111 ? -7.046  6.457   20.821  1.00 13.58 ? 111 LEU   B CD2 1 
ATOM   1618 N  N   . SER   B 1 112 ? -3.524  8.304   17.910  1.00 10.37 ? 112 SER   B N   1 
ATOM   1619 C  CA  . SER   B 1 112 ? -2.983  9.356   17.087  1.00 11.32 ? 112 SER   B CA  1 
ATOM   1620 C  C   . SER   B 1 112 ? -4.135  10.026  16.309  1.00 10.55 ? 112 SER   B C   1 
ATOM   1621 O  O   . SER   B 1 112 ? -5.206  9.456   16.203  1.00 11.47 ? 112 SER   B O   1 
ATOM   1622 C  CB  . SER   B 1 112 ? -1.937  8.812   16.087  1.00 11.32 ? 112 SER   B CB  1 
ATOM   1623 O  OG  . SER   B 1 112 ? -0.838  8.267   16.752  1.00 13.54 ? 112 SER   B OG  1 
ATOM   1624 N  N   . PRO   B 1 113 ? -3.923  11.212  15.719  1.00 10.63 ? 113 PRO   B N   1 
ATOM   1625 C  CA  . PRO   B 1 113 ? -5.087  11.860  15.096  1.00 11.48 ? 113 PRO   B CA  1 
ATOM   1626 C  C   . PRO   B 1 113 ? -5.703  11.087  13.950  1.00 11.83 ? 113 PRO   B C   1 
ATOM   1627 O  O   . PRO   B 1 113 ? -6.900  11.132  13.765  1.00 12.17 ? 113 PRO   B O   1 
ATOM   1628 C  CB  . PRO   B 1 113 ? -4.472  13.212  14.649  1.00 12.41 ? 113 PRO   B CB  1 
ATOM   1629 C  CG  . PRO   B 1 113 ? -3.417  13.453  15.678  1.00 13.55 ? 113 PRO   B CG  1 
ATOM   1630 C  CD  . PRO   B 1 113 ? -2.799  12.118  15.975  1.00 11.62 ? 113 PRO   B CD  1 
ATOM   1631 N  N   . TYR   B 1 114 ? -4.891  10.376  13.160  1.00 10.28 ? 114 TYR   B N   1 
ATOM   1632 C  CA  . TYR   B 1 114 ? -5.374  9.607   11.974  1.00 11.23 ? 114 TYR   B CA  1 
ATOM   1633 C  C   . TYR   B 1 114 ? -5.175  8.078   12.112  1.00 11.21 ? 114 TYR   B C   1 
ATOM   1634 O  O   . TYR   B 1 114 ? -5.293  7.377   11.124  1.00 13.38 ? 114 TYR   B O   1 
ATOM   1635 C  CB  . TYR   B 1 114 ? -4.729  10.145  10.689  1.00 11.31 ? 114 TYR   B CB  1 
ATOM   1636 C  CG  . TYR   B 1 114 ? -5.505  11.298  10.097  1.00 11.73 ? 114 TYR   B CG  1 
ATOM   1637 C  CD1 . TYR   B 1 114 ? -5.606  12.514  10.756  1.00 15.74 ? 114 TYR   B CD1 1 
ATOM   1638 C  CD2 . TYR   B 1 114 ? -6.196  11.150  8.908   1.00 12.40 ? 114 TYR   B CD2 1 
ATOM   1639 C  CE1 . TYR   B 1 114 ? -6.344  13.562  10.228  1.00 19.60 ? 114 TYR   B CE1 1 
ATOM   1640 C  CE2 . TYR   B 1 114 ? -6.937  12.185  8.368   1.00 15.13 ? 114 TYR   B CE2 1 
ATOM   1641 C  CZ  . TYR   B 1 114 ? -7.013  13.394  9.029   1.00 17.67 ? 114 TYR   B CZ  1 
ATOM   1642 O  OH  . TYR   B 1 114 ? -7.756  14.406  8.489   1.00 22.75 ? 114 TYR   B OH  1 
ATOM   1643 N  N   . SER   B 1 115 ? -4.912  7.627   13.330  1.00 11.16 ? 115 SER   B N   1 
ATOM   1644 C  CA  A SER   B 1 115 ? -4.696  6.216   13.546  0.50 11.09 ? 115 SER   B CA  1 
ATOM   1645 C  CA  B SER   B 1 115 ? -4.718  6.217   13.542  0.50 11.49 ? 115 SER   B CA  1 
ATOM   1646 C  C   . SER   B 1 115 ? -4.935  5.875   15.000  1.00 11.42 ? 115 SER   B C   1 
ATOM   1647 O  O   . SER   B 1 115 ? -4.621  6.682   15.893  1.00 14.92 ? 115 SER   B O   1 
ATOM   1648 C  CB  A SER   B 1 115 ? -3.246  5.841   13.221  0.50 11.85 ? 115 SER   B CB  1 
ATOM   1649 C  CB  B SER   B 1 115 ? -3.294  5.805   13.168  0.50 15.31 ? 115 SER   B CB  1 
ATOM   1650 O  OG  A SER   B 1 115 ? -3.010  4.437   13.276  0.50 11.00 ? 115 SER   B OG  1 
ATOM   1651 O  OG  B SER   B 1 115 ? -2.342  6.181   14.188  0.50 27.89 ? 115 SER   B OG  1 
ATOM   1652 N  N   . TYR   B 1 116 ? -5.432  4.693   15.274  1.00 12.17 ? 116 TYR   B N   1 
ATOM   1653 C  CA  . TYR   B 1 116 ? -5.429  4.203   16.623  1.00 12.30 ? 116 TYR   B CA  1 
ATOM   1654 C  C   . TYR   B 1 116 ? -5.203  2.684   16.617  1.00 11.55 ? 116 TYR   B C   1 
ATOM   1655 O  O   . TYR   B 1 116 ? -5.458  2.020   15.662  1.00 12.49 ? 116 TYR   B O   1 
ATOM   1656 C  CB  . TYR   B 1 116 ? -6.654  4.534   17.434  1.00 13.26 ? 116 TYR   B CB  1 
ATOM   1657 C  CG  . TYR   B 1 116 ? -7.932  3.930   16.933  1.00 14.34 ? 116 TYR   B CG  1 
ATOM   1658 C  CD1 . TYR   B 1 116 ? -8.307  2.665   17.320  1.00 15.68 ? 116 TYR   B CD1 1 
ATOM   1659 C  CD2 . TYR   B 1 116 ? -8.736  4.625   16.043  1.00 17.67 ? 116 TYR   B CD2 1 
ATOM   1660 C  CE1 . TYR   B 1 116 ? -9.492  2.083   16.805  1.00 19.62 ? 116 TYR   B CE1 1 
ATOM   1661 C  CE2 . TYR   B 1 116 ? -9.904  4.113   15.590  1.00 20.94 ? 116 TYR   B CE2 1 
ATOM   1662 C  CZ  . TYR   B 1 116 ? -10.285 2.863   15.964  1.00 20.23 ? 116 TYR   B CZ  1 
ATOM   1663 O  OH  . TYR   B 1 116 ? -11.455 2.375   15.438  1.00 30.31 ? 116 TYR   B OH  1 
ATOM   1664 N  N   . SER   B 1 117 ? -4.716  2.203   17.758  1.00 12.72 ? 117 SER   B N   1 
ATOM   1665 C  CA  A SER   B 1 117 ? -4.650  0.779   17.985  0.70 13.96 ? 117 SER   B CA  1 
ATOM   1666 C  CA  B SER   B 1 117 ? -4.462  0.799   18.070  0.30 12.97 ? 117 SER   B CA  1 
ATOM   1667 C  C   . SER   B 1 117 ? -5.287  0.459   19.296  1.00 14.87 ? 117 SER   B C   1 
ATOM   1668 O  O   . SER   B 1 117 ? -5.351  1.257   20.247  1.00 15.89 ? 117 SER   B O   1 
ATOM   1669 C  CB  A SER   B 1 117 ? -3.263  0.284   17.945  0.70 17.12 ? 117 SER   B CB  1 
ATOM   1670 C  CB  B SER   B 1 117 ? -3.001  0.629   18.440  0.30 12.57 ? 117 SER   B CB  1 
ATOM   1671 O  OG  A SER   B 1 117 ? -2.673  0.458   19.165  0.70 19.86 ? 117 SER   B OG  1 
ATOM   1672 O  OG  B SER   B 1 117 ? -2.595  -0.720  18.455  0.30 16.41 ? 117 SER   B OG  1 
ATOM   1673 N  N   . THR   B 1 118 ? -5.851  -0.717  19.321  1.00 16.26 ? 118 THR   B N   1 
ATOM   1674 C  CA  . THR   B 1 118 ? -6.417  -1.193  20.522  1.00 16.40 ? 118 THR   B CA  1 
ATOM   1675 C  C   . THR   B 1 118 ? -6.047  -2.617  20.793  1.00 15.09 ? 118 THR   B C   1 
ATOM   1676 O  O   . THR   B 1 118 ? -5.953  -3.412  19.865  1.00 19.58 ? 118 THR   B O   1 
ATOM   1677 C  CB  . THR   B 1 118 ? -7.904  -1.033  20.506  1.00 18.74 ? 118 THR   B CB  1 
ATOM   1678 O  OG1 . THR   B 1 118 ? -8.329  -1.258  21.810  1.00 20.91 ? 118 THR   B OG1 1 
ATOM   1679 C  CG2 . THR   B 1 118 ? -8.770  -1.849  19.539  1.00 17.97 ? 118 THR   B CG2 1 
ATOM   1680 N  N   . THR   B 1 119 ? -5.810  -2.949  22.031  1.00 13.33 ? 119 THR   B N   1 
ATOM   1681 C  CA  A THR   B 1 119 ? -5.344  -4.297  22.397  0.50 12.70 ? 119 THR   B CA  1 
ATOM   1682 C  CA  B THR   B 1 119 ? -5.379  -4.276  22.401  0.50 12.79 ? 119 THR   B CA  1 
ATOM   1683 C  C   . THR   B 1 119 ? -6.113  -4.686  23.665  1.00 12.21 ? 119 THR   B C   1 
ATOM   1684 O  O   . THR   B 1 119 ? -6.494  -3.845  24.444  1.00 16.15 ? 119 THR   B O   1 
ATOM   1685 C  CB  A THR   B 1 119 ? -3.780  -4.477  22.602  0.50 16.52 ? 119 THR   B CB  1 
ATOM   1686 C  CB  B THR   B 1 119 ? -3.875  -4.297  22.642  0.50 17.18 ? 119 THR   B CB  1 
ATOM   1687 O  OG1 A THR   B 1 119 ? -3.465  -5.887  22.638  0.50 22.31 ? 119 THR   B OG1 1 
ATOM   1688 O  OG1 B THR   B 1 119 ? -3.263  -3.624  21.538  0.50 16.37 ? 119 THR   B OG1 1 
ATOM   1689 C  CG2 A THR   B 1 119 ? -3.287  -3.885  23.894  0.50 19.45 ? 119 THR   B CG2 1 
ATOM   1690 C  CG2 B THR   B 1 119 ? -3.382  -5.794  22.797  0.50 20.02 ? 119 THR   B CG2 1 
ATOM   1691 N  N   . ALA   B 1 120 ? -6.305  -5.931  23.871  1.00 13.85 ? 120 ALA   B N   1 
ATOM   1692 C  CA  . ALA   B 1 120 ? -6.926  -6.466  25.069  1.00 13.42 ? 120 ALA   B CA  1 
ATOM   1693 C  C   . ALA   B 1 120 ? -5.898  -7.237  25.825  1.00 14.52 ? 120 ALA   B C   1 
ATOM   1694 O  O   . ALA   B 1 120 ? -5.197  -8.089  25.223  1.00 17.10 ? 120 ALA   B O   1 
ATOM   1695 C  CB  . ALA   B 1 120 ? -8.097  -7.377  24.721  1.00 16.69 ? 120 ALA   B CB  1 
ATOM   1696 N  N   . VAL   B 1 121 ? -5.796  -7.000  27.120  1.00 13.36 ? 121 VAL   B N   1 
ATOM   1697 C  CA  . VAL   B 1 121 ? -5.007  -7.778  28.017  1.00 15.63 ? 121 VAL   B CA  1 
ATOM   1698 C  C   . VAL   B 1 121 ? -5.999  -8.483  28.889  1.00 16.56 ? 121 VAL   B C   1 
ATOM   1699 O  O   . VAL   B 1 121 ? -6.762  -7.846  29.636  1.00 18.54 ? 121 VAL   B O   1 
ATOM   1700 C  CB  . VAL   B 1 121 ? -4.029  -6.914  28.780  1.00 18.60 ? 121 VAL   B CB  1 
ATOM   1701 C  CG1 . VAL   B 1 121 ? -3.086  -7.716  29.683  1.00 24.19 ? 121 VAL   B CG1 1 
ATOM   1702 C  CG2 . VAL   B 1 121 ? -3.260  -6.009  27.758  1.00 28.09 ? 121 VAL   B CG2 1 
ATOM   1703 N  N   . VAL   B 1 122 ? -6.056  -9.810  28.822  1.00 16.08 ? 122 VAL   B N   1 
ATOM   1704 C  CA  . VAL   B 1 122 ? -7.075  -10.620 29.446  1.00 16.99 ? 122 VAL   B CA  1 
ATOM   1705 C  C   . VAL   B 1 122 ? -6.378  -11.559 30.357  1.00 20.44 ? 122 VAL   B C   1 
ATOM   1706 O  O   . VAL   B 1 122 ? -5.529  -12.344 29.974  1.00 22.70 ? 122 VAL   B O   1 
ATOM   1707 C  CB  . VAL   B 1 122 ? -7.935  -11.394 28.382  1.00 20.14 ? 122 VAL   B CB  1 
ATOM   1708 C  CG1 . VAL   B 1 122 ? -9.039  -12.170 29.059  1.00 26.40 ? 122 VAL   B CG1 1 
ATOM   1709 C  CG2 . VAL   B 1 122 ? -8.517  -10.453 27.289  1.00 22.80 ? 122 VAL   B CG2 1 
ATOM   1710 N  N   . THR   B 1 123 ? -6.729  -11.529 31.610  1.00 27.03 ? 123 THR   B N   1 
ATOM   1711 C  CA  . THR   B 1 123 ? -6.045  -12.347 32.771  1.00 29.32 ? 123 THR   B CA  1 
ATOM   1712 C  C   . THR   B 1 123 ? -7.080  -13.066 33.658  1.00 43.41 ? 123 THR   B C   1 
ATOM   1713 O  O   . THR   B 1 123 ? -8.236  -12.690 33.593  1.00 31.45 ? 123 THR   B O   1 
ATOM   1714 C  CB  . THR   B 1 123 ? -5.184  -11.368 33.702  1.00 42.07 ? 123 THR   B CB  1 
ATOM   1715 O  OG1 . THR   B 1 123 ? -6.005  -10.364 34.299  1.00 47.26 ? 123 THR   B OG1 1 
ATOM   1716 C  CG2 . THR   B 1 123 ? -4.065  -10.563 32.945  0.70 54.33 ? 123 THR   B CG2 1 
HETATM 1717 C  C1  . A1ISU C 2 .   ? -0.003  0.000   24.728  0.40 34.96 ? 201 A1ISU B C1  1 
HETATM 1718 C  C2  . A1ISU C 2 .   ? -1.155  -0.194  24.028  0.40 29.97 ? 201 A1ISU B C2  1 
HETATM 1719 C  C3  . A1ISU C 2 .   ? -1.214  -0.202  22.646  0.40 31.02 ? 201 A1ISU B C3  1 
HETATM 1720 C  C4  . A1ISU C 2 .   ? 0.000   0.002   21.963  0.40 25.51 ? 201 A1ISU B C4  1 
HETATM 1721 C  C5  . A1ISU C 2 .   ? 1.213   0.205   22.648  0.40 31.01 ? 201 A1ISU B C5  1 
HETATM 1722 CL CL1 . A1ISU C 2 .   ? -2.838  -0.554  21.844  0.40 33.85 ? 201 A1ISU B CL1 1 
HETATM 1723 N  N   . A1ISU C 2 .   ? -0.003  0.000   26.080  0.40 30.13 ? 201 A1ISU B N   1 
HETATM 1724 CL CL  . A1ISU C 2 .   ? 2.837   0.557   21.846  0.40 33.80 ? 201 A1ISU B CL  1 
HETATM 1725 C  C   . A1ISU C 2 .   ? 1.150   0.196   24.030  0.40 29.62 ? 201 A1ISU B C   1 
HETATM 1726 O  O   . HOH   D 3 .   ? -13.360 0.349   -2.258  1.00 24.67 ? 201 HOH   A O   1 
HETATM 1727 O  O   . HOH   D 3 .   ? -20.026 -8.308  12.452  1.00 17.85 ? 202 HOH   A O   1 
HETATM 1728 O  O   . HOH   D 3 .   ? -24.060 11.127  7.208   1.00 30.96 ? 203 HOH   A O   1 
HETATM 1729 O  O   . HOH   D 3 .   ? -15.487 -11.482 20.668  1.00 21.18 ? 204 HOH   A O   1 
HETATM 1730 O  O   . HOH   D 3 .   ? -19.808 -7.629  14.703  1.00 32.48 ? 205 HOH   A O   1 
HETATM 1731 O  O   . HOH   D 3 .   ? -11.530 14.403  5.308   1.00 20.44 ? 206 HOH   A O   1 
HETATM 1732 O  O   . HOH   D 3 .   ? -24.310 -4.537  4.414   1.00 24.50 ? 207 HOH   A O   1 
HETATM 1733 O  O   . HOH   D 3 .   ? -11.422 -10.244 15.552  1.00 13.55 ? 208 HOH   A O   1 
HETATM 1734 O  O   . HOH   D 3 .   ? -12.625 12.732  9.193   1.00 18.06 ? 209 HOH   A O   1 
HETATM 1735 O  O   . HOH   D 3 .   ? -11.883 -7.581  -3.809  1.00 36.05 ? 210 HOH   A O   1 
HETATM 1736 O  O   . HOH   D 3 .   ? -13.819 -3.792  17.904  1.00 16.06 ? 211 HOH   A O   1 
HETATM 1737 O  O   . HOH   D 3 .   ? -9.429  -9.411  17.385  1.00 14.35 ? 212 HOH   A O   1 
HETATM 1738 O  O   . HOH   D 3 .   ? -19.694 15.067  11.171  1.00 32.35 ? 213 HOH   A O   1 
HETATM 1739 O  O   . HOH   D 3 .   ? -10.570 -21.347 18.517  1.00 18.67 ? 214 HOH   A O   1 
HETATM 1740 O  O   . HOH   D 3 .   ? -8.831  -15.801 4.598   1.00 32.69 ? 215 HOH   A O   1 
HETATM 1741 O  O   . HOH   D 3 .   ? 4.271   -13.878 4.891   1.00 21.50 ? 216 HOH   A O   1 
HETATM 1742 O  O   . HOH   D 3 .   ? -12.759 -21.798 14.512  1.00 19.02 ? 217 HOH   A O   1 
HETATM 1743 O  O   . HOH   D 3 .   ? -14.421 11.619  -2.807  1.00 27.56 ? 218 HOH   A O   1 
HETATM 1744 O  O   . HOH   D 3 .   ? -20.988 -9.076  16.833  1.00 36.28 ? 219 HOH   A O   1 
HETATM 1745 O  O   . HOH   D 3 .   ? -12.785 16.805  3.019   1.00 27.88 ? 220 HOH   A O   1 
HETATM 1746 O  O   . HOH   D 3 .   ? -14.410 3.258   -3.880  1.00 23.48 ? 221 HOH   A O   1 
HETATM 1747 O  O   . HOH   D 3 .   ? -8.790  4.219   10.092  1.00 18.39 ? 222 HOH   A O   1 
HETATM 1748 O  O   . HOH   D 3 .   ? -15.115 -18.076 9.810   1.00 24.90 ? 223 HOH   A O   1 
HETATM 1749 O  O   . HOH   D 3 .   ? -1.889  -4.071  16.821  1.00 33.07 ? 224 HOH   A O   1 
HETATM 1750 O  O   . HOH   D 3 .   ? -2.306  -5.843  14.962  1.00 18.44 ? 225 HOH   A O   1 
HETATM 1751 O  O   . HOH   D 3 .   ? -14.375 -11.855 7.135   1.00 16.47 ? 226 HOH   A O   1 
HETATM 1752 O  O   . HOH   D 3 .   ? -7.805  -14.961 26.637  1.00 34.32 ? 227 HOH   A O   1 
HETATM 1753 O  O   . HOH   D 3 .   ? -7.995  -19.224 19.844  1.00 20.67 ? 228 HOH   A O   1 
HETATM 1754 O  O   . HOH   D 3 .   ? -10.209 -6.844  14.939  0.90 18.72 ? 229 HOH   A O   1 
HETATM 1755 O  O   . HOH   D 3 .   ? -25.187 8.923   -1.767  1.00 35.48 ? 230 HOH   A O   1 
HETATM 1756 O  O   . HOH   D 3 .   ? -15.687 -13.485 3.829   1.00 26.18 ? 231 HOH   A O   1 
HETATM 1757 O  O   . HOH   D 3 .   ? -3.934  -19.972 12.923  1.00 25.89 ? 232 HOH   A O   1 
HETATM 1758 O  O   . HOH   D 3 .   ? -7.978  -8.571  14.641  1.00 12.92 ? 233 HOH   A O   1 
HETATM 1759 O  O   . HOH   D 3 .   ? -2.674  -15.965 10.689  1.00 25.93 ? 234 HOH   A O   1 
HETATM 1760 O  O   . HOH   D 3 .   ? -9.308  -16.682 7.183   1.00 25.67 ? 235 HOH   A O   1 
HETATM 1761 O  O   . HOH   D 3 .   ? -23.682 -2.053  3.606   1.00 21.89 ? 236 HOH   A O   1 
HETATM 1762 O  O   . HOH   D 3 .   ? -13.688 -15.434 19.648  1.00 28.41 ? 237 HOH   A O   1 
HETATM 1763 O  O   . HOH   D 3 .   ? -12.634 -13.815 6.346   1.00 23.35 ? 238 HOH   A O   1 
HETATM 1764 O  O   . HOH   D 3 .   ? -26.783 14.417  3.284   1.00 20.54 ? 239 HOH   A O   1 
HETATM 1765 O  O   . HOH   D 3 .   ? -5.788  7.936   0.050   1.00 28.62 ? 240 HOH   A O   1 
HETATM 1766 O  O   . HOH   D 3 .   ? -3.194  0.265   10.588  1.00 26.64 ? 241 HOH   A O   1 
HETATM 1767 O  O   . HOH   D 3 .   ? -5.080  -14.128 4.531   1.00 24.49 ? 242 HOH   A O   1 
HETATM 1768 O  O   . HOH   D 3 .   ? -14.124 15.132  6.317   1.00 22.43 ? 243 HOH   A O   1 
HETATM 1769 O  O   . HOH   D 3 .   ? -6.940  -16.727 20.711  1.00 29.06 ? 244 HOH   A O   1 
HETATM 1770 O  O   . HOH   D 3 .   ? -21.380 8.364   14.796  1.00 37.24 ? 245 HOH   A O   1 
HETATM 1771 O  O   . HOH   D 3 .   ? -11.225 -5.236  -4.911  1.00 31.32 ? 246 HOH   A O   1 
HETATM 1772 O  O   . HOH   D 3 .   ? -13.013 -21.616 17.221  1.00 24.48 ? 247 HOH   A O   1 
HETATM 1773 O  O   . HOH   D 3 .   ? -21.401 16.231  -9.017  1.00 39.02 ? 248 HOH   A O   1 
HETATM 1774 O  O   . HOH   D 3 .   ? -11.992 20.365  -2.309  1.00 35.07 ? 249 HOH   A O   1 
HETATM 1775 O  O   . HOH   D 3 .   ? -16.873 -13.301 6.333   1.00 36.13 ? 250 HOH   A O   1 
HETATM 1776 O  O   . HOH   D 3 .   ? -24.526 -2.364  1.060   1.00 33.13 ? 251 HOH   A O   1 
HETATM 1777 O  O   . HOH   D 3 .   ? -10.482 16.710  4.482   1.00 30.41 ? 252 HOH   A O   1 
HETATM 1778 O  O   . HOH   D 3 .   ? -8.951  -19.270 5.978   1.00 35.93 ? 253 HOH   A O   1 
HETATM 1779 O  O   . HOH   D 3 .   ? -4.674  -16.349 24.537  1.00 34.31 ? 254 HOH   A O   1 
HETATM 1780 O  O   . HOH   D 3 .   ? -15.390 -21.886 13.802  1.00 42.24 ? 255 HOH   A O   1 
HETATM 1781 O  O   . HOH   D 3 .   ? -2.744  -17.345 13.338  1.00 26.84 ? 256 HOH   A O   1 
HETATM 1782 O  O   . HOH   D 3 .   ? -4.370  -16.195 19.613  1.00 27.75 ? 257 HOH   A O   1 
HETATM 1783 O  O   . HOH   D 3 .   ? -2.098  -16.507 15.858  1.00 25.07 ? 258 HOH   A O   1 
HETATM 1784 O  O   . HOH   D 3 .   ? -2.805  -17.819 18.070  1.00 28.47 ? 259 HOH   A O   1 
HETATM 1785 O  O   . HOH   E 3 .   ? -13.372 0.353   34.467  1.00 29.81 ? 301 HOH   B O   1 
HETATM 1786 O  O   . HOH   E 3 .   ? -12.411 -13.554 26.843  1.00 28.76 ? 302 HOH   B O   1 
HETATM 1787 O  O   . HOH   E 3 .   ? -0.067  -0.123  18.072  0.50 29.58 ? 303 HOH   B O   1 
HETATM 1788 O  O   . HOH   E 3 .   ? -14.712 12.324  11.791  1.00 18.15 ? 304 HOH   B O   1 
HETATM 1789 O  O   . HOH   E 3 .   ? -10.725 10.911  16.776  1.00 13.32 ? 305 HOH   B O   1 
HETATM 1790 O  O   . HOH   E 3 .   ? -2.024  20.661  21.243  1.00 37.29 ? 306 HOH   B O   1 
HETATM 1791 O  O   . HOH   E 3 .   ? -9.032  -3.802  22.393  1.00 23.77 ? 307 HOH   B O   1 
HETATM 1792 O  O   . HOH   E 3 .   ? -9.392  15.783  10.143  1.00 36.18 ? 308 HOH   B O   1 
HETATM 1793 O  O   . HOH   E 3 .   ? -13.554 4.481   14.480  1.00 17.60 ? 309 HOH   B O   1 
HETATM 1794 O  O   . HOH   E 3 .   ? -2.168  3.498   15.682  1.00 27.63 ? 310 HOH   B O   1 
HETATM 1795 O  O   . HOH   E 3 .   ? -13.555 -11.829 23.281  1.00 24.65 ? 311 HOH   B O   1 
HETATM 1796 O  O   . HOH   E 3 .   ? -20.414 10.547  15.665  1.00 34.99 ? 312 HOH   B O   1 
HETATM 1797 O  O   . HOH   E 3 .   ? -2.248  -7.413  24.535  0.80 21.81 ? 313 HOH   B O   1 
HETATM 1798 O  O   . HOH   E 3 .   ? -13.612 18.655  23.110  1.00 26.35 ? 314 HOH   B O   1 
HETATM 1799 O  O   . HOH   E 3 .   ? -6.203  5.990   37.594  1.00 33.45 ? 315 HOH   B O   1 
HETATM 1800 O  O   . HOH   E 3 .   ? -11.252 7.944   36.173  1.00 29.96 ? 316 HOH   B O   1 
HETATM 1801 O  O   . HOH   E 3 .   ? -4.205  16.145  12.259  1.00 22.87 ? 317 HOH   B O   1 
HETATM 1802 O  O   . HOH   E 3 .   ? -9.699  19.602  16.432  1.00 16.72 ? 318 HOH   B O   1 
HETATM 1803 O  O   . HOH   E 3 .   ? -8.778  9.711   15.211  1.00 15.90 ? 319 HOH   B O   1 
HETATM 1804 O  O   . HOH   E 3 .   ? -13.295 12.451  25.245  1.00 17.47 ? 320 HOH   B O   1 
HETATM 1805 O  O   . HOH   E 3 .   ? -14.751 -2.549  36.151  1.00 26.57 ? 321 HOH   B O   1 
HETATM 1806 O  O   . HOH   E 3 .   ? -7.359  8.767   17.847  1.00 13.05 ? 322 HOH   B O   1 
HETATM 1807 O  O   . HOH   E 3 .   ? -20.852 -13.719 20.980  1.00 32.22 ? 323 HOH   B O   1 
HETATM 1808 O  O   . HOH   E 3 .   ? -1.364  5.591   17.474  1.00 25.63 ? 324 HOH   B O   1 
HETATM 1809 O  O   . HOH   E 3 .   ? -3.875  14.002  27.953  1.00 21.57 ? 325 HOH   B O   1 
HETATM 1810 O  O   . HOH   E 3 .   ? -5.078  -13.820 27.560  1.00 25.83 ? 326 HOH   B O   1 
HETATM 1811 O  O   . HOH   E 3 .   ? -6.203  -7.738  32.445  1.00 29.41 ? 327 HOH   B O   1 
HETATM 1812 O  O   . HOH   E 3 .   ? -4.578  19.931  13.315  1.00 28.93 ? 328 HOH   B O   1 
HETATM 1813 O  O   . HOH   E 3 .   ? -11.671 14.499  25.993  1.00 28.52 ? 329 HOH   B O   1 
HETATM 1814 O  O   . HOH   E 3 .   ? -10.748 5.446   37.247  1.00 32.06 ? 330 HOH   B O   1 
HETATM 1815 O  O   . HOH   E 3 .   ? -14.957 8.800   35.588  1.00 27.44 ? 331 HOH   B O   1 
HETATM 1816 O  O   . HOH   E 3 .   ? -6.906  15.081  5.766   1.00 32.01 ? 332 HOH   B O   1 
HETATM 1817 O  O   . HOH   E 3 .   ? -17.641 7.783   24.250  1.00 30.97 ? 333 HOH   B O   1 
HETATM 1818 O  O   . HOH   E 3 .   ? -21.858 -6.848  17.608  1.00 32.24 ? 334 HOH   B O   1 
HETATM 1819 O  O   . HOH   E 3 .   ? -7.023  11.697  38.081  1.00 31.51 ? 335 HOH   B O   1 
HETATM 1820 O  O   . HOH   E 3 .   ? -8.060  16.723  25.489  1.00 35.65 ? 336 HOH   B O   1 
HETATM 1821 O  O   . HOH   E 3 .   ? -10.376 13.354  7.461   1.00 24.27 ? 337 HOH   B O   1 
HETATM 1822 O  O   . HOH   E 3 .   ? -9.392  23.484  21.986  1.00 29.18 ? 338 HOH   B O   1 
HETATM 1823 O  O   . HOH   E 3 .   ? -0.269  -1.983  16.261  1.00 31.45 ? 339 HOH   B O   1 
HETATM 1824 O  O   . HOH   E 3 .   ? -5.145  17.173  9.568   1.00 70.03 ? 340 HOH   B O   1 
HETATM 1825 O  O   . HOH   E 3 .   ? -23.533 1.008   37.142  1.00 23.27 ? 341 HOH   B O   1 
HETATM 1826 O  O   . HOH   E 3 .   ? -13.446 17.573  14.229  1.00 33.26 ? 342 HOH   B O   1 
HETATM 1827 O  O   . HOH   E 3 .   ? -11.582 19.509  14.473  1.00 19.57 ? 343 HOH   B O   1 
HETATM 1828 O  O   . HOH   E 3 .   ? -27.613 7.703   38.956  1.00 25.69 ? 344 HOH   B O   1 
HETATM 1829 O  O   . HOH   E 3 .   ? -31.282 5.964   37.229  1.00 38.72 ? 345 HOH   B O   1 
HETATM 1830 O  O   . HOH   E 3 .   ? -31.319 9.287   40.138  1.00 29.41 ? 346 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  C   . CYS   A 10  ? 0.3418 0.4479 0.6835 -0.0782 0.0587  0.1101  10  CYS   A C   
2    O  O   . CYS   A 10  ? 0.2922 0.4835 0.9042 -0.0233 0.0050  0.1547  10  CYS   A O   
3    N  N   . PRO   A 11  ? 0.3456 0.2612 0.2964 -0.0305 -0.0853 0.0468  11  PRO   A N   
4    C  CA  . PRO   A 11  ? 0.2277 0.2102 0.3271 -0.0793 -0.1262 0.0347  11  PRO   A CA  
5    C  C   . PRO   A 11  ? 0.2270 0.1908 0.2523 0.0260  -0.1019 0.0156  11  PRO   A C   
6    O  O   . PRO   A 11  ? 0.2172 0.1952 0.2512 -0.0037 -0.0809 0.0257  11  PRO   A O   
7    C  CB  . PRO   A 11  ? 0.4434 0.3192 0.3427 0.1100  -0.0688 0.1024  11  PRO   A CB  
8    C  CG  . PRO   A 11  ? 0.4222 0.4375 0.4573 0.0189  -0.1065 0.0100  11  PRO   A CG  
9    C  CD  . PRO   A 11  ? 0.3897 0.3660 0.2799 -0.0588 -0.1438 0.0156  11  PRO   A CD  
10   N  N   . LEU   A 12  ? 0.2316 0.1729 0.2667 0.0149  -0.0987 0.0024  12  LEU   A N   
11   C  CA  . LEU   A 12  ? 0.2157 0.1483 0.2828 -0.0106 -0.0790 0.0221  12  LEU   A CA  
12   C  C   . LEU   A 12  ? 0.2442 0.1558 0.2467 0.0149  -0.0842 0.0133  12  LEU   A C   
13   O  O   . LEU   A 12  ? 0.3339 0.1852 0.3652 0.0385  -0.1862 -0.0531 12  LEU   A O   
14   C  CB  . LEU   A 12  ? 0.2120 0.1903 0.2661 -0.0267 -0.0615 0.0082  12  LEU   A CB  
15   C  CG  . LEU   A 12  ? 0.2221 0.2062 0.2866 -0.0303 -0.0727 0.0061  12  LEU   A CG  
16   C  CD1 . LEU   A 12  ? 0.2261 0.2227 0.2764 -0.0107 -0.0474 -0.0140 12  LEU   A CD1 
17   C  CD2 . LEU   A 12  ? 0.2008 0.2425 0.4370 -0.0363 -0.0447 0.0116  12  LEU   A CD2 
18   N  N   . MET   A 13  ? 0.2138 0.1415 0.2138 0.0060  -0.0538 0.0178  13  MET   A N   
19   C  CA  . MET   A 13  ? 0.2291 0.1311 0.2198 0.0270  -0.0397 0.0120  13  MET   A CA  
20   C  C   . MET   A 13  ? 0.1818 0.1210 0.2229 -0.0028 -0.0354 -0.0076 13  MET   A C   
21   O  O   . MET   A 13  ? 0.2017 0.1125 0.2283 -0.0125 -0.0542 0.0057  13  MET   A O   
22   C  CB  . MET   A 13  ? 0.2809 0.2261 0.2308 0.0873  -0.0014 0.0636  13  MET   A CB  
23   C  CG  . MET   A 13  ? 0.2580 0.3158 0.3231 0.0071  0.0533  0.0186  13  MET   A CG  
24   S  SD  . MET   A 13  ? 0.2084 0.2224 0.2952 0.0275  0.0013  0.0256  13  MET   A SD  
25   C  CE  . MET   A 13  ? 0.2169 0.2835 0.3571 -0.0015 0.0897  0.0118  13  MET   A CE  
26   N  N   . VAL   A 14  ? 0.1847 0.1263 0.2091 0.0243  -0.0337 -0.0042 14  VAL   A N   
27   C  CA  . VAL   A 14  ? 0.1718 0.1318 0.2058 0.0153  -0.0245 -0.0179 14  VAL   A CA  
28   C  C   . VAL   A 14  ? 0.1921 0.1297 0.1982 0.0355  -0.0175 0.0001  14  VAL   A C   
29   O  O   . VAL   A 14  ? 0.2494 0.1692 0.2330 0.0759  -0.0852 -0.0519 14  VAL   A O   
30   C  CB  . VAL   A 14  ? 0.1963 0.1283 0.2292 -0.0156 -0.0270 -0.0083 14  VAL   A CB  
31   C  CG1 . VAL   A 14  ? 0.2327 0.1914 0.2388 -0.0241 -0.0556 0.0568  14  VAL   A CG1 
32   C  CG2 . VAL   A 14  ? 0.1545 0.1816 0.2546 -0.0081 -0.0079 -0.0102 14  VAL   A CG2 
33   N  N   . LYS   A 15  ? 0.1813 0.1138 0.1856 0.0303  -0.0241 0.0090  15  LYS   A N   
34   C  CA  . LYS   A 15  ? 0.1924 0.1446 0.1883 0.0440  -0.0123 -0.0154 15  LYS   A CA  
35   C  C   . LYS   A 15  ? 0.1774 0.1125 0.1880 0.0168  -0.0165 -0.0010 15  LYS   A C   
36   O  O   . LYS   A 15  ? 0.2453 0.1194 0.1975 0.0416  -0.0553 -0.0132 15  LYS   A O   
37   C  CB  . LYS   A 15  ? 0.2073 0.2018 0.2304 0.0279  0.0120  0.0563  15  LYS   A CB  
38   C  CG  . LYS   A 15  ? 0.1308 0.2917 0.2906 0.0413  -0.0089 0.0296  15  LYS   A CG  
39   C  CD  . LYS   A 15  ? 0.2186 0.4410 0.4342 0.0492  0.0846  0.0593  15  LYS   A CD  
40   C  CE  . LYS   A 15  ? 0.1763 0.4096 0.4946 0.0302  0.1194  0.0440  15  LYS   A CE  
41   N  NZ  . LYS   A 15  ? 0.3796 0.4303 0.5701 0.0634  0.1913  0.0757  15  LYS   A NZ  
42   N  N   . VAL   A 16  ? 0.1531 0.1187 0.1888 0.0189  -0.0075 0.0037  16  VAL   A N   
43   C  CA  . VAL   A 16  ? 0.1313 0.1213 0.1886 0.0267  -0.0055 -0.0186 16  VAL   A CA  
44   C  C   . VAL   A 16  ? 0.1428 0.1206 0.1650 0.0299  -0.0087 -0.0013 16  VAL   A C   
45   O  O   . VAL   A 16  ? 0.1550 0.1496 0.1829 0.0357  -0.0192 -0.0153 16  VAL   A O   
46   C  CB  . VAL   A 16  ? 0.1405 0.1384 0.2118 0.0353  -0.0167 -0.0174 16  VAL   A CB  
47   C  CG1 . VAL   A 16  ? 0.1543 0.1618 0.2091 0.0342  0.0066  0.0100  16  VAL   A CG1 
48   C  CG2 . VAL   A 16  ? 0.1355 0.1745 0.2282 0.0415  -0.0160 0.0054  16  VAL   A CG2 
49   N  N   . LEU   A 17  ? 0.1302 0.1340 0.1752 0.0329  -0.0084 -0.0121 17  LEU   A N   
50   C  CA  . LEU   A 17  ? 0.1126 0.1316 0.1871 0.0234  -0.0079 -0.0174 17  LEU   A CA  
51   C  C   . LEU   A 17  ? 0.1133 0.1237 0.1885 0.0309  0.0004  -0.0156 17  LEU   A C   
52   O  O   . LEU   A 17  ? 0.1369 0.1304 0.2024 0.0263  0.0272  -0.0088 17  LEU   A O   
53   C  CB  . LEU   A 17  ? 0.1188 0.1674 0.2390 0.0200  -0.0120 -0.0064 17  LEU   A CB  
54   C  CG  . LEU   A 17  ? 0.1836 0.1978 0.2334 0.0071  0.0180  0.0249  17  LEU   A CG  
55   C  CD1 . LEU   A 17  ? 0.1926 0.1952 0.3444 -0.0282 0.0400  -0.0090 17  LEU   A CD1 
56   C  CD2 . LEU   A 17  ? 0.3101 0.2309 0.2415 -0.0295 0.0377  0.0174  17  LEU   A CD2 
57   N  N   . ASP   A 18  ? 0.1222 0.1543 0.1939 0.0317  0.0096  -0.0052 18  ASP   A N   
58   C  CA  . ASP   A 18  ? 0.1206 0.1308 0.2033 0.0245  0.0007  -0.0089 18  ASP   A CA  
59   C  C   . ASP   A 18  ? 0.1123 0.1325 0.2106 0.0156  0.0142  -0.0123 18  ASP   A C   
60   O  O   . ASP   A 18  ? 0.1118 0.1510 0.2048 0.0313  0.0104  -0.0005 18  ASP   A O   
61   C  CB  . ASP   A 18  ? 0.1161 0.1313 0.2253 0.0201  -0.0231 -0.0120 18  ASP   A CB  
62   C  CG  . ASP   A 18  ? 0.1403 0.1090 0.2457 0.0136  -0.0247 -0.0113 18  ASP   A CG  
63   O  OD1 . ASP   A 18  ? 0.1631 0.1259 0.2627 0.0026  -0.0322 0.0079  18  ASP   A OD1 
64   O  OD2 . ASP   A 18  ? 0.1686 0.1356 0.3316 0.0061  -0.0460 -0.0072 18  ASP   A OD2 
65   N  N   . ALA   A 19  ? 0.0991 0.1241 0.1979 0.0266  0.0200  -0.0100 19  ALA   A N   
66   C  CA  . ALA   A 19  ? 0.1031 0.1318 0.2020 -0.0103 0.0097  -0.0007 19  ALA   A CA  
67   C  C   . ALA   A 19  ? 0.0817 0.1208 0.1918 0.0160  0.0135  0.0060  19  ALA   A C   
68   O  O   . ALA   A 19  ? 0.0963 0.1581 0.2446 0.0121  0.0072  -0.0016 19  ALA   A O   
69   C  CB  . ALA   A 19  ? 0.1659 0.1181 0.2109 0.0076  0.0011  -0.0151 19  ALA   A CB  
70   N  N   . VAL   A 20  ? 0.1010 0.1286 0.2180 0.0215  0.0121  0.0011  20  VAL   A N   
71   C  CA  . VAL   A 20  ? 0.1292 0.1325 0.2202 0.0188  -0.0036 0.0053  20  VAL   A CA  
72   C  C   . VAL   A 20  ? 0.1381 0.1401 0.2372 0.0288  0.0014  0.0162  20  VAL   A C   
73   O  O   . VAL   A 20  ? 0.1527 0.1856 0.2496 0.0612  0.0141  -0.0097 20  VAL   A O   
74   C  CB  . VAL   A 20  ? 0.1307 0.1427 0.2388 0.0123  -0.0069 0.0246  20  VAL   A CB  
75   C  CG1 . VAL   A 20  ? 0.1982 0.1387 0.2943 0.0250  -0.0001 0.0420  20  VAL   A CG1 
76   C  CG2 . VAL   A 20  ? 0.1650 0.1807 0.2397 0.0018  0.0495  -0.0051 20  VAL   A CG2 
77   N  N   . ARG   A 21  ? 0.1547 0.1553 0.2104 0.0402  0.0274  -0.0060 21  ARG   A N   
78   C  CA  . ARG   A 21  ? 0.2073 0.1547 0.2396 0.0372  0.0216  -0.0053 21  ARG   A CA  
79   C  C   . ARG   A 21  ? 0.1485 0.1705 0.2045 0.0231  0.0187  -0.0075 21  ARG   A C   
80   O  O   . ARG   A 21  ? 0.1808 0.1971 0.2528 0.0509  0.0420  -0.0184 21  ARG   A O   
81   C  CB  . ARG   A 21  ? 0.3126 0.1948 0.2651 -0.0608 0.0590  -0.0516 21  ARG   A CB  
82   N  N   . GLY   A 22  ? 0.1265 0.1370 0.2407 0.0151  -0.0040 0.0026  22  GLY   A N   
83   C  CA  . GLY   A 22  ? 0.1186 0.1756 0.2328 -0.0040 0.0076  -0.0206 22  GLY   A CA  
84   C  C   . GLY   A 22  ? 0.1053 0.1550 0.2094 -0.0024 0.0161  -0.0238 22  GLY   A C   
85   O  O   . GLY   A 22  ? 0.1167 0.2003 0.2308 -0.0151 0.0245  -0.0207 22  GLY   A O   
86   N  N   . SER   A 23  ? 0.1084 0.1728 0.2252 0.0132  0.0085  -0.0269 23  SER   A N   
87   C  CA  . SER   A 23  ? 0.1149 0.1617 0.2277 0.0108  0.0102  -0.0053 23  SER   A CA  
88   C  C   . SER   A 23  ? 0.1330 0.1516 0.2164 0.0172  0.0141  -0.0067 23  SER   A C   
89   O  O   . SER   A 23  ? 0.1546 0.2076 0.2003 0.0518  0.0165  -0.0352 23  SER   A O   
90   C  CB  . SER   A 23  ? 0.1807 0.1763 0.2543 0.0332  -0.0173 -0.0052 23  SER   A CB  
91   O  OG  . SER   A 23  ? 0.2210 0.2040 0.3507 -0.0407 0.0085  -0.0171 23  SER   A OG  
92   N  N   . PRO   A 24  ? 0.1477 0.1786 0.1875 0.0289  0.0043  -0.0201 24  PRO   A N   
93   C  CA  . PRO   A 24  ? 0.1572 0.1792 0.2284 0.0549  -0.0025 -0.0027 24  PRO   A CA  
94   C  C   . PRO   A 24  ? 0.1677 0.1456 0.2318 0.0211  0.0026  -0.0238 24  PRO   A C   
95   O  O   . PRO   A 24  ? 0.1591 0.1415 0.3138 0.0279  0.0163  -0.0067 24  PRO   A O   
96   C  CB  . PRO   A 24  ? 0.1916 0.2244 0.2478 0.0561  -0.0177 0.0165  24  PRO   A CB  
97   C  CG  . PRO   A 24  ? 0.2589 0.5407 0.2132 0.1409  -0.0069 -0.0561 24  PRO   A CG  
98   C  CD  . PRO   A 24  ? 0.1684 0.2037 0.2247 0.0309  -0.0071 -0.0067 24  PRO   A CD  
99   N  N   . ALA   A 25  ? 0.1533 0.1318 0.2244 0.0300  -0.0023 -0.0153 25  ALA   A N   
100  C  CA  . ALA   A 25  ? 0.1322 0.1412 0.2307 0.0262  -0.0125 0.0142  25  ALA   A CA  
101  C  C   . ALA   A 25  ? 0.1375 0.1253 0.2507 0.0394  -0.0082 -0.0111 25  ALA   A C   
102  O  O   . ALA   A 25  ? 0.1473 0.1319 0.2664 0.0248  -0.0308 -0.0050 25  ALA   A O   
103  C  CB  . ALA   A 25  ? 0.1395 0.1591 0.2337 0.0207  -0.0053 -0.0128 25  ALA   A CB  
104  N  N   . ILE   A 26  ? 0.1586 0.1365 0.2607 0.0361  -0.0187 -0.0217 26  ILE   A N   
105  C  CA  A ILE   A 26  ? 0.1760 0.1204 0.2517 0.0208  0.0000  -0.0035 26  ILE   A CA  
106  C  CA  B ILE   A 26  ? 0.1591 0.1621 0.2609 0.0275  -0.0101 -0.0257 26  ILE   A CA  
107  C  C   . ILE   A 26  ? 0.1953 0.1532 0.2901 0.0206  -0.0176 -0.0206 26  ILE   A C   
108  O  O   . ILE   A 26  ? 0.1881 0.1665 0.3029 0.0378  -0.0189 -0.0186 26  ILE   A O   
109  C  CB  A ILE   A 26  ? 0.2238 0.1241 0.3291 0.0177  0.0012  -0.0416 26  ILE   A CB  
110  C  CB  B ILE   A 26  ? 0.1763 0.2345 0.2991 0.0613  -0.0135 -0.0301 26  ILE   A CB  
111  C  CG1 A ILE   A 26  ? 0.2399 0.1945 0.3216 0.0189  0.0046  0.0057  26  ILE   A CG1 
112  C  CG1 B ILE   A 26  ? 0.2073 0.1896 0.3718 0.0344  0.0272  -0.0783 26  ILE   A CG1 
113  C  CG2 A ILE   A 26  ? 0.3100 0.1952 0.2785 -0.0629 0.0524  -0.0873 26  ILE   A CG2 
114  C  CG2 B ILE   A 26  ? 0.1714 0.2764 0.2642 0.0712  -0.0085 -0.1022 26  ILE   A CG2 
115  C  CD1 A ILE   A 26  ? 0.2165 0.3654 0.3449 0.1221  0.0095  0.0119  26  ILE   A CD1 
116  C  CD1 B ILE   A 26  ? 0.3529 0.2432 0.4941 0.0693  0.0101  -0.1632 26  ILE   A CD1 
117  N  N   . ASN   A 27  ? 0.1806 0.1514 0.2850 0.0321  -0.0167 -0.0445 27  ASN   A N   
118  C  CA  A ASN   A 27  ? 0.1757 0.1914 0.3021 0.0090  -0.0237 -0.0285 27  ASN   A CA  
119  C  CA  B ASN   A 27  ? 0.1685 0.1537 0.3391 0.0244  -0.0247 -0.0665 27  ASN   A CA  
120  C  C   . ASN   A 27  ? 0.1565 0.1372 0.2679 0.0059  -0.0341 -0.0264 27  ASN   A C   
121  O  O   . ASN   A 27  ? 0.2016 0.1503 0.3229 -0.0205 0.0011  -0.0224 27  ASN   A O   
122  C  CB  A ASN   A 27  ? 0.2032 0.1970 0.3238 0.0073  0.0185  -0.0633 27  ASN   A CB  
123  C  CB  B ASN   A 27  ? 0.2467 0.1589 0.4050 -0.0172 -0.0694 -0.1172 27  ASN   A CB  
124  C  CG  A ASN   A 27  ? 0.2470 0.1335 0.3786 0.0558  -0.0404 -0.0450 27  ASN   A CG  
125  C  CG  B ASN   A 27  ? 0.2828 0.3745 0.3547 0.0190  -0.1098 -0.0941 27  ASN   A CG  
126  O  OD1 A ASN   A 27  ? 0.2953 0.2100 0.4822 -0.0272 -0.1231 0.0121  27  ASN   A OD1 
127  O  OD1 B ASN   A 27  ? 0.4588 0.2937 0.3499 -0.0141 -0.0983 -0.1457 27  ASN   A OD1 
128  N  ND2 A ASN   A 27  ? 0.2935 0.1353 0.6906 0.0443  -0.0583 0.0064  27  ASN   A ND2 
129  N  ND2 B ASN   A 27  ? 0.2811 0.2858 0.5337 -0.0172 -0.0449 -0.0354 27  ASN   A ND2 
130  N  N   . VAL   A 28  ? 0.1672 0.1442 0.2663 0.0210  -0.0383 -0.0280 28  VAL   A N   
131  C  CA  . VAL   A 28  ? 0.1788 0.1039 0.2399 0.0157  -0.0393 -0.0005 28  VAL   A CA  
132  C  C   . VAL   A 28  ? 0.1536 0.1169 0.2253 0.0054  -0.0222 -0.0020 28  VAL   A C   
133  O  O   . VAL   A 28  ? 0.1532 0.1505 0.2334 0.0045  -0.0319 0.0000  28  VAL   A O   
134  C  CB  . VAL   A 28  ? 0.1730 0.1427 0.2097 0.0157  -0.0359 -0.0013 28  VAL   A CB  
135  C  CG1 . VAL   A 28  ? 0.1707 0.1687 0.2388 0.0059  -0.0429 -0.0361 28  VAL   A CG1 
136  C  CG2 . VAL   A 28  ? 0.1439 0.1934 0.2629 0.0476  -0.0428 0.0102  28  VAL   A CG2 
137  N  N   . ALA   A 29  ? 0.1688 0.1140 0.2467 0.0193  -0.0336 -0.0139 29  ALA   A N   
138  C  CA  . ALA   A 29  ? 0.1542 0.1051 0.2427 0.0119  -0.0371 -0.0049 29  ALA   A CA  
139  C  C   . ALA   A 29  ? 0.1355 0.1334 0.2265 0.0084  -0.0414 -0.0032 29  ALA   A C   
140  O  O   . ALA   A 29  ? 0.1615 0.1379 0.2321 0.0119  -0.0493 -0.0136 29  ALA   A O   
141  C  CB  . ALA   A 29  ? 0.1572 0.1212 0.3047 -0.0121 -0.0323 -0.0098 29  ALA   A CB  
142  N  N   . VAL   A 30  ? 0.1226 0.1313 0.2297 0.0101  -0.0396 -0.0135 30  VAL   A N   
143  C  CA  . VAL   A 30  ? 0.1344 0.1087 0.2139 0.0045  -0.0351 0.0049  30  VAL   A CA  
144  C  C   . VAL   A 30  ? 0.1260 0.1361 0.2199 0.0019  -0.0276 -0.0125 30  VAL   A C   
145  O  O   . VAL   A 30  ? 0.1558 0.1455 0.2274 0.0077  -0.0591 -0.0298 30  VAL   A O   
146  C  CB  . VAL   A 30  ? 0.1438 0.1273 0.2448 -0.0019 -0.0334 0.0018  30  VAL   A CB  
147  C  CG1 . VAL   A 30  ? 0.1851 0.1126 0.2986 -0.0343 -0.0330 -0.0073 30  VAL   A CG1 
148  C  CG2 . VAL   A 30  ? 0.1513 0.1790 0.2454 0.0089  -0.0205 -0.0133 30  VAL   A CG2 
149  N  N   . HIS   A 31  ? 0.1206 0.1409 0.2323 0.0095  -0.0377 -0.0254 31  HIS   A N   
150  C  CA  . HIS   A 31  ? 0.1178 0.1225 0.2530 -0.0068 -0.0405 -0.0197 31  HIS   A CA  
151  C  C   . HIS   A 31  ? 0.1239 0.1408 0.2570 0.0000  -0.0402 -0.0267 31  HIS   A C   
152  O  O   . HIS   A 31  ? 0.1985 0.1339 0.2788 0.0228  -0.0809 -0.0354 31  HIS   A O   
153  C  CB  . HIS   A 31  ? 0.1463 0.1600 0.2956 0.0188  -0.0167 -0.0389 31  HIS   A CB  
154  C  CG  . HIS   A 31  ? 0.1523 0.1930 0.3151 0.0050  -0.0179 -0.0592 31  HIS   A CG  
155  N  ND1 . HIS   A 31  ? 0.1924 0.2234 0.3734 -0.0412 -0.0433 -0.0269 31  HIS   A ND1 
156  C  CD2 . HIS   A 31  ? 0.1850 0.1612 0.3526 -0.0345 -0.0123 -0.0074 31  HIS   A CD2 
157  C  CE1 . HIS   A 31  ? 0.2043 0.1961 0.5014 -0.0330 -0.0389 -0.0439 31  HIS   A CE1 
158  N  NE2 . HIS   A 31  ? 0.2227 0.1672 0.3983 -0.0541 -0.0025 -0.0529 31  HIS   A NE2 
159  N  N   . VAL   A 32  ? 0.1216 0.1312 0.2433 0.0032  -0.0556 -0.0236 32  VAL   A N   
160  C  CA  . VAL   A 32  ? 0.1133 0.1212 0.2429 -0.0057 -0.0485 -0.0233 32  VAL   A CA  
161  C  C   . VAL   A 32  ? 0.1090 0.1385 0.2722 -0.0189 -0.0601 -0.0245 32  VAL   A C   
162  O  O   . VAL   A 32  ? 0.1288 0.1323 0.2715 0.0005  -0.0528 -0.0358 32  VAL   A O   
163  C  CB  . VAL   A 32  ? 0.1406 0.1520 0.2304 0.0009  -0.0333 -0.0247 32  VAL   A CB  
164  C  CG1 . VAL   A 32  ? 0.1596 0.1453 0.2844 -0.0161 -0.0422 -0.0133 32  VAL   A CG1 
165  C  CG2 . VAL   A 32  ? 0.1698 0.1550 0.2679 0.0180  -0.0209 -0.0240 32  VAL   A CG2 
166  N  N   . PHE   A 33  ? 0.1168 0.1433 0.2689 -0.0081 -0.0460 -0.0496 33  PHE   A N   
167  C  CA  . PHE   A 33  ? 0.0885 0.1511 0.3088 -0.0059 -0.0256 -0.0217 33  PHE   A CA  
168  C  C   . PHE   A 33  ? 0.0985 0.1541 0.2976 -0.0027 -0.0499 -0.0377 33  PHE   A C   
169  O  O   . PHE   A 33  ? 0.1261 0.1128 0.3312 0.0027  -0.0561 -0.0321 33  PHE   A O   
170  C  CB  . PHE   A 33  ? 0.1357 0.1606 0.3192 -0.0162 -0.0171 -0.0372 33  PHE   A CB  
171  C  CG  . PHE   A 33  ? 0.1704 0.1823 0.3287 -0.0065 0.0246  -0.0457 33  PHE   A CG  
172  C  CD1 . PHE   A 33  ? 0.1884 0.1685 0.3333 -0.0054 0.0071  -0.0443 33  PHE   A CD1 
173  C  CD2 . PHE   A 33  ? 0.1732 0.1800 0.4477 -0.0260 0.0119  -0.0507 33  PHE   A CD2 
174  C  CE1 . PHE   A 33  ? 0.2355 0.1971 0.3864 -0.0050 0.0383  -0.0288 33  PHE   A CE1 
175  C  CE2 . PHE   A 33  ? 0.2240 0.1787 0.5031 -0.0391 0.0620  -0.0520 33  PHE   A CE2 
176  C  CZ  . PHE   A 33  ? 0.2265 0.1888 0.4364 -0.0063 0.0812  -0.0488 33  PHE   A CZ  
177  N  N   . ARG   A 34  ? 0.0994 0.1734 0.3744 0.0165  -0.0539 -0.0571 34  ARG   A N   
178  C  CA  . ARG   A 34  ? 0.1361 0.1301 0.3893 0.0202  -0.0582 -0.0846 34  ARG   A CA  
179  C  C   . ARG   A 34  ? 0.1391 0.1872 0.4233 0.0139  -0.0449 -0.1116 34  ARG   A C   
180  O  O   . ARG   A 34  ? 0.1287 0.2589 0.5566 0.0000  -0.0399 -0.1785 34  ARG   A O   
181  C  CB  . ARG   A 34  ? 0.2088 0.1631 0.4091 0.0602  -0.0981 -0.0864 34  ARG   A CB  
182  C  CG  . ARG   A 34  ? 0.2361 0.2050 0.4251 0.0055  -0.0897 -0.0346 34  ARG   A CG  
183  C  CD  . ARG   A 34  ? 0.0912 0.1600 0.3815 0.0026  -0.0264 -0.0599 34  ARG   A CD  
184  N  NE  . ARG   A 34  ? 0.1595 0.1812 0.3235 0.0620  -0.0373 0.0099  34  ARG   A NE  
185  C  CZ  . ARG   A 34  ? 0.1431 0.1584 0.3480 0.0064  -0.0455 -0.0137 34  ARG   A CZ  
186  N  NH1 . ARG   A 34  ? 0.1411 0.1380 0.3644 -0.0035 -0.0326 0.0253  34  ARG   A NH1 
187  N  NH2 . ARG   A 34  ? 0.1974 0.1116 0.2799 0.0010  -0.0441 0.0094  34  ARG   A NH2 
188  N  N   . LYS   A 35  ? 0.1263 0.2105 0.4421 -0.0070 -0.0157 -0.1431 35  LYS   A N   
189  C  CA  . LYS   A 35  ? 0.1812 0.2755 0.4972 -0.0080 0.0451  -0.1777 35  LYS   A CA  
190  C  C   . LYS   A 35  ? 0.1162 0.2523 0.5112 0.0181  0.0245  -0.1594 35  LYS   A C   
191  O  O   . LYS   A 35  ? 0.1723 0.3455 0.5437 0.0168  -0.0556 -0.0870 35  LYS   A O   
192  C  CB  . LYS   A 35  ? 0.2026 0.2648 0.5407 -0.0637 0.0525  -0.1818 35  LYS   A CB  
193  C  CG  . LYS   A 35  ? 0.2509 0.4362 0.5658 -0.0596 0.0689  -0.2138 35  LYS   A CG  
194  C  CD  . LYS   A 35  ? 0.3782 0.2349 0.3327 -0.0675 0.0607  -0.0485 35  LYS   A CD  
195  C  CE  . LYS   A 35  ? 0.3121 0.2914 0.5050 0.0719  0.1235  -0.0017 35  LYS   A CE  
196  N  NZ  . LYS   A 35  ? 0.3668 0.5090 0.5607 0.2331  0.1280  -0.0528 35  LYS   A NZ  
197  N  N   . ALA   A 36  ? 0.1766 0.3367 0.4706 0.0224  -0.0129 -0.0604 36  ALA   A N   
198  C  CA  . ALA   A 36  ? 0.1819 0.3311 0.5139 -0.0184 -0.0464 0.0373  36  ALA   A CA  
199  C  C   . ALA   A 36  ? 0.2827 0.3650 0.4066 0.0758  0.0160  0.0597  36  ALA   A C   
200  O  O   . ALA   A 36  ? 0.3243 0.3660 0.3687 0.0925  -0.0262 -0.0166 36  ALA   A O   
201  N  N   . ALA   A 37  ? 0.3810 0.5197 0.5241 0.2533  0.0348  0.0559  37  ALA   A N   
202  C  CA  . ALA   A 37  ? 0.4917 0.4075 0.6528 0.2503  0.0611  0.1193  37  ALA   A CA  
203  C  C   . ALA   A 37  ? 0.3338 0.5894 0.4954 0.1673  0.0584  0.0075  37  ALA   A C   
204  O  O   . ALA   A 37  ? 0.6538 0.3993 0.6480 0.1765  0.0764  0.0005  37  ALA   A O   
205  N  N   . ASP   A 38  ? 0.2564 0.6212 0.5024 0.0955  0.1467  0.0528  38  ASP   A N   
206  C  CA  . ASP   A 38  ? 0.3410 0.5982 0.4681 0.1083  0.1131  0.0771  38  ASP   A CA  
207  C  C   . ASP   A 38  ? 0.2307 0.3687 0.4270 0.1285  0.0613  -0.0229 38  ASP   A C   
208  O  O   . ASP   A 38  ? 0.3901 0.5596 0.4622 0.0568  0.1009  0.0075  38  ASP   A O   
209  C  CB  . ASP   A 38  ? 0.1973 0.7508 0.6953 0.0754  -0.0278 0.1633  38  ASP   A CB  
210  N  N   . ASP   A 39  ? 0.2494 0.4741 0.6638 0.1161  0.0562  -0.1198 39  ASP   A N   
211  C  CA  . ASP   A 39  ? 0.3242 0.4303 1.0241 0.1342  -0.2412 -0.0916 39  ASP   A CA  
212  C  C   . ASP   A 39  ? 0.3998 0.4208 0.7884 -0.1077 0.1300  0.0314  39  ASP   A C   
213  N  N   . THR   A 40  ? 0.2118 0.3207 0.5453 0.0270  0.1151  0.0487  40  THR   A N   
214  C  CA  . THR   A 40  ? 0.2059 0.2905 0.4946 -0.0496 0.0978  0.0394  40  THR   A CA  
215  C  C   . THR   A 40  ? 0.2853 0.6679 0.4746 -0.1612 0.2390  -0.0600 40  THR   A C   
216  O  O   . THR   A 40  ? 0.2174 0.2718 0.6198 -0.0218 0.1286  -0.1599 40  THR   A O   
217  C  CB  . THR   A 40  ? 0.1734 0.4337 0.4655 -0.0665 0.1007  0.0431  40  THR   A CB  
218  O  OG1 . THR   A 40  ? 0.2440 0.4910 0.5004 -0.0110 0.0366  -0.0816 40  THR   A OG1 
219  C  CG2 . THR   A 40  ? 0.2392 0.3252 0.4138 0.0107  0.0566  0.0507  40  THR   A CG2 
220  N  N   . TRP   A 41  ? 0.3042 1.0458 0.9714 0.1230  -0.1211 -0.3123 41  TRP   A N   
221  C  CA  . TRP   A 41  ? 0.3108 0.4705 0.5026 -0.1764 0.0082  -0.1736 41  TRP   A CA  
222  C  C   . TRP   A 41  ? 0.1946 0.4799 0.5099 -0.1773 0.0852  -0.1512 41  TRP   A C   
223  O  O   . TRP   A 41  ? 0.4702 0.5329 0.6670 -0.2386 0.0621  -0.1782 41  TRP   A O   
224  C  CB  . TRP   A 41  ? 0.3815 0.3944 0.4090 -0.2276 0.1278  -0.1063 41  TRP   A CB  
225  C  CG  . TRP   A 41  ? 0.4606 0.3729 0.3994 -0.2031 0.1157  -0.0938 41  TRP   A CG  
226  C  CD1 . TRP   A 41  ? 0.3743 0.5771 0.4500 -0.1933 0.0130  -0.0158 41  TRP   A CD1 
227  C  CD2 . TRP   A 41  ? 0.2654 0.2811 0.4392 -0.0901 0.0804  -0.1415 41  TRP   A CD2 
228  N  NE1 . TRP   A 41  ? 0.5124 0.5794 0.4164 -0.2319 0.0486  -0.1096 41  TRP   A NE1 
229  C  CE2 . TRP   A 41  ? 0.2404 0.5913 0.4961 -0.1584 0.1379  -0.1666 41  TRP   A CE2 
230  C  CE3 . TRP   A 41  ? 0.1488 0.2316 0.4729 -0.0089 0.0516  -0.1173 41  TRP   A CE3 
231  C  CZ2 . TRP   A 41  ? 0.3106 0.4600 0.4129 -0.1132 0.0539  -0.1227 41  TRP   A CZ2 
232  C  CZ3 . TRP   A 41  ? 0.1190 0.2450 0.5091 0.0100  -0.0224 -0.0496 41  TRP   A CZ3 
233  C  CH2 . TRP   A 41  ? 0.1695 0.2816 0.5328 -0.0170 0.0551  0.0232  41  TRP   A CH2 
234  N  N   . GLU   A 42  ? 0.1849 0.2488 0.5528 -0.0439 0.0163  -0.2077 42  GLU   A N   
235  C  CA  . GLU   A 42  ? 0.1319 0.2797 0.5285 0.0168  -0.0492 -0.1533 42  GLU   A CA  
236  C  C   . GLU   A 42  ? 0.1146 0.1943 0.5611 -0.0088 -0.0223 -0.1006 42  GLU   A C   
237  O  O   . GLU   A 42  ? 0.1333 0.1939 0.4645 -0.0093 -0.0406 -0.0863 42  GLU   A O   
238  C  CB  . GLU   A 42  ? 0.1899 0.2942 0.5796 0.0746  -0.0537 -0.1264 42  GLU   A CB  
239  N  N   . PRO   A 43  ? 0.1436 0.2322 0.4946 -0.0117 -0.0092 -0.1262 43  PRO   A N   
240  C  CA  . PRO   A 43  ? 0.1869 0.1827 0.3944 -0.0142 -0.0440 -0.0745 43  PRO   A CA  
241  C  C   . PRO   A 43  ? 0.1232 0.2125 0.4137 0.0322  -0.1022 -0.0850 43  PRO   A C   
242  O  O   . PRO   A 43  ? 0.1360 0.3069 0.5269 0.0206  -0.1111 -0.0368 43  PRO   A O   
243  C  CB  . PRO   A 43  ? 0.1527 0.1930 0.5422 -0.0280 -0.0362 -0.1266 43  PRO   A CB  
244  C  CG  . PRO   A 43  ? 0.2027 0.4435 0.8136 -0.0621 0.0363  -0.3235 43  PRO   A CG  
245  C  CD  . PRO   A 43  ? 0.1749 0.3013 0.5100 -0.0662 0.0248  -0.1677 43  PRO   A CD  
246  N  N   . PHE   A 44  ? 0.1411 0.2078 0.3577 0.0119  -0.0600 -0.0351 44  PHE   A N   
247  C  CA  . PHE   A 44  ? 0.1631 0.2069 0.3206 0.0503  -0.0984 -0.0590 44  PHE   A CA  
248  C  C   . PHE   A 44  ? 0.1566 0.1917 0.2744 0.0125  -0.0750 -0.0354 44  PHE   A C   
249  O  O   . PHE   A 44  ? 0.2521 0.1879 0.3281 0.0699  -0.1125 -0.0407 44  PHE   A O   
250  C  CB  . PHE   A 44  ? 0.2123 0.1566 0.3112 0.0233  -0.0958 -0.0260 44  PHE   A CB  
251  C  CG  . PHE   A 44  ? 0.2107 0.1575 0.2969 0.0194  -0.0645 -0.0268 44  PHE   A CG  
252  C  CD1 . PHE   A 44  ? 0.3070 0.1803 0.3327 0.0228  -0.1308 0.0025  44  PHE   A CD1 
253  C  CD2 . PHE   A 44  ? 0.2330 0.1458 0.2967 0.0357  -0.0341 -0.0065 44  PHE   A CD2 
254  C  CE1 . PHE   A 44  ? 0.3140 0.1964 0.3577 0.0211  -0.1152 -0.0172 44  PHE   A CE1 
255  C  CE2 . PHE   A 44  ? 0.3132 0.2067 0.3432 -0.0085 -0.0494 -0.0262 44  PHE   A CE2 
256  C  CZ  . PHE   A 44  ? 0.3859 0.2124 0.2809 -0.0522 -0.0983 0.0400  44  PHE   A CZ  
257  N  N   . ALA   A 45  ? 0.1565 0.1576 0.3072 0.0137  -0.0878 -0.0167 45  ALA   A N   
258  C  CA  . ALA   A 45  ? 0.1820 0.1549 0.2695 0.0163  -0.0757 0.0025  45  ALA   A CA  
259  C  C   . ALA   A 45  ? 0.1495 0.1336 0.2560 -0.0135 -0.0715 -0.0340 45  ALA   A C   
260  O  O   . ALA   A 45  ? 0.1811 0.1470 0.2602 0.0251  -0.0699 -0.0459 45  ALA   A O   
261  C  CB  . ALA   A 45  ? 0.1984 0.1780 0.3121 0.0194  -0.0403 0.0185  45  ALA   A CB  
262  N  N   . SER   A 46  ? 0.1655 0.1360 0.2279 -0.0039 -0.0713 -0.0299 46  SER   A N   
263  C  CA  . SER   A 46  ? 0.1488 0.1455 0.2204 0.0043  -0.0592 -0.0266 46  SER   A CA  
264  C  C   . SER   A 46  ? 0.1660 0.1501 0.2211 -0.0146 -0.0736 -0.0161 46  SER   A C   
265  O  O   . SER   A 46  ? 0.1777 0.1524 0.2485 -0.0029 -0.0776 -0.0193 46  SER   A O   
266  C  CB  . SER   A 46  ? 0.1296 0.1521 0.2698 -0.0084 -0.0360 -0.0339 46  SER   A CB  
267  O  OG  . SER   A 46  ? 0.1554 0.1596 0.3064 -0.0265 -0.0637 -0.0100 46  SER   A OG  
268  N  N   . GLY   A 47  ? 0.1565 0.1434 0.2216 -0.0022 -0.0604 -0.0207 47  GLY   A N   
269  C  CA  . GLY   A 47  ? 0.1713 0.1606 0.2216 -0.0100 -0.0602 -0.0209 47  GLY   A CA  
270  C  C   . GLY   A 47  ? 0.1473 0.1537 0.1924 0.0066  -0.0290 -0.0243 47  GLY   A C   
271  O  O   . GLY   A 47  ? 0.1600 0.1598 0.2279 0.0045  -0.0397 -0.0264 47  GLY   A O   
272  N  N   . LYS   A 48  ? 0.1492 0.1797 0.2176 0.0063  -0.0183 -0.0155 48  LYS   A N   
273  C  CA  . LYS   A 48  ? 0.1058 0.2196 0.2889 0.0132  -0.0430 -0.0009 48  LYS   A CA  
274  C  C   . LYS   A 48  ? 0.1714 0.1286 0.2387 0.0047  -0.0317 -0.0191 48  LYS   A C   
275  O  O   . LYS   A 48  ? 0.1608 0.2116 0.2545 0.0234  -0.0288 -0.0203 48  LYS   A O   
276  C  CB  . LYS   A 48  ? 0.1318 0.3016 0.5095 -0.0448 0.0026  -0.0073 48  LYS   A CB  
277  C  CG  . LYS   A 48  ? 0.1683 0.2894 0.3505 0.0470  0.0171  0.0570  48  LYS   A CG  
278  N  N   . THR   A 49  ? 0.1457 0.1387 0.2338 0.0036  -0.0354 -0.0232 49  THR   A N   
279  C  CA  . THR   A 49  ? 0.1599 0.0971 0.2403 0.0183  -0.0320 -0.0068 49  THR   A CA  
280  C  C   . THR   A 49  ? 0.2059 0.0919 0.2479 0.0263  -0.0578 -0.0326 49  THR   A C   
281  O  O   . THR   A 49  ? 0.2007 0.1948 0.3450 0.0521  -0.0733 -0.1488 49  THR   A O   
282  C  CB  . THR   A 49  ? 0.1359 0.1167 0.2482 0.0170  -0.0453 -0.0153 49  THR   A CB  
283  O  OG1 . THR   A 49  ? 0.1525 0.1273 0.2381 0.0213  -0.0432 -0.0178 49  THR   A OG1 
284  C  CG2 . THR   A 49  ? 0.1891 0.1214 0.2355 0.0247  -0.0357 -0.0237 49  THR   A CG2 
285  N  N   . SER   A 50  ? 0.2094 0.1807 0.2330 0.0208  -0.0057 0.0074  50  SER   A N   
286  C  CA  . SER   A 50  ? 0.2859 0.2231 0.2416 0.0771  -0.0260 -0.0658 50  SER   A CA  
287  C  C   . SER   A 50  ? 0.2327 0.2272 0.2746 0.0735  -0.0061 -0.0655 50  SER   A C   
288  O  O   . SER   A 50  ? 0.2174 0.2121 0.2628 0.0453  -0.0021 -0.0571 50  SER   A O   
289  C  CB  . SER   A 50  ? 0.4522 0.2935 0.2257 0.1414  -0.0247 -0.0668 50  SER   A CB  
290  O  OG  . SER   A 50  ? 0.4185 0.2540 0.2620 0.1097  0.0638  -0.0127 50  SER   A OG  
291  N  N   . GLU   A 51  ? 0.2499 0.2855 0.2508 0.0960  -0.0285 -0.0783 51  GLU   A N   
292  C  CA  . GLU   A 51  ? 0.2860 0.2709 0.2554 0.1013  -0.0173 -0.0721 51  GLU   A CA  
293  C  C   . GLU   A 51  ? 0.2312 0.2846 0.2623 0.0718  -0.0297 -0.0384 51  GLU   A C   
294  O  O   . GLU   A 51  ? 0.2612 0.2994 0.2714 0.0771  -0.0146 -0.0186 51  GLU   A O   
295  C  CB  . GLU   A 51  ? 0.3393 0.4011 0.3760 0.1582  -0.0248 -0.1332 51  GLU   A CB  
296  N  N   . SER   A 52  ? 0.2640 0.2681 0.2587 0.0988  0.0289  -0.0309 52  SER   A N   
297  C  CA  . SER   A 52  ? 0.2600 0.2743 0.2263 0.0513  0.0211  -0.0278 52  SER   A CA  
298  C  C   . SER   A 52  ? 0.1998 0.2222 0.2258 0.0527  -0.0068 -0.0174 52  SER   A C   
299  O  O   . SER   A 52  ? 0.1985 0.2285 0.2526 0.0402  0.0117  0.0101  52  SER   A O   
300  C  CB  . SER   A 52  ? 0.3676 0.2915 0.2585 0.0409  0.1007  -0.0206 52  SER   A CB  
301  O  OG  . SER   A 52  ? 0.4955 0.3907 0.3685 0.0788  -0.0464 0.0643  52  SER   A OG  
302  N  N   . GLY   A 53  ? 0.1797 0.1867 0.2250 0.0576  -0.0099 -0.0279 53  GLY   A N   
303  C  CA  . GLY   A 53  ? 0.1341 0.1978 0.2227 0.0385  -0.0087 -0.0047 53  GLY   A CA  
304  C  C   . GLY   A 53  ? 0.1418 0.1715 0.1970 0.0375  -0.0212 -0.0135 53  GLY   A C   
305  O  O   . GLY   A 53  ? 0.2052 0.1534 0.2106 0.0417  -0.0243 -0.0254 53  GLY   A O   
306  N  N   . GLU   A 54  ? 0.1974 0.1625 0.2072 0.0479  -0.0143 -0.0110 54  GLU   A N   
307  C  CA  . GLU   A 54  ? 0.1766 0.1504 0.2164 0.0393  -0.0138 -0.0218 54  GLU   A CA  
308  C  C   . GLU   A 54  ? 0.1812 0.1690 0.1829 0.0327  -0.0228 -0.0317 54  GLU   A C   
309  O  O   . GLU   A 54  ? 0.2290 0.1646 0.2379 0.0517  -0.0568 -0.0504 54  GLU   A O   
310  C  CB  . GLU   A 54  ? 0.2073 0.2094 0.2727 0.0548  0.0267  0.0152  54  GLU   A CB  
311  C  CG  . GLU   A 54  ? 0.1749 0.3060 0.3750 0.0581  0.0310  0.0266  54  GLU   A CG  
312  C  CD  . GLU   A 54  ? 0.1506 0.3008 0.4072 0.0043  0.0804  -0.0315 54  GLU   A CD  
313  O  OE1 . GLU   A 54  ? 0.2358 0.5413 0.4882 -0.0920 0.0471  0.1599  54  GLU   A OE1 
314  O  OE2 . GLU   A 54  ? 0.1949 0.3848 0.5711 -0.0734 0.0412  0.0435  54  GLU   A OE2 
315  N  N   . LEU   A 55  ? 0.1839 0.1485 0.2065 0.0166  -0.0315 -0.0303 55  LEU   A N   
316  C  CA  . LEU   A 55  ? 0.1803 0.1489 0.2008 0.0306  -0.0309 -0.0201 55  LEU   A CA  
317  C  C   . LEU   A 55  ? 0.1456 0.1868 0.2344 -0.0129 -0.0127 0.0030  55  LEU   A C   
318  O  O   . LEU   A 55  ? 0.1973 0.1587 0.2627 0.0043  -0.0313 -0.0085 55  LEU   A O   
319  C  CB  . LEU   A 55  ? 0.2062 0.1317 0.2108 0.0081  -0.0356 -0.0182 55  LEU   A CB  
320  C  CG  . LEU   A 55  ? 0.1804 0.1555 0.2346 0.0138  -0.0095 -0.0034 55  LEU   A CG  
321  C  CD1 . LEU   A 55  ? 0.1945 0.1893 0.2596 0.0006  -0.0540 -0.0026 55  LEU   A CD1 
322  C  CD2 . LEU   A 55  ? 0.1875 0.1577 0.2612 0.0073  -0.0204 -0.0207 55  LEU   A CD2 
323  N  N   . HIS   A 56  ? 0.2196 0.2383 0.2350 0.0334  -0.0389 0.0065  56  HIS   A N   
324  C  CA  . HIS   A 56  ? 0.2821 0.2801 0.2611 0.0082  -0.0532 0.0883  56  HIS   A CA  
325  C  C   . HIS   A 56  ? 0.3058 0.2877 0.2379 0.0522  -0.0321 0.0101  56  HIS   A C   
326  O  O   . HIS   A 56  ? 0.2860 0.2899 0.3342 0.0353  -0.1196 0.0325  56  HIS   A O   
327  C  CB  . HIS   A 56  ? 0.2555 0.4577 0.3558 0.0980  0.0094  0.0960  56  HIS   A CB  
328  C  CG  . HIS   A 56  ? 0.2639 0.4642 0.3558 0.0506  0.0729  0.1473  56  HIS   A CG  
329  N  ND1 . HIS   A 56  ? 0.2891 0.6169 0.7293 0.1174  -0.0152 0.1084  56  HIS   A ND1 
330  C  CD2 . HIS   A 56  ? 0.3006 0.4764 0.4490 0.0437  0.0265  0.0234  56  HIS   A CD2 
331  C  CE1 . HIS   A 56  ? 0.2806 0.4798 0.6625 0.1144  0.0649  0.2555  56  HIS   A CE1 
332  N  NE2 . HIS   A 56  ? 0.3281 0.5846 0.4850 0.0469  0.0535  0.0132  56  HIS   A NE2 
333  N  N   . GLY   A 57  ? 0.2537 0.2663 0.2986 0.0461  -0.0173 0.0093  57  GLY   A N   
334  C  CA  . GLY   A 57  ? 0.3382 0.2668 0.2774 0.0938  -0.0676 -0.0359 57  GLY   A CA  
335  C  C   . GLY   A 57  ? 0.3004 0.2145 0.3386 0.0934  -0.0726 0.0058  57  GLY   A C   
336  O  O   . GLY   A 57  ? 0.2963 0.3553 0.3936 0.0714  -0.1355 -0.0427 57  GLY   A O   
337  N  N   . LEU   A 58  ? 0.2535 0.2173 0.3080 0.0239  -0.0651 -0.0293 58  LEU   A N   
338  C  CA  . LEU   A 58  ? 0.2312 0.1504 0.3078 -0.0042 -0.0632 -0.0069 58  LEU   A CA  
339  C  C   . LEU   A 58  ? 0.2302 0.2193 0.3176 0.0269  -0.0577 -0.0002 58  LEU   A C   
340  O  O   . LEU   A 58  ? 0.2283 0.2092 0.4020 0.0249  -0.0308 -0.0036 58  LEU   A O   
341  C  CB  . LEU   A 58  ? 0.1809 0.2035 0.3593 0.0378  -0.0448 -0.0459 58  LEU   A CB  
342  C  CG  . LEU   A 58  ? 0.1850 0.2124 0.3464 0.0567  -0.0566 -0.0267 58  LEU   A CG  
343  C  CD1 . LEU   A 58  ? 0.2408 0.2395 0.3563 0.0691  -0.0941 -0.0521 58  LEU   A CD1 
344  C  CD2 . LEU   A 58  ? 0.2394 0.2168 0.4119 0.0480  -0.0557 0.0256  58  LEU   A CD2 
345  N  N   . THR   A 59  ? 0.2372 0.2340 0.2939 0.0470  -0.0667 -0.0066 59  THR   A N   
346  C  CA  . THR   A 59  ? 0.2342 0.2384 0.2977 0.0487  -0.0953 -0.0196 59  THR   A CA  
347  C  C   . THR   A 59  ? 0.2577 0.2274 0.2851 0.0810  -0.0603 0.0048  59  THR   A C   
348  O  O   . THR   A 59  ? 0.2494 0.2855 0.3314 0.0606  -0.0349 0.0236  59  THR   A O   
349  C  CB  . THR   A 59  ? 0.2652 0.1862 0.2845 0.0374  -0.0941 -0.0130 59  THR   A CB  
350  O  OG1 . THR   A 59  ? 0.2511 0.2232 0.3356 0.0613  -0.0795 -0.0201 59  THR   A OG1 
351  C  CG2 . THR   A 59  ? 0.2503 0.2110 0.3319 0.0651  -0.1399 -0.0584 59  THR   A CG2 
352  N  N   . THR   A 60  ? 0.2592 0.2432 0.3878 0.0594  -0.0981 0.0226  60  THR   A N   
353  C  CA  . THR   A 60  ? 0.3355 0.2886 0.2762 0.1346  -0.0606 0.0448  60  THR   A CA  
354  C  C   . THR   A 60  ? 0.2094 0.2670 0.3128 0.0492  -0.0069 0.0454  60  THR   A C   
355  O  O   . THR   A 60  ? 0.2367 0.2650 0.2979 0.0284  -0.0353 0.0515  60  THR   A O   
356  C  CB  . THR   A 60  ? 0.3827 0.2982 0.3179 0.1374  -0.0911 0.0305  60  THR   A CB  
357  O  OG1 . THR   A 60  ? 0.3546 0.3248 0.3654 0.0958  -0.1397 -0.0108 60  THR   A OG1 
358  C  CG2 . THR   A 60  ? 0.5755 0.3553 0.3797 0.0899  -0.1380 0.0086  60  THR   A CG2 
359  N  N   . GLU   A 61  ? 0.3476 0.2947 0.3769 0.0842  0.0667  0.0882  61  GLU   A N   
360  C  CA  . GLU   A 61  ? 0.4509 0.2979 0.4671 0.1624  0.0955  0.1214  61  GLU   A CA  
361  C  C   . GLU   A 61  ? 0.3931 0.2509 0.4106 0.0356  0.0525  0.0790  61  GLU   A C   
362  O  O   . GLU   A 61  ? 0.2853 0.3145 0.4874 0.0109  0.0043  -0.0101 61  GLU   A O   
363  C  CB  . GLU   A 61  ? 0.6390 0.2775 0.4728 0.0843  0.1143  0.0834  61  GLU   A CB  
364  N  N   . GLU   A 62  ? 0.3649 0.2886 0.3520 0.1067  -0.0059 0.0827  62  GLU   A N   
365  C  CA  . GLU   A 62  ? 0.4050 0.2873 0.3256 0.1432  -0.0253 0.0723  62  GLU   A CA  
366  C  C   . GLU   A 62  ? 0.2616 0.1845 0.3570 0.0322  -0.0761 0.0368  62  GLU   A C   
367  O  O   . GLU   A 62  ? 0.2701 0.2034 0.3631 0.0580  -0.0278 0.0357  62  GLU   A O   
368  C  CB  . GLU   A 62  ? 0.3651 0.4856 0.4176 0.1604  -0.0760 0.0484  62  GLU   A CB  
369  C  CG  . GLU   A 62  ? 0.3393 0.3192 0.3867 0.0596  -0.1225 0.0368  62  GLU   A CG  
370  C  CD  . GLU   A 62  ? 0.2276 0.2875 0.3820 0.1021  -0.0080 0.0572  62  GLU   A CD  
371  O  OE1 . GLU   A 62  ? 0.2321 0.2460 0.4042 0.0459  -0.0847 -0.0081 62  GLU   A OE1 
372  O  OE2 . GLU   A 62  ? 0.2403 0.3947 0.4245 0.1670  0.0530  0.1276  62  GLU   A OE2 
373  N  N   . GLU   A 63  ? 0.2235 0.2065 0.2765 0.0192  -0.0929 0.0280  63  GLU   A N   
374  C  CA  . GLU   A 63  ? 0.2152 0.1650 0.3066 -0.0198 -0.1262 0.0284  63  GLU   A CA  
375  C  C   . GLU   A 63  ? 0.1860 0.1759 0.2833 0.0552  -0.0663 0.0003  63  GLU   A C   
376  O  O   . GLU   A 63  ? 0.1801 0.1773 0.3119 0.0211  -0.0979 -0.0354 63  GLU   A O   
378  N  N   . PHE   A 64  ? 0.1767 0.2036 0.2717 0.0164  -0.0751 0.0299  64  PHE   A N   
379  C  CA  . PHE   A 64  ? 0.1972 0.1363 0.2869 0.0437  -0.0795 -0.0065 64  PHE   A CA  
380  C  C   . PHE   A 64  ? 0.1770 0.1364 0.2514 0.0091  -0.0586 0.0192  64  PHE   A C   
381  O  O   . PHE   A 64  ? 0.2022 0.1623 0.3691 -0.0023 -0.0842 0.0209  64  PHE   A O   
382  C  CB  . PHE   A 64  ? 0.1982 0.1208 0.3180 0.0199  -0.0778 -0.0172 64  PHE   A CB  
383  C  CG  . PHE   A 64  ? 0.1756 0.1535 0.2836 0.0248  -0.1046 -0.0251 64  PHE   A CG  
384  C  CD1 . PHE   A 64  ? 0.2069 0.2199 0.2960 0.0660  -0.0975 0.0020  64  PHE   A CD1 
385  C  CD2 . PHE   A 64  ? 0.1737 0.2869 0.3239 0.0079  -0.0829 -0.0303 64  PHE   A CD2 
386  C  CE1 . PHE   A 64  ? 0.2239 0.2399 0.3058 0.0953  -0.1047 -0.0343 64  PHE   A CE1 
387  C  CE2 . PHE   A 64  ? 0.2310 0.4140 0.3744 0.0067  -0.1581 -0.0314 64  PHE   A CE2 
388  C  CZ  . PHE   A 64  ? 0.2697 0.2291 0.3029 0.0939  -0.1151 -0.0314 64  PHE   A CZ  
389  N  N   . VAL   A 65  ? 0.1695 0.1561 0.3363 0.0362  -0.0981 -0.0163 65  VAL   A N   
390  C  CA  . VAL   A 65  ? 0.2136 0.1032 0.3054 0.0277  -0.1050 0.0190  65  VAL   A CA  
391  C  C   . VAL   A 65  ? 0.2257 0.1302 0.3024 0.0292  -0.1240 0.0109  65  VAL   A C   
392  O  O   . VAL   A 65  ? 0.2601 0.1376 0.2936 0.0373  -0.1357 -0.0154 65  VAL   A O   
393  C  CB  . VAL   A 65  ? 0.2075 0.1410 0.3017 0.0243  -0.1070 -0.0106 65  VAL   A CB  
394  C  CG1 . VAL   A 65  ? 0.2250 0.2399 0.3259 0.0781  -0.1359 -0.0267 65  VAL   A CG1 
395  C  CG2 . VAL   A 65  ? 0.2122 0.1686 0.3824 0.0466  -0.1130 -0.0325 65  VAL   A CG2 
396  N  N   . GLU   A 66  ? 0.2122 0.1296 0.3398 0.0392  -0.1410 -0.0064 66  GLU   A N   
397  C  CA  . GLU   A 66  ? 0.2262 0.1432 0.2954 0.0258  -0.1016 0.0134  66  GLU   A CA  
398  C  C   . GLU   A 66  ? 0.1940 0.1590 0.2968 0.0629  -0.0796 -0.0104 66  GLU   A C   
399  O  O   . GLU   A 66  ? 0.1831 0.2359 0.4221 0.0427  -0.1118 0.0354  66  GLU   A O   
400  C  CB  . GLU   A 66  ? 0.2968 0.2035 0.3230 0.0177  -0.1169 -0.0243 66  GLU   A CB  
401  C  CG  . GLU   A 66  ? 0.2443 0.2170 0.3723 0.0172  -0.1615 -0.0258 66  GLU   A CG  
402  C  CD  . GLU   A 66  ? 0.2769 0.1599 0.3552 0.0064  -0.1990 -0.0243 66  GLU   A CD  
403  O  OE1 . GLU   A 66  ? 0.2627 0.1728 0.2364 -0.0413 -0.1173 0.0494  66  GLU   A OE1 
404  O  OE2 . GLU   A 66  ? 0.3017 0.1420 0.3477 0.0506  -0.1793 -0.0032 66  GLU   A OE2 
405  N  N   . GLY   A 67  ? 0.1982 0.1587 0.3049 0.0276  -0.0945 0.0100  67  GLY   A N   
406  C  CA  . GLY   A 67  ? 0.2037 0.1736 0.3547 0.0387  -0.0781 0.0129  67  GLY   A CA  
407  C  C   . GLY   A 67  ? 0.1594 0.1352 0.2914 0.0250  -0.0533 -0.0169 67  GLY   A C   
408  O  O   . GLY   A 67  ? 0.1569 0.1776 0.2913 0.0152  -0.0699 0.0001  67  GLY   A O   
409  N  N   . ILE   A 68  ? 0.1420 0.1553 0.2943 0.0413  -0.0629 -0.0312 68  ILE   A N   
410  C  CA  . ILE   A 68  ? 0.1092 0.1362 0.2801 0.0159  -0.0250 -0.0306 68  ILE   A CA  
411  C  C   . ILE   A 68  ? 0.1318 0.1506 0.2601 0.0088  -0.0566 -0.0266 68  ILE   A C   
412  O  O   . ILE   A 68  ? 0.1277 0.1616 0.3433 0.0173  -0.0598 -0.0596 68  ILE   A O   
413  C  CB  . ILE   A 68  ? 0.1487 0.1611 0.3035 0.0095  -0.0401 -0.0413 68  ILE   A CB  
414  C  CG1 . ILE   A 68  ? 0.2321 0.1787 0.3158 -0.0001 0.0136  -0.0303 68  ILE   A CG1 
415  C  CG2 . ILE   A 68  ? 0.2130 0.2070 0.2851 0.0197  -0.0312 -0.0140 68  ILE   A CG2 
416  C  CD1 . ILE   A 68  ? 0.3347 0.2369 0.3311 0.0166  0.0450  -0.0613 68  ILE   A CD1 
417  N  N   . TYR   A 69  ? 0.1177 0.1115 0.2732 0.0009  -0.0426 -0.0304 69  TYR   A N   
418  C  CA  . TYR   A 69  ? 0.1059 0.1477 0.2498 -0.0039 -0.0362 -0.0332 69  TYR   A CA  
419  C  C   . TYR   A 69  ? 0.1070 0.1235 0.2304 0.0030  -0.0575 -0.0218 69  TYR   A C   
420  O  O   . TYR   A 69  ? 0.1464 0.1237 0.2501 -0.0100 -0.0560 -0.0044 69  TYR   A O   
421  C  CB  . TYR   A 69  ? 0.1386 0.1110 0.2602 0.0143  -0.0527 -0.0193 69  TYR   A CB  
422  C  CG  . TYR   A 69  ? 0.1472 0.1338 0.2593 0.0169  -0.0464 -0.0046 69  TYR   A CG  
423  C  CD1 . TYR   A 69  ? 0.1811 0.1274 0.2445 0.0089  -0.0623 -0.0162 69  TYR   A CD1 
424  C  CD2 . TYR   A 69  ? 0.1990 0.1331 0.2768 0.0230  -0.0835 -0.0257 69  TYR   A CD2 
425  C  CE1 . TYR   A 69  ? 0.1946 0.1426 0.2722 0.0412  -0.0923 -0.0004 69  TYR   A CE1 
426  C  CE2 . TYR   A 69  ? 0.1873 0.1424 0.3067 0.0194  -0.0957 -0.0239 69  TYR   A CE2 
427  C  CZ  . TYR   A 69  ? 0.1850 0.1334 0.3304 0.0307  -0.1056 0.0069  69  TYR   A CZ  
428  O  OH  . TYR   A 69  ? 0.2154 0.1522 0.3305 0.0114  -0.1130 0.0046  69  TYR   A OH  
429  N  N   . LYS   A 70  ? 0.1272 0.1163 0.2521 -0.0019 -0.0537 -0.0319 70  LYS   A N   
430  C  CA  . LYS   A 70  ? 0.1319 0.1344 0.2444 0.0020  -0.0276 -0.0215 70  LYS   A CA  
431  C  C   . LYS   A 70  ? 0.1274 0.1124 0.2357 -0.0076 -0.0436 -0.0088 70  LYS   A C   
432  O  O   . LYS   A 70  ? 0.1499 0.1542 0.2702 0.0100  -0.0623 -0.0314 70  LYS   A O   
433  C  CB  . LYS   A 70  ? 0.1668 0.1643 0.2972 -0.0253 0.0157  -0.0440 70  LYS   A CB  
434  C  CG  . LYS   A 70  ? 0.2911 0.1726 0.3180 -0.0840 -0.0054 0.0089  70  LYS   A CG  
435  C  CD  . LYS   A 70  ? 0.3672 0.4238 0.4045 -0.0836 0.0869  0.1148  70  LYS   A CD  
436  C  CE  . LYS   A 70  ? 0.3177 0.4196 0.4249 -0.0265 0.1170  0.0952  70  LYS   A CE  
437  N  NZ  . LYS   A 70  ? 0.2499 0.4599 0.5546 0.0210  0.1786  0.1808  70  LYS   A NZ  
438  N  N   . VAL   A 71  ? 0.1348 0.1065 0.2436 -0.0021 -0.0508 -0.0057 71  VAL   A N   
439  C  CA  . VAL   A 71  ? 0.1531 0.0982 0.2337 0.0159  -0.0505 -0.0050 71  VAL   A CA  
440  C  C   . VAL   A 71  ? 0.1486 0.1022 0.2363 0.0213  -0.0535 -0.0236 71  VAL   A C   
441  O  O   . VAL   A 71  ? 0.1905 0.1387 0.2578 -0.0135 -0.0719 0.0018  71  VAL   A O   
442  C  CB  . VAL   A 71  ? 0.1501 0.1579 0.2229 0.0049  -0.0505 -0.0007 71  VAL   A CB  
443  C  CG1 . VAL   A 71  ? 0.1877 0.1669 0.2585 0.0217  -0.0166 -0.0272 71  VAL   A CG1 
444  C  CG2 . VAL   A 71  ? 0.1831 0.1769 0.2613 -0.0418 -0.0458 0.0098  71  VAL   A CG2 
445  N  N   . GLU   A 72  ? 0.1414 0.1050 0.2329 0.0009  -0.0374 -0.0077 72  GLU   A N   
446  C  CA  . GLU   A 72  ? 0.1322 0.1362 0.2389 0.0131  -0.0188 -0.0034 72  GLU   A CA  
447  C  C   . GLU   A 72  ? 0.1343 0.1285 0.2179 0.0159  -0.0379 0.0015  72  GLU   A C   
448  O  O   . GLU   A 72  ? 0.1620 0.1382 0.2439 0.0227  -0.0465 -0.0121 72  GLU   A O   
449  C  CB  . GLU   A 72  ? 0.1665 0.1675 0.2867 0.0316  0.0300  -0.0213 72  GLU   A CB  
450  C  CG  . GLU   A 72  ? 0.1912 0.1789 0.3022 0.0138  0.0319  0.0107  72  GLU   A CG  
451  C  CD  . GLU   A 72  ? 0.1941 0.3712 0.4073 0.0505  0.1353  0.1186  72  GLU   A CD  
452  O  OE1 . GLU   A 72  ? 0.2199 0.3088 0.6124 -0.0091 0.1697  0.0269  72  GLU   A OE1 
453  O  OE2 . GLU   A 72  ? 0.3593 0.2716 0.2815 -0.0275 -0.0074 0.0209  72  GLU   A OE2 
454  N  N   . ILE   A 73  ? 0.1426 0.1304 0.1980 0.0161  -0.0174 -0.0168 73  ILE   A N   
455  C  CA  . ILE   A 73  ? 0.1306 0.1517 0.1925 0.0187  -0.0172 0.0023  73  ILE   A CA  
456  C  C   . ILE   A 73  ? 0.1405 0.1240 0.2113 0.0260  -0.0418 -0.0111 73  ILE   A C   
457  O  O   . ILE   A 73  ? 0.1469 0.1449 0.2173 0.0082  -0.0256 0.0035  73  ILE   A O   
458  C  CB  . ILE   A 73  ? 0.1547 0.1384 0.2027 0.0121  -0.0076 0.0223  73  ILE   A CB  
459  C  CG1 . ILE   A 73  ? 0.1596 0.1682 0.2210 -0.0250 -0.0158 0.0055  73  ILE   A CG1 
460  C  CG2 . ILE   A 73  ? 0.1658 0.1486 0.2410 0.0370  -0.0024 0.0054  73  ILE   A CG2 
461  C  CD1 . ILE   A 73  ? 0.1623 0.2232 0.2654 -0.0549 -0.0186 -0.0024 73  ILE   A CD1 
462  N  N   . ASP   A 74  ? 0.1433 0.1330 0.2175 0.0045  -0.0142 0.0000  74  ASP   A N   
463  C  CA  . ASP   A 74  ? 0.1449 0.1426 0.2273 0.0000  -0.0463 0.0269  74  ASP   A CA  
464  C  C   . ASP   A 74  ? 0.1313 0.1437 0.2143 0.0112  -0.0167 -0.0049 74  ASP   A C   
465  O  O   . ASP   A 74  ? 0.1677 0.1409 0.2476 0.0149  -0.0372 -0.0051 74  ASP   A O   
466  C  CB  . ASP   A 74  ? 0.1363 0.1480 0.3044 0.0117  -0.0340 0.0035  74  ASP   A CB  
467  C  CG  . ASP   A 74  ? 0.1260 0.1609 0.2890 -0.0069 -0.0404 0.0248  74  ASP   A CG  
468  O  OD1 . ASP   A 74  ? 0.1658 0.1370 0.3375 -0.0090 -0.0040 0.0184  74  ASP   A OD1 
469  O  OD2 . ASP   A 74  ? 0.1724 0.1763 0.4272 -0.0400 -0.1051 0.0549  74  ASP   A OD2 
470  N  N   . THR   A 75  ? 0.1411 0.1024 0.2267 0.0095  -0.0123 -0.0006 75  THR   A N   
471  C  CA  . THR   A 75  ? 0.1284 0.1211 0.2133 0.0260  -0.0105 0.0036  75  THR   A CA  
472  C  C   . THR   A 75  ? 0.1346 0.1125 0.2351 -0.0109 -0.0088 0.0081  75  THR   A C   
473  O  O   . THR   A 75  ? 0.1460 0.1120 0.2510 0.0196  -0.0049 0.0000  75  THR   A O   
474  C  CB  . THR   A 75  ? 0.1308 0.1354 0.2555 0.0123  -0.0004 0.0114  75  THR   A CB  
475  O  OG1 . THR   A 75  ? 0.1344 0.1148 0.2504 0.0055  -0.0116 0.0050  75  THR   A OG1 
476  C  CG2 . THR   A 75  ? 0.1459 0.1320 0.2781 0.0014  -0.0072 0.0425  75  THR   A CG2 
477  N  N   . LYS   A 76  ? 0.1181 0.1247 0.2587 -0.0025 -0.0029 0.0114  76  LYS   A N   
478  C  CA  . LYS   A 76  ? 0.1429 0.1109 0.2645 -0.0047 -0.0063 0.0250  76  LYS   A CA  
479  C  C   . LYS   A 76  ? 0.1616 0.0970 0.2630 0.0099  -0.0128 0.0162  76  LYS   A C   
480  O  O   . LYS   A 76  ? 0.1699 0.1111 0.2657 0.0095  -0.0130 0.0150  76  LYS   A O   
481  C  CB  . LYS   A 76  ? 0.1577 0.1357 0.2563 0.0014  0.0299  0.0246  76  LYS   A CB  
482  C  CG  . LYS   A 76  ? 0.1948 0.1504 0.2709 -0.0019 0.0402  0.0338  76  LYS   A CG  
483  C  CD  . LYS   A 76  ? 0.2520 0.1999 0.3418 -0.0459 0.1126  0.0440  76  LYS   A CD  
484  C  CE  . LYS   A 76  ? 0.2318 0.2387 0.4272 -0.0275 0.0948  0.0683  76  LYS   A CE  
485  N  NZ  . LYS   A 76  ? 0.3113 0.2750 0.4666 -0.0256 0.1641  0.0302  76  LYS   A NZ  
486  N  N   . SER   A 77  ? 0.1458 0.1259 0.2595 0.0155  -0.0237 0.0094  77  SER   A N   
487  C  CA  . SER   A 77  ? 0.1559 0.1332 0.2927 -0.0108 -0.0365 -0.0038 77  SER   A CA  
488  C  C   . SER   A 77  ? 0.1464 0.1213 0.2861 0.0066  -0.0235 -0.0065 77  SER   A C   
489  O  O   . SER   A 77  ? 0.1711 0.1395 0.2702 0.0024  -0.0146 -0.0019 77  SER   A O   
490  C  CB  . SER   A 77  ? 0.1589 0.1461 0.2950 -0.0187 -0.0254 0.0052  77  SER   A CB  
491  O  OG  . SER   A 77  ? 0.1749 0.1843 0.3966 -0.0430 -0.0398 0.0039  77  SER   A OG  
492  N  N   . TYR   A 78  ? 0.1622 0.1245 0.2507 0.0083  -0.0155 0.0082  78  TYR   A N   
493  C  CA  . TYR   A 78  ? 0.1570 0.1254 0.2310 0.0022  -0.0196 0.0010  78  TYR   A CA  
494  C  C   . TYR   A 78  ? 0.1603 0.1087 0.2512 0.0079  -0.0144 -0.0142 78  TYR   A C   
495  O  O   . TYR   A 78  ? 0.1803 0.1206 0.2504 0.0122  -0.0321 -0.0060 78  TYR   A O   
496  C  CB  . TYR   A 78  ? 0.1748 0.1287 0.2158 0.0073  -0.0200 0.0019  78  TYR   A CB  
497  C  CG  . TYR   A 78  ? 0.1767 0.1124 0.2264 0.0041  -0.0318 0.0161  78  TYR   A CG  
498  C  CD1 . TYR   A 78  ? 0.1738 0.1205 0.2384 0.0070  -0.0240 0.0044  78  TYR   A CD1 
499  C  CD2 . TYR   A 78  ? 0.1569 0.1010 0.2632 -0.0103 -0.0291 0.0032  78  TYR   A CD2 
500  C  CE1 . TYR   A 78  ? 0.1827 0.1525 0.2172 0.0059  -0.0107 -0.0056 78  TYR   A CE1 
501  C  CE2 . TYR   A 78  ? 0.1423 0.1376 0.2362 -0.0128 -0.0374 0.0017  78  TYR   A CE2 
502  C  CZ  . TYR   A 78  ? 0.1471 0.1167 0.2562 0.0029  -0.0168 -0.0028 78  TYR   A CZ  
503  O  OH  . TYR   A 78  ? 0.1580 0.1669 0.2979 -0.0094 0.0003  -0.0131 78  TYR   A OH  
504  N  N   . TRP   A 79  ? 0.1368 0.1000 0.2277 0.0096  0.0084  -0.0051 79  TRP   A N   
505  C  CA  . TRP   A 79  ? 0.1621 0.1071 0.2376 0.0069  -0.0277 0.0156  79  TRP   A CA  
506  C  C   . TRP   A 79  ? 0.1499 0.1072 0.2465 -0.0051 -0.0286 0.0027  79  TRP   A C   
507  O  O   . TRP   A 79  ? 0.1581 0.0971 0.2618 0.0038  -0.0068 0.0003  79  TRP   A O   
508  C  CB  . TRP   A 79  ? 0.1505 0.1036 0.2165 -0.0165 0.0002  0.0144  79  TRP   A CB  
509  C  CG  . TRP   A 79  ? 0.1218 0.0947 0.2027 0.0048  -0.0090 -0.0034 79  TRP   A CG  
510  C  CD1 . TRP   A 79  ? 0.1252 0.0932 0.2182 -0.0015 -0.0060 0.0012  79  TRP   A CD1 
511  C  CD2 . TRP   A 79  ? 0.1279 0.0939 0.2290 0.0153  -0.0147 -0.0102 79  TRP   A CD2 
512  N  NE1 . TRP   A 79  ? 0.1304 0.0876 0.2194 0.0073  -0.0098 0.0077  79  TRP   A NE1 
513  C  CE2 . TRP   A 79  ? 0.1242 0.0943 0.2148 0.0051  -0.0130 -0.0032 79  TRP   A CE2 
514  C  CE3 . TRP   A 79  ? 0.1280 0.1305 0.2374 0.0165  -0.0048 -0.0183 79  TRP   A CE3 
515  C  CZ2 . TRP   A 79  ? 0.1301 0.0952 0.2261 -0.0019 0.0051  0.0095  79  TRP   A CZ2 
516  C  CZ3 . TRP   A 79  ? 0.1419 0.1206 0.2488 0.0327  -0.0110 -0.0163 79  TRP   A CZ3 
517  C  CH2 . TRP   A 79  ? 0.1499 0.1241 0.2434 0.0029  0.0015  0.0025  79  TRP   A CH2 
518  N  N   . LYS   A 80  ? 0.1636 0.0693 0.2701 0.0035  -0.0195 0.0028  80  LYS   A N   
519  C  CA  . LYS   A 80  ? 0.1772 0.0876 0.2977 -0.0088 -0.0266 -0.0050 80  LYS   A CA  
520  C  C   . LYS   A 80  ? 0.1735 0.0850 0.3210 -0.0066 -0.0447 -0.0165 80  LYS   A C   
521  O  O   . LYS   A 80  ? 0.1838 0.0884 0.3398 -0.0174 -0.0188 -0.0160 80  LYS   A O   
522  C  CB  . LYS   A 80  ? 0.1450 0.1297 0.3101 -0.0025 -0.0267 0.0187  80  LYS   A CB  
523  C  CG  . LYS   A 80  ? 0.1598 0.1514 0.3358 0.0147  -0.0066 0.0241  80  LYS   A CG  
524  C  CD  . LYS   A 80  ? 0.1907 0.1966 0.3474 0.0411  0.0139  0.0457  80  LYS   A CD  
525  C  CE  . LYS   A 80  ? 0.2372 0.1732 0.3905 0.0102  0.0177  0.0400  80  LYS   A CE  
526  N  NZ  . LYS   A 80  ? 0.2483 0.2826 0.4156 0.0238  0.0578  0.1356  80  LYS   A NZ  
527  N  N   . ALA   A 81  ? 0.2014 0.1157 0.3009 0.0013  -0.0443 -0.0014 81  ALA   A N   
528  C  CA  . ALA   A 81  ? 0.2075 0.1351 0.3299 -0.0030 -0.0192 -0.0456 81  ALA   A CA  
529  C  C   . ALA   A 81  ? 0.2130 0.1376 0.3091 -0.0108 -0.0338 -0.0052 81  ALA   A C   
530  O  O   . ALA   A 81  ? 0.2615 0.1450 0.3901 0.0278  -0.0830 -0.0428 81  ALA   A O   
531  C  CB  . ALA   A 81  ? 0.3001 0.1925 0.3022 -0.0070 -0.0459 -0.0034 81  ALA   A CB  
532  N  N   . LEU   A 82  ? 0.1966 0.1300 0.2833 0.0073  -0.0132 -0.0066 82  LEU   A N   
533  C  CA  . LEU   A 82  ? 0.1869 0.1320 0.3004 0.0036  -0.0140 0.0186  82  LEU   A CA  
534  C  C   . LEU   A 82  ? 0.1758 0.1113 0.3258 0.0271  -0.0196 0.0179  82  LEU   A C   
535  O  O   . LEU   A 82  ? 0.1983 0.1589 0.3606 0.0319  0.0049  0.0275  82  LEU   A O   
536  C  CB  . LEU   A 82  ? 0.1862 0.1536 0.3226 0.0089  0.0144  0.0052  82  LEU   A CB  
537  C  CG  . LEU   A 82  ? 0.2196 0.1399 0.3271 0.0073  0.0214  0.0238  82  LEU   A CG  
538  C  CD1 . LEU   A 82  ? 0.3533 0.1541 0.3864 -0.0448 0.1144  -0.0006 82  LEU   A CD1 
539  C  CD2 . LEU   A 82  ? 0.3884 0.2049 0.3778 0.0271  0.1500  -0.0478 82  LEU   A CD2 
540  N  N   . GLY   A 83  ? 0.1812 0.1006 0.3061 0.0121  -0.0125 0.0053  83  GLY   A N   
541  C  CA  . GLY   A 83  ? 0.2169 0.1232 0.2981 0.0249  -0.0137 0.0027  83  GLY   A CA  
542  C  C   . GLY   A 83  ? 0.1614 0.1251 0.2812 0.0116  -0.0163 0.0263  83  GLY   A C   
543  O  O   . GLY   A 83  ? 0.2155 0.0983 0.2963 0.0033  -0.0307 0.0258  83  GLY   A O   
544  N  N   . ILE   A 84  ? 0.1681 0.1082 0.2655 0.0215  -0.0150 0.0091  84  ILE   A N   
545  C  CA  . ILE   A 84  ? 0.1755 0.1012 0.2795 0.0081  -0.0149 0.0208  84  ILE   A CA  
546  C  C   . ILE   A 84  ? 0.1672 0.1124 0.2772 0.0005  -0.0293 -0.0123 84  ILE   A C   
547  O  O   . ILE   A 84  ? 0.1536 0.1418 0.2802 0.0155  -0.0129 0.0053  84  ILE   A O   
548  C  CB  . ILE   A 84  ? 0.1774 0.1498 0.2779 -0.0008 -0.0158 -0.0110 84  ILE   A CB  
549  C  CG1 . ILE   A 84  ? 0.1860 0.2036 0.4436 -0.0293 0.0159  -0.0755 84  ILE   A CG1 
550  C  CG2 . ILE   A 84  ? 0.2238 0.1544 0.2806 -0.0524 -0.0105 -0.0252 84  ILE   A CG2 
551  C  CD1 . ILE   A 84  ? 0.2807 0.2295 0.4748 0.0440  0.0246  0.0684  84  ILE   A CD1 
552  N  N   . SER   A 85  ? 0.2022 0.1157 0.2564 0.0102  -0.0125 0.0225  85  SER   A N   
553  C  CA  . SER   A 85  ? 0.2270 0.1226 0.2786 0.0250  -0.0137 0.0122  85  SER   A CA  
554  C  C   . SER   A 85  ? 0.2005 0.1269 0.2520 -0.0048 -0.0021 0.0248  85  SER   A C   
555  O  O   . SER   A 85  ? 0.2728 0.1249 0.2647 0.0010  -0.0114 0.0256  85  SER   A O   
556  C  CB  . SER   A 85  ? 0.2695 0.1332 0.3095 -0.0359 0.0197  0.0660  85  SER   A CB  
557  O  OG  . SER   A 85  ? 0.2699 0.1446 0.3346 -0.0101 0.0432  0.0459  85  SER   A OG  
558  N  N   . PRO   A 86  ? 0.1659 0.1208 0.2303 0.0040  0.0082  0.0212  86  PRO   A N   
559  C  CA  . PRO   A 86  ? 0.1433 0.1234 0.2482 -0.0004 0.0096  0.0190  86  PRO   A CA  
560  C  C   . PRO   A 86  ? 0.1104 0.1555 0.2511 0.0160  0.0308  0.0525  86  PRO   A C   
561  O  O   . PRO   A 86  ? 0.1583 0.1548 0.2578 0.0031  0.0243  -0.0017 86  PRO   A O   
562  C  CB  . PRO   A 86  ? 0.1352 0.1360 0.2327 0.0133  0.0084  0.0052  86  PRO   A CB  
563  C  CG  . PRO   A 86  ? 0.1413 0.1117 0.2527 0.0211  0.0147  0.0040  86  PRO   A CG  
564  C  CD  . PRO   A 86  ? 0.1507 0.1312 0.2580 0.0012  -0.0009 -0.0087 86  PRO   A CD  
565  N  N   . PHE   A 87  ? 0.1152 0.1295 0.2468 0.0211  0.0142  0.0260  87  PHE   A N   
566  C  CA  . PHE   A 87  ? 0.1191 0.1569 0.2170 0.0371  0.0081  -0.0062 87  PHE   A CA  
567  C  C   . PHE   A 87  ? 0.1165 0.1538 0.1955 0.0095  0.0120  -0.0176 87  PHE   A C   
568  O  O   . PHE   A 87  ? 0.1247 0.1625 0.2352 0.0146  0.0229  0.0030  87  PHE   A O   
569  C  CB  . PHE   A 87  ? 0.1265 0.1825 0.2144 0.0313  0.0040  -0.0059 87  PHE   A CB  
570  C  CG  . PHE   A 87  ? 0.1046 0.2845 0.2518 0.0325  -0.0024 -0.0334 87  PHE   A CG  
571  C  CD1 . PHE   A 87  ? 0.1701 0.2930 0.2680 -0.0112 0.0388  -0.0515 87  PHE   A CD1 
572  C  CD2 . PHE   A 87  ? 0.1501 0.2480 0.3013 0.0605  -0.0367 -0.0804 87  PHE   A CD2 
573  C  CE1 . PHE   A 87  ? 0.1634 0.4489 0.3123 -0.0619 0.0337  -0.1711 87  PHE   A CE1 
574  C  CE2 . PHE   A 87  ? 0.1975 0.3749 0.4631 0.0443  -0.0459 -0.2183 87  PHE   A CE2 
575  C  CZ  . PHE   A 87  ? 0.1624 0.4215 0.4934 -0.0037 0.0439  -0.2822 87  PHE   A CZ  
576  N  N   . HIS   A 88  ? 0.1123 0.1656 0.2018 0.0379  0.0110  0.0082  88  HIS   A N   
577  C  CA  . HIS   A 88  ? 0.1251 0.1437 0.2187 0.0289  -0.0041 -0.0017 88  HIS   A CA  
578  C  C   . HIS   A 88  ? 0.1194 0.1154 0.2262 0.0189  0.0083  0.0002  88  HIS   A C   
579  O  O   . HIS   A 88  ? 0.1531 0.1289 0.2428 0.0234  -0.0083 -0.0027 88  HIS   A O   
580  C  CB  . HIS   A 88  ? 0.1332 0.1330 0.2264 0.0216  -0.0118 -0.0084 88  HIS   A CB  
581  C  CG  . HIS   A 88  ? 0.1221 0.1409 0.3064 0.0208  -0.0106 -0.0456 88  HIS   A CG  
582  N  ND1 . HIS   A 88  ? 0.1165 0.1447 0.2782 0.0253  0.0063  -0.0061 88  HIS   A ND1 
583  C  CD2 . HIS   A 88  ? 0.1335 0.2228 0.4729 0.0501  -0.0375 -0.1720 88  HIS   A CD2 
584  C  CE1 . HIS   A 88  ? 0.1476 0.1748 0.3813 0.0350  -0.0281 -0.0795 88  HIS   A CE1 
585  N  NE2 . HIS   A 88  ? 0.1239 0.2562 0.5357 0.0355  -0.0555 -0.2078 88  HIS   A NE2 
586  N  N   . GLU   A 89  ? 0.1101 0.1419 0.2208 0.0189  -0.0087 0.0099  89  GLU   A N   
587  C  CA  . GLU   A 89  ? 0.1358 0.1247 0.2411 0.0032  -0.0208 0.0181  89  GLU   A CA  
588  C  C   . GLU   A 89  ? 0.1834 0.1740 0.2104 0.0258  -0.0221 0.0266  89  GLU   A C   
589  O  O   . GLU   A 89  ? 0.2591 0.1641 0.2583 0.0128  -0.0519 0.0083  89  GLU   A O   
590  C  CB  . GLU   A 89  ? 0.1005 0.2069 0.2780 0.0002  -0.0102 0.0251  89  GLU   A CB  
591  C  CG  . GLU   A 89  ? 0.1490 0.2717 0.2889 -0.0123 0.0195  0.0074  89  GLU   A CG  
592  C  CD  . GLU   A 89  ? 0.2111 0.3151 0.2831 -0.0274 0.0068  0.0628  89  GLU   A CD  
593  O  OE1 . GLU   A 89  ? 0.2393 0.2673 0.4434 -0.0464 -0.0303 0.0123  89  GLU   A OE1 
594  O  OE2 . GLU   A 89  ? 0.2206 0.2666 0.3211 -0.0208 0.0462  0.0361  89  GLU   A OE2 
595  N  N   . HIS   A 90  ? 0.1723 0.1463 0.2214 0.0275  -0.0064 0.0206  90  HIS   A N   
596  C  CA  . HIS   A 90  ? 0.1596 0.1503 0.2121 0.0219  -0.0233 0.0136  90  HIS   A CA  
597  C  C   . HIS   A 90  ? 0.2275 0.1550 0.1874 0.0396  -0.0403 -0.0193 90  HIS   A C   
598  O  O   . HIS   A 90  ? 0.3133 0.1624 0.2084 -0.0059 -0.0298 0.0090  90  HIS   A O   
599  C  CB  . HIS   A 90  ? 0.1760 0.2255 0.2424 0.0433  -0.0123 0.0497  90  HIS   A CB  
600  C  CG  . HIS   A 90  ? 0.2103 0.3335 0.3414 0.1363  -0.0076 0.0832  90  HIS   A CG  
601  N  ND1 . HIS   A 90  ? 0.3240 0.5178 0.3461 0.1346  -0.0240 0.0326  90  HIS   A ND1 
602  C  CD2 . HIS   A 90  ? 0.3913 0.2786 0.6118 0.1009  0.1682  -0.0940 90  HIS   A CD2 
603  C  CE1 . HIS   A 90  ? 0.2662 0.2699 0.6289 0.0588  0.0912  -0.0086 90  HIS   A CE1 
604  N  NE2 . HIS   A 90  ? 0.4218 0.2277 0.5662 0.0687  0.1908  0.0365  90  HIS   A NE2 
605  N  N   . ALA   A 91  ? 0.2211 0.1661 0.2057 0.0018  -0.0537 0.0052  91  ALA   A N   
606  C  CA  . ALA   A 91  ? 0.3167 0.1436 0.2047 -0.0420 -0.0748 0.0065  91  ALA   A CA  
607  C  C   . ALA   A 91  ? 0.3195 0.1514 0.2126 -0.0252 -0.0582 -0.0042 91  ALA   A C   
608  O  O   . ALA   A 91  ? 0.2960 0.1426 0.2333 0.0442  -0.0713 -0.0184 91  ALA   A O   
609  C  CB  . ALA   A 91  ? 0.2935 0.1870 0.2728 -0.0346 -0.0568 0.0080  91  ALA   A CB  
610  N  N   . GLU   A 92  ? 0.3639 0.1480 0.2200 0.0344  -0.0595 0.0118  92  GLU   A N   
611  C  CA  . GLU   A 92  ? 0.4006 0.1386 0.2689 0.0333  -0.0594 0.0172  92  GLU   A CA  
612  C  C   . GLU   A 92  ? 0.3801 0.1430 0.2721 -0.0071 -0.1010 -0.0123 92  GLU   A C   
613  O  O   . GLU   A 92  ? 0.6953 0.1665 0.3543 -0.0216 -0.2388 0.0076  92  GLU   A O   
614  C  CB  . GLU   A 92  ? 0.3267 0.2874 0.4279 -0.0128 0.0184  0.0767  92  GLU   A CB  
615  N  N   . VAL   A 93  ? 0.2196 0.1589 0.2411 0.0399  -0.0449 0.0051  93  VAL   A N   
616  C  CA  . VAL   A 93  ? 0.1637 0.2345 0.2108 0.0257  -0.0436 0.0125  93  VAL   A CA  
617  C  C   . VAL   A 93  ? 0.1539 0.1387 0.2431 -0.0288 -0.0656 -0.0077 93  VAL   A C   
618  O  O   . VAL   A 93  ? 0.1897 0.1170 0.2683 0.0069  -0.0741 -0.0317 93  VAL   A O   
619  C  CB  . VAL   A 93  ? 0.1515 0.2117 0.2988 -0.0123 -0.0420 -0.0332 93  VAL   A CB  
620  C  CG1 . VAL   A 93  ? 0.2964 0.2312 0.3021 -0.0946 0.0436  -0.0789 93  VAL   A CG1 
621  C  CG2 . VAL   A 93  ? 0.2366 0.3433 0.3127 0.1267  -0.0318 -0.0477 93  VAL   A CG2 
622  N  N   . VAL   A 94  ? 0.1418 0.1509 0.2074 -0.0284 -0.0531 0.0035  94  VAL   A N   
623  C  CA  . VAL   A 94  ? 0.1192 0.1552 0.2291 -0.0168 -0.0205 0.0117  94  VAL   A CA  
624  C  C   . VAL   A 94  ? 0.0992 0.1501 0.2203 0.0013  -0.0255 -0.0121 94  VAL   A C   
625  O  O   . VAL   A 94  ? 0.1340 0.1335 0.2236 -0.0140 -0.0309 -0.0068 94  VAL   A O   
626  C  CB  . VAL   A 94  ? 0.1533 0.1774 0.2316 -0.0441 -0.0088 -0.0339 94  VAL   A CB  
627  C  CG1 . VAL   A 94  ? 0.1398 0.2360 0.2909 -0.0020 0.0013  -0.0443 94  VAL   A CG1 
628  C  CG2 . VAL   A 94  ? 0.2367 0.1746 0.2746 -0.0707 0.0147  -0.0508 94  VAL   A CG2 
629  N  N   . PHE   A 95  ? 0.1173 0.1413 0.2320 -0.0094 -0.0335 -0.0074 95  PHE   A N   
630  C  CA  . PHE   A 95  ? 0.1213 0.1199 0.2233 -0.0020 -0.0406 -0.0127 95  PHE   A CA  
631  C  C   . PHE   A 95  ? 0.1487 0.1307 0.2079 -0.0239 -0.0255 -0.0177 95  PHE   A C   
632  O  O   . PHE   A 95  ? 0.1422 0.1342 0.2578 -0.0060 -0.0547 -0.0084 95  PHE   A O   
633  C  CB  . PHE   A 95  ? 0.1218 0.1481 0.2253 -0.0102 -0.0426 -0.0060 95  PHE   A CB  
634  C  CG  . PHE   A 95  ? 0.0887 0.2312 0.2624 -0.0023 -0.0151 -0.0313 95  PHE   A CG  
635  C  CD1 . PHE   A 95  ? 0.2042 0.2103 0.3440 -0.0686 0.0510  -0.1036 95  PHE   A CD1 
636  C  CD2 . PHE   A 95  ? 0.1579 0.2627 0.2425 0.0327  -0.0396 -0.0554 95  PHE   A CD2 
637  C  CE1 . PHE   A 95  ? 0.1622 0.3323 0.3963 -0.0626 0.0538  -0.1643 95  PHE   A CE1 
638  C  CE2 . PHE   A 95  ? 0.1728 0.4204 0.2833 0.0953  -0.0417 -0.0791 95  PHE   A CE2 
639  C  CZ  . PHE   A 95  ? 0.1228 0.4974 0.2949 0.0200  -0.0133 -0.1806 95  PHE   A CZ  
640  N  N   . THR   A 96  ? 0.1388 0.1225 0.2501 -0.0045 -0.0515 -0.0180 96  THR   A N   
641  C  CA  . THR   A 96  ? 0.1517 0.1244 0.2396 -0.0051 -0.0467 0.0150  96  THR   A CA  
642  C  C   . THR   A 96  ? 0.1501 0.1463 0.2540 -0.0023 -0.0563 0.0012  96  THR   A C   
643  O  O   . THR   A 96  ? 0.1494 0.3159 0.2511 -0.0460 -0.0638 0.0136  96  THR   A O   
644  C  CB  . THR   A 96  ? 0.1816 0.1457 0.2739 0.0164  -0.0379 -0.0035 96  THR   A CB  
645  O  OG1 . THR   A 96  ? 0.2489 0.1731 0.3051 0.0340  -0.0494 -0.0153 96  THR   A OG1 
646  C  CG2 . THR   A 96  ? 0.3112 0.1538 0.3533 0.0186  -0.1066 0.0305  96  THR   A CG2 
647  N  N   . ALA   A 97  ? 0.1530 0.1750 0.2489 0.0013  -0.0672 0.0054  97  ALA   A N   
648  C  CA  . ALA   A 97  ? 0.1932 0.1491 0.2483 0.0003  -0.0652 0.0092  97  ALA   A CA  
649  C  C   . ALA   A 97  ? 0.1437 0.2034 0.2622 0.0225  -0.0560 0.0134  97  ALA   A C   
650  O  O   . ALA   A 97  ? 0.1334 0.2777 0.3048 0.0081  -0.0521 0.0611  97  ALA   A O   
651  C  CB  . ALA   A 97  ? 0.3644 0.1574 0.2595 -0.0515 -0.0725 -0.0133 97  ALA   A CB  
652  N  N   . ASN   A 98  ? 0.1529 0.1869 0.2793 0.0218  -0.0545 0.0405  98  ASN   A N   
653  C  CA  . ASN   A 98  ? 0.1799 0.1771 0.3309 0.0390  -0.0701 0.0535  98  ASN   A CA  
654  C  C   . ASN   A 98  ? 0.2171 0.1911 0.3569 0.0788  -0.0044 0.0592  98  ASN   A C   
655  O  O   . ASN   A 98  ? 0.3091 0.2147 0.4617 0.1117  -0.0389 0.0757  98  ASN   A O   
656  C  CB  . ASN   A 98  ? 0.2098 0.2321 0.3433 0.0537  -0.0678 0.0514  98  ASN   A CB  
657  C  CG  . ASN   A 98  ? 0.2256 0.2246 0.2432 0.0020  -0.0701 0.0476  98  ASN   A CG  
658  O  OD1 . ASN   A 98  ? 0.3043 0.2272 0.3353 -0.0588 -0.0951 0.0029  98  ASN   A OD1 
659  N  ND2 . ASN   A 98  ? 0.2257 0.1701 0.2833 0.0417  -0.0594 0.0372  98  ASN   A ND2 
660  N  N   . ASP   A 99  ? 0.2574 0.1881 0.3469 0.0690  -0.0323 0.0290  99  ASP   A N   
661  C  CA  . ASP   A 99  ? 0.2770 0.1956 0.3764 0.0441  -0.0287 0.0229  99  ASP   A CA  
662  C  C   . ASP   A 99  ? 0.3067 0.2319 0.4529 0.0668  0.0096  0.0246  99  ASP   A C   
663  O  O   . ASP   A 99  ? 0.3828 0.1787 0.5990 0.0402  0.0205  -0.0123 99  ASP   A O   
664  C  CB  . ASP   A 99  ? 0.3254 0.2569 0.3561 0.0368  -0.0049 0.0082  99  ASP   A CB  
665  N  N   . SER   A 100 ? 0.3981 0.1861 0.4794 0.0143  0.0704  0.0145  100 SER   A N   
666  C  CA  . SER   A 100 ? 0.4308 0.2413 0.5215 -0.0388 0.0607  0.0498  100 SER   A CA  
667  C  C   . SER   A 100 ? 0.4133 0.2285 0.5158 -0.0116 0.0071  0.0606  100 SER   A C   
668  O  O   . SER   A 100 ? 0.6366 0.4084 0.7985 -0.1890 0.0817  0.1274  100 SER   A O   
669  C  CB  . SER   A 100 ? 0.4066 0.3825 0.4686 -0.0765 0.0610  0.0314  100 SER   A CB  
670  O  OG  . SER   A 100 ? 0.4419 0.2243 0.7859 -0.0593 -0.0034 0.0824  100 SER   A OG  
671  N  N   . GLY   A 101 ? 0.3400 0.1852 0.4510 0.0649  0.0231  0.0406  101 GLY   A N   
672  C  CA  . GLY   A 101 ? 0.2651 0.1745 0.4370 0.0379  -0.0376 0.0689  101 GLY   A CA  
673  C  C   . GLY   A 101 ? 0.2409 0.1926 0.3829 0.0302  -0.0508 0.0774  101 GLY   A C   
674  O  O   . GLY   A 101 ? 0.2791 0.1924 0.3974 0.0430  -0.0515 0.0670  101 GLY   A O   
675  N  N   . PRO   A 102 ? 0.2340 0.2063 0.3854 0.0033  -0.0902 0.0990  102 PRO   A N   
676  C  CA  . PRO   A 102 ? 0.2274 0.1818 0.3809 -0.0037 -0.0829 0.0499  102 PRO   A CA  
677  C  C   . PRO   A 102 ? 0.2160 0.1761 0.3938 -0.0147 -0.0955 0.0851  102 PRO   A C   
678  O  O   . PRO   A 102 ? 0.2267 0.1979 0.4039 -0.0022 -0.0559 0.1064  102 PRO   A O   
679  C  CB  . PRO   A 102 ? 0.2997 0.2019 0.3869 0.0130  -0.1247 0.0563  102 PRO   A CB  
680  C  CG  . PRO   A 102 ? 0.4381 0.2967 0.4570 0.0659  -0.1502 0.1142  102 PRO   A CG  
681  C  CD  . PRO   A 102 ? 0.2813 0.2351 0.3940 0.0726  -0.1082 0.0988  102 PRO   A CD  
682  N  N   . ARG   A 103 ? 0.2005 0.1617 0.3440 -0.0017 -0.0799 0.0709  103 ARG   A N   
683  C  CA  . ARG   A 103 ? 0.1682 0.1539 0.3048 -0.0104 -0.0487 0.0537  103 ARG   A CA  
684  C  C   . ARG   A 103 ? 0.1877 0.1645 0.2910 -0.0226 -0.0790 0.0554  103 ARG   A C   
685  O  O   . ARG   A 103 ? 0.2306 0.1709 0.3110 -0.0074 -0.0854 0.0461  103 ARG   A O   
686  C  CB  . ARG   A 103 ? 0.1902 0.1639 0.3389 0.0038  -0.0935 0.0491  103 ARG   A CB  
687  C  CG  . ARG   A 103 ? 0.2549 0.1387 0.3389 -0.0102 -0.0667 0.0287  103 ARG   A CG  
688  C  CD  . ARG   A 103 ? 0.3074 0.1703 0.3961 -0.0230 -0.0401 0.0454  103 ARG   A CD  
689  N  NE  . ARG   A 103 ? 0.3273 0.1902 0.5787 -0.0406 -0.0513 0.0253  103 ARG   A NE  
690  C  CZ  . ARG   A 103 ? 0.3464 0.1948 0.6597 -0.0585 -0.0981 0.0141  103 ARG   A CZ  
691  N  NH1 . ARG   A 103 ? 0.3113 0.1653 0.6190 -0.0260 -0.0489 0.0329  103 ARG   A NH1 
692  N  NH2 . ARG   A 103 ? 0.3400 0.2113 0.7383 -0.0288 -0.0880 -0.0137 103 ARG   A NH2 
693  N  N   . ARG   A 104 ? 0.1951 0.1775 0.2565 -0.0093 -0.0625 0.0682  104 ARG   A N   
694  C  CA  . ARG   A 104 ? 0.2492 0.1410 0.2524 -0.0130 -0.0668 0.0140  104 ARG   A CA  
695  C  C   . ARG   A 104 ? 0.1780 0.1357 0.2345 -0.0104 -0.0464 0.0248  104 ARG   A C   
696  O  O   . ARG   A 104 ? 0.2040 0.1625 0.2851 -0.0420 -0.0605 0.0673  104 ARG   A O   
697  C  CB  . ARG   A 104 ? 0.3164 0.2095 0.2284 0.0270  -0.0320 0.0011  104 ARG   A CB  
698  C  CG  . ARG   A 104 ? 0.5666 0.3329 0.2700 0.0333  -0.0301 0.0339  104 ARG   A CG  
699  C  CD  . ARG   A 104 ? 0.5062 0.5368 0.3085 0.0103  -0.0330 -0.0401 104 ARG   A CD  
700  N  N   . TYR   A 105 ? 0.1605 0.1496 0.2388 -0.0209 -0.0544 0.0296  105 TYR   A N   
701  C  CA  . TYR   A 105 ? 0.1674 0.1288 0.2305 -0.0124 -0.0421 0.0070  105 TYR   A CA  
702  C  C   . TYR   A 105 ? 0.1599 0.1312 0.2276 -0.0218 -0.0560 0.0135  105 TYR   A C   
703  O  O   . TYR   A 105 ? 0.1945 0.1384 0.2897 0.0015  -0.1012 0.0138  105 TYR   A O   
704  C  CB  . TYR   A 105 ? 0.1781 0.1506 0.2377 -0.0140 -0.0335 0.0420  105 TYR   A CB  
705  C  CG  . TYR   A 105 ? 0.1515 0.1272 0.2944 -0.0114 -0.0509 0.0314  105 TYR   A CG  
706  C  CD1 . TYR   A 105 ? 0.1573 0.1632 0.2677 -0.0006 -0.0610 0.0005  105 TYR   A CD1 
707  C  CD2 . TYR   A 105 ? 0.1529 0.1844 0.2807 0.0023  -0.0372 0.0178  105 TYR   A CD2 
708  C  CE1 . TYR   A 105 ? 0.1493 0.1671 0.3065 0.0160  -0.0721 -0.0186 105 TYR   A CE1 
709  C  CE2 . TYR   A 105 ? 0.1669 0.1921 0.2535 0.0114  -0.0475 0.0105  105 TYR   A CE2 
710  C  CZ  . TYR   A 105 ? 0.1424 0.1416 0.2973 -0.0014 -0.0398 0.0076  105 TYR   A CZ  
711  O  OH  . TYR   A 105 ? 0.1604 0.1500 0.3121 0.0121  -0.0557 0.0014  105 TYR   A OH  
712  N  N   . THR   A 106 ? 0.1633 0.1211 0.2188 -0.0246 -0.0462 0.0147  106 THR   A N   
713  C  CA  . THR   A 106 ? 0.1794 0.1229 0.2216 0.0060  -0.0132 0.0250  106 THR   A CA  
714  C  C   . THR   A 106 ? 0.1862 0.1021 0.2159 -0.0026 -0.0322 0.0151  106 THR   A C   
715  O  O   . THR   A 106 ? 0.1974 0.1408 0.2381 -0.0220 -0.0573 0.0139  106 THR   A O   
716  C  CB  . THR   A 106 ? 0.1911 0.1949 0.2514 0.0043  -0.0058 -0.0070 106 THR   A CB  
717  O  OG1 . THR   A 106 ? 0.2162 0.3932 0.2894 0.0361  0.0324  0.0147  106 THR   A OG1 
718  C  CG2 . THR   A 106 ? 0.2454 0.2135 0.3434 0.0672  -0.0259 -0.0216 106 THR   A CG2 
719  N  N   . ILE   A 107 ? 0.1763 0.1135 0.2082 0.0193  -0.0411 0.0223  107 ILE   A N   
720  C  CA  . ILE   A 107 ? 0.2199 0.0944 0.2145 0.0026  -0.0386 0.0119  107 ILE   A CA  
721  C  C   . ILE   A 107 ? 0.2203 0.0956 0.2036 -0.0101 -0.0355 -0.0094 107 ILE   A C   
722  O  O   . ILE   A 107 ? 0.2305 0.1136 0.2356 0.0140  -0.0629 -0.0176 107 ILE   A O   
723  C  CB  . ILE   A 107 ? 0.2102 0.1330 0.2489 0.0016  -0.0049 -0.0350 107 ILE   A CB  
724  C  CG1 . ILE   A 107 ? 0.2572 0.1673 0.3285 -0.0043 -0.0162 -0.0331 107 ILE   A CG1 
725  C  CG2 . ILE   A 107 ? 0.2645 0.2139 0.2641 -0.0094 0.0338  0.0054  107 ILE   A CG2 
726  C  CD1 . ILE   A 107 ? 0.2355 0.1439 0.4275 0.0103  -0.0397 -0.0251 107 ILE   A CD1 
727  N  N   . ALA   A 108 ? 0.1992 0.1036 0.2039 0.0007  -0.0244 -0.0085 108 ALA   A N   
728  C  CA  . ALA   A 108 ? 0.2151 0.1297 0.2012 0.0173  -0.0227 0.0024  108 ALA   A CA  
729  C  C   . ALA   A 108 ? 0.1905 0.1204 0.2059 0.0406  -0.0120 -0.0351 108 ALA   A C   
730  O  O   . ALA   A 108 ? 0.3452 0.1167 0.2036 0.0325  -0.0019 -0.0023 108 ALA   A O   
731  C  CB  . ALA   A 108 ? 0.1846 0.1956 0.2587 0.0256  -0.0119 0.0013  108 ALA   A CB  
732  N  N   . ALA   A 109 ? 0.1726 0.1136 0.1839 0.0413  -0.0286 -0.0079 109 ALA   A N   
733  C  CA  . ALA   A 109 ? 0.1326 0.1247 0.2027 0.0479  -0.0305 -0.0213 109 ALA   A CA  
734  C  C   . ALA   A 109 ? 0.1362 0.1168 0.1806 0.0296  -0.0193 0.0040  109 ALA   A C   
735  O  O   . ALA   A 109 ? 0.1999 0.1538 0.1942 0.0695  -0.0192 -0.0266 109 ALA   A O   
736  C  CB  . ALA   A 109 ? 0.1240 0.1488 0.2693 0.0238  -0.0201 -0.0004 109 ALA   A CB  
737  N  N   . LEU   A 110 ? 0.1219 0.1149 0.1804 0.0331  -0.0105 0.0024  110 LEU   A N   
738  C  CA  . LEU   A 110 ? 0.1090 0.1302 0.1821 0.0255  -0.0102 0.0085  110 LEU   A CA  
739  C  C   . LEU   A 110 ? 0.1424 0.1170 0.1726 0.0333  -0.0052 -0.0015 110 LEU   A C   
740  O  O   . LEU   A 110 ? 0.1722 0.1129 0.1932 -0.0008 0.0068  0.0006  110 LEU   A O   
741  C  CB  . LEU   A 110 ? 0.1306 0.1372 0.2197 -0.0015 -0.0168 0.0110  110 LEU   A CB  
742  C  CG  . LEU   A 110 ? 0.1376 0.1625 0.2616 0.0229  -0.0192 0.0360  110 LEU   A CG  
743  C  CD1 . LEU   A 110 ? 0.1698 0.2113 0.2381 0.0345  0.0287  0.0511  110 LEU   A CD1 
744  C  CD2 . LEU   A 110 ? 0.1532 0.2890 0.3485 0.0006  -0.0789 -0.0434 110 LEU   A CD2 
745  N  N   . LEU   A 111 ? 0.1057 0.1184 0.1842 0.0252  0.0131  -0.0019 111 LEU   A N   
746  C  CA  . LEU   A 111 ? 0.1026 0.1415 0.1808 0.0196  0.0166  0.0026  111 LEU   A CA  
747  C  C   . LEU   A 111 ? 0.1053 0.1077 0.1919 0.0123  0.0029  -0.0233 111 LEU   A C   
748  O  O   . LEU   A 111 ? 0.1103 0.1158 0.1885 0.0067  0.0142  -0.0042 111 LEU   A O   
749  C  CB  . LEU   A 111 ? 0.1049 0.1547 0.1907 0.0109  0.0049  0.0168  111 LEU   A CB  
750  C  CG  . LEU   A 111 ? 0.1128 0.1307 0.2216 0.0231  -0.0007 0.0223  111 LEU   A CG  
751  C  CD1 . LEU   A 111 ? 0.1285 0.1635 0.2457 0.0022  -0.0233 0.0063  111 LEU   A CD1 
752  C  CD2 . LEU   A 111 ? 0.1361 0.1353 0.2511 0.0257  -0.0054 0.0270  111 LEU   A CD2 
753  N  N   . SER   A 112 ? 0.1157 0.1154 0.1755 0.0149  0.0113  -0.0010 112 SER   A N   
754  C  CA  . SER   A 112 ? 0.1109 0.1215 0.1872 0.0252  0.0087  0.0093  112 SER   A CA  
755  C  C   . SER   A 112 ? 0.0951 0.0875 0.1931 0.0219  0.0205  0.0073  112 SER   A C   
756  O  O   . SER   A 112 ? 0.1133 0.1066 0.2175 0.0175  0.0142  -0.0032 112 SER   A O   
757  C  CB  . SER   A 112 ? 0.0994 0.1457 0.1969 0.0034  -0.0027 0.0250  112 SER   A CB  
758  O  OG  . SER   A 112 ? 0.1228 0.1827 0.2373 -0.0107 -0.0026 0.0152  112 SER   A OG  
759  N  N   . PRO   A 113 ? 0.1027 0.1086 0.1945 0.0218  0.0034  0.0161  113 PRO   A N   
760  C  CA  . PRO   A 113 ? 0.0963 0.1274 0.2044 0.0066  0.0140  0.0096  113 PRO   A CA  
761  C  C   . PRO   A 113 ? 0.0884 0.1148 0.1991 0.0135  0.0055  0.0156  113 PRO   A C   
762  O  O   . PRO   A 113 ? 0.0978 0.1519 0.2295 0.0090  0.0185  0.0025  113 PRO   A O   
763  C  CB  . PRO   A 113 ? 0.1483 0.1018 0.2237 -0.0029 0.0271  0.0101  113 PRO   A CB  
764  C  CG  . PRO   A 113 ? 0.1839 0.1064 0.2262 0.0312  0.0154  0.0132  113 PRO   A CG  
765  C  CD  . PRO   A 113 ? 0.1230 0.1105 0.2116 0.0286  0.0194  0.0013  113 PRO   A CD  
766  N  N   . TYR   A 114 ? 0.0985 0.1095 0.2009 0.0144  0.0094  0.0051  114 TYR   A N   
767  C  CA  . TYR   A 114 ? 0.1329 0.1056 0.1903 0.0268  0.0074  0.0242  114 TYR   A CA  
768  C  C   . TYR   A 114 ? 0.1255 0.1109 0.2073 0.0291  0.0121  0.0057  114 TYR   A C   
769  O  O   . TYR   A 114 ? 0.1993 0.1195 0.2051 0.0264  0.0356  0.0013  114 TYR   A O   
770  C  CB  . TYR   A 114 ? 0.1252 0.1482 0.1883 0.0190  0.0124  0.0021  114 TYR   A CB  
771  C  CG  . TYR   A 114 ? 0.1536 0.1041 0.1984 0.0169  -0.0030 0.0186  114 TYR   A CG  
772  C  CD1 . TYR   A 114 ? 0.3705 0.1204 0.2204 0.0218  0.0536  0.0167  114 TYR   A CD1 
773  C  CD2 . TYR   A 114 ? 0.1371 0.1566 0.2130 0.0152  0.0174  0.0190  114 TYR   A CD2 
774  C  CE1 . TYR   A 114 ? 0.5674 0.1151 0.2770 -0.0611 0.0789  0.0163  114 TYR   A CE1 
775  C  CE2 . TYR   A 114 ? 0.2016 0.2045 0.2565 -0.0154 -0.0160 0.0462  114 TYR   A CE2 
776  C  CZ  . TYR   A 114 ? 0.3842 0.1984 0.2736 -0.0930 0.0507  0.0551  114 TYR   A CZ  
777  O  OH  . TYR   A 114 ? 0.5930 0.3068 0.3264 -0.2438 -0.0186 0.0774  114 TYR   A OH  
778  N  N   . SER   A 115 ? 0.1584 0.0889 0.2036 0.0383  0.0366  0.0197  115 SER   A N   
779  C  CA  . SER   A 115 ? 0.1189 0.0982 0.2001 0.0313  0.0176  -0.0093 115 SER   A CA  
780  C  C   . SER   A 115 ? 0.1679 0.0878 0.2040 0.0181  0.0046  0.0201  115 SER   A C   
781  O  O   . SER   A 115 ? 0.2163 0.1178 0.1902 0.0311  0.0342  -0.0097 115 SER   A O   
782  C  CB  . SER   A 115 ? 0.1324 0.1320 0.2226 0.0254  0.0227  -0.0137 115 SER   A CB  
783  O  OG  . SER   A 115 ? 0.1642 0.1700 0.3130 -0.0076 0.0178  -0.0238 115 SER   A OG  
784  N  N   . TYR   A 116 ? 0.1589 0.1007 0.2013 0.0005  0.0304  0.0131  116 TYR   A N   
785  C  CA  . TYR   A 116 ? 0.1791 0.0825 0.2171 0.0251  0.0270  0.0052  116 TYR   A CA  
786  C  C   . TYR   A 116 ? 0.1494 0.1133 0.1679 0.0282  -0.0027 0.0079  116 TYR   A C   
787  O  O   . TYR   A 116 ? 0.1648 0.1225 0.1756 0.0033  0.0063  -0.0107 116 TYR   A O   
788  C  CB  . TYR   A 116 ? 0.2294 0.1194 0.2148 -0.0156 -0.0195 -0.0094 116 TYR   A CB  
789  C  CG  . TYR   A 116 ? 0.1595 0.1605 0.2513 -0.0340 -0.0068 -0.0088 116 TYR   A CG  
790  C  CD1 . TYR   A 116 ? 0.1600 0.1547 0.3255 0.0131  -0.0162 -0.0134 116 TYR   A CD1 
791  C  CD2 . TYR   A 116 ? 0.1806 0.2247 0.2960 -0.0541 0.0092  -0.0207 116 TYR   A CD2 
792  C  CE1 . TYR   A 116 ? 0.1568 0.2572 0.4572 0.0393  -0.0334 -0.0624 116 TYR   A CE1 
793  C  CE2 . TYR   A 116 ? 0.1409 0.3476 0.2811 -0.0301 0.0169  -0.0441 116 TYR   A CE2 
794  C  CZ  . TYR   A 116 ? 0.1678 0.3831 0.4412 0.0442  0.0407  -0.1189 116 TYR   A CZ  
795  O  OH  . TYR   A 116 ? 0.2309 0.2685 0.6673 -0.0094 0.0446  0.0131  116 TYR   A OH  
796  N  N   . SER   A 117 ? 0.1790 0.1004 0.1852 0.0090  0.0171  -0.0042 117 SER   A N   
797  C  CA  A SER   A 117 ? 0.2197 0.0835 0.1811 0.0054  0.0028  -0.0066 117 SER   A CA  
798  C  CA  B SER   A 117 ? 0.2129 0.0828 0.1908 0.0000  0.0019  0.0024  117 SER   A CA  
799  C  C   . SER   A 117 ? 0.2571 0.0953 0.1853 -0.0018 0.0150  -0.0010 117 SER   A C   
800  O  O   . SER   A 117 ? 0.3251 0.1252 0.1904 0.0363  -0.0127 -0.0102 117 SER   A O   
801  C  CB  A SER   A 117 ? 0.2307 0.2176 0.2337 -0.0968 -0.0181 0.0044  117 SER   A CB  
802  C  CB  B SER   A 117 ? 0.2322 0.1494 0.2838 -0.0711 0.0067  -0.0152 117 SER   A CB  
803  O  OG  A SER   A 117 ? 0.2474 0.2200 0.4353 -0.0719 0.0032  0.0551  117 SER   A OG  
804  O  OG  B SER   A 117 ? 0.2062 0.1977 0.3221 -0.0153 0.0602  -0.0387 117 SER   A OG  
805  N  N   . THR   A 118 ? 0.2835 0.0907 0.1763 0.0047  -0.0078 0.0085  118 THR   A N   
806  C  CA  . THR   A 118 ? 0.2253 0.0925 0.2190 -0.0011 -0.0125 0.0035  118 THR   A CA  
807  C  C   . THR   A 118 ? 0.2358 0.1059 0.2026 0.0006  -0.0254 0.0034  118 THR   A C   
808  O  O   . THR   A 118 ? 0.3381 0.1005 0.2116 -0.0281 -0.0198 0.0025  118 THR   A O   
809  C  CB  . THR   A 118 ? 0.2376 0.1264 0.2430 -0.0287 0.0058  0.0005  118 THR   A CB  
810  O  OG1 . THR   A 118 ? 0.2209 0.1595 0.2756 0.0197  -0.0450 -0.0184 118 THR   A OG1 
811  C  CG2 . THR   A 118 ? 0.2764 0.1650 0.2269 0.0303  0.0383  -0.0154 118 THR   A CG2 
812  N  N   . THR   A 119 ? 0.2242 0.0981 0.1860 0.0071  -0.0328 0.0040  119 THR   A N   
813  C  CA  . THR   A 119 ? 0.1904 0.1173 0.2004 -0.0154 -0.0445 0.0169  119 THR   A CA  
814  C  C   . THR   A 119 ? 0.1528 0.1083 0.2070 -0.0114 0.0088  -0.0047 119 THR   A C   
815  O  O   . THR   A 119 ? 0.2992 0.1015 0.2474 -0.0048 -0.1076 0.0115  119 THR   A O   
816  C  CB  . THR   A 119 ? 0.1707 0.3131 0.3378 0.0532  -0.0524 0.0761  119 THR   A CB  
817  O  OG1 . THR   A 119 ? 0.2728 0.2775 0.3661 0.0505  -0.0689 0.0235  119 THR   A OG1 
818  C  CG2 . THR   A 119 ? 0.1484 0.4617 0.4496 -0.0840 -0.0811 0.2814  119 THR   A CG2 
819  N  N   . ALA   A 120 ? 0.1530 0.1138 0.2102 -0.0083 -0.0423 0.0098  120 ALA   A N   
820  C  CA  . ALA   A 120 ? 0.1554 0.1211 0.2257 -0.0096 -0.0293 0.0156  120 ALA   A CA  
821  C  C   . ALA   A 120 ? 0.1441 0.1141 0.2519 -0.0111 -0.0471 0.0181  120 ALA   A C   
822  O  O   . ALA   A 120 ? 0.1807 0.1397 0.2258 -0.0261 -0.0373 0.0247  120 ALA   A O   
823  C  CB  . ALA   A 120 ? 0.1627 0.1441 0.3447 0.0481  -0.0047 0.0292  120 ALA   A CB  
824  N  N   . VAL   A 121 ? 0.1373 0.1321 0.2327 -0.0041 -0.0363 0.0204  121 VAL   A N   
825  C  CA  . VAL   A 121 ? 0.1370 0.1834 0.2367 -0.0119 -0.0401 0.0256  121 VAL   A CA  
826  C  C   . VAL   A 121 ? 0.1319 0.1723 0.2141 -0.0451 -0.0340 0.0313  121 VAL   A C   
827  O  O   . VAL   A 121 ? 0.1741 0.1672 0.2606 -0.0364 -0.0678 0.0468  121 VAL   A O   
828  C  CB  . VAL   A 121 ? 0.1441 0.2679 0.2422 0.0114  -0.0199 0.0112  121 VAL   A CB  
829  C  CG1 . VAL   A 121 ? 0.2170 0.2345 0.3638 -0.0474 0.0980  -0.0346 121 VAL   A CG1 
830  C  CG2 . VAL   A 121 ? 0.1992 0.3967 0.3524 0.1299  -0.0045 0.0181  121 VAL   A CG2 
831  N  N   . VAL   A 122 ? 0.1224 0.1550 0.2476 -0.0277 -0.0458 0.0336  122 VAL   A N   
832  C  CA  . VAL   A 122 ? 0.1379 0.1852 0.2383 -0.0325 -0.0418 0.0469  122 VAL   A CA  
833  C  C   . VAL   A 122 ? 0.1695 0.1525 0.2834 -0.0233 -0.0427 0.0548  122 VAL   A C   
834  O  O   . VAL   A 122 ? 0.1868 0.2025 0.2918 -0.0626 -0.0462 0.0554  122 VAL   A O   
835  C  CB  . VAL   A 122 ? 0.1544 0.2133 0.2486 0.0012  -0.0414 0.0228  122 VAL   A CB  
836  C  CG1 . VAL   A 122 ? 0.1746 0.2228 0.2998 0.0213  -0.0419 0.0337  122 VAL   A CG1 
837  C  CG2 . VAL   A 122 ? 0.1766 0.2730 0.2694 -0.0297 -0.0369 0.0445  122 VAL   A CG2 
838  N  N   . THR   A 123 ? 0.1872 0.1924 0.2597 -0.0241 -0.0256 0.0334  123 THR   A N   
839  C  CA  . THR   A 123 ? 0.3058 0.2218 0.2337 -0.0928 -0.0204 0.1009  123 THR   A CA  
840  C  C   . THR   A 123 ? 0.2528 0.2708 0.3011 -0.0430 -0.0421 0.0948  123 THR   A C   
841  O  O   . THR   A 123 ? 0.2520 0.2255 0.3385 -0.0360 -0.0581 0.0927  123 THR   A O   
842  C  CB  . THR   A 123 ? 0.5598 0.4860 0.1635 -0.0148 0.0958  0.0920  123 THR   A CB  
843  O  OG1 . THR   A 123 ? 0.4422 0.4492 0.3332 -0.0240 0.0643  0.0079  123 THR   A OG1 
844  C  CG2 . THR   A 123 ? 0.6980 0.0310 0.0434 -0.0089 0.0249  0.0028  123 THR   A CG2 
845  N  N   . ASN   A 124 ? 0.2559 0.2315 0.4120 -0.0722 -0.1097 0.1709  124 ASN   A N   
846  C  CA  . ASN   A 124 ? 0.3013 0.2794 0.4198 -0.0655 -0.0595 0.2021  124 ASN   A CA  
847  C  C   . ASN   A 124 ? 0.3883 0.4709 0.4051 -0.1153 -0.0856 0.1216  124 ASN   A C   
848  O  O   . ASN   A 124 ? 0.3512 0.5484 0.4949 0.0457  0.0615  0.2694  124 ASN   A O   
849  C  CB  . ASN   A 124 ? 0.3318 0.2993 0.4305 -0.0083 -0.0361 0.1662  124 ASN   A CB  
850  C  CG  . ASN   A 124 ? 0.3534 0.2522 0.4586 -0.0199 0.0104  0.1785  124 ASN   A CG  
851  O  OD1 . ASN   A 124 ? 0.5586 0.3899 0.4875 0.0084  -0.1338 0.2282  124 ASN   A OD1 
852  N  ND2 . ASN   A 124 ? 0.4674 0.2337 0.7287 0.1199  -0.0425 0.1041  124 ASN   A ND2 
853  N  N   . PRO   A 125 ? 0.4482 0.5468 0.3725 -0.0992 -0.1025 0.0492  125 PRO   A N   
854  C  CA  . PRO   A 125 ? 0.5679 0.7336 0.4964 -0.0303 0.0241  0.1067  125 PRO   A CA  
855  C  C   . PRO   A 125 ? 0.5135 0.9479 0.3592 -0.1454 -0.0024 0.2413  125 PRO   A C   
856  O  O   . PRO   A 125 ? 0.4763 0.6367 0.7204 0.1088  0.1446  0.3333  125 PRO   A O   
857  C  CB  . PRO   A 125 ? 0.7024 0.6617 0.5989 -0.0261 -0.0323 0.0176  125 PRO   A CB  
858  C  CG  . PRO   A 125 ? 0.6435 0.6093 0.4424 -0.1048 -0.1096 -0.0334 125 PRO   A CG  
859  C  CD  . PRO   A 125 ? 0.3841 0.5250 0.4424 -0.1733 -0.2120 0.0925  125 PRO   A CD  
860  C  C   . CYS   B 10  ? 0.2923 0.5809 0.7940 -0.1314 -0.1237 0.3487  10  CYS   B C   
861  O  O   . CYS   B 10  ? 0.4641 0.5116 0.7791 -0.1682 -0.2114 0.0904  10  CYS   B O   
862  N  N   . PRO   B 11  ? 0.3424 0.3269 0.3208 0.0094  0.0895  0.0479  11  PRO   B N   
863  C  CA  . PRO   B 11  ? 0.2819 0.2613 0.3417 0.1279  0.0949  0.0384  11  PRO   B CA  
864  C  C   . PRO   B 11  ? 0.2218 0.2023 0.3234 -0.0013 0.1363  -0.0222 11  PRO   B C   
865  O  O   . PRO   B 11  ? 0.2488 0.2173 0.3421 0.0295  0.1211  0.0089  11  PRO   B O   
866  C  CB  . PRO   B 11  ? 0.5803 0.3183 0.4153 -0.0937 0.1872  0.0724  11  PRO   B CB  
867  C  CG  . PRO   B 11  ? 0.4323 0.3606 0.5286 0.0373  0.0750  -0.0060 11  PRO   B CG  
868  C  CD  . PRO   B 11  ? 0.3519 0.4140 0.3119 0.0229  0.1720  0.0117  11  PRO   B CD  
869  N  N   . LEU   B 12  ? 0.2356 0.2135 0.2621 0.0112  0.0836  -0.0169 12  LEU   B N   
870  C  CA  . LEU   B 12  ? 0.2209 0.1887 0.2776 0.0281  0.0883  0.0044  12  LEU   B CA  
871  C  C   . LEU   B 12  ? 0.2225 0.2188 0.2748 0.0124  0.0751  -0.0106 12  LEU   B C   
872  O  O   . LEU   B 12  ? 0.3086 0.2378 0.3704 -0.0123 0.1648  -0.0505 12  LEU   B O   
873  C  CB  . LEU   B 12  ? 0.2178 0.2251 0.2981 -0.0035 0.0805  0.0062  12  LEU   B CB  
874  C  CG  . LEU   B 12  ? 0.2320 0.2326 0.3443 0.0352  0.0811  0.0538  12  LEU   B CG  
875  C  CD1 . LEU   B 12  ? 0.2631 0.2057 0.3404 0.0505  0.0639  -0.0075 12  LEU   B CD1 
876  C  CD2 . LEU   B 12  ? 0.2619 0.3386 0.4318 0.0856  0.0214  0.0174  12  LEU   B CD2 
877  N  N   . MET   B 13  ? 0.2421 0.1637 0.2299 0.0295  0.0714  0.0008  13  MET   B N   
878  C  CA  A MET   B 13  ? 0.2711 0.1412 0.2384 0.0245  0.0544  0.0061  13  MET   B CA  
879  C  CA  B MET   B 13  ? 0.2910 0.1431 0.2575 0.0070  0.0707  0.0239  13  MET   B CA  
880  C  C   . MET   B 13  ? 0.2010 0.1466 0.2188 -0.0004 0.0391  -0.0104 13  MET   B C   
881  O  O   . MET   B 13  ? 0.2321 0.1440 0.2381 0.0240  0.0462  0.0043  13  MET   B O   
882  C  CB  A MET   B 13  ? 0.3001 0.2996 0.2452 -0.0767 -0.0014 0.0341  13  MET   B CB  
883  C  CB  B MET   B 13  ? 0.3535 0.1713 0.2201 0.0033  0.0441  0.0553  13  MET   B CB  
884  C  CG  A MET   B 13  ? 0.3068 0.2818 0.2683 0.0552  0.0716  -0.1052 13  MET   B CG  
885  C  CG  B MET   B 13  ? 0.3721 0.3443 0.3357 -0.0480 0.0322  0.0500  13  MET   B CG  
886  S  SD  A MET   B 13  ? 0.2732 0.2274 0.2965 -0.0019 0.0119  0.0051  13  MET   B SD  
887  S  SD  B MET   B 13  ? 0.4459 0.7857 0.5893 0.1009  -0.1543 0.0293  13  MET   B SD  
888  C  CE  A MET   B 13  ? 0.1694 0.3137 0.3120 0.0205  0.0103  -0.0337 13  MET   B CE  
889  C  CE  B MET   B 13  ? 0.8955 0.4896 0.4570 0.0056  0.0624  -0.1825 13  MET   B CE  
890  N  N   . VAL   B 14  ? 0.1754 0.1418 0.2150 0.0060  0.0425  -0.0102 14  VAL   B N   
891  C  CA  . VAL   B 14  ? 0.2133 0.1061 0.2240 0.0034  0.0259  -0.0135 14  VAL   B CA  
892  C  C   . VAL   B 14  ? 0.2261 0.1357 0.2017 -0.0142 0.0441  -0.0146 14  VAL   B C   
893  O  O   . VAL   B 14  ? 0.2472 0.2007 0.2436 -0.0370 0.0835  -0.0797 14  VAL   B O   
894  C  CB  . VAL   B 14  ? 0.2034 0.1478 0.2340 0.0422  0.0380  0.0009  14  VAL   B CB  
895  C  CG1 . VAL   B 14  ? 0.2243 0.1769 0.2469 0.0273  0.0434  0.0277  14  VAL   B CG1 
896  C  CG2 . VAL   B 14  ? 0.1827 0.1997 0.2735 0.0182  0.0124  -0.0199 14  VAL   B CG2 
897  N  N   . LYS   B 15  ? 0.2113 0.1345 0.1814 -0.0138 0.0312  -0.0038 15  LYS   B N   
898  C  CA  . LYS   B 15  ? 0.1921 0.1460 0.1943 -0.0180 0.0069  -0.0142 15  LYS   B CA  
899  C  C   . LYS   B 15  ? 0.1560 0.1570 0.1973 -0.0082 0.0171  0.0026  15  LYS   B C   
900  O  O   . LYS   B 15  ? 0.2447 0.1559 0.2015 -0.0402 0.0409  -0.0249 15  LYS   B O   
901  C  CB  . LYS   B 15  ? 0.2037 0.2048 0.2364 -0.0118 -0.0140 0.0319  15  LYS   B CB  
902  C  CG  . LYS   B 15  ? 0.1966 0.3815 0.4316 -0.0117 0.0205  0.0981  15  LYS   B CG  
903  C  CD  . LYS   B 15  ? 0.1887 0.3569 0.4318 0.0367  -0.0357 0.0319  15  LYS   B CD  
904  C  CE  . LYS   B 15  ? 0.1618 0.4498 0.6045 0.0105  -0.0748 0.0541  15  LYS   B CE  
905  N  NZ  . LYS   B 15  ? 0.2765 0.3767 0.6319 0.0284  -0.1183 -0.0236 15  LYS   B NZ  
906  N  N   . VAL   B 16  ? 0.1867 0.1446 0.1943 -0.0265 0.0053  0.0039  16  VAL   B N   
907  C  CA  . VAL   B 16  ? 0.1839 0.1226 0.2006 -0.0319 0.0133  -0.0153 16  VAL   B CA  
908  C  C   . VAL   B 16  ? 0.1782 0.1619 0.1615 -0.0227 0.0006  -0.0054 16  VAL   B C   
909  O  O   . VAL   B 16  ? 0.1906 0.1691 0.1905 -0.0342 0.0058  -0.0159 16  VAL   B O   
910  C  CB  . VAL   B 16  ? 0.1565 0.1571 0.2022 -0.0181 0.0101  -0.0046 16  VAL   B CB  
911  C  CG1 . VAL   B 16  ? 0.2038 0.2052 0.2090 -0.0252 0.0041  0.0156  16  VAL   B CG1 
912  C  CG2 . VAL   B 16  ? 0.1742 0.1799 0.2427 -0.0309 0.0064  -0.0206 16  VAL   B CG2 
913  N  N   . LEU   B 17  ? 0.1606 0.1248 0.1714 -0.0329 -0.0103 -0.0138 17  LEU   B N   
914  C  CA  . LEU   B 17  ? 0.1392 0.1347 0.1956 -0.0277 -0.0117 -0.0064 17  LEU   B CA  
915  C  C   . LEU   B 17  ? 0.1192 0.1128 0.1954 -0.0095 -0.0108 -0.0026 17  LEU   B C   
916  O  O   . LEU   B 17  ? 0.1524 0.1429 0.2150 -0.0267 -0.0397 -0.0186 17  LEU   B O   
917  C  CB  . LEU   B 17  ? 0.1587 0.1334 0.2565 -0.0059 0.0236  0.0148  17  LEU   B CB  
918  C  CG  . LEU   B 17  ? 0.2380 0.1727 0.2523 -0.0123 -0.0318 0.0214  17  LEU   B CG  
919  C  CD1 . LEU   B 17  ? 0.2465 0.2403 0.3405 0.0563  -0.0320 -0.0114 17  LEU   B CD1 
920  C  CD2 . LEU   B 17  ? 0.2928 0.2253 0.2510 -0.0043 -0.0670 0.0063  17  LEU   B CD2 
921  N  N   . ASP   B 18  ? 0.1230 0.1351 0.1933 -0.0210 -0.0108 -0.0127 18  ASP   B N   
922  C  CA  . ASP   B 18  ? 0.1192 0.1287 0.1936 -0.0023 -0.0059 0.0095  18  ASP   B CA  
923  C  C   . ASP   B 18  ? 0.1161 0.1364 0.2035 -0.0045 -0.0118 -0.0168 18  ASP   B C   
924  O  O   . ASP   B 18  ? 0.1117 0.1752 0.2055 -0.0184 -0.0076 -0.0100 18  ASP   B O   
925  C  CB  . ASP   B 18  ? 0.1108 0.1290 0.2334 -0.0084 0.0176  -0.0258 18  ASP   B CB  
926  C  CG  . ASP   B 18  ? 0.1435 0.1220 0.2310 -0.0048 0.0164  -0.0244 18  ASP   B CG  
927  O  OD1 . ASP   B 18  ? 0.1363 0.1555 0.2351 0.0076  0.0015  0.0073  18  ASP   B OD1 
928  O  OD2 . ASP   B 18  ? 0.2027 0.1377 0.2944 0.0174  0.0566  -0.0041 18  ASP   B OD2 
929  N  N   . ALA   B 19  ? 0.0963 0.1489 0.1999 0.0044  -0.0225 -0.0125 19  ALA   B N   
930  C  CA  . ALA   B 19  ? 0.0895 0.1924 0.2075 0.0122  -0.0009 0.0076  19  ALA   B CA  
931  C  C   . ALA   B 19  ? 0.0959 0.2090 0.2014 -0.0119 -0.0129 -0.0157 19  ALA   B C   
932  O  O   . ALA   B 19  ? 0.0997 0.2647 0.2492 -0.0244 0.0095  -0.0339 19  ALA   B O   
933  C  CB  . ALA   B 19  ? 0.1504 0.1534 0.2260 0.0046  0.0096  -0.0289 19  ALA   B CB  
934  N  N   . VAL   B 20  ? 0.1112 0.1667 0.2262 -0.0205 -0.0111 0.0243  20  VAL   B N   
935  C  CA  . VAL   B 20  ? 0.1233 0.2165 0.2243 -0.0397 -0.0112 0.0341  20  VAL   B CA  
936  C  C   . VAL   B 20  ? 0.1403 0.2059 0.2580 -0.0511 -0.0233 0.0200  20  VAL   B C   
937  O  O   . VAL   B 20  ? 0.1595 0.3108 0.2895 -0.1091 -0.0313 0.0250  20  VAL   B O   
938  C  CB  . VAL   B 20  ? 0.1297 0.2185 0.2368 -0.0246 -0.0277 0.0259  20  VAL   B CB  
939  C  CG1 . VAL   B 20  ? 0.1929 0.2178 0.3411 -0.0614 -0.0462 0.0890  20  VAL   B CG1 
940  C  CG2 . VAL   B 20  ? 0.1518 0.3447 0.2140 -0.0172 -0.0361 0.0030  20  VAL   B CG2 
941  N  N   . ARG   B 21  ? 0.1459 0.1752 0.2340 -0.0386 -0.0322 0.0126  21  ARG   B N   
942  C  CA  . ARG   B 21  ? 0.1901 0.1864 0.2478 -0.0231 -0.0338 -0.0004 21  ARG   B CA  
943  C  C   . ARG   B 21  ? 0.1527 0.1717 0.2226 -0.0137 -0.0054 -0.0105 21  ARG   B C   
944  O  O   . ARG   B 21  ? 0.2020 0.2066 0.2826 -0.0393 -0.0562 -0.0322 21  ARG   B O   
945  C  CB  . ARG   B 21  ? 0.2455 0.2473 0.2918 0.0729  -0.0838 -0.0807 21  ARG   B CB  
946  C  CG  . ARG   B 21  ? 0.1810 0.0847 0.5011 0.0234  -0.0993 -0.0599 21  ARG   B CG  
947  C  CD  . ARG   B 21  ? 0.3130 0.1989 0.4844 0.1643  -0.1049 -0.1116 21  ARG   B CD  
948  N  NE  . ARG   B 21  ? 0.3423 0.2288 0.5859 0.0002  -0.0681 -0.0884 21  ARG   B NE  
949  C  CZ  . ARG   B 21  ? 0.4308 0.0886 0.6644 0.0548  -0.1083 -0.0307 21  ARG   B CZ  
950  N  N   . GLY   B 22  ? 0.1161 0.1877 0.2230 0.0124  -0.0113 -0.0023 22  GLY   B N   
951  C  CA  . GLY   B 22  ? 0.1109 0.2141 0.2154 -0.0052 -0.0120 -0.0043 22  GLY   B CA  
952  C  C   . GLY   B 22  ? 0.1130 0.1768 0.2206 -0.0003 -0.0163 -0.0092 22  GLY   B C   
953  O  O   . GLY   B 22  ? 0.1402 0.1725 0.2146 0.0008  -0.0349 -0.0038 22  GLY   B O   
954  N  N   . SER   B 23  ? 0.1113 0.2115 0.2242 -0.0075 -0.0173 -0.0187 23  SER   B N   
955  C  CA  . SER   B 23  ? 0.1480 0.2304 0.2236 -0.0233 0.0128  -0.0192 23  SER   B CA  
956  C  C   . SER   B 23  ? 0.1289 0.2099 0.2101 0.0086  -0.0249 -0.0093 23  SER   B C   
957  O  O   . SER   B 23  ? 0.1601 0.2146 0.2146 -0.0335 -0.0215 -0.0274 23  SER   B O   
958  C  CB  . SER   B 23  ? 0.2185 0.2256 0.2690 0.0203  0.0105  -0.0234 23  SER   B CB  
959  O  OG  . SER   B 23  ? 0.2778 0.2135 0.3555 0.0304  0.0423  -0.0007 23  SER   B OG  
960  N  N   . PRO   B 24  ? 0.1509 0.1791 0.2116 -0.0175 -0.0149 -0.0283 24  PRO   B N   
961  C  CA  . PRO   B 24  ? 0.1629 0.1903 0.2446 -0.0062 -0.0229 -0.0205 24  PRO   B CA  
962  C  C   . PRO   B 24  ? 0.1414 0.1766 0.2287 -0.0234 0.0183  -0.0099 24  PRO   B C   
963  O  O   . PRO   B 24  ? 0.1497 0.1588 0.2960 -0.0127 0.0028  -0.0137 24  PRO   B O   
964  C  CB  . PRO   B 24  ? 0.1566 0.2870 0.2221 0.0203  -0.0150 0.0021  24  PRO   B CB  
965  C  CG  . PRO   B 24  ? 0.2244 0.5361 0.2557 -0.0654 0.0042  -0.0690 24  PRO   B CG  
966  C  CD  . PRO   B 24  ? 0.1545 0.2249 0.2251 -0.0198 -0.0149 -0.0136 24  PRO   B CD  
967  N  N   . ALA   B 25  ? 0.1438 0.1617 0.2372 -0.0101 -0.0098 -0.0089 25  ALA   B N   
968  C  CA  . ALA   B 25  ? 0.1293 0.1684 0.2449 -0.0221 0.0150  0.0260  25  ALA   B CA  
969  C  C   . ALA   B 25  ? 0.1425 0.1455 0.2418 -0.0184 0.0039  0.0177  25  ALA   B C   
970  O  O   . ALA   B 25  ? 0.1557 0.1528 0.2448 -0.0071 0.0328  -0.0022 25  ALA   B O   
971  C  CB  . ALA   B 25  ? 0.1605 0.1847 0.2411 -0.0235 -0.0051 -0.0019 25  ALA   B CB  
972  N  N   . ILE   B 26  ? 0.1731 0.1434 0.2646 -0.0251 0.0200  -0.0086 26  ILE   B N   
973  C  CA  . ILE   B 26  ? 0.1648 0.1857 0.2414 -0.0068 0.0112  -0.0003 26  ILE   B CA  
974  C  C   . ILE   B 26  ? 0.1775 0.1625 0.2392 0.0068  0.0048  -0.0247 26  ILE   B C   
975  O  O   . ILE   B 26  ? 0.2054 0.1779 0.2448 0.0109  0.0208  -0.0144 26  ILE   B O   
976  C  CB  . ILE   B 26  ? 0.1621 0.3248 0.2793 -0.0080 -0.0067 -0.0510 26  ILE   B CB  
977  C  CG1 . ILE   B 26  ? 0.2330 0.2225 0.2996 -0.0056 -0.0351 -0.0419 26  ILE   B CG1 
978  C  CG2 . ILE   B 26  ? 0.3687 0.3193 0.3981 0.0027  -0.0099 -0.1312 26  ILE   B CG2 
979  C  CD1 . ILE   B 26  ? 0.3147 0.4091 0.5400 -0.1525 -0.0372 -0.0181 26  ILE   B CD1 
980  N  N   . ASN   B 27  ? 0.1623 0.1614 0.2758 0.0123  0.0077  -0.0429 27  ASN   B N   
981  C  CA  . ASN   B 27  ? 0.1910 0.1478 0.2622 0.0271  0.0285  -0.0177 27  ASN   B CA  
982  C  C   . ASN   B 27  ? 0.1713 0.1683 0.2863 0.0315  -0.0108 -0.0180 27  ASN   B C   
983  O  O   . ASN   B 27  ? 0.2329 0.1931 0.3348 0.0632  -0.0164 -0.0346 27  ASN   B O   
984  C  CB  . ASN   B 27  ? 0.2146 0.1553 0.3161 0.0442  0.0050  -0.0471 27  ASN   B CB  
985  C  CG  . ASN   B 27  ? 0.3780 0.1902 0.3491 0.0251  0.0305  -0.0495 27  ASN   B CG  
986  O  OD1 . ASN   B 27  ? 0.4539 0.2814 0.3638 0.0780  0.0656  -0.0589 27  ASN   B OD1 
987  N  ND2 . ASN   B 27  ? 0.3541 0.2262 0.5319 0.0151  -0.0364 -0.0872 27  ASN   B ND2 
988  N  N   . VAL   B 28  ? 0.1462 0.1568 0.2823 -0.0020 0.0230  -0.0097 28  VAL   B N   
989  C  CA  . VAL   B 28  ? 0.1551 0.1605 0.2683 -0.0251 0.0109  0.0000  28  VAL   B CA  
990  C  C   . VAL   B 28  ? 0.1494 0.1781 0.2222 -0.0257 0.0187  -0.0081 28  VAL   B C   
991  O  O   . VAL   B 28  ? 0.1659 0.2010 0.2317 0.0115  0.0387  0.0192  28  VAL   B O   
992  C  CB  . VAL   B 28  ? 0.1609 0.1783 0.2331 -0.0115 0.0136  -0.0016 28  VAL   B CB  
993  C  CG1 . VAL   B 28  ? 0.1784 0.2406 0.2440 -0.0299 0.0032  -0.0301 28  VAL   B CG1 
994  C  CG2 . VAL   B 28  ? 0.1653 0.2359 0.2789 -0.0437 0.0149  0.0393  28  VAL   B CG2 
995  N  N   . ALA   B 29  ? 0.1397 0.1702 0.2546 -0.0104 0.0095  0.0018  29  ALA   B N   
996  C  CA  . ALA   B 29  ? 0.1524 0.1615 0.2403 -0.0013 0.0294  -0.0021 29  ALA   B CA  
997  C  C   . ALA   B 29  ? 0.1739 0.1481 0.2143 0.0136  0.0193  -0.0195 29  ALA   B C   
998  O  O   . ALA   B 29  ? 0.1763 0.1565 0.2306 -0.0064 0.0260  -0.0003 29  ALA   B O   
999  C  CB  . ALA   B 29  ? 0.1371 0.1759 0.3326 0.0244  0.0123  -0.0163 29  ALA   B CB  
1000 N  N   . VAL   B 30  ? 0.1601 0.1332 0.2378 0.0198  0.0473  0.0057  30  VAL   B N   
1001 C  CA  . VAL   B 30  ? 0.1462 0.1509 0.2191 0.0214  0.0181  -0.0145 30  VAL   B CA  
1002 C  C   . VAL   B 30  ? 0.1852 0.1357 0.2266 0.0280  0.0419  -0.0188 30  VAL   B C   
1003 O  O   . VAL   B 30  ? 0.1980 0.1452 0.2650 -0.0100 0.0758  -0.0341 30  VAL   B O   
1004 C  CB  . VAL   B 30  ? 0.1480 0.1654 0.2327 0.0289  0.0312  -0.0267 30  VAL   B CB  
1005 C  CG1 . VAL   B 30  ? 0.2271 0.1374 0.2714 0.0399  0.0630  -0.0077 30  VAL   B CG1 
1006 C  CG2 . VAL   B 30  ? 0.1538 0.2004 0.2666 0.0357  0.0409  -0.0235 30  VAL   B CG2 
1007 N  N   . HIS   B 31  ? 0.1583 0.1567 0.2379 0.0180  0.0485  -0.0086 31  HIS   B N   
1008 C  CA  . HIS   B 31  ? 0.1537 0.1384 0.2616 0.0315  0.0435  -0.0056 31  HIS   B CA  
1009 C  C   . HIS   B 31  ? 0.1552 0.1519 0.2279 0.0115  0.0618  -0.0140 31  HIS   B C   
1010 O  O   . HIS   B 31  ? 0.1937 0.1496 0.2646 -0.0094 0.0767  -0.0237 31  HIS   B O   
1011 C  CB  . HIS   B 31  ? 0.1519 0.1759 0.3508 0.0153  0.0146  -0.0277 31  HIS   B CB  
1012 C  CG  . HIS   B 31  ? 0.1948 0.1739 0.3937 0.0298  0.0007  0.0414  31  HIS   B CG  
1013 N  ND1 . HIS   B 31  ? 0.3401 0.2015 0.4692 0.0563  0.0537  0.0011  31  HIS   B ND1 
1014 C  CD2 . HIS   B 31  ? 0.1828 0.2167 0.4163 0.0809  0.0144  -0.0176 31  HIS   B CD2 
1015 C  CE1 . HIS   B 31  ? 0.2865 0.1704 0.4066 0.0091  0.0258  -0.0150 31  HIS   B CE1 
1016 N  NE2 . HIS   B 31  ? 0.3514 0.2032 0.5697 0.1002  0.0026  0.0244  31  HIS   B NE2 
1017 N  N   . VAL   B 32  ? 0.1895 0.1391 0.2431 0.0266  0.0931  0.0042  32  VAL   B N   
1018 C  CA  . VAL   B 32  ? 0.1462 0.1589 0.2687 0.0380  0.0528  -0.0067 32  VAL   B CA  
1019 C  C   . VAL   B 32  ? 0.1466 0.1856 0.2512 0.0425  0.0629  0.0008  32  VAL   B C   
1020 O  O   . VAL   B 32  ? 0.1938 0.1565 0.3407 0.0283  0.1084  -0.0062 32  VAL   B O   
1021 C  CB  . VAL   B 32  ? 0.1771 0.1671 0.2599 0.0164  0.0267  0.0003  32  VAL   B CB  
1022 C  CG1 . VAL   B 32  ? 0.1720 0.1531 0.2991 0.0254  0.0344  -0.0044 32  VAL   B CG1 
1023 C  CG2 . VAL   B 32  ? 0.2206 0.1824 0.3116 0.0194  0.0062  -0.0213 32  VAL   B CG2 
1024 N  N   . PHE   B 33  ? 0.1381 0.1937 0.2685 0.0222  0.0537  -0.0167 33  PHE   B N   
1025 C  CA  . PHE   B 33  ? 0.1036 0.2035 0.3195 0.0225  0.0397  0.0316  33  PHE   B CA  
1026 C  C   . PHE   B 33  ? 0.1435 0.2146 0.2834 0.0337  0.0559  0.0390  33  PHE   B C   
1027 O  O   . PHE   B 33  ? 0.1361 0.1870 0.2849 0.0093  0.0559  0.0322  33  PHE   B O   
1028 C  CB  . PHE   B 33  ? 0.1360 0.2191 0.3527 -0.0035 0.0089  0.0524  33  PHE   B CB  
1029 C  CG  . PHE   B 33  ? 0.1571 0.2361 0.4064 0.0017  0.0119  0.1103  33  PHE   B CG  
1030 C  CD1 . PHE   B 33  ? 0.1950 0.2195 0.3287 -0.0314 0.0107  0.0455  33  PHE   B CD1 
1031 C  CD2 . PHE   B 33  ? 0.2297 0.2419 0.6745 0.0180  -0.0383 0.1896  33  PHE   B CD2 
1032 C  CE1 . PHE   B 33  ? 0.2285 0.2651 0.3876 -0.0541 -0.0162 0.0639  33  PHE   B CE1 
1033 C  CE2 . PHE   B 33  ? 0.2859 0.1754 0.8367 0.0077  -0.0216 0.1137  33  PHE   B CE2 
1034 C  CZ  . PHE   B 33  ? 0.2778 0.2859 0.7336 -0.0220 -0.1131 0.1943  33  PHE   B CZ  
1035 N  N   . ARG   B 34  ? 0.1227 0.2255 0.3164 0.0221  0.0687  0.0224  34  ARG   B N   
1036 C  CA  . ARG   B 34  ? 0.1623 0.2336 0.3004 -0.0309 0.0467  0.0448  34  ARG   B CA  
1037 C  C   . ARG   B 34  ? 0.1755 0.2302 0.3377 -0.0290 0.0096  0.0191  34  ARG   B C   
1038 O  O   . ARG   B 34  ? 0.1458 0.2896 0.4881 0.0093  -0.0160 -0.0280 34  ARG   B O   
1039 C  CB  . ARG   B 34  ? 0.2292 0.2223 0.3087 -0.0147 0.0894  0.0438  34  ARG   B CB  
1040 N  N   . LYS   B 35  ? 0.2117 0.2397 0.3367 -0.0372 0.0119  0.0382  35  LYS   B N   
1041 C  CA  . LYS   B 35  ? 0.2186 0.2702 0.4011 -0.0397 -0.0421 0.0732  35  LYS   B CA  
1042 C  C   . LYS   B 35  ? 0.1410 0.3421 0.4091 -0.0548 -0.0166 0.0655  35  LYS   B C   
1043 O  O   . LYS   B 35  ? 0.1946 0.2973 0.4630 -0.0600 -0.0179 0.1096  35  LYS   B O   
1044 C  CB  . LYS   B 35  ? 0.2154 0.3239 0.4097 -0.0631 -0.0557 0.0547  35  LYS   B CB  
1045 C  CG  . LYS   B 35  ? 0.3828 0.3594 0.4092 -0.0620 -0.0708 -0.0070 35  LYS   B CG  
1046 C  CD  . LYS   B 35  ? 0.4750 0.5172 0.3884 0.0210  -0.0840 0.0368  35  LYS   B CD  
1047 C  CE  . LYS   B 35  ? 0.4918 0.4349 0.4478 0.0424  -0.0128 0.1270  35  LYS   B CE  
1048 N  NZ  . LYS   B 35  ? 0.4691 0.5280 0.4151 0.0987  0.0249  0.1189  35  LYS   B NZ  
1049 N  N   . ALA   B 36  ? 0.1831 0.3143 0.4751 -0.0484 -0.0065 0.0933  36  ALA   B N   
1050 C  CA  . ALA   B 36  ? 0.1555 0.3936 0.3944 0.0010  0.0012  0.0848  36  ALA   B CA  
1051 C  C   . ALA   B 36  ? 0.3269 0.4615 0.4317 -0.1412 -0.0326 0.1127  36  ALA   B C   
1052 O  O   . ALA   B 36  ? 0.2554 0.4859 0.4808 -0.1195 -0.0757 0.1239  36  ALA   B O   
1053 C  CB  . ALA   B 36  ? 0.1726 0.3475 0.6701 0.0111  -0.0459 0.1684  36  ALA   B CB  
1054 N  N   . ALA   B 37  ? 0.2576 0.4303 0.4715 -0.0564 0.0070  0.1105  37  ALA   B N   
1055 C  CA  . ALA   B 37  ? 0.4235 0.4325 0.5128 -0.1518 -0.1012 0.1484  37  ALA   B CA  
1056 C  C   . ALA   B 37  ? 0.2721 0.5764 0.5755 -0.1183 -0.0914 0.2082  37  ALA   B C   
1057 O  O   . ALA   B 37  ? 0.8061 0.5107 0.8129 -0.2102 -0.1665 0.0367  37  ALA   B O   
1058 C  CB  . ALA   B 37  ? 0.4221 0.6056 0.4841 -0.2519 -0.0839 0.1745  37  ALA   B CB  
1059 N  N   . ASP   B 38  ? 0.2924 0.6040 0.5117 -0.1200 -0.0888 0.1815  38  ASP   B N   
1060 C  CA  . ASP   B 38  ? 0.2795 0.6053 0.4588 -0.1200 -0.0812 0.1311  38  ASP   B CA  
1061 C  C   . ASP   B 38  ? 0.2978 0.6911 0.5864 -0.1510 -0.0914 0.2349  38  ASP   B C   
1062 O  O   . ASP   B 38  ? 0.4666 0.6675 0.5803 -0.1655 -0.1706 0.2441  38  ASP   B O   
1063 C  CB  . ASP   B 38  ? 0.2459 0.6992 0.6038 -0.0637 -0.0036 0.1508  38  ASP   B CB  
1064 C  CG  . ASP   B 38  ? 0.2290 0.4436 0.7143 0.1485  -0.0447 0.1777  38  ASP   B CG  
1065 O  OD1 . ASP   B 38  ? 0.2169 0.4121 0.4805 0.0205  -0.0347 0.1993  38  ASP   B OD1 
1066 O  OD2 . ASP   B 38  ? 0.2488 0.4586 0.7202 0.0967  0.0713  0.2393  38  ASP   B OD2 
1067 N  N   . ASP   B 39  ? 0.3666 0.5542 0.5318 -0.1222 -0.0737 0.2639  39  ASP   B N   
1068 C  CA  . ASP   B 39  ? 0.3145 0.7595 0.4900 -0.0972 -0.0538 0.1878  39  ASP   B CA  
1069 C  C   . ASP   B 39  ? 0.2301 0.7264 0.6477 -0.0296 0.0148  0.1192  39  ASP   B C   
1070 O  O   . ASP   B 39  ? 0.3305 0.7372 0.5662 -0.0331 0.0204  0.1888  39  ASP   B O   
1071 C  CB  . ASP   B 39  ? 0.2752 0.6995 0.4276 0.0165  0.1136  0.1821  39  ASP   B CB  
1072 C  CG  . ASP   B 39  ? 0.6169 0.6910 0.4468 0.0904  -0.0530 0.0801  39  ASP   B CG  
1073 O  OD1 . ASP   B 39  ? 0.3541 0.4696 0.7058 -0.0026 -0.0892 0.1920  39  ASP   B OD1 
1074 O  OD2 . ASP   B 39  ? 0.5323 0.6164 0.4674 0.1677  -0.0282 0.0566  39  ASP   B OD2 
1075 N  N   . THR   B 40  ? 0.2053 0.4188 0.4742 -0.0916 -0.0690 0.2230  40  THR   B N   
1076 C  CA  . THR   B 40  ? 0.2161 0.3716 0.5592 -0.0372 -0.0806 0.1917  40  THR   B CA  
1077 C  C   . THR   B 40  ? 0.1508 0.3032 0.5114 0.0148  -0.0272 0.1718  40  THR   B C   
1078 O  O   . THR   B 40  ? 0.1746 0.3185 0.3988 -0.0322 -0.0408 0.1534  40  THR   B O   
1079 C  CB  . THR   B 40  ? 0.2506 0.4996 0.8552 0.0023  -0.2032 0.0088  40  THR   B CB  
1080 O  OG1 . THR   B 40  ? 0.0765 0.8957 1.3317 0.2086  0.0101  0.2051  40  THR   B OG1 
1081 C  CG2 . THR   B 40  ? 0.3145 0.5634 0.6783 -0.0874 -0.1301 0.2694  40  THR   B CG2 
1082 N  N   . TRP   B 41  ? 0.1993 0.2918 0.6069 -0.0013 -0.0374 0.1865  41  TRP   B N   
1083 C  CA  . TRP   B 41  ? 0.1772 0.3304 0.5113 -0.0002 0.0024  0.1262  41  TRP   B CA  
1084 C  C   . TRP   B 41  ? 0.2163 0.3035 0.6487 0.0340  0.0625  0.1204  41  TRP   B C   
1085 O  O   . TRP   B 41  ? 0.4798 0.2920 0.7924 0.1724  0.0681  0.0369  41  TRP   B O   
1086 C  CB  . TRP   B 41  ? 0.2060 0.3267 0.5072 -0.0109 0.0035  0.1306  41  TRP   B CB  
1087 C  CG  . TRP   B 41  ? 0.2463 0.3933 0.4559 -0.0177 -0.0876 0.1963  41  TRP   B CG  
1088 C  CD1 . TRP   B 41  ? 0.6486 0.2537 0.5070 0.2257  -0.2313 0.1571  41  TRP   B CD1 
1089 C  CD2 . TRP   B 41  ? 0.1913 0.2805 0.3452 -0.0408 -0.0052 0.0628  41  TRP   B CD2 
1090 N  NE1 . TRP   B 41  ? 0.4467 0.3807 0.4498 0.0461  -0.0360 0.1866  41  TRP   B NE1 
1091 C  CE2 . TRP   B 41  ? 0.2851 0.2747 0.4002 0.0182  -0.0302 0.1285  41  TRP   B CE2 
1092 C  CE3 . TRP   B 41  ? 0.1770 0.2571 0.3327 -0.0057 -0.0151 0.0521  41  TRP   B CE3 
1093 C  CZ2 . TRP   B 41  ? 0.2793 0.3507 0.4598 0.0086  0.0604  0.0359  41  TRP   B CZ2 
1094 C  CZ3 . TRP   B 41  ? 0.1481 0.2645 0.4661 -0.0106 0.0311  0.0473  41  TRP   B CZ3 
1095 C  CH2 . TRP   B 41  ? 0.1760 0.2531 0.4971 -0.0113 0.0128  0.0482  41  TRP   B CH2 
1096 N  N   . GLU   B 42  ? 0.1639 0.3023 0.5694 0.0036  0.0134  0.0059  42  GLU   B N   
1097 C  CA  . GLU   B 42  ? 0.1699 0.3023 0.5694 0.0226  0.0006  -0.0045 42  GLU   B CA  
1098 C  C   . GLU   B 42  ? 0.1659 0.2950 0.4738 0.0004  0.0095  0.0415  42  GLU   B C   
1099 O  O   . GLU   B 42  ? 0.1548 0.2677 0.4305 0.0372  0.0705  0.0091  42  GLU   B O   
1100 C  CB  . GLU   B 42  ? 0.2359 0.3176 0.5699 -0.0600 0.0263  -0.0155 42  GLU   B CB  
1101 C  CG  . GLU   B 42  ? 0.1843 0.3849 0.4655 -0.0237 -0.0097 -0.0661 42  GLU   B CG  
1102 C  CD  . GLU   B 42  ? 0.2222 0.5042 0.4218 -0.1139 0.1643  -0.0792 42  GLU   B CD  
1103 O  OE1 . GLU   B 42  ? 0.3085 0.5199 0.4980 -0.1888 0.0255  0.0537  42  GLU   B OE1 
1104 O  OE2 . GLU   B 42  ? 0.6139 0.3711 0.4245 -0.1327 0.0994  -0.0770 42  GLU   B OE2 
1105 N  N   . PRO   B 43  ? 0.2733 0.3060 0.4234 0.0415  -0.0643 0.0084  43  PRO   B N   
1106 C  CA  . PRO   B 43  ? 0.3161 0.2665 0.4252 0.0069  -0.0651 -0.0134 43  PRO   B CA  
1107 C  C   . PRO   B 43  ? 0.2882 0.3001 0.3454 -0.0026 0.0754  -0.0807 43  PRO   B C   
1108 O  O   . PRO   B 43  ? 0.3611 0.4529 0.4775 -0.0384 0.0633  -0.0870 43  PRO   B O   
1109 C  CB  . PRO   B 43  ? 0.2691 0.2370 0.2951 0.0102  -0.0274 -0.0005 43  PRO   B CB  
1110 C  CG  . PRO   B 43  ? 0.2669 0.2399 0.2806 0.0388  -0.0417 -0.0301 43  PRO   B CG  
1111 C  CD  . PRO   B 43  ? 0.2716 0.2658 0.3301 0.0304  -0.0204 0.0077  43  PRO   B CD  
1112 N  N   . PHE   B 44  ? 0.2795 0.1569 0.4301 -0.0305 0.0038  -0.0177 44  PHE   B N   
1113 C  CA  . PHE   B 44  ? 0.3523 0.2995 0.4004 -0.0107 0.0611  0.0053  44  PHE   B CA  
1114 C  C   . PHE   B 44  ? 0.4023 0.5260 0.3218 -0.2292 0.1211  -0.0224 44  PHE   B C   
1115 O  O   . PHE   B 44  ? 0.4407 0.5257 0.3532 -0.3294 0.1587  -0.0857 44  PHE   B O   
1116 C  CB  . PHE   B 44  ? 0.4078 0.2424 0.5025 0.0425  0.0507  0.0452  44  PHE   B CB  
1117 C  CG  . PHE   B 44  ? 0.3790 0.1013 0.6595 0.0358  -0.1093 -0.0286 44  PHE   B CG  
1118 C  CD1 . PHE   B 44  ? 0.2900 0.2094 0.4335 0.0244  0.0572  0.1333  44  PHE   B CD1 
1119 C  CD2 . PHE   B 44  ? 0.4216 0.2868 0.4537 -0.0292 0.0397  0.0796  44  PHE   B CD2 
1120 C  CE1 . PHE   B 44  ? 0.3721 0.1552 0.3484 0.0199  -0.0051 0.0230  44  PHE   B CE1 
1121 C  CE2 . PHE   B 44  ? 0.3882 0.1604 0.4322 -0.0047 0.0114  0.0578  44  PHE   B CE2 
1122 C  CZ  . PHE   B 44  ? 0.4181 0.2412 0.3735 -0.0368 0.0313  0.0811  44  PHE   B CZ  
1123 N  N   . ALA   B 45  ? 0.4206 0.3392 0.2936 -0.2027 0.1464  -0.0906 45  ALA   B N   
1124 C  CA  . ALA   B 45  ? 0.3752 0.2762 0.2789 -0.1081 0.1871  -0.0643 45  ALA   B CA  
1125 C  C   . ALA   B 45  ? 0.2948 0.1722 0.3088 -0.0618 0.1504  -0.0792 45  ALA   B C   
1126 O  O   . ALA   B 45  ? 0.3097 0.2041 0.3270 -0.0768 0.1690  -0.0838 45  ALA   B O   
1127 C  CB  . ALA   B 45  ? 0.4171 0.2211 0.3753 -0.0958 0.2031  -0.0500 45  ALA   B CB  
1128 N  N   . SER   B 46  ? 0.2537 0.1645 0.2941 -0.0255 0.1306  -0.0588 46  SER   B N   
1129 C  CA  . SER   B 46  ? 0.2081 0.1650 0.2704 0.0033  0.1064  -0.0404 46  SER   B CA  
1130 C  C   . SER   B 46  ? 0.1723 0.2237 0.2631 0.0356  0.1040  -0.0511 46  SER   B C   
1131 O  O   . SER   B 46  ? 0.1896 0.1746 0.3061 -0.0013 0.0923  -0.0399 46  SER   B O   
1132 C  CB  . SER   B 46  ? 0.1727 0.1895 0.2655 0.0055  0.0581  -0.0528 46  SER   B CB  
1133 O  OG  . SER   B 46  ? 0.1930 0.2211 0.2799 0.0105  0.0552  -0.0680 46  SER   B OG  
1134 N  N   . GLY   B 47  ? 0.1932 0.1979 0.2367 -0.0053 0.0787  -0.0485 47  GLY   B N   
1135 C  CA  . GLY   B 47  ? 0.1869 0.1952 0.2168 0.0302  0.0495  -0.0247 47  GLY   B CA  
1136 C  C   . GLY   B 47  ? 0.1858 0.1386 0.2528 -0.0023 0.0600  -0.0367 47  GLY   B C   
1137 O  O   . GLY   B 47  ? 0.1908 0.1978 0.2473 0.0005  0.0558  -0.0435 47  GLY   B O   
1138 N  N   . LYS   B 48  ? 0.1746 0.2610 0.2618 0.0026  0.0654  -0.0571 48  LYS   B N   
1139 C  CA  A LYS   B 48  ? 0.1382 0.2170 0.2706 -0.0053 0.0153  -0.1392 48  LYS   B CA  
1140 C  CA  B LYS   B 48  ? 0.2033 0.1184 0.3297 0.0372  0.0499  0.0149  48  LYS   B CA  
1141 C  C   . LYS   B 48  ? 0.1716 0.1903 0.2499 0.0217  0.0304  -0.0228 48  LYS   B C   
1142 O  O   . LYS   B 48  ? 0.1778 0.2486 0.2555 -0.0054 0.0445  -0.0096 48  LYS   B O   
1143 C  CB  A LYS   B 48  ? 0.1580 0.2354 0.3219 0.0820  0.0295  -0.0609 48  LYS   B CB  
1144 C  CB  B LYS   B 48  ? 0.2156 0.1254 0.0495 -0.0414 0.0187  0.0410  48  LYS   B CB  
1145 C  CG  A LYS   B 48  ? 0.2797 0.3516 0.3458 -0.0463 0.0495  -0.2848 48  LYS   B CG  
1146 C  CG  B LYS   B 48  ? 0.3861 0.1561 0.3471 0.0510  0.0312  0.1441  48  LYS   B CG  
1147 C  CD  A LYS   B 48  ? 0.2862 0.3488 0.4465 -0.1011 -0.0725 0.1092  48  LYS   B CD  
1148 C  CD  B LYS   B 48  ? 0.4476 0.3304 0.4169 0.0836  0.1440  -0.1040 48  LYS   B CD  
1149 N  N   . THR   B 49  ? 0.1583 0.1911 0.2224 0.0033  0.0348  0.0000  49  THR   B N   
1150 C  CA  . THR   B 49  ? 0.1605 0.1726 0.2248 0.0021  0.0196  -0.0020 49  THR   B CA  
1151 C  C   . THR   B 49  ? 0.2346 0.0824 0.2590 0.0094  0.0259  0.0501  49  THR   B C   
1152 O  O   . THR   B 49  ? 0.1756 0.1392 0.3535 -0.0016 0.0509  -0.0466 49  THR   B O   
1153 C  CB  . THR   B 49  ? 0.1499 0.1405 0.2537 -0.0032 0.0372  -0.0518 49  THR   B CB  
1154 O  OG1 . THR   B 49  ? 0.1725 0.1360 0.2360 0.0018  0.0233  -0.0164 49  THR   B OG1 
1155 C  CG2 . THR   B 49  ? 0.1757 0.1629 0.2320 -0.0014 0.0300  -0.0253 49  THR   B CG2 
1156 N  N   . SER   B 50  ? 0.2221 0.1335 0.2258 0.0007  0.0486  -0.0061 50  SER   B N   
1157 C  CA  . SER   B 50  ? 0.2439 0.2265 0.2003 -0.0159 0.0359  -0.0510 50  SER   B CA  
1158 C  C   . SER   B 50  ? 0.2181 0.1977 0.2372 0.0206  0.0079  -0.0608 50  SER   B C   
1159 O  O   . SER   B 50  ? 0.1963 0.1988 0.2486 -0.0057 0.0115  -0.0513 50  SER   B O   
1160 C  CB  . SER   B 50  ? 0.2651 0.2847 0.2257 -0.0274 0.0436  -0.0354 50  SER   B CB  
1161 O  OG  . SER   B 50  ? 0.2612 0.2380 0.2561 0.0009  -0.0079 -0.0223 50  SER   B OG  
1162 N  N   . GLU   B 51  ? 0.2182 0.2732 0.2133 0.0010  0.0001  -0.0611 51  GLU   B N   
1163 C  CA  . GLU   B 51  ? 0.2476 0.2524 0.2883 -0.0373 0.0245  -0.0620 51  GLU   B CA  
1164 C  C   . GLU   B 51  ? 0.2219 0.2619 0.2580 -0.0341 0.0112  -0.0534 51  GLU   B C   
1165 O  O   . GLU   B 51  ? 0.2342 0.2810 0.2889 -0.0142 0.0060  0.0035  51  GLU   B O   
1166 C  CB  . GLU   B 51  ? 0.2670 0.3581 0.4485 -0.0310 -0.0003 -0.2152 51  GLU   B CB  
1167 N  N   . SER   B 52  ? 0.1925 0.2591 0.2483 -0.0069 -0.0016 -0.0488 52  SER   B N   
1168 C  CA  . SER   B 52  ? 0.1763 0.2594 0.2526 0.0183  -0.0119 -0.0251 52  SER   B CA  
1169 C  C   . SER   B 52  ? 0.1991 0.2047 0.2261 0.0020  0.0255  -0.0255 52  SER   B C   
1170 O  O   . SER   B 52  ? 0.2062 0.2452 0.2369 0.0186  0.0062  -0.0011 52  SER   B O   
1171 C  CB  . SER   B 52  ? 0.3382 0.2849 0.2779 0.0009  -0.0566 0.0066  52  SER   B CB  
1172 O  OG  . SER   B 52  ? 0.4066 0.3195 0.3362 0.0190  0.0567  0.0197  52  SER   B OG  
1173 N  N   . GLY   B 53  ? 0.1927 0.1721 0.2285 0.0062  0.0097  -0.0219 53  GLY   B N   
1174 C  CA  . GLY   B 53  ? 0.1759 0.1833 0.2183 0.0039  0.0317  -0.0142 53  GLY   B CA  
1175 C  C   . GLY   B 53  ? 0.1891 0.1592 0.2075 0.0031  0.0140  -0.0146 53  GLY   B C   
1176 O  O   . GLY   B 53  ? 0.2307 0.1734 0.2104 -0.0057 0.0274  -0.0330 53  GLY   B O   
1177 N  N   . GLU   B 54  ? 0.2334 0.1692 0.2076 -0.0212 0.0223  -0.0138 54  GLU   B N   
1178 C  CA  . GLU   B 54  ? 0.2164 0.1577 0.2054 -0.0061 0.0186  -0.0189 54  GLU   B CA  
1179 C  C   . GLU   B 54  ? 0.2286 0.1619 0.2120 -0.0170 0.0241  -0.0184 54  GLU   B C   
1180 O  O   . GLU   B 54  ? 0.2363 0.1714 0.2516 -0.0272 0.0480  -0.0367 54  GLU   B O   
1181 C  CB  . GLU   B 54  ? 0.2238 0.2250 0.2917 -0.0060 0.0056  0.0212  54  GLU   B CB  
1182 C  CG  . GLU   B 54  ? 0.2520 0.2611 0.3782 -0.0136 -0.0185 0.0135  54  GLU   B CG  
1183 C  CD  . GLU   B 54  ? 0.2887 0.4508 0.4664 0.0822  -0.0274 0.0747  54  GLU   B CD  
1184 O  OE1 . GLU   B 54  ? 0.2870 0.4469 0.4583 -0.0230 -0.1152 0.1594  54  GLU   B OE1 
1185 O  OE2 . GLU   B 54  ? 0.2685 0.3239 0.6169 0.0596  -0.0025 0.0758  54  GLU   B OE2 
1186 N  N   . LEU   B 55  ? 0.2295 0.1436 0.2225 0.0031  0.0336  -0.0219 55  LEU   B N   
1187 C  CA  . LEU   B 55  ? 0.1735 0.1535 0.2359 0.0023  0.0191  -0.0327 55  LEU   B CA  
1188 C  C   . LEU   B 55  ? 0.1833 0.1462 0.2762 0.0076  0.0325  -0.0396 55  LEU   B C   
1189 O  O   . LEU   B 55  ? 0.2596 0.1447 0.2827 0.0037  0.0551  0.0073  55  LEU   B O   
1190 C  CB  . LEU   B 55  ? 0.2291 0.1487 0.2364 -0.0076 0.0510  0.0003  55  LEU   B CB  
1191 C  CG  . LEU   B 55  ? 0.2159 0.1763 0.2485 -0.0293 0.0230  0.0380  55  LEU   B CG  
1192 C  CD1 . LEU   B 55  ? 0.2240 0.2249 0.2730 0.0343  0.0688  -0.0234 55  LEU   B CD1 
1193 C  CD2 . LEU   B 55  ? 0.2503 0.2316 0.2396 0.0156  0.0276  0.0279  55  LEU   B CD2 
1194 N  N   . HIS   B 56  ? 0.3106 0.2166 0.2504 0.0114  0.0898  -0.0126 56  HIS   B N   
1195 C  CA  . HIS   B 56  ? 0.3362 0.2941 0.3584 0.0806  0.1143  0.1307  56  HIS   B CA  
1196 C  C   . HIS   B 56  ? 0.3454 0.2595 0.2861 0.0427  0.1038  0.0533  56  HIS   B C   
1197 O  O   . HIS   B 56  ? 0.3285 0.2692 0.3471 0.0381  0.1181  0.0348  56  HIS   B O   
1198 C  CB  . HIS   B 56  ? 0.3648 0.3299 0.3970 0.0263  0.0047  0.1190  56  HIS   B CB  
1199 C  CG  . HIS   B 56  ? 0.4282 0.3180 0.3317 0.0102  -0.0469 0.0930  56  HIS   B CG  
1200 N  ND1 . HIS   B 56  ? 0.3558 0.4978 0.6311 -0.0282 -0.0677 0.1384  56  HIS   B ND1 
1201 C  CD2 . HIS   B 56  ? 0.5858 0.3947 0.4208 0.1282  -0.0352 0.1143  56  HIS   B CD2 
1202 C  CE1 . HIS   B 56  ? 0.2610 0.4872 0.4700 -0.0441 -0.0528 0.1728  56  HIS   B CE1 
1203 N  NE2 . HIS   B 56  ? 0.5839 0.5304 0.5484 0.0699  -0.0530 0.0067  56  HIS   B NE2 
1204 N  N   . GLY   B 57  ? 0.3963 0.2734 0.3170 0.0038  0.0966  0.0550  57  GLY   B N   
1205 C  CA  . GLY   B 57  ? 0.4417 0.3815 0.3406 -0.0364 0.1816  0.0165  57  GLY   B CA  
1206 C  C   . GLY   B 57  ? 0.3752 0.2230 0.4835 0.0453  0.1870  0.0314  57  GLY   B C   
1207 O  O   . GLY   B 57  ? 0.3903 0.3851 0.4877 0.1021  0.2317  0.0728  57  GLY   B O   
1208 N  N   . LEU   B 58  ? 0.2365 0.2478 0.5004 0.0315  0.0710  -0.0864 58  LEU   B N   
1209 C  CA  . LEU   B 58  ? 0.3172 0.1547 0.4503 -0.0308 0.1357  -0.0388 58  LEU   B CA  
1210 C  C   . LEU   B 58  ? 0.2640 0.2311 0.5345 -0.0185 0.1592  0.0539  58  LEU   B C   
1211 O  O   . LEU   B 58  ? 0.2739 0.2385 0.6279 -0.0181 0.1085  -0.0164 58  LEU   B O   
1212 C  CB  . LEU   B 58  ? 0.3327 0.2083 0.4603 -0.0051 0.1466  -0.0640 58  LEU   B CB  
1213 C  CG  . LEU   B 58  ? 0.2615 0.2365 0.4233 -0.0480 0.1019  -0.0854 58  LEU   B CG  
1214 C  CD1 . LEU   B 58  ? 0.3334 0.3208 0.4768 -0.0958 0.1672  -0.1405 58  LEU   B CD1 
1215 C  CD2 . LEU   B 58  ? 0.3808 0.2194 0.5111 0.0061  0.1526  0.0305  58  LEU   B CD2 
1216 N  N   . THR   B 59  ? 0.3169 0.1861 0.5501 -0.0071 0.1234  -0.0168 59  THR   B N   
1217 C  CA  . THR   B 59  ? 0.2659 0.2057 0.6009 -0.0191 0.1238  -0.0583 59  THR   B CA  
1218 C  C   . THR   B 59  ? 0.3813 0.2260 0.4654 -0.0139 0.1929  -0.0458 59  THR   B C   
1219 O  O   . THR   B 59  ? 0.3755 0.3334 0.4428 -0.0262 0.1460  0.0090  59  THR   B O   
1220 C  CB  . THR   B 59  ? 0.2801 0.2060 0.5494 -0.0136 0.0842  0.0524  59  THR   B CB  
1221 O  OG1 . THR   B 59  ? 0.2842 0.2947 0.6417 -0.0391 0.0658  0.0833  59  THR   B OG1 
1222 C  CG2 . THR   B 59  ? 0.2548 0.2718 0.4273 0.0120  0.0988  0.0034  59  THR   B CG2 
1223 N  N   . THR   B 60  ? 0.3240 0.3097 0.5414 -0.0892 0.1671  -0.0464 60  THR   B N   
1224 C  CA  . THR   B 60  ? 0.3804 0.3403 0.4120 -0.1128 0.1638  -0.0239 60  THR   B CA  
1225 C  C   . THR   B 60  ? 0.2862 0.3257 0.3358 -0.1070 0.0707  0.0384  60  THR   B C   
1226 O  O   . THR   B 60  ? 0.2196 0.2944 0.3533 -0.0384 0.0792  0.0188  60  THR   B O   
1227 C  CB  . THR   B 60  ? 0.4466 0.3173 0.4807 0.0666  0.2108  -0.0351 60  THR   B CB  
1228 O  OG1 . THR   B 60  ? 0.4364 0.5102 0.5334 0.0001  0.2627  -0.0521 60  THR   B OG1 
1229 C  CG2 . THR   B 60  ? 0.5286 0.3843 0.4973 0.0843  0.2140  -0.0787 60  THR   B CG2 
1230 N  N   . GLU   B 61  ? 0.4291 0.2835 0.2989 -0.0958 0.0427  -0.0025 61  GLU   B N   
1231 C  CA  . GLU   B 61  ? 0.2998 0.2518 0.4329 -0.0039 0.0360  0.0028  61  GLU   B CA  
1232 C  C   . GLU   B 61  ? 0.3790 0.4045 0.3197 -0.0875 0.0310  0.0376  61  GLU   B C   
1233 O  O   . GLU   B 61  ? 0.3469 0.3773 0.4930 -0.0421 0.0177  -0.0303 61  GLU   B O   
1234 C  CB  . GLU   B 61  ? 0.5400 0.3990 0.4275 -0.0261 -0.0179 0.1366  61  GLU   B CB  
1235 N  N   . GLU   B 62  ? 0.4050 0.3788 0.3820 -0.1003 0.0785  0.0770  62  GLU   B N   
1236 C  CA  . GLU   B 62  ? 0.4055 0.3360 0.5865 -0.1616 0.0483  -0.0336 62  GLU   B CA  
1237 C  C   . GLU   B 62  ? 0.3876 0.3673 0.4933 -0.1527 0.0798  0.0582  62  GLU   B C   
1238 O  O   . GLU   B 62  ? 0.3163 0.2914 0.5198 -0.0715 0.0967  0.0468  62  GLU   B O   
1239 N  N   . GLU   B 63  ? 0.3036 0.2697 0.4151 -0.0124 0.1906  -0.0068 63  GLU   B N   
1240 C  CA  . GLU   B 63  ? 0.2406 0.2581 0.4210 -0.0400 0.1323  -0.0260 63  GLU   B CA  
1241 C  C   . GLU   B 63  ? 0.1859 0.2219 0.3534 -0.0171 0.0971  0.0093  63  GLU   B C   
1242 O  O   . GLU   B 63  ? 0.2059 0.2126 0.4620 -0.0054 0.0977  0.0207  63  GLU   B O   
1244 N  N   . PHE   B 64  ? 0.2054 0.1963 0.3566 -0.0098 0.1020  0.0389  64  PHE   B N   
1245 C  CA  . PHE   B 64  ? 0.1435 0.2222 0.3769 0.0080  0.1153  0.0594  64  PHE   B CA  
1246 C  C   . PHE   B 64  ? 0.2380 0.1646 0.2961 0.0243  0.0503  0.0233  64  PHE   B C   
1247 O  O   . PHE   B 64  ? 0.2069 0.2272 0.3143 0.0145  0.0610  0.0401  64  PHE   B O   
1248 C  CB  . PHE   B 64  ? 0.1811 0.2478 0.3023 -0.0145 0.0808  0.0352  64  PHE   B CB  
1249 C  CG  . PHE   B 64  ? 0.1933 0.2306 0.3009 -0.0529 0.0498  -0.0183 64  PHE   B CG  
1250 C  CD1 . PHE   B 64  ? 0.1988 0.3349 0.2847 -0.0654 0.0417  0.0004  64  PHE   B CD1 
1251 C  CD2 . PHE   B 64  ? 0.2329 0.3144 0.3778 0.0021  0.1197  -0.0023 64  PHE   B CD2 
1252 C  CE1 . PHE   B 64  ? 0.2739 0.3651 0.3163 -0.1153 0.0746  -0.0092 64  PHE   B CE1 
1253 C  CE2 . PHE   B 64  ? 0.3193 0.3380 0.3371 0.0122  0.1301  -0.0437 64  PHE   B CE2 
1254 C  CZ  . PHE   B 64  ? 0.2687 0.3237 0.2941 -0.0970 0.1219  -0.0162 64  PHE   B CZ  
1255 N  N   . VAL   B 65  ? 0.2175 0.1820 0.2927 -0.0177 0.0637  -0.0537 65  VAL   B N   
1256 C  CA  . VAL   B 65  ? 0.1469 0.2867 0.4068 0.0419  0.0412  -0.0688 65  VAL   B CA  
1257 C  C   . VAL   B 65  ? 0.2239 0.2618 0.2276 -0.0048 0.0859  -0.0643 65  VAL   B C   
1258 O  O   . VAL   B 65  ? 0.2413 0.2581 0.2938 -0.0320 0.0677  0.1076  65  VAL   B O   
1259 C  CB  . VAL   B 65  ? 0.2040 0.1972 0.4153 0.0176  0.0609  0.1361  65  VAL   B CB  
1260 C  CG1 . VAL   B 65  ? 0.2591 0.2287 0.3695 -0.0318 0.1396  0.0427  65  VAL   B CG1 
1261 C  CG2 . VAL   B 65  ? 0.2545 0.2969 0.5338 -0.1108 0.1039  0.0497  65  VAL   B CG2 
1262 N  N   . GLU   B 66  ? 0.1873 0.2279 0.2725 -0.0060 0.0617  0.0304  66  GLU   B N   
1263 C  CA  . GLU   B 66  ? 0.1907 0.2228 0.3061 -0.0496 0.0735  0.0374  66  GLU   B CA  
1264 C  C   . GLU   B 66  ? 0.2036 0.2895 0.2962 -0.0569 0.0448  0.0781  66  GLU   B C   
1265 O  O   . GLU   B 66  ? 0.1885 0.4090 0.3849 -0.0079 0.0844  0.1596  66  GLU   B O   
1266 C  CB  . GLU   B 66  ? 0.2238 0.2429 0.2762 -0.0251 0.0514  0.0590  66  GLU   B CB  
1267 C  CG  . GLU   B 66  ? 0.2690 0.2656 0.3187 -0.0116 0.1450  0.0656  66  GLU   B CG  
1268 C  CD  . GLU   B 66  ? 0.1926 0.1004 0.6658 -0.0426 0.0981  0.0347  66  GLU   B CD  
1269 O  OE1 . GLU   B 66  ? 0.2393 0.1788 0.3367 -0.0002 0.0952  0.0078  66  GLU   B OE1 
1270 N  N   . GLY   B 67  ? 0.1999 0.3008 0.3064 -0.0551 0.0396  0.1088  67  GLY   B N   
1271 C  CA  . GLY   B 67  ? 0.2076 0.3303 0.2949 -0.0268 0.0384  0.1290  67  GLY   B CA  
1272 C  C   . GLY   B 67  ? 0.1735 0.2472 0.2928 -0.0778 0.0172  0.0748  67  GLY   B C   
1273 O  O   . GLY   B 67  ? 0.1864 0.1944 0.2709 -0.0172 0.0352  0.0598  67  GLY   B O   
1274 N  N   . ILE   B 68  ? 0.1660 0.2904 0.2941 -0.0500 0.0355  0.0851  68  ILE   B N   
1275 C  CA  . ILE   B 68  ? 0.1753 0.1980 0.2872 -0.0403 0.0084  0.0730  68  ILE   B CA  
1276 C  C   . ILE   B 68  ? 0.1386 0.1916 0.2873 -0.0173 0.0285  0.0559  68  ILE   B C   
1277 O  O   . ILE   B 68  ? 0.1336 0.2620 0.3379 0.0003  0.0392  0.0553  68  ILE   B O   
1278 C  CB  . ILE   B 68  ? 0.1810 0.2201 0.3156 -0.0284 -0.0143 0.0509  68  ILE   B CB  
1279 C  CG1 . ILE   B 68  ? 0.2927 0.2351 0.3274 -0.0546 -0.0080 0.0420  68  ILE   B CG1 
1280 C  CG2 . ILE   B 68  ? 0.2102 0.2902 0.2889 -0.0559 0.0218  0.0522  68  ILE   B CG2 
1281 C  CD1 . ILE   B 68  ? 0.3302 0.2931 0.3467 -0.0575 -0.0506 0.0452  68  ILE   B CD1 
1282 N  N   . TYR   B 69  ? 0.1532 0.1585 0.2772 -0.0022 0.0499  0.0257  69  TYR   B N   
1283 C  CA  . TYR   B 69  ? 0.1387 0.1631 0.2834 0.0053  0.0632  0.0421  69  TYR   B CA  
1284 C  C   . TYR   B 69  ? 0.1267 0.1759 0.2574 0.0069  0.0571  0.0145  69  TYR   B C   
1285 O  O   . TYR   B 69  ? 0.1619 0.1466 0.2905 0.0118  0.0694  0.0483  69  TYR   B O   
1286 C  CB  . TYR   B 69  ? 0.1543 0.1533 0.3092 -0.0066 0.0509  0.0159  69  TYR   B CB  
1287 C  CG  . TYR   B 69  ? 0.1748 0.1568 0.3107 -0.0238 0.0713  0.0862  69  TYR   B CG  
1288 C  CD1 . TYR   B 69  ? 0.1783 0.1574 0.2981 -0.0184 0.0552  0.0269  69  TYR   B CD1 
1289 C  CD2 . TYR   B 69  ? 0.2384 0.2292 0.3248 0.0646  0.1119  0.0663  69  TYR   B CD2 
1290 C  CE1 . TYR   B 69  ? 0.1613 0.1822 0.3431 0.0040  0.0831  0.0755  69  TYR   B CE1 
1291 C  CE2 . TYR   B 69  ? 0.2164 0.2109 0.3119 0.0568  0.1008  0.0690  69  TYR   B CE2 
1292 C  CZ  . TYR   B 69  ? 0.1907 0.2028 0.2957 0.0370  0.0746  0.0635  69  TYR   B CZ  
1293 O  OH  . TYR   B 69  ? 0.2110 0.2432 0.2855 0.0077  0.0928  0.0698  69  TYR   B OH  
1294 N  N   . LYS   B 70  ? 0.1375 0.1511 0.2476 0.0016  0.0703  -0.0061 70  LYS   B N   
1295 C  CA  . LYS   B 70  ? 0.1369 0.1378 0.2459 0.0036  0.0512  0.0217  70  LYS   B CA  
1296 C  C   . LYS   B 70  ? 0.1289 0.1597 0.2594 0.0153  0.0555  0.0086  70  LYS   B C   
1297 O  O   . LYS   B 70  ? 0.1359 0.1880 0.2775 0.0045  0.0608  -0.0133 70  LYS   B O   
1298 C  CB  . LYS   B 70  ? 0.1824 0.1739 0.2843 -0.0139 0.0004  0.0167  70  LYS   B CB  
1299 C  CG  . LYS   B 70  ? 0.2129 0.1673 0.3072 -0.0013 -0.0088 0.0487  70  LYS   B CG  
1300 C  CD  . LYS   B 70  ? 0.2922 0.2024 0.3653 -0.0474 -0.0199 0.0749  70  LYS   B CD  
1301 C  CE  . LYS   B 70  ? 0.2553 0.3750 0.3644 -0.0198 -0.0168 0.1216  70  LYS   B CE  
1302 N  NZ  . LYS   B 70  ? 0.4405 0.5011 0.4721 -0.0062 -0.1398 0.1859  70  LYS   B NZ  
1303 N  N   . VAL   B 71  ? 0.1489 0.1400 0.2321 0.0079  0.0558  0.0064  71  VAL   B N   
1304 C  CA  . VAL   B 71  ? 0.1342 0.1479 0.2236 0.0025  0.0631  -0.0172 71  VAL   B CA  
1305 C  C   . VAL   B 71  ? 0.1325 0.1616 0.2398 -0.0101 0.0642  -0.0122 71  VAL   B C   
1306 O  O   . VAL   B 71  ? 0.1950 0.1691 0.2690 0.0091  0.0955  0.0036  71  VAL   B O   
1307 C  CB  . VAL   B 71  ? 0.1333 0.1754 0.2523 0.0134  0.0479  -0.0154 71  VAL   B CB  
1308 C  CG1 . VAL   B 71  ? 0.2202 0.1830 0.2536 -0.0330 0.0163  -0.0088 71  VAL   B CG1 
1309 C  CG2 . VAL   B 71  ? 0.1946 0.2035 0.2979 0.0357  0.0395  0.0189  71  VAL   B CG2 
1310 N  N   . GLU   B 72  ? 0.1463 0.1481 0.2464 -0.0079 0.0543  -0.0049 72  GLU   B N   
1311 C  CA  . GLU   B 72  ? 0.1499 0.1691 0.2267 -0.0157 0.0215  -0.0195 72  GLU   B CA  
1312 C  C   . GLU   B 72  ? 0.1604 0.1422 0.2062 -0.0125 0.0328  0.0075  72  GLU   B C   
1313 O  O   . GLU   B 72  ? 0.1811 0.1827 0.2392 -0.0263 0.0426  -0.0110 72  GLU   B O   
1314 C  CB  . GLU   B 72  ? 0.1569 0.2298 0.2962 -0.0024 -0.0153 0.0073  72  GLU   B CB  
1315 C  CG  . GLU   B 72  ? 0.1941 0.2485 0.3609 -0.0788 -0.0501 0.0350  72  GLU   B CG  
1316 C  CD  . GLU   B 72  ? 0.3038 0.3010 0.4379 -0.0318 -0.1660 0.0575  72  GLU   B CD  
1317 O  OE1 . GLU   B 72  ? 0.3763 0.3587 0.6399 0.0632  -0.1472 0.1746  72  GLU   B OE1 
1318 O  OE2 . GLU   B 72  ? 0.5328 0.3466 0.4535 -0.0453 -0.2071 0.1800  72  GLU   B OE2 
1319 N  N   . ILE   B 73  ? 0.1600 0.1454 0.1983 -0.0127 0.0274  0.0046  73  ILE   B N   
1320 C  CA  . ILE   B 73  ? 0.1590 0.1507 0.2122 -0.0265 0.0239  -0.0211 73  ILE   B CA  
1321 C  C   . ILE   B 73  ? 0.1415 0.1182 0.2266 -0.0162 0.0208  0.0021  73  ILE   B C   
1322 O  O   . ILE   B 73  ? 0.1780 0.1658 0.2085 -0.0207 0.0114  0.0036  73  ILE   B O   
1323 C  CB  . ILE   B 73  ? 0.1399 0.1732 0.2299 -0.0078 0.0212  0.0132  73  ILE   B CB  
1324 C  CG1 . ILE   B 73  ? 0.1717 0.1768 0.2426 0.0125  0.0323  0.0215  73  ILE   B CG1 
1325 C  CG2 . ILE   B 73  ? 0.1536 0.1981 0.2700 -0.0387 -0.0097 0.0141  73  ILE   B CG2 
1326 C  CD1 . ILE   B 73  ? 0.1864 0.2027 0.2878 0.0594  0.0363  -0.0038 73  ILE   B CD1 
1327 N  N   . ASP   B 74  ? 0.1615 0.1370 0.2260 0.0054  0.0079  -0.0007 74  ASP   B N   
1328 C  CA  . ASP   B 74  ? 0.1372 0.1407 0.2485 -0.0029 0.0225  0.0039  74  ASP   B CA  
1329 C  C   . ASP   B 74  ? 0.1422 0.1469 0.2681 0.0042  0.0072  0.0236  74  ASP   B C   
1330 O  O   . ASP   B 74  ? 0.1601 0.1571 0.2704 -0.0094 0.0142  0.0047  74  ASP   B O   
1331 C  CB  . ASP   B 74  ? 0.1397 0.1623 0.3240 0.0241  0.0531  0.0004  74  ASP   B CB  
1332 C  CG  . ASP   B 74  ? 0.1511 0.1709 0.4170 0.0405  0.0685  0.0496  74  ASP   B CG  
1333 O  OD1 . ASP   B 74  ? 0.1805 0.1791 0.3887 0.0057  0.0161  0.0501  74  ASP   B OD1 
1334 O  OD2 . ASP   B 74  ? 0.2155 0.2357 0.4990 0.0794  0.1143  0.0808  74  ASP   B OD2 
1335 N  N   . THR   B 75  ? 0.1289 0.1440 0.2457 -0.0065 0.0090  0.0007  75  THR   B N   
1336 C  CA  . THR   B 75  ? 0.1345 0.1451 0.2198 -0.0082 -0.0200 0.0164  75  THR   B CA  
1337 C  C   . THR   B 75  ? 0.1240 0.1248 0.2330 0.0008  0.0063  0.0166  75  THR   B C   
1338 O  O   . THR   B 75  ? 0.1384 0.1213 0.2379 -0.0084 0.0009  0.0028  75  THR   B O   
1339 C  CB  . THR   B 75  ? 0.1349 0.1268 0.2591 -0.0122 0.0023  0.0051  75  THR   B CB  
1340 O  OG1 . THR   B 75  ? 0.1473 0.1260 0.2421 -0.0129 0.0083  -0.0101 75  THR   B OG1 
1341 C  CG2 . THR   B 75  ? 0.1642 0.1276 0.2764 0.0038  0.0058  0.0304  75  THR   B CG2 
1342 N  N   . LYS   B 76  ? 0.1167 0.1225 0.2418 -0.0056 0.0032  0.0158  76  LYS   B N   
1343 C  CA  . LYS   B 76  ? 0.1442 0.1494 0.2283 -0.0010 0.0049  0.0154  76  LYS   B CA  
1344 C  C   . LYS   B 76  ? 0.1598 0.1276 0.2284 0.0111  -0.0066 0.0183  76  LYS   B C   
1345 O  O   . LYS   B 76  ? 0.1582 0.1308 0.2671 -0.0082 -0.0176 0.0119  76  LYS   B O   
1346 C  CB  . LYS   B 76  ? 0.1611 0.1311 0.2655 0.0134  -0.0099 0.0298  76  LYS   B CB  
1347 C  CG  . LYS   B 76  ? 0.2193 0.1420 0.3306 -0.0025 -0.0855 0.0153  76  LYS   B CG  
1348 C  CD  . LYS   B 76  ? 0.2327 0.1829 0.3924 0.0183  -0.1354 0.0211  76  LYS   B CD  
1349 C  CE  . LYS   B 76  ? 0.3546 0.2702 0.4703 -0.0417 -0.1728 0.0893  76  LYS   B CE  
1350 N  NZ  . LYS   B 76  ? 0.4639 0.2323 0.5874 0.0690  -0.3249 -0.0286 76  LYS   B NZ  
1351 N  N   . SER   B 77  ? 0.1748 0.1145 0.2403 0.0045  0.0094  0.0065  77  SER   B N   
1352 C  CA  . SER   B 77  ? 0.1472 0.1384 0.2898 0.0181  0.0138  0.0131  77  SER   B CA  
1353 C  C   . SER   B 77  ? 0.1674 0.1290 0.2579 0.0054  0.0287  0.0201  77  SER   B C   
1354 O  O   . SER   B 77  ? 0.1826 0.1303 0.2953 0.0117  0.0188  0.0077  77  SER   B O   
1355 C  CB  . SER   B 77  ? 0.1611 0.2314 0.3418 0.0237  0.0426  0.0447  77  SER   B CB  
1356 O  OG  . SER   B 77  ? 0.1976 0.2250 0.4186 0.0568  0.0530  0.0349  77  SER   B OG  
1357 N  N   . TYR   B 78  ? 0.1785 0.1386 0.2404 0.0123  0.0091  -0.0043 78  TYR   B N   
1358 C  CA  . TYR   B 78  ? 0.2013 0.1291 0.2192 0.0053  0.0135  -0.0112 78  TYR   B CA  
1359 C  C   . TYR   B 78  ? 0.1665 0.1031 0.2440 0.0173  -0.0215 -0.0007 78  TYR   B C   
1360 O  O   . TYR   B 78  ? 0.1975 0.1219 0.2470 0.0004  -0.0199 -0.0201 78  TYR   B O   
1361 C  CB  . TYR   B 78  ? 0.1982 0.1354 0.2349 0.0196  -0.0048 0.0168  78  TYR   B CB  
1362 C  CG  . TYR   B 78  ? 0.2058 0.1067 0.2185 0.0118  0.0083  0.0041  78  TYR   B CG  
1363 C  CD1 . TYR   B 78  ? 0.1655 0.1469 0.2247 0.0253  0.0112  -0.0136 78  TYR   B CD1 
1364 C  CD2 . TYR   B 78  ? 0.2059 0.1449 0.2071 0.0209  0.0142  -0.0044 78  TYR   B CD2 
1365 C  CE1 . TYR   B 78  ? 0.1897 0.1651 0.2429 0.0292  0.0295  0.0077  78  TYR   B CE1 
1366 C  CE2 . TYR   B 78  ? 0.1925 0.1431 0.2551 0.0569  0.0235  0.0040  78  TYR   B CE2 
1367 C  CZ  . TYR   B 78  ? 0.1392 0.1811 0.2578 0.0334  0.0017  0.0112  78  TYR   B CZ  
1368 O  OH  . TYR   B 78  ? 0.1678 0.2015 0.2604 0.0526  0.0071  0.0080  78  TYR   B OH  
1369 N  N   . TRP   B 79  ? 0.1541 0.1100 0.2326 0.0029  -0.0183 -0.0070 79  TRP   B N   
1370 C  CA  . TRP   B 79  ? 0.1618 0.0900 0.2239 -0.0071 0.0091  -0.0202 79  TRP   B CA  
1371 C  C   . TRP   B 79  ? 0.1704 0.1033 0.2395 0.0099  -0.0085 -0.0205 79  TRP   B C   
1372 O  O   . TRP   B 79  ? 0.1736 0.0859 0.2623 0.0039  -0.0158 0.0004  79  TRP   B O   
1373 C  CB  . TRP   B 79  ? 0.1459 0.0889 0.2389 0.0126  -0.0228 0.0059  79  TRP   B CB  
1374 C  CG  . TRP   B 79  ? 0.1269 0.1183 0.2101 -0.0037 -0.0035 -0.0022 79  TRP   B CG  
1375 C  CD1 . TRP   B 79  ? 0.1388 0.1041 0.2165 0.0184  -0.0133 0.0021  79  TRP   B CD1 
1376 C  CD2 . TRP   B 79  ? 0.1199 0.1014 0.2100 -0.0152 -0.0010 -0.0116 79  TRP   B CD2 
1377 N  NE1 . TRP   B 79  ? 0.1354 0.0925 0.2099 -0.0036 -0.0038 -0.0091 79  TRP   B NE1 
1378 C  CE2 . TRP   B 79  ? 0.1199 0.1022 0.2145 0.0013  0.0045  -0.0093 79  TRP   B CE2 
1379 C  CE3 . TRP   B 79  ? 0.1402 0.1063 0.2188 -0.0149 -0.0196 -0.0244 79  TRP   B CE3 
1380 C  CZ2 . TRP   B 79  ? 0.1265 0.1202 0.2164 0.0157  0.0060  -0.0013 79  TRP   B CZ2 
1381 C  CZ3 . TRP   B 79  ? 0.1167 0.1342 0.2611 -0.0023 -0.0059 -0.0168 79  TRP   B CZ3 
1382 C  CH2 . TRP   B 79  ? 0.1237 0.1254 0.2555 -0.0029 -0.0131 -0.0191 79  TRP   B CH2 
1383 N  N   . LYS   B 80  ? 0.1738 0.0983 0.2547 0.0073  0.0008  0.0088  80  LYS   B N   
1384 C  CA  . LYS   B 80  ? 0.2159 0.1050 0.2558 0.0023  -0.0121 0.0029  80  LYS   B CA  
1385 C  C   . LYS   B 80  ? 0.2039 0.1018 0.2816 0.0057  0.0142  0.0026  80  LYS   B C   
1386 O  O   . LYS   B 80  ? 0.2239 0.1073 0.3111 0.0175  0.0082  -0.0121 80  LYS   B O   
1387 C  CB  . LYS   B 80  ? 0.1771 0.1234 0.3274 0.0466  -0.0215 0.0032  80  LYS   B CB  
1388 C  CG  . LYS   B 80  ? 0.1978 0.1495 0.3188 0.0225  -0.0478 0.0523  80  LYS   B CG  
1389 C  CD  . LYS   B 80  ? 0.1851 0.2473 0.4560 0.0014  -0.0289 0.0492  80  LYS   B CD  
1390 C  CE  . LYS   B 80  ? 0.1402 0.2793 0.4455 0.0169  -0.0633 0.0582  80  LYS   B CE  
1391 N  NZ  . LYS   B 80  ? 0.2754 0.3747 0.5429 -0.1350 -0.0531 0.1763  80  LYS   B NZ  
1392 N  N   . ALA   B 81  ? 0.2104 0.1254 0.2772 0.0106  0.0056  -0.0231 81  ALA   B N   
1393 C  CA  . ALA   B 81  ? 0.2998 0.1631 0.2658 -0.0336 0.0180  -0.0370 81  ALA   B CA  
1394 C  C   . ALA   B 81  ? 0.3075 0.1517 0.3176 -0.0122 -0.0605 -0.0323 81  ALA   B C   
1395 O  O   . ALA   B 81  ? 0.3419 0.1953 0.3943 -0.0567 -0.0301 -0.0942 81  ALA   B O   
1396 C  CB  . ALA   B 81  ? 0.3032 0.2100 0.2519 -0.0222 0.0307  -0.0157 81  ALA   B CB  
1397 N  N   . LEU   B 82  ? 0.2489 0.1501 0.3327 -0.0213 -0.0753 -0.0078 82  LEU   B N   
1398 C  CA  . LEU   B 82  ? 0.2241 0.1407 0.3178 -0.0195 -0.0785 -0.0224 82  LEU   B CA  
1399 C  C   . LEU   B 82  ? 0.2180 0.1462 0.3307 0.0000  -0.0665 -0.0073 82  LEU   B C   
1400 O  O   . LEU   B 82  ? 0.2087 0.1907 0.3633 -0.0199 -0.0429 -0.0066 82  LEU   B O   
1401 C  CB  . LEU   B 82  ? 0.2117 0.1782 0.3254 0.0071  -0.0912 -0.0292 82  LEU   B CB  
1402 C  CG  . LEU   B 82  ? 0.3756 0.2221 0.3807 -0.0312 -0.1896 0.0044  82  LEU   B CG  
1403 C  CD1 . LEU   B 82  ? 0.4654 0.1966 0.4619 0.0126  -0.2110 -0.0043 82  LEU   B CD1 
1404 C  CD2 . LEU   B 82  ? 0.3956 0.2584 0.3749 -0.0242 -0.1409 0.0028  82  LEU   B CD2 
1405 N  N   . GLY   B 83  ? 0.2186 0.1502 0.3044 -0.0028 -0.0440 -0.0331 83  GLY   B N   
1406 C  CA  . GLY   B 83  ? 0.2021 0.1325 0.2958 -0.0141 -0.0374 -0.0059 83  GLY   B CA  
1407 C  C   . GLY   B 83  ? 0.2022 0.1059 0.3360 0.0034  -0.0194 0.0041  83  GLY   B C   
1408 O  O   . GLY   B 83  ? 0.2561 0.1192 0.3537 -0.0319 0.0116  0.0384  83  GLY   B O   
1409 N  N   . ILE   B 84  ? 0.1729 0.1213 0.2888 -0.0043 -0.0247 0.0096  84  ILE   B N   
1410 C  CA  . ILE   B 84  ? 0.1717 0.1357 0.2760 -0.0069 -0.0146 0.0056  84  ILE   B CA  
1411 C  C   . ILE   B 84  ? 0.1766 0.1055 0.2613 -0.0102 -0.0033 -0.0077 84  ILE   B C   
1412 O  O   . ILE   B 84  ? 0.1867 0.1143 0.2658 -0.0101 -0.0081 0.0123  84  ILE   B O   
1413 C  CB  . ILE   B 84  ? 0.1660 0.1250 0.3413 0.0183  -0.0529 -0.0151 84  ILE   B CB  
1414 C  CG1 . ILE   B 84  ? 0.1761 0.1551 0.3527 0.0062  -0.0577 -0.0144 84  ILE   B CG1 
1415 C  CG2 . ILE   B 84  ? 0.2594 0.1825 0.4404 0.0999  -0.1238 -0.1102 84  ILE   B CG2 
1416 C  CD1 . ILE   B 84  ? 0.2213 0.1587 0.4240 -0.0038 -0.0777 -0.0071 84  ILE   B CD1 
1417 N  N   . SER   B 85  ? 0.1839 0.1060 0.2779 -0.0047 0.0139  -0.0091 85  SER   B N   
1418 C  CA  A SER   B 85  ? 0.1809 0.1064 0.2800 0.0196  -0.0067 0.0009  85  SER   B CA  
1419 C  CA  B SER   B 85  ? 0.1724 0.1076 0.2790 0.0063  -0.0065 0.0173  85  SER   B CA  
1420 C  C   . SER   B 85  ? 0.1333 0.1135 0.2754 0.0145  -0.0104 -0.0091 85  SER   B C   
1421 O  O   . SER   B 85  ? 0.1643 0.1069 0.3219 0.0028  -0.0063 -0.0256 85  SER   B O   
1422 C  CB  A SER   B 85  ? 0.3175 0.0785 0.3049 0.0741  0.0054  -0.0069 85  SER   B CB  
1423 C  CB  B SER   B 85  ? 0.1474 0.2494 0.2957 -0.0430 0.0514  0.0344  85  SER   B CB  
1424 O  OG  A SER   B 85  ? 0.2482 0.0733 0.2886 -0.0053 0.0154  0.0182  85  SER   B OG  
1425 O  OG  B SER   B 85  ? 0.2590 0.2179 0.3829 0.0049  -0.0312 0.0216  85  SER   B OG  
1426 N  N   . PRO   B 86  ? 0.1395 0.1266 0.2621 0.0134  -0.0172 -0.0014 86  PRO   B N   
1427 C  CA  . PRO   B 86  ? 0.1914 0.0957 0.2805 -0.0071 -0.0639 0.0081  86  PRO   B CA  
1428 C  C   . PRO   B 86  ? 0.1266 0.1284 0.2444 0.0060  -0.0531 0.0219  86  PRO   B C   
1429 O  O   . PRO   B 86  ? 0.1833 0.1469 0.2863 0.0290  -0.0600 -0.0017 86  PRO   B O   
1430 C  CB  . PRO   B 86  ? 0.3289 0.1230 0.2391 -0.0503 -0.0771 0.0100  86  PRO   B CB  
1431 C  CG  . PRO   B 86  ? 0.2826 0.1386 0.2688 -0.0540 -0.0064 0.0154  86  PRO   B CG  
1432 C  CD  . PRO   B 86  ? 0.1485 0.1558 0.2580 -0.0022 -0.0294 0.0034  86  PRO   B CD  
1433 N  N   . PHE   B 87  ? 0.1257 0.1054 0.2177 -0.0083 -0.0382 0.0131  87  PHE   B N   
1434 C  CA  . PHE   B 87  ? 0.1209 0.1525 0.1990 -0.0121 -0.0217 0.0264  87  PHE   B CA  
1435 C  C   . PHE   B 87  ? 0.1116 0.1410 0.1907 -0.0047 -0.0253 -0.0155 87  PHE   B C   
1436 O  O   . PHE   B 87  ? 0.1082 0.1430 0.2311 0.0026  -0.0282 0.0067  87  PHE   B O   
1437 C  CB  . PHE   B 87  ? 0.1294 0.1632 0.2093 -0.0096 -0.0174 -0.0030 87  PHE   B CB  
1438 C  CG  . PHE   B 87  ? 0.1061 0.1868 0.2224 0.0081  -0.0025 -0.0088 87  PHE   B CG  
1439 C  CD1 . PHE   B 87  ? 0.1217 0.2269 0.2437 -0.0086 -0.0169 0.0148  87  PHE   B CD1 
1440 C  CD2 . PHE   B 87  ? 0.1183 0.1788 0.2493 -0.0204 -0.0213 -0.0185 87  PHE   B CD2 
1441 C  CE1 . PHE   B 87  ? 0.1651 0.2515 0.2675 0.0415  -0.0289 -0.0459 87  PHE   B CE1 
1442 C  CE2 . PHE   B 87  ? 0.1211 0.2273 0.2977 -0.0096 -0.0231 -0.0608 87  PHE   B CE2 
1443 C  CZ  . PHE   B 87  ? 0.1309 0.2620 0.2761 0.0378  -0.0605 -0.0866 87  PHE   B CZ  
1444 N  N   . HIS   B 88  ? 0.1033 0.1508 0.1808 -0.0259 -0.0162 0.0030  88  HIS   B N   
1445 C  CA  . HIS   B 88  ? 0.1231 0.1049 0.2089 -0.0260 0.0022  0.0030  88  HIS   B CA  
1446 C  C   . HIS   B 88  ? 0.1381 0.1200 0.2117 -0.0002 -0.0208 -0.0095 88  HIS   B C   
1447 O  O   . HIS   B 88  ? 0.1268 0.1421 0.2277 -0.0110 -0.0158 -0.0265 88  HIS   B O   
1448 C  CB  . HIS   B 88  ? 0.1230 0.1158 0.2324 -0.0247 -0.0015 -0.0171 88  HIS   B CB  
1449 C  CG  . HIS   B 88  ? 0.1253 0.1281 0.2858 -0.0120 -0.0107 -0.0217 88  HIS   B CG  
1450 N  ND1 . HIS   B 88  ? 0.1357 0.1990 0.3937 0.0027  0.0135  -0.0340 88  HIS   B ND1 
1451 C  CD2 . HIS   B 88  ? 0.0971 0.1146 0.2586 -0.0133 -0.0516 0.0116  88  HIS   B CD2 
1452 C  CE1 . HIS   B 88  ? 0.1326 0.0962 0.3728 -0.0092 0.0113  -0.0616 88  HIS   B CE1 
1453 N  NE2 . HIS   B 88  ? 0.2618 0.1451 0.3944 0.0482  -0.0253 -0.0402 88  HIS   B NE2 
1454 N  N   . GLU   B 89  ? 0.1102 0.1406 0.2233 -0.0105 -0.0055 -0.0052 89  GLU   B N   
1455 C  CA  . GLU   B 89  ? 0.1289 0.1381 0.2292 -0.0181 0.0145  -0.0122 89  GLU   B CA  
1456 C  C   . GLU   B 89  ? 0.1541 0.1423 0.2413 -0.0367 0.0249  -0.0254 89  GLU   B C   
1457 O  O   . GLU   B 89  ? 0.2918 0.1517 0.2559 -0.0194 0.0639  -0.0380 89  GLU   B O   
1458 C  CB  . GLU   B 89  ? 0.1287 0.1898 0.2495 -0.0091 0.0089  -0.0288 89  GLU   B CB  
1459 C  CG  . GLU   B 89  ? 0.1390 0.2216 0.2919 0.0059  -0.0154 -0.0159 89  GLU   B CG  
1460 C  CD  . GLU   B 89  ? 0.2109 0.2392 0.2764 0.0511  -0.0070 0.0142  89  GLU   B CD  
1461 O  OE1 . GLU   B 89  ? 0.2696 0.2581 0.3991 0.0639  0.0423  -0.0322 89  GLU   B OE1 
1462 O  OE2 . GLU   B 89  ? 0.2409 0.2148 0.3279 0.0203  -0.0283 -0.0038 89  GLU   B OE2 
1463 N  N   . HIS   B 90  ? 0.1487 0.1699 0.2204 -0.0329 -0.0065 -0.0066 90  HIS   B N   
1464 C  CA  . HIS   B 90  ? 0.1687 0.1522 0.2124 -0.0364 0.0097  -0.0043 90  HIS   B CA  
1465 C  C   . HIS   B 90  ? 0.2682 0.1537 0.1934 -0.0435 0.0094  -0.0096 90  HIS   B C   
1466 O  O   . HIS   B 90  ? 0.2981 0.1775 0.2051 -0.0272 0.0127  -0.0086 90  HIS   B O   
1467 C  CB  . HIS   B 90  ? 0.1952 0.2154 0.2358 -0.0555 -0.0031 0.0222  90  HIS   B CB  
1468 C  CG  . HIS   B 90  ? 0.2309 0.3312 0.3266 -0.1399 -0.0181 0.0944  90  HIS   B CG  
1469 N  ND1 . HIS   B 90  ? 0.3494 0.4110 0.4999 -0.2325 -0.0689 -0.0644 90  HIS   B ND1 
1470 C  CD2 . HIS   B 90  ? 0.2383 0.3700 0.3559 -0.0912 -0.0565 0.0976  90  HIS   B CD2 
1471 C  CE1 . HIS   B 90  ? 0.3392 0.4026 0.5859 -0.2089 -0.1409 0.0208  90  HIS   B CE1 
1472 N  NE2 . HIS   B 90  ? 0.2816 0.5366 0.4783 -0.1409 -0.1028 0.0442  90  HIS   B NE2 
1473 N  N   . ALA   B 91  ? 0.2939 0.1654 0.1974 0.0005  0.0379  0.0023  91  ALA   B N   
1474 C  CA  . ALA   B 91  ? 0.3292 0.1674 0.2235 -0.0051 0.0668  0.0013  91  ALA   B CA  
1475 C  C   . ALA   B 91  ? 0.3365 0.1383 0.2588 0.0157  0.0862  0.0122  91  ALA   B C   
1476 O  O   . ALA   B 91  ? 0.2990 0.1851 0.2506 -0.0108 0.0693  -0.0113 91  ALA   B O   
1477 C  CB  . ALA   B 91  ? 0.3799 0.1688 0.2623 0.0612  0.0881  0.0112  91  ALA   B CB  
1478 N  N   . GLU   B 92  ? 0.5625 0.1242 0.2706 -0.0709 0.1203  0.0169  92  GLU   B N   
1479 C  CA  . GLU   B 92  ? 0.4232 0.1679 0.2901 -0.0375 0.0992  0.0073  92  GLU   B CA  
1480 C  C   . GLU   B 92  ? 0.5188 0.1571 0.2964 -0.0677 0.1853  0.0049  92  GLU   B C   
1481 O  O   . GLU   B 92  ? 0.6240 0.2317 0.3128 -0.0345 0.2087  0.0205  92  GLU   B O   
1482 C  CB  . GLU   B 92  ? 0.4341 0.3472 0.5197 -0.0039 0.0304  0.1675  92  GLU   B CB  
1483 N  N   . VAL   B 93  ? 0.2803 0.1684 0.2624 -0.0714 0.1075  -0.0071 93  VAL   B N   
1484 C  CA  . VAL   B 93  ? 0.1425 0.2552 0.2406 -0.0135 0.0362  0.0214  93  VAL   B CA  
1485 C  C   . VAL   B 93  ? 0.1420 0.1194 0.2404 0.0136  0.0578  0.0045  93  VAL   B C   
1486 O  O   . VAL   B 93  ? 0.1713 0.1549 0.2804 -0.0195 0.0721  -0.0469 93  VAL   B O   
1487 C  CB  . VAL   B 93  ? 0.1737 0.2336 0.3102 -0.0114 0.0379  0.0003  93  VAL   B CB  
1488 C  CG1 . VAL   B 93  ? 0.2642 0.2354 0.3620 0.0431  0.0111  -0.0657 93  VAL   B CG1 
1489 C  CG2 . VAL   B 93  ? 0.1965 0.3433 0.3711 -0.0442 0.0098  0.0076  93  VAL   B CG2 
1490 N  N   . VAL   B 94  ? 0.1266 0.1695 0.2221 0.0184  0.0417  0.0124  94  VAL   B N   
1491 C  CA  . VAL   B 94  ? 0.1188 0.1254 0.2592 0.0041  0.0414  0.0081  94  VAL   B CA  
1492 C  C   . VAL   B 94  ? 0.1283 0.1727 0.1978 -0.0058 0.0169  -0.0039 94  VAL   B C   
1493 O  O   . VAL   B 94  ? 0.1485 0.1395 0.2345 0.0036  0.0270  0.0051  94  VAL   B O   
1494 C  CB  . VAL   B 94  ? 0.1465 0.1592 0.2548 0.0196  -0.0025 0.0090  94  VAL   B CB  
1495 C  CG1 . VAL   B 94  ? 0.1324 0.2484 0.3167 -0.0252 0.0073  -0.0162 94  VAL   B CG1 
1496 C  CG2 . VAL   B 94  ? 0.2106 0.1957 0.2870 0.0235  -0.0046 0.0335  94  VAL   B CG2 
1497 N  N   . PHE   B 95  ? 0.1349 0.1488 0.2220 0.0102  0.0445  0.0038  95  PHE   B N   
1498 C  CA  . PHE   B 95  ? 0.1605 0.1375 0.2228 -0.0018 0.0268  0.0068  95  PHE   B CA  
1499 C  C   . PHE   B 95  ? 0.1400 0.1470 0.2529 -0.0026 0.0256  0.0140  95  PHE   B C   
1500 O  O   . PHE   B 95  ? 0.1682 0.1586 0.2812 0.0107  0.0569  0.0338  95  PHE   B O   
1501 C  CB  . PHE   B 95  ? 0.1568 0.1428 0.2511 -0.0014 0.0193  -0.0005 95  PHE   B CB  
1502 C  CG  . PHE   B 95  ? 0.1533 0.1704 0.2486 0.0243  0.0364  0.0073  95  PHE   B CG  
1503 C  CD1 . PHE   B 95  ? 0.1616 0.1720 0.2886 0.0064  0.0011  -0.0208 95  PHE   B CD1 
1504 C  CD2 . PHE   B 95  ? 0.1938 0.2136 0.2511 -0.0053 0.0363  -0.0166 95  PHE   B CD2 
1505 C  CE1 . PHE   B 95  ? 0.1874 0.2275 0.3313 0.0233  0.0135  -0.0753 95  PHE   B CE1 
1506 C  CE2 . PHE   B 95  ? 0.2280 0.3380 0.2701 0.0346  0.0447  -0.0329 95  PHE   B CE2 
1507 C  CZ  . PHE   B 95  ? 0.1973 0.2670 0.3071 0.0119  0.0666  -0.0555 95  PHE   B CZ  
1508 N  N   . THR   B 96  ? 0.2076 0.1373 0.2944 -0.0139 0.0609  -0.0024 96  THR   B N   
1509 C  CA  . THR   B 96  ? 0.2032 0.1781 0.2822 -0.0186 0.0512  0.0705  96  THR   B CA  
1510 C  C   . THR   B 96  ? 0.2010 0.1463 0.3539 0.0130  0.0825  0.0571  96  THR   B C   
1511 O  O   . THR   B 96  ? 0.2213 0.2323 0.3073 0.0630  0.0434  0.0448  96  THR   B O   
1512 C  CB  . THR   B 96  ? 0.2519 0.1263 0.3369 -0.0204 0.0223  0.0273  96  THR   B CB  
1513 O  OG1 . THR   B 96  ? 0.2788 0.1868 0.3306 -0.0357 0.0546  0.0420  96  THR   B OG1 
1514 C  CG2 . THR   B 96  ? 0.3472 0.2075 0.3320 -0.0521 0.0609  0.0826  96  THR   B CG2 
1515 N  N   . ALA   B 97  ? 0.1962 0.1998 0.2710 0.0053  0.0358  0.0376  97  ALA   B N   
1516 C  CA  . ALA   B 97  ? 0.1839 0.2128 0.3272 0.0125  0.0444  0.0127  97  ALA   B CA  
1517 C  C   . ALA   B 97  ? 0.1591 0.3020 0.3447 0.0187  0.0505  0.0840  97  ALA   B C   
1518 O  O   . ALA   B 97  ? 0.2126 0.3120 0.3588 -0.0202 0.0480  0.1366  97  ALA   B O   
1519 C  CB  . ALA   B 97  ? 0.2759 0.3218 0.2963 0.0852  -0.0207 -0.0052 97  ALA   B CB  
1520 N  N   . ASN   B 98  ? 0.2124 0.2779 0.3614 -0.0055 0.0382  0.1048  98  ASN   B N   
1521 C  CA  . ASN   B 98  ? 0.2373 0.2254 0.4110 0.0360  0.0529  0.0802  98  ASN   B CA  
1522 C  C   . ASN   B 98  ? 0.4154 0.1695 0.4447 -0.0473 0.1737  0.0156  98  ASN   B C   
1523 O  O   . ASN   B 98  ? 0.4034 0.2461 0.5814 -0.0818 0.2022  0.0667  98  ASN   B O   
1524 C  CB  . ASN   B 98  ? 0.2229 0.2741 0.3528 -0.0270 0.0374  0.0559  98  ASN   B CB  
1525 C  CG  . ASN   B 98  ? 0.2459 0.3853 0.3295 -0.0692 0.0532  -0.0762 98  ASN   B CG  
1526 O  OD1 . ASN   B 98  ? 0.2464 0.2421 0.3670 -0.0029 0.0315  0.0592  98  ASN   B OD1 
1527 N  ND2 . ASN   B 98  ? 0.3439 0.6984 0.4614 0.0782  0.1249  -0.2025 98  ASN   B ND2 
1528 N  N   . ASP   B 99  ? 0.2298 0.1003 0.3699 -0.0178 0.0884  0.0443  99  ASP   B N   
1529 C  CA  . ASP   B 99  ? 0.2089 0.1973 0.3949 -0.0186 0.0762  -0.0110 99  ASP   B CA  
1530 C  C   . ASP   B 99  ? 0.4529 0.1858 0.3564 -0.0360 0.1030  0.0656  99  ASP   B C   
1531 O  O   . ASP   B 99  ? 0.2895 0.1875 0.4152 -0.0008 0.1317  0.0190  99  ASP   B O   
1532 C  CB  . ASP   B 99  ? 0.3865 0.2351 0.3331 -0.1180 0.0382  -0.0818 99  ASP   B CB  
1533 N  N   . SER   B 100 ? 0.4983 0.2506 0.4709 0.0817  0.0454  -0.0502 100 SER   B N   
1534 C  CA  . SER   B 100 ? 0.6235 0.2697 0.6043 0.1844  0.0389  -0.0481 100 SER   B CA  
1535 C  C   . SER   B 100 ? 0.9281 0.3412 0.6078 -0.0413 0.0541  -0.1955 100 SER   B C   
1536 C  CB  . SER   B 100 ? 0.5240 0.3379 0.5908 0.1264  0.0411  -0.0746 100 SER   B CB  
1537 O  OG  . SER   B 100 ? 0.6211 0.2757 0.5565 0.0635  0.1172  0.0111  100 SER   B OG  
1538 N  N   . GLY   B 101 ? 0.3468 0.2302 0.5831 -0.0636 0.0097  0.1457  101 GLY   B N   
1539 C  CA  . GLY   B 101 ? 0.5681 0.2720 0.5302 -0.0521 0.0610  0.1482  101 GLY   B CA  
1540 C  C   . GLY   B 101 ? 0.6891 0.3022 0.4743 -0.0160 0.2510  0.1253  101 GLY   B C   
1541 O  O   . GLY   B 101 ? 0.3840 0.3097 0.4301 -0.0760 0.0331  0.1013  101 GLY   B O   
1542 N  N   . PRO   B 102 ? 0.3207 0.2715 0.4372 -0.0129 0.0570  0.1343  102 PRO   B N   
1543 C  CA  . PRO   B 102 ? 0.3655 0.2397 0.4941 -0.0203 0.0517  0.0813  102 PRO   B CA  
1544 C  C   . PRO   B 102 ? 0.2884 0.3023 0.5579 0.0397  0.0411  0.2007  102 PRO   B C   
1545 O  O   . PRO   B 102 ? 0.3871 0.3227 0.5916 0.0717  0.0588  0.2220  102 PRO   B O   
1546 C  CB  . PRO   B 102 ? 0.4180 0.2612 0.4880 0.0142  0.1421  0.1019  102 PRO   B CB  
1547 C  CG  . PRO   B 102 ? 0.5119 0.3190 0.5539 -0.1574 0.1401  0.0502  102 PRO   B CG  
1548 C  CD  . PRO   B 102 ? 0.3771 0.3205 0.4515 -0.0057 0.1167  0.1309  102 PRO   B CD  
1549 N  N   . ARG   B 103 ? 0.1810 0.2196 0.3159 0.0342  0.0221  0.1016  103 ARG   B N   
1550 C  CA  . ARG   B 103 ? 0.1872 0.1657 0.3507 0.0349  0.1026  0.0653  103 ARG   B CA  
1551 C  C   . ARG   B 103 ? 0.3725 0.1802 0.2461 0.1307  0.0266  0.0515  103 ARG   B C   
1552 O  O   . ARG   B 103 ? 0.3052 0.1377 0.4368 -0.0194 0.1753  0.0364  103 ARG   B O   
1553 C  CB  . ARG   B 103 ? 0.2551 0.2114 0.4039 0.1011  0.1107  0.0626  103 ARG   B CB  
1554 C  CG  . ARG   B 103 ? 0.3291 0.1719 0.4106 0.0440  0.1465  0.1066  103 ARG   B CG  
1555 C  CD  . ARG   B 103 ? 0.2794 0.1972 0.3999 0.0393  0.1348  0.0609  103 ARG   B CD  
1556 N  NE  . ARG   B 103 ? 0.4626 0.2665 0.4378 0.1691  0.0602  -0.0200 103 ARG   B NE  
1557 C  CZ  . ARG   B 103 ? 0.5839 0.2231 0.5747 0.1770  0.1430  0.0636  103 ARG   B CZ  
1558 N  NH1 . ARG   B 103 ? 0.3914 0.2152 0.5500 0.0929  0.0484  0.0874  103 ARG   B NH1 
1559 N  NH2 . ARG   B 103 ? 0.3589 0.2995 0.6679 0.1602  -0.1830 -0.0371 103 ARG   B NH2 
1560 N  N   . ARG   B 104 ? 0.3743 0.2319 0.3019 -0.0044 0.1053  0.0134  104 ARG   B N   
1561 C  CA  . ARG   B 104 ? 0.2674 0.2002 0.3418 0.0339  0.1421  0.0131  104 ARG   B CA  
1562 C  C   . ARG   B 104 ? 0.2544 0.1952 0.3165 -0.0042 0.1456  0.0199  104 ARG   B C   
1563 O  O   . ARG   B 104 ? 0.3094 0.2011 0.3113 0.0618  0.1165  0.0700  104 ARG   B O   
1564 C  CB  . ARG   B 104 ? 0.4879 0.3231 0.2748 -0.0897 0.0777  0.0443  104 ARG   B CB  
1565 N  N   . TYR   B 105 ? 0.1922 0.1721 0.2877 0.0123  0.0808  -0.0218 105 TYR   B N   
1566 C  CA  . TYR   B 105 ? 0.1784 0.1931 0.2656 0.0065  0.0642  0.0040  105 TYR   B CA  
1567 C  C   . TYR   B 105 ? 0.2094 0.1602 0.2569 0.0139  0.0660  0.0041  105 TYR   B C   
1568 O  O   . TYR   B 105 ? 0.2283 0.1827 0.2870 0.0127  0.0935  -0.0004 105 TYR   B O   
1569 C  CB  . TYR   B 105 ? 0.1982 0.2191 0.2684 0.0135  0.0350  -0.0266 105 TYR   B CB  
1570 C  CG  . TYR   B 105 ? 0.1904 0.1991 0.3180 0.0017  0.0207  -0.0100 105 TYR   B CG  
1571 C  CD1 . TYR   B 105 ? 0.2623 0.2483 0.3360 -0.0031 -0.0050 -0.0103 105 TYR   B CD1 
1572 C  CD2 . TYR   B 105 ? 0.2092 0.2170 0.3433 -0.0260 0.0401  0.0060  105 TYR   B CD2 
1573 C  CE1 . TYR   B 105 ? 0.3017 0.2540 0.3208 -0.0201 -0.0135 -0.0145 105 TYR   B CE1 
1574 C  CE2 . TYR   B 105 ? 0.2388 0.2528 0.3640 -0.0496 0.0791  -0.0156 105 TYR   B CE2 
1575 C  CZ  . TYR   B 105 ? 0.1857 0.2165 0.3218 -0.0219 0.0132  -0.0060 105 TYR   B CZ  
1576 O  OH  . TYR   B 105 ? 0.2100 0.2576 0.4186 -0.0218 -0.0175 0.0046  105 TYR   B OH  
1577 N  N   . THR   B 106 ? 0.1692 0.1602 0.2201 0.0218  0.0398  -0.0024 106 THR   B N   
1578 C  CA  . THR   B 106 ? 0.1923 0.1422 0.2380 0.0124  0.0465  0.0156  106 THR   B CA  
1579 C  C   . THR   B 106 ? 0.2221 0.1330 0.2206 0.0330  0.0465  0.0168  106 THR   B C   
1580 O  O   . THR   B 106 ? 0.2282 0.1535 0.2372 0.0396  0.0484  0.0036  106 THR   B O   
1581 C  CB  . THR   B 106 ? 0.1716 0.2351 0.2502 -0.0024 0.0359  0.0061  106 THR   B CB  
1582 O  OG1 . THR   B 106 ? 0.2660 0.3069 0.2942 0.0345  0.0068  0.0005  106 THR   B OG1 
1583 C  CG2 . THR   B 106 ? 0.2221 0.2569 0.3396 -0.0491 0.0253  -0.0242 106 THR   B CG2 
1584 N  N   . ILE   B 107 ? 0.2060 0.1346 0.2048 0.0206  0.0262  -0.0074 107 ILE   B N   
1585 C  CA  . ILE   B 107 ? 0.2567 0.0981 0.2158 0.0179  0.0317  -0.0316 107 ILE   B CA  
1586 C  C   . ILE   B 107 ? 0.2649 0.1076 0.1938 0.0216  0.0364  -0.0160 107 ILE   B C   
1587 O  O   . ILE   B 107 ? 0.2418 0.1361 0.2338 -0.0100 0.0533  -0.0301 107 ILE   B O   
1588 C  CB  . ILE   B 107 ? 0.2467 0.1235 0.2746 0.0203  0.0006  -0.0152 107 ILE   B CB  
1589 C  CG1 . ILE   B 107 ? 0.3881 0.2523 0.3405 -0.0442 0.0248  -0.0227 107 ILE   B CG1 
1590 C  CG2 . ILE   B 107 ? 0.2893 0.2202 0.2497 0.0317  -0.0138 -0.0011 107 ILE   B CG2 
1591 C  CD1 . ILE   B 107 ? 0.2739 0.2145 0.3783 0.0005  0.0349  -0.0189 107 ILE   B CD1 
1592 N  N   . ALA   B 108 ? 0.2037 0.1301 0.1967 0.0100  0.0135  -0.0201 108 ALA   B N   
1593 C  CA  . ALA   B 108 ? 0.2690 0.1762 0.2090 -0.0628 0.0422  -0.0320 108 ALA   B CA  
1594 C  C   . ALA   B 108 ? 0.2680 0.1364 0.2201 -0.0306 0.0185  -0.0360 108 ALA   B C   
1595 O  O   . ALA   B 108 ? 0.5265 0.1060 0.2100 -0.0291 0.0231  -0.0164 108 ALA   B O   
1596 C  CB  . ALA   B 108 ? 0.2116 0.2878 0.2727 -0.0764 0.0040  0.0054  108 ALA   B CB  
1597 N  N   . ALA   B 109 ? 0.1708 0.1439 0.1928 -0.0373 0.0296  -0.0227 109 ALA   B N   
1598 C  CA  . ALA   B 109 ? 0.1760 0.1213 0.2088 -0.0387 0.0327  -0.0362 109 ALA   B CA  
1599 C  C   . ALA   B 109 ? 0.1400 0.1474 0.1985 -0.0295 0.0087  -0.0113 109 ALA   B C   
1600 O  O   . ALA   B 109 ? 0.1900 0.1955 0.2111 -0.0701 0.0424  -0.0436 109 ALA   B O   
1601 C  CB  . ALA   B 109 ? 0.1438 0.1631 0.2875 -0.0042 0.0122  0.0094  109 ALA   B CB  
1602 N  N   . LEU   B 110 ? 0.1323 0.1152 0.1904 -0.0128 0.0072  0.0000  110 LEU   B N   
1603 C  CA  . LEU   B 110 ? 0.1222 0.1279 0.1796 0.0035  0.0102  0.0249  110 LEU   B CA  
1604 C  C   . LEU   B 110 ? 0.1196 0.1129 0.2024 -0.0112 0.0055  -0.0045 110 LEU   B C   
1605 O  O   . LEU   B 110 ? 0.2052 0.1227 0.2032 0.0246  -0.0296 -0.0075 110 LEU   B O   
1606 C  CB  . LEU   B 110 ? 0.1453 0.1475 0.2045 0.0067  0.0069  0.0244  110 LEU   B CB  
1607 C  CG  . LEU   B 110 ? 0.1389 0.2248 0.2185 0.0050  0.0051  0.0429  110 LEU   B CG  
1608 C  CD1 . LEU   B 110 ? 0.1335 0.2463 0.2662 -0.0249 -0.0106 0.0567  110 LEU   B CD1 
1609 C  CD2 . LEU   B 110 ? 0.1687 0.3384 0.3238 0.0875  0.0692  0.0428  110 LEU   B CD2 
1610 N  N   . LEU   B 111 ? 0.1038 0.1275 0.1878 -0.0086 -0.0236 0.0108  111 LEU   B N   
1611 C  CA  . LEU   B 111 ? 0.1101 0.1209 0.1847 0.0135  -0.0069 0.0011  111 LEU   B CA  
1612 C  C   . LEU   B 111 ? 0.0915 0.1268 0.1846 0.0052  -0.0217 0.0036  111 LEU   B C   
1613 O  O   . LEU   B 111 ? 0.1018 0.1293 0.1867 0.0009  -0.0210 -0.0041 111 LEU   B O   
1614 C  CB  . LEU   B 111 ? 0.1356 0.1408 0.1880 -0.0085 -0.0251 -0.0041 111 LEU   B CB  
1615 C  CG  . LEU   B 111 ? 0.1181 0.1511 0.1845 0.0080  0.0159  0.0300  111 LEU   B CG  
1616 C  CD1 . LEU   B 111 ? 0.1355 0.1679 0.2232 0.0093  0.0134  0.0074  111 LEU   B CD1 
1617 C  CD2 . LEU   B 111 ? 0.1167 0.1525 0.2466 -0.0291 -0.0008 0.0066  111 LEU   B CD2 
1618 N  N   . SER   B 112 ? 0.0980 0.1098 0.1859 -0.0122 -0.0144 -0.0008 112 SER   B N   
1619 C  CA  . SER   B 112 ? 0.1060 0.1189 0.2052 -0.0100 -0.0183 0.0096  112 SER   B CA  
1620 C  C   . SER   B 112 ? 0.0874 0.1026 0.2109 -0.0004 0.0017  0.0030  112 SER   B C   
1621 O  O   . SER   B 112 ? 0.0982 0.1150 0.2224 -0.0081 0.0007  0.0043  112 SER   B O   
1622 C  CB  . SER   B 112 ? 0.0992 0.1330 0.1979 -0.0008 0.0037  0.0288  112 SER   B CB  
1623 O  OG  . SER   B 112 ? 0.1249 0.1619 0.2276 0.0163  -0.0119 0.0194  112 SER   B OG  
1624 N  N   . PRO   B 113 ? 0.1000 0.0996 0.2041 -0.0078 -0.0078 0.0071  113 PRO   B N   
1625 C  CA  . PRO   B 113 ? 0.1190 0.0994 0.2179 -0.0063 -0.0175 0.0211  113 PRO   B CA  
1626 C  C   . PRO   B 113 ? 0.0947 0.1282 0.2265 0.0158  -0.0094 0.0208  113 PRO   B C   
1627 O  O   . PRO   B 113 ? 0.1025 0.1349 0.2247 0.0088  -0.0098 0.0094  113 PRO   B O   
1628 C  CB  . PRO   B 113 ? 0.1249 0.1220 0.2245 0.0143  -0.0192 0.0198  113 PRO   B CB  
1629 C  CG  . PRO   B 113 ? 0.1566 0.1366 0.2214 -0.0102 -0.0227 0.0232  113 PRO   B CG  
1630 C  CD  . PRO   B 113 ? 0.1272 0.1026 0.2117 -0.0180 -0.0162 0.0146  113 PRO   B CD  
1631 N  N   . TYR   B 114 ? 0.0873 0.1004 0.2029 -0.0073 -0.0221 0.0098  114 TYR   B N   
1632 C  CA  . TYR   B 114 ? 0.1138 0.1076 0.2054 -0.0207 -0.0115 0.0288  114 TYR   B CA  
1633 C  C   . TYR   B 114 ? 0.1113 0.1229 0.1915 -0.0242 0.0011  -0.0013 114 TYR   B C   
1634 O  O   . TYR   B 114 ? 0.1695 0.1311 0.2076 -0.0124 -0.0311 0.0133  114 TYR   B O   
1635 C  CB  . TYR   B 114 ? 0.1084 0.1160 0.2054 -0.0172 -0.0128 0.0000  114 TYR   B CB  
1636 C  CG  . TYR   B 114 ? 0.1308 0.1102 0.2043 -0.0162 -0.0191 0.0308  114 TYR   B CG  
1637 C  CD1 . TYR   B 114 ? 0.2266 0.1301 0.2412 -0.0240 -0.0561 0.0180  114 TYR   B CD1 
1638 C  CD2 . TYR   B 114 ? 0.1364 0.1258 0.2091 0.0038  -0.0126 0.0153  114 TYR   B CD2 
1639 C  CE1 . TYR   B 114 ? 0.3251 0.1303 0.2893 0.0118  -0.0893 -0.0171 114 TYR   B CE1 
1640 C  CE2 . TYR   B 114 ? 0.1572 0.1725 0.2451 0.0062  -0.0039 0.0423  114 TYR   B CE2 
1641 C  CZ  . TYR   B 114 ? 0.2697 0.1206 0.2810 0.0185  -0.0425 0.0316  114 TYR   B CZ  
1642 O  OH  . TYR   B 114 ? 0.3606 0.1827 0.3208 0.0871  -0.0548 0.0317  114 TYR   B OH  
1643 N  N   . SER   B 115 ? 0.1294 0.0962 0.1983 -0.0169 -0.0335 0.0117  115 SER   B N   
1644 C  CA  A SER   B 115 ? 0.1181 0.0910 0.2122 -0.0145 -0.0398 0.0210  115 SER   B CA  
1645 C  CA  B SER   B 115 ? 0.1289 0.0891 0.2183 -0.0210 -0.0377 0.0177  115 SER   B CA  
1646 C  C   . SER   B 115 ? 0.1316 0.0877 0.2146 -0.0118 -0.0301 0.0149  115 SER   B C   
1647 O  O   . SER   B 115 ? 0.2381 0.1106 0.2180 -0.0438 -0.0488 0.0039  115 SER   B O   
1648 C  CB  A SER   B 115 ? 0.1122 0.1121 0.2259 0.0006  -0.0467 0.0039  115 SER   B CB  
1649 C  CB  B SER   B 115 ? 0.1345 0.1502 0.2969 -0.0233 0.0084  0.0338  115 SER   B CB  
1650 O  OG  A SER   B 115 ? 0.1037 0.0962 0.2181 0.0239  -0.0146 0.0031  115 SER   B OG  
1651 O  OG  B SER   B 115 ? 0.2703 0.2712 0.5179 -0.0618 -0.0748 -0.0169 115 SER   B OG  
1652 N  N   . TYR   B 116 ? 0.1767 0.0994 0.1862 -0.0204 -0.0512 0.0097  116 TYR   B N   
1653 C  CA  . TYR   B 116 ? 0.1661 0.0965 0.2047 -0.0015 -0.0190 0.0023  116 TYR   B CA  
1654 C  C   . TYR   B 116 ? 0.1429 0.1238 0.1719 -0.0120 0.0051  0.0027  116 TYR   B C   
1655 O  O   . TYR   B 116 ? 0.1830 0.1086 0.1828 0.0001  -0.0240 -0.0026 116 TYR   B O   
1656 C  CB  . TYR   B 116 ? 0.2053 0.0939 0.2045 0.0221  -0.0061 -0.0027 116 TYR   B CB  
1657 C  CG  . TYR   B 116 ? 0.1522 0.1521 0.2403 0.0247  0.0159  -0.0026 116 TYR   B CG  
1658 C  CD1 . TYR   B 116 ? 0.1670 0.1575 0.2710 0.0112  0.0264  -0.0218 116 TYR   B CD1 
1659 C  CD2 . TYR   B 116 ? 0.2113 0.1774 0.2824 0.0515  0.0115  -0.0224 116 TYR   B CD2 
1660 C  CE1 . TYR   B 116 ? 0.1571 0.2162 0.3722 0.0083  0.0343  -0.0626 116 TYR   B CE1 
1661 C  CE2 . TYR   B 116 ? 0.1897 0.2917 0.3142 0.0169  0.0002  -0.0311 116 TYR   B CE2 
1662 C  CZ  . TYR   B 116 ? 0.1207 0.2548 0.3931 0.0110  0.0066  -0.0693 116 TYR   B CZ  
1663 O  OH  . TYR   B 116 ? 0.1867 0.4603 0.5044 -0.0299 -0.0301 -0.1564 116 TYR   B OH  
1664 N  N   . SER   B 117 ? 0.1953 0.1137 0.1740 0.0104  -0.0262 -0.0134 117 SER   B N   
1665 C  CA  A SER   B 117 ? 0.2494 0.0924 0.1884 0.0394  -0.0215 -0.0051 117 SER   B CA  
1666 C  CA  B SER   B 117 ? 0.2057 0.1028 0.1841 -0.0169 -0.0440 -0.0013 117 SER   B CA  
1667 C  C   . SER   B 117 ? 0.2643 0.0888 0.2118 0.0222  -0.0286 -0.0055 117 SER   B C   
1668 O  O   . SER   B 117 ? 0.2948 0.1025 0.2062 0.0061  -0.0067 -0.0206 117 SER   B O   
1669 C  CB  A SER   B 117 ? 0.2634 0.1730 0.2139 0.0739  -0.0262 -0.0170 117 SER   B CB  
1670 C  CB  B SER   B 117 ? 0.1894 0.1490 0.1390 0.0497  0.0138  -0.0295 117 SER   B CB  
1671 O  OG  A SER   B 117 ? 0.2028 0.2562 0.2955 -0.0180 -0.0519 -0.0074 117 SER   B OG  
1672 O  OG  B SER   B 117 ? 0.2803 0.1172 0.2259 -0.0047 0.0021  -0.0186 117 SER   B OG  
1673 N  N   . THR   B 118 ? 0.3404 0.0924 0.1849 -0.0079 0.0042  -0.0069 118 THR   B N   
1674 C  CA  . THR   B 118 ? 0.3107 0.0985 0.2138 0.0076  -0.0259 -0.0080 118 THR   B CA  
1675 C  C   . THR   B 118 ? 0.2633 0.1129 0.1970 -0.0138 0.0283  -0.0146 118 THR   B C   
1676 O  O   . THR   B 118 ? 0.4186 0.1209 0.2043 0.0398  -0.0019 -0.0019 118 THR   B O   
1677 C  CB  . THR   B 118 ? 0.3423 0.1211 0.2484 0.0614  -0.0310 -0.0069 118 THR   B CB  
1678 O  OG1 . THR   B 118 ? 0.2491 0.2166 0.3287 0.0253  0.0339  0.0004  118 THR   B OG1 
1679 C  CG2 . THR   B 118 ? 0.2902 0.1705 0.2219 -0.0128 -0.0115 -0.0136 118 THR   B CG2 
1680 N  N   . THR   B 119 ? 0.2130 0.1140 0.1792 -0.0090 0.0311  0.0047  119 THR   B N   
1681 C  CA  A THR   B 119 ? 0.1587 0.1208 0.2029 -0.0085 0.0204  0.0086  119 THR   B CA  
1682 C  CA  B THR   B 119 ? 0.1632 0.1215 0.2012 0.0028  0.0266  0.0031  119 THR   B CA  
1683 C  C   . THR   B 119 ? 0.1691 0.1103 0.1843 0.0207  0.0217  0.0032  119 THR   B C   
1684 O  O   . THR   B 119 ? 0.2645 0.1074 0.2417 -0.0148 0.0885  -0.0052 119 THR   B O   
1685 C  CB  A THR   B 119 ? 0.1630 0.1846 0.2801 0.0031  0.0690  -0.0308 119 THR   B CB  
1686 C  CB  B THR   B 119 ? 0.1814 0.2262 0.2451 -0.0344 0.0146  0.0425  119 THR   B CB  
1687 O  OG1 A THR   B 119 ? 0.2284 0.2303 0.3888 0.0800  0.0255  0.0778  119 THR   B OG1 
1688 O  OG1 B THR   B 119 ? 0.1799 0.2000 0.2418 -0.0286 0.0427  0.0224  119 THR   B OG1 
1689 C  CG2 A THR   B 119 ? 0.1816 0.2806 0.2766 -0.0873 0.0590  -0.0469 119 THR   B CG2 
1690 C  CG2 B THR   B 119 ? 0.1048 0.2459 0.4096 -0.0260 0.0662  0.0565  119 THR   B CG2 
1691 N  N   . ALA   B 120 ? 0.2025 0.1074 0.2163 0.0153  0.0352  0.0049  120 ALA   B N   
1692 C  CA  . ALA   B 120 ? 0.1721 0.1314 0.2062 0.0187  0.0205  0.0192  120 ALA   B CA  
1693 C  C   . ALA   B 120 ? 0.1896 0.1033 0.2588 0.0091  0.0134  0.0188  120 ALA   B C   
1694 O  O   . ALA   B 120 ? 0.2689 0.1403 0.2404 0.0692  0.0568  0.0249  120 ALA   B O   
1695 C  CB  . ALA   B 120 ? 0.1703 0.1856 0.2781 -0.0114 0.0000  0.0311  120 ALA   B CB  
1696 N  N   . VAL   B 121 ? 0.1485 0.1266 0.2322 0.0198  0.0279  0.0105  121 VAL   B N   
1697 C  CA  . VAL   B 121 ? 0.1418 0.2018 0.2502 0.0200  0.0335  0.0405  121 VAL   B CA  
1698 C  C   . VAL   B 121 ? 0.2259 0.1795 0.2237 0.0644  0.0406  0.0529  121 VAL   B C   
1699 O  O   . VAL   B 121 ? 0.2574 0.1759 0.2709 0.0507  0.0858  0.0567  121 VAL   B O   
1700 C  CB  . VAL   B 121 ? 0.2027 0.2295 0.2744 -0.0012 -0.0026 -0.0161 121 VAL   B CB  
1701 C  CG1 . VAL   B 121 ? 0.2290 0.3558 0.3344 0.0721  -0.0527 -0.0317 121 VAL   B CG1 
1702 C  CG2 . VAL   B 121 ? 0.2828 0.4218 0.3624 -0.1726 -0.0160 0.0036  121 VAL   B CG2 
1703 N  N   . VAL   B 122 ? 0.1659 0.1824 0.2623 0.0351  0.0591  0.0325  122 VAL   B N   
1704 C  CA  . VAL   B 122 ? 0.1815 0.1796 0.2844 0.0551  0.0765  0.0524  122 VAL   B CA  
1705 C  C   . VAL   B 122 ? 0.2608 0.1778 0.3380 0.0614  0.0867  0.0677  122 VAL   B C   
1706 O  O   . VAL   B 122 ? 0.2771 0.2116 0.3735 0.1004  0.0826  0.0856  122 VAL   B O   
1707 C  CB  . VAL   B 122 ? 0.2302 0.1867 0.3482 0.0228  0.0938  0.0111  122 VAL   B CB  
1708 C  CG1 . VAL   B 122 ? 0.2621 0.2726 0.4683 -0.0031 0.0834  0.1395  122 VAL   B CG1 
1709 C  CG2 . VAL   B 122 ? 0.2405 0.2642 0.3614 0.0305  0.0490  0.0661  122 VAL   B CG2 
1710 N  N   . THR   B 123 ? 0.3318 0.2793 0.4157 0.0705  0.1339  0.0861  123 THR   B N   
1711 C  CA  . THR   B 123 ? 0.4731 0.1889 0.4520 0.1147  0.0003  0.1435  123 THR   B CA  
1712 C  C   . THR   B 123 ? 0.3485 0.8746 0.4262 0.0426  0.1745  0.1276  123 THR   B C   
1713 O  O   . THR   B 123 ? 0.4554 0.3416 0.3977 0.0811  0.1621  0.1590  123 THR   B O   
1714 C  CB  . THR   B 123 ? 0.7384 0.6734 0.1866 0.0600  -0.0376 0.0942  123 THR   B CB  
1715 O  OG1 . THR   B 123 ? 0.6991 0.6827 0.4136 0.2099  -0.1342 -0.0471 123 THR   B OG1 
1716 C  CG2 . THR   B 123 ? 0.4902 0.7328 0.8410 -0.0085 -0.3211 0.2627  123 THR   B CG2 
1717 C  C1  . A1ISU C .   ? 0.4295 0.4866 0.4121 -0.0631 0.0010  0.0003  201 A1ISU B C1  
1718 C  C2  . A1ISU C .   ? 0.3165 0.3490 0.4731 -0.0982 0.0814  -0.0646 201 A1ISU B C2  
1719 C  C3  . A1ISU C .   ? 0.3929 0.2754 0.5104 0.0461  0.0621  0.0893  201 A1ISU B C3  
1720 C  C4  . A1ISU C .   ? 0.3840 0.1706 0.4147 -0.0162 -0.0007 0.0005  201 A1ISU B C4  
1721 C  C5  . A1ISU C .   ? 0.3935 0.2783 0.5063 0.0473  -0.0626 -0.0902 201 A1ISU B C5  
1722 CL CL1 . A1ISU C .   ? 0.4615 0.3484 0.4759 0.1432  0.0462  0.1023  201 A1ISU B CL1 
1723 N  N   . A1ISU C .   ? 0.3698 0.3488 0.4260 0.0215  0.0001  0.0002  201 A1ISU B N   
1724 CL CL  . A1ISU C .   ? 0.4638 0.3423 0.4780 0.1472  -0.0469 -0.1059 201 A1ISU B CL  
1725 C  C   . A1ISU C .   ? 0.3113 0.3405 0.4733 -0.0966 -0.0822 0.0696  201 A1ISU B C   
1726 O  O   . HOH   D .   ? 0.2673 0.2785 0.3915 0.0061  -0.0681 0.0277  201 HOH   A O   
1727 O  O   . HOH   D .   ? 0.1689 0.2198 0.2892 -0.0172 -0.0424 -0.0359 202 HOH   A O   
1728 O  O   . HOH   D .   ? 0.1588 0.3223 0.6950 0.0495  -0.0846 0.0139  203 HOH   A O   
1729 O  O   . HOH   D .   ? 0.2338 0.2138 0.3568 -0.0185 0.0756  0.0094  204 HOH   A O   
1730 O  O   . HOH   D .   ? 0.2762 0.4208 0.5369 -0.0104 -0.0284 -0.0561 205 HOH   A O   
1731 O  O   . HOH   D .   ? 0.2595 0.2054 0.3114 -0.0031 -0.0410 -0.0290 206 HOH   A O   
1732 O  O   . HOH   D .   ? 0.2785 0.2214 0.4308 -0.0499 -0.0926 0.0129  207 HOH   A O   
1733 O  O   . HOH   D .   ? 0.1615 0.1136 0.2397 0.0314  -0.0178 0.0048  208 HOH   A O   
1734 O  O   . HOH   D .   ? 0.1631 0.2301 0.2926 -0.0121 -0.0633 0.0279  209 HOH   A O   
1735 O  O   . HOH   D .   ? 0.5233 0.5887 0.2576 0.1668  0.0075  -0.0063 210 HOH   A O   
1736 O  O   . HOH   D .   ? 0.1640 0.2211 0.2251 -0.0185 0.0318  -0.0251 211 HOH   A O   
1737 O  O   . HOH   D .   ? 0.1365 0.1440 0.2647 0.0342  0.0002  -0.0018 212 HOH   A O   
1738 O  O   . HOH   D .   ? 0.3876 0.2854 0.5558 0.1253  0.0477  -0.0520 213 HOH   A O   
1739 O  O   . HOH   D .   ? 0.2520 0.1079 0.3492 0.0160  -0.0095 0.0367  214 HOH   A O   
1740 O  O   . HOH   D .   ? 0.4741 0.2461 0.5219 -0.0263 -0.0498 0.0328  215 HOH   A O   
1741 O  O   . HOH   D .   ? 0.3011 0.2014 0.3143 0.0214  0.1090  -0.0330 216 HOH   A O   
1742 O  O   . HOH   D .   ? 0.2134 0.1289 0.3804 -0.0006 -0.0093 0.0220  217 HOH   A O   
1743 O  O   . HOH   D .   ? 0.2747 0.2946 0.4777 -0.0183 -0.0804 0.0445  218 HOH   A O   
1744 O  O   . HOH   D .   ? 0.3254 0.6115 0.4413 0.0231  -0.0652 0.0617  219 HOH   A O   
1745 O  O   . HOH   D .   ? 0.2835 0.2922 0.4834 0.0042  -0.0585 0.0005  220 HOH   A O   
1746 O  O   . HOH   D .   ? 0.2292 0.3311 0.3316 0.0207  -0.0757 -0.0189 221 HOH   A O   
1747 O  O   . HOH   D .   ? 0.1950 0.1619 0.3418 0.0320  -0.0170 0.0136  222 HOH   A O   
1748 O  O   . HOH   D .   ? 0.2605 0.2097 0.4759 -0.0182 -0.0855 -0.0158 223 HOH   A O   
1749 O  O   . HOH   D .   ? 0.4884 0.3796 0.3884 -0.2198 0.1590  -0.0847 224 HOH   A O   
1750 O  O   . HOH   D .   ? 0.2366 0.1835 0.2802 0.0141  -0.0023 0.0225  225 HOH   A O   
1751 O  O   . HOH   D .   ? 0.2008 0.1445 0.2804 -0.0097 -0.0348 0.0041  226 HOH   A O   
1752 O  O   . HOH   D .   ? 0.4526 0.3993 0.4522 -0.0977 0.0381  0.0003  227 HOH   A O   
1753 O  O   . HOH   D .   ? 0.3074 0.1769 0.3011 0.0450  -0.0540 0.0089  228 HOH   A O   
1754 O  O   . HOH   D .   ? 0.2202 0.1990 0.2918 -0.0153 0.0047  -0.0178 229 HOH   A O   
1755 O  O   . HOH   D .   ? 0.2366 0.5870 0.5243 -0.0656 -0.0470 -0.1580 230 HOH   A O   
1756 O  O   . HOH   D .   ? 0.2214 0.2894 0.4837 -0.0136 -0.0770 0.0273  231 HOH   A O   
1757 O  O   . HOH   D .   ? 0.2589 0.2139 0.5108 -0.0007 0.0216  -0.0005 232 HOH   A O   
1758 O  O   . HOH   D .   ? 0.1439 0.1077 0.2391 0.0111  -0.0031 0.0121  233 HOH   A O   
1759 O  O   . HOH   D .   ? 0.2877 0.2235 0.4737 0.0016  0.0443  0.0096  234 HOH   A O   
1760 O  O   . HOH   D .   ? 0.5086 0.1796 0.2869 0.0145  0.0168  -0.0181 235 HOH   A O   
1761 O  O   . HOH   D .   ? 0.2285 0.2240 0.3790 -0.0588 0.0093  -0.0566 236 HOH   A O   
1762 O  O   . HOH   D .   ? 0.2509 0.3207 0.5078 -0.0845 0.0574  -0.0356 237 HOH   A O   
1763 O  O   . HOH   D .   ? 0.3020 0.2024 0.3827 0.0857  -0.1080 -0.0480 238 HOH   A O   
1764 O  O   . HOH   D .   ? 0.2590 0.2656 0.2558 -0.0135 -0.0390 0.0424  239 HOH   A O   
1765 O  O   . HOH   D .   ? 0.2821 0.4825 0.3226 0.0833  0.0217  0.0352  240 HOH   A O   
1766 O  O   . HOH   D .   ? 0.4022 0.2239 0.3860 0.0772  0.0427  0.0831  241 HOH   A O   
1767 O  O   . HOH   D .   ? 0.3172 0.1747 0.4385 0.0784  -0.0517 -0.0112 242 HOH   A O   
1768 O  O   . HOH   D .   ? 0.2248 0.2644 0.3627 0.0034  -0.0256 0.0072  243 HOH   A O   
1769 O  O   . HOH   D .   ? 0.3512 0.2398 0.5129 0.0021  -0.0860 -0.0354 244 HOH   A O   
1770 O  O   . HOH   D .   ? 0.3817 0.5968 0.4364 0.0423  0.0801  -0.0580 245 HOH   A O   
1771 O  O   . HOH   D .   ? 0.5328 0.3880 0.2690 0.0645  -0.0295 -0.0657 246 HOH   A O   
1772 O  O   . HOH   D .   ? 0.2660 0.1811 0.4830 0.0100  -0.0342 0.0252  247 HOH   A O   
1773 O  O   . HOH   D .   ? 0.3914 0.3838 0.7071 0.0317  -0.0814 -0.1193 248 HOH   A O   
1774 O  O   . HOH   D .   ? 0.3247 0.3143 0.6932 -0.0066 -0.1387 0.1413  249 HOH   A O   
1775 O  O   . HOH   D .   ? 0.6229 0.3120 0.4377 -0.2130 -0.2261 0.0664  250 HOH   A O   
1776 O  O   . HOH   D .   ? 0.3557 0.4520 0.4511 -0.1074 -0.0532 -0.1312 251 HOH   A O   
1777 O  O   . HOH   D .   ? 0.4083 0.2719 0.4752 -0.0008 -0.0194 0.0905  252 HOH   A O   
1778 O  O   . HOH   D .   ? 0.5606 0.2622 0.5422 0.0616  0.0520  -0.0886 253 HOH   A O   
1779 O  O   . HOH   D .   ? 0.4798 0.2825 0.5411 -0.1454 0.1308  0.0296  254 HOH   A O   
1780 O  O   . HOH   D .   ? 0.2953 0.3704 0.9391 0.0184  -0.1228 -0.1235 255 HOH   A O   
1781 O  O   . HOH   D .   ? 0.3236 0.1977 0.4985 -0.0367 -0.0857 0.0462  256 HOH   A O   
1782 O  O   . HOH   D .   ? 0.2792 0.1720 0.6030 -0.0595 -0.1024 0.0591  257 HOH   A O   
1783 O  O   . HOH   D .   ? 0.2841 0.2527 0.4157 -0.0161 0.0120  0.0126  258 HOH   A O   
1784 O  O   . HOH   D .   ? 0.3973 0.2819 0.4023 -0.1143 0.0048  -0.0151 259 HOH   A O   
1785 O  O   . HOH   E .   ? 0.3770 0.2813 0.4743 0.0475  0.1333  -0.0124 301 HOH   B O   
1786 O  O   . HOH   E .   ? 0.4562 0.2158 0.4205 0.0078  0.0174  -0.0140 302 HOH   B O   
1787 O  O   . HOH   E .   ? 0.2806 0.4350 0.4079 0.0048  -0.1734 0.0373  303 HOH   B O   
1788 O  O   . HOH   E .   ? 0.2059 0.1793 0.3042 0.0233  -0.0502 -0.0210 304 HOH   B O   
1789 O  O   . HOH   E .   ? 0.1546 0.1318 0.2194 -0.0245 -0.0162 0.0096  305 HOH   B O   
1790 O  O   . HOH   E .   ? 0.2758 0.3762 0.7645 -0.0561 -0.1508 0.0793  306 HOH   B O   
1791 O  O   . HOH   E .   ? 0.2635 0.2644 0.3752 -0.0238 -0.0016 -0.0205 307 HOH   B O   
1792 O  O   . HOH   E .   ? 0.4376 0.3706 0.5665 0.0026  -0.0859 0.0462  308 HOH   B O   
1793 O  O   . HOH   E .   ? 0.1931 0.2345 0.2410 0.0174  -0.0588 -0.0304 309 HOH   B O   
1794 O  O   . HOH   E .   ? 0.2413 0.3387 0.4698 -0.0311 -0.0077 0.1538  310 HOH   B O   
1795 O  O   . HOH   E .   ? 0.2607 0.3025 0.3732 0.0560  0.0781  0.0631  311 HOH   B O   
1796 O  O   . HOH   E .   ? 0.3290 0.3809 0.6196 0.0409  0.0473  -0.0254 312 HOH   B O   
1797 O  O   . HOH   E .   ? 0.2401 0.2474 0.3410 0.0261  0.0357  -0.0291 313 HOH   B O   
1798 O  O   . HOH   E .   ? 0.3374 0.1738 0.4898 0.0422  0.1276  -0.0318 314 HOH   B O   
1799 O  O   . HOH   E .   ? 0.4912 0.4132 0.3665 0.0529  -0.0554 0.0802  315 HOH   B O   
1800 O  O   . HOH   E .   ? 0.5464 0.2941 0.2976 -0.0424 -0.0073 -0.0035 316 HOH   B O   
1801 O  O   . HOH   E .   ? 0.2248 0.1301 0.5139 0.0232  0.0988  0.0245  317 HOH   B O   
1802 O  O   . HOH   E .   ? 0.2091 0.1237 0.3023 0.0103  0.0097  0.0203  318 HOH   B O   
1803 O  O   . HOH   E .   ? 0.1516 0.1983 0.2541 -0.0500 -0.0003 0.0114  319 HOH   B O   
1804 O  O   . HOH   E .   ? 0.2257 0.1604 0.2775 0.0000  0.0030  0.0009  320 HOH   B O   
1805 O  O   . HOH   E .   ? 0.3081 0.3034 0.3977 0.0464  0.1576  0.0037  321 HOH   B O   
1806 O  O   . HOH   E .   ? 0.1323 0.1239 0.2396 -0.0049 0.0145  -0.0042 322 HOH   B O   
1807 O  O   . HOH   E .   ? 0.4245 0.2895 0.5100 -0.1461 -0.0516 0.0231  323 HOH   B O   
1808 O  O   . HOH   E .   ? 0.4286 0.1820 0.3629 0.0333  0.0140  0.0358  324 HOH   B O   
1809 O  O   . HOH   E .   ? 0.2564 0.2362 0.3269 -0.0565 0.0024  -0.0242 325 HOH   B O   
1810 O  O   . HOH   E .   ? 0.4224 0.1931 0.3656 -0.0210 0.1581  0.0159  326 HOH   B O   
1811 O  O   . HOH   E .   ? 0.3650 0.4526 0.2998 -0.0550 0.0469  0.0329  327 HOH   B O   
1812 O  O   . HOH   E .   ? 0.3123 0.3274 0.4594 -0.1097 0.1378  -0.0376 328 HOH   B O   
1813 O  O   . HOH   E .   ? 0.4275 0.2678 0.3880 -0.0792 0.0072  -0.0303 329 HOH   B O   
1814 O  O   . HOH   E .   ? 0.6483 0.2909 0.2789 0.0569  0.0190  -0.0538 330 HOH   B O   
1815 O  O   . HOH   E .   ? 0.2942 0.4765 0.2717 0.0821  0.0462  -0.0446 331 HOH   B O   
1816 O  O   . HOH   E .   ? 0.2877 0.3751 0.5534 0.0823  -0.0442 -0.0561 332 HOH   B O   
1817 O  O   . HOH   E .   ? 0.3486 0.1967 0.6313 0.0510  0.1156  0.0279  333 HOH   B O   
1818 O  O   . HOH   E .   ? 0.2877 0.5095 0.4276 -0.0898 -0.0048 -0.0532 334 HOH   B O   
1819 O  O   . HOH   E .   ? 0.3784 0.4399 0.3786 0.0115  0.0302  -0.2008 335 HOH   B O   
1820 O  O   . HOH   E .   ? 0.6222 0.2898 0.4422 -0.0151 -0.0415 -0.0306 336 HOH   B O   
1821 O  O   . HOH   E .   ? 0.1907 0.2919 0.4394 0.0303  -0.0526 0.0402  337 HOH   B O   
1822 O  O   . HOH   E .   ? 0.5369 0.1698 0.4019 -0.0088 -0.0325 0.0478  338 HOH   B O   
1823 O  O   . HOH   E .   ? 0.3993 0.2794 0.5162 0.0515  -0.1307 -0.0167 339 HOH   B O   
1824 O  O   . HOH   E .   ? 1.4897 0.2661 0.9048 0.0849  0.5249  0.0663  340 HOH   B O   
1825 O  O   . HOH   E .   ? 0.3888 0.1548 0.3405 0.0168  0.0734  -0.0031 341 HOH   B O   
1826 O  O   . HOH   E .   ? 0.3326 0.2430 0.6880 -0.0659 -0.0501 0.0295  342 HOH   B O   
1827 O  O   . HOH   E .   ? 0.2173 0.1351 0.3910 0.0093  0.0007  0.0272  343 HOH   B O   
1828 O  O   . HOH   E .   ? 0.2844 0.2902 0.4013 -0.0177 0.0649  -0.0397 344 HOH   B O   
1829 O  O   . HOH   E .   ? 0.5983 0.3203 0.5524 -0.1314 0.0739  -0.1072 345 HOH   B O   
1830 O  O   . HOH   E .   ? 0.2352 0.3494 0.5326 0.0150  0.0617  -0.0963 346 HOH   B O   
# 
